data_9BVI
# 
_entry.id   9BVI 
# 
_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   9BVI         pdb_00009bvi 10.2210/pdb9bvi/pdb 
WWPDB D_1000283495 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-05 ? 
2 'Structure model' 1 1 2025-02-26 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BVI 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              stephen.fesik@Vanderbilt.Edu 
_pdbx_contact_author.name_first         Stephen 
_pdbx_contact_author.name_last          Fesik 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5957-6192 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Phan, J.'    1 ? 
'Fesik, S.W.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                2680 
_citation.page_last                 2693 
_citation.title                     'Discovery of Small Molecules that Bind to Son of Sevenless 2 (SOS2).' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02007 
_citation.pdbx_database_id_PubMed   39818983 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zak, K.M.'          1  ? 
primary 'Waterson, A.G.'     2  ? 
primary 'Geist, L.'          3  ? 
primary 'Braun, N.'          4  ? 
primary 'Hauer, K.'          5  ? 
primary 'Rumpel, K.'         6  ? 
primary 'Ramharter, J.'      7  ? 
primary 'Stadtmueller, H.'   8  ? 
primary 'Wolkerstorfer, B.'  9  ? 
primary 'Schoenbauer, D.'    10 ? 
primary 'Cui, J.'            11 ? 
primary 'Phan, J.'           12 ? 
primary 'Abbott, J.R.'       13 ? 
primary 'Sarkar, D.'         14 ? 
primary 'Hodges, T.R.'       15 ? 
primary 'Arnold, A.'         16 ? 
primary 'Sensintaffar, J.L.' 17 ? 
primary 'Fesik, S.W.'        18 ? 
primary 'Kessler, D.'        19 ? 
# 
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 'Son of sevenless homolog 2'                                 60492.211 1   ? ? ? ? 
2 non-polymer syn '4-{[4-(4-methylpiperazin-1-yl)quinazolin-2-yl]amino}phenol' 335.403   1   ? ? ? ? 
3 water       nat water                                                        18.015    461 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        SOS-2 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSYYHHHHHHLESTSLYKKAGFENLYFQEQPLRLPSPEVYRFVVKDSEENIVFEDNLQSRSGIPIIKGGTVVKLIERLTY
HMYADPNFVRTFLTTYRSFCKPQELLSLLIERFEIPEPEPTDADKLAIEKGEQPISADLKRFRKEYVQPVQLRILNVFRH
WVEHHFYDFERDLELLERLESFISSVRGKAMKKWVESIAKIIRRKKQAQANGVSHNITFESPPPPIEWHISKPGQFETFD
LMTLHPIEIARQLTLLESDLYRKVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVEAENFEERVAVLSRI
IEILQVFQDLNNFNGVLEIVSAVNSVSVYRLDHTFEALQERKRKILDEAVELSQDHFKKYLVKLKSINPPCVPFFGIYLT
NILKTEEGNNDFLKKKGKDLINFSKRRKVAEITGEIQQYQNQPYCLRIEPDMRRFFENLNPMGSASEKEFTDYLFNKSLE
IEPRNCKQPPRFPRKSTFSLKSPGIRPNTGRHGS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSYYHHHHHHLESTSLYKKAGFENLYFQEQPLRLPSPEVYRFVVKDSEENIVFEDNLQSRSGIPIIKGGTVVKLIERLTY
HMYADPNFVRTFLTTYRSFCKPQELLSLLIERFEIPEPEPTDADKLAIEKGEQPISADLKRFRKEYVQPVQLRILNVFRH
WVEHHFYDFERDLELLERLESFISSVRGKAMKKWVESIAKIIRRKKQAQANGVSHNITFESPPPPIEWHISKPGQFETFD
LMTLHPIEIARQLTLLESDLYRKVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVEAENFEERVAVLSRI
IEILQVFQDLNNFNGVLEIVSAVNSVSVYRLDHTFEALQERKRKILDEAVELSQDHFKKYLVKLKSINPPCVPFFGIYLT
NILKTEEGNNDFLKKKGKDLINFSKRRKVAEITGEIQQYQNQPYCLRIEPDMRRFFENLNPMGSASEKEFTDYLFNKSLE
IEPRNCKQPPRFPRKSTFSLKSPGIRPNTGRHGS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-{[4-(4-methylpiperazin-1-yl)quinazolin-2-yl]amino}phenol' A1ASW 
3 water                                                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   TYR n 
1 4   TYR n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  LEU n 
1 12  GLU n 
1 13  SER n 
1 14  THR n 
1 15  SER n 
1 16  LEU n 
1 17  TYR n 
1 18  LYS n 
1 19  LYS n 
1 20  ALA n 
1 21  GLY n 
1 22  PHE n 
1 23  GLU n 
1 24  ASN n 
1 25  LEU n 
1 26  TYR n 
1 27  PHE n 
1 28  GLN n 
1 29  GLU n 
1 30  GLN n 
1 31  PRO n 
1 32  LEU n 
1 33  ARG n 
1 34  LEU n 
1 35  PRO n 
1 36  SER n 
1 37  PRO n 
1 38  GLU n 
1 39  VAL n 
1 40  TYR n 
1 41  ARG n 
1 42  PHE n 
1 43  VAL n 
1 44  VAL n 
1 45  LYS n 
1 46  ASP n 
1 47  SER n 
1 48  GLU n 
1 49  GLU n 
1 50  ASN n 
1 51  ILE n 
1 52  VAL n 
1 53  PHE n 
1 54  GLU n 
1 55  ASP n 
1 56  ASN n 
1 57  LEU n 
1 58  GLN n 
1 59  SER n 
1 60  ARG n 
1 61  SER n 
1 62  GLY n 
1 63  ILE n 
1 64  PRO n 
1 65  ILE n 
1 66  ILE n 
1 67  LYS n 
1 68  GLY n 
1 69  GLY n 
1 70  THR n 
1 71  VAL n 
1 72  VAL n 
1 73  LYS n 
1 74  LEU n 
1 75  ILE n 
1 76  GLU n 
1 77  ARG n 
1 78  LEU n 
1 79  THR n 
1 80  TYR n 
1 81  HIS n 
1 82  MET n 
1 83  TYR n 
1 84  ALA n 
1 85  ASP n 
1 86  PRO n 
1 87  ASN n 
1 88  PHE n 
1 89  VAL n 
1 90  ARG n 
1 91  THR n 
1 92  PHE n 
1 93  LEU n 
1 94  THR n 
1 95  THR n 
1 96  TYR n 
1 97  ARG n 
1 98  SER n 
1 99  PHE n 
1 100 CYS n 
1 101 LYS n 
1 102 PRO n 
1 103 GLN n 
1 104 GLU n 
1 105 LEU n 
1 106 LEU n 
1 107 SER n 
1 108 LEU n 
1 109 LEU n 
1 110 ILE n 
1 111 GLU n 
1 112 ARG n 
1 113 PHE n 
1 114 GLU n 
1 115 ILE n 
1 116 PRO n 
1 117 GLU n 
1 118 PRO n 
1 119 GLU n 
1 120 PRO n 
1 121 THR n 
1 122 ASP n 
1 123 ALA n 
1 124 ASP n 
1 125 LYS n 
1 126 LEU n 
1 127 ALA n 
1 128 ILE n 
1 129 GLU n 
1 130 LYS n 
1 131 GLY n 
1 132 GLU n 
1 133 GLN n 
1 134 PRO n 
1 135 ILE n 
1 136 SER n 
1 137 ALA n 
1 138 ASP n 
1 139 LEU n 
1 140 LYS n 
1 141 ARG n 
1 142 PHE n 
1 143 ARG n 
1 144 LYS n 
1 145 GLU n 
1 146 TYR n 
1 147 VAL n 
1 148 GLN n 
1 149 PRO n 
1 150 VAL n 
1 151 GLN n 
1 152 LEU n 
1 153 ARG n 
1 154 ILE n 
1 155 LEU n 
1 156 ASN n 
1 157 VAL n 
1 158 PHE n 
1 159 ARG n 
1 160 HIS n 
1 161 TRP n 
1 162 VAL n 
1 163 GLU n 
1 164 HIS n 
1 165 HIS n 
1 166 PHE n 
1 167 TYR n 
1 168 ASP n 
1 169 PHE n 
1 170 GLU n 
1 171 ARG n 
1 172 ASP n 
1 173 LEU n 
1 174 GLU n 
1 175 LEU n 
1 176 LEU n 
1 177 GLU n 
1 178 ARG n 
1 179 LEU n 
1 180 GLU n 
1 181 SER n 
1 182 PHE n 
1 183 ILE n 
1 184 SER n 
1 185 SER n 
1 186 VAL n 
1 187 ARG n 
1 188 GLY n 
1 189 LYS n 
1 190 ALA n 
1 191 MET n 
1 192 LYS n 
1 193 LYS n 
1 194 TRP n 
1 195 VAL n 
1 196 GLU n 
1 197 SER n 
1 198 ILE n 
1 199 ALA n 
1 200 LYS n 
1 201 ILE n 
1 202 ILE n 
1 203 ARG n 
1 204 ARG n 
1 205 LYS n 
1 206 LYS n 
1 207 GLN n 
1 208 ALA n 
1 209 GLN n 
1 210 ALA n 
1 211 ASN n 
1 212 GLY n 
1 213 VAL n 
1 214 SER n 
1 215 HIS n 
1 216 ASN n 
1 217 ILE n 
1 218 THR n 
1 219 PHE n 
1 220 GLU n 
1 221 SER n 
1 222 PRO n 
1 223 PRO n 
1 224 PRO n 
1 225 PRO n 
1 226 ILE n 
1 227 GLU n 
1 228 TRP n 
1 229 HIS n 
1 230 ILE n 
1 231 SER n 
1 232 LYS n 
1 233 PRO n 
1 234 GLY n 
1 235 GLN n 
1 236 PHE n 
1 237 GLU n 
1 238 THR n 
1 239 PHE n 
1 240 ASP n 
1 241 LEU n 
1 242 MET n 
1 243 THR n 
1 244 LEU n 
1 245 HIS n 
1 246 PRO n 
1 247 ILE n 
1 248 GLU n 
1 249 ILE n 
1 250 ALA n 
1 251 ARG n 
1 252 GLN n 
1 253 LEU n 
1 254 THR n 
1 255 LEU n 
1 256 LEU n 
1 257 GLU n 
1 258 SER n 
1 259 ASP n 
1 260 LEU n 
1 261 TYR n 
1 262 ARG n 
1 263 LYS n 
1 264 VAL n 
1 265 GLN n 
1 266 PRO n 
1 267 SER n 
1 268 GLU n 
1 269 LEU n 
1 270 VAL n 
1 271 GLY n 
1 272 SER n 
1 273 VAL n 
1 274 TRP n 
1 275 THR n 
1 276 LYS n 
1 277 GLU n 
1 278 ASP n 
1 279 LYS n 
1 280 GLU n 
1 281 ILE n 
1 282 ASN n 
1 283 SER n 
1 284 PRO n 
1 285 ASN n 
1 286 LEU n 
1 287 LEU n 
1 288 LYS n 
1 289 MET n 
1 290 ILE n 
1 291 ARG n 
1 292 HIS n 
1 293 THR n 
1 294 THR n 
1 295 ASN n 
1 296 LEU n 
1 297 THR n 
1 298 LEU n 
1 299 TRP n 
1 300 PHE n 
1 301 GLU n 
1 302 LYS n 
1 303 CYS n 
1 304 ILE n 
1 305 VAL n 
1 306 GLU n 
1 307 ALA n 
1 308 GLU n 
1 309 ASN n 
1 310 PHE n 
1 311 GLU n 
1 312 GLU n 
1 313 ARG n 
1 314 VAL n 
1 315 ALA n 
1 316 VAL n 
1 317 LEU n 
1 318 SER n 
1 319 ARG n 
1 320 ILE n 
1 321 ILE n 
1 322 GLU n 
1 323 ILE n 
1 324 LEU n 
1 325 GLN n 
1 326 VAL n 
1 327 PHE n 
1 328 GLN n 
1 329 ASP n 
1 330 LEU n 
1 331 ASN n 
1 332 ASN n 
1 333 PHE n 
1 334 ASN n 
1 335 GLY n 
1 336 VAL n 
1 337 LEU n 
1 338 GLU n 
1 339 ILE n 
1 340 VAL n 
1 341 SER n 
1 342 ALA n 
1 343 VAL n 
1 344 ASN n 
1 345 SER n 
1 346 VAL n 
1 347 SER n 
1 348 VAL n 
1 349 TYR n 
1 350 ARG n 
1 351 LEU n 
1 352 ASP n 
1 353 HIS n 
1 354 THR n 
1 355 PHE n 
1 356 GLU n 
1 357 ALA n 
1 358 LEU n 
1 359 GLN n 
1 360 GLU n 
1 361 ARG n 
1 362 LYS n 
1 363 ARG n 
1 364 LYS n 
1 365 ILE n 
1 366 LEU n 
1 367 ASP n 
1 368 GLU n 
1 369 ALA n 
1 370 VAL n 
1 371 GLU n 
1 372 LEU n 
1 373 SER n 
1 374 GLN n 
1 375 ASP n 
1 376 HIS n 
1 377 PHE n 
1 378 LYS n 
1 379 LYS n 
1 380 TYR n 
1 381 LEU n 
1 382 VAL n 
1 383 LYS n 
1 384 LEU n 
1 385 LYS n 
1 386 SER n 
1 387 ILE n 
1 388 ASN n 
1 389 PRO n 
1 390 PRO n 
1 391 CYS n 
1 392 VAL n 
1 393 PRO n 
1 394 PHE n 
1 395 PHE n 
1 396 GLY n 
1 397 ILE n 
1 398 TYR n 
1 399 LEU n 
1 400 THR n 
1 401 ASN n 
1 402 ILE n 
1 403 LEU n 
1 404 LYS n 
1 405 THR n 
1 406 GLU n 
1 407 GLU n 
1 408 GLY n 
1 409 ASN n 
1 410 ASN n 
1 411 ASP n 
1 412 PHE n 
1 413 LEU n 
1 414 LYS n 
1 415 LYS n 
1 416 LYS n 
1 417 GLY n 
1 418 LYS n 
1 419 ASP n 
1 420 LEU n 
1 421 ILE n 
1 422 ASN n 
1 423 PHE n 
1 424 SER n 
1 425 LYS n 
1 426 ARG n 
1 427 ARG n 
1 428 LYS n 
1 429 VAL n 
1 430 ALA n 
1 431 GLU n 
1 432 ILE n 
1 433 THR n 
1 434 GLY n 
1 435 GLU n 
1 436 ILE n 
1 437 GLN n 
1 438 GLN n 
1 439 TYR n 
1 440 GLN n 
1 441 ASN n 
1 442 GLN n 
1 443 PRO n 
1 444 TYR n 
1 445 CYS n 
1 446 LEU n 
1 447 ARG n 
1 448 ILE n 
1 449 GLU n 
1 450 PRO n 
1 451 ASP n 
1 452 MET n 
1 453 ARG n 
1 454 ARG n 
1 455 PHE n 
1 456 PHE n 
1 457 GLU n 
1 458 ASN n 
1 459 LEU n 
1 460 ASN n 
1 461 PRO n 
1 462 MET n 
1 463 GLY n 
1 464 SER n 
1 465 ALA n 
1 466 SER n 
1 467 GLU n 
1 468 LYS n 
1 469 GLU n 
1 470 PHE n 
1 471 THR n 
1 472 ASP n 
1 473 TYR n 
1 474 LEU n 
1 475 PHE n 
1 476 ASN n 
1 477 LYS n 
1 478 SER n 
1 479 LEU n 
1 480 GLU n 
1 481 ILE n 
1 482 GLU n 
1 483 PRO n 
1 484 ARG n 
1 485 ASN n 
1 486 CYS n 
1 487 LYS n 
1 488 GLN n 
1 489 PRO n 
1 490 PRO n 
1 491 ARG n 
1 492 PHE n 
1 493 PRO n 
1 494 ARG n 
1 495 LYS n 
1 496 SER n 
1 497 THR n 
1 498 PHE n 
1 499 SER n 
1 500 LEU n 
1 501 LYS n 
1 502 SER n 
1 503 PRO n 
1 504 GLY n 
1 505 ILE n 
1 506 ARG n 
1 507 PRO n 
1 508 ASN n 
1 509 THR n 
1 510 GLY n 
1 511 ARG n 
1 512 HIS n 
1 513 GLY n 
1 514 SER 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                   514 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOS2 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ASW non-polymer         . '4-{[4-(4-methylpiperazin-1-yl)quinazolin-2-yl]amino}phenol' ? 'C19 H21 N5 O'   335.403 
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   -28  ?    ?   ?   A . n 
A 1 2   SER 2   -27  ?    ?   ?   A . n 
A 1 3   TYR 3   -26  ?    ?   ?   A . n 
A 1 4   TYR 4   -25  ?    ?   ?   A . n 
A 1 5   HIS 5   -24  ?    ?   ?   A . n 
A 1 6   HIS 6   -23  ?    ?   ?   A . n 
A 1 7   HIS 7   -22  ?    ?   ?   A . n 
A 1 8   HIS 8   -21  ?    ?   ?   A . n 
A 1 9   HIS 9   -20  ?    ?   ?   A . n 
A 1 10  HIS 10  -19  ?    ?   ?   A . n 
A 1 11  LEU 11  -18  ?    ?   ?   A . n 
A 1 12  GLU 12  -17  ?    ?   ?   A . n 
A 1 13  SER 13  -16  ?    ?   ?   A . n 
A 1 14  THR 14  -15  ?    ?   ?   A . n 
A 1 15  SER 15  -14  ?    ?   ?   A . n 
A 1 16  LEU 16  -13  ?    ?   ?   A . n 
A 1 17  TYR 17  -12  ?    ?   ?   A . n 
A 1 18  LYS 18  -11  ?    ?   ?   A . n 
A 1 19  LYS 19  -10  ?    ?   ?   A . n 
A 1 20  ALA 20  -9   ?    ?   ?   A . n 
A 1 21  GLY 21  -8   ?    ?   ?   A . n 
A 1 22  PHE 22  -7   ?    ?   ?   A . n 
A 1 23  GLU 23  -6   ?    ?   ?   A . n 
A 1 24  ASN 24  -5   ?    ?   ?   A . n 
A 1 25  LEU 25  -4   -4   LEU LEU A . n 
A 1 26  TYR 26  -3   -3   TYR TYR A . n 
A 1 27  PHE 27  -2   -2   PHE PHE A . n 
A 1 28  GLN 28  -1   -1   GLN GLN A . n 
A 1 29  GLU 29  566  566  GLU GLU A . n 
A 1 30  GLN 30  567  567  GLN GLN A . n 
A 1 31  PRO 31  568  568  PRO PRO A . n 
A 1 32  LEU 32  569  569  LEU LEU A . n 
A 1 33  ARG 33  570  570  ARG ARG A . n 
A 1 34  LEU 34  571  571  LEU LEU A . n 
A 1 35  PRO 35  572  572  PRO PRO A . n 
A 1 36  SER 36  573  573  SER SER A . n 
A 1 37  PRO 37  574  574  PRO PRO A . n 
A 1 38  GLU 38  575  575  GLU GLU A . n 
A 1 39  VAL 39  576  576  VAL VAL A . n 
A 1 40  TYR 40  577  577  TYR TYR A . n 
A 1 41  ARG 41  578  578  ARG ARG A . n 
A 1 42  PHE 42  579  579  PHE PHE A . n 
A 1 43  VAL 43  580  580  VAL VAL A . n 
A 1 44  VAL 44  581  581  VAL VAL A . n 
A 1 45  LYS 45  582  582  LYS LYS A . n 
A 1 46  ASP 46  583  583  ASP ASP A . n 
A 1 47  SER 47  584  584  SER SER A . n 
A 1 48  GLU 48  585  585  GLU GLU A . n 
A 1 49  GLU 49  586  586  GLU GLU A . n 
A 1 50  ASN 50  587  587  ASN ASN A . n 
A 1 51  ILE 51  588  588  ILE ILE A . n 
A 1 52  VAL 52  589  589  VAL VAL A . n 
A 1 53  PHE 53  590  590  PHE PHE A . n 
A 1 54  GLU 54  591  591  GLU GLU A . n 
A 1 55  ASP 55  592  592  ASP ASP A . n 
A 1 56  ASN 56  593  ?    ?   ?   A . n 
A 1 57  LEU 57  594  ?    ?   ?   A . n 
A 1 58  GLN 58  595  ?    ?   ?   A . n 
A 1 59  SER 59  596  ?    ?   ?   A . n 
A 1 60  ARG 60  597  ?    ?   ?   A . n 
A 1 61  SER 61  598  ?    ?   ?   A . n 
A 1 62  GLY 62  599  599  GLY GLY A . n 
A 1 63  ILE 63  600  600  ILE ILE A . n 
A 1 64  PRO 64  601  601  PRO PRO A . n 
A 1 65  ILE 65  602  602  ILE ILE A . n 
A 1 66  ILE 66  603  603  ILE ILE A . n 
A 1 67  LYS 67  604  604  LYS LYS A . n 
A 1 68  GLY 68  605  605  GLY GLY A . n 
A 1 69  GLY 69  606  606  GLY GLY A . n 
A 1 70  THR 70  607  607  THR THR A . n 
A 1 71  VAL 71  608  608  VAL VAL A . n 
A 1 72  VAL 72  609  609  VAL VAL A . n 
A 1 73  LYS 73  610  610  LYS LYS A . n 
A 1 74  LEU 74  611  611  LEU LEU A . n 
A 1 75  ILE 75  612  612  ILE ILE A . n 
A 1 76  GLU 76  613  613  GLU GLU A . n 
A 1 77  ARG 77  614  614  ARG ARG A . n 
A 1 78  LEU 78  615  615  LEU LEU A . n 
A 1 79  THR 79  616  616  THR THR A . n 
A 1 80  TYR 80  617  617  TYR TYR A . n 
A 1 81  HIS 81  618  618  HIS HIS A . n 
A 1 82  MET 82  619  619  MET MET A . n 
A 1 83  TYR 83  620  620  TYR TYR A . n 
A 1 84  ALA 84  621  621  ALA ALA A . n 
A 1 85  ASP 85  622  622  ASP ASP A . n 
A 1 86  PRO 86  623  623  PRO PRO A . n 
A 1 87  ASN 87  624  624  ASN ASN A . n 
A 1 88  PHE 88  625  625  PHE PHE A . n 
A 1 89  VAL 89  626  626  VAL VAL A . n 
A 1 90  ARG 90  627  627  ARG ARG A . n 
A 1 91  THR 91  628  628  THR THR A . n 
A 1 92  PHE 92  629  629  PHE PHE A . n 
A 1 93  LEU 93  630  630  LEU LEU A . n 
A 1 94  THR 94  631  631  THR THR A . n 
A 1 95  THR 95  632  632  THR THR A . n 
A 1 96  TYR 96  633  633  TYR TYR A . n 
A 1 97  ARG 97  634  634  ARG ARG A . n 
A 1 98  SER 98  635  635  SER SER A . n 
A 1 99  PHE 99  636  636  PHE PHE A . n 
A 1 100 CYS 100 637  637  CYS CYS A . n 
A 1 101 LYS 101 638  638  LYS LYS A . n 
A 1 102 PRO 102 639  639  PRO PRO A . n 
A 1 103 GLN 103 640  640  GLN GLN A . n 
A 1 104 GLU 104 641  641  GLU GLU A . n 
A 1 105 LEU 105 642  642  LEU LEU A . n 
A 1 106 LEU 106 643  643  LEU LEU A . n 
A 1 107 SER 107 644  644  SER SER A . n 
A 1 108 LEU 108 645  645  LEU LEU A . n 
A 1 109 LEU 109 646  646  LEU LEU A . n 
A 1 110 ILE 110 647  647  ILE ILE A . n 
A 1 111 GLU 111 648  648  GLU GLU A . n 
A 1 112 ARG 112 649  649  ARG ARG A . n 
A 1 113 PHE 113 650  650  PHE PHE A . n 
A 1 114 GLU 114 651  651  GLU GLU A . n 
A 1 115 ILE 115 652  652  ILE ILE A . n 
A 1 116 PRO 116 653  653  PRO PRO A . n 
A 1 117 GLU 117 654  654  GLU GLU A . n 
A 1 118 PRO 118 655  655  PRO PRO A . n 
A 1 119 GLU 119 656  656  GLU GLU A . n 
A 1 120 PRO 120 657  657  PRO PRO A . n 
A 1 121 THR 121 658  658  THR THR A . n 
A 1 122 ASP 122 659  659  ASP ASP A . n 
A 1 123 ALA 123 660  660  ALA ALA A . n 
A 1 124 ASP 124 661  661  ASP ASP A . n 
A 1 125 LYS 125 662  662  LYS LYS A . n 
A 1 126 LEU 126 663  663  LEU LEU A . n 
A 1 127 ALA 127 664  664  ALA ALA A . n 
A 1 128 ILE 128 665  665  ILE ILE A . n 
A 1 129 GLU 129 666  666  GLU GLU A . n 
A 1 130 LYS 130 667  667  LYS LYS A . n 
A 1 131 GLY 131 668  668  GLY GLY A . n 
A 1 132 GLU 132 669  669  GLU GLU A . n 
A 1 133 GLN 133 670  670  GLN GLN A . n 
A 1 134 PRO 134 671  671  PRO PRO A . n 
A 1 135 ILE 135 672  672  ILE ILE A . n 
A 1 136 SER 136 673  673  SER SER A . n 
A 1 137 ALA 137 674  674  ALA ALA A . n 
A 1 138 ASP 138 675  675  ASP ASP A . n 
A 1 139 LEU 139 676  676  LEU LEU A . n 
A 1 140 LYS 140 677  677  LYS LYS A . n 
A 1 141 ARG 141 678  678  ARG ARG A . n 
A 1 142 PHE 142 679  679  PHE PHE A . n 
A 1 143 ARG 143 680  680  ARG ARG A . n 
A 1 144 LYS 144 681  681  LYS LYS A . n 
A 1 145 GLU 145 682  682  GLU GLU A . n 
A 1 146 TYR 146 683  683  TYR TYR A . n 
A 1 147 VAL 147 684  684  VAL VAL A . n 
A 1 148 GLN 148 685  685  GLN GLN A . n 
A 1 149 PRO 149 686  686  PRO PRO A . n 
A 1 150 VAL 150 687  687  VAL VAL A . n 
A 1 151 GLN 151 688  688  GLN GLN A . n 
A 1 152 LEU 152 689  689  LEU LEU A . n 
A 1 153 ARG 153 690  690  ARG ARG A . n 
A 1 154 ILE 154 691  691  ILE ILE A . n 
A 1 155 LEU 155 692  692  LEU LEU A . n 
A 1 156 ASN 156 693  693  ASN ASN A . n 
A 1 157 VAL 157 694  694  VAL VAL A . n 
A 1 158 PHE 158 695  695  PHE PHE A . n 
A 1 159 ARG 159 696  696  ARG ARG A . n 
A 1 160 HIS 160 697  697  HIS HIS A . n 
A 1 161 TRP 161 698  698  TRP TRP A . n 
A 1 162 VAL 162 699  699  VAL VAL A . n 
A 1 163 GLU 163 700  700  GLU GLU A . n 
A 1 164 HIS 164 701  701  HIS HIS A . n 
A 1 165 HIS 165 702  702  HIS HIS A . n 
A 1 166 PHE 166 703  703  PHE PHE A . n 
A 1 167 TYR 167 704  704  TYR TYR A . n 
A 1 168 ASP 168 705  705  ASP ASP A . n 
A 1 169 PHE 169 706  706  PHE PHE A . n 
A 1 170 GLU 170 707  707  GLU GLU A . n 
A 1 171 ARG 171 708  708  ARG ARG A . n 
A 1 172 ASP 172 709  709  ASP ASP A . n 
A 1 173 LEU 173 710  710  LEU LEU A . n 
A 1 174 GLU 174 711  711  GLU GLU A . n 
A 1 175 LEU 175 712  712  LEU LEU A . n 
A 1 176 LEU 176 713  713  LEU LEU A . n 
A 1 177 GLU 177 714  714  GLU GLU A . n 
A 1 178 ARG 178 715  715  ARG ARG A . n 
A 1 179 LEU 179 716  716  LEU LEU A . n 
A 1 180 GLU 180 717  717  GLU GLU A . n 
A 1 181 SER 181 718  718  SER SER A . n 
A 1 182 PHE 182 719  719  PHE PHE A . n 
A 1 183 ILE 183 720  720  ILE ILE A . n 
A 1 184 SER 184 721  721  SER SER A . n 
A 1 185 SER 185 722  722  SER SER A . n 
A 1 186 VAL 186 723  723  VAL VAL A . n 
A 1 187 ARG 187 724  724  ARG ARG A . n 
A 1 188 GLY 188 725  725  GLY GLY A . n 
A 1 189 LYS 189 726  726  LYS LYS A . n 
A 1 190 ALA 190 727  727  ALA ALA A . n 
A 1 191 MET 191 728  728  MET MET A . n 
A 1 192 LYS 192 729  729  LYS LYS A . n 
A 1 193 LYS 193 730  730  LYS LYS A . n 
A 1 194 TRP 194 731  731  TRP TRP A . n 
A 1 195 VAL 195 732  732  VAL VAL A . n 
A 1 196 GLU 196 733  733  GLU GLU A . n 
A 1 197 SER 197 734  734  SER SER A . n 
A 1 198 ILE 198 735  735  ILE ILE A . n 
A 1 199 ALA 199 736  736  ALA ALA A . n 
A 1 200 LYS 200 737  737  LYS LYS A . n 
A 1 201 ILE 201 738  738  ILE ILE A . n 
A 1 202 ILE 202 739  739  ILE ILE A . n 
A 1 203 ARG 203 740  740  ARG ARG A . n 
A 1 204 ARG 204 741  741  ARG ARG A . n 
A 1 205 LYS 205 742  742  LYS LYS A . n 
A 1 206 LYS 206 743  743  LYS LYS A . n 
A 1 207 GLN 207 744  744  GLN GLN A . n 
A 1 208 ALA 208 745  745  ALA ALA A . n 
A 1 209 GLN 209 746  ?    ?   ?   A . n 
A 1 210 ALA 210 747  ?    ?   ?   A . n 
A 1 211 ASN 211 748  ?    ?   ?   A . n 
A 1 212 GLY 212 749  ?    ?   ?   A . n 
A 1 213 VAL 213 750  ?    ?   ?   A . n 
A 1 214 SER 214 751  ?    ?   ?   A . n 
A 1 215 HIS 215 752  ?    ?   ?   A . n 
A 1 216 ASN 216 753  ?    ?   ?   A . n 
A 1 217 ILE 217 754  754  ILE ILE A . n 
A 1 218 THR 218 755  755  THR THR A . n 
A 1 219 PHE 219 756  756  PHE PHE A . n 
A 1 220 GLU 220 757  757  GLU GLU A . n 
A 1 221 SER 221 758  758  SER SER A . n 
A 1 222 PRO 222 759  759  PRO PRO A . n 
A 1 223 PRO 223 760  760  PRO PRO A . n 
A 1 224 PRO 224 761  761  PRO PRO A . n 
A 1 225 PRO 225 762  762  PRO PRO A . n 
A 1 226 ILE 226 763  763  ILE ILE A . n 
A 1 227 GLU 227 764  764  GLU GLU A . n 
A 1 228 TRP 228 765  765  TRP TRP A . n 
A 1 229 HIS 229 766  766  HIS HIS A . n 
A 1 230 ILE 230 767  767  ILE ILE A . n 
A 1 231 SER 231 768  768  SER SER A . n 
A 1 232 LYS 232 769  769  LYS LYS A . n 
A 1 233 PRO 233 770  770  PRO PRO A . n 
A 1 234 GLY 234 771  771  GLY GLY A . n 
A 1 235 GLN 235 772  772  GLN GLN A . n 
A 1 236 PHE 236 773  773  PHE PHE A . n 
A 1 237 GLU 237 774  774  GLU GLU A . n 
A 1 238 THR 238 775  775  THR THR A . n 
A 1 239 PHE 239 776  776  PHE PHE A . n 
A 1 240 ASP 240 777  777  ASP ASP A . n 
A 1 241 LEU 241 778  778  LEU LEU A . n 
A 1 242 MET 242 779  779  MET MET A . n 
A 1 243 THR 243 780  780  THR THR A . n 
A 1 244 LEU 244 781  781  LEU LEU A . n 
A 1 245 HIS 245 782  782  HIS HIS A . n 
A 1 246 PRO 246 783  783  PRO PRO A . n 
A 1 247 ILE 247 784  784  ILE ILE A . n 
A 1 248 GLU 248 785  785  GLU GLU A . n 
A 1 249 ILE 249 786  786  ILE ILE A . n 
A 1 250 ALA 250 787  787  ALA ALA A . n 
A 1 251 ARG 251 788  788  ARG ARG A . n 
A 1 252 GLN 252 789  789  GLN GLN A . n 
A 1 253 LEU 253 790  790  LEU LEU A . n 
A 1 254 THR 254 791  791  THR THR A . n 
A 1 255 LEU 255 792  792  LEU LEU A . n 
A 1 256 LEU 256 793  793  LEU LEU A . n 
A 1 257 GLU 257 794  794  GLU GLU A . n 
A 1 258 SER 258 795  795  SER SER A . n 
A 1 259 ASP 259 796  796  ASP ASP A . n 
A 1 260 LEU 260 797  797  LEU LEU A . n 
A 1 261 TYR 261 798  798  TYR TYR A . n 
A 1 262 ARG 262 799  799  ARG ARG A . n 
A 1 263 LYS 263 800  800  LYS LYS A . n 
A 1 264 VAL 264 801  801  VAL VAL A . n 
A 1 265 GLN 265 802  802  GLN GLN A . n 
A 1 266 PRO 266 803  803  PRO PRO A . n 
A 1 267 SER 267 804  804  SER SER A . n 
A 1 268 GLU 268 805  805  GLU GLU A . n 
A 1 269 LEU 269 806  806  LEU LEU A . n 
A 1 270 VAL 270 807  807  VAL VAL A . n 
A 1 271 GLY 271 808  808  GLY GLY A . n 
A 1 272 SER 272 809  809  SER SER A . n 
A 1 273 VAL 273 810  810  VAL VAL A . n 
A 1 274 TRP 274 811  811  TRP TRP A . n 
A 1 275 THR 275 812  812  THR THR A . n 
A 1 276 LYS 276 813  813  LYS LYS A . n 
A 1 277 GLU 277 814  814  GLU GLU A . n 
A 1 278 ASP 278 815  815  ASP ASP A . n 
A 1 279 LYS 279 816  816  LYS LYS A . n 
A 1 280 GLU 280 817  817  GLU GLU A . n 
A 1 281 ILE 281 818  818  ILE ILE A . n 
A 1 282 ASN 282 819  819  ASN ASN A . n 
A 1 283 SER 283 820  820  SER SER A . n 
A 1 284 PRO 284 821  821  PRO PRO A . n 
A 1 285 ASN 285 822  822  ASN ASN A . n 
A 1 286 LEU 286 823  823  LEU LEU A . n 
A 1 287 LEU 287 824  824  LEU LEU A . n 
A 1 288 LYS 288 825  825  LYS LYS A . n 
A 1 289 MET 289 826  826  MET MET A . n 
A 1 290 ILE 290 827  827  ILE ILE A . n 
A 1 291 ARG 291 828  828  ARG ARG A . n 
A 1 292 HIS 292 829  829  HIS HIS A . n 
A 1 293 THR 293 830  830  THR THR A . n 
A 1 294 THR 294 831  831  THR THR A . n 
A 1 295 ASN 295 832  832  ASN ASN A . n 
A 1 296 LEU 296 833  833  LEU LEU A . n 
A 1 297 THR 297 834  834  THR THR A . n 
A 1 298 LEU 298 835  835  LEU LEU A . n 
A 1 299 TRP 299 836  836  TRP TRP A . n 
A 1 300 PHE 300 837  837  PHE PHE A . n 
A 1 301 GLU 301 838  838  GLU GLU A . n 
A 1 302 LYS 302 839  839  LYS LYS A . n 
A 1 303 CYS 303 840  840  CYS CYS A . n 
A 1 304 ILE 304 841  841  ILE ILE A . n 
A 1 305 VAL 305 842  842  VAL VAL A . n 
A 1 306 GLU 306 843  843  GLU GLU A . n 
A 1 307 ALA 307 844  844  ALA ALA A . n 
A 1 308 GLU 308 845  845  GLU GLU A . n 
A 1 309 ASN 309 846  846  ASN ASN A . n 
A 1 310 PHE 310 847  847  PHE PHE A . n 
A 1 311 GLU 311 848  848  GLU GLU A . n 
A 1 312 GLU 312 849  849  GLU GLU A . n 
A 1 313 ARG 313 850  850  ARG ARG A . n 
A 1 314 VAL 314 851  851  VAL VAL A . n 
A 1 315 ALA 315 852  852  ALA ALA A . n 
A 1 316 VAL 316 853  853  VAL VAL A . n 
A 1 317 LEU 317 854  854  LEU LEU A . n 
A 1 318 SER 318 855  855  SER SER A . n 
A 1 319 ARG 319 856  856  ARG ARG A . n 
A 1 320 ILE 320 857  857  ILE ILE A . n 
A 1 321 ILE 321 858  858  ILE ILE A . n 
A 1 322 GLU 322 859  859  GLU GLU A . n 
A 1 323 ILE 323 860  860  ILE ILE A . n 
A 1 324 LEU 324 861  861  LEU LEU A . n 
A 1 325 GLN 325 862  862  GLN GLN A . n 
A 1 326 VAL 326 863  863  VAL VAL A . n 
A 1 327 PHE 327 864  864  PHE PHE A . n 
A 1 328 GLN 328 865  865  GLN GLN A . n 
A 1 329 ASP 329 866  866  ASP ASP A . n 
A 1 330 LEU 330 867  867  LEU LEU A . n 
A 1 331 ASN 331 868  868  ASN ASN A . n 
A 1 332 ASN 332 869  869  ASN ASN A . n 
A 1 333 PHE 333 870  870  PHE PHE A . n 
A 1 334 ASN 334 871  871  ASN ASN A . n 
A 1 335 GLY 335 872  872  GLY GLY A . n 
A 1 336 VAL 336 873  873  VAL VAL A . n 
A 1 337 LEU 337 874  874  LEU LEU A . n 
A 1 338 GLU 338 875  875  GLU GLU A . n 
A 1 339 ILE 339 876  876  ILE ILE A . n 
A 1 340 VAL 340 877  877  VAL VAL A . n 
A 1 341 SER 341 878  878  SER SER A . n 
A 1 342 ALA 342 879  879  ALA ALA A . n 
A 1 343 VAL 343 880  880  VAL VAL A . n 
A 1 344 ASN 344 881  881  ASN ASN A . n 
A 1 345 SER 345 882  882  SER SER A . n 
A 1 346 VAL 346 883  883  VAL VAL A . n 
A 1 347 SER 347 884  884  SER SER A . n 
A 1 348 VAL 348 885  885  VAL VAL A . n 
A 1 349 TYR 349 886  886  TYR TYR A . n 
A 1 350 ARG 350 887  887  ARG ARG A . n 
A 1 351 LEU 351 888  888  LEU LEU A . n 
A 1 352 ASP 352 889  889  ASP ASP A . n 
A 1 353 HIS 353 890  890  HIS HIS A . n 
A 1 354 THR 354 891  891  THR THR A . n 
A 1 355 PHE 355 892  892  PHE PHE A . n 
A 1 356 GLU 356 893  893  GLU GLU A . n 
A 1 357 ALA 357 894  894  ALA ALA A . n 
A 1 358 LEU 358 895  895  LEU LEU A . n 
A 1 359 GLN 359 896  896  GLN GLN A . n 
A 1 360 GLU 360 897  897  GLU GLU A . n 
A 1 361 ARG 361 898  898  ARG ARG A . n 
A 1 362 LYS 362 899  899  LYS LYS A . n 
A 1 363 ARG 363 900  900  ARG ARG A . n 
A 1 364 LYS 364 901  901  LYS LYS A . n 
A 1 365 ILE 365 902  902  ILE ILE A . n 
A 1 366 LEU 366 903  903  LEU LEU A . n 
A 1 367 ASP 367 904  904  ASP ASP A . n 
A 1 368 GLU 368 905  905  GLU GLU A . n 
A 1 369 ALA 369 906  906  ALA ALA A . n 
A 1 370 VAL 370 907  907  VAL VAL A . n 
A 1 371 GLU 371 908  908  GLU GLU A . n 
A 1 372 LEU 372 909  909  LEU LEU A . n 
A 1 373 SER 373 910  910  SER SER A . n 
A 1 374 GLN 374 911  911  GLN GLN A . n 
A 1 375 ASP 375 912  912  ASP ASP A . n 
A 1 376 HIS 376 913  913  HIS HIS A . n 
A 1 377 PHE 377 914  914  PHE PHE A . n 
A 1 378 LYS 378 915  915  LYS LYS A . n 
A 1 379 LYS 379 916  916  LYS LYS A . n 
A 1 380 TYR 380 917  917  TYR TYR A . n 
A 1 381 LEU 381 918  918  LEU LEU A . n 
A 1 382 VAL 382 919  919  VAL VAL A . n 
A 1 383 LYS 383 920  920  LYS LYS A . n 
A 1 384 LEU 384 921  921  LEU LEU A . n 
A 1 385 LYS 385 922  922  LYS LYS A . n 
A 1 386 SER 386 923  923  SER SER A . n 
A 1 387 ILE 387 924  924  ILE ILE A . n 
A 1 388 ASN 388 925  925  ASN ASN A . n 
A 1 389 PRO 389 926  926  PRO PRO A . n 
A 1 390 PRO 390 927  927  PRO PRO A . n 
A 1 391 CYS 391 928  928  CYS CYS A . n 
A 1 392 VAL 392 929  929  VAL VAL A . n 
A 1 393 PRO 393 930  930  PRO PRO A . n 
A 1 394 PHE 394 931  931  PHE PHE A . n 
A 1 395 PHE 395 932  932  PHE PHE A . n 
A 1 396 GLY 396 933  933  GLY GLY A . n 
A 1 397 ILE 397 934  934  ILE ILE A . n 
A 1 398 TYR 398 935  935  TYR TYR A . n 
A 1 399 LEU 399 936  936  LEU LEU A . n 
A 1 400 THR 400 937  937  THR THR A . n 
A 1 401 ASN 401 938  938  ASN ASN A . n 
A 1 402 ILE 402 939  939  ILE ILE A . n 
A 1 403 LEU 403 940  940  LEU LEU A . n 
A 1 404 LYS 404 941  941  LYS LYS A . n 
A 1 405 THR 405 942  942  THR THR A . n 
A 1 406 GLU 406 943  943  GLU GLU A . n 
A 1 407 GLU 407 944  944  GLU GLU A . n 
A 1 408 GLY 408 945  945  GLY GLY A . n 
A 1 409 ASN 409 946  946  ASN ASN A . n 
A 1 410 ASN 410 947  947  ASN ASN A . n 
A 1 411 ASP 411 948  948  ASP ASP A . n 
A 1 412 PHE 412 949  949  PHE PHE A . n 
A 1 413 LEU 413 950  950  LEU LEU A . n 
A 1 414 LYS 414 951  951  LYS LYS A . n 
A 1 415 LYS 415 952  952  LYS LYS A . n 
A 1 416 LYS 416 953  953  LYS LYS A . n 
A 1 417 GLY 417 954  954  GLY GLY A . n 
A 1 418 LYS 418 955  955  LYS LYS A . n 
A 1 419 ASP 419 956  956  ASP ASP A . n 
A 1 420 LEU 420 957  957  LEU LEU A . n 
A 1 421 ILE 421 958  958  ILE ILE A . n 
A 1 422 ASN 422 959  959  ASN ASN A . n 
A 1 423 PHE 423 960  960  PHE PHE A . n 
A 1 424 SER 424 961  961  SER SER A . n 
A 1 425 LYS 425 962  962  LYS LYS A . n 
A 1 426 ARG 426 963  963  ARG ARG A . n 
A 1 427 ARG 427 964  964  ARG ARG A . n 
A 1 428 LYS 428 965  965  LYS LYS A . n 
A 1 429 VAL 429 966  966  VAL VAL A . n 
A 1 430 ALA 430 967  967  ALA ALA A . n 
A 1 431 GLU 431 968  968  GLU GLU A . n 
A 1 432 ILE 432 969  969  ILE ILE A . n 
A 1 433 THR 433 970  970  THR THR A . n 
A 1 434 GLY 434 971  971  GLY GLY A . n 
A 1 435 GLU 435 972  972  GLU GLU A . n 
A 1 436 ILE 436 973  973  ILE ILE A . n 
A 1 437 GLN 437 974  974  GLN GLN A . n 
A 1 438 GLN 438 975  975  GLN GLN A . n 
A 1 439 TYR 439 976  976  TYR TYR A . n 
A 1 440 GLN 440 977  977  GLN GLN A . n 
A 1 441 ASN 441 978  978  ASN ASN A . n 
A 1 442 GLN 442 979  979  GLN GLN A . n 
A 1 443 PRO 443 980  980  PRO PRO A . n 
A 1 444 TYR 444 981  981  TYR TYR A . n 
A 1 445 CYS 445 982  982  CYS CYS A . n 
A 1 446 LEU 446 983  983  LEU LEU A . n 
A 1 447 ARG 447 984  984  ARG ARG A . n 
A 1 448 ILE 448 985  985  ILE ILE A . n 
A 1 449 GLU 449 986  986  GLU GLU A . n 
A 1 450 PRO 450 987  987  PRO PRO A . n 
A 1 451 ASP 451 988  988  ASP ASP A . n 
A 1 452 MET 452 989  989  MET MET A . n 
A 1 453 ARG 453 990  990  ARG ARG A . n 
A 1 454 ARG 454 991  991  ARG ARG A . n 
A 1 455 PHE 455 992  992  PHE PHE A . n 
A 1 456 PHE 456 993  993  PHE PHE A . n 
A 1 457 GLU 457 994  994  GLU GLU A . n 
A 1 458 ASN 458 995  995  ASN ASN A . n 
A 1 459 LEU 459 996  996  LEU LEU A . n 
A 1 460 ASN 460 997  997  ASN ASN A . n 
A 1 461 PRO 461 998  998  PRO PRO A . n 
A 1 462 MET 462 999  999  MET MET A . n 
A 1 463 GLY 463 1000 1000 GLY GLY A . n 
A 1 464 SER 464 1001 1001 SER SER A . n 
A 1 465 ALA 465 1002 1002 ALA ALA A . n 
A 1 466 SER 466 1003 1003 SER SER A . n 
A 1 467 GLU 467 1004 1004 GLU GLU A . n 
A 1 468 LYS 468 1005 1005 LYS LYS A . n 
A 1 469 GLU 469 1006 1006 GLU GLU A . n 
A 1 470 PHE 470 1007 1007 PHE PHE A . n 
A 1 471 THR 471 1008 1008 THR THR A . n 
A 1 472 ASP 472 1009 1009 ASP ASP A . n 
A 1 473 TYR 473 1010 1010 TYR TYR A . n 
A 1 474 LEU 474 1011 1011 LEU LEU A . n 
A 1 475 PHE 475 1012 1012 PHE PHE A . n 
A 1 476 ASN 476 1013 1013 ASN ASN A . n 
A 1 477 LYS 477 1014 1014 LYS LYS A . n 
A 1 478 SER 478 1015 1015 SER SER A . n 
A 1 479 LEU 479 1016 1016 LEU LEU A . n 
A 1 480 GLU 480 1017 1017 GLU GLU A . n 
A 1 481 ILE 481 1018 1018 ILE ILE A . n 
A 1 482 GLU 482 1019 1019 GLU GLU A . n 
A 1 483 PRO 483 1020 1020 PRO PRO A . n 
A 1 484 ARG 484 1021 1021 ARG ARG A . n 
A 1 485 ASN 485 1022 1022 ASN ASN A . n 
A 1 486 CYS 486 1023 1023 CYS CYS A . n 
A 1 487 LYS 487 1024 1024 LYS LYS A . n 
A 1 488 GLN 488 1025 1025 GLN GLN A . n 
A 1 489 PRO 489 1026 1026 PRO PRO A . n 
A 1 490 PRO 490 1027 1027 PRO PRO A . n 
A 1 491 ARG 491 1028 1028 ARG ARG A . n 
A 1 492 PHE 492 1029 1029 PHE PHE A . n 
A 1 493 PRO 493 1030 1030 PRO PRO A . n 
A 1 494 ARG 494 1031 1031 ARG ARG A . n 
A 1 495 LYS 495 1032 1032 LYS LYS A . n 
A 1 496 SER 496 1033 1033 SER SER A . n 
A 1 497 THR 497 1034 1034 THR THR A . n 
A 1 498 PHE 498 1035 1035 PHE PHE A . n 
A 1 499 SER 499 1036 1036 SER SER A . n 
A 1 500 LEU 500 1037 1037 LEU LEU A . n 
A 1 501 LYS 501 1038 1038 LYS LYS A . n 
A 1 502 SER 502 1039 1039 SER SER A . n 
A 1 503 PRO 503 1040 1040 PRO PRO A . n 
A 1 504 GLY 504 1041 1041 GLY GLY A . n 
A 1 505 ILE 505 1042 1042 ILE ILE A . n 
A 1 506 ARG 506 1043 1043 ARG ARG A . n 
A 1 507 PRO 507 1044 1044 PRO PRO A . n 
A 1 508 ASN 508 1045 1045 ASN ASN A . n 
A 1 509 THR 509 1046 ?    ?   ?   A . n 
A 1 510 GLY 510 1047 ?    ?   ?   A . n 
A 1 511 ARG 511 1048 ?    ?   ?   A . n 
A 1 512 HIS 512 1049 ?    ?   ?   A . n 
A 1 513 GLY 513 1050 ?    ?   ?   A . n 
A 1 514 SER 514 1051 ?    ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ASW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ASW 
_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 
B 2 A1ASW 1   2001 2001 A1ASW LIG A . 
C 3 HOH   1   2101 321  HOH   HOH A . 
C 3 HOH   2   2102 319  HOH   HOH A . 
C 3 HOH   3   2103 286  HOH   HOH A . 
C 3 HOH   4   2104 450  HOH   HOH A . 
C 3 HOH   5   2105 435  HOH   HOH A . 
C 3 HOH   6   2106 339  HOH   HOH A . 
C 3 HOH   7   2107 134  HOH   HOH A . 
C 3 HOH   8   2108 240  HOH   HOH A . 
C 3 HOH   9   2109 112  HOH   HOH A . 
C 3 HOH   10  2110 137  HOH   HOH A . 
C 3 HOH   11  2111 56   HOH   HOH A . 
C 3 HOH   12  2112 303  HOH   HOH A . 
C 3 HOH   13  2113 412  HOH   HOH A . 
C 3 HOH   14  2114 383  HOH   HOH A . 
C 3 HOH   15  2115 154  HOH   HOH A . 
C 3 HOH   16  2116 266  HOH   HOH A . 
C 3 HOH   17  2117 265  HOH   HOH A . 
C 3 HOH   18  2118 253  HOH   HOH A . 
C 3 HOH   19  2119 76   HOH   HOH A . 
C 3 HOH   20  2120 178  HOH   HOH A . 
C 3 HOH   21  2121 150  HOH   HOH A . 
C 3 HOH   22  2122 201  HOH   HOH A . 
C 3 HOH   23  2123 243  HOH   HOH A . 
C 3 HOH   24  2124 395  HOH   HOH A . 
C 3 HOH   25  2125 32   HOH   HOH A . 
C 3 HOH   26  2126 93   HOH   HOH A . 
C 3 HOH   27  2127 451  HOH   HOH A . 
C 3 HOH   28  2128 3    HOH   HOH A . 
C 3 HOH   29  2129 344  HOH   HOH A . 
C 3 HOH   30  2130 42   HOH   HOH A . 
C 3 HOH   31  2131 131  HOH   HOH A . 
C 3 HOH   32  2132 205  HOH   HOH A . 
C 3 HOH   33  2133 370  HOH   HOH A . 
C 3 HOH   34  2134 66   HOH   HOH A . 
C 3 HOH   35  2135 182  HOH   HOH A . 
C 3 HOH   36  2136 315  HOH   HOH A . 
C 3 HOH   37  2137 25   HOH   HOH A . 
C 3 HOH   38  2138 13   HOH   HOH A . 
C 3 HOH   39  2139 63   HOH   HOH A . 
C 3 HOH   40  2140 122  HOH   HOH A . 
C 3 HOH   41  2141 202  HOH   HOH A . 
C 3 HOH   42  2142 106  HOH   HOH A . 
C 3 HOH   43  2143 251  HOH   HOH A . 
C 3 HOH   44  2144 188  HOH   HOH A . 
C 3 HOH   45  2145 12   HOH   HOH A . 
C 3 HOH   46  2146 313  HOH   HOH A . 
C 3 HOH   47  2147 35   HOH   HOH A . 
C 3 HOH   48  2148 333  HOH   HOH A . 
C 3 HOH   49  2149 351  HOH   HOH A . 
C 3 HOH   50  2150 28   HOH   HOH A . 
C 3 HOH   51  2151 10   HOH   HOH A . 
C 3 HOH   52  2152 440  HOH   HOH A . 
C 3 HOH   53  2153 430  HOH   HOH A . 
C 3 HOH   54  2154 52   HOH   HOH A . 
C 3 HOH   55  2155 236  HOH   HOH A . 
C 3 HOH   56  2156 167  HOH   HOH A . 
C 3 HOH   57  2157 375  HOH   HOH A . 
C 3 HOH   58  2158 157  HOH   HOH A . 
C 3 HOH   59  2159 91   HOH   HOH A . 
C 3 HOH   60  2160 20   HOH   HOH A . 
C 3 HOH   61  2161 360  HOH   HOH A . 
C 3 HOH   62  2162 454  HOH   HOH A . 
C 3 HOH   63  2163 133  HOH   HOH A . 
C 3 HOH   64  2164 95   HOH   HOH A . 
C 3 HOH   65  2165 172  HOH   HOH A . 
C 3 HOH   66  2166 165  HOH   HOH A . 
C 3 HOH   67  2167 399  HOH   HOH A . 
C 3 HOH   68  2168 9    HOH   HOH A . 
C 3 HOH   69  2169 24   HOH   HOH A . 
C 3 HOH   70  2170 58   HOH   HOH A . 
C 3 HOH   71  2171 43   HOH   HOH A . 
C 3 HOH   72  2172 367  HOH   HOH A . 
C 3 HOH   73  2173 67   HOH   HOH A . 
C 3 HOH   74  2174 26   HOH   HOH A . 
C 3 HOH   75  2175 115  HOH   HOH A . 
C 3 HOH   76  2176 96   HOH   HOH A . 
C 3 HOH   77  2177 77   HOH   HOH A . 
C 3 HOH   78  2178 73   HOH   HOH A . 
C 3 HOH   79  2179 189  HOH   HOH A . 
C 3 HOH   80  2180 75   HOH   HOH A . 
C 3 HOH   81  2181 89   HOH   HOH A . 
C 3 HOH   82  2182 297  HOH   HOH A . 
C 3 HOH   83  2183 455  HOH   HOH A . 
C 3 HOH   84  2184 215  HOH   HOH A . 
C 3 HOH   85  2185 79   HOH   HOH A . 
C 3 HOH   86  2186 161  HOH   HOH A . 
C 3 HOH   87  2187 220  HOH   HOH A . 
C 3 HOH   88  2188 59   HOH   HOH A . 
C 3 HOH   89  2189 312  HOH   HOH A . 
C 3 HOH   90  2190 83   HOH   HOH A . 
C 3 HOH   91  2191 318  HOH   HOH A . 
C 3 HOH   92  2192 290  HOH   HOH A . 
C 3 HOH   93  2193 136  HOH   HOH A . 
C 3 HOH   94  2194 109  HOH   HOH A . 
C 3 HOH   95  2195 126  HOH   HOH A . 
C 3 HOH   96  2196 132  HOH   HOH A . 
C 3 HOH   97  2197 269  HOH   HOH A . 
C 3 HOH   98  2198 208  HOH   HOH A . 
C 3 HOH   99  2199 295  HOH   HOH A . 
C 3 HOH   100 2200 276  HOH   HOH A . 
C 3 HOH   101 2201 191  HOH   HOH A . 
C 3 HOH   102 2202 304  HOH   HOH A . 
C 3 HOH   103 2203 145  HOH   HOH A . 
C 3 HOH   104 2204 31   HOH   HOH A . 
C 3 HOH   105 2205 30   HOH   HOH A . 
C 3 HOH   106 2206 18   HOH   HOH A . 
C 3 HOH   107 2207 316  HOH   HOH A . 
C 3 HOH   108 2208 62   HOH   HOH A . 
C 3 HOH   109 2209 391  HOH   HOH A . 
C 3 HOH   110 2210 180  HOH   HOH A . 
C 3 HOH   111 2211 403  HOH   HOH A . 
C 3 HOH   112 2212 5    HOH   HOH A . 
C 3 HOH   113 2213 16   HOH   HOH A . 
C 3 HOH   114 2214 7    HOH   HOH A . 
C 3 HOH   115 2215 159  HOH   HOH A . 
C 3 HOH   116 2216 81   HOH   HOH A . 
C 3 HOH   117 2217 211  HOH   HOH A . 
C 3 HOH   118 2218 6    HOH   HOH A . 
C 3 HOH   119 2219 33   HOH   HOH A . 
C 3 HOH   120 2220 228  HOH   HOH A . 
C 3 HOH   121 2221 55   HOH   HOH A . 
C 3 HOH   122 2222 307  HOH   HOH A . 
C 3 HOH   123 2223 68   HOH   HOH A . 
C 3 HOH   124 2224 280  HOH   HOH A . 
C 3 HOH   125 2225 39   HOH   HOH A . 
C 3 HOH   126 2226 190  HOH   HOH A . 
C 3 HOH   127 2227 46   HOH   HOH A . 
C 3 HOH   128 2228 8    HOH   HOH A . 
C 3 HOH   129 2229 135  HOH   HOH A . 
C 3 HOH   130 2230 129  HOH   HOH A . 
C 3 HOH   131 2231 210  HOH   HOH A . 
C 3 HOH   132 2232 123  HOH   HOH A . 
C 3 HOH   133 2233 4    HOH   HOH A . 
C 3 HOH   134 2234 64   HOH   HOH A . 
C 3 HOH   135 2235 354  HOH   HOH A . 
C 3 HOH   136 2236 69   HOH   HOH A . 
C 3 HOH   137 2237 217  HOH   HOH A . 
C 3 HOH   138 2238 371  HOH   HOH A . 
C 3 HOH   139 2239 372  HOH   HOH A . 
C 3 HOH   140 2240 14   HOH   HOH A . 
C 3 HOH   141 2241 11   HOH   HOH A . 
C 3 HOH   142 2242 78   HOH   HOH A . 
C 3 HOH   143 2243 429  HOH   HOH A . 
C 3 HOH   144 2244 101  HOH   HOH A . 
C 3 HOH   145 2245 384  HOH   HOH A . 
C 3 HOH   146 2246 88   HOH   HOH A . 
C 3 HOH   147 2247 258  HOH   HOH A . 
C 3 HOH   148 2248 287  HOH   HOH A . 
C 3 HOH   149 2249 47   HOH   HOH A . 
C 3 HOH   150 2250 241  HOH   HOH A . 
C 3 HOH   151 2251 284  HOH   HOH A . 
C 3 HOH   152 2252 29   HOH   HOH A . 
C 3 HOH   153 2253 151  HOH   HOH A . 
C 3 HOH   154 2254 94   HOH   HOH A . 
C 3 HOH   155 2255 358  HOH   HOH A . 
C 3 HOH   156 2256 156  HOH   HOH A . 
C 3 HOH   157 2257 1    HOH   HOH A . 
C 3 HOH   158 2258 200  HOH   HOH A . 
C 3 HOH   159 2259 273  HOH   HOH A . 
C 3 HOH   160 2260 212  HOH   HOH A . 
C 3 HOH   161 2261 184  HOH   HOH A . 
C 3 HOH   162 2262 50   HOH   HOH A . 
C 3 HOH   163 2263 282  HOH   HOH A . 
C 3 HOH   164 2264 92   HOH   HOH A . 
C 3 HOH   165 2265 186  HOH   HOH A . 
C 3 HOH   166 2266 2    HOH   HOH A . 
C 3 HOH   167 2267 87   HOH   HOH A . 
C 3 HOH   168 2268 23   HOH   HOH A . 
C 3 HOH   169 2269 390  HOH   HOH A . 
C 3 HOH   170 2270 148  HOH   HOH A . 
C 3 HOH   171 2271 404  HOH   HOH A . 
C 3 HOH   172 2272 388  HOH   HOH A . 
C 3 HOH   173 2273 198  HOH   HOH A . 
C 3 HOH   174 2274 113  HOH   HOH A . 
C 3 HOH   175 2275 447  HOH   HOH A . 
C 3 HOH   176 2276 434  HOH   HOH A . 
C 3 HOH   177 2277 222  HOH   HOH A . 
C 3 HOH   178 2278 38   HOH   HOH A . 
C 3 HOH   179 2279 306  HOH   HOH A . 
C 3 HOH   180 2280 216  HOH   HOH A . 
C 3 HOH   181 2281 213  HOH   HOH A . 
C 3 HOH   182 2282 41   HOH   HOH A . 
C 3 HOH   183 2283 271  HOH   HOH A . 
C 3 HOH   184 2284 234  HOH   HOH A . 
C 3 HOH   185 2285 326  HOH   HOH A . 
C 3 HOH   186 2286 348  HOH   HOH A . 
C 3 HOH   187 2287 70   HOH   HOH A . 
C 3 HOH   188 2288 362  HOH   HOH A . 
C 3 HOH   189 2289 279  HOH   HOH A . 
C 3 HOH   190 2290 110  HOH   HOH A . 
C 3 HOH   191 2291 244  HOH   HOH A . 
C 3 HOH   192 2292 223  HOH   HOH A . 
C 3 HOH   193 2293 400  HOH   HOH A . 
C 3 HOH   194 2294 71   HOH   HOH A . 
C 3 HOH   195 2295 424  HOH   HOH A . 
C 3 HOH   196 2296 193  HOH   HOH A . 
C 3 HOH   197 2297 152  HOH   HOH A . 
C 3 HOH   198 2298 341  HOH   HOH A . 
C 3 HOH   199 2299 143  HOH   HOH A . 
C 3 HOH   200 2300 227  HOH   HOH A . 
C 3 HOH   201 2301 104  HOH   HOH A . 
C 3 HOH   202 2302 410  HOH   HOH A . 
C 3 HOH   203 2303 270  HOH   HOH A . 
C 3 HOH   204 2304 27   HOH   HOH A . 
C 3 HOH   205 2305 85   HOH   HOH A . 
C 3 HOH   206 2306 254  HOH   HOH A . 
C 3 HOH   207 2307 386  HOH   HOH A . 
C 3 HOH   208 2308 378  HOH   HOH A . 
C 3 HOH   209 2309 116  HOH   HOH A . 
C 3 HOH   210 2310 147  HOH   HOH A . 
C 3 HOH   211 2311 86   HOH   HOH A . 
C 3 HOH   212 2312 163  HOH   HOH A . 
C 3 HOH   213 2313 103  HOH   HOH A . 
C 3 HOH   214 2314 389  HOH   HOH A . 
C 3 HOH   215 2315 340  HOH   HOH A . 
C 3 HOH   216 2316 385  HOH   HOH A . 
C 3 HOH   217 2317 120  HOH   HOH A . 
C 3 HOH   218 2318 369  HOH   HOH A . 
C 3 HOH   219 2319 170  HOH   HOH A . 
C 3 HOH   220 2320 409  HOH   HOH A . 
C 3 HOH   221 2321 45   HOH   HOH A . 
C 3 HOH   222 2322 296  HOH   HOH A . 
C 3 HOH   223 2323 204  HOH   HOH A . 
C 3 HOH   224 2324 173  HOH   HOH A . 
C 3 HOH   225 2325 229  HOH   HOH A . 
C 3 HOH   226 2326 255  HOH   HOH A . 
C 3 HOH   227 2327 21   HOH   HOH A . 
C 3 HOH   228 2328 117  HOH   HOH A . 
C 3 HOH   229 2329 268  HOH   HOH A . 
C 3 HOH   230 2330 124  HOH   HOH A . 
C 3 HOH   231 2331 218  HOH   HOH A . 
C 3 HOH   232 2332 242  HOH   HOH A . 
C 3 HOH   233 2333 317  HOH   HOH A . 
C 3 HOH   234 2334 97   HOH   HOH A . 
C 3 HOH   235 2335 394  HOH   HOH A . 
C 3 HOH   236 2336 80   HOH   HOH A . 
C 3 HOH   237 2337 335  HOH   HOH A . 
C 3 HOH   238 2338 54   HOH   HOH A . 
C 3 HOH   239 2339 301  HOH   HOH A . 
C 3 HOH   240 2340 102  HOH   HOH A . 
C 3 HOH   241 2341 22   HOH   HOH A . 
C 3 HOH   242 2342 305  HOH   HOH A . 
C 3 HOH   243 2343 176  HOH   HOH A . 
C 3 HOH   244 2344 411  HOH   HOH A . 
C 3 HOH   245 2345 162  HOH   HOH A . 
C 3 HOH   246 2346 407  HOH   HOH A . 
C 3 HOH   247 2347 108  HOH   HOH A . 
C 3 HOH   248 2348 37   HOH   HOH A . 
C 3 HOH   249 2349 221  HOH   HOH A . 
C 3 HOH   250 2350 98   HOH   HOH A . 
C 3 HOH   251 2351 177  HOH   HOH A . 
C 3 HOH   252 2352 100  HOH   HOH A . 
C 3 HOH   253 2353 194  HOH   HOH A . 
C 3 HOH   254 2354 462  HOH   HOH A . 
C 3 HOH   255 2355 187  HOH   HOH A . 
C 3 HOH   256 2356 17   HOH   HOH A . 
C 3 HOH   257 2357 51   HOH   HOH A . 
C 3 HOH   258 2358 277  HOH   HOH A . 
C 3 HOH   259 2359 294  HOH   HOH A . 
C 3 HOH   260 2360 179  HOH   HOH A . 
C 3 HOH   261 2361 127  HOH   HOH A . 
C 3 HOH   262 2362 275  HOH   HOH A . 
C 3 HOH   263 2363 60   HOH   HOH A . 
C 3 HOH   264 2364 141  HOH   HOH A . 
C 3 HOH   265 2365 413  HOH   HOH A . 
C 3 HOH   266 2366 125  HOH   HOH A . 
C 3 HOH   267 2367 111  HOH   HOH A . 
C 3 HOH   268 2368 84   HOH   HOH A . 
C 3 HOH   269 2369 414  HOH   HOH A . 
C 3 HOH   270 2370 356  HOH   HOH A . 
C 3 HOH   271 2371 65   HOH   HOH A . 
C 3 HOH   272 2372 334  HOH   HOH A . 
C 3 HOH   273 2373 15   HOH   HOH A . 
C 3 HOH   274 2374 203  HOH   HOH A . 
C 3 HOH   275 2375 40   HOH   HOH A . 
C 3 HOH   276 2376 245  HOH   HOH A . 
C 3 HOH   277 2377 338  HOH   HOH A . 
C 3 HOH   278 2378 206  HOH   HOH A . 
C 3 HOH   279 2379 168  HOH   HOH A . 
C 3 HOH   280 2380 381  HOH   HOH A . 
C 3 HOH   281 2381 138  HOH   HOH A . 
C 3 HOH   282 2382 443  HOH   HOH A . 
C 3 HOH   283 2383 439  HOH   HOH A . 
C 3 HOH   284 2384 164  HOH   HOH A . 
C 3 HOH   285 2385 114  HOH   HOH A . 
C 3 HOH   286 2386 53   HOH   HOH A . 
C 3 HOH   287 2387 380  HOH   HOH A . 
C 3 HOH   288 2388 332  HOH   HOH A . 
C 3 HOH   289 2389 250  HOH   HOH A . 
C 3 HOH   290 2390 107  HOH   HOH A . 
C 3 HOH   291 2391 121  HOH   HOH A . 
C 3 HOH   292 2392 233  HOH   HOH A . 
C 3 HOH   293 2393 300  HOH   HOH A . 
C 3 HOH   294 2394 350  HOH   HOH A . 
C 3 HOH   295 2395 214  HOH   HOH A . 
C 3 HOH   296 2396 364  HOH   HOH A . 
C 3 HOH   297 2397 352  HOH   HOH A . 
C 3 HOH   298 2398 310  HOH   HOH A . 
C 3 HOH   299 2399 438  HOH   HOH A . 
C 3 HOH   300 2400 196  HOH   HOH A . 
C 3 HOH   301 2401 226  HOH   HOH A . 
C 3 HOH   302 2402 224  HOH   HOH A . 
C 3 HOH   303 2403 368  HOH   HOH A . 
C 3 HOH   304 2404 207  HOH   HOH A . 
C 3 HOH   305 2405 34   HOH   HOH A . 
C 3 HOH   306 2406 298  HOH   HOH A . 
C 3 HOH   307 2407 140  HOH   HOH A . 
C 3 HOH   308 2408 458  HOH   HOH A . 
C 3 HOH   309 2409 457  HOH   HOH A . 
C 3 HOH   310 2410 175  HOH   HOH A . 
C 3 HOH   311 2411 418  HOH   HOH A . 
C 3 HOH   312 2412 437  HOH   HOH A . 
C 3 HOH   313 2413 142  HOH   HOH A . 
C 3 HOH   314 2414 308  HOH   HOH A . 
C 3 HOH   315 2415 82   HOH   HOH A . 
C 3 HOH   316 2416 139  HOH   HOH A . 
C 3 HOH   317 2417 267  HOH   HOH A . 
C 3 HOH   318 2418 288  HOH   HOH A . 
C 3 HOH   319 2419 169  HOH   HOH A . 
C 3 HOH   320 2420 449  HOH   HOH A . 
C 3 HOH   321 2421 323  HOH   HOH A . 
C 3 HOH   322 2422 199  HOH   HOH A . 
C 3 HOH   323 2423 259  HOH   HOH A . 
C 3 HOH   324 2424 382  HOH   HOH A . 
C 3 HOH   325 2425 343  HOH   HOH A . 
C 3 HOH   326 2426 377  HOH   HOH A . 
C 3 HOH   327 2427 431  HOH   HOH A . 
C 3 HOH   328 2428 461  HOH   HOH A . 
C 3 HOH   329 2429 392  HOH   HOH A . 
C 3 HOH   330 2430 328  HOH   HOH A . 
C 3 HOH   331 2431 453  HOH   HOH A . 
C 3 HOH   332 2432 105  HOH   HOH A . 
C 3 HOH   333 2433 420  HOH   HOH A . 
C 3 HOH   334 2434 302  HOH   HOH A . 
C 3 HOH   335 2435 166  HOH   HOH A . 
C 3 HOH   336 2436 36   HOH   HOH A . 
C 3 HOH   337 2437 376  HOH   HOH A . 
C 3 HOH   338 2438 263  HOH   HOH A . 
C 3 HOH   339 2439 262  HOH   HOH A . 
C 3 HOH   340 2440 299  HOH   HOH A . 
C 3 HOH   341 2441 406  HOH   HOH A . 
C 3 HOH   342 2442 185  HOH   HOH A . 
C 3 HOH   343 2443 158  HOH   HOH A . 
C 3 HOH   344 2444 428  HOH   HOH A . 
C 3 HOH   345 2445 444  HOH   HOH A . 
C 3 HOH   346 2446 44   HOH   HOH A . 
C 3 HOH   347 2447 446  HOH   HOH A . 
C 3 HOH   348 2448 336  HOH   HOH A . 
C 3 HOH   349 2449 118  HOH   HOH A . 
C 3 HOH   350 2450 363  HOH   HOH A . 
C 3 HOH   351 2451 357  HOH   HOH A . 
C 3 HOH   352 2452 153  HOH   HOH A . 
C 3 HOH   353 2453 291  HOH   HOH A . 
C 3 HOH   354 2454 249  HOH   HOH A . 
C 3 HOH   355 2455 396  HOH   HOH A . 
C 3 HOH   356 2456 247  HOH   HOH A . 
C 3 HOH   357 2457 195  HOH   HOH A . 
C 3 HOH   358 2458 452  HOH   HOH A . 
C 3 HOH   359 2459 379  HOH   HOH A . 
C 3 HOH   360 2460 349  HOH   HOH A . 
C 3 HOH   361 2461 355  HOH   HOH A . 
C 3 HOH   362 2462 272  HOH   HOH A . 
C 3 HOH   363 2463 345  HOH   HOH A . 
C 3 HOH   364 2464 459  HOH   HOH A . 
C 3 HOH   365 2465 285  HOH   HOH A . 
C 3 HOH   366 2466 342  HOH   HOH A . 
C 3 HOH   367 2467 416  HOH   HOH A . 
C 3 HOH   368 2468 393  HOH   HOH A . 
C 3 HOH   369 2469 387  HOH   HOH A . 
C 3 HOH   370 2470 309  HOH   HOH A . 
C 3 HOH   371 2471 405  HOH   HOH A . 
C 3 HOH   372 2472 425  HOH   HOH A . 
C 3 HOH   373 2473 260  HOH   HOH A . 
C 3 HOH   374 2474 366  HOH   HOH A . 
C 3 HOH   375 2475 192  HOH   HOH A . 
C 3 HOH   376 2476 155  HOH   HOH A . 
C 3 HOH   377 2477 314  HOH   HOH A . 
C 3 HOH   378 2478 421  HOH   HOH A . 
C 3 HOH   379 2479 398  HOH   HOH A . 
C 3 HOH   380 2480 436  HOH   HOH A . 
C 3 HOH   381 2481 289  HOH   HOH A . 
C 3 HOH   382 2482 397  HOH   HOH A . 
C 3 HOH   383 2483 448  HOH   HOH A . 
C 3 HOH   384 2484 219  HOH   HOH A . 
C 3 HOH   385 2485 359  HOH   HOH A . 
C 3 HOH   386 2486 373  HOH   HOH A . 
C 3 HOH   387 2487 346  HOH   HOH A . 
C 3 HOH   388 2488 292  HOH   HOH A . 
C 3 HOH   389 2489 422  HOH   HOH A . 
C 3 HOH   390 2490 160  HOH   HOH A . 
C 3 HOH   391 2491 128  HOH   HOH A . 
C 3 HOH   392 2492 231  HOH   HOH A . 
C 3 HOH   393 2493 293  HOH   HOH A . 
C 3 HOH   394 2494 365  HOH   HOH A . 
C 3 HOH   395 2495 327  HOH   HOH A . 
C 3 HOH   396 2496 256  HOH   HOH A . 
C 3 HOH   397 2497 361  HOH   HOH A . 
C 3 HOH   398 2498 337  HOH   HOH A . 
C 3 HOH   399 2499 130  HOH   HOH A . 
C 3 HOH   400 2500 442  HOH   HOH A . 
C 3 HOH   401 2501 353  HOH   HOH A . 
C 3 HOH   402 2502 197  HOH   HOH A . 
C 3 HOH   403 2503 61   HOH   HOH A . 
C 3 HOH   404 2504 238  HOH   HOH A . 
C 3 HOH   405 2505 48   HOH   HOH A . 
C 3 HOH   406 2506 119  HOH   HOH A . 
C 3 HOH   407 2507 311  HOH   HOH A . 
C 3 HOH   408 2508 322  HOH   HOH A . 
C 3 HOH   409 2509 433  HOH   HOH A . 
C 3 HOH   410 2510 99   HOH   HOH A . 
C 3 HOH   411 2511 427  HOH   HOH A . 
C 3 HOH   412 2512 264  HOH   HOH A . 
C 3 HOH   413 2513 225  HOH   HOH A . 
C 3 HOH   414 2514 144  HOH   HOH A . 
C 3 HOH   415 2515 445  HOH   HOH A . 
C 3 HOH   416 2516 261  HOH   HOH A . 
C 3 HOH   417 2517 232  HOH   HOH A . 
C 3 HOH   418 2518 278  HOH   HOH A . 
C 3 HOH   419 2519 183  HOH   HOH A . 
C 3 HOH   420 2520 423  HOH   HOH A . 
C 3 HOH   421 2521 246  HOH   HOH A . 
C 3 HOH   422 2522 252  HOH   HOH A . 
C 3 HOH   423 2523 419  HOH   HOH A . 
C 3 HOH   424 2524 415  HOH   HOH A . 
C 3 HOH   425 2525 283  HOH   HOH A . 
C 3 HOH   426 2526 239  HOH   HOH A . 
C 3 HOH   427 2527 257  HOH   HOH A . 
C 3 HOH   428 2528 426  HOH   HOH A . 
C 3 HOH   429 2529 181  HOH   HOH A . 
C 3 HOH   430 2530 274  HOH   HOH A . 
C 3 HOH   431 2531 174  HOH   HOH A . 
C 3 HOH   432 2532 209  HOH   HOH A . 
C 3 HOH   433 2533 146  HOH   HOH A . 
C 3 HOH   434 2534 347  HOH   HOH A . 
C 3 HOH   435 2535 90   HOH   HOH A . 
C 3 HOH   436 2536 74   HOH   HOH A . 
C 3 HOH   437 2537 237  HOH   HOH A . 
C 3 HOH   438 2538 72   HOH   HOH A . 
C 3 HOH   439 2539 331  HOH   HOH A . 
C 3 HOH   440 2540 235  HOH   HOH A . 
C 3 HOH   441 2541 324  HOH   HOH A . 
C 3 HOH   442 2542 401  HOH   HOH A . 
C 3 HOH   443 2543 230  HOH   HOH A . 
C 3 HOH   444 2544 171  HOH   HOH A . 
C 3 HOH   445 2545 374  HOH   HOH A . 
C 3 HOH   446 2546 19   HOH   HOH A . 
C 3 HOH   447 2547 149  HOH   HOH A . 
C 3 HOH   448 2548 330  HOH   HOH A . 
C 3 HOH   449 2549 248  HOH   HOH A . 
C 3 HOH   450 2550 49   HOH   HOH A . 
C 3 HOH   451 2551 402  HOH   HOH A . 
C 3 HOH   452 2552 417  HOH   HOH A . 
C 3 HOH   453 2553 281  HOH   HOH A . 
C 3 HOH   454 2554 320  HOH   HOH A . 
C 3 HOH   455 2555 57   HOH   HOH A . 
C 3 HOH   456 2556 456  HOH   HOH A . 
C 3 HOH   457 2557 325  HOH   HOH A . 
C 3 HOH   458 2558 329  HOH   HOH A . 
C 3 HOH   459 2559 432  HOH   HOH A . 
C 3 HOH   460 2560 460  HOH   HOH A . 
C 3 HOH   461 2561 441  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? dev_1565 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BVI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.014 
_cell.length_a_esd                 ? 
_cell.length_b                     86.382 
_cell.length_b_esd                 ? 
_cell.length_c                     106.367 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9BVI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BVI 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.98 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '22% PEG3350, 100 mM Bis-Tris propane, pH 7.5, 200 mM sodium sulfate, 5% glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-08-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.978 
_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                        'APS BEAMLINE 21-ID-F' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-F 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BVI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               50.00 
_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                                     56235 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_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                               0.972 
_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                                0.070 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   1.000 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.066 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.80 1.83  ? ? ? ? ? ? 2792 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.039 ? ? 1.266 0.395 ? 1  1 0.760 0.929 ? 100.0 ? 1.202 ? ? ? ? ? ? ? ? ? 
1.83 1.86  ? ? ? ? ? ? 2748 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.065 ? ? 1.018 0.318 ? 2  1 0.822 0.950 ? 100.0 ? 0.966 ? ? ? ? ? ? ? ? ? 
1.86 1.90  ? ? ? ? ? ? 2793 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.057 ? ? 0.862 0.269 ? 3  1 0.854 0.960 ? 100.0 ? 0.818 ? ? ? ? ? ? ? ? ? 
1.90 1.94  ? ? ? ? ? ? 2780 ? ? ? ? ? ? ? ? ? ? ? 10.2 1.138 ? ? 0.759 0.238 ? 4  1 0.880 0.967 ? 100.0 ? 0.720 ? ? ? ? ? ? ? ? ? 
1.94 1.98  ? ? ? ? ? ? 2765 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.029 ? ? 0.546 0.170 ? 5  1 0.940 0.984 ? 100.0 ? 0.519 ? ? ? ? ? ? ? ? ? 
1.98 2.03  ? ? ? ? ? ? 2774 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.065 ? ? 0.381 0.119 ? 6  1 0.963 0.991 ? 100.0 ? 0.362 ? ? ? ? ? ? ? ? ? 
2.03 2.08  ? ? ? ? ? ? 2800 ? ? ? ? ? ? ? ? ? ? ? 10.3 0.971 ? ? 0.329 0.102 ? 7  1 0.972 0.993 ? 100.0 ? 0.312 ? ? ? ? ? ? ? ? ? 
2.08 2.13  ? ? ? ? ? ? 2756 ? ? ? ? ? ? ? ? ? ? ? 10.3 0.758 ? ? 0.261 0.082 ? 8  1 0.975 0.994 ? 100.0 ? 0.248 ? ? ? ? ? ? ? ? ? 
2.13 2.20  ? ? ? ? ? ? 2777 ? ? ? ? ? ? ? ? ? ? ? 10.4 1.058 ? ? 0.203 0.063 ? 9  1 0.988 0.997 ? 100.0 ? 0.193 ? ? ? ? ? ? ? ? ? 
2.20 2.27  ? ? ? ? ? ? 2792 ? ? ? ? ? ? ? ? ? ? ? 10.3 0.759 ? ? 0.192 0.060 ? 10 1 0.987 0.997 ? 100.0 ? 0.183 ? ? ? ? ? ? ? ? ? 
2.27 2.35  ? ? ? ? ? ? 2800 ? ? ? ? ? ? ? ? ? ? ? 10.3 0.831 ? ? 0.154 0.048 ? 11 1 0.993 0.998 ? 100.0 ? 0.147 ? ? ? ? ? ? ? ? ? 
2.35 2.44  ? ? ? ? ? ? 2800 ? ? ? ? ? ? ? ? ? ? ? 10.4 1.058 ? ? 0.131 0.041 ? 12 1 0.993 0.998 ? 100.0 ? 0.124 ? ? ? ? ? ? ? ? ? 
2.44 2.55  ? ? ? ? ? ? 2789 ? ? ? ? ? ? ? ? ? ? ? 10.4 1.012 ? ? 0.107 0.033 ? 13 1 0.995 0.999 ? 100.0 ? 0.101 ? ? ? ? ? ? ? ? ? 
2.55 2.69  ? ? ? ? ? ? 2825 ? ? ? ? ? ? ? ? ? ? ? 10.3 0.878 ? ? 0.091 0.028 ? 14 1 0.997 0.999 ? 100.0 ? 0.086 ? ? ? ? ? ? ? ? ? 
2.69 2.86  ? ? ? ? ? ? 2806 ? ? ? ? ? ? ? ? ? ? ? 10.3 0.960 ? ? 0.073 0.023 ? 15 1 0.998 0.999 ? 100.0 ? 0.069 ? ? ? ? ? ? ? ? ? 
2.86 3.08  ? ? ? ? ? ? 2822 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.051 ? ? 0.071 0.022 ? 16 1 0.998 0.999 ? 100.0 ? 0.068 ? ? ? ? ? ? ? ? ? 
3.08 3.39  ? ? ? ? ? ? 2852 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.069 ? ? 0.067 0.021 ? 17 1 0.998 0.999 ? 100.0 ? 0.064 ? ? ? ? ? ? ? ? ? 
3.39 3.88  ? ? ? ? ? ? 2848 ? ? ? ? ? ? ? ? ? ? ? 10.2 0.846 ? ? 0.052 0.016 ? 18 1 0.999 1.000 ? 100.0 ? 0.049 ? ? ? ? ? ? ? ? ? 
3.88 4.88  ? ? ? ? ? ? 2895 ? ? ? ? ? ? ? ? ? ? ? 10.1 0.930 ? ? 0.039 0.012 ? 19 1 0.999 1.000 ? 100.0 ? 0.037 ? ? ? ? ? ? ? ? ? 
4.88 50.00 ? ? ? ? ? ? 3021 ? ? ? ? ? ? ? ? ? ? ? 9.4  0.869 ? ? 0.036 0.012 ? 20 1 0.999 1.000 ? 99.4  ? 0.034 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BVI 
_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                            1.787 
_refine.ls_d_res_low                             33.527 
_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                     56160 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.26 
_refine.ls_percent_reflns_R_free                 3.56 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1746 
_refine.ls_R_factor_R_free                       0.2021 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1736 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.27 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.20 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.787 
_refine_hist.d_res_low                        33.527 
_refine_hist.number_atoms_solvent             462 
_refine_hist.number_atoms_total               4399 
_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        3912 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_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' ? 0.006  ? 4090 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.974  ? 5531 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.903 ? 1615 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 596  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 716  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.787  1.8316 . . 128 3467 90.00  . . . . 0.2663 . . . . . . . . . . . 0.3015 
'X-RAY DIFFRACTION' 1.8316 1.8811 . . 142 3845 100.00 . . . . 0.2346 . . . . . . . . . . . 0.2561 
'X-RAY DIFFRACTION' 1.8811 1.9365 . . 141 3840 100.00 . . . . 0.2372 . . . . . . . . . . . 0.2956 
'X-RAY DIFFRACTION' 1.9365 1.9990 . . 141 3837 100.00 . . . . 0.2008 . . . . . . . . . . . 0.2401 
'X-RAY DIFFRACTION' 1.9990 2.0704 . . 144 3887 100.00 . . . . 0.1959 . . . . . . . . . . . 0.2451 
'X-RAY DIFFRACTION' 2.0704 2.1533 . . 141 3828 100.00 . . . . 0.1879 . . . . . . . . . . . 0.2188 
'X-RAY DIFFRACTION' 2.1533 2.2513 . . 143 3868 100.00 . . . . 0.1817 . . . . . . . . . . . 0.2208 
'X-RAY DIFFRACTION' 2.2513 2.3699 . . 144 3885 100.00 . . . . 0.1832 . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 2.3699 2.5184 . . 142 3854 100.00 . . . . 0.1812 . . . . . . . . . . . 0.2132 
'X-RAY DIFFRACTION' 2.5184 2.7127 . . 144 3910 100.00 . . . . 0.1800 . . . . . . . . . . . 0.2151 
'X-RAY DIFFRACTION' 2.7127 2.9856 . . 144 3914 100.00 . . . . 0.1866 . . . . . . . . . . . 0.2349 
'X-RAY DIFFRACTION' 2.9856 3.4172 . . 146 3927 100.00 . . . . 0.1831 . . . . . . . . . . . 0.1954 
'X-RAY DIFFRACTION' 3.4172 4.3039 . . 147 3982 100.00 . . . . 0.1541 . . . . . . . . . . . 0.1829 
'X-RAY DIFFRACTION' 4.3039 33.52  . . 152 4117 100.00 . . . . 0.1464 . . . . . . . . . . . 0.1593 
# 
_struct.entry_id                     9BVI 
_struct.title                        'Identification of multiple ligand hotspots on SOS2, compound 2' 
_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        9BVI 
_struct_keywords.text            
;small molecule complex crystal structure, SOS2, guanosine nucleotide exchange factor, RAS-activator, SIGNALING PROTEIN, oncogenes, inhibitor of SOS-mediated guanosine nucleotide exchange
;
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SOS2_HUMAN 
_struct_ref.pdbx_db_accession          Q07890 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EQPLRLPSPEVYRFVVKDSEENIVFEDNLQSRSGIPIIKGGTVVKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSL
LIERFEIPEPEPTDADKLAIEKGEQPISADLKRFRKEYVQPVQLRILNVFRHWVEHHFYDFERDLELLERLESFISSVRG
KAMKKWVESIAKIIRRKKQAQANGVSHNITFESPPPPIEWHISKPGQFETFDLMTLHPIEIARQLTLLESDLYRKVQPSE
LVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVEAENFEERVAVLSRIIEILQVFQDLNNFNGVLEIVSAVNSVSV
YRLDHTFEALQERKRKILDEAVELSQDHFKKYLVKLKSINPPCVPFFGIYLTNILKTEEGNNDFLKKKGKDLINFSKRRK
VAEITGEIQQYQNQPYCLRIEPDMRRFFENLNPMGSASEKEFTDYLFNKSLEIEPRNCKQPPRFPRKSTFSLKSPGIRPN
TGRHGS
;
_struct_ref.pdbx_align_begin           562 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BVI 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 29 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 514 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q07890 
_struct_ref_seq.db_align_beg                  562 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1047 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       566 
_struct_ref_seq.pdbx_auth_seq_align_end       1051 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BVI MET A 1  ? UNP Q07890 ? ? 'expression tag' -28 1  
1 9BVI SER A 2  ? UNP Q07890 ? ? 'expression tag' -27 2  
1 9BVI TYR A 3  ? UNP Q07890 ? ? 'expression tag' -26 3  
1 9BVI TYR A 4  ? UNP Q07890 ? ? 'expression tag' -25 4  
1 9BVI HIS A 5  ? UNP Q07890 ? ? 'expression tag' -24 5  
1 9BVI HIS A 6  ? UNP Q07890 ? ? 'expression tag' -23 6  
1 9BVI HIS A 7  ? UNP Q07890 ? ? 'expression tag' -22 7  
1 9BVI HIS A 8  ? UNP Q07890 ? ? 'expression tag' -21 8  
1 9BVI HIS A 9  ? UNP Q07890 ? ? 'expression tag' -20 9  
1 9BVI HIS A 10 ? UNP Q07890 ? ? 'expression tag' -19 10 
1 9BVI LEU A 11 ? UNP Q07890 ? ? 'expression tag' -18 11 
1 9BVI GLU A 12 ? UNP Q07890 ? ? 'expression tag' -17 12 
1 9BVI SER A 13 ? UNP Q07890 ? ? 'expression tag' -16 13 
1 9BVI THR A 14 ? UNP Q07890 ? ? 'expression tag' -15 14 
1 9BVI SER A 15 ? UNP Q07890 ? ? 'expression tag' -14 15 
1 9BVI LEU A 16 ? UNP Q07890 ? ? 'expression tag' -13 16 
1 9BVI TYR A 17 ? UNP Q07890 ? ? 'expression tag' -12 17 
1 9BVI LYS A 18 ? UNP Q07890 ? ? 'expression tag' -11 18 
1 9BVI LYS A 19 ? UNP Q07890 ? ? 'expression tag' -10 19 
1 9BVI ALA A 20 ? UNP Q07890 ? ? 'expression tag' -9  20 
1 9BVI GLY A 21 ? UNP Q07890 ? ? 'expression tag' -8  21 
1 9BVI PHE A 22 ? UNP Q07890 ? ? 'expression tag' -7  22 
1 9BVI GLU A 23 ? UNP Q07890 ? ? 'expression tag' -6  23 
1 9BVI ASN A 24 ? UNP Q07890 ? ? 'expression tag' -5  24 
1 9BVI LEU A 25 ? UNP Q07890 ? ? 'expression tag' -4  25 
1 9BVI TYR A 26 ? UNP Q07890 ? ? 'expression tag' -3  26 
1 9BVI PHE A 27 ? UNP Q07890 ? ? 'expression tag' -2  27 
1 9BVI GLN A 28 ? UNP Q07890 ? ? 'expression tag' -1  28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  25490 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TYR A 40  ? VAL A 44  ? TYR A 577  VAL A 581  5 ? 5  
HELX_P HELX_P2  AA2 THR A 70  ? THR A 79  ? THR A 607  THR A 616  1 ? 10 
HELX_P HELX_P3  AA3 ASP A 85  ? TYR A 96  ? ASP A 622  TYR A 633  1 ? 12 
HELX_P HELX_P4  AA4 ARG A 97  ? PHE A 99  ? ARG A 634  PHE A 636  5 ? 3  
HELX_P HELX_P5  AA5 LYS A 101 ? GLU A 114 ? LYS A 638  GLU A 651  1 ? 14 
HELX_P HELX_P6  AA6 THR A 121 ? GLY A 131 ? THR A 658  GLY A 668  1 ? 11 
HELX_P HELX_P7  AA7 SER A 136 ? TYR A 146 ? SER A 673  TYR A 683  1 ? 11 
HELX_P HELX_P8  AA8 TYR A 146 ? HIS A 165 ? TYR A 683  HIS A 702  1 ? 20 
HELX_P HELX_P9  AA9 PHE A 166 ? ASP A 172 ? PHE A 703  ASP A 709  1 ? 7  
HELX_P HELX_P10 AB1 ASP A 172 ? SER A 185 ? ASP A 709  SER A 722  1 ? 14 
HELX_P HELX_P11 AB2 GLY A 188 ? ALA A 208 ? GLY A 725  ALA A 745  1 ? 21 
HELX_P HELX_P12 AB3 GLN A 235 ? PHE A 239 ? GLN A 772  PHE A 776  5 ? 5  
HELX_P HELX_P13 AB4 HIS A 245 ? LYS A 263 ? HIS A 782  LYS A 800  1 ? 19 
HELX_P HELX_P14 AB5 GLN A 265 ? LYS A 276 ? GLN A 802  LYS A 813  5 ? 12 
HELX_P HELX_P15 AB6 ASP A 278 ? SER A 283 ? ASP A 815  SER A 820  1 ? 6  
HELX_P HELX_P16 AB7 SER A 283 ? GLU A 306 ? SER A 820  GLU A 843  1 ? 24 
HELX_P HELX_P17 AB8 ASN A 309 ? LEU A 330 ? ASN A 846  LEU A 867  1 ? 22 
HELX_P HELX_P18 AB9 ASN A 332 ? SER A 345 ? ASN A 869  SER A 882  1 ? 14 
HELX_P HELX_P19 AC1 SER A 345 ? ARG A 350 ? SER A 882  ARG A 887  1 ? 6  
HELX_P HELX_P20 AC2 LEU A 351 ? ALA A 357 ? LEU A 888  ALA A 894  1 ? 7  
HELX_P HELX_P21 AC3 GLN A 359 ? ILE A 387 ? GLN A 896  ILE A 924  1 ? 29 
HELX_P HELX_P22 AC4 PHE A 395 ? GLY A 408 ? PHE A 932  GLY A 945  1 ? 14 
HELX_P HELX_P23 AC5 PHE A 423 ? GLN A 438 ? PHE A 960  GLN A 975  1 ? 16 
HELX_P HELX_P24 AC6 GLU A 449 ? ASN A 458 ? GLU A 986  ASN A 995  1 ? 10 
HELX_P HELX_P25 AC7 SER A 466 ? GLU A 482 ? SER A 1003 GLU A 1019 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           389 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            926 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    390 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     927 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.35 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   4 
_struct_sheet.details          ? 
# 
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 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 51  ? PHE A 53  ? ILE A 588 PHE A 590 
AA1 2 ILE A 66  ? GLY A 69  ? ILE A 603 GLY A 606 
AA1 3 LEU A 420 ? ASN A 422 ? LEU A 957 ASN A 959 
AA1 4 PHE A 412 ? LEU A 413 ? PHE A 949 LEU A 950 
# 
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 VAL A 52  ? N VAL A 589 O GLY A 68  ? O GLY A 605 
AA1 2 3 N GLY A 69  ? N GLY A 606 O ILE A 421 ? O ILE A 958 
AA1 3 4 O LEU A 420 ? O LEU A 957 N LEU A 413 ? N LEU A 950 
# 
_pdbx_entry_details.entry_id                   9BVI 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 2111 ? ? O   A HOH 2388 ? ? 1.84 
2 1 O   A HOH 2372 ? ? O   A HOH 2463 ? ? 2.13 
3 1 OD1 A ASP 796  ? ? NH2 A ARG 799  ? B 2.16 
4 1 O   A HOH 2450 ? ? O   A HOH 2454 ? ? 2.16 
5 1 O   A HOH 2310 ? ? O   A HOH 2541 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     2112 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     2454 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              1.77 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              1028 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              1028 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              1028 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.80 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            3.50 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A -2  ? ? -171.31 133.28  
2 1 ASN A 587 ? ? -141.26 -12.53  
3 1 PHE A 636 ? ? -141.66 -1.39   
4 1 HIS A 766 ? ? -117.20 -109.81 
5 1 ASN A 978 ? ? -119.30 53.61   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -18.2605 -15.4974 -28.3819 0.2290 ? -0.0125 ? -0.0089 ? 0.2508 ? -0.0272 ? 0.2206 ? 0.0474 ? 
0.2038 ? 0.2744  ? 0.2917 ? 0.4108  ? 0.2906  ? -0.0370 ? 0.0952  ? -0.0368 ? -0.1570 ? 0.0435  ? 0.0646  ? -0.0482 ? 0.0523  ? 
-0.0000 ? 
2 'X-RAY DIFFRACTION' ? refined -21.0527 -17.6826 -16.3601 0.2256 ? -0.0230 ? 0.0008  ? 0.2051 ? -0.0219 ? 0.2172 ? 0.4506 ? 
0.1401 ? 0.1444  ? 1.4602 ? 0.4334  ? 1.7823  ? 0.0823  ? -0.0942 ? 0.0286  ? 0.1403  ? -0.0904 ? 0.1846  ? 0.1914  ? -0.1099 ? 
-0.0020 ? 
3 'X-RAY DIFFRACTION' ? refined -8.5753  -11.4022 0.0822   0.4292 ? -0.0972 ? 0.0229  ? 0.3827 ? -0.0466 ? 0.2576 ? 0.6536 ? 
0.2194 ? 0.7777  ? 0.5376 ? -0.1625 ? -0.0386 ? 0.1741  ? -0.4128 ? -0.1226 ? 0.1985  ? -0.1259 ? -0.0181 ? 0.1231  ? -0.0878 ? 
-0.0116 ? 
4 'X-RAY DIFFRACTION' ? refined 21.9291  8.4581   -4.8127  0.2030 ? -0.0156 ? -0.0167 ? 0.2014 ? -0.0039 ? 0.1971 ? 0.8668 ? 
0.7099 ? 0.0519  ? 1.3862 ? -0.0604 ? 0.7929  ? 0.0718  ? -0.0234 ? -0.0561 ? 0.0541  ? -0.1082 ? -0.0373 ? 0.0905  ? 0.0453  ? 
0.0003  ? 
5 'X-RAY DIFFRACTION' ? refined 22.9109  0.3481   -17.9841 0.3554 ? -0.0143 ? 0.0044  ? 0.2618 ? -0.0096 ? 0.3072 ? 0.2787 ? 
0.0812 ? -0.1944 ? 0.8647 ? -0.3255 ? 0.7707  ? -0.0126 ? 0.2635  ? -0.0897 ? -0.1771 ? 0.0590  ? -0.0745 ? 0.4602  ? -0.0134 ? 
0.0000  ? 
6 'X-RAY DIFFRACTION' ? refined -2.6049  -3.1735  -25.1886 0.2764 ? -0.0413 ? -0.0137 ? 0.3453 ? 0.0347  ? 0.3305 ? 0.2994 ? 
0.3765 ? -0.0000 ? 0.5373 ? 0.2211  ? 0.2481  ? -0.1152 ? 0.5833  ? 0.4377  ? -0.1228 ? -0.0182 ? -0.1356 ? -0.0560 ? 0.3588  ? 
0.0001  ? 
7 'X-RAY DIFFRACTION' ? refined 17.0997  4.8309   2.6394   0.3041 ? -0.0435 ? 0.0031  ? 0.3035 ? 0.0493  ? 0.2700 ? 0.6359 ? 
0.2098 ? -0.1281 ? 0.1909 ? 0.0923  ? 0.5152  ? 0.1068  ? -0.1691 ? -0.1665 ? 0.2653  ? 0.0617  ? 0.3918  ? 0.1238  ? -0.2917 ? 
-0.0004 ? 
8 'X-RAY DIFFRACTION' ? refined 32.2755  21.4282  -5.4539  0.2494 ? -0.0508 ? -0.0256 ? 0.2882 ? 0.0272  ? 0.2536 ? 0.6194 ? 
0.3381 ? -0.0862 ? 0.3077 ? 0.1897  ? 0.6593  ? 0.0955  ? 0.0399  ? -0.0562 ? 0.2115  ? -0.0890 ? -0.0544 ? -0.3460 ? 0.1948  ? 
-0.0000 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid -4 through 616 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 617 through 701 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 702 through 762 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 763 through 896 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 897 through 944 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 945 through 976 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 977 through 1003 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1004 through 1045 )
;
# 
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 -28  ? A MET 1   
2  1 Y 1 A SER -27  ? A SER 2   
3  1 Y 1 A TYR -26  ? A TYR 3   
4  1 Y 1 A TYR -25  ? A TYR 4   
5  1 Y 1 A HIS -24  ? A HIS 5   
6  1 Y 1 A HIS -23  ? A HIS 6   
7  1 Y 1 A HIS -22  ? A HIS 7   
8  1 Y 1 A HIS -21  ? A HIS 8   
9  1 Y 1 A HIS -20  ? A HIS 9   
10 1 Y 1 A HIS -19  ? A HIS 10  
11 1 Y 1 A LEU -18  ? A LEU 11  
12 1 Y 1 A GLU -17  ? A GLU 12  
13 1 Y 1 A SER -16  ? A SER 13  
14 1 Y 1 A THR -15  ? A THR 14  
15 1 Y 1 A SER -14  ? A SER 15  
16 1 Y 1 A LEU -13  ? A LEU 16  
17 1 Y 1 A TYR -12  ? A TYR 17  
18 1 Y 1 A LYS -11  ? A LYS 18  
19 1 Y 1 A LYS -10  ? A LYS 19  
20 1 Y 1 A ALA -9   ? A ALA 20  
21 1 Y 1 A GLY -8   ? A GLY 21  
22 1 Y 1 A PHE -7   ? A PHE 22  
23 1 Y 1 A GLU -6   ? A GLU 23  
24 1 Y 1 A ASN -5   ? A ASN 24  
25 1 Y 1 A ASN 593  ? A ASN 56  
26 1 Y 1 A LEU 594  ? A LEU 57  
27 1 Y 1 A GLN 595  ? A GLN 58  
28 1 Y 1 A SER 596  ? A SER 59  
29 1 Y 1 A ARG 597  ? A ARG 60  
30 1 Y 1 A SER 598  ? A SER 61  
31 1 Y 1 A GLN 746  ? A GLN 209 
32 1 Y 1 A ALA 747  ? A ALA 210 
33 1 Y 1 A ASN 748  ? A ASN 211 
34 1 Y 1 A GLY 749  ? A GLY 212 
35 1 Y 1 A VAL 750  ? A VAL 213 
36 1 Y 1 A SER 751  ? A SER 214 
37 1 Y 1 A HIS 752  ? A HIS 215 
38 1 Y 1 A ASN 753  ? A ASN 216 
39 1 Y 1 A THR 1046 ? A THR 509 
40 1 Y 1 A GLY 1047 ? A GLY 510 
41 1 Y 1 A ARG 1048 ? A ARG 511 
42 1 Y 1 A HIS 1049 ? A HIS 512 
43 1 Y 1 A GLY 1050 ? A GLY 513 
44 1 Y 1 A SER 1051 ? A SER 514 
# 
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 
A1ASW N1   N N N 1   
A1ASW N3   N Y N 2   
A1ASW C4   C N N 3   
A1ASW C5   C N N 4   
A1ASW C6   C Y N 5   
A1ASW C7   C Y N 6   
A1ASW C8   C Y N 7   
A1ASW C10  C Y N 8   
A1ASW C13  C Y N 9   
A1ASW C15  C Y N 10  
A1ASW C17  C Y N 11  
A1ASW C1   C N N 12  
A1ASW C2   C N N 13  
A1ASW C3   C N N 14  
A1ASW N2   N N N 15  
A1ASW N4   N N N 16  
A1ASW C9   C Y N 17  
A1ASW C11  C Y N 18  
A1ASW O1   O N N 19  
A1ASW C12  C Y N 20  
A1ASW N5   N Y N 21  
A1ASW C14  C Y N 22  
A1ASW C16  C Y N 23  
A1ASW C18  C Y N 24  
A1ASW C19  C Y N 25  
A1ASW H2   H N N 26  
A1ASW H3   H N N 27  
A1ASW H4   H N N 28  
A1ASW H5   H N N 29  
A1ASW H6   H N N 30  
A1ASW H7   H N N 31  
A1ASW H8   H N N 32  
A1ASW H9   H N N 33  
A1ASW H10  H N N 34  
A1ASW H11  H N N 35  
A1ASW H12  H N N 36  
A1ASW H13  H N N 37  
A1ASW H14  H N N 38  
A1ASW H15  H N N 39  
A1ASW H16  H N N 40  
A1ASW H17  H N N 41  
A1ASW H18  H N N 42  
A1ASW H19  H N N 43  
A1ASW H20  H N N 44  
A1ASW H21  H N N 45  
A1ASW H22  H N N 46  
ALA   N    N N N 47  
ALA   CA   C N S 48  
ALA   C    C N N 49  
ALA   O    O N N 50  
ALA   CB   C N N 51  
ALA   OXT  O N N 52  
ALA   H    H N N 53  
ALA   H2   H N N 54  
ALA   HA   H N N 55  
ALA   HB1  H N N 56  
ALA   HB2  H N N 57  
ALA   HB3  H N N 58  
ALA   HXT  H N N 59  
ARG   N    N N N 60  
ARG   CA   C N S 61  
ARG   C    C N N 62  
ARG   O    O N N 63  
ARG   CB   C N N 64  
ARG   CG   C N N 65  
ARG   CD   C N N 66  
ARG   NE   N N N 67  
ARG   CZ   C N N 68  
ARG   NH1  N N N 69  
ARG   NH2  N N N 70  
ARG   OXT  O N N 71  
ARG   H    H N N 72  
ARG   H2   H N N 73  
ARG   HA   H N N 74  
ARG   HB2  H N N 75  
ARG   HB3  H N N 76  
ARG   HG2  H N N 77  
ARG   HG3  H N N 78  
ARG   HD2  H N N 79  
ARG   HD3  H N N 80  
ARG   HE   H N N 81  
ARG   HH11 H N N 82  
ARG   HH12 H N N 83  
ARG   HH21 H N N 84  
ARG   HH22 H N N 85  
ARG   HXT  H N N 86  
ASN   N    N N N 87  
ASN   CA   C N S 88  
ASN   C    C N N 89  
ASN   O    O N N 90  
ASN   CB   C N N 91  
ASN   CG   C N N 92  
ASN   OD1  O N N 93  
ASN   ND2  N N N 94  
ASN   OXT  O N N 95  
ASN   H    H N N 96  
ASN   H2   H N N 97  
ASN   HA   H N N 98  
ASN   HB2  H N N 99  
ASN   HB3  H N N 100 
ASN   HD21 H N N 101 
ASN   HD22 H N N 102 
ASN   HXT  H N N 103 
ASP   N    N N N 104 
ASP   CA   C N S 105 
ASP   C    C N N 106 
ASP   O    O N N 107 
ASP   CB   C N N 108 
ASP   CG   C N N 109 
ASP   OD1  O N N 110 
ASP   OD2  O N N 111 
ASP   OXT  O N N 112 
ASP   H    H N N 113 
ASP   H2   H N N 114 
ASP   HA   H N N 115 
ASP   HB2  H N N 116 
ASP   HB3  H N N 117 
ASP   HD2  H N N 118 
ASP   HXT  H N N 119 
CYS   N    N N N 120 
CYS   CA   C N R 121 
CYS   C    C N N 122 
CYS   O    O N N 123 
CYS   CB   C N N 124 
CYS   SG   S N N 125 
CYS   OXT  O N N 126 
CYS   H    H N N 127 
CYS   H2   H N N 128 
CYS   HA   H N N 129 
CYS   HB2  H N N 130 
CYS   HB3  H N N 131 
CYS   HG   H N N 132 
CYS   HXT  H N N 133 
GLN   N    N N N 134 
GLN   CA   C N S 135 
GLN   C    C N N 136 
GLN   O    O N N 137 
GLN   CB   C N N 138 
GLN   CG   C N N 139 
GLN   CD   C N N 140 
GLN   OE1  O N N 141 
GLN   NE2  N N N 142 
GLN   OXT  O N N 143 
GLN   H    H N N 144 
GLN   H2   H N N 145 
GLN   HA   H N N 146 
GLN   HB2  H N N 147 
GLN   HB3  H N N 148 
GLN   HG2  H N N 149 
GLN   HG3  H N N 150 
GLN   HE21 H N N 151 
GLN   HE22 H N N 152 
GLN   HXT  H N N 153 
GLU   N    N N N 154 
GLU   CA   C N S 155 
GLU   C    C N N 156 
GLU   O    O N N 157 
GLU   CB   C N N 158 
GLU   CG   C N N 159 
GLU   CD   C N N 160 
GLU   OE1  O N N 161 
GLU   OE2  O N N 162 
GLU   OXT  O N N 163 
GLU   H    H N N 164 
GLU   H2   H N N 165 
GLU   HA   H N N 166 
GLU   HB2  H N N 167 
GLU   HB3  H N N 168 
GLU   HG2  H N N 169 
GLU   HG3  H N N 170 
GLU   HE2  H N N 171 
GLU   HXT  H N N 172 
GLY   N    N N N 173 
GLY   CA   C N N 174 
GLY   C    C N N 175 
GLY   O    O N N 176 
GLY   OXT  O N N 177 
GLY   H    H N N 178 
GLY   H2   H N N 179 
GLY   HA2  H N N 180 
GLY   HA3  H N N 181 
GLY   HXT  H N N 182 
HIS   N    N N N 183 
HIS   CA   C N S 184 
HIS   C    C N N 185 
HIS   O    O N N 186 
HIS   CB   C N N 187 
HIS   CG   C Y N 188 
HIS   ND1  N Y N 189 
HIS   CD2  C Y N 190 
HIS   CE1  C Y N 191 
HIS   NE2  N Y N 192 
HIS   OXT  O N N 193 
HIS   H    H N N 194 
HIS   H2   H N N 195 
HIS   HA   H N N 196 
HIS   HB2  H N N 197 
HIS   HB3  H N N 198 
HIS   HD1  H N N 199 
HIS   HD2  H N N 200 
HIS   HE1  H N N 201 
HIS   HE2  H N N 202 
HIS   HXT  H N N 203 
HOH   O    O N N 204 
HOH   H1   H N N 205 
HOH   H2   H N N 206 
ILE   N    N N N 207 
ILE   CA   C N S 208 
ILE   C    C N N 209 
ILE   O    O N N 210 
ILE   CB   C N S 211 
ILE   CG1  C N N 212 
ILE   CG2  C N N 213 
ILE   CD1  C N N 214 
ILE   OXT  O N N 215 
ILE   H    H N N 216 
ILE   H2   H N N 217 
ILE   HA   H N N 218 
ILE   HB   H N N 219 
ILE   HG12 H N N 220 
ILE   HG13 H N N 221 
ILE   HG21 H N N 222 
ILE   HG22 H N N 223 
ILE   HG23 H N N 224 
ILE   HD11 H N N 225 
ILE   HD12 H N N 226 
ILE   HD13 H N N 227 
ILE   HXT  H N N 228 
LEU   N    N N N 229 
LEU   CA   C N S 230 
LEU   C    C N N 231 
LEU   O    O N N 232 
LEU   CB   C N N 233 
LEU   CG   C N N 234 
LEU   CD1  C N N 235 
LEU   CD2  C N N 236 
LEU   OXT  O N N 237 
LEU   H    H N N 238 
LEU   H2   H N N 239 
LEU   HA   H N N 240 
LEU   HB2  H N N 241 
LEU   HB3  H N N 242 
LEU   HG   H N N 243 
LEU   HD11 H N N 244 
LEU   HD12 H N N 245 
LEU   HD13 H N N 246 
LEU   HD21 H N N 247 
LEU   HD22 H N N 248 
LEU   HD23 H N N 249 
LEU   HXT  H N N 250 
LYS   N    N N N 251 
LYS   CA   C N S 252 
LYS   C    C N N 253 
LYS   O    O N N 254 
LYS   CB   C N N 255 
LYS   CG   C N N 256 
LYS   CD   C N N 257 
LYS   CE   C N N 258 
LYS   NZ   N N N 259 
LYS   OXT  O N N 260 
LYS   H    H N N 261 
LYS   H2   H N N 262 
LYS   HA   H N N 263 
LYS   HB2  H N N 264 
LYS   HB3  H N N 265 
LYS   HG2  H N N 266 
LYS   HG3  H N N 267 
LYS   HD2  H N N 268 
LYS   HD3  H N N 269 
LYS   HE2  H N N 270 
LYS   HE3  H N N 271 
LYS   HZ1  H N N 272 
LYS   HZ2  H N N 273 
LYS   HZ3  H N N 274 
LYS   HXT  H N N 275 
MET   N    N N N 276 
MET   CA   C N S 277 
MET   C    C N N 278 
MET   O    O N N 279 
MET   CB   C N N 280 
MET   CG   C N N 281 
MET   SD   S N N 282 
MET   CE   C N N 283 
MET   OXT  O N N 284 
MET   H    H N N 285 
MET   H2   H N N 286 
MET   HA   H N N 287 
MET   HB2  H N N 288 
MET   HB3  H N N 289 
MET   HG2  H N N 290 
MET   HG3  H N N 291 
MET   HE1  H N N 292 
MET   HE2  H N N 293 
MET   HE3  H N N 294 
MET   HXT  H N N 295 
PHE   N    N N N 296 
PHE   CA   C N S 297 
PHE   C    C N N 298 
PHE   O    O N N 299 
PHE   CB   C N N 300 
PHE   CG   C Y N 301 
PHE   CD1  C Y N 302 
PHE   CD2  C Y N 303 
PHE   CE1  C Y N 304 
PHE   CE2  C Y N 305 
PHE   CZ   C Y N 306 
PHE   OXT  O N N 307 
PHE   H    H N N 308 
PHE   H2   H N N 309 
PHE   HA   H N N 310 
PHE   HB2  H N N 311 
PHE   HB3  H N N 312 
PHE   HD1  H N N 313 
PHE   HD2  H N N 314 
PHE   HE1  H N N 315 
PHE   HE2  H N N 316 
PHE   HZ   H N N 317 
PHE   HXT  H N N 318 
PRO   N    N N N 319 
PRO   CA   C N S 320 
PRO   C    C N N 321 
PRO   O    O N N 322 
PRO   CB   C N N 323 
PRO   CG   C N N 324 
PRO   CD   C N N 325 
PRO   OXT  O N N 326 
PRO   H    H N N 327 
PRO   HA   H N N 328 
PRO   HB2  H N N 329 
PRO   HB3  H N N 330 
PRO   HG2  H N N 331 
PRO   HG3  H N N 332 
PRO   HD2  H N N 333 
PRO   HD3  H N N 334 
PRO   HXT  H N N 335 
SER   N    N N N 336 
SER   CA   C N S 337 
SER   C    C N N 338 
SER   O    O N N 339 
SER   CB   C N N 340 
SER   OG   O N N 341 
SER   OXT  O N N 342 
SER   H    H N N 343 
SER   H2   H N N 344 
SER   HA   H N N 345 
SER   HB2  H N N 346 
SER   HB3  H N N 347 
SER   HG   H N N 348 
SER   HXT  H N N 349 
THR   N    N N N 350 
THR   CA   C N S 351 
THR   C    C N N 352 
THR   O    O N N 353 
THR   CB   C N R 354 
THR   OG1  O N N 355 
THR   CG2  C N N 356 
THR   OXT  O N N 357 
THR   H    H N N 358 
THR   H2   H N N 359 
THR   HA   H N N 360 
THR   HB   H N N 361 
THR   HG1  H N N 362 
THR   HG21 H N N 363 
THR   HG22 H N N 364 
THR   HG23 H N N 365 
THR   HXT  H N N 366 
TRP   N    N N N 367 
TRP   CA   C N S 368 
TRP   C    C N N 369 
TRP   O    O N N 370 
TRP   CB   C N N 371 
TRP   CG   C Y N 372 
TRP   CD1  C Y N 373 
TRP   CD2  C Y N 374 
TRP   NE1  N Y N 375 
TRP   CE2  C Y N 376 
TRP   CE3  C Y N 377 
TRP   CZ2  C Y N 378 
TRP   CZ3  C Y N 379 
TRP   CH2  C Y N 380 
TRP   OXT  O N N 381 
TRP   H    H N N 382 
TRP   H2   H N N 383 
TRP   HA   H N N 384 
TRP   HB2  H N N 385 
TRP   HB3  H N N 386 
TRP   HD1  H N N 387 
TRP   HE1  H N N 388 
TRP   HE3  H N N 389 
TRP   HZ2  H N N 390 
TRP   HZ3  H N N 391 
TRP   HH2  H N N 392 
TRP   HXT  H N N 393 
TYR   N    N N N 394 
TYR   CA   C N S 395 
TYR   C    C N N 396 
TYR   O    O N N 397 
TYR   CB   C N N 398 
TYR   CG   C Y N 399 
TYR   CD1  C Y N 400 
TYR   CD2  C Y N 401 
TYR   CE1  C Y N 402 
TYR   CE2  C Y N 403 
TYR   CZ   C Y N 404 
TYR   OH   O N N 405 
TYR   OXT  O N N 406 
TYR   H    H N N 407 
TYR   H2   H N N 408 
TYR   HA   H N N 409 
TYR   HB2  H N N 410 
TYR   HB3  H N N 411 
TYR   HD1  H N N 412 
TYR   HD2  H N N 413 
TYR   HE1  H N N 414 
TYR   HE2  H N N 415 
TYR   HH   H N N 416 
TYR   HXT  H N N 417 
VAL   N    N N N 418 
VAL   CA   C N S 419 
VAL   C    C N N 420 
VAL   O    O N N 421 
VAL   CB   C N N 422 
VAL   CG1  C N N 423 
VAL   CG2  C N N 424 
VAL   OXT  O N N 425 
VAL   H    H N N 426 
VAL   H2   H N N 427 
VAL   HA   H N N 428 
VAL   HB   H N N 429 
VAL   HG11 H N N 430 
VAL   HG12 H N N 431 
VAL   HG13 H N N 432 
VAL   HG21 H N N 433 
VAL   HG22 H N N 434 
VAL   HG23 H N N 435 
VAL   HXT  H N N 436 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1ASW C1  N1   sing N N 1   
A1ASW C5  N1   sing N N 2   
A1ASW C5  C4   sing N N 3   
A1ASW N1  C2   sing N N 4   
A1ASW C2  C3   sing N N 5   
A1ASW C10 C9   doub Y N 6   
A1ASW C10 C11  sing Y N 7   
A1ASW C9  C8   sing Y N 8   
A1ASW C4  N2   sing N N 9   
A1ASW O1  C11  sing N N 10  
A1ASW C11 C12  doub Y N 11  
A1ASW C8  N4   sing N N 12  
A1ASW C8  C13  doub Y N 13  
A1ASW N2  C3   sing N N 14  
A1ASW N2  C6   sing N N 15  
A1ASW N3  C6   doub Y N 16  
A1ASW N3  C7   sing Y N 17  
A1ASW N4  C7   sing N N 18  
A1ASW C6  C19  sing Y N 19  
A1ASW C7  N5   doub Y N 20  
A1ASW C12 C13  sing Y N 21  
A1ASW N5  C14  sing Y N 22  
A1ASW C19 C14  doub Y N 23  
A1ASW C19 C18  sing Y N 24  
A1ASW C14 C15  sing Y N 25  
A1ASW C18 C17  doub Y N 26  
A1ASW C15 C16  doub Y N 27  
A1ASW C17 C16  sing Y N 28  
A1ASW C4  H2   sing N N 29  
A1ASW C4  H3   sing N N 30  
A1ASW C5  H4   sing N N 31  
A1ASW C5  H5   sing N N 32  
A1ASW C10 H6   sing N N 33  
A1ASW C13 H7   sing N N 34  
A1ASW C15 H8   sing N N 35  
A1ASW C17 H9   sing N N 36  
A1ASW C1  H10  sing N N 37  
A1ASW C1  H11  sing N N 38  
A1ASW C1  H12  sing N N 39  
A1ASW C2  H13  sing N N 40  
A1ASW C2  H14  sing N N 41  
A1ASW C3  H15  sing N N 42  
A1ASW C3  H16  sing N N 43  
A1ASW N4  H17  sing N N 44  
A1ASW C9  H18  sing N N 45  
A1ASW O1  H19  sing N N 46  
A1ASW C12 H20  sing N N 47  
A1ASW C16 H21  sing N N 48  
A1ASW C18 H22  sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   'Lustgarten Foundation' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'SOS1 homology model' 
# 
_atom_sites.entry_id                    9BVI 
_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]   0.015622 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011576 
_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]   0.009401 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU   A 1 25  ? -14.739 -30.595 -34.524 1.00 55.77  ? -4   LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 25  ? -13.568 -30.790 -35.378 1.00 54.01  ? -4   LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 25  ? -13.894 -31.660 -36.595 1.00 47.17  ? -4   LEU   A C   1 
ATOM   4    O O   . LEU   A 1 25  ? -13.815 -31.204 -37.733 1.00 53.05  ? -4   LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 25  ? -12.419 -31.411 -34.581 1.00 64.46  ? -4   LEU   A CB  1 
ATOM   6    C CG  . LEU   A 1 25  ? -11.051 -30.735 -34.733 1.00 65.14  ? -4   LEU   A CG  1 
ATOM   7    C CD1 . LEU   A 1 25  ? -10.729 -30.438 -36.197 1.00 62.05  ? -4   LEU   A CD1 1 
ATOM   8    C CD2 . LEU   A 1 25  ? -10.985 -29.465 -33.897 1.00 70.51  ? -4   LEU   A CD2 1 
ATOM   9    N N   . TYR   A 1 26  ? -14.272 -32.909 -36.350 1.00 40.42  ? -3   TYR   A N   1 
ATOM   10   C CA  . TYR   A 1 26  ? -14.609 -33.834 -37.428 1.00 34.94  ? -3   TYR   A CA  1 
ATOM   11   C C   . TYR   A 1 26  ? -16.104 -34.175 -37.439 1.00 29.32  ? -3   TYR   A C   1 
ATOM   12   O O   . TYR   A 1 26  ? -16.537 -35.095 -38.130 1.00 30.54  ? -3   TYR   A O   1 
ATOM   13   C CB  . TYR   A 1 26  ? -13.759 -35.102 -37.297 1.00 40.91  ? -3   TYR   A CB  1 
ATOM   14   C CG  . TYR   A 1 26  ? -12.283 -34.778 -37.175 1.00 40.61  ? -3   TYR   A CG  1 
ATOM   15   C CD1 . TYR   A 1 26  ? -11.587 -34.240 -38.250 1.00 39.10  ? -3   TYR   A CD1 1 
ATOM   16   C CD2 . TYR   A 1 26  ? -11.594 -34.984 -35.984 1.00 44.46  ? -3   TYR   A CD2 1 
ATOM   17   C CE1 . TYR   A 1 26  ? -10.245 -33.922 -38.149 1.00 44.96  ? -3   TYR   A CE1 1 
ATOM   18   C CE2 . TYR   A 1 26  ? -10.247 -34.669 -35.874 1.00 43.10  ? -3   TYR   A CE2 1 
ATOM   19   C CZ  . TYR   A 1 26  ? -9.579  -34.136 -36.962 1.00 46.64  ? -3   TYR   A CZ  1 
ATOM   20   O OH  . TYR   A 1 26  ? -8.236  -33.813 -36.882 1.00 47.07  ? -3   TYR   A OH  1 
ATOM   21   N N   . PHE   A 1 27  ? -16.875 -33.413 -36.665 1.00 28.57  ? -2   PHE   A N   1 
ATOM   22   C CA  . PHE   A 1 27  ? -18.327 -33.578 -36.577 1.00 29.86  ? -2   PHE   A CA  1 
ATOM   23   C C   . PHE   A 1 27  ? -18.866 -32.400 -35.775 1.00 28.75  ? -2   PHE   A C   1 
ATOM   24   O O   . PHE   A 1 27  ? -18.303 -32.061 -34.738 1.00 27.79  ? -2   PHE   A O   1 
ATOM   25   C CB  . PHE   A 1 27  ? -18.681 -34.917 -35.914 1.00 29.73  ? -2   PHE   A CB  1 
ATOM   26   C CG  . PHE   A 1 27  ? -20.139 -35.082 -35.595 1.00 30.02  ? -2   PHE   A CG  1 
ATOM   27   C CD1 . PHE   A 1 27  ? -21.032 -35.526 -36.563 1.00 27.66  ? -2   PHE   A CD1 1 
ATOM   28   C CD2 . PHE   A 1 27  ? -20.617 -34.815 -34.323 1.00 32.67  ? -2   PHE   A CD2 1 
ATOM   29   C CE1 . PHE   A 1 27  ? -22.377 -35.698 -36.269 1.00 25.92  ? -2   PHE   A CE1 1 
ATOM   30   C CE2 . PHE   A 1 27  ? -21.972 -34.983 -34.023 1.00 30.55  ? -2   PHE   A CE2 1 
ATOM   31   C CZ  . PHE   A 1 27  ? -22.847 -35.426 -35.001 1.00 25.75  ? -2   PHE   A CZ  1 
ATOM   32   N N   . GLN   A 1 28  ? -19.932 -31.755 -36.250 1.00 23.61  ? -1   GLN   A N   1 
ATOM   33   C CA  . GLN   A 1 28  ? -20.490 -30.629 -35.502 1.00 21.04  ? -1   GLN   A CA  1 
ATOM   34   C C   . GLN   A 1 28  ? -21.580 -31.145 -34.581 1.00 24.73  ? -1   GLN   A C   1 
ATOM   35   O O   . GLN   A 1 28  ? -22.526 -31.811 -35.017 1.00 24.85  ? -1   GLN   A O   1 
ATOM   36   C CB  . GLN   A 1 28  ? -21.031 -29.541 -36.438 1.00 22.36  ? -1   GLN   A CB  1 
ATOM   37   C CG  . GLN   A 1 28  ? -19.926 -28.897 -37.283 1.00 26.60  ? -1   GLN   A CG  1 
ATOM   38   C CD  . GLN   A 1 28  ? -20.454 -28.069 -38.439 1.00 28.51  ? -1   GLN   A CD  1 
ATOM   39   O OE1 . GLN   A 1 28  ? -20.472 -26.830 -38.381 1.00 29.63  ? -1   GLN   A OE1 1 
ATOM   40   N NE2 . GLN   A 1 28  ? -20.888 -28.742 -39.502 1.00 26.00  ? -1   GLN   A NE2 1 
ATOM   41   N N   . GLU   A 1 29  ? -21.408 -30.865 -33.294 1.00 27.28  ? 566  GLU   A N   1 
ATOM   42   C CA  . GLU   A 1 29  ? -22.365 -31.274 -32.279 1.00 28.79  ? 566  GLU   A CA  1 
ATOM   43   C C   . GLU   A 1 29  ? -23.521 -30.281 -32.211 1.00 25.84  ? 566  GLU   A C   1 
ATOM   44   O O   . GLU   A 1 29  ? -23.413 -29.160 -32.688 1.00 26.73  ? 566  GLU   A O   1 
ATOM   45   C CB  . GLU   A 1 29  ? -21.681 -31.383 -30.909 1.00 28.47  ? 566  GLU   A CB  1 
ATOM   46   C CG  . GLU   A 1 29  ? -20.636 -32.477 -30.866 1.00 33.82  ? 566  GLU   A CG  1 
ATOM   47   C CD  . GLU   A 1 29  ? -19.932 -32.571 -29.518 1.00 57.05  ? 566  GLU   A CD  1 
ATOM   48   O OE1 . GLU   A 1 29  ? -20.119 -31.660 -28.679 1.00 62.07  ? 566  GLU   A OE1 1 
ATOM   49   O OE2 . GLU   A 1 29  ? -19.189 -33.558 -29.306 1.00 58.74  ? 566  GLU   A OE2 1 
ATOM   50   N N   . GLN   A 1 30  ? -24.613 -30.720 -31.597 1.00 26.57  ? 567  GLN   A N   1 
ATOM   51   C CA  . GLN   A 1 30  ? -25.791 -29.897 -31.395 1.00 27.25  ? 567  GLN   A CA  1 
ATOM   52   C C   . GLN   A 1 30  ? -25.432 -28.642 -30.595 1.00 23.11  ? 567  GLN   A C   1 
ATOM   53   O O   . GLN   A 1 30  ? -24.790 -28.739 -29.547 1.00 26.87  ? 567  GLN   A O   1 
ATOM   54   C CB  . GLN   A 1 30  ? -26.869 -30.719 -30.662 1.00 30.56  ? 567  GLN   A CB  1 
ATOM   55   C CG  . GLN   A 1 30  ? -28.189 -29.995 -30.479 1.00 31.85  ? 567  GLN   A CG  1 
ATOM   56   C CD  . GLN   A 1 30  ? -29.035 -30.554 -29.336 1.00 47.26  ? 567  GLN   A CD  1 
ATOM   57   O OE1 . GLN   A 1 30  ? -28.511 -31.017 -28.315 1.00 43.71  ? 567  GLN   A OE1 1 
ATOM   58   N NE2 . GLN   A 1 30  ? -30.350 -30.490 -29.497 1.00 43.32  ? 567  GLN   A NE2 1 
ATOM   59   N N   . PRO   A 1 31  ? -25.843 -27.459 -31.079 1.00 22.44  ? 568  PRO   A N   1 
ATOM   60   C CA  . PRO   A 1 31  ? -25.636 -26.209 -30.342 1.00 21.94  ? 568  PRO   A CA  1 
ATOM   61   C C   . PRO   A 1 31  ? -26.354 -26.181 -28.991 1.00 24.36  ? 568  PRO   A C   1 
ATOM   62   O O   . PRO   A 1 31  ? -27.414 -26.791 -28.873 1.00 23.62  ? 568  PRO   A O   1 
ATOM   63   C CB  . PRO   A 1 31  ? -26.235 -25.148 -31.279 1.00 23.76  ? 568  PRO   A CB  1 
ATOM   64   C CG  . PRO   A 1 31  ? -26.225 -25.774 -32.624 1.00 28.49  ? 568  PRO   A CG  1 
ATOM   65   C CD  . PRO   A 1 31  ? -26.507 -27.222 -32.374 1.00 25.06  ? 568  PRO   A CD  1 
ATOM   66   N N   . LEU   A 1 32  ? -25.790 -25.486 -28.002 1.00 22.28  ? 569  LEU   A N   1 
ATOM   67   C CA  . LEU   A 1 32  ? -26.520 -25.181 -26.758 1.00 23.05  ? 569  LEU   A CA  1 
ATOM   68   C C   . LEU   A 1 32  ? -27.701 -24.260 -27.036 1.00 29.75  ? 569  LEU   A C   1 
ATOM   69   O O   . LEU   A 1 32  ? -27.644 -23.414 -27.925 1.00 28.47  ? 569  LEU   A O   1 
ATOM   70   C CB  . LEU   A 1 32  ? -25.596 -24.497 -25.752 1.00 27.42  ? 569  LEU   A CB  1 
ATOM   71   C CG  . LEU   A 1 32  ? -24.879 -25.196 -24.601 1.00 40.77  ? 569  LEU   A CG  1 
ATOM   72   C CD1 . LEU   A 1 32  ? -24.884 -26.689 -24.712 1.00 34.49  ? 569  LEU   A CD1 1 
ATOM   73   C CD2 . LEU   A 1 32  ? -23.455 -24.651 -24.462 1.00 33.86  ? 569  LEU   A CD2 1 
ATOM   74   N N   . ARG   A 1 33  ? -28.765 -24.403 -26.258 1.00 25.55  ? 570  ARG   A N   1 
ATOM   75   C CA  . ARG   A 1 33  ? -29.884 -23.488 -26.340 1.00 23.43  ? 570  ARG   A CA  1 
ATOM   76   C C   . ARG   A 1 33  ? -29.697 -22.407 -25.268 1.00 31.09  ? 570  ARG   A C   1 
ATOM   77   O O   . ARG   A 1 33  ? -29.752 -22.705 -24.075 1.00 27.08  ? 570  ARG   A O   1 
ATOM   78   C CB  . ARG   A 1 33  ? -31.208 -24.225 -26.141 1.00 25.93  ? 570  ARG   A CB  1 
ATOM   79   C CG  . ARG   A 1 33  ? -32.414 -23.331 -26.339 1.00 29.35  ? 570  ARG   A CG  1 
ATOM   80   C CD  . ARG   A 1 33  ? -33.731 -24.069 -26.145 1.00 29.46  ? 570  ARG   A CD  1 
ATOM   81   N NE  . ARG   A 1 33  ? -34.830 -23.165 -26.447 1.00 37.09  ? 570  ARG   A NE  1 
ATOM   82   C CZ  . ARG   A 1 33  ? -35.735 -22.750 -25.569 1.00 39.95  ? 570  ARG   A CZ  1 
ATOM   83   N NH1 . ARG   A 1 33  ? -35.714 -23.188 -24.315 1.00 30.83  ? 570  ARG   A NH1 1 
ATOM   84   N NH2 . ARG   A 1 33  ? -36.687 -21.912 -25.960 1.00 40.57  ? 570  ARG   A NH2 1 
ATOM   85   N N   . LEU   A 1 34  ? -29.461 -21.169 -25.707 1.00 27.01  ? 571  LEU   A N   1 
ATOM   86   C CA  . LEU   A 1 34  ? -29.112 -20.047 -24.828 1.00 25.60  ? 571  LEU   A CA  1 
ATOM   87   C C   . LEU   A 1 34  ? -30.265 -19.082 -24.658 1.00 25.44  ? 571  LEU   A C   1 
ATOM   88   O O   . LEU   A 1 34  ? -31.152 -19.033 -25.513 1.00 29.11  ? 571  LEU   A O   1 
ATOM   89   C CB  . LEU   A 1 34  ? -27.904 -19.276 -25.397 1.00 25.11  ? 571  LEU   A CB  1 
ATOM   90   C CG  . LEU   A 1 34  ? -26.660 -20.109 -25.663 1.00 28.31  ? 571  LEU   A CG  1 
ATOM   91   C CD1 . LEU   A 1 34  ? -25.552 -19.246 -26.275 1.00 43.73  ? 571  LEU   A CD1 1 
ATOM   92   C CD2 . LEU   A 1 34  ? -26.186 -20.774 -24.383 1.00 29.83  ? 571  LEU   A CD2 1 
ATOM   93   N N   . PRO   A 1 35  ? -30.249 -18.287 -23.565 1.00 22.98  ? 572  PRO   A N   1 
ATOM   94   C CA  . PRO   A 1 35  ? -31.219 -17.193 -23.443 1.00 25.76  ? 572  PRO   A CA  1 
ATOM   95   C C   . PRO   A 1 35  ? -31.015 -16.164 -24.557 1.00 29.12  ? 572  PRO   A C   1 
ATOM   96   O O   . PRO   A 1 35  ? -29.947 -16.161 -25.186 1.00 27.34  ? 572  PRO   A O   1 
ATOM   97   C CB  . PRO   A 1 35  ? -30.896 -16.572 -22.084 1.00 27.62  ? 572  PRO   A CB  1 
ATOM   98   C CG  . PRO   A 1 35  ? -29.428 -16.892 -21.850 1.00 25.41  ? 572  PRO   A CG  1 
ATOM   99   C CD  . PRO   A 1 35  ? -29.251 -18.278 -22.475 1.00 21.73  ? 572  PRO   A CD  1 
ATOM   100  N N   . SER   A 1 36  ? -31.995 -15.297 -24.799 1.00 29.15  ? 573  SER   A N   1 
ATOM   101  C CA  . SER   A 1 36  ? -31.845 -14.296 -25.854 1.00 25.82  ? 573  SER   A CA  1 
ATOM   102  C C   . SER   A 1 36  ? -30.880 -13.188 -25.430 1.00 27.88  ? 573  SER   A C   1 
ATOM   103  O O   . SER   A 1 36  ? -30.725 -12.904 -24.236 1.00 30.15  ? 573  SER   A O   1 
ATOM   104  C CB  . SER   A 1 36  ? -33.189 -13.679 -26.224 1.00 29.87  ? 573  SER   A CB  1 
ATOM   105  O OG  . SER   A 1 36  ? -33.526 -12.672 -25.290 1.00 38.42  ? 573  SER   A OG  1 
ATOM   106  N N   . PRO   A 1 37  ? -30.219 -12.565 -26.410 1.00 28.27  ? 574  PRO   A N   1 
ATOM   107  C CA  . PRO   A 1 37  ? -29.289 -11.477 -26.101 1.00 34.02  ? 574  PRO   A CA  1 
ATOM   108  C C   . PRO   A 1 37  ? -30.000 -10.268 -25.505 1.00 40.22  ? 574  PRO   A C   1 
ATOM   109  O O   . PRO   A 1 37  ? -29.346 -9.446  -24.872 1.00 32.46  ? 574  PRO   A O   1 
ATOM   110  C CB  . PRO   A 1 37  ? -28.669 -11.143 -27.462 1.00 33.93  ? 574  PRO   A CB  1 
ATOM   111  C CG  . PRO   A 1 37  ? -29.610 -11.719 -28.476 1.00 36.05  ? 574  PRO   A CG  1 
ATOM   112  C CD  . PRO   A 1 37  ? -30.171 -12.944 -27.831 1.00 30.00  ? 574  PRO   A CD  1 
ATOM   113  N N   . GLU   A 1 38  ? -31.318 -10.178 -25.685 1.00 34.86  ? 575  GLU   A N   1 
ATOM   114  C CA  . GLU   A 1 38  ? -32.085 -9.073  -25.117 1.00 37.54  ? 575  GLU   A CA  1 
ATOM   115  C C   . GLU   A 1 38  ? -32.204 -9.183  -23.599 1.00 38.49  ? 575  GLU   A C   1 
ATOM   116  O O   . GLU   A 1 38  ? -32.432 -8.183  -22.921 1.00 41.27  ? 575  GLU   A O   1 
ATOM   117  C CB  . GLU   A 1 38  ? -33.487 -8.998  -25.736 1.00 38.36  ? 575  GLU   A CB  1 
ATOM   118  C CG  . GLU   A 1 38  ? -33.521 -8.408  -27.141 1.00 37.03  ? 575  GLU   A CG  1 
ATOM   119  C CD  . GLU   A 1 38  ? -33.050 -9.390  -28.203 1.00 48.13  ? 575  GLU   A CD  1 
ATOM   120  O OE1 . GLU   A 1 38  ? -33.196 -10.619 -28.006 1.00 39.89  ? 575  GLU   A OE1 1 
ATOM   121  O OE2 . GLU   A 1 38  ? -32.527 -8.928  -29.234 1.00 47.56  ? 575  GLU   A OE2 1 
ATOM   122  N N   . VAL   A 1 39  ? -32.066 -10.393 -23.062 1.00 28.40  ? 576  VAL   A N   1 
ATOM   123  C CA  . VAL   A 1 39  ? -32.083 -10.554 -21.609 1.00 32.23  ? 576  VAL   A CA  1 
ATOM   124  C C   . VAL   A 1 39  ? -30.704 -10.872 -21.023 1.00 32.56  ? 576  VAL   A C   1 
ATOM   125  O O   . VAL   A 1 39  ? -30.537 -10.852 -19.807 1.00 32.80  ? 576  VAL   A O   1 
ATOM   126  C CB  . VAL   A 1 39  ? -33.064 -11.657 -21.155 1.00 32.75  ? 576  VAL   A CB  1 
ATOM   127  C CG1 . VAL   A 1 39  ? -34.497 -11.283 -21.518 1.00 33.91  ? 576  VAL   A CG1 1 
ATOM   128  C CG2 . VAL   A 1 39  ? -32.675 -13.012 -21.739 1.00 37.00  ? 576  VAL   A CG2 1 
ATOM   129  N N   . TYR   A 1 40  ? -29.726 -11.167 -21.876 1.00 27.28  ? 577  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 40  ? -28.378 -11.497 -21.398 1.00 29.11  ? 577  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 40  ? -27.333 -11.133 -22.472 1.00 27.17  ? 577  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 40  ? -27.145 -11.868 -23.438 1.00 26.61  ? 577  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 40  ? -28.324 -12.987 -21.019 1.00 22.90  ? 577  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 40  ? -27.029 -13.442 -20.376 1.00 23.28  ? 577  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 40  ? -26.674 -13.012 -19.100 1.00 23.51  ? 577  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 40  ? -26.187 -14.330 -21.030 1.00 23.75  ? 577  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 40  ? -25.488 -13.427 -18.503 1.00 23.98  ? 577  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 40  ? -24.986 -14.761 -20.436 1.00 27.91  ? 577  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 40  ? -24.651 -14.300 -19.174 1.00 23.81  ? 577  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 40  ? -23.476 -14.720 -18.580 1.00 22.40  ? 577  TYR   A OH  1 
ATOM   141  N N   . ARG   A 1 41  ? -26.671 -9.987  -22.294 1.00 24.67  ? 578  ARG   A N   1 
ATOM   142  C CA  . ARG   A 1 41  ? -25.847 -9.341  -23.331 1.00 28.08  ? 578  ARG   A CA  1 
ATOM   143  C C   . ARG   A 1 41  ? -24.731 -10.196 -23.897 1.00 25.28  ? 578  ARG   A C   1 
ATOM   144  O O   . ARG   A 1 41  ? -24.331 -10.038 -25.044 1.00 29.56  ? 578  ARG   A O   1 
ATOM   145  C CB  . ARG   A 1 41  ? -25.179 -8.073  -22.775 1.00 32.91  ? 578  ARG   A CB  1 
ATOM   146  C CG  . ARG   A 1 41  ? -26.054 -6.918  -22.493 1.00 47.43  ? 578  ARG   A CG  1 
ATOM   147  C CD  . ARG   A 1 41  ? -25.179 -5.682  -22.451 1.00 34.59  ? 578  ARG   A CD  1 
ATOM   148  N NE  . ARG   A 1 41  ? -24.434 -5.523  -21.203 1.00 29.63  ? 578  ARG   A NE  1 
ATOM   149  C CZ  . ARG   A 1 41  ? -23.588 -4.519  -20.996 1.00 31.63  ? 578  ARG   A CZ  1 
ATOM   150  N NH1 . ARG   A 1 41  ? -22.935 -4.398  -19.845 1.00 32.74  ? 578  ARG   A NH1 1 
ATOM   151  N NH2 . ARG   A 1 41  ? -23.405 -3.626  -21.960 1.00 30.57  ? 578  ARG   A NH2 1 
ATOM   152  N N   . PHE   A 1 42  ? -24.205 -11.083 -23.070 1.00 24.91  ? 579  PHE   A N   1 
ATOM   153  C CA  . PHE   A 1 42  ? -22.979 -11.774 -23.432 1.00 26.46  ? 579  PHE   A CA  1 
ATOM   154  C C   . PHE   A 1 42  ? -23.168 -12.797 -24.550 1.00 35.53  ? 579  PHE   A C   1 
ATOM   155  O O   . PHE   A 1 42  ? -22.190 -13.220 -25.156 1.00 35.17  ? 579  PHE   A O   1 
ATOM   156  C CB  . PHE   A 1 42  ? -22.383 -12.433 -22.193 1.00 26.28  ? 579  PHE   A CB  1 
ATOM   157  C CG  . PHE   A 1 42  ? -22.110 -11.462 -21.079 1.00 25.92  ? 579  PHE   A CG  1 
ATOM   158  C CD1 . PHE   A 1 42  ? -20.893 -10.788 -21.005 1.00 27.31  ? 579  PHE   A CD1 1 
ATOM   159  C CD2 . PHE   A 1 42  ? -23.081 -11.194 -20.121 1.00 24.81  ? 579  PHE   A CD2 1 
ATOM   160  C CE1 . PHE   A 1 42  ? -20.650 -9.871  -19.976 1.00 25.79  ? 579  PHE   A CE1 1 
ATOM   161  C CE2 . PHE   A 1 42  ? -22.836 -10.284 -19.091 1.00 27.60  ? 579  PHE   A CE2 1 
ATOM   162  C CZ  . PHE   A 1 42  ? -21.619 -9.631  -19.022 1.00 29.05  ? 579  PHE   A CZ  1 
ATOM   163  N N   . VAL   A 1 43  ? -24.410 -13.182 -24.848 1.00 27.61  ? 580  VAL   A N   1 
ATOM   164  C CA  . VAL   A 1 43  ? -24.617 -14.190 -25.892 1.00 28.23  ? 580  VAL   A CA  1 
ATOM   165  C C   . VAL   A 1 43  ? -24.912 -13.563 -27.254 1.00 29.45  ? 580  VAL   A C   1 
ATOM   166  O O   . VAL   A 1 43  ? -25.228 -14.281 -28.205 1.00 27.07  ? 580  VAL   A O   1 
ATOM   167  C CB  . VAL   A 1 43  ? -25.754 -15.171 -25.537 1.00 27.84  ? 580  VAL   A CB  1 
ATOM   168  C CG1 . VAL   A 1 43  ? -25.381 -15.991 -24.301 1.00 27.75  ? 580  VAL   A CG1 1 
ATOM   169  C CG2 . VAL   A 1 43  ? -27.054 -14.442 -25.332 1.00 29.65  ? 580  VAL   A CG2 1 
ATOM   170  N N   . VAL   A 1 44  ? -24.799 -12.238 -27.356 1.00 26.46  ? 581  VAL   A N   1 
ATOM   171  C CA  . VAL   A 1 44  ? -24.814 -11.594 -28.670 1.00 27.58  ? 581  VAL   A CA  1 
ATOM   172  C C   . VAL   A 1 44  ? -23.795 -12.301 -29.576 1.00 26.74  ? 581  VAL   A C   1 
ATOM   173  O O   . VAL   A 1 44  ? -22.683 -12.629 -29.146 1.00 28.81  ? 581  VAL   A O   1 
ATOM   174  C CB  . VAL   A 1 44  ? -24.494 -10.083 -28.585 1.00 32.21  ? 581  VAL   A CB  1 
ATOM   175  C CG1 . VAL   A 1 44  ? -24.242 -9.497  -29.965 1.00 35.06  ? 581  VAL   A CG1 1 
ATOM   176  C CG2 . VAL   A 1 44  ? -25.637 -9.331  -27.914 1.00 41.56  ? 581  VAL   A CG2 1 
ATOM   177  N N   . LYS   A 1 45  ? -24.186 -12.576 -30.817 1.00 25.71  ? 582  LYS   A N   1 
ATOM   178  C CA  . LYS   A 1 45  ? -23.332 -13.348 -31.732 1.00 26.47  ? 582  LYS   A CA  1 
ATOM   179  C C   . LYS   A 1 45  ? -21.963 -12.686 -31.977 1.00 28.49  ? 582  LYS   A C   1 
ATOM   180  O O   . LYS   A 1 45  ? -21.896 -11.496 -32.300 1.00 27.56  ? 582  LYS   A O   1 
ATOM   181  C CB  . LYS   A 1 45  ? -24.065 -13.544 -33.067 1.00 28.35  ? 582  LYS   A CB  1 
ATOM   182  C CG  . LYS   A 1 45  ? -23.281 -14.301 -34.140 1.00 29.31  ? 582  LYS   A CG  1 
ATOM   183  C CD  . LYS   A 1 45  ? -23.090 -15.763 -33.773 1.00 40.94  ? 582  LYS   A CD  1 
ATOM   184  C CE  . LYS   A 1 45  ? -22.414 -16.522 -34.896 1.00 41.93  ? 582  LYS   A CE  1 
ATOM   185  N NZ  . LYS   A 1 45  ? -22.304 -17.975 -34.583 1.00 31.04  ? 582  LYS   A NZ  1 
ATOM   186  N N   . ASP   A 1 46  ? -20.883 -13.457 -31.811 1.00 24.22  ? 583  ASP   A N   1 
ATOM   187  C CA  . ASP   A 1 46  ? -19.542 -12.992 -32.180 1.00 26.90  ? 583  ASP   A CA  1 
ATOM   188  C C   . ASP   A 1 46  ? -19.519 -12.506 -33.618 1.00 27.97  ? 583  ASP   A C   1 
ATOM   189  O O   . ASP   A 1 46  ? -20.045 -13.177 -34.515 1.00 28.00  ? 583  ASP   A O   1 
ATOM   190  C CB  . ASP   A 1 46  ? -18.484 -14.095 -32.080 1.00 26.57  ? 583  ASP   A CB  1 
ATOM   191  C CG  . ASP   A 1 46  ? -18.098 -14.445 -30.661 1.00 33.13  ? 583  ASP   A CG  1 
ATOM   192  O OD1 . ASP   A 1 46  ? -18.617 -13.836 -29.696 1.00 31.40  ? 583  ASP   A OD1 1 
ATOM   193  O OD2 . ASP   A 1 46  ? -17.244 -15.356 -30.527 1.00 34.48  ? 583  ASP   A OD2 1 
ATOM   194  N N   . SER   A 1 47  ? -18.854 -11.380 -33.846 1.00 27.11  ? 584  SER   A N   1 
ATOM   195  C CA  . SER   A 1 47  ? -18.586 -10.897 -35.195 1.00 27.75  ? 584  SER   A CA  1 
ATOM   196  C C   . SER   A 1 47  ? -17.343 -10.028 -35.146 1.00 31.50  ? 584  SER   A C   1 
ATOM   197  O O   . SER   A 1 47  ? -16.837 -9.714  -34.061 1.00 30.92  ? 584  SER   A O   1 
ATOM   198  C CB  . SER   A 1 47  ? -19.759 -10.088 -35.749 1.00 27.28  ? 584  SER   A CB  1 
ATOM   199  O OG  . SER   A 1 47  ? -19.767 -8.791  -35.168 1.00 31.35  ? 584  SER   A OG  1 
ATOM   200  N N   . GLU   A 1 48  ? -16.873 -9.603  -36.313 1.00 30.93  ? 585  GLU   A N   1 
ATOM   201  C CA  . GLU   A 1 48  ? -15.767 -8.650  -36.373 1.00 29.85  ? 585  GLU   A CA  1 
ATOM   202  C C   . GLU   A 1 48  ? -16.154 -7.275  -35.811 1.00 33.79  ? 585  GLU   A C   1 
ATOM   203  O O   . GLU   A 1 48  ? -15.297 -6.417  -35.624 1.00 37.26  ? 585  GLU   A O   1 
ATOM   204  C CB  . GLU   A 1 48  ? -15.270 -8.504  -37.815 1.00 38.95  ? 585  GLU   A CB  1 
ATOM   205  C CG  . GLU   A 1 48  ? -14.428 -9.674  -38.310 1.00 56.23  ? 585  GLU   A CG  1 
ATOM   206  C CD  . GLU   A 1 48  ? -13.850 -9.427  -39.702 1.00 78.04  ? 585  GLU   A CD  1 
ATOM   207  O OE1 . GLU   A 1 48  ? -14.158 -8.369  -40.305 1.00 82.68  ? 585  GLU   A OE1 1 
ATOM   208  O OE2 . GLU   A 1 48  ? -13.089 -10.291 -40.195 1.00 79.90  ? 585  GLU   A OE2 1 
ATOM   209  N N   . GLU   A 1 49  ? -17.444 -7.066  -35.554 1.00 31.01  ? 586  GLU   A N   1 
ATOM   210  C CA  . GLU   A 1 49  ? -17.913 -5.825  -34.955 1.00 30.80  ? 586  GLU   A CA  1 
ATOM   211  C C   . GLU   A 1 49  ? -17.885 -5.840  -33.423 1.00 31.08  ? 586  GLU   A C   1 
ATOM   212  O O   . GLU   A 1 49  ? -18.175 -4.824  -32.793 1.00 31.88  ? 586  GLU   A O   1 
ATOM   213  C CB  . GLU   A 1 49  ? -19.342 -5.501  -35.422 1.00 34.47  ? 586  GLU   A CB  1 
ATOM   214  C CG  . GLU   A 1 49  ? -19.538 -5.528  -36.931 1.00 42.79  ? 586  GLU   A CG  1 
ATOM   215  C CD  . GLU   A 1 49  ? -18.466 -4.755  -37.681 1.00 48.64  ? 586  GLU   A CD  1 
ATOM   216  O OE1 . GLU   A 1 49  ? -18.075 -3.656  -37.225 1.00 46.57  ? 586  GLU   A OE1 1 
ATOM   217  O OE2 . GLU   A 1 49  ? -18.010 -5.253  -38.732 1.00 48.69  ? 586  GLU   A OE2 1 
ATOM   218  N N   . ASN   A 1 50  ? -17.560 -6.972  -32.805 1.00 27.65  ? 587  ASN   A N   1 
ATOM   219  C CA  . ASN   A 1 50  ? -17.486 -6.959  -31.355 1.00 27.74  ? 587  ASN   A CA  1 
ATOM   220  C C   . ASN   A 1 50  ? -16.348 -7.781  -30.757 1.00 29.09  ? 587  ASN   A C   1 
ATOM   221  O O   . ASN   A 1 50  ? -16.050 -7.637  -29.573 1.00 26.07  ? 587  ASN   A O   1 
ATOM   222  C CB  . ASN   A 1 50  ? -18.838 -7.385  -30.745 1.00 27.49  ? 587  ASN   A CB  1 
ATOM   223  C CG  . ASN   A 1 50  ? -19.324 -8.745  -31.241 1.00 27.70  ? 587  ASN   A CG  1 
ATOM   224  O OD1 . ASN   A 1 50  ? -18.541 -9.661  -31.455 1.00 25.63  ? 587  ASN   A OD1 1 
ATOM   225  N ND2 . ASN   A 1 50  ? -20.638 -8.872  -31.417 1.00 27.97  ? 587  ASN   A ND2 1 
ATOM   226  N N   . ILE   A 1 51  ? -15.695 -8.624  -31.553 1.00 28.00  ? 588  ILE   A N   1 
ATOM   227  C CA  . ILE   A 1 51  ? -14.511 -9.315  -31.046 1.00 29.03  ? 588  ILE   A CA  1 
ATOM   228  C C   . ILE   A 1 51  ? -13.574 -9.725  -32.175 1.00 32.92  ? 588  ILE   A C   1 
ATOM   229  O O   . ILE   A 1 51  ? -14.010 -10.244 -33.205 1.00 30.29  ? 588  ILE   A O   1 
ATOM   230  C CB  . ILE   A 1 51  ? -14.895 -10.549 -30.198 1.00 32.28  ? 588  ILE   A CB  1 
ATOM   231  C CG1 . ILE   A 1 51  ? -13.647 -11.145 -29.541 1.00 33.34  ? 588  ILE   A CG1 1 
ATOM   232  C CG2 . ILE   A 1 51  ? -15.698 -11.584 -31.026 1.00 29.75  ? 588  ILE   A CG2 1 
ATOM   233  C CD1 . ILE   A 1 51  ? -13.953 -12.124 -28.451 1.00 37.40  ? 588  ILE   A CD1 1 
ATOM   234  N N   . VAL   A 1 52  ? -12.282 -9.463  -31.994 1.00 29.11  ? 589  VAL   A N   1 
ATOM   235  C CA  . VAL   A 1 52  ? -11.286 -9.804  -33.020 1.00 27.58  ? 589  VAL   A CA  1 
ATOM   236  C C   . VAL   A 1 52  ? -10.091 -10.512 -32.398 1.00 31.23  ? 589  VAL   A C   1 
ATOM   237  O O   . VAL   A 1 52  ? -9.723  -10.254 -31.246 1.00 28.17  ? 589  VAL   A O   1 
ATOM   238  C CB  . VAL   A 1 52  ? -10.799 -8.560  -33.802 1.00 36.07  ? 589  VAL   A CB  1 
ATOM   239  C CG1 . VAL   A 1 52  ? -11.955 -7.911  -34.545 1.00 37.98  ? 589  VAL   A CG1 1 
ATOM   240  C CG2 . VAL   A 1 52  ? -10.152 -7.558  -32.879 1.00 35.39  ? 589  VAL   A CG2 1 
ATOM   241  N N   . PHE   A 1 53  ? -9.510  -11.430 -33.164 1.00 28.95  ? 590  PHE   A N   1 
ATOM   242  C CA  . PHE   A 1 53  ? -8.408  -12.261 -32.695 1.00 25.70  ? 590  PHE   A CA  1 
ATOM   243  C C   . PHE   A 1 53  ? -7.139  -12.016 -33.509 1.00 36.03  ? 590  PHE   A C   1 
ATOM   244  O O   . PHE   A 1 53  ? -7.216  -11.545 -34.647 1.00 35.98  ? 590  PHE   A O   1 
ATOM   245  C CB  . PHE   A 1 53  ? -8.806  -13.734 -32.768 1.00 30.69  ? 590  PHE   A CB  1 
ATOM   246  C CG  . PHE   A 1 53  ? -10.038 -14.062 -31.978 1.00 31.24  ? 590  PHE   A CG  1 
ATOM   247  C CD1 . PHE   A 1 53  ? -9.943  -14.381 -30.636 1.00 31.93  ? 590  PHE   A CD1 1 
ATOM   248  C CD2 . PHE   A 1 53  ? -11.294 -14.048 -32.578 1.00 33.69  ? 590  PHE   A CD2 1 
ATOM   249  C CE1 . PHE   A 1 53  ? -11.082 -14.684 -29.901 1.00 37.28  ? 590  PHE   A CE1 1 
ATOM   250  C CE2 . PHE   A 1 53  ? -12.434 -14.350 -31.845 1.00 34.90  ? 590  PHE   A CE2 1 
ATOM   251  C CZ  . PHE   A 1 53  ? -12.323 -14.668 -30.507 1.00 33.05  ? 590  PHE   A CZ  1 
ATOM   252  N N   . GLU   A 1 54  ? -5.980  -12.316 -32.918 1.00 31.87  ? 591  GLU   A N   1 
ATOM   253  C CA  . GLU   A 1 54  ? -4.700  -12.278 -33.644 1.00 33.03  ? 591  GLU   A CA  1 
ATOM   254  C C   . GLU   A 1 54  ? -4.568  -13.495 -34.561 1.00 51.36  ? 591  GLU   A C   1 
ATOM   255  O O   . GLU   A 1 54  ? -5.407  -14.401 -34.510 1.00 50.83  ? 591  GLU   A O   1 
ATOM   256  C CB  . GLU   A 1 54  ? -3.504  -12.250 -32.681 1.00 30.19  ? 591  GLU   A CB  1 
ATOM   257  C CG  . GLU   A 1 54  ? -3.385  -11.029 -31.779 1.00 33.50  ? 591  GLU   A CG  1 
ATOM   258  C CD  . GLU   A 1 54  ? -2.909  -9.775  -32.500 1.00 45.92  ? 591  GLU   A CD  1 
ATOM   259  O OE1 . GLU   A 1 54  ? -2.653  -8.759  -31.823 1.00 48.11  ? 591  GLU   A OE1 1 
ATOM   260  O OE2 . GLU   A 1 54  ? -2.789  -9.792  -33.742 1.00 49.91  ? 591  GLU   A OE2 1 
ATOM   261  N N   . ASP   A 1 55  ? -3.520  -13.509 -35.388 1.00 71.02  ? 592  ASP   A N   1 
ATOM   262  C CA  . ASP   A 1 55  ? -3.181  -14.687 -36.182 1.00 77.85  ? 592  ASP   A CA  1 
ATOM   263  C C   . ASP   A 1 55  ? -1.741  -15.134 -35.948 1.00 84.38  ? 592  ASP   A C   1 
ATOM   264  O O   . ASP   A 1 55  ? -0.872  -14.911 -36.782 1.00 89.53  ? 592  ASP   A O   1 
ATOM   265  C CB  . ASP   A 1 55  ? -3.406  -14.421 -37.668 1.00 77.07  ? 592  ASP   A CB  1 
ATOM   266  C CG  . ASP   A 1 55  ? -4.857  -14.111 -37.991 1.00 89.25  ? 592  ASP   A CG  1 
ATOM   267  O OD1 . ASP   A 1 55  ? -5.427  -13.180 -37.379 1.00 94.43  ? 592  ASP   A OD1 1 
ATOM   268  O OD2 . ASP   A 1 55  ? -5.434  -14.836 -38.828 1.00 95.58  ? 592  ASP   A OD2 1 
ATOM   269  N N   . GLY   A 1 62  ? -3.298  -23.617 -27.821 1.00 58.38  ? 599  GLY   A N   1 
ATOM   270  C CA  . GLY   A 1 62  ? -4.228  -23.651 -28.936 1.00 61.47  ? 599  GLY   A CA  1 
ATOM   271  C C   . GLY   A 1 62  ? -5.366  -22.657 -28.780 1.00 58.85  ? 599  GLY   A C   1 
ATOM   272  O O   . GLY   A 1 62  ? -6.239  -22.555 -29.640 1.00 55.27  ? 599  GLY   A O   1 
ATOM   273  N N   . ILE   A 1 63  ? -5.356  -21.922 -27.673 1.00 57.01  ? 600  ILE   A N   1 
ATOM   274  C CA  . ILE   A 1 63  ? -6.390  -20.931 -27.389 1.00 50.21  ? 600  ILE   A CA  1 
ATOM   275  C C   . ILE   A 1 63  ? -6.203  -19.697 -28.258 1.00 38.51  ? 600  ILE   A C   1 
ATOM   276  O O   . ILE   A 1 63  ? -5.100  -19.162 -28.345 1.00 46.96  ? 600  ILE   A O   1 
ATOM   277  C CB  . ILE   A 1 63  ? -6.372  -20.524 -25.898 1.00 49.01  ? 600  ILE   A CB  1 
ATOM   278  C CG1 . ILE   A 1 63  ? -6.866  -21.676 -25.026 1.00 56.58  ? 600  ILE   A CG1 1 
ATOM   279  C CG2 . ILE   A 1 63  ? -7.226  -19.296 -25.650 1.00 49.16  ? 600  ILE   A CG2 1 
ATOM   280  C CD1 . ILE   A 1 63  ? -6.666  -21.434 -23.552 1.00 60.22  ? 600  ILE   A CD1 1 
ATOM   281  N N   . PRO   A 1 64  ? -7.281  -19.240 -28.911 1.00 40.29  ? 601  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 64  ? -7.170  -18.032 -29.735 1.00 41.73  ? 601  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 64  ? -6.703  -16.833 -28.910 1.00 40.84  ? 601  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 64  ? -7.025  -16.734 -27.725 1.00 41.06  ? 601  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 64  ? -8.595  -17.825 -30.267 1.00 45.22  ? 601  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 64  ? -9.479  -18.621 -29.356 1.00 48.58  ? 601  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 64  ? -8.651  -19.778 -28.883 1.00 45.88  ? 601  PRO   A CD  1 
ATOM   288  N N   . ILE   A 1 65  ? -5.920  -15.955 -29.529 1.00 33.99  ? 602  ILE   A N   1 
ATOM   289  C CA  . ILE   A 1 65  ? -5.366  -14.801 -28.836 1.00 32.05  ? 602  ILE   A CA  1 
ATOM   290  C C   . ILE   A 1 65  ? -6.225  -13.588 -29.165 1.00 28.65  ? 602  ILE   A C   1 
ATOM   291  O O   . ILE   A 1 65  ? -6.371  -13.206 -30.324 1.00 30.38  ? 602  ILE   A O   1 
ATOM   292  C CB  . ILE   A 1 65  ? -3.889  -14.558 -29.235 1.00 38.44  ? 602  ILE   A CB  1 
ATOM   293  C CG1 . ILE   A 1 65  ? -3.032  -15.765 -28.843 1.00 41.47  ? 602  ILE   A CG1 1 
ATOM   294  C CG2 . ILE   A 1 65  ? -3.328  -13.302 -28.560 1.00 32.27  ? 602  ILE   A CG2 1 
ATOM   295  C CD1 . ILE   A 1 65  ? -1.633  -15.733 -29.442 1.00 51.45  ? 602  ILE   A CD1 1 
ATOM   296  N N   . ILE   A 1 66  ? -6.816  -12.990 -28.145 1.00 30.13  ? 603  ILE   A N   1 
ATOM   297  C CA  . ILE   A 1 66  ? -7.729  -11.884 -28.373 1.00 26.08  ? 603  ILE   A CA  1 
ATOM   298  C C   . ILE   A 1 66  ? -6.982  -10.610 -28.716 1.00 28.60  ? 603  ILE   A C   1 
ATOM   299  O O   . ILE   A 1 66  ? -6.078  -10.209 -27.990 1.00 32.98  ? 603  ILE   A O   1 
ATOM   300  C CB  . ILE   A 1 66  ? -8.605  -11.656 -27.139 1.00 26.34  ? 603  ILE   A CB  1 
ATOM   301  C CG1 . ILE   A 1 66  ? -9.510  -12.870 -26.943 1.00 36.16  ? 603  ILE   A CG1 1 
ATOM   302  C CG2 . ILE   A 1 66  ? -9.442  -10.409 -27.303 1.00 36.19  ? 603  ILE   A CG2 1 
ATOM   303  C CD1 . ILE   A 1 66  ? -10.082 -12.970 -25.567 1.00 36.22  ? 603  ILE   A CD1 1 
ATOM   304  N N   . LYS   A 1 67  ? -7.369  -9.983  -29.825 1.00 26.28  ? 604  LYS   A N   1 
ATOM   305  C CA  . LYS   A 1 67  ? -6.783  -8.723  -30.257 1.00 28.51  ? 604  LYS   A CA  1 
ATOM   306  C C   . LYS   A 1 67  ? -7.572  -7.549  -29.686 1.00 26.01  ? 604  LYS   A C   1 
ATOM   307  O O   . LYS   A 1 67  ? -7.002  -6.555  -29.243 1.00 28.48  ? 604  LYS   A O   1 
ATOM   308  C CB  . LYS   A 1 67  ? -6.739  -8.647  -31.797 1.00 27.76  ? 604  LYS   A CB  1 
ATOM   309  C CG  . LYS   A 1 67  ? -6.099  -7.374  -32.341 1.00 30.96  ? 604  LYS   A CG  1 
ATOM   310  C CD  . LYS   A 1 67  ? -6.096  -7.361  -33.876 1.00 34.92  ? 604  LYS   A CD  1 
ATOM   311  C CE  . LYS   A 1 67  ? -5.452  -6.090  -34.426 1.00 46.63  ? 604  LYS   A CE  1 
ATOM   312  N NZ  . LYS   A 1 67  ? -5.393  -6.123  -35.923 1.00 56.01  ? 604  LYS   A NZ  1 
ATOM   313  N N   . GLY   A 1 68  ? -8.895  -7.665  -29.690 1.00 25.38  ? 605  GLY   A N   1 
ATOM   314  C CA  . GLY   A 1 68  ? -9.714  -6.600  -29.151 1.00 24.22  ? 605  GLY   A CA  1 
ATOM   315  C C   . GLY   A 1 68  ? -11.169 -6.992  -29.102 1.00 24.44  ? 605  GLY   A C   1 
ATOM   316  O O   . GLY   A 1 68  ? -11.533 -8.064  -29.577 1.00 25.93  ? 605  GLY   A O   1 
ATOM   317  N N   . GLY   A 1 69  ? -11.997 -6.135  -28.513 1.00 29.03  ? 606  GLY   A N   1 
ATOM   318  C CA  . GLY   A 1 69  ? -13.425 -6.397  -28.479 1.00 26.46  ? 606  GLY   A CA  1 
ATOM   319  C C   . GLY   A 1 69  ? -14.145 -5.333  -27.688 1.00 27.02  ? 606  GLY   A C   1 
ATOM   320  O O   . GLY   A 1 69  ? -13.516 -4.446  -27.115 1.00 26.64  ? 606  GLY   A O   1 
ATOM   321  N N   . THR   A 1 70  ? -15.468 -5.423  -27.644 1.00 23.12  ? 607  THR   A N   1 
ATOM   322  C CA  . THR   A 1 70  ? -16.223 -4.625  -26.698 1.00 21.79  ? 607  THR   A CA  1 
ATOM   323  C C   . THR   A 1 70  ? -15.869 -5.133  -25.296 1.00 23.01  ? 607  THR   A C   1 
ATOM   324  O O   . THR   A 1 70  ? -15.415 -6.269  -25.136 1.00 24.47  ? 607  THR   A O   1 
ATOM   325  C CB  . THR   A 1 70  ? -17.729 -4.728  -26.937 1.00 27.42  ? 607  THR   A CB  1 
ATOM   326  O OG1 . THR   A 1 70  ? -18.147 -6.093  -26.789 1.00 28.55  ? 607  THR   A OG1 1 
ATOM   327  C CG2 . THR   A 1 70  ? -18.099 -4.242  -28.348 1.00 26.79  ? 607  THR   A CG2 1 
ATOM   328  N N   . VAL   A 1 71  ? -16.062 -4.308  -24.278 1.00 23.66  ? 608  VAL   A N   1 
ATOM   329  C CA  . VAL   A 1 71  ? -15.765 -4.779  -22.937 1.00 24.85  ? 608  VAL   A CA  1 
ATOM   330  C C   . VAL   A 1 71  ? -16.660 -5.969  -22.594 1.00 27.41  ? 608  VAL   A C   1 
ATOM   331  O O   . VAL   A 1 71  ? -16.240 -6.859  -21.869 1.00 25.15  ? 608  VAL   A O   1 
ATOM   332  C CB  . VAL   A 1 71  ? -15.915 -3.665  -21.877 1.00 27.28  ? 608  VAL   A CB  1 
ATOM   333  C CG1 . VAL   A 1 71  ? -17.376 -3.308  -21.662 1.00 29.50  ? 608  VAL   A CG1 1 
ATOM   334  C CG2 . VAL   A 1 71  ? -15.284 -4.115  -20.583 1.00 30.29  ? 608  VAL   A CG2 1 
ATOM   335  N N   . VAL   A 1 72  ? -17.879 -6.008  -23.138 1.00 24.32  ? 609  VAL   A N   1 
ATOM   336  C CA  . VAL   A 1 72  ? -18.767 -7.142  -22.878 1.00 24.34  ? 609  VAL   A CA  1 
ATOM   337  C C   . VAL   A 1 72  ? -18.173 -8.441  -23.410 1.00 25.20  ? 609  VAL   A C   1 
ATOM   338  O O   . VAL   A 1 72  ? -18.173 -9.472  -22.724 1.00 25.48  ? 609  VAL   A O   1 
ATOM   339  C CB  . VAL   A 1 72  ? -20.155 -6.921  -23.500 1.00 33.21  ? 609  VAL   A CB  1 
ATOM   340  C CG1 . VAL   A 1 72  ? -20.926 -8.230  -23.565 1.00 28.55  ? 609  VAL   A CG1 1 
ATOM   341  C CG2 . VAL   A 1 72  ? -20.920 -5.902  -22.677 1.00 29.18  ? 609  VAL   A CG2 1 
ATOM   342  N N   . LYS   A 1 73  ? -17.635 -8.387  -24.627 1.00 21.71  ? 610  LYS   A N   1 
ATOM   343  C CA  . LYS   A 1 73  ? -17.024 -9.573  -25.217 1.00 23.26  ? 610  LYS   A CA  1 
ATOM   344  C C   . LYS   A 1 73  ? -15.715 -9.945  -24.513 1.00 23.71  ? 610  LYS   A C   1 
ATOM   345  O O   . LYS   A 1 73  ? -15.387 -11.130 -24.386 1.00 22.84  ? 610  LYS   A O   1 
ATOM   346  C CB  . LYS   A 1 73  ? -16.794 -9.357  -26.712 1.00 22.92  ? 610  LYS   A CB  1 
ATOM   347  C CG  . LYS   A 1 73  ? -18.066 -9.560  -27.556 1.00 27.43  ? 610  LYS   A CG  1 
ATOM   348  C CD  . LYS   A 1 73  ? -18.495 -11.030 -27.528 1.00 29.11  ? 610  LYS   A CD  1 
ATOM   349  C CE  . LYS   A 1 73  ? -19.894 -11.243 -28.110 1.00 27.99  ? 610  LYS   A CE  1 
ATOM   350  N NZ  . LYS   A 1 73  ? -20.332 -12.643 -27.891 1.00 27.90  ? 610  LYS   A NZ  1 
ATOM   351  N N   . LEU   A 1 74  ? -14.959 -8.948  -24.057 1.00 23.73  ? 611  LEU   A N   1 
ATOM   352  C CA  . LEU   A 1 74  ? -13.749 -9.247  -23.291 1.00 23.94  ? 611  LEU   A CA  1 
ATOM   353  C C   . LEU   A 1 74  ? -14.105 -9.992  -22.005 1.00 23.23  ? 611  LEU   A C   1 
ATOM   354  O O   . LEU   A 1 74  ? -13.443 -10.961 -21.641 1.00 24.37  ? 611  LEU   A O   1 
ATOM   355  C CB  . LEU   A 1 74  ? -12.968 -7.962  -22.964 1.00 24.47  ? 611  LEU   A CB  1 
ATOM   356  C CG  . LEU   A 1 74  ? -12.339 -7.217  -24.151 1.00 26.05  ? 611  LEU   A CG  1 
ATOM   357  C CD1 . LEU   A 1 74  ? -11.577 -5.972  -23.657 1.00 21.64  ? 611  LEU   A CD1 1 
ATOM   358  C CD2 . LEU   A 1 74  ? -11.408 -8.128  -24.912 1.00 27.40  ? 611  LEU   A CD2 1 
ATOM   359  N N   . ILE   A 1 75  ? -15.163 -9.543  -21.331 1.00 21.68  ? 612  ILE   A N   1 
ATOM   360  C CA  . ILE   A 1 75  ? -15.646 -10.214 -20.128 1.00 24.16  ? 612  ILE   A CA  1 
ATOM   361  C C   . ILE   A 1 75  ? -16.122 -11.624 -20.448 1.00 23.32  ? 612  ILE   A C   1 
ATOM   362  O O   . ILE   A 1 75  ? -15.835 -12.557 -19.698 1.00 22.73  ? 612  ILE   A O   1 
ATOM   363  C CB  . ILE   A 1 75  ? -16.791 -9.407  -19.461 1.00 25.05  ? 612  ILE   A CB  1 
ATOM   364  C CG1 . ILE   A 1 75  ? -16.253 -8.069  -18.930 1.00 27.44  ? 612  ILE   A CG1 1 
ATOM   365  C CG2 . ILE   A 1 75  ? -17.454 -10.213 -18.322 1.00 24.43  ? 612  ILE   A CG2 1 
ATOM   366  C CD1 . ILE   A 1 75  ? -15.317 -8.229  -17.739 1.00 27.75  ? 612  ILE   A CD1 1 
ATOM   367  N N   . GLU   A 1 76  ? -16.838 -11.785 -21.564 1.00 22.68  ? 613  GLU   A N   1 
ATOM   368  C CA  . GLU   A 1 76  ? -17.324 -13.107 -21.931 1.00 21.86  ? 613  GLU   A CA  1 
ATOM   369  C C   . GLU   A 1 76  ? -16.148 -14.082 -22.048 1.00 25.13  ? 613  GLU   A C   1 
ATOM   370  O O   . GLU   A 1 76  ? -16.181 -15.191 -21.495 1.00 23.47  ? 613  GLU   A O   1 
ATOM   371  C CB  . GLU   A 1 76  ? -18.106 -13.082 -23.248 1.00 22.83  ? 613  GLU   A CB  1 
ATOM   372  C CG  . GLU   A 1 76  ? -18.796 -14.436 -23.520 1.00 25.20  ? 613  GLU   A CG  1 
ATOM   373  C CD  . GLU   A 1 76  ? -19.228 -14.634 -24.965 1.00 39.23  ? 613  GLU   A CD  1 
ATOM   374  O OE1 . GLU   A 1 76  ? -19.097 -13.694 -25.770 1.00 38.43  ? 613  GLU   A OE1 1 
ATOM   375  O OE2 . GLU   A 1 76  ? -19.707 -15.748 -25.289 1.00 38.66  ? 613  GLU   A OE2 1 
ATOM   376  N N   . ARG   A 1 77  ? -15.108 -13.665 -22.769 1.00 20.03  ? 614  ARG   A N   1 
ATOM   377  C CA  . ARG   A 1 77  ? -13.949 -14.527 -22.968 1.00 21.89  ? 614  ARG   A CA  1 
ATOM   378  C C   . ARG   A 1 77  ? -13.120 -14.690 -21.701 1.00 24.33  ? 614  ARG   A C   1 
ATOM   379  O O   . ARG   A 1 77  ? -12.423 -15.697 -21.525 1.00 24.11  ? 614  ARG   A O   1 
ATOM   380  C CB  . ARG   A 1 77  ? -13.084 -13.967 -24.090 1.00 24.43  ? 614  ARG   A CB  1 
ATOM   381  C CG  . ARG   A 1 77  ? -13.795 -14.023 -25.427 1.00 26.14  ? 614  ARG   A CG  1 
ATOM   382  C CD  . ARG   A 1 77  ? -13.806 -15.459 -25.924 1.00 28.78  ? 614  ARG   A CD  1 
ATOM   383  N NE  . ARG   A 1 77  ? -14.618 -15.642 -27.121 1.00 30.87  ? 614  ARG   A NE  1 
ATOM   384  C CZ  . ARG   A 1 77  ? -14.366 -16.558 -28.053 1.00 35.46  ? 614  ARG   A CZ  1 
ATOM   385  N NH1 . ARG   A 1 77  ? -15.155 -16.665 -29.118 1.00 35.12  ? 614  ARG   A NH1 1 
ATOM   386  N NH2 . ARG   A 1 77  ? -13.316 -17.359 -27.925 1.00 33.63  ? 614  ARG   A NH2 1 
ATOM   387  N N   . LEU   A 1 78  ? -13.174 -13.689 -20.835 1.00 23.92  ? 615  LEU   A N   1 
ATOM   388  C CA  . LEU   A 1 78  ? -12.512 -13.773 -19.532 1.00 23.38  ? 615  LEU   A CA  1 
ATOM   389  C C   . LEU   A 1 78  ? -13.093 -14.920 -18.703 1.00 27.04  ? 615  LEU   A C   1 
ATOM   390  O O   . LEU   A 1 78  ? -12.438 -15.482 -17.819 1.00 23.46  ? 615  LEU   A O   1 
ATOM   391  C CB  . LEU   A 1 78  ? -12.673 -12.453 -18.787 1.00 21.99  ? 615  LEU   A CB  1 
ATOM   392  C CG  . LEU   A 1 78  ? -11.946 -12.273 -17.456 1.00 24.35  ? 615  LEU   A CG  1 
ATOM   393  C CD1 . LEU   A 1 78  ? -10.438 -12.276 -17.696 1.00 23.27  ? 615  LEU   A CD1 1 
ATOM   394  C CD2 . LEU   A 1 78  ? -12.396 -10.965 -16.794 1.00 24.40  ? 615  LEU   A CD2 1 
ATOM   395  N N   . THR   A 1 79  ? -14.349 -15.244 -18.994 1.00 23.65  ? 616  THR   A N   1 
ATOM   396  C CA  . THR   A 1 79  ? -15.104 -16.231 -18.220 1.00 20.44  ? 616  THR   A CA  1 
ATOM   397  C C   . THR   A 1 79  ? -15.797 -17.207 -19.161 1.00 23.34  ? 616  THR   A C   1 
ATOM   398  O O   . THR   A 1 79  ? -16.961 -17.553 -18.974 1.00 22.37  ? 616  THR   A O   1 
ATOM   399  C CB  . THR   A 1 79  ? -16.147 -15.541 -17.337 1.00 22.65  ? 616  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 79  ? -16.950 -14.678 -18.151 1.00 21.93  ? 616  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 79  ? -15.449 -14.686 -16.276 1.00 24.93  ? 616  THR   A CG2 1 
ATOM   402  N N   . TYR   A 1 80  ? -15.059 -17.656 -20.164 1.00 21.33  ? 617  TYR   A N   1 
ATOM   403  C CA  . TYR   A 1 80  ? -15.643 -18.386 -21.289 1.00 22.83  ? 617  TYR   A CA  1 
ATOM   404  C C   . TYR   A 1 80  ? -16.071 -19.785 -20.879 1.00 25.44  ? 617  TYR   A C   1 
ATOM   405  O O   . TYR   A 1 80  ? -15.370 -20.445 -20.107 1.00 28.64  ? 617  TYR   A O   1 
ATOM   406  C CB  . TYR   A 1 80  ? -14.623 -18.448 -22.420 1.00 23.17  ? 617  TYR   A CB  1 
ATOM   407  C CG  . TYR   A 1 80  ? -15.201 -18.747 -23.775 1.00 22.76  ? 617  TYR   A CG  1 
ATOM   408  C CD1 . TYR   A 1 80  ? -16.249 -17.993 -24.284 1.00 28.29  ? 617  TYR   A CD1 1 
ATOM   409  C CD2 . TYR   A 1 80  ? -14.670 -19.758 -24.566 1.00 28.39  ? 617  TYR   A CD2 1 
ATOM   410  C CE1 . TYR   A 1 80  ? -16.767 -18.250 -25.544 1.00 29.68  ? 617  TYR   A CE1 1 
ATOM   411  C CE2 . TYR   A 1 80  ? -15.190 -20.025 -25.829 1.00 31.09  ? 617  TYR   A CE2 1 
ATOM   412  C CZ  . TYR   A 1 80  ? -16.236 -19.270 -26.303 1.00 38.36  ? 617  TYR   A CZ  1 
ATOM   413  O OH  . TYR   A 1 80  ? -16.746 -19.528 -27.554 1.00 37.92  ? 617  TYR   A OH  1 
ATOM   414  N N   . HIS   A 1 81  ? -17.212 -20.244 -21.388 1.00 25.50  ? 618  HIS   A N   1 
ATOM   415  C CA  . HIS   A 1 81  ? -17.710 -21.548 -20.961 1.00 30.06  ? 618  HIS   A CA  1 
ATOM   416  C C   . HIS   A 1 81  ? -16.918 -22.752 -21.486 1.00 35.30  ? 618  HIS   A C   1 
ATOM   417  O O   . HIS   A 1 81  ? -16.933 -23.812 -20.864 1.00 33.51  ? 618  HIS   A O   1 
ATOM   418  C CB  . HIS   A 1 81  ? -19.196 -21.706 -21.339 1.00 25.42  ? 618  HIS   A CB  1 
ATOM   419  C CG  . HIS   A 1 81  ? -19.455 -21.908 -22.799 1.00 29.22  ? 618  HIS   A CG  1 
ATOM   420  N ND1 . HIS   A 1 81  ? -19.411 -20.879 -23.721 1.00 29.65  ? 618  HIS   A ND1 1 
ATOM   421  C CD2 . HIS   A 1 81  ? -19.827 -23.012 -23.497 1.00 30.20  ? 618  HIS   A CD2 1 
ATOM   422  C CE1 . HIS   A 1 81  ? -19.713 -21.344 -24.915 1.00 37.53  ? 618  HIS   A CE1 1 
ATOM   423  N NE2 . HIS   A 1 81  ? -19.963 -22.639 -24.813 1.00 30.46  ? 618  HIS   A NE2 1 
ATOM   424  N N   A MET   A 1 82  ? -16.217 -22.595 -22.605 0.37 28.17  ? 619  MET   A N   1 
ATOM   425  N N   B MET   A 1 82  ? -16.219 -22.593 -22.606 0.63 26.72  ? 619  MET   A N   1 
ATOM   426  C CA  A MET   A 1 82  ? -15.609 -23.755 -23.265 0.37 29.73  ? 619  MET   A CA  1 
ATOM   427  C CA  B MET   A 1 82  ? -15.607 -23.752 -23.261 0.63 28.71  ? 619  MET   A CA  1 
ATOM   428  C C   A MET   A 1 82  ? -14.234 -24.162 -22.732 0.37 32.94  ? 619  MET   A C   1 
ATOM   429  C C   B MET   A 1 82  ? -14.276 -24.184 -22.642 0.63 33.93  ? 619  MET   A C   1 
ATOM   430  O O   A MET   A 1 82  ? -13.825 -25.309 -22.913 0.37 32.03  ? 619  MET   A O   1 
ATOM   431  O O   B MET   A 1 82  ? -13.941 -25.366 -22.662 0.63 31.73  ? 619  MET   A O   1 
ATOM   432  C CB  A MET   A 1 82  ? -15.514 -23.513 -24.771 0.37 34.79  ? 619  MET   A CB  1 
ATOM   433  C CB  B MET   A 1 82  ? -15.416 -23.478 -24.754 0.63 29.76  ? 619  MET   A CB  1 
ATOM   434  C CG  A MET   A 1 82  ? -16.791 -23.863 -25.518 0.37 49.70  ? 619  MET   A CG  1 
ATOM   435  C CG  B MET   A 1 82  ? -16.716 -23.428 -25.543 0.63 44.52  ? 619  MET   A CG  1 
ATOM   436  S SD  A MET   A 1 82  ? -16.687 -23.584 -27.294 0.37 67.97  ? 619  MET   A SD  1 
ATOM   437  S SD  B MET   A 1 82  ? -17.658 -24.969 -25.435 0.63 55.82  ? 619  MET   A SD  1 
ATOM   438  C CE  A MET   A 1 82  ? -18.313 -24.141 -27.805 0.37 68.84  ? 619  MET   A CE  1 
ATOM   439  C CE  B MET   A 1 82  ? -16.604 -26.071 -26.372 0.63 60.46  ? 619  MET   A CE  1 
ATOM   440  N N   . TYR   A 1 83  ? -13.523 -23.241 -22.086 1.00 31.88  ? 620  TYR   A N   1 
ATOM   441  C CA  . TYR   A 1 83  ? -12.227 -23.564 -21.479 1.00 36.20  ? 620  TYR   A CA  1 
ATOM   442  C C   . TYR   A 1 83  ? -11.725 -22.424 -20.600 1.00 33.33  ? 620  TYR   A C   1 
ATOM   443  O O   . TYR   A 1 83  ? -12.173 -21.283 -20.731 1.00 29.69  ? 620  TYR   A O   1 
ATOM   444  C CB  . TYR   A 1 83  ? -11.171 -23.860 -22.549 1.00 34.99  ? 620  TYR   A CB  1 
ATOM   445  C CG  . TYR   A 1 83  ? -11.188 -22.835 -23.644 1.00 31.75  ? 620  TYR   A CG  1 
ATOM   446  C CD1 . TYR   A 1 83  ? -10.612 -21.585 -23.463 1.00 30.81  ? 620  TYR   A CD1 1 
ATOM   447  C CD2 . TYR   A 1 83  ? -11.814 -23.099 -24.851 1.00 33.34  ? 620  TYR   A CD2 1 
ATOM   448  C CE1 . TYR   A 1 83  ? -10.654 -20.634 -24.448 1.00 33.41  ? 620  TYR   A CE1 1 
ATOM   449  C CE2 . TYR   A 1 83  ? -11.853 -22.160 -25.845 1.00 37.06  ? 620  TYR   A CE2 1 
ATOM   450  C CZ  . TYR   A 1 83  ? -11.273 -20.931 -25.642 1.00 33.16  ? 620  TYR   A CZ  1 
ATOM   451  O OH  . TYR   A 1 83  ? -11.316 -19.987 -26.628 1.00 36.38  ? 620  TYR   A OH  1 
ATOM   452  N N   . ALA   A 1 84  ? -10.779 -22.753 -19.725 1.00 41.59  ? 621  ALA   A N   1 
ATOM   453  C CA  . ALA   A 1 84  ? -10.063 -21.766 -18.929 1.00 39.05  ? 621  ALA   A CA  1 
ATOM   454  C C   . ALA   A 1 84  ? -9.035  -21.034 -19.785 1.00 33.97  ? 621  ALA   A C   1 
ATOM   455  O O   . ALA   A 1 84  ? -8.552  -21.563 -20.791 1.00 30.57  ? 621  ALA   A O   1 
ATOM   456  C CB  . ALA   A 1 84  ? -9.383  -22.435 -17.748 1.00 42.83  ? 621  ALA   A CB  1 
ATOM   457  N N   . ASP   A 1 85  ? -8.683  -19.823 -19.365 1.00 32.71  ? 622  ASP   A N   1 
ATOM   458  C CA  . ASP   A 1 85  ? -7.748  -18.991 -20.110 1.00 26.06  ? 622  ASP   A CA  1 
ATOM   459  C C   . ASP   A 1 85  ? -6.889  -18.194 -19.124 1.00 31.17  ? 622  ASP   A C   1 
ATOM   460  O O   . ASP   A 1 85  ? -7.035  -16.982 -19.011 1.00 28.66  ? 622  ASP   A O   1 
ATOM   461  C CB  . ASP   A 1 85  ? -8.514  -18.062 -21.049 1.00 29.06  ? 622  ASP   A CB  1 
ATOM   462  C CG  . ASP   A 1 85  ? -7.635  -17.437 -22.115 1.00 35.62  ? 622  ASP   A CG  1 
ATOM   463  O OD1 . ASP   A 1 85  ? -6.395  -17.544 -22.012 1.00 33.88  ? 622  ASP   A OD1 1 
ATOM   464  O OD2 . ASP   A 1 85  ? -8.187  -16.815 -23.053 1.00 35.73  ? 622  ASP   A OD2 1 
ATOM   465  N N   . PRO   A 1 86  ? -5.996  -18.882 -18.397 1.00 34.29  ? 623  PRO   A N   1 
ATOM   466  C CA  . PRO   A 1 86  ? -5.243  -18.232 -17.318 1.00 32.31  ? 623  PRO   A CA  1 
ATOM   467  C C   . PRO   A 1 86  ? -4.341  -17.093 -17.786 1.00 27.73  ? 623  PRO   A C   1 
ATOM   468  O O   . PRO   A 1 86  ? -4.159  -16.133 -17.043 1.00 27.82  ? 623  PRO   A O   1 
ATOM   469  C CB  . PRO   A 1 86  ? -4.402  -19.379 -16.732 1.00 33.96  ? 623  PRO   A CB  1 
ATOM   470  C CG  . PRO   A 1 86  ? -4.311  -20.379 -17.817 1.00 37.04  ? 623  PRO   A CG  1 
ATOM   471  C CD  . PRO   A 1 86  ? -5.650  -20.309 -18.515 1.00 34.72  ? 623  PRO   A CD  1 
ATOM   472  N N   . ASN   A 1 87  ? -3.778  -17.184 -18.984 1.00 27.44  ? 624  ASN   A N   1 
ATOM   473  C CA  . ASN   A 1 87  ? -2.930  -16.091 -19.430 1.00 33.50  ? 624  ASN   A CA  1 
ATOM   474  C C   . ASN   A 1 87  ? -3.759  -14.835 -19.636 1.00 28.87  ? 624  ASN   A C   1 
ATOM   475  O O   . ASN   A 1 87  ? -3.335  -13.734 -19.280 1.00 28.31  ? 624  ASN   A O   1 
ATOM   476  C CB  . ASN   A 1 87  ? -2.177  -16.466 -20.700 1.00 37.23  ? 624  ASN   A CB  1 
ATOM   477  C CG  . ASN   A 1 87  ? -1.103  -17.496 -20.436 1.00 40.98  ? 624  ASN   A CG  1 
ATOM   478  O OD1 . ASN   A 1 87  ? -0.556  -17.562 -19.336 1.00 40.76  ? 624  ASN   A OD1 1 
ATOM   479  N ND2 . ASN   A 1 87  ? -0.799  -18.306 -21.438 1.00 42.28  ? 624  ASN   A ND2 1 
ATOM   480  N N   . PHE   A 1 88  ? -4.954  -15.007 -20.190 1.00 25.16  ? 625  PHE   A N   1 
ATOM   481  C CA  . PHE   A 1 88  ? -5.835  -13.866 -20.413 1.00 25.74  ? 625  PHE   A CA  1 
ATOM   482  C C   . PHE   A 1 88  ? -6.320  -13.298 -19.085 1.00 23.35  ? 625  PHE   A C   1 
ATOM   483  O O   . PHE   A 1 88  ? -6.341  -12.083 -18.910 1.00 24.94  ? 625  PHE   A O   1 
ATOM   484  C CB  . PHE   A 1 88  ? -7.012  -14.260 -21.303 1.00 23.73  ? 625  PHE   A CB  1 
ATOM   485  C CG  . PHE   A 1 88  ? -7.928  -13.116 -21.648 1.00 24.51  ? 625  PHE   A CG  1 
ATOM   486  C CD1 . PHE   A 1 88  ? -7.440  -11.960 -22.253 1.00 29.07  ? 625  PHE   A CD1 1 
ATOM   487  C CD2 . PHE   A 1 88  ? -9.285  -13.212 -21.390 1.00 25.62  ? 625  PHE   A CD2 1 
ATOM   488  C CE1 . PHE   A 1 88  ? -8.301  -10.915 -22.590 1.00 28.95  ? 625  PHE   A CE1 1 
ATOM   489  C CE2 . PHE   A 1 88  ? -10.145 -12.188 -21.719 1.00 23.51  ? 625  PHE   A CE2 1 
ATOM   490  C CZ  . PHE   A 1 88  ? -9.661  -11.032 -22.317 1.00 24.81  ? 625  PHE   A CZ  1 
ATOM   491  N N   . VAL   A 1 89  ? -6.682  -14.169 -18.142 1.00 21.27  ? 626  VAL   A N   1 
ATOM   492  C CA  . VAL   A 1 89  ? -7.116  -13.694 -16.821 1.00 20.65  ? 626  VAL   A CA  1 
ATOM   493  C C   . VAL   A 1 89  ? -6.026  -12.833 -16.172 1.00 26.51  ? 626  VAL   A C   1 
ATOM   494  O O   . VAL   A 1 89  ? -6.290  -11.752 -15.639 1.00 22.91  ? 626  VAL   A O   1 
ATOM   495  C CB  . VAL   A 1 89  ? -7.462  -14.873 -15.890 1.00 26.11  ? 626  VAL   A CB  1 
ATOM   496  C CG1 . VAL   A 1 89  ? -7.636  -14.396 -14.451 1.00 20.84  ? 626  VAL   A CG1 1 
ATOM   497  C CG2 . VAL   A 1 89  ? -8.715  -15.616 -16.408 1.00 26.32  ? 626  VAL   A CG2 1 
ATOM   498  N N   . ARG   A 1 90  ? -4.793  -13.312 -16.235 1.00 24.86  ? 627  ARG   A N   1 
ATOM   499  C CA  . ARG   A 1 90  ? -3.686  -12.573 -15.608 1.00 25.84  ? 627  ARG   A CA  1 
ATOM   500  C C   . ARG   A 1 90  ? -3.469  -11.218 -16.274 1.00 27.55  ? 627  ARG   A C   1 
ATOM   501  O O   . ARG   A 1 90  ? -3.355  -10.198 -15.594 1.00 28.95  ? 627  ARG   A O   1 
ATOM   502  C CB  . ARG   A 1 90  ? -2.377  -13.366 -15.656 1.00 25.97  ? 627  ARG   A CB  1 
ATOM   503  C CG  . ARG   A 1 90  ? -1.239  -12.664 -14.885 1.00 33.68  ? 627  ARG   A CG  1 
ATOM   504  C CD  . ARG   A 1 90  ? 0.113   -13.284 -15.142 1.00 42.93  ? 627  ARG   A CD  1 
ATOM   505  N NE  . ARG   A 1 90  ? 0.010   -14.675 -15.558 1.00 58.83  ? 627  ARG   A NE  1 
ATOM   506  C CZ  . ARG   A 1 90  ? 0.173   -15.094 -16.808 1.00 58.97  ? 627  ARG   A CZ  1 
ATOM   507  N NH1 . ARG   A 1 90  ? 0.049   -16.386 -17.090 1.00 51.46  ? 627  ARG   A NH1 1 
ATOM   508  N NH2 . ARG   A 1 90  ? 0.454   -14.222 -17.773 1.00 58.49  ? 627  ARG   A NH2 1 
ATOM   509  N N   . THR   A 1 91  ? -3.407  -11.215 -17.604 1.00 25.57  ? 628  THR   A N   1 
ATOM   510  C CA  . THR   A 1 91  ? -3.148  -9.984  -18.346 1.00 28.96  ? 628  THR   A CA  1 
ATOM   511  C C   . THR   A 1 91  ? -4.305  -9.007  -18.206 1.00 26.01  ? 628  THR   A C   1 
ATOM   512  O O   . THR   A 1 91  ? -4.106  -7.799  -18.017 1.00 26.04  ? 628  THR   A O   1 
ATOM   513  C CB  . THR   A 1 91  ? -2.896  -10.288 -19.817 1.00 31.72  ? 628  THR   A CB  1 
ATOM   514  O OG1 . THR   A 1 91  ? -1.780  -11.180 -19.908 1.00 36.03  ? 628  THR   A OG1 1 
ATOM   515  C CG2 . THR   A 1 91  ? -2.582  -9.014  -20.590 1.00 28.57  ? 628  THR   A CG2 1 
ATOM   516  N N   . PHE   A 1 92  ? -5.519  -9.536  -18.275 1.00 21.38  ? 629  PHE   A N   1 
ATOM   517  C CA  . PHE   A 1 92  ? -6.699  -8.706  -18.072 1.00 21.39  ? 629  PHE   A CA  1 
ATOM   518  C C   . PHE   A 1 92  ? -6.639  -8.022  -16.698 1.00 20.29  ? 629  PHE   A C   1 
ATOM   519  O O   . PHE   A 1 92  ? -6.800  -6.797  -16.594 1.00 21.83  ? 629  PHE   A O   1 
ATOM   520  C CB  . PHE   A 1 92  ? -7.976  -9.539  -18.205 1.00 20.56  ? 629  PHE   A CB  1 
ATOM   521  C CG  . PHE   A 1 92  ? -9.228  -8.729  -18.123 1.00 23.80  ? 629  PHE   A CG  1 
ATOM   522  C CD1 . PHE   A 1 92  ? -9.724  -8.315  -16.894 1.00 20.52  ? 629  PHE   A CD1 1 
ATOM   523  C CD2 . PHE   A 1 92  ? -9.926  -8.380  -19.273 1.00 25.51  ? 629  PHE   A CD2 1 
ATOM   524  C CE1 . PHE   A 1 92  ? -10.878 -7.552  -16.815 1.00 23.40  ? 629  PHE   A CE1 1 
ATOM   525  C CE2 . PHE   A 1 92  ? -11.095 -7.614  -19.198 1.00 22.71  ? 629  PHE   A CE2 1 
ATOM   526  C CZ  . PHE   A 1 92  ? -11.567 -7.210  -17.969 1.00 22.48  ? 629  PHE   A CZ  1 
ATOM   527  N N   . LEU   A 1 93  ? -6.374  -8.776  -15.639 1.00 23.90  ? 630  LEU   A N   1 
ATOM   528  C CA  . LEU   A 1 93  ? -6.442  -8.167  -14.311 1.00 22.10  ? 630  LEU   A CA  1 
ATOM   529  C C   . LEU   A 1 93  ? -5.322  -7.155  -14.082 1.00 25.83  ? 630  LEU   A C   1 
ATOM   530  O O   . LEU   A 1 93  ? -5.480  -6.216  -13.295 1.00 26.17  ? 630  LEU   A O   1 
ATOM   531  C CB  . LEU   A 1 93  ? -6.417  -9.237  -13.214 1.00 22.23  ? 630  LEU   A CB  1 
ATOM   532  C CG  . LEU   A 1 93  ? -7.784  -9.945  -13.136 1.00 22.77  ? 630  LEU   A CG  1 
ATOM   533  C CD1 . LEU   A 1 93  ? -7.739  -11.124 -12.159 1.00 24.62  ? 630  LEU   A CD1 1 
ATOM   534  C CD2 . LEU   A 1 93  ? -8.914  -8.977  -12.778 1.00 24.28  ? 630  LEU   A CD2 1 
ATOM   535  N N   . THR   A 1 94  ? -4.202  -7.352  -14.765 1.00 22.45  ? 631  THR   A N   1 
ATOM   536  C CA  . THR   A 1 94  ? -3.091  -6.389  -14.692 1.00 22.89  ? 631  THR   A CA  1 
ATOM   537  C C   . THR   A 1 94  ? -3.424  -5.084  -15.423 1.00 25.53  ? 631  THR   A C   1 
ATOM   538  O O   . THR   A 1 94  ? -3.044  -3.999  -14.977 1.00 25.49  ? 631  THR   A O   1 
ATOM   539  C CB  . THR   A 1 94  ? -1.800  -7.000  -15.282 1.00 26.35  ? 631  THR   A CB  1 
ATOM   540  O OG1 . THR   A 1 94  ? -1.379  -8.092  -14.451 1.00 29.44  ? 631  THR   A OG1 1 
ATOM   541  C CG2 . THR   A 1 94  ? -0.655  -5.953  -15.379 1.00 24.15  ? 631  THR   A CG2 1 
ATOM   542  N N   . THR   A 1 95  ? -4.140  -5.186  -16.541 1.00 24.65  ? 632  THR   A N   1 
ATOM   543  C CA  . THR   A 1 95  ? -4.276  -4.039  -17.435 1.00 23.64  ? 632  THR   A CA  1 
ATOM   544  C C   . THR   A 1 95  ? -5.669  -3.409  -17.540 1.00 22.73  ? 632  THR   A C   1 
ATOM   545  O O   . THR   A 1 95  ? -5.803  -2.373  -18.181 1.00 26.51  ? 632  THR   A O   1 
ATOM   546  C CB  . THR   A 1 95  ? -3.857  -4.400  -18.882 1.00 28.89  ? 632  THR   A CB  1 
ATOM   547  O OG1 . THR   A 1 95  ? -4.757  -5.383  -19.420 1.00 26.61  ? 632  THR   A OG1 1 
ATOM   548  C CG2 . THR   A 1 95  ? -2.423  -4.925  -18.920 1.00 29.85  ? 632  THR   A CG2 1 
ATOM   549  N N   . TYR   A 1 96  ? -6.701  -4.000  -16.938 1.00 22.70  ? 633  TYR   A N   1 
ATOM   550  C CA  . TYR   A 1 96  ? -8.065  -3.578  -17.290 1.00 24.52  ? 633  TYR   A CA  1 
ATOM   551  C C   . TYR   A 1 96  ? -8.389  -2.136  -16.921 1.00 27.54  ? 633  TYR   A C   1 
ATOM   552  O O   . TYR   A 1 96  ? -9.328  -1.559  -17.470 1.00 27.12  ? 633  TYR   A O   1 
ATOM   553  C CB  . TYR   A 1 96  ? -9.132  -4.496  -16.646 1.00 20.61  ? 633  TYR   A CB  1 
ATOM   554  C CG  . TYR   A 1 96  ? -9.387  -4.177  -15.180 1.00 23.24  ? 633  TYR   A CG  1 
ATOM   555  C CD1 . TYR   A 1 96  ? -10.339 -3.230  -14.795 1.00 24.48  ? 633  TYR   A CD1 1 
ATOM   556  C CD2 . TYR   A 1 96  ? -8.675  -4.826  -14.184 1.00 22.36  ? 633  TYR   A CD2 1 
ATOM   557  C CE1 . TYR   A 1 96  ? -10.560 -2.934  -13.462 1.00 24.28  ? 633  TYR   A CE1 1 
ATOM   558  C CE2 . TYR   A 1 96  ? -8.903  -4.548  -12.854 1.00 22.84  ? 633  TYR   A CE2 1 
ATOM   559  C CZ  . TYR   A 1 96  ? -9.848  -3.604  -12.498 1.00 25.46  ? 633  TYR   A CZ  1 
ATOM   560  O OH  . TYR   A 1 96  ? -10.065 -3.311  -11.171 1.00 28.40  ? 633  TYR   A OH  1 
ATOM   561  N N   . ARG   A 1 97  ? -7.637  -1.549  -15.985 1.00 26.22  ? 634  ARG   A N   1 
ATOM   562  C CA  . ARG   A 1 97  ? -8.004  -0.231  -15.484 1.00 25.27  ? 634  ARG   A CA  1 
ATOM   563  C C   . ARG   A 1 97  ? -7.789  0.824   -16.561 1.00 29.63  ? 634  ARG   A C   1 
ATOM   564  O O   . ARG   A 1 97  ? -8.303  1.935   -16.456 1.00 29.52  ? 634  ARG   A O   1 
ATOM   565  C CB  . ARG   A 1 97  ? -7.213  0.108   -14.211 1.00 28.62  ? 634  ARG   A CB  1 
ATOM   566  C CG  . ARG   A 1 97  ? -7.480  -0.870  -13.074 1.00 26.09  ? 634  ARG   A CG  1 
ATOM   567  C CD  . ARG   A 1 97  ? -6.366  -0.891  -12.047 1.00 27.97  ? 634  ARG   A CD  1 
ATOM   568  N NE  . ARG   A 1 97  ? -6.466  -2.077  -11.214 1.00 27.31  ? 634  ARG   A NE  1 
ATOM   569  C CZ  . ARG   A 1 97  ? -6.004  -3.282  -11.549 1.00 29.16  ? 634  ARG   A CZ  1 
ATOM   570  N NH1 . ARG   A 1 97  ? -5.369  -3.475  -12.708 1.00 26.82  ? 634  ARG   A NH1 1 
ATOM   571  N NH2 . ARG   A 1 97  ? -6.165  -4.299  -10.712 1.00 27.07  ? 634  ARG   A NH2 1 
ATOM   572  N N   . SER   A 1 98  ? -7.035  0.458   -17.593 1.00 26.01  ? 635  SER   A N   1 
ATOM   573  C CA  . SER   A 1 98  ? -6.821  1.308   -18.761 1.00 29.39  ? 635  SER   A CA  1 
ATOM   574  C C   . SER   A 1 98  ? -8.003  1.316   -19.741 1.00 28.49  ? 635  SER   A C   1 
ATOM   575  O O   . SER   A 1 98  ? -7.992  2.084   -20.703 1.00 31.38  ? 635  SER   A O   1 
ATOM   576  C CB  . SER   A 1 98  ? -5.559  0.878   -19.513 1.00 31.07  ? 635  SER   A CB  1 
ATOM   577  O OG  . SER   A 1 98  ? -5.732  -0.391  -20.120 1.00 26.61  ? 635  SER   A OG  1 
ATOM   578  N N   . PHE   A 1 99  ? -9.011  0.469   -19.520 1.00 28.53  ? 636  PHE   A N   1 
ATOM   579  C CA  . PHE   A 1 99  ? -10.205 0.497   -20.383 1.00 31.51  ? 636  PHE   A CA  1 
ATOM   580  C C   . PHE   A 1 99  ? -11.524 0.269   -19.628 1.00 30.28  ? 636  PHE   A C   1 
ATOM   581  O O   . PHE   A 1 99  ? -12.609 0.345   -20.218 1.00 31.92  ? 636  PHE   A O   1 
ATOM   582  C CB  . PHE   A 1 99  ? -10.086 -0.522  -21.542 1.00 29.18  ? 636  PHE   A CB  1 
ATOM   583  C CG  . PHE   A 1 99  ? -9.846  -1.962  -21.115 1.00 28.72  ? 636  PHE   A CG  1 
ATOM   584  C CD1 . PHE   A 1 99  ? -10.902 -2.779  -20.723 1.00 27.81  ? 636  PHE   A CD1 1 
ATOM   585  C CD2 . PHE   A 1 99  ? -8.567  -2.514  -21.171 1.00 26.93  ? 636  PHE   A CD2 1 
ATOM   586  C CE1 . PHE   A 1 99  ? -10.685 -4.105  -20.351 1.00 25.45  ? 636  PHE   A CE1 1 
ATOM   587  C CE2 . PHE   A 1 99  ? -8.341  -3.832  -20.814 1.00 24.49  ? 636  PHE   A CE2 1 
ATOM   588  C CZ  . PHE   A 1 99  ? -9.398  -4.636  -20.404 1.00 23.82  ? 636  PHE   A CZ  1 
ATOM   589  N N   . CYS   A 1 100 ? -11.448 0.049   -18.325 1.00 24.52  ? 637  CYS   A N   1 
ATOM   590  C CA  . CYS   A 1 100 ? -12.650 -0.278  -17.558 1.00 28.20  ? 637  CYS   A CA  1 
ATOM   591  C C   . CYS   A 1 100 ? -12.424 0.057   -16.086 1.00 33.02  ? 637  CYS   A C   1 
ATOM   592  O O   . CYS   A 1 100 ? -11.350 -0.211  -15.557 1.00 31.46  ? 637  CYS   A O   1 
ATOM   593  C CB  . CYS   A 1 100 ? -12.985 -1.767  -17.755 1.00 25.52  ? 637  CYS   A CB  1 
ATOM   594  S SG  . CYS   A 1 100 ? -14.353 -2.426  -16.769 1.00 30.12  ? 637  CYS   A SG  1 
ATOM   595  N N   . LYS   A 1 101 ? -13.407 0.663   -15.421 1.00 28.92  ? 638  LYS   A N   1 
ATOM   596  C CA  . LYS   A 1 101 ? -13.244 0.990   -14.005 1.00 29.90  ? 638  LYS   A CA  1 
ATOM   597  C C   . LYS   A 1 101 ? -13.451 -0.237  -13.116 1.00 27.28  ? 638  LYS   A C   1 
ATOM   598  O O   . LYS   A 1 101 ? -14.205 -1.141  -13.477 1.00 29.70  ? 638  LYS   A O   1 
ATOM   599  C CB  . LYS   A 1 101 ? -14.216 2.098   -13.583 1.00 32.51  ? 638  LYS   A CB  1 
ATOM   600  C CG  . LYS   A 1 101 ? -14.017 3.417   -14.308 1.00 37.43  ? 638  LYS   A CG  1 
ATOM   601  C CD  . LYS   A 1 101 ? -13.400 4.453   -13.401 1.00 53.11  ? 638  LYS   A CD  1 
ATOM   602  C CE  . LYS   A 1 101 ? -13.517 5.844   -14.007 1.00 67.25  ? 638  LYS   A CE  1 
ATOM   603  N NZ  . LYS   A 1 101 ? -14.942 6.278   -14.166 1.00 70.50  ? 638  LYS   A NZ  1 
ATOM   604  N N   . PRO   A 1 102 ? -12.778 -0.278  -11.953 1.00 32.12  ? 639  PRO   A N   1 
ATOM   605  C CA  . PRO   A 1 102 ? -12.963 -1.379  -10.996 1.00 28.49  ? 639  PRO   A CA  1 
ATOM   606  C C   . PRO   A 1 102 ? -14.439 -1.649  -10.644 1.00 30.91  ? 639  PRO   A C   1 
ATOM   607  O O   . PRO   A 1 102 ? -14.855 -2.804  -10.659 1.00 28.56  ? 639  PRO   A O   1 
ATOM   608  C CB  . PRO   A 1 102 ? -12.184 -0.900  -9.765  1.00 33.86  ? 639  PRO   A CB  1 
ATOM   609  C CG  . PRO   A 1 102 ? -11.104 -0.018  -10.333 1.00 34.48  ? 639  PRO   A CG  1 
ATOM   610  C CD  . PRO   A 1 102 ? -11.721 0.663   -11.524 1.00 34.78  ? 639  PRO   A CD  1 
ATOM   611  N N   . GLN   A 1 103 ? -15.216 -0.611  -10.338 1.00 33.97  ? 640  GLN   A N   1 
ATOM   612  C CA  . GLN   A 1 103 ? -16.640 -0.792  -10.034 1.00 32.05  ? 640  GLN   A CA  1 
ATOM   613  C C   . GLN   A 1 103 ? -17.396 -1.352  -11.237 1.00 30.40  ? 640  GLN   A C   1 
ATOM   614  O O   . GLN   A 1 103 ? -18.321 -2.156  -11.098 1.00 31.17  ? 640  GLN   A O   1 
ATOM   615  C CB  . GLN   A 1 103 ? -17.269 0.534   -9.608  1.00 36.01  ? 640  GLN   A CB  1 
ATOM   616  C CG  . GLN   A 1 103 ? -16.774 1.056   -8.259  1.00 34.53  ? 640  GLN   A CG  1 
ATOM   617  C CD  . GLN   A 1 103 ? -17.525 0.444   -7.091  1.00 45.76  ? 640  GLN   A CD  1 
ATOM   618  O OE1 . GLN   A 1 103 ? -18.469 -0.325  -7.282  1.00 51.22  ? 640  GLN   A OE1 1 
ATOM   619  N NE2 . GLN   A 1 103 ? -17.114 0.788   -5.876  1.00 40.35  ? 640  GLN   A NE2 1 
ATOM   620  N N   . GLU   A 1 104 ? -16.998 -0.896  -12.419 1.00 27.75  ? 641  GLU   A N   1 
ATOM   621  C CA  . GLU   A 1 104 ? -17.591 -1.329  -13.676 1.00 33.81  ? 641  GLU   A CA  1 
ATOM   622  C C   . GLU   A 1 104 ? -17.289 -2.812  -13.930 1.00 31.80  ? 641  GLU   A C   1 
ATOM   623  O O   . GLU   A 1 104 ? -18.165 -3.574  -14.348 1.00 24.63  ? 641  GLU   A O   1 
ATOM   624  C CB  . GLU   A 1 104 ? -17.064 -0.446  -14.811 1.00 32.74  ? 641  GLU   A CB  1 
ATOM   625  C CG  . GLU   A 1 104 ? -17.639 -0.709  -16.181 1.00 35.32  ? 641  GLU   A CG  1 
ATOM   626  C CD  . GLU   A 1 104 ? -16.906 0.072   -17.268 1.00 45.34  ? 641  GLU   A CD  1 
ATOM   627  O OE1 . GLU   A 1 104 ? -17.083 -0.269  -18.458 1.00 38.28  ? 641  GLU   A OE1 1 
ATOM   628  O OE2 . GLU   A 1 104 ? -16.143 1.013   -16.928 1.00 37.94  ? 641  GLU   A OE2 1 
ATOM   629  N N   . LEU   A 1 105 ? -16.053 -3.225  -13.659 1.00 27.75  ? 642  LEU   A N   1 
ATOM   630  C CA  . LEU   A 1 105 ? -15.667 -4.630  -13.812 1.00 23.32  ? 642  LEU   A CA  1 
ATOM   631  C C   . LEU   A 1 105 ? -16.490 -5.516  -12.885 1.00 24.31  ? 642  LEU   A C   1 
ATOM   632  O O   . LEU   A 1 105 ? -16.998 -6.561  -13.312 1.00 24.07  ? 642  LEU   A O   1 
ATOM   633  C CB  . LEU   A 1 105 ? -14.163 -4.818  -13.547 1.00 27.63  ? 642  LEU   A CB  1 
ATOM   634  C CG  . LEU   A 1 105 ? -13.662 -6.263  -13.422 1.00 24.51  ? 642  LEU   A CG  1 
ATOM   635  C CD1 . LEU   A 1 105 ? -13.950 -7.061  -14.695 1.00 22.23  ? 642  LEU   A CD1 1 
ATOM   636  C CD2 . LEU   A 1 105 ? -12.178 -6.310  -13.107 1.00 21.69  ? 642  LEU   A CD2 1 
ATOM   637  N N   . LEU   A 1 106 ? -16.644 -5.098  -11.629 1.00 22.87  ? 643  LEU   A N   1 
ATOM   638  C CA  . LEU   A 1 106 ? -17.466 -5.868  -10.683 1.00 25.03  ? 643  LEU   A CA  1 
ATOM   639  C C   . LEU   A 1 106 ? -18.913 -5.972  -11.177 1.00 25.79  ? 643  LEU   A C   1 
ATOM   640  O O   . LEU   A 1 106 ? -19.511 -7.050  -11.132 1.00 24.21  ? 643  LEU   A O   1 
ATOM   641  C CB  . LEU   A 1 106 ? -17.436 -5.256  -9.271  1.00 23.76  ? 643  LEU   A CB  1 
ATOM   642  C CG  . LEU   A 1 106 ? -18.251 -6.040  -8.225  1.00 24.54  ? 643  LEU   A CG  1 
ATOM   643  C CD1 . LEU   A 1 106 ? -17.887 -7.535  -8.179  1.00 25.89  ? 643  LEU   A CD1 1 
ATOM   644  C CD2 . LEU   A 1 106 ? -18.101 -5.406  -6.829  1.00 26.39  ? 643  LEU   A CD2 1 
ATOM   645  N N   . SER   A 1 107 ? -19.470 -4.868  -11.679 1.00 28.78  ? 644  SER   A N   1 
ATOM   646  C CA  . SER   A 1 107 ? -20.839 -4.902  -12.202 1.00 25.58  ? 644  SER   A CA  1 
ATOM   647  C C   . SER   A 1 107 ? -20.952 -5.858  -13.393 1.00 27.45  ? 644  SER   A C   1 
ATOM   648  O O   . SER   A 1 107 ? -21.926 -6.613  -13.500 1.00 26.81  ? 644  SER   A O   1 
ATOM   649  C CB  . SER   A 1 107 ? -21.303 -3.500  -12.601 1.00 33.26  ? 644  SER   A CB  1 
ATOM   650  O OG  . SER   A 1 107 ? -21.370 -2.660  -11.459 1.00 32.41  ? 644  SER   A OG  1 
ATOM   651  N N   . LEU   A 1 108 ? -19.957 -5.830  -14.279 1.00 23.60  ? 645  LEU   A N   1 
ATOM   652  C CA  . LEU   A 1 108 ? -19.951 -6.716  -15.439 1.00 23.67  ? 645  LEU   A CA  1 
ATOM   653  C C   . LEU   A 1 108 ? -19.873 -8.181  -15.019 1.00 25.69  ? 645  LEU   A C   1 
ATOM   654  O O   . LEU   A 1 108 ? -20.531 -9.030  -15.613 1.00 24.19  ? 645  LEU   A O   1 
ATOM   655  C CB  . LEU   A 1 108 ? -18.787 -6.384  -16.382 1.00 23.07  ? 645  LEU   A CB  1 
ATOM   656  C CG  . LEU   A 1 108 ? -19.003 -5.094  -17.178 1.00 28.34  ? 645  LEU   A CG  1 
ATOM   657  C CD1 . LEU   A 1 108 ? -17.679 -4.601  -17.743 1.00 26.31  ? 645  LEU   A CD1 1 
ATOM   658  C CD2 . LEU   A 1 108 ? -19.995 -5.343  -18.296 1.00 30.75  ? 645  LEU   A CD2 1 
ATOM   659  N N   . LEU   A 1 109 ? -19.081 -8.484  -13.993 1.00 23.76  ? 646  LEU   A N   1 
ATOM   660  C CA  . LEU   A 1 109 ? -18.910 -9.885  -13.585 1.00 20.36  ? 646  LEU   A CA  1 
ATOM   661  C C   . LEU   A 1 109 ? -20.167 -10.400 -12.911 1.00 26.19  ? 646  LEU   A C   1 
ATOM   662  O O   . LEU   A 1 109 ? -20.536 -11.560 -13.075 1.00 25.55  ? 646  LEU   A O   1 
ATOM   663  C CB  . LEU   A 1 109 ? -17.705 -10.041 -12.659 1.00 22.13  ? 646  LEU   A CB  1 
ATOM   664  C CG  . LEU   A 1 109 ? -16.362 -9.933  -13.391 1.00 23.13  ? 646  LEU   A CG  1 
ATOM   665  C CD1 . LEU   A 1 109 ? -15.220 -9.751  -12.378 1.00 24.40  ? 646  LEU   A CD1 1 
ATOM   666  C CD2 . LEU   A 1 109 ? -16.099 -11.139 -14.262 1.00 22.90  ? 646  LEU   A CD2 1 
ATOM   667  N N   . ILE   A 1 110 ? -20.825 -9.524  -12.158 1.00 23.87  ? 647  ILE   A N   1 
ATOM   668  C CA  . ILE   A 1 110 ? -22.090 -9.876  -11.523 1.00 22.67  ? 647  ILE   A CA  1 
ATOM   669  C C   . ILE   A 1 110 ? -23.165 -10.084 -12.602 1.00 25.47  ? 647  ILE   A C   1 
ATOM   670  O O   . ILE   A 1 110 ? -23.916 -11.049 -12.547 1.00 28.09  ? 647  ILE   A O   1 
ATOM   671  C CB  . ILE   A 1 110 ? -22.503 -8.807  -10.510 1.00 28.19  ? 647  ILE   A CB  1 
ATOM   672  C CG1 . ILE   A 1 110 ? -21.532 -8.856  -9.321  1.00 24.28  ? 647  ILE   A CG1 1 
ATOM   673  C CG2 . ILE   A 1 110 ? -23.966 -8.982  -10.076 1.00 29.67  ? 647  ILE   A CG2 1 
ATOM   674  C CD1 . ILE   A 1 110 ? -21.755 -7.759  -8.279  1.00 28.02  ? 647  ILE   A CD1 1 
ATOM   675  N N   . GLU   A 1 111 ? -23.207 -9.188  -13.585 1.00 25.86  ? 648  GLU   A N   1 
ATOM   676  C CA  . GLU   A 1 111 ? -24.095 -9.340  -14.738 1.00 27.42  ? 648  GLU   A CA  1 
ATOM   677  C C   . GLU   A 1 111 ? -23.856 -10.667 -15.466 1.00 28.22  ? 648  GLU   A C   1 
ATOM   678  O O   . GLU   A 1 111 ? -24.805 -11.340 -15.863 1.00 25.12  ? 648  GLU   A O   1 
ATOM   679  C CB  . GLU   A 1 111 ? -23.900 -8.166  -15.703 1.00 25.42  ? 648  GLU   A CB  1 
ATOM   680  C CG  . GLU   A 1 111 ? -24.903 -8.122  -16.835 1.00 28.12  ? 648  GLU   A CG  1 
ATOM   681  C CD  . GLU   A 1 111 ? -24.598 -7.044  -17.869 1.00 35.08  ? 648  GLU   A CD  1 
ATOM   682  O OE1 . GLU   A 1 111 ? -25.287 -7.008  -18.913 1.00 34.16  ? 648  GLU   A OE1 1 
ATOM   683  O OE2 . GLU   A 1 111 ? -23.675 -6.234  -17.636 1.00 33.87  ? 648  GLU   A OE2 1 
ATOM   684  N N   . ARG   A 1 112 ? -22.583 -11.026 -15.643 1.00 24.73  ? 649  ARG   A N   1 
ATOM   685  C CA  . ARG   A 1 112 ? -22.203 -12.287 -16.284 1.00 22.80  ? 649  ARG   A CA  1 
ATOM   686  C C   . ARG   A 1 112 ? -22.710 -13.481 -15.475 1.00 24.81  ? 649  ARG   A C   1 
ATOM   687  O O   . ARG   A 1 112 ? -23.137 -14.491 -16.042 1.00 21.62  ? 649  ARG   A O   1 
ATOM   688  C CB  . ARG   A 1 112 ? -20.677 -12.345 -16.443 1.00 23.65  ? 649  ARG   A CB  1 
ATOM   689  C CG  . ARG   A 1 112 ? -20.129 -13.602 -17.110 1.00 27.28  ? 649  ARG   A CG  1 
ATOM   690  C CD  . ARG   A 1 112 ? -20.232 -13.536 -18.636 1.00 21.61  ? 649  ARG   A CD  1 
ATOM   691  N NE  . ARG   A 1 112 ? -19.485 -14.629 -19.267 1.00 23.00  ? 649  ARG   A NE  1 
ATOM   692  C CZ  . ARG   A 1 112 ? -20.013 -15.530 -20.096 1.00 22.33  ? 649  ARG   A CZ  1 
ATOM   693  N NH1 . ARG   A 1 112 ? -21.311 -15.512 -20.403 1.00 20.14  ? 649  ARG   A NH1 1 
ATOM   694  N NH2 . ARG   A 1 112 ? -19.234 -16.456 -20.634 1.00 22.59  ? 649  ARG   A NH2 1 
ATOM   695  N N   . PHE   A 1 113 ? -22.695 -13.338 -14.148 1.00 21.86  ? 650  PHE   A N   1 
ATOM   696  C CA  . PHE   A 1 113 ? -23.028 -14.440 -13.245 1.00 25.28  ? 650  PHE   A CA  1 
ATOM   697  C C   . PHE   A 1 113 ? -24.501 -14.766 -13.264 1.00 24.78  ? 650  PHE   A C   1 
ATOM   698  O O   . PHE   A 1 113 ? -24.876 -15.930 -13.190 1.00 26.67  ? 650  PHE   A O   1 
ATOM   699  C CB  . PHE   A 1 113 ? -22.595 -14.098 -11.807 1.00 27.19  ? 650  PHE   A CB  1 
ATOM   700  C CG  . PHE   A 1 113 ? -22.582 -15.277 -10.870 1.00 26.13  ? 650  PHE   A CG  1 
ATOM   701  C CD1 . PHE   A 1 113 ? -23.746 -15.684 -10.224 1.00 28.68  ? 650  PHE   A CD1 1 
ATOM   702  C CD2 . PHE   A 1 113 ? -21.393 -15.961 -10.621 1.00 27.18  ? 650  PHE   A CD2 1 
ATOM   703  C CE1 . PHE   A 1 113 ? -23.731 -16.764 -9.355  1.00 32.65  ? 650  PHE   A CE1 1 
ATOM   704  C CE2 . PHE   A 1 113 ? -21.359 -17.038 -9.750  1.00 27.35  ? 650  PHE   A CE2 1 
ATOM   705  C CZ  . PHE   A 1 113 ? -22.533 -17.441 -9.114  1.00 27.93  ? 650  PHE   A CZ  1 
ATOM   706  N N   . GLU   A 1 114 ? -25.329 -13.729 -13.335 1.00 26.03  ? 651  GLU   A N   1 
ATOM   707  C CA  . GLU   A 1 114 ? -26.769 -13.901 -13.163 1.00 24.86  ? 651  GLU   A CA  1 
ATOM   708  C C   . GLU   A 1 114 ? -27.408 -14.269 -14.499 1.00 26.52  ? 651  GLU   A C   1 
ATOM   709  O O   . GLU   A 1 114 ? -28.080 -13.466 -15.144 1.00 31.09  ? 651  GLU   A O   1 
ATOM   710  C CB  . GLU   A 1 114 ? -27.365 -12.639 -12.545 1.00 26.18  ? 651  GLU   A CB  1 
ATOM   711  C CG  . GLU   A 1 114 ? -26.722 -12.363 -11.174 1.00 34.78  ? 651  GLU   A CG  1 
ATOM   712  C CD  . GLU   A 1 114 ? -27.255 -11.125 -10.472 1.00 51.62  ? 651  GLU   A CD  1 
ATOM   713  O OE1 . GLU   A 1 114 ? -27.786 -10.219 -11.155 1.00 55.21  ? 651  GLU   A OE1 1 
ATOM   714  O OE2 . GLU   A 1 114 ? -27.135 -11.066 -9.226  1.00 59.08  ? 651  GLU   A OE2 1 
ATOM   715  N N   . ILE   A 1 115 ? -27.151 -15.505 -14.912 1.00 25.68  ? 652  ILE   A N   1 
ATOM   716  C CA  . ILE   A 1 115 ? -27.577 -15.994 -16.214 1.00 22.95  ? 652  ILE   A CA  1 
ATOM   717  C C   . ILE   A 1 115 ? -29.029 -16.455 -16.161 1.00 24.92  ? 652  ILE   A C   1 
ATOM   718  O O   . ILE   A 1 115 ? -29.370 -17.322 -15.365 1.00 26.39  ? 652  ILE   A O   1 
ATOM   719  C CB  . ILE   A 1 115 ? -26.692 -17.153 -16.678 1.00 25.50  ? 652  ILE   A CB  1 
ATOM   720  C CG1 . ILE   A 1 115 ? -25.214 -16.725 -16.619 1.00 24.27  ? 652  ILE   A CG1 1 
ATOM   721  C CG2 . ILE   A 1 115 ? -27.087 -17.614 -18.087 1.00 26.60  ? 652  ILE   A CG2 1 
ATOM   722  C CD1 . ILE   A 1 115 ? -24.232 -17.869 -16.694 1.00 23.40  ? 652  ILE   A CD1 1 
ATOM   723  N N   . PRO   A 1 116 ? -29.892 -15.867 -17.007 1.00 27.32  ? 653  PRO   A N   1 
ATOM   724  C CA  . PRO   A 1 116 ? -31.283 -16.326 -17.066 1.00 26.97  ? 653  PRO   A CA  1 
ATOM   725  C C   . PRO   A 1 116 ? -31.382 -17.601 -17.904 1.00 29.29  ? 653  PRO   A C   1 
ATOM   726  O O   . PRO   A 1 116 ? -30.592 -17.785 -18.834 1.00 27.09  ? 653  PRO   A O   1 
ATOM   727  C CB  . PRO   A 1 116 ? -32.012 -15.161 -17.740 1.00 32.37  ? 653  PRO   A CB  1 
ATOM   728  C CG  . PRO   A 1 116 ? -30.961 -14.571 -18.645 1.00 33.72  ? 653  PRO   A CG  1 
ATOM   729  C CD  . PRO   A 1 116 ? -29.631 -14.747 -17.931 1.00 26.75  ? 653  PRO   A CD  1 
ATOM   730  N N   . GLU   A 1 117 ? -32.323 -18.480 -17.581 1.00 26.80  ? 654  GLU   A N   1 
ATOM   731  C CA  . GLU   A 1 117 ? -32.492 -19.684 -18.385 1.00 30.19  ? 654  GLU   A CA  1 
ATOM   732  C C   . GLU   A 1 117 ? -33.389 -19.335 -19.574 1.00 28.48  ? 654  GLU   A C   1 
ATOM   733  O O   . GLU   A 1 117 ? -34.247 -18.456 -19.459 1.00 28.71  ? 654  GLU   A O   1 
ATOM   734  C CB  . GLU   A 1 117 ? -33.083 -20.828 -17.542 1.00 30.60  ? 654  GLU   A CB  1 
ATOM   735  C CG  . GLU   A 1 117 ? -32.219 -21.142 -16.326 1.00 32.93  ? 654  GLU   A CG  1 
ATOM   736  C CD  . GLU   A 1 117 ? -32.655 -22.356 -15.543 1.00 36.85  ? 654  GLU   A CD  1 
ATOM   737  O OE1 . GLU   A 1 117 ? -33.849 -22.734 -15.597 1.00 32.77  ? 654  GLU   A OE1 1 
ATOM   738  O OE2 . GLU   A 1 117 ? -31.781 -22.923 -14.846 1.00 37.42  ? 654  GLU   A OE2 1 
ATOM   739  N N   . PRO   A 1 118 ? -33.185 -20.007 -20.719 1.00 27.63  ? 655  PRO   A N   1 
ATOM   740  C CA  . PRO   A 1 118 ? -34.044 -19.774 -21.885 1.00 29.51  ? 655  PRO   A CA  1 
ATOM   741  C C   . PRO   A 1 118 ? -35.513 -19.999 -21.531 1.00 32.57  ? 655  PRO   A C   1 
ATOM   742  O O   . PRO   A 1 118 ? -35.788 -20.811 -20.648 1.00 36.32  ? 655  PRO   A O   1 
ATOM   743  C CB  . PRO   A 1 118 ? -33.592 -20.835 -22.902 1.00 34.63  ? 655  PRO   A CB  1 
ATOM   744  C CG  . PRO   A 1 118 ? -32.314 -21.408 -22.374 1.00 34.39  ? 655  PRO   A CG  1 
ATOM   745  C CD  . PRO   A 1 118 ? -32.266 -21.144 -20.903 1.00 32.11  ? 655  PRO   A CD  1 
ATOM   746  N N   . GLU   A 1 119 ? -36.420 -19.310 -22.216 1.00 32.81  ? 656  GLU   A N   1 
ATOM   747  C CA  . GLU   A 1 119 ? -37.856 -19.556 -22.083 1.00 39.51  ? 656  GLU   A CA  1 
ATOM   748  C C   . GLU   A 1 119 ? -38.182 -21.031 -22.317 1.00 37.85  ? 656  GLU   A C   1 
ATOM   749  O O   . GLU   A 1 119 ? -37.813 -21.580 -23.347 1.00 34.32  ? 656  GLU   A O   1 
ATOM   750  C CB  . GLU   A 1 119 ? -38.634 -18.701 -23.084 1.00 54.48  ? 656  GLU   A CB  1 
ATOM   751  C CG  . GLU   A 1 119 ? -39.746 -17.868 -22.484 1.00 76.72  ? 656  GLU   A CG  1 
ATOM   752  C CD  . GLU   A 1 119 ? -39.216 -16.702 -21.673 1.00 90.02  ? 656  GLU   A CD  1 
ATOM   753  O OE1 . GLU   A 1 119 ? -39.001 -15.617 -22.257 1.00 87.35  ? 656  GLU   A OE1 1 
ATOM   754  O OE2 . GLU   A 1 119 ? -39.008 -16.873 -20.451 1.00 96.82  ? 656  GLU   A OE2 1 
ATOM   755  N N   . PRO   A 1 120 ? -38.874 -21.679 -21.367 1.00 40.31  ? 657  PRO   A N   1 
ATOM   756  C CA  . PRO   A 1 120 ? -39.291 -23.065 -21.613 1.00 39.24  ? 657  PRO   A CA  1 
ATOM   757  C C   . PRO   A 1 120 ? -40.130 -23.196 -22.881 1.00 39.75  ? 657  PRO   A C   1 
ATOM   758  O O   . PRO   A 1 120 ? -40.960 -22.337 -23.170 1.00 37.79  ? 657  PRO   A O   1 
ATOM   759  C CB  . PRO   A 1 120 ? -40.114 -23.409 -20.368 1.00 48.23  ? 657  PRO   A CB  1 
ATOM   760  C CG  . PRO   A 1 120 ? -39.495 -22.561 -19.292 1.00 55.25  ? 657  PRO   A CG  1 
ATOM   761  C CD  . PRO   A 1 120 ? -39.153 -21.258 -19.982 1.00 50.91  ? 657  PRO   A CD  1 
ATOM   762  N N   . THR   A 1 121 ? -39.890 -24.253 -23.642 1.00 39.54  ? 658  THR   A N   1 
ATOM   763  C CA  . THR   A 1 121 ? -40.651 -24.496 -24.855 1.00 48.60  ? 658  THR   A CA  1 
ATOM   764  C C   . THR   A 1 121 ? -42.050 -24.996 -24.477 1.00 48.90  ? 658  THR   A C   1 
ATOM   765  O O   . THR   A 1 121 ? -42.318 -25.272 -23.305 1.00 51.78  ? 658  THR   A O   1 
ATOM   766  C CB  . THR   A 1 121 ? -39.936 -25.513 -25.760 1.00 56.42  ? 658  THR   A CB  1 
ATOM   767  O OG1 . THR   A 1 121 ? -40.357 -25.335 -27.117 1.00 81.54  ? 658  THR   A OG1 1 
ATOM   768  C CG2 . THR   A 1 121 ? -40.250 -26.914 -25.317 1.00 32.66  ? 658  THR   A CG2 1 
ATOM   769  N N   . ASP   A 1 122 ? -42.947 -25.092 -25.452 1.00 41.70  ? 659  ASP   A N   1 
ATOM   770  C CA  . ASP   A 1 122 ? -44.303 -25.561 -25.164 1.00 50.50  ? 659  ASP   A CA  1 
ATOM   771  C C   . ASP   A 1 122 ? -44.296 -26.985 -24.614 1.00 49.65  ? 659  ASP   A C   1 
ATOM   772  O O   . ASP   A 1 122 ? -45.037 -27.297 -23.679 1.00 53.11  ? 659  ASP   A O   1 
ATOM   773  C CB  . ASP   A 1 122 ? -45.181 -25.483 -26.413 1.00 60.45  ? 659  ASP   A CB  1 
ATOM   774  C CG  . ASP   A 1 122 ? -45.619 -24.064 -26.726 1.00 71.73  ? 659  ASP   A CG  1 
ATOM   775  O OD1 . ASP   A 1 122 ? -45.633 -23.228 -25.791 1.00 74.53  ? 659  ASP   A OD1 1 
ATOM   776  O OD2 . ASP   A 1 122 ? -45.951 -23.786 -27.901 1.00 70.65  ? 659  ASP   A OD2 1 
ATOM   777  N N   . ALA   A 1 123 ? -43.459 -27.843 -25.189 1.00 53.05  ? 660  ALA   A N   1 
ATOM   778  C CA  . ALA   A 1 123 ? -43.331 -29.215 -24.705 1.00 54.87  ? 660  ALA   A CA  1 
ATOM   779  C C   . ALA   A 1 123 ? -42.732 -29.258 -23.293 1.00 53.27  ? 660  ALA   A C   1 
ATOM   780  O O   . ALA   A 1 123 ? -43.145 -30.072 -22.466 1.00 49.67  ? 660  ALA   A O   1 
ATOM   781  C CB  . ALA   A 1 123 ? -42.493 -30.037 -25.665 1.00 52.36  ? 660  ALA   A CB  1 
ATOM   782  N N   . ASP   A 1 124 ? -41.768 -28.378 -23.026 1.00 44.10  ? 661  ASP   A N   1 
ATOM   783  C CA  . ASP   A 1 124 ? -41.197 -28.226 -21.689 1.00 39.14  ? 661  ASP   A CA  1 
ATOM   784  C C   . ASP   A 1 124 ? -42.287 -27.930 -20.666 1.00 49.45  ? 661  ASP   A C   1 
ATOM   785  O O   . ASP   A 1 124 ? -42.314 -28.514 -19.579 1.00 46.26  ? 661  ASP   A O   1 
ATOM   786  C CB  . ASP   A 1 124 ? -40.166 -27.093 -21.646 1.00 38.91  ? 661  ASP   A CB  1 
ATOM   787  C CG  . ASP   A 1 124 ? -38.905 -27.404 -22.434 1.00 45.10  ? 661  ASP   A CG  1 
ATOM   788  O OD1 . ASP   A 1 124 ? -38.766 -28.552 -22.906 1.00 42.00  ? 661  ASP   A OD1 1 
ATOM   789  O OD2 . ASP   A 1 124 ? -38.060 -26.484 -22.584 1.00 36.31  ? 661  ASP   A OD2 1 
ATOM   790  N N   . LYS   A 1 125 ? -43.169 -26.997 -21.021 1.00 46.24  ? 662  LYS   A N   1 
ATOM   791  C CA  . LYS   A 1 125 ? -44.230 -26.543 -20.124 1.00 48.88  ? 662  LYS   A CA  1 
ATOM   792  C C   . LYS   A 1 125 ? -45.216 -27.661 -19.801 1.00 51.62  ? 662  LYS   A C   1 
ATOM   793  O O   . LYS   A 1 125 ? -45.720 -27.756 -18.677 1.00 55.19  ? 662  LYS   A O   1 
ATOM   794  C CB  . LYS   A 1 125 ? -44.964 -25.344 -20.732 1.00 52.46  ? 662  LYS   A CB  1 
ATOM   795  C CG  . LYS   A 1 125 ? -44.176 -24.046 -20.613 1.00 56.51  ? 662  LYS   A CG  1 
ATOM   796  C CD  . LYS   A 1 125 ? -44.844 -22.880 -21.325 1.00 56.63  ? 662  LYS   A CD  1 
ATOM   797  C CE  . LYS   A 1 125 ? -43.974 -21.626 -21.196 1.00 62.52  ? 662  LYS   A CE  1 
ATOM   798  N NZ  . LYS   A 1 125 ? -44.532 -20.463 -21.952 1.00 66.57  ? 662  LYS   A NZ  1 
ATOM   799  N N   . LEU   A 1 126 ? -45.495 -28.502 -20.792 1.00 54.98  ? 663  LEU   A N   1 
ATOM   800  C CA  . LEU   A 1 126 ? -46.332 -29.678 -20.585 1.00 54.54  ? 663  LEU   A CA  1 
ATOM   801  C C   . LEU   A 1 126 ? -45.726 -30.629 -19.554 1.00 59.41  ? 663  LEU   A C   1 
ATOM   802  O O   . LEU   A 1 126 ? -46.395 -31.042 -18.606 1.00 59.13  ? 663  LEU   A O   1 
ATOM   803  C CB  . LEU   A 1 126 ? -46.538 -30.422 -21.905 1.00 57.51  ? 663  LEU   A CB  1 
ATOM   804  C CG  . LEU   A 1 126 ? -47.729 -30.022 -22.770 1.00 62.57  ? 663  LEU   A CG  1 
ATOM   805  C CD1 . LEU   A 1 126 ? -47.618 -30.678 -24.139 1.00 67.29  ? 663  LEU   A CD1 1 
ATOM   806  C CD2 . LEU   A 1 126 ? -49.023 -30.421 -22.079 1.00 60.01  ? 663  LEU   A CD2 1 
ATOM   807  N N   . ALA   A 1 127 ? -44.457 -30.975 -19.764 1.00 54.36  ? 664  ALA   A N   1 
ATOM   808  C CA  . ALA   A 1 127 ? -43.739 -31.913 -18.904 1.00 54.98  ? 664  ALA   A CA  1 
ATOM   809  C C   . ALA   A 1 127 ? -43.657 -31.422 -17.457 1.00 57.98  ? 664  ALA   A C   1 
ATOM   810  O O   . ALA   A 1 127 ? -43.822 -32.202 -16.518 1.00 52.55  ? 664  ALA   A O   1 
ATOM   811  C CB  . ALA   A 1 127 ? -42.334 -32.165 -19.456 1.00 51.78  ? 664  ALA   A CB  1 
ATOM   812  N N   . ILE   A 1 128 ? -43.396 -30.129 -17.283 1.00 52.35  ? 665  ILE   A N   1 
ATOM   813  C CA  . ILE   A 1 128 ? -43.346 -29.527 -15.953 1.00 55.14  ? 665  ILE   A CA  1 
ATOM   814  C C   . ILE   A 1 128 ? -44.700 -29.633 -15.245 1.00 62.07  ? 665  ILE   A C   1 
ATOM   815  O O   . ILE   A 1 128 ? -44.781 -30.047 -14.086 1.00 63.87  ? 665  ILE   A O   1 
ATOM   816  C CB  . ILE   A 1 128 ? -42.907 -28.050 -16.037 1.00 53.16  ? 665  ILE   A CB  1 
ATOM   817  C CG1 . ILE   A 1 128 ? -41.420 -27.973 -16.395 1.00 48.69  ? 665  ILE   A CG1 1 
ATOM   818  C CG2 . ILE   A 1 128 ? -43.201 -27.327 -14.730 1.00 62.97  ? 665  ILE   A CG2 1 
ATOM   819  C CD1 . ILE   A 1 128 ? -40.915 -26.571 -16.679 1.00 47.04  ? 665  ILE   A CD1 1 
ATOM   820  N N   . GLU   A 1 129 ? -45.763 -29.291 -15.962 1.00 55.06  ? 666  GLU   A N   1 
ATOM   821  C CA  . GLU   A 1 129 ? -47.102 -29.313 -15.398 1.00 66.10  ? 666  GLU   A CA  1 
ATOM   822  C C   . GLU   A 1 129 ? -47.572 -30.740 -15.112 1.00 70.23  ? 666  GLU   A C   1 
ATOM   823  O O   . GLU   A 1 129 ? -48.302 -30.977 -14.149 1.00 72.57  ? 666  GLU   A O   1 
ATOM   824  C CB  . GLU   A 1 129 ? -48.077 -28.614 -16.340 1.00 71.75  ? 666  GLU   A CB  1 
ATOM   825  C CG  . GLU   A 1 129 ? -49.424 -28.297 -15.710 1.00 79.66  ? 666  GLU   A CG  1 
ATOM   826  C CD  . GLU   A 1 129 ? -50.027 -27.022 -16.266 1.00 85.18  ? 666  GLU   A CD  1 
ATOM   827  O OE1 . GLU   A 1 129 ? -51.249 -27.016 -16.542 1.00 82.94  ? 666  GLU   A OE1 1 
ATOM   828  O OE2 . GLU   A 1 129 ? -49.271 -26.032 -16.430 1.00 85.71  ? 666  GLU   A OE2 1 
ATOM   829  N N   . LYS   A 1 130 ? -47.149 -31.684 -15.951 1.00 64.84  ? 667  LYS   A N   1 
ATOM   830  C CA  . LYS   A 1 130 ? -47.455 -33.098 -15.741 1.00 66.00  ? 667  LYS   A CA  1 
ATOM   831  C C   . LYS   A 1 130 ? -46.901 -33.565 -14.392 1.00 71.07  ? 667  LYS   A C   1 
ATOM   832  O O   . LYS   A 1 130 ? -47.539 -34.350 -13.681 1.00 70.52  ? 667  LYS   A O   1 
ATOM   833  C CB  . LYS   A 1 130 ? -46.885 -33.950 -16.881 1.00 56.08  ? 667  LYS   A CB  1 
ATOM   834  C CG  . LYS   A 1 130 ? -47.102 -35.450 -16.713 1.00 57.78  ? 667  LYS   A CG  1 
ATOM   835  C CD  . LYS   A 1 130 ? -46.564 -36.246 -17.897 1.00 52.16  ? 667  LYS   A CD  1 
ATOM   836  C CE  . LYS   A 1 130 ? -46.785 -37.737 -17.685 1.00 61.29  ? 667  LYS   A CE  1 
ATOM   837  N NZ  . LYS   A 1 130 ? -46.813 -38.509 -18.962 1.00 60.45  ? 667  LYS   A NZ  1 
ATOM   838  N N   . GLY   A 1 131 ? -45.717 -33.062 -14.047 1.00 64.49  ? 668  GLY   A N   1 
ATOM   839  C CA  . GLY   A 1 131 ? -45.087 -33.358 -12.774 1.00 68.79  ? 668  GLY   A CA  1 
ATOM   840  C C   . GLY   A 1 131 ? -44.175 -34.571 -12.799 1.00 69.60  ? 668  GLY   A C   1 
ATOM   841  O O   . GLY   A 1 131 ? -44.417 -35.527 -13.545 1.00 67.20  ? 668  GLY   A O   1 
ATOM   842  N N   . GLU   A 1 132 ? -43.124 -34.522 -11.980 1.00 63.91  ? 669  GLU   A N   1 
ATOM   843  C CA  . GLU   A 1 132 ? -42.207 -35.651 -11.788 1.00 70.13  ? 669  GLU   A CA  1 
ATOM   844  C C   . GLU   A 1 132 ? -41.536 -36.104 -13.085 1.00 71.30  ? 669  GLU   A C   1 
ATOM   845  O O   . GLU   A 1 132 ? -41.159 -37.272 -13.227 1.00 67.69  ? 669  GLU   A O   1 
ATOM   846  C CB  . GLU   A 1 132 ? -42.937 -36.840 -11.145 1.00 73.17  ? 669  GLU   A CB  1 
ATOM   847  C CG  . GLU   A 1 132 ? -42.917 -36.848 -9.620  1.00 68.04  ? 669  GLU   A CG  1 
ATOM   848  C CD  . GLU   A 1 132 ? -43.539 -38.108 -9.040  1.00 78.39  ? 669  GLU   A CD  1 
ATOM   849  O OE1 . GLU   A 1 132 ? -44.710 -38.406 -9.375  1.00 81.61  ? 669  GLU   A OE1 1 
ATOM   850  O OE2 . GLU   A 1 132 ? -42.854 -38.807 -8.260  1.00 82.72  ? 669  GLU   A OE2 1 
ATOM   851  N N   . GLN   A 1 133 ? -41.398 -35.176 -14.026 1.00 60.37  ? 670  GLN   A N   1 
ATOM   852  C CA  . GLN   A 1 133 ? -40.655 -35.428 -15.254 1.00 57.04  ? 670  GLN   A CA  1 
ATOM   853  C C   . GLN   A 1 133 ? -39.281 -34.782 -15.130 1.00 56.15  ? 670  GLN   A C   1 
ATOM   854  O O   . GLN   A 1 133 ? -39.151 -33.725 -14.505 1.00 60.86  ? 670  GLN   A O   1 
ATOM   855  C CB  . GLN   A 1 133 ? -41.390 -34.864 -16.475 1.00 54.24  ? 670  GLN   A CB  1 
ATOM   856  C CG  . GLN   A 1 133 ? -42.845 -35.274 -16.581 1.00 56.54  ? 670  GLN   A CG  1 
ATOM   857  C CD  . GLN   A 1 133 ? -43.016 -36.768 -16.759 1.00 65.10  ? 670  GLN   A CD  1 
ATOM   858  O OE1 . GLN   A 1 133 ? -43.815 -37.394 -16.064 1.00 68.81  ? 670  GLN   A OE1 1 
ATOM   859  N NE2 . GLN   A 1 133 ? -42.267 -37.347 -17.695 1.00 58.57  ? 670  GLN   A NE2 1 
ATOM   860  N N   . PRO   A 1 134 ? -38.252 -35.411 -15.720 1.00 54.39  ? 671  PRO   A N   1 
ATOM   861  C CA  . PRO   A 1 134 ? -36.930 -34.770 -15.739 1.00 57.74  ? 671  PRO   A CA  1 
ATOM   862  C C   . PRO   A 1 134 ? -36.992 -33.462 -16.519 1.00 55.67  ? 671  PRO   A C   1 
ATOM   863  O O   . PRO   A 1 134 ? -37.848 -33.341 -17.401 1.00 58.40  ? 671  PRO   A O   1 
ATOM   864  C CB  . PRO   A 1 134 ? -36.043 -35.798 -16.449 1.00 51.45  ? 671  PRO   A CB  1 
ATOM   865  C CG  . PRO   A 1 134 ? -36.996 -36.617 -17.273 1.00 57.28  ? 671  PRO   A CG  1 
ATOM   866  C CD  . PRO   A 1 134 ? -38.271 -36.679 -16.474 1.00 57.41  ? 671  PRO   A CD  1 
ATOM   867  N N   . ILE   A 1 135 ? -36.122 -32.504 -16.200 1.00 57.92  ? 672  ILE   A N   1 
ATOM   868  C CA  . ILE   A 1 135 ? -36.027 -31.266 -16.975 1.00 45.42  ? 672  ILE   A CA  1 
ATOM   869  C C   . ILE   A 1 135 ? -35.625 -31.608 -18.415 1.00 43.35  ? 672  ILE   A C   1 
ATOM   870  O O   . ILE   A 1 135 ? -35.146 -32.716 -18.674 1.00 42.11  ? 672  ILE   A O   1 
ATOM   871  C CB  . ILE   A 1 135 ? -35.014 -30.284 -16.362 1.00 43.14  ? 672  ILE   A CB  1 
ATOM   872  C CG1 . ILE   A 1 135 ? -33.609 -30.877 -16.403 1.00 47.97  ? 672  ILE   A CG1 1 
ATOM   873  C CG2 . ILE   A 1 135 ? -35.396 -29.945 -14.926 1.00 49.31  ? 672  ILE   A CG2 1 
ATOM   874  C CD1 . ILE   A 1 135 ? -32.554 -29.990 -15.792 1.00 51.57  ? 672  ILE   A CD1 1 
ATOM   875  N N   . SER   A 1 136 ? -35.821 -30.680 -19.351 1.00 36.75  ? 673  SER   A N   1 
ATOM   876  C CA  . SER   A 1 136 ? -35.539 -30.977 -20.755 1.00 35.46  ? 673  SER   A CA  1 
ATOM   877  C C   . SER   A 1 136 ? -34.053 -31.254 -20.949 1.00 33.54  ? 673  SER   A C   1 
ATOM   878  O O   . SER   A 1 136 ? -33.216 -30.740 -20.203 1.00 36.11  ? 673  SER   A O   1 
ATOM   879  C CB  . SER   A 1 136 ? -35.969 -29.826 -21.662 1.00 32.57  ? 673  SER   A CB  1 
ATOM   880  O OG  . SER   A 1 136 ? -35.010 -28.785 -21.612 1.00 31.57  ? 673  SER   A OG  1 
ATOM   881  N N   . ALA   A 1 137 ? -33.730 -32.071 -21.946 1.00 33.64  ? 674  ALA   A N   1 
ATOM   882  C CA  . ALA   A 1 137 ? -32.337 -32.350 -22.282 1.00 30.13  ? 674  ALA   A CA  1 
ATOM   883  C C   . ALA   A 1 137 ? -31.565 -31.062 -22.576 1.00 30.64  ? 674  ALA   A C   1 
ATOM   884  O O   . ALA   A 1 137 ? -30.401 -30.927 -22.175 1.00 29.79  ? 674  ALA   A O   1 
ATOM   885  C CB  . ALA   A 1 137 ? -32.264 -33.308 -23.475 1.00 35.81  ? 674  ALA   A CB  1 
ATOM   886  N N   . ASP   A 1 138 ? -32.207 -30.111 -23.254 1.00 28.28  ? 675  ASP   A N   1 
ATOM   887  C CA  . ASP   A 1 138 ? -31.559 -28.845 -23.590 1.00 24.91  ? 675  ASP   A CA  1 
ATOM   888  C C   . ASP   A 1 138 ? -31.273 -28.036 -22.337 1.00 26.22  ? 675  ASP   A C   1 
ATOM   889  O O   . ASP   A 1 138 ? -30.234 -27.389 -22.232 1.00 26.13  ? 675  ASP   A O   1 
ATOM   890  C CB  . ASP   A 1 138 ? -32.422 -28.015 -24.550 1.00 31.19  ? 675  ASP   A CB  1 
ATOM   891  C CG  . ASP   A 1 138 ? -32.261 -28.438 -26.009 1.00 47.77  ? 675  ASP   A CG  1 
ATOM   892  O OD1 . ASP   A 1 138 ? -31.360 -29.258 -26.303 1.00 45.13  ? 675  ASP   A OD1 1 
ATOM   893  O OD2 . ASP   A 1 138 ? -33.032 -27.940 -26.863 1.00 40.58  ? 675  ASP   A OD2 1 
ATOM   894  N N   . LEU   A 1 139 ? -32.193 -28.072 -21.377 1.00 25.84  ? 676  LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 139 ? -32.003 -27.284 -20.159 1.00 25.04  ? 676  LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 139 ? -30.906 -27.909 -19.309 1.00 26.99  ? 676  LEU   A C   1 
ATOM   897  O O   . LEU   A 1 139 ? -30.088 -27.193 -18.718 1.00 26.10  ? 676  LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 139 ? -33.311 -27.169 -19.356 1.00 26.94  ? 676  LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 139 ? -33.220 -26.304 -18.088 1.00 28.16  ? 676  LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 139 ? -32.704 -24.901 -18.412 1.00 33.90  ? 676  LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 139 ? -34.573 -26.234 -17.352 1.00 32.27  ? 676  LEU   A CD2 1 
ATOM   902  N N   . LYS   A 1 140 ? -30.880 -29.242 -19.263 1.00 29.99  ? 677  LYS   A N   1 
ATOM   903  C CA  . LYS   A 1 140 ? -29.825 -29.958 -18.537 1.00 29.05  ? 677  LYS   A CA  1 
ATOM   904  C C   . LYS   A 1 140 ? -28.440 -29.585 -19.101 1.00 27.96  ? 677  LYS   A C   1 
ATOM   905  O O   . LYS   A 1 140 ? -27.518 -29.254 -18.354 1.00 28.98  ? 677  LYS   A O   1 
ATOM   906  C CB  . LYS   A 1 140 ? -30.044 -31.477 -18.616 1.00 30.51  ? 677  LYS   A CB  1 
ATOM   907  C CG  . LYS   A 1 140 ? -29.097 -32.287 -17.724 1.00 35.28  ? 677  LYS   A CG  1 
ATOM   908  C CD  . LYS   A 1 140 ? -29.328 -33.799 -17.819 1.00 52.78  ? 677  LYS   A CD  1 
ATOM   909  C CE  . LYS   A 1 140 ? -28.312 -34.573 -16.961 1.00 56.97  ? 677  LYS   A CE  1 
ATOM   910  N NZ  . LYS   A 1 140 ? -28.524 -36.049 -16.992 1.00 60.89  ? 677  LYS   A NZ  1 
ATOM   911  N N   . ARG   A 1 141 ? -28.305 -29.619 -20.427 1.00 26.09  ? 678  ARG   A N   1 
ATOM   912  C CA  . ARG   A 1 141 ? -27.037 -29.255 -21.073 1.00 28.85  ? 678  ARG   A CA  1 
ATOM   913  C C   . ARG   A 1 141 ? -26.632 -27.826 -20.766 1.00 25.61  ? 678  ARG   A C   1 
ATOM   914  O O   . ARG   A 1 141 ? -25.464 -27.542 -20.489 1.00 26.17  ? 678  ARG   A O   1 
ATOM   915  C CB  . ARG   A 1 141 ? -27.126 -29.416 -22.595 1.00 27.88  ? 678  ARG   A CB  1 
ATOM   916  C CG  . ARG   A 1 141 ? -27.053 -30.838 -23.118 1.00 33.46  ? 678  ARG   A CG  1 
ATOM   917  C CD  . ARG   A 1 141 ? -26.750 -30.811 -24.618 1.00 39.31  ? 678  ARG   A CD  1 
ATOM   918  N NE  . ARG   A 1 141 ? -25.403 -30.303 -24.899 1.00 41.69  ? 678  ARG   A NE  1 
ATOM   919  C CZ  . ARG   A 1 141 ? -25.028 -29.770 -26.063 1.00 42.74  ? 678  ARG   A CZ  1 
ATOM   920  N NH1 . ARG   A 1 141 ? -25.902 -29.638 -27.053 1.00 31.09  ? 678  ARG   A NH1 1 
ATOM   921  N NH2 . ARG   A 1 141 ? -23.780 -29.345 -26.234 1.00 42.58  ? 678  ARG   A NH2 1 
ATOM   922  N N   . PHE   A 1 142 ? -27.600 -26.921 -20.842 1.00 24.49  ? 679  PHE   A N   1 
ATOM   923  C CA  . PHE   A 1 142 ? -27.337 -25.506 -20.587 1.00 22.31  ? 679  PHE   A CA  1 
ATOM   924  C C   . PHE   A 1 142 ? -26.810 -25.313 -19.156 1.00 24.48  ? 679  PHE   A C   1 
ATOM   925  O O   . PHE   A 1 142 ? -25.803 -24.639 -18.938 1.00 26.03  ? 679  PHE   A O   1 
ATOM   926  C CB  . PHE   A 1 142 ? -28.607 -24.693 -20.836 1.00 22.81  ? 679  PHE   A CB  1 
ATOM   927  C CG  . PHE   A 1 142 ? -28.480 -23.250 -20.482 1.00 25.51  ? 679  PHE   A CG  1 
ATOM   928  C CD1 . PHE   A 1 142 ? -27.705 -22.406 -21.259 1.00 27.75  ? 679  PHE   A CD1 1 
ATOM   929  C CD2 . PHE   A 1 142 ? -29.149 -22.732 -19.382 1.00 27.89  ? 679  PHE   A CD2 1 
ATOM   930  C CE1 . PHE   A 1 142 ? -27.582 -21.061 -20.934 1.00 31.28  ? 679  PHE   A CE1 1 
ATOM   931  C CE2 . PHE   A 1 142 ? -29.035 -21.384 -19.061 1.00 26.95  ? 679  PHE   A CE2 1 
ATOM   932  C CZ  . PHE   A 1 142 ? -28.249 -20.556 -19.836 1.00 25.08  ? 679  PHE   A CZ  1 
ATOM   933  N N   . ARG   A 1 143 ? -27.460 -25.934 -18.179 1.00 24.82  ? 680  ARG   A N   1 
ATOM   934  C CA  . ARG   A 1 143 ? -27.030 -25.766 -16.791 1.00 24.41  ? 680  ARG   A CA  1 
ATOM   935  C C   . ARG   A 1 143 ? -25.632 -26.345 -16.558 1.00 26.05  ? 680  ARG   A C   1 
ATOM   936  O O   . ARG   A 1 143 ? -24.818 -25.762 -15.851 1.00 27.97  ? 680  ARG   A O   1 
ATOM   937  C CB  . ARG   A 1 143 ? -28.031 -26.413 -15.838 1.00 28.34  ? 680  ARG   A CB  1 
ATOM   938  C CG  . ARG   A 1 143 ? -29.363 -25.694 -15.763 1.00 27.30  ? 680  ARG   A CG  1 
ATOM   939  C CD  . ARG   A 1 143 ? -30.282 -26.374 -14.763 1.00 28.19  ? 680  ARG   A CD  1 
ATOM   940  N NE  . ARG   A 1 143 ? -31.530 -25.639 -14.583 1.00 33.36  ? 680  ARG   A NE  1 
ATOM   941  C CZ  . ARG   A 1 143 ? -32.612 -26.138 -13.987 1.00 39.03  ? 680  ARG   A CZ  1 
ATOM   942  N NH1 . ARG   A 1 143 ? -32.603 -27.374 -13.506 1.00 38.05  ? 680  ARG   A NH1 1 
ATOM   943  N NH2 . ARG   A 1 143 ? -33.709 -25.401 -13.879 1.00 38.32  ? 680  ARG   A NH2 1 
ATOM   944  N N   . LYS   A 1 144 ? -25.351 -27.470 -17.194 1.00 26.57  ? 681  LYS   A N   1 
ATOM   945  C CA  . LYS   A 1 144 ? -24.107 -28.191 -16.969 1.00 27.70  ? 681  LYS   A CA  1 
ATOM   946  C C   . LYS   A 1 144 ? -22.955 -27.637 -17.794 1.00 27.63  ? 681  LYS   A C   1 
ATOM   947  O O   . LYS   A 1 144 ? -21.834 -27.502 -17.308 1.00 28.86  ? 681  LYS   A O   1 
ATOM   948  C CB  . LYS   A 1 144 ? -24.307 -29.667 -17.298 1.00 30.68  ? 681  LYS   A CB  1 
ATOM   949  C CG  . LYS   A 1 144 ? -23.109 -30.552 -17.015 1.00 46.85  ? 681  LYS   A CG  1 
ATOM   950  C CD  . LYS   A 1 144 ? -23.534 -32.019 -17.063 1.00 62.94  ? 681  LYS   A CD  1 
ATOM   951  C CE  . LYS   A 1 144 ? -22.406 -32.966 -16.674 1.00 71.88  ? 681  LYS   A CE  1 
ATOM   952  N NZ  . LYS   A 1 144 ? -21.433 -33.146 -17.789 1.00 78.48  ? 681  LYS   A NZ  1 
ATOM   953  N N   . GLU   A 1 145 ? -23.223 -27.330 -19.058 1.00 25.87  ? 682  GLU   A N   1 
ATOM   954  C CA  . GLU   A 1 145 ? -22.143 -26.965 -19.969 1.00 22.90  ? 682  GLU   A CA  1 
ATOM   955  C C   . GLU   A 1 145 ? -21.956 -25.464 -20.109 1.00 28.58  ? 682  GLU   A C   1 
ATOM   956  O O   . GLU   A 1 145 ? -20.925 -25.016 -20.614 1.00 28.79  ? 682  GLU   A O   1 
ATOM   957  C CB  . GLU   A 1 145 ? -22.381 -27.578 -21.348 1.00 24.63  ? 682  GLU   A CB  1 
ATOM   958  C CG  . GLU   A 1 145 ? -22.439 -29.092 -21.307 1.00 28.19  ? 682  GLU   A CG  1 
ATOM   959  C CD  . GLU   A 1 145 ? -22.760 -29.684 -22.666 1.00 40.14  ? 682  GLU   A CD  1 
ATOM   960  O OE1 . GLU   A 1 145 ? -22.320 -29.109 -23.686 1.00 37.80  ? 682  GLU   A OE1 1 
ATOM   961  O OE2 . GLU   A 1 145 ? -23.467 -30.710 -22.713 1.00 44.48  ? 682  GLU   A OE2 1 
ATOM   962  N N   . TYR   A 1 146 ? -22.928 -24.678 -19.661 1.00 22.51  ? 683  TYR   A N   1 
ATOM   963  C CA  . TYR   A 1 146 ? -22.804 -23.226 -19.805 1.00 21.45  ? 683  TYR   A CA  1 
ATOM   964  C C   . TYR   A 1 146 ? -22.822 -22.525 -18.463 1.00 25.16  ? 683  TYR   A C   1 
ATOM   965  O O   . TYR   A 1 146 ? -21.847 -21.891 -18.069 1.00 26.79  ? 683  TYR   A O   1 
ATOM   966  C CB  . TYR   A 1 146 ? -23.922 -22.656 -20.697 1.00 20.42  ? 683  TYR   A CB  1 
ATOM   967  C CG  . TYR   A 1 146 ? -23.659 -21.215 -21.105 1.00 22.54  ? 683  TYR   A CG  1 
ATOM   968  C CD1 . TYR   A 1 146 ? -22.919 -20.923 -22.258 1.00 24.90  ? 683  TYR   A CD1 1 
ATOM   969  C CD2 . TYR   A 1 146 ? -24.127 -20.148 -20.333 1.00 23.23  ? 683  TYR   A CD2 1 
ATOM   970  C CE1 . TYR   A 1 146 ? -22.655 -19.612 -22.631 1.00 23.97  ? 683  TYR   A CE1 1 
ATOM   971  C CE2 . TYR   A 1 146 ? -23.863 -18.809 -20.699 1.00 24.78  ? 683  TYR   A CE2 1 
ATOM   972  C CZ  . TYR   A 1 146 ? -23.132 -18.565 -21.852 1.00 25.47  ? 683  TYR   A CZ  1 
ATOM   973  O OH  . TYR   A 1 146 ? -22.869 -17.275 -22.233 1.00 23.79  ? 683  TYR   A OH  1 
ATOM   974  N N   . VAL   A 1 147 ? -23.934 -22.645 -17.746 1.00 25.68  ? 684  VAL   A N   1 
ATOM   975  C CA  . VAL   A 1 147 ? -24.090 -21.902 -16.503 1.00 27.68  ? 684  VAL   A CA  1 
ATOM   976  C C   . VAL   A 1 147 ? -23.009 -22.245 -15.470 1.00 27.09  ? 684  VAL   A C   1 
ATOM   977  O O   . VAL   A 1 147 ? -22.341 -21.352 -14.945 1.00 26.71  ? 684  VAL   A O   1 
ATOM   978  C CB  . VAL   A 1 147 ? -25.473 -22.144 -15.886 1.00 23.18  ? 684  VAL   A CB  1 
ATOM   979  C CG1 . VAL   A 1 147 ? -25.591 -21.427 -14.531 1.00 26.99  ? 684  VAL   A CG1 1 
ATOM   980  C CG2 . VAL   A 1 147 ? -26.552 -21.669 -16.841 1.00 23.09  ? 684  VAL   A CG2 1 
ATOM   981  N N   . GLN   A 1 148 ? -22.832 -23.525 -15.166 1.00 25.15  ? 685  GLN   A N   1 
ATOM   982  C CA  . GLN   A 1 148 ? -21.883 -23.878 -14.112 1.00 27.56  ? 685  GLN   A CA  1 
ATOM   983  C C   . GLN   A 1 148 ? -20.437 -23.506 -14.479 1.00 23.98  ? 685  GLN   A C   1 
ATOM   984  O O   . GLN   A 1 148 ? -19.753 -22.898 -13.666 1.00 27.18  ? 685  GLN   A O   1 
ATOM   985  C CB  . GLN   A 1 148 ? -21.980 -25.364 -13.742 1.00 37.11  ? 685  GLN   A CB  1 
ATOM   986  C CG  . GLN   A 1 148 ? -21.017 -25.758 -12.632 1.00 37.19  ? 685  GLN   A CG  1 
ATOM   987  C CD  . GLN   A 1 148 ? -21.386 -27.076 -11.967 1.00 48.54  ? 685  GLN   A CD  1 
ATOM   988  O OE1 . GLN   A 1 148 ? -22.352 -27.152 -11.208 1.00 55.72  ? 685  GLN   A OE1 1 
ATOM   989  N NE2 . GLN   A 1 148 ? -20.616 -28.113 -12.245 1.00 46.32  ? 685  GLN   A NE2 1 
ATOM   990  N N   . PRO   A 1 149 ? -19.971 -23.834 -15.697 1.00 26.84  ? 686  PRO   A N   1 
ATOM   991  C CA  . PRO   A 1 149 ? -18.613 -23.390 -16.037 1.00 28.33  ? 686  PRO   A CA  1 
ATOM   992  C C   . PRO   A 1 149 ? -18.426 -21.879 -15.999 1.00 30.41  ? 686  PRO   A C   1 
ATOM   993  O O   . PRO   A 1 149 ? -17.393 -21.443 -15.501 1.00 27.84  ? 686  PRO   A O   1 
ATOM   994  C CB  . PRO   A 1 149 ? -18.422 -23.891 -17.469 1.00 24.38  ? 686  PRO   A CB  1 
ATOM   995  C CG  . PRO   A 1 149 ? -19.324 -25.059 -17.572 1.00 32.57  ? 686  PRO   A CG  1 
ATOM   996  C CD  . PRO   A 1 149 ? -20.530 -24.700 -16.754 1.00 27.78  ? 686  PRO   A CD  1 
ATOM   997  N N   . VAL   A 1 150 ? -19.365 -21.105 -16.541 1.00 23.03  ? 687  VAL   A N   1 
ATOM   998  C CA  . VAL   A 1 150 ? -19.206 -19.649 -16.534 1.00 21.73  ? 687  VAL   A CA  1 
ATOM   999  C C   . VAL   A 1 150 ? -19.166 -19.138 -15.092 1.00 27.27  ? 687  VAL   A C   1 
ATOM   1000 O O   . VAL   A 1 150 ? -18.315 -18.313 -14.729 1.00 25.01  ? 687  VAL   A O   1 
ATOM   1001 C CB  . VAL   A 1 150 ? -20.338 -18.950 -17.315 1.00 21.33  ? 687  VAL   A CB  1 
ATOM   1002 C CG1 . VAL   A 1 150 ? -20.301 -17.434 -17.081 1.00 22.65  ? 687  VAL   A CG1 1 
ATOM   1003 C CG2 . VAL   A 1 150 ? -20.218 -19.257 -18.799 1.00 22.10  ? 687  VAL   A CG2 1 
ATOM   1004 N N   . GLN   A 1 151 ? -20.078 -19.628 -14.259 1.00 25.71  ? 688  GLN   A N   1 
ATOM   1005 C CA  . GLN   A 1 151 ? -20.134 -19.149 -12.879 1.00 26.29  ? 688  GLN   A CA  1 
ATOM   1006 C C   . GLN   A 1 151 ? -18.856 -19.486 -12.102 1.00 26.56  ? 688  GLN   A C   1 
ATOM   1007 O O   . GLN   A 1 151 ? -18.373 -18.661 -11.323 1.00 24.99  ? 688  GLN   A O   1 
ATOM   1008 C CB  . GLN   A 1 151 ? -21.373 -19.703 -12.170 1.00 24.97  ? 688  GLN   A CB  1 
ATOM   1009 C CG  . GLN   A 1 151 ? -22.618 -18.927 -12.576 1.00 22.47  ? 688  GLN   A CG  1 
ATOM   1010 C CD  . GLN   A 1 151 ? -23.886 -19.443 -11.960 1.00 28.57  ? 688  GLN   A CD  1 
ATOM   1011 O OE1 . GLN   A 1 151 ? -23.921 -20.538 -11.402 1.00 25.55  ? 688  GLN   A OE1 1 
ATOM   1012 N NE2 . GLN   A 1 151 ? -24.949 -18.648 -12.053 1.00 30.07  ? 688  GLN   A NE2 1 
ATOM   1013 N N   . LEU   A 1 152 ? -18.293 -20.667 -12.339 1.00 25.48  ? 689  LEU   A N   1 
ATOM   1014 C CA  . LEU   A 1 152 ? -17.026 -21.036 -11.707 1.00 26.99  ? 689  LEU   A CA  1 
ATOM   1015 C C   . LEU   A 1 152 ? -15.866 -20.180 -12.225 1.00 26.12  ? 689  LEU   A C   1 
ATOM   1016 O O   . LEU   A 1 152 ? -14.964 -19.813 -11.459 1.00 27.13  ? 689  LEU   A O   1 
ATOM   1017 C CB  . LEU   A 1 152 ? -16.719 -22.509 -11.939 1.00 29.55  ? 689  LEU   A CB  1 
ATOM   1018 C CG  . LEU   A 1 152 ? -17.638 -23.506 -11.232 1.00 33.77  ? 689  LEU   A CG  1 
ATOM   1019 C CD1 . LEU   A 1 152 ? -17.254 -24.928 -11.601 1.00 35.71  ? 689  LEU   A CD1 1 
ATOM   1020 C CD2 . LEU   A 1 152 ? -17.564 -23.288 -9.728  1.00 39.57  ? 689  LEU   A CD2 1 
ATOM   1021 N N   . ARG   A 1 153 ? -15.872 -19.872 -13.520 1.00 23.48  ? 690  ARG   A N   1 
ATOM   1022 C CA  . ARG   A 1 153 ? -14.831 -18.988 -14.061 1.00 25.31  ? 690  ARG   A CA  1 
ATOM   1023 C C   . ARG   A 1 153 ? -14.910 -17.589 -13.475 1.00 24.33  ? 690  ARG   A C   1 
ATOM   1024 O O   . ARG   A 1 153 ? -13.880 -16.934 -13.284 1.00 22.86  ? 690  ARG   A O   1 
ATOM   1025 C CB  . ARG   A 1 153 ? -14.908 -18.904 -15.579 1.00 27.84  ? 690  ARG   A CB  1 
ATOM   1026 C CG  . ARG   A 1 153 ? -14.808 -20.256 -16.230 1.00 41.94  ? 690  ARG   A CG  1 
ATOM   1027 C CD  . ARG   A 1 153 ? -13.594 -20.428 -17.077 1.00 41.25  ? 690  ARG   A CD  1 
ATOM   1028 N NE  . ARG   A 1 153 ? -13.793 -21.566 -17.958 1.00 49.54  ? 690  ARG   A NE  1 
ATOM   1029 C CZ  . ARG   A 1 153 ? -13.534 -22.820 -17.620 1.00 43.61  ? 690  ARG   A CZ  1 
ATOM   1030 N NH1 . ARG   A 1 153 ? -13.041 -23.094 -16.420 1.00 52.12  ? 690  ARG   A NH1 1 
ATOM   1031 N NH2 . ARG   A 1 153 ? -13.760 -23.799 -18.484 1.00 47.78  ? 690  ARG   A NH2 1 
ATOM   1032 N N   . ILE   A 1 154 ? -16.123 -17.114 -13.196 1.00 23.38  ? 691  ILE   A N   1 
ATOM   1033 C CA  . ILE   A 1 154 ? -16.277 -15.820 -12.540 1.00 24.08  ? 691  ILE   A CA  1 
ATOM   1034 C C   . ILE   A 1 154 ? -15.680 -15.864 -11.143 1.00 24.32  ? 691  ILE   A C   1 
ATOM   1035 O O   . ILE   A 1 154 ? -14.941 -14.954 -10.738 1.00 22.83  ? 691  ILE   A O   1 
ATOM   1036 C CB  . ILE   A 1 154 ? -17.760 -15.405 -12.465 1.00 23.88  ? 691  ILE   A CB  1 
ATOM   1037 C CG1 . ILE   A 1 154 ? -18.268 -15.129 -13.877 1.00 23.80  ? 691  ILE   A CG1 1 
ATOM   1038 C CG2 . ILE   A 1 154 ? -17.944 -14.179 -11.566 1.00 20.60  ? 691  ILE   A CG2 1 
ATOM   1039 C CD1 . ILE   A 1 154 ? -19.787 -15.070 -13.959 1.00 23.17  ? 691  ILE   A CD1 1 
ATOM   1040 N N   . LEU   A 1 155 ? -16.004 -16.911 -10.393 1.00 24.47  ? 692  LEU   A N   1 
ATOM   1041 C CA  . LEU   A 1 155 ? -15.443 -17.030 -9.045  1.00 24.92  ? 692  LEU   A CA  1 
ATOM   1042 C C   . LEU   A 1 155 ? -13.910 -17.128 -9.096  1.00 23.97  ? 692  LEU   A C   1 
ATOM   1043 O O   . LEU   A 1 155 ? -13.223 -16.580 -8.233  1.00 29.02  ? 692  LEU   A O   1 
ATOM   1044 C CB  . LEU   A 1 155 ? -16.053 -18.229 -8.318  1.00 25.58  ? 692  LEU   A CB  1 
ATOM   1045 C CG  . LEU   A 1 155 ? -17.571 -18.103 -8.089  1.00 28.85  ? 692  LEU   A CG  1 
ATOM   1046 C CD1 . LEU   A 1 155 ? -18.128 -19.274 -7.276  1.00 32.12  ? 692  LEU   A CD1 1 
ATOM   1047 C CD2 . LEU   A 1 155 ? -17.952 -16.773 -7.433  1.00 31.73  ? 692  LEU   A CD2 1 
ATOM   1048 N N   . ASN   A 1 156 ? -13.373 -17.789 -10.117 1.00 24.73  ? 693  ASN   A N   1 
ATOM   1049 C CA  . ASN   A 1 156 ? -11.922 -17.819 -10.317 1.00 26.20  ? 693  ASN   A CA  1 
ATOM   1050 C C   . ASN   A 1 156 ? -11.351 -16.424 -10.539 1.00 31.81  ? 693  ASN   A C   1 
ATOM   1051 O O   . ASN   A 1 156 ? -10.310 -16.075 -9.979  1.00 28.30  ? 693  ASN   A O   1 
ATOM   1052 C CB  . ASN   A 1 156 ? -11.539 -18.720 -11.495 1.00 23.73  ? 693  ASN   A CB  1 
ATOM   1053 C CG  . ASN   A 1 156 ? -10.032 -18.729 -11.767 1.00 32.07  ? 693  ASN   A CG  1 
ATOM   1054 O OD1 . ASN   A 1 156 ? -9.245  -19.153 -10.925 1.00 34.59  ? 693  ASN   A OD1 1 
ATOM   1055 N ND2 . ASN   A 1 156 ? -9.634  -18.267 -12.948 1.00 34.38  ? 693  ASN   A ND2 1 
ATOM   1056 N N   . VAL   A 1 157 ? -12.019 -15.629 -11.369 1.00 25.25  ? 694  VAL   A N   1 
ATOM   1057 C CA  . VAL   A 1 157 ? -11.561 -14.261 -11.605 1.00 21.37  ? 694  VAL   A CA  1 
ATOM   1058 C C   . VAL   A 1 157 ? -11.564 -13.458 -10.298 1.00 26.02  ? 694  VAL   A C   1 
ATOM   1059 O O   . VAL   A 1 157 ? -10.576 -12.772 -9.983  1.00 24.69  ? 694  VAL   A O   1 
ATOM   1060 C CB  . VAL   A 1 157 ? -12.427 -13.555 -12.663 1.00 21.68  ? 694  VAL   A CB  1 
ATOM   1061 C CG1 . VAL   A 1 157 ? -12.101 -12.056 -12.712 1.00 21.58  ? 694  VAL   A CG1 1 
ATOM   1062 C CG2 . VAL   A 1 157 ? -12.215 -14.215 -14.028 1.00 24.98  ? 694  VAL   A CG2 1 
ATOM   1063 N N   . PHE   A 1 158 ? -12.654 -13.550 -9.530  1.00 23.55  ? 695  PHE   A N   1 
ATOM   1064 C CA  . PHE   A 1 158 ? -12.724 -12.897 -8.218  1.00 27.46  ? 695  PHE   A CA  1 
ATOM   1065 C C   . PHE   A 1 158 ? -11.521 -13.268 -7.337  1.00 25.76  ? 695  PHE   A C   1 
ATOM   1066 O O   . PHE   A 1 158 ? -10.891 -12.405 -6.716  1.00 25.05  ? 695  PHE   A O   1 
ATOM   1067 C CB  . PHE   A 1 158 ? -14.023 -13.277 -7.494  1.00 26.44  ? 695  PHE   A CB  1 
ATOM   1068 C CG  . PHE   A 1 158 ? -15.262 -12.585 -8.019  1.00 26.91  ? 695  PHE   A CG  1 
ATOM   1069 C CD1 . PHE   A 1 158 ? -15.193 -11.369 -8.675  1.00 25.16  ? 695  PHE   A CD1 1 
ATOM   1070 C CD2 . PHE   A 1 158 ? -16.517 -13.150 -7.803  1.00 32.77  ? 695  PHE   A CD2 1 
ATOM   1071 C CE1 . PHE   A 1 158 ? -16.349 -10.742 -9.130  1.00 32.92  ? 695  PHE   A CE1 1 
ATOM   1072 C CE2 . PHE   A 1 158 ? -17.669 -12.533 -8.258  1.00 29.63  ? 695  PHE   A CE2 1 
ATOM   1073 C CZ  . PHE   A 1 158 ? -17.585 -11.327 -8.925  1.00 28.18  ? 695  PHE   A CZ  1 
ATOM   1074 N N   . ARG   A 1 159 ? -11.221 -14.558 -7.278  1.00 25.59  ? 696  ARG   A N   1 
ATOM   1075 C CA  . ARG   A 1 159 ? -10.114 -15.086 -6.475  1.00 24.29  ? 696  ARG   A CA  1 
ATOM   1076 C C   . ARG   A 1 159 ? -8.761  -14.488 -6.878  1.00 27.63  ? 696  ARG   A C   1 
ATOM   1077 O O   . ARG   A 1 159 ? -7.972  -14.074 -6.019  1.00 28.50  ? 696  ARG   A O   1 
ATOM   1078 C CB  . ARG   A 1 159 ? -10.078 -16.613 -6.611  1.00 36.90  ? 696  ARG   A CB  1 
ATOM   1079 C CG  . ARG   A 1 159 ? -9.436  -17.366 -5.468  1.00 53.09  ? 696  ARG   A CG  1 
ATOM   1080 C CD  . ARG   A 1 159 ? -9.601  -18.883 -5.636  1.00 59.77  ? 696  ARG   A CD  1 
ATOM   1081 N NE  . ARG   A 1 159 ? -9.139  -19.323 -6.949  1.00 75.36  ? 696  ARG   A NE  1 
ATOM   1082 C CZ  . ARG   A 1 159 ? -8.995  -20.605 -7.295  1.00 85.26  ? 696  ARG   A CZ  1 
ATOM   1083 N NH1 . ARG   A 1 159 ? -8.578  -20.939 -8.517  1.00 83.30  ? 696  ARG   A NH1 1 
ATOM   1084 N NH2 . ARG   A 1 159 ? -9.210  -21.576 -6.400  1.00 88.85  ? 696  ARG   A NH2 1 
ATOM   1085 N N   . HIS   A 1 160 ? -8.480  -14.460 -8.180  1.00 25.40  ? 697  HIS   A N   1 
ATOM   1086 C CA  . HIS   A 1 160 ? -7.254  -13.833 -8.669  1.00 26.64  ? 697  HIS   A CA  1 
ATOM   1087 C C   . HIS   A 1 160 ? -7.242  -12.320 -8.428  1.00 27.58  ? 697  HIS   A C   1 
ATOM   1088 O O   . HIS   A 1 160 ? -6.197  -11.729 -8.152  1.00 28.36  ? 697  HIS   A O   1 
ATOM   1089 C CB  . HIS   A 1 160 ? -7.071  -14.122 -10.158 1.00 27.14  ? 697  HIS   A CB  1 
ATOM   1090 C CG  . HIS   A 1 160 ? -6.629  -15.525 -10.441 1.00 38.05  ? 697  HIS   A CG  1 
ATOM   1091 N ND1 . HIS   A 1 160 ? -5.337  -15.837 -10.811 1.00 44.34  ? 697  HIS   A ND1 1 
ATOM   1092 C CD2 . HIS   A 1 160 ? -7.299  -16.701 -10.387 1.00 37.56  ? 697  HIS   A CD2 1 
ATOM   1093 C CE1 . HIS   A 1 160 ? -5.235  -17.144 -10.980 1.00 43.91  ? 697  HIS   A CE1 1 
ATOM   1094 N NE2 . HIS   A 1 160 ? -6.411  -17.691 -10.731 1.00 41.41  ? 697  HIS   A NE2 1 
ATOM   1095 N N   . TRP   A 1 161 ? -8.409  -11.699 -8.536  1.00 24.33  ? 698  TRP   A N   1 
ATOM   1096 C CA  . TRP   A 1 161 ? -8.532  -10.259 -8.356  1.00 22.44  ? 698  TRP   A CA  1 
ATOM   1097 C C   . TRP   A 1 161 ? -8.164  -9.861  -6.921  1.00 27.40  ? 698  TRP   A C   1 
ATOM   1098 O O   . TRP   A 1 161 ? -7.333  -8.977  -6.717  1.00 26.21  ? 698  TRP   A O   1 
ATOM   1099 C CB  . TRP   A 1 161 ? -9.955  -9.824  -8.693  1.00 24.64  ? 698  TRP   A CB  1 
ATOM   1100 C CG  . TRP   A 1 161 ? -10.182 -8.354  -8.794  1.00 25.98  ? 698  TRP   A CG  1 
ATOM   1101 C CD1 . TRP   A 1 161 ? -9.261  -7.350  -8.626  1.00 24.49  ? 698  TRP   A CD1 1 
ATOM   1102 C CD2 . TRP   A 1 161 ? -11.421 -7.715  -9.107  1.00 24.13  ? 698  TRP   A CD2 1 
ATOM   1103 N NE1 . TRP   A 1 161 ? -9.867  -6.123  -8.803  1.00 24.60  ? 698  TRP   A NE1 1 
ATOM   1104 C CE2 . TRP   A 1 161 ? -11.188 -6.323  -9.102  1.00 27.51  ? 698  TRP   A CE2 1 
ATOM   1105 C CE3 . TRP   A 1 161 ? -12.715 -8.192  -9.371  1.00 24.90  ? 698  TRP   A CE3 1 
ATOM   1106 C CZ2 . TRP   A 1 161 ? -12.205 -5.403  -9.363  1.00 24.90  ? 698  TRP   A CZ2 1 
ATOM   1107 C CZ3 . TRP   A 1 161 ? -13.706 -7.288  -9.631  1.00 23.54  ? 698  TRP   A CZ3 1 
ATOM   1108 C CH2 . TRP   A 1 161 ? -13.458 -5.908  -9.624  1.00 25.16  ? 698  TRP   A CH2 1 
ATOM   1109 N N   . VAL   A 1 162 ? -8.755  -10.523 -5.929  1.00 26.85  ? 699  VAL   A N   1 
ATOM   1110 C CA  . VAL   A 1 162 ? -8.441  -10.176 -4.538  1.00 27.29  ? 699  VAL   A CA  1 
ATOM   1111 C C   . VAL   A 1 162 ? -7.061  -10.678 -4.110  1.00 32.36  ? 699  VAL   A C   1 
ATOM   1112 O O   . VAL   A 1 162 ? -6.437  -10.098 -3.226  1.00 35.26  ? 699  VAL   A O   1 
ATOM   1113 C CB  . VAL   A 1 162 ? -9.517  -10.705 -3.544  1.00 31.38  ? 699  VAL   A CB  1 
ATOM   1114 C CG1 . VAL   A 1 162 ? -10.843 -9.990  -3.777  1.00 29.02  ? 699  VAL   A CG1 1 
ATOM   1115 C CG2 . VAL   A 1 162 ? -9.674  -12.219 -3.630  1.00 33.75  ? 699  VAL   A CG2 1 
ATOM   1116 N N   . GLU   A 1 163 ? -6.574  -11.741 -4.733  1.00 29.16  ? 700  GLU   A N   1 
ATOM   1117 C CA  . GLU   A 1 163 ? -5.252  -12.265 -4.382  1.00 30.33  ? 700  GLU   A CA  1 
ATOM   1118 C C   . GLU   A 1 163 ? -4.131  -11.352 -4.866  1.00 34.67  ? 700  GLU   A C   1 
ATOM   1119 O O   . GLU   A 1 163 ? -3.206  -11.035 -4.105  1.00 35.10  ? 700  GLU   A O   1 
ATOM   1120 C CB  . GLU   A 1 163 ? -5.045  -13.659 -4.966  1.00 32.73  ? 700  GLU   A CB  1 
ATOM   1121 C CG  . GLU   A 1 163 ? -3.711  -14.308 -4.595  1.00 35.85  ? 700  GLU   A CG  1 
ATOM   1122 C CD  . GLU   A 1 163 ? -3.581  -14.562 -3.099  1.00 53.21  ? 700  GLU   A CD  1 
ATOM   1123 O OE1 . GLU   A 1 163 ? -4.445  -15.270 -2.535  1.00 49.15  ? 700  GLU   A OE1 1 
ATOM   1124 O OE2 . GLU   A 1 163 ? -2.620  -14.046 -2.485  1.00 56.65  ? 700  GLU   A OE2 1 
ATOM   1125 N N   . HIS   A 1 164 ? -4.214  -10.923 -6.125  1.00 31.62  ? 701  HIS   A N   1 
ATOM   1126 C CA  . HIS   A 1 164 ? -3.087  -10.240 -6.772  1.00 35.05  ? 701  HIS   A CA  1 
ATOM   1127 C C   . HIS   A 1 164 ? -3.265  -8.738  -6.974  1.00 35.40  ? 701  HIS   A C   1 
ATOM   1128 O O   . HIS   A 1 164 ? -2.317  -8.033  -7.354  1.00 33.44  ? 701  HIS   A O   1 
ATOM   1129 C CB  . HIS   A 1 164 ? -2.806  -10.898 -8.125  1.00 29.09  ? 701  HIS   A CB  1 
ATOM   1130 C CG  . HIS   A 1 164 ? -2.442  -12.342 -8.021  1.00 35.36  ? 701  HIS   A CG  1 
ATOM   1131 N ND1 . HIS   A 1 164 ? -1.281  -12.772 -7.410  1.00 42.07  ? 701  HIS   A ND1 1 
ATOM   1132 C CD2 . HIS   A 1 164 ? -3.084  -13.460 -8.435  1.00 35.94  ? 701  HIS   A CD2 1 
ATOM   1133 C CE1 . HIS   A 1 164 ? -1.223  -14.093 -7.463  1.00 43.36  ? 701  HIS   A CE1 1 
ATOM   1134 N NE2 . HIS   A 1 164 ? -2.307  -14.532 -8.077  1.00 42.53  ? 701  HIS   A NE2 1 
ATOM   1135 N N   . HIS   A 1 165 ? -4.468  -8.242  -6.712  1.00 27.99  ? 702  HIS   A N   1 
ATOM   1136 C CA  . HIS   A 1 165 ? -4.760  -6.829  -6.904  1.00 23.76  ? 702  HIS   A CA  1 
ATOM   1137 C C   . HIS   A 1 165 ? -5.624  -6.265  -5.802  1.00 31.59  ? 702  HIS   A C   1 
ATOM   1138 O O   . HIS   A 1 165 ? -6.539  -5.465  -6.055  1.00 27.01  ? 702  HIS   A O   1 
ATOM   1139 C CB  . HIS   A 1 165 ? -5.428  -6.619  -8.267  1.00 24.96  ? 702  HIS   A CB  1 
ATOM   1140 C CG  . HIS   A 1 165 ? -4.623  -7.142  -9.410  1.00 29.12  ? 702  HIS   A CG  1 
ATOM   1141 N ND1 . HIS   A 1 165 ? -3.623  -6.401  -10.016 1.00 29.39  ? 702  HIS   A ND1 1 
ATOM   1142 C CD2 . HIS   A 1 165 ? -4.637  -8.333  -10.045 1.00 27.70  ? 702  HIS   A CD2 1 
ATOM   1143 C CE1 . HIS   A 1 165 ? -3.072  -7.119  -10.976 1.00 28.69  ? 702  HIS   A CE1 1 
ATOM   1144 N NE2 . HIS   A 1 165 ? -3.671  -8.296  -11.015 1.00 27.85  ? 702  HIS   A NE2 1 
ATOM   1145 N N   . PHE   A 1 166 ? -5.317  -6.646  -4.563  1.00 32.99  ? 703  PHE   A N   1 
ATOM   1146 C CA  . PHE   A 1 166 ? -6.175  -6.269  -3.455  1.00 34.24  ? 703  PHE   A CA  1 
ATOM   1147 C C   . PHE   A 1 166 ? -6.196  -4.754  -3.234  1.00 30.53  ? 703  PHE   A C   1 
ATOM   1148 O O   . PHE   A 1 166 ? -7.126  -4.234  -2.626  1.00 33.69  ? 703  PHE   A O   1 
ATOM   1149 C CB  . PHE   A 1 166 ? -5.755  -6.970  -2.165  1.00 34.62  ? 703  PHE   A CB  1 
ATOM   1150 C CG  . PHE   A 1 166 ? -6.771  -6.828  -1.060  1.00 41.82  ? 703  PHE   A CG  1 
ATOM   1151 C CD1 . PHE   A 1 166 ? -7.975  -7.517  -1.124  1.00 41.32  ? 703  PHE   A CD1 1 
ATOM   1152 C CD2 . PHE   A 1 166 ? -6.543  -5.985  0.018   1.00 41.68  ? 703  PHE   A CD2 1 
ATOM   1153 C CE1 . PHE   A 1 166 ? -8.926  -7.392  -0.125  1.00 43.97  ? 703  PHE   A CE1 1 
ATOM   1154 C CE2 . PHE   A 1 166 ? -7.492  -5.852  1.027   1.00 36.93  ? 703  PHE   A CE2 1 
ATOM   1155 C CZ  . PHE   A 1 166 ? -8.688  -6.560  0.952   1.00 40.87  ? 703  PHE   A CZ  1 
ATOM   1156 N N   . TYR   A 1 167 ? -5.185  -4.049  -3.748  1.00 33.25  ? 704  TYR   A N   1 
ATOM   1157 C CA  . TYR   A 1 167 ? -5.154  -2.590  -3.643  1.00 34.09  ? 704  TYR   A CA  1 
ATOM   1158 C C   . TYR   A 1 167 ? -6.388  -1.925  -4.265  1.00 32.47  ? 704  TYR   A C   1 
ATOM   1159 O O   . TYR   A 1 167 ? -6.781  -0.843  -3.830  1.00 32.68  ? 704  TYR   A O   1 
ATOM   1160 C CB  . TYR   A 1 167 ? -3.874  -2.020  -4.281  1.00 35.51  ? 704  TYR   A CB  1 
ATOM   1161 C CG  . TYR   A 1 167 ? -3.603  -2.534  -5.667  1.00 28.92  ? 704  TYR   A CG  1 
ATOM   1162 C CD1 . TYR   A 1 167 ? -4.227  -1.965  -6.772  1.00 31.75  ? 704  TYR   A CD1 1 
ATOM   1163 C CD2 . TYR   A 1 167 ? -2.712  -3.587  -5.882  1.00 27.47  ? 704  TYR   A CD2 1 
ATOM   1164 C CE1 . TYR   A 1 167 ? -3.991  -2.445  -8.045  1.00 29.28  ? 704  TYR   A CE1 1 
ATOM   1165 C CE2 . TYR   A 1 167 ? -2.473  -4.068  -7.156  1.00 30.42  ? 704  TYR   A CE2 1 
ATOM   1166 C CZ  . TYR   A 1 167 ? -3.121  -3.491  -8.230  1.00 28.92  ? 704  TYR   A CZ  1 
ATOM   1167 O OH  . TYR   A 1 167 ? -2.881  -3.946  -9.495  1.00 30.31  ? 704  TYR   A OH  1 
ATOM   1168 N N   . ASP   A 1 168 ? -7.003  -2.551  -5.273  1.00 31.67  ? 705  ASP   A N   1 
ATOM   1169 C CA  . ASP   A 1 168 ? -8.259  -2.024  -5.818  1.00 29.43  ? 705  ASP   A CA  1 
ATOM   1170 C C   . ASP   A 1 168 ? -9.290  -1.880  -4.708  1.00 30.57  ? 705  ASP   A C   1 
ATOM   1171 O O   . ASP   A 1 168 ? -10.083 -0.940  -4.692  1.00 30.39  ? 705  ASP   A O   1 
ATOM   1172 C CB  . ASP   A 1 168 ? -8.846  -2.938  -6.905  1.00 25.70  ? 705  ASP   A CB  1 
ATOM   1173 C CG  . ASP   A 1 168 ? -8.170  -2.787  -8.260  1.00 30.63  ? 705  ASP   A CG  1 
ATOM   1174 O OD1 . ASP   A 1 168 ? -7.538  -1.746  -8.524  1.00 26.79  ? 705  ASP   A OD1 1 
ATOM   1175 O OD2 . ASP   A 1 168 ? -8.306  -3.721  -9.079  1.00 29.52  ? 705  ASP   A OD2 1 
ATOM   1176 N N   . PHE   A 1 169 ? -9.288  -2.841  -3.789  1.00 30.95  ? 706  PHE   A N   1 
ATOM   1177 C CA  . PHE   A 1 169 ? -10.295 -2.883  -2.741  1.00 29.77  ? 706  PHE   A CA  1 
ATOM   1178 C C   . PHE   A 1 169 ? -9.886  -2.013  -1.552  1.00 35.11  ? 706  PHE   A C   1 
ATOM   1179 O O   . PHE   A 1 169 ? -10.737 -1.508  -0.838  1.00 39.13  ? 706  PHE   A O   1 
ATOM   1180 C CB  . PHE   A 1 169 ? -10.542 -4.333  -2.323  1.00 31.80  ? 706  PHE   A CB  1 
ATOM   1181 C CG  . PHE   A 1 169 ? -11.039 -5.190  -3.459  1.00 30.40  ? 706  PHE   A CG  1 
ATOM   1182 C CD1 . PHE   A 1 169 ? -12.391 -5.273  -3.736  1.00 31.60  ? 706  PHE   A CD1 1 
ATOM   1183 C CD2 . PHE   A 1 169 ? -10.148 -5.868  -4.283  1.00 33.91  ? 706  PHE   A CD2 1 
ATOM   1184 C CE1 . PHE   A 1 169 ? -12.857 -6.051  -4.804  1.00 30.84  ? 706  PHE   A CE1 1 
ATOM   1185 C CE2 . PHE   A 1 169 ? -10.604 -6.635  -5.355  1.00 33.61  ? 706  PHE   A CE2 1 
ATOM   1186 C CZ  . PHE   A 1 169 ? -11.958 -6.719  -5.613  1.00 33.21  ? 706  PHE   A CZ  1 
ATOM   1187 N N   . GLU   A 1 170 ? -8.582  -1.829  -1.367  1.00 35.46  ? 707  GLU   A N   1 
ATOM   1188 C CA  . GLU   A 1 170 ? -8.075  -0.942  -0.323  1.00 39.80  ? 707  GLU   A CA  1 
ATOM   1189 C C   . GLU   A 1 170 ? -8.385  0.512   -0.668  1.00 42.31  ? 707  GLU   A C   1 
ATOM   1190 O O   . GLU   A 1 170 ? -8.705  1.319   0.208   1.00 41.66  ? 707  GLU   A O   1 
ATOM   1191 C CB  . GLU   A 1 170 ? -6.569  -1.132  -0.142  1.00 43.82  ? 707  GLU   A CB  1 
ATOM   1192 C CG  . GLU   A 1 170 ? -6.173  -2.491  0.405   1.00 42.29  ? 707  GLU   A CG  1 
ATOM   1193 C CD  . GLU   A 1 170 ? -4.673  -2.707  0.416   1.00 48.48  ? 707  GLU   A CD  1 
ATOM   1194 O OE1 . GLU   A 1 170 ? -3.982  -2.090  -0.421  1.00 51.91  ? 707  GLU   A OE1 1 
ATOM   1195 O OE2 . GLU   A 1 170 ? -4.182  -3.487  1.264   1.00 50.77  ? 707  GLU   A OE2 1 
ATOM   1196 N N   . ARG   A 1 171 ? -8.294  0.826   -1.958  1.00 39.55  ? 708  ARG   A N   1 
ATOM   1197 C CA  . ARG   A 1 171 ? -8.527  2.171   -2.476  1.00 43.91  ? 708  ARG   A CA  1 
ATOM   1198 C C   . ARG   A 1 171 ? -10.003 2.518   -2.581  1.00 43.02  ? 708  ARG   A C   1 
ATOM   1199 O O   . ARG   A 1 171 ? -10.363 3.689   -2.694  1.00 46.95  ? 708  ARG   A O   1 
ATOM   1200 C CB  . ARG   A 1 171 ? -7.885  2.324   -3.858  1.00 41.88  ? 708  ARG   A CB  1 
ATOM   1201 C CG  . ARG   A 1 171 ? -6.380  2.223   -3.866  1.00 37.04  ? 708  ARG   A CG  1 
ATOM   1202 C CD  . ARG   A 1 171 ? -5.887  2.034   -5.285  1.00 38.41  ? 708  ARG   A CD  1 
ATOM   1203 N NE  . ARG   A 1 171 ? -4.453  1.788   -5.341  1.00 48.09  ? 708  ARG   A NE  1 
ATOM   1204 C CZ  . ARG   A 1 171 ? -3.790  1.555   -6.467  1.00 46.20  ? 708  ARG   A CZ  1 
ATOM   1205 N NH1 . ARG   A 1 171 ? -4.439  1.534   -7.626  1.00 44.60  ? 708  ARG   A NH1 1 
ATOM   1206 N NH2 . ARG   A 1 171 ? -2.481  1.337   -6.434  1.00 57.76  ? 708  ARG   A NH2 1 
ATOM   1207 N N   . ASP   A 1 172 ? -10.857 1.501   -2.567  1.00 37.78  ? 709  ASP   A N   1 
ATOM   1208 C CA  . ASP   A 1 172 ? -12.284 1.718   -2.740  1.00 35.97  ? 709  ASP   A CA  1 
ATOM   1209 C C   . ASP   A 1 172 ? -13.061 0.791   -1.819  1.00 46.90  ? 709  ASP   A C   1 
ATOM   1210 O O   . ASP   A 1 172 ? -13.265 -0.381  -2.129  1.00 35.88  ? 709  ASP   A O   1 
ATOM   1211 C CB  . ASP   A 1 172 ? -12.687 1.495   -4.202  1.00 37.56  ? 709  ASP   A CB  1 
ATOM   1212 C CG  . ASP   A 1 172 ? -14.142 1.878   -4.485  1.00 47.04  ? 709  ASP   A CG  1 
ATOM   1213 O OD1 . ASP   A 1 172 ? -14.955 1.955   -3.536  1.00 45.10  ? 709  ASP   A OD1 1 
ATOM   1214 O OD2 . ASP   A 1 172 ? -14.477 2.091   -5.670  1.00 50.10  ? 709  ASP   A OD2 1 
ATOM   1215 N N   . LEU   A 1 173 ? -13.509 1.327   -0.689  1.00 43.48  ? 710  LEU   A N   1 
ATOM   1216 C CA  . LEU   A 1 173 ? -14.196 0.512   0.300   1.00 45.47  ? 710  LEU   A CA  1 
ATOM   1217 C C   . LEU   A 1 173 ? -15.533 -0.025  -0.187  1.00 36.41  ? 710  LEU   A C   1 
ATOM   1218 O O   . LEU   A 1 173 ? -15.932 -1.120  0.208   1.00 40.17  ? 710  LEU   A O   1 
ATOM   1219 C CB  . LEU   A 1 173 ? -14.401 1.306   1.596   1.00 52.45  ? 710  LEU   A CB  1 
ATOM   1220 C CG  . LEU   A 1 173 ? -13.121 1.556   2.398   1.00 61.77  ? 710  LEU   A CG  1 
ATOM   1221 C CD1 . LEU   A 1 173 ? -13.448 1.924   3.840   1.00 62.26  ? 710  LEU   A CD1 1 
ATOM   1222 C CD2 . LEU   A 1 173 ? -12.195 0.343   2.335   1.00 61.62  ? 710  LEU   A CD2 1 
ATOM   1223 N N   . GLU   A 1 174 ? -16.234 0.737   -1.024  1.00 41.08  ? 711  GLU   A N   1 
ATOM   1224 C CA  . GLU   A 1 174 ? -17.533 0.286   -1.507  1.00 45.94  ? 711  GLU   A CA  1 
ATOM   1225 C C   . GLU   A 1 174 ? -17.362 -0.893  -2.452  1.00 42.79  ? 711  GLU   A C   1 
ATOM   1226 O O   . GLU   A 1 174 ? -18.216 -1.770  -2.506  1.00 37.29  ? 711  GLU   A O   1 
ATOM   1227 C CB  . GLU   A 1 174 ? -18.309 1.397   -2.219  1.00 48.89  ? 711  GLU   A CB  1 
ATOM   1228 C CG  . GLU   A 1 174 ? -19.797 1.061   -2.362  1.00 60.19  ? 711  GLU   A CG  1 
ATOM   1229 C CD  . GLU   A 1 174 ? -20.442 1.640   -3.613  1.00 72.85  ? 711  GLU   A CD  1 
ATOM   1230 O OE1 . GLU   A 1 174 ? -19.795 2.462   -4.299  1.00 77.62  ? 711  GLU   A OE1 1 
ATOM   1231 O OE2 . GLU   A 1 174 ? -21.602 1.264   -3.909  1.00 73.45  ? 711  GLU   A OE2 1 
ATOM   1232 N N   . LEU   A 1 175 ? -16.262 -0.903  -3.201  1.00 36.87  ? 712  LEU   A N   1 
ATOM   1233 C CA  . LEU   A 1 175 ? -15.961 -2.020  -4.093  1.00 31.80  ? 712  LEU   A CA  1 
ATOM   1234 C C   . LEU   A 1 175 ? -15.904 -3.340  -3.313  1.00 32.30  ? 712  LEU   A C   1 
ATOM   1235 O O   . LEU   A 1 175 ? -16.504 -4.339  -3.720  1.00 31.87  ? 712  LEU   A O   1 
ATOM   1236 C CB  . LEU   A 1 175 ? -14.634 -1.779  -4.829  1.00 33.62  ? 712  LEU   A CB  1 
ATOM   1237 C CG  . LEU   A 1 175 ? -14.239 -2.812  -5.888  1.00 30.45  ? 712  LEU   A CG  1 
ATOM   1238 C CD1 . LEU   A 1 175 ? -15.222 -2.780  -7.048  1.00 33.18  ? 712  LEU   A CD1 1 
ATOM   1239 C CD2 . LEU   A 1 175 ? -12.813 -2.586  -6.374  1.00 33.49  ? 712  LEU   A CD2 1 
ATOM   1240 N N   . LEU   A 1 176 ? -15.193 -3.339  -2.185  1.00 32.46  ? 713  LEU   A N   1 
ATOM   1241 C CA  . LEU   A 1 176 ? -15.042 -4.558  -1.386  1.00 34.38  ? 713  LEU   A CA  1 
ATOM   1242 C C   . LEU   A 1 176 ? -16.363 -4.960  -0.748  1.00 35.55  ? 713  LEU   A C   1 
ATOM   1243 O O   . LEU   A 1 176 ? -16.726 -6.140  -0.727  1.00 34.97  ? 713  LEU   A O   1 
ATOM   1244 C CB  . LEU   A 1 176 ? -13.972 -4.379  -0.308  1.00 32.32  ? 713  LEU   A CB  1 
ATOM   1245 C CG  . LEU   A 1 176 ? -13.658 -5.599  0.561   1.00 37.89  ? 713  LEU   A CG  1 
ATOM   1246 C CD1 . LEU   A 1 176 ? -13.255 -6.804  -0.289  1.00 36.31  ? 713  LEU   A CD1 1 
ATOM   1247 C CD2 . LEU   A 1 176 ? -12.562 -5.245  1.562   1.00 42.88  ? 713  LEU   A CD2 1 
ATOM   1248 N N   . GLU   A 1 177 ? -17.092 -3.975  -0.240  1.00 38.30  ? 714  GLU   A N   1 
ATOM   1249 C CA  . GLU   A 1 177 ? -18.395 -4.244  0.360   1.00 40.90  ? 714  GLU   A CA  1 
ATOM   1250 C C   . GLU   A 1 177 ? -19.355 -4.845  -0.658  1.00 34.02  ? 714  GLU   A C   1 
ATOM   1251 O O   . GLU   A 1 177 ? -20.090 -5.786  -0.333  1.00 35.04  ? 714  GLU   A O   1 
ATOM   1252 C CB  . GLU   A 1 177 ? -18.985 -2.965  0.959   1.00 48.76  ? 714  GLU   A CB  1 
ATOM   1253 C CG  . GLU   A 1 177 ? -18.353 -2.542  2.277   1.00 58.47  ? 714  GLU   A CG  1 
ATOM   1254 C CD  . GLU   A 1 177 ? -19.396 -2.291  3.355   1.00 77.38  ? 714  GLU   A CD  1 
ATOM   1255 O OE1 . GLU   A 1 177 ? -20.473 -2.928  3.306   1.00 78.52  ? 714  GLU   A OE1 1 
ATOM   1256 O OE2 . GLU   A 1 177 ? -19.141 -1.458  4.250   1.00 81.02  ? 714  GLU   A OE2 1 
ATOM   1257 N N   . ARG   A 1 178 ? -19.352 -4.313  -1.883  1.00 32.46  ? 715  ARG   A N   1 
ATOM   1258 C CA  . ARG   A 1 178 ? -20.167 -4.880  -2.963  1.00 33.08  ? 715  ARG   A CA  1 
ATOM   1259 C C   . ARG   A 1 178 ? -19.762 -6.318  -3.266  1.00 30.81  ? 715  ARG   A C   1 
ATOM   1260 O O   . ARG   A 1 178 ? -20.617 -7.197  -3.429  1.00 33.10  ? 715  ARG   A O   1 
ATOM   1261 C CB  . ARG   A 1 178 ? -20.055 -4.062  -4.252  1.00 35.17  ? 715  ARG   A CB  1 
ATOM   1262 C CG  . ARG   A 1 178 ? -20.802 -2.743  -4.285  1.00 44.12  ? 715  ARG   A CG  1 
ATOM   1263 C CD  . ARG   A 1 178 ? -20.659 -2.119  -5.672  1.00 35.18  ? 715  ARG   A CD  1 
ATOM   1264 N NE  . ARG   A 1 178 ? -21.369 -2.885  -6.683  1.00 40.99  ? 715  ARG   A NE  1 
ATOM   1265 C CZ  . ARG   A 1 178 ? -21.088 -2.861  -7.984  1.00 34.02  ? 715  ARG   A CZ  1 
ATOM   1266 N NH1 . ARG   A 1 178 ? -20.098 -2.103  -8.446  1.00 32.19  ? 715  ARG   A NH1 1 
ATOM   1267 N NH2 . ARG   A 1 178 ? -21.791 -3.606  -8.821  1.00 36.07  ? 715  ARG   A NH2 1 
ATOM   1268 N N   . LEU   A 1 179 ? -18.459 -6.560  -3.363  1.00 28.31  ? 716  LEU   A N   1 
ATOM   1269 C CA  . LEU   A 1 179 ? -18.000 -7.914  -3.669  1.00 30.65  ? 716  LEU   A CA  1 
ATOM   1270 C C   . LEU   A 1 179 ? -18.418 -8.886  -2.565  1.00 31.96  ? 716  LEU   A C   1 
ATOM   1271 O O   . LEU   A 1 179 ? -18.991 -9.938  -2.839  1.00 33.40  ? 716  LEU   A O   1 
ATOM   1272 C CB  . LEU   A 1 179 ? -16.488 -7.951  -3.856  1.00 33.39  ? 716  LEU   A CB  1 
ATOM   1273 C CG  . LEU   A 1 179 ? -15.915 -9.360  -4.038  1.00 33.72  ? 716  LEU   A CG  1 
ATOM   1274 C CD1 . LEU   A 1 179 ? -16.532 -10.064 -5.242  1.00 35.53  ? 716  LEU   A CD1 1 
ATOM   1275 C CD2 . LEU   A 1 179 ? -14.401 -9.303  -4.174  1.00 34.71  ? 716  LEU   A CD2 1 
ATOM   1276 N N   . GLU   A 1 180 ? -18.154 -8.518  -1.317  1.00 31.07  ? 717  GLU   A N   1 
ATOM   1277 C CA  . GLU   A 1 180 ? -18.494 -9.377  -0.184  1.00 31.80  ? 717  GLU   A CA  1 
ATOM   1278 C C   . GLU   A 1 180 ? -19.985 -9.649  -0.118  1.00 40.79  ? 717  GLU   A C   1 
ATOM   1279 O O   . GLU   A 1 180 ? -20.412 -10.774 0.153   1.00 38.87  ? 717  GLU   A O   1 
ATOM   1280 C CB  . GLU   A 1 180 ? -18.020 -8.741  1.121   1.00 39.14  ? 717  GLU   A CB  1 
ATOM   1281 C CG  . GLU   A 1 180 ? -16.513 -8.697  1.235   1.00 44.12  ? 717  GLU   A CG  1 
ATOM   1282 C CD  . GLU   A 1 180 ? -16.043 -7.997  2.489   1.00 54.24  ? 717  GLU   A CD  1 
ATOM   1283 O OE1 . GLU   A 1 180 ? -16.552 -6.893  2.791   1.00 50.83  ? 717  GLU   A OE1 1 
ATOM   1284 O OE2 . GLU   A 1 180 ? -15.156 -8.553  3.165   1.00 57.06  ? 717  GLU   A OE2 1 
ATOM   1285 N N   . SER   A 1 181 ? -20.780 -8.615  -0.366  1.00 36.80  ? 718  SER   A N   1 
ATOM   1286 C CA  . SER   A 1 181 ? -22.224 -8.775  -0.362  1.00 36.03  ? 718  SER   A CA  1 
ATOM   1287 C C   . SER   A 1 181 ? -22.640 -9.758  -1.447  1.00 40.86  ? 718  SER   A C   1 
ATOM   1288 O O   . SER   A 1 181 ? -23.473 -10.646 -1.220  1.00 34.61  ? 718  SER   A O   1 
ATOM   1289 C CB  . SER   A 1 181 ? -22.913 -7.426  -0.564  1.00 48.26  ? 718  SER   A CB  1 
ATOM   1290 O OG  . SER   A 1 181 ? -24.262 -7.603  -0.955  1.00 55.70  ? 718  SER   A OG  1 
ATOM   1291 N N   . PHE   A 1 182 ? -22.045 -9.616  -2.627  1.00 34.53  ? 719  PHE   A N   1 
ATOM   1292 C CA  . PHE   A 1 182 ? -22.412 -10.501 -3.717  1.00 31.76  ? 719  PHE   A CA  1 
ATOM   1293 C C   . PHE   A 1 182 ? -22.093 -11.959 -3.401  1.00 33.79  ? 719  PHE   A C   1 
ATOM   1294 O O   . PHE   A 1 182 ? -22.931 -12.829 -3.615  1.00 35.19  ? 719  PHE   A O   1 
ATOM   1295 C CB  . PHE   A 1 182 ? -21.730 -10.112 -5.026  1.00 29.71  ? 719  PHE   A CB  1 
ATOM   1296 C CG  . PHE   A 1 182 ? -21.976 -11.102 -6.107  1.00 34.21  ? 719  PHE   A CG  1 
ATOM   1297 C CD1 . PHE   A 1 182 ? -23.200 -11.133 -6.760  1.00 36.55  ? 719  PHE   A CD1 1 
ATOM   1298 C CD2 . PHE   A 1 182 ? -21.026 -12.058 -6.422  1.00 34.11  ? 719  PHE   A CD2 1 
ATOM   1299 C CE1 . PHE   A 1 182 ? -23.456 -12.075 -7.739  1.00 36.02  ? 719  PHE   A CE1 1 
ATOM   1300 C CE2 . PHE   A 1 182 ? -21.280 -13.012 -7.403  1.00 33.40  ? 719  PHE   A CE2 1 
ATOM   1301 C CZ  . PHE   A 1 182 ? -22.498 -13.016 -8.060  1.00 32.82  ? 719  PHE   A CZ  1 
ATOM   1302 N N   . ILE   A 1 183 ? -20.896 -12.241 -2.891  1.00 35.62  ? 720  ILE   A N   1 
ATOM   1303 C CA  . ILE   A 1 183 ? -20.530 -13.646 -2.700  1.00 32.51  ? 720  ILE   A CA  1 
ATOM   1304 C C   . ILE   A 1 183 ? -21.319 -14.281 -1.551  1.00 39.71  ? 720  ILE   A C   1 
ATOM   1305 O O   . ILE   A 1 183 ? -21.479 -15.498 -1.509  1.00 42.86  ? 720  ILE   A O   1 
ATOM   1306 C CB  . ILE   A 1 183 ? -19.017 -13.832 -2.466  1.00 37.80  ? 720  ILE   A CB  1 
ATOM   1307 C CG1 . ILE   A 1 183 ? -18.578 -13.225 -1.142  1.00 45.89  ? 720  ILE   A CG1 1 
ATOM   1308 C CG2 . ILE   A 1 183 ? -18.210 -13.234 -3.616  1.00 33.27  ? 720  ILE   A CG2 1 
ATOM   1309 C CD1 . ILE   A 1 183 ? -17.070 -13.254 -0.960  1.00 54.26  ? 720  ILE   A CD1 1 
ATOM   1310 N N   . SER   A 1 184 ? -21.831 -13.463 -0.636  1.00 45.63  ? 721  SER   A N   1 
ATOM   1311 C CA  . SER   A 1 184 ? -22.723 -13.972 0.409   1.00 46.49  ? 721  SER   A CA  1 
ATOM   1312 C C   . SER   A 1 184 ? -24.079 -14.381 -0.176  1.00 53.99  ? 721  SER   A C   1 
ATOM   1313 O O   . SER   A 1 184 ? -24.790 -15.205 0.398   1.00 53.31  ? 721  SER   A O   1 
ATOM   1314 C CB  . SER   A 1 184 ? -22.924 -12.930 1.508   1.00 51.04  ? 721  SER   A CB  1 
ATOM   1315 O OG  . SER   A 1 184 ? -23.727 -11.855 1.049   1.00 63.26  ? 721  SER   A OG  1 
ATOM   1316 N N   . SER   A 1 185 ? -24.427 -13.808 -1.326  1.00 51.53  ? 722  SER   A N   1 
ATOM   1317 C CA  . SER   A 1 185 ? -25.709 -14.089 -1.973  1.00 49.44  ? 722  SER   A CA  1 
ATOM   1318 C C   . SER   A 1 185 ? -25.681 -15.356 -2.830  1.00 45.91  ? 722  SER   A C   1 
ATOM   1319 O O   . SER   A 1 185 ? -26.723 -15.821 -3.282  1.00 51.61  ? 722  SER   A O   1 
ATOM   1320 C CB  . SER   A 1 185 ? -26.139 -12.902 -2.840  1.00 47.16  ? 722  SER   A CB  1 
ATOM   1321 O OG  . SER   A 1 185 ? -25.450 -12.892 -4.083  1.00 46.70  ? 722  SER   A OG  1 
ATOM   1322 N N   . VAL   A 1 186 ? -24.497 -15.918 -3.058  1.00 44.72  ? 723  VAL   A N   1 
ATOM   1323 C CA  . VAL   A 1 186 ? -24.386 -17.085 -3.938  1.00 46.52  ? 723  VAL   A CA  1 
ATOM   1324 C C   . VAL   A 1 186 ? -24.923 -18.355 -3.266  1.00 62.71  ? 723  VAL   A C   1 
ATOM   1325 O O   . VAL   A 1 186 ? -24.619 -18.628 -2.106  1.00 61.38  ? 723  VAL   A O   1 
ATOM   1326 C CB  . VAL   A 1 186 ? -22.926 -17.298 -4.396  1.00 44.99  ? 723  VAL   A CB  1 
ATOM   1327 C CG1 . VAL   A 1 186 ? -22.778 -18.601 -5.178  1.00 44.36  ? 723  VAL   A CG1 1 
ATOM   1328 C CG2 . VAL   A 1 186 ? -22.471 -16.117 -5.246  1.00 37.65  ? 723  VAL   A CG2 1 
ATOM   1329 N N   . ARG   A 1 187 ? -25.736 -19.113 -4.003  1.00 67.74  ? 724  ARG   A N   1 
ATOM   1330 C CA  . ARG   A 1 187 ? -26.355 -20.341 -3.490  1.00 70.13  ? 724  ARG   A CA  1 
ATOM   1331 C C   . ARG   A 1 187 ? -25.690 -21.609 -4.028  1.00 68.71  ? 724  ARG   A C   1 
ATOM   1332 O O   . ARG   A 1 187 ? -25.009 -21.583 -5.057  1.00 72.64  ? 724  ARG   A O   1 
ATOM   1333 C CB  . ARG   A 1 187 ? -27.842 -20.378 -3.848  1.00 66.57  ? 724  ARG   A CB  1 
ATOM   1334 C CG  . ARG   A 1 187 ? -28.664 -19.213 -3.324  1.00 73.47  ? 724  ARG   A CG  1 
ATOM   1335 C CD  . ARG   A 1 187 ? -29.113 -19.446 -1.890  1.00 80.92  ? 724  ARG   A CD  1 
ATOM   1336 N NE  . ARG   A 1 187 ? -28.101 -19.043 -0.917  1.00 87.44  ? 724  ARG   A NE  1 
ATOM   1337 C CZ  . ARG   A 1 187 ? -28.000 -17.817 -0.412  1.00 90.39  ? 724  ARG   A CZ  1 
ATOM   1338 N NH1 . ARG   A 1 187 ? -28.847 -16.868 -0.793  1.00 89.68  ? 724  ARG   A NH1 1 
ATOM   1339 N NH2 . ARG   A 1 187 ? -27.050 -17.535 0.471   1.00 87.89  ? 724  ARG   A NH2 1 
ATOM   1340 N N   . GLY   A 1 188 ? -25.903 -22.721 -3.331  1.00 62.59  ? 725  GLY   A N   1 
ATOM   1341 C CA  . GLY   A 1 188 ? -25.496 -24.023 -3.832  1.00 66.14  ? 725  GLY   A CA  1 
ATOM   1342 C C   . GLY   A 1 188 ? -24.144 -24.499 -3.346  1.00 69.50  ? 725  GLY   A C   1 
ATOM   1343 O O   . GLY   A 1 188 ? -23.165 -23.749 -3.360  1.00 70.98  ? 725  GLY   A O   1 
ATOM   1344 N N   . LYS   A 1 189 ? -24.089 -25.763 -2.939  1.00 69.84  ? 726  LYS   A N   1 
ATOM   1345 C CA  . LYS   A 1 189 ? -22.870 -26.355 -2.398  1.00 78.36  ? 726  LYS   A CA  1 
ATOM   1346 C C   . LYS   A 1 189 ? -21.746 -26.432 -3.431  1.00 78.17  ? 726  LYS   A C   1 
ATOM   1347 O O   . LYS   A 1 189 ? -20.570 -26.541 -3.075  1.00 77.26  ? 726  LYS   A O   1 
ATOM   1348 C CB  . LYS   A 1 189 ? -23.154 -27.757 -1.853  1.00 84.42  ? 726  LYS   A CB  1 
ATOM   1349 C CG  . LYS   A 1 189 ? -24.011 -27.792 -0.600  1.00 88.69  ? 726  LYS   A CG  1 
ATOM   1350 C CD  . LYS   A 1 189 ? -24.159 -29.223 -0.098  1.00 90.18  ? 726  LYS   A CD  1 
ATOM   1351 C CE  . LYS   A 1 189 ? -24.935 -29.284 1.208   1.00 87.84  ? 726  LYS   A CE  1 
ATOM   1352 N NZ  . LYS   A 1 189 ? -25.126 -30.689 1.666   1.00 85.87  ? 726  LYS   A NZ  1 
ATOM   1353 N N   . ALA   A 1 190 ? -22.110 -26.371 -4.708  1.00 76.60  ? 727  ALA   A N   1 
ATOM   1354 C CA  . ALA   A 1 190 ? -21.140 -26.488 -5.791  1.00 80.95  ? 727  ALA   A CA  1 
ATOM   1355 C C   . ALA   A 1 190 ? -20.133 -25.338 -5.794  1.00 85.88  ? 727  ALA   A C   1 
ATOM   1356 O O   . ALA   A 1 190 ? -19.062 -25.444 -6.396  1.00 88.31  ? 727  ALA   A O   1 
ATOM   1357 C CB  . ALA   A 1 190 ? -21.857 -26.558 -7.130  1.00 82.38  ? 727  ALA   A CB  1 
ATOM   1358 N N   . MET   A 1 191 ? -20.474 -24.242 -5.120  1.00 78.30  ? 728  MET   A N   1 
ATOM   1359 C CA  . MET   A 1 191 ? -19.634 -23.051 -5.145  1.00 68.70  ? 728  MET   A CA  1 
ATOM   1360 C C   . MET   A 1 191 ? -19.197 -22.598 -3.765  1.00 63.63  ? 728  MET   A C   1 
ATOM   1361 O O   . MET   A 1 191 ? -18.438 -21.636 -3.637  1.00 48.79  ? 728  MET   A O   1 
ATOM   1362 C CB  . MET   A 1 191 ? -20.368 -21.905 -5.826  1.00 66.32  ? 728  MET   A CB  1 
ATOM   1363 C CG  . MET   A 1 191 ? -21.245 -22.350 -6.953  1.00 66.42  ? 728  MET   A CG  1 
ATOM   1364 S SD  . MET   A 1 191 ? -21.252 -21.159 -8.284  1.00 53.23  ? 728  MET   A SD  1 
ATOM   1365 C CE  . MET   A 1 191 ? -23.024 -21.020 -8.523  1.00 63.00  ? 728  MET   A CE  1 
ATOM   1366 N N   . LYS   A 1 192 ? -19.680 -23.277 -2.730  1.00 69.84  ? 729  LYS   A N   1 
ATOM   1367 C CA  . LYS   A 1 192 ? -19.361 -22.855 -1.373  1.00 67.69  ? 729  LYS   A CA  1 
ATOM   1368 C C   . LYS   A 1 192 ? -17.866 -22.952 -1.112  1.00 59.41  ? 729  LYS   A C   1 
ATOM   1369 O O   . LYS   A 1 192 ? -17.308 -22.127 -0.395  1.00 63.09  ? 729  LYS   A O   1 
ATOM   1370 C CB  . LYS   A 1 192 ? -20.152 -23.668 -0.351  1.00 71.30  ? 729  LYS   A CB  1 
ATOM   1371 C CG  . LYS   A 1 192 ? -21.526 -23.079 -0.098  1.00 80.87  ? 729  LYS   A CG  1 
ATOM   1372 C CD  . LYS   A 1 192 ? -21.443 -21.558 0.001   1.00 85.08  ? 729  LYS   A CD  1 
ATOM   1373 C CE  . LYS   A 1 192 ? -22.461 -20.886 -0.905  1.00 85.61  ? 729  LYS   A CE  1 
ATOM   1374 N NZ  . LYS   A 1 192 ? -22.355 -21.365 -2.309  1.00 84.42  ? 729  LYS   A NZ  1 
ATOM   1375 N N   . LYS   A 1 193 ? -17.218 -23.940 -1.722  1.00 64.16  ? 730  LYS   A N   1 
ATOM   1376 C CA  . LYS   A 1 193 ? -15.766 -24.061 -1.650  1.00 63.71  ? 730  LYS   A CA  1 
ATOM   1377 C C   . LYS   A 1 193 ? -15.108 -22.810 -2.222  1.00 58.60  ? 730  LYS   A C   1 
ATOM   1378 O O   . LYS   A 1 193 ? -14.176 -22.258 -1.630  1.00 46.08  ? 730  LYS   A O   1 
ATOM   1379 C CB  . LYS   A 1 193 ? -15.280 -25.298 -2.407  1.00 69.09  ? 730  LYS   A CB  1 
ATOM   1380 C CG  . LYS   A 1 193 ? -16.145 -26.528 -2.202  1.00 82.72  ? 730  LYS   A CG  1 
ATOM   1381 C CD  . LYS   A 1 193 ? -15.302 -27.792 -2.143  1.00 87.51  ? 730  LYS   A CD  1 
ATOM   1382 C CE  . LYS   A 1 193 ? -16.049 -28.976 -2.732  1.00 86.95  ? 730  LYS   A CE  1 
ATOM   1383 N NZ  . LYS   A 1 193 ? -16.359 -28.757 -4.173  1.00 83.93  ? 730  LYS   A NZ  1 
ATOM   1384 N N   . TRP   A 1 194 ? -15.613 -22.365 -3.372  1.00 52.52  ? 731  TRP   A N   1 
ATOM   1385 C CA  . TRP   A 1 194 ? -15.090 -21.183 -4.051  1.00 44.73  ? 731  TRP   A CA  1 
ATOM   1386 C C   . TRP   A 1 194 ? -15.356 -19.898 -3.274  1.00 46.85  ? 731  TRP   A C   1 
ATOM   1387 O O   . TRP   A 1 194 ? -14.459 -19.068 -3.104  1.00 43.09  ? 731  TRP   A O   1 
ATOM   1388 C CB  . TRP   A 1 194 ? -15.694 -21.065 -5.450  1.00 51.48  ? 731  TRP   A CB  1 
ATOM   1389 C CG  . TRP   A 1 194 ? -15.046 -21.940 -6.487  1.00 52.58  ? 731  TRP   A CG  1 
ATOM   1390 C CD1 . TRP   A 1 194 ? -15.449 -23.185 -6.884  1.00 52.89  ? 731  TRP   A CD1 1 
ATOM   1391 C CD2 . TRP   A 1 194 ? -13.881 -21.628 -7.265  1.00 64.26  ? 731  TRP   A CD2 1 
ATOM   1392 N NE1 . TRP   A 1 194 ? -14.605 -23.667 -7.860  1.00 57.39  ? 731  TRP   A NE1 1 
ATOM   1393 C CE2 . TRP   A 1 194 ? -13.636 -22.730 -8.113  1.00 60.79  ? 731  TRP   A CE2 1 
ATOM   1394 C CE3 . TRP   A 1 194 ? -13.017 -20.525 -7.323  1.00 66.30  ? 731  TRP   A CE3 1 
ATOM   1395 C CZ2 . TRP   A 1 194 ? -12.565 -22.762 -9.008  1.00 61.72  ? 731  TRP   A CZ2 1 
ATOM   1396 C CZ3 . TRP   A 1 194 ? -11.955 -20.560 -8.211  1.00 59.99  ? 731  TRP   A CZ3 1 
ATOM   1397 C CH2 . TRP   A 1 194 ? -11.740 -21.669 -9.046  1.00 65.09  ? 731  TRP   A CH2 1 
ATOM   1398 N N   . VAL   A 1 195 ? -16.591 -19.732 -2.813  1.00 43.41  ? 732  VAL   A N   1 
ATOM   1399 C CA  . VAL   A 1 195 ? -16.956 -18.544 -2.048  1.00 50.03  ? 732  VAL   A CA  1 
ATOM   1400 C C   . VAL   A 1 195 ? -16.121 -18.433 -0.770  1.00 51.09  ? 732  VAL   A C   1 
ATOM   1401 O O   . VAL   A 1 195 ? -15.544 -17.381 -0.493  1.00 45.21  ? 732  VAL   A O   1 
ATOM   1402 C CB  . VAL   A 1 195 ? -18.458 -18.542 -1.698  1.00 54.75  ? 732  VAL   A CB  1 
ATOM   1403 C CG1 . VAL   A 1 195 ? -18.735 -17.636 -0.512  1.00 58.14  ? 732  VAL   A CG1 1 
ATOM   1404 C CG2 . VAL   A 1 195 ? -19.277 -18.115 -2.907  1.00 51.15  ? 732  VAL   A CG2 1 
ATOM   1405 N N   . GLU   A 1 196 ? -16.041 -19.523 -0.009  1.00 45.61  ? 733  GLU   A N   1 
ATOM   1406 C CA  . GLU   A 1 196 ? -15.253 -19.541 1.226   1.00 50.94  ? 733  GLU   A CA  1 
ATOM   1407 C C   . GLU   A 1 196 ? -13.769 -19.285 0.960   1.00 48.25  ? 733  GLU   A C   1 
ATOM   1408 O O   . GLU   A 1 196 ? -13.089 -18.637 1.756   1.00 53.83  ? 733  GLU   A O   1 
ATOM   1409 C CB  . GLU   A 1 196 ? -15.449 -20.874 1.964   1.00 58.78  ? 733  GLU   A CB  1 
ATOM   1410 C CG  . GLU   A 1 196 ? -16.753 -20.919 2.770   1.00 67.45  ? 733  GLU   A CG  1 
ATOM   1411 C CD  . GLU   A 1 196 ? -17.275 -22.329 3.028   1.00 79.06  ? 733  GLU   A CD  1 
ATOM   1412 O OE1 . GLU   A 1 196 ? -16.599 -23.313 2.650   1.00 81.01  ? 733  GLU   A OE1 1 
ATOM   1413 O OE2 . GLU   A 1 196 ? -18.376 -22.451 3.612   1.00 81.66  ? 733  GLU   A OE2 1 
ATOM   1414 N N   . SER   A 1 197 ? -13.275 -19.775 -0.170  1.00 40.05  ? 734  SER   A N   1 
ATOM   1415 C CA  . SER   A 1 197 ? -11.898 -19.521 -0.565  1.00 40.60  ? 734  SER   A CA  1 
ATOM   1416 C C   . SER   A 1 197 ? -11.650 -18.030 -0.819  1.00 47.11  ? 734  SER   A C   1 
ATOM   1417 O O   . SER   A 1 197 ? -10.605 -17.482 -0.434  1.00 36.98  ? 734  SER   A O   1 
ATOM   1418 C CB  . SER   A 1 197 ? -11.557 -20.339 -1.809  1.00 51.66  ? 734  SER   A CB  1 
ATOM   1419 O OG  . SER   A 1 197 ? -10.308 -19.952 -2.347  1.00 62.92  ? 734  SER   A OG  1 
ATOM   1420 N N   . ILE   A 1 198 ? -12.609 -17.373 -1.468  1.00 44.56  ? 735  ILE   A N   1 
ATOM   1421 C CA  . ILE   A 1 198 ? -12.507 -15.935 -1.706  1.00 37.94  ? 735  ILE   A CA  1 
ATOM   1422 C C   . ILE   A 1 198 ? -12.558 -15.181 -0.377  1.00 37.05  ? 735  ILE   A C   1 
ATOM   1423 O O   . ILE   A 1 198 ? -11.784 -14.249 -0.156  1.00 40.70  ? 735  ILE   A O   1 
ATOM   1424 C CB  . ILE   A 1 198 ? -13.626 -15.417 -2.630  1.00 36.07  ? 735  ILE   A CB  1 
ATOM   1425 C CG1 . ILE   A 1 198 ? -13.519 -16.057 -4.014  1.00 39.32  ? 735  ILE   A CG1 1 
ATOM   1426 C CG2 . ILE   A 1 198 ? -13.547 -13.909 -2.769  1.00 40.50  ? 735  ILE   A CG2 1 
ATOM   1427 C CD1 . ILE   A 1 198 ? -14.788 -15.938 -4.835  1.00 36.05  ? 735  ILE   A CD1 1 
ATOM   1428 N N   . ALA   A 1 199 ? -13.469 -15.593 0.502   1.00 39.26  ? 736  ALA   A N   1 
ATOM   1429 C CA  . ALA   A 1 199 ? -13.587 -14.995 1.833   1.00 40.92  ? 736  ALA   A CA  1 
ATOM   1430 C C   . ALA   A 1 199 ? -12.279 -15.113 2.599   1.00 45.04  ? 736  ALA   A C   1 
ATOM   1431 O O   . ALA   A 1 199 ? -11.814 -14.148 3.206   1.00 44.00  ? 736  ALA   A O   1 
ATOM   1432 C CB  . ALA   A 1 199 ? -14.714 -15.649 2.613   1.00 40.13  ? 736  ALA   A CB  1 
ATOM   1433 N N   . LYS   A 1 200 ? -11.684 -16.299 2.551   1.00 41.73  ? 737  LYS   A N   1 
ATOM   1434 C CA  . LYS   A 1 200 ? -10.442 -16.568 3.267   1.00 45.48  ? 737  LYS   A CA  1 
ATOM   1435 C C   . LYS   A 1 200 ? -9.317  -15.652 2.800   1.00 51.10  ? 737  LYS   A C   1 
ATOM   1436 O O   . LYS   A 1 200 ? -8.549  -15.128 3.615   1.00 46.89  ? 737  LYS   A O   1 
ATOM   1437 C CB  . LYS   A 1 200 ? -10.033 -18.030 3.094   1.00 50.32  ? 737  LYS   A CB  1 
ATOM   1438 C CG  . LYS   A 1 200 ? -8.797  -18.411 3.892   1.00 53.62  ? 737  LYS   A CG  1 
ATOM   1439 C CD  . LYS   A 1 200 ? -8.498  -19.892 3.779   1.00 55.74  ? 737  LYS   A CD  1 
ATOM   1440 C CE  . LYS   A 1 200 ? -7.408  -20.304 4.758   1.00 63.31  ? 737  LYS   A CE  1 
ATOM   1441 N NZ  . LYS   A 1 200 ? -7.326  -21.782 4.915   1.00 65.86  ? 737  LYS   A NZ  1 
ATOM   1442 N N   . ILE   A 1 201 ? -9.217  -15.450 1.489   1.00 38.48  ? 738  ILE   A N   1 
ATOM   1443 C CA  . ILE   A 1 201 ? -8.209  -14.545 0.950   1.00 38.97  ? 738  ILE   A CA  1 
ATOM   1444 C C   . ILE   A 1 201 ? -8.472  -13.121 1.430   1.00 34.52  ? 738  ILE   A C   1 
ATOM   1445 O O   . ILE   A 1 201 ? -7.548  -12.405 1.804   1.00 37.60  ? 738  ILE   A O   1 
ATOM   1446 C CB  . ILE   A 1 201 ? -8.174  -14.575 -0.593  1.00 37.91  ? 738  ILE   A CB  1 
ATOM   1447 C CG1 . ILE   A 1 201 ? -7.741  -15.952 -1.084  1.00 37.32  ? 738  ILE   A CG1 1 
ATOM   1448 C CG2 . ILE   A 1 201 ? -7.230  -13.511 -1.140  1.00 35.31  ? 738  ILE   A CG2 1 
ATOM   1449 C CD1 . ILE   A 1 201 ? -7.966  -16.152 -2.559  1.00 43.75  ? 738  ILE   A CD1 1 
ATOM   1450 N N   . ILE   A 1 202 ? -9.736  -12.716 1.440   1.00 36.99  ? 739  ILE   A N   1 
ATOM   1451 C CA  . ILE   A 1 202 ? -10.073 -11.362 1.866   1.00 39.65  ? 739  ILE   A CA  1 
ATOM   1452 C C   . ILE   A 1 202 ? -9.741  -11.175 3.351   1.00 49.35  ? 739  ILE   A C   1 
ATOM   1453 O O   . ILE   A 1 202 ? -9.245  -10.123 3.749   1.00 47.31  ? 739  ILE   A O   1 
ATOM   1454 C CB  . ILE   A 1 202 ? -11.556 -11.038 1.598   1.00 40.61  ? 739  ILE   A CB  1 
ATOM   1455 C CG1 . ILE   A 1 202 ? -11.826 -11.050 0.085   1.00 38.73  ? 739  ILE   A CG1 1 
ATOM   1456 C CG2 . ILE   A 1 202 ? -11.924 -9.685  2.194   1.00 48.58  ? 739  ILE   A CG2 1 
ATOM   1457 C CD1 . ILE   A 1 202 ? -13.253 -10.723 -0.301  1.00 35.52  ? 739  ILE   A CD1 1 
ATOM   1458 N N   . ARG   A 1 203 ? -9.995  -12.208 4.155   1.00 53.42  ? 740  ARG   A N   1 
ATOM   1459 C CA  . ARG   A 1 203 ? -9.630  -12.196 5.574   1.00 56.43  ? 740  ARG   A CA  1 
ATOM   1460 C C   . ARG   A 1 203 ? -8.134  -11.977 5.781   1.00 61.43  ? 740  ARG   A C   1 
ATOM   1461 O O   . ARG   A 1 203 ? -7.726  -11.108 6.559   1.00 61.48  ? 740  ARG   A O   1 
ATOM   1462 C CB  . ARG   A 1 203 ? -10.046 -13.501 6.256   1.00 59.83  ? 740  ARG   A CB  1 
ATOM   1463 C CG  . ARG   A 1 203 ? -11.475 -13.521 6.769   1.00 68.69  ? 740  ARG   A CG  1 
ATOM   1464 C CD  . ARG   A 1 203 ? -11.695 -14.663 7.765   1.00 70.74  ? 740  ARG   A CD  1 
ATOM   1465 N NE  . ARG   A 1 203 ? -11.397 -15.978 7.197   1.00 69.94  ? 740  ARG   A NE  1 
ATOM   1466 C CZ  . ARG   A 1 203 ? -12.269 -16.713 6.512   1.00 67.59  ? 740  ARG   A CZ  1 
ATOM   1467 N NH1 . ARG   A 1 203 ? -13.498 -16.261 6.299   1.00 63.38  ? 740  ARG   A NH1 1 
ATOM   1468 N NH2 . ARG   A 1 203 ? -11.910 -17.900 6.035   1.00 71.46  ? 740  ARG   A NH2 1 
ATOM   1469 N N   . ARG   A 1 204 ? -7.322  -12.771 5.087   1.00 51.90  ? 741  ARG   A N   1 
ATOM   1470 C CA  . ARG   A 1 204 ? -5.871  -12.664 5.188   1.00 53.41  ? 741  ARG   A CA  1 
ATOM   1471 C C   . ARG   A 1 204 ? -5.368  -11.294 4.738   1.00 62.62  ? 741  ARG   A C   1 
ATOM   1472 O O   . ARG   A 1 204 ? -4.471  -10.724 5.355   1.00 68.46  ? 741  ARG   A O   1 
ATOM   1473 C CB  . ARG   A 1 204 ? -5.193  -13.763 4.368   1.00 52.34  ? 741  ARG   A CB  1 
ATOM   1474 C CG  . ARG   A 1 204 ? -3.791  -13.411 3.902   1.00 47.94  ? 741  ARG   A CG  1 
ATOM   1475 C CD  . ARG   A 1 204 ? -3.039  -14.628 3.384   1.00 51.44  ? 741  ARG   A CD  1 
ATOM   1476 N NE  . ARG   A 1 204 ? -3.803  -15.410 2.409   1.00 56.14  ? 741  ARG   A NE  1 
ATOM   1477 C CZ  . ARG   A 1 204 ? -3.743  -15.241 1.091   1.00 58.47  ? 741  ARG   A CZ  1 
ATOM   1478 N NH1 . ARG   A 1 204 ? -2.963  -14.301 0.570   1.00 52.28  ? 741  ARG   A NH1 1 
ATOM   1479 N NH2 . ARG   A 1 204 ? -4.470  -16.010 0.292   1.00 51.35  ? 741  ARG   A NH2 1 
ATOM   1480 N N   . LYS   A 1 205 ? -5.950  -10.765 3.665   1.00 52.99  ? 742  LYS   A N   1 
ATOM   1481 C CA  . LYS   A 1 205 ? -5.550  -9.460  3.152   1.00 49.63  ? 742  LYS   A CA  1 
ATOM   1482 C C   . LYS   A 1 205 ? -5.873  -8.331  4.134   1.00 55.77  ? 742  LYS   A C   1 
ATOM   1483 O O   . LYS   A 1 205 ? -5.062  -7.424  4.324   1.00 59.21  ? 742  LYS   A O   1 
ATOM   1484 C CB  . LYS   A 1 205 ? -6.227  -9.182  1.809   1.00 48.26  ? 742  LYS   A CB  1 
ATOM   1485 C CG  . LYS   A 1 205 ? -5.799  -10.106 0.685   1.00 46.26  ? 742  LYS   A CG  1 
ATOM   1486 C CD  . LYS   A 1 205 ? -4.387  -9.828  0.230   1.00 48.33  ? 742  LYS   A CD  1 
ATOM   1487 C CE  . LYS   A 1 205 ? -3.969  -10.815 -0.842  1.00 43.41  ? 742  LYS   A CE  1 
ATOM   1488 N NZ  . LYS   A 1 205 ? -2.593  -10.547 -1.321  1.00 38.67  ? 742  LYS   A NZ  1 
ATOM   1489 N N   . LYS   A 1 206 ? -7.058  -8.386  4.742   1.00 64.56  ? 743  LYS   A N   1 
ATOM   1490 C CA  . LYS   A 1 206 ? -7.508  -7.337  5.658   1.00 70.78  ? 743  LYS   A CA  1 
ATOM   1491 C C   . LYS   A 1 206 ? -6.644  -7.259  6.910   1.00 79.66  ? 743  LYS   A C   1 
ATOM   1492 O O   . LYS   A 1 206 ? -6.367  -6.169  7.409   1.00 81.23  ? 743  LYS   A O   1 
ATOM   1493 C CB  . LYS   A 1 206 ? -8.967  -7.551  6.066   1.00 68.39  ? 743  LYS   A CB  1 
ATOM   1494 C CG  . LYS   A 1 206 ? -9.993  -6.859  5.177   1.00 67.34  ? 743  LYS   A CG  1 
ATOM   1495 C CD  . LYS   A 1 206 ? -11.345 -6.790  5.872   1.00 71.48  ? 743  LYS   A CD  1 
ATOM   1496 C CE  . LYS   A 1 206 ? -12.488 -6.691  4.880   1.00 70.24  ? 743  LYS   A CE  1 
ATOM   1497 N NZ  . LYS   A 1 206 ? -13.818 -6.763  5.547   1.00 70.84  ? 743  LYS   A NZ  1 
ATOM   1498 N N   . GLN   A 1 207 ? -6.228  -8.417  7.416   1.00 81.66  ? 744  GLN   A N   1 
ATOM   1499 C CA  . GLN   A 1 207 ? -5.397  -8.478  8.613   1.00 83.80  ? 744  GLN   A CA  1 
ATOM   1500 C C   . GLN   A 1 207 ? -4.058  -7.770  8.419   1.00 87.65  ? 744  GLN   A C   1 
ATOM   1501 O O   . GLN   A 1 207 ? -3.688  -6.900  9.214   1.00 96.24  ? 744  GLN   A O   1 
ATOM   1502 C CB  . GLN   A 1 207 ? -5.157  -9.930  9.028   1.00 81.57  ? 744  GLN   A CB  1 
ATOM   1503 C CG  . GLN   A 1 207 ? -6.353  -10.584 9.705   1.00 86.86  ? 744  GLN   A CG  1 
ATOM   1504 C CD  . GLN   A 1 207 ? -5.959  -11.423 10.910  1.00 90.27  ? 744  GLN   A CD  1 
ATOM   1505 O OE1 . GLN   A 1 207 ? -5.025  -12.224 10.849  1.00 94.47  ? 744  GLN   A OE1 1 
ATOM   1506 N NE2 . GLN   A 1 207 ? -6.666  -11.232 12.019  1.00 84.60  ? 744  GLN   A NE2 1 
ATOM   1507 N N   . ALA   A 1 208 ? -3.345  -8.143  7.358   1.00 75.73  ? 745  ALA   A N   1 
ATOM   1508 C CA  . ALA   A 1 208 ? -2.010  -7.616  7.080   1.00 71.85  ? 745  ALA   A CA  1 
ATOM   1509 C C   . ALA   A 1 208 ? -1.946  -6.083  7.097   1.00 71.74  ? 745  ALA   A C   1 
ATOM   1510 O O   . ALA   A 1 208 ? -2.900  -5.396  6.726   1.00 74.51  ? 745  ALA   A O   1 
ATOM   1511 C CB  . ALA   A 1 208 ? -1.518  -8.145  5.740   1.00 62.66  ? 745  ALA   A CB  1 
ATOM   1512 N N   . ILE   A 1 217 ? 12.458  -9.786  9.753   1.00 75.28  ? 754  ILE   A N   1 
ATOM   1513 C CA  . ILE   A 1 217 ? 13.466  -10.076 8.735   1.00 73.36  ? 754  ILE   A CA  1 
ATOM   1514 C C   . ILE   A 1 217 ? 14.494  -11.094 9.243   1.00 66.31  ? 754  ILE   A C   1 
ATOM   1515 O O   . ILE   A 1 217 ? 15.086  -10.916 10.310  1.00 63.66  ? 754  ILE   A O   1 
ATOM   1516 C CB  . ILE   A 1 217 ? 14.185  -8.786  8.282   1.00 73.32  ? 754  ILE   A CB  1 
ATOM   1517 C CG1 . ILE   A 1 217 ? 13.223  -7.898  7.491   1.00 73.15  ? 754  ILE   A CG1 1 
ATOM   1518 C CG2 . ILE   A 1 217 ? 15.409  -9.115  7.440   1.00 70.67  ? 754  ILE   A CG2 1 
ATOM   1519 C CD1 . ILE   A 1 217 ? 13.812  -6.568  7.081   1.00 74.68  ? 754  ILE   A CD1 1 
ATOM   1520 N N   . THR   A 1 218 ? 14.699  -12.162 8.474   1.00 64.87  ? 755  THR   A N   1 
ATOM   1521 C CA  . THR   A 1 218 ? 15.617  -13.231 8.869   1.00 69.78  ? 755  THR   A CA  1 
ATOM   1522 C C   . THR   A 1 218 ? 16.759  -13.443 7.875   1.00 66.41  ? 755  THR   A C   1 
ATOM   1523 O O   . THR   A 1 218 ? 16.625  -13.172 6.678   1.00 61.29  ? 755  THR   A O   1 
ATOM   1524 C CB  . THR   A 1 218 ? 14.879  -14.572 9.038   1.00 69.01  ? 755  THR   A CB  1 
ATOM   1525 O OG1 . THR   A 1 218 ? 14.368  -15.003 7.768   1.00 67.88  ? 755  THR   A OG1 1 
ATOM   1526 C CG2 . THR   A 1 218 ? 13.737  -14.433 10.032  1.00 70.53  ? 755  THR   A CG2 1 
ATOM   1527 N N   . PHE   A 1 219 ? 17.877  -13.951 8.384   1.00 58.79  ? 756  PHE   A N   1 
ATOM   1528 C CA  . PHE   A 1 219 ? 19.059  -14.179 7.565   1.00 59.25  ? 756  PHE   A CA  1 
ATOM   1529 C C   . PHE   A 1 219 ? 19.534  -15.630 7.617   1.00 64.30  ? 756  PHE   A C   1 
ATOM   1530 O O   . PHE   A 1 219 ? 19.701  -16.203 8.695   1.00 54.19  ? 756  PHE   A O   1 
ATOM   1531 C CB  . PHE   A 1 219 ? 20.178  -13.237 8.006   1.00 54.86  ? 756  PHE   A CB  1 
ATOM   1532 C CG  . PHE   A 1 219 ? 19.813  -11.780 7.894   1.00 60.04  ? 756  PHE   A CG  1 
ATOM   1533 C CD1 . PHE   A 1 219 ? 19.829  -11.140 6.661   1.00 58.59  ? 756  PHE   A CD1 1 
ATOM   1534 C CD2 . PHE   A 1 219 ? 19.442  -11.054 9.018   1.00 56.41  ? 756  PHE   A CD2 1 
ATOM   1535 C CE1 . PHE   A 1 219 ? 19.490  -9.798  6.552   1.00 59.29  ? 756  PHE   A CE1 1 
ATOM   1536 C CE2 . PHE   A 1 219 ? 19.102  -9.709  8.917   1.00 58.13  ? 756  PHE   A CE2 1 
ATOM   1537 C CZ  . PHE   A 1 219 ? 19.126  -9.082  7.681   1.00 56.05  ? 756  PHE   A CZ  1 
ATOM   1538 N N   . GLU   A 1 220 ? 19.754  -16.210 6.438   1.00 70.02  ? 757  GLU   A N   1 
ATOM   1539 C CA  . GLU   A 1 220 ? 20.217  -17.591 6.313   1.00 77.49  ? 757  GLU   A CA  1 
ATOM   1540 C C   . GLU   A 1 220 ? 21.675  -17.708 6.762   1.00 80.41  ? 757  GLU   A C   1 
ATOM   1541 O O   . GLU   A 1 220 ? 22.084  -18.700 7.364   1.00 74.23  ? 757  GLU   A O   1 
ATOM   1542 C CB  . GLU   A 1 220 ? 20.052  -18.070 4.867   1.00 77.24  ? 757  GLU   A CB  1 
ATOM   1543 C CG  . GLU   A 1 220 ? 19.958  -19.577 4.716   1.00 78.51  ? 757  GLU   A CG  1 
ATOM   1544 C CD  . GLU   A 1 220 ? 21.207  -20.188 4.111   1.00 85.12  ? 757  GLU   A CD  1 
ATOM   1545 O OE1 . GLU   A 1 220 ? 21.537  -21.338 4.469   1.00 84.16  ? 757  GLU   A OE1 1 
ATOM   1546 O OE2 . GLU   A 1 220 ? 21.856  -19.525 3.274   1.00 87.78  ? 757  GLU   A OE2 1 
ATOM   1547 N N   . SER   A 1 221 ? 22.447  -16.672 6.453   1.00 80.78  ? 758  SER   A N   1 
ATOM   1548 C CA  . SER   A 1 221 ? 23.816  -16.523 6.927   1.00 80.22  ? 758  SER   A CA  1 
ATOM   1549 C C   . SER   A 1 221 ? 23.970  -15.098 7.458   1.00 74.60  ? 758  SER   A C   1 
ATOM   1550 O O   . SER   A 1 221 ? 23.343  -14.183 6.935   1.00 71.15  ? 758  SER   A O   1 
ATOM   1551 C CB  . SER   A 1 221 ? 24.812  -16.825 5.801   1.00 80.22  ? 758  SER   A CB  1 
ATOM   1552 O OG  . SER   A 1 221 ? 24.402  -16.225 4.587   1.00 77.46  ? 758  SER   A OG  1 
ATOM   1553 N N   . PRO   A 1 222 ? 24.798  -14.908 8.500   1.00 67.45  ? 759  PRO   A N   1 
ATOM   1554 C CA  . PRO   A 1 222 ? 24.943  -13.596 9.146   1.00 65.77  ? 759  PRO   A CA  1 
ATOM   1555 C C   . PRO   A 1 222 ? 25.325  -12.480 8.175   1.00 56.55  ? 759  PRO   A C   1 
ATOM   1556 O O   . PRO   A 1 222 ? 26.316  -12.617 7.451   1.00 46.55  ? 759  PRO   A O   1 
ATOM   1557 C CB  . PRO   A 1 222 ? 26.067  -13.829 10.163  1.00 64.50  ? 759  PRO   A CB  1 
ATOM   1558 C CG  . PRO   A 1 222 ? 26.007  -15.289 10.451  1.00 67.32  ? 759  PRO   A CG  1 
ATOM   1559 C CD  . PRO   A 1 222 ? 25.631  -15.934 9.150   1.00 70.79  ? 759  PRO   A CD  1 
ATOM   1560 N N   . PRO   A 1 223 ? 24.537  -11.391 8.149   1.00 51.80  ? 760  PRO   A N   1 
ATOM   1561 C CA  . PRO   A 1 223 ? 24.914  -10.233 7.330   1.00 43.13  ? 760  PRO   A CA  1 
ATOM   1562 C C   . PRO   A 1 223 ? 26.187  -9.598  7.860   1.00 38.38  ? 760  PRO   A C   1 
ATOM   1563 O O   . PRO   A 1 223 ? 26.488  -9.731  9.048   1.00 38.70  ? 760  PRO   A O   1 
ATOM   1564 C CB  . PRO   A 1 223 ? 23.718  -9.283  7.479   1.00 41.86  ? 760  PRO   A CB  1 
ATOM   1565 C CG  . PRO   A 1 223 ? 23.067  -9.683  8.756   1.00 48.26  ? 760  PRO   A CG  1 
ATOM   1566 C CD  . PRO   A 1 223 ? 23.273  -11.172 8.874   1.00 46.47  ? 760  PRO   A CD  1 
ATOM   1567 N N   . PRO   A 1 224 ? 26.940  -8.913  6.994   1.00 40.39  ? 761  PRO   A N   1 
ATOM   1568 C CA  . PRO   A 1 224 ? 28.166  -8.276  7.479   1.00 37.33  ? 761  PRO   A CA  1 
ATOM   1569 C C   . PRO   A 1 224 ? 27.876  -7.174  8.499   1.00 38.67  ? 761  PRO   A C   1 
ATOM   1570 O O   . PRO   A 1 224 ? 26.794  -6.584  8.495   1.00 40.84  ? 761  PRO   A O   1 
ATOM   1571 C CB  . PRO   A 1 224 ? 28.796  -7.705  6.200   1.00 38.21  ? 761  PRO   A CB  1 
ATOM   1572 C CG  . PRO   A 1 224 ? 27.661  -7.577  5.235   1.00 37.86  ? 761  PRO   A CG  1 
ATOM   1573 C CD  . PRO   A 1 224 ? 26.741  -8.719  5.550   1.00 39.35  ? 761  PRO   A CD  1 
ATOM   1574 N N   . PRO   A 1 225 ? 28.840  -6.900  9.384   1.00 43.74  ? 762  PRO   A N   1 
ATOM   1575 C CA  . PRO   A 1 225 ? 28.648  -5.821  10.356  1.00 39.09  ? 762  PRO   A CA  1 
ATOM   1576 C C   . PRO   A 1 225 ? 28.485  -4.461  9.682   1.00 39.57  ? 762  PRO   A C   1 
ATOM   1577 O O   . PRO   A 1 225 ? 29.118  -4.212  8.653   1.00 35.51  ? 762  PRO   A O   1 
ATOM   1578 C CB  . PRO   A 1 225 ? 29.935  -5.863  11.185  1.00 46.60  ? 762  PRO   A CB  1 
ATOM   1579 C CG  . PRO   A 1 225 ? 30.942  -6.531  10.287  1.00 46.87  ? 762  PRO   A CG  1 
ATOM   1580 C CD  . PRO   A 1 225 ? 30.160  -7.539  9.514   1.00 43.30  ? 762  PRO   A CD  1 
ATOM   1581 N N   . ILE   A 1 226 ? 27.651  -3.604  10.263  1.00 35.60  ? 763  ILE   A N   1 
ATOM   1582 C CA  . ILE   A 1 226 ? 27.491  -2.230  9.787   1.00 36.88  ? 763  ILE   A CA  1 
ATOM   1583 C C   . ILE   A 1 226 ? 28.833  -1.507  9.853   1.00 37.96  ? 763  ILE   A C   1 
ATOM   1584 O O   . ILE   A 1 226 ? 29.568  -1.646  10.843  1.00 35.76  ? 763  ILE   A O   1 
ATOM   1585 C CB  . ILE   A 1 226 ? 26.453  -1.453  10.632  1.00 38.21  ? 763  ILE   A CB  1 
ATOM   1586 C CG1 . ILE   A 1 226 ? 25.177  -2.275  10.808  1.00 42.48  ? 763  ILE   A CG1 1 
ATOM   1587 C CG2 . ILE   A 1 226 ? 26.163  -0.094  10.030  1.00 33.43  ? 763  ILE   A CG2 1 
ATOM   1588 C CD1 . ILE   A 1 226 ? 24.534  -2.649  9.537   1.00 31.03  ? 763  ILE   A CD1 1 
ATOM   1589 N N   . GLU   A 1 227 ? 29.149  -0.750  8.805   1.00 29.50  ? 764  GLU   A N   1 
ATOM   1590 C CA  . GLU   A 1 227 ? 30.396  0.013   8.736   1.00 32.48  ? 764  GLU   A CA  1 
ATOM   1591 C C   . GLU   A 1 227 ? 30.181  1.472   9.125   1.00 34.64  ? 764  GLU   A C   1 
ATOM   1592 O O   . GLU   A 1 227 ? 29.217  2.108   8.683   1.00 30.89  ? 764  GLU   A O   1 
ATOM   1593 C CB  . GLU   A 1 227 ? 30.988  -0.056  7.325   1.00 31.75  ? 764  GLU   A CB  1 
ATOM   1594 C CG  . GLU   A 1 227 ? 31.344  -1.464  6.863   1.00 30.69  ? 764  GLU   A CG  1 
ATOM   1595 C CD  . GLU   A 1 227 ? 32.731  -1.888  7.305   1.00 42.37  ? 764  GLU   A CD  1 
ATOM   1596 O OE1 . GLU   A 1 227 ? 33.480  -1.033  7.821   1.00 39.61  ? 764  GLU   A OE1 1 
ATOM   1597 O OE2 . GLU   A 1 227 ? 33.073  -3.074  7.130   1.00 40.99  ? 764  GLU   A OE2 1 
ATOM   1598 N N   . TRP   A 1 228 ? 31.088  1.999   9.945   1.00 32.25  ? 765  TRP   A N   1 
ATOM   1599 C CA  . TRP   A 1 228 ? 31.040  3.390   10.375  1.00 31.13  ? 765  TRP   A CA  1 
ATOM   1600 C C   . TRP   A 1 228 ? 32.363  4.085   10.098  1.00 30.78  ? 765  TRP   A C   1 
ATOM   1601 O O   . TRP   A 1 228 ? 33.428  3.467   10.153  1.00 34.15  ? 765  TRP   A O   1 
ATOM   1602 C CB  . TRP   A 1 228 ? 30.697  3.492   11.864  1.00 35.43  ? 765  TRP   A CB  1 
ATOM   1603 C CG  . TRP   A 1 228 ? 29.352  2.909   12.200  1.00 32.91  ? 765  TRP   A CG  1 
ATOM   1604 C CD1 . TRP   A 1 228 ? 29.093  1.642   12.654  1.00 34.32  ? 765  TRP   A CD1 1 
ATOM   1605 C CD2 . TRP   A 1 228 ? 28.085  3.569   12.099  1.00 34.14  ? 765  TRP   A CD2 1 
ATOM   1606 N NE1 . TRP   A 1 228 ? 27.740  1.475   12.831  1.00 35.72  ? 765  TRP   A NE1 1 
ATOM   1607 C CE2 . TRP   A 1 228 ? 27.099  2.643   12.502  1.00 32.11  ? 765  TRP   A CE2 1 
ATOM   1608 C CE3 . TRP   A 1 228 ? 27.685  4.851   11.697  1.00 36.48  ? 765  TRP   A CE3 1 
ATOM   1609 C CZ2 . TRP   A 1 228 ? 25.738  2.960   12.521  1.00 37.85  ? 765  TRP   A CZ2 1 
ATOM   1610 C CZ3 . TRP   A 1 228 ? 26.336  5.165   11.714  1.00 36.01  ? 765  TRP   A CZ3 1 
ATOM   1611 C CH2 . TRP   A 1 228 ? 25.377  4.222   12.127  1.00 34.63  ? 765  TRP   A CH2 1 
ATOM   1612 N N   . HIS   A 1 229 ? 32.276  5.377   9.799   1.00 33.66  ? 766  HIS   A N   1 
ATOM   1613 C CA  . HIS   A 1 229 ? 33.431  6.201   9.459   1.00 32.71  ? 766  HIS   A CA  1 
ATOM   1614 C C   . HIS   A 1 229 ? 33.553  7.292   10.527  1.00 35.03  ? 766  HIS   A C   1 
ATOM   1615 O O   . HIS   A 1 229 ? 33.860  6.990   11.683  1.00 37.86  ? 766  HIS   A O   1 
ATOM   1616 C CB  . HIS   A 1 229 ? 33.273  6.770   8.036   1.00 29.02  ? 766  HIS   A CB  1 
ATOM   1617 C CG  . HIS   A 1 229 ? 34.393  7.666   7.595   1.00 32.55  ? 766  HIS   A CG  1 
ATOM   1618 N ND1 . HIS   A 1 229 ? 35.718  7.405   7.877   1.00 32.77  ? 766  HIS   A ND1 1 
ATOM   1619 C CD2 . HIS   A 1 229 ? 34.377  8.822   6.888   1.00 32.82  ? 766  HIS   A CD2 1 
ATOM   1620 C CE1 . HIS   A 1 229 ? 36.471  8.366   7.367   1.00 34.77  ? 766  HIS   A CE1 1 
ATOM   1621 N NE2 . HIS   A 1 229 ? 35.683  9.241   6.767   1.00 34.39  ? 766  HIS   A NE2 1 
ATOM   1622 N N   . ILE   A 1 230 ? 33.275  8.542   10.177  1.00 31.72  ? 767  ILE   A N   1 
ATOM   1623 C CA  . ILE   A 1 230 ? 33.393  9.635   11.150  1.00 33.35  ? 767  ILE   A CA  1 
ATOM   1624 C C   . ILE   A 1 230 ? 32.142  9.736   12.020  1.00 42.08  ? 767  ILE   A C   1 
ATOM   1625 O O   . ILE   A 1 230 ? 32.243  9.776   13.251  1.00 35.45  ? 767  ILE   A O   1 
ATOM   1626 C CB  . ILE   A 1 230 ? 33.655  10.986  10.467  1.00 35.75  ? 767  ILE   A CB  1 
ATOM   1627 C CG1 . ILE   A 1 230 ? 35.003  10.961  9.751   1.00 36.57  ? 767  ILE   A CG1 1 
ATOM   1628 C CG2 . ILE   A 1 230 ? 33.643  12.114  11.489  1.00 39.85  ? 767  ILE   A CG2 1 
ATOM   1629 C CD1 . ILE   A 1 230 ? 35.219  12.142  8.813   1.00 37.86  ? 767  ILE   A CD1 1 
ATOM   1630 N N   . SER   A 1 231 ? 30.967  9.782   11.391  1.00 32.07  ? 768  SER   A N   1 
ATOM   1631 C CA  . SER   A 1 231 ? 29.709  9.716   12.136  1.00 36.80  ? 768  SER   A CA  1 
ATOM   1632 C C   . SER   A 1 231 ? 29.616  8.374   12.858  1.00 42.52  ? 768  SER   A C   1 
ATOM   1633 O O   . SER   A 1 231 ? 29.916  7.329   12.286  1.00 47.58  ? 768  SER   A O   1 
ATOM   1634 C CB  . SER   A 1 231 ? 28.499  9.907   11.217  1.00 41.67  ? 768  SER   A CB  1 
ATOM   1635 O OG  . SER   A 1 231 ? 28.314  11.272  10.878  1.00 40.37  ? 768  SER   A OG  1 
ATOM   1636 N N   . LYS   A 1 232 ? 29.212  8.413   14.120  1.00 43.86  ? 769  LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 232 ? 29.140  7.206   14.929  1.00 50.61  ? 769  LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 232 ? 27.676  6.849   15.191  1.00 44.32  ? 769  LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 232 ? 26.806  7.712   15.045  1.00 36.96  ? 769  LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 232 ? 29.925  7.406   16.228  1.00 58.42  ? 769  LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 232 ? 31.419  7.573   15.998  1.00 62.26  ? 769  LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 232 ? 31.961  6.458   15.105  1.00 64.76  ? 769  LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 232 ? 33.473  6.554   14.937  1.00 67.72  ? 769  LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 232 ? 33.996  5.508   14.006  1.00 66.12  ? 769  LYS   A NZ  1 
ATOM   1645 N N   . PRO   A 1 233 ? 27.399  5.575   15.542  1.00 42.61  ? 770  PRO   A N   1 
ATOM   1646 C CA  . PRO   A 1 233 ? 26.015  5.139   15.759  1.00 39.11  ? 770  PRO   A CA  1 
ATOM   1647 C C   . PRO   A 1 233 ? 25.228  6.121   16.612  1.00 50.57  ? 770  PRO   A C   1 
ATOM   1648 O O   . PRO   A 1 233 ? 25.747  6.617   17.610  1.00 43.48  ? 770  PRO   A O   1 
ATOM   1649 C CB  . PRO   A 1 233 ? 26.181  3.800   16.480  1.00 48.92  ? 770  PRO   A CB  1 
ATOM   1650 C CG  . PRO   A 1 233 ? 27.475  3.272   15.974  1.00 47.60  ? 770  PRO   A CG  1 
ATOM   1651 C CD  . PRO   A 1 233 ? 28.357  4.465   15.733  1.00 42.67  ? 770  PRO   A CD  1 
ATOM   1652 N N   . GLY   A 1 234 ? 24.006  6.425   16.194  1.00 50.80  ? 771  GLY   A N   1 
ATOM   1653 C CA  . GLY   A 1 234 ? 23.144  7.317   16.948  1.00 52.38  ? 771  GLY   A CA  1 
ATOM   1654 C C   . GLY   A 1 234 ? 23.294  8.796   16.652  1.00 42.31  ? 771  GLY   A C   1 
ATOM   1655 O O   . GLY   A 1 234 ? 22.367  9.562   16.899  1.00 54.38  ? 771  GLY   A O   1 
ATOM   1656 N N   . GLN   A 1 235 ? 24.445  9.204   16.120  1.00 47.10  ? 772  GLN   A N   1 
ATOM   1657 C CA  . GLN   A 1 235 ? 24.711  10.621  15.861  1.00 46.58  ? 772  GLN   A CA  1 
ATOM   1658 C C   . GLN   A 1 235 ? 24.103  11.107  14.548  1.00 40.04  ? 772  GLN   A C   1 
ATOM   1659 O O   . GLN   A 1 235 ? 24.802  11.701  13.733  1.00 41.46  ? 772  GLN   A O   1 
ATOM   1660 C CB  . GLN   A 1 235 ? 26.217  10.888  15.822  1.00 51.15  ? 772  GLN   A CB  1 
ATOM   1661 C CG  . GLN   A 1 235 ? 27.024  10.301  16.962  1.00 65.84  ? 772  GLN   A CG  1 
ATOM   1662 C CD  . GLN   A 1 235 ? 28.518  10.493  16.749  1.00 74.49  ? 772  GLN   A CD  1 
ATOM   1663 O OE1 . GLN   A 1 235 ? 28.978  10.661  15.618  1.00 69.49  ? 772  GLN   A OE1 1 
ATOM   1664 N NE2 . GLN   A 1 235 ? 29.282  10.478  17.837  1.00 83.77  ? 772  GLN   A NE2 1 
ATOM   1665 N N   . PHE   A 1 236 ? 22.813  10.873  14.334  1.00 40.03  ? 773  PHE   A N   1 
ATOM   1666 C CA  . PHE   A 1 236 ? 22.244  11.102  13.006  1.00 41.60  ? 773  PHE   A CA  1 
ATOM   1667 C C   . PHE   A 1 236 ? 22.265  12.574  12.578  1.00 48.29  ? 773  PHE   A C   1 
ATOM   1668 O O   . PHE   A 1 236 ? 22.149  12.880  11.389  1.00 40.87  ? 773  PHE   A O   1 
ATOM   1669 C CB  . PHE   A 1 236 ? 20.820  10.541  12.927  1.00 44.28  ? 773  PHE   A CB  1 
ATOM   1670 C CG  . PHE   A 1 236 ? 19.843  11.211  13.844  1.00 56.89  ? 773  PHE   A CG  1 
ATOM   1671 C CD1 . PHE   A 1 236 ? 19.236  12.405  13.478  1.00 58.11  ? 773  PHE   A CD1 1 
ATOM   1672 C CD2 . PHE   A 1 236 ? 19.500  10.631  15.059  1.00 60.00  ? 773  PHE   A CD2 1 
ATOM   1673 C CE1 . PHE   A 1 236 ? 18.325  13.023  14.314  1.00 57.72  ? 773  PHE   A CE1 1 
ATOM   1674 C CE2 . PHE   A 1 236 ? 18.585  11.241  15.898  1.00 59.03  ? 773  PHE   A CE2 1 
ATOM   1675 C CZ  . PHE   A 1 236 ? 17.998  12.442  15.526  1.00 60.20  ? 773  PHE   A CZ  1 
ATOM   1676 N N   . GLU   A 1 237 ? 22.445  13.482  13.536  1.00 49.23  ? 774  GLU   A N   1 
ATOM   1677 C CA  . GLU   A 1 237 ? 22.524  14.915  13.231  1.00 44.68  ? 774  GLU   A CA  1 
ATOM   1678 C C   . GLU   A 1 237 ? 23.787  15.270  12.436  1.00 40.40  ? 774  GLU   A C   1 
ATOM   1679 O O   . GLU   A 1 237 ? 23.833  16.285  11.750  1.00 42.57  ? 774  GLU   A O   1 
ATOM   1680 C CB  . GLU   A 1 237 ? 22.484  15.748  14.521  1.00 56.90  ? 774  GLU   A CB  1 
ATOM   1681 C CG  . GLU   A 1 237 ? 21.281  15.485  15.416  1.00 68.71  ? 774  GLU   A CG  1 
ATOM   1682 C CD  . GLU   A 1 237 ? 21.476  14.278  16.320  1.00 83.21  ? 774  GLU   A CD  1 
ATOM   1683 O OE1 . GLU   A 1 237 ? 20.523  13.910  17.042  1.00 91.29  ? 774  GLU   A OE1 1 
ATOM   1684 O OE2 . GLU   A 1 237 ? 22.586  13.699  16.310  1.00 82.27  ? 774  GLU   A OE2 1 
ATOM   1685 N N   . THR   A 1 238 ? 24.805  14.423  12.535  1.00 36.10  ? 775  THR   A N   1 
ATOM   1686 C CA  . THR   A 1 238 ? 26.092  14.665  11.888  1.00 44.92  ? 775  THR   A CA  1 
ATOM   1687 C C   . THR   A 1 238 ? 26.232  13.947  10.546  1.00 38.83  ? 775  THR   A C   1 
ATOM   1688 O O   . THR   A 1 238 ? 27.216  14.151  9.829   1.00 37.90  ? 775  THR   A O   1 
ATOM   1689 C CB  . THR   A 1 238 ? 27.256  14.217  12.796  1.00 45.06  ? 775  THR   A CB  1 
ATOM   1690 O OG1 . THR   A 1 238 ? 27.321  12.780  12.838  1.00 42.61  ? 775  THR   A OG1 1 
ATOM   1691 C CG2 . THR   A 1 238 ? 27.064  14.769  14.198  1.00 46.50  ? 775  THR   A CG2 1 
ATOM   1692 N N   . PHE   A 1 239 ? 25.250  13.111  10.217  1.00 34.66  ? 776  PHE   A N   1 
ATOM   1693 C CA  . PHE   A 1 239 ? 25.294  12.308  8.994   1.00 32.46  ? 776  PHE   A CA  1 
ATOM   1694 C C   . PHE   A 1 239 ? 25.442  13.194  7.766   1.00 34.98  ? 776  PHE   A C   1 
ATOM   1695 O O   . PHE   A 1 239 ? 24.769  14.213  7.635   1.00 31.19  ? 776  PHE   A O   1 
ATOM   1696 C CB  . PHE   A 1 239 ? 24.034  11.443  8.849   1.00 30.88  ? 776  PHE   A CB  1 
ATOM   1697 C CG  . PHE   A 1 239 ? 23.961  10.280  9.811   1.00 31.06  ? 776  PHE   A CG  1 
ATOM   1698 C CD1 . PHE   A 1 239 ? 24.936  10.081  10.778  1.00 32.95  ? 776  PHE   A CD1 1 
ATOM   1699 C CD2 . PHE   A 1 239 ? 22.911  9.384   9.737   1.00 31.77  ? 776  PHE   A CD2 1 
ATOM   1700 C CE1 . PHE   A 1 239 ? 24.859  9.000   11.656  1.00 31.57  ? 776  PHE   A CE1 1 
ATOM   1701 C CE2 . PHE   A 1 239 ? 22.825  8.310   10.612  1.00 36.13  ? 776  PHE   A CE2 1 
ATOM   1702 C CZ  . PHE   A 1 239 ? 23.798  8.122   11.578  1.00 30.64  ? 776  PHE   A CZ  1 
ATOM   1703 N N   . ASP   A 1 240 ? 26.338  12.800  6.871   1.00 33.70  ? 777  ASP   A N   1 
ATOM   1704 C CA  . ASP   A 1 240 ? 26.508  13.487  5.599   1.00 31.49  ? 777  ASP   A CA  1 
ATOM   1705 C C   . ASP   A 1 240 ? 27.303  12.580  4.676   1.00 28.55  ? 777  ASP   A C   1 
ATOM   1706 O O   . ASP   A 1 240 ? 27.826  11.549  5.113   1.00 30.97  ? 777  ASP   A O   1 
ATOM   1707 C CB  . ASP   A 1 240 ? 27.206  14.832  5.788   1.00 38.38  ? 777  ASP   A CB  1 
ATOM   1708 C CG  . ASP   A 1 240 ? 26.921  15.801  4.654   1.00 54.52  ? 777  ASP   A CG  1 
ATOM   1709 O OD1 . ASP   A 1 240 ? 26.125  15.450  3.735   1.00 47.90  ? 777  ASP   A OD1 1 
ATOM   1710 O OD2 . ASP   A 1 240 ? 27.495  16.915  4.687   1.00 55.57  ? 777  ASP   A OD2 1 
ATOM   1711 N N   . LEU   A 1 241 ? 27.378  12.937  3.399   1.00 25.68  ? 778  LEU   A N   1 
ATOM   1712 C CA  . LEU   A 1 241 ? 28.060  12.094  2.415   1.00 21.26  ? 778  LEU   A CA  1 
ATOM   1713 C C   . LEU   A 1 241 ? 29.473  11.694  2.839   1.00 26.59  ? 778  LEU   A C   1 
ATOM   1714 O O   . LEU   A 1 241 ? 29.896  10.559  2.634   1.00 28.05  ? 778  LEU   A O   1 
ATOM   1715 C CB  . LEU   A 1 241 ? 28.129  12.814  1.065   1.00 22.10  ? 778  LEU   A CB  1 
ATOM   1716 C CG  . LEU   A 1 241 ? 28.969  12.112  0.005   1.00 30.21  ? 778  LEU   A CG  1 
ATOM   1717 C CD1 . LEU   A 1 241 ? 28.247  10.883  -0.505  1.00 27.59  ? 778  LEU   A CD1 1 
ATOM   1718 C CD2 . LEU   A 1 241 ? 29.281  13.059  -1.134  1.00 36.13  ? 778  LEU   A CD2 1 
ATOM   1719 N N   . MET   A 1 242 ? 30.204  12.631  3.435   1.00 28.02  ? 779  MET   A N   1 
ATOM   1720 C CA  . MET   A 1 242 ? 31.618  12.394  3.689   1.00 24.81  ? 779  MET   A CA  1 
ATOM   1721 C C   . MET   A 1 242 ? 31.898  11.871  5.094   1.00 29.01  ? 779  MET   A C   1 
ATOM   1722 O O   . MET   A 1 242 ? 33.001  11.393  5.362   1.00 31.81  ? 779  MET   A O   1 
ATOM   1723 C CB  . MET   A 1 242 ? 32.410  13.677  3.453   1.00 26.51  ? 779  MET   A CB  1 
ATOM   1724 C CG  . MET   A 1 242 ? 32.410  14.132  1.981   1.00 28.99  ? 779  MET   A CG  1 
ATOM   1725 S SD  . MET   A 1 242 ? 33.320  13.028  0.895   1.00 33.85  ? 779  MET   A SD  1 
ATOM   1726 C CE  . MET   A 1 242 ? 34.977  13.599  1.157   1.00 33.16  ? 779  MET   A CE  1 
ATOM   1727 N N   . THR   A 1 243 ? 30.911  11.959  5.982   1.00 27.22  ? 780  THR   A N   1 
ATOM   1728 C CA  . THR   A 1 243 ? 31.108  11.485  7.353   1.00 27.40  ? 780  THR   A CA  1 
ATOM   1729 C C   . THR   A 1 243 ? 30.561  10.077  7.569   1.00 28.92  ? 780  THR   A C   1 
ATOM   1730 O O   . THR   A 1 243 ? 30.984  9.374   8.480   1.00 30.99  ? 780  THR   A O   1 
ATOM   1731 C CB  . THR   A 1 243 ? 30.463  12.426  8.368   1.00 31.22  ? 780  THR   A CB  1 
ATOM   1732 O OG1 . THR   A 1 243 ? 29.072  12.587  8.055   1.00 36.43  ? 780  THR   A OG1 1 
ATOM   1733 C CG2 . THR   A 1 243 ? 31.157  13.785  8.332   1.00 35.42  ? 780  THR   A CG2 1 
ATOM   1734 N N   . LEU   A 1 244 ? 29.609  9.665   6.741   1.00 24.35  ? 781  LEU   A N   1 
ATOM   1735 C CA  . LEU   A 1 244 ? 29.164  8.271   6.774   1.00 25.72  ? 781  LEU   A CA  1 
ATOM   1736 C C   . LEU   A 1 244 ? 30.195  7.396   6.063   1.00 26.36  ? 781  LEU   A C   1 
ATOM   1737 O O   . LEU   A 1 244 ? 31.078  7.901   5.360   1.00 29.82  ? 781  LEU   A O   1 
ATOM   1738 C CB  . LEU   A 1 244 ? 27.778  8.128   6.130   1.00 25.24  ? 781  LEU   A CB  1 
ATOM   1739 C CG  . LEU   A 1 244 ? 26.624  8.728   6.941   1.00 26.34  ? 781  LEU   A CG  1 
ATOM   1740 C CD1 . LEU   A 1 244 ? 25.360  8.846   6.082   1.00 27.45  ? 781  LEU   A CD1 1 
ATOM   1741 C CD2 . LEU   A 1 244 ? 26.345  7.871   8.191   1.00 25.93  ? 781  LEU   A CD2 1 
ATOM   1742 N N   . HIS   A 1 245 ? 30.107  6.086   6.257   1.00 23.77  ? 782  HIS   A N   1 
ATOM   1743 C CA  . HIS   A 1 245 ? 31.031  5.182   5.583   1.00 28.21  ? 782  HIS   A CA  1 
ATOM   1744 C C   . HIS   A 1 245 ? 30.523  4.882   4.163   1.00 29.31  ? 782  HIS   A C   1 
ATOM   1745 O O   . HIS   A 1 245 ? 29.360  4.533   3.994   1.00 25.37  ? 782  HIS   A O   1 
ATOM   1746 C CB  . HIS   A 1 245 ? 31.196  3.892   6.393   1.00 27.45  ? 782  HIS   A CB  1 
ATOM   1747 C CG  . HIS   A 1 245 ? 32.416  3.109   6.027   1.00 30.40  ? 782  HIS   A CG  1 
ATOM   1748 N ND1 . HIS   A 1 245 ? 32.607  2.568   4.770   1.00 26.39  ? 782  HIS   A ND1 1 
ATOM   1749 C CD2 . HIS   A 1 245 ? 33.523  2.794   6.742   1.00 30.78  ? 782  HIS   A CD2 1 
ATOM   1750 C CE1 . HIS   A 1 245 ? 33.769  1.944   4.736   1.00 26.16  ? 782  HIS   A CE1 1 
ATOM   1751 N NE2 . HIS   A 1 245 ? 34.345  2.061   5.923   1.00 30.05  ? 782  HIS   A NE2 1 
ATOM   1752 N N   . PRO   A 1 246 ? 31.389  5.014   3.137   1.00 26.76  ? 783  PRO   A N   1 
ATOM   1753 C CA  . PRO   A 1 246 ? 30.914  4.818   1.759   1.00 24.23  ? 783  PRO   A CA  1 
ATOM   1754 C C   . PRO   A 1 246 ? 30.343  3.419   1.515   1.00 25.37  ? 783  PRO   A C   1 
ATOM   1755 O O   . PRO   A 1 246 ? 29.378  3.282   0.765   1.00 24.61  ? 783  PRO   A O   1 
ATOM   1756 C CB  . PRO   A 1 246 ? 32.172  5.054   0.908   1.00 25.90  ? 783  PRO   A CB  1 
ATOM   1757 C CG  . PRO   A 1 246 ? 33.330  4.850   1.861   1.00 27.81  ? 783  PRO   A CG  1 
ATOM   1758 C CD  . PRO   A 1 246 ? 32.822  5.359   3.186   1.00 24.55  ? 783  PRO   A CD  1 
ATOM   1759 N N   . ILE   A 1 247 ? 30.912  2.390   2.138   1.00 22.82  ? 784  ILE   A N   1 
ATOM   1760 C CA  . ILE   A 1 247 ? 30.320  1.056   2.018   1.00 21.84  ? 784  ILE   A CA  1 
ATOM   1761 C C   . ILE   A 1 247 ? 28.884  1.062   2.521   1.00 21.65  ? 784  ILE   A C   1 
ATOM   1762 O O   . ILE   A 1 247 ? 27.974  0.517   1.877   1.00 25.60  ? 784  ILE   A O   1 
ATOM   1763 C CB  . ILE   A 1 247 ? 31.099  -0.004  2.812   1.00 28.95  ? 784  ILE   A CB  1 
ATOM   1764 C CG1 . ILE   A 1 247 ? 32.509  -0.162  2.255   1.00 30.01  ? 784  ILE   A CG1 1 
ATOM   1765 C CG2 . ILE   A 1 247 ? 30.361  -1.344  2.773   1.00 33.78  ? 784  ILE   A CG2 1 
ATOM   1766 C CD1 . ILE   A 1 247 ? 33.381  -1.107  3.074   1.00 28.49  ? 784  ILE   A CD1 1 
ATOM   1767 N N   . GLU   A 1 248 ? 28.676  1.692   3.672   1.00 23.72  ? 785  GLU   A N   1 
ATOM   1768 C CA  . GLU   A 1 248 ? 27.364  1.618   4.311   1.00 21.52  ? 785  GLU   A CA  1 
ATOM   1769 C C   . GLU   A 1 248 ? 26.353  2.541   3.620   1.00 22.85  ? 785  GLU   A C   1 
ATOM   1770 O O   . GLU   A 1 248 ? 25.164  2.228   3.576   1.00 23.25  ? 785  GLU   A O   1 
ATOM   1771 C CB  . GLU   A 1 248 ? 27.454  1.939   5.802   1.00 25.99  ? 785  GLU   A CB  1 
ATOM   1772 C CG  . GLU   A 1 248 ? 26.327  1.294   6.612   1.00 27.46  ? 785  GLU   A CG  1 
ATOM   1773 C CD  . GLU   A 1 248 ? 26.266  -0.215  6.448   1.00 27.90  ? 785  GLU   A CD  1 
ATOM   1774 O OE1 . GLU   A 1 248 ? 25.171  -0.734  6.143   1.00 27.78  ? 785  GLU   A OE1 1 
ATOM   1775 O OE2 . GLU   A 1 248 ? 27.307  -0.898  6.613   1.00 30.60  ? 785  GLU   A OE2 1 
ATOM   1776 N N   . ILE   A 1 249 ? 26.813  3.668   3.085   1.00 23.36  ? 786  ILE   A N   1 
ATOM   1777 C CA  . ILE   A 1 249 ? 25.930  4.486   2.244   1.00 22.32  ? 786  ILE   A CA  1 
ATOM   1778 C C   . ILE   A 1 249 ? 25.364  3.627   1.104   1.00 23.79  ? 786  ILE   A C   1 
ATOM   1779 O O   . ILE   A 1 249 ? 24.148  3.581   0.859   1.00 23.19  ? 786  ILE   A O   1 
ATOM   1780 C CB  . ILE   A 1 249 ? 26.670  5.721   1.663   1.00 19.60  ? 786  ILE   A CB  1 
ATOM   1781 C CG1 . ILE   A 1 249 ? 26.971  6.722   2.782   1.00 24.13  ? 786  ILE   A CG1 1 
ATOM   1782 C CG2 . ILE   A 1 249 ? 25.814  6.391   0.557   1.00 19.62  ? 786  ILE   A CG2 1 
ATOM   1783 C CD1 . ILE   A 1 249 ? 27.855  7.902   2.346   1.00 26.30  ? 786  ILE   A CD1 1 
ATOM   1784 N N   . ALA   A 1 250 ? 26.246  2.927   0.404   1.00 22.32  ? 787  ALA   A N   1 
ATOM   1785 C CA  . ALA   A 1 250 ? 25.821  2.089   -0.712  1.00 24.36  ? 787  ALA   A CA  1 
ATOM   1786 C C   . ALA   A 1 250 ? 24.889  0.957   -0.248  1.00 22.14  ? 787  ALA   A C   1 
ATOM   1787 O O   . ALA   A 1 250 ? 23.875  0.673   -0.882  1.00 23.17  ? 787  ALA   A O   1 
ATOM   1788 C CB  . ALA   A 1 250 ? 27.029  1.519   -1.428  1.00 20.57  ? 787  ALA   A CB  1 
ATOM   1789 N N   . ARG   A 1 251 ? 25.216  0.329   0.876   1.00 24.77  ? 788  ARG   A N   1 
ATOM   1790 C CA  . ARG   A 1 251 ? 24.361  -0.739  1.400   1.00 21.75  ? 788  ARG   A CA  1 
ATOM   1791 C C   . ARG   A 1 251 ? 22.971  -0.227  1.747   1.00 24.04  ? 788  ARG   A C   1 
ATOM   1792 O O   . ARG   A 1 251 ? 21.966  -0.849  1.384   1.00 23.70  ? 788  ARG   A O   1 
ATOM   1793 C CB  . ARG   A 1 251 ? 24.975  -1.371  2.644   1.00 21.93  ? 788  ARG   A CB  1 
ATOM   1794 C CG  . ARG   A 1 251 ? 26.156  -2.269  2.377   1.00 26.69  ? 788  ARG   A CG  1 
ATOM   1795 C CD  . ARG   A 1 251 ? 26.739  -2.681  3.713   1.00 27.24  ? 788  ARG   A CD  1 
ATOM   1796 N NE  . ARG   A 1 251 ? 27.896  -3.551  3.579   1.00 30.11  ? 788  ARG   A NE  1 
ATOM   1797 C CZ  . ARG   A 1 251 ? 28.659  -3.907  4.607   1.00 32.75  ? 788  ARG   A CZ  1 
ATOM   1798 N NH1 . ARG   A 1 251 ? 28.375  -3.453  5.822   1.00 27.38  ? 788  ARG   A NH1 1 
ATOM   1799 N NH2 . ARG   A 1 251 ? 29.692  -4.717  4.423   1.00 30.46  ? 788  ARG   A NH2 1 
ATOM   1800 N N   . GLN   A 1 252 ? 22.914  0.889   2.468   1.00 24.06  ? 789  GLN   A N   1 
ATOM   1801 C CA  . GLN   A 1 252 ? 21.623  1.354   2.970   1.00 23.56  ? 789  GLN   A CA  1 
ATOM   1802 C C   . GLN   A 1 252 ? 20.770  1.875   1.827   1.00 27.69  ? 789  GLN   A C   1 
ATOM   1803 O O   . GLN   A 1 252 ? 19.540  1.685   1.812   1.00 21.74  ? 789  GLN   A O   1 
ATOM   1804 C CB  . GLN   A 1 252 ? 21.803  2.423   4.046   1.00 20.47  ? 789  GLN   A CB  1 
ATOM   1805 C CG  . GLN   A 1 252 ? 22.441  1.886   5.350   1.00 22.78  ? 789  GLN   A CG  1 
ATOM   1806 C CD  . GLN   A 1 252 ? 21.691  0.686   5.922   1.00 31.55  ? 789  GLN   A CD  1 
ATOM   1807 O OE1 . GLN   A 1 252 ? 20.457  0.700   6.036   1.00 27.10  ? 789  GLN   A OE1 1 
ATOM   1808 N NE2 . GLN   A 1 252 ? 22.434  -0.365  6.278   1.00 27.94  ? 789  GLN   A NE2 1 
ATOM   1809 N N   . LEU   A 1 253 ? 21.416  2.525   0.860   1.00 23.01  ? 790  LEU   A N   1 
ATOM   1810 C CA  . LEU   A 1 253 ? 20.677  2.981   -0.324  1.00 22.28  ? 790  LEU   A CA  1 
ATOM   1811 C C   . LEU   A 1 253 ? 20.206  1.797   -1.161  1.00 24.49  ? 790  LEU   A C   1 
ATOM   1812 O O   . LEU   A 1 253 ? 19.130  1.841   -1.769  1.00 24.39  ? 790  LEU   A O   1 
ATOM   1813 C CB  . LEU   A 1 253 ? 21.528  3.928   -1.177  1.00 20.52  ? 790  LEU   A CB  1 
ATOM   1814 C CG  . LEU   A 1 253 ? 21.537  5.380   -0.661  1.00 20.49  ? 790  LEU   A CG  1 
ATOM   1815 C CD1 . LEU   A 1 253 ? 22.610  6.209   -1.372  1.00 20.77  ? 790  LEU   A CD1 1 
ATOM   1816 C CD2 . LEU   A 1 253 ? 20.178  6.067   -0.820  1.00 21.12  ? 790  LEU   A CD2 1 
ATOM   1817 N N   . THR   A 1 254 ? 21.002  0.736   -1.204  1.00 23.08  ? 791  THR   A N   1 
ATOM   1818 C CA  . THR   A 1 254 ? 20.596  -0.455  -1.939  1.00 25.77  ? 791  THR   A CA  1 
ATOM   1819 C C   . THR   A 1 254 ? 19.397  -1.122  -1.265  1.00 24.83  ? 791  THR   A C   1 
ATOM   1820 O O   . THR   A 1 254 ? 18.455  -1.543  -1.946  1.00 23.31  ? 791  THR   A O   1 
ATOM   1821 C CB  . THR   A 1 254 ? 21.757  -1.439  -2.080  1.00 24.88  ? 791  THR   A CB  1 
ATOM   1822 O OG1 . THR   A 1 254 ? 22.749  -0.837  -2.922  1.00 23.97  ? 791  THR   A OG1 1 
ATOM   1823 C CG2 . THR   A 1 254 ? 21.293  -2.768  -2.732  1.00 25.01  ? 791  THR   A CG2 1 
ATOM   1824 N N   . LEU   A 1 255 ? 19.409  -1.209  0.061   1.00 24.03  ? 792  LEU   A N   1 
ATOM   1825 C CA  . LEU   A 1 255 ? 18.244  -1.757  0.781   1.00 24.75  ? 792  LEU   A CA  1 
ATOM   1826 C C   . LEU   A 1 255 ? 16.997  -0.910  0.528   1.00 27.16  ? 792  LEU   A C   1 
ATOM   1827 O O   . LEU   A 1 255 ? 15.915  -1.442  0.281   1.00 27.02  ? 792  LEU   A O   1 
ATOM   1828 C CB  . LEU   A 1 255 ? 18.516  -1.844  2.286   1.00 26.10  ? 792  LEU   A CB  1 
ATOM   1829 C CG  . LEU   A 1 255 ? 19.478  -2.962  2.685   1.00 26.24  ? 792  LEU   A CG  1 
ATOM   1830 C CD1 . LEU   A 1 255 ? 19.838  -2.847  4.164   1.00 28.33  ? 792  LEU   A CD1 1 
ATOM   1831 C CD2 . LEU   A 1 255 ? 18.868  -4.326  2.390   1.00 28.34  ? 792  LEU   A CD2 1 
ATOM   1832 N N   . LEU   A 1 256 ? 17.151  0.410   0.590   1.00 22.93  ? 793  LEU   A N   1 
ATOM   1833 C CA  . LEU   A 1 256 ? 16.036  1.312   0.337   1.00 27.12  ? 793  LEU   A CA  1 
ATOM   1834 C C   . LEU   A 1 256 ? 15.502  1.142   -1.087  1.00 28.49  ? 793  LEU   A C   1 
ATOM   1835 O O   . LEU   A 1 256 ? 14.297  0.990   -1.292  1.00 26.34  ? 793  LEU   A O   1 
ATOM   1836 C CB  . LEU   A 1 256 ? 16.461  2.765   0.591   1.00 23.52  ? 793  LEU   A CB  1 
ATOM   1837 C CG  . LEU   A 1 256 ? 15.473  3.896   0.302   1.00 27.66  ? 793  LEU   A CG  1 
ATOM   1838 C CD1 . LEU   A 1 256 ? 14.126  3.592   0.943   1.00 31.13  ? 793  LEU   A CD1 1 
ATOM   1839 C CD2 . LEU   A 1 256 ? 16.023  5.224   0.817   1.00 27.43  ? 793  LEU   A CD2 1 
ATOM   1840 N N   . GLU   A 1 257 ? 16.394  1.162   -2.073  1.00 21.23  ? 794  GLU   A N   1 
ATOM   1841 C CA  . GLU   A 1 257 ? 15.973  1.095   -3.478  1.00 22.82  ? 794  GLU   A CA  1 
ATOM   1842 C C   . GLU   A 1 257 ? 15.390  -0.274  -3.823  1.00 28.46  ? 794  GLU   A C   1 
ATOM   1843 O O   . GLU   A 1 257 ? 14.472  -0.382  -4.641  1.00 24.93  ? 794  GLU   A O   1 
ATOM   1844 C CB  . GLU   A 1 257 ? 17.157  1.439   -4.382  1.00 24.07  ? 794  GLU   A CB  1 
ATOM   1845 C CG  . GLU   A 1 257 ? 17.506  2.916   -4.221  1.00 27.69  ? 794  GLU   A CG  1 
ATOM   1846 C CD  . GLU   A 1 257 ? 18.724  3.376   -5.004  1.00 31.02  ? 794  GLU   A CD  1 
ATOM   1847 O OE1 . GLU   A 1 257 ? 19.053  4.570   -4.872  1.00 27.16  ? 794  GLU   A OE1 1 
ATOM   1848 O OE2 . GLU   A 1 257 ? 19.345  2.576   -5.735  1.00 29.60  ? 794  GLU   A OE2 1 
ATOM   1849 N N   . SER   A 1 258 ? 15.917  -1.315  -3.188  1.00 23.99  ? 795  SER   A N   1 
ATOM   1850 C CA  . SER   A 1 258 ? 15.375  -2.658  -3.359  1.00 22.40  ? 795  SER   A CA  1 
ATOM   1851 C C   . SER   A 1 258 ? 13.927  -2.705  -2.862  1.00 25.82  ? 795  SER   A C   1 
ATOM   1852 O O   . SER   A 1 258 ? 13.040  -3.255  -3.525  1.00 26.92  ? 795  SER   A O   1 
ATOM   1853 C CB  . SER   A 1 258 ? 16.225  -3.682  -2.606  1.00 27.18  ? 795  SER   A CB  1 
ATOM   1854 O OG  . SER   A 1 258 ? 15.591  -4.948  -2.615  1.00 30.15  ? 795  SER   A OG  1 
ATOM   1855 N N   . ASP   A 1 259 ? 13.693  -2.111  -1.698  1.00 25.75  ? 796  ASP   A N   1 
ATOM   1856 C CA  . ASP   A 1 259 ? 12.347  -2.067  -1.127  1.00 28.30  ? 796  ASP   A CA  1 
ATOM   1857 C C   . ASP   A 1 259 ? 11.379  -1.283  -2.015  1.00 32.39  ? 796  ASP   A C   1 
ATOM   1858 O O   . ASP   A 1 259 ? 10.252  -1.722  -2.240  1.00 30.39  ? 796  ASP   A O   1 
ATOM   1859 C CB  . ASP   A 1 259 ? 12.373  -1.458  0.276   1.00 28.21  ? 796  ASP   A CB  1 
ATOM   1860 C CG  . ASP   A 1 259 ? 12.807  -2.454  1.340   1.00 38.66  ? 796  ASP   A CG  1 
ATOM   1861 O OD1 . ASP   A 1 259 ? 12.800  -3.668  1.054   1.00 49.98  ? 796  ASP   A OD1 1 
ATOM   1862 O OD2 . ASP   A 1 259 ? 13.149  -2.021  2.463   1.00 42.26  ? 796  ASP   A OD2 1 
ATOM   1863 N N   . LEU   A 1 260 ? 11.819  -0.127  -2.509  1.00 26.39  ? 797  LEU   A N   1 
ATOM   1864 C CA  . LEU   A 1 260 ? 10.992  0.680   -3.407  1.00 23.97  ? 797  LEU   A CA  1 
ATOM   1865 C C   . LEU   A 1 260 ? 10.659  -0.079  -4.681  1.00 28.30  ? 797  LEU   A C   1 
ATOM   1866 O O   . LEU   A 1 260 ? 9.518   -0.058  -5.153  1.00 26.82  ? 797  LEU   A O   1 
ATOM   1867 C CB  . LEU   A 1 260 ? 11.696  1.985   -3.766  1.00 23.95  ? 797  LEU   A CB  1 
ATOM   1868 C CG  . LEU   A 1 260 ? 11.882  2.928   -2.582  1.00 28.36  ? 797  LEU   A CG  1 
ATOM   1869 C CD1 . LEU   A 1 260 ? 12.770  4.098   -2.997  1.00 31.20  ? 797  LEU   A CD1 1 
ATOM   1870 C CD2 . LEU   A 1 260 ? 10.515  3.410   -2.074  1.00 30.71  ? 797  LEU   A CD2 1 
ATOM   1871 N N   . TYR   A 1 261 ? 11.663  -0.744  -5.243  1.00 24.38  ? 798  TYR   A N   1 
ATOM   1872 C CA  . TYR   A 1 261 ? 11.477  -1.481  -6.492  1.00 25.80  ? 798  TYR   A CA  1 
ATOM   1873 C C   . TYR   A 1 261 ? 10.478  -2.607  -6.306  1.00 30.17  ? 798  TYR   A C   1 
ATOM   1874 O O   . TYR   A 1 261 ? 9.579   -2.801  -7.130  1.00 26.33  ? 798  TYR   A O   1 
ATOM   1875 C CB  . TYR   A 1 261 ? 12.824  -2.034  -6.980  1.00 26.52  ? 798  TYR   A CB  1 
ATOM   1876 C CG  . TYR   A 1 261 ? 12.762  -2.824  -8.267  1.00 29.56  ? 798  TYR   A CG  1 
ATOM   1877 C CD1 . TYR   A 1 261 ? 12.539  -4.201  -8.260  1.00 32.49  ? 798  TYR   A CD1 1 
ATOM   1878 C CD2 . TYR   A 1 261 ? 12.943  -2.199  -9.492  1.00 32.63  ? 798  TYR   A CD2 1 
ATOM   1879 C CE1 . TYR   A 1 261 ? 12.480  -4.922  -9.439  1.00 33.13  ? 798  TYR   A CE1 1 
ATOM   1880 C CE2 . TYR   A 1 261 ? 12.889  -2.912  -10.676 1.00 32.61  ? 798  TYR   A CE2 1 
ATOM   1881 C CZ  . TYR   A 1 261 ? 12.655  -4.269  -10.643 1.00 33.27  ? 798  TYR   A CZ  1 
ATOM   1882 O OH  . TYR   A 1 261 ? 12.608  -4.974  -11.826 1.00 35.73  ? 798  TYR   A OH  1 
ATOM   1883 N N   A ARG   A 1 262 ? 10.635  -3.335  -5.203  0.59 26.19  ? 799  ARG   A N   1 
ATOM   1884 N N   B ARG   A 1 262 ? 10.639  -3.346  -5.212  0.41 27.00  ? 799  ARG   A N   1 
ATOM   1885 C CA  A ARG   A 1 262 ? 9.822   -4.514  -4.908  0.59 29.15  ? 799  ARG   A CA  1 
ATOM   1886 C CA  B ARG   A 1 262 ? 9.813   -4.518  -4.932  0.41 28.54  ? 799  ARG   A CA  1 
ATOM   1887 C C   A ARG   A 1 262 ? 8.341   -4.177  -4.775  0.59 30.07  ? 799  ARG   A C   1 
ATOM   1888 C C   B ARG   A 1 262 ? 8.333   -4.164  -4.815  0.41 29.77  ? 799  ARG   A C   1 
ATOM   1889 O O   A ARG   A 1 262 ? 7.479   -5.005  -5.072  0.59 27.86  ? 799  ARG   A O   1 
ATOM   1890 O O   B ARG   A 1 262 ? 7.464   -4.966  -5.168  0.41 28.80  ? 799  ARG   A O   1 
ATOM   1891 C CB  A ARG   A 1 262 ? 10.321  -5.185  -3.623  0.59 32.62  ? 799  ARG   A CB  1 
ATOM   1892 C CB  B ARG   A 1 262 ? 10.298  -5.204  -3.650  0.41 32.92  ? 799  ARG   A CB  1 
ATOM   1893 C CG  A ARG   A 1 262 ? 9.470   -6.350  -3.133  0.59 42.74  ? 799  ARG   A CG  1 
ATOM   1894 C CG  B ARG   A 1 262 ? 9.326   -6.217  -3.054  0.41 41.16  ? 799  ARG   A CG  1 
ATOM   1895 C CD  A ARG   A 1 262 ? 10.009  -6.935  -1.824  0.59 49.82  ? 799  ARG   A CD  1 
ATOM   1896 C CD  B ARG   A 1 262 ? 9.966   -7.047  -1.941  0.41 48.01  ? 799  ARG   A CD  1 
ATOM   1897 N NE  A ARG   A 1 262 ? 10.191  -5.921  -0.786  0.59 48.62  ? 799  ARG   A NE  1 
ATOM   1898 N NE  B ARG   A 1 262 ? 10.754  -6.242  -1.011  0.41 50.52  ? 799  ARG   A NE  1 
ATOM   1899 C CZ  A ARG   A 1 262 ? 9.214   -5.446  -0.019  0.59 46.05  ? 799  ARG   A CZ  1 
ATOM   1900 C CZ  B ARG   A 1 262 ? 12.083  -6.259  -0.953  0.41 49.51  ? 799  ARG   A CZ  1 
ATOM   1901 N NH1 A ARG   A 1 262 ? 7.970   -5.881  -0.172  0.59 43.48  ? 799  ARG   A NH1 1 
ATOM   1902 N NH1 B ARG   A 1 262 ? 12.771  -7.043  -1.767  0.41 47.90  ? 799  ARG   A NH1 1 
ATOM   1903 N NH2 A ARG   A 1 262 ? 9.479   -4.526  0.896   0.59 48.05  ? 799  ARG   A NH2 1 
ATOM   1904 N NH2 B ARG   A 1 262 ? 12.725  -5.500  -0.079  0.41 45.96  ? 799  ARG   A NH2 1 
ATOM   1905 N N   . LYS   A 1 263 ? 8.044   -2.958  -4.341  1.00 26.39  ? 800  LYS   A N   1 
ATOM   1906 C CA  . LYS   A 1 263 ? 6.658   -2.566  -4.092  1.00 24.50  ? 800  LYS   A CA  1 
ATOM   1907 C C   . LYS   A 1 263 ? 5.891   -2.061  -5.310  1.00 27.43  ? 800  LYS   A C   1 
ATOM   1908 O O   . LYS   A 1 263 ? 4.684   -1.807  -5.214  1.00 29.15  ? 800  LYS   A O   1 
ATOM   1909 C CB  . LYS   A 1 263 ? 6.614   -1.496  -2.994  1.00 26.15  ? 800  LYS   A CB  1 
ATOM   1910 C CG  . LYS   A 1 263 ? 6.946   -2.054  -1.618  1.00 32.83  ? 800  LYS   A CG  1 
ATOM   1911 C CD  . LYS   A 1 263 ? 7.049   -0.968  -0.566  1.00 42.24  ? 800  LYS   A CD  1 
ATOM   1912 C CE  . LYS   A 1 263 ? 7.354   -1.584  0.790   1.00 54.01  ? 800  LYS   A CE  1 
ATOM   1913 N NZ  . LYS   A 1 263 ? 7.846   -0.576  1.767   1.00 57.82  ? 800  LYS   A NZ  1 
ATOM   1914 N N   . VAL   A 1 264 ? 6.561   -1.912  -6.448  1.00 23.91  ? 801  VAL   A N   1 
ATOM   1915 C CA  . VAL   A 1 264 ? 5.864   -1.414  -7.640  1.00 27.29  ? 801  VAL   A CA  1 
ATOM   1916 C C   . VAL   A 1 264 ? 4.981   -2.498  -8.270  1.00 28.22  ? 801  VAL   A C   1 
ATOM   1917 O O   . VAL   A 1 264 ? 5.453   -3.578  -8.610  1.00 29.41  ? 801  VAL   A O   1 
ATOM   1918 C CB  . VAL   A 1 264 ? 6.843   -0.885  -8.699  1.00 23.82  ? 801  VAL   A CB  1 
ATOM   1919 C CG1 . VAL   A 1 264 ? 6.077   -0.445  -9.953  1.00 26.41  ? 801  VAL   A CG1 1 
ATOM   1920 C CG2 . VAL   A 1 264 ? 7.624   0.306   -8.139  1.00 22.24  ? 801  VAL   A CG2 1 
ATOM   1921 N N   . GLN   A 1 265 ? 3.691   -2.203  -8.390  1.00 27.56  ? 802  GLN   A N   1 
ATOM   1922 C CA  . GLN   A 1 265 ? 2.758   -3.095  -9.070  1.00 25.56  ? 802  GLN   A CA  1 
ATOM   1923 C C   . GLN   A 1 265 ? 2.671   -2.718  -10.544 1.00 28.06  ? 802  GLN   A C   1 
ATOM   1924 O O   . GLN   A 1 265 ? 2.630   -1.538  -10.877 1.00 29.40  ? 802  GLN   A O   1 
ATOM   1925 C CB  . GLN   A 1 265 ? 1.362   -3.013  -8.432  1.00 27.89  ? 802  GLN   A CB  1 
ATOM   1926 C CG  . GLN   A 1 265 ? 1.359   -3.326  -6.948  1.00 32.40  ? 802  GLN   A CG  1 
ATOM   1927 C CD  . GLN   A 1 265 ? 1.989   -4.675  -6.663  1.00 42.88  ? 802  GLN   A CD  1 
ATOM   1928 O OE1 . GLN   A 1 265 ? 1.588   -5.690  -7.237  1.00 37.19  ? 802  GLN   A OE1 1 
ATOM   1929 N NE2 . GLN   A 1 265 ? 2.997   -4.690  -5.798  1.00 41.37  ? 802  GLN   A NE2 1 
ATOM   1930 N N   . PRO   A 1 266 ? 2.614   -3.725  -11.428 1.00 28.31  ? 803  PRO   A N   1 
ATOM   1931 C CA  . PRO   A 1 266 ? 2.491   -3.538  -12.882 1.00 27.08  ? 803  PRO   A CA  1 
ATOM   1932 C C   . PRO   A 1 266 ? 1.385   -2.560  -13.303 1.00 26.85  ? 803  PRO   A C   1 
ATOM   1933 O O   . PRO   A 1 266 ? 1.605   -1.774  -14.213 1.00 31.13  ? 803  PRO   A O   1 
ATOM   1934 C CB  . PRO   A 1 266 ? 2.177   -4.953  -13.381 1.00 31.30  ? 803  PRO   A CB  1 
ATOM   1935 C CG  . PRO   A 1 266 ? 2.873   -5.835  -12.406 1.00 36.14  ? 803  PRO   A CG  1 
ATOM   1936 C CD  . PRO   A 1 266 ? 2.786   -5.144  -11.067 1.00 27.01  ? 803  PRO   A CD  1 
ATOM   1937 N N   . SER   A 1 267 ? 0.231   -2.590  -12.642 1.00 28.73  ? 804  SER   A N   1 
ATOM   1938 C CA  . SER   A 1 267 ? -0.871  -1.703  -13.017 1.00 27.58  ? 804  SER   A CA  1 
ATOM   1939 C C   . SER   A 1 267 ? -0.530  -0.225  -12.814 1.00 28.21  ? 804  SER   A C   1 
ATOM   1940 O O   . SER   A 1 267 ? -1.184  0.646   -13.388 1.00 29.76  ? 804  SER   A O   1 
ATOM   1941 C CB  . SER   A 1 267 ? -2.141  -2.041  -12.225 1.00 28.97  ? 804  SER   A CB  1 
ATOM   1942 O OG  . SER   A 1 267 ? -1.959  -1.787  -10.838 1.00 27.44  ? 804  SER   A OG  1 
ATOM   1943 N N   . GLU   A 1 268 ? 0.476   0.063   -11.985 1.00 25.01  ? 805  GLU   A N   1 
ATOM   1944 C CA  . GLU   A 1 268 ? 0.915   1.448   -11.777 1.00 23.50  ? 805  GLU   A CA  1 
ATOM   1945 C C   . GLU   A 1 268 ? 1.593   1.995   -13.031 1.00 28.93  ? 805  GLU   A C   1 
ATOM   1946 O O   . GLU   A 1 268 ? 1.730   3.205   -13.183 1.00 26.43  ? 805  GLU   A O   1 
ATOM   1947 C CB  . GLU   A 1 268 ? 1.875   1.557   -10.578 1.00 21.45  ? 805  GLU   A CB  1 
ATOM   1948 C CG  . GLU   A 1 268 ? 1.301   0.952   -9.291  1.00 26.16  ? 805  GLU   A CG  1 
ATOM   1949 C CD  . GLU   A 1 268 ? 2.175   1.223   -8.063  1.00 29.51  ? 805  GLU   A CD  1 
ATOM   1950 O OE1 . GLU   A 1 268 ? 2.624   2.381   -7.898  1.00 29.48  ? 805  GLU   A OE1 1 
ATOM   1951 O OE2 . GLU   A 1 268 ? 2.392   0.280   -7.264  1.00 33.73  ? 805  GLU   A OE2 1 
ATOM   1952 N N   . LEU   A 1 269 ? 2.005   1.094   -13.917 1.00 29.60  ? 806  LEU   A N   1 
ATOM   1953 C CA  . LEU   A 1 269 ? 2.683   1.447   -15.165 1.00 30.76  ? 806  LEU   A CA  1 
ATOM   1954 C C   . LEU   A 1 269 ? 1.763   1.451   -16.384 1.00 32.57  ? 806  LEU   A C   1 
ATOM   1955 O O   . LEU   A 1 269 ? 2.034   2.114   -17.387 1.00 40.74  ? 806  LEU   A O   1 
ATOM   1956 C CB  . LEU   A 1 269 ? 3.825   0.471   -15.402 1.00 28.86  ? 806  LEU   A CB  1 
ATOM   1957 C CG  . LEU   A 1 269 ? 4.927   0.623   -14.339 1.00 33.33  ? 806  LEU   A CG  1 
ATOM   1958 C CD1 . LEU   A 1 269 ? 5.359   -0.710  -13.790 1.00 38.66  ? 806  LEU   A CD1 1 
ATOM   1959 C CD2 . LEU   A 1 269 ? 6.097   1.332   -14.940 1.00 43.86  ? 806  LEU   A CD2 1 
ATOM   1960 N N   . VAL   A 1 270 ? 0.678   0.700   -16.307 1.00 27.62  ? 807  VAL   A N   1 
ATOM   1961 C CA  . VAL   A 1 270 ? -0.208  0.556   -17.464 1.00 24.47  ? 807  VAL   A CA  1 
ATOM   1962 C C   . VAL   A 1 270 ? -0.924  1.866   -17.786 1.00 34.55  ? 807  VAL   A C   1 
ATOM   1963 O O   . VAL   A 1 270 ? -1.356  2.583   -16.888 1.00 34.92  ? 807  VAL   A O   1 
ATOM   1964 C CB  . VAL   A 1 270 ? -1.252  -0.556  -17.232 1.00 28.99  ? 807  VAL   A CB  1 
ATOM   1965 C CG1 . VAL   A 1 270 ? -2.248  -0.631  -18.402 1.00 31.60  ? 807  VAL   A CG1 1 
ATOM   1966 C CG2 . VAL   A 1 270 ? -0.571  -1.895  -17.052 1.00 29.04  ? 807  VAL   A CG2 1 
ATOM   1967 N N   . GLY   A 1 271 ? -1.047  2.179   -19.072 1.00 35.25  ? 808  GLY   A N   1 
ATOM   1968 C CA  . GLY   A 1 271 ? -1.809  3.340   -19.497 1.00 37.17  ? 808  GLY   A CA  1 
ATOM   1969 C C   . GLY   A 1 271 ? -1.120  4.647   -19.145 1.00 37.71  ? 808  GLY   A C   1 
ATOM   1970 O O   . GLY   A 1 271 ? -1.740  5.713   -19.187 1.00 37.56  ? 808  GLY   A O   1 
ATOM   1971 N N   . SER   A 1 272 ? 0.162   4.560   -18.796 1.00 32.48  ? 809  SER   A N   1 
ATOM   1972 C CA  . SER   A 1 272 ? 0.939   5.721   -18.357 1.00 35.67  ? 809  SER   A CA  1 
ATOM   1973 C C   . SER   A 1 272 ? 0.230   6.483   -17.242 1.00 35.14  ? 809  SER   A C   1 
ATOM   1974 O O   . SER   A 1 272 ? 0.273   7.712   -17.210 1.00 35.32  ? 809  SER   A O   1 
ATOM   1975 C CB  . SER   A 1 272 ? 1.217   6.674   -19.526 1.00 47.81  ? 809  SER   A CB  1 
ATOM   1976 O OG  . SER   A 1 272 ? 1.871   6.014   -20.593 1.00 51.99  ? 809  SER   A OG  1 
ATOM   1977 N N   . VAL   A 1 273 ? -0.416  5.760   -16.327 1.00 31.91  ? 810  VAL   A N   1 
ATOM   1978 C CA  . VAL   A 1 273 ? -1.243  6.414   -15.319 1.00 33.72  ? 810  VAL   A CA  1 
ATOM   1979 C C   . VAL   A 1 273 ? -0.426  7.272   -14.345 1.00 32.22  ? 810  VAL   A C   1 
ATOM   1980 O O   . VAL   A 1 273 ? -0.974  8.182   -13.724 1.00 36.47  ? 810  VAL   A O   1 
ATOM   1981 C CB  . VAL   A 1 273 ? -2.086  5.400   -14.506 1.00 31.87  ? 810  VAL   A CB  1 
ATOM   1982 C CG1 . VAL   A 1 273 ? -3.340  5.027   -15.271 1.00 41.30  ? 810  VAL   A CG1 1 
ATOM   1983 C CG2 . VAL   A 1 273 ? -1.267  4.160   -14.124 1.00 25.69  ? 810  VAL   A CG2 1 
ATOM   1984 N N   . TRP   A 1 274 ? 0.876   7.004   -14.220 1.00 31.21  ? 811  TRP   A N   1 
ATOM   1985 C CA  . TRP   A 1 274 ? 1.715   7.771   -13.295 1.00 32.65  ? 811  TRP   A CA  1 
ATOM   1986 C C   . TRP   A 1 274 ? 1.981   9.184   -13.812 1.00 29.15  ? 811  TRP   A C   1 
ATOM   1987 O O   . TRP   A 1 274 ? 2.510   10.030  -13.088 1.00 32.68  ? 811  TRP   A O   1 
ATOM   1988 C CB  . TRP   A 1 274 ? 3.045   7.042   -13.026 1.00 28.77  ? 811  TRP   A CB  1 
ATOM   1989 C CG  . TRP   A 1 274 ? 4.101   7.193   -14.093 1.00 29.76  ? 811  TRP   A CG  1 
ATOM   1990 C CD1 . TRP   A 1 274 ? 5.092   8.141   -14.142 1.00 31.45  ? 811  TRP   A CD1 1 
ATOM   1991 C CD2 . TRP   A 1 274 ? 4.295   6.349   -15.242 1.00 28.47  ? 811  TRP   A CD2 1 
ATOM   1992 N NE1 . TRP   A 1 274 ? 5.878   7.940   -15.257 1.00 36.25  ? 811  TRP   A NE1 1 
ATOM   1993 C CE2 . TRP   A 1 274 ? 5.411   6.852   -15.946 1.00 31.56  ? 811  TRP   A CE2 1 
ATOM   1994 C CE3 . TRP   A 1 274 ? 3.635   5.220   -15.737 1.00 31.87  ? 811  TRP   A CE3 1 
ATOM   1995 C CZ2 . TRP   A 1 274 ? 5.879   6.261   -17.125 1.00 30.00  ? 811  TRP   A CZ2 1 
ATOM   1996 C CZ3 . TRP   A 1 274 ? 4.093   4.638   -16.907 1.00 36.37  ? 811  TRP   A CZ3 1 
ATOM   1997 C CH2 . TRP   A 1 274 ? 5.206   5.161   -17.591 1.00 35.48  ? 811  TRP   A CH2 1 
ATOM   1998 N N   . THR   A 1 275 ? 1.604   9.444   -15.059 1.00 31.35  ? 812  THR   A N   1 
ATOM   1999 C CA  . THR   A 1 275 ? 1.816   10.756  -15.656 1.00 35.95  ? 812  THR   A CA  1 
ATOM   2000 C C   . THR   A 1 275 ? 0.514   11.525  -15.792 1.00 44.26  ? 812  THR   A C   1 
ATOM   2001 O O   . THR   A 1 275 ? 0.485   12.598  -16.389 1.00 38.23  ? 812  THR   A O   1 
ATOM   2002 C CB  . THR   A 1 275 ? 2.459   10.655  -17.050 1.00 33.63  ? 812  THR   A CB  1 
ATOM   2003 O OG1 . THR   A 1 275 ? 1.512   10.102  -17.971 1.00 36.30  ? 812  THR   A OG1 1 
ATOM   2004 C CG2 . THR   A 1 275 ? 3.703   9.773   -17.013 1.00 33.34  ? 812  THR   A CG2 1 
ATOM   2005 N N   . LYS   A 1 276 ? -0.561  10.974  -15.240 1.00 42.13  ? 813  LYS   A N   1 
ATOM   2006 C CA  . LYS   A 1 276 ? -1.886  11.536  -15.454 1.00 48.20  ? 813  LYS   A CA  1 
ATOM   2007 C C   . LYS   A 1 276 ? -2.512  12.046  -14.163 1.00 49.82  ? 813  LYS   A C   1 
ATOM   2008 O O   . LYS   A 1 276 ? -1.921  11.935  -13.089 1.00 44.60  ? 813  LYS   A O   1 
ATOM   2009 C CB  . LYS   A 1 276 ? -2.800  10.500  -16.117 1.00 49.83  ? 813  LYS   A CB  1 
ATOM   2010 C CG  . LYS   A 1 276 ? -2.381  10.155  -17.541 1.00 56.33  ? 813  LYS   A CG  1 
ATOM   2011 C CD  . LYS   A 1 276 ? -3.356  9.195   -18.205 1.00 70.36  ? 813  LYS   A CD  1 
ATOM   2012 C CE  . LYS   A 1 276 ? -2.971  8.935   -19.655 1.00 72.79  ? 813  LYS   A CE  1 
ATOM   2013 N NZ  . LYS   A 1 276 ? -3.887  7.953   -20.306 1.00 76.90  ? 813  LYS   A NZ  1 
ATOM   2014 N N   . GLU   A 1 277 ? -3.720  12.596  -14.294 1.00 50.25  ? 814  GLU   A N   1 
ATOM   2015 C CA  . GLU   A 1 277 ? -4.387  13.366  -13.245 1.00 53.10  ? 814  GLU   A CA  1 
ATOM   2016 C C   . GLU   A 1 277 ? -4.430  12.679  -11.880 1.00 50.61  ? 814  GLU   A C   1 
ATOM   2017 O O   . GLU   A 1 277 ? -4.121  13.298  -10.856 1.00 55.78  ? 814  GLU   A O   1 
ATOM   2018 C CB  . GLU   A 1 277 ? -5.813  13.704  -13.697 1.00 66.51  ? 814  GLU   A CB  1 
ATOM   2019 C CG  . GLU   A 1 277 ? -6.529  14.723  -12.828 1.00 80.54  ? 814  GLU   A CG  1 
ATOM   2020 C CD  . GLU   A 1 277 ? -7.822  15.214  -13.459 1.00 95.07  ? 814  GLU   A CD  1 
ATOM   2021 O OE1 . GLU   A 1 277 ? -8.880  14.588  -13.224 1.00 93.52  ? 814  GLU   A OE1 1 
ATOM   2022 O OE2 . GLU   A 1 277 ? -7.777  16.223  -14.198 1.00 103.61 ? 814  GLU   A OE2 1 
ATOM   2023 N N   . ASP   A 1 278 ? -4.805  11.405  -11.865 1.00 41.89  ? 815  ASP   A N   1 
ATOM   2024 C CA  . ASP   A 1 278 ? -4.933  10.675  -10.604 1.00 41.81  ? 815  ASP   A CA  1 
ATOM   2025 C C   . ASP   A 1 278 ? -3.688  9.855   -10.246 1.00 38.80  ? 815  ASP   A C   1 
ATOM   2026 O O   . ASP   A 1 278 ? -3.791  8.843   -9.550  1.00 35.83  ? 815  ASP   A O   1 
ATOM   2027 C CB  . ASP   A 1 278 ? -6.145  9.749   -10.656 1.00 42.17  ? 815  ASP   A CB  1 
ATOM   2028 C CG  . ASP   A 1 278 ? -7.456  10.504  -10.645 1.00 51.44  ? 815  ASP   A CG  1 
ATOM   2029 O OD1 . ASP   A 1 278 ? -7.464  11.684  -10.227 1.00 53.01  ? 815  ASP   A OD1 1 
ATOM   2030 O OD2 . ASP   A 1 278 ? -8.478  9.910   -11.046 1.00 56.85  ? 815  ASP   A OD2 1 
ATOM   2031 N N   . LYS   A 1 279 ? -2.522  10.306  -10.699 1.00 34.47  ? 816  LYS   A N   1 
ATOM   2032 C CA  . LYS   A 1 279 ? -1.284  9.552   -10.503 1.00 32.06  ? 816  LYS   A CA  1 
ATOM   2033 C C   . LYS   A 1 279 ? -1.010  9.198   -9.031  1.00 32.20  ? 816  LYS   A C   1 
ATOM   2034 O O   . LYS   A 1 279 ? -0.464  8.136   -8.747  1.00 30.94  ? 816  LYS   A O   1 
ATOM   2035 C CB  . LYS   A 1 279 ? -0.094  10.330  -11.083 1.00 32.13  ? 816  LYS   A CB  1 
ATOM   2036 C CG  . LYS   A 1 279 ? 0.147   11.682  -10.442 1.00 37.61  ? 816  LYS   A CG  1 
ATOM   2037 C CD  . LYS   A 1 279 ? 1.444   12.323  -10.926 1.00 38.92  ? 816  LYS   A CD  1 
ATOM   2038 C CE  . LYS   A 1 279 ? 1.252   13.085  -12.222 1.00 47.11  ? 816  LYS   A CE  1 
ATOM   2039 N NZ  . LYS   A 1 279 ? 0.403   14.305  -12.032 1.00 49.89  ? 816  LYS   A NZ  1 
ATOM   2040 N N   . GLU   A 1 280 ? -1.390  10.061  -8.088  1.00 35.37  ? 817  GLU   A N   1 
ATOM   2041 C CA  . GLU   A 1 280 ? -1.001  9.818   -6.701  1.00 33.28  ? 817  GLU   A CA  1 
ATOM   2042 C C   . GLU   A 1 280 ? -1.754  8.627   -6.127  1.00 36.39  ? 817  GLU   A C   1 
ATOM   2043 O O   . GLU   A 1 280 ? -1.248  7.921   -5.248  1.00 40.55  ? 817  GLU   A O   1 
ATOM   2044 C CB  . GLU   A 1 280 ? -1.224  11.059  -5.833  1.00 36.94  ? 817  GLU   A CB  1 
ATOM   2045 C CG  . GLU   A 1 280 ? -0.539  12.329  -6.341  1.00 38.53  ? 817  GLU   A CG  1 
ATOM   2046 C CD  . GLU   A 1 280 ? 0.988   12.279  -6.263  1.00 45.29  ? 817  GLU   A CD  1 
ATOM   2047 O OE1 . GLU   A 1 280 ? 1.541   11.468  -5.482  1.00 41.07  ? 817  GLU   A OE1 1 
ATOM   2048 O OE2 . GLU   A 1 280 ? 1.632   13.069  -6.985  1.00 41.95  ? 817  GLU   A OE2 1 
ATOM   2049 N N   . ILE   A 1 281 ? -2.961  8.398   -6.638  1.00 34.15  ? 818  ILE   A N   1 
ATOM   2050 C CA  . ILE   A 1 281 ? -3.784  7.272   -6.208  1.00 36.19  ? 818  ILE   A CA  1 
ATOM   2051 C C   . ILE   A 1 281 ? -3.415  5.988   -6.958  1.00 33.34  ? 818  ILE   A C   1 
ATOM   2052 O O   . ILE   A 1 281 ? -3.318  4.909   -6.363  1.00 34.17  ? 818  ILE   A O   1 
ATOM   2053 C CB  . ILE   A 1 281 ? -5.293  7.584   -6.414  1.00 38.51  ? 818  ILE   A CB  1 
ATOM   2054 C CG1 . ILE   A 1 281 ? -5.769  8.600   -5.378  1.00 50.48  ? 818  ILE   A CG1 1 
ATOM   2055 C CG2 . ILE   A 1 281 ? -6.139  6.320   -6.315  1.00 42.83  ? 818  ILE   A CG2 1 
ATOM   2056 C CD1 . ILE   A 1 281 ? -5.691  8.087   -3.960  1.00 57.95  ? 818  ILE   A CD1 1 
ATOM   2057 N N   . ASN   A 1 282 ? -3.198  6.115   -8.263  1.00 34.44  ? 819  ASN   A N   1 
ATOM   2058 C CA  . ASN   A 1 282 ? -3.001  4.954   -9.121  1.00 30.12  ? 819  ASN   A CA  1 
ATOM   2059 C C   . ASN   A 1 282 ? -1.568  4.426   -9.156  1.00 28.29  ? 819  ASN   A C   1 
ATOM   2060 O O   . ASN   A 1 282 ? -1.351  3.248   -9.442  1.00 27.56  ? 819  ASN   A O   1 
ATOM   2061 C CB  . ASN   A 1 282 ? -3.454  5.284   -10.544 1.00 28.41  ? 819  ASN   A CB  1 
ATOM   2062 C CG  . ASN   A 1 282 ? -4.958  5.484   -10.635 1.00 35.90  ? 819  ASN   A CG  1 
ATOM   2063 O OD1 . ASN   A 1 282 ? -5.717  4.849   -9.903  1.00 38.11  ? 819  ASN   A OD1 1 
ATOM   2064 N ND2 . ASN   A 1 282 ? -5.392  6.376   -11.521 1.00 32.65  ? 819  ASN   A ND2 1 
ATOM   2065 N N   . SER   A 1 283 ? -0.594  5.293   -8.878  1.00 23.79  ? 820  SER   A N   1 
ATOM   2066 C CA  . SER   A 1 283 ? 0.813   4.889   -8.983  1.00 25.58  ? 820  SER   A CA  1 
ATOM   2067 C C   . SER   A 1 283 ? 1.677   5.285   -7.789  1.00 23.23  ? 820  SER   A C   1 
ATOM   2068 O O   . SER   A 1 283 ? 2.791   5.789   -7.981  1.00 26.72  ? 820  SER   A O   1 
ATOM   2069 C CB  . SER   A 1 283 ? 1.431   5.493   -10.248 1.00 28.74  ? 820  SER   A CB  1 
ATOM   2070 O OG  . SER   A 1 283 ? 0.648   5.200   -11.393 1.00 31.56  ? 820  SER   A OG  1 
ATOM   2071 N N   . PRO   A 1 284 ? 1.198   5.045   -6.555  1.00 28.75  ? 821  PRO   A N   1 
ATOM   2072 C CA  . PRO   A 1 284 ? 1.941   5.590   -5.408  1.00 30.02  ? 821  PRO   A CA  1 
ATOM   2073 C C   . PRO   A 1 284 ? 3.344   5.014   -5.241  1.00 27.63  ? 821  PRO   A C   1 
ATOM   2074 O O   . PRO   A 1 284 ? 4.264   5.751   -4.867  1.00 26.29  ? 821  PRO   A O   1 
ATOM   2075 C CB  . PRO   A 1 284 ? 1.062   5.208   -4.216  1.00 32.47  ? 821  PRO   A CB  1 
ATOM   2076 C CG  . PRO   A 1 284 ? 0.358   3.971   -4.664  1.00 31.18  ? 821  PRO   A CG  1 
ATOM   2077 C CD  . PRO   A 1 284 ? 0.068   4.201   -6.120  1.00 29.82  ? 821  PRO   A CD  1 
ATOM   2078 N N   . ASN   A 1 285 ? 3.519   3.727   -5.516  1.00 26.03  ? 822  ASN   A N   1 
ATOM   2079 C CA  . ASN   A 1 285 ? 4.820   3.104   -5.300  1.00 25.85  ? 822  ASN   A CA  1 
ATOM   2080 C C   . ASN   A 1 285 ? 5.783   3.472   -6.412  1.00 24.59  ? 822  ASN   A C   1 
ATOM   2081 O O   . ASN   A 1 285 ? 6.948   3.765   -6.159  1.00 24.03  ? 822  ASN   A O   1 
ATOM   2082 C CB  . ASN   A 1 285 ? 4.676   1.587   -5.186  1.00 25.56  ? 822  ASN   A CB  1 
ATOM   2083 C CG  . ASN   A 1 285 ? 3.705   1.194   -4.095  1.00 32.46  ? 822  ASN   A CG  1 
ATOM   2084 O OD1 . ASN   A 1 285 ? 4.002   1.347   -2.908  1.00 31.46  ? 822  ASN   A OD1 1 
ATOM   2085 N ND2 . ASN   A 1 285 ? 2.528   0.711   -4.489  1.00 28.99  ? 822  ASN   A ND2 1 
ATOM   2086 N N   . LEU   A 1 286 ? 5.283   3.485   -7.642  1.00 23.73  ? 823  LEU   A N   1 
ATOM   2087 C CA  . LEU   A 1 286 ? 6.087   3.934   -8.771  1.00 22.94  ? 823  LEU   A CA  1 
ATOM   2088 C C   . LEU   A 1 286 ? 6.553   5.382   -8.570  1.00 24.62  ? 823  LEU   A C   1 
ATOM   2089 O O   . LEU   A 1 286 ? 7.732   5.700   -8.759  1.00 23.72  ? 823  LEU   A O   1 
ATOM   2090 C CB  . LEU   A 1 286 ? 5.295   3.792   -10.073 1.00 25.90  ? 823  LEU   A CB  1 
ATOM   2091 C CG  . LEU   A 1 286 ? 6.005   4.287   -11.343 1.00 26.45  ? 823  LEU   A CG  1 
ATOM   2092 C CD1 . LEU   A 1 286 ? 7.376   3.678   -11.458 1.00 34.25  ? 823  LEU   A CD1 1 
ATOM   2093 C CD2 . LEU   A 1 286 ? 5.180   3.959   -12.576 1.00 28.45  ? 823  LEU   A CD2 1 
ATOM   2094 N N   . LEU   A 1 287 ? 5.646   6.267   -8.168  1.00 24.76  ? 824  LEU   A N   1 
ATOM   2095 C CA  . LEU   A 1 287 ? 6.046   7.653   -7.926  1.00 27.09  ? 824  LEU   A CA  1 
ATOM   2096 C C   . LEU   A 1 287 ? 7.094   7.778   -6.813  1.00 29.08  ? 824  LEU   A C   1 
ATOM   2097 O O   . LEU   A 1 287 ? 8.020   8.581   -6.930  1.00 25.99  ? 824  LEU   A O   1 
ATOM   2098 C CB  . LEU   A 1 287 ? 4.821   8.501   -7.598  1.00 26.59  ? 824  LEU   A CB  1 
ATOM   2099 C CG  . LEU   A 1 287 ? 3.946   8.807   -8.811  1.00 31.12  ? 824  LEU   A CG  1 
ATOM   2100 C CD1 . LEU   A 1 287 ? 2.682   9.537   -8.369  1.00 29.32  ? 824  LEU   A CD1 1 
ATOM   2101 C CD2 . LEU   A 1 287 ? 4.714   9.632   -9.836  1.00 28.58  ? 824  LEU   A CD2 1 
ATOM   2102 N N   . LYS   A 1 288 ? 6.963   6.986   -5.751  1.00 24.28  ? 825  LYS   A N   1 
ATOM   2103 C CA  . LYS   A 1 288 ? 7.952   7.016   -4.675  1.00 26.72  ? 825  LYS   A CA  1 
ATOM   2104 C C   . LYS   A 1 288 ? 9.323   6.651   -5.203  1.00 24.02  ? 825  LYS   A C   1 
ATOM   2105 O O   . LYS   A 1 288 ? 10.337  7.245   -4.815  1.00 23.29  ? 825  LYS   A O   1 
ATOM   2106 C CB  . LYS   A 1 288 ? 7.582   6.056   -3.542  1.00 27.69  ? 825  LYS   A CB  1 
ATOM   2107 C CG  . LYS   A 1 288 ? 6.565   6.605   -2.544  1.00 44.22  ? 825  LYS   A CG  1 
ATOM   2108 C CD  . LYS   A 1 288 ? 6.658   5.858   -1.207  1.00 48.24  ? 825  LYS   A CD  1 
ATOM   2109 C CE  . LYS   A 1 288 ? 8.009   6.125   -0.531  1.00 54.80  ? 825  LYS   A CE  1 
ATOM   2110 N NZ  . LYS   A 1 288 ? 8.192   5.421   0.777   1.00 57.41  ? 825  LYS   A NZ  1 
ATOM   2111 N N   A MET   A 1 289 ? 9.353   5.660   -6.088  0.54 24.24  ? 826  MET   A N   1 
ATOM   2112 N N   B MET   A 1 289 ? 9.350   5.667   -6.092  0.46 24.28  ? 826  MET   A N   1 
ATOM   2113 C CA  A MET   A 1 289 ? 10.602  5.187   -6.683  0.54 24.89  ? 826  MET   A CA  1 
ATOM   2114 C CA  B MET   A 1 289 ? 10.600  5.182   -6.669  0.46 24.77  ? 826  MET   A CA  1 
ATOM   2115 C C   A MET   A 1 289 ? 11.232  6.255   -7.565  0.54 25.04  ? 826  MET   A C   1 
ATOM   2116 C C   B MET   A 1 289 ? 11.236  6.223   -7.589  0.46 24.86  ? 826  MET   A C   1 
ATOM   2117 O O   A MET   A 1 289 ? 12.415  6.567   -7.438  0.54 22.39  ? 826  MET   A O   1 
ATOM   2118 O O   B MET   A 1 289 ? 12.431  6.493   -7.499  0.46 22.73  ? 826  MET   A O   1 
ATOM   2119 C CB  A MET   A 1 289 ? 10.360  3.926   -7.509  0.54 26.54  ? 826  MET   A CB  1 
ATOM   2120 C CB  B MET   A 1 289 ? 10.349  3.879   -7.427  0.46 26.55  ? 826  MET   A CB  1 
ATOM   2121 C CG  A MET   A 1 289 ? 11.605  3.399   -8.193  0.54 28.00  ? 826  MET   A CG  1 
ATOM   2122 C CG  B MET   A 1 289 ? 11.306  3.621   -8.566  0.46 35.93  ? 826  MET   A CG  1 
ATOM   2123 S SD  A MET   A 1 289 ? 12.633  2.481   -7.052  0.54 32.94  ? 826  MET   A SD  1 
ATOM   2124 S SD  B MET   A 1 289 ? 11.529  1.855   -8.808  0.46 33.78  ? 826  MET   A SD  1 
ATOM   2125 C CE  A MET   A 1 289 ? 13.823  1.732   -8.165  0.54 39.46  ? 826  MET   A CE  1 
ATOM   2126 C CE  B MET   A 1 289 ? 12.727  1.567   -7.505  0.46 40.53  ? 826  MET   A CE  1 
ATOM   2127 N N   . ILE   A 1 290 ? 10.431  6.808   -8.472  1.00 24.07  ? 827  ILE   A N   1 
ATOM   2128 C CA  . ILE   A 1 290 ? 10.898  7.866   -9.355  1.00 24.20  ? 827  ILE   A CA  1 
ATOM   2129 C C   . ILE   A 1 290 ? 11.404  9.075   -8.573  1.00 24.26  ? 827  ILE   A C   1 
ATOM   2130 O O   . ILE   A 1 290 ? 12.439  9.661   -8.901  1.00 26.29  ? 827  ILE   A O   1 
ATOM   2131 C CB  . ILE   A 1 290 ? 9.766   8.316   -10.318 1.00 27.81  ? 827  ILE   A CB  1 
ATOM   2132 C CG1 . ILE   A 1 290 ? 9.418   7.175   -11.279 1.00 29.66  ? 827  ILE   A CG1 1 
ATOM   2133 C CG2 . ILE   A 1 290 ? 10.182  9.565   -11.088 1.00 31.04  ? 827  ILE   A CG2 1 
ATOM   2134 C CD1 . ILE   A 1 290 ? 8.167   7.448   -12.136 1.00 30.32  ? 827  ILE   A CD1 1 
ATOM   2135 N N   . ARG   A 1 291 ? 10.660  9.456   -7.542  1.00 23.26  ? 828  ARG   A N   1 
ATOM   2136 C CA  . ARG   A 1 291 ? 10.994  10.647  -6.775  1.00 26.72  ? 828  ARG   A CA  1 
ATOM   2137 C C   . ARG   A 1 291 ? 12.257  10.428  -5.950  1.00 27.80  ? 828  ARG   A C   1 
ATOM   2138 O O   . ARG   A 1 291 ? 13.073  11.354  -5.783  1.00 26.30  ? 828  ARG   A O   1 
ATOM   2139 C CB  . ARG   A 1 291 ? 9.810   11.050  -5.893  1.00 23.55  ? 828  ARG   A CB  1 
ATOM   2140 C CG  . ARG   A 1 291 ? 8.677   11.630  -6.753  1.00 27.74  ? 828  ARG   A CG  1 
ATOM   2141 C CD  . ARG   A 1 291 ? 7.396   11.895  -5.964  1.00 38.40  ? 828  ARG   A CD  1 
ATOM   2142 N NE  . ARG   A 1 291 ? 6.395   12.515  -6.835  1.00 39.62  ? 828  ARG   A NE  1 
ATOM   2143 C CZ  . ARG   A 1 291 ? 5.081   12.474  -6.633  1.00 40.24  ? 828  ARG   A CZ  1 
ATOM   2144 N NH1 . ARG   A 1 291 ? 4.578   11.826  -5.589  1.00 35.92  ? 828  ARG   A NH1 1 
ATOM   2145 N NH2 . ARG   A 1 291 ? 4.269   13.075  -7.493  1.00 38.69  ? 828  ARG   A NH2 1 
ATOM   2146 N N   . HIS   A 1 292 ? 12.429  9.203   -5.461  1.00 23.91  ? 829  HIS   A N   1 
ATOM   2147 C CA  . HIS   A 1 292 ? 13.679  8.844   -4.782  1.00 23.62  ? 829  HIS   A CA  1 
ATOM   2148 C C   . HIS   A 1 292 ? 14.874  9.037   -5.715  1.00 24.60  ? 829  HIS   A C   1 
ATOM   2149 O O   . HIS   A 1 292 ? 15.895  9.635   -5.339  1.00 22.92  ? 829  HIS   A O   1 
ATOM   2150 C CB  . HIS   A 1 292 ? 13.669  7.396   -4.291  1.00 22.87  ? 829  HIS   A CB  1 
ATOM   2151 C CG  . HIS   A 1 292 ? 15.037  6.901   -3.923  1.00 24.85  ? 829  HIS   A CG  1 
ATOM   2152 N ND1 . HIS   A 1 292 ? 15.617  7.172   -2.705  1.00 26.67  ? 829  HIS   A ND1 1 
ATOM   2153 C CD2 . HIS   A 1 292 ? 15.959  6.214   -4.640  1.00 26.81  ? 829  HIS   A CD2 1 
ATOM   2154 C CE1 . HIS   A 1 292 ? 16.840  6.655   -2.677  1.00 26.36  ? 829  HIS   A CE1 1 
ATOM   2155 N NE2 . HIS   A 1 292 ? 17.066  6.069   -3.835  1.00 21.84  ? 829  HIS   A NE2 1 
ATOM   2156 N N   . THR   A 1 293 ? 14.740  8.535   -6.936  1.00 20.81  ? 830  THR   A N   1 
ATOM   2157 C CA  . THR   A 1 293 ? 15.831  8.609   -7.908  1.00 26.62  ? 830  THR   A CA  1 
ATOM   2158 C C   . THR   A 1 293 ? 16.157  10.057  -8.244  1.00 23.88  ? 830  THR   A C   1 
ATOM   2159 O O   . THR   A 1 293 ? 17.324  10.444  -8.260  1.00 24.05  ? 830  THR   A O   1 
ATOM   2160 C CB  . THR   A 1 293 ? 15.491  7.833   -9.202  1.00 28.72  ? 830  THR   A CB  1 
ATOM   2161 O OG1 . THR   A 1 293 ? 15.465  6.434   -8.901  1.00 29.66  ? 830  THR   A OG1 1 
ATOM   2162 C CG2 . THR   A 1 293 ? 16.550  8.095   -10.293 1.00 29.35  ? 830  THR   A CG2 1 
ATOM   2163 N N   . THR   A 1 294 ? 15.124  10.867  -8.479  1.00 22.74  ? 831  THR   A N   1 
ATOM   2164 C CA  . THR   A 1 294 ? 15.317  12.300  -8.729  1.00 22.25  ? 831  THR   A CA  1 
ATOM   2165 C C   . THR   A 1 294 ? 16.031  12.976  -7.564  1.00 26.16  ? 831  THR   A C   1 
ATOM   2166 O O   . THR   A 1 294 ? 17.006  13.689  -7.759  1.00 24.17  ? 831  THR   A O   1 
ATOM   2167 C CB  . THR   A 1 294 ? 13.981  13.014  -8.968  1.00 28.04  ? 831  THR   A CB  1 
ATOM   2168 O OG1 . THR   A 1 294 ? 13.352  12.424  -10.104 1.00 30.08  ? 831  THR   A OG1 1 
ATOM   2169 C CG2 . THR   A 1 294 ? 14.199  14.493  -9.228  1.00 33.82  ? 831  THR   A CG2 1 
ATOM   2170 N N   . ASN   A 1 295 ? 15.548  12.742  -6.349  1.00 21.52  ? 832  ASN   A N   1 
ATOM   2171 C CA  . ASN   A 1 295 ? 16.134  13.400  -5.189  1.00 25.79  ? 832  ASN   A CA  1 
ATOM   2172 C C   . ASN   A 1 295 ? 17.567  12.938  -4.924  1.00 24.02  ? 832  ASN   A C   1 
ATOM   2173 O O   . ASN   A 1 295 ? 18.427  13.741  -4.598  1.00 24.09  ? 832  ASN   A O   1 
ATOM   2174 C CB  . ASN   A 1 295 ? 15.269  13.180  -3.946  1.00 24.87  ? 832  ASN   A CB  1 
ATOM   2175 C CG  . ASN   A 1 295 ? 14.124  14.171  -3.858  1.00 42.74  ? 832  ASN   A CG  1 
ATOM   2176 O OD1 . ASN   A 1 295 ? 14.274  15.342  -4.213  1.00 38.97  ? 832  ASN   A OD1 1 
ATOM   2177 N ND2 . ASN   A 1 295 ? 12.964  13.703  -3.401  1.00 38.77  ? 832  ASN   A ND2 1 
ATOM   2178 N N   . LEU   A 1 296 ? 17.833  11.649  -5.070  1.00 21.39  ? 833  LEU   A N   1 
ATOM   2179 C CA  . LEU   A 1 296 ? 19.181  11.163  -4.800  1.00 19.03  ? 833  LEU   A CA  1 
ATOM   2180 C C   . LEU   A 1 296 ? 20.169  11.699  -5.844  1.00 21.88  ? 833  LEU   A C   1 
ATOM   2181 O O   . LEU   A 1 296 ? 21.280  12.120  -5.503  1.00 20.28  ? 833  LEU   A O   1 
ATOM   2182 C CB  . LEU   A 1 296 ? 19.211  9.636   -4.760  1.00 20.49  ? 833  LEU   A CB  1 
ATOM   2183 C CG  . LEU   A 1 296 ? 20.579  9.091   -4.330  1.00 24.47  ? 833  LEU   A CG  1 
ATOM   2184 C CD1 . LEU   A 1 296 ? 20.867  9.423   -2.858  1.00 25.73  ? 833  LEU   A CD1 1 
ATOM   2185 C CD2 . LEU   A 1 296 ? 20.626  7.603   -4.556  1.00 30.75  ? 833  LEU   A CD2 1 
ATOM   2186 N N   . THR   A 1 297 ? 19.763  11.718  -7.113  1.00 19.72  ? 834  THR   A N   1 
ATOM   2187 C CA  . THR   A 1 297 ? 20.623  12.275  -8.164  1.00 18.61  ? 834  THR   A CA  1 
ATOM   2188 C C   . THR   A 1 297 ? 20.927  13.746  -7.869  1.00 18.70  ? 834  THR   A C   1 
ATOM   2189 O O   . THR   A 1 297 ? 22.086  14.183  -7.939  1.00 19.14  ? 834  THR   A O   1 
ATOM   2190 C CB  . THR   A 1 297 ? 19.965  12.142  -9.553  1.00 24.48  ? 834  THR   A CB  1 
ATOM   2191 O OG1 . THR   A 1 297 ? 19.661  10.760  -9.798  1.00 25.43  ? 834  THR   A OG1 1 
ATOM   2192 C CG2 . THR   A 1 297 ? 20.898  12.644  -10.650 1.00 21.24  ? 834  THR   A CG2 1 
ATOM   2193 N N   . LEU   A 1 298 ? 19.895  14.520  -7.539  1.00 19.99  ? 835  LEU   A N   1 
ATOM   2194 C CA  . LEU   A 1 298 ? 20.112  15.939  -7.231  1.00 18.81  ? 835  LEU   A CA  1 
ATOM   2195 C C   . LEU   A 1 298 ? 20.977  16.082  -5.989  1.00 19.34  ? 835  LEU   A C   1 
ATOM   2196 O O   . LEU   A 1 298 ? 21.737  17.030  -5.892  1.00 20.42  ? 835  LEU   A O   1 
ATOM   2197 C CB  . LEU   A 1 298 ? 18.784  16.681  -7.022  1.00 19.41  ? 835  LEU   A CB  1 
ATOM   2198 C CG  . LEU   A 1 298 ? 17.936  16.817  -8.288  1.00 23.96  ? 835  LEU   A CG  1 
ATOM   2199 C CD1 . LEU   A 1 298 ? 16.607  17.503  -7.966  1.00 23.17  ? 835  LEU   A CD1 1 
ATOM   2200 C CD2 . LEU   A 1 298 ? 18.708  17.580  -9.361  1.00 27.40  ? 835  LEU   A CD2 1 
ATOM   2201 N N   . TRP   A 1 299 ? 20.847  15.170  -5.025  1.00 20.73  ? 836  TRP   A N   1 
ATOM   2202 C CA  . TRP   A 1 299 ? 21.696  15.263  -3.826  1.00 21.76  ? 836  TRP   A CA  1 
ATOM   2203 C C   . TRP   A 1 299 ? 23.173  15.041  -4.164  1.00 18.58  ? 836  TRP   A C   1 
ATOM   2204 O O   . TRP   A 1 299 ? 24.036  15.758  -3.664  1.00 20.29  ? 836  TRP   A O   1 
ATOM   2205 C CB  . TRP   A 1 299 ? 21.243  14.255  -2.770  1.00 21.79  ? 836  TRP   A CB  1 
ATOM   2206 C CG  . TRP   A 1 299 ? 22.029  14.280  -1.491  1.00 20.50  ? 836  TRP   A CG  1 
ATOM   2207 C CD1 . TRP   A 1 299 ? 22.051  15.269  -0.557  1.00 25.71  ? 836  TRP   A CD1 1 
ATOM   2208 C CD2 . TRP   A 1 299 ? 22.878  13.241  -1.004  1.00 21.25  ? 836  TRP   A CD2 1 
ATOM   2209 N NE1 . TRP   A 1 299 ? 22.872  14.912  0.489   1.00 26.88  ? 836  TRP   A NE1 1 
ATOM   2210 C CE2 . TRP   A 1 299 ? 23.387  13.664  0.241   1.00 23.04  ? 836  TRP   A CE2 1 
ATOM   2211 C CE3 . TRP   A 1 299 ? 23.245  11.988  -1.493  1.00 23.42  ? 836  TRP   A CE3 1 
ATOM   2212 C CZ2 . TRP   A 1 299 ? 24.253  12.879  1.000   1.00 22.64  ? 836  TRP   A CZ2 1 
ATOM   2213 C CZ3 . TRP   A 1 299 ? 24.103  11.196  -0.734  1.00 26.95  ? 836  TRP   A CZ3 1 
ATOM   2214 C CH2 . TRP   A 1 299 ? 24.594  11.650  0.499   1.00 26.16  ? 836  TRP   A CH2 1 
ATOM   2215 N N   . PHE   A 1 300 ? 23.472  14.050  -5.001  1.00 17.86  ? 837  PHE   A N   1 
ATOM   2216 C CA  . PHE   A 1 300 ? 24.869  13.851  -5.413  1.00 18.25  ? 837  PHE   A CA  1 
ATOM   2217 C C   . PHE   A 1 300 ? 25.397  15.109  -6.108  1.00 24.06  ? 837  PHE   A C   1 
ATOM   2218 O O   . PHE   A 1 300 ? 26.536  15.548  -5.854  1.00 20.40  ? 837  PHE   A O   1 
ATOM   2219 C CB  . PHE   A 1 300 ? 25.007  12.639  -6.341  1.00 18.60  ? 837  PHE   A CB  1 
ATOM   2220 C CG  . PHE   A 1 300 ? 24.904  11.314  -5.640  1.00 20.32  ? 837  PHE   A CG  1 
ATOM   2221 C CD1 . PHE   A 1 300 ? 25.675  11.037  -4.524  1.00 21.73  ? 837  PHE   A CD1 1 
ATOM   2222 C CD2 . PHE   A 1 300 ? 24.041  10.335  -6.111  1.00 21.73  ? 837  PHE   A CD2 1 
ATOM   2223 C CE1 . PHE   A 1 300 ? 25.596  9.792   -3.890  1.00 24.59  ? 837  PHE   A CE1 1 
ATOM   2224 C CE2 . PHE   A 1 300 ? 23.959  9.082   -5.476  1.00 24.56  ? 837  PHE   A CE2 1 
ATOM   2225 C CZ  . PHE   A 1 300 ? 24.747  8.822   -4.375  1.00 19.63  ? 837  PHE   A CZ  1 
ATOM   2226 N N   . GLU   A 1 301 ? 24.582  15.709  -6.976  1.00 20.32  ? 838  GLU   A N   1 
ATOM   2227 C CA  . GLU   A 1 301 ? 25.003  16.923  -7.680  1.00 19.99  ? 838  GLU   A CA  1 
ATOM   2228 C C   . GLU   A 1 301 ? 25.257  18.065  -6.706  1.00 18.84  ? 838  GLU   A C   1 
ATOM   2229 O O   . GLU   A 1 301 ? 26.251  18.773  -6.811  1.00 19.31  ? 838  GLU   A O   1 
ATOM   2230 C CB  . GLU   A 1 301 ? 23.945  17.352  -8.705  1.00 17.70  ? 838  GLU   A CB  1 
ATOM   2231 C CG  . GLU   A 1 301 ? 23.709  16.298  -9.790  1.00 19.28  ? 838  GLU   A CG  1 
ATOM   2232 C CD  . GLU   A 1 301 ? 22.573  16.640  -10.734 1.00 26.90  ? 838  GLU   A CD  1 
ATOM   2233 O OE1 . GLU   A 1 301 ? 22.220  17.834  -10.871 1.00 21.74  ? 838  GLU   A OE1 1 
ATOM   2234 O OE2 . GLU   A 1 301 ? 22.042  15.706  -11.367 1.00 22.88  ? 838  GLU   A OE2 1 
ATOM   2235 N N   . LYS   A 1 302 ? 24.334  18.238  -5.771  1.00 18.80  ? 839  LYS   A N   1 
ATOM   2236 C CA  . LYS   A 1 302 ? 24.456  19.272  -4.754  1.00 18.78  ? 839  LYS   A CA  1 
ATOM   2237 C C   . LYS   A 1 302 ? 25.750  19.111  -3.937  1.00 21.29  ? 839  LYS   A C   1 
ATOM   2238 O O   . LYS   A 1 302 ? 26.466  20.090  -3.675  1.00 22.07  ? 839  LYS   A O   1 
ATOM   2239 C CB  . LYS   A 1 302 ? 23.227  19.225  -3.837  1.00 18.83  ? 839  LYS   A CB  1 
ATOM   2240 C CG  . LYS   A 1 302 ? 23.211  20.305  -2.752  1.00 22.84  ? 839  LYS   A CG  1 
ATOM   2241 C CD  . LYS   A 1 302 ? 22.036  20.098  -1.786  1.00 24.20  ? 839  LYS   A CD  1 
ATOM   2242 C CE  . LYS   A 1 302 ? 22.128  21.079  -0.616  1.00 30.03  ? 839  LYS   A CE  1 
ATOM   2243 N NZ  . LYS   A 1 302 ? 20.821  21.210  0.054   1.00 38.96  ? 839  LYS   A NZ  1 
ATOM   2244 N N   . CYS   A 1 303 ? 26.047  17.880  -3.525  1.00 20.52  ? 840  CYS   A N   1 
ATOM   2245 C CA  . CYS   A 1 303 ? 27.265  17.620  -2.753  1.00 19.12  ? 840  CYS   A CA  1 
ATOM   2246 C C   . CYS   A 1 303 ? 28.511  18.036  -3.518  1.00 22.80  ? 840  CYS   A C   1 
ATOM   2247 O O   . CYS   A 1 303 ? 29.458  18.576  -2.939  1.00 21.78  ? 840  CYS   A O   1 
ATOM   2248 C CB  . CYS   A 1 303 ? 27.377  16.136  -2.383  1.00 21.61  ? 840  CYS   A CB  1 
ATOM   2249 S SG  . CYS   A 1 303 ? 26.178  15.591  -1.151  1.00 25.32  ? 840  CYS   A SG  1 
ATOM   2250 N N   . ILE   A 1 304 ? 28.521  17.753  -4.812  1.00 20.28  ? 841  ILE   A N   1 
ATOM   2251 C CA  . ILE   A 1 304 ? 29.679  18.086  -5.636  1.00 20.13  ? 841  ILE   A CA  1 
ATOM   2252 C C   . ILE   A 1 304 ? 29.811  19.599  -5.830  1.00 22.62  ? 841  ILE   A C   1 
ATOM   2253 O O   . ILE   A 1 304 ? 30.871  20.174  -5.556  1.00 22.82  ? 841  ILE   A O   1 
ATOM   2254 C CB  . ILE   A 1 304 ? 29.610  17.382  -7.017  1.00 18.73  ? 841  ILE   A CB  1 
ATOM   2255 C CG1 . ILE   A 1 304 ? 29.773  15.864  -6.849  1.00 20.07  ? 841  ILE   A CG1 1 
ATOM   2256 C CG2 . ILE   A 1 304 ? 30.703  17.918  -7.977  1.00 20.43  ? 841  ILE   A CG2 1 
ATOM   2257 C CD1 . ILE   A 1 304 ? 29.326  15.047  -8.065  1.00 22.44  ? 841  ILE   A CD1 1 
ATOM   2258 N N   A VAL   A 1 305 ? 28.734  20.233  -6.275  0.28 19.90  ? 842  VAL   A N   1 
ATOM   2259 N N   B VAL   A 1 305 ? 28.755  20.262  -6.296  0.72 19.63  ? 842  VAL   A N   1 
ATOM   2260 C CA  A VAL   A 1 305 ? 28.791  21.637  -6.661  0.28 21.90  ? 842  VAL   A CA  1 
ATOM   2261 C CA  B VAL   A 1 305 ? 28.909  21.679  -6.651  0.72 22.54  ? 842  VAL   A CA  1 
ATOM   2262 C C   A VAL   A 1 305 ? 28.928  22.571  -5.445  0.28 23.79  ? 842  VAL   A C   1 
ATOM   2263 C C   B VAL   A 1 305 ? 28.970  22.589  -5.418  0.72 22.77  ? 842  VAL   A C   1 
ATOM   2264 O O   A VAL   A 1 305 ? 29.513  23.651  -5.545  0.28 25.81  ? 842  VAL   A O   1 
ATOM   2265 O O   B VAL   A 1 305 ? 29.523  23.687  -5.484  0.72 25.38  ? 842  VAL   A O   1 
ATOM   2266 C CB  A VAL   A 1 305 ? 27.549  22.019  -7.493  0.28 22.53  ? 842  VAL   A CB  1 
ATOM   2267 C CB  B VAL   A 1 305 ? 27.782  22.175  -7.593  0.72 23.58  ? 842  VAL   A CB  1 
ATOM   2268 C CG1 A VAL   A 1 305 ? 27.708  23.386  -8.071  0.28 20.70  ? 842  VAL   A CG1 1 
ATOM   2269 C CG1 B VAL   A 1 305 ? 27.729  21.314  -8.862  0.72 21.31  ? 842  VAL   A CG1 1 
ATOM   2270 C CG2 A VAL   A 1 305 ? 27.369  21.030  -8.636  0.28 22.92  ? 842  VAL   A CG2 1 
ATOM   2271 C CG2 B VAL   A 1 305 ? 26.450  22.181  -6.895  0.72 23.88  ? 842  VAL   A CG2 1 
ATOM   2272 N N   . GLU   A 1 306 ? 28.410  22.148  -4.294  1.00 23.49  ? 843  GLU   A N   1 
ATOM   2273 C CA  . GLU   A 1 306 ? 28.504  22.961  -3.083  1.00 23.62  ? 843  GLU   A CA  1 
ATOM   2274 C C   . GLU   A 1 306 ? 29.847  22.818  -2.372  1.00 28.71  ? 843  GLU   A C   1 
ATOM   2275 O O   . GLU   A 1 306 ? 30.142  23.565  -1.434  1.00 31.45  ? 843  GLU   A O   1 
ATOM   2276 C CB  . GLU   A 1 306 ? 27.364  22.636  -2.119  1.00 22.77  ? 843  GLU   A CB  1 
ATOM   2277 C CG  . GLU   A 1 306 ? 26.062  23.232  -2.598  1.00 24.58  ? 843  GLU   A CG  1 
ATOM   2278 C CD  . GLU   A 1 306 ? 24.963  23.145  -1.564  1.00 33.46  ? 843  GLU   A CD  1 
ATOM   2279 O OE1 . GLU   A 1 306 ? 25.130  22.430  -0.549  1.00 30.78  ? 843  GLU   A OE1 1 
ATOM   2280 O OE2 . GLU   A 1 306 ? 23.928  23.798  -1.777  1.00 30.40  ? 843  GLU   A OE2 1 
ATOM   2281 N N   . ALA   A 1 307 ? 30.663  21.870  -2.813  1.00 26.95  ? 844  ALA   A N   1 
ATOM   2282 C CA  . ALA   A 1 307 ? 32.019  21.747  -2.284  1.00 24.70  ? 844  ALA   A CA  1 
ATOM   2283 C C   . ALA   A 1 307 ? 32.906  22.753  -3.013  1.00 27.90  ? 844  ALA   A C   1 
ATOM   2284 O O   . ALA   A 1 307 ? 33.482  22.444  -4.051  1.00 27.11  ? 844  ALA   A O   1 
ATOM   2285 C CB  . ALA   A 1 307 ? 32.546  20.319  -2.449  1.00 24.70  ? 844  ALA   A CB  1 
ATOM   2286 N N   . GLU   A 1 308 ? 32.996  23.969  -2.482  1.00 26.47  ? 845  GLU   A N   1 
ATOM   2287 C CA  . GLU   A 1 308 ? 33.667  25.048  -3.212  1.00 25.17  ? 845  GLU   A CA  1 
ATOM   2288 C C   . GLU   A 1 308 ? 35.194  24.905  -3.181  1.00 29.18  ? 845  GLU   A C   1 
ATOM   2289 O O   . GLU   A 1 308 ? 35.867  25.204  -4.166  1.00 26.87  ? 845  GLU   A O   1 
ATOM   2290 C CB  . GLU   A 1 308 ? 33.216  26.408  -2.665  1.00 26.83  ? 845  GLU   A CB  1 
ATOM   2291 C CG  . GLU   A 1 308 ? 31.696  26.617  -2.837  1.00 32.82  ? 845  GLU   A CG  1 
ATOM   2292 C CD  . GLU   A 1 308 ? 31.193  27.930  -2.273  1.00 49.81  ? 845  GLU   A CD  1 
ATOM   2293 O OE1 . GLU   A 1 308 ? 32.024  28.803  -1.936  1.00 50.56  ? 845  GLU   A OE1 1 
ATOM   2294 O OE2 . GLU   A 1 308 ? 29.957  28.089  -2.173  1.00 52.35  ? 845  GLU   A OE2 1 
ATOM   2295 N N   . ASN   A 1 309 ? 35.735  24.421  -2.068  1.00 25.04  ? 846  ASN   A N   1 
ATOM   2296 C CA  . ASN   A 1 309 ? 37.163  24.125  -1.967  1.00 27.83  ? 846  ASN   A CA  1 
ATOM   2297 C C   . ASN   A 1 309 ? 37.532  23.001  -2.925  1.00 28.26  ? 846  ASN   A C   1 
ATOM   2298 O O   . ASN   A 1 309 ? 36.897  21.947  -2.913  1.00 25.53  ? 846  ASN   A O   1 
ATOM   2299 C CB  . ASN   A 1 309 ? 37.530  23.750  -0.525  1.00 27.96  ? 846  ASN   A CB  1 
ATOM   2300 C CG  . ASN   A 1 309 ? 38.974  23.301  -0.381  1.00 29.66  ? 846  ASN   A CG  1 
ATOM   2301 O OD1 . ASN   A 1 309 ? 39.281  22.106  -0.411  1.00 30.09  ? 846  ASN   A OD1 1 
ATOM   2302 N ND2 . ASN   A 1 309 ? 39.874  24.266  -0.213  1.00 32.31  ? 846  ASN   A ND2 1 
ATOM   2303 N N   . PHE   A 1 310 ? 38.536  23.236  -3.770  1.00 30.49  ? 847  PHE   A N   1 
ATOM   2304 C CA  . PHE   A 1 310 ? 38.858  22.308  -4.847  1.00 26.53  ? 847  PHE   A CA  1 
ATOM   2305 C C   . PHE   A 1 310 ? 39.207  20.906  -4.339  1.00 27.99  ? 847  PHE   A C   1 
ATOM   2306 O O   . PHE   A 1 310 ? 38.682  19.921  -4.851  1.00 24.80  ? 847  PHE   A O   1 
ATOM   2307 C CB  . PHE   A 1 310 ? 40.014  22.840  -5.702  1.00 25.81  ? 847  PHE   A CB  1 
ATOM   2308 C CG  . PHE   A 1 310 ? 40.348  21.953  -6.873  1.00 29.70  ? 847  PHE   A CG  1 
ATOM   2309 C CD1 . PHE   A 1 310 ? 39.431  21.772  -7.892  1.00 33.00  ? 847  PHE   A CD1 1 
ATOM   2310 C CD2 . PHE   A 1 310 ? 41.568  21.301  -6.957  1.00 30.17  ? 847  PHE   A CD2 1 
ATOM   2311 C CE1 . PHE   A 1 310 ? 39.722  20.961  -8.970  1.00 30.21  ? 847  PHE   A CE1 1 
ATOM   2312 C CE2 . PHE   A 1 310 ? 41.861  20.485  -8.031  1.00 36.31  ? 847  PHE   A CE2 1 
ATOM   2313 C CZ  . PHE   A 1 310 ? 40.937  20.316  -9.039  1.00 33.49  ? 847  PHE   A CZ  1 
ATOM   2314 N N   . GLU   A 1 311 ? 40.088  20.821  -3.338  1.00 25.61  ? 848  GLU   A N   1 
ATOM   2315 C CA  . GLU   A 1 311 ? 40.505  19.515  -2.816  1.00 26.68  ? 848  GLU   A CA  1 
ATOM   2316 C C   . GLU   A 1 311 ? 39.332  18.759  -2.209  1.00 27.35  ? 848  GLU   A C   1 
ATOM   2317 O O   . GLU   A 1 311 ? 39.201  17.526  -2.363  1.00 26.37  ? 848  GLU   A O   1 
ATOM   2318 C CB  . GLU   A 1 311 ? 41.616  19.665  -1.770  1.00 31.81  ? 848  GLU   A CB  1 
ATOM   2319 C CG  . GLU   A 1 311 ? 42.962  20.021  -2.380  1.00 36.85  ? 848  GLU   A CG  1 
ATOM   2320 C CD  . GLU   A 1 311 ? 43.008  21.442  -2.912  1.00 43.04  ? 848  GLU   A CD  1 
ATOM   2321 O OE1 . GLU   A 1 311 ? 42.277  22.308  -2.386  1.00 37.76  ? 848  GLU   A OE1 1 
ATOM   2322 O OE2 . GLU   A 1 311 ? 43.774  21.701  -3.867  1.00 45.46  ? 848  GLU   A OE2 1 
ATOM   2323 N N   . GLU   A 1 312 ? 38.479  19.502  -1.516  1.00 24.82  ? 849  GLU   A N   1 
ATOM   2324 C CA  . GLU   A 1 312 ? 37.290  18.897  -0.921  1.00 26.32  ? 849  GLU   A CA  1 
ATOM   2325 C C   . GLU   A 1 312 ? 36.382  18.340  -2.011  1.00 28.77  ? 849  GLU   A C   1 
ATOM   2326 O O   . GLU   A 1 312 ? 35.848  17.243  -1.892  1.00 25.80  ? 849  GLU   A O   1 
ATOM   2327 C CB  . GLU   A 1 312 ? 36.543  19.923  -0.077  1.00 30.63  ? 849  GLU   A CB  1 
ATOM   2328 C CG  . GLU   A 1 312 ? 35.348  19.376  0.665   1.00 43.32  ? 849  GLU   A CG  1 
ATOM   2329 C CD  . GLU   A 1 312 ? 34.732  20.413  1.591   1.00 65.82  ? 849  GLU   A CD  1 
ATOM   2330 O OE1 . GLU   A 1 312 ? 35.475  21.305  2.080   1.00 62.28  ? 849  GLU   A OE1 1 
ATOM   2331 O OE2 . GLU   A 1 312 ? 33.503  20.339  1.817   1.00 71.03  ? 849  GLU   A OE2 1 
ATOM   2332 N N   . ARG   A 1 313 ? 36.236  19.093  -3.090  1.00 23.09  ? 850  ARG   A N   1 
ATOM   2333 C CA  . ARG   A 1 313 ? 35.318  18.691  -4.156  1.00 20.72  ? 850  ARG   A CA  1 
ATOM   2334 C C   . ARG   A 1 313 ? 35.833  17.437  -4.850  1.00 23.63  ? 850  ARG   A C   1 
ATOM   2335 O O   . ARG   A 1 313 ? 35.074  16.529  -5.189  1.00 22.20  ? 850  ARG   A O   1 
ATOM   2336 C CB  . ARG   A 1 313 ? 35.145  19.833  -5.163  1.00 20.12  ? 850  ARG   A CB  1 
ATOM   2337 C CG  . ARG   A 1 313 ? 34.104  19.548  -6.239  1.00 22.09  ? 850  ARG   A CG  1 
ATOM   2338 C CD  . ARG   A 1 313 ? 33.646  20.835  -6.932  1.00 22.62  ? 850  ARG   A CD  1 
ATOM   2339 N NE  . ARG   A 1 313 ? 34.668  21.437  -7.795  1.00 24.52  ? 850  ARG   A NE  1 
ATOM   2340 C CZ  . ARG   A 1 313 ? 35.351  22.543  -7.496  1.00 27.33  ? 850  ARG   A CZ  1 
ATOM   2341 N NH1 . ARG   A 1 313 ? 35.147  23.175  -6.345  1.00 24.95  ? 850  ARG   A NH1 1 
ATOM   2342 N NH2 . ARG   A 1 313 ? 36.241  23.020  -8.349  1.00 26.50  ? 850  ARG   A NH2 1 
ATOM   2343 N N   . VAL   A 1 314 ? 37.138  17.392  -5.078  1.00 22.99  ? 851  VAL   A N   1 
ATOM   2344 C CA  . VAL   A 1 314 ? 37.725  16.216  -5.678  1.00 24.66  ? 851  VAL   A CA  1 
ATOM   2345 C C   . VAL   A 1 314 ? 37.506  15.003  -4.771  1.00 26.12  ? 851  VAL   A C   1 
ATOM   2346 O O   . VAL   A 1 314 ? 37.224  13.911  -5.261  1.00 25.44  ? 851  VAL   A O   1 
ATOM   2347 C CB  . VAL   A 1 314 ? 39.219  16.425  -5.962  1.00 24.80  ? 851  VAL   A CB  1 
ATOM   2348 C CG1 . VAL   A 1 314 ? 39.869  15.121  -6.373  1.00 31.85  ? 851  VAL   A CG1 1 
ATOM   2349 C CG2 . VAL   A 1 314 ? 39.389  17.496  -7.060  1.00 25.62  ? 851  VAL   A CG2 1 
ATOM   2350 N N   . ALA   A 1 315 ? 37.596  15.210  -3.457  1.00 27.29  ? 852  ALA   A N   1 
ATOM   2351 C CA  . ALA   A 1 315 ? 37.391  14.128  -2.499  1.00 26.01  ? 852  ALA   A CA  1 
ATOM   2352 C C   . ALA   A 1 315 ? 35.929  13.681  -2.481  1.00 22.91  ? 852  ALA   A C   1 
ATOM   2353 O O   . ALA   A 1 315 ? 35.643  12.496  -2.321  1.00 24.58  ? 852  ALA   A O   1 
ATOM   2354 C CB  . ALA   A 1 315 ? 37.831  14.552  -1.106  1.00 27.54  ? 852  ALA   A CB  1 
ATOM   2355 N N   . VAL   A 1 316 ? 35.013  14.628  -2.671  1.00 23.08  ? 853  VAL   A N   1 
ATOM   2356 C CA  . VAL   A 1 316 ? 33.585  14.290  -2.736  1.00 18.95  ? 853  VAL   A CA  1 
ATOM   2357 C C   . VAL   A 1 316 ? 33.266  13.447  -3.968  1.00 22.29  ? 853  VAL   A C   1 
ATOM   2358 O O   . VAL   A 1 316 ? 32.591  12.404  -3.870  1.00 22.60  ? 853  VAL   A O   1 
ATOM   2359 C CB  . VAL   A 1 316 ? 32.726  15.564  -2.717  1.00 22.20  ? 853  VAL   A CB  1 
ATOM   2360 C CG1 . VAL   A 1 316 ? 31.311  15.273  -3.196  1.00 24.62  ? 853  VAL   A CG1 1 
ATOM   2361 C CG2 . VAL   A 1 316 ? 32.714  16.163  -1.295  1.00 23.70  ? 853  VAL   A CG2 1 
ATOM   2362 N N   . LEU   A 1 317 ? 33.757  13.880  -5.122  1.00 22.89  ? 854  LEU   A N   1 
ATOM   2363 C CA  . LEU   A 1 317 ? 33.543  13.125  -6.358  1.00 22.74  ? 854  LEU   A CA  1 
ATOM   2364 C C   . LEU   A 1 317 ? 34.165  11.741  -6.240  1.00 25.11  ? 854  LEU   A C   1 
ATOM   2365 O O   . LEU   A 1 317 ? 33.587  10.752  -6.687  1.00 24.85  ? 854  LEU   A O   1 
ATOM   2366 C CB  . LEU   A 1 317 ? 34.140  13.863  -7.567  1.00 20.27  ? 854  LEU   A CB  1 
ATOM   2367 C CG  . LEU   A 1 317 ? 33.936  13.185  -8.929  1.00 24.91  ? 854  LEU   A CG  1 
ATOM   2368 C CD1 . LEU   A 1 317 ? 32.446  12.935  -9.198  1.00 25.52  ? 854  LEU   A CD1 1 
ATOM   2369 C CD2 . LEU   A 1 317 ? 34.558  14.016  -10.061 1.00 26.70  ? 854  LEU   A CD2 1 
ATOM   2370 N N   . SER   A 1 318 ? 35.361  11.679  -5.644  1.00 24.91  ? 855  SER   A N   1 
ATOM   2371 C CA  . SER   A 1 318 ? 36.039  10.405  -5.433  1.00 23.08  ? 855  SER   A CA  1 
ATOM   2372 C C   . SER   A 1 318 ? 35.213  9.481   -4.535  1.00 22.62  ? 855  SER   A C   1 
ATOM   2373 O O   . SER   A 1 318 ? 35.133  8.287   -4.793  1.00 25.63  ? 855  SER   A O   1 
ATOM   2374 C CB  . SER   A 1 318 ? 37.429  10.626  -4.829  1.00 25.86  ? 855  SER   A CB  1 
ATOM   2375 O OG  . SER   A 1 318 ? 38.234  11.379  -5.724  1.00 31.07  ? 855  SER   A OG  1 
ATOM   2376 N N   . ARG   A 1 319 ? 34.596  10.041  -3.500  1.00 26.42  ? 856  ARG   A N   1 
ATOM   2377 C CA  . ARG   A 1 319 ? 33.786  9.251   -2.575  1.00 23.67  ? 856  ARG   A CA  1 
ATOM   2378 C C   . ARG   A 1 319 ? 32.549  8.725   -3.281  1.00 23.89  ? 856  ARG   A C   1 
ATOM   2379 O O   . ARG   A 1 319 ? 32.118  7.593   -3.050  1.00 24.45  ? 856  ARG   A O   1 
ATOM   2380 C CB  . ARG   A 1 319 ? 33.374  10.082  -1.360  1.00 22.80  ? 856  ARG   A CB  1 
ATOM   2381 C CG  . ARG   A 1 319 ? 32.910  9.260   -0.160  1.00 21.09  ? 856  ARG   A CG  1 
ATOM   2382 C CD  . ARG   A 1 319 ? 34.050  8.443   0.471   1.00 23.06  ? 856  ARG   A CD  1 
ATOM   2383 N NE  . ARG   A 1 319 ? 35.116  9.325   0.948   1.00 25.23  ? 856  ARG   A NE  1 
ATOM   2384 C CZ  . ARG   A 1 319 ? 35.127  9.911   2.143   1.00 28.64  ? 856  ARG   A CZ  1 
ATOM   2385 N NH1 . ARG   A 1 319 ? 34.135  9.702   3.013   1.00 26.77  ? 856  ARG   A NH1 1 
ATOM   2386 N NH2 . ARG   A 1 319 ? 36.135  10.720  2.470   1.00 30.23  ? 856  ARG   A NH2 1 
ATOM   2387 N N   . ILE   A 1 320 ? 31.985  9.553   -4.153  1.00 21.33  ? 857  ILE   A N   1 
ATOM   2388 C CA  . ILE   A 1 320 ? 30.808  9.148   -4.923  1.00 20.43  ? 857  ILE   A CA  1 
ATOM   2389 C C   . ILE   A 1 320 ? 31.169  8.007   -5.880  1.00 23.57  ? 857  ILE   A C   1 
ATOM   2390 O O   . ILE   A 1 320 ? 30.384  7.078   -6.077  1.00 22.38  ? 857  ILE   A O   1 
ATOM   2391 C CB  . ILE   A 1 320 ? 30.206  10.355  -5.666  1.00 22.54  ? 857  ILE   A CB  1 
ATOM   2392 C CG1 . ILE   A 1 320 ? 29.557  11.281  -4.631  1.00 20.42  ? 857  ILE   A CG1 1 
ATOM   2393 C CG2 . ILE   A 1 320 ? 29.188  9.900   -6.740  1.00 21.10  ? 857  ILE   A CG2 1 
ATOM   2394 C CD1 . ILE   A 1 320 ? 29.131  12.644  -5.151  1.00 22.99  ? 857  ILE   A CD1 1 
ATOM   2395 N N   . ILE   A 1 321 ? 32.379  8.034   -6.432  1.00 22.41  ? 858  ILE   A N   1 
ATOM   2396 C CA  . ILE   A 1 321 ? 32.806  6.918   -7.278  1.00 23.25  ? 858  ILE   A CA  1 
ATOM   2397 C C   . ILE   A 1 321 ? 32.986  5.640   -6.435  1.00 25.61  ? 858  ILE   A C   1 
ATOM   2398 O O   . ILE   A 1 321 ? 32.658  4.538   -6.884  1.00 28.34  ? 858  ILE   A O   1 
ATOM   2399 C CB  . ILE   A 1 321 ? 34.091  7.264   -8.038  1.00 24.90  ? 858  ILE   A CB  1 
ATOM   2400 C CG1 . ILE   A 1 321 ? 33.803  8.395   -9.027  1.00 26.13  ? 858  ILE   A CG1 1 
ATOM   2401 C CG2 . ILE   A 1 321 ? 34.613  6.051   -8.800  1.00 29.24  ? 858  ILE   A CG2 1 
ATOM   2402 C CD1 . ILE   A 1 321 ? 35.051  8.976   -9.698  1.00 29.12  ? 858  ILE   A CD1 1 
ATOM   2403 N N   . GLU   A 1 322 ? 33.475  5.779   -5.205  1.00 23.98  ? 859  GLU   A N   1 
ATOM   2404 C CA  . GLU   A 1 322 ? 33.585  4.610   -4.340  1.00 23.65  ? 859  GLU   A CA  1 
ATOM   2405 C C   . GLU   A 1 322 ? 32.207  4.017   -4.035  1.00 24.99  ? 859  GLU   A C   1 
ATOM   2406 O O   . GLU   A 1 322 ? 32.041  2.800   -4.017  1.00 26.59  ? 859  GLU   A O   1 
ATOM   2407 C CB  . GLU   A 1 322 ? 34.298  4.952   -3.047  1.00 27.63  ? 859  GLU   A CB  1 
ATOM   2408 C CG  . GLU   A 1 322 ? 35.786  5.236   -3.276  1.00 26.93  ? 859  GLU   A CG  1 
ATOM   2409 C CD  . GLU   A 1 322 ? 36.519  5.510   -1.987  1.00 41.09  ? 859  GLU   A CD  1 
ATOM   2410 O OE1 . GLU   A 1 322 ? 35.968  6.237   -1.144  1.00 37.06  ? 859  GLU   A OE1 1 
ATOM   2411 O OE2 . GLU   A 1 322 ? 37.641  4.989   -1.808  1.00 50.91  ? 859  GLU   A OE2 1 
ATOM   2412 N N   . ILE   A 1 323 ? 31.235  4.881   -3.780  1.00 22.39  ? 860  ILE   A N   1 
ATOM   2413 C CA  . ILE   A 1 323 ? 29.857  4.430   -3.550  1.00 20.30  ? 860  ILE   A CA  1 
ATOM   2414 C C   . ILE   A 1 323 ? 29.353  3.698   -4.803  1.00 21.29  ? 860  ILE   A C   1 
ATOM   2415 O O   . ILE   A 1 323 ? 28.737  2.625   -4.705  1.00 21.74  ? 860  ILE   A O   1 
ATOM   2416 C CB  . ILE   A 1 323 ? 28.943  5.622   -3.180  1.00 22.05  ? 860  ILE   A CB  1 
ATOM   2417 C CG1 . ILE   A 1 323 ? 29.355  6.168   -1.808  1.00 22.18  ? 860  ILE   A CG1 1 
ATOM   2418 C CG2 . ILE   A 1 323 ? 27.456  5.195   -3.171  1.00 24.36  ? 860  ILE   A CG2 1 
ATOM   2419 C CD1 . ILE   A 1 323 ? 28.813  7.570   -1.511  1.00 24.97  ? 860  ILE   A CD1 1 
ATOM   2420 N N   . LEU   A 1 324 ? 29.666  4.243   -5.977  1.00 22.78  ? 861  LEU   A N   1 
ATOM   2421 C CA  . LEU   A 1 324 ? 29.305  3.577   -7.239  1.00 21.58  ? 861  LEU   A CA  1 
ATOM   2422 C C   . LEU   A 1 324 ? 29.896  2.168   -7.322  1.00 23.94  ? 861  LEU   A C   1 
ATOM   2423 O O   . LEU   A 1 324 ? 29.222  1.232   -7.730  1.00 26.55  ? 861  LEU   A O   1 
ATOM   2424 C CB  . LEU   A 1 324 ? 29.773  4.403   -8.447  1.00 22.95  ? 861  LEU   A CB  1 
ATOM   2425 C CG  . LEU   A 1 324 ? 29.412  3.804   -9.814  1.00 29.50  ? 861  LEU   A CG  1 
ATOM   2426 C CD1 . LEU   A 1 324 ? 29.089  4.903   -10.790 1.00 28.85  ? 861  LEU   A CD1 1 
ATOM   2427 C CD2 . LEU   A 1 324 ? 30.542  2.951   -10.374 1.00 30.62  ? 861  LEU   A CD2 1 
ATOM   2428 N N   . GLN   A 1 325 ? 31.169  2.033   -6.966  1.00 24.48  ? 862  GLN   A N   1 
ATOM   2429 C CA  . GLN   A 1 325 ? 31.818  0.718   -6.946  1.00 22.86  ? 862  GLN   A CA  1 
ATOM   2430 C C   . GLN   A 1 325 ? 31.064  -0.287  -6.090  1.00 26.14  ? 862  GLN   A C   1 
ATOM   2431 O O   . GLN   A 1 325 ? 30.862  -1.440  -6.488  1.00 30.59  ? 862  GLN   A O   1 
ATOM   2432 C CB  . GLN   A 1 325 ? 33.248  0.827   -6.417  1.00 30.36  ? 862  GLN   A CB  1 
ATOM   2433 C CG  . GLN   A 1 325 ? 34.238  1.493   -7.322  1.00 50.12  ? 862  GLN   A CG  1 
ATOM   2434 C CD  . GLN   A 1 325 ? 35.615  1.561   -6.677  1.00 58.18  ? 862  GLN   A CD  1 
ATOM   2435 O OE1 . GLN   A 1 325 ? 36.024  2.601   -6.161  1.00 56.35  ? 862  GLN   A OE1 1 
ATOM   2436 N NE2 . GLN   A 1 325 ? 36.326  0.440   -6.687  1.00 61.97  ? 862  GLN   A NE2 1 
ATOM   2437 N N   . VAL   A 1 326 ? 30.655  0.136   -4.900  1.00 21.06  ? 863  VAL   A N   1 
ATOM   2438 C CA  . VAL   A 1 326 ? 29.935  -0.782  -4.017  1.00 24.35  ? 863  VAL   A CA  1 
ATOM   2439 C C   . VAL   A 1 326 ? 28.518  -1.096  -4.547  1.00 26.83  ? 863  VAL   A C   1 
ATOM   2440 O O   . VAL   A 1 326 ? 28.046  -2.238  -4.433  1.00 27.51  ? 863  VAL   A O   1 
ATOM   2441 C CB  . VAL   A 1 326 ? 29.857  -0.223  -2.597  1.00 25.97  ? 863  VAL   A CB  1 
ATOM   2442 C CG1 . VAL   A 1 326 ? 29.148  -1.216  -1.684  1.00 28.58  ? 863  VAL   A CG1 1 
ATOM   2443 C CG2 . VAL   A 1 326 ? 31.282  0.036   -2.052  1.00 29.81  ? 863  VAL   A CG2 1 
ATOM   2444 N N   . PHE   A 1 327 ? 27.837  -0.089  -5.105  1.00 24.37  ? 864  PHE   A N   1 
ATOM   2445 C CA  . PHE   A 1 327 ? 26.585  -0.324  -5.854  1.00 24.61  ? 864  PHE   A CA  1 
ATOM   2446 C C   . PHE   A 1 327 ? 26.793  -1.412  -6.912  1.00 26.34  ? 864  PHE   A C   1 
ATOM   2447 O O   . PHE   A 1 327 ? 26.014  -2.364  -7.008  1.00 28.21  ? 864  PHE   A O   1 
ATOM   2448 C CB  . PHE   A 1 327 ? 26.096  0.943   -6.575  1.00 24.20  ? 864  PHE   A CB  1 
ATOM   2449 C CG  . PHE   A 1 327 ? 25.319  1.917   -5.723  1.00 20.90  ? 864  PHE   A CG  1 
ATOM   2450 C CD1 . PHE   A 1 327 ? 24.597  1.508   -4.610  1.00 24.08  ? 864  PHE   A CD1 1 
ATOM   2451 C CD2 . PHE   A 1 327 ? 25.281  3.257   -6.086  1.00 21.71  ? 864  PHE   A CD2 1 
ATOM   2452 C CE1 . PHE   A 1 327 ? 23.865  2.425   -3.868  1.00 23.12  ? 864  PHE   A CE1 1 
ATOM   2453 C CE2 . PHE   A 1 327 ? 24.540  4.179   -5.361  1.00 23.88  ? 864  PHE   A CE2 1 
ATOM   2454 C CZ  . PHE   A 1 327 ? 23.838  3.767   -4.249  1.00 21.36  ? 864  PHE   A CZ  1 
ATOM   2455 N N   . GLN   A 1 328 ? 27.847  -1.253  -7.711  1.00 26.04  ? 865  GLN   A N   1 
ATOM   2456 C CA  . GLN   A 1 328 ? 28.220  -2.245  -8.731  1.00 27.12  ? 865  GLN   A CA  1 
ATOM   2457 C C   . GLN   A 1 328 ? 28.440  -3.647  -8.125  1.00 28.89  ? 865  GLN   A C   1 
ATOM   2458 O O   . GLN   A 1 328 ? 27.930  -4.647  -8.632  1.00 32.77  ? 865  GLN   A O   1 
ATOM   2459 C CB  . GLN   A 1 328 ? 29.500  -1.815  -9.456  1.00 35.45  ? 865  GLN   A CB  1 
ATOM   2460 C CG  . GLN   A 1 328 ? 29.315  -0.823  -10.584 1.00 47.65  ? 865  GLN   A CG  1 
ATOM   2461 C CD  . GLN   A 1 328 ? 29.260  -1.499  -11.938 1.00 57.32  ? 865  GLN   A CD  1 
ATOM   2462 O OE1 . GLN   A 1 328 ? 28.829  -2.645  -12.050 1.00 70.00  ? 865  GLN   A OE1 1 
ATOM   2463 N NE2 . GLN   A 1 328 ? 29.700  -0.797  -12.972 1.00 48.81  ? 865  GLN   A NE2 1 
ATOM   2464 N N   . ASP   A 1 329 ? 29.212  -3.715  -7.046  1.00 28.48  ? 866  ASP   A N   1 
ATOM   2465 C CA  . ASP   A 1 329 ? 29.465  -4.993  -6.378  1.00 29.50  ? 866  ASP   A CA  1 
ATOM   2466 C C   . ASP   A 1 329 ? 28.171  -5.645  -5.893  1.00 32.31  ? 866  ASP   A C   1 
ATOM   2467 O O   . ASP   A 1 329 ? 28.065  -6.869  -5.847  1.00 32.61  ? 866  ASP   A O   1 
ATOM   2468 C CB  . ASP   A 1 329 ? 30.409  -4.814  -5.184  1.00 30.60  ? 866  ASP   A CB  1 
ATOM   2469 C CG  . ASP   A 1 329 ? 31.783  -4.331  -5.593  1.00 48.51  ? 866  ASP   A CG  1 
ATOM   2470 O OD1 . ASP   A 1 329 ? 32.152  -4.497  -6.780  1.00 50.50  ? 866  ASP   A OD1 1 
ATOM   2471 O OD2 . ASP   A 1 329 ? 32.494  -3.781  -4.720  1.00 54.57  ? 866  ASP   A OD2 1 
ATOM   2472 N N   . LEU   A 1 330 ? 27.194  -4.818  -5.527  1.00 27.70  ? 867  LEU   A N   1 
ATOM   2473 C CA  . LEU   A 1 330 ? 25.912  -5.294  -5.010  1.00 32.85  ? 867  LEU   A CA  1 
ATOM   2474 C C   . LEU   A 1 330 ? 24.861  -5.517  -6.106  1.00 29.63  ? 867  LEU   A C   1 
ATOM   2475 O O   . LEU   A 1 330 ? 23.706  -5.840  -5.809  1.00 32.28  ? 867  LEU   A O   1 
ATOM   2476 C CB  . LEU   A 1 330 ? 25.370  -4.301  -3.978  1.00 27.66  ? 867  LEU   A CB  1 
ATOM   2477 C CG  . LEU   A 1 330 ? 26.125  -4.184  -2.650  1.00 27.34  ? 867  LEU   A CG  1 
ATOM   2478 C CD1 . LEU   A 1 330 ? 25.591  -3.000  -1.840  1.00 26.32  ? 867  LEU   A CD1 1 
ATOM   2479 C CD2 . LEU   A 1 330 ? 25.980  -5.469  -1.854  1.00 26.35  ? 867  LEU   A CD2 1 
ATOM   2480 N N   . ASN   A 1 331 ? 25.261  -5.347  -7.368  1.00 26.44  ? 868  ASN   A N   1 
ATOM   2481 C CA  . ASN   A 1 331 ? 24.326  -5.380  -8.499  1.00 28.68  ? 868  ASN   A CA  1 
ATOM   2482 C C   . ASN   A 1 331 ? 23.162  -4.405  -8.361  1.00 28.37  ? 868  ASN   A C   1 
ATOM   2483 O O   . ASN   A 1 331 ? 22.064  -4.696  -8.833  1.00 30.03  ? 868  ASN   A O   1 
ATOM   2484 C CB  . ASN   A 1 331 ? 23.753  -6.791  -8.708  1.00 28.19  ? 868  ASN   A CB  1 
ATOM   2485 C CG  . ASN   A 1 331 ? 24.799  -7.786  -9.156  1.00 36.32  ? 868  ASN   A CG  1 
ATOM   2486 O OD1 . ASN   A 1 331 ? 25.803  -7.418  -9.764  1.00 36.27  ? 868  ASN   A OD1 1 
ATOM   2487 N ND2 . ASN   A 1 331 ? 24.567  -9.060  -8.857  1.00 41.84  ? 868  ASN   A ND2 1 
ATOM   2488 N N   . ASN   A 1 332 ? 23.397  -3.260  -7.717  1.00 24.98  ? 869  ASN   A N   1 
ATOM   2489 C CA  . ASN   A 1 332 ? 22.389  -2.211  -7.677  1.00 24.69  ? 869  ASN   A CA  1 
ATOM   2490 C C   . ASN   A 1 332 ? 22.639  -1.280  -8.847  1.00 30.04  ? 869  ASN   A C   1 
ATOM   2491 O O   . ASN   A 1 332 ? 23.319  -0.267  -8.704  1.00 24.54  ? 869  ASN   A O   1 
ATOM   2492 C CB  . ASN   A 1 332 ? 22.416  -1.433  -6.348  1.00 23.48  ? 869  ASN   A CB  1 
ATOM   2493 C CG  . ASN   A 1 332 ? 21.383  -0.318  -6.320  1.00 24.80  ? 869  ASN   A CG  1 
ATOM   2494 O OD1 . ASN   A 1 332 ? 20.673  -0.119  -7.304  1.00 25.14  ? 869  ASN   A OD1 1 
ATOM   2495 N ND2 . ASN   A 1 332 ? 21.297  0.417   -5.207  1.00 24.95  ? 869  ASN   A ND2 1 
ATOM   2496 N N   . PHE   A 1 333 ? 22.102  -1.624  -10.013 1.00 27.28  ? 870  PHE   A N   1 
ATOM   2497 C CA  . PHE   A 1 333 ? 22.331  -0.791  -11.189 1.00 27.11  ? 870  PHE   A CA  1 
ATOM   2498 C C   . PHE   A 1 333 ? 21.477  0.470   -11.159 1.00 27.73  ? 870  PHE   A C   1 
ATOM   2499 O O   . PHE   A 1 333 ? 21.804  1.453   -11.808 1.00 27.56  ? 870  PHE   A O   1 
ATOM   2500 C CB  . PHE   A 1 333 ? 22.094  -1.613  -12.457 1.00 31.35  ? 870  PHE   A CB  1 
ATOM   2501 C CG  . PHE   A 1 333 ? 23.138  -2.673  -12.663 1.00 34.52  ? 870  PHE   A CG  1 
ATOM   2502 C CD1 . PHE   A 1 333 ? 24.391  -2.332  -13.146 1.00 36.97  ? 870  PHE   A CD1 1 
ATOM   2503 C CD2 . PHE   A 1 333 ? 22.893  -3.990  -12.313 1.00 46.79  ? 870  PHE   A CD2 1 
ATOM   2504 C CE1 . PHE   A 1 333 ? 25.372  -3.296  -13.311 1.00 45.66  ? 870  PHE   A CE1 1 
ATOM   2505 C CE2 . PHE   A 1 333 ? 23.866  -4.959  -12.479 1.00 42.95  ? 870  PHE   A CE2 1 
ATOM   2506 C CZ  . PHE   A 1 333 ? 25.105  -4.613  -12.973 1.00 48.02  ? 870  PHE   A CZ  1 
ATOM   2507 N N   . ASN   A 1 334 ? 20.391  0.450   -10.393 1.00 27.80  ? 871  ASN   A N   1 
ATOM   2508 C CA  . ASN   A 1 334 ? 19.634  1.664   -10.167 1.00 25.46  ? 871  ASN   A CA  1 
ATOM   2509 C C   . ASN   A 1 334 ? 20.550  2.732   -9.558  1.00 28.16  ? 871  ASN   A C   1 
ATOM   2510 O O   . ASN   A 1 334 ? 20.607  3.872   -10.028 1.00 24.99  ? 871  ASN   A O   1 
ATOM   2511 C CB  . ASN   A 1 334 ? 18.448  1.397   -9.250  1.00 26.55  ? 871  ASN   A CB  1 
ATOM   2512 C CG  . ASN   A 1 334 ? 17.494  2.557   -9.201  1.00 37.44  ? 871  ASN   A CG  1 
ATOM   2513 O OD1 . ASN   A 1 334 ? 16.714  2.756   -10.127 1.00 38.96  ? 871  ASN   A OD1 1 
ATOM   2514 N ND2 . ASN   A 1 334 ? 17.552  3.339   -8.124  1.00 33.72  ? 871  ASN   A ND2 1 
ATOM   2515 N N   . GLY   A 1 335 ? 21.282  2.340   -8.525  1.00 23.40  ? 872  GLY   A N   1 
ATOM   2516 C CA  . GLY   A 1 335 ? 22.223  3.236   -7.875  1.00 20.03  ? 872  GLY   A CA  1 
ATOM   2517 C C   . GLY   A 1 335 ? 23.387  3.625   -8.773  1.00 22.06  ? 872  GLY   A C   1 
ATOM   2518 O O   . GLY   A 1 335 ? 23.819  4.773   -8.756  1.00 22.39  ? 872  GLY   A O   1 
ATOM   2519 N N   . VAL   A 1 336 ? 23.919  2.671   -9.535  1.00 20.90  ? 873  VAL   A N   1 
ATOM   2520 C CA  . VAL   A 1 336 ? 25.031  2.989   -10.428 1.00 22.57  ? 873  VAL   A CA  1 
ATOM   2521 C C   . VAL   A 1 336 ? 24.619  4.072   -11.404 1.00 22.78  ? 873  VAL   A C   1 
ATOM   2522 O O   . VAL   A 1 336 ? 25.361  5.036   -11.640 1.00 22.95  ? 873  VAL   A O   1 
ATOM   2523 C CB  . VAL   A 1 336 ? 25.501  1.750   -11.227 1.00 22.48  ? 873  VAL   A CB  1 
ATOM   2524 C CG1 . VAL   A 1 336 ? 26.488  2.151   -12.326 1.00 24.06  ? 873  VAL   A CG1 1 
ATOM   2525 C CG2 . VAL   A 1 336 ? 26.135  0.722   -10.288 1.00 22.38  ? 873  VAL   A CG2 1 
ATOM   2526 N N   . LEU   A 1 337 ? 23.429  3.916   -11.989 1.00 21.95  ? 874  LEU   A N   1 
ATOM   2527 C CA  . LEU   A 1 337 ? 23.010  4.856   -13.019 1.00 27.18  ? 874  LEU   A CA  1 
ATOM   2528 C C   . LEU   A 1 337 ? 22.483  6.181   -12.446 1.00 26.87  ? 874  LEU   A C   1 
ATOM   2529 O O   . LEU   A 1 337 ? 22.482  7.193   -13.154 1.00 25.17  ? 874  LEU   A O   1 
ATOM   2530 C CB  . LEU   A 1 337 ? 21.966  4.222   -13.948 1.00 25.04  ? 874  LEU   A CB  1 
ATOM   2531 C CG  . LEU   A 1 337 ? 22.544  3.325   -15.057 1.00 33.10  ? 874  LEU   A CG  1 
ATOM   2532 C CD1 . LEU   A 1 337 ? 23.759  3.962   -15.753 1.00 34.76  ? 874  LEU   A CD1 1 
ATOM   2533 C CD2 . LEU   A 1 337 ? 22.897  1.967   -14.564 1.00 45.85  ? 874  LEU   A CD2 1 
ATOM   2534 N N   . GLU   A 1 338 ? 22.058  6.200   -11.181 1.00 22.97  ? 875  GLU   A N   1 
ATOM   2535 C CA  . GLU   A 1 338 ? 21.782  7.471   -10.506 1.00 22.77  ? 875  GLU   A CA  1 
ATOM   2536 C C   . GLU   A 1 338 ? 23.046  8.329   -10.433 1.00 22.44  ? 875  GLU   A C   1 
ATOM   2537 O O   . GLU   A 1 338 ? 23.010  9.548   -10.635 1.00 22.50  ? 875  GLU   A O   1 
ATOM   2538 C CB  . GLU   A 1 338 ? 21.245  7.249   -9.087  1.00 27.39  ? 875  GLU   A CB  1 
ATOM   2539 C CG  . GLU   A 1 338 ? 19.786  6.826   -9.055  1.00 35.61  ? 875  GLU   A CG  1 
ATOM   2540 C CD  . GLU   A 1 338 ? 19.364  6.239   -7.714  1.00 31.22  ? 875  GLU   A CD  1 
ATOM   2541 O OE1 . GLU   A 1 338 ? 20.231  5.715   -6.982  1.00 31.87  ? 875  GLU   A OE1 1 
ATOM   2542 O OE2 . GLU   A 1 338 ? 18.157  6.283   -7.406  1.00 37.95  ? 875  GLU   A OE2 1 
ATOM   2543 N N   . ILE   A 1 339 ? 24.161  7.688   -10.107 1.00 20.34  ? 876  ILE   A N   1 
ATOM   2544 C CA  . ILE   A 1 339 ? 25.430  8.408   -10.041 1.00 18.81  ? 876  ILE   A CA  1 
ATOM   2545 C C   . ILE   A 1 339 ? 25.923  8.825   -11.430 1.00 23.37  ? 876  ILE   A C   1 
ATOM   2546 O O   . ILE   A 1 339 ? 26.407  9.942   -11.603 1.00 21.02  ? 876  ILE   A O   1 
ATOM   2547 C CB  . ILE   A 1 339 ? 26.476  7.567   -9.308  1.00 20.58  ? 876  ILE   A CB  1 
ATOM   2548 C CG1 . ILE   A 1 339 ? 26.140  7.624   -7.809  1.00 20.26  ? 876  ILE   A CG1 1 
ATOM   2549 C CG2 . ILE   A 1 339 ? 27.887  8.121   -9.561  1.00 20.51  ? 876  ILE   A CG2 1 
ATOM   2550 C CD1 . ILE   A 1 339 ? 26.927  6.636   -6.927  1.00 21.99  ? 876  ILE   A CD1 1 
ATOM   2551 N N   . VAL   A 1 340 ? 25.767  7.955   -12.424 1.00 23.82  ? 877  VAL   A N   1 
ATOM   2552 C CA  . VAL   A 1 340 ? 26.099  8.325   -13.803 1.00 21.01  ? 877  VAL   A CA  1 
ATOM   2553 C C   . VAL   A 1 340 ? 25.261  9.537   -14.241 1.00 22.07  ? 877  VAL   A C   1 
ATOM   2554 O O   . VAL   A 1 340 ? 25.764  10.485  -14.860 1.00 21.30  ? 877  VAL   A O   1 
ATOM   2555 C CB  . VAL   A 1 340 ? 25.873  7.148   -14.759 1.00 23.36  ? 877  VAL   A CB  1 
ATOM   2556 C CG1 . VAL   A 1 340 ? 26.022  7.603   -16.244 1.00 24.80  ? 877  VAL   A CG1 1 
ATOM   2557 C CG2 . VAL   A 1 340 ? 26.863  6.034   -14.422 1.00 21.39  ? 877  VAL   A CG2 1 
ATOM   2558 N N   . SER   A 1 341 ? 23.984  9.506   -13.889 1.00 21.45  ? 878  SER   A N   1 
ATOM   2559 C CA  . SER   A 1 341 ? 23.090  10.608  -14.221 1.00 19.77  ? 878  SER   A CA  1 
ATOM   2560 C C   . SER   A 1 341 ? 23.595  11.899  -13.571 1.00 24.20  ? 878  SER   A C   1 
ATOM   2561 O O   . SER   A 1 341 ? 23.622  12.958  -14.193 1.00 22.10  ? 878  SER   A O   1 
ATOM   2562 C CB  . SER   A 1 341 ? 21.664  10.272  -13.763 1.00 24.06  ? 878  SER   A CB  1 
ATOM   2563 O OG  . SER   A 1 341 ? 20.743  11.282  -14.106 1.00 25.71  ? 878  SER   A OG  1 
ATOM   2564 N N   . ALA   A 1 342 ? 24.024  11.798  -12.319 1.00 20.04  ? 879  ALA   A N   1 
ATOM   2565 C CA  . ALA   A 1 342 ? 24.514  12.962  -11.593 1.00 19.65  ? 879  ALA   A CA  1 
ATOM   2566 C C   . ALA   A 1 342 ? 25.758  13.554  -12.241 1.00 21.56  ? 879  ALA   A C   1 
ATOM   2567 O O   . ALA   A 1 342 ? 25.848  14.763  -12.377 1.00 19.09  ? 879  ALA   A O   1 
ATOM   2568 C CB  . ALA   A 1 342 ? 24.802  12.606  -10.119 1.00 18.53  ? 879  ALA   A CB  1 
ATOM   2569 N N   . VAL   A 1 343 ? 26.718  12.731  -12.663 1.00 19.31  ? 880  VAL   A N   1 
ATOM   2570 C CA  . VAL   A 1 343 ? 27.917  13.325  -13.262 1.00 19.64  ? 880  VAL   A CA  1 
ATOM   2571 C C   . VAL   A 1 343 ? 27.676  13.789  -14.707 1.00 23.08  ? 880  VAL   A C   1 
ATOM   2572 O O   . VAL   A 1 343 ? 28.414  14.648  -15.205 1.00 22.08  ? 880  VAL   A O   1 
ATOM   2573 C CB  . VAL   A 1 343 ? 29.125  12.358  -13.198 1.00 24.46  ? 880  VAL   A CB  1 
ATOM   2574 C CG1 . VAL   A 1 343 ? 29.505  12.103  -11.731 1.00 23.71  ? 880  VAL   A CG1 1 
ATOM   2575 C CG2 . VAL   A 1 343 ? 28.847  11.051  -13.929 1.00 24.40  ? 880  VAL   A CG2 1 
ATOM   2576 N N   . ASN   A 1 344 ? 26.629  13.270  -15.358 1.00 21.44  ? 881  ASN   A N   1 
ATOM   2577 C CA  . ASN   A 1 344 ? 26.229  13.773  -16.685 1.00 22.75  ? 881  ASN   A CA  1 
ATOM   2578 C C   . ASN   A 1 344 ? 25.477  15.109  -16.638 1.00 20.85  ? 881  ASN   A C   1 
ATOM   2579 O O   . ASN   A 1 344 ? 25.342  15.774  -17.662 1.00 22.96  ? 881  ASN   A O   1 
ATOM   2580 C CB  . ASN   A 1 344 ? 25.333  12.768  -17.426 1.00 21.75  ? 881  ASN   A CB  1 
ATOM   2581 C CG  . ASN   A 1 344 ? 26.113  11.650  -18.082 1.00 28.47  ? 881  ASN   A CG  1 
ATOM   2582 O OD1 . ASN   A 1 344 ? 27.335  11.687  -18.149 1.00 27.51  ? 881  ASN   A OD1 1 
ATOM   2583 N ND2 . ASN   A 1 344 ? 25.398  10.638  -18.573 1.00 25.95  ? 881  ASN   A ND2 1 
ATOM   2584 N N   . SER   A 1 345 ? 24.947  15.470  -15.466 1.00 21.64  ? 882  SER   A N   1 
ATOM   2585 C CA  . SER   A 1 345 ? 24.158  16.695  -15.326 1.00 19.06  ? 882  SER   A CA  1 
ATOM   2586 C C   . SER   A 1 345 ? 24.939  17.919  -15.815 1.00 26.62  ? 882  SER   A C   1 
ATOM   2587 O O   . SER   A 1 345 ? 26.153  17.965  -15.706 1.00 22.21  ? 882  SER   A O   1 
ATOM   2588 C CB  . SER   A 1 345 ? 23.722  16.898  -13.868 1.00 21.54  ? 882  SER   A CB  1 
ATOM   2589 O OG  . SER   A 1 345 ? 24.817  17.268  -13.044 1.00 21.48  ? 882  SER   A OG  1 
ATOM   2590 N N   . VAL   A 1 346 ? 24.256  18.918  -16.366 1.00 21.78  ? 883  VAL   A N   1 
ATOM   2591 C CA  . VAL   A 1 346 ? 25.023  19.999  -16.991 1.00 21.23  ? 883  VAL   A CA  1 
ATOM   2592 C C   . VAL   A 1 346 ? 25.875  20.781  -15.977 1.00 24.79  ? 883  VAL   A C   1 
ATOM   2593 O O   . VAL   A 1 346 ? 26.942  21.283  -16.330 1.00 25.90  ? 883  VAL   A O   1 
ATOM   2594 C CB  . VAL   A 1 346 ? 24.099  20.973  -17.773 1.00 25.65  ? 883  VAL   A CB  1 
ATOM   2595 C CG1 . VAL   A 1 346 ? 23.485  20.247  -18.977 1.00 31.52  ? 883  VAL   A CG1 1 
ATOM   2596 C CG2 . VAL   A 1 346 ? 23.005  21.537  -16.866 1.00 25.33  ? 883  VAL   A CG2 1 
ATOM   2597 N N   . SER   A 1 347 ? 25.444  20.843  -14.719 1.00 22.41  ? 884  SER   A N   1 
ATOM   2598 C CA  . SER   A 1 347 ? 26.204  21.586  -13.703 1.00 20.26  ? 884  SER   A CA  1 
ATOM   2599 C C   . SER   A 1 347 ? 27.472  20.843  -13.287 1.00 24.63  ? 884  SER   A C   1 
ATOM   2600 O O   . SER   A 1 347 ? 28.485  21.466  -12.928 1.00 23.10  ? 884  SER   A O   1 
ATOM   2601 C CB  . SER   A 1 347 ? 25.347  21.853  -12.467 1.00 26.57  ? 884  SER   A CB  1 
ATOM   2602 O OG  . SER   A 1 347 ? 25.005  20.644  -11.811 1.00 29.90  ? 884  SER   A OG  1 
ATOM   2603 N N   . VAL   A 1 348 ? 27.421  19.515  -13.308 1.00 20.20  ? 885  VAL   A N   1 
ATOM   2604 C CA  . VAL   A 1 348 ? 28.600  18.734  -12.877 1.00 18.27  ? 885  VAL   A CA  1 
ATOM   2605 C C   . VAL   A 1 348 ? 29.560  18.425  -14.032 1.00 21.11  ? 885  VAL   A C   1 
ATOM   2606 O O   . VAL   A 1 348 ? 30.776  18.530  -13.893 1.00 20.94  ? 885  VAL   A O   1 
ATOM   2607 C CB  . VAL   A 1 348 ? 28.171  17.415  -12.210 1.00 23.54  ? 885  VAL   A CB  1 
ATOM   2608 C CG1 . VAL   A 1 348 ? 29.401  16.526  -11.887 1.00 20.01  ? 885  VAL   A CG1 1 
ATOM   2609 C CG2 . VAL   A 1 348 ? 27.410  17.708  -10.925 1.00 22.74  ? 885  VAL   A CG2 1 
ATOM   2610 N N   . TYR   A 1 349 ? 28.990  18.047  -15.171 1.00 20.47  ? 886  TYR   A N   1 
ATOM   2611 C CA  . TYR   A 1 349 ? 29.737  17.614  -16.348 1.00 21.09  ? 886  TYR   A CA  1 
ATOM   2612 C C   . TYR   A 1 349 ? 30.736  18.664  -16.787 1.00 26.39  ? 886  TYR   A C   1 
ATOM   2613 O O   . TYR   A 1 349 ? 31.802  18.328  -17.320 1.00 24.32  ? 886  TYR   A O   1 
ATOM   2614 C CB  . TYR   A 1 349 ? 28.766  17.308  -17.512 1.00 21.80  ? 886  TYR   A CB  1 
ATOM   2615 C CG  . TYR   A 1 349 ? 29.414  16.689  -18.742 1.00 21.64  ? 886  TYR   A CG  1 
ATOM   2616 C CD1 . TYR   A 1 349 ? 29.646  15.318  -18.810 1.00 23.50  ? 886  TYR   A CD1 1 
ATOM   2617 C CD2 . TYR   A 1 349 ? 29.770  17.474  -19.840 1.00 21.57  ? 886  TYR   A CD2 1 
ATOM   2618 C CE1 . TYR   A 1 349 ? 30.237  14.743  -19.925 1.00 26.17  ? 886  TYR   A CE1 1 
ATOM   2619 C CE2 . TYR   A 1 349 ? 30.349  16.899  -20.972 1.00 29.11  ? 886  TYR   A CE2 1 
ATOM   2620 C CZ  . TYR   A 1 349 ? 30.584  15.535  -20.995 1.00 29.26  ? 886  TYR   A CZ  1 
ATOM   2621 O OH  . TYR   A 1 349 ? 31.167  14.952  -22.100 1.00 31.76  ? 886  TYR   A OH  1 
ATOM   2622 N N   . ARG   A 1 350 ? 30.402  19.934  -16.555 1.00 24.33  ? 887  ARG   A N   1 
ATOM   2623 C CA  . ARG   A 1 350 ? 31.269  21.025  -16.993 1.00 24.29  ? 887  ARG   A CA  1 
ATOM   2624 C C   . ARG   A 1 350 ? 32.482  21.273  -16.089 1.00 29.72  ? 887  ARG   A C   1 
ATOM   2625 O O   . ARG   A 1 350 ? 33.317  22.128  -16.395 1.00 26.96  ? 887  ARG   A O   1 
ATOM   2626 C CB  . ARG   A 1 350 ? 30.465  22.325  -17.133 1.00 23.44  ? 887  ARG   A CB  1 
ATOM   2627 C CG  . ARG   A 1 350 ? 29.845  22.864  -15.848 1.00 20.49  ? 887  ARG   A CG  1 
ATOM   2628 C CD  . ARG   A 1 350 ? 29.267  24.261  -16.089 1.00 23.87  ? 887  ARG   A CD  1 
ATOM   2629 N NE  . ARG   A 1 350 ? 30.303  25.177  -16.542 1.00 24.26  ? 887  ARG   A NE  1 
ATOM   2630 C CZ  . ARG   A 1 350 ? 31.193  25.766  -15.741 1.00 24.26  ? 887  ARG   A CZ  1 
ATOM   2631 N NH1 . ARG   A 1 350 ? 32.105  26.575  -16.267 1.00 28.87  ? 887  ARG   A NH1 1 
ATOM   2632 N NH2 . ARG   A 1 350 ? 31.180  25.567  -14.421 1.00 21.81  ? 887  ARG   A NH2 1 
ATOM   2633 N N   . LEU   A 1 351 ? 32.596  20.533  -14.992 1.00 22.06  ? 888  LEU   A N   1 
ATOM   2634 C CA  . LEU   A 1 351 ? 33.681  20.768  -14.033 1.00 21.19  ? 888  LEU   A CA  1 
ATOM   2635 C C   . LEU   A 1 351 ? 34.957  20.015  -14.435 1.00 24.92  ? 888  LEU   A C   1 
ATOM   2636 O O   . LEU   A 1 351 ? 35.424  19.101  -13.734 1.00 23.25  ? 888  LEU   A O   1 
ATOM   2637 C CB  . LEU   A 1 351 ? 33.240  20.358  -12.618 1.00 21.60  ? 888  LEU   A CB  1 
ATOM   2638 C CG  . LEU   A 1 351 ? 32.053  21.141  -12.043 1.00 23.88  ? 888  LEU   A CG  1 
ATOM   2639 C CD1 . LEU   A 1 351 ? 31.596  20.536  -10.736 1.00 25.63  ? 888  LEU   A CD1 1 
ATOM   2640 C CD2 . LEU   A 1 351 ? 32.411  22.612  -11.827 1.00 23.21  ? 888  LEU   A CD2 1 
ATOM   2641 N N   . ASP   A 1 352 ? 35.534  20.406  -15.565 1.00 25.92  ? 889  ASP   A N   1 
ATOM   2642 C CA  . ASP   A 1 352 ? 36.668  19.667  -16.120 1.00 26.09  ? 889  ASP   A CA  1 
ATOM   2643 C C   . ASP   A 1 352 ? 37.865  19.582  -15.176 1.00 25.80  ? 889  ASP   A C   1 
ATOM   2644 O O   . ASP   A 1 352 ? 38.555  18.571  -15.152 1.00 30.14  ? 889  ASP   A O   1 
ATOM   2645 C CB  . ASP   A 1 352 ? 37.123  20.289  -17.436 1.00 25.70  ? 889  ASP   A CB  1 
ATOM   2646 C CG  . ASP   A 1 352 ? 36.115  20.092  -18.564 1.00 40.66  ? 889  ASP   A CG  1 
ATOM   2647 O OD1 . ASP   A 1 352 ? 35.190  19.268  -18.416 1.00 44.06  ? 889  ASP   A OD1 1 
ATOM   2648 O OD2 . ASP   A 1 352 ? 36.265  20.757  -19.606 1.00 50.20  ? 889  ASP   A OD2 1 
ATOM   2649 N N   . HIS   A 1 353 ? 38.110  20.630  -14.397 1.00 25.11  ? 890  HIS   A N   1 
ATOM   2650 C CA  . HIS   A 1 353 ? 39.263  20.616  -13.494 1.00 28.23  ? 890  HIS   A CA  1 
ATOM   2651 C C   . HIS   A 1 353 ? 39.106  19.548  -12.407 1.00 31.61  ? 890  HIS   A C   1 
ATOM   2652 O O   . HIS   A 1 353 ? 40.081  18.936  -11.976 1.00 28.47  ? 890  HIS   A O   1 
ATOM   2653 C CB  . HIS   A 1 353 ? 39.466  21.987  -12.853 1.00 29.66  ? 890  HIS   A CB  1 
ATOM   2654 C CG  . HIS   A 1 353 ? 39.794  23.064  -13.833 1.00 33.42  ? 890  HIS   A CG  1 
ATOM   2655 N ND1 . HIS   A 1 353 ? 41.009  23.133  -14.482 1.00 39.55  ? 890  HIS   A ND1 1 
ATOM   2656 C CD2 . HIS   A 1 353 ? 39.072  24.121  -14.271 1.00 37.48  ? 890  HIS   A CD2 1 
ATOM   2657 C CE1 . HIS   A 1 353 ? 41.018  24.184  -15.281 1.00 37.45  ? 890  HIS   A CE1 1 
ATOM   2658 N NE2 . HIS   A 1 353 ? 39.856  24.802  -15.172 1.00 39.85  ? 890  HIS   A NE2 1 
ATOM   2659 N N   . THR   A 1 354 ? 37.872  19.335  -11.967 1.00 27.50  ? 891  THR   A N   1 
ATOM   2660 C CA  . THR   A 1 354 ? 37.591  18.361  -10.925 1.00 24.63  ? 891  THR   A CA  1 
ATOM   2661 C C   . THR   A 1 354 ? 37.800  16.945  -11.434 1.00 26.69  ? 891  THR   A C   1 
ATOM   2662 O O   . THR   A 1 354 ? 38.405  16.119  -10.761 1.00 27.15  ? 891  THR   A O   1 
ATOM   2663 C CB  . THR   A 1 354 ? 36.149  18.521  -10.394 1.00 22.69  ? 891  THR   A CB  1 
ATOM   2664 O OG1 . THR   A 1 354 ? 35.986  19.856  -9.906  1.00 26.40  ? 891  THR   A OG1 1 
ATOM   2665 C CG2 . THR   A 1 354 ? 35.874  17.507  -9.247  1.00 26.58  ? 891  THR   A CG2 1 
ATOM   2666 N N   . PHE   A 1 355 ? 37.299  16.660  -12.630 1.00 27.14  ? 892  PHE   A N   1 
ATOM   2667 C CA  . PHE   A 1 355 ? 37.481  15.338  -13.218 1.00 29.00  ? 892  PHE   A CA  1 
ATOM   2668 C C   . PHE   A 1 355 ? 38.956  15.061  -13.526 1.00 29.73  ? 892  PHE   A C   1 
ATOM   2669 O O   . PHE   A 1 355 ? 39.429  13.936  -13.355 1.00 33.08  ? 892  PHE   A O   1 
ATOM   2670 C CB  . PHE   A 1 355 ? 36.640  15.193  -14.484 1.00 27.62  ? 892  PHE   A CB  1 
ATOM   2671 C CG  . PHE   A 1 355 ? 35.168  14.985  -14.204 1.00 27.08  ? 892  PHE   A CG  1 
ATOM   2672 C CD1 . PHE   A 1 355 ? 34.678  13.719  -13.944 1.00 26.94  ? 892  PHE   A CD1 1 
ATOM   2673 C CD2 . PHE   A 1 355 ? 34.296  16.060  -14.162 1.00 34.31  ? 892  PHE   A CD2 1 
ATOM   2674 C CE1 . PHE   A 1 355 ? 33.332  13.513  -13.669 1.00 26.82  ? 892  PHE   A CE1 1 
ATOM   2675 C CE2 . PHE   A 1 355 ? 32.946  15.871  -13.892 1.00 26.71  ? 892  PHE   A CE2 1 
ATOM   2676 C CZ  . PHE   A 1 355 ? 32.464  14.588  -13.640 1.00 29.27  ? 892  PHE   A CZ  1 
ATOM   2677 N N   . GLU   A 1 356 ? 39.677  16.080  -13.969 1.00 29.54  ? 893  GLU   A N   1 
ATOM   2678 C CA  . GLU   A 1 356 ? 41.089  15.892  -14.312 1.00 27.71  ? 893  GLU   A CA  1 
ATOM   2679 C C   . GLU   A 1 356 ? 41.928  15.527  -13.082 1.00 33.67  ? 893  GLU   A C   1 
ATOM   2680 O O   . GLU   A 1 356 ? 42.945  14.837  -13.195 1.00 32.80  ? 893  GLU   A O   1 
ATOM   2681 C CB  . GLU   A 1 356 ? 41.647  17.150  -14.982 1.00 33.06  ? 893  GLU   A CB  1 
ATOM   2682 C CG  . GLU   A 1 356 ? 43.075  16.985  -15.510 1.00 52.50  ? 893  GLU   A CG  1 
ATOM   2683 C CD  . GLU   A 1 356 ? 43.207  15.841  -16.509 1.00 69.45  ? 893  GLU   A CD  1 
ATOM   2684 O OE1 . GLU   A 1 356 ? 42.257  15.610  -17.290 1.00 62.23  ? 893  GLU   A OE1 1 
ATOM   2685 O OE2 . GLU   A 1 356 ? 44.263  15.170  -16.511 1.00 79.52  ? 893  GLU   A OE2 1 
ATOM   2686 N N   . ALA   A 1 357 ? 41.489  15.964  -11.907 1.00 27.93  ? 894  ALA   A N   1 
ATOM   2687 C CA  . ALA   A 1 357 ? 42.251  15.740  -10.673 1.00 33.39  ? 894  ALA   A CA  1 
ATOM   2688 C C   . ALA   A 1 357 ? 41.980  14.387  -10.010 1.00 35.14  ? 894  ALA   A C   1 
ATOM   2689 O O   . ALA   A 1 357 ? 42.672  14.016  -9.052  1.00 33.95  ? 894  ALA   A O   1 
ATOM   2690 C CB  . ALA   A 1 357 ? 41.981  16.868  -9.676  1.00 35.08  ? 894  ALA   A CB  1 
ATOM   2691 N N   . LEU   A 1 358 ? 40.988  13.649  -10.508 1.00 30.19  ? 895  LEU   A N   1 
ATOM   2692 C CA  . LEU   A 1 358 ? 40.698  12.304  -10.006 1.00 34.37  ? 895  LEU   A CA  1 
ATOM   2693 C C   . LEU   A 1 358 ? 41.884  11.389  -10.228 1.00 39.15  ? 895  LEU   A C   1 
ATOM   2694 O O   . LEU   A 1 358 ? 42.540  11.490  -11.263 1.00 34.70  ? 895  LEU   A O   1 
ATOM   2695 C CB  . LEU   A 1 358 ? 39.486  11.696  -10.717 1.00 28.23  ? 895  LEU   A CB  1 
ATOM   2696 C CG  . LEU   A 1 358 ? 38.087  12.224  -10.475 1.00 30.49  ? 895  LEU   A CG  1 
ATOM   2697 C CD1 . LEU   A 1 358 ? 37.158  11.470  -11.414 1.00 29.21  ? 895  LEU   A CD1 1 
ATOM   2698 C CD2 . LEU   A 1 358 ? 37.703  11.991  -9.020  1.00 31.28  ? 895  LEU   A CD2 1 
ATOM   2699 N N   . GLN   A 1 359 ? 42.145  10.476  -9.299  1.00 34.43  ? 896  GLN   A N   1 
ATOM   2700 C CA  . GLN   A 1 359 ? 43.187  9.491   -9.556  1.00 42.29  ? 896  GLN   A CA  1 
ATOM   2701 C C   . GLN   A 1 359 ? 42.723  8.595   -10.709 1.00 43.40  ? 896  GLN   A C   1 
ATOM   2702 O O   . GLN   A 1 359 ? 41.525  8.340   -10.874 1.00 35.02  ? 896  GLN   A O   1 
ATOM   2703 C CB  . GLN   A 1 359 ? 43.544  8.697   -8.291  1.00 49.70  ? 896  GLN   A CB  1 
ATOM   2704 C CG  . GLN   A 1 359 ? 42.646  7.538   -7.944  1.00 62.39  ? 896  GLN   A CG  1 
ATOM   2705 C CD  . GLN   A 1 359 ? 43.142  6.791   -6.715  1.00 71.48  ? 896  GLN   A CD  1 
ATOM   2706 O OE1 . GLN   A 1 359 ? 43.961  7.307   -5.954  1.00 76.38  ? 896  GLN   A OE1 1 
ATOM   2707 N NE2 . GLN   A 1 359 ? 42.654  5.569   -6.521  1.00 67.66  ? 896  GLN   A NE2 1 
ATOM   2708 N N   A GLU   A 1 360 ? 43.683  8.151   -11.515 0.49 42.50  ? 897  GLU   A N   1 
ATOM   2709 N N   B GLU   A 1 360 ? 43.683  8.135   -11.506 0.51 42.36  ? 897  GLU   A N   1 
ATOM   2710 C CA  A GLU   A 1 360 ? 43.413  7.421   -12.752 0.49 45.98  ? 897  GLU   A CA  1 
ATOM   2711 C CA  B GLU   A 1 360 ? 43.404  7.428   -12.755 0.51 45.95  ? 897  GLU   A CA  1 
ATOM   2712 C C   A GLU   A 1 360 ? 42.537  6.187   -12.553 0.49 42.79  ? 897  GLU   A C   1 
ATOM   2713 C C   B GLU   A 1 360 ? 42.553  6.172   -12.566 0.51 42.83  ? 897  GLU   A C   1 
ATOM   2714 O O   A GLU   A 1 360 ? 41.675  5.889   -13.379 0.49 41.57  ? 897  GLU   A O   1 
ATOM   2715 O O   B GLU   A 1 360 ? 41.726  5.844   -13.415 0.51 41.39  ? 897  GLU   A O   1 
ATOM   2716 C CB  A GLU   A 1 360 ? 44.737  7.011   -13.411 0.49 48.73  ? 897  GLU   A CB  1 
ATOM   2717 C CB  B GLU   A 1 360 ? 44.723  7.063   -13.448 0.51 48.73  ? 897  GLU   A CB  1 
ATOM   2718 C CG  A GLU   A 1 360 ? 44.602  5.987   -14.532 0.49 54.27  ? 897  GLU   A CG  1 
ATOM   2719 C CG  B GLU   A 1 360 ? 44.561  6.491   -14.849 0.51 56.06  ? 897  GLU   A CG  1 
ATOM   2720 C CD  A GLU   A 1 360 ? 43.962  6.558   -15.785 0.49 60.72  ? 897  GLU   A CD  1 
ATOM   2721 C CD  B GLU   A 1 360 ? 45.892  6.213   -15.526 0.51 66.06  ? 897  GLU   A CD  1 
ATOM   2722 O OE1 A GLU   A 1 360 ? 43.971  7.796   -15.952 0.49 61.22  ? 897  GLU   A OE1 1 
ATOM   2723 O OE1 B GLU   A 1 360 ? 46.938  6.598   -14.963 0.51 61.18  ? 897  GLU   A OE1 1 
ATOM   2724 O OE2 A GLU   A 1 360 ? 43.451  5.769   -16.606 0.49 68.51  ? 897  GLU   A OE2 1 
ATOM   2725 O OE2 B GLU   A 1 360 ? 45.892  5.610   -16.622 0.51 75.74  ? 897  GLU   A OE2 1 
ATOM   2726 N N   . ARG   A 1 361 ? 42.756  5.471   -11.456 1.00 38.93  ? 898  ARG   A N   1 
ATOM   2727 C CA  . ARG   A 1 361 ? 42.005  4.252   -11.192 1.00 42.23  ? 898  ARG   A CA  1 
ATOM   2728 C C   . ARG   A 1 361 ? 40.515  4.543   -10.952 1.00 41.72  ? 898  ARG   A C   1 
ATOM   2729 O O   . ARG   A 1 361 ? 39.640  3.809   -11.423 1.00 39.29  ? 898  ARG   A O   1 
ATOM   2730 C CB  . ARG   A 1 361 ? 42.604  3.503   -9.998  1.00 51.58  ? 898  ARG   A CB  1 
ATOM   2731 C CG  . ARG   A 1 361 ? 41.847  2.244   -9.652  1.00 59.15  ? 898  ARG   A CG  1 
ATOM   2732 C CD  . ARG   A 1 361 ? 42.538  1.377   -8.601  1.00 58.11  ? 898  ARG   A CD  1 
ATOM   2733 N NE  . ARG   A 1 361 ? 41.555  0.739   -7.722  1.00 60.50  ? 898  ARG   A NE  1 
ATOM   2734 C CZ  . ARG   A 1 361 ? 40.655  -0.163  -8.114  1.00 61.83  ? 898  ARG   A CZ  1 
ATOM   2735 N NH1 . ARG   A 1 361 ? 40.599  -0.562  -9.382  1.00 64.12  ? 898  ARG   A NH1 1 
ATOM   2736 N NH2 . ARG   A 1 361 ? 39.801  -0.674  -7.232  1.00 58.65  ? 898  ARG   A NH2 1 
ATOM   2737 N N   . LYS   A 1 362 ? 40.228  5.618   -10.230 1.00 40.95  ? 899  LYS   A N   1 
ATOM   2738 C CA  . LYS   A 1 362 ? 38.841  5.976   -9.959  1.00 39.51  ? 899  LYS   A CA  1 
ATOM   2739 C C   . LYS   A 1 362 ? 38.198  6.530   -11.219 1.00 40.18  ? 899  LYS   A C   1 
ATOM   2740 O O   . LYS   A 1 362 ? 37.009  6.311   -11.475 1.00 36.10  ? 899  LYS   A O   1 
ATOM   2741 C CB  . LYS   A 1 362 ? 38.749  6.980   -8.813  1.00 43.95  ? 899  LYS   A CB  1 
ATOM   2742 C CG  . LYS   A 1 362 ? 39.114  6.372   -7.469  1.00 47.52  ? 899  LYS   A CG  1 
ATOM   2743 C CD  . LYS   A 1 362 ? 38.358  7.024   -6.330  1.00 50.98  ? 899  LYS   A CD  1 
ATOM   2744 C CE  . LYS   A 1 362 ? 38.662  6.326   -5.021  1.00 55.65  ? 899  LYS   A CE  1 
ATOM   2745 N NZ  . LYS   A 1 362 ? 40.103  6.435   -4.671  1.00 64.38  ? 899  LYS   A NZ  1 
ATOM   2746 N N   . ARG   A 1 363 ? 38.987  7.232   -12.023 1.00 35.46  ? 900  ARG   A N   1 
ATOM   2747 C CA  . ARG   A 1 363 ? 38.474  7.747   -13.282 1.00 33.23  ? 900  ARG   A CA  1 
ATOM   2748 C C   . ARG   A 1 363 ? 38.057  6.604   -14.199 1.00 38.20  ? 900  ARG   A C   1 
ATOM   2749 O O   . ARG   A 1 363 ? 37.002  6.654   -14.833 1.00 34.26  ? 900  ARG   A O   1 
ATOM   2750 C CB  . ARG   A 1 363 ? 39.512  8.619   -13.968 1.00 42.89  ? 900  ARG   A CB  1 
ATOM   2751 C CG  . ARG   A 1 363 ? 38.912  9.661   -14.864 1.00 51.89  ? 900  ARG   A CG  1 
ATOM   2752 C CD  . ARG   A 1 363 ? 39.857  10.819  -14.982 1.00 57.41  ? 900  ARG   A CD  1 
ATOM   2753 N NE  . ARG   A 1 363 ? 41.163  10.395  -15.475 1.00 54.90  ? 900  ARG   A NE  1 
ATOM   2754 C CZ  . ARG   A 1 363 ? 42.285  11.054  -15.221 1.00 63.61  ? 900  ARG   A CZ  1 
ATOM   2755 N NH1 . ARG   A 1 363 ? 42.240  12.147  -14.467 1.00 63.05  ? 900  ARG   A NH1 1 
ATOM   2756 N NH2 . ARG   A 1 363 ? 43.441  10.619  -15.707 1.00 54.21  ? 900  ARG   A NH2 1 
ATOM   2757 N N   . LYS   A 1 364 ? 38.879  5.563   -14.251 1.00 32.81  ? 901  LYS   A N   1 
ATOM   2758 C CA  . LYS   A 1 364 ? 38.575  4.403   -15.076 1.00 33.55  ? 901  LYS   A CA  1 
ATOM   2759 C C   . LYS   A 1 364 ? 37.308  3.728   -14.594 1.00 35.11  ? 901  LYS   A C   1 
ATOM   2760 O O   . LYS   A 1 364 ? 36.490  3.274   -15.397 1.00 34.55  ? 901  LYS   A O   1 
ATOM   2761 C CB  . LYS   A 1 364 ? 39.740  3.405   -15.065 1.00 42.05  ? 901  LYS   A CB  1 
ATOM   2762 C CG  . LYS   A 1 364 ? 40.855  3.741   -16.048 1.00 53.32  ? 901  LYS   A CG  1 
ATOM   2763 C CD  . LYS   A 1 364 ? 41.964  2.708   -15.967 1.00 61.35  ? 901  LYS   A CD  1 
ATOM   2764 C CE  . LYS   A 1 364 ? 42.862  2.729   -17.193 1.00 64.26  ? 901  LYS   A CE  1 
ATOM   2765 N NZ  . LYS   A 1 364 ? 43.930  1.707   -17.079 1.00 63.84  ? 901  LYS   A NZ  1 
ATOM   2766 N N   . ILE   A 1 365 ? 37.136  3.677   -13.278 1.00 30.44  ? 902  ILE   A N   1 
ATOM   2767 C CA  . ILE   A 1 365 ? 35.971  3.003   -12.720 1.00 28.21  ? 902  ILE   A CA  1 
ATOM   2768 C C   . ILE   A 1 365 ? 34.725  3.772   -13.109 1.00 30.97  ? 902  ILE   A C   1 
ATOM   2769 O O   . ILE   A 1 365 ? 33.747  3.186   -13.568 1.00 28.48  ? 902  ILE   A O   1 
ATOM   2770 C CB  . ILE   A 1 365 ? 36.074  2.856   -11.198 1.00 32.35  ? 902  ILE   A CB  1 
ATOM   2771 C CG1 . ILE   A 1 365 ? 37.079  1.745   -10.892 1.00 41.40  ? 902  ILE   A CG1 1 
ATOM   2772 C CG2 . ILE   A 1 365 ? 34.711  2.542   -10.605 1.00 33.78  ? 902  ILE   A CG2 1 
ATOM   2773 C CD1 . ILE   A 1 365 ? 37.519  1.673   -9.461  1.00 47.66  ? 902  ILE   A CD1 1 
ATOM   2774 N N   . LEU   A 1 366 ? 34.781  5.093   -12.971 1.00 29.43  ? 903  LEU   A N   1 
ATOM   2775 C CA  . LEU   A 1 366 ? 33.651  5.940   -13.347 1.00 29.37  ? 903  LEU   A CA  1 
ATOM   2776 C C   . LEU   A 1 366 ? 33.339  5.827   -14.834 1.00 28.24  ? 903  LEU   A C   1 
ATOM   2777 O O   . LEU   A 1 366 ? 32.182  5.741   -15.226 1.00 26.52  ? 903  LEU   A O   1 
ATOM   2778 C CB  . LEU   A 1 366 ? 33.923  7.402   -12.991 1.00 27.30  ? 903  LEU   A CB  1 
ATOM   2779 C CG  . LEU   A 1 366 ? 32.780  8.346   -13.384 1.00 29.21  ? 903  LEU   A CG  1 
ATOM   2780 C CD1 . LEU   A 1 366 ? 31.465  7.901   -12.773 1.00 31.22  ? 903  LEU   A CD1 1 
ATOM   2781 C CD2 . LEU   A 1 366 ? 33.095  9.761   -12.951 1.00 33.61  ? 903  LEU   A CD2 1 
ATOM   2782 N N   . ASP   A 1 367 ? 34.370  5.813   -15.671 1.00 27.75  ? 904  ASP   A N   1 
ATOM   2783 C CA  . ASP   A 1 367 ? 34.110  5.784   -17.106 1.00 31.05  ? 904  ASP   A CA  1 
ATOM   2784 C C   . ASP   A 1 367 ? 33.559  4.442   -17.572 1.00 34.37  ? 904  ASP   A C   1 
ATOM   2785 O O   . ASP   A 1 367 ? 32.726  4.400   -18.472 1.00 32.20  ? 904  ASP   A O   1 
ATOM   2786 C CB  . ASP   A 1 367 ? 35.372  6.160   -17.878 1.00 33.73  ? 904  ASP   A CB  1 
ATOM   2787 C CG  . ASP   A 1 367 ? 35.634  7.643   -17.833 1.00 34.09  ? 904  ASP   A CG  1 
ATOM   2788 O OD1 . ASP   A 1 367 ? 34.679  8.365   -17.479 1.00 38.06  ? 904  ASP   A OD1 1 
ATOM   2789 O OD2 . ASP   A 1 367 ? 36.761  8.095   -18.129 1.00 30.90  ? 904  ASP   A OD2 1 
ATOM   2790 N N   . GLU   A 1 368 ? 33.981  3.347   -16.948 1.00 30.26  ? 905  GLU   A N   1 
ATOM   2791 C CA  . GLU   A 1 368 ? 33.376  2.067   -17.303 1.00 33.48  ? 905  GLU   A CA  1 
ATOM   2792 C C   . GLU   A 1 368 ? 31.877  2.048   -16.961 1.00 35.97  ? 905  GLU   A C   1 
ATOM   2793 O O   . GLU   A 1 368 ? 31.070  1.461   -17.690 1.00 33.49  ? 905  GLU   A O   1 
ATOM   2794 C CB  . GLU   A 1 368 ? 34.096  0.908   -16.613 1.00 41.35  ? 905  GLU   A CB  1 
ATOM   2795 C CG  . GLU   A 1 368 ? 33.477  -0.442  -16.932 1.00 48.72  ? 905  GLU   A CG  1 
ATOM   2796 C CD  . GLU   A 1 368 ? 34.447  -1.594  -16.763 1.00 57.58  ? 905  GLU   A CD  1 
ATOM   2797 O OE1 . GLU   A 1 368 ? 35.333  -1.506  -15.885 1.00 54.37  ? 905  GLU   A OE1 1 
ATOM   2798 O OE2 . GLU   A 1 368 ? 34.322  -2.583  -17.519 1.00 64.76  ? 905  GLU   A OE2 1 
ATOM   2799 N N   . ALA   A 1 369 ? 31.497  2.706   -15.870 1.00 32.61  ? 906  ALA   A N   1 
ATOM   2800 C CA  . ALA   A 1 369 ? 30.091  2.744   -15.493 1.00 30.70  ? 906  ALA   A CA  1 
ATOM   2801 C C   . ALA   A 1 369 ? 29.306  3.617   -16.459 1.00 28.37  ? 906  ALA   A C   1 
ATOM   2802 O O   . ALA   A 1 369 ? 28.203  3.261   -16.858 1.00 27.88  ? 906  ALA   A O   1 
ATOM   2803 C CB  . ALA   A 1 369 ? 29.918  3.243   -14.064 1.00 29.56  ? 906  ALA   A CB  1 
ATOM   2804 N N   . VAL   A 1 370 ? 29.873  4.759   -16.834 1.00 27.08  ? 907  VAL   A N   1 
ATOM   2805 C CA  . VAL   A 1 370 ? 29.190  5.660   -17.752 1.00 27.77  ? 907  VAL   A CA  1 
ATOM   2806 C C   . VAL   A 1 370 ? 28.957  4.928   -19.071 1.00 29.64  ? 907  VAL   A C   1 
ATOM   2807 O O   . VAL   A 1 370 ? 27.932  5.100   -19.717 1.00 29.94  ? 907  VAL   A O   1 
ATOM   2808 C CB  . VAL   A 1 370 ? 29.992  6.958   -17.987 1.00 29.76  ? 907  VAL   A CB  1 
ATOM   2809 C CG1 . VAL   A 1 370 ? 29.410  7.759   -19.139 1.00 34.96  ? 907  VAL   A CG1 1 
ATOM   2810 C CG2 . VAL   A 1 370 ? 29.988  7.807   -16.719 1.00 31.42  ? 907  VAL   A CG2 1 
ATOM   2811 N N   . GLU   A 1 371 ? 29.898  4.075   -19.438 1.00 31.12  ? 908  GLU   A N   1 
ATOM   2812 C CA  . GLU   A 1 371 ? 29.797  3.356   -20.700 1.00 32.14  ? 908  GLU   A CA  1 
ATOM   2813 C C   . GLU   A 1 371 ? 28.648  2.360   -20.715 1.00 36.91  ? 908  GLU   A C   1 
ATOM   2814 O O   . GLU   A 1 371 ? 28.115  2.051   -21.790 1.00 34.48  ? 908  GLU   A O   1 
ATOM   2815 C CB  . GLU   A 1 371 ? 31.122  2.669   -21.012 1.00 33.01  ? 908  GLU   A CB  1 
ATOM   2816 C CG  . GLU   A 1 371 ? 32.100  3.635   -21.654 1.00 46.80  ? 908  GLU   A CG  1 
ATOM   2817 C CD  . GLU   A 1 371 ? 33.554  3.231   -21.474 1.00 56.59  ? 908  GLU   A CD  1 
ATOM   2818 O OE1 . GLU   A 1 371 ? 34.427  4.117   -21.615 1.00 52.11  ? 908  GLU   A OE1 1 
ATOM   2819 O OE2 . GLU   A 1 371 ? 33.821  2.038   -21.198 1.00 52.31  ? 908  GLU   A OE2 1 
ATOM   2820 N N   . LEU   A 1 372 ? 28.232  1.888   -19.537 1.00 29.74  ? 909  LEU   A N   1 
ATOM   2821 C CA  . LEU   A 1 372 ? 27.046  1.028   -19.448 1.00 28.67  ? 909  LEU   A CA  1 
ATOM   2822 C C   . LEU   A 1 372 ? 25.823  1.669   -20.089 1.00 32.75  ? 909  LEU   A C   1 
ATOM   2823 O O   . LEU   A 1 372 ? 24.959  0.975   -20.609 1.00 32.07  ? 909  LEU   A O   1 
ATOM   2824 C CB  . LEU   A 1 372 ? 26.711  0.689   -17.989 1.00 30.27  ? 909  LEU   A CB  1 
ATOM   2825 C CG  . LEU   A 1 372 ? 27.638  -0.253  -17.232 1.00 32.93  ? 909  LEU   A CG  1 
ATOM   2826 C CD1 . LEU   A 1 372 ? 27.202  -0.315  -15.776 1.00 39.80  ? 909  LEU   A CD1 1 
ATOM   2827 C CD2 . LEU   A 1 372 ? 27.627  -1.651  -17.846 1.00 33.52  ? 909  LEU   A CD2 1 
ATOM   2828 N N   . SER   A 1 373 ? 25.749  2.996   -20.044 1.00 30.63  ? 910  SER   A N   1 
ATOM   2829 C CA  . SER   A 1 373 ? 24.551  3.691   -20.492 1.00 29.77  ? 910  SER   A CA  1 
ATOM   2830 C C   . SER   A 1 373 ? 24.598  4.061   -21.970 1.00 34.88  ? 910  SER   A C   1 
ATOM   2831 O O   . SER   A 1 373 ? 23.571  4.403   -22.554 1.00 33.50  ? 910  SER   A O   1 
ATOM   2832 C CB  . SER   A 1 373 ? 24.330  4.958   -19.658 1.00 32.25  ? 910  SER   A CB  1 
ATOM   2833 O OG  . SER   A 1 373 ? 25.399  5.878   -19.834 1.00 33.11  ? 910  SER   A OG  1 
ATOM   2834 N N   . GLN   A 1 374 ? 25.783  3.987   -22.571 1.00 34.28  ? 911  GLN   A N   1 
ATOM   2835 C CA  . GLN   A 1 374 ? 25.960  4.433   -23.952 1.00 41.38  ? 911  GLN   A CA  1 
ATOM   2836 C C   . GLN   A 1 374 ? 25.261  3.512   -24.954 1.00 47.94  ? 911  GLN   A C   1 
ATOM   2837 O O   . GLN   A 1 374 ? 25.011  2.332   -24.660 1.00 37.87  ? 911  GLN   A O   1 
ATOM   2838 C CB  . GLN   A 1 374 ? 27.451  4.556   -24.274 1.00 40.27  ? 911  GLN   A CB  1 
ATOM   2839 C CG  . GLN   A 1 374 ? 28.073  5.822   -23.681 1.00 40.20  ? 911  GLN   A CG  1 
ATOM   2840 C CD  . GLN   A 1 374 ? 29.584  5.778   -23.601 1.00 44.89  ? 911  GLN   A CD  1 
ATOM   2841 O OE1 . GLN   A 1 374 ? 30.228  4.868   -24.132 1.00 38.99  ? 911  GLN   A OE1 1 
ATOM   2842 N NE2 . GLN   A 1 374 ? 30.161  6.759   -22.918 1.00 43.52  ? 911  GLN   A NE2 1 
ATOM   2843 N N   A ASP   A 1 375 ? 24.937  4.074   -26.118 0.53 47.44  ? 912  ASP   A N   1 
ATOM   2844 N N   B ASP   A 1 375 ? 24.955  4.055   -26.133 0.47 47.48  ? 912  ASP   A N   1 
ATOM   2845 C CA  A ASP   A 1 375 ? 24.289  3.341   -27.201 0.53 48.35  ? 912  ASP   A CA  1 
ATOM   2846 C CA  B ASP   A 1 375 ? 24.288  3.312   -27.205 0.47 49.21  ? 912  ASP   A CA  1 
ATOM   2847 C C   A ASP   A 1 375 ? 23.011  2.659   -26.715 0.53 43.50  ? 912  ASP   A C   1 
ATOM   2848 C C   B ASP   A 1 375 ? 23.006  2.649   -26.708 0.47 43.55  ? 912  ASP   A C   1 
ATOM   2849 O O   A ASP   A 1 375 ? 22.848  1.446   -26.851 0.53 41.85  ? 912  ASP   A O   1 
ATOM   2850 O O   B ASP   A 1 375 ? 22.834  1.435   -26.829 0.47 41.61  ? 912  ASP   A O   1 
ATOM   2851 C CB  A ASP   A 1 375 ? 25.261  2.321   -27.800 0.53 54.82  ? 912  ASP   A CB  1 
ATOM   2852 C CB  B ASP   A 1 375 ? 25.235  2.265   -27.805 0.47 56.25  ? 912  ASP   A CB  1 
ATOM   2853 C CG  A ASP   A 1 375 ? 26.590  2.948   -28.192 0.53 59.50  ? 912  ASP   A CG  1 
ATOM   2854 C CG  B ASP   A 1 375 ? 24.740  1.714   -29.133 0.47 61.33  ? 912  ASP   A CG  1 
ATOM   2855 O OD1 A ASP   A 1 375 ? 26.578  4.056   -28.768 0.53 64.03  ? 912  ASP   A OD1 1 
ATOM   2856 O OD1 B ASP   A 1 375 ? 23.805  2.303   -29.717 0.47 64.27  ? 912  ASP   A OD1 1 
ATOM   2857 O OD2 A ASP   A 1 375 ? 27.646  2.347   -27.911 0.53 55.46  ? 912  ASP   A OD2 1 
ATOM   2858 O OD2 B ASP   A 1 375 ? 25.294  0.695   -29.595 0.47 60.88  ? 912  ASP   A OD2 1 
ATOM   2859 N N   . HIS   A 1 376 ? 22.120  3.461   -26.138 1.00 39.47  ? 913  HIS   A N   1 
ATOM   2860 C CA  . HIS   A 1 376 ? 20.852  2.986   -25.586 1.00 42.72  ? 913  HIS   A CA  1 
ATOM   2861 C C   . HIS   A 1 376 ? 21.042  1.834   -24.591 1.00 42.10  ? 913  HIS   A C   1 
ATOM   2862 O O   . HIS   A 1 376 ? 20.393  0.789   -24.688 1.00 42.58  ? 913  HIS   A O   1 
ATOM   2863 C CB  . HIS   A 1 376 ? 19.904  2.594   -26.723 1.00 50.55  ? 913  HIS   A CB  1 
ATOM   2864 C CG  . HIS   A 1 376 ? 19.629  3.717   -27.677 1.00 56.88  ? 913  HIS   A CG  1 
ATOM   2865 N ND1 . HIS   A 1 376 ? 19.197  4.958   -27.257 1.00 58.49  ? 913  HIS   A ND1 1 
ATOM   2866 C CD2 . HIS   A 1 376 ? 19.744  3.794   -29.023 1.00 56.66  ? 913  HIS   A CD2 1 
ATOM   2867 C CE1 . HIS   A 1 376 ? 19.054  5.750   -28.305 1.00 58.65  ? 913  HIS   A CE1 1 
ATOM   2868 N NE2 . HIS   A 1 376 ? 19.377  5.068   -29.389 1.00 59.48  ? 913  HIS   A NE2 1 
ATOM   2869 N N   . PHE   A 1 377 ? 21.953  2.051   -23.640 1.00 38.19  ? 914  PHE   A N   1 
ATOM   2870 C CA  . PHE   A 1 377 ? 22.211  1.117   -22.541 1.00 38.23  ? 914  PHE   A CA  1 
ATOM   2871 C C   . PHE   A 1 377 ? 22.611  -0.279  -23.011 1.00 39.07  ? 914  PHE   A C   1 
ATOM   2872 O O   . PHE   A 1 377 ? 22.308  -1.265  -22.351 1.00 35.42  ? 914  PHE   A O   1 
ATOM   2873 C CB  . PHE   A 1 377 ? 20.981  1.033   -21.624 1.00 33.79  ? 914  PHE   A CB  1 
ATOM   2874 C CG  . PHE   A 1 377 ? 20.703  2.312   -20.893 1.00 35.24  ? 914  PHE   A CG  1 
ATOM   2875 C CD1 . PHE   A 1 377 ? 19.912  3.294   -21.463 1.00 35.17  ? 914  PHE   A CD1 1 
ATOM   2876 C CD2 . PHE   A 1 377 ? 21.270  2.551   -19.653 1.00 33.73  ? 914  PHE   A CD2 1 
ATOM   2877 C CE1 . PHE   A 1 377 ? 19.676  4.487   -20.798 1.00 42.74  ? 914  PHE   A CE1 1 
ATOM   2878 C CE2 . PHE   A 1 377 ? 21.036  3.741   -18.984 1.00 32.49  ? 914  PHE   A CE2 1 
ATOM   2879 C CZ  . PHE   A 1 377 ? 20.245  4.709   -19.554 1.00 29.80  ? 914  PHE   A CZ  1 
ATOM   2880 N N   . LYS   A 1 378 ? 23.308  -0.348  -24.142 1.00 39.83  ? 915  LYS   A N   1 
ATOM   2881 C CA  . LYS   A 1 378 ? 23.720  -1.629  -24.711 1.00 40.96  ? 915  LYS   A CA  1 
ATOM   2882 C C   . LYS   A 1 378 ? 24.494  -2.497  -23.716 1.00 37.81  ? 915  LYS   A C   1 
ATOM   2883 O O   . LYS   A 1 378 ? 24.113  -3.637  -23.461 1.00 40.08  ? 915  LYS   A O   1 
ATOM   2884 C CB  . LYS   A 1 378 ? 24.560  -1.405  -25.971 1.00 42.63  ? 915  LYS   A CB  1 
ATOM   2885 C CG  . LYS   A 1 378 ? 24.929  -2.695  -26.707 1.00 51.37  ? 915  LYS   A CG  1 
ATOM   2886 C CD  . LYS   A 1 378 ? 25.853  -2.412  -27.891 1.00 57.62  ? 915  LYS   A CD  1 
ATOM   2887 C CE  . LYS   A 1 378 ? 26.426  -3.693  -28.494 1.00 67.15  ? 915  LYS   A CE  1 
ATOM   2888 N NZ  . LYS   A 1 378 ? 25.403  -4.513  -29.206 1.00 69.96  ? 915  LYS   A NZ  1 
ATOM   2889 N N   . LYS   A 1 379 ? 25.571  -1.961  -23.149 1.00 31.26  ? 916  LYS   A N   1 
ATOM   2890 C CA  . LYS   A 1 379 ? 26.414  -2.752  -22.255 1.00 31.42  ? 916  LYS   A CA  1 
ATOM   2891 C C   . LYS   A 1 379 ? 25.736  -3.038  -20.914 1.00 33.78  ? 916  LYS   A C   1 
ATOM   2892 O O   . LYS   A 1 379 ? 26.000  -4.071  -20.293 1.00 33.75  ? 916  LYS   A O   1 
ATOM   2893 C CB  . LYS   A 1 379 ? 27.762  -2.056  -22.036 1.00 39.05  ? 916  LYS   A CB  1 
ATOM   2894 C CG  . LYS   A 1 379 ? 28.728  -2.201  -23.218 1.00 34.43  ? 916  LYS   A CG  1 
ATOM   2895 C CD  . LYS   A 1 379 ? 29.950  -1.319  -23.041 1.00 39.28  ? 916  LYS   A CD  1 
ATOM   2896 C CE  . LYS   A 1 379 ? 30.958  -1.521  -24.166 1.00 45.15  ? 916  LYS   A CE  1 
ATOM   2897 N NZ  . LYS   A 1 379 ? 32.094  -0.565  -24.021 1.00 47.59  ? 916  LYS   A NZ  1 
ATOM   2898 N N   . TYR   A 1 380 ? 24.869  -2.129  -20.464 1.00 34.63  ? 917  TYR   A N   1 
ATOM   2899 C CA  . TYR   A 1 380 ? 24.051  -2.388  -19.279 1.00 33.14  ? 917  TYR   A CA  1 
ATOM   2900 C C   . TYR   A 1 380 ? 23.151  -3.610  -19.476 1.00 34.48  ? 917  TYR   A C   1 
ATOM   2901 O O   . TYR   A 1 380 ? 23.044  -4.477  -18.595 1.00 34.22  ? 917  TYR   A O   1 
ATOM   2902 C CB  . TYR   A 1 380 ? 23.169  -1.181  -18.916 1.00 35.26  ? 917  TYR   A CB  1 
ATOM   2903 C CG  . TYR   A 1 380 ? 22.045  -1.581  -17.975 1.00 32.27  ? 917  TYR   A CG  1 
ATOM   2904 C CD1 . TYR   A 1 380 ? 22.324  -2.017  -16.682 1.00 34.06  ? 917  TYR   A CD1 1 
ATOM   2905 C CD2 . TYR   A 1 380 ? 20.717  -1.569  -18.389 1.00 32.40  ? 917  TYR   A CD2 1 
ATOM   2906 C CE1 . TYR   A 1 380 ? 21.312  -2.411  -15.821 1.00 30.82  ? 917  TYR   A CE1 1 
ATOM   2907 C CE2 . TYR   A 1 380 ? 19.685  -1.965  -17.529 1.00 29.63  ? 917  TYR   A CE2 1 
ATOM   2908 C CZ  . TYR   A 1 380 ? 19.997  -2.380  -16.244 1.00 30.73  ? 917  TYR   A CZ  1 
ATOM   2909 O OH  . TYR   A 1 380 ? 18.993  -2.770  -15.383 1.00 31.49  ? 917  TYR   A OH  1 
ATOM   2910 N N   . LEU   A 1 381 ? 22.489  -3.658  -20.626 1.00 36.86  ? 918  LEU   A N   1 
ATOM   2911 C CA  . LEU   A 1 381 ? 21.526  -4.714  -20.907 1.00 38.54  ? 918  LEU   A CA  1 
ATOM   2912 C C   . LEU   A 1 381 ? 22.172  -6.096  -20.956 1.00 49.21  ? 918  LEU   A C   1 
ATOM   2913 O O   . LEU   A 1 381 ? 21.575  -7.072  -20.504 1.00 54.81  ? 918  LEU   A O   1 
ATOM   2914 C CB  . LEU   A 1 381 ? 20.800  -4.424  -22.215 1.00 44.34  ? 918  LEU   A CB  1 
ATOM   2915 C CG  . LEU   A 1 381 ? 19.764  -3.307  -22.091 1.00 42.42  ? 918  LEU   A CG  1 
ATOM   2916 C CD1 . LEU   A 1 381 ? 19.108  -3.009  -23.437 1.00 43.27  ? 918  LEU   A CD1 1 
ATOM   2917 C CD2 . LEU   A 1 381 ? 18.723  -3.677  -21.047 1.00 42.39  ? 918  LEU   A CD2 1 
ATOM   2918 N N   . VAL   A 1 382 ? 23.387  -6.187  -21.489 1.00 41.45  ? 919  VAL   A N   1 
ATOM   2919 C CA  . VAL   A 1 382 ? 24.072  -7.474  -21.483 1.00 51.27  ? 919  VAL   A CA  1 
ATOM   2920 C C   . VAL   A 1 382 ? 24.513  -7.826  -20.060 1.00 42.63  ? 919  VAL   A C   1 
ATOM   2921 O O   . VAL   A 1 382 ? 24.505  -8.993  -19.681 1.00 39.29  ? 919  VAL   A O   1 
ATOM   2922 C CB  . VAL   A 1 382 ? 25.288  -7.511  -22.457 1.00 49.71  ? 919  VAL   A CB  1 
ATOM   2923 C CG1 . VAL   A 1 382 ? 24.908  -6.925  -23.801 1.00 50.47  ? 919  VAL   A CG1 1 
ATOM   2924 C CG2 . VAL   A 1 382 ? 26.490  -6.794  -21.889 1.00 57.41  ? 919  VAL   A CG2 1 
ATOM   2925 N N   . LYS   A 1 383 ? 24.863  -6.824  -19.258 1.00 36.69  ? 920  LYS   A N   1 
ATOM   2926 C CA  . LYS   A 1 383 ? 25.287  -7.098  -17.895 1.00 33.08  ? 920  LYS   A CA  1 
ATOM   2927 C C   . LYS   A 1 383 ? 24.109  -7.570  -17.042 1.00 37.69  ? 920  LYS   A C   1 
ATOM   2928 O O   . LYS   A 1 383 ? 24.266  -8.447  -16.191 1.00 42.27  ? 920  LYS   A O   1 
ATOM   2929 C CB  . LYS   A 1 383 ? 25.946  -5.868  -17.269 1.00 40.70  ? 920  LYS   A CB  1 
ATOM   2930 C CG  . LYS   A 1 383 ? 26.801  -6.228  -16.073 1.00 56.18  ? 920  LYS   A CG  1 
ATOM   2931 C CD  . LYS   A 1 383 ? 27.685  -5.081  -15.633 1.00 64.69  ? 920  LYS   A CD  1 
ATOM   2932 C CE  . LYS   A 1 383 ? 28.578  -5.502  -14.471 1.00 68.61  ? 920  LYS   A CE  1 
ATOM   2933 N NZ  . LYS   A 1 383 ? 29.237  -4.329  -13.824 1.00 68.88  ? 920  LYS   A NZ  1 
ATOM   2934 N N   . LEU   A 1 384 ? 22.927  -7.008  -17.287 1.00 39.33  ? 921  LEU   A N   1 
ATOM   2935 C CA  . LEU   A 1 384 ? 21.730  -7.372  -16.525 1.00 44.36  ? 921  LEU   A CA  1 
ATOM   2936 C C   . LEU   A 1 384 ? 21.362  -8.844  -16.720 1.00 47.90  ? 921  LEU   A C   1 
ATOM   2937 O O   . LEU   A 1 384 ? 20.999  -9.535  -15.769 1.00 52.63  ? 921  LEU   A O   1 
ATOM   2938 C CB  . LEU   A 1 384 ? 20.541  -6.488  -16.921 1.00 42.50  ? 921  LEU   A CB  1 
ATOM   2939 C CG  . LEU   A 1 384 ? 19.204  -6.760  -16.213 1.00 41.74  ? 921  LEU   A CG  1 
ATOM   2940 C CD1 . LEU   A 1 384 ? 19.324  -6.531  -14.710 1.00 41.55  ? 921  LEU   A CD1 1 
ATOM   2941 C CD2 . LEU   A 1 384 ? 18.067  -5.913  -16.797 1.00 43.36  ? 921  LEU   A CD2 1 
ATOM   2942 N N   . LYS   A 1 385 ? 21.469  -9.323  -17.953 1.00 53.24  ? 922  LYS   A N   1 
ATOM   2943 C CA  . LYS   A 1 385 ? 21.033  -10.676 -18.278 1.00 61.92  ? 922  LYS   A CA  1 
ATOM   2944 C C   . LYS   A 1 385 ? 21.951  -11.746 -17.683 1.00 52.09  ? 922  LYS   A C   1 
ATOM   2945 O O   . LYS   A 1 385 ? 21.566  -12.905 -17.577 1.00 57.61  ? 922  LYS   A O   1 
ATOM   2946 C CB  . LYS   A 1 385 ? 20.942  -10.862 -19.796 1.00 71.32  ? 922  LYS   A CB  1 
ATOM   2947 C CG  . LYS   A 1 385 ? 22.257  -11.262 -20.466 1.00 77.27  ? 922  LYS   A CG  1 
ATOM   2948 C CD  . LYS   A 1 385 ? 22.050  -11.734 -21.908 1.00 80.11  ? 922  LYS   A CD  1 
ATOM   2949 C CE  . LYS   A 1 385 ? 22.213  -10.601 -22.917 1.00 81.49  ? 922  LYS   A CE  1 
ATOM   2950 N NZ  . LYS   A 1 385 ? 21.220  -9.506  -22.726 1.00 84.32  ? 922  LYS   A NZ  1 
ATOM   2951 N N   . SER   A 1 386 ? 23.156  -11.356 -17.283 1.00 45.75  ? 923  SER   A N   1 
ATOM   2952 C CA  . SER   A 1 386 ? 24.148  -12.320 -16.824 1.00 54.24  ? 923  SER   A CA  1 
ATOM   2953 C C   . SER   A 1 386 ? 24.239  -12.452 -15.303 1.00 59.27  ? 923  SER   A C   1 
ATOM   2954 O O   . SER   A 1 386 ? 24.600  -13.510 -14.793 1.00 70.58  ? 923  SER   A O   1 
ATOM   2955 C CB  . SER   A 1 386 ? 25.528  -11.952 -17.379 1.00 63.59  ? 923  SER   A CB  1 
ATOM   2956 O OG  . SER   A 1 386 ? 26.019  -10.756 -16.791 1.00 68.23  ? 923  SER   A OG  1 
ATOM   2957 N N   . ILE   A 1 387 ? 23.923  -11.391 -14.572 1.00 58.28  ? 924  ILE   A N   1 
ATOM   2958 C CA  . ILE   A 1 387 ? 24.215  -11.402 -13.143 1.00 60.05  ? 924  ILE   A CA  1 
ATOM   2959 C C   . ILE   A 1 387 ? 23.233  -12.249 -12.348 1.00 55.73  ? 924  ILE   A C   1 
ATOM   2960 O O   . ILE   A 1 387 ? 22.146  -12.594 -12.820 1.00 46.09  ? 924  ILE   A O   1 
ATOM   2961 C CB  . ILE   A 1 387 ? 24.252  -9.971  -12.541 1.00 64.81  ? 924  ILE   A CB  1 
ATOM   2962 C CG1 . ILE   A 1 387 ? 23.170  -9.082  -13.159 1.00 64.88  ? 924  ILE   A CG1 1 
ATOM   2963 C CG2 . ILE   A 1 387 ? 25.640  -9.356  -12.722 1.00 56.38  ? 924  ILE   A CG2 1 
ATOM   2964 C CD1 . ILE   A 1 387 ? 21.770  -9.333  -12.636 1.00 59.29  ? 924  ILE   A CD1 1 
ATOM   2965 N N   . ASN   A 1 388 ? 23.646  -12.584 -11.132 1.00 53.10  ? 925  ASN   A N   1 
ATOM   2966 C CA  . ASN   A 1 388 ? 22.835  -13.383 -10.239 1.00 56.13  ? 925  ASN   A CA  1 
ATOM   2967 C C   . ASN   A 1 388 ? 22.223  -12.507 -9.160  1.00 50.59  ? 925  ASN   A C   1 
ATOM   2968 O O   . ASN   A 1 388 ? 22.844  -11.542 -8.713  1.00 52.10  ? 925  ASN   A O   1 
ATOM   2969 C CB  . ASN   A 1 388 ? 23.678  -14.499 -9.615  1.00 59.34  ? 925  ASN   A CB  1 
ATOM   2970 C CG  . ASN   A 1 388 ? 24.309  -15.410 -10.660 1.00 65.84  ? 925  ASN   A CG  1 
ATOM   2971 O OD1 . ASN   A 1 388 ? 23.640  -15.874 -11.585 1.00 66.18  ? 925  ASN   A OD1 1 
ATOM   2972 N ND2 . ASN   A 1 388 ? 25.604  -15.665 -10.516 1.00 67.99  ? 925  ASN   A ND2 1 
ATOM   2973 N N   . PRO   A 1 389 ? 20.993  -12.833 -8.746  1.00 50.17  ? 926  PRO   A N   1 
ATOM   2974 C CA  . PRO   A 1 389 ? 20.331  -12.146 -7.634  1.00 50.03  ? 926  PRO   A CA  1 
ATOM   2975 C C   . PRO   A 1 389 ? 21.171  -12.223 -6.358  1.00 46.93  ? 926  PRO   A C   1 
ATOM   2976 O O   . PRO   A 1 389 ? 21.962  -13.156 -6.207  1.00 45.44  ? 926  PRO   A O   1 
ATOM   2977 C CB  . PRO   A 1 389 ? 19.019  -12.921 -7.470  1.00 57.57  ? 926  PRO   A CB  1 
ATOM   2978 C CG  . PRO   A 1 389 ? 18.786  -13.567 -8.802  1.00 61.96  ? 926  PRO   A CG  1 
ATOM   2979 C CD  . PRO   A 1 389 ? 20.149  -13.893 -9.327  1.00 55.34  ? 926  PRO   A CD  1 
ATOM   2980 N N   . PRO   A 1 390 ? 21.003  -11.255 -5.451  1.00 40.50  ? 927  PRO   A N   1 
ATOM   2981 C CA  . PRO   A 1 390 ? 20.082  -10.116 -5.580  1.00 37.37  ? 927  PRO   A CA  1 
ATOM   2982 C C   . PRO   A 1 390 ? 20.603  -8.966  -6.448  1.00 40.02  ? 927  PRO   A C   1 
ATOM   2983 O O   . PRO   A 1 390 ? 21.812  -8.747  -6.559  1.00 35.40  ? 927  PRO   A O   1 
ATOM   2984 C CB  . PRO   A 1 390 ? 19.904  -9.658  -4.127  1.00 35.04  ? 927  PRO   A CB  1 
ATOM   2985 C CG  . PRO   A 1 390 ? 21.208  -10.029 -3.473  1.00 45.62  ? 927  PRO   A CG  1 
ATOM   2986 C CD  . PRO   A 1 390 ? 21.624  -11.325 -4.115  1.00 38.03  ? 927  PRO   A CD  1 
ATOM   2987 N N   . CYS   A 1 391 ? 19.673  -8.236  -7.048  1.00 37.28  ? 928  CYS   A N   1 
ATOM   2988 C CA  . CYS   A 1 391 ? 20.025  -7.075  -7.849  1.00 34.85  ? 928  CYS   A CA  1 
ATOM   2989 C C   . CYS   A 1 391 ? 18.914  -6.039  -7.787  1.00 29.51  ? 928  CYS   A C   1 
ATOM   2990 O O   . CYS   A 1 391 ? 17.799  -6.349  -7.371  1.00 40.50  ? 928  CYS   A O   1 
ATOM   2991 C CB  . CYS   A 1 391 ? 20.271  -7.458  -9.302  1.00 45.28  ? 928  CYS   A CB  1 
ATOM   2992 S SG  . CYS   A 1 391 ? 18.763  -7.831  -10.176 1.00 51.70  ? 928  CYS   A SG  1 
ATOM   2993 N N   . VAL   A 1 392 ? 19.229  -4.807  -8.177  1.00 26.66  ? 929  VAL   A N   1 
ATOM   2994 C CA  . VAL   A 1 392 ? 18.215  -3.780  -8.367  1.00 24.04  ? 929  VAL   A CA  1 
ATOM   2995 C C   . VAL   A 1 392 ? 18.378  -3.199  -9.763  1.00 33.28  ? 929  VAL   A C   1 
ATOM   2996 O O   . VAL   A 1 392 ? 19.288  -2.413  -10.014 1.00 30.33  ? 929  VAL   A O   1 
ATOM   2997 C CB  . VAL   A 1 392 ? 18.314  -2.637  -7.342  1.00 27.25  ? 929  VAL   A CB  1 
ATOM   2998 C CG1 . VAL   A 1 392 ? 17.123  -1.710  -7.501  1.00 28.01  ? 929  VAL   A CG1 1 
ATOM   2999 C CG2 . VAL   A 1 392 ? 18.381  -3.186  -5.923  1.00 27.21  ? 929  VAL   A CG2 1 
ATOM   3000 N N   . PRO   A 1 393 ? 17.492  -3.585  -10.685 1.00 33.50  ? 930  PRO   A N   1 
ATOM   3001 C CA  . PRO   A 1 393 ? 17.604  -3.114  -12.067 1.00 28.03  ? 930  PRO   A CA  1 
ATOM   3002 C C   . PRO   A 1 393 ? 17.454  -1.607  -12.175 1.00 30.31  ? 930  PRO   A C   1 
ATOM   3003 O O   . PRO   A 1 393 ? 16.811  -0.977  -11.334 1.00 30.73  ? 930  PRO   A O   1 
ATOM   3004 C CB  . PRO   A 1 393 ? 16.438  -3.827  -12.774 1.00 26.64  ? 930  PRO   A CB  1 
ATOM   3005 C CG  . PRO   A 1 393 ? 16.140  -5.003  -11.927 1.00 38.68  ? 930  PRO   A CG  1 
ATOM   3006 C CD  . PRO   A 1 393 ? 16.409  -4.565  -10.517 1.00 29.94  ? 930  PRO   A CD  1 
ATOM   3007 N N   . PHE   A 1 394 ? 18.057  -1.036  -13.210 1.00 24.77  ? 931  PHE   A N   1 
ATOM   3008 C CA  . PHE   A 1 394 ? 17.790  0.341   -13.600 1.00 28.13  ? 931  PHE   A CA  1 
ATOM   3009 C C   . PHE   A 1 394 ? 16.339  0.425   -14.051 1.00 34.38  ? 931  PHE   A C   1 
ATOM   3010 O O   . PHE   A 1 394 ? 15.928  -0.287  -14.960 1.00 34.64  ? 931  PHE   A O   1 
ATOM   3011 C CB  . PHE   A 1 394 ? 18.746  0.769   -14.711 1.00 30.42  ? 931  PHE   A CB  1 
ATOM   3012 C CG  . PHE   A 1 394 ? 18.423  2.099   -15.333 1.00 30.37  ? 931  PHE   A CG  1 
ATOM   3013 C CD1 . PHE   A 1 394 ? 18.363  3.252   -14.566 1.00 34.71  ? 931  PHE   A CD1 1 
ATOM   3014 C CD2 . PHE   A 1 394 ? 18.223  2.196   -16.705 1.00 34.11  ? 931  PHE   A CD2 1 
ATOM   3015 C CE1 . PHE   A 1 394 ? 18.082  4.485   -15.156 1.00 36.35  ? 931  PHE   A CE1 1 
ATOM   3016 C CE2 . PHE   A 1 394 ? 17.939  3.422   -17.303 1.00 34.60  ? 931  PHE   A CE2 1 
ATOM   3017 C CZ  . PHE   A 1 394 ? 17.862  4.565   -16.525 1.00 34.40  ? 931  PHE   A CZ  1 
ATOM   3018 N N   . PHE   A 1 395 ? 15.560  1.277   -13.400 1.00 31.83  ? 932  PHE   A N   1 
ATOM   3019 C CA  . PHE   A 1 395 ? 14.125  1.316   -13.645 1.00 40.10  ? 932  PHE   A CA  1 
ATOM   3020 C C   . PHE   A 1 395 ? 13.749  2.141   -14.878 1.00 43.67  ? 932  PHE   A C   1 
ATOM   3021 O O   . PHE   A 1 395 ? 12.718  1.892   -15.508 1.00 38.15  ? 932  PHE   A O   1 
ATOM   3022 C CB  . PHE   A 1 395 ? 13.396  1.862   -12.413 1.00 47.12  ? 932  PHE   A CB  1 
ATOM   3023 C CG  . PHE   A 1 395 ? 12.001  1.344   -12.275 1.00 54.02  ? 932  PHE   A CG  1 
ATOM   3024 C CD1 . PHE   A 1 395 ? 11.765  0.116   -11.685 1.00 60.39  ? 932  PHE   A CD1 1 
ATOM   3025 C CD2 . PHE   A 1 395 ? 10.928  2.064   -12.759 1.00 66.79  ? 932  PHE   A CD2 1 
ATOM   3026 C CE1 . PHE   A 1 395 ? 10.480  -0.379  -11.563 1.00 61.20  ? 932  PHE   A CE1 1 
ATOM   3027 C CE2 . PHE   A 1 395 ? 9.643   1.570   -12.646 1.00 67.13  ? 932  PHE   A CE2 1 
ATOM   3028 C CZ  . PHE   A 1 395 ? 9.419   0.352   -12.046 1.00 59.13  ? 932  PHE   A CZ  1 
ATOM   3029 N N   . GLY   A 1 396 ? 14.590  3.112   -15.223 1.00 36.66  ? 933  GLY   A N   1 
ATOM   3030 C CA  . GLY   A 1 396 ? 14.291  4.044   -16.296 1.00 38.41  ? 933  GLY   A CA  1 
ATOM   3031 C C   . GLY   A 1 396 ? 13.987  3.448   -17.654 1.00 43.56  ? 933  GLY   A C   1 
ATOM   3032 O O   . GLY   A 1 396 ? 13.184  3.988   -18.414 1.00 44.92  ? 933  GLY   A O   1 
ATOM   3033 N N   . ILE   A 1 397 ? 14.616  2.326   -17.975 1.00 42.64  ? 934  ILE   A N   1 
ATOM   3034 C CA  . ILE   A 1 397 ? 14.464  1.759   -19.301 1.00 39.09  ? 934  ILE   A CA  1 
ATOM   3035 C C   . ILE   A 1 397 ? 13.060  1.158   -19.480 1.00 36.42  ? 934  ILE   A C   1 
ATOM   3036 O O   . ILE   A 1 397 ? 12.513  1.171   -20.583 1.00 35.88  ? 934  ILE   A O   1 
ATOM   3037 C CB  . ILE   A 1 397 ? 15.558  0.705   -19.579 1.00 51.76  ? 934  ILE   A CB  1 
ATOM   3038 C CG1 . ILE   A 1 397 ? 15.572  0.320   -21.058 1.00 52.46  ? 934  ILE   A CG1 1 
ATOM   3039 C CG2 . ILE   A 1 397 ? 15.404  -0.507  -18.670 1.00 48.45  ? 934  ILE   A CG2 1 
ATOM   3040 C CD1 . ILE   A 1 397 ? 16.790  -0.490  -21.449 1.00 59.34  ? 934  ILE   A CD1 1 
ATOM   3041 N N   . TYR   A 1 398 ? 12.467  0.673   -18.393 1.00 40.44  ? 935  TYR   A N   1 
ATOM   3042 C CA  . TYR   A 1 398 ? 11.100  0.151   -18.451 1.00 34.79  ? 935  TYR   A CA  1 
ATOM   3043 C C   . TYR   A 1 398 ? 10.109  1.289   -18.663 1.00 32.77  ? 935  TYR   A C   1 
ATOM   3044 O O   . TYR   A 1 398 ? 9.154   1.154   -19.430 1.00 36.38  ? 935  TYR   A O   1 
ATOM   3045 C CB  . TYR   A 1 398 ? 10.742  -0.621  -17.182 1.00 31.54  ? 935  TYR   A CB  1 
ATOM   3046 C CG  . TYR   A 1 398 ? 11.684  -1.767  -16.849 1.00 36.93  ? 935  TYR   A CG  1 
ATOM   3047 C CD1 . TYR   A 1 398 ? 11.860  -2.834  -17.724 1.00 42.70  ? 935  TYR   A CD1 1 
ATOM   3048 C CD2 . TYR   A 1 398 ? 12.380  -1.787  -15.650 1.00 39.11  ? 935  TYR   A CD2 1 
ATOM   3049 C CE1 . TYR   A 1 398 ? 12.718  -3.880  -17.413 1.00 44.07  ? 935  TYR   A CE1 1 
ATOM   3050 C CE2 . TYR   A 1 398 ? 13.231  -2.827  -15.331 1.00 40.70  ? 935  TYR   A CE2 1 
ATOM   3051 C CZ  . TYR   A 1 398 ? 13.400  -3.867  -16.214 1.00 38.84  ? 935  TYR   A CZ  1 
ATOM   3052 O OH  . TYR   A 1 398 ? 14.257  -4.896  -15.888 1.00 49.66  ? 935  TYR   A OH  1 
ATOM   3053 N N   . LEU   A 1 399 ? 10.333  2.407   -17.981 1.00 33.31  ? 936  LEU   A N   1 
ATOM   3054 C CA  . LEU   A 1 399 ? 9.443   3.559   -18.111 1.00 34.19  ? 936  LEU   A CA  1 
ATOM   3055 C C   . LEU   A 1 399 ? 9.453   4.116   -19.532 1.00 36.59  ? 936  LEU   A C   1 
ATOM   3056 O O   . LEU   A 1 399 ? 8.403   4.418   -20.108 1.00 34.48  ? 936  LEU   A O   1 
ATOM   3057 C CB  . LEU   A 1 399 ? 9.837   4.653   -17.122 1.00 35.95  ? 936  LEU   A CB  1 
ATOM   3058 C CG  . LEU   A 1 399 ? 9.717   4.288   -15.644 1.00 37.60  ? 936  LEU   A CG  1 
ATOM   3059 C CD1 . LEU   A 1 399 ? 10.360  5.370   -14.772 1.00 42.58  ? 936  LEU   A CD1 1 
ATOM   3060 C CD2 . LEU   A 1 399 ? 8.271   4.079   -15.266 1.00 42.33  ? 936  LEU   A CD2 1 
ATOM   3061 N N   . THR   A 1 400 ? 10.652  4.250   -20.093 1.00 29.74  ? 937  THR   A N   1 
ATOM   3062 C CA  . THR   A 1 400 ? 10.806  4.695   -21.465 1.00 30.71  ? 937  THR   A CA  1 
ATOM   3063 C C   . THR   A 1 400 ? 10.084  3.769   -22.448 1.00 36.40  ? 937  THR   A C   1 
ATOM   3064 O O   . THR   A 1 400 ? 9.314   4.236   -23.296 1.00 34.52  ? 937  THR   A O   1 
ATOM   3065 C CB  . THR   A 1 400 ? 12.301  4.793   -21.823 1.00 36.19  ? 937  THR   A CB  1 
ATOM   3066 O OG1 . THR   A 1 400 ? 12.909  5.761   -20.964 1.00 43.21  ? 937  THR   A OG1 1 
ATOM   3067 C CG2 . THR   A 1 400 ? 12.479  5.216   -23.265 1.00 44.60  ? 937  THR   A CG2 1 
ATOM   3068 N N   . ASN   A 1 401 ? 10.307  2.462   -22.324 1.00 35.71  ? 938  ASN   A N   1 
ATOM   3069 C CA  . ASN   A 1 401 ? 9.670   1.504   -23.234 1.00 38.17  ? 938  ASN   A CA  1 
ATOM   3070 C C   . ASN   A 1 401 ? 8.147   1.487   -23.093 1.00 37.92  ? 938  ASN   A C   1 
ATOM   3071 O O   . ASN   A 1 401 ? 7.426   1.353   -24.079 1.00 39.66  ? 938  ASN   A O   1 
ATOM   3072 C CB  . ASN   A 1 401 ? 10.215  0.090   -23.018 1.00 39.90  ? 938  ASN   A CB  1 
ATOM   3073 C CG  . ASN   A 1 401 ? 11.689  -0.026  -23.354 1.00 57.24  ? 938  ASN   A CG  1 
ATOM   3074 O OD1 . ASN   A 1 401 ? 12.272  0.879   -23.952 1.00 62.17  ? 938  ASN   A OD1 1 
ATOM   3075 N ND2 . ASN   A 1 401 ? 12.299  -1.146  -22.971 1.00 60.76  ? 938  ASN   A ND2 1 
ATOM   3076 N N   . ILE   A 1 402 ? 7.657   1.624   -21.868 1.00 33.31  ? 939  ILE   A N   1 
ATOM   3077 C CA  . ILE   A 1 402 ? 6.216   1.668   -21.668 1.00 31.71  ? 939  ILE   A CA  1 
ATOM   3078 C C   . ILE   A 1 402 ? 5.630   2.937   -22.291 1.00 35.59  ? 939  ILE   A C   1 
ATOM   3079 O O   . ILE   A 1 402 ? 4.610   2.869   -22.980 1.00 38.15  ? 939  ILE   A O   1 
ATOM   3080 C CB  . ILE   A 1 402 ? 5.859   1.558   -20.172 1.00 38.56  ? 939  ILE   A CB  1 
ATOM   3081 C CG1 . ILE   A 1 402 ? 6.142   0.124   -19.709 1.00 39.36  ? 939  ILE   A CG1 1 
ATOM   3082 C CG2 . ILE   A 1 402 ? 4.381   1.893   -19.943 1.00 35.31  ? 939  ILE   A CG2 1 
ATOM   3083 C CD1 . ILE   A 1 402 ? 6.079   -0.092  -18.221 1.00 42.74  ? 939  ILE   A CD1 1 
ATOM   3084 N N   . LEU   A 1 403 ? 6.292   4.078   -22.101 1.00 34.00  ? 940  LEU   A N   1 
ATOM   3085 C CA  . LEU   A 1 403 ? 5.800   5.318   -22.694 1.00 35.41  ? 940  LEU   A CA  1 
ATOM   3086 C C   . LEU   A 1 403 ? 5.737   5.210   -24.220 1.00 37.86  ? 940  LEU   A C   1 
ATOM   3087 O O   . LEU   A 1 403 ? 4.742   5.597   -24.823 1.00 37.84  ? 940  LEU   A O   1 
ATOM   3088 C CB  . LEU   A 1 403 ? 6.665   6.506   -22.275 1.00 35.36  ? 940  LEU   A CB  1 
ATOM   3089 C CG  . LEU   A 1 403 ? 6.485   7.012   -20.838 1.00 36.44  ? 940  LEU   A CG  1 
ATOM   3090 C CD1 . LEU   A 1 403 ? 7.594   8.013   -20.460 1.00 34.14  ? 940  LEU   A CD1 1 
ATOM   3091 C CD2 . LEU   A 1 403 ? 5.092   7.620   -20.628 1.00 45.05  ? 940  LEU   A CD2 1 
ATOM   3092 N N   . LYS   A 1 404 ? 6.778   4.655   -24.832 1.00 36.58  ? 941  LYS   A N   1 
ATOM   3093 C CA  . LYS   A 1 404 ? 6.801   4.461   -26.283 1.00 36.97  ? 941  LYS   A CA  1 
ATOM   3094 C C   . LYS   A 1 404 ? 5.650   3.577   -26.744 1.00 40.10  ? 941  LYS   A C   1 
ATOM   3095 O O   . LYS   A 1 404 ? 4.977   3.877   -27.732 1.00 41.74  ? 941  LYS   A O   1 
ATOM   3096 C CB  . LYS   A 1 404 ? 8.122   3.838   -26.731 1.00 40.07  ? 941  LYS   A CB  1 
ATOM   3097 C CG  . LYS   A 1 404 ? 9.330   4.743   -26.557 1.00 57.27  ? 941  LYS   A CG  1 
ATOM   3098 C CD  . LYS   A 1 404 ? 10.608  4.070   -27.057 1.00 67.79  ? 941  LYS   A CD  1 
ATOM   3099 C CE  . LYS   A 1 404 ? 11.822  4.977   -26.868 1.00 68.91  ? 941  LYS   A CE  1 
ATOM   3100 N NZ  . LYS   A 1 404 ? 13.094  4.270   -27.181 1.00 68.85  ? 941  LYS   A NZ  1 
ATOM   3101 N N   . THR   A 1 405 ? 5.432   2.480   -26.029 1.00 36.02  ? 942  THR   A N   1 
ATOM   3102 C CA  . THR   A 1 405 ? 4.393   1.530   -26.409 1.00 34.24  ? 942  THR   A CA  1 
ATOM   3103 C C   . THR   A 1 405 ? 3.003   2.150   -26.274 1.00 34.32  ? 942  THR   A C   1 
ATOM   3104 O O   . THR   A 1 405 ? 2.147   1.946   -27.137 1.00 37.37  ? 942  THR   A O   1 
ATOM   3105 C CB  . THR   A 1 405 ? 4.478   0.236   -25.562 1.00 38.51  ? 942  THR   A CB  1 
ATOM   3106 O OG1 . THR   A 1 405 ? 5.792   -0.319  -25.684 1.00 40.90  ? 942  THR   A OG1 1 
ATOM   3107 C CG2 . THR   A 1 405 ? 3.465   -0.792  -26.036 1.00 36.54  ? 942  THR   A CG2 1 
ATOM   3108 N N   . GLU   A 1 406 ? 2.778   2.906   -25.199 1.00 35.82  ? 943  GLU   A N   1 
ATOM   3109 C CA  . GLU   A 1 406 ? 1.491   3.579   -25.009 1.00 42.49  ? 943  GLU   A CA  1 
ATOM   3110 C C   . GLU   A 1 406 ? 1.264   4.608   -26.127 1.00 49.03  ? 943  GLU   A C   1 
ATOM   3111 O O   . GLU   A 1 406 ? 0.178   4.688   -26.703 1.00 46.30  ? 943  GLU   A O   1 
ATOM   3112 C CB  . GLU   A 1 406 ? 1.417   4.255   -23.632 1.00 37.76  ? 943  GLU   A CB  1 
ATOM   3113 C CG  . GLU   A 1 406 ? 1.354   3.287   -22.444 1.00 38.61  ? 943  GLU   A CG  1 
ATOM   3114 C CD  . GLU   A 1 406 ? -0.018  2.649   -22.267 1.00 58.11  ? 943  GLU   A CD  1 
ATOM   3115 O OE1 . GLU   A 1 406 ? -1.008  3.191   -22.813 1.00 61.22  ? 943  GLU   A OE1 1 
ATOM   3116 O OE2 . GLU   A 1 406 ? -0.108  1.608   -21.577 1.00 55.39  ? 943  GLU   A OE2 1 
ATOM   3117 N N   . GLU   A 1 407 ? 2.303   5.382   -26.435 1.00 42.62  ? 944  GLU   A N   1 
ATOM   3118 C CA  . GLU   A 1 407 ? 2.240   6.371   -27.511 1.00 46.11  ? 944  GLU   A CA  1 
ATOM   3119 C C   . GLU   A 1 407 ? 2.086   5.744   -28.896 1.00 44.19  ? 944  GLU   A C   1 
ATOM   3120 O O   . GLU   A 1 407 ? 1.400   6.291   -29.762 1.00 51.21  ? 944  GLU   A O   1 
ATOM   3121 C CB  . GLU   A 1 407 ? 3.501   7.246   -27.501 1.00 56.37  ? 944  GLU   A CB  1 
ATOM   3122 C CG  . GLU   A 1 407 ? 3.666   8.105   -26.259 1.00 73.58  ? 944  GLU   A CG  1 
ATOM   3123 C CD  . GLU   A 1 407 ? 2.754   9.311   -26.259 1.00 88.16  ? 944  GLU   A CD  1 
ATOM   3124 O OE1 . GLU   A 1 407 ? 2.909   10.172  -27.152 1.00 95.60  ? 944  GLU   A OE1 1 
ATOM   3125 O OE2 . GLU   A 1 407 ? 1.882   9.396   -25.369 1.00 88.67  ? 944  GLU   A OE2 1 
ATOM   3126 N N   . GLY   A 1 408 ? 2.730   4.601   -29.109 1.00 43.19  ? 945  GLY   A N   1 
ATOM   3127 C CA  . GLY   A 1 408 ? 2.827   4.023   -30.440 1.00 45.20  ? 945  GLY   A CA  1 
ATOM   3128 C C   . GLY   A 1 408 ? 1.717   3.055   -30.812 1.00 47.63  ? 945  GLY   A C   1 
ATOM   3129 O O   . GLY   A 1 408 ? 1.773   2.415   -31.860 1.00 45.04  ? 945  GLY   A O   1 
ATOM   3130 N N   . ASN   A 1 409 ? 0.711   2.939   -29.952 1.00 38.40  ? 946  ASN   A N   1 
ATOM   3131 C CA  . ASN   A 1 409 ? -0.427  2.057   -30.209 1.00 36.44  ? 946  ASN   A CA  1 
ATOM   3132 C C   . ASN   A 1 409 ? -1.727  2.725   -29.798 1.00 40.14  ? 946  ASN   A C   1 
ATOM   3133 O O   . ASN   A 1 409 ? -1.790  3.375   -28.754 1.00 38.29  ? 946  ASN   A O   1 
ATOM   3134 C CB  . ASN   A 1 409 ? -0.272  0.733   -29.458 1.00 40.01  ? 946  ASN   A CB  1 
ATOM   3135 C CG  . ASN   A 1 409 ? 0.895   -0.090  -29.955 1.00 48.55  ? 946  ASN   A CG  1 
ATOM   3136 O OD1 . ASN   A 1 409 ? 0.769   -0.834  -30.926 1.00 48.49  ? 946  ASN   A OD1 1 
ATOM   3137 N ND2 . ASN   A 1 409 ? 2.036   0.022   -29.277 1.00 40.87  ? 946  ASN   A ND2 1 
ATOM   3138 N N   . ASN   A 1 410 ? -2.770  2.560   -30.603 1.00 38.74  ? 947  ASN   A N   1 
ATOM   3139 C CA  . ASN   A 1 410 ? -4.049  3.187   -30.285 1.00 35.67  ? 947  ASN   A CA  1 
ATOM   3140 C C   . ASN   A 1 410 ? -4.803  2.401   -29.216 1.00 35.99  ? 947  ASN   A C   1 
ATOM   3141 O O   . ASN   A 1 410 ? -4.727  1.174   -29.184 1.00 35.39  ? 947  ASN   A O   1 
ATOM   3142 C CB  . ASN   A 1 410 ? -4.915  3.323   -31.535 1.00 47.70  ? 947  ASN   A CB  1 
ATOM   3143 C CG  . ASN   A 1 410 ? -5.921  4.455   -31.418 1.00 68.10  ? 947  ASN   A CG  1 
ATOM   3144 O OD1 . ASN   A 1 410 ? -7.006  4.296   -30.841 1.00 56.47  ? 947  ASN   A OD1 1 
ATOM   3145 N ND2 . ASN   A 1 410 ? -5.560  5.613   -31.958 1.00 74.41  ? 947  ASN   A ND2 1 
ATOM   3146 N N   . ASP   A 1 411 ? -5.532  3.110   -28.353 1.00 33.18  ? 948  ASP   A N   1 
ATOM   3147 C CA  . ASP   A 1 411 ? -6.345  2.463   -27.327 1.00 31.13  ? 948  ASP   A CA  1 
ATOM   3148 C C   . ASP   A 1 411 ? -7.508  1.685   -27.932 1.00 30.10  ? 948  ASP   A C   1 
ATOM   3149 O O   . ASP   A 1 411 ? -8.034  0.758   -27.318 1.00 31.24  ? 948  ASP   A O   1 
ATOM   3150 C CB  . ASP   A 1 411 ? -6.892  3.488   -26.337 1.00 37.76  ? 948  ASP   A CB  1 
ATOM   3151 C CG  . ASP   A 1 411 ? -5.879  3.881   -25.275 1.00 39.37  ? 948  ASP   A CG  1 
ATOM   3152 O OD1 . ASP   A 1 411 ? -4.857  3.177   -25.110 1.00 35.52  ? 948  ASP   A OD1 1 
ATOM   3153 O OD2 . ASP   A 1 411 ? -6.126  4.890   -24.590 1.00 46.03  ? 948  ASP   A OD2 1 
ATOM   3154 N N   . PHE   A 1 412 ? -7.923  2.090   -29.127 1.00 29.72  ? 949  PHE   A N   1 
ATOM   3155 C CA  . PHE   A 1 412 ? -9.096  1.502   -29.747 1.00 34.74  ? 949  PHE   A CA  1 
ATOM   3156 C C   . PHE   A 1 412 ? -8.799  0.956   -31.128 1.00 35.62  ? 949  PHE   A C   1 
ATOM   3157 O O   . PHE   A 1 412 ? -7.882  1.417   -31.811 1.00 37.12  ? 949  PHE   A O   1 
ATOM   3158 C CB  . PHE   A 1 412 ? -10.228 2.532   -29.843 1.00 37.92  ? 949  PHE   A CB  1 
ATOM   3159 C CG  . PHE   A 1 412 ? -10.764 2.965   -28.509 1.00 38.08  ? 949  PHE   A CG  1 
ATOM   3160 C CD1 . PHE   A 1 412 ? -11.747 2.222   -27.869 1.00 37.41  ? 949  PHE   A CD1 1 
ATOM   3161 C CD2 . PHE   A 1 412 ? -10.279 4.110   -27.890 1.00 43.77  ? 949  PHE   A CD2 1 
ATOM   3162 C CE1 . PHE   A 1 412 ? -12.238 2.611   -26.631 1.00 40.07  ? 949  PHE   A CE1 1 
ATOM   3163 C CE2 . PHE   A 1 412 ? -10.768 4.503   -26.649 1.00 41.49  ? 949  PHE   A CE2 1 
ATOM   3164 C CZ  . PHE   A 1 412 ? -11.743 3.756   -26.024 1.00 36.55  ? 949  PHE   A CZ  1 
ATOM   3165 N N   . LEU   A 1 413 ? -9.588  -0.033  -31.524 1.00 36.67  ? 950  LEU   A N   1 
ATOM   3166 C CA  . LEU   A 1 413 ? -9.659  -0.464  -32.906 1.00 37.81  ? 950  LEU   A CA  1 
ATOM   3167 C C   . LEU   A 1 413 ? -10.867 0.226   -33.535 1.00 39.53  ? 950  LEU   A C   1 
ATOM   3168 O O   . LEU   A 1 413 ? -11.984 0.102   -33.037 1.00 35.20  ? 950  LEU   A O   1 
ATOM   3169 C CB  . LEU   A 1 413 ? -9.790  -1.983  -32.994 1.00 34.26  ? 950  LEU   A CB  1 
ATOM   3170 C CG  . LEU   A 1 413 ? -8.759  -2.740  -32.149 1.00 37.12  ? 950  LEU   A CG  1 
ATOM   3171 C CD1 . LEU   A 1 413 ? -9.053  -4.231  -32.162 1.00 34.17  ? 950  LEU   A CD1 1 
ATOM   3172 C CD2 . LEU   A 1 413 ? -7.353  -2.458  -32.663 1.00 39.38  ? 950  LEU   A CD2 1 
ATOM   3173 N N   . LYS   A 1 414 ? -10.639 0.955   -34.620 1.00 44.67  ? 951  LYS   A N   1 
ATOM   3174 C CA  . LYS   A 1 414 ? -11.701 1.724   -35.263 1.00 51.60  ? 951  LYS   A CA  1 
ATOM   3175 C C   . LYS   A 1 414 ? -12.726 0.822   -35.956 1.00 49.13  ? 951  LYS   A C   1 
ATOM   3176 O O   . LYS   A 1 414 ? -12.367 -0.125  -36.661 1.00 43.87  ? 951  LYS   A O   1 
ATOM   3177 C CB  . LYS   A 1 414 ? -11.087 2.712   -36.260 1.00 63.50  ? 951  LYS   A CB  1 
ATOM   3178 C CG  . LYS   A 1 414 ? -9.911  3.494   -35.679 1.00 77.19  ? 951  LYS   A CG  1 
ATOM   3179 C CD  . LYS   A 1 414 ? -9.016  4.084   -36.767 1.00 86.59  ? 951  LYS   A CD  1 
ATOM   3180 C CE  . LYS   A 1 414 ? -7.599  4.330   -36.252 1.00 86.79  ? 951  LYS   A CE  1 
ATOM   3181 N NZ  . LYS   A 1 414 ? -6.731  4.976   -37.277 1.00 86.96  ? 951  LYS   A NZ  1 
ATOM   3182 N N   . LYS   A 1 415 ? -14.005 1.110   -35.721 1.00 42.35  ? 952  LYS   A N   1 
ATOM   3183 C CA  . LYS   A 1 415 ? -15.105 0.380   -36.344 1.00 41.51  ? 952  LYS   A CA  1 
ATOM   3184 C C   . LYS   A 1 415 ? -16.136 1.355   -36.890 1.00 50.78  ? 952  LYS   A C   1 
ATOM   3185 O O   . LYS   A 1 415 ? -16.115 2.541   -36.568 1.00 48.35  ? 952  LYS   A O   1 
ATOM   3186 C CB  . LYS   A 1 415 ? -15.778 -0.573  -35.349 1.00 39.40  ? 952  LYS   A CB  1 
ATOM   3187 C CG  . LYS   A 1 415 ? -14.886 -1.705  -34.860 1.00 42.32  ? 952  LYS   A CG  1 
ATOM   3188 C CD  . LYS   A 1 415 ? -14.628 -2.728  -35.959 1.00 46.72  ? 952  LYS   A CD  1 
ATOM   3189 C CE  . LYS   A 1 415 ? -13.429 -3.603  -35.629 1.00 43.43  ? 952  LYS   A CE  1 
ATOM   3190 N NZ  . LYS   A 1 415 ? -13.301 -4.776  -36.542 1.00 40.51  ? 952  LYS   A NZ  1 
ATOM   3191 N N   . LYS   A 1 416 ? -17.042 0.843   -37.715 1.00 53.23  ? 953  LYS   A N   1 
ATOM   3192 C CA  . LYS   A 1 416 ? -18.152 1.640   -38.215 1.00 64.26  ? 953  LYS   A CA  1 
ATOM   3193 C C   . LYS   A 1 416 ? -19.097 1.963   -37.058 1.00 58.67  ? 953  LYS   A C   1 
ATOM   3194 O O   . LYS   A 1 416 ? -19.588 3.085   -36.937 1.00 59.55  ? 953  LYS   A O   1 
ATOM   3195 C CB  . LYS   A 1 416 ? -18.876 0.891   -39.337 1.00 72.19  ? 953  LYS   A CB  1 
ATOM   3196 C CG  . LYS   A 1 416 ? -20.079 1.602   -39.921 1.00 84.47  ? 953  LYS   A CG  1 
ATOM   3197 C CD  . LYS   A 1 416 ? -20.788 0.699   -40.922 1.00 91.45  ? 953  LYS   A CD  1 
ATOM   3198 C CE  . LYS   A 1 416 ? -22.156 1.240   -41.300 1.00 90.47  ? 953  LYS   A CE  1 
ATOM   3199 N NZ  . LYS   A 1 416 ? -22.053 2.543   -42.004 1.00 88.66  ? 953  LYS   A NZ  1 
ATOM   3200 N N   . GLY   A 1 417 ? -19.338 0.975   -36.201 1.00 45.16  ? 954  GLY   A N   1 
ATOM   3201 C CA  . GLY   A 1 417 ? -20.098 1.191   -34.981 1.00 45.89  ? 954  GLY   A CA  1 
ATOM   3202 C C   . GLY   A 1 417 ? -19.189 1.576   -33.822 1.00 50.94  ? 954  GLY   A C   1 
ATOM   3203 O O   . GLY   A 1 417 ? -18.226 2.316   -34.002 1.00 50.71  ? 954  GLY   A O   1 
ATOM   3204 N N   . LYS   A 1 418 ? -19.497 1.073   -32.630 1.00 46.63  ? 955  LYS   A N   1 
ATOM   3205 C CA  . LYS   A 1 418 ? -18.666 1.316   -31.456 1.00 50.23  ? 955  LYS   A CA  1 
ATOM   3206 C C   . LYS   A 1 418 ? -17.251 0.771   -31.671 1.00 48.87  ? 955  LYS   A C   1 
ATOM   3207 O O   . LYS   A 1 418 ? -17.069 -0.375  -32.084 1.00 40.47  ? 955  LYS   A O   1 
ATOM   3208 C CB  . LYS   A 1 418 ? -19.303 0.682   -30.215 1.00 55.92  ? 955  LYS   A CB  1 
ATOM   3209 C CG  . LYS   A 1 418 ? -18.370 0.568   -29.017 1.00 67.80  ? 955  LYS   A CG  1 
ATOM   3210 C CD  . LYS   A 1 418 ? -18.202 1.889   -28.272 1.00 77.79  ? 955  LYS   A CD  1 
ATOM   3211 C CE  . LYS   A 1 418 ? -19.192 1.988   -27.127 1.00 84.29  ? 955  LYS   A CE  1 
ATOM   3212 N NZ  . LYS   A 1 418 ? -19.393 0.651   -26.494 1.00 87.50  ? 955  LYS   A NZ  1 
ATOM   3213 N N   . ASP   A 1 419 ? -16.247 1.601   -31.411 1.00 46.08  ? 956  ASP   A N   1 
ATOM   3214 C CA  . ASP   A 1 419 ? -14.865 1.163   -31.556 1.00 45.17  ? 956  ASP   A CA  1 
ATOM   3215 C C   . ASP   A 1 419 ? -14.533 0.119   -30.495 1.00 42.41  ? 956  ASP   A C   1 
ATOM   3216 O O   . ASP   A 1 419 ? -15.090 0.128   -29.399 1.00 35.22  ? 956  ASP   A O   1 
ATOM   3217 C CB  . ASP   A 1 419 ? -13.906 2.351   -31.455 1.00 30.00  ? 956  ASP   A CB  1 
ATOM   3218 C CG  . ASP   A 1 419 ? -13.969 3.255   -32.670 1.00 30.00  ? 956  ASP   A CG  1 
ATOM   3219 O OD1 . ASP   A 1 419 ? -14.527 2.828   -33.702 1.00 30.00  ? 956  ASP   A OD1 1 
ATOM   3220 O OD2 . ASP   A 1 419 ? -13.487 4.408   -32.686 1.00 30.00  ? 956  ASP   A OD2 1 
ATOM   3221 N N   . LEU   A 1 420 ? -13.632 -0.792  -30.836 1.00 30.53  ? 957  LEU   A N   1 
ATOM   3222 C CA  . LEU   A 1 420 ? -13.293 -1.882  -29.937 1.00 29.11  ? 957  LEU   A CA  1 
ATOM   3223 C C   . LEU   A 1 420 ? -12.080 -1.528  -29.092 1.00 27.49  ? 957  LEU   A C   1 
ATOM   3224 O O   . LEU   A 1 420 ? -11.207 -0.775  -29.513 1.00 31.94  ? 957  LEU   A O   1 
ATOM   3225 C CB  . LEU   A 1 420 ? -13.027 -3.163  -30.727 1.00 27.20  ? 957  LEU   A CB  1 
ATOM   3226 C CG  . LEU   A 1 420 ? -14.110 -3.642  -31.694 1.00 32.27  ? 957  LEU   A CG  1 
ATOM   3227 C CD1 . LEU   A 1 420 ? -13.728 -5.010  -32.242 1.00 34.58  ? 957  LEU   A CD1 1 
ATOM   3228 C CD2 . LEU   A 1 420 ? -15.470 -3.701  -31.012 1.00 30.91  ? 957  LEU   A CD2 1 
ATOM   3229 N N   . ILE   A 1 421 ? -12.034 -2.072  -27.882 1.00 25.78  ? 958  ILE   A N   1 
ATOM   3230 C CA  . ILE   A 1 421 ? -10.856 -1.933  -27.055 1.00 26.77  ? 958  ILE   A CA  1 
ATOM   3231 C C   . ILE   A 1 421 ? -9.702  -2.692  -27.697 1.00 28.65  ? 958  ILE   A C   1 
ATOM   3232 O O   . ILE   A 1 421 ? -9.860  -3.850  -28.059 1.00 27.45  ? 958  ILE   A O   1 
ATOM   3233 C CB  . ILE   A 1 421 ? -11.119 -2.470  -25.649 1.00 24.40  ? 958  ILE   A CB  1 
ATOM   3234 C CG1 . ILE   A 1 421 ? -12.180 -1.593  -24.971 1.00 26.96  ? 958  ILE   A CG1 1 
ATOM   3235 C CG2 . ILE   A 1 421 ? -9.799  -2.536  -24.849 1.00 25.35  ? 958  ILE   A CG2 1 
ATOM   3236 C CD1 . ILE   A 1 421 ? -12.865 -2.254  -23.774 1.00 31.56  ? 958  ILE   A CD1 1 
ATOM   3237 N N   . ASN   A 1 422 ? -8.555  -2.034  -27.850 1.00 27.72  ? 959  ASN   A N   1 
ATOM   3238 C CA  . ASN   A 1 422 ? -7.360  -2.674  -28.394 1.00 26.28  ? 959  ASN   A CA  1 
ATOM   3239 C C   . ASN   A 1 422 ? -6.644  -3.450  -27.287 1.00 25.91  ? 959  ASN   A C   1 
ATOM   3240 O O   . ASN   A 1 422 ? -5.823  -2.878  -26.568 1.00 26.90  ? 959  ASN   A O   1 
ATOM   3241 C CB  . ASN   A 1 422 ? -6.427  -1.626  -29.024 1.00 29.08  ? 959  ASN   A CB  1 
ATOM   3242 C CG  . ASN   A 1 422 ? -5.157  -2.236  -29.584 1.00 30.35  ? 959  ASN   A CG  1 
ATOM   3243 O OD1 . ASN   A 1 422 ? -4.985  -3.455  -29.572 1.00 32.95  ? 959  ASN   A OD1 1 
ATOM   3244 N ND2 . ASN   A 1 422 ? -4.255  -1.389  -30.085 1.00 29.99  ? 959  ASN   A ND2 1 
ATOM   3245 N N   . PHE   A 1 423 ? -6.954  -4.742  -27.142 1.00 23.74  ? 960  PHE   A N   1 
ATOM   3246 C CA  . PHE   A 1 423 ? -6.376  -5.494  -26.025 1.00 25.91  ? 960  PHE   A CA  1 
ATOM   3247 C C   . PHE   A 1 423 ? -4.921  -5.868  -26.286 1.00 24.84  ? 960  PHE   A C   1 
ATOM   3248 O O   . PHE   A 1 423 ? -4.118  -5.973  -25.356 1.00 24.65  ? 960  PHE   A O   1 
ATOM   3249 C CB  . PHE   A 1 423 ? -7.181  -6.762  -25.702 1.00 22.43  ? 960  PHE   A CB  1 
ATOM   3250 C CG  . PHE   A 1 423 ? -6.775  -7.383  -24.398 1.00 23.55  ? 960  PHE   A CG  1 
ATOM   3251 C CD1 . PHE   A 1 423 ? -7.190  -6.826  -23.203 1.00 26.27  ? 960  PHE   A CD1 1 
ATOM   3252 C CD2 . PHE   A 1 423 ? -5.959  -8.505  -24.368 1.00 24.77  ? 960  PHE   A CD2 1 
ATOM   3253 C CE1 . PHE   A 1 423 ? -6.801  -7.374  -21.988 1.00 24.71  ? 960  PHE   A CE1 1 
ATOM   3254 C CE2 . PHE   A 1 423 ? -5.570  -9.067  -23.170 1.00 23.30  ? 960  PHE   A CE2 1 
ATOM   3255 C CZ  . PHE   A 1 423 ? -5.994  -8.501  -21.974 1.00 25.80  ? 960  PHE   A CZ  1 
ATOM   3256 N N   . SER   A 1 424 ? -4.568  -6.048  -27.555 1.00 26.90  ? 961  SER   A N   1 
ATOM   3257 C CA  . SER   A 1 424 ? -3.196  -6.432  -27.876 1.00 29.90  ? 961  SER   A CA  1 
ATOM   3258 C C   . SER   A 1 424 ? -2.205  -5.362  -27.419 1.00 32.68  ? 961  SER   A C   1 
ATOM   3259 O O   . SER   A 1 424 ? -1.086  -5.681  -27.032 1.00 32.89  ? 961  SER   A O   1 
ATOM   3260 C CB  . SER   A 1 424 ? -3.054  -6.704  -29.371 1.00 32.86  ? 961  SER   A CB  1 
ATOM   3261 O OG  . SER   A 1 424 ? -3.644  -7.952  -29.687 1.00 39.32  ? 961  SER   A OG  1 
ATOM   3262 N N   . LYS   A 1 425 ? -2.627  -4.099  -27.437 1.00 26.71  ? 962  LYS   A N   1 
ATOM   3263 C CA  . LYS   A 1 425 ? -1.807  -3.032  -26.875 1.00 26.60  ? 962  LYS   A CA  1 
ATOM   3264 C C   . LYS   A 1 425 ? -1.530  -3.279  -25.397 1.00 25.64  ? 962  LYS   A C   1 
ATOM   3265 O O   . LYS   A 1 425 ? -0.408  -3.096  -24.918 1.00 28.62  ? 962  LYS   A O   1 
ATOM   3266 C CB  . LYS   A 1 425 ? -2.491  -1.667  -27.044 1.00 27.19  ? 962  LYS   A CB  1 
ATOM   3267 C CG  . LYS   A 1 425 ? -1.729  -0.514  -26.374 1.00 32.76  ? 962  LYS   A CG  1 
ATOM   3268 C CD  . LYS   A 1 425 ? -2.490  0.801   -26.482 1.00 27.85  ? 962  LYS   A CD  1 
ATOM   3269 C CE  . LYS   A 1 425 ? -1.702  1.964   -25.859 1.00 31.75  ? 962  LYS   A CE  1 
ATOM   3270 N NZ  . LYS   A 1 425 ? -2.370  3.277   -26.098 1.00 35.05  ? 962  LYS   A NZ  1 
ATOM   3271 N N   . ARG   A 1 426 ? -2.558  -3.689  -24.664 1.00 25.22  ? 963  ARG   A N   1 
ATOM   3272 C CA  . ARG   A 1 426 ? -2.389  -3.922  -23.233 1.00 23.59  ? 963  ARG   A CA  1 
ATOM   3273 C C   . ARG   A 1 426 ? -1.473  -5.101  -22.979 1.00 28.26  ? 963  ARG   A C   1 
ATOM   3274 O O   . ARG   A 1 426 ? -0.663  -5.073  -22.051 1.00 28.71  ? 963  ARG   A O   1 
ATOM   3275 C CB  . ARG   A 1 426 ? -3.739  -4.156  -22.563 1.00 22.46  ? 963  ARG   A CB  1 
ATOM   3276 C CG  . ARG   A 1 426 ? -4.454  -2.869  -22.143 1.00 24.04  ? 963  ARG   A CG  1 
ATOM   3277 C CD  . ARG   A 1 426 ? -4.887  -2.009  -23.355 1.00 27.70  ? 963  ARG   A CD  1 
ATOM   3278 N NE  . ARG   A 1 426 ? -5.652  -0.828  -22.951 1.00 26.75  ? 963  ARG   A NE  1 
ATOM   3279 C CZ  . ARG   A 1 426 ? -6.422  -0.121  -23.776 1.00 29.37  ? 963  ARG   A CZ  1 
ATOM   3280 N NH1 . ARG   A 1 426 ? -6.528  -0.492  -25.046 1.00 26.70  ? 963  ARG   A NH1 1 
ATOM   3281 N NH2 . ARG   A 1 426 ? -7.097  0.939   -23.335 1.00 30.85  ? 963  ARG   A NH2 1 
ATOM   3282 N N   . ARG   A 1 427 ? -1.614  -6.138  -23.801 1.00 25.86  ? 964  ARG   A N   1 
ATOM   3283 C CA  . ARG   A 1 427 ? -0.748  -7.310  -23.712 1.00 27.56  ? 964  ARG   A CA  1 
ATOM   3284 C C   . ARG   A 1 427 ? 0.713   -6.916  -23.894 1.00 29.68  ? 964  ARG   A C   1 
ATOM   3285 O O   . ARG   A 1 427 ? 1.585   -7.401  -23.176 1.00 28.82  ? 964  ARG   A O   1 
ATOM   3286 C CB  . ARG   A 1 427 ? -1.146  -8.354  -24.757 1.00 27.33  ? 964  ARG   A CB  1 
ATOM   3287 C CG  . ARG   A 1 427 ? -0.295  -9.626  -24.722 1.00 32.22  ? 964  ARG   A CG  1 
ATOM   3288 C CD  . ARG   A 1 427 ? -0.781  -10.668 -25.735 1.00 29.56  ? 964  ARG   A CD  1 
ATOM   3289 N NE  . ARG   A 1 427 ? -2.156  -11.103 -25.463 1.00 32.28  ? 964  ARG   A NE  1 
ATOM   3290 C CZ  . ARG   A 1 427 ? -3.210  -10.809 -26.225 1.00 36.03  ? 964  ARG   A CZ  1 
ATOM   3291 N NH1 . ARG   A 1 427 ? -3.064  -10.085 -27.332 1.00 30.56  ? 964  ARG   A NH1 1 
ATOM   3292 N NH2 . ARG   A 1 427 ? -4.421  -11.253 -25.883 1.00 33.89  ? 964  ARG   A NH2 1 
ATOM   3293 N N   . LYS   A 1 428 ? 0.981   -6.028  -24.846 1.00 28.59  ? 965  LYS   A N   1 
ATOM   3294 C CA  . LYS   A 1 428 ? 2.362   -5.583  -25.079 1.00 28.08  ? 965  LYS   A CA  1 
ATOM   3295 C C   . LYS   A 1 428 ? 2.928   -4.860  -23.867 1.00 29.30  ? 965  LYS   A C   1 
ATOM   3296 O O   . LYS   A 1 428 ? 4.094   -5.039  -23.523 1.00 30.54  ? 965  LYS   A O   1 
ATOM   3297 C CB  . LYS   A 1 428 ? 2.447   -4.671  -26.298 1.00 32.54  ? 965  LYS   A CB  1 
ATOM   3298 C CG  . LYS   A 1 428 ? 2.109   -5.349  -27.605 1.00 44.91  ? 965  LYS   A CG  1 
ATOM   3299 C CD  . LYS   A 1 428 ? 2.273   -4.365  -28.749 1.00 51.07  ? 965  LYS   A CD  1 
ATOM   3300 C CE  . LYS   A 1 428 ? 1.730   -4.918  -30.048 1.00 52.97  ? 965  LYS   A CE  1 
ATOM   3301 N NZ  . LYS   A 1 428 ? 1.697   -3.839  -31.068 1.00 64.97  ? 965  LYS   A NZ  1 
ATOM   3302 N N   . VAL   A 1 429 ? 2.118   -4.018  -23.233 1.00 29.64  ? 966  VAL   A N   1 
ATOM   3303 C CA  . VAL   A 1 429 ? 2.563   -3.339  -22.018 1.00 29.03  ? 966  VAL   A CA  1 
ATOM   3304 C C   . VAL   A 1 429 ? 2.812   -4.361  -20.909 1.00 31.29  ? 966  VAL   A C   1 
ATOM   3305 O O   . VAL   A 1 429 ? 3.822   -4.306  -20.209 1.00 27.93  ? 966  VAL   A O   1 
ATOM   3306 C CB  . VAL   A 1 429 ? 1.530   -2.286  -21.544 1.00 33.13  ? 966  VAL   A CB  1 
ATOM   3307 C CG1 . VAL   A 1 429 ? 1.912   -1.746  -20.162 1.00 34.34  ? 966  VAL   A CG1 1 
ATOM   3308 C CG2 . VAL   A 1 429 ? 1.435   -1.155  -22.554 1.00 33.42  ? 966  VAL   A CG2 1 
ATOM   3309 N N   . ALA   A 1 430 ? 1.891   -5.309  -20.757 1.00 26.11  ? 967  ALA   A N   1 
ATOM   3310 C CA  . ALA   A 1 430 ? 2.028   -6.317  -19.712 1.00 26.03  ? 967  ALA   A CA  1 
ATOM   3311 C C   . ALA   A 1 430 ? 3.296   -7.154  -19.889 1.00 29.76  ? 967  ALA   A C   1 
ATOM   3312 O O   . ALA   A 1 430 ? 3.870   -7.618  -18.903 1.00 28.01  ? 967  ALA   A O   1 
ATOM   3313 C CB  . ALA   A 1 430 ? 0.799   -7.219  -19.677 1.00 24.09  ? 967  ALA   A CB  1 
ATOM   3314 N N   . GLU   A 1 431 ? 3.725   -7.352  -21.137 1.00 31.82  ? 968  GLU   A N   1 
ATOM   3315 C CA  . GLU   A 1 431 ? 4.991   -8.049  -21.395 1.00 34.98  ? 968  GLU   A CA  1 
ATOM   3316 C C   . GLU   A 1 431 ? 6.142   -7.282  -20.753 1.00 33.30  ? 968  GLU   A C   1 
ATOM   3317 O O   . GLU   A 1 431 ? 7.010   -7.874  -20.114 1.00 29.73  ? 968  GLU   A O   1 
ATOM   3318 C CB  . GLU   A 1 431 ? 5.269   -8.216  -22.898 1.00 41.89  ? 968  GLU   A CB  1 
ATOM   3319 C CG  . GLU   A 1 431 ? 4.156   -8.853  -23.727 1.00 63.09  ? 968  GLU   A CG  1 
ATOM   3320 C CD  . GLU   A 1 431 ? 4.112   -10.373 -23.646 1.00 80.03  ? 968  GLU   A CD  1 
ATOM   3321 O OE1 . GLU   A 1 431 ? 3.434   -10.990 -24.501 1.00 74.49  ? 968  GLU   A OE1 1 
ATOM   3322 O OE2 . GLU   A 1 431 ? 4.746   -10.951 -22.735 1.00 88.53  ? 968  GLU   A OE2 1 
ATOM   3323 N N   . ILE   A 1 432 ? 6.144   -5.965  -20.914 1.00 28.11  ? 969  ILE   A N   1 
ATOM   3324 C CA  . ILE   A 1 432 ? 7.187   -5.144  -20.284 1.00 29.97  ? 969  ILE   A CA  1 
ATOM   3325 C C   . ILE   A 1 432 ? 7.092   -5.189  -18.756 1.00 28.38  ? 969  ILE   A C   1 
ATOM   3326 O O   . ILE   A 1 432 ? 8.097   -5.380  -18.073 1.00 31.69  ? 969  ILE   A O   1 
ATOM   3327 C CB  . ILE   A 1 432 ? 7.115   -3.685  -20.763 1.00 36.71  ? 969  ILE   A CB  1 
ATOM   3328 C CG1 . ILE   A 1 432 ? 7.229   -3.635  -22.290 1.00 34.40  ? 969  ILE   A CG1 1 
ATOM   3329 C CG2 . ILE   A 1 432 ? 8.224   -2.856  -20.109 1.00 36.59  ? 969  ILE   A CG2 1 
ATOM   3330 C CD1 . ILE   A 1 432 ? 6.863   -2.303  -22.898 1.00 42.65  ? 969  ILE   A CD1 1 
ATOM   3331 N N   . THR   A 1 433 ? 5.892   -5.036  -18.200 1.00 34.10  ? 970  THR   A N   1 
ATOM   3332 C CA  . THR   A 1 433 ? 5.766   -5.071  -16.741 1.00 29.25  ? 970  THR   A CA  1 
ATOM   3333 C C   . THR   A 1 433 ? 6.116   -6.441  -16.160 1.00 33.96  ? 970  THR   A C   1 
ATOM   3334 O O   . THR   A 1 433 ? 6.554   -6.537  -15.021 1.00 30.72  ? 970  THR   A O   1 
ATOM   3335 C CB  . THR   A 1 433 ? 4.348   -4.669  -16.266 1.00 29.41  ? 970  THR   A CB  1 
ATOM   3336 O OG1 . THR   A 1 433 ? 3.363   -5.547  -16.831 1.00 29.90  ? 970  THR   A OG1 1 
ATOM   3337 C CG2 . THR   A 1 433 ? 4.048   -3.230  -16.666 1.00 31.63  ? 970  THR   A CG2 1 
ATOM   3338 N N   . GLY   A 1 434 ? 5.946   -7.505  -16.944 1.00 31.15  ? 971  GLY   A N   1 
ATOM   3339 C CA  . GLY   A 1 434 ? 6.340   -8.833  -16.491 1.00 36.61  ? 971  GLY   A CA  1 
ATOM   3340 C C   . GLY   A 1 434 ? 7.836   -8.949  -16.235 1.00 40.03  ? 971  GLY   A C   1 
ATOM   3341 O O   . GLY   A 1 434 ? 8.279   -9.705  -15.365 1.00 37.18  ? 971  GLY   A O   1 
ATOM   3342 N N   . GLU   A 1 435 ? 8.613   -8.191  -17.004 1.00 31.34  ? 972  GLU   A N   1 
ATOM   3343 C CA  . GLU   A 1 435 ? 10.064  -8.192  -16.887 1.00 32.38  ? 972  GLU   A CA  1 
ATOM   3344 C C   . GLU   A 1 435 ? 10.494  -7.552  -15.576 1.00 37.59  ? 972  GLU   A C   1 
ATOM   3345 O O   . GLU   A 1 435 ? 11.456  -7.992  -14.946 1.00 35.76  ? 972  GLU   A O   1 
ATOM   3346 C CB  . GLU   A 1 435 ? 10.705  -7.447  -18.058 1.00 40.52  ? 972  GLU   A CB  1 
ATOM   3347 C CG  . GLU   A 1 435 ? 10.479  -8.083  -19.424 1.00 50.85  ? 972  GLU   A CG  1 
ATOM   3348 C CD  . GLU   A 1 435 ? 11.238  -7.367  -20.540 1.00 72.57  ? 972  GLU   A CD  1 
ATOM   3349 O OE1 . GLU   A 1 435 ? 10.782  -6.292  -20.997 1.00 72.54  ? 972  GLU   A OE1 1 
ATOM   3350 O OE2 . GLU   A 1 435 ? 12.298  -7.880  -20.959 1.00 83.83  ? 972  GLU   A OE2 1 
ATOM   3351 N N   . ILE   A 1 436 ? 9.781   -6.503  -15.177 1.00 32.04  ? 973  ILE   A N   1 
ATOM   3352 C CA  . ILE   A 1 436 ? 10.056  -5.828  -13.910 1.00 35.13  ? 973  ILE   A CA  1 
ATOM   3353 C C   . ILE   A 1 436 ? 9.868   -6.803  -12.755 1.00 41.20  ? 973  ILE   A C   1 
ATOM   3354 O O   . ILE   A 1 436 ? 10.682  -6.874  -11.837 1.00 38.62  ? 973  ILE   A O   1 
ATOM   3355 C CB  . ILE   A 1 436 ? 9.138   -4.604  -13.722 1.00 36.34  ? 973  ILE   A CB  1 
ATOM   3356 C CG1 . ILE   A 1 436 ? 9.398   -3.581  -14.832 1.00 43.28  ? 973  ILE   A CG1 1 
ATOM   3357 C CG2 . ILE   A 1 436 ? 9.347   -3.975  -12.347 1.00 36.59  ? 973  ILE   A CG2 1 
ATOM   3358 C CD1 . ILE   A 1 436 ? 8.437   -2.410  -14.834 1.00 41.41  ? 973  ILE   A CD1 1 
ATOM   3359 N N   . GLN   A 1 437 ? 8.803   -7.592  -12.832 1.00 43.02  ? 974  GLN   A N   1 
ATOM   3360 C CA  . GLN   A 1 437 ? 8.450   -8.491  -11.742 1.00 40.02  ? 974  GLN   A CA  1 
ATOM   3361 C C   . GLN   A 1 437 ? 9.485   -9.572  -11.464 1.00 41.68  ? 974  GLN   A C   1 
ATOM   3362 O O   . GLN   A 1 437 ? 9.599   -10.035 -10.331 1.00 42.54  ? 974  GLN   A O   1 
ATOM   3363 C CB  . GLN   A 1 437 ? 7.090   -9.137  -12.024 1.00 42.34  ? 974  GLN   A CB  1 
ATOM   3364 C CG  . GLN   A 1 437 ? 5.945   -8.153  -11.886 1.00 45.43  ? 974  GLN   A CG  1 
ATOM   3365 C CD  . GLN   A 1 437 ? 4.585   -8.799  -12.027 1.00 47.85  ? 974  GLN   A CD  1 
ATOM   3366 O OE1 . GLN   A 1 437 ? 4.229   -9.288  -13.097 1.00 47.35  ? 974  GLN   A OE1 1 
ATOM   3367 N NE2 . GLN   A 1 437 ? 3.812   -8.797  -10.944 1.00 44.64  ? 974  GLN   A NE2 1 
ATOM   3368 N N   . GLN   A 1 438 ? 10.254  -9.973  -12.471 1.00 43.93  ? 975  GLN   A N   1 
ATOM   3369 C CA  . GLN   A 1 438 ? 11.142  -11.118 -12.282 1.00 51.04  ? 975  GLN   A CA  1 
ATOM   3370 C C   . GLN   A 1 438 ? 12.289  -10.805 -11.315 1.00 52.08  ? 975  GLN   A C   1 
ATOM   3371 O O   . GLN   A 1 438 ? 12.972  -11.713 -10.853 1.00 46.34  ? 975  GLN   A O   1 
ATOM   3372 C CB  . GLN   A 1 438 ? 11.693  -11.613 -13.628 1.00 55.71  ? 975  GLN   A CB  1 
ATOM   3373 C CG  . GLN   A 1 438 ? 12.665  -10.672 -14.301 1.00 66.66  ? 975  GLN   A CG  1 
ATOM   3374 C CD  . GLN   A 1 438 ? 13.290  -11.257 -15.558 1.00 70.61  ? 975  GLN   A CD  1 
ATOM   3375 O OE1 . GLN   A 1 438 ? 14.119  -12.165 -15.486 1.00 70.11  ? 975  GLN   A OE1 1 
ATOM   3376 N NE2 . GLN   A 1 438 ? 12.902  -10.730 -16.717 1.00 67.36  ? 975  GLN   A NE2 1 
ATOM   3377 N N   . TYR   A 1 439 ? 12.475  -9.527  -10.979 1.00 51.23  ? 976  TYR   A N   1 
ATOM   3378 C CA  . TYR   A 1 439 ? 13.554  -9.126  -10.068 1.00 45.22  ? 976  TYR   A CA  1 
ATOM   3379 C C   . TYR   A 1 439 ? 13.066  -8.654  -8.687  1.00 40.25  ? 976  TYR   A C   1 
ATOM   3380 O O   . TYR   A 1 439 ? 13.855  -8.140  -7.890  1.00 41.29  ? 976  TYR   A O   1 
ATOM   3381 C CB  . TYR   A 1 439 ? 14.397  -8.016  -10.713 1.00 45.15  ? 976  TYR   A CB  1 
ATOM   3382 C CG  . TYR   A 1 439 ? 15.041  -8.410  -12.027 1.00 43.99  ? 976  TYR   A CG  1 
ATOM   3383 C CD1 . TYR   A 1 439 ? 16.169  -9.227  -12.056 1.00 48.86  ? 976  TYR   A CD1 1 
ATOM   3384 C CD2 . TYR   A 1 439 ? 14.529  -7.959  -13.238 1.00 50.85  ? 976  TYR   A CD2 1 
ATOM   3385 C CE1 . TYR   A 1 439 ? 16.762  -9.594  -13.254 1.00 52.64  ? 976  TYR   A CE1 1 
ATOM   3386 C CE2 . TYR   A 1 439 ? 15.120  -8.317  -14.448 1.00 52.60  ? 976  TYR   A CE2 1 
ATOM   3387 C CZ  . TYR   A 1 439 ? 16.233  -9.138  -14.448 1.00 55.58  ? 976  TYR   A CZ  1 
ATOM   3388 O OH  . TYR   A 1 439 ? 16.818  -9.497  -15.643 1.00 53.02  ? 976  TYR   A OH  1 
ATOM   3389 N N   . GLN   A 1 440 ? 11.784  -8.850  -8.394  1.00 44.14  ? 977  GLN   A N   1 
ATOM   3390 C CA  . GLN   A 1 440 ? 11.186  -8.286  -7.185  1.00 41.26  ? 977  GLN   A CA  1 
ATOM   3391 C C   . GLN   A 1 440 ? 11.192  -9.197  -5.953  1.00 48.35  ? 977  GLN   A C   1 
ATOM   3392 O O   . GLN   A 1 440 ? 10.770  -8.790  -4.870  1.00 46.40  ? 977  GLN   A O   1 
ATOM   3393 C CB  . GLN   A 1 440 ? 9.745   -7.852  -7.485  1.00 38.33  ? 977  GLN   A CB  1 
ATOM   3394 C CG  . GLN   A 1 440 ? 9.662   -6.554  -8.290  1.00 35.45  ? 977  GLN   A CG  1 
ATOM   3395 C CD  . GLN   A 1 440 ? 8.244   -6.140  -8.591  1.00 36.48  ? 977  GLN   A CD  1 
ATOM   3396 O OE1 . GLN   A 1 440 ? 7.378   -6.984  -8.826  1.00 38.66  ? 977  GLN   A OE1 1 
ATOM   3397 N NE2 . GLN   A 1 440 ? 7.991   -4.836  -8.581  1.00 34.34  ? 977  GLN   A NE2 1 
ATOM   3398 N N   . ASN   A 1 441 ? 11.669  -10.421 -6.092  1.00 48.78  ? 978  ASN   A N   1 
ATOM   3399 C CA  . ASN   A 1 441 ? 11.697  -11.305 -4.935  1.00 59.83  ? 978  ASN   A CA  1 
ATOM   3400 C C   . ASN   A 1 441 ? 13.123  -11.724 -4.614  1.00 56.58  ? 978  ASN   A C   1 
ATOM   3401 O O   . ASN   A 1 441 ? 13.422  -12.910 -4.504  1.00 57.51  ? 978  ASN   A O   1 
ATOM   3402 C CB  . ASN   A 1 441 ? 10.810  -12.532 -5.171  1.00 72.06  ? 978  ASN   A CB  1 
ATOM   3403 C CG  . ASN   A 1 441 ? 9.815   -12.328 -6.312  1.00 85.45  ? 978  ASN   A CG  1 
ATOM   3404 O OD1 . ASN   A 1 441 ? 8.781   -11.672 -6.149  1.00 85.70  ? 978  ASN   A OD1 1 
ATOM   3405 N ND2 . ASN   A 1 441 ? 10.130  -12.889 -7.478  1.00 86.97  ? 978  ASN   A ND2 1 
ATOM   3406 N N   . GLN   A 1 442 ? 14.002  -10.737 -4.456  1.00 56.13  ? 979  GLN   A N   1 
ATOM   3407 C CA  . GLN   A 1 442 ? 15.420  -10.999 -4.229  1.00 58.95  ? 979  GLN   A CA  1 
ATOM   3408 C C   . GLN   A 1 442 ? 15.983  -10.157 -3.086  1.00 46.68  ? 979  GLN   A C   1 
ATOM   3409 O O   . GLN   A 1 442 ? 16.606  -9.119  -3.328  1.00 42.17  ? 979  GLN   A O   1 
ATOM   3410 C CB  . GLN   A 1 442 ? 16.223  -10.720 -5.500  1.00 65.09  ? 979  GLN   A CB  1 
ATOM   3411 C CG  . GLN   A 1 442 ? 15.740  -11.464 -6.735  1.00 67.38  ? 979  GLN   A CG  1 
ATOM   3412 C CD  . GLN   A 1 442 ? 16.390  -10.948 -8.005  1.00 68.36  ? 979  GLN   A CD  1 
ATOM   3413 O OE1 . GLN   A 1 442 ? 17.309  -10.124 -7.957  1.00 63.68  ? 979  GLN   A OE1 1 
ATOM   3414 N NE2 . GLN   A 1 442 ? 15.920  -11.430 -9.149  1.00 67.50  ? 979  GLN   A NE2 1 
ATOM   3415 N N   . PRO   A 1 443 ? 15.771  -10.599 -1.838  1.00 41.53  ? 980  PRO   A N   1 
ATOM   3416 C CA  . PRO   A 1 443 ? 16.250  -9.871  -0.659  1.00 42.72  ? 980  PRO   A CA  1 
ATOM   3417 C C   . PRO   A 1 443 ? 17.769  -9.839  -0.549  1.00 40.86  ? 980  PRO   A C   1 
ATOM   3418 O O   . PRO   A 1 443 ? 18.434  -10.817 -0.879  1.00 38.70  ? 980  PRO   A O   1 
ATOM   3419 C CB  . PRO   A 1 443 ? 15.651  -10.661 0.507   1.00 55.46  ? 980  PRO   A CB  1 
ATOM   3420 C CG  . PRO   A 1 443 ? 15.457  -12.032 -0.036  1.00 54.04  ? 980  PRO   A CG  1 
ATOM   3421 C CD  . PRO   A 1 443 ? 15.056  -11.830 -1.468  1.00 47.89  ? 980  PRO   A CD  1 
ATOM   3422 N N   . TYR   A 1 444 ? 18.302  -8.712  -0.079  1.00 36.36  ? 981  TYR   A N   1 
ATOM   3423 C CA  . TYR   A 1 444 ? 19.732  -8.578  0.193   1.00 33.20  ? 981  TYR   A CA  1 
ATOM   3424 C C   . TYR   A 1 444 ? 20.089  -9.091  1.585   1.00 35.69  ? 981  TYR   A C   1 
ATOM   3425 O O   . TYR   A 1 444 ? 19.343  -8.897  2.543   1.00 36.46  ? 981  TYR   A O   1 
ATOM   3426 C CB  . TYR   A 1 444 ? 20.176  -7.113  0.066   1.00 31.80  ? 981  TYR   A CB  1 
ATOM   3427 C CG  . TYR   A 1 444 ? 20.410  -6.675  -1.362  1.00 29.77  ? 981  TYR   A CG  1 
ATOM   3428 C CD1 . TYR   A 1 444 ? 19.356  -6.243  -2.154  1.00 30.27  ? 981  TYR   A CD1 1 
ATOM   3429 C CD2 . TYR   A 1 444 ? 21.687  -6.700  -1.915  1.00 32.28  ? 981  TYR   A CD2 1 
ATOM   3430 C CE1 . TYR   A 1 444 ? 19.556  -5.857  -3.461  1.00 29.76  ? 981  TYR   A CE1 1 
ATOM   3431 C CE2 . TYR   A 1 444 ? 21.901  -6.307  -3.225  1.00 29.08  ? 981  TYR   A CE2 1 
ATOM   3432 C CZ  . TYR   A 1 444 ? 20.833  -5.884  -3.990  1.00 30.21  ? 981  TYR   A CZ  1 
ATOM   3433 O OH  . TYR   A 1 444 ? 21.030  -5.493  -5.293  1.00 32.67  ? 981  TYR   A OH  1 
ATOM   3434 N N   . CYS   A 1 445 ? 21.253  -9.717  1.690   1.00 32.52  ? 982  CYS   A N   1 
ATOM   3435 C CA  . CYS   A 1 445 ? 21.758  -10.173 2.973   1.00 38.79  ? 982  CYS   A CA  1 
ATOM   3436 C C   . CYS   A 1 445 ? 22.508  -9.030  3.648   1.00 37.34  ? 982  CYS   A C   1 
ATOM   3437 O O   . CYS   A 1 445 ? 23.711  -9.111  3.889   1.00 35.73  ? 982  CYS   A O   1 
ATOM   3438 C CB  . CYS   A 1 445 ? 22.659  -11.394 2.788   1.00 41.73  ? 982  CYS   A CB  1 
ATOM   3439 S SG  . CYS   A 1 445 ? 23.108  -12.207 4.336   1.00 51.86  ? 982  CYS   A SG  1 
ATOM   3440 N N   . LEU   A 1 446 ? 21.784  -7.949  3.926   1.00 32.47  ? 983  LEU   A N   1 
ATOM   3441 C CA  . LEU   A 1 446 ? 22.365  -6.749  4.524   1.00 27.93  ? 983  LEU   A CA  1 
ATOM   3442 C C   . LEU   A 1 446 ? 21.441  -6.273  5.629   1.00 31.60  ? 983  LEU   A C   1 
ATOM   3443 O O   . LEU   A 1 446 ? 20.222  -6.294  5.465   1.00 33.43  ? 983  LEU   A O   1 
ATOM   3444 C CB  . LEU   A 1 446 ? 22.560  -5.648  3.476   1.00 29.61  ? 983  LEU   A CB  1 
ATOM   3445 C CG  . LEU   A 1 446 ? 23.496  -5.947  2.304   1.00 34.14  ? 983  LEU   A CG  1 
ATOM   3446 C CD1 . LEU   A 1 446 ? 23.333  -4.909  1.196   1.00 31.42  ? 983  LEU   A CD1 1 
ATOM   3447 C CD2 . LEU   A 1 446 ? 24.945  -6.001  2.775   1.00 34.84  ? 983  LEU   A CD2 1 
ATOM   3448 N N   . ARG   A 1 447 ? 22.019  -5.867  6.753   1.00 31.59  ? 984  ARG   A N   1 
ATOM   3449 C CA  . ARG   A 1 447 ? 21.246  -5.389  7.887   1.00 34.39  ? 984  ARG   A CA  1 
ATOM   3450 C C   . ARG   A 1 447 ? 20.893  -3.910  7.715   1.00 32.39  ? 984  ARG   A C   1 
ATOM   3451 O O   . ARG   A 1 447 ? 21.732  -3.110  7.291   1.00 31.75  ? 984  ARG   A O   1 
ATOM   3452 C CB  . ARG   A 1 447 ? 22.025  -5.617  9.183   1.00 39.18  ? 984  ARG   A CB  1 
ATOM   3453 C CG  . ARG   A 1 447 ? 21.219  -5.369  10.440  1.00 46.52  ? 984  ARG   A CG  1 
ATOM   3454 C CD  . ARG   A 1 447 ? 22.047  -5.661  11.683  1.00 53.88  ? 984  ARG   A CD  1 
ATOM   3455 N NE  . ARG   A 1 447 ? 22.595  -7.016  11.680  1.00 58.22  ? 984  ARG   A NE  1 
ATOM   3456 C CZ  . ARG   A 1 447 ? 21.913  -8.103  12.031  1.00 55.29  ? 984  ARG   A CZ  1 
ATOM   3457 N NH1 . ARG   A 1 447 ? 20.645  -8.003  12.403  1.00 48.23  ? 984  ARG   A NH1 1 
ATOM   3458 N NH2 . ARG   A 1 447 ? 22.498  -9.293  12.001  1.00 56.84  ? 984  ARG   A NH2 1 
ATOM   3459 N N   . ILE   A 1 448 ? 19.645  -3.556  8.010   1.00 29.95  ? 985  ILE   A N   1 
ATOM   3460 C CA  . ILE   A 1 448 ? 19.205  -2.160  7.945   1.00 26.84  ? 985  ILE   A CA  1 
ATOM   3461 C C   . ILE   A 1 448 ? 19.810  -1.364  9.101   1.00 33.09  ? 985  ILE   A C   1 
ATOM   3462 O O   . ILE   A 1 448 ? 19.870  -1.863  10.232  1.00 35.49  ? 985  ILE   A O   1 
ATOM   3463 C CB  . ILE   A 1 448 ? 17.657  -2.053  7.990   1.00 38.85  ? 985  ILE   A CB  1 
ATOM   3464 C CG1 . ILE   A 1 448 ? 17.047  -2.611  6.708   1.00 48.12  ? 985  ILE   A CG1 1 
ATOM   3465 C CG2 . ILE   A 1 448 ? 17.196  -0.612  8.192   1.00 35.19  ? 985  ILE   A CG2 1 
ATOM   3466 C CD1 . ILE   A 1 448 ? 15.530  -2.533  6.670   1.00 55.64  ? 985  ILE   A CD1 1 
ATOM   3467 N N   . GLU   A 1 449 ? 20.287  -0.153  8.805   1.00 29.66  ? 986  GLU   A N   1 
ATOM   3468 C CA  . GLU   A 1 449 ? 20.682  0.809   9.829   1.00 26.81  ? 986  GLU   A CA  1 
ATOM   3469 C C   . GLU   A 1 449 ? 19.572  1.853   9.904   1.00 27.86  ? 986  GLU   A C   1 
ATOM   3470 O O   . GLU   A 1 449 ? 19.434  2.664   8.987   1.00 30.54  ? 986  GLU   A O   1 
ATOM   3471 C CB  . GLU   A 1 449 ? 22.036  1.449   9.488   1.00 29.89  ? 986  GLU   A CB  1 
ATOM   3472 C CG  . GLU   A 1 449 ? 22.873  1.884   10.687  1.00 33.06  ? 986  GLU   A CG  1 
ATOM   3473 C CD  . GLU   A 1 449 ? 22.158  2.888   11.571  1.00 38.82  ? 986  GLU   A CD  1 
ATOM   3474 O OE1 . GLU   A 1 449 ? 22.194  2.725   12.817  1.00 37.74  ? 986  GLU   A OE1 1 
ATOM   3475 O OE2 . GLU   A 1 449 ? 21.554  3.836   11.019  1.00 38.84  ? 986  GLU   A OE2 1 
ATOM   3476 N N   . PRO   A 1 450 ? 18.754  1.821   10.976  1.00 31.59  ? 987  PRO   A N   1 
ATOM   3477 C CA  . PRO   A 1 450 ? 17.529  2.635   11.005  1.00 31.83  ? 987  PRO   A CA  1 
ATOM   3478 C C   . PRO   A 1 450 ? 17.760  4.144   10.846  1.00 35.82  ? 987  PRO   A C   1 
ATOM   3479 O O   . PRO   A 1 450 ? 17.019  4.776   10.093  1.00 33.92  ? 987  PRO   A O   1 
ATOM   3480 C CB  . PRO   A 1 450 ? 16.928  2.311   12.382  1.00 35.10  ? 987  PRO   A CB  1 
ATOM   3481 C CG  . PRO   A 1 450 ? 17.426  0.945   12.683  1.00 44.96  ? 987  PRO   A CG  1 
ATOM   3482 C CD  . PRO   A 1 450 ? 18.829  0.907   12.130  1.00 34.91  ? 987  PRO   A CD  1 
ATOM   3483 N N   . ASP   A 1 451 ? 18.759  4.714   11.517  1.00 33.47  ? 988  ASP   A N   1 
ATOM   3484 C CA  . ASP   A 1 451 ? 19.031  6.150   11.375  1.00 30.24  ? 988  ASP   A CA  1 
ATOM   3485 C C   . ASP   A 1 451 ? 19.486  6.510   9.957   1.00 27.59  ? 988  ASP   A C   1 
ATOM   3486 O O   . ASP   A 1 451 ? 19.065  7.526   9.398   1.00 29.52  ? 988  ASP   A O   1 
ATOM   3487 C CB  . ASP   A 1 451 ? 20.102  6.602   12.370  1.00 30.27  ? 988  ASP   A CB  1 
ATOM   3488 C CG  . ASP   A 1 451 ? 19.594  6.663   13.803  1.00 39.72  ? 988  ASP   A CG  1 
ATOM   3489 O OD1 . ASP   A 1 451 ? 18.386  6.894   14.010  1.00 39.30  ? 988  ASP   A OD1 1 
ATOM   3490 O OD2 . ASP   A 1 451 ? 20.421  6.499   14.725  1.00 41.03  ? 988  ASP   A OD2 1 
ATOM   3491 N N   . MET   A 1 452 ? 20.367  5.695   9.387   1.00 24.99  ? 989  MET   A N   1 
ATOM   3492 C CA  . MET   A 1 452 ? 20.823  5.946   8.017   1.00 25.46  ? 989  MET   A CA  1 
ATOM   3493 C C   . MET   A 1 452 ? 19.669  5.784   7.018   1.00 27.31  ? 989  MET   A C   1 
ATOM   3494 O O   . MET   A 1 452 ? 19.562  6.532   6.055   1.00 27.84  ? 989  MET   A O   1 
ATOM   3495 C CB  . MET   A 1 452 ? 21.976  5.016   7.642   1.00 27.26  ? 989  MET   A CB  1 
ATOM   3496 C CG  . MET   A 1 452 ? 23.263  5.297   8.406   1.00 26.55  ? 989  MET   A CG  1 
ATOM   3497 S SD  . MET   A 1 452 ? 24.595  4.216   7.847   1.00 30.74  ? 989  MET   A SD  1 
ATOM   3498 C CE  . MET   A 1 452 ? 24.782  4.720   6.116   1.00 26.25  ? 989  MET   A CE  1 
ATOM   3499 N N   . ARG   A 1 453 ? 18.809  4.802   7.254   1.00 27.85  ? 990  ARG   A N   1 
ATOM   3500 C CA  . ARG   A 1 453 ? 17.609  4.631   6.429   1.00 26.55  ? 990  ARG   A CA  1 
ATOM   3501 C C   . ARG   A 1 453 ? 16.737  5.895   6.438   1.00 29.40  ? 990  ARG   A C   1 
ATOM   3502 O O   . ARG   A 1 453 ? 16.322  6.373   5.382   1.00 28.12  ? 990  ARG   A O   1 
ATOM   3503 C CB  . ARG   A 1 453 ? 16.797  3.430   6.909   1.00 26.02  ? 990  ARG   A CB  1 
ATOM   3504 C CG  . ARG   A 1 453 ? 15.475  3.222   6.181   1.00 33.94  ? 990  ARG   A CG  1 
ATOM   3505 C CD  . ARG   A 1 453 ? 15.692  2.947   4.702   1.00 38.45  ? 990  ARG   A CD  1 
ATOM   3506 N NE  . ARG   A 1 453 ? 14.565  2.215   4.137   1.00 44.68  ? 990  ARG   A NE  1 
ATOM   3507 C CZ  . ARG   A 1 453 ? 14.581  0.924   3.814   1.00 45.19  ? 990  ARG   A CZ  1 
ATOM   3508 N NH1 . ARG   A 1 453 ? 15.683  0.198   3.967   1.00 32.10  ? 990  ARG   A NH1 1 
ATOM   3509 N NH2 . ARG   A 1 453 ? 13.484  0.361   3.318   1.00 42.97  ? 990  ARG   A NH2 1 
ATOM   3510 N N   . ARG   A 1 454 ? 16.469  6.436   7.626   1.00 29.22  ? 991  ARG   A N   1 
ATOM   3511 C CA  . ARG   A 1 454 ? 15.669  7.655   7.740   1.00 27.91  ? 991  ARG   A CA  1 
ATOM   3512 C C   . ARG   A 1 454 ? 16.355  8.816   7.034   1.00 33.64  ? 991  ARG   A C   1 
ATOM   3513 O O   . ARG   A 1 454 ? 15.698  9.618   6.369   1.00 32.23  ? 991  ARG   A O   1 
ATOM   3514 C CB  . ARG   A 1 454 ? 15.407  8.021   9.207   1.00 30.32  ? 991  ARG   A CB  1 
ATOM   3515 C CG  . ARG   A 1 454 ? 14.320  7.193   9.876   1.00 42.50  ? 991  ARG   A CG  1 
ATOM   3516 C CD  . ARG   A 1 454 ? 14.058  7.643   11.318  1.00 48.18  ? 991  ARG   A CD  1 
ATOM   3517 N NE  . ARG   A 1 454 ? 15.047  7.120   12.260  1.00 54.94  ? 991  ARG   A NE  1 
ATOM   3518 C CZ  . ARG   A 1 454 ? 14.965  5.928   12.847  1.00 52.27  ? 991  ARG   A CZ  1 
ATOM   3519 N NH1 . ARG   A 1 454 ? 13.939  5.128   12.586  1.00 46.57  ? 991  ARG   A NH1 1 
ATOM   3520 N NH2 . ARG   A 1 454 ? 15.910  5.531   13.689  1.00 42.79  ? 991  ARG   A NH2 1 
ATOM   3521 N N   . PHE   A 1 455 ? 17.676  8.897   7.167   1.00 24.93  ? 992  PHE   A N   1 
ATOM   3522 C CA  . PHE   A 1 455 ? 18.441  9.961   6.514   1.00 24.87  ? 992  PHE   A CA  1 
ATOM   3523 C C   . PHE   A 1 455 ? 18.213  9.947   5.005   1.00 28.75  ? 992  PHE   A C   1 
ATOM   3524 O O   . PHE   A 1 455 ? 17.959  10.988  4.395   1.00 28.81  ? 992  PHE   A O   1 
ATOM   3525 C CB  . PHE   A 1 455 ? 19.932  9.816   6.825   1.00 23.62  ? 992  PHE   A CB  1 
ATOM   3526 C CG  . PHE   A 1 455 ? 20.806  10.830  6.137   1.00 26.61  ? 992  PHE   A CG  1 
ATOM   3527 C CD1 . PHE   A 1 455 ? 20.919  12.127  6.633   1.00 32.63  ? 992  PHE   A CD1 1 
ATOM   3528 C CD2 . PHE   A 1 455 ? 21.541  10.482  5.014   1.00 28.28  ? 992  PHE   A CD2 1 
ATOM   3529 C CE1 . PHE   A 1 455 ? 21.742  13.058  6.009   1.00 32.31  ? 992  PHE   A CE1 1 
ATOM   3530 C CE2 . PHE   A 1 455 ? 22.363  11.407  4.390   1.00 32.43  ? 992  PHE   A CE2 1 
ATOM   3531 C CZ  . PHE   A 1 455 ? 22.463  12.702  4.892   1.00 28.54  ? 992  PHE   A CZ  1 
ATOM   3532 N N   . PHE   A 1 456 ? 18.276  8.765   4.400   1.00 26.83  ? 993  PHE   A N   1 
ATOM   3533 C CA  . PHE   A 1 456 ? 18.144  8.697   2.950   1.00 26.63  ? 993  PHE   A CA  1 
ATOM   3534 C C   . PHE   A 1 456 ? 16.687  8.820   2.510   1.00 33.60  ? 993  PHE   A C   1 
ATOM   3535 O O   . PHE   A 1 456 ? 16.412  9.352   1.442   1.00 28.51  ? 993  PHE   A O   1 
ATOM   3536 C CB  . PHE   A 1 456 ? 18.804  7.424   2.429   1.00 26.92  ? 993  PHE   A CB  1 
ATOM   3537 C CG  . PHE   A 1 456 ? 20.306  7.490   2.510   1.00 22.91  ? 993  PHE   A CG  1 
ATOM   3538 C CD1 . PHE   A 1 456 ? 20.993  8.457   1.788   1.00 23.65  ? 993  PHE   A CD1 1 
ATOM   3539 C CD2 . PHE   A 1 456 ? 21.023  6.637   3.335   1.00 28.13  ? 993  PHE   A CD2 1 
ATOM   3540 C CE1 . PHE   A 1 456 ? 22.374  8.563   1.865   1.00 28.10  ? 993  PHE   A CE1 1 
ATOM   3541 C CE2 . PHE   A 1 456 ? 22.415  6.733   3.411   1.00 32.10  ? 993  PHE   A CE2 1 
ATOM   3542 C CZ  . PHE   A 1 456 ? 23.082  7.701   2.676   1.00 30.32  ? 993  PHE   A CZ  1 
ATOM   3543 N N   . GLU   A 1 457 ? 15.753  8.370   3.340   1.00 27.60  ? 994  GLU   A N   1 
ATOM   3544 C CA  . GLU   A 1 457 ? 14.335  8.554   3.019   1.00 26.74  ? 994  GLU   A CA  1 
ATOM   3545 C C   . GLU   A 1 457 ? 13.938  10.032  3.044   1.00 31.41  ? 994  GLU   A C   1 
ATOM   3546 O O   . GLU   A 1 457 ? 13.046  10.469  2.311   1.00 35.83  ? 994  GLU   A O   1 
ATOM   3547 C CB  . GLU   A 1 457 ? 13.460  7.764   3.998   1.00 32.48  ? 994  GLU   A CB  1 
ATOM   3548 C CG  . GLU   A 1 457 ? 13.441  6.276   3.719   1.00 36.48  ? 994  GLU   A CG  1 
ATOM   3549 C CD  . GLU   A 1 457 ? 12.773  5.458   4.821   1.00 48.73  ? 994  GLU   A CD  1 
ATOM   3550 O OE1 . GLU   A 1 457 ? 12.577  5.970   5.951   1.00 45.61  ? 994  GLU   A OE1 1 
ATOM   3551 O OE2 . GLU   A 1 457 ? 12.448  4.286   4.546   1.00 41.70  ? 994  GLU   A OE2 1 
ATOM   3552 N N   . ASN   A 1 458 ? 14.597  10.796  3.902   1.00 31.22  ? 995  ASN   A N   1 
ATOM   3553 C CA  . ASN   A 1 458 ? 14.230  12.183  4.120   1.00 34.17  ? 995  ASN   A CA  1 
ATOM   3554 C C   . ASN   A 1 458 ? 15.075  13.209  3.352   1.00 33.97  ? 995  ASN   A C   1 
ATOM   3555 O O   . ASN   A 1 458 ? 14.912  14.413  3.564   1.00 33.77  ? 995  ASN   A O   1 
ATOM   3556 C CB  . ASN   A 1 458 ? 14.301  12.492  5.612   1.00 41.86  ? 995  ASN   A CB  1 
ATOM   3557 C CG  . ASN   A 1 458 ? 13.323  11.659  6.422   1.00 45.12  ? 995  ASN   A CG  1 
ATOM   3558 O OD1 . ASN   A 1 458 ? 12.296  11.210  5.904   1.00 44.54  ? 995  ASN   A OD1 1 
ATOM   3559 N ND2 . ASN   A 1 458 ? 13.644  11.434  7.695   1.00 41.13  ? 995  ASN   A ND2 1 
ATOM   3560 N N   . LEU   A 1 459 ? 15.968  12.749  2.471   1.00 28.74  ? 996  LEU   A N   1 
ATOM   3561 C CA  . LEU   A 1 459 ? 16.804  13.666  1.682   1.00 30.44  ? 996  LEU   A CA  1 
ATOM   3562 C C   . LEU   A 1 459 ? 15.954  14.699  0.959   1.00 30.26  ? 996  LEU   A C   1 
ATOM   3563 O O   . LEU   A 1 459 ? 14.987  14.341  0.282   1.00 28.85  ? 996  LEU   A O   1 
ATOM   3564 C CB  . LEU   A 1 459 ? 17.640  12.917  0.640   1.00 34.40  ? 996  LEU   A CB  1 
ATOM   3565 C CG  . LEU   A 1 459 ? 18.980  12.285  1.016   1.00 39.89  ? 996  LEU   A CG  1 
ATOM   3566 C CD1 . LEU   A 1 459 ? 19.659  11.785  -0.254  1.00 40.60  ? 996  LEU   A CD1 1 
ATOM   3567 C CD2 . LEU   A 1 459 ? 19.867  13.259  1.772   1.00 41.55  ? 996  LEU   A CD2 1 
ATOM   3568 N N   . ASN   A 1 460 ? 16.314  15.970  1.114   1.00 25.57  ? 997  ASN   A N   1 
ATOM   3569 C CA  . ASN   A 1 460 ? 15.594  17.061  0.448   1.00 27.68  ? 997  ASN   A CA  1 
ATOM   3570 C C   . ASN   A 1 460 ? 16.563  18.093  -0.099  1.00 31.87  ? 997  ASN   A C   1 
ATOM   3571 O O   . ASN   A 1 460 ? 16.652  19.212  0.405   1.00 32.77  ? 997  ASN   A O   1 
ATOM   3572 C CB  . ASN   A 1 460 ? 14.602  17.741  1.399   1.00 32.98  ? 997  ASN   A CB  1 
ATOM   3573 C CG  . ASN   A 1 460 ? 13.775  18.807  0.697   1.00 34.79  ? 997  ASN   A CG  1 
ATOM   3574 O OD1 . ASN   A 1 460 ? 13.286  18.593  -0.414  1.00 46.05  ? 997  ASN   A OD1 1 
ATOM   3575 N ND2 . ASN   A 1 460 ? 13.650  19.969  1.320   1.00 44.20  ? 997  ASN   A ND2 1 
ATOM   3576 N N   . PRO   A 1 461 ? 17.299  17.722  -1.152  1.00 24.36  ? 998  PRO   A N   1 
ATOM   3577 C CA  . PRO   A 1 461 ? 18.314  18.642  -1.669  1.00 21.67  ? 998  PRO   A CA  1 
ATOM   3578 C C   . PRO   A 1 461 ? 17.752  19.989  -2.132  1.00 25.96  ? 998  PRO   A C   1 
ATOM   3579 O O   . PRO   A 1 461 ? 18.452  20.995  -2.018  1.00 27.34  ? 998  PRO   A O   1 
ATOM   3580 C CB  . PRO   A 1 461 ? 18.920  17.874  -2.849  1.00 22.19  ? 998  PRO   A CB  1 
ATOM   3581 C CG  . PRO   A 1 461 ? 17.899  16.822  -3.205  1.00 27.98  ? 998  PRO   A CG  1 
ATOM   3582 C CD  . PRO   A 1 461 ? 17.220  16.469  -1.922  1.00 25.11  ? 998  PRO   A CD  1 
ATOM   3583 N N   . MET   A 1 462 ? 16.522  20.017  -2.639  1.00 26.01  ? 999  MET   A N   1 
ATOM   3584 C CA  . MET   A 1 462 ? 15.985  21.245  -3.211  1.00 27.12  ? 999  MET   A CA  1 
ATOM   3585 C C   . MET   A 1 462 ? 15.603  22.265  -2.150  1.00 25.64  ? 999  MET   A C   1 
ATOM   3586 O O   . MET   A 1 462 ? 15.512  23.449  -2.444  1.00 31.46  ? 999  MET   A O   1 
ATOM   3587 C CB  . MET   A 1 462 ? 14.773  20.948  -4.097  1.00 26.49  ? 999  MET   A CB  1 
ATOM   3588 C CG  . MET   A 1 462 ? 15.150  20.297  -5.419  1.00 29.84  ? 999  MET   A CG  1 
ATOM   3589 S SD  . MET   A 1 462 ? 13.714  19.932  -6.442  1.00 45.36  ? 999  MET   A SD  1 
ATOM   3590 C CE  . MET   A 1 462 ? 13.417  18.210  -6.051  1.00 57.26  ? 999  MET   A CE  1 
ATOM   3591 N N   . GLY   A 1 463 ? 15.388  21.809  -0.917  1.00 29.42  ? 1000 GLY   A N   1 
ATOM   3592 C CA  . GLY   A 1 463 ? 14.931  22.700  0.140   1.00 31.94  ? 1000 GLY   A CA  1 
ATOM   3593 C C   . GLY   A 1 463 ? 13.596  23.323  -0.230  1.00 31.55  ? 1000 GLY   A C   1 
ATOM   3594 O O   . GLY   A 1 463 ? 12.638  22.611  -0.535  1.00 33.74  ? 1000 GLY   A O   1 
ATOM   3595 N N   . SER   A 1 464 ? 13.532  24.652  -0.227  1.00 28.01  ? 1001 SER   A N   1 
ATOM   3596 C CA  . SER   A 1 464 ? 12.297  25.338  -0.588  1.00 31.12  ? 1001 SER   A CA  1 
ATOM   3597 C C   . SER   A 1 464 ? 12.213  25.662  -2.075  1.00 33.57  ? 1001 SER   A C   1 
ATOM   3598 O O   . SER   A 1 464 ? 11.204  26.197  -2.548  1.00 33.64  ? 1001 SER   A O   1 
ATOM   3599 C CB  . SER   A 1 464 ? 12.156  26.629  0.220   1.00 34.13  ? 1001 SER   A CB  1 
ATOM   3600 O OG  . SER   A 1 464 ? 11.792  26.340  1.556   1.00 47.55  ? 1001 SER   A OG  1 
ATOM   3601 N N   . ALA   A 1 465 ? 13.268  25.348  -2.817  1.00 29.28  ? 1002 ALA   A N   1 
ATOM   3602 C CA  . ALA   A 1 465 ? 13.306  25.722  -4.227  1.00 29.12  ? 1002 ALA   A CA  1 
ATOM   3603 C C   . ALA   A 1 465 ? 12.453  24.807  -5.100  1.00 30.31  ? 1002 ALA   A C   1 
ATOM   3604 O O   . ALA   A 1 465 ? 12.264  23.626  -4.798  1.00 31.85  ? 1002 ALA   A O   1 
ATOM   3605 C CB  . ALA   A 1 465 ? 14.762  25.733  -4.731  1.00 30.52  ? 1002 ALA   A CB  1 
ATOM   3606 N N   . SER   A 1 466 ? 11.937  25.361  -6.192  1.00 33.38  ? 1003 SER   A N   1 
ATOM   3607 C CA  . SER   A 1 466 ? 11.331  24.545  -7.234  1.00 38.56  ? 1003 SER   A CA  1 
ATOM   3608 C C   . SER   A 1 466 ? 12.444  23.786  -7.950  1.00 31.36  ? 1003 SER   A C   1 
ATOM   3609 O O   . SER   A 1 466 ? 13.629  24.129  -7.817  1.00 30.83  ? 1003 SER   A O   1 
ATOM   3610 C CB  . SER   A 1 466 ? 10.550  25.410  -8.224  1.00 42.85  ? 1003 SER   A CB  1 
ATOM   3611 O OG  . SER   A 1 466 ? 11.440  26.243  -8.961  1.00 36.75  ? 1003 SER   A OG  1 
ATOM   3612 N N   . GLU   A 1 467 ? 12.085  22.751  -8.703  1.00 31.85  ? 1004 GLU   A N   1 
ATOM   3613 C CA  . GLU   A 1 467 ? 13.101  22.002  -9.432  1.00 31.04  ? 1004 GLU   A CA  1 
ATOM   3614 C C   . GLU   A 1 467 ? 13.822  22.926  -10.415 1.00 27.71  ? 1004 GLU   A C   1 
ATOM   3615 O O   . GLU   A 1 467 ? 15.037  22.842  -10.573 1.00 31.59  ? 1004 GLU   A O   1 
ATOM   3616 C CB  . GLU   A 1 467 ? 12.493  20.802  -10.162 1.00 42.52  ? 1004 GLU   A CB  1 
ATOM   3617 C CG  . GLU   A 1 467 ? 13.541  19.942  -10.883 1.00 50.59  ? 1004 GLU   A CG  1 
ATOM   3618 C CD  . GLU   A 1 467 ? 13.194  18.455  -10.909 1.00 64.13  ? 1004 GLU   A CD  1 
ATOM   3619 O OE1 . GLU   A 1 467 ? 13.739  17.730  -11.772 1.00 62.99  ? 1004 GLU   A OE1 1 
ATOM   3620 O OE2 . GLU   A 1 467 ? 12.394  18.005  -10.060 1.00 70.30  ? 1004 GLU   A OE2 1 
ATOM   3621 N N   . LYS   A 1 468 ? 13.072  23.826  -11.048 1.00 37.48  ? 1005 LYS   A N   1 
ATOM   3622 C CA  . LYS   A 1 468 ? 13.663  24.814  -11.954 1.00 38.30  ? 1005 LYS   A CA  1 
ATOM   3623 C C   . LYS   A 1 468 ? 14.612  25.746  -11.212 1.00 30.43  ? 1005 LYS   A C   1 
ATOM   3624 O O   . LYS   A 1 468 ? 15.734  26.000  -11.665 1.00 32.28  ? 1005 LYS   A O   1 
ATOM   3625 C CB  . LYS   A 1 468 ? 12.579  25.645  -12.652 1.00 39.12  ? 1005 LYS   A CB  1 
ATOM   3626 C CG  . LYS   A 1 468 ? 13.141  26.824  -13.455 1.00 42.88  ? 1005 LYS   A CG  1 
ATOM   3627 C CD  . LYS   A 1 468 ? 13.663  26.357  -14.810 1.00 60.48  ? 1005 LYS   A CD  1 
ATOM   3628 C CE  . LYS   A 1 468 ? 14.907  27.119  -15.250 1.00 63.67  ? 1005 LYS   A CE  1 
ATOM   3629 N NZ  . LYS   A 1 468 ? 16.019  26.168  -15.579 1.00 60.14  ? 1005 LYS   A NZ  1 
ATOM   3630 N N   . GLU   A 1 469 ? 14.155  26.269  -10.081 1.00 29.25  ? 1006 GLU   A N   1 
ATOM   3631 C CA  . GLU   A 1 469 ? 14.992  27.150  -9.284  1.00 27.65  ? 1006 GLU   A CA  1 
ATOM   3632 C C   . GLU   A 1 469 ? 16.257  26.431  -8.838  1.00 29.18  ? 1006 GLU   A C   1 
ATOM   3633 O O   . GLU   A 1 469 ? 17.339  27.013  -8.855  1.00 25.94  ? 1006 GLU   A O   1 
ATOM   3634 C CB  . GLU   A 1 469 ? 14.233  27.679  -8.068  1.00 27.07  ? 1006 GLU   A CB  1 
ATOM   3635 C CG  . GLU   A 1 469 ? 13.230  28.755  -8.422  1.00 29.00  ? 1006 GLU   A CG  1 
ATOM   3636 C CD  . GLU   A 1 469 ? 12.307  29.102  -7.270  1.00 38.92  ? 1006 GLU   A CD  1 
ATOM   3637 O OE1 . GLU   A 1 469 ? 12.072  28.231  -6.408  1.00 38.03  ? 1006 GLU   A OE1 1 
ATOM   3638 O OE2 . GLU   A 1 469 ? 11.812  30.248  -7.236  1.00 37.91  ? 1006 GLU   A OE2 1 
ATOM   3639 N N   . PHE   A 1 470 ? 16.122  25.166  -8.442  1.00 25.16  ? 1007 PHE   A N   1 
ATOM   3640 C CA  . PHE   A 1 470 ? 17.265  24.436  -7.917  1.00 23.76  ? 1007 PHE   A CA  1 
ATOM   3641 C C   . PHE   A 1 470 ? 18.260  24.106  -9.035  1.00 25.99  ? 1007 PHE   A C   1 
ATOM   3642 O O   . PHE   A 1 470 ? 19.470  24.171  -8.841  1.00 25.52  ? 1007 PHE   A O   1 
ATOM   3643 C CB  . PHE   A 1 470 ? 16.835  23.155  -7.211  1.00 25.66  ? 1007 PHE   A CB  1 
ATOM   3644 C CG  . PHE   A 1 470 ? 17.959  22.488  -6.468  1.00 24.27  ? 1007 PHE   A CG  1 
ATOM   3645 C CD1 . PHE   A 1 470 ? 18.528  23.095  -5.351  1.00 27.13  ? 1007 PHE   A CD1 1 
ATOM   3646 C CD2 . PHE   A 1 470 ? 18.468  21.272  -6.898  1.00 26.12  ? 1007 PHE   A CD2 1 
ATOM   3647 C CE1 . PHE   A 1 470 ? 19.577  22.485  -4.669  1.00 27.74  ? 1007 PHE   A CE1 1 
ATOM   3648 C CE2 . PHE   A 1 470 ? 19.509  20.659  -6.224  1.00 27.47  ? 1007 PHE   A CE2 1 
ATOM   3649 C CZ  . PHE   A 1 470 ? 20.067  21.266  -5.110  1.00 30.74  ? 1007 PHE   A CZ  1 
ATOM   3650 N N   . THR   A 1 471 ? 17.732  23.769  -10.205 1.00 26.51  ? 1008 THR   A N   1 
ATOM   3651 C CA  . THR   A 1 471 ? 18.552  23.553  -11.396 1.00 28.54  ? 1008 THR   A CA  1 
ATOM   3652 C C   . THR   A 1 471 ? 19.407  24.781  -11.723 1.00 26.05  ? 1008 THR   A C   1 
ATOM   3653 O O   . THR   A 1 471 ? 20.609  24.668  -11.965 1.00 26.59  ? 1008 THR   A O   1 
ATOM   3654 C CB  . THR   A 1 471 ? 17.665  23.209  -12.603 1.00 31.83  ? 1008 THR   A CB  1 
ATOM   3655 O OG1 . THR   A 1 471 ? 16.953  22.001  -12.324 1.00 33.99  ? 1008 THR   A OG1 1 
ATOM   3656 C CG2 . THR   A 1 471 ? 18.501  23.022  -13.862 1.00 34.56  ? 1008 THR   A CG2 1 
ATOM   3657 N N   . ASP   A 1 472 ? 18.789  25.955  -11.719 1.00 25.97  ? 1009 ASP   A N   1 
ATOM   3658 C CA  . ASP   A 1 472 ? 19.525  27.184  -11.965 1.00 26.67  ? 1009 ASP   A CA  1 
ATOM   3659 C C   . ASP   A 1 472 ? 20.550  27.411  -10.862 1.00 25.67  ? 1009 ASP   A C   1 
ATOM   3660 O O   . ASP   A 1 472 ? 21.682  27.805  -11.133 1.00 26.37  ? 1009 ASP   A O   1 
ATOM   3661 C CB  . ASP   A 1 472 ? 18.585  28.389  -12.053 1.00 28.58  ? 1009 ASP   A CB  1 
ATOM   3662 C CG  . ASP   A 1 472 ? 17.670  28.329  -13.250 1.00 36.35  ? 1009 ASP   A CG  1 
ATOM   3663 O OD1 . ASP   A 1 472 ? 17.931  27.520  -14.167 1.00 33.27  ? 1009 ASP   A OD1 1 
ATOM   3664 O OD2 . ASP   A 1 472 ? 16.683  29.099  -13.270 1.00 37.75  ? 1009 ASP   A OD2 1 
ATOM   3665 N N   . TYR   A 1 473 ? 20.153  27.164  -9.617  1.00 26.74  ? 1010 TYR   A N   1 
ATOM   3666 C CA  . TYR   A 1 473 ? 21.080  27.315  -8.495  1.00 22.96  ? 1010 TYR   A CA  1 
ATOM   3667 C C   . TYR   A 1 473 ? 22.335  26.463  -8.688  1.00 22.75  ? 1010 TYR   A C   1 
ATOM   3668 O O   . TYR   A 1 473 ? 23.451  26.955  -8.529  1.00 25.95  ? 1010 TYR   A O   1 
ATOM   3669 C CB  . TYR   A 1 473 ? 20.409  26.952  -7.169  1.00 26.32  ? 1010 TYR   A CB  1 
ATOM   3670 C CG  . TYR   A 1 473 ? 21.403  26.722  -6.049  1.00 31.54  ? 1010 TYR   A CG  1 
ATOM   3671 C CD1 . TYR   A 1 473 ? 22.020  27.795  -5.407  1.00 32.09  ? 1010 TYR   A CD1 1 
ATOM   3672 C CD2 . TYR   A 1 473 ? 21.742  25.435  -5.653  1.00 26.01  ? 1010 TYR   A CD2 1 
ATOM   3673 C CE1 . TYR   A 1 473 ? 22.941  27.590  -4.388  1.00 35.39  ? 1010 TYR   A CE1 1 
ATOM   3674 C CE2 . TYR   A 1 473 ? 22.667  25.215  -4.632  1.00 30.56  ? 1010 TYR   A CE2 1 
ATOM   3675 C CZ  . TYR   A 1 473 ? 23.262  26.301  -4.009  1.00 37.74  ? 1010 TYR   A CZ  1 
ATOM   3676 O OH  . TYR   A 1 473 ? 24.174  26.087  -2.992  1.00 36.36  ? 1010 TYR   A OH  1 
ATOM   3677 N N   . LEU   A 1 474 ? 22.151  25.188  -9.023  1.00 21.29  ? 1011 LEU   A N   1 
ATOM   3678 C CA  . LEU   A 1 474 ? 23.300  24.315  -9.249  1.00 20.71  ? 1011 LEU   A CA  1 
ATOM   3679 C C   . LEU   A 1 474 ? 24.197  24.863  -10.346 1.00 26.44  ? 1011 LEU   A C   1 
ATOM   3680 O O   . LEU   A 1 474 ? 25.425  24.841  -10.220 1.00 24.47  ? 1011 LEU   A O   1 
ATOM   3681 C CB  . LEU   A 1 474 ? 22.861  22.903  -9.633  1.00 24.66  ? 1011 LEU   A CB  1 
ATOM   3682 C CG  . LEU   A 1 474 ? 22.148  22.057  -8.581  1.00 29.33  ? 1011 LEU   A CG  1 
ATOM   3683 C CD1 . LEU   A 1 474 ? 21.614  20.791  -9.222  1.00 30.44  ? 1011 LEU   A CD1 1 
ATOM   3684 C CD2 . LEU   A 1 474 ? 23.086  21.728  -7.444  1.00 27.30  ? 1011 LEU   A CD2 1 
ATOM   3685 N N   . PHE   A 1 475 ? 23.597  25.355  -11.428 1.00 24.42  ? 1012 PHE   A N   1 
ATOM   3686 C CA  . PHE   A 1 475 ? 24.432  25.765  -12.550 1.00 22.36  ? 1012 PHE   A CA  1 
ATOM   3687 C C   . PHE   A 1 475 ? 25.230  27.005  -12.201 1.00 24.56  ? 1012 PHE   A C   1 
ATOM   3688 O O   . PHE   A 1 475 ? 26.415  27.125  -12.542 1.00 25.72  ? 1012 PHE   A O   1 
ATOM   3689 C CB  . PHE   A 1 475 ? 23.606  26.020  -13.820 1.00 22.49  ? 1012 PHE   A CB  1 
ATOM   3690 C CG  . PHE   A 1 475 ? 24.463  26.022  -15.066 1.00 27.19  ? 1012 PHE   A CG  1 
ATOM   3691 C CD1 . PHE   A 1 475 ? 24.827  24.815  -15.674 1.00 24.33  ? 1012 PHE   A CD1 1 
ATOM   3692 C CD2 . PHE   A 1 475 ? 24.983  27.211  -15.567 1.00 24.79  ? 1012 PHE   A CD2 1 
ATOM   3693 C CE1 . PHE   A 1 475 ? 25.655  24.801  -16.790 1.00 27.97  ? 1012 PHE   A CE1 1 
ATOM   3694 C CE2 . PHE   A 1 475 ? 25.816  27.205  -16.691 1.00 26.56  ? 1012 PHE   A CE2 1 
ATOM   3695 C CZ  . PHE   A 1 475 ? 26.150  25.999  -17.300 1.00 28.78  ? 1012 PHE   A CZ  1 
ATOM   3696 N N   . ASN   A 1 476 ? 24.585  27.940  -11.513 1.00 24.16  ? 1013 ASN   A N   1 
ATOM   3697 C CA  . ASN   A 1 476 ? 25.273  29.165  -11.169 1.00 28.36  ? 1013 ASN   A CA  1 
ATOM   3698 C C   . ASN   A 1 476 ? 26.361  28.903  -10.138 1.00 26.89  ? 1013 ASN   A C   1 
ATOM   3699 O O   . ASN   A 1 476 ? 27.396  29.562  -10.172 1.00 28.34  ? 1013 ASN   A O   1 
ATOM   3700 C CB  . ASN   A 1 476 ? 24.273  30.220  -10.696 1.00 30.66  ? 1013 ASN   A CB  1 
ATOM   3701 C CG  . ASN   A 1 476 ? 23.428  30.747  -11.853 1.00 32.64  ? 1013 ASN   A CG  1 
ATOM   3702 O OD1 . ASN   A 1 476 ? 23.955  31.036  -12.924 1.00 29.73  ? 1013 ASN   A OD1 1 
ATOM   3703 N ND2 . ASN   A 1 476 ? 22.113  30.814  -11.661 1.00 29.70  ? 1013 ASN   A ND2 1 
ATOM   3704 N N   . LYS   A 1 477 ? 26.149  27.926  -9.258  1.00 27.11  ? 1014 LYS   A N   1 
ATOM   3705 C CA  . LYS   A 1 477 ? 27.191  27.544  -8.303  1.00 26.93  ? 1014 LYS   A CA  1 
ATOM   3706 C C   . LYS   A 1 477 ? 28.374  26.916  -9.050  1.00 25.84  ? 1014 LYS   A C   1 
ATOM   3707 O O   . LYS   A 1 477 ? 29.538  27.188  -8.737  1.00 24.95  ? 1014 LYS   A O   1 
ATOM   3708 C CB  . LYS   A 1 477 ? 26.636  26.593  -7.242  1.00 32.66  ? 1014 LYS   A CB  1 
ATOM   3709 C CG  . LYS   A 1 477 ? 27.631  26.194  -6.156  1.00 37.20  ? 1014 LYS   A CG  1 
ATOM   3710 C CD  . LYS   A 1 477 ? 28.238  27.389  -5.441  1.00 35.65  ? 1014 LYS   A CD  1 
ATOM   3711 C CE  . LYS   A 1 477 ? 27.294  27.941  -4.399  1.00 42.43  ? 1014 LYS   A CE  1 
ATOM   3712 N NZ  . LYS   A 1 477 ? 27.952  29.058  -3.644  1.00 43.91  ? 1014 LYS   A NZ  1 
ATOM   3713 N N   . SER   A 1 478 ? 28.065  26.094  -10.052 1.00 23.47  ? 1015 SER   A N   1 
ATOM   3714 C CA  . SER   A 1 478 ? 29.092  25.489  -10.908 1.00 25.67  ? 1015 SER   A CA  1 
ATOM   3715 C C   . SER   A 1 478 ? 29.939  26.573  -11.582 1.00 25.65  ? 1015 SER   A C   1 
ATOM   3716 O O   . SER   A 1 478 ? 31.168  26.481  -11.645 1.00 25.32  ? 1015 SER   A O   1 
ATOM   3717 C CB  . SER   A 1 478 ? 28.434  24.589  -11.961 1.00 24.58  ? 1015 SER   A CB  1 
ATOM   3718 O OG  . SER   A 1 478 ? 29.403  23.965  -12.800 1.00 26.08  ? 1015 SER   A OG  1 
ATOM   3719 N N   . LEU   A 1 479 ? 29.275  27.613  -12.076 1.00 26.68  ? 1016 LEU   A N   1 
ATOM   3720 C CA  . LEU   A 1 479 ? 29.978  28.714  -12.744 1.00 26.23  ? 1016 LEU   A CA  1 
ATOM   3721 C C   . LEU   A 1 479 ? 30.863  29.468  -11.761 1.00 24.88  ? 1016 LEU   A C   1 
ATOM   3722 O O   . LEU   A 1 479 ? 31.914  29.986  -12.137 1.00 29.58  ? 1016 LEU   A O   1 
ATOM   3723 C CB  . LEU   A 1 479 ? 28.990  29.685  -13.391 1.00 27.06  ? 1016 LEU   A CB  1 
ATOM   3724 C CG  . LEU   A 1 479 ? 28.264  29.202  -14.649 1.00 27.51  ? 1016 LEU   A CG  1 
ATOM   3725 C CD1 . LEU   A 1 479 ? 27.228  30.238  -15.065 1.00 28.33  ? 1016 LEU   A CD1 1 
ATOM   3726 C CD2 . LEU   A 1 479 ? 29.256  28.968  -15.771 1.00 26.47  ? 1016 LEU   A CD2 1 
ATOM   3727 N N   . GLU   A 1 480 ? 30.425  29.532  -10.508 1.00 27.49  ? 1017 GLU   A N   1 
ATOM   3728 C CA  . GLU   A 1 480 ? 31.201  30.200  -9.466  1.00 28.72  ? 1017 GLU   A CA  1 
ATOM   3729 C C   . GLU   A 1 480 ? 32.473  29.421  -9.117  1.00 28.84  ? 1017 GLU   A C   1 
ATOM   3730 O O   . GLU   A 1 480 ? 33.567  30.000  -9.026  1.00 28.81  ? 1017 GLU   A O   1 
ATOM   3731 C CB  . GLU   A 1 480 ? 30.341  30.399  -8.216  1.00 32.63  ? 1017 GLU   A CB  1 
ATOM   3732 C CG  . GLU   A 1 480 ? 31.105  30.989  -7.042  1.00 39.81  ? 1017 GLU   A CG  1 
ATOM   3733 C CD  . GLU   A 1 480 ? 30.250  31.149  -5.797  1.00 52.63  ? 1017 GLU   A CD  1 
ATOM   3734 O OE1 . GLU   A 1 480 ? 29.075  30.718  -5.813  1.00 51.62  ? 1017 GLU   A OE1 1 
ATOM   3735 O OE2 . GLU   A 1 480 ? 30.760  31.710  -4.801  1.00 57.02  ? 1017 GLU   A OE2 1 
ATOM   3736 N N   . ILE   A 1 481 ? 32.352  28.109  -8.941  1.00 27.12  ? 1018 ILE   A N   1 
ATOM   3737 C CA  . ILE   A 1 481 ? 33.512  27.333  -8.505  1.00 25.56  ? 1018 ILE   A CA  1 
ATOM   3738 C C   . ILE   A 1 481 ? 34.490  27.004  -9.633  1.00 26.92  ? 1018 ILE   A C   1 
ATOM   3739 O O   . ILE   A 1 481 ? 35.675  26.810  -9.362  1.00 28.64  ? 1018 ILE   A O   1 
ATOM   3740 C CB  . ILE   A 1 481 ? 33.098  26.023  -7.812  1.00 26.80  ? 1018 ILE   A CB  1 
ATOM   3741 C CG1 . ILE   A 1 481 ? 32.270  25.135  -8.749  1.00 25.34  ? 1018 ILE   A CG1 1 
ATOM   3742 C CG2 . ILE   A 1 481 ? 32.320  26.328  -6.556  1.00 27.17  ? 1018 ILE   A CG2 1 
ATOM   3743 C CD1 . ILE   A 1 481 ? 31.763  23.843  -8.083  1.00 26.08  ? 1018 ILE   A CD1 1 
ATOM   3744 N N   . GLU   A 1 482 ? 34.007  26.922  -10.872 1.00 24.54  ? 1019 GLU   A N   1 
ATOM   3745 C CA  . GLU   A 1 482 ? 34.896  26.780  -12.031 1.00 24.61  ? 1019 GLU   A CA  1 
ATOM   3746 C C   . GLU   A 1 482 ? 34.384  27.651  -13.174 1.00 27.45  ? 1019 GLU   A C   1 
ATOM   3747 O O   . GLU   A 1 482 ? 33.661  27.185  -14.045 1.00 27.83  ? 1019 GLU   A O   1 
ATOM   3748 C CB  . GLU   A 1 482 ? 35.027  25.314  -12.497 1.00 26.04  ? 1019 GLU   A CB  1 
ATOM   3749 C CG  . GLU   A 1 482 ? 35.719  24.411  -11.475 1.00 23.52  ? 1019 GLU   A CG  1 
ATOM   3750 C CD  . GLU   A 1 482 ? 36.108  23.020  -12.001 1.00 32.54  ? 1019 GLU   A CD  1 
ATOM   3751 O OE1 . GLU   A 1 482 ? 36.213  22.822  -13.237 1.00 30.57  ? 1019 GLU   A OE1 1 
ATOM   3752 O OE2 . GLU   A 1 482 ? 36.341  22.115  -11.160 1.00 27.97  ? 1019 GLU   A OE2 1 
ATOM   3753 N N   . PRO   A 1 483 ? 34.759  28.940  -13.172 1.00 29.72  ? 1020 PRO   A N   1 
ATOM   3754 C CA  . PRO   A 1 483 ? 34.280  29.873  -14.203 1.00 28.75  ? 1020 PRO   A CA  1 
ATOM   3755 C C   . PRO   A 1 483 ? 34.661  29.440  -15.609 1.00 31.94  ? 1020 PRO   A C   1 
ATOM   3756 O O   . PRO   A 1 483 ? 35.648  28.727  -15.768 1.00 30.25  ? 1020 PRO   A O   1 
ATOM   3757 C CB  . PRO   A 1 483 ? 34.978  31.190  -13.837 1.00 28.78  ? 1020 PRO   A CB  1 
ATOM   3758 C CG  . PRO   A 1 483 ? 35.220  31.070  -12.347 1.00 27.12  ? 1020 PRO   A CG  1 
ATOM   3759 C CD  . PRO   A 1 483 ? 35.565  29.610  -12.140 1.00 33.82  ? 1020 PRO   A CD  1 
ATOM   3760 N N   . ARG   A 1 484 ? 33.875  29.852  -16.601 1.00 32.66  ? 1021 ARG   A N   1 
ATOM   3761 C CA  . ARG   A 1 484 ? 34.203  29.589  -17.997 1.00 30.71  ? 1021 ARG   A CA  1 
ATOM   3762 C C   . ARG   A 1 484 ? 35.589  30.134  -18.324 1.00 39.88  ? 1021 ARG   A C   1 
ATOM   3763 O O   . ARG   A 1 484 ? 35.945  31.231  -17.895 1.00 37.28  ? 1021 ARG   A O   1 
ATOM   3764 C CB  . ARG   A 1 484 ? 33.161  30.205  -18.939 1.00 35.50  ? 1021 ARG   A CB  1 
ATOM   3765 C CG  . ARG   A 1 484 ? 31.810  29.498  -18.934 1.00 38.87  ? 1021 ARG   A CG  1 
ATOM   3766 C CD  . ARG   A 1 484 ? 30.930  29.984  -20.086 1.00 42.13  ? 1021 ARG   A CD  1 
ATOM   3767 N NE  . ARG   A 1 484 ? 31.644  29.902  -21.358 1.00 43.55  ? 1021 ARG   A NE  1 
ATOM   3768 C CZ  . ARG   A 1 484 ? 32.013  30.955  -22.084 1.00 51.08  ? 1021 ARG   A CZ  1 
ATOM   3769 N NH1 . ARG   A 1 484 ? 31.720  32.188  -21.686 1.00 61.39  ? 1021 ARG   A NH1 1 
ATOM   3770 N NH2 . ARG   A 1 484 ? 32.670  30.771  -23.219 1.00 43.70  ? 1021 ARG   A NH2 1 
ATOM   3771 N N   . ASN   A 1 485 ? 36.359  29.353  -19.077 1.00 43.39  ? 1022 ASN   A N   1 
ATOM   3772 C CA  . ASN   A 1 485 ? 37.694  29.750  -19.519 1.00 50.43  ? 1022 ASN   A CA  1 
ATOM   3773 C C   . ASN   A 1 485 ? 38.645  30.079  -18.372 1.00 47.96  ? 1022 ASN   A C   1 
ATOM   3774 O O   . ASN   A 1 485 ? 39.481  30.971  -18.489 1.00 56.58  ? 1022 ASN   A O   1 
ATOM   3775 C CB  . ASN   A 1 485 ? 37.612  30.957  -20.456 1.00 48.43  ? 1022 ASN   A CB  1 
ATOM   3776 C CG  . ASN   A 1 485 ? 36.750  30.699  -21.671 1.00 52.67  ? 1022 ASN   A CG  1 
ATOM   3777 O OD1 . ASN   A 1 485 ? 35.970  31.560  -22.078 1.00 47.20  ? 1022 ASN   A OD1 1 
ATOM   3778 N ND2 . ASN   A 1 485 ? 36.883  29.512  -22.258 1.00 49.47  ? 1022 ASN   A ND2 1 
ATOM   3779 N N   . CYS   A 1 486 ? 38.504  29.385  -17.253 1.00 45.73  ? 1023 CYS   A N   1 
ATOM   3780 C CA  . CYS   A 1 486 ? 39.459  29.554  -16.173 1.00 43.73  ? 1023 CYS   A CA  1 
ATOM   3781 C C   . CYS   A 1 486 ? 40.503  28.463  -16.307 1.00 47.99  ? 1023 CYS   A C   1 
ATOM   3782 O O   . CYS   A 1 486 ? 40.166  27.288  -16.424 1.00 42.27  ? 1023 CYS   A O   1 
ATOM   3783 C CB  . CYS   A 1 486 ? 38.780  29.498  -14.807 1.00 53.29  ? 1023 CYS   A CB  1 
ATOM   3784 S SG  . CYS   A 1 486 ? 39.248  30.868  -13.721 1.00 90.69  ? 1023 CYS   A SG  1 
ATOM   3785 N N   . LYS   A 1 487 ? 41.773  28.848  -16.325 1.00 43.79  ? 1024 LYS   A N   1 
ATOM   3786 C CA  . LYS   A 1 487 ? 42.828  27.862  -16.502 1.00 56.75  ? 1024 LYS   A CA  1 
ATOM   3787 C C   . LYS   A 1 487 ? 43.104  27.133  -15.197 1.00 53.39  ? 1024 LYS   A C   1 
ATOM   3788 O O   . LYS   A 1 487 ? 43.557  25.989  -15.201 1.00 61.70  ? 1024 LYS   A O   1 
ATOM   3789 C CB  . LYS   A 1 487 ? 44.091  28.526  -17.048 1.00 74.51  ? 1024 LYS   A CB  1 
ATOM   3790 C CG  . LYS   A 1 487 ? 43.910  29.026  -18.474 1.00 88.67  ? 1024 LYS   A CG  1 
ATOM   3791 C CD  . LYS   A 1 487 ? 45.201  29.538  -19.082 1.00 98.79  ? 1024 LYS   A CD  1 
ATOM   3792 C CE  . LYS   A 1 487 ? 45.000  29.864  -20.554 1.00 103.91 ? 1024 LYS   A CE  1 
ATOM   3793 N NZ  . LYS   A 1 487 ? 46.236  30.401  -21.184 1.00 105.27 ? 1024 LYS   A NZ  1 
ATOM   3794 N N   . GLN   A 1 488 ? 42.817  27.791  -14.082 1.00 45.98  ? 1025 GLN   A N   1 
ATOM   3795 C CA  . GLN   A 1 488 ? 42.895  27.135  -12.781 1.00 64.56  ? 1025 GLN   A CA  1 
ATOM   3796 C C   . GLN   A 1 488 ? 41.714  27.521  -11.887 1.00 67.28  ? 1025 GLN   A C   1 
ATOM   3797 O O   . GLN   A 1 488 ? 41.369  28.702  -11.772 1.00 69.79  ? 1025 GLN   A O   1 
ATOM   3798 C CB  . GLN   A 1 488 ? 44.219  27.463  -12.085 1.00 70.31  ? 1025 GLN   A CB  1 
ATOM   3799 C CG  . GLN   A 1 488 ? 45.404  26.673  -12.628 1.00 83.51  ? 1025 GLN   A CG  1 
ATOM   3800 C CD  . GLN   A 1 488 ? 46.729  27.092  -12.010 1.00 98.56  ? 1025 GLN   A CD  1 
ATOM   3801 O OE1 . GLN   A 1 488 ? 46.822  28.127  -11.350 1.00 100.81 ? 1025 GLN   A OE1 1 
ATOM   3802 N NE2 . GLN   A 1 488 ? 47.764  26.285  -12.224 1.00 104.57 ? 1025 GLN   A NE2 1 
ATOM   3803 N N   . PRO   A 1 489 ? 41.095  26.515  -11.246 1.00 62.25  ? 1026 PRO   A N   1 
ATOM   3804 C CA  . PRO   A 1 489 ? 39.958  26.738  -10.346 1.00 63.80  ? 1026 PRO   A CA  1 
ATOM   3805 C C   . PRO   A 1 489 ? 40.353  27.664  -9.202  1.00 65.24  ? 1026 PRO   A C   1 
ATOM   3806 O O   . PRO   A 1 489 ? 41.352  27.391  -8.533  1.00 61.17  ? 1026 PRO   A O   1 
ATOM   3807 C CB  . PRO   A 1 489 ? 39.633  25.331  -9.833  1.00 67.56  ? 1026 PRO   A CB  1 
ATOM   3808 C CG  . PRO   A 1 489 ? 40.930  24.579  -9.948  1.00 66.15  ? 1026 PRO   A CG  1 
ATOM   3809 C CD  . PRO   A 1 489 ? 41.578  25.122  -11.192 1.00 59.36  ? 1026 PRO   A CD  1 
ATOM   3810 N N   . PRO   A 1 490 ? 39.594  28.750  -8.985  1.00 63.69  ? 1027 PRO   A N   1 
ATOM   3811 C CA  . PRO   A 1 490 ? 39.965  29.693  -7.927  1.00 64.93  ? 1027 PRO   A CA  1 
ATOM   3812 C C   . PRO   A 1 490 ? 39.939  29.032  -6.552  1.00 51.86  ? 1027 PRO   A C   1 
ATOM   3813 O O   . PRO   A 1 490 ? 39.283  27.999  -6.358  1.00 52.79  ? 1027 PRO   A O   1 
ATOM   3814 C CB  . PRO   A 1 490 ? 38.897  30.791  -8.031  1.00 68.17  ? 1027 PRO   A CB  1 
ATOM   3815 C CG  . PRO   A 1 490 ? 38.302  30.629  -9.395  1.00 66.45  ? 1027 PRO   A CG  1 
ATOM   3816 C CD  . PRO   A 1 490 ? 38.359  29.157  -9.673  1.00 62.43  ? 1027 PRO   A CD  1 
ATOM   3817 N N   . ARG   A 1 491 ? 40.670  29.628  -5.617  1.00 49.09  ? 1028 ARG   A N   1 
ATOM   3818 C CA  . ARG   A 1 491 ? 40.776  29.115  -4.263  1.00 48.91  ? 1028 ARG   A CA  1 
ATOM   3819 C C   . ARG   A 1 491 ? 39.563  29.506  -3.434  1.00 38.96  ? 1028 ARG   A C   1 
ATOM   3820 O O   . ARG   A 1 491 ? 39.205  30.679  -3.353  1.00 43.76  ? 1028 ARG   A O   1 
ATOM   3821 C CB  . ARG   A 1 491 ? 42.056  29.629  -3.594  1.00 53.91  ? 1028 ARG   A CB  1 
ATOM   3822 C CG  . ARG   A 1 491 ? 43.052  28.540  -3.237  1.00 70.96  ? 1028 ARG   A CG  1 
ATOM   3823 C CD  . ARG   A 1 491 ? 43.487  27.781  -4.486  1.00 77.30  ? 1028 ARG   A CD  1 
ATOM   3824 N NE  . ARG   A 1 491 ? 43.366  26.309  -4.518  1.00 82.76  ? 1028 ARG   A NE  1 
ATOM   3825 C CZ  . ARG   A 1 491 ? 42.777  25.494  -3.632  1.00 78.46  ? 1028 ARG   A CZ  1 
ATOM   3826 N NH1 . ARG   A 1 491 ? 42.160  25.918  -2.534  1.00 82.34  ? 1028 ARG   A NH1 1 
ATOM   3827 N NH2 . ARG   A 1 491 ? 42.790  24.194  -3.875  1.00 67.82  ? 1028 ARG   A NH2 1 
ATOM   3828 N N   . PHE   A 1 492 ? 38.926  28.511  -2.833  1.00 32.55  ? 1029 PHE   A N   1 
ATOM   3829 C CA  . PHE   A 1 492 ? 37.876  28.739  -1.860  1.00 28.96  ? 1029 PHE   A CA  1 
ATOM   3830 C C   . PHE   A 1 492 ? 38.296  28.032  -0.579  1.00 32.70  ? 1029 PHE   A C   1 
ATOM   3831 O O   . PHE   A 1 492 ? 38.915  26.971  -0.634  1.00 37.12  ? 1029 PHE   A O   1 
ATOM   3832 C CB  . PHE   A 1 492 ? 36.524  28.194  -2.348  1.00 31.13  ? 1029 PHE   A CB  1 
ATOM   3833 C CG  . PHE   A 1 492 ? 35.965  28.917  -3.529  1.00 32.06  ? 1029 PHE   A CG  1 
ATOM   3834 C CD1 . PHE   A 1 492 ? 36.274  28.513  -4.821  1.00 28.57  ? 1029 PHE   A CD1 1 
ATOM   3835 C CD2 . PHE   A 1 492 ? 35.117  29.998  -3.349  1.00 43.37  ? 1029 PHE   A CD2 1 
ATOM   3836 C CE1 . PHE   A 1 492 ? 35.744  29.179  -5.909  1.00 37.48  ? 1029 PHE   A CE1 1 
ATOM   3837 C CE2 . PHE   A 1 492 ? 34.584  30.668  -4.432  1.00 43.79  ? 1029 PHE   A CE2 1 
ATOM   3838 C CZ  . PHE   A 1 492 ? 34.899  30.259  -5.714  1.00 37.01  ? 1029 PHE   A CZ  1 
ATOM   3839 N N   . PRO   A 1 493 ? 37.961  28.613  0.577   1.00 38.32  ? 1030 PRO   A N   1 
ATOM   3840 C CA  . PRO   A 1 493 ? 38.353  28.039  1.869   1.00 35.72  ? 1030 PRO   A CA  1 
ATOM   3841 C C   . PRO   A 1 493 ? 37.693  26.696  2.164   1.00 45.57  ? 1030 PRO   A C   1 
ATOM   3842 O O   . PRO   A 1 493 ? 36.584  26.428  1.715   1.00 34.37  ? 1030 PRO   A O   1 
ATOM   3843 C CB  . PRO   A 1 493 ? 37.901  29.102  2.878   1.00 44.76  ? 1030 PRO   A CB  1 
ATOM   3844 C CG  . PRO   A 1 493 ? 36.873  29.916  2.166   1.00 44.18  ? 1030 PRO   A CG  1 
ATOM   3845 C CD  . PRO   A 1 493 ? 37.281  29.910  0.720   1.00 40.69  ? 1030 PRO   A CD  1 
ATOM   3846 N N   . ARG   A 1 494 ? 38.390  25.848  2.911   1.00 50.65  ? 1031 ARG   A N   1 
ATOM   3847 C CA  . ARG   A 1 494 ? 37.855  24.551  3.289   1.00 50.93  ? 1031 ARG   A CA  1 
ATOM   3848 C C   . ARG   A 1 494 ? 36.687  24.781  4.251   1.00 57.58  ? 1031 ARG   A C   1 
ATOM   3849 O O   . ARG   A 1 494 ? 36.713  25.711  5.055   1.00 51.50  ? 1031 ARG   A O   1 
ATOM   3850 C CB  . ARG   A 1 494 ? 38.956  23.682  3.919   1.00 62.13  ? 1031 ARG   A CB  1 
ATOM   3851 C CG  . ARG   A 1 494 ? 38.596  22.207  4.159   1.00 64.11  ? 1031 ARG   A CG  1 
ATOM   3852 C CD  . ARG   A 1 494 ? 39.009  21.279  3.009   1.00 59.34  ? 1031 ARG   A CD  1 
ATOM   3853 N NE  . ARG   A 1 494 ? 40.404  21.458  2.584   1.00 60.23  ? 1031 ARG   A NE  1 
ATOM   3854 C CZ  . ARG   A 1 494 ? 41.438  20.718  2.995   1.00 63.31  ? 1031 ARG   A CZ  1 
ATOM   3855 N NH1 . ARG   A 1 494 ? 41.265  19.728  3.865   1.00 44.10  ? 1031 ARG   A NH1 1 
ATOM   3856 N NH2 . ARG   A 1 494 ? 42.660  20.972  2.537   1.00 64.28  ? 1031 ARG   A NH2 1 
ATOM   3857 N N   . LYS   A 1 495 ? 35.659  23.950  4.155   1.00 52.22  ? 1032 LYS   A N   1 
ATOM   3858 C CA  . LYS   A 1 495 ? 34.461  24.131  4.963   1.00 61.20  ? 1032 LYS   A CA  1 
ATOM   3859 C C   . LYS   A 1 495 ? 34.507  23.270  6.227   1.00 56.35  ? 1032 LYS   A C   1 
ATOM   3860 O O   . LYS   A 1 495 ? 34.218  23.737  7.323   1.00 56.78  ? 1032 LYS   A O   1 
ATOM   3861 C CB  . LYS   A 1 495 ? 33.213  23.800  4.141   1.00 73.54  ? 1032 LYS   A CB  1 
ATOM   3862 C CG  . LYS   A 1 495 ? 31.939  24.397  4.702   1.00 79.91  ? 1032 LYS   A CG  1 
ATOM   3863 C CD  . LYS   A 1 495 ? 32.116  25.888  4.948   1.00 86.99  ? 1032 LYS   A CD  1 
ATOM   3864 C CE  . LYS   A 1 495 ? 30.869  26.514  5.556   1.00 93.56  ? 1032 LYS   A CE  1 
ATOM   3865 N NZ  . LYS   A 1 495 ? 29.729  26.545  4.599   1.00 95.48  ? 1032 LYS   A NZ  1 
ATOM   3866 N N   . SER   A 1 496 ? 34.882  22.011  6.064   1.00 46.15  ? 1033 SER   A N   1 
ATOM   3867 C CA  . SER   A 1 496 ? 34.934  21.080  7.179   1.00 58.35  ? 1033 SER   A CA  1 
ATOM   3868 C C   . SER   A 1 496 ? 36.352  20.941  7.692   1.00 55.22  ? 1033 SER   A C   1 
ATOM   3869 O O   . SER   A 1 496 ? 37.305  21.335  7.016   1.00 45.77  ? 1033 SER   A O   1 
ATOM   3870 C CB  . SER   A 1 496 ? 34.403  19.715  6.755   1.00 66.94  ? 1033 SER   A CB  1 
ATOM   3871 O OG  . SER   A 1 496 ? 35.144  19.206  5.656   1.00 68.15  ? 1033 SER   A OG  1 
ATOM   3872 N N   . THR   A 1 497 ? 36.496  20.371  8.883   1.00 53.66  ? 1034 THR   A N   1 
ATOM   3873 C CA  . THR   A 1 497 ? 37.822  20.171  9.450   1.00 60.21  ? 1034 THR   A CA  1 
ATOM   3874 C C   . THR   A 1 497 ? 38.241  18.707  9.451   1.00 59.57  ? 1034 THR   A C   1 
ATOM   3875 O O   . THR   A 1 497 ? 39.391  18.396  9.770   1.00 62.15  ? 1034 THR   A O   1 
ATOM   3876 C CB  . THR   A 1 497 ? 37.908  20.702  10.895  1.00 66.50  ? 1034 THR   A CB  1 
ATOM   3877 O OG1 . THR   A 1 497 ? 36.904  20.070  11.699  1.00 65.83  ? 1034 THR   A OG1 1 
ATOM   3878 C CG2 . THR   A 1 497 ? 37.706  22.205  10.923  1.00 62.86  ? 1034 THR   A CG2 1 
ATOM   3879 N N   . PHE   A 1 498 ? 37.325  17.802  9.111   1.00 48.51  ? 1035 PHE   A N   1 
ATOM   3880 C CA  . PHE   A 1 498 ? 37.675  16.386  9.162   1.00 46.90  ? 1035 PHE   A CA  1 
ATOM   3881 C C   . PHE   A 1 498 ? 38.565  15.998  7.985   1.00 47.90  ? 1035 PHE   A C   1 
ATOM   3882 O O   . PHE   A 1 498 ? 38.644  16.722  6.985   1.00 48.73  ? 1035 PHE   A O   1 
ATOM   3883 C CB  . PHE   A 1 498 ? 36.420  15.498  9.213   1.00 45.99  ? 1035 PHE   A CB  1 
ATOM   3884 C CG  . PHE   A 1 498 ? 35.366  15.845  8.197   1.00 65.53  ? 1035 PHE   A CG  1 
ATOM   3885 C CD1 . PHE   A 1 498 ? 35.554  15.574  6.846   1.00 72.54  ? 1035 PHE   A CD1 1 
ATOM   3886 C CD2 . PHE   A 1 498 ? 34.165  16.406  8.598   1.00 69.19  ? 1035 PHE   A CD2 1 
ATOM   3887 C CE1 . PHE   A 1 498 ? 34.574  15.885  5.907   1.00 62.06  ? 1035 PHE   A CE1 1 
ATOM   3888 C CE2 . PHE   A 1 498 ? 33.179  16.715  7.667   1.00 67.22  ? 1035 PHE   A CE2 1 
ATOM   3889 C CZ  . PHE   A 1 498 ? 33.386  16.455  6.320   1.00 61.37  ? 1035 PHE   A CZ  1 
ATOM   3890 N N   . SER   A 1 499 ? 39.255  14.868  8.131   1.00 39.58  ? 1036 SER   A N   1 
ATOM   3891 C CA  . SER   A 1 499 ? 40.053  14.298  7.053   1.00 37.79  ? 1036 SER   A CA  1 
ATOM   3892 C C   . SER   A 1 499 ? 39.202  14.120  5.800   1.00 39.69  ? 1036 SER   A C   1 
ATOM   3893 O O   . SER   A 1 499 ? 38.015  13.821  5.894   1.00 43.04  ? 1036 SER   A O   1 
ATOM   3894 C CB  . SER   A 1 499 ? 40.635  12.953  7.477   1.00 36.36  ? 1036 SER   A CB  1 
ATOM   3895 O OG  . SER   A 1 499 ? 41.417  12.379  6.441   1.00 37.87  ? 1036 SER   A OG  1 
ATOM   3896 N N   . LEU   A 1 500 ? 39.806  14.326  4.634   1.00 34.73  ? 1037 LEU   A N   1 
ATOM   3897 C CA  . LEU   A 1 500 ? 39.139  14.053  3.368   1.00 40.52  ? 1037 LEU   A CA  1 
ATOM   3898 C C   . LEU   A 1 500 ? 39.395  12.615  2.955   1.00 36.49  ? 1037 LEU   A C   1 
ATOM   3899 O O   . LEU   A 1 500 ? 38.827  12.132  1.976   1.00 39.04  ? 1037 LEU   A O   1 
ATOM   3900 C CB  . LEU   A 1 500 ? 39.634  15.001  2.275   1.00 35.79  ? 1037 LEU   A CB  1 
ATOM   3901 C CG  . LEU   A 1 500 ? 39.421  16.498  2.479   1.00 36.31  ? 1037 LEU   A CG  1 
ATOM   3902 C CD1 . LEU   A 1 500 ? 39.936  17.238  1.258   1.00 31.49  ? 1037 LEU   A CD1 1 
ATOM   3903 C CD2 . LEU   A 1 500 ? 37.944  16.798  2.720   1.00 46.11  ? 1037 LEU   A CD2 1 
ATOM   3904 N N   . LYS   A 1 501 ? 40.267  11.944  3.707   1.00 35.23  ? 1038 LYS   A N   1 
ATOM   3905 C CA  . LYS   A 1 501 ? 40.702  10.593  3.369   1.00 31.49  ? 1038 LYS   A CA  1 
ATOM   3906 C C   . LYS   A 1 501 ? 39.558  9.628   3.522   1.00 29.72  ? 1038 LYS   A C   1 
ATOM   3907 O O   . LYS   A 1 501 ? 38.878  9.614   4.547   1.00 32.72  ? 1038 LYS   A O   1 
ATOM   3908 C CB  . LYS   A 1 501 ? 41.876  10.143  4.242   1.00 32.73  ? 1038 LYS   A CB  1 
ATOM   3909 C CG  . LYS   A 1 501 ? 43.238  10.461  3.645   1.00 55.52  ? 1038 LYS   A CG  1 
ATOM   3910 C CD  . LYS   A 1 501 ? 44.360  10.293  4.664   1.00 67.67  ? 1038 LYS   A CD  1 
ATOM   3911 C CE  . LYS   A 1 501 ? 44.254  8.960   5.389   1.00 71.99  ? 1038 LYS   A CE  1 
ATOM   3912 N NZ  . LYS   A 1 501 ? 44.230  7.800   4.448   1.00 70.81  ? 1038 LYS   A NZ  1 
ATOM   3913 N N   . SER   A 1 502 ? 39.342  8.826   2.492   1.00 31.18  ? 1039 SER   A N   1 
ATOM   3914 C CA  . SER   A 1 502 ? 38.299  7.813   2.554   1.00 27.99  ? 1039 SER   A CA  1 
ATOM   3915 C C   . SER   A 1 502 ? 38.768  6.606   3.348   1.00 31.47  ? 1039 SER   A C   1 
ATOM   3916 O O   . SER   A 1 502 ? 39.948  6.276   3.324   1.00 35.96  ? 1039 SER   A O   1 
ATOM   3917 C CB  . SER   A 1 502 ? 37.891  7.383   1.151   1.00 30.60  ? 1039 SER   A CB  1 
ATOM   3918 O OG  . SER   A 1 502 ? 37.051  6.251   1.216   1.00 34.79  ? 1039 SER   A OG  1 
ATOM   3919 N N   . PRO   A 1 503 ? 37.838  5.934   4.053   1.00 34.14  ? 1040 PRO   A N   1 
ATOM   3920 C CA  . PRO   A 1 503 ? 38.175  4.664   4.705   1.00 34.42  ? 1040 PRO   A CA  1 
ATOM   3921 C C   . PRO   A 1 503 ? 38.272  3.534   3.685   1.00 38.65  ? 1040 PRO   A C   1 
ATOM   3922 O O   . PRO   A 1 503 ? 38.655  2.428   4.040   1.00 42.97  ? 1040 PRO   A O   1 
ATOM   3923 C CB  . PRO   A 1 503 ? 37.007  4.437   5.673   1.00 33.65  ? 1040 PRO   A CB  1 
ATOM   3924 C CG  . PRO   A 1 503 ? 35.848  5.148   5.022   1.00 29.53  ? 1040 PRO   A CG  1 
ATOM   3925 C CD  . PRO   A 1 503 ? 36.457  6.364   4.349   1.00 34.19  ? 1040 PRO   A CD  1 
ATOM   3926 N N   . GLY   A 1 504 ? 37.926  3.818   2.431   1.00 35.85  ? 1041 GLY   A N   1 
ATOM   3927 C CA  . GLY   A 1 504 ? 37.988  2.821   1.375   1.00 38.21  ? 1041 GLY   A CA  1 
ATOM   3928 C C   . GLY   A 1 504 ? 36.763  1.927   1.349   1.00 40.51  ? 1041 GLY   A C   1 
ATOM   3929 O O   . GLY   A 1 504 ? 35.839  2.091   2.144   1.00 39.77  ? 1041 GLY   A O   1 
ATOM   3930 N N   . ILE   A 1 505 ? 36.744  0.971   0.430   1.00 35.94  ? 1042 ILE   A N   1 
ATOM   3931 C CA  . ILE   A 1 505 ? 35.547  0.158   0.256   1.00 30.71  ? 1042 ILE   A CA  1 
ATOM   3932 C C   . ILE   A 1 505 ? 35.788  -1.308  0.605   1.00 34.35  ? 1042 ILE   A C   1 
ATOM   3933 O O   . ILE   A 1 505 ? 34.986  -2.169  0.248   1.00 35.92  ? 1042 ILE   A O   1 
ATOM   3934 C CB  . ILE   A 1 505 ? 35.007  0.250   -1.180  1.00 34.85  ? 1042 ILE   A CB  1 
ATOM   3935 C CG1 . ILE   A 1 505 ? 36.066  -0.202  -2.189  1.00 42.80  ? 1042 ILE   A CG1 1 
ATOM   3936 C CG2 . ILE   A 1 505 ? 34.536  1.668   -1.484  1.00 42.26  ? 1042 ILE   A CG2 1 
ATOM   3937 C CD1 . ILE   A 1 505 ? 35.512  -0.402  -3.586  1.00 49.46  ? 1042 ILE   A CD1 1 
ATOM   3938 N N   . ARG   A 1 506 ? 36.888  -1.581  1.302   1.00 42.35  ? 1043 ARG   A N   1 
ATOM   3939 C CA  . ARG   A 1 506 ? 37.143  -2.925  1.817   1.00 48.57  ? 1043 ARG   A CA  1 
ATOM   3940 C C   . ARG   A 1 506 ? 36.534  -3.052  3.217   1.00 41.31  ? 1043 ARG   A C   1 
ATOM   3941 O O   . ARG   A 1 506 ? 36.839  -2.256  4.100   1.00 46.72  ? 1043 ARG   A O   1 
ATOM   3942 C CB  . ARG   A 1 506 ? 38.648  -3.227  1.844   1.00 54.34  ? 1043 ARG   A CB  1 
ATOM   3943 C CG  . ARG   A 1 506 ? 38.983  -4.671  2.227   1.00 73.62  ? 1043 ARG   A CG  1 
ATOM   3944 C CD  . ARG   A 1 506 ? 40.491  -4.947  2.340   1.00 78.90  ? 1043 ARG   A CD  1 
ATOM   3945 N NE  . ARG   A 1 506 ? 40.748  -6.349  2.671   1.00 81.55  ? 1043 ARG   A NE  1 
ATOM   3946 C CZ  . ARG   A 1 506 ? 41.955  -6.882  2.857   1.00 78.72  ? 1043 ARG   A CZ  1 
ATOM   3947 N NH1 . ARG   A 1 506 ? 43.048  -6.133  2.752   1.00 67.33  ? 1043 ARG   A NH1 1 
ATOM   3948 N NH2 . ARG   A 1 506 ? 42.069  -8.174  3.152   1.00 73.48  ? 1043 ARG   A NH2 1 
ATOM   3949 N N   . PRO   A 1 507 ? 35.657  -4.046  3.419   1.00 45.44  ? 1044 PRO   A N   1 
ATOM   3950 C CA  . PRO   A 1 507 ? 35.033  -4.250  4.733   1.00 51.09  ? 1044 PRO   A CA  1 
ATOM   3951 C C   . PRO   A 1 507 ? 36.050  -4.702  5.775   1.00 60.20  ? 1044 PRO   A C   1 
ATOM   3952 O O   . PRO   A 1 507 ? 37.126  -5.168  5.401   1.00 56.99  ? 1044 PRO   A O   1 
ATOM   3953 C CB  . PRO   A 1 507 ? 33.993  -5.351  4.472   1.00 49.90  ? 1044 PRO   A CB  1 
ATOM   3954 C CG  . PRO   A 1 507 ? 33.820  -5.395  2.988   1.00 54.78  ? 1044 PRO   A CG  1 
ATOM   3955 C CD  . PRO   A 1 507 ? 35.150  -4.997  2.417   1.00 49.58  ? 1044 PRO   A CD  1 
ATOM   3956 N N   . ASN   A 1 508 ? 35.716  -4.576  7.055   1.00 70.05  ? 1045 ASN   A N   1 
ATOM   3957 C CA  . ASN   A 1 508 ? 36.649  -4.959  8.110   1.00 77.92  ? 1045 ASN   A CA  1 
ATOM   3958 C C   . ASN   A 1 508 ? 36.290  -6.300  8.749   1.00 74.59  ? 1045 ASN   A C   1 
ATOM   3959 O O   . ASN   A 1 508 ? 35.782  -7.201  8.079   1.00 74.02  ? 1045 ASN   A O   1 
ATOM   3960 C CB  . ASN   A 1 508 ? 36.720  -3.865  9.181   1.00 82.61  ? 1045 ASN   A CB  1 
ATOM   3961 C CG  . ASN   A 1 508 ? 35.571  -3.934  10.169  1.00 88.30  ? 1045 ASN   A CG  1 
ATOM   3962 O OD1 . ASN   A 1 508 ? 34.450  -4.307  9.820   1.00 89.34  ? 1045 ASN   A OD1 1 
ATOM   3963 N ND2 . ASN   A 1 508 ? 35.848  -3.571  11.418  1.00 90.05  ? 1045 ASN   A ND2 1 
HETATM 3964 N N1  . A1ASW B 2 .   ? 35.138  16.974  -19.982 1.00 35.91  ? 2001 A1ASW A N1  1 
HETATM 3965 N N3  . A1ASW B 2 .   ? 35.728  13.040  -17.910 1.00 32.71  ? 2001 A1ASW A N3  1 
HETATM 3966 C C4  . A1ASW B 2 .   ? 33.502  15.813  -18.588 1.00 28.54  ? 2001 A1ASW A C4  1 
HETATM 3967 C C5  . A1ASW B 2 .   ? 33.909  16.181  -19.997 1.00 30.37  ? 2001 A1ASW A C5  1 
HETATM 3968 C C6  . A1ASW B 2 .   ? 34.566  13.688  -17.750 1.00 34.41  ? 2001 A1ASW A C6  1 
HETATM 3969 C C7  . A1ASW B 2 .   ? 35.779  11.707  -17.732 1.00 30.92  ? 2001 A1ASW A C7  1 
HETATM 3970 C C8  . A1ASW B 2 .   ? 38.276  11.596  -18.022 1.00 35.90  ? 2001 A1ASW A C8  1 
HETATM 3971 C C10 . A1ASW B 2 .   ? 40.548  11.370  -18.801 1.00 42.00  ? 2001 A1ASW A C10 1 
HETATM 3972 C C13 . A1ASW B 2 .   ? 38.624  12.826  -17.459 1.00 44.73  ? 2001 A1ASW A C13 1 
HETATM 3973 C C15 . A1ASW B 2 .   ? 32.406  10.783  -16.826 1.00 34.09  ? 2001 A1ASW A C15 1 
HETATM 3974 C C17 . A1ASW B 2 .   ? 31.048  12.762  -16.785 1.00 29.05  ? 2001 A1ASW A C17 1 
HETATM 3975 C C1  . A1ASW B 2 .   ? 35.522  17.366  -21.338 1.00 47.42  ? 2001 A1ASW A C1  1 
HETATM 3976 C C2  . A1ASW B 2 .   ? 36.208  16.222  -19.328 1.00 40.12  ? 2001 A1ASW A C2  1 
HETATM 3977 C C3  . A1ASW B 2 .   ? 35.814  15.822  -17.922 1.00 35.53  ? 2001 A1ASW A C3  1 
HETATM 3978 N N2  . A1ASW B 2 .   ? 34.584  15.041  -17.983 1.00 32.92  ? 2001 A1ASW A N2  1 
HETATM 3979 N N4  . A1ASW B 2 .   ? 36.966  11.071  -17.908 1.00 29.09  ? 2001 A1ASW A N4  1 
HETATM 3980 C C9  . A1ASW B 2 .   ? 39.257  10.874  -18.681 1.00 47.62  ? 2001 A1ASW A C9  1 
HETATM 3981 C C11 . A1ASW B 2 .   ? 40.879  12.594  -18.247 1.00 51.57  ? 2001 A1ASW A C11 1 
HETATM 3982 O O1  . A1ASW B 2 .   ? 42.146  13.092  -18.351 1.00 59.50  ? 2001 A1ASW A O1  1 
HETATM 3983 C C12 . A1ASW B 2 .   ? 39.904  13.324  -17.572 1.00 48.42  ? 2001 A1ASW A C12 1 
HETATM 3984 N N5  . A1ASW B 2 .   ? 34.734  10.942  -17.387 1.00 32.65  ? 2001 A1ASW A N5  1 
HETATM 3985 C C14 . A1ASW B 2 .   ? 33.526  11.553  -17.196 1.00 33.97  ? 2001 A1ASW A C14 1 
HETATM 3986 C C16 . A1ASW B 2 .   ? 31.196  11.379  -16.631 1.00 35.70  ? 2001 A1ASW A C16 1 
HETATM 3987 C C18 . A1ASW B 2 .   ? 32.109  13.532  -17.152 1.00 30.36  ? 2001 A1ASW A C18 1 
HETATM 3988 C C19 . A1ASW B 2 .   ? 33.387  12.956  -17.368 1.00 31.60  ? 2001 A1ASW A C19 1 
HETATM 3989 O O   . HOH   C 3 .   ? 19.425  -7.603  -20.625 1.00 57.80  ? 2101 HOH   A O   1 
HETATM 3990 O O   . HOH   C 3 .   ? -0.852  -12.614 -2.602  1.00 56.48  ? 2102 HOH   A O   1 
HETATM 3991 O O   . HOH   C 3 .   ? -1.674  5.133   -23.930 1.00 51.22  ? 2103 HOH   A O   1 
HETATM 3992 O O   . HOH   C 3 .   ? 12.024  -2.947  -21.469 1.00 51.83  ? 2104 HOH   A O   1 
HETATM 3993 O O   . HOH   C 3 .   ? 44.626  20.130  -5.447  1.00 54.17  ? 2105 HOH   A O   1 
HETATM 3994 O O   . HOH   C 3 .   ? 31.195  -0.166  -14.736 1.00 47.10  ? 2106 HOH   A O   1 
HETATM 3995 O O   . HOH   C 3 .   ? 40.020  4.815   -1.521  1.00 48.65  ? 2107 HOH   A O   1 
HETATM 3996 O O   . HOH   C 3 .   ? 11.541  7.826   7.090   1.00 47.78  ? 2108 HOH   A O   1 
HETATM 3997 O O   . HOH   C 3 .   ? 24.928  -6.763  11.013  1.00 41.73  ? 2109 HOH   A O   1 
HETATM 3998 O O   . HOH   C 3 .   ? 32.241  16.267  -23.903 1.00 46.08  ? 2110 HOH   A O   1 
HETATM 3999 O O   . HOH   C 3 .   ? -11.068 -17.649 -25.810 1.00 37.55  ? 2111 HOH   A O   1 
HETATM 4000 O O   . HOH   C 3 .   ? 42.303  27.075  -0.329  1.00 53.00  ? 2112 HOH   A O   1 
HETATM 4001 O O   . HOH   C 3 .   ? 34.481  20.447  11.238  1.00 56.40  ? 2113 HOH   A O   1 
HETATM 4002 O O   . HOH   C 3 .   ? 7.019   -7.826  -1.430  1.00 52.61  ? 2114 HOH   A O   1 
HETATM 4003 O O   . HOH   C 3 .   ? 32.902  -0.285  -21.418 1.00 44.88  ? 2115 HOH   A O   1 
HETATM 4004 O O   . HOH   C 3 .   ? 15.329  -6.112  -6.980  1.00 53.70  ? 2116 HOH   A O   1 
HETATM 4005 O O   . HOH   C 3 .   ? -12.714 1.834   -7.447  1.00 47.95  ? 2117 HOH   A O   1 
HETATM 4006 O O   . HOH   C 3 .   ? -38.810 -34.079 -19.610 1.00 49.01  ? 2118 HOH   A O   1 
HETATM 4007 O O   . HOH   C 3 .   ? -35.702 -26.752 -23.436 1.00 33.84  ? 2119 HOH   A O   1 
HETATM 4008 O O   . HOH   C 3 .   ? -29.226 -19.285 -13.782 1.00 39.27  ? 2120 HOH   A O   1 
HETATM 4009 O O   . HOH   C 3 .   ? 38.901  6.733   -18.071 1.00 42.33  ? 2121 HOH   A O   1 
HETATM 4010 O O   . HOH   C 3 .   ? -19.036 -1.784  -35.807 1.00 44.60  ? 2122 HOH   A O   1 
HETATM 4011 O O   . HOH   C 3 .   ? 38.320  2.597   -5.052  1.00 46.68  ? 2123 HOH   A O   1 
HETATM 4012 O O   . HOH   C 3 .   ? -24.233 -32.164 -20.763 1.00 52.09  ? 2124 HOH   A O   1 
HETATM 4013 O O   . HOH   C 3 .   ? -21.960 -16.786 -24.566 1.00 34.16  ? 2125 HOH   A O   1 
HETATM 4014 O O   . HOH   C 3 .   ? 19.950  26.727  -15.511 1.00 36.86  ? 2126 HOH   A O   1 
HETATM 4015 O O   . HOH   C 3 .   ? -15.353 -0.592  -26.957 1.00 49.76  ? 2127 HOH   A O   1 
HETATM 4016 O O   . HOH   C 3 .   ? 31.543  8.596   2.717   1.00 27.53  ? 2128 HOH   A O   1 
HETATM 4017 O O   . HOH   C 3 .   ? -20.079 -16.309 -27.774 1.00 48.91  ? 2129 HOH   A O   1 
HETATM 4018 O O   . HOH   C 3 .   ? -22.193 -7.946  -34.968 1.00 39.19  ? 2130 HOH   A O   1 
HETATM 4019 O O   . HOH   C 3 .   ? -7.487  0.821   -8.287  1.00 36.09  ? 2131 HOH   A O   1 
HETATM 4020 O O   . HOH   C 3 .   ? -13.976 -12.003 -35.095 1.00 43.78  ? 2132 HOH   A O   1 
HETATM 4021 O O   . HOH   C 3 .   ? 38.670  16.973  -17.180 1.00 46.07  ? 2133 HOH   A O   1 
HETATM 4022 O O   . HOH   C 3 .   ? -0.184  -6.801  -8.756  1.00 35.89  ? 2134 HOH   A O   1 
HETATM 4023 O O   . HOH   C 3 .   ? 46.623  3.249   -15.861 1.00 50.60  ? 2135 HOH   A O   1 
HETATM 4024 O O   . HOH   C 3 .   ? -19.356 -1.194  -19.280 1.00 51.72  ? 2136 HOH   A O   1 
HETATM 4025 O O   . HOH   C 3 .   ? 32.959  19.364  -19.733 1.00 31.51  ? 2137 HOH   A O   1 
HETATM 4026 O O   . HOH   C 3 .   ? 20.572  18.295  -12.821 1.00 28.28  ? 2138 HOH   A O   1 
HETATM 4027 O O   . HOH   C 3 .   ? 26.665  0.585   -23.688 1.00 32.71  ? 2139 HOH   A O   1 
HETATM 4028 O O   . HOH   C 3 .   ? 34.327  32.478  -8.824  1.00 37.03  ? 2140 HOH   A O   1 
HETATM 4029 O O   . HOH   C 3 .   ? 31.081  20.717  0.945   1.00 50.80  ? 2141 HOH   A O   1 
HETATM 4030 O O   . HOH   C 3 .   ? 1.274   9.154   -4.312  1.00 38.55  ? 2142 HOH   A O   1 
HETATM 4031 O O   . HOH   C 3 .   ? 46.535  9.167   -15.174 1.00 65.93  ? 2143 HOH   A O   1 
HETATM 4032 O O   . HOH   C 3 .   ? 15.491  30.305  -11.283 1.00 46.84  ? 2144 HOH   A O   1 
HETATM 4033 O O   . HOH   C 3 .   ? 16.505  -2.635  -16.169 1.00 35.25  ? 2145 HOH   A O   1 
HETATM 4034 O O   . HOH   C 3 .   ? 10.621  9.818   1.585   1.00 43.54  ? 2146 HOH   A O   1 
HETATM 4035 O O   . HOH   C 3 .   ? 29.872  6.776   9.731   1.00 36.17  ? 2147 HOH   A O   1 
HETATM 4036 O O   . HOH   C 3 .   ? 16.152  4.087   -12.308 1.00 53.20  ? 2148 HOH   A O   1 
HETATM 4037 O O   . HOH   C 3 .   ? 34.161  9.692   15.031  1.00 53.58  ? 2149 HOH   A O   1 
HETATM 4038 O O   . HOH   C 3 .   ? -3.557  0.758   -14.495 1.00 28.78  ? 2150 HOH   A O   1 
HETATM 4039 O O   . HOH   C 3 .   ? 14.380  17.993  -2.721  1.00 32.85  ? 2151 HOH   A O   1 
HETATM 4040 O O   . HOH   C 3 .   ? -19.525 -35.838 -30.567 1.00 53.02  ? 2152 HOH   A O   1 
HETATM 4041 O O   . HOH   C 3 .   ? -32.207 -22.574 -12.271 1.00 49.16  ? 2153 HOH   A O   1 
HETATM 4042 O O   . HOH   C 3 .   ? -16.903 -14.400 -27.534 1.00 36.13  ? 2154 HOH   A O   1 
HETATM 4043 O O   . HOH   C 3 .   ? 0.621   -9.411  -15.546 1.00 45.04  ? 2155 HOH   A O   1 
HETATM 4044 O O   . HOH   C 3 .   ? 26.677  30.762  -6.912  1.00 50.42  ? 2156 HOH   A O   1 
HETATM 4045 O O   . HOH   C 3 .   ? -4.770  -16.532 -23.828 1.00 50.07  ? 2157 HOH   A O   1 
HETATM 4046 O O   . HOH   C 3 .   ? 5.957   -5.404  -25.361 1.00 39.07  ? 2158 HOH   A O   1 
HETATM 4047 O O   . HOH   C 3 .   ? -18.648 -2.244  -33.115 1.00 38.70  ? 2159 HOH   A O   1 
HETATM 4048 O O   . HOH   C 3 .   ? -27.182 -8.680  -19.694 1.00 35.28  ? 2160 HOH   A O   1 
HETATM 4049 O O   . HOH   C 3 .   ? -22.328 -28.151 -28.775 1.00 43.52  ? 2161 HOH   A O   1 
HETATM 4050 O O   . HOH   C 3 .   ? -43.866 -32.507 -23.211 1.00 50.89  ? 2162 HOH   A O   1 
HETATM 4051 O O   . HOH   C 3 .   ? 41.357  16.019  -2.678  1.00 33.15  ? 2163 HOH   A O   1 
HETATM 4052 O O   . HOH   C 3 .   ? 19.924  3.545   13.911  1.00 48.95  ? 2164 HOH   A O   1 
HETATM 4053 O O   . HOH   C 3 .   ? -10.182 0.818   -6.677  1.00 40.37  ? 2165 HOH   A O   1 
HETATM 4054 O O   . HOH   C 3 .   ? 16.732  9.094   12.828  1.00 44.46  ? 2166 HOH   A O   1 
HETATM 4055 O O   . HOH   C 3 .   ? -33.696 -18.900 -26.276 1.00 47.48  ? 2167 HOH   A O   1 
HETATM 4056 O O   . HOH   C 3 .   ? -27.429 -10.894 -15.842 1.00 26.96  ? 2168 HOH   A O   1 
HETATM 4057 O O   . HOH   C 3 .   ? -22.975 -26.950 -34.107 1.00 28.95  ? 2169 HOH   A O   1 
HETATM 4058 O O   . HOH   C 3 .   ? -30.018 -31.519 -25.877 1.00 37.83  ? 2170 HOH   A O   1 
HETATM 4059 O O   . HOH   C 3 .   ? -4.333  -19.009 -21.160 1.00 35.06  ? 2171 HOH   A O   1 
HETATM 4060 O O   . HOH   C 3 .   ? 28.384  0.861   -25.819 1.00 42.82  ? 2172 HOH   A O   1 
HETATM 4061 O O   . HOH   C 3 .   ? 27.544  32.151  -10.815 1.00 38.48  ? 2173 HOH   A O   1 
HETATM 4062 O O   . HOH   C 3 .   ? 31.265  -5.042  7.011   1.00 34.86  ? 2174 HOH   A O   1 
HETATM 4063 O O   . HOH   C 3 .   ? 22.713  5.233   14.153  1.00 43.23  ? 2175 HOH   A O   1 
HETATM 4064 O O   . HOH   C 3 .   ? 40.571  10.540  -6.737  1.00 35.23  ? 2176 HOH   A O   1 
HETATM 4065 O O   . HOH   C 3 .   ? -35.441 -27.037 -26.100 1.00 34.82  ? 2177 HOH   A O   1 
HETATM 4066 O O   . HOH   C 3 .   ? 24.869  -5.761  6.807   1.00 31.95  ? 2178 HOH   A O   1 
HETATM 4067 O O   . HOH   C 3 .   ? -29.383 -16.648 -27.770 1.00 41.01  ? 2179 HOH   A O   1 
HETATM 4068 O O   . HOH   C 3 .   ? 26.509  20.288  0.316   1.00 38.94  ? 2180 HOH   A O   1 
HETATM 4069 O O   . HOH   C 3 .   ? -3.657  0.443   -1.277  1.00 45.30  ? 2181 HOH   A O   1 
HETATM 4070 O O   . HOH   C 3 .   ? 10.187  27.946  -10.637 1.00 44.88  ? 2182 HOH   A O   1 
HETATM 4071 O O   . HOH   C 3 .   ? 24.605  28.117  -1.267  1.00 55.87  ? 2183 HOH   A O   1 
HETATM 4072 O O   . HOH   C 3 .   ? -3.162  -17.090 -8.218  1.00 55.46  ? 2184 HOH   A O   1 
HETATM 4073 O O   . HOH   C 3 .   ? 29.226  19.468  -0.400  1.00 31.43  ? 2185 HOH   A O   1 
HETATM 4074 O O   . HOH   C 3 .   ? 17.050  -8.466  3.906   1.00 45.01  ? 2186 HOH   A O   1 
HETATM 4075 O O   . HOH   C 3 .   ? -24.004 -23.236 -11.528 1.00 42.21  ? 2187 HOH   A O   1 
HETATM 4076 O O   . HOH   C 3 .   ? -23.090 -6.569  -4.320  1.00 35.04  ? 2188 HOH   A O   1 
HETATM 4077 O O   . HOH   C 3 .   ? 0.097   -7.256  -12.345 1.00 42.68  ? 2189 HOH   A O   1 
HETATM 4078 O O   . HOH   C 3 .   ? 3.632   7.980   -3.471  1.00 31.54  ? 2190 HOH   A O   1 
HETATM 4079 O O   . HOH   C 3 .   ? 11.607  31.821  -9.429  1.00 46.65  ? 2191 HOH   A O   1 
HETATM 4080 O O   . HOH   C 3 .   ? 39.417  25.782  -4.032  1.00 41.87  ? 2192 HOH   A O   1 
HETATM 4081 O O   . HOH   C 3 .   ? -3.483  4.633   -3.673  1.00 37.54  ? 2193 HOH   A O   1 
HETATM 4082 O O   . HOH   C 3 .   ? 17.788  29.656  -8.460  1.00 36.71  ? 2194 HOH   A O   1 
HETATM 4083 O O   . HOH   C 3 .   ? 10.485  28.336  -4.214  1.00 36.65  ? 2195 HOH   A O   1 
HETATM 4084 O O   . HOH   C 3 .   ? 10.511  8.781   -2.588  1.00 33.57  ? 2196 HOH   A O   1 
HETATM 4085 O O   . HOH   C 3 .   ? 22.290  24.937  0.059   1.00 53.66  ? 2197 HOH   A O   1 
HETATM 4086 O O   . HOH   C 3 .   ? -29.066 -33.152 -21.380 1.00 39.94  ? 2198 HOH   A O   1 
HETATM 4087 O O   . HOH   C 3 .   ? -15.893 -16.001 -32.791 1.00 44.09  ? 2199 HOH   A O   1 
HETATM 4088 O O   . HOH   C 3 .   ? -22.328 -17.720 -0.200  1.00 49.95  ? 2200 HOH   A O   1 
HETATM 4089 O O   . HOH   C 3 .   ? -18.615 -26.252 -21.328 1.00 41.08  ? 2201 HOH   A O   1 
HETATM 4090 O O   . HOH   C 3 .   ? 39.470  19.095  5.950   1.00 48.67  ? 2202 HOH   A O   1 
HETATM 4091 O O   . HOH   C 3 .   ? 28.581  26.005  -1.090  1.00 44.33  ? 2203 HOH   A O   1 
HETATM 4092 O O   . HOH   C 3 .   ? 33.568  23.298  -18.840 1.00 34.50  ? 2204 HOH   A O   1 
HETATM 4093 O O   . HOH   C 3 .   ? -29.228 -22.054 -14.470 1.00 32.09  ? 2205 HOH   A O   1 
HETATM 4094 O O   . HOH   C 3 .   ? 17.990  13.576  5.247   1.00 36.05  ? 2206 HOH   A O   1 
HETATM 4095 O O   . HOH   C 3 .   ? 37.086  5.793   9.602   1.00 42.14  ? 2207 HOH   A O   1 
HETATM 4096 O O   . HOH   C 3 .   ? 3.021   -2.589  -3.195  1.00 33.64  ? 2208 HOH   A O   1 
HETATM 4097 O O   . HOH   C 3 .   ? 28.337  16.620  9.508   1.00 47.65  ? 2209 HOH   A O   1 
HETATM 4098 O O   . HOH   C 3 .   ? 17.489  -6.328  5.528   1.00 32.56  ? 2210 HOH   A O   1 
HETATM 4099 O O   . HOH   C 3 .   ? -0.398  -0.436  -6.438  1.00 47.47  ? 2211 HOH   A O   1 
HETATM 4100 O O   . HOH   C 3 .   ? -4.611  -1.757  -15.040 1.00 24.91  ? 2212 HOH   A O   1 
HETATM 4101 O O   . HOH   C 3 .   ? 24.269  -3.314  6.010   1.00 29.92  ? 2213 HOH   A O   1 
HETATM 4102 O O   . HOH   C 3 .   ? -0.665  -4.810  -10.849 1.00 31.34  ? 2214 HOH   A O   1 
HETATM 4103 O O   . HOH   C 3 .   ? 4.672   -6.707  -8.521  1.00 41.03  ? 2215 HOH   A O   1 
HETATM 4104 O O   . HOH   C 3 .   ? -36.027 -22.857 -17.251 1.00 36.29  ? 2216 HOH   A O   1 
HETATM 4105 O O   . HOH   C 3 .   ? -35.532 -23.495 -20.161 1.00 38.53  ? 2217 HOH   A O   1 
HETATM 4106 O O   . HOH   C 3 .   ? 7.958   2.024   -4.288  1.00 28.56  ? 2218 HOH   A O   1 
HETATM 4107 O O   . HOH   C 3 .   ? 28.174  4.575   8.092   1.00 30.71  ? 2219 HOH   A O   1 
HETATM 4108 O O   . HOH   C 3 .   ? 37.512  2.557   -17.841 1.00 43.96  ? 2220 HOH   A O   1 
HETATM 4109 O O   . HOH   C 3 .   ? 33.084  0.535   -13.301 1.00 37.80  ? 2221 HOH   A O   1 
HETATM 4110 O O   . HOH   C 3 .   ? 15.244  16.537  5.274   1.00 54.72  ? 2222 HOH   A O   1 
HETATM 4111 O O   . HOH   C 3 .   ? 15.092  4.405   -7.084  1.00 38.55  ? 2223 HOH   A O   1 
HETATM 4112 O O   . HOH   C 3 .   ? 7.349   -10.580 -19.763 1.00 40.96  ? 2224 HOH   A O   1 
HETATM 4113 O O   . HOH   C 3 .   ? 35.809  23.805  -15.773 1.00 36.80  ? 2225 HOH   A O   1 
HETATM 4114 O O   . HOH   C 3 .   ? -9.985  3.112   -14.623 1.00 48.25  ? 2226 HOH   A O   1 
HETATM 4115 O O   . HOH   C 3 .   ? 31.724  32.504  -13.235 1.00 35.59  ? 2227 HOH   A O   1 
HETATM 4116 O O   . HOH   C 3 .   ? -19.364 -18.094 -22.844 1.00 24.67  ? 2228 HOH   A O   1 
HETATM 4117 O O   . HOH   C 3 .   ? 37.054  25.564  -7.329  1.00 32.57  ? 2229 HOH   A O   1 
HETATM 4118 O O   . HOH   C 3 .   ? 30.049  33.547  -19.965 1.00 38.22  ? 2230 HOH   A O   1 
HETATM 4119 O O   . HOH   C 3 .   ? -12.674 1.679   -22.630 1.00 44.86  ? 2231 HOH   A O   1 
HETATM 4120 O O   . HOH   C 3 .   ? -10.906 -17.304 -23.176 1.00 37.48  ? 2232 HOH   A O   1 
HETATM 4121 O O   . HOH   C 3 .   ? 22.791  20.299  -13.426 1.00 23.35  ? 2233 HOH   A O   1 
HETATM 4122 O O   . HOH   C 3 .   ? -24.373 -5.917  -12.422 1.00 32.90  ? 2234 HOH   A O   1 
HETATM 4123 O O   . HOH   C 3 .   ? 39.039  -0.285  2.455   1.00 59.47  ? 2235 HOH   A O   1 
HETATM 4124 O O   . HOH   C 3 .   ? -21.041 -13.641 -37.052 1.00 37.40  ? 2236 HOH   A O   1 
HETATM 4125 O O   . HOH   C 3 .   ? 5.171   -6.509  -4.820  1.00 52.74  ? 2237 HOH   A O   1 
HETATM 4126 O O   . HOH   C 3 .   ? 36.329  1.535   7.779   1.00 52.19  ? 2238 HOH   A O   1 
HETATM 4127 O O   . HOH   C 3 .   ? -13.716 -19.218 4.404   1.00 52.57  ? 2239 HOH   A O   1 
HETATM 4128 O O   . HOH   C 3 .   ? 36.970  10.620  -0.770  1.00 27.03  ? 2240 HOH   A O   1 
HETATM 4129 O O   . HOH   C 3 .   ? 18.750  10.285  -12.375 1.00 26.23  ? 2241 HOH   A O   1 
HETATM 4130 O O   . HOH   C 3 .   ? 30.675  -0.537  -19.574 1.00 43.40  ? 2242 HOH   A O   1 
HETATM 4131 O O   . HOH   C 3 .   ? -1.752  -11.257 -35.859 1.00 50.25  ? 2243 HOH   A O   1 
HETATM 4132 O O   . HOH   C 3 .   ? -2.898  0.991   -9.907  1.00 42.78  ? 2244 HOH   A O   1 
HETATM 4133 O O   . HOH   C 3 .   ? -16.960 -1.787  -38.950 1.00 48.89  ? 2245 HOH   A O   1 
HETATM 4134 O O   . HOH   C 3 .   ? 5.802   10.052  -3.836  1.00 35.98  ? 2246 HOH   A O   1 
HETATM 4135 O O   . HOH   C 3 .   ? 0.232   15.138  -8.201  1.00 50.51  ? 2247 HOH   A O   1 
HETATM 4136 O O   . HOH   C 3 .   ? -7.611  4.744   -21.412 1.00 46.86  ? 2248 HOH   A O   1 
HETATM 4137 O O   . HOH   C 3 .   ? -23.309 -24.319 -28.459 1.00 38.37  ? 2249 HOH   A O   1 
HETATM 4138 O O   . HOH   C 3 .   ? 25.725  33.179  -12.847 1.00 50.24  ? 2250 HOH   A O   1 
HETATM 4139 O O   . HOH   C 3 .   ? 29.053  -2.357  13.482  1.00 44.55  ? 2251 HOH   A O   1 
HETATM 4140 O O   . HOH   C 3 .   ? -23.702 -9.938  -33.735 1.00 27.79  ? 2252 HOH   A O   1 
HETATM 4141 O O   . HOH   C 3 .   ? -35.523 -17.927 -24.459 1.00 36.34  ? 2253 HOH   A O   1 
HETATM 4142 O O   . HOH   C 3 .   ? 42.755  19.547  -12.464 1.00 34.09  ? 2254 HOH   A O   1 
HETATM 4143 O O   . HOH   C 3 .   ? -2.371  1.201   -33.006 1.00 50.96  ? 2255 HOH   A O   1 
HETATM 4144 O O   . HOH   C 3 .   ? -11.054 -17.904 -17.777 1.00 38.63  ? 2256 HOH   A O   1 
HETATM 4145 O O   . HOH   C 3 .   ? 21.925  23.001  -13.780 1.00 23.47  ? 2257 HOH   A O   1 
HETATM 4146 O O   . HOH   C 3 .   ? -28.759 -28.297 -26.653 1.00 42.74  ? 2258 HOH   A O   1 
HETATM 4147 O O   . HOH   C 3 .   ? -11.648 -17.837 -14.838 1.00 43.60  ? 2259 HOH   A O   1 
HETATM 4148 O O   . HOH   C 3 .   ? 9.682   -9.469  9.849   1.00 65.01  ? 2260 HOH   A O   1 
HETATM 4149 O O   . HOH   C 3 .   ? -29.659 -20.317 -28.363 1.00 39.82  ? 2261 HOH   A O   1 
HETATM 4150 O O   . HOH   C 3 .   ? -20.895 -6.367  -27.237 1.00 33.91  ? 2262 HOH   A O   1 
HETATM 4151 O O   . HOH   C 3 .   ? -15.495 -23.524 -15.143 1.00 44.52  ? 2263 HOH   A O   1 
HETATM 4152 O O   . HOH   C 3 .   ? -37.233 -25.792 -19.997 1.00 39.74  ? 2264 HOH   A O   1 
HETATM 4153 O O   . HOH   C 3 .   ? -12.147 -18.549 -20.113 1.00 34.56  ? 2265 HOH   A O   1 
HETATM 4154 O O   . HOH   C 3 .   ? 18.301  1.155   4.277   1.00 27.92  ? 2266 HOH   A O   1 
HETATM 4155 O O   . HOH   C 3 .   ? 4.687   11.792  -13.241 1.00 37.61  ? 2267 HOH   A O   1 
HETATM 4156 O O   . HOH   C 3 .   ? -21.339 -24.900 -36.538 1.00 29.19  ? 2268 HOH   A O   1 
HETATM 4157 O O   . HOH   C 3 .   ? -18.400 -17.687 -28.877 1.00 50.13  ? 2269 HOH   A O   1 
HETATM 4158 O O   . HOH   C 3 .   ? -9.531  1.467   -24.629 1.00 35.62  ? 2270 HOH   A O   1 
HETATM 4159 O O   . HOH   C 3 .   ? 12.374  4.692   8.442   1.00 55.73  ? 2271 HOH   A O   1 
HETATM 4160 O O   . HOH   C 3 .   ? -30.579 -29.211 -12.857 1.00 48.00  ? 2272 HOH   A O   1 
HETATM 4161 O O   . HOH   C 3 .   ? 17.766  -5.588  8.497   1.00 42.70  ? 2273 HOH   A O   1 
HETATM 4162 O O   . HOH   C 3 .   ? 18.387  17.201  2.561   1.00 41.28  ? 2274 HOH   A O   1 
HETATM 4163 O O   . HOH   C 3 .   ? -20.300 -27.371 -24.586 1.00 50.06  ? 2275 HOH   A O   1 
HETATM 4164 O O   . HOH   C 3 .   ? -2.961  -4.272  9.905   1.00 65.13  ? 2276 HOH   A O   1 
HETATM 4165 O O   . HOH   C 3 .   ? 23.626  30.583  -15.684 1.00 37.11  ? 2277 HOH   A O   1 
HETATM 4166 O O   . HOH   C 3 .   ? 25.873  8.524   -20.675 1.00 32.28  ? 2278 HOH   A O   1 
HETATM 4167 O O   . HOH   C 3 .   ? 18.722  5.476   -24.529 1.00 49.14  ? 2279 HOH   A O   1 
HETATM 4168 O O   . HOH   C 3 .   ? 14.476  3.611   9.744   1.00 45.17  ? 2280 HOH   A O   1 
HETATM 4169 O O   . HOH   C 3 .   ? -3.825  2.478   -22.581 1.00 38.60  ? 2281 HOH   A O   1 
HETATM 4170 O O   . HOH   C 3 .   ? -2.970  -10.408 -12.751 1.00 27.98  ? 2282 HOH   A O   1 
HETATM 4171 O O   . HOH   C 3 .   ? -4.120  -4.374  -32.097 1.00 39.78  ? 2283 HOH   A O   1 
HETATM 4172 O O   . HOH   C 3 .   ? 18.345  10.040  10.461  1.00 39.28  ? 2284 HOH   A O   1 
HETATM 4173 O O   . HOH   C 3 .   ? -1.329  -12.326 -22.449 1.00 54.82  ? 2285 HOH   A O   1 
HETATM 4174 O O   . HOH   C 3 .   ? 26.424  -4.702  12.557  1.00 51.58  ? 2286 HOH   A O   1 
HETATM 4175 O O   . HOH   C 3 .   ? -15.221 -0.657  -20.624 1.00 38.29  ? 2287 HOH   A O   1 
HETATM 4176 O O   . HOH   C 3 .   ? 12.978  -12.070 -7.979  1.00 61.07  ? 2288 HOH   A O   1 
HETATM 4177 O O   . HOH   C 3 .   ? 28.710  -10.402 10.663  1.00 51.37  ? 2289 HOH   A O   1 
HETATM 4178 O O   . HOH   C 3 .   ? -34.413 -15.570 -23.356 1.00 32.32  ? 2290 HOH   A O   1 
HETATM 4179 O O   . HOH   C 3 .   ? 29.254  29.419  0.224   1.00 53.78  ? 2291 HOH   A O   1 
HETATM 4180 O O   . HOH   C 3 .   ? -23.559 -4.630  -6.261  1.00 48.41  ? 2292 HOH   A O   1 
HETATM 4181 O O   . HOH   C 3 .   ? 36.929  0.572   5.305   1.00 61.50  ? 2293 HOH   A O   1 
HETATM 4182 O O   . HOH   C 3 .   ? 14.228  8.658   -0.733  1.00 34.41  ? 2294 HOH   A O   1 
HETATM 4183 O O   . HOH   C 3 .   ? -8.273  6.708   -24.944 1.00 48.71  ? 2295 HOH   A O   1 
HETATM 4184 O O   . HOH   C 3 .   ? -27.687 -19.074 -11.442 1.00 39.45  ? 2296 HOH   A O   1 
HETATM 4185 O O   . HOH   C 3 .   ? 20.178  30.771  -9.585  1.00 36.77  ? 2297 HOH   A O   1 
HETATM 4186 O O   . HOH   C 3 .   ? -1.576  6.394   -28.144 1.00 50.91  ? 2298 HOH   A O   1 
HETATM 4187 O O   . HOH   C 3 .   ? 2.955   -8.016  -15.297 1.00 34.07  ? 2299 HOH   A O   1 
HETATM 4188 O O   . HOH   C 3 .   ? 22.680  -5.267  -25.298 1.00 42.28  ? 2300 HOH   A O   1 
HETATM 4189 O O   . HOH   C 3 .   ? -25.396 -21.888 -28.780 1.00 48.09  ? 2301 HOH   A O   1 
HETATM 4190 O O   . HOH   C 3 .   ? 25.700  29.997  -2.174  1.00 55.03  ? 2302 HOH   A O   1 
HETATM 4191 O O   . HOH   C 3 .   ? -29.356 -6.817  -23.775 1.00 47.91  ? 2303 HOH   A O   1 
HETATM 4192 O O   . HOH   C 3 .   ? -28.741 -26.748 -24.572 1.00 29.09  ? 2304 HOH   A O   1 
HETATM 4193 O O   . HOH   C 3 .   ? -22.815 -4.157  -15.885 1.00 40.19  ? 2305 HOH   A O   1 
HETATM 4194 O O   . HOH   C 3 .   ? 23.046  0.315   14.077  1.00 50.32  ? 2306 HOH   A O   1 
HETATM 4195 O O   . HOH   C 3 .   ? -27.064 -33.471 -28.422 1.00 44.28  ? 2307 HOH   A O   1 
HETATM 4196 O O   . HOH   C 3 .   ? 24.290  -9.134  -5.202  1.00 45.75  ? 2308 HOH   A O   1 
HETATM 4197 O O   . HOH   C 3 .   ? -10.756 -11.894 -35.687 1.00 39.95  ? 2309 HOH   A O   1 
HETATM 4198 O O   . HOH   C 3 .   ? -35.778 -33.392 -23.429 1.00 46.60  ? 2310 HOH   A O   1 
HETATM 4199 O O   . HOH   C 3 .   ? -4.581  -16.789 -14.294 1.00 32.23  ? 2311 HOH   A O   1 
HETATM 4200 O O   . HOH   C 3 .   ? 29.568  15.531  3.284   1.00 42.31  ? 2312 HOH   A O   1 
HETATM 4201 O O   . HOH   C 3 .   ? 10.611  13.187  -9.804  1.00 42.81  ? 2313 HOH   A O   1 
HETATM 4202 O O   . HOH   C 3 .   ? 34.876  27.450  -20.615 1.00 49.37  ? 2314 HOH   A O   1 
HETATM 4203 O O   . HOH   C 3 .   ? 32.987  0.369   11.335  1.00 46.19  ? 2315 HOH   A O   1 
HETATM 4204 O O   . HOH   C 3 .   ? -3.091  12.636  -8.267  1.00 47.96  ? 2316 HOH   A O   1 
HETATM 4205 O O   . HOH   C 3 .   ? -3.173  -5.956  11.870  1.00 52.58  ? 2317 HOH   A O   1 
HETATM 4206 O O   . HOH   C 3 .   ? -39.260 -31.343 -23.339 1.00 50.18  ? 2318 HOH   A O   1 
HETATM 4207 O O   . HOH   C 3 .   ? 35.707  26.199  -17.122 1.00 43.52  ? 2319 HOH   A O   1 
HETATM 4208 O O   . HOH   C 3 .   ? 17.996  21.308  1.830   1.00 43.53  ? 2320 HOH   A O   1 
HETATM 4209 O O   . HOH   C 3 .   ? 29.109  11.047  -20.311 1.00 31.61  ? 2321 HOH   A O   1 
HETATM 4210 O O   . HOH   C 3 .   ? 27.583  20.977  -19.113 1.00 38.84  ? 2322 HOH   A O   1 
HETATM 4211 O O   . HOH   C 3 .   ? -33.906 -17.924 -15.249 1.00 40.65  ? 2323 HOH   A O   1 
HETATM 4212 O O   . HOH   C 3 .   ? -5.235  5.965   -28.214 1.00 49.08  ? 2324 HOH   A O   1 
HETATM 4213 O O   . HOH   C 3 .   ? -26.881 -4.621  -18.752 1.00 47.17  ? 2325 HOH   A O   1 
HETATM 4214 O O   . HOH   C 3 .   ? 13.096  -5.616  -5.166  1.00 37.01  ? 2326 HOH   A O   1 
HETATM 4215 O O   . HOH   C 3 .   ? -17.083 -1.675  -24.848 1.00 29.24  ? 2327 HOH   A O   1 
HETATM 4216 O O   . HOH   C 3 .   ? -6.268  -13.805 -25.435 1.00 41.02  ? 2328 HOH   A O   1 
HETATM 4217 O O   . HOH   C 3 .   ? -32.811 -34.414 -18.657 1.00 46.63  ? 2329 HOH   A O   1 
HETATM 4218 O O   . HOH   C 3 .   ? 19.046  23.743  -1.353  1.00 43.26  ? 2330 HOH   A O   1 
HETATM 4219 O O   . HOH   C 3 .   ? -34.659 -15.818 -20.571 1.00 38.43  ? 2331 HOH   A O   1 
HETATM 4220 O O   . HOH   C 3 .   ? -2.286  -0.094  -22.431 1.00 37.03  ? 2332 HOH   A O   1 
HETATM 4221 O O   . HOH   C 3 .   ? -5.436  -16.364 -32.383 1.00 50.06  ? 2333 HOH   A O   1 
HETATM 4222 O O   . HOH   C 3 .   ? 29.844  26.196  -19.214 1.00 36.20  ? 2334 HOH   A O   1 
HETATM 4223 O O   . HOH   C 3 .   ? 15.658  4.870   -20.757 1.00 50.23  ? 2335 HOH   A O   1 
HETATM 4224 O O   . HOH   C 3 .   ? 42.595  23.137  0.372   1.00 40.20  ? 2336 HOH   A O   1 
HETATM 4225 O O   . HOH   C 3 .   ? 16.433  -6.646  -4.829  1.00 41.77  ? 2337 HOH   A O   1 
HETATM 4226 O O   . HOH   C 3 .   ? 35.889  11.807  5.148   1.00 42.19  ? 2338 HOH   A O   1 
HETATM 4227 O O   . HOH   C 3 .   ? -15.121 -37.174 -39.576 1.00 50.24  ? 2339 HOH   A O   1 
HETATM 4228 O O   . HOH   C 3 .   ? -23.781 -3.622  -24.839 1.00 41.60  ? 2340 HOH   A O   1 
HETATM 4229 O O   . HOH   C 3 .   ? -31.323 -24.692 -22.655 1.00 26.96  ? 2341 HOH   A O   1 
HETATM 4230 O O   . HOH   C 3 .   ? 25.745  -9.488  1.847   1.00 48.53  ? 2342 HOH   A O   1 
HETATM 4231 O O   . HOH   C 3 .   ? 7.583   2.585   0.589   1.00 42.45  ? 2343 HOH   A O   1 
HETATM 4232 O O   . HOH   C 3 .   ? -36.886 -18.532 -18.241 1.00 52.89  ? 2344 HOH   A O   1 
HETATM 4233 O O   . HOH   C 3 .   ? 16.532  -6.415  0.142   1.00 42.47  ? 2345 HOH   A O   1 
HETATM 4234 O O   . HOH   C 3 .   ? -20.821 -4.491  -31.626 1.00 51.77  ? 2346 HOH   A O   1 
HETATM 4235 O O   . HOH   C 3 .   ? 40.140  11.735  -0.601  1.00 36.06  ? 2347 HOH   A O   1 
HETATM 4236 O O   . HOH   C 3 .   ? 12.167  11.063  -2.443  1.00 36.39  ? 2348 HOH   A O   1 
HETATM 4237 O O   . HOH   C 3 .   ? -42.489 -23.475 -27.847 1.00 54.16  ? 2349 HOH   A O   1 
HETATM 4238 O O   . HOH   C 3 .   ? 34.250  23.143  0.167   1.00 36.57  ? 2350 HOH   A O   1 
HETATM 4239 O O   . HOH   C 3 .   ? 42.723  20.807  -14.919 1.00 45.07  ? 2351 HOH   A O   1 
HETATM 4240 O O   . HOH   C 3 .   ? 13.543  9.928   -11.621 1.00 42.52  ? 2352 HOH   A O   1 
HETATM 4241 O O   . HOH   C 3 .   ? 32.991  26.019  -19.003 1.00 42.00  ? 2353 HOH   A O   1 
HETATM 4242 O O   . HOH   C 3 .   ? 26.253  -11.669 -10.158 1.00 60.78  ? 2354 HOH   A O   1 
HETATM 4243 O O   . HOH   C 3 .   ? -34.499 -30.639 -25.002 1.00 33.63  ? 2355 HOH   A O   1 
HETATM 4244 O O   . HOH   C 3 .   ? -21.049 -18.916 -37.059 1.00 29.92  ? 2356 HOH   A O   1 
HETATM 4245 O O   . HOH   C 3 .   ? 6.628   2.303   -2.024  1.00 31.52  ? 2357 HOH   A O   1 
HETATM 4246 O O   . HOH   C 3 .   ? -10.024 -25.586 -19.677 1.00 46.44  ? 2358 HOH   A O   1 
HETATM 4247 O O   . HOH   C 3 .   ? 4.595   -1.027  -30.263 1.00 53.78  ? 2359 HOH   A O   1 
HETATM 4248 O O   . HOH   C 3 .   ? 9.255   21.962  -8.678  1.00 47.10  ? 2360 HOH   A O   1 
HETATM 4249 O O   . HOH   C 3 .   ? 24.058  29.515  -7.221  1.00 37.34  ? 2361 HOH   A O   1 
HETATM 4250 O O   . HOH   C 3 .   ? -4.257  2.194   -16.629 1.00 44.94  ? 2362 HOH   A O   1 
HETATM 4251 O O   . HOH   C 3 .   ? -25.812 -24.872 -13.232 1.00 36.45  ? 2363 HOH   A O   1 
HETATM 4252 O O   . HOH   C 3 .   ? -17.718 -11.201 -38.631 1.00 37.99  ? 2364 HOH   A O   1 
HETATM 4253 O O   . HOH   C 3 .   ? 9.864   1.503   1.252   1.00 56.80  ? 2365 HOH   A O   1 
HETATM 4254 O O   . HOH   C 3 .   ? -39.696 -29.739 -19.011 1.00 44.47  ? 2366 HOH   A O   1 
HETATM 4255 O O   . HOH   C 3 .   ? -37.440 -28.322 -18.639 1.00 41.36  ? 2367 HOH   A O   1 
HETATM 4256 O O   . HOH   C 3 .   ? -3.845  8.353   -13.066 1.00 38.39  ? 2368 HOH   A O   1 
HETATM 4257 O O   . HOH   C 3 .   ? 16.909  -11.397 4.341   1.00 52.55  ? 2369 HOH   A O   1 
HETATM 4258 O O   . HOH   C 3 .   ? -2.477  1.717   -3.153  1.00 59.41  ? 2370 HOH   A O   1 
HETATM 4259 O O   . HOH   C 3 .   ? -21.122 -16.059 -30.437 1.00 30.11  ? 2371 HOH   A O   1 
HETATM 4260 O O   . HOH   C 3 .   ? 23.278  16.384  3.016   1.00 45.61  ? 2372 HOH   A O   1 
HETATM 4261 O O   . HOH   C 3 .   ? -26.968 -12.030 -31.652 1.00 31.28  ? 2373 HOH   A O   1 
HETATM 4262 O O   . HOH   C 3 .   ? 18.914  5.210   -12.050 1.00 35.35  ? 2374 HOH   A O   1 
HETATM 4263 O O   . HOH   C 3 .   ? 31.800  31.921  -16.200 1.00 32.51  ? 2375 HOH   A O   1 
HETATM 4264 O O   . HOH   C 3 .   ? 10.131  24.022  -11.300 1.00 46.67  ? 2376 HOH   A O   1 
HETATM 4265 O O   . HOH   C 3 .   ? -24.230 -4.988  -9.777  1.00 42.08  ? 2377 HOH   A O   1 
HETATM 4266 O O   . HOH   C 3 .   ? 23.469  -9.830  -0.274  1.00 51.59  ? 2378 HOH   A O   1 
HETATM 4267 O O   . HOH   C 3 .   ? -28.663 -9.637  -17.856 1.00 33.82  ? 2379 HOH   A O   1 
HETATM 4268 O O   . HOH   C 3 .   ? -27.558 -30.193 -15.534 1.00 38.24  ? 2380 HOH   A O   1 
HETATM 4269 O O   . HOH   C 3 .   ? -34.367 -5.934  -23.106 1.00 45.05  ? 2381 HOH   A O   1 
HETATM 4270 O O   . HOH   C 3 .   ? -23.369 -7.433  -26.109 1.00 47.33  ? 2382 HOH   A O   1 
HETATM 4271 O O   . HOH   C 3 .   ? 2.504   7.611   -23.021 1.00 53.67  ? 2383 HOH   A O   1 
HETATM 4272 O O   . HOH   C 3 .   ? -14.822 -34.149 -33.703 1.00 48.29  ? 2384 HOH   A O   1 
HETATM 4273 O O   . HOH   C 3 .   ? 0.900   -8.990  -10.358 1.00 40.76  ? 2385 HOH   A O   1 
HETATM 4274 O O   . HOH   C 3 .   ? -18.935 -35.549 -39.836 1.00 28.25  ? 2386 HOH   A O   1 
HETATM 4275 O O   . HOH   C 3 .   ? 16.332  10.506  -2.522  1.00 44.25  ? 2387 HOH   A O   1 
HETATM 4276 O O   . HOH   C 3 .   ? -9.605  -16.625 -26.234 1.00 55.94  ? 2388 HOH   A O   1 
HETATM 4277 O O   . HOH   C 3 .   ? 20.644  -14.299 4.329   1.00 53.45  ? 2389 HOH   A O   1 
HETATM 4278 O O   . HOH   C 3 .   ? -24.280 -33.577 -30.783 1.00 41.34  ? 2390 HOH   A O   1 
HETATM 4279 O O   . HOH   C 3 .   ? 28.539  -5.041  1.068   1.00 35.49  ? 2391 HOH   A O   1 
HETATM 4280 O O   . HOH   C 3 .   ? 28.787  -5.153  -20.386 1.00 44.04  ? 2392 HOH   A O   1 
HETATM 4281 O O   . HOH   C 3 .   ? -2.638  -5.462  -3.045  1.00 51.32  ? 2393 HOH   A O   1 
HETATM 4282 O O   . HOH   C 3 .   ? -7.958  0.600   -35.911 1.00 53.73  ? 2394 HOH   A O   1 
HETATM 4283 O O   . HOH   C 3 .   ? -29.732 -23.202 -30.066 1.00 44.89  ? 2395 HOH   A O   1 
HETATM 4284 O O   . HOH   C 3 .   ? -15.052 2.921   -18.970 1.00 51.43  ? 2396 HOH   A O   1 
HETATM 4285 O O   . HOH   C 3 .   ? 7.410   15.090  -7.995  1.00 54.97  ? 2397 HOH   A O   1 
HETATM 4286 O O   . HOH   C 3 .   ? -24.676 -19.197 -33.205 1.00 44.29  ? 2398 HOH   A O   1 
HETATM 4287 O O   . HOH   C 3 .   ? 2.813   -10.427 -18.734 1.00 50.95  ? 2399 HOH   A O   1 
HETATM 4288 O O   . HOH   C 3 .   ? 40.940  8.925   -0.053  1.00 41.94  ? 2400 HOH   A O   1 
HETATM 4289 O O   . HOH   C 3 .   ? 24.186  -6.385  -27.187 1.00 50.86  ? 2401 HOH   A O   1 
HETATM 4290 O O   . HOH   C 3 .   ? -6.216  4.104   -16.656 1.00 48.65  ? 2402 HOH   A O   1 
HETATM 4291 O O   . HOH   C 3 .   ? 41.182  9.210   -4.165  1.00 49.49  ? 2403 HOH   A O   1 
HETATM 4292 O O   . HOH   C 3 .   ? 39.138  1.098   -1.407  1.00 52.91  ? 2404 HOH   A O   1 
HETATM 4293 O O   . HOH   C 3 .   ? -34.112 -24.730 -22.260 1.00 29.70  ? 2405 HOH   A O   1 
HETATM 4294 O O   . HOH   C 3 .   ? 0.528   -10.752 -17.993 1.00 42.49  ? 2406 HOH   A O   1 
HETATM 4295 O O   . HOH   C 3 .   ? 28.267  8.977   -22.098 1.00 36.18  ? 2407 HOH   A O   1 
HETATM 4296 O O   . HOH   C 3 .   ? -8.294  5.158   -8.340  1.00 51.22  ? 2408 HOH   A O   1 
HETATM 4297 O O   . HOH   C 3 .   ? -2.390  -17.799 -23.969 1.00 53.76  ? 2409 HOH   A O   1 
HETATM 4298 O O   . HOH   C 3 .   ? 18.041  19.273  -13.093 1.00 32.90  ? 2410 HOH   A O   1 
HETATM 4299 O O   . HOH   C 3 .   ? -12.969 4.309   -0.424  1.00 58.07  ? 2411 HOH   A O   1 
HETATM 4300 O O   . HOH   C 3 .   ? -33.272 -30.605 -28.314 1.00 52.85  ? 2412 HOH   A O   1 
HETATM 4301 O O   . HOH   C 3 .   ? -14.231 2.249   -9.998  1.00 37.16  ? 2413 HOH   A O   1 
HETATM 4302 O O   . HOH   C 3 .   ? -37.012 -29.237 -25.298 1.00 48.90  ? 2414 HOH   A O   1 
HETATM 4303 O O   . HOH   C 3 .   ? -2.678  -7.999  -3.862  1.00 40.99  ? 2415 HOH   A O   1 
HETATM 4304 O O   . HOH   C 3 .   ? 44.797  3.492   -7.163  1.00 54.77  ? 2416 HOH   A O   1 
HETATM 4305 O O   . HOH   C 3 .   ? -0.723  -9.821  -29.279 1.00 48.40  ? 2417 HOH   A O   1 
HETATM 4306 O O   . HOH   C 3 .   ? 6.405   -9.812  -8.191  1.00 47.81  ? 2418 HOH   A O   1 
HETATM 4307 O O   . HOH   C 3 .   ? -40.036 -31.363 -16.586 1.00 50.39  ? 2419 HOH   A O   1 
HETATM 4308 O O   . HOH   C 3 .   ? 25.644  7.051   -26.224 1.00 56.79  ? 2420 HOH   A O   1 
HETATM 4309 O O   . HOH   C 3 .   ? -16.802 -30.591 -38.081 1.00 54.80  ? 2421 HOH   A O   1 
HETATM 4310 O O   . HOH   C 3 .   ? 17.744  25.548  -2.231  1.00 48.82  ? 2422 HOH   A O   1 
HETATM 4311 O O   . HOH   C 3 .   ? 33.154  12.826  -21.108 1.00 52.23  ? 2423 HOH   A O   1 
HETATM 4312 O O   . HOH   C 3 .   ? -31.688 -5.362  -23.896 1.00 45.51  ? 2424 HOH   A O   1 
HETATM 4313 O O   . HOH   C 3 .   ? 25.718  -0.489  14.074  1.00 52.13  ? 2425 HOH   A O   1 
HETATM 4314 O O   . HOH   C 3 .   ? 16.576  16.639  -12.326 1.00 51.49  ? 2426 HOH   A O   1 
HETATM 4315 O O   . HOH   C 3 .   ? 31.529  -4.519  -1.879  1.00 54.29  ? 2427 HOH   A O   1 
HETATM 4316 O O   . HOH   C 3 .   ? -21.380 -0.042  -13.105 1.00 55.95  ? 2428 HOH   A O   1 
HETATM 4317 O O   . HOH   C 3 .   ? 45.395  5.498   -9.844  1.00 54.33  ? 2429 HOH   A O   1 
HETATM 4318 O O   . HOH   C 3 .   ? 20.534  31.468  -14.241 1.00 34.24  ? 2430 HOH   A O   1 
HETATM 4319 O O   . HOH   C 3 .   ? 15.847  26.734  -0.287  1.00 56.54  ? 2431 HOH   A O   1 
HETATM 4320 O O   . HOH   C 3 .   ? -20.689 -2.094  -22.029 1.00 42.63  ? 2432 HOH   A O   1 
HETATM 4321 O O   . HOH   C 3 .   ? -21.853 -6.398  -29.920 1.00 48.48  ? 2433 HOH   A O   1 
HETATM 4322 O O   . HOH   C 3 .   ? -27.637 -14.230 -30.214 1.00 44.95  ? 2434 HOH   A O   1 
HETATM 4323 O O   . HOH   C 3 .   ? -27.929 -8.821  -14.019 1.00 47.76  ? 2435 HOH   A O   1 
HETATM 4324 O O   . HOH   C 3 .   ? -3.877  -13.012 -23.271 1.00 38.71  ? 2436 HOH   A O   1 
HETATM 4325 O O   . HOH   C 3 .   ? 33.959  33.575  -16.996 1.00 48.60  ? 2437 HOH   A O   1 
HETATM 4326 O O   . HOH   C 3 .   ? 32.517  25.090  0.493   1.00 44.26  ? 2438 HOH   A O   1 
HETATM 4327 O O   . HOH   C 3 .   ? -10.881 -21.317 -14.780 1.00 51.59  ? 2439 HOH   A O   1 
HETATM 4328 O O   . HOH   C 3 .   ? -6.562  -18.238 -14.000 1.00 35.99  ? 2440 HOH   A O   1 
HETATM 4329 O O   . HOH   C 3 .   ? -1.620  6.114   -30.973 1.00 50.21  ? 2441 HOH   A O   1 
HETATM 4330 O O   . HOH   C 3 .   ? -26.380 -8.735  -7.061  1.00 53.75  ? 2442 HOH   A O   1 
HETATM 4331 O O   . HOH   C 3 .   ? 20.408  18.118  1.075   1.00 35.67  ? 2443 HOH   A O   1 
HETATM 4332 O O   . HOH   C 3 .   ? 20.026  14.349  9.329   1.00 50.54  ? 2444 HOH   A O   1 
HETATM 4333 O O   . HOH   C 3 .   ? -12.905 5.772   -3.044  1.00 59.55  ? 2445 HOH   A O   1 
HETATM 4334 O O   . HOH   C 3 .   ? -19.542 -3.336  -24.180 1.00 30.12  ? 2446 HOH   A O   1 
HETATM 4335 O O   . HOH   C 3 .   ? -26.524 -14.602 -6.732  1.00 53.85  ? 2447 HOH   A O   1 
HETATM 4336 O O   . HOH   C 3 .   ? -7.733  -19.532 -15.613 1.00 48.25  ? 2448 HOH   A O   1 
HETATM 4337 O O   . HOH   C 3 .   ? -36.307 -35.018 -20.833 1.00 51.90  ? 2449 HOH   A O   1 
HETATM 4338 O O   . HOH   C 3 .   ? 10.972  16.615  -1.857  1.00 58.22  ? 2450 HOH   A O   1 
HETATM 4339 O O   . HOH   C 3 .   ? 5.056   13.623  -10.752 1.00 46.77  ? 2451 HOH   A O   1 
HETATM 4340 O O   . HOH   C 3 .   ? 14.030  11.354  -1.073  1.00 47.49  ? 2452 HOH   A O   1 
HETATM 4341 O O   . HOH   C 3 .   ? 0.071   -1.614  -3.957  1.00 48.08  ? 2453 HOH   A O   1 
HETATM 4342 O O   . HOH   C 3 .   ? 11.749  15.334  -0.304  1.00 60.27  ? 2454 HOH   A O   1 
HETATM 4343 O O   . HOH   C 3 .   ? -24.067 -24.964 -9.179  1.00 53.53  ? 2455 HOH   A O   1 
HETATM 4344 O O   . HOH   C 3 .   ? -10.067 -19.352 -16.197 1.00 46.56  ? 2456 HOH   A O   1 
HETATM 4345 O O   . HOH   C 3 .   ? -4.057  -12.750 -11.700 1.00 36.69  ? 2457 HOH   A O   1 
HETATM 4346 O O   . HOH   C 3 .   ? -20.672 -2.078  -16.217 1.00 55.28  ? 2458 HOH   A O   1 
HETATM 4347 O O   . HOH   C 3 .   ? 32.721  -7.658  6.498   1.00 51.87  ? 2459 HOH   A O   1 
HETATM 4348 O O   . HOH   C 3 .   ? 38.371  8.502   -2.333  1.00 43.57  ? 2460 HOH   A O   1 
HETATM 4349 O O   . HOH   C 3 .   ? -17.284 -9.836  -41.055 1.00 46.36  ? 2461 HOH   A O   1 
HETATM 4350 O O   . HOH   C 3 .   ? 16.660  11.810  9.505   1.00 48.00  ? 2462 HOH   A O   1 
HETATM 4351 O O   . HOH   C 3 .   ? 22.967  18.174  1.895   1.00 43.57  ? 2463 HOH   A O   1 
HETATM 4352 O O   . HOH   C 3 .   ? -10.557 4.005   -22.269 1.00 52.99  ? 2464 HOH   A O   1 
HETATM 4353 O O   . HOH   C 3 .   ? 27.986  -6.953  -29.638 1.00 55.59  ? 2465 HOH   A O   1 
HETATM 4354 O O   . HOH   C 3 .   ? -25.798 -27.128 -12.205 1.00 53.47  ? 2466 HOH   A O   1 
HETATM 4355 O O   . HOH   C 3 .   ? -16.161 -32.270 -40.312 1.00 50.54  ? 2467 HOH   A O   1 
HETATM 4356 O O   . HOH   C 3 .   ? -36.252 -25.746 -28.520 1.00 44.70  ? 2468 HOH   A O   1 
HETATM 4357 O O   . HOH   C 3 .   ? 39.070  18.527  -20.021 1.00 49.59  ? 2469 HOH   A O   1 
HETATM 4358 O O   . HOH   C 3 .   ? 26.554  -7.029  -26.870 1.00 51.15  ? 2470 HOH   A O   1 
HETATM 4359 O O   . HOH   C 3 .   ? 41.202  19.056  -17.881 1.00 57.15  ? 2471 HOH   A O   1 
HETATM 4360 O O   . HOH   C 3 .   ? 11.750  29.782  -2.019  1.00 56.26  ? 2472 HOH   A O   1 
HETATM 4361 O O   . HOH   C 3 .   ? -39.041 -31.741 -20.743 1.00 45.42  ? 2473 HOH   A O   1 
HETATM 4362 O O   . HOH   C 3 .   ? -5.183  4.438   -20.986 1.00 54.24  ? 2474 HOH   A O   1 
HETATM 4363 O O   . HOH   C 3 .   ? -4.709  2.347   -12.409 1.00 39.62  ? 2475 HOH   A O   1 
HETATM 4364 O O   . HOH   C 3 .   ? -26.589 -7.212  -12.913 1.00 37.64  ? 2476 HOH   A O   1 
HETATM 4365 O O   . HOH   C 3 .   ? -5.820  -16.918 -6.946  1.00 51.85  ? 2477 HOH   A O   1 
HETATM 4366 O O   . HOH   C 3 .   ? 14.520  28.725  -2.037  1.00 46.47  ? 2478 HOH   A O   1 
HETATM 4367 O O   . HOH   C 3 .   ? -26.956 -17.094 -6.835  1.00 56.18  ? 2479 HOH   A O   1 
HETATM 4368 O O   . HOH   C 3 .   ? 40.418  12.405  -2.911  1.00 52.43  ? 2480 HOH   A O   1 
HETATM 4369 O O   . HOH   C 3 .   ? 19.572  -12.672 3.206   1.00 52.72  ? 2481 HOH   A O   1 
HETATM 4370 O O   . HOH   C 3 .   ? -37.368 -23.545 -29.241 1.00 48.88  ? 2482 HOH   A O   1 
HETATM 4371 O O   . HOH   C 3 .   ? 19.514  33.141  -10.278 1.00 49.05  ? 2483 HOH   A O   1 
HETATM 4372 O O   . HOH   C 3 .   ? -29.616 -25.329 -11.349 1.00 48.17  ? 2484 HOH   A O   1 
HETATM 4373 O O   . HOH   C 3 .   ? -28.874 -7.880  -29.130 1.00 49.83  ? 2485 HOH   A O   1 
HETATM 4374 O O   . HOH   C 3 .   ? -7.302  -32.075 -40.200 1.00 50.04  ? 2486 HOH   A O   1 
HETATM 4375 O O   . HOH   C 3 .   ? 24.606  18.359  0.114   1.00 40.68  ? 2487 HOH   A O   1 
HETATM 4376 O O   . HOH   C 3 .   ? -31.743 -32.221 -32.693 1.00 45.92  ? 2488 HOH   A O   1 
HETATM 4377 O O   . HOH   C 3 .   ? 24.057  34.618  -11.361 1.00 59.32  ? 2489 HOH   A O   1 
HETATM 4378 O O   . HOH   C 3 .   ? -21.357 -3.934  -26.130 1.00 31.93  ? 2490 HOH   A O   1 
HETATM 4379 O O   . HOH   C 3 .   ? -37.236 -20.389 -17.015 1.00 44.54  ? 2491 HOH   A O   1 
HETATM 4380 O O   . HOH   C 3 .   ? 21.687  33.872  -14.448 1.00 43.19  ? 2492 HOH   A O   1 
HETATM 4381 O O   . HOH   C 3 .   ? -18.753 1.433   -22.678 1.00 54.31  ? 2493 HOH   A O   1 
HETATM 4382 O O   . HOH   C 3 .   ? 28.898  16.720  0.999   1.00 44.39  ? 2494 HOH   A O   1 
HETATM 4383 O O   . HOH   C 3 .   ? 17.470  14.460  -11.606 1.00 48.49  ? 2495 HOH   A O   1 
HETATM 4384 O O   . HOH   C 3 .   ? -26.542 -33.170 -20.239 1.00 49.42  ? 2496 HOH   A O   1 
HETATM 4385 O O   . HOH   C 3 .   ? 29.684  -12.228 -17.249 1.00 48.98  ? 2497 HOH   A O   1 
HETATM 4386 O O   . HOH   C 3 .   ? 13.337  7.296   -12.152 1.00 44.97  ? 2498 HOH   A O   1 
HETATM 4387 O O   . HOH   C 3 .   ? -31.752 -19.108 -12.706 1.00 42.36  ? 2499 HOH   A O   1 
HETATM 4388 O O   . HOH   C 3 .   ? 29.303  -1.273  -27.533 1.00 50.34  ? 2500 HOH   A O   1 
HETATM 4389 O O   . HOH   C 3 .   ? 29.682  33.343  -12.203 1.00 52.05  ? 2501 HOH   A O   1 
HETATM 4390 O O   . HOH   C 3 .   ? 26.772  33.202  -8.534  1.00 44.68  ? 2502 HOH   A O   1 
HETATM 4391 O O   . HOH   C 3 .   ? -22.335 -18.366 -26.918 1.00 42.35  ? 2503 HOH   A O   1 
HETATM 4392 O O   . HOH   C 3 .   ? -29.131 -6.942  -20.916 1.00 43.10  ? 2504 HOH   A O   1 
HETATM 4393 O O   . HOH   C 3 .   ? 27.989  33.786  -21.797 1.00 37.49  ? 2505 HOH   A O   1 
HETATM 4394 O O   . HOH   C 3 .   ? -22.219 -25.343 -31.741 1.00 40.81  ? 2506 HOH   A O   1 
HETATM 4395 O O   . HOH   C 3 .   ? -0.513  -11.045 -11.694 1.00 42.82  ? 2507 HOH   A O   1 
HETATM 4396 O O   . HOH   C 3 .   ? -2.466  -17.868 -12.984 1.00 59.55  ? 2508 HOH   A O   1 
HETATM 4397 O O   . HOH   C 3 .   ? 3.343   6.792   -0.973  1.00 60.09  ? 2509 HOH   A O   1 
HETATM 4398 O O   . HOH   C 3 .   ? 22.197  31.271  -7.549  1.00 35.32  ? 2510 HOH   A O   1 
HETATM 4399 O O   . HOH   C 3 .   ? 8.953   -5.844  -24.697 1.00 56.81  ? 2511 HOH   A O   1 
HETATM 4400 O O   . HOH   C 3 .   ? 15.134  10.877  14.060  1.00 57.99  ? 2512 HOH   A O   1 
HETATM 4401 O O   . HOH   C 3 .   ? -18.404 2.952   -13.229 1.00 49.94  ? 2513 HOH   A O   1 
HETATM 4402 O O   . HOH   C 3 .   ? 23.559  33.550  -8.852  1.00 45.52  ? 2514 HOH   A O   1 
HETATM 4403 O O   . HOH   C 3 .   ? 10.430  14.847  -8.149  1.00 51.90  ? 2515 HOH   A O   1 
HETATM 4404 O O   . HOH   C 3 .   ? 11.847  7.360   -0.230  1.00 44.88  ? 2516 HOH   A O   1 
HETATM 4405 O O   . HOH   C 3 .   ? -19.328 -20.638 -35.880 1.00 36.75  ? 2517 HOH   A O   1 
HETATM 4406 O O   . HOH   C 3 .   ? 4.433   13.496  -15.210 1.00 53.51  ? 2518 HOH   A O   1 
HETATM 4407 O O   . HOH   C 3 .   ? -28.147 -23.593 -12.798 1.00 39.96  ? 2519 HOH   A O   1 
HETATM 4408 O O   . HOH   C 3 .   ? -16.003 -25.930 -15.400 1.00 50.20  ? 2520 HOH   A O   1 
HETATM 4409 O O   . HOH   C 3 .   ? -23.267 -7.782  -37.350 1.00 55.81  ? 2521 HOH   A O   1 
HETATM 4410 O O   . HOH   C 3 .   ? -18.956 -23.038 -37.162 1.00 49.04  ? 2522 HOH   A O   1 
HETATM 4411 O O   . HOH   C 3 .   ? -3.561  -21.565 -21.604 1.00 50.82  ? 2523 HOH   A O   1 
HETATM 4412 O O   . HOH   C 3 .   ? 30.526  -3.321  -19.412 1.00 58.40  ? 2524 HOH   A O   1 
HETATM 4413 O O   . HOH   C 3 .   ? 29.621  21.167  -20.627 1.00 41.18  ? 2525 HOH   A O   1 
HETATM 4414 O O   . HOH   C 3 .   ? -30.889 -35.271 -20.531 1.00 52.69  ? 2526 HOH   A O   1 
HETATM 4415 O O   . HOH   C 3 .   ? -25.002 -3.616  -14.068 1.00 44.16  ? 2527 HOH   A O   1 
HETATM 4416 O O   . HOH   C 3 .   ? -34.342 -32.343 -26.924 1.00 57.12  ? 2528 HOH   A O   1 
HETATM 4417 O O   . HOH   C 3 .   ? -37.805 -24.504 -15.802 1.00 43.14  ? 2529 HOH   A O   1 
HETATM 4418 O O   . HOH   C 3 .   ? -22.537 -5.622  -33.582 1.00 57.69  ? 2530 HOH   A O   1 
HETATM 4419 O O   . HOH   C 3 .   ? -13.154 -30.027 -30.507 1.00 54.15  ? 2531 HOH   A O   1 
HETATM 4420 O O   . HOH   C 3 .   ? -9.024  2.646   -11.743 1.00 44.69  ? 2532 HOH   A O   1 
HETATM 4421 O O   . HOH   C 3 .   ? -16.338 0.167   -22.793 1.00 38.47  ? 2533 HOH   A O   1 
HETATM 4422 O O   . HOH   C 3 .   ? 25.795  34.056  -15.602 1.00 54.17  ? 2534 HOH   A O   1 
HETATM 4423 O O   . HOH   C 3 .   ? 8.192   10.397  -2.439  1.00 38.70  ? 2535 HOH   A O   1 
HETATM 4424 O O   . HOH   C 3 .   ? 29.454  32.220  -17.802 1.00 38.23  ? 2536 HOH   A O   1 
HETATM 4425 O O   . HOH   C 3 .   ? 38.491  4.175   -19.500 1.00 44.63  ? 2537 HOH   A O   1 
HETATM 4426 O O   . HOH   C 3 .   ? 27.871  28.124  -19.589 1.00 33.40  ? 2538 HOH   A O   1 
HETATM 4427 O O   . HOH   C 3 .   ? -35.619 -14.190 -18.729 1.00 35.87  ? 2539 HOH   A O   1 
HETATM 4428 O O   . HOH   C 3 .   ? 31.658  22.723  -20.581 1.00 41.39  ? 2540 HOH   A O   1 
HETATM 4429 O O   . HOH   C 3 .   ? -37.447 -32.618 -24.591 1.00 53.45  ? 2541 HOH   A O   1 
HETATM 4430 O O   . HOH   C 3 .   ? -37.486 -27.310 -15.670 1.00 45.77  ? 2542 HOH   A O   1 
HETATM 4431 O O   . HOH   C 3 .   ? 20.854  -3.806  -26.745 1.00 47.13  ? 2543 HOH   A O   1 
HETATM 4432 O O   . HOH   C 3 .   ? 28.135  -5.255  -25.515 1.00 44.94  ? 2544 HOH   A O   1 
HETATM 4433 O O   . HOH   C 3 .   ? 17.975  13.903  8.036   1.00 49.56  ? 2545 HOH   A O   1 
HETATM 4434 O O   . HOH   C 3 .   ? -25.131 -11.336 -35.660 1.00 30.28  ? 2546 HOH   A O   1 
HETATM 4435 O O   . HOH   C 3 .   ? -25.196 -5.725  -26.612 1.00 40.49  ? 2547 HOH   A O   1 
HETATM 4436 O O   . HOH   C 3 .   ? -22.741 -23.179 -30.858 1.00 45.56  ? 2548 HOH   A O   1 
HETATM 4437 O O   . HOH   C 3 .   ? 19.318  16.026  4.862   1.00 51.88  ? 2549 HOH   A O   1 
HETATM 4438 O O   . HOH   C 3 .   ? -27.292 -12.433 -34.510 1.00 30.27  ? 2550 HOH   A O   1 
HETATM 4439 O O   . HOH   C 3 .   ? 25.510  22.057  -20.913 1.00 46.19  ? 2551 HOH   A O   1 
HETATM 4440 O O   . HOH   C 3 .   ? 33.418  34.567  -12.924 1.00 55.73  ? 2552 HOH   A O   1 
HETATM 4441 O O   . HOH   C 3 .   ? 9.164   12.767  -12.631 1.00 55.32  ? 2553 HOH   A O   1 
HETATM 4442 O O   . HOH   C 3 .   ? -25.738 -6.404  -7.942  1.00 47.19  ? 2554 HOH   A O   1 
HETATM 4443 O O   . HOH   C 3 .   ? -25.982 -8.322  -32.833 1.00 43.09  ? 2555 HOH   A O   1 
HETATM 4444 O O   . HOH   C 3 .   ? 1.286   -5.927  9.535   1.00 63.44  ? 2556 HOH   A O   1 
HETATM 4445 O O   . HOH   C 3 .   ? 27.810  -7.866  0.656   1.00 50.52  ? 2557 HOH   A O   1 
HETATM 4446 O O   . HOH   C 3 .   ? -31.396 -36.825 -12.618 1.00 56.28  ? 2558 HOH   A O   1 
HETATM 4447 O O   . HOH   C 3 .   ? -39.707 -20.672 -15.948 1.00 50.84  ? 2559 HOH   A O   1 
HETATM 4448 O O   . HOH   C 3 .   ? -23.514 -3.925  -35.750 1.00 59.78  ? 2560 HOH   A O   1 
HETATM 4449 O O   . HOH   C 3 .   ? -24.743 -5.557  -29.014 1.00 51.43  ? 2561 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LEU A 25  ? 0.6894 0.7347 0.6949 -0.0029 -0.0162 -0.0679 -4   LEU A N   
2    C CA  . LEU A 25  ? 0.6658 0.7166 0.6698 -0.0042 -0.0147 -0.0735 -4   LEU A CA  
3    C C   . LEU A 25  ? 0.5791 0.6310 0.5821 -0.0043 -0.0168 -0.0755 -4   LEU A C   
4    O O   . LEU A 25  ? 0.6548 0.7080 0.6529 -0.0072 -0.0154 -0.0761 -4   LEU A O   
5    C CB  . LEU A 25  ? 0.7954 0.8497 0.8042 -0.0021 -0.0149 -0.0784 -4   LEU A CB  
6    C CG  . LEU A 25  ? 0.8026 0.8623 0.8100 -0.0040 -0.0113 -0.0828 -4   LEU A CG  
7    C CD1 . LEU A 25  ? 0.7639 0.8274 0.7663 -0.0076 -0.0094 -0.0854 -4   LEU A CD1 
8    C CD2 . LEU A 25  ? 0.8718 0.9295 0.8776 -0.0051 -0.0084 -0.0790 -4   LEU A CD2 
9    N N   . TYR A 26  ? 0.4926 0.5435 0.4998 -0.0014 -0.0203 -0.0765 -3   TYR A N   
10   C CA  . TYR A 26  ? 0.4229 0.4749 0.4299 -0.0010 -0.0226 -0.0783 -3   TYR A CA  
11   C C   . TYR A 26  ? 0.3534 0.4000 0.3605 0.0001  -0.0252 -0.0735 -3   TYR A C   
12   O O   . TYR A 26  ? 0.3687 0.4153 0.3765 0.0012  -0.0277 -0.0745 -3   TYR A O   
13   C CB  . TYR A 26  ? 0.4956 0.5516 0.5073 0.0015  -0.0249 -0.0843 -3   TYR A CB  
14   C CG  . TYR A 26  ? 0.4896 0.5514 0.5022 0.0007  -0.0225 -0.0899 -3   TYR A CG  
15   C CD1 . TYR A 26  ? 0.4698 0.5368 0.4789 -0.0027 -0.0194 -0.0932 -3   TYR A CD1 
16   C CD2 . TYR A 26  ? 0.5369 0.5988 0.5535 0.0029  -0.0231 -0.0919 -3   TYR A CD2 
17   C CE1 . TYR A 26  ? 0.5418 0.6147 0.5519 -0.0038 -0.0169 -0.0989 -3   TYR A CE1 
18   C CE2 . TYR A 26  ? 0.5174 0.5848 0.5352 0.0023  -0.0209 -0.0975 -3   TYR A CE2 
19   C CZ  . TYR A 26  ? 0.5613 0.6347 0.5761 -0.0011 -0.0176 -0.1011 -3   TYR A CZ  
20   O OH  . TYR A 26  ? 0.5642 0.6438 0.5804 -0.0021 -0.0150 -0.1073 -3   TYR A OH  
21   N N   . PHE A 27  ? 0.3456 0.3878 0.3523 -0.0001 -0.0246 -0.0686 -2   PHE A N   
22   C CA  . PHE A 27  ? 0.3633 0.4007 0.3705 0.0007  -0.0267 -0.0644 -2   PHE A CA  
23   C C   . PHE A 27  ? 0.3505 0.3848 0.3571 -0.0003 -0.0251 -0.0602 -2   PHE A C   
24   O O   . PHE A 27  ? 0.3376 0.3724 0.3459 0.0000  -0.0237 -0.0602 -2   PHE A O   
25   C CB  . PHE A 27  ? 0.3607 0.3966 0.3722 0.0033  -0.0299 -0.0651 -2   PHE A CB  
26   C CG  . PHE A 27  ? 0.3657 0.3969 0.3781 0.0038  -0.0316 -0.0613 -2   PHE A CG  
27   C CD1 . PHE A 27  ? 0.3364 0.3665 0.3479 0.0041  -0.0335 -0.0605 -2   PHE A CD1 
28   C CD2 . PHE A 27  ? 0.3996 0.4279 0.4140 0.0039  -0.0314 -0.0587 -2   PHE A CD2 
29   C CE1 . PHE A 27  ? 0.3151 0.3415 0.3280 0.0044  -0.0350 -0.0576 -2   PHE A CE1 
30   C CE2 . PHE A 27  ? 0.3734 0.3982 0.3891 0.0039  -0.0328 -0.0559 -2   PHE A CE2 
31   C CZ  . PHE A 27  ? 0.3131 0.3371 0.3281 0.0042  -0.0346 -0.0555 -2   PHE A CZ  
32   N N   . GLN A 28  ? 0.2872 0.3183 0.2915 -0.0013 -0.0256 -0.0569 -1   GLN A N   
33   C CA  . GLN A 28  ? 0.2556 0.2841 0.2599 -0.0020 -0.0246 -0.0533 -1   GLN A CA  
34   C C   . GLN A 28  ? 0.3017 0.3276 0.3105 -0.0005 -0.0264 -0.0514 -1   GLN A C   
35   O O   . GLN A 28  ? 0.3034 0.3276 0.3131 0.0003  -0.0287 -0.0511 -1   GLN A O   
36   C CB  . GLN A 28  ? 0.2748 0.3007 0.2740 -0.0039 -0.0247 -0.0512 -1   GLN A CB  
37   C CG  . GLN A 28  ? 0.3299 0.3577 0.3232 -0.0065 -0.0225 -0.0530 -1   GLN A CG  
38   C CD  . GLN A 28  ? 0.3575 0.3815 0.3441 -0.0087 -0.0234 -0.0513 -1   GLN A CD  
39   O OE1 . GLN A 28  ? 0.3738 0.3953 0.3565 -0.0106 -0.0227 -0.0493 -1   GLN A OE1 
40   N NE2 . GLN A 28  ? 0.3265 0.3496 0.3116 -0.0086 -0.0253 -0.0523 -1   GLN A NE2 
41   N N   . GLU A 29  ? 0.3331 0.3588 0.3446 -0.0003 -0.0252 -0.0504 566  GLU A N   
42   C CA  . GLU A 29  ? 0.3517 0.3751 0.3671 0.0003  -0.0264 -0.0489 566  GLU A CA  
43   C C   . GLU A 29  ? 0.3148 0.3363 0.3306 -0.0005 -0.0266 -0.0461 566  GLU A C   
44   O O   . GLU A 29  ? 0.3271 0.3485 0.3401 -0.0015 -0.0257 -0.0450 566  GLU A O   
45   C CB  . GLU A 29  ? 0.3468 0.3704 0.3645 0.0005  -0.0252 -0.0492 566  GLU A CB  
46   C CG  . GLU A 29  ? 0.4142 0.4388 0.4320 0.0018  -0.0261 -0.0525 566  GLU A CG  
47   C CD  . GLU A 29  ? 0.7081 0.7319 0.7277 0.0021  -0.0254 -0.0529 566  GLU A CD  
48   O OE1 . GLU A 29  ? 0.7716 0.7947 0.7921 0.0012  -0.0235 -0.0505 566  GLU A OE1 
49   O OE2 . GLU A 29  ? 0.7293 0.7529 0.7495 0.0034  -0.0271 -0.0558 566  GLU A OE2 
50   N N   . GLN A 30  ? 0.3234 0.3434 0.3427 -0.0004 -0.0279 -0.0454 567  GLN A N   
51   C CA  . GLN A 30  ? 0.3318 0.3506 0.3528 -0.0010 -0.0283 -0.0437 567  GLN A CA  
52   C C   . GLN A 30  ? 0.2790 0.2985 0.3006 -0.0019 -0.0263 -0.0422 567  GLN A C   
53   O O   . GLN A 30  ? 0.3259 0.3462 0.3489 -0.0021 -0.0246 -0.0421 567  GLN A O   
54   C CB  . GLN A 30  ? 0.3728 0.3906 0.3978 -0.0012 -0.0295 -0.0440 567  GLN A CB  
55   C CG  . GLN A 30  ? 0.3883 0.4057 0.4163 -0.0018 -0.0303 -0.0434 567  GLN A CG  
56   C CD  . GLN A 30  ? 0.5820 0.5994 0.6143 -0.0030 -0.0301 -0.0439 567  GLN A CD  
57   O OE1 . GLN A 30  ? 0.5370 0.5541 0.5696 -0.0039 -0.0289 -0.0438 567  GLN A OE1 
58   N NE2 . GLN A 30  ? 0.5311 0.5485 0.5662 -0.0033 -0.0316 -0.0448 567  GLN A NE2 
59   N N   . PRO A 31  ? 0.2713 0.2900 0.2914 -0.0023 -0.0268 -0.0410 568  PRO A N   
60   C CA  . PRO A 31  ? 0.2646 0.2839 0.2853 -0.0030 -0.0253 -0.0394 568  PRO A CA  
61   C C   . PRO A 31  ? 0.2930 0.3131 0.3194 -0.0034 -0.0248 -0.0390 568  PRO A C   
62   O O   . PRO A 31  ? 0.2828 0.3025 0.3124 -0.0034 -0.0263 -0.0399 568  PRO A O   
63   C CB  . PRO A 31  ? 0.2893 0.3063 0.3071 -0.0032 -0.0273 -0.0386 568  PRO A CB  
64   C CG  . PRO A 31  ? 0.3511 0.3666 0.3649 -0.0029 -0.0289 -0.0396 568  PRO A CG  
65   C CD  . PRO A 31  ? 0.3060 0.3227 0.3233 -0.0020 -0.0292 -0.0411 568  PRO A CD  
66   N N   . LEU A 32  ? 0.2659 0.2872 0.2935 -0.0039 -0.0227 -0.0379 569  LEU A N   
67   C CA  . LEU A 32  ? 0.2736 0.2959 0.3064 -0.0047 -0.0221 -0.0375 569  LEU A CA  
68   C C   . LEU A 32  ? 0.3577 0.3800 0.3928 -0.0047 -0.0242 -0.0375 569  LEU A C   
69   O O   . LEU A 32  ? 0.3430 0.3639 0.3748 -0.0042 -0.0256 -0.0369 569  LEU A O   
70   C CB  . LEU A 32  ? 0.3284 0.3519 0.3617 -0.0051 -0.0195 -0.0361 569  LEU A CB  
71   C CG  . LEU A 32  ? 0.4970 0.5206 0.5315 -0.0056 -0.0175 -0.0362 569  LEU A CG  
72   C CD1 . LEU A 32  ? 0.4182 0.4402 0.4520 -0.0055 -0.0185 -0.0378 569  LEU A CD1 
73   C CD2 . LEU A 32  ? 0.4100 0.4344 0.4419 -0.0050 -0.0153 -0.0355 569  LEU A CD2 
74   N N   . ARG A 33  ? 0.3022 0.3258 0.3428 -0.0055 -0.0246 -0.0385 570  ARG A N   
75   C CA  . ARG A 33  ? 0.2740 0.2983 0.3180 -0.0054 -0.0268 -0.0394 570  ARG A CA  
76   C C   . ARG A 33  ? 0.3693 0.3957 0.4163 -0.0061 -0.0253 -0.0383 570  ARG A C   
77   O O   . ARG A 33  ? 0.3166 0.3450 0.3673 -0.0075 -0.0232 -0.0386 570  ARG A O   
78   C CB  . ARG A 33  ? 0.3037 0.3290 0.3526 -0.0061 -0.0280 -0.0420 570  ARG A CB  
79   C CG  . ARG A 33  ? 0.3452 0.3715 0.3983 -0.0057 -0.0309 -0.0439 570  ARG A CG  
80   C CD  . ARG A 33  ? 0.3443 0.3723 0.4026 -0.0066 -0.0319 -0.0472 570  ARG A CD  
81   N NE  . ARG A 33  ? 0.4392 0.4682 0.5017 -0.0056 -0.0351 -0.0497 570  ARG A NE  
82   C CZ  . ARG A 33  ? 0.4718 0.5048 0.5414 -0.0068 -0.0352 -0.0525 570  ARG A CZ  
83   N NH1 . ARG A 33  ? 0.3541 0.3903 0.4269 -0.0095 -0.0318 -0.0530 570  ARG A NH1 
84   N NH2 . ARG A 33  ? 0.4781 0.5117 0.5516 -0.0055 -0.0389 -0.0553 570  ARG A NH2 
85   N N   . LEU A 34  ? 0.3186 0.3442 0.3634 -0.0053 -0.0266 -0.0371 571  LEU A N   
86   C CA  . LEU A 34  ? 0.2995 0.3268 0.3462 -0.0056 -0.0253 -0.0357 571  LEU A CA  
87   C C   . LEU A 34  ? 0.2955 0.3241 0.3471 -0.0053 -0.0282 -0.0373 571  LEU A C   
88   O O   . LEU A 34  ? 0.3425 0.3694 0.3943 -0.0045 -0.0318 -0.0391 571  LEU A O   
89   C CB  . LEU A 34  ? 0.2963 0.3215 0.3363 -0.0051 -0.0247 -0.0333 571  LEU A CB  
90   C CG  . LEU A 34  ? 0.3386 0.3631 0.3738 -0.0052 -0.0221 -0.0326 571  LEU A CG  
91   C CD1 . LEU A 34  ? 0.5366 0.5596 0.5652 -0.0053 -0.0214 -0.0309 571  LEU A CD1 
92   C CD2 . LEU A 34  ? 0.3560 0.3827 0.3947 -0.0059 -0.0189 -0.0325 571  LEU A CD2 
93   N N   . PRO A 35  ? 0.2619 0.2934 0.3178 -0.0059 -0.0270 -0.0368 572  PRO A N   
94   C CA  . PRO A 35  ? 0.2950 0.3280 0.3557 -0.0053 -0.0302 -0.0385 572  PRO A CA  
95   C C   . PRO A 35  ? 0.3410 0.3696 0.3958 -0.0038 -0.0339 -0.0373 572  PRO A C   
96   O O   . PRO A 35  ? 0.3220 0.3474 0.3692 -0.0038 -0.0328 -0.0347 572  PRO A O   
97   C CB  . PRO A 35  ? 0.3159 0.3526 0.3809 -0.0063 -0.0276 -0.0376 572  PRO A CB  
98   C CG  . PRO A 35  ? 0.2901 0.3255 0.3498 -0.0066 -0.0237 -0.0342 572  PRO A CG  
99   C CD  . PRO A 35  ? 0.2455 0.2787 0.3016 -0.0068 -0.0229 -0.0348 572  PRO A CD  
100  N N   . SER A 36  ? 0.3406 0.3688 0.3983 -0.0028 -0.0385 -0.0394 573  SER A N   
101  C CA  . SER A 36  ? 0.3025 0.3251 0.3535 -0.0017 -0.0428 -0.0383 573  SER A CA  
102  C C   . SER A 36  ? 0.3298 0.3519 0.3775 -0.0019 -0.0417 -0.0352 573  SER A C   
103  O O   . SER A 36  ? 0.3551 0.3819 0.4084 -0.0024 -0.0391 -0.0348 573  SER A O   
104  C CB  . SER A 36  ? 0.3527 0.3743 0.4080 -0.0002 -0.0489 -0.0419 573  SER A CB  
105  O OG  . SER A 36  ? 0.4577 0.4828 0.5191 0.0001  -0.0500 -0.0430 573  SER A OG  
106  N N   . PRO A 37  ? 0.3399 0.3561 0.3781 -0.0020 -0.0436 -0.0330 574  PRO A N   
107  C CA  . PRO A 37  ? 0.4144 0.4296 0.4484 -0.0025 -0.0427 -0.0300 574  PRO A CA  
108  C C   . PRO A 37  ? 0.4909 0.5072 0.5302 -0.0015 -0.0466 -0.0311 574  PRO A C   
109  O O   . PRO A 37  ? 0.3924 0.4098 0.4310 -0.0017 -0.0452 -0.0289 574  PRO A O   
110  C CB  . PRO A 37  ? 0.4198 0.4277 0.4418 -0.0034 -0.0448 -0.0282 574  PRO A CB  
111  C CG  . PRO A 37  ? 0.4481 0.4524 0.4692 -0.0027 -0.0488 -0.0307 574  PRO A CG  
112  C CD  . PRO A 37  ? 0.3665 0.3768 0.3967 -0.0021 -0.0459 -0.0329 574  PRO A CD  
113  N N   . GLU A 38  ? 0.4212 0.4375 0.4659 -0.0001 -0.0515 -0.0347 575  GLU A N   
114  C CA  . GLU A 38  ? 0.4525 0.4705 0.5034 0.0011  -0.0557 -0.0368 575  GLU A CA  
115  C C   . GLU A 38  ? 0.4582 0.4849 0.5195 0.0007  -0.0516 -0.0377 575  GLU A C   
116  O O   . GLU A 38  ? 0.4910 0.5201 0.5569 0.0013  -0.0535 -0.0383 575  GLU A O   
117  C CB  . GLU A 38  ? 0.4623 0.4784 0.5170 0.0028  -0.0623 -0.0414 575  GLU A CB  
118  C CG  . GLU A 38  ? 0.4522 0.4582 0.4964 0.0034  -0.0686 -0.0408 575  GLU A CG  
119  C CD  . GLU A 38  ? 0.5971 0.5987 0.6331 0.0023  -0.0666 -0.0391 575  GLU A CD  
120  O OE1 . GLU A 38  ? 0.4897 0.4958 0.5301 0.0020  -0.0625 -0.0402 575  GLU A OE1 
121  O OE2 . GLU A 38  ? 0.5963 0.5899 0.6210 0.0016  -0.0692 -0.0368 575  GLU A OE2 
122  N N   . VAL A 39  ? 0.3278 0.3587 0.3926 -0.0006 -0.0462 -0.0379 576  VAL A N   
123  C CA  . VAL A 39  ? 0.3710 0.4092 0.4442 -0.0016 -0.0419 -0.0385 576  VAL A CA  
124  C C   . VAL A 39  ? 0.3764 0.4151 0.4457 -0.0029 -0.0359 -0.0343 576  VAL A C   
125  O O   . VAL A 39  ? 0.3760 0.4195 0.4508 -0.0038 -0.0324 -0.0340 576  VAL A O   
126  C CB  . VAL A 39  ? 0.3735 0.4163 0.4544 -0.0027 -0.0404 -0.0424 576  VAL A CB  
127  C CG1 . VAL A 39  ? 0.3858 0.4297 0.4728 -0.0015 -0.0462 -0.0476 576  VAL A CG1 
128  C CG2 . VAL A 39  ? 0.4299 0.4702 0.5057 -0.0035 -0.0377 -0.0414 576  VAL A CG2 
129  N N   . TYR A 40  ? 0.3142 0.3480 0.3742 -0.0029 -0.0347 -0.0314 577  TYR A N   
130  C CA  . TYR A 40  ? 0.3384 0.3728 0.3949 -0.0038 -0.0292 -0.0282 577  TYR A CA  
131  C C   . TYR A 40  ? 0.3192 0.3482 0.3649 -0.0038 -0.0296 -0.0255 577  TYR A C   
132  O O   . TYR A 40  ? 0.3150 0.3409 0.3553 -0.0041 -0.0297 -0.0258 577  TYR A O   
133  C CB  . TYR A 40  ? 0.2584 0.2948 0.3171 -0.0049 -0.0254 -0.0291 577  TYR A CB  
134  C CG  . TYR A 40  ? 0.2637 0.3007 0.3200 -0.0056 -0.0203 -0.0267 577  TYR A CG  
135  C CD1 . TYR A 40  ? 0.2641 0.3044 0.3247 -0.0060 -0.0175 -0.0255 577  TYR A CD1 
136  C CD2 . TYR A 40  ? 0.2725 0.3070 0.3228 -0.0057 -0.0185 -0.0260 577  TYR A CD2 
137  C CE1 . TYR A 40  ? 0.2708 0.3112 0.3293 -0.0064 -0.0133 -0.0236 577  TYR A CE1 
138  C CE2 . TYR A 40  ? 0.3256 0.3606 0.3742 -0.0061 -0.0143 -0.0244 577  TYR A CE2 
139  C CZ  . TYR A 40  ? 0.2715 0.3091 0.3241 -0.0064 -0.0118 -0.0232 577  TYR A CZ  
140  O OH  . TYR A 40  ? 0.2542 0.2919 0.3052 -0.0065 -0.0081 -0.0221 577  TYR A OH  
141  N N   . ARG A 41  ? 0.2890 0.3170 0.3315 -0.0038 -0.0297 -0.0231 578  ARG A N   
142  C CA  . ARG A 41  ? 0.3376 0.3600 0.3693 -0.0043 -0.0309 -0.0210 578  ARG A CA  
143  C C   . ARG A 41  ? 0.3047 0.3259 0.3298 -0.0055 -0.0269 -0.0201 578  ARG A C   
144  O O   . ARG A 41  ? 0.3635 0.3799 0.3797 -0.0065 -0.0283 -0.0196 578  ARG A O   
145  C CB  . ARG A 41  ? 0.3992 0.4218 0.4293 -0.0044 -0.0305 -0.0185 578  ARG A CB  
146  C CG  . ARG A 41  ? 0.5820 0.6044 0.6158 -0.0033 -0.0354 -0.0191 578  ARG A CG  
147  C CD  . ARG A 41  ? 0.4223 0.4422 0.4499 -0.0038 -0.0356 -0.0161 578  ARG A CD  
148  N NE  . ARG A 41  ? 0.3561 0.3813 0.3884 -0.0037 -0.0306 -0.0143 578  ARG A NE  
149  C CZ  . ARG A 41  ? 0.3833 0.4074 0.4112 -0.0041 -0.0298 -0.0116 578  ARG A CZ  
150  N NH1 . ARG A 41  ? 0.3942 0.4231 0.4267 -0.0038 -0.0253 -0.0101 578  ARG A NH1 
151  N NH2 . ARG A 41  ? 0.3752 0.3929 0.3934 -0.0050 -0.0338 -0.0104 578  ARG A NH2 
152  N N   . PHE A 42  ? 0.2972 0.3226 0.3266 -0.0055 -0.0222 -0.0201 579  PHE A N   
153  C CA  . PHE A 42  ? 0.3188 0.3438 0.3427 -0.0064 -0.0183 -0.0197 579  PHE A CA  
154  C C   . PHE A 42  ? 0.4357 0.4583 0.4559 -0.0067 -0.0194 -0.0214 579  PHE A C   
155  O O   . PHE A 42  ? 0.4333 0.4551 0.4478 -0.0076 -0.0172 -0.0215 579  PHE A O   
156  C CB  . PHE A 42  ? 0.3133 0.3425 0.3428 -0.0061 -0.0137 -0.0195 579  PHE A CB  
157  C CG  . PHE A 42  ? 0.3067 0.3383 0.3397 -0.0057 -0.0123 -0.0177 579  PHE A CG  
158  C CD1 . PHE A 42  ? 0.3259 0.3573 0.3543 -0.0061 -0.0098 -0.0159 579  PHE A CD1 
159  C CD2 . PHE A 42  ? 0.2891 0.3235 0.3302 -0.0052 -0.0135 -0.0181 579  PHE A CD2 
160  C CE1 . PHE A 42  ? 0.3048 0.3385 0.3366 -0.0056 -0.0085 -0.0141 579  PHE A CE1 
161  C CE2 . PHE A 42  ? 0.3223 0.3592 0.3670 -0.0049 -0.0122 -0.0165 579  PHE A CE2 
162  C CZ  . PHE A 42  ? 0.3425 0.3789 0.3825 -0.0050 -0.0098 -0.0143 579  PHE A CZ  
163  N N   . VAL A 43  ? 0.3345 0.3564 0.3582 -0.0061 -0.0228 -0.0231 580  VAL A N   
164  C CA  . VAL A 43  ? 0.3441 0.3638 0.3646 -0.0063 -0.0238 -0.0246 580  VAL A CA  
165  C C   . VAL A 43  ? 0.3641 0.3782 0.3769 -0.0068 -0.0280 -0.0245 580  VAL A C   
166  O O   . VAL A 43  ? 0.3356 0.3474 0.3456 -0.0069 -0.0295 -0.0258 580  VAL A O   
167  C CB  . VAL A 43  ? 0.3360 0.3578 0.3639 -0.0054 -0.0247 -0.0268 580  VAL A CB  
168  C CG1 . VAL A 43  ? 0.3317 0.3576 0.3652 -0.0055 -0.0206 -0.0270 580  VAL A CG1 
169  C CG2 . VAL A 43  ? 0.3573 0.3791 0.3902 -0.0047 -0.0288 -0.0279 580  VAL A CG2 
170  N N   . VAL A 44  ? 0.3285 0.3398 0.3372 -0.0073 -0.0301 -0.0230 581  VAL A N   
171  C CA  . VAL A 44  ? 0.3482 0.3526 0.3470 -0.0086 -0.0339 -0.0225 581  VAL A CA  
172  C C   . VAL A 44  ? 0.3405 0.3438 0.3317 -0.0105 -0.0310 -0.0226 581  VAL A C   
173  O O   . VAL A 44  ? 0.3656 0.3726 0.3566 -0.0112 -0.0261 -0.0223 581  VAL A O   
174  C CB  . VAL A 44  ? 0.4096 0.4108 0.4033 -0.0095 -0.0359 -0.0204 581  VAL A CB  
175  C CG1 . VAL A 44  ? 0.4526 0.4457 0.4336 -0.0118 -0.0392 -0.0197 581  VAL A CG1 
176  C CG2 . VAL A 44  ? 0.5255 0.5271 0.5264 -0.0075 -0.0402 -0.0210 581  VAL A CG2 
177  N N   . LYS A 45  ? 0.3310 0.3295 0.3163 -0.0113 -0.0340 -0.0235 582  LYS A N   
178  C CA  . LYS A 45  ? 0.3429 0.3409 0.3217 -0.0132 -0.0314 -0.0243 582  LYS A CA  
179  C C   . LYS A 45  ? 0.3717 0.3689 0.3418 -0.0161 -0.0283 -0.0232 582  LYS A C   
180  O O   . LYS A 45  ? 0.3640 0.3562 0.3270 -0.0178 -0.0308 -0.0216 582  LYS A O   
181  C CB  . LYS A 45  ? 0.3707 0.3626 0.3438 -0.0137 -0.0358 -0.0252 582  LYS A CB  
182  C CG  . LYS A 45  ? 0.3855 0.3767 0.3516 -0.0160 -0.0336 -0.0262 582  LYS A CG  
183  C CD  . LYS A 45  ? 0.5282 0.5258 0.5016 -0.0143 -0.0301 -0.0281 582  LYS A CD  
184  C CE  . LYS A 45  ? 0.5429 0.5402 0.5101 -0.0163 -0.0286 -0.0296 582  LYS A CE  
185  N NZ  . LYS A 45  ? 0.4008 0.4036 0.3751 -0.0144 -0.0262 -0.0316 582  LYS A NZ  
186  N N   . ASP A 46  ? 0.3157 0.3179 0.2866 -0.0167 -0.0233 -0.0243 583  ASP A N   
187  C CA  . ASP A 46  ? 0.3524 0.3547 0.3151 -0.0199 -0.0199 -0.0243 583  ASP A CA  
188  C C   . ASP A 46  ? 0.3723 0.3676 0.3227 -0.0234 -0.0226 -0.0243 583  ASP A C   
189  O O   . ASP A 46  ? 0.3741 0.3670 0.3227 -0.0236 -0.0247 -0.0255 583  ASP A O   
190  C CB  . ASP A 46  ? 0.3454 0.3537 0.3104 -0.0200 -0.0150 -0.0269 583  ASP A CB  
191  C CG  . ASP A 46  ? 0.4233 0.4377 0.3978 -0.0174 -0.0117 -0.0270 583  ASP A CG  
192  O OD1 . ASP A 46  ? 0.3997 0.4142 0.3792 -0.0158 -0.0127 -0.0249 583  ASP A OD1 
193  O OD2 . ASP A 46  ? 0.4383 0.4570 0.4150 -0.0171 -0.0084 -0.0294 583  ASP A OD2 
194  N N   . SER A 47  ? 0.3655 0.3575 0.3071 -0.0266 -0.0222 -0.0230 584  SER A N   
195  C CA  . SER A 47  ? 0.3804 0.3656 0.3084 -0.0311 -0.0240 -0.0232 584  SER A CA  
196  C C   . SER A 47  ? 0.4304 0.4158 0.3506 -0.0350 -0.0205 -0.0227 584  SER A C   
197  O O   . SER A 47  ? 0.4196 0.4099 0.3453 -0.0335 -0.0175 -0.0220 584  SER A O   
198  C CB  . SER A 47  ? 0.3793 0.3551 0.3021 -0.0312 -0.0311 -0.0213 584  SER A CB  
199  O OG  . SER A 47  ? 0.4325 0.4053 0.3531 -0.0314 -0.0330 -0.0189 584  SER A OG  
200  N N   . GLU A 48  ? 0.4295 0.4093 0.3363 -0.0401 -0.0209 -0.0232 585  GLU A N   
201  C CA  . GLU A 48  ? 0.4193 0.3981 0.3168 -0.0447 -0.0181 -0.0229 585  GLU A CA  
202  C C   . GLU A 48  ? 0.4720 0.4453 0.3668 -0.0443 -0.0217 -0.0193 585  GLU A C   
203  O O   . GLU A 48  ? 0.5180 0.4910 0.4066 -0.0473 -0.0194 -0.0185 585  GLU A O   
204  C CB  . GLU A 48  ? 0.5415 0.5146 0.4241 -0.0511 -0.0181 -0.0244 585  GLU A CB  
205  C CG  . GLU A 48  ? 0.7573 0.7377 0.6414 -0.0527 -0.0129 -0.0287 585  GLU A CG  
206  C CD  . GLU A 48  ? 1.0404 1.0157 0.9092 -0.0600 -0.0123 -0.0305 585  GLU A CD  
207  O OE1 . GLU A 48  ? 1.1068 1.0716 0.9629 -0.0639 -0.0164 -0.0280 585  GLU A OE1 
208  O OE2 . GLU A 48  ? 1.0618 1.0432 0.9308 -0.0621 -0.0081 -0.0346 585  GLU A OE2 
209  N N   . GLU A 49  ? 0.4364 0.4057 0.3361 -0.0406 -0.0275 -0.0175 586  GLU A N   
210  C CA  . GLU A 49  ? 0.4354 0.4003 0.3344 -0.0395 -0.0316 -0.0146 586  GLU A CA  
211  C C   . GLU A 49  ? 0.4316 0.4049 0.3444 -0.0350 -0.0288 -0.0138 586  GLU A C   
212  O O   . GLU A 49  ? 0.4422 0.4133 0.3557 -0.0338 -0.0316 -0.0116 586  GLU A O   
213  C CB  . GLU A 49  ? 0.4851 0.4415 0.3829 -0.0377 -0.0398 -0.0137 586  GLU A CB  
214  C CG  . GLU A 49  ? 0.5981 0.5451 0.4828 -0.0417 -0.0435 -0.0143 586  GLU A CG  
215  C CD  . GLU A 49  ? 0.6795 0.6208 0.5478 -0.0485 -0.0419 -0.0137 586  GLU A CD  
216  O OE1 . GLU A 49  ? 0.6555 0.5944 0.5193 -0.0499 -0.0424 -0.0117 586  GLU A OE1 
217  O OE2 . GLU A 49  ? 0.6836 0.6229 0.5434 -0.0527 -0.0401 -0.0154 586  GLU A OE2 
218  N N   . ASN A 50  ? 0.3817 0.3640 0.3049 -0.0324 -0.0239 -0.0157 587  ASN A N   
219  C CA  . ASN A 50  ? 0.3765 0.3659 0.3115 -0.0287 -0.0213 -0.0149 587  ASN A CA  
220  C C   . ASN A 50  ? 0.3890 0.3870 0.3294 -0.0283 -0.0143 -0.0168 587  ASN A C   
221  O O   . ASN A 50  ? 0.3465 0.3494 0.2945 -0.0260 -0.0117 -0.0160 587  ASN A O   
222  C CB  . ASN A 50  ? 0.3691 0.3598 0.3155 -0.0241 -0.0248 -0.0148 587  ASN A CB  
223  C CG  . ASN A 50  ? 0.3699 0.3623 0.3203 -0.0229 -0.0248 -0.0171 587  ASN A CG  
224  O OD1 . ASN A 50  ? 0.3423 0.3387 0.2928 -0.0238 -0.0204 -0.0190 587  ASN A OD1 
225  N ND2 . ASN A 50  ? 0.3731 0.3625 0.3272 -0.0208 -0.0299 -0.0173 587  ASN A ND2 
226  N N   . ILE A 51  ? 0.3759 0.3755 0.3125 -0.0305 -0.0114 -0.0196 588  ILE A N   
227  C CA  . ILE A 51  ? 0.3849 0.3922 0.3259 -0.0302 -0.0053 -0.0221 588  ILE A CA  
228  C C   . ILE A 51  ? 0.4368 0.4446 0.3693 -0.0344 -0.0025 -0.0254 588  ILE A C   
229  O O   . ILE A 51  ? 0.4059 0.4107 0.3344 -0.0358 -0.0047 -0.0265 588  ILE A O   
230  C CB  . ILE A 51  ? 0.4198 0.4328 0.3738 -0.0256 -0.0043 -0.0233 588  ILE A CB  
231  C CG1 . ILE A 51  ? 0.4294 0.4495 0.3880 -0.0250 0.0012  -0.0259 588  ILE A CG1 
232  C CG2 . ILE A 51  ? 0.3881 0.3994 0.3428 -0.0250 -0.0070 -0.0248 588  ILE A CG2 
233  C CD1 . ILE A 51  ? 0.4754 0.4998 0.4459 -0.0207 0.0019  -0.0265 588  ILE A CD1 
234  N N   . VAL A 52  ? 0.3881 0.3999 0.3179 -0.0367 0.0023  -0.0272 589  VAL A N   
235  C CA  . VAL A 52  ? 0.3708 0.3844 0.2929 -0.0412 0.0055  -0.0312 589  VAL A CA  
236  C C   . VAL A 52  ? 0.4117 0.4343 0.3407 -0.0400 0.0110  -0.0353 589  VAL A C   
237  O O   . VAL A 52  ? 0.3696 0.3957 0.3052 -0.0373 0.0131  -0.0344 589  VAL A O   
238  C CB  . VAL A 52  ? 0.4851 0.4929 0.3925 -0.0474 0.0055  -0.0302 589  VAL A CB  
239  C CG1 . VAL A 52  ? 0.5153 0.5129 0.4147 -0.0488 -0.0008 -0.0267 589  VAL A CG1 
240  C CG2 . VAL A 52  ? 0.4759 0.4853 0.3835 -0.0474 0.0079  -0.0285 589  VAL A CG2 
241  N N   . PHE A 53  ? 0.3819 0.4082 0.3098 -0.0418 0.0131  -0.0400 590  PHE A N   
242  C CA  . PHE A 53  ? 0.3355 0.3704 0.2704 -0.0403 0.0176  -0.0451 590  PHE A CA  
243  C C   . PHE A 53  ? 0.4680 0.5061 0.3946 -0.0460 0.0218  -0.0499 590  PHE A C   
244  O O   . PHE A 53  ? 0.4727 0.5063 0.3879 -0.0513 0.0210  -0.0498 590  PHE A O   
245  C CB  . PHE A 53  ? 0.3951 0.4329 0.3382 -0.0368 0.0162  -0.0476 590  PHE A CB  
246  C CG  . PHE A 53  ? 0.4003 0.4354 0.3514 -0.0318 0.0125  -0.0435 590  PHE A CG  
247  C CD1 . PHE A 53  ? 0.4046 0.4429 0.3656 -0.0274 0.0134  -0.0430 590  PHE A CD1 
248  C CD2 . PHE A 53  ? 0.4342 0.4633 0.3827 -0.0318 0.0080  -0.0405 590  PHE A CD2 
249  C CE1 . PHE A 53  ? 0.4708 0.5068 0.4388 -0.0236 0.0102  -0.0397 590  PHE A CE1 
250  C CE2 . PHE A 53  ? 0.4475 0.4748 0.4036 -0.0275 0.0049  -0.0374 590  PHE A CE2 
251  C CZ  . PHE A 53  ? 0.4197 0.4507 0.3854 -0.0237 0.0061  -0.0371 590  PHE A CZ  
252  N N   . GLU A 54  ? 0.4111 0.4568 0.3431 -0.0451 0.0261  -0.0544 591  GLU A N   
253  C CA  . GLU A 54  ? 0.4260 0.4767 0.3521 -0.0502 0.0305  -0.0606 591  GLU A CA  
254  C C   . GLU A 54  ? 0.6565 0.7109 0.5839 -0.0510 0.0305  -0.0660 591  GLU A C   
255  O O   . GLU A 54  ? 0.6481 0.7014 0.5817 -0.0470 0.0271  -0.0648 591  GLU A O   
256  C CB  . GLU A 54  ? 0.3855 0.4435 0.3181 -0.0485 0.0349  -0.0644 591  GLU A CB  
257  C CG  . GLU A 54  ? 0.4286 0.4842 0.3599 -0.0481 0.0359  -0.0599 591  GLU A CG  
258  C CD  . GLU A 54  ? 0.5915 0.6441 0.5092 -0.0552 0.0379  -0.0594 591  GLU A CD  
259  O OE1 . GLU A 54  ? 0.6202 0.6715 0.5362 -0.0554 0.0391  -0.0565 591  GLU A OE1 
260  O OE2 . GLU A 54  ? 0.6457 0.6969 0.5538 -0.0608 0.0382  -0.0619 591  GLU A OE2 
261  N N   . ASP A 55  ? 0.9059 0.9651 0.8275 -0.0563 0.0342  -0.0722 592  ASP A N   
262  C CA  . ASP A 55  ? 0.9897 1.0544 0.9138 -0.0570 0.0348  -0.0786 592  ASP A CA  
263  C C   . ASP A 55  ? 1.0671 1.1422 0.9967 -0.0573 0.0394  -0.0872 592  ASP A C   
264  O O   . ASP A 55  ? 1.1333 1.2124 1.0561 -0.0635 0.0429  -0.0927 592  ASP A O   
265  C CB  . ASP A 55  ? 0.9854 1.0460 0.8968 -0.0639 0.0343  -0.0790 592  ASP A CB  
266  C CG  . ASP A 55  ? 1.1447 1.1949 1.0513 -0.0632 0.0291  -0.0714 592  ASP A CG  
267  O OD1 . ASP A 55  ? 1.2131 1.2571 1.1178 -0.0619 0.0272  -0.0653 592  ASP A OD1 
268  O OD2 . ASP A 55  ? 1.2258 1.2743 1.1314 -0.0635 0.0267  -0.0721 592  ASP A OD2 
269  N N   . GLY A 62  ? 0.7096 0.7849 0.7236 -0.0055 0.0153  -0.0909 599  GLY A N   
270  C CA  . GLY A 62  ? 0.7509 0.8247 0.7599 -0.0082 0.0144  -0.0881 599  GLY A CA  
271  C C   . GLY A 62  ? 0.7210 0.7892 0.7258 -0.0097 0.0146  -0.0795 599  GLY A C   
272  O O   . GLY A 62  ? 0.6780 0.7439 0.6783 -0.0117 0.0135  -0.0764 599  GLY A O   
273  N N   . ILE A 63  ? 0.6979 0.7640 0.7043 -0.0085 0.0158  -0.0758 600  ILE A N   
274  C CA  . ILE A 63  ? 0.6144 0.6755 0.6177 -0.0095 0.0157  -0.0681 600  ILE A CA  
275  C C   . ILE A 63  ? 0.4686 0.5306 0.4640 -0.0141 0.0186  -0.0669 600  ILE A C   
276  O O   . ILE A 63  ? 0.5750 0.6410 0.5684 -0.0159 0.0220  -0.0704 600  ILE A O   
277  C CB  . ILE A 63  ? 0.5985 0.6575 0.6063 -0.0069 0.0162  -0.0650 600  ILE A CB  
278  C CG1 . ILE A 63  ? 0.6933 0.7491 0.7072 -0.0032 0.0127  -0.0647 600  ILE A CG1 
279  C CG2 . ILE A 63  ? 0.6026 0.6581 0.6073 -0.0084 0.0167  -0.0581 600  ILE A CG2 
280  C CD1 . ILE A 63  ? 0.7386 0.7925 0.7568 -0.0008 0.0132  -0.0627 600  ILE A CD1 
281  N N   . PRO A 64  ? 0.4943 0.5521 0.4846 -0.0160 0.0169  -0.0622 601  PRO A N   
282  C CA  . PRO A 64  ? 0.5158 0.5727 0.4972 -0.0207 0.0188  -0.0606 601  PRO A CA  
283  C C   . PRO A 64  ? 0.5048 0.5616 0.4853 -0.0211 0.0214  -0.0582 601  PRO A C   
284  O O   . PRO A 64  ? 0.5062 0.5615 0.4924 -0.0179 0.0207  -0.0551 601  PRO A O   
285  C CB  . PRO A 64  ? 0.5631 0.6140 0.5410 -0.0213 0.0154  -0.0554 601  PRO A CB  
286  C CG  . PRO A 64  ? 0.6036 0.6526 0.5895 -0.0169 0.0125  -0.0532 601  PRO A CG  
287  C CD  . PRO A 64  ? 0.5658 0.6191 0.5582 -0.0142 0.0131  -0.0583 601  PRO A CD  
288  N N   . ILE A 65  ? 0.4200 0.4784 0.3931 -0.0254 0.0245  -0.0598 602  ILE A N   
289  C CA  . ILE A 65  ? 0.3959 0.4546 0.3674 -0.0262 0.0272  -0.0580 602  ILE A CA  
290  C C   . ILE A 65  ? 0.3574 0.4099 0.3213 -0.0289 0.0255  -0.0518 602  ILE A C   
291  O O   . ILE A 65  ? 0.3832 0.4331 0.3379 -0.0333 0.0250  -0.0518 602  ILE A O   
292  C CB  . ILE A 65  ? 0.4760 0.5406 0.4441 -0.0295 0.0317  -0.0642 602  ILE A CB  
293  C CG1 . ILE A 65  ? 0.5094 0.5801 0.4861 -0.0263 0.0326  -0.0710 602  ILE A CG1 
294  C CG2 . ILE A 65  ? 0.3986 0.4631 0.3643 -0.0306 0.0346  -0.0620 602  ILE A CG2 
295  C CD1 . ILE A 65  ? 0.6344 0.7120 0.6085 -0.0297 0.0367  -0.0788 602  ILE A CD1 
296  N N   . ILE A 66  ? 0.3759 0.4255 0.3433 -0.0263 0.0243  -0.0467 603  ILE A N   
297  C CA  . ILE A 66  ? 0.3286 0.3722 0.2900 -0.0280 0.0217  -0.0410 603  ILE A CA  
298  C C   . ILE A 66  ? 0.3639 0.4066 0.3160 -0.0325 0.0242  -0.0406 603  ILE A C   
299  O O   . ILE A 66  ? 0.4175 0.4638 0.3718 -0.0320 0.0276  -0.0417 603  ILE A O   
300  C CB  . ILE A 66  ? 0.3301 0.3717 0.2990 -0.0239 0.0196  -0.0363 603  ILE A CB  
301  C CG1 . ILE A 66  ? 0.4522 0.4934 0.4284 -0.0206 0.0167  -0.0364 603  ILE A CG1 
302  C CG2 . ILE A 66  ? 0.4587 0.4946 0.4219 -0.0255 0.0168  -0.0312 603  ILE A CG2 
303  C CD1 . ILE A 66  ? 0.4500 0.4912 0.4351 -0.0166 0.0158  -0.0336 603  ILE A CD1 
304  N N   . LYS A 67  ? 0.3399 0.3774 0.2813 -0.0368 0.0223  -0.0391 604  LYS A N   
305  C CA  . LYS A 67  ? 0.3726 0.4076 0.3031 -0.0419 0.0239  -0.0383 604  LYS A CA  
306  C C   . LYS A 67  ? 0.3434 0.3726 0.2724 -0.0409 0.0207  -0.0320 604  LYS A C   
307  O O   . LYS A 67  ? 0.3758 0.4049 0.3016 -0.0422 0.0226  -0.0306 604  LYS A O   
308  C CB  . LYS A 67  ? 0.3684 0.3998 0.2867 -0.0479 0.0232  -0.0401 604  LYS A CB  
309  C CG  . LYS A 67  ? 0.4145 0.4423 0.3194 -0.0542 0.0248  -0.0396 604  LYS A CG  
310  C CD  . LYS A 67  ? 0.4704 0.4938 0.3625 -0.0607 0.0240  -0.0415 604  LYS A CD  
311  C CE  . LYS A 67  ? 0.6251 0.6441 0.5025 -0.0678 0.0254  -0.0410 604  LYS A CE  
312  N NZ  . LYS A 67  ? 0.7499 0.7643 0.6139 -0.0748 0.0249  -0.0433 604  LYS A NZ  
313  N N   . GLY A 68  ? 0.3361 0.3606 0.2676 -0.0384 0.0157  -0.0286 605  GLY A N   
314  C CA  . GLY A 68  ? 0.3231 0.3427 0.2543 -0.0371 0.0120  -0.0234 605  GLY A CA  
315  C C   . GLY A 68  ? 0.3253 0.3414 0.2618 -0.0338 0.0068  -0.0212 605  GLY A C   
316  O O   . GLY A 68  ? 0.3430 0.3600 0.2822 -0.0329 0.0061  -0.0233 605  GLY A O   
317  N N   . GLY A 69  ? 0.3840 0.3967 0.3224 -0.0319 0.0032  -0.0172 606  GLY A N   
318  C CA  . GLY A 69  ? 0.3508 0.3604 0.2942 -0.0291 -0.0020 -0.0156 606  GLY A CA  
319  C C   . GLY A 69  ? 0.3577 0.3650 0.3041 -0.0271 -0.0054 -0.0120 606  GLY A C   
320  O O   . GLY A 69  ? 0.3530 0.3611 0.2979 -0.0277 -0.0036 -0.0104 606  GLY A O   
321  N N   . THR A 70  ? 0.3076 0.3122 0.2586 -0.0247 -0.0104 -0.0110 607  THR A N   
322  C CA  . THR A 70  ? 0.2888 0.2933 0.2460 -0.0220 -0.0134 -0.0085 607  THR A CA  
323  C C   . THR A 70  ? 0.2976 0.3100 0.2667 -0.0189 -0.0089 -0.0087 607  THR A C   
324  O O   . THR A 70  ? 0.3133 0.3300 0.2866 -0.0181 -0.0051 -0.0109 607  THR A O   
325  C CB  . THR A 70  ? 0.3599 0.3610 0.3208 -0.0200 -0.0196 -0.0085 607  THR A CB  
326  O OG1 . THR A 70  ? 0.3701 0.3754 0.3392 -0.0180 -0.0181 -0.0107 607  THR A OG1 
327  C CG2 . THR A 70  ? 0.3592 0.3512 0.3077 -0.0230 -0.0247 -0.0084 607  THR A CG2 
328  N N   . VAL A 71  ? 0.3037 0.3175 0.2777 -0.0171 -0.0095 -0.0065 608  VAL A N   
329  C CA  . VAL A 71  ? 0.3129 0.3334 0.2977 -0.0144 -0.0054 -0.0066 608  VAL A CA  
330  C C   . VAL A 71  ? 0.3415 0.3645 0.3354 -0.0121 -0.0061 -0.0083 608  VAL A C   
331  O O   . VAL A 71  ? 0.3093 0.3368 0.3095 -0.0108 -0.0023 -0.0094 608  VAL A O   
332  C CB  . VAL A 71  ? 0.3419 0.3637 0.3309 -0.0129 -0.0062 -0.0039 608  VAL A CB  
333  C CG1 . VAL A 71  ? 0.3686 0.3890 0.3631 -0.0111 -0.0119 -0.0034 608  VAL A CG1 
334  C CG2 . VAL A 71  ? 0.3751 0.4031 0.3728 -0.0109 -0.0011 -0.0040 608  VAL A CG2 
335  N N   . VAL A 72  ? 0.3034 0.3232 0.2976 -0.0118 -0.0111 -0.0087 609  VAL A N   
336  C CA  . VAL A 72  ? 0.3001 0.3222 0.3024 -0.0100 -0.0118 -0.0105 609  VAL A CA  
337  C C   . VAL A 72  ? 0.3112 0.3344 0.3118 -0.0107 -0.0087 -0.0128 609  VAL A C   
338  O O   . VAL A 72  ? 0.3113 0.3381 0.3188 -0.0093 -0.0063 -0.0140 609  VAL A O   
339  C CB  . VAL A 72  ? 0.4137 0.4321 0.4161 -0.0096 -0.0179 -0.0111 609  VAL A CB  
340  C CG1 . VAL A 72  ? 0.3521 0.3723 0.3604 -0.0086 -0.0181 -0.0135 609  VAL A CG1 
341  C CG2 . VAL A 72  ? 0.3603 0.3797 0.3686 -0.0081 -0.0210 -0.0100 609  VAL A CG2 
342  N N   . LYS A 73  ? 0.2714 0.2913 0.2623 -0.0130 -0.0089 -0.0134 610  LYS A N   
343  C CA  . LYS A 73  ? 0.2912 0.3124 0.2803 -0.0138 -0.0063 -0.0160 610  LYS A CA  
344  C C   . LYS A 73  ? 0.2946 0.3205 0.2859 -0.0135 -0.0008 -0.0170 610  LYS A C   
345  O O   . LYS A 73  ? 0.2815 0.3101 0.2763 -0.0125 0.0012  -0.0194 610  LYS A O   
346  C CB  . LYS A 73  ? 0.2922 0.3087 0.2701 -0.0168 -0.0078 -0.0167 610  LYS A CB  
347  C CG  . LYS A 73  ? 0.3513 0.3632 0.3278 -0.0167 -0.0131 -0.0169 610  LYS A CG  
348  C CD  . LYS A 73  ? 0.3694 0.3842 0.3525 -0.0149 -0.0125 -0.0191 610  LYS A CD  
349  C CE  . LYS A 73  ? 0.3560 0.3672 0.3402 -0.0140 -0.0176 -0.0194 610  LYS A CE  
350  N NZ  . LYS A 73  ? 0.3515 0.3658 0.3428 -0.0122 -0.0168 -0.0214 610  LYS A NZ  
351  N N   . LEU A 74  ? 0.2954 0.3219 0.2844 -0.0141 0.0012  -0.0155 611  LEU A N   
352  C CA  . LEU A 74  ? 0.2955 0.3265 0.2874 -0.0135 0.0061  -0.0167 611  LEU A CA  
353  C C   . LEU A 74  ? 0.2821 0.3160 0.2846 -0.0104 0.0069  -0.0167 611  LEU A C   
354  O O   . LEU A 74  ? 0.2946 0.3311 0.3003 -0.0094 0.0095  -0.0190 611  LEU A O   
355  C CB  . LEU A 74  ? 0.3036 0.3347 0.2916 -0.0146 0.0080  -0.0148 611  LEU A CB  
356  C CG  . LEU A 74  ? 0.3286 0.3566 0.3046 -0.0185 0.0081  -0.0151 611  LEU A CG  
357  C CD1 . LEU A 74  ? 0.2736 0.3020 0.2465 -0.0195 0.0101  -0.0131 611  LEU A CD1 
358  C CD2 . LEU A 74  ? 0.3461 0.3763 0.3187 -0.0203 0.0112  -0.0192 611  LEU A CD2 
359  N N   . ILE A 75  ? 0.2609 0.2943 0.2685 -0.0092 0.0044  -0.0144 612  ILE A N   
360  C CA  . ILE A 75  ? 0.2884 0.3241 0.3053 -0.0071 0.0050  -0.0144 612  ILE A CA  
361  C C   . ILE A 75  ? 0.2771 0.3126 0.2963 -0.0067 0.0041  -0.0168 612  ILE A C   
362  O O   . ILE A 75  ? 0.2677 0.3047 0.2914 -0.0056 0.0059  -0.0180 612  ILE A O   
363  C CB  . ILE A 75  ? 0.2980 0.3338 0.3200 -0.0064 0.0022  -0.0121 612  ILE A CB  
364  C CG1 . ILE A 75  ? 0.3284 0.3649 0.3493 -0.0064 0.0033  -0.0096 612  ILE A CG1 
365  C CG2 . ILE A 75  ? 0.2863 0.3244 0.3174 -0.0051 0.0027  -0.0126 612  ILE A CG2 
366  C CD1 . ILE A 75  ? 0.3299 0.3695 0.3551 -0.0053 0.0076  -0.0093 612  ILE A CD1 
367  N N   . GLU A 76  ? 0.2711 0.3041 0.2866 -0.0076 0.0010  -0.0174 613  GLU A N   
368  C CA  . GLU A 76  ? 0.2601 0.2928 0.2775 -0.0072 -0.0001 -0.0196 613  GLU A CA  
369  C C   . GLU A 76  ? 0.3015 0.3357 0.3175 -0.0071 0.0029  -0.0222 613  GLU A C   
370  O O   . GLU A 76  ? 0.2788 0.3136 0.2992 -0.0059 0.0034  -0.0237 613  GLU A O   
371  C CB  . GLU A 76  ? 0.2751 0.3046 0.2877 -0.0082 -0.0037 -0.0201 613  GLU A CB  
372  C CG  . GLU A 76  ? 0.3042 0.3336 0.3198 -0.0075 -0.0050 -0.0221 613  GLU A CG  
373  C CD  . GLU A 76  ? 0.4848 0.5111 0.4946 -0.0085 -0.0078 -0.0231 613  GLU A CD  
374  O OE1 . GLU A 76  ? 0.4778 0.5014 0.4809 -0.0100 -0.0091 -0.0222 613  GLU A OE1 
375  O OE2 . GLU A 76  ? 0.4770 0.5032 0.4887 -0.0080 -0.0088 -0.0248 613  GLU A OE2 
376  N N   . ARG A 77  ? 0.2391 0.2735 0.2486 -0.0084 0.0046  -0.0231 614  ARG A N   
377  C CA  . ARG A 77  ? 0.2622 0.2987 0.2707 -0.0083 0.0072  -0.0264 614  ARG A CA  
378  C C   . ARG A 77  ? 0.2907 0.3295 0.3042 -0.0066 0.0101  -0.0269 614  ARG A C   
379  O O   . ARG A 77  ? 0.2869 0.3269 0.3022 -0.0056 0.0112  -0.0300 614  ARG A O   
380  C CB  . ARG A 77  ? 0.2972 0.3338 0.2973 -0.0108 0.0086  -0.0278 614  ARG A CB  
381  C CG  . ARG A 77  ? 0.3217 0.3553 0.3162 -0.0126 0.0057  -0.0279 614  ARG A CG  
382  C CD  . ARG A 77  ? 0.3543 0.3889 0.3505 -0.0119 0.0051  -0.0312 614  ARG A CD  
383  N NE  . ARG A 77  ? 0.3831 0.4147 0.3749 -0.0132 0.0021  -0.0312 614  ARG A NE  
384  C CZ  . ARG A 77  ? 0.4418 0.4741 0.4313 -0.0139 0.0020  -0.0343 614  ARG A CZ  
385  N NH1 . ARG A 77  ? 0.4400 0.4690 0.4254 -0.0151 -0.0009 -0.0339 614  ARG A NH1 
386  N NH2 . ARG A 77  ? 0.4167 0.4529 0.4081 -0.0133 0.0045  -0.0380 614  ARG A NH2 
387  N N   . LEU A 78  ? 0.2848 0.3238 0.3002 -0.0063 0.0109  -0.0240 615  LEU A N   
388  C CA  . LEU A 78  ? 0.2758 0.3164 0.2962 -0.0046 0.0134  -0.0240 615  LEU A CA  
389  C C   . LEU A 78  ? 0.3205 0.3600 0.3469 -0.0032 0.0121  -0.0246 615  LEU A C   
390  O O   . LEU A 78  ? 0.2741 0.3137 0.3036 -0.0019 0.0135  -0.0259 615  LEU A O   
391  C CB  . LEU A 78  ? 0.2576 0.2985 0.2793 -0.0046 0.0140  -0.0204 615  LEU A CB  
392  C CG  . LEU A 78  ? 0.2856 0.3280 0.3117 -0.0031 0.0168  -0.0198 615  LEU A CG  
393  C CD1 . LEU A 78  ? 0.2723 0.3166 0.2953 -0.0030 0.0199  -0.0226 615  LEU A CD1 
394  C CD2 . LEU A 78  ? 0.2854 0.3283 0.3134 -0.0031 0.0167  -0.0159 615  LEU A CD2 
395  N N   . THR A 79  ? 0.2777 0.3157 0.3052 -0.0037 0.0093  -0.0237 616  THR A N   
396  C CA  . THR A 79  ? 0.2359 0.2724 0.2683 -0.0031 0.0080  -0.0240 616  THR A CA  
397  C C   . THR A 79  ? 0.2735 0.3087 0.3045 -0.0035 0.0054  -0.0257 616  THR A C   
398  O O   . THR A 79  ? 0.2607 0.2949 0.2945 -0.0039 0.0034  -0.0251 616  THR A O   
399  C CB  . THR A 79  ? 0.2622 0.2990 0.2992 -0.0035 0.0073  -0.0211 616  THR A CB  
400  O OG1 . THR A 79  ? 0.2537 0.2906 0.2887 -0.0042 0.0052  -0.0198 616  THR A OG1 
401  C CG2 . THR A 79  ? 0.2900 0.3282 0.3291 -0.0029 0.0099  -0.0193 616  THR A CG2 
402  N N   . TYR A 80  ? 0.2831 0.2630 0.2644 0.0048  -0.0159 -0.0155 617  TYR A N   
403  C CA  . TYR A 80  ? 0.3051 0.2785 0.2839 0.0062  -0.0178 -0.0147 617  TYR A CA  
404  C C   . TYR A 80  ? 0.3448 0.3077 0.3139 0.0055  -0.0198 -0.0137 617  TYR A C   
405  O O   . TYR A 80  ? 0.3893 0.3483 0.3505 0.0075  -0.0213 -0.0130 617  TYR A O   
406  C CB  . TYR A 80  ? 0.3093 0.2843 0.2868 0.0114  -0.0186 -0.0146 617  TYR A CB  
407  C CG  . TYR A 80  ? 0.3070 0.2758 0.2820 0.0125  -0.0200 -0.0142 617  TYR A CG  
408  C CD1 . TYR A 80  ? 0.3753 0.3442 0.3555 0.0095  -0.0201 -0.0143 617  TYR A CD1 
409  C CD2 . TYR A 80  ? 0.3831 0.3457 0.3500 0.0172  -0.0219 -0.0140 617  TYR A CD2 
410  C CE1 . TYR A 80  ? 0.3960 0.3588 0.3728 0.0106  -0.0226 -0.0140 617  TYR A CE1 
411  C CE2 . TYR A 80  ? 0.4212 0.3766 0.3836 0.0179  -0.0235 -0.0138 617  TYR A CE2 
412  C CZ  . TYR A 80  ? 0.5115 0.4672 0.4787 0.0143  -0.0242 -0.0137 617  TYR A CZ  
413  O OH  . TYR A 80  ? 0.5103 0.4584 0.4721 0.0151  -0.0271 -0.0136 617  TYR A OH  
414  N N   . HIS A 81  ? 0.3476 0.3051 0.3163 0.0023  -0.0206 -0.0136 618  HIS A N   
415  C CA  . HIS A 81  ? 0.4127 0.3585 0.3710 -0.0006 -0.0220 -0.0127 618  HIS A CA  
416  C C   . HIS A 81  ? 0.4873 0.4214 0.4327 0.0051  -0.0258 -0.0116 618  HIS A C   
417  O O   . HIS A 81  ? 0.4730 0.3945 0.4058 0.0041  -0.0273 -0.0105 618  HIS A O   
418  C CB  . HIS A 81  ? 0.3526 0.2977 0.3157 -0.0069 -0.0217 -0.0136 618  HIS A CB  
419  C CG  . HIS A 81  ? 0.4014 0.3439 0.3650 -0.0047 -0.0253 -0.0138 618  HIS A CG  
420  N ND1 . HIS A 81  ? 0.4013 0.3516 0.3735 -0.0015 -0.0258 -0.0145 618  HIS A ND1 
421  C CD2 . HIS A 81  ? 0.4205 0.3517 0.3753 -0.0058 -0.0287 -0.0136 618  HIS A CD2 
422  C CE1 . HIS A 81  ? 0.5046 0.4487 0.4728 -0.0004 -0.0296 -0.0146 618  HIS A CE1 
423  N NE2 . HIS A 81  ? 0.4220 0.3550 0.3802 -0.0029 -0.0314 -0.0142 618  HIS A NE2 
424  N N   A MET A 82  ? 0.3957 0.3322 0.3424 0.0111  -0.0270 -0.0121 619  MET A N   
425  N N   B MET A 82  ? 0.3773 0.3139 0.3240 0.0111  -0.0270 -0.0121 619  MET A N   
426  C CA  A MET A 82  ? 0.4233 0.3483 0.3580 0.0171  -0.0301 -0.0119 619  MET A CA  
427  C CA  B MET A 82  ? 0.4103 0.3353 0.3450 0.0171  -0.0301 -0.0119 619  MET A CA  
428  C C   A MET A 82  ? 0.4657 0.3908 0.3952 0.0248  -0.0314 -0.0120 619  MET A C   
429  C C   B MET A 82  ? 0.4785 0.4031 0.4076 0.0245  -0.0314 -0.0119 619  MET A C   
430  O O   A MET A 82  ? 0.4625 0.3749 0.3796 0.0303  -0.0345 -0.0119 619  MET A O   
431  O O   B MET A 82  ? 0.4595 0.3705 0.3755 0.0292  -0.0347 -0.0116 619  MET A O   
432  C CB  A MET A 82  ? 0.4864 0.4127 0.4229 0.0201  -0.0303 -0.0128 619  MET A CB  
433  C CB  B MET A 82  ? 0.4223 0.3494 0.3591 0.0206  -0.0302 -0.0129 619  MET A CB  
434  C CG  A MET A 82  ? 0.6786 0.5970 0.6127 0.0150  -0.0325 -0.0129 619  MET A CG  
435  C CG  B MET A 82  ? 0.6101 0.5332 0.5482 0.0151  -0.0316 -0.0130 619  MET A CG  
436  S SD  A MET A 82  ? 0.9112 0.8281 0.8434 0.0186  -0.0337 -0.0138 619  MET A SD  
437  S SD  B MET A 82  ? 0.7638 0.6685 0.6885 0.0104  -0.0353 -0.0126 619  MET A SD  
438  C CE  A MET A 82  ? 0.9261 0.8338 0.8557 0.0113  -0.0382 -0.0142 619  MET A CE  
439  C CE  B MET A 82  ? 0.8327 0.7231 0.7414 0.0197  -0.0378 -0.0132 619  MET A CE  
440  N N   . TYR A 83  ? 0.4446 0.3835 0.3832 0.0257  -0.0296 -0.0125 620  TYR A N   
441  C CA  . TYR A 83  ? 0.4991 0.4411 0.4351 0.0330  -0.0319 -0.0132 620  TYR A CA  
442  C C   . TYR A 83  ? 0.4543 0.4114 0.4008 0.0307  -0.0302 -0.0139 620  TYR A C   
443  O O   . TYR A 83  ? 0.4019 0.3678 0.3583 0.0250  -0.0265 -0.0142 620  TYR A O   
444  C CB  . TYR A 83  ? 0.4820 0.4283 0.4191 0.0419  -0.0322 -0.0151 620  TYR A CB  
445  C CG  . TYR A 83  ? 0.4339 0.3912 0.3812 0.0395  -0.0278 -0.0162 620  TYR A CG  
446  C CD1 . TYR A 83  ? 0.4122 0.3863 0.3721 0.0372  -0.0246 -0.0172 620  TYR A CD1 
447  C CD2 . TYR A 83  ? 0.4584 0.4073 0.4009 0.0388  -0.0272 -0.0161 620  TYR A CD2 
448  C CE1 . TYR A 83  ? 0.4410 0.4215 0.4070 0.0342  -0.0205 -0.0177 620  TYR A CE1 
449  C CE2 . TYR A 83  ? 0.5012 0.4571 0.4498 0.0366  -0.0238 -0.0166 620  TYR A CE2 
450  C CZ  . TYR A 83  ? 0.4431 0.4140 0.4029 0.0343  -0.0202 -0.0172 620  TYR A CZ  
451  O OH  . TYR A 83  ? 0.4816 0.4561 0.4444 0.0315  -0.0168 -0.0173 620  TYR A OH  
452  N N   . ALA A 84  ? 0.5592 0.5183 0.5027 0.0357  -0.0337 -0.0143 621  ALA A N   
453  C CA  . ALA A 84  ? 0.5191 0.4930 0.4717 0.0344  -0.0333 -0.0156 621  ALA A CA  
454  C C   . ALA A 84  ? 0.4443 0.4361 0.4104 0.0374  -0.0310 -0.0182 621  ALA A C   
455  O O   . ALA A 84  ? 0.4007 0.3935 0.3671 0.0436  -0.0308 -0.0194 621  ALA A O   
456  C CB  . ALA A 84  ? 0.5714 0.5408 0.5151 0.0392  -0.0392 -0.0154 621  ALA A CB  
457  N N   . ASP A 85  ? 0.4203 0.4257 0.3967 0.0326  -0.0288 -0.0195 622  ASP A N   
458  C CA  . ASP A 85  ? 0.3264 0.3487 0.3152 0.0327  -0.0255 -0.0220 622  ASP A CA  
459  C C   . ASP A 85  ? 0.3837 0.4201 0.3804 0.0301  -0.0269 -0.0240 622  ASP A C   
460  O O   . ASP A 85  ? 0.3483 0.3900 0.3507 0.0225  -0.0234 -0.0245 622  ASP A O   
461  C CB  . ASP A 85  ? 0.3639 0.3845 0.3557 0.0262  -0.0199 -0.0211 622  ASP A CB  
462  C CG  . ASP A 85  ? 0.4402 0.4731 0.4401 0.0261  -0.0156 -0.0231 622  ASP A CG  
463  O OD1 . ASP A 85  ? 0.4110 0.4582 0.4179 0.0298  -0.0160 -0.0259 622  ASP A OD1 
464  O OD2 . ASP A 85  ? 0.4434 0.4719 0.4425 0.0222  -0.0117 -0.0221 622  ASP A OD2 
465  N N   . PRO A 86  ? 0.4218 0.4632 0.4178 0.0368  -0.0329 -0.0254 623  PRO A N   
466  C CA  . PRO A 86  ? 0.3907 0.4442 0.3925 0.0343  -0.0361 -0.0275 623  PRO A CA  
467  C C   . PRO A 86  ? 0.3206 0.3949 0.3381 0.0296  -0.0321 -0.0308 623  PRO A C   
468  O O   . PRO A 86  ? 0.3185 0.3989 0.3398 0.0226  -0.0323 -0.0320 623  PRO A O   
469  C CB  . PRO A 86  ? 0.4126 0.4671 0.4104 0.0450  -0.0444 -0.0285 623  PRO A CB  
470  C CG  . PRO A 86  ? 0.4537 0.5041 0.4496 0.0535  -0.0436 -0.0286 623  PRO A CG  
471  C CD  . PRO A 86  ? 0.4322 0.4666 0.4206 0.0475  -0.0379 -0.0254 623  PRO A CD  
472  N N   . ASN A 87  ? 0.3109 0.3952 0.3365 0.0325  -0.0281 -0.0325 624  ASN A N   
473  C CA  . ASN A 87  ? 0.3768 0.4800 0.4161 0.0262  -0.0232 -0.0357 624  ASN A CA  
474  C C   . ASN A 87  ? 0.3220 0.4167 0.3584 0.0150  -0.0175 -0.0337 624  ASN A C   
475  O O   . ASN A 87  ? 0.3099 0.4133 0.3525 0.0069  -0.0158 -0.0355 624  ASN A O   
476  C CB  . ASN A 87  ? 0.4176 0.5325 0.4644 0.0311  -0.0187 -0.0381 624  ASN A CB  
477  C CG  . ASN A 87  ? 0.4583 0.5870 0.5119 0.0428  -0.0243 -0.0417 624  ASN A CG  
478  O OD1 . ASN A 87  ? 0.4513 0.5884 0.5090 0.0449  -0.0314 -0.0433 624  ASN A OD1 
479  N ND2 . ASN A 87  ? 0.4740 0.6043 0.5280 0.0511  -0.0218 -0.0431 624  ASN A ND2 
480  N N   . PHE A 88  ? 0.2841 0.3609 0.3108 0.0148  -0.0151 -0.0303 625  PHE A N   
481  C CA  . PHE A 88  ? 0.2958 0.3630 0.3193 0.0063  -0.0108 -0.0286 625  PHE A CA  
482  C C   . PHE A 88  ? 0.2682 0.3304 0.2887 0.0016  -0.0134 -0.0283 625  PHE A C   
483  O O   . PHE A 88  ? 0.2876 0.3502 0.3098 -0.0060 -0.0106 -0.0292 625  PHE A O   
484  C CB  . PHE A 88  ? 0.2783 0.3296 0.2935 0.0083  -0.0091 -0.0255 625  PHE A CB  
485  C CG  . PHE A 88  ? 0.2924 0.3340 0.3047 0.0016  -0.0056 -0.0240 625  PHE A CG  
486  C CD1 . PHE A 88  ? 0.3481 0.3934 0.3630 -0.0047 -0.0010 -0.0248 625  PHE A CD1 
487  C CD2 . PHE A 88  ? 0.3129 0.3411 0.3195 0.0016  -0.0070 -0.0220 625  PHE A CD2 
488  C CE1 . PHE A 88  ? 0.3523 0.3855 0.3622 -0.0095 0.0012  -0.0233 625  PHE A CE1 
489  C CE2 . PHE A 88  ? 0.2896 0.3093 0.2944 -0.0027 -0.0047 -0.0211 625  PHE A CE2 
490  C CZ  . PHE A 88  ? 0.3054 0.3263 0.3109 -0.0076 -0.0011 -0.0216 625  PHE A CZ  
491  N N   . VAL A 89  ? 0.2461 0.3019 0.2603 0.0059  -0.0183 -0.0274 626  VAL A N   
492  C CA  . VAL A 89  ? 0.2417 0.2919 0.2510 0.0015  -0.0202 -0.0275 626  VAL A CA  
493  C C   . VAL A 89  ? 0.3091 0.3729 0.3252 -0.0032 -0.0217 -0.0308 626  VAL A C   
494  O O   . VAL A 89  ? 0.2651 0.3257 0.2798 -0.0105 -0.0199 -0.0317 626  VAL A O   
495  C CB  . VAL A 89  ? 0.3173 0.3584 0.3166 0.0065  -0.0254 -0.0260 626  VAL A CB  
496  C CG1 . VAL A 89  ? 0.2538 0.2909 0.2469 0.0019  -0.0274 -0.0268 626  VAL A CG1 
497  C CG2 . VAL A 89  ? 0.3272 0.3536 0.3192 0.0084  -0.0235 -0.0231 626  VAL A CG2 
498  N N   . ARG A 90  ? 0.2805 0.3597 0.3042 0.0010  -0.0253 -0.0330 627  ARG A N   
499  C CA  . ARG A 90  ? 0.2848 0.3799 0.3169 -0.0038 -0.0278 -0.0367 627  ARG A CA  
500  C C   . ARG A 90  ? 0.3026 0.4029 0.3412 -0.0136 -0.0211 -0.0382 627  ARG A C   
501  O O   . ARG A 90  ? 0.3206 0.4208 0.3585 -0.0218 -0.0212 -0.0399 627  ARG A O   
502  C CB  . ARG A 90  ? 0.2767 0.3910 0.3190 0.0036  -0.0330 -0.0396 627  ARG A CB  
503  C CG  . ARG A 90  ? 0.3649 0.4977 0.4171 -0.0015 -0.0371 -0.0441 627  ARG A CG  
504  C CD  . ARG A 90  ? 0.4689 0.6261 0.5362 0.0055  -0.0412 -0.0481 627  ARG A CD  
505  N NE  . ARG A 90  ? 0.6731 0.8255 0.7368 0.0186  -0.0438 -0.0465 627  ARG A NE  
506  C CZ  . ARG A 90  ? 0.6712 0.8287 0.7407 0.0231  -0.0381 -0.0468 627  ARG A CZ  
507  N NH1 . ARG A 90  ? 0.5805 0.7306 0.6442 0.0352  -0.0412 -0.0455 627  ARG A NH1 
508  N NH2 . ARG A 90  ? 0.6586 0.8263 0.7375 0.0150  -0.0293 -0.0484 627  ARG A NH2 
509  N N   . THR A 91  ? 0.2753 0.3780 0.3180 -0.0132 -0.0154 -0.0375 628  THR A N   
510  C CA  . THR A 91  ? 0.3163 0.4215 0.3624 -0.0228 -0.0087 -0.0385 628  THR A CA  
511  C C   . THR A 91  ? 0.2892 0.3742 0.3247 -0.0287 -0.0060 -0.0362 628  THR A C   
512  O O   . THR A 91  ? 0.2904 0.3738 0.3252 -0.0379 -0.0036 -0.0377 628  THR A O   
513  C CB  . THR A 91  ? 0.3489 0.4581 0.3982 -0.0206 -0.0031 -0.0379 628  THR A CB  
514  O OG1 . THR A 91  ? 0.3930 0.5225 0.4535 -0.0141 -0.0053 -0.0410 628  THR A OG1 
515  C CG2 . THR A 91  ? 0.3087 0.4182 0.3586 -0.0316 0.0042  -0.0386 628  THR A CG2 
516  N N   . PHE A 92  ? 0.2384 0.3081 0.2657 -0.0232 -0.0065 -0.0331 629  PHE A N   
517  C CA  . PHE A 92  ? 0.2470 0.2995 0.2661 -0.0267 -0.0045 -0.0316 629  PHE A CA  
518  C C   . PHE A 92  ? 0.2345 0.2855 0.2509 -0.0317 -0.0068 -0.0339 629  PHE A C   
519  O O   . PHE A 92  ? 0.2577 0.3012 0.2706 -0.0386 -0.0041 -0.0350 629  PHE A O   
520  C CB  . PHE A 92  ? 0.2423 0.2830 0.2559 -0.0200 -0.0054 -0.0288 629  PHE A CB  
521  C CG  . PHE A 92  ? 0.2902 0.3161 0.2981 -0.0221 -0.0032 -0.0280 629  PHE A CG  
522  C CD1 . PHE A 92  ? 0.2517 0.2723 0.2558 -0.0243 -0.0039 -0.0294 629  PHE A CD1 
523  C CD2 . PHE A 92  ? 0.3155 0.3325 0.3214 -0.0213 -0.0007 -0.0261 629  PHE A CD2 
524  C CE1 . PHE A 92  ? 0.2934 0.3019 0.2938 -0.0250 -0.0015 -0.0296 629  PHE A CE1 
525  C CE2 . PHE A 92  ? 0.2855 0.2900 0.2875 -0.0217 0.0004  -0.0259 629  PHE A CE2 
526  C CZ  . PHE A 92  ? 0.2842 0.2853 0.2845 -0.0232 0.0003  -0.0279 629  PHE A CZ  
527  N N   . LEU A 93  ? 0.2788 0.3348 0.2947 -0.0284 -0.0120 -0.0348 630  LEU A N   
528  C CA  . LEU A 93  ? 0.2593 0.3110 0.2695 -0.0330 -0.0142 -0.0369 630  LEU A CA  
529  C C   . LEU A 93  ? 0.3016 0.3632 0.3165 -0.0415 -0.0147 -0.0405 630  LEU A C   
530  O O   . LEU A 93  ? 0.3106 0.3645 0.3193 -0.0477 -0.0146 -0.0425 630  LEU A O   
531  C CB  . LEU A 93  ? 0.2624 0.3147 0.2676 -0.0277 -0.0201 -0.0368 630  LEU A CB  
532  C CG  . LEU A 93  ? 0.2768 0.3146 0.2738 -0.0230 -0.0183 -0.0338 630  LEU A CG  
533  C CD1 . LEU A 93  ? 0.3037 0.3390 0.2927 -0.0182 -0.0238 -0.0329 630  LEU A CD1 
534  C CD2 . LEU A 93  ? 0.3023 0.3269 0.2933 -0.0274 -0.0135 -0.0344 630  LEU A CD2 
535  N N   . THR A 94  ? 0.2494 0.3282 0.2754 -0.0421 -0.0149 -0.0417 631  THR A N   
536  C CA  . THR A 94  ? 0.2488 0.3395 0.2814 -0.0519 -0.0146 -0.0454 631  THR A CA  
537  C C   . THR A 94  ? 0.2879 0.3664 0.3158 -0.0607 -0.0076 -0.0450 631  THR A C   
538  O O   . THR A 94  ? 0.2889 0.3652 0.3143 -0.0705 -0.0071 -0.0477 631  THR A O   
539  C CB  . THR A 94  ? 0.2793 0.3947 0.3272 -0.0499 -0.0157 -0.0475 631  THR A CB  
540  O OG1 . THR A 94  ? 0.3139 0.4396 0.3650 -0.0415 -0.0239 -0.0485 631  THR A OG1 
541  C CG2 . THR A 94  ? 0.2435 0.3737 0.3004 -0.0621 -0.0137 -0.0518 631  THR A CG2 
542  N N   . THR A 95  ? 0.2810 0.3496 0.3058 -0.0573 -0.0027 -0.0416 632  THR A N   
543  C CA  . THR A 95  ? 0.2739 0.3311 0.2933 -0.0649 0.0033  -0.0408 632  THR A CA  
544  C C   . THR A 95  ? 0.2749 0.3072 0.2816 -0.0631 0.0052  -0.0384 632  THR A C   
545  O O   . THR A 95  ? 0.3295 0.3488 0.3290 -0.0690 0.0091  -0.0378 632  THR A O   
546  C CB  . THR A 95  ? 0.3365 0.4006 0.3605 -0.0640 0.0080  -0.0392 632  THR A CB  
547  O OG1 . THR A 95  ? 0.3106 0.3683 0.3322 -0.0532 0.0073  -0.0358 632  THR A OG1 
548  C CG2 . THR A 95  ? 0.3349 0.4259 0.3735 -0.0657 0.0075  -0.0425 632  THR A CG2 
549  N N   . TYR A 96  ? 0.2778 0.3033 0.2815 -0.0552 0.0025  -0.0373 633  TYR A N   
550  C CA  . TYR A 96  ? 0.3099 0.3162 0.3056 -0.0514 0.0045  -0.0353 633  TYR A CA  
551  C C   . TYR A 96  ? 0.3568 0.3466 0.3430 -0.0574 0.0062  -0.0371 633  TYR A C   
552  O O   . TYR A 96  ? 0.3591 0.3327 0.3387 -0.0548 0.0079  -0.0357 633  TYR A O   
553  C CB  . TYR A 96  ? 0.2610 0.2654 0.2568 -0.0430 0.0022  -0.0344 633  TYR A CB  
554  C CG  . TYR A 96  ? 0.2972 0.2977 0.2883 -0.0448 0.0008  -0.0373 633  TYR A CG  
555  C CD1 . TYR A 96  ? 0.3203 0.3054 0.3042 -0.0452 0.0031  -0.0388 633  TYR A CD1 
556  C CD2 . TYR A 96  ? 0.2818 0.2932 0.2745 -0.0454 -0.0029 -0.0388 633  TYR A CD2 
557  C CE1 . TYR A 96  ? 0.3212 0.3021 0.2994 -0.0469 0.0027  -0.0419 633  TYR A CE1 
558  C CE2 . TYR A 96  ? 0.2920 0.2981 0.2778 -0.0473 -0.0042 -0.0414 633  TYR A CE2 
559  C CZ  . TYR A 96  ? 0.3328 0.3236 0.3111 -0.0484 -0.0008 -0.0430 633  TYR A CZ  
560  O OH  . TYR A 96  ? 0.3747 0.3595 0.3447 -0.0505 -0.0012 -0.0461 633  TYR A OH  
561  N N   . ARG A 97  ? 0.3396 0.3324 0.3244 -0.0650 0.0052  -0.0404 634  ARG A N   
562  C CA  . ARG A 97  ? 0.3373 0.3118 0.3110 -0.0701 0.0065  -0.0427 634  ARG A CA  
563  C C   . ARG A 97  ? 0.3992 0.3606 0.3659 -0.0764 0.0100  -0.0415 634  ARG A C   
564  O O   . ARG A 97  ? 0.4087 0.3495 0.3637 -0.0785 0.0112  -0.0425 634  ARG A O   
565  C CB  . ARG A 97  ? 0.3783 0.3583 0.3507 -0.0774 0.0038  -0.0469 634  ARG A CB  
566  C CG  . ARG A 97  ? 0.3427 0.3311 0.3175 -0.0714 0.0001  -0.0478 634  ARG A CG  
567  C CD  . ARG A 97  ? 0.3621 0.3624 0.3383 -0.0779 -0.0045 -0.0513 634  ARG A CD  
568  N NE  . ARG A 97  ? 0.3500 0.3593 0.3282 -0.0711 -0.0088 -0.0510 634  ARG A NE  
569  C CZ  . ARG A 97  ? 0.3649 0.3903 0.3527 -0.0657 -0.0117 -0.0489 634  ARG A CZ  
570  N NH1 . ARG A 97  ? 0.3280 0.3649 0.3261 -0.0661 -0.0102 -0.0475 634  ARG A NH1 
571  N NH2 . ARG A 97  ? 0.3382 0.3667 0.3237 -0.0597 -0.0159 -0.0484 634  ARG A NH2 
572  N N   . SER A 98  ? 0.3480 0.3201 0.3203 -0.0791 0.0118  -0.0395 635  SER A N   
573  C CA  . SER A 98  ? 0.3980 0.3570 0.3617 -0.0853 0.0159  -0.0375 635  SER A CA  
574  C C   . SER A 98  ? 0.3949 0.3367 0.3511 -0.0765 0.0163  -0.0337 635  SER A C   
575  O O   . SER A 98  ? 0.4406 0.3661 0.3855 -0.0806 0.0189  -0.0316 635  SER A O   
576  C CB  . SER A 98  ? 0.4100 0.3883 0.3824 -0.0917 0.0188  -0.0373 635  SER A CB  
577  O OG  . SER A 98  ? 0.3463 0.3373 0.3275 -0.0822 0.0182  -0.0350 635  SER A OG  
578  N N   . PHE A 99  ? 0.3926 0.3373 0.3541 -0.0651 0.0135  -0.0328 636  PHE A N   
579  C CA  . PHE A 99  ? 0.4371 0.3670 0.3931 -0.0565 0.0126  -0.0298 636  PHE A CA  
580  C C   . PHE A 99  ? 0.4217 0.3482 0.3806 -0.0469 0.0099  -0.0312 636  PHE A C   
581  O O   . PHE A 99  ? 0.4468 0.3627 0.4032 -0.0392 0.0083  -0.0297 636  PHE A O   
582  C CB  . PHE A 99  ? 0.4029 0.3420 0.3636 -0.0526 0.0128  -0.0265 636  PHE A CB  
583  C CG  . PHE A 99  ? 0.3853 0.3465 0.3595 -0.0480 0.0113  -0.0270 636  PHE A CG  
584  C CD1 . PHE A 99  ? 0.3713 0.3347 0.3506 -0.0390 0.0083  -0.0267 636  PHE A CD1 
585  C CD2 . PHE A 99  ? 0.3541 0.3335 0.3356 -0.0527 0.0128  -0.0278 636  PHE A CD2 
586  C CE1 . PHE A 99  ? 0.3330 0.3126 0.3213 -0.0353 0.0067  -0.0268 636  PHE A CE1 
587  C CE2 . PHE A 99  ? 0.3140 0.3106 0.3058 -0.0472 0.0106  -0.0282 636  PHE A CE2 
588  C CZ  . PHE A 99  ? 0.3054 0.3004 0.2992 -0.0387 0.0074  -0.0273 636  PHE A CZ  
589  N N   . CYS A 100 ? 0.3444 0.2794 0.3080 -0.0477 0.0095  -0.0343 637  CYS A N   
590  C CA  . CYS A 100 ? 0.3900 0.3243 0.3569 -0.0397 0.0085  -0.0360 637  CYS A CA  
591  C C   . CYS A 100 ? 0.4517 0.3868 0.4162 -0.0436 0.0090  -0.0401 637  CYS A C   
592  O O   . CYS A 100 ? 0.4277 0.3737 0.3941 -0.0499 0.0083  -0.0409 637  CYS A O   
593  C CB  . CYS A 100 ? 0.3476 0.2971 0.3248 -0.0336 0.0070  -0.0339 637  CYS A CB  
594  S SG  . CYS A 100 ? 0.4029 0.3559 0.3856 -0.0263 0.0070  -0.0360 637  CYS A SG  
595  N N   . LYS A 101 ? 0.4049 0.3288 0.3652 -0.0396 0.0101  -0.0430 638  LYS A N   
596  C CA  . LYS A 101 ? 0.4193 0.3419 0.3748 -0.0433 0.0110  -0.0473 638  LYS A CA  
597  C C   . LYS A 101 ? 0.3790 0.3164 0.3409 -0.0406 0.0108  -0.0477 638  LYS A C   
598  O O   . LYS A 101 ? 0.4048 0.3491 0.3743 -0.0343 0.0109  -0.0457 638  LYS A O   
599  C CB  . LYS A 101 ? 0.4611 0.3655 0.4086 -0.0394 0.0131  -0.0510 638  LYS A CB  
600  C CG  . LYS A 101 ? 0.5338 0.4181 0.4704 -0.0422 0.0129  -0.0509 638  LYS A CG  
601  C CD  . LYS A 101 ? 0.7407 0.6124 0.6648 -0.0504 0.0138  -0.0549 638  LYS A CD  
602  C CE  . LYS A 101 ? 0.9331 0.7788 0.8431 -0.0515 0.0139  -0.0554 638  LYS A CE  
603  N NZ  . LYS A 101 ? 0.9793 0.8117 0.8878 -0.0389 0.0143  -0.0570 638  LYS A NZ  
604  N N   . PRO A 102 ? 0.4408 0.3815 0.3981 -0.0461 0.0100  -0.0502 639  PRO A N   
605  C CA  . PRO A 102 ? 0.3912 0.3416 0.3499 -0.0441 0.0095  -0.0505 639  PRO A CA  
606  C C   . PRO A 102 ? 0.4225 0.3696 0.3825 -0.0373 0.0135  -0.0518 639  PRO A C   
607  O O   . PRO A 102 ? 0.3880 0.3439 0.3534 -0.0340 0.0136  -0.0497 639  PRO A O   
608  C CB  . PRO A 102 ? 0.4633 0.4108 0.4123 -0.0511 0.0080  -0.0541 639  PRO A CB  
609  C CG  . PRO A 102 ? 0.4722 0.4178 0.4202 -0.0584 0.0061  -0.0543 639  PRO A CG  
610  C CD  . PRO A 102 ? 0.4789 0.4142 0.4282 -0.0553 0.0088  -0.0527 639  PRO A CD  
611  N N   . GLN A 103 ? 0.4669 0.4016 0.4220 -0.0354 0.0171  -0.0557 640  GLN A N   
612  C CA  . GLN A 103 ? 0.4414 0.3758 0.4004 -0.0287 0.0217  -0.0580 640  GLN A CA  
613  C C   . GLN A 103 ? 0.4142 0.3554 0.3857 -0.0223 0.0209  -0.0549 640  GLN A C   
614  O O   . GLN A 103 ? 0.4189 0.3681 0.3975 -0.0187 0.0232  -0.0551 640  GLN A O   
615  C CB  . GLN A 103 ? 0.4989 0.4185 0.4510 -0.0264 0.0252  -0.0634 640  GLN A CB  
616  C CG  . GLN A 103 ? 0.4875 0.3990 0.4256 -0.0323 0.0269  -0.0677 640  GLN A CG  
617  C CD  . GLN A 103 ? 0.6291 0.5447 0.5647 -0.0311 0.0321  -0.0708 640  GLN A CD  
618  O OE1 . GLN A 103 ? 0.6917 0.6170 0.6374 -0.0263 0.0351  -0.0701 640  GLN A OE1 
619  N NE2 . GLN A 103 ? 0.5681 0.4759 0.4893 -0.0362 0.0333  -0.0744 640  GLN A NE2 
620  N N   . GLU A 104 ? 0.3815 0.3185 0.3543 -0.0218 0.0176  -0.0521 641  GLU A N   
621  C CA  . GLU A 104 ? 0.4538 0.3948 0.4359 -0.0161 0.0156  -0.0489 641  GLU A CA  
622  C C   . GLU A 104 ? 0.4216 0.3767 0.4100 -0.0171 0.0138  -0.0451 641  GLU A C   
623  O O   . GLU A 104 ? 0.3258 0.2875 0.3225 -0.0127 0.0137  -0.0441 641  GLU A O   
624  C CB  . GLU A 104 ? 0.4456 0.3756 0.4230 -0.0167 0.0127  -0.0467 641  GLU A CB  
625  C CG  . GLU A 104 ? 0.4761 0.4063 0.4594 -0.0108 0.0098  -0.0434 641  GLU A CG  
626  C CD  . GLU A 104 ? 0.6102 0.5279 0.5848 -0.0136 0.0075  -0.0405 641  GLU A CD  
627  O OE1 . GLU A 104 ? 0.5201 0.4378 0.4966 -0.0105 0.0048  -0.0371 641  GLU A OE1 
628  O OE2 . GLU A 104 ? 0.5233 0.4305 0.4878 -0.0197 0.0087  -0.0417 641  GLU A OE2 
629  N N   . LEU A 105 ? 0.3702 0.3297 0.3546 -0.0228 0.0120  -0.0434 642  LEU A N   
630  C CA  . LEU A 105 ? 0.3089 0.2797 0.2973 -0.0228 0.0098  -0.0401 642  LEU A CA  
631  C C   . LEU A 105 ? 0.3200 0.2947 0.3090 -0.0216 0.0121  -0.0413 642  LEU A C   
632  O O   . LEU A 105 ? 0.3135 0.2936 0.3076 -0.0191 0.0115  -0.0391 642  LEU A O   
633  C CB  . LEU A 105 ? 0.3631 0.3389 0.3478 -0.0281 0.0070  -0.0392 642  LEU A CB  
634  C CG  . LEU A 105 ? 0.3196 0.3055 0.3062 -0.0271 0.0041  -0.0366 642  LEU A CG  
635  C CD1 . LEU A 105 ? 0.2874 0.2769 0.2804 -0.0227 0.0030  -0.0333 642  LEU A CD1 
636  C CD2 . LEU A 105 ? 0.2822 0.2749 0.2671 -0.0312 0.0006  -0.0368 642  LEU A CD2 
637  N N   . LEU A 106 ? 0.3054 0.2760 0.2875 -0.0241 0.0152  -0.0448 643  LEU A N   
638  C CA  . LEU A 106 ? 0.3326 0.3054 0.3129 -0.0242 0.0188  -0.0462 643  LEU A CA  
639  C C   . LEU A 106 ? 0.3377 0.3137 0.3284 -0.0196 0.0223  -0.0475 643  LEU A C   
640  O O   . LEU A 106 ? 0.3147 0.2965 0.3088 -0.0198 0.0236  -0.0463 643  LEU A O   
641  C CB  . LEU A 106 ? 0.3224 0.2885 0.2917 -0.0278 0.0224  -0.0504 643  LEU A CB  
642  C CG  . LEU A 106 ? 0.3337 0.3005 0.2982 -0.0292 0.0275  -0.0519 643  LEU A CG  
643  C CD1 . LEU A 106 ? 0.3506 0.3212 0.3118 -0.0309 0.0243  -0.0475 643  LEU A CD1 
644  C CD2 . LEU A 106 ? 0.3647 0.3230 0.3151 -0.0330 0.0308  -0.0562 643  LEU A CD2 
645  N N   . SER A 107 ? 0.3752 0.3473 0.3709 -0.0156 0.0233  -0.0500 644  SER A N   
646  C CA  . SER A 107 ? 0.3288 0.3062 0.3367 -0.0101 0.0253  -0.0518 644  SER A CA  
647  C C   . SER A 107 ? 0.3477 0.3317 0.3635 -0.0084 0.0208  -0.0474 644  SER A C   
648  O O   . SER A 107 ? 0.3341 0.3262 0.3585 -0.0074 0.0223  -0.0480 644  SER A O   
649  C CB  . SER A 107 ? 0.4279 0.3978 0.4382 -0.0044 0.0252  -0.0551 644  SER A CB  
650  O OG  . SER A 107 ? 0.4219 0.3848 0.4246 -0.0054 0.0301  -0.0600 644  SER A OG  
651  N N   . LEU A 108 ? 0.3012 0.2817 0.3136 -0.0087 0.0157  -0.0435 645  LEU A N   
652  C CA  . LEU A 108 ? 0.2992 0.2839 0.3164 -0.0071 0.0115  -0.0395 645  LEU A CA  
653  C C   . LEU A 108 ? 0.3231 0.3138 0.3391 -0.0103 0.0119  -0.0376 645  LEU A C   
654  O O   . LEU A 108 ? 0.3007 0.2958 0.3226 -0.0091 0.0105  -0.0363 645  LEU A O   
655  C CB  . LEU A 108 ? 0.2948 0.2746 0.3070 -0.0076 0.0076  -0.0361 645  LEU A CB  
656  C CG  . LEU A 108 ? 0.3649 0.3355 0.3764 -0.0043 0.0062  -0.0368 645  LEU A CG  
657  C CD1 . LEU A 108 ? 0.3439 0.3085 0.3473 -0.0080 0.0046  -0.0342 645  LEU A CD1 
658  C CD2 . LEU A 108 ? 0.3927 0.3644 0.4114 0.0014  0.0029  -0.0358 645  LEU A CD2 
659  N N   . LEU A 109 ? 0.3021 0.2914 0.3091 -0.0144 0.0130  -0.0374 646  LEU A N   
660  C CA  . LEU A 109 ? 0.2600 0.2512 0.2624 -0.0169 0.0124  -0.0350 646  LEU A CA  
661  C C   . LEU A 109 ? 0.3324 0.3259 0.3369 -0.0190 0.0174  -0.0372 646  LEU A C   
662  O O   . LEU A 109 ? 0.3239 0.3187 0.3282 -0.0205 0.0169  -0.0353 646  LEU A O   
663  C CB  . LEU A 109 ? 0.2871 0.2754 0.2782 -0.0199 0.0109  -0.0343 646  LEU A CB  
664  C CG  . LEU A 109 ? 0.2993 0.2893 0.2902 -0.0187 0.0058  -0.0320 646  LEU A CG  
665  C CD1 . LEU A 109 ? 0.3185 0.3079 0.3009 -0.0217 0.0040  -0.0327 646  LEU A CD1 
666  C CD2 . LEU A 109 ? 0.2952 0.2875 0.2873 -0.0161 0.0023  -0.0285 646  LEU A CD2 
667  N N   . ILE A 110 ? 0.3023 0.2961 0.3086 -0.0194 0.0227  -0.0416 647  ILE A N   
668  C CA  . ILE A 110 ? 0.2841 0.2827 0.2947 -0.0217 0.0291  -0.0449 647  ILE A CA  
669  C C   . ILE A 110 ? 0.3114 0.3187 0.3377 -0.0185 0.0280  -0.0455 647  ILE A C   
670  O O   . ILE A 110 ? 0.3416 0.3540 0.3716 -0.0220 0.0302  -0.0455 647  ILE A O   
671  C CB  . ILE A 110 ? 0.3550 0.3522 0.3640 -0.0218 0.0355  -0.0503 647  ILE A CB  
672  C CG1 . ILE A 110 ? 0.3143 0.3026 0.3056 -0.0264 0.0362  -0.0497 647  ILE A CG1 
673  C CG2 . ILE A 110 ? 0.3675 0.3736 0.3860 -0.0229 0.0432  -0.0549 647  ILE A CG2 
674  C CD1 . ILE A 110 ? 0.3650 0.3489 0.3508 -0.0269 0.0421  -0.0551 647  ILE A CD1 
675  N N   . GLU A 111 ? 0.3135 0.3213 0.3478 -0.0124 0.0241  -0.0459 648  GLU A N   
676  C CA  . GLU A 111 ? 0.3264 0.3412 0.3742 -0.0085 0.0206  -0.0461 648  GLU A CA  
677  C C   . GLU A 111 ? 0.3372 0.3521 0.3829 -0.0110 0.0162  -0.0416 648  GLU A C   
678  O O   . GLU A 111 ? 0.2925 0.3147 0.3473 -0.0121 0.0158  -0.0425 648  GLU A O   
679  C CB  . GLU A 111 ? 0.3018 0.3117 0.3523 -0.0015 0.0157  -0.0460 648  GLU A CB  
680  C CG  . GLU A 111 ? 0.3297 0.3456 0.3932 0.0039  0.0112  -0.0469 648  GLU A CG  
681  C CD  . GLU A 111 ? 0.4216 0.4283 0.4829 0.0105  0.0054  -0.0457 648  GLU A CD  
682  O OE1 . GLU A 111 ? 0.4067 0.4156 0.4756 0.0155  -0.0002 -0.0456 648  GLU A OE1 
683  O OE2 . GLU A 111 ? 0.4134 0.4095 0.4640 0.0100  0.0061  -0.0447 648  GLU A OE2 
684  N N   . ARG A 112 ? 0.2995 0.3067 0.3336 -0.0120 0.0129  -0.0373 649  ARG A N   
685  C CA  . ARG A 112 ? 0.2773 0.2822 0.3069 -0.0134 0.0088  -0.0333 649  ARG A CA  
686  C C   . ARG A 112 ? 0.3040 0.3093 0.3295 -0.0195 0.0123  -0.0334 649  ARG A C   
687  O O   . ARG A 112 ? 0.2631 0.2686 0.2897 -0.0213 0.0101  -0.0320 649  ARG A O   
688  C CB  . ARG A 112 ? 0.2939 0.2922 0.3127 -0.0124 0.0055  -0.0299 649  ARG A CB  
689  C CG  . ARG A 112 ? 0.3429 0.3378 0.3558 -0.0122 0.0013  -0.0262 649  ARG A CG  
690  C CD  . ARG A 112 ? 0.2696 0.2644 0.2871 -0.0082 -0.0031 -0.0249 649  ARG A CD  
691  N NE  . ARG A 112 ? 0.2912 0.2815 0.3012 -0.0071 -0.0066 -0.0219 649  ARG A NE  
692  C CZ  . ARG A 112 ? 0.2836 0.2715 0.2935 -0.0068 -0.0095 -0.0209 649  ARG A CZ  
693  N NH1 . ARG A 112 ? 0.2517 0.2433 0.2701 -0.0082 -0.0099 -0.0227 649  ARG A NH1 
694  N NH2 . ARG A 112 ? 0.2916 0.2738 0.2930 -0.0050 -0.0124 -0.0186 649  ARG A NH2 
695  N N   . PHE A 113 ? 0.2692 0.2730 0.2884 -0.0232 0.0178  -0.0352 650  PHE A N   
696  C CA  . PHE A 113 ? 0.3166 0.3170 0.3270 -0.0301 0.0217  -0.0347 650  PHE A CA  
697  C C   . PHE A 113 ? 0.3034 0.3129 0.3253 -0.0342 0.0264  -0.0379 650  PHE A C   
698  O O   . PHE A 113 ? 0.3299 0.3364 0.3469 -0.0401 0.0273  -0.0365 650  PHE A O   
699  C CB  . PHE A 113 ? 0.3467 0.3416 0.3449 -0.0331 0.0264  -0.0359 650  PHE A CB  
700  C CG  . PHE A 113 ? 0.3416 0.3273 0.3238 -0.0399 0.0289  -0.0339 650  PHE A CG  
701  C CD1 . PHE A 113 ? 0.3729 0.3611 0.3557 -0.0470 0.0367  -0.0365 650  PHE A CD1 
702  C CD2 . PHE A 113 ? 0.3643 0.3385 0.3301 -0.0391 0.0234  -0.0297 650  PHE A CD2 
703  C CE1 . PHE A 113 ? 0.4332 0.4095 0.3978 -0.0543 0.0394  -0.0343 650  PHE A CE1 
704  C CE2 . PHE A 113 ? 0.3765 0.3385 0.3242 -0.0446 0.0247  -0.0275 650  PHE A CE2 
705  C CZ  . PHE A 113 ? 0.3846 0.3462 0.3303 -0.0527 0.0329  -0.0295 650  PHE A CZ  
706  N N   . GLU A 114 ? 0.3105 0.3309 0.3475 -0.0312 0.0295  -0.0427 651  GLU A N   
707  C CA  . GLU A 114 ? 0.2868 0.3200 0.3379 -0.0351 0.0352  -0.0473 651  GLU A CA  
708  C C   . GLU A 114 ? 0.3006 0.3415 0.3655 -0.0330 0.0289  -0.0471 651  GLU A C   
709  O O   . GLU A 114 ? 0.3495 0.4010 0.4308 -0.0270 0.0267  -0.0505 651  GLU A O   
710  C CB  . GLU A 114 ? 0.2973 0.3392 0.3584 -0.0316 0.0413  -0.0533 651  GLU A CB  
711  C CG  . GLU A 114 ? 0.4149 0.4471 0.4593 -0.0348 0.0473  -0.0536 651  GLU A CG  
712  C CD  . GLU A 114 ? 0.6241 0.6621 0.6751 -0.0314 0.0541  -0.0600 651  GLU A CD  
713  O OE1 . GLU A 114 ? 0.6616 0.7078 0.7285 -0.0237 0.0519  -0.0634 651  GLU A OE1 
714  O OE2 . GLU A 114 ? 0.7245 0.7570 0.7632 -0.0361 0.0613  -0.0618 651  GLU A OE2 
715  N N   . ILE A 115 ? 0.2952 0.3289 0.3514 -0.0375 0.0253  -0.0430 652  ILE A N   
716  C CA  . ILE A 115 ? 0.2566 0.2939 0.3213 -0.0362 0.0183  -0.0422 652  ILE A CA  
717  C C   . ILE A 115 ? 0.2716 0.3235 0.3516 -0.0428 0.0219  -0.0467 652  ILE A C   
718  O O   . ILE A 115 ? 0.2929 0.3432 0.3666 -0.0526 0.0281  -0.0470 652  ILE A O   
719  C CB  . ILE A 115 ? 0.2997 0.3218 0.3475 -0.0381 0.0131  -0.0366 652  ILE A CB  
720  C CG1 . ILE A 115 ? 0.2922 0.3032 0.3268 -0.0320 0.0103  -0.0329 652  ILE A CG1 
721  C CG2 . ILE A 115 ? 0.3108 0.3346 0.3651 -0.0364 0.0054  -0.0359 652  ILE A CG2 
722  C CD1 . ILE A 115 ? 0.2920 0.2884 0.3087 -0.0332 0.0069  -0.0282 652  ILE A CD1 
723  N N   . PRO A 116 ? 0.2906 0.3569 0.3906 -0.0377 0.0179  -0.0504 653  PRO A N   
724  C CA  . PRO A 116 ? 0.2744 0.3582 0.3923 -0.0441 0.0202  -0.0554 653  PRO A CA  
725  C C   . PRO A 116 ? 0.3074 0.3854 0.4202 -0.0503 0.0140  -0.0525 653  PRO A C   
726  O O   . PRO A 116 ? 0.2874 0.3524 0.3896 -0.0453 0.0057  -0.0479 653  PRO A O   
727  C CB  . PRO A 116 ? 0.3302 0.4298 0.4700 -0.0339 0.0157  -0.0602 653  PRO A CB  
728  C CG  . PRO A 116 ? 0.3559 0.4405 0.4847 -0.0241 0.0069  -0.0553 653  PRO A CG  
729  C CD  . PRO A 116 ? 0.2812 0.3479 0.3874 -0.0262 0.0107  -0.0503 653  PRO A CD  
730  N N   . GLU A 117 ? 0.2708 0.3574 0.3900 -0.0616 0.0185  -0.0553 654  GLU A N   
731  C CA  . GLU A 117 ? 0.3179 0.3978 0.4316 -0.0684 0.0124  -0.0531 654  GLU A CA  
732  C C   . GLU A 117 ? 0.2832 0.3801 0.4190 -0.0638 0.0037  -0.0571 654  GLU A C   
733  O O   . GLU A 117 ? 0.2714 0.3896 0.4299 -0.0597 0.0054  -0.0629 654  GLU A O   
734  C CB  . GLU A 117 ? 0.3250 0.4041 0.4333 -0.0843 0.0208  -0.0542 654  GLU A CB  
735  C CG  . GLU A 117 ? 0.3689 0.4293 0.4530 -0.0881 0.0285  -0.0502 654  GLU A CG  
736  C CD  . GLU A 117 ? 0.4254 0.4777 0.4969 -0.1041 0.0361  -0.0499 654  GLU A CD  
737  O OE1 . GLU A 117 ? 0.3632 0.4316 0.4505 -0.1144 0.0396  -0.0547 654  GLU A OE1 
738  O OE2 . GLU A 117 ? 0.4490 0.4785 0.4943 -0.1066 0.0383  -0.0449 654  GLU A OE2 
739  N N   . PRO A 118 ? 0.2782 0.3649 0.4066 -0.0636 -0.0061 -0.0541 655  PRO A N   
740  C CA  . PRO A 118 ? 0.2912 0.3921 0.4380 -0.0599 -0.0159 -0.0577 655  PRO A CA  
741  C C   . PRO A 118 ? 0.3131 0.4399 0.4847 -0.0691 -0.0120 -0.0650 655  PRO A C   
742  O O   . PRO A 118 ? 0.3618 0.4888 0.5294 -0.0822 -0.0028 -0.0658 655  PRO A O   
743  C CB  . PRO A 118 ? 0.3681 0.4502 0.4973 -0.0628 -0.0245 -0.0534 655  PRO A CB  
744  C CG  . PRO A 118 ? 0.3823 0.4399 0.4843 -0.0641 -0.0201 -0.0473 655  PRO A CG  
745  C CD  . PRO A 118 ? 0.3520 0.4139 0.4543 -0.0680 -0.0082 -0.0481 655  PRO A CD  
746  N N   . GLU A 119 ? 0.3009 0.4488 0.4968 -0.0626 -0.0190 -0.0703 656  GLU A N   
747  C CA  . GLU A 119 ? 0.3672 0.5436 0.5905 -0.0708 -0.0172 -0.0782 656  GLU A CA  
748  C C   . GLU A 119 ? 0.3503 0.5214 0.5663 -0.0870 -0.0182 -0.0775 656  GLU A C   
749  O O   . GLU A 119 ? 0.3154 0.4706 0.5180 -0.0863 -0.0287 -0.0738 656  GLU A O   
750  C CB  . GLU A 119 ? 0.5424 0.7382 0.7896 -0.0592 -0.0291 -0.0831 656  GLU A CB  
751  C CG  . GLU A 119 ? 0.8024 1.0307 1.0818 -0.0557 -0.0238 -0.0920 656  GLU A CG  
752  C CD  . GLU A 119 ? 0.9733 1.1976 1.2494 -0.0449 -0.0161 -0.0916 656  GLU A CD  
753  O OE1 . GLU A 119 ? 0.9399 1.1610 1.2180 -0.0292 -0.0242 -0.0912 656  GLU A OE1 
754  O OE2 . GLU A 119 ? 1.0622 1.2848 1.3318 -0.0524 -0.0021 -0.0917 656  GLU A OE2 
755  N N   . PRO A 120 ? 0.3753 0.5580 0.5984 -0.1022 -0.0070 -0.0813 657  PRO A N   
756  C CA  . PRO A 120 ? 0.3657 0.5431 0.5822 -0.1190 -0.0081 -0.0812 657  PRO A CA  
757  C C   . PRO A 120 ? 0.3607 0.5536 0.5960 -0.1186 -0.0219 -0.0855 657  PRO A C   
758  O O   . PRO A 120 ? 0.3165 0.5379 0.5814 -0.1109 -0.0261 -0.0919 657  PRO A O   
759  C CB  . PRO A 120 ? 0.4699 0.6646 0.6979 -0.1345 0.0071  -0.0864 657  PRO A CB  
760  C CG  . PRO A 120 ? 0.5625 0.7530 0.7838 -0.1266 0.0176  -0.0848 657  PRO A CG  
761  C CD  . PRO A 120 ? 0.5025 0.6980 0.7337 -0.1059 0.0082  -0.0848 657  PRO A CD  
762  N N   . THR A 121 ? 0.3707 0.5438 0.5877 -0.1259 -0.0296 -0.0820 658  THR A N   
763  C CA  . THR A 121 ? 0.4769 0.6616 0.7079 -0.1270 -0.0434 -0.0859 658  THR A CA  
764  C C   . THR A 121 ? 0.4616 0.6767 0.7198 -0.1438 -0.0387 -0.0943 658  THR A C   
765  O O   . THR A 121 ? 0.4949 0.7168 0.7557 -0.1556 -0.0240 -0.0961 658  THR A O   
766  C CB  . THR A 121 ? 0.5972 0.7489 0.7976 -0.1302 -0.0524 -0.0800 658  THR A CB  
767  O OG1 . THR A 121 ? 0.9101 1.0683 1.1197 -0.1239 -0.0684 -0.0823 658  THR A OG1 
768  C CG2 . THR A 121 ? 0.3035 0.4453 0.4922 -0.1512 -0.0463 -0.0802 658  THR A CG2 
769  N N   . ASP A 122 ? 0.3573 0.5913 0.6357 -0.1454 -0.0511 -0.0998 659  ASP A N   
770  C CA  . ASP A 122 ? 0.4483 0.7148 0.7558 -0.1620 -0.0475 -0.1087 659  ASP A CA  
771  C C   . ASP A 122 ? 0.4502 0.6988 0.7373 -0.1852 -0.0382 -0.1067 659  ASP A C   
772  O O   . ASP A 122 ? 0.4828 0.7507 0.7844 -0.2008 -0.0252 -0.1117 659  ASP A O   
773  C CB  . ASP A 122 ? 0.5597 0.8472 0.8901 -0.1593 -0.0650 -0.1146 659  ASP A CB  
774  C CG  . ASP A 122 ? 0.6834 0.9988 1.0433 -0.1393 -0.0722 -0.1195 659  ASP A CG  
775  O OD1 . ASP A 122 ? 0.7100 1.0394 1.0825 -0.1323 -0.0608 -0.1214 659  ASP A OD1 
776  O OD2 . ASP A 122 ? 0.6647 0.9862 1.0334 -0.1303 -0.0897 -0.1215 659  ASP A OD2 
777  N N   . ALA A 123 ? 0.5176 0.7283 0.7699 -0.1876 -0.0446 -0.0995 660  ALA A N   
778  C CA  . ALA A 123 ? 0.5572 0.7435 0.7840 -0.2081 -0.0370 -0.0966 660  ALA A CA  
779  C C   . ALA A 123 ? 0.5475 0.7196 0.7569 -0.2117 -0.0196 -0.0923 660  ALA A C   
780  O O   . ALA A 123 ? 0.5046 0.6743 0.7082 -0.2313 -0.0082 -0.0935 660  ALA A O   
781  C CB  . ALA A 123 ? 0.5500 0.6972 0.7423 -0.2064 -0.0482 -0.0902 660  ALA A CB  
782  N N   . ASP A 124 ? 0.4378 0.5999 0.6380 -0.1935 -0.0179 -0.0875 661  ASP A N   
783  C CA  . ASP A 124 ? 0.3832 0.5348 0.5693 -0.1944 -0.0029 -0.0840 661  ASP A CA  
784  C C   . ASP A 124 ? 0.4933 0.6785 0.7070 -0.2056 0.0110  -0.0916 661  ASP A C   
785  O O   . ASP A 124 ? 0.4608 0.6364 0.6604 -0.2200 0.0248  -0.0905 661  ASP A O   
786  C CB  . ASP A 124 ? 0.3845 0.5289 0.5648 -0.1723 -0.0046 -0.0795 661  ASP A CB  
787  C CG  . ASP A 124 ? 0.4849 0.5942 0.6345 -0.1619 -0.0146 -0.0715 661  ASP A CG  
788  O OD1 . ASP A 124 ? 0.4599 0.5469 0.5891 -0.1713 -0.0193 -0.0690 661  ASP A OD1 
789  O OD2 . ASP A 124 ? 0.3765 0.4808 0.5223 -0.1445 -0.0174 -0.0682 661  ASP A OD2 
790  N N   . LYS A 125 ? 0.4271 0.6509 0.6791 -0.1980 0.0073  -0.0994 662  LYS A N   
791  C CA  . LYS A 125 ? 0.4376 0.6987 0.7210 -0.2053 0.0203  -0.1081 662  LYS A CA  
792  C C   . LYS A 125 ? 0.4706 0.7364 0.7545 -0.2261 0.0269  -0.1099 662  LYS A C   
793  O O   . LYS A 125 ? 0.5126 0.7863 0.7980 -0.2344 0.0423  -0.1113 662  LYS A O   
794  C CB  . LYS A 125 ? 0.4568 0.7563 0.7803 -0.1894 0.0119  -0.1158 662  LYS A CB  
795  C CG  . LYS A 125 ? 0.5109 0.8047 0.8314 -0.1662 0.0106  -0.1128 662  LYS A CG  
796  C CD  . LYS A 125 ? 0.4902 0.8158 0.8456 -0.1490 0.0000  -0.1196 662  LYS A CD  
797  C CE  . LYS A 125 ? 0.5715 0.8854 0.9185 -0.1272 -0.0010 -0.1157 662  LYS A CE  
798  N NZ  . LYS A 125 ? 0.6053 0.9434 0.9809 -0.1087 -0.0128 -0.1214 662  LYS A NZ  
799  N N   . LEU A 126 ? 0.5170 0.7751 0.7969 -0.2331 0.0149  -0.1091 663  LEU A N   
800  C CA  . LEU A 126 ? 0.5141 0.7693 0.7887 -0.2522 0.0196  -0.1091 663  LEU A CA  
801  C C   . LEU A 126 ? 0.6005 0.8200 0.8368 -0.2660 0.0327  -0.1027 663  LEU A C   
802  O O   . LEU A 126 ? 0.5953 0.8204 0.8311 -0.2783 0.0463  -0.1040 663  LEU A O   
803  C CB  . LEU A 126 ? 0.5555 0.8023 0.8274 -0.2562 0.0029  -0.1088 663  LEU A CB  
804  C CG  . LEU A 126 ? 0.5945 0.8786 0.9042 -0.2520 -0.0083 -0.1157 663  LEU A CG  
805  C CD1 . LEU A 126 ? 0.6630 0.9310 0.9626 -0.2536 -0.0265 -0.1143 663  LEU A CD1 
806  C CD2 . LEU A 126 ? 0.5477 0.8563 0.8763 -0.2660 0.0028  -0.1203 663  LEU A CD2 
807  N N   . ALA A 127 ? 0.5603 0.7420 0.7631 -0.2633 0.0281  -0.0958 664  ALA A N   
808  C CA  . ALA A 127 ? 0.5953 0.7371 0.7568 -0.2737 0.0374  -0.0886 664  ALA A CA  
809  C C   . ALA A 127 ? 0.6328 0.7790 0.7913 -0.2744 0.0546  -0.0884 664  ALA A C   
810  O O   . ALA A 127 ? 0.5768 0.7062 0.7137 -0.2875 0.0659  -0.0858 664  ALA A O   
811  C CB  . ALA A 127 ? 0.5783 0.6815 0.7074 -0.2665 0.0278  -0.0817 664  ALA A CB  
812  N N   . ILE A 128 ? 0.5478 0.7150 0.7262 -0.2600 0.0561  -0.0913 665  ILE A N   
813  C CA  . ILE A 128 ? 0.5813 0.7549 0.7590 -0.2590 0.0718  -0.0921 665  ILE A CA  
814  C C   . ILE A 128 ? 0.6535 0.8542 0.8506 -0.2692 0.0838  -0.0981 665  ILE A C   
815  O O   . ILE A 128 ? 0.6869 0.8752 0.8647 -0.2795 0.0978  -0.0965 665  ILE A O   
816  C CB  . ILE A 128 ? 0.5423 0.7360 0.7415 -0.2403 0.0699  -0.0953 665  ILE A CB  
817  C CG1 . ILE A 128 ? 0.5085 0.6652 0.6762 -0.2244 0.0600  -0.0856 665  ILE A CG1 
818  C CG2 . ILE A 128 ? 0.6591 0.8678 0.8655 -0.2389 0.0862  -0.0985 665  ILE A CG2 
819  C CD1 . ILE A 128 ? 0.4790 0.6473 0.6609 -0.2004 0.0541  -0.0858 665  ILE A CD1 
820  N N   . GLU A 129 ? 0.5405 0.7770 0.7746 -0.2665 0.0777  -0.1052 666  GLU A N   
821  C CA  . GLU A 129 ? 0.6626 0.9292 0.9197 -0.2751 0.0880  -0.1119 666  GLU A CA  
822  C C   . GLU A 129 ? 0.7281 0.9764 0.9641 -0.2964 0.0933  -0.1096 666  GLU A C   
823  O O   . GLU A 129 ? 0.7544 1.0117 0.9912 -0.3076 0.1076  -0.1126 666  GLU A O   
824  C CB  . GLU A 129 ? 0.7058 1.0136 1.0067 -0.2655 0.0777  -0.1196 666  GLU A CB  
825  C CG  . GLU A 129 ? 0.7837 1.1287 1.1144 -0.2696 0.0887  -0.1279 666  GLU A CG  
826  C CD  . GLU A 129 ? 0.8268 1.2111 1.1986 -0.2511 0.0812  -0.1353 666  GLU A CD  
827  O OE1 . GLU A 129 ? 0.7777 1.1940 1.1794 -0.2539 0.0796  -0.1419 666  GLU A OE1 
828  O OE2 . GLU A 129 ? 0.8336 1.2159 1.2071 -0.2336 0.0765  -0.1344 666  GLU A OE2 
829  N N   . LYS A 130 ? 0.6754 0.8969 0.8912 -0.3020 0.0819  -0.1044 667  LYS A N   
830  C CA  . LYS A 130 ? 0.7066 0.9041 0.8971 -0.3214 0.0855  -0.1014 667  LYS A CA  
831  C C   . LYS A 130 ? 0.7937 0.9601 0.9465 -0.3297 0.1003  -0.0962 667  LYS A C   
832  O O   . LYS A 130 ? 0.7924 0.9534 0.9336 -0.3459 0.1110  -0.0969 667  LYS A O   
833  C CB  . LYS A 130 ? 0.5974 0.7657 0.7679 -0.3226 0.0699  -0.0964 667  LYS A CB  
834  C CG  . LYS A 130 ? 0.6389 0.7773 0.7792 -0.3415 0.0727  -0.0928 667  LYS A CG  
835  C CD  . LYS A 130 ? 0.5837 0.6934 0.7048 -0.3411 0.0568  -0.0887 667  LYS A CD  
836  C CE  . LYS A 130 ? 0.7204 0.7986 0.8098 -0.3593 0.0600  -0.0854 667  LYS A CE  
837  N NZ  . LYS A 130 ? 0.7164 0.7803 0.7999 -0.3616 0.0448  -0.0848 667  LYS A NZ  
838  N N   . GLY A 131 ? 0.7238 0.8695 0.8571 -0.3184 0.1005  -0.0911 668  GLY A N   
839  C CA  . GLY A 131 ? 0.8003 0.9159 0.8974 -0.3233 0.1128  -0.0860 668  GLY A CA  
840  C C   . GLY A 131 ? 0.8435 0.9079 0.8932 -0.3296 0.1080  -0.0768 668  GLY A C   
841  O O   . GLY A 131 ? 0.8197 0.8716 0.8618 -0.3375 0.1001  -0.0756 668  GLY A O   
842  N N   . GLU A 132 ? 0.7923 0.8263 0.8096 -0.3253 0.1123  -0.0707 669  GLU A N   
843  C CA  . GLU A 132 ? 0.9044 0.8871 0.8729 -0.3294 0.1088  -0.0617 669  GLU A CA  
844  C C   . GLU A 132 ? 0.9284 0.8917 0.8888 -0.3226 0.0920  -0.0578 669  GLU A C   
845  O O   . GLU A 132 ? 0.9067 0.8324 0.8328 -0.3283 0.0873  -0.0523 669  GLU A O   
846  C CB  . GLU A 132 ? 0.9556 0.9225 0.9021 -0.3484 0.1173  -0.0615 669  GLU A CB  
847  C CG  . GLU A 132 ? 0.9024 0.8571 0.8258 -0.3548 0.1324  -0.0604 669  GLU A CG  
848  C CD  . GLU A 132 ? 1.0495 0.9831 0.9459 -0.3739 0.1397  -0.0597 669  GLU A CD  
849  O OE1 . GLU A 132 ? 1.0742 1.0326 0.9939 -0.3857 0.1426  -0.0657 669  GLU A OE1 
850  O OE2 . GLU A 132 ? 1.1333 1.0250 0.9848 -0.3771 0.1419  -0.0533 669  GLU A OE2 
851  N N   . GLN A 133 ? 0.7716 0.7596 0.7625 -0.3100 0.0828  -0.0610 670  GLN A N   
852  C CA  . GLN A 133 ? 0.7380 0.7081 0.7210 -0.3015 0.0669  -0.0578 670  GLN A CA  
853  C C   . GLN A 133 ? 0.7378 0.6899 0.7058 -0.2866 0.0633  -0.0529 670  GLN A C   
854  O O   . GLN A 133 ? 0.7861 0.7574 0.7690 -0.2802 0.0703  -0.0549 670  GLN A O   
855  C CB  . GLN A 133 ? 0.6765 0.6837 0.7007 -0.2973 0.0574  -0.0648 670  GLN A CB  
856  C CG  . GLN A 133 ? 0.6891 0.7227 0.7364 -0.3109 0.0609  -0.0709 670  GLN A CG  
857  C CD  . GLN A 133 ? 0.8178 0.8199 0.8358 -0.3247 0.0587  -0.0675 670  GLN A CD  
858  O OE1 . GLN A 133 ? 0.8658 0.8694 0.8793 -0.3396 0.0688  -0.0689 670  GLN A OE1 
859  N NE2 . GLN A 133 ? 0.7521 0.7246 0.7488 -0.3196 0.0456  -0.0632 670  GLN A NE2 
860  N N   . PRO A 134 ? 0.7378 0.6527 0.6761 -0.2805 0.0523  -0.0467 671  PRO A N   
861  C CA  . PRO A 134 ? 0.7883 0.6899 0.7156 -0.2598 0.0465  -0.0418 671  PRO A CA  
862  C C   . PRO A 134 ? 0.7372 0.6759 0.7023 -0.2422 0.0401  -0.0460 671  PRO A C   
863  O O   . PRO A 134 ? 0.7544 0.7180 0.7465 -0.2459 0.0352  -0.0517 671  PRO A O   
864  C CB  . PRO A 134 ? 0.7336 0.5939 0.6272 -0.2548 0.0347  -0.0358 671  PRO A CB  
865  C CG  . PRO A 134 ? 0.8049 0.6671 0.7045 -0.2708 0.0307  -0.0398 671  PRO A CG  
866  C CD  . PRO A 134 ? 0.7924 0.6799 0.7090 -0.2858 0.0435  -0.0441 671  PRO A CD  
867  N N   . ILE A 135 ? 0.7643 0.7059 0.7305 -0.2240 0.0398  -0.0435 672  ILE A N   
868  C CA  . ILE A 135 ? 0.5864 0.5565 0.5828 -0.2061 0.0329  -0.0465 672  ILE A CA  
869  C C   . ILE A 135 ? 0.5650 0.5243 0.5578 -0.1974 0.0180  -0.0448 672  ILE A C   
870  O O   . ILE A 135 ? 0.5699 0.4966 0.5336 -0.2014 0.0134  -0.0406 672  ILE A O   
871  C CB  . ILE A 135 ? 0.5595 0.5280 0.5516 -0.1894 0.0349  -0.0432 672  ILE A CB  
872  C CG1 . ILE A 135 ? 0.6450 0.5758 0.6019 -0.1800 0.0283  -0.0354 672  ILE A CG1 
873  C CG2 . ILE A 135 ? 0.6347 0.6116 0.6275 -0.1979 0.0497  -0.0451 672  ILE A CG2 
874  C CD1 . ILE A 135 ? 0.6929 0.6217 0.6447 -0.1648 0.0295  -0.0323 672  ILE A CD1 
875  N N   . SER A 136 ? 0.4639 0.4484 0.4839 -0.1854 0.0104  -0.0483 673  SER A N   
876  C CA  . SER A 136 ? 0.4519 0.4271 0.4683 -0.1781 -0.0033 -0.0473 673  SER A CA  
877  C C   . SER A 136 ? 0.4485 0.3911 0.4346 -0.1647 -0.0084 -0.0402 673  SER A C   
878  O O   . SER A 136 ? 0.4854 0.4229 0.4637 -0.1556 -0.0039 -0.0369 673  SER A O   
879  C CB  . SER A 136 ? 0.3943 0.4005 0.4429 -0.1665 -0.0105 -0.0518 673  SER A CB  
880  O OG  . SER A 136 ? 0.3814 0.3881 0.4300 -0.1482 -0.0114 -0.0488 673  SER A OG  
881  N N   . ALA A 137 ? 0.4625 0.3837 0.4319 -0.1636 -0.0179 -0.0385 674  ALA A N   
882  C CA  . ALA A 137 ? 0.4362 0.3291 0.3794 -0.1497 -0.0233 -0.0329 674  ALA A CA  
883  C C   . ALA A 137 ? 0.4334 0.3410 0.3897 -0.1308 -0.0256 -0.0320 674  ALA A C   
884  O O   . ALA A 137 ? 0.4324 0.3260 0.3735 -0.1203 -0.0244 -0.0277 674  ALA A O   
885  C CB  . ALA A 137 ? 0.5203 0.3924 0.4478 -0.1509 -0.0332 -0.0327 674  ALA A CB  
886  N N   . ASP A 138 ? 0.3850 0.3203 0.3691 -0.1267 -0.0292 -0.0361 675  ASP A N   
887  C CA  . ASP A 138 ? 0.3343 0.2821 0.3300 -0.1101 -0.0315 -0.0353 675  ASP A CA  
888  C C   . ASP A 138 ? 0.3457 0.3033 0.3473 -0.1072 -0.0221 -0.0345 675  ASP A C   
889  O O   . ASP A 138 ? 0.3475 0.3012 0.3439 -0.0949 -0.0221 -0.0316 675  ASP A O   
890  C CB  . ASP A 138 ? 0.3966 0.3696 0.4189 -0.1068 -0.0381 -0.0400 675  ASP A CB  
891  C CG  . ASP A 138 ? 0.6136 0.5745 0.6268 -0.1026 -0.0496 -0.0396 675  ASP A CG  
892  O OD1 . ASP A 138 ? 0.5980 0.5317 0.5850 -0.1001 -0.0518 -0.0359 675  ASP A OD1 
893  O OD2 . ASP A 138 ? 0.5108 0.4889 0.5423 -0.1012 -0.0567 -0.0434 675  ASP A OD2 
894  N N   . LEU A 139 ? 0.3329 0.3037 0.3451 -0.1193 -0.0136 -0.0376 676  LEU A N   
895  C CA  . LEU A 139 ? 0.3180 0.2981 0.3352 -0.1172 -0.0042 -0.0375 676  LEU A CA  
896  C C   . LEU A 139 ? 0.3619 0.3143 0.3492 -0.1166 -0.0007 -0.0319 676  LEU A C   
897  O O   . LEU A 139 ? 0.3519 0.3039 0.3360 -0.1075 0.0019  -0.0298 676  LEU A O   
898  C CB  . LEU A 139 ? 0.3283 0.3305 0.3646 -0.1306 0.0052  -0.0430 676  LEU A CB  
899  C CG  . LEU A 139 ? 0.3385 0.3511 0.3802 -0.1287 0.0157  -0.0439 676  LEU A CG  
900  C CD1 . LEU A 139 ? 0.4025 0.4278 0.4579 -0.1117 0.0122  -0.0443 676  LEU A CD1 
901  C CD2 . LEU A 139 ? 0.3762 0.4124 0.4377 -0.1423 0.0261  -0.0503 676  LEU A CD2 
902  N N   . LYS A 140 ? 0.4155 0.3438 0.3801 -0.1261 -0.0016 -0.0295 677  LYS A N   
903  C CA  . LYS A 140 ? 0.4239 0.3225 0.3574 -0.1243 -0.0004 -0.0240 677  LYS A CA  
904  C C   . LYS A 140 ? 0.4155 0.3055 0.3413 -0.1062 -0.0076 -0.0207 677  LYS A C   
905  O O   . LYS A 140 ? 0.4336 0.3176 0.3500 -0.0989 -0.0055 -0.0179 677  LYS A O   
906  C CB  . LYS A 140 ? 0.4598 0.3307 0.3686 -0.1362 -0.0020 -0.0222 677  LYS A CB  
907  C CG  . LYS A 140 ? 0.5426 0.3806 0.4172 -0.1354 -0.0007 -0.0167 677  LYS A CG  
908  C CD  . LYS A 140 ? 0.7839 0.5905 0.6312 -0.1471 -0.0027 -0.0148 677  LYS A CD  
909  C CE  . LYS A 140 ? 0.8606 0.6320 0.6720 -0.1434 -0.0031 -0.0091 677  LYS A CE  
910  N NZ  . LYS A 140 ? 0.9322 0.6684 0.7132 -0.1547 -0.0050 -0.0070 677  LYS A NZ  
911  N N   . ARG A 141 ? 0.3902 0.2806 0.3204 -0.0996 -0.0159 -0.0213 678  ARG A N   
912  C CA  . ARG A 141 ? 0.4290 0.3135 0.3536 -0.0835 -0.0217 -0.0188 678  ARG A CA  
913  C C   . ARG A 141 ? 0.3755 0.2804 0.3172 -0.0742 -0.0189 -0.0194 678  ARG A C   
914  O O   . ARG A 141 ? 0.3874 0.2863 0.3206 -0.0644 -0.0194 -0.0167 678  ARG A O   
915  C CB  . ARG A 141 ? 0.4160 0.2998 0.3437 -0.0792 -0.0300 -0.0201 678  ARG A CB  
916  C CG  . ARG A 141 ? 0.5033 0.3602 0.4079 -0.0835 -0.0347 -0.0190 678  ARG A CG  
917  C CD  . ARG A 141 ? 0.5783 0.4328 0.4827 -0.0749 -0.0428 -0.0199 678  ARG A CD  
918  N NE  . ARG A 141 ? 0.6107 0.4629 0.5104 -0.0593 -0.0441 -0.0177 678  ARG A NE  
919  C CZ  . ARG A 141 ? 0.6205 0.4781 0.5252 -0.0501 -0.0486 -0.0185 678  ARG A CZ  
920  N NH1 . ARG A 141 ? 0.4675 0.3322 0.3814 -0.0538 -0.0535 -0.0212 678  ARG A NH1 
921  N NH2 . ARG A 141 ? 0.6203 0.4766 0.5208 -0.0376 -0.0483 -0.0168 678  ARG A NH2 
922  N N   . PHE A 142 ? 0.3451 0.2743 0.3112 -0.0771 -0.0166 -0.0232 679  PHE A N   
923  C CA  . PHE A 142 ? 0.3061 0.2534 0.2882 -0.0688 -0.0142 -0.0242 679  PHE A CA  
924  C C   . PHE A 142 ? 0.3377 0.2811 0.3111 -0.0696 -0.0070 -0.0226 679  PHE A C   
925  O O   . PHE A 142 ? 0.3584 0.3014 0.3292 -0.0603 -0.0073 -0.0209 679  PHE A O   
926  C CB  . PHE A 142 ? 0.2952 0.2676 0.3039 -0.0720 -0.0131 -0.0292 679  PHE A CB  
927  C CG  . PHE A 142 ? 0.3189 0.3076 0.3428 -0.0642 -0.0100 -0.0308 679  PHE A CG  
928  C CD1 . PHE A 142 ? 0.3465 0.3357 0.3722 -0.0523 -0.0151 -0.0294 679  PHE A CD1 
929  C CD2 . PHE A 142 ? 0.3406 0.3432 0.3758 -0.0693 -0.0016 -0.0340 679  PHE A CD2 
930  C CE1 . PHE A 142 ? 0.3833 0.3846 0.4207 -0.0458 -0.0125 -0.0308 679  PHE A CE1 
931  C CE2 . PHE A 142 ? 0.3203 0.3358 0.3679 -0.0617 0.0010  -0.0358 679  PHE A CE2 
932  C CZ  . PHE A 142 ? 0.2970 0.3109 0.3452 -0.0501 -0.0048 -0.0341 679  PHE A CZ  
933  N N   . ARG A 143 ? 0.3456 0.2847 0.3127 -0.0814 -0.0006 -0.0231 680  ARG A N   
934  C CA  . ARG A 143 ? 0.3459 0.2796 0.3022 -0.0830 0.0061  -0.0217 680  ARG A CA  
935  C C   . ARG A 143 ? 0.3825 0.2931 0.3140 -0.0757 0.0018  -0.0167 680  ARG A C   
936  O O   . ARG A 143 ? 0.4084 0.3188 0.3358 -0.0696 0.0030  -0.0154 680  ARG A O   
937  C CB  . ARG A 143 ? 0.3981 0.3293 0.3493 -0.0984 0.0144  -0.0231 680  ARG A CB  
938  C CG  . ARG A 143 ? 0.3668 0.3255 0.3451 -0.1050 0.0207  -0.0291 680  ARG A CG  
939  C CD  . ARG A 143 ? 0.3809 0.3372 0.3530 -0.1216 0.0305  -0.0308 680  ARG A CD  
940  N NE  . ARG A 143 ? 0.4271 0.4130 0.4273 -0.1271 0.0378  -0.0374 680  ARG A NE  
941  C CZ  . ARG A 143 ? 0.4954 0.4881 0.4993 -0.1428 0.0469  -0.0409 680  ARG A CZ  
942  N NH1 . ARG A 143 ? 0.4994 0.4685 0.4778 -0.1555 0.0499  -0.0376 680  ARG A NH1 
943  N NH2 . ARG A 143 ? 0.4668 0.4898 0.4995 -0.1459 0.0532  -0.0478 680  ARG A NH2 
944  N N   . LYS A 144 ? 0.4007 0.2924 0.3166 -0.0757 -0.0039 -0.0144 681  LYS A N   
945  C CA  . LYS A 144 ? 0.4307 0.2993 0.3225 -0.0685 -0.0085 -0.0102 681  LYS A CA  
946  C C   . LYS A 144 ? 0.4263 0.3000 0.3235 -0.0535 -0.0145 -0.0096 681  LYS A C   
947  O O   . LYS A 144 ? 0.4466 0.3151 0.3350 -0.0453 -0.0162 -0.0077 681  LYS A O   
948  C CB  . LYS A 144 ? 0.4838 0.3274 0.3546 -0.0744 -0.0118 -0.0085 681  LYS A CB  
949  C CG  . LYS A 144 ? 0.7066 0.5234 0.5503 -0.0665 -0.0170 -0.0045 681  LYS A CG  
950  C CD  . LYS A 144 ? 0.9278 0.7163 0.7475 -0.0754 -0.0186 -0.0029 681  LYS A CD  
951  C CE  . LYS A 144 ? 1.0608 0.8193 0.8509 -0.0669 -0.0242 0.0010  681  LYS A CE  
952  N NZ  . LYS A 144 ? 1.1456 0.9010 0.9354 -0.0519 -0.0319 0.0008  681  LYS A NZ  
953  N N   . GLU A 145 ? 0.3960 0.2799 0.3069 -0.0504 -0.0179 -0.0115 682  GLU A N   
954  C CA  . GLU A 145 ? 0.3571 0.2430 0.2699 -0.0377 -0.0229 -0.0109 682  GLU A CA  
955  C C   . GLU A 145 ? 0.4152 0.3228 0.3479 -0.0324 -0.0211 -0.0125 682  GLU A C   
956  O O   . GLU A 145 ? 0.4166 0.3270 0.3504 -0.0228 -0.0236 -0.0119 682  GLU A O   
957  C CB  . GLU A 145 ? 0.3820 0.2611 0.2926 -0.0366 -0.0282 -0.0116 682  GLU A CB  
958  C CG  . GLU A 145 ? 0.4431 0.2969 0.3310 -0.0409 -0.0308 -0.0101 682  GLU A CG  
959  C CD  . GLU A 145 ? 0.5980 0.4443 0.4828 -0.0408 -0.0361 -0.0114 682  GLU A CD  
960  O OE1 . GLU A 145 ? 0.5630 0.4176 0.4557 -0.0324 -0.0389 -0.0124 682  GLU A OE1 
961  O OE2 . GLU A 145 ? 0.6620 0.4931 0.5352 -0.0501 -0.0372 -0.0116 682  GLU A OE2 
962  N N   . TYR A 146 ? 0.3281 0.2510 0.2762 -0.0385 -0.0165 -0.0148 683  TYR A N   
963  C CA  . TYR A 146 ? 0.3031 0.2437 0.2682 -0.0333 -0.0151 -0.0165 683  TYR A CA  
964  C C   . TYR A 146 ? 0.3469 0.2942 0.3149 -0.0358 -0.0090 -0.0172 683  TYR A C   
965  O O   . TYR A 146 ? 0.3676 0.3164 0.3338 -0.0301 -0.0088 -0.0164 683  TYR A O   
966  C CB  . TYR A 146 ? 0.2796 0.2337 0.2625 -0.0351 -0.0164 -0.0194 683  TYR A CB  
967  C CG  . TYR A 146 ? 0.2978 0.2647 0.2939 -0.0278 -0.0168 -0.0205 683  TYR A CG  
968  C CD1 . TYR A 146 ? 0.3293 0.2934 0.3233 -0.0202 -0.0216 -0.0192 683  TYR A CD1 
969  C CD2 . TYR A 146 ? 0.2981 0.2779 0.3067 -0.0288 -0.0119 -0.0229 683  TYR A CD2 
970  C CE1 . TYR A 146 ? 0.3118 0.2843 0.3147 -0.0147 -0.0217 -0.0198 683  TYR A CE1 
971  C CE2 . TYR A 146 ? 0.3119 0.2997 0.3299 -0.0222 -0.0126 -0.0238 683  TYR A CE2 
972  C CZ  . TYR A 146 ? 0.3233 0.3066 0.3377 -0.0157 -0.0176 -0.0220 683  TYR A CZ  
973  O OH  . TYR A 146 ? 0.2984 0.2866 0.3191 -0.0104 -0.0181 -0.0225 683  TYR A OH  
974  N N   . VAL A 147 ? 0.3506 0.3023 0.3229 -0.0450 -0.0037 -0.0193 684  VAL A N   
975  C CA  . VAL A 147 ? 0.3725 0.3312 0.3479 -0.0477 0.0031  -0.0209 684  VAL A CA  
976  C C   . VAL A 147 ? 0.3762 0.3209 0.3321 -0.0463 0.0034  -0.0179 684  VAL A C   
977  O O   . VAL A 147 ? 0.3693 0.3188 0.3268 -0.0418 0.0044  -0.0182 684  VAL A O   
978  C CB  . VAL A 147 ? 0.3112 0.2765 0.2930 -0.0589 0.0099  -0.0240 684  VAL A CB  
979  C CG1 . VAL A 147 ? 0.3577 0.3282 0.3396 -0.0617 0.0180  -0.0259 684  VAL A CG1 
980  C CG2 . VAL A 147 ? 0.2968 0.2796 0.3011 -0.0591 0.0087  -0.0278 684  VAL A CG2 
981  N N   . GLN A 148 ? 0.3641 0.2906 0.3007 -0.0501 0.0020  -0.0151 685  GLN A N   
982  C CA  . GLN A 148 ? 0.4061 0.3183 0.3229 -0.0483 0.0013  -0.0123 685  GLN A CA  
983  C C   . GLN A 148 ? 0.3607 0.2737 0.2767 -0.0364 -0.0051 -0.0109 685  GLN A C   
984  O O   . GLN A 148 ? 0.4014 0.3167 0.3148 -0.0336 -0.0047 -0.0109 685  GLN A O   
985  C CB  . GLN A 148 ? 0.5427 0.4314 0.4359 -0.0541 0.0001  -0.0094 685  GLN A CB  
986  C CG  . GLN A 148 ? 0.5569 0.4287 0.4275 -0.0514 -0.0020 -0.0063 685  GLN A CG  
987  C CD  . GLN A 148 ? 0.7178 0.5642 0.5625 -0.0599 -0.0010 -0.0035 685  GLN A CD  
988  O OE1 . GLN A 148 ? 0.8106 0.6553 0.6513 -0.0719 0.0069  -0.0045 685  GLN A OE1 
989  N NE2 . GLN A 148 ? 0.7026 0.5285 0.5287 -0.0539 -0.0085 -0.0004 685  GLN A NE2 
990  N N   . PRO A 149 ? 0.3964 0.3084 0.3150 -0.0297 -0.0107 -0.0102 686  PRO A N   
991  C CA  . PRO A 149 ? 0.4132 0.3296 0.3338 -0.0192 -0.0152 -0.0096 686  PRO A CA  
992  C C   . PRO A 149 ? 0.4280 0.3625 0.3651 -0.0174 -0.0126 -0.0119 686  PRO A C   
993  O O   . PRO A 149 ? 0.3951 0.3323 0.3303 -0.0129 -0.0142 -0.0117 686  PRO A O   
994  C CB  . PRO A 149 ? 0.3631 0.2774 0.2857 -0.0141 -0.0195 -0.0094 686  PRO A CB  
995  C CG  . PRO A 149 ? 0.4753 0.3750 0.3871 -0.0208 -0.0196 -0.0085 686  PRO A CG  
996  C CD  . PRO A 149 ? 0.4108 0.3162 0.3283 -0.0315 -0.0133 -0.0099 686  PRO A CD  
997  N N   . VAL A 150 ? 0.3255 0.2714 0.2780 -0.0203 -0.0095 -0.0141 687  VAL A N   
998  C CA  . VAL A 150 ? 0.3001 0.2596 0.2660 -0.0182 -0.0073 -0.0161 687  VAL A CA  
999  C C   . VAL A 150 ? 0.3713 0.3315 0.3332 -0.0217 -0.0032 -0.0172 687  VAL A C   
1000 O O   . VAL A 150 ? 0.3409 0.3054 0.3039 -0.0186 -0.0037 -0.0177 687  VAL A O   
1001 C CB  . VAL A 150 ? 0.2865 0.2559 0.2681 -0.0198 -0.0055 -0.0185 687  VAL A CB  
1002 C CG1 . VAL A 150 ? 0.2963 0.2758 0.2884 -0.0181 -0.0028 -0.0208 687  VAL A CG1 
1003 C CG2 . VAL A 150 ? 0.2959 0.2640 0.2798 -0.0156 -0.0103 -0.0175 687  VAL A CG2 
1004 N N   . GLN A 151 ? 0.3552 0.3105 0.3113 -0.0289 0.0012  -0.0177 688  GLN A N   
1005 C CA  . GLN A 151 ? 0.3647 0.3192 0.3150 -0.0329 0.0060  -0.0190 688  GLN A CA  
1006 C C   . GLN A 151 ? 0.3768 0.3215 0.3107 -0.0297 0.0016  -0.0167 688  GLN A C   
1007 O O   . GLN A 151 ? 0.3565 0.3041 0.2891 -0.0292 0.0026  -0.0180 688  GLN A O   
1008 C CB  . GLN A 151 ? 0.3506 0.3014 0.2966 -0.0423 0.0126  -0.0201 688  GLN A CB  
1009 C CG  . GLN A 151 ? 0.3070 0.2735 0.2733 -0.0447 0.0178  -0.0243 688  GLN A CG  
1010 C CD  . GLN A 151 ? 0.3841 0.3514 0.3501 -0.0547 0.0254  -0.0264 688  GLN A CD  
1011 O OE1 . GLN A 151 ? 0.3561 0.3096 0.3050 -0.0610 0.0265  -0.0240 688  GLN A OE1 
1012 N NE2 . GLN A 151 ? 0.3913 0.3748 0.3762 -0.0561 0.0307  -0.0312 688  GLN A NE2 
1013 N N   . LEU A 152 ? 0.3713 0.3040 0.2927 -0.0269 -0.0038 -0.0135 689  LEU A N   
1014 C CA  . LEU A 152 ? 0.3979 0.3224 0.3051 -0.0218 -0.0097 -0.0116 689  LEU A CA  
1015 C C   . LEU A 152 ? 0.3787 0.3163 0.2977 -0.0143 -0.0138 -0.0128 689  LEU A C   
1016 O O   . LEU A 152 ? 0.3925 0.3314 0.3069 -0.0121 -0.0167 -0.0132 689  LEU A O   
1017 C CB  . LEU A 152 ? 0.4412 0.3489 0.3325 -0.0190 -0.0150 -0.0084 689  LEU A CB  
1018 C CG  . LEU A 152 ? 0.5067 0.3963 0.3800 -0.0276 -0.0118 -0.0066 689  LEU A CG  
1019 C CD1 . LEU A 152 ? 0.5433 0.4138 0.3998 -0.0237 -0.0180 -0.0035 689  LEU A CD1 
1020 C CD2 . LEU A 152 ? 0.5876 0.4698 0.4462 -0.0320 -0.0095 -0.0064 689  LEU A CD2 
1021 N N   . ARG A 153 ? 0.3373 0.2843 0.2706 -0.0110 -0.0141 -0.0134 690  ARG A N   
1022 C CA  . ARG A 153 ? 0.3526 0.3122 0.2969 -0.0057 -0.0164 -0.0147 690  ARG A CA  
1023 C C   . ARG A 153 ? 0.3348 0.3032 0.2866 -0.0093 -0.0126 -0.0172 690  ARG A C   
1024 O O   . ARG A 153 ? 0.3128 0.2883 0.2675 -0.0072 -0.0149 -0.0183 690  ARG A O   
1025 C CB  . ARG A 153 ? 0.3791 0.3444 0.3342 -0.0026 -0.0165 -0.0147 690  ARG A CB  
1026 C CG  . ARG A 153 ? 0.5637 0.5193 0.5107 0.0013  -0.0202 -0.0128 690  ARG A CG  
1027 C CD  . ARG A 153 ? 0.5523 0.5129 0.5020 0.0093  -0.0239 -0.0130 690  ARG A CD  
1028 N NE  . ARG A 153 ? 0.6629 0.6135 0.6060 0.0125  -0.0261 -0.0118 690  ARG A NE  
1029 C CZ  . ARG A 153 ? 0.5972 0.5339 0.5258 0.0160  -0.0301 -0.0104 690  ARG A CZ  
1030 N NH1 . ARG A 153 ? 0.7098 0.6416 0.6290 0.0170  -0.0328 -0.0097 690  ARG A NH1 
1031 N NH2 . ARG A 153 ? 0.6559 0.5819 0.5777 0.0185  -0.0319 -0.0097 690  ARG A NH2 
1032 N N   . ILE A 154 ? 0.3215 0.2899 0.2767 -0.0148 -0.0068 -0.0186 691  ILE A N   
1033 C CA  . ILE A 154 ? 0.3271 0.3009 0.2869 -0.0177 -0.0030 -0.0215 691  ILE A CA  
1034 C C   . ILE A 154 ? 0.3364 0.3046 0.2829 -0.0197 -0.0041 -0.0218 691  ILE A C   
1035 O O   . ILE A 154 ? 0.3156 0.2884 0.2634 -0.0195 -0.0053 -0.0236 691  ILE A O   
1036 C CB  . ILE A 154 ? 0.3218 0.2973 0.2884 -0.0220 0.0037  -0.0237 691  ILE A CB  
1037 C CG1 . ILE A 154 ? 0.3141 0.2958 0.2943 -0.0192 0.0031  -0.0239 691  ILE A CG1 
1038 C CG2 . ILE A 154 ? 0.2790 0.2569 0.2467 -0.0246 0.0081  -0.0272 691  ILE A CG2 
1039 C CD1 . ILE A 154 ? 0.3023 0.2874 0.2909 -0.0224 0.0079  -0.0261 691  ILE A CD1 
1040 N N   . LEU A 155 ? 0.3469 0.3038 0.2789 -0.0221 -0.0041 -0.0200 692  LEU A N   
1041 C CA  . LEU A 155 ? 0.3608 0.3094 0.2765 -0.0237 -0.0061 -0.0199 692  LEU A CA  
1042 C C   . LEU A 155 ? 0.3482 0.3002 0.2624 -0.0174 -0.0150 -0.0191 692  LEU A C   
1043 O O   . LEU A 155 ? 0.4136 0.3664 0.3225 -0.0180 -0.0176 -0.0206 692  LEU A O   
1044 C CB  . LEU A 155 ? 0.3808 0.3133 0.2779 -0.0278 -0.0047 -0.0176 692  LEU A CB  
1045 C CG  . LEU A 155 ? 0.4215 0.3535 0.3211 -0.0356 0.0052  -0.0194 692  LEU A CG  
1046 C CD1 . LEU A 155 ? 0.4756 0.3904 0.3544 -0.0418 0.0077  -0.0170 692  LEU A CD1 
1047 C CD2 . LEU A 155 ? 0.4537 0.3930 0.3590 -0.0387 0.0115  -0.0236 692  LEU A CD2 
1048 N N   . ASN A 156 ? 0.3550 0.3100 0.2746 -0.0113 -0.0195 -0.0174 693  ASN A N   
1049 C CA  . ASN A 156 ? 0.3700 0.3327 0.2928 -0.0046 -0.0270 -0.0176 693  ASN A CA  
1050 C C   . ASN A 156 ? 0.4311 0.4092 0.3684 -0.0060 -0.0258 -0.0207 693  ASN A C   
1051 O O   . ASN A 156 ? 0.3847 0.3689 0.3216 -0.0049 -0.0308 -0.0223 693  ASN A O   
1052 C CB  . ASN A 156 ? 0.3368 0.3009 0.2641 0.0023  -0.0303 -0.0160 693  ASN A CB  
1053 C CG  . ASN A 156 ? 0.4362 0.4121 0.3702 0.0098  -0.0370 -0.0173 693  ASN A CG  
1054 O OD1 . ASN A 156 ? 0.4720 0.4453 0.3970 0.0135  -0.0438 -0.0173 693  ASN A OD1 
1055 N ND2 . ASN A 156 ? 0.4558 0.4452 0.4054 0.0119  -0.0352 -0.0186 693  ASN A ND2 
1056 N N   . VAL A 157 ? 0.3421 0.3257 0.2915 -0.0087 -0.0199 -0.0217 694  VAL A N   
1057 C CA  . VAL A 157 ? 0.2858 0.2800 0.2460 -0.0110 -0.0183 -0.0244 694  VAL A CA  
1058 C C   . VAL A 157 ? 0.3481 0.3393 0.3012 -0.0161 -0.0174 -0.0268 694  VAL A C   
1059 O O   . VAL A 157 ? 0.3282 0.3264 0.2836 -0.0173 -0.0206 -0.0289 694  VAL A O   
1060 C CB  . VAL A 157 ? 0.2856 0.2818 0.2564 -0.0125 -0.0127 -0.0247 694  VAL A CB  
1061 C CG1 . VAL A 157 ? 0.2804 0.2820 0.2577 -0.0160 -0.0105 -0.0274 694  VAL A CG1 
1062 C CG2 . VAL A 157 ? 0.3242 0.3237 0.3011 -0.0077 -0.0141 -0.0228 694  VAL A CG2 
1063 N N   . PHE A 158 ? 0.3233 0.3043 0.2673 -0.0196 -0.0129 -0.0269 695  PHE A N   
1064 C CA  . PHE A 158 ? 0.3780 0.3536 0.3118 -0.0244 -0.0114 -0.0294 695  PHE A CA  
1065 C C   . PHE A 158 ? 0.3603 0.3349 0.2834 -0.0231 -0.0196 -0.0293 695  PHE A C   
1066 O O   . PHE A 158 ? 0.3509 0.3283 0.2725 -0.0259 -0.0218 -0.0320 695  PHE A O   
1067 C CB  . PHE A 158 ? 0.3721 0.3368 0.2957 -0.0280 -0.0050 -0.0294 695  PHE A CB  
1068 C CG  . PHE A 158 ? 0.3734 0.3410 0.3082 -0.0298 0.0032  -0.0314 695  PHE A CG  
1069 C CD1 . PHE A 158 ? 0.3448 0.3193 0.2920 -0.0290 0.0045  -0.0337 695  PHE A CD1 
1070 C CD2 . PHE A 158 ? 0.4501 0.4130 0.3821 -0.0324 0.0093  -0.0313 695  PHE A CD2 
1071 C CE1 . PHE A 158 ? 0.4392 0.4155 0.3960 -0.0290 0.0108  -0.0358 695  PHE A CE1 
1072 C CE2 . PHE A 158 ? 0.4044 0.3725 0.3488 -0.0331 0.0160  -0.0339 695  PHE A CE2 
1073 C CZ  . PHE A 158 ? 0.3798 0.3544 0.3365 -0.0305 0.0162  -0.0361 695  PHE A CZ  
1074 N N   . ARG A 159 ? 0.3626 0.3321 0.2776 -0.0187 -0.0249 -0.0262 696  ARG A N   
1075 C CA  . ARG A 159 ? 0.3504 0.3179 0.2545 -0.0155 -0.0343 -0.0258 696  ARG A CA  
1076 C C   . ARG A 159 ? 0.3822 0.3673 0.3005 -0.0128 -0.0404 -0.0282 696  ARG A C   
1077 O O   . ARG A 159 ? 0.3939 0.3815 0.3074 -0.0143 -0.0462 -0.0304 696  ARG A O   
1078 C CB  . ARG A 159 ? 0.5167 0.4744 0.4107 -0.0095 -0.0389 -0.0219 696  ARG A CB  
1079 C CG  . ARG A 159 ? 0.7325 0.6785 0.6062 -0.0066 -0.0478 -0.0207 696  ARG A CG  
1080 C CD  . ARG A 159 ? 0.8264 0.7575 0.6869 -0.0012 -0.0513 -0.0165 696  ARG A CD  
1081 N NE  . ARG A 159 ? 1.0149 0.9570 0.8914 0.0062  -0.0534 -0.0162 696  ARG A NE  
1082 C CZ  . ARG A 159 ? 1.1467 1.0782 1.0145 0.0132  -0.0581 -0.0134 696  ARG A CZ  
1083 N NH1 . ARG A 159 ? 1.1138 1.0555 0.9959 0.0200  -0.0591 -0.0137 696  ARG A NH1 
1084 N NH2 . ARG A 159 ? 1.2082 1.1170 1.0506 0.0137  -0.0620 -0.0103 696  ARG A NH2 
1085 N N   . HIS A 160 ? 0.3442 0.3414 0.2794 -0.0096 -0.0392 -0.0280 697  HIS A N   
1086 C CA  . HIS A 160 ? 0.3488 0.3643 0.2991 -0.0088 -0.0428 -0.0307 697  HIS A CA  
1087 C C   . HIS A 160 ? 0.3577 0.3775 0.3128 -0.0171 -0.0389 -0.0341 697  HIS A C   
1088 O O   . HIS A 160 ? 0.3619 0.3930 0.3226 -0.0194 -0.0435 -0.0370 697  HIS A O   
1089 C CB  . HIS A 160 ? 0.3470 0.3723 0.3118 -0.0044 -0.0405 -0.0298 697  HIS A CB  
1090 C CG  . HIS A 160 ? 0.4863 0.5109 0.4484 0.0049  -0.0462 -0.0279 697  HIS A CG  
1091 N ND1 . HIS A 160 ? 0.5573 0.5977 0.5297 0.0112  -0.0521 -0.0297 697  HIS A ND1 
1092 C CD2 . HIS A 160 ? 0.4894 0.4986 0.4390 0.0091  -0.0469 -0.0246 697  HIS A CD2 
1093 C CE1 . HIS A 160 ? 0.5563 0.5901 0.5221 0.0201  -0.0565 -0.0277 697  HIS A CE1 
1094 N NE2 . HIS A 160 ? 0.5362 0.5498 0.4872 0.0185  -0.0536 -0.0244 697  HIS A NE2 
1095 N N   . TRP A 161 ? 0.3203 0.3309 0.2734 -0.0215 -0.0308 -0.0339 698  TRP A N   
1096 C CA  . TRP A 161 ? 0.2955 0.3061 0.2509 -0.0284 -0.0267 -0.0371 698  TRP A CA  
1097 C C   . TRP A 161 ? 0.3642 0.3697 0.3070 -0.0326 -0.0306 -0.0398 698  TRP A C   
1098 O O   . TRP A 161 ? 0.3456 0.3581 0.2921 -0.0372 -0.0333 -0.0429 698  TRP A O   
1099 C CB  . TRP A 161 ? 0.3268 0.3276 0.2818 -0.0300 -0.0180 -0.0367 698  TRP A CB  
1100 C CG  . TRP A 161 ? 0.3435 0.3421 0.3014 -0.0351 -0.0134 -0.0397 698  TRP A CG  
1101 C CD1 . TRP A 161 ? 0.3226 0.3257 0.2824 -0.0403 -0.0156 -0.0426 698  TRP A CD1 
1102 C CD2 . TRP A 161 ? 0.3223 0.3130 0.2814 -0.0355 -0.0062 -0.0403 698  TRP A CD2 
1103 N NE1 . TRP A 161 ? 0.3268 0.3219 0.2862 -0.0439 -0.0100 -0.0447 698  TRP A NE1 
1104 C CE2 . TRP A 161 ? 0.3659 0.3539 0.3254 -0.0402 -0.0045 -0.0435 698  TRP A CE2 
1105 C CE3 . TRP A 161 ? 0.3334 0.3193 0.2934 -0.0325 -0.0014 -0.0390 698  TRP A CE3 
1106 C CZ2 . TRP A 161 ? 0.3356 0.3148 0.2956 -0.0401 0.0014  -0.0451 698  TRP A CZ2 
1107 C CZ3 . TRP A 161 ? 0.3169 0.2977 0.2800 -0.0326 0.0043  -0.0410 698  TRP A CZ3 
1108 C CH2 . TRP A 161 ? 0.3388 0.3155 0.3015 -0.0356 0.0055  -0.0440 698  TRP A CH2 
1109 N N   . VAL A 162 ? 0.3671 0.3597 0.2936 -0.0319 -0.0310 -0.0386 699  VAL A N   
1110 C CA  . VAL A 162 ? 0.3801 0.3655 0.2913 -0.0359 -0.0348 -0.0411 699  VAL A CA  
1111 C C   . VAL A 162 ? 0.4419 0.4358 0.3519 -0.0330 -0.0467 -0.0415 699  VAL A C   
1112 O O   . VAL A 162 ? 0.4809 0.4749 0.3840 -0.0370 -0.0519 -0.0446 699  VAL A O   
1113 C CB  . VAL A 162 ? 0.4446 0.4117 0.3359 -0.0370 -0.0306 -0.0400 699  VAL A CB  
1114 C CG1 . VAL A 162 ? 0.4156 0.3771 0.3097 -0.0403 -0.0190 -0.0414 699  VAL A CG1 
1115 C CG2 . VAL A 162 ? 0.4787 0.4404 0.3631 -0.0314 -0.0336 -0.0354 699  VAL A CG2 
1116 N N   . GLU A 163 ? 0.3966 0.3980 0.3133 -0.0255 -0.0516 -0.0388 700  GLU A N   
1117 C CA  . GLU A 163 ? 0.4076 0.4194 0.3256 -0.0207 -0.0637 -0.0397 700  GLU A CA  
1118 C C   . GLU A 163 ? 0.4488 0.4823 0.3861 -0.0239 -0.0664 -0.0438 700  GLU A C   
1119 O O   . GLU A 163 ? 0.4522 0.4930 0.3883 -0.0259 -0.0749 -0.0470 700  GLU A O   
1120 C CB  . GLU A 163 ? 0.4369 0.4500 0.3567 -0.0106 -0.0679 -0.0362 700  GLU A CB  
1121 C CG  . GLU A 163 ? 0.4724 0.4961 0.3937 -0.0031 -0.0812 -0.0374 700  GLU A CG  
1122 C CD  . GLU A 163 ? 0.7050 0.7138 0.6029 -0.0033 -0.0898 -0.0373 700  GLU A CD  
1123 O OE1 . GLU A 163 ? 0.6684 0.6545 0.5446 -0.0027 -0.0879 -0.0337 700  GLU A OE1 
1124 O OE2 . GLU A 163 ? 0.7441 0.7637 0.6447 -0.0049 -0.0983 -0.0411 700  GLU A OE2 
1125 N N   . HIS A 164 ? 0.4011 0.4447 0.3556 -0.0251 -0.0594 -0.0438 701  HIS A N   
1126 C CA  . HIS A 164 ? 0.4309 0.4963 0.4046 -0.0283 -0.0610 -0.0472 701  HIS A CA  
1127 C C   . HIS A 164 ? 0.4343 0.4989 0.4117 -0.0391 -0.0541 -0.0499 701  HIS A C   
1128 O O   . HIS A 164 ? 0.3997 0.4805 0.3905 -0.0446 -0.0552 -0.0532 701  HIS A O   
1129 C CB  . HIS A 164 ? 0.3460 0.4240 0.3353 -0.0217 -0.0587 -0.0456 701  HIS A CB  
1130 C CG  . HIS A 164 ? 0.4257 0.5054 0.4125 -0.0102 -0.0663 -0.0437 701  HIS A CG  
1131 N ND1 . HIS A 164 ? 0.5053 0.5979 0.4952 -0.0054 -0.0775 -0.0463 701  HIS A ND1 
1132 C CD2 . HIS A 164 ? 0.4389 0.5076 0.4192 -0.0024 -0.0649 -0.0398 701  HIS A CD2 
1133 C CE1 . HIS A 164 ? 0.5248 0.6130 0.5095 0.0060  -0.0827 -0.0438 701  HIS A CE1 
1134 N NE2 . HIS A 164 ? 0.5217 0.5945 0.4998 0.0073  -0.0749 -0.0398 701  HIS A NE2 
1135 N N   . HIS A 165 ? 0.4223 0.3430 0.2982 -0.0546 0.0232  -0.0720 702  HIS A N   
1136 C CA  . HIS A 165 ? 0.3657 0.2925 0.2447 -0.0547 0.0260  -0.0798 702  HIS A CA  
1137 C C   . HIS A 165 ? 0.4639 0.3991 0.3374 -0.0606 0.0282  -0.0833 702  HIS A C   
1138 O O   . HIS A 165 ? 0.4039 0.3421 0.2802 -0.0620 0.0314  -0.0902 702  HIS A O   
1139 C CB  . HIS A 165 ? 0.3806 0.3017 0.2660 -0.0520 0.0286  -0.0844 702  HIS A CB  
1140 C CG  . HIS A 165 ? 0.4342 0.3479 0.3244 -0.0460 0.0270  -0.0819 702  HIS A CG  
1141 N ND1 . HIS A 165 ? 0.4347 0.3513 0.3306 -0.0420 0.0259  -0.0837 702  HIS A ND1 
1142 C CD2 . HIS A 165 ? 0.4192 0.3237 0.3096 -0.0431 0.0259  -0.0778 702  HIS A CD2 
1143 C CE1 . HIS A 165 ? 0.4270 0.3371 0.3260 -0.0370 0.0252  -0.0812 702  HIS A CE1 
1144 N NE2 . HIS A 165 ? 0.4201 0.3224 0.3158 -0.0373 0.0250  -0.0780 702  HIS A NE2 
1145 N N   . PHE A 166 ? 0.4827 0.4223 0.3486 -0.0643 0.0264  -0.0788 703  PHE A N   
1146 C CA  . PHE A 166 ? 0.4979 0.4462 0.3570 -0.0702 0.0289  -0.0816 703  PHE A CA  
1147 C C   . PHE A 166 ? 0.4472 0.4040 0.3087 -0.0699 0.0300  -0.0904 703  PHE A C   
1148 O O   . PHE A 166 ? 0.4856 0.4499 0.3444 -0.0737 0.0331  -0.0959 703  PHE A O   
1149 C CB  . PHE A 166 ? 0.5047 0.4561 0.3545 -0.0748 0.0261  -0.0746 703  PHE A CB  
1150 C CG  . PHE A 166 ? 0.5954 0.5563 0.4371 -0.0814 0.0293  -0.0765 703  PHE A CG  
1151 C CD1 . PHE A 166 ? 0.5897 0.5501 0.4301 -0.0848 0.0323  -0.0749 703  PHE A CD1 
1152 C CD2 . PHE A 166 ? 0.5925 0.5631 0.4282 -0.0841 0.0293  -0.0801 703  PHE A CD2 
1153 C CE1 . PHE A 166 ? 0.6223 0.5929 0.4557 -0.0909 0.0359  -0.0765 703  PHE A CE1 
1154 C CE2 . PHE A 166 ? 0.5316 0.5121 0.3595 -0.0901 0.0329  -0.0825 703  PHE A CE2 
1155 C CZ  . PHE A 166 ? 0.5816 0.5627 0.4085 -0.0936 0.0365  -0.0807 703  PHE A CZ  
1156 N N   . TYR A 167 ? 0.4798 0.4359 0.3474 -0.0653 0.0270  -0.0919 704  TYR A N   
1157 C CA  . TYR A 167 ? 0.4866 0.4502 0.3584 -0.0645 0.0264  -0.1000 704  TYR A CA  
1158 C C   . TYR A 167 ? 0.4635 0.4288 0.3415 -0.0655 0.0299  -0.1085 704  TYR A C   
1159 O O   . TYR A 167 ? 0.4628 0.4362 0.3428 -0.0669 0.0299  -0.1162 704  TYR A O   
1160 C CB  . TYR A 167 ? 0.5027 0.4648 0.3817 -0.0593 0.0219  -0.0988 704  TYR A CB  
1161 C CG  . TYR A 167 ? 0.4197 0.3735 0.3056 -0.0551 0.0223  -0.0961 704  TYR A CG  
1162 C CD1 . TYR A 167 ? 0.4533 0.4058 0.3472 -0.0540 0.0240  -0.1018 704  TYR A CD1 
1163 C CD2 . TYR A 167 ? 0.4038 0.3512 0.2886 -0.0525 0.0206  -0.0882 704  TYR A CD2 
1164 C CE1 . TYR A 167 ? 0.4227 0.3678 0.3218 -0.0504 0.0245  -0.0995 704  TYR A CE1 
1165 C CE2 . TYR A 167 ? 0.4416 0.3820 0.3323 -0.0483 0.0212  -0.0865 704  TYR A CE2 
1166 C CZ  . TYR A 167 ? 0.4207 0.3602 0.3178 -0.0472 0.0233  -0.0922 704  TYR A CZ  
1167 O OH  . TYR A 167 ? 0.4389 0.3718 0.3408 -0.0432 0.0240  -0.0908 704  TYR A OH  
1168 N N   . ASP A 168 ? 0.4548 0.4121 0.3365 -0.0648 0.0324  -0.1073 705  ASP A N   
1169 C CA  . ASP A 168 ? 0.4245 0.3818 0.3121 -0.0665 0.0356  -0.1147 705  ASP A CA  
1170 C C   . ASP A 168 ? 0.4379 0.4035 0.3201 -0.0716 0.0390  -0.1186 705  ASP A C   
1171 O O   . ASP A 168 ? 0.4321 0.4031 0.3196 -0.0733 0.0405  -0.1274 705  ASP A O   
1172 C CB  . ASP A 168 ? 0.3801 0.3261 0.2702 -0.0656 0.0377  -0.1115 705  ASP A CB  
1173 C CG  . ASP A 168 ? 0.4425 0.3815 0.3401 -0.0609 0.0355  -0.1110 705  ASP A CG  
1174 O OD1 . ASP A 168 ? 0.3903 0.3339 0.2938 -0.0592 0.0328  -0.1147 705  ASP A OD1 
1175 O OD2 . ASP A 168 ? 0.4316 0.3606 0.3292 -0.0590 0.0362  -0.1068 705  ASP A OD2 
1176 N N   . PHE A 169 ? 0.4456 0.4126 0.3178 -0.0744 0.0400  -0.1121 706  PHE A N   
1177 C CA  . PHE A 169 ? 0.4299 0.4054 0.2958 -0.0797 0.0439  -0.1145 706  PHE A CA  
1178 C C   . PHE A 169 ? 0.4953 0.4827 0.3560 -0.0811 0.0427  -0.1191 706  PHE A C   
1179 O O   . PHE A 169 ? 0.5438 0.5407 0.4024 -0.0844 0.0459  -0.1256 706  PHE A O   
1180 C CB  . PHE A 169 ? 0.4595 0.4317 0.3172 -0.0828 0.0448  -0.1047 706  PHE A CB  
1181 C CG  . PHE A 169 ? 0.4440 0.4042 0.3068 -0.0811 0.0453  -0.1006 706  PHE A CG  
1182 C CD1 . PHE A 169 ? 0.4585 0.4178 0.3245 -0.0835 0.0494  -0.1032 706  PHE A CD1 
1183 C CD2 . PHE A 169 ? 0.4912 0.4409 0.3563 -0.0767 0.0416  -0.0946 706  PHE A CD2 
1184 C CE1 . PHE A 169 ? 0.4515 0.3983 0.3219 -0.0817 0.0492  -0.0993 706  PHE A CE1 
1185 C CE2 . PHE A 169 ? 0.4898 0.4280 0.3592 -0.0745 0.0416  -0.0915 706  PHE A CE2 
1186 C CZ  . PHE A 169 ? 0.4846 0.4209 0.3564 -0.0771 0.0452  -0.0937 706  PHE A CZ  
1187 N N   . GLU A 170 ? 0.5006 0.4870 0.3596 -0.0784 0.0378  -0.1159 707  GLU A N   
1188 C CA  . GLU A 170 ? 0.5539 0.5497 0.4085 -0.0789 0.0354  -0.1200 707  GLU A CA  
1189 C C   . GLU A 170 ? 0.5806 0.5818 0.4450 -0.0767 0.0343  -0.1314 707  GLU A C   
1190 O O   . GLU A 170 ? 0.5699 0.5812 0.4318 -0.0783 0.0345  -0.1388 707  GLU A O   
1191 C CB  . GLU A 170 ? 0.6072 0.5987 0.4590 -0.0762 0.0297  -0.1128 707  GLU A CB  
1192 C CG  . GLU A 170 ? 0.5924 0.5795 0.4348 -0.0792 0.0292  -0.1020 707  GLU A CG  
1193 C CD  . GLU A 170 ? 0.6728 0.6540 0.5151 -0.0762 0.0233  -0.0949 707  GLU A CD  
1194 O OE1 . GLU A 170 ? 0.7143 0.6924 0.5657 -0.0709 0.0206  -0.0965 707  GLU A OE1 
1195 O OE2 . GLU A 170 ? 0.7051 0.6852 0.5388 -0.0795 0.0212  -0.0874 707  GLU A OE2 
1196 N N   . ARG A 171 ? 0.5441 0.5387 0.4199 -0.0733 0.0328  -0.1329 708  ARG A N   
1197 C CA  . ARG A 171 ? 0.5941 0.5926 0.4817 -0.0715 0.0302  -0.1427 708  ARG A CA  
1198 C C   . ARG A 171 ? 0.5799 0.5821 0.4725 -0.0746 0.0346  -0.1515 708  ARG A C   
1199 O O   . ARG A 171 ? 0.6243 0.6322 0.5273 -0.0736 0.0319  -0.1595 708  ARG A O   
1200 C CB  . ARG A 171 ? 0.5677 0.5580 0.4654 -0.0676 0.0267  -0.1401 708  ARG A CB  
1201 C CG  . ARG A 171 ? 0.5078 0.4957 0.4039 -0.0639 0.0217  -0.1327 708  ARG A CG  
1202 C CD  . ARG A 171 ? 0.5251 0.5050 0.4295 -0.0606 0.0203  -0.1289 708  ARG A CD  
1203 N NE  . ARG A 171 ? 0.6487 0.6263 0.5520 -0.0569 0.0164  -0.1211 708  ARG A NE  
1204 C CZ  . ARG A 171 ? 0.6247 0.5967 0.5340 -0.0534 0.0152  -0.1168 708  ARG A CZ  
1205 N NH1 . ARG A 171 ? 0.6037 0.5714 0.5195 -0.0535 0.0174  -0.1194 708  ARG A NH1 
1206 N NH2 . ARG A 171 ? 0.7716 0.7425 0.6805 -0.0501 0.0119  -0.1099 708  ARG A NH2 
1207 N N   . ASP A 172 ? 0.5163 0.5152 0.4041 -0.0776 0.0404  -0.1478 709  ASP A N   
1208 C CA  . ASP A 172 ? 0.4908 0.4919 0.3841 -0.0806 0.0449  -0.1549 709  ASP A CA  
1209 C C   . ASP A 172 ? 0.6313 0.6367 0.5140 -0.0850 0.0508  -0.1513 709  ASP A C   
1210 O O   . ASP A 172 ? 0.4957 0.4933 0.3744 -0.0860 0.0530  -0.1427 709  ASP A O   
1211 C CB  . ASP A 172 ? 0.5116 0.5007 0.4148 -0.0796 0.0451  -0.1538 709  ASP A CB  
1212 C CG  . ASP A 172 ? 0.6272 0.6180 0.5420 -0.0805 0.0476  -0.1567 709  ASP A CG  
1213 O OD1 . ASP A 172 ? 0.6006 0.6007 0.5124 -0.0835 0.0515  -0.1607 709  ASP A OD1 
1214 O OD2 . ASP A 172 ? 0.6645 0.6476 0.5915 -0.0781 0.0454  -0.1543 709  ASP A OD2 
1215 N N   . LEU A 173 ? 0.5851 0.6035 0.4634 -0.0875 0.0530  -0.1581 710  LEU A N   
1216 C CA  . LEU A 173 ? 0.6116 0.6369 0.4790 -0.0922 0.0585  -0.1544 710  LEU A CA  
1217 C C   . LEU A 173 ? 0.4963 0.5185 0.3685 -0.0950 0.0639  -0.1542 710  LEU A C   
1218 O O   . LEU A 173 ? 0.5466 0.5687 0.4108 -0.0984 0.0671  -0.1459 710  LEU A O   
1219 C CB  . LEU A 173 ? 0.6966 0.7378 0.5583 -0.0942 0.0600  -0.1631 710  LEU A CB  
1220 C CG  . LEU A 173 ? 0.8167 0.8611 0.6693 -0.0926 0.0550  -0.1607 710  LEU A CG  
1221 C CD1 . LEU A 173 ? 0.8211 0.8810 0.6634 -0.0958 0.0577  -0.1665 710  LEU A CD1 
1222 C CD2 . LEU A 173 ? 0.8207 0.8556 0.6650 -0.0929 0.0528  -0.1465 710  LEU A CD2 
1223 N N   . GLU A 174 ? 0.5519 0.5713 0.4376 -0.0940 0.0642  -0.1627 711  GLU A N   
1224 C CA  . GLU A 174 ? 0.6130 0.6282 0.5044 -0.0967 0.0690  -0.1625 711  GLU A CA  
1225 C C   . GLU A 174 ? 0.5786 0.5780 0.4691 -0.0956 0.0678  -0.1509 711  GLU A C   
1226 O O   . GLU A 174 ? 0.5106 0.5067 0.3997 -0.0982 0.0713  -0.1453 711  GLU A O   
1227 C CB  . GLU A 174 ? 0.6437 0.6589 0.5551 -0.0940 0.0670  -0.1687 711  GLU A CB  
1228 C CG  . GLU A 174 ? 0.7852 0.7999 0.7018 -0.0978 0.0728  -0.1704 711  GLU A CG  
1229 C CD  . GLU A 174 ? 0.9420 0.9477 0.8783 -0.0947 0.0694  -0.1696 711  GLU A CD  
1230 O OE1 . GLU A 174 ? 0.9999 1.0028 0.9464 -0.0895 0.0624  -0.1681 711  GLU A OE1 
1231 O OE2 . GLU A 174 ? 0.9494 0.9512 0.8904 -0.0976 0.0734  -0.1697 711  GLU A OE2 
1232 N N   . LEU A 175 ? 0.5063 0.4965 0.3982 -0.0915 0.0627  -0.1473 712  LEU A N   
1233 C CA  . LEU A 175 ? 0.4474 0.4230 0.3380 -0.0896 0.0611  -0.1370 712  LEU A CA  
1234 C C   . LEU A 175 ? 0.4572 0.4340 0.3359 -0.0920 0.0622  -0.1261 712  LEU A C   
1235 O O   . LEU A 175 ? 0.4546 0.4231 0.3331 -0.0930 0.0631  -0.1191 712  LEU A O   
1236 C CB  . LEU A 175 ? 0.4718 0.4407 0.3647 -0.0847 0.0556  -0.1352 712  LEU A CB  
1237 C CG  . LEU A 175 ? 0.4367 0.3907 0.3296 -0.0817 0.0536  -0.1264 712  LEU A CG  
1238 C CD1 . LEU A 175 ? 0.4717 0.4151 0.3738 -0.0819 0.0549  -0.1289 712  LEU A CD1 
1239 C CD2 . LEU A 175 ? 0.4759 0.4269 0.3696 -0.0770 0.0489  -0.1244 712  LEU A CD2 
1240 N N   . LEU A 176 ? 0.4592 0.4458 0.3282 -0.0932 0.0613  -0.1243 713  LEU A N   
1241 C CA  . LEU A 176 ? 0.4866 0.4751 0.3446 -0.0964 0.0611  -0.1136 713  LEU A CA  
1242 C C   . LEU A 176 ? 0.4998 0.4960 0.3550 -0.1019 0.0663  -0.1127 713  LEU A C   
1243 O O   . LEU A 176 ? 0.4950 0.4870 0.3468 -0.1043 0.0660  -0.1028 713  LEU A O   
1244 C CB  . LEU A 176 ? 0.4609 0.4578 0.3092 -0.0972 0.0586  -0.1122 713  LEU A CB  
1245 C CG  . LEU A 176 ? 0.5347 0.5334 0.3717 -0.1013 0.0569  -0.1007 713  LEU A CG  
1246 C CD1 . LEU A 176 ? 0.5187 0.5030 0.3579 -0.0990 0.0527  -0.0904 713  LEU A CD1 
1247 C CD2 . LEU A 176 ? 0.5984 0.6040 0.4268 -0.1020 0.0539  -0.1004 713  LEU A CD2 
1248 N N   . GLU A 177 ? 0.5299 0.5378 0.3875 -0.1039 0.0707  -0.1230 714  GLU A N   
1249 C CA  . GLU A 177 ? 0.5603 0.5773 0.4165 -0.1090 0.0765  -0.1233 714  GLU A CA  
1250 C C   . GLU A 177 ? 0.4742 0.4793 0.3390 -0.1088 0.0776  -0.1195 714  GLU A C   
1251 O O   . GLU A 177 ? 0.4877 0.4944 0.3491 -0.1127 0.0795  -0.1115 714  GLU A O   
1252 C CB  . GLU A 177 ? 0.6538 0.6853 0.5134 -0.1101 0.0808  -0.1371 714  GLU A CB  
1253 C CG  . GLU A 177 ? 0.7757 0.8219 0.6240 -0.1118 0.0809  -0.1401 714  GLU A CG  
1254 C CD  . GLU A 177 ? 1.0106 1.0748 0.8549 -0.1167 0.0877  -0.1457 714  GLU A CD  
1255 O OE1 . GLU A 177 ? 1.0239 1.0895 0.8700 -0.1201 0.0920  -0.1417 714  GLU A OE1 
1256 O OE2 . GLU A 177 ? 1.0540 1.1311 0.8933 -0.1169 0.0885  -0.1542 714  GLU A OE2 
1257 N N   . ARG A 178 ? 0.4548 0.4478 0.3307 -0.1047 0.0758  -0.1246 715  ARG A N   
1258 C CA  . ARG A 178 ? 0.4647 0.4436 0.3486 -0.1041 0.0758  -0.1207 715  ARG A CA  
1259 C C   . ARG A 178 ? 0.4416 0.4095 0.3197 -0.1032 0.0718  -0.1069 715  ARG A C   
1260 O O   . ARG A 178 ? 0.4720 0.4347 0.3509 -0.1052 0.0724  -0.0998 715  ARG A O   
1261 C CB  . ARG A 178 ? 0.4911 0.4584 0.3868 -0.1001 0.0736  -0.1281 715  ARG A CB  
1262 C CG  . ARG A 178 ? 0.5987 0.5726 0.5049 -0.1014 0.0764  -0.1415 715  ARG A CG  
1263 C CD  . ARG A 178 ? 0.4862 0.4465 0.4040 -0.0984 0.0727  -0.1462 715  ARG A CD  
1264 N NE  . ARG A 178 ? 0.5637 0.5077 0.4860 -0.0985 0.0725  -0.1402 715  ARG A NE  
1265 C CZ  . ARG A 178 ? 0.4787 0.4073 0.4067 -0.0956 0.0688  -0.1394 715  ARG A CZ  
1266 N NH1 . ARG A 178 ? 0.4532 0.3839 0.3859 -0.0909 0.0639  -0.1403 715  ARG A NH1 
1267 N NH2 . ARG A 178 ? 0.5086 0.4222 0.4396 -0.0958 0.0685  -0.1338 715  ARG A NH2 
1268 N N   . LEU A 179 ? 0.4129 0.3768 0.2861 -0.0999 0.0671  -0.1031 716  LEU A N   
1269 C CA  . LEU A 179 ? 0.4474 0.4009 0.3164 -0.0986 0.0623  -0.0909 716  LEU A CA  
1270 C C   . LEU A 179 ? 0.4638 0.4260 0.3244 -0.1042 0.0626  -0.0817 716  LEU A C   
1271 O O   . LEU A 179 ? 0.4842 0.4392 0.3456 -0.1053 0.0605  -0.0729 716  LEU A O   
1272 C CB  . LEU A 179 ? 0.4843 0.4340 0.3503 -0.0944 0.0574  -0.0892 716  LEU A CB  
1273 C CG  . LEU A 179 ? 0.4928 0.4334 0.3550 -0.0930 0.0517  -0.0772 716  LEU A CG  
1274 C CD1 . LEU A 179 ? 0.5189 0.4437 0.3875 -0.0901 0.0500  -0.0735 716  LEU A CD1 
1275 C CD2 . LEU A 179 ? 0.5069 0.4449 0.3672 -0.0889 0.0474  -0.0765 716  LEU A CD2 
1276 N N   . GLU A 180 ? 0.4499 0.4279 0.3026 -0.1081 0.0646  -0.0836 717  GLU A N   
1277 C CA  . GLU A 180 ? 0.4587 0.4471 0.3025 -0.1145 0.0647  -0.0748 717  GLU A CA  
1278 C C   . GLU A 180 ? 0.5702 0.5622 0.4175 -0.1184 0.0691  -0.0732 717  GLU A C   
1279 O O   . GLU A 180 ? 0.5468 0.5387 0.3913 -0.1221 0.0667  -0.0619 717  GLU A O   
1280 C CB  . GLU A 180 ? 0.5492 0.5544 0.3835 -0.1181 0.0669  -0.0791 717  GLU A CB  
1281 C CG  . GLU A 180 ? 0.6150 0.6166 0.4447 -0.1153 0.0615  -0.0776 717  GLU A CG  
1282 C CD  . GLU A 180 ? 0.7413 0.7578 0.5616 -0.1185 0.0632  -0.0822 717  GLU A CD  
1283 O OE1 . GLU A 180 ? 0.6944 0.7208 0.5162 -0.1185 0.0684  -0.0933 717  GLU A OE1 
1284 O OE2 . GLU A 180 ? 0.7795 0.7972 0.5913 -0.1209 0.0586  -0.0748 717  GLU A OE2 
1285 N N   . SER A 181 ? 0.5161 0.5116 0.3706 -0.1178 0.0750  -0.0842 718  SER A N   
1286 C CA  . SER A 181 ? 0.5036 0.5021 0.3633 -0.1212 0.0795  -0.0836 718  SER A CA  
1287 C C   . SER A 181 ? 0.5687 0.5489 0.4348 -0.1190 0.0753  -0.0745 718  SER A C   
1288 O O   . SER A 181 ? 0.4893 0.4704 0.3552 -0.1226 0.0750  -0.0652 718  SER A O   
1289 C CB  . SER A 181 ? 0.6538 0.6573 0.5226 -0.1203 0.0855  -0.0982 718  SER A CB  
1290 O OG  . SER A 181 ? 0.7463 0.7465 0.6236 -0.1221 0.0889  -0.0975 718  SER A OG  
1291 N N   . PHE A 182 ? 0.4923 0.4559 0.3639 -0.1129 0.0714  -0.0768 719  PHE A N   
1292 C CA  . PHE A 182 ? 0.4614 0.4066 0.3387 -0.1101 0.0671  -0.0692 719  PHE A CA  
1293 C C   . PHE A 182 ? 0.4902 0.4325 0.3610 -0.1114 0.0606  -0.0548 719  PHE A C   
1294 O O   . PHE A 182 ? 0.5091 0.4453 0.3827 -0.1129 0.0584  -0.0461 719  PHE A O   
1295 C CB  . PHE A 182 ? 0.4390 0.3680 0.3219 -0.1035 0.0640  -0.0743 719  PHE A CB  
1296 C CG  . PHE A 182 ? 0.5011 0.4109 0.3878 -0.1002 0.0589  -0.0663 719  PHE A CG  
1297 C CD1 . PHE A 182 ? 0.5313 0.4316 0.4260 -0.1009 0.0604  -0.0663 719  PHE A CD1 
1298 C CD2 . PHE A 182 ? 0.5041 0.4053 0.3868 -0.0966 0.0520  -0.0585 719  PHE A CD2 
1299 C CE1 . PHE A 182 ? 0.5297 0.4114 0.4274 -0.0977 0.0550  -0.0586 719  PHE A CE1 
1300 C CE2 . PHE A 182 ? 0.4998 0.3833 0.3860 -0.0931 0.0466  -0.0514 719  PHE A CE2 
1301 C CZ  . PHE A 182 ? 0.4935 0.3670 0.3866 -0.0936 0.0480  -0.0514 719  PHE A CZ  
1302 N N   . ILE A 183 ? 0.5145 0.4610 0.3777 -0.1111 0.0567  -0.0517 720  ILE A N   
1303 C CA  . ILE A 183 ? 0.4781 0.4201 0.3372 -0.1121 0.0489  -0.0382 720  ILE A CA  
1304 C C   . ILE A 183 ? 0.5662 0.5222 0.4204 -0.1201 0.0495  -0.0294 720  ILE A C   
1305 O O   . ILE A 183 ? 0.6077 0.5593 0.4616 -0.1219 0.0426  -0.0171 720  ILE A O   
1306 C CB  . ILE A 183 ? 0.5470 0.4889 0.4005 -0.1100 0.0438  -0.0367 720  ILE A CB  
1307 C CG1 . ILE A 183 ? 0.6462 0.6064 0.4910 -0.1150 0.0473  -0.0400 720  ILE A CG1 
1308 C CG2 . ILE A 183 ? 0.4920 0.4214 0.3505 -0.1022 0.0432  -0.0445 720  ILE A CG2 
1309 C CD1 . ILE A 183 ? 0.7542 0.7129 0.5946 -0.1127 0.0425  -0.0395 720  ILE A CD1 
1310 N N   . SER A 184 ? 0.6365 0.6098 0.4873 -0.1249 0.0572  -0.0357 721  SER A N   
1311 C CA  . SER A 184 ? 0.6438 0.6322 0.4904 -0.1328 0.0591  -0.0282 721  SER A CA  
1312 C C   . SER A 184 ? 0.7381 0.7197 0.5934 -0.1332 0.0601  -0.0237 721  SER A C   
1313 O O   . SER A 184 ? 0.7276 0.7165 0.5815 -0.1388 0.0585  -0.0130 721  SER A O   
1314 C CB  . SER A 184 ? 0.6965 0.7058 0.5371 -0.1372 0.0678  -0.0375 721  SER A CB  
1315 O OG  . SER A 184 ? 0.8484 0.8581 0.6972 -0.1348 0.0753  -0.0497 721  SER A OG  
1316 N N   . SER A 185 ? 0.7086 0.6762 0.5733 -0.1275 0.0622  -0.0315 722  SER A N   
1317 C CA  . SER A 185 ? 0.6820 0.6407 0.5560 -0.1275 0.0630  -0.0282 722  SER A CA  
1318 C C   . SER A 185 ? 0.6425 0.5821 0.5199 -0.1242 0.0533  -0.0160 722  SER A C   
1319 O O   . SER A 185 ? 0.7151 0.6466 0.5994 -0.1246 0.0520  -0.0101 722  SER A O   
1320 C CB  . SER A 185 ? 0.6526 0.6036 0.5358 -0.1237 0.0689  -0.0418 722  SER A CB  
1321 O OG  . SER A 185 ? 0.6522 0.5833 0.5391 -0.1168 0.0640  -0.0441 722  SER A OG  
1322 N N   . VAL A 186 ? 0.6312 0.5633 0.5045 -0.1208 0.0458  -0.0122 723  VAL A N   
1323 C CA  . VAL A 186 ? 0.6591 0.5723 0.5362 -0.1166 0.0359  -0.0023 723  VAL A CA  
1324 C C   . VAL A 186 ? 0.8629 0.7812 0.7387 -0.1220 0.0291  0.0134  723  VAL A C   
1325 O O   . VAL A 186 ? 0.8429 0.7778 0.7115 -0.1282 0.0283  0.0184  723  VAL A O   
1326 C CB  . VAL A 186 ? 0.6436 0.5480 0.5178 -0.1109 0.0299  -0.0039 723  VAL A CB  
1327 C CG1 . VAL A 186 ? 0.6402 0.5271 0.5180 -0.1066 0.0187  0.0064  723  VAL A CG1 
1328 C CG2 . VAL A 186 ? 0.5520 0.4496 0.4290 -0.1052 0.0354  -0.0178 723  VAL A CG2 
1329 N N   . ARG A 187 ? 0.9290 0.8330 0.8120 -0.1200 0.0237  0.0213  724  ARG A N   
1330 C CA  . ARG A 187 ? 0.9578 0.8652 0.8418 -0.1249 0.0158  0.0372  724  ARG A CA  
1331 C C   . ARG A 187 ? 0.9442 0.8366 0.8298 -0.1207 0.0018  0.0472  724  ARG A C   
1332 O O   . ARG A 187 ? 0.9989 0.8745 0.8866 -0.1128 -0.0013 0.0417  724  ARG A O   
1333 C CB  . ARG A 187 ? 0.9116 0.8141 0.8036 -0.1261 0.0183  0.0409  724  ARG A CB  
1334 C CG  . ARG A 187 ? 0.9938 0.9113 0.8865 -0.1305 0.0316  0.0316  724  ARG A CG  
1335 C CD  . ARG A 187 ? 1.0816 1.0240 0.9690 -0.1399 0.0343  0.0389  724  ARG A CD  
1336 N NE  . ARG A 187 ? 1.1620 1.1214 1.0388 -0.1431 0.0373  0.0339  724  ARG A NE  
1337 C CZ  . ARG A 187 ? 1.1961 1.1691 1.0690 -0.1444 0.0481  0.0204  724  ARG A CZ  
1338 N NH1 . ARG A 187 ? 1.1851 1.1575 1.0649 -0.1430 0.0570  0.0103  724  ARG A NH1 
1339 N NH2 . ARG A 187 ? 1.1633 1.1501 1.0261 -0.1472 0.0494  0.0171  724  ARG A NH2 
1340 N N   . GLY A 188 ? 0.8647 0.7638 0.7498 -0.1261 -0.0071 0.0618  725  GLY A N   
1341 C CA  . GLY A 188 ? 0.9130 0.7977 0.8022 -0.1225 -0.0221 0.0724  725  GLY A CA  
1342 C C   . GLY A 188 ? 0.9557 0.8450 0.8401 -0.1231 -0.0294 0.0743  725  GLY A C   
1343 O O   . GLY A 188 ? 0.9753 0.8665 0.8549 -0.1205 -0.0238 0.0633  725  GLY A O   
1344 N N   . LYS A 189 ? 0.9589 0.8492 0.8456 -0.1267 -0.0428 0.0886  726  LYS A N   
1345 C CA  . LYS A 189 ? 1.0664 0.9610 0.9501 -0.1287 -0.0517 0.0922  726  LYS A CA  
1346 C C   . LYS A 189 ? 1.0689 0.9459 0.9554 -0.1184 -0.0561 0.0844  726  LYS A C   
1347 O O   . LYS A 189 ? 1.0572 0.9376 0.9409 -0.1187 -0.0596 0.0826  726  LYS A O   
1348 C CB  . LYS A 189 ? 1.1407 1.0385 1.0286 -0.1348 -0.0671 0.1099  726  LYS A CB  
1349 C CG  . LYS A 189 ? 1.1888 1.1085 1.0726 -0.1468 -0.0642 0.1193  726  LYS A CG  
1350 C CD  . LYS A 189 ? 1.2050 1.1277 1.0938 -0.1531 -0.0815 0.1377  726  LYS A CD  
1351 C CE  . LYS A 189 ? 1.1690 1.1157 1.0529 -0.1661 -0.0788 0.1478  726  LYS A CE  
1352 N NZ  . LYS A 189 ? 1.1409 1.0909 1.0308 -0.1729 -0.0968 0.1668  726  LYS A NZ  
1353 N N   . ALA A 190 ? 1.0533 0.9117 0.9454 -0.1095 -0.0557 0.0798  727  ALA A N   
1354 C CA  . ALA A 190 ? 1.1130 0.9547 1.0080 -0.0993 -0.0597 0.0725  727  ALA A CA  
1355 C C   . ALA A 190 ? 1.1757 1.0225 1.0648 -0.0970 -0.0489 0.0586  727  ALA A C   
1356 O O   . ALA A 190 ? 1.2088 1.0471 1.0993 -0.0902 -0.0523 0.0533  727  ALA A O   
1357 C CB  . ALA A 190 ? 1.1359 0.9574 1.0368 -0.0911 -0.0604 0.0702  727  ALA A CB  
1358 N N   . MET A 191 ? 1.0768 0.9381 0.9601 -0.1024 -0.0364 0.0527  728  MET A N   
1359 C CA  . MET A 191 ? 0.9553 0.8213 0.8336 -0.1002 -0.0263 0.0395  728  MET A CA  
1360 C C   . MET A 191 ? 0.8869 0.7732 0.7574 -0.1084 -0.0220 0.0394  728  MET A C   
1361 O O   . MET A 191 ? 0.6986 0.5901 0.5649 -0.1071 -0.0148 0.0294  728  MET A O   
1362 C CB  . MET A 191 ? 0.9261 0.7883 0.8055 -0.0973 -0.0147 0.0290  728  MET A CB  
1363 C CG  . MET A 191 ? 0.9311 0.7753 0.8173 -0.0922 -0.0182 0.0315  728  MET A CG  
1364 S SD  . MET A 191 ? 0.7676 0.5989 0.6561 -0.0847 -0.0090 0.0167  728  MET A SD  
1365 C CE  . MET A 191 ? 0.8912 0.7176 0.7848 -0.0878 -0.0053 0.0198  728  MET A CE  
1366 N N   . LYS A 192 ? 0.9624 0.8603 0.8308 -0.1171 -0.0267 0.0507  729  LYS A N   
1367 C CA  . LYS A 192 ? 0.9315 0.8492 0.7912 -0.1258 -0.0224 0.0510  729  LYS A CA  
1368 C C   . LYS A 192 ? 0.8276 0.7451 0.6846 -0.1247 -0.0272 0.0492  729  LYS A C   
1369 O O   . LYS A 192 ? 0.8729 0.8016 0.7226 -0.1278 -0.0206 0.0431  729  LYS A O   
1370 C CB  . LYS A 192 ? 0.9736 0.9040 0.8316 -0.1359 -0.0276 0.0647  729  LYS A CB  
1371 C CG  . LYS A 192 ? 1.0918 1.0319 0.9489 -0.1398 -0.0176 0.0635  729  LYS A CG  
1372 C CD  . LYS A 192 ? 1.1444 1.0919 0.9964 -0.1383 -0.0030 0.0480  729  LYS A CD  
1373 C CE  . LYS A 192 ? 1.1517 1.0911 1.0099 -0.1334 0.0050  0.0406  729  LYS A CE  
1374 N NZ  . LYS A 192 ? 1.1416 1.0579 1.0081 -0.1243 -0.0014 0.0408  729  LYS A NZ  
1375 N N   . LYS A 193 ? 0.8901 0.7943 0.7535 -0.1199 -0.0389 0.0541  730  LYS A N   
1376 C CA  . LYS A 193 ? 0.8853 0.7869 0.7484 -0.1175 -0.0438 0.0518  730  LYS A CA  
1377 C C   . LYS A 193 ? 0.8222 0.7210 0.6833 -0.1106 -0.0333 0.0374  730  LYS A C   
1378 O O   . LYS A 193 ? 0.6629 0.5689 0.5190 -0.1124 -0.0306 0.0333  730  LYS A O   
1379 C CB  . LYS A 193 ? 0.9554 0.8419 0.8278 -0.1118 -0.0578 0.0577  730  LYS A CB  
1380 C CG  . LYS A 193 ? 1.1268 1.0121 1.0040 -0.1163 -0.0693 0.0715  730  LYS A CG  
1381 C CD  . LYS A 193 ? 1.1872 1.0665 1.0714 -0.1162 -0.0858 0.0797  730  LYS A CD  
1382 C CE  . LYS A 193 ? 1.1807 1.0490 1.0741 -0.1138 -0.0983 0.0893  730  LYS A CE  
1383 N NZ  . LYS A 193 ? 1.1466 0.9981 1.0444 -0.1020 -0.0947 0.0813  730  LYS A NZ  
1384 N N   . TRP A 194 ? 0.7474 0.6356 0.6125 -0.1031 -0.0279 0.0303  731  TRP A N   
1385 C CA  . TRP A 194 ? 0.6499 0.5350 0.5145 -0.0967 -0.0187 0.0172  731  TRP A CA  
1386 C C   . TRP A 194 ? 0.6742 0.5741 0.5319 -0.1016 -0.0073 0.0100  731  TRP A C   
1387 O O   . TRP A 194 ? 0.6262 0.5304 0.4808 -0.1002 -0.0031 0.0027  731  TRP A O   
1388 C CB  . TRP A 194 ? 0.7385 0.6086 0.6091 -0.0888 -0.0166 0.0124  731  TRP A CB  
1389 C CG  . TRP A 194 ? 0.7555 0.6098 0.6324 -0.0806 -0.0256 0.0138  731  TRP A CG  
1390 C CD1 . TRP A 194 ? 0.7612 0.6051 0.6435 -0.0787 -0.0361 0.0225  731  TRP A CD1 
1391 C CD2 . TRP A 194 ? 0.9050 0.7528 0.7839 -0.0729 -0.0249 0.0061  731  TRP A CD2 
1392 N NE1 . TRP A 194 ? 0.8207 0.6519 0.7079 -0.0700 -0.0420 0.0198  731  TRP A NE1 
1393 C CE2 . TRP A 194 ? 0.8635 0.6974 0.7487 -0.0664 -0.0348 0.0098  731  TRP A CE2 
1394 C CE3 . TRP A 194 ? 0.9298 0.7828 0.8063 -0.0707 -0.0174 -0.0034 731  TRP A CE3 
1395 C CZ2 . TRP A 194 ? 0.8768 0.7027 0.7655 -0.0579 -0.0364 0.0038  731  TRP A CZ2 
1396 C CZ3 . TRP A 194 ? 0.8513 0.6963 0.7315 -0.0627 -0.0193 -0.0083 731  TRP A CZ3 
1397 C CH2 . TRP A 194 ? 0.9183 0.7503 0.8044 -0.0563 -0.0282 -0.0049 731  TRP A CH2 
1398 N N   . VAL A 195 ? 0.6287 0.5364 0.4844 -0.1072 -0.0027 0.0121  732  VAL A N   
1399 C CA  . VAL A 195 ? 0.7094 0.6321 0.5592 -0.1119 0.0079  0.0048  732  VAL A CA  
1400 C C   . VAL A 195 ? 0.7211 0.6575 0.5625 -0.1180 0.0070  0.0067  732  VAL A C   
1401 O O   . VAL A 195 ? 0.6459 0.5885 0.4834 -0.1172 0.0130  -0.0023 732  VAL A O   
1402 C CB  . VAL A 195 ? 0.7669 0.6967 0.6168 -0.1173 0.0123  0.0079  732  VAL A CB  
1403 C CG1 . VAL A 195 ? 0.8058 0.7553 0.6480 -0.1242 0.0210  0.0031  732  VAL A CG1 
1404 C CG2 . VAL A 195 ? 0.7228 0.6403 0.5802 -0.1114 0.0167  0.0017  732  VAL A CG2 
1405 N N   . GLU A 196 ? 0.6511 0.5917 0.4902 -0.1243 -0.0014 0.0186  733  GLU A N   
1406 C CA  . GLU A 196 ? 0.7174 0.6699 0.5483 -0.1313 -0.0037 0.0219  733  GLU A CA  
1407 C C   . GLU A 196 ? 0.6854 0.6309 0.5169 -0.1260 -0.0065 0.0172  733  GLU A C   
1408 O O   . GLU A 196 ? 0.7555 0.7096 0.5801 -0.1290 -0.0037 0.0137  733  GLU A O   
1409 C CB  . GLU A 196 ? 0.8156 0.7722 0.6457 -0.1394 -0.0142 0.0368  733  GLU A CB  
1410 C CG  . GLU A 196 ? 0.9220 0.8934 0.7475 -0.1479 -0.0100 0.0420  733  GLU A CG  
1411 C CD  . GLU A 196 ? 1.0678 1.0393 0.8968 -0.1539 -0.0213 0.0576  733  GLU A CD  
1412 O OE1 . GLU A 196 ? 1.0943 1.0545 0.9293 -0.1517 -0.0334 0.0644  733  GLU A OE1 
1413 O OE2 . GLU A 196 ? 1.0975 1.0811 0.9239 -0.1607 -0.0184 0.0631  733  GLU A OE2 
1414 N N   . SER A 197 ? 0.5839 0.5138 0.4239 -0.1179 -0.0119 0.0169  734  SER A N   
1415 C CA  . SER A 197 ? 0.5925 0.5156 0.4346 -0.1119 -0.0139 0.0121  734  SER A CA  
1416 C C   . SER A 197 ? 0.6745 0.6008 0.5145 -0.1078 -0.0034 -0.0006 734  SER A C   
1417 O O   . SER A 197 ? 0.5461 0.4756 0.3832 -0.1073 -0.0029 -0.0040 734  SER A O   
1418 C CB  . SER A 197 ? 0.7347 0.6415 0.5867 -0.1036 -0.0209 0.0135  734  SER A CB  
1419 O OG  . SER A 197 ? 0.8783 0.7792 0.7332 -0.0968 -0.0209 0.0073  734  SER A OG  
1420 N N   . ILE A 198 ? 0.6420 0.5671 0.4841 -0.1049 0.0041  -0.0073 735  ILE A N   
1421 C CA  . ILE A 198 ? 0.5571 0.4859 0.3985 -0.1016 0.0131  -0.0192 735  ILE A CA  
1422 C C   . ILE A 198 ? 0.5434 0.4885 0.3758 -0.1086 0.0178  -0.0216 735  ILE A C   
1423 O O   . ILE A 198 ? 0.5891 0.5381 0.4192 -0.1070 0.0205  -0.0283 735  ILE A O   
1424 C CB  . ILE A 198 ? 0.5332 0.4573 0.3798 -0.0983 0.0193  -0.0255 735  ILE A CB  
1425 C CG1 . ILE A 198 ? 0.5775 0.4846 0.4319 -0.0908 0.0149  -0.0243 735  ILE A CG1 
1426 C CG2 . ILE A 198 ? 0.5876 0.5170 0.4343 -0.0962 0.0273  -0.0376 735  ILE A CG2 
1427 C CD1 . ILE A 198 ? 0.5367 0.4370 0.3960 -0.0892 0.0185  -0.0266 735  ILE A CD1 
1428 N N   . ALA A 199 ? 0.5698 0.5246 0.3972 -0.1164 0.0185  -0.0159 736  ALA A N   
1429 C CA  . ALA A 199 ? 0.5886 0.5600 0.4063 -0.1237 0.0228  -0.0176 736  ALA A CA  
1430 C C   . ALA A 199 ? 0.6421 0.6154 0.4538 -0.1260 0.0175  -0.0143 736  ALA A C   
1431 O O   . ALA A 199 ? 0.6282 0.6093 0.4343 -0.1268 0.0213  -0.0208 736  ALA A O   
1432 C CB  . ALA A 199 ? 0.5766 0.5582 0.3901 -0.1320 0.0231  -0.0097 736  ALA A CB  
1433 N N   . LYS A 200 ? 0.6019 0.5676 0.4159 -0.1270 0.0079  -0.0042 737  LYS A N   
1434 C CA  . LYS A 200 ? 0.6507 0.6167 0.4607 -0.1300 0.0013  0.0003  737  LYS A CA  
1435 C C   . LYS A 200 ? 0.7229 0.6834 0.5354 -0.1226 0.0032  -0.0082 737  LYS A C   
1436 O O   . LYS A 200 ? 0.6699 0.6357 0.4760 -0.1253 0.0030  -0.0095 737  LYS A O   
1437 C CB  . LYS A 200 ? 0.7132 0.6702 0.5286 -0.1313 -0.0103 0.0117  737  LYS A CB  
1438 C CG  . LYS A 200 ? 0.7561 0.7128 0.5682 -0.1356 -0.0181 0.0174  737  LYS A CG  
1439 C CD  . LYS A 200 ? 0.7834 0.7322 0.6023 -0.1378 -0.0307 0.0287  737  LYS A CD  
1440 C CE  . LYS A 200 ? 0.8801 0.8300 0.6955 -0.1445 -0.0391 0.0354  737  LYS A CE  
1441 N NZ  . LYS A 200 ? 0.9119 0.8573 0.7333 -0.1496 -0.0525 0.0476  737  LYS A NZ  
1442 N N   . ILE A 201 ? 0.5635 0.5134 0.3851 -0.1135 0.0047  -0.0135 738  ILE A N   
1443 C CA  . ILE A 201 ? 0.5699 0.5156 0.3949 -0.1065 0.0066  -0.0213 738  ILE A CA  
1444 C C   . ILE A 201 ? 0.5119 0.4682 0.3316 -0.1073 0.0145  -0.0307 738  ILE A C   
1445 O O   . ILE A 201 ? 0.5510 0.5094 0.3684 -0.1062 0.0143  -0.0340 738  ILE A O   
1446 C CB  . ILE A 201 ? 0.5571 0.4908 0.3924 -0.0972 0.0072  -0.0253 738  ILE A CB  
1447 C CG1 . ILE A 201 ? 0.5512 0.4742 0.3924 -0.0951 -0.0015 -0.0171 738  ILE A CG1 
1448 C CG2 . ILE A 201 ? 0.5236 0.4555 0.3624 -0.0906 0.0099  -0.0334 738  ILE A CG2 
1449 C CD1 . ILE A 201 ? 0.6337 0.5452 0.4835 -0.0868 -0.0010 -0.0204 738  ILE A CD1 
1450 N N   . ILE A 202 ? 0.5414 0.5041 0.3600 -0.1092 0.0210  -0.0351 739  ILE A N   
1451 C CA  . ILE A 202 ? 0.5729 0.5459 0.3878 -0.1097 0.0281  -0.0452 739  ILE A CA  
1452 C C   . ILE A 202 ? 0.6956 0.6803 0.4991 -0.1168 0.0274  -0.0432 739  ILE A C   
1453 O O   . ILE A 202 ? 0.6691 0.6589 0.4696 -0.1155 0.0293  -0.0501 739  ILE A O   
1454 C CB  . ILE A 202 ? 0.5827 0.5604 0.4000 -0.1108 0.0349  -0.0502 739  ILE A CB  
1455 C CG1 . ILE A 202 ? 0.5594 0.5244 0.3877 -0.1037 0.0355  -0.0533 739  ILE A CG1 
1456 C CG2 . ILE A 202 ? 0.6806 0.6707 0.4944 -0.1120 0.0414  -0.0610 739  ILE A CG2 
1457 C CD1 . ILE A 202 ? 0.5168 0.4837 0.3491 -0.1044 0.0415  -0.0581 739  ILE A CD1 
1458 N N   . ARG A 203 ? 0.7480 0.7366 0.5452 -0.1244 0.0239  -0.0333 740  ARG A N   
1459 C CA  . ARG A 203 ? 0.7867 0.7854 0.5721 -0.1322 0.0222  -0.0298 740  ARG A CA  
1460 C C   . ARG A 203 ? 0.8523 0.8450 0.6367 -0.1300 0.0166  -0.0289 740  ARG A C   
1461 O O   . ARG A 203 ? 0.8531 0.8525 0.6303 -0.1314 0.0182  -0.0336 740  ARG A O   
1462 C CB  . ARG A 203 ? 0.8302 0.8324 0.6108 -0.1410 0.0173  -0.0174 740  ARG A CB  
1463 C CG  . ARG A 203 ? 0.9395 0.9550 0.7153 -0.1470 0.0234  -0.0175 740  ARG A CG  
1464 C CD  . ARG A 203 ? 0.9655 0.9881 0.7340 -0.1577 0.0178  -0.0046 740  ARG A CD  
1465 N NE  . ARG A 203 ? 0.9570 0.9674 0.7332 -0.1575 0.0081  0.0064  740  ARG A NE  
1466 C CZ  . ARG A 203 ? 0.9261 0.9325 0.7097 -0.1564 0.0070  0.0110  740  ARG A CZ  
1467 N NH1 . ARG A 203 ? 0.8701 0.8833 0.6547 -0.1557 0.0153  0.0059  740  ARG A NH1 
1468 N NH2 . ARG A 203 ? 0.9763 0.9716 0.7672 -0.1558 -0.0031 0.0205  740  ARG A NH2 
1469 N N   . ARG A 204 ? 0.7333 0.7132 0.5253 -0.1264 0.0098  -0.0228 741  ARG A N   
1470 C CA  . ARG A 204 ? 0.7544 0.7274 0.5475 -0.1240 0.0041  -0.0211 741  ARG A CA  
1471 C C   . ARG A 204 ? 0.8702 0.8427 0.6664 -0.1166 0.0083  -0.0315 741  ARG A C   
1472 O O   . ARG A 204 ? 0.9451 0.9187 0.7372 -0.1170 0.0060  -0.0324 741  ARG A O   
1473 C CB  . ARG A 204 ? 0.7420 0.7018 0.5449 -0.1204 -0.0034 -0.0141 741  ARG A CB  
1474 C CG  . ARG A 204 ? 0.6871 0.6383 0.4963 -0.1138 -0.0067 -0.0158 741  ARG A CG  
1475 C CD  . ARG A 204 ? 0.7322 0.6722 0.5501 -0.1119 -0.0152 -0.0081 741  ARG A CD  
1476 N NE  . ARG A 204 ? 0.7911 0.7260 0.6160 -0.1086 -0.0153 -0.0070 741  ARG A NE  
1477 C CZ  . ARG A 204 ? 0.8199 0.7477 0.6540 -0.0994 -0.0127 -0.0123 741  ARG A CZ  
1478 N NH1 . ARG A 204 ? 0.7409 0.6670 0.5786 -0.0928 -0.0097 -0.0188 741  ARG A NH1 
1479 N NH2 . ARG A 204 ? 0.7298 0.6523 0.5691 -0.0970 -0.0136 -0.0107 741  ARG A NH2 
1480 N N   . LYS A 205 ? 0.7463 0.7170 0.5502 -0.1101 0.0135  -0.0390 742  LYS A N   
1481 C CA  . LYS A 205 ? 0.7021 0.6730 0.5106 -0.1034 0.0166  -0.0486 742  LYS A CA  
1482 C C   . LYS A 205 ? 0.7785 0.7615 0.5788 -0.1065 0.0205  -0.0558 742  LYS A C   
1483 O O   . LYS A 205 ? 0.8220 0.8056 0.6222 -0.1035 0.0190  -0.0598 742  LYS A O   
1484 C CB  . LYS A 205 ? 0.6829 0.6495 0.5012 -0.0972 0.0210  -0.0547 742  LYS A CB  
1485 C CG  . LYS A 205 ? 0.6588 0.6131 0.4859 -0.0923 0.0173  -0.0496 742  LYS A CG  
1486 C CD  . LYS A 205 ? 0.6852 0.6333 0.5178 -0.0864 0.0134  -0.0495 742  LYS A CD  
1487 C CE  . LYS A 205 ? 0.6238 0.5608 0.4647 -0.0815 0.0099  -0.0450 742  LYS A CE  
1488 N NZ  . LYS A 205 ? 0.5634 0.4955 0.4104 -0.0756 0.0068  -0.0449 742  LYS A NZ  
1489 N N   . LYS A 206 ? 0.8888 0.8816 0.6827 -0.1121 0.0252  -0.0574 743  LYS A N   
1490 C CA  . LYS A 206 ? 0.9658 0.9715 0.7521 -0.1148 0.0296  -0.0655 743  LYS A CA  
1491 C C   . LYS A 206 ? 1.0807 1.0900 0.8559 -0.1194 0.0253  -0.0618 743  LYS A C   
1492 O O   . LYS A 206 ? 1.1000 1.1148 0.8716 -0.1180 0.0260  -0.0692 743  LYS A O   
1493 C CB  . LYS A 206 ? 0.9334 0.9497 0.7154 -0.1203 0.0357  -0.0671 743  LYS A CB  
1494 C CG  . LYS A 206 ? 0.9165 0.9344 0.7079 -0.1159 0.0419  -0.0768 743  LYS A CG  
1495 C CD  . LYS A 206 ? 0.9661 0.9976 0.7521 -0.1217 0.0485  -0.0802 743  LYS A CD  
1496 C CE  . LYS A 206 ? 0.9477 0.9769 0.7441 -0.1190 0.0534  -0.0849 743  LYS A CE  
1497 N NZ  . LYS A 206 ? 0.9523 0.9948 0.7446 -0.1248 0.0598  -0.0868 743  LYS A NZ  
1498 N N   . GLN A 207 ? 1.1091 1.1147 0.8791 -0.1251 0.0202  -0.0505 744  GLN A N   
1499 C CA  . GLN A 207 ? 1.1392 1.1466 0.8984 -0.1307 0.0152  -0.0455 744  GLN A CA  
1500 C C   . GLN A 207 ? 1.1893 1.1886 0.9525 -0.1247 0.0106  -0.0474 744  GLN A C   
1501 O O   . GLN A 207 ? 1.2989 1.3028 1.0548 -0.1254 0.0101  -0.0516 744  GLN A O   
1502 C CB  . GLN A 207 ? 1.1134 1.1167 0.8693 -0.1381 0.0090  -0.0322 744  GLN A CB  
1503 C CG  . GLN A 207 ? 1.1793 1.1939 0.9273 -0.1469 0.0121  -0.0283 744  GLN A CG  
1504 C CD  . GLN A 207 ? 1.2252 1.2423 0.9622 -0.1576 0.0056  -0.0174 744  GLN A CD  
1505 O OE1 . GLN A 207 ? 1.2808 1.2872 1.0213 -0.1590 -0.0029 -0.0085 744  GLN A OE1 
1506 N NE2 . GLN A 207 ? 1.1530 1.1847 0.8769 -0.1655 0.0095  -0.0183 744  GLN A NE2 
1507 N N   . ALA A 208 ? 1.0384 1.0257 0.8132 -0.1187 0.0071  -0.0442 745  ALA A N   
1508 C CA  . ALA A 208 ? 0.9902 0.9692 0.7704 -0.1129 0.0022  -0.0441 745  ALA A CA  
1509 C C   . ALA A 208 ? 0.9869 0.9713 0.7677 -0.1079 0.0047  -0.0547 745  ALA A C   
1510 O O   . ALA A 208 ? 1.0188 1.0102 0.8020 -0.1055 0.0107  -0.0637 745  ALA A O   
1511 C CB  . ALA A 208 ? 0.8729 0.8411 0.6669 -0.1061 0.0003  -0.0414 745  ALA A CB  
1512 N N   . ILE A 217 ? 1.0552 0.9238 0.8815 -0.1124 -0.0814 0.0315  754  ILE A N   
1513 C CA  . ILE A 217 ? 1.0268 0.8886 0.8718 -0.1045 -0.0834 0.0338  754  ILE A CA  
1514 C C   . ILE A 217 ? 0.9396 0.7885 0.7913 -0.1104 -0.0936 0.0437  754  ILE A C   
1515 O O   . ILE A 217 ? 0.9108 0.7523 0.7558 -0.1168 -0.1004 0.0496  754  ILE A O   
1516 C CB  . ILE A 217 ? 1.0242 0.8863 0.8754 -0.0952 -0.0821 0.0310  754  ILE A CB  
1517 C CG1 . ILE A 217 ? 1.0185 0.8931 0.8680 -0.0884 -0.0728 0.0209  754  ILE A CG1 
1518 C CG2 . ILE A 217 ? 0.9867 0.8416 0.8568 -0.0884 -0.0854 0.0352  754  ILE A CG2 
1519 C CD1 . ILE A 217 ? 1.0352 0.9118 0.8905 -0.0801 -0.0725 0.0182  754  ILE A CD1 
1520 N N   . THR A 218 ? 0.9178 0.7637 0.7831 -0.1084 -0.0950 0.0454  755  THR A N   
1521 C CA  . THR A 218 ? 0.9810 0.8151 0.8552 -0.1140 -0.1053 0.0542  755  THR A CA  
1522 C C   . THR A 218 ? 0.9334 0.7615 0.8283 -0.1049 -0.1071 0.0551  755  THR A C   
1523 O O   . THR A 218 ? 0.8637 0.6982 0.7669 -0.0947 -0.0999 0.0488  755  THR A O   
1524 C CB  . THR A 218 ? 0.9714 0.8062 0.8444 -0.1219 -0.1085 0.0566  755  THR A CB  
1525 O OG1 . THR A 218 ? 0.9520 0.7925 0.8346 -0.1139 -0.1027 0.0508  755  THR A OG1 
1526 C CG2 . THR A 218 ? 0.9950 0.8371 0.8478 -0.1316 -0.1065 0.0563  755  THR A CG2 
1527 N N   . PHE A 219 ? 0.8382 0.6541 0.7415 -0.1090 -0.1169 0.0630  756  PHE A N   
1528 C CA  . PHE A 219 ? 0.8392 0.6492 0.7630 -0.1011 -0.1193 0.0646  756  PHE A CA  
1529 C C   . PHE A 219 ? 0.9016 0.7029 0.8384 -0.1060 -0.1285 0.0696  756  PHE A C   
1530 O O   . PHE A 219 ? 0.7779 0.5708 0.7103 -0.1173 -0.1378 0.0768  756  PHE A O   
1531 C CB  . PHE A 219 ? 0.7852 0.5880 0.7111 -0.0993 -0.1228 0.0692  756  PHE A CB  
1532 C CG  . PHE A 219 ? 0.8514 0.6626 0.7673 -0.0936 -0.1154 0.0642  756  PHE A CG  
1533 C CD1 . PHE A 219 ? 0.8271 0.6473 0.7518 -0.0819 -0.1075 0.0580  756  PHE A CD1 
1534 C CD2 . PHE A 219 ? 0.8115 0.6222 0.7096 -0.1001 -0.1170 0.0654  756  PHE A CD2 
1535 C CE1 . PHE A 219 ? 0.8359 0.6639 0.7529 -0.0771 -0.1021 0.0536  756  PHE A CE1 
1536 C CE2 . PHE A 219 ? 0.8333 0.6518 0.7235 -0.0946 -0.1113 0.0601  756  PHE A CE2 
1537 C CZ  . PHE A 219 ? 0.8008 0.6279 0.7011 -0.0833 -0.1043 0.0544  756  PHE A CZ  
1538 N N   . GLU A 220 ? 0.9680 0.7715 0.9211 -0.0974 -0.1262 0.0657  757  GLU A N   
1539 C CA  . GLU A 220 ? 1.0599 0.8561 1.0283 -0.1002 -0.1351 0.0689  757  GLU A CA  
1540 C C   . GLU A 220 ? 1.0967 0.8801 1.0784 -0.1021 -0.1444 0.0762  757  GLU A C   
1541 O O   . GLU A 220 ? 1.0193 0.7929 1.0081 -0.1105 -0.1556 0.0823  757  GLU A O   
1542 C CB  . GLU A 220 ? 1.0500 0.8529 1.0317 -0.0891 -0.1293 0.0614  757  GLU A CB  
1543 C CG  . GLU A 220 ? 1.0638 0.8625 1.0568 -0.0924 -0.1376 0.0624  757  GLU A CG  
1544 C CD  . GLU A 220 ? 1.1418 0.9341 1.1583 -0.0863 -0.1430 0.0628  757  GLU A CD  
1545 O OE1 . GLU A 220 ? 1.1287 0.9130 1.1561 -0.0924 -0.1545 0.0668  757  GLU A OE1 
1546 O OE2 . GLU A 220 ? 1.1715 0.9675 1.1963 -0.0755 -0.1361 0.0590  757  GLU A OE2 
1547 N N   . SER A 221 ? 1.1000 0.8836 1.0858 -0.0944 -0.1402 0.0760  758  SER A N   
1548 C CA  . SER A 221 ? 1.0932 0.8647 1.0899 -0.0957 -0.1480 0.0834  758  SER A CA  
1549 C C   . SER A 221 ? 1.0262 0.7979 1.0102 -0.0950 -0.1450 0.0854  758  SER A C   
1550 O O   . SER A 221 ? 0.9815 0.7646 0.9571 -0.0883 -0.1352 0.0793  758  SER A O   
1551 C CB  . SER A 221 ? 1.0853 0.8570 1.1057 -0.0848 -0.1470 0.0813  758  SER A CB  
1552 O OG  . SER A 221 ? 1.0456 0.8310 1.0666 -0.0731 -0.1349 0.0730  758  SER A OG  
1553 N N   . PRO A 222 ? 0.9404 0.6990 0.9235 -0.1020 -0.1541 0.0941  759  PRO A N   
1554 C CA  . PRO A 222 ? 0.9239 0.6809 0.8940 -0.1021 -0.1532 0.0966  759  PRO A CA  
1555 C C   . PRO A 222 ? 0.8020 0.5673 0.7792 -0.0889 -0.1453 0.0929  759  PRO A C   
1556 O O   . PRO A 222 ? 0.6696 0.4328 0.6663 -0.0817 -0.1460 0.0945  759  PRO A O   
1557 C CB  . PRO A 222 ? 0.9123 0.6511 0.8875 -0.1102 -0.1658 0.1072  759  PRO A CB  
1558 C CG  . PRO A 222 ? 0.9480 0.6804 0.9297 -0.1192 -0.1736 0.1099  759  PRO A CG  
1559 C CD  . PRO A 222 ? 0.9840 0.7275 0.9784 -0.1105 -0.1668 0.1020  759  PRO A CD  
1560 N N   . PRO A 223 ? 0.7435 0.5188 0.7058 -0.0858 -0.1381 0.0878  760  PRO A N   
1561 C CA  . PRO A 223 ? 0.6291 0.4121 0.5977 -0.0745 -0.1324 0.0853  760  PRO A CA  
1562 C C   . PRO A 223 ? 0.5705 0.3419 0.5459 -0.0738 -0.1402 0.0942  760  PRO A C   
1563 O O   . PRO A 223 ? 0.5814 0.3397 0.5494 -0.0830 -0.1490 0.1010  760  PRO A O   
1564 C CB  . PRO A 223 ? 0.6155 0.4095 0.5652 -0.0743 -0.1257 0.0785  760  PRO A CB  
1565 C CG  . PRO A 223 ? 0.7045 0.4927 0.6364 -0.0864 -0.1302 0.0804  760  PRO A CG  
1566 C CD  . PRO A 223 ? 0.6818 0.4624 0.6217 -0.0929 -0.1355 0.0841  760  PRO A CD  
1567 N N   . PRO A 224 ? 0.5897 0.3657 0.5792 -0.0635 -0.1376 0.0949  761  PRO A N   
1568 C CA  . PRO A 224 ? 0.5522 0.3170 0.5491 -0.0625 -0.1456 0.1042  761  PRO A CA  
1569 C C   . PRO A 224 ? 0.5764 0.3375 0.5552 -0.0662 -0.1494 0.1062  761  PRO A C   
1570 O O   . PRO A 224 ? 0.6054 0.3772 0.5693 -0.0657 -0.1436 0.0989  761  PRO A O   
1571 C CB  . PRO A 224 ? 0.5541 0.3292 0.5685 -0.0501 -0.1402 0.1033  761  PRO A CB  
1572 C CG  . PRO A 224 ? 0.5456 0.3383 0.5545 -0.0452 -0.1291 0.0925  761  PRO A CG  
1573 C CD  . PRO A 224 ? 0.5681 0.3593 0.5677 -0.0528 -0.1279 0.0879  761  PRO A CD  
1574 N N   . PRO A 225 ? 0.6453 0.3909 0.6256 -0.0697 -0.1596 0.1158  762  PRO A N   
1575 C CA  . PRO A 225 ? 0.5935 0.3347 0.5570 -0.0724 -0.1642 0.1177  762  PRO A CA  
1576 C C   . PRO A 225 ? 0.5950 0.3490 0.5594 -0.0622 -0.1596 0.1137  762  PRO A C   
1577 O O   . PRO A 225 ? 0.5355 0.2959 0.5177 -0.0532 -0.1570 0.1150  762  PRO A O   
1578 C CB  . PRO A 225 ? 0.6914 0.4169 0.6625 -0.0757 -0.1746 0.1278  762  PRO A CB  
1579 C CG  . PRO A 225 ? 0.6839 0.4163 0.6806 -0.0691 -0.1713 0.1279  762  PRO A CG  
1580 C CD  . PRO A 225 ? 0.6387 0.3696 0.6370 -0.0711 -0.1677 0.1253  762  PRO A CD  
1581 N N   . ILE A 226 ? 0.5141 0.4081 0.4304 -0.0813 -0.1161 0.0964  763  ILE A N   
1582 C CA  . ILE A 226 ? 0.5253 0.4324 0.4433 -0.0799 -0.1068 0.0872  763  ILE A CA  
1583 C C   . ILE A 226 ? 0.5314 0.4493 0.4615 -0.0769 -0.1136 0.0923  763  ILE A C   
1584 O O   . ILE A 226 ? 0.5065 0.4210 0.4314 -0.0838 -0.1252 0.1023  763  ILE A O   
1585 C CB  . ILE A 226 ? 0.5510 0.4556 0.4451 -0.0936 -0.1005 0.0819  763  ILE A CB  
1586 C CG1 . ILE A 226 ? 0.6131 0.5067 0.4943 -0.0990 -0.0954 0.0789  763  ILE A CG1 
1587 C CG2 . ILE A 226 ? 0.4852 0.4019 0.3830 -0.0908 -0.0901 0.0717  763  ILE A CG2 
1588 C CD1 . ILE A 226 ? 0.4629 0.3590 0.3571 -0.0885 -0.0870 0.0711  763  ILE A CD1 
1589 N N   . GLU A 227 ? 0.4149 0.3453 0.3606 -0.0675 -0.1068 0.0857  764  GLU A N   
1590 C CA  . GLU A 227 ? 0.4443 0.3865 0.4031 -0.0644 -0.1117 0.0894  764  GLU A CA  
1591 C C   . GLU A 227 ? 0.4738 0.4222 0.4203 -0.0725 -0.1072 0.0844  764  GLU A C   
1592 O O   . GLU A 227 ? 0.4280 0.3777 0.3681 -0.0728 -0.0961 0.0745  764  GLU A O   
1593 C CB  . GLU A 227 ? 0.4234 0.3755 0.4073 -0.0496 -0.1069 0.0857  764  GLU A CB  
1594 C CG  . GLU A 227 ? 0.4069 0.3532 0.4060 -0.0403 -0.1106 0.0899  764  GLU A CG  
1595 C CD  . GLU A 227 ? 0.5484 0.4978 0.5639 -0.0376 -0.1232 0.1013  764  GLU A CD  
1596 O OE1 . GLU A 227 ? 0.5100 0.4682 0.5267 -0.0421 -0.1286 0.1055  764  GLU A OE1 
1597 O OE2 . GLU A 227 ? 0.5288 0.4717 0.5568 -0.0308 -0.1278 0.1060  764  GLU A OE2 
1598 N N   . TRP A 228 ? 0.4433 0.3949 0.3872 -0.0792 -0.1162 0.0913  765  TRP A N   
1599 C CA  . TRP A 228 ? 0.4315 0.3878 0.3637 -0.0874 -0.1129 0.0871  765  TRP A CA  
1600 C C   . TRP A 228 ? 0.4172 0.3863 0.3661 -0.0834 -0.1182 0.0910  765  TRP A C   
1601 O O   . TRP A 228 ? 0.4536 0.4261 0.4178 -0.0794 -0.1285 0.1003  765  TRP A O   
1602 C CB  . TRP A 228 ? 0.4983 0.4440 0.4038 -0.1038 -0.1181 0.0908  765  TRP A CB  
1603 C CG  . TRP A 228 ? 0.4762 0.4101 0.3642 -0.1094 -0.1116 0.0864  765  TRP A CG  
1604 C CD1 . TRP A 228 ? 0.4999 0.4227 0.3815 -0.1121 -0.1174 0.0928  765  TRP A CD1 
1605 C CD2 . TRP A 228 ? 0.4962 0.4287 0.3724 -0.1129 -0.0982 0.0748  765  TRP A CD2 
1606 N NE1 . TRP A 228 ? 0.5254 0.4405 0.3914 -0.1177 -0.1079 0.0856  765  TRP A NE1 
1607 C CE2 . TRP A 228 ? 0.4784 0.3999 0.3418 -0.1180 -0.0960 0.0745  765  TRP A CE2 
1608 C CE3 . TRP A 228 ? 0.5234 0.4628 0.3998 -0.1121 -0.0879 0.0648  765  TRP A CE3 
1609 C CZ2 . TRP A 228 ? 0.5558 0.4744 0.4080 -0.1223 -0.0835 0.0643  765  TRP A CZ2 
1610 C CZ3 . TRP A 228 ? 0.5221 0.4580 0.3882 -0.1157 -0.0760 0.0550  765  TRP A CZ3 
1611 C CH2 . TRP A 228 ? 0.5116 0.4378 0.3663 -0.1207 -0.0738 0.0547  765  TRP A CH2 
1612 N N   . HIS A 229 ? 0.4519 0.4280 0.3989 -0.0847 -0.1110 0.0838  766  HIS A N   
1613 C CA  . HIS A 229 ? 0.4308 0.4195 0.3926 -0.0818 -0.1141 0.0861  766  HIS A CA  
1614 C C   . HIS A 229 ? 0.4671 0.4539 0.4102 -0.0957 -0.1173 0.0865  766  HIS A C   
1615 O O   . HIS A 229 ? 0.5092 0.4896 0.4396 -0.1060 -0.1276 0.0943  766  HIS A O   
1616 C CB  . HIS A 229 ? 0.3762 0.3739 0.3525 -0.0708 -0.1027 0.0773  766  HIS A CB  
1617 C CG  . HIS A 229 ? 0.4116 0.4224 0.4028 -0.0681 -0.1042 0.0788  766  HIS A CG  
1618 N ND1 . HIS A 229 ? 0.4069 0.4253 0.4128 -0.0676 -0.1151 0.0884  766  HIS A ND1 
1619 C CD2 . HIS A 229 ? 0.4117 0.4294 0.4059 -0.0663 -0.0965 0.0721  766  HIS A CD2 
1620 C CE1 . HIS A 229 ? 0.4246 0.4547 0.4418 -0.0658 -0.1134 0.0872  766  HIS A CE1 
1621 N NE2 . HIS A 229 ? 0.4228 0.4519 0.4321 -0.0652 -0.1022 0.0775  766  HIS A NE2 
1622 N N   . ILE A 230 ? 0.4249 0.4156 0.3646 -0.0967 -0.1086 0.0782  767  ILE A N   
1623 C CA  . ILE A 230 ? 0.4525 0.4403 0.3742 -0.1100 -0.1106 0.0774  767  ILE A CA  
1624 C C   . ILE A 230 ? 0.5765 0.5508 0.4716 -0.1206 -0.1047 0.0715  767  ILE A C   
1625 O O   . ILE A 230 ? 0.5017 0.4682 0.3772 -0.1340 -0.1111 0.0755  767  ILE A O   
1626 C CB  . ILE A 230 ? 0.4777 0.4739 0.4066 -0.1074 -0.1041 0.0712  767  ILE A CB  
1627 C CG1 . ILE A 230 ? 0.4751 0.4853 0.4290 -0.0993 -0.1101 0.0776  767  ILE A CG1 
1628 C CG2 . ILE A 230 ? 0.5384 0.5291 0.4467 -0.1216 -0.1048 0.0689  767  ILE A CG2 
1629 C CD1 . ILE A 230 ? 0.4854 0.5043 0.4489 -0.0948 -0.1025 0.0714  767  ILE A CD1 
1630 N N   . SER A 231 ? 0.4507 0.4225 0.3452 -0.1153 -0.0924 0.0620  768  SER A N   
1631 C CA  . SER A 231 ? 0.5216 0.4819 0.3946 -0.1241 -0.0855 0.0560  768  SER A CA  
1632 C C   . SER A 231 ? 0.5998 0.5518 0.4639 -0.1288 -0.0931 0.0637  768  SER A C   
1633 O O   . SER A 231 ? 0.6581 0.6125 0.5371 -0.1196 -0.0977 0.0691  768  SER A O   
1634 C CB  . SER A 231 ? 0.5810 0.5423 0.4599 -0.1161 -0.0720 0.0454  768  SER A CB  
1635 O OG  . SER A 231 ? 0.5629 0.5277 0.4431 -0.1157 -0.0644 0.0375  768  SER A OG  
1636 N N   . LYS A 232 ? 0.6287 0.5700 0.4677 -0.1435 -0.0943 0.0641  769  LYS A N   
1637 C CA  . LYS A 232 ? 0.7214 0.6531 0.5484 -0.1503 -0.1024 0.0723  769  LYS A CA  
1638 C C   . LYS A 232 ? 0.6498 0.5724 0.4619 -0.1550 -0.0915 0.0647  769  LYS A C   
1639 O O   . LYS A 232 ? 0.5578 0.4810 0.3656 -0.1561 -0.0787 0.0534  769  LYS A O   
1640 C CB  . LYS A 232 ? 0.8286 0.7544 0.6367 -0.1654 -0.1142 0.0806  769  LYS A CB  
1641 C CG  . LYS A 232 ? 0.8681 0.8039 0.6937 -0.1608 -0.1269 0.0899  769  LYS A CG  
1642 C CD  . LYS A 232 ? 0.8886 0.8310 0.7410 -0.1460 -0.1330 0.0970  769  LYS A CD  
1643 C CE  . LYS A 232 ? 0.9158 0.8691 0.7879 -0.1417 -0.1456 0.1067  769  LYS A CE  
1644 N NZ  . LYS A 232 ? 0.8840 0.8439 0.7843 -0.1264 -0.1495 0.1121  769  LYS A NZ  
1645 N N   . PRO A 233 ? 0.6327 0.5472 0.4389 -0.1574 -0.0964 0.0709  770  PRO A N   
1646 C CA  . PRO A 233 ? 0.5953 0.5019 0.3888 -0.1620 -0.0861 0.0642  770  PRO A CA  
1647 C C   . PRO A 233 ? 0.7495 0.6511 0.5207 -0.1753 -0.0758 0.0550  770  PRO A C   
1648 O O   . PRO A 233 ? 0.6674 0.5640 0.4204 -0.1878 -0.0810 0.0580  770  PRO A O   
1649 C CB  . PRO A 233 ? 0.7267 0.6225 0.5094 -0.1686 -0.0971 0.0754  770  PRO A CB  
1650 C CG  . PRO A 233 ? 0.7012 0.6026 0.5046 -0.1583 -0.1105 0.0861  770  PRO A CG  
1651 C CD  . PRO A 233 ? 0.6322 0.5443 0.4447 -0.1556 -0.1119 0.0847  770  PRO A CD  
1652 N N   . GLY A 234 ? 0.7511 0.6542 0.5247 -0.1726 -0.0612 0.0435  771  GLY A N   
1653 C CA  . GLY A 234 ? 0.7788 0.6774 0.5342 -0.1841 -0.0492 0.0332  771  GLY A CA  
1654 C C   . GLY A 234 ? 0.6470 0.5520 0.4085 -0.1813 -0.0425 0.0249  771  GLY A C   
1655 O O   . GLY A 234 ? 0.8027 0.7060 0.5577 -0.1858 -0.0294 0.0138  771  GLY A O   
1656 N N   . GLN A 235 ? 0.7008 0.6130 0.4759 -0.1739 -0.0511 0.0301  772  GLN A N   
1657 C CA  . GLN A 235 ? 0.6909 0.6081 0.4708 -0.1721 -0.0462 0.0234  772  GLN A CA  
1658 C C   . GLN A 235 ? 0.5973 0.5237 0.4003 -0.1575 -0.0366 0.0152  772  GLN A C   
1659 O O   . GLN A 235 ? 0.6073 0.5418 0.4263 -0.1485 -0.0393 0.0162  772  GLN A O   
1660 C CB  . GLN A 235 ? 0.7454 0.6672 0.5308 -0.1710 -0.0594 0.0326  772  GLN A CB  
1661 C CG  . GLN A 235 ? 0.9401 0.8545 0.7072 -0.1836 -0.0729 0.0436  772  GLN A CG  
1662 C CD  . GLN A 235 ? 1.0431 0.9651 0.8222 -0.1802 -0.0865 0.0532  772  GLN A CD  
1663 O OE1 . GLN A 235 ? 0.9677 0.9009 0.7715 -0.1663 -0.0867 0.0534  772  GLN A OE1 
1664 N NE2 . GLN A 235 ? 1.1684 1.0845 0.9299 -0.1936 -0.0978 0.0612  772  GLN A NE2 
1665 N N   . PHE A 236 ? 0.5969 0.5223 0.4019 -0.1556 -0.0257 0.0076  773  PHE A N   
1666 C CA  . PHE A 236 ? 0.6060 0.5404 0.4341 -0.1414 -0.0192 0.0021  773  PHE A CA  
1667 C C   . PHE A 236 ? 0.6867 0.6253 0.5229 -0.1377 -0.0130 -0.0053 773  PHE A C   
1668 O O   . PHE A 236 ? 0.5836 0.5300 0.4393 -0.1256 -0.0110 -0.0074 773  PHE A O   
1669 C CB  . PHE A 236 ? 0.6401 0.5731 0.4691 -0.1413 -0.0096 -0.0042 773  PHE A CB  
1670 C CG  . PHE A 236 ? 0.8063 0.7337 0.6214 -0.1520 0.0024  -0.0140 773  PHE A CG  
1671 C CD1 . PHE A 236 ? 0.8174 0.7484 0.6423 -0.1482 0.0128  -0.0241 773  PHE A CD1 
1672 C CD2 . PHE A 236 ? 0.8564 0.7743 0.6490 -0.1661 0.0038  -0.0132 773  PHE A CD2 
1673 C CE1 . PHE A 236 ? 0.8176 0.7435 0.6318 -0.1575 0.0251  -0.0341 773  PHE A CE1 
1674 C CE2 . PHE A 236 ? 0.8501 0.7629 0.6298 -0.1765 0.0165  -0.0233 773  PHE A CE2 
1675 C CZ  . PHE A 236 ? 0.8596 0.7766 0.6510 -0.1718 0.0276  -0.0341 773  PHE A CZ  
1676 N N   . GLU A 237 ? 0.7060 0.6385 0.5262 -0.1485 -0.0105 -0.0089 774  GLU A N   
1677 C CA  . GLU A 237 ? 0.6457 0.5800 0.4719 -0.1461 -0.0050 -0.0157 774  GLU A CA  
1678 C C   . GLU A 237 ? 0.5848 0.5264 0.4240 -0.1383 -0.0145 -0.0089 774  GLU A C   
1679 O O   . GLU A 237 ? 0.6072 0.5525 0.4578 -0.1322 -0.0109 -0.0132 774  GLU A O   
1680 C CB  . GLU A 237 ? 0.8114 0.7356 0.6151 -0.1610 -0.0002 -0.0213 774  GLU A CB  
1681 C CG  . GLU A 237 ? 0.9684 0.8850 0.7572 -0.1706 0.0107  -0.0290 774  GLU A CG  
1682 C CD  . GLU A 237 ? 1.1605 1.0710 0.9300 -0.1811 0.0038  -0.0213 774  GLU A CD  
1683 O OE1 . GLU A 237 ? 1.2694 1.1737 1.0257 -0.1898 0.0122  -0.0264 774  GLU A OE1 
1684 O OE2 . GLU A 237 ? 1.1486 1.0604 0.9168 -0.1809 -0.0102 -0.0098 774  GLU A OE2 
1685 N N   . THR A 238 ? 0.5299 0.4735 0.3681 -0.1388 -0.0265 0.0018  775  THR A N   
1686 C CA  . THR A 238 ? 0.6348 0.5862 0.4856 -0.1326 -0.0356 0.0088  775  THR A CA  
1687 C C   . THR A 238 ? 0.5472 0.5080 0.4201 -0.1180 -0.0379 0.0125  775  THR A C   
1688 O O   . THR A 238 ? 0.5284 0.4970 0.4145 -0.1115 -0.0434 0.0172  775  THR A O   
1689 C CB  . THR A 238 ? 0.6411 0.5903 0.4806 -0.1416 -0.0483 0.0190  775  THR A CB  
1690 O OG1 . THR A 238 ? 0.6096 0.5587 0.4508 -0.1395 -0.0550 0.0266  775  THR A OG1 
1691 C CG2 . THR A 238 ? 0.6717 0.6099 0.4852 -0.1581 -0.0465 0.0155  775  THR A CG2 
1692 N N   . PHE A 239 ? 0.4936 0.4534 0.3697 -0.1136 -0.0333 0.0101  776  PHE A N   
1693 C CA  . PHE A 239 ? 0.4575 0.4242 0.3516 -0.1010 -0.0350 0.0130  776  PHE A CA  
1694 C C   . PHE A 239 ? 0.4815 0.4559 0.3917 -0.0914 -0.0317 0.0097  776  PHE A C   
1695 O O   . PHE A 239 ? 0.4338 0.4073 0.3440 -0.0917 -0.0241 0.0023  776  PHE A O   
1696 C CB  . PHE A 239 ? 0.4387 0.4022 0.3324 -0.0993 -0.0293 0.0092  776  PHE A CB  
1697 C CG  . PHE A 239 ? 0.4479 0.4040 0.3281 -0.1070 -0.0339 0.0144  776  PHE A CG  
1698 C CD1 . PHE A 239 ? 0.4770 0.4292 0.3457 -0.1153 -0.0431 0.0220  776  PHE A CD1 
1699 C CD2 . PHE A 239 ? 0.4584 0.4113 0.3376 -0.1065 -0.0296 0.0120  776  PHE A CD2 
1700 C CE1 . PHE A 239 ? 0.4666 0.4109 0.3221 -0.1229 -0.0483 0.0277  776  PHE A CE1 
1701 C CE2 . PHE A 239 ? 0.5206 0.4656 0.3866 -0.1142 -0.0340 0.0172  776  PHE A CE2 
1702 C CZ  . PHE A 239 ? 0.4568 0.3971 0.3105 -0.1225 -0.0434 0.0252  776  PHE A CZ  
1703 N N   . ASP A 240 ? 0.4583 0.4400 0.3822 -0.0830 -0.0372 0.0153  777  ASP A N   
1704 C CA  . ASP A 240 ? 0.4232 0.4120 0.3614 -0.0741 -0.0343 0.0131  777  ASP A CA  
1705 C C   . ASP A 240 ? 0.3792 0.3746 0.3309 -0.0653 -0.0391 0.0189  777  ASP A C   
1706 O O   . ASP A 240 ? 0.4104 0.4048 0.3614 -0.0662 -0.0453 0.0249  777  ASP A O   
1707 C CB  . ASP A 240 ? 0.5103 0.5007 0.4471 -0.0780 -0.0349 0.0125  777  ASP A CB  
1708 C CG  . ASP A 240 ? 0.7101 0.7042 0.6571 -0.0712 -0.0294 0.0079  777  ASP A CG  
1709 O OD1 . ASP A 240 ? 0.6232 0.6188 0.5779 -0.0639 -0.0254 0.0050  777  ASP A OD1 
1710 O OD2 . ASP A 240 ? 0.7232 0.7182 0.6700 -0.0739 -0.0298 0.0076  777  ASP A OD2 
1711 N N   . LEU A 241 ? 0.3370 0.3382 0.3006 -0.0570 -0.0361 0.0170  778  LEU A N   
1712 C CA  . LEU A 241 ? 0.2748 0.2819 0.2511 -0.0485 -0.0385 0.0209  778  LEU A CA  
1713 C C   . LEU A 241 ? 0.3391 0.3507 0.3205 -0.0495 -0.0464 0.0287  778  LEU A C   
1714 O O   . LEU A 241 ? 0.3548 0.3675 0.3434 -0.0449 -0.0498 0.0328  778  LEU A O   
1715 C CB  . LEU A 241 ? 0.2803 0.2931 0.2661 -0.0419 -0.0343 0.0180  778  LEU A CB  
1716 C CG  . LEU A 241 ? 0.3768 0.3961 0.3750 -0.0341 -0.0354 0.0211  778  LEU A CG  
1717 C CD1 . LEU A 241 ? 0.3445 0.3600 0.3438 -0.0291 -0.0335 0.0194  778  LEU A CD1 
1718 C CD2 . LEU A 241 ? 0.4477 0.4727 0.4523 -0.0305 -0.0319 0.0193  778  LEU A CD2 
1719 N N   . MET A 242 ? 0.3573 0.3713 0.3360 -0.0555 -0.0495 0.0309  779  MET A N   
1720 C CA  . MET A 242 ? 0.3116 0.3323 0.2987 -0.0559 -0.0574 0.0386  779  MET A CA  
1721 C C   . MET A 242 ? 0.3697 0.3854 0.3470 -0.0644 -0.0656 0.0444  779  MET A C   
1722 O O   . MET A 242 ? 0.4007 0.4215 0.3866 -0.0642 -0.0738 0.0521  779  MET A O   
1723 C CB  . MET A 242 ? 0.3295 0.3569 0.3208 -0.0580 -0.0574 0.0388  779  MET A CB  
1724 C CG  . MET A 242 ? 0.3553 0.3887 0.3575 -0.0499 -0.0508 0.0351  779  MET A CG  
1725 S SD  . MET A 242 ? 0.4071 0.4500 0.4288 -0.0395 -0.0514 0.0390  779  MET A SD  
1726 C CE  . MET A 242 ? 0.3907 0.4451 0.4240 -0.0426 -0.0576 0.0457  779  MET A CE  
1727 N N   . THR A 243 ? 0.3562 0.3620 0.3160 -0.0720 -0.0635 0.0409  780  THR A N   
1728 C CA  . THR A 243 ? 0.3650 0.3643 0.3117 -0.0819 -0.0712 0.0464  780  THR A CA  
1729 C C   . THR A 243 ? 0.3873 0.3802 0.3312 -0.0803 -0.0730 0.0488  780  THR A C   
1730 O O   . THR A 243 ? 0.4169 0.4057 0.3548 -0.0860 -0.0816 0.0561  780  THR A O   
1731 C CB  . THR A 243 ? 0.4230 0.4141 0.3492 -0.0936 -0.0679 0.0413  780  THR A CB  
1732 O OG1 . THR A 243 ? 0.4922 0.4783 0.4136 -0.0918 -0.0573 0.0323  780  THR A OG1 
1733 C CG2 . THR A 243 ? 0.4742 0.4699 0.4017 -0.0969 -0.0681 0.0402  780  THR A CG2 
1734 N N   . LEU A 244 ? 0.3286 0.3201 0.2764 -0.0732 -0.0653 0.0431  781  LEU A N   
1735 C CA  . LEU A 244 ? 0.3480 0.3337 0.2955 -0.0707 -0.0670 0.0454  781  LEU A CA  
1736 C C   . LEU A 244 ? 0.3480 0.3396 0.3142 -0.0611 -0.0725 0.0517  781  LEU A C   
1737 O O   . LEU A 244 ? 0.3838 0.3851 0.3640 -0.0556 -0.0727 0.0525  781  LEU A O   
1738 C CB  . LEU A 244 ? 0.3438 0.3261 0.2893 -0.0671 -0.0573 0.0371  781  LEU A CB  
1739 C CG  . LEU A 244 ? 0.3655 0.3412 0.2942 -0.0764 -0.0512 0.0309  781  LEU A CG  
1740 C CD1 . LEU A 244 ? 0.3782 0.3542 0.3107 -0.0713 -0.0416 0.0225  781  LEU A CD1 
1741 C CD2 . LEU A 244 ? 0.3688 0.3348 0.2816 -0.0861 -0.0555 0.0350  781  LEU A CD2 
1742 N N   . HIS A 245 ? 0.3169 0.3024 0.2838 -0.0595 -0.0767 0.0560  782  HIS A N   
1743 C CA  . HIS A 245 ? 0.3653 0.3552 0.3514 -0.0497 -0.0810 0.0611  782  HIS A CA  
1744 C C   . HIS A 245 ? 0.3753 0.3672 0.3713 -0.0393 -0.0720 0.0541  782  HIS A C   
1745 O O   . HIS A 245 ? 0.3306 0.3154 0.3178 -0.0399 -0.0667 0.0489  782  HIS A O   
1746 C CB  . HIS A 245 ? 0.3594 0.3405 0.3428 -0.0522 -0.0900 0.0692  782  HIS A CB  
1747 C CG  . HIS A 245 ? 0.3881 0.3741 0.3928 -0.0437 -0.0969 0.0764  782  HIS A CG  
1748 N ND1 . HIS A 245 ? 0.3301 0.3200 0.3524 -0.0316 -0.0914 0.0730  782  HIS A ND1 
1749 C CD2 . HIS A 245 ? 0.3896 0.3778 0.4021 -0.0456 -0.1086 0.0867  782  HIS A CD2 
1750 C CE1 . HIS A 245 ? 0.3196 0.3138 0.3605 -0.0259 -0.0985 0.0802  782  HIS A CE1 
1751 N NE2 . HIS A 245 ? 0.3705 0.3642 0.4070 -0.0339 -0.1097 0.0891  782  HIS A NE2 
1752 N N   . PRO A 246 ? 0.3339 0.3353 0.3476 -0.0305 -0.0702 0.0538  783  PRO A N   
1753 C CA  . PRO A 246 ? 0.2993 0.3019 0.3195 -0.0221 -0.0614 0.0468  783  PRO A CA  
1754 C C   . PRO A 246 ? 0.3170 0.3101 0.3371 -0.0181 -0.0608 0.0462  783  PRO A C   
1755 O O   . PRO A 246 ? 0.3100 0.2996 0.3256 -0.0159 -0.0540 0.0395  783  PRO A O   
1756 C CB  . PRO A 246 ? 0.3103 0.3243 0.3494 -0.0147 -0.0607 0.0482  783  PRO A CB  
1757 C CG  . PRO A 246 ? 0.3307 0.3483 0.3778 -0.0172 -0.0708 0.0574  783  PRO A CG  
1758 C CD  . PRO A 246 ? 0.2976 0.3092 0.3258 -0.0287 -0.0757 0.0597  783  PRO A CD  
1759 N N   . ILE A 247 ? 0.2845 0.2730 0.3095 -0.0175 -0.0685 0.0533  784  ILE A N   
1760 C CA  . ILE A 247 ? 0.2764 0.2538 0.2996 -0.0149 -0.0685 0.0531  784  ILE A CA  
1761 C C   . ILE A 247 ? 0.2835 0.2521 0.2871 -0.0228 -0.0658 0.0493  784  ILE A C   
1762 O O   . ILE A 247 ? 0.3364 0.2993 0.3368 -0.0204 -0.0603 0.0439  784  ILE A O   
1763 C CB  . ILE A 247 ? 0.3659 0.3379 0.3959 -0.0145 -0.0787 0.0627  784  ILE A CB  
1764 C CG1 . ILE A 247 ? 0.3684 0.3498 0.4221 -0.0054 -0.0808 0.0661  784  ILE A CG1 
1765 C CG2 . ILE A 247 ? 0.4333 0.3915 0.4586 -0.0132 -0.0787 0.0623  784  ILE A CG2 
1766 C CD1 . ILE A 247 ? 0.3471 0.3246 0.4110 -0.0045 -0.0924 0.0768  784  ILE A CD1 
1767 N N   . GLU A 248 ? 0.3144 0.2819 0.3049 -0.0327 -0.0692 0.0519  785  GLU A N   
1768 C CA  . GLU A 248 ? 0.2954 0.2544 0.2679 -0.0412 -0.0665 0.0487  785  GLU A CA  
1769 C C   . GLU A 248 ? 0.3119 0.2753 0.2810 -0.0409 -0.0566 0.0392  785  GLU A C   
1770 O O   . GLU A 248 ? 0.3214 0.2794 0.2826 -0.0436 -0.0520 0.0346  785  GLU A O   
1771 C CB  . GLU A 248 ? 0.3582 0.3133 0.3160 -0.0529 -0.0726 0.0541  785  GLU A CB  
1772 C CG  . GLU A 248 ? 0.3864 0.3300 0.3269 -0.0617 -0.0718 0.0537  785  GLU A CG  
1773 C CD  . GLU A 248 ? 0.3939 0.3281 0.3380 -0.0580 -0.0757 0.0577  785  GLU A CD  
1774 O OE1 . GLU A 248 ? 0.3961 0.3246 0.3349 -0.0586 -0.0701 0.0528  785  GLU A OE1 
1775 O OE2 . GLU A 248 ? 0.4258 0.3581 0.3788 -0.0545 -0.0845 0.0660  785  GLU A OE2 
1776 N N   . ILE A 249 ? 0.3129 0.2860 0.2885 -0.0380 -0.0538 0.0365  786  ILE A N   
1777 C CA  . ILE A 249 ? 0.2986 0.2756 0.2738 -0.0362 -0.0454 0.0283  786  ILE A CA  
1778 C C   . ILE A 249 ? 0.3163 0.2906 0.2969 -0.0293 -0.0416 0.0245  786  ILE A C   
1779 O O   . ILE A 249 ? 0.3115 0.2829 0.2866 -0.0310 -0.0369 0.0192  786  ILE A O   
1780 C CB  . ILE A 249 ? 0.2582 0.2452 0.2412 -0.0330 -0.0437 0.0271  786  ILE A CB  
1781 C CG1 . ILE A 249 ? 0.3178 0.3061 0.2928 -0.0414 -0.0463 0.0291  786  ILE A CG1 
1782 C CG2 . ILE A 249 ? 0.2569 0.2470 0.2416 -0.0295 -0.0362 0.0196  786  ILE A CG2 
1783 C CD1 . ILE A 249 ? 0.3399 0.3373 0.3223 -0.0394 -0.0460 0.0291  786  ILE A CD1 
1784 N N   . ALA A 250 ? 0.2937 0.2691 0.2854 -0.0218 -0.0434 0.0268  787  ALA A N   
1785 C CA  . ALA A 250 ? 0.3194 0.2911 0.3151 -0.0156 -0.0395 0.0228  787  ALA A CA  
1786 C C   . ALA A 250 ? 0.2977 0.2583 0.2851 -0.0192 -0.0407 0.0229  787  ALA A C   
1787 O O   . ALA A 250 ? 0.3130 0.2704 0.2970 -0.0190 -0.0364 0.0176  787  ALA A O   
1788 C CB  . ALA A 250 ? 0.2660 0.2401 0.2754 -0.0073 -0.0405 0.0250  787  ALA A CB  
1789 N N   . ARG A 251 ? 0.3344 0.2889 0.3179 -0.0234 -0.0470 0.0293  788  ARG A N   
1790 C CA  . ARG A 251 ? 0.3030 0.2461 0.2774 -0.0281 -0.0484 0.0302  788  ARG A CA  
1791 C C   . ARG A 251 ? 0.3360 0.2787 0.2986 -0.0358 -0.0435 0.0251  788  ARG A C   
1792 O O   . ARG A 251 ? 0.3346 0.2722 0.2939 -0.0368 -0.0404 0.0214  788  ARG A O   
1793 C CB  . ARG A 251 ? 0.3089 0.2452 0.2793 -0.0328 -0.0569 0.0391  788  ARG A CB  
1794 C CG  . ARG A 251 ? 0.3655 0.2992 0.3494 -0.0250 -0.0625 0.0448  788  ARG A CG  
1795 C CD  . ARG A 251 ? 0.3759 0.3039 0.3553 -0.0310 -0.0725 0.0547  788  ARG A CD  
1796 N NE  . ARG A 251 ? 0.4079 0.3336 0.4027 -0.0235 -0.0791 0.0613  788  ARG A NE  
1797 C CZ  . ARG A 251 ? 0.4422 0.3644 0.4378 -0.0269 -0.0896 0.0714  788  ARG A CZ  
1798 N NH1 . ARG A 251 ? 0.3805 0.3004 0.3594 -0.0386 -0.0942 0.0755  788  ARG A NH1 
1799 N NH2 . ARG A 251 ? 0.4080 0.3285 0.4210 -0.0189 -0.0956 0.0773  788  ARG A NH2 
1800 N N   . GLN A 252 ? 0.3363 0.2844 0.2934 -0.0416 -0.0427 0.0248  789  GLN A N   
1801 C CA  . GLN A 252 ? 0.3335 0.2810 0.2807 -0.0493 -0.0376 0.0200  789  GLN A CA  
1802 C C   . GLN A 252 ? 0.3817 0.3351 0.3351 -0.0450 -0.0310 0.0124  789  GLN A C   
1803 O O   . GLN A 252 ? 0.3082 0.2598 0.2581 -0.0486 -0.0270 0.0081  789  GLN A O   
1804 C CB  . GLN A 252 ? 0.2960 0.2464 0.2352 -0.0568 -0.0377 0.0208  789  GLN A CB  
1805 C CG  . GLN A 252 ? 0.3311 0.2743 0.2602 -0.0642 -0.0451 0.0288  789  GLN A CG  
1806 C CD  . GLN A 252 ? 0.4490 0.3814 0.3682 -0.0702 -0.0462 0.0307  789  GLN A CD  
1807 O OE1 . GLN A 252 ? 0.3952 0.3261 0.3083 -0.0751 -0.0398 0.0252  789  GLN A OE1 
1808 N NE2 . GLN A 252 ? 0.4061 0.3308 0.3248 -0.0698 -0.0545 0.0389  789  GLN A NE2 
1809 N N   . LEU A 253 ? 0.3169 0.2775 0.2797 -0.0377 -0.0302 0.0111  790  LEU A N   
1810 C CA  . LEU A 253 ? 0.3044 0.2697 0.2725 -0.0336 -0.0253 0.0050  790  LEU A CA  
1811 C C   . LEU A 253 ? 0.3338 0.2935 0.3033 -0.0304 -0.0251 0.0034  790  LEU A C   
1812 O O   . LEU A 253 ? 0.3321 0.2927 0.3019 -0.0310 -0.0219 -0.0013 790  LEU A O   
1813 C CB  . LEU A 253 ? 0.2768 0.2500 0.2528 -0.0276 -0.0248 0.0046  790  LEU A CB  
1814 C CG  . LEU A 253 ? 0.2748 0.2540 0.2498 -0.0310 -0.0231 0.0035  790  LEU A CG  
1815 C CD1 . LEU A 253 ? 0.2737 0.2596 0.2557 -0.0259 -0.0236 0.0047  790  LEU A CD1 
1816 C CD2 . LEU A 253 ? 0.2822 0.2635 0.2569 -0.0335 -0.0184 -0.0023 790  LEU A CD2 
1817 N N   . THR A 254 ? 0.3175 0.2711 0.2885 -0.0272 -0.0286 0.0072  791  THR A N   
1818 C CA  . THR A 254 ? 0.3540 0.3001 0.3251 -0.0246 -0.0282 0.0054  791  THR A CA  
1819 C C   . THR A 254 ? 0.3471 0.2863 0.3099 -0.0321 -0.0280 0.0047  791  THR A C   
1820 O O   . THR A 254 ? 0.3289 0.2660 0.2909 -0.0326 -0.0257 0.0004  791  THR A O   
1821 C CB  . THR A 254 ? 0.3430 0.2832 0.3192 -0.0190 -0.0316 0.0095  791  THR A CB  
1822 O OG1 . THR A 254 ? 0.3260 0.2736 0.3111 -0.0121 -0.0301 0.0087  791  THR A OG1 
1823 C CG2 . THR A 254 ? 0.3486 0.2782 0.3234 -0.0172 -0.0310 0.0072  791  THR A CG2 
1824 N N   . LEU A 255 ? 0.3404 0.2764 0.2964 -0.0388 -0.0304 0.0088  792  LEU A N   
1825 C CA  . LEU A 255 ? 0.3543 0.2845 0.3015 -0.0473 -0.0291 0.0080  792  LEU A CA  
1826 C C   . LEU A 255 ? 0.3818 0.3200 0.3302 -0.0504 -0.0232 0.0014  792  LEU A C   
1827 O O   . LEU A 255 ? 0.3811 0.3170 0.3285 -0.0535 -0.0210 -0.0017 792  LEU A O   
1828 C CB  . LEU A 255 ? 0.3762 0.3017 0.3136 -0.0552 -0.0323 0.0135  792  LEU A CB  
1829 C CG  . LEU A 255 ? 0.3820 0.2972 0.3178 -0.0539 -0.0396 0.0211  792  LEU A CG  
1830 C CD1 . LEU A 255 ? 0.4132 0.3248 0.3383 -0.0625 -0.0440 0.0275  792  LEU A CD1 
1831 C CD2 . LEU A 255 ? 0.4131 0.3173 0.3465 -0.0547 -0.0403 0.0210  792  LEU A CD2 
1832 N N   . LEU A 256 ? 0.3241 0.2714 0.2758 -0.0495 -0.0209 -0.0004 793  LEU A N   
1833 C CA  . LEU A 256 ? 0.3731 0.3283 0.3290 -0.0513 -0.0156 -0.0063 793  LEU A CA  
1834 C C   . LEU A 256 ? 0.3871 0.3448 0.3505 -0.0460 -0.0150 -0.0099 793  LEU A C   
1835 O O   . LEU A 256 ? 0.3587 0.3181 0.3241 -0.0492 -0.0126 -0.0135 793  LEU A O   
1836 C CB  . LEU A 256 ? 0.3240 0.2868 0.2826 -0.0505 -0.0138 -0.0073 793  LEU A CB  
1837 C CG  . LEU A 256 ? 0.3713 0.3424 0.3370 -0.0508 -0.0087 -0.0130 793  LEU A CG  
1838 C CD1 . LEU A 256 ? 0.4160 0.3867 0.3801 -0.0581 -0.0042 -0.0165 793  LEU A CD1 
1839 C CD2 . LEU A 256 ? 0.3670 0.3424 0.3329 -0.0512 -0.0072 -0.0134 793  LEU A CD2 
1840 N N   . GLU A 257 ? 0.2937 0.2520 0.2609 -0.0386 -0.0172 -0.0090 794  GLU A N   
1841 C CA  . GLU A 257 ? 0.3117 0.2718 0.2835 -0.0343 -0.0169 -0.0124 794  GLU A CA  
1842 C C   . GLU A 257 ? 0.3872 0.3389 0.3554 -0.0361 -0.0179 -0.0133 794  GLU A C   
1843 O O   . GLU A 257 ? 0.3412 0.2944 0.3114 -0.0368 -0.0174 -0.0167 794  GLU A O   
1844 C CB  . GLU A 257 ? 0.3258 0.2878 0.3008 -0.0271 -0.0180 -0.0113 794  GLU A CB  
1845 C CG  . GLU A 257 ? 0.3674 0.3382 0.3463 -0.0260 -0.0168 -0.0111 794  GLU A CG  
1846 C CD  . GLU A 257 ? 0.4076 0.3813 0.3896 -0.0200 -0.0174 -0.0097 794  GLU A CD  
1847 O OE1 . GLU A 257 ? 0.3557 0.3357 0.3405 -0.0196 -0.0168 -0.0093 794  GLU A OE1 
1848 O OE2 . GLU A 257 ? 0.3911 0.3607 0.3730 -0.0159 -0.0179 -0.0094 794  GLU A OE2 
1849 N N   . SER A 258 ? 0.3354 0.2778 0.2983 -0.0373 -0.0200 -0.0098 795  SER A N   
1850 C CA  . SER A 258 ? 0.3201 0.2525 0.2787 -0.0398 -0.0211 -0.0103 795  SER A CA  
1851 C C   . SER A 258 ? 0.3632 0.2977 0.3202 -0.0480 -0.0190 -0.0126 795  SER A C   
1852 O O   . SER A 258 ? 0.3776 0.3102 0.3349 -0.0499 -0.0189 -0.0156 795  SER A O   
1853 C CB  . SER A 258 ? 0.3858 0.3073 0.3397 -0.0399 -0.0243 -0.0051 795  SER A CB  
1854 O OG  . SER A 258 ? 0.4287 0.3394 0.3776 -0.0437 -0.0253 -0.0054 795  SER A OG  
1855 N N   . ASP A 259 ? 0.3614 0.3000 0.3169 -0.0532 -0.0171 -0.0115 796  ASP A N   
1856 C CA  . ASP A 259 ? 0.3927 0.3346 0.3481 -0.0612 -0.0136 -0.0142 796  ASP A CA  
1857 C C   . ASP A 259 ? 0.4375 0.3901 0.4032 -0.0597 -0.0114 -0.0193 796  ASP A C   
1858 O O   . ASP A 259 ? 0.4108 0.3646 0.3793 -0.0641 -0.0104 -0.0218 796  ASP A O   
1859 C CB  . ASP A 259 ? 0.3923 0.3364 0.3431 -0.0672 -0.0108 -0.0130 796  ASP A CB  
1860 C CG  . ASP A 259 ? 0.5326 0.4651 0.4713 -0.0729 -0.0133 -0.0077 796  ASP A CG  
1861 O OD1 . ASP A 259 ? 0.6803 0.6031 0.6156 -0.0732 -0.0165 -0.0057 796  ASP A OD1 
1862 O OD2 . ASP A 259 ? 0.5804 0.5126 0.5125 -0.0777 -0.0125 -0.0054 796  ASP A OD2 
1863 N N   . LEU A 260 ? 0.3567 0.3171 0.3288 -0.0540 -0.0111 -0.0202 797  LEU A N   
1864 C CA  . LEU A 260 ? 0.3195 0.2894 0.3020 -0.0520 -0.0105 -0.0238 797  LEU A CA  
1865 C C   . LEU A 260 ? 0.3754 0.3420 0.3580 -0.0503 -0.0139 -0.0249 797  LEU A C   
1866 O O   . LEU A 260 ? 0.3528 0.3244 0.3419 -0.0530 -0.0142 -0.0274 797  LEU A O   
1867 C CB  . LEU A 260 ? 0.3155 0.2917 0.3028 -0.0461 -0.0105 -0.0236 797  LEU A CB  
1868 C CG  . LEU A 260 ? 0.3699 0.3500 0.3577 -0.0484 -0.0068 -0.0236 797  LEU A CG  
1869 C CD1 . LEU A 260 ? 0.4034 0.3876 0.3944 -0.0425 -0.0076 -0.0227 797  LEU A CD1 
1870 C CD2 . LEU A 260 ? 0.3945 0.3816 0.3906 -0.0534 -0.0021 -0.0277 797  LEU A CD2 
1871 N N   . TYR A 261 ? 0.3307 0.2889 0.3065 -0.0460 -0.0165 -0.0231 798  TYR A N   
1872 C CA  . TYR A 261 ? 0.3512 0.3044 0.3246 -0.0447 -0.0191 -0.0248 798  TYR A CA  
1873 C C   . TYR A 261 ? 0.4095 0.3570 0.3800 -0.0514 -0.0196 -0.0259 798  TYR A C   
1874 O O   . TYR A 261 ? 0.3594 0.3088 0.3322 -0.0538 -0.0215 -0.0284 798  TYR A O   
1875 C CB  . TYR A 261 ? 0.3654 0.3098 0.3325 -0.0389 -0.0201 -0.0234 798  TYR A CB  
1876 C CG  . TYR A 261 ? 0.4079 0.3451 0.3702 -0.0378 -0.0216 -0.0260 798  TYR A CG  
1877 C CD1 . TYR A 261 ? 0.4511 0.3764 0.4071 -0.0408 -0.0223 -0.0268 798  TYR A CD1 
1878 C CD2 . TYR A 261 ? 0.4454 0.3864 0.4080 -0.0345 -0.0223 -0.0278 798  TYR A CD2 
1879 C CE1 . TYR A 261 ? 0.4637 0.3811 0.4139 -0.0404 -0.0233 -0.0300 798  TYR A CE1 
1880 C CE2 . TYR A 261 ? 0.4500 0.3834 0.4057 -0.0346 -0.0233 -0.0308 798  TYR A CE2 
1881 C CZ  . TYR A 261 ? 0.4643 0.3859 0.4139 -0.0375 -0.0235 -0.0322 798  TYR A CZ  
1882 O OH  . TYR A 261 ? 0.5011 0.4140 0.4426 -0.0382 -0.0240 -0.0359 798  TYR A OH  
1883 N N   A ARG A 262 ? 0.3631 0.3037 0.3282 -0.0551 -0.0186 -0.0237 799  ARG A N   
1884 N N   B ARG A 262 ? 0.3734 0.3139 0.3384 -0.0551 -0.0186 -0.0237 799  ARG A N   
1885 C CA  A ARG A 262 ? 0.4047 0.3377 0.3653 -0.0621 -0.0190 -0.0241 799  ARG A CA  
1886 C CA  B ARG A 262 ? 0.3969 0.3299 0.3575 -0.0621 -0.0190 -0.0242 799  ARG A CA  
1887 C C   A ARG A 262 ? 0.4103 0.3534 0.3788 -0.0686 -0.0173 -0.0268 799  ARG A C   
1888 C C   B ARG A 262 ? 0.4064 0.3496 0.3751 -0.0685 -0.0173 -0.0269 799  ARG A C   
1889 O O   A ARG A 262 ? 0.3838 0.3235 0.3514 -0.0740 -0.0185 -0.0283 799  ARG A O   
1890 O O   B ARG A 262 ? 0.3953 0.3355 0.3634 -0.0736 -0.0187 -0.0285 799  ARG A O   
1891 C CB  A ARG A 262 ? 0.4541 0.3782 0.4071 -0.0654 -0.0185 -0.0201 799  ARG A CB  
1892 C CB  B ARG A 262 ? 0.4580 0.3820 0.4109 -0.0655 -0.0185 -0.0202 799  ARG A CB  
1893 C CG  A ARG A 262 ? 0.5870 0.5028 0.5343 -0.0740 -0.0186 -0.0198 799  ARG A CG  
1894 C CG  B ARG A 262 ? 0.5659 0.4837 0.5143 -0.0747 -0.0180 -0.0201 799  ARG A CG  
1895 C CD  A ARG A 262 ? 0.6828 0.5890 0.6211 -0.0779 -0.0189 -0.0148 799  ARG A CD  
1896 C CD  B ARG A 262 ? 0.6602 0.5655 0.5984 -0.0779 -0.0192 -0.0150 799  ARG A CD  
1897 N NE  A ARG A 262 ? 0.6646 0.5791 0.6037 -0.0797 -0.0160 -0.0134 799  ARG A NE  
1898 N NE  B ARG A 262 ? 0.6911 0.6004 0.6283 -0.0765 -0.0183 -0.0119 799  ARG A NE  
1899 C CZ  A ARG A 262 ? 0.6288 0.5512 0.5695 -0.0873 -0.0114 -0.0154 799  ARG A CZ  
1900 C CZ  B ARG A 262 ? 0.6805 0.5847 0.6158 -0.0700 -0.0213 -0.0081 799  ARG A CZ  
1901 N NH1 A ARG A 262 ? 0.5947 0.5192 0.5383 -0.0937 -0.0094 -0.0184 799  ARG A NH1 
1902 N NH1 B ARG A 262 ? 0.6633 0.5584 0.5984 -0.0639 -0.0244 -0.0074 799  ARG A NH1 
1903 N NH2 A ARG A 262 ? 0.6525 0.5806 0.5923 -0.0889 -0.0083 -0.0148 799  ARG A NH2 
1904 N NH2 B ARG A 262 ? 0.6346 0.5430 0.5686 -0.0701 -0.0210 -0.0051 799  ARG A NH2 
1905 N N   . LYS A 263 ? 0.3567 0.3121 0.3341 -0.0683 -0.0143 -0.0277 800  LYS A N   
1906 C CA  . LYS A 263 ? 0.3256 0.2918 0.3137 -0.0739 -0.0116 -0.0305 800  LYS A CA  
1907 C C   . LYS A 263 ? 0.3558 0.3311 0.3552 -0.0719 -0.0148 -0.0328 800  LYS A C   
1908 O O   . LYS A 263 ? 0.3704 0.3555 0.3817 -0.0763 -0.0134 -0.0349 800  LYS A O   
1909 C CB  . LYS A 263 ? 0.3419 0.3165 0.3353 -0.0749 -0.0061 -0.0312 800  LYS A CB  
1910 C CG  . LYS A 263 ? 0.4329 0.3996 0.4149 -0.0809 -0.0028 -0.0291 800  LYS A CG  
1911 C CD  . LYS A 263 ? 0.5492 0.5224 0.5333 -0.0822 0.0028  -0.0302 800  LYS A CD  
1912 C CE  . LYS A 263 ? 0.7059 0.6702 0.6759 -0.0898 0.0053  -0.0276 800  LYS A CE  
1913 N NZ  . LYS A 263 ? 0.7543 0.7213 0.7212 -0.0907 0.0094  -0.0279 800  LYS A NZ  
1914 N N   . VAL A 264 ? 0.3134 0.2857 0.3096 -0.0658 -0.0191 -0.0322 801  VAL A N   
1915 C CA  . VAL A 264 ? 0.3507 0.3306 0.3555 -0.0647 -0.0234 -0.0334 801  VAL A CA  
1916 C C   . VAL A 264 ? 0.3645 0.3405 0.3672 -0.0707 -0.0271 -0.0346 801  VAL A C   
1917 O O   . VAL A 264 ? 0.3882 0.3512 0.3779 -0.0716 -0.0286 -0.0346 801  VAL A O   
1918 C CB  . VAL A 264 ? 0.3092 0.2867 0.3092 -0.0576 -0.0266 -0.0324 801  VAL A CB  
1919 C CG1 . VAL A 264 ? 0.3376 0.3215 0.3441 -0.0580 -0.0322 -0.0329 801  VAL A CG1 
1920 C CG2 . VAL A 264 ? 0.2862 0.2689 0.2900 -0.0523 -0.0235 -0.0311 801  VAL A CG2 
1921 N N   . GLN A 265 ? 0.3478 0.3350 0.3643 -0.0750 -0.0284 -0.0358 802  GLN A N   
1922 C CA  . GLN A 265 ? 0.3231 0.3086 0.3394 -0.0815 -0.0330 -0.0368 802  GLN A CA  
1923 C C   . GLN A 265 ? 0.3541 0.3413 0.3707 -0.0793 -0.0404 -0.0363 802  GLN A C   
1924 O O   . GLN A 265 ? 0.3645 0.3614 0.3913 -0.0748 -0.0421 -0.0352 802  GLN A O   
1925 C CB  . GLN A 265 ? 0.3430 0.3409 0.3758 -0.0881 -0.0309 -0.0380 802  GLN A CB  
1926 C CG  . GLN A 265 ? 0.4011 0.3976 0.4324 -0.0920 -0.0229 -0.0386 802  GLN A CG  
1927 C CD  . GLN A 265 ? 0.5460 0.5251 0.5580 -0.0952 -0.0226 -0.0376 802  GLN A CD  
1928 O OE1 . GLN A 265 ? 0.4782 0.4502 0.4845 -0.1000 -0.0265 -0.0380 802  GLN A OE1 
1929 N NE2 . GLN A 265 ? 0.5327 0.5043 0.5349 -0.0925 -0.0187 -0.0361 802  GLN A NE2 
1930 N N   . PRO A 266 ? 0.3648 0.3416 0.3693 -0.0830 -0.0449 -0.0372 803  PRO A N   
1931 C CA  . PRO A 266 ? 0.3508 0.3269 0.3513 -0.0832 -0.0524 -0.0369 803  PRO A CA  
1932 C C   . PRO A 266 ? 0.3361 0.3286 0.3555 -0.0846 -0.0581 -0.0351 803  PRO A C   
1933 O O   . PRO A 266 ? 0.3896 0.3846 0.4087 -0.0814 -0.0631 -0.0334 803  PRO A O   
1934 C CB  . PRO A 266 ? 0.4127 0.3763 0.4002 -0.0904 -0.0551 -0.0390 803  PRO A CB  
1935 C CG  . PRO A 266 ? 0.4810 0.4329 0.4592 -0.0897 -0.0485 -0.0399 803  PRO A CG  
1936 C CD  . PRO A 266 ? 0.3574 0.3200 0.3487 -0.0876 -0.0428 -0.0384 803  PRO A CD  
1937 N N   . SER A 267 ? 0.3506 0.3541 0.3868 -0.0894 -0.0573 -0.0354 804  SER A N   
1938 C CA  . SER A 267 ? 0.3233 0.3434 0.3812 -0.0904 -0.0630 -0.0336 804  SER A CA  
1939 C C   . SER A 267 ? 0.3241 0.3534 0.3944 -0.0822 -0.0613 -0.0319 804  SER A C   
1940 O O   . SER A 267 ? 0.3348 0.3751 0.4209 -0.0811 -0.0676 -0.0295 804  SER A O   
1941 C CB  . SER A 267 ? 0.3312 0.3624 0.4071 -0.0970 -0.0605 -0.0349 804  SER A CB  
1942 O OG  . SER A 267 ? 0.3087 0.3433 0.3906 -0.0949 -0.0501 -0.0367 804  SER A OG  
1943 N N   . GLU A 268 ? 0.2874 0.3119 0.3511 -0.0768 -0.0533 -0.0329 805  GLU A N   
1944 C CA  . GLU A 268 ? 0.2629 0.2940 0.3359 -0.0693 -0.0514 -0.0316 805  GLU A CA  
1945 C C   . GLU A 268 ? 0.3364 0.3629 0.4001 -0.0653 -0.0583 -0.0288 805  GLU A C   
1946 O O   . GLU A 268 ? 0.2995 0.3322 0.3726 -0.0602 -0.0597 -0.0267 805  GLU A O   
1947 C CB  . GLU A 268 ? 0.2409 0.2672 0.3070 -0.0658 -0.0418 -0.0332 805  GLU A CB  
1948 C CG  . GLU A 268 ? 0.2981 0.3268 0.3691 -0.0711 -0.0344 -0.0359 805  GLU A CG  
1949 C CD  . GLU A 268 ? 0.3439 0.3687 0.4086 -0.0685 -0.0259 -0.0368 805  GLU A CD  
1950 O OE1 . GLU A 268 ? 0.3402 0.3692 0.4105 -0.0628 -0.0240 -0.0365 805  GLU A OE1 
1951 O OE2 . GLU A 268 ? 0.4036 0.4207 0.4574 -0.0727 -0.0216 -0.0376 805  GLU A OE2 
1952 N N   . LEU A 269 ? 0.3552 0.3700 0.3996 -0.0683 -0.0621 -0.0289 806  LEU A N   
1953 C CA  . LEU A 269 ? 0.3762 0.3848 0.4076 -0.0662 -0.0678 -0.0268 806  LEU A CA  
1954 C C   . LEU A 269 ? 0.3975 0.4091 0.4310 -0.0716 -0.0788 -0.0244 806  LEU A C   
1955 O O   . LEU A 269 ? 0.5032 0.5136 0.5313 -0.0705 -0.0850 -0.0215 806  LEU A O   
1956 C CB  . LEU A 269 ? 0.3654 0.3581 0.3731 -0.0659 -0.0640 -0.0292 806  LEU A CB  
1957 C CG  . LEU A 269 ? 0.4238 0.4136 0.4291 -0.0599 -0.0549 -0.0301 806  LEU A CG  
1958 C CD1 . LEU A 269 ? 0.4990 0.4773 0.4925 -0.0618 -0.0500 -0.0328 806  LEU A CD1 
1959 C CD2 . LEU A 269 ? 0.5613 0.5474 0.5576 -0.0544 -0.0545 -0.0288 806  LEU A CD2 
1960 N N   . VAL A 270 ? 0.3312 0.3464 0.3717 -0.0784 -0.0818 -0.0254 807  VAL A N   
1961 C CA  . VAL A 270 ? 0.2904 0.3078 0.3315 -0.0850 -0.0933 -0.0229 807  VAL A CA  
1962 C C   . VAL A 270 ? 0.4059 0.4377 0.4690 -0.0826 -0.1009 -0.0180 807  VAL A C   
1963 O O   . VAL A 270 ? 0.3990 0.4430 0.4849 -0.0784 -0.0969 -0.0178 807  VAL A O   
1964 C CB  . VAL A 270 ? 0.3456 0.3647 0.3912 -0.0934 -0.0948 -0.0249 807  VAL A CB  
1965 C CG1 . VAL A 270 ? 0.3764 0.3995 0.4249 -0.1010 -0.1080 -0.0218 807  VAL A CG1 
1966 C CG2 . VAL A 270 ? 0.3592 0.3618 0.3822 -0.0962 -0.0887 -0.0293 807  VAL A CG2 
1967 N N   . GLY A 271 ? 0.4179 0.4476 0.4737 -0.0855 -0.1118 -0.0140 808  GLY A N   
1968 C CA  . GLY A 271 ? 0.4310 0.4733 0.5079 -0.0841 -0.1215 -0.0082 808  GLY A CA  
1969 C C   . GLY A 271 ? 0.4344 0.4795 0.5189 -0.0748 -0.1175 -0.0063 808  GLY A C   
1970 O O   . GLY A 271 ? 0.4212 0.4775 0.5283 -0.0716 -0.1231 -0.0020 808  GLY A O   
1971 N N   . SER A 272 ? 0.3776 0.4124 0.4442 -0.0704 -0.1080 -0.0094 809  SER A N   
1972 C CA  . SER A 272 ? 0.4157 0.4520 0.4873 -0.0622 -0.1029 -0.0083 809  SER A CA  
1973 C C   . SER A 272 ? 0.3946 0.4447 0.4958 -0.0576 -0.0987 -0.0088 809  SER A C   
1974 O O   . SER A 272 ? 0.3909 0.4460 0.5052 -0.0522 -0.1003 -0.0058 809  SER A O   
1975 C CB  . SER A 272 ? 0.5724 0.6062 0.6380 -0.0616 -0.1124 -0.0024 809  SER A CB  
1976 O OG  . SER A 272 ? 0.6392 0.6600 0.6763 -0.0666 -0.1153 -0.0025 809  SER A OG  
1977 N N   . VAL A 273 ? 0.3485 0.4040 0.4598 -0.0600 -0.0929 -0.0128 810  VAL A N   
1978 C CA  . VAL A 273 ? 0.3572 0.4265 0.4975 -0.0570 -0.0883 -0.0142 810  VAL A CA  
1979 C C   . VAL A 273 ? 0.3378 0.4061 0.4802 -0.0498 -0.0781 -0.0164 810  VAL A C   
1980 O O   . VAL A 273 ? 0.3804 0.4589 0.5464 -0.0460 -0.0752 -0.0170 810  VAL A O   
1981 C CB  . VAL A 273 ? 0.3291 0.4040 0.4778 -0.0625 -0.0830 -0.0184 810  VAL A CB  
1982 C CG1 . VAL A 273 ? 0.4414 0.5246 0.6031 -0.0688 -0.0937 -0.0157 810  VAL A CG1 
1983 C CG2 . VAL A 273 ? 0.2639 0.3255 0.3866 -0.0657 -0.0760 -0.0221 810  VAL A CG2 
1984 N N   . TRP A 274 ? 0.3368 0.3932 0.4557 -0.0481 -0.0728 -0.0177 811  TRP A N   
1985 C CA  . TRP A 274 ? 0.3556 0.4105 0.4745 -0.0423 -0.0639 -0.0196 811  TRP A CA  
1986 C C   . TRP A 274 ? 0.3082 0.3647 0.4345 -0.0368 -0.0685 -0.0157 811  TRP A C   
1987 O O   . TRP A 274 ? 0.3515 0.4081 0.4819 -0.0321 -0.0621 -0.0170 811  TRP A O   
1988 C CB  . TRP A 274 ? 0.3191 0.3616 0.4125 -0.0422 -0.0579 -0.0215 811  TRP A CB  
1989 C CG  . TRP A 274 ? 0.3410 0.3742 0.4156 -0.0405 -0.0623 -0.0185 811  TRP A CG  
1990 C CD1 . TRP A 274 ? 0.3649 0.3953 0.4349 -0.0356 -0.0607 -0.0169 811  TRP A CD1 
1991 C CD2 . TRP A 274 ? 0.3332 0.3585 0.3901 -0.0445 -0.0682 -0.0174 811  TRP A CD2 
1992 N NE1 . TRP A 274 ? 0.4347 0.4567 0.4860 -0.0363 -0.0648 -0.0147 811  TRP A NE1 
1993 C CE2 . TRP A 274 ? 0.3795 0.3978 0.4219 -0.0417 -0.0691 -0.0153 811  TRP A CE2 
1994 C CE3 . TRP A 274 ? 0.3789 0.4017 0.4302 -0.0508 -0.0723 -0.0184 811  TRP A CE3 
1995 C CZ2 . TRP A 274 ? 0.3695 0.3786 0.3919 -0.0450 -0.0732 -0.0146 811  TRP A CZ2 
1996 C CZ3 . TRP A 274 ? 0.4461 0.4589 0.4770 -0.0541 -0.0769 -0.0178 811  TRP A CZ3 
1997 C CH2 . TRP A 274 ? 0.4419 0.4479 0.4584 -0.0511 -0.0769 -0.0161 811  TRP A CH2 
1998 N N   . THR A 275 ? 0.3355 0.3926 0.4629 -0.0381 -0.0800 -0.0106 812  THR A N   
1999 C CA  . THR A 275 ? 0.3918 0.4491 0.5251 -0.0338 -0.0859 -0.0057 812  THR A CA  
2000 C C   . THR A 275 ? 0.4830 0.5522 0.6463 -0.0324 -0.0929 -0.0028 812  THR A C   
2001 O O   . THR A 275 ? 0.4039 0.4735 0.5750 -0.0292 -0.1002 0.0024  812  THR A O   
2002 C CB  . THR A 275 ? 0.3730 0.4208 0.4839 -0.0365 -0.0947 -0.0009 812  THR A CB  
2003 O OG1 . THR A 275 ? 0.4054 0.4557 0.5180 -0.0424 -0.1054 0.0020  812  THR A OG1 
2004 C CG2 . THR A 275 ? 0.3823 0.4189 0.4657 -0.0378 -0.0877 -0.0043 812  THR A CG2 
2005 N N   . LYS A 276 ? 0.4470 0.5260 0.6278 -0.0349 -0.0909 -0.0058 813  LYS A N   
2006 C CA  . LYS A 276 ? 0.5092 0.6011 0.7210 -0.0342 -0.0983 -0.0029 813  LYS A CA  
2007 C C   . LYS A 276 ? 0.5172 0.6196 0.7562 -0.0301 -0.0876 -0.0083 813  LYS A C   
2008 O O   . LYS A 276 ? 0.4547 0.5537 0.6861 -0.0289 -0.0749 -0.0141 813  LYS A O   
2009 C CB  . LYS A 276 ? 0.5281 0.6244 0.7409 -0.0417 -0.1069 -0.0012 813  LYS A CB  
2010 C CG  . LYS A 276 ? 0.6218 0.7082 0.8102 -0.0464 -0.1190 0.0045  813  LYS A CG  
2011 C CD  . LYS A 276 ? 0.7976 0.8883 0.9876 -0.0547 -0.1284 0.0062  813  LYS A CD  
2012 C CE  . LYS A 276 ? 0.8404 0.9203 1.0049 -0.0603 -0.1406 0.0116  813  LYS A CE  
2013 N NZ  . LYS A 276 ? 0.8920 0.9745 1.0552 -0.0696 -0.1500 0.0129  813  LYS A NZ  
2014 N N   . GLU A 277 ? 0.5076 0.6230 0.7787 -0.0285 -0.0932 -0.0062 814  GLU A N   
2015 C CA  . GLU A 277 ? 0.5299 0.6559 0.8319 -0.0234 -0.0840 -0.0109 814  GLU A CA  
2016 C C   . GLU A 277 ? 0.4981 0.6265 0.7982 -0.0262 -0.0679 -0.0198 814  GLU A C   
2017 O O   . GLU A 277 ? 0.5624 0.6900 0.8671 -0.0224 -0.0560 -0.0252 814  GLU A O   
2018 C CB  . GLU A 277 ? 0.6826 0.8238 1.0205 -0.0228 -0.0934 -0.0072 814  GLU A CB  
2019 C CG  . GLU A 277 ? 0.8444 0.9968 1.2189 -0.0161 -0.0852 -0.0114 814  GLU A CG  
2020 C CD  . GLU A 277 ? 1.0111 1.1780 1.4232 -0.0140 -0.0971 -0.0060 814  GLU A CD  
2021 O OE1 . GLU A 277 ? 0.9800 1.1608 1.4127 -0.0179 -0.0960 -0.0082 814  GLU A OE1 
2022 O OE2 . GLU A 277 ? 1.1168 1.2813 1.5385 -0.0088 -0.1079 0.0009  814  GLU A OE2 
2023 N N   . ASP A 278 ? 0.3897 0.5201 0.6817 -0.0335 -0.0678 -0.0213 815  ASP A N   
2024 C CA  . ASP A 278 ? 0.3889 0.5214 0.6785 -0.0375 -0.0536 -0.0289 815  ASP A CA  
2025 C C   . ASP A 278 ? 0.3680 0.4853 0.6211 -0.0405 -0.0479 -0.0308 815  ASP A C   
2026 O O   . ASP A 278 ? 0.3336 0.4501 0.5779 -0.0464 -0.0407 -0.0347 815  ASP A O   
2027 C CB  . ASP A 278 ? 0.3846 0.5286 0.6891 -0.0443 -0.0558 -0.0296 815  ASP A CB  
2028 C CG  . ASP A 278 ? 0.4821 0.6440 0.8283 -0.0415 -0.0578 -0.0294 815  ASP A CG  
2029 O OD1 . ASP A 278 ? 0.4949 0.6600 0.8592 -0.0342 -0.0528 -0.0312 815  ASP A OD1 
2030 O OD2 . ASP A 278 ? 0.5420 0.7146 0.9036 -0.0465 -0.0642 -0.0276 815  ASP A OD2 
2031 N N   . LYS A 279 ? 0.3234 0.4293 0.5569 -0.0366 -0.0510 -0.0278 816  LYS A N   
2032 C CA  . LYS A 279 ? 0.3083 0.4004 0.5094 -0.0386 -0.0470 -0.0287 816  LYS A CA  
2033 C C   . LYS A 279 ? 0.3127 0.4028 0.5079 -0.0407 -0.0330 -0.0350 816  LYS A C   
2034 O O   . LYS A 279 ? 0.3065 0.3885 0.4805 -0.0450 -0.0302 -0.0360 816  LYS A O   
2035 C CB  . LYS A 279 ? 0.3174 0.3998 0.5035 -0.0334 -0.0508 -0.0251 816  LYS A CB  
2036 C CG  . LYS A 279 ? 0.3821 0.4662 0.5806 -0.0273 -0.0450 -0.0267 816  LYS A CG  
2037 C CD  . LYS A 279 ? 0.4083 0.4818 0.5888 -0.0234 -0.0477 -0.0233 816  LYS A CD  
2038 C CE  . LYS A 279 ? 0.5096 0.5837 0.6968 -0.0207 -0.0601 -0.0166 816  LYS A CE  
2039 N NZ  . LYS A 279 ? 0.5319 0.6145 0.7491 -0.0159 -0.0610 -0.0163 816  LYS A NZ  
2040 N N   . GLU A 280 ? 0.3445 0.4414 0.5579 -0.0382 -0.0243 -0.0392 817  GLU A N   
2041 C CA  . GLU A 280 ? 0.3226 0.4158 0.5262 -0.0410 -0.0112 -0.0449 817  GLU A CA  
2042 C C   . GLU A 280 ? 0.3606 0.4577 0.5644 -0.0490 -0.0065 -0.0479 817  GLU A C   
2043 O O   . GLU A 280 ? 0.4218 0.5117 0.6073 -0.0536 0.0007  -0.0504 817  GLU A O   
2044 C CB  . GLU A 280 ? 0.3613 0.4595 0.5826 -0.0372 -0.0021 -0.0496 817  GLU A CB  
2045 C CG  . GLU A 280 ? 0.3825 0.4763 0.6052 -0.0295 -0.0065 -0.0467 817  GLU A CG  
2046 C CD  . GLU A 280 ? 0.4824 0.5626 0.6760 -0.0289 -0.0064 -0.0449 817  GLU A CD  
2047 O OE1 . GLU A 280 ? 0.4372 0.5114 0.6118 -0.0336 -0.0003 -0.0470 817  GLU A OE1 
2048 O OE2 . GLU A 280 ? 0.4425 0.5183 0.6331 -0.0238 -0.0126 -0.0408 817  GLU A OE2 
2049 N N   . ILE A 281 ? 0.3215 0.4300 0.5461 -0.0510 -0.0112 -0.0472 818  ILE A N   
2050 C CA  . ILE A 281 ? 0.3449 0.4583 0.5719 -0.0593 -0.0076 -0.0497 818  ILE A CA  
2051 C C   . ILE A 281 ? 0.3195 0.4234 0.5239 -0.0639 -0.0159 -0.0457 818  ILE A C   
2052 O O   . ILE A 281 ? 0.3370 0.4350 0.5264 -0.0706 -0.0112 -0.0475 818  ILE A O   
2053 C CB  . ILE A 281 ? 0.3566 0.4879 0.6187 -0.0599 -0.0090 -0.0507 818  ILE A CB  
2054 C CG1 . ILE A 281 ? 0.4975 0.6379 0.7824 -0.0571 0.0034  -0.0569 818  ILE A CG1 
2055 C CG2 . ILE A 281 ? 0.4092 0.5455 0.6728 -0.0692 -0.0088 -0.0516 818  ILE A CG2 
2056 C CD1 . ILE A 281 ? 0.5969 0.7345 0.8705 -0.0638 0.0183  -0.0634 818  ILE A CD1 
2057 N N   . ASN A 282 ? 0.3354 0.4366 0.5365 -0.0608 -0.0282 -0.0405 819  ASN A N   
2058 C CA  . ASN A 282 ? 0.2899 0.3827 0.4720 -0.0655 -0.0364 -0.0375 819  ASN A CA  
2059 C C   . ASN A 282 ? 0.2828 0.3585 0.4336 -0.0644 -0.0355 -0.0367 819  ASN A C   
2060 O O   . ASN A 282 ? 0.2824 0.3491 0.4157 -0.0692 -0.0379 -0.0362 819  ASN A O   
2061 C CB  . ASN A 282 ? 0.2637 0.3609 0.4547 -0.0641 -0.0501 -0.0324 819  ASN A CB  
2062 C CG  . ASN A 282 ? 0.3424 0.4567 0.5649 -0.0666 -0.0533 -0.0323 819  ASN A CG  
2063 O OD1 . ASN A 282 ? 0.3651 0.4860 0.5967 -0.0724 -0.0470 -0.0359 819  ASN A OD1 
2064 N ND2 . ASN A 282 ? 0.2930 0.4146 0.5329 -0.0626 -0.0633 -0.0279 819  ASN A ND2 
2065 N N   . SER A 283 ? 0.2293 0.3006 0.3741 -0.0582 -0.0321 -0.0365 820  SER A N   
2066 C CA  . SER A 283 ? 0.2657 0.3224 0.3839 -0.0564 -0.0318 -0.0353 820  SER A CA  
2067 C C   . SER A 283 ? 0.2397 0.2922 0.3508 -0.0541 -0.0223 -0.0375 820  SER A C   
2068 O O   . SER A 283 ? 0.2897 0.3357 0.3899 -0.0492 -0.0230 -0.0357 820  SER A O   
2069 C CB  . SER A 283 ? 0.3089 0.3619 0.4213 -0.0514 -0.0404 -0.0312 820  SER A CB  
2070 O OG  . SER A 283 ? 0.3418 0.3981 0.4591 -0.0543 -0.0503 -0.0286 820  SER A OG  
2071 N N   . PRO A 284 ? 0.3069 0.3627 0.4228 -0.0585 -0.0135 -0.0412 821  PRO A N   
2072 C CA  . PRO A 284 ? 0.3261 0.3785 0.4358 -0.0571 -0.0050 -0.0433 821  PRO A CA  
2073 C C   . PRO A 284 ? 0.3087 0.3475 0.3936 -0.0565 -0.0054 -0.0411 821  PRO A C   
2074 O O   . PRO A 284 ? 0.2947 0.3303 0.3740 -0.0527 -0.0030 -0.0407 821  PRO A O   
2075 C CB  . PRO A 284 ? 0.3532 0.4107 0.4698 -0.0641 0.0041  -0.0477 821  PRO A CB  
2076 C CG  . PRO A 284 ? 0.3372 0.3948 0.4526 -0.0699 -0.0001 -0.0467 821  PRO A CG  
2077 C CD  . PRO A 284 ? 0.3158 0.3773 0.4399 -0.0659 -0.0107 -0.0436 821  PRO A CD  
2078 N N   . ASN A 285 ? 0.2955 0.3264 0.3669 -0.0600 -0.0085 -0.0395 822  ASN A N   
2079 C CA  . ASN A 285 ? 0.3043 0.3226 0.3551 -0.0591 -0.0086 -0.0374 822  ASN A CA  
2080 C C   . ASN A 285 ? 0.2918 0.3061 0.3364 -0.0525 -0.0145 -0.0346 822  ASN A C   
2081 O O   . ASN A 285 ? 0.2896 0.2986 0.3249 -0.0489 -0.0133 -0.0331 822  ASN A O   
2082 C CB  . ASN A 285 ? 0.3072 0.3172 0.3467 -0.0650 -0.0095 -0.0369 822  ASN A CB  
2083 C CG  . ASN A 285 ? 0.3917 0.4055 0.4361 -0.0728 -0.0033 -0.0394 822  ASN A CG  
2084 O OD1 . ASN A 285 ? 0.3814 0.3934 0.4207 -0.0754 0.0030  -0.0402 822  ASN A OD1 
2085 N ND2 . ASN A 285 ? 0.3426 0.3622 0.3968 -0.0774 -0.0050 -0.0407 822  ASN A ND2 
2086 N N   . LEU A 286 ? 0.2783 0.2954 0.3280 -0.0514 -0.0209 -0.0337 823  LEU A N   
2087 C CA  . LEU A 286 ? 0.2714 0.2852 0.3151 -0.0462 -0.0262 -0.0313 823  LEU A CA  
2088 C C   . LEU A 286 ? 0.2886 0.3074 0.3393 -0.0410 -0.0245 -0.0305 823  LEU A C   
2089 O O   . LEU A 286 ? 0.2822 0.2959 0.3233 -0.0371 -0.0245 -0.0289 823  LEU A O   
2090 C CB  . LEU A 286 ? 0.3066 0.3231 0.3545 -0.0476 -0.0338 -0.0303 823  LEU A CB  
2091 C CG  . LEU A 286 ? 0.3172 0.3302 0.3576 -0.0437 -0.0395 -0.0277 823  LEU A CG  
2092 C CD1 . LEU A 286 ? 0.4258 0.4276 0.4478 -0.0415 -0.0372 -0.0276 823  LEU A CD1 
2093 C CD2 . LEU A 286 ? 0.3420 0.3559 0.3831 -0.0472 -0.0476 -0.0266 823  LEU A CD2 
2094 N N   . LEU A 287 ? 0.2814 0.3098 0.3496 -0.0410 -0.0227 -0.0320 824  LEU A N   
2095 C CA  . LEU A 287 ? 0.3074 0.3391 0.3826 -0.0363 -0.0207 -0.0318 824  LEU A CA  
2096 C C   . LEU A 287 ? 0.3379 0.3643 0.4025 -0.0360 -0.0142 -0.0327 824  LEU A C   
2097 O O   . LEU A 287 ? 0.3008 0.3250 0.3615 -0.0321 -0.0145 -0.0311 824  LEU A O   
2098 C CB  . LEU A 287 ? 0.2901 0.3325 0.3878 -0.0363 -0.0188 -0.0341 824  LEU A CB  
2099 C CG  . LEU A 287 ? 0.3408 0.3895 0.4521 -0.0350 -0.0274 -0.0315 824  LEU A CG  
2100 C CD1 . LEU A 287 ? 0.3054 0.3658 0.4427 -0.0347 -0.0249 -0.0341 824  LEU A CD1 
2101 C CD2 . LEU A 287 ? 0.3117 0.3567 0.4177 -0.0302 -0.0339 -0.0273 824  LEU A CD2 
2102 N N   . LYS A 288 ? 0.2797 0.3038 0.3390 -0.0409 -0.0089 -0.0348 825  LYS A N   
2103 C CA  . LYS A 288 ? 0.3164 0.3348 0.3642 -0.0418 -0.0041 -0.0349 825  LYS A CA  
2104 C C   . LYS A 288 ? 0.2895 0.3001 0.3230 -0.0384 -0.0080 -0.0312 825  LYS A C   
2105 O O   . LYS A 288 ? 0.2827 0.2911 0.3110 -0.0363 -0.0068 -0.0299 825  LYS A O   
2106 C CB  . LYS A 288 ? 0.3316 0.3471 0.3733 -0.0487 0.0009  -0.0366 825  LYS A CB  
2107 C CG  . LYS A 288 ? 0.5349 0.5574 0.5880 -0.0529 0.0084  -0.0413 825  LYS A CG  
2108 C CD  . LYS A 288 ? 0.5917 0.6087 0.6324 -0.0605 0.0142  -0.0423 825  LYS A CD  
2109 C CE  . LYS A 288 ? 0.6825 0.6918 0.7081 -0.0600 0.0146  -0.0400 825  LYS A CE  
2110 N NZ  . LYS A 288 ? 0.7224 0.7250 0.7337 -0.0681 0.0186  -0.0398 825  LYS A NZ  
2111 N N   A MET A 289 ? 0.2956 0.3020 0.3233 -0.0383 -0.0125 -0.0297 826  MET A N   
2112 N N   B MET A 289 ? 0.2960 0.3025 0.3238 -0.0383 -0.0125 -0.0297 826  MET A N   
2113 C CA  A MET A 289 ? 0.3103 0.3094 0.3260 -0.0350 -0.0153 -0.0270 826  MET A CA  
2114 C CA  B MET A 289 ? 0.3087 0.3079 0.3244 -0.0350 -0.0152 -0.0270 826  MET A CA  
2115 C C   A MET A 289 ? 0.3108 0.3124 0.3283 -0.0299 -0.0178 -0.0254 826  MET A C   
2116 C C   B MET A 289 ? 0.3086 0.3101 0.3260 -0.0299 -0.0179 -0.0254 826  MET A C   
2117 O O   A MET A 289 ? 0.2799 0.2790 0.2917 -0.0271 -0.0170 -0.0236 826  MET A O   
2118 O O   B MET A 289 ? 0.2845 0.2833 0.2959 -0.0270 -0.0172 -0.0236 826  MET A O   
2119 C CB  A MET A 289 ? 0.3351 0.3286 0.3446 -0.0364 -0.0186 -0.0270 826  MET A CB  
2120 C CB  B MET A 289 ? 0.3354 0.3287 0.3447 -0.0367 -0.0184 -0.0271 826  MET A CB  
2121 C CG  A MET A 289 ? 0.3599 0.3457 0.3584 -0.0327 -0.0203 -0.0253 826  MET A CG  
2122 C CG  B MET A 289 ? 0.4588 0.4466 0.4597 -0.0326 -0.0214 -0.0257 826  MET A CG  
2123 S SD  A MET A 289 ? 0.4281 0.4057 0.4178 -0.0332 -0.0176 -0.0236 826  MET A SD  
2124 S SD  B MET A 289 ? 0.4393 0.4155 0.4287 -0.0346 -0.0221 -0.0262 826  MET A SD  
2125 C CE  A MET A 289 ? 0.5161 0.4855 0.4975 -0.0283 -0.0193 -0.0229 826  MET A CE  
2126 C CE  B MET A 289 ? 0.5280 0.4994 0.5126 -0.0332 -0.0189 -0.0239 826  MET A CE  
2127 N N   . ILE A 290 ? 0.2940 0.3005 0.3199 -0.0291 -0.0213 -0.0255 827  ILE A N   
2128 C CA  . ILE A 290 ? 0.2946 0.3029 0.3219 -0.0252 -0.0244 -0.0234 827  ILE A CA  
2129 C C   . ILE A 290 ? 0.2929 0.3039 0.3248 -0.0231 -0.0210 -0.0232 827  ILE A C   
2130 O O   . ILE A 290 ? 0.3208 0.3301 0.3479 -0.0203 -0.0216 -0.0211 827  ILE A O   
2131 C CB  . ILE A 290 ? 0.3352 0.3487 0.3726 -0.0256 -0.0298 -0.0229 827  ILE A CB  
2132 C CG1 . ILE A 290 ? 0.3626 0.3720 0.3923 -0.0283 -0.0341 -0.0228 827  ILE A CG1 
2133 C CG2 . ILE A 290 ? 0.3750 0.3898 0.4146 -0.0221 -0.0332 -0.0200 827  ILE A CG2 
2134 C CD1 . ILE A 290 ? 0.3658 0.3807 0.4057 -0.0302 -0.0408 -0.0218 827  ILE A CD1 
2135 N N   . ARG A 291 ? 0.2758 0.2909 0.3171 -0.0251 -0.0170 -0.0259 828  ARG A N   
2136 C CA  . ARG A 291 ? 0.3176 0.3343 0.3633 -0.0239 -0.0133 -0.0267 828  ARG A CA  
2137 C C   . ARG A 291 ? 0.3370 0.3488 0.3704 -0.0247 -0.0104 -0.0258 828  ARG A C   
2138 O O   . ARG A 291 ? 0.3186 0.3298 0.3506 -0.0230 -0.0098 -0.0247 828  ARG A O   
2139 C CB  . ARG A 291 ? 0.2713 0.2932 0.3301 -0.0263 -0.0086 -0.0308 828  ARG A CB  
2140 C CG  . ARG A 291 ? 0.3167 0.3451 0.3922 -0.0241 -0.0125 -0.0307 828  ARG A CG  
2141 C CD  . ARG A 291 ? 0.4439 0.4790 0.5361 -0.0262 -0.0073 -0.0353 828  ARG A CD  
2142 N NE  . ARG A 291 ? 0.4510 0.4928 0.5617 -0.0233 -0.0123 -0.0343 828  ARG A NE  
2143 C CZ  . ARG A 291 ? 0.4501 0.4999 0.5789 -0.0247 -0.0106 -0.0371 828  ARG A CZ  
2144 N NH1 . ARG A 291 ? 0.3945 0.4465 0.5240 -0.0295 -0.0030 -0.0416 828  ARG A NH1 
2145 N NH2 . ARG A 291 ? 0.4225 0.4784 0.5691 -0.0216 -0.0169 -0.0350 828  ARG A NH2 
2146 N N   . HIS A 292 ? 0.2920 0.2998 0.3168 -0.0276 -0.0094 -0.0258 829  HIS A N   
2147 C CA  . HIS A 292 ? 0.2935 0.2965 0.3074 -0.0282 -0.0085 -0.0237 829  HIS A CA  
2148 C C   . HIS A 292 ? 0.3078 0.3094 0.3175 -0.0237 -0.0118 -0.0204 829  HIS A C   
2149 O O   . HIS A 292 ? 0.2875 0.2890 0.2945 -0.0228 -0.0113 -0.0187 829  HIS A O   
2150 C CB  . HIS A 292 ? 0.2884 0.2861 0.2944 -0.0315 -0.0083 -0.0232 829  HIS A CB  
2151 C CG  . HIS A 292 ? 0.3182 0.3109 0.3150 -0.0307 -0.0096 -0.0197 829  HIS A CG  
2152 N ND1 . HIS A 292 ? 0.3435 0.3346 0.3354 -0.0339 -0.0080 -0.0185 829  HIS A ND1 
2153 C CD2 . HIS A 292 ? 0.3456 0.3348 0.3383 -0.0270 -0.0125 -0.0171 829  HIS A CD2 
2154 C CE1 . HIS A 292 ? 0.3425 0.3301 0.3290 -0.0320 -0.0108 -0.0146 829  HIS A CE1 
2155 N NE2 . HIS A 292 ? 0.2852 0.2718 0.2730 -0.0274 -0.0130 -0.0140 829  HIS A NE2 
2156 N N   . THR A 293 ? 0.2603 0.2612 0.2693 -0.0214 -0.0149 -0.0198 830  THR A N   
2157 C CA  . THR A 293 ? 0.3359 0.3353 0.3401 -0.0178 -0.0169 -0.0175 830  THR A CA  
2158 C C   . THR A 293 ? 0.2986 0.3018 0.3069 -0.0159 -0.0174 -0.0162 830  THR A C   
2159 O O   . THR A 293 ? 0.3019 0.3050 0.3071 -0.0143 -0.0169 -0.0142 830  THR A O   
2160 C CB  . THR A 293 ? 0.3645 0.3613 0.3653 -0.0171 -0.0195 -0.0179 830  THR A CB  
2161 O OG1 . THR A 293 ? 0.3800 0.3715 0.3757 -0.0185 -0.0188 -0.0188 830  THR A OG1 
2162 C CG2 . THR A 293 ? 0.3745 0.3704 0.3702 -0.0140 -0.0203 -0.0162 830  THR A CG2 
2163 N N   . THR A 294 ? 0.2803 0.2867 0.2968 -0.0163 -0.0186 -0.0173 831  THR A N   
2164 C CA  . THR A 294 ? 0.2718 0.2804 0.2931 -0.0146 -0.0194 -0.0160 831  THR A CA  
2165 C C   . THR A 294 ? 0.3215 0.3300 0.3425 -0.0155 -0.0159 -0.0163 831  THR A C   
2166 O O   . THR A 294 ? 0.2972 0.3055 0.3156 -0.0144 -0.0163 -0.0141 831  THR A O   
2167 C CB  . THR A 294 ? 0.3401 0.3520 0.3734 -0.0146 -0.0213 -0.0171 831  THR A CB  
2168 O OG1 . THR A 294 ? 0.3661 0.3780 0.3989 -0.0146 -0.0260 -0.0161 831  THR A OG1 
2169 C CG2 . THR A 294 ? 0.4113 0.4238 0.4499 -0.0127 -0.0226 -0.0154 831  THR A CG2 
2170 N N   . ASN A 295 ? 0.2622 0.2707 0.2848 -0.0184 -0.0123 -0.0190 832  ASN A N   
2171 C CA  . ASN A 295 ? 0.3174 0.3248 0.3377 -0.0206 -0.0091 -0.0197 832  ASN A CA  
2172 C C   . ASN A 295 ? 0.2987 0.3042 0.3096 -0.0210 -0.0100 -0.0165 832  ASN A C   
2173 O O   . ASN A 295 ? 0.3002 0.3057 0.3094 -0.0215 -0.0098 -0.0152 832  ASN A O   
2174 C CB  . ASN A 295 ? 0.3053 0.3124 0.3272 -0.0249 -0.0045 -0.0238 832  ASN A CB  
2175 C CG  . ASN A 295 ? 0.5267 0.5365 0.5608 -0.0246 -0.0017 -0.0276 832  ASN A CG  
2176 O OD1 . ASN A 295 ? 0.4771 0.4871 0.5166 -0.0222 -0.0025 -0.0272 832  ASN A OD1 
2177 N ND2 . ASN A 295 ? 0.4738 0.4856 0.5136 -0.0270 0.0015  -0.0312 832  ASN A ND2 
2178 N N   . LEU A 296 ? 0.2676 0.2715 0.2737 -0.0206 -0.0112 -0.0152 833  LEU A N   
2179 C CA  . LEU A 296 ? 0.2400 0.2427 0.2403 -0.0203 -0.0124 -0.0119 833  LEU A CA  
2180 C C   . LEU A 296 ? 0.2749 0.2800 0.2763 -0.0166 -0.0139 -0.0094 833  LEU A C   
2181 O O   . LEU A 296 ? 0.2545 0.2611 0.2549 -0.0169 -0.0142 -0.0069 833  LEU A O   
2182 C CB  . LEU A 296 ? 0.2609 0.2602 0.2573 -0.0202 -0.0133 -0.0111 833  LEU A CB  
2183 C CG  . LEU A 296 ? 0.3128 0.3109 0.3060 -0.0195 -0.0150 -0.0073 833  LEU A CG  
2184 C CD1 . LEU A 296 ? 0.3304 0.3275 0.3198 -0.0247 -0.0150 -0.0060 833  LEU A CD1 
2185 C CD2 . LEU A 296 ? 0.3946 0.3882 0.3857 -0.0180 -0.0161 -0.0065 833  LEU A CD2 
2186 N N   . THR A 297 ? 0.2470 0.2526 0.2498 -0.0140 -0.0149 -0.0099 834  THR A N   
2187 C CA  . THR A 297 ? 0.2325 0.2399 0.2347 -0.0116 -0.0156 -0.0077 834  THR A CA  
2188 C C   . THR A 297 ? 0.2320 0.2414 0.2370 -0.0128 -0.0156 -0.0067 834  THR A C   
2189 O O   . THR A 297 ? 0.2373 0.2486 0.2412 -0.0126 -0.0154 -0.0042 834  THR A O   
2190 C CB  . THR A 297 ? 0.3075 0.3140 0.3087 -0.0102 -0.0172 -0.0084 834  THR A CB  
2191 O OG1 . THR A 297 ? 0.3217 0.3252 0.3195 -0.0098 -0.0171 -0.0099 834  THR A OG1 
2192 C CG2 . THR A 297 ? 0.2671 0.2748 0.2652 -0.0090 -0.0173 -0.0062 834  THR A CG2 
2193 N N   . LEU A 298 ? 0.2473 0.2559 0.2565 -0.0140 -0.0155 -0.0087 835  LEU A N   
2194 C CA  . LEU A 298 ? 0.2313 0.2400 0.2433 -0.0151 -0.0151 -0.0083 835  LEU A CA  
2195 C C   . LEU A 298 ? 0.2391 0.2476 0.2479 -0.0181 -0.0135 -0.0080 835  LEU A C   
2196 O O   . LEU A 298 ? 0.2529 0.2617 0.2614 -0.0193 -0.0137 -0.0064 835  LEU A O   
2197 C CB  . LEU A 298 ? 0.2369 0.2444 0.2564 -0.0153 -0.0146 -0.0113 835  LEU A CB  
2198 C CG  . LEU A 298 ? 0.2928 0.3007 0.3170 -0.0128 -0.0181 -0.0103 835  LEU A CG  
2199 C CD1 . LEU A 298 ? 0.2790 0.2870 0.3145 -0.0125 -0.0176 -0.0132 835  LEU A CD1 
2200 C CD2 . LEU A 298 ? 0.3375 0.3448 0.3587 -0.0119 -0.0209 -0.0063 835  LEU A CD2 
2201 N N   . TRP A 299 ? 0.2580 0.2656 0.2639 -0.0202 -0.0123 -0.0092 836  TRP A N   
2202 C CA  . TRP A 299 ? 0.2729 0.2798 0.2741 -0.0241 -0.0120 -0.0081 836  TRP A CA  
2203 C C   . TRP A 299 ? 0.2319 0.2421 0.2321 -0.0229 -0.0144 -0.0036 836  TRP A C   
2204 O O   . TRP A 299 ? 0.2536 0.2648 0.2526 -0.0255 -0.0152 -0.0018 836  TRP A O   
2205 C CB  . TRP A 299 ? 0.2755 0.2799 0.2723 -0.0274 -0.0111 -0.0095 836  TRP A CB  
2206 C CG  . TRP A 299 ? 0.2620 0.2647 0.2520 -0.0327 -0.0118 -0.0078 836  TRP A CG  
2207 C CD1 . TRP A 299 ? 0.3300 0.3304 0.3163 -0.0378 -0.0100 -0.0097 836  TRP A CD1 
2208 C CD2 . TRP A 299 ? 0.2730 0.2755 0.2590 -0.0338 -0.0151 -0.0036 836  TRP A CD2 
2209 N NE1 . TRP A 299 ? 0.3479 0.3468 0.3265 -0.0429 -0.0125 -0.0068 836  TRP A NE1 
2210 C CE2 . TRP A 299 ? 0.2986 0.2991 0.2778 -0.0403 -0.0161 -0.0026 836  TRP A CE2 
2211 C CE3 . TRP A 299 ? 0.2996 0.3028 0.2873 -0.0301 -0.0175 -0.0008 836  TRP A CE3 
2212 C CZ2 . TRP A 299 ? 0.2953 0.2950 0.2698 -0.0433 -0.0205 0.0023  836  TRP A CZ2 
2213 C CZ3 . TRP A 299 ? 0.3457 0.3478 0.3304 -0.0321 -0.0212 0.0036  836  TRP A CZ3 
2214 C CH2 . TRP A 299 ? 0.3383 0.3390 0.3167 -0.0387 -0.0233 0.0056  836  TRP A CH2 
2215 N N   . PHE A 300 ? 0.2219 0.2337 0.2231 -0.0191 -0.0153 -0.0020 837  PHE A N   
2216 C CA  . PHE A 300 ? 0.2248 0.2407 0.2277 -0.0172 -0.0164 0.0016  837  PHE A CA  
2217 C C   . PHE A 300 ? 0.2969 0.3156 0.3016 -0.0173 -0.0161 0.0028  837  PHE A C   
2218 O O   . PHE A 300 ? 0.2487 0.2712 0.2551 -0.0188 -0.0169 0.0057  837  PHE A O   
2219 C CB  . PHE A 300 ? 0.2288 0.2450 0.2329 -0.0128 -0.0159 0.0017  837  PHE A CB  
2220 C CG  . PHE A 300 ? 0.2519 0.2651 0.2549 -0.0127 -0.0169 0.0020  837  PHE A CG  
2221 C CD1 . PHE A 300 ? 0.2694 0.2833 0.2728 -0.0150 -0.0194 0.0053  837  PHE A CD1 
2222 C CD2 . PHE A 300 ? 0.2717 0.2809 0.2729 -0.0109 -0.0161 -0.0004 837  PHE A CD2 
2223 C CE1 . PHE A 300 ? 0.3075 0.3174 0.3094 -0.0151 -0.0212 0.0065  837  PHE A CE1 
2224 C CE2 . PHE A 300 ? 0.3094 0.3146 0.3092 -0.0112 -0.0173 0.0003  837  PHE A CE2 
2225 C CZ  . PHE A 300 ? 0.2467 0.2521 0.2469 -0.0131 -0.0199 0.0039  837  PHE A CZ  
2226 N N   . GLU A 301 ? 0.2501 0.2670 0.2549 -0.0161 -0.0154 0.0011  838  GLU A N   
2227 C CA  . GLU A 301 ? 0.2454 0.2634 0.2509 -0.0167 -0.0156 0.0027  838  GLU A CA  
2228 C C   . GLU A 301 ? 0.2312 0.2479 0.2368 -0.0206 -0.0159 0.0029  838  GLU A C   
2229 O O   . GLU A 301 ? 0.2362 0.2554 0.2422 -0.0224 -0.0164 0.0055  838  GLU A O   
2230 C CB  . GLU A 301 ? 0.2174 0.2323 0.2228 -0.0152 -0.0163 0.0016  838  GLU A CB  
2231 C CG  . GLU A 301 ? 0.2382 0.2533 0.2411 -0.0125 -0.0162 0.0012  838  GLU A CG  
2232 C CD  . GLU A 301 ? 0.3360 0.3479 0.3383 -0.0120 -0.0184 0.0007  838  GLU A CD  
2233 O OE1 . GLU A 301 ? 0.2705 0.2806 0.2751 -0.0129 -0.0202 0.0018  838  GLU A OE1 
2234 O OE2 . GLU A 301 ? 0.2863 0.2971 0.2861 -0.0108 -0.0188 -0.0006 838  GLU A OE2 
2235 N N   . LYS A 302 ? 0.2321 0.2449 0.2373 -0.0225 -0.0152 -0.0003 839  LYS A N   
2236 C CA  . LYS A 302 ? 0.2334 0.2432 0.2372 -0.0269 -0.0147 -0.0014 839  LYS A CA  
2237 C C   . LYS A 302 ? 0.2651 0.2779 0.2658 -0.0306 -0.0162 0.0014  839  LYS A C   
2238 O O   . LYS A 302 ? 0.2754 0.2879 0.2751 -0.0341 -0.0169 0.0028  839  LYS A O   
2239 C CB  . LYS A 302 ? 0.2356 0.2408 0.2389 -0.0285 -0.0122 -0.0063 839  LYS A CB  
2240 C CG  . LYS A 302 ? 0.2889 0.2894 0.2896 -0.0336 -0.0102 -0.0091 839  LYS A CG  
2241 C CD  . LYS A 302 ? 0.3076 0.3043 0.3075 -0.0358 -0.0062 -0.0146 839  LYS A CD  
2242 C CE  . LYS A 302 ? 0.3851 0.3760 0.3798 -0.0420 -0.0032 -0.0182 839  LYS A CE  
2243 N NZ  . LYS A 302 ? 0.4989 0.4858 0.4957 -0.0433 0.0025  -0.0249 839  LYS A NZ  
2244 N N   . CYS A 303 ? 0.2549 0.2700 0.2545 -0.0302 -0.0173 0.0028  840  CYS A N   
2245 C CA  . CYS A 303 ? 0.2365 0.2550 0.2350 -0.0335 -0.0201 0.0066  840  CYS A CA  
2246 C C   . CYS A 303 ? 0.2793 0.3043 0.2829 -0.0324 -0.0213 0.0105  840  CYS A C   
2247 O O   . CYS A 303 ? 0.2654 0.2930 0.2691 -0.0367 -0.0236 0.0131  840  CYS A O   
2248 C CB  . CYS A 303 ? 0.2677 0.2873 0.2661 -0.0320 -0.0219 0.0083  840  CYS A CB  
2249 S SG  . CYS A 303 ? 0.3198 0.3321 0.3101 -0.0361 -0.0209 0.0048  840  CYS A SG  
2250 N N   . ILE A 304 ? 0.2450 0.2729 0.2527 -0.0273 -0.0196 0.0107  841  ILE A N   
2251 C CA  . ILE A 304 ? 0.2393 0.2738 0.2518 -0.0265 -0.0193 0.0139  841  ILE A CA  
2252 C C   . ILE A 304 ? 0.2720 0.3047 0.2827 -0.0302 -0.0192 0.0143  841  ILE A C   
2253 O O   . ILE A 304 ? 0.2724 0.3094 0.2853 -0.0338 -0.0205 0.0172  841  ILE A O   
2254 C CB  . ILE A 304 ? 0.2201 0.2567 0.2348 -0.0212 -0.0166 0.0134  841  ILE A CB  
2255 C CG1 . ILE A 304 ? 0.2354 0.2738 0.2534 -0.0175 -0.0166 0.0135  841  ILE A CG1 
2256 C CG2 . ILE A 304 ? 0.2383 0.2812 0.2566 -0.0214 -0.0147 0.0159  841  ILE A CG2 
2257 C CD1 . ILE A 304 ? 0.2662 0.3032 0.2832 -0.0128 -0.0135 0.0111  841  ILE A CD1 
2258 N N   A VAL A 305 ? 0.2408 0.2670 0.2484 -0.0294 -0.0180 0.0116  842  VAL A N   
2259 N N   B VAL A 305 ? 0.2373 0.2636 0.2449 -0.0295 -0.0180 0.0116  842  VAL A N   
2260 C CA  A VAL A 305 ? 0.2675 0.2906 0.2740 -0.0321 -0.0181 0.0122  842  VAL A CA  
2261 C CA  B VAL A 305 ? 0.2754 0.2989 0.2820 -0.0324 -0.0182 0.0125  842  VAL A CA  
2262 C C   A VAL A 305 ? 0.2937 0.3126 0.2977 -0.0377 -0.0191 0.0113  842  VAL A C   
2263 C C   B VAL A 305 ? 0.2807 0.2997 0.2847 -0.0379 -0.0192 0.0113  842  VAL A C   
2264 O O   A VAL A 305 ? 0.3198 0.3377 0.3233 -0.0413 -0.0198 0.0130  842  VAL A O   
2265 O O   B VAL A 305 ? 0.3144 0.3320 0.3177 -0.0416 -0.0198 0.0129  842  VAL A O   
2266 C CB  A VAL A 305 ? 0.2778 0.2947 0.2834 -0.0292 -0.0176 0.0103  842  VAL A CB  
2267 C CB  B VAL A 305 ? 0.2909 0.3084 0.2965 -0.0298 -0.0177 0.0110  842  VAL A CB  
2268 C CG1 A VAL A 305 ? 0.2561 0.2693 0.2610 -0.0316 -0.0184 0.0122  842  VAL A CG1 
2269 C CG1 B VAL A 305 ? 0.2611 0.2819 0.2665 -0.0258 -0.0169 0.0120  842  VAL A CG1 
2270 C CG2 A VAL A 305 ? 0.2817 0.3016 0.2873 -0.0250 -0.0169 0.0108  842  VAL A CG2 
2271 C CG2 B VAL A 305 ? 0.2968 0.3081 0.3025 -0.0289 -0.0174 0.0068  842  VAL A CG2 
2272 N N   . GLU A 306 ? 0.2919 0.3077 0.2931 -0.0392 -0.0191 0.0084  843  GLU A N   
2273 C CA  . GLU A 306 ? 0.2968 0.3074 0.2931 -0.0456 -0.0195 0.0066  843  GLU A CA  
2274 C C   . GLU A 306 ? 0.3599 0.3761 0.3550 -0.0506 -0.0228 0.0105  843  GLU A C   
2275 O O   . GLU A 306 ? 0.3977 0.4098 0.3875 -0.0573 -0.0238 0.0097  843  GLU A O   
2276 C CB  . GLU A 306 ? 0.2894 0.2939 0.2818 -0.0465 -0.0173 0.0015  843  GLU A CB  
2277 C CG  . GLU A 306 ? 0.3134 0.3117 0.3088 -0.0431 -0.0142 -0.0027 843  GLU A CG  
2278 C CD  . GLU A 306 ? 0.4287 0.4212 0.4215 -0.0451 -0.0106 -0.0086 843  GLU A CD  
2279 O OE1 . GLU A 306 ? 0.3967 0.3896 0.3832 -0.0490 -0.0106 -0.0092 843  GLU A OE1 
2280 O OE2 . GLU A 306 ? 0.3900 0.3776 0.3875 -0.0428 -0.0078 -0.0125 843  GLU A OE2 
2281 N N   . ALA A 307 ? 0.3326 0.3579 0.3334 -0.0477 -0.0245 0.0146  844  ALA A N   
2282 C CA  . ALA A 307 ? 0.3009 0.3334 0.3043 -0.0518 -0.0284 0.0193  844  ALA A CA  
2283 C C   . ALA A 307 ? 0.3387 0.3754 0.3461 -0.0537 -0.0282 0.0219  844  ALA A C   
2284 O O   . ALA A 307 ? 0.3237 0.3680 0.3384 -0.0499 -0.0269 0.0244  844  ALA A O   
2285 C CB  . ALA A 307 ? 0.2957 0.3364 0.3063 -0.0472 -0.0299 0.0225  844  ALA A CB  
2286 N N   . GLU A 308 ? 0.3243 0.3552 0.3263 -0.0602 -0.0290 0.0210  845  GLU A N   
2287 C CA  . GLU A 308 ? 0.3065 0.3390 0.3109 -0.0627 -0.0286 0.0232  845  GLU A CA  
2288 C C   . GLU A 308 ? 0.3508 0.3954 0.3627 -0.0660 -0.0317 0.0288  845  GLU A C   
2289 O O   . GLU A 308 ? 0.3173 0.3684 0.3353 -0.0653 -0.0301 0.0314  845  GLU A O   
2290 C CB  . GLU A 308 ? 0.3341 0.3548 0.3305 -0.0684 -0.0283 0.0200  845  GLU A CB  
2291 C CG  . GLU A 308 ? 0.4147 0.4247 0.4076 -0.0642 -0.0248 0.0145  845  GLU A CG  
2292 C CD  . GLU A 308 ? 0.6360 0.6334 0.6230 -0.0689 -0.0235 0.0105  845  GLU A CD  
2293 O OE1 . GLU A 308 ? 0.6471 0.6429 0.6312 -0.0757 -0.0254 0.0121  845  GLU A OE1 
2294 O OE2 . GLU A 308 ? 0.6714 0.6605 0.6574 -0.0658 -0.0205 0.0055  845  GLU A OE2 
2295 N N   . ASN A 309 ? 0.2970 0.3452 0.3091 -0.0699 -0.0362 0.0307  846  ASN A N   
2296 C CA  . ASN A 309 ? 0.3244 0.3858 0.3470 -0.0723 -0.0401 0.0366  846  ASN A CA  
2297 C C   . ASN A 309 ? 0.3222 0.3944 0.3574 -0.0640 -0.0376 0.0386  846  ASN A C   
2298 O O   . ASN A 309 ? 0.2882 0.3586 0.3233 -0.0582 -0.0367 0.0369  846  ASN A O   
2299 C CB  . ASN A 309 ? 0.3271 0.3888 0.3465 -0.0783 -0.0469 0.0388  846  ASN A CB  
2300 C CG  . ASN A 309 ? 0.3390 0.4156 0.3723 -0.0800 -0.0522 0.0457  846  ASN A CG  
2301 O OD1 . ASN A 309 ? 0.3385 0.4228 0.3818 -0.0746 -0.0540 0.0486  846  ASN A OD1 
2302 N ND2 . ASN A 309 ? 0.3707 0.4513 0.4057 -0.0876 -0.0551 0.0485  846  ASN A ND2 
2303 N N   . PHE A 310 ? 0.3433 0.4261 0.3890 -0.0639 -0.0358 0.0416  847  PHE A N   
2304 C CA  . PHE A 310 ? 0.2864 0.3783 0.3432 -0.0563 -0.0312 0.0421  847  PHE A CA  
2305 C C   . PHE A 310 ? 0.2993 0.3981 0.3662 -0.0517 -0.0342 0.0442  847  PHE A C   
2306 O O   . PHE A 310 ? 0.2589 0.3561 0.3271 -0.0444 -0.0308 0.0418  847  PHE A O   
2307 C CB  . PHE A 310 ? 0.2701 0.3734 0.3371 -0.0585 -0.0283 0.0450  847  PHE A CB  
2308 C CG  . PHE A 310 ? 0.3131 0.4250 0.3904 -0.0514 -0.0218 0.0444  847  PHE A CG  
2309 C CD1 . PHE A 310 ? 0.3603 0.4646 0.4290 -0.0468 -0.0161 0.0403  847  PHE A CD1 
2310 C CD2 . PHE A 310 ? 0.3077 0.4350 0.4034 -0.0495 -0.0213 0.0476  847  PHE A CD2 
2311 C CE1 . PHE A 310 ? 0.3204 0.4311 0.3961 -0.0412 -0.0096 0.0389  847  PHE A CE1 
2312 C CE2 . PHE A 310 ? 0.3801 0.5143 0.4851 -0.0430 -0.0139 0.0458  847  PHE A CE2 
2313 C CZ  . PHE A 310 ? 0.3512 0.4765 0.4448 -0.0393 -0.0078 0.0412  847  PHE A CZ  
2314 N N   . GLU A 311 ? 0.2646 0.3700 0.3383 -0.0562 -0.0410 0.0489  848  GLU A N   
2315 C CA  . GLU A 311 ? 0.2723 0.3841 0.3572 -0.0520 -0.0452 0.0522  848  GLU A CA  
2316 C C   . GLU A 311 ? 0.2888 0.3885 0.3619 -0.0496 -0.0467 0.0495  848  GLU A C   
2317 O O   . GLU A 311 ? 0.2738 0.3747 0.3534 -0.0427 -0.0462 0.0496  848  GLU A O   
2318 C CB  . GLU A 311 ? 0.3316 0.4519 0.4249 -0.0587 -0.0542 0.0588  848  GLU A CB  
2319 C CG  . GLU A 311 ? 0.3839 0.5204 0.4957 -0.0596 -0.0530 0.0625  848  GLU A CG  
2320 C CD  . GLU A 311 ? 0.4655 0.6001 0.5696 -0.0657 -0.0490 0.0605  848  GLU A CD  
2321 O OE1 . GLU A 311 ? 0.4089 0.5306 0.4951 -0.0717 -0.0507 0.0581  848  GLU A OE1 
2322 O OE2 . GLU A 311 ? 0.4886 0.6340 0.6047 -0.0647 -0.0438 0.0613  848  GLU A OE2 
2323 N N   . GLU A 312 ? 0.2664 0.3542 0.3225 -0.0554 -0.0480 0.0467  849  GLU A N   
2324 C CA  . GLU A 312 ? 0.2931 0.3695 0.3373 -0.0542 -0.0484 0.0435  849  GLU A CA  
2325 C C   . GLU A 312 ? 0.3255 0.3983 0.3692 -0.0458 -0.0413 0.0388  849  GLU A C   
2326 O O   . GLU A 312 ? 0.2891 0.3587 0.3324 -0.0414 -0.0413 0.0380  849  GLU A O   
2327 C CB  . GLU A 312 ? 0.3573 0.4221 0.3845 -0.0622 -0.0491 0.0402  849  GLU A CB  
2328 C CG  . GLU A 312 ? 0.5259 0.5795 0.5407 -0.0625 -0.0488 0.0366  849  GLU A CG  
2329 C CD  . GLU A 312 ? 0.8197 0.8624 0.8188 -0.0710 -0.0486 0.0328  849  GLU A CD  
2330 O OE1 . GLU A 312 ? 0.7752 0.8190 0.7720 -0.0786 -0.0521 0.0347  849  GLU A OE1 
2331 O OE2 . GLU A 312 ? 0.8920 0.9252 0.8818 -0.0704 -0.0447 0.0274  849  GLU A OE2 
2332 N N   . ARG A 313 ? 0.2536 0.3266 0.2971 -0.0443 -0.0357 0.0362  850  ARG A N   
2333 C CA  . ARG A 313 ? 0.2259 0.2946 0.2669 -0.0378 -0.0298 0.0320  850  ARG A CA  
2334 C C   . ARG A 313 ? 0.2564 0.3325 0.3089 -0.0307 -0.0276 0.0330  850  ARG A C   
2335 O O   . ARG A 313 ? 0.2407 0.3120 0.2909 -0.0256 -0.0254 0.0302  850  ARG A O   
2336 C CB  . ARG A 313 ? 0.2200 0.2869 0.2574 -0.0389 -0.0256 0.0301  850  ARG A CB  
2337 C CG  . ARG A 313 ? 0.2486 0.3097 0.2812 -0.0336 -0.0209 0.0262  850  ARG A CG  
2338 C CD  . ARG A 313 ? 0.2594 0.3149 0.2854 -0.0361 -0.0189 0.0249  850  ARG A CD  
2339 N NE  . ARG A 313 ? 0.2796 0.3421 0.3100 -0.0381 -0.0167 0.0277  850  ARG A NE  
2340 C CZ  . ARG A 313 ? 0.3146 0.3786 0.3453 -0.0442 -0.0184 0.0301  850  ARG A CZ  
2341 N NH1 . ARG A 313 ? 0.2877 0.3462 0.3140 -0.0490 -0.0223 0.0298  850  ARG A NH1 
2342 N NH2 . ARG A 313 ? 0.3005 0.3712 0.3352 -0.0463 -0.0158 0.0325  850  ARG A NH2 
2343 N N   . VAL A 314 ? 0.2400 0.3277 0.3059 -0.0306 -0.0279 0.0367  851  VAL A N   
2344 C CA  . VAL A 314 ? 0.2542 0.3493 0.3335 -0.0236 -0.0251 0.0373  851  VAL A CA  
2345 C C   . VAL A 314 ? 0.2730 0.3649 0.3544 -0.0209 -0.0301 0.0389  851  VAL A C   
2346 O O   . VAL A 314 ? 0.2640 0.3539 0.3488 -0.0144 -0.0271 0.0368  851  VAL A O   
2347 C CB  . VAL A 314 ? 0.2455 0.3553 0.3417 -0.0243 -0.0244 0.0412  851  VAL A CB  
2348 C CG1 . VAL A 314 ? 0.3266 0.4440 0.4396 -0.0166 -0.0218 0.0416  851  VAL A CG1 
2349 C CG2 . VAL A 314 ? 0.2561 0.3682 0.3490 -0.0269 -0.0181 0.0393  851  VAL A CG2 
2350 N N   . ALA A 315 ? 0.2897 0.3797 0.3675 -0.0266 -0.0378 0.0426  852  ALA A N   
2351 C CA  . ALA A 315 ? 0.2749 0.3607 0.3526 -0.0257 -0.0436 0.0451  852  ALA A CA  
2352 C C   . ALA A 315 ? 0.2448 0.3178 0.3080 -0.0242 -0.0411 0.0402  852  ALA A C   
2353 O O   . ALA A 315 ? 0.2665 0.3358 0.3315 -0.0201 -0.0423 0.0406  852  ALA A O   
2354 C CB  . ALA A 315 ? 0.2954 0.3815 0.3696 -0.0340 -0.0527 0.0504  852  ALA A CB  
2355 N N   . VAL A 316 ? 0.2534 0.3198 0.3037 -0.0273 -0.0376 0.0357  853  VAL A N   
2356 C CA  . VAL A 316 ? 0.2085 0.2642 0.2473 -0.0259 -0.0348 0.0308  853  VAL A CA  
2357 C C   . VAL A 316 ? 0.2493 0.3050 0.2925 -0.0182 -0.0294 0.0277  853  VAL A C   
2358 O O   . VAL A 316 ? 0.2561 0.3059 0.2966 -0.0153 -0.0294 0.0263  853  VAL A O   
2359 C CB  . VAL A 316 ? 0.2554 0.3051 0.2829 -0.0304 -0.0324 0.0268  853  VAL A CB  
2360 C CG1 . VAL A 316 ? 0.2911 0.3329 0.3116 -0.0273 -0.0283 0.0216  853  VAL A CG1 
2361 C CG2 . VAL A 316 ? 0.2786 0.3243 0.2977 -0.0387 -0.0370 0.0281  853  VAL A CG2 
2362 N N   . LEU A 317 ? 0.2533 0.3147 0.3019 -0.0157 -0.0247 0.0267  854  LEU A N   
2363 C CA  . LEU A 317 ? 0.2506 0.3116 0.3016 -0.0094 -0.0190 0.0234  854  LEU A CA  
2364 C C   . LEU A 317 ? 0.2761 0.3397 0.3382 -0.0042 -0.0198 0.0251  854  LEU A C   
2365 O O   . LEU A 317 ? 0.2754 0.3333 0.3355 0.0000  -0.0173 0.0221  854  LEU A O   
2366 C CB  . LEU A 317 ? 0.2163 0.2835 0.2704 -0.0091 -0.0137 0.0225  854  LEU A CB  
2367 C CG  . LEU A 317 ? 0.2757 0.3415 0.3293 -0.0042 -0.0071 0.0185  854  LEU A CG  
2368 C CD1 . LEU A 317 ? 0.2913 0.3462 0.3321 -0.0037 -0.0069 0.0145  854  LEU A CD1 
2369 C CD2 . LEU A 317 ? 0.2963 0.3677 0.3505 -0.0057 -0.0018 0.0180  854  LEU A CD2 
2370 N N   . SER A 318 ? 0.2666 0.3387 0.3411 -0.0047 -0.0236 0.0302  855  SER A N   
2371 C CA  . SER A 318 ? 0.2380 0.3130 0.3261 0.0006  -0.0255 0.0328  855  SER A CA  
2372 C C   . SER A 318 ? 0.2380 0.3026 0.3187 0.0004  -0.0305 0.0337  855  SER A C   
2373 O O   . SER A 318 ? 0.2758 0.3367 0.3615 0.0059  -0.0293 0.0328  855  SER A O   
2374 C CB  . SER A 318 ? 0.2640 0.3506 0.3679 -0.0009 -0.0305 0.0392  855  SER A CB  
2375 O OG  . SER A 318 ? 0.3238 0.4207 0.4359 -0.0007 -0.0250 0.0383  855  SER A OG  
2376 N N   . ARG A 319 ? 0.2920 0.3513 0.3604 -0.0064 -0.0355 0.0350  856  ARG A N   
2377 C CA  . ARG A 319 ? 0.2636 0.3130 0.3230 -0.0083 -0.0398 0.0359  856  ARG A CA  
2378 C C   . ARG A 319 ? 0.2721 0.3128 0.3228 -0.0053 -0.0343 0.0298  856  ARG A C   
2379 O O   . ARG A 319 ? 0.2819 0.3157 0.3313 -0.0032 -0.0357 0.0300  856  ARG A O   
2380 C CB  . ARG A 319 ? 0.2580 0.3036 0.3046 -0.0173 -0.0446 0.0375  856  ARG A CB  
2381 C CG  . ARG A 319 ? 0.2419 0.2790 0.2803 -0.0212 -0.0505 0.0405  856  ARG A CG  
2382 C CD  . ARG A 319 ? 0.2617 0.3026 0.3119 -0.0202 -0.0586 0.0485  856  ARG A CD  
2383 N NE  . ARG A 319 ? 0.2843 0.3341 0.3400 -0.0248 -0.0635 0.0532  856  ARG A NE  
2384 C CZ  . ARG A 319 ? 0.3323 0.3793 0.3767 -0.0343 -0.0697 0.0563  856  ARG A CZ  
2385 N NH1 . ARG A 319 ? 0.3181 0.3539 0.3450 -0.0404 -0.0710 0.0551  856  ARG A NH1 
2386 N NH2 . ARG A 319 ? 0.3477 0.4032 0.3977 -0.0387 -0.0742 0.0604  856  ARG A NH2 
2387 N N   . ILE A 320 ? 0.2416 0.2825 0.2866 -0.0055 -0.0288 0.0250  857  ILE A N   
2388 C CA  . ILE A 320 ? 0.2351 0.2688 0.2724 -0.0032 -0.0243 0.0195  857  ILE A CA  
2389 C C   . ILE A 320 ? 0.2724 0.3058 0.3174 0.0037  -0.0206 0.0178  857  ILE A C   
2390 O O   . ILE A 320 ? 0.2614 0.2870 0.3018 0.0055  -0.0196 0.0151  857  ILE A O   
2391 C CB  . ILE A 320 ? 0.2638 0.2980 0.2945 -0.0052 -0.0205 0.0158  857  ILE A CB  
2392 C CG1 . ILE A 320 ? 0.2407 0.2720 0.2632 -0.0115 -0.0232 0.0160  857  ILE A CG1 
2393 C CG2 . ILE A 320 ? 0.2492 0.2779 0.2745 -0.0023 -0.0163 0.0108  857  ILE A CG2 
2394 C CD1 . ILE A 320 ? 0.2745 0.3063 0.2929 -0.0137 -0.0208 0.0135  857  ILE A CD1 
2395 N N   . ILE A 321 ? 0.2509 0.2927 0.3080 0.0072  -0.0184 0.0192  858  ILE A N   
2396 C CA  . ILE A 321 ? 0.2589 0.3000 0.3245 0.0139  -0.0139 0.0169  858  ILE A CA  
2397 C C   . ILE A 321 ? 0.2882 0.3245 0.3604 0.0166  -0.0188 0.0203  858  ILE A C   
2398 O O   . ILE A 321 ? 0.3252 0.3542 0.3975 0.0208  -0.0162 0.0173  858  ILE A O   
2399 C CB  . ILE A 321 ? 0.2717 0.3238 0.3505 0.0168  -0.0091 0.0171  858  ILE A CB  
2400 C CG1 . ILE A 321 ? 0.2896 0.3439 0.3594 0.0137  -0.0040 0.0137  858  ILE A CG1 
2401 C CG2 . ILE A 321 ? 0.3235 0.3748 0.4129 0.0239  -0.0036 0.0142  858  ILE A CG2 
2402 C CD1 . ILE A 321 ? 0.3200 0.3859 0.4008 0.0144  0.0008  0.0143  858  ILE A CD1 
2403 N N   . GLU A 322 ? 0.2652 0.3044 0.3416 0.0136  -0.0264 0.0267  859  GLU A N   
2404 C CA  . GLU A 322 ? 0.2615 0.2948 0.3424 0.0151  -0.0325 0.0310  859  GLU A CA  
2405 C C   . GLU A 322 ? 0.2879 0.3083 0.3533 0.0124  -0.0332 0.0285  859  GLU A C   
2406 O O   . GLU A 322 ? 0.3102 0.3226 0.3777 0.0158  -0.0341 0.0286  859  GLU A O   
2407 C CB  . GLU A 322 ? 0.3089 0.3469 0.3940 0.0105  -0.0416 0.0390  859  GLU A CB  
2408 C CG  . GLU A 322 ? 0.2889 0.3404 0.3940 0.0138  -0.0421 0.0426  859  GLU A CG  
2409 C CD  . GLU A 322 ? 0.4651 0.5213 0.5749 0.0087  -0.0527 0.0513  859  GLU A CD  
2410 O OE1 . GLU A 322 ? 0.4205 0.4731 0.5147 0.0004  -0.0567 0.0525  859  GLU A OE1 
2411 O OE2 . GLU A 322 ? 0.5806 0.6438 0.7099 0.0127  -0.0570 0.0568  859  GLU A OE2 
2412 N N   . ILE A 323 ? 0.2605 0.2787 0.3114 0.0063  -0.0328 0.0262  860  ILE A N   
2413 C CA  . ILE A 323 ? 0.2420 0.2498 0.2795 0.0033  -0.0325 0.0232  860  ILE A CA  
2414 C C   . ILE A 323 ? 0.2563 0.2593 0.2934 0.0084  -0.0264 0.0173  860  ILE A C   
2415 O O   . ILE A 323 ? 0.2664 0.2600 0.2997 0.0090  -0.0270 0.0163  860  ILE A O   
2416 C CB  . ILE A 323 ? 0.2681 0.2762 0.2934 -0.0034 -0.0317 0.0209  860  ILE A CB  
2417 C CG1 . ILE A 323 ? 0.2701 0.2800 0.2927 -0.0098 -0.0377 0.0261  860  ILE A CG1 
2418 C CG2 . ILE A 323 ? 0.3040 0.3034 0.3182 -0.0059 -0.0298 0.0167  860  ILE A CG2 
2419 C CD1 . ILE A 323 ? 0.3077 0.3195 0.3216 -0.0157 -0.0360 0.0236  860  ILE A CD1 
2420 N N   . LEU A 324 ? 0.2722 0.2808 0.3125 0.0115  -0.0206 0.0136  861  LEU A N   
2421 C CA  . LEU A 324 ? 0.2592 0.2631 0.2978 0.0155  -0.0147 0.0078  861  LEU A CA  
2422 C C   . LEU A 324 ? 0.2877 0.2864 0.3355 0.0212  -0.0143 0.0082  861  LEU A C   
2423 O O   . LEU A 324 ? 0.3257 0.3148 0.3682 0.0224  -0.0124 0.0046  861  LEU A O   
2424 C CB  . LEU A 324 ? 0.2735 0.2846 0.3138 0.0170  -0.0087 0.0046  861  LEU A CB  
2425 C CG  . LEU A 324 ? 0.3599 0.3654 0.3953 0.0197  -0.0022 -0.0017 861  LEU A CG  
2426 C CD1 . LEU A 324 ? 0.3532 0.3623 0.3807 0.0169  0.0012  -0.0045 861  LEU A CD1 
2427 C CD2 . LEU A 324 ? 0.3697 0.3764 0.4172 0.0260  0.0027  -0.0032 861  LEU A CD2 
2428 N N   . GLN A 325 ? 0.2874 0.2925 0.3501 0.0248  -0.0161 0.0126  862  GLN A N   
2429 C CA  . GLN A 325 ? 0.2644 0.2648 0.3393 0.0310  -0.0165 0.0138  862  GLN A CA  
2430 C C   . GLN A 325 ? 0.3123 0.3002 0.3806 0.0291  -0.0223 0.0163  862  GLN A C   
2431 O O   . GLN A 325 ? 0.3716 0.3497 0.4409 0.0329  -0.0202 0.0135  862  GLN A O   
2432 C CB  . GLN A 325 ? 0.3497 0.3602 0.4436 0.0342  -0.0200 0.0201  862  GLN A CB  
2433 C CG  . GLN A 325 ? 0.5921 0.6148 0.6974 0.0375  -0.0133 0.0177  862  GLN A CG  
2434 C CD  . GLN A 325 ? 0.6835 0.7173 0.8097 0.0401  -0.0181 0.0247  862  GLN A CD  
2435 O OE1 . GLN A 325 ? 0.6569 0.7002 0.7841 0.0356  -0.0220 0.0289  862  GLN A OE1 
2436 N NE2 . GLN A 325 ? 0.7262 0.7584 0.8698 0.0473  -0.0182 0.0261  862  GLN A NE2 
2437 N N   . VAL A 326 ? 0.2506 0.2383 0.3113 0.0226  -0.0293 0.0214  863  VAL A N   
2438 C CA  . VAL A 326 ? 0.2988 0.2747 0.3517 0.0194  -0.0347 0.0242  863  VAL A CA  
2439 C C   . VAL A 326 ? 0.3381 0.3049 0.3764 0.0167  -0.0305 0.0178  863  VAL A C   
2440 O O   . VAL A 326 ? 0.3516 0.3069 0.3868 0.0170  -0.0318 0.0175  863  VAL A O   
2441 C CB  . VAL A 326 ? 0.3210 0.2985 0.3674 0.0118  -0.0425 0.0308  863  VAL A CB  
2442 C CG1 . VAL A 326 ? 0.3614 0.3261 0.3986 0.0075  -0.0478 0.0341  863  VAL A CG1 
2443 C CG2 . VAL A 326 ? 0.3617 0.3482 0.4229 0.0137  -0.0481 0.0380  863  VAL A CG2 
2444 N N   . PHE A 327 ? 0.3080 0.2798 0.3382 0.0137  -0.0263 0.0131  864  PHE A N   
2445 C CA  . PHE A 327 ? 0.3167 0.2821 0.3361 0.0119  -0.0223 0.0067  864  PHE A CA  
2446 C C   . PHE A 327 ? 0.3399 0.2981 0.3627 0.0177  -0.0179 0.0024  864  PHE A C   
2447 O O   . PHE A 327 ? 0.3693 0.3167 0.3857 0.0165  -0.0179 0.0001  864  PHE A O   
2448 C CB  . PHE A 327 ? 0.3107 0.2837 0.3249 0.0097  -0.0185 0.0027  864  PHE A CB  
2449 C CG  . PHE A 327 ? 0.2702 0.2465 0.2774 0.0031  -0.0210 0.0041  864  PHE A CG  
2450 C CD1 . PHE A 327 ? 0.3145 0.2851 0.3155 -0.0021 -0.0246 0.0062  864  PHE A CD1 
2451 C CD2 . PHE A 327 ? 0.2779 0.2624 0.2845 0.0019  -0.0191 0.0027  864  PHE A CD2 
2452 C CE1 . PHE A 327 ? 0.3033 0.2768 0.2982 -0.0082 -0.0252 0.0062  864  PHE A CE1 
2453 C CE2 . PHE A 327 ? 0.3065 0.2932 0.3078 -0.0036 -0.0204 0.0029  864  PHE A CE2 
2454 C CZ  . PHE A 327 ? 0.2780 0.2596 0.2738 -0.0086 -0.0229 0.0043  864  PHE A CZ  
2455 N N   . GLN A 328 ? 0.3309 0.2950 0.3637 0.0234  -0.0135 0.0008  865  GLN A N   
2456 C CA  . GLN A 328 ? 0.3452 0.3027 0.3824 0.0292  -0.0078 -0.0042 865  GLN A CA  
2457 C C   . GLN A 328 ? 0.3693 0.3156 0.4128 0.0324  -0.0112 -0.0015 865  GLN A C   
2458 O O   . GLN A 328 ? 0.4241 0.3584 0.4625 0.0333  -0.0087 -0.0059 865  GLN A O   
2459 C CB  . GLN A 328 ? 0.4433 0.4105 0.4930 0.0346  -0.0022 -0.0055 865  GLN A CB  
2460 C CG  . GLN A 328 ? 0.5983 0.5718 0.6404 0.0326  0.0039  -0.0105 865  GLN A CG  
2461 C CD  . GLN A 328 ? 0.7246 0.6909 0.7622 0.0350  0.0121  -0.0185 865  GLN A CD  
2462 O OE1 . GLN A 328 ? 0.8904 0.8445 0.9247 0.0362  0.0126  -0.0214 865  GLN A OE1 
2463 N NE2 . GLN A 328 ? 0.6152 0.5880 0.6514 0.0350  0.0187  -0.0222 865  GLN A NE2 
2464 N N   . ASP A 329 ? 0.3594 0.3090 0.4135 0.0336  -0.0176 0.0062  866  ASP A N   
2465 C CA  . ASP A 329 ? 0.3738 0.3125 0.4346 0.0364  -0.0226 0.0104  866  ASP A CA  
2466 C C   . ASP A 329 ? 0.4188 0.3446 0.4641 0.0302  -0.0260 0.0104  866  ASP A C   
2467 O O   . ASP A 329 ? 0.4267 0.3393 0.4731 0.0323  -0.0271 0.0105  866  ASP A O   
2468 C CB  . ASP A 329 ? 0.3816 0.3267 0.4543 0.0368  -0.0310 0.0201  866  ASP A CB  
2469 C CG  . ASP A 329 ? 0.5978 0.5560 0.6894 0.0432  -0.0282 0.0209  866  ASP A CG  
2470 O OD1 . ASP A 329 ? 0.6203 0.5799 0.7185 0.0489  -0.0193 0.0140  866  ASP A OD1 
2471 O OD2 . ASP A 329 ? 0.6690 0.6361 0.7684 0.0417  -0.0349 0.0284  866  ASP A OD2 
2472 N N   . LEU A 330 ? 0.3638 0.2932 0.3955 0.0225  -0.0273 0.0102  867  LEU A N   
2473 C CA  . LEU A 330 ? 0.4369 0.3565 0.4546 0.0155  -0.0299 0.0101  867  LEU A CA  
2474 C C   . LEU A 330 ? 0.4012 0.3155 0.4091 0.0141  -0.0241 0.0019  867  LEU A C   
2475 O O   . LEU A 330 ? 0.4405 0.3484 0.4376 0.0079  -0.0255 0.0010  867  LEU A O   
2476 C CB  . LEU A 330 ? 0.3717 0.2981 0.3811 0.0076  -0.0336 0.0138  867  LEU A CB  
2477 C CG  . LEU A 330 ? 0.3658 0.2942 0.3790 0.0055  -0.0412 0.0227  867  LEU A CG  
2478 C CD1 . LEU A 330 ? 0.3535 0.2893 0.3572 -0.0026 -0.0424 0.0239  867  LEU A CD1 
2479 C CD2 . LEU A 330 ? 0.3587 0.2732 0.3692 0.0034  -0.0470 0.0278  867  LEU A CD2 
2480 N N   . ASN A 331 ? 0.3585 0.2759 0.3700 0.0190  -0.0176 -0.0040 868  ASN A N   
2481 C CA  . ASN A 331 ? 0.3916 0.3054 0.3926 0.0168  -0.0128 -0.0116 868  ASN A CA  
2482 C C   . ASN A 331 ? 0.3888 0.3092 0.3800 0.0096  -0.0141 -0.0122 868  ASN A C   
2483 O O   . ASN A 331 ? 0.4146 0.3297 0.3966 0.0055  -0.0134 -0.0162 868  ASN A O   
2484 C CB  . ASN A 331 ? 0.3927 0.2903 0.3883 0.0161  -0.0126 -0.0145 868  ASN A CB  
2485 C CG  . ASN A 331 ? 0.4950 0.3843 0.5005 0.0240  -0.0094 -0.0162 868  ASN A CG  
2486 O OD1 . ASN A 331 ? 0.4890 0.3853 0.5038 0.0298  -0.0047 -0.0181 868  ASN A OD1 
2487 N ND2 . ASN A 331 ? 0.5703 0.4446 0.5747 0.0241  -0.0115 -0.0156 868  ASN A ND2 
2488 N N   . ASN A 332 ? 0.3411 0.2728 0.3351 0.0081  -0.0161 -0.0084 869  ASN A N   
2489 C CA  . ASN A 332 ? 0.3373 0.2760 0.3248 0.0025  -0.0164 -0.0096 869  ASN A CA  
2490 C C   . ASN A 332 ? 0.4024 0.3488 0.3903 0.0048  -0.0124 -0.0131 869  ASN A C   
2491 O O   . ASN A 332 ? 0.3279 0.2837 0.3208 0.0060  -0.0122 -0.0109 869  ASN A O   
2492 C CB  . ASN A 332 ? 0.3195 0.2646 0.3081 -0.0012 -0.0201 -0.0043 869  ASN A CB  
2493 C CG  . ASN A 332 ? 0.3354 0.2875 0.3195 -0.0062 -0.0194 -0.0064 869  ASN A CG  
2494 O OD1 . ASN A 332 ? 0.3404 0.2932 0.3215 -0.0066 -0.0172 -0.0107 869  ASN A OD1 
2495 N ND2 . ASN A 332 ? 0.3359 0.2926 0.3195 -0.0102 -0.0213 -0.0033 869  ASN A ND2 
2496 N N   . PHE A 333 ? 0.3710 0.3127 0.3528 0.0044  -0.0095 -0.0185 870  PHE A N   
2497 C CA  . PHE A 333 ? 0.3676 0.3151 0.3474 0.0055  -0.0061 -0.0215 870  PHE A CA  
2498 C C   . PHE A 333 ? 0.3737 0.3292 0.3507 0.0011  -0.0084 -0.0207 870  PHE A C   
2499 O O   . PHE A 333 ? 0.3693 0.3315 0.3463 0.0017  -0.0069 -0.0209 870  PHE A O   
2500 C CB  . PHE A 333 ? 0.4269 0.3654 0.3990 0.0057  -0.0025 -0.0275 870  PHE A CB  
2501 C CG  . PHE A 333 ? 0.4678 0.3991 0.4449 0.0113  0.0016  -0.0293 870  PHE A CG  
2502 C CD1 . PHE A 333 ? 0.4945 0.4314 0.4786 0.0162  0.0065  -0.0299 870  PHE A CD1 
2503 C CD2 . PHE A 333 ? 0.6273 0.5466 0.6037 0.0117  0.0006  -0.0301 870  PHE A CD2 
2504 C CE1 . PHE A 333 ? 0.6039 0.5351 0.5959 0.0221  0.0109  -0.0318 870  PHE A CE1 
2505 C CE2 . PHE A 333 ? 0.5789 0.4910 0.5621 0.0177  0.0043  -0.0317 870  PHE A CE2 
2506 C CZ  . PHE A 333 ? 0.6381 0.5565 0.6300 0.0232  0.0096  -0.0327 870  PHE A CZ  
2507 N N   . ASN A 334 ? 0.3753 0.3302 0.3506 -0.0033 -0.0117 -0.0196 871  ASN A N   
2508 C CA  . ASN A 334 ? 0.3428 0.3057 0.3190 -0.0066 -0.0136 -0.0187 871  ASN A CA  
2509 C C   . ASN A 334 ? 0.3724 0.3434 0.3544 -0.0048 -0.0134 -0.0153 871  ASN A C   
2510 O O   . ASN A 334 ? 0.3298 0.3072 0.3127 -0.0047 -0.0130 -0.0151 871  ASN A O   
2511 C CB  . ASN A 334 ? 0.3572 0.3187 0.3328 -0.0115 -0.0158 -0.0184 871  ASN A CB  
2512 C CG  . ASN A 334 ? 0.4918 0.4609 0.4700 -0.0146 -0.0169 -0.0188 871  ASN A CG  
2513 O OD1 . ASN A 334 ? 0.5112 0.4813 0.4880 -0.0159 -0.0180 -0.0209 871  ASN A OD1 
2514 N ND2 . ASN A 334 ? 0.4416 0.4159 0.4238 -0.0158 -0.0168 -0.0167 871  ASN A ND2 
2515 N N   . GLY A 335 ? 0.3112 0.2812 0.2968 -0.0037 -0.0142 -0.0120 872  GLY A N   
2516 C CA  . GLY A 335 ? 0.2645 0.2415 0.2552 -0.0027 -0.0147 -0.0084 872  GLY A CA  
2517 C C   . GLY A 335 ? 0.2873 0.2689 0.2821 0.0017  -0.0121 -0.0085 872  GLY A C   
2518 O O   . GLY A 335 ? 0.2882 0.2770 0.2855 0.0014  -0.0120 -0.0069 872  GLY A O   
2519 N N   . VAL A 336 ? 0.2739 0.2508 0.2695 0.0056  -0.0095 -0.0105 873  VAL A N   
2520 C CA  . VAL A 336 ? 0.2920 0.2736 0.2918 0.0094  -0.0055 -0.0113 873  VAL A CA  
2521 C C   . VAL A 336 ? 0.2954 0.2810 0.2893 0.0071  -0.0040 -0.0133 873  VAL A C   
2522 O O   . VAL A 336 ? 0.2941 0.2869 0.2912 0.0076  -0.0026 -0.0117 873  VAL A O   
2523 C CB  . VAL A 336 ? 0.2929 0.2675 0.2935 0.0135  -0.0013 -0.0149 873  VAL A CB  
2524 C CG1 . VAL A 336 ? 0.3104 0.2900 0.3136 0.0163  0.0046  -0.0171 873  VAL A CG1 
2525 C CG2 . VAL A 336 ? 0.2901 0.2608 0.2994 0.0169  -0.0033 -0.0118 873  VAL A CG2 
2526 N N   . LEU A 337 ? 0.2893 0.2700 0.2749 0.0042  -0.0048 -0.0163 874  LEU A N   
2527 C CA  . LEU A 337 ? 0.3567 0.3399 0.3363 0.0018  -0.0046 -0.0175 874  LEU A CA  
2528 C C   . LEU A 337 ? 0.3499 0.3392 0.3319 -0.0009 -0.0081 -0.0145 874  LEU A C   
2529 O O   . LEU A 337 ? 0.3280 0.3207 0.3078 -0.0021 -0.0083 -0.0139 874  LEU A O   
2530 C CB  . LEU A 337 ? 0.3351 0.3110 0.3052 -0.0008 -0.0051 -0.0213 874  LEU A CB  
2531 C CG  . LEU A 337 ? 0.4414 0.4109 0.4053 0.0007  -0.0001 -0.0255 874  LEU A CG  
2532 C CD1 . LEU A 337 ? 0.4604 0.4350 0.4252 0.0025  0.0049  -0.0255 874  LEU A CD1 
2533 C CD2 . LEU A 337 ? 0.6039 0.5667 0.5714 0.0039  0.0019  -0.0272 874  LEU A CD2 
2534 N N   . GLU A 338 ? 0.2988 0.2890 0.2850 -0.0020 -0.0107 -0.0128 875  GLU A N   
2535 C CA  . GLU A 338 ? 0.2933 0.2889 0.2828 -0.0041 -0.0126 -0.0107 875  GLU A CA  
2536 C C   . GLU A 338 ? 0.2861 0.2873 0.2793 -0.0027 -0.0113 -0.0080 875  GLU A C   
2537 O O   . GLU A 338 ? 0.2855 0.2903 0.2792 -0.0040 -0.0120 -0.0069 875  GLU A O   
2538 C CB  . GLU A 338 ? 0.3514 0.3461 0.3432 -0.0064 -0.0141 -0.0100 875  GLU A CB  
2539 C CG  . GLU A 338 ? 0.4571 0.4486 0.4471 -0.0091 -0.0153 -0.0125 875  GLU A CG  
2540 C CD  . GLU A 338 ? 0.4023 0.3913 0.3925 -0.0120 -0.0157 -0.0122 875  GLU A CD  
2541 O OE1 . GLU A 338 ? 0.4112 0.3984 0.4011 -0.0114 -0.0158 -0.0098 875  GLU A OE1 
2542 O OE2 . GLU A 338 ? 0.4873 0.4763 0.4783 -0.0152 -0.0159 -0.0140 875  GLU A OE2 
2543 N N   . ILE A 339 ? 0.2580 0.2600 0.2550 -0.0002 -0.0099 -0.0067 876  ILE A N   
2544 C CA  . ILE A 339 ? 0.2347 0.2433 0.2369 0.0009  -0.0088 -0.0039 876  ILE A CA  
2545 C C   . ILE A 339 ? 0.2924 0.3032 0.2923 0.0019  -0.0053 -0.0052 876  ILE A C   
2546 O O   . ILE A 339 ? 0.2606 0.2764 0.2617 0.0005  -0.0050 -0.0033 876  ILE A O   
2547 C CB  . ILE A 339 ? 0.2543 0.2640 0.2636 0.0035  -0.0090 -0.0016 876  ILE A CB  
2548 C CG1 . ILE A 339 ? 0.2506 0.2593 0.2600 0.0003  -0.0133 0.0010  876  ILE A CG1 
2549 C CG2 . ILE A 339 ? 0.2484 0.2660 0.2650 0.0052  -0.0071 0.0007  876  ILE A CG2 
2550 C CD1 . ILE A 339 ? 0.2711 0.2786 0.2860 0.0019  -0.0157 0.0044  876  ILE A CD1 
2551 N N   . VAL A 340 ? 0.3012 0.3073 0.2965 0.0033  -0.0024 -0.0085 877  VAL A N   
2552 C CA  . VAL A 340 ? 0.2672 0.2740 0.2570 0.0027  0.0013  -0.0102 877  VAL A CA  
2553 C C   . VAL A 340 ? 0.2827 0.2896 0.2662 -0.0012 -0.0020 -0.0090 877  VAL A C   
2554 O O   . VAL A 340 ? 0.2725 0.2827 0.2540 -0.0029 -0.0008 -0.0074 877  VAL A O   
2555 C CB  . VAL A 340 ? 0.3017 0.3013 0.2847 0.0037  0.0047  -0.0148 877  VAL A CB  
2556 C CG1 . VAL A 340 ? 0.3235 0.3222 0.2965 0.0011  0.0083  -0.0168 877  VAL A CG1 
2557 C CG2 . VAL A 340 ? 0.2739 0.2733 0.2654 0.0085  0.0086  -0.0160 877  VAL A CG2 
2558 N N   . SER A 341 ? 0.2766 0.2800 0.2582 -0.0028 -0.0063 -0.0094 878  SER A N   
2559 C CA  . SER A 341 ? 0.2562 0.2596 0.2351 -0.0057 -0.0102 -0.0080 878  SER A CA  
2560 C C   . SER A 341 ? 0.3088 0.3174 0.2934 -0.0063 -0.0111 -0.0047 878  SER A C   
2561 O O   . SER A 341 ? 0.2827 0.2920 0.2649 -0.0082 -0.0123 -0.0027 878  SER A O   
2562 C CB  . SER A 341 ? 0.3112 0.3116 0.2912 -0.0068 -0.0140 -0.0092 878  SER A CB  
2563 O OG  . SER A 341 ? 0.3319 0.3327 0.3121 -0.0090 -0.0181 -0.0078 878  SER A OG  
2564 N N   . ALA A 342 ? 0.2530 0.2642 0.2442 -0.0053 -0.0108 -0.0039 879  ALA A N   
2565 C CA  . ALA A 342 ? 0.2453 0.2604 0.2409 -0.0067 -0.0116 -0.0012 879  ALA A CA  
2566 C C   . ALA A 342 ? 0.2681 0.2874 0.2637 -0.0069 -0.0092 0.0009  879  ALA A C   
2567 O O   . ALA A 342 ? 0.2365 0.2569 0.2318 -0.0091 -0.0104 0.0029  879  ALA A O   
2568 C CB  . ALA A 342 ? 0.2290 0.2454 0.2295 -0.0067 -0.0122 -0.0007 879  ALA A CB  
2569 N N   . VAL A 343 ? 0.2384 0.2601 0.2351 -0.0048 -0.0055 0.0003  880  VAL A N   
2570 C CA  . VAL A 343 ? 0.2403 0.2674 0.2384 -0.0056 -0.0022 0.0020  880  VAL A CA  
2571 C C   . VAL A 343 ? 0.2880 0.3123 0.2766 -0.0080 -0.0008 0.0015  880  VAL A C   
2572 O O   . VAL A 343 ? 0.2745 0.3022 0.2621 -0.0104 0.0010  0.0036  880  VAL A O   
2573 C CB  . VAL A 343 ? 0.2973 0.3292 0.3028 -0.0023 0.0021  0.0015  880  VAL A CB  
2574 C CG1 . VAL A 343 ? 0.2837 0.3187 0.2984 -0.0012 -0.0011 0.0038  880  VAL A CG1 
2575 C CG2 . VAL A 343 ? 0.2994 0.3264 0.3012 0.0004  0.0054  -0.0026 880  VAL A CG2 
2576 N N   . ASN A 344 ? 0.2719 0.2899 0.2528 -0.0082 -0.0021 -0.0009 881  ASN A N   
2577 C CA  . ASN A 344 ? 0.2936 0.3076 0.2634 -0.0117 -0.0027 -0.0005 881  ASN A CA  
2578 C C   . ASN A 344 ? 0.2704 0.2826 0.2394 -0.0145 -0.0086 0.0031  881  ASN A C   
2579 O O   . ASN A 344 ? 0.3009 0.3102 0.2615 -0.0180 -0.0101 0.0051  881  ASN A O   
2580 C CB  . ASN A 344 ? 0.2859 0.2934 0.2472 -0.0120 -0.0032 -0.0039 881  ASN A CB  
2581 C CG  . ASN A 344 ? 0.3726 0.3791 0.3301 -0.0107 0.0039  -0.0079 881  ASN A CG  
2582 O OD1 . ASN A 344 ? 0.3573 0.3690 0.3190 -0.0097 0.0096  -0.0080 881  ASN A OD1 
2583 N ND2 . ASN A 344 ? 0.3453 0.3452 0.2956 -0.0109 0.0038  -0.0115 881  ASN A ND2 
2584 N N   . SER A 345 ? 0.2774 0.2903 0.2546 -0.0131 -0.0120 0.0037  882  SER A N   
2585 C CA  . SER A 345 ? 0.2450 0.2554 0.2239 -0.0148 -0.0171 0.0063  882  SER A CA  
2586 C C   . SER A 345 ? 0.3413 0.3525 0.3177 -0.0178 -0.0169 0.0100  882  SER A C   
2587 O O   . SER A 345 ? 0.2836 0.2993 0.2611 -0.0183 -0.0128 0.0106  882  SER A O   
2588 C CB  . SER A 345 ? 0.2728 0.2844 0.2611 -0.0133 -0.0183 0.0053  882  SER A CB  
2589 O OG  . SER A 345 ? 0.2694 0.2850 0.2617 -0.0136 -0.0159 0.0063  882  SER A OG  
2590 N N   . VAL A 346 ? 0.2823 0.2889 0.2562 -0.0200 -0.0218 0.0130  883  VAL A N   
2591 C CA  . VAL A 346 ? 0.2772 0.2831 0.2463 -0.0238 -0.0218 0.0170  883  VAL A CA  
2592 C C   . VAL A 346 ? 0.3187 0.3281 0.2952 -0.0241 -0.0199 0.0180  883  VAL A C   
2593 O O   . VAL A 346 ? 0.3328 0.3446 0.3065 -0.0271 -0.0173 0.0203  883  VAL A O   
2594 C CB  . VAL A 346 ? 0.3369 0.3357 0.3021 -0.0262 -0.0287 0.0211  883  VAL A CB  
2595 C CG1 . VAL A 346 ? 0.4158 0.4112 0.3705 -0.0280 -0.0310 0.0210  883  VAL A CG1 
2596 C CG2 . VAL A 346 ? 0.3297 0.3262 0.3063 -0.0234 -0.0333 0.0208  883  VAL A CG2 
2597 N N   . SER A 347 ? 0.2855 0.2953 0.2707 -0.0217 -0.0209 0.0160  884  SER A N   
2598 C CA  . SER A 347 ? 0.2558 0.2678 0.2463 -0.0231 -0.0197 0.0167  884  SER A CA  
2599 C C   . SER A 347 ? 0.3078 0.3276 0.3003 -0.0229 -0.0153 0.0160  884  SER A C   
2600 O O   . SER A 347 ? 0.2866 0.3098 0.2813 -0.0255 -0.0141 0.0179  884  SER A O   
2601 C CB  . SER A 347 ? 0.3344 0.3435 0.3316 -0.0216 -0.0214 0.0141  884  SER A CB  
2602 O OG  . SER A 347 ? 0.3750 0.3867 0.3745 -0.0190 -0.0199 0.0107  884  SER A OG  
2603 N N   . VAL A 348 ? 0.2507 0.2731 0.2435 -0.0198 -0.0131 0.0134  885  VAL A N   
2604 C CA  . VAL A 348 ? 0.2223 0.2521 0.2197 -0.0188 -0.0095 0.0130  885  VAL A CA  
2605 C C   . VAL A 348 ? 0.2577 0.2918 0.2525 -0.0193 -0.0048 0.0136  885  VAL A C   
2606 O O   . VAL A 348 ? 0.2514 0.2926 0.2516 -0.0203 -0.0020 0.0151  885  VAL A O   
2607 C CB  . VAL A 348 ? 0.2882 0.3179 0.2885 -0.0151 -0.0093 0.0101  885  VAL A CB  
2608 C CG1 . VAL A 348 ? 0.2389 0.2758 0.2457 -0.0132 -0.0063 0.0104  885  VAL A CG1 
2609 C CG2 . VAL A 348 ? 0.2782 0.3048 0.2810 -0.0156 -0.0125 0.0092  885  VAL A CG2 
2610 N N   . TYR A 349 ? 0.2539 0.2837 0.2404 -0.0192 -0.0039 0.0123  886  TYR A N   
2611 C CA  . TYR A 349 ? 0.2625 0.2947 0.2440 -0.0203 0.0017  0.0115  886  TYR A CA  
2612 C C   . TYR A 349 ? 0.3286 0.3647 0.3092 -0.0248 0.0039  0.0148  886  TYR A C   
2613 O O   . TYR A 349 ? 0.2999 0.3422 0.2820 -0.0255 0.0104  0.0140  886  TYR A O   
2614 C CB  . TYR A 349 ? 0.2782 0.3028 0.2472 -0.0215 0.0006  0.0100  886  TYR A CB  
2615 C CG  . TYR A 349 ? 0.2787 0.3038 0.2395 -0.0232 0.0075  0.0077  886  TYR A CG  
2616 C CD1 . TYR A 349 ? 0.3012 0.3275 0.2642 -0.0195 0.0125  0.0030  886  TYR A CD1 
2617 C CD2 . TYR A 349 ? 0.2819 0.3055 0.2322 -0.0290 0.0092  0.0101  886  TYR A CD2 
2618 C CE1 . TYR A 349 ? 0.3375 0.3636 0.2930 -0.0211 0.0201  -0.0003 886  TYR A CE1 
2619 C CE2 . TYR A 349 ? 0.3804 0.4040 0.3217 -0.0315 0.0167  0.0071  886  TYR A CE2 
2620 C CZ  . TYR A 349 ? 0.3809 0.4059 0.3252 -0.0273 0.0225  0.0015  886  TYR A CZ  
2621 O OH  . TYR A 349 ? 0.4156 0.4400 0.3511 -0.0297 0.0313  -0.0025 886  TYR A OH  
2622 N N   . ARG A 350 ? 0.3043 0.3368 0.2833 -0.0280 -0.0009 0.0182  887  ARG A N   
2623 C CA  . ARG A 350 ? 0.3038 0.3384 0.2808 -0.0332 0.0005  0.0219  887  ARG A CA  
2624 C C   . ARG A 350 ? 0.3656 0.4095 0.3540 -0.0339 0.0026  0.0231  887  ARG A C   
2625 O O   . ARG A 350 ? 0.3298 0.3767 0.3178 -0.0387 0.0042  0.0261  887  ARG A O   
2626 C CB  . ARG A 350 ? 0.2979 0.3236 0.2692 -0.0365 -0.0059 0.0255  887  ARG A CB  
2627 C CG  . ARG A 350 ? 0.2591 0.2817 0.2378 -0.0346 -0.0109 0.0255  887  ARG A CG  
2628 C CD  . ARG A 350 ? 0.3060 0.3198 0.2810 -0.0378 -0.0161 0.0291  887  ARG A CD  
2629 N NE  . ARG A 350 ? 0.3117 0.3267 0.2834 -0.0436 -0.0145 0.0330  887  ARG A NE  
2630 C CZ  . ARG A 350 ? 0.3084 0.3275 0.2861 -0.0460 -0.0134 0.0339  887  ARG A CZ  
2631 N NH1 . ARG A 350 ? 0.3674 0.3877 0.3417 -0.0519 -0.0118 0.0376  887  ARG A NH1 
2632 N NH2 . ARG A 350 ? 0.2736 0.2952 0.2598 -0.0434 -0.0141 0.0313  887  ARG A NH2 
2633 N N   . LEU A 351 ? 0.2639 0.3121 0.2620 -0.0297 0.0020  0.0212  888  LEU A N   
2634 C CA  . LEU A 351 ? 0.2464 0.3031 0.2555 -0.0309 0.0020  0.0231  888  LEU A CA  
2635 C C   . LEU A 351 ? 0.2870 0.3550 0.3047 -0.0297 0.0085  0.0226  888  LEU A C   
2636 O O   . LEU A 351 ? 0.2602 0.3345 0.2887 -0.0258 0.0089  0.0217  888  LEU A O   
2637 C CB  . LEU A 351 ? 0.2502 0.3057 0.2647 -0.0281 -0.0024 0.0221  888  LEU A CB  
2638 C CG  . LEU A 351 ? 0.2843 0.3299 0.2932 -0.0293 -0.0075 0.0217  888  LEU A CG  
2639 C CD1 . LEU A 351 ? 0.3057 0.3501 0.3181 -0.0271 -0.0102 0.0199  888  LEU A CD1 
2640 C CD2 . LEU A 351 ? 0.2769 0.3205 0.2845 -0.0348 -0.0095 0.0246  888  LEU A CD2 
2641 N N   . ASP A 352 ? 0.3003 0.3707 0.3137 -0.0333 0.0136  0.0233  889  ASP A N   
2642 C CA  . ASP A 352 ? 0.2961 0.3772 0.3180 -0.0321 0.0217  0.0217  889  ASP A CA  
2643 C C   . ASP A 352 ? 0.2822 0.3760 0.3222 -0.0314 0.0215  0.0238  889  ASP A C   
2644 O O   . ASP A 352 ? 0.3301 0.4323 0.3826 -0.0270 0.0259  0.0220  889  ASP A O   
2645 C CB  . ASP A 352 ? 0.2939 0.3756 0.3069 -0.0380 0.0277  0.0223  889  ASP A CB  
2646 C CG  . ASP A 352 ? 0.4931 0.5634 0.4882 -0.0388 0.0287  0.0201  889  ASP A CG  
2647 O OD1 . ASP A 352 ? 0.5392 0.6034 0.5314 -0.0341 0.0263  0.0172  889  ASP A OD1 
2648 O OD2 . ASP A 352 ? 0.6187 0.6864 0.6024 -0.0450 0.0316  0.0215  889  ASP A OD2 
2649 N N   . HIS A 353 ? 0.2724 0.3672 0.3145 -0.0359 0.0161  0.0278  890  HIS A N   
2650 C CA  . HIS A 353 ? 0.3022 0.4093 0.3609 -0.0366 0.0147  0.0306  890  HIS A CA  
2651 C C   . HIS A 353 ? 0.3416 0.4500 0.4094 -0.0307 0.0104  0.0300  890  HIS A C   
2652 O O   . HIS A 353 ? 0.2925 0.4123 0.3768 -0.0285 0.0108  0.0314  890  HIS A O   
2653 C CB  . HIS A 353 ? 0.3216 0.4274 0.3780 -0.0437 0.0092  0.0346  890  HIS A CB  
2654 C CG  . HIS A 353 ? 0.3719 0.4770 0.4210 -0.0503 0.0128  0.0363  890  HIS A CG  
2655 N ND1 . HIS A 353 ? 0.4425 0.5599 0.5005 -0.0533 0.0194  0.0375  890  HIS A ND1 
2656 C CD2 . HIS A 353 ? 0.4321 0.5254 0.4664 -0.0547 0.0106  0.0374  890  HIS A CD2 
2657 C CE1 . HIS A 353 ? 0.4211 0.5339 0.4680 -0.0601 0.0212  0.0393  890  HIS A CE1 
2658 N NE2 . HIS A 353 ? 0.4612 0.5590 0.4938 -0.0609 0.0155  0.0396  890  HIS A NE2 
2659 N N   . THR A 354 ? 0.2968 0.3936 0.3544 -0.0286 0.0060  0.0282  891  THR A N   
2660 C CA  . THR A 354 ? 0.2590 0.3549 0.3220 -0.0242 0.0016  0.0279  891  THR A CA  
2661 C C   . THR A 354 ? 0.2813 0.3806 0.3520 -0.0174 0.0065  0.0251  891  THR A C   
2662 O O   . THR A 354 ? 0.2807 0.3863 0.3647 -0.0140 0.0047  0.0266  891  THR A O   
2663 C CB  . THR A 354 ? 0.2431 0.3258 0.2931 -0.0242 -0.0031 0.0261  891  THR A CB  
2664 O OG1 . THR A 354 ? 0.2935 0.3722 0.3374 -0.0303 -0.0069 0.0280  891  THR A OG1 
2665 C CG2 . THR A 354 ? 0.2915 0.3728 0.3455 -0.0210 -0.0075 0.0261  891  THR A CG2 
2666 N N   . PHE A 355 ? 0.2916 0.3859 0.3536 -0.0157 0.0125  0.0212  892  PHE A N   
2667 C CA  . PHE A 355 ? 0.3127 0.4086 0.3804 -0.0097 0.0184  0.0175  892  PHE A CA  
2668 C C   . PHE A 355 ? 0.3114 0.4212 0.3969 -0.0083 0.0245  0.0181  892  PHE A C   
2669 O O   . PHE A 355 ? 0.3479 0.4620 0.4469 -0.0023 0.0265  0.0169  892  PHE A O   
2670 C CB  . PHE A 355 ? 0.3035 0.3902 0.3556 -0.0098 0.0234  0.0130  892  PHE A CB  
2671 C CG  . PHE A 355 ? 0.3050 0.3793 0.3445 -0.0089 0.0180  0.0116  892  PHE A CG  
2672 C CD1 . PHE A 355 ? 0.3042 0.3740 0.3453 -0.0037 0.0176  0.0088  892  PHE A CD1 
2673 C CD2 . PHE A 355 ? 0.4028 0.4702 0.4307 -0.0133 0.0133  0.0131  892  PHE A CD2 
2674 C CE1 . PHE A 355 ? 0.3095 0.3691 0.3403 -0.0035 0.0130  0.0074  892  PHE A CE1 
2675 C CE2 . PHE A 355 ? 0.3126 0.3702 0.3319 -0.0123 0.0088  0.0117  892  PHE A CE2 
2676 C CZ  . PHE A 355 ? 0.3458 0.4000 0.3665 -0.0076 0.0087  0.0088  892  PHE A CZ  
2677 N N   . GLU A 356 ? 0.3063 0.4232 0.3929 -0.0137 0.0274  0.0200  893  GLU A N   
2678 C CA  . GLU A 356 ? 0.2721 0.4038 0.3771 -0.0130 0.0341  0.0204  893  GLU A CA  
2679 C C   . GLU A 356 ? 0.3369 0.4792 0.4632 -0.0104 0.0280  0.0249  893  GLU A C   
2680 O O   . GLU A 356 ? 0.3152 0.4692 0.4618 -0.0062 0.0326  0.0246  893  GLU A O   
2681 C CB  . GLU A 356 ? 0.3396 0.4764 0.4403 -0.0208 0.0379  0.0222  893  GLU A CB  
2682 C CG  . GLU A 356 ? 0.5741 0.7271 0.6936 -0.0209 0.0469  0.0218  893  GLU A CG  
2683 C CD  . GLU A 356 ? 0.7875 0.9410 0.9101 -0.0153 0.0581  0.0151  893  GLU A CD  
2684 O OE1 . GLU A 356 ? 0.7070 0.8476 0.8100 -0.0154 0.0610  0.0109  893  GLU A OE1 
2685 O OE2 . GLU A 356 ? 0.9032 1.0698 1.0484 -0.0111 0.0639  0.0141  893  GLU A OE2 
2686 N N   . ALA A 357 ? 0.2671 0.4050 0.3891 -0.0129 0.0176  0.0289  894  ALA A N   
2687 C CA  . ALA A 357 ? 0.3276 0.4743 0.4666 -0.0125 0.0100  0.0341  894  ALA A CA  
2688 C C   . ALA A 357 ? 0.3486 0.4918 0.4946 -0.0054 0.0061  0.0341  894  ALA A C   
2689 O O   . ALA A 357 ? 0.3260 0.4766 0.4876 -0.0044 -0.0006 0.0390  894  ALA A O   
2690 C CB  . ALA A 357 ? 0.3535 0.4963 0.4829 -0.0200 0.0009  0.0383  894  ALA A CB  
2691 N N   . LEU A 358 ? 0.2936 0.4253 0.4281 -0.0010 0.0095  0.0291  895  LEU A N   
2692 C CA  . LEU A 358 ? 0.3463 0.4731 0.4864 0.0056  0.0067  0.0286  895  LEU A CA  
2693 C C   . LEU A 358 ? 0.3946 0.5331 0.5597 0.0119  0.0108  0.0290  895  LEU A C   
2694 O O   . LEU A 358 ? 0.3333 0.4795 0.5057 0.0129  0.0206  0.0258  895  LEU A O   
2695 C CB  . LEU A 358 ? 0.2786 0.3917 0.4023 0.0085  0.0110  0.0225  895  LEU A CB  
2696 C CG  . LEU A 358 ? 0.3189 0.4190 0.4207 0.0045  0.0068  0.0214  895  LEU A CG  
2697 C CD1 . LEU A 358 ? 0.3098 0.3997 0.4004 0.0079  0.0123  0.0154  895  LEU A CD1 
2698 C CD2 . LEU A 358 ? 0.3305 0.4265 0.4316 0.0035  -0.0030 0.0254  895  LEU A CD2 
2699 N N   . GLN A 359 ? 0.3303 0.4696 0.5084 0.0162  0.0040  0.0328  896  GLN A N   
2700 C CA  . GLN A 359 ? 0.4179 0.5670 0.6219 0.0237  0.0081  0.0328  896  GLN A CA  
2701 C C   . GLN A 359 ? 0.4363 0.5772 0.6355 0.0297  0.0192  0.0245  896  GLN A C   
2702 O O   . GLN A 359 ? 0.3419 0.4681 0.5204 0.0293  0.0191  0.0208  896  GLN A O   
2703 C CB  . GLN A 359 ? 0.5063 0.6567 0.7253 0.0268  -0.0032 0.0398  896  GLN A CB  
2704 C CG  . GLN A 359 ? 0.6747 0.8101 0.8858 0.0314  -0.0064 0.0385  896  GLN A CG  
2705 C CD  . GLN A 359 ? 0.7838 0.9211 1.0108 0.0338  -0.0181 0.0466  896  GLN A CD  
2706 O OE1 . GLN A 359 ? 0.8383 0.9866 1.0772 0.0301  -0.0261 0.0538  896  GLN A OE1 
2707 N NE2 . GLN A 359 ? 0.7393 0.8653 0.9661 0.0394  -0.0199 0.0459  896  GLN A NE2 
2708 N N   A GLU A 360 ? 0.4350 0.5228 0.6571 0.1071  0.0182  0.0304  897  GLU A N   
2709 N N   B GLU A 360 ? 0.4333 0.5209 0.6553 0.1072  0.0181  0.0304  897  GLU A N   
2710 C CA  A GLU A 360 ? 0.4849 0.5669 0.6952 0.1111  0.0264  0.0260  897  GLU A CA  
2711 C CA  B GLU A 360 ? 0.4845 0.5665 0.6948 0.1110  0.0264  0.0260  897  GLU A CA  
2712 C C   A GLU A 360 ? 0.4598 0.5179 0.6483 0.1114  0.0248  0.0210  897  GLU A C   
2713 C C   B GLU A 360 ? 0.4602 0.5183 0.6488 0.1116  0.0249  0.0210  897  GLU A C   
2714 O O   A GLU A 360 ? 0.4523 0.5018 0.6253 0.1085  0.0291  0.0173  897  GLU A O   
2715 O O   B GLU A 360 ? 0.4500 0.4995 0.6231 0.1090  0.0294  0.0172  897  GLU A O   
2716 C CB  A GLU A 360 ? 0.5118 0.6047 0.7348 0.1220  0.0325  0.0265  897  GLU A CB  
2717 C CB  B GLU A 360 ? 0.5116 0.6051 0.7348 0.1217  0.0327  0.0266  897  GLU A CB  
2718 C CG  A GLU A 360 ? 0.5905 0.6727 0.7990 0.1280  0.0408  0.0214  897  GLU A CG  
2719 C CG  B GLU A 360 ? 0.6097 0.6988 0.8214 0.1256  0.0425  0.0224  897  GLU A CG  
2720 C CD  A GLU A 360 ? 0.6733 0.7598 0.8742 0.1228  0.0478  0.0198  897  GLU A CD  
2721 C CD  B GLU A 360 ? 0.7279 0.8289 0.9533 0.1365  0.0499  0.0235  897  GLU A CD  
2722 O OE1 A GLU A 360 ? 0.6705 0.7729 0.8826 0.1171  0.0481  0.0235  897  GLU A OE1 
2723 O OE1 B GLU A 360 ? 0.6541 0.7701 0.9005 0.1402  0.0472  0.0282  897  GLU A OE1 
2724 O OE2 A GLU A 360 ? 0.7822 0.8555 0.9652 0.1243  0.0527  0.0150  897  GLU A OE2 
2725 O OE2 B GLU A 360 ? 0.8558 0.9512 1.0708 0.1413  0.0584  0.0198  897  GLU A OE2 
2726 N N   . ARG A 361 ? 0.4151 0.4622 0.6020 0.1147  0.0185  0.0211  898  ARG A N   
2727 C CA  . ARG A 361 ? 0.4716 0.4951 0.6381 0.1154  0.0169  0.0165  898  ARG A CA  
2728 C C   . ARG A 361 ? 0.4735 0.4864 0.6252 0.1043  0.0140  0.0152  898  ARG A C   
2729 O O   . ARG A 361 ? 0.4537 0.4517 0.5874 0.1022  0.0163  0.0109  898  ARG A O   
2730 C CB  . ARG A 361 ? 0.5920 0.6067 0.7609 0.1214  0.0104  0.0177  898  ARG A CB  
2731 C CG  . ARG A 361 ? 0.7035 0.6928 0.8512 0.1220  0.0087  0.0133  898  ARG A CG  
2732 C CD  . ARG A 361 ? 0.6930 0.6727 0.8423 0.1296  0.0033  0.0144  898  ARG A CD  
2733 N NE  . ARG A 361 ? 0.7366 0.6941 0.8679 0.1249  -0.0021 0.0124  898  ARG A NE  
2734 C CZ  . ARG A 361 ? 0.7666 0.7049 0.8776 0.1231  0.0008  0.0074  898  ARG A CZ  
2735 N NH1 . ARG A 361 ? 0.7984 0.7355 0.9026 0.1257  0.0087  0.0035  898  ARG A NH1 
2736 N NH2 . ARG A 361 ? 0.7375 0.6569 0.8340 0.1184  -0.0043 0.0062  898  ARG A NH2 
2737 N N   . LYS A 362 ? 0.4588 0.4792 0.6180 0.0971  0.0092  0.0191  899  LYS A N   
2738 C CA  . LYS A 362 ? 0.4473 0.4592 0.5946 0.0870  0.0070  0.0187  899  LYS A CA  
2739 C C   . LYS A 362 ? 0.4543 0.4741 0.5984 0.0824  0.0132  0.0179  899  LYS A C   
2740 O O   . LYS A 362 ? 0.4106 0.4205 0.5404 0.0763  0.0136  0.0158  899  LYS A O   
2741 C CB  . LYS A 362 ? 0.4993 0.5157 0.6547 0.0812  0.0008  0.0232  899  LYS A CB  
2742 C CG  . LYS A 362 ? 0.5490 0.5538 0.7029 0.0841  -0.0065 0.0238  899  LYS A CG  
2743 C CD  . LYS A 362 ? 0.5962 0.5946 0.7463 0.0759  -0.0121 0.0263  899  LYS A CD  
2744 C CE  . LYS A 362 ? 0.6614 0.6459 0.8072 0.0787  -0.0193 0.0267  899  LYS A CE  
2745 N NZ  . LYS A 362 ? 0.7628 0.7588 0.9247 0.0854  -0.0226 0.0295  899  LYS A NZ  
2746 N N   . ARG A 363 ? 0.3841 0.4219 0.5415 0.0851  0.0180  0.0198  900  ARG A N   
2747 C CA  . ARG A 363 ? 0.3542 0.3998 0.5084 0.0814  0.0242  0.0192  900  ARG A CA  
2748 C C   . ARG A 363 ? 0.4274 0.4599 0.5642 0.0839  0.0284  0.0138  900  ARG A C   
2749 O O   . ARG A 363 ? 0.3829 0.4113 0.5077 0.0776  0.0299  0.0122  900  ARG A O   
2750 C CB  . ARG A 363 ? 0.4640 0.5304 0.6354 0.0848  0.0291  0.0222  900  ARG A CB  
2751 C CG  . ARG A 363 ? 0.5742 0.6514 0.7460 0.0784  0.0332  0.0240  900  ARG A CG  
2752 C CD  . ARG A 363 ? 0.6308 0.7282 0.8224 0.0793  0.0354  0.0286  900  ARG A CD  
2753 N NE  . ARG A 363 ? 0.5930 0.6984 0.7945 0.0886  0.0399  0.0281  900  ARG A NE  
2754 C CZ  . ARG A 363 ? 0.6915 0.8128 0.9127 0.0914  0.0399  0.0321  900  ARG A CZ  
2755 N NH1 . ARG A 363 ? 0.6786 0.8074 0.9097 0.0851  0.0353  0.0363  900  ARG A NH1 
2756 N NH2 . ARG A 363 ? 0.5667 0.6957 0.7975 0.1002  0.0446  0.0319  900  ARG A NH2 
2757 N N   . LYS A 364 ? 0.3620 0.3875 0.4972 0.0929  0.0301  0.0110  901  LYS A N   
2758 C CA  . LYS A 364 ? 0.3822 0.3929 0.4995 0.0958  0.0344  0.0055  901  LYS A CA  
2759 C C   . LYS A 364 ? 0.4146 0.4057 0.5136 0.0892  0.0298  0.0027  901  LYS A C   
2760 O O   . LYS A 364 ? 0.4160 0.3979 0.4989 0.0853  0.0322  -0.0009 901  LYS A O   
2761 C CB  . LYS A 364 ? 0.4908 0.4964 0.6106 0.1076  0.0372  0.0035  901  LYS A CB  
2762 C CG  . LYS A 364 ? 0.6241 0.6457 0.7561 0.1149  0.0450  0.0046  901  LYS A CG  
2763 C CD  . LYS A 364 ? 0.7268 0.7428 0.8616 0.1271  0.0479  0.0032  901  LYS A CD  
2764 C CE  . LYS A 364 ? 0.7583 0.7847 0.8987 0.1347  0.0580  0.0028  901  LYS A CE  
2765 N NZ  . LYS A 364 ? 0.7538 0.7745 0.8975 0.1473  0.0613  0.0019  901  LYS A NZ  
2766 N N   . ILE A 365 ? 0.3569 0.3416 0.4581 0.0874  0.0229  0.0045  902  ILE A N   
2767 C CA  . ILE A 365 ? 0.3405 0.3063 0.4252 0.0814  0.0187  0.0022  902  ILE A CA  
2768 C C   . ILE A 365 ? 0.3753 0.3457 0.4556 0.0707  0.0185  0.0035  902  ILE A C   
2769 O O   . ILE A 365 ? 0.3529 0.3118 0.4174 0.0658  0.0190  0.0004  902  ILE A O   
2770 C CB  . ILE A 365 ? 0.3943 0.3525 0.4822 0.0818  0.0117  0.0043  902  ILE A CB  
2771 C CG1 . ILE A 365 ? 0.5126 0.4609 0.5994 0.0923  0.0117  0.0022  902  ILE A CG1 
2772 C CG2 . ILE A 365 ? 0.4225 0.3652 0.4960 0.0732  0.0078  0.0034  902  ILE A CG2 
2773 C CD1 . ILE A 365 ? 0.5912 0.5354 0.6843 0.0947  0.0049  0.0051  902  ILE A CD1 
2774 N N   . LEU A 366 ? 0.3454 0.3329 0.4399 0.0673  0.0180  0.0083  903  LEU A N   
2775 C CA  . LEU A 366 ? 0.3432 0.3370 0.4358 0.0580  0.0183  0.0105  903  LEU A CA  
2776 C C   . LEU A 366 ? 0.3304 0.3276 0.4149 0.0568  0.0237  0.0081  903  LEU A C   
2777 O O   . LEU A 366 ? 0.3139 0.3063 0.3874 0.0496  0.0231  0.0074  903  LEU A O   
2778 C CB  . LEU A 366 ? 0.3055 0.3168 0.4150 0.0557  0.0178  0.0162  903  LEU A CB  
2779 C CG  . LEU A 366 ? 0.3276 0.3460 0.4361 0.0469  0.0186  0.0192  903  LEU A CG  
2780 C CD1 . LEU A 366 ? 0.3618 0.3662 0.4582 0.0401  0.0147  0.0187  903  LEU A CD1 
2781 C CD2 . LEU A 366 ? 0.3731 0.4064 0.4974 0.0450  0.0183  0.0247  903  LEU A CD2 
2782 N N   . ASP A 367 ? 0.3198 0.3251 0.4094 0.0637  0.0289  0.0070  904  ASP A N   
2783 C CA  . ASP A 367 ? 0.3634 0.3718 0.4444 0.0625  0.0343  0.0048  904  ASP A CA  
2784 C C   . ASP A 367 ? 0.4192 0.4079 0.4789 0.0620  0.0348  -0.0011 904  ASP A C   
2785 O O   . ASP A 367 ? 0.3962 0.3831 0.4441 0.0562  0.0360  -0.0026 904  ASP A O   
2786 C CB  . ASP A 367 ? 0.3891 0.4113 0.4812 0.0701  0.0407  0.0054  904  ASP A CB  
2787 C CG  . ASP A 367 ? 0.3809 0.4235 0.4908 0.0678  0.0413  0.0113  904  ASP A CG  
2788 O OD1 . ASP A 367 ? 0.4301 0.4754 0.5405 0.0598  0.0379  0.0143  904  ASP A OD1 
2789 O OD2 . ASP A 367 ? 0.3316 0.3872 0.4551 0.0737  0.0454  0.0130  904  ASP A OD2 
2790 N N   . GLU A 368 ? 0.3740 0.3474 0.4281 0.0675  0.0334  -0.0044 905  GLU A N   
2791 C CA  . GLU A 368 ? 0.4290 0.3816 0.4616 0.0660  0.0334  -0.0100 905  GLU A CA  
2792 C C   . GLU A 368 ? 0.4663 0.4114 0.4890 0.0548  0.0281  -0.0095 905  GLU A C   
2793 O O   . GLU A 368 ? 0.4438 0.3788 0.4498 0.0495  0.0285  -0.0130 905  GLU A O   
2794 C CB  . GLU A 368 ? 0.5354 0.4720 0.5639 0.0743  0.0329  -0.0131 905  GLU A CB  
2795 C CG  . GLU A 368 ? 0.6444 0.5573 0.6495 0.0726  0.0332  -0.0191 905  GLU A CG  
2796 C CD  . GLU A 368 ? 0.7632 0.6615 0.7630 0.0834  0.0360  -0.0228 905  GLU A CD  
2797 O OE1 . GLU A 368 ? 0.7164 0.6193 0.7303 0.0906  0.0345  -0.0201 905  GLU A OE1 
2798 O OE2 . GLU A 368 ? 0.8658 0.7477 0.8470 0.0847  0.0397  -0.0282 905  GLU A OE2 
2799 N N   . ALA A 369 ? 0.4185 0.3687 0.4516 0.0509  0.0233  -0.0051 906  ALA A N   
2800 C CA  . ALA A 369 ? 0.3987 0.3432 0.4245 0.0407  0.0189  -0.0039 906  ALA A CA  
2801 C C   . ALA A 369 ? 0.3644 0.3225 0.3910 0.0335  0.0202  -0.0013 906  ALA A C   
2802 O O   . ALA A 369 ? 0.3644 0.3160 0.3788 0.0259  0.0185  -0.0025 906  ALA A O   
2803 C CB  . ALA A 369 ? 0.3806 0.3261 0.4165 0.0390  0.0142  0.0003  906  ALA A CB  
2804 N N   . VAL A 370 ? 0.3370 0.3140 0.3780 0.0358  0.0232  0.0024  907  VAL A N   
2805 C CA  . VAL A 370 ? 0.3408 0.3313 0.3832 0.0296  0.0247  0.0055  907  VAL A CA  
2806 C C   . VAL A 370 ? 0.3721 0.3561 0.3979 0.0284  0.0273  0.0009  907  VAL A C   
2807 O O   . VAL A 370 ? 0.3777 0.3639 0.3961 0.0207  0.0261  0.0019  907  VAL A O   
2808 C CB  . VAL A 370 ? 0.3534 0.3641 0.4134 0.0332  0.0282  0.0100  907  VAL A CB  
2809 C CG1 . VAL A 370 ? 0.4153 0.4387 0.4745 0.0281  0.0306  0.0126  907  VAL A CG1 
2810 C CG2 . VAL A 370 ? 0.3677 0.3843 0.4420 0.0320  0.0250  0.0149  907  VAL A CG2 
2811 N N   . GLU A 371 ? 0.3961 0.3711 0.4152 0.0361  0.0309  -0.0041 908  GLU A N   
2812 C CA  . GLU A 371 ? 0.4177 0.3844 0.4192 0.0356  0.0342  -0.0090 908  GLU A CA  
2813 C C   . GLU A 371 ? 0.4904 0.4393 0.4728 0.0279  0.0300  -0.0125 908  GLU A C   
2814 O O   . GLU A 371 ? 0.4659 0.4107 0.4334 0.0231  0.0308  -0.0151 908  GLU A O   
2815 C CB  . GLU A 371 ? 0.4315 0.3918 0.4309 0.0466  0.0399  -0.0132 908  GLU A CB  
2816 C CG  . GLU A 371 ? 0.5951 0.5743 0.6086 0.0524  0.0458  -0.0104 908  GLU A CG  
2817 C CD  . GLU A 371 ? 0.7169 0.6952 0.7379 0.0643  0.0505  -0.0120 908  GLU A CD  
2818 O OE1 . GLU A 371 ? 0.6488 0.6444 0.6866 0.0690  0.0542  -0.0084 908  GLU A OE1 
2819 O OE2 . GLU A 371 ? 0.6722 0.6326 0.6827 0.0690  0.0508  -0.0166 908  GLU A OE2 
2820 N N   . LEU A 372 ? 0.4031 0.3415 0.3855 0.0259  0.0252  -0.0124 909  LEU A N   
2821 C CA  . LEU A 372 ? 0.4002 0.3229 0.3663 0.0172  0.0208  -0.0149 909  LEU A CA  
2822 C C   . LEU A 372 ? 0.4489 0.3820 0.4134 0.0066  0.0182  -0.0115 909  LEU A C   
2823 O O   . LEU A 372 ? 0.4492 0.3719 0.3976 -0.0008 0.0158  -0.0143 909  LEU A O   
2824 C CB  . LEU A 372 ? 0.4224 0.3358 0.3921 0.0160  0.0163  -0.0137 909  LEU A CB  
2825 C CG  . LEU A 372 ? 0.4623 0.3600 0.4291 0.0248  0.0171  -0.0174 909  LEU A CG  
2826 C CD1 . LEU A 372 ? 0.5495 0.4413 0.5214 0.0225  0.0122  -0.0147 909  LEU A CD1 
2827 C CD2 . LEU A 372 ? 0.4843 0.3603 0.4290 0.0255  0.0186  -0.0245 909  LEU A CD2 
2828 N N   . SER A 373 ? 0.4097 0.3633 0.3909 0.0056  0.0185  -0.0052 910  SER A N   
2829 C CA  . SER A 373 ? 0.3946 0.3595 0.3771 -0.0040 0.0157  -0.0006 910  SER A CA  
2830 C C   . SER A 373 ? 0.4583 0.4323 0.4349 -0.0052 0.0186  -0.0009 910  SER A C   
2831 O O   . SER A 373 ? 0.4396 0.4204 0.4129 -0.0135 0.0158  0.0021  910  SER A O   
2832 C CB  . SER A 373 ? 0.4140 0.3950 0.4165 -0.0048 0.0148  0.0068  910  SER A CB  
2833 O OG  . SER A 373 ? 0.4159 0.4106 0.4316 0.0024  0.0192  0.0089  910  SER A OG  
2834 N N   . GLN A 374 ? 0.4510 0.4251 0.4264 0.0032  0.0242  -0.0040 911  GLN A N   
2835 C CA  . GLN A 374 ? 0.5396 0.5227 0.5099 0.0032  0.0280  -0.0040 911  GLN A CA  
2836 C C   . GLN A 374 ? 0.6349 0.6047 0.5817 -0.0034 0.0262  -0.0087 911  GLN A C   
2837 O O   . GLN A 374 ? 0.5185 0.4690 0.4513 -0.0052 0.0239  -0.0138 911  GLN A O   
2838 C CB  . GLN A 374 ? 0.5226 0.5089 0.4984 0.0143  0.0351  -0.0060 911  GLN A CB  
2839 C CG  . GLN A 374 ? 0.5076 0.5128 0.5071 0.0187  0.0370  0.0000  911  GLN A CG  
2840 C CD  . GLN A 374 ? 0.5636 0.5705 0.5714 0.0298  0.0428  -0.0018 911  GLN A CD  
2841 O OE1 . GLN A 374 ? 0.4967 0.4920 0.4928 0.0353  0.0468  -0.0073 911  GLN A OE1 
2842 N NE2 . GLN A 374 ? 0.5347 0.5559 0.5630 0.0332  0.0435  0.0031  911  GLN A NE2 
2843 N N   A ASP A 375 ? 0.6269 0.6066 0.5690 -0.0073 0.0271  -0.0068 912  ASP A N   
2844 N N   B ASP A 375 ? 0.6276 0.6070 0.5694 -0.0072 0.0272  -0.0070 912  ASP A N   
2845 C CA  A ASP A 375 ? 0.6497 0.6184 0.5688 -0.0142 0.0252  -0.0108 912  ASP A CA  
2846 C CA  B ASP A 375 ? 0.6610 0.6292 0.5796 -0.0142 0.0252  -0.0110 912  ASP A CA  
2847 C C   A ASP A 375 ? 0.5943 0.5531 0.5053 -0.0245 0.0175  -0.0112 912  ASP A C   
2848 C C   B ASP A 375 ? 0.5951 0.5537 0.5060 -0.0245 0.0174  -0.0112 912  ASP A C   
2849 O O   A ASP A 375 ? 0.5866 0.5250 0.4786 -0.0270 0.0161  -0.0175 912  ASP A O   
2850 O O   B ASP A 375 ? 0.5836 0.5218 0.4756 -0.0271 0.0160  -0.0175 912  ASP A O   
2851 C CB  A ASP A 375 ? 0.7435 0.6943 0.6453 -0.0072 0.0310  -0.0189 912  ASP A CB  
2852 C CB  B ASP A 375 ? 0.7622 0.7121 0.6631 -0.0075 0.0308  -0.0191 912  ASP A CB  
2853 C CG  A ASP A 375 ? 0.7960 0.7570 0.7078 0.0036  0.0393  -0.0183 912  ASP A CG  
2854 C CG  B ASP A 375 ? 0.8381 0.7779 0.7141 -0.0139 0.0302  -0.0232 912  ASP A CG  
2855 O OD1 A ASP A 375 ? 0.8444 0.8235 0.7650 0.0028  0.0409  -0.0132 912  ASP A OD1 
2856 O OD1 B ASP A 375 ? 0.8721 0.8229 0.7468 -0.0227 0.0258  -0.0190 912  ASP A OD1 
2857 O OD2 A ASP A 375 ? 0.7482 0.6995 0.6596 0.0130  0.0443  -0.0225 912  ASP A OD2 
2858 O OD2 B ASP A 375 ? 0.8451 0.7657 0.7025 -0.0101 0.0342  -0.0304 912  ASP A OD2 
2859 N N   . HIS A 376 ? 0.5336 0.5067 0.4595 -0.0303 0.0129  -0.0041 913  HIS A N   
2860 C CA  . HIS A 376 ? 0.5777 0.5452 0.5003 -0.0402 0.0058  -0.0028 913  HIS A CA  
2861 C C   . HIS A 376 ? 0.5788 0.5257 0.4952 -0.0383 0.0050  -0.0080 913  HIS A C   
2862 O O   . HIS A 376 ? 0.5957 0.5266 0.4956 -0.0451 0.0012  -0.0121 913  HIS A O   
2863 C CB  . HIS A 376 ? 0.6839 0.6484 0.5885 -0.0506 0.0014  -0.0038 913  HIS A CB  
2864 C CG  . HIS A 376 ? 0.7554 0.7400 0.6657 -0.0529 0.0015  0.0020  913  HIS A CG  
2865 N ND1 . HIS A 376 ? 0.7617 0.7673 0.6932 -0.0536 0.0006  0.0108  913  HIS A ND1 
2866 C CD2 . HIS A 376 ? 0.7567 0.7427 0.6534 -0.0544 0.0027  0.0005  913  HIS A CD2 
2867 C CE1 . HIS A 376 ? 0.7592 0.7786 0.6905 -0.0553 0.0010  0.0146  913  HIS A CE1 
2868 N NE2 . HIS A 376 ? 0.7805 0.7886 0.6907 -0.0559 0.0021  0.0085  913  HIS A NE2 
2869 N N   . PHE A 377 ? 0.5246 0.4721 0.4542 -0.0290 0.0085  -0.0077 914  PHE A N   
2870 C CA  . PHE A 377 ? 0.5319 0.4620 0.4588 -0.0259 0.0078  -0.0115 914  PHE A CA  
2871 C C   . PHE A 377 ? 0.5578 0.4644 0.4623 -0.0241 0.0093  -0.0200 914  PHE A C   
2872 O O   . PHE A 377 ? 0.5204 0.4093 0.4160 -0.0263 0.0068  -0.0233 914  PHE A O   
2873 C CB  . PHE A 377 ? 0.4746 0.4035 0.4056 -0.0347 0.0018  -0.0078 914  PHE A CB  
2874 C CG  . PHE A 377 ? 0.4792 0.4275 0.4324 -0.0347 0.0014  0.0003  914  PHE A CG  
2875 C CD1 . PHE A 377 ? 0.4696 0.4363 0.4304 -0.0407 -0.0002 0.0066  914  PHE A CD1 
2876 C CD2 . PHE A 377 ? 0.4561 0.4037 0.4219 -0.0283 0.0027  0.0018  914  PHE A CD2 
2877 C CE1 . PHE A 377 ? 0.5534 0.5366 0.5339 -0.0401 0.0002  0.0140  914  PHE A CE1 
2878 C CE2 . PHE A 377 ? 0.4288 0.3924 0.4133 -0.0283 0.0027  0.0089  914  PHE A CE2 
2879 C CZ  . PHE A 377 ? 0.3865 0.3675 0.3783 -0.0340 0.0018  0.0150  914  PHE A CZ  
2880 N N   . LYS A 378 ? 0.5710 0.4765 0.4658 -0.0198 0.0140  -0.0236 915  LYS A N   
2881 C CA  . LYS A 378 ? 0.6007 0.4830 0.4724 -0.0176 0.0167  -0.0318 915  LYS A CA  
2882 C C   . LYS A 378 ? 0.5665 0.4321 0.4378 -0.0092 0.0188  -0.0357 915  LYS A C   
2883 O O   . LYS A 378 ? 0.6076 0.4520 0.4631 -0.0126 0.0166  -0.0403 915  LYS A O   
2884 C CB  . LYS A 378 ? 0.6231 0.5088 0.4879 -0.0118 0.0231  -0.0343 915  LYS A CB  
2885 C CG  . LYS A 378 ? 0.7509 0.6116 0.5893 -0.0099 0.0266  -0.0429 915  LYS A CG  
2886 C CD  . LYS A 378 ? 0.8307 0.6951 0.6634 -0.0029 0.0344  -0.0449 915  LYS A CD  
2887 C CE  . LYS A 378 ? 0.9686 0.8066 0.7762 0.0016  0.0397  -0.0536 915  LYS A CE  
2888 N NZ  . LYS A 378 ? 1.0190 0.8393 0.7997 -0.0101 0.0352  -0.0581 915  LYS A NZ  
2889 N N   . LYS A 379 ? 0.4745 0.3497 0.3633 0.0015  0.0228  -0.0335 916  LYS A N   
2890 C CA  . LYS A 379 ? 0.4813 0.3421 0.3706 0.0106  0.0249  -0.0366 916  LYS A CA  
2891 C C   . LYS A 379 ? 0.5119 0.3660 0.4057 0.0062  0.0190  -0.0347 916  LYS A C   
2892 O O   . LYS A 379 ? 0.5208 0.3555 0.4060 0.0098  0.0190  -0.0385 916  LYS A O   
2893 C CB  . LYS A 379 ? 0.5671 0.4418 0.4750 0.0228  0.0302  -0.0342 916  LYS A CB  
2894 C CG  . LYS A 379 ? 0.5113 0.3851 0.4117 0.0303  0.0379  -0.0379 916  LYS A CG  
2895 C CD  . LYS A 379 ? 0.5595 0.4515 0.4815 0.0407  0.0427  -0.0341 916  LYS A CD  
2896 C CE  . LYS A 379 ? 0.6366 0.5272 0.5518 0.0490  0.0513  -0.0376 916  LYS A CE  
2897 N NZ  . LYS A 379 ? 0.6529 0.5639 0.5912 0.0580  0.0557  -0.0331 916  LYS A NZ  
2898 N N   . TYR A 380 ? 0.5131 0.3828 0.4201 -0.0011 0.0145  -0.0285 917  TYR A N   
2899 C CA  . TYR A 380 ? 0.4955 0.3586 0.4050 -0.0067 0.0092  -0.0263 917  TYR A CA  
2900 C C   . TYR A 380 ? 0.5268 0.3686 0.4146 -0.0153 0.0060  -0.0310 917  TYR A C   
2901 O O   . TYR A 380 ? 0.5313 0.3558 0.4130 -0.0151 0.0043  -0.0332 917  TYR A O   
2902 C CB  . TYR A 380 ? 0.5101 0.3936 0.4361 -0.0137 0.0058  -0.0187 917  TYR A CB  
2903 C CG  . TYR A 380 ? 0.4756 0.3506 0.3997 -0.0221 0.0006  -0.0169 917  TYR A CG  
2904 C CD1 . TYR A 380 ? 0.5012 0.3649 0.4282 -0.0180 -0.0002 -0.0172 917  TYR A CD1 
2905 C CD2 . TYR A 380 ? 0.4780 0.3560 0.3971 -0.0340 -0.0034 -0.0148 917  TYR A CD2 
2906 C CE1 . TYR A 380 ? 0.4638 0.3188 0.3884 -0.0255 -0.0042 -0.0156 917  TYR A CE1 
2907 C CE2 . TYR A 380 ? 0.4458 0.3163 0.3637 -0.0417 -0.0076 -0.0130 917  TYR A CE2 
2908 C CZ  . TYR A 380 ? 0.4628 0.3214 0.3833 -0.0373 -0.0076 -0.0134 917  TYR A CZ  
2909 O OH  . TYR A 380 ? 0.4755 0.3262 0.3946 -0.0448 -0.0111 -0.0114 917  TYR A OH  
2910 N N   . LEU A 381 ? 0.5604 0.4036 0.4365 -0.0232 0.0049  -0.0323 918  LEU A N   
2911 C CA  . LEU A 381 ? 0.5946 0.4195 0.4503 -0.0334 0.0011  -0.0363 918  LEU A CA  
2912 C C   . LEU A 381 ? 0.7455 0.5429 0.5812 -0.0281 0.0041  -0.0443 918  LEU A C   
2913 O O   . LEU A 381 ? 0.8270 0.6054 0.6501 -0.0338 0.0010  -0.0471 918  LEU A O   
2914 C CB  . LEU A 381 ? 0.6682 0.5012 0.5151 -0.0425 -0.0009 -0.0359 918  LEU A CB  
2915 C CG  . LEU A 381 ? 0.6307 0.4869 0.4942 -0.0508 -0.0055 -0.0277 918  LEU A CG  
2916 C CD1 . LEU A 381 ? 0.6415 0.5064 0.4963 -0.0593 -0.0078 -0.0269 918  LEU A CD1 
2917 C CD2 . LEU A 381 ? 0.6312 0.4818 0.4975 -0.0589 -0.0107 -0.0252 918  LEU A CD2 
2918 N N   . VAL A 382 ? 0.6491 0.4439 0.4819 -0.0171 0.0104  -0.0478 919  VAL A N   
2919 C CA  . VAL A 382 ? 0.7882 0.5568 0.6031 -0.0105 0.0142  -0.0550 919  VAL A CA  
2920 C C   . VAL A 382 ? 0.6782 0.4391 0.5023 -0.0036 0.0138  -0.0539 919  VAL A C   
2921 O O   . VAL A 382 ? 0.6490 0.3857 0.4580 -0.0030 0.0138  -0.0584 919  VAL A O   
2922 C CB  . VAL A 382 ? 0.7705 0.5380 0.5801 0.0003  0.0221  -0.0587 919  VAL A CB  
2923 C CG1 . VAL A 382 ? 0.7785 0.5573 0.5819 -0.0060 0.0225  -0.0585 919  VAL A CG1 
2924 C CG2 . VAL A 382 ? 0.8556 0.6384 0.6875 0.0133  0.0263  -0.0551 919  VAL A CG2 
2925 N N   . LYS A 383 ? 0.5886 0.3690 0.4365 0.0011  0.0132  -0.0478 920  LYS A N   
2926 C CA  . LYS A 383 ? 0.5423 0.3161 0.3986 0.0074  0.0122  -0.0464 920  LYS A CA  
2927 C C   . LYS A 383 ? 0.6061 0.3689 0.4571 -0.0028 0.0064  -0.0454 920  LYS A C   
2928 O O   . LYS A 383 ? 0.6725 0.4166 0.5169 0.0002  0.0058  -0.0475 920  LYS A O   
2929 C CB  . LYS A 383 ? 0.6225 0.4195 0.5044 0.0140  0.0127  -0.0402 920  LYS A CB  
2930 C CG  . LYS A 383 ? 0.8188 0.6080 0.7077 0.0237  0.0129  -0.0398 920  LYS A CG  
2931 C CD  . LYS A 383 ? 0.9115 0.7226 0.8239 0.0313  0.0140  -0.0345 920  LYS A CD  
2932 C CE  . LYS A 383 ? 0.9620 0.7648 0.8803 0.0410  0.0135  -0.0341 920  LYS A CE  
2933 N NZ  . LYS A 383 ? 0.9506 0.7744 0.8920 0.0457  0.0126  -0.0282 920  LYS A NZ  
2934 N N   . LEU A 384 ? 0.6221 0.3964 0.4758 -0.0147 0.0023  -0.0419 921  LEU A N   
2935 C CA  . LEU A 384 ? 0.6895 0.4560 0.5400 -0.0251 -0.0029 -0.0401 921  LEU A CA  
2936 C C   . LEU A 384 ? 0.7521 0.4902 0.5779 -0.0298 -0.0036 -0.0467 921  LEU A C   
2937 O O   . LEU A 384 ? 0.8187 0.5414 0.6398 -0.0320 -0.0057 -0.0471 921  LEU A O   
2938 C CB  . LEU A 384 ? 0.6569 0.4426 0.5154 -0.0367 -0.0067 -0.0349 921  LEU A CB  
2939 C CG  . LEU A 384 ? 0.6491 0.4302 0.5067 -0.0484 -0.0117 -0.0320 921  LEU A CG  
2940 C CD1 . LEU A 384 ? 0.6425 0.4232 0.5129 -0.0442 -0.0121 -0.0281 921  LEU A CD1 
2941 C CD2 . LEU A 384 ? 0.6602 0.4615 0.5256 -0.0593 -0.0151 -0.0266 921  LEU A CD2 
2942 N N   . LYS A 385 ? 0.8280 0.5581 0.6369 -0.0313 -0.0016 -0.0520 922  LYS A N   
2943 C CA  . LYS A 385 ? 0.9555 0.6581 0.7389 -0.0374 -0.0024 -0.0585 922  LYS A CA  
2944 C C   . LYS A 385 ? 0.8427 0.5208 0.6158 -0.0269 0.0014  -0.0633 922  LYS A C   
2945 O O   . LYS A 385 ? 0.9275 0.5804 0.6811 -0.0315 0.0005  -0.0679 922  LYS A O   
2946 C CB  . LYS A 385 ? 1.0811 0.7810 0.8477 -0.0418 -0.0011 -0.0629 922  LYS A CB  
2947 C CG  . LYS A 385 ? 1.1633 0.8527 0.9200 -0.0292 0.0063  -0.0685 922  LYS A CG  
2948 C CD  . LYS A 385 ? 1.2106 0.8892 0.9439 -0.0349 0.0076  -0.0742 922  LYS A CD  
2949 C CE  . LYS A 385 ? 1.2169 0.9199 0.9594 -0.0345 0.0090  -0.0713 922  LYS A CE  
2950 N NZ  . LYS A 385 ? 1.2382 0.9668 0.9989 -0.0441 0.0027  -0.0637 922  LYS A NZ  
2951 N N   . SER A 386 ? 0.7555 0.4410 0.5419 -0.0130 0.0055  -0.0619 923  SER A N   
2952 C CA  . SER A 386 ? 0.8729 0.5371 0.6508 -0.0015 0.0096  -0.0660 923  SER A CA  
2953 C C   . SER A 386 ? 0.9348 0.5947 0.7227 0.0022  0.0071  -0.0625 923  SER A C   
2954 O O   . SER A 386 ? 1.0899 0.7263 0.8657 0.0074  0.0085  -0.0659 923  SER A O   
2955 C CB  . SER A 386 ? 0.9858 0.6592 0.7711 0.0125  0.0160  -0.0668 923  SER A CB  
2956 O OG  . SER A 386 ? 1.0273 0.7263 0.8389 0.0181  0.0153  -0.0603 923  SER A OG  
2957 N N   . ILE A 387 ? 0.9082 0.5894 0.7169 -0.0001 0.0036  -0.0558 924  ILE A N   
2958 C CA  . ILE A 387 ? 0.9282 0.6064 0.7469 0.0053  0.0018  -0.0524 924  ILE A CA  
2959 C C   . ILE A 387 ? 0.8842 0.5424 0.6908 -0.0034 -0.0018 -0.0530 924  ILE A C   
2960 O O   . ILE A 387 ? 0.7681 0.4201 0.5631 -0.0156 -0.0040 -0.0546 924  ILE A O   
2961 C CB  . ILE A 387 ? 0.9710 0.6767 0.8150 0.0060  -0.0002 -0.0451 924  ILE A CB  
2962 C CG1 . ILE A 387 ? 0.9636 0.6879 0.8136 -0.0058 -0.0026 -0.0419 924  ILE A CG1 
2963 C CG2 . ILE A 387 ? 0.8549 0.5747 0.7127 0.0191  0.0034  -0.0440 924  ILE A CG2 
2964 C CD1 . ILE A 387 ? 0.8966 0.6146 0.7417 -0.0187 -0.0070 -0.0399 924  ILE A CD1 
2965 N N   . ASN A 388 ? 0.8533 0.5015 0.6627 0.0030  -0.0025 -0.0514 925  ASN A N   
2966 C CA  . ASN A 388 ? 0.9018 0.5303 0.7006 -0.0038 -0.0054 -0.0515 925  ASN A CA  
2967 C C   . ASN A 388 ? 0.8214 0.4641 0.6366 -0.0085 -0.0091 -0.0446 925  ASN A C   
2968 O O   . ASN A 388 ? 0.8286 0.4892 0.6617 -0.0017 -0.0091 -0.0404 925  ASN A O   
2969 C CB  . ASN A 388 ? 0.9547 0.5582 0.7420 0.0065  -0.0035 -0.0548 925  ASN A CB  
2970 C CG  . ASN A 388 ? 1.0482 0.6353 0.8181 0.0121  0.0012  -0.0616 925  ASN A CG  
2971 O OD1 . ASN A 388 ? 1.0606 0.6388 0.8150 0.0032  0.0017  -0.0659 925  ASN A OD1 
2972 N ND2 . ASN A 388 ? 1.0760 0.6589 0.8484 0.0268  0.0048  -0.0626 925  ASN A ND2 
2973 N N   . PRO A 389 ? 0.8211 0.4555 0.6297 -0.0203 -0.0119 -0.0435 926  PRO A N   
2974 C CA  . PRO A 389 ? 0.8118 0.4556 0.6334 -0.0249 -0.0145 -0.0371 926  PRO A CA  
2975 C C   . PRO A 389 ? 0.7737 0.4099 0.5996 -0.0145 -0.0146 -0.0351 926  PRO A C   
2976 O O   . PRO A 389 ? 0.7649 0.3820 0.5795 -0.0063 -0.0133 -0.0390 926  PRO A O   
2977 C CB  . PRO A 389 ? 0.9167 0.5453 0.7253 -0.0380 -0.0165 -0.0377 926  PRO A CB  
2978 C CG  . PRO A 389 ? 0.9797 0.6011 0.7732 -0.0434 -0.0159 -0.0434 926  PRO A CG  
2979 C CD  . PRO A 389 ? 0.8998 0.5149 0.6880 -0.0304 -0.0124 -0.0482 926  PRO A CD  
2980 N N   . PRO A 390 ? 0.6825 0.3327 0.5238 -0.0148 -0.0162 -0.0290 927  PRO A N   
2981 C CA  . PRO A 390 ? 0.6308 0.3032 0.4859 -0.0235 -0.0171 -0.0239 927  PRO A CA  
2982 C C   . PRO A 390 ? 0.6508 0.3490 0.5209 -0.0199 -0.0159 -0.0224 927  PRO A C   
2983 O O   . PRO A 390 ? 0.5889 0.2918 0.4644 -0.0091 -0.0146 -0.0235 927  PRO A O   
2984 C CB  . PRO A 390 ? 0.5988 0.2709 0.4618 -0.0229 -0.0183 -0.0185 927  PRO A CB  
2985 C CG  . PRO A 390 ? 0.7371 0.3984 0.5980 -0.0102 -0.0184 -0.0201 927  PRO A CG  
2986 C CD  . PRO A 390 ? 0.6532 0.2948 0.4970 -0.0069 -0.0172 -0.0266 927  PRO A CD  
2987 N N   . CYS A 391 ? 0.6080 0.3232 0.4853 -0.0290 -0.0163 -0.0195 928  CYS A N   
2988 C CA  . CYS A 391 ? 0.5642 0.3042 0.4558 -0.0267 -0.0151 -0.0173 928  CYS A CA  
2989 C C   . CYS A 391 ? 0.4862 0.2447 0.3903 -0.0358 -0.0160 -0.0111 928  CYS A C   
2990 O O   . CYS A 391 ? 0.6287 0.3810 0.5290 -0.0449 -0.0173 -0.0091 928  CYS A O   
2991 C CB  . CYS A 391 ? 0.6990 0.4396 0.5818 -0.0269 -0.0137 -0.0224 928  CYS A CB  
2992 S SG  . CYS A 391 ? 0.7840 0.5236 0.6568 -0.0422 -0.0158 -0.0231 928  CYS A SG  
2993 N N   . VAL A 392 ? 0.4375 0.2186 0.3569 -0.0331 -0.0148 -0.0076 929  VAL A N   
2994 C CA  . VAL A 392 ? 0.3939 0.1943 0.3253 -0.0410 -0.0150 -0.0016 929  VAL A CA  
2995 C C   . VAL A 392 ? 0.5036 0.3215 0.4392 -0.0413 -0.0141 -0.0021 929  VAL A C   
2996 O O   . VAL A 392 ? 0.4589 0.2894 0.4042 -0.0338 -0.0123 -0.0013 929  VAL A O   
2997 C CB  . VAL A 392 ? 0.4256 0.2372 0.3726 -0.0379 -0.0141 0.0046  929  VAL A CB  
2998 C CG1 . VAL A 392 ? 0.4259 0.2546 0.3837 -0.0464 -0.0138 0.0109  929  VAL A CG1 
2999 C CG2 . VAL A 392 ? 0.4330 0.2262 0.3747 -0.0358 -0.0149 0.0047  929  VAL A CG2 
3000 N N   . PRO A 393 ? 0.5088 0.3273 0.4367 -0.0503 -0.0156 -0.0032 930  PRO A N   
3001 C CA  . PRO A 393 ? 0.4342 0.2674 0.3635 -0.0512 -0.0151 -0.0038 930  PRO A CA  
3002 C C   . PRO A 393 ? 0.4484 0.3069 0.3966 -0.0508 -0.0139 0.0030  930  PRO A C   
3003 O O   . PRO A 393 ? 0.4478 0.3130 0.4068 -0.0537 -0.0141 0.0089  930  PRO A O   
3004 C CB  . PRO A 393 ? 0.4223 0.2501 0.3396 -0.0631 -0.0181 -0.0052 930  PRO A CB  
3005 C CG  . PRO A 393 ? 0.5868 0.3911 0.4919 -0.0658 -0.0194 -0.0081 930  PRO A CG  
3006 C CD  . PRO A 393 ? 0.4727 0.2764 0.3886 -0.0602 -0.0181 -0.0043 930  PRO A CD  
3007 N N   . PHE A 394 ? 0.3727 0.2443 0.3243 -0.0471 -0.0122 0.0024  931  PHE A N   
3008 C CA  . PHE A 394 ? 0.4020 0.2974 0.3692 -0.0482 -0.0112 0.0087  931  PHE A CA  
3009 C C   . PHE A 394 ? 0.4787 0.3817 0.4459 -0.0599 -0.0141 0.0126  931  PHE A C   
3010 O O   . PHE A 394 ? 0.4879 0.3858 0.4425 -0.0658 -0.0164 0.0093  931  PHE A O   
3011 C CB  . PHE A 394 ? 0.4274 0.3328 0.3955 -0.0421 -0.0086 0.0065  931  PHE A CB  
3012 C CG  . PHE A 394 ? 0.4145 0.3435 0.3960 -0.0440 -0.0077 0.0126  931  PHE A CG  
3013 C CD1 . PHE A 394 ? 0.4595 0.4013 0.4579 -0.0421 -0.0062 0.0191  931  PHE A CD1 
3014 C CD2 . PHE A 394 ? 0.4609 0.3981 0.4370 -0.0475 -0.0079 0.0119  931  PHE A CD2 
3015 C CE1 . PHE A 394 ? 0.4694 0.4320 0.4797 -0.0434 -0.0049 0.0249  931  PHE A CE1 
3016 C CE2 . PHE A 394 ? 0.4559 0.4146 0.4440 -0.0489 -0.0070 0.0178  931  PHE A CE2 
3017 C CZ  . PHE A 394 ? 0.4434 0.4148 0.4489 -0.0467 -0.0053 0.0245  931  PHE A CZ  
3018 N N   . PHE A 395 ? 0.4378 0.3526 0.4189 -0.0632 -0.0140 0.0199  932  PHE A N   
3019 C CA  . PHE A 395 ? 0.5395 0.4616 0.5225 -0.0741 -0.0168 0.0247  932  PHE A CA  
3020 C C   . PHE A 395 ? 0.5758 0.5186 0.5649 -0.0775 -0.0174 0.0285  932  PHE A C   
3021 O O   . PHE A 395 ? 0.5054 0.4528 0.4912 -0.0869 -0.0209 0.0304  932  PHE A O   
3022 C CB  . PHE A 395 ? 0.6231 0.5486 0.6185 -0.0760 -0.0156 0.0314  932  PHE A CB  
3023 C CG  . PHE A 395 ? 0.7118 0.6354 0.7053 -0.0870 -0.0184 0.0344  932  PHE A CG  
3024 C CD1 . PHE A 395 ? 0.8036 0.7064 0.7847 -0.0905 -0.0201 0.0303  932  PHE A CD1 
3025 C CD2 . PHE A 395 ? 0.8635 0.8062 0.8680 -0.0938 -0.0195 0.0417  932  PHE A CD2 
3026 C CE1 . PHE A 395 ? 0.8147 0.7160 0.7946 -0.1012 -0.0227 0.0332  932  PHE A CE1 
3027 C CE2 . PHE A 395 ? 0.8681 0.8104 0.8723 -0.1042 -0.0223 0.0449  932  PHE A CE2 
3028 C CZ  . PHE A 395 ? 0.7776 0.6994 0.7697 -0.1082 -0.0239 0.0406  932  PHE A CZ  
3029 N N   . GLY A 396 ? 0.4801 0.4352 0.4777 -0.0700 -0.0143 0.0298  933  GLY A N   
3030 C CA  . GLY A 396 ? 0.4931 0.4685 0.4978 -0.0721 -0.0143 0.0343  933  GLY A CA  
3031 C C   . GLY A 396 ? 0.5629 0.5380 0.5542 -0.0781 -0.0176 0.0310  933  GLY A C   
3032 O O   . GLY A 396 ? 0.5734 0.5640 0.5692 -0.0841 -0.0198 0.0361  933  GLY A O   
3033 N N   . ILE A 397 ? 0.5629 0.5201 0.5371 -0.0766 -0.0182 0.0226  934  ILE A N   
3034 C CA  . ILE A 397 ? 0.5239 0.4785 0.4828 -0.0817 -0.0208 0.0186  934  ILE A CA  
3035 C C   . ILE A 397 ? 0.4928 0.4454 0.4456 -0.0947 -0.0267 0.0205  934  ILE A C   
3036 O O   . ILE A 397 ? 0.4856 0.4455 0.4323 -0.1016 -0.0301 0.0213  934  ILE A O   
3037 C CB  . ILE A 397 ? 0.6972 0.6312 0.6383 -0.0758 -0.0189 0.0089  934  ILE A CB  
3038 C CG1 . ILE A 397 ? 0.7120 0.6442 0.6370 -0.0796 -0.0202 0.0048  934  ILE A CG1 
3039 C CG2 . ILE A 397 ? 0.6660 0.5777 0.5971 -0.0777 -0.0203 0.0045  934  ILE A CG2 
3040 C CD1 . ILE A 397 ? 0.8103 0.7249 0.7196 -0.0718 -0.0165 -0.0039 934  ILE A CD1 
3041 N N   . TYR A 398 ? 0.5459 0.4897 0.5010 -0.0982 -0.0279 0.0216  935  TYR A N   
3042 C CA  . TYR A 398 ? 0.4755 0.4189 0.4276 -0.1109 -0.0333 0.0243  935  TYR A CA  
3043 C C   . TYR A 398 ? 0.4354 0.4043 0.4055 -0.1157 -0.0348 0.0344  935  TYR A C   
3044 O O   . TYR A 398 ? 0.4794 0.4560 0.4468 -0.1258 -0.0399 0.0372  935  TYR A O   
3045 C CB  . TYR A 398 ? 0.4401 0.3675 0.3908 -0.1130 -0.0334 0.0234  935  TYR A CB  
3046 C CG  . TYR A 398 ? 0.5227 0.4242 0.4564 -0.1077 -0.0318 0.0141  935  TYR A CG  
3047 C CD1 . TYR A 398 ? 0.6081 0.4938 0.5206 -0.1114 -0.0341 0.0065  935  TYR A CD1 
3048 C CD2 . TYR A 398 ? 0.5520 0.4440 0.4901 -0.0991 -0.0280 0.0131  935  TYR A CD2 
3049 C CE1 . TYR A 398 ? 0.6387 0.5001 0.5357 -0.1058 -0.0321 -0.0016 935  TYR A CE1 
3050 C CE2 . TYR A 398 ? 0.5848 0.4536 0.5081 -0.0938 -0.0267 0.0053  935  TYR A CE2 
3051 C CZ  . TYR A 398 ? 0.5730 0.4267 0.4762 -0.0968 -0.0284 -0.0019 935  TYR A CZ  
3052 O OH  . TYR A 398 ? 0.7227 0.5528 0.6114 -0.0907 -0.0265 -0.0093 935  TYR A OH  
3053 N N   . LEU A 399 ? 0.4321 0.4135 0.4200 -0.1087 -0.0304 0.0402  936  LEU A N   
3054 C CA  . LEU A 399 ? 0.4294 0.4344 0.4352 -0.1119 -0.0307 0.0504  936  LEU A CA  
3055 C C   . LEU A 399 ? 0.4551 0.4753 0.4596 -0.1133 -0.0327 0.0520  936  LEU A C   
3056 O O   . LEU A 399 ? 0.4217 0.4567 0.4316 -0.1213 -0.0367 0.0583  936  LEU A O   
3057 C CB  . LEU A 399 ? 0.4435 0.4561 0.4663 -0.1031 -0.0248 0.0553  936  LEU A CB  
3058 C CG  . LEU A 399 ? 0.4679 0.4674 0.4935 -0.1018 -0.0226 0.0553  936  LEU A CG  
3059 C CD1 . LEU A 399 ? 0.5248 0.5293 0.5636 -0.0923 -0.0168 0.0586  936  LEU A CD1 
3060 C CD2 . LEU A 399 ? 0.5243 0.5282 0.5561 -0.1116 -0.0252 0.0614  936  LEU A CD2 
3061 N N   . THR A 400 ? 0.3719 0.3886 0.3693 -0.1054 -0.0298 0.0467  937  THR A N   
3062 C CA  . THR A 400 ? 0.3819 0.4100 0.3750 -0.1061 -0.0310 0.0472  937  THR A CA  
3063 C C   . THR A 400 ? 0.4612 0.4841 0.4377 -0.1171 -0.0378 0.0444  937  THR A C   
3064 O O   . THR A 400 ? 0.4311 0.4697 0.4106 -0.1235 -0.0418 0.0500  937  THR A O   
3065 C CB  . THR A 400 ? 0.4557 0.4773 0.4421 -0.0956 -0.0261 0.0408  937  THR A CB  
3066 O OG1 . THR A 400 ? 0.5367 0.5654 0.5395 -0.0866 -0.0206 0.0443  937  THR A OG1 
3067 C CG2 . THR A 400 ? 0.5607 0.5927 0.5410 -0.0962 -0.0268 0.0411  937  THR A CG2 
3068 N N   . ASN A 401 ? 0.4658 0.4663 0.4246 -0.1195 -0.0394 0.0360  938  ASN A N   
3069 C CA  . ASN A 401 ? 0.5059 0.4982 0.4463 -0.1305 -0.0459 0.0324  938  ASN A CA  
3070 C C   . ASN A 401 ? 0.4962 0.4994 0.4450 -0.1428 -0.0522 0.0398  938  ASN A C   
3071 O O   . ASN A 401 ? 0.5184 0.5283 0.4604 -0.1523 -0.0583 0.0415  938  ASN A O   
3072 C CB  . ASN A 401 ? 0.5442 0.5081 0.4638 -0.1304 -0.0455 0.0219  938  ASN A CB  
3073 C CG  . ASN A 401 ? 0.7709 0.7238 0.6804 -0.1190 -0.0397 0.0145  938  ASN A CG  
3074 O OD1 . ASN A 401 ? 0.8269 0.7930 0.7422 -0.1127 -0.0366 0.0165  938  ASN A OD1 
3075 N ND2 . ASN A 401 ? 0.8285 0.7571 0.7230 -0.1161 -0.0380 0.0061  938  ASN A ND2 
3076 N N   . ILE A 402 ? 0.4323 0.4376 0.3959 -0.1427 -0.0506 0.0444  939  ILE A N   
3077 C CA  . ILE A 402 ? 0.4045 0.4218 0.3787 -0.1536 -0.0556 0.0523  939  ILE A CA  
3078 C C   . ILE A 402 ? 0.4388 0.4840 0.4296 -0.1545 -0.0569 0.0624  939  ILE A C   
3079 O O   . ILE A 402 ? 0.4672 0.5237 0.4585 -0.1650 -0.0636 0.0671  939  ILE A O   
3080 C CB  . ILE A 402 ? 0.4888 0.5012 0.4750 -0.1525 -0.0525 0.0551  939  ILE A CB  
3081 C CG1 . ILE A 402 ? 0.5144 0.4990 0.4820 -0.1550 -0.0533 0.0459  939  ILE A CG1 
3082 C CG2 . ILE A 402 ? 0.4364 0.4663 0.4388 -0.1620 -0.0560 0.0654  939  ILE A CG2 
3083 C CD1 . ILE A 402 ? 0.5580 0.5328 0.5330 -0.1520 -0.0493 0.0467  939  ILE A CD1 
3084 N N   . LEU A 403 ? 0.4108 0.4669 0.4144 -0.1438 -0.0508 0.0657  940  LEU A N   
3085 C CA  . LEU A 403 ? 0.4151 0.4966 0.4339 -0.1436 -0.0513 0.0754  940  LEU A CA  
3086 C C   . LEU A 403 ? 0.4487 0.5355 0.4542 -0.1491 -0.0569 0.0740  940  LEU A C   
3087 O O   . LEU A 403 ? 0.4404 0.5447 0.4528 -0.1565 -0.0623 0.0818  940  LEU A O   
3088 C CB  . LEU A 403 ? 0.4075 0.4966 0.4393 -0.1310 -0.0434 0.0780  940  LEU A CB  
3089 C CG  . LEU A 403 ? 0.4150 0.5055 0.4640 -0.1263 -0.0380 0.0828  940  LEU A CG  
3090 C CD1 . LEU A 403 ? 0.3827 0.4752 0.4393 -0.1138 -0.0305 0.0827  940  LEU A CD1 
3091 C CD2 . LEU A 403 ? 0.5116 0.6213 0.5787 -0.1323 -0.0398 0.0945  940  LEU A CD2 
3092 N N   . LYS A 404 ? 0.4443 0.5153 0.4301 -0.1455 -0.0558 0.0643  941  LYS A N   
3093 C CA  . LYS A 404 ? 0.4543 0.5266 0.4238 -0.1505 -0.0606 0.0618  941  LYS A CA  
3094 C C   . LYS A 404 ? 0.4980 0.5681 0.4575 -0.1653 -0.0700 0.0623  941  LYS A C   
3095 O O   . LYS A 404 ? 0.5146 0.5986 0.4728 -0.1725 -0.0761 0.0672  941  LYS A O   
3096 C CB  . LYS A 404 ? 0.5073 0.5592 0.4558 -0.1440 -0.0568 0.0505  941  LYS A CB  
3097 C CG  . LYS A 404 ? 0.7209 0.7770 0.6779 -0.1302 -0.0483 0.0501  941  LYS A CG  
3098 C CD  . LYS A 404 ? 0.8674 0.9042 0.8043 -0.1239 -0.0445 0.0393  941  LYS A CD  
3099 C CE  . LYS A 404 ? 0.8764 0.9187 0.8233 -0.1106 -0.0362 0.0393  941  LYS A CE  
3100 N NZ  . LYS A 404 ? 0.8875 0.9109 0.8174 -0.1036 -0.0316 0.0292  941  LYS A NZ  
3101 N N   . THR A 405 ? 0.4548 0.5070 0.4069 -0.1700 -0.0714 0.0572  942  THR A N   
3102 C CA  . THR A 405 ? 0.4375 0.4848 0.3787 -0.1848 -0.0802 0.0567  942  THR A CA  
3103 C C   . THR A 405 ? 0.4232 0.4953 0.3857 -0.1929 -0.0853 0.0691  942  THR A C   
3104 O O   . THR A 405 ? 0.4607 0.5411 0.4182 -0.2044 -0.0939 0.0723  942  THR A O   
3105 C CB  . THR A 405 ? 0.5038 0.5258 0.4334 -0.1876 -0.0797 0.0489  942  THR A CB  
3106 O OG1 . THR A 405 ? 0.5478 0.5473 0.4587 -0.1791 -0.0746 0.0380  942  THR A OG1 
3107 C CG2 . THR A 405 ? 0.4857 0.5008 0.4018 -0.2037 -0.0890 0.0476  942  THR A CG2 
3108 N N   . GLU A 406 ? 0.4304 0.5142 0.4165 -0.1869 -0.0801 0.0763  943  GLU A N   
3109 C CA  . GLU A 406 ? 0.4992 0.6075 0.5078 -0.1929 -0.0834 0.0889  943  GLU A CA  
3110 C C   . GLU A 406 ? 0.5724 0.7035 0.5872 -0.1928 -0.0864 0.0963  943  GLU A C   
3111 O O   . GLU A 406 ? 0.5305 0.6778 0.5510 -0.2029 -0.0942 0.1037  943  GLU A O   
3112 C CB  . GLU A 406 ? 0.4298 0.5440 0.4608 -0.1849 -0.0756 0.0947  943  GLU A CB  
3113 C CG  . GLU A 406 ? 0.4482 0.5428 0.4759 -0.1867 -0.0735 0.0899  943  GLU A CG  
3114 C CD  . GLU A 406 ? 0.6920 0.7914 0.7247 -0.2005 -0.0801 0.0950  943  GLU A CD  
3115 O OE1 . GLU A 406 ? 0.7193 0.8417 0.7651 -0.2070 -0.0851 0.1047  943  GLU A OE1 
3116 O OE2 . GLU A 406 ? 0.6666 0.7472 0.6908 -0.2048 -0.0802 0.0896  943  GLU A OE2 
3117 N N   . GLU A 407 ? 0.4911 0.6235 0.5049 -0.1814 -0.0804 0.0944  944  GLU A N   
3118 C CA  . GLU A 407 ? 0.5275 0.6793 0.5452 -0.1800 -0.0823 0.1007  944  GLU A CA  
3119 C C   . GLU A 407 ? 0.5119 0.6599 0.5075 -0.1895 -0.0910 0.0967  944  GLU A C   
3120 O O   . GLU A 407 ? 0.5929 0.7598 0.5930 -0.1948 -0.0969 0.1045  944  GLU A O   
3121 C CB  . GLU A 407 ? 0.6571 0.8081 0.6766 -0.1657 -0.0733 0.0984  944  GLU A CB  
3122 C CG  . GLU A 407 ? 0.8657 1.0228 0.9072 -0.1560 -0.0649 0.1035  944  GLU A CG  
3123 C CD  . GLU A 407 ? 1.0338 1.2173 1.0985 -0.1559 -0.0649 0.1172  944  GLU A CD  
3124 O OE1 . GLU A 407 ? 1.1230 1.3200 1.1894 -0.1529 -0.0650 0.1215  944  GLU A OE1 
3125 O OE2 . GLU A 407 ? 1.0326 1.2229 1.1135 -0.1584 -0.0645 0.1238  944  GLU A OE2 
3126 N N   . GLY A 408 ? 0.4365 0.6124 0.5921 -0.1081 -0.0239 0.1564  945  GLY A N   
3127 C CA  . GLY A 408 ? 0.4595 0.6580 0.5998 -0.1086 -0.0178 0.1606  945  GLY A CA  
3128 C C   . GLY A 408 ? 0.4986 0.6913 0.6197 -0.1013 -0.0163 0.1516  945  GLY A C   
3129 O O   . GLY A 408 ? 0.4647 0.6755 0.5711 -0.1007 -0.0106 0.1529  945  GLY A O   
3130 N N   . ASN A 409 ? 0.3902 0.5576 0.5111 -0.0960 -0.0212 0.1422  946  ASN A N   
3131 C CA  . ASN A 409 ? 0.3738 0.5334 0.4774 -0.0891 -0.0202 0.1329  946  ASN A CA  
3132 C C   . ASN A 409 ? 0.4270 0.5617 0.5364 -0.0899 -0.0286 0.1342  946  ASN A C   
3133 O O   . ASN A 409 ? 0.4048 0.5211 0.5290 -0.0911 -0.0337 0.1325  946  ASN A O   
3134 C CB  . ASN A 409 ? 0.4242 0.5790 0.5169 -0.0787 -0.0152 0.1133  946  ASN A CB  
3135 C CG  . ASN A 409 ? 0.5264 0.7063 0.6118 -0.0766 -0.0065 0.1103  946  ASN A CG  
3136 O OD1 . ASN A 409 ? 0.5259 0.7209 0.5955 -0.0746 -0.0008 0.1095  946  ASN A OD1 
3137 N ND2 . ASN A 409 ? 0.4238 0.6082 0.5207 -0.0770 -0.0053 0.1083  946  ASN A ND2 
3138 N N   . ASN A 410 ? 0.4132 0.5471 0.5115 -0.0894 -0.0298 0.1369  947  ASN A N   
3139 C CA  . ASN A 410 ? 0.3798 0.4910 0.4845 -0.0901 -0.0378 0.1382  947  ASN A CA  
3140 C C   . ASN A 410 ? 0.3931 0.4821 0.4923 -0.0812 -0.0379 0.1191  947  ASN A C   
3141 O O   . ASN A 410 ? 0.3894 0.4829 0.4725 -0.0737 -0.0316 0.1061  947  ASN A O   
3142 C CB  . ASN A 410 ? 0.5330 0.6510 0.6284 -0.0929 -0.0399 0.1483  947  ASN A CB  
3143 C CG  . ASN A 410 ? 0.7929 0.8927 0.9020 -0.0975 -0.0496 0.1571  947  ASN A CG  
3144 O OD1 . ASN A 410 ? 0.6523 0.7316 0.7616 -0.0928 -0.0532 0.1477  947  ASN A OD1 
3145 N ND2 . ASN A 410 ? 0.8664 0.9734 0.9876 -0.1068 -0.0539 0.1752  947  ASN A ND2 
3146 N N   . ASP A 411 ? 0.3611 0.4262 0.4735 -0.0822 -0.0447 0.1174  948  ASP A N   
3147 C CA  . ASP A 411 ? 0.3444 0.3865 0.4520 -0.0749 -0.0452 0.0996  948  ASP A CA  
3148 C C   . ASP A 411 ? 0.3378 0.3776 0.4284 -0.0697 -0.0441 0.0933  948  ASP A C   
3149 O O   . ASP A 411 ? 0.3601 0.3871 0.4399 -0.0623 -0.0416 0.0767  948  ASP A O   
3150 C CB  . ASP A 411 ? 0.4301 0.4477 0.5568 -0.0784 -0.0526 0.1000  948  ASP A CB  
3151 C CG  . ASP A 411 ? 0.4478 0.4602 0.5878 -0.0806 -0.0527 0.0979  948  ASP A CG  
3152 O OD1 . ASP A 411 ? 0.3973 0.4217 0.5305 -0.0776 -0.0471 0.0924  948  ASP A OD1 
3153 O OD2 . ASP A 411 ? 0.5318 0.5278 0.6894 -0.0853 -0.0586 0.1014  948  ASP A OD2 
3154 N N   . PHE A 412 ? 0.3298 0.3812 0.4181 -0.0739 -0.0463 0.1067  949  PHE A N   
3155 C CA  . PHE A 412 ? 0.3990 0.4480 0.4731 -0.0700 -0.0464 0.1024  949  PHE A CA  
3156 C C   . PHE A 412 ? 0.4071 0.4815 0.4648 -0.0707 -0.0413 0.1096  949  PHE A C   
3157 O O   . PHE A 412 ? 0.4185 0.5121 0.4796 -0.0769 -0.0400 0.1229  949  PHE A O   
3158 C CB  . PHE A 412 ? 0.4399 0.4738 0.5269 -0.0742 -0.0555 0.1107  949  PHE A CB  
3159 C CG  . PHE A 412 ? 0.4462 0.4529 0.5477 -0.0730 -0.0601 0.1014  949  PHE A CG  
3160 C CD1 . PHE A 412 ? 0.4464 0.4350 0.5399 -0.0661 -0.0593 0.0844  949  PHE A CD1 
3161 C CD2 . PHE A 412 ? 0.5137 0.5129 0.6364 -0.0791 -0.0647 0.1094  949  PHE A CD2 
3162 C CE1 . PHE A 412 ? 0.4843 0.4476 0.5907 -0.0656 -0.0630 0.0752  949  PHE A CE1 
3163 C CE2 . PHE A 412 ? 0.4888 0.4629 0.6247 -0.0785 -0.0685 0.1003  949  PHE A CE2 
3164 C CZ  . PHE A 412 ? 0.4349 0.3911 0.5626 -0.0719 -0.0675 0.0832  949  PHE A CZ  
3165 N N   . LEU A 413 ? 0.4264 0.5009 0.4661 -0.0648 -0.0383 0.1002  950  LEU A N   
3166 C CA  . LEU A 413 ? 0.4391 0.5345 0.4629 -0.0661 -0.0349 0.1074  950  LEU A CA  
3167 C C   . LEU A 413 ? 0.4622 0.5505 0.4893 -0.0698 -0.0428 0.1171  950  LEU A C   
3168 O O   . LEU A 413 ? 0.4135 0.4826 0.4413 -0.0657 -0.0465 0.1080  950  LEU A O   
3169 C CB  . LEU A 413 ? 0.4000 0.5002 0.4017 -0.0575 -0.0266 0.0912  950  LEU A CB  
3170 C CG  . LEU A 413 ? 0.4363 0.5382 0.4358 -0.0522 -0.0198 0.0786  950  LEU A CG  
3171 C CD1 . LEU A 413 ? 0.4059 0.5087 0.3838 -0.0432 -0.0124 0.0618  950  LEU A CD1 
3172 C CD2 . LEU A 413 ? 0.4558 0.5809 0.4596 -0.0575 -0.0159 0.0895  950  LEU A CD2 
3173 N N   . LYS A 414 ? 0.5214 0.6251 0.5507 -0.0778 -0.0456 0.1354  951  LYS A N   
3174 C CA  . LYS A 414 ? 0.6096 0.7074 0.6436 -0.0822 -0.0542 0.1469  951  LYS A CA  
3175 C C   . LYS A 414 ? 0.5841 0.6838 0.5989 -0.0775 -0.0527 0.1404  951  LYS A C   
3176 O O   . LYS A 414 ? 0.5179 0.6352 0.5136 -0.0755 -0.0450 0.1372  951  LYS A O   
3177 C CB  . LYS A 414 ? 0.7529 0.8672 0.7928 -0.0925 -0.0574 0.1686  951  LYS A CB  
3178 C CG  . LYS A 414 ? 0.9200 1.0362 0.9765 -0.0974 -0.0573 0.1750  951  LYS A CG  
3179 C CD  . LYS A 414 ? 1.0319 1.1705 1.0877 -0.1069 -0.0564 0.1935  951  LYS A CD  
3180 C CE  . LYS A 414 ? 1.0283 1.1754 1.0937 -0.1096 -0.0518 0.1946  951  LYS A CE  
3181 N NZ  . LYS A 414 ? 1.0235 1.1915 1.0892 -0.1196 -0.0510 0.2126  951  LYS A NZ  
3182 N N   . LYS A 415 ? 0.5024 0.5838 0.5230 -0.0757 -0.0599 0.1377  952  LYS A N   
3183 C CA  . LYS A 415 ? 0.4971 0.5783 0.5018 -0.0717 -0.0598 0.1321  952  LYS A CA  
3184 C C   . LYS A 415 ? 0.6135 0.6875 0.6286 -0.0766 -0.0707 0.1450  952  LYS A C   
3185 O O   . LYS A 415 ? 0.5789 0.6436 0.6146 -0.0817 -0.0783 0.1553  952  LYS A O   
3186 C CB  . LYS A 415 ? 0.4782 0.5420 0.4770 -0.0621 -0.0564 0.1100  952  LYS A CB  
3187 C CG  . LYS A 415 ? 0.5174 0.5876 0.5031 -0.0562 -0.0457 0.0958  952  LYS A CG  
3188 C CD  . LYS A 415 ? 0.5734 0.6659 0.5357 -0.0547 -0.0380 0.0952  952  LYS A CD  
3189 C CE  . LYS A 415 ? 0.5311 0.6347 0.4844 -0.0509 -0.0280 0.0861  952  LYS A CE  
3190 N NZ  . LYS A 415 ? 0.4957 0.6179 0.4254 -0.0479 -0.0194 0.0814  952  LYS A NZ  
3191 N N   . LYS A 416 ? 0.6479 0.7259 0.6487 -0.0749 -0.0717 0.1444  953  LYS A N   
3192 C CA  . LYS A 416 ? 0.7873 0.8572 0.7969 -0.0784 -0.0824 0.1547  953  LYS A CA  
3193 C C   . LYS A 416 ? 0.7197 0.7630 0.7464 -0.0739 -0.0879 0.1437  953  LYS A C   
3194 O O   . LYS A 416 ? 0.7282 0.7599 0.7746 -0.0781 -0.0977 0.1534  953  LYS A O   
3195 C CB  . LYS A 416 ? 0.8910 0.9721 0.8799 -0.0772 -0.0814 0.1549  953  LYS A CB  
3196 C CG  . LYS A 416 ? 1.0464 1.1202 1.0428 -0.0802 -0.0928 0.1650  953  LYS A CG  
3197 C CD  . LYS A 416 ? 1.1389 1.2231 1.1128 -0.0781 -0.0908 0.1623  953  LYS A CD  
3198 C CE  . LYS A 416 ? 1.1274 1.2008 1.1093 -0.0791 -0.1021 0.1678  953  LYS A CE  
3199 N NZ  . LYS A 416 ? 1.0989 1.1761 1.0938 -0.0885 -0.1124 0.1907  953  LYS A NZ  
3200 N N   . GLY A 417 ? 0.5545 0.5877 0.5735 -0.0658 -0.0815 0.1232  954  GLY A N   
3201 C CA  . GLY A 417 ? 0.5673 0.5750 0.6012 -0.0617 -0.0850 0.1106  954  GLY A CA  
3202 C C   . GLY A 417 ? 0.6296 0.6285 0.6772 -0.0623 -0.0828 0.1067  954  GLY A C   
3203 O O   . GLY A 417 ? 0.6207 0.6290 0.6771 -0.0684 -0.0840 0.1203  954  GLY A O   
3204 N N   . LYS A 418 ? 0.5807 0.5613 0.6296 -0.0564 -0.0797 0.0882  955  LYS A N   
3205 C CA  . LYS A 418 ? 0.6258 0.5969 0.6857 -0.0565 -0.0773 0.0825  955  LYS A CA  
3206 C C   . LYS A 418 ? 0.6062 0.5967 0.6541 -0.0567 -0.0692 0.0844  955  LYS A C   
3207 O O   . LYS A 418 ? 0.5029 0.5052 0.5296 -0.0520 -0.0617 0.0767  955  LYS A O   
3208 C CB  . LYS A 418 ? 0.7058 0.6544 0.7646 -0.0500 -0.0746 0.0608  955  LYS A CB  
3209 C CG  . LYS A 418 ? 0.8575 0.7979 0.9205 -0.0489 -0.0701 0.0518  955  LYS A CG  
3210 C CD  . LYS A 418 ? 0.9799 0.9068 1.0691 -0.0548 -0.0767 0.0591  955  LYS A CD  
3211 C CE  . LYS A 418 ? 1.0680 0.9674 1.1672 -0.0524 -0.0792 0.0442  955  LYS A CE  
3212 N NZ  . LYS A 418 ? 1.1176 1.0091 1.1977 -0.0449 -0.0716 0.0232  955  LYS A NZ  
3213 N N   . ASP A 419 ? 0.5649 0.5592 0.6268 -0.0621 -0.0706 0.0946  956  ASP A N   
3214 C CA  . ASP A 419 ? 0.5501 0.5626 0.6034 -0.0626 -0.0632 0.0964  956  ASP A CA  
3215 C C   . ASP A 419 ? 0.5210 0.5250 0.5653 -0.0552 -0.0560 0.0765  956  ASP A C   
3216 O O   . ASP A 419 ? 0.4351 0.4167 0.4865 -0.0522 -0.0577 0.0642  956  ASP A O   
3221 N N   . LEU A 420 ? 0.3700 0.3916 0.3985 -0.0524 -0.0478 0.0731  957  LEU A N   
3222 C CA  . LEU A 420 ? 0.3578 0.3727 0.3755 -0.0451 -0.0409 0.0545  957  LEU A CA  
3223 C C   . LEU A 420 ? 0.3336 0.3480 0.3630 -0.0470 -0.0397 0.0550  957  LEU A C   
3224 O O   . LEU A 420 ? 0.3819 0.4104 0.4213 -0.0533 -0.0409 0.0696  957  LEU A O   
3225 C CB  . LEU A 420 ? 0.3353 0.3687 0.3293 -0.0401 -0.0324 0.0488  957  LEU A CB  
3226 C CG  . LEU A 420 ? 0.4030 0.4407 0.3825 -0.0383 -0.0324 0.0486  957  LEU A CG  
3227 C CD1 . LEU A 420 ? 0.4347 0.4886 0.3907 -0.0328 -0.0228 0.0399  957  LEU A CD1 
3228 C CD2 . LEU A 420 ? 0.3934 0.4062 0.3750 -0.0346 -0.0366 0.0369  957  LEU A CD2 
3229 N N   . ILE A 421 ? 0.3180 0.3157 0.3460 -0.0418 -0.0375 0.0387  958  ILE A N   
3230 C CA  . ILE A 421 ? 0.3278 0.3254 0.3640 -0.0427 -0.0358 0.0371  958  ILE A CA  
3231 C C   . ILE A 421 ? 0.3474 0.3700 0.3714 -0.0408 -0.0283 0.0387  958  ILE A C   
3232 O O   . ILE A 421 ? 0.3363 0.3654 0.3412 -0.0347 -0.0223 0.0292  958  ILE A O   
3233 C CB  . ILE A 421 ? 0.3064 0.2801 0.3408 -0.0374 -0.0350 0.0184  958  ILE A CB  
3234 C CG1 . ILE A 421 ? 0.3419 0.2911 0.3913 -0.0404 -0.0422 0.0173  958  ILE A CG1 
3235 C CG2 . ILE A 421 ? 0.3158 0.2918 0.3554 -0.0375 -0.0325 0.0158  958  ILE A CG2 
3236 C CD1 . ILE A 421 ? 0.4108 0.3346 0.4539 -0.0351 -0.0411 -0.0028 958  ILE A CD1 
3237 N N   . ASN A 422 ? 0.3270 0.3636 0.3625 -0.0463 -0.0285 0.0506  959  ASN A N   
3238 C CA  . ASN A 422 ? 0.3037 0.3643 0.3306 -0.0451 -0.0213 0.0520  959  ASN A CA  
3239 C C   . ASN A 422 ? 0.3022 0.3558 0.3263 -0.0391 -0.0174 0.0370  959  ASN A C   
3240 O O   . ASN A 422 ? 0.3109 0.3617 0.3494 -0.0421 -0.0194 0.0396  959  ASN A O   
3241 C CB  . ASN A 422 ? 0.3284 0.4071 0.3692 -0.0540 -0.0230 0.0709  959  ASN A CB  
3242 C CG  . ASN A 422 ? 0.3385 0.4427 0.3721 -0.0533 -0.0153 0.0723  959  ASN A CG  
3243 O OD1 . ASN A 422 ? 0.3749 0.4842 0.3930 -0.0461 -0.0087 0.0597  959  ASN A OD1 
3244 N ND2 . ASN A 422 ? 0.3245 0.4451 0.3697 -0.0611 -0.0159 0.0874  959  ASN A ND2 
3245 N N   . PHE A 423 ? 0.2821 0.3324 0.2877 -0.0309 -0.0121 0.0215  960  PHE A N   
3246 C CA  . PHE A 423 ? 0.3138 0.3544 0.3162 -0.0250 -0.0094 0.0067  960  PHE A CA  
3247 C C   . PHE A 423 ? 0.2929 0.3559 0.2952 -0.0244 -0.0040 0.0092  960  PHE A C   
3248 O O   . PHE A 423 ? 0.2901 0.3479 0.2987 -0.0228 -0.0041 0.0033  960  PHE A O   
3249 C CB  . PHE A 423 ? 0.2807 0.3084 0.2633 -0.0163 -0.0058 -0.0114 960  PHE A CB  
3250 C CG  . PHE A 423 ? 0.3010 0.3127 0.2812 -0.0111 -0.0049 -0.0265 960  PHE A CG  
3251 C CD1 . PHE A 423 ? 0.3405 0.3265 0.3310 -0.0129 -0.0106 -0.0316 960  PHE A CD1 
3252 C CD2 . PHE A 423 ? 0.3169 0.3391 0.2852 -0.0048 0.0015  -0.0354 960  PHE A CD2 
3253 C CE1 . PHE A 423 ? 0.3269 0.2975 0.3146 -0.0088 -0.0102 -0.0451 960  PHE A CE1 
3254 C CE2 . PHE A 423 ? 0.3042 0.3112 0.2701 -0.0002 0.0016  -0.0488 960  PHE A CE2 
3255 C CZ  . PHE A 423 ? 0.3414 0.3223 0.3165 -0.0024 -0.0044 -0.0535 960  PHE A CZ  
3256 N N   . SER A 424 ? 0.3127 0.4009 0.3086 -0.0261 0.0006  0.0179  961  SER A N   
3257 C CA  . SER A 424 ? 0.3430 0.4539 0.3392 -0.0257 0.0064  0.0198  961  SER A CA  
3258 C C   . SER A 424 ? 0.3701 0.4841 0.3875 -0.0323 0.0026  0.0299  961  SER A C   
3259 O O   . SER A 424 ? 0.3685 0.4911 0.3900 -0.0305 0.0056  0.0264  961  SER A O   
3260 C CB  . SER A 424 ? 0.3751 0.5123 0.3611 -0.0278 0.0121  0.0284  961  SER A CB  
3261 O OG  . SER A 424 ? 0.4638 0.6011 0.4290 -0.0203 0.0175  0.0161  961  SER A OG  
3262 N N   . LYS A 425 ? 0.2923 0.3987 0.3238 -0.0398 -0.0041 0.0422  962  LYS A N   
3263 C CA  . LYS A 425 ? 0.2844 0.3899 0.3365 -0.0462 -0.0084 0.0509  962  LYS A CA  
3264 C C   . LYS A 425 ? 0.2771 0.3631 0.3342 -0.0420 -0.0104 0.0379  962  LYS A C   
3265 O O   . LYS A 425 ? 0.3092 0.4014 0.3766 -0.0434 -0.0100 0.0389  962  LYS A O   
3266 C CB  . LYS A 425 ? 0.2902 0.3866 0.3561 -0.0544 -0.0158 0.0647  962  LYS A CB  
3267 C CG  . LYS A 425 ? 0.3548 0.4476 0.4425 -0.0612 -0.0205 0.0732  962  LYS A CG  
3268 C CD  . LYS A 425 ? 0.2919 0.3732 0.3931 -0.0687 -0.0281 0.0858  962  LYS A CD  
3269 C CE  . LYS A 425 ? 0.3350 0.4135 0.4580 -0.0759 -0.0324 0.0947  962  LYS A CE  
3270 N NZ  . LYS A 425 ? 0.3751 0.4449 0.5118 -0.0836 -0.0395 0.1084  962  LYS A NZ  
3271 N N   . ARG A 426 ? 0.2822 0.3441 0.3318 -0.0372 -0.0126 0.0256  963  ARG A N   
3272 C CA  . ARG A 426 ? 0.2674 0.3085 0.3202 -0.0339 -0.0148 0.0129  963  ARG A CA  
3273 C C   . ARG A 426 ? 0.3269 0.3771 0.3696 -0.0268 -0.0091 0.0018  963  ARG A C   
3274 O O   . ARG A 426 ? 0.3317 0.3767 0.3823 -0.0264 -0.0106 -0.0025 963  ARG A O   
3275 C CB  . ARG A 426 ? 0.2647 0.2783 0.3102 -0.0306 -0.0178 0.0014  963  ARG A CB  
3276 C CG  . ARG A 426 ? 0.2853 0.2812 0.3471 -0.0376 -0.0252 0.0087  963  ARG A CG  
3277 C CD  . ARG A 426 ? 0.3253 0.3342 0.3932 -0.0437 -0.0272 0.0255  963  ARG A CD  
3278 N NE  . ARG A 426 ? 0.3140 0.3048 0.3977 -0.0497 -0.0344 0.0315  963  ARG A NE  
3279 C CZ  . ARG A 426 ? 0.3448 0.3381 0.4331 -0.0540 -0.0378 0.0429  963  ARG A CZ  
3280 N NH1 . ARG A 426 ? 0.3081 0.3210 0.3851 -0.0532 -0.0346 0.0494  963  ARG A NH1 
3281 N NH2 . ARG A 426 ? 0.3642 0.3400 0.4680 -0.0590 -0.0445 0.0475  963  ARG A NH2 
3282 N N   . ARG A 427 ? 0.2978 0.3614 0.3232 -0.0212 -0.0028 -0.0030 964  ARG A N   
3283 C CA  . ARG A 427 ? 0.3191 0.3936 0.3346 -0.0142 0.0031  -0.0132 964  ARG A CA  
3284 C C   . ARG A 427 ? 0.3341 0.4301 0.3636 -0.0178 0.0045  -0.0043 964  ARG A C   
3285 O O   . ARG A 427 ? 0.3226 0.4184 0.3542 -0.0140 0.0054  -0.0121 964  ARG A O   
3286 C CB  . ARG A 427 ? 0.3181 0.4063 0.3141 -0.0089 0.0101  -0.0174 964  ARG A CB  
3287 C CG  . ARG A 427 ? 0.3797 0.4795 0.3653 -0.0011 0.0167  -0.0284 964  ARG A CG  
3288 C CD  . ARG A 427 ? 0.3486 0.4603 0.3142 0.0039  0.0238  -0.0333 964  ARG A CD  
3289 N NE  . ARG A 427 ? 0.3950 0.4850 0.3466 0.0077  0.0224  -0.0430 964  ARG A NE  
3290 C CZ  . ARG A 427 ? 0.4445 0.5340 0.3904 0.0050  0.0217  -0.0374 964  ARG A CZ  
3291 N NH1 . ARG A 427 ? 0.3666 0.4758 0.3186 -0.0019 0.0222  -0.0218 964  ARG A NH1 
3292 N NH2 . ARG A 427 ? 0.4282 0.4974 0.3620 0.0089  0.0206  -0.0477 964  ARG A NH2 
3293 N N   . LYS A 428 ? 0.3110 0.4251 0.3500 -0.0255 0.0046  0.0118  965  LYS A N   
3294 C CA  . LYS A 428 ? 0.2928 0.4283 0.3457 -0.0299 0.0063  0.0209  965  LYS A CA  
3295 C C   . LYS A 428 ? 0.3070 0.4289 0.3772 -0.0329 0.0003  0.0210  965  LYS A C   
3296 O O   . LYS A 428 ? 0.3169 0.4491 0.3944 -0.0319 0.0018  0.0192  965  LYS A O   
3297 C CB  . LYS A 428 ? 0.3408 0.4956 0.4001 -0.0386 0.0069  0.0388  965  LYS A CB  
3298 C CG  . LYS A 428 ? 0.4970 0.6696 0.5399 -0.0370 0.0134  0.0402  965  LYS A CG  
3299 C CD  . LYS A 428 ? 0.5666 0.7575 0.6164 -0.0468 0.0133  0.0587  965  LYS A CD  
3300 C CE  . LYS A 428 ? 0.5915 0.7968 0.6242 -0.0464 0.0186  0.0610  965  LYS A CE  
3301 N NZ  . LYS A 428 ? 0.7372 0.9551 0.7761 -0.0567 0.0168  0.0797  965  LYS A NZ  
3302 N N   . VAL A 429 ? 0.3165 0.4159 0.3939 -0.0368 -0.0065 0.0233  966  VAL A N   
3303 C CA  . VAL A 429 ? 0.3087 0.3929 0.4015 -0.0399 -0.0122 0.0226  966  VAL A CA  
3304 C C   . VAL A 429 ? 0.3445 0.4149 0.4294 -0.0319 -0.0118 0.0054  966  VAL A C   
3305 O O   . VAL A 429 ? 0.2983 0.3703 0.3927 -0.0322 -0.0131 0.0035  966  VAL A O   
3306 C CB  . VAL A 429 ? 0.3654 0.4265 0.4668 -0.0455 -0.0191 0.0271  966  VAL A CB  
3307 C CG1 . VAL A 429 ? 0.3825 0.4249 0.4973 -0.0480 -0.0245 0.0233  966  VAL A CG1 
3308 C CG2 . VAL A 429 ? 0.3612 0.4355 0.4731 -0.0541 -0.0206 0.0454  966  VAL A CG2 
3309 N N   . ALA A 430 ? 0.2894 0.3461 0.3565 -0.0250 -0.0102 -0.0072 967  ALA A N   
3310 C CA  . ALA A 430 ? 0.2967 0.3382 0.3542 -0.0175 -0.0102 -0.0239 967  ALA A CA  
3311 C C   . ALA A 430 ? 0.3377 0.3997 0.3934 -0.0125 -0.0054 -0.0276 967  ALA A C   
3312 O O   . ALA A 430 ? 0.3185 0.3712 0.3745 -0.0087 -0.0072 -0.0371 967  ALA A O   
3313 C CB  . ALA A 430 ? 0.2842 0.3095 0.3215 -0.0111 -0.0084 -0.0362 967  ALA A CB  
3314 N N   . GLU A 431 ? 0.3553 0.4448 0.4091 -0.0126 0.0005  -0.0203 968  GLU A N   
3315 C CA  . GLU A 431 ? 0.3876 0.4992 0.4424 -0.0087 0.0055  -0.0227 968  GLU A CA  
3316 C C   . GLU A 431 ? 0.3581 0.4739 0.4332 -0.0135 0.0016  -0.0169 968  GLU A C   
3317 O O   . GLU A 431 ? 0.3118 0.4290 0.3890 -0.0089 0.0016  -0.0250 968  GLU A O   
3318 C CB  . GLU A 431 ? 0.4664 0.6077 0.5177 -0.0099 0.0127  -0.0144 968  GLU A CB  
3319 C CG  . GLU A 431 ? 0.7413 0.8823 0.7734 -0.0065 0.0169  -0.0176 968  GLU A CG  
3320 C CD  . GLU A 431 ? 0.9622 1.1023 0.9762 0.0039  0.0221  -0.0335 968  GLU A CD  
3321 O OE1 . GLU A 431 ? 0.8952 1.0413 0.8937 0.0067  0.0271  -0.0357 968  GLU A OE1 
3322 O OE2 . GLU A 431 ? 1.0717 1.2050 1.0869 0.0092  0.0210  -0.0436 968  GLU A OE2 
3323 N N   . ILE A 432 ? 0.2867 0.4042 0.3771 -0.0228 -0.0020 -0.0030 969  ILE A N   
3324 C CA  . ILE A 432 ? 0.3026 0.4231 0.4128 -0.0283 -0.0060 0.0030  969  ILE A CA  
3325 C C   . ILE A 432 ? 0.2910 0.3839 0.4032 -0.0263 -0.0124 -0.0073 969  ILE A C   
3326 O O   . ILE A 432 ? 0.3296 0.4250 0.4494 -0.0248 -0.0138 -0.0114 969  ILE A O   
3327 C CB  . ILE A 432 ? 0.3812 0.5071 0.5066 -0.0390 -0.0087 0.0202  969  ILE A CB  
3328 C CG1 . ILE A 432 ? 0.3439 0.4968 0.4662 -0.0418 -0.0026 0.0307  969  ILE A CG1 
3329 C CG2 . ILE A 432 ? 0.3717 0.5011 0.5175 -0.0448 -0.0124 0.0260  969  ILE A CG2 
3330 C CD1 . ILE A 432 ? 0.4441 0.5997 0.5767 -0.0519 -0.0053 0.0474  969  ILE A CD1 
3331 N N   . THR A 433 ? 0.3747 0.4412 0.4799 -0.0265 -0.0162 -0.0121 970  THR A N   
3332 C CA  . THR A 433 ? 0.3219 0.3613 0.4280 -0.0255 -0.0220 -0.0222 970  THR A CA  
3333 C C   . THR A 433 ? 0.3878 0.4223 0.4802 -0.0159 -0.0203 -0.0379 970  THR A C   
3334 O O   . THR A 433 ? 0.3504 0.3706 0.4462 -0.0152 -0.0247 -0.0449 970  THR A O   
3335 C CB  . THR A 433 ? 0.3351 0.3465 0.4359 -0.0278 -0.0258 -0.0253 970  THR A CB  
3336 O OG1 . THR A 433 ? 0.3486 0.3571 0.4303 -0.0217 -0.0217 -0.0324 970  THR A OG1 
3337 C CG2 . THR A 433 ? 0.3573 0.3706 0.4741 -0.0375 -0.0287 -0.0098 970  THR A CG2 
3338 N N   . GLY A 434 ? 0.3534 0.3997 0.4305 -0.0088 -0.0142 -0.0434 971  GLY A N   
3339 C CA  . GLY A 434 ? 0.4276 0.4713 0.4922 0.0005  -0.0123 -0.0577 971  GLY A CA  
3340 C C   . GLY A 434 ? 0.4613 0.5213 0.5384 0.0015  -0.0127 -0.0568 971  GLY A C   
3341 O O   . GLY A 434 ? 0.4299 0.4801 0.5026 0.0071  -0.0149 -0.0679 971  GLY A O   
3342 N N   . GLU A 435 ? 0.3377 0.4226 0.4306 -0.0042 -0.0107 -0.0435 972  GLU A N   
3343 C CA  . GLU A 435 ? 0.3398 0.4434 0.4470 -0.0042 -0.0106 -0.0413 972  GLU A CA  
3344 C C   . GLU A 435 ? 0.4074 0.4936 0.5272 -0.0082 -0.0186 -0.0420 972  GLU A C   
3345 O O   . GLU A 435 ? 0.3817 0.4704 0.5065 -0.0047 -0.0206 -0.0477 972  GLU A O   
3346 C CB  . GLU A 435 ? 0.4285 0.5620 0.5491 -0.0106 -0.0063 -0.0264 972  GLU A CB  
3347 C CG  . GLU A 435 ? 0.5561 0.7107 0.6654 -0.0074 0.0021  -0.0250 972  GLU A CG  
3348 C CD  . GLU A 435 ? 0.8166 1.0014 0.9392 -0.0144 0.0065  -0.0107 972  GLU A CD  
3349 O OE1 . GLU A 435 ? 0.8143 0.9993 0.9426 -0.0228 0.0052  0.0019  972  GLU A OE1 
3350 O OE2 . GLU A 435 ? 0.9500 1.1579 1.0773 -0.0117 0.0114  -0.0120 972  GLU A OE2 
3351 N N   . ILE A 436 ? 0.3412 0.4098 0.4663 -0.0156 -0.0232 -0.0360 973  ILE A N   
3352 C CA  . ILE A 436 ? 0.3830 0.4326 0.5192 -0.0204 -0.0308 -0.0367 973  ILE A CA  
3353 C C   . ILE A 436 ? 0.4723 0.4981 0.5951 -0.0136 -0.0342 -0.0528 973  ILE A C   
3354 O O   . ILE A 436 ? 0.4391 0.4598 0.5686 -0.0133 -0.0387 -0.0569 973  ILE A O   
3355 C CB  . ILE A 436 ? 0.4018 0.4348 0.5443 -0.0291 -0.0345 -0.0288 973  ILE A CB  
3356 C CG1 . ILE A 436 ? 0.4773 0.5333 0.6338 -0.0365 -0.0318 -0.0119 973  ILE A CG1 
3357 C CG2 . ILE A 436 ? 0.4090 0.4201 0.5613 -0.0340 -0.0419 -0.0311 973  ILE A CG2 
3358 C CD1 . ILE A 436 ? 0.4563 0.4981 0.6189 -0.0445 -0.0350 -0.0033 973  ILE A CD1 
3359 N N   . GLN A 437 ? 0.5066 0.5183 0.6096 -0.0080 -0.0320 -0.0622 974  GLN A N   
3360 C CA  . GLN A 437 ? 0.4822 0.4682 0.5702 -0.0023 -0.0352 -0.0776 974  GLN A CA  
3361 C C   . GLN A 437 ? 0.5015 0.4962 0.5861 0.0056  -0.0349 -0.0861 974  GLN A C   
3362 O O   . GLN A 437 ? 0.5211 0.4954 0.5997 0.0081  -0.0399 -0.0963 974  GLN A O   
3363 C CB  . GLN A 437 ? 0.5233 0.4950 0.5906 0.0020  -0.0319 -0.0855 974  GLN A CB  
3364 C CG  . GLN A 437 ? 0.5676 0.5214 0.6372 -0.0053 -0.0343 -0.0809 974  GLN A CG  
3365 C CD  . GLN A 437 ? 0.6104 0.5478 0.6600 -0.0012 -0.0317 -0.0900 974  GLN A CD  
3366 O OE1 . GLN A 437 ? 0.6020 0.5543 0.6428 0.0028  -0.0259 -0.0888 974  GLN A OE1 
3367 N NE2 . GLN A 437 ? 0.5824 0.4890 0.6246 -0.0026 -0.0358 -0.0994 974  GLN A NE2 
3368 N N   . GLN A 438 ? 0.5186 0.5431 0.6073 0.0093  -0.0293 -0.0822 975  GLN A N   
3369 C CA  . GLN A 438 ? 0.6073 0.6401 0.6919 0.0180  -0.0284 -0.0915 975  GLN A CA  
3370 C C   . GLN A 438 ? 0.6158 0.6473 0.7158 0.0159  -0.0351 -0.0912 975  GLN A C   
3371 O O   . GLN A 438 ? 0.5441 0.5758 0.6409 0.0228  -0.0367 -0.1001 975  GLN A O   
3372 C CB  . GLN A 438 ? 0.6549 0.7208 0.7411 0.0221  -0.0201 -0.0877 975  GLN A CB  
3373 C CG  . GLN A 438 ? 0.7770 0.8706 0.8851 0.0154  -0.0184 -0.0736 975  GLN A CG  
3374 C CD  . GLN A 438 ? 0.8159 0.9418 0.9251 0.0195  -0.0099 -0.0715 975  GLN A CD  
3375 O OE1 . GLN A 438 ? 0.8060 0.9424 0.9155 0.0266  -0.0085 -0.0790 975  GLN A OE1 
3376 N NE2 . GLN A 438 ? 0.7692 0.9110 0.8792 0.0147  -0.0044 -0.0612 975  GLN A NE2 
3377 N N   . TYR A 439 ? 0.6003 0.6294 0.7167 0.0063  -0.0393 -0.0812 976  TYR A N   
3378 C CA  . TYR A 439 ? 0.5193 0.5475 0.6512 0.0033  -0.0458 -0.0801 976  TYR A CA  
3379 C C   . TYR A 439 ? 0.4682 0.4632 0.5979 -0.0017 -0.0538 -0.0844 976  TYR A C   
3380 O O   . TYR A 439 ? 0.4779 0.4700 0.6209 -0.0059 -0.0597 -0.0823 976  TYR A O   
3381 C CB  . TYR A 439 ? 0.5022 0.5562 0.6572 -0.0043 -0.0443 -0.0651 976  TYR A CB  
3382 C CG  . TYR A 439 ? 0.4746 0.5628 0.6339 -0.0007 -0.0364 -0.0606 976  TYR A CG  
3383 C CD1 . TYR A 439 ? 0.5290 0.6344 0.6931 0.0059  -0.0353 -0.0658 976  TYR A CD1 
3384 C CD2 . TYR A 439 ? 0.5566 0.6598 0.7155 -0.0042 -0.0300 -0.0511 976  TYR A CD2 
3385 C CE1 . TYR A 439 ? 0.5650 0.7017 0.7334 0.0088  -0.0275 -0.0624 976  TYR A CE1 
3386 C CE2 . TYR A 439 ? 0.5675 0.7017 0.7295 -0.0017 -0.0224 -0.0471 976  TYR A CE2 
3387 C CZ  . TYR A 439 ? 0.5980 0.7490 0.7648 0.0047  -0.0208 -0.0531 976  TYR A CZ  
3388 O OH  . TYR A 439 ? 0.5541 0.7360 0.7244 0.0068  -0.0127 -0.0499 976  TYR A OH  
3389 N N   . GLN A 440 ? 0.4931 0.5291 0.6548 -0.1394 -0.0979 0.0498  977  GLN A N   
3390 C CA  . GLN A 440 ? 0.4570 0.4963 0.6144 -0.1370 -0.0860 0.0579  977  GLN A CA  
3391 C C   . GLN A 440 ? 0.5552 0.5784 0.7036 -0.1419 -0.0810 0.0651  977  GLN A C   
3392 O O   . GLN A 440 ? 0.5319 0.5563 0.6748 -0.1404 -0.0710 0.0718  977  GLN A O   
3393 C CB  . GLN A 440 ? 0.4050 0.4687 0.5826 -0.1401 -0.0803 0.0616  977  GLN A CB  
3394 C CG  . GLN A 440 ? 0.3611 0.4416 0.5441 -0.1324 -0.0813 0.0572  977  GLN A CG  
3395 C CD  . GLN A 440 ? 0.3591 0.4642 0.5626 -0.1349 -0.0759 0.0611  977  GLN A CD  
3396 O OE1 . GLN A 440 ? 0.3791 0.4920 0.5977 -0.1442 -0.0762 0.0636  977  GLN A OE1 
3397 N NE2 . GLN A 440 ? 0.3276 0.4451 0.5322 -0.1268 -0.0708 0.0615  977  GLN A NE2 
3398 N N   . ASN A 441 ? 0.5664 0.5742 0.7129 -0.1477 -0.0876 0.0639  978  ASN A N   
3399 C CA  . ASN A 441 ? 0.7147 0.7063 0.8523 -0.1523 -0.0832 0.0713  978  ASN A CA  
3400 C C   . ASN A 441 ? 0.6877 0.6560 0.8061 -0.1482 -0.0891 0.0686  978  ASN A C   
3401 O O   . ASN A 441 ? 0.7051 0.6581 0.8220 -0.1538 -0.0933 0.0699  978  ASN A O   
3402 C CB  . ASN A 441 ? 0.8637 0.8569 1.0173 -0.1643 -0.0840 0.0746  978  ASN A CB  
3403 C CG  . ASN A 441 ? 1.0182 1.0344 1.1941 -0.1684 -0.0858 0.0712  978  ASN A CG  
3404 O OD1 . ASN A 441 ? 1.0119 1.0466 1.1977 -0.1686 -0.0783 0.0751  978  ASN A OD1 
3405 N ND2 . ASN A 441 ? 1.0350 1.0505 1.2190 -0.1717 -0.0959 0.0638  978  ASN A ND2 
3406 N N   . GLN A 442 ? 0.6877 0.6534 0.7914 -0.1383 -0.0893 0.0649  979  GLN A N   
3407 C CA  . GLN A 442 ? 0.7362 0.6819 0.8216 -0.1334 -0.0954 0.0613  979  GLN A CA  
3408 C C   . GLN A 442 ? 0.5893 0.5292 0.6549 -0.1256 -0.0886 0.0645  979  GLN A C   
3409 O O   . GLN A 442 ? 0.5338 0.4772 0.5914 -0.1174 -0.0895 0.0589  979  GLN A O   
3410 C CB  . GLN A 442 ? 0.8130 0.7602 0.8998 -0.1292 -0.1057 0.0504  979  GLN A CB  
3411 C CG  . GLN A 442 ? 0.8332 0.7876 0.9393 -0.1367 -0.1130 0.0459  979  GLN A CG  
3412 C CD  . GLN A 442 ? 0.8428 0.8033 0.9511 -0.1323 -0.1219 0.0353  979  GLN A CD  
3413 O OE1 . GLN A 442 ? 0.7893 0.7464 0.8838 -0.1237 -0.1233 0.0311  979  GLN A OE1 
3414 N NE2 . GLN A 442 ? 0.8235 0.7940 0.9473 -0.1367 -0.1263 0.0304  979  GLN A NE2 
3415 N N   . PRO A 443 ? 0.5298 0.4610 0.5872 -0.1284 -0.0816 0.0733  980  PRO A N   
3416 C CA  . PRO A 443 ? 0.5529 0.4791 0.5913 -0.1220 -0.0745 0.0768  980  PRO A CA  
3417 C C   . PRO A 443 ? 0.5410 0.4511 0.5604 -0.1152 -0.0811 0.0718  980  PRO A C   
3418 O O   . PRO A 443 ? 0.5189 0.4151 0.5366 -0.1173 -0.0896 0.0697  980  PRO A O   
3419 C CB  . PRO A 443 ? 0.7171 0.6368 0.7533 -0.1288 -0.0673 0.0875  980  PRO A CB  
3420 C CG  . PRO A 443 ? 0.6980 0.6099 0.7455 -0.1372 -0.0741 0.0883  980  PRO A CG  
3421 C CD  . PRO A 443 ? 0.6093 0.5352 0.6750 -0.1383 -0.0799 0.0806  980  PRO A CD  
3422 N N   . TYR A 444 ? 0.4880 0.4000 0.4934 -0.1071 -0.0769 0.0698  981  TYR A N   
3423 C CA  . TYR A 444 ? 0.4594 0.3573 0.4449 -0.1004 -0.0818 0.0656  981  TYR A CA  
3424 C C   . TYR A 444 ? 0.5009 0.3849 0.4701 -0.1013 -0.0773 0.0736  981  TYR A C   
3425 O O   . TYR A 444 ? 0.5096 0.3985 0.4774 -0.1037 -0.0673 0.0813  981  TYR A O   
3426 C CB  . TYR A 444 ? 0.4416 0.3478 0.4189 -0.0917 -0.0792 0.0594  981  TYR A CB  
3427 C CG  . TYR A 444 ? 0.4101 0.3242 0.3969 -0.0890 -0.0871 0.0497  981  TYR A CG  
3428 C CD1 . TYR A 444 ? 0.4043 0.3358 0.4099 -0.0911 -0.0852 0.0488  981  TYR A CD1 
3429 C CD2 . TYR A 444 ? 0.4482 0.3529 0.4253 -0.0843 -0.0964 0.0416  981  TYR A CD2 
3430 C CE1 . TYR A 444 ? 0.3925 0.3317 0.4066 -0.0890 -0.0926 0.0405  981  TYR A CE1 
3431 C CE2 . TYR A 444 ? 0.4023 0.3147 0.3879 -0.0823 -0.1036 0.0328  981  TYR A CE2 
3432 C CZ  . TYR A 444 ? 0.4048 0.3343 0.4086 -0.0847 -0.1017 0.0325  981  TYR A CZ  
3433 O OH  . TYR A 444 ? 0.4306 0.3684 0.4425 -0.0830 -0.1089 0.0242  981  TYR A OH  
3434 N N   . CYS A 445 ? 0.4704 0.3379 0.4272 -0.0990 -0.0849 0.0717  982  CYS A N   
3435 C CA  . CYS A 445 ? 0.5601 0.4140 0.4997 -0.0989 -0.0819 0.0790  982  CYS A CA  
3436 C C   . CYS A 445 ? 0.5476 0.4028 0.4683 -0.0907 -0.0775 0.0766  982  CYS A C   
3437 O O   . CYS A 445 ? 0.5363 0.3802 0.4413 -0.0859 -0.0826 0.0738  982  CYS A O   
3438 C CB  . CYS A 445 ? 0.6047 0.4404 0.5403 -0.0999 -0.0921 0.0784  982  CYS A CB  
3439 S SG  . CYS A 445 ? 0.7448 0.5633 0.6622 -0.1013 -0.0890 0.0896  982  CYS A SG  
3440 N N   . LEU A 446 ? 0.4804 0.3501 0.4032 -0.0893 -0.0679 0.0772  983  LEU A N   
3441 C CA  . LEU A 446 ? 0.4273 0.3001 0.3339 -0.0821 -0.0625 0.0742  983  LEU A CA  
3442 C C   . LEU A 446 ? 0.4716 0.3527 0.3764 -0.0843 -0.0493 0.0819  983  LEU A C   
3443 O O   . LEU A 446 ? 0.4857 0.3779 0.4067 -0.0892 -0.0442 0.0855  983  LEU A O   
3444 C CB  . LEU A 446 ? 0.4434 0.3265 0.3550 -0.0763 -0.0650 0.0641  983  LEU A CB  
3445 C CG  . LEU A 446 ? 0.5022 0.3793 0.4155 -0.0737 -0.0777 0.0551  983  LEU A CG  
3446 C CD1 . LEU A 446 ? 0.4603 0.3506 0.3830 -0.0699 -0.0790 0.0468  983  LEU A CD1 
3447 C CD2 . LEU A 446 ? 0.5228 0.3863 0.4149 -0.0684 -0.0823 0.0521  983  LEU A CD2 
3448 N N   . ARG A 447 ? 0.4795 0.3560 0.3649 -0.0811 -0.0440 0.0842  984  ARG A N   
3449 C CA  . ARG A 447 ? 0.5138 0.3979 0.3952 -0.0831 -0.0311 0.0910  984  ARG A CA  
3450 C C   . ARG A 447 ? 0.4827 0.3815 0.3666 -0.0779 -0.0237 0.0853  984  ARG A C   
3451 O O   . ARG A 447 ? 0.4773 0.3756 0.3535 -0.0711 -0.0269 0.0770  984  ARG A O   
3452 C CB  . ARG A 447 ? 0.5854 0.4587 0.4446 -0.0823 -0.0286 0.0960  984  ARG A CB  
3453 C CG  . ARG A 447 ? 0.6777 0.5575 0.5323 -0.0859 -0.0157 0.1041  984  ARG A CG  
3454 C CD  . ARG A 447 ? 0.7820 0.6512 0.6141 -0.0854 -0.0142 0.1092  984  ARG A CD  
3455 N NE  . ARG A 447 ? 0.8431 0.6966 0.6722 -0.0885 -0.0235 0.1141  984  ARG A NE  
3456 C CZ  . ARG A 447 ? 0.8053 0.6543 0.6412 -0.0962 -0.0227 0.1236  984  ARG A CZ  
3457 N NH1 . ARG A 447 ? 0.7089 0.5687 0.5550 -0.1019 -0.0131 0.1292  984  ARG A NH1 
3458 N NH2 . ARG A 447 ? 0.8311 0.6647 0.6638 -0.0981 -0.0315 0.1275  984  ARG A NH2 
3459 N N   . ILE A 448 ? 0.4436 0.3552 0.3389 -0.0813 -0.0138 0.0897  985  ILE A N   
3460 C CA  . ILE A 448 ? 0.3986 0.3241 0.2971 -0.0764 -0.0055 0.0852  985  ILE A CA  
3461 C C   . ILE A 448 ? 0.4854 0.4087 0.3630 -0.0722 0.0024  0.0848  985  ILE A C   
3462 O O   . ILE A 448 ? 0.5217 0.4393 0.3876 -0.0758 0.0068  0.0917  985  ILE A O   
3463 C CB  . ILE A 448 ? 0.5393 0.4800 0.4568 -0.0812 0.0032  0.0904  985  ILE A CB  
3464 C CG1 . ILE A 448 ? 0.6476 0.5936 0.5870 -0.0846 -0.0044 0.0891  985  ILE A CG1 
3465 C CG2 . ILE A 448 ? 0.4881 0.4422 0.4070 -0.0760 0.0136  0.0870  985  ILE A CG2 
3466 C CD1 . ILE A 448 ? 0.7311 0.6930 0.6901 -0.0894 0.0034  0.0938  985  ILE A CD1 
3467 N N   . GLU A 449 ? 0.4425 0.3699 0.3147 -0.0650 0.0040  0.0766  986  GLU A N   
3468 C CA  . GLU A 449 ? 0.4119 0.3402 0.2667 -0.0611 0.0132  0.0751  986  GLU A CA  
3469 C C   . GLU A 449 ? 0.4161 0.3600 0.2827 -0.0599 0.0247  0.0747  986  GLU A C   
3470 O O   . GLU A 449 ? 0.4443 0.3952 0.3207 -0.0553 0.0236  0.0684  986  GLU A O   
3471 C CB  . GLU A 449 ? 0.4581 0.3794 0.2980 -0.0539 0.0073  0.0659  986  GLU A CB  
3472 C CG  . GLU A 449 ? 0.5080 0.4238 0.3241 -0.0516 0.0129  0.0655  986  GLU A CG  
3473 C CD  . GLU A 449 ? 0.5782 0.5045 0.3924 -0.0511 0.0275  0.0666  986  GLU A CD  
3474 O OE1 . GLU A 449 ? 0.5695 0.4941 0.3704 -0.0539 0.0345  0.0718  986  GLU A OE1 
3475 O OE2 . GLU A 449 ? 0.5711 0.5076 0.3971 -0.0479 0.0322  0.0623  986  GLU A OE2 
3476 N N   . PRO A 450 ? 0.4615 0.4111 0.3277 -0.0641 0.0358  0.0816  987  PRO A N   
3477 C CA  . PRO A 450 ? 0.4544 0.4198 0.3354 -0.0638 0.0465  0.0822  987  PRO A CA  
3478 C C   . PRO A 450 ? 0.5040 0.4753 0.3817 -0.0559 0.0522  0.0739  987  PRO A C   
3479 O O   . PRO A 450 ? 0.4705 0.4529 0.3653 -0.0534 0.0542  0.0715  987  PRO A O   
3480 C CB  . PRO A 450 ? 0.4970 0.4649 0.3720 -0.0696 0.0572  0.0903  987  PRO A CB  
3481 C CG  . PRO A 450 ? 0.6288 0.5837 0.4957 -0.0751 0.0495  0.0964  987  PRO A CG  
3482 C CD  . PRO A 450 ? 0.5099 0.4523 0.3643 -0.0700 0.0382  0.0899  987  PRO A CD  
3483 N N   . ASP A 451 ? 0.4836 0.4480 0.3403 -0.0520 0.0546  0.0698  988  ASP A N   
3484 C CA  . ASP A 451 ? 0.4425 0.4112 0.2953 -0.0447 0.0601  0.0617  988  ASP A CA  
3485 C C   . ASP A 451 ? 0.4068 0.3744 0.2673 -0.0396 0.0501  0.0544  988  ASP A C   
3486 O O   . ASP A 451 ? 0.4250 0.4010 0.2955 -0.0349 0.0540  0.0501  988  ASP A O   
3487 C CB  . ASP A 451 ? 0.4539 0.4147 0.2814 -0.0424 0.0639  0.0583  988  ASP A CB  
3488 C CG  . ASP A 451 ? 0.5749 0.5400 0.3943 -0.0463 0.0766  0.0638  988  ASP A CG  
3489 O OD1 . ASP A 451 ? 0.5610 0.5376 0.3946 -0.0483 0.0857  0.0673  988  ASP A OD1 
3490 O OD2 . ASP A 451 ? 0.6008 0.5584 0.3995 -0.0472 0.0776  0.0643  988  ASP A OD2 
3491 N N   . MET A 452 ? 0.3790 0.3360 0.2344 -0.0403 0.0374  0.0531  989  MET A N   
3492 C CA  . MET A 452 ? 0.3829 0.3389 0.2454 -0.0362 0.0274  0.0462  989  MET A CA  
3493 C C   . MET A 452 ? 0.3942 0.3614 0.2822 -0.0380 0.0254  0.0485  989  MET A C   
3494 O O   . MET A 452 ? 0.3956 0.3689 0.2933 -0.0336 0.0233  0.0434  989  MET A O   
3495 C CB  . MET A 452 ? 0.4136 0.3564 0.2660 -0.0370 0.0143  0.0444  989  MET A CB  
3496 C CG  . MET A 452 ? 0.4162 0.3489 0.2438 -0.0340 0.0144  0.0405  989  MET A CG  
3497 S SD  . MET A 452 ? 0.4772 0.3955 0.2954 -0.0343 -0.0015 0.0378  989  MET A SD  
3498 C CE  . MET A 452 ? 0.4146 0.3366 0.2462 -0.0301 -0.0108 0.0290  989  MET A CE  
3499 N N   . ARG A 453 ? 0.3964 0.3667 0.2951 -0.0447 0.0261  0.0564  990  ARG A N   
3500 C CA  . ARG A 453 ? 0.3676 0.3503 0.2909 -0.0472 0.0255  0.0591  990  ARG A CA  
3501 C C   . ARG A 453 ? 0.3956 0.3924 0.3291 -0.0429 0.0362  0.0578  990  ARG A C   
3502 O O   . ARG A 453 ? 0.3714 0.3770 0.3203 -0.0400 0.0333  0.0549  990  ARG A O   
3503 C CB  . ARG A 453 ? 0.3579 0.3417 0.2891 -0.0557 0.0267  0.0681  990  ARG A CB  
3504 C CG  . ARG A 453 ? 0.4449 0.4430 0.4015 -0.0591 0.0272  0.0714  990  ARG A CG  
3505 C CD  . ARG A 453 ? 0.4980 0.4965 0.4663 -0.0584 0.0148  0.0669  990  ARG A CD  
3506 N NE  . ARG A 453 ? 0.5663 0.5749 0.5564 -0.0646 0.0129  0.0716  990  ARG A NE  
3507 C CZ  . ARG A 453 ? 0.5733 0.5758 0.5679 -0.0713 0.0048  0.0745  990  ARG A CZ  
3508 N NH1 . ARG A 453 ? 0.4181 0.4041 0.3976 -0.0721 -0.0028 0.0733  990  ARG A NH1 
3509 N NH2 . ARG A 453 ? 0.5348 0.5480 0.5498 -0.0771 0.0042  0.0784  990  ARG A NH2 
3510 N N   . ARG A 454 ? 0.3953 0.3945 0.3204 -0.0424 0.0486  0.0598  991  ARG A N   
3511 C CA  . ARG A 454 ? 0.3714 0.3833 0.3056 -0.0380 0.0597  0.0584  991  ARG A CA  
3512 C C   . ARG A 454 ? 0.4459 0.4563 0.3762 -0.0298 0.0576  0.0498  991  ARG A C   
3513 O O   . ARG A 454 ? 0.4195 0.4405 0.3648 -0.0258 0.0602  0.0480  991  ARG A O   
3514 C CB  . ARG A 454 ? 0.4051 0.4184 0.3284 -0.0391 0.0734  0.0611  991  ARG A CB  
3515 C CG  . ARG A 454 ? 0.5538 0.5742 0.4866 -0.0467 0.0791  0.0699  991  ARG A CG  
3516 C CD  . ARG A 454 ? 0.6286 0.6517 0.5504 -0.0477 0.0932  0.0721  991  ARG A CD  
3517 N NE  . ARG A 454 ? 0.7264 0.7364 0.6247 -0.0504 0.0920  0.0733  991  ARG A NE  
3518 C CZ  . ARG A 454 ? 0.6956 0.7008 0.5897 -0.0579 0.0900  0.0807  991  ARG A CZ  
3519 N NH1 . ARG A 454 ? 0.6152 0.6273 0.5268 -0.0638 0.0892  0.0872  991  ARG A NH1 
3520 N NH2 . ARG A 454 ? 0.5866 0.5802 0.4589 -0.0595 0.0888  0.0818  991  ARG A NH2 
3521 N N   . PHE A 455 ? 0.3465 0.3439 0.2567 -0.0274 0.0527  0.0446  992  PHE A N   
3522 C CA  . PHE A 455 ? 0.3487 0.3433 0.2531 -0.0202 0.0502  0.0362  992  PHE A CA  
3523 C C   . PHE A 455 ? 0.3902 0.3902 0.3120 -0.0185 0.0405  0.0341  992  PHE A C   
3524 O O   . PHE A 455 ? 0.3861 0.3928 0.3160 -0.0131 0.0429  0.0305  992  PHE A O   
3525 C CB  . PHE A 455 ? 0.3456 0.3255 0.2263 -0.0191 0.0446  0.0313  992  PHE A CB  
3526 C CG  . PHE A 455 ? 0.3871 0.3633 0.2607 -0.0124 0.0413  0.0223  992  PHE A CG  
3527 C CD1 . PHE A 455 ? 0.4655 0.4431 0.3313 -0.0073 0.0516  0.0178  992  PHE A CD1 
3528 C CD2 . PHE A 455 ? 0.4097 0.3808 0.2840 -0.0115 0.0281  0.0182  992  PHE A CD2 
3529 C CE1 . PHE A 455 ? 0.4652 0.4387 0.3239 -0.0016 0.0487  0.0097  992  PHE A CE1 
3530 C CE2 . PHE A 455 ? 0.4658 0.4335 0.3329 -0.0058 0.0251  0.0100  992  PHE A CE2 
3531 C CZ  . PHE A 455 ? 0.4189 0.3876 0.2781 -0.0009 0.0355  0.0059  992  PHE A CZ  
3532 N N   . PHE A 456 ? 0.3647 0.3620 0.2926 -0.0234 0.0296  0.0366  993  PHE A N   
3533 C CA  . PHE A 456 ? 0.3554 0.3578 0.2985 -0.0225 0.0197  0.0342  993  PHE A CA  
3534 C C   . PHE A 456 ? 0.4301 0.4489 0.3976 -0.0237 0.0238  0.0389  993  PHE A C   
3535 O O   . PHE A 456 ? 0.3587 0.3855 0.3391 -0.0204 0.0201  0.0364  993  PHE A O   
3536 C CB  . PHE A 456 ? 0.3630 0.3563 0.3035 -0.0271 0.0066  0.0340  993  PHE A CB  
3537 C CG  . PHE A 456 ? 0.3241 0.3032 0.2431 -0.0243 0.0007  0.0276  993  PHE A CG  
3538 C CD1 . PHE A 456 ? 0.3353 0.3136 0.2498 -0.0182 -0.0024 0.0199  993  PHE A CD1 
3539 C CD2 . PHE A 456 ? 0.3994 0.3666 0.3027 -0.0275 -0.0014 0.0294  993  PHE A CD2 
3540 C CE1 . PHE A 456 ? 0.4022 0.3684 0.2969 -0.0156 -0.0076 0.0136  993  PHE A CE1 
3541 C CE2 . PHE A 456 ? 0.4602 0.4154 0.3439 -0.0245 -0.0068 0.0233  993  PHE A CE2 
3542 C CZ  . PHE A 456 ? 0.4391 0.3942 0.3187 -0.0187 -0.0098 0.0152  993  PHE A CZ  
3543 N N   . GLU A 457 ? 0.3502 0.3747 0.3240 -0.0283 0.0317  0.0459  994  GLU A N   
3544 C CA  . GLU A 457 ? 0.3259 0.3673 0.3229 -0.0293 0.0368  0.0503  994  GLU A CA  
3545 C C   . GLU A 457 ? 0.3807 0.4308 0.3821 -0.0217 0.0463  0.0477  994  GLU A C   
3546 O O   . GLU A 457 ? 0.4256 0.4893 0.4465 -0.0196 0.0471  0.0488  994  GLU A O   
3547 C CB  . GLU A 457 ? 0.3958 0.4412 0.3971 -0.0362 0.0439  0.0581  994  GLU A CB  
3548 C CG  . GLU A 457 ? 0.4466 0.4876 0.4519 -0.0443 0.0346  0.0621  994  GLU A CG  
3549 C CD  . GLU A 457 ? 0.6016 0.6433 0.6068 -0.0516 0.0416  0.0699  994  GLU A CD  
3550 O OE1 . GLU A 457 ? 0.5644 0.6072 0.5613 -0.0505 0.0532  0.0716  994  GLU A OE1 
3551 O OE2 . GLU A 457 ? 0.5099 0.5510 0.5233 -0.0586 0.0356  0.0740  994  GLU A OE2 
3552 N N   . ASN A 458 ? 0.3868 0.4291 0.3703 -0.0177 0.0536  0.0441  995  ASN A N   
3553 C CA  . ASN A 458 ? 0.4211 0.4699 0.4072 -0.0108 0.0643  0.0416  995  ASN A CA  
3554 C C   . ASN A 458 ? 0.4224 0.4661 0.4022 -0.0034 0.0603  0.0340  995  ASN A C   
3555 O O   . ASN A 458 ? 0.4189 0.4657 0.3986 0.0027  0.0693  0.0313  995  ASN A O   
3556 C CB  . ASN A 458 ? 0.5247 0.5696 0.4960 -0.0112 0.0768  0.0422  995  ASN A CB  
3557 C CG  . ASN A 458 ? 0.5613 0.6131 0.5401 -0.0181 0.0828  0.0500  995  ASN A CG  
3558 O OD1 . ASN A 458 ? 0.5432 0.6067 0.5423 -0.0211 0.0813  0.0547  995  ASN A OD1 
3559 N ND2 . ASN A 458 ? 0.5185 0.5637 0.4806 -0.0212 0.0896  0.0513  995  ASN A ND2 
3560 N N   . LEU A 459 ? 0.3605 0.3965 0.3351 -0.0040 0.0473  0.0305  996  LEU A N   
3561 C CA  . LEU A 459 ? 0.3857 0.4169 0.3540 0.0023  0.0428  0.0234  996  LEU A CA  
3562 C C   . LEU A 459 ? 0.3731 0.4170 0.3595 0.0079  0.0466  0.0236  996  LEU A C   
3563 O O   . LEU A 459 ? 0.3443 0.4006 0.3513 0.0060  0.0437  0.0282  996  LEU A O   
3564 C CB  . LEU A 459 ? 0.4388 0.4637 0.4045 0.0001  0.0275  0.0203  996  LEU A CB  
3565 C CG  . LEU A 459 ? 0.5209 0.5301 0.4646 -0.0022 0.0211  0.0165  996  LEU A CG  
3566 C CD1 . LEU A 459 ? 0.5303 0.5363 0.4759 -0.0030 0.0064  0.0126  996  LEU A CD1 
3567 C CD2 . LEU A 459 ? 0.5518 0.5519 0.4749 0.0026  0.0279  0.0109  996  LEU A CD2 
3568 N N   . ASN A 460 ? 0.3174 0.3581 0.2962 0.0146  0.0532  0.0188  997  ASN A N   
3569 C CA  . ASN A 460 ? 0.3352 0.3864 0.3299 0.0210  0.0573  0.0189  997  ASN A CA  
3570 C C   . ASN A 460 ? 0.3948 0.4377 0.3785 0.0271  0.0548  0.0117  997  ASN A C   
3571 O O   . ASN A 460 ? 0.4091 0.4492 0.3867 0.0325  0.0647  0.0087  997  ASN A O   
3572 C CB  . ASN A 460 ? 0.3974 0.4566 0.3993 0.0235  0.0726  0.0220  997  ASN A CB  
3573 C CG  . ASN A 460 ? 0.4102 0.4810 0.4307 0.0303  0.0766  0.0229  997  ASN A CG  
3574 O OD1 . ASN A 460 ? 0.5439 0.6243 0.5814 0.0303  0.0685  0.0256  997  ASN A OD1 
3575 N ND2 . ASN A 460 ? 0.5307 0.6005 0.5480 0.0361  0.0887  0.0205  997  ASN A ND2 
3576 N N   . PRO A 461 ? 0.3019 0.3407 0.2831 0.0261  0.0416  0.0087  998  PRO A N   
3577 C CA  . PRO A 461 ? 0.2747 0.3049 0.2438 0.0312  0.0388  0.0016  998  PRO A CA  
3578 C C   . PRO A 461 ? 0.3230 0.3601 0.3033 0.0386  0.0451  0.0015  998  PRO A C   
3579 O O   . PRO A 461 ? 0.3474 0.3760 0.3153 0.0433  0.0490  -0.0041 998  PRO A O   
3580 C CB  . PRO A 461 ? 0.2815 0.3103 0.2515 0.0280  0.0231  -0.0003 998  PRO A CB  
3581 C CG  . PRO A 461 ? 0.3444 0.3850 0.3338 0.0228  0.0187  0.0066  998  PRO A CG  
3582 C CD  . PRO A 461 ? 0.3073 0.3496 0.2970 0.0201  0.0292  0.0114  998  PRO A CD  
3583 N N   . MET A 462 ? 0.3109 0.3629 0.3144 0.0395  0.0461  0.0075  999  MET A N   
3584 C CA  . MET A 462 ? 0.3186 0.3776 0.3343 0.0469  0.0506  0.0080  999  MET A CA  
3585 C C   . MET A 462 ? 0.3011 0.3588 0.3144 0.0519  0.0664  0.0075  999  MET A C   
3586 O O   . MET A 462 ? 0.3735 0.4314 0.3903 0.0588  0.0713  0.0058  999  MET A O   
3587 C CB  . MET A 462 ? 0.2959 0.3726 0.3379 0.0465  0.0465  0.0148  999  MET A CB  
3588 C CG  . MET A 462 ? 0.3361 0.4153 0.3823 0.0433  0.0309  0.0142  999  MET A CG  
3589 S SD  . MET A 462 ? 0.5150 0.6165 0.5918 0.0422  0.0261  0.0221  999  MET A SD  
3590 C CE  . MET A 462 ? 0.6640 0.7682 0.7435 0.0318  0.0213  0.0254  999  MET A CE  
3591 N N   . GLY A 463 ? 0.3515 0.4076 0.3587 0.0483  0.0745  0.0088  1000 GLY A N   
3592 C CA  . GLY A 463 ? 0.3836 0.4401 0.3897 0.0523  0.0901  0.0083  1000 GLY A CA  
3593 C C   . GLY A 463 ? 0.3654 0.4372 0.3963 0.0573  0.0961  0.0135  1000 GLY A C   
3594 O O   . GLY A 463 ? 0.3827 0.4678 0.4316 0.0543  0.0931  0.0199  1000 GLY A O   
3595 N N   . SER A 464 ? 0.3206 0.3907 0.3528 0.0650  0.1044  0.0108  1001 SER A N   
3596 C CA  . SER A 464 ? 0.3473 0.4316 0.4033 0.0709  0.1103  0.0157  1001 SER A CA  
3597 C C   . SER A 464 ? 0.3722 0.4622 0.4411 0.0747  0.1000  0.0175  1001 SER A C   
3598 O O   . SER A 464 ? 0.3618 0.4646 0.4516 0.0799  0.1030  0.0222  1001 SER A O   
3599 C CB  . SER A 464 ? 0.3880 0.4681 0.4407 0.0776  0.1256  0.0123  1001 SER A CB  
3600 O OG  . SER A 464 ? 0.5591 0.6402 0.6074 0.0743  0.1366  0.0125  1001 SER A OG  
3601 N N   . ALA A 465 ? 0.3250 0.4060 0.3816 0.0724  0.0879  0.0139  1002 ALA A N   
3602 C CA  . ALA A 465 ? 0.3182 0.4037 0.3846 0.0758  0.0782  0.0150  1002 ALA A CA  
3603 C C   . ALA A 465 ? 0.3208 0.4229 0.4078 0.0720  0.0686  0.0217  1002 ALA A C   
3604 O O   . ALA A 465 ? 0.3390 0.4445 0.4267 0.0648  0.0651  0.0239  1002 ALA A O   
3605 C CB  . ALA A 465 ? 0.3478 0.4184 0.3935 0.0744  0.0688  0.0082  1002 ALA A CB  
3606 N N   . SER A 466 ? 0.3508 0.4631 0.4543 0.0768  0.0645  0.0252  1003 SER A N   
3607 C CA  . SER A 466 ? 0.4055 0.5329 0.5265 0.0730  0.0532  0.0304  1003 SER A CA  
3608 C C   . SER A 466 ? 0.3217 0.4407 0.4290 0.0672  0.0391  0.0261  1003 SER A C   
3609 O O   . SER A 466 ? 0.3273 0.4303 0.4140 0.0679  0.0380  0.0195  1003 SER A O   
3610 C CB  . SER A 466 ? 0.4487 0.5894 0.5899 0.0800  0.0523  0.0352  1003 SER A CB  
3611 O OG  . SER A 466 ? 0.3781 0.5091 0.5093 0.0844  0.0476  0.0312  1003 SER A OG  
3612 N N   . GLU A 467 ? 0.3991 0.3986 0.4126 0.0853  0.0463  -0.0194 1004 GLU A N   
3613 C CA  . GLU A 467 ? 0.3800 0.3954 0.4041 0.0809  0.0420  -0.0166 1004 GLU A CA  
3614 C C   . GLU A 467 ? 0.3402 0.3532 0.3594 0.0801  0.0390  -0.0113 1004 GLU A C   
3615 O O   . GLU A 467 ? 0.3887 0.4037 0.4077 0.0725  0.0350  -0.0077 1004 GLU A O   
3616 C CB  . GLU A 467 ? 0.5114 0.5504 0.5540 0.0865  0.0431  -0.0202 1004 GLU A CB  
3617 C CG  . GLU A 467 ? 0.6037 0.6598 0.6586 0.0819  0.0390  -0.0182 1004 GLU A CG  
3618 C CD  . GLU A 467 ? 0.7636 0.8380 0.8351 0.0833  0.0401  -0.0225 1004 GLU A CD  
3619 O OE1 . GLU A 467 ? 0.7390 0.8308 0.8235 0.0824  0.0380  -0.0222 1004 GLU A OE1 
3620 O OE2 . GLU A 467 ? 0.8429 0.9139 0.9142 0.0848  0.0433  -0.0265 1004 GLU A OE2 
3621 N N   . LYS A 468 ? 0.4670 0.4753 0.4819 0.0876  0.0409  -0.0108 1005 LYS A N   
3622 C CA  . LYS A 468 ? 0.4812 0.4847 0.4894 0.0869  0.0384  -0.0053 1005 LYS A CA  
3623 C C   . LYS A 468 ? 0.3945 0.3760 0.3858 0.0782  0.0367  -0.0017 1005 LYS A C   
3624 O O   . LYS A 468 ? 0.4186 0.4007 0.4071 0.0715  0.0331  0.0026  1005 LYS A O   
3625 C CB  . LYS A 468 ? 0.4935 0.4938 0.4991 0.0973  0.0407  -0.0052 1005 LYS A CB  
3626 C CG  . LYS A 468 ? 0.5478 0.5383 0.5432 0.0963  0.0382  0.0010  1005 LYS A CG  
3627 C CD  . LYS A 468 ? 0.7600 0.7716 0.7663 0.0957  0.0350  0.0037  1005 LYS A CD  
3628 C CE  . LYS A 468 ? 0.8063 0.8099 0.8028 0.0876  0.0314  0.0098  1005 LYS A CE  
3629 N NZ  . LYS A 468 ? 0.7523 0.7736 0.7591 0.0796  0.0282  0.0099  1005 LYS A NZ  
3630 N N   . GLU A 469 ? 0.3895 0.3523 0.3695 0.0779  0.0397  -0.0038 1006 GLU A N   
3631 C CA  . GLU A 469 ? 0.3819 0.3234 0.3453 0.0692  0.0387  -0.0011 1006 GLU A CA  
3632 C C   . GLU A 469 ? 0.3985 0.3461 0.3643 0.0583  0.0348  0.0004  1006 GLU A C   
3633 O O   . GLU A 469 ? 0.3629 0.3027 0.3199 0.0504  0.0320  0.0044  1006 GLU A O   
3634 C CB  . GLU A 469 ? 0.3846 0.3069 0.3369 0.0704  0.0430  -0.0049 1006 GLU A CB  
3635 C CG  . GLU A 469 ? 0.4153 0.3254 0.3611 0.0798  0.0464  -0.0054 1006 GLU A CG  
3636 C CD  . GLU A 469 ? 0.5485 0.4436 0.4867 0.0825  0.0513  -0.0106 1006 GLU A CD  
3637 O OE1 . GLU A 469 ? 0.5339 0.4345 0.4764 0.0800  0.0528  -0.0148 1006 GLU A OE1 
3638 O OE2 . GLU A 469 ? 0.5449 0.4225 0.4729 0.0870  0.0539  -0.0106 1006 GLU A OE2 
3639 N N   . PHE A 470 ? 0.3389 0.3006 0.3166 0.0580  0.0347  -0.0028 1007 PHE A N   
3640 C CA  . PHE A 470 ? 0.3184 0.2855 0.2990 0.0483  0.0309  -0.0013 1007 PHE A CA  
3641 C C   . PHE A 470 ? 0.3380 0.3213 0.3282 0.0457  0.0266  0.0020  1007 PHE A C   
3642 O O   . PHE A 470 ? 0.3336 0.3157 0.3204 0.0368  0.0229  0.0050  1007 PHE A O   
3643 C CB  . PHE A 470 ? 0.3357 0.3127 0.3265 0.0489  0.0318  -0.0052 1007 PHE A CB  
3644 C CG  . PHE A 470 ? 0.3171 0.2963 0.3088 0.0391  0.0278  -0.0034 1007 PHE A CG  
3645 C CD1 . PHE A 470 ? 0.3643 0.3259 0.3407 0.0308  0.0269  -0.0018 1007 PHE A CD1 
3646 C CD2 . PHE A 470 ? 0.3285 0.3275 0.3366 0.0383  0.0247  -0.0033 1007 PHE A CD2 
3647 C CE1 . PHE A 470 ? 0.3707 0.3353 0.3481 0.0218  0.0227  0.0003  1007 PHE A CE1 
3648 C CE2 . PHE A 470 ? 0.3443 0.3455 0.3540 0.0299  0.0206  -0.0012 1007 PHE A CE2 
3649 C CZ  . PHE A 470 ? 0.3964 0.3809 0.3908 0.0217  0.0193  0.0008  1007 PHE A CZ  
3650 N N   . THR A 471 ? 0.3353 0.3345 0.3375 0.0532  0.0273  0.0011  1008 THR A N   
3651 C CA  . THR A 471 ? 0.3527 0.3678 0.3638 0.0513  0.0240  0.0038  1008 THR A CA  
3652 C C   . THR A 471 ? 0.3300 0.3324 0.3272 0.0456  0.0219  0.0087  1008 THR A C   
3653 O O   . THR A 471 ? 0.3344 0.3427 0.3331 0.0378  0.0182  0.0112  1008 THR A O   
3654 C CB  . THR A 471 ? 0.3848 0.4166 0.4081 0.0608  0.0258  0.0019  1008 THR A CB  
3655 O OG1 . THR A 471 ? 0.4034 0.4480 0.4401 0.0650  0.0277  -0.0029 1008 THR A OG1 
3656 C CG2 . THR A 471 ? 0.4109 0.4594 0.4428 0.0582  0.0226  0.0043  1008 THR A CG2 
3657 N N   . ASP A 472 ? 0.3394 0.3241 0.3231 0.0493  0.0244  0.0100  1009 ASP A N   
3658 C CA  . ASP A 472 ? 0.3582 0.3280 0.3271 0.0438  0.0229  0.0146  1009 ASP A CA  
3659 C C   . ASP A 472 ? 0.3534 0.3104 0.3117 0.0327  0.0211  0.0157  1009 ASP A C   
3660 O O   . ASP A 472 ? 0.3643 0.3203 0.3175 0.0245  0.0180  0.0192  1009 ASP A O   
3661 C CB  . ASP A 472 ? 0.3928 0.3438 0.3492 0.0506  0.0262  0.0155  1009 ASP A CB  
3662 C CG  . ASP A 472 ? 0.4842 0.4475 0.4496 0.0610  0.0272  0.0155  1009 ASP A CG  
3663 O OD1 . ASP A 472 ? 0.4331 0.4187 0.4125 0.0615  0.0252  0.0156  1009 ASP A OD1 
3664 O OD2 . ASP A 472 ? 0.5082 0.4592 0.4669 0.0688  0.0301  0.0154  1009 ASP A OD2 
3665 N N   . TYR A 473 ? 0.3711 0.3191 0.3258 0.0321  0.0230  0.0127  1010 TYR A N   
3666 C CA  . TYR A 473 ? 0.3302 0.2672 0.2749 0.0213  0.0212  0.0136  1010 TYR A CA  
3667 C C   . TYR A 473 ? 0.3184 0.2727 0.2734 0.0138  0.0162  0.0152  1010 TYR A C   
3668 O O   . TYR A 473 ? 0.3635 0.3124 0.3102 0.0045  0.0134  0.0181  1010 TYR A O   
3669 C CB  . TYR A 473 ? 0.3765 0.3053 0.3182 0.0219  0.0238  0.0098  1010 TYR A CB  
3670 C CG  . TYR A 473 ? 0.4462 0.3704 0.3820 0.0108  0.0210  0.0106  1010 TYR A CG  
3671 C CD1 . TYR A 473 ? 0.4655 0.3702 0.3834 0.0024  0.0209  0.0125  1010 TYR A CD1 
3672 C CD2 . TYR A 473 ? 0.3668 0.3064 0.3150 0.0085  0.0183  0.0097  1010 TYR A CD2 
3673 C CE1 . TYR A 473 ? 0.5102 0.4119 0.4225 -0.0081 0.0181  0.0133  1010 TYR A CE1 
3674 C CE2 . TYR A 473 ? 0.4274 0.3635 0.3704 -0.0016 0.0152  0.0110  1010 TYR A CE2 
3675 C CZ  . TYR A 473 ? 0.5304 0.4482 0.4554 -0.0099 0.0150  0.0128  1010 TYR A CZ  
3676 O OH  . TYR A 473 ? 0.5154 0.4309 0.4351 -0.0201 0.0117  0.0142  1010 TYR A OH  
3677 N N   . LEU A 474 ? 0.2869 0.2620 0.2599 0.0178  0.0152  0.0131  1011 LEU A N   
3678 C CA  . LEU A 474 ? 0.2699 0.2624 0.2547 0.0118  0.0107  0.0142  1011 LEU A CA  
3679 C C   . LEU A 474 ? 0.3406 0.3390 0.3249 0.0079  0.0082  0.0174  1011 LEU A C   
3680 O O   . LEU A 474 ? 0.3148 0.3167 0.2984 -0.0010 0.0045  0.0194  1011 LEU A O   
3681 C CB  . LEU A 474 ? 0.3059 0.3199 0.3112 0.0179  0.0107  0.0110  1011 LEU A CB  
3682 C CG  . LEU A 474 ? 0.3643 0.3769 0.3733 0.0205  0.0123  0.0079  1011 LEU A CG  
3683 C CD1 . LEU A 474 ? 0.3647 0.3983 0.3937 0.0273  0.0131  0.0047  1011 LEU A CD1 
3684 C CD2 . LEU A 474 ? 0.3412 0.3496 0.3465 0.0113  0.0088  0.0094  1011 LEU A CD2 
3685 N N   . PHE A 475 ? 0.3144 0.3146 0.2989 0.0143  0.0102  0.0179  1012 PHE A N   
3686 C CA  . PHE A 475 ? 0.2855 0.2936 0.2706 0.0104  0.0079  0.0209  1012 PHE A CA  
3687 C C   . PHE A 475 ? 0.3260 0.3149 0.2921 0.0015  0.0069  0.0245  1012 PHE A C   
3688 O O   . PHE A 475 ? 0.3388 0.3338 0.3046 -0.0069 0.0038  0.0266  1012 PHE A O   
3689 C CB  . PHE A 475 ? 0.2836 0.2982 0.2726 0.0189  0.0100  0.0211  1012 PHE A CB  
3690 C CG  . PHE A 475 ? 0.3360 0.3662 0.3310 0.0149  0.0074  0.0232  1012 PHE A CG  
3691 C CD1 . PHE A 475 ? 0.2848 0.3405 0.2993 0.0152  0.0058  0.0207  1012 PHE A CD1 
3692 C CD2 . PHE A 475 ? 0.3141 0.3330 0.2949 0.0099  0.0067  0.0275  1012 PHE A CD2 
3693 C CE1 . PHE A 475 ? 0.3239 0.3947 0.3441 0.0108  0.0036  0.0219  1012 PHE A CE1 
3694 C CE2 . PHE A 475 ? 0.3300 0.3637 0.3157 0.0052  0.0044  0.0292  1012 PHE A CE2 
3695 C CZ  . PHE A 475 ? 0.3426 0.4027 0.3481 0.0056  0.0029  0.0262  1012 PHE A CZ  
3696 N N   . ASN A 476 ? 0.3340 0.2998 0.2843 0.0030  0.0099  0.0249  1013 ASN A N   
3697 C CA  . ASN A 476 ? 0.4001 0.3459 0.3315 -0.0054 0.0096  0.0280  1013 ASN A CA  
3698 C C   . ASN A 476 ? 0.3830 0.3277 0.3112 -0.0163 0.0067  0.0279  1013 ASN A C   
3699 O O   . ASN A 476 ? 0.4063 0.3454 0.3250 -0.0258 0.0047  0.0305  1013 ASN A O   
3700 C CB  . ASN A 476 ? 0.4427 0.3637 0.3587 -0.0005 0.0138  0.0278  1013 ASN A CB  
3701 C CG  . ASN A 476 ? 0.4677 0.3882 0.3841 0.0087  0.0158  0.0294  1013 ASN A CG  
3702 O OD1 . ASN A 476 ? 0.4284 0.3558 0.3454 0.0066  0.0139  0.0326  1013 ASN A OD1 
3703 N ND2 . ASN A 476 ? 0.4326 0.3466 0.3494 0.0190  0.0194  0.0271  1013 ASN A ND2 
3704 N N   . LYS A 477 ? 0.3809 0.3318 0.3174 -0.0151 0.0063  0.0251  1014 LYS A N   
3705 C CA  . LYS A 477 ? 0.3785 0.3310 0.3138 -0.0250 0.0028  0.0255  1014 LYS A CA  
3706 C C   . LYS A 477 ? 0.3531 0.3274 0.3014 -0.0300 -0.0018 0.0267  1014 LYS A C   
3707 O O   . LYS A 477 ? 0.3439 0.3175 0.2867 -0.0402 -0.0050 0.0285  1014 LYS A O   
3708 C CB  . LYS A 477 ? 0.4483 0.4029 0.3898 -0.0222 0.0032  0.0226  1014 LYS A CB  
3709 C CG  . LYS A 477 ? 0.5061 0.4615 0.4457 -0.0320 -0.0007 0.0235  1014 LYS A CG  
3710 C CD  . LYS A 477 ? 0.5002 0.4355 0.4190 -0.0419 -0.0006 0.0252  1014 LYS A CD  
3711 C CE  . LYS A 477 ? 0.5978 0.5119 0.5025 -0.0403 0.0038  0.0232  1014 LYS A CE  
3712 N NZ  . LYS A 477 ? 0.6297 0.5246 0.5143 -0.0510 0.0040  0.0245  1014 LYS A NZ  
3713 N N   . SER A 478 ? 0.3107 0.3046 0.2764 -0.0230 -0.0020 0.0254  1015 SER A N   
3714 C CA  . SER A 478 ? 0.3267 0.3425 0.3062 -0.0267 -0.0057 0.0258  1015 SER A CA  
3715 C C   . SER A 478 ? 0.3317 0.3427 0.3000 -0.0342 -0.0066 0.0288  1015 SER A C   
3716 O O   . SER A 478 ? 0.3238 0.3439 0.2945 -0.0429 -0.0102 0.0297  1015 SER A O   
3717 C CB  . SER A 478 ? 0.3001 0.3356 0.2981 -0.0173 -0.0045 0.0234  1015 SER A CB  
3718 O OG  . SER A 478 ? 0.3070 0.3646 0.3194 -0.0208 -0.0077 0.0230  1015 SER A OG  
3719 N N   . LEU A 479 ? 0.3538 0.3502 0.3098 -0.0309 -0.0034 0.0304  1016 LEU A N   
3720 C CA  . LEU A 479 ? 0.3545 0.3439 0.2981 -0.0380 -0.0039 0.0337  1016 LEU A CA  
3721 C C   . LEU A 479 ? 0.3483 0.3215 0.2757 -0.0493 -0.0051 0.0353  1016 LEU A C   
3722 O O   . LEU A 479 ? 0.4091 0.3838 0.3308 -0.0585 -0.0071 0.0372  1016 LEU A O   
3723 C CB  . LEU A 479 ? 0.3735 0.3481 0.3065 -0.0313 -0.0002 0.0356  1016 LEU A CB  
3724 C CG  . LEU A 479 ? 0.3693 0.3604 0.3157 -0.0218 0.0007  0.0350  1016 LEU A CG  
3725 C CD1 . LEU A 479 ? 0.3897 0.3631 0.3237 -0.0149 0.0040  0.0373  1016 LEU A CD1 
3726 C CD2 . LEU A 479 ? 0.3467 0.3575 0.3014 -0.0275 -0.0020 0.0360  1016 LEU A CD2 
3727 N N   . GLU A 480 ? 0.3888 0.3472 0.3085 -0.0489 -0.0038 0.0341  1017 GLU A N   
3728 C CA  . GLU A 480 ? 0.4146 0.3578 0.3188 -0.0598 -0.0048 0.0351  1017 GLU A CA  
3729 C C   . GLU A 480 ? 0.4072 0.3679 0.3209 -0.0683 -0.0098 0.0349  1017 GLU A C   
3730 O O   . GLU A 480 ? 0.4105 0.3688 0.3154 -0.0792 -0.0119 0.0364  1017 GLU A O   
3731 C CB  . GLU A 480 ? 0.4737 0.3980 0.3681 -0.0571 -0.0018 0.0334  1017 GLU A CB  
3732 C CG  . GLU A 480 ? 0.5746 0.4844 0.4534 -0.0686 -0.0027 0.0339  1017 GLU A CG  
3733 C CD  . GLU A 480 ? 0.7461 0.6382 0.6154 -0.0664 0.0004  0.0317  1017 GLU A CD  
3734 O OE1 . GLU A 480 ? 0.7310 0.6233 0.6070 -0.0558 0.0032  0.0297  1017 GLU A OE1 
3735 O OE2 . GLU A 480 ? 0.8110 0.6896 0.6661 -0.0758 0.0003  0.0317  1017 GLU A OE2 
3736 N N   . ILE A 481 ? 0.3732 0.3519 0.3051 -0.0635 -0.0119 0.0329  1018 ILE A N   
3737 C CA  . ILE A 481 ? 0.3450 0.3396 0.2865 -0.0707 -0.0169 0.0328  1018 ILE A CA  
3738 C C   . ILE A 481 ? 0.3507 0.3671 0.3049 -0.0739 -0.0199 0.0330  1018 ILE A C   
3739 O O   . ILE A 481 ? 0.3683 0.3943 0.3254 -0.0825 -0.0240 0.0335  1018 ILE A O   
3740 C CB  . ILE A 481 ? 0.3526 0.3572 0.3086 -0.0649 -0.0184 0.0310  1018 ILE A CB  
3741 C CG1 . ILE A 481 ? 0.3230 0.3428 0.2969 -0.0535 -0.0168 0.0289  1018 ILE A CG1 
3742 C CG2 . ILE A 481 ? 0.3685 0.3527 0.3111 -0.0642 -0.0159 0.0306  1018 ILE A CG2 
3743 C CD1 . ILE A 481 ? 0.3250 0.3531 0.3126 -0.0477 -0.0176 0.0269  1018 ILE A CD1 
3744 N N   . GLU A 482 ? 0.3150 0.3402 0.2772 -0.0672 -0.0179 0.0324  1019 GLU A N   
3745 C CA  . GLU A 482 ? 0.3062 0.3506 0.2781 -0.0710 -0.0200 0.0324  1019 GLU A CA  
3746 C C   . GLU A 482 ? 0.3470 0.3851 0.3110 -0.0683 -0.0166 0.0338  1019 GLU A C   
3747 O O   . GLU A 482 ? 0.3446 0.3931 0.3196 -0.0597 -0.0150 0.0326  1019 GLU A O   
3748 C CB  . GLU A 482 ? 0.3068 0.3782 0.3042 -0.0656 -0.0222 0.0294  1019 GLU A CB  
3749 C CG  . GLU A 482 ? 0.2690 0.3489 0.2758 -0.0689 -0.0264 0.0286  1019 GLU A CG  
3750 C CD  . GLU A 482 ? 0.3656 0.4727 0.3980 -0.0651 -0.0290 0.0258  1019 GLU A CD  
3751 O OE1 . GLU A 482 ? 0.3319 0.4546 0.3749 -0.0631 -0.0282 0.0241  1019 GLU A OE1 
3752 O OE2 . GLU A 482 ? 0.3026 0.4155 0.3445 -0.0645 -0.0320 0.0253  1019 GLU A OE2 
3753 N N   . PRO A 483 ? 0.3881 0.4087 0.3324 -0.0759 -0.0157 0.0366  1020 PRO A N   
3754 C CA  . PRO A 483 ? 0.3822 0.3937 0.3166 -0.0738 -0.0128 0.0388  1020 PRO A CA  
3755 C C   . PRO A 483 ? 0.4103 0.4450 0.3583 -0.0735 -0.0138 0.0383  1020 PRO A C   
3756 O O   . PRO A 483 ? 0.3777 0.4329 0.3387 -0.0787 -0.0169 0.0363  1020 PRO A O   
3757 C CB  . PRO A 483 ? 0.3967 0.3878 0.3089 -0.0850 -0.0125 0.0417  1020 PRO A CB  
3758 C CG  . PRO A 483 ? 0.3806 0.3623 0.2876 -0.0892 -0.0136 0.0406  1020 PRO A CG  
3759 C CD  . PRO A 483 ? 0.4499 0.4564 0.3790 -0.0868 -0.0171 0.0378  1020 PRO A CD  
3760 N N   . ARG A 484 ? 0.4211 0.4531 0.3665 -0.0673 -0.0113 0.0398  1021 ARG A N   
3761 C CA  . ARG A 484 ? 0.3862 0.4389 0.3419 -0.0679 -0.0119 0.0396  1021 ARG A CA  
3762 C C   . ARG A 484 ? 0.5032 0.5599 0.4522 -0.0813 -0.0140 0.0408  1021 ARG A C   
3763 O O   . ARG A 484 ? 0.4836 0.5197 0.4131 -0.0888 -0.0136 0.0437  1021 ARG A O   
3764 C CB  . ARG A 484 ? 0.4516 0.4964 0.4007 -0.0604 -0.0090 0.0422  1021 ARG A CB  
3765 C CG  . ARG A 484 ? 0.4895 0.5380 0.4495 -0.0467 -0.0070 0.0402  1021 ARG A CG  
3766 C CD  . ARG A 484 ? 0.5323 0.5796 0.4890 -0.0399 -0.0050 0.0427  1021 ARG A CD  
3767 N NE  . ARG A 484 ? 0.5420 0.6084 0.5045 -0.0454 -0.0063 0.0432  1021 ARG A NE  
3768 C CZ  . ARG A 484 ? 0.6450 0.7028 0.5929 -0.0516 -0.0064 0.0476  1021 ARG A CZ  
3769 N NH1 . ARG A 484 ? 0.7920 0.8216 0.7189 -0.0526 -0.0051 0.0520  1021 ARG A NH1 
3770 N NH2 . ARG A 484 ? 0.5428 0.6203 0.4972 -0.0570 -0.0075 0.0473  1021 ARG A NH2 
3771 N N   . ASN A 485 ? 0.5333 0.6166 0.4989 -0.0845 -0.0160 0.0381  1022 ASN A N   
3772 C CA  . ASN A 485 ? 0.6207 0.7125 0.5828 -0.0973 -0.0179 0.0384  1022 ASN A CA  
3773 C C   . ASN A 485 ? 0.5954 0.6781 0.5487 -0.1071 -0.0201 0.0385  1022 ASN A C   
3774 O O   . ASN A 485 ? 0.7115 0.7873 0.6509 -0.1182 -0.0205 0.0404  1022 ASN A O   
3775 C CB  . ASN A 485 ? 0.6051 0.6849 0.5499 -0.1014 -0.0160 0.0426  1022 ASN A CB  
3776 C CG  . ASN A 485 ? 0.6529 0.7430 0.6055 -0.0928 -0.0142 0.0428  1022 ASN A CG  
3777 O OD1 . ASN A 485 ? 0.5938 0.6669 0.5325 -0.0891 -0.0122 0.0470  1022 ASN A OD1 
3778 N ND2 . ASN A 485 ? 0.5955 0.7136 0.5704 -0.0895 -0.0151 0.0384  1022 ASN A ND2 
3779 N N   . CYS A 486 ? 0.5651 0.6473 0.5253 -0.1035 -0.0215 0.0367  1023 CYS A N   
3780 C CA  . CYS A 486 ? 0.5433 0.6208 0.4974 -0.1130 -0.0241 0.0367  1023 CYS A CA  
3781 C C   . CYS A 486 ? 0.5807 0.6870 0.5558 -0.1164 -0.0280 0.0331  1023 CYS A C   
3782 O O   . CYS A 486 ? 0.4959 0.6189 0.4911 -0.1080 -0.0288 0.0303  1023 CYS A O   
3783 C CB  . CYS A 486 ? 0.6725 0.7320 0.6203 -0.1085 -0.0237 0.0372  1023 CYS A CB  
3784 S SG  . CYS A 486 ? 1.1648 1.1958 1.0853 -0.1199 -0.0232 0.0400  1023 CYS A SG  
3785 N N   . LYS A 487 ? 0.5266 0.6393 0.4978 -0.1285 -0.0303 0.0329  1024 LYS A N   
3786 C CA  . LYS A 487 ? 0.6745 0.8156 0.6663 -0.1319 -0.0340 0.0292  1024 LYS A CA  
3787 C C   . LYS A 487 ? 0.6287 0.7718 0.6279 -0.1310 -0.0376 0.0284  1024 LYS A C   
3788 O O   . LYS A 487 ? 0.7194 0.8848 0.7400 -0.1283 -0.0406 0.0254  1024 LYS A O   
3789 C CB  . LYS A 487 ? 0.8987 1.0478 0.8844 -0.1454 -0.0351 0.0289  1024 LYS A CB  
3790 C CG  . LYS A 487 ? 1.0780 1.2307 1.0602 -0.1463 -0.0320 0.0294  1024 LYS A CG  
3791 C CD  . LYS A 487 ? 1.2035 1.3678 1.1822 -0.1600 -0.0330 0.0284  1024 LYS A CD  
3792 C CE  . LYS A 487 ? 1.2665 1.4375 1.2441 -0.1605 -0.0303 0.0286  1024 LYS A CE  
3793 N NZ  . LYS A 487 ? 1.2816 1.4636 1.2545 -0.1746 -0.0308 0.0276  1024 LYS A NZ  
3794 N N   . GLN A 488 ? 0.5487 0.6682 0.5301 -0.1333 -0.0372 0.0312  1025 GLN A N   
3795 C CA  . GLN A 488 ? 0.7827 0.9014 0.7689 -0.1318 -0.0404 0.0310  1025 GLN A CA  
3796 C C   . GLN A 488 ? 0.8307 0.9232 0.8025 -0.1261 -0.0375 0.0332  1025 GLN A C   
3797 O O   . GLN A 488 ? 0.8772 0.9469 0.8277 -0.1296 -0.0344 0.0354  1025 GLN A O   
3798 C CB  . GLN A 488 ? 0.8563 0.9783 0.8368 -0.1446 -0.0442 0.0313  1025 GLN A CB  
3799 C CG  . GLN A 488 ? 1.0066 1.1589 1.0075 -0.1484 -0.0483 0.0283  1025 GLN A CG  
3800 C CD  . GLN A 488 ? 1.1979 1.3544 1.1925 -0.1616 -0.0520 0.0285  1025 GLN A CD  
3801 O OE1 . GLN A 488 ? 1.2404 1.3767 1.2132 -0.1695 -0.0510 0.0309  1025 GLN A OE1 
3802 N NE2 . GLN A 488 ? 1.2586 1.4419 1.2727 -0.1641 -0.0563 0.0258  1025 GLN A NE2 
3803 N N   . PRO A 489 ? 0.7620 0.8577 0.7455 -0.1173 -0.0386 0.0324  1026 PRO A N   
3804 C CA  . PRO A 489 ? 0.7930 0.8663 0.7649 -0.1116 -0.0359 0.0337  1026 PRO A CA  
3805 C C   . PRO A 489 ? 0.8247 0.8783 0.7756 -0.1214 -0.0364 0.0357  1026 PRO A C   
3806 O O   . PRO A 489 ? 0.7695 0.8317 0.7231 -0.1289 -0.0408 0.0358  1026 PRO A O   
3807 C CB  . PRO A 489 ? 0.8300 0.9160 0.8209 -0.1035 -0.0384 0.0322  1026 PRO A CB  
3808 C CG  . PRO A 489 ? 0.7985 0.9088 0.8059 -0.1087 -0.0437 0.0311  1026 PRO A CG  
3809 C CD  . PRO A 489 ? 0.7091 0.8294 0.7169 -0.1139 -0.0428 0.0301  1026 PRO A CD  
3810 N N   . PRO A 490 ? 0.8205 0.8484 0.7511 -0.1214 -0.0320 0.0371  1027 PRO A N   
3811 C CA  . PRO A 490 ? 0.8496 0.8579 0.7594 -0.1313 -0.0318 0.0384  1027 PRO A CA  
3812 C C   . PRO A 490 ? 0.6837 0.6913 0.5955 -0.1315 -0.0345 0.0382  1027 PRO A C   
3813 O O   . PRO A 490 ? 0.6883 0.7035 0.6140 -0.1221 -0.0352 0.0374  1027 PRO A O   
3814 C CB  . PRO A 490 ? 0.9059 0.8873 0.7971 -0.1278 -0.0259 0.0394  1027 PRO A CB  
3815 C CG  . PRO A 490 ? 0.8782 0.8677 0.7791 -0.1189 -0.0238 0.0393  1027 PRO A CG  
3816 C CD  . PRO A 490 ? 0.8101 0.8259 0.7361 -0.1121 -0.0270 0.0373  1027 PRO A CD  
3817 N N   . ARG A 491 ? 0.6562 0.6549 0.5539 -0.1427 -0.0361 0.0391  1028 ARG A N   
3818 C CA  . ARG A 491 ? 0.6545 0.6522 0.5517 -0.1450 -0.0391 0.0394  1028 ARG A CA  
3819 C C   . ARG A 491 ? 0.5411 0.5148 0.4244 -0.1406 -0.0346 0.0391  1028 ARG A C   
3820 O O   . ARG A 491 ? 0.6156 0.5672 0.4797 -0.1439 -0.0301 0.0391  1028 ARG A O   
3821 C CB  . ARG A 491 ? 0.7208 0.7195 0.6078 -0.1595 -0.0426 0.0402  1028 ARG A CB  
3822 C CG  . ARG A 491 ? 0.9228 0.9462 0.8271 -0.1621 -0.0497 0.0406  1028 ARG A CG  
3823 C CD  . ARG A 491 ? 0.9874 1.0357 0.9138 -0.1571 -0.0518 0.0395  1028 ARG A CD  
3824 N NE  . ARG A 491 ? 1.0420 1.1102 0.9924 -0.1479 -0.0555 0.0392  1028 ARG A NE  
3825 C CZ  . ARG A 491 ? 0.9865 1.0526 0.9420 -0.1419 -0.0570 0.0400  1028 ARG A CZ  
3826 N NH1 . ARG A 491 ? 1.0481 1.0936 0.9870 -0.1436 -0.0552 0.0411  1028 ARG A NH1 
3827 N NH2 . ARG A 491 ? 0.8378 0.9231 0.8161 -0.1340 -0.0602 0.0395  1028 ARG A NH2 
3828 N N   . PHE A 492 ? 0.4551 0.4331 0.3485 -0.1331 -0.0357 0.0388  1029 PHE A N   
3829 C CA  . PHE A 492 ? 0.4204 0.3783 0.3018 -0.1301 -0.0321 0.0381  1029 PHE A CA  
3830 C C   . PHE A 492 ? 0.4654 0.4286 0.3485 -0.1349 -0.0367 0.0391  1029 PHE A C   
3831 O O   . PHE A 492 ? 0.5085 0.4929 0.4090 -0.1339 -0.0422 0.0401  1029 PHE A O   
3832 C CB  . PHE A 492 ? 0.4449 0.4020 0.3360 -0.1160 -0.0284 0.0367  1029 PHE A CB  
3833 C CG  . PHE A 492 ? 0.4599 0.4103 0.3480 -0.1106 -0.0238 0.0361  1029 PHE A CG  
3834 C CD1 . PHE A 492 ? 0.4045 0.3732 0.3077 -0.1068 -0.0252 0.0363  1029 PHE A CD1 
3835 C CD2 . PHE A 492 ? 0.6173 0.5431 0.4876 -0.1093 -0.0182 0.0354  1029 PHE A CD2 
3836 C CE1 . PHE A 492 ? 0.5206 0.4832 0.4204 -0.1020 -0.0213 0.0363  1029 PHE A CE1 
3837 C CE2 . PHE A 492 ? 0.6258 0.5449 0.4932 -0.1039 -0.0144 0.0356  1029 PHE A CE2 
3838 C CZ  . PHE A 492 ? 0.5289 0.4665 0.4107 -0.1005 -0.0161 0.0362  1029 PHE A CZ  
3839 N N   . PRO A 493 ? 0.5489 0.4931 0.4141 -0.1401 -0.0346 0.0387  1030 PRO A N   
3840 C CA  . PRO A 493 ? 0.5152 0.4628 0.3793 -0.1458 -0.0390 0.0400  1030 PRO A CA  
3841 C C   . PRO A 493 ? 0.6312 0.5889 0.5112 -0.1363 -0.0408 0.0404  1030 PRO A C   
3842 O O   . PRO A 493 ? 0.4887 0.4428 0.3743 -0.1257 -0.0367 0.0387  1030 PRO A O   
3843 C CB  . PRO A 493 ? 0.6461 0.5683 0.4860 -0.1525 -0.0344 0.0386  1030 PRO A CB  
3844 C CG  . PRO A 493 ? 0.6469 0.5522 0.4795 -0.1454 -0.0272 0.0364  1030 PRO A CG  
3845 C CD  . PRO A 493 ? 0.5946 0.5127 0.4389 -0.1418 -0.0280 0.0371  1030 PRO A CD  
3846 N N   . ARG A 494 ? 0.6887 0.6595 0.5762 -0.1403 -0.0472 0.0427  1031 ARG A N   
3847 C CA  . ARG A 494 ? 0.6847 0.6642 0.5863 -0.1325 -0.0495 0.0436  1031 ARG A CA  
3848 C C   . ARG A 494 ? 0.7802 0.7399 0.6677 -0.1311 -0.0447 0.0422  1031 ARG A C   
3849 O O   . ARG A 494 ? 0.7153 0.6587 0.5828 -0.1397 -0.0425 0.0416  1031 ARG A O   
3850 C CB  . ARG A 494 ? 0.8175 0.8143 0.7288 -0.1380 -0.0579 0.0471  1031 ARG A CB  
3851 C CG  . ARG A 494 ? 0.8327 0.8414 0.7619 -0.1298 -0.0613 0.0487  1031 ARG A CG  
3852 C CD  . ARG A 494 ? 0.7565 0.7873 0.7107 -0.1220 -0.0643 0.0486  1031 ARG A CD  
3853 N NE  . ARG A 494 ? 0.7608 0.8069 0.7209 -0.1288 -0.0693 0.0497  1031 ARG A NE  
3854 C CZ  . ARG A 494 ? 0.7907 0.8531 0.7617 -0.1323 -0.0770 0.0526  1031 ARG A CZ  
3855 N NH1 . ARG A 494 ? 0.5445 0.6096 0.5216 -0.1299 -0.0810 0.0555  1031 ARG A NH1 
3856 N NH2 . ARG A 494 ? 0.7967 0.8731 0.7727 -0.1384 -0.0808 0.0528  1031 ARG A NH2 
3857 N N   . LYS A 495 ? 0.7084 0.6697 0.6061 -0.1207 -0.0426 0.0411  1032 LYS A N   
3858 C CA  . LYS A 495 ? 0.8319 0.7757 0.7176 -0.1185 -0.0375 0.0391  1032 LYS A CA  
3859 C C   . LYS A 495 ? 0.7698 0.7161 0.6554 -0.1221 -0.0416 0.0414  1032 LYS A C   
3860 O O   . LYS A 495 ? 0.7856 0.7175 0.6542 -0.1286 -0.0397 0.0408  1032 LYS A O   
3861 C CB  . LYS A 495 ? 0.9852 0.9284 0.8806 -0.1054 -0.0322 0.0361  1032 LYS A CB  
3862 C CG  . LYS A 495 ? 1.0774 1.0003 0.9583 -0.1030 -0.0251 0.0327  1032 LYS A CG  
3863 C CD  . LYS A 495 ? 1.1805 1.0846 1.0401 -0.1108 -0.0216 0.0314  1032 LYS A CD  
3864 C CE  . LYS A 495 ? 1.2754 1.1589 1.1207 -0.1085 -0.0143 0.0274  1032 LYS A CE  
3865 N NZ  . LYS A 495 ? 1.2978 1.1794 1.1505 -0.0958 -0.0090 0.0246  1032 LYS A NZ  
3866 N N   . SER A 496 ? 0.6281 0.5927 0.5327 -0.1180 -0.0472 0.0441  1033 SER A N   
3867 C CA  . SER A 496 ? 0.7810 0.7490 0.6873 -0.1205 -0.0517 0.0471  1033 SER A CA  
3868 C C   . SER A 496 ? 0.7375 0.7162 0.6442 -0.1302 -0.0598 0.0515  1033 SER A C   
3869 O O   . SER A 496 ? 0.6135 0.6012 0.5243 -0.1333 -0.0622 0.0518  1033 SER A O   
3870 C CB  . SER A 496 ? 0.8787 0.8590 0.8057 -0.1097 -0.0528 0.0475  1033 SER A CB  
3871 O OG  . SER A 496 ? 0.8813 0.8801 0.8278 -0.1053 -0.0565 0.0483  1033 SER A OG  
3872 N N   . THR A 497 ? 0.7190 0.6978 0.6218 -0.1352 -0.0642 0.0548  1034 THR A N   
3873 C CA  . THR A 497 ? 0.7979 0.7879 0.7016 -0.1442 -0.0725 0.0594  1034 THR A CA  
3874 C C   . THR A 497 ? 0.7768 0.7850 0.7016 -0.1390 -0.0799 0.0637  1034 THR A C   
3875 O O   . THR A 497 ? 0.8035 0.8244 0.7335 -0.1445 -0.0877 0.0678  1034 THR A O   
3876 C CB  . THR A 497 ? 0.8892 0.8666 0.7710 -0.1561 -0.0733 0.0608  1034 THR A CB  
3877 O OG1 . THR A 497 ? 0.8845 0.8540 0.7630 -0.1532 -0.0716 0.0612  1034 THR A OG1 
3878 C CG2 . THR A 497 ? 0.8558 0.8158 0.7168 -0.1626 -0.0666 0.0566  1034 THR A CG2 
3879 N N   . PHE A 498 ? 0.6321 0.6416 0.5694 -0.1284 -0.0776 0.0628  1035 PHE A N   
3880 C CA  . PHE A 498 ? 0.6001 0.6249 0.5570 -0.1234 -0.0843 0.0669  1035 PHE A CA  
3881 C C   . PHE A 498 ? 0.5992 0.6435 0.5774 -0.1185 -0.0879 0.0667  1035 PHE A C   
3882 O O   . PHE A 498 ? 0.6090 0.6545 0.5880 -0.1171 -0.0839 0.0629  1035 PHE A O   
3883 C CB  . PHE A 498 ? 0.5882 0.6080 0.5513 -0.1143 -0.0806 0.0658  1035 PHE A CB  
3884 C CG  . PHE A 498 ? 0.8367 0.8509 0.8022 -0.1057 -0.0719 0.0598  1035 PHE A CG  
3885 C CD1 . PHE A 498 ? 0.9151 0.9423 0.8989 -0.0978 -0.0712 0.0575  1035 PHE A CD1 
3886 C CD2 . PHE A 498 ? 0.8942 0.8908 0.8441 -0.1054 -0.0645 0.0563  1035 PHE A CD2 
3887 C CE1 . PHE A 498 ? 0.7831 0.8060 0.7690 -0.0900 -0.0636 0.0524  1035 PHE A CE1 
3888 C CE2 . PHE A 498 ? 0.8698 0.8620 0.8224 -0.0970 -0.0570 0.0511  1035 PHE A CE2 
3889 C CZ  . PHE A 498 ? 0.7853 0.7908 0.7558 -0.0894 -0.0567 0.0494  1035 PHE A CZ  
3890 N N   . SER A 499 ? 0.4831 0.5427 0.4783 -0.1164 -0.0956 0.0710  1036 SER A N   
3891 C CA  . SER A 499 ? 0.4460 0.5256 0.4643 -0.1108 -0.0991 0.0705  1036 SER A CA  
3892 C C   . SER A 499 ? 0.4657 0.5467 0.4956 -0.1002 -0.0922 0.0652  1036 SER A C   
3893 O O   . SER A 499 ? 0.5124 0.5831 0.5399 -0.0946 -0.0871 0.0635  1036 SER A O   
3894 C CB  . SER A 499 ? 0.4176 0.5106 0.4532 -0.1080 -0.1075 0.0757  1036 SER A CB  
3895 O OG  . SER A 499 ? 0.4223 0.5352 0.4813 -0.1024 -0.1107 0.0746  1036 SER A OG  
3896 N N   . LEU A 500 ? 0.3947 0.4886 0.4364 -0.0981 -0.0919 0.0625  1037 LEU A N   
3897 C CA  . LEU A 500 ? 0.4619 0.5606 0.5169 -0.0882 -0.0864 0.0577  1037 LEU A CA  
3898 C C   . LEU A 500 ? 0.3966 0.5123 0.4776 -0.0802 -0.0904 0.0584  1037 LEU A C   
3899 O O   . LEU A 500 ? 0.4223 0.5439 0.5171 -0.0715 -0.0864 0.0546  1037 LEU A O   
3900 C CB  . LEU A 500 ? 0.4004 0.5045 0.4548 -0.0903 -0.0837 0.0542  1037 LEU A CB  
3901 C CG  . LEU A 500 ? 0.4209 0.5081 0.4507 -0.0978 -0.0791 0.0530  1037 LEU A CG  
3902 C CD1 . LEU A 500 ? 0.3564 0.4510 0.3889 -0.0989 -0.0769 0.0500  1037 LEU A CD1 
3903 C CD2 . LEU A 500 ? 0.5556 0.6237 0.5728 -0.0935 -0.0718 0.0509  1037 LEU A CD2 
3904 N N   . LYS A 501 ? 0.3758 0.4996 0.4633 -0.0832 -0.0986 0.0633  1038 LYS A N   
3905 C CA  . LYS A 501 ? 0.3143 0.4548 0.4272 -0.0761 -0.1034 0.0644  1038 LYS A CA  
3906 C C   . LYS A 501 ? 0.2923 0.4259 0.4110 -0.0680 -0.1004 0.0642  1038 LYS A C   
3907 O O   . LYS A 501 ? 0.3401 0.4587 0.4443 -0.0704 -0.0997 0.0669  1038 LYS A O   
3908 C CB  . LYS A 501 ? 0.3257 0.4750 0.4429 -0.0813 -0.1133 0.0704  1038 LYS A CB  
3909 C CG  . LYS A 501 ? 0.6049 0.7724 0.7321 -0.0850 -0.1177 0.0696  1038 LYS A CG  
3910 C CD  . LYS A 501 ? 0.7569 0.9312 0.8831 -0.0920 -0.1273 0.0757  1038 LYS A CD  
3911 C CE  . LYS A 501 ? 0.8074 0.9830 0.9450 -0.0867 -0.1330 0.0809  1038 LYS A CE  
3912 N NZ  . LYS A 501 ? 0.7787 0.9678 0.9438 -0.0755 -0.1330 0.0783  1038 LYS A NZ  
3913 N N   . SER A 502 ? 0.3001 0.4450 0.4397 -0.0589 -0.0983 0.0605  1039 SER A N   
3914 C CA  . SER A 502 ? 0.2587 0.3987 0.4059 -0.0511 -0.0953 0.0598  1039 SER A CA  
3915 C C   . SER A 502 ? 0.2976 0.4420 0.4561 -0.0499 -0.1029 0.0655  1039 SER A C   
3916 O O   . SER A 502 ? 0.3458 0.5040 0.5167 -0.0511 -0.1100 0.0680  1039 SER A O   
3917 C CB  . SER A 502 ? 0.2822 0.4330 0.4476 -0.0423 -0.0901 0.0536  1039 SER A CB  
3918 O OG  . SER A 502 ? 0.3326 0.4812 0.5082 -0.0350 -0.0882 0.0530  1039 SER A OG  
3919 N N   . PRO A 503 ? 0.3367 0.4694 0.4911 -0.0474 -0.1016 0.0675  1040 PRO A N   
3920 C CA  . PRO A 503 ? 0.3350 0.4710 0.5016 -0.0450 -0.1084 0.0729  1040 PRO A CA  
3921 C C   . PRO A 503 ? 0.3746 0.5249 0.5689 -0.0352 -0.1081 0.0696  1040 PRO A C   
3922 O O   . PRO A 503 ? 0.4232 0.5782 0.6314 -0.0320 -0.1138 0.0736  1040 PRO A O   
3923 C CB  . PRO A 503 ? 0.3364 0.4542 0.4878 -0.0460 -0.1054 0.0750  1040 PRO A CB  
3924 C CG  . PRO A 503 ? 0.2900 0.3998 0.4323 -0.0437 -0.0952 0.0681  1040 PRO A CG  
3925 C CD  . PRO A 503 ? 0.3488 0.4641 0.4860 -0.0474 -0.0939 0.0651  1040 PRO A CD  
3926 N N   . GLY A 504 ? 0.3344 0.4915 0.5363 -0.0306 -0.1014 0.0624  1041 GLY A N   
3927 C CA  . GLY A 504 ? 0.3510 0.5222 0.5786 -0.0219 -0.1001 0.0581  1041 GLY A CA  
3928 C C   . GLY A 504 ? 0.3812 0.5447 0.6132 -0.0154 -0.0950 0.0561  1041 GLY A C   
3929 O O   . GLY A 504 ? 0.3830 0.5303 0.5979 -0.0177 -0.0923 0.0579  1041 GLY A O   
3930 N N   . ILE A 505 ? 0.3117 0.4871 0.5667 -0.0077 -0.0933 0.0518  1042 ILE A N   
3931 C CA  . ILE A 505 ? 0.2459 0.4151 0.5056 -0.0017 -0.0874 0.0488  1042 ILE A CA  
3932 C C   . ILE A 505 ? 0.2873 0.4567 0.5612 0.0029  -0.0909 0.0513  1042 ILE A C   
3933 O O   . ILE A 505 ? 0.3062 0.4725 0.5863 0.0085  -0.0853 0.0473  1042 ILE A O   
3934 C CB  . ILE A 505 ? 0.2937 0.4704 0.5601 0.0038  -0.0783 0.0393  1042 ILE A CB  
3935 C CG1 . ILE A 505 ? 0.3895 0.5762 0.6606 0.0071  -0.0757 0.0331  1042 ILE A CG1 
3936 C CG2 . ILE A 505 ? 0.3936 0.5672 0.6447 -0.0001 -0.0742 0.0372  1042 ILE A CG2 
3937 C CD1 . ILE A 505 ? 0.4724 0.6635 0.7436 0.0123  -0.0658 0.0236  1042 ILE A CD1 
3938 N N   . ARG A 506 ? 0.3878 0.5587 0.6627 0.0004  -0.0989 0.0572  1043 ARG A N   
3939 C CA  . ARG A 506 ? 0.4647 0.6321 0.7487 0.0041  -0.1025 0.0607  1043 ARG A CA  
3940 C C   . ARG A 506 ? 0.3793 0.5345 0.6557 -0.0003 -0.1088 0.0703  1043 ARG A C   
3941 O O   . ARG A 506 ? 0.4563 0.6047 0.7139 -0.0078 -0.1126 0.0755  1043 ARG A O   
3942 C CB  . ARG A 506 ? 0.5337 0.7087 0.8222 0.0043  -0.1074 0.0618  1043 ARG A CB  
3943 C CG  . ARG A 506 ? 0.7752 0.9473 1.0748 0.0091  -0.1106 0.0648  1043 ARG A CG  
3944 C CD  . ARG A 506 ? 0.8377 1.0180 1.1423 0.0094  -0.1161 0.0664  1043 ARG A CD  
3945 N NE  . ARG A 506 ? 0.8685 1.0454 1.1845 0.0145  -0.1191 0.0693  1043 ARG A NE  
3946 C CZ  . ARG A 506 ? 0.8284 1.0112 1.1515 0.0162  -0.1242 0.0713  1043 ARG A CZ  
3947 N NH1 . ARG A 506 ? 0.6817 0.8749 1.0017 0.0131  -0.1268 0.0704  1043 ARG A NH1 
3948 N NH2 . ARG A 506 ? 0.7598 0.9383 1.0936 0.0210  -0.1267 0.0741  1043 ARG A NH2 
3949 N N   . PRO A 507 ? 0.4332 0.5797 0.7135 0.0037  -0.1059 0.0704  1044 PRO A N   
3950 C CA  . PRO A 507 ? 0.5169 0.6454 0.7790 -0.0009 -0.1076 0.0770  1044 PRO A CA  
3951 C C   . PRO A 507 ? 0.6322 0.7598 0.8952 -0.0039 -0.1187 0.0870  1044 PRO A C   
3952 O O   . PRO A 507 ? 0.5806 0.7216 0.8631 -0.0002 -0.1248 0.0882  1044 PRO A O   
3953 C CB  . PRO A 507 ? 0.5006 0.6235 0.7719 0.0050  -0.1019 0.0737  1044 PRO A CB  
3954 C CG  . PRO A 507 ? 0.5521 0.6885 0.8407 0.0116  -0.0952 0.0641  1044 PRO A CG  
3955 C CD  . PRO A 507 ? 0.4791 0.6295 0.7752 0.0118  -0.0988 0.0628  1044 PRO A CD  
3956 N N   . ASN A 508 ? 0.7687 0.8813 1.0113 -0.0105 -0.1215 0.0938  1045 ASN A N   
3957 C CA  . ASN A 508 ? 0.8692 0.9807 1.1106 -0.0141 -0.1325 0.1040  1045 ASN A CA  
3958 C C   . ASN A 508 ? 0.8285 0.9303 1.0755 -0.0113 -0.1355 0.1098  1045 ASN A C   
3959 O O   . ASN A 508 ? 0.8156 0.9183 1.0785 -0.0040 -0.1310 0.1055  1045 ASN A O   
3960 C CB  . ASN A 508 ? 0.9408 1.0433 1.1549 -0.0247 -0.1349 0.1087  1045 ASN A CB  
3961 C CG  . ASN A 508 ? 1.0262 1.1097 1.2192 -0.0297 -0.1314 0.1113  1045 ASN A CG  
3962 O OD1 . ASN A 508 ? 1.0414 1.1182 1.2350 -0.0261 -0.1234 0.1062  1045 ASN A OD1 
3963 N ND2 . ASN A 508 ? 1.0574 1.1328 1.2314 -0.0385 -0.1372 0.1189  1045 ASN A ND2 
# 
