data_9BVF
# 
_entry.id   9BVF 
# 
_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   9BVF         pdb_00009bvf 10.2210/pdb9bvf/pdb 
WWPDB D_1000283496 ?            ?                   
# 
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                        9BVF 
_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-[(3S)-3-methyl-1,4-diazepan-1-yl]quinazolin-2-yl}amino)phenol' 349.430   1   ? ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                  78.133    1   ? ? ? ? 
4 non-polymer syn 'SULFATE ION'                                                         96.063    1   ? ? ? ? 
5 water       nat water                                                                 18.015    404 ? ? ? ? 
# 
_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-[(3S)-3-methyl-1,4-diazepan-1-yl]quinazolin-2-yl}amino)phenol' A1ASX 
3 'DIMETHYL SULFOXIDE'                                                  DMS   
4 'SULFATE ION'                                                         SO4   
5 water                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
A1ASX non-polymer         . '4-({4-[(3S)-3-methyl-1,4-diazepan-1-yl]quinazolin-2-yl}amino)phenol' ? 'C20 H23 N5 O'   349.430 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                  ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                             ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                       ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                               ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                             ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                 ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                            ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                               ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                            ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                         ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                               ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                                         ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                             ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                            ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                              ? 'C9 H11 N O3'    181.189 
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  -27  SER SER A . n 
A 1 3   TYR 3   -26  -26  TYR TYR A . n 
A 1 4   TYR 4   -25  -25  TYR TYR A . n 
A 1 5   HIS 5   -24  -24  HIS HIS A . n 
A 1 6   HIS 6   -23  -23  HIS HIS 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  593  ASN ASN A . n 
A 1 57  LEU 57  594  594  LEU LEU A . n 
A 1 58  GLN 58  595  595  GLN GLN 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  ?    ?   ?   A . n 
A 1 127 ALA 127 664  ?    ?   ?   A . n 
A 1 128 ILE 128 665  ?    ?   ?   A . n 
A 1 129 GLU 129 666  ?    ?   ?   A . n 
A 1 130 LYS 130 667  ?    ?   ?   A . n 
A 1 131 GLY 131 668  ?    ?   ?   A . n 
A 1 132 GLU 132 669  ?    ?   ?   A . n 
A 1 133 GLN 133 670  ?    ?   ?   A . n 
A 1 134 PRO 134 671  ?    ?   ?   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        A1ASX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ASX 
_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 A1ASX 1   1101 1101 A1ASX LIG A . 
C 3 DMS   1   1102 1201 DMS   DMS A . 
D 4 SO4   1   1103 1301 SO4   SO4 A . 
E 5 HOH   1   1201 397  HOH   HOH A . 
E 5 HOH   2   1202 256  HOH   HOH A . 
E 5 HOH   3   1203 258  HOH   HOH A . 
E 5 HOH   4   1204 230  HOH   HOH A . 
E 5 HOH   5   1205 299  HOH   HOH A . 
E 5 HOH   6   1206 199  HOH   HOH A . 
E 5 HOH   7   1207 383  HOH   HOH A . 
E 5 HOH   8   1208 369  HOH   HOH A . 
E 5 HOH   9   1209 280  HOH   HOH A . 
E 5 HOH   10  1210 55   HOH   HOH A . 
E 5 HOH   11  1211 216  HOH   HOH A . 
E 5 HOH   12  1212 100  HOH   HOH A . 
E 5 HOH   13  1213 228  HOH   HOH A . 
E 5 HOH   14  1214 353  HOH   HOH A . 
E 5 HOH   15  1215 370  HOH   HOH A . 
E 5 HOH   16  1216 44   HOH   HOH A . 
E 5 HOH   17  1217 12   HOH   HOH A . 
E 5 HOH   18  1218 218  HOH   HOH A . 
E 5 HOH   19  1219 13   HOH   HOH A . 
E 5 HOH   20  1220 252  HOH   HOH A . 
E 5 HOH   21  1221 393  HOH   HOH A . 
E 5 HOH   22  1222 332  HOH   HOH A . 
E 5 HOH   23  1223 226  HOH   HOH A . 
E 5 HOH   24  1224 196  HOH   HOH A . 
E 5 HOH   25  1225 238  HOH   HOH A . 
E 5 HOH   26  1226 48   HOH   HOH A . 
E 5 HOH   27  1227 74   HOH   HOH A . 
E 5 HOH   28  1228 25   HOH   HOH A . 
E 5 HOH   29  1229 235  HOH   HOH A . 
E 5 HOH   30  1230 82   HOH   HOH A . 
E 5 HOH   31  1231 143  HOH   HOH A . 
E 5 HOH   32  1232 86   HOH   HOH A . 
E 5 HOH   33  1233 18   HOH   HOH A . 
E 5 HOH   34  1234 219  HOH   HOH A . 
E 5 HOH   35  1235 297  HOH   HOH A . 
E 5 HOH   36  1236 141  HOH   HOH A . 
E 5 HOH   37  1237 3    HOH   HOH A . 
E 5 HOH   38  1238 371  HOH   HOH A . 
E 5 HOH   39  1239 115  HOH   HOH A . 
E 5 HOH   40  1240 361  HOH   HOH A . 
E 5 HOH   41  1241 85   HOH   HOH A . 
E 5 HOH   42  1242 355  HOH   HOH A . 
E 5 HOH   43  1243 99   HOH   HOH A . 
E 5 HOH   44  1244 117  HOH   HOH A . 
E 5 HOH   45  1245 271  HOH   HOH A . 
E 5 HOH   46  1246 185  HOH   HOH A . 
E 5 HOH   47  1247 40   HOH   HOH A . 
E 5 HOH   48  1248 254  HOH   HOH A . 
E 5 HOH   49  1249 21   HOH   HOH A . 
E 5 HOH   50  1250 155  HOH   HOH A . 
E 5 HOH   51  1251 293  HOH   HOH A . 
E 5 HOH   52  1252 58   HOH   HOH A . 
E 5 HOH   53  1253 109  HOH   HOH A . 
E 5 HOH   54  1254 184  HOH   HOH A . 
E 5 HOH   55  1255 38   HOH   HOH A . 
E 5 HOH   56  1256 87   HOH   HOH A . 
E 5 HOH   57  1257 243  HOH   HOH A . 
E 5 HOH   58  1258 198  HOH   HOH A . 
E 5 HOH   59  1259 27   HOH   HOH A . 
E 5 HOH   60  1260 177  HOH   HOH A . 
E 5 HOH   61  1261 204  HOH   HOH A . 
E 5 HOH   62  1262 277  HOH   HOH A . 
E 5 HOH   63  1263 91   HOH   HOH A . 
E 5 HOH   64  1264 153  HOH   HOH A . 
E 5 HOH   65  1265 180  HOH   HOH A . 
E 5 HOH   66  1266 9    HOH   HOH A . 
E 5 HOH   67  1267 244  HOH   HOH A . 
E 5 HOH   68  1268 158  HOH   HOH A . 
E 5 HOH   69  1269 76   HOH   HOH A . 
E 5 HOH   70  1270 110  HOH   HOH A . 
E 5 HOH   71  1271 29   HOH   HOH A . 
E 5 HOH   72  1272 2    HOH   HOH A . 
E 5 HOH   73  1273 118  HOH   HOH A . 
E 5 HOH   74  1274 120  HOH   HOH A . 
E 5 HOH   75  1275 168  HOH   HOH A . 
E 5 HOH   76  1276 43   HOH   HOH A . 
E 5 HOH   77  1277 162  HOH   HOH A . 
E 5 HOH   78  1278 166  HOH   HOH A . 
E 5 HOH   79  1279 54   HOH   HOH A . 
E 5 HOH   80  1280 236  HOH   HOH A . 
E 5 HOH   81  1281 385  HOH   HOH A . 
E 5 HOH   82  1282 266  HOH   HOH A . 
E 5 HOH   83  1283 389  HOH   HOH A . 
E 5 HOH   84  1284 131  HOH   HOH A . 
E 5 HOH   85  1285 291  HOH   HOH A . 
E 5 HOH   86  1286 324  HOH   HOH A . 
E 5 HOH   87  1287 112  HOH   HOH A . 
E 5 HOH   88  1288 107  HOH   HOH A . 
E 5 HOH   89  1289 102  HOH   HOH A . 
E 5 HOH   90  1290 71   HOH   HOH A . 
E 5 HOH   91  1291 165  HOH   HOH A . 
E 5 HOH   92  1292 128  HOH   HOH A . 
E 5 HOH   93  1293 95   HOH   HOH A . 
E 5 HOH   94  1294 56   HOH   HOH A . 
E 5 HOH   95  1295 88   HOH   HOH A . 
E 5 HOH   96  1296 294  HOH   HOH A . 
E 5 HOH   97  1297 26   HOH   HOH A . 
E 5 HOH   98  1298 23   HOH   HOH A . 
E 5 HOH   99  1299 374  HOH   HOH A . 
E 5 HOH   100 1300 53   HOH   HOH A . 
E 5 HOH   101 1301 6    HOH   HOH A . 
E 5 HOH   102 1302 214  HOH   HOH A . 
E 5 HOH   103 1303 59   HOH   HOH A . 
E 5 HOH   104 1304 129  HOH   HOH A . 
E 5 HOH   105 1305 318  HOH   HOH A . 
E 5 HOH   106 1306 16   HOH   HOH A . 
E 5 HOH   107 1307 68   HOH   HOH A . 
E 5 HOH   108 1308 255  HOH   HOH A . 
E 5 HOH   109 1309 127  HOH   HOH A . 
E 5 HOH   110 1310 350  HOH   HOH A . 
E 5 HOH   111 1311 7    HOH   HOH A . 
E 5 HOH   112 1312 348  HOH   HOH A . 
E 5 HOH   113 1313 337  HOH   HOH A . 
E 5 HOH   114 1314 257  HOH   HOH A . 
E 5 HOH   115 1315 368  HOH   HOH A . 
E 5 HOH   116 1316 134  HOH   HOH A . 
E 5 HOH   117 1317 167  HOH   HOH A . 
E 5 HOH   118 1318 10   HOH   HOH A . 
E 5 HOH   119 1319 283  HOH   HOH A . 
E 5 HOH   120 1320 49   HOH   HOH A . 
E 5 HOH   121 1321 362  HOH   HOH A . 
E 5 HOH   122 1322 31   HOH   HOH A . 
E 5 HOH   123 1323 269  HOH   HOH A . 
E 5 HOH   124 1324 50   HOH   HOH A . 
E 5 HOH   125 1325 90   HOH   HOH A . 
E 5 HOH   126 1326 98   HOH   HOH A . 
E 5 HOH   127 1327 316  HOH   HOH A . 
E 5 HOH   128 1328 246  HOH   HOH A . 
E 5 HOH   129 1329 209  HOH   HOH A . 
E 5 HOH   130 1330 57   HOH   HOH A . 
E 5 HOH   131 1331 103  HOH   HOH A . 
E 5 HOH   132 1332 157  HOH   HOH A . 
E 5 HOH   133 1333 272  HOH   HOH A . 
E 5 HOH   134 1334 193  HOH   HOH A . 
E 5 HOH   135 1335 262  HOH   HOH A . 
E 5 HOH   136 1336 126  HOH   HOH A . 
E 5 HOH   137 1337 296  HOH   HOH A . 
E 5 HOH   138 1338 20   HOH   HOH A . 
E 5 HOH   139 1339 5    HOH   HOH A . 
E 5 HOH   140 1340 163  HOH   HOH A . 
E 5 HOH   141 1341 89   HOH   HOH A . 
E 5 HOH   142 1342 28   HOH   HOH A . 
E 5 HOH   143 1343 188  HOH   HOH A . 
E 5 HOH   144 1344 231  HOH   HOH A . 
E 5 HOH   145 1345 92   HOH   HOH A . 
E 5 HOH   146 1346 220  HOH   HOH A . 
E 5 HOH   147 1347 330  HOH   HOH A . 
E 5 HOH   148 1348 239  HOH   HOH A . 
E 5 HOH   149 1349 79   HOH   HOH A . 
E 5 HOH   150 1350 80   HOH   HOH A . 
E 5 HOH   151 1351 33   HOH   HOH A . 
E 5 HOH   152 1352 313  HOH   HOH A . 
E 5 HOH   153 1353 96   HOH   HOH A . 
E 5 HOH   154 1354 70   HOH   HOH A . 
E 5 HOH   155 1355 289  HOH   HOH A . 
E 5 HOH   156 1356 45   HOH   HOH A . 
E 5 HOH   157 1357 152  HOH   HOH A . 
E 5 HOH   158 1358 93   HOH   HOH A . 
E 5 HOH   159 1359 72   HOH   HOH A . 
E 5 HOH   160 1360 52   HOH   HOH A . 
E 5 HOH   161 1361 197  HOH   HOH A . 
E 5 HOH   162 1362 17   HOH   HOH A . 
E 5 HOH   163 1363 8    HOH   HOH A . 
E 5 HOH   164 1364 136  HOH   HOH A . 
E 5 HOH   165 1365 42   HOH   HOH A . 
E 5 HOH   166 1366 139  HOH   HOH A . 
E 5 HOH   167 1367 281  HOH   HOH A . 
E 5 HOH   168 1368 63   HOH   HOH A . 
E 5 HOH   169 1369 182  HOH   HOH A . 
E 5 HOH   170 1370 135  HOH   HOH A . 
E 5 HOH   171 1371 261  HOH   HOH A . 
E 5 HOH   172 1372 264  HOH   HOH A . 
E 5 HOH   173 1373 77   HOH   HOH A . 
E 5 HOH   174 1374 302  HOH   HOH A . 
E 5 HOH   175 1375 142  HOH   HOH A . 
E 5 HOH   176 1376 154  HOH   HOH A . 
E 5 HOH   177 1377 61   HOH   HOH A . 
E 5 HOH   178 1378 132  HOH   HOH A . 
E 5 HOH   179 1379 47   HOH   HOH A . 
E 5 HOH   180 1380 334  HOH   HOH A . 
E 5 HOH   181 1381 222  HOH   HOH A . 
E 5 HOH   182 1382 263  HOH   HOH A . 
E 5 HOH   183 1383 69   HOH   HOH A . 
E 5 HOH   184 1384 39   HOH   HOH A . 
E 5 HOH   185 1385 37   HOH   HOH A . 
E 5 HOH   186 1386 65   HOH   HOH A . 
E 5 HOH   187 1387 24   HOH   HOH A . 
E 5 HOH   188 1388 30   HOH   HOH A . 
E 5 HOH   189 1389 176  HOH   HOH A . 
E 5 HOH   190 1390 161  HOH   HOH A . 
E 5 HOH   191 1391 304  HOH   HOH A . 
E 5 HOH   192 1392 215  HOH   HOH A . 
E 5 HOH   193 1393 116  HOH   HOH A . 
E 5 HOH   194 1394 265  HOH   HOH A . 
E 5 HOH   195 1395 83   HOH   HOH A . 
E 5 HOH   196 1396 303  HOH   HOH A . 
E 5 HOH   197 1397 391  HOH   HOH A . 
E 5 HOH   198 1398 147  HOH   HOH A . 
E 5 HOH   199 1399 191  HOH   HOH A . 
E 5 HOH   200 1400 366  HOH   HOH A . 
E 5 HOH   201 1401 248  HOH   HOH A . 
E 5 HOH   202 1402 336  HOH   HOH A . 
E 5 HOH   203 1403 144  HOH   HOH A . 
E 5 HOH   204 1404 14   HOH   HOH A . 
E 5 HOH   205 1405 11   HOH   HOH A . 
E 5 HOH   206 1406 171  HOH   HOH A . 
E 5 HOH   207 1407 35   HOH   HOH A . 
E 5 HOH   208 1408 247  HOH   HOH A . 
E 5 HOH   209 1409 394  HOH   HOH A . 
E 5 HOH   210 1410 137  HOH   HOH A . 
E 5 HOH   211 1411 392  HOH   HOH A . 
E 5 HOH   212 1412 356  HOH   HOH A . 
E 5 HOH   213 1413 178  HOH   HOH A . 
E 5 HOH   214 1414 36   HOH   HOH A . 
E 5 HOH   215 1415 119  HOH   HOH A . 
E 5 HOH   216 1416 159  HOH   HOH A . 
E 5 HOH   217 1417 84   HOH   HOH A . 
E 5 HOH   218 1418 311  HOH   HOH A . 
E 5 HOH   219 1419 270  HOH   HOH A . 
E 5 HOH   220 1420 183  HOH   HOH A . 
E 5 HOH   221 1421 260  HOH   HOH A . 
E 5 HOH   222 1422 64   HOH   HOH A . 
E 5 HOH   223 1423 217  HOH   HOH A . 
E 5 HOH   224 1424 73   HOH   HOH A . 
E 5 HOH   225 1425 66   HOH   HOH A . 
E 5 HOH   226 1426 207  HOH   HOH A . 
E 5 HOH   227 1427 229  HOH   HOH A . 
E 5 HOH   228 1428 104  HOH   HOH A . 
E 5 HOH   229 1429 200  HOH   HOH A . 
E 5 HOH   230 1430 268  HOH   HOH A . 
E 5 HOH   231 1431 367  HOH   HOH A . 
E 5 HOH   232 1432 301  HOH   HOH A . 
E 5 HOH   233 1433 267  HOH   HOH A . 
E 5 HOH   234 1434 125  HOH   HOH A . 
E 5 HOH   235 1435 363  HOH   HOH A . 
E 5 HOH   236 1436 46   HOH   HOH A . 
E 5 HOH   237 1437 108  HOH   HOH A . 
E 5 HOH   238 1438 312  HOH   HOH A . 
E 5 HOH   239 1439 94   HOH   HOH A . 
E 5 HOH   240 1440 62   HOH   HOH A . 
E 5 HOH   241 1441 145  HOH   HOH A . 
E 5 HOH   242 1442 308  HOH   HOH A . 
E 5 HOH   243 1443 351  HOH   HOH A . 
E 5 HOH   244 1444 390  HOH   HOH A . 
E 5 HOH   245 1445 250  HOH   HOH A . 
E 5 HOH   246 1446 359  HOH   HOH A . 
E 5 HOH   247 1447 186  HOH   HOH A . 
E 5 HOH   248 1448 354  HOH   HOH A . 
E 5 HOH   249 1449 123  HOH   HOH A . 
E 5 HOH   250 1450 105  HOH   HOH A . 
E 5 HOH   251 1451 360  HOH   HOH A . 
E 5 HOH   252 1452 111  HOH   HOH A . 
E 5 HOH   253 1453 195  HOH   HOH A . 
E 5 HOH   254 1454 364  HOH   HOH A . 
E 5 HOH   255 1455 75   HOH   HOH A . 
E 5 HOH   256 1456 213  HOH   HOH A . 
E 5 HOH   257 1457 279  HOH   HOH A . 
E 5 HOH   258 1458 240  HOH   HOH A . 
E 5 HOH   259 1459 81   HOH   HOH A . 
E 5 HOH   260 1460 78   HOH   HOH A . 
E 5 HOH   261 1461 245  HOH   HOH A . 
E 5 HOH   262 1462 22   HOH   HOH A . 
E 5 HOH   263 1463 210  HOH   HOH A . 
E 5 HOH   264 1464 223  HOH   HOH A . 
E 5 HOH   265 1465 275  HOH   HOH A . 
E 5 HOH   266 1466 156  HOH   HOH A . 
E 5 HOH   267 1467 373  HOH   HOH A . 
E 5 HOH   268 1468 224  HOH   HOH A . 
E 5 HOH   269 1469 241  HOH   HOH A . 
E 5 HOH   270 1470 192  HOH   HOH A . 
E 5 HOH   271 1471 202  HOH   HOH A . 
E 5 HOH   272 1472 326  HOH   HOH A . 
E 5 HOH   273 1473 133  HOH   HOH A . 
E 5 HOH   274 1474 172  HOH   HOH A . 
E 5 HOH   275 1475 19   HOH   HOH A . 
E 5 HOH   276 1476 274  HOH   HOH A . 
E 5 HOH   277 1477 212  HOH   HOH A . 
E 5 HOH   278 1478 60   HOH   HOH A . 
E 5 HOH   279 1479 379  HOH   HOH A . 
E 5 HOH   280 1480 179  HOH   HOH A . 
E 5 HOH   281 1481 206  HOH   HOH A . 
E 5 HOH   282 1482 113  HOH   HOH A . 
E 5 HOH   283 1483 292  HOH   HOH A . 
E 5 HOH   284 1484 32   HOH   HOH A . 
E 5 HOH   285 1485 402  HOH   HOH A . 
E 5 HOH   286 1486 51   HOH   HOH A . 
E 5 HOH   287 1487 378  HOH   HOH A . 
E 5 HOH   288 1488 194  HOH   HOH A . 
E 5 HOH   289 1489 122  HOH   HOH A . 
E 5 HOH   290 1490 221  HOH   HOH A . 
E 5 HOH   291 1491 375  HOH   HOH A . 
E 5 HOH   292 1492 384  HOH   HOH A . 
E 5 HOH   293 1493 285  HOH   HOH A . 
E 5 HOH   294 1494 114  HOH   HOH A . 
E 5 HOH   295 1495 399  HOH   HOH A . 
E 5 HOH   296 1496 4    HOH   HOH A . 
E 5 HOH   297 1497 305  HOH   HOH A . 
E 5 HOH   298 1498 387  HOH   HOH A . 
E 5 HOH   299 1499 211  HOH   HOH A . 
E 5 HOH   300 1500 15   HOH   HOH A . 
E 5 HOH   301 1501 140  HOH   HOH A . 
E 5 HOH   302 1502 320  HOH   HOH A . 
E 5 HOH   303 1503 41   HOH   HOH A . 
E 5 HOH   304 1504 190  HOH   HOH A . 
E 5 HOH   305 1505 251  HOH   HOH A . 
E 5 HOH   306 1506 1    HOH   HOH A . 
E 5 HOH   307 1507 130  HOH   HOH A . 
E 5 HOH   308 1508 151  HOH   HOH A . 
E 5 HOH   309 1509 106  HOH   HOH A . 
E 5 HOH   310 1510 358  HOH   HOH A . 
E 5 HOH   311 1511 346  HOH   HOH A . 
E 5 HOH   312 1512 288  HOH   HOH A . 
E 5 HOH   313 1513 323  HOH   HOH A . 
E 5 HOH   314 1514 327  HOH   HOH A . 
E 5 HOH   315 1515 357  HOH   HOH A . 
E 5 HOH   316 1516 300  HOH   HOH A . 
E 5 HOH   317 1517 309  HOH   HOH A . 
E 5 HOH   318 1518 349  HOH   HOH A . 
E 5 HOH   319 1519 372  HOH   HOH A . 
E 5 HOH   320 1520 273  HOH   HOH A . 
E 5 HOH   321 1521 352  HOH   HOH A . 
E 5 HOH   322 1522 380  HOH   HOH A . 
E 5 HOH   323 1523 398  HOH   HOH A . 
E 5 HOH   324 1524 347  HOH   HOH A . 
E 5 HOH   325 1525 282  HOH   HOH A . 
E 5 HOH   326 1526 284  HOH   HOH A . 
E 5 HOH   327 1527 203  HOH   HOH A . 
E 5 HOH   328 1528 34   HOH   HOH A . 
E 5 HOH   329 1529 175  HOH   HOH A . 
E 5 HOH   330 1530 227  HOH   HOH A . 
E 5 HOH   331 1531 315  HOH   HOH A . 
E 5 HOH   332 1532 276  HOH   HOH A . 
E 5 HOH   333 1533 310  HOH   HOH A . 
E 5 HOH   334 1534 189  HOH   HOH A . 
E 5 HOH   335 1535 344  HOH   HOH A . 
E 5 HOH   336 1536 343  HOH   HOH A . 
E 5 HOH   337 1537 278  HOH   HOH A . 
E 5 HOH   338 1538 341  HOH   HOH A . 
E 5 HOH   339 1539 233  HOH   HOH A . 
E 5 HOH   340 1540 382  HOH   HOH A . 
E 5 HOH   341 1541 259  HOH   HOH A . 
E 5 HOH   342 1542 287  HOH   HOH A . 
E 5 HOH   343 1543 317  HOH   HOH A . 
E 5 HOH   344 1544 225  HOH   HOH A . 
E 5 HOH   345 1545 333  HOH   HOH A . 
E 5 HOH   346 1546 253  HOH   HOH A . 
E 5 HOH   347 1547 306  HOH   HOH A . 
E 5 HOH   348 1548 319  HOH   HOH A . 
E 5 HOH   349 1549 405  HOH   HOH A . 
E 5 HOH   350 1550 160  HOH   HOH A . 
E 5 HOH   351 1551 339  HOH   HOH A . 
E 5 HOH   352 1552 101  HOH   HOH A . 
E 5 HOH   353 1553 242  HOH   HOH A . 
E 5 HOH   354 1554 377  HOH   HOH A . 
E 5 HOH   355 1555 234  HOH   HOH A . 
E 5 HOH   356 1556 345  HOH   HOH A . 
E 5 HOH   357 1557 148  HOH   HOH A . 
E 5 HOH   358 1558 173  HOH   HOH A . 
E 5 HOH   359 1559 164  HOH   HOH A . 
E 5 HOH   360 1560 121  HOH   HOH A . 
E 5 HOH   361 1561 295  HOH   HOH A . 
E 5 HOH   362 1562 322  HOH   HOH A . 
E 5 HOH   363 1563 395  HOH   HOH A . 
E 5 HOH   364 1564 150  HOH   HOH A . 
E 5 HOH   365 1565 376  HOH   HOH A . 
E 5 HOH   366 1566 149  HOH   HOH A . 
E 5 HOH   367 1567 328  HOH   HOH A . 
E 5 HOH   368 1568 170  HOH   HOH A . 
E 5 HOH   369 1569 331  HOH   HOH A . 
E 5 HOH   370 1570 174  HOH   HOH A . 
E 5 HOH   371 1571 181  HOH   HOH A . 
E 5 HOH   372 1572 386  HOH   HOH A . 
E 5 HOH   373 1573 208  HOH   HOH A . 
E 5 HOH   374 1574 396  HOH   HOH A . 
E 5 HOH   375 1575 381  HOH   HOH A . 
E 5 HOH   376 1576 365  HOH   HOH A . 
E 5 HOH   377 1577 187  HOH   HOH A . 
E 5 HOH   378 1578 321  HOH   HOH A . 
E 5 HOH   379 1579 338  HOH   HOH A . 
E 5 HOH   380 1580 249  HOH   HOH A . 
E 5 HOH   381 1581 404  HOH   HOH A . 
E 5 HOH   382 1582 237  HOH   HOH A . 
E 5 HOH   383 1583 400  HOH   HOH A . 
E 5 HOH   384 1584 205  HOH   HOH A . 
E 5 HOH   385 1585 286  HOH   HOH A . 
E 5 HOH   386 1586 335  HOH   HOH A . 
E 5 HOH   387 1587 403  HOH   HOH A . 
E 5 HOH   388 1588 97   HOH   HOH A . 
E 5 HOH   389 1589 124  HOH   HOH A . 
E 5 HOH   390 1590 314  HOH   HOH A . 
E 5 HOH   391 1591 290  HOH   HOH A . 
E 5 HOH   392 1592 67   HOH   HOH A . 
E 5 HOH   393 1593 146  HOH   HOH A . 
E 5 HOH   394 1594 388  HOH   HOH A . 
E 5 HOH   395 1595 325  HOH   HOH A . 
E 5 HOH   396 1596 342  HOH   HOH A . 
E 5 HOH   397 1597 329  HOH   HOH A . 
E 5 HOH   398 1598 307  HOH   HOH A . 
E 5 HOH   399 1599 138  HOH   HOH A . 
E 5 HOH   400 1600 201  HOH   HOH A . 
E 5 HOH   401 1601 169  HOH   HOH A . 
E 5 HOH   402 1602 232  HOH   HOH A . 
E 5 HOH   403 1603 340  HOH   HOH A . 
E 5 HOH   404 1604 298  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   ? ? ? '(1.14_3260: ???)' 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                     9BVF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.016 
_cell.length_a_esd                 ? 
_cell.length_b                     86.246 
_cell.length_b_esd                 ? 
_cell.length_c                     107.238 
_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                         9BVF 
_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                   9BVF 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.93 
_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 
# 
_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                                       9BVF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.822 
_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                                     52763 
_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                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.008 
_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                                0.099 
_reflns.pdbx_Rpim_I_all                                0.038 
_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                              0.091 
_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 
1.83 1.86  ? ? ? ? ? ? 2621 ? ? ? ? ? ? ? ? ? ? ? 6.5 1.064 ? ? 1.131 0.440 ? 1  1 0.659 0.891 ? 100.0 ? 1.040 ? ? ? ? ? ? ? ? ? 
1.86 1.90  ? ? ? ? ? ? 2580 ? ? ? ? ? ? ? ? ? ? ? 6.6 1.094 ? ? 0.929 0.359 ? 2  1 0.773 0.934 ? 100.0 ? 0.856 ? ? ? ? ? ? ? ? ? 
1.90 1.93  ? ? ? ? ? ? 2594 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.074 ? ? 0.766 0.294 ? 3  1 0.813 0.947 ? 100.0 ? 0.707 ? ? ? ? ? ? ? ? ? 
1.93 1.97  ? ? ? ? ? ? 2619 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.103 ? ? 0.655 0.251 ? 4  1 0.867 0.964 ? 100.0 ? 0.604 ? ? ? ? ? ? ? ? ? 
1.97 2.01  ? ? ? ? ? ? 2598 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.084 ? ? 0.512 0.197 ? 5  1 0.906 0.975 ? 100.0 ? 0.473 ? ? ? ? ? ? ? ? ? 
2.01 2.06  ? ? ? ? ? ? 2603 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.091 ? ? 0.392 0.150 ? 6  1 0.949 0.987 ? 100.0 ? 0.362 ? ? ? ? ? ? ? ? ? 
2.06 2.11  ? ? ? ? ? ? 2619 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.089 ? ? 0.334 0.128 ? 7  1 0.957 0.989 ? 100.0 ? 0.308 ? ? ? ? ? ? ? ? ? 
2.11 2.17  ? ? ? ? ? ? 2590 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.078 ? ? 0.285 0.109 ? 8  1 0.969 0.992 ? 100.0 ? 0.263 ? ? ? ? ? ? ? ? ? 
2.17 2.23  ? ? ? ? ? ? 2625 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.050 ? ? 0.250 0.096 ? 9  1 0.974 0.993 ? 100.0 ? 0.231 ? ? ? ? ? ? ? ? ? 
2.23 2.31  ? ? ? ? ? ? 2601 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.055 ? ? 0.217 0.083 ? 10 1 0.978 0.994 ? 100.0 ? 0.200 ? ? ? ? ? ? ? ? ? 
2.31 2.39  ? ? ? ? ? ? 2612 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.010 ? ? 0.189 0.072 ? 11 1 0.980 0.995 ? 100.0 ? 0.174 ? ? ? ? ? ? ? ? ? 
2.39 2.48  ? ? ? ? ? ? 2642 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.031 ? ? 0.166 0.064 ? 12 1 0.986 0.997 ? 100.0 ? 0.153 ? ? ? ? ? ? ? ? ? 
2.48 2.60  ? ? ? ? ? ? 2628 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.052 ? ? 0.145 0.056 ? 13 1 0.988 0.997 ? 100.0 ? 0.134 ? ? ? ? ? ? ? ? ? 
2.60 2.73  ? ? ? ? ? ? 2624 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.004 ? ? 0.128 0.049 ? 14 1 0.990 0.997 ? 100.0 ? 0.118 ? ? ? ? ? ? ? ? ? 
2.73 2.90  ? ? ? ? ? ? 2663 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.061 ? ? 0.120 0.046 ? 15 1 0.990 0.997 ? 100.0 ? 0.110 ? ? ? ? ? ? ? ? ? 
2.90 3.13  ? ? ? ? ? ? 2635 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.067 ? ? 0.122 0.047 ? 16 1 0.988 0.997 ? 99.9  ? 0.113 ? ? ? ? ? ? ? ? ? 
3.13 3.44  ? ? ? ? ? ? 2656 ? ? ? ? ? ? ? ? ? ? ? 6.7 1.000 ? ? 0.117 0.045 ? 17 1 0.989 0.997 ? 100.0 ? 0.108 ? ? ? ? ? ? ? ? ? 
3.44 3.94  ? ? ? ? ? ? 2695 ? ? ? ? ? ? ? ? ? ? ? 6.4 0.971 ? ? 0.091 0.036 ? 18 1 0.991 0.998 ? 99.7  ? 0.084 ? ? ? ? ? ? ? ? ? 
3.94 4.97  ? ? ? ? ? ? 2705 ? ? ? ? ? ? ? ? ? ? ? 6.5 0.826 ? ? 0.070 0.027 ? 19 1 0.995 0.999 ? 99.9  ? 0.064 ? ? ? ? ? ? ? ? ? 
4.97 50.00 ? ? ? ? ? ? 2853 ? ? ? ? ? ? ? ? ? ? ? 6.2 0.345 ? ? 0.048 0.019 ? 20 1 0.998 0.999 ? 99.9  ? 0.044 ? ? ? ? ? ? ? ? ? 
# 
_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                                 9BVF 
_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                            1.822 
_refine.ls_d_res_low                             31.508 
_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                     52675 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.54 
_refine.ls_percent_reflns_R_free                 3.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1801 
_refine.ls_R_factor_R_free                       0.2132 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1787 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 23.03 
_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                            0.23 
_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.pdbx_number_atoms_protein        3919 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             405 
_refine_hist.number_atoms_total               4359 
_refine_hist.d_res_high                       1.822 
_refine_hist.d_res_low                        31.508 
# 
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  ? 4134 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.807  ? 5592 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.379 ? 2552 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 600  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 721  ? 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' 1.8224 1.8680 . . 133 3393 94.00  . . . . 0.2899 . . . . . . . . . . . 0.3297 
'X-RAY DIFFRACTION' 1.8680 1.9185 . . 142 3582 100.00 . . . . 0.2511 . . . . . . . . . . . 0.3226 
'X-RAY DIFFRACTION' 1.9185 1.9749 . . 142 3594 100.00 . . . . 0.2348 . . . . . . . . . . . 0.2915 
'X-RAY DIFFRACTION' 1.9749 2.0386 . . 141 3572 100.00 . . . . 0.2137 . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 2.0386 2.1115 . . 142 3598 100.00 . . . . 0.2033 . . . . . . . . . . . 0.2624 
'X-RAY DIFFRACTION' 2.1115 2.1960 . . 141 3595 100.00 . . . . 0.1989 . . . . . . . . . . . 0.2687 
'X-RAY DIFFRACTION' 2.1960 2.2959 . . 143 3614 100.00 . . . . 0.1894 . . . . . . . . . . . 0.2007 
'X-RAY DIFFRACTION' 2.2959 2.4169 . . 143 3617 100.00 . . . . 0.1902 . . . . . . . . . . . 0.2292 
'X-RAY DIFFRACTION' 2.4169 2.5683 . . 143 3607 100.00 . . . . 0.1916 . . . . . . . . . . . 0.2410 
'X-RAY DIFFRACTION' 2.5683 2.7665 . . 143 3634 100.00 . . . . 0.1910 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 2.7665 3.0447 . . 143 3643 100.00 . . . . 0.1903 . . . . . . . . . . . 0.2385 
'X-RAY DIFFRACTION' 3.0447 3.4848 . . 145 3668 100.00 . . . . 0.1845 . . . . . . . . . . . 0.2161 
'X-RAY DIFFRACTION' 3.4848 4.3885 . . 146 3693 100.00 . . . . 0.1500 . . . . . . . . . . . 0.1758 
'X-RAY DIFFRACTION' 4.3885 31.5   . . 153 3865 100.00 . . . . 0.1555 . . . . . . . . . . . 0.1768 
# 
_struct.entry_id                     9BVF 
_struct.title                        'Identification of multiple ligand hotspots on SOS2, compound 6' 
_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        9BVF 
_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 ? 
D N N 4 ? 
E N N 5 ? 
# 
_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              9BVF 
_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 9BVF MET A 1  ? UNP Q07890 ? ? 'expression tag' -28 1  
1 9BVF SER A 2  ? UNP Q07890 ? ? 'expression tag' -27 2  
1 9BVF TYR A 3  ? UNP Q07890 ? ? 'expression tag' -26 3  
1 9BVF TYR A 4  ? UNP Q07890 ? ? 'expression tag' -25 4  
1 9BVF HIS A 5  ? UNP Q07890 ? ? 'expression tag' -24 5  
1 9BVF HIS A 6  ? UNP Q07890 ? ? 'expression tag' -23 6  
1 9BVF HIS A 7  ? UNP Q07890 ? ? 'expression tag' -22 7  
1 9BVF HIS A 8  ? UNP Q07890 ? ? 'expression tag' -21 8  
1 9BVF HIS A 9  ? UNP Q07890 ? ? 'expression tag' -20 9  
1 9BVF HIS A 10 ? UNP Q07890 ? ? 'expression tag' -19 10 
1 9BVF LEU A 11 ? UNP Q07890 ? ? 'expression tag' -18 11 
1 9BVF GLU A 12 ? UNP Q07890 ? ? 'expression tag' -17 12 
1 9BVF SER A 13 ? UNP Q07890 ? ? 'expression tag' -16 13 
1 9BVF THR A 14 ? UNP Q07890 ? ? 'expression tag' -15 14 
1 9BVF SER A 15 ? UNP Q07890 ? ? 'expression tag' -14 15 
1 9BVF LEU A 16 ? UNP Q07890 ? ? 'expression tag' -13 16 
1 9BVF TYR A 17 ? UNP Q07890 ? ? 'expression tag' -12 17 
1 9BVF LYS A 18 ? UNP Q07890 ? ? 'expression tag' -11 18 
1 9BVF LYS A 19 ? UNP Q07890 ? ? 'expression tag' -10 19 
1 9BVF ALA A 20 ? UNP Q07890 ? ? 'expression tag' -9  20 
1 9BVF GLY A 21 ? UNP Q07890 ? ? 'expression tag' -8  21 
1 9BVF PHE A 22 ? UNP Q07890 ? ? 'expression tag' -7  22 
1 9BVF GLU A 23 ? UNP Q07890 ? ? 'expression tag' -6  23 
1 9BVF ASN A 24 ? UNP Q07890 ? ? 'expression tag' -5  24 
1 9BVF LEU A 25 ? UNP Q07890 ? ? 'expression tag' -4  25 
1 9BVF TYR A 26 ? UNP Q07890 ? ? 'expression tag' -3  26 
1 9BVF PHE A 27 ? UNP Q07890 ? ? 'expression tag' -2  27 
1 9BVF 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)' 370   ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  25280 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 SER A 136 ? TYR A 146 ? SER A 673  TYR A 683  1 ? 11 
HELX_P HELX_P7  AA7 TYR A 146 ? HIS A 165 ? TYR A 683  HIS A 702  1 ? 20 
HELX_P HELX_P8  AA8 PHE A 166 ? ASP A 172 ? PHE A 703  ASP A 709  1 ? 7  
HELX_P HELX_P9  AA9 ASP A 172 ? VAL A 186 ? ASP A 709  VAL A 723  1 ? 15 
HELX_P HELX_P10 AB1 GLY A 188 ? ALA A 208 ? GLY A 725  ALA A 745  1 ? 21 
HELX_P HELX_P11 AB2 GLN A 235 ? PHE A 239 ? GLN A 772  PHE A 776  5 ? 5  
HELX_P HELX_P12 AB3 HIS A 245 ? LYS A 263 ? HIS A 782  LYS A 800  1 ? 19 
HELX_P HELX_P13 AB4 GLN A 265 ? LYS A 276 ? GLN A 802  LYS A 813  5 ? 12 
HELX_P HELX_P14 AB5 ASP A 278 ? SER A 283 ? ASP A 815  SER A 820  1 ? 6  
HELX_P HELX_P15 AB6 SER A 283 ? GLU A 306 ? SER A 820  GLU A 843  1 ? 24 
HELX_P HELX_P16 AB7 ASN A 309 ? LEU A 330 ? ASN A 846  LEU A 867  1 ? 22 
HELX_P HELX_P17 AB8 ASN A 332 ? ASN A 344 ? ASN A 869  ASN A 881  1 ? 13 
HELX_P HELX_P18 AB9 SER A 345 ? ARG A 350 ? SER A 882  ARG A 887  1 ? 6  
HELX_P HELX_P19 AC1 LEU A 351 ? LEU A 358 ? LEU A 888  LEU A 895  1 ? 8  
HELX_P HELX_P20 AC2 GLN A 359 ? ILE A 387 ? GLN A 896  ILE A 924  1 ? 29 
HELX_P HELX_P21 AC3 PHE A 395 ? ASN A 409 ? PHE A 932  ASN A 946  1 ? 15 
HELX_P HELX_P22 AC4 PHE A 423 ? GLN A 438 ? PHE A 960  GLN A 975  1 ? 16 
HELX_P HELX_P23 AC5 GLU A 449 ? ASN A 458 ? GLU A 986  ASN A 995  1 ? 10 
HELX_P HELX_P24 AC6 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       0.22 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 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 TYR A 3   ? TYR A 4   ? TYR A -26 TYR A -25 
AA1 2 ARG A 33  ? LEU A 34  ? ARG A 570 LEU A 571 
AA2 1 ILE A 51  ? PHE A 53  ? ILE A 588 PHE A 590 
AA2 2 ILE A 66  ? GLY A 69  ? ILE A 603 GLY A 606 
AA2 3 LEU A 420 ? ASN A 422 ? LEU A 957 ASN A 959 
AA2 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 TYR A 3   ? N TYR A -26 O LEU A 34  ? O LEU A 571 
AA2 1 2 N VAL A 52  ? N VAL A 589 O GLY A 68  ? O GLY A 605 
AA2 2 3 N GLY A 69  ? N GLY A 606 O ILE A 421 ? O ILE A 958 
AA2 3 4 O LEU A 420 ? O LEU A 957 N LEU A 413 ? N LEU A 950 
# 
_pdbx_entry_details.entry_id                   9BVF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 OD1 A ASN 593  ? ? O A HOH 1201 ? ? 1.71 
2  1 O   A HOH 1562 ? ? O A HOH 1569 ? ? 1.93 
3  1 O   A HOH 1529 ? ? O A HOH 1602 ? ? 1.94 
4  1 OE1 A GLU 838  ? ? O A HOH 1202 ? ? 2.04 
5  1 O   A HOH 1209 ? ? O A HOH 1479 ? ? 2.04 
6  1 NE2 A GLN 865  ? ? O A HOH 1203 ? ? 2.05 
7  1 OE1 A GLU 1004 ? ? O A HOH 1204 ? ? 2.09 
8  1 NH1 A ARG 1021 ? ? O A HOH 1205 ? ? 2.11 
9  1 O   A HOH 1313 ? ? O A HOH 1438 ? ? 2.13 
10 1 O1  A SO4 1103 ? ? O A HOH 1206 ? ? 2.14 
11 1 O   A HOH 1505 ? ? O A HOH 1532 ? ? 2.15 
12 1 O   A HOH 1446 ? ? O A HOH 1536 ? ? 2.16 
13 1 OD1 A ASN 995  ? ? O A HOH 1207 ? ? 2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 587 ? ? -140.11 -12.42  
2 1 PHE A 636 ? ? -142.14 -0.28   
3 1 ASP A 659 ? ? -61.70  93.25   
4 1 ALA A 660 ? ? 161.59  -50.10  
5 1 TYR A 683 ? ? -120.96 -58.86  
6 1 HIS A 766 ? ? -114.71 -105.71 
7 1 ASP A 815 ? ? -93.06  31.92   
8 1 ASN A 978 ? ? -115.18 51.56   
# 
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 -19.2313 -17.4548 -30.4923 0.3841 ? -0.0003 ? -0.0342 ? 0.3675 ? -0.0324 ? 0.3098 ? 1.0651 ? 
0.4645  ? -0.2752 ? 0.6701 ? 0.4795  ? 1.4497 ? -0.1677 ? 0.1361  ? -0.0371 ? -0.3235 ? 0.1221  ? -0.0397 ? -0.0398 ? 0.1752  ? 
-0.0043 ? 
2 'X-RAY DIFFRACTION' ? refined -17.3294 -13.5486 -14.3070 0.2267 ? 0.0170  ? 0.0050  ? 0.2149 ? -0.0138 ? 0.1935 ? 3.1579 ? 
1.1555  ? 0.1192  ? 3.8055 ? 0.7038  ? 2.5656 ? 0.0738  ? -0.0224 ? -0.0729 ? 0.1556  ? -0.1090 ? 0.0656  ? 0.1482  ? -0.0993 ? 
0.0059  ? 
3 'X-RAY DIFFRACTION' ? refined -2.6546  -15.5466 2.9483   0.5225 ? -0.0362 ? -0.0277 ? 0.3942 ? 0.1120  ? 0.4129 ? 8.2230 ? 
1.7208  ? 2.6770  ? 0.4774 ? 0.7637  ? 1.1095 ? 0.3590  ? -0.8606 ? -0.9554 ? 0.1381  ? -0.2643 ? -0.3096 ? 0.1512  ? -0.3091 ? 
-0.1326 ? 
4 'X-RAY DIFFRACTION' ? refined 22.3156  6.2438   -8.1137  0.2258 ? 0.0189  ? 0.0091  ? 0.1794 ? -0.0063 ? 0.1889 ? 2.4678 ? 
1.0468  ? 0.2372  ? 1.9314 ? 0.1969  ? 0.9129 ? 0.0542  ? 0.0778  ? -0.0316 ? -0.0002 ? -0.0040 ? 0.0388  ? 0.1158  ? 0.0060  ? 
0.0193  ? 
5 'X-RAY DIFFRACTION' ? refined -2.4015  -2.9016  -25.0995 0.3659 ? -0.0469 ? 0.0752  ? 0.3584 ? 0.0189  ? 0.3249 ? 8.0384 ? 
0.5850  ? 4.2979  ? 3.5702 ? -0.2063 ? 6.0084 ? -0.0211 ? 0.9713  ? 0.4331  ? -0.5166 ? 0.1006  ? -0.0729 ? -0.0995 ? 0.2788  ? 
-0.0629 ? 
6 'X-RAY DIFFRACTION' ? refined 17.3521  4.8490   2.8585   0.3164 ? -0.0281 ? 0.0528  ? 0.3701 ? 0.0150  ? 0.2619 ? 2.3225 ? 
-0.4319 ? 0.2186  ? 3.4130 ? -0.8758 ? 1.9190 ? 0.1062  ? -0.2214 ? -0.1572 ? 0.4461  ? -0.0448 ? 0.1297  ? 0.0592  ? -0.2750 ? 
-0.0758 ? 
7 'X-RAY DIFFRACTION' ? refined 32.8458  21.0871  -4.7249  0.3291 ? -0.0227 ? 0.0314  ? 0.2875 ? -0.0342 ? 0.3298 ? 3.4014 ? 
-1.3963 ? 1.6845  ? 3.6367 ? -1.3189 ? 2.6371 ? -0.1286 ? 0.0387  ? 0.3401  ? 0.0968  ? -0.0567 ? -0.3709 ? -0.3787 ? 0.0617  ? 
0.1863  ? 
# 
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 -27 through 602 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 603 through 725 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 726 through 762 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 763 through 944 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 945 through 976 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 977 through 1003 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;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 HIS -22  ? A HIS 7   
3  1 Y 1 A HIS -21  ? A HIS 8   
4  1 Y 1 A HIS -20  ? A HIS 9   
5  1 Y 1 A HIS -19  ? A HIS 10  
6  1 Y 1 A LEU -18  ? A LEU 11  
7  1 Y 1 A GLU -17  ? A GLU 12  
8  1 Y 1 A SER -16  ? A SER 13  
9  1 Y 1 A THR -15  ? A THR 14  
10 1 Y 1 A SER -14  ? A SER 15  
11 1 Y 1 A LEU -13  ? A LEU 16  
12 1 Y 1 A TYR -12  ? A TYR 17  
13 1 Y 1 A LYS -11  ? A LYS 18  
14 1 Y 1 A LYS -10  ? A LYS 19  
15 1 Y 1 A ALA -9   ? A ALA 20  
16 1 Y 1 A GLY -8   ? A GLY 21  
17 1 Y 1 A PHE -7   ? A PHE 22  
18 1 Y 1 A GLU -6   ? A GLU 23  
19 1 Y 1 A ASN -5   ? A ASN 24  
20 1 Y 1 A SER 596  ? A SER 59  
21 1 Y 1 A ARG 597  ? A ARG 60  
22 1 Y 1 A SER 598  ? A SER 61  
23 1 Y 1 A LEU 663  ? A LEU 126 
24 1 Y 1 A ALA 664  ? A ALA 127 
25 1 Y 1 A ILE 665  ? A ILE 128 
26 1 Y 1 A GLU 666  ? A GLU 129 
27 1 Y 1 A LYS 667  ? A LYS 130 
28 1 Y 1 A GLY 668  ? A GLY 131 
29 1 Y 1 A GLU 669  ? A GLU 132 
30 1 Y 1 A GLN 670  ? A GLN 133 
31 1 Y 1 A PRO 671  ? A PRO 134 
32 1 Y 1 A GLN 746  ? A GLN 209 
33 1 Y 1 A ALA 747  ? A ALA 210 
34 1 Y 1 A ASN 748  ? A ASN 211 
35 1 Y 1 A GLY 749  ? A GLY 212 
36 1 Y 1 A VAL 750  ? A VAL 213 
37 1 Y 1 A SER 751  ? A SER 214 
38 1 Y 1 A HIS 752  ? A HIS 215 
39 1 Y 1 A ASN 753  ? A ASN 216 
40 1 Y 1 A THR 1046 ? A THR 509 
41 1 Y 1 A GLY 1047 ? A GLY 510 
42 1 Y 1 A ARG 1048 ? A ARG 511 
43 1 Y 1 A HIS 1049 ? A HIS 512 
44 1 Y 1 A GLY 1050 ? A GLY 513 
45 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 
A1ASX N1   N N N 1   
A1ASX N3   N Y N 2   
A1ASX C4   C N N 3   
A1ASX C5   C N N 4   
A1ASX C6   C N N 5   
A1ASX C7   C Y N 6   
A1ASX C8   C Y N 7   
A1ASX C10  C Y N 8   
A1ASX C13  C Y N 9   
A1ASX C15  C Y N 10  
A1ASX C17  C Y N 11  
A1ASX C20  C Y N 12  
A1ASX C1   C N N 13  
A1ASX C11  C Y N 14  
A1ASX C12  C Y N 15  
A1ASX C14  C Y N 16  
A1ASX C16  C Y N 17  
A1ASX C18  C Y N 18  
A1ASX C19  C Y N 19  
A1ASX C2   C N S 20  
A1ASX C3   C N N 21  
A1ASX C9   C Y N 22  
A1ASX N2   N N N 23  
A1ASX N4   N N N 24  
A1ASX N5   N Y N 25  
A1ASX O1   O N N 26  
A1ASX H1   H N N 27  
A1ASX H2   H N N 28  
A1ASX H3   H N N 29  
A1ASX H4   H N N 30  
A1ASX H5   H N N 31  
A1ASX H6   H N N 32  
A1ASX H7   H N N 33  
A1ASX H8   H N N 34  
A1ASX H9   H N N 35  
A1ASX H10  H N N 36  
A1ASX H11  H N N 37  
A1ASX H12  H N N 38  
A1ASX H13  H N N 39  
A1ASX H14  H N N 40  
A1ASX H15  H N N 41  
A1ASX H16  H N N 42  
A1ASX H17  H N N 43  
A1ASX H18  H N N 44  
A1ASX H19  H N N 45  
A1ASX H20  H N N 46  
A1ASX H21  H N N 47  
A1ASX H23  H N N 48  
A1ASX H24  H N N 49  
ALA   N    N N N 50  
ALA   CA   C N S 51  
ALA   C    C N N 52  
ALA   O    O N N 53  
ALA   CB   C N N 54  
ALA   OXT  O N N 55  
ALA   H    H N N 56  
ALA   H2   H N N 57  
ALA   HA   H N N 58  
ALA   HB1  H N N 59  
ALA   HB2  H N N 60  
ALA   HB3  H N N 61  
ALA   HXT  H N N 62  
ARG   N    N N N 63  
ARG   CA   C N S 64  
ARG   C    C N N 65  
ARG   O    O N N 66  
ARG   CB   C N N 67  
ARG   CG   C N N 68  
ARG   CD   C N N 69  
ARG   NE   N N N 70  
ARG   CZ   C N N 71  
ARG   NH1  N N N 72  
ARG   NH2  N N N 73  
ARG   OXT  O N N 74  
ARG   H    H N N 75  
ARG   H2   H N N 76  
ARG   HA   H N N 77  
ARG   HB2  H N N 78  
ARG   HB3  H N N 79  
ARG   HG2  H N N 80  
ARG   HG3  H N N 81  
ARG   HD2  H N N 82  
ARG   HD3  H N N 83  
ARG   HE   H N N 84  
ARG   HH11 H N N 85  
ARG   HH12 H N N 86  
ARG   HH21 H N N 87  
ARG   HH22 H N N 88  
ARG   HXT  H N N 89  
ASN   N    N N N 90  
ASN   CA   C N S 91  
ASN   C    C N N 92  
ASN   O    O N N 93  
ASN   CB   C N N 94  
ASN   CG   C N N 95  
ASN   OD1  O N N 96  
ASN   ND2  N N N 97  
ASN   OXT  O N N 98  
ASN   H    H N N 99  
ASN   H2   H N N 100 
ASN   HA   H N N 101 
ASN   HB2  H N N 102 
ASN   HB3  H N N 103 
ASN   HD21 H N N 104 
ASN   HD22 H N N 105 
ASN   HXT  H N N 106 
ASP   N    N N N 107 
ASP   CA   C N S 108 
ASP   C    C N N 109 
ASP   O    O N N 110 
ASP   CB   C N N 111 
ASP   CG   C N N 112 
ASP   OD1  O N N 113 
ASP   OD2  O N N 114 
ASP   OXT  O N N 115 
ASP   H    H N N 116 
ASP   H2   H N N 117 
ASP   HA   H N N 118 
ASP   HB2  H N N 119 
ASP   HB3  H N N 120 
ASP   HD2  H N N 121 
ASP   HXT  H N N 122 
CYS   N    N N N 123 
CYS   CA   C N R 124 
CYS   C    C N N 125 
CYS   O    O N N 126 
CYS   CB   C N N 127 
CYS   SG   S N N 128 
CYS   OXT  O N N 129 
CYS   H    H N N 130 
CYS   H2   H N N 131 
CYS   HA   H N N 132 
CYS   HB2  H N N 133 
CYS   HB3  H N N 134 
CYS   HG   H N N 135 
CYS   HXT  H N N 136 
DMS   S    S N N 137 
DMS   O    O N N 138 
DMS   C1   C N N 139 
DMS   C2   C N N 140 
DMS   H11  H N N 141 
DMS   H12  H N N 142 
DMS   H13  H N N 143 
DMS   H21  H N N 144 
DMS   H22  H N N 145 
DMS   H23  H N N 146 
GLN   N    N N N 147 
GLN   CA   C N S 148 
GLN   C    C N N 149 
GLN   O    O N N 150 
GLN   CB   C N N 151 
GLN   CG   C N N 152 
GLN   CD   C N N 153 
GLN   OE1  O N N 154 
GLN   NE2  N N N 155 
GLN   OXT  O N N 156 
GLN   H    H N N 157 
GLN   H2   H N N 158 
GLN   HA   H N N 159 
GLN   HB2  H N N 160 
GLN   HB3  H N N 161 
GLN   HG2  H N N 162 
GLN   HG3  H N N 163 
GLN   HE21 H N N 164 
GLN   HE22 H N N 165 
GLN   HXT  H N N 166 
GLU   N    N N N 167 
GLU   CA   C N S 168 
GLU   C    C N N 169 
GLU   O    O N N 170 
GLU   CB   C N N 171 
GLU   CG   C N N 172 
GLU   CD   C N N 173 
GLU   OE1  O N N 174 
GLU   OE2  O N N 175 
GLU   OXT  O N N 176 
GLU   H    H N N 177 
GLU   H2   H N N 178 
GLU   HA   H N N 179 
GLU   HB2  H N N 180 
GLU   HB3  H N N 181 
GLU   HG2  H N N 182 
GLU   HG3  H N N 183 
GLU   HE2  H N N 184 
GLU   HXT  H N N 185 
GLY   N    N N N 186 
GLY   CA   C N N 187 
GLY   C    C N N 188 
GLY   O    O N N 189 
GLY   OXT  O N N 190 
GLY   H    H N N 191 
GLY   H2   H N N 192 
GLY   HA2  H N N 193 
GLY   HA3  H N N 194 
GLY   HXT  H N N 195 
HIS   N    N N N 196 
HIS   CA   C N S 197 
HIS   C    C N N 198 
HIS   O    O N N 199 
HIS   CB   C N N 200 
HIS   CG   C Y N 201 
HIS   ND1  N Y N 202 
HIS   CD2  C Y N 203 
HIS   CE1  C Y N 204 
HIS   NE2  N Y N 205 
HIS   OXT  O N N 206 
HIS   H    H N N 207 
HIS   H2   H N N 208 
HIS   HA   H N N 209 
HIS   HB2  H N N 210 
HIS   HB3  H N N 211 
HIS   HD1  H N N 212 
HIS   HD2  H N N 213 
HIS   HE1  H N N 214 
HIS   HE2  H N N 215 
HIS   HXT  H N N 216 
HOH   O    O N N 217 
HOH   H1   H N N 218 
HOH   H2   H N N 219 
ILE   N    N N N 220 
ILE   CA   C N S 221 
ILE   C    C N N 222 
ILE   O    O N N 223 
ILE   CB   C N S 224 
ILE   CG1  C N N 225 
ILE   CG2  C N N 226 
ILE   CD1  C N N 227 
ILE   OXT  O N N 228 
ILE   H    H N N 229 
ILE   H2   H N N 230 
ILE   HA   H N N 231 
ILE   HB   H N N 232 
ILE   HG12 H N N 233 
ILE   HG13 H N N 234 
ILE   HG21 H N N 235 
ILE   HG22 H N N 236 
ILE   HG23 H N N 237 
ILE   HD11 H N N 238 
ILE   HD12 H N N 239 
ILE   HD13 H N N 240 
ILE   HXT  H N N 241 
LEU   N    N N N 242 
LEU   CA   C N S 243 
LEU   C    C N N 244 
LEU   O    O N N 245 
LEU   CB   C N N 246 
LEU   CG   C N N 247 
LEU   CD1  C N N 248 
LEU   CD2  C N N 249 
LEU   OXT  O N N 250 
LEU   H    H N N 251 
LEU   H2   H N N 252 
LEU   HA   H N N 253 
LEU   HB2  H N N 254 
LEU   HB3  H N N 255 
LEU   HG   H N N 256 
LEU   HD11 H N N 257 
LEU   HD12 H N N 258 
LEU   HD13 H N N 259 
LEU   HD21 H N N 260 
LEU   HD22 H N N 261 
LEU   HD23 H N N 262 
LEU   HXT  H N N 263 
LYS   N    N N N 264 
LYS   CA   C N S 265 
LYS   C    C N N 266 
LYS   O    O N N 267 
LYS   CB   C N N 268 
LYS   CG   C N N 269 
LYS   CD   C N N 270 
LYS   CE   C N N 271 
LYS   NZ   N N N 272 
LYS   OXT  O N N 273 
LYS   H    H N N 274 
LYS   H2   H N N 275 
LYS   HA   H N N 276 
LYS   HB2  H N N 277 
LYS   HB3  H N N 278 
LYS   HG2  H N N 279 
LYS   HG3  H N N 280 
LYS   HD2  H N N 281 
LYS   HD3  H N N 282 
LYS   HE2  H N N 283 
LYS   HE3  H N N 284 
LYS   HZ1  H N N 285 
LYS   HZ2  H N N 286 
LYS   HZ3  H N N 287 
LYS   HXT  H N N 288 
MET   N    N N N 289 
MET   CA   C N S 290 
MET   C    C N N 291 
MET   O    O N N 292 
MET   CB   C N N 293 
MET   CG   C N N 294 
MET   SD   S N N 295 
MET   CE   C N N 296 
MET   OXT  O N N 297 
MET   H    H N N 298 
MET   H2   H N N 299 
MET   HA   H N N 300 
MET   HB2  H N N 301 
MET   HB3  H N N 302 
MET   HG2  H N N 303 
MET   HG3  H N N 304 
MET   HE1  H N N 305 
MET   HE2  H N N 306 
MET   HE3  H N N 307 
MET   HXT  H N N 308 
PHE   N    N N N 309 
PHE   CA   C N S 310 
PHE   C    C N N 311 
PHE   O    O N N 312 
PHE   CB   C N N 313 
PHE   CG   C Y N 314 
PHE   CD1  C Y N 315 
PHE   CD2  C Y N 316 
PHE   CE1  C Y N 317 
PHE   CE2  C Y N 318 
PHE   CZ   C Y N 319 
PHE   OXT  O N N 320 
PHE   H    H N N 321 
PHE   H2   H N N 322 
PHE   HA   H N N 323 
PHE   HB2  H N N 324 
PHE   HB3  H N N 325 
PHE   HD1  H N N 326 
PHE   HD2  H N N 327 
PHE   HE1  H N N 328 
PHE   HE2  H N N 329 
PHE   HZ   H N N 330 
PHE   HXT  H N N 331 
PRO   N    N N N 332 
PRO   CA   C N S 333 
PRO   C    C N N 334 
PRO   O    O N N 335 
PRO   CB   C N N 336 
PRO   CG   C N N 337 
PRO   CD   C N N 338 
PRO   OXT  O N N 339 
PRO   H    H N N 340 
PRO   HA   H N N 341 
PRO   HB2  H N N 342 
PRO   HB3  H N N 343 
PRO   HG2  H N N 344 
PRO   HG3  H N N 345 
PRO   HD2  H N N 346 
PRO   HD3  H N N 347 
PRO   HXT  H N N 348 
SER   N    N N N 349 
SER   CA   C N S 350 
SER   C    C N N 351 
SER   O    O N N 352 
SER   CB   C N N 353 
SER   OG   O N N 354 
SER   OXT  O N N 355 
SER   H    H N N 356 
SER   H2   H N N 357 
SER   HA   H N N 358 
SER   HB2  H N N 359 
SER   HB3  H N N 360 
SER   HG   H N N 361 
SER   HXT  H N N 362 
SO4   S    S N N 363 
SO4   O1   O N N 364 
SO4   O2   O N N 365 
SO4   O3   O N N 366 
SO4   O4   O N N 367 
THR   N    N N N 368 
THR   CA   C N S 369 
THR   C    C N N 370 
THR   O    O N N 371 
THR   CB   C N R 372 
THR   OG1  O N N 373 
THR   CG2  C N N 374 
THR   OXT  O N N 375 
THR   H    H N N 376 
THR   H2   H N N 377 
THR   HA   H N N 378 
THR   HB   H N N 379 
THR   HG1  H N N 380 
THR   HG21 H N N 381 
THR   HG22 H N N 382 
THR   HG23 H N N 383 
THR   HXT  H N N 384 
TRP   N    N N N 385 
TRP   CA   C N S 386 
TRP   C    C N N 387 
TRP   O    O N N 388 
TRP   CB   C N N 389 
TRP   CG   C Y N 390 
TRP   CD1  C Y N 391 
TRP   CD2  C Y N 392 
TRP   NE1  N Y N 393 
TRP   CE2  C Y N 394 
TRP   CE3  C Y N 395 
TRP   CZ2  C Y N 396 
TRP   CZ3  C Y N 397 
TRP   CH2  C Y N 398 
TRP   OXT  O N N 399 
TRP   H    H N N 400 
TRP   H2   H N N 401 
TRP   HA   H N N 402 
TRP   HB2  H N N 403 
TRP   HB3  H N N 404 
TRP   HD1  H N N 405 
TRP   HE1  H N N 406 
TRP   HE3  H N N 407 
TRP   HZ2  H N N 408 
TRP   HZ3  H N N 409 
TRP   HH2  H N N 410 
TRP   HXT  H N N 411 
TYR   N    N N N 412 
TYR   CA   C N S 413 
TYR   C    C N N 414 
TYR   O    O N N 415 
TYR   CB   C N N 416 
TYR   CG   C Y N 417 
TYR   CD1  C Y N 418 
TYR   CD2  C Y N 419 
TYR   CE1  C Y N 420 
TYR   CE2  C Y N 421 
TYR   CZ   C Y N 422 
TYR   OH   O N N 423 
TYR   OXT  O N N 424 
TYR   H    H N N 425 
TYR   H2   H N N 426 
TYR   HA   H N N 427 
TYR   HB2  H N N 428 
TYR   HB3  H N N 429 
TYR   HD1  H N N 430 
TYR   HD2  H N N 431 
TYR   HE1  H N N 432 
TYR   HE2  H N N 433 
TYR   HH   H N N 434 
TYR   HXT  H N N 435 
VAL   N    N N N 436 
VAL   CA   C N S 437 
VAL   C    C N N 438 
VAL   O    O N N 439 
VAL   CB   C N N 440 
VAL   CG1  C N N 441 
VAL   CG2  C N N 442 
VAL   OXT  O N N 443 
VAL   H    H N N 444 
VAL   H2   H N N 445 
VAL   HA   H N N 446 
VAL   HB   H N N 447 
VAL   HG11 H N N 448 
VAL   HG12 H N N 449 
VAL   HG13 H N N 450 
VAL   HG21 H N N 451 
VAL   HG22 H N N 452 
VAL   HG23 H N N 453 
VAL   HXT  H N N 454 
# 
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 
A1ASX N2  C6   sing N N 1   
A1ASX N2  C2   sing N N 2   
A1ASX C6  C5   sing N N 3   
A1ASX C1  C2   sing N N 4   
A1ASX C2  C3   sing N N 5   
A1ASX C5  C4   sing N N 6   
A1ASX C11 C10  doub Y N 7   
A1ASX C11 C12  sing Y N 8   
A1ASX C10 C9   sing Y N 9   
A1ASX O1  C12  sing N N 10  
A1ASX C12 C13  doub Y N 11  
A1ASX C3  N1   sing N N 12  
A1ASX C4  N1   sing N N 13  
A1ASX N1  C7   sing N N 14  
A1ASX C9  N4   sing N N 15  
A1ASX C9  C14  doub Y N 16  
A1ASX N3  C7   doub Y N 17  
A1ASX N3  C8   sing Y N 18  
A1ASX N4  C8   sing N N 19  
A1ASX C7  C20  sing Y N 20  
A1ASX C8  N5   doub Y N 21  
A1ASX C13 C14  sing Y N 22  
A1ASX C20 C19  doub Y N 23  
A1ASX C20 C15  sing Y N 24  
A1ASX N5  C15  sing Y N 25  
A1ASX C19 C18  sing Y N 26  
A1ASX C15 C16  doub Y N 27  
A1ASX C18 C17  doub Y N 28  
A1ASX C16 C17  sing Y N 29  
A1ASX C4  H1   sing N N 30  
A1ASX C4  H2   sing N N 31  
A1ASX C5  H3   sing N N 32  
A1ASX C5  H4   sing N N 33  
A1ASX C6  H5   sing N N 34  
A1ASX C6  H6   sing N N 35  
A1ASX C10 H7   sing N N 36  
A1ASX C13 H8   sing N N 37  
A1ASX C17 H9   sing N N 38  
A1ASX C1  H10  sing N N 39  
A1ASX C1  H11  sing N N 40  
A1ASX C1  H12  sing N N 41  
A1ASX C11 H13  sing N N 42  
A1ASX C14 H14  sing N N 43  
A1ASX C16 H15  sing N N 44  
A1ASX C18 H16  sing N N 45  
A1ASX C19 H17  sing N N 46  
A1ASX C2  H18  sing N N 47  
A1ASX C3  H19  sing N N 48  
A1ASX C3  H20  sing N N 49  
A1ASX N2  H21  sing N N 50  
A1ASX N4  H23  sing N N 51  
A1ASX O1  H24  sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
CYS   N   CA   sing N N 122 
CYS   N   H    sing N N 123 
CYS   N   H2   sing N N 124 
CYS   CA  C    sing N N 125 
CYS   CA  CB   sing N N 126 
CYS   CA  HA   sing N N 127 
CYS   C   O    doub N N 128 
CYS   C   OXT  sing N N 129 
CYS   CB  SG   sing N N 130 
CYS   CB  HB2  sing N N 131 
CYS   CB  HB3  sing N N 132 
CYS   SG  HG   sing N N 133 
CYS   OXT HXT  sing N N 134 
DMS   S   O    doub N N 135 
DMS   S   C1   sing N N 136 
DMS   S   C2   sing N N 137 
DMS   C1  H11  sing N N 138 
DMS   C1  H12  sing N N 139 
DMS   C1  H13  sing N N 140 
DMS   C2  H21  sing N N 141 
DMS   C2  H22  sing N N 142 
DMS   C2  H23  sing N N 143 
GLN   N   CA   sing N N 144 
GLN   N   H    sing N N 145 
GLN   N   H2   sing N N 146 
GLN   CA  C    sing N N 147 
GLN   CA  CB   sing N N 148 
GLN   CA  HA   sing N N 149 
GLN   C   O    doub N N 150 
GLN   C   OXT  sing N N 151 
GLN   CB  CG   sing N N 152 
GLN   CB  HB2  sing N N 153 
GLN   CB  HB3  sing N N 154 
GLN   CG  CD   sing N N 155 
GLN   CG  HG2  sing N N 156 
GLN   CG  HG3  sing N N 157 
GLN   CD  OE1  doub N N 158 
GLN   CD  NE2  sing N N 159 
GLN   NE2 HE21 sing N N 160 
GLN   NE2 HE22 sing N N 161 
GLN   OXT HXT  sing N N 162 
GLU   N   CA   sing N N 163 
GLU   N   H    sing N N 164 
GLU   N   H2   sing N N 165 
GLU   CA  C    sing N N 166 
GLU   CA  CB   sing N N 167 
GLU   CA  HA   sing N N 168 
GLU   C   O    doub N N 169 
GLU   C   OXT  sing N N 170 
GLU   CB  CG   sing N N 171 
GLU   CB  HB2  sing N N 172 
GLU   CB  HB3  sing N N 173 
GLU   CG  CD   sing N N 174 
GLU   CG  HG2  sing N N 175 
GLU   CG  HG3  sing N N 176 
GLU   CD  OE1  doub N N 177 
GLU   CD  OE2  sing N N 178 
GLU   OE2 HE2  sing N N 179 
GLU   OXT HXT  sing N N 180 
GLY   N   CA   sing N N 181 
GLY   N   H    sing N N 182 
GLY   N   H2   sing N N 183 
GLY   CA  C    sing N N 184 
GLY   CA  HA2  sing N N 185 
GLY   CA  HA3  sing N N 186 
GLY   C   O    doub N N 187 
GLY   C   OXT  sing N N 188 
GLY   OXT HXT  sing N N 189 
HIS   N   CA   sing N N 190 
HIS   N   H    sing N N 191 
HIS   N   H2   sing N N 192 
HIS   CA  C    sing N N 193 
HIS   CA  CB   sing N N 194 
HIS   CA  HA   sing N N 195 
HIS   C   O    doub N N 196 
HIS   C   OXT  sing N N 197 
HIS   CB  CG   sing N N 198 
HIS   CB  HB2  sing N N 199 
HIS   CB  HB3  sing N N 200 
HIS   CG  ND1  sing Y N 201 
HIS   CG  CD2  doub Y N 202 
HIS   ND1 CE1  doub Y N 203 
HIS   ND1 HD1  sing N N 204 
HIS   CD2 NE2  sing Y N 205 
HIS   CD2 HD2  sing N N 206 
HIS   CE1 NE2  sing Y N 207 
HIS   CE1 HE1  sing N N 208 
HIS   NE2 HE2  sing N N 209 
HIS   OXT HXT  sing N N 210 
HOH   O   H1   sing N N 211 
HOH   O   H2   sing N N 212 
ILE   N   CA   sing N N 213 
ILE   N   H    sing N N 214 
ILE   N   H2   sing N N 215 
ILE   CA  C    sing N N 216 
ILE   CA  CB   sing N N 217 
ILE   CA  HA   sing N N 218 
ILE   C   O    doub N N 219 
ILE   C   OXT  sing N N 220 
ILE   CB  CG1  sing N N 221 
ILE   CB  CG2  sing N N 222 
ILE   CB  HB   sing N N 223 
ILE   CG1 CD1  sing N N 224 
ILE   CG1 HG12 sing N N 225 
ILE   CG1 HG13 sing N N 226 
ILE   CG2 HG21 sing N N 227 
ILE   CG2 HG22 sing N N 228 
ILE   CG2 HG23 sing N N 229 
ILE   CD1 HD11 sing N N 230 
ILE   CD1 HD12 sing N N 231 
ILE   CD1 HD13 sing N N 232 
ILE   OXT HXT  sing N N 233 
LEU   N   CA   sing N N 234 
LEU   N   H    sing N N 235 
LEU   N   H2   sing N N 236 
LEU   CA  C    sing N N 237 
LEU   CA  CB   sing N N 238 
LEU   CA  HA   sing N N 239 
LEU   C   O    doub N N 240 
LEU   C   OXT  sing N N 241 
LEU   CB  CG   sing N N 242 
LEU   CB  HB2  sing N N 243 
LEU   CB  HB3  sing N N 244 
LEU   CG  CD1  sing N N 245 
LEU   CG  CD2  sing N N 246 
LEU   CG  HG   sing N N 247 
LEU   CD1 HD11 sing N N 248 
LEU   CD1 HD12 sing N N 249 
LEU   CD1 HD13 sing N N 250 
LEU   CD2 HD21 sing N N 251 
LEU   CD2 HD22 sing N N 252 
LEU   CD2 HD23 sing N N 253 
LEU   OXT HXT  sing N N 254 
LYS   N   CA   sing N N 255 
LYS   N   H    sing N N 256 
LYS   N   H2   sing N N 257 
LYS   CA  C    sing N N 258 
LYS   CA  CB   sing N N 259 
LYS   CA  HA   sing N N 260 
LYS   C   O    doub N N 261 
LYS   C   OXT  sing N N 262 
LYS   CB  CG   sing N N 263 
LYS   CB  HB2  sing N N 264 
LYS   CB  HB3  sing N N 265 
LYS   CG  CD   sing N N 266 
LYS   CG  HG2  sing N N 267 
LYS   CG  HG3  sing N N 268 
LYS   CD  CE   sing N N 269 
LYS   CD  HD2  sing N N 270 
LYS   CD  HD3  sing N N 271 
LYS   CE  NZ   sing N N 272 
LYS   CE  HE2  sing N N 273 
LYS   CE  HE3  sing N N 274 
LYS   NZ  HZ1  sing N N 275 
LYS   NZ  HZ2  sing N N 276 
LYS   NZ  HZ3  sing N N 277 
LYS   OXT HXT  sing N N 278 
MET   N   CA   sing N N 279 
MET   N   H    sing N N 280 
MET   N   H2   sing N N 281 
MET   CA  C    sing N N 282 
MET   CA  CB   sing N N 283 
MET   CA  HA   sing N N 284 
MET   C   O    doub N N 285 
MET   C   OXT  sing N N 286 
MET   CB  CG   sing N N 287 
MET   CB  HB2  sing N N 288 
MET   CB  HB3  sing N N 289 
MET   CG  SD   sing N N 290 
MET   CG  HG2  sing N N 291 
MET   CG  HG3  sing N N 292 
MET   SD  CE   sing N N 293 
MET   CE  HE1  sing N N 294 
MET   CE  HE2  sing N N 295 
MET   CE  HE3  sing N N 296 
MET   OXT HXT  sing N N 297 
PHE   N   CA   sing N N 298 
PHE   N   H    sing N N 299 
PHE   N   H2   sing N N 300 
PHE   CA  C    sing N N 301 
PHE   CA  CB   sing N N 302 
PHE   CA  HA   sing N N 303 
PHE   C   O    doub N N 304 
PHE   C   OXT  sing N N 305 
PHE   CB  CG   sing N N 306 
PHE   CB  HB2  sing N N 307 
PHE   CB  HB3  sing N N 308 
PHE   CG  CD1  doub Y N 309 
PHE   CG  CD2  sing Y N 310 
PHE   CD1 CE1  sing Y N 311 
PHE   CD1 HD1  sing N N 312 
PHE   CD2 CE2  doub Y N 313 
PHE   CD2 HD2  sing N N 314 
PHE   CE1 CZ   doub Y N 315 
PHE   CE1 HE1  sing N N 316 
PHE   CE2 CZ   sing Y N 317 
PHE   CE2 HE2  sing N N 318 
PHE   CZ  HZ   sing N N 319 
PHE   OXT HXT  sing N N 320 
PRO   N   CA   sing N N 321 
PRO   N   CD   sing N N 322 
PRO   N   H    sing N N 323 
PRO   CA  C    sing N N 324 
PRO   CA  CB   sing N N 325 
PRO   CA  HA   sing N N 326 
PRO   C   O    doub N N 327 
PRO   C   OXT  sing N N 328 
PRO   CB  CG   sing N N 329 
PRO   CB  HB2  sing N N 330 
PRO   CB  HB3  sing N N 331 
PRO   CG  CD   sing N N 332 
PRO   CG  HG2  sing N N 333 
PRO   CG  HG3  sing N N 334 
PRO   CD  HD2  sing N N 335 
PRO   CD  HD3  sing N N 336 
PRO   OXT HXT  sing N N 337 
SER   N   CA   sing N N 338 
SER   N   H    sing N N 339 
SER   N   H2   sing N N 340 
SER   CA  C    sing N N 341 
SER   CA  CB   sing N N 342 
SER   CA  HA   sing N N 343 
SER   C   O    doub N N 344 
SER   C   OXT  sing N N 345 
SER   CB  OG   sing N N 346 
SER   CB  HB2  sing N N 347 
SER   CB  HB3  sing N N 348 
SER   OG  HG   sing N N 349 
SER   OXT HXT  sing N N 350 
SO4   S   O1   doub N N 351 
SO4   S   O2   doub N N 352 
SO4   S   O3   sing N N 353 
SO4   S   O4   sing N N 354 
THR   N   CA   sing N N 355 
THR   N   H    sing N N 356 
THR   N   H2   sing N N 357 
THR   CA  C    sing N N 358 
THR   CA  CB   sing N N 359 
THR   CA  HA   sing N N 360 
THR   C   O    doub N N 361 
THR   C   OXT  sing N N 362 
THR   CB  OG1  sing N N 363 
THR   CB  CG2  sing N N 364 
THR   CB  HB   sing N N 365 
THR   OG1 HG1  sing N N 366 
THR   CG2 HG21 sing N N 367 
THR   CG2 HG22 sing N N 368 
THR   CG2 HG23 sing N N 369 
THR   OXT HXT  sing N N 370 
TRP   N   CA   sing N N 371 
TRP   N   H    sing N N 372 
TRP   N   H2   sing N N 373 
TRP   CA  C    sing N N 374 
TRP   CA  CB   sing N N 375 
TRP   CA  HA   sing N N 376 
TRP   C   O    doub N N 377 
TRP   C   OXT  sing N N 378 
TRP   CB  CG   sing N N 379 
TRP   CB  HB2  sing N N 380 
TRP   CB  HB3  sing N N 381 
TRP   CG  CD1  doub Y N 382 
TRP   CG  CD2  sing Y N 383 
TRP   CD1 NE1  sing Y N 384 
TRP   CD1 HD1  sing N N 385 
TRP   CD2 CE2  doub Y N 386 
TRP   CD2 CE3  sing Y N 387 
TRP   NE1 CE2  sing Y N 388 
TRP   NE1 HE1  sing N N 389 
TRP   CE2 CZ2  sing Y N 390 
TRP   CE3 CZ3  doub Y N 391 
TRP   CE3 HE3  sing N N 392 
TRP   CZ2 CH2  doub Y N 393 
TRP   CZ2 HZ2  sing N N 394 
TRP   CZ3 CH2  sing Y N 395 
TRP   CZ3 HZ3  sing N N 396 
TRP   CH2 HH2  sing N N 397 
TRP   OXT HXT  sing N N 398 
TYR   N   CA   sing N N 399 
TYR   N   H    sing N N 400 
TYR   N   H2   sing N N 401 
TYR   CA  C    sing N N 402 
TYR   CA  CB   sing N N 403 
TYR   CA  HA   sing N N 404 
TYR   C   O    doub N N 405 
TYR   C   OXT  sing N N 406 
TYR   CB  CG   sing N N 407 
TYR   CB  HB2  sing N N 408 
TYR   CB  HB3  sing N N 409 
TYR   CG  CD1  doub Y N 410 
TYR   CG  CD2  sing Y N 411 
TYR   CD1 CE1  sing Y N 412 
TYR   CD1 HD1  sing N N 413 
TYR   CD2 CE2  doub Y N 414 
TYR   CD2 HD2  sing N N 415 
TYR   CE1 CZ   doub Y N 416 
TYR   CE1 HE1  sing N N 417 
TYR   CE2 CZ   sing Y N 418 
TYR   CE2 HE2  sing N N 419 
TYR   CZ  OH   sing N N 420 
TYR   OH  HH   sing N N 421 
TYR   OXT HXT  sing N N 422 
VAL   N   CA   sing N N 423 
VAL   N   H    sing N N 424 
VAL   N   H2   sing N N 425 
VAL   CA  C    sing N N 426 
VAL   CA  CB   sing N N 427 
VAL   CA  HA   sing N N 428 
VAL   C   O    doub N N 429 
VAL   C   OXT  sing N N 430 
VAL   CB  CG1  sing N N 431 
VAL   CB  CG2  sing N N 432 
VAL   CB  HB   sing N N 433 
VAL   CG1 HG11 sing N N 434 
VAL   CG1 HG12 sing N N 435 
VAL   CG1 HG13 sing N N 436 
VAL   CG2 HG21 sing N N 437 
VAL   CG2 HG22 sing N N 438 
VAL   CG2 HG23 sing N N 439 
VAL   OXT HXT  sing N N 440 
# 
_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                    9BVF 
_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]   0.015869 
_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]   0.011595 
_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]   0.009325 
_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   . SER   A 1 2   ? -33.529 -20.416 -30.413 1.00 67.00  ? -27  SER   A N   1 
ATOM   2    C CA  . SER   A 1 2   ? -33.628 -19.234 -31.267 1.00 64.83  ? -27  SER   A CA  1 
ATOM   3    C C   . SER   A 1 2   ? -32.277 -18.541 -31.415 1.00 58.80  ? -27  SER   A C   1 
ATOM   4    O O   . SER   A 1 2   ? -31.967 -17.972 -32.465 1.00 54.68  ? -27  SER   A O   1 
ATOM   5    C CB  . SER   A 1 2   ? -34.662 -18.258 -30.712 1.00 67.11  ? -27  SER   A CB  1 
ATOM   6    O OG  . SER   A 1 2   ? -35.926 -18.885 -30.603 1.00 77.69  ? -27  SER   A OG  1 
ATOM   7    N N   . TYR   A 1 3   ? -31.489 -18.572 -30.345 1.00 53.75  ? -26  TYR   A N   1 
ATOM   8    C CA  . TYR   A 1 3   ? -30.099 -18.141 -30.373 1.00 48.76  ? -26  TYR   A CA  1 
ATOM   9    C C   . TYR   A 1 3   ? -29.223 -19.323 -29.986 1.00 47.52  ? -26  TYR   A C   1 
ATOM   10   O O   . TYR   A 1 3   ? -29.600 -20.129 -29.127 1.00 44.96  ? -26  TYR   A O   1 
ATOM   11   C CB  . TYR   A 1 3   ? -29.843 -16.957 -29.425 1.00 48.86  ? -26  TYR   A CB  1 
ATOM   12   C CG  . TYR   A 1 3   ? -30.438 -15.644 -29.901 1.00 58.92  ? -26  TYR   A CG  1 
ATOM   13   C CD1 . TYR   A 1 3   ? -31.763 -15.318 -29.626 1.00 72.44  ? -26  TYR   A CD1 1 
ATOM   14   C CD2 . TYR   A 1 3   ? -29.677 -14.732 -30.630 1.00 60.44  ? -26  TYR   A CD2 1 
ATOM   15   C CE1 . TYR   A 1 3   ? -32.321 -14.115 -30.059 1.00 73.74  ? -26  TYR   A CE1 1 
ATOM   16   C CE2 . TYR   A 1 3   ? -30.230 -13.524 -31.073 1.00 65.55  ? -26  TYR   A CE2 1 
ATOM   17   C CZ  . TYR   A 1 3   ? -31.555 -13.222 -30.782 1.00 65.97  ? -26  TYR   A CZ  1 
ATOM   18   O OH  . TYR   A 1 3   ? -32.121 -12.028 -31.199 1.00 58.65  ? -26  TYR   A OH  1 
ATOM   19   N N   . TYR   A 1 4   ? -28.061 -19.429 -30.629 1.00 41.53  ? -25  TYR   A N   1 
ATOM   20   C CA  . TYR   A 1 4   ? -27.177 -20.568 -30.436 1.00 43.58  ? -25  TYR   A CA  1 
ATOM   21   C C   . TYR   A 1 4   ? -25.736 -20.093 -30.305 1.00 46.40  ? -25  TYR   A C   1 
ATOM   22   O O   . TYR   A 1 4   ? -25.369 -18.997 -30.741 1.00 53.39  ? -25  TYR   A O   1 
ATOM   23   C CB  . TYR   A 1 4   ? -27.294 -21.582 -31.589 1.00 42.65  ? -25  TYR   A CB  1 
ATOM   24   C CG  . TYR   A 1 4   ? -28.695 -22.131 -31.750 1.00 38.62  ? -25  TYR   A CG  1 
ATOM   25   C CD1 . TYR   A 1 4   ? -29.146 -23.198 -30.968 1.00 34.38  ? -25  TYR   A CD1 1 
ATOM   26   C CD2 . TYR   A 1 4   ? -29.570 -21.574 -32.672 1.00 33.02  ? -25  TYR   A CD2 1 
ATOM   27   C CE1 . TYR   A 1 4   ? -30.447 -23.692 -31.114 1.00 35.92  ? -25  TYR   A CE1 1 
ATOM   28   C CE2 . TYR   A 1 4   ? -30.864 -22.056 -32.828 1.00 33.13  ? -25  TYR   A CE2 1 
ATOM   29   C CZ  . TYR   A 1 4   ? -31.302 -23.105 -32.042 1.00 39.47  ? -25  TYR   A CZ  1 
ATOM   30   O OH  . TYR   A 1 4   ? -32.589 -23.571 -32.211 1.00 38.90  ? -25  TYR   A OH  1 
ATOM   31   N N   . HIS   A 1 5   ? -24.923 -20.940 -29.683 1.00 41.17  ? -24  HIS   A N   1 
ATOM   32   C CA  . HIS   A 1 5   ? -23.488 -20.710 -29.614 1.00 45.21  ? -24  HIS   A CA  1 
ATOM   33   C C   . HIS   A 1 5   ? -22.835 -21.223 -30.888 1.00 42.04  ? -24  HIS   A C   1 
ATOM   34   O O   . HIS   A 1 5   ? -23.053 -22.370 -31.287 1.00 42.60  ? -24  HIS   A O   1 
ATOM   35   C CB  . HIS   A 1 5   ? -22.863 -21.399 -28.404 1.00 39.17  ? -24  HIS   A CB  1 
ATOM   36   C CG  . HIS   A 1 5   ? -21.381 -21.210 -28.327 1.00 61.31  ? -24  HIS   A CG  1 
ATOM   37   N ND1 . HIS   A 1 5   ? -20.486 -22.199 -28.677 1.00 68.19  ? -24  HIS   A ND1 1 
ATOM   38   C CD2 . HIS   A 1 5   ? -20.636 -20.135 -27.977 1.00 64.68  ? -24  HIS   A CD2 1 
ATOM   39   C CE1 . HIS   A 1 5   ? -19.254 -21.749 -28.523 1.00 71.30  ? -24  HIS   A CE1 1 
ATOM   40   N NE2 . HIS   A 1 5   ? -19.317 -20.498 -28.100 1.00 67.42  ? -24  HIS   A NE2 1 
ATOM   41   N N   . HIS   A 1 6   ? -22.020 -20.380 -31.509 1.00 48.69  ? -23  HIS   A N   1 
ATOM   42   C CA  . HIS   A 1 6   ? -21.352 -20.755 -32.748 1.00 52.75  ? -23  HIS   A CA  1 
ATOM   43   C C   . HIS   A 1 6   ? -20.014 -21.427 -32.470 1.00 53.90  ? -23  HIS   A C   1 
ATOM   44   O O   . HIS   A 1 6   ? -19.078 -20.774 -32.027 1.00 56.95  ? -23  HIS   A O   1 
ATOM   45   C CB  . HIS   A 1 6   ? -21.161 -19.523 -33.628 1.00 51.41  ? -23  HIS   A CB  1 
ATOM   46   C CG  . HIS   A 1 6   ? -22.448 -18.904 -34.074 1.00 45.34  ? -23  HIS   A CG  1 
ATOM   47   N ND1 . HIS   A 1 6   ? -22.756 -18.712 -35.403 1.00 45.71  ? -23  HIS   A ND1 1 
ATOM   48   C CD2 . HIS   A 1 6   ? -23.516 -18.457 -33.371 1.00 46.98  ? -23  HIS   A CD2 1 
ATOM   49   C CE1 . HIS   A 1 6   ? -23.954 -18.165 -35.498 1.00 55.63  ? -23  HIS   A CE1 1 
ATOM   50   N NE2 . HIS   A 1 6   ? -24.439 -18.002 -34.280 1.00 50.98  ? -23  HIS   A NE2 1 
ATOM   51   N N   . LEU   A 1 25  ? -14.975 -30.667 -35.110 1.00 65.71  ? -4   LEU   A N   1 
ATOM   52   C CA  . LEU   A 1 25  ? -13.760 -30.949 -35.881 1.00 62.90  ? -4   LEU   A CA  1 
ATOM   53   C C   . LEU   A 1 25  ? -14.038 -31.817 -37.110 1.00 59.95  ? -4   LEU   A C   1 
ATOM   54   O O   . LEU   A 1 25  ? -13.990 -31.333 -38.243 1.00 76.63  ? -4   LEU   A O   1 
ATOM   55   C CB  . LEU   A 1 25  ? -12.715 -31.630 -34.999 1.00 67.63  ? -4   LEU   A CB  1 
ATOM   56   C CG  . LEU   A 1 25  ? -11.320 -30.997 -35.002 1.00 67.19  ? -4   LEU   A CG  1 
ATOM   57   C CD1 . LEU   A 1 25  ? -10.848 -30.686 -36.419 1.00 65.42  ? -4   LEU   A CD1 1 
ATOM   58   C CD2 . LEU   A 1 25  ? -11.309 -29.749 -34.140 1.00 65.67  ? -4   LEU   A CD2 1 
ATOM   59   N N   . TYR   A 1 26  ? -14.310 -33.103 -36.886 1.00 41.88  ? -3   TYR   A N   1 
ATOM   60   C CA  . TYR   A 1 26  ? -14.664 -34.020 -37.961 1.00 38.08  ? -3   TYR   A CA  1 
ATOM   61   C C   . TYR   A 1 26  ? -16.152 -34.362 -37.959 1.00 37.67  ? -3   TYR   A C   1 
ATOM   62   O O   . TYR   A 1 26  ? -16.579 -35.289 -38.663 1.00 38.46  ? -3   TYR   A O   1 
ATOM   63   C CB  . TYR   A 1 26  ? -13.806 -35.278 -37.865 1.00 45.84  ? -3   TYR   A CB  1 
ATOM   64   C CG  . TYR   A 1 26  ? -12.333 -34.933 -37.863 1.00 42.74  ? -3   TYR   A CG  1 
ATOM   65   C CD1 . TYR   A 1 26  ? -11.738 -34.383 -38.990 1.00 49.99  ? -3   TYR   A CD1 1 
ATOM   66   C CD2 . TYR   A 1 26  ? -11.543 -35.126 -36.731 1.00 50.24  ? -3   TYR   A CD2 1 
ATOM   67   C CE1 . TYR   A 1 26  ? -10.391 -34.051 -39.005 1.00 52.07  ? -3   TYR   A CE1 1 
ATOM   68   C CE2 . TYR   A 1 26  ? -10.180 -34.795 -36.736 1.00 40.40  ? -3   TYR   A CE2 1 
ATOM   69   C CZ  . TYR   A 1 26  ? -9.619  -34.257 -37.880 1.00 47.43  ? -3   TYR   A CZ  1 
ATOM   70   O OH  . TYR   A 1 26  ? -8.282  -33.915 -37.917 1.00 47.89  ? -3   TYR   A OH  1 
ATOM   71   N N   . PHE   A 1 27  ? -16.939 -33.622 -37.193 1.00 36.54  ? -2   PHE   A N   1 
ATOM   72   C CA  . PHE   A 1 27  ? -18.377 -33.802 -37.081 1.00 41.62  ? -2   PHE   A CA  1 
ATOM   73   C C   . PHE   A 1 27  ? -18.926 -32.607 -36.325 1.00 37.02  ? -2   PHE   A C   1 
ATOM   74   O O   . PHE   A 1 27  ? -18.335 -32.177 -35.331 1.00 35.30  ? -2   PHE   A O   1 
ATOM   75   C CB  . PHE   A 1 27  ? -18.721 -35.109 -36.352 1.00 36.49  ? -2   PHE   A CB  1 
ATOM   76   C CG  . PHE   A 1 27  ? -20.196 -35.288 -36.092 1.00 36.06  ? -2   PHE   A CG  1 
ATOM   77   C CD1 . PHE   A 1 27  ? -21.037 -35.741 -37.097 1.00 36.60  ? -2   PHE   A CD1 1 
ATOM   78   C CD2 . PHE   A 1 27  ? -20.731 -35.012 -34.848 1.00 35.20  ? -2   PHE   A CD2 1 
ATOM   79   C CE1 . PHE   A 1 27  ? -22.393 -35.894 -36.866 1.00 36.30  ? -2   PHE   A CE1 1 
ATOM   80   C CE2 . PHE   A 1 27  ? -22.092 -35.168 -34.609 1.00 39.59  ? -2   PHE   A CE2 1 
ATOM   81   C CZ  . PHE   A 1 27  ? -22.918 -35.605 -35.622 1.00 35.44  ? -2   PHE   A CZ  1 
ATOM   82   N N   . GLN   A 1 28  ? -20.043 -32.058 -36.808 1.00 34.50  ? -1   GLN   A N   1 
ATOM   83   C CA  . GLN   A 1 28  ? -20.675 -30.895 -36.189 1.00 33.46  ? -1   GLN   A CA  1 
ATOM   84   C C   . GLN   A 1 28  ? -21.761 -31.413 -35.253 1.00 35.01  ? -1   GLN   A C   1 
ATOM   85   O O   . GLN   A 1 28  ? -22.750 -31.997 -35.702 1.00 33.37  ? -1   GLN   A O   1 
ATOM   86   C CB  . GLN   A 1 28  ? -21.256 -29.940 -37.238 1.00 34.06  ? -1   GLN   A CB  1 
ATOM   87   C CG  . GLN   A 1 28  ? -20.248 -28.942 -37.831 1.00 61.69  ? -1   GLN   A CG  1 
ATOM   88   C CD  . GLN   A 1 28  ? -20.825 -28.063 -38.957 1.00 71.92  ? -1   GLN   A CD  1 
ATOM   89   O OE1 . GLN   A 1 28  ? -20.724 -26.832 -38.900 1.00 71.66  ? -1   GLN   A OE1 1 
ATOM   90   N NE2 . GLN   A 1 28  ? -21.405 -28.694 -39.990 1.00 34.46  ? -1   GLN   A NE2 1 
ATOM   91   N N   . GLU   A 1 29  ? -21.561 -31.210 -33.957 1.00 32.41  ? 566  GLU   A N   1 
ATOM   92   C CA  . GLU   A 1 29  ? -22.549 -31.557 -32.951 1.00 43.76  ? 566  GLU   A CA  1 
ATOM   93   C C   . GLU   A 1 29  ? -23.682 -30.535 -32.942 1.00 33.91  ? 566  GLU   A C   1 
ATOM   94   O O   . GLU   A 1 29  ? -23.562 -29.426 -33.463 1.00 32.48  ? 566  GLU   A O   1 
ATOM   95   C CB  . GLU   A 1 29  ? -21.908 -31.616 -31.561 1.00 52.69  ? 566  GLU   A CB  1 
ATOM   96   C CG  . GLU   A 1 29  ? -20.696 -32.523 -31.470 1.00 73.86  ? 566  GLU   A CG  1 
ATOM   97   C CD  . GLU   A 1 29  ? -20.034 -32.512 -30.098 1.00 88.76  ? 566  GLU   A CD  1 
ATOM   98   O OE1 . GLU   A 1 29  ? -20.237 -31.545 -29.322 1.00 90.31  ? 566  GLU   A OE1 1 
ATOM   99   O OE2 . GLU   A 1 29  ? -19.303 -33.483 -29.805 1.00 91.29  ? 566  GLU   A OE2 1 
ATOM   100  N N   . GLN   A 1 30  ? -24.786 -30.934 -32.328 1.00 39.79  ? 567  GLN   A N   1 
ATOM   101  C CA  . GLN   A 1 30  ? -25.927 -30.050 -32.133 1.00 34.30  ? 567  GLN   A CA  1 
ATOM   102  C C   . GLN   A 1 30  ? -25.506 -28.764 -31.421 1.00 32.00  ? 567  GLN   A C   1 
ATOM   103  O O   . GLN   A 1 30  ? -24.768 -28.821 -30.428 1.00 32.32  ? 567  GLN   A O   1 
ATOM   104  C CB  . GLN   A 1 30  ? -26.981 -30.799 -31.320 1.00 42.15  ? 567  GLN   A CB  1 
ATOM   105  C CG  . GLN   A 1 30  ? -28.261 -30.053 -31.068 1.00 47.08  ? 567  GLN   A CG  1 
ATOM   106  C CD  . GLN   A 1 30  ? -29.074 -30.699 -29.967 1.00 57.13  ? 567  GLN   A CD  1 
ATOM   107  O OE1 . GLN   A 1 30  ? -28.674 -30.696 -28.800 1.00 58.64  ? 567  GLN   A OE1 1 
ATOM   108  N NE2 . GLN   A 1 30  ? -30.216 -31.271 -30.333 1.00 67.60  ? 567  GLN   A NE2 1 
ATOM   109  N N   . PRO   A 1 31  ? -25.952 -27.593 -31.882 1.00 30.67  ? 568  PRO   A N   1 
ATOM   110  C CA  . PRO   A 1 31  ? -25.581 -26.348 -31.209 1.00 29.83  ? 568  PRO   A CA  1 
ATOM   111  C C   . PRO   A 1 31  ? -26.241 -26.221 -29.849 1.00 35.91  ? 568  PRO   A C   1 
ATOM   112  O O   . PRO   A 1 31  ? -27.370 -26.658 -29.625 1.00 33.85  ? 568  PRO   A O   1 
ATOM   113  C CB  . PRO   A 1 31  ? -26.093 -25.260 -32.160 1.00 33.86  ? 568  PRO   A CB  1 
ATOM   114  C CG  . PRO   A 1 31  ? -26.477 -25.954 -33.409 1.00 35.92  ? 568  PRO   A CG  1 
ATOM   115  C CD  . PRO   A 1 31  ? -26.777 -27.354 -33.073 1.00 33.61  ? 568  PRO   A CD  1 
ATOM   116  N N   . LEU   A 1 32  ? -25.522 -25.582 -28.942 1.00 31.48  ? 569  LEU   A N   1 
ATOM   117  C CA  . LEU   A 1 32  ? -26.049 -25.250 -27.633 1.00 29.52  ? 569  LEU   A CA  1 
ATOM   118  C C   . LEU   A 1 32  ? -27.037 -24.093 -27.751 1.00 39.08  ? 569  LEU   A C   1 
ATOM   119  O O   . LEU   A 1 32  ? -26.718 -23.054 -28.337 1.00 32.96  ? 569  LEU   A O   1 
ATOM   120  C CB  . LEU   A 1 32  ? -24.888 -24.871 -26.720 1.00 34.14  ? 569  LEU   A CB  1 
ATOM   121  C CG  . LEU   A 1 32  ? -25.140 -24.638 -25.246 1.00 42.86  ? 569  LEU   A CG  1 
ATOM   122  C CD1 . LEU   A 1 32  ? -25.533 -25.942 -24.586 1.00 48.46  ? 569  LEU   A CD1 1 
ATOM   123  C CD2 . LEU   A 1 32  ? -23.862 -24.072 -24.638 1.00 45.00  ? 569  LEU   A CD2 1 
ATOM   124  N N   . ARG   A 1 33  ? -28.235 -24.264 -27.197 1.00 38.42  ? 570  ARG   A N   1 
ATOM   125  C CA  . ARG   A 1 33  ? -29.218 -23.189 -27.223 1.00 46.14  ? 570  ARG   A CA  1 
ATOM   126  C C   . ARG   A 1 33  ? -28.952 -22.212 -26.083 1.00 38.43  ? 570  ARG   A C   1 
ATOM   127  O O   . ARG   A 1 33  ? -28.697 -22.626 -24.949 1.00 35.23  ? 570  ARG   A O   1 
ATOM   128  C CB  . ARG   A 1 33  ? -30.637 -23.743 -27.123 1.00 46.45  ? 570  ARG   A CB  1 
ATOM   129  C CG  . ARG   A 1 33  ? -31.696 -22.694 -27.413 1.00 56.74  ? 570  ARG   A CG  1 
ATOM   130  C CD  . ARG   A 1 33  ? -33.016 -23.317 -27.830 1.00 64.54  ? 570  ARG   A CD  1 
ATOM   131  N NE  . ARG   A 1 33  ? -33.846 -23.675 -26.687 1.00 65.90  ? 570  ARG   A NE  1 
ATOM   132  C CZ  . ARG   A 1 33  ? -34.792 -22.890 -26.183 1.00 62.36  ? 570  ARG   A CZ  1 
ATOM   133  N NH1 . ARG   A 1 33  ? -35.030 -21.702 -26.725 1.00 52.11  ? 570  ARG   A NH1 1 
ATOM   134  N NH2 . ARG   A 1 33  ? -35.498 -23.294 -25.138 1.00 63.73  ? 570  ARG   A NH2 1 
ATOM   135  N N   . LEU   A 1 34  ? -29.020 -20.918 -26.385 1.00 30.24  ? 571  LEU   A N   1 
ATOM   136  C CA  . LEU   A 1 34  ? -28.685 -19.864 -25.441 1.00 29.60  ? 571  LEU   A CA  1 
ATOM   137  C C   . LEU   A 1 34  ? -29.862 -18.924 -25.250 1.00 28.65  ? 571  LEU   A C   1 
ATOM   138  O O   . LEU   A 1 34  ? -30.773 -18.877 -26.083 1.00 31.39  ? 571  LEU   A O   1 
ATOM   139  C CB  . LEU   A 1 34  ? -27.474 -19.046 -25.916 1.00 34.41  ? 571  LEU   A CB  1 
ATOM   140  C CG  . LEU   A 1 34  ? -26.162 -19.788 -26.156 1.00 36.40  ? 571  LEU   A CG  1 
ATOM   141  C CD1 . LEU   A 1 34  ? -25.131 -18.830 -26.727 1.00 43.78  ? 571  LEU   A CD1 1 
ATOM   142  C CD2 . LEU   A 1 34  ? -25.648 -20.416 -24.875 1.00 36.00  ? 571  LEU   A CD2 1 
ATOM   143  N N   . PRO   A 1 35  ? -29.871 -18.151 -24.167 1.00 28.59  ? 572  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 35  ? -30.876 -17.100 -24.025 1.00 30.59  ? 572  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 35  ? -30.649 -16.016 -25.060 1.00 36.19  ? 572  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 35  ? -29.610 -15.945 -25.721 1.00 32.71  ? 572  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 35  ? -30.645 -16.582 -22.603 1.00 35.58  ? 572  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 35  ? -29.193 -16.882 -22.344 1.00 31.86  ? 572  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 35  ? -28.985 -18.220 -22.991 1.00 25.88  ? 572  PRO   A CD  1 
ATOM   150  N N   . SER   A 1 36  ? -31.650 -15.161 -25.183 1.00 32.71  ? 573  SER   A N   1 
ATOM   151  C CA  . SER   A 1 36  ? -31.581 -14.037 -26.097 1.00 34.37  ? 573  SER   A CA  1 
ATOM   152  C C   . SER   A 1 36  ? -30.599 -12.980 -25.590 1.00 35.49  ? 573  SER   A C   1 
ATOM   153  O O   . SER   A 1 36  ? -30.426 -12.811 -24.382 1.00 39.30  ? 573  SER   A O   1 
ATOM   154  C CB  . SER   A 1 36  ? -32.962 -13.411 -26.255 1.00 39.94  ? 573  SER   A CB  1 
ATOM   155  O OG  . SER   A 1 36  ? -32.859 -12.096 -26.762 1.00 47.95  ? 573  SER   A OG  1 
ATOM   156  N N   . PRO   A 1 37  ? -29.937 -12.260 -26.497 1.00 33.88  ? 574  PRO   A N   1 
ATOM   157  C CA  . PRO   A 1 37  ? -29.104 -11.131 -26.061 1.00 43.46  ? 574  PRO   A CA  1 
ATOM   158  C C   . PRO   A 1 37  ? -29.906 -10.035 -25.397 1.00 46.55  ? 574  PRO   A C   1 
ATOM   159  O O   . PRO   A 1 37  ? -29.335 -9.254  -24.630 1.00 44.70  ? 574  PRO   A O   1 
ATOM   160  C CB  . PRO   A 1 37  ? -28.459 -10.637 -27.364 1.00 49.21  ? 574  PRO   A CB  1 
ATOM   161  C CG  . PRO   A 1 37  ? -28.617 -11.762 -28.330 1.00 50.04  ? 574  PRO   A CG  1 
ATOM   162  C CD  . PRO   A 1 37  ? -29.879 -12.460 -27.950 1.00 38.84  ? 574  PRO   A CD  1 
ATOM   163  N N   . GLU   A 1 38  ? -31.213 -9.951  -25.671 1.00 43.52  ? 575  GLU   A N   1 
ATOM   164  C CA  . GLU   A 1 38  ? -32.049 -8.951  -25.012 1.00 49.96  ? 575  GLU   A CA  1 
ATOM   165  C C   . GLU   A 1 38  ? -32.055 -9.140  -23.505 1.00 43.03  ? 575  GLU   A C   1 
ATOM   166  O O   . GLU   A 1 38  ? -32.231 -8.172  -22.761 1.00 49.37  ? 575  GLU   A O   1 
ATOM   167  C CB  . GLU   A 1 38  ? -33.486 -9.008  -25.551 1.00 62.23  ? 575  GLU   A CB  1 
ATOM   168  C CG  . GLU   A 1 38  ? -33.714 -8.319  -26.893 1.00 80.55  ? 575  GLU   A CG  1 
ATOM   169  C CD  . GLU   A 1 38  ? -32.853 -8.887  -28.012 1.00 95.54  ? 575  GLU   A CD  1 
ATOM   170  O OE1 . GLU   A 1 38  ? -31.879 -8.210  -28.413 1.00 97.89  ? 575  GLU   A OE1 1 
ATOM   171  O OE2 . GLU   A 1 38  ? -33.148 -10.010 -28.486 1.00 97.43  ? 575  GLU   A OE2 1 
ATOM   172  N N   . VAL   A 1 39  ? -31.863 -10.372 -23.035 1.00 35.05  ? 576  VAL   A N   1 
ATOM   173  C CA  . VAL   A 1 39  ? -31.834 -10.652 -21.604 1.00 33.29  ? 576  VAL   A CA  1 
ATOM   174  C C   . VAL   A 1 39  ? -30.445 -11.019 -21.097 1.00 40.08  ? 576  VAL   A C   1 
ATOM   175  O O   . VAL   A 1 39  ? -30.259 -11.107 -19.870 1.00 40.87  ? 576  VAL   A O   1 
ATOM   176  C CB  . VAL   A 1 39  ? -32.845 -11.751 -21.223 1.00 34.98  ? 576  VAL   A CB  1 
ATOM   177  C CG1 . VAL   A 1 39  ? -34.252 -11.304 -21.578 1.00 43.26  ? 576  VAL   A CG1 1 
ATOM   178  C CG2 . VAL   A 1 39  ? -32.512 -13.081 -21.913 1.00 33.88  ? 576  VAL   A CG2 1 
ATOM   179  N N   . TYR   A 1 40  ? -29.458 -11.211 -21.982 1.00 34.96  ? 577  TYR   A N   1 
ATOM   180  C CA  . TYR   A 1 40  ? -28.115 -11.581 -21.530 1.00 28.26  ? 577  TYR   A CA  1 
ATOM   181  C C   . TYR   A 1 40  ? -27.125 -11.145 -22.617 1.00 32.14  ? 577  TYR   A C   1 
ATOM   182  O O   . TYR   A 1 40  ? -26.991 -11.817 -23.647 1.00 34.96  ? 577  TYR   A O   1 
ATOM   183  C CB  . TYR   A 1 40  ? -28.037 -13.072 -21.235 1.00 27.62  ? 577  TYR   A CB  1 
ATOM   184  C CG  . TYR   A 1 40  ? -26.748 -13.539 -20.574 1.00 27.42  ? 577  TYR   A CG  1 
ATOM   185  C CD1 . TYR   A 1 40  ? -26.411 -13.144 -19.279 1.00 28.64  ? 577  TYR   A CD1 1 
ATOM   186  C CD2 . TYR   A 1 40  ? -25.887 -14.415 -21.230 1.00 31.28  ? 577  TYR   A CD2 1 
ATOM   187  C CE1 . TYR   A 1 40  ? -25.227 -13.588 -18.662 1.00 28.77  ? 577  TYR   A CE1 1 
ATOM   188  C CE2 . TYR   A 1 40  ? -24.695 -14.864 -20.620 1.00 25.24  ? 577  TYR   A CE2 1 
ATOM   189  C CZ  . TYR   A 1 40  ? -24.373 -14.442 -19.346 1.00 28.64  ? 577  TYR   A CZ  1 
ATOM   190  O OH  . TYR   A 1 40  ? -23.203 -14.888 -18.751 1.00 25.84  ? 577  TYR   A OH  1 
ATOM   191  N N   . ARG   A 1 41  ? -26.445 -10.023 -22.362 1.00 30.66  ? 578  ARG   A N   1 
ATOM   192  C CA  . ARG   A 1 41  ? -25.664 -9.331  -23.384 1.00 39.96  ? 578  ARG   A CA  1 
ATOM   193  C C   . ARG   A 1 41  ? -24.598 -10.220 -23.995 1.00 35.44  ? 578  ARG   A C   1 
ATOM   194  O O   . ARG   A 1 41  ? -24.202 -10.013 -25.149 1.00 33.34  ? 578  ARG   A O   1 
ATOM   195  C CB  . ARG   A 1 41  ? -24.975 -8.101  -22.785 1.00 37.94  ? 578  ARG   A CB  1 
ATOM   196  C CG  . ARG   A 1 41  ? -25.873 -6.935  -22.546 1.00 51.43  ? 578  ARG   A CG  1 
ATOM   197  C CD  . ARG   A 1 41  ? -25.048 -5.671  -22.468 1.00 46.13  ? 578  ARG   A CD  1 
ATOM   198  N NE  . ARG   A 1 41  ? -24.308 -5.574  -21.217 1.00 38.93  ? 578  ARG   A NE  1 
ATOM   199  C CZ  . ARG   A 1 41  ? -23.442 -4.603  -20.944 1.00 42.53  ? 578  ARG   A CZ  1 
ATOM   200  N NH1 . ARG   A 1 41  ? -22.818 -4.575  -19.775 1.00 43.87  ? 578  ARG   A NH1 1 
ATOM   201  N NH2 . ARG   A 1 41  ? -23.190 -3.666  -21.849 1.00 40.63  ? 578  ARG   A NH2 1 
ATOM   202  N N   . PHE   A 1 42  ? -24.094 -11.184 -23.231 1.00 31.69  ? 579  PHE   A N   1 
ATOM   203  C CA  . PHE   A 1 42  ? -22.841 -11.834 -23.592 1.00 31.18  ? 579  PHE   A CA  1 
ATOM   204  C C   . PHE   A 1 42  ? -22.981 -12.851 -24.711 1.00 42.69  ? 579  PHE   A C   1 
ATOM   205  O O   . PHE   A 1 42  ? -21.961 -13.307 -25.233 1.00 50.20  ? 579  PHE   A O   1 
ATOM   206  C CB  . PHE   A 1 42  ? -22.240 -12.502 -22.357 1.00 31.96  ? 579  PHE   A CB  1 
ATOM   207  C CG  . PHE   A 1 42  ? -21.962 -11.545 -21.248 1.00 32.44  ? 579  PHE   A CG  1 
ATOM   208  C CD1 . PHE   A 1 42  ? -20.755 -10.877 -21.179 1.00 28.62  ? 579  PHE   A CD1 1 
ATOM   209  C CD2 . PHE   A 1 42  ? -22.921 -11.293 -20.282 1.00 27.74  ? 579  PHE   A CD2 1 
ATOM   210  C CE1 . PHE   A 1 42  ? -20.511 -9.967  -20.162 1.00 30.69  ? 579  PHE   A CE1 1 
ATOM   211  C CE2 . PHE   A 1 42  ? -22.685 -10.393 -19.258 1.00 27.35  ? 579  PHE   A CE2 1 
ATOM   212  C CZ  . PHE   A 1 42  ? -21.471 -9.732  -19.193 1.00 29.09  ? 579  PHE   A CZ  1 
ATOM   213  N N   . VAL   A 1 43  ? -24.198 -13.203 -25.117 1.00 34.11  ? 580  VAL   A N   1 
ATOM   214  C CA  . VAL   A 1 43  ? -24.335 -14.269 -26.102 1.00 36.62  ? 580  VAL   A CA  1 
ATOM   215  C C   . VAL   A 1 43  ? -24.467 -13.712 -27.517 1.00 38.02  ? 580  VAL   A C   1 
ATOM   216  O O   . VAL   A 1 43  ? -24.684 -14.474 -28.464 1.00 41.92  ? 580  VAL   A O   1 
ATOM   217  C CB  . VAL   A 1 43  ? -25.514 -15.191 -25.748 1.00 39.81  ? 580  VAL   A CB  1 
ATOM   218  C CG1 . VAL   A 1 43  ? -25.205 -15.933 -24.460 1.00 45.94  ? 580  VAL   A CG1 1 
ATOM   219  C CG2 . VAL   A 1 43  ? -26.793 -14.400 -25.605 1.00 38.23  ? 580  VAL   A CG2 1 
ATOM   220  N N   . VAL   A 1 44  ? -24.309 -12.392 -27.678 1.00 35.39  ? 581  VAL   A N   1 
ATOM   221  C CA  . VAL   A 1 44  ? -24.268 -11.807 -29.018 1.00 38.57  ? 581  VAL   A CA  1 
ATOM   222  C C   . VAL   A 1 44  ? -23.176 -12.491 -29.834 1.00 40.14  ? 581  VAL   A C   1 
ATOM   223  O O   . VAL   A 1 44  ? -22.081 -12.755 -29.329 1.00 38.53  ? 581  VAL   A O   1 
ATOM   224  C CB  . VAL   A 1 44  ? -24.028 -10.288 -28.942 1.00 41.17  ? 581  VAL   A CB  1 
ATOM   225  C CG1 . VAL   A 1 44  ? -23.780 -9.715  -30.326 1.00 50.36  ? 581  VAL   A CG1 1 
ATOM   226  C CG2 . VAL   A 1 44  ? -25.215 -9.584  -28.302 1.00 54.09  ? 581  VAL   A CG2 1 
ATOM   227  N N   . LYS   A 1 45  ? -23.470 -12.793 -31.102 1.00 41.85  ? 582  LYS   A N   1 
ATOM   228  C CA  . LYS   A 1 45  ? -22.501 -13.493 -31.947 1.00 34.16  ? 582  LYS   A CA  1 
ATOM   229  C C   . LYS   A 1 45  ? -21.206 -12.696 -32.093 1.00 37.07  ? 582  LYS   A C   1 
ATOM   230  O O   . LYS   A 1 45  ? -21.234 -11.473 -32.240 1.00 35.15  ? 582  LYS   A O   1 
ATOM   231  C CB  . LYS   A 1 45  ? -23.095 -13.757 -33.334 1.00 42.99  ? 582  LYS   A CB  1 
ATOM   232  C CG  . LYS   A 1 45  ? -22.186 -14.586 -34.239 1.00 57.22  ? 582  LYS   A CG  1 
ATOM   233  C CD  . LYS   A 1 45  ? -22.800 -14.839 -35.610 1.00 62.08  ? 582  LYS   A CD  1 
ATOM   234  C CE  . LYS   A 1 45  ? -21.847 -15.630 -36.502 1.00 61.74  ? 582  LYS   A CE  1 
ATOM   235  N NZ  . LYS   A 1 45  ? -20.616 -14.861 -36.820 1.00 63.21  ? 582  LYS   A NZ  1 
ATOM   236  N N   . ASP   A 1 46  ? -20.068 -13.401 -32.052 1.00 37.00  ? 583  ASP   A N   1 
ATOM   237  C CA  . ASP   A 1 46  ? -18.778 -12.774 -32.318 1.00 37.41  ? 583  ASP   A CA  1 
ATOM   238  C C   . ASP   A 1 46  ? -18.775 -12.190 -33.725 1.00 40.95  ? 583  ASP   A C   1 
ATOM   239  O O   . ASP   A 1 46  ? -19.349 -12.768 -34.652 1.00 44.06  ? 583  ASP   A O   1 
ATOM   240  C CB  . ASP   A 1 46  ? -17.633 -13.793 -32.197 1.00 41.56  ? 583  ASP   A CB  1 
ATOM   241  C CG  . ASP   A 1 46  ? -17.359 -14.238 -30.762 1.00 43.40  ? 583  ASP   A CG  1 
ATOM   242  O OD1 . ASP   A 1 46  ? -17.935 -13.668 -29.809 1.00 40.76  ? 583  ASP   A OD1 1 
ATOM   243  O OD2 . ASP   A 1 46  ? -16.554 -15.174 -30.589 1.00 46.17  ? 583  ASP   A OD2 1 
ATOM   244  N N   . SER   A 1 47  ? -18.133 -11.036 -33.884 1.00 48.37  ? 584  SER   A N   1 
ATOM   245  C CA  . SER   A 1 47  ? -17.928 -10.467 -35.210 1.00 41.71  ? 584  SER   A CA  1 
ATOM   246  C C   . SER   A 1 47  ? -16.767 -9.489  -35.147 1.00 48.23  ? 584  SER   A C   1 
ATOM   247  O O   . SER   A 1 47  ? -16.320 -9.081  -34.069 1.00 48.23  ? 584  SER   A O   1 
ATOM   248  C CB  . SER   A 1 47  ? -19.185 -9.762  -35.737 1.00 42.44  ? 584  SER   A CB  1 
ATOM   249  O OG  . SER   A 1 47  ? -19.276 -8.449  -35.204 1.00 41.50  ? 584  SER   A OG  1 
ATOM   250  N N   . GLU   A 1 48  ? -16.299 -9.098  -36.330 1.00 44.95  ? 585  GLU   A N   1 
ATOM   251  C CA  . GLU   A 1 48  ? -15.290 -8.051  -36.427 1.00 57.22  ? 585  GLU   A CA  1 
ATOM   252  C C   . GLU   A 1 48  ? -15.727 -6.771  -35.733 1.00 52.01  ? 585  GLU   A C   1 
ATOM   253  O O   . GLU   A 1 48  ? -14.878 -5.948  -35.379 1.00 49.71  ? 585  GLU   A O   1 
ATOM   254  C CB  . GLU   A 1 48  ? -14.976 -7.759  -37.897 1.00 69.22  ? 585  GLU   A CB  1 
ATOM   255  C CG  . GLU   A 1 48  ? -14.467 -8.967  -38.668 1.00 87.64  ? 585  GLU   A CG  1 
ATOM   256  C CD  . GLU   A 1 48  ? -13.083 -9.403  -38.221 1.00 98.34  ? 585  GLU   A CD  1 
ATOM   257  O OE1 . GLU   A 1 48  ? -12.193 -8.533  -38.114 1.00 102.59 ? 585  GLU   A OE1 1 
ATOM   258  O OE2 . GLU   A 1 48  ? -12.887 -10.612 -37.970 1.00 101.40 ? 585  GLU   A OE2 1 
ATOM   259  N N   . GLU   A 1 49  ? -17.026 -6.585  -35.521 1.00 50.10  ? 586  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 49  ? -17.520 -5.375  -34.886 1.00 47.43  ? 586  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 49  ? -17.521 -5.456  -33.364 1.00 38.08  ? 586  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 49  ? -17.819 -4.449  -32.712 1.00 36.37  ? 586  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 49  ? -18.927 -5.042  -35.396 1.00 51.26  ? 586  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 49  ? -19.109 -5.256  -36.900 1.00 59.34  ? 586  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 49  ? -17.994 -4.638  -37.738 1.00 71.27  ? 586  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 49  ? -17.580 -3.492  -37.451 1.00 76.15  ? 586  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 49  ? -17.527 -5.307  -38.686 1.00 75.83  ? 586  GLU   A OE2 1 
ATOM   268  N N   . ASN   A 1 50  ? -17.175 -6.606  -32.775 1.00 39.90  ? 587  ASN   A N   1 
ATOM   269  C CA  . ASN   A 1 50  ? -17.101 -6.660  -31.316 1.00 38.80  ? 587  ASN   A CA  1 
ATOM   270  C C   . ASN   A 1 50  ? -15.938 -7.461  -30.735 1.00 36.74  ? 587  ASN   A C   1 
ATOM   271  O O   . ASN   A 1 50  ? -15.701 -7.334  -29.532 1.00 38.36  ? 587  ASN   A O   1 
ATOM   272  C CB  . ASN   A 1 50  ? -18.421 -7.195  -30.734 1.00 34.52  ? 587  ASN   A CB  1 
ATOM   273  C CG  . ASN   A 1 50  ? -18.805 -8.545  -31.293 1.00 39.88  ? 587  ASN   A CG  1 
ATOM   274  O OD1 . ASN   A 1 50  ? -17.945 -9.386  -31.564 1.00 34.67  ? 587  ASN   A OD1 1 
ATOM   275  N ND2 . ASN   A 1 50  ? -20.111 -8.761  -31.484 1.00 40.67  ? 587  ASN   A ND2 1 
ATOM   276  N N   . ILE   A 1 51  ? -15.205 -8.262  -31.508 1.00 34.17  ? 588  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 51  ? -14.022 -8.945  -30.979 1.00 37.37  ? 588  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 51  ? -13.103 -9.312  -32.140 1.00 44.35  ? 588  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 51  ? -13.558 -9.769  -33.191 1.00 42.65  ? 588  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 51  ? -14.412 -10.191 -30.145 1.00 39.65  ? 588  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 51  ? -13.169 -10.813 -29.507 1.00 39.40  ? 588  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 51  ? -15.158 -11.226 -30.993 1.00 36.04  ? 588  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 51  ? -13.490 -11.819 -28.434 1.00 41.85  ? 588  ILE   A CD1 1 
ATOM   284  N N   . VAL   A 1 52  ? -11.797 -9.098  -31.950 1.00 42.95  ? 589  VAL   A N   1 
ATOM   285  C CA  . VAL   A 1 52  ? -10.821 -9.445  -32.976 1.00 38.37  ? 589  VAL   A CA  1 
ATOM   286  C C   . VAL   A 1 52  ? -9.661  -10.181 -32.328 1.00 39.18  ? 589  VAL   A C   1 
ATOM   287  O O   . VAL   A 1 52  ? -9.272  -9.896  -31.189 1.00 39.86  ? 589  VAL   A O   1 
ATOM   288  C CB  . VAL   A 1 52  ? -10.316 -8.219  -33.771 1.00 43.37  ? 589  VAL   A CB  1 
ATOM   289  C CG1 . VAL   A 1 52  ? -11.461 -7.581  -34.537 1.00 53.61  ? 589  VAL   A CG1 1 
ATOM   290  C CG2 . VAL   A 1 52  ? -9.663  -7.218  -32.855 1.00 43.33  ? 589  VAL   A CG2 1 
ATOM   291  N N   . PHE   A 1 53  ? -9.113  -11.140 -33.068 1.00 33.81  ? 590  PHE   A N   1 
ATOM   292  C CA  . PHE   A 1 53  ? -8.059  -12.013 -32.579 1.00 43.57  ? 590  PHE   A CA  1 
ATOM   293  C C   . PHE   A 1 53  ? -6.773  -11.769 -33.355 1.00 47.11  ? 590  PHE   A C   1 
ATOM   294  O O   . PHE   A 1 53  ? -6.798  -11.314 -34.501 1.00 51.34  ? 590  PHE   A O   1 
ATOM   295  C CB  . PHE   A 1 53  ? -8.472  -13.485 -32.698 1.00 46.51  ? 590  PHE   A CB  1 
ATOM   296  C CG  . PHE   A 1 53  ? -9.726  -13.818 -31.932 1.00 38.50  ? 590  PHE   A CG  1 
ATOM   297  C CD1 . PHE   A 1 53  ? -10.976 -13.681 -32.520 1.00 39.64  ? 590  PHE   A CD1 1 
ATOM   298  C CD2 . PHE   A 1 53  ? -9.651  -14.243 -30.616 1.00 43.41  ? 590  PHE   A CD2 1 
ATOM   299  C CE1 . PHE   A 1 53  ? -12.125 -13.971 -31.812 1.00 43.03  ? 590  PHE   A CE1 1 
ATOM   300  C CE2 . PHE   A 1 53  ? -10.796 -14.537 -29.905 1.00 42.94  ? 590  PHE   A CE2 1 
ATOM   301  C CZ  . PHE   A 1 53  ? -12.035 -14.405 -30.503 1.00 39.61  ? 590  PHE   A CZ  1 
ATOM   302  N N   . GLU   A 1 54  ? -5.647  -12.065 -32.706 1.00 44.57  ? 591  GLU   A N   1 
ATOM   303  C CA  . GLU   A 1 54  ? -4.361  -12.068 -33.389 1.00 44.68  ? 591  GLU   A CA  1 
ATOM   304  C C   . GLU   A 1 54  ? -4.324  -13.283 -34.306 1.00 58.66  ? 591  GLU   A C   1 
ATOM   305  O O   . GLU   A 1 54  ? -3.854  -14.354 -33.912 1.00 68.40  ? 591  GLU   A O   1 
ATOM   306  C CB  . GLU   A 1 54  ? -3.203  -12.086 -32.387 1.00 46.02  ? 591  GLU   A CB  1 
ATOM   307  C CG  . GLU   A 1 54  ? -3.119  -10.853 -31.473 1.00 46.22  ? 591  GLU   A CG  1 
ATOM   308  C CD  . GLU   A 1 54  ? -2.572  -9.605  -32.165 1.00 53.19  ? 591  GLU   A CD  1 
ATOM   309  O OE1 . GLU   A 1 54  ? -2.284  -8.607  -31.466 1.00 48.63  ? 591  GLU   A OE1 1 
ATOM   310  O OE2 . GLU   A 1 54  ? -2.427  -9.616  -33.404 1.00 56.24  ? 591  GLU   A OE2 1 
ATOM   311  N N   . ASP   A 1 55  ? -4.850  -13.136 -35.520 1.00 57.86  ? 592  ASP   A N   1 
ATOM   312  C CA  . ASP   A 1 55  ? -4.958  -14.278 -36.420 1.00 63.81  ? 592  ASP   A CA  1 
ATOM   313  C C   . ASP   A 1 55  ? -3.632  -14.594 -37.091 1.00 63.31  ? 592  ASP   A C   1 
ATOM   314  O O   . ASP   A 1 55  ? -3.427  -15.721 -37.557 1.00 62.20  ? 592  ASP   A O   1 
ATOM   315  C CB  . ASP   A 1 55  ? -6.041  -14.013 -37.460 1.00 69.76  ? 592  ASP   A CB  1 
ATOM   316  C CG  . ASP   A 1 55  ? -7.411  -13.894 -36.833 1.00 74.59  ? 592  ASP   A CG  1 
ATOM   317  O OD1 . ASP   A 1 55  ? -7.833  -14.855 -36.157 1.00 75.95  ? 592  ASP   A OD1 1 
ATOM   318  O OD2 . ASP   A 1 55  ? -8.053  -12.838 -36.992 1.00 79.03  ? 592  ASP   A OD2 1 
ATOM   319  N N   . ASN   A 1 56  ? -2.679  -13.688 -36.998 1.00 66.29  ? 593  ASN   A N   1 
ATOM   320  C CA  . ASN   A 1 56  ? -1.374  -14.022 -37.610 1.00 82.56  ? 593  ASN   A CA  1 
ATOM   321  C C   . ASN   A 1 56  ? -0.490  -14.644 -36.534 1.00 80.33  ? 593  ASN   A C   1 
ATOM   322  O O   . ASN   A 1 56  ? 0.606   -15.066 -36.834 1.00 78.60  ? 593  ASN   A O   1 
ATOM   323  C CB  . ASN   A 1 56  ? -0.774  -12.851 -38.382 1.00 92.32  ? 593  ASN   A CB  1 
ATOM   324  C CG  . ASN   A 1 56  ? 0.388   -13.286 -39.241 1.00 100.27 ? 593  ASN   A CG  1 
ATOM   325  O OD1 . ASN   A 1 56  ? 0.373   -14.368 -39.819 1.00 89.23  ? 593  ASN   A OD1 1 
ATOM   326  N ND2 . ASN   A 1 56  ? 1.422   -12.465 -39.287 1.00 103.97 ? 593  ASN   A ND2 1 
ATOM   327  N N   . LEU   A 1 57  ? -0.993  -14.691 -35.310 1.00 77.67  ? 594  LEU   A N   1 
ATOM   328  C CA  . LEU   A 1 57  ? -0.232  -15.264 -34.209 1.00 77.94  ? 594  LEU   A CA  1 
ATOM   329  C C   . LEU   A 1 57  ? -0.903  -16.540 -33.729 1.00 82.86  ? 594  LEU   A C   1 
ATOM   330  O O   . LEU   A 1 57  ? -2.117  -16.728 -33.877 1.00 84.40  ? 594  LEU   A O   1 
ATOM   331  C CB  . LEU   A 1 57  ? -0.112  -14.267 -33.029 1.00 68.34  ? 594  LEU   A CB  1 
ATOM   332  C CG  . LEU   A 1 57  ? 0.810   -13.069 -33.255 1.00 64.04  ? 594  LEU   A CG  1 
ATOM   333  C CD1 . LEU   A 1 57  ? 0.985   -12.309 -31.944 1.00 61.71  ? 594  LEU   A CD1 1 
ATOM   334  C CD2 . LEU   A 1 57  ? 2.143   -13.537 -33.802 1.00 62.93  ? 594  LEU   A CD2 1 
ATOM   335  N N   . GLN   A 1 58  ? -0.096  -17.404 -33.145 1.00 86.53  ? 595  GLN   A N   1 
ATOM   336  C CA  . GLN   A 1 58  ? -0.566  -18.698 -32.686 1.00 88.43  ? 595  GLN   A CA  1 
ATOM   337  C C   . GLN   A 1 58  ? -0.583  -18.808 -31.168 1.00 88.44  ? 595  GLN   A C   1 
ATOM   338  O O   . GLN   A 1 58  ? 0.477   -18.850 -30.544 1.00 88.97  ? 595  GLN   A O   1 
ATOM   339  C CB  . GLN   A 1 58  ? 0.327   -19.774 -33.270 1.00 84.84  ? 595  GLN   A CB  1 
ATOM   340  C CG  . GLN   A 1 58  ? -0.421  -20.897 -33.957 1.00 86.67  ? 595  GLN   A CG  1 
ATOM   341  C CD  . GLN   A 1 58  ? 0.521   -21.863 -34.665 1.00 93.29  ? 595  GLN   A CD  1 
ATOM   342  O OE1 . GLN   A 1 58  ? 1.708   -21.563 -34.843 1.00 102.27 ? 595  GLN   A OE1 1 
ATOM   343  N NE2 . GLN   A 1 58  ? 0.003   -23.028 -35.069 1.00 85.72  ? 595  GLN   A NE2 1 
ATOM   344  N N   . GLY   A 1 62  ? -2.753  -22.966 -27.903 1.00 60.18  ? 599  GLY   A N   1 
ATOM   345  C CA  . GLY   A 1 62  ? -3.978  -23.361 -28.571 1.00 54.08  ? 599  GLY   A CA  1 
ATOM   346  C C   . GLY   A 1 62  ? -5.082  -22.326 -28.471 1.00 51.81  ? 599  GLY   A C   1 
ATOM   347  O O   . GLY   A 1 62  ? -5.891  -22.188 -29.386 1.00 56.68  ? 599  GLY   A O   1 
ATOM   348  N N   . ILE   A 1 63  ? -5.111  -21.603 -27.357 1.00 52.24  ? 600  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 63  ? -6.127  -20.562 -27.144 1.00 48.76  ? 600  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 63  ? -5.902  -19.433 -28.141 1.00 44.53  ? 600  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 63  ? -4.763  -18.952 -28.281 1.00 47.87  ? 600  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 63  ? -6.059  -20.034 -25.708 1.00 45.49  ? 600  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 63  ? -6.428  -21.116 -24.702 1.00 50.08  ? 600  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 63  ? -6.978  -18.834 -25.532 1.00 52.76  ? 600  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 63  ? -6.198  -20.681 -23.270 1.00 52.38  ? 600  ILE   A CD1 1 
ATOM   356  N N   . PRO   A 1 64  ? -6.934  -18.973 -28.840 1.00 40.95  ? 601  PRO   A N   1 
ATOM   357  C CA  . PRO   A 1 64  ? -6.768  -17.792 -29.693 1.00 46.45  ? 601  PRO   A CA  1 
ATOM   358  C C   . PRO   A 1 64  ? -6.366  -16.584 -28.858 1.00 48.10  ? 601  PRO   A C   1 
ATOM   359  O O   . PRO   A 1 64  ? -6.783  -16.433 -27.710 1.00 48.55  ? 601  PRO   A O   1 
ATOM   360  C CB  . PRO   A 1 64  ? -8.151  -17.616 -30.333 1.00 47.87  ? 601  PRO   A CB  1 
ATOM   361  C CG  . PRO   A 1 64  ? -9.097  -18.421 -29.461 1.00 45.17  ? 601  PRO   A CG  1 
ATOM   362  C CD  . PRO   A 1 64  ? -8.283  -19.554 -28.935 1.00 41.37  ? 601  PRO   A CD  1 
ATOM   363  N N   . ILE   A 1 65  ? -5.517  -15.739 -29.432 1.00 40.48  ? 602  ILE   A N   1 
ATOM   364  C CA  . ILE   A 1 65  ? -5.004  -14.565 -28.736 1.00 37.88  ? 602  ILE   A CA  1 
ATOM   365  C C   . ILE   A 1 65  ? -5.912  -13.389 -29.057 1.00 40.13  ? 602  ILE   A C   1 
ATOM   366  O O   . ILE   A 1 65  ? -6.105  -13.046 -30.227 1.00 40.87  ? 602  ILE   A O   1 
ATOM   367  C CB  . ILE   A 1 65  ? -3.557  -14.261 -29.148 1.00 40.30  ? 602  ILE   A CB  1 
ATOM   368  C CG1 . ILE   A 1 65  ? -2.652  -15.444 -28.823 1.00 40.66  ? 602  ILE   A CG1 1 
ATOM   369  C CG2 . ILE   A 1 65  ? -3.065  -13.014 -28.434 1.00 39.88  ? 602  ILE   A CG2 1 
ATOM   370  C CD1 . ILE   A 1 65  ? -1.363  -15.463 -29.659 1.00 49.34  ? 602  ILE   A CD1 1 
ATOM   371  N N   . ILE   A 1 66  ? -6.465  -12.765 -28.023 1.00 36.63  ? 603  ILE   A N   1 
ATOM   372  C CA  . ILE   A 1 66  ? -7.381  -11.653 -28.233 1.00 34.99  ? 603  ILE   A CA  1 
ATOM   373  C C   . ILE   A 1 66  ? -6.589  -10.404 -28.582 1.00 39.88  ? 603  ILE   A C   1 
ATOM   374  O O   . ILE   A 1 66  ? -5.636  -10.039 -27.883 1.00 41.98  ? 603  ILE   A O   1 
ATOM   375  C CB  . ILE   A 1 66  ? -8.258  -11.435 -26.995 1.00 37.57  ? 603  ILE   A CB  1 
ATOM   376  C CG1 . ILE   A 1 66  ? -9.216  -12.608 -26.846 1.00 38.49  ? 603  ILE   A CG1 1 
ATOM   377  C CG2 . ILE   A 1 66  ? -9.026  -10.121 -27.108 1.00 39.52  ? 603  ILE   A CG2 1 
ATOM   378  C CD1 . ILE   A 1 66  ? -9.848  -12.682 -25.494 1.00 39.82  ? 603  ILE   A CD1 1 
ATOM   379  N N   . LYS   A 1 67  ? -6.959  -9.768  -29.690 1.00 37.62  ? 604  LYS   A N   1 
ATOM   380  C CA  . LYS   A 1 67  ? -6.367  -8.504  -30.101 1.00 35.36  ? 604  LYS   A CA  1 
ATOM   381  C C   . LYS   A 1 67  ? -7.154  -7.328  -29.526 1.00 42.73  ? 604  LYS   A C   1 
ATOM   382  O O   . LYS   A 1 67  ? -6.576  -6.366  -29.003 1.00 35.98  ? 604  LYS   A O   1 
ATOM   383  C CB  . LYS   A 1 67  ? -6.316  -8.440  -31.632 1.00 39.83  ? 604  LYS   A CB  1 
ATOM   384  C CG  . LYS   A 1 67  ? -5.657  -7.204  -32.191 1.00 44.67  ? 604  LYS   A CG  1 
ATOM   385  C CD  . LYS   A 1 67  ? -5.676  -7.209  -33.713 1.00 50.38  ? 604  LYS   A CD  1 
ATOM   386  C CE  . LYS   A 1 67  ? -5.236  -5.868  -34.267 1.00 56.47  ? 604  LYS   A CE  1 
ATOM   387  N NZ  . LYS   A 1 67  ? -5.610  -5.711  -35.704 1.00 65.90  ? 604  LYS   A NZ  1 
ATOM   388  N N   . GLY   A 1 68  ? -8.475  -7.399  -29.599 1.00 38.19  ? 605  GLY   A N   1 
ATOM   389  C CA  . GLY   A 1 68  ? -9.296  -6.357  -29.011 1.00 32.95  ? 605  GLY   A CA  1 
ATOM   390  C C   . GLY   A 1 68  ? -10.752 -6.761  -29.018 1.00 34.23  ? 605  GLY   A C   1 
ATOM   391  O O   . GLY   A 1 68  ? -11.138 -7.785  -29.585 1.00 39.34  ? 605  GLY   A O   1 
ATOM   392  N N   . GLY   A 1 69  ? -11.563 -5.939  -28.370 1.00 32.95  ? 606  GLY   A N   1 
ATOM   393  C CA  . GLY   A 1 69  ? -12.991 -6.181  -28.386 1.00 33.75  ? 606  GLY   A CA  1 
ATOM   394  C C   . GLY   A 1 69  ? -13.684 -5.150  -27.535 1.00 32.59  ? 606  GLY   A C   1 
ATOM   395  O O   . GLY   A 1 69  ? -13.044 -4.330  -26.875 1.00 34.33  ? 606  GLY   A O   1 
ATOM   396  N N   . THR   A 1 70  ? -15.016 -5.197  -27.568 1.00 32.27  ? 607  THR   A N   1 
ATOM   397  C CA  . THR   A 1 70  ? -15.783 -4.441  -26.599 1.00 33.49  ? 607  THR   A CA  1 
ATOM   398  C C   . THR   A 1 70  ? -15.545 -5.025  -25.212 1.00 30.70  ? 607  THR   A C   1 
ATOM   399  O O   . THR   A 1 70  ? -15.155 -6.183  -25.063 1.00 30.65  ? 607  THR   A O   1 
ATOM   400  C CB  . THR   A 1 70  ? -17.270 -4.477  -26.946 1.00 34.29  ? 607  THR   A CB  1 
ATOM   401  O OG1 . THR   A 1 70  ? -17.758 -5.822  -26.818 1.00 35.78  ? 607  THR   A OG1 1 
ATOM   402  C CG2 . THR   A 1 70  ? -17.479 -4.008  -28.372 1.00 36.15  ? 607  THR   A CG2 1 
ATOM   403  N N   . VAL   A 1 71  ? -15.778 -4.208  -24.183 1.00 27.41  ? 608  VAL   A N   1 
ATOM   404  C CA  . VAL   A 1 71  ? -15.524 -4.706  -22.838 1.00 27.68  ? 608  VAL   A CA  1 
ATOM   405  C C   . VAL   A 1 71  ? -16.431 -5.887  -22.534 1.00 31.44  ? 608  VAL   A C   1 
ATOM   406  O O   . VAL   A 1 71  ? -16.029 -6.821  -21.823 1.00 33.30  ? 608  VAL   A O   1 
ATOM   407  C CB  . VAL   A 1 71  ? -15.667 -3.585  -21.789 1.00 31.11  ? 608  VAL   A CB  1 
ATOM   408  C CG1 . VAL   A 1 71  ? -17.129 -3.212  -21.580 1.00 31.75  ? 608  VAL   A CG1 1 
ATOM   409  C CG2 . VAL   A 1 71  ? -15.032 -4.026  -20.469 1.00 29.66  ? 608  VAL   A CG2 1 
ATOM   410  N N   . VAL   A 1 72  ? -17.641 -5.899  -23.101 1.00 30.71  ? 609  VAL   A N   1 
ATOM   411  C CA  . VAL   A 1 72  ? -18.529 -7.044  -22.917 1.00 31.75  ? 609  VAL   A CA  1 
ATOM   412  C C   . VAL   A 1 72  ? -17.898 -8.307  -23.487 1.00 29.01  ? 609  VAL   A C   1 
ATOM   413  O O   . VAL   A 1 72  ? -17.925 -9.370  -22.856 1.00 30.72  ? 609  VAL   A O   1 
ATOM   414  C CB  . VAL   A 1 72  ? -19.909 -6.763  -23.543 1.00 35.36  ? 609  VAL   A CB  1 
ATOM   415  C CG1 . VAL   A 1 72  ? -20.655 -8.070  -23.810 1.00 31.36  ? 609  VAL   A CG1 1 
ATOM   416  C CG2 . VAL   A 1 72  ? -20.722 -5.865  -22.627 1.00 35.11  ? 609  VAL   A CG2 1 
ATOM   417  N N   . LYS   A 1 73  ? -17.306 -8.219  -24.680 1.00 24.68  ? 610  LYS   A N   1 
ATOM   418  C CA  . LYS   A 1 73  ? -16.683 -9.417  -25.243 1.00 29.21  ? 610  LYS   A CA  1 
ATOM   419  C C   . LYS   A 1 73  ? -15.426 -9.803  -24.474 1.00 29.03  ? 610  LYS   A C   1 
ATOM   420  O O   . LYS   A 1 73  ? -15.137 -10.997 -24.302 1.00 26.22  ? 610  LYS   A O   1 
ATOM   421  C CB  . LYS   A 1 73  ? -16.365 -9.213  -26.724 1.00 35.11  ? 610  LYS   A CB  1 
ATOM   422  C CG  . LYS   A 1 73  ? -17.560 -9.444  -27.636 1.00 40.78  ? 610  LYS   A CG  1 
ATOM   423  C CD  . LYS   A 1 73  ? -17.939 -10.917 -27.657 1.00 39.01  ? 610  LYS   A CD  1 
ATOM   424  C CE  . LYS   A 1 73  ? -19.298 -11.119 -28.323 1.00 40.52  ? 610  LYS   A CE  1 
ATOM   425  N NZ  . LYS   A 1 73  ? -19.756 -12.527 -28.176 1.00 36.67  ? 610  LYS   A NZ  1 
ATOM   426  N N   . LEU   A 1 74  ? -14.660 -8.814  -23.997 1.00 30.93  ? 611  LEU   A N   1 
ATOM   427  C CA  . LEU   A 1 74  ? -13.491 -9.152  -23.190 1.00 29.69  ? 611  LEU   A CA  1 
ATOM   428  C C   . LEU   A 1 74  ? -13.914 -9.888  -21.923 1.00 27.59  ? 611  LEU   A C   1 
ATOM   429  O O   . LEU   A 1 74  ? -13.277 -10.868 -21.523 1.00 27.12  ? 611  LEU   A O   1 
ATOM   430  C CB  . LEU   A 1 74  ? -12.675 -7.899  -22.845 1.00 27.46  ? 611  LEU   A CB  1 
ATOM   431  C CG  . LEU   A 1 74  ? -12.075 -7.088  -23.994 1.00 28.80  ? 611  LEU   A CG  1 
ATOM   432  C CD1 . LEU   A 1 74  ? -11.324 -5.827  -23.491 1.00 30.42  ? 611  LEU   A CD1 1 
ATOM   433  C CD2 . LEU   A 1 74  ? -11.164 -7.943  -24.855 1.00 29.65  ? 611  LEU   A CD2 1 
ATOM   434  N N   . ILE   A 1 75  ? -15.009 -9.451  -21.298 1.00 24.55  ? 612  ILE   A N   1 
ATOM   435  C CA  . ILE   A 1 75  ? -15.499 -10.140 -20.104 1.00 28.73  ? 612  ILE   A CA  1 
ATOM   436  C C   . ILE   A 1 75  ? -15.966 -11.550 -20.442 1.00 26.50  ? 612  ILE   A C   1 
ATOM   437  O O   . ILE   A 1 75  ? -15.717 -12.506 -19.689 1.00 25.24  ? 612  ILE   A O   1 
ATOM   438  C CB  . ILE   A 1 75  ? -16.630 -9.328  -19.458 1.00 25.79  ? 612  ILE   A CB  1 
ATOM   439  C CG1 . ILE   A 1 75  ? -16.075 -8.007  -18.895 1.00 26.23  ? 612  ILE   A CG1 1 
ATOM   440  C CG2 . ILE   A 1 75  ? -17.317 -10.162 -18.374 1.00 25.20  ? 612  ILE   A CG2 1 
ATOM   441  C CD1 . ILE   A 1 75  ? -15.200 -8.217  -17.698 1.00 29.19  ? 612  ILE   A CD1 1 
ATOM   442  N N   . GLU   A 1 76  ? -16.665 -11.703 -21.565 1.00 28.31  ? 613  GLU   A N   1 
ATOM   443  C CA  . GLU   A 1 76  ? -17.122 -13.038 -21.953 1.00 28.97  ? 613  GLU   A CA  1 
ATOM   444  C C   . GLU   A 1 76  ? -15.942 -13.989 -22.096 1.00 27.74  ? 613  GLU   A C   1 
ATOM   445  O O   . GLU   A 1 76  ? -15.962 -15.109 -21.575 1.00 29.16  ? 613  GLU   A O   1 
ATOM   446  C CB  . GLU   A 1 76  ? -17.923 -12.983 -23.257 1.00 35.73  ? 613  GLU   A CB  1 
ATOM   447  C CG  . GLU   A 1 76  ? -18.606 -14.332 -23.570 1.00 40.07  ? 613  GLU   A CG  1 
ATOM   448  C CD  . GLU   A 1 76  ? -18.840 -14.591 -25.052 1.00 42.66  ? 613  GLU   A CD  1 
ATOM   449  O OE1 . GLU   A 1 76  ? -18.747 -13.646 -25.864 1.00 45.54  ? 613  GLU   A OE1 1 
ATOM   450  O OE2 . GLU   A 1 76  ? -19.123 -15.760 -25.398 1.00 55.09  ? 613  GLU   A OE2 1 
ATOM   451  N N   . ARG   A 1 77  ? -14.894 -13.548 -22.791 1.00 28.19  ? 614  ARG   A N   1 
ATOM   452  C CA  . ARG   A 1 77  ? -13.712 -14.386 -22.984 1.00 27.04  ? 614  ARG   A CA  1 
ATOM   453  C C   . ARG   A 1 77  ? -12.911 -14.566 -21.698 1.00 25.45  ? 614  ARG   A C   1 
ATOM   454  O O   . ARG   A 1 77  ? -12.207 -15.578 -21.546 1.00 29.76  ? 614  ARG   A O   1 
ATOM   455  C CB  . ARG   A 1 77  ? -12.830 -13.781 -24.072 1.00 30.79  ? 614  ARG   A CB  1 
ATOM   456  C CG  . ARG   A 1 77  ? -13.409 -13.914 -25.471 1.00 33.84  ? 614  ARG   A CG  1 
ATOM   457  C CD  . ARG   A 1 77  ? -13.282 -15.348 -25.974 1.00 34.65  ? 614  ARG   A CD  1 
ATOM   458  N NE  . ARG   A 1 77  ? -14.007 -15.526 -27.224 1.00 28.77  ? 614  ARG   A NE  1 
ATOM   459  C CZ  . ARG   A 1 77  ? -13.759 -16.480 -28.109 1.00 35.50  ? 614  ARG   A CZ  1 
ATOM   460  N NH1 . ARG   A 1 77  ? -14.489 -16.555 -29.217 1.00 34.98  ? 614  ARG   A NH1 1 
ATOM   461  N NH2 . ARG   A 1 77  ? -12.787 -17.357 -27.880 1.00 37.57  ? 614  ARG   A NH2 1 
ATOM   462  N N   . LEU   A 1 78  ? -12.980 -13.589 -20.788 1.00 28.12  ? 615  LEU   A N   1 
ATOM   463  C CA  . LEU   A 1 78  ? -12.344 -13.704 -19.477 1.00 25.37  ? 615  LEU   A CA  1 
ATOM   464  C C   . LEU   A 1 78  ? -12.948 -14.849 -18.670 1.00 28.94  ? 615  LEU   A C   1 
ATOM   465  O O   . LEU   A 1 78  ? -12.290 -15.424 -17.793 1.00 27.86  ? 615  LEU   A O   1 
ATOM   466  C CB  . LEU   A 1 78  ? -12.519 -12.380 -18.717 1.00 24.59  ? 615  LEU   A CB  1 
ATOM   467  C CG  . LEU   A 1 78  ? -11.782 -12.211 -17.389 1.00 24.95  ? 615  LEU   A CG  1 
ATOM   468  C CD1 . LEU   A 1 78  ? -10.268 -12.202 -17.633 1.00 26.82  ? 615  LEU   A CD1 1 
ATOM   469  C CD2 . LEU   A 1 78  ? -12.232 -10.937 -16.712 1.00 28.66  ? 615  LEU   A CD2 1 
ATOM   470  N N   . THR   A 1 79  ? -14.191 -15.193 -18.970 1.00 25.05  ? 616  THR   A N   1 
ATOM   471  C CA  . THR   A 1 79  ? -14.983 -16.181 -18.250 1.00 24.17  ? 616  THR   A CA  1 
ATOM   472  C C   . THR   A 1 79  ? -15.617 -17.158 -19.230 1.00 30.58  ? 616  THR   A C   1 
ATOM   473  O O   . THR   A 1 79  ? -16.779 -17.540 -19.090 1.00 26.79  ? 616  THR   A O   1 
ATOM   474  C CB  . THR   A 1 79  ? -16.044 -15.479 -17.414 1.00 23.49  ? 616  THR   A CB  1 
ATOM   475  O OG1 . THR   A 1 79  ? -16.770 -14.577 -18.263 1.00 25.71  ? 616  THR   A OG1 1 
ATOM   476  C CG2 . THR   A 1 79  ? -15.387 -14.690 -16.290 1.00 27.60  ? 616  THR   A CG2 1 
ATOM   477  N N   . TYR   A 1 80  ? -14.847 -17.570 -20.239 1.00 25.35  ? 617  TYR   A N   1 
ATOM   478  C CA  . TYR   A 1 80  ? -15.377 -18.318 -21.368 1.00 25.13  ? 617  TYR   A CA  1 
ATOM   479  C C   . TYR   A 1 80  ? -15.788 -19.726 -20.951 1.00 31.54  ? 617  TYR   A C   1 
ATOM   480  O O   . TYR   A 1 80  ? -15.078 -20.404 -20.202 1.00 30.97  ? 617  TYR   A O   1 
ATOM   481  C CB  . TYR   A 1 80  ? -14.322 -18.393 -22.468 1.00 27.45  ? 617  TYR   A CB  1 
ATOM   482  C CG  . TYR   A 1 80  ? -14.853 -18.657 -23.851 1.00 31.68  ? 617  TYR   A CG  1 
ATOM   483  C CD1 . TYR   A 1 80  ? -15.851 -17.861 -24.394 1.00 34.43  ? 617  TYR   A CD1 1 
ATOM   484  C CD2 . TYR   A 1 80  ? -14.341 -19.690 -24.626 1.00 29.14  ? 617  TYR   A CD2 1 
ATOM   485  C CE1 . TYR   A 1 80  ? -16.335 -18.090 -25.666 1.00 31.63  ? 617  TYR   A CE1 1 
ATOM   486  C CE2 . TYR   A 1 80  ? -14.820 -19.922 -25.907 1.00 41.51  ? 617  TYR   A CE2 1 
ATOM   487  C CZ  . TYR   A 1 80  ? -15.819 -19.116 -26.418 1.00 38.68  ? 617  TYR   A CZ  1 
ATOM   488  O OH  . TYR   A 1 80  ? -16.305 -19.333 -27.689 1.00 40.11  ? 617  TYR   A OH  1 
ATOM   489  N N   . HIS   A 1 81  ? -16.925 -20.189 -21.464 1.00 28.30  ? 618  HIS   A N   1 
ATOM   490  C CA  . HIS   A 1 81  ? -17.432 -21.465 -20.957 1.00 33.46  ? 618  HIS   A CA  1 
ATOM   491  C C   . HIS   A 1 81  ? -16.635 -22.659 -21.461 1.00 36.76  ? 618  HIS   A C   1 
ATOM   492  O O   . HIS   A 1 81  ? -16.645 -23.714 -20.821 1.00 41.55  ? 618  HIS   A O   1 
ATOM   493  C CB  . HIS   A 1 81  ? -18.918 -21.658 -21.299 1.00 28.39  ? 618  HIS   A CB  1 
ATOM   494  C CG  . HIS   A 1 81  ? -19.213 -21.918 -22.748 1.00 29.26  ? 618  HIS   A CG  1 
ATOM   495  N ND1 . HIS   A 1 81  ? -19.199 -20.927 -23.704 1.00 32.56  ? 618  HIS   A ND1 1 
ATOM   496  C CD2 . HIS   A 1 81  ? -19.595 -23.050 -23.391 1.00 31.90  ? 618  HIS   A CD2 1 
ATOM   497  C CE1 . HIS   A 1 81  ? -19.531 -21.437 -24.877 1.00 34.32  ? 618  HIS   A CE1 1 
ATOM   498  N NE2 . HIS   A 1 81  ? -19.778 -22.726 -24.715 1.00 34.81  ? 618  HIS   A NE2 1 
ATOM   499  N N   A MET   A 1 82  ? -15.928 -22.516 -22.581 0.67 32.49  ? 619  MET   A N   1 
ATOM   500  N N   B MET   A 1 82  ? -15.934 -22.530 -22.589 0.33 34.06  ? 619  MET   A N   1 
ATOM   501  C CA  A MET   A 1 82  ? -15.367 -23.698 -23.224 0.67 37.38  ? 619  MET   A CA  1 
ATOM   502  C CA  B MET   A 1 82  ? -15.385 -23.725 -23.221 0.33 37.68  ? 619  MET   A CA  1 
ATOM   503  C C   A MET   A 1 82  ? -14.064 -24.156 -22.591 0.67 36.42  ? 619  MET   A C   1 
ATOM   504  C C   B MET   A 1 82  ? -14.017 -24.135 -22.686 0.33 36.79  ? 619  MET   A C   1 
ATOM   505  O O   A MET   A 1 82  ? -13.762 -25.352 -22.619 0.67 34.72  ? 619  MET   A O   1 
ATOM   506  O O   B MET   A 1 82  ? -13.631 -25.294 -22.873 0.33 37.15  ? 619  MET   A O   1 
ATOM   507  C CB  A MET   A 1 82  ? -15.156 -23.434 -24.708 0.67 38.68  ? 619  MET   A CB  1 
ATOM   508  C CB  B MET   A 1 82  ? -15.320 -23.539 -24.737 0.33 40.56  ? 619  MET   A CB  1 
ATOM   509  C CG  A MET   A 1 82  ? -16.377 -22.868 -25.377 0.67 45.51  ? 619  MET   A CG  1 
ATOM   510  C CG  B MET   A 1 82  ? -16.690 -23.575 -25.392 0.33 47.68  ? 619  MET   A CG  1 
ATOM   511  S SD  A MET   A 1 82  ? -16.423 -23.314 -27.107 0.67 48.54  ? 619  MET   A SD  1 
ATOM   512  S SD  B MET   A 1 82  ? -16.664 -24.080 -27.120 0.33 62.04  ? 619  MET   A SD  1 
ATOM   513  C CE  A MET   A 1 82  ? -17.156 -24.954 -26.956 0.67 58.64  ? 619  MET   A CE  1 
ATOM   514  C CE  B MET   A 1 82  ? -15.794 -22.703 -27.857 0.33 52.07  ? 619  MET   A CE  1 
ATOM   515  N N   . TYR   A 1 83  ? -13.283 -23.239 -22.027 1.00 36.68  ? 620  TYR   A N   1 
ATOM   516  C CA  . TYR   A 1 83  ? -11.983 -23.598 -21.466 1.00 36.14  ? 620  TYR   A CA  1 
ATOM   517  C C   . TYR   A 1 83  ? -11.482 -22.480 -20.568 1.00 32.60  ? 620  TYR   A C   1 
ATOM   518  O O   . TYR   A 1 83  ? -11.929 -21.336 -20.661 1.00 33.40  ? 620  TYR   A O   1 
ATOM   519  C CB  . TYR   A 1 83  ? -10.948 -23.878 -22.558 1.00 41.88  ? 620  TYR   A CB  1 
ATOM   520  C CG  . TYR   A 1 83  ? -10.948 -22.835 -23.644 1.00 38.56  ? 620  TYR   A CG  1 
ATOM   521  C CD1 . TYR   A 1 83  ? -10.438 -21.563 -23.415 1.00 32.87  ? 620  TYR   A CD1 1 
ATOM   522  C CD2 . TYR   A 1 83  ? -11.484 -23.114 -24.893 1.00 40.74  ? 620  TYR   A CD2 1 
ATOM   523  C CE1 . TYR   A 1 83  ? -10.449 -20.599 -24.402 1.00 42.83  ? 620  TYR   A CE1 1 
ATOM   524  C CE2 . TYR   A 1 83  ? -11.503 -22.162 -25.886 1.00 39.09  ? 620  TYR   A CE2 1 
ATOM   525  C CZ  . TYR   A 1 83  ? -10.981 -20.910 -25.640 1.00 40.05  ? 620  TYR   A CZ  1 
ATOM   526  O OH  . TYR   A 1 83  ? -11.002 -19.971 -26.644 1.00 46.15  ? 620  TYR   A OH  1 
ATOM   527  N N   . ALA   A 1 84  ? -10.520 -22.828 -19.724 1.00 44.30  ? 621  ALA   A N   1 
ATOM   528  C CA  . ALA   A 1 84  ? -9.853  -21.856 -18.873 1.00 41.68  ? 621  ALA   A CA  1 
ATOM   529  C C   . ALA   A 1 84  ? -8.819  -21.076 -19.680 1.00 34.64  ? 621  ALA   A C   1 
ATOM   530  O O   . ALA   A 1 84  ? -8.298  -21.551 -20.691 1.00 32.46  ? 621  ALA   A O   1 
ATOM   531  C CB  . ALA   A 1 84  ? -9.182  -22.565 -17.694 1.00 49.91  ? 621  ALA   A CB  1 
ATOM   532  N N   . ASP   A 1 85  ? -8.510  -19.864 -19.207 1.00 35.98  ? 622  ASP   A N   1 
ATOM   533  C CA  . ASP   A 1 85  ? -7.563  -18.977 -19.890 1.00 35.21  ? 622  ASP   A CA  1 
ATOM   534  C C   . ASP   A 1 85  ? -6.746  -18.220 -18.846 1.00 34.32  ? 622  ASP   A C   1 
ATOM   535  O O   . ASP   A 1 85  ? -6.875  -17.002 -18.692 1.00 32.68  ? 622  ASP   A O   1 
ATOM   536  C CB  . ASP   A 1 85  ? -8.309  -18.023 -20.822 1.00 30.47  ? 622  ASP   A CB  1 
ATOM   537  C CG  . ASP   A 1 85  ? -7.411  -17.402 -21.875 1.00 38.33  ? 622  ASP   A CG  1 
ATOM   538  O OD1 . ASP   A 1 85  ? -6.172  -17.525 -21.757 1.00 35.06  ? 622  ASP   A OD1 1 
ATOM   539  O OD2 . ASP   A 1 85  ? -7.949  -16.786 -22.824 1.00 36.98  ? 622  ASP   A OD2 1 
ATOM   540  N N   . PRO   A 1 86  ? -5.889  -18.929 -18.097 1.00 34.19  ? 623  PRO   A N   1 
ATOM   541  C CA  . PRO   A 1 86  ? -5.151  -18.267 -17.003 1.00 35.55  ? 623  PRO   A CA  1 
ATOM   542  C C   . PRO   A 1 86  ? -4.275  -17.118 -17.459 1.00 35.36  ? 623  PRO   A C   1 
ATOM   543  O O   . PRO   A 1 86  ? -4.127  -16.133 -16.719 1.00 33.88  ? 623  PRO   A O   1 
ATOM   544  C CB  . PRO   A 1 86  ? -4.307  -19.403 -16.402 1.00 34.71  ? 623  PRO   A CB  1 
ATOM   545  C CG  . PRO   A 1 86  ? -4.240  -20.452 -17.481 1.00 38.38  ? 623  PRO   A CG  1 
ATOM   546  C CD  . PRO   A 1 86  ? -5.538  -20.354 -18.224 1.00 33.42  ? 623  PRO   A CD  1 
ATOM   547  N N   . ASN   A 1 87  ? -3.680  -17.205 -18.650 1.00 33.67  ? 624  ASN   A N   1 
ATOM   548  C CA  . ASN   A 1 87  ? -2.821  -16.113 -19.102 1.00 34.47  ? 624  ASN   A CA  1 
ATOM   549  C C   . ASN   A 1 87  ? -3.634  -14.847 -19.346 1.00 35.63  ? 624  ASN   A C   1 
ATOM   550  O O   . ASN   A 1 87  ? -3.218  -13.749 -18.960 1.00 35.30  ? 624  ASN   A O   1 
ATOM   551  C CB  . ASN   A 1 87  ? -2.061  -16.523 -20.360 1.00 37.24  ? 624  ASN   A CB  1 
ATOM   552  C CG  . ASN   A 1 87  ? -0.998  -17.580 -20.082 1.00 47.07  ? 624  ASN   A CG  1 
ATOM   553  O OD1 . ASN   A 1 87  ? -0.515  -17.712 -18.958 1.00 46.82  ? 624  ASN   A OD1 1 
ATOM   554  N ND2 . ASN   A 1 87  ? -0.625  -18.328 -21.111 1.00 46.94  ? 624  ASN   A ND2 1 
ATOM   555  N N   . PHE   A 1 88  ? -4.800  -14.984 -19.973 1.00 29.00  ? 625  PHE   A N   1 
ATOM   556  C CA  . PHE   A 1 88  ? -5.670  -13.828 -20.181 1.00 24.97  ? 625  PHE   A CA  1 
ATOM   557  C C   . PHE   A 1 88  ? -6.196  -13.280 -18.861 1.00 30.49  ? 625  PHE   A C   1 
ATOM   558  O O   . PHE   A 1 88  ? -6.235  -12.056 -18.669 1.00 29.76  ? 625  PHE   A O   1 
ATOM   559  C CB  . PHE   A 1 88  ? -6.813  -14.198 -21.124 1.00 26.09  ? 625  PHE   A CB  1 
ATOM   560  C CG  . PHE   A 1 88  ? -7.724  -13.039 -21.470 1.00 27.07  ? 625  PHE   A CG  1 
ATOM   561  C CD1 . PHE   A 1 88  ? -7.217  -11.892 -22.073 1.00 32.36  ? 625  PHE   A CD1 1 
ATOM   562  C CD2 . PHE   A 1 88  ? -9.084  -13.126 -21.257 1.00 28.91  ? 625  PHE   A CD2 1 
ATOM   563  C CE1 . PHE   A 1 88  ? -8.063  -10.838 -22.412 1.00 30.21  ? 625  PHE   A CE1 1 
ATOM   564  C CE2 . PHE   A 1 88  ? -9.933  -12.080 -21.589 1.00 29.94  ? 625  PHE   A CE2 1 
ATOM   565  C CZ  . PHE   A 1 88  ? -9.419  -10.932 -22.164 1.00 28.01  ? 625  PHE   A CZ  1 
ATOM   566  N N   . VAL   A 1 89  ? -6.586  -14.159 -17.930 1.00 25.38  ? 626  VAL   A N   1 
ATOM   567  C CA  . VAL   A 1 89  ? -7.051  -13.688 -16.624 1.00 23.79  ? 626  VAL   A CA  1 
ATOM   568  C C   . VAL   A 1 89  ? -5.987  -12.826 -15.954 1.00 25.94  ? 626  VAL   A C   1 
ATOM   569  O O   . VAL   A 1 89  ? -6.279  -11.733 -15.439 1.00 27.34  ? 626  VAL   A O   1 
ATOM   570  C CB  . VAL   A 1 89  ? -7.452  -14.871 -15.723 1.00 31.97  ? 626  VAL   A CB  1 
ATOM   571  C CG1 . VAL   A 1 89  ? -7.742  -14.351 -14.306 1.00 25.26  ? 626  VAL   A CG1 1 
ATOM   572  C CG2 . VAL   A 1 89  ? -8.694  -15.581 -16.295 1.00 33.01  ? 626  VAL   A CG2 1 
ATOM   573  N N   . ARG   A 1 90  ? -4.738  -13.300 -15.955 1.00 26.30  ? 627  ARG   A N   1 
ATOM   574  C CA  . ARG   A 1 90  ? -3.664  -12.553 -15.294 1.00 29.78  ? 627  ARG   A CA  1 
ATOM   575  C C   . ARG   A 1 90  ? -3.437  -11.202 -15.966 1.00 32.55  ? 627  ARG   A C   1 
ATOM   576  O O   . ARG   A 1 90  ? -3.367  -10.162 -15.297 1.00 31.82  ? 627  ARG   A O   1 
ATOM   577  C CB  . ARG   A 1 90  ? -2.372  -13.367 -15.287 1.00 33.56  ? 627  ARG   A CB  1 
ATOM   578  C CG  . ARG   A 1 90  ? -1.224  -12.653 -14.562 1.00 34.32  ? 627  ARG   A CG  1 
ATOM   579  C CD  . ARG   A 1 90  ? 0.136   -13.308 -14.737 1.00 41.56  ? 627  ARG   A CD  1 
ATOM   580  N NE  . ARG   A 1 90  ? 0.053   -14.710 -15.124 1.00 64.06  ? 627  ARG   A NE  1 
ATOM   581  C CZ  . ARG   A 1 90  ? 0.210   -15.144 -16.371 1.00 76.71  ? 627  ARG   A CZ  1 
ATOM   582  N NH1 . ARG   A 1 90  ? 0.114   -16.439 -16.634 1.00 71.03  ? 627  ARG   A NH1 1 
ATOM   583  N NH2 . ARG   A 1 90  ? 0.453   -14.282 -17.354 1.00 83.19  ? 627  ARG   A NH2 1 
ATOM   584  N N   . THR   A 1 91  ? -3.314  -11.203 -17.296 1.00 29.40  ? 628  THR   A N   1 
ATOM   585  C CA  . THR   A 1 91  ? -3.033  -9.963  -18.015 1.00 29.29  ? 628  THR   A CA  1 
ATOM   586  C C   . THR   A 1 91  ? -4.191  -8.985  -17.915 1.00 30.45  ? 628  THR   A C   1 
ATOM   587  O O   . THR   A 1 91  ? -3.988  -7.776  -17.732 1.00 28.60  ? 628  THR   A O   1 
ATOM   588  C CB  . THR   A 1 91  ? -2.724  -10.281 -19.471 1.00 30.86  ? 628  THR   A CB  1 
ATOM   589  O OG1 . THR   A 1 91  ? -1.620  -11.177 -19.502 1.00 35.73  ? 628  THR   A OG1 1 
ATOM   590  C CG2 . THR   A 1 91  ? -2.349  -9.024  -20.230 1.00 31.26  ? 628  THR   A CG2 1 
ATOM   591  N N   . PHE   A 1 92  ? -5.414  -9.494  -18.025 1.00 26.67  ? 629  PHE   A N   1 
ATOM   592  C CA  . PHE   A 1 92  ? -6.581  -8.643  -17.852 1.00 25.13  ? 629  PHE   A CA  1 
ATOM   593  C C   . PHE   A 1 92  ? -6.566  -7.971  -16.485 1.00 31.57  ? 629  PHE   A C   1 
ATOM   594  O O   . PHE   A 1 92  ? -6.713  -6.748  -16.381 1.00 28.87  ? 629  PHE   A O   1 
ATOM   595  C CB  . PHE   A 1 92  ? -7.855  -9.471  -18.029 1.00 25.09  ? 629  PHE   A CB  1 
ATOM   596  C CG  . PHE   A 1 92  ? -9.116  -8.652  -17.981 1.00 23.01  ? 629  PHE   A CG  1 
ATOM   597  C CD1 . PHE   A 1 92  ? -9.659  -8.270  -16.768 1.00 25.98  ? 629  PHE   A CD1 1 
ATOM   598  C CD2 . PHE   A 1 92  ? -9.763  -8.279  -19.145 1.00 27.87  ? 629  PHE   A CD2 1 
ATOM   599  C CE1 . PHE   A 1 92  ? -10.824 -7.522  -16.711 1.00 26.46  ? 629  PHE   A CE1 1 
ATOM   600  C CE2 . PHE   A 1 92  ? -10.935 -7.517  -19.095 1.00 23.64  ? 629  PHE   A CE2 1 
ATOM   601  C CZ  . PHE   A 1 92  ? -11.462 -7.146  -17.871 1.00 27.80  ? 629  PHE   A CZ  1 
ATOM   602  N N   . LEU   A 1 93  ? -6.407  -8.754  -15.412 1.00 25.37  ? 630  LEU   A N   1 
ATOM   603  C CA  . LEU   A 1 93  ? -6.535  -8.139  -14.091 1.00 26.75  ? 630  LEU   A CA  1 
ATOM   604  C C   . LEU   A 1 93  ? -5.397  -7.160  -13.800 1.00 28.72  ? 630  LEU   A C   1 
ATOM   605  O O   . LEU   A 1 93  ? -5.578  -6.243  -12.993 1.00 27.99  ? 630  LEU   A O   1 
ATOM   606  C CB  . LEU   A 1 93  ? -6.630  -9.225  -13.007 1.00 24.96  ? 630  LEU   A CB  1 
ATOM   607  C CG  . LEU   A 1 93  ? -8.065  -9.806  -12.975 1.00 22.89  ? 630  LEU   A CG  1 
ATOM   608  C CD1 . LEU   A 1 93  ? -8.170  -10.999 -12.021 1.00 23.21  ? 630  LEU   A CD1 1 
ATOM   609  C CD2 . LEU   A 1 93  ? -9.097  -8.752  -12.604 1.00 25.04  ? 630  LEU   A CD2 1 
ATOM   610  N N   . THR   A 1 94  ? -4.241  -7.329  -14.449 1.00 26.73  ? 631  THR   A N   1 
ATOM   611  C CA  . THR   A 1 94  ? -3.162  -6.348  -14.337 1.00 27.82  ? 631  THR   A CA  1 
ATOM   612  C C   . THR   A 1 94  ? -3.484  -5.059  -15.091 1.00 30.16  ? 631  THR   A C   1 
ATOM   613  O O   . THR   A 1 94  ? -3.113  -3.969  -14.645 1.00 28.47  ? 631  THR   A O   1 
ATOM   614  C CB  . THR   A 1 94  ? -1.869  -6.961  -14.866 1.00 29.87  ? 631  THR   A CB  1 
ATOM   615  O OG1 . THR   A 1 94  ? -1.423  -7.967  -13.954 1.00 34.12  ? 631  THR   A OG1 1 
ATOM   616  C CG2 . THR   A 1 94  ? -0.752  -5.890  -15.043 1.00 28.28  ? 631  THR   A CG2 1 
ATOM   617  N N   . THR   A 1 95  ? -4.157  -5.152  -16.244 1.00 31.60  ? 632  THR   A N   1 
ATOM   618  C CA  . THR   A 1 95  ? -4.217  -4.013  -17.150 1.00 26.96  ? 632  THR   A CA  1 
ATOM   619  C C   . THR   A 1 95  ? -5.591  -3.371  -17.286 1.00 27.58  ? 632  THR   A C   1 
ATOM   620  O O   . THR   A 1 95  ? -5.682  -2.319  -17.924 1.00 26.52  ? 632  THR   A O   1 
ATOM   621  C CB  . THR   A 1 95  ? -3.738  -4.419  -18.551 1.00 29.25  ? 632  THR   A CB  1 
ATOM   622  O OG1 . THR   A 1 95  ? -4.599  -5.445  -19.074 1.00 28.42  ? 632  THR   A OG1 1 
ATOM   623  C CG2 . THR   A 1 95  ? -2.296  -4.926  -18.517 1.00 29.68  ? 632  THR   A CG2 1 
ATOM   624  N N   . TYR   A 1 96  ? -6.653  -3.954  -16.715 1.00 25.93  ? 633  TYR   A N   1 
ATOM   625  C CA  . TYR   A 1 96  ? -8.008  -3.537  -17.088 1.00 28.88  ? 633  TYR   A CA  1 
ATOM   626  C C   . TYR   A 1 96  ? -8.327  -2.100  -16.688 1.00 29.07  ? 633  TYR   A C   1 
ATOM   627  O O   . TYR   A 1 96  ? -9.238  -1.499  -17.268 1.00 28.74  ? 633  TYR   A O   1 
ATOM   628  C CB  . TYR   A 1 96  ? -9.061  -4.464  -16.463 1.00 22.81  ? 633  TYR   A CB  1 
ATOM   629  C CG  . TYR   A 1 96  ? -9.352  -4.155  -15.001 1.00 23.09  ? 633  TYR   A CG  1 
ATOM   630  C CD1 . TYR   A 1 96  ? -10.281 -3.183  -14.639 1.00 25.29  ? 633  TYR   A CD1 1 
ATOM   631  C CD2 . TYR   A 1 96  ? -8.690  -4.833  -13.987 1.00 23.72  ? 633  TYR   A CD2 1 
ATOM   632  C CE1 . TYR   A 1 96  ? -10.534 -2.890  -13.320 1.00 28.39  ? 633  TYR   A CE1 1 
ATOM   633  C CE2 . TYR   A 1 96  ? -8.949  -4.560  -12.653 1.00 24.57  ? 633  TYR   A CE2 1 
ATOM   634  C CZ  . TYR   A 1 96  ? -9.871  -3.582  -12.328 1.00 27.56  ? 633  TYR   A CZ  1 
ATOM   635  O OH  . TYR   A 1 96  ? -10.130 -3.284  -10.996 1.00 28.12  ? 633  TYR   A OH  1 
ATOM   636  N N   . ARG   A 1 97  ? -7.629  -1.545  -15.690 1.00 27.06  ? 634  ARG   A N   1 
ATOM   637  C CA  . ARG   A 1 97  ? -7.987  -0.212  -15.229 1.00 27.55  ? 634  ARG   A CA  1 
ATOM   638  C C   . ARG   A 1 97  ? -7.751  0.833   -16.304 1.00 32.11  ? 634  ARG   A C   1 
ATOM   639  O O   . ARG   A 1 97  ? -8.312  1.934   -16.225 1.00 30.70  ? 634  ARG   A O   1 
ATOM   640  C CB  . ARG   A 1 97  ? -7.206  0.121   -13.949 1.00 29.32  ? 634  ARG   A CB  1 
ATOM   641  C CG  . ARG   A 1 97  ? -7.508  -0.878  -12.806 1.00 25.97  ? 634  ARG   A CG  1 
ATOM   642  C CD  . ARG   A 1 97  ? -6.398  -0.931  -11.747 1.00 26.96  ? 634  ARG   A CD  1 
ATOM   643  N NE  . ARG   A 1 97  ? -6.517  -2.142  -10.942 1.00 28.82  ? 634  ARG   A NE  1 
ATOM   644  C CZ  . ARG   A 1 97  ? -6.036  -3.330  -11.304 1.00 29.92  ? 634  ARG   A CZ  1 
ATOM   645  N NH1 . ARG   A 1 97  ? -5.372  -3.468  -12.441 1.00 28.31  ? 634  ARG   A NH1 1 
ATOM   646  N NH2 . ARG   A 1 97  ? -6.213  -4.382  -10.520 1.00 25.66  ? 634  ARG   A NH2 1 
ATOM   647  N N   . SER   A 1 98  ? -6.944  0.510   -17.309 1.00 29.90  ? 635  SER   A N   1 
ATOM   648  C CA  . SER   A 1 98  ? -6.733  1.413   -18.432 1.00 28.90  ? 635  SER   A CA  1 
ATOM   649  C C   . SER   A 1 98  ? -7.903  1.414   -19.415 1.00 33.26  ? 635  SER   A C   1 
ATOM   650  O O   . SER   A 1 98  ? -7.870  2.190   -20.374 1.00 33.27  ? 635  SER   A O   1 
ATOM   651  C CB  . SER   A 1 98  ? -5.447  1.040   -19.180 1.00 30.47  ? 635  SER   A CB  1 
ATOM   652  O OG  . SER   A 1 98  ? -5.575  -0.255  -19.752 1.00 30.59  ? 635  SER   A OG  1 
ATOM   653  N N   . PHE   A 1 99  ? -8.916  0.554   -19.227 1.00 28.71  ? 636  PHE   A N   1 
ATOM   654  C CA  . PHE   A 1 99  ? -10.082 0.603   -20.101 1.00 36.53  ? 636  PHE   A CA  1 
ATOM   655  C C   . PHE   A 1 99  ? -11.405 0.347   -19.390 1.00 31.19  ? 636  PHE   A C   1 
ATOM   656  O O   . PHE   A 1 99  ? -12.452 0.407   -20.043 1.00 31.49  ? 636  PHE   A O   1 
ATOM   657  C CB  . PHE   A 1 99  ? -9.933  -0.381  -21.286 1.00 29.27  ? 636  PHE   A CB  1 
ATOM   658  C CG  . PHE   A 1 99  ? -9.681  -1.832  -20.889 1.00 31.35  ? 636  PHE   A CG  1 
ATOM   659  C CD1 . PHE   A 1 99  ? -10.726 -2.659  -20.484 1.00 28.46  ? 636  PHE   A CD1 1 
ATOM   660  C CD2 . PHE   A 1 99  ? -8.402  -2.379  -20.985 1.00 30.33  ? 636  PHE   A CD2 1 
ATOM   661  C CE1 . PHE   A 1 99  ? -10.491 -4.002  -20.144 1.00 28.09  ? 636  PHE   A CE1 1 
ATOM   662  C CE2 . PHE   A 1 99  ? -8.151  -3.720  -20.644 1.00 30.50  ? 636  PHE   A CE2 1 
ATOM   663  C CZ  . PHE   A 1 99  ? -9.208  -4.535  -20.226 1.00 25.75  ? 636  PHE   A CZ  1 
ATOM   664  N N   . CYS   A 1 100 ? -11.401 0.102   -18.081 1.00 26.45  ? 637  CYS   A N   1 
ATOM   665  C CA  . CYS   A 1 100 ? -12.618 -0.277  -17.375 1.00 26.33  ? 637  CYS   A CA  1 
ATOM   666  C C   . CYS   A 1 100 ? -12.451 0.078   -15.904 1.00 30.01  ? 637  CYS   A C   1 
ATOM   667  O O   . CYS   A 1 100 ? -11.395 -0.180  -15.330 1.00 26.99  ? 637  CYS   A O   1 
ATOM   668  C CB  . CYS   A 1 100 ? -12.892 -1.777  -17.554 1.00 27.02  ? 637  CYS   A CB  1 
ATOM   669  S SG  . CYS   A 1 100 ? -14.328 -2.401  -16.636 1.00 30.13  ? 637  CYS   A SG  1 
ATOM   670  N N   . LYS   A 1 101 ? -13.501 0.673   -15.287 1.00 26.50  ? 638  LYS   A N   1 
ATOM   671  C CA  . LYS   A 1 101 ? -13.354 1.008   -13.871 1.00 28.91  ? 638  LYS   A CA  1 
ATOM   672  C C   . LYS   A 1 101 ? -13.564 -0.231  -13.004 1.00 27.57  ? 638  LYS   A C   1 
ATOM   673  O O   . LYS   A 1 101 ? -14.300 -1.138  -13.390 1.00 28.29  ? 638  LYS   A O   1 
ATOM   674  C CB  . LYS   A 1 101 ? -14.351 2.085   -13.453 1.00 28.12  ? 638  LYS   A CB  1 
ATOM   675  C CG  . LYS   A 1 101 ? -14.094 3.457   -14.061 1.00 37.89  ? 638  LYS   A CG  1 
ATOM   676  C CD  . LYS   A 1 101 ? -13.305 4.327   -13.102 1.00 45.73  ? 638  LYS   A CD  1 
ATOM   677  C CE  . LYS   A 1 101 ? -13.278 5.775   -13.557 1.00 46.68  ? 638  LYS   A CE  1 
ATOM   678  N NZ  . LYS   A 1 101 ? -14.618 6.418   -13.441 1.00 54.19  ? 638  LYS   A NZ  1 
ATOM   679  N N   . PRO   A 1 102 ? -12.927 -0.286  -11.824 1.00 27.87  ? 639  PRO   A N   1 
ATOM   680  C CA  . PRO   A 1 102 ? -13.153 -1.436  -10.925 1.00 31.50  ? 639  PRO   A CA  1 
ATOM   681  C C   . PRO   A 1 102 ? -14.623 -1.703  -10.617 1.00 27.35  ? 639  PRO   A C   1 
ATOM   682  O O   . PRO   A 1 102 ? -15.052 -2.857  -10.689 1.00 27.98  ? 639  PRO   A O   1 
ATOM   683  C CB  . PRO   A 1 102 ? -12.370 -1.051  -9.667  1.00 31.35  ? 639  PRO   A CB  1 
ATOM   684  C CG  . PRO   A 1 102 ? -11.231 -0.185  -10.187 1.00 25.76  ? 639  PRO   A CG  1 
ATOM   685  C CD  . PRO   A 1 102 ? -11.833 0.592   -11.358 1.00 28.15  ? 639  PRO   A CD  1 
ATOM   686  N N   . GLN   A 1 103 ? -15.399 -0.672  -10.266 1.00 26.24  ? 640  GLN   A N   1 
ATOM   687  C CA  . GLN   A 1 103 ? -16.837 -0.861  -10.048 1.00 25.84  ? 640  GLN   A CA  1 
ATOM   688  C C   . GLN   A 1 103 ? -17.510 -1.427  -11.286 1.00 29.23  ? 640  GLN   A C   1 
ATOM   689  O O   . GLN   A 1 103 ? -18.385 -2.303  -11.196 1.00 29.89  ? 640  GLN   A O   1 
ATOM   690  C CB  . GLN   A 1 103 ? -17.475 0.478   -9.672  1.00 28.05  ? 640  GLN   A CB  1 
ATOM   691  C CG  . GLN   A 1 103 ? -17.071 0.988   -8.310  1.00 32.98  ? 640  GLN   A CG  1 
ATOM   692  C CD  . GLN   A 1 103 ? -17.868 0.350   -7.199  1.00 38.37  ? 640  GLN   A CD  1 
ATOM   693  O OE1 . GLN   A 1 103 ? -18.991 -0.107  -7.417  1.00 38.65  ? 640  GLN   A OE1 1 
ATOM   694  N NE2 . GLN   A 1 103 ? -17.305 0.330   -5.998  1.00 35.27  ? 640  GLN   A NE2 1 
ATOM   695  N N   . GLU   A 1 104 ? -17.134 -0.910  -12.450 1.00 26.09  ? 641  GLU   A N   1 
ATOM   696  C CA  . GLU   A 1 104 ? -17.692 -1.376  -13.713 1.00 29.62  ? 641  GLU   A CA  1 
ATOM   697  C C   . GLU   A 1 104 ? -17.351 -2.838  -13.943 1.00 30.82  ? 641  GLU   A C   1 
ATOM   698  O O   . GLU   A 1 104 ? -18.206 -3.622  -14.376 1.00 29.29  ? 641  GLU   A O   1 
ATOM   699  C CB  . GLU   A 1 104 ? -17.151 -0.494  -14.840 1.00 30.58  ? 641  GLU   A CB  1 
ATOM   700  C CG  . GLU   A 1 104 ? -17.616 -0.778  -16.252 1.00 33.88  ? 641  GLU   A CG  1 
ATOM   701  C CD  . GLU   A 1 104 ? -16.884 0.118   -17.254 1.00 39.40  ? 641  GLU   A CD  1 
ATOM   702  O OE1 . GLU   A 1 104 ? -17.113 -0.020  -18.475 1.00 39.12  ? 641  GLU   A OE1 1 
ATOM   703  O OE2 . GLU   A 1 104 ? -16.068 0.963   -16.802 1.00 35.28  ? 641  GLU   A OE2 1 
ATOM   704  N N   . LEU   A 1 105 ? -16.106 -3.227  -13.635 1.00 26.24  ? 642  LEU   A N   1 
ATOM   705  C CA  . LEU   A 1 105 ? -15.695 -4.623  -13.789 1.00 29.81  ? 642  LEU   A CA  1 
ATOM   706  C C   . LEU   A 1 105 ? -16.516 -5.543  -12.890 1.00 26.80  ? 642  LEU   A C   1 
ATOM   707  O O   . LEU   A 1 105 ? -16.986 -6.600  -13.331 1.00 25.70  ? 642  LEU   A O   1 
ATOM   708  C CB  . LEU   A 1 105 ? -14.197 -4.774  -13.495 1.00 25.47  ? 642  LEU   A CB  1 
ATOM   709  C CG  . LEU   A 1 105 ? -13.695 -6.222  -13.395 1.00 23.72  ? 642  LEU   A CG  1 
ATOM   710  C CD1 . LEU   A 1 105 ? -13.963 -6.959  -14.700 1.00 22.45  ? 642  LEU   A CD1 1 
ATOM   711  C CD2 . LEU   A 1 105 ? -12.199 -6.288  -13.007 1.00 23.25  ? 642  LEU   A CD2 1 
ATOM   712  N N   . LEU   A 1 106 ? -16.700 -5.164  -11.625 1.00 27.15  ? 643  LEU   A N   1 
ATOM   713  C CA  . LEU   A 1 106 ? -17.485 -6.008  -10.732 1.00 23.57  ? 643  LEU   A CA  1 
ATOM   714  C C   . LEU   A 1 106 ? -18.921 -6.137  -11.234 1.00 29.04  ? 643  LEU   A C   1 
ATOM   715  O O   . LEU   A 1 106 ? -19.486 -7.237  -11.245 1.00 28.63  ? 643  LEU   A O   1 
ATOM   716  C CB  . LEU   A 1 106 ? -17.446 -5.449  -9.310  1.00 23.43  ? 643  LEU   A CB  1 
ATOM   717  C CG  . LEU   A 1 106 ? -18.250 -6.226  -8.260  1.00 25.95  ? 643  LEU   A CG  1 
ATOM   718  C CD1 . LEU   A 1 106 ? -17.793 -7.697  -8.252  1.00 25.81  ? 643  LEU   A CD1 1 
ATOM   719  C CD2 . LEU   A 1 106 ? -18.107 -5.606  -6.887  1.00 25.67  ? 643  LEU   A CD2 1 
ATOM   720  N N   . SER   A 1 107 ? -19.521 -5.025  -11.683 1.00 26.08  ? 644  SER   A N   1 
ATOM   721  C CA  . SER   A 1 107 ? -20.890 -5.099  -12.203 1.00 27.84  ? 644  SER   A CA  1 
ATOM   722  C C   . SER   A 1 107 ? -20.971 -6.009  -13.427 1.00 23.83  ? 644  SER   A C   1 
ATOM   723  O O   . SER   A 1 107 ? -21.919 -6.793  -13.562 1.00 27.70  ? 644  SER   A O   1 
ATOM   724  C CB  . SER   A 1 107 ? -21.407 -3.700  -12.532 1.00 24.50  ? 644  SER   A CB  1 
ATOM   725  O OG  . SER   A 1 107 ? -21.602 -2.960  -11.342 1.00 26.82  ? 644  SER   A OG  1 
ATOM   726  N N   . LEU   A 1 108 ? -19.973 -5.932  -14.316 1.00 25.39  ? 645  LEU   A N   1 
ATOM   727  C CA  . LEU   A 1 108 ? -19.950 -6.802  -15.491 1.00 26.70  ? 645  LEU   A CA  1 
ATOM   728  C C   . LEU   A 1 108 ? -19.812 -8.266  -15.099 1.00 30.00  ? 645  LEU   A C   1 
ATOM   729  O O   . LEU   A 1 108 ? -20.443 -9.138  -15.706 1.00 27.76  ? 645  LEU   A O   1 
ATOM   730  C CB  . LEU   A 1 108 ? -18.805 -6.407  -16.427 1.00 31.61  ? 645  LEU   A CB  1 
ATOM   731  C CG  . LEU   A 1 108 ? -19.027 -5.198  -17.349 1.00 31.81  ? 645  LEU   A CG  1 
ATOM   732  C CD1 . LEU   A 1 108 ? -17.700 -4.605  -17.812 1.00 27.54  ? 645  LEU   A CD1 1 
ATOM   733  C CD2 . LEU   A 1 108 ? -19.871 -5.601  -18.552 1.00 42.57  ? 645  LEU   A CD2 1 
ATOM   734  N N   . LEU   A 1 109 ? -18.974 -8.566  -14.103 1.00 22.82  ? 646  LEU   A N   1 
ATOM   735  C CA  . LEU   A 1 109 ? -18.832 -9.965  -13.695 1.00 25.31  ? 646  LEU   A CA  1 
ATOM   736  C C   . LEU   A 1 109 ? -20.109 -10.488 -13.040 1.00 26.22  ? 646  LEU   A C   1 
ATOM   737  O O   . LEU   A 1 109 ? -20.484 -11.653 -13.229 1.00 25.66  ? 646  LEU   A O   1 
ATOM   738  C CB  . LEU   A 1 109 ? -17.634 -10.113 -12.755 1.00 25.91  ? 646  LEU   A CB  1 
ATOM   739  C CG  . LEU   A 1 109 ? -16.252 -9.993  -13.405 1.00 26.47  ? 646  LEU   A CG  1 
ATOM   740  C CD1 . LEU   A 1 109 ? -15.170 -9.847  -12.339 1.00 24.41  ? 646  LEU   A CD1 1 
ATOM   741  C CD2 . LEU   A 1 109 ? -15.955 -11.169 -14.323 1.00 27.18  ? 646  LEU   A CD2 1 
ATOM   742  N N   . ILE   A 1 110 ? -20.776 -9.652  -12.252 1.00 25.42  ? 647  ILE   A N   1 
ATOM   743  C CA  . ILE   A 1 110 ? -22.038 -10.048 -11.648 1.00 24.91  ? 647  ILE   A CA  1 
ATOM   744  C C   . ILE   A 1 110 ? -23.089 -10.260 -12.728 1.00 29.47  ? 647  ILE   A C   1 
ATOM   745  O O   . ILE   A 1 110 ? -23.879 -11.206 -12.668 1.00 29.84  ? 647  ILE   A O   1 
ATOM   746  C CB  . ILE   A 1 110 ? -22.467 -8.998  -10.602 1.00 29.24  ? 647  ILE   A CB  1 
ATOM   747  C CG1 . ILE   A 1 110 ? -21.525 -9.053  -9.394  1.00 26.73  ? 647  ILE   A CG1 1 
ATOM   748  C CG2 . ILE   A 1 110 ? -23.949 -9.175  -10.177 1.00 31.25  ? 647  ILE   A CG2 1 
ATOM   749  C CD1 . ILE   A 1 110 ? -21.786 -8.004  -8.324  1.00 28.18  ? 647  ILE   A CD1 1 
ATOM   750  N N   . GLU   A 1 111 ? -23.107 -9.382  -13.735 1.00 26.54  ? 648  GLU   A N   1 
ATOM   751  C CA  . GLU   A 1 111 ? -24.036 -9.532  -14.852 1.00 26.95  ? 648  GLU   A CA  1 
ATOM   752  C C   . GLU   A 1 111 ? -23.761 -10.828 -15.596 1.00 30.03  ? 648  GLU   A C   1 
ATOM   753  O O   . GLU   A 1 111 ? -24.689 -11.544 -15.990 1.00 29.04  ? 648  GLU   A O   1 
ATOM   754  C CB  . GLU   A 1 111 ? -23.907 -8.323  -15.783 1.00 33.68  ? 648  GLU   A CB  1 
ATOM   755  C CG  . GLU   A 1 111 ? -24.742 -8.383  -17.043 1.00 32.94  ? 648  GLU   A CG  1 
ATOM   756  C CD  . GLU   A 1 111 ? -24.434 -7.232  -18.002 1.00 37.73  ? 648  GLU   A CD  1 
ATOM   757  O OE1 . GLU   A 1 111 ? -25.142 -7.096  -19.021 1.00 38.61  ? 648  GLU   A OE1 1 
ATOM   758  O OE2 . GLU   A 1 111 ? -23.479 -6.460  -17.733 1.00 32.04  ? 648  GLU   A OE2 1 
ATOM   759  N N   . ARG   A 1 112 ? -22.479 -11.155 -15.759 1.00 24.53  ? 649  ARG   A N   1 
ATOM   760  C CA  . ARG   A 1 112 ? -22.088 -12.406 -16.392 1.00 24.54  ? 649  ARG   A CA  1 
ATOM   761  C C   . ARG   A 1 112 ? -22.558 -13.613 -15.589 1.00 29.94  ? 649  ARG   A C   1 
ATOM   762  O O   . ARG   A 1 112 ? -22.919 -14.639 -16.173 1.00 29.22  ? 649  ARG   A O   1 
ATOM   763  C CB  . ARG   A 1 112 ? -20.570 -12.432 -16.543 1.00 24.72  ? 649  ARG   A CB  1 
ATOM   764  C CG  . ARG   A 1 112 ? -20.022 -13.682 -17.231 1.00 21.66  ? 649  ARG   A CG  1 
ATOM   765  C CD  . ARG   A 1 112 ? -20.058 -13.566 -18.759 1.00 25.96  ? 649  ARG   A CD  1 
ATOM   766  N NE  . ARG   A 1 112 ? -19.289 -14.646 -19.402 1.00 25.27  ? 649  ARG   A NE  1 
ATOM   767  C CZ  . ARG   A 1 112 ? -19.791 -15.526 -20.272 1.00 27.35  ? 649  ARG   A CZ  1 
ATOM   768  N NH1 . ARG   A 1 112 ? -21.063 -15.486 -20.636 1.00 27.62  ? 649  ARG   A NH1 1 
ATOM   769  N NH2 . ARG   A 1 112 ? -19.006 -16.439 -20.805 1.00 24.55  ? 649  ARG   A NH2 1 
ATOM   770  N N   . PHE   A 1 113 ? -22.556 -13.500 -14.252 1.00 23.98  ? 650  PHE   A N   1 
ATOM   771  C CA  . PHE   A 1 113 ? -22.893 -14.621 -13.380 1.00 23.88  ? 650  PHE   A CA  1 
ATOM   772  C C   . PHE   A 1 113 ? -24.367 -14.967 -13.460 1.00 28.11  ? 650  PHE   A C   1 
ATOM   773  O O   . PHE   A 1 113 ? -24.740 -16.141 -13.391 1.00 30.09  ? 650  PHE   A O   1 
ATOM   774  C CB  . PHE   A 1 113 ? -22.542 -14.277 -11.937 1.00 30.10  ? 650  PHE   A CB  1 
ATOM   775  C CG  . PHE   A 1 113 ? -22.491 -15.457 -11.028 1.00 29.43  ? 650  PHE   A CG  1 
ATOM   776  C CD1 . PHE   A 1 113 ? -23.644 -15.944 -10.417 1.00 29.49  ? 650  PHE   A CD1 1 
ATOM   777  C CD2 . PHE   A 1 113 ? -21.285 -16.074 -10.753 1.00 28.13  ? 650  PHE   A CD2 1 
ATOM   778  C CE1 . PHE   A 1 113 ? -23.579 -17.031 -9.571  1.00 35.47  ? 650  PHE   A CE1 1 
ATOM   779  C CE2 . PHE   A 1 113 ? -21.220 -17.151 -9.902  1.00 25.55  ? 650  PHE   A CE2 1 
ATOM   780  C CZ  . PHE   A 1 113 ? -22.355 -17.626 -9.309  1.00 30.18  ? 650  PHE   A CZ  1 
ATOM   781  N N   . GLU   A 1 114 ? -25.215 -13.953 -13.572 1.00 30.74  ? 651  GLU   A N   1 
ATOM   782  C CA  . GLU   A 1 114 ? -26.656 -14.114 -13.412 1.00 28.75  ? 651  GLU   A CA  1 
ATOM   783  C C   . GLU   A 1 114 ? -27.250 -14.489 -14.769 1.00 36.22  ? 651  GLU   A C   1 
ATOM   784  O O   . GLU   A 1 114 ? -27.880 -13.688 -15.463 1.00 32.52  ? 651  GLU   A O   1 
ATOM   785  C CB  . GLU   A 1 114 ? -27.248 -12.842 -12.817 1.00 32.16  ? 651  GLU   A CB  1 
ATOM   786  C CG  . GLU   A 1 114 ? -26.644 -12.566 -11.425 1.00 40.42  ? 651  GLU   A CG  1 
ATOM   787  C CD  . GLU   A 1 114 ? -27.273 -11.404 -10.690 1.00 51.38  ? 651  GLU   A CD  1 
ATOM   788  O OE1 . GLU   A 1 114 ? -27.773 -10.464 -11.345 1.00 44.49  ? 651  GLU   A OE1 1 
ATOM   789  O OE2 . GLU   A 1 114 ? -27.262 -11.439 -9.442  1.00 48.17  ? 651  GLU   A OE2 1 
ATOM   790  N N   . ILE   A 1 115 ? -27.058 -15.753 -15.129 1.00 31.39  ? 652  ILE   A N   1 
ATOM   791  C CA  . ILE   A 1 115 ? -27.358 -16.244 -16.473 1.00 27.13  ? 652  ILE   A CA  1 
ATOM   792  C C   . ILE   A 1 115 ? -28.819 -16.674 -16.521 1.00 33.24  ? 652  ILE   A C   1 
ATOM   793  O O   . ILE   A 1 115 ? -29.210 -17.595 -15.783 1.00 30.94  ? 652  ILE   A O   1 
ATOM   794  C CB  . ILE   A 1 115 ? -26.442 -17.412 -16.856 1.00 30.42  ? 652  ILE   A CB  1 
ATOM   795  C CG1 . ILE   A 1 115 ? -24.974 -16.989 -16.756 1.00 29.05  ? 652  ILE   A CG1 1 
ATOM   796  C CG2 . ILE   A 1 115 ? -26.789 -17.883 -18.254 1.00 26.06  ? 652  ILE   A CG2 1 
ATOM   797  C CD1 . ILE   A 1 115 ? -23.972 -18.125 -16.791 1.00 30.12  ? 652  ILE   A CD1 1 
ATOM   798  N N   . PRO   A 1 116 ? -29.640 -16.080 -17.383 1.00 28.65  ? 653  PRO   A N   1 
ATOM   799  C CA  . PRO   A 1 116 ? -31.011 -16.563 -17.553 1.00 33.31  ? 653  PRO   A CA  1 
ATOM   800  C C   . PRO   A 1 116 ? -31.049 -17.814 -18.420 1.00 33.85  ? 653  PRO   A C   1 
ATOM   801  O O   . PRO   A 1 116 ? -30.217 -18.004 -19.309 1.00 33.26  ? 653  PRO   A O   1 
ATOM   802  C CB  . PRO   A 1 116 ? -31.705 -15.384 -18.245 1.00 35.84  ? 653  PRO   A CB  1 
ATOM   803  C CG  . PRO   A 1 116 ? -30.633 -14.738 -19.043 1.00 32.98  ? 653  PRO   A CG  1 
ATOM   804  C CD  . PRO   A 1 116 ? -29.347 -14.904 -18.225 1.00 32.21  ? 653  PRO   A CD  1 
ATOM   805  N N   . GLU   A 1 117 ? -32.028 -18.679 -18.150 1.00 35.16  ? 654  GLU   A N   1 
ATOM   806  C CA  . GLU   A 1 117 ? -32.157 -19.865 -18.991 1.00 35.46  ? 654  GLU   A CA  1 
ATOM   807  C C   . GLU   A 1 117 ? -32.956 -19.553 -20.259 1.00 38.54  ? 654  GLU   A C   1 
ATOM   808  O O   . GLU   A 1 117 ? -33.783 -18.637 -20.270 1.00 40.79  ? 654  GLU   A O   1 
ATOM   809  C CB  . GLU   A 1 117 ? -32.816 -21.003 -18.212 1.00 35.98  ? 654  GLU   A CB  1 
ATOM   810  C CG  . GLU   A 1 117 ? -31.941 -21.441 -17.040 1.00 36.19  ? 654  GLU   A CG  1 
ATOM   811  C CD  . GLU   A 1 117 ? -32.474 -22.619 -16.234 1.00 49.50  ? 654  GLU   A CD  1 
ATOM   812  O OE1 . GLU   A 1 117 ? -33.652 -23.007 -16.380 1.00 49.62  ? 654  GLU   A OE1 1 
ATOM   813  O OE2 . GLU   A 1 117 ? -31.683 -23.158 -15.433 1.00 49.44  ? 654  GLU   A OE2 1 
ATOM   814  N N   . PRO   A 1 118 ? -32.690 -20.270 -21.355 1.00 36.11  ? 655  PRO   A N   1 
ATOM   815  C CA  . PRO   A 1 118 ? -33.466 -20.056 -22.581 1.00 40.42  ? 655  PRO   A CA  1 
ATOM   816  C C   . PRO   A 1 118 ? -34.948 -20.297 -22.339 1.00 46.56  ? 655  PRO   A C   1 
ATOM   817  O O   . PRO   A 1 118 ? -35.336 -21.172 -21.559 1.00 44.89  ? 655  PRO   A O   1 
ATOM   818  C CB  . PRO   A 1 118 ? -32.888 -21.093 -23.554 1.00 41.52  ? 655  PRO   A CB  1 
ATOM   819  C CG  . PRO   A 1 118 ? -31.549 -21.401 -23.048 1.00 38.66  ? 655  PRO   A CG  1 
ATOM   820  C CD  . PRO   A 1 118 ? -31.599 -21.240 -21.549 1.00 42.82  ? 655  PRO   A CD  1 
ATOM   821  N N   . GLU   A 1 119 ? -35.781 -19.517 -23.023 1.00 47.94  ? 656  GLU   A N   1 
ATOM   822  C CA  . GLU   A 1 119 ? -37.223 -19.639 -22.842 1.00 58.08  ? 656  GLU   A CA  1 
ATOM   823  C C   . GLU   A 1 119 ? -37.680 -21.021 -23.289 1.00 63.06  ? 656  GLU   A C   1 
ATOM   824  O O   . GLU   A 1 119 ? -37.407 -21.412 -24.431 1.00 70.60  ? 656  GLU   A O   1 
ATOM   825  C CB  . GLU   A 1 119 ? -37.977 -18.560 -23.620 1.00 70.30  ? 656  GLU   A CB  1 
ATOM   826  C CG  . GLU   A 1 119 ? -39.012 -17.807 -22.780 1.00 86.85  ? 656  GLU   A CG  1 
ATOM   827  C CD  . GLU   A 1 119 ? -38.383 -17.082 -21.599 1.00 98.54  ? 656  GLU   A CD  1 
ATOM   828  O OE1 . GLU   A 1 119 ? -37.587 -16.145 -21.826 1.00 100.44 ? 656  GLU   A OE1 1 
ATOM   829  O OE2 . GLU   A 1 119 ? -38.670 -17.461 -20.442 1.00 103.32 ? 656  GLU   A OE2 1 
ATOM   830  N N   . PRO   A 1 120 ? -38.344 -21.793 -22.431 1.00 63.79  ? 657  PRO   A N   1 
ATOM   831  C CA  . PRO   A 1 120 ? -38.772 -23.138 -22.832 1.00 69.30  ? 657  PRO   A CA  1 
ATOM   832  C C   . PRO   A 1 120 ? -39.714 -23.076 -24.022 1.00 62.10  ? 657  PRO   A C   1 
ATOM   833  O O   . PRO   A 1 120 ? -40.518 -22.152 -24.153 1.00 67.34  ? 657  PRO   A O   1 
ATOM   834  C CB  . PRO   A 1 120 ? -39.480 -23.678 -21.580 1.00 74.30  ? 657  PRO   A CB  1 
ATOM   835  C CG  . PRO   A 1 120 ? -38.941 -22.860 -20.451 1.00 74.03  ? 657  PRO   A CG  1 
ATOM   836  C CD  . PRO   A 1 120 ? -38.685 -21.496 -21.028 1.00 72.54  ? 657  PRO   A CD  1 
ATOM   837  N N   . THR   A 1 121 ? -39.580 -24.059 -24.908 1.00 70.04  ? 658  THR   A N   1 
ATOM   838  C CA  . THR   A 1 121 ? -40.477 -24.210 -26.043 1.00 75.95  ? 658  THR   A CA  1 
ATOM   839  C C   . THR   A 1 121 ? -41.746 -24.948 -25.621 1.00 80.98  ? 658  THR   A C   1 
ATOM   840  O O   . THR   A 1 121 ? -41.786 -25.641 -24.599 1.00 80.45  ? 658  THR   A O   1 
ATOM   841  C CB  . THR   A 1 121 ? -39.794 -24.969 -27.185 1.00 80.71  ? 658  THR   A CB  1 
ATOM   842  O OG1 . THR   A 1 121 ? -39.358 -26.253 -26.718 1.00 86.22  ? 658  THR   A OG1 1 
ATOM   843  C CG2 . THR   A 1 121 ? -38.592 -24.188 -27.730 1.00 77.50  ? 658  THR   A CG2 1 
ATOM   844  N N   . ASP   A 1 122 ? -42.800 -24.774 -26.421 1.00 84.99  ? 659  ASP   A N   1 
ATOM   845  C CA  . ASP   A 1 122 ? -44.015 -25.562 -26.248 1.00 91.97  ? 659  ASP   A CA  1 
ATOM   846  C C   . ASP   A 1 122 ? -43.701 -27.036 -26.452 1.00 100.63 ? 659  ASP   A C   1 
ATOM   847  O O   . ASP   A 1 122 ? -43.737 -27.537 -27.583 1.00 111.03 ? 659  ASP   A O   1 
ATOM   848  C CB  . ASP   A 1 122 ? -45.107 -25.124 -27.224 1.00 99.99  ? 659  ASP   A CB  1 
ATOM   849  C CG  . ASP   A 1 122 ? -44.689 -23.947 -28.078 1.00 107.46 ? 659  ASP   A CG  1 
ATOM   850  O OD1 . ASP   A 1 122 ? -45.127 -22.815 -27.785 1.00 109.12 ? 659  ASP   A OD1 1 
ATOM   851  O OD2 . ASP   A 1 122 ? -43.911 -24.150 -29.036 1.00 111.54 ? 659  ASP   A OD2 1 
ATOM   852  N N   . ALA   A 1 123 ? -43.409 -27.718 -25.344 1.00 101.64 ? 660  ALA   A N   1 
ATOM   853  C CA  . ALA   A 1 123 ? -42.926 -29.093 -25.277 1.00 101.20 ? 660  ALA   A CA  1 
ATOM   854  C C   . ALA   A 1 123 ? -42.313 -29.256 -23.897 1.00 94.94  ? 660  ALA   A C   1 
ATOM   855  O O   . ALA   A 1 123 ? -42.624 -30.199 -23.160 1.00 89.23  ? 660  ALA   A O   1 
ATOM   856  C CB  . ALA   A 1 123 ? -41.891 -29.403 -26.361 1.00 102.64 ? 660  ALA   A CB  1 
ATOM   857  N N   . ASP   A 1 124 ? -41.441 -28.309 -23.550 1.00 82.66  ? 661  ASP   A N   1 
ATOM   858  C CA  . ASP   A 1 124 ? -40.948 -28.216 -22.184 1.00 91.03  ? 661  ASP   A CA  1 
ATOM   859  C C   . ASP   A 1 124 ? -42.071 -27.829 -21.227 1.00 96.52  ? 661  ASP   A C   1 
ATOM   860  O O   . ASP   A 1 124 ? -42.183 -28.395 -20.133 1.00 102.17 ? 661  ASP   A O   1 
ATOM   861  C CB  . ASP   A 1 124 ? -39.800 -27.204 -22.112 1.00 85.62  ? 661  ASP   A CB  1 
ATOM   862  C CG  . ASP   A 1 124 ? -38.734 -27.441 -23.173 1.00 78.28  ? 661  ASP   A CG  1 
ATOM   863  O OD1 . ASP   A 1 124 ? -38.747 -28.518 -23.800 1.00 78.09  ? 661  ASP   A OD1 1 
ATOM   864  O OD2 . ASP   A 1 124 ? -37.886 -26.542 -23.383 1.00 71.22  ? 661  ASP   A OD2 1 
ATOM   865  N N   . LYS   A 1 125 ? -42.922 -26.885 -21.627 1.00 91.86  ? 662  LYS   A N   1 
ATOM   866  C CA  . LYS   A 1 125 ? -43.999 -26.386 -20.770 1.00 89.71  ? 662  LYS   A CA  1 
ATOM   867  C C   . LYS   A 1 125 ? -45.047 -27.456 -20.451 1.00 89.66  ? 662  LYS   A C   1 
ATOM   868  O O   . LYS   A 1 125 ? -45.539 -27.557 -19.324 1.00 87.26  ? 662  LYS   A O   1 
ATOM   869  C CB  . LYS   A 1 125 ? -44.675 -25.174 -21.422 1.00 89.27  ? 662  LYS   A CB  1 
ATOM   870  C CG  . LYS   A 1 125 ? -43.738 -23.990 -21.610 1.00 87.72  ? 662  LYS   A CG  1 
ATOM   871  C CD  . LYS   A 1 125 ? -44.490 -22.690 -21.855 1.00 89.50  ? 662  LYS   A CD  1 
ATOM   872  C CE  . LYS   A 1 125 ? -43.606 -21.499 -21.516 1.00 86.03  ? 662  LYS   A CE  1 
ATOM   873  N NZ  . LYS   A 1 125 ? -43.754 -20.370 -22.479 1.00 89.71  ? 662  LYS   A NZ  1 
ATOM   874  N N   . ILE   A 1 135 ? -36.581 -32.393 -16.940 1.00 93.52  ? 672  ILE   A N   1 
ATOM   875  C CA  . ILE   A 1 135 ? -35.876 -31.258 -17.532 1.00 84.19  ? 672  ILE   A CA  1 
ATOM   876  C C   . ILE   A 1 135 ? -35.421 -31.634 -18.943 1.00 83.75  ? 672  ILE   A C   1 
ATOM   877  O O   . ILE   A 1 135 ? -34.863 -32.707 -19.145 1.00 90.00  ? 672  ILE   A O   1 
ATOM   878  C CB  . ILE   A 1 135 ? -34.696 -30.822 -16.639 1.00 75.77  ? 672  ILE   A CB  1 
ATOM   879  C CG1 . ILE   A 1 135 ? -35.221 -30.089 -15.400 1.00 79.18  ? 672  ILE   A CG1 1 
ATOM   880  C CG2 . ILE   A 1 135 ? -33.710 -29.964 -17.416 1.00 67.03  ? 672  ILE   A CG2 1 
ATOM   881  C CD1 . ILE   A 1 135 ? -34.375 -30.279 -14.155 1.00 79.06  ? 672  ILE   A CD1 1 
ATOM   882  N N   . SER   A 1 136 ? -35.672 -30.756 -19.914 1.00 74.69  ? 673  SER   A N   1 
ATOM   883  C CA  . SER   A 1 136 ? -35.360 -31.067 -21.303 1.00 65.93  ? 673  SER   A CA  1 
ATOM   884  C C   . SER   A 1 136 ? -33.867 -31.330 -21.478 1.00 51.61  ? 673  SER   A C   1 
ATOM   885  O O   . SER   A 1 136 ? -33.037 -30.923 -20.658 1.00 47.34  ? 673  SER   A O   1 
ATOM   886  C CB  . SER   A 1 136 ? -35.793 -29.924 -22.218 1.00 55.59  ? 673  SER   A CB  1 
ATOM   887  O OG  . SER   A 1 136 ? -34.833 -28.880 -22.186 1.00 55.58  ? 673  SER   A OG  1 
ATOM   888  N N   . ALA   A 1 137 ? -33.527 -32.036 -22.559 1.00 51.51  ? 674  ALA   A N   1 
ATOM   889  C CA  . ALA   A 1 137 ? -32.122 -32.352 -22.807 1.00 54.70  ? 674  ALA   A CA  1 
ATOM   890  C C   . ALA   A 1 137 ? -31.318 -31.093 -23.117 1.00 49.74  ? 674  ALA   A C   1 
ATOM   891  O O   . ALA   A 1 137 ? -30.160 -30.966 -22.693 1.00 45.13  ? 674  ALA   A O   1 
ATOM   892  C CB  . ALA   A 1 137 ? -32.009 -33.373 -23.942 1.00 58.17  ? 674  ALA   A CB  1 
ATOM   893  N N   . ASP   A 1 138 ? -31.926 -30.140 -23.834 1.00 57.04  ? 675  ASP   A N   1 
ATOM   894  C CA  . ASP   A 1 138 ? -31.246 -28.883 -24.143 1.00 52.26  ? 675  ASP   A CA  1 
ATOM   895  C C   . ASP   A 1 138 ? -30.950 -28.090 -22.880 1.00 43.30  ? 675  ASP   A C   1 
ATOM   896  O O   . ASP   A 1 138 ? -29.869 -27.500 -22.744 1.00 37.73  ? 675  ASP   A O   1 
ATOM   897  C CB  . ASP   A 1 138 ? -32.094 -28.041 -25.100 1.00 56.98  ? 675  ASP   A CB  1 
ATOM   898  C CG  . ASP   A 1 138 ? -32.063 -28.563 -26.519 1.00 78.30  ? 675  ASP   A CG  1 
ATOM   899  O OD1 . ASP   A 1 138 ? -31.421 -29.608 -26.757 1.00 83.87  ? 675  ASP   A OD1 1 
ATOM   900  O OD2 . ASP   A 1 138 ? -32.676 -27.923 -27.399 1.00 89.17  ? 675  ASP   A OD2 1 
ATOM   901  N N   . LEU   A 1 139 ? -31.903 -28.058 -21.946 1.00 39.38  ? 676  LEU   A N   1 
ATOM   902  C CA  . LEU   A 1 139 ? -31.717 -27.300 -20.714 1.00 40.03  ? 676  LEU   A CA  1 
ATOM   903  C C   . LEU   A 1 139 ? -30.687 -27.962 -19.809 1.00 38.99  ? 676  LEU   A C   1 
ATOM   904  O O   . LEU   A 1 139 ? -29.879 -27.272 -19.174 1.00 39.26  ? 676  LEU   A O   1 
ATOM   905  C CB  . LEU   A 1 139 ? -33.054 -27.146 -19.988 1.00 50.80  ? 676  LEU   A CB  1 
ATOM   906  C CG  . LEU   A 1 139 ? -33.030 -26.301 -18.709 1.00 55.88  ? 676  LEU   A CG  1 
ATOM   907  C CD1 . LEU   A 1 139 ? -32.458 -24.929 -18.993 1.00 52.53  ? 676  LEU   A CD1 1 
ATOM   908  C CD2 . LEU   A 1 139 ? -34.432 -26.192 -18.093 1.00 53.40  ? 676  LEU   A CD2 1 
ATOM   909  N N   . LYS   A 1 140 ? -30.699 -29.299 -19.732 1.00 39.67  ? 677  LYS   A N   1 
ATOM   910  C CA  . LYS   A 1 140 ? -29.658 -29.988 -18.977 1.00 37.81  ? 677  LYS   A CA  1 
ATOM   911  C C   . LYS   A 1 140 ? -28.283 -29.670 -19.548 1.00 36.04  ? 677  LYS   A C   1 
ATOM   912  O O   . LYS   A 1 140 ? -27.348 -29.352 -18.802 1.00 34.60  ? 677  LYS   A O   1 
ATOM   913  C CB  . LYS   A 1 140 ? -29.911 -31.499 -18.970 1.00 43.91  ? 677  LYS   A CB  1 
ATOM   914  C CG  . LYS   A 1 140 ? -28.911 -32.266 -18.107 1.00 53.41  ? 677  LYS   A CG  1 
ATOM   915  C CD  . LYS   A 1 140 ? -29.161 -33.764 -18.130 1.00 65.63  ? 677  LYS   A CD  1 
ATOM   916  C CE  . LYS   A 1 140 ? -28.151 -34.507 -17.267 1.00 69.45  ? 677  LYS   A CE  1 
ATOM   917  N NZ  . LYS   A 1 140 ? -28.540 -35.932 -17.051 1.00 68.52  ? 677  LYS   A NZ  1 
ATOM   918  N N   . ARG   A 1 141 ? -28.149 -29.729 -20.880 1.00 37.45  ? 678  ARG   A N   1 
ATOM   919  C CA  . ARG   A 1 141 ? -26.908 -29.301 -21.534 1.00 44.28  ? 678  ARG   A CA  1 
ATOM   920  C C   . ARG   A 1 141 ? -26.524 -27.886 -21.120 1.00 38.35  ? 678  ARG   A C   1 
ATOM   921  O O   . ARG   A 1 141 ? -25.358 -27.597 -20.811 1.00 34.51  ? 678  ARG   A O   1 
ATOM   922  C CB  . ARG   A 1 141 ? -27.064 -29.351 -23.054 1.00 42.76  ? 678  ARG   A CB  1 
ATOM   923  C CG  . ARG   A 1 141 ? -26.383 -30.482 -23.761 1.00 63.04  ? 678  ARG   A CG  1 
ATOM   924  C CD  . ARG   A 1 141 ? -26.321 -30.183 -25.255 1.00 61.54  ? 678  ARG   A CD  1 
ATOM   925  N NE  . ARG   A 1 141 ? -25.055 -29.556 -25.640 1.00 53.39  ? 678  ARG   A NE  1 
ATOM   926  C CZ  . ARG   A 1 141 ? -24.757 -29.173 -26.877 1.00 43.76  ? 678  ARG   A CZ  1 
ATOM   927  N NH1 . ARG   A 1 141 ? -25.638 -29.333 -27.853 1.00 40.08  ? 678  ARG   A NH1 1 
ATOM   928  N NH2 . ARG   A 1 141 ? -23.576 -28.630 -27.140 1.00 45.88  ? 678  ARG   A NH2 1 
ATOM   929  N N   . PHE   A 1 142 ? -27.499 -26.978 -21.145 1.00 35.90  ? 679  PHE   A N   1 
ATOM   930  C CA  . PHE   A 1 142 ? -27.215 -25.577 -20.861 1.00 33.47  ? 679  PHE   A CA  1 
ATOM   931  C C   . PHE   A 1 142 ? -26.662 -25.394 -19.449 1.00 31.80  ? 679  PHE   A C   1 
ATOM   932  O O   . PHE   A 1 142 ? -25.659 -24.699 -19.249 1.00 30.27  ? 679  PHE   A O   1 
ATOM   933  C CB  . PHE   A 1 142 ? -28.484 -24.743 -21.063 1.00 34.96  ? 679  PHE   A CB  1 
ATOM   934  C CG  . PHE   A 1 142 ? -28.273 -23.271 -20.841 1.00 33.13  ? 679  PHE   A CG  1 
ATOM   935  C CD1 . PHE   A 1 142 ? -27.538 -22.525 -21.746 1.00 35.61  ? 679  PHE   A CD1 1 
ATOM   936  C CD2 . PHE   A 1 142 ? -28.815 -22.629 -19.732 1.00 37.24  ? 679  PHE   A CD2 1 
ATOM   937  C CE1 . PHE   A 1 142 ? -27.329 -21.163 -21.549 1.00 34.24  ? 679  PHE   A CE1 1 
ATOM   938  C CE2 . PHE   A 1 142 ? -28.614 -21.256 -19.531 1.00 32.72  ? 679  PHE   A CE2 1 
ATOM   939  C CZ  . PHE   A 1 142 ? -27.873 -20.529 -20.440 1.00 34.96  ? 679  PHE   A CZ  1 
ATOM   940  N N   . ARG   A 1 143 ? -27.279 -26.040 -18.457 1.00 32.66  ? 680  ARG   A N   1 
ATOM   941  C CA  . ARG   A 1 143 ? -26.812 -25.844 -17.087 1.00 35.11  ? 680  ARG   A CA  1 
ATOM   942  C C   . ARG   A 1 143 ? -25.439 -26.459 -16.866 1.00 31.90  ? 680  ARG   A C   1 
ATOM   943  O O   . ARG   A 1 143 ? -24.650 -25.942 -16.074 1.00 33.10  ? 680  ARG   A O   1 
ATOM   944  C CB  . ARG   A 1 143 ? -27.815 -26.434 -16.103 1.00 36.45  ? 680  ARG   A CB  1 
ATOM   945  C CG  . ARG   A 1 143 ? -29.187 -25.787 -16.157 1.00 38.76  ? 680  ARG   A CG  1 
ATOM   946  C CD  . ARG   A 1 143 ? -30.142 -26.539 -15.263 1.00 43.80  ? 680  ARG   A CD  1 
ATOM   947  N NE  . ARG   A 1 143 ? -31.422 -25.856 -15.162 1.00 47.45  ? 680  ARG   A NE  1 
ATOM   948  C CZ  . ARG   A 1 143 ? -32.460 -26.331 -14.490 1.00 52.11  ? 680  ARG   A CZ  1 
ATOM   949  N NH1 . ARG   A 1 143 ? -32.364 -27.493 -13.858 1.00 53.35  ? 680  ARG   A NH1 1 
ATOM   950  N NH2 . ARG   A 1 143 ? -33.590 -25.642 -14.452 1.00 60.09  ? 680  ARG   A NH2 1 
ATOM   951  N N   . LYS   A 1 144 ? -25.149 -27.557 -17.552 1.00 32.05  ? 681  LYS   A N   1 
ATOM   952  C CA  . LYS   A 1 144 ? -23.916 -28.312 -17.355 1.00 31.39  ? 681  LYS   A CA  1 
ATOM   953  C C   . LYS   A 1 144 ? -22.762 -27.771 -18.188 1.00 35.52  ? 681  LYS   A C   1 
ATOM   954  O O   . LYS   A 1 144 ? -21.638 -27.665 -17.686 1.00 32.58  ? 681  LYS   A O   1 
ATOM   955  C CB  . LYS   A 1 144 ? -24.167 -29.781 -17.695 1.00 37.66  ? 681  LYS   A CB  1 
ATOM   956  C CG  . LYS   A 1 144 ? -23.088 -30.770 -17.304 1.00 53.21  ? 681  LYS   A CG  1 
ATOM   957  C CD  . LYS   A 1 144 ? -23.609 -32.217 -17.481 1.00 64.55  ? 681  LYS   A CD  1 
ATOM   958  C CE  . LYS   A 1 144 ? -22.487 -33.236 -17.421 1.00 78.56  ? 681  LYS   A CE  1 
ATOM   959  N NZ  . LYS   A 1 144 ? -21.393 -32.862 -18.358 1.00 83.89  ? 681  LYS   A NZ  1 
ATOM   960  N N   . GLU   A 1 145 ? -23.024 -27.438 -19.456 1.00 32.20  ? 682  GLU   A N   1 
ATOM   961  C CA  . GLU   A 1 145 ? -21.984 -27.001 -20.377 1.00 31.72  ? 682  GLU   A CA  1 
ATOM   962  C C   . GLU   A 1 145 ? -21.761 -25.502 -20.362 1.00 29.89  ? 682  GLU   A C   1 
ATOM   963  O O   . GLU   A 1 145 ? -20.690 -25.043 -20.775 1.00 35.37  ? 682  GLU   A O   1 
ATOM   964  C CB  . GLU   A 1 145 ? -22.320 -27.414 -21.814 1.00 36.32  ? 682  GLU   A CB  1 
ATOM   965  C CG  . GLU   A 1 145 ? -22.372 -28.902 -22.029 1.00 51.99  ? 682  GLU   A CG  1 
ATOM   966  C CD  . GLU   A 1 145 ? -22.605 -29.265 -23.484 1.00 53.59  ? 682  GLU   A CD  1 
ATOM   967  O OE1 . GLU   A 1 145 ? -22.212 -28.483 -24.377 1.00 55.37  ? 682  GLU   A OE1 1 
ATOM   968  O OE2 . GLU   A 1 145 ? -23.191 -30.335 -23.728 1.00 66.55  ? 682  GLU   A OE2 1 
ATOM   969  N N   . TYR   A 1 146 ? -22.740 -24.720 -19.911 1.00 28.06  ? 683  TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 146 ? -22.625 -23.270 -19.999 1.00 25.30  ? 683  TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 146 ? -22.708 -22.593 -18.639 1.00 30.03  ? 683  TYR   A C   1 
ATOM   972  O O   . TYR   A 1 146 ? -21.755 -21.906 -18.243 1.00 27.47  ? 683  TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 146 ? -23.688 -22.704 -20.954 1.00 30.19  ? 683  TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 146 ? -23.408 -21.268 -21.325 1.00 27.68  ? 683  TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 146 ? -22.600 -20.953 -22.411 1.00 29.50  ? 683  TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 146 ? -23.927 -20.227 -20.570 1.00 30.44  ? 683  TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 146 ? -22.317 -19.617 -22.737 1.00 26.41  ? 683  TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 146 ? -23.661 -18.909 -20.887 1.00 28.99  ? 683  TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 146 ? -22.860 -18.616 -21.973 1.00 32.27  ? 683  TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 146 ? -22.595 -17.304 -22.296 1.00 28.67  ? 683  TYR   A OH  1 
ATOM   981  N N   . VAL   A 1 147 ? -23.802 -22.775 -17.899 1.00 26.92  ? 684  VAL   A N   1 
ATOM   982  C CA  . VAL   A 1 147 ? -24.011 -22.007 -16.671 1.00 27.17  ? 684  VAL   A CA  1 
ATOM   983  C C   . VAL   A 1 147 ? -22.938 -22.328 -15.631 1.00 31.53  ? 684  VAL   A C   1 
ATOM   984  O O   . VAL   A 1 147 ? -22.279 -21.427 -15.101 1.00 30.07  ? 684  VAL   A O   1 
ATOM   985  C CB  . VAL   A 1 147 ? -25.411 -22.257 -16.093 1.00 30.83  ? 684  VAL   A CB  1 
ATOM   986  C CG1 . VAL   A 1 147 ? -25.540 -21.477 -14.795 1.00 30.97  ? 684  VAL   A CG1 1 
ATOM   987  C CG2 . VAL   A 1 147 ? -26.479 -21.818 -17.075 1.00 29.43  ? 684  VAL   A CG2 1 
ATOM   988  N N   . GLN   A 1 148 ? -22.797 -23.605 -15.264 1.00 31.80  ? 685  GLN   A N   1 
ATOM   989  C CA  . GLN   A 1 148 ? -21.840 -23.914 -14.201 1.00 26.10  ? 685  GLN   A CA  1 
ATOM   990  C C   . GLN   A 1 148 ? -20.414 -23.547 -14.594 1.00 26.88  ? 685  GLN   A C   1 
ATOM   991  O O   . GLN   A 1 148 ? -19.735 -22.876 -13.796 1.00 28.87  ? 685  GLN   A O   1 
ATOM   992  C CB  . GLN   A 1 148 ? -21.954 -25.380 -13.760 1.00 38.68  ? 685  GLN   A CB  1 
ATOM   993  C CG  . GLN   A 1 148 ? -21.041 -25.650 -12.565 1.00 41.35  ? 685  GLN   A CG  1 
ATOM   994  C CD  . GLN   A 1 148 ? -21.321 -26.958 -11.853 1.00 57.34  ? 685  GLN   A CD  1 
ATOM   995  O OE1 . GLN   A 1 148 ? -22.225 -27.042 -11.023 1.00 59.02  ? 685  GLN   A OE1 1 
ATOM   996  N NE2 . GLN   A 1 148 ? -20.527 -27.981 -12.159 1.00 54.42  ? 685  GLN   A NE2 1 
ATOM   997  N N   . PRO   A 1 149 ? -19.907 -23.896 -15.787 1.00 26.71  ? 686  PRO   A N   1 
ATOM   998  C CA  . PRO   A 1 149 ? -18.530 -23.483 -16.119 1.00 29.76  ? 686  PRO   A CA  1 
ATOM   999  C C   . PRO   A 1 149 ? -18.322 -21.982 -16.087 1.00 32.28  ? 686  PRO   A C   1 
ATOM   1000 O O   . PRO   A 1 149 ? -17.306 -21.525 -15.548 1.00 29.09  ? 686  PRO   A O   1 
ATOM   1001 C CB  . PRO   A 1 149 ? -18.328 -24.047 -17.530 1.00 27.53  ? 686  PRO   A CB  1 
ATOM   1002 C CG  . PRO   A 1 149 ? -19.226 -25.251 -17.562 1.00 29.63  ? 686  PRO   A CG  1 
ATOM   1003 C CD  . PRO   A 1 149 ? -20.452 -24.806 -16.812 1.00 28.34  ? 686  PRO   A CD  1 
ATOM   1004 N N   . VAL   A 1 150 ? -19.252 -21.197 -16.641 1.00 28.24  ? 687  VAL   A N   1 
ATOM   1005 C CA  . VAL   A 1 150 ? -19.081 -19.743 -16.623 1.00 23.95  ? 687  VAL   A CA  1 
ATOM   1006 C C   . VAL   A 1 150 ? -19.066 -19.221 -15.194 1.00 29.39  ? 687  VAL   A C   1 
ATOM   1007 O O   . VAL   A 1 150 ? -18.242 -18.365 -14.836 1.00 27.89  ? 687  VAL   A O   1 
ATOM   1008 C CB  . VAL   A 1 150 ? -20.175 -19.050 -17.456 1.00 26.14  ? 687  VAL   A CB  1 
ATOM   1009 C CG1 . VAL   A 1 150 ? -20.159 -17.552 -17.175 1.00 23.36  ? 687  VAL   A CG1 1 
ATOM   1010 C CG2 . VAL   A 1 150 ? -19.937 -19.295 -18.924 1.00 24.02  ? 687  VAL   A CG2 1 
ATOM   1011 N N   . GLN   A 1 151 ? -19.977 -19.717 -14.357 1.00 27.12  ? 688  GLN   A N   1 
ATOM   1012 C CA  . GLN   A 1 151 ? -20.026 -19.263 -12.970 1.00 27.72  ? 688  GLN   A CA  1 
ATOM   1013 C C   . GLN   A 1 151 ? -18.730 -19.589 -12.233 1.00 27.92  ? 688  GLN   A C   1 
ATOM   1014 O O   . GLN   A 1 151 ? -18.223 -18.767 -11.467 1.00 26.75  ? 688  GLN   A O   1 
ATOM   1015 C CB  . GLN   A 1 151 ? -21.237 -19.878 -12.268 1.00 24.11  ? 688  GLN   A CB  1 
ATOM   1016 C CG  . GLN   A 1 151 ? -22.526 -19.198 -12.781 1.00 25.10  ? 688  GLN   A CG  1 
ATOM   1017 C CD  . GLN   A 1 151 ? -23.783 -19.687 -12.123 1.00 30.94  ? 688  GLN   A CD  1 
ATOM   1018 O OE1 . GLN   A 1 151 ? -23.802 -20.755 -11.508 1.00 28.64  ? 688  GLN   A OE1 1 
ATOM   1019 N NE2 . GLN   A 1 151 ? -24.870 -18.909 -12.267 1.00 31.68  ? 688  GLN   A NE2 1 
ATOM   1020 N N   . LEU   A 1 152 ? -18.170 -20.778 -12.463 1.00 29.82  ? 689  LEU   A N   1 
ATOM   1021 C CA  . LEU   A 1 152 ? -16.896 -21.123 -11.833 1.00 28.07  ? 689  LEU   A CA  1 
ATOM   1022 C C   . LEU   A 1 152 ? -15.748 -20.285 -12.389 1.00 29.91  ? 689  LEU   A C   1 
ATOM   1023 O O   . LEU   A 1 152 ? -14.806 -19.960 -11.650 1.00 26.96  ? 689  LEU   A O   1 
ATOM   1024 C CB  . LEU   A 1 152 ? -16.600 -22.609 -12.023 1.00 28.73  ? 689  LEU   A CB  1 
ATOM   1025 C CG  . LEU   A 1 152 ? -17.583 -23.623 -11.409 1.00 31.96  ? 689  LEU   A CG  1 
ATOM   1026 C CD1 . LEU   A 1 152 ? -17.234 -25.036 -11.831 1.00 36.67  ? 689  LEU   A CD1 1 
ATOM   1027 C CD2 . LEU   A 1 152 ? -17.576 -23.530 -9.885  1.00 43.13  ? 689  LEU   A CD2 1 
ATOM   1028 N N   . ARG   A 1 153 ? -15.790 -19.939 -13.682 1.00 27.27  ? 690  ARG   A N   1 
ATOM   1029 C CA  . ARG   A 1 153 ? -14.775 -19.039 -14.227 1.00 29.59  ? 690  ARG   A CA  1 
ATOM   1030 C C   . ARG   A 1 153 ? -14.817 -17.700 -13.513 1.00 31.40  ? 690  ARG   A C   1 
ATOM   1031 O O   . ARG   A 1 153 ? -13.777 -17.102 -13.220 1.00 27.67  ? 690  ARG   A O   1 
ATOM   1032 C CB  . ARG   A 1 153 ? -14.988 -18.800 -15.720 1.00 30.72  ? 690  ARG   A CB  1 
ATOM   1033 C CG  . ARG   A 1 153 ? -15.037 -20.034 -16.599 1.00 41.63  ? 690  ARG   A CG  1 
ATOM   1034 C CD  . ARG   A 1 153 ? -13.682 -20.590 -16.950 1.00 35.40  ? 690  ARG   A CD  1 
ATOM   1035 N NE  . ARG   A 1 153 ? -13.859 -21.656 -17.920 1.00 39.05  ? 690  ARG   A NE  1 
ATOM   1036 C CZ  . ARG   A 1 153 ? -13.406 -22.890 -17.762 1.00 47.70  ? 690  ARG   A CZ  1 
ATOM   1037 N NH1 . ARG   A 1 153 ? -12.692 -23.205 -16.688 1.00 49.34  ? 690  ARG   A NH1 1 
ATOM   1038 N NH2 . ARG   A 1 153 ? -13.642 -23.794 -18.696 1.00 46.50  ? 690  ARG   A NH2 1 
ATOM   1039 N N   . ILE   A 1 154 ? -16.023 -17.196 -13.259 1.00 26.93  ? 691  ILE   A N   1 
ATOM   1040 C CA  . ILE   A 1 154 ? -16.167 -15.910 -12.584 1.00 24.46  ? 691  ILE   A CA  1 
ATOM   1041 C C   . ILE   A 1 154 ? -15.598 -15.986 -11.180 1.00 27.82  ? 691  ILE   A C   1 
ATOM   1042 O O   . ILE   A 1 154 ? -14.895 -15.075 -10.731 1.00 28.11  ? 691  ILE   A O   1 
ATOM   1043 C CB  . ILE   A 1 154 ? -17.648 -15.485 -12.559 1.00 22.72  ? 691  ILE   A CB  1 
ATOM   1044 C CG1 . ILE   A 1 154 ? -18.133 -15.151 -13.969 1.00 25.40  ? 691  ILE   A CG1 1 
ATOM   1045 C CG2 . ILE   A 1 154 ? -17.850 -14.289 -11.629 1.00 25.07  ? 691  ILE   A CG2 1 
ATOM   1046 C CD1 . ILE   A 1 154 ? -19.653 -15.279 -14.101 1.00 25.88  ? 691  ILE   A CD1 1 
ATOM   1047 N N   . LEU   A 1 155 ? -15.914 -17.061 -10.451 1.00 24.57  ? 692  LEU   A N   1 
ATOM   1048 C CA  . LEU   A 1 155 ? -15.367 -17.192 -9.103  1.00 26.55  ? 692  LEU   A CA  1 
ATOM   1049 C C   . LEU   A 1 155 ? -13.851 -17.283 -9.132  1.00 31.06  ? 692  LEU   A C   1 
ATOM   1050 O O   . LEU   A 1 155 ? -13.183 -16.817 -8.200  1.00 28.54  ? 692  LEU   A O   1 
ATOM   1051 C CB  . LEU   A 1 155 ? -15.969 -18.412 -8.399  1.00 31.00  ? 692  LEU   A CB  1 
ATOM   1052 C CG  . LEU   A 1 155 ? -17.476 -18.273 -8.150  1.00 30.63  ? 692  LEU   A CG  1 
ATOM   1053 C CD1 . LEU   A 1 155 ? -18.065 -19.505 -7.479  1.00 31.30  ? 692  LEU   A CD1 1 
ATOM   1054 C CD2 . LEU   A 1 155 ? -17.762 -17.042 -7.318  1.00 29.67  ? 692  LEU   A CD2 1 
ATOM   1055 N N   . ASN   A 1 156 ? -13.289 -17.880 -10.187 1.00 28.33  ? 693  ASN   A N   1 
ATOM   1056 C CA  . ASN   A 1 156 ? -11.836 -17.915 -10.299 1.00 28.81  ? 693  ASN   A CA  1 
ATOM   1057 C C   . ASN   A 1 156 ? -11.278 -16.520 -10.534 1.00 25.50  ? 693  ASN   A C   1 
ATOM   1058 O O   . ASN   A 1 156 ? -10.245 -16.153 -9.959  1.00 29.56  ? 693  ASN   A O   1 
ATOM   1059 C CB  . ASN   A 1 156 ? -11.404 -18.857 -11.423 1.00 25.83  ? 693  ASN   A CB  1 
ATOM   1060 C CG  . ASN   A 1 156 ? -9.903  -18.869 -11.603 1.00 37.11  ? 693  ASN   A CG  1 
ATOM   1061 O OD1 . ASN   A 1 156 ? -9.164  -19.370 -10.743 1.00 41.14  ? 693  ASN   A OD1 1 
ATOM   1062 N ND2 . ASN   A 1 156 ? -9.437  -18.302 -12.712 1.00 33.88  ? 693  ASN   A ND2 1 
ATOM   1063 N N   . VAL   A 1 157 ? -11.957 -15.725 -11.364 1.00 27.00  ? 694  VAL   A N   1 
ATOM   1064 C CA  . VAL   A 1 157 ? -11.541 -14.338 -11.572 1.00 25.54  ? 694  VAL   A CA  1 
ATOM   1065 C C   . VAL   A 1 157 ? -11.596 -13.556 -10.259 1.00 28.46  ? 694  VAL   A C   1 
ATOM   1066 O O   . VAL   A 1 157 ? -10.662 -12.811 -9.927  1.00 27.33  ? 694  VAL   A O   1 
ATOM   1067 C CB  . VAL   A 1 157 ? -12.404 -13.687 -12.671 1.00 23.97  ? 694  VAL   A CB  1 
ATOM   1068 C CG1 . VAL   A 1 157 ? -12.151 -12.174 -12.725 1.00 24.78  ? 694  VAL   A CG1 1 
ATOM   1069 C CG2 . VAL   A 1 157 ? -12.076 -14.338 -14.025 1.00 23.87  ? 694  VAL   A CG2 1 
ATOM   1070 N N   . PHE   A 1 158 ? -12.673 -13.730 -9.476  1.00 25.41  ? 695  PHE   A N   1 
ATOM   1071 C CA  . PHE   A 1 158 ? -12.752 -13.048 -8.181  1.00 24.09  ? 695  PHE   A CA  1 
ATOM   1072 C C   . PHE   A 1 158 ? -11.584 -13.452 -7.291  1.00 25.23  ? 695  PHE   A C   1 
ATOM   1073 O O   . PHE   A 1 158 ? -11.004 -12.612 -6.587  1.00 27.89  ? 695  PHE   A O   1 
ATOM   1074 C CB  . PHE   A 1 158 ? -14.054 -13.384 -7.446  1.00 22.22  ? 695  PHE   A CB  1 
ATOM   1075 C CG  . PHE   A 1 158 ? -15.299 -12.730 -8.007  1.00 27.09  ? 695  PHE   A CG  1 
ATOM   1076 C CD1 . PHE   A 1 158 ? -15.248 -11.548 -8.721  1.00 27.90  ? 695  PHE   A CD1 1 
ATOM   1077 C CD2 . PHE   A 1 158 ? -16.537 -13.315 -7.774  1.00 28.21  ? 695  PHE   A CD2 1 
ATOM   1078 C CE1 . PHE   A 1 158 ? -16.416 -10.955 -9.201  1.00 28.15  ? 695  PHE   A CE1 1 
ATOM   1079 C CE2 . PHE   A 1 158 ? -17.699 -12.738 -8.250  1.00 27.41  ? 695  PHE   A CE2 1 
ATOM   1080 C CZ  . PHE   A 1 158 ? -17.646 -11.561 -8.969  1.00 24.53  ? 695  PHE   A CZ  1 
ATOM   1081 N N   A ARG   A 1 159 ? -11.240 -14.743 -7.296  0.52 25.57  ? 696  ARG   A N   1 
ATOM   1082 N N   B ARG   A 1 159 ? -11.236 -14.743 -7.292  0.48 25.55  ? 696  ARG   A N   1 
ATOM   1083 C CA  A ARG   A 1 159 ? -10.140 -15.225 -6.467  0.52 25.68  ? 696  ARG   A CA  1 
ATOM   1084 C CA  B ARG   A 1 159 ? -10.138 -15.208 -6.451  0.48 25.58  ? 696  ARG   A CA  1 
ATOM   1085 C C   A ARG   A 1 159 ? -8.827  -14.591 -6.892  0.52 28.46  ? 696  ARG   A C   1 
ATOM   1086 C C   B ARG   A 1 159 ? -8.823  -14.584 -6.890  0.48 28.37  ? 696  ARG   A C   1 
ATOM   1087 O O   A ARG   A 1 159 ? -8.060  -14.103 -6.056  0.52 29.47  ? 696  ARG   A O   1 
ATOM   1088 O O   B ARG   A 1 159 ? -8.049  -14.097 -6.059  0.48 29.61  ? 696  ARG   A O   1 
ATOM   1089 C CB  A ARG   A 1 159 ? -10.046 -16.750 -6.548  0.52 27.62  ? 696  ARG   A CB  1 
ATOM   1090 C CB  B ARG   A 1 159 ? -10.040 -16.735 -6.487  0.48 28.35  ? 696  ARG   A CB  1 
ATOM   1091 C CG  A ARG   A 1 159 ? -8.971  -17.357 -5.650  0.52 37.18  ? 696  ARG   A CG  1 
ATOM   1092 C CG  B ARG   A 1 159 ? -8.950  -17.302 -5.568  0.48 36.64  ? 696  ARG   A CG  1 
ATOM   1093 C CD  A ARG   A 1 159 ? -8.915  -18.876 -5.794  0.52 40.42  ? 696  ARG   A CD  1 
ATOM   1094 C CD  B ARG   A 1 159 ? -8.412  -18.619 -6.101  0.48 45.57  ? 696  ARG   A CD  1 
ATOM   1095 N NE  A ARG   A 1 159 ? -8.475  -19.260 -7.132  0.52 44.73  ? 696  ARG   A NE  1 
ATOM   1096 N NE  B ARG   A 1 159 ? -8.293  -18.533 -7.549  0.48 46.81  ? 696  ARG   A NE  1 
ATOM   1097 C CZ  A ARG   A 1 159 ? -8.246  -20.509 -7.520  0.52 44.97  ? 696  ARG   A CZ  1 
ATOM   1098 C CZ  B ARG   A 1 159 ? -7.278  -17.967 -8.194  0.48 39.30  ? 696  ARG   A CZ  1 
ATOM   1099 N NH1 A ARG   A 1 159 ? -7.849  -20.750 -8.763  0.52 45.53  ? 696  ARG   A NH1 1 
ATOM   1100 N NH1 B ARG   A 1 159 ? -7.303  -17.922 -9.514  0.48 32.97  ? 696  ARG   A NH1 1 
ATOM   1101 N NH2 A ARG   A 1 159 ? -8.412  -21.511 -6.666  0.52 32.00  ? 696  ARG   A NH2 1 
ATOM   1102 N NH2 B ARG   A 1 159 ? -6.248  -17.444 -7.528  0.48 38.19  ? 696  ARG   A NH2 1 
ATOM   1103 N N   . HIS   A 1 160 ? -8.554  -14.590 -8.199  1.00 29.47  ? 697  HIS   A N   1 
ATOM   1104 C CA  . HIS   A 1 160 ? -7.337  -13.961 -8.698  1.00 30.96  ? 697  HIS   A CA  1 
ATOM   1105 C C   . HIS   A 1 160 ? -7.339  -12.474 -8.389  1.00 31.84  ? 697  HIS   A C   1 
ATOM   1106 O O   . HIS   A 1 160 ? -6.294  -11.906 -8.067  1.00 29.30  ? 697  HIS   A O   1 
ATOM   1107 C CB  . HIS   A 1 160 ? -7.205  -14.192 -10.207 1.00 29.11  ? 697  HIS   A CB  1 
ATOM   1108 C CG  . HIS   A 1 160 ? -5.869  -13.798 -10.768 1.00 33.01  ? 697  HIS   A CG  1 
ATOM   1109 N ND1 . HIS   A 1 160 ? -4.887  -14.719 -11.071 1.00 34.22  ? 697  HIS   A ND1 1 
ATOM   1110 C CD2 . HIS   A 1 160 ? -5.357  -12.585 -11.085 1.00 31.70  ? 697  HIS   A CD2 1 
ATOM   1111 C CE1 . HIS   A 1 160 ? -3.829  -14.089 -11.552 1.00 37.84  ? 697  HIS   A CE1 1 
ATOM   1112 N NE2 . HIS   A 1 160 ? -4.092  -12.793 -11.579 1.00 31.37  ? 697  HIS   A NE2 1 
ATOM   1113 N N   . TRP   A 1 161 ? -8.515  -11.839 -8.451  1.00 25.32  ? 698  TRP   A N   1 
ATOM   1114 C CA  . TRP   A 1 161 ? -8.601  -10.396 -8.224  1.00 25.54  ? 698  TRP   A CA  1 
ATOM   1115 C C   . TRP   A 1 161 ? -8.232  -10.040 -6.787  1.00 27.93  ? 698  TRP   A C   1 
ATOM   1116 O O   . TRP   A 1 161 ? -7.413  -9.146  -6.543  1.00 26.80  ? 698  TRP   A O   1 
ATOM   1117 C CB  . TRP   A 1 161 ? -10.018 -9.934  -8.567  1.00 24.44  ? 698  TRP   A CB  1 
ATOM   1118 C CG  . TRP   A 1 161 ? -10.260 -8.443  -8.655  1.00 24.48  ? 698  TRP   A CG  1 
ATOM   1119 C CD1 . TRP   A 1 161 ? -9.364  -7.431  -8.435  1.00 25.16  ? 698  TRP   A CD1 1 
ATOM   1120 C CD2 . TRP   A 1 161 ? -11.497 -7.825  -8.998  1.00 25.19  ? 698  TRP   A CD2 1 
ATOM   1121 N NE1 . TRP   A 1 161 ? -9.983  -6.209  -8.633  1.00 25.59  ? 698  TRP   A NE1 1 
ATOM   1122 C CE2 . TRP   A 1 161 ? -11.295 -6.430  -8.971  1.00 26.74  ? 698  TRP   A CE2 1 
ATOM   1123 C CE3 . TRP   A 1 161 ? -12.761 -8.324  -9.339  1.00 23.64  ? 698  TRP   A CE3 1 
ATOM   1124 C CZ2 . TRP   A 1 161 ? -12.316 -5.518  -9.265  1.00 26.29  ? 698  TRP   A CZ2 1 
ATOM   1125 C CZ3 . TRP   A 1 161 ? -13.779 -7.427  -9.615  1.00 23.81  ? 698  TRP   A CZ3 1 
ATOM   1126 C CH2 . TRP   A 1 161 ? -13.548 -6.026  -9.581  1.00 25.33  ? 698  TRP   A CH2 1 
ATOM   1127 N N   . VAL   A 1 162 ? -8.804  -10.750 -5.811  1.00 25.82  ? 699  VAL   A N   1 
ATOM   1128 C CA  . VAL   A 1 162 ? -8.491  -10.409 -4.429  1.00 29.23  ? 699  VAL   A CA  1 
ATOM   1129 C C   . VAL   A 1 162 ? -7.116  -10.895 -4.036  1.00 33.06  ? 699  VAL   A C   1 
ATOM   1130 O O   . VAL   A 1 162 ? -6.512  -10.326 -3.130  1.00 31.44  ? 699  VAL   A O   1 
ATOM   1131 C CB  . VAL   A 1 162 ? -9.532  -10.937 -3.422  1.00 31.47  ? 699  VAL   A CB  1 
ATOM   1132 C CG1 . VAL   A 1 162 ? -10.882 -10.255 -3.641  1.00 28.45  ? 699  VAL   A CG1 1 
ATOM   1133 C CG2 . VAL   A 1 162 ? -9.646  -12.468 -3.480  1.00 26.56  ? 699  VAL   A CG2 1 
ATOM   1134 N N   . GLU   A 1 163 ? -6.593  -11.925 -4.703  1.00 29.92  ? 700  GLU   A N   1 
ATOM   1135 C CA  . GLU   A 1 163 ? -5.280  -12.439 -4.338  1.00 28.71  ? 700  GLU   A CA  1 
ATOM   1136 C C   . GLU   A 1 163 ? -4.167  -11.505 -4.796  1.00 30.59  ? 700  GLU   A C   1 
ATOM   1137 O O   . GLU   A 1 163 ? -3.193  -11.273 -4.060  1.00 36.01  ? 700  GLU   A O   1 
ATOM   1138 C CB  . GLU   A 1 163 ? -5.072  -13.832 -4.943  1.00 30.91  ? 700  GLU   A CB  1 
ATOM   1139 C CG  . GLU   A 1 163 ? -3.706  -14.441 -4.594  1.00 43.53  ? 700  GLU   A CG  1 
ATOM   1140 C CD  . GLU   A 1 163 ? -3.567  -14.729 -3.111  1.00 62.89  ? 700  GLU   A CD  1 
ATOM   1141 O OE1 . GLU   A 1 163 ? -4.420  -15.463 -2.569  1.00 71.64  ? 700  GLU   A OE1 1 
ATOM   1142 O OE2 . GLU   A 1 163 ? -2.625  -14.205 -2.482  1.00 73.39  ? 700  GLU   A OE2 1 
ATOM   1143 N N   . HIS   A 1 164 ? -4.281  -10.971 -6.007  1.00 31.83  ? 701  HIS   A N   1 
ATOM   1144 C CA  . HIS   A 1 164 ? -3.175  -10.266 -6.640  1.00 34.27  ? 701  HIS   A CA  1 
ATOM   1145 C C   . HIS   A 1 164 ? -3.406  -8.769  -6.802  1.00 33.08  ? 701  HIS   A C   1 
ATOM   1146 O O   . HIS   A 1 164 ? -2.454  -8.040  -7.108  1.00 29.09  ? 701  HIS   A O   1 
ATOM   1147 C CB  . HIS   A 1 164 ? -2.889  -10.887 -8.012  1.00 30.93  ? 701  HIS   A CB  1 
ATOM   1148 C CG  . HIS   A 1 164 ? -2.482  -12.326 -7.941  1.00 31.77  ? 701  HIS   A CG  1 
ATOM   1149 N ND1 . HIS   A 1 164 ? -1.255  -12.726 -7.459  1.00 33.22  ? 701  HIS   A ND1 1 
ATOM   1150 C CD2 . HIS   A 1 164 ? -3.135  -13.460 -8.297  1.00 31.07  ? 701  HIS   A CD2 1 
ATOM   1151 C CE1 . HIS   A 1 164 ? -1.172  -14.044 -7.504  1.00 37.95  ? 701  HIS   A CE1 1 
ATOM   1152 N NE2 . HIS   A 1 164 ? -2.301  -14.514 -8.008  1.00 31.99  ? 701  HIS   A NE2 1 
ATOM   1153 N N   . HIS   A 1 165 ? -4.623  -8.284  -6.590  1.00 27.92  ? 702  HIS   A N   1 
ATOM   1154 C CA  . HIS   A 1 165 ? -4.911  -6.862  -6.763  1.00 25.63  ? 702  HIS   A CA  1 
ATOM   1155 C C   . HIS   A 1 165 ? -5.817  -6.373  -5.650  1.00 27.88  ? 702  HIS   A C   1 
ATOM   1156 O O   . HIS   A 1 165 ? -6.810  -5.674  -5.888  1.00 30.40  ? 702  HIS   A O   1 
ATOM   1157 C CB  . HIS   A 1 165 ? -5.515  -6.602  -8.140  1.00 24.67  ? 702  HIS   A CB  1 
ATOM   1158 C CG  . HIS   A 1 165 ? -4.698  -7.180  -9.256  1.00 27.72  ? 702  HIS   A CG  1 
ATOM   1159 N ND1 . HIS   A 1 165 ? -3.627  -6.516  -9.817  1.00 33.59  ? 702  HIS   A ND1 1 
ATOM   1160 C CD2 . HIS   A 1 165 ? -4.764  -8.382  -9.880  1.00 32.33  ? 702  HIS   A CD2 1 
ATOM   1161 C CE1 . HIS   A 1 165 ? -3.076  -7.280  -10.746 1.00 33.98  ? 702  HIS   A CE1 1 
ATOM   1162 N NE2 . HIS   A 1 165 ? -3.749  -8.416  -10.806 1.00 28.63  ? 702  HIS   A NE2 1 
ATOM   1163 N N   . PHE   A 1 166 ? -5.501  -6.761  -4.411  1.00 28.46  ? 703  PHE   A N   1 
ATOM   1164 C CA  . PHE   A 1 166 ? -6.392  -6.403  -3.319  1.00 34.53  ? 703  PHE   A CA  1 
ATOM   1165 C C   . PHE   A 1 166 ? -6.408  -4.901  -3.073  1.00 36.42  ? 703  PHE   A C   1 
ATOM   1166 O O   . PHE   A 1 166 ? -7.371  -4.399  -2.484  1.00 34.06  ? 703  PHE   A O   1 
ATOM   1167 C CB  . PHE   A 1 166 ? -6.018  -7.140  -2.030  1.00 37.99  ? 703  PHE   A CB  1 
ATOM   1168 C CG  . PHE   A 1 166 ? -7.079  -7.044  -0.961  1.00 41.38  ? 703  PHE   A CG  1 
ATOM   1169 C CD1 . PHE   A 1 166 ? -8.287  -7.730  -1.101  1.00 36.82  ? 703  PHE   A CD1 1 
ATOM   1170 C CD2 . PHE   A 1 166 ? -6.893  -6.242  0.155   1.00 40.75  ? 703  PHE   A CD2 1 
ATOM   1171 C CE1 . PHE   A 1 166 ? -9.285  -7.630  -0.130  1.00 37.28  ? 703  PHE   A CE1 1 
ATOM   1172 C CE2 . PHE   A 1 166 ? -7.882  -6.139  1.132   1.00 44.29  ? 703  PHE   A CE2 1 
ATOM   1173 C CZ  . PHE   A 1 166 ? -9.080  -6.835  0.987   1.00 41.92  ? 703  PHE   A CZ  1 
ATOM   1174 N N   . TYR   A 1 167 ? -5.384  -4.171  -3.534  1.00 29.10  ? 704  TYR   A N   1 
ATOM   1175 C CA  . TYR   A 1 167 ? -5.407  -2.718  -3.383  1.00 29.82  ? 704  TYR   A CA  1 
ATOM   1176 C C   . TYR   A 1 167 ? -6.639  -2.085  -4.036  1.00 30.86  ? 704  TYR   A C   1 
ATOM   1177 O O   . TYR   A 1 167 ? -7.045  -0.993  -3.624  1.00 33.80  ? 704  TYR   A O   1 
ATOM   1178 C CB  . TYR   A 1 167 ? -4.129  -2.107  -3.959  1.00 38.24  ? 704  TYR   A CB  1 
ATOM   1179 C CG  . TYR   A 1 167 ? -3.823  -2.584  -5.357  1.00 37.71  ? 704  TYR   A CG  1 
ATOM   1180 C CD1 . TYR   A 1 167 ? -4.486  -2.052  -6.460  1.00 33.42  ? 704  TYR   A CD1 1 
ATOM   1181 C CD2 . TYR   A 1 167 ? -2.875  -3.575  -5.573  1.00 31.49  ? 704  TYR   A CD2 1 
ATOM   1182 C CE1 . TYR   A 1 167 ? -4.202  -2.495  -7.742  1.00 33.14  ? 704  TYR   A CE1 1 
ATOM   1183 C CE2 . TYR   A 1 167 ? -2.590  -4.022  -6.841  1.00 35.04  ? 704  TYR   A CE2 1 
ATOM   1184 C CZ  . TYR   A 1 167 ? -3.245  -3.486  -7.918  1.00 29.82  ? 704  TYR   A CZ  1 
ATOM   1185 O OH  . TYR   A 1 167 ? -2.941  -3.952  -9.175  1.00 31.53  ? 704  TYR   A OH  1 
ATOM   1186 N N   . ASP   A 1 168 ? -7.245  -2.727  -5.051  1.00 29.48  ? 705  ASP   A N   1 
ATOM   1187 C CA  . ASP   A 1 168 ? -8.482  -2.170  -5.606  1.00 35.23  ? 705  ASP   A CA  1 
ATOM   1188 C C   . ASP   A 1 168 ? -9.532  -2.029  -4.513  1.00 36.98  ? 705  ASP   A C   1 
ATOM   1189 O O   . ASP   A 1 168 ? -10.298 -1.054  -4.490  1.00 30.84  ? 705  ASP   A O   1 
ATOM   1190 C CB  . ASP   A 1 168 ? -9.061  -3.044  -6.734  1.00 23.74  ? 705  ASP   A CB  1 
ATOM   1191 C CG  . ASP   A 1 168 ? -8.337  -2.887  -8.077  1.00 29.55  ? 705  ASP   A CG  1 
ATOM   1192 O OD1 . ASP   A 1 168 ? -7.628  -1.881  -8.309  1.00 26.71  ? 705  ASP   A OD1 1 
ATOM   1193 O OD2 . ASP   A 1 168 ? -8.494  -3.800  -8.919  1.00 26.67  ? 705  ASP   A OD2 1 
ATOM   1194 N N   . PHE   A 1 169 ? -9.571  -3.003  -3.598  1.00 31.61  ? 706  PHE   A N   1 
ATOM   1195 C CA  . PHE   A 1 169 ? -10.551 -3.097  -2.524  1.00 30.03  ? 706  PHE   A CA  1 
ATOM   1196 C C   . PHE   A 1 169 ? -10.159 -2.267  -1.309  1.00 37.89  ? 706  PHE   A C   1 
ATOM   1197 O O   . PHE   A 1 169 ? -11.039 -1.784  -0.582  1.00 39.21  ? 706  PHE   A O   1 
ATOM   1198 C CB  . PHE   A 1 169 ? -10.739 -4.578  -2.148  1.00 32.26  ? 706  PHE   A CB  1 
ATOM   1199 C CG  . PHE   A 1 169 ? -11.195 -5.433  -3.305  1.00 30.76  ? 706  PHE   A CG  1 
ATOM   1200 C CD1 . PHE   A 1 169 ? -12.533 -5.479  -3.658  1.00 33.53  ? 706  PHE   A CD1 1 
ATOM   1201 C CD2 . PHE   A 1 169 ? -10.282 -6.147  -4.066  1.00 30.95  ? 706  PHE   A CD2 1 
ATOM   1202 C CE1 . PHE   A 1 169 ? -12.962 -6.236  -4.747  1.00 31.59  ? 706  PHE   A CE1 1 
ATOM   1203 C CE2 . PHE   A 1 169 ? -10.693 -6.906  -5.159  1.00 28.51  ? 706  PHE   A CE2 1 
ATOM   1204 C CZ  . PHE   A 1 169 ? -12.042 -6.958  -5.497  1.00 32.33  ? 706  PHE   A CZ  1 
ATOM   1205 N N   . GLU   A 1 170 ? -8.854  -2.068  -1.087  1.00 35.10  ? 707  GLU   A N   1 
ATOM   1206 C CA  . GLU   A 1 170 ? -8.411  -1.098  -0.090  1.00 34.78  ? 707  GLU   A CA  1 
ATOM   1207 C C   . GLU   A 1 170 ? -8.715  0.324   -0.530  1.00 36.87  ? 707  GLU   A C   1 
ATOM   1208 O O   . GLU   A 1 170 ? -8.957  1.199   0.310   1.00 38.30  ? 707  GLU   A O   1 
ATOM   1209 C CB  . GLU   A 1 170 ? -6.906  -1.238  0.160   1.00 38.01  ? 707  GLU   A CB  1 
ATOM   1210 C CG  . GLU   A 1 170 ? -6.472  -2.659  0.512   1.00 39.91  ? 707  GLU   A CG  1 
ATOM   1211 C CD  . GLU   A 1 170 ? -4.961  -2.825  0.552   1.00 48.29  ? 707  GLU   A CD  1 
ATOM   1212 O OE1 . GLU   A 1 170 ? -4.257  -2.129  -0.214  1.00 46.90  ? 707  GLU   A OE1 1 
ATOM   1213 O OE2 . GLU   A 1 170 ? -4.484  -3.653  1.356   1.00 51.20  ? 707  GLU   A OE2 1 
ATOM   1214 N N   . ARG   A 1 171 ? -8.672  0.581   -1.833  1.00 31.79  ? 708  ARG   A N   1 
ATOM   1215 C CA  . ARG   A 1 171 ? -8.856  1.934   -2.324  1.00 34.74  ? 708  ARG   A CA  1 
ATOM   1216 C C   . ARG   A 1 171 ? -10.326 2.307   -2.419  1.00 37.20  ? 708  ARG   A C   1 
ATOM   1217 O O   . ARG   A 1 171 ? -10.648 3.500   -2.465  1.00 41.63  ? 708  ARG   A O   1 
ATOM   1218 C CB  . ARG   A 1 171 ? -8.189  2.088   -3.694  1.00 34.20  ? 708  ARG   A CB  1 
ATOM   1219 C CG  . ARG   A 1 171 ? -6.660  2.117   -3.640  1.00 34.96  ? 708  ARG   A CG  1 
ATOM   1220 C CD  . ARG   A 1 171 ? -6.047  1.941   -5.036  1.00 37.59  ? 708  ARG   A CD  1 
ATOM   1221 N NE  . ARG   A 1 171 ? -4.606  1.693   -4.962  1.00 40.29  ? 708  ARG   A NE  1 
ATOM   1222 C CZ  . ARG   A 1 171 ? -3.837  1.424   -6.012  1.00 39.72  ? 708  ARG   A CZ  1 
ATOM   1223 N NH1 . ARG   A 1 171 ? -4.361  1.374   -7.231  1.00 35.91  ? 708  ARG   A NH1 1 
ATOM   1224 N NH2 . ARG   A 1 171 ? -2.542  1.210   -5.841  1.00 46.21  ? 708  ARG   A NH2 1 
ATOM   1225 N N   . ASP   A 1 172 ? -11.218 1.314   -2.437  1.00 31.11  ? 709  ASP   A N   1 
ATOM   1226 C CA  . ASP   A 1 172 ? -12.652 1.532   -2.628  1.00 36.04  ? 709  ASP   A CA  1 
ATOM   1227 C C   . ASP   A 1 172 ? -13.392 0.547   -1.723  1.00 36.42  ? 709  ASP   A C   1 
ATOM   1228 O O   . ASP   A 1 172 ? -13.674 -0.579  -2.129  1.00 34.45  ? 709  ASP   A O   1 
ATOM   1229 C CB  . ASP   A 1 172 ? -13.021 1.358   -4.093  1.00 28.96  ? 709  ASP   A CB  1 
ATOM   1230 C CG  . ASP   A 1 172 ? -14.485 1.667   -4.371  1.00 37.93  ? 709  ASP   A CG  1 
ATOM   1231 O OD1 . ASP   A 1 172 ? -15.229 2.012   -3.425  1.00 41.36  ? 709  ASP   A OD1 1 
ATOM   1232 O OD2 . ASP   A 1 172 ? -14.879 1.572   -5.553  1.00 37.06  ? 709  ASP   A OD2 1 
ATOM   1233 N N   . LEU   A 1 173 ? -13.708 0.982   -0.498  1.00 36.57  ? 710  LEU   A N   1 
ATOM   1234 C CA  . LEU   A 1 173 ? -14.378 0.088   0.444   1.00 36.45  ? 710  LEU   A CA  1 
ATOM   1235 C C   . LEU   A 1 173 ? -15.719 -0.400  -0.089  1.00 38.08  ? 710  LEU   A C   1 
ATOM   1236 O O   . LEU   A 1 173 ? -16.120 -1.534  0.196   1.00 38.40  ? 710  LEU   A O   1 
ATOM   1237 C CB  . LEU   A 1 173 ? -14.578 0.776   1.789   1.00 39.31  ? 710  LEU   A CB  1 
ATOM   1238 C CG  . LEU   A 1 173 ? -13.328 1.236   2.547   1.00 50.72  ? 710  LEU   A CG  1 
ATOM   1239 C CD1 . LEU   A 1 173 ? -13.700 1.668   3.963   1.00 53.85  ? 710  LEU   A CD1 1 
ATOM   1240 C CD2 . LEU   A 1 173 ? -12.261 0.149   2.570   1.00 58.45  ? 710  LEU   A CD2 1 
ATOM   1241 N N   . GLU   A 1 174 ? -16.423 0.436   -0.858  1.00 37.79  ? 711  GLU   A N   1 
ATOM   1242 C CA  . GLU   A 1 174 ? -17.697 0.006   -1.435  1.00 42.90  ? 711  GLU   A CA  1 
ATOM   1243 C C   . GLU   A 1 174 ? -17.511 -1.165  -2.393  1.00 33.59  ? 711  GLU   A C   1 
ATOM   1244 O O   . GLU   A 1 174 ? -18.384 -2.040  -2.484  1.00 34.84  ? 711  GLU   A O   1 
ATOM   1245 C CB  . GLU   A 1 174 ? -18.388 1.172   -2.150  1.00 46.23  ? 711  GLU   A CB  1 
ATOM   1246 C CG  . GLU   A 1 174 ? -19.838 0.873   -2.534  1.00 59.10  ? 711  GLU   A CG  1 
ATOM   1247 C CD  . GLU   A 1 174 ? -20.410 1.852   -3.549  1.00 69.15  ? 711  GLU   A CD  1 
ATOM   1248 O OE1 . GLU   A 1 174 ? -19.784 2.905   -3.788  1.00 76.85  ? 711  GLU   A OE1 1 
ATOM   1249 O OE2 . GLU   A 1 174 ? -21.486 1.561   -4.116  1.00 69.28  ? 711  GLU   A OE2 1 
ATOM   1250 N N   . LEU   A 1 175 ? -16.385 -1.206  -3.112  1.00 29.83  ? 712  LEU   A N   1 
ATOM   1251 C CA  . LEU   A 1 175 ? -16.127 -2.314  -4.016  1.00 27.55  ? 712  LEU   A CA  1 
ATOM   1252 C C   . LEU   A 1 175 ? -16.065 -3.634  -3.258  1.00 34.30  ? 712  LEU   A C   1 
ATOM   1253 O O   . LEU   A 1 175 ? -16.626 -4.647  -3.700  1.00 31.36  ? 712  LEU   A O   1 
ATOM   1254 C CB  . LEU   A 1 175 ? -14.823 -2.073  -4.775  1.00 25.18  ? 712  LEU   A CB  1 
ATOM   1255 C CG  . LEU   A 1 175 ? -14.518 -3.029  -5.907  1.00 26.56  ? 712  LEU   A CG  1 
ATOM   1256 C CD1 . LEU   A 1 175 ? -15.472 -2.758  -7.070  1.00 31.47  ? 712  LEU   A CD1 1 
ATOM   1257 C CD2 . LEU   A 1 175 ? -13.044 -2.876  -6.349  1.00 28.20  ? 712  LEU   A CD2 1 
ATOM   1258 N N   . LEU   A 1 176 ? -15.380 -3.639  -2.110  1.00 34.26  ? 713  LEU   A N   1 
ATOM   1259 C CA  . LEU   A 1 176 ? -15.309 -4.845  -1.290  1.00 35.50  ? 713  LEU   A CA  1 
ATOM   1260 C C   . LEU   A 1 176 ? -16.674 -5.201  -0.715  1.00 32.91  ? 713  LEU   A C   1 
ATOM   1261 O O   . LEU   A 1 176 ? -17.057 -6.372  -0.700  1.00 34.81  ? 713  LEU   A O   1 
ATOM   1262 C CB  . LEU   A 1 176 ? -14.301 -4.659  -0.159  1.00 30.03  ? 713  LEU   A CB  1 
ATOM   1263 C CG  . LEU   A 1 176 ? -14.049 -5.881  0.726   1.00 37.57  ? 713  LEU   A CG  1 
ATOM   1264 C CD1 . LEU   A 1 176 ? -13.623 -7.077  -0.122  1.00 38.89  ? 713  LEU   A CD1 1 
ATOM   1265 C CD2 . LEU   A 1 176 ? -12.986 -5.546  1.768   1.00 43.68  ? 713  LEU   A CD2 1 
ATOM   1266 N N   . GLU   A 1 177 ? -17.412 -4.210  -0.213  1.00 37.90  ? 714  GLU   A N   1 
ATOM   1267 C CA  . GLU   A 1 177 ? -18.746 -4.501  0.310   1.00 37.29  ? 714  GLU   A CA  1 
ATOM   1268 C C   . GLU   A 1 177 ? -19.617 -5.144  -0.759  1.00 36.61  ? 714  GLU   A C   1 
ATOM   1269 O O   . GLU   A 1 177 ? -20.313 -6.130  -0.494  1.00 60.51  ? 714  GLU   A O   1 
ATOM   1270 C CB  . GLU   A 1 177 ? -19.405 -3.234  0.857   1.00 39.85  ? 714  GLU   A CB  1 
ATOM   1271 C CG  . GLU   A 1 177 ? -18.906 -2.835  2.233   1.00 57.25  ? 714  GLU   A CG  1 
ATOM   1272 C CD  . GLU   A 1 177 ? -19.352 -1.449  2.629   1.00 70.67  ? 714  GLU   A CD  1 
ATOM   1273 O OE1 . GLU   A 1 177 ? -19.118 -1.063  3.792   1.00 76.25  ? 714  GLU   A OE1 1 
ATOM   1274 O OE2 . GLU   A 1 177 ? -19.932 -0.748  1.770   1.00 78.17  ? 714  GLU   A OE2 1 
ATOM   1275 N N   . ARG   A 1 178 ? -19.580 -4.609  -1.984  1.00 34.60  ? 715  ARG   A N   1 
ATOM   1276 C CA  . ARG   A 1 178 ? -20.348 -5.223  -3.064  1.00 31.49  ? 715  ARG   A CA  1 
ATOM   1277 C C   . ARG   A 1 178 ? -19.905 -6.666  -3.304  1.00 30.71  ? 715  ARG   A C   1 
ATOM   1278 O O   . ARG   A 1 178 ? -20.739 -7.563  -3.475  1.00 31.40  ? 715  ARG   A O   1 
ATOM   1279 C CB  . ARG   A 1 178 ? -20.206 -4.414  -4.352  1.00 26.22  ? 715  ARG   A CB  1 
ATOM   1280 C CG  . ARG   A 1 178 ? -20.891 -3.049  -4.352  1.00 31.97  ? 715  ARG   A CG  1 
ATOM   1281 C CD  . ARG   A 1 178 ? -20.744 -2.413  -5.722  1.00 32.80  ? 715  ARG   A CD  1 
ATOM   1282 N NE  . ARG   A 1 178 ? -21.453 -3.188  -6.729  1.00 32.66  ? 715  ARG   A NE  1 
ATOM   1283 C CZ  . ARG   A 1 178 ? -21.131 -3.233  -8.020  1.00 37.47  ? 715  ARG   A CZ  1 
ATOM   1284 N NH1 . ARG   A 1 178 ? -20.092 -2.541  -8.496  1.00 34.07  ? 715  ARG   A NH1 1 
ATOM   1285 N NH2 . ARG   A 1 178 ? -21.851 -3.978  -8.842  1.00 29.45  ? 715  ARG   A NH2 1 
ATOM   1286 N N   . LEU   A 1 179 ? -18.596 -6.906  -3.320  1.00 29.87  ? 716  LEU   A N   1 
ATOM   1287 C CA  . LEU   A 1 179 ? -18.102 -8.241  -3.645  1.00 29.77  ? 716  LEU   A CA  1 
ATOM   1288 C C   . LEU   A 1 179 ? -18.469 -9.227  -2.550  1.00 27.65  ? 716  LEU   A C   1 
ATOM   1289 O O   . LEU   A 1 179 ? -18.927 -10.339 -2.830  1.00 34.79  ? 716  LEU   A O   1 
ATOM   1290 C CB  . LEU   A 1 179 ? -16.584 -8.219  -3.856  1.00 26.86  ? 716  LEU   A CB  1 
ATOM   1291 C CG  . LEU   A 1 179 ? -15.962 -9.617  -4.014  1.00 34.61  ? 716  LEU   A CG  1 
ATOM   1292 C CD1 . LEU   A 1 179 ? -16.514 -10.323 -5.235  1.00 30.89  ? 716  LEU   A CD1 1 
ATOM   1293 C CD2 . LEU   A 1 179 ? -14.442 -9.538  -4.071  1.00 34.41  ? 716  LEU   A CD2 1 
ATOM   1294 N N   . GLU   A 1 180 ? -18.280 -8.832  -1.291  1.00 29.92  ? 717  GLU   A N   1 
ATOM   1295 C CA  . GLU   A 1 180 ? -18.618 -9.733  -0.199  1.00 36.48  ? 717  GLU   A CA  1 
ATOM   1296 C C   . GLU   A 1 180 ? -20.111 -10.004 -0.157  1.00 43.50  ? 717  GLU   A C   1 
ATOM   1297 O O   . GLU   A 1 180 ? -20.534 -11.143 0.064   1.00 40.43  ? 717  GLU   A O   1 
ATOM   1298 C CB  . GLU   A 1 180 ? -18.138 -9.155  1.127   1.00 37.72  ? 717  GLU   A CB  1 
ATOM   1299 C CG  . GLU   A 1 180 ? -16.627 -9.010  1.172   1.00 37.56  ? 717  GLU   A CG  1 
ATOM   1300 C CD  . GLU   A 1 180 ? -16.129 -8.568  2.525   1.00 48.50  ? 717  GLU   A CD  1 
ATOM   1301 O OE1 . GLU   A 1 180 ? -16.739 -7.657  3.127   1.00 57.61  ? 717  GLU   A OE1 1 
ATOM   1302 O OE2 . GLU   A 1 180 ? -15.125 -9.136  2.992   1.00 58.01  ? 717  GLU   A OE2 1 
ATOM   1303 N N   . SER   A 1 181 ? -20.925 -8.971  -0.374  1.00 39.65  ? 718  SER   A N   1 
ATOM   1304 C CA  . SER   A 1 181 ? -22.366 -9.175  -0.442  1.00 41.65  ? 718  SER   A CA  1 
ATOM   1305 C C   . SER   A 1 181 ? -22.728 -10.125 -1.579  1.00 36.17  ? 718  SER   A C   1 
ATOM   1306 O O   . SER   A 1 181 ? -23.569 -11.017 -1.409  1.00 37.72  ? 718  SER   A O   1 
ATOM   1307 C CB  . SER   A 1 181 ? -23.074 -7.824  -0.601  1.00 43.94  ? 718  SER   A CB  1 
ATOM   1308 O OG  . SER   A 1 181 ? -24.466 -7.993  -0.809  1.00 47.98  ? 718  SER   A OG  1 
ATOM   1309 N N   . PHE   A 1 182 ? -22.080 -9.981  -2.736  1.00 35.97  ? 719  PHE   A N   1 
ATOM   1310 C CA  . PHE   A 1 182 ? -22.453 -10.843 -3.850  1.00 36.27  ? 719  PHE   A CA  1 
ATOM   1311 C C   . PHE   A 1 182 ? -22.098 -12.297 -3.564  1.00 39.07  ? 719  PHE   A C   1 
ATOM   1312 O O   . PHE   A 1 182 ? -22.923 -13.198 -3.776  1.00 36.36  ? 719  PHE   A O   1 
ATOM   1313 C CB  . PHE   A 1 182 ? -21.802 -10.408 -5.158  1.00 32.37  ? 719  PHE   A CB  1 
ATOM   1314 C CG  . PHE   A 1 182 ? -22.134 -11.339 -6.289  1.00 37.73  ? 719  PHE   A CG  1 
ATOM   1315 C CD1 . PHE   A 1 182 ? -23.403 -11.327 -6.856  1.00 36.84  ? 719  PHE   A CD1 1 
ATOM   1316 C CD2 . PHE   A 1 182 ? -21.218 -12.280 -6.726  1.00 37.03  ? 719  PHE   A CD2 1 
ATOM   1317 C CE1 . PHE   A 1 182 ? -23.731 -12.204 -7.873  1.00 33.87  ? 719  PHE   A CE1 1 
ATOM   1318 C CE2 . PHE   A 1 182 ? -21.543 -13.161 -7.739  1.00 34.89  ? 719  PHE   A CE2 1 
ATOM   1319 C CZ  . PHE   A 1 182 ? -22.794 -13.122 -8.312  1.00 36.95  ? 719  PHE   A CZ  1 
ATOM   1320 N N   . ILE   A 1 183 ? -20.873 -12.553 -3.089  1.00 35.92  ? 720  ILE   A N   1 
ATOM   1321 C CA  . ILE   A 1 183 ? -20.482 -13.944 -2.874  1.00 42.08  ? 720  ILE   A CA  1 
ATOM   1322 C C   . ILE   A 1 183 ? -21.290 -14.577 -1.747  1.00 39.50  ? 720  ILE   A C   1 
ATOM   1323 O O   . ILE   A 1 183 ? -21.476 -15.801 -1.739  1.00 40.13  ? 720  ILE   A O   1 
ATOM   1324 C CB  . ILE   A 1 183 ? -18.961 -14.081 -2.633  1.00 36.62  ? 720  ILE   A CB  1 
ATOM   1325 C CG1 . ILE   A 1 183 ? -18.533 -13.383 -1.346  1.00 44.99  ? 720  ILE   A CG1 1 
ATOM   1326 C CG2 . ILE   A 1 183 ? -18.163 -13.539 -3.842  1.00 34.85  ? 720  ILE   A CG2 1 
ATOM   1327 C CD1 . ILE   A 1 183 ? -17.029 -13.408 -1.120  1.00 46.69  ? 720  ILE   A CD1 1 
ATOM   1328 N N   A SER   A 1 184 ? -21.786 -13.775 -0.797  0.47 37.71  ? 721  SER   A N   1 
ATOM   1329 N N   B SER   A 1 184 ? -21.791 -13.782 -0.798  0.53 37.80  ? 721  SER   A N   1 
ATOM   1330 C CA  A SER   A 1 184 ? -22.691 -14.298 0.219   0.47 38.69  ? 721  SER   A CA  1 
ATOM   1331 C CA  B SER   A 1 184 ? -22.680 -14.332 0.216   0.53 38.64  ? 721  SER   A CA  1 
ATOM   1332 C C   A SER   A 1 184 ? -24.002 -14.787 -0.380  0.47 40.59  ? 721  SER   A C   1 
ATOM   1333 C C   B SER   A 1 184 ? -24.034 -14.737 -0.350  0.53 40.57  ? 721  SER   A C   1 
ATOM   1334 O O   A SER   A 1 184 ? -24.678 -15.621 0.234   0.47 43.74  ? 721  SER   A O   1 
ATOM   1335 O O   B SER   A 1 184 ? -24.772 -15.469 0.320   0.53 44.60  ? 721  SER   A O   1 
ATOM   1336 C CB  A SER   A 1 184 ? -22.988 -13.236 1.278   0.47 43.65  ? 721  SER   A CB  1 
ATOM   1337 C CB  B SER   A 1 184 ? -22.873 -13.329 1.354   0.53 43.35  ? 721  SER   A CB  1 
ATOM   1338 O OG  A SER   A 1 184 ? -24.106 -12.442 0.906   0.47 47.57  ? 721  SER   A OG  1 
ATOM   1339 O OG  B SER   A 1 184 ? -21.650 -13.090 2.030   0.53 48.50  ? 721  SER   A OG  1 
ATOM   1340 N N   . SER   A 1 185 ? -24.373 -14.286 -1.556  1.00 44.54  ? 722  SER   A N   1 
ATOM   1341 C CA  . SER   A 1 185 ? -25.611 -14.674 -2.217  1.00 49.70  ? 722  SER   A CA  1 
ATOM   1342 C C   . SER   A 1 185 ? -25.461 -15.922 -3.077  1.00 46.69  ? 722  SER   A C   1 
ATOM   1343 O O   . SER   A 1 185 ? -26.472 -16.471 -3.524  1.00 44.22  ? 722  SER   A O   1 
ATOM   1344 C CB  . SER   A 1 185 ? -26.112 -13.530 -3.106  1.00 45.50  ? 722  SER   A CB  1 
ATOM   1345 O OG  . SER   A 1 185 ? -25.402 -13.529 -4.335  1.00 45.05  ? 722  SER   A OG  1 
ATOM   1346 N N   . VAL   A 1 186 ? -24.235 -16.367 -3.341  1.00 36.22  ? 723  VAL   A N   1 
ATOM   1347 C CA  . VAL   A 1 186 ? -24.026 -17.504 -4.231  1.00 37.89  ? 723  VAL   A CA  1 
ATOM   1348 C C   . VAL   A 1 186 ? -24.511 -18.768 -3.529  1.00 51.20  ? 723  VAL   A C   1 
ATOM   1349 O O   . VAL   A 1 186 ? -24.058 -19.101 -2.427  1.00 49.01  ? 723  VAL   A O   1 
ATOM   1350 C CB  . VAL   A 1 186 ? -22.551 -17.610 -4.646  1.00 37.56  ? 723  VAL   A CB  1 
ATOM   1351 C CG1 . VAL   A 1 186 ? -22.264 -18.934 -5.347  1.00 41.76  ? 723  VAL   A CG1 1 
ATOM   1352 C CG2 . VAL   A 1 186 ? -22.169 -16.432 -5.553  1.00 35.49  ? 723  VAL   A CG2 1 
ATOM   1353 N N   . ARG   A 1 187 ? -25.455 -19.463 -4.153  1.00 48.86  ? 724  ARG   A N   1 
ATOM   1354 C CA  . ARG   A 1 187 ? -26.005 -20.692 -3.601  1.00 55.16  ? 724  ARG   A CA  1 
ATOM   1355 C C   . ARG   A 1 187 ? -25.401 -21.910 -4.283  1.00 55.34  ? 724  ARG   A C   1 
ATOM   1356 O O   . ARG   A 1 187 ? -24.914 -21.834 -5.414  1.00 57.25  ? 724  ARG   A O   1 
ATOM   1357 C CB  . ARG   A 1 187 ? -27.532 -20.723 -3.746  1.00 60.28  ? 724  ARG   A CB  1 
ATOM   1358 C CG  . ARG   A 1 187 ? -28.274 -19.688 -2.913  1.00 70.12  ? 724  ARG   A CG  1 
ATOM   1359 C CD  . ARG   A 1 187 ? -28.210 -20.005 -1.419  1.00 84.14  ? 724  ARG   A CD  1 
ATOM   1360 N NE  . ARG   A 1 187 ? -26.949 -19.585 -0.812  1.00 92.12  ? 724  ARG   A NE  1 
ATOM   1361 C CZ  . ARG   A 1 187 ? -26.784 -18.458 -0.127  1.00 88.49  ? 724  ARG   A CZ  1 
ATOM   1362 N NH1 . ARG   A 1 187 ? -27.807 -17.631 0.055   1.00 83.90  ? 724  ARG   A NH1 1 
ATOM   1363 N NH2 . ARG   A 1 187 ? -25.597 -18.163 0.383   1.00 86.17  ? 724  ARG   A NH2 1 
ATOM   1364 N N   . GLY   A 1 188 ? -25.439 -23.037 -3.579  1.00 63.81  ? 725  GLY   A N   1 
ATOM   1365 C CA  . GLY   A 1 188 ? -25.013 -24.292 -4.165  1.00 66.07  ? 725  GLY   A CA  1 
ATOM   1366 C C   . GLY   A 1 188 ? -23.774 -24.872 -3.521  1.00 63.89  ? 725  GLY   A C   1 
ATOM   1367 O O   . GLY   A 1 188 ? -22.750 -24.190 -3.412  1.00 51.32  ? 725  GLY   A O   1 
ATOM   1368 N N   . LYS   A 1 189 ? -23.863 -26.138 -3.093  1.00 62.94  ? 726  LYS   A N   1 
ATOM   1369 C CA  . LYS   A 1 189 ? -22.712 -26.831 -2.522  1.00 74.53  ? 726  LYS   A CA  1 
ATOM   1370 C C   . LYS   A 1 189 ? -21.520 -26.820 -3.466  1.00 62.23  ? 726  LYS   A C   1 
ATOM   1371 O O   . LYS   A 1 189 ? -20.373 -26.788 -3.012  1.00 71.76  ? 726  LYS   A O   1 
ATOM   1372 C CB  . LYS   A 1 189 ? -23.081 -28.276 -2.187  1.00 83.78  ? 726  LYS   A CB  1 
ATOM   1373 C CG  . LYS   A 1 189 ? -23.679 -28.502 -0.813  1.00 89.53  ? 726  LYS   A CG  1 
ATOM   1374 C CD  . LYS   A 1 189 ? -24.010 -29.984 -0.634  1.00 96.04  ? 726  LYS   A CD  1 
ATOM   1375 C CE  . LYS   A 1 189 ? -24.089 -30.381 0.831   1.00 101.77 ? 726  LYS   A CE  1 
ATOM   1376 N NZ  . LYS   A 1 189 ? -25.327 -29.890 1.493   1.00 104.04 ? 726  LYS   A NZ  1 
ATOM   1377 N N   . ALA   A 1 190 ? -21.769 -26.875 -4.778  1.00 51.29  ? 727  ALA   A N   1 
ATOM   1378 C CA  . ALA   A 1 190 ? -20.677 -26.931 -5.743  1.00 57.58  ? 727  ALA   A CA  1 
ATOM   1379 C C   . ALA   A 1 190 ? -19.812 -25.682 -5.705  1.00 59.22  ? 727  ALA   A C   1 
ATOM   1380 O O   . ALA   A 1 190 ? -18.636 -25.738 -6.083  1.00 63.86  ? 727  ALA   A O   1 
ATOM   1381 C CB  . ALA   A 1 190 ? -21.226 -27.124 -7.157  1.00 61.69  ? 727  ALA   A CB  1 
ATOM   1382 N N   . MET   A 1 191 ? -20.360 -24.560 -5.259  1.00 48.04  ? 728  MET   A N   1 
ATOM   1383 C CA  . MET   A 1 191 ? -19.638 -23.305 -5.288  1.00 50.27  ? 728  MET   A CA  1 
ATOM   1384 C C   . MET   A 1 191 ? -19.232 -22.822 -3.911  1.00 53.64  ? 728  MET   A C   1 
ATOM   1385 O O   . MET   A 1 191 ? -18.544 -21.802 -3.810  1.00 41.95  ? 728  MET   A O   1 
ATOM   1386 C CB  . MET   A 1 191 ? -20.482 -22.252 -6.003  1.00 37.68  ? 728  MET   A CB  1 
ATOM   1387 C CG  . MET   A 1 191 ? -20.898 -22.760 -7.358  1.00 53.88  ? 728  MET   A CG  1 
ATOM   1388 S SD  . MET   A 1 191 ? -21.026 -21.459 -8.558  1.00 56.85  ? 728  MET   A SD  1 
ATOM   1389 C CE  . MET   A 1 191 ? -22.745 -20.998 -8.352  1.00 64.41  ? 728  MET   A CE  1 
ATOM   1390 N N   . LYS   A 1 192 ? -19.600 -23.545 -2.852  1.00 54.36  ? 729  LYS   A N   1 
ATOM   1391 C CA  . LYS   A 1 192 ? -19.271 -23.090 -1.507  1.00 58.02  ? 729  LYS   A CA  1 
ATOM   1392 C C   . LYS   A 1 192 ? -17.768 -23.077 -1.269  1.00 52.52  ? 729  LYS   A C   1 
ATOM   1393 O O   . LYS   A 1 192 ? -17.254 -22.182 -0.591  1.00 52.31  ? 729  LYS   A O   1 
ATOM   1394 C CB  . LYS   A 1 192 ? -19.981 -23.958 -0.472  1.00 61.91  ? 729  LYS   A CB  1 
ATOM   1395 C CG  . LYS   A 1 192 ? -21.458 -23.643 -0.412  1.00 81.28  ? 729  LYS   A CG  1 
ATOM   1396 C CD  . LYS   A 1 192 ? -22.208 -24.565 0.520   1.00 96.17  ? 729  LYS   A CD  1 
ATOM   1397 C CE  . LYS   A 1 192 ? -23.698 -24.266 0.459   1.00 97.34  ? 729  LYS   A CE  1 
ATOM   1398 N NZ  . LYS   A 1 192 ? -24.477 -25.142 1.373   1.00 101.21 ? 729  LYS   A NZ  1 
ATOM   1399 N N   . LYS   A 1 193 ? -17.042 -24.051 -1.825  1.00 48.67  ? 730  LYS   A N   1 
ATOM   1400 C CA  . LYS   A 1 193 ? -15.599 -24.085 -1.609  1.00 46.85  ? 730  LYS   A CA  1 
ATOM   1401 C C   . LYS   A 1 193 ? -14.911 -22.912 -2.286  1.00 45.05  ? 730  LYS   A C   1 
ATOM   1402 O O   . LYS   A 1 193 ? -13.930 -22.382 -1.755  1.00 39.48  ? 730  LYS   A O   1 
ATOM   1403 C CB  . LYS   A 1 193 ? -15.010 -25.408 -2.094  1.00 53.56  ? 730  LYS   A CB  1 
ATOM   1404 C CG  . LYS   A 1 193 ? -15.365 -25.792 -3.525  1.00 63.74  ? 730  LYS   A CG  1 
ATOM   1405 C CD  . LYS   A 1 193 ? -14.868 -27.213 -3.842  1.00 68.83  ? 730  LYS   A CD  1 
ATOM   1406 C CE  . LYS   A 1 193 ? -16.030 -28.175 -4.061  1.00 74.04  ? 730  LYS   A CE  1 
ATOM   1407 N NZ  . LYS   A 1 193 ? -16.822 -27.828 -5.275  1.00 83.26  ? 730  LYS   A NZ  1 
ATOM   1408 N N   . TRP   A 1 194 ? -15.426 -22.470 -3.433  1.00 38.19  ? 731  TRP   A N   1 
ATOM   1409 C CA  . TRP   A 1 194 ? -14.878 -21.277 -4.067  1.00 37.73  ? 731  TRP   A CA  1 
ATOM   1410 C C   . TRP   A 1 194 ? -15.170 -20.036 -3.229  1.00 46.34  ? 731  TRP   A C   1 
ATOM   1411 O O   . TRP   A 1 194 ? -14.294 -19.186 -3.016  1.00 35.55  ? 731  TRP   A O   1 
ATOM   1412 C CB  . TRP   A 1 194 ? -15.461 -21.114 -5.468  1.00 41.78  ? 731  TRP   A CB  1 
ATOM   1413 C CG  . TRP   A 1 194 ? -14.849 -21.980 -6.532  1.00 46.65  ? 731  TRP   A CG  1 
ATOM   1414 C CD1 . TRP   A 1 194 ? -15.342 -23.156 -7.014  1.00 43.55  ? 731  TRP   A CD1 1 
ATOM   1415 C CD2 . TRP   A 1 194 ? -13.655 -21.706 -7.283  1.00 43.28  ? 731  TRP   A CD2 1 
ATOM   1416 N NE1 . TRP   A 1 194 ? -14.524 -23.638 -8.008  1.00 50.21  ? 731  TRP   A NE1 1 
ATOM   1417 C CE2 . TRP   A 1 194 ? -13.486 -22.762 -8.195  1.00 44.33  ? 731  TRP   A CE2 1 
ATOM   1418 C CE3 . TRP   A 1 194 ? -12.715 -20.669 -7.268  1.00 51.29  ? 731  TRP   A CE3 1 
ATOM   1419 C CZ2 . TRP   A 1 194 ? -12.406 -22.826 -9.077  1.00 55.47  ? 731  TRP   A CZ2 1 
ATOM   1420 C CZ3 . TRP   A 1 194 ? -11.644 -20.729 -8.149  1.00 57.53  ? 731  TRP   A CZ3 1 
ATOM   1421 C CH2 . TRP   A 1 194 ? -11.501 -21.802 -9.042  1.00 55.17  ? 731  TRP   A CH2 1 
ATOM   1422 N N   . VAL   A 1 195 ? -16.414 -19.904 -2.770  1.00 34.94  ? 732  VAL   A N   1 
ATOM   1423 C CA  . VAL   A 1 195 ? -16.787 -18.760 -1.949  1.00 40.15  ? 732  VAL   A CA  1 
ATOM   1424 C C   . VAL   A 1 195 ? -15.923 -18.700 -0.702  1.00 43.12  ? 732  VAL   A C   1 
ATOM   1425 O O   . VAL   A 1 195 ? -15.425 -17.632 -0.321  1.00 42.31  ? 732  VAL   A O   1 
ATOM   1426 C CB  . VAL   A 1 195 ? -18.283 -18.828 -1.596  1.00 38.03  ? 732  VAL   A CB  1 
ATOM   1427 C CG1 . VAL   A 1 195 ? -18.614 -17.798 -0.523  1.00 37.56  ? 732  VAL   A CG1 1 
ATOM   1428 C CG2 . VAL   A 1 195 ? -19.117 -18.589 -2.847  1.00 35.59  ? 732  VAL   A CG2 1 
ATOM   1429 N N   . GLU   A 1 196 ? -15.715 -19.849 -0.055  1.00 37.40  ? 733  GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 196 ? -14.932 -19.864 1.170   1.00 40.30  ? 733  GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 196 ? -13.456 -19.631 0.887   1.00 39.99  ? 733  GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 196 ? -12.751 -19.080 1.735   1.00 44.53  ? 733  GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 196 ? -15.178 -21.172 1.929   1.00 50.17  ? 733  GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 196 ? -16.591 -21.202 2.528   1.00 64.72  ? 733  GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 196 ? -16.950 -22.505 3.231   1.00 83.93  ? 733  GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 196 ? -16.361 -23.556 2.898   1.00 87.43  ? 733  GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 196 ? -17.835 -22.473 4.117   1.00 86.63  ? 733  GLU   A OE2 1 
ATOM   1438 N N   . SER   A 1 197 ? -12.983 -19.998 -0.306  1.00 40.28  ? 734  SER   A N   1 
ATOM   1439 C CA  . SER   A 1 197 ? -11.609 -19.681 -0.681  1.00 41.62  ? 734  SER   A CA  1 
ATOM   1440 C C   . SER   A 1 197 ? -11.427 -18.180 -0.901  1.00 37.89  ? 734  SER   A C   1 
ATOM   1441 O O   . SER   A 1 197 ? -10.409 -17.607 -0.497  1.00 39.12  ? 734  SER   A O   1 
ATOM   1442 C CB  . SER   A 1 197 ? -11.220 -20.468 -1.932  1.00 44.40  ? 734  SER   A CB  1 
ATOM   1443 O OG  . SER   A 1 197 ? -9.949  -20.072 -2.408  1.00 57.50  ? 734  SER   A OG  1 
ATOM   1444 N N   . ILE   A 1 198 ? -12.405 -17.527 -1.535  1.00 38.01  ? 735  ILE   A N   1 
ATOM   1445 C CA  . ILE   A 1 198 ? -12.337 -16.078 -1.720  1.00 33.39  ? 735  ILE   A CA  1 
ATOM   1446 C C   . ILE   A 1 198 ? -12.392 -15.369 -0.373  1.00 34.81  ? 735  ILE   A C   1 
ATOM   1447 O O   . ILE   A 1 198 ? -11.609 -14.448 -0.106  1.00 36.80  ? 735  ILE   A O   1 
ATOM   1448 C CB  . ILE   A 1 198 ? -13.463 -15.597 -2.654  1.00 30.96  ? 735  ILE   A CB  1 
ATOM   1449 C CG1 . ILE   A 1 198 ? -13.270 -16.166 -4.063  1.00 30.87  ? 735  ILE   A CG1 1 
ATOM   1450 C CG2 . ILE   A 1 198 ? -13.487 -14.076 -2.706  1.00 30.78  ? 735  ILE   A CG2 1 
ATOM   1451 C CD1 . ILE   A 1 198 ? -14.472 -16.019 -4.949  1.00 38.60  ? 735  ILE   A CD1 1 
ATOM   1452 N N   . ALA   A 1 199 ? -13.318 -15.789 0.497   1.00 33.65  ? 736  ALA   A N   1 
ATOM   1453 C CA  . ALA   A 1 199 ? -13.451 -15.155 1.808   1.00 41.94  ? 736  ALA   A CA  1 
ATOM   1454 C C   . ALA   A 1 199 ? -12.181 -15.330 2.630   1.00 42.80  ? 736  ALA   A C   1 
ATOM   1455 O O   . ALA   A 1 199 ? -11.752 -14.407 3.338   1.00 42.14  ? 736  ALA   A O   1 
ATOM   1456 C CB  . ALA   A 1 199 ? -14.660 -15.732 2.553   1.00 38.74  ? 736  ALA   A CB  1 
ATOM   1457 N N   . LYS   A 1 200 ? -11.555 -16.504 2.532   1.00 37.72  ? 737  LYS   A N   1 
ATOM   1458 C CA  . LYS   A 1 200 ? -10.312 -16.743 3.257   1.00 46.49  ? 737  LYS   A CA  1 
ATOM   1459 C C   . LYS   A 1 200 ? -9.213  -15.779 2.820   1.00 47.86  ? 737  LYS   A C   1 
ATOM   1460 O O   . LYS   A 1 200 ? -8.473  -15.248 3.658   1.00 48.79  ? 737  LYS   A O   1 
ATOM   1461 C CB  . LYS   A 1 200 ? -9.867  -18.188 3.054   1.00 44.35  ? 737  LYS   A CB  1 
ATOM   1462 C CG  . LYS   A 1 200 ? -8.578  -18.533 3.760   1.00 47.85  ? 737  LYS   A CG  1 
ATOM   1463 C CD  . LYS   A 1 200 ? -8.308  -20.030 3.679   1.00 54.62  ? 737  LYS   A CD  1 
ATOM   1464 C CE  . LYS   A 1 200 ? -7.083  -20.415 4.507   1.00 65.32  ? 737  LYS   A CE  1 
ATOM   1465 N NZ  . LYS   A 1 200 ? -7.163  -21.820 5.004   1.00 69.27  ? 737  LYS   A NZ  1 
ATOM   1466 N N   . ILE   A 1 201 ? -9.081  -15.547 1.511   1.00 37.05  ? 738  ILE   A N   1 
ATOM   1467 C CA  . ILE   A 1 201 ? -8.080  -14.601 1.025   1.00 33.18  ? 738  ILE   A CA  1 
ATOM   1468 C C   . ILE   A 1 201 ? -8.368  -13.202 1.550   1.00 43.18  ? 738  ILE   A C   1 
ATOM   1469 O O   . ILE   A 1 201 ? -7.465  -12.504 2.026   1.00 40.58  ? 738  ILE   A O   1 
ATOM   1470 C CB  . ILE   A 1 201 ? -8.031  -14.627 -0.511  1.00 33.10  ? 738  ILE   A CB  1 
ATOM   1471 C CG1 . ILE   A 1 201 ? -7.482  -15.971 -0.985  1.00 45.41  ? 738  ILE   A CG1 1 
ATOM   1472 C CG2 . ILE   A 1 201 ? -7.238  -13.442 -1.046  1.00 33.07  ? 738  ILE   A CG2 1 
ATOM   1473 C CD1 . ILE   A 1 201 ? -7.654  -16.217 -2.453  1.00 45.72  ? 738  ILE   A CD1 1 
ATOM   1474 N N   . ILE   A 1 202 ? -9.630  -12.772 1.476   1.00 44.06  ? 739  ILE   A N   1 
ATOM   1475 C CA  . ILE   A 1 202 ? -10.001 -11.455 1.988   1.00 36.06  ? 739  ILE   A CA  1 
ATOM   1476 C C   . ILE   A 1 202 ? -9.657  -11.348 3.469   1.00 41.01  ? 739  ILE   A C   1 
ATOM   1477 O O   . ILE   A 1 202 ? -9.063  -10.360 3.915   1.00 41.21  ? 739  ILE   A O   1 
ATOM   1478 C CB  . ILE   A 1 202 ? -11.494 -11.184 1.733   1.00 37.72  ? 739  ILE   A CB  1 
ATOM   1479 C CG1 . ILE   A 1 202 ? -11.771 -11.079 0.229   1.00 35.65  ? 739  ILE   A CG1 1 
ATOM   1480 C CG2 . ILE   A 1 202 ? -11.943 -9.930  2.487   1.00 42.70  ? 739  ILE   A CG2 1 
ATOM   1481 C CD1 . ILE   A 1 202 ? -13.260 -11.025 -0.113  1.00 33.61  ? 739  ILE   A CD1 1 
ATOM   1482 N N   . ARG   A 1 203 ? -10.013 -12.377 4.246   1.00 42.51  ? 740  ARG   A N   1 
ATOM   1483 C CA  . ARG   A 1 203 ? -9.660  -12.429 5.665   1.00 54.07  ? 740  ARG   A CA  1 
ATOM   1484 C C   . ARG   A 1 203 ? -8.173  -12.179 5.882   1.00 55.66  ? 740  ARG   A C   1 
ATOM   1485 O O   . ARG   A 1 203 ? -7.783  -11.338 6.701   1.00 57.19  ? 740  ARG   A O   1 
ATOM   1486 C CB  . ARG   A 1 203 ? -10.048 -13.786 6.251   1.00 58.27  ? 740  ARG   A CB  1 
ATOM   1487 C CG  . ARG   A 1 203 ? -11.119 -13.731 7.320   1.00 70.31  ? 740  ARG   A CG  1 
ATOM   1488 C CD  . ARG   A 1 203 ? -11.129 -15.004 8.167   1.00 76.94  ? 740  ARG   A CD  1 
ATOM   1489 N NE  . ARG   A 1 203 ? -11.008 -16.228 7.374   1.00 77.32  ? 740  ARG   A NE  1 
ATOM   1490 C CZ  . ARG   A 1 203 ? -11.994 -16.767 6.662   1.00 76.81  ? 740  ARG   A CZ  1 
ATOM   1491 N NH1 . ARG   A 1 203 ? -13.187 -16.188 6.620   1.00 77.23  ? 740  ARG   A NH1 1 
ATOM   1492 N NH2 . ARG   A 1 203 ? -11.787 -17.887 5.983   1.00 72.04  ? 740  ARG   A NH2 1 
ATOM   1493 N N   . ARG   A 1 204 ? -7.327  -12.909 5.153   1.00 47.55  ? 741  ARG   A N   1 
ATOM   1494 C CA  . ARG   A 1 204 ? -5.888  -12.760 5.320   1.00 47.38  ? 741  ARG   A CA  1 
ATOM   1495 C C   . ARG   A 1 204 ? -5.420  -11.371 4.904   1.00 55.83  ? 741  ARG   A C   1 
ATOM   1496 O O   . ARG   A 1 204 ? -4.573  -10.769 5.575   1.00 63.85  ? 741  ARG   A O   1 
ATOM   1497 C CB  . ARG   A 1 204 ? -5.156  -13.839 4.523   1.00 50.17  ? 741  ARG   A CB  1 
ATOM   1498 C CG  . ARG   A 1 204 ? -3.736  -13.465 4.128   1.00 57.44  ? 741  ARG   A CG  1 
ATOM   1499 C CD  . ARG   A 1 204 ? -2.945  -14.665 3.630   1.00 66.25  ? 741  ARG   A CD  1 
ATOM   1500 N NE  . ARG   A 1 204 ? -3.705  -15.503 2.702   1.00 73.81  ? 741  ARG   A NE  1 
ATOM   1501 C CZ  . ARG   A 1 204 ? -3.773  -15.304 1.389   1.00 66.30  ? 741  ARG   A CZ  1 
ATOM   1502 N NH1 . ARG   A 1 204 ? -3.136  -14.282 0.836   1.00 60.26  ? 741  ARG   A NH1 1 
ATOM   1503 N NH2 . ARG   A 1 204 ? -4.483  -16.129 0.631   1.00 67.42  ? 741  ARG   A NH2 1 
ATOM   1504 N N   . LYS   A 1 205 ? -5.958  -10.844 3.800   1.00 48.29  ? 742  LYS   A N   1 
ATOM   1505 C CA  . LYS   A 1 205 ? -5.519  -9.535  3.322   1.00 43.85  ? 742  LYS   A CA  1 
ATOM   1506 C C   . LYS   A 1 205 ? -5.897  -8.426  4.299   1.00 50.40  ? 742  LYS   A C   1 
ATOM   1507 O O   . LYS   A 1 205 ? -5.120  -7.486  4.502   1.00 53.75  ? 742  LYS   A O   1 
ATOM   1508 C CB  . LYS   A 1 205 ? -6.103  -9.254  1.935   1.00 42.73  ? 742  LYS   A CB  1 
ATOM   1509 C CG  . LYS   A 1 205 ? -5.649  -10.206 0.840   1.00 41.33  ? 742  LYS   A CG  1 
ATOM   1510 C CD  . LYS   A 1 205 ? -4.304  -9.820  0.255   1.00 47.86  ? 742  LYS   A CD  1 
ATOM   1511 C CE  . LYS   A 1 205 ? -3.951  -10.730 -0.907  1.00 44.31  ? 742  LYS   A CE  1 
ATOM   1512 N NZ  . LYS   A 1 205 ? -2.524  -10.653 -1.314  1.00 53.76  ? 742  LYS   A NZ  1 
ATOM   1513 N N   A LYS   A 1 206 ? -7.082  -8.518  4.911   0.52 51.07  ? 743  LYS   A N   1 
ATOM   1514 N N   B LYS   A 1 206 ? -7.081  -8.520  4.914   0.48 51.13  ? 743  LYS   A N   1 
ATOM   1515 C CA  A LYS   A 1 206 ? -7.490  -7.525  5.902   0.52 56.49  ? 743  LYS   A CA  1 
ATOM   1516 C CA  B LYS   A 1 206 ? -7.487  -7.523  5.902   0.48 56.51  ? 743  LYS   A CA  1 
ATOM   1517 C C   A LYS   A 1 206 ? -6.582  -7.551  7.127   0.52 64.87  ? 743  LYS   A C   1 
ATOM   1518 C C   B LYS   A 1 206 ? -6.584  -7.551  7.130   0.48 64.85  ? 743  LYS   A C   1 
ATOM   1519 O O   A LYS   A 1 206 ? -6.307  -6.504  7.726   0.52 68.12  ? 743  LYS   A O   1 
ATOM   1520 O O   B LYS   A 1 206 ? -6.317  -6.506  7.736   0.48 68.09  ? 743  LYS   A O   1 
ATOM   1521 C CB  A LYS   A 1 206 ? -8.941  -7.762  6.321   0.52 55.68  ? 743  LYS   A CB  1 
ATOM   1522 C CB  B LYS   A 1 206 ? -8.940  -7.752  6.322   0.48 55.68  ? 743  LYS   A CB  1 
ATOM   1523 C CG  A LYS   A 1 206 ? -9.981  -6.996  5.523   0.52 55.64  ? 743  LYS   A CG  1 
ATOM   1524 C CG  B LYS   A 1 206 ? -9.982  -7.129  5.413   0.48 55.61  ? 743  LYS   A CG  1 
ATOM   1525 C CD  A LYS   A 1 206 ? -11.379 -7.323  6.034   0.52 58.16  ? 743  LYS   A CD  1 
ATOM   1526 C CD  B LYS   A 1 206 ? -11.363 -7.238  6.047   0.48 58.18  ? 743  LYS   A CD  1 
ATOM   1527 C CE  A LYS   A 1 206 ? -12.465 -6.705  5.172   0.52 56.86  ? 743  LYS   A CE  1 
ATOM   1528 C CE  B LYS   A 1 206 ? -12.470 -7.078  5.021   0.48 56.66  ? 743  LYS   A CE  1 
ATOM   1529 N NZ  A LYS   A 1 206 ? -13.676 -7.578  5.129   0.52 52.80  ? 743  LYS   A NZ  1 
ATOM   1530 N NZ  B LYS   A 1 206 ? -13.406 -5.983  5.389   0.48 53.75  ? 743  LYS   A NZ  1 
ATOM   1531 N N   . GLN   A 1 207 ? -6.117  -8.739  7.521   1.00 70.70  ? 744  GLN   A N   1 
ATOM   1532 C CA  . GLN   A 1 207 ? -5.273  -8.853  8.708   1.00 74.16  ? 744  GLN   A CA  1 
ATOM   1533 C C   . GLN   A 1 207 ? -3.955  -8.111  8.527   1.00 73.00  ? 744  GLN   A C   1 
ATOM   1534 O O   . GLN   A 1 207 ? -3.517  -7.375  9.419   1.00 78.73  ? 744  GLN   A O   1 
ATOM   1535 C CB  . GLN   A 1 207 ? -5.014  -10.326 9.025   1.00 76.52  ? 744  GLN   A CB  1 
ATOM   1536 C CG  . GLN   A 1 207 ? -6.009  -10.935 9.987   1.00 91.31  ? 744  GLN   A CG  1 
ATOM   1537 C CD  . GLN   A 1 207 ? -5.334  -11.545 11.202  1.00 107.46 ? 744  GLN   A CD  1 
ATOM   1538 O OE1 . GLN   A 1 207 ? -4.795  -12.651 11.139  1.00 117.50 ? 744  GLN   A OE1 1 
ATOM   1539 N NE2 . GLN   A 1 207 ? -5.357  -10.822 12.318  1.00 107.91 ? 744  GLN   A NE2 1 
ATOM   1540 N N   . ALA   A 1 208 ? -3.313  -8.290  7.378   1.00 67.07  ? 745  ALA   A N   1 
ATOM   1541 C CA  . ALA   A 1 208 ? -2.000  -7.703  7.122   1.00 67.80  ? 745  ALA   A CA  1 
ATOM   1542 C C   . ALA   A 1 208 ? -2.005  -6.176  7.240   1.00 74.01  ? 745  ALA   A C   1 
ATOM   1543 O O   . ALA   A 1 208 ? -3.022  -5.517  7.008   1.00 79.87  ? 745  ALA   A O   1 
ATOM   1544 C CB  . ALA   A 1 208 ? -1.499  -8.125  5.743   1.00 53.98  ? 745  ALA   A CB  1 
ATOM   1545 N N   . ILE   A 1 217 ? 12.756  -9.722  9.979   1.00 73.72  ? 754  ILE   A N   1 
ATOM   1546 C CA  . ILE   A 1 217 ? 13.668  -10.143 8.918   1.00 64.04  ? 754  ILE   A CA  1 
ATOM   1547 C C   . ILE   A 1 217 ? 14.636  -11.216 9.424   1.00 63.55  ? 754  ILE   A C   1 
ATOM   1548 O O   . ILE   A 1 217 ? 15.259  -11.073 10.484  1.00 60.75  ? 754  ILE   A O   1 
ATOM   1549 C CB  . ILE   A 1 217 ? 14.428  -8.931  8.336   1.00 59.96  ? 754  ILE   A CB  1 
ATOM   1550 C CG1 . ILE   A 1 217 ? 13.464  -8.044  7.546   1.00 53.41  ? 754  ILE   A CG1 1 
ATOM   1551 C CG2 . ILE   A 1 217 ? 15.600  -9.386  7.463   1.00 50.58  ? 754  ILE   A CG2 1 
ATOM   1552 C CD1 . ILE   A 1 217 ? 13.959  -6.631  7.332   1.00 54.92  ? 754  ILE   A CD1 1 
ATOM   1553 N N   . THR   A 1 218 ? 14.753  -12.295 8.655   1.00 68.29  ? 755  THR   A N   1 
ATOM   1554 C CA  . THR   A 1 218 ? 15.580  -13.437 9.009   1.00 67.81  ? 755  THR   A CA  1 
ATOM   1555 C C   . THR   A 1 218 ? 16.716  -13.595 8.006   1.00 52.82  ? 755  THR   A C   1 
ATOM   1556 O O   . THR   A 1 218 ? 16.583  -13.243 6.829   1.00 49.19  ? 755  THR   A O   1 
ATOM   1557 C CB  . THR   A 1 218 ? 14.749  -14.725 9.055   1.00 72.08  ? 755  THR   A CB  1 
ATOM   1558 O OG1 . THR   A 1 218 ? 14.451  -15.158 7.720   1.00 77.79  ? 755  THR   A OG1 1 
ATOM   1559 C CG2 . THR   A 1 218 ? 13.445  -14.487 9.794   1.00 72.58  ? 755  THR   A CG2 1 
ATOM   1560 N N   . PHE   A 1 219 ? 17.829  -14.149 8.479   1.00 50.47  ? 756  PHE   A N   1 
ATOM   1561 C CA  . PHE   A 1 219 ? 19.019  -14.355 7.665   1.00 45.59  ? 756  PHE   A CA  1 
ATOM   1562 C C   . PHE   A 1 219 ? 19.427  -15.821 7.708   1.00 43.11  ? 756  PHE   A C   1 
ATOM   1563 O O   . PHE   A 1 219 ? 19.551  -16.404 8.792   1.00 48.28  ? 756  PHE   A O   1 
ATOM   1564 C CB  . PHE   A 1 219 ? 20.158  -13.460 8.152   1.00 42.19  ? 756  PHE   A CB  1 
ATOM   1565 C CG  . PHE   A 1 219 ? 19.849  -11.991 8.047   1.00 41.44  ? 756  PHE   A CG  1 
ATOM   1566 C CD1 . PHE   A 1 219 ? 19.942  -11.339 6.826   1.00 42.08  ? 756  PHE   A CD1 1 
ATOM   1567 C CD2 . PHE   A 1 219 ? 19.446  -11.268 9.159   1.00 46.42  ? 756  PHE   A CD2 1 
ATOM   1568 C CE1 . PHE   A 1 219 ? 19.642  -9.982  6.718   1.00 49.12  ? 756  PHE   A CE1 1 
ATOM   1569 C CE2 . PHE   A 1 219 ? 19.149  -9.906  9.060   1.00 42.51  ? 756  PHE   A CE2 1 
ATOM   1570 C CZ  . PHE   A 1 219 ? 19.248  -9.269  7.837   1.00 43.52  ? 756  PHE   A CZ  1 
ATOM   1571 N N   . GLU   A 1 220 ? 19.615  -16.418 6.522   1.00 44.18  ? 757  GLU   A N   1 
ATOM   1572 C CA  . GLU   A 1 220 ? 20.091  -17.801 6.439   1.00 47.82  ? 757  GLU   A CA  1 
ATOM   1573 C C   . GLU   A 1 220 ? 21.582  -17.894 6.736   1.00 53.60  ? 757  GLU   A C   1 
ATOM   1574 O O   . GLU   A 1 220 ? 22.075  -18.957 7.143   1.00 56.47  ? 757  GLU   A O   1 
ATOM   1575 C CB  . GLU   A 1 220 ? 19.782  -18.370 5.049   1.00 52.62  ? 757  GLU   A CB  1 
ATOM   1576 C CG  . GLU   A 1 220 ? 20.161  -19.833 4.831   1.00 61.49  ? 757  GLU   A CG  1 
ATOM   1577 C CD  . GLU   A 1 220 ? 21.528  -20.009 4.179   1.00 72.99  ? 757  GLU   A CD  1 
ATOM   1578 O OE1 . GLU   A 1 220 ? 22.128  -21.098 4.342   1.00 73.30  ? 757  GLU   A OE1 1 
ATOM   1579 O OE2 . GLU   A 1 220 ? 21.995  -19.064 3.503   1.00 74.30  ? 757  GLU   A OE2 1 
ATOM   1580 N N   . SER   A 1 221 ? 22.312  -16.803 6.526   1.00 55.76  ? 758  SER   A N   1 
ATOM   1581 C CA  . SER   A 1 221 ? 23.719  -16.669 6.866   1.00 62.48  ? 758  SER   A CA  1 
ATOM   1582 C C   . SER   A 1 221 ? 23.932  -15.268 7.421   1.00 53.83  ? 758  SER   A C   1 
ATOM   1583 O O   . SER   A 1 221 ? 23.211  -14.336 7.047   1.00 49.94  ? 758  SER   A O   1 
ATOM   1584 C CB  . SER   A 1 221 ? 24.626  -16.911 5.647   1.00 67.40  ? 758  SER   A CB  1 
ATOM   1585 O OG  . SER   A 1 221 ? 24.199  -16.150 4.533   1.00 74.98  ? 758  SER   A OG  1 
ATOM   1586 N N   . PRO   A 1 222 ? 24.887  -15.094 8.327   1.00 50.69  ? 759  PRO   A N   1 
ATOM   1587 C CA  . PRO   A 1 222 ? 24.978  -13.837 9.083   1.00 44.87  ? 759  PRO   A CA  1 
ATOM   1588 C C   . PRO   A 1 222 ? 25.373  -12.674 8.190   1.00 45.93  ? 759  PRO   A C   1 
ATOM   1589 O O   . PRO   A 1 222 ? 26.381  -12.745 7.468   1.00 48.24  ? 759  PRO   A O   1 
ATOM   1590 C CB  . PRO   A 1 222 ? 26.063  -14.128 10.130  1.00 46.11  ? 759  PRO   A CB  1 
ATOM   1591 C CG  . PRO   A 1 222 ? 26.179  -15.627 10.181  1.00 57.78  ? 759  PRO   A CG  1 
ATOM   1592 C CD  . PRO   A 1 222 ? 25.852  -16.104 8.800   1.00 54.34  ? 759  PRO   A CD  1 
ATOM   1593 N N   . PRO   A 1 223 ? 24.610  -11.575 8.218   1.00 43.80  ? 760  PRO   A N   1 
ATOM   1594 C CA  . PRO   A 1 223 ? 24.994  -10.404 7.436   1.00 39.05  ? 760  PRO   A CA  1 
ATOM   1595 C C   . PRO   A 1 223 ? 26.248  -9.771  8.009   1.00 41.03  ? 760  PRO   A C   1 
ATOM   1596 O O   . PRO   A 1 223 ? 26.516  -9.881  9.218   1.00 40.05  ? 760  PRO   A O   1 
ATOM   1597 C CB  . PRO   A 1 223 ? 23.777  -9.470  7.578   1.00 36.19  ? 760  PRO   A CB  1 
ATOM   1598 C CG  . PRO   A 1 223 ? 23.207  -9.827  8.896   1.00 46.72  ? 760  PRO   A CG  1 
ATOM   1599 C CD  . PRO   A 1 223 ? 23.432  -11.312 9.063   1.00 44.78  ? 760  PRO   A CD  1 
ATOM   1600 N N   . PRO   A 1 224 ? 27.045  -9.096  7.184   1.00 38.20  ? 761  PRO   A N   1 
ATOM   1601 C CA  . PRO   A 1 224 ? 28.302  -8.496  7.671   1.00 36.93  ? 761  PRO   A CA  1 
ATOM   1602 C C   . PRO   A 1 224 ? 28.042  -7.390  8.680   1.00 39.37  ? 761  PRO   A C   1 
ATOM   1603 O O   . PRO   A 1 224 ? 26.964  -6.774  8.688   1.00 38.26  ? 761  PRO   A O   1 
ATOM   1604 C CB  . PRO   A 1 224 ? 28.940  -7.933  6.391   1.00 36.66  ? 761  PRO   A CB  1 
ATOM   1605 C CG  . PRO   A 1 224 ? 27.775  -7.661  5.492   1.00 36.02  ? 761  PRO   A CG  1 
ATOM   1606 C CD  . PRO   A 1 224 ? 26.810  -8.797  5.760   1.00 36.45  ? 761  PRO   A CD  1 
ATOM   1607 N N   . PRO   A 1 225 ? 29.021  -7.090  9.533   1.00 40.34  ? 762  PRO   A N   1 
ATOM   1608 C CA  . PRO   A 1 225 ? 28.854  -5.987  10.487  1.00 37.26  ? 762  PRO   A CA  1 
ATOM   1609 C C   . PRO   A 1 225 ? 28.664  -4.658  9.772   1.00 35.30  ? 762  PRO   A C   1 
ATOM   1610 O O   . PRO   A 1 225 ? 29.277  -4.405  8.733   1.00 35.67  ? 762  PRO   A O   1 
ATOM   1611 C CB  . PRO   A 1 225 ? 30.164  -6.001  11.284  1.00 43.00  ? 762  PRO   A CB  1 
ATOM   1612 C CG  . PRO   A 1 225 ? 31.153  -6.689  10.379  1.00 45.78  ? 762  PRO   A CG  1 
ATOM   1613 C CD  . PRO   A 1 225 ? 30.352  -7.718  9.631   1.00 38.72  ? 762  PRO   A CD  1 
ATOM   1614 N N   . ILE   A 1 226 ? 27.806  -3.808  10.351  1.00 38.87  ? 763  ILE   A N   1 
ATOM   1615 C CA  . ILE   A 1 226 ? 27.636  -2.441  9.863   1.00 36.00  ? 763  ILE   A CA  1 
ATOM   1616 C C   . ILE   A 1 226 ? 28.970  -1.717  9.912   1.00 33.95  ? 763  ILE   A C   1 
ATOM   1617 O O   . ILE   A 1 226 ? 29.716  -1.834  10.891  1.00 37.47  ? 763  ILE   A O   1 
ATOM   1618 C CB  . ILE   A 1 226 ? 26.589  -1.690  10.707  1.00 41.02  ? 763  ILE   A CB  1 
ATOM   1619 C CG1 . ILE   A 1 226 ? 25.279  -2.478  10.785  1.00 47.86  ? 763  ILE   A CG1 1 
ATOM   1620 C CG2 . ILE   A 1 226 ? 26.346  -0.292  10.156  1.00 34.94  ? 763  ILE   A CG2 1 
ATOM   1621 C CD1 . ILE   A 1 226 ? 24.741  -2.846  9.452   1.00 48.84  ? 763  ILE   A CD1 1 
ATOM   1622 N N   . GLU   A 1 227 ? 29.272  -0.943  8.864   1.00 29.62  ? 764  GLU   A N   1 
ATOM   1623 C CA  . GLU   A 1 227 ? 30.541  -0.225  8.772   1.00 35.90  ? 764  GLU   A CA  1 
ATOM   1624 C C   . GLU   A 1 227 ? 30.344  1.237   9.151   1.00 35.55  ? 764  GLU   A C   1 
ATOM   1625 O O   . GLU   A 1 227 ? 29.379  1.873   8.715   1.00 35.44  ? 764  GLU   A O   1 
ATOM   1626 C CB  . GLU   A 1 227 ? 31.126  -0.312  7.360   1.00 30.25  ? 764  GLU   A CB  1 
ATOM   1627 C CG  . GLU   A 1 227 ? 31.471  -1.730  6.901   1.00 34.46  ? 764  GLU   A CG  1 
ATOM   1628 C CD  . GLU   A 1 227 ? 32.839  -2.188  7.365   1.00 41.82  ? 764  GLU   A CD  1 
ATOM   1629 O OE1 . GLU   A 1 227 ? 33.630  -1.335  7.811   1.00 39.64  ? 764  GLU   A OE1 1 
ATOM   1630 O OE2 . GLU   A 1 227 ? 33.119  -3.403  7.279   1.00 38.14  ? 764  GLU   A OE2 1 
ATOM   1631 N N   . TRP   A 1 228 ? 31.274  1.768   9.950   1.00 32.46  ? 765  TRP   A N   1 
ATOM   1632 C CA  . TRP   A 1 228 ? 31.221  3.138   10.444  1.00 32.71  ? 765  TRP   A CA  1 
ATOM   1633 C C   . TRP   A 1 228 ? 32.544  3.834   10.175  1.00 37.12  ? 765  TRP   A C   1 
ATOM   1634 O O   . TRP   A 1 228 ? 33.608  3.217   10.256  1.00 37.05  ? 765  TRP   A O   1 
ATOM   1635 C CB  . TRP   A 1 228 ? 30.901  3.178   11.948  1.00 37.57  ? 765  TRP   A CB  1 
ATOM   1636 C CG  . TRP   A 1 228 ? 29.516  2.640   12.274  1.00 37.30  ? 765  TRP   A CG  1 
ATOM   1637 C CD1 . TRP   A 1 228 ? 29.204  1.390   12.730  1.00 43.18  ? 765  TRP   A CD1 1 
ATOM   1638 C CD2 . TRP   A 1 228 ? 28.274  3.345   12.157  1.00 36.49  ? 765  TRP   A CD2 1 
ATOM   1639 N NE1 . TRP   A 1 228 ? 27.843  1.274   12.907  1.00 39.47  ? 765  TRP   A NE1 1 
ATOM   1640 C CE2 . TRP   A 1 228 ? 27.250  2.459   12.556  1.00 37.93  ? 765  TRP   A CE2 1 
ATOM   1641 C CE3 . TRP   A 1 228 ? 27.927  4.638   11.745  1.00 39.35  ? 765  TRP   A CE3 1 
ATOM   1642 C CZ2 . TRP   A 1 228 ? 25.899  2.827   12.563  1.00 39.30  ? 765  TRP   A CZ2 1 
ATOM   1643 C CZ3 . TRP   A 1 228 ? 26.582  5.003   11.754  1.00 38.37  ? 765  TRP   A CZ3 1 
ATOM   1644 C CH2 . TRP   A 1 228 ? 25.586  4.099   12.161  1.00 36.83  ? 765  TRP   A CH2 1 
ATOM   1645 N N   . HIS   A 1 229 ? 32.465  5.124   9.855   1.00 33.84  ? 766  HIS   A N   1 
ATOM   1646 C CA  . HIS   A 1 229 ? 33.634  5.904   9.470   1.00 33.15  ? 766  HIS   A CA  1 
ATOM   1647 C C   . HIS   A 1 229 ? 33.868  6.972   10.528  1.00 35.24  ? 766  HIS   A C   1 
ATOM   1648 O O   . HIS   A 1 229 ? 34.302  6.656   11.642  1.00 39.49  ? 766  HIS   A O   1 
ATOM   1649 C CB  . HIS   A 1 229 ? 33.444  6.511   8.077   1.00 28.08  ? 766  HIS   A CB  1 
ATOM   1650 C CG  . HIS   A 1 229 ? 34.601  7.341   7.615   1.00 33.77  ? 766  HIS   A CG  1 
ATOM   1651 N ND1 . HIS   A 1 229 ? 35.910  7.047   7.944   1.00 29.97  ? 766  HIS   A ND1 1 
ATOM   1652 C CD2 . HIS   A 1 229 ? 34.643  8.469   6.868   1.00 33.40  ? 766  HIS   A CD2 1 
ATOM   1653 C CE1 . HIS   A 1 229 ? 36.709  7.961   7.420   1.00 35.63  ? 766  HIS   A CE1 1 
ATOM   1654 N NE2 . HIS   A 1 229 ? 35.966  8.836   6.762   1.00 34.72  ? 766  HIS   A NE2 1 
ATOM   1655 N N   . ILE   A 1 230 ? 33.546  8.224   10.209  1.00 36.98  ? 767  ILE   A N   1 
ATOM   1656 C CA  . ILE   A 1 230 ? 33.658  9.324   11.168  1.00 31.71  ? 767  ILE   A CA  1 
ATOM   1657 C C   . ILE   A 1 230 ? 32.398  9.451   12.014  1.00 45.04  ? 767  ILE   A C   1 
ATOM   1658 O O   . ILE   A 1 230 ? 32.471  9.494   13.245  1.00 44.01  ? 767  ILE   A O   1 
ATOM   1659 C CB  . ILE   A 1 230 ? 33.977  10.638  10.427  1.00 31.85  ? 767  ILE   A CB  1 
ATOM   1660 C CG1 . ILE   A 1 230 ? 35.375  10.581  9.805   1.00 41.18  ? 767  ILE   A CG1 1 
ATOM   1661 C CG2 . ILE   A 1 230 ? 33.882  11.813  11.393  1.00 38.95  ? 767  ILE   A CG2 1 
ATOM   1662 C CD1 . ILE   A 1 230 ? 35.678  11.767  8.902   1.00 37.52  ? 767  ILE   A CD1 1 
ATOM   1663 N N   . SER   A 1 231 ? 31.224  9.494   11.383  1.00 34.83  ? 768  SER   A N   1 
ATOM   1664 C CA  . SER   A 1 231 ? 29.984  9.453   12.143  1.00 46.61  ? 768  SER   A CA  1 
ATOM   1665 C C   . SER   A 1 231 ? 29.846  8.094   12.823  1.00 49.22  ? 768  SER   A C   1 
ATOM   1666 O O   . SER   A 1 231 ? 30.098  7.048   12.214  1.00 48.03  ? 768  SER   A O   1 
ATOM   1667 C CB  . SER   A 1 231 ? 28.782  9.724   11.232  1.00 51.92  ? 768  SER   A CB  1 
ATOM   1668 O OG  . SER   A 1 231 ? 28.753  11.073  10.782  1.00 40.36  ? 768  SER   A OG  1 
ATOM   1669 N N   . LYS   A 1 232 ? 29.459  8.109   14.084  1.00 48.55  ? 769  LYS   A N   1 
ATOM   1670 C CA  . LYS   A 1 232 ? 29.362  6.895   14.874  1.00 53.91  ? 769  LYS   A CA  1 
ATOM   1671 C C   . LYS   A 1 232 ? 27.905  6.576   15.178  1.00 53.81  ? 769  LYS   A C   1 
ATOM   1672 O O   . LYS   A 1 232 ? 27.031  7.438   15.025  1.00 49.03  ? 769  LYS   A O   1 
ATOM   1673 C CB  . LYS   A 1 232 ? 30.167  7.046   16.171  1.00 54.96  ? 769  LYS   A CB  1 
ATOM   1674 C CG  . LYS   A 1 232 ? 31.671  7.136   15.928  1.00 58.96  ? 769  LYS   A CG  1 
ATOM   1675 C CD  . LYS   A 1 232 ? 32.148  6.037   14.984  1.00 63.14  ? 769  LYS   A CD  1 
ATOM   1676 C CE  . LYS   A 1 232 ? 33.659  6.079   14.796  1.00 71.35  ? 769  LYS   A CE  1 
ATOM   1677 N NZ  . LYS   A 1 232 ? 34.141  5.020   13.859  1.00 73.58  ? 769  LYS   A NZ  1 
ATOM   1678 N N   . PRO   A 1 233 ? 27.598  5.334   15.564  1.00 57.17  ? 770  PRO   A N   1 
ATOM   1679 C CA  . PRO   A 1 233 ? 26.198  4.959   15.803  1.00 55.35  ? 770  PRO   A CA  1 
ATOM   1680 C C   . PRO   A 1 233 ? 25.487  5.966   16.692  1.00 56.27  ? 770  PRO   A C   1 
ATOM   1681 O O   . PRO   A 1 233 ? 26.023  6.409   17.710  1.00 58.28  ? 770  PRO   A O   1 
ATOM   1682 C CB  . PRO   A 1 233 ? 26.314  3.591   16.483  1.00 59.36  ? 770  PRO   A CB  1 
ATOM   1683 C CG  . PRO   A 1 233 ? 27.578  3.017   15.935  1.00 54.68  ? 770  PRO   A CG  1 
ATOM   1684 C CD  . PRO   A 1 233 ? 28.504  4.173   15.679  1.00 53.83  ? 770  PRO   A CD  1 
ATOM   1685 N N   . GLY   A 1 234 ? 24.283  6.355   16.275  1.00 57.34  ? 771  GLY   A N   1 
ATOM   1686 C CA  . GLY   A 1 234 ? 23.468  7.280   17.032  1.00 60.99  ? 771  GLY   A CA  1 
ATOM   1687 C C   . GLY   A 1 234 ? 23.716  8.751   16.763  1.00 58.06  ? 771  GLY   A C   1 
ATOM   1688 O O   . GLY   A 1 234 ? 22.878  9.577   17.144  1.00 64.95  ? 771  GLY   A O   1 
ATOM   1689 N N   . GLN   A 1 235 ? 24.824  9.107   16.119  1.00 52.05  ? 772  GLN   A N   1 
ATOM   1690 C CA  . GLN   A 1 235 ? 25.167  10.513  15.885  1.00 58.79  ? 772  GLN   A CA  1 
ATOM   1691 C C   . GLN   A 1 235 ? 24.533  11.042  14.602  1.00 54.65  ? 772  GLN   A C   1 
ATOM   1692 O O   . GLN   A 1 235 ? 25.219  11.604  13.748  1.00 51.07  ? 772  GLN   A O   1 
ATOM   1693 C CB  . GLN   A 1 235 ? 26.681  10.681  15.841  1.00 55.87  ? 772  GLN   A CB  1 
ATOM   1694 C CG  . GLN   A 1 235 ? 27.439  10.147  17.046  1.00 62.86  ? 772  GLN   A CG  1 
ATOM   1695 C CD  . GLN   A 1 235 ? 28.945  10.254  16.863  1.00 70.27  ? 772  GLN   A CD  1 
ATOM   1696 O OE1 . GLN   A 1 235 ? 29.429  10.523  15.761  1.00 68.95  ? 772  GLN   A OE1 1 
ATOM   1697 N NE2 . GLN   A 1 235 ? 29.692  10.050  17.945  1.00 68.08  ? 772  GLN   A NE2 1 
ATOM   1698 N N   . PHE   A 1 236 ? 23.211  10.885  14.458  1.00 54.22  ? 773  PHE   A N   1 
ATOM   1699 C CA  . PHE   A 1 236 ? 22.596  11.087  13.151  1.00 52.26  ? 773  PHE   A CA  1 
ATOM   1700 C C   . PHE   A 1 236 ? 22.619  12.543  12.691  1.00 51.04  ? 773  PHE   A C   1 
ATOM   1701 O O   . PHE   A 1 236 ? 22.452  12.794  11.493  1.00 48.47  ? 773  PHE   A O   1 
ATOM   1702 C CB  . PHE   A 1 236 ? 21.164  10.540  13.139  1.00 60.51  ? 773  PHE   A CB  1 
ATOM   1703 C CG  . PHE   A 1 236 ? 20.209  11.273  14.035  1.00 73.68  ? 773  PHE   A CG  1 
ATOM   1704 C CD1 . PHE   A 1 236 ? 19.423  12.305  13.539  1.00 75.53  ? 773  PHE   A CD1 1 
ATOM   1705 C CD2 . PHE   A 1 236 ? 20.067  10.907  15.369  1.00 82.02  ? 773  PHE   A CD2 1 
ATOM   1706 C CE1 . PHE   A 1 236 ? 18.528  12.975  14.364  1.00 79.26  ? 773  PHE   A CE1 1 
ATOM   1707 C CE2 . PHE   A 1 236 ? 19.177  11.572  16.202  1.00 81.44  ? 773  PHE   A CE2 1 
ATOM   1708 C CZ  . PHE   A 1 236 ? 18.406  12.607  15.697  1.00 80.87  ? 773  PHE   A CZ  1 
ATOM   1709 N N   . GLU   A 1 237 ? 22.839  13.510  13.588  1.00 50.60  ? 774  GLU   A N   1 
ATOM   1710 C CA  . GLU   A 1 237 ? 22.915  14.896  13.130  1.00 51.55  ? 774  GLU   A CA  1 
ATOM   1711 C C   . GLU   A 1 237 ? 24.222  15.197  12.399  1.00 44.32  ? 774  GLU   A C   1 
ATOM   1712 O O   . GLU   A 1 237 ? 24.285  16.178  11.652  1.00 54.59  ? 774  GLU   A O   1 
ATOM   1713 C CB  . GLU   A 1 237 ? 22.742  15.878  14.297  1.00 65.78  ? 774  GLU   A CB  1 
ATOM   1714 C CG  . GLU   A 1 237 ? 21.527  15.629  15.177  1.00 77.76  ? 774  GLU   A CG  1 
ATOM   1715 C CD  . GLU   A 1 237 ? 21.823  14.639  16.290  1.00 98.43  ? 774  GLU   A CD  1 
ATOM   1716 O OE1 . GLU   A 1 237 ? 20.901  14.318  17.072  1.00 107.00 ? 774  GLU   A OE1 1 
ATOM   1717 O OE2 . GLU   A 1 237 ? 22.984  14.182  16.381  1.00 103.10 ? 774  GLU   A OE2 1 
ATOM   1718 N N   . THR   A 1 238 ? 25.258  14.384  12.586  1.00 45.43  ? 775  THR   A N   1 
ATOM   1719 C CA  . THR   A 1 238 ? 26.524  14.563  11.884  1.00 50.21  ? 775  THR   A CA  1 
ATOM   1720 C C   . THR   A 1 238 ? 26.595  13.791  10.570  1.00 45.24  ? 775  THR   A C   1 
ATOM   1721 O O   . THR   A 1 238 ? 27.596  13.916  9.854   1.00 35.70  ? 775  THR   A O   1 
ATOM   1722 C CB  . THR   A 1 238 ? 27.701  14.135  12.774  1.00 54.92  ? 775  THR   A CB  1 
ATOM   1723 O OG1 . THR   A 1 238 ? 27.850  12.707  12.723  1.00 50.90  ? 775  THR   A OG1 1 
ATOM   1724 C CG2 . THR   A 1 238 ? 27.469  14.559  14.215  1.00 58.68  ? 775  THR   A CG2 1 
ATOM   1725 N N   . PHE   A 1 239 ? 25.567  12.999  10.246  1.00 38.54  ? 776  PHE   A N   1 
ATOM   1726 C CA  . PHE   A 1 239 ? 25.577  12.175  9.040   1.00 34.13  ? 776  PHE   A CA  1 
ATOM   1727 C C   . PHE   A 1 239 ? 25.717  13.031  7.787   1.00 35.08  ? 776  PHE   A C   1 
ATOM   1728 O O   . PHE   A 1 239 ? 25.018  14.036  7.627   1.00 35.08  ? 776  PHE   A O   1 
ATOM   1729 C CB  . PHE   A 1 239 ? 24.287  11.351  8.935   1.00 36.37  ? 776  PHE   A CB  1 
ATOM   1730 C CG  . PHE   A 1 239 ? 24.215  10.162  9.867   1.00 31.66  ? 776  PHE   A CG  1 
ATOM   1731 C CD1 . PHE   A 1 239 ? 25.119  9.996   10.899  1.00 34.86  ? 776  PHE   A CD1 1 
ATOM   1732 C CD2 . PHE   A 1 239 ? 23.220  9.210   9.700   1.00 33.87  ? 776  PHE   A CD2 1 
ATOM   1733 C CE1 . PHE   A 1 239 ? 25.034  8.916   11.754  1.00 37.43  ? 776  PHE   A CE1 1 
ATOM   1734 C CE2 . PHE   A 1 239 ? 23.130  8.123   10.551  1.00 40.35  ? 776  PHE   A CE2 1 
ATOM   1735 C CZ  . PHE   A 1 239 ? 24.042  7.974   11.580  1.00 39.22  ? 776  PHE   A CZ  1 
ATOM   1736 N N   . ASP   A 1 240 ? 26.594  12.605  6.881   1.00 28.86  ? 777  ASP   A N   1 
ATOM   1737 C CA  . ASP   A 1 240 ? 26.800  13.285  5.609   1.00 34.51  ? 777  ASP   A CA  1 
ATOM   1738 C C   . ASP   A 1 240 ? 27.579  12.347  4.696   1.00 34.20  ? 777  ASP   A C   1 
ATOM   1739 O O   . ASP   A 1 240 ? 28.054  11.289  5.123   1.00 31.06  ? 777  ASP   A O   1 
ATOM   1740 C CB  . ASP   A 1 240 ? 27.540  14.614  5.792   1.00 46.69  ? 777  ASP   A CB  1 
ATOM   1741 C CG  . ASP   A 1 240 ? 27.220  15.614  4.696   1.00 60.18  ? 777  ASP   A CG  1 
ATOM   1742 O OD1 . ASP   A 1 240 ? 26.542  15.239  3.707   1.00 63.38  ? 777  ASP   A OD1 1 
ATOM   1743 O OD2 . ASP   A 1 240 ? 27.650  16.780  4.827   1.00 61.16  ? 777  ASP   A OD2 1 
ATOM   1744 N N   . LEU   A 1 241 ? 27.705  12.751  3.429   1.00 26.93  ? 778  LEU   A N   1 
ATOM   1745 C CA  . LEU   A 1 241 ? 28.347  11.890  2.440   1.00 26.25  ? 778  LEU   A CA  1 
ATOM   1746 C C   . LEU   A 1 241 ? 29.759  11.497  2.872   1.00 31.64  ? 778  LEU   A C   1 
ATOM   1747 O O   . LEU   A 1 241 ? 30.173  10.347  2.695   1.00 27.67  ? 778  LEU   A O   1 
ATOM   1748 C CB  . LEU   A 1 241 ? 28.400  12.600  1.095   1.00 24.49  ? 778  LEU   A CB  1 
ATOM   1749 C CG  . LEU   A 1 241 ? 29.168  11.860  0.012   1.00 34.32  ? 778  LEU   A CG  1 
ATOM   1750 C CD1 . LEU   A 1 241 ? 28.315  10.719  -0.515  1.00 31.06  ? 778  LEU   A CD1 1 
ATOM   1751 C CD2 . LEU   A 1 241 ? 29.578  12.812  -1.097  1.00 40.13  ? 778  LEU   A CD2 1 
ATOM   1752 N N   . MET   A 1 242 ? 30.519  12.440  3.437   1.00 30.92  ? 779  MET   A N   1 
ATOM   1753 C CA  . MET   A 1 242 ? 31.924  12.176  3.719   1.00 28.61  ? 779  MET   A CA  1 
ATOM   1754 C C   . MET   A 1 242 ? 32.162  11.632  5.121   1.00 32.19  ? 779  MET   A C   1 
ATOM   1755 O O   . MET   A 1 242 ? 33.251  11.110  5.381   1.00 33.91  ? 779  MET   A O   1 
ATOM   1756 C CB  . MET   A 1 242 ? 32.760  13.450  3.511   1.00 26.81  ? 779  MET   A CB  1 
ATOM   1757 C CG  . MET   A 1 242 ? 32.772  13.960  2.060   1.00 27.66  ? 779  MET   A CG  1 
ATOM   1758 S SD  . MET   A 1 242 ? 33.678  12.768  1.002   1.00 32.36  ? 779  MET   A SD  1 
ATOM   1759 C CE  . MET   A 1 242 ? 35.362  13.354  1.161   1.00 30.38  ? 779  MET   A CE  1 
ATOM   1760 N N   . THR   A 1 243 ? 31.187  11.734  6.028   1.00 29.84  ? 780  THR   A N   1 
ATOM   1761 C CA  . THR   A 1 243 ? 31.375  11.245  7.393   1.00 31.21  ? 780  THR   A CA  1 
ATOM   1762 C C   . THR   A 1 243 ? 30.866  9.824   7.589   1.00 32.26  ? 780  THR   A C   1 
ATOM   1763 O O   . THR   A 1 243 ? 31.331  9.121   8.496   1.00 30.96  ? 780  THR   A O   1 
ATOM   1764 C CB  . THR   A 1 243 ? 30.669  12.166  8.395   1.00 32.08  ? 780  THR   A CB  1 
ATOM   1765 O OG1 . THR   A 1 243 ? 29.293  12.323  8.018   1.00 37.39  ? 780  THR   A OG1 1 
ATOM   1766 C CG2 . THR   A 1 243 ? 31.341  13.526  8.423   1.00 36.70  ? 780  THR   A CG2 1 
ATOM   1767 N N   . LEU   A 1 244 ? 29.904  9.402   6.782   1.00 29.34  ? 781  LEU   A N   1 
ATOM   1768 C CA  . LEU   A 1 244 ? 29.453  8.023   6.819   1.00 29.70  ? 781  LEU   A CA  1 
ATOM   1769 C C   . LEU   A 1 244 ? 30.445  7.150   6.061   1.00 29.31  ? 781  LEU   A C   1 
ATOM   1770 O O   . LEU   A 1 244 ? 31.280  7.638   5.301   1.00 27.16  ? 781  LEU   A O   1 
ATOM   1771 C CB  . LEU   A 1 244 ? 28.051  7.911   6.213   1.00 27.54  ? 781  LEU   A CB  1 
ATOM   1772 C CG  . LEU   A 1 244 ? 26.883  8.443   7.049   1.00 32.90  ? 781  LEU   A CG  1 
ATOM   1773 C CD1 . LEU   A 1 244 ? 25.627  8.580   6.194   1.00 28.15  ? 781  LEU   A CD1 1 
ATOM   1774 C CD2 . LEU   A 1 244 ? 26.602  7.535   8.254   1.00 31.71  ? 781  LEU   A CD2 1 
ATOM   1775 N N   . HIS   A 1 245 ? 30.355  5.854   6.278   1.00 27.31  ? 782  HIS   A N   1 
ATOM   1776 C CA  . HIS   A 1 245 ? 31.259  4.931   5.601   1.00 24.25  ? 782  HIS   A CA  1 
ATOM   1777 C C   . HIS   A 1 245 ? 30.754  4.649   4.188   1.00 27.57  ? 782  HIS   A C   1 
ATOM   1778 O O   . HIS   A 1 245 ? 29.574  4.334   4.015   1.00 25.74  ? 782  HIS   A O   1 
ATOM   1779 C CB  . HIS   A 1 245 ? 31.353  3.641   6.391   1.00 24.16  ? 782  HIS   A CB  1 
ATOM   1780 C CG  . HIS   A 1 245 ? 32.579  2.838   6.095   1.00 26.00  ? 782  HIS   A CG  1 
ATOM   1781 N ND1 . HIS   A 1 245 ? 32.798  2.247   4.868   1.00 26.23  ? 782  HIS   A ND1 1 
ATOM   1782 C CD2 . HIS   A 1 245 ? 33.649  2.528   6.865   1.00 28.56  ? 782  HIS   A CD2 1 
ATOM   1783 C CE1 . HIS   A 1 245 ? 33.959  1.614   4.895   1.00 27.13  ? 782  HIS   A CE1 1 
ATOM   1784 N NE2 . HIS   A 1 245 ? 34.493  1.766   6.095   1.00 30.63  ? 782  HIS   A NE2 1 
ATOM   1785 N N   . PRO   A 1 246 ? 31.608  4.747   3.162   1.00 24.94  ? 783  PRO   A N   1 
ATOM   1786 C CA  . PRO   A 1 246 ? 31.122  4.531   1.789   1.00 29.71  ? 783  PRO   A CA  1 
ATOM   1787 C C   . PRO   A 1 246 ? 30.534  3.143   1.572   1.00 28.19  ? 783  PRO   A C   1 
ATOM   1788 O O   . PRO   A 1 246 ? 29.577  3.000   0.803   1.00 27.33  ? 783  PRO   A O   1 
ATOM   1789 C CB  . PRO   A 1 246 ? 32.376  4.758   0.933   1.00 26.09  ? 783  PRO   A CB  1 
ATOM   1790 C CG  . PRO   A 1 246 ? 33.537  4.556   1.887   1.00 27.82  ? 783  PRO   A CG  1 
ATOM   1791 C CD  . PRO   A 1 246 ? 33.042  5.102   3.201   1.00 23.65  ? 783  PRO   A CD  1 
ATOM   1792 N N   . ILE   A 1 247 ? 31.076  2.116   2.223   1.00 26.33  ? 784  ILE   A N   1 
ATOM   1793 C CA  . ILE   A 1 247 ? 30.456  0.788   2.135   1.00 26.55  ? 784  ILE   A CA  1 
ATOM   1794 C C   . ILE   A 1 247 ? 29.016  0.844   2.623   1.00 28.57  ? 784  ILE   A C   1 
ATOM   1795 O O   . ILE   A 1 247 ? 28.092  0.336   1.969   1.00 26.87  ? 784  ILE   A O   1 
ATOM   1796 C CB  . ILE   A 1 247 ? 31.254  -0.244  2.951   1.00 26.67  ? 784  ILE   A CB  1 
ATOM   1797 C CG1 . ILE   A 1 247 ? 32.676  -0.413  2.416   1.00 32.79  ? 784  ILE   A CG1 1 
ATOM   1798 C CG2 . ILE   A 1 247 ? 30.525  -1.576  2.946   1.00 24.52  ? 784  ILE   A CG2 1 
ATOM   1799 C CD1 . ILE   A 1 247 ? 33.500  -1.425  3.248   1.00 30.27  ? 784  ILE   A CD1 1 
ATOM   1800 N N   . GLU   A 1 248 ? 28.807  1.441   3.798   1.00 28.53  ? 785  GLU   A N   1 
ATOM   1801 C CA  . GLU   A 1 248 ? 27.484  1.399   4.411   1.00 28.06  ? 785  GLU   A CA  1 
ATOM   1802 C C   . GLU   A 1 248 ? 26.502  2.329   3.711   1.00 29.66  ? 785  GLU   A C   1 
ATOM   1803 O O   . GLU   A 1 248 ? 25.302  2.026   3.675   1.00 26.12  ? 785  GLU   A O   1 
ATOM   1804 C CB  . GLU   A 1 248 ? 27.573  1.735   5.902   1.00 29.17  ? 785  GLU   A CB  1 
ATOM   1805 C CG  . GLU   A 1 248 ? 26.479  1.085   6.747   1.00 24.76  ? 785  GLU   A CG  1 
ATOM   1806 C CD  . GLU   A 1 248 ? 26.441  -0.423  6.581   1.00 33.30  ? 785  GLU   A CD  1 
ATOM   1807 O OE1 . GLU   A 1 248 ? 25.369  -0.971  6.243   1.00 31.76  ? 785  GLU   A OE1 1 
ATOM   1808 O OE2 . GLU   A 1 248 ? 27.498  -1.062  6.780   1.00 31.11  ? 785  GLU   A OE2 1 
ATOM   1809 N N   . ILE   A 1 249 ? 26.978  3.454   3.163   1.00 22.72  ? 786  ILE   A N   1 
ATOM   1810 C CA  . ILE   A 1 249 ? 26.113  4.274   2.314   1.00 27.85  ? 786  ILE   A CA  1 
ATOM   1811 C C   . ILE   A 1 249 ? 25.531  3.430   1.189   1.00 28.54  ? 786  ILE   A C   1 
ATOM   1812 O O   . ILE   A 1 249 ? 24.312  3.400   0.973   1.00 25.90  ? 786  ILE   A O   1 
ATOM   1813 C CB  . ILE   A 1 249 ? 26.882  5.482   1.754   1.00 21.99  ? 786  ILE   A CB  1 
ATOM   1814 C CG1 . ILE   A 1 249 ? 27.174  6.509   2.850   1.00 22.79  ? 786  ILE   A CG1 1 
ATOM   1815 C CG2 . ILE   A 1 249 ? 26.073  6.131   0.620   1.00 22.23  ? 786  ILE   A CG2 1 
ATOM   1816 C CD1 . ILE   A 1 249 ? 28.209  7.585   2.402   1.00 25.48  ? 786  ILE   A CD1 1 
ATOM   1817 N N   . ALA   A 1 250 ? 26.391  2.690   0.481   1.00 27.82  ? 787  ALA   A N   1 
ATOM   1818 C CA  . ALA   A 1 250 ? 25.899  1.882   -0.628  1.00 23.16  ? 787  ALA   A CA  1 
ATOM   1819 C C   . ALA   A 1 250 ? 24.995  0.756   -0.141  1.00 25.33  ? 787  ALA   A C   1 
ATOM   1820 O O   . ALA   A 1 250 ? 23.960  0.490   -0.759  1.00 26.92  ? 787  ALA   A O   1 
ATOM   1821 C CB  . ALA   A 1 250 ? 27.060  1.320   -1.439  1.00 23.92  ? 787  ALA   A CB  1 
ATOM   1822 N N   . ARG   A 1 251 ? 25.363  0.088   0.959   1.00 23.67  ? 788  ARG   A N   1 
ATOM   1823 C CA  . ARG   A 1 251 ? 24.503  -0.975  1.494   1.00 22.28  ? 788  ARG   A CA  1 
ATOM   1824 C C   . ARG   A 1 251 ? 23.125  -0.442  1.867   1.00 29.30  ? 788  ARG   A C   1 
ATOM   1825 O O   . ARG   A 1 251 ? 22.096  -1.067  1.563   1.00 26.97  ? 788  ARG   A O   1 
ATOM   1826 C CB  . ARG   A 1 251 ? 25.128  -1.615  2.731   1.00 25.77  ? 788  ARG   A CB  1 
ATOM   1827 C CG  . ARG   A 1 251 ? 26.351  -2.486  2.477   1.00 26.88  ? 788  ARG   A CG  1 
ATOM   1828 C CD  . ARG   A 1 251 ? 27.002  -2.792  3.810   1.00 29.71  ? 788  ARG   A CD  1 
ATOM   1829 N NE  . ARG   A 1 251 ? 28.082  -3.757  3.704   1.00 26.78  ? 788  ARG   A NE  1 
ATOM   1830 C CZ  . ARG   A 1 251 ? 28.799  -4.162  4.739   1.00 29.57  ? 788  ARG   A CZ  1 
ATOM   1831 N NH1 . ARG   A 1 251 ? 28.536  -3.672  5.945   1.00 30.75  ? 788  ARG   A NH1 1 
ATOM   1832 N NH2 . ARG   A 1 251 ? 29.766  -5.058  4.571   1.00 31.74  ? 788  ARG   A NH2 1 
ATOM   1833 N N   . GLN   A 1 252 ? 23.087  0.678   2.597   1.00 25.99  ? 789  GLN   A N   1 
ATOM   1834 C CA  . GLN   A 1 252 ? 21.803  1.169   3.094   1.00 26.40  ? 789  GLN   A CA  1 
ATOM   1835 C C   . GLN   A 1 252 ? 20.958  1.737   1.962   1.00 27.51  ? 789  GLN   A C   1 
ATOM   1836 O O   . GLN   A 1 252 ? 19.727  1.589   1.966   1.00 25.75  ? 789  GLN   A O   1 
ATOM   1837 C CB  . GLN   A 1 252 ? 22.008  2.218   4.190   1.00 23.89  ? 789  GLN   A CB  1 
ATOM   1838 C CG  . GLN   A 1 252 ? 22.667  1.695   5.461   1.00 25.72  ? 789  GLN   A CG  1 
ATOM   1839 C CD  . GLN   A 1 252 ? 21.884  0.556   6.100   1.00 31.21  ? 789  GLN   A CD  1 
ATOM   1840 O OE1 . GLN   A 1 252 ? 20.651  0.593   6.163   1.00 33.15  ? 789  GLN   A OE1 1 
ATOM   1841 N NE2 . GLN   A 1 252 ? 22.596  -0.464  6.573   1.00 31.52  ? 789  GLN   A NE2 1 
ATOM   1842 N N   . LEU   A 1 253 ? 21.590  2.396   0.983   1.00 25.36  ? 790  LEU   A N   1 
ATOM   1843 C CA  . LEU   A 1 253 ? 20.809  2.831   -0.172  1.00 28.55  ? 790  LEU   A CA  1 
ATOM   1844 C C   . LEU   A 1 253 ? 20.306  1.640   -0.976  1.00 31.07  ? 790  LEU   A C   1 
ATOM   1845 O O   . LEU   A 1 253 ? 19.195  1.679   -1.526  1.00 26.45  ? 790  LEU   A O   1 
ATOM   1846 C CB  . LEU   A 1 253 ? 21.625  3.769   -1.057  1.00 24.68  ? 790  LEU   A CB  1 
ATOM   1847 C CG  . LEU   A 1 253 ? 21.710  5.208   -0.534  1.00 22.02  ? 790  LEU   A CG  1 
ATOM   1848 C CD1 . LEU   A 1 253 ? 22.782  5.996   -1.295  1.00 21.10  ? 790  LEU   A CD1 1 
ATOM   1849 C CD2 . LEU   A 1 253 ? 20.380  5.932   -0.622  1.00 25.35  ? 790  LEU   A CD2 1 
ATOM   1850 N N   . THR   A 1 254 ? 21.078  0.556   -1.008  1.00 28.96  ? 791  THR   A N   1 
ATOM   1851 C CA  . THR   A 1 254 ? 20.641  -0.637  -1.723  1.00 26.53  ? 791  THR   A CA  1 
ATOM   1852 C C   . THR   A 1 254 ? 19.444  -1.293  -1.038  1.00 31.67  ? 791  THR   A C   1 
ATOM   1853 O O   . THR   A 1 254 ? 18.485  -1.695  -1.709  1.00 27.09  ? 791  THR   A O   1 
ATOM   1854 C CB  . THR   A 1 254 ? 21.801  -1.618  -1.850  1.00 25.03  ? 791  THR   A CB  1 
ATOM   1855 O OG1 . THR   A 1 254 ? 22.809  -1.015  -2.675  1.00 23.69  ? 791  THR   A OG1 1 
ATOM   1856 C CG2 . THR   A 1 254 ? 21.322  -2.922  -2.499  1.00 24.42  ? 791  THR   A CG2 1 
ATOM   1857 N N   . LEU   A 1 255 ? 19.490  -1.437  0.294   1.00 27.77  ? 792  LEU   A N   1 
ATOM   1858 C CA  . LEU   A 1 255 ? 18.334  -1.973  1.008   1.00 30.80  ? 792  LEU   A CA  1 
ATOM   1859 C C   . LEU   A 1 255 ? 17.106  -1.104  0.775   1.00 26.73  ? 792  LEU   A C   1 
ATOM   1860 O O   . LEU   A 1 255 ? 15.986  -1.612  0.623   1.00 29.05  ? 792  LEU   A O   1 
ATOM   1861 C CB  . LEU   A 1 255 ? 18.624  -2.076  2.508   1.00 26.45  ? 792  LEU   A CB  1 
ATOM   1862 C CG  . LEU   A 1 255 ? 19.659  -3.114  2.939   1.00 32.51  ? 792  LEU   A CG  1 
ATOM   1863 C CD1 . LEU   A 1 255 ? 20.052  -2.899  4.389   1.00 34.15  ? 792  LEU   A CD1 1 
ATOM   1864 C CD2 . LEU   A 1 255 ? 19.077  -4.509  2.740   1.00 34.25  ? 792  LEU   A CD2 1 
ATOM   1865 N N   . LEU   A 1 256 ? 17.298  0.212   0.769   1.00 23.25  ? 793  LEU   A N   1 
ATOM   1866 C CA  . LEU   A 1 256 ? 16.180  1.126   0.568   1.00 25.49  ? 793  LEU   A CA  1 
ATOM   1867 C C   . LEU   A 1 256 ? 15.630  1.001   -0.845  1.00 32.30  ? 793  LEU   A C   1 
ATOM   1868 O O   . LEU   A 1 256 ? 14.411  0.903   -1.042  1.00 27.61  ? 793  LEU   A O   1 
ATOM   1869 C CB  . LEU   A 1 256 ? 16.634  2.558   0.868   1.00 25.86  ? 793  LEU   A CB  1 
ATOM   1870 C CG  . LEU   A 1 256 ? 15.690  3.723   0.568   1.00 27.69  ? 793  LEU   A CG  1 
ATOM   1871 C CD1 . LEU   A 1 256 ? 14.333  3.419   1.156   1.00 42.04  ? 793  LEU   A CD1 1 
ATOM   1872 C CD2 . LEU   A 1 256 ? 16.267  5.012   1.187   1.00 28.25  ? 793  LEU   A CD2 1 
ATOM   1873 N N   . GLU   A 1 257 ? 16.516  0.972   -1.846  1.00 24.90  ? 794  GLU   A N   1 
ATOM   1874 C CA  . GLU   A 1 257 ? 16.044  0.896   -3.225  1.00 28.38  ? 794  GLU   A CA  1 
ATOM   1875 C C   . GLU   A 1 257 ? 15.460  -0.473  -3.542  1.00 27.72  ? 794  GLU   A C   1 
ATOM   1876 O O   . GLU   A 1 257 ? 14.493  -0.572  -4.310  1.00 30.03  ? 794  GLU   A O   1 
ATOM   1877 C CB  . GLU   A 1 257 ? 17.178  1.242   -4.177  1.00 22.43  ? 794  GLU   A CB  1 
ATOM   1878 C CG  . GLU   A 1 257 ? 17.565  2.720   -4.013  1.00 24.61  ? 794  GLU   A CG  1 
ATOM   1879 C CD  . GLU   A 1 257 ? 18.761  3.157   -4.837  1.00 28.86  ? 794  GLU   A CD  1 
ATOM   1880 O OE1 . GLU   A 1 257 ? 19.127  4.347   -4.734  1.00 28.66  ? 794  GLU   A OE1 1 
ATOM   1881 O OE2 . GLU   A 1 257 ? 19.323  2.334   -5.595  1.00 31.22  ? 794  GLU   A OE2 1 
ATOM   1882 N N   . SER   A 1 258 ? 16.024  -1.528  -2.957  1.00 25.77  ? 795  SER   A N   1 
ATOM   1883 C CA  . SER   A 1 258 ? 15.442  -2.856  -3.107  1.00 27.24  ? 795  SER   A CA  1 
ATOM   1884 C C   . SER   A 1 258 ? 14.018  -2.890  -2.570  1.00 34.04  ? 795  SER   A C   1 
ATOM   1885 O O   . SER   A 1 258 ? 13.123  -3.495  -3.181  1.00 27.75  ? 795  SER   A O   1 
ATOM   1886 C CB  . SER   A 1 258 ? 16.321  -3.880  -2.385  1.00 26.48  ? 795  SER   A CB  1 
ATOM   1887 O OG  . SER   A 1 258 ? 15.670  -5.129  -2.241  1.00 28.96  ? 795  SER   A OG  1 
ATOM   1888 N N   . ASP   A 1 259 ? 13.794  -2.283  -1.402  1.00 28.52  ? 796  ASP   A N   1 
ATOM   1889 C CA  . ASP   A 1 259 ? 12.444  -2.250  -0.847  1.00 35.21  ? 796  ASP   A CA  1 
ATOM   1890 C C   . ASP   A 1 259 ? 11.497  -1.471  -1.746  1.00 35.45  ? 796  ASP   A C   1 
ATOM   1891 O O   . ASP   A 1 259 ? 10.361  -1.902  -1.973  1.00 31.97  ? 796  ASP   A O   1 
ATOM   1892 C CB  . ASP   A 1 259 ? 12.449  -1.643  0.554   1.00 37.80  ? 796  ASP   A CB  1 
ATOM   1893 C CG  . ASP   A 1 259 ? 12.999  -2.589  1.602   1.00 47.08  ? 796  ASP   A CG  1 
ATOM   1894 O OD1 . ASP   A 1 259 ? 13.126  -3.802  1.315   1.00 48.24  ? 796  ASP   A OD1 1 
ATOM   1895 O OD2 . ASP   A 1 259 ? 13.302  -2.115  2.722   1.00 46.44  ? 796  ASP   A OD2 1 
ATOM   1896 N N   . LEU   A 1 260 ? 11.939  -0.310  -2.251  1.00 25.36  ? 797  LEU   A N   1 
ATOM   1897 C CA  . LEU   A 1 260 ? 11.058  0.495   -3.091  1.00 27.56  ? 797  LEU   A CA  1 
ATOM   1898 C C   . LEU   A 1 260 ? 10.722  -0.236  -4.380  1.00 31.06  ? 797  LEU   A C   1 
ATOM   1899 O O   . LEU   A 1 260 ? 9.562   -0.250  -4.813  1.00 29.35  ? 797  LEU   A O   1 
ATOM   1900 C CB  . LEU   A 1 260 ? 11.707  1.845   -3.390  1.00 26.45  ? 797  LEU   A CB  1 
ATOM   1901 C CG  . LEU   A 1 260 ? 11.916  2.722   -2.159  1.00 29.32  ? 797  LEU   A CG  1 
ATOM   1902 C CD1 . LEU   A 1 260 ? 12.650  3.999   -2.564  1.00 31.99  ? 797  LEU   A CD1 1 
ATOM   1903 C CD2 . LEU   A 1 260 ? 10.576  3.025   -1.496  1.00 32.00  ? 797  LEU   A CD2 1 
ATOM   1904 N N   . TYR   A 1 261 ? 11.730  -0.871  -4.991  1.00 26.40  ? 798  TYR   A N   1 
ATOM   1905 C CA  . TYR   A 1 261 ? 11.510  -1.642  -6.208  1.00 28.14  ? 798  TYR   A CA  1 
ATOM   1906 C C   . TYR   A 1 261 ? 10.540  -2.790  -5.964  1.00 31.08  ? 798  TYR   A C   1 
ATOM   1907 O O   . TYR   A 1 261 ? 9.621   -3.020  -6.765  1.00 30.61  ? 798  TYR   A O   1 
ATOM   1908 C CB  . TYR   A 1 261 ? 12.855  -2.160  -6.727  1.00 29.25  ? 798  TYR   A CB  1 
ATOM   1909 C CG  . TYR   A 1 261 ? 12.791  -2.957  -8.015  1.00 32.94  ? 798  TYR   A CG  1 
ATOM   1910 C CD1 . TYR   A 1 261 ? 12.611  -4.338  -8.000  1.00 29.76  ? 798  TYR   A CD1 1 
ATOM   1911 C CD2 . TYR   A 1 261 ? 12.939  -2.334  -9.243  1.00 35.30  ? 798  TYR   A CD2 1 
ATOM   1912 C CE1 . TYR   A 1 261 ? 12.545  -5.069  -9.186  1.00 30.50  ? 798  TYR   A CE1 1 
ATOM   1913 C CE2 . TYR   A 1 261 ? 12.882  -3.061  -10.434 1.00 33.70  ? 798  TYR   A CE2 1 
ATOM   1914 C CZ  . TYR   A 1 261 ? 12.693  -4.423  -10.396 1.00 33.64  ? 798  TYR   A CZ  1 
ATOM   1915 O OH  . TYR   A 1 261 ? 12.647  -5.123  -11.582 1.00 33.95  ? 798  TYR   A OH  1 
ATOM   1916 N N   . ARG   A 1 262 ? 10.724  -3.517  -4.857  1.00 27.68  ? 799  ARG   A N   1 
ATOM   1917 C CA  . ARG   A 1 262 ? 9.890   -4.684  -4.571  1.00 25.61  ? 799  ARG   A CA  1 
ATOM   1918 C C   . ARG   A 1 262 ? 8.413   -4.313  -4.442  1.00 28.96  ? 799  ARG   A C   1 
ATOM   1919 O O   . ARG   A 1 262 ? 7.540   -5.131  -4.759  1.00 29.14  ? 799  ARG   A O   1 
ATOM   1920 C CB  . ARG   A 1 262 ? 10.387  -5.377  -3.293  1.00 30.21  ? 799  ARG   A CB  1 
ATOM   1921 C CG  . ARG   A 1 262 ? 9.466   -6.494  -2.780  1.00 42.53  ? 799  ARG   A CG  1 
ATOM   1922 C CD  . ARG   A 1 262 ? 9.963   -7.115  -1.474  1.00 48.80  ? 799  ARG   A CD  1 
ATOM   1923 N NE  . ARG   A 1 262 ? 10.258  -6.115  -0.451  1.00 59.90  ? 799  ARG   A NE  1 
ATOM   1924 C CZ  . ARG   A 1 262 ? 9.350   -5.581  0.362   1.00 60.23  ? 799  ARG   A CZ  1 
ATOM   1925 N NH1 . ARG   A 1 262 ? 8.078   -5.942  0.273   1.00 47.78  ? 799  ARG   A NH1 1 
ATOM   1926 N NH2 . ARG   A 1 262 ? 9.714   -4.680  1.262   1.00 61.95  ? 799  ARG   A NH2 1 
ATOM   1927 N N   . LYS   A 1 263 ? 8.107   -3.106  -3.979  1.00 27.83  ? 800  LYS   A N   1 
ATOM   1928 C CA  . LYS   A 1 263 ? 6.711   -2.751  -3.712  1.00 25.27  ? 800  LYS   A CA  1 
ATOM   1929 C C   . LYS   A 1 263 ? 5.950   -2.239  -4.931  1.00 29.09  ? 800  LYS   A C   1 
ATOM   1930 O O   . LYS   A 1 263 ? 4.748   -1.957  -4.817  1.00 31.04  ? 800  LYS   A O   1 
ATOM   1931 C CB  . LYS   A 1 263 ? 6.639   -1.700  -2.600  1.00 35.13  ? 800  LYS   A CB  1 
ATOM   1932 C CG  . LYS   A 1 263 ? 7.087   -2.213  -1.237  1.00 38.92  ? 800  LYS   A CG  1 
ATOM   1933 C CD  . LYS   A 1 263 ? 7.031   -1.113  -0.190  1.00 44.56  ? 800  LYS   A CD  1 
ATOM   1934 C CE  . LYS   A 1 263 ? 7.381   -1.650  1.184   1.00 60.78  ? 800  LYS   A CE  1 
ATOM   1935 N NZ  . LYS   A 1 263 ? 7.249   -0.599  2.228   1.00 66.89  ? 800  LYS   A NZ  1 
ATOM   1936 N N   . VAL   A 1 264 ? 6.591   -2.095  -6.086  1.00 28.68  ? 801  VAL   A N   1 
ATOM   1937 C CA  . VAL   A 1 264 ? 5.884   -1.561  -7.245  1.00 26.09  ? 801  VAL   A CA  1 
ATOM   1938 C C   . VAL   A 1 264 ? 4.988   -2.635  -7.840  1.00 29.00  ? 801  VAL   A C   1 
ATOM   1939 O O   . VAL   A 1 264 ? 5.437   -3.745  -8.139  1.00 28.54  ? 801  VAL   A O   1 
ATOM   1940 C CB  . VAL   A 1 264 ? 6.878   -1.026  -8.287  1.00 28.89  ? 801  VAL   A CB  1 
ATOM   1941 C CG1 . VAL   A 1 264 ? 6.137   -0.554  -9.522  1.00 26.23  ? 801  VAL   A CG1 1 
ATOM   1942 C CG2 . VAL   A 1 264 ? 7.694   0.133   -7.687  1.00 28.61  ? 801  VAL   A CG2 1 
ATOM   1943 N N   . GLN   A 1 265 ? 3.701   -2.313  -8.006  1.00 26.82  ? 802  GLN   A N   1 
ATOM   1944 C CA  . GLN   A 1 265 ? 2.791   -3.231  -8.659  1.00 27.57  ? 802  GLN   A CA  1 
ATOM   1945 C C   . GLN   A 1 265 ? 2.677   -2.894  -10.140 1.00 27.95  ? 802  GLN   A C   1 
ATOM   1946 O O   . GLN   A 1 265 ? 2.675   -1.718  -10.509 1.00 28.73  ? 802  GLN   A O   1 
ATOM   1947 C CB  . GLN   A 1 265 ? 1.393   -3.177  -8.029  1.00 28.63  ? 802  GLN   A CB  1 
ATOM   1948 C CG  . GLN   A 1 265 ? 1.359   -3.542  -6.558  1.00 35.33  ? 802  GLN   A CG  1 
ATOM   1949 C CD  . GLN   A 1 265 ? 1.958   -4.911  -6.299  1.00 51.32  ? 802  GLN   A CD  1 
ATOM   1950 O OE1 . GLN   A 1 265 ? 1.575   -5.897  -6.929  1.00 42.51  ? 802  GLN   A OE1 1 
ATOM   1951 N NE2 . GLN   A 1 265 ? 2.917   -4.974  -5.381  1.00 49.11  ? 802  GLN   A NE2 1 
ATOM   1952 N N   . PRO   A 1 266 ? 2.532   -3.914  -10.992 1.00 28.67  ? 803  PRO   A N   1 
ATOM   1953 C CA  . PRO   A 1 266 ? 2.417   -3.667  -12.444 1.00 31.17  ? 803  PRO   A CA  1 
ATOM   1954 C C   . PRO   A 1 266 ? 1.320   -2.682  -12.859 1.00 33.04  ? 803  PRO   A C   1 
ATOM   1955 O O   . PRO   A 1 266 ? 1.541   -1.901  -13.793 1.00 30.15  ? 803  PRO   A O   1 
ATOM   1956 C CB  . PRO   A 1 266 ? 2.149   -5.082  -12.996 1.00 35.25  ? 803  PRO   A CB  1 
ATOM   1957 C CG  . PRO   A 1 266 ? 2.808   -5.979  -12.017 1.00 40.23  ? 803  PRO   A CG  1 
ATOM   1958 C CD  . PRO   A 1 266 ? 2.627   -5.350  -10.676 1.00 35.52  ? 803  PRO   A CD  1 
ATOM   1959 N N   . SER   A 1 267 ? 0.144   -2.694  -12.220 1.00 27.99  ? 804  SER   A N   1 
ATOM   1960 C CA  . SER   A 1 267 ? -0.904  -1.764  -12.642 1.00 33.93  ? 804  SER   A CA  1 
ATOM   1961 C C   . SER   A 1 267 ? -0.515  -0.302  -12.420 1.00 31.73  ? 804  SER   A C   1 
ATOM   1962 O O   . SER   A 1 267 ? -1.127  0.584   -13.029 1.00 33.47  ? 804  SER   A O   1 
ATOM   1963 C CB  . SER   A 1 267 ? -2.223  -2.058  -11.920 1.00 33.19  ? 804  SER   A CB  1 
ATOM   1964 O OG  . SER   A 1 267 ? -2.108  -1.766  -10.537 1.00 33.29  ? 804  SER   A OG  1 
ATOM   1965 N N   . GLU   A 1 268 ? 0.485   -0.027  -11.567 1.00 28.50  ? 805  GLU   A N   1 
ATOM   1966 C CA  . GLU   A 1 268 ? 0.964   1.342   -11.391 1.00 28.40  ? 805  GLU   A CA  1 
ATOM   1967 C C   . GLU   A 1 268 ? 1.647   1.881   -12.640 1.00 31.56  ? 805  GLU   A C   1 
ATOM   1968 O O   . GLU   A 1 268 ? 1.800   3.098   -12.774 1.00 32.24  ? 805  GLU   A O   1 
ATOM   1969 C CB  . GLU   A 1 268 ? 1.938   1.409   -10.202 1.00 27.11  ? 805  GLU   A CB  1 
ATOM   1970 C CG  . GLU   A 1 268 ? 1.334   0.857   -8.903  1.00 29.48  ? 805  GLU   A CG  1 
ATOM   1971 C CD  . GLU   A 1 268 ? 2.233   1.031   -7.678  1.00 30.58  ? 805  GLU   A CD  1 
ATOM   1972 O OE1 . GLU   A 1 268 ? 2.807   2.122   -7.490  1.00 30.07  ? 805  GLU   A OE1 1 
ATOM   1973 O OE2 . GLU   A 1 268 ? 2.333   0.081   -6.882  1.00 33.71  ? 805  GLU   A OE2 1 
ATOM   1974 N N   . LEU   A 1 269 ? 2.067   0.994   -13.542 1.00 30.20  ? 806  LEU   A N   1 
ATOM   1975 C CA  . LEU   A 1 269 ? 2.775   1.331   -14.769 1.00 33.46  ? 806  LEU   A CA  1 
ATOM   1976 C C   . LEU   A 1 269 ? 1.891   1.325   -16.009 1.00 35.59  ? 806  LEU   A C   1 
ATOM   1977 O O   . LEU   A 1 269 ? 2.277   1.903   -17.034 1.00 43.31  ? 806  LEU   A O   1 
ATOM   1978 C CB  . LEU   A 1 269 ? 3.925   0.336   -14.974 1.00 32.35  ? 806  LEU   A CB  1 
ATOM   1979 C CG  . LEU   A 1 269 ? 4.952   0.425   -13.844 1.00 34.85  ? 806  LEU   A CG  1 
ATOM   1980 C CD1 . LEU   A 1 269 ? 5.393   -0.935  -13.383 1.00 41.74  ? 806  LEU   A CD1 1 
ATOM   1981 C CD2 . LEU   A 1 269 ? 6.121   1.227   -14.353 1.00 40.80  ? 806  LEU   A CD2 1 
ATOM   1982 N N   . VAL   A 1 270 ? 0.714   0.719   -15.933 1.00 32.33  ? 807  VAL   A N   1 
ATOM   1983 C CA  . VAL   A 1 270 ? -0.141  0.537   -17.102 1.00 31.43  ? 807  VAL   A CA  1 
ATOM   1984 C C   . VAL   A 1 270 ? -0.868  1.834   -17.416 1.00 35.19  ? 807  VAL   A C   1 
ATOM   1985 O O   . VAL   A 1 270 ? -1.341  2.530   -16.513 1.00 37.19  ? 807  VAL   A O   1 
ATOM   1986 C CB  . VAL   A 1 270 ? -1.143  -0.606  -16.860 1.00 32.43  ? 807  VAL   A CB  1 
ATOM   1987 C CG1 . VAL   A 1 270 ? -2.153  -0.712  -18.018 1.00 34.31  ? 807  VAL   A CG1 1 
ATOM   1988 C CG2 . VAL   A 1 270 ? -0.409  -1.942  -16.673 1.00 31.48  ? 807  VAL   A CG2 1 
ATOM   1989 N N   . GLY   A 1 271 ? -0.990  2.147   -18.703 1.00 40.25  ? 808  GLY   A N   1 
ATOM   1990 C CA  . GLY   A 1 271 ? -1.718  3.335   -19.098 1.00 46.03  ? 808  GLY   A CA  1 
ATOM   1991 C C   . GLY   A 1 271 ? -1.058  4.621   -18.669 1.00 44.07  ? 808  GLY   A C   1 
ATOM   1992 O O   . GLY   A 1 271 ? -1.724  5.659   -18.617 1.00 38.17  ? 808  GLY   A O   1 
ATOM   1993 N N   . SER   A 1 272 ? 0.236   4.569   -18.345 1.00 36.28  ? 809  SER   A N   1 
ATOM   1994 C CA  . SER   A 1 272 ? 1.006   5.733   -17.915 1.00 42.57  ? 809  SER   A CA  1 
ATOM   1995 C C   . SER   A 1 272 ? 0.325   6.472   -16.766 1.00 45.59  ? 809  SER   A C   1 
ATOM   1996 O O   . SER   A 1 272 ? 0.398   7.697   -16.672 1.00 51.72  ? 809  SER   A O   1 
ATOM   1997 C CB  . SER   A 1 272 ? 1.263   6.680   -19.091 1.00 49.85  ? 809  SER   A CB  1 
ATOM   1998 O OG  . SER   A 1 272 ? 2.106   6.076   -20.057 1.00 59.01  ? 809  SER   A OG  1 
ATOM   1999 N N   . VAL   A 1 273 ? -0.340  5.724   -15.876 1.00 41.21  ? 810  VAL   A N   1 
ATOM   2000 C CA  . VAL   A 1 273 ? -1.158  6.375   -14.855 1.00 42.38  ? 810  VAL   A CA  1 
ATOM   2001 C C   . VAL   A 1 273 ? -0.313  7.181   -13.873 1.00 40.80  ? 810  VAL   A C   1 
ATOM   2002 O O   . VAL   A 1 273 ? -0.843  8.080   -13.209 1.00 43.32  ? 810  VAL   A O   1 
ATOM   2003 C CB  . VAL   A 1 273 ? -2.045  5.376   -14.078 1.00 41.91  ? 810  VAL   A CB  1 
ATOM   2004 C CG1 . VAL   A 1 273 ? -3.275  5.007   -14.891 1.00 44.15  ? 810  VAL   A CG1 1 
ATOM   2005 C CG2 . VAL   A 1 273 ? -1.257  4.128   -13.666 1.00 31.18  ? 810  VAL   A CG2 1 
ATOM   2006 N N   . TRP   A 1 274 ? 0.993   6.915   -13.776 1.00 30.74  ? 811  TRP   A N   1 
ATOM   2007 C CA  . TRP   A 1 274 ? 1.788   7.667   -12.817 1.00 31.56  ? 811  TRP   A CA  1 
ATOM   2008 C C   . TRP   A 1 274 ? 2.051   9.093   -13.276 1.00 35.86  ? 811  TRP   A C   1 
ATOM   2009 O O   . TRP   A 1 274 ? 2.572   9.886   -12.485 1.00 36.45  ? 811  TRP   A O   1 
ATOM   2010 C CB  . TRP   A 1 274 ? 3.120   6.962   -12.525 1.00 35.23  ? 811  TRP   A CB  1 
ATOM   2011 C CG  . TRP   A 1 274 ? 4.172   7.104   -13.570 1.00 31.14  ? 811  TRP   A CG  1 
ATOM   2012 C CD1 . TRP   A 1 274 ? 5.162   8.051   -13.619 1.00 35.86  ? 811  TRP   A CD1 1 
ATOM   2013 C CD2 . TRP   A 1 274 ? 4.380   6.249   -14.701 1.00 30.47  ? 811  TRP   A CD2 1 
ATOM   2014 N NE1 . TRP   A 1 274 ? 5.949   7.852   -14.725 1.00 34.45  ? 811  TRP   A NE1 1 
ATOM   2015 C CE2 . TRP   A 1 274 ? 5.499   6.747   -15.399 1.00 34.31  ? 811  TRP   A CE2 1 
ATOM   2016 C CE3 . TRP   A 1 274 ? 3.712   5.123   -15.204 1.00 32.65  ? 811  TRP   A CE3 1 
ATOM   2017 C CZ2 . TRP   A 1 274 ? 5.970   6.158   -16.571 1.00 35.83  ? 811  TRP   A CZ2 1 
ATOM   2018 C CZ3 . TRP   A 1 274 ? 4.187   4.532   -16.362 1.00 39.97  ? 811  TRP   A CZ3 1 
ATOM   2019 C CH2 . TRP   A 1 274 ? 5.309   5.051   -17.034 1.00 40.01  ? 811  TRP   A CH2 1 
ATOM   2020 N N   . THR   A 1 275 ? 1.712   9.428   -14.522 1.00 40.36  ? 812  THR   A N   1 
ATOM   2021 C CA  . THR   A 1 275 ? 1.844   10.785  -15.039 1.00 43.95  ? 812  THR   A CA  1 
ATOM   2022 C C   . THR   A 1 275 ? 0.513   11.505  -15.139 1.00 43.07  ? 812  THR   A C   1 
ATOM   2023 O O   . THR   A 1 275 ? 0.485   12.666  -15.565 1.00 48.24  ? 812  THR   A O   1 
ATOM   2024 C CB  . THR   A 1 275 ? 2.504   10.773  -16.424 1.00 32.78  ? 812  THR   A CB  1 
ATOM   2025 O OG1 . THR   A 1 275 ? 1.607   10.166  -17.369 1.00 39.92  ? 812  THR   A OG1 1 
ATOM   2026 C CG2 . THR   A 1 275 ? 3.799   9.973   -16.382 1.00 35.79  ? 812  THR   A CG2 1 
ATOM   2027 N N   . LYS   A 1 276 ? -0.584  10.860  -14.780 1.00 45.91  ? 813  LYS   A N   1 
ATOM   2028 C CA  . LYS   A 1 276 ? -1.894  11.430  -15.020 1.00 49.11  ? 813  LYS   A CA  1 
ATOM   2029 C C   . LYS   A 1 276 ? -2.518  11.908  -13.708 1.00 51.21  ? 813  LYS   A C   1 
ATOM   2030 O O   . LYS   A 1 276 ? -1.914  11.817  -12.631 1.00 50.66  ? 813  LYS   A O   1 
ATOM   2031 C CB  . LYS   A 1 276 ? -2.786  10.414  -15.751 1.00 51.07  ? 813  LYS   A CB  1 
ATOM   2032 C CG  . LYS   A 1 276 ? -2.223  9.958   -17.104 1.00 49.14  ? 813  LYS   A CG  1 
ATOM   2033 C CD  . LYS   A 1 276 ? -3.248  9.115   -17.865 1.00 55.48  ? 813  LYS   A CD  1 
ATOM   2034 C CE  . LYS   A 1 276 ? -2.782  8.768   -19.275 1.00 64.80  ? 813  LYS   A CE  1 
ATOM   2035 N NZ  . LYS   A 1 276 ? -3.881  8.184   -20.106 1.00 73.19  ? 813  LYS   A NZ  1 
ATOM   2036 N N   . GLU   A 1 277 ? -3.758  12.387  -13.821 1.00 50.85  ? 814  GLU   A N   1 
ATOM   2037 C CA  . GLU   A 1 277 ? -4.445  13.140  -12.774 1.00 58.95  ? 814  GLU   A CA  1 
ATOM   2038 C C   . GLU   A 1 277 ? -4.373  12.467  -11.402 1.00 49.10  ? 814  GLU   A C   1 
ATOM   2039 O O   . GLU   A 1 277 ? -3.945  13.085  -10.419 1.00 64.95  ? 814  GLU   A O   1 
ATOM   2040 C CB  . GLU   A 1 277 ? -5.894  13.340  -13.221 1.00 70.12  ? 814  GLU   A CB  1 
ATOM   2041 C CG  . GLU   A 1 277 ? -6.787  14.153  -12.329 1.00 85.07  ? 814  GLU   A CG  1 
ATOM   2042 C CD  . GLU   A 1 277 ? -8.159  14.336  -12.962 1.00 100.66 ? 814  GLU   A CD  1 
ATOM   2043 O OE1 . GLU   A 1 277 ? -9.178  14.004  -12.315 1.00 104.82 ? 814  GLU   A OE1 1 
ATOM   2044 O OE2 . GLU   A 1 277 ? -8.209  14.787  -14.127 1.00 103.87 ? 814  GLU   A OE2 1 
ATOM   2045 N N   . ASP   A 1 278 ? -4.787  11.201  -11.312 1.00 43.71  ? 815  ASP   A N   1 
ATOM   2046 C CA  . ASP   A 1 278 ? -4.875  10.493  -10.037 1.00 49.92  ? 815  ASP   A CA  1 
ATOM   2047 C C   . ASP   A 1 278 ? -3.611  9.694   -9.700  1.00 43.16  ? 815  ASP   A C   1 
ATOM   2048 O O   . ASP   A 1 278 ? -3.696  8.656   -9.027  1.00 43.70  ? 815  ASP   A O   1 
ATOM   2049 C CB  . ASP   A 1 278 ? -6.092  9.574   -10.045 1.00 51.76  ? 815  ASP   A CB  1 
ATOM   2050 C CG  . ASP   A 1 278 ? -7.387  10.326  -10.270 1.00 59.26  ? 815  ASP   A CG  1 
ATOM   2051 O OD1 . ASP   A 1 278 ? -7.557  11.411  -9.683  1.00 56.47  ? 815  ASP   A OD1 1 
ATOM   2052 O OD2 . ASP   A 1 278 ? -8.227  9.828   -11.043 1.00 57.31  ? 815  ASP   A OD2 1 
ATOM   2053 N N   . LYS   A 1 279 ? -2.443  10.173  -10.128 1.00 41.12  ? 816  LYS   A N   1 
ATOM   2054 C CA  . LYS   A 1 279 ? -1.203  9.408   -9.991  1.00 42.28  ? 816  LYS   A CA  1 
ATOM   2055 C C   . LYS   A 1 279 ? -0.933  9.000   -8.544  1.00 42.25  ? 816  LYS   A C   1 
ATOM   2056 O O   . LYS   A 1 279 ? -0.408  7.906   -8.290  1.00 34.29  ? 816  LYS   A O   1 
ATOM   2057 C CB  . LYS   A 1 279 ? -0.031  10.220  -10.546 1.00 40.26  ? 816  LYS   A CB  1 
ATOM   2058 C CG  . LYS   A 1 279 ? 0.166   11.580  -9.872  1.00 44.97  ? 816  LYS   A CG  1 
ATOM   2059 C CD  . LYS   A 1 279 ? 1.427   12.313  -10.353 1.00 46.94  ? 816  LYS   A CD  1 
ATOM   2060 C CE  . LYS   A 1 279 ? 1.237   12.950  -11.722 1.00 59.20  ? 816  LYS   A CE  1 
ATOM   2061 N NZ  . LYS   A 1 279 ? 0.553   14.272  -11.636 1.00 72.64  ? 816  LYS   A NZ  1 
ATOM   2062 N N   . GLU   A 1 280 ? -1.274  9.860   -7.579  1.00 37.61  ? 817  GLU   A N   1 
ATOM   2063 C CA  . GLU   A 1 280 ? -0.901  9.569   -6.197  1.00 40.12  ? 817  GLU   A CA  1 
ATOM   2064 C C   . GLU   A 1 280 ? -1.659  8.366   -5.660  1.00 39.34  ? 817  GLU   A C   1 
ATOM   2065 O O   . GLU   A 1 280 ? -1.116  7.608   -4.846  1.00 41.41  ? 817  GLU   A O   1 
ATOM   2066 C CB  . GLU   A 1 280 ? -1.148  10.784  -5.302  1.00 44.26  ? 817  GLU   A CB  1 
ATOM   2067 C CG  . GLU   A 1 280 ? -0.502  12.056  -5.785  1.00 41.95  ? 817  GLU   A CG  1 
ATOM   2068 C CD  . GLU   A 1 280 ? 1.011   12.017  -5.713  1.00 38.83  ? 817  GLU   A CD  1 
ATOM   2069 O OE1 . GLU   A 1 280 ? 1.567   11.198  -4.939  1.00 39.87  ? 817  GLU   A OE1 1 
ATOM   2070 O OE2 . GLU   A 1 280 ? 1.649   12.784  -6.461  1.00 41.49  ? 817  GLU   A OE2 1 
ATOM   2071 N N   . ILE   A 1 281 ? -2.902  8.179   -6.105  1.00 35.17  ? 818  ILE   A N   1 
ATOM   2072 C CA  . ILE   A 1 281 ? -3.707  7.036   -5.694  1.00 37.91  ? 818  ILE   A CA  1 
ATOM   2073 C C   . ILE   A 1 281 ? -3.332  5.789   -6.483  1.00 34.48  ? 818  ILE   A C   1 
ATOM   2074 O O   . ILE   A 1 281 ? -3.327  4.675   -5.942  1.00 34.14  ? 818  ILE   A O   1 
ATOM   2075 C CB  . ILE   A 1 281 ? -5.203  7.373   -5.865  1.00 38.46  ? 818  ILE   A CB  1 
ATOM   2076 C CG1 . ILE   A 1 281 ? -5.617  8.487   -4.898  1.00 50.97  ? 818  ILE   A CG1 1 
ATOM   2077 C CG2 . ILE   A 1 281 ? -6.078  6.137   -5.684  1.00 45.86  ? 818  ILE   A CG2 1 
ATOM   2078 C CD1 . ILE   A 1 281 ? -5.518  8.093   -3.448  1.00 63.85  ? 818  ILE   A CD1 1 
ATOM   2079 N N   . ASN   A 1 282 ? -3.044  5.943   -7.775  1.00 35.56  ? 819  ASN   A N   1 
ATOM   2080 C CA  . ASN   A 1 282 ? -2.913  4.787   -8.654  1.00 35.56  ? 819  ASN   A CA  1 
ATOM   2081 C C   . ASN   A 1 282 ? -1.490  4.272   -8.755  1.00 31.86  ? 819  ASN   A C   1 
ATOM   2082 O O   . ASN   A 1 282 ? -1.297  3.094   -9.090  1.00 35.96  ? 819  ASN   A O   1 
ATOM   2083 C CB  . ASN   A 1 282 ? -3.427  5.120   -10.058 1.00 33.74  ? 819  ASN   A CB  1 
ATOM   2084 C CG  . ASN   A 1 282 ? -4.940  5.242   -10.112 1.00 35.01  ? 819  ASN   A CG  1 
ATOM   2085 O OD1 . ASN   A 1 282 ? -5.655  4.577   -9.371  1.00 41.81  ? 819  ASN   A OD1 1 
ATOM   2086 N ND2 . ASN   A 1 282 ? -5.429  6.109   -10.991 1.00 45.46  ? 819  ASN   A ND2 1 
ATOM   2087 N N   . SER   A 1 283 ? -0.494  5.107   -8.455  1.00 29.91  ? 820  SER   A N   1 
ATOM   2088 C CA  . SER   A 1 283 ? 0.910   4.713   -8.599  1.00 28.20  ? 820  SER   A CA  1 
ATOM   2089 C C   . SER   A 1 283 ? 1.766   5.083   -7.390  1.00 27.62  ? 820  SER   A C   1 
ATOM   2090 O O   . SER   A 1 283 ? 2.880   5.587   -7.547  1.00 28.10  ? 820  SER   A O   1 
ATOM   2091 C CB  . SER   A 1 283 ? 1.489   5.357   -9.854  1.00 34.55  ? 820  SER   A CB  1 
ATOM   2092 O OG  . SER   A 1 283 ? 0.652   5.096   -10.973 1.00 34.57  ? 820  SER   A OG  1 
ATOM   2093 N N   . PRO   A 1 284 ? 1.299   4.814   -6.164  1.00 33.36  ? 821  PRO   A N   1 
ATOM   2094 C CA  . PRO   A 1 284 ? 2.024   5.355   -5.003  1.00 33.35  ? 821  PRO   A CA  1 
ATOM   2095 C C   . PRO   A 1 284 ? 3.406   4.767   -4.830  1.00 30.76  ? 821  PRO   A C   1 
ATOM   2096 O O   . PRO   A 1 284 ? 4.333   5.494   -4.455  1.00 28.25  ? 821  PRO   A O   1 
ATOM   2097 C CB  . PRO   A 1 284 ? 1.114   5.010   -3.819  1.00 35.65  ? 821  PRO   A CB  1 
ATOM   2098 C CG  . PRO   A 1 284 ? 0.353   3.788   -4.290  1.00 39.23  ? 821  PRO   A CG  1 
ATOM   2099 C CD  . PRO   A 1 284 ? 0.130   4.019   -5.755  1.00 33.29  ? 821  PRO   A CD  1 
ATOM   2100 N N   . ASN   A 1 285 ? 3.580   3.470   -5.076  1.00 28.87  ? 822  ASN   A N   1 
ATOM   2101 C CA  . ASN   A 1 285 ? 4.903   2.877   -4.896  1.00 23.87  ? 822  ASN   A CA  1 
ATOM   2102 C C   . ASN   A 1 285 ? 5.846   3.260   -6.025  1.00 28.69  ? 822  ASN   A C   1 
ATOM   2103 O O   . ASN   A 1 285 ? 7.033   3.541   -5.790  1.00 27.92  ? 822  ASN   A O   1 
ATOM   2104 C CB  . ASN   A 1 285 ? 4.742   1.362   -4.770  1.00 28.36  ? 822  ASN   A CB  1 
ATOM   2105 C CG  . ASN   A 1 285 ? 3.797   1.004   -3.672  1.00 35.58  ? 822  ASN   A CG  1 
ATOM   2106 O OD1 . ASN   A 1 285 ? 4.123   1.184   -2.504  1.00 33.71  ? 822  ASN   A OD1 1 
ATOM   2107 N ND2 . ASN   A 1 285 ? 2.598   0.515   -4.029  1.00 31.39  ? 822  ASN   A ND2 1 
ATOM   2108 N N   . LEU   A 1 286 ? 5.334   3.298   -7.254  1.00 27.17  ? 823  LEU   A N   1 
ATOM   2109 C CA  . LEU   A 1 286 ? 6.139   3.770   -8.377  1.00 28.29  ? 823  LEU   A CA  1 
ATOM   2110 C C   . LEU   A 1 286 ? 6.628   5.201   -8.144  1.00 29.35  ? 823  LEU   A C   1 
ATOM   2111 O O   . LEU   A 1 286 ? 7.794   5.526   -8.396  1.00 27.83  ? 823  LEU   A O   1 
ATOM   2112 C CB  . LEU   A 1 286 ? 5.317   3.677   -9.659  1.00 31.47  ? 823  LEU   A CB  1 
ATOM   2113 C CG  . LEU   A 1 286 ? 5.898   4.204   -10.970 1.00 35.18  ? 823  LEU   A CG  1 
ATOM   2114 C CD1 . LEU   A 1 286 ? 7.221   3.633   -11.191 1.00 33.38  ? 823  LEU   A CD1 1 
ATOM   2115 C CD2 . LEU   A 1 286 ? 4.979   3.834   -12.122 1.00 34.21  ? 823  LEU   A CD2 1 
ATOM   2116 N N   . LEU   A 1 287 ? 5.747   6.073   -7.653  1.00 29.11  ? 824  LEU   A N   1 
ATOM   2117 C CA  . LEU   A 1 287 ? 6.136   7.472   -7.445  1.00 28.64  ? 824  LEU   A CA  1 
ATOM   2118 C C   . LEU   A 1 287 ? 7.199   7.595   -6.357  1.00 30.46  ? 824  LEU   A C   1 
ATOM   2119 O O   . LEU   A 1 287 ? 8.137   8.396   -6.482  1.00 28.30  ? 824  LEU   A O   1 
ATOM   2120 C CB  . LEU   A 1 287 ? 4.896   8.306   -7.099  1.00 27.11  ? 824  LEU   A CB  1 
ATOM   2121 C CG  . LEU   A 1 287 ? 3.969   8.588   -8.277  1.00 32.58  ? 824  LEU   A CG  1 
ATOM   2122 C CD1 . LEU   A 1 287 ? 2.660   9.218   -7.803  1.00 30.17  ? 824  LEU   A CD1 1 
ATOM   2123 C CD2 . LEU   A 1 287 ? 4.656   9.459   -9.307  1.00 29.99  ? 824  LEU   A CD2 1 
ATOM   2124 N N   . LYS   A 1 288 ? 7.086   6.790   -5.296  1.00 30.32  ? 825  LYS   A N   1 
ATOM   2125 C CA  . LYS   A 1 288 ? 8.127   6.784   -4.269  1.00 31.61  ? 825  LYS   A CA  1 
ATOM   2126 C C   . LYS   A 1 288 ? 9.471   6.372   -4.850  1.00 29.38  ? 825  LYS   A C   1 
ATOM   2127 O O   . LYS   A 1 288 ? 10.516  6.932   -4.481  1.00 29.85  ? 825  LYS   A O   1 
ATOM   2128 C CB  . LYS   A 1 288 ? 7.739   5.857   -3.119  1.00 33.65  ? 825  LYS   A CB  1 
ATOM   2129 C CG  . LYS   A 1 288 ? 6.573   6.342   -2.287  1.00 41.11  ? 825  LYS   A CG  1 
ATOM   2130 C CD  . LYS   A 1 288 ? 6.534   5.617   -0.953  1.00 55.55  ? 825  LYS   A CD  1 
ATOM   2131 C CE  . LYS   A 1 288 ? 7.930   5.589   -0.331  1.00 72.52  ? 825  LYS   A CE  1 
ATOM   2132 N NZ  . LYS   A 1 288 ? 7.902   5.333   1.136   1.00 82.42  ? 825  LYS   A NZ  1 
ATOM   2133 N N   A MET   A 1 289 ? 9.469   5.391   -5.758  0.67 26.30  ? 826  MET   A N   1 
ATOM   2134 N N   B MET   A 1 289 ? 9.468   5.411   -5.772  0.33 26.81  ? 826  MET   A N   1 
ATOM   2135 C CA  A MET   A 1 289 ? 10.712  4.966   -6.404  0.67 25.73  ? 826  MET   A CA  1 
ATOM   2136 C CA  B MET   A 1 289 ? 10.720  4.976   -6.382  0.33 26.12  ? 826  MET   A CA  1 
ATOM   2137 C C   A MET   A 1 289 ? 11.286  6.088   -7.260  0.67 29.13  ? 826  MET   A C   1 
ATOM   2138 C C   B MET   A 1 289 ? 11.296  6.053   -7.296  0.33 27.64  ? 826  MET   A C   1 
ATOM   2139 O O   A MET   A 1 289 ? 12.480  6.417   -7.165  0.67 27.54  ? 826  MET   A O   1 
ATOM   2140 O O   B MET   A 1 289 ? 12.510  6.305   -7.285  0.33 28.50  ? 826  MET   A O   1 
ATOM   2141 C CB  A MET   A 1 289 ? 10.451  3.715   -7.250  0.67 28.92  ? 826  MET   A CB  1 
ATOM   2142 C CB  B MET   A 1 289 ? 10.484  3.676   -7.144  0.33 29.31  ? 826  MET   A CB  1 
ATOM   2143 C CG  A MET   A 1 289 ? 11.684  3.127   -7.927  0.67 34.25  ? 826  MET   A CG  1 
ATOM   2144 C CG  B MET   A 1 289 ? 11.452  3.426   -8.269  0.33 36.30  ? 826  MET   A CG  1 
ATOM   2145 S SD  A MET   A 1 289 ? 12.707  2.238   -6.751  0.67 34.55  ? 826  MET   A SD  1 
ATOM   2146 S SD  B MET   A 1 289 ? 11.766  1.670   -8.382  0.33 40.28  ? 826  MET   A SD  1 
ATOM   2147 C CE  A MET   A 1 289 ? 13.863  1.403   -7.841  0.67 43.80  ? 826  MET   A CE  1 
ATOM   2148 C CE  B MET   A 1 289 ? 12.983  1.503   -7.079  0.33 40.95  ? 826  MET   A CE  1 
ATOM   2149 N N   . ILE   A 1 290 ? 10.441  6.705   -8.085  1.00 25.99  ? 827  ILE   A N   1 
ATOM   2150 C CA  . ILE   A 1 290 ? 10.907  7.780   -8.954  1.00 26.12  ? 827  ILE   A CA  1 
ATOM   2151 C C   . ILE   A 1 290 ? 11.414  8.954   -8.129  1.00 33.29  ? 827  ILE   A C   1 
ATOM   2152 O O   . ILE   A 1 290 ? 12.471  9.525   -8.424  1.00 35.02  ? 827  ILE   A O   1 
ATOM   2153 C CB  . ILE   A 1 290 ? 9.786   8.201   -9.916  1.00 32.95  ? 827  ILE   A CB  1 
ATOM   2154 C CG1 . ILE   A 1 290 ? 9.474   7.061   -10.887 1.00 32.18  ? 827  ILE   A CG1 1 
ATOM   2155 C CG2 . ILE   A 1 290 ? 10.158  9.483   -10.654 1.00 39.46  ? 827  ILE   A CG2 1 
ATOM   2156 C CD1 . ILE   A 1 290 ? 8.160   7.254   -11.624 1.00 38.13  ? 827  ILE   A CD1 1 
ATOM   2157 N N   . ARG   A 1 291 ? 10.679  9.324   -7.080  1.00 27.09  ? 828  ARG   A N   1 
ATOM   2158 C CA  . ARG   A 1 291 ? 11.047  10.487  -6.281  1.00 29.30  ? 828  ARG   A CA  1 
ATOM   2159 C C   . ARG   A 1 291 ? 12.309  10.240  -5.468  1.00 33.99  ? 828  ARG   A C   1 
ATOM   2160 O O   . ARG   A 1 291 ? 13.110  11.164  -5.260  1.00 29.54  ? 828  ARG   A O   1 
ATOM   2161 C CB  . ARG   A 1 291 ? 9.889   10.863  -5.365  1.00 28.33  ? 828  ARG   A CB  1 
ATOM   2162 C CG  . ARG   A 1 291 ? 8.771   11.495  -6.149  1.00 30.97  ? 828  ARG   A CG  1 
ATOM   2163 C CD  . ARG   A 1 291 ? 7.446   11.490  -5.430  1.00 37.34  ? 828  ARG   A CD  1 
ATOM   2164 N NE  . ARG   A 1 291 ? 6.464   12.146  -6.279  1.00 39.56  ? 828  ARG   A NE  1 
ATOM   2165 C CZ  . ARG   A 1 291 ? 5.156   12.118  -6.079  1.00 42.15  ? 828  ARG   A CZ  1 
ATOM   2166 N NH1 . ARG   A 1 291 ? 4.650   11.457  -5.047  1.00 38.41  ? 828  ARG   A NH1 1 
ATOM   2167 N NH2 . ARG   A 1 291 ? 4.359   12.750  -6.928  1.00 38.28  ? 828  ARG   A NH2 1 
ATOM   2168 N N   . HIS   A 1 292 ? 12.494  9.014   -4.975  1.00 29.07  ? 829  HIS   A N   1 
ATOM   2169 C CA  . HIS   A 1 292 ? 13.764  8.685   -4.342  1.00 30.95  ? 829  HIS   A CA  1 
ATOM   2170 C C   . HIS   A 1 292 ? 14.922  8.897   -5.310  1.00 31.50  ? 829  HIS   A C   1 
ATOM   2171 O O   . HIS   A 1 292 ? 15.954  9.466   -4.947  1.00 26.78  ? 829  HIS   A O   1 
ATOM   2172 C CB  . HIS   A 1 292 ? 13.772  7.244   -3.839  1.00 26.08  ? 829  HIS   A CB  1 
ATOM   2173 C CG  . HIS   A 1 292 ? 15.150  6.759   -3.514  1.00 26.84  ? 829  HIS   A CG  1 
ATOM   2174 N ND1 . HIS   A 1 292 ? 15.772  7.040   -2.314  1.00 25.75  ? 829  HIS   A ND1 1 
ATOM   2175 C CD2 . HIS   A 1 292 ? 16.054  6.081   -4.258  1.00 24.74  ? 829  HIS   A CD2 1 
ATOM   2176 C CE1 . HIS   A 1 292 ? 16.991  6.528   -2.324  1.00 27.51  ? 829  HIS   A CE1 1 
ATOM   2177 N NE2 . HIS   A 1 292 ? 17.184  5.935   -3.488  1.00 25.32  ? 829  HIS   A NE2 1 
ATOM   2178 N N   . THR   A 1 293 ? 14.771  8.432   -6.547  1.00 24.83  ? 830  THR   A N   1 
ATOM   2179 C CA  . THR   A 1 293 ? 15.874  8.518   -7.501  1.00 28.44  ? 830  THR   A CA  1 
ATOM   2180 C C   . THR   A 1 293 ? 16.168  9.967   -7.854  1.00 32.22  ? 830  THR   A C   1 
ATOM   2181 O O   . THR   A 1 293 ? 17.337  10.369  -7.932  1.00 27.99  ? 830  THR   A O   1 
ATOM   2182 C CB  . THR   A 1 293 ? 15.547  7.707   -8.756  1.00 29.07  ? 830  THR   A CB  1 
ATOM   2183 O OG1 . THR   A 1 293 ? 15.589  6.306   -8.445  1.00 30.82  ? 830  THR   A OG1 1 
ATOM   2184 C CG2 . THR   A 1 293 ? 16.555  8.017   -9.885  1.00 31.32  ? 830  THR   A CG2 1 
ATOM   2185 N N   . THR   A 1 294 ? 15.113  10.765  -8.052  1.00 32.04  ? 831  THR   A N   1 
ATOM   2186 C CA  . THR   A 1 294 ? 15.280  12.194  -8.294  1.00 32.44  ? 831  THR   A CA  1 
ATOM   2187 C C   . THR   A 1 294 ? 16.054  12.841  -7.165  1.00 34.35  ? 831  THR   A C   1 
ATOM   2188 O O   . THR   A 1 294 ? 17.023  13.571  -7.393  1.00 27.05  ? 831  THR   A O   1 
ATOM   2189 C CB  . THR   A 1 294 ? 13.914  12.868  -8.435  1.00 30.85  ? 831  THR   A CB  1 
ATOM   2190 O OG1 . THR   A 1 294 ? 13.254  12.352  -9.588  1.00 36.65  ? 831  THR   A OG1 1 
ATOM   2191 C CG2 . THR   A 1 294 ? 14.057  14.394  -8.561  1.00 40.43  ? 831  THR   A CG2 1 
ATOM   2192 N N   . ASN   A 1 295 ? 15.638  12.574  -5.930  1.00 28.28  ? 832  ASN   A N   1 
ATOM   2193 C CA  . ASN   A 1 295 ? 16.258  13.247  -4.801  1.00 26.94  ? 832  ASN   A CA  1 
ATOM   2194 C C   . ASN   A 1 295 ? 17.695  12.798  -4.612  1.00 21.65  ? 832  ASN   A C   1 
ATOM   2195 O O   . ASN   A 1 295 ? 18.573  13.622  -4.321  1.00 25.70  ? 832  ASN   A O   1 
ATOM   2196 C CB  . ASN   A 1 295 ? 15.450  13.009  -3.527  1.00 26.97  ? 832  ASN   A CB  1 
ATOM   2197 C CG  . ASN   A 1 295 ? 14.420  14.084  -3.297  1.00 49.07  ? 832  ASN   A CG  1 
ATOM   2198 O OD1 . ASN   A 1 295 ? 14.723  15.274  -3.383  1.00 52.17  ? 832  ASN   A OD1 1 
ATOM   2199 N ND2 . ASN   A 1 295 ? 13.189  13.675  -3.021  1.00 60.00  ? 832  ASN   A ND2 1 
ATOM   2200 N N   . LEU   A 1 296 ? 17.959  11.500  -4.777  1.00 23.67  ? 833  LEU   A N   1 
ATOM   2201 C CA  . LEU   A 1 296 ? 19.318  11.014  -4.568  1.00 24.25  ? 833  LEU   A CA  1 
ATOM   2202 C C   . LEU   A 1 296 ? 20.257  11.526  -5.654  1.00 29.46  ? 833  LEU   A C   1 
ATOM   2203 O O   . LEU   A 1 296 ? 21.401  11.909  -5.364  1.00 25.42  ? 833  LEU   A O   1 
ATOM   2204 C CB  . LEU   A 1 296 ? 19.324  9.479   -4.518  1.00 22.78  ? 833  LEU   A CB  1 
ATOM   2205 C CG  . LEU   A 1 296 ? 20.597  8.856   -3.949  1.00 36.63  ? 833  LEU   A CG  1 
ATOM   2206 C CD1 . LEU   A 1 296 ? 20.798  9.238   -2.495  1.00 30.95  ? 833  LEU   A CD1 1 
ATOM   2207 C CD2 . LEU   A 1 296 ? 20.531  7.339   -4.116  1.00 36.74  ? 833  LEU   A CD2 1 
ATOM   2208 N N   . THR   A 1 297 ? 19.786  11.567  -6.908  1.00 23.11  ? 834  THR   A N   1 
ATOM   2209 C CA  . THR   A 1 297 ? 20.630  12.067  -7.990  1.00 23.39  ? 834  THR   A CA  1 
ATOM   2210 C C   . THR   A 1 297 ? 20.991  13.530  -7.771  1.00 27.42  ? 834  THR   A C   1 
ATOM   2211 O O   . THR   A 1 297 ? 22.156  13.928  -7.914  1.00 23.91  ? 834  THR   A O   1 
ATOM   2212 C CB  . THR   A 1 297 ? 19.926  11.868  -9.333  1.00 26.48  ? 834  THR   A CB  1 
ATOM   2213 O OG1 . THR   A 1 297 ? 19.693  10.462  -9.526  1.00 27.95  ? 834  THR   A OG1 1 
ATOM   2214 C CG2 . THR   A 1 297 ? 20.809  12.375  -10.480 1.00 29.64  ? 834  THR   A CG2 1 
ATOM   2215 N N   . LEU   A 1 298 ? 20.006  14.339  -7.407  1.00 25.59  ? 835  LEU   A N   1 
ATOM   2216 C CA  . LEU   A 1 298 ? 20.259  15.733  -7.074  1.00 24.85  ? 835  LEU   A CA  1 
ATOM   2217 C C   . LEU   A 1 298 ? 21.186  15.873  -5.872  1.00 26.11  ? 835  LEU   A C   1 
ATOM   2218 O O   . LEU   A 1 298 ? 21.988  16.813  -5.819  1.00 25.87  ? 835  LEU   A O   1 
ATOM   2219 C CB  . LEU   A 1 298 ? 18.938  16.443  -6.805  1.00 24.33  ? 835  LEU   A CB  1 
ATOM   2220 C CG  . LEU   A 1 298 ? 18.133  16.861  -8.025  1.00 33.63  ? 835  LEU   A CG  1 
ATOM   2221 C CD1 . LEU   A 1 298 ? 16.784  17.444  -7.599  1.00 33.62  ? 835  LEU   A CD1 1 
ATOM   2222 C CD2 . LEU   A 1 298 ? 18.939  17.898  -8.810  1.00 32.46  ? 835  LEU   A CD2 1 
ATOM   2223 N N   . TRP   A 1 299 ? 21.059  14.986  -4.883  1.00 22.56  ? 836  TRP   A N   1 
ATOM   2224 C CA  . TRP   A 1 299 ? 21.932  15.057  -3.713  1.00 24.53  ? 836  TRP   A CA  1 
ATOM   2225 C C   . TRP   A 1 299 ? 23.389  14.783  -4.077  1.00 25.32  ? 836  TRP   A C   1 
ATOM   2226 O O   . TRP   A 1 299 ? 24.303  15.477  -3.592  1.00 24.85  ? 836  TRP   A O   1 
ATOM   2227 C CB  . TRP   A 1 299 ? 21.463  14.060  -2.662  1.00 26.90  ? 836  TRP   A CB  1 
ATOM   2228 C CG  . TRP   A 1 299 ? 22.284  14.043  -1.401  1.00 24.50  ? 836  TRP   A CG  1 
ATOM   2229 C CD1 . TRP   A 1 299 ? 22.330  15.013  -0.439  1.00 29.13  ? 836  TRP   A CD1 1 
ATOM   2230 C CD2 . TRP   A 1 299 ? 23.126  12.980  -0.940  1.00 28.05  ? 836  TRP   A CD2 1 
ATOM   2231 N NE1 . TRP   A 1 299 ? 23.174  14.626  0.581   1.00 31.72  ? 836  TRP   A NE1 1 
ATOM   2232 C CE2 . TRP   A 1 299 ? 23.667  13.383  0.300   1.00 29.62  ? 836  TRP   A CE2 1 
ATOM   2233 C CE3 . TRP   A 1 299 ? 23.478  11.729  -1.455  1.00 27.96  ? 836  TRP   A CE3 1 
ATOM   2234 C CZ2 . TRP   A 1 299 ? 24.544  12.584  1.025   1.00 24.52  ? 836  TRP   A CZ2 1 
ATOM   2235 C CZ3 . TRP   A 1 299 ? 24.351  10.934  -0.725  1.00 29.77  ? 836  TRP   A CZ3 1 
ATOM   2236 C CH2 . TRP   A 1 299 ? 24.865  11.367  0.503   1.00 24.03  ? 836  TRP   A CH2 1 
ATOM   2237 N N   . PHE   A 1 300 ? 23.634  13.769  -4.911  1.00 23.36  ? 837  PHE   A N   1 
ATOM   2238 C CA  . PHE   A 1 300 ? 25.009  13.547  -5.373  1.00 20.73  ? 837  PHE   A CA  1 
ATOM   2239 C C   . PHE   A 1 300 ? 25.545  14.771  -6.110  1.00 25.03  ? 837  PHE   A C   1 
ATOM   2240 O O   . PHE   A 1 300 ? 26.684  15.198  -5.867  1.00 24.62  ? 837  PHE   A O   1 
ATOM   2241 C CB  . PHE   A 1 300 ? 25.091  12.311  -6.266  1.00 20.05  ? 837  PHE   A CB  1 
ATOM   2242 C CG  . PHE   A 1 300 ? 25.002  11.002  -5.518  1.00 24.78  ? 837  PHE   A CG  1 
ATOM   2243 C CD1 . PHE   A 1 300 ? 25.839  10.725  -4.440  1.00 26.86  ? 837  PHE   A CD1 1 
ATOM   2244 C CD2 . PHE   A 1 300 ? 24.101  10.033  -5.920  1.00 22.05  ? 837  PHE   A CD2 1 
ATOM   2245 C CE1 . PHE   A 1 300 ? 25.756  9.505   -3.779  1.00 26.10  ? 837  PHE   A CE1 1 
ATOM   2246 C CE2 . PHE   A 1 300 ? 24.015  8.820   -5.257  1.00 27.03  ? 837  PHE   A CE2 1 
ATOM   2247 C CZ  . PHE   A 1 300 ? 24.830  8.556   -4.193  1.00 25.29  ? 837  PHE   A CZ  1 
ATOM   2248 N N   . GLU   A 1 301 ? 24.742  15.368  -6.999  1.00 22.16  ? 838  GLU   A N   1 
ATOM   2249 C CA  . GLU   A 1 301 ? 25.185  16.587  -7.684  1.00 22.15  ? 838  GLU   A CA  1 
ATOM   2250 C C   . GLU   A 1 301 ? 25.506  17.695  -6.687  1.00 24.68  ? 838  GLU   A C   1 
ATOM   2251 O O   . GLU   A 1 301 ? 26.522  18.397  -6.817  1.00 25.37  ? 838  GLU   A O   1 
ATOM   2252 C CB  . GLU   A 1 301 ? 24.110  17.088  -8.655  1.00 29.01  ? 838  GLU   A CB  1 
ATOM   2253 C CG  . GLU   A 1 301 ? 23.771  16.144  -9.784  1.00 41.00  ? 838  GLU   A CG  1 
ATOM   2254 C CD  . GLU   A 1 301 ? 22.485  16.531  -10.488 1.00 47.10  ? 838  GLU   A CD  1 
ATOM   2255 O OE1 . GLU   A 1 301 ? 22.228  17.762  -10.636 1.00 29.90  ? 838  GLU   A OE1 1 
ATOM   2256 O OE2 . GLU   A 1 301 ? 21.742  15.595  -10.877 1.00 41.00  ? 838  GLU   A OE2 1 
ATOM   2257 N N   . LYS   A 1 302 ? 24.606  17.906  -5.722  1.00 25.73  ? 839  LYS   A N   1 
ATOM   2258 C CA  . LYS   A 1 302 ? 24.791  18.948  -4.717  1.00 24.04  ? 839  LYS   A CA  1 
ATOM   2259 C C   . LYS   A 1 302 ? 26.081  18.744  -3.942  1.00 27.41  ? 839  LYS   A C   1 
ATOM   2260 O O   . LYS   A 1 302 ? 26.834  19.699  -3.723  1.00 25.59  ? 839  LYS   A O   1 
ATOM   2261 C CB  . LYS   A 1 302 ? 23.598  18.970  -3.760  1.00 28.25  ? 839  LYS   A CB  1 
ATOM   2262 C CG  . LYS   A 1 302 ? 23.612  20.115  -2.723  1.00 26.99  ? 839  LYS   A CG  1 
ATOM   2263 C CD  . LYS   A 1 302 ? 22.412  19.973  -1.803  1.00 24.24  ? 839  LYS   A CD  1 
ATOM   2264 C CE  . LYS   A 1 302 ? 22.461  20.961  -0.634  1.00 28.83  ? 839  LYS   A CE  1 
ATOM   2265 N NZ  . LYS   A 1 302 ? 21.144  20.953  0.055   1.00 37.63  ? 839  LYS   A NZ  1 
ATOM   2266 N N   . CYS   A 1 303 ? 26.353  17.504  -3.518  1.00 22.74  ? 840  CYS   A N   1 
ATOM   2267 C CA  . CYS   A 1 303 ? 27.558  17.232  -2.732  1.00 24.42  ? 840  CYS   A CA  1 
ATOM   2268 C C   . CYS   A 1 303 ? 28.810  17.641  -3.486  1.00 27.08  ? 840  CYS   A C   1 
ATOM   2269 O O   . CYS   A 1 303 ? 29.751  18.191  -2.896  1.00 25.95  ? 840  CYS   A O   1 
ATOM   2270 C CB  . CYS   A 1 303 ? 27.633  15.749  -2.368  1.00 26.86  ? 840  CYS   A CB  1 
ATOM   2271 S SG  . CYS   A 1 303 ? 26.388  15.255  -1.127  1.00 29.58  ? 840  CYS   A SG  1 
ATOM   2272 N N   . ILE   A 1 304 ? 28.833  17.382  -4.791  1.00 24.15  ? 841  ILE   A N   1 
ATOM   2273 C CA  . ILE   A 1 304 ? 30.001  17.708  -5.606  1.00 20.51  ? 841  ILE   A CA  1 
ATOM   2274 C C   . ILE   A 1 304 ? 30.145  19.218  -5.773  1.00 25.70  ? 841  ILE   A C   1 
ATOM   2275 O O   . ILE   A 1 304 ? 31.207  19.794  -5.508  1.00 28.38  ? 841  ILE   A O   1 
ATOM   2276 C CB  . ILE   A 1 304 ? 29.904  17.015  -6.975  1.00 22.90  ? 841  ILE   A CB  1 
ATOM   2277 C CG1 . ILE   A 1 304 ? 29.971  15.494  -6.816  1.00 20.97  ? 841  ILE   A CG1 1 
ATOM   2278 C CG2 . ILE   A 1 304 ? 31.018  17.504  -7.894  1.00 24.75  ? 841  ILE   A CG2 1 
ATOM   2279 C CD1 . ILE   A 1 304 ? 29.655  14.718  -8.088  1.00 24.43  ? 841  ILE   A CD1 1 
ATOM   2280 N N   A VAL   A 1 305 ? 29.071  19.875  -6.219  0.59 24.73  ? 842  VAL   A N   1 
ATOM   2281 N N   B VAL   A 1 305 ? 29.098  19.891  -6.251  0.41 25.34  ? 842  VAL   A N   1 
ATOM   2282 C CA  A VAL   A 1 305 ? 29.160  21.269  -6.642  0.59 26.62  ? 842  VAL   A CA  1 
ATOM   2283 C CA  B VAL   A 1 305 ? 29.317  21.288  -6.625  0.41 25.20  ? 842  VAL   A CA  1 
ATOM   2284 C C   A VAL   A 1 305 ? 29.279  22.211  -5.447  0.59 27.57  ? 842  VAL   A C   1 
ATOM   2285 C C   B VAL   A 1 305 ? 29.394  22.193  -5.400  0.41 27.89  ? 842  VAL   A C   1 
ATOM   2286 O O   A VAL   A 1 305 ? 29.874  23.294  -5.555  0.59 30.35  ? 842  VAL   A O   1 
ATOM   2287 O O   B VAL   A 1 305 ? 30.040  23.249  -5.448  0.41 27.67  ? 842  VAL   A O   1 
ATOM   2288 C CB  A VAL   A 1 305 ? 27.938  21.588  -7.525  0.59 30.53  ? 842  VAL   A CB  1 
ATOM   2289 C CB  B VAL   A 1 305 ? 28.232  21.772  -7.599  0.41 28.06  ? 842  VAL   A CB  1 
ATOM   2290 C CG1 A VAL   A 1 305 ? 27.886  23.042  -7.894  0.59 26.46  ? 842  VAL   A CG1 1 
ATOM   2291 C CG1 B VAL   A 1 305 ? 28.242  20.920  -8.858  0.41 28.53  ? 842  VAL   A CG1 1 
ATOM   2292 C CG2 A VAL   A 1 305 ? 27.982  20.726  -8.775  0.59 30.89  ? 842  VAL   A CG2 1 
ATOM   2293 C CG2 B VAL   A 1 305 ? 26.900  21.714  -6.925  0.41 27.11  ? 842  VAL   A CG2 1 
ATOM   2294 N N   . GLU   A 1 306 ? 28.752  21.819  -4.291  1.00 26.38  ? 843  GLU   A N   1 
ATOM   2295 C CA  . GLU   A 1 306 ? 28.873  22.651  -3.098  1.00 29.88  ? 843  GLU   A CA  1 
ATOM   2296 C C   . GLU   A 1 306 ? 30.189  22.439  -2.365  1.00 33.05  ? 843  GLU   A C   1 
ATOM   2297 O O   . GLU   A 1 306 ? 30.467  23.150  -1.392  1.00 32.43  ? 843  GLU   A O   1 
ATOM   2298 C CB  . GLU   A 1 306 ? 27.723  22.402  -2.139  1.00 29.87  ? 843  GLU   A CB  1 
ATOM   2299 C CG  . GLU   A 1 306 ? 26.389  22.910  -2.664  1.00 30.86  ? 843  GLU   A CG  1 
ATOM   2300 C CD  . GLU   A 1 306 ? 25.330  22.948  -1.588  1.00 36.96  ? 843  GLU   A CD  1 
ATOM   2301 O OE1 . GLU   A 1 306 ? 25.447  22.193  -0.602  1.00 35.65  ? 843  GLU   A OE1 1 
ATOM   2302 O OE2 . GLU   A 1 306 ? 24.390  23.746  -1.730  1.00 37.14  ? 843  GLU   A OE2 1 
ATOM   2303 N N   . ALA   A 1 307 ? 30.990  21.478  -2.790  1.00 27.02  ? 844  ALA   A N   1 
ATOM   2304 C CA  . ALA   A 1 307 ? 32.341  21.334  -2.253  1.00 24.87  ? 844  ALA   A CA  1 
ATOM   2305 C C   . ALA   A 1 307 ? 33.208  22.353  -2.974  1.00 25.80  ? 844  ALA   A C   1 
ATOM   2306 O O   . ALA   A 1 307 ? 33.751  22.081  -4.045  1.00 30.97  ? 844  ALA   A O   1 
ATOM   2307 C CB  . ALA   A 1 307 ? 32.852  19.909  -2.450  1.00 27.38  ? 844  ALA   A CB  1 
ATOM   2308 N N   . GLU   A 1 308 ? 33.329  23.560  -2.387  1.00 27.68  ? 845  GLU   A N   1 
ATOM   2309 C CA  . GLU   A 1 308 ? 33.995  24.648  -3.090  1.00 25.14  ? 845  GLU   A CA  1 
ATOM   2310 C C   . GLU   A 1 308 ? 35.510  24.477  -3.079  1.00 27.33  ? 845  GLU   A C   1 
ATOM   2311 O O   . GLU   A 1 308 ? 36.179  24.780  -4.072  1.00 27.32  ? 845  GLU   A O   1 
ATOM   2312 C CB  . GLU   A 1 308 ? 33.591  26.002  -2.478  1.00 28.37  ? 845  GLU   A CB  1 
ATOM   2313 C CG  . GLU   A 1 308 ? 32.099  26.264  -2.632  1.00 28.48  ? 845  GLU   A CG  1 
ATOM   2314 C CD  . GLU   A 1 308 ? 31.660  27.575  -2.023  1.00 46.27  ? 845  GLU   A CD  1 
ATOM   2315 O OE1 . GLU   A 1 308 ? 32.544  28.343  -1.602  1.00 43.81  ? 845  GLU   A OE1 1 
ATOM   2316 O OE2 . GLU   A 1 308 ? 30.436  27.828  -1.963  1.00 42.39  ? 845  GLU   A OE2 1 
ATOM   2317 N N   . ASN   A 1 309 ? 36.058  24.004  -1.964  1.00 29.97  ? 846  ASN   A N   1 
ATOM   2318 C CA  . ASN   A 1 309 ? 37.480  23.703  -1.898  1.00 28.53  ? 846  ASN   A CA  1 
ATOM   2319 C C   . ASN   A 1 309 ? 37.814  22.598  -2.898  1.00 28.47  ? 846  ASN   A C   1 
ATOM   2320 O O   . ASN   A 1 309 ? 37.184  21.533  -2.904  1.00 29.40  ? 846  ASN   A O   1 
ATOM   2321 C CB  . ASN   A 1 309 ? 37.854  23.295  -0.467  1.00 29.68  ? 846  ASN   A CB  1 
ATOM   2322 C CG  . ASN   A 1 309 ? 39.314  22.874  -0.331  1.00 29.20  ? 846  ASN   A CG  1 
ATOM   2323 O OD1 . ASN   A 1 309 ? 39.633  21.704  -0.455  1.00 27.30  ? 846  ASN   A OD1 1 
ATOM   2324 N ND2 . ASN   A 1 309 ? 40.200  23.836  -0.064  1.00 27.82  ? 846  ASN   A ND2 1 
ATOM   2325 N N   . PHE   A 1 310 ? 38.797  22.873  -3.761  1.00 29.51  ? 847  PHE   A N   1 
ATOM   2326 C CA  . PHE   A 1 310 ? 39.132  21.965  -4.853  1.00 31.29  ? 847  PHE   A CA  1 
ATOM   2327 C C   . PHE   A 1 310 ? 39.461  20.561  -4.350  1.00 28.12  ? 847  PHE   A C   1 
ATOM   2328 O O   . PHE   A 1 310 ? 38.951  19.565  -4.877  1.00 25.97  ? 847  PHE   A O   1 
ATOM   2329 C CB  . PHE   A 1 310 ? 40.304  22.543  -5.644  1.00 29.66  ? 847  PHE   A CB  1 
ATOM   2330 C CG  . PHE   A 1 310 ? 40.687  21.726  -6.836  1.00 31.32  ? 847  PHE   A CG  1 
ATOM   2331 C CD1 . PHE   A 1 310 ? 39.711  21.209  -7.671  1.00 32.09  ? 847  PHE   A CD1 1 
ATOM   2332 C CD2 . PHE   A 1 310 ? 42.010  21.485  -7.135  1.00 37.97  ? 847  PHE   A CD2 1 
ATOM   2333 C CE1 . PHE   A 1 310 ? 40.055  20.451  -8.774  1.00 29.08  ? 847  PHE   A CE1 1 
ATOM   2334 C CE2 . PHE   A 1 310 ? 42.356  20.722  -8.237  1.00 46.24  ? 847  PHE   A CE2 1 
ATOM   2335 C CZ  . PHE   A 1 310 ? 41.367  20.202  -9.052  1.00 32.05  ? 847  PHE   A CZ  1 
ATOM   2336 N N   . GLU   A 1 311 ? 40.354  20.456  -3.361  1.00 27.39  ? 848  GLU   A N   1 
ATOM   2337 C CA  . GLU   A 1 311 ? 40.786  19.136  -2.912  1.00 25.61  ? 848  GLU   A CA  1 
ATOM   2338 C C   . GLU   A 1 311 ? 39.642  18.388  -2.247  1.00 27.61  ? 848  GLU   A C   1 
ATOM   2339 O O   . GLU   A 1 311 ? 39.524  17.163  -2.381  1.00 27.73  ? 848  GLU   A O   1 
ATOM   2340 C CB  . GLU   A 1 311 ? 41.973  19.260  -1.955  1.00 28.09  ? 848  GLU   A CB  1 
ATOM   2341 C CG  . GLU   A 1 311 ? 43.262  19.722  -2.636  1.00 30.48  ? 848  GLU   A CG  1 
ATOM   2342 C CD  . GLU   A 1 311 ? 43.224  21.190  -3.064  1.00 31.34  ? 848  GLU   A CD  1 
ATOM   2343 O OE1 . GLU   A 1 311 ? 42.535  22.016  -2.423  1.00 29.66  ? 848  GLU   A OE1 1 
ATOM   2344 O OE2 . GLU   A 1 311 ? 43.904  21.531  -4.047  1.00 34.76  ? 848  GLU   A OE2 1 
ATOM   2345 N N   . GLU   A 1 312 ? 38.795  19.112  -1.525  1.00 28.81  ? 849  GLU   A N   1 
ATOM   2346 C CA  . GLU   A 1 312 ? 37.613  18.498  -0.931  1.00 29.57  ? 849  GLU   A CA  1 
ATOM   2347 C C   . GLU   A 1 312 ? 36.665  17.968  -2.008  1.00 29.92  ? 849  GLU   A C   1 
ATOM   2348 O O   . GLU   A 1 312 ? 36.124  16.860  -1.884  1.00 28.69  ? 849  GLU   A O   1 
ATOM   2349 C CB  . GLU   A 1 312 ? 36.931  19.526  -0.036  1.00 28.54  ? 849  GLU   A CB  1 
ATOM   2350 C CG  . GLU   A 1 312 ? 35.720  19.051  0.712   1.00 33.16  ? 849  GLU   A CG  1 
ATOM   2351 C CD  . GLU   A 1 312 ? 35.201  20.148  1.613   1.00 58.52  ? 849  GLU   A CD  1 
ATOM   2352 O OE1 . GLU   A 1 312 ? 35.943  20.553  2.533   1.00 58.90  ? 849  GLU   A OE1 1 
ATOM   2353 O OE2 . GLU   A 1 312 ? 34.075  20.630  1.366   1.00 73.73  ? 849  GLU   A OE2 1 
ATOM   2354 N N   . ARG   A 1 313 ? 36.497  18.721  -3.100  1.00 25.54  ? 850  ARG   A N   1 
ATOM   2355 C CA  . ARG   A 1 313 ? 35.592  18.293  -4.166  1.00 25.73  ? 850  ARG   A CA  1 
ATOM   2356 C C   . ARG   A 1 313 ? 36.120  17.056  -4.881  1.00 27.61  ? 850  ARG   A C   1 
ATOM   2357 O O   . ARG   A 1 313 ? 35.352  16.142  -5.206  1.00 25.65  ? 850  ARG   A O   1 
ATOM   2358 C CB  . ARG   A 1 313 ? 35.374  19.439  -5.154  1.00 26.30  ? 850  ARG   A CB  1 
ATOM   2359 C CG  . ARG   A 1 313 ? 34.363  19.139  -6.265  1.00 26.16  ? 850  ARG   A CG  1 
ATOM   2360 C CD  . ARG   A 1 313 ? 33.968  20.408  -6.989  1.00 25.21  ? 850  ARG   A CD  1 
ATOM   2361 N NE  . ARG   A 1 313 ? 35.069  20.996  -7.750  1.00 26.23  ? 850  ARG   A NE  1 
ATOM   2362 C CZ  . ARG   A 1 313 ? 35.730  22.103  -7.401  1.00 32.51  ? 850  ARG   A CZ  1 
ATOM   2363 N NH1 . ARG   A 1 313 ? 35.420  22.745  -6.277  1.00 30.37  ? 850  ARG   A NH1 1 
ATOM   2364 N NH2 . ARG   A 1 313 ? 36.702  22.571  -8.182  1.00 29.46  ? 850  ARG   A NH2 1 
ATOM   2365 N N   . VAL   A 1 314 ? 37.428  16.985  -5.112  1.00 23.83  ? 851  VAL   A N   1 
ATOM   2366 C CA  . VAL   A 1 314 ? 37.992  15.774  -5.705  1.00 23.29  ? 851  VAL   A CA  1 
ATOM   2367 C C   . VAL   A 1 314 ? 37.783  14.590  -4.777  1.00 29.87  ? 851  VAL   A C   1 
ATOM   2368 O O   . VAL   A 1 314 ? 37.511  13.471  -5.227  1.00 25.90  ? 851  VAL   A O   1 
ATOM   2369 C CB  . VAL   A 1 314 ? 39.485  15.972  -6.040  1.00 23.55  ? 851  VAL   A CB  1 
ATOM   2370 C CG1 . VAL   A 1 314 ? 40.127  14.656  -6.516  1.00 25.05  ? 851  VAL   A CG1 1 
ATOM   2371 C CG2 . VAL   A 1 314 ? 39.657  17.075  -7.094  1.00 28.13  ? 851  VAL   A CG2 1 
ATOM   2372 N N   . ALA   A 1 315 ? 37.903  14.811  -3.467  1.00 23.18  ? 852  ALA   A N   1 
ATOM   2373 C CA  . ALA   A 1 315 ? 37.676  13.708  -2.539  1.00 25.81  ? 852  ALA   A CA  1 
ATOM   2374 C C   . ALA   A 1 315 ? 36.200  13.322  -2.502  1.00 27.37  ? 852  ALA   A C   1 
ATOM   2375 O O   . ALA   A 1 315 ? 35.870  12.135  -2.364  1.00 26.75  ? 852  ALA   A O   1 
ATOM   2376 C CB  . ALA   A 1 315 ? 38.174  14.078  -1.143  1.00 27.80  ? 852  ALA   A CB  1 
ATOM   2377 N N   . VAL   A 1 316 ? 35.306  14.301  -2.654  1.00 22.60  ? 853  VAL   A N   1 
ATOM   2378 C CA  . VAL   A 1 316 ? 33.877  13.998  -2.701  1.00 24.46  ? 853  VAL   A CA  1 
ATOM   2379 C C   . VAL   A 1 316 ? 33.562  13.156  -3.925  1.00 25.71  ? 853  VAL   A C   1 
ATOM   2380 O O   . VAL   A 1 316 ? 32.903  12.115  -3.830  1.00 25.88  ? 853  VAL   A O   1 
ATOM   2381 C CB  . VAL   A 1 316 ? 33.041  15.284  -2.696  1.00 20.84  ? 853  VAL   A CB  1 
ATOM   2382 C CG1 . VAL   A 1 316 ? 31.586  14.941  -3.098  1.00 23.45  ? 853  VAL   A CG1 1 
ATOM   2383 C CG2 . VAL   A 1 316 ? 33.068  15.954  -1.319  1.00 25.54  ? 853  VAL   A CG2 1 
ATOM   2384 N N   . LEU   A 1 317 ? 34.036  13.590  -5.100  1.00 23.74  ? 854  LEU   A N   1 
ATOM   2385 C CA  . LEU   A 1 317 ? 33.810  12.798  -6.309  1.00 25.31  ? 854  LEU   A CA  1 
ATOM   2386 C C   . LEU   A 1 317 ? 34.414  11.402  -6.174  1.00 25.77  ? 854  LEU   A C   1 
ATOM   2387 O O   . LEU   A 1 317 ? 33.785  10.404  -6.557  1.00 25.49  ? 854  LEU   A O   1 
ATOM   2388 C CB  . LEU   A 1 317 ? 34.381  13.520  -7.532  1.00 25.22  ? 854  LEU   A CB  1 
ATOM   2389 C CG  . LEU   A 1 317 ? 34.224  12.791  -8.876  1.00 27.08  ? 854  LEU   A CG  1 
ATOM   2390 C CD1 . LEU   A 1 317 ? 32.753  12.416  -9.137  1.00 30.72  ? 854  LEU   A CD1 1 
ATOM   2391 C CD2 . LEU   A 1 317 ? 34.770  13.645  -10.024 1.00 24.37  ? 854  LEU   A CD2 1 
ATOM   2392 N N   . SER   A 1 318 ? 35.625  11.300  -5.605  1.00 23.15  ? 855  SER   A N   1 
ATOM   2393 C CA  . SER   A 1 318 ? 36.242  9.978   -5.449  1.00 21.52  ? 855  SER   A CA  1 
ATOM   2394 C C   . SER   A 1 318 ? 35.411  9.079   -4.540  1.00 24.76  ? 855  SER   A C   1 
ATOM   2395 O O   . SER   A 1 318 ? 35.261  7.880   -4.809  1.00 25.27  ? 855  SER   A O   1 
ATOM   2396 C CB  . SER   A 1 318 ? 37.663  10.119  -4.903  1.00 26.20  ? 855  SER   A CB  1 
ATOM   2397 O OG  . SER   A 1 318 ? 38.432  10.990  -5.723  1.00 31.64  ? 855  SER   A OG  1 
ATOM   2398 N N   . ARG   A 1 319 ? 34.853  9.643   -3.466  1.00 25.67  ? 856  ARG   A N   1 
ATOM   2399 C CA  . ARG   A 1 319 ? 34.010  8.862   -2.555  1.00 22.91  ? 856  ARG   A CA  1 
ATOM   2400 C C   . ARG   A 1 319 ? 32.765  8.356   -3.263  1.00 25.51  ? 856  ARG   A C   1 
ATOM   2401 O O   . ARG   A 1 319 ? 32.337  7.209   -3.051  1.00 22.71  ? 856  ARG   A O   1 
ATOM   2402 C CB  . ARG   A 1 319 ? 33.602  9.728   -1.359  1.00 24.77  ? 856  ARG   A CB  1 
ATOM   2403 C CG  . ARG   A 1 319 ? 33.097  8.963   -0.153  1.00 23.00  ? 856  ARG   A CG  1 
ATOM   2404 C CD  . ARG   A 1 319 ? 34.227  8.169   0.524   1.00 23.72  ? 856  ARG   A CD  1 
ATOM   2405 N NE  . ARG   A 1 319 ? 35.303  9.053   0.967   1.00 25.97  ? 856  ARG   A NE  1 
ATOM   2406 C CZ  . ARG   A 1 319 ? 35.376  9.619   2.172   1.00 32.95  ? 856  ARG   A CZ  1 
ATOM   2407 N NH1 . ARG   A 1 319 ? 34.438  9.405   3.094   1.00 25.19  ? 856  ARG   A NH1 1 
ATOM   2408 N NH2 . ARG   A 1 319 ? 36.403  10.413  2.460   1.00 28.63  ? 856  ARG   A NH2 1 
ATOM   2409 N N   . ILE   A 1 320 ? 32.162  9.207   -4.094  1.00 25.97  ? 857  ILE   A N   1 
ATOM   2410 C CA  . ILE   A 1 320 ? 30.966  8.818   -4.839  1.00 26.73  ? 857  ILE   A CA  1 
ATOM   2411 C C   . ILE   A 1 320 ? 31.298  7.691   -5.810  1.00 27.98  ? 857  ILE   A C   1 
ATOM   2412 O O   . ILE   A 1 320 ? 30.513  6.760   -6.004  1.00 24.30  ? 857  ILE   A O   1 
ATOM   2413 C CB  . ILE   A 1 320 ? 30.379  10.060  -5.545  1.00 23.30  ? 857  ILE   A CB  1 
ATOM   2414 C CG1 . ILE   A 1 320 ? 29.809  11.028  -4.510  1.00 23.83  ? 857  ILE   A CG1 1 
ATOM   2415 C CG2 . ILE   A 1 320 ? 29.314  9.675   -6.560  1.00 22.29  ? 857  ILE   A CG2 1 
ATOM   2416 C CD1 . ILE   A 1 320 ? 29.353  12.355  -5.092  1.00 21.59  ? 857  ILE   A CD1 1 
ATOM   2417 N N   . ILE   A 1 321 ? 32.487  7.732   -6.404  1.00 22.36  ? 858  ILE   A N   1 
ATOM   2418 C CA  . ILE   A 1 321 ? 32.903  6.625   -7.258  1.00 21.44  ? 858  ILE   A CA  1 
ATOM   2419 C C   . ILE   A 1 321 ? 33.066  5.345   -6.438  1.00 23.86  ? 858  ILE   A C   1 
ATOM   2420 O O   . ILE   A 1 321 ? 32.765  4.244   -6.921  1.00 27.53  ? 858  ILE   A O   1 
ATOM   2421 C CB  . ILE   A 1 321 ? 34.194  7.005   -8.012  1.00 21.17  ? 858  ILE   A CB  1 
ATOM   2422 C CG1 . ILE   A 1 321 ? 33.902  8.126   -9.023  1.00 23.01  ? 858  ILE   A CG1 1 
ATOM   2423 C CG2 . ILE   A 1 321 ? 34.829  5.771   -8.680  1.00 24.17  ? 858  ILE   A CG2 1 
ATOM   2424 C CD1 . ILE   A 1 321 ? 35.183  8.906   -9.462  1.00 27.67  ? 858  ILE   A CD1 1 
ATOM   2425 N N   . GLU   A 1 322 ? 33.550  5.455   -5.193  1.00 23.38  ? 859  GLU   A N   1 
ATOM   2426 C CA  . GLU   A 1 322 ? 33.658  4.259   -4.348  1.00 24.77  ? 859  GLU   A CA  1 
ATOM   2427 C C   . GLU   A 1 322 ? 32.284  3.700   -3.997  1.00 27.31  ? 859  GLU   A C   1 
ATOM   2428 O O   . GLU   A 1 322 ? 32.085  2.475   -3.994  1.00 26.06  ? 859  GLU   A O   1 
ATOM   2429 C CB  . GLU   A 1 322 ? 34.438  4.576   -3.073  1.00 26.95  ? 859  GLU   A CB  1 
ATOM   2430 C CG  . GLU   A 1 322 ? 35.914  4.858   -3.331  1.00 32.19  ? 859  GLU   A CG  1 
ATOM   2431 C CD  . GLU   A 1 322 ? 36.673  5.278   -2.088  1.00 37.71  ? 859  GLU   A CD  1 
ATOM   2432 O OE1 . GLU   A 1 322 ? 36.044  5.507   -1.039  1.00 32.81  ? 859  GLU   A OE1 1 
ATOM   2433 O OE2 . GLU   A 1 322 ? 37.910  5.389   -2.166  1.00 37.32  ? 859  GLU   A OE2 1 
ATOM   2434 N N   . ILE   A 1 323 ? 31.332  4.580   -3.677  1.00 25.99  ? 860  ILE   A N   1 
ATOM   2435 C CA  . ILE   A 1 323 ? 29.953  4.147   -3.463  1.00 23.46  ? 860  ILE   A CA  1 
ATOM   2436 C C   . ILE   A 1 323 ? 29.424  3.446   -4.703  1.00 27.84  ? 860  ILE   A C   1 
ATOM   2437 O O   . ILE   A 1 323 ? 28.774  2.398   -4.613  1.00 25.16  ? 860  ILE   A O   1 
ATOM   2438 C CB  . ILE   A 1 323 ? 29.090  5.362   -3.070  1.00 23.61  ? 860  ILE   A CB  1 
ATOM   2439 C CG1 . ILE   A 1 323 ? 29.506  5.866   -1.680  1.00 23.26  ? 860  ILE   A CG1 1 
ATOM   2440 C CG2 . ILE   A 1 323 ? 27.588  5.019   -3.078  1.00 25.60  ? 860  ILE   A CG2 1 
ATOM   2441 C CD1 . ILE   A 1 323 ? 29.020  7.305   -1.382  1.00 22.77  ? 860  ILE   A CD1 1 
ATOM   2442 N N   . LEU   A 1 324 ? 29.713  3.997   -5.884  1.00 25.94  ? 861  LEU   A N   1 
ATOM   2443 C CA  . LEU   A 1 324 ? 29.334  3.330   -7.127  1.00 26.96  ? 861  LEU   A CA  1 
ATOM   2444 C C   . LEU   A 1 324 ? 29.910  1.926   -7.204  1.00 28.56  ? 861  LEU   A C   1 
ATOM   2445 O O   . LEU   A 1 324 ? 29.211  0.984   -7.588  1.00 26.60  ? 861  LEU   A O   1 
ATOM   2446 C CB  . LEU   A 1 324 ? 29.788  4.155   -8.338  1.00 31.11  ? 861  LEU   A CB  1 
ATOM   2447 C CG  . LEU   A 1 324 ? 29.401  3.596   -9.722  1.00 28.16  ? 861  LEU   A CG  1 
ATOM   2448 C CD1 . LEU   A 1 324 ? 29.281  4.717   -10.727 1.00 29.36  ? 861  LEU   A CD1 1 
ATOM   2449 C CD2 . LEU   A 1 324 ? 30.393  2.558   -10.249 1.00 29.06  ? 861  LEU   A CD2 1 
ATOM   2450 N N   . GLN   A 1 325 ? 31.200  1.772   -6.882  1.00 24.22  ? 862  GLN   A N   1 
ATOM   2451 C CA  . GLN   A 1 325 ? 31.800  0.442   -6.916  1.00 26.41  ? 862  GLN   A CA  1 
ATOM   2452 C C   . GLN   A 1 325 ? 31.044  -0.533  -6.033  1.00 28.29  ? 862  GLN   A C   1 
ATOM   2453 O O   . GLN   A 1 325 ? 30.826  -1.691  -6.412  1.00 26.85  ? 862  GLN   A O   1 
ATOM   2454 C CB  . GLN   A 1 325 ? 33.246  0.502   -6.458  1.00 30.67  ? 862  GLN   A CB  1 
ATOM   2455 C CG  . GLN   A 1 325 ? 34.139  1.225   -7.372  1.00 46.10  ? 862  GLN   A CG  1 
ATOM   2456 C CD  . GLN   A 1 325 ? 35.564  1.151   -6.903  1.00 61.39  ? 862  GLN   A CD  1 
ATOM   2457 O OE1 . GLN   A 1 325 ? 36.051  2.059   -6.230  1.00 52.78  ? 862  GLN   A OE1 1 
ATOM   2458 N NE2 . GLN   A 1 325 ? 36.243  0.056   -7.239  1.00 63.70  ? 862  GLN   A NE2 1 
ATOM   2459 N N   . VAL   A 1 326 ? 30.667  -0.097  -4.835  1.00 24.21  ? 863  VAL   A N   1 
ATOM   2460 C CA  . VAL   A 1 326 ? 29.974  -1.008  -3.930  1.00 29.94  ? 863  VAL   A CA  1 
ATOM   2461 C C   . VAL   A 1 326 ? 28.570  -1.303  -4.454  1.00 25.30  ? 863  VAL   A C   1 
ATOM   2462 O O   . VAL   A 1 326 ? 28.102  -2.451  -4.385  1.00 27.91  ? 863  VAL   A O   1 
ATOM   2463 C CB  . VAL   A 1 326 ? 29.961  -0.436  -2.499  1.00 27.10  ? 863  VAL   A CB  1 
ATOM   2464 C CG1 . VAL   A 1 326 ? 29.192  -1.360  -1.568  1.00 28.91  ? 863  VAL   A CG1 1 
ATOM   2465 C CG2 . VAL   A 1 326 ? 31.417  -0.293  -1.981  1.00 28.98  ? 863  VAL   A CG2 1 
ATOM   2466 N N   . PHE   A 1 327 ? 27.881  -0.287  -4.997  1.00 25.77  ? 864  PHE   A N   1 
ATOM   2467 C CA  . PHE   A 1 327 ? 26.633  -0.563  -5.715  1.00 24.72  ? 864  PHE   A CA  1 
ATOM   2468 C C   . PHE   A 1 327 ? 26.842  -1.685  -6.725  1.00 29.61  ? 864  PHE   A C   1 
ATOM   2469 O O   . PHE   A 1 327 ? 26.049  -2.633  -6.795  1.00 28.35  ? 864  PHE   A O   1 
ATOM   2470 C CB  . PHE   A 1 327 ? 26.130  0.684   -6.449  1.00 19.81  ? 864  PHE   A CB  1 
ATOM   2471 C CG  . PHE   A 1 327 ? 25.347  1.661   -5.592  1.00 24.41  ? 864  PHE   A CG  1 
ATOM   2472 C CD1 . PHE   A 1 327 ? 24.634  1.243   -4.475  1.00 25.35  ? 864  PHE   A CD1 1 
ATOM   2473 C CD2 . PHE   A 1 327 ? 25.313  3.011   -5.940  1.00 23.95  ? 864  PHE   A CD2 1 
ATOM   2474 C CE1 . PHE   A 1 327 ? 23.897  2.150   -3.723  1.00 23.09  ? 864  PHE   A CE1 1 
ATOM   2475 C CE2 . PHE   A 1 327 ? 24.584  3.936   -5.201  1.00 25.08  ? 864  PHE   A CE2 1 
ATOM   2476 C CZ  . PHE   A 1 327 ? 23.861  3.505   -4.085  1.00 25.91  ? 864  PHE   A CZ  1 
ATOM   2477 N N   . GLN   A 1 328 ? 27.909  -1.593  -7.523  1.00 28.24  ? 865  GLN   A N   1 
ATOM   2478 C CA  . GLN   A 1 328 ? 28.170  -2.628  -8.525  1.00 31.93  ? 865  GLN   A CA  1 
ATOM   2479 C C   . GLN   A 1 328 ? 28.395  -3.978  -7.879  1.00 32.76  ? 865  GLN   A C   1 
ATOM   2480 O O   . GLN   A 1 328 ? 27.878  -4.999  -8.351  1.00 30.90  ? 865  GLN   A O   1 
ATOM   2481 C CB  . GLN   A 1 328 ? 29.385  -2.268  -9.376  1.00 32.17  ? 865  GLN   A CB  1 
ATOM   2482 C CG  . GLN   A 1 328 ? 29.086  -1.316  -10.484 1.00 54.18  ? 865  GLN   A CG  1 
ATOM   2483 C CD  . GLN   A 1 328 ? 29.401  -1.904  -11.826 1.00 57.14  ? 865  GLN   A CD  1 
ATOM   2484 O OE1 . GLN   A 1 328 ? 29.115  -3.068  -12.090 1.00 68.07  ? 865  GLN   A OE1 1 
ATOM   2485 N NE2 . GLN   A 1 328 ? 30.009  -1.109  -12.682 1.00 48.30  ? 865  GLN   A NE2 1 
ATOM   2486 N N   . ASP   A 1 329 ? 29.233  -4.016  -6.840  1.00 28.03  ? 866  ASP   A N   1 
ATOM   2487 C CA  . ASP   A 1 329 ? 29.467  -5.276  -6.142  1.00 28.04  ? 866  ASP   A CA  1 
ATOM   2488 C C   . ASP   A 1 329 ? 28.165  -5.893  -5.655  1.00 27.73  ? 866  ASP   A C   1 
ATOM   2489 O O   . ASP   A 1 329 ? 28.061  -7.123  -5.578  1.00 31.10  ? 866  ASP   A O   1 
ATOM   2490 C CB  . ASP   A 1 329 ? 30.409  -5.073  -4.958  1.00 33.26  ? 866  ASP   A CB  1 
ATOM   2491 C CG  . ASP   A 1 329 ? 31.794  -4.610  -5.382  1.00 54.19  ? 866  ASP   A CG  1 
ATOM   2492 O OD1 . ASP   A 1 329 ? 32.186  -4.842  -6.548  1.00 54.84  ? 866  ASP   A OD1 1 
ATOM   2493 O OD2 . ASP   A 1 329 ? 32.494  -4.017  -4.533  1.00 64.09  ? 866  ASP   A OD2 1 
ATOM   2494 N N   . LEU   A 1 330 ? 27.184  -5.071  -5.296  1.00 29.94  ? 867  LEU   A N   1 
ATOM   2495 C CA  . LEU   A 1 330 ? 25.895  -5.535  -4.794  1.00 37.23  ? 867  LEU   A CA  1 
ATOM   2496 C C   . LEU   A 1 330 ? 24.881  -5.774  -5.901  1.00 36.96  ? 867  LEU   A C   1 
ATOM   2497 O O   . LEU   A 1 330 ? 23.719  -6.090  -5.603  1.00 33.12  ? 867  LEU   A O   1 
ATOM   2498 C CB  . LEU   A 1 330 ? 25.318  -4.512  -3.799  1.00 31.75  ? 867  LEU   A CB  1 
ATOM   2499 C CG  . LEU   A 1 330 ? 26.047  -4.435  -2.456  1.00 27.48  ? 867  LEU   A CG  1 
ATOM   2500 C CD1 . LEU   A 1 330 ? 25.576  -3.220  -1.662  1.00 28.62  ? 867  LEU   A CD1 1 
ATOM   2501 C CD2 . LEU   A 1 330 ? 25.853  -5.721  -1.656  1.00 28.46  ? 867  LEU   A CD2 1 
ATOM   2502 N N   . ASN   A 1 331 ? 25.282  -5.617  -7.162  1.00 29.44  ? 868  ASN   A N   1 
ATOM   2503 C CA  . ASN   A 1 331 ? 24.354  -5.695  -8.286  1.00 29.83  ? 868  ASN   A CA  1 
ATOM   2504 C C   . ASN   A 1 331 ? 23.197  -4.715  -8.143  1.00 30.14  ? 868  ASN   A C   1 
ATOM   2505 O O   . ASN   A 1 331 ? 22.088  -4.993  -8.605  1.00 31.86  ? 868  ASN   A O   1 
ATOM   2506 C CB  . ASN   A 1 331 ? 23.817  -7.118  -8.463  1.00 32.71  ? 868  ASN   A CB  1 
ATOM   2507 C CG  . ASN   A 1 331 ? 24.855  -8.069  -9.012  1.00 42.02  ? 868  ASN   A CG  1 
ATOM   2508 O OD1 . ASN   A 1 331 ? 25.734  -7.667  -9.769  1.00 41.94  ? 868  ASN   A OD1 1 
ATOM   2509 N ND2 . ASN   A 1 331 ? 24.749  -9.341  -8.647  1.00 44.07  ? 868  ASN   A ND2 1 
ATOM   2510 N N   . ASN   A 1 332 ? 23.427  -3.555  -7.506  1.00 26.19  ? 869  ASN   A N   1 
ATOM   2511 C CA  . ASN   A 1 332 ? 22.430  -2.488  -7.509  1.00 24.91  ? 869  ASN   A CA  1 
ATOM   2512 C C   . ASN   A 1 332 ? 22.720  -1.543  -8.673  1.00 32.59  ? 869  ASN   A C   1 
ATOM   2513 O O   . ASN   A 1 332 ? 23.343  -0.484  -8.526  1.00 24.68  ? 869  ASN   A O   1 
ATOM   2514 C CB  . ASN   A 1 332 ? 22.402  -1.714  -6.192  1.00 25.82  ? 869  ASN   A CB  1 
ATOM   2515 C CG  . ASN   A 1 332 ? 21.375  -0.571  -6.223  1.00 24.41  ? 869  ASN   A CG  1 
ATOM   2516 O OD1 . ASN   A 1 332 ? 20.661  -0.398  -7.214  1.00 27.57  ? 869  ASN   A OD1 1 
ATOM   2517 N ND2 . ASN   A 1 332 ? 21.322  0.238   -5.148  1.00 26.19  ? 869  ASN   A ND2 1 
ATOM   2518 N N   . PHE   A 1 333 ? 22.206  -1.912  -9.846  1.00 31.81  ? 870  PHE   A N   1 
ATOM   2519 C CA  . PHE   A 1 333 ? 22.423  -1.094  -11.028 1.00 33.28  ? 870  PHE   A CA  1 
ATOM   2520 C C   . PHE   A 1 333 ? 21.549  0.140   -11.036 1.00 31.72  ? 870  PHE   A C   1 
ATOM   2521 O O   . PHE   A 1 333 ? 21.860  1.094   -11.749 1.00 26.94  ? 870  PHE   A O   1 
ATOM   2522 C CB  . PHE   A 1 333 ? 22.200  -1.932  -12.288 1.00 33.69  ? 870  PHE   A CB  1 
ATOM   2523 C CG  . PHE   A 1 333 ? 23.241  -2.981  -12.474 1.00 36.68  ? 870  PHE   A CG  1 
ATOM   2524 C CD1 . PHE   A 1 333 ? 24.520  -2.629  -12.871 1.00 51.34  ? 870  PHE   A CD1 1 
ATOM   2525 C CD2 . PHE   A 1 333 ? 22.966  -4.307  -12.205 1.00 40.25  ? 870  PHE   A CD2 1 
ATOM   2526 C CE1 . PHE   A 1 333 ? 25.500  -3.588  -13.023 1.00 49.62  ? 870  PHE   A CE1 1 
ATOM   2527 C CE2 . PHE   A 1 333 ? 23.931  -5.268  -12.361 1.00 44.52  ? 870  PHE   A CE2 1 
ATOM   2528 C CZ  . PHE   A 1 333 ? 25.205  -4.909  -12.764 1.00 52.68  ? 870  PHE   A CZ  1 
ATOM   2529 N N   . ASN   A 1 334 ? 20.467  0.152   -10.255 1.00 28.02  ? 871  ASN   A N   1 
ATOM   2530 C CA  . ASN   A 1 334 ? 19.754  1.394   -10.031 1.00 24.68  ? 871  ASN   A CA  1 
ATOM   2531 C C   . ASN   A 1 334 ? 20.673  2.435   -9.391  1.00 29.77  ? 871  ASN   A C   1 
ATOM   2532 O O   . ASN   A 1 334 ? 20.790  3.570   -9.875  1.00 26.86  ? 871  ASN   A O   1 
ATOM   2533 C CB  . ASN   A 1 334 ? 18.532  1.141   -9.156  1.00 30.21  ? 871  ASN   A CB  1 
ATOM   2534 C CG  . ASN   A 1 334 ? 17.634  2.331   -9.096  1.00 39.29  ? 871  ASN   A CG  1 
ATOM   2535 O OD1 . ASN   A 1 334 ? 16.816  2.531   -9.996  1.00 38.69  ? 871  ASN   A OD1 1 
ATOM   2536 N ND2 . ASN   A 1 334 ? 17.795  3.162   -8.059  1.00 31.57  ? 871  ASN   A ND2 1 
ATOM   2537 N N   . GLY   A 1 335 ? 21.365  2.049   -8.321  1.00 27.14  ? 872  GLY   A N   1 
ATOM   2538 C CA  . GLY   A 1 335 ? 22.295  2.976   -7.678  1.00 20.70  ? 872  GLY   A CA  1 
ATOM   2539 C C   . GLY   A 1 335 ? 23.458  3.370   -8.572  1.00 24.03  ? 872  GLY   A C   1 
ATOM   2540 O O   . GLY   A 1 335 ? 23.864  4.543   -8.596  1.00 24.37  ? 872  GLY   A O   1 
ATOM   2541 N N   . VAL   A 1 336 ? 24.004  2.413   -9.332  1.00 22.52  ? 873  VAL   A N   1 
ATOM   2542 C CA  . VAL   A 1 336 ? 25.095  2.741   -10.256 1.00 21.35  ? 873  VAL   A CA  1 
ATOM   2543 C C   . VAL   A 1 336 ? 24.665  3.833   -11.222 1.00 29.47  ? 873  VAL   A C   1 
ATOM   2544 O O   . VAL   A 1 336 ? 25.374  4.831   -11.426 1.00 26.66  ? 873  VAL   A O   1 
ATOM   2545 C CB  . VAL   A 1 336 ? 25.560  1.490   -11.024 1.00 21.52  ? 873  VAL   A CB  1 
ATOM   2546 C CG1 . VAL   A 1 336 ? 26.515  1.895   -12.174 1.00 28.22  ? 873  VAL   A CG1 1 
ATOM   2547 C CG2 . VAL   A 1 336 ? 26.222  0.524   -10.077 1.00 26.57  ? 873  VAL   A CG2 1 
ATOM   2548 N N   . LEU   A 1 337 ? 23.489  3.667   -11.831 1.00 25.46  ? 874  LEU   A N   1 
ATOM   2549 C CA  . LEU   A 1 337 ? 23.103  4.607   -12.873 1.00 22.35  ? 874  LEU   A CA  1 
ATOM   2550 C C   . LEU   A 1 337 ? 22.560  5.912   -12.301 1.00 25.16  ? 874  LEU   A C   1 
ATOM   2551 O O   . LEU   A 1 337 ? 22.556  6.925   -13.007 1.00 27.01  ? 874  LEU   A O   1 
ATOM   2552 C CB  . LEU   A 1 337 ? 22.083  3.974   -13.828 1.00 33.05  ? 874  LEU   A CB  1 
ATOM   2553 C CG  . LEU   A 1 337 ? 22.572  3.084   -14.995 1.00 37.81  ? 874  LEU   A CG  1 
ATOM   2554 C CD1 . LEU   A 1 337 ? 23.880  3.565   -15.623 1.00 36.97  ? 874  LEU   A CD1 1 
ATOM   2555 C CD2 . LEU   A 1 337 ? 22.654  1.644   -14.626 1.00 45.28  ? 874  LEU   A CD2 1 
ATOM   2556 N N   . GLU   A 1 338 ? 22.127  5.917   -11.039 1.00 25.04  ? 875  GLU   A N   1 
ATOM   2557 C CA  . GLU   A 1 338 ? 21.830  7.176   -10.367 1.00 22.92  ? 875  GLU   A CA  1 
ATOM   2558 C C   . GLU   A 1 338 ? 23.082  8.040   -10.258 1.00 29.97  ? 875  GLU   A C   1 
ATOM   2559 O O   . GLU   A 1 338 ? 23.034  9.262   -10.455 1.00 26.19  ? 875  GLU   A O   1 
ATOM   2560 C CB  . GLU   A 1 338 ? 21.265  6.907   -8.973  1.00 25.94  ? 875  GLU   A CB  1 
ATOM   2561 C CG  . GLU   A 1 338 ? 19.822  6.388   -8.968  1.00 33.84  ? 875  GLU   A CG  1 
ATOM   2562 C CD  . GLU   A 1 338 ? 19.381  5.932   -7.586  1.00 35.45  ? 875  GLU   A CD  1 
ATOM   2563 O OE1 . GLU   A 1 338 ? 20.264  5.585   -6.771  1.00 33.63  ? 875  GLU   A OE1 1 
ATOM   2564 O OE2 . GLU   A 1 338 ? 18.160  5.919   -7.321  1.00 38.31  ? 875  GLU   A OE2 1 
ATOM   2565 N N   . ILE   A 1 339 ? 24.215  7.419   -9.934  1.00 26.71  ? 876  ILE   A N   1 
ATOM   2566 C CA  . ILE   A 1 339 ? 25.452  8.186   -9.839  1.00 24.94  ? 876  ILE   A CA  1 
ATOM   2567 C C   . ILE   A 1 339 ? 25.919  8.630   -11.223 1.00 22.60  ? 876  ILE   A C   1 
ATOM   2568 O O   . ILE   A 1 339 ? 26.348  9.769   -11.405 1.00 23.81  ? 876  ILE   A O   1 
ATOM   2569 C CB  . ILE   A 1 339 ? 26.509  7.357   -9.093  1.00 23.06  ? 876  ILE   A CB  1 
ATOM   2570 C CG1 . ILE   A 1 339 ? 26.163  7.351   -7.595  1.00 22.94  ? 876  ILE   A CG1 1 
ATOM   2571 C CG2 . ILE   A 1 339 ? 27.917  7.924   -9.323  1.00 24.73  ? 876  ILE   A CG2 1 
ATOM   2572 C CD1 . ILE   A 1 339 ? 26.996  6.383   -6.745  1.00 20.77  ? 876  ILE   A CD1 1 
ATOM   2573 N N   . VAL   A 1 340 ? 25.842  7.746   -12.219 1.00 23.47  ? 877  VAL   A N   1 
ATOM   2574 C CA  . VAL   A 1 340 ? 26.162  8.145   -13.590 1.00 24.63  ? 877  VAL   A CA  1 
ATOM   2575 C C   . VAL   A 1 340 ? 25.312  9.339   -14.005 1.00 24.17  ? 877  VAL   A C   1 
ATOM   2576 O O   . VAL   A 1 340 ? 25.807  10.317  -14.581 1.00 24.39  ? 877  VAL   A O   1 
ATOM   2577 C CB  . VAL   A 1 340 ? 25.980  6.959   -14.553 1.00 24.65  ? 877  VAL   A CB  1 
ATOM   2578 C CG1 . VAL   A 1 340 ? 26.160  7.402   -16.012 1.00 24.75  ? 877  VAL   A CG1 1 
ATOM   2579 C CG2 . VAL   A 1 340 ? 26.954  5.850   -14.210 1.00 23.98  ? 877  VAL   A CG2 1 
ATOM   2580 N N   . SER   A 1 341 ? 24.012  9.267   -13.727 1.00 25.61  ? 878  SER   A N   1 
ATOM   2581 C CA  . SER   A 1 341 ? 23.126  10.393  -14.023 1.00 20.51  ? 878  SER   A CA  1 
ATOM   2582 C C   . SER   A 1 341 ? 23.606  11.677  -13.349 1.00 23.20  ? 878  SER   A C   1 
ATOM   2583 O O   . SER   A 1 341 ? 23.585  12.754  -13.960 1.00 25.90  ? 878  SER   A O   1 
ATOM   2584 C CB  . SER   A 1 341 ? 21.705  10.020  -13.579 1.00 25.92  ? 878  SER   A CB  1 
ATOM   2585 O OG  . SER   A 1 341 ? 20.759  10.991  -13.972 1.00 38.14  ? 878  SER   A OG  1 
ATOM   2586 N N   . ALA   A 1 342 ? 24.061  11.584  -12.091 1.00 28.59  ? 879  ALA   A N   1 
ATOM   2587 C CA  . ALA   A 1 342 ? 24.513  12.780  -11.373 1.00 26.20  ? 879  ALA   A CA  1 
ATOM   2588 C C   . ALA   A 1 342 ? 25.758  13.393  -12.014 1.00 24.53  ? 879  ALA   A C   1 
ATOM   2589 O O   . ALA   A 1 342 ? 25.855  14.620  -12.163 1.00 24.73  ? 879  ALA   A O   1 
ATOM   2590 C CB  . ALA   A 1 342 ? 24.792  12.437  -9.904  1.00 26.95  ? 879  ALA   A CB  1 
ATOM   2591 N N   . VAL   A 1 343 ? 26.734  12.564  -12.386 1.00 24.93  ? 880  VAL   A N   1 
ATOM   2592 C CA  . VAL   A 1 343 ? 27.961  13.133  -12.937 1.00 25.14  ? 880  VAL   A CA  1 
ATOM   2593 C C   . VAL   A 1 343 ? 27.762  13.613  -14.366 1.00 28.72  ? 880  VAL   A C   1 
ATOM   2594 O O   . VAL   A 1 343 ? 28.582  14.402  -14.862 1.00 26.86  ? 880  VAL   A O   1 
ATOM   2595 C CB  . VAL   A 1 343 ? 29.139  12.142  -12.857 1.00 28.64  ? 880  VAL   A CB  1 
ATOM   2596 C CG1 . VAL   A 1 343 ? 29.454  11.823  -11.401 1.00 28.40  ? 880  VAL   A CG1 1 
ATOM   2597 C CG2 . VAL   A 1 343 ? 28.834  10.862  -13.640 1.00 27.82  ? 880  VAL   A CG2 1 
ATOM   2598 N N   . ASN   A 1 344 ? 26.689  13.172  -15.039 1.00 26.43  ? 881  ASN   A N   1 
ATOM   2599 C CA  . ASN   A 1 344 ? 26.344  13.700  -16.355 1.00 24.44  ? 881  ASN   A CA  1 
ATOM   2600 C C   . ASN   A 1 344 ? 25.605  15.032  -16.286 1.00 28.66  ? 881  ASN   A C   1 
ATOM   2601 O O   . ASN   A 1 344 ? 25.408  15.665  -17.329 1.00 28.93  ? 881  ASN   A O   1 
ATOM   2602 C CB  . ASN   A 1 344 ? 25.474  12.715  -17.142 1.00 26.96  ? 881  ASN   A CB  1 
ATOM   2603 C CG  . ASN   A 1 344 ? 26.272  11.574  -17.745 1.00 30.85  ? 881  ASN   A CG  1 
ATOM   2604 O OD1 . ASN   A 1 344 ? 27.485  11.654  -17.849 1.00 33.18  ? 881  ASN   A OD1 1 
ATOM   2605 N ND2 . ASN   A 1 344 ? 25.581  10.518  -18.176 1.00 27.39  ? 881  ASN   A ND2 1 
ATOM   2606 N N   . SER   A 1 345 ? 25.167  15.457  -15.111 1.00 25.07  ? 882  SER   A N   1 
ATOM   2607 C CA  . SER   A 1 345 ? 24.523  16.761  -15.020 1.00 27.60  ? 882  SER   A CA  1 
ATOM   2608 C C   . SER   A 1 345 ? 25.506  17.838  -15.483 1.00 23.67  ? 882  SER   A C   1 
ATOM   2609 O O   . SER   A 1 345 ? 26.716  17.727  -15.270 1.00 28.74  ? 882  SER   A O   1 
ATOM   2610 C CB  . SER   A 1 345 ? 24.053  17.023  -13.587 1.00 30.56  ? 882  SER   A CB  1 
ATOM   2611 O OG  . SER   A 1 345 ? 25.150  17.146  -12.702 1.00 34.97  ? 882  SER   A OG  1 
ATOM   2612 N N   A VAL   A 1 346 ? 24.976  18.885  -16.126 0.41 28.09  ? 883  VAL   A N   1 
ATOM   2613 N N   B VAL   A 1 346 ? 24.981  18.877  -16.140 0.59 27.89  ? 883  VAL   A N   1 
ATOM   2614 C CA  A VAL   A 1 346 ? 25.853  19.875  -16.750 0.41 33.10  ? 883  VAL   A CA  1 
ATOM   2615 C CA  B VAL   A 1 346 ? 25.874  19.862  -16.745 0.59 33.46  ? 883  VAL   A CA  1 
ATOM   2616 C C   A VAL   A 1 346 ? 26.740  20.546  -15.709 0.41 33.31  ? 883  VAL   A C   1 
ATOM   2617 C C   B VAL   A 1 346 ? 26.762  20.498  -15.686 0.59 33.61  ? 883  VAL   A C   1 
ATOM   2618 O O   A VAL   A 1 346 ? 27.927  20.797  -15.955 0.41 32.35  ? 883  VAL   A O   1 
ATOM   2619 O O   B VAL   A 1 346 ? 27.970  20.671  -15.893 0.59 30.84  ? 883  VAL   A O   1 
ATOM   2620 C CB  A VAL   A 1 346 ? 25.035  20.908  -17.548 0.41 35.24  ? 883  VAL   A CB  1 
ATOM   2621 C CB  B VAL   A 1 346 ? 25.079  20.924  -17.522 0.59 34.85  ? 883  VAL   A CB  1 
ATOM   2622 C CG1 A VAL   A 1 346 ? 24.497  20.281  -18.823 0.41 40.44  ? 883  VAL   A CG1 1 
ATOM   2623 C CG1 B VAL   A 1 346 ? 26.039  21.866  -18.243 0.59 34.92  ? 883  VAL   A CG1 1 
ATOM   2624 C CG2 A VAL   A 1 346 ? 23.900  21.483  -16.705 0.41 32.89  ? 883  VAL   A CG2 1 
ATOM   2625 C CG2 B VAL   A 1 346 ? 24.125  20.260  -18.503 0.59 41.87  ? 883  VAL   A CG2 1 
ATOM   2626 N N   . SER   A 1 347 ? 26.189  20.827  -14.525 1.00 27.17  ? 884  SER   A N   1 
ATOM   2627 C CA  . SER   A 1 347 ? 26.965  21.521  -13.498 1.00 27.96  ? 884  SER   A CA  1 
ATOM   2628 C C   . SER   A 1 347 ? 28.162  20.698  -13.023 1.00 31.19  ? 884  SER   A C   1 
ATOM   2629 O O   . SER   A 1 347 ? 29.195  21.269  -12.654 1.00 28.71  ? 884  SER   A O   1 
ATOM   2630 C CB  . SER   A 1 347 ? 26.059  21.877  -12.321 1.00 36.74  ? 884  SER   A CB  1 
ATOM   2631 O OG  . SER   A 1 347 ? 25.656  20.699  -11.644 1.00 36.59  ? 884  SER   A OG  1 
ATOM   2632 N N   . VAL   A 1 348 ? 28.051  19.370  -13.030 1.00 27.57  ? 885  VAL   A N   1 
ATOM   2633 C CA  . VAL   A 1 348 ? 29.170  18.509  -12.656 1.00 25.03  ? 885  VAL   A CA  1 
ATOM   2634 C C   . VAL   A 1 348 ? 30.056  18.202  -13.855 1.00 23.33  ? 885  VAL   A C   1 
ATOM   2635 O O   . VAL   A 1 348 ? 31.284  18.288  -13.773 1.00 27.65  ? 885  VAL   A O   1 
ATOM   2636 C CB  . VAL   A 1 348 ? 28.655  17.199  -12.015 1.00 27.80  ? 885  VAL   A CB  1 
ATOM   2637 C CG1 . VAL   A 1 348 ? 29.815  16.208  -11.832 1.00 25.79  ? 885  VAL   A CG1 1 
ATOM   2638 C CG2 . VAL   A 1 348 ? 27.984  17.474  -10.666 1.00 22.86  ? 885  VAL   A CG2 1 
ATOM   2639 N N   . TYR   A 1 349 ? 29.430  17.811  -14.968 1.00 26.23  ? 886  TYR   A N   1 
ATOM   2640 C CA  . TYR   A 1 349 ? 30.157  17.380  -16.160 1.00 26.89  ? 886  TYR   A CA  1 
ATOM   2641 C C   . TYR   A 1 349 ? 31.189  18.413  -16.602 1.00 32.76  ? 886  TYR   A C   1 
ATOM   2642 O O   . TYR   A 1 349 ? 32.279  18.053  -17.069 1.00 29.01  ? 886  TYR   A O   1 
ATOM   2643 C CB  . TYR   A 1 349 ? 29.154  17.120  -17.287 1.00 28.52  ? 886  TYR   A CB  1 
ATOM   2644 C CG  . TYR   A 1 349 ? 29.728  16.399  -18.482 1.00 28.57  ? 886  TYR   A CG  1 
ATOM   2645 C CD1 . TYR   A 1 349 ? 29.869  15.015  -18.469 1.00 28.88  ? 886  TYR   A CD1 1 
ATOM   2646 C CD2 . TYR   A 1 349 ? 30.138  17.091  -19.618 1.00 32.64  ? 886  TYR   A CD2 1 
ATOM   2647 C CE1 . TYR   A 1 349 ? 30.399  14.339  -19.556 1.00 29.22  ? 886  TYR   A CE1 1 
ATOM   2648 C CE2 . TYR   A 1 349 ? 30.674  16.419  -20.717 1.00 34.83  ? 886  TYR   A CE2 1 
ATOM   2649 C CZ  . TYR   A 1 349 ? 30.794  15.037  -20.673 1.00 31.61  ? 886  TYR   A CZ  1 
ATOM   2650 O OH  . TYR   A 1 349 ? 31.318  14.334  -21.738 1.00 36.09  ? 886  TYR   A OH  1 
ATOM   2651 N N   . ARG   A 1 350 ? 30.871  19.708  -16.458 1.00 28.49  ? 887  ARG   A N   1 
ATOM   2652 C CA  . ARG   A 1 350 ? 31.783  20.751  -16.919 1.00 28.36  ? 887  ARG   A CA  1 
ATOM   2653 C C   . ARG   A 1 350 ? 32.989  20.977  -16.006 1.00 33.10  ? 887  ARG   A C   1 
ATOM   2654 O O   . ARG   A 1 350 ? 33.807  21.851  -16.305 1.00 31.60  ? 887  ARG   A O   1 
ATOM   2655 C CB  . ARG   A 1 350 ? 31.031  22.079  -17.089 1.00 35.82  ? 887  ARG   A CB  1 
ATOM   2656 C CG  . ARG   A 1 350 ? 30.548  22.703  -15.786 1.00 31.61  ? 887  ARG   A CG  1 
ATOM   2657 C CD  . ARG   A 1 350 ? 30.086  24.160  -15.995 1.00 30.78  ? 887  ARG   A CD  1 
ATOM   2658 N NE  . ARG   A 1 350 ? 31.191  25.022  -16.413 1.00 31.26  ? 887  ARG   A NE  1 
ATOM   2659 C CZ  . ARG   A 1 350 ? 32.088  25.570  -15.589 1.00 35.36  ? 887  ARG   A CZ  1 
ATOM   2660 N NH1 . ARG   A 1 350 ? 33.067  26.332  -16.074 1.00 37.84  ? 887  ARG   A NH1 1 
ATOM   2661 N NH2 . ARG   A 1 350 ? 32.024  25.347  -14.279 1.00 28.61  ? 887  ARG   A NH2 1 
ATOM   2662 N N   . LEU   A 1 351 ? 33.128  20.239  -14.910 1.00 27.76  ? 888  LEU   A N   1 
ATOM   2663 C CA  . LEU   A 1 351 ? 34.213  20.483  -13.951 1.00 29.62  ? 888  LEU   A CA  1 
ATOM   2664 C C   . LEU   A 1 351 ? 35.478  19.738  -14.382 1.00 30.97  ? 888  LEU   A C   1 
ATOM   2665 O O   . LEU   A 1 351 ? 35.932  18.796  -13.733 1.00 29.29  ? 888  LEU   A O   1 
ATOM   2666 C CB  . LEU   A 1 351 ? 33.781  20.062  -12.553 1.00 26.50  ? 888  LEU   A CB  1 
ATOM   2667 C CG  . LEU   A 1 351 ? 32.572  20.804  -11.993 1.00 27.07  ? 888  LEU   A CG  1 
ATOM   2668 C CD1 . LEU   A 1 351 ? 32.166  20.220  -10.654 1.00 25.98  ? 888  LEU   A CD1 1 
ATOM   2669 C CD2 . LEU   A 1 351 ? 32.902  22.294  -11.848 1.00 26.81  ? 888  LEU   A CD2 1 
ATOM   2670 N N   . ASP   A 1 352 ? 36.067  20.205  -15.488 1.00 28.71  ? 889  ASP   A N   1 
ATOM   2671 C CA  . ASP   A 1 352 ? 37.218  19.507  -16.062 1.00 34.31  ? 889  ASP   A CA  1 
ATOM   2672 C C   . ASP   A 1 352 ? 38.356  19.351  -15.060 1.00 31.30  ? 889  ASP   A C   1 
ATOM   2673 O O   . ASP   A 1 352 ? 38.975  18.283  -14.981 1.00 32.28  ? 889  ASP   A O   1 
ATOM   2674 C CB  . ASP   A 1 352 ? 37.715  20.232  -17.310 1.00 37.55  ? 889  ASP   A CB  1 
ATOM   2675 C CG  . ASP   A 1 352 ? 36.757  20.100  -18.478 1.00 49.53  ? 889  ASP   A CG  1 
ATOM   2676 O OD1 . ASP   A 1 352 ? 36.249  18.984  -18.715 1.00 49.32  ? 889  ASP   A OD1 1 
ATOM   2677 O OD2 . ASP   A 1 352 ? 36.519  21.116  -19.159 1.00 61.52  ? 889  ASP   A OD2 1 
ATOM   2678 N N   . HIS   A 1 353 ? 38.651  20.395  -14.281 1.00 30.51  ? 890  HIS   A N   1 
ATOM   2679 C CA  . HIS   A 1 353 ? 39.767  20.284  -13.345 1.00 31.41  ? 890  HIS   A CA  1 
ATOM   2680 C C   . HIS   A 1 353 ? 39.524  19.196  -12.310 1.00 30.37  ? 890  HIS   A C   1 
ATOM   2681 O O   . HIS   A 1 353 ? 40.474  18.533  -11.868 1.00 29.97  ? 890  HIS   A O   1 
ATOM   2682 C CB  . HIS   A 1 353 ? 40.019  21.616  -12.654 1.00 32.87  ? 890  HIS   A CB  1 
ATOM   2683 C CG  . HIS   A 1 353 ? 40.404  22.711  -13.593 1.00 39.36  ? 890  HIS   A CG  1 
ATOM   2684 N ND1 . HIS   A 1 353 ? 41.635  22.767  -14.205 1.00 41.64  ? 890  HIS   A ND1 1 
ATOM   2685 C CD2 . HIS   A 1 353 ? 39.714  23.789  -14.032 1.00 38.88  ? 890  HIS   A CD2 1 
ATOM   2686 C CE1 . HIS   A 1 353 ? 41.687  23.836  -14.981 1.00 45.31  ? 890  HIS   A CE1 1 
ATOM   2687 N NE2 . HIS   A 1 353 ? 40.535  24.475  -14.890 1.00 40.16  ? 890  HIS   A NE2 1 
ATOM   2688 N N   . THR   A 1 354 ? 38.262  18.996  -11.921 1.00 28.27  ? 891  THR   A N   1 
ATOM   2689 C CA  . THR   A 1 354 ? 37.934  17.984  -10.923 1.00 26.00  ? 891  THR   A CA  1 
ATOM   2690 C C   . THR   A 1 354 ? 38.104  16.574  -11.495 1.00 29.90  ? 891  THR   A C   1 
ATOM   2691 O O   . THR   A 1 354 ? 38.678  15.701  -10.836 1.00 29.58  ? 891  THR   A O   1 
ATOM   2692 C CB  . THR   A 1 354 ? 36.507  18.205  -10.398 1.00 25.34  ? 891  THR   A CB  1 
ATOM   2693 O OG1 . THR   A 1 354 ? 36.409  19.492  -9.769  1.00 27.83  ? 891  THR   A OG1 1 
ATOM   2694 C CG2 . THR   A 1 354 ? 36.121  17.123  -9.385  1.00 26.14  ? 891  THR   A CG2 1 
ATOM   2695 N N   . PHE   A 1 355 ? 37.657  16.340  -12.731 1.00 27.42  ? 892  PHE   A N   1 
ATOM   2696 C CA  . PHE   A 1 355 ? 37.838  15.011  -13.315 1.00 30.93  ? 892  PHE   A CA  1 
ATOM   2697 C C   . PHE   A 1 355 ? 39.297  14.723  -13.638 1.00 36.60  ? 892  PHE   A C   1 
ATOM   2698 O O   . PHE   A 1 355 ? 39.729  13.567  -13.570 1.00 31.65  ? 892  PHE   A O   1 
ATOM   2699 C CB  . PHE   A 1 355 ? 36.970  14.854  -14.564 1.00 27.91  ? 892  PHE   A CB  1 
ATOM   2700 C CG  . PHE   A 1 355 ? 35.516  14.705  -14.252 1.00 27.45  ? 892  PHE   A CG  1 
ATOM   2701 C CD1 . PHE   A 1 355 ? 35.013  13.484  -13.860 1.00 27.09  ? 892  PHE   A CD1 1 
ATOM   2702 C CD2 . PHE   A 1 355 ? 34.665  15.791  -14.307 1.00 31.26  ? 892  PHE   A CD2 1 
ATOM   2703 C CE1 . PHE   A 1 355 ? 33.679  13.321  -13.556 1.00 29.08  ? 892  PHE   A CE1 1 
ATOM   2704 C CE2 . PHE   A 1 355 ? 33.320  15.645  -13.994 1.00 32.15  ? 892  PHE   A CE2 1 
ATOM   2705 C CZ  . PHE   A 1 355 ? 32.827  14.408  -13.617 1.00 30.74  ? 892  PHE   A CZ  1 
ATOM   2706 N N   . GLU   A 1 356 ? 40.076  15.743  -13.985 1.00 31.58  ? 893  GLU   A N   1 
ATOM   2707 C CA  . GLU   A 1 356 ? 41.480  15.492  -14.283 1.00 32.18  ? 893  GLU   A CA  1 
ATOM   2708 C C   . GLU   A 1 356 ? 42.289  15.239  -13.017 1.00 31.80  ? 893  GLU   A C   1 
ATOM   2709 O O   . GLU   A 1 356 ? 43.341  14.589  -13.074 1.00 33.19  ? 893  GLU   A O   1 
ATOM   2710 C CB  . GLU   A 1 356 ? 42.068  16.666  -15.056 1.00 39.86  ? 893  GLU   A CB  1 
ATOM   2711 C CG  . GLU   A 1 356 ? 41.454  16.854  -16.404 1.00 51.46  ? 893  GLU   A CG  1 
ATOM   2712 C CD  . GLU   A 1 356 ? 41.972  15.883  -17.437 1.00 66.41  ? 893  GLU   A CD  1 
ATOM   2713 O OE1 . GLU   A 1 356 ? 42.776  14.983  -17.086 1.00 64.56  ? 893  GLU   A OE1 1 
ATOM   2714 O OE2 . GLU   A 1 356 ? 41.563  16.035  -18.607 1.00 61.16  ? 893  GLU   A OE2 1 
ATOM   2715 N N   . ALA   A 1 357 ? 41.806  15.720  -11.866 1.00 27.29  ? 894  ALA   A N   1 
ATOM   2716 C CA  . ALA   A 1 357 ? 42.517  15.518  -10.610 1.00 33.27  ? 894  ALA   A CA  1 
ATOM   2717 C C   . ALA   A 1 357 ? 42.240  14.147  -10.003 1.00 36.45  ? 894  ALA   A C   1 
ATOM   2718 O O   . ALA   A 1 357 ? 42.984  13.711  -9.114  1.00 31.13  ? 894  ALA   A O   1 
ATOM   2719 C CB  . ALA   A 1 357 ? 42.150  16.624  -9.610  1.00 30.00  ? 894  ALA   A CB  1 
ATOM   2720 N N   . LEU   A 1 358 ? 41.194  13.462  -10.461 1.00 29.92  ? 895  LEU   A N   1 
ATOM   2721 C CA  . LEU   A 1 358 ? 40.942  12.102  -10.001 1.00 33.39  ? 895  LEU   A CA  1 
ATOM   2722 C C   . LEU   A 1 358 ? 42.153  11.227  -10.252 1.00 35.52  ? 895  LEU   A C   1 
ATOM   2723 O O   . LEU   A 1 358 ? 42.793  11.316  -11.304 1.00 34.62  ? 895  LEU   A O   1 
ATOM   2724 C CB  . LEU   A 1 358 ? 39.754  11.481  -10.732 1.00 34.20  ? 895  LEU   A CB  1 
ATOM   2725 C CG  . LEU   A 1 358 ? 38.335  11.931  -10.449 1.00 31.94  ? 895  LEU   A CG  1 
ATOM   2726 C CD1 . LEU   A 1 358 ? 37.424  11.190  -11.394 1.00 30.76  ? 895  LEU   A CD1 1 
ATOM   2727 C CD2 . LEU   A 1 358 ? 37.990  11.632  -8.980  1.00 29.53  ? 895  LEU   A CD2 1 
ATOM   2728 N N   . GLN   A 1 359 ? 42.444  10.357  -9.285  1.00 34.30  ? 896  GLN   A N   1 
ATOM   2729 C CA  . GLN   A 1 359 ? 43.348  9.244   -9.535  1.00 41.59  ? 896  GLN   A CA  1 
ATOM   2730 C C   . GLN   A 1 359 ? 42.879  8.466   -10.751 1.00 40.60  ? 896  GLN   A C   1 
ATOM   2731 O O   . GLN   A 1 359 ? 41.680  8.240   -10.939 1.00 32.30  ? 896  GLN   A O   1 
ATOM   2732 C CB  . GLN   A 1 359 ? 43.397  8.301   -8.333  1.00 40.72  ? 896  GLN   A CB  1 
ATOM   2733 C CG  . GLN   A 1 359 ? 44.221  8.794   -7.160  1.00 45.03  ? 896  GLN   A CG  1 
ATOM   2734 C CD  . GLN   A 1 359 ? 44.083  7.874   -5.969  1.00 55.83  ? 896  GLN   A CD  1 
ATOM   2735 O OE1 . GLN   A 1 359 ? 42.974  7.494   -5.596  1.00 52.69  ? 896  GLN   A OE1 1 
ATOM   2736 N NE2 . GLN   A 1 359 ? 45.207  7.489   -5.381  1.00 58.75  ? 896  GLN   A NE2 1 
ATOM   2737 N N   . GLU   A 1 360 ? 43.836  8.035   -11.567 1.00 39.84  ? 897  GLU   A N   1 
ATOM   2738 C CA  . GLU   A 1 360 ? 43.497  7.233   -12.734 1.00 40.72  ? 897  GLU   A CA  1 
ATOM   2739 C C   . GLU   A 1 360 ? 42.679  6.006   -12.345 1.00 35.26  ? 897  GLU   A C   1 
ATOM   2740 O O   . GLU   A 1 360 ? 41.761  5.606   -13.069 1.00 36.77  ? 897  GLU   A O   1 
ATOM   2741 C CB  . GLU   A 1 360 ? 44.782  6.832   -13.462 1.00 46.71  ? 897  GLU   A CB  1 
ATOM   2742 C CG  . GLU   A 1 360 ? 44.572  6.495   -14.905 1.00 51.65  ? 897  GLU   A CG  1 
ATOM   2743 C CD  . GLU   A 1 360 ? 45.880  6.312   -15.639 1.00 53.98  ? 897  GLU   A CD  1 
ATOM   2744 O OE1 . GLU   A 1 360 ? 46.821  7.083   -15.367 1.00 56.95  ? 897  GLU   A OE1 1 
ATOM   2745 O OE2 . GLU   A 1 360 ? 45.960  5.392   -16.475 1.00 62.48  ? 897  GLU   A OE2 1 
ATOM   2746 N N   . ARG   A 1 361 ? 42.976  5.411   -11.185 1.00 40.77  ? 898  ARG   A N   1 
ATOM   2747 C CA  . ARG   A 1 361 ? 42.236  4.225   -10.768 1.00 37.33  ? 898  ARG   A CA  1 
ATOM   2748 C C   . ARG   A 1 361 ? 40.763  4.551   -10.567 1.00 38.79  ? 898  ARG   A C   1 
ATOM   2749 O O   . ARG   A 1 361 ? 39.892  3.726   -10.863 1.00 40.67  ? 898  ARG   A O   1 
ATOM   2750 C CB  . ARG   A 1 361 ? 42.847  3.635   -9.491  1.00 39.79  ? 898  ARG   A CB  1 
ATOM   2751 C CG  . ARG   A 1 361 ? 42.603  4.452   -8.201  1.00 40.20  ? 898  ARG   A CG  1 
ATOM   2752 C CD  . ARG   A 1 361 ? 43.537  3.992   -7.056  1.00 33.85  ? 898  ARG   A CD  1 
ATOM   2753 N NE  . ARG   A 1 361 ? 44.916  4.351   -7.342  1.00 32.49  ? 898  ARG   A NE  1 
ATOM   2754 C CZ  . ARG   A 1 361 ? 45.935  4.170   -6.507  1.00 42.03  ? 898  ARG   A CZ  1 
ATOM   2755 N NH1 . ARG   A 1 361 ? 45.735  3.634   -5.311  1.00 41.44  ? 898  ARG   A NH1 1 
ATOM   2756 N NH2 . ARG   A 1 361 ? 47.160  4.523   -6.864  1.00 43.28  ? 898  ARG   A NH2 1 
ATOM   2757 N N   . LYS   A 1 362 ? 40.468  5.762   -10.078 1.00 30.70  ? 899  LYS   A N   1 
ATOM   2758 C CA  . LYS   A 1 362 ? 39.081  6.174   -9.881  1.00 29.93  ? 899  LYS   A CA  1 
ATOM   2759 C C   . LYS   A 1 362 ? 38.418  6.489   -11.212 1.00 30.31  ? 899  LYS   A C   1 
ATOM   2760 O O   . LYS   A 1 362 ? 37.261  6.114   -11.451 1.00 32.35  ? 899  LYS   A O   1 
ATOM   2761 C CB  . LYS   A 1 362 ? 39.044  7.391   -8.963  1.00 31.23  ? 899  LYS   A CB  1 
ATOM   2762 C CG  . LYS   A 1 362 ? 38.425  7.153   -7.617  1.00 38.27  ? 899  LYS   A CG  1 
ATOM   2763 C CD  . LYS   A 1 362 ? 39.259  6.246   -6.760  1.00 43.04  ? 899  LYS   A CD  1 
ATOM   2764 C CE  . LYS   A 1 362 ? 38.617  6.089   -5.403  1.00 40.22  ? 899  LYS   A CE  1 
ATOM   2765 N NZ  . LYS   A 1 362 ? 39.407  5.157   -4.569  1.00 34.43  ? 899  LYS   A NZ  1 
ATOM   2766 N N   . ARG   A 1 363 ? 39.158  7.158   -12.092 1.00 35.76  ? 900  ARG   A N   1 
ATOM   2767 C CA  . ARG   A 1 363 ? 38.688  7.465   -13.434 1.00 35.02  ? 900  ARG   A CA  1 
ATOM   2768 C C   . ARG   A 1 363 ? 38.251  6.211   -14.183 1.00 38.05  ? 900  ARG   A C   1 
ATOM   2769 O O   . ARG   A 1 363 ? 37.195  6.185   -14.817 1.00 34.57  ? 900  ARG   A O   1 
ATOM   2770 C CB  . ARG   A 1 363 ? 39.812  8.167   -14.190 1.00 32.84  ? 900  ARG   A CB  1 
ATOM   2771 C CG  . ARG   A 1 363 ? 39.375  8.854   -15.434 1.00 48.87  ? 900  ARG   A CG  1 
ATOM   2772 C CD  . ARG   A 1 363 ? 40.539  8.993   -16.370 1.00 56.53  ? 900  ARG   A CD  1 
ATOM   2773 N NE  . ARG   A 1 363 ? 41.628  9.774   -15.795 1.00 63.80  ? 900  ARG   A NE  1 
ATOM   2774 C CZ  . ARG   A 1 363 ? 42.839  9.848   -16.335 1.00 70.59  ? 900  ARG   A CZ  1 
ATOM   2775 N NH1 . ARG   A 1 363 ? 43.099  9.181   -17.451 1.00 73.22  ? 900  ARG   A NH1 1 
ATOM   2776 N NH2 . ARG   A 1 363 ? 43.787  10.576  -15.763 1.00 67.34  ? 900  ARG   A NH2 1 
ATOM   2777 N N   . LYS   A 1 364 ? 39.073  5.164   -14.152 1.00 37.04  ? 901  LYS   A N   1 
ATOM   2778 C CA  . LYS   A 1 364 ? 38.723  3.967   -14.907 1.00 36.66  ? 901  LYS   A CA  1 
ATOM   2779 C C   . LYS   A 1 364 ? 37.446  3.333   -14.364 1.00 33.33  ? 901  LYS   A C   1 
ATOM   2780 O O   . LYS   A 1 364 ? 36.604  2.855   -15.134 1.00 37.25  ? 901  LYS   A O   1 
ATOM   2781 C CB  . LYS   A 1 364 ? 39.911  2.991   -14.901 1.00 40.89  ? 901  LYS   A CB  1 
ATOM   2782 C CG  . LYS   A 1 364 ? 41.162  3.587   -15.580 1.00 46.92  ? 901  LYS   A CG  1 
ATOM   2783 C CD  . LYS   A 1 364 ? 42.077  2.526   -16.162 1.00 65.66  ? 901  LYS   A CD  1 
ATOM   2784 C CE  . LYS   A 1 364 ? 42.215  2.669   -17.673 1.00 72.19  ? 901  LYS   A CE  1 
ATOM   2785 N NZ  . LYS   A 1 364 ? 43.021  3.867   -18.051 1.00 73.09  ? 901  LYS   A NZ  1 
ATOM   2786 N N   . ILE   A 1 365 ? 37.246  3.368   -13.047 1.00 30.87  ? 902  ILE   A N   1 
ATOM   2787 C CA  . ILE   A 1 365 ? 36.020  2.821   -12.475 1.00 30.98  ? 902  ILE   A CA  1 
ATOM   2788 C C   . ILE   A 1 365 ? 34.812  3.626   -12.932 1.00 34.89  ? 902  ILE   A C   1 
ATOM   2789 O O   . ILE   A 1 365 ? 33.783  3.070   -13.328 1.00 30.04  ? 902  ILE   A O   1 
ATOM   2790 C CB  . ILE   A 1 365 ? 36.108  2.798   -10.945 1.00 35.66  ? 902  ILE   A CB  1 
ATOM   2791 C CG1 . ILE   A 1 365 ? 37.117  1.736   -10.501 1.00 43.45  ? 902  ILE   A CG1 1 
ATOM   2792 C CG2 . ILE   A 1 365 ? 34.745  2.570   -10.369 1.00 29.96  ? 902  ILE   A CG2 1 
ATOM   2793 C CD1 . ILE   A 1 365 ? 37.770  2.061   -9.199  1.00 55.54  ? 902  ILE   A CD1 1 
ATOM   2794 N N   . LEU   A 1 366 ? 34.908  4.953   -12.841 1.00 28.70  ? 903  LEU   A N   1 
ATOM   2795 C CA  . LEU   A 1 366 ? 33.806  5.807   -13.274 1.00 31.92  ? 903  LEU   A CA  1 
ATOM   2796 C C   . LEU   A 1 366 ? 33.464  5.564   -14.735 1.00 29.05  ? 903  LEU   A C   1 
ATOM   2797 O O   . LEU   A 1 366 ? 32.292  5.423   -15.095 1.00 30.93  ? 903  LEU   A O   1 
ATOM   2798 C CB  . LEU   A 1 366 ? 34.170  7.278   -13.063 1.00 26.17  ? 903  LEU   A CB  1 
ATOM   2799 C CG  . LEU   A 1 366 ? 33.134  8.272   -13.580 1.00 37.52  ? 903  LEU   A CG  1 
ATOM   2800 C CD1 . LEU   A 1 366 ? 31.804  8.038   -12.891 1.00 35.65  ? 903  LEU   A CD1 1 
ATOM   2801 C CD2 . LEU   A 1 366 ? 33.631  9.670   -13.314 1.00 48.05  ? 903  LEU   A CD2 1 
ATOM   2802 N N   . ASP   A 1 367 ? 34.478  5.531   -15.596 1.00 29.82  ? 904  ASP   A N   1 
ATOM   2803 C CA  . ASP   A 1 367 ? 34.200  5.481   -17.022 1.00 37.69  ? 904  ASP   A CA  1 
ATOM   2804 C C   . ASP   A 1 367 ? 33.666  4.125   -17.448 1.00 37.05  ? 904  ASP   A C   1 
ATOM   2805 O O   . ASP   A 1 367 ? 32.852  4.050   -18.376 1.00 37.58  ? 904  ASP   A O   1 
ATOM   2806 C CB  . ASP   A 1 367 ? 35.459  5.868   -17.793 1.00 36.58  ? 904  ASP   A CB  1 
ATOM   2807 C CG  . ASP   A 1 367 ? 35.742  7.354   -17.685 1.00 39.52  ? 904  ASP   A CG  1 
ATOM   2808 O OD1 . ASP   A 1 367 ? 34.810  8.063   -17.260 1.00 35.54  ? 904  ASP   A OD1 1 
ATOM   2809 O OD2 . ASP   A 1 367 ? 36.861  7.813   -17.995 1.00 34.42  ? 904  ASP   A OD2 1 
ATOM   2810 N N   . GLU   A 1 368 ? 34.088  3.045   -16.784 1.00 31.42  ? 905  GLU   A N   1 
ATOM   2811 C CA  . GLU   A 1 368 ? 33.482  1.753   -17.079 1.00 40.34  ? 905  GLU   A CA  1 
ATOM   2812 C C   . GLU   A 1 368 ? 31.987  1.763   -16.769 1.00 30.47  ? 905  GLU   A C   1 
ATOM   2813 O O   . GLU   A 1 368 ? 31.186  1.183   -17.512 1.00 33.55  ? 905  GLU   A O   1 
ATOM   2814 C CB  . GLU   A 1 368 ? 34.191  0.647   -16.303 1.00 47.69  ? 905  GLU   A CB  1 
ATOM   2815 C CG  . GLU   A 1 368 ? 33.535  -0.699  -16.478 1.00 60.64  ? 905  GLU   A CG  1 
ATOM   2816 C CD  . GLU   A 1 368 ? 34.545  -1.790  -16.674 1.00 78.31  ? 905  GLU   A CD  1 
ATOM   2817 O OE1 . GLU   A 1 368 ? 34.886  -2.467  -15.680 1.00 85.81  ? 905  GLU   A OE1 1 
ATOM   2818 O OE2 . GLU   A 1 368 ? 35.018  -1.946  -17.820 1.00 84.53  ? 905  GLU   A OE2 1 
ATOM   2819 N N   . ALA   A 1 369 ? 31.586  2.429   -15.684 1.00 31.80  ? 906  ALA   A N   1 
ATOM   2820 C CA  . ALA   A 1 369 ? 30.166  2.471   -15.359 1.00 29.48  ? 906  ALA   A CA  1 
ATOM   2821 C C   . ALA   A 1 369 ? 29.404  3.375   -16.316 1.00 29.23  ? 906  ALA   A C   1 
ATOM   2822 O O   . ALA   A 1 369 ? 28.257  3.073   -16.678 1.00 29.31  ? 906  ALA   A O   1 
ATOM   2823 C CB  . ALA   A 1 369 ? 29.952  2.927   -13.916 1.00 30.17  ? 906  ALA   A CB  1 
ATOM   2824 N N   . VAL   A 1 370 ? 30.007  4.500   -16.713 1.00 31.88  ? 907  VAL   A N   1 
ATOM   2825 C CA  . VAL   A 1 370 ? 29.352  5.384   -17.676 1.00 32.93  ? 907  VAL   A CA  1 
ATOM   2826 C C   . VAL   A 1 370 ? 29.064  4.634   -18.969 1.00 35.69  ? 907  VAL   A C   1 
ATOM   2827 O O   . VAL   A 1 370 ? 28.003  4.804   -19.583 1.00 32.61  ? 907  VAL   A O   1 
ATOM   2828 C CB  . VAL   A 1 370 ? 30.210  6.645   -17.920 1.00 38.68  ? 907  VAL   A CB  1 
ATOM   2829 C CG1 . VAL   A 1 370 ? 29.699  7.431   -19.129 1.00 40.95  ? 907  VAL   A CG1 1 
ATOM   2830 C CG2 . VAL   A 1 370 ? 30.210  7.521   -16.680 1.00 32.45  ? 907  VAL   A CG2 1 
ATOM   2831 N N   . GLU   A 1 371 ? 29.985  3.760   -19.385 1.00 34.19  ? 908  GLU   A N   1 
ATOM   2832 C CA  . GLU   A 1 371 ? 29.800  3.048   -20.638 1.00 35.88  ? 908  GLU   A CA  1 
ATOM   2833 C C   . GLU   A 1 371 ? 28.638  2.051   -20.586 1.00 37.95  ? 908  GLU   A C   1 
ATOM   2834 O O   . GLU   A 1 371 ? 28.097  1.703   -21.640 1.00 34.78  ? 908  GLU   A O   1 
ATOM   2835 C CB  . GLU   A 1 371 ? 31.116  2.374   -21.032 1.00 44.03  ? 908  GLU   A CB  1 
ATOM   2836 C CG  . GLU   A 1 371 ? 32.143  3.394   -21.559 1.00 59.17  ? 908  GLU   A CG  1 
ATOM   2837 C CD  . GLU   A 1 371 ? 33.592  2.931   -21.453 1.00 70.37  ? 908  GLU   A CD  1 
ATOM   2838 O OE1 . GLU   A 1 371 ? 34.502  3.794   -21.471 1.00 62.95  ? 908  GLU   A OE1 1 
ATOM   2839 O OE2 . GLU   A 1 371 ? 33.821  1.710   -21.345 1.00 69.44  ? 908  GLU   A OE2 1 
ATOM   2840 N N   . LEU   A 1 372 ? 28.224  1.606   -19.395 1.00 36.44  ? 909  LEU   A N   1 
ATOM   2841 C CA  . LEU   A 1 372 ? 27.025  0.772   -19.292 1.00 38.34  ? 909  LEU   A CA  1 
ATOM   2842 C C   . LEU   A 1 372 ? 25.821  1.441   -19.945 1.00 36.67  ? 909  LEU   A C   1 
ATOM   2843 O O   . LEU   A 1 372 ? 24.968  0.767   -20.531 1.00 30.53  ? 909  LEU   A O   1 
ATOM   2844 C CB  . LEU   A 1 372 ? 26.705  0.475   -17.825 1.00 36.24  ? 909  LEU   A CB  1 
ATOM   2845 C CG  . LEU   A 1 372 ? 27.722  -0.368  -17.068 1.00 39.80  ? 909  LEU   A CG  1 
ATOM   2846 C CD1 . LEU   A 1 372 ? 27.354  -0.415  -15.599 1.00 46.52  ? 909  LEU   A CD1 1 
ATOM   2847 C CD2 . LEU   A 1 372 ? 27.737  -1.765  -17.671 1.00 38.41  ? 909  LEU   A CD2 1 
ATOM   2848 N N   . SER   A 1 373 ? 25.731  2.770   -19.841 1.00 35.94  ? 910  SER   A N   1 
ATOM   2849 C CA  . SER   A 1 373 ? 24.566  3.514   -20.306 1.00 33.60  ? 910  SER   A CA  1 
ATOM   2850 C C   . SER   A 1 373 ? 24.617  3.840   -21.787 1.00 36.70  ? 910  SER   A C   1 
ATOM   2851 O O   . SER   A 1 373 ? 23.576  4.152   -22.373 1.00 42.70  ? 910  SER   A O   1 
ATOM   2852 C CB  . SER   A 1 373 ? 24.431  4.821   -19.513 1.00 35.78  ? 910  SER   A CB  1 
ATOM   2853 O OG  . SER   A 1 373 ? 25.562  5.664   -19.721 1.00 33.92  ? 910  SER   A OG  1 
ATOM   2854 N N   . GLN   A 1 374 ? 25.790  3.760   -22.409 1.00 35.14  ? 911  GLN   A N   1 
ATOM   2855 C CA  . GLN   A 1 374 ? 25.944  4.237   -23.774 1.00 41.21  ? 911  GLN   A CA  1 
ATOM   2856 C C   . GLN   A 1 374 ? 25.263  3.303   -24.767 1.00 39.09  ? 911  GLN   A C   1 
ATOM   2857 O O   . GLN   A 1 374 ? 24.985  2.136   -24.481 1.00 43.78  ? 911  GLN   A O   1 
ATOM   2858 C CB  . GLN   A 1 374 ? 27.427  4.410   -24.110 1.00 41.44  ? 911  GLN   A CB  1 
ATOM   2859 C CG  . GLN   A 1 374 ? 28.073  5.511   -23.271 1.00 38.18  ? 911  GLN   A CG  1 
ATOM   2860 C CD  . GLN   A 1 374 ? 29.574  5.589   -23.423 1.00 51.51  ? 911  GLN   A CD  1 
ATOM   2861 O OE1 . GLN   A 1 374 ? 30.209  4.701   -23.997 1.00 47.22  ? 911  GLN   A OE1 1 
ATOM   2862 N NE2 . GLN   A 1 374 ? 30.155  6.658   -22.896 1.00 57.27  ? 911  GLN   A NE2 1 
ATOM   2863 N N   . ASP   A 1 375 ? 24.967  3.854   -25.943 1.00 41.13  ? 912  ASP   A N   1 
ATOM   2864 C CA  . ASP   A 1 375 ? 24.277  3.140   -27.016 1.00 35.71  ? 912  ASP   A CA  1 
ATOM   2865 C C   . ASP   A 1 375 ? 23.004  2.470   -26.501 1.00 41.74  ? 912  ASP   A C   1 
ATOM   2866 O O   . ASP   A 1 375 ? 22.786  1.267   -26.663 1.00 45.39  ? 912  ASP   A O   1 
ATOM   2867 C CB  . ASP   A 1 375 ? 25.210  2.122   -27.673 1.00 51.46  ? 912  ASP   A CB  1 
ATOM   2868 C CG  . ASP   A 1 375 ? 26.490  2.754   -28.172 1.00 78.69  ? 912  ASP   A CG  1 
ATOM   2869 O OD1 . ASP   A 1 375 ? 26.423  3.847   -28.770 1.00 87.45  ? 912  ASP   A OD1 1 
ATOM   2870 O OD2 . ASP   A 1 375 ? 27.567  2.163   -27.950 1.00 88.04  ? 912  ASP   A OD2 1 
ATOM   2871 N N   . HIS   A 1 376 ? 22.152  3.283   -25.878 1.00 45.39  ? 913  HIS   A N   1 
ATOM   2872 C CA  . HIS   A 1 376 ? 20.876  2.812   -25.342 1.00 43.27  ? 913  HIS   A CA  1 
ATOM   2873 C C   . HIS   A 1 376 ? 21.084  1.641   -24.379 1.00 41.78  ? 913  HIS   A C   1 
ATOM   2874 O O   . HIS   A 1 376 ? 20.447  0.590   -24.493 1.00 37.74  ? 913  HIS   A O   1 
ATOM   2875 C CB  . HIS   A 1 376 ? 19.908  2.433   -26.469 1.00 47.88  ? 913  HIS   A CB  1 
ATOM   2876 C CG  . HIS   A 1 376 ? 19.765  3.483   -27.528 1.00 60.72  ? 913  HIS   A CG  1 
ATOM   2877 N ND1 . HIS   A 1 376 ? 19.127  4.685   -27.305 1.00 65.67  ? 913  HIS   A ND1 1 
ATOM   2878 C CD2 . HIS   A 1 376 ? 20.171  3.508   -28.819 1.00 66.99  ? 913  HIS   A CD2 1 
ATOM   2879 C CE1 . HIS   A 1 376 ? 19.153  5.407   -28.411 1.00 67.87  ? 913  HIS   A CE1 1 
ATOM   2880 N NE2 . HIS   A 1 376 ? 19.781  4.716   -29.345 1.00 68.25  ? 913  HIS   A NE2 1 
ATOM   2881 N N   . PHE   A 1 377 ? 22.014  1.824   -23.437 1.00 37.96  ? 914  PHE   A N   1 
ATOM   2882 C CA  . PHE   A 1 377 ? 22.230  0.889   -22.329 1.00 36.35  ? 914  PHE   A CA  1 
ATOM   2883 C C   . PHE   A 1 377 ? 22.610  -0.508  -22.817 1.00 41.10  ? 914  PHE   A C   1 
ATOM   2884 O O   . PHE   A 1 377 ? 22.295  -1.508  -22.170 1.00 40.24  ? 914  PHE   A O   1 
ATOM   2885 C CB  . PHE   A 1 377 ? 21.003  0.827   -21.408 1.00 34.16  ? 914  PHE   A CB  1 
ATOM   2886 C CG  . PHE   A 1 377 ? 20.700  2.134   -20.738 1.00 37.59  ? 914  PHE   A CG  1 
ATOM   2887 C CD1 . PHE   A 1 377 ? 19.848  3.047   -21.335 1.00 38.92  ? 914  PHE   A CD1 1 
ATOM   2888 C CD2 . PHE   A 1 377 ? 21.295  2.464   -19.527 1.00 36.26  ? 914  PHE   A CD2 1 
ATOM   2889 C CE1 . PHE   A 1 377 ? 19.579  4.260   -20.723 1.00 42.72  ? 914  PHE   A CE1 1 
ATOM   2890 C CE2 . PHE   A 1 377 ? 21.035  3.672   -18.914 1.00 36.90  ? 914  PHE   A CE2 1 
ATOM   2891 C CZ  . PHE   A 1 377 ? 20.179  4.573   -19.515 1.00 38.80  ? 914  PHE   A CZ  1 
ATOM   2892 N N   . LYS   A 1 378 ? 23.302  -0.574  -23.956 1.00 39.40  ? 915  LYS   A N   1 
ATOM   2893 C CA  . LYS   A 1 378 ? 23.715  -1.850  -24.533 1.00 41.93  ? 915  LYS   A CA  1 
ATOM   2894 C C   . LYS   A 1 378 ? 24.465  -2.701  -23.514 1.00 36.92  ? 915  LYS   A C   1 
ATOM   2895 O O   . LYS   A 1 378 ? 24.072  -3.834  -23.216 1.00 39.12  ? 915  LYS   A O   1 
ATOM   2896 C CB  . LYS   A 1 378 ? 24.581  -1.596  -25.771 1.00 39.85  ? 915  LYS   A CB  1 
ATOM   2897 C CG  . LYS   A 1 378 ? 24.921  -2.842  -26.587 1.00 47.52  ? 915  LYS   A CG  1 
ATOM   2898 C CD  . LYS   A 1 378 ? 26.001  -2.535  -27.614 1.00 50.84  ? 915  LYS   A CD  1 
ATOM   2899 C CE  . LYS   A 1 378 ? 26.411  -3.769  -28.403 1.00 61.01  ? 915  LYS   A CE  1 
ATOM   2900 N NZ  . LYS   A 1 378 ? 25.350  -4.209  -29.352 1.00 67.01  ? 915  LYS   A NZ  1 
ATOM   2901 N N   . LYS   A 1 379 ? 25.540  -2.153  -22.947 1.00 35.65  ? 916  LYS   A N   1 
ATOM   2902 C CA  . LYS   A 1 379 ? 26.371  -2.941  -22.044 1.00 40.73  ? 916  LYS   A CA  1 
ATOM   2903 C C   . LYS   A 1 379 ? 25.648  -3.246  -20.736 1.00 42.45  ? 916  LYS   A C   1 
ATOM   2904 O O   . LYS   A 1 379 ? 25.809  -4.340  -20.177 1.00 39.52  ? 916  LYS   A O   1 
ATOM   2905 C CB  . LYS   A 1 379 ? 27.695  -2.217  -21.802 1.00 31.87  ? 916  LYS   A CB  1 
ATOM   2906 C CG  . LYS   A 1 379 ? 28.617  -2.302  -23.018 1.00 40.20  ? 916  LYS   A CG  1 
ATOM   2907 C CD  . LYS   A 1 379 ? 29.865  -1.452  -22.850 1.00 43.24  ? 916  LYS   A CD  1 
ATOM   2908 C CE  . LYS   A 1 379 ? 30.875  -1.701  -23.983 1.00 51.21  ? 916  LYS   A CE  1 
ATOM   2909 N NZ  . LYS   A 1 379 ? 32.023  -0.749  -23.891 1.00 48.05  ? 916  LYS   A NZ  1 
ATOM   2910 N N   . TYR   A 1 380 ? 24.829  -2.309  -20.245 1.00 36.72  ? 917  TYR   A N   1 
ATOM   2911 C CA  . TYR   A 1 380 ? 24.020  -2.596  -19.064 1.00 35.16  ? 917  TYR   A CA  1 
ATOM   2912 C C   . TYR   A 1 380 ? 23.102  -3.790  -19.306 1.00 31.70  ? 917  TYR   A C   1 
ATOM   2913 O O   . TYR   A 1 380 ? 22.988  -4.687  -18.463 1.00 34.87  ? 917  TYR   A O   1 
ATOM   2914 C CB  . TYR   A 1 380 ? 23.183  -1.380  -18.653 1.00 35.45  ? 917  TYR   A CB  1 
ATOM   2915 C CG  . TYR   A 1 380 ? 22.042  -1.775  -17.728 1.00 30.52  ? 917  TYR   A CG  1 
ATOM   2916 C CD1 . TYR   A 1 380 ? 22.297  -2.187  -16.427 1.00 28.96  ? 917  TYR   A CD1 1 
ATOM   2917 C CD2 . TYR   A 1 380 ? 20.725  -1.788  -18.169 1.00 32.70  ? 917  TYR   A CD2 1 
ATOM   2918 C CE1 . TYR   A 1 380 ? 21.262  -2.586  -15.576 1.00 29.71  ? 917  TYR   A CE1 1 
ATOM   2919 C CE2 . TYR   A 1 380 ? 19.679  -2.178  -17.319 1.00 29.27  ? 917  TYR   A CE2 1 
ATOM   2920 C CZ  . TYR   A 1 380 ? 19.966  -2.568  -16.022 1.00 34.30  ? 917  TYR   A CZ  1 
ATOM   2921 O OH  . TYR   A 1 380 ? 18.955  -2.965  -15.164 1.00 33.93  ? 917  TYR   A OH  1 
ATOM   2922 N N   . LEU   A 1 381 ? 22.412  -3.805  -20.449 1.00 32.41  ? 918  LEU   A N   1 
ATOM   2923 C CA  . LEU   A 1 381 ? 21.464  -4.879  -20.712 1.00 30.90  ? 918  LEU   A CA  1 
ATOM   2924 C C   . LEU   A 1 381 ? 22.168  -6.230  -20.811 1.00 40.28  ? 918  LEU   A C   1 
ATOM   2925 O O   . LEU   A 1 381 ? 21.610  -7.253  -20.401 1.00 37.92  ? 918  LEU   A O   1 
ATOM   2926 C CB  . LEU   A 1 381 ? 20.676  -4.575  -21.987 1.00 41.09  ? 918  LEU   A CB  1 
ATOM   2927 C CG  . LEU   A 1 381 ? 19.700  -3.393  -21.886 1.00 41.71  ? 918  LEU   A CG  1 
ATOM   2928 C CD1 . LEU   A 1 381 ? 19.051  -3.070  -23.224 1.00 41.61  ? 918  LEU   A CD1 1 
ATOM   2929 C CD2 . LEU   A 1 381 ? 18.634  -3.672  -20.847 1.00 37.50  ? 918  LEU   A CD2 1 
ATOM   2930 N N   . VAL   A 1 382 ? 23.396  -6.255  -21.330 1.00 43.50  ? 919  VAL   A N   1 
ATOM   2931 C CA  . VAL   A 1 382 ? 24.161  -7.499  -21.321 1.00 47.38  ? 919  VAL   A CA  1 
ATOM   2932 C C   . VAL   A 1 382 ? 24.445  -7.928  -19.887 1.00 40.33  ? 919  VAL   A C   1 
ATOM   2933 O O   . VAL   A 1 382 ? 24.295  -9.102  -19.534 1.00 50.04  ? 919  VAL   A O   1 
ATOM   2934 C CB  . VAL   A 1 382 ? 25.455  -7.348  -22.145 1.00 48.48  ? 919  VAL   A CB  1 
ATOM   2935 C CG1 . VAL   A 1 382 ? 26.376  -8.541  -21.921 1.00 52.17  ? 919  VAL   A CG1 1 
ATOM   2936 C CG2 . VAL   A 1 382 ? 25.128  -7.219  -23.632 1.00 49.00  ? 919  VAL   A CG2 1 
ATOM   2937 N N   . LYS   A 1 383 ? 24.813  -6.977  -19.028 1.00 39.71  ? 920  LYS   A N   1 
ATOM   2938 C CA  . LYS   A 1 383 ? 25.161  -7.314  -17.650 1.00 41.39  ? 920  LYS   A CA  1 
ATOM   2939 C C   . LYS   A 1 383 ? 23.938  -7.774  -16.859 1.00 42.81  ? 920  LYS   A C   1 
ATOM   2940 O O   . LYS   A 1 383 ? 24.033  -8.695  -16.040 1.00 38.60  ? 920  LYS   A O   1 
ATOM   2941 C CB  . LYS   A 1 383 ? 25.838  -6.115  -16.980 1.00 39.52  ? 920  LYS   A CB  1 
ATOM   2942 C CG  . LYS   A 1 383 ? 26.898  -6.479  -15.949 1.00 55.64  ? 920  LYS   A CG  1 
ATOM   2943 C CD  . LYS   A 1 383 ? 27.940  -5.381  -15.798 1.00 58.80  ? 920  LYS   A CD  1 
ATOM   2944 C CE  . LYS   A 1 383 ? 29.167  -5.611  -16.694 1.00 63.88  ? 920  LYS   A CE  1 
ATOM   2945 N NZ  . LYS   A 1 383 ? 30.142  -6.614  -16.154 1.00 64.10  ? 920  LYS   A NZ  1 
ATOM   2946 N N   . LEU   A 1 384 ? 22.780  -7.153  -17.091 1.00 32.71  ? 921  LEU   A N   1 
ATOM   2947 C CA  . LEU   A 1 384 ? 21.570  -7.559  -16.378 1.00 35.48  ? 921  LEU   A CA  1 
ATOM   2948 C C   . LEU   A 1 384 ? 21.211  -9.015  -16.661 1.00 46.12  ? 921  LEU   A C   1 
ATOM   2949 O O   . LEU   A 1 384 ? 20.823  -9.755  -15.749 1.00 45.45  ? 921  LEU   A O   1 
ATOM   2950 C CB  . LEU   A 1 384 ? 20.404  -6.643  -16.749 1.00 36.63  ? 921  LEU   A CB  1 
ATOM   2951 C CG  . LEU   A 1 384 ? 19.038  -6.956  -16.118 1.00 42.08  ? 921  LEU   A CG  1 
ATOM   2952 C CD1 . LEU   A 1 384 ? 19.053  -6.813  -14.595 1.00 35.95  ? 921  LEU   A CD1 1 
ATOM   2953 C CD2 . LEU   A 1 384 ? 17.923  -6.109  -16.730 1.00 41.69  ? 921  LEU   A CD2 1 
ATOM   2954 N N   . LYS   A 1 385 ? 21.326  -9.450  -17.918 1.00 40.98  ? 922  LYS   A N   1 
ATOM   2955 C CA  . LYS   A 1 385 ? 20.867  -10.796 -18.255 1.00 48.78  ? 922  LYS   A CA  1 
ATOM   2956 C C   . LYS   A 1 385 ? 21.761  -11.875 -17.655 1.00 46.28  ? 922  LYS   A C   1 
ATOM   2957 O O   . LYS   A 1 385 ? 21.354  -13.040 -17.598 1.00 56.80  ? 922  LYS   A O   1 
ATOM   2958 C CB  . LYS   A 1 385 ? 20.769  -10.963 -19.778 1.00 57.52  ? 922  LYS   A CB  1 
ATOM   2959 C CG  . LYS   A 1 385 ? 21.944  -11.671 -20.449 1.00 71.10  ? 922  LYS   A CG  1 
ATOM   2960 C CD  . LYS   A 1 385 ? 21.924  -11.475 -21.972 1.00 76.76  ? 922  LYS   A CD  1 
ATOM   2961 C CE  . LYS   A 1 385 ? 21.132  -12.556 -22.711 1.00 84.39  ? 922  LYS   A CE  1 
ATOM   2962 N NZ  . LYS   A 1 385 ? 22.006  -13.624 -23.296 1.00 86.51  ? 922  LYS   A NZ  1 
ATOM   2963 N N   . SER   A 1 386 ? 22.946  -11.513 -17.169 1.00 44.57  ? 923  SER   A N   1 
ATOM   2964 C CA  . SER   A 1 386 ? 23.907  -12.484 -16.675 1.00 54.93  ? 923  SER   A CA  1 
ATOM   2965 C C   . SER   A 1 386 ? 24.039  -12.503 -15.157 1.00 53.84  ? 923  SER   A C   1 
ATOM   2966 O O   . SER   A 1 386 ? 24.631  -13.445 -14.621 1.00 66.94  ? 923  SER   A O   1 
ATOM   2967 C CB  . SER   A 1 386 ? 25.287  -12.215 -17.285 1.00 58.40  ? 923  SER   A CB  1 
ATOM   2968 O OG  . SER   A 1 386 ? 25.886  -11.069 -16.704 1.00 66.69  ? 923  SER   A OG  1 
ATOM   2969 N N   . ILE   A 1 387 ? 23.527  -11.505 -14.449 1.00 52.68  ? 924  ILE   A N   1 
ATOM   2970 C CA  . ILE   A 1 387 ? 23.843  -11.402 -13.031 1.00 59.14  ? 924  ILE   A CA  1 
ATOM   2971 C C   . ILE   A 1 387 ? 23.045  -12.427 -12.237 1.00 61.20  ? 924  ILE   A C   1 
ATOM   2972 O O   . ILE   A 1 387 ? 22.041  -12.979 -12.698 1.00 57.36  ? 924  ILE   A O   1 
ATOM   2973 C CB  . ILE   A 1 387 ? 23.622  -9.976  -12.486 1.00 61.73  ? 924  ILE   A CB  1 
ATOM   2974 C CG1 . ILE   A 1 387 ? 22.349  -9.335  -13.053 1.00 56.48  ? 924  ILE   A CG1 1 
ATOM   2975 C CG2 . ILE   A 1 387 ? 24.853  -9.131  -12.772 1.00 62.26  ? 924  ILE   A CG2 1 
ATOM   2976 C CD1 . ILE   A 1 387 ? 21.042  -9.945  -12.559 1.00 55.96  ? 924  ILE   A CD1 1 
ATOM   2977 N N   . ASN   A 1 388 ? 23.512  -12.686 -11.029 1.00 59.52  ? 925  ASN   A N   1 
ATOM   2978 C CA  . ASN   A 1 388 ? 22.770  -13.561 -10.150 1.00 61.05  ? 925  ASN   A CA  1 
ATOM   2979 C C   . ASN   A 1 388 ? 22.178  -12.768 -8.989  1.00 60.93  ? 925  ASN   A C   1 
ATOM   2980 O O   . ASN   A 1 388 ? 22.766  -11.769 -8.552  1.00 51.23  ? 925  ASN   A O   1 
ATOM   2981 C CB  . ASN   A 1 388 ? 23.666  -14.689 -9.628  1.00 60.83  ? 925  ASN   A CB  1 
ATOM   2982 C CG  . ASN   A 1 388 ? 23.947  -15.740 -10.697 1.00 70.87  ? 925  ASN   A CG  1 
ATOM   2983 O OD1 . ASN   A 1 388 ? 23.042  -16.166 -11.416 1.00 77.31  ? 925  ASN   A OD1 1 
ATOM   2984 N ND2 . ASN   A 1 388 ? 25.203  -16.147 -10.814 1.00 77.36  ? 925  ASN   A ND2 1 
ATOM   2985 N N   . PRO   A 1 389 ? 21.001  -13.160 -8.509  1.00 51.40  ? 926  PRO   A N   1 
ATOM   2986 C CA  . PRO   A 1 389 ? 20.343  -12.416 -7.433  1.00 45.14  ? 926  PRO   A CA  1 
ATOM   2987 C C   . PRO   A 1 389 ? 21.151  -12.490 -6.151  1.00 40.34  ? 926  PRO   A C   1 
ATOM   2988 O O   . PRO   A 1 389 ? 21.947  -13.423 -5.968  1.00 41.40  ? 926  PRO   A O   1 
ATOM   2989 C CB  . PRO   A 1 389 ? 18.994  -13.136 -7.285  1.00 55.12  ? 926  PRO   A CB  1 
ATOM   2990 C CG  . PRO   A 1 389 ? 18.782  -13.817 -8.605  1.00 61.02  ? 926  PRO   A CG  1 
ATOM   2991 C CD  . PRO   A 1 389 ? 20.149  -14.243 -9.031  1.00 55.02  ? 926  PRO   A CD  1 
ATOM   2992 N N   . PRO   A 1 390 ? 20.977  -11.522 -5.231  1.00 37.18  ? 927  PRO   A N   1 
ATOM   2993 C CA  . PRO   A 1 390 ? 20.049  -10.386 -5.372  1.00 37.95  ? 927  PRO   A CA  1 
ATOM   2994 C C   . PRO   A 1 390 ? 20.586  -9.222  -6.200  1.00 35.52  ? 927  PRO   A C   1 
ATOM   2995 O O   . PRO   A 1 390 ? 21.796  -9.012  -6.284  1.00 40.93  ? 927  PRO   A O   1 
ATOM   2996 C CB  . PRO   A 1 390 ? 19.821  -9.934  -3.927  1.00 38.94  ? 927  PRO   A CB  1 
ATOM   2997 C CG  . PRO   A 1 390 ? 21.068  -10.321 -3.220  1.00 45.28  ? 927  PRO   A CG  1 
ATOM   2998 C CD  . PRO   A 1 390 ? 21.545  -11.603 -3.875  1.00 44.84  ? 927  PRO   A CD  1 
ATOM   2999 N N   . CYS   A 1 391 ? 19.670  -8.474  -6.812  1.00 31.29  ? 928  CYS   A N   1 
ATOM   3000 C CA  . CYS   A 1 391 ? 20.045  -7.316  -7.611  1.00 37.19  ? 928  CYS   A CA  1 
ATOM   3001 C C   . CYS   A 1 391 ? 18.925  -6.294  -7.540  1.00 39.97  ? 928  CYS   A C   1 
ATOM   3002 O O   . CYS   A 1 391 ? 17.797  -6.618  -7.169  1.00 41.69  ? 928  CYS   A O   1 
ATOM   3003 C CB  . CYS   A 1 391 ? 20.299  -7.702  -9.064  1.00 40.27  ? 928  CYS   A CB  1 
ATOM   3004 S SG  . CYS   A 1 391 ? 18.764  -8.199  -9.876  1.00 43.02  ? 928  CYS   A SG  1 
ATOM   3005 N N   . VAL   A 1 392 ? 19.254  -5.047  -7.885  1.00 28.06  ? 929  VAL   A N   1 
ATOM   3006 C CA  . VAL   A 1 392 ? 18.251  -4.017  -8.116  1.00 24.93  ? 929  VAL   A CA  1 
ATOM   3007 C C   . VAL   A 1 392 ? 18.432  -3.487  -9.534  1.00 33.20  ? 929  VAL   A C   1 
ATOM   3008 O O   . VAL   A 1 392 ? 19.395  -2.753  -9.805  1.00 32.05  ? 929  VAL   A O   1 
ATOM   3009 C CB  . VAL   A 1 392 ? 18.343  -2.880  -7.088  1.00 24.63  ? 929  VAL   A CB  1 
ATOM   3010 C CG1 . VAL   A 1 392 ? 17.140  -1.965  -7.221  1.00 27.48  ? 929  VAL   A CG1 1 
ATOM   3011 C CG2 . VAL   A 1 392 ? 18.475  -3.427  -5.683  1.00 26.90  ? 929  VAL   A CG2 1 
ATOM   3012 N N   . PRO   A 1 393 ? 17.546  -3.833  -10.465 1.00 37.13  ? 930  PRO   A N   1 
ATOM   3013 C CA  . PRO   A 1 393 ? 17.695  -3.356  -11.840 1.00 27.79  ? 930  PRO   A CA  1 
ATOM   3014 C C   . PRO   A 1 393 ? 17.485  -1.856  -11.932 1.00 29.19  ? 930  PRO   A C   1 
ATOM   3015 O O   . PRO   A 1 393 ? 16.812  -1.230  -11.106 1.00 30.01  ? 930  PRO   A O   1 
ATOM   3016 C CB  . PRO   A 1 393 ? 16.591  -4.104  -12.604 1.00 38.80  ? 930  PRO   A CB  1 
ATOM   3017 C CG  . PRO   A 1 393 ? 16.163  -5.215  -11.693 1.00 37.01  ? 930  PRO   A CG  1 
ATOM   3018 C CD  . PRO   A 1 393 ? 16.361  -4.697  -10.308 1.00 38.69  ? 930  PRO   A CD  1 
ATOM   3019 N N   . PHE   A 1 394 ? 18.084  -1.282  -12.966 1.00 25.31  ? 931  PHE   A N   1 
ATOM   3020 C CA  . PHE   A 1 394 ? 17.825  0.110   -13.305 1.00 23.58  ? 931  PHE   A CA  1 
ATOM   3021 C C   . PHE   A 1 394 ? 16.371  0.270   -13.712 1.00 34.03  ? 931  PHE   A C   1 
ATOM   3022 O O   . PHE   A 1 394 ? 15.926  -0.319  -14.700 1.00 32.81  ? 931  PHE   A O   1 
ATOM   3023 C CB  . PHE   A 1 394 ? 18.753  0.531   -14.439 1.00 26.97  ? 931  PHE   A CB  1 
ATOM   3024 C CG  . PHE   A 1 394 ? 18.498  1.909   -14.957 1.00 31.77  ? 931  PHE   A CG  1 
ATOM   3025 C CD1 . PHE   A 1 394 ? 18.391  2.982   -14.094 1.00 34.71  ? 931  PHE   A CD1 1 
ATOM   3026 C CD2 . PHE   A 1 394 ? 18.373  2.126   -16.319 1.00 35.40  ? 931  PHE   A CD2 1 
ATOM   3027 C CE1 . PHE   A 1 394 ? 18.147  4.252   -14.584 1.00 36.71  ? 931  PHE   A CE1 1 
ATOM   3028 C CE2 . PHE   A 1 394 ? 18.131  3.395   -16.809 1.00 44.43  ? 931  PHE   A CE2 1 
ATOM   3029 C CZ  . PHE   A 1 394 ? 18.018  4.451   -15.942 1.00 36.78  ? 931  PHE   A CZ  1 
ATOM   3030 N N   . PHE   A 1 395 ? 15.633  1.062   -12.942 1.00 31.30  ? 932  PHE   A N   1 
ATOM   3031 C CA  . PHE   A 1 395 ? 14.197  1.177   -13.136 1.00 35.29  ? 932  PHE   A CA  1 
ATOM   3032 C C   . PHE   A 1 395 ? 13.827  2.051   -14.328 1.00 38.86  ? 932  PHE   A C   1 
ATOM   3033 O O   . PHE   A 1 395 ? 12.817  1.789   -14.990 1.00 36.53  ? 932  PHE   A O   1 
ATOM   3034 C CB  . PHE   A 1 395 ? 13.571  1.740   -11.867 1.00 46.20  ? 932  PHE   A CB  1 
ATOM   3035 C CG  . PHE   A 1 395 ? 12.158  1.349   -11.681 1.00 46.92  ? 932  PHE   A CG  1 
ATOM   3036 C CD1 . PHE   A 1 395 ? 11.823  0.032   -11.420 1.00 58.15  ? 932  PHE   A CD1 1 
ATOM   3037 C CD2 . PHE   A 1 395 ? 11.160  2.292   -11.749 1.00 51.56  ? 932  PHE   A CD2 1 
ATOM   3038 C CE1 . PHE   A 1 395 ? 10.512  -0.341  -11.239 1.00 58.63  ? 932  PHE   A CE1 1 
ATOM   3039 C CE2 . PHE   A 1 395 ? 9.858   1.925   -11.570 1.00 58.73  ? 932  PHE   A CE2 1 
ATOM   3040 C CZ  . PHE   A 1 395 ? 9.526   0.607   -11.316 1.00 61.80  ? 932  PHE   A CZ  1 
ATOM   3041 N N   . GLY   A 1 396 ? 14.626  3.081   -14.618 1.00 40.95  ? 933  GLY   A N   1 
ATOM   3042 C CA  . GLY   A 1 396 ? 14.233  4.054   -15.622 1.00 43.59  ? 933  GLY   A CA  1 
ATOM   3043 C C   . GLY   A 1 396 ? 14.015  3.471   -17.002 1.00 43.17  ? 933  GLY   A C   1 
ATOM   3044 O O   . GLY   A 1 396 ? 13.192  3.976   -17.768 1.00 43.16  ? 933  GLY   A O   1 
ATOM   3045 N N   . ILE   A 1 397 ? 14.736  2.402   -17.345 1.00 37.96  ? 934  ILE   A N   1 
ATOM   3046 C CA  . ILE   A 1 397 ? 14.597  1.866   -18.693 1.00 34.08  ? 934  ILE   A CA  1 
ATOM   3047 C C   . ILE   A 1 397 ? 13.212  1.247   -18.896 1.00 39.35  ? 934  ILE   A C   1 
ATOM   3048 O O   . ILE   A 1 397 ? 12.652  1.308   -19.998 1.00 34.55  ? 934  ILE   A O   1 
ATOM   3049 C CB  . ILE   A 1 397 ? 15.739  0.872   -18.985 1.00 49.53  ? 934  ILE   A CB  1 
ATOM   3050 C CG1 . ILE   A 1 397 ? 15.610  0.290   -20.390 1.00 46.40  ? 934  ILE   A CG1 1 
ATOM   3051 C CG2 . ILE   A 1 397 ? 15.782  -0.241  -17.948 1.00 47.25  ? 934  ILE   A CG2 1 
ATOM   3052 C CD1 . ILE   A 1 397 ? 16.946  -0.135  -20.961 1.00 52.99  ? 934  ILE   A CD1 1 
ATOM   3053 N N   . TYR   A 1 398 ? 12.622  0.672   -17.847 1.00 43.71  ? 935  TYR   A N   1 
ATOM   3054 C CA  . TYR   A 1 398 ? 11.272  0.128   -17.978 1.00 40.06  ? 935  TYR   A CA  1 
ATOM   3055 C C   . TYR   A 1 398 ? 10.261  1.243   -18.188 1.00 29.95  ? 935  TYR   A C   1 
ATOM   3056 O O   . TYR   A 1 398 ? 9.382   1.141   -19.051 1.00 33.66  ? 935  TYR   A O   1 
ATOM   3057 C CB  . TYR   A 1 398 ? 10.904  -0.685  -16.738 1.00 43.12  ? 935  TYR   A CB  1 
ATOM   3058 C CG  . TYR   A 1 398 ? 11.796  -1.872  -16.489 1.00 36.21  ? 935  TYR   A CG  1 
ATOM   3059 C CD1 . TYR   A 1 398 ? 11.852  -2.919  -17.394 1.00 38.89  ? 935  TYR   A CD1 1 
ATOM   3060 C CD2 . TYR   A 1 398 ? 12.559  -1.958  -15.335 1.00 30.90  ? 935  TYR   A CD2 1 
ATOM   3061 C CE1 . TYR   A 1 398 ? 12.666  -4.015  -17.163 1.00 41.65  ? 935  TYR   A CE1 1 
ATOM   3062 C CE2 . TYR   A 1 398 ? 13.362  -3.049  -15.094 1.00 36.41  ? 935  TYR   A CE2 1 
ATOM   3063 C CZ  . TYR   A 1 398 ? 13.414  -4.073  -16.013 1.00 40.09  ? 935  TYR   A CZ  1 
ATOM   3064 O OH  . TYR   A 1 398 ? 14.227  -5.160  -15.782 1.00 45.51  ? 935  TYR   A OH  1 
ATOM   3065 N N   . LEU   A 1 399 ? 10.367  2.307   -17.382 1.00 37.43  ? 936  LEU   A N   1 
ATOM   3066 C CA  . LEU   A 1 399 ? 9.499   3.473   -17.527 1.00 32.19  ? 936  LEU   A CA  1 
ATOM   3067 C C   . LEU   A 1 399 ? 9.557   4.028   -18.942 1.00 36.11  ? 936  LEU   A C   1 
ATOM   3068 O O   . LEU   A 1 399 ? 8.526   4.358   -19.534 1.00 35.95  ? 936  LEU   A O   1 
ATOM   3069 C CB  . LEU   A 1 399 ? 9.898   4.545   -16.512 1.00 33.17  ? 936  LEU   A CB  1 
ATOM   3070 C CG  . LEU   A 1 399 ? 9.782   4.172   -15.031 1.00 43.53  ? 936  LEU   A CG  1 
ATOM   3071 C CD1 . LEU   A 1 399 ? 10.397  5.232   -14.131 1.00 37.00  ? 936  LEU   A CD1 1 
ATOM   3072 C CD2 . LEU   A 1 399 ? 8.325   3.957   -14.661 1.00 50.81  ? 936  LEU   A CD2 1 
ATOM   3073 N N   . THR   A 1 400 ? 10.759  4.132   -19.500 1.00 39.16  ? 937  THR   A N   1 
ATOM   3074 C CA  . THR   A 1 400 ? 10.919  4.636   -20.857 1.00 31.10  ? 937  THR   A CA  1 
ATOM   3075 C C   . THR   A 1 400 ? 10.269  3.712   -21.880 1.00 31.30  ? 937  THR   A C   1 
ATOM   3076 O O   . THR   A 1 400 ? 9.558   4.179   -22.775 1.00 36.95  ? 937  THR   A O   1 
ATOM   3077 C CB  . THR   A 1 400 ? 12.413  4.836   -21.140 1.00 37.29  ? 937  THR   A CB  1 
ATOM   3078 O OG1 . THR   A 1 400 ? 12.872  5.956   -20.377 1.00 41.29  ? 937  THR   A OG1 1 
ATOM   3079 C CG2 . THR   A 1 400 ? 12.668  5.074   -22.614 1.00 43.96  ? 937  THR   A CG2 1 
ATOM   3080 N N   . ASN   A 1 401 ? 10.487  2.396   -21.756 1.00 39.55  ? 938  ASN   A N   1 
ATOM   3081 C CA  . ASN   A 1 401 ? 9.893   1.455   -22.701 1.00 38.44  ? 938  ASN   A CA  1 
ATOM   3082 C C   . ASN   A 1 401 ? 8.370   1.428   -22.594 1.00 35.30  ? 938  ASN   A C   1 
ATOM   3083 O O   . ASN   A 1 401 ? 7.687   1.271   -23.607 1.00 34.66  ? 938  ASN   A O   1 
ATOM   3084 C CB  . ASN   A 1 401 ? 10.464  0.049   -22.486 1.00 51.20  ? 938  ASN   A CB  1 
ATOM   3085 C CG  . ASN   A 1 401 ? 11.900  -0.083  -22.971 1.00 67.71  ? 938  ASN   A CG  1 
ATOM   3086 O OD1 . ASN   A 1 401 ? 12.353  0.689   -23.817 1.00 66.80  ? 938  ASN   A OD1 1 
ATOM   3087 N ND2 . ASN   A 1 401 ? 12.621  -1.068  -22.439 1.00 65.39  ? 938  ASN   A ND2 1 
ATOM   3088 N N   . ILE   A 1 402 ? 7.824   1.601   -21.389 1.00 40.90  ? 939  ILE   A N   1 
ATOM   3089 C CA  . ILE   A 1 402 ? 6.371   1.635   -21.252 1.00 42.15  ? 939  ILE   A CA  1 
ATOM   3090 C C   . ILE   A 1 402 ? 5.807   2.905   -21.875 1.00 38.39  ? 939  ILE   A C   1 
ATOM   3091 O O   . ILE   A 1 402 ? 4.805   2.859   -22.599 1.00 42.02  ? 939  ILE   A O   1 
ATOM   3092 C CB  . ILE   A 1 402 ? 5.976   1.490   -19.773 1.00 42.06  ? 939  ILE   A CB  1 
ATOM   3093 C CG1 . ILE   A 1 402 ? 6.295   0.067   -19.306 1.00 43.85  ? 939  ILE   A CG1 1 
ATOM   3094 C CG2 . ILE   A 1 402 ? 4.491   1.821   -19.574 1.00 37.70  ? 939  ILE   A CG2 1 
ATOM   3095 C CD1 . ILE   A 1 402 ? 6.246   -0.122  -17.811 1.00 50.05  ? 939  ILE   A CD1 1 
ATOM   3096 N N   . LEU   A 1 403 ? 6.457   4.054   -21.632 1.00 39.63  ? 940  LEU   A N   1 
ATOM   3097 C CA  . LEU   A 1 403 ? 6.008   5.294   -22.265 1.00 43.37  ? 940  LEU   A CA  1 
ATOM   3098 C C   . LEU   A 1 403 ? 6.067   5.190   -23.786 1.00 40.00  ? 940  LEU   A C   1 
ATOM   3099 O O   . LEU   A 1 403 ? 5.164   5.669   -24.484 1.00 41.95  ? 940  LEU   A O   1 
ATOM   3100 C CB  . LEU   A 1 403 ? 6.845   6.473   -21.767 1.00 44.81  ? 940  LEU   A CB  1 
ATOM   3101 C CG  . LEU   A 1 403 ? 6.568   6.926   -20.330 1.00 44.65  ? 940  LEU   A CG  1 
ATOM   3102 C CD1 . LEU   A 1 403 ? 7.585   7.963   -19.871 1.00 42.84  ? 940  LEU   A CD1 1 
ATOM   3103 C CD2 . LEU   A 1 403 ? 5.152   7.478   -20.206 1.00 48.19  ? 940  LEU   A CD2 1 
ATOM   3104 N N   . LYS   A 1 404 ? 7.116   4.557   -24.319 1.00 41.60  ? 941  LYS   A N   1 
ATOM   3105 C CA  . LYS   A 1 404 ? 7.199   4.358   -25.764 1.00 42.52  ? 941  LYS   A CA  1 
ATOM   3106 C C   . LYS   A 1 404 ? 6.043   3.506   -26.260 1.00 46.99  ? 941  LYS   A C   1 
ATOM   3107 O O   . LYS   A 1 404 ? 5.410   3.821   -27.277 1.00 43.81  ? 941  LYS   A O   1 
ATOM   3108 C CB  . LYS   A 1 404 ? 8.527   3.701   -26.135 1.00 49.96  ? 941  LYS   A CB  1 
ATOM   3109 C CG  . LYS   A 1 404 ? 9.712   4.634   -26.211 1.00 63.49  ? 941  LYS   A CG  1 
ATOM   3110 C CD  . LYS   A 1 404 ? 10.918  3.872   -26.728 1.00 78.07  ? 941  LYS   A CD  1 
ATOM   3111 C CE  . LYS   A 1 404 ? 12.170  4.724   -26.729 1.00 85.97  ? 941  LYS   A CE  1 
ATOM   3112 N NZ  . LYS   A 1 404 ? 13.380  3.898   -27.001 1.00 89.84  ? 941  LYS   A NZ  1 
ATOM   3113 N N   . THR   A 1 405 ? 5.756   2.415   -25.546 1.00 43.69  ? 942  THR   A N   1 
ATOM   3114 C CA  . THR   A 1 405 ? 4.692   1.509   -25.963 1.00 45.36  ? 942  THR   A CA  1 
ATOM   3115 C C   . THR   A 1 405 ? 3.323   2.168   -25.842 1.00 41.37  ? 942  THR   A C   1 
ATOM   3116 O O   . THR   A 1 405 ? 2.457   1.968   -26.699 1.00 44.91  ? 942  THR   A O   1 
ATOM   3117 C CB  . THR   A 1 405 ? 4.747   0.228   -25.130 1.00 40.20  ? 942  THR   A CB  1 
ATOM   3118 O OG1 . THR   A 1 405 ? 6.079   -0.295  -25.160 1.00 49.34  ? 942  THR   A OG1 1 
ATOM   3119 C CG2 . THR   A 1 405 ? 3.777   -0.819  -25.680 1.00 44.12  ? 942  THR   A CG2 1 
ATOM   3120 N N   . GLU   A 1 406 ? 3.104   2.940   -24.775 1.00 40.88  ? 943  GLU   A N   1 
ATOM   3121 C CA  . GLU   A 1 406 ? 1.832   3.641   -24.632 1.00 46.82  ? 943  GLU   A CA  1 
ATOM   3122 C C   . GLU   A 1 406 ? 1.635   4.642   -25.761 1.00 44.49  ? 943  GLU   A C   1 
ATOM   3123 O O   . GLU   A 1 406 ? 0.528   4.785   -26.296 1.00 47.07  ? 943  GLU   A O   1 
ATOM   3124 C CB  . GLU   A 1 406 ? 1.770   4.350   -23.275 1.00 53.13  ? 943  GLU   A CB  1 
ATOM   3125 C CG  . GLU   A 1 406 ? 1.641   3.430   -22.070 1.00 48.89  ? 943  GLU   A CG  1 
ATOM   3126 C CD  . GLU   A 1 406 ? 0.257   2.812   -21.940 1.00 48.62  ? 943  GLU   A CD  1 
ATOM   3127 O OE1 . GLU   A 1 406 ? -0.709  3.331   -22.559 1.00 46.36  ? 943  GLU   A OE1 1 
ATOM   3128 O OE2 . GLU   A 1 406 ? 0.137   1.797   -21.218 1.00 46.31  ? 943  GLU   A OE2 1 
ATOM   3129 N N   . GLU   A 1 407 ? 2.704   5.342   -26.141 1.00 49.78  ? 944  GLU   A N   1 
ATOM   3130 C CA  . GLU   A 1 407 ? 2.588   6.388   -27.150 1.00 51.83  ? 944  GLU   A CA  1 
ATOM   3131 C C   . GLU   A 1 407 ? 2.468   5.811   -28.555 1.00 49.03  ? 944  GLU   A C   1 
ATOM   3132 O O   . GLU   A 1 407 ? 1.788   6.397   -29.407 1.00 53.92  ? 944  GLU   A O   1 
ATOM   3133 C CB  . GLU   A 1 407 ? 3.791   7.326   -27.056 1.00 63.18  ? 944  GLU   A CB  1 
ATOM   3134 C CG  . GLU   A 1 407 ? 3.474   8.672   -26.440 1.00 76.96  ? 944  GLU   A CG  1 
ATOM   3135 C CD  . GLU   A 1 407 ? 2.971   9.661   -27.465 1.00 92.14  ? 944  GLU   A CD  1 
ATOM   3136 O OE1 . GLU   A 1 407 ? 3.132   9.395   -28.675 1.00 99.01  ? 944  GLU   A OE1 1 
ATOM   3137 O OE2 . GLU   A 1 407 ? 2.418   10.705  -27.064 1.00 99.49  ? 944  GLU   A OE2 1 
ATOM   3138 N N   . GLY   A 1 408 ? 3.093   4.664   -28.808 1.00 55.57  ? 945  GLY   A N   1 
ATOM   3139 C CA  . GLY   A 1 408 ? 3.170   4.065   -30.122 1.00 58.19  ? 945  GLY   A CA  1 
ATOM   3140 C C   . GLY   A 1 408 ? 2.029   3.153   -30.511 1.00 50.72  ? 945  GLY   A C   1 
ATOM   3141 O O   . GLY   A 1 408 ? 2.032   2.633   -31.631 1.00 52.08  ? 945  GLY   A O   1 
ATOM   3142 N N   . ASN   A 1 409 ? 1.050   2.952   -29.630 1.00 46.29  ? 946  ASN   A N   1 
ATOM   3143 C CA  . ASN   A 1 409 ? -0.095  2.087   -29.883 1.00 49.50  ? 946  ASN   A CA  1 
ATOM   3144 C C   . ASN   A 1 409 ? -1.367  2.796   -29.443 1.00 49.07  ? 946  ASN   A C   1 
ATOM   3145 O O   . ASN   A 1 409 ? -1.400  3.411   -28.376 1.00 48.42  ? 946  ASN   A O   1 
ATOM   3146 C CB  . ASN   A 1 409 ? 0.020   0.753   -29.127 1.00 42.17  ? 946  ASN   A CB  1 
ATOM   3147 C CG  . ASN   A 1 409 ? 1.271   -0.026  -29.494 1.00 51.78  ? 946  ASN   A CG  1 
ATOM   3148 O OD1 . ASN   A 1 409 ? 1.234   -0.930  -30.330 1.00 52.58  ? 946  ASN   A OD1 1 
ATOM   3149 N ND2 . ASN   A 1 409 ? 2.387   0.321   -28.865 1.00 54.52  ? 946  ASN   A ND2 1 
ATOM   3150 N N   A ASN   A 1 410 ? -2.417  2.680   -30.255 0.48 51.13  ? 947  ASN   A N   1 
ATOM   3151 N N   B ASN   A 1 410 ? -2.414  2.707   -30.257 0.52 51.37  ? 947  ASN   A N   1 
ATOM   3152 C CA  A ASN   A 1 410 ? -3.695  3.317   -29.958 0.48 49.66  ? 947  ASN   A CA  1 
ATOM   3153 C CA  B ASN   A 1 410 ? -3.664  3.370   -29.917 0.52 49.49  ? 947  ASN   A CA  1 
ATOM   3154 C C   A ASN   A 1 410 ? -4.448  2.551   -28.874 0.48 45.76  ? 947  ASN   A C   1 
ATOM   3155 C C   B ASN   A 1 410 ? -4.430  2.571   -28.870 0.52 45.76  ? 947  ASN   A C   1 
ATOM   3156 O O   A ASN   A 1 410 ? -4.412  1.316   -28.830 0.48 41.30  ? 947  ASN   A O   1 
ATOM   3157 O O   B ASN   A 1 410 ? -4.382  1.337   -28.847 0.52 41.18  ? 947  ASN   A O   1 
ATOM   3158 C CB  A ASN   A 1 410 ? -4.549  3.402   -31.226 0.48 51.93  ? 947  ASN   A CB  1 
ATOM   3159 C CB  B ASN   A 1 410 ? -4.533  3.572   -31.158 0.52 52.07  ? 947  ASN   A CB  1 
ATOM   3160 C CG  A ASN   A 1 410 ? -3.960  4.334   -32.267 0.48 53.90  ? 947  ASN   A CG  1 
ATOM   3161 C CG  B ASN   A 1 410 ? -5.509  4.725   -30.999 0.52 54.06  ? 947  ASN   A CG  1 
ATOM   3162 O OD1 A ASN   A 1 410 ? -3.474  5.415   -31.941 0.48 59.16  ? 947  ASN   A OD1 1 
ATOM   3163 O OD1 B ASN   A 1 410 ? -6.539  4.605   -30.328 0.52 45.97  ? 947  ASN   A OD1 1 
ATOM   3164 N ND2 A ASN   A 1 410 ? -4.005  3.920   -33.527 0.48 52.98  ? 947  ASN   A ND2 1 
ATOM   3165 N ND2 B ASN   A 1 410 ? -5.181  5.858   -31.614 0.52 57.77  ? 947  ASN   A ND2 1 
ATOM   3166 N N   . ASP   A 1 411 ? -5.135  3.292   -27.994 1.00 44.00  ? 948  ASP   A N   1 
ATOM   3167 C CA  . ASP   A 1 411 ? -5.961  2.638   -26.981 1.00 40.68  ? 948  ASP   A CA  1 
ATOM   3168 C C   . ASP   A 1 411 ? -7.110  1.864   -27.610 1.00 40.17  ? 948  ASP   A C   1 
ATOM   3169 O O   . ASP   A 1 411 ? -7.599  0.887   -27.025 1.00 42.78  ? 948  ASP   A O   1 
ATOM   3170 C CB  . ASP   A 1 411 ? -6.535  3.658   -25.997 1.00 42.97  ? 948  ASP   A CB  1 
ATOM   3171 C CG  . ASP   A 1 411 ? -5.562  4.036   -24.901 1.00 51.19  ? 948  ASP   A CG  1 
ATOM   3172 O OD1 . ASP   A 1 411 ? -4.602  3.273   -24.653 1.00 40.71  ? 948  ASP   A OD1 1 
ATOM   3173 O OD2 . ASP   A 1 411 ? -5.773  5.107   -24.287 1.00 59.35  ? 948  ASP   A OD2 1 
ATOM   3174 N N   . PHE   A 1 412 ? -7.571  2.289   -28.781 1.00 40.52  ? 949  PHE   A N   1 
ATOM   3175 C CA  . PHE   A 1 412 ? -8.725  1.675   -29.420 1.00 44.49  ? 949  PHE   A CA  1 
ATOM   3176 C C   . PHE   A 1 412 ? -8.372  1.181   -30.816 1.00 47.20  ? 949  PHE   A C   1 
ATOM   3177 O O   . PHE   A 1 412 ? -7.488  1.726   -31.482 1.00 47.42  ? 949  PHE   A O   1 
ATOM   3178 C CB  . PHE   A 1 412 ? -9.899  2.667   -29.516 1.00 41.61  ? 949  PHE   A CB  1 
ATOM   3179 C CG  . PHE   A 1 412 ? -10.474 3.057   -28.186 1.00 47.36  ? 949  PHE   A CG  1 
ATOM   3180 C CD1 . PHE   A 1 412 ? -11.474 2.292   -27.597 1.00 40.95  ? 949  PHE   A CD1 1 
ATOM   3181 C CD2 . PHE   A 1 412 ? -10.024 4.190   -27.523 1.00 48.34  ? 949  PHE   A CD2 1 
ATOM   3182 C CE1 . PHE   A 1 412 ? -12.012 2.649   -26.362 1.00 45.40  ? 949  PHE   A CE1 1 
ATOM   3183 C CE2 . PHE   A 1 412 ? -10.555 4.550   -26.286 1.00 47.93  ? 949  PHE   A CE2 1 
ATOM   3184 C CZ  . PHE   A 1 412 ? -11.553 3.778   -25.709 1.00 47.80  ? 949  PHE   A CZ  1 
ATOM   3185 N N   . LEU   A 1 413 ? -9.078  0.140   -31.254 1.00 40.65  ? 950  LEU   A N   1 
ATOM   3186 C CA  . LEU   A 1 413 ? -9.110  -0.239  -32.661 1.00 47.19  ? 950  LEU   A CA  1 
ATOM   3187 C C   . LEU   A 1 413 ? -10.294 0.461   -33.314 1.00 52.46  ? 950  LEU   A C   1 
ATOM   3188 O O   . LEU   A 1 413 ? -11.425 0.363   -32.828 1.00 46.62  ? 950  LEU   A O   1 
ATOM   3189 C CB  . LEU   A 1 413 ? -9.235  -1.752  -32.818 1.00 42.21  ? 950  LEU   A CB  1 
ATOM   3190 C CG  . LEU   A 1 413 ? -8.217  -2.525  -31.981 1.00 47.12  ? 950  LEU   A CG  1 
ATOM   3191 C CD1 . LEU   A 1 413 ? -8.513  -4.010  -32.004 1.00 44.44  ? 950  LEU   A CD1 1 
ATOM   3192 C CD2 . LEU   A 1 413 ? -6.818  -2.239  -32.493 1.00 48.73  ? 950  LEU   A CD2 1 
ATOM   3193 N N   . LYS   A 1 414 ? -10.036 1.170   -34.401 1.00 59.12  ? 951  LYS   A N   1 
ATOM   3194 C CA  . LYS   A 1 414 ? -11.065 2.000   -35.007 1.00 66.19  ? 951  LYS   A CA  1 
ATOM   3195 C C   . LYS   A 1 414 ? -12.045 1.142   -35.801 1.00 67.11  ? 951  LYS   A C   1 
ATOM   3196 O O   . LYS   A 1 414 ? -11.637 0.270   -36.575 1.00 67.75  ? 951  LYS   A O   1 
ATOM   3197 C CB  . LYS   A 1 414 ? -10.406 3.065   -35.881 1.00 74.30  ? 951  LYS   A CB  1 
ATOM   3198 C CG  . LYS   A 1 414 ? -9.277  3.772   -35.128 1.00 80.78  ? 951  LYS   A CG  1 
ATOM   3199 C CD  . LYS   A 1 414 ? -8.617  4.872   -35.937 1.00 92.63  ? 951  LYS   A CD  1 
ATOM   3200 C CE  . LYS   A 1 414 ? -7.097  4.746   -35.903 1.00 89.98  ? 951  LYS   A CE  1 
ATOM   3201 N NZ  . LYS   A 1 414 ? -6.579  4.054   -37.119 1.00 89.53  ? 951  LYS   A NZ  1 
ATOM   3202 N N   . LYS   A 1 415 ? -13.340 1.371   -35.577 1.00 72.45  ? 952  LYS   A N   1 
ATOM   3203 C CA  . LYS   A 1 415 ? -14.411 0.660   -36.262 1.00 68.19  ? 952  LYS   A CA  1 
ATOM   3204 C C   . LYS   A 1 415 ? -15.427 1.660   -36.788 1.00 71.02  ? 952  LYS   A C   1 
ATOM   3205 O O   . LYS   A 1 415 ? -15.436 2.830   -36.396 1.00 70.57  ? 952  LYS   A O   1 
ATOM   3206 C CB  . LYS   A 1 415 ? -15.128 -0.339  -35.341 1.00 61.02  ? 952  LYS   A CB  1 
ATOM   3207 C CG  . LYS   A 1 415 ? -14.278 -1.503  -34.891 1.00 57.88  ? 952  LYS   A CG  1 
ATOM   3208 C CD  . LYS   A 1 415 ? -13.756 -2.304  -36.074 1.00 66.36  ? 952  LYS   A CD  1 
ATOM   3209 C CE  . LYS   A 1 415 ? -12.996 -3.527  -35.579 1.00 66.03  ? 952  LYS   A CE  1 
ATOM   3210 N NZ  . LYS   A 1 415 ? -12.144 -4.174  -36.615 1.00 66.88  ? 952  LYS   A NZ  1 
ATOM   3211 N N   . LYS   A 1 416 ? -16.299 1.177   -37.678 1.00 63.82  ? 953  LYS   A N   1 
ATOM   3212 C CA  . LYS   A 1 416 ? -17.394 2.013   -38.160 1.00 74.74  ? 953  LYS   A CA  1 
ATOM   3213 C C   . LYS   A 1 416 ? -18.327 2.393   -37.018 1.00 80.20  ? 953  LYS   A C   1 
ATOM   3214 O O   . LYS   A 1 416 ? -18.700 3.562   -36.865 1.00 90.28  ? 953  LYS   A O   1 
ATOM   3215 C CB  . LYS   A 1 416 ? -18.165 1.300   -39.272 1.00 78.06  ? 953  LYS   A CB  1 
ATOM   3216 C CG  . LYS   A 1 416 ? -19.454 2.020   -39.636 1.00 85.30  ? 953  LYS   A CG  1 
ATOM   3217 C CD  . LYS   A 1 416 ? -20.004 1.617   -40.988 1.00 89.43  ? 953  LYS   A CD  1 
ATOM   3218 C CE  . LYS   A 1 416 ? -20.955 2.689   -41.497 1.00 95.99  ? 953  LYS   A CE  1 
ATOM   3219 N NZ  . LYS   A 1 416 ? -21.515 2.369   -42.835 1.00 101.48 ? 953  LYS   A NZ  1 
ATOM   3220 N N   . GLY   A 1 417 ? -18.717 1.415   -36.205 1.00 66.94  ? 954  GLY   A N   1 
ATOM   3221 C CA  . GLY   A 1 417 ? -19.494 1.693   -35.015 1.00 67.23  ? 954  GLY   A CA  1 
ATOM   3222 C C   . GLY   A 1 417 ? -18.608 1.926   -33.808 1.00 71.96  ? 954  GLY   A C   1 
ATOM   3223 O O   . GLY   A 1 417 ? -17.589 2.616   -33.904 1.00 83.30  ? 954  GLY   A O   1 
ATOM   3224 N N   . LYS   A 1 418 ? -18.987 1.354   -32.667 1.00 67.78  ? 955  LYS   A N   1 
ATOM   3225 C CA  . LYS   A 1 418 ? -18.194 1.504   -31.457 1.00 63.92  ? 955  LYS   A CA  1 
ATOM   3226 C C   . LYS   A 1 418 ? -16.789 0.961   -31.685 1.00 60.82  ? 955  LYS   A C   1 
ATOM   3227 O O   . LYS   A 1 418 ? -16.609 -0.144  -32.203 1.00 61.36  ? 955  LYS   A O   1 
ATOM   3228 C CB  . LYS   A 1 418 ? -18.875 0.779   -30.293 1.00 69.47  ? 955  LYS   A CB  1 
ATOM   3229 C CG  . LYS   A 1 418 ? -18.283 1.076   -28.920 1.00 76.31  ? 955  LYS   A CG  1 
ATOM   3230 C CD  . LYS   A 1 418 ? -19.271 0.731   -27.810 1.00 86.82  ? 955  LYS   A CD  1 
ATOM   3231 C CE  . LYS   A 1 418 ? -19.733 -0.717  -27.901 1.00 92.66  ? 955  LYS   A CE  1 
ATOM   3232 N NZ  . LYS   A 1 418 ? -21.057 -0.924  -27.244 1.00 97.57  ? 955  LYS   A NZ  1 
ATOM   3233 N N   . ASP   A 1 419 ? -15.790 1.757   -31.336 1.00 61.19  ? 956  ASP   A N   1 
ATOM   3234 C CA  . ASP   A 1 419 ? -14.419 1.302   -31.469 1.00 56.35  ? 956  ASP   A CA  1 
ATOM   3235 C C   . ASP   A 1 419 ? -14.093 0.319   -30.353 1.00 51.29  ? 956  ASP   A C   1 
ATOM   3236 O O   . ASP   A 1 419 ? -14.630 0.401   -29.246 1.00 51.57  ? 956  ASP   A O   1 
ATOM   3237 C CB  . ASP   A 1 419 ? -13.448 2.484   -31.443 1.00 30.00  ? 956  ASP   A CB  1 
ATOM   3238 C CG  . ASP   A 1 419 ? -13.512 3.318   -32.707 1.00 30.00  ? 956  ASP   A CG  1 
ATOM   3239 O OD1 . ASP   A 1 419 ? -14.082 2.839   -33.709 1.00 30.00  ? 956  ASP   A OD1 1 
ATOM   3240 O OD2 . ASP   A 1 419 ? -13.019 4.463   -32.792 1.00 30.00  ? 956  ASP   A OD2 1 
ATOM   3241 N N   . LEU   A 1 420 ? -13.215 -0.628  -30.662 1.00 45.51  ? 957  LEU   A N   1 
ATOM   3242 C CA  . LEU   A 1 420 ? -12.879 -1.696  -29.736 1.00 38.50  ? 957  LEU   A CA  1 
ATOM   3243 C C   . LEU   A 1 420 ? -11.670 -1.314  -28.896 1.00 36.50  ? 957  LEU   A C   1 
ATOM   3244 O O   . LEU   A 1 420 ? -10.782 -0.585  -29.346 1.00 39.06  ? 957  LEU   A O   1 
ATOM   3245 C CB  . LEU   A 1 420 ? -12.583 -2.993  -30.490 1.00 44.18  ? 957  LEU   A CB  1 
ATOM   3246 C CG  . LEU   A 1 420 ? -13.587 -3.389  -31.570 1.00 45.79  ? 957  LEU   A CG  1 
ATOM   3247 C CD1 . LEU   A 1 420 ? -13.216 -4.741  -32.164 1.00 46.68  ? 957  LEU   A CD1 1 
ATOM   3248 C CD2 . LEU   A 1 420 ? -15.002 -3.408  -31.004 1.00 41.65  ? 957  LEU   A CD2 1 
ATOM   3249 N N   . ILE   A 1 421 ? -11.648 -1.823  -27.665 1.00 34.42  ? 958  ILE   A N   1 
ATOM   3250 C CA  . ILE   A 1 421 ? -10.474 -1.710  -26.809 1.00 32.49  ? 958  ILE   A CA  1 
ATOM   3251 C C   . ILE   A 1 421 ? -9.324  -2.476  -27.448 1.00 34.12  ? 958  ILE   A C   1 
ATOM   3252 O O   . ILE   A 1 421 ? -9.471  -3.649  -27.806 1.00 33.33  ? 958  ILE   A O   1 
ATOM   3253 C CB  . ILE   A 1 421 ? -10.793 -2.251  -25.406 1.00 33.20  ? 958  ILE   A CB  1 
ATOM   3254 C CG1 . ILE   A 1 421 ? -11.897 -1.402  -24.758 1.00 34.50  ? 958  ILE   A CG1 1 
ATOM   3255 C CG2 . ILE   A 1 421 ? -9.524  -2.328  -24.533 1.00 29.10  ? 958  ILE   A CG2 1 
ATOM   3256 C CD1 . ILE   A 1 421 ? -12.651 -2.098  -23.633 1.00 37.30  ? 958  ILE   A CD1 1 
ATOM   3257 N N   . ASN   A 1 422 ? -8.179  -1.812  -27.611 1.00 34.71  ? 959  ASN   A N   1 
ATOM   3258 C CA  . ASN   A 1 422 ? -6.977  -2.466  -28.129 1.00 32.03  ? 959  ASN   A CA  1 
ATOM   3259 C C   . ASN   A 1 422 ? -6.332  -3.236  -26.988 1.00 30.95  ? 959  ASN   A C   1 
ATOM   3260 O O   . ASN   A 1 422 ? -5.559  -2.678  -26.208 1.00 34.23  ? 959  ASN   A O   1 
ATOM   3261 C CB  . ASN   A 1 422 ? -6.011  -1.441  -28.716 1.00 33.70  ? 959  ASN   A CB  1 
ATOM   3262 C CG  . ASN   A 1 422 ? -4.743  -2.081  -29.267 1.00 40.64  ? 959  ASN   A CG  1 
ATOM   3263 O OD1 . ASN   A 1 422 ? -4.544  -3.296  -29.150 1.00 39.03  ? 959  ASN   A OD1 1 
ATOM   3264 N ND2 . ASN   A 1 422 ? -3.888  -1.270  -29.889 1.00 38.56  ? 959  ASN   A ND2 1 
ATOM   3265 N N   . PHE   A 1 423 ? -6.643  -4.527  -26.875 1.00 31.15  ? 960  PHE   A N   1 
ATOM   3266 C CA  . PHE   A 1 423 ? -6.090  -5.277  -25.754 1.00 33.39  ? 960  PHE   A CA  1 
ATOM   3267 C C   . PHE   A 1 423 ? -4.642  -5.673  -25.997 1.00 33.28  ? 960  PHE   A C   1 
ATOM   3268 O O   . PHE   A 1 423 ? -3.867  -5.771  -25.041 1.00 31.26  ? 960  PHE   A O   1 
ATOM   3269 C CB  . PHE   A 1 423 ? -6.915  -6.527  -25.452 1.00 32.21  ? 960  PHE   A CB  1 
ATOM   3270 C CG  . PHE   A 1 423 ? -6.514  -7.197  -24.170 1.00 29.26  ? 960  PHE   A CG  1 
ATOM   3271 C CD1 . PHE   A 1 423 ? -6.956  -6.704  -22.957 1.00 33.06  ? 960  PHE   A CD1 1 
ATOM   3272 C CD2 . PHE   A 1 423 ? -5.650  -8.280  -24.175 1.00 28.88  ? 960  PHE   A CD2 1 
ATOM   3273 C CE1 . PHE   A 1 423 ? -6.565  -7.289  -21.767 1.00 33.18  ? 960  PHE   A CE1 1 
ATOM   3274 C CE2 . PHE   A 1 423 ? -5.263  -8.874  -22.996 1.00 31.11  ? 960  PHE   A CE2 1 
ATOM   3275 C CZ  . PHE   A 1 423 ? -5.722  -8.382  -21.788 1.00 35.48  ? 960  PHE   A CZ  1 
ATOM   3276 N N   . SER   A 1 424 ? -4.260  -5.890  -27.256 1.00 33.73  ? 961  SER   A N   1 
ATOM   3277 C CA  . SER   A 1 424 ? -2.873  -6.234  -27.546 1.00 36.32  ? 961  SER   A CA  1 
ATOM   3278 C C   . SER   A 1 424 ? -1.919  -5.170  -27.023 1.00 38.85  ? 961  SER   A C   1 
ATOM   3279 O O   . SER   A 1 424 ? -0.816  -5.491  -26.560 1.00 34.56  ? 961  SER   A O   1 
ATOM   3280 C CB  . SER   A 1 424 ? -2.694  -6.440  -29.047 1.00 44.47  ? 961  SER   A CB  1 
ATOM   3281 O OG  . SER   A 1 424 ? -3.239  -7.696  -29.423 1.00 49.54  ? 961  SER   A OG  1 
ATOM   3282 N N   . LYS   A 1 425 ? -2.325  -3.899  -27.078 1.00 31.13  ? 962  LYS   A N   1 
ATOM   3283 C CA  . LYS   A 1 425 ? -1.508  -2.853  -26.472 1.00 35.06  ? 962  LYS   A CA  1 
ATOM   3284 C C   . LYS   A 1 425 ? -1.252  -3.150  -25.001 1.00 39.31  ? 962  LYS   A C   1 
ATOM   3285 O O   . LYS   A 1 425 ? -0.117  -3.028  -24.520 1.00 33.41  ? 962  LYS   A O   1 
ATOM   3286 C CB  . LYS   A 1 425 ? -2.187  -1.494  -26.635 1.00 33.93  ? 962  LYS   A CB  1 
ATOM   3287 C CG  . LYS   A 1 425 ? -1.468  -0.335  -25.942 1.00 36.15  ? 962  LYS   A CG  1 
ATOM   3288 C CD  . LYS   A 1 425 ? -2.226  0.975   -26.123 1.00 39.81  ? 962  LYS   A CD  1 
ATOM   3289 C CE  . LYS   A 1 425 ? -1.444  2.161   -25.551 1.00 33.97  ? 962  LYS   A CE  1 
ATOM   3290 N NZ  . LYS   A 1 425 ? -2.124  3.474   -25.762 1.00 37.04  ? 962  LYS   A NZ  1 
ATOM   3291 N N   . ARG   A 1 426 ? -2.301  -3.540  -24.268 1.00 29.28  ? 963  ARG   A N   1 
ATOM   3292 C CA  . ARG   A 1 426 ? -2.152  -3.788  -22.839 1.00 32.37  ? 963  ARG   A CA  1 
ATOM   3293 C C   . ARG   A 1 426 ? -1.252  -4.990  -22.594 1.00 32.26  ? 963  ARG   A C   1 
ATOM   3294 O O   . ARG   A 1 426 ? -0.439  -4.987  -21.659 1.00 33.74  ? 963  ARG   A O   1 
ATOM   3295 C CB  . ARG   A 1 426 ? -3.526  -4.001  -22.193 1.00 29.42  ? 963  ARG   A CB  1 
ATOM   3296 C CG  . ARG   A 1 426 ? -4.241  -2.697  -21.789 1.00 30.26  ? 963  ARG   A CG  1 
ATOM   3297 C CD  . ARG   A 1 426 ? -4.607  -1.826  -22.998 1.00 27.70  ? 963  ARG   A CD  1 
ATOM   3298 N NE  . ARG   A 1 426 ? -5.417  -0.668  -22.610 1.00 28.92  ? 963  ARG   A NE  1 
ATOM   3299 C CZ  . ARG   A 1 426 ? -6.193  0.020   -23.445 1.00 33.03  ? 963  ARG   A CZ  1 
ATOM   3300 N NH1 . ARG   A 1 426 ? -6.293  -0.351  -24.717 1.00 29.87  ? 963  ARG   A NH1 1 
ATOM   3301 N NH2 . ARG   A 1 426 ? -6.879  1.071   -23.004 1.00 31.44  ? 963  ARG   A NH2 1 
ATOM   3302 N N   . ARG   A 1 427 ? -1.380  -6.019  -23.434 1.00 35.41  ? 964  ARG   A N   1 
ATOM   3303 C CA  . ARG   A 1 427 ? -0.517  -7.190  -23.326 1.00 32.64  ? 964  ARG   A CA  1 
ATOM   3304 C C   . ARG   A 1 427 ? 0.949   -6.807  -23.487 1.00 39.96  ? 964  ARG   A C   1 
ATOM   3305 O O   . ARG   A 1 427 ? 1.805   -7.247  -22.710 1.00 34.20  ? 964  ARG   A O   1 
ATOM   3306 C CB  . ARG   A 1 427 ? -0.916  -8.229  -24.372 1.00 35.23  ? 964  ARG   A CB  1 
ATOM   3307 C CG  . ARG   A 1 427 ? -0.046  -9.473  -24.379 1.00 34.59  ? 964  ARG   A CG  1 
ATOM   3308 C CD  . ARG   A 1 427 ? -0.494  -10.475 -25.439 1.00 43.68  ? 964  ARG   A CD  1 
ATOM   3309 N NE  . ARG   A 1 427 ? -1.859  -10.937 -25.200 1.00 47.51  ? 964  ARG   A NE  1 
ATOM   3310 C CZ  . ARG   A 1 427 ? -2.899  -10.603 -25.956 1.00 45.99  ? 964  ARG   A CZ  1 
ATOM   3311 N NH1 . ARG   A 1 427 ? -2.729  -9.818  -27.013 1.00 40.28  ? 964  ARG   A NH1 1 
ATOM   3312 N NH2 . ARG   A 1 427 ? -4.106  -11.075 -25.666 1.00 41.83  ? 964  ARG   A NH2 1 
ATOM   3313 N N   . LYS   A 1 428 ? 1.250   -5.977  -24.494 1.00 30.46  ? 965  LYS   A N   1 
ATOM   3314 C CA  . LYS   A 1 428 ? 2.617   -5.509  -24.701 1.00 34.67  ? 965  LYS   A CA  1 
ATOM   3315 C C   . LYS   A 1 428 ? 3.143   -4.786  -23.466 1.00 33.77  ? 965  LYS   A C   1 
ATOM   3316 O O   . LYS   A 1 428 ? 4.303   -4.970  -23.076 1.00 33.52  ? 965  LYS   A O   1 
ATOM   3317 C CB  . LYS   A 1 428 ? 2.687   -4.583  -25.920 1.00 39.21  ? 965  LYS   A CB  1 
ATOM   3318 C CG  . LYS   A 1 428 ? 2.264   -5.202  -27.238 1.00 47.64  ? 965  LYS   A CG  1 
ATOM   3319 C CD  . LYS   A 1 428 ? 2.235   -4.144  -28.334 1.00 62.31  ? 965  LYS   A CD  1 
ATOM   3320 C CE  . LYS   A 1 428 ? 1.788   -4.714  -29.668 1.00 77.20  ? 965  LYS   A CE  1 
ATOM   3321 N NZ  . LYS   A 1 428 ? 1.798   -3.667  -30.727 1.00 87.61  ? 965  LYS   A NZ  1 
ATOM   3322 N N   . VAL   A 1 429 ? 2.311   -3.951  -22.841 1.00 34.53  ? 966  VAL   A N   1 
ATOM   3323 C CA  . VAL   A 1 429 ? 2.746   -3.288  -21.618 1.00 38.24  ? 966  VAL   A CA  1 
ATOM   3324 C C   . VAL   A 1 429 ? 2.928   -4.310  -20.500 1.00 35.42  ? 966  VAL   A C   1 
ATOM   3325 O O   . VAL   A 1 429 ? 3.911   -4.265  -19.753 1.00 33.21  ? 966  VAL   A O   1 
ATOM   3326 C CB  . VAL   A 1 429 ? 1.756   -2.177  -21.224 1.00 35.97  ? 966  VAL   A CB  1 
ATOM   3327 C CG1 . VAL   A 1 429 ? 2.070   -1.667  -19.831 1.00 37.37  ? 966  VAL   A CG1 1 
ATOM   3328 C CG2 . VAL   A 1 429 ? 1.813   -1.038  -22.232 1.00 36.16  ? 966  VAL   A CG2 1 
ATOM   3329 N N   . ALA   A 1 430 ? 2.001   -5.262  -20.382 1.00 31.71  ? 967  ALA   A N   1 
ATOM   3330 C CA  . ALA   A 1 430 ? 2.131   -6.297  -19.360 1.00 37.39  ? 967  ALA   A CA  1 
ATOM   3331 C C   . ALA   A 1 430 ? 3.388   -7.137  -19.547 1.00 36.89  ? 967  ALA   A C   1 
ATOM   3332 O O   . ALA   A 1 430 ? 3.938   -7.644  -18.560 1.00 35.93  ? 967  ALA   A O   1 
ATOM   3333 C CB  . ALA   A 1 430 ? 0.898   -7.205  -19.357 1.00 32.47  ? 967  ALA   A CB  1 
ATOM   3334 N N   . GLU   A 1 431 ? 3.844   -7.324  -20.792 1.00 33.47  ? 968  GLU   A N   1 
ATOM   3335 C CA  . GLU   A 1 431 ? 5.097   -8.047  -21.006 1.00 39.47  ? 968  GLU   A CA  1 
ATOM   3336 C C   . GLU   A 1 431 ? 6.244   -7.342  -20.303 1.00 41.39  ? 968  GLU   A C   1 
ATOM   3337 O O   . GLU   A 1 431 ? 7.116   -7.981  -19.704 1.00 37.06  ? 968  GLU   A O   1 
ATOM   3338 C CB  . GLU   A 1 431 ? 5.415   -8.172  -22.499 1.00 48.35  ? 968  GLU   A CB  1 
ATOM   3339 C CG  . GLU   A 1 431 ? 4.330   -8.792  -23.365 1.00 71.37  ? 968  GLU   A CG  1 
ATOM   3340 C CD  . GLU   A 1 431 ? 4.420   -10.304 -23.459 1.00 87.34  ? 968  GLU   A CD  1 
ATOM   3341 O OE1 . GLU   A 1 431 ? 3.503   -10.917 -24.054 1.00 89.82  ? 968  GLU   A OE1 1 
ATOM   3342 O OE2 . GLU   A 1 431 ? 5.406   -10.877 -22.948 1.00 93.05  ? 968  GLU   A OE2 1 
ATOM   3343 N N   . ILE   A 1 432 ? 6.258   -6.017  -20.371 1.00 34.81  ? 969  ILE   A N   1 
ATOM   3344 C CA  . ILE   A 1 432 ? 7.338   -5.249  -19.772 1.00 34.24  ? 969  ILE   A CA  1 
ATOM   3345 C C   . ILE   A 1 432 ? 7.226   -5.278  -18.253 1.00 36.78  ? 969  ILE   A C   1 
ATOM   3346 O O   . ILE   A 1 432 ? 8.231   -5.422  -17.546 1.00 37.18  ? 969  ILE   A O   1 
ATOM   3347 C CB  . ILE   A 1 432 ? 7.321   -3.818  -20.335 1.00 37.50  ? 969  ILE   A CB  1 
ATOM   3348 C CG1 . ILE   A 1 432 ? 7.481   -3.865  -21.856 1.00 39.48  ? 969  ILE   A CG1 1 
ATOM   3349 C CG2 . ILE   A 1 432 ? 8.362   -2.954  -19.645 1.00 42.51  ? 969  ILE   A CG2 1 
ATOM   3350 C CD1 . ILE   A 1 432 ? 7.337   -2.515  -22.529 1.00 46.32  ? 969  ILE   A CD1 1 
ATOM   3351 N N   . THR   A 1 433 ? 6.007   -5.173  -17.721 1.00 35.01  ? 970  THR   A N   1 
ATOM   3352 C CA  . THR   A 1 433 ? 5.863   -5.231  -16.273 1.00 32.16  ? 970  THR   A CA  1 
ATOM   3353 C C   . THR   A 1 433 ? 6.159   -6.625  -15.744 1.00 32.79  ? 970  THR   A C   1 
ATOM   3354 O O   . THR   A 1 433 ? 6.578   -6.771  -14.591 1.00 33.44  ? 970  THR   A O   1 
ATOM   3355 C CB  . THR   A 1 433 ? 4.461   -4.777  -15.839 1.00 35.68  ? 970  THR   A CB  1 
ATOM   3356 O OG1 . THR   A 1 433 ? 3.467   -5.683  -16.346 1.00 35.94  ? 970  THR   A OG1 1 
ATOM   3357 C CG2 . THR   A 1 433 ? 4.166   -3.379  -16.342 1.00 33.88  ? 970  THR   A CG2 1 
ATOM   3358 N N   . GLY   A 1 434 ? 5.978   -7.656  -16.571 1.00 28.40  ? 971  GLY   A N   1 
ATOM   3359 C CA  . GLY   A 1 434 ? 6.347   -8.996  -16.150 1.00 33.66  ? 971  GLY   A CA  1 
ATOM   3360 C C   . GLY   A 1 434 ? 7.838   -9.122  -15.913 1.00 38.51  ? 971  GLY   A C   1 
ATOM   3361 O O   . GLY   A 1 434 ? 8.274   -9.877  -15.039 1.00 35.63  ? 971  GLY   A O   1 
ATOM   3362 N N   . GLU   A 1 435 ? 8.636   -8.364  -16.672 1.00 35.40  ? 972  GLU   A N   1 
ATOM   3363 C CA  . GLU   A 1 435 ? 10.081  -8.367  -16.474 1.00 42.29  ? 972  GLU   A CA  1 
ATOM   3364 C C   . GLU   A 1 435 ? 10.451  -7.721  -15.149 1.00 36.93  ? 972  GLU   A C   1 
ATOM   3365 O O   . GLU   A 1 435 ? 11.352  -8.203  -14.452 1.00 40.64  ? 972  GLU   A O   1 
ATOM   3366 C CB  . GLU   A 1 435 ? 10.779  -7.634  -17.618 1.00 46.09  ? 972  GLU   A CB  1 
ATOM   3367 C CG  . GLU   A 1 435 ? 10.599  -8.247  -18.986 1.00 57.25  ? 972  GLU   A CG  1 
ATOM   3368 C CD  . GLU   A 1 435 ? 11.618  -7.716  -19.974 1.00 81.13  ? 972  GLU   A CD  1 
ATOM   3369 O OE1 . GLU   A 1 435 ? 12.462  -6.889  -19.565 1.00 84.30  ? 972  GLU   A OE1 1 
ATOM   3370 O OE2 . GLU   A 1 435 ? 11.581  -8.129  -21.153 1.00 89.74  ? 972  GLU   A OE2 1 
ATOM   3371 N N   . ILE   A 1 436 ? 9.777   -6.625  -14.796 1.00 32.98  ? 973  ILE   A N   1 
ATOM   3372 C CA  . ILE   A 1 436 ? 10.051  -5.952  -13.528 1.00 32.61  ? 973  ILE   A CA  1 
ATOM   3373 C C   . ILE   A 1 436 ? 9.865   -6.923  -12.377 1.00 35.94  ? 973  ILE   A C   1 
ATOM   3374 O O   . ILE   A 1 436 ? 10.682  -6.993  -11.455 1.00 37.50  ? 973  ILE   A O   1 
ATOM   3375 C CB  . ILE   A 1 436 ? 9.143   -4.720  -13.361 1.00 33.59  ? 973  ILE   A CB  1 
ATOM   3376 C CG1 . ILE   A 1 436 ? 9.498   -3.641  -14.382 1.00 41.82  ? 973  ILE   A CG1 1 
ATOM   3377 C CG2 . ILE   A 1 436 ? 9.226   -4.192  -11.937 1.00 34.40  ? 973  ILE   A CG2 1 
ATOM   3378 C CD1 . ILE   A 1 436 ? 8.615   -2.409  -14.265 1.00 40.15  ? 973  ILE   A CD1 1 
ATOM   3379 N N   . GLN   A 1 437 ? 8.790   -7.705  -12.430 1.00 31.44  ? 974  GLN   A N   1 
ATOM   3380 C CA  . GLN   A 1 437 ? 8.462   -8.581  -11.318 1.00 33.71  ? 974  GLN   A CA  1 
ATOM   3381 C C   . GLN   A 1 437 ? 9.482   -9.701  -11.114 1.00 37.97  ? 974  GLN   A C   1 
ATOM   3382 O O   . GLN   A 1 437 ? 9.579   -10.233 -10.001 1.00 37.69  ? 974  GLN   A O   1 
ATOM   3383 C CB  . GLN   A 1 437 ? 7.066   -9.163  -11.531 1.00 34.67  ? 974  GLN   A CB  1 
ATOM   3384 C CG  . GLN   A 1 437 ? 5.968   -8.115  -11.469 1.00 37.00  ? 974  GLN   A CG  1 
ATOM   3385 C CD  . GLN   A 1 437 ? 4.576   -8.743  -11.498 1.00 45.43  ? 974  GLN   A CD  1 
ATOM   3386 O OE1 . GLN   A 1 437 ? 4.103   -9.188  -12.548 1.00 41.69  ? 974  GLN   A OE1 1 
ATOM   3387 N NE2 . GLN   A 1 437 ? 3.920   -8.786  -10.340 1.00 47.18  ? 974  GLN   A NE2 1 
ATOM   3388 N N   . GLN   A 1 438 ? 10.247  -10.072 -12.146 1.00 41.40  ? 975  GLN   A N   1 
ATOM   3389 C CA  . GLN   A 1 438 ? 11.205  -11.168 -11.980 1.00 45.17  ? 975  GLN   A CA  1 
ATOM   3390 C C   . GLN   A 1 438 ? 12.187  -10.905 -10.845 1.00 46.11  ? 975  GLN   A C   1 
ATOM   3391 O O   . GLN   A 1 438 ? 12.701  -11.854 -10.243 1.00 42.94  ? 975  GLN   A O   1 
ATOM   3392 C CB  . GLN   A 1 438 ? 12.014  -11.402 -13.255 1.00 51.55  ? 975  GLN   A CB  1 
ATOM   3393 C CG  . GLN   A 1 438 ? 11.247  -11.660 -14.525 1.00 63.65  ? 975  GLN   A CG  1 
ATOM   3394 C CD  . GLN   A 1 438 ? 12.187  -11.743 -15.721 1.00 84.12  ? 975  GLN   A CD  1 
ATOM   3395 O OE1 . GLN   A 1 438 ? 13.403  -11.889 -15.559 1.00 82.55  ? 975  GLN   A OE1 1 
ATOM   3396 N NE2 . GLN   A 1 438 ? 11.631  -11.639 -16.924 1.00 91.05  ? 975  GLN   A NE2 1 
ATOM   3397 N N   . TYR   A 1 439 ? 12.488  -9.632  -10.564 1.00 40.87  ? 976  TYR   A N   1 
ATOM   3398 C CA  . TYR   A 1 439 ? 13.555  -9.267  -9.641  1.00 38.97  ? 976  TYR   A CA  1 
ATOM   3399 C C   . TYR   A 1 439 ? 13.042  -8.804  -8.276  1.00 37.92  ? 976  TYR   A C   1 
ATOM   3400 O O   . TYR   A 1 439 ? 13.834  -8.326  -7.457  1.00 39.48  ? 976  TYR   A O   1 
ATOM   3401 C CB  . TYR   A 1 439 ? 14.440  -8.184  -10.273 1.00 38.95  ? 976  TYR   A CB  1 
ATOM   3402 C CG  . TYR   A 1 439 ? 15.043  -8.589  -11.611 1.00 41.79  ? 976  TYR   A CG  1 
ATOM   3403 C CD1 . TYR   A 1 439 ? 16.183  -9.390  -11.676 1.00 46.10  ? 976  TYR   A CD1 1 
ATOM   3404 C CD2 . TYR   A 1 439 ? 14.472  -8.171  -12.806 1.00 44.49  ? 976  TYR   A CD2 1 
ATOM   3405 C CE1 . TYR   A 1 439 ? 16.728  -9.762  -12.893 1.00 53.80  ? 976  TYR   A CE1 1 
ATOM   3406 C CE2 . TYR   A 1 439 ? 15.009  -8.541  -14.028 1.00 44.81  ? 976  TYR   A CE2 1 
ATOM   3407 C CZ  . TYR   A 1 439 ? 16.133  -9.337  -14.067 1.00 52.94  ? 976  TYR   A CZ  1 
ATOM   3408 O OH  . TYR   A 1 439 ? 16.668  -9.699  -15.285 1.00 58.80  ? 976  TYR   A OH  1 
ATOM   3409 N N   . GLN   A 1 440 ? 11.752  -8.973  -7.991  1.00 38.82  ? 977  GLN   A N   1 
ATOM   3410 C CA  . GLN   A 1 440 ? 11.178  -8.420  -6.771  1.00 38.02  ? 977  GLN   A CA  1 
ATOM   3411 C C   . GLN   A 1 440 ? 11.207  -9.358  -5.563  1.00 44.95  ? 977  GLN   A C   1 
ATOM   3412 O O   . GLN   A 1 440 ? 10.835  -8.929  -4.467  1.00 47.08  ? 977  GLN   A O   1 
ATOM   3413 C CB  . GLN   A 1 440 ? 9.738   -7.980  -7.030  1.00 39.04  ? 977  GLN   A CB  1 
ATOM   3414 C CG  . GLN   A 1 440 ? 9.653   -6.742  -7.911  1.00 38.04  ? 977  GLN   A CG  1 
ATOM   3415 C CD  . GLN   A 1 440 ? 8.227   -6.298  -8.135  1.00 39.24  ? 977  GLN   A CD  1 
ATOM   3416 O OE1 . GLN   A 1 440 ? 7.341   -7.126  -8.404  1.00 41.48  ? 977  GLN   A OE1 1 
ATOM   3417 N NE2 . GLN   A 1 440 ? 7.982   -4.995  -7.994  1.00 38.00  ? 977  GLN   A NE2 1 
ATOM   3418 N N   . ASN   A 1 441 ? 11.640  -10.605 -5.702  1.00 46.04  ? 978  ASN   A N   1 
ATOM   3419 C CA  . ASN   A 1 441 ? 11.664  -11.450 -4.509  1.00 61.50  ? 978  ASN   A CA  1 
ATOM   3420 C C   . ASN   A 1 441 ? 13.088  -11.841 -4.133  1.00 59.04  ? 978  ASN   A C   1 
ATOM   3421 O O   . ASN   A 1 441 ? 13.374  -13.023 -3.930  1.00 65.07  ? 978  ASN   A O   1 
ATOM   3422 C CB  . ASN   A 1 441 ? 10.821  -12.712 -4.712  1.00 71.89  ? 978  ASN   A CB  1 
ATOM   3423 C CG  . ASN   A 1 441 ? 9.429   -12.419 -5.259  1.00 87.62  ? 978  ASN   A CG  1 
ATOM   3424 O OD1 . ASN   A 1 441 ? 8.895   -11.320 -5.101  1.00 86.88  ? 978  ASN   A OD1 1 
ATOM   3425 N ND2 . ASN   A 1 441 ? 8.832   -13.420 -5.902  1.00 93.61  ? 978  ASN   A ND2 1 
ATOM   3426 N N   . GLN   A 1 442 ? 13.986  -10.863 -4.021  1.00 52.60  ? 979  GLN   A N   1 
ATOM   3427 C CA  . GLN   A 1 442 ? 15.420  -11.121 -3.871  1.00 52.27  ? 979  GLN   A CA  1 
ATOM   3428 C C   . GLN   A 1 442 ? 15.983  -10.297 -2.722  1.00 43.60  ? 979  GLN   A C   1 
ATOM   3429 O O   . GLN   A 1 442 ? 16.628  -9.263  -2.943  1.00 47.21  ? 979  GLN   A O   1 
ATOM   3430 C CB  . GLN   A 1 442 ? 16.176  -10.797 -5.160  1.00 54.63  ? 979  GLN   A CB  1 
ATOM   3431 C CG  . GLN   A 1 442 ? 15.603  -11.420 -6.417  1.00 58.63  ? 979  GLN   A CG  1 
ATOM   3432 C CD  . GLN   A 1 442 ? 16.436  -11.099 -7.641  1.00 60.10  ? 979  GLN   A CD  1 
ATOM   3433 O OE1 . GLN   A 1 442 ? 17.411  -10.345 -7.563  1.00 55.50  ? 979  GLN   A OE1 1 
ATOM   3434 N NE2 . GLN   A 1 442 ? 16.072  -11.681 -8.776  1.00 52.22  ? 979  GLN   A NE2 1 
ATOM   3435 N N   . PRO   A 1 443 ? 15.775  -10.730 -1.483  1.00 37.85  ? 980  PRO   A N   1 
ATOM   3436 C CA  . PRO   A 1 443 ? 16.263  -9.949  -0.343  1.00 35.35  ? 980  PRO   A CA  1 
ATOM   3437 C C   . PRO   A 1 443 ? 17.778  -10.001 -0.250  1.00 40.11  ? 980  PRO   A C   1 
ATOM   3438 O O   . PRO   A 1 443 ? 18.416  -10.991 -0.626  1.00 37.42  ? 980  PRO   A O   1 
ATOM   3439 C CB  . PRO   A 1 443 ? 15.610  -10.634 0.861   1.00 43.92  ? 980  PRO   A CB  1 
ATOM   3440 C CG  . PRO   A 1 443 ? 15.339  -12.029 0.391   1.00 45.00  ? 980  PRO   A CG  1 
ATOM   3441 C CD  . PRO   A 1 443 ? 15.037  -11.935 -1.066  1.00 43.36  ? 980  PRO   A CD  1 
ATOM   3442 N N   . TYR   A 1 444 ? 18.349  -8.908  0.257   1.00 32.94  ? 981  TYR   A N   1 
ATOM   3443 C CA  . TYR   A 1 444 ? 19.781  -8.790  0.479   1.00 32.40  ? 981  TYR   A CA  1 
ATOM   3444 C C   . TYR   A 1 444 ? 20.145  -9.289  1.865   1.00 33.24  ? 981  TYR   A C   1 
ATOM   3445 O O   . TYR   A 1 444 ? 19.415  -9.057  2.830   1.00 37.91  ? 981  TYR   A O   1 
ATOM   3446 C CB  . TYR   A 1 444 ? 20.231  -7.330  0.341   1.00 31.90  ? 981  TYR   A CB  1 
ATOM   3447 C CG  . TYR   A 1 444 ? 20.455  -6.898  -1.086  1.00 29.99  ? 981  TYR   A CG  1 
ATOM   3448 C CD1 . TYR   A 1 444 ? 19.400  -6.439  -1.865  1.00 29.71  ? 981  TYR   A CD1 1 
ATOM   3449 C CD2 . TYR   A 1 444 ? 21.722  -6.979  -1.663  1.00 29.89  ? 981  TYR   A CD2 1 
ATOM   3450 C CE1 . TYR   A 1 444 ? 19.593  -6.060  -3.174  1.00 29.34  ? 981  TYR   A CE1 1 
ATOM   3451 C CE2 . TYR   A 1 444 ? 21.932  -6.597  -2.979  1.00 32.32  ? 981  TYR   A CE2 1 
ATOM   3452 C CZ  . TYR   A 1 444 ? 20.863  -6.124  -3.727  1.00 31.03  ? 981  TYR   A CZ  1 
ATOM   3453 O OH  . TYR   A 1 444 ? 21.036  -5.743  -5.036  1.00 31.36  ? 981  TYR   A OH  1 
ATOM   3454 N N   . CYS   A 1 445 ? 21.296  -9.953  1.965   1.00 34.10  ? 982  CYS   A N   1 
ATOM   3455 C CA  . CYS   A 1 445 ? 21.819  -10.385 3.261   1.00 37.07  ? 982  CYS   A CA  1 
ATOM   3456 C C   . CYS   A 1 445 ? 22.590  -9.235  3.911   1.00 38.09  ? 982  CYS   A C   1 
ATOM   3457 O O   . CYS   A 1 445 ? 23.806  -9.283  4.102   1.00 35.63  ? 982  CYS   A O   1 
ATOM   3458 C CB  . CYS   A 1 445 ? 22.691  -11.623 3.100   1.00 40.21  ? 982  CYS   A CB  1 
ATOM   3459 S SG  . CYS   A 1 445 ? 23.224  -12.341 4.675   1.00 42.76  ? 982  CYS   A SG  1 
ATOM   3460 N N   . LEU   A 1 446 ? 21.847  -8.170  4.217   1.00 32.75  ? 983  LEU   A N   1 
ATOM   3461 C CA  . LEU   A 1 446 ? 22.414  -6.947  4.771   1.00 31.83  ? 983  LEU   A CA  1 
ATOM   3462 C C   . LEU   A 1 446 ? 21.516  -6.432  5.887   1.00 35.02  ? 983  LEU   A C   1 
ATOM   3463 O O   . LEU   A 1 446 ? 20.287  -6.444  5.768   1.00 36.63  ? 983  LEU   A O   1 
ATOM   3464 C CB  . LEU   A 1 446 ? 22.574  -5.870  3.695   1.00 30.24  ? 983  LEU   A CB  1 
ATOM   3465 C CG  . LEU   A 1 446 ? 23.479  -6.170  2.498   1.00 36.41  ? 983  LEU   A CG  1 
ATOM   3466 C CD1 . LEU   A 1 446 ? 23.389  -5.034  1.468   1.00 32.76  ? 983  LEU   A CD1 1 
ATOM   3467 C CD2 . LEU   A 1 446 ? 24.918  -6.361  2.943   1.00 34.54  ? 983  LEU   A CD2 1 
ATOM   3468 N N   . ARG   A 1 447 ? 22.130  -5.958  6.962   1.00 32.52  ? 984  ARG   A N   1 
ATOM   3469 C CA  . ARG   A 1 447 ? 21.381  -5.487  8.118   1.00 34.97  ? 984  ARG   A CA  1 
ATOM   3470 C C   . ARG   A 1 447 ? 20.997  -4.022  7.923   1.00 35.52  ? 984  ARG   A C   1 
ATOM   3471 O O   . ARG   A 1 447 ? 21.828  -3.213  7.504   1.00 33.65  ? 984  ARG   A O   1 
ATOM   3472 C CB  . ARG   A 1 447 ? 22.206  -5.656  9.396   1.00 41.49  ? 984  ARG   A CB  1 
ATOM   3473 C CG  . ARG   A 1 447 ? 21.403  -5.470  10.661  1.00 57.63  ? 984  ARG   A CG  1 
ATOM   3474 C CD  . ARG   A 1 447 ? 22.190  -5.901  11.892  1.00 59.72  ? 984  ARG   A CD  1 
ATOM   3475 N NE  . ARG   A 1 447 ? 22.624  -7.294  11.831  1.00 63.79  ? 984  ARG   A NE  1 
ATOM   3476 C CZ  . ARG   A 1 447 ? 21.864  -8.334  12.164  1.00 62.51  ? 984  ARG   A CZ  1 
ATOM   3477 N NH1 . ARG   A 1 447 ? 20.616  -8.151  12.574  1.00 56.81  ? 984  ARG   A NH1 1 
ATOM   3478 N NH2 . ARG   A 1 447 ? 22.351  -9.563  12.079  1.00 66.48  ? 984  ARG   A NH2 1 
ATOM   3479 N N   . ILE   A 1 448 ? 19.735  -3.688  8.228   1.00 33.17  ? 985  ILE   A N   1 
ATOM   3480 C CA  . ILE   A 1 448 ? 19.284  -2.298  8.154   1.00 34.27  ? 985  ILE   A CA  1 
ATOM   3481 C C   . ILE   A 1 448 ? 19.942  -1.485  9.263   1.00 33.28  ? 985  ILE   A C   1 
ATOM   3482 O O   . ILE   A 1 448 ? 20.090  -1.956  10.401  1.00 35.26  ? 985  ILE   A O   1 
ATOM   3483 C CB  . ILE   A 1 448 ? 17.748  -2.225  8.255   1.00 36.61  ? 985  ILE   A CB  1 
ATOM   3484 C CG1 . ILE   A 1 448 ? 17.089  -2.808  7.006   1.00 40.80  ? 985  ILE   A CG1 1 
ATOM   3485 C CG2 . ILE   A 1 448 ? 17.279  -0.791  8.440   1.00 40.29  ? 985  ILE   A CG2 1 
ATOM   3486 C CD1 . ILE   A 1 448 ? 15.569  -2.953  7.121   1.00 51.56  ? 985  ILE   A CD1 1 
ATOM   3487 N N   . GLU   A 1 449 ? 20.363  -0.264  8.933   1.00 31.94  ? 986  GLU   A N   1 
ATOM   3488 C CA  . GLU   A 1 449 ? 20.780  0.704   9.944   1.00 34.21  ? 986  GLU   A CA  1 
ATOM   3489 C C   . GLU   A 1 449 ? 19.704  1.776   10.037  1.00 32.78  ? 986  GLU   A C   1 
ATOM   3490 O O   . GLU   A 1 449 ? 19.611  2.626   9.135   1.00 31.73  ? 986  GLU   A O   1 
ATOM   3491 C CB  . GLU   A 1 449 ? 22.130  1.332   9.590   1.00 30.93  ? 986  GLU   A CB  1 
ATOM   3492 C CG  . GLU   A 1 449 ? 23.018  1.656   10.808  1.00 33.78  ? 986  GLU   A CG  1 
ATOM   3493 C CD  . GLU   A 1 449 ? 22.411  2.710   11.732  1.00 36.07  ? 986  GLU   A CD  1 
ATOM   3494 O OE1 . GLU   A 1 449 ? 22.454  2.533   12.969  1.00 37.12  ? 986  GLU   A OE1 1 
ATOM   3495 O OE2 . GLU   A 1 449 ? 21.898  3.724   11.219  1.00 37.90  ? 986  GLU   A OE2 1 
ATOM   3496 N N   . PRO   A 1 450 ? 18.884  1.791   11.097  1.00 33.64  ? 987  PRO   A N   1 
ATOM   3497 C CA  . PRO   A 1 450 ? 17.692  2.661   11.086  1.00 35.39  ? 987  PRO   A CA  1 
ATOM   3498 C C   . PRO   A 1 450 ? 18.001  4.142   10.950  1.00 32.94  ? 987  PRO   A C   1 
ATOM   3499 O O   . PRO   A 1 450 ? 17.302  4.838   10.205  1.00 35.34  ? 987  PRO   A O   1 
ATOM   3500 C CB  . PRO   A 1 450 ? 17.017  2.348   12.431  1.00 36.64  ? 987  PRO   A CB  1 
ATOM   3501 C CG  . PRO   A 1 450 ? 17.522  0.984   12.802  1.00 42.78  ? 987  PRO   A CG  1 
ATOM   3502 C CD  . PRO   A 1 450 ? 18.938  0.939   12.297  1.00 35.05  ? 987  PRO   A CD  1 
ATOM   3503 N N   . ASP   A 1 451 ? 19.020  4.650   11.648  1.00 33.62  ? 988  ASP   A N   1 
ATOM   3504 C CA  . ASP   A 1 451 ? 19.353  6.070   11.518  1.00 33.75  ? 988  ASP   A CA  1 
ATOM   3505 C C   . ASP   A 1 451 ? 19.802  6.411   10.103  1.00 34.40  ? 988  ASP   A C   1 
ATOM   3506 O O   . ASP   A 1 451 ? 19.398  7.445   9.545   1.00 33.31  ? 988  ASP   A O   1 
ATOM   3507 C CB  . ASP   A 1 451 ? 20.432  6.455   12.528  1.00 34.95  ? 988  ASP   A CB  1 
ATOM   3508 C CG  . ASP   A 1 451 ? 19.898  6.523   13.951  1.00 42.57  ? 988  ASP   A CG  1 
ATOM   3509 O OD1 . ASP   A 1 451 ? 18.699  6.823   14.116  1.00 46.97  ? 988  ASP   A OD1 1 
ATOM   3510 O OD2 . ASP   A 1 451 ? 20.673  6.288   14.901  1.00 43.34  ? 988  ASP   A OD2 1 
ATOM   3511 N N   . MET   A 1 452 ? 20.665  5.580   9.511   1.00 30.58  ? 989  MET   A N   1 
ATOM   3512 C CA  . MET   A 1 452 ? 21.092  5.847   8.138   1.00 29.21  ? 989  MET   A CA  1 
ATOM   3513 C C   . MET   A 1 452 ? 19.917  5.751   7.171   1.00 30.53  ? 989  MET   A C   1 
ATOM   3514 O O   . MET   A 1 452 ? 19.823  6.526   6.210   1.00 29.27  ? 989  MET   A O   1 
ATOM   3515 C CB  . MET   A 1 452 ? 22.209  4.884   7.732   1.00 33.05  ? 989  MET   A CB  1 
ATOM   3516 C CG  . MET   A 1 452 ? 23.477  5.031   8.550   1.00 32.61  ? 989  MET   A CG  1 
ATOM   3517 S SD  . MET   A 1 452 ? 24.833  4.000   7.932   1.00 29.93  ? 989  MET   A SD  1 
ATOM   3518 C CE  . MET   A 1 452 ? 25.008  4.587   6.240   1.00 27.16  ? 989  MET   A CE  1 
ATOM   3519 N N   . ARG   A 1 453 ? 19.007  4.810   7.405   1.00 29.60  ? 990  ARG   A N   1 
ATOM   3520 C CA  . ARG   A 1 453 ? 17.860  4.678   6.517   1.00 29.48  ? 990  ARG   A CA  1 
ATOM   3521 C C   . ARG   A 1 453 ? 17.001  5.938   6.556   1.00 32.77  ? 990  ARG   A C   1 
ATOM   3522 O O   . ARG   A 1 453 ? 16.577  6.445   5.511   1.00 34.97  ? 990  ARG   A O   1 
ATOM   3523 C CB  . ARG   A 1 453 ? 17.047  3.440   6.902   1.00 30.11  ? 990  ARG   A CB  1 
ATOM   3524 C CG  . ARG   A 1 453 ? 15.718  3.329   6.207   1.00 43.96  ? 990  ARG   A CG  1 
ATOM   3525 C CD  . ARG   A 1 453 ? 15.875  2.963   4.761   1.00 52.26  ? 990  ARG   A CD  1 
ATOM   3526 N NE  . ARG   A 1 453 ? 14.707  2.217   4.322   1.00 56.36  ? 990  ARG   A NE  1 
ATOM   3527 C CZ  . ARG   A 1 453 ? 14.674  0.901   4.127   1.00 51.06  ? 990  ARG   A CZ  1 
ATOM   3528 N NH1 . ARG   A 1 453 ? 15.762  0.165   4.301   1.00 36.22  ? 990  ARG   A NH1 1 
ATOM   3529 N NH2 . ARG   A 1 453 ? 13.543  0.323   3.739   1.00 42.20  ? 990  ARG   A NH2 1 
ATOM   3530 N N   . ARG   A 1 454 ? 16.754  6.474   7.757   1.00 32.20  ? 991  ARG   A N   1 
ATOM   3531 C CA  . ARG   A 1 454 ? 15.978  7.708   7.870   1.00 30.46  ? 991  ARG   A CA  1 
ATOM   3532 C C   . ARG   A 1 454 ? 16.681  8.867   7.175   1.00 33.20  ? 991  ARG   A C   1 
ATOM   3533 O O   . ARG   A 1 454 ? 16.036  9.694   6.521   1.00 33.95  ? 991  ARG   A O   1 
ATOM   3534 C CB  . ARG   A 1 454 ? 15.736  8.055   9.335   1.00 38.77  ? 991  ARG   A CB  1 
ATOM   3535 C CG  . ARG   A 1 454 ? 14.630  7.270   9.997   1.00 52.49  ? 991  ARG   A CG  1 
ATOM   3536 C CD  . ARG   A 1 454 ? 14.373  7.782   11.415  1.00 56.97  ? 991  ARG   A CD  1 
ATOM   3537 N NE  . ARG   A 1 454 ? 15.381  7.293   12.353  1.00 56.45  ? 991  ARG   A NE  1 
ATOM   3538 C CZ  . ARG   A 1 454 ? 15.345  6.089   12.921  1.00 65.32  ? 991  ARG   A CZ  1 
ATOM   3539 N NH1 . ARG   A 1 454 ? 14.349  5.251   12.648  1.00 63.14  ? 991  ARG   A NH1 1 
ATOM   3540 N NH2 . ARG   A 1 454 ? 16.303  5.718   13.761  1.00 64.53  ? 991  ARG   A NH2 1 
ATOM   3541 N N   . PHE   A 1 455 ? 18.009  8.939   7.312   1.00 33.73  ? 992  PHE   A N   1 
ATOM   3542 C CA  . PHE   A 1 455 ? 18.775  9.993   6.657   1.00 30.63  ? 992  PHE   A CA  1 
ATOM   3543 C C   . PHE   A 1 455 ? 18.551  9.979   5.150   1.00 29.72  ? 992  PHE   A C   1 
ATOM   3544 O O   . PHE   A 1 455 ? 18.306  11.022  4.538   1.00 32.16  ? 992  PHE   A O   1 
ATOM   3545 C CB  . PHE   A 1 455 ? 20.255  9.837   6.998   1.00 28.75  ? 992  PHE   A CB  1 
ATOM   3546 C CG  . PHE   A 1 455 ? 21.157  10.797  6.272   1.00 32.92  ? 992  PHE   A CG  1 
ATOM   3547 C CD1 . PHE   A 1 455 ? 21.293  12.103  6.709   1.00 33.58  ? 992  PHE   A CD1 1 
ATOM   3548 C CD2 . PHE   A 1 455 ? 21.877  10.388  5.159   1.00 32.70  ? 992  PHE   A CD2 1 
ATOM   3549 C CE1 . PHE   A 1 455 ? 22.127  12.987  6.051   1.00 31.65  ? 992  PHE   A CE1 1 
ATOM   3550 C CE2 . PHE   A 1 455 ? 22.705  11.274  4.489   1.00 33.42  ? 992  PHE   A CE2 1 
ATOM   3551 C CZ  . PHE   A 1 455 ? 22.827  12.577  4.942   1.00 30.39  ? 992  PHE   A CZ  1 
ATOM   3552 N N   . PHE   A 1 456 ? 18.614  8.794   4.529   1.00 27.46  ? 993  PHE   A N   1 
ATOM   3553 C CA  . PHE   A 1 456 ? 18.457  8.753   3.078   1.00 31.04  ? 993  PHE   A CA  1 
ATOM   3554 C C   . PHE   A 1 456 ? 17.001  8.922   2.655   1.00 30.73  ? 993  PHE   A C   1 
ATOM   3555 O O   . PHE   A 1 456 ? 16.737  9.417   1.550   1.00 31.29  ? 993  PHE   A O   1 
ATOM   3556 C CB  . PHE   A 1 456 ? 19.041  7.456   2.522   1.00 25.98  ? 993  PHE   A CB  1 
ATOM   3557 C CG  . PHE   A 1 456 ? 20.544  7.413   2.615   1.00 26.05  ? 993  PHE   A CG  1 
ATOM   3558 C CD1 . PHE   A 1 456 ? 21.308  8.348   1.924   1.00 29.57  ? 993  PHE   A CD1 1 
ATOM   3559 C CD2 . PHE   A 1 456 ? 21.187  6.491   3.422   1.00 27.36  ? 993  PHE   A CD2 1 
ATOM   3560 C CE1 . PHE   A 1 456 ? 22.683  8.344   2.011   1.00 28.40  ? 993  PHE   A CE1 1 
ATOM   3561 C CE2 . PHE   A 1 456 ? 22.567  6.477   3.514   1.00 33.20  ? 993  PHE   A CE2 1 
ATOM   3562 C CZ  . PHE   A 1 456 ? 23.316  7.401   2.804   1.00 29.76  ? 993  PHE   A CZ  1 
ATOM   3563 N N   . GLU   A 1 457 ? 16.048  8.537   3.513   1.00 30.30  ? 994  GLU   A N   1 
ATOM   3564 C CA  . GLU   A 1 457 ? 14.635  8.780   3.221   1.00 27.49  ? 994  GLU   A CA  1 
ATOM   3565 C C   . GLU   A 1 457 ? 14.262  10.259  3.315   1.00 38.77  ? 994  GLU   A C   1 
ATOM   3566 O O   . GLU   A 1 457 ? 13.275  10.678  2.701   1.00 59.11  ? 994  GLU   A O   1 
ATOM   3567 C CB  . GLU   A 1 457 ? 13.736  7.981   4.176   1.00 35.97  ? 994  GLU   A CB  1 
ATOM   3568 C CG  . GLU   A 1 457 ? 13.794  6.474   3.986   1.00 41.18  ? 994  GLU   A CG  1 
ATOM   3569 C CD  . GLU   A 1 457 ? 12.894  5.714   4.944   1.00 40.38  ? 994  GLU   A CD  1 
ATOM   3570 O OE1 . GLU   A 1 457 ? 12.702  6.156   6.097   1.00 37.68  ? 994  GLU   A OE1 1 
ATOM   3571 O OE2 . GLU   A 1 457 ? 12.382  4.655   4.532   1.00 41.30  ? 994  GLU   A OE2 1 
ATOM   3572 N N   . ASN   A 1 458 ? 15.021  11.052  4.069   1.00 33.43  ? 995  ASN   A N   1 
ATOM   3573 C CA  . ASN   A 1 458 ? 14.675  12.443  4.338   1.00 37.09  ? 995  ASN   A CA  1 
ATOM   3574 C C   . ASN   A 1 458 ? 15.509  13.447  3.554   1.00 35.57  ? 995  ASN   A C   1 
ATOM   3575 O O   . ASN   A 1 458 ? 15.403  14.650  3.812   1.00 37.40  ? 995  ASN   A O   1 
ATOM   3576 C CB  . ASN   A 1 458 ? 14.797  12.723  5.833   1.00 45.54  ? 995  ASN   A CB  1 
ATOM   3577 C CG  . ASN   A 1 458 ? 13.760  11.982  6.632   1.00 59.86  ? 995  ASN   A CG  1 
ATOM   3578 O OD1 . ASN   A 1 458 ? 12.646  11.766  6.159   1.00 61.52  ? 995  ASN   A OD1 1 
ATOM   3579 N ND2 . ASN   A 1 458 ? 14.120  11.568  7.840   1.00 57.62  ? 995  ASN   A ND2 1 
ATOM   3580 N N   . LEU   A 1 459 ? 16.330  12.995  2.612   1.00 31.05  ? 996  LEU   A N   1 
ATOM   3581 C CA  . LEU   A 1 459 ? 17.162  13.929  1.860   1.00 32.17  ? 996  LEU   A CA  1 
ATOM   3582 C C   . LEU   A 1 459 ? 16.298  14.965  1.155   1.00 30.67  ? 996  LEU   A C   1 
ATOM   3583 O O   . LEU   A 1 459 ? 15.286  14.628  0.542   1.00 39.02  ? 996  LEU   A O   1 
ATOM   3584 C CB  . LEU   A 1 459 ? 18.004  13.179  0.832   1.00 35.02  ? 996  LEU   A CB  1 
ATOM   3585 C CG  . LEU   A 1 459 ? 19.159  12.310  1.330   1.00 33.21  ? 996  LEU   A CG  1 
ATOM   3586 C CD1 . LEU   A 1 459 ? 19.855  11.717  0.128   1.00 30.67  ? 996  LEU   A CD1 1 
ATOM   3587 C CD2 . LEU   A 1 459 ? 20.117  13.131  2.165   1.00 37.23  ? 996  LEU   A CD2 1 
ATOM   3588 N N   . ASN   A 1 460 ? 16.713  16.229  1.223   1.00 33.04  ? 997  ASN   A N   1 
ATOM   3589 C CA  . ASN   A 1 460 ? 16.002  17.323  0.558   1.00 27.92  ? 997  ASN   A CA  1 
ATOM   3590 C C   . ASN   A 1 460 ? 17.016  18.297  -0.020  1.00 29.15  ? 997  ASN   A C   1 
ATOM   3591 O O   . ASN   A 1 460 ? 17.139  19.438  0.439   1.00 34.69  ? 997  ASN   A O   1 
ATOM   3592 C CB  . ASN   A 1 460 ? 15.064  18.035  1.528   1.00 31.18  ? 997  ASN   A CB  1 
ATOM   3593 C CG  . ASN   A 1 460 ? 14.313  19.177  0.870   1.00 30.67  ? 997  ASN   A CG  1 
ATOM   3594 O OD1 . ASN   A 1 460 ? 13.789  19.038  -0.230  1.00 38.37  ? 997  ASN   A OD1 1 
ATOM   3595 N ND2 . ASN   A 1 460 ? 14.283  20.326  1.538   1.00 42.86  ? 997  ASN   A ND2 1 
ATOM   3596 N N   . PRO   A 1 461 ? 17.734  17.887  -1.063  1.00 25.64  ? 998  PRO   A N   1 
ATOM   3597 C CA  . PRO   A 1 461 ? 18.799  18.746  -1.595  1.00 26.89  ? 998  PRO   A CA  1 
ATOM   3598 C C   . PRO   A 1 461 ? 18.301  20.108  -2.047  1.00 26.69  ? 998  PRO   A C   1 
ATOM   3599 O O   . PRO   A 1 461 ? 19.049  21.085  -1.936  1.00 30.15  ? 998  PRO   A O   1 
ATOM   3600 C CB  . PRO   A 1 461 ? 19.358  17.928  -2.768  1.00 27.14  ? 998  PRO   A CB  1 
ATOM   3601 C CG  . PRO   A 1 461 ? 18.276  16.901  -3.077  1.00 28.22  ? 998  PRO   A CG  1 
ATOM   3602 C CD  . PRO   A 1 461 ? 17.636  16.602  -1.784  1.00 28.44  ? 998  PRO   A CD  1 
ATOM   3603 N N   . MET   A 1 462 ? 17.048  20.211  -2.502  1.00 30.17  ? 999  MET   A N   1 
ATOM   3604 C CA  . MET   A 1 462 ? 16.554  21.466  -3.070  1.00 32.94  ? 999  MET   A CA  1 
ATOM   3605 C C   . MET   A 1 462 ? 16.293  22.546  -2.024  1.00 34.66  ? 999  MET   A C   1 
ATOM   3606 O O   . MET   A 1 462 ? 16.124  23.716  -2.394  1.00 31.53  ? 999  MET   A O   1 
ATOM   3607 C CB  . MET   A 1 462 ? 15.277  21.213  -3.882  1.00 34.81  ? 999  MET   A CB  1 
ATOM   3608 C CG  . MET   A 1 462 ? 15.507  20.313  -5.094  1.00 48.68  ? 999  MET   A CG  1 
ATOM   3609 S SD  . MET   A 1 462 ? 14.147  20.420  -6.283  1.00 55.53  ? 999  MET   A SD  1 
ATOM   3610 C CE  . MET   A 1 462 ? 13.740  18.681  -6.461  1.00 56.25  ? 999  MET   A CE  1 
ATOM   3611 N N   . GLY   A 1 463 ? 16.278  22.200  -0.740  1.00 32.13  ? 1000 GLY   A N   1 
ATOM   3612 C CA  . GLY   A 1 463 ? 15.880  23.184  0.257   1.00 31.23  ? 1000 GLY   A CA  1 
ATOM   3613 C C   . GLY   A 1 463 ? 14.481  23.705  -0.041  1.00 33.11  ? 1000 GLY   A C   1 
ATOM   3614 O O   . GLY   A 1 463 ? 13.541  22.936  -0.258  1.00 35.71  ? 1000 GLY   A O   1 
ATOM   3615 N N   . SER   A 1 464 ? 14.347  25.032  -0.088  1.00 33.61  ? 1001 SER   A N   1 
ATOM   3616 C CA  . SER   A 1 464 ? 13.097  25.701  -0.448  1.00 34.80  ? 1001 SER   A CA  1 
ATOM   3617 C C   . SER   A 1 464 ? 13.051  26.125  -1.911  1.00 35.36  ? 1001 SER   A C   1 
ATOM   3618 O O   . SER   A 1 464 ? 12.073  26.745  -2.341  1.00 35.62  ? 1001 SER   A O   1 
ATOM   3619 C CB  . SER   A 1 464 ? 12.899  26.923  0.441   1.00 36.96  ? 1001 SER   A CB  1 
ATOM   3620 O OG  . SER   A 1 464 ? 12.622  26.521  1.769   1.00 44.92  ? 1001 SER   A OG  1 
ATOM   3621 N N   . ALA   A 1 465 ? 14.085  25.818  -2.683  1.00 35.55  ? 1002 ALA   A N   1 
ATOM   3622 C CA  . ALA   A 1 465 ? 14.089  26.162  -4.093  1.00 37.95  ? 1002 ALA   A CA  1 
ATOM   3623 C C   . ALA   A 1 465 ? 13.167  25.233  -4.875  1.00 32.92  ? 1002 ALA   A C   1 
ATOM   3624 O O   . ALA   A 1 465 ? 12.955  24.074  -4.507  1.00 36.15  ? 1002 ALA   A O   1 
ATOM   3625 C CB  . ALA   A 1 465 ? 15.514  26.081  -4.657  1.00 32.33  ? 1002 ALA   A CB  1 
ATOM   3626 N N   . SER   A 1 466 ? 12.604  25.759  -5.959  1.00 38.43  ? 1003 SER   A N   1 
ATOM   3627 C CA  . SER   A 1 466 ? 11.998  24.894  -6.955  1.00 36.28  ? 1003 SER   A CA  1 
ATOM   3628 C C   . SER   A 1 466 ? 13.092  24.129  -7.695  1.00 38.15  ? 1003 SER   A C   1 
ATOM   3629 O O   . SER   A 1 466 ? 14.286  24.433  -7.582  1.00 36.59  ? 1003 SER   A O   1 
ATOM   3630 C CB  . SER   A 1 466 ? 11.174  25.711  -7.947  1.00 38.89  ? 1003 SER   A CB  1 
ATOM   3631 O OG  . SER   A 1 466 ? 12.036  26.496  -8.760  1.00 47.13  ? 1003 SER   A OG  1 
ATOM   3632 N N   . GLU   A 1 467 ? 12.681  23.137  -8.488  1.00 44.63  ? 1004 GLU   A N   1 
ATOM   3633 C CA  . GLU   A 1 467 ? 13.678  22.374  -9.236  1.00 38.39  ? 1004 GLU   A CA  1 
ATOM   3634 C C   . GLU   A 1 467 ? 14.433  23.269  -10.211 1.00 33.84  ? 1004 GLU   A C   1 
ATOM   3635 O O   . GLU   A 1 467 ? 15.658  23.155  -10.348 1.00 37.55  ? 1004 GLU   A O   1 
ATOM   3636 C CB  . GLU   A 1 467 ? 13.027  21.193  -9.964  1.00 53.93  ? 1004 GLU   A CB  1 
ATOM   3637 C CG  . GLU   A 1 467 ? 14.049  20.128  -10.404 1.00 69.85  ? 1004 GLU   A CG  1 
ATOM   3638 C CD  . GLU   A 1 467 ? 13.429  18.785  -10.763 1.00 85.78  ? 1004 GLU   A CD  1 
ATOM   3639 O OE1 . GLU   A 1 467 ? 12.346  18.770  -11.387 1.00 93.93  ? 1004 GLU   A OE1 1 
ATOM   3640 O OE2 . GLU   A 1 467 ? 14.034  17.744  -10.426 1.00 85.87  ? 1004 GLU   A OE2 1 
ATOM   3641 N N   . LYS   A 1 468 ? 13.726  24.179  -10.880 1.00 43.51  ? 1005 LYS   A N   1 
ATOM   3642 C CA  . LYS   A 1 468 ? 14.384  25.097  -11.803 1.00 41.30  ? 1005 LYS   A CA  1 
ATOM   3643 C C   . LYS   A 1 468 ? 15.340  26.024  -11.062 1.00 42.66  ? 1005 LYS   A C   1 
ATOM   3644 O O   . LYS   A 1 468 ? 16.482  26.226  -11.489 1.00 38.01  ? 1005 LYS   A O   1 
ATOM   3645 C CB  . LYS   A 1 468 ? 13.343  25.908  -12.572 1.00 43.79  ? 1005 LYS   A CB  1 
ATOM   3646 C CG  . LYS   A 1 468 ? 13.931  26.876  -13.588 1.00 52.06  ? 1005 LYS   A CG  1 
ATOM   3647 C CD  . LYS   A 1 468 ? 14.983  26.177  -14.442 1.00 63.20  ? 1005 LYS   A CD  1 
ATOM   3648 C CE  . LYS   A 1 468 ? 15.351  26.990  -15.674 1.00 71.29  ? 1005 LYS   A CE  1 
ATOM   3649 N NZ  . LYS   A 1 468 ? 16.549  26.421  -16.354 1.00 71.12  ? 1005 LYS   A NZ  1 
ATOM   3650 N N   . GLU   A 1 469 ? 14.877  26.618  -9.955  1.00 35.03  ? 1006 GLU   A N   1 
ATOM   3651 C CA  . GLU   A 1 469 ? 15.759  27.434  -9.128  1.00 34.75  ? 1006 GLU   A CA  1 
ATOM   3652 C C   . GLU   A 1 469 ? 16.981  26.646  -8.691  1.00 34.66  ? 1006 GLU   A C   1 
ATOM   3653 O O   . GLU   A 1 469 ? 18.117  27.135  -8.772  1.00 35.10  ? 1006 GLU   A O   1 
ATOM   3654 C CB  . GLU   A 1 469 ? 15.002  27.948  -7.907  1.00 36.31  ? 1006 GLU   A CB  1 
ATOM   3655 C CG  . GLU   A 1 469 ? 14.080  29.108  -8.213  1.00 38.35  ? 1006 GLU   A CG  1 
ATOM   3656 C CD  . GLU   A 1 469 ? 13.180  29.443  -7.046  1.00 41.19  ? 1006 GLU   A CD  1 
ATOM   3657 O OE1 . GLU   A 1 469 ? 13.063  28.599  -6.133  1.00 40.16  ? 1006 GLU   A OE1 1 
ATOM   3658 O OE2 . GLU   A 1 469 ? 12.600  30.550  -7.046  1.00 42.22  ? 1006 GLU   A OE2 1 
ATOM   3659 N N   . PHE   A 1 470 ? 16.768  25.416  -8.216  1.00 32.39  ? 1007 PHE   A N   1 
ATOM   3660 C CA  . PHE   A 1 470 ? 17.890  24.641  -7.696  1.00 30.90  ? 1007 PHE   A CA  1 
ATOM   3661 C C   . PHE   A 1 470 ? 18.882  24.294  -8.802  1.00 32.64  ? 1007 PHE   A C   1 
ATOM   3662 O O   . PHE   A 1 470 ? 20.101  24.398  -8.610  1.00 31.88  ? 1007 PHE   A O   1 
ATOM   3663 C CB  . PHE   A 1 470 ? 17.385  23.373  -7.006  1.00 30.87  ? 1007 PHE   A CB  1 
ATOM   3664 C CG  . PHE   A 1 470 ? 18.463  22.634  -6.285  1.00 32.16  ? 1007 PHE   A CG  1 
ATOM   3665 C CD1 . PHE   A 1 470 ? 19.138  23.233  -5.225  1.00 42.35  ? 1007 PHE   A CD1 1 
ATOM   3666 C CD2 . PHE   A 1 470 ? 18.842  21.366  -6.685  1.00 37.71  ? 1007 PHE   A CD2 1 
ATOM   3667 C CE1 . PHE   A 1 470 ? 20.166  22.563  -4.570  1.00 36.19  ? 1007 PHE   A CE1 1 
ATOM   3668 C CE2 . PHE   A 1 470 ? 19.869  20.697  -6.031  1.00 35.37  ? 1007 PHE   A CE2 1 
ATOM   3669 C CZ  . PHE   A 1 470 ? 20.515  21.297  -4.972  1.00 34.27  ? 1007 PHE   A CZ  1 
ATOM   3670 N N   . THR   A 1 471 ? 18.373  23.890  -9.967  1.00 33.96  ? 1008 THR   A N   1 
ATOM   3671 C CA  . THR   A 1 471 ? 19.235  23.599  -11.110 1.00 38.73  ? 1008 THR   A CA  1 
ATOM   3672 C C   . THR   A 1 471 ? 20.058  24.817  -11.509 1.00 34.05  ? 1008 THR   A C   1 
ATOM   3673 O O   . THR   A 1 471 ? 21.258  24.700  -11.784 1.00 34.95  ? 1008 THR   A O   1 
ATOM   3674 C CB  . THR   A 1 471 ? 18.380  23.127  -12.288 1.00 44.19  ? 1008 THR   A CB  1 
ATOM   3675 O OG1 . THR   A 1 471 ? 17.830  21.839  -11.988 1.00 57.09  ? 1008 THR   A OG1 1 
ATOM   3676 C CG2 . THR   A 1 471 ? 19.214  23.024  -13.547 1.00 56.32  ? 1008 THR   A CG2 1 
ATOM   3677 N N   . ASP   A 1 472 ? 19.428  25.996  -11.551 1.00 33.64  ? 1009 ASP   A N   1 
ATOM   3678 C CA  . ASP   A 1 472 ? 20.169  27.218  -11.864 1.00 32.53  ? 1009 ASP   A CA  1 
ATOM   3679 C C   . ASP   A 1 472 ? 21.194  27.533  -10.780 1.00 37.17  ? 1009 ASP   A C   1 
ATOM   3680 O O   . ASP   A 1 472 ? 22.317  27.961  -11.082 1.00 37.28  ? 1009 ASP   A O   1 
ATOM   3681 C CB  . ASP   A 1 472 ? 19.208  28.399  -12.046 1.00 38.79  ? 1009 ASP   A CB  1 
ATOM   3682 C CG  . ASP   A 1 472 ? 18.343  28.271  -13.291 1.00 47.76  ? 1009 ASP   A CG  1 
ATOM   3683 O OD1 . ASP   A 1 472 ? 18.531  27.310  -14.067 1.00 50.17  ? 1009 ASP   A OD1 1 
ATOM   3684 O OD2 . ASP   A 1 472 ? 17.458  29.132  -13.483 1.00 47.56  ? 1009 ASP   A OD2 1 
ATOM   3685 N N   . TYR   A 1 473 ? 20.828  27.320  -9.514  1.00 32.62  ? 1010 TYR   A N   1 
ATOM   3686 C CA  . TYR   A 1 473 ? 21.767  27.532  -8.415  1.00 31.33  ? 1010 TYR   A CA  1 
ATOM   3687 C C   . TYR   A 1 473 ? 23.016  26.668  -8.577  1.00 32.56  ? 1010 TYR   A C   1 
ATOM   3688 O O   . TYR   A 1 473 ? 24.143  27.157  -8.429  1.00 29.10  ? 1010 TYR   A O   1 
ATOM   3689 C CB  . TYR   A 1 473 ? 21.080  27.249  -7.076  1.00 30.61  ? 1010 TYR   A CB  1 
ATOM   3690 C CG  . TYR   A 1 473 ? 22.029  26.906  -5.948  1.00 31.08  ? 1010 TYR   A CG  1 
ATOM   3691 C CD1 . TYR   A 1 473 ? 22.735  27.904  -5.275  1.00 43.60  ? 1010 TYR   A CD1 1 
ATOM   3692 C CD2 . TYR   A 1 473 ? 22.217  25.588  -5.557  1.00 33.76  ? 1010 TYR   A CD2 1 
ATOM   3693 C CE1 . TYR   A 1 473 ? 23.605  27.595  -4.244  1.00 39.77  ? 1010 TYR   A CE1 1 
ATOM   3694 C CE2 . TYR   A 1 473 ? 23.081  25.265  -4.530  1.00 37.74  ? 1010 TYR   A CE2 1 
ATOM   3695 C CZ  . TYR   A 1 473 ? 23.768  26.278  -3.869  1.00 41.12  ? 1010 TYR   A CZ  1 
ATOM   3696 O OH  . TYR   A 1 473 ? 24.630  25.961  -2.841  1.00 43.09  ? 1010 TYR   A OH  1 
ATOM   3697 N N   . LEU   A 1 474 ? 22.831  25.376  -8.878  1.00 32.47  ? 1011 LEU   A N   1 
ATOM   3698 C CA  . LEU   A 1 474 ? 23.969  24.469  -9.035  1.00 31.98  ? 1011 LEU   A CA  1 
ATOM   3699 C C   . LEU   A 1 474 ? 24.869  24.899  -10.179 1.00 35.16  ? 1011 LEU   A C   1 
ATOM   3700 O O   . LEU   A 1 474 ? 26.100  24.814  -10.079 1.00 27.02  ? 1011 LEU   A O   1 
ATOM   3701 C CB  . LEU   A 1 474 ? 23.487  23.039  -9.283  1.00 29.58  ? 1011 LEU   A CB  1 
ATOM   3702 C CG  . LEU   A 1 474 ? 22.745  22.319  -8.165  1.00 39.22  ? 1011 LEU   A CG  1 
ATOM   3703 C CD1 . LEU   A 1 474 ? 22.309  20.946  -8.625  1.00 40.34  ? 1011 LEU   A CD1 1 
ATOM   3704 C CD2 . LEU   A 1 474 ? 23.612  22.222  -6.936  1.00 38.68  ? 1011 LEU   A CD2 1 
ATOM   3705 N N   . PHE   A 1 475 ? 24.284  25.328  -11.297 1.00 33.44  ? 1012 PHE   A N   1 
ATOM   3706 C CA  . PHE   A 1 475 ? 25.140  25.720  -12.408 1.00 36.35  ? 1012 PHE   A CA  1 
ATOM   3707 C C   . PHE   A 1 475 ? 25.929  26.978  -12.064 1.00 33.52  ? 1012 PHE   A C   1 
ATOM   3708 O O   . PHE   A 1 475 ? 27.114  27.084  -12.403 1.00 31.47  ? 1012 PHE   A O   1 
ATOM   3709 C CB  . PHE   A 1 475 ? 24.332  25.933  -13.687 1.00 32.09  ? 1012 PHE   A CB  1 
ATOM   3710 C CG  . PHE   A 1 475 ? 25.196  26.125  -14.897 1.00 36.23  ? 1012 PHE   A CG  1 
ATOM   3711 C CD1 . PHE   A 1 475 ? 25.928  25.064  -15.403 1.00 38.96  ? 1012 PHE   A CD1 1 
ATOM   3712 C CD2 . PHE   A 1 475 ? 25.313  27.367  -15.503 1.00 39.79  ? 1012 PHE   A CD2 1 
ATOM   3713 C CE1 . PHE   A 1 475 ? 26.751  25.232  -16.511 1.00 45.43  ? 1012 PHE   A CE1 1 
ATOM   3714 C CE2 . PHE   A 1 475 ? 26.127  27.540  -16.609 1.00 42.32  ? 1012 PHE   A CE2 1 
ATOM   3715 C CZ  . PHE   A 1 475 ? 26.845  26.473  -17.113 1.00 38.36  ? 1012 PHE   A CZ  1 
ATOM   3716 N N   . ASN   A 1 476 ? 25.292  27.939  -11.389 1.00 31.64  ? 1013 ASN   A N   1 
ATOM   3717 C CA  . ASN   A 1 476 ? 26.010  29.145  -11.000 1.00 36.48  ? 1013 ASN   A CA  1 
ATOM   3718 C C   . ASN   A 1 476 ? 27.132  28.823  -10.030 1.00 33.07  ? 1013 ASN   A C   1 
ATOM   3719 O O   . ASN   A 1 476 ? 28.201  29.446  -10.075 1.00 32.08  ? 1013 ASN   A O   1 
ATOM   3720 C CB  . ASN   A 1 476 ? 25.048  30.157  -10.385 1.00 36.97  ? 1013 ASN   A CB  1 
ATOM   3721 C CG  . ASN   A 1 476 ? 24.127  30.755  -11.413 1.00 43.54  ? 1013 ASN   A CG  1 
ATOM   3722 O OD1 . ASN   A 1 476 ? 24.489  30.858  -12.588 1.00 43.13  ? 1013 ASN   A OD1 1 
ATOM   3723 N ND2 . ASN   A 1 476 ? 22.929  31.151  -10.988 1.00 51.92  ? 1013 ASN   A ND2 1 
ATOM   3724 N N   . LYS   A 1 477 ? 26.904  27.852  -9.144  1.00 29.63  ? 1014 LYS   A N   1 
ATOM   3725 C CA  . LYS   A 1 477 ? 27.945  27.443  -8.212  1.00 36.41  ? 1014 LYS   A CA  1 
ATOM   3726 C C   . LYS   A 1 477 ? 29.085  26.756  -8.954  1.00 31.50  ? 1014 LYS   A C   1 
ATOM   3727 O O   . LYS   A 1 477 ? 30.263  27.015  -8.678  1.00 29.76  ? 1014 LYS   A O   1 
ATOM   3728 C CB  . LYS   A 1 477 ? 27.337  26.534  -7.145  1.00 30.20  ? 1014 LYS   A CB  1 
ATOM   3729 C CG  . LYS   A 1 477 ? 28.299  26.075  -6.073  1.00 32.23  ? 1014 LYS   A CG  1 
ATOM   3730 C CD  . LYS   A 1 477 ? 28.929  27.232  -5.322  1.00 32.91  ? 1014 LYS   A CD  1 
ATOM   3731 C CE  . LYS   A 1 477 ? 27.908  27.973  -4.484  1.00 43.18  ? 1014 LYS   A CE  1 
ATOM   3732 N NZ  . LYS   A 1 477 ? 28.590  28.955  -3.586  1.00 42.34  ? 1014 LYS   A NZ  1 
ATOM   3733 N N   . SER   A 1 478 ? 28.744  25.907  -9.930  1.00 29.21  ? 1015 SER   A N   1 
ATOM   3734 C CA  . SER   A 1 478 ? 29.749  25.315  -10.809 1.00 30.47  ? 1015 SER   A CA  1 
ATOM   3735 C C   . SER   A 1 478 ? 30.619  26.390  -11.450 1.00 34.69  ? 1015 SER   A C   1 
ATOM   3736 O O   . SER   A 1 478 ? 31.849  26.299  -11.437 1.00 31.01  ? 1015 SER   A O   1 
ATOM   3737 C CB  . SER   A 1 478 ? 29.060  24.467  -11.883 1.00 31.02  ? 1015 SER   A CB  1 
ATOM   3738 O OG  . SER   A 1 478 ? 29.987  23.834  -12.751 1.00 28.31  ? 1015 SER   A OG  1 
ATOM   3739 N N   . LEU   A 1 479 ? 29.989  27.426  -12.000 1.00 30.97  ? 1016 LEU   A N   1 
ATOM   3740 C CA  . LEU   A 1 479 ? 30.746  28.522  -12.607 1.00 32.93  ? 1016 LEU   A CA  1 
ATOM   3741 C C   . LEU   A 1 479 ? 31.635  29.227  -11.585 1.00 34.69  ? 1016 LEU   A C   1 
ATOM   3742 O O   . LEU   A 1 479 ? 32.736  29.686  -11.920 1.00 38.53  ? 1016 LEU   A O   1 
ATOM   3743 C CB  . LEU   A 1 479 ? 29.784  29.523  -13.252 1.00 34.02  ? 1016 LEU   A CB  1 
ATOM   3744 C CG  . LEU   A 1 479 ? 29.066  29.059  -14.520 1.00 36.11  ? 1016 LEU   A CG  1 
ATOM   3745 C CD1 . LEU   A 1 479 ? 28.113  30.133  -15.046 1.00 37.45  ? 1016 LEU   A CD1 1 
ATOM   3746 C CD2 . LEU   A 1 479 ? 30.060  28.684  -15.593 1.00 43.26  ? 1016 LEU   A CD2 1 
ATOM   3747 N N   . GLU   A 1 480 ? 31.164  29.347  -10.339 1.00 35.61  ? 1017 GLU   A N   1 
ATOM   3748 C CA  . GLU   A 1 480 ? 31.949  30.009  -9.300  1.00 35.53  ? 1017 GLU   A CA  1 
ATOM   3749 C C   . GLU   A 1 480 ? 33.188  29.193  -8.927  1.00 35.46  ? 1017 GLU   A C   1 
ATOM   3750 O O   . GLU   A 1 480 ? 34.276  29.753  -8.749  1.00 38.79  ? 1017 GLU   A O   1 
ATOM   3751 C CB  . GLU   A 1 480 ? 31.070  30.245  -8.068  1.00 40.50  ? 1017 GLU   A CB  1 
ATOM   3752 C CG  . GLU   A 1 480 ? 31.780  30.954  -6.912  1.00 49.14  ? 1017 GLU   A CG  1 
ATOM   3753 C CD  . GLU   A 1 480 ? 30.901  31.082  -5.675  1.00 54.64  ? 1017 GLU   A CD  1 
ATOM   3754 O OE1 . GLU   A 1 480 ? 29.780  30.524  -5.684  1.00 44.50  ? 1017 GLU   A OE1 1 
ATOM   3755 O OE2 . GLU   A 1 480 ? 31.332  31.733  -4.695  1.00 50.16  ? 1017 GLU   A OE2 1 
ATOM   3756 N N   . ILE   A 1 481 ? 33.044  27.871  -8.803  1.00 37.29  ? 1018 ILE   A N   1 
ATOM   3757 C CA  . ILE   A 1 481 ? 34.129  27.049  -8.265  1.00 32.45  ? 1018 ILE   A CA  1 
ATOM   3758 C C   . ILE   A 1 481 ? 35.146  26.681  -9.337  1.00 34.41  ? 1018 ILE   A C   1 
ATOM   3759 O O   . ILE   A 1 481 ? 36.323  26.451  -9.020  1.00 33.53  ? 1018 ILE   A O   1 
ATOM   3760 C CB  . ILE   A 1 481 ? 33.561  25.796  -7.573  1.00 35.82  ? 1018 ILE   A CB  1 
ATOM   3761 C CG1 . ILE   A 1 481 ? 32.803  24.899  -8.567  1.00 29.44  ? 1018 ILE   A CG1 1 
ATOM   3762 C CG2 . ILE   A 1 481 ? 32.683  26.201  -6.394  1.00 33.32  ? 1018 ILE   A CG2 1 
ATOM   3763 C CD1 . ILE   A 1 481 ? 32.209  23.584  -7.935  1.00 26.78  ? 1018 ILE   A CD1 1 
ATOM   3764 N N   . GLU   A 1 482 ? 34.733  26.615  -10.603 1.00 32.45  ? 1019 GLU   A N   1 
ATOM   3765 C CA  . GLU   A 1 482 ? 35.654  26.449  -11.726 1.00 33.82  ? 1019 GLU   A CA  1 
ATOM   3766 C C   . GLU   A 1 482 ? 35.214  27.393  -12.829 1.00 37.41  ? 1019 GLU   A C   1 
ATOM   3767 O O   . GLU   A 1 482 ? 34.479  27.009  -13.744 1.00 37.02  ? 1019 GLU   A O   1 
ATOM   3768 C CB  . GLU   A 1 482 ? 35.692  24.995  -12.217 1.00 32.74  ? 1019 GLU   A CB  1 
ATOM   3769 C CG  . GLU   A 1 482 ? 36.524  24.101  -11.317 1.00 37.17  ? 1019 GLU   A CG  1 
ATOM   3770 C CD  . GLU   A 1 482 ? 36.680  22.669  -11.822 1.00 34.23  ? 1019 GLU   A CD  1 
ATOM   3771 O OE1 . GLU   A 1 482 ? 36.645  22.426  -13.051 1.00 32.32  ? 1019 GLU   A OE1 1 
ATOM   3772 O OE2 . GLU   A 1 482 ? 36.857  21.784  -10.967 1.00 30.31  ? 1019 GLU   A OE2 1 
ATOM   3773 N N   . PRO   A 1 483 ? 35.632  28.653  -12.765 1.00 37.18  ? 1020 PRO   A N   1 
ATOM   3774 C CA  . PRO   A 1 483 ? 35.203  29.610  -13.787 1.00 38.81  ? 1020 PRO   A CA  1 
ATOM   3775 C C   . PRO   A 1 483 ? 35.708  29.197  -15.157 1.00 46.92  ? 1020 PRO   A C   1 
ATOM   3776 O O   . PRO   A 1 483 ? 36.717  28.499  -15.288 1.00 43.39  ? 1020 PRO   A O   1 
ATOM   3777 C CB  . PRO   A 1 483 ? 35.827  30.931  -13.321 1.00 42.97  ? 1020 PRO   A CB  1 
ATOM   3778 C CG  . PRO   A 1 483 ? 35.962  30.759  -11.827 1.00 46.77  ? 1020 PRO   A CG  1 
ATOM   3779 C CD  . PRO   A 1 483 ? 36.359  29.308  -11.666 1.00 41.39  ? 1020 PRO   A CD  1 
ATOM   3780 N N   . ARG   A 1 484 ? 34.973  29.621  -16.182 1.00 41.82  ? 1021 ARG   A N   1 
ATOM   3781 C CA  . ARG   A 1 484 ? 35.362  29.339  -17.556 1.00 53.32  ? 1021 ARG   A CA  1 
ATOM   3782 C C   . ARG   A 1 484 ? 36.796  29.773  -17.812 1.00 54.17  ? 1021 ARG   A C   1 
ATOM   3783 O O   . ARG   A 1 484 ? 37.203  30.868  -17.422 1.00 52.59  ? 1021 ARG   A O   1 
ATOM   3784 C CB  . ARG   A 1 484 ? 34.421  30.059  -18.519 1.00 56.72  ? 1021 ARG   A CB  1 
ATOM   3785 C CG  . ARG   A 1 484 ? 33.449  29.136  -19.190 1.00 59.29  ? 1021 ARG   A CG  1 
ATOM   3786 C CD  . ARG   A 1 484 ? 32.104  29.794  -19.347 1.00 61.61  ? 1021 ARG   A CD  1 
ATOM   3787 N NE  . ARG   A 1 484 ? 31.066  28.791  -19.551 1.00 66.09  ? 1021 ARG   A NE  1 
ATOM   3788 C CZ  . ARG   A 1 484 ? 29.789  28.980  -19.243 1.00 76.08  ? 1021 ARG   A CZ  1 
ATOM   3789 N NH1 . ARG   A 1 484 ? 29.402  30.134  -18.715 1.00 85.25  ? 1021 ARG   A NH1 1 
ATOM   3790 N NH2 . ARG   A 1 484 ? 28.907  28.018  -19.465 1.00 70.49  ? 1021 ARG   A NH2 1 
ATOM   3791 N N   . ASN   A 1 485 ? 37.567  28.883  -18.431 1.00 57.38  ? 1022 ASN   A N   1 
ATOM   3792 C CA  . ASN   A 1 485 ? 38.933  29.155  -18.858 1.00 60.51  ? 1022 ASN   A CA  1 
ATOM   3793 C C   . ASN   A 1 485 ? 39.879  29.466  -17.694 1.00 62.84  ? 1022 ASN   A C   1 
ATOM   3794 O O   . ASN   A 1 485 ? 40.944  30.046  -17.905 1.00 63.93  ? 1022 ASN   A O   1 
ATOM   3795 C CB  . ASN   A 1 485 ? 38.969  30.298  -19.883 1.00 69.60  ? 1022 ASN   A CB  1 
ATOM   3796 C CG  . ASN   A 1 485 ? 38.036  30.062  -21.068 1.00 69.83  ? 1022 ASN   A CG  1 
ATOM   3797 O OD1 . ASN   A 1 485 ? 37.166  30.886  -21.360 1.00 75.42  ? 1022 ASN   A OD1 1 
ATOM   3798 N ND2 . ASN   A 1 485 ? 38.224  28.946  -21.761 1.00 65.30  ? 1022 ASN   A ND2 1 
ATOM   3799 N N   . CYS   A 1 486 ? 39.534  29.108  -16.457 1.00 55.18  ? 1023 CYS   A N   1 
ATOM   3800 C CA  . CYS   A 1 486 ? 40.506  29.224  -15.377 1.00 59.39  ? 1023 CYS   A CA  1 
ATOM   3801 C C   . CYS   A 1 486 ? 41.576  28.155  -15.560 1.00 64.16  ? 1023 CYS   A C   1 
ATOM   3802 O O   . CYS   A 1 486 ? 41.265  26.990  -15.823 1.00 71.21  ? 1023 CYS   A O   1 
ATOM   3803 C CB  . CYS   A 1 486 ? 39.832  29.092  -14.008 1.00 58.92  ? 1023 CYS   A CB  1 
ATOM   3804 S SG  . CYS   A 1 486 ? 39.117  27.447  -13.619 1.00 49.73  ? 1023 CYS   A SG  1 
ATOM   3805 N N   . LYS   A 1 487 ? 42.842  28.553  -15.470 1.00 61.21  ? 1024 LYS   A N   1 
ATOM   3806 C CA  . LYS   A 1 487 ? 43.898  27.569  -15.661 1.00 65.73  ? 1024 LYS   A CA  1 
ATOM   3807 C C   . LYS   A 1 487 ? 44.090  26.693  -14.429 1.00 66.94  ? 1024 LYS   A C   1 
ATOM   3808 O O   . LYS   A 1 487 ? 44.642  25.594  -14.550 1.00 70.01  ? 1024 LYS   A O   1 
ATOM   3809 C CB  . LYS   A 1 487 ? 45.201  28.269  -16.062 1.00 83.17  ? 1024 LYS   A CB  1 
ATOM   3810 C CG  . LYS   A 1 487 ? 45.062  29.170  -17.307 1.00 92.93  ? 1024 LYS   A CG  1 
ATOM   3811 C CD  . LYS   A 1 487 ? 45.547  28.497  -18.597 1.00 97.91  ? 1024 LYS   A CD  1 
ATOM   3812 C CE  . LYS   A 1 487 ? 45.150  29.302  -19.838 1.00 101.01 ? 1024 LYS   A CE  1 
ATOM   3813 N NZ  . LYS   A 1 487 ? 44.539  28.438  -20.894 1.00 101.65 ? 1024 LYS   A NZ  1 
ATOM   3814 N N   . GLN   A 1 488 ? 43.623  27.139  -13.262 1.00 57.46  ? 1025 GLN   A N   1 
ATOM   3815 C CA  . GLN   A 1 488 ? 43.518  26.308  -12.069 1.00 61.53  ? 1025 GLN   A CA  1 
ATOM   3816 C C   . GLN   A 1 488 ? 42.282  26.758  -11.302 1.00 46.46  ? 1025 GLN   A C   1 
ATOM   3817 O O   . GLN   A 1 488 ? 41.866  27.914  -11.434 1.00 50.02  ? 1025 GLN   A O   1 
ATOM   3818 C CB  . GLN   A 1 488 ? 44.772  26.403  -11.187 1.00 67.01  ? 1025 GLN   A CB  1 
ATOM   3819 C CG  . GLN   A 1 488 ? 44.774  27.538  -10.169 1.00 78.70  ? 1025 GLN   A CG  1 
ATOM   3820 C CD  . GLN   A 1 488 ? 46.172  27.855  -9.661  1.00 98.20  ? 1025 GLN   A CD  1 
ATOM   3821 O OE1 . GLN   A 1 488 ? 47.163  27.672  -10.368 1.00 109.25 ? 1025 GLN   A OE1 1 
ATOM   3822 N NE2 . GLN   A 1 488 ? 46.255  28.334  -8.424  1.00 100.26 ? 1025 GLN   A NE2 1 
ATOM   3823 N N   . PRO   A 1 489 ? 41.661  25.877  -10.521 1.00 43.69  ? 1026 PRO   A N   1 
ATOM   3824 C CA  . PRO   A 1 489 ? 40.495  26.287  -9.733  1.00 45.03  ? 1026 PRO   A CA  1 
ATOM   3825 C C   . PRO   A 1 489 ? 40.894  27.268  -8.646  1.00 50.64  ? 1026 PRO   A C   1 
ATOM   3826 O O   . PRO   A 1 489 ? 41.968  27.128  -8.043  1.00 47.62  ? 1026 PRO   A O   1 
ATOM   3827 C CB  . PRO   A 1 489 ? 39.987  24.963  -9.138  1.00 44.37  ? 1026 PRO   A CB  1 
ATOM   3828 C CG  . PRO   A 1 489 ? 40.504  23.918  -10.069 1.00 43.33  ? 1026 PRO   A CG  1 
ATOM   3829 C CD  . PRO   A 1 489 ? 41.857  24.418  -10.482 1.00 41.25  ? 1026 PRO   A CD  1 
ATOM   3830 N N   . PRO   A 1 490 ? 40.062  28.273  -8.367  1.00 49.36  ? 1027 PRO   A N   1 
ATOM   3831 C CA  . PRO   A 1 490 ? 40.397  29.233  -7.310  1.00 55.25  ? 1027 PRO   A CA  1 
ATOM   3832 C C   . PRO   A 1 490 ? 40.456  28.562  -5.947  1.00 50.72  ? 1027 PRO   A C   1 
ATOM   3833 O O   . PRO   A 1 490 ? 39.955  27.454  -5.739  1.00 48.85  ? 1027 PRO   A O   1 
ATOM   3834 C CB  . PRO   A 1 490 ? 39.255  30.255  -7.375  1.00 63.85  ? 1027 PRO   A CB  1 
ATOM   3835 C CG  . PRO   A 1 490 ? 38.607  30.048  -8.714  1.00 58.43  ? 1027 PRO   A CG  1 
ATOM   3836 C CD  . PRO   A 1 490 ? 38.795  28.604  -9.040  1.00 50.73  ? 1027 PRO   A CD  1 
ATOM   3837 N N   . ARG   A 1 491 ? 41.083  29.253  -5.001  1.00 49.14  ? 1028 ARG   A N   1 
ATOM   3838 C CA  . ARG   A 1 491 ? 41.149  28.717  -3.649  1.00 52.88  ? 1028 ARG   A CA  1 
ATOM   3839 C C   . ARG   A 1 491 ? 39.885  29.088  -2.890  1.00 50.67  ? 1028 ARG   A C   1 
ATOM   3840 O O   . ARG   A 1 491 ? 39.484  30.254  -2.865  1.00 48.00  ? 1028 ARG   A O   1 
ATOM   3841 C CB  . ARG   A 1 491 ? 42.384  29.224  -2.900  1.00 53.25  ? 1028 ARG   A CB  1 
ATOM   3842 C CG  . ARG   A 1 491 ? 42.519  28.633  -1.481  1.00 57.51  ? 1028 ARG   A CG  1 
ATOM   3843 C CD  . ARG   A 1 491 ? 43.710  29.177  -0.738  1.00 71.64  ? 1028 ARG   A CD  1 
ATOM   3844 N NE  . ARG   A 1 491 ? 43.427  30.407  -0.016  1.00 71.96  ? 1028 ARG   A NE  1 
ATOM   3845 C CZ  . ARG   A 1 491 ? 44.330  31.359  0.206   1.00 90.26  ? 1028 ARG   A CZ  1 
ATOM   3846 N NH1 . ARG   A 1 491 ? 45.573  31.231  -0.251  1.00 86.25  ? 1028 ARG   A NH1 1 
ATOM   3847 N NH2 . ARG   A 1 491 ? 43.966  32.435  0.884   1.00 100.85 ? 1028 ARG   A NH2 1 
ATOM   3848 N N   . PHE   A 1 492 ? 39.255  28.087  -2.292  1.00 43.56  ? 1029 PHE   A N   1 
ATOM   3849 C CA  . PHE   A 1 492 ? 38.156  28.248  -1.362  1.00 37.35  ? 1029 PHE   A CA  1 
ATOM   3850 C C   . PHE   A 1 492 ? 38.508  27.540  -0.065  1.00 45.91  ? 1029 PHE   A C   1 
ATOM   3851 O O   . PHE   A 1 492 ? 39.221  26.532  -0.076  1.00 43.30  ? 1029 PHE   A O   1 
ATOM   3852 C CB  . PHE   A 1 492 ? 36.849  27.667  -1.934  1.00 35.01  ? 1029 PHE   A CB  1 
ATOM   3853 C CG  . PHE   A 1 492 ? 36.354  28.388  -3.161  1.00 38.19  ? 1029 PHE   A CG  1 
ATOM   3854 C CD1 . PHE   A 1 492 ? 36.776  27.999  -4.426  1.00 39.71  ? 1029 PHE   A CD1 1 
ATOM   3855 C CD2 . PHE   A 1 492 ? 35.482  29.457  -3.052  1.00 47.57  ? 1029 PHE   A CD2 1 
ATOM   3856 C CE1 . PHE   A 1 492 ? 36.330  28.662  -5.556  1.00 36.68  ? 1029 PHE   A CE1 1 
ATOM   3857 C CE2 . PHE   A 1 492 ? 35.033  30.120  -4.180  1.00 52.40  ? 1029 PHE   A CE2 1 
ATOM   3858 C CZ  . PHE   A 1 492 ? 35.458  29.716  -5.432  1.00 43.82  ? 1029 PHE   A CZ  1 
ATOM   3859 N N   . PRO   A 1 493 ? 38.026  28.045  1.062   1.00 47.55  ? 1030 PRO   A N   1 
ATOM   3860 C CA  . PRO   A 1 493 ? 38.311  27.393  2.343   1.00 47.71  ? 1030 PRO   A CA  1 
ATOM   3861 C C   . PRO   A 1 493 ? 37.684  26.014  2.435   1.00 43.54  ? 1030 PRO   A C   1 
ATOM   3862 O O   . PRO   A 1 493 ? 36.638  25.736  1.847   1.00 38.63  ? 1030 PRO   A O   1 
ATOM   3863 C CB  . PRO   A 1 493 ? 37.705  28.354  3.376   1.00 51.84  ? 1030 PRO   A CB  1 
ATOM   3864 C CG  . PRO   A 1 493 ? 36.741  29.204  2.597   1.00 50.42  ? 1030 PRO   A CG  1 
ATOM   3865 C CD  . PRO   A 1 493 ? 37.319  29.327  1.231   1.00 46.11  ? 1030 PRO   A CD  1 
ATOM   3866 N N   . ARG   A 1 494 ? 38.346  25.145  3.191   1.00 43.46  ? 1031 ARG   A N   1 
ATOM   3867 C CA  . ARG   A 1 494 ? 37.850  23.798  3.425   1.00 45.30  ? 1031 ARG   A CA  1 
ATOM   3868 C C   . ARG   A 1 494 ? 36.555  23.866  4.241   1.00 51.19  ? 1031 ARG   A C   1 
ATOM   3869 O O   . ARG   A 1 494 ? 36.363  24.751  5.081   1.00 48.15  ? 1031 ARG   A O   1 
ATOM   3870 C CB  . ARG   A 1 494 ? 38.945  22.976  4.133   1.00 56.89  ? 1031 ARG   A CB  1 
ATOM   3871 C CG  . ARG   A 1 494 ? 38.928  21.450  3.989   1.00 58.22  ? 1031 ARG   A CG  1 
ATOM   3872 C CD  . ARG   A 1 494 ? 39.343  20.878  2.617   1.00 50.22  ? 1031 ARG   A CD  1 
ATOM   3873 N NE  . ARG   A 1 494 ? 40.766  20.939  2.232   1.00 48.49  ? 1031 ARG   A NE  1 
ATOM   3874 C CZ  . ARG   A 1 494 ? 41.766  20.261  2.804   1.00 44.47  ? 1031 ARG   A CZ  1 
ATOM   3875 N NH1 . ARG   A 1 494 ? 41.556  19.487  3.855   1.00 33.39  ? 1031 ARG   A NH1 1 
ATOM   3876 N NH2 . ARG   A 1 494 ? 43.002  20.380  2.336   1.00 45.97  ? 1031 ARG   A NH2 1 
ATOM   3877 N N   . LYS   A 1 495 ? 35.638  22.941  3.964   1.00 59.57  ? 1032 LYS   A N   1 
ATOM   3878 C CA  . LYS   A 1 495 ? 34.345  23.013  4.633   1.00 63.37  ? 1032 LYS   A CA  1 
ATOM   3879 C C   . LYS   A 1 495 ? 34.366  22.355  6.004   1.00 58.88  ? 1032 LYS   A C   1 
ATOM   3880 O O   . LYS   A 1 495 ? 33.703  22.833  6.929   1.00 65.67  ? 1032 LYS   A O   1 
ATOM   3881 C CB  . LYS   A 1 495 ? 33.255  22.374  3.772   1.00 60.11  ? 1032 LYS   A CB  1 
ATOM   3882 C CG  . LYS   A 1 495 ? 31.879  22.964  4.011   1.00 65.78  ? 1032 LYS   A CG  1 
ATOM   3883 C CD  . LYS   A 1 495 ? 31.833  24.410  3.540   1.00 78.41  ? 1032 LYS   A CD  1 
ATOM   3884 C CE  . LYS   A 1 495 ? 31.205  25.334  4.570   1.00 84.40  ? 1032 LYS   A CE  1 
ATOM   3885 N NZ  . LYS   A 1 495 ? 29.980  25.998  4.037   1.00 88.56  ? 1032 LYS   A NZ  1 
ATOM   3886 N N   . SER   A 1 496 ? 35.109  21.267  6.162   1.00 55.87  ? 1033 SER   A N   1 
ATOM   3887 C CA  . SER   A 1 496 ? 35.202  20.599  7.446   1.00 48.68  ? 1033 SER   A CA  1 
ATOM   3888 C C   . SER   A 1 496 ? 36.662  20.390  7.799   1.00 49.22  ? 1033 SER   A C   1 
ATOM   3889 O O   . SER   A 1 496 ? 37.552  20.476  6.949   1.00 52.94  ? 1033 SER   A O   1 
ATOM   3890 C CB  . SER   A 1 496 ? 34.473  19.260  7.439   1.00 54.13  ? 1033 SER   A CB  1 
ATOM   3891 O OG  . SER   A 1 496 ? 35.374  18.225  7.113   1.00 46.42  ? 1033 SER   A OG  1 
ATOM   3892 N N   . THR   A 1 497 ? 36.901  20.116  9.072   1.00 45.60  ? 1034 THR   A N   1 
ATOM   3893 C CA  . THR   A 1 497 ? 38.252  19.927  9.563   1.00 43.80  ? 1034 THR   A CA  1 
ATOM   3894 C C   . THR   A 1 497 ? 38.677  18.466  9.573   1.00 40.43  ? 1034 THR   A C   1 
ATOM   3895 O O   . THR   A 1 497 ? 39.766  18.163  10.070  1.00 44.96  ? 1034 THR   A O   1 
ATOM   3896 C CB  . THR   A 1 497 ? 38.389  20.501  10.971  1.00 54.93  ? 1034 THR   A CB  1 
ATOM   3897 O OG1 . THR   A 1 497 ? 37.545  19.759  11.861  1.00 65.01  ? 1034 THR   A OG1 1 
ATOM   3898 C CG2 . THR   A 1 497 ? 37.996  21.981  10.989  1.00 51.91  ? 1034 THR   A CG2 1 
ATOM   3899 N N   A PHE   A 1 498 ? 37.853  17.552  9.073   0.44 43.52  ? 1035 PHE   A N   1 
ATOM   3900 N N   B PHE   A 1 498 ? 37.857  17.572  9.024   0.56 43.14  ? 1035 PHE   A N   1 
ATOM   3901 C CA  A PHE   A 1 498 ? 38.267  16.161  9.153   0.44 44.90  ? 1035 PHE   A CA  1 
ATOM   3902 C CA  B PHE   A 1 498 ? 38.147  16.148  9.019   0.56 44.70  ? 1035 PHE   A CA  1 
ATOM   3903 C C   A PHE   A 1 498 ? 39.003  15.730  7.892   0.44 37.75  ? 1035 PHE   A C   1 
ATOM   3904 C C   B PHE   A 1 498 ? 39.083  15.777  7.878   0.56 36.93  ? 1035 PHE   A C   1 
ATOM   3905 O O   A PHE   A 1 498 ? 38.945  16.377  6.842   0.44 32.68  ? 1035 PHE   A O   1 
ATOM   3906 O O   B PHE   A 1 498 ? 39.202  16.485  6.872   0.56 33.30  ? 1035 PHE   A O   1 
ATOM   3907 C CB  A PHE   A 1 498 ? 37.086  15.220  9.434   0.44 53.29  ? 1035 PHE   A CB  1 
ATOM   3908 C CB  B PHE   A 1 498 ? 36.867  15.323  8.875   0.56 52.60  ? 1035 PHE   A CB  1 
ATOM   3909 C CG  A PHE   A 1 498 ? 35.858  15.477  8.600   0.44 57.87  ? 1035 PHE   A CG  1 
ATOM   3910 C CG  B PHE   A 1 498 ? 35.867  15.537  9.969   0.56 58.88  ? 1035 PHE   A CG  1 
ATOM   3911 C CD1 A PHE   A 1 498 ? 35.819  15.149  7.251   0.44 57.70  ? 1035 PHE   A CD1 1 
ATOM   3912 C CD1 B PHE   A 1 498 ? 36.207  15.334  11.295  0.56 61.78  ? 1035 PHE   A CD1 1 
ATOM   3913 C CD2 A PHE   A 1 498 ? 34.714  15.990  9.191   0.44 62.69  ? 1035 PHE   A CD2 1 
ATOM   3914 C CD2 B PHE   A 1 498 ? 34.568  15.904  9.664   0.56 62.94  ? 1035 PHE   A CD2 1 
ATOM   3915 C CE1 A PHE   A 1 498 ? 34.669  15.368  6.501   0.44 59.92  ? 1035 PHE   A CE1 1 
ATOM   3916 C CE1 B PHE   A 1 498 ? 35.274  15.518  12.297  0.56 67.39  ? 1035 PHE   A CE1 1 
ATOM   3917 C CE2 A PHE   A 1 498 ? 33.566  16.206  8.452   0.44 63.87  ? 1035 PHE   A CE2 1 
ATOM   3918 C CE2 B PHE   A 1 498 ? 33.632  16.085  10.660  0.56 64.04  ? 1035 PHE   A CE2 1 
ATOM   3919 C CZ  A PHE   A 1 498 ? 33.544  15.898  7.103   0.44 60.37  ? 1035 PHE   A CZ  1 
ATOM   3920 C CZ  B PHE   A 1 498 ? 33.985  15.893  11.978  0.56 67.22  ? 1035 PHE   A CZ  1 
ATOM   3921 N N   . SER   A 1 499 ? 39.725  14.619  8.030   1.00 38.82  ? 1036 SER   A N   1 
ATOM   3922 C CA  . SER   A 1 499 ? 40.475  14.041  6.932   1.00 36.65  ? 1036 SER   A CA  1 
ATOM   3923 C C   . SER   A 1 499 ? 39.573  13.814  5.726   1.00 35.12  ? 1036 SER   A C   1 
ATOM   3924 O O   . SER   A 1 499 ? 38.403  13.458  5.865   1.00 34.25  ? 1036 SER   A O   1 
ATOM   3925 C CB  . SER   A 1 499 ? 41.082  12.720  7.385   1.00 41.44  ? 1036 SER   A CB  1 
ATOM   3926 O OG  . SER   A 1 499 ? 41.741  12.081  6.313   1.00 34.23  ? 1036 SER   A OG  1 
ATOM   3927 N N   . LEU   A 1 500 ? 40.118  14.054  4.536   1.00 35.63  ? 1037 LEU   A N   1 
ATOM   3928 C CA  . LEU   A 1 500 ? 39.429  13.730  3.301   1.00 27.77  ? 1037 LEU   A CA  1 
ATOM   3929 C C   . LEU   A 1 500 ? 39.648  12.279  2.896   1.00 31.33  ? 1037 LEU   A C   1 
ATOM   3930 O O   . LEU   A 1 500 ? 39.040  11.818  1.920   1.00 29.97  ? 1037 LEU   A O   1 
ATOM   3931 C CB  . LEU   A 1 500 ? 39.899  14.652  2.169   1.00 29.07  ? 1037 LEU   A CB  1 
ATOM   3932 C CG  . LEU   A 1 500 ? 39.771  16.179  2.328   1.00 31.08  ? 1037 LEU   A CG  1 
ATOM   3933 C CD1 . LEU   A 1 500 ? 40.359  16.872  1.106   1.00 28.67  ? 1037 LEU   A CD1 1 
ATOM   3934 C CD2 . LEU   A 1 500 ? 38.318  16.602  2.508   1.00 39.88  ? 1037 LEU   A CD2 1 
ATOM   3935 N N   . LYS   A 1 501 ? 40.503  11.568  3.631   1.00 29.77  ? 1038 LYS   A N   1 
ATOM   3936 C CA  . LYS   A 1 501 ? 40.916  10.215  3.284   1.00 28.91  ? 1038 LYS   A CA  1 
ATOM   3937 C C   . LYS   A 1 501 ? 39.747  9.243   3.429   1.00 27.81  ? 1038 LYS   A C   1 
ATOM   3938 O O   . LYS   A 1 501 ? 39.076  9.222   4.464   1.00 28.23  ? 1038 LYS   A O   1 
ATOM   3939 C CB  . LYS   A 1 501 ? 42.062  9.801   4.209   1.00 35.62  ? 1038 LYS   A CB  1 
ATOM   3940 C CG  . LYS   A 1 501 ? 43.110  8.878   3.632   1.00 61.93  ? 1038 LYS   A CG  1 
ATOM   3941 C CD  . LYS   A 1 501 ? 44.400  8.980   4.448   1.00 75.50  ? 1038 LYS   A CD  1 
ATOM   3942 C CE  . LYS   A 1 501 ? 45.223  10.186  4.006   1.00 81.82  ? 1038 LYS   A CE  1 
ATOM   3943 N NZ  . LYS   A 1 501 ? 45.941  10.851  5.128   1.00 84.64  ? 1038 LYS   A NZ  1 
ATOM   3944 N N   . SER   A 1 502 ? 39.532  8.405   2.407   1.00 27.54  ? 1039 SER   A N   1 
ATOM   3945 C CA  . SER   A 1 502 ? 38.482  7.403   2.517   1.00 27.20  ? 1039 SER   A CA  1 
ATOM   3946 C C   . SER   A 1 502 ? 38.966  6.230   3.366   1.00 28.31  ? 1039 SER   A C   1 
ATOM   3947 O O   . SER   A 1 502 ? 40.151  5.887   3.349   1.00 30.01  ? 1039 SER   A O   1 
ATOM   3948 C CB  . SER   A 1 502 ? 38.081  6.888   1.136   1.00 30.23  ? 1039 SER   A CB  1 
ATOM   3949 O OG  . SER   A 1 502 ? 37.191  5.783   1.247   1.00 32.78  ? 1039 SER   A OG  1 
ATOM   3950 N N   . PRO   A 1 503 ? 38.073  5.599   4.129   1.00 28.68  ? 1040 PRO   A N   1 
ATOM   3951 C CA  . PRO   A 1 503 ? 38.443  4.328   4.767   1.00 33.76  ? 1040 PRO   A CA  1 
ATOM   3952 C C   . PRO   A 1 503 ? 38.533  3.187   3.781   1.00 37.94  ? 1040 PRO   A C   1 
ATOM   3953 O O   . PRO   A 1 503 ? 38.924  2.086   4.179   1.00 39.98  ? 1040 PRO   A O   1 
ATOM   3954 C CB  . PRO   A 1 503 ? 37.315  4.100   5.773   1.00 30.48  ? 1040 PRO   A CB  1 
ATOM   3955 C CG  . PRO   A 1 503 ? 36.108  4.739   5.087   1.00 30.71  ? 1040 PRO   A CG  1 
ATOM   3956 C CD  . PRO   A 1 503 ? 36.695  6.002   4.457   1.00 29.64  ? 1040 PRO   A CD  1 
ATOM   3957 N N   . GLY   A 1 504 ? 38.163  3.403   2.518   1.00 34.68  ? 1041 GLY   A N   1 
ATOM   3958 C CA  . GLY   A 1 504 ? 38.221  2.360   1.514   1.00 37.76  ? 1041 GLY   A CA  1 
ATOM   3959 C C   . GLY   A 1 504 ? 36.978  1.487   1.514   1.00 41.72  ? 1041 GLY   A C   1 
ATOM   3960 O O   . GLY   A 1 504 ? 36.090  1.594   2.363   1.00 35.90  ? 1041 GLY   A O   1 
ATOM   3961 N N   . ILE   A 1 505 ? 36.913  0.592   0.534   1.00 32.52  ? 1042 ILE   A N   1 
ATOM   3962 C CA  . ILE   A 1 505 ? 35.718  -0.211  0.355   1.00 32.74  ? 1042 ILE   A CA  1 
ATOM   3963 C C   . ILE   A 1 505 ? 35.979  -1.682  0.662   1.00 36.25  ? 1042 ILE   A C   1 
ATOM   3964 O O   . ILE   A 1 505 ? 35.163  -2.533  0.316   1.00 39.43  ? 1042 ILE   A O   1 
ATOM   3965 C CB  . ILE   A 1 505 ? 35.112  -0.028  -1.044  1.00 34.57  ? 1042 ILE   A CB  1 
ATOM   3966 C CG1 . ILE   A 1 505 ? 36.113  -0.405  -2.134  1.00 45.04  ? 1042 ILE   A CG1 1 
ATOM   3967 C CG2 . ILE   A 1 505 ? 34.620  1.407   -1.207  1.00 33.13  ? 1042 ILE   A CG2 1 
ATOM   3968 C CD1 . ILE   A 1 505 ? 35.505  -0.329  -3.520  1.00 45.82  ? 1042 ILE   A CD1 1 
ATOM   3969 N N   . ARG   A 1 506 ? 37.089  -1.996  1.324   1.00 37.08  ? 1043 ARG   A N   1 
ATOM   3970 C CA  . ARG   A 1 506 ? 37.266  -3.347  1.852   1.00 42.28  ? 1043 ARG   A CA  1 
ATOM   3971 C C   . ARG   A 1 506 ? 36.481  -3.490  3.152   1.00 42.95  ? 1043 ARG   A C   1 
ATOM   3972 O O   . ARG   A 1 506 ? 36.691  -2.702  4.082   1.00 47.35  ? 1043 ARG   A O   1 
ATOM   3973 C CB  . ARG   A 1 506 ? 38.737  -3.669  2.099   1.00 39.60  ? 1043 ARG   A CB  1 
ATOM   3974 C CG  . ARG   A 1 506 ? 38.922  -5.128  2.464   1.00 60.77  ? 1043 ARG   A CG  1 
ATOM   3975 C CD  . ARG   A 1 506 ? 40.334  -5.509  2.856   1.00 69.27  ? 1043 ARG   A CD  1 
ATOM   3976 N NE  . ARG   A 1 506 ? 40.434  -6.965  2.940   1.00 75.48  ? 1043 ARG   A NE  1 
ATOM   3977 C CZ  . ARG   A 1 506 ? 41.525  -7.629  3.308   1.00 75.00  ? 1043 ARG   A CZ  1 
ATOM   3978 N NH1 . ARG   A 1 506 ? 42.632  -6.966  3.636   1.00 65.34  ? 1043 ARG   A NH1 1 
ATOM   3979 N NH2 . ARG   A 1 506 ? 41.505  -8.960  3.346   1.00 63.58  ? 1043 ARG   A NH2 1 
ATOM   3980 N N   . PRO   A 1 507 ? 35.579  -4.464  3.261   1.00 48.86  ? 1044 PRO   A N   1 
ATOM   3981 C CA  . PRO   A 1 507 ? 34.846  -4.659  4.519   1.00 56.90  ? 1044 PRO   A CA  1 
ATOM   3982 C C   . PRO   A 1 507 ? 35.791  -5.069  5.642   1.00 68.05  ? 1044 PRO   A C   1 
ATOM   3983 O O   . PRO   A 1 507 ? 36.820  -5.706  5.409   1.00 66.00  ? 1044 PRO   A O   1 
ATOM   3984 C CB  . PRO   A 1 507 ? 33.853  -5.783  4.185   1.00 52.64  ? 1044 PRO   A CB  1 
ATOM   3985 C CG  . PRO   A 1 507 ? 33.890  -5.939  2.678   1.00 59.36  ? 1044 PRO   A CG  1 
ATOM   3986 C CD  . PRO   A 1 507 ? 35.244  -5.478  2.247   1.00 57.11  ? 1044 PRO   A CD  1 
ATOM   3987 N N   . ASN   A 1 508 ? 35.437  -4.699  6.872   1.00 69.27  ? 1045 ASN   A N   1 
ATOM   3988 C CA  . ASN   A 1 508 ? 36.285  -5.013  8.030   1.00 76.66  ? 1045 ASN   A CA  1 
ATOM   3989 C C   . ASN   A 1 508 ? 35.875  -6.314  8.691   1.00 76.35  ? 1045 ASN   A C   1 
ATOM   3990 O O   . ASN   A 1 508 ? 34.953  -6.329  9.497   1.00 83.11  ? 1045 ASN   A O   1 
ATOM   3991 C CB  . ASN   A 1 508 ? 36.252  -3.886  9.070   1.00 85.77  ? 1045 ASN   A CB  1 
ATOM   3992 C CG  . ASN   A 1 508 ? 37.007  -2.638  8.612   1.00 92.00  ? 1045 ASN   A CG  1 
ATOM   3993 O OD1 . ASN   A 1 508 ? 38.134  -2.391  9.043   1.00 99.00  ? 1045 ASN   A OD1 1 
ATOM   3994 N ND2 . ASN   A 1 508 ? 36.385  -1.849  7.742   1.00 82.51  ? 1045 ASN   A ND2 1 
HETATM 3995 N N1  . A1ASX B 2 .   ? 35.035  14.743  -18.045 1.00 32.12  ? 1101 A1ASX A N1  1 
HETATM 3996 N N3  . A1ASX B 2 .   ? 36.018  12.695  -17.873 1.00 31.29  ? 1101 A1ASX A N3  1 
HETATM 3997 C C4  . A1ASX B 2 .   ? 33.938  15.682  -18.285 1.00 40.65  ? 1101 A1ASX A C4  1 
HETATM 3998 C C5  . A1ASX B 2 .   ? 34.072  16.458  -19.592 1.00 46.13  ? 1101 A1ASX A C5  1 
HETATM 3999 C C6  . A1ASX B 2 .   ? 34.678  15.657  -20.719 1.00 52.42  ? 1101 A1ASX A C6  1 
HETATM 4000 C C7  . A1ASX B 2 .   ? 34.905  13.424  -17.726 1.00 33.93  ? 1101 A1ASX A C7  1 
HETATM 4001 C C8  . A1ASX B 2 .   ? 36.004  11.378  -17.629 1.00 61.85  ? 1101 A1ASX A C8  1 
HETATM 4002 C C10 . A1ASX B 2 .   ? 39.293  10.715  -18.994 1.00 57.87  ? 1101 A1ASX A C10 1 
HETATM 4003 C C13 . A1ASX B 2 .   ? 40.245  12.739  -17.367 1.00 45.39  ? 1101 A1ASX A C13 1 
HETATM 4004 C C15 . A1ASX B 2 .   ? 33.775  11.388  -17.012 1.00 51.31  ? 1101 A1ASX A C15 1 
HETATM 4005 C C17 . A1ASX B 2 .   ? 31.459  11.344  -16.348 1.00 50.59  ? 1101 A1ASX A C17 1 
HETATM 4006 C C20 . A1ASX B 2 .   ? 33.687  12.786  -17.256 1.00 37.54  ? 1101 A1ASX A C20 1 
HETATM 4007 C C1  . A1ASX B 2 .   ? 38.363  15.200  -19.840 1.00 51.30  ? 1101 A1ASX A C1  1 
HETATM 4008 C C11 . A1ASX B 2 .   ? 40.573  11.206  -19.181 1.00 63.53  ? 1101 A1ASX A C11 1 
HETATM 4009 C C12 . A1ASX B 2 .   ? 41.056  12.221  -18.367 1.00 66.08  ? 1101 A1ASX A C12 1 
HETATM 4010 C C14 . A1ASX B 2 .   ? 38.968  12.240  -17.186 1.00 46.48  ? 1101 A1ASX A C14 1 
HETATM 4011 C C16 . A1ASX B 2 .   ? 32.637  10.691  -16.556 1.00 41.92  ? 1101 A1ASX A C16 1 
HETATM 4012 C C18 . A1ASX B 2 .   ? 31.360  12.719  -16.575 1.00 48.31  ? 1101 A1ASX A C18 1 
HETATM 4013 C C19 . A1ASX B 2 .   ? 32.437  13.419  -17.023 1.00 47.08  ? 1101 A1ASX A C19 1 
HETATM 4014 C C2  . A1ASX B 2 .   ? 36.869  14.948  -19.703 1.00 52.03  ? 1101 A1ASX A C2  1 
HETATM 4015 C C3  . A1ASX B 2 .   ? 36.373  15.284  -18.286 1.00 47.99  ? 1101 A1ASX A C3  1 
HETATM 4016 C C9  . A1ASX B 2 .   ? 38.468  11.233  -18.004 1.00 51.07  ? 1101 A1ASX A C9  1 
HETATM 4017 N N2  . A1ASX B 2 .   ? 36.147  15.737  -20.728 1.00 56.69  ? 1101 A1ASX A N2  1 
HETATM 4018 N N4  . A1ASX B 2 .   ? 37.166  10.711  -17.822 1.00 47.16  ? 1101 A1ASX A N4  1 
HETATM 4019 N N5  . A1ASX B 2 .   ? 34.941  10.696  -17.206 1.00 52.17  ? 1101 A1ASX A N5  1 
HETATM 4020 O O1  . A1ASX B 2 .   ? 42.319  12.704  -18.549 1.00 89.73  ? 1101 A1ASX A O1  1 
HETATM 4021 S S   . DMS   C 3 .   ? -3.201  -17.469 -10.139 1.00 79.41  ? 1102 DMS   A S   1 
HETATM 4022 O O   . DMS   C 3 .   ? -2.935  -18.305 -8.927  1.00 79.44  ? 1102 DMS   A O   1 
HETATM 4023 C C1  . DMS   C 3 .   ? -1.888  -17.715 -11.372 1.00 82.66  ? 1102 DMS   A C1  1 
HETATM 4024 C C2  . DMS   C 3 .   ? -4.621  -18.093 -11.073 1.00 80.33  ? 1102 DMS   A C2  1 
HETATM 4025 S S   . SO4   D 4 .   ? 46.717  5.364   -10.231 1.00 52.20  ? 1103 SO4   A S   1 
HETATM 4026 O O1  . SO4   D 4 .   ? 47.181  6.566   -10.915 1.00 57.33  ? 1103 SO4   A O1  1 
HETATM 4027 O O2  . SO4   D 4 .   ? 46.511  4.267   -11.171 1.00 54.11  ? 1103 SO4   A O2  1 
HETATM 4028 O O3  . SO4   D 4 .   ? 47.725  4.936   -9.265  1.00 79.55  ? 1103 SO4   A O3  1 
HETATM 4029 O O4  . SO4   D 4 .   ? 45.475  5.704   -9.550  1.00 48.58  ? 1103 SO4   A O4  1 
HETATM 4030 O O   . HOH   E 5 .   ? 0.387   -16.079 -39.720 1.00 60.73  ? 1201 HOH   A O   1 
HETATM 4031 O O   . HOH   E 5 .   ? 23.500  19.309  -11.033 1.00 52.46  ? 1202 HOH   A O   1 
HETATM 4032 O O   . HOH   E 5 .   ? 31.027  -0.389  -14.306 1.00 44.80  ? 1203 HOH   A O   1 
HETATM 4033 O O   . HOH   E 5 .   ? 10.615  19.851  -10.923 1.00 63.33  ? 1204 HOH   A O   1 
HETATM 4034 O O   . HOH   E 5 .   ? 27.319  30.204  -19.070 1.00 51.36  ? 1205 HOH   A O   1 
HETATM 4035 O O   . HOH   E 5 .   ? 46.816  8.669   -10.740 1.00 42.29  ? 1206 HOH   A O   1 
HETATM 4036 O O   . HOH   E 5 .   ? 10.621  11.233  5.602   1.00 55.97  ? 1207 HOH   A O   1 
HETATM 4037 O O   . HOH   E 5 .   ? -14.574 -14.498 6.376   1.00 68.80  ? 1208 HOH   A O   1 
HETATM 4038 O O   . HOH   E 5 .   ? -2.374  -23.818 -25.887 1.00 67.77  ? 1209 HOH   A O   1 
HETATM 4039 O O   . HOH   E 5 .   ? 29.224  32.267  -18.086 1.00 57.01  ? 1210 HOH   A O   1 
HETATM 4040 O O   . HOH   E 5 .   ? -18.401 -1.829  -36.205 1.00 58.73  ? 1211 HOH   A O   1 
HETATM 4041 O O   . HOH   E 5 .   ? 33.103  -0.416  -21.046 1.00 45.89  ? 1212 HOH   A O   1 
HETATM 4042 O O   . HOH   E 5 .   ? 33.899  28.838  0.229   1.00 53.13  ? 1213 HOH   A O   1 
HETATM 4043 O O   . HOH   E 5 .   ? -22.202 -0.866  1.212   1.00 69.07  ? 1214 HOH   A O   1 
HETATM 4044 O O   . HOH   E 5 .   ? 39.519  26.179  -17.167 1.00 59.02  ? 1215 HOH   A O   1 
HETATM 4045 O O   . HOH   E 5 .   ? -10.827 -17.746 -25.875 1.00 38.62  ? 1216 HOH   A O   1 
HETATM 4046 O O   . HOH   E 5 .   ? 16.687  -2.760  -15.856 1.00 33.17  ? 1217 HOH   A O   1 
HETATM 4047 O O   . HOH   E 5 .   ? -4.122  6.395   -23.134 1.00 49.18  ? 1218 HOH   A O   1 
HETATM 4048 O O   . HOH   E 5 .   ? 20.471  18.160  -12.212 1.00 50.71  ? 1219 HOH   A O   1 
HETATM 4049 O O   . HOH   E 5 .   ? 41.628  11.403  -14.036 1.00 43.06  ? 1220 HOH   A O   1 
HETATM 4050 O O   . HOH   E 5 .   ? -19.822 -35.319 -31.271 1.00 69.94  ? 1221 HOH   A O   1 
HETATM 4051 O O   . HOH   E 5 .   ? -31.819 -27.235 -29.588 1.00 50.38  ? 1222 HOH   A O   1 
HETATM 4052 O O   . HOH   E 5 .   ? -30.449 -17.811 -34.382 1.00 47.30  ? 1223 HOH   A O   1 
HETATM 4053 O O   . HOH   E 5 .   ? 0.568   -9.258  -14.666 1.00 37.05  ? 1224 HOH   A O   1 
HETATM 4054 O O   . HOH   E 5 .   ? 33.043  12.550  -21.397 1.00 53.43  ? 1225 HOH   A O   1 
HETATM 4055 O O   . HOH   E 5 .   ? 26.743  0.499   -23.371 1.00 38.80  ? 1226 HOH   A O   1 
HETATM 4056 O O   . HOH   E 5 .   ? 1.391   8.865   -3.961  1.00 39.74  ? 1227 HOH   A O   1 
HETATM 4057 O O   . HOH   E 5 .   ? -29.330 -22.425 -14.806 1.00 41.47  ? 1228 HOH   A O   1 
HETATM 4058 O O   . HOH   E 5 .   ? 15.460  -4.702  1.788   1.00 50.54  ? 1229 HOH   A O   1 
HETATM 4059 O O   . HOH   E 5 .   ? 22.841  5.041   14.405  1.00 45.92  ? 1230 HOH   A O   1 
HETATM 4060 O O   . HOH   E 5 .   ? 38.242  2.144   -4.925  1.00 45.48  ? 1231 HOH   A O   1 
HETATM 4061 O O   . HOH   E 5 .   ? -10.760 -16.960 -23.140 1.00 39.90  ? 1232 HOH   A O   1 
HETATM 4062 O O   . HOH   E 5 .   ? -26.904 -8.766  -19.863 1.00 34.01  ? 1233 HOH   A O   1 
HETATM 4063 O O   . HOH   E 5 .   ? -21.679 -7.689  -34.703 1.00 50.14  ? 1234 HOH   A O   1 
HETATM 4064 O O   . HOH   E 5 .   ? 39.288  -10.229 3.023   1.00 60.26  ? 1235 HOH   A O   1 
HETATM 4065 O O   . HOH   E 5 .   ? 11.593  8.240   7.131   1.00 47.28  ? 1236 HOH   A O   1 
HETATM 4066 O O   . HOH   E 5 .   ? 31.834  8.226   2.852   1.00 25.86  ? 1237 HOH   A O   1 
HETATM 4067 O O   . HOH   E 5 .   ? -44.779 -28.822 -22.791 1.00 71.68  ? 1238 HOH   A O   1 
HETATM 4068 O O   . HOH   E 5 .   ? -29.033 -19.697 -14.284 1.00 44.50  ? 1239 HOH   A O   1 
HETATM 4069 O O   . HOH   E 5 .   ? -41.744 -26.635 -28.966 1.00 74.54  ? 1240 HOH   A O   1 
HETATM 4070 O O   . HOH   E 5 .   ? 34.917  32.239  -8.377  1.00 39.08  ? 1241 HOH   A O   1 
HETATM 4071 O O   . HOH   E 5 .   ? -32.985 -19.164 -27.408 1.00 52.91  ? 1242 HOH   A O   1 
HETATM 4072 O O   . HOH   E 5 .   ? 39.066  6.457   -18.217 1.00 43.05  ? 1243 HOH   A O   1 
HETATM 4073 O O   . HOH   E 5 .   ? 17.693  -6.362  5.898   1.00 33.92  ? 1244 HOH   A O   1 
HETATM 4074 O O   . HOH   E 5 .   ? 14.521  -6.724  -17.842 1.00 45.69  ? 1245 HOH   A O   1 
HETATM 4075 O O   . HOH   E 5 .   ? 26.738  30.009  -2.084  1.00 52.04  ? 1246 HOH   A O   1 
HETATM 4076 O O   . HOH   E 5 .   ? -16.599 -14.323 -27.666 1.00 45.20  ? 1247 HOH   A O   1 
HETATM 4077 O O   . HOH   E 5 .   ? -14.597 -34.567 -34.745 1.00 57.12  ? 1248 HOH   A O   1 
HETATM 4078 O O   . HOH   E 5 .   ? 31.369  -5.321  7.014   1.00 32.30  ? 1249 HOH   A O   1 
HETATM 4079 O O   . HOH   E 5 .   ? -22.472 -18.035 -0.637  1.00 42.92  ? 1250 HOH   A O   1 
HETATM 4080 O O   . HOH   E 5 .   ? 15.355  -6.178  -6.332  1.00 49.18  ? 1251 HOH   A O   1 
HETATM 4081 O O   . HOH   E 5 .   ? 29.457  19.028  -0.432  1.00 37.58  ? 1252 HOH   A O   1 
HETATM 4082 O O   . HOH   E 5 .   ? 17.126  9.054   13.202  1.00 56.80  ? 1253 HOH   A O   1 
HETATM 4083 O O   . HOH   E 5 .   ? 12.801  4.731   8.294   1.00 51.69  ? 1254 HOH   A O   1 
HETATM 4084 O O   . HOH   E 5 .   ? -20.322 -6.190  -27.219 1.00 39.87  ? 1255 HOH   A O   1 
HETATM 4085 O O   . HOH   E 5 .   ? 11.401  28.645  -4.021  1.00 34.64  ? 1256 HOH   A O   1 
HETATM 4086 O O   . HOH   E 5 .   ? -12.595 -23.710 0.075   1.00 58.49  ? 1257 HOH   A O   1 
HETATM 4087 O O   . HOH   E 5 .   ? -5.867  -18.248 1.339   1.00 52.38  ? 1258 HOH   A O   1 
HETATM 4088 O O   . HOH   E 5 .   ? -21.725 -16.839 -24.732 1.00 37.36  ? 1259 HOH   A O   1 
HETATM 4089 O O   . HOH   E 5 .   ? -2.295  1.100   -32.353 1.00 52.33  ? 1260 HOH   A O   1 
HETATM 4090 O O   . HOH   E 5 .   ? 34.158  26.555  1.538   1.00 45.26  ? 1261 HOH   A O   1 
HETATM 4091 O O   . HOH   E 5 .   ? 16.423  -6.921  -4.131  1.00 45.79  ? 1262 HOH   A O   1 
HETATM 4092 O O   . HOH   E 5 .   ? 39.984  4.132   -1.132  1.00 35.24  ? 1263 HOH   A O   1 
HETATM 4093 O O   . HOH   E 5 .   ? 22.426  24.792  -0.312  1.00 48.14  ? 1264 HOH   A O   1 
HETATM 4094 O O   . HOH   E 5 .   ? -4.544  -16.455 -23.543 1.00 44.46  ? 1265 HOH   A O   1 
HETATM 4095 O O   . HOH   E 5 .   ? -27.295 -11.100 -16.052 1.00 33.24  ? 1266 HOH   A O   1 
HETATM 4096 O O   . HOH   E 5 .   ? 16.831  -11.477 4.861   1.00 49.82  ? 1267 HOH   A O   1 
HETATM 4097 O O   . HOH   E 5 .   ? 29.260  -2.643  13.389  1.00 54.76  ? 1268 HOH   A O   1 
HETATM 4098 O O   . HOH   E 5 .   ? 40.348  11.366  -0.358  1.00 37.88  ? 1269 HOH   A O   1 
HETATM 4099 O O   . HOH   E 5 .   ? 27.535  30.980  -7.048  1.00 54.96  ? 1270 HOH   A O   1 
HETATM 4100 O O   . HOH   E 5 .   ? 30.064  6.417   9.622   1.00 38.11  ? 1271 HOH   A O   1 
HETATM 4101 O O   . HOH   E 5 .   ? 18.568  1.023   4.552   1.00 27.25  ? 1272 HOH   A O   1 
HETATM 4102 O O   . HOH   E 5 .   ? 45.596  3.011   -15.326 1.00 34.29  ? 1273 HOH   A O   1 
HETATM 4103 O O   . HOH   E 5 .   ? 15.806  30.077  -11.609 1.00 42.08  ? 1274 HOH   A O   1 
HETATM 4104 O O   . HOH   E 5 .   ? -0.944  -17.189 -14.298 1.00 53.31  ? 1275 HOH   A O   1 
HETATM 4105 O O   . HOH   E 5 .   ? 32.996  0.564   -12.829 1.00 38.12  ? 1276 HOH   A O   1 
HETATM 4106 O O   . HOH   E 5 .   ? 10.883  28.023  -10.628 1.00 39.02  ? 1277 HOH   A O   1 
HETATM 4107 O O   . HOH   E 5 .   ? 37.374  5.346   9.400   1.00 44.40  ? 1278 HOH   A O   1 
HETATM 4108 O O   . HOH   E 5 .   ? 25.063  -6.104  6.925   1.00 31.99  ? 1279 HOH   A O   1 
HETATM 4109 O O   . HOH   E 5 .   ? -33.718 -5.950  -22.913 1.00 45.58  ? 1280 HOH   A O   1 
HETATM 4110 O O   . HOH   E 5 .   ? 44.861  14.077  -15.670 1.00 63.55  ? 1281 HOH   A O   1 
HETATM 4111 O O   . HOH   E 5 .   ? -34.919 -17.837 -24.924 1.00 52.30  ? 1282 HOH   A O   1 
HETATM 4112 O O   . HOH   E 5 .   ? 38.080  -8.146  2.430   1.00 61.95  ? 1283 HOH   A O   1 
HETATM 4113 O O   . HOH   E 5 .   ? -34.374 -16.150 -21.084 1.00 42.01  ? 1284 HOH   A O   1 
HETATM 4114 O O   . HOH   E 5 .   ? -20.590 -28.549 -15.378 1.00 44.14  ? 1285 HOH   A O   1 
HETATM 4115 O O   . HOH   E 5 .   ? -24.402 -16.523 -30.343 1.00 50.44  ? 1286 HOH   A O   1 
HETATM 4116 O O   . HOH   E 5 .   ? -10.489 0.589   -6.607  1.00 38.81  ? 1287 HOH   A O   1 
HETATM 4117 O O   . HOH   E 5 .   ? 17.074  -8.624  4.077   1.00 37.75  ? 1288 HOH   A O   1 
HETATM 4118 O O   . HOH   E 5 .   ? -11.067 -17.805 -17.545 1.00 38.34  ? 1289 HOH   A O   1 
HETATM 4119 O O   . HOH   E 5 .   ? 34.592  23.013  0.230   1.00 39.57  ? 1290 HOH   A O   1 
HETATM 4120 O O   . HOH   E 5 .   ? 10.994  9.419   2.019   1.00 49.04  ? 1291 HOH   A O   1 
HETATM 4121 O O   . HOH   E 5 .   ? -28.706 -33.138 -22.032 1.00 52.73  ? 1292 HOH   A O   1 
HETATM 4122 O O   . HOH   E 5 .   ? 3.079   -7.947  -14.931 1.00 36.62  ? 1293 HOH   A O   1 
HETATM 4123 O O   . HOH   E 5 .   ? 26.794  20.017  0.254   1.00 43.41  ? 1294 HOH   A O   1 
HETATM 4124 O O   . HOH   E 5 .   ? -7.700  0.813   -8.156  1.00 43.67  ? 1295 HOH   A O   1 
HETATM 4125 O O   . HOH   E 5 .   ? -6.537  2.981   -11.365 1.00 52.42  ? 1296 HOH   A O   1 
HETATM 4126 O O   . HOH   E 5 .   ? 34.152  22.911  -18.767 1.00 43.39  ? 1297 HOH   A O   1 
HETATM 4127 O O   . HOH   E 5 .   ? -3.575  0.759   -14.161 1.00 31.01  ? 1298 HOH   A O   1 
HETATM 4128 O O   . HOH   E 5 .   ? -9.563  -4.496  -35.878 1.00 61.09  ? 1299 HOH   A O   1 
HETATM 4129 O O   . HOH   E 5 .   ? 14.385  8.254   -0.335  1.00 37.94  ? 1300 HOH   A O   1 
HETATM 4130 O O   . HOH   E 5 .   ? 8.107   1.838   -3.890  1.00 39.82  ? 1301 HOH   A O   1 
HETATM 4131 O O   . HOH   E 5 .   ? -1.803  5.636   -23.466 1.00 51.75  ? 1302 HOH   A O   1 
HETATM 4132 O O   . HOH   E 5 .   ? 42.779  22.502  0.230   1.00 33.89  ? 1303 HOH   A O   1 
HETATM 4133 O O   . HOH   E 5 .   ? -3.427  2.548   -22.323 1.00 41.24  ? 1304 HOH   A O   1 
HETATM 4134 O O   . HOH   E 5 .   ? -1.780  14.561  -9.728  1.00 60.28  ? 1305 HOH   A O   1 
HETATM 4135 O O   . HOH   E 5 .   ? 24.264  -3.497  6.342   1.00 32.56  ? 1306 HOH   A O   1 
HETATM 4136 O O   . HOH   E 5 .   ? 43.060  19.116  -12.450 1.00 34.80  ? 1307 HOH   A O   1 
HETATM 4137 O O   . HOH   E 5 .   ? -23.426 -0.981  -11.696 1.00 37.98  ? 1308 HOH   A O   1 
HETATM 4138 O O   . HOH   E 5 .   ? -14.037 -11.856 -34.863 1.00 54.87  ? 1309 HOH   A O   1 
HETATM 4139 O O   . HOH   E 5 .   ? 15.917  4.323   -11.831 1.00 45.52  ? 1310 HOH   A O   1 
HETATM 4140 O O   . HOH   E 5 .   ? -0.700  -4.811  -10.456 1.00 30.76  ? 1311 HOH   A O   1 
HETATM 4141 O O   . HOH   E 5 .   ? 39.548  18.976  5.834   1.00 40.88  ? 1312 HOH   A O   1 
HETATM 4142 O O   . HOH   E 5 .   ? 20.508  -0.824  -26.819 1.00 59.54  ? 1313 HOH   A O   1 
HETATM 4143 O O   . HOH   E 5 .   ? -4.007  0.485   -0.946  1.00 40.92  ? 1314 HOH   A O   1 
HETATM 4144 O O   . HOH   E 5 .   ? -1.177  -2.199  -30.426 1.00 54.79  ? 1315 HOH   A O   1 
HETATM 4145 O O   . HOH   E 5 .   ? 45.088  2.769   -12.953 1.00 36.63  ? 1316 HOH   A O   1 
HETATM 4146 O O   . HOH   E 5 .   ? 12.340  31.888  -9.410  1.00 44.82  ? 1317 HOH   A O   1 
HETATM 4147 O O   . HOH   E 5 .   ? 14.838  18.232  -2.618  1.00 36.50  ? 1318 HOH   A O   1 
HETATM 4148 O O   . HOH   E 5 .   ? -15.468 -11.845 2.863   1.00 51.12  ? 1319 HOH   A O   1 
HETATM 4149 O O   . HOH   E 5 .   ? -24.393 -6.148  -12.593 1.00 34.91  ? 1320 HOH   A O   1 
HETATM 4150 O O   . HOH   E 5 .   ? 13.571  10.063  -11.050 1.00 51.38  ? 1321 HOH   A O   1 
HETATM 4151 O O   . HOH   E 5 .   ? 36.032  23.475  -15.501 1.00 34.06  ? 1322 HOH   A O   1 
HETATM 4152 O O   . HOH   E 5 .   ? 38.905  -0.564  2.786   1.00 49.84  ? 1323 HOH   A O   1 
HETATM 4153 O O   . HOH   E 5 .   ? -0.336  -6.967  -8.570  1.00 42.00  ? 1324 HOH   A O   1 
HETATM 4154 O O   . HOH   E 5 .   ? 41.716  15.575  -2.803  1.00 30.03  ? 1325 HOH   A O   1 
HETATM 4155 O O   . HOH   E 5 .   ? -9.203  1.756   -24.285 1.00 33.54  ? 1326 HOH   A O   1 
HETATM 4156 O O   . HOH   E 5 .   ? 6.037   -7.397  -4.399  1.00 55.86  ? 1327 HOH   A O   1 
HETATM 4157 O O   . HOH   E 5 .   ? 24.167  -9.771  -5.117  1.00 46.53  ? 1328 HOH   A O   1 
HETATM 4158 O O   . HOH   E 5 .   ? -2.872  -10.398 -12.501 1.00 27.12  ? 1329 HOH   A O   1 
HETATM 4159 O O   . HOH   E 5 .   ? 30.728  -0.863  -19.295 1.00 39.31  ? 1330 HOH   A O   1 
HETATM 4160 O O   . HOH   E 5 .   ? 6.217   -5.472  -24.990 1.00 44.59  ? 1331 HOH   A O   1 
HETATM 4161 O O   . HOH   E 5 .   ? 7.378   -10.681 -19.228 1.00 43.69  ? 1332 HOH   A O   1 
HETATM 4162 O O   . HOH   E 5 .   ? -22.535 2.787   -6.352  1.00 42.54  ? 1333 HOH   A O   1 
HETATM 4163 O O   . HOH   E 5 .   ? -21.227 -19.372 -37.605 1.00 54.04  ? 1334 HOH   A O   1 
HETATM 4164 O O   . HOH   E 5 .   ? 40.897  1.154   -10.966 1.00 39.41  ? 1335 HOH   A O   1 
HETATM 4165 O O   . HOH   E 5 .   ? -33.785 -18.100 -16.096 1.00 53.36  ? 1336 HOH   A O   1 
HETATM 4166 O O   . HOH   E 5 .   ? -18.357 -26.492 -21.125 1.00 45.25  ? 1337 HOH   A O   1 
HETATM 4167 O O   . HOH   E 5 .   ? 23.228  16.435  -18.855 1.00 44.30  ? 1338 HOH   A O   1 
HETATM 4168 O O   . HOH   E 5 .   ? -4.623  -1.646  -14.625 1.00 25.59  ? 1339 HOH   A O   1 
HETATM 4169 O O   . HOH   E 5 .   ? 25.735  -9.867  2.200   1.00 44.57  ? 1340 HOH   A O   1 
HETATM 4170 O O   . HOH   E 5 .   ? 10.654  8.388   -2.127  1.00 38.10  ? 1341 HOH   A O   1 
HETATM 4171 O O   . HOH   E 5 .   ? 28.339  4.397   8.231   1.00 32.88  ? 1342 HOH   A O   1 
HETATM 4172 O O   . HOH   E 5 .   ? 45.133  19.708  -5.736  1.00 55.68  ? 1343 HOH   A O   1 
HETATM 4173 O O   . HOH   E 5 .   ? -13.652 -12.703 4.421   1.00 52.07  ? 1344 HOH   A O   1 
HETATM 4174 O O   . HOH   E 5 .   ? 37.407  25.089  -6.862  1.00 31.90  ? 1345 HOH   A O   1 
HETATM 4175 O O   . HOH   E 5 .   ? 13.469  -5.864  -0.508  1.00 48.50  ? 1346 HOH   A O   1 
HETATM 4176 O O   . HOH   E 5 .   ? 41.043  8.876   -4.160  1.00 41.15  ? 1347 HOH   A O   1 
HETATM 4177 O O   . HOH   E 5 .   ? -8.035  7.107   -11.556 1.00 44.51  ? 1348 HOH   A O   1 
HETATM 4178 O O   . HOH   E 5 .   ? 25.263  -6.918  11.051  1.00 44.61  ? 1349 HOH   A O   1 
HETATM 4179 O O   . HOH   E 5 .   ? 18.766  17.195  2.825   1.00 37.94  ? 1350 HOH   A O   1 
HETATM 4180 O O   . HOH   E 5 .   ? -4.084  -19.079 -20.784 1.00 39.71  ? 1351 HOH   A O   1 
HETATM 4181 O O   . HOH   E 5 .   ? -9.142  -16.079 -26.284 1.00 50.01  ? 1352 HOH   A O   1 
HETATM 4182 O O   . HOH   E 5 .   ? 28.906  25.610  -1.280  1.00 42.73  ? 1353 HOH   A O   1 
HETATM 4183 O O   . HOH   E 5 .   ? 40.874  10.149  -6.753  1.00 34.42  ? 1354 HOH   A O   1 
HETATM 4184 O O   . HOH   E 5 .   ? 28.356  -6.928  -10.329 1.00 56.57  ? 1355 HOH   A O   1 
HETATM 4185 O O   . HOH   E 5 .   ? -29.542 -31.577 -26.182 1.00 47.48  ? 1356 HOH   A O   1 
HETATM 4186 O O   . HOH   E 5 .   ? -12.942 1.858   -7.529  1.00 32.60  ? 1357 HOH   A O   1 
HETATM 4187 O O   . HOH   E 5 .   ? -3.357  4.374   -3.173  1.00 39.73  ? 1358 HOH   A O   1 
HETATM 4188 O O   . HOH   E 5 .   ? -2.838  0.826   -9.582  1.00 35.59  ? 1359 HOH   A O   1 
HETATM 4189 O O   . HOH   E 5 .   ? -15.089 -0.433  -20.390 1.00 34.67  ? 1360 HOH   A O   1 
HETATM 4190 O O   . HOH   E 5 .   ? 13.794  5.136   -10.232 1.00 51.34  ? 1361 HOH   A O   1 
HETATM 4191 O O   . HOH   E 5 .   ? 18.382  13.686  5.367   1.00 42.94  ? 1362 HOH   A O   1 
HETATM 4192 O O   . HOH   E 5 .   ? -19.028 -18.235 -22.943 1.00 31.35  ? 1363 HOH   A O   1 
HETATM 4193 O O   . HOH   E 5 .   ? 37.768  2.229   -17.594 1.00 42.56  ? 1364 HOH   A O   1 
HETATM 4194 O O   . HOH   E 5 .   ? 36.374  11.323  5.100   1.00 41.56  ? 1365 HOH   A O   1 
HETATM 4195 O O   . HOH   E 5 .   ? 28.451  -5.247  -20.271 1.00 41.47  ? 1366 HOH   A O   1 
HETATM 4196 O O   . HOH   E 5 .   ? -19.541 -1.189  -19.217 1.00 42.32  ? 1367 HOH   A O   1 
HETATM 4197 O O   . HOH   E 5 .   ? -22.763 -4.364  -16.025 1.00 35.39  ? 1368 HOH   A O   1 
HETATM 4198 O O   . HOH   E 5 .   ? -17.901 -17.411 -28.948 1.00 46.90  ? 1369 HOH   A O   1 
HETATM 4199 O O   . HOH   E 5 .   ? 22.590  -5.143  -25.196 1.00 42.54  ? 1370 HOH   A O   1 
HETATM 4200 O O   . HOH   E 5 .   ? 41.062  8.598   0.069   1.00 40.25  ? 1371 HOH   A O   1 
HETATM 4201 O O   . HOH   E 5 .   ? 12.764  -12.503 -7.518  1.00 52.48  ? 1372 HOH   A O   1 
HETATM 4202 O O   . HOH   E 5 .   ? 18.583  29.852  -8.268  1.00 36.85  ? 1373 HOH   A O   1 
HETATM 4203 O O   . HOH   E 5 .   ? 32.022  -0.681  -10.777 1.00 50.22  ? 1374 HOH   A O   1 
HETATM 4204 O O   . HOH   E 5 .   ? -1.992  0.137   -21.993 1.00 40.28  ? 1375 HOH   A O   1 
HETATM 4205 O O   . HOH   E 5 .   ? -11.566 -17.908 -14.757 1.00 41.36  ? 1376 HOH   A O   1 
HETATM 4206 O O   . HOH   E 5 .   ? 3.728   7.796   -2.955  1.00 32.54  ? 1377 HOH   A O   1 
HETATM 4207 O O   . HOH   E 5 .   ? -24.214 -23.518 -11.846 1.00 48.71  ? 1378 HOH   A O   1 
HETATM 4208 O O   . HOH   E 5 .   ? 2.911   -2.876  -2.885  1.00 41.42  ? 1379 HOH   A O   1 
HETATM 4209 O O   . HOH   E 5 .   ? 7.065   -12.176 -13.934 1.00 56.10  ? 1380 HOH   A O   1 
HETATM 4210 O O   . HOH   E 5 .   ? 36.055  1.178   -19.701 1.00 55.47  ? 1381 HOH   A O   1 
HETATM 4211 O O   . HOH   E 5 .   ? 42.632  24.821  -2.742  1.00 36.67  ? 1382 HOH   A O   1 
HETATM 4212 O O   . HOH   E 5 .   ? 19.969  3.339   14.049  1.00 58.60  ? 1383 HOH   A O   1 
HETATM 4213 O O   . HOH   E 5 .   ? 6.658   2.094   -1.645  1.00 36.64  ? 1384 HOH   A O   1 
HETATM 4214 O O   . HOH   E 5 .   ? -22.825 -24.999 -29.559 1.00 50.88  ? 1385 HOH   A O   1 
HETATM 4215 O O   . HOH   E 5 .   ? 4.665   11.790  -12.552 1.00 43.20  ? 1386 HOH   A O   1 
HETATM 4216 O O   . HOH   E 5 .   ? -22.812 -9.873  -33.961 1.00 53.61  ? 1387 HOH   A O   1 
HETATM 4217 O O   . HOH   E 5 .   ? 26.211  8.380   -20.197 1.00 40.65  ? 1388 HOH   A O   1 
HETATM 4218 O O   . HOH   E 5 .   ? 38.632  8.130   -2.228  1.00 38.04  ? 1389 HOH   A O   1 
HETATM 4219 O O   . HOH   E 5 .   ? 40.132  25.572  -3.623  1.00 32.73  ? 1390 HOH   A O   1 
HETATM 4220 O O   . HOH   E 5 .   ? -9.397  5.615   -3.884  1.00 43.02  ? 1391 HOH   A O   1 
HETATM 4221 O O   . HOH   E 5 .   ? -4.526  6.016   -27.480 1.00 51.37  ? 1392 HOH   A O   1 
HETATM 4222 O O   . HOH   E 5 .   ? 9.985   22.310  -8.147  1.00 45.54  ? 1393 HOH   A O   1 
HETATM 4223 O O   . HOH   E 5 .   ? -4.143  2.291   -16.112 1.00 41.90  ? 1394 HOH   A O   1 
HETATM 4224 O O   . HOH   E 5 .   ? -10.375 -11.690 -35.822 1.00 49.13  ? 1395 HOH   A O   1 
HETATM 4225 O O   . HOH   E 5 .   ? 10.615  13.376  -9.330  1.00 50.95  ? 1396 HOH   A O   1 
HETATM 4226 O O   . HOH   E 5 .   ? -37.093 -28.293 -19.926 1.00 56.64  ? 1397 HOH   A O   1 
HETATM 4227 O O   . HOH   E 5 .   ? 20.610  -14.764 4.433   1.00 47.77  ? 1398 HOH   A O   1 
HETATM 4228 O O   . HOH   E 5 .   ? 12.043  -3.564  -21.203 1.00 53.21  ? 1399 HOH   A O   1 
HETATM 4229 O O   . HOH   E 5 .   ? 23.561  0.235   14.231  1.00 54.23  ? 1400 HOH   A O   1 
HETATM 4230 O O   . HOH   E 5 .   ? -0.374  -0.602  -6.182  1.00 41.60  ? 1401 HOH   A O   1 
HETATM 4231 O O   . HOH   E 5 .   ? 18.165  -13.223 -2.374  1.00 48.02  ? 1402 HOH   A O   1 
HETATM 4232 O O   . HOH   E 5 .   ? 42.292  18.728  11.259  1.00 48.00  ? 1403 HOH   A O   1 
HETATM 4233 O O   . HOH   E 5 .   ? 37.318  10.169  -0.897  1.00 24.31  ? 1404 HOH   A O   1 
HETATM 4234 O O   . HOH   E 5 .   ? 18.713  9.966   -12.271 1.00 34.79  ? 1405 HOH   A O   1 
HETATM 4235 O O   . HOH   E 5 .   ? -24.280 -5.102  -9.829  1.00 33.79  ? 1406 HOH   A O   1 
HETATM 4236 O O   . HOH   E 5 .   ? 29.077  10.854  -20.077 1.00 41.08  ? 1407 HOH   A O   1 
HETATM 4237 O O   . HOH   E 5 .   ? -12.474 1.930   -22.457 1.00 44.29  ? 1408 HOH   A O   1 
HETATM 4238 O O   . HOH   E 5 .   ? 20.641  31.813  -12.564 1.00 63.77  ? 1409 HOH   A O   1 
HETATM 4239 O O   . HOH   E 5 .   ? -26.859 -4.822  -18.819 1.00 53.23  ? 1410 HOH   A O   1 
HETATM 4240 O O   . HOH   E 5 .   ? 22.392  6.092   -25.407 1.00 60.32  ? 1411 HOH   A O   1 
HETATM 4241 O O   . HOH   E 5 .   ? -28.033 -9.347  -13.964 1.00 40.88  ? 1412 HOH   A O   1 
HETATM 4242 O O   . HOH   E 5 .   ? -14.773 2.922   -18.438 1.00 36.06  ? 1413 HOH   A O   1 
HETATM 4243 O O   . HOH   E 5 .   ? 32.697  32.348  -12.974 1.00 43.24  ? 1414 HOH   A O   1 
HETATM 4244 O O   . HOH   E 5 .   ? -11.895 -18.533 -20.075 1.00 34.82  ? 1415 HOH   A O   1 
HETATM 4245 O O   . HOH   E 5 .   ? 6.653   -9.822  -7.721  1.00 43.43  ? 1416 HOH   A O   1 
HETATM 4246 O O   . HOH   E 5 .   ? -6.142  -13.835 -25.385 1.00 44.74  ? 1417 HOH   A O   1 
HETATM 4247 O O   . HOH   E 5 .   ? 43.060  -11.141 4.372   1.00 60.57  ? 1418 HOH   A O   1 
HETATM 4248 O O   . HOH   E 5 .   ? 35.312  -1.041  -13.226 1.00 44.16  ? 1419 HOH   A O   1 
HETATM 4249 O O   . HOH   E 5 .   ? 37.176  0.156   5.387   1.00 53.87  ? 1420 HOH   A O   1 
HETATM 4250 O O   . HOH   E 5 .   ? -6.635  -18.263 -13.339 1.00 44.75  ? 1421 HOH   A O   1 
HETATM 4251 O O   . HOH   E 5 .   ? -4.528  -16.550 -13.905 1.00 36.21  ? 1422 HOH   A O   1 
HETATM 4252 O O   . HOH   E 5 .   ? 0.312   15.088  -7.540  1.00 55.39  ? 1423 HOH   A O   1 
HETATM 4253 O O   . HOH   E 5 .   ? -20.747 -2.143  -21.904 1.00 46.34  ? 1424 HOH   A O   1 
HETATM 4254 O O   . HOH   E 5 .   ? 5.645   9.856   -2.869  1.00 37.15  ? 1425 HOH   A O   1 
HETATM 4255 O O   . HOH   E 5 .   ? 27.802  25.517  -20.373 1.00 31.62  ? 1426 HOH   A O   1 
HETATM 4256 O O   . HOH   E 5 .   ? 31.877  -4.634  -1.787  1.00 45.84  ? 1427 HOH   A O   1 
HETATM 4257 O O   . HOH   E 5 .   ? 20.868  18.257  1.044   1.00 43.63  ? 1428 HOH   A O   1 
HETATM 4258 O O   . HOH   E 5 .   ? -31.520 -11.473 -17.293 1.00 49.87  ? 1429 HOH   A O   1 
HETATM 4259 O O   . HOH   E 5 .   ? 43.111  12.558  -6.461  1.00 40.48  ? 1430 HOH   A O   1 
HETATM 4260 O O   . HOH   E 5 .   ? -7.966  -19.262 -0.448  1.00 48.98  ? 1431 HOH   A O   1 
HETATM 4261 O O   . HOH   E 5 .   ? 45.183  2.655   -19.564 1.00 57.02  ? 1432 HOH   A O   1 
HETATM 4262 O O   . HOH   E 5 .   ? 23.256  -10.233 -0.161  1.00 47.99  ? 1433 HOH   A O   1 
HETATM 4263 O O   . HOH   E 5 .   ? 17.748  -5.747  8.740   1.00 39.91  ? 1434 HOH   A O   1 
HETATM 4264 O O   . HOH   E 5 .   ? 18.820  21.122  2.113   1.00 48.53  ? 1435 HOH   A O   1 
HETATM 4265 O O   . HOH   E 5 .   ? -23.297 -6.707  -4.570  1.00 36.59  ? 1436 HOH   A O   1 
HETATM 4266 O O   . HOH   E 5 .   ? 16.553  -6.661  0.706   1.00 35.58  ? 1437 HOH   A O   1 
HETATM 4267 O O   . HOH   E 5 .   ? 21.720  -0.664  -28.569 1.00 56.94  ? 1438 HOH   A O   1 
HETATM 4268 O O   . HOH   E 5 .   ? -14.455 2.064   -9.915  1.00 25.89  ? 1439 HOH   A O   1 
HETATM 4269 O O   . HOH   E 5 .   ? -3.669  8.354   -12.524 1.00 35.76  ? 1440 HOH   A O   1 
HETATM 4270 O O   . HOH   E 5 .   ? -9.425  -19.497 -16.456 1.00 45.10  ? 1441 HOH   A O   1 
HETATM 4271 O O   . HOH   E 5 .   ? 18.730  -7.714  -20.187 1.00 51.53  ? 1442 HOH   A O   1 
HETATM 4272 O O   . HOH   E 5 .   ? -13.141 3.799   0.058   1.00 43.74  ? 1443 HOH   A O   1 
HETATM 4273 O O   . HOH   E 5 .   ? -39.368 -31.498 -16.971 1.00 71.95  ? 1444 HOH   A O   1 
HETATM 4274 O O   . HOH   E 5 .   ? -8.653  4.490   -17.621 1.00 49.52  ? 1445 HOH   A O   1 
HETATM 4275 O O   . HOH   E 5 .   ? 18.911  15.393  -11.641 1.00 47.01  ? 1446 HOH   A O   1 
HETATM 4276 O O   . HOH   E 5 .   ? 11.580  4.831   1.709   1.00 52.27  ? 1447 HOH   A O   1 
HETATM 4277 O O   . HOH   E 5 .   ? -19.924 -16.290 -31.524 1.00 49.58  ? 1448 HOH   A O   1 
HETATM 4278 O O   . HOH   E 5 .   ? -33.730 -17.586 -34.787 1.00 41.97  ? 1449 HOH   A O   1 
HETATM 4279 O O   . HOH   E 5 .   ? 4.440   -6.901  -7.974  1.00 40.31  ? 1450 HOH   A O   1 
HETATM 4280 O O   . HOH   E 5 .   ? 33.557  -0.058  10.460  1.00 58.66  ? 1451 HOH   A O   1 
HETATM 4281 O O   . HOH   E 5 .   ? -28.593 -9.532  -18.023 1.00 45.43  ? 1452 HOH   A O   1 
HETATM 4282 O O   . HOH   E 5 .   ? 46.905  13.581  4.593   1.00 49.21  ? 1453 HOH   A O   1 
HETATM 4283 O O   . HOH   E 5 .   ? 36.694  1.174   7.959   1.00 57.21  ? 1454 HOH   A O   1 
HETATM 4284 O O   . HOH   E 5 .   ? -24.637 -33.754 -31.488 1.00 46.58  ? 1455 HOH   A O   1 
HETATM 4285 O O   . HOH   E 5 .   ? -2.995  12.430  -7.708  1.00 42.37  ? 1456 HOH   A O   1 
HETATM 4286 O O   . HOH   E 5 .   ? 39.108  1.103   -1.367  1.00 47.83  ? 1457 HOH   A O   1 
HETATM 4287 O O   . HOH   E 5 .   ? -25.662 -18.830 -7.030  1.00 52.05  ? 1458 HOH   A O   1 
HETATM 4288 O O   . HOH   E 5 .   ? 1.014   -9.122  -9.913  1.00 41.40  ? 1459 HOH   A O   1 
HETATM 4289 O O   . HOH   E 5 .   ? -34.211 -15.522 -23.741 1.00 46.26  ? 1460 HOH   A O   1 
HETATM 4290 O O   . HOH   E 5 .   ? -12.860 -10.266 6.069   1.00 57.46  ? 1461 HOH   A O   1 
HETATM 4291 O O   . HOH   E 5 .   ? -28.568 -26.842 -25.326 1.00 47.69  ? 1462 HOH   A O   1 
HETATM 4292 O O   . HOH   E 5 .   ? 29.982  15.428  3.591   1.00 39.67  ? 1463 HOH   A O   1 
HETATM 4293 O O   . HOH   E 5 .   ? 4.734   -1.264  -29.749 1.00 57.92  ? 1464 HOH   A O   1 
HETATM 4294 O O   . HOH   E 5 .   ? -15.418 -2.409  2.945   1.00 44.86  ? 1465 HOH   A O   1 
HETATM 4295 O O   . HOH   E 5 .   ? -10.085 -25.750 -19.374 1.00 52.45  ? 1466 HOH   A O   1 
HETATM 4296 O O   . HOH   E 5 .   ? 17.491  0.398   -24.214 1.00 52.94  ? 1467 HOH   A O   1 
HETATM 4297 O O   . HOH   E 5 .   ? 38.030  32.478  -4.204  1.00 56.87  ? 1468 HOH   A O   1 
HETATM 4298 O O   . HOH   E 5 .   ? 13.273  -5.858  -4.988  1.00 41.00  ? 1469 HOH   A O   1 
HETATM 4299 O O   . HOH   E 5 .   ? 16.709  26.838  -0.281  1.00 41.86  ? 1470 HOH   A O   1 
HETATM 4300 O O   . HOH   E 5 .   ? 30.615  1.726   -24.775 1.00 57.70  ? 1471 HOH   A O   1 
HETATM 4301 O O   . HOH   E 5 .   ? -10.856 3.063   -15.152 1.00 47.15  ? 1472 HOH   A O   1 
HETATM 4302 O O   . HOH   E 5 .   ? -23.794 -5.019  -6.462  1.00 36.06  ? 1473 HOH   A O   1 
HETATM 4303 O O   . HOH   E 5 .   ? 25.821  -0.453  14.265  1.00 44.68  ? 1474 HOH   A O   1 
HETATM 4304 O O   . HOH   E 5 .   ? -16.769 -1.471  -24.854 1.00 36.04  ? 1475 HOH   A O   1 
HETATM 4305 O O   . HOH   E 5 .   ? 31.688  -5.129  -9.480  1.00 52.76  ? 1476 HOH   A O   1 
HETATM 4306 O O   . HOH   E 5 .   ? 19.698  23.885  -1.119  1.00 48.27  ? 1477 HOH   A O   1 
HETATM 4307 O O   . HOH   E 5 .   ? -3.022  -8.262  -3.651  1.00 33.98  ? 1478 HOH   A O   1 
HETATM 4308 O O   . HOH   E 5 .   ? -3.069  -22.084 -25.056 1.00 62.38  ? 1479 HOH   A O   1 
HETATM 4309 O O   . HOH   E 5 .   ? 28.436  0.618   -25.528 1.00 44.54  ? 1480 HOH   A O   1 
HETATM 4310 O O   . HOH   E 5 .   ? -1.738  7.001   -1.973  1.00 51.80  ? 1481 HOH   A O   1 
HETATM 4311 O O   . HOH   E 5 .   ? 7.399   2.393   0.797   1.00 49.52  ? 1482 HOH   A O   1 
HETATM 4312 O O   . HOH   E 5 .   ? -25.854 -24.948 -13.508 1.00 45.77  ? 1483 HOH   A O   1 
HETATM 4313 O O   . HOH   E 5 .   ? 32.958  31.771  -15.595 1.00 46.33  ? 1484 HOH   A O   1 
HETATM 4314 O O   . HOH   E 5 .   ? 41.006  30.407  1.787   1.00 56.93  ? 1485 HOH   A O   1 
HETATM 4315 O O   . HOH   E 5 .   ? 28.492  32.272  -11.105 1.00 48.88  ? 1486 HOH   A O   1 
HETATM 4316 O O   . HOH   E 5 .   ? -35.882 -33.286 -23.985 1.00 64.77  ? 1487 HOH   A O   1 
HETATM 4317 O O   . HOH   E 5 .   ? -20.583 -24.776 -26.788 1.00 47.14  ? 1488 HOH   A O   1 
HETATM 4318 O O   . HOH   E 5 .   ? -27.815 -19.513 -11.920 1.00 41.64  ? 1489 HOH   A O   1 
HETATM 4319 O O   . HOH   E 5 .   ? -18.379 -27.472 -14.233 1.00 53.41  ? 1490 HOH   A O   1 
HETATM 4320 O O   . HOH   E 5 .   ? 5.231   13.526  -9.723  1.00 56.91  ? 1491 HOH   A O   1 
HETATM 4321 O O   . HOH   E 5 .   ? -35.499 -12.086 -28.257 1.00 60.18  ? 1492 HOH   A O   1 
HETATM 4322 O O   . HOH   E 5 .   ? -8.457  0.468   3.219   1.00 55.58  ? 1493 HOH   A O   1 
HETATM 4323 O O   . HOH   E 5 .   ? 43.235  20.271  -14.910 1.00 42.29  ? 1494 HOH   A O   1 
HETATM 4324 O O   . HOH   E 5 .   ? 22.000  29.056  -13.910 1.00 56.89  ? 1495 HOH   A O   1 
HETATM 4325 O O   . HOH   E 5 .   ? 23.235  20.485  -13.495 1.00 48.21  ? 1496 HOH   A O   1 
HETATM 4326 O O   . HOH   E 5 .   ? 25.009  29.806  -7.173  1.00 48.97  ? 1497 HOH   A O   1 
HETATM 4327 O O   . HOH   E 5 .   ? 30.735  -7.403  2.859   1.00 52.98  ? 1498 HOH   A O   1 
HETATM 4328 O O   . HOH   E 5 .   ? 21.914  18.843  -16.113 1.00 41.69  ? 1499 HOH   A O   1 
HETATM 4329 O O   . HOH   E 5 .   ? -26.353 -12.458 -32.093 1.00 48.49  ? 1500 HOH   A O   1 
HETATM 4330 O O   . HOH   E 5 .   ? 18.938  10.204  10.807  1.00 49.57  ? 1501 HOH   A O   1 
HETATM 4331 O O   . HOH   E 5 .   ? -6.025  3.982   -16.005 1.00 50.70  ? 1502 HOH   A O   1 
HETATM 4332 O O   . HOH   E 5 .   ? -19.088 -35.652 -40.410 1.00 32.72  ? 1503 HOH   A O   1 
HETATM 4333 O O   . HOH   E 5 .   ? 3.121   -10.374 -17.388 1.00 49.97  ? 1504 HOH   A O   1 
HETATM 4334 O O   . HOH   E 5 .   ? 39.097  -1.065  -7.563  1.00 36.68  ? 1505 HOH   A O   1 
HETATM 4335 O O   . HOH   E 5 .   ? 22.392  22.856  -13.985 1.00 45.64  ? 1506 HOH   A O   1 
HETATM 4336 O O   . HOH   E 5 .   ? 14.394  3.948   9.651   1.00 50.56  ? 1507 HOH   A O   1 
HETATM 4337 O O   . HOH   E 5 .   ? -11.029 -21.467 -14.745 1.00 43.75  ? 1508 HOH   A O   1 
HETATM 4338 O O   . HOH   E 5 .   ? -20.878 -3.800  -26.050 1.00 43.71  ? 1509 HOH   A O   1 
HETATM 4339 O O   . HOH   E 5 .   ? 32.699  24.413  0.553   1.00 51.59  ? 1510 HOH   A O   1 
HETATM 4340 O O   . HOH   E 5 .   ? -20.656 -2.598  -16.049 1.00 42.71  ? 1511 HOH   A O   1 
HETATM 4341 O O   . HOH   E 5 .   ? -12.588 -21.975 -12.624 1.00 50.14  ? 1512 HOH   A O   1 
HETATM 4342 O O   . HOH   E 5 .   ? 29.263  -11.114 10.205  1.00 55.87  ? 1513 HOH   A O   1 
HETATM 4343 O O   . HOH   E 5 .   ? 39.556  12.897  10.688  1.00 58.21  ? 1514 HOH   A O   1 
HETATM 4344 O O   . HOH   E 5 .   ? 0.492   -10.615 -17.181 1.00 46.07  ? 1515 HOH   A O   1 
HETATM 4345 O O   . HOH   E 5 .   ? 26.168  27.404  -20.981 1.00 56.18  ? 1516 HOH   A O   1 
HETATM 4346 O O   . HOH   E 5 .   ? 24.204  -6.270  -27.199 1.00 52.54  ? 1517 HOH   A O   1 
HETATM 4347 O O   . HOH   E 5 .   ? 18.573  25.740  -2.066  1.00 49.62  ? 1518 HOH   A O   1 
HETATM 4348 O O   . HOH   E 5 .   ? -4.442  -4.620  10.757  1.00 62.53  ? 1519 HOH   A O   1 
HETATM 4349 O O   . HOH   E 5 .   ? 22.981  31.353  -7.759  1.00 46.85  ? 1520 HOH   A O   1 
HETATM 4350 O O   . HOH   E 5 .   ? 23.412  16.070  3.476   1.00 50.54  ? 1521 HOH   A O   1 
HETATM 4351 O O   . HOH   E 5 .   ? 15.633  -1.463  -23.615 1.00 64.76  ? 1522 HOH   A O   1 
HETATM 4352 O O   . HOH   E 5 .   ? 9.563   -9.016  10.131  1.00 70.71  ? 1523 HOH   A O   1 
HETATM 4353 O O   . HOH   E 5 .   ? 10.105  14.369  -3.904  1.00 49.07  ? 1524 HOH   A O   1 
HETATM 4354 O O   . HOH   E 5 .   ? -7.464  -19.742 -15.331 1.00 50.61  ? 1525 HOH   A O   1 
HETATM 4355 O O   . HOH   E 5 .   ? 12.770  16.630  3.961   1.00 56.03  ? 1526 HOH   A O   1 
HETATM 4356 O O   . HOH   E 5 .   ? -24.360 -24.995 -9.554  1.00 58.93  ? 1527 HOH   A O   1 
HETATM 4357 O O   . HOH   E 5 .   ? -19.335 -3.217  -24.077 1.00 38.73  ? 1528 HOH   A O   1 
HETATM 4358 O O   . HOH   E 5 .   ? 26.610  -4.431  13.402  1.00 58.24  ? 1529 HOH   A O   1 
HETATM 4359 O O   . HOH   E 5 .   ? 11.708  27.135  4.935   1.00 44.39  ? 1530 HOH   A O   1 
HETATM 4360 O O   . HOH   E 5 .   ? -12.014 -26.726 -18.752 1.00 62.98  ? 1531 HOH   A O   1 
HETATM 4361 O O   . HOH   E 5 .   ? 38.751  -1.288  -5.449  1.00 46.79  ? 1532 HOH   A O   1 
HETATM 4362 O O   . HOH   E 5 .   ? 29.620  -7.504  -19.381 1.00 50.86  ? 1533 HOH   A O   1 
HETATM 4363 O O   . HOH   E 5 .   ? 40.479  11.846  -3.140  1.00 42.01  ? 1534 HOH   A O   1 
HETATM 4364 O O   . HOH   E 5 .   ? 15.775  2.992   15.758  1.00 62.04  ? 1535 HOH   A O   1 
HETATM 4365 O O   . HOH   E 5 .   ? 17.187  14.463  -10.719 1.00 50.62  ? 1536 HOH   A O   1 
HETATM 4366 O O   . HOH   E 5 .   ? 0.342   -21.231 -28.051 1.00 60.88  ? 1537 HOH   A O   1 
HETATM 4367 O O   . HOH   E 5 .   ? 0.471   -23.113 -26.665 1.00 71.44  ? 1538 HOH   A O   1 
HETATM 4368 O O   . HOH   E 5 .   ? 30.939  -2.876  -15.514 1.00 59.44  ? 1539 HOH   A O   1 
HETATM 4369 O O   . HOH   E 5 .   ? 3.704   13.643  -14.639 1.00 62.80  ? 1540 HOH   A O   1 
HETATM 4370 O O   . HOH   E 5 .   ? -20.020 1.023   -12.816 1.00 29.52  ? 1541 HOH   A O   1 
HETATM 4371 O O   . HOH   E 5 .   ? -21.792 -17.119 -30.277 1.00 56.16  ? 1542 HOH   A O   1 
HETATM 4372 O O   . HOH   E 5 .   ? 23.789  -14.956 1.253   1.00 54.53  ? 1543 HOH   A O   1 
HETATM 4373 O O   . HOH   E 5 .   ? 28.981  -12.584 -17.571 1.00 44.68  ? 1544 HOH   A O   1 
HETATM 4374 O O   . HOH   E 5 .   ? 14.433  -3.789  -21.031 1.00 59.16  ? 1545 HOH   A O   1 
HETATM 4375 O O   . HOH   E 5 .   ? -24.834 -2.318  -9.856  1.00 54.24  ? 1546 HOH   A O   1 
HETATM 4376 O O   . HOH   E 5 .   ? 12.875  30.204  -2.013  1.00 56.06  ? 1547 HOH   A O   1 
HETATM 4377 O O   . HOH   E 5 .   ? 35.878  11.493  -21.231 1.00 58.53  ? 1548 HOH   A O   1 
HETATM 4378 O O   . HOH   E 5 .   ? 13.665  2.010   13.983  1.00 68.87  ? 1549 HOH   A O   1 
HETATM 4379 O O   . HOH   E 5 .   ? 19.103  -12.592 3.276   1.00 41.33  ? 1550 HOH   A O   1 
HETATM 4380 O O   . HOH   E 5 .   ? -6.912  4.260   -13.877 1.00 50.91  ? 1551 HOH   A O   1 
HETATM 4381 O O   . HOH   E 5 .   ? -26.526 -7.491  -13.014 1.00 39.51  ? 1552 HOH   A O   1 
HETATM 4382 O O   . HOH   E 5 .   ? -11.350 3.683   -18.814 1.00 54.88  ? 1553 HOH   A O   1 
HETATM 4383 O O   . HOH   E 5 .   ? 15.421  29.124  -1.776  1.00 47.22  ? 1554 HOH   A O   1 
HETATM 4384 O O   . HOH   E 5 .   ? 44.027  21.863  -11.555 1.00 50.04  ? 1555 HOH   A O   1 
HETATM 4385 O O   . HOH   E 5 .   ? -8.672  -21.935 0.538   1.00 54.20  ? 1556 HOH   A O   1 
HETATM 4386 O O   . HOH   E 5 .   ? -26.316 -32.945 -20.413 1.00 41.57  ? 1557 HOH   A O   1 
HETATM 4387 O O   . HOH   E 5 .   ? 23.143  18.108  1.935   1.00 40.27  ? 1558 HOH   A O   1 
HETATM 4388 O O   . HOH   E 5 .   ? -0.212  -10.761 -11.776 1.00 43.13  ? 1559 HOH   A O   1 
HETATM 4389 O O   . HOH   E 5 .   ? -4.380  2.103   -11.949 1.00 42.59  ? 1560 HOH   A O   1 
HETATM 4390 O O   . HOH   E 5 .   ? 50.891  4.268   -7.190  1.00 51.33  ? 1561 HOH   A O   1 
HETATM 4391 O O   . HOH   E 5 .   ? -0.159  -15.028 -11.066 1.00 59.27  ? 1562 HOH   A O   1 
HETATM 4392 O O   . HOH   E 5 .   ? 45.498  17.404  -11.785 1.00 55.33  ? 1563 HOH   A O   1 
HETATM 4393 O O   . HOH   E 5 .   ? 43.448  35.949  -0.426  1.00 39.28  ? 1564 HOH   A O   1 
HETATM 4394 O O   . HOH   E 5 .   ? 0.257   -2.422  -3.392  1.00 52.53  ? 1565 HOH   A O   1 
HETATM 4395 O O   . HOH   E 5 .   ? 38.160  -3.951  -14.337 1.00 43.32  ? 1566 HOH   A O   1 
HETATM 4396 O O   . HOH   E 5 .   ? 13.425  7.743   -11.702 1.00 52.08  ? 1567 HOH   A O   1 
HETATM 4397 O O   . HOH   E 5 .   ? -35.277 -14.510 -19.186 1.00 40.70  ? 1568 HOH   A O   1 
HETATM 4398 O O   . HOH   E 5 .   ? 0.466   -13.204 -10.912 1.00 54.32  ? 1569 HOH   A O   1 
HETATM 4399 O O   . HOH   E 5 .   ? 24.824  18.175  -0.003  1.00 38.18  ? 1570 HOH   A O   1 
HETATM 4400 O O   . HOH   E 5 .   ? 32.598  -7.793  6.765   1.00 42.17  ? 1571 HOH   A O   1 
HETATM 4401 O O   . HOH   E 5 .   ? -5.249  2.408   0.407   1.00 66.20  ? 1572 HOH   A O   1 
HETATM 4402 O O   . HOH   E 5 .   ? 29.326  16.545  1.195   1.00 51.78  ? 1573 HOH   A O   1 
HETATM 4403 O O   . HOH   E 5 .   ? 15.647  29.028  2.455   1.00 65.21  ? 1574 HOH   A O   1 
HETATM 4404 O O   . HOH   E 5 .   ? 39.165  4.210   -19.182 1.00 56.63  ? 1575 HOH   A O   1 
HETATM 4405 O O   . HOH   E 5 .   ? 13.096  30.517  2.091   1.00 45.98  ? 1576 HOH   A O   1 
HETATM 4406 O O   . HOH   E 5 .   ? -3.178  -21.503 -21.233 1.00 48.34  ? 1577 HOH   A O   1 
HETATM 4407 O O   . HOH   E 5 .   ? -26.062 -27.618 -12.636 1.00 57.69  ? 1578 HOH   A O   1 
HETATM 4408 O O   . HOH   E 5 .   ? -31.854 -19.863 -12.988 1.00 58.84  ? 1579 HOH   A O   1 
HETATM 4409 O O   . HOH   E 5 .   ? 3.254   6.801   -0.677  1.00 55.75  ? 1580 HOH   A O   1 
HETATM 4410 O O   . HOH   E 5 .   ? 13.224  30.036  -11.703 1.00 55.75  ? 1581 HOH   A O   1 
HETATM 4411 O O   . HOH   E 5 .   ? 15.691  -5.291  4.409   1.00 61.19  ? 1582 HOH   A O   1 
HETATM 4412 O O   . HOH   E 5 .   ? -17.045 -36.079 -32.399 1.00 58.60  ? 1583 HOH   A O   1 
HETATM 4413 O O   . HOH   E 5 .   ? -9.328  4.811   -6.362  1.00 46.47  ? 1584 HOH   A O   1 
HETATM 4414 O O   . HOH   E 5 .   ? -28.249 -23.901 -12.911 1.00 53.33  ? 1585 HOH   A O   1 
HETATM 4415 O O   . HOH   E 5 .   ? 22.170  -13.323 -0.608  1.00 58.19  ? 1586 HOH   A O   1 
HETATM 4416 O O   . HOH   E 5 .   ? 25.604  31.447  -17.047 1.00 55.93  ? 1587 HOH   A O   1 
HETATM 4417 O O   . HOH   E 5 .   ? -16.222 0.177   -22.758 1.00 37.17  ? 1588 HOH   A O   1 
HETATM 4418 O O   . HOH   E 5 .   ? 27.285  33.308  -8.207  1.00 55.33  ? 1589 HOH   A O   1 
HETATM 4419 O O   . HOH   E 5 .   ? -18.747 1.357   -22.338 1.00 52.41  ? 1590 HOH   A O   1 
HETATM 4420 O O   . HOH   E 5 .   ? -8.909  2.376   -11.415 1.00 48.82  ? 1591 HOH   A O   1 
HETATM 4421 O O   . HOH   E 5 .   ? 39.638  32.958  1.851   1.00 36.35  ? 1592 HOH   A O   1 
HETATM 4422 O O   . HOH   E 5 .   ? 19.735  16.012  4.700   1.00 52.93  ? 1593 HOH   A O   1 
HETATM 4423 O O   . HOH   E 5 .   ? 40.059  4.886   8.267   1.00 59.84  ? 1594 HOH   A O   1 
HETATM 4424 O O   . HOH   E 5 .   ? 28.069  -5.303  -25.263 1.00 49.92  ? 1595 HOH   A O   1 
HETATM 4425 O O   . HOH   E 5 .   ? -21.313 -0.152  -15.080 1.00 43.91  ? 1596 HOH   A O   1 
HETATM 4426 O O   . HOH   E 5 .   ? 3.786   11.209  -0.407  1.00 62.57  ? 1597 HOH   A O   1 
HETATM 4427 O O   . HOH   E 5 .   ? -6.782  -22.321 -14.916 1.00 46.74  ? 1598 HOH   A O   1 
HETATM 4428 O O   . HOH   E 5 .   ? 20.587  -3.781  -26.511 1.00 49.41  ? 1599 HOH   A O   1 
HETATM 4429 O O   . HOH   E 5 .   ? -14.668 1.448   -24.183 1.00 45.00  ? 1600 HOH   A O   1 
HETATM 4430 O O   . HOH   E 5 .   ? 27.931  -7.914  1.037   1.00 44.12  ? 1601 HOH   A O   1 
HETATM 4431 O O   . HOH   E 5 .   ? 25.252  -3.632  14.537  1.00 62.30  ? 1602 HOH   A O   1 
HETATM 4432 O O   . HOH   E 5 .   ? 24.866  -9.723  -2.406  1.00 57.54  ? 1603 HOH   A O   1 
HETATM 4433 O O   . HOH   E 5 .   ? -5.533  4.844   -1.122  1.00 49.66  ? 1604 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   . SER A 2   ? 0.8718 0.8585 0.8152 0.0002  -0.0968 -0.0538 -27  SER A N   
2    C CA  . SER A 2   ? 0.8471 0.8323 0.7839 0.0013  -0.1064 -0.0492 -27  SER A CA  
3    C C   . SER A 2   ? 0.7757 0.7519 0.7066 0.0027  -0.1033 -0.0428 -27  SER A C   
4    O O   . SER A 2   ? 0.7300 0.6998 0.6479 0.0002  -0.1068 -0.0389 -27  SER A O   
5    C CB  . SER A 2   ? 0.8689 0.8631 0.8180 0.0067  -0.1170 -0.0492 -27  SER A CB  
6    O OG  . SER A 2   ? 0.9972 1.0023 0.9523 0.0048  -0.1198 -0.0561 -27  SER A OG  
7    N N   . TYR A 3   ? 0.7086 0.6850 0.6486 0.0060  -0.0969 -0.0419 -26  TYR A N   
8    C CA  . TYR A 3   ? 0.6488 0.6192 0.5846 0.0064  -0.0917 -0.0375 -26  TYR A CA  
9    C C   . TYR A 3   ? 0.6329 0.6026 0.5699 0.0059  -0.0801 -0.0397 -26  TYR A C   
10   O O   . TYR A 3   ? 0.5962 0.5700 0.5420 0.0077  -0.0767 -0.0429 -26  TYR A O   
11   C CB  . TYR A 3   ? 0.6459 0.6187 0.5920 0.0114  -0.0951 -0.0341 -26  TYR A CB  
12   C CG  . TYR A 3   ? 0.7754 0.7449 0.7186 0.0128  -0.1058 -0.0307 -26  TYR A CG  
13   C CD1 . TYR A 3   ? 0.9416 0.9172 0.8935 0.0162  -0.1146 -0.0329 -26  TYR A CD1 
14   C CD2 . TYR A 3   ? 0.8016 0.7614 0.7333 0.0107  -0.1071 -0.0253 -26  TYR A CD2 
15   C CE1 . TYR A 3   ? 0.9600 0.9318 0.9099 0.0191  -0.1249 -0.0293 -26  TYR A CE1 
16   C CE2 . TYR A 3   ? 0.8696 0.8235 0.7974 0.0125  -0.1172 -0.0212 -26  TYR A CE2 
17   C CZ  . TYR A 3   ? 0.8699 0.8296 0.8072 0.0175  -0.1264 -0.0230 -26  TYR A CZ  
18   O OH  . TYR A 3   ? 0.7802 0.7335 0.7146 0.0209  -0.1368 -0.0186 -26  TYR A OH  
19   N N   . TYR A 4   ? 0.5620 0.5262 0.4898 0.0036  -0.0739 -0.0382 -25  TYR A N   
20   C CA  . TYR A 4   ? 0.5881 0.5511 0.5166 0.0040  -0.0630 -0.0405 -25  TYR A CA  
21   C C   . TYR A 4   ? 0.6235 0.5873 0.5522 0.0055  -0.0580 -0.0375 -25  TYR A C   
22   O O   . TYR A 4   ? 0.7143 0.6766 0.6377 0.0034  -0.0616 -0.0342 -25  TYR A O   
23   C CB  . TYR A 4   ? 0.5824 0.5393 0.4987 -0.0016 -0.0585 -0.0447 -25  TYR A CB  
24   C CG  . TYR A 4   ? 0.5315 0.4891 0.4470 -0.0043 -0.0626 -0.0487 -25  TYR A CG  
25   C CD1 . TYR A 4   ? 0.4751 0.4332 0.3980 -0.0030 -0.0580 -0.0525 -25  TYR A CD1 
26   C CD2 . TYR A 4   ? 0.4630 0.4214 0.3703 -0.0085 -0.0714 -0.0487 -25  TYR A CD2 
27   C CE1 . TYR A 4   ? 0.4941 0.4542 0.4164 -0.0069 -0.0613 -0.0572 -25  TYR A CE1 
28   C CE2 . TYR A 4   ? 0.4630 0.4252 0.3706 -0.0113 -0.0756 -0.0532 -25  TYR A CE2 
29   C CZ  . TYR A 4   ? 0.5402 0.5037 0.4557 -0.0110 -0.0702 -0.0579 -25  TYR A CZ  
30   O OH  . TYR A 4   ? 0.5313 0.4998 0.4469 -0.0151 -0.0738 -0.0633 -25  TYR A OH  
31   N N   . HIS A 5   ? 0.5543 0.5205 0.4893 0.0091  -0.0495 -0.0387 -24  HIS A N   
32   C CA  . HIS A 5   ? 0.6041 0.5737 0.5401 0.0105  -0.0435 -0.0373 -24  HIS A CA  
33   C C   . HIS A 5   ? 0.5697 0.5339 0.4937 0.0057  -0.0372 -0.0401 -24  HIS A C   
34   O O   . HIS A 5   ? 0.5797 0.5388 0.5002 0.0051  -0.0322 -0.0440 -24  HIS A O   
35   C CB  . HIS A 5   ? 0.5213 0.4974 0.4697 0.0174  -0.0377 -0.0371 -24  HIS A CB  
36   C CG  . HIS A 5   ? 0.7985 0.7814 0.7495 0.0194  -0.0317 -0.0364 -24  HIS A CG  
37   N ND1 . HIS A 5   ? 0.8861 0.8686 0.8362 0.0215  -0.0229 -0.0391 -24  HIS A ND1 
38   C CD2 . HIS A 5   ? 0.8373 0.8282 0.7920 0.0190  -0.0330 -0.0342 -24  HIS A CD2 
39   C CE1 . HIS A 5   ? 0.9211 0.9130 0.8751 0.0229  -0.0193 -0.0386 -24  HIS A CE1 
40   N NE2 . HIS A 5   ? 0.8693 0.8665 0.8257 0.0208  -0.0252 -0.0357 -24  HIS A NE2 
41   N N   . HIS A 6   ? 0.6560 0.6209 0.5732 0.0018  -0.0366 -0.0387 -23  HIS A N   
42   C CA  . HIS A 6   ? 0.7128 0.6738 0.6178 -0.0039 -0.0303 -0.0418 -23  HIS A CA  
43   C C   . HIS A 6   ? 0.7229 0.6904 0.6348 0.0000  -0.0199 -0.0447 -23  HIS A C   
44   O O   . HIS A 6   ? 0.7568 0.7326 0.6743 0.0014  -0.0183 -0.0431 -23  HIS A O   
45   C CB  . HIS A 6   ? 0.7011 0.6589 0.5933 -0.0113 -0.0346 -0.0389 -23  HIS A CB  
46   C CG  . HIS A 6   ? 0.6291 0.5801 0.5133 -0.0144 -0.0452 -0.0358 -23  HIS A CG  
47   N ND1 . HIS A 6   ? 0.6421 0.5860 0.5089 -0.0222 -0.0479 -0.0356 -23  HIS A ND1 
48   C CD2 . HIS A 6   ? 0.6473 0.5987 0.5389 -0.0104 -0.0541 -0.0332 -23  HIS A CD2 
49   C CE1 . HIS A 6   ? 0.7697 0.7101 0.6338 -0.0221 -0.0585 -0.0324 -23  HIS A CE1 
50   N NE2 . HIS A 6   ? 0.7042 0.6492 0.5838 -0.0148 -0.0622 -0.0313 -23  HIS A NE2 
51   N N   . LEU A 25  ? 0.8745 0.8201 0.8021 0.0276  0.0613  -0.0930 -4   LEU A N   
52   C CA  . LEU A 25  ? 0.8357 0.7887 0.7655 0.0280  0.0715  -0.1012 -4   LEU A CA  
53   C C   . LEU A 25  ? 0.8066 0.7465 0.7246 0.0203  0.0800  -0.1111 -4   LEU A C   
54   O O   . LEU A 25  ? 1.0211 0.9641 0.9266 0.0079  0.0815  -0.1159 -4   LEU A O   
55   C CB  . LEU A 25  ? 0.8873 0.8470 0.8351 0.0440  0.0769  -0.1010 -4   LEU A CB  
56   C CG  . LEU A 25  ? 0.8711 0.8532 0.8286 0.0469  0.0797  -0.1031 -4   LEU A CG  
57   C CD1 . LEU A 25  ? 0.8507 0.8375 0.7976 0.0345  0.0862  -0.1123 -4   LEU A CD1 
58   C CD2 . LEU A 25  ? 0.8459 0.8418 0.8075 0.0465  0.0695  -0.0942 -4   LEU A CD2 
59   N N   . TYR A 26  ? 0.5817 0.5066 0.5031 0.0270  0.0861  -0.1143 -3   TYR A N   
60   C CA  . TYR A 26  ? 0.5418 0.4525 0.4523 0.0195  0.0949  -0.1244 -3   TYR A CA  
61   C C   . TYR A 26  ? 0.5456 0.4402 0.4454 0.0126  0.0902  -0.1227 -3   TYR A C   
62   O O   . TYR A 26  ? 0.5631 0.4437 0.4546 0.0071  0.0976  -0.1310 -3   TYR A O   
63   C CB  . TYR A 26  ? 0.6388 0.5429 0.5601 0.0313  0.1072  -0.1312 -3   TYR A CB  
64   C CG  . TYR A 26  ? 0.5889 0.5124 0.5225 0.0384  0.1115  -0.1337 -3   TYR A CG  
65   C CD1 . TYR A 26  ? 0.6790 0.6145 0.6057 0.0277  0.1159  -0.1414 -3   TYR A CD1 
66   C CD2 . TYR A 26  ? 0.6754 0.6066 0.6270 0.0550  0.1111  -0.1285 -3   TYR A CD2 
67   C CE1 . TYR A 26  ? 0.6951 0.6502 0.6332 0.0329  0.1204  -0.1447 -3   TYR A CE1 
68   C CE2 . TYR A 26  ? 0.5396 0.4919 0.5035 0.0613  0.1149  -0.1316 -3   TYR A CE2 
69   C CZ  . TYR A 26  ? 0.6268 0.5911 0.5842 0.0498  0.1199  -0.1402 -3   TYR A CZ  
70   O OH  . TYR A 26  ? 0.6211 0.6078 0.5906 0.0545  0.1243  -0.1445 -3   TYR A OH  
71   N N   . PHE A 27  ? 0.5302 0.4277 0.4303 0.0123  0.0785  -0.1132 -2   PHE A N   
72   C CA  . PHE A 27  ? 0.6011 0.4874 0.4929 0.0059  0.0728  -0.1113 -2   PHE A CA  
73   C C   . PHE A 27  ? 0.5386 0.4350 0.4329 0.0058  0.0594  -0.1011 -2   PHE A C   
74   O O   . PHE A 27  ? 0.5099 0.4151 0.4163 0.0155  0.0562  -0.0944 -2   PHE A O   
75   C CB  . PHE A 27  ? 0.5402 0.4092 0.4372 0.0137  0.0785  -0.1121 -2   PHE A CB  
76   C CG  . PHE A 27  ? 0.5402 0.3997 0.4301 0.0069  0.0728  -0.1103 -2   PHE A CG  
77   C CD1 . PHE A 27  ? 0.5545 0.4054 0.4308 -0.0057 0.0758  -0.1184 -2   PHE A CD1 
78   C CD2 . PHE A 27  ? 0.5265 0.3873 0.4235 0.0126  0.0649  -0.1013 -2   PHE A CD2 
79   C CE1 . PHE A 27  ? 0.5545 0.3994 0.4252 -0.0124 0.0706  -0.1177 -2   PHE A CE1 
80   C CE2 . PHE A 27  ? 0.5864 0.4403 0.4776 0.0058  0.0601  -0.1008 -2   PHE A CE2 
81   C CZ  . PHE A 27  ? 0.5404 0.3870 0.4190 -0.0065 0.0628  -0.1090 -2   PHE A CZ  
82   N N   . GLN A 28  ? 0.5105 0.4066 0.3936 -0.0049 0.0516  -0.1004 -1   GLN A N   
83   C CA  . GLN A 28  ? 0.4938 0.3986 0.3788 -0.0054 0.0388  -0.0917 -1   GLN A CA  
84   C C   . GLN A 28  ? 0.5147 0.4118 0.4039 -0.0026 0.0352  -0.0890 -1   GLN A C   
85   O O   . GLN A 28  ? 0.4995 0.3881 0.3805 -0.0099 0.0359  -0.0937 -1   GLN A O   
86   C CB  . GLN A 28  ? 0.5045 0.4141 0.3756 -0.0175 0.0314  -0.0918 -1   GLN A CB  
87   C CG  . GLN A 28  ? 0.8523 0.7720 0.7197 -0.0204 0.0311  -0.0905 -1   GLN A CG  
88   C CD  . GLN A 28  ? 0.9868 0.9083 0.8374 -0.0328 0.0240  -0.0900 -1   GLN A CD  
89   O OE1 . GLN A 28  ? 0.9820 0.9101 0.8307 -0.0341 0.0161  -0.0834 -1   GLN A OE1 
90   N NE2 . GLN A 28  ? 0.5187 0.4341 0.3564 -0.0420 0.0270  -0.0968 -1   GLN A NE2 
91   N N   . GLU A 29  ? 0.4762 0.3774 0.3779 0.0072  0.0319  -0.0820 566  GLU A N   
92   C CA  . GLU A 29  ? 0.6203 0.5162 0.5262 0.0094  0.0280  -0.0787 566  GLU A CA  
93   C C   . GLU A 29  ? 0.4941 0.3975 0.3968 0.0027  0.0162  -0.0757 566  GLU A C   
94   O O   . GLU A 29  ? 0.4740 0.3867 0.3733 -0.0010 0.0100  -0.0738 566  GLU A O   
95   C CB  . GLU A 29  ? 0.7277 0.6271 0.6471 0.0217  0.0281  -0.0719 566  GLU A CB  
96   C CG  . GLU A 29  ? 0.9957 0.8900 0.9206 0.0309  0.0384  -0.0736 566  GLU A CG  
97   C CD  . GLU A 29  ? 1.1780 1.0785 1.1160 0.0434  0.0371  -0.0661 566  GLU A CD  
98   O OE1 . GLU A 29  ? 1.1919 1.1043 1.1351 0.0441  0.0284  -0.0599 566  GLU A OE1 
99   O OE2 . GLU A 29  ? 1.2109 1.1041 1.1537 0.0526  0.0448  -0.0665 566  GLU A OE2 
100  N N   . GLN A 30  ? 0.5697 0.4686 0.4735 0.0013  0.0135  -0.0756 567  GLN A N   
101  C CA  . GLN A 30  ? 0.4974 0.4045 0.4013 -0.0032 0.0023  -0.0732 567  GLN A CA  
102  C C   . GLN A 30  ? 0.4611 0.3808 0.3739 0.0024  -0.0055 -0.0658 567  GLN A C   
103  O O   . GLN A 30  ? 0.4612 0.3832 0.3836 0.0108  -0.0032 -0.0615 567  GLN A O   
104  C CB  . GLN A 30  ? 0.5978 0.4992 0.5045 -0.0041 0.0026  -0.0744 567  GLN A CB  
105  C CG  . GLN A 30  ? 0.6565 0.5674 0.5650 -0.0086 -0.0080 -0.0737 567  GLN A CG  
106  C CD  . GLN A 30  ? 0.7831 0.6906 0.6969 -0.0081 -0.0070 -0.0739 567  GLN A CD  
107  O OE1 . GLN A 30  ? 0.7991 0.7073 0.7216 -0.0008 -0.0063 -0.0686 567  GLN A OE1 
108  N NE2 . GLN A 30  ? 0.9186 0.8232 0.8267 -0.0167 -0.0067 -0.0803 567  GLN A NE2 
109  N N   . PRO A 31  ? 0.4426 0.3704 0.3522 -0.0019 -0.0148 -0.0640 568  PRO A N   
110  C CA  . PRO A 31  ? 0.4261 0.3639 0.3435 0.0028  -0.0216 -0.0576 568  PRO A CA  
111  C C   . PRO A 31  ? 0.4978 0.4401 0.4265 0.0072  -0.0260 -0.0546 568  PRO A C   
112  O O   . PRO A 31  ? 0.4722 0.4128 0.4011 0.0043  -0.0281 -0.0572 568  PRO A O   
113  C CB  . PRO A 31  ? 0.4787 0.4200 0.3876 -0.0036 -0.0303 -0.0568 568  PRO A CB  
114  C CG  . PRO A 31  ? 0.5113 0.4462 0.4072 -0.0115 -0.0272 -0.0627 568  PRO A CG  
115  C CD  . PRO A 31  ? 0.4839 0.4114 0.3817 -0.0111 -0.0194 -0.0676 568  PRO A CD  
116  N N   . LEU A 32  ? 0.4361 0.3858 0.3742 0.0134  -0.0273 -0.0497 569  LEU A N   
117  C CA  . LEU A 32  ? 0.4056 0.3617 0.3542 0.0171  -0.0320 -0.0467 569  LEU A CA  
118  C C   . LEU A 32  ? 0.5243 0.4866 0.4738 0.0137  -0.0424 -0.0463 569  LEU A C   
119  O O   . LEU A 32  ? 0.4472 0.4119 0.3933 0.0124  -0.0468 -0.0444 569  LEU A O   
120  C CB  . LEU A 32  ? 0.4587 0.4223 0.4163 0.0240  -0.0300 -0.0421 569  LEU A CB  
121  C CG  . LEU A 32  ? 0.5629 0.5342 0.5315 0.0283  -0.0329 -0.0390 569  LEU A CG  
122  C CD1 . LEU A 32  ? 0.6359 0.6003 0.6052 0.0301  -0.0279 -0.0396 569  LEU A CD1 
123  C CD2 . LEU A 32  ? 0.5844 0.5654 0.5599 0.0336  -0.0316 -0.0351 569  LEU A CD2 
124  N N   . ARG A 33  ? 0.5138 0.4783 0.4676 0.0123  -0.0462 -0.0483 570  ARG A N   
125  C CA  . ARG A 33  ? 0.6083 0.5798 0.5651 0.0107  -0.0564 -0.0485 570  ARG A CA  
126  C C   . ARG A 33  ? 0.5039 0.4840 0.4722 0.0156  -0.0600 -0.0448 570  ARG A C   
127  O O   . ARG A 33  ? 0.4598 0.4431 0.4356 0.0189  -0.0562 -0.0438 570  ARG A O   
128  C CB  . ARG A 33  ? 0.6113 0.5844 0.5693 0.0067  -0.0589 -0.0535 570  ARG A CB  
129  C CG  . ARG A 33  ? 0.7380 0.7191 0.6987 0.0055  -0.0698 -0.0546 570  ARG A CG  
130  C CD  . ARG A 33  ? 0.8368 0.8203 0.7951 -0.0001 -0.0721 -0.0609 570  ARG A CD  
131  N NE  . ARG A 33  ? 0.8483 0.8386 0.8169 -0.0002 -0.0717 -0.0642 570  ARG A NE  
132  C CZ  . ARG A 33  ? 0.7962 0.7982 0.7751 0.0011  -0.0796 -0.0661 570  ARG A CZ  
133  N NH1 . ARG A 33  ? 0.6644 0.6711 0.6445 0.0037  -0.0890 -0.0643 570  ARG A NH1 
134  N NH2 . ARG A 33  ? 0.8085 0.8171 0.7960 -0.0002 -0.0779 -0.0699 570  ARG A NH2 
135  N N   . LEU A 34  ? 0.3989 0.3823 0.3677 0.0158  -0.0673 -0.0428 571  LEU A N   
136  C CA  . LEU A 34  ? 0.3853 0.3757 0.3638 0.0195  -0.0703 -0.0400 571  LEU A CA  
137  C C   . LEU A 34  ? 0.3694 0.3648 0.3541 0.0198  -0.0796 -0.0415 571  LEU A C   
138  O O   . LEU A 34  ? 0.4064 0.3999 0.3863 0.0174  -0.0851 -0.0435 571  LEU A O   
139  C CB  . LEU A 34  ? 0.4485 0.4366 0.4222 0.0197  -0.0692 -0.0362 571  LEU A CB  
140  C CG  . LEU A 34  ? 0.4761 0.4618 0.4453 0.0202  -0.0601 -0.0352 571  LEU A CG  
141  C CD1 . LEU A 34  ? 0.5715 0.5564 0.5355 0.0186  -0.0599 -0.0326 571  LEU A CD1 
142  C CD2 . LEU A 34  ? 0.4655 0.4577 0.4444 0.0249  -0.0548 -0.0345 571  LEU A CD2 
143  N N   . PRO A 35  ? 0.3625 0.3652 0.3583 0.0228  -0.0818 -0.0410 572  PRO A N   
144  C CA  . PRO A 35  ? 0.3843 0.3912 0.3869 0.0241  -0.0906 -0.0427 572  PRO A CA  
145  C C   . PRO A 35  ? 0.4604 0.4596 0.4550 0.0240  -0.0962 -0.0392 572  PRO A C   
146  O O   . PRO A 35  ? 0.4219 0.4141 0.4067 0.0222  -0.0927 -0.0356 572  PRO A O   
147  C CB  . PRO A 35  ? 0.4403 0.4559 0.4556 0.0267  -0.0894 -0.0431 572  PRO A CB  
148  C CG  . PRO A 35  ? 0.3946 0.4091 0.4067 0.0269  -0.0818 -0.0395 572  PRO A CG  
149  C CD  . PRO A 35  ? 0.3239 0.3324 0.3270 0.0253  -0.0764 -0.0393 572  PRO A CD  
150  N N   . SER A 36  ? 0.4144 0.4151 0.4135 0.0261  -0.1051 -0.0403 573  SER A N   
151  C CA  . SER A 36  ? 0.4410 0.4327 0.4322 0.0267  -0.1117 -0.0362 573  SER A CA  
152  C C   . SER A 36  ? 0.4558 0.4437 0.4491 0.0278  -0.1097 -0.0330 573  SER A C   
153  O O   . SER A 36  ? 0.4974 0.4930 0.5026 0.0294  -0.1067 -0.0353 573  SER A O   
154  C CB  . SER A 36  ? 0.5084 0.5034 0.5057 0.0303  -0.1222 -0.0384 573  SER A CB  
155  O OG  . SER A 36  ? 0.6146 0.5999 0.6074 0.0328  -0.1287 -0.0337 573  SER A OG  
156  N N   . PRO A 37  ? 0.4434 0.4197 0.4242 0.0257  -0.1110 -0.0280 574  PRO A N   
157  C CA  . PRO A 37  ? 0.5658 0.5376 0.5480 0.0256  -0.1094 -0.0256 574  PRO A CA  
158  C C   . PRO A 37  ? 0.6010 0.5732 0.5945 0.0303  -0.1161 -0.0272 574  PRO A C   
159  O O   . PRO A 37  ? 0.5756 0.5478 0.5749 0.0303  -0.1134 -0.0276 574  PRO A O   
160  C CB  . PRO A 37  ? 0.6494 0.6070 0.6134 0.0214  -0.1102 -0.0200 574  PRO A CB  
161  C CG  . PRO A 37  ? 0.6633 0.6209 0.6171 0.0186  -0.1091 -0.0202 574  PRO A CG  
162  C CD  . PRO A 37  ? 0.5150 0.4820 0.4789 0.0222  -0.1130 -0.0247 574  PRO A CD  
163  N N   . GLU A 38  ? 0.5609 0.5344 0.5583 0.0344  -0.1246 -0.0288 575  GLU A N   
164  C CA  . GLU A 38  ? 0.6376 0.6127 0.6480 0.0400  -0.1310 -0.0315 575  GLU A CA  
165  C C   . GLU A 38  ? 0.5395 0.5286 0.5667 0.0407  -0.1257 -0.0376 575  GLU A C   
166  O O   . GLU A 38  ? 0.6164 0.6058 0.6538 0.0435  -0.1273 -0.0401 575  GLU A O   
167  C CB  . GLU A 38  ? 0.7908 0.7692 0.8043 0.0447  -0.1409 -0.0332 575  GLU A CB  
168  C CG  . GLU A 38  ? 1.0325 0.9964 1.0317 0.0462  -0.1495 -0.0266 575  GLU A CG  
169  C CD  . GLU A 38  ? 1.2319 1.1871 1.2110 0.0394  -0.1457 -0.0213 575  GLU A CD  
170  O OE1 . GLU A 38  ? 1.2701 1.2116 1.2375 0.0363  -0.1433 -0.0157 575  GLU A OE1 
171  O OE2 . GLU A 38  ? 1.2549 1.2172 1.2299 0.0366  -0.1446 -0.0232 575  GLU A OE2 
172  N N   . VAL A 39  ? 0.4342 0.4339 0.4637 0.0379  -0.1192 -0.0401 576  VAL A N   
173  C CA  . VAL A 39  ? 0.4028 0.4159 0.4460 0.0378  -0.1141 -0.0451 576  VAL A CA  
174  C C   . VAL A 39  ? 0.4892 0.5044 0.5291 0.0342  -0.1050 -0.0429 576  VAL A C   
175  O O   . VAL A 39  ? 0.4923 0.5184 0.5422 0.0338  -0.1009 -0.0461 576  VAL A O   
176  C CB  . VAL A 39  ? 0.4180 0.4430 0.4681 0.0378  -0.1141 -0.0502 576  VAL A CB  
177  C CG1 . VAL A 39  ? 0.5199 0.5472 0.5765 0.0418  -0.1233 -0.0539 576  VAL A CG1 
178  C CG2 . VAL A 39  ? 0.4088 0.4312 0.4474 0.0344  -0.1097 -0.0479 576  VAL A CG2 
179  N N   . TYR A 40  ? 0.4318 0.4382 0.4583 0.0315  -0.1019 -0.0379 577  TYR A N   
180  C CA  . TYR A 40  ? 0.3460 0.3569 0.3707 0.0288  -0.0935 -0.0363 577  TYR A CA  
181  C C   . TYR A 40  ? 0.4036 0.4030 0.4144 0.0257  -0.0919 -0.0316 577  TYR A C   
182  O O   . TYR A 40  ? 0.4451 0.4385 0.4449 0.0241  -0.0912 -0.0294 577  TYR A O   
183  C CB  . TYR A 40  ? 0.3354 0.3537 0.3605 0.0288  -0.0883 -0.0370 577  TYR A CB  
184  C CG  . TYR A 40  ? 0.3299 0.3557 0.3561 0.0280  -0.0804 -0.0356 577  TYR A CG  
185  C CD1 . TYR A 40  ? 0.3382 0.3754 0.3746 0.0282  -0.0783 -0.0373 577  TYR A CD1 
186  C CD2 . TYR A 40  ? 0.3828 0.4056 0.4001 0.0273  -0.0751 -0.0329 577  TYR A CD2 
187  C CE1 . TYR A 40  ? 0.3364 0.3828 0.3740 0.0281  -0.0718 -0.0357 577  TYR A CE1 
188  C CE2 . TYR A 40  ? 0.3027 0.3341 0.3223 0.0279  -0.0684 -0.0317 577  TYR A CE2 
189  C CZ  . TYR A 40  ? 0.3384 0.3819 0.3679 0.0285  -0.0672 -0.0327 577  TYR A CZ  
190  O OH  . TYR A 40  ? 0.2986 0.3527 0.3306 0.0296  -0.0615 -0.0312 577  TYR A OH  
191  N N   . ARG A 41  ? 0.3858 0.3823 0.3969 0.0238  -0.0909 -0.0309 578  ARG A N   
192  C CA  . ARG A 41  ? 0.5124 0.4961 0.5097 0.0196  -0.0903 -0.0268 578  ARG A CA  
193  C C   . ARG A 41  ? 0.4576 0.4433 0.4457 0.0163  -0.0835 -0.0250 578  ARG A C   
194  O O   . ARG A 41  ? 0.4394 0.4141 0.4134 0.0125  -0.0834 -0.0218 578  ARG A O   
195  C CB  . ARG A 41  ? 0.4862 0.4687 0.4866 0.0168  -0.0881 -0.0275 578  ARG A CB  
196  C CG  . ARG A 41  ? 0.6583 0.6323 0.6637 0.0195  -0.0947 -0.0286 578  ARG A CG  
197  C CD  . ARG A 41  ? 0.5955 0.5606 0.5967 0.0147  -0.0919 -0.0279 578  ARG A CD  
198  N NE  . ARG A 41  ? 0.4957 0.4759 0.5076 0.0121  -0.0853 -0.0325 578  ARG A NE  
199  C CZ  . ARG A 41  ? 0.5429 0.5201 0.5529 0.0064  -0.0809 -0.0336 578  ARG A CZ  
200  N NH1 . ARG A 41  ? 0.5509 0.5448 0.5713 0.0039  -0.0753 -0.0383 578  ARG A NH1 
201  N NH2 . ARG A 41  ? 0.5297 0.4874 0.5265 0.0025  -0.0821 -0.0300 578  ARG A NH2 
202  N N   . PHE A 42  ? 0.4031 0.4023 0.3986 0.0176  -0.0775 -0.0270 579  PHE A N   
203  C CA  . PHE A 42  ? 0.3971 0.4005 0.3870 0.0152  -0.0700 -0.0261 579  PHE A CA  
204  C C   . PHE A 42  ? 0.5485 0.5454 0.5282 0.0149  -0.0691 -0.0250 579  PHE A C   
205  O O   . PHE A 42  ? 0.6451 0.6435 0.6188 0.0126  -0.0629 -0.0247 579  PHE A O   
206  C CB  . PHE A 42  ? 0.3975 0.4177 0.3991 0.0180  -0.0647 -0.0280 579  PHE A CB  
207  C CG  . PHE A 42  ? 0.3976 0.4265 0.4086 0.0170  -0.0646 -0.0298 579  PHE A CG  
208  C CD1 . PHE A 42  ? 0.3481 0.3818 0.3577 0.0127  -0.0600 -0.0301 579  PHE A CD1 
209  C CD2 . PHE A 42  ? 0.3333 0.3662 0.3545 0.0195  -0.0686 -0.0320 579  PHE A CD2 
210  C CE1 . PHE A 42  ? 0.3688 0.4107 0.3866 0.0106  -0.0595 -0.0326 579  PHE A CE1 
211  C CE2 . PHE A 42  ? 0.3228 0.3639 0.3525 0.0179  -0.0680 -0.0347 579  PHE A CE2 
212  C CZ  . PHE A 42  ? 0.3440 0.3894 0.3718 0.0133  -0.0634 -0.0349 579  PHE A CZ  
213  N N   . VAL A 43  ? 0.4424 0.4333 0.4202 0.0167  -0.0747 -0.0252 580  VAL A N   
214  C CA  . VAL A 43  ? 0.4788 0.4650 0.4474 0.0157  -0.0729 -0.0253 580  VAL A CA  
215  C C   . VAL A 43  ? 0.5060 0.4793 0.4590 0.0111  -0.0767 -0.0228 580  VAL A C   
216  O O   . VAL A 43  ? 0.5600 0.5289 0.5037 0.0091  -0.0760 -0.0232 580  VAL A O   
217  C CB  . VAL A 43  ? 0.5163 0.5052 0.4909 0.0189  -0.0754 -0.0278 580  VAL A CB  
218  C CG1 . VAL A 43  ? 0.5863 0.5863 0.5727 0.0225  -0.0703 -0.0294 580  VAL A CG1 
219  C CG2 . VAL A 43  ? 0.4955 0.4826 0.4744 0.0205  -0.0846 -0.0284 580  VAL A CG2 
220  N N   . VAL A 44  ? 0.4764 0.4429 0.4253 0.0089  -0.0803 -0.0200 581  VAL A N   
221  C CA  . VAL A 44  ? 0.5269 0.4798 0.4586 0.0038  -0.0835 -0.0164 581  VAL A CA  
222  C C   . VAL A 44  ? 0.5503 0.5035 0.4713 -0.0015 -0.0752 -0.0170 581  VAL A C   
223  O O   . VAL A 44  ? 0.5251 0.4873 0.4516 -0.0021 -0.0673 -0.0190 581  VAL A O   
224  C CB  . VAL A 44  ? 0.5639 0.5080 0.4925 0.0017  -0.0867 -0.0131 581  VAL A CB  
225  C CG1 . VAL A 44  ? 0.6922 0.6210 0.6002 -0.0047 -0.0886 -0.0084 581  VAL A CG1 
226  C CG2 . VAL A 44  ? 0.7248 0.6669 0.6633 0.0076  -0.0954 -0.0130 581  VAL A CG2 
227  N N   . LYS A 45  ? 0.5796 0.5246 0.4858 -0.0055 -0.0771 -0.0157 582  LYS A N   
228  C CA  . LYS A 45  ? 0.4855 0.4310 0.3815 -0.0109 -0.0688 -0.0175 582  LYS A CA  
229  C C   . LYS A 45  ? 0.5245 0.4691 0.4148 -0.0167 -0.0632 -0.0164 582  LYS A C   
230  O O   . LYS A 45  ? 0.5055 0.4408 0.3890 -0.0198 -0.0675 -0.0123 582  LYS A O   
231  C CB  . LYS A 45  ? 0.6059 0.5423 0.4851 -0.0157 -0.0725 -0.0163 582  LYS A CB  
232  C CG  . LYS A 45  ? 0.7892 0.7267 0.6581 -0.0217 -0.0633 -0.0196 582  LYS A CG  
233  C CD  . LYS A 45  ? 0.8594 0.7888 0.7106 -0.0275 -0.0670 -0.0189 582  LYS A CD  
234  C CE  . LYS A 45  ? 0.8579 0.7888 0.6990 -0.0343 -0.0568 -0.0233 582  LYS A CE  
235  N NZ  . LYS A 45  ? 0.8798 0.8091 0.7129 -0.0407 -0.0514 -0.0219 582  LYS A NZ  
236  N N   . ASP A 46  ? 0.5196 0.4738 0.4125 -0.0182 -0.0532 -0.0202 583  ASP A N   
237  C CA  . ASP A 46  ? 0.5262 0.4821 0.4131 -0.0250 -0.0467 -0.0206 583  ASP A CA  
238  C C   . ASP A 46  ? 0.5831 0.5248 0.4479 -0.0344 -0.0484 -0.0175 583  ASP A C   
239  O O   . ASP A 46  ? 0.6280 0.5638 0.4824 -0.0361 -0.0505 -0.0174 583  ASP A O   
240  C CB  . ASP A 46  ? 0.5717 0.5420 0.4655 -0.0241 -0.0360 -0.0262 583  ASP A CB  
241  C CG  . ASP A 46  ? 0.5832 0.5685 0.4974 -0.0155 -0.0337 -0.0282 583  ASP A CG  
242  O OD1 . ASP A 46  ? 0.5465 0.5325 0.4696 -0.0117 -0.0394 -0.0261 583  ASP A OD1 
243  O OD2 . ASP A 46  ? 0.6121 0.6088 0.5334 -0.0124 -0.0262 -0.0321 583  ASP A OD2 
244  N N   . SER A 47  ? 0.6818 0.6176 0.5383 -0.0414 -0.0474 -0.0150 584  SER A N   
245  C CA  . SER A 47  ? 0.6098 0.5319 0.4432 -0.0518 -0.0476 -0.0118 584  SER A CA  
246  C C   . SER A 47  ? 0.6942 0.6157 0.5225 -0.0603 -0.0414 -0.0119 584  SER A C   
247  O O   . SER A 47  ? 0.6868 0.6168 0.5290 -0.0577 -0.0391 -0.0138 584  SER A O   
248  C CB  . SER A 47  ? 0.6289 0.5330 0.4505 -0.0511 -0.0596 -0.0046 584  SER A CB  
249  O OG  . SER A 47  ? 0.6202 0.5145 0.4421 -0.0511 -0.0640 -0.0002 584  SER A OG  
250  N N   . GLU A 48  ? 0.6632 0.5747 0.4701 -0.0715 -0.0387 -0.0102 585  GLU A N   
251  C CA  . GLU A 48  ? 0.8229 0.7304 0.6207 -0.0819 -0.0331 -0.0098 585  GLU A CA  
252  C C   . GLU A 48  ? 0.7607 0.6553 0.5600 -0.0804 -0.0397 -0.0045 585  GLU A C   
253  O O   . GLU A 48  ? 0.7317 0.6266 0.5303 -0.0872 -0.0343 -0.0058 585  GLU A O   
254  C CB  . GLU A 48  ? 0.9883 0.8826 0.7591 -0.0950 -0.0310 -0.0071 585  GLU A CB  
255  C CG  . GLU A 48  ? 1.2184 1.1251 0.9865 -0.0982 -0.0232 -0.0136 585  GLU A CG  
256  C CD  . GLU A 48  ? 1.3423 1.2707 1.1234 -0.1004 -0.0106 -0.0227 585  GLU A CD  
257  O OE1 . GLU A 48  ? 1.3974 1.3265 1.1742 -0.1092 -0.0052 -0.0236 585  GLU A OE1 
258  O OE2 . GLU A 48  ? 1.3708 1.3155 1.1666 -0.0932 -0.0060 -0.0291 585  GLU A OE2 
259  N N   . GLU A 49  ? 0.7391 0.6232 0.5411 -0.0718 -0.0508 0.0007  586  GLU A N   
260  C CA  . GLU A 49  ? 0.7090 0.5798 0.5133 -0.0692 -0.0572 0.0052  586  GLU A CA  
261  C C   . GLU A 49  ? 0.5770 0.4633 0.4067 -0.0608 -0.0560 0.0003  586  GLU A C   
262  O O   . GLU A 49  ? 0.5569 0.4342 0.3906 -0.0592 -0.0597 0.0023  586  GLU A O   
263  C CB  . GLU A 49  ? 0.7664 0.6192 0.5620 -0.0635 -0.0701 0.0127  586  GLU A CB  
264  C CG  . GLU A 49  ? 0.8804 0.7220 0.6521 -0.0702 -0.0727 0.0174  586  GLU A CG  
265  C CD  . GLU A 49  ? 1.0421 0.8737 0.7921 -0.0850 -0.0651 0.0190  586  GLU A CD  
266  O OE1 . GLU A 49  ? 1.1097 0.9290 0.8546 -0.0900 -0.0637 0.0216  586  GLU A OE1 
267  O OE2 . GLU A 49  ? 1.1024 0.9386 0.8400 -0.0925 -0.0600 0.0170  586  GLU A OE2 
268  N N   . ASN A 50  ? 0.5871 0.4956 0.4332 -0.0557 -0.0508 -0.0060 587  ASN A N   
269  C CA  . ASN A 50  ? 0.5606 0.4845 0.4291 -0.0488 -0.0496 -0.0101 587  ASN A CA  
270  C C   . ASN A 50  ? 0.5223 0.4702 0.4035 -0.0489 -0.0396 -0.0169 587  ASN A C   
271  O O   . ASN A 50  ? 0.5330 0.4941 0.4304 -0.0451 -0.0381 -0.0199 587  ASN A O   
272  C CB  . ASN A 50  ? 0.5015 0.4271 0.3828 -0.0370 -0.0579 -0.0093 587  ASN A CB  
273  C CG  . ASN A 50  ? 0.5677 0.4991 0.4485 -0.0332 -0.0581 -0.0104 587  ASN A CG  
274  O OD1 . ASN A 50  ? 0.4980 0.4405 0.3788 -0.0356 -0.0502 -0.0141 587  ASN A OD1 
275  N ND2 . ASN A 50  ? 0.5801 0.5043 0.4609 -0.0272 -0.0670 -0.0078 587  ASN A ND2 
276  N N   . ILE A 51  ? 0.4893 0.4445 0.3645 -0.0527 -0.0330 -0.0196 588  ILE A N   
277  C CA  . ILE A 51  ? 0.5178 0.4964 0.4056 -0.0521 -0.0237 -0.0262 588  ILE A CA  
278  C C   . ILE A 51  ? 0.6098 0.5906 0.4848 -0.0606 -0.0158 -0.0291 588  ILE A C   
279  O O   . ILE A 51  ? 0.5960 0.5662 0.4583 -0.0622 -0.0174 -0.0273 588  ILE A O   
280  C CB  . ILE A 51  ? 0.5358 0.5288 0.4420 -0.0396 -0.0247 -0.0283 588  ILE A CB  
281  C CG1 . ILE A 51  ? 0.5198 0.5373 0.4399 -0.0375 -0.0161 -0.0341 588  ILE A CG1 
282  C CG2 . ILE A 51  ? 0.4947 0.4801 0.3944 -0.0360 -0.0271 -0.0272 588  ILE A CG2 
283  C CD1 . ILE A 51  ? 0.5404 0.5710 0.4786 -0.0253 -0.0176 -0.0350 588  ILE A CD1 
284  N N   . VAL A 52  ? 0.5857 0.5819 0.4644 -0.0667 -0.0069 -0.0343 589  VAL A N   
285  C CA  . VAL A 52  ? 0.5291 0.5309 0.3977 -0.0753 0.0018  -0.0387 589  VAL A CA  
286  C C   . VAL A 52  ? 0.5237 0.5542 0.4107 -0.0712 0.0103  -0.0465 589  VAL A C   
287  O O   . VAL A 52  ? 0.5225 0.5677 0.4245 -0.0678 0.0108  -0.0483 589  VAL A O   
288  C CB  . VAL A 52  ? 0.6037 0.5924 0.4519 -0.0910 0.0049  -0.0373 589  VAL A CB  
289  C CG1 . VAL A 52  ? 0.7497 0.7091 0.5782 -0.0938 -0.0041 -0.0287 589  VAL A CG1 
290  C CG2 . VAL A 52  ? 0.5983 0.5945 0.4536 -0.0956 0.0076  -0.0393 589  VAL A CG2 
291  N N   . PHE A 53  ? 0.4532 0.4922 0.3390 -0.0713 0.0169  -0.0513 590  PHE A N   
292  C CA  . PHE A 53  ? 0.5619 0.6278 0.4656 -0.0652 0.0246  -0.0587 590  PHE A CA  
293  C C   . PHE A 53  ? 0.6052 0.6827 0.5020 -0.0771 0.0350  -0.0658 590  PHE A C   
294  O O   . PHE A 53  ? 0.6705 0.7332 0.5468 -0.0892 0.0369  -0.0651 590  PHE A O   
295  C CB  . PHE A 53  ? 0.5961 0.6636 0.5074 -0.0534 0.0245  -0.0598 590  PHE A CB  
296  C CG  . PHE A 53  ? 0.4958 0.5534 0.4139 -0.0425 0.0151  -0.0537 590  PHE A CG  
297  C CD1 . PHE A 53  ? 0.5223 0.5569 0.4268 -0.0440 0.0078  -0.0482 590  PHE A CD1 
298  C CD2 . PHE A 53  ? 0.5464 0.6188 0.4841 -0.0312 0.0136  -0.0537 590  PHE A CD2 
299  C CE1 . PHE A 53  ? 0.5653 0.5929 0.4768 -0.0348 -0.0002 -0.0438 590  PHE A CE1 
300  C CE2 . PHE A 53  ? 0.5415 0.6054 0.4848 -0.0225 0.0057  -0.0487 590  PHE A CE2 
301  C CZ  . PHE A 53  ? 0.5108 0.5527 0.4415 -0.0244 -0.0009 -0.0442 590  PHE A CZ  
302  N N   . GLU A 54  ? 0.5580 0.6633 0.4721 -0.0739 0.0415  -0.0726 591  GLU A N   
303  C CA  . GLU A 54  ? 0.5546 0.6766 0.4665 -0.0833 0.0524  -0.0814 591  GLU A CA  
304  C C   . GLU A 54  ? 0.7323 0.8542 0.6425 -0.0792 0.0570  -0.0854 591  GLU A C   
305  O O   . GLU A 54  ? 0.8433 0.9838 0.7716 -0.0673 0.0605  -0.0903 591  GLU A O   
306  C CB  . GLU A 54  ? 0.5536 0.7083 0.4867 -0.0796 0.0574  -0.0880 591  GLU A CB  
307  C CG  . GLU A 54  ? 0.5546 0.7120 0.4896 -0.0856 0.0544  -0.0858 591  GLU A CG  
308  C CD  . GLU A 54  ? 0.6511 0.8018 0.5680 -0.1055 0.0599  -0.0883 591  GLU A CD  
309  O OE1 . GLU A 54  ? 0.5911 0.7466 0.5099 -0.1121 0.0598  -0.0887 591  GLU A OE1 
310  O OE2 . GLU A 54  ? 0.6990 0.8390 0.5989 -0.1153 0.0647  -0.0899 591  GLU A OE2 
311  N N   . ASP A 55  ? 0.7367 0.8369 0.6249 -0.0887 0.0567  -0.0832 592  ASP A N   
312  C CA  . ASP A 55  ? 0.8140 0.9116 0.6990 -0.0857 0.0607  -0.0872 592  ASP A CA  
313  C C   . ASP A 55  ? 0.8002 0.9182 0.6871 -0.0926 0.0733  -0.0984 592  ASP A C   
314  O O   . ASP A 55  ? 0.7823 0.9064 0.6746 -0.0868 0.0788  -0.1046 592  ASP A O   
315  C CB  . ASP A 55  ? 0.9071 0.9759 0.7676 -0.0936 0.0553  -0.0808 592  ASP A CB  
316  C CG  . ASP A 55  ? 0.9738 1.0249 0.8351 -0.0848 0.0430  -0.0710 592  ASP A CG  
317  O OD1 . ASP A 55  ? 0.9843 1.0399 0.8614 -0.0707 0.0404  -0.0709 592  ASP A OD1 
318  O OD2 . ASP A 55  ? 1.0411 1.0739 0.8876 -0.0920 0.0361  -0.0637 592  ASP A OD2 
319  N N   . ASN A 56  ? 0.8357 0.9645 0.7184 -0.1053 0.0785  -0.1019 593  ASN A N   
320  C CA  . ASN A 56  ? 1.0316 1.1855 0.9198 -0.1119 0.0909  -0.1139 593  ASN A CA  
321  C C   . ASN A 56  ? 0.9827 1.1686 0.9008 -0.0974 0.0942  -0.1205 593  ASN A C   
322  O O   . ASN A 56  ? 0.9498 1.1598 0.8769 -0.0991 0.1044  -0.1316 593  ASN A O   
323  C CB  . ASN A 56  ? 1.1606 1.3139 1.0331 -0.1317 0.0950  -0.1150 593  ASN A CB  
324  C CG  . ASN A 56  ? 1.2714 1.4038 1.1345 -0.1349 0.0851  -0.1039 593  ASN A CG  
325  O OD1 . ASN A 56  ? 1.1270 1.2591 1.0044 -0.1216 0.0770  -0.0985 593  ASN A OD1 
326  N ND2 . ASN A 56  ? 1.3328 1.4465 1.1711 -0.1527 0.0860  -0.1006 593  ASN A ND2 
327  N N   . LEU A 57  ? 0.9435 1.1308 0.8768 -0.0831 0.0859  -0.1142 594  LEU A N   
328  C CA  . LEU A 57  ? 0.9280 1.1450 0.8883 -0.0690 0.0872  -0.1185 594  LEU A CA  
329  C C   . LEU A 57  ? 0.9880 1.1995 0.9609 -0.0495 0.0823  -0.1147 594  LEU A C   
330  O O   . LEU A 57  ? 1.0198 1.2048 0.9822 -0.0469 0.0754  -0.1069 594  LEU A O   
331  C CB  . LEU A 57  ? 0.8008 1.0274 0.7684 -0.0704 0.0821  -0.1147 594  LEU A CB  
332  C CG  . LEU A 57  ? 0.7447 0.9835 0.7050 -0.0886 0.0886  -0.1205 594  LEU A CG  
333  C CD1 . LEU A 57  ? 0.7068 0.9592 0.6787 -0.0874 0.0841  -0.1183 594  LEU A CD1 
334  C CD2 . LEU A 57  ? 0.7181 0.9858 0.6873 -0.0917 0.1003  -0.1333 594  LEU A CD2 
335  N N   . GLN A 58  ? 1.0186 1.2556 1.0137 -0.0360 0.0860  -0.1202 595  GLN A N   
336  C CA  . GLN A 58  ? 1.0399 1.2726 1.0475 -0.0172 0.0828  -0.1173 595  GLN A CA  
337  C C   . GLN A 58  ? 1.0296 1.2755 1.0553 -0.0034 0.0758  -0.1117 595  GLN A C   
338  O O   . GLN A 58  ? 1.0204 1.2965 1.0635 0.0020  0.0787  -0.1167 595  GLN A O   
339  C CB  . GLN A 58  ? 0.9856 1.2340 1.0039 -0.0104 0.0926  -0.1277 595  GLN A CB  
340  C CG  . GLN A 58  ? 1.0184 1.2440 1.0305 -0.0040 0.0937  -0.1273 595  GLN A CG  
341  C CD  . GLN A 58  ? 1.0941 1.3346 1.1158 0.0007  0.1050  -0.1393 595  GLN A CD  
342  O OE1 . GLN A 58  ? 1.1963 1.4634 1.2262 -0.0038 0.1123  -0.1484 595  GLN A OE1 
343  N NE2 . GLN A 58  ? 1.0041 1.2278 1.0252 0.0096  0.1068  -0.1401 595  GLN A NE2 
344  N N   . GLY A 62  ? 0.6676 0.8867 0.7322 0.0648  0.0561  -0.0872 599  GLY A N   
345  C CA  . GLY A 62  ? 0.6062 0.7931 0.6555 0.0613  0.0548  -0.0841 599  GLY A CA  
346  C C   . GLY A 62  ? 0.5877 0.7580 0.6228 0.0498  0.0471  -0.0778 599  GLY A C   
347  O O   . GLY A 62  ? 0.6619 0.8106 0.6812 0.0408  0.0469  -0.0776 599  GLY A O   
348  N N   . ILE A 63  ? 0.5874 0.7687 0.6287 0.0504  0.0408  -0.0728 600  ILE A N   
349  C CA  . ILE A 63  ? 0.5519 0.7189 0.5820 0.0407  0.0335  -0.0672 600  ILE A CA  
350  C C   . ILE A 63  ? 0.5036 0.6680 0.5205 0.0242  0.0362  -0.0712 600  ILE A C   
351  O O   . ILE A 63  ? 0.5375 0.7224 0.5589 0.0192  0.0416  -0.0770 600  ILE A O   
352  C CB  . ILE A 63  ? 0.5017 0.6840 0.5427 0.0446  0.0274  -0.0626 600  ILE A CB  
353  C CG1 . ILE A 63  ? 0.5568 0.7382 0.6076 0.0598  0.0239  -0.0571 600  ILE A CG1 
354  C CG2 . ILE A 63  ? 0.6015 0.7709 0.6322 0.0339  0.0210  -0.0585 600  ILE A CG2 
355  C CD1 . ILE A 63  ? 0.5758 0.7764 0.6378 0.0639  0.0186  -0.0532 600  ILE A CD1 
356  N N   . PRO A 64  ? 0.4719 0.6122 0.4720 0.0152  0.0327  -0.0682 601  PRO A N   
357  C CA  . PRO A 64  ? 0.5478 0.6834 0.5335 -0.0007 0.0342  -0.0702 601  PRO A CA  
358  C C   . PRO A 64  ? 0.5630 0.7116 0.5531 -0.0060 0.0317  -0.0690 601  PRO A C   
359  O O   . PRO A 64  ? 0.5646 0.7165 0.5634 0.0001  0.0256  -0.0645 601  PRO A O   
360  C CB  . PRO A 64  ? 0.5810 0.6879 0.5498 -0.0057 0.0282  -0.0650 601  PRO A CB  
361  C CG  . PRO A 64  ? 0.5464 0.6464 0.5236 0.0066  0.0223  -0.0599 601  PRO A CG  
362  C CD  . PRO A 64  ? 0.4873 0.6040 0.4805 0.0189  0.0274  -0.0631 601  PRO A CD  
363  N N   . ILE A 65  ? 0.4659 0.6226 0.4497 -0.0183 0.0371  -0.0739 602  ILE A N   
364  C CA  . ILE A 65  ? 0.4275 0.5972 0.4146 -0.0256 0.0365  -0.0745 602  ILE A CA  
365  C C   . ILE A 65  ? 0.4701 0.6149 0.4398 -0.0367 0.0311  -0.0692 602  ILE A C   
366  O O   . ILE A 65  ? 0.4911 0.6189 0.4431 -0.0468 0.0328  -0.0692 602  ILE A O   
367  C CB  . ILE A 65  ? 0.4497 0.6423 0.4394 -0.0338 0.0459  -0.0834 602  ILE A CB  
368  C CG1 . ILE A 65  ? 0.4392 0.6578 0.4480 -0.0209 0.0508  -0.0888 602  ILE A CG1 
369  C CG2 . ILE A 65  ? 0.4394 0.6445 0.4314 -0.0429 0.0458  -0.0845 602  ILE A CG2 
370  C CD1 . ILE A 65  ? 0.5424 0.7802 0.5520 -0.0284 0.0614  -0.0990 602  ILE A CD1 
371  N N   . ILE A 66  ? 0.4620 0.5412 0.3887 -0.0150 0.1311  -0.0713 603  ILE A N   
372  C CA  . ILE A 66  ? 0.4586 0.5218 0.3492 -0.0232 0.1185  -0.0511 603  ILE A CA  
373  C C   . ILE A 66  ? 0.5211 0.5888 0.4053 -0.0369 0.1304  -0.0404 603  ILE A C   
374  O O   . ILE A 66  ? 0.5311 0.6120 0.4519 -0.0361 0.1357  -0.0409 603  ILE A O   
375  C CB  . ILE A 66  ? 0.4900 0.5426 0.3951 -0.0127 0.0952  -0.0396 603  ILE A CB  
376  C CG1 . ILE A 66  ? 0.5048 0.5501 0.4074 -0.0039 0.0846  -0.0480 603  ILE A CG1 
377  C CG2 . ILE A 66  ? 0.5280 0.5659 0.4076 -0.0191 0.0835  -0.0195 603  ILE A CG2 
378  C CD1 . ILE A 66  ? 0.5166 0.5558 0.4406 0.0061  0.0674  -0.0414 603  ILE A CD1 
379  N N   . LYS A 67  ? 0.5121 0.5683 0.3491 -0.0508 0.1341  -0.0306 604  LYS A N   
380  C CA  . LYS A 67  ? 0.4893 0.5423 0.3117 -0.0666 0.1441  -0.0163 604  LYS A CA  
381  C C   . LYS A 67  ? 0.5921 0.6236 0.4080 -0.0650 0.1225  0.0067  604  LYS A C   
382  O O   . LYS A 67  ? 0.5010 0.5310 0.3352 -0.0700 0.1245  0.0157  604  LYS A O   
383  C CB  . LYS A 67  ? 0.5655 0.6136 0.3344 -0.0841 0.1598  -0.0161 604  LYS A CB  
384  C CG  . LYS A 67  ? 0.6359 0.6780 0.3834 -0.1041 0.1736  -0.0005 604  LYS A CG  
385  C CD  . LYS A 67  ? 0.7313 0.7662 0.4168 -0.1232 0.1886  0.0007  604  LYS A CD  
386  C CE  . LYS A 67  ? 0.8213 0.8416 0.4826 -0.1417 0.1947  0.0227  604  LYS A CE  
387  N NZ  . LYS A 67  ? 0.9650 0.9692 0.5697 -0.1520 0.1917  0.0317  604  LYS A NZ  
388  N N   . GLY A 68  ? 0.5472 0.5627 0.3409 -0.0580 0.1017  0.0146  605  GLY A N   
389  C CA  . GLY A 68  ? 0.4869 0.4834 0.2816 -0.0533 0.0814  0.0333  605  GLY A CA  
390  C C   . GLY A 68  ? 0.5099 0.4981 0.2927 -0.0427 0.0598  0.0357  605  GLY A C   
391  O O   . GLY A 68  ? 0.5775 0.5721 0.3452 -0.0418 0.0597  0.0246  605  GLY A O   
392  N N   . GLY A 69  ? 0.4948 0.4694 0.2877 -0.0352 0.0420  0.0487  606  GLY A N   
393  C CA  . GLY A 69  ? 0.5084 0.4782 0.2959 -0.0257 0.0212  0.0518  606  GLY A CA  
394  C C   . GLY A 69  ? 0.4909 0.4480 0.2993 -0.0167 0.0064  0.0634  606  GLY A C   
395  O O   . GLY A 69  ? 0.5094 0.4599 0.3349 -0.0181 0.0122  0.0674  606  GLY A O   
396  N N   . THR A 70  ? 0.4874 0.4421 0.2967 -0.0078 -0.0126 0.0672  607  THR A N   
397  C CA  . THR A 70  ? 0.4954 0.4431 0.3340 0.0037  -0.0245 0.0719  607  THR A CA  
398  C C   . THR A 70  ? 0.4444 0.4050 0.3171 0.0099  -0.0161 0.0560  607  THR A C   
399  O O   . THR A 70  ? 0.4380 0.4130 0.3135 0.0086  -0.0076 0.0427  607  THR A O   
400  C CB  . THR A 70  ? 0.5050 0.4537 0.3443 0.0122  -0.0459 0.0768  607  THR A CB  
401  O OG1 . THR A 70  ? 0.5148 0.4834 0.3613 0.0143  -0.0461 0.0609  607  THR A OG1 
402  C CG2 . THR A 70  ? 0.5462 0.4818 0.3454 0.0051  -0.0576 0.0940  607  THR A CG2 
403  N N   . VAL A 71  ? 0.3970 0.3501 0.2942 0.0164  -0.0190 0.0573  608  VAL A N   
404  C CA  . VAL A 71  ? 0.3888 0.3520 0.3110 0.0201  -0.0118 0.0435  608  VAL A CA  
405  C C   . VAL A 71  ? 0.4287 0.4066 0.3594 0.0258  -0.0160 0.0331  608  VAL A C   
406  O O   . VAL A 71  ? 0.4462 0.4335 0.3854 0.0254  -0.0088 0.0225  608  VAL A O   
407  C CB  . VAL A 71  ? 0.4294 0.3806 0.3718 0.0244  -0.0132 0.0443  608  VAL A CB  
408  C CG1 . VAL A 71  ? 0.4334 0.3822 0.3907 0.0354  -0.0251 0.0453  608  VAL A CG1 
409  C CG2 . VAL A 71  ? 0.4031 0.3629 0.3610 0.0235  -0.0047 0.0316  608  VAL A CG2 
410  N N   . VAL A 72  ? 0.4193 0.3991 0.3485 0.0303  -0.0286 0.0368  609  VAL A N   
411  C CA  . VAL A 72  ? 0.4244 0.4191 0.3627 0.0328  -0.0321 0.0266  609  VAL A CA  
412  C C   . VAL A 72  ? 0.3934 0.3945 0.3142 0.0259  -0.0251 0.0190  609  VAL A C   
413  O O   . VAL A 72  ? 0.4095 0.4176 0.3403 0.0260  -0.0200 0.0082  609  VAL A O   
414  C CB  . VAL A 72  ? 0.4671 0.4660 0.4103 0.0380  -0.0491 0.0320  609  VAL A CB  
415  C CG1 . VAL A 72  ? 0.4107 0.4257 0.3552 0.0356  -0.0531 0.0218  609  VAL A CG1 
416  C CG2 . VAL A 72  ? 0.4538 0.4519 0.4284 0.0478  -0.0531 0.0321  609  VAL A CG2 
417  N N   . LYS A 73  ? 0.3490 0.3458 0.2427 0.0194  -0.0235 0.0241  610  LYS A N   
418  C CA  . LYS A 73  ? 0.4094 0.4121 0.2886 0.0134  -0.0143 0.0133  610  LYS A CA  
419  C C   . LYS A 73  ? 0.4017 0.4065 0.2948 0.0134  0.0008  0.0059  610  LYS A C   
420  O O   . LYS A 73  ? 0.3626 0.3724 0.2614 0.0138  0.0067  -0.0060 610  LYS A O   
421  C CB  . LYS A 73  ? 0.4975 0.4959 0.3407 0.0046  -0.0138 0.0187  610  LYS A CB  
422  C CG  . LYS A 73  ? 0.5747 0.5750 0.3996 0.0029  -0.0305 0.0208  610  LYS A CG  
423  C CD  . LYS A 73  ? 0.5478 0.5579 0.3766 0.0016  -0.0293 0.0032  610  LYS A CD  
424  C CE  . LYS A 73  ? 0.5678 0.5836 0.3882 0.0001  -0.0493 0.0040  610  LYS A CE  
425  N NZ  . LYS A 73  ? 0.5132 0.5369 0.3433 -0.0023 -0.0482 -0.0138 610  LYS A NZ  
426  N N   . LEU A 74  ? 0.4247 0.4249 0.3254 0.0129  0.0056  0.0127  611  LEU A N   
427  C CA  . LEU A 74  ? 0.4014 0.4069 0.3197 0.0132  0.0161  0.0059  611  LEU A CA  
428  C C   . LEU A 74  ? 0.3675 0.3754 0.3055 0.0197  0.0120  -0.0007 611  LEU A C   
429  O O   . LEU A 74  ? 0.3567 0.3690 0.3045 0.0214  0.0167  -0.0086 611  LEU A O   
430  C CB  . LEU A 74  ? 0.3727 0.3735 0.2973 0.0096  0.0199  0.0136  611  LEU A CB  
431  C CG  . LEU A 74  ? 0.3980 0.3937 0.3024 -0.0001 0.0267  0.0222  611  LEU A CG  
432  C CD1 . LEU A 74  ? 0.4174 0.4060 0.3324 -0.0051 0.0301  0.0294  611  LEU A CD1 
433  C CD2 . LEU A 74  ? 0.4078 0.4152 0.3035 -0.0059 0.0408  0.0132  611  LEU A CD2 
434  N N   . ILE A 75  ? 0.3282 0.3324 0.2721 0.0233  0.0036  0.0026  612  ILE A N   
435  C CA  . ILE A 75  ? 0.3762 0.3819 0.3335 0.0264  0.0019  -0.0031 612  ILE A CA  
436  C C   . ILE A 75  ? 0.3480 0.3566 0.3023 0.0260  0.0014  -0.0104 612  ILE A C   
437  O O   . ILE A 75  ? 0.3304 0.3371 0.2916 0.0266  0.0035  -0.0151 612  ILE A O   
438  C CB  . ILE A 75  ? 0.3368 0.3405 0.3027 0.0294  -0.0035 -0.0006 612  ILE A CB  
439  C CG1 . ILE A 75  ? 0.3432 0.3396 0.3138 0.0295  -0.0018 0.0037  612  ILE A CG1 
440  C CG2 . ILE A 75  ? 0.3254 0.3319 0.3001 0.0295  -0.0026 -0.0070 612  ILE A CG2 
441  C CD1 . ILE A 75  ? 0.3791 0.3751 0.3548 0.0274  0.0023  -0.0005 612  ILE A CD1 
442  N N   . GLU A 76  ? 0.3738 0.3849 0.3169 0.0241  -0.0029 -0.0109 613  GLU A N   
443  C CA  . GLU A 76  ? 0.3828 0.3952 0.3226 0.0217  -0.0035 -0.0200 613  GLU A CA  
444  C C   . GLU A 76  ? 0.3688 0.3777 0.3074 0.0216  0.0056  -0.0276 613  GLU A C   
445  O O   . GLU A 76  ? 0.3858 0.3897 0.3326 0.0224  0.0069  -0.0338 613  GLU A O   
446  C CB  . GLU A 76  ? 0.4724 0.4889 0.3963 0.0180  -0.0113 -0.0202 613  GLU A CB  
447  C CG  . GLU A 76  ? 0.5272 0.5450 0.4502 0.0137  -0.0137 -0.0316 613  GLU A CG  
448  C CD  . GLU A 76  ? 0.5676 0.5873 0.4661 0.0076  -0.0185 -0.0363 613  GLU A CD  
449  O OE1 . GLU A 76  ? 0.6097 0.6305 0.4901 0.0065  -0.0230 -0.0277 613  GLU A OE1 
450  O OE2 . GLU A 76  ? 0.7266 0.7447 0.6217 0.0027  -0.0181 -0.0487 613  GLU A OE2 
451  N N   . ARG A 77  ? 0.3764 0.3876 0.3072 0.0206  0.0126  -0.0270 614  ARG A N   
452  C CA  . ARG A 77  ? 0.3595 0.3714 0.2963 0.0220  0.0229  -0.0363 614  ARG A CA  
453  C C   . ARG A 77  ? 0.3319 0.3432 0.2920 0.0278  0.0233  -0.0347 614  ARG A C   
454  O O   . ARG A 77  ? 0.3827 0.3922 0.3558 0.0321  0.0272  -0.0425 614  ARG A O   
455  C CB  . ARG A 77  ? 0.4094 0.4274 0.3330 0.0173  0.0329  -0.0368 614  ARG A CB  
456  C CG  . ARG A 77  ? 0.4584 0.4753 0.3521 0.0101  0.0332  -0.0406 614  ARG A CG  
457  C CD  . ARG A 77  ? 0.4698 0.4847 0.3619 0.0100  0.0399  -0.0583 614  ARG A CD  
458  N NE  . ARG A 77  ? 0.4067 0.4200 0.2666 0.0015  0.0370  -0.0634 614  ARG A NE  
459  C CZ  . ARG A 77  ? 0.4971 0.5085 0.3432 -0.0028 0.0463  -0.0806 614  ARG A CZ  
460  N NH1 . ARG A 77  ? 0.5025 0.5123 0.3144 -0.0123 0.0409  -0.0845 614  ARG A NH1 
461  N NH2 . ARG A 77  ? 0.5164 0.5274 0.3839 0.0028  0.0600  -0.0946 614  ARG A NH2 
462  N N   . LEU A 78  ? 0.3637 0.3754 0.3292 0.0282  0.0185  -0.0253 615  LEU A N   
463  C CA  . LEU A 78  ? 0.3239 0.3344 0.3057 0.0318  0.0154  -0.0229 615  LEU A CA  
464  C C   . LEU A 78  ? 0.3718 0.3721 0.3558 0.0339  0.0101  -0.0243 615  LEU A C   
465  O O   . LEU A 78  ? 0.3559 0.3519 0.3507 0.0375  0.0065  -0.0230 615  LEU A O   
466  C CB  . LEU A 78  ? 0.3142 0.3248 0.2954 0.0296  0.0116  -0.0150 615  LEU A CB  
467  C CG  . LEU A 78  ? 0.3151 0.3255 0.3074 0.0305  0.0072  -0.0126 615  LEU A CG  
468  C CD1 . LEU A 78  ? 0.3296 0.3509 0.3385 0.0317  0.0105  -0.0151 615  LEU A CD1 
469  C CD2 . LEU A 78  ? 0.3647 0.3719 0.3523 0.0271  0.0048  -0.0084 615  LEU A CD2 
470  N N   . THR A 79  ? 0.3272 0.3233 0.3014 0.0307  0.0085  -0.0260 616  THR A N   
471  C CA  . THR A 79  ? 0.3195 0.3052 0.2938 0.0288  0.0051  -0.0265 616  THR A CA  
472  C C   . THR A 79  ? 0.4033 0.3854 0.3731 0.0260  0.0065  -0.0352 616  THR A C   
473  O O   . THR A 79  ? 0.3569 0.3364 0.3244 0.0206  0.0040  -0.0363 616  THR A O   
474  C CB  . THR A 79  ? 0.3112 0.2988 0.2826 0.0248  0.0027  -0.0213 616  THR A CB  
475  O OG1 . THR A 79  ? 0.3368 0.3344 0.3057 0.0239  0.0021  -0.0218 616  THR A OG1 
476  C CG2 . THR A 79  ? 0.3629 0.3501 0.3356 0.0260  0.0014  -0.0154 616  THR A CG2 
477  N N   . TYR A 80  ? 0.3369 0.3198 0.3063 0.0285  0.0115  -0.0433 617  TYR A N   
478  C CA  . TYR A 80  ? 0.3382 0.3186 0.2981 0.0243  0.0134  -0.0544 617  TYR A CA  
479  C C   . TYR A 80  ? 0.4230 0.3865 0.3889 0.0227  0.0119  -0.0599 617  TYR A C   
480  O O   . TYR A 80  ? 0.4159 0.3669 0.3938 0.0282  0.0121  -0.0581 617  TYR A O   
481  C CB  . TYR A 80  ? 0.3673 0.3523 0.3236 0.0265  0.0226  -0.0638 617  TYR A CB  
482  C CG  . TYR A 80  ? 0.4271 0.4137 0.3627 0.0195  0.0248  -0.0747 617  TYR A CG  
483  C CD1 . TYR A 80  ? 0.4653 0.4598 0.3833 0.0131  0.0171  -0.0690 617  TYR A CD1 
484  C CD2 . TYR A 80  ? 0.3979 0.3779 0.3316 0.0196  0.0336  -0.0914 617  TYR A CD2 
485  C CE1 . TYR A 80  ? 0.4369 0.4331 0.3318 0.0055  0.0157  -0.0779 617  TYR A CE1 
486  C CE2 . TYR A 80  ? 0.5625 0.5434 0.4714 0.0110  0.0354  -0.1030 617  TYR A CE2 
487  C CZ  . TYR A 80  ? 0.5309 0.5202 0.4184 0.0034  0.0253  -0.0953 617  TYR A CZ  
488  O OH  . TYR A 80  ? 0.5582 0.5486 0.4172 -0.0062 0.0236  -0.1057 617  TYR A OH  
489  N N   . HIS A 81  ? 0.3851 0.3469 0.3434 0.0145  0.0091  -0.0661 618  HIS A N   
490  C CA  . HIS A 81  ? 0.4546 0.3979 0.4190 0.0101  0.0079  -0.0698 618  HIS A CA  
491  C C   . HIS A 81  ? 0.5007 0.4264 0.4695 0.0141  0.0131  -0.0823 618  HIS A C   
492  O O   . HIS A 81  ? 0.5660 0.4695 0.5432 0.0139  0.0120  -0.0820 618  HIS A O   
493  C CB  . HIS A 81  ? 0.3899 0.3386 0.3504 -0.0017 0.0033  -0.0742 618  HIS A CB  
494  C CG  . HIS A 81  ? 0.4031 0.3569 0.3515 -0.0069 0.0020  -0.0885 618  HIS A CG  
495  N ND1 . HIS A 81  ? 0.4438 0.4153 0.3781 -0.0062 -0.0007 -0.0883 618  HIS A ND1 
496  C CD2 . HIS A 81  ? 0.4418 0.3836 0.3866 -0.0147 0.0022  -0.1034 618  HIS A CD2 
497  C CE1 . HIS A 81  ? 0.4711 0.4425 0.3905 -0.0135 -0.0026 -0.1021 618  HIS A CE1 
498  N NE2 . HIS A 81  ? 0.4806 0.4348 0.4072 -0.0188 -0.0007 -0.1130 618  HIS A NE2 
499  N N   A MET A 82  ? 0.4460 0.3793 0.4091 0.0174  0.0196  -0.0936 619  MET A N   
500  N N   B MET A 82  ? 0.4660 0.3991 0.4290 0.0173  0.0196  -0.0938 619  MET A N   
501  C CA  A MET A 82  ? 0.5118 0.4290 0.4796 0.0200  0.0267  -0.1110 619  MET A CA  
502  C CA  B MET A 82  ? 0.5157 0.4324 0.4835 0.0199  0.0266  -0.1111 619  MET A CA  
503  C C   A MET A 82  ? 0.4951 0.4021 0.4867 0.0338  0.0302  -0.1095 619  MET A C   
504  C C   B MET A 82  ? 0.4995 0.4076 0.4907 0.0339  0.0310  -0.1107 619  MET A C   
505  O O   A MET A 82  ? 0.4766 0.3617 0.4809 0.0381  0.0326  -0.1198 619  MET A O   
506  O O   B MET A 82  ? 0.5065 0.3948 0.5100 0.0385  0.0350  -0.1232 619  MET A O   
507  C CB  A MET A 82  ? 0.5302 0.4598 0.4795 0.0163  0.0347  -0.1263 619  MET A CB  
508  C CB  B MET A 82  ? 0.5551 0.4830 0.5031 0.0148  0.0339  -0.1273 619  MET A CB  
509  C CG  A MET A 82  ? 0.6206 0.5624 0.5460 0.0039  0.0269  -0.1253 619  MET A CG  
510  C CG  B MET A 82  ? 0.6509 0.5822 0.5785 0.0009  0.0261  -0.1321 619  MET A CG  
511  S SD  A MET A 82  ? 0.6684 0.6107 0.5651 -0.0054 0.0333  -0.1488 619  MET A SD  
512  S SD  B MET A 82  ? 0.8420 0.7728 0.7423 -0.0079 0.0332  -0.1574 619  MET A SD  
513  C CE  A MET A 82  ? 0.8018 0.7181 0.7083 -0.0120 0.0305  -0.1646 619  MET A CE  
514  C CE  B MET A 82  ? 0.7148 0.6681 0.5957 -0.0053 0.0408  -0.1512 619  MET A CE  
515  N N   . TYR A 83  ? 0.4903 0.4123 0.4909 0.0410  0.0293  -0.0975 620  TYR A N   
516  C CA  . TYR A 83  ? 0.4759 0.3938 0.5036 0.0546  0.0300  -0.0963 620  TYR A CA  
517  C C   . TYR A 83  ? 0.4237 0.3579 0.4571 0.0578  0.0239  -0.0794 620  TYR A C   
518  O O   . TYR A 83  ? 0.4340 0.3839 0.4513 0.0508  0.0237  -0.0727 620  TYR A O   
519  C CB  . TYR A 83  ? 0.5414 0.4678 0.5818 0.0613  0.0442  -0.1158 620  TYR A CB  
520  C CG  . TYR A 83  ? 0.4985 0.4487 0.5177 0.0532  0.0544  -0.1212 620  TYR A CG  
521  C CD1 . TYR A 83  ? 0.4191 0.3907 0.4393 0.0531  0.0547  -0.1094 620  TYR A CD1 
522  C CD2 . TYR A 83  ? 0.5348 0.4835 0.5296 0.0440  0.0626  -0.1373 620  TYR A CD2 
523  C CE1 . TYR A 83  ? 0.5471 0.5355 0.5448 0.0445  0.0633  -0.1114 620  TYR A CE1 
524  C CE2 . TYR A 83  ? 0.5163 0.4833 0.4855 0.0353  0.0699  -0.1393 620  TYR A CE2 
525  C CZ  . TYR A 83  ? 0.5218 0.5074 0.4926 0.0357  0.0706  -0.1253 620  TYR A CZ  
526  O OH  . TYR A 83  ? 0.6040 0.6031 0.5465 0.0259  0.0775  -0.1248 620  TYR A OH  
527  N N   . ALA A 84  ? 0.5655 0.4947 0.6231 0.0688  0.0178  -0.0735 621  ALA A N   
528  C CA  . ALA A 84  ? 0.5243 0.4693 0.5901 0.0718  0.0109  -0.0603 621  ALA A CA  
529  C C   . ALA A 84  ? 0.4214 0.3934 0.5013 0.0747  0.0221  -0.0691 621  ALA A C   
530  O O   . ALA A 84  ? 0.3883 0.3653 0.4798 0.0785  0.0347  -0.0856 621  ALA A O   
531  C CB  . ALA A 84  ? 0.6267 0.5569 0.7127 0.0818  -0.0031 -0.0501 621  ALA A CB  
532  N N   . ASP A 85  ? 0.4331 0.4221 0.5117 0.0714  0.0187  -0.0590 622  ASP A N   
533  C CA  . ASP A 85  ? 0.4109 0.4254 0.5015 0.0705  0.0298  -0.0649 622  ASP A CA  
534  C C   . ASP A 85  ? 0.3893 0.4167 0.4981 0.0726  0.0196  -0.0542 622  ASP A C   
535  O O   . ASP A 85  ? 0.3696 0.4062 0.4657 0.0642  0.0195  -0.0471 622  ASP A O   
536  C CB  . ASP A 85  ? 0.3593 0.3797 0.4187 0.0584  0.0390  -0.0653 622  ASP A CB  
537  C CG  . ASP A 85  ? 0.4502 0.4912 0.5151 0.0548  0.0553  -0.0739 622  ASP A CG  
538  O OD1 . ASP A 85  ? 0.3926 0.4489 0.4907 0.0611  0.0602  -0.0797 622  ASP A OD1 
539  O OD2 . ASP A 85  ? 0.4422 0.4846 0.4783 0.0449  0.0630  -0.0744 622  ASP A OD2 
540  N N   . PRO A 86  ? 0.3775 0.4046 0.5170 0.0838  0.0091  -0.0529 623  PRO A N   
541  C CA  . PRO A 86  ? 0.3857 0.4247 0.5403 0.0847  -0.0050 -0.0424 623  PRO A CA  
542  C C   . PRO A 86  ? 0.3682 0.4364 0.5389 0.0791  0.0047  -0.0471 623  PRO A C   
543  O O   . PRO A 86  ? 0.3487 0.4238 0.5148 0.0724  -0.0038 -0.0384 623  PRO A O   
544  C CB  . PRO A 86  ? 0.3648 0.3995 0.5545 0.0998  -0.0184 -0.0419 623  PRO A CB  
545  C CG  . PRO A 86  ? 0.4083 0.4373 0.6128 0.1080  -0.0041 -0.0579 623  PRO A CG  
546  C CD  . PRO A 86  ? 0.3642 0.3787 0.5270 0.0966  0.0079  -0.0611 623  PRO A CD  
547  N N   . ASN A 87  ? 0.3355 0.4202 0.5236 0.0801  0.0236  -0.0614 624  ASN A N   
548  C CA  . ASN A 87  ? 0.3316 0.4436 0.5345 0.0719  0.0351  -0.0652 624  ASN A CA  
549  C C   . ASN A 87  ? 0.3618 0.4673 0.5248 0.0566  0.0396  -0.0567 624  ASN A C   
550  O O   . ASN A 87  ? 0.3525 0.4688 0.5199 0.0485  0.0370  -0.0509 624  ASN A O   
551  C CB  . ASN A 87  ? 0.3528 0.4833 0.5788 0.0741  0.0580  -0.0834 624  ASN A CB  
552  C CG  . ASN A 87  ? 0.4549 0.5985 0.7349 0.0910  0.0541  -0.0936 624  ASN A CG  
553  O OD1 . ASN A 87  ? 0.4419 0.5890 0.7479 0.0991  0.0330  -0.0851 624  ASN A OD1 
554  N ND2 . ASN A 87  ? 0.4453 0.5958 0.7424 0.0965  0.0738  -0.1126 624  ASN A ND2 
555  N N   . PHE A 88  ? 0.2962 0.3832 0.4226 0.0528  0.0447  -0.0560 625  PHE A N   
556  C CA  . PHE A 88  ? 0.2594 0.3381 0.3513 0.0412  0.0457  -0.0468 625  PHE A CA  
557  C C   . PHE A 88  ? 0.3355 0.4036 0.4193 0.0402  0.0287  -0.0348 625  PHE A C   
558  O O   . PHE A 88  ? 0.3286 0.3978 0.4042 0.0319  0.0281  -0.0286 625  PHE A O   
559  C CB  . PHE A 88  ? 0.2893 0.3534 0.3485 0.0386  0.0514  -0.0492 625  PHE A CB  
560  C CG  . PHE A 88  ? 0.3150 0.3711 0.3426 0.0288  0.0506  -0.0392 625  PHE A CG  
561  C CD1 . PHE A 88  ? 0.3812 0.4451 0.4032 0.0192  0.0597  -0.0354 625  PHE A CD1 
562  C CD2 . PHE A 88  ? 0.3506 0.3911 0.3566 0.0291  0.0410  -0.0338 625  PHE A CD2 
563  C CE1 . PHE A 88  ? 0.3671 0.4193 0.3615 0.0119  0.0568  -0.0246 625  PHE A CE1 
564  C CE2 . PHE A 88  ? 0.3734 0.4074 0.3568 0.0228  0.0385  -0.0250 625  PHE A CE2 
565  C CZ  . PHE A 88  ? 0.3497 0.3876 0.3268 0.0151  0.0453  -0.0197 625  PHE A CZ  
566  N N   . VAL A 89  ? 0.2747 0.3305 0.3592 0.0475  0.0157  -0.0319 626  VAL A N   
567  C CA  . VAL A 89  ? 0.2617 0.3076 0.3346 0.0449  0.0017  -0.0222 626  VAL A CA  
568  C C   . VAL A 89  ? 0.2778 0.3385 0.3693 0.0414  -0.0043 -0.0203 626  VAL A C   
569  O O   . VAL A 89  ? 0.3012 0.3584 0.3793 0.0335  -0.0071 -0.0160 626  VAL A O   
570  C CB  . VAL A 89  ? 0.3717 0.4017 0.4412 0.0513  -0.0104 -0.0183 626  VAL A CB  
571  C CG1 . VAL A 89  ? 0.2942 0.3163 0.3490 0.0464  -0.0233 -0.0093 626  VAL A CG1 
572  C CG2 . VAL A 89  ? 0.3970 0.4112 0.4462 0.0509  -0.0047 -0.0203 626  VAL A CG2 
573  N N   . ARG A 90  ? 0.2652 0.3433 0.3910 0.0474  -0.0064 -0.0251 627  ARG A N   
574  C CA  . ARG A 90  ? 0.2954 0.3915 0.4444 0.0433  -0.0144 -0.0244 627  ARG A CA  
575  C C   . ARG A 90  ? 0.3280 0.4339 0.4751 0.0308  -0.0009 -0.0264 627  ARG A C   
576  O O   . ARG A 90  ? 0.3210 0.4257 0.4623 0.0218  -0.0072 -0.0230 627  ARG A O   
577  C CB  . ARG A 90  ? 0.3211 0.4385 0.5157 0.0535  -0.0191 -0.0303 627  ARG A CB  
578  C CG  . ARG A 90  ? 0.3132 0.4536 0.5373 0.0488  -0.0307 -0.0303 627  ARG A CG  
579  C CD  . ARG A 90  ? 0.3765 0.5461 0.6567 0.0590  -0.0332 -0.0383 627  ARG A CD  
580  N NE  . ARG A 90  ? 0.6598 0.8219 0.9525 0.0751  -0.0315 -0.0421 627  ARG A NE  
581  C CZ  . ARG A 90  ? 0.8124 0.9828 1.1194 0.0789  -0.0091 -0.0545 627  ARG A CZ  
582  N NH1 . ARG A 90  ? 0.7403 0.8999 1.0585 0.0936  -0.0087 -0.0596 627  ARG A NH1 
583  N NH2 . ARG A 90  ? 0.8891 1.0758 1.1959 0.0668  0.0135  -0.0621 627  ARG A NH2 
584  N N   . THR A 91  ? 0.2848 0.3979 0.4341 0.0288  0.0180  -0.0322 628  THR A N   
585  C CA  . THR A 91  ? 0.2827 0.4023 0.4279 0.0153  0.0316  -0.0318 628  THR A CA  
586  C C   . THR A 91  ? 0.3179 0.4133 0.4257 0.0082  0.0295  -0.0228 628  THR A C   
587  O O   . THR A 91  ? 0.2958 0.3891 0.4019 -0.0024 0.0300  -0.0193 628  THR A O   
588  C CB  . THR A 91  ? 0.2984 0.4282 0.4459 0.0134  0.0529  -0.0392 628  THR A CB  
589  O OG1 . THR A 91  ? 0.3380 0.4920 0.5276 0.0218  0.0560  -0.0502 628  THR A OG1 
590  C CG2 . THR A 91  ? 0.3041 0.4387 0.4447 -0.0028 0.0678  -0.0365 628  THR A CG2 
591  N N   . PHE A 92  ? 0.2849 0.3622 0.3663 0.0140  0.0269  -0.0199 629  PHE A N   
592  C CA  . PHE A 92  ? 0.2814 0.3385 0.3348 0.0102  0.0235  -0.0127 629  PHE A CA  
593  C C   . PHE A 92  ? 0.3641 0.4157 0.4197 0.0074  0.0117  -0.0109 629  PHE A C   
594  O O   . PHE A 92  ? 0.3351 0.3779 0.3838 -0.0003 0.0127  -0.0081 629  PHE A O   
595  C CB  . PHE A 92  ? 0.2919 0.3361 0.3253 0.0173  0.0210  -0.0119 629  PHE A CB  
596  C CG  . PHE A 92  ? 0.2783 0.3062 0.2900 0.0151  0.0182  -0.0060 629  PHE A CG  
597  C CD1 . PHE A 92  ? 0.3198 0.3389 0.3284 0.0155  0.0099  -0.0050 629  PHE A CD1 
598  C CD2 . PHE A 92  ? 0.3474 0.3693 0.3422 0.0130  0.0235  -0.0021 629  PHE A CD2 
599  C CE1 . PHE A 92  ? 0.3343 0.3407 0.3302 0.0154  0.0087  -0.0020 629  PHE A CE1 
600  C CE2 . PHE A 92  ? 0.3027 0.3111 0.2846 0.0134  0.0185  0.0035  629  PHE A CE2 
601  C CZ  . PHE A 92  ? 0.3562 0.3578 0.3421 0.0155  0.0121  0.0025  629  PHE A CZ  
602  N N   . LEU A 93  ? 0.2826 0.3364 0.3448 0.0130  -0.0002 -0.0124 630  LEU A N   
603  C CA  . LEU A 93  ? 0.3050 0.3513 0.3599 0.0085  -0.0113 -0.0116 630  LEU A CA  
604  C C   . LEU A 93  ? 0.3201 0.3778 0.3934 -0.0009 -0.0135 -0.0144 630  LEU A C   
605  O O   . LEU A 93  ? 0.3174 0.3654 0.3808 -0.0082 -0.0185 -0.0157 630  LEU A O   
606  C CB  . LEU A 93  ? 0.2848 0.3281 0.3353 0.0145  -0.0246 -0.0103 630  LEU A CB  
607  C CG  . LEU A 93  ? 0.2726 0.2988 0.2985 0.0183  -0.0218 -0.0078 630  LEU A CG  
608  C CD1 . LEU A 93  ? 0.2813 0.3007 0.2998 0.0224  -0.0330 -0.0042 630  LEU A CD1 
609  C CD2 . LEU A 93  ? 0.3105 0.3239 0.3169 0.0126  -0.0179 -0.0088 630  LEU A CD2 
610  N N   . THR A 94  ? 0.2783 0.3574 0.3801 -0.0020 -0.0086 -0.0170 631  THR A N   
611  C CA  . THR A 94  ? 0.2802 0.3729 0.4038 -0.0136 -0.0083 -0.0203 631  THR A CA  
612  C C   . THR A 94  ? 0.3187 0.3978 0.4293 -0.0246 0.0050  -0.0175 631  THR A C   
613  O O   . THR A 94  ? 0.2972 0.3724 0.4119 -0.0362 0.0028  -0.0192 631  THR A O   
614  C CB  . THR A 94  ? 0.2829 0.4060 0.4459 -0.0115 -0.0042 -0.0252 631  THR A CB  
615  O OG1 . THR A 94  ? 0.3273 0.4614 0.5076 -0.0015 -0.0220 -0.0264 631  THR A OG1 
616  C CG2 . THR A 94  ? 0.2479 0.3889 0.4376 -0.0267 0.0015  -0.0292 631  THR A CG2 
617  N N   . THR A 95  ? 0.3457 0.4153 0.4396 -0.0220 0.0177  -0.0129 632  THR A N   
618  C CA  . THR A 95  ? 0.2942 0.3522 0.3781 -0.0330 0.0297  -0.0075 632  THR A CA  
619  C C   . THR A 95  ? 0.3218 0.3503 0.3757 -0.0306 0.0283  -0.0004 632  THR A C   
620  O O   . THR A 95  ? 0.3166 0.3298 0.3612 -0.0392 0.0348  0.0064  632  THR A O   
621  C CB  . THR A 95  ? 0.3176 0.3889 0.4047 -0.0356 0.0462  -0.0067 632  THR A CB  
622  O OG1 . THR A 95  ? 0.3146 0.3815 0.3837 -0.0239 0.0469  -0.0062 632  THR A OG1 
623  C CG2 . THR A 95  ? 0.2992 0.4035 0.4251 -0.0382 0.0508  -0.0158 632  THR A CG2 
624  N N   . TYR A 96  ? 0.3082 0.3282 0.3488 -0.0195 0.0200  -0.0013 633  TYR A N   
625  C CA  . TYR A 96  ? 0.3599 0.3585 0.3790 -0.0149 0.0199  0.0046  633  TYR A CA  
626  C C   . TYR A 96  ? 0.3705 0.3474 0.3865 -0.0204 0.0181  0.0064  633  TYR A C   
627  O O   . TYR A 96  ? 0.3765 0.3351 0.3805 -0.0175 0.0186  0.0135  633  TYR A O   
628  C CB  . TYR A 96  ? 0.2862 0.2836 0.2971 -0.0039 0.0131  0.0014  633  TYR A CB  
629  C CG  . TYR A 96  ? 0.2921 0.2827 0.3027 -0.0040 0.0059  -0.0049 633  TYR A CG  
630  C CD1 . TYR A 96  ? 0.3282 0.3007 0.3319 -0.0035 0.0057  -0.0060 633  TYR A CD1 
631  C CD2 . TYR A 96  ? 0.2943 0.2961 0.3108 -0.0048 -0.0011 -0.0100 633  TYR A CD2 
632  C CE1 . TYR A 96  ? 0.3707 0.3370 0.3710 -0.0052 0.0022  -0.0146 633  TYR A CE1 
633  C CE2 . TYR A 96  ? 0.3102 0.3047 0.3186 -0.0073 -0.0074 -0.0158 633  TYR A CE2 
634  C CZ  . TYR A 96  ? 0.3570 0.3341 0.3561 -0.0083 -0.0041 -0.0194 633  TYR A CZ  
635  O OH  . TYR A 96  ? 0.3702 0.3400 0.3584 -0.0124 -0.0075 -0.0282 633  TYR A OH  
636  N N   . ARG A 97  ? 0.3410 0.3185 0.3684 -0.0278 0.0146  -0.0005 634  ARG A N   
637  C CA  . ARG A 97  ? 0.3561 0.3096 0.3809 -0.0327 0.0135  -0.0020 634  ARG A CA  
638  C C   . ARG A 97  ? 0.4199 0.3569 0.4431 -0.0411 0.0205  0.0084  634  ARG A C   
639  O O   . ARG A 97  ? 0.4123 0.3223 0.4318 -0.0419 0.0196  0.0105  634  ARG A O   
640  C CB  . ARG A 97  ? 0.3738 0.3318 0.4084 -0.0415 0.0075  -0.0136 634  ARG A CB  
641  C CG  . ARG A 97  ? 0.3297 0.2990 0.3579 -0.0346 -0.0010 -0.0214 634  ARG A CG  
642  C CD  . ARG A 97  ? 0.3346 0.3178 0.3720 -0.0440 -0.0105 -0.0298 634  ARG A CD  
643  N NE  . ARG A 97  ? 0.3568 0.3521 0.3861 -0.0372 -0.0198 -0.0314 634  ARG A NE  
644  C CZ  . ARG A 97  ? 0.3607 0.3756 0.4003 -0.0306 -0.0229 -0.0263 634  ARG A CZ  
645  N NH1 . ARG A 97  ? 0.3295 0.3577 0.3885 -0.0305 -0.0156 -0.0218 634  ARG A NH1 
646  N NH2 . ARG A 97  ? 0.3086 0.3279 0.3384 -0.0248 -0.0325 -0.0259 634  ARG A NH2 
647  N N   . SER A 98  ? 0.3864 0.3375 0.4121 -0.0477 0.0283  0.0148  635  SER A N   
648  C CA  . SER A 98  ? 0.3823 0.3165 0.3993 -0.0580 0.0364  0.0275  635  SER A CA  
649  C C   . SER A 98  ? 0.4512 0.3679 0.4445 -0.0489 0.0347  0.0402  635  SER A C   
650  O O   . SER A 98  ? 0.4624 0.3597 0.4418 -0.0570 0.0388  0.0540  635  SER A O   
651  C CB  . SER A 98  ? 0.3910 0.3492 0.4174 -0.0703 0.0485  0.0282  635  SER A CB  
652  O OG  . SER A 98  ? 0.3873 0.3665 0.4083 -0.0611 0.0516  0.0268  635  SER A OG  
653  N N   . PHE A 99  ? 0.3932 0.3164 0.3811 -0.0337 0.0278  0.0369  636  PHE A N   
654  C CA  . PHE A 99  ? 0.5031 0.4121 0.4727 -0.0252 0.0228  0.0481  636  PHE A CA  
655  C C   . PHE A 99  ? 0.4347 0.3411 0.4093 -0.0098 0.0131  0.0420  636  PHE A C   
656  O O   . PHE A 99  ? 0.4443 0.3421 0.4101 -0.0016 0.0064  0.0503  636  PHE A O   
657  C CB  . PHE A 99  ? 0.4115 0.3366 0.3641 -0.0264 0.0279  0.0528  636  PHE A CB  
658  C CG  . PHE A 99  ? 0.4253 0.3786 0.3873 -0.0208 0.0300  0.0397  636  PHE A CG  
659  C CD1 . PHE A 99  ? 0.3870 0.3454 0.3491 -0.0082 0.0221  0.0343  636  PHE A CD1 
660  C CD2 . PHE A 99  ? 0.4017 0.3760 0.3746 -0.0284 0.0403  0.0331  636  PHE A CD2 
661  C CE1 . PHE A 99  ? 0.3731 0.3517 0.3423 -0.0037 0.0235  0.0242  636  PHE A CE1 
662  C CE2 . PHE A 99  ? 0.3926 0.3892 0.3770 -0.0214 0.0408  0.0221  636  PHE A CE2 
663  C CZ  . PHE A 99  ? 0.3342 0.3301 0.3143 -0.0093 0.0319  0.0185  636  PHE A CZ  
664  N N   . CYS A 100 ? 0.3674 0.2817 0.3557 -0.0069 0.0122  0.0281  637  CYS A N   
665  C CA  . CYS A 100 ? 0.3639 0.2801 0.3565 0.0052  0.0071  0.0206  637  CYS A CA  
666  C C   . CYS A 100 ? 0.4083 0.3217 0.4104 0.0030  0.0080  0.0066  637  CYS A C   
667  O O   . CYS A 100 ? 0.3659 0.2896 0.3699 -0.0054 0.0095  0.0010  637  CYS A O   
668  C CB  . CYS A 100 ? 0.3669 0.3053 0.3545 0.0102  0.0066  0.0180  637  CYS A CB  
669  S SG  . CYS A 100 ? 0.4022 0.3467 0.3959 0.0210  0.0033  0.0083  637  CYS A SG  
670  N N   . LYS A 101 ? 0.3658 0.2663 0.3746 0.0105  0.0068  0.0000  638  LYS A N   
671  C CA  . LYS A 101 ? 0.3965 0.2935 0.4084 0.0064  0.0095  -0.0157 638  LYS A CA  
672  C C   . LYS A 101 ? 0.3752 0.2924 0.3799 0.0076  0.0100  -0.0240 638  LYS A C   
673  O O   . LYS A 101 ? 0.3809 0.3098 0.3842 0.0148  0.0094  -0.0204 638  LYS A O   
674  C CB  . LYS A 101 ? 0.3898 0.2659 0.4127 0.0135  0.0113  -0.0235 638  LYS A CB  
675  C CG  . LYS A 101 ? 0.5207 0.3683 0.5507 0.0114  0.0098  -0.0159 638  LYS A CG  
676  C CD  . LYS A 101 ? 0.6246 0.4572 0.6559 -0.0004 0.0133  -0.0290 638  LYS A CD  
677  C CE  . LYS A 101 ? 0.6450 0.4425 0.6861 -0.0016 0.0127  -0.0237 638  LYS A CE  
678  N NZ  . LYS A 101 ? 0.7408 0.5201 0.7980 0.0144  0.0126  -0.0291 638  LYS A NZ  
679  N N   . PRO A 102 ? 0.3803 0.3001 0.3785 -0.0008 0.0099  -0.0346 639  PRO A N   
680  C CA  . PRO A 102 ? 0.4257 0.3596 0.4118 -0.0010 0.0093  -0.0400 639  PRO A CA  
681  C C   . PRO A 102 ? 0.3729 0.3073 0.3588 0.0066  0.0154  -0.0458 639  PRO A C   
682  O O   . PRO A 102 ? 0.3784 0.3253 0.3593 0.0094  0.0153  -0.0421 639  PRO A O   
683  C CB  . PRO A 102 ? 0.4284 0.3585 0.4044 -0.0123 0.0066  -0.0510 639  PRO A CB  
684  C CG  . PRO A 102 ? 0.3555 0.2804 0.3429 -0.0195 0.0034  -0.0475 639  PRO A CG  
685  C CD  . PRO A 102 ? 0.3863 0.2972 0.3859 -0.0125 0.0083  -0.0398 639  PRO A CD  
686  N N   . GLN A 103 ? 0.3605 0.2817 0.3549 0.0098  0.0216  -0.0560 640  GLN A N   
687  C CA  . GLN A 103 ? 0.3509 0.2770 0.3538 0.0178  0.0292  -0.0631 640  GLN A CA  
688  C C   . GLN A 103 ? 0.3861 0.3227 0.4019 0.0276  0.0248  -0.0506 640  GLN A C   
689  O O   . GLN A 103 ? 0.3889 0.3399 0.4070 0.0303  0.0280  -0.0523 640  GLN A O   
690  C CB  . GLN A 103 ? 0.3792 0.2888 0.3979 0.0224  0.0362  -0.0766 640  GLN A CB  
691  C CG  . GLN A 103 ? 0.4502 0.3498 0.4532 0.0116  0.0430  -0.0943 640  GLN A CG  
692  C CD  . GLN A 103 ? 0.5190 0.4298 0.5092 0.0079  0.0546  -0.1082 640  GLN A CD  
693  O OE1 . GLN A 103 ? 0.5135 0.4370 0.5181 0.0157  0.0610  -0.1089 640  GLN A OE1 
694  N NE2 . GLN A 103 ? 0.4906 0.3971 0.4526 -0.0057 0.0572  -0.1194 640  GLN A NE2 
695  N N   . GLU A 104 ? 0.3466 0.2754 0.3692 0.0313  0.0177  -0.0382 641  GLU A N   
696  C CA  . GLU A 104 ? 0.3864 0.3234 0.4155 0.0388  0.0113  -0.0259 641  GLU A CA  
697  C C   . GLU A 104 ? 0.4006 0.3546 0.4160 0.0346  0.0099  -0.0213 641  GLU A C   
698  O O   . GLU A 104 ? 0.3756 0.3418 0.3954 0.0389  0.0082  -0.0197 641  GLU A O   
699  C CB  . GLU A 104 ? 0.4038 0.3251 0.4332 0.0396  0.0047  -0.0123 641  GLU A CB  
700  C CG  . GLU A 104 ? 0.4444 0.3699 0.4731 0.0454  -0.0039 0.0020  641  GLU A CG  
701  C CD  . GLU A 104 ? 0.5235 0.4299 0.5435 0.0417  -0.0085 0.0167  641  GLU A CD  
702  O OE1 . GLU A 104 ? 0.5229 0.4292 0.5341 0.0437  -0.0161 0.0302  641  GLU A OE1 
703  O OE2 . GLU A 104 ? 0.4767 0.3673 0.4965 0.0349  -0.0043 0.0146  641  GLU A OE2 
704  N N   . LEU A 105 ? 0.3468 0.3017 0.3487 0.0263  0.0097  -0.0201 642  LEU A N   
705  C CA  . LEU A 105 ? 0.3907 0.3587 0.3833 0.0239  0.0080  -0.0167 642  LEU A CA  
706  C C   . LEU A 105 ? 0.3516 0.3266 0.3401 0.0233  0.0115  -0.0235 642  LEU A C   
707  O O   . LEU A 105 ? 0.3350 0.3185 0.3230 0.0249  0.0106  -0.0207 642  LEU A O   
708  C CB  . LEU A 105 ? 0.3373 0.3065 0.3238 0.0168  0.0060  -0.0153 642  LEU A CB  
709  C CG  . LEU A 105 ? 0.3135 0.2935 0.2944 0.0160  0.0034  -0.0134 642  LEU A CG  
710  C CD1 . LEU A 105 ? 0.2946 0.2810 0.2773 0.0206  0.0036  -0.0080 642  LEU A CD1 
711  C CD2 . LEU A 105 ? 0.3053 0.2898 0.2883 0.0108  -0.0009 -0.0131 642  LEU A CD2 
712  N N   . LEU A 106 ? 0.3592 0.3296 0.3428 0.0191  0.0165  -0.0330 643  LEU A N   
713  C CA  . LEU A 106 ? 0.3148 0.2906 0.2902 0.0155  0.0224  -0.0387 643  LEU A CA  
714  C C   . LEU A 106 ? 0.3750 0.3601 0.3682 0.0216  0.0270  -0.0413 643  LEU A C   
715  O O   . LEU A 106 ? 0.3677 0.3612 0.3589 0.0192  0.0287  -0.0402 643  LEU A O   
716  C CB  . LEU A 106 ? 0.3198 0.2883 0.2820 0.0081  0.0288  -0.0500 643  LEU A CB  
717  C CG  . LEU A 106 ? 0.3556 0.3277 0.3029 0.0008  0.0380  -0.0562 643  LEU A CG  
718  C CD1 . LEU A 106 ? 0.3585 0.3320 0.2899 -0.0035 0.0310  -0.0447 643  LEU A CD1 
719  C CD2 . LEU A 106 ? 0.3616 0.3251 0.2886 -0.0086 0.0448  -0.0684 643  LEU A CD2 
720  N N   . SER A 107 ? 0.3314 0.3147 0.3448 0.0295  0.0276  -0.0445 644  SER A N   
721  C CA  . SER A 107 ? 0.3416 0.3375 0.3786 0.0367  0.0287  -0.0469 644  SER A CA  
722  C C   . SER A 107 ? 0.2879 0.2925 0.3250 0.0386  0.0191  -0.0361 644  SER A C   
723  O O   . SER A 107 ? 0.3290 0.3476 0.3760 0.0380  0.0203  -0.0387 644  SER A O   
724  C CB  . SER A 107 ? 0.2934 0.2830 0.3546 0.0472  0.0272  -0.0500 644  SER A CB  
725  O OG  . SER A 107 ? 0.3237 0.3070 0.3885 0.0455  0.0391  -0.0651 644  SER A OG  
726  N N   . LEU A 108 ? 0.3141 0.3110 0.3397 0.0391  0.0108  -0.0255 645  LEU A N   
727  C CA  . LEU A 108 ? 0.3302 0.3337 0.3507 0.0394  0.0034  -0.0178 645  LEU A CA  
728  C C   . LEU A 108 ? 0.3738 0.3826 0.3834 0.0326  0.0068  -0.0202 645  LEU A C   
729  O O   . LEU A 108 ? 0.3416 0.3589 0.3542 0.0318  0.0039  -0.0202 645  LEU A O   
730  C CB  . LEU A 108 ? 0.3996 0.3939 0.4075 0.0391  -0.0017 -0.0081 645  LEU A CB  
731  C CG  . LEU A 108 ? 0.4030 0.3891 0.4164 0.0448  -0.0088 0.0000  645  LEU A CG  
732  C CD1 . LEU A 108 ? 0.3577 0.3314 0.3571 0.0401  -0.0081 0.0078  645  LEU A CD1 
733  C CD2 . LEU A 108 ? 0.5362 0.5309 0.5505 0.0483  -0.0186 0.0055  645  LEU A CD2 
734  N N   . LEU A 109 ? 0.2897 0.2915 0.2860 0.0271  0.0111  -0.0216 646  LEU A N   
735  C CA  . LEU A 109 ? 0.3248 0.3266 0.3104 0.0213  0.0124  -0.0213 646  LEU A CA  
736  C C   . LEU A 109 ? 0.3324 0.3405 0.3232 0.0166  0.0193  -0.0273 646  LEU A C   
737  O O   . LEU A 109 ? 0.3254 0.3352 0.3145 0.0123  0.0193  -0.0266 646  LEU A O   
738  C CB  . LEU A 109 ? 0.3405 0.3330 0.3110 0.0173  0.0117  -0.0192 646  LEU A CB  
739  C CG  . LEU A 109 ? 0.3482 0.3390 0.3183 0.0201  0.0059  -0.0141 646  LEU A CG  
740  C CD1 . LEU A 109 ? 0.3267 0.3124 0.2885 0.0163  0.0027  -0.0135 646  LEU A CD1 
741  C CD2 . LEU A 109 ? 0.3563 0.3492 0.3272 0.0222  0.0033  -0.0115 646  LEU A CD2 
742  N N   . ILE A 110 ? 0.3188 0.3301 0.3171 0.0161  0.0269  -0.0346 647  ILE A N   
743  C CA  . ILE A 110 ? 0.3057 0.3272 0.3134 0.0105  0.0370  -0.0423 647  ILE A CA  
744  C C   . ILE A 110 ? 0.3496 0.3873 0.3827 0.0149  0.0326  -0.0435 647  ILE A C   
745  O O   . ILE A 110 ? 0.3494 0.3959 0.3885 0.0078  0.0365  -0.0463 647  ILE A O   
746  C CB  . ILE A 110 ? 0.3586 0.3813 0.3711 0.0098  0.0485  -0.0532 647  ILE A CB  
747  C CG1 . ILE A 110 ? 0.3426 0.3499 0.3230 0.0009  0.0519  -0.0528 647  ILE A CG1 
748  C CG2 . ILE A 110 ? 0.3712 0.4114 0.4048 0.0057  0.0618  -0.0643 647  ILE A CG2 
749  C CD1 . ILE A 110 ? 0.3627 0.3678 0.3404 -0.0018 0.0639  -0.0660 647  ILE A CD1 
750  N N   . GLU A 111 ? 0.3067 0.3476 0.3540 0.0255  0.0230  -0.0407 648  GLU A N   
751  C CA  . GLU A 111 ? 0.2998 0.3558 0.3682 0.0300  0.0139  -0.0401 648  GLU A CA  
752  C C   . GLU A 111 ? 0.3441 0.3988 0.3980 0.0239  0.0079  -0.0358 648  GLU A C   
753  O O   . GLU A 111 ? 0.3227 0.3909 0.3899 0.0199  0.0055  -0.0397 648  GLU A O   
754  C CB  . GLU A 111 ? 0.3833 0.4362 0.4603 0.0417  0.0024  -0.0339 648  GLU A CB  
755  C CG  . GLU A 111 ? 0.3641 0.4305 0.4570 0.0466  -0.0122 -0.0303 648  GLU A CG  
756  C CD  . GLU A 111 ? 0.4287 0.4851 0.5199 0.0564  -0.0254 -0.0196 648  GLU A CD  
757  O OE1 . GLU A 111 ? 0.4331 0.4987 0.5353 0.0614  -0.0406 -0.0146 648  GLU A OE1 
758  O OE2 . GLU A 111 ? 0.3672 0.4053 0.4449 0.0579  -0.0216 -0.0153 648  GLU A OE2 
759  N N   . ARG A 112 ? 0.2879 0.3269 0.3172 0.0228  0.0062  -0.0296 649  ARG A N   
760  C CA  . ARG A 112 ? 0.2939 0.3283 0.3102 0.0181  0.0027  -0.0281 649  ARG A CA  
761  C C   . ARG A 112 ? 0.3633 0.3958 0.3784 0.0081  0.0100  -0.0321 649  ARG A C   
762  O O   . ARG A 112 ? 0.3536 0.3871 0.3695 0.0029  0.0072  -0.0345 649  ARG A O   
763  C CB  . ARG A 112 ? 0.3072 0.3274 0.3046 0.0202  0.0019  -0.0226 649  ARG A CB  
764  C CG  . ARG A 112 ? 0.2740 0.2880 0.2609 0.0176  -0.0001 -0.0233 649  ARG A CG  
765  C CD  . ARG A 112 ? 0.3280 0.3474 0.3109 0.0197  -0.0068 -0.0237 649  ARG A CD  
766  N NE  . ARG A 112 ? 0.3256 0.3372 0.2972 0.0178  -0.0055 -0.0273 649  ARG A NE  
767  C CZ  . ARG A 112 ? 0.3528 0.3657 0.3206 0.0135  -0.0085 -0.0341 649  ARG A CZ  
768  N NH1 . ARG A 112 ? 0.3500 0.3742 0.3253 0.0099  -0.0151 -0.0366 649  ARG A NH1 
769  N NH2 . ARG A 112 ? 0.3234 0.3273 0.2822 0.0128  -0.0051 -0.0398 649  ARG A NH2 
770  N N   . PHE A 113 ? 0.2910 0.3187 0.3015 0.0035  0.0195  -0.0328 650  PHE A N   
771  C CA  . PHE A 113 ? 0.2949 0.3156 0.2970 -0.0083 0.0273  -0.0334 650  PHE A CA  
772  C C   . PHE A 113 ? 0.3353 0.3735 0.3593 -0.0157 0.0327  -0.0410 650  PHE A C   
773  O O   . PHE A 113 ? 0.3629 0.3961 0.3843 -0.0264 0.0353  -0.0414 650  PHE A O   
774  C CB  . PHE A 113 ? 0.3822 0.3935 0.3678 -0.0130 0.0359  -0.0319 650  PHE A CB  
775  C CG  . PHE A 113 ? 0.3858 0.3812 0.3511 -0.0255 0.0409  -0.0271 650  PHE A CG  
776  C CD1 . PHE A 113 ? 0.3835 0.3846 0.3524 -0.0386 0.0532  -0.0314 650  PHE A CD1 
777  C CD2 . PHE A 113 ? 0.3836 0.3579 0.3273 -0.0245 0.0331  -0.0175 650  PHE A CD2 
778  C CE1 . PHE A 113 ? 0.4737 0.4552 0.4190 -0.0521 0.0577  -0.0242 650  PHE A CE1 
779  C CE2 . PHE A 113 ? 0.3643 0.3191 0.2873 -0.0354 0.0350  -0.0100 650  PHE A CE2 
780  C CZ  . PHE A 113 ? 0.4233 0.3795 0.3440 -0.0499 0.0473  -0.0123 650  PHE A CZ  
781  N N   . GLU A 114 ? 0.3535 0.4121 0.4024 -0.0104 0.0343  -0.0475 651  GLU A N   
782  C CA  . GLU A 114 ? 0.3111 0.3925 0.3889 -0.0172 0.0416  -0.0568 651  GLU A CA  
783  C C   . GLU A 114 ? 0.3944 0.4903 0.4915 -0.0152 0.0276  -0.0585 651  GLU A C   
784  O O   . GLU A 114 ? 0.3323 0.4476 0.4557 -0.0058 0.0184  -0.0614 651  GLU A O   
785  C CB  . GLU A 114 ? 0.3416 0.4385 0.4418 -0.0106 0.0501  -0.0646 651  GLU A CB  
786  C CG  . GLU A 114 ? 0.4604 0.5412 0.5343 -0.0160 0.0644  -0.0650 651  GLU A CG  
787  C CD  . GLU A 114 ? 0.5880 0.6819 0.6821 -0.0119 0.0773  -0.0771 651  GLU A CD  
788  O OE1 . GLU A 114 ? 0.4848 0.5936 0.6121 0.0017  0.0706  -0.0817 651  GLU A OE1 
789  O OE2 . GLU A 114 ? 0.5556 0.6434 0.6312 -0.0225 0.0939  -0.0822 651  GLU A OE2 
790  N N   . ILE A 115 ? 0.3416 0.4262 0.4249 -0.0246 0.0248  -0.0568 652  ILE A N   
791  C CA  . ILE A 115 ? 0.2828 0.3748 0.3732 -0.0246 0.0103  -0.0592 652  ILE A CA  
792  C C   . ILE A 115 ? 0.3405 0.4584 0.4642 -0.0351 0.0118  -0.0689 652  ILE A C   
793  O O   . ILE A 115 ? 0.3126 0.4263 0.4368 -0.0504 0.0243  -0.0720 652  ILE A O   
794  C CB  . ILE A 115 ? 0.3424 0.4086 0.4047 -0.0296 0.0077  -0.0562 652  ILE A CB  
795  C CG1 . ILE A 115 ? 0.3404 0.3862 0.3770 -0.0193 0.0071  -0.0478 652  ILE A CG1 
796  C CG2 . ILE A 115 ? 0.2834 0.3571 0.3495 -0.0313 -0.0059 -0.0619 652  ILE A CG2 
797  C CD1 . ILE A 115 ? 0.3700 0.3896 0.3847 -0.0222 0.0077  -0.0453 652  ILE A CD1 
798  N N   . PRO A 116 ? 0.2640 0.4083 0.4163 -0.0287 -0.0015 -0.0732 653  PRO A N   
799  C CA  . PRO A 116 ? 0.3010 0.4742 0.4904 -0.0393 -0.0031 -0.0835 653  PRO A CA  
800  C C   . PRO A 116 ? 0.3143 0.4801 0.4918 -0.0517 -0.0127 -0.0871 653  PRO A C   
801  O O   . PRO A 116 ? 0.3228 0.4701 0.4708 -0.0471 -0.0240 -0.0831 653  PRO A O   
802  C CB  . PRO A 116 ? 0.3123 0.5140 0.5353 -0.0245 -0.0193 -0.0846 653  PRO A CB  
803  C CG  . PRO A 116 ? 0.2939 0.4747 0.4845 -0.0109 -0.0328 -0.0734 653  PRO A CG  
804  C CD  . PRO A 116 ? 0.3075 0.4559 0.4604 -0.0118 -0.0171 -0.0673 653  PRO A CD  
805  N N   . GLU A 117 ? 0.3182 0.4984 0.5195 -0.0690 -0.0063 -0.0963 654  GLU A N   
806  C CA  . GLU A 117 ? 0.3273 0.4999 0.5203 -0.0823 -0.0158 -0.1023 654  GLU A CA  
807  C C   . GLU A 117 ? 0.3480 0.5513 0.5650 -0.0794 -0.0399 -0.1089 654  GLU A C   
808  O O   . GLU A 117 ? 0.3527 0.5896 0.6076 -0.0711 -0.0466 -0.1104 654  GLU A O   
809  C CB  . GLU A 117 ? 0.3304 0.5010 0.5359 -0.1051 0.0004  -0.1087 654  GLU A CB  
810  C CG  . GLU A 117 ? 0.3562 0.4900 0.5287 -0.1092 0.0200  -0.0992 654  GLU A CG  
811  C CD  . GLU A 117 ? 0.5277 0.6500 0.7030 -0.1335 0.0366  -0.1015 654  GLU A CD  
812  O OE1 . GLU A 117 ? 0.5087 0.6576 0.7191 -0.1492 0.0381  -0.1122 654  GLU A OE1 
813  O OE2 . GLU A 117 ? 0.5503 0.6358 0.6924 -0.1376 0.0475  -0.0914 654  GLU A OE2 
814  N N   . PRO A 118 ? 0.3288 0.5200 0.5232 -0.0851 -0.0542 -0.1130 655  PRO A N   
815  C CA  . PRO A 118 ? 0.3686 0.5878 0.5794 -0.0852 -0.0799 -0.1191 655  PRO A CA  
816  C C   . PRO A 118 ? 0.4148 0.6738 0.6807 -0.0980 -0.0821 -0.1302 655  PRO A C   
817  O O   . PRO A 118 ? 0.3896 0.6464 0.6695 -0.1154 -0.0642 -0.1370 655  PRO A O   
818  C CB  . PRO A 118 ? 0.4041 0.5975 0.5760 -0.0953 -0.0876 -0.1258 655  PRO A CB  
819  C CG  . PRO A 118 ? 0.3941 0.5468 0.5281 -0.0905 -0.0699 -0.1191 655  PRO A CG  
820  C CD  . PRO A 118 ? 0.4417 0.5922 0.5929 -0.0902 -0.0486 -0.1127 655  PRO A CD  
821  N N   . GLU A 119 ? 0.4091 0.7048 0.7076 -0.0897 -0.1047 -0.1313 656  GLU A N   
822  C CA  . GLU A 119 ? 0.5016 0.8428 0.8623 -0.0998 -0.1088 -0.1429 656  GLU A CA  
823  C C   . GLU A 119 ? 0.5645 0.9059 0.9254 -0.1255 -0.1128 -0.1569 656  GLU A C   
824  O O   . GLU A 119 ? 0.6742 1.0042 1.0039 -0.1292 -0.1334 -0.1598 656  GLU A O   
825  C CB  . GLU A 119 ? 0.6315 1.0111 1.0284 -0.0838 -0.1382 -0.1404 656  GLU A CB  
826  C CG  . GLU A 119 ? 0.8037 1.2256 1.2705 -0.0761 -0.1299 -0.1449 656  GLU A CG  
827  C CD  . GLU A 119 ? 0.9610 1.3638 1.4194 -0.0633 -0.1020 -0.1377 656  GLU A CD  
828  O OE1 . GLU A 119 ? 1.0015 1.3831 1.4315 -0.0435 -0.1090 -0.1245 656  GLU A OE1 
829  O OE2 . GLU A 119 ? 1.0135 1.4213 1.4908 -0.0750 -0.0727 -0.1453 656  GLU A OE2 
830  N N   . PRO A 120 ? 0.5601 0.9116 0.9519 -0.1453 -0.0925 -0.1664 657  PRO A N   
831  C CA  . PRO A 120 ? 0.6309 0.9784 1.0236 -0.1720 -0.0954 -0.1802 657  PRO A CA  
832  C C   . PRO A 120 ? 0.5234 0.9008 0.9355 -0.1726 -0.1264 -0.1846 657  PRO A C   
833  O O   . PRO A 120 ? 0.5644 0.9790 1.0151 -0.1589 -0.1391 -0.1799 657  PRO A O   
834  C CB  . PRO A 120 ? 0.6807 1.0360 1.1062 -0.1896 -0.0660 -0.1836 657  PRO A CB  
835  C CG  . PRO A 120 ? 0.6810 1.0293 1.1024 -0.1754 -0.0434 -0.1734 657  PRO A CG  
836  C CD  . PRO A 120 ? 0.6569 1.0199 1.0794 -0.1464 -0.0636 -0.1654 657  PRO A CD  
837  N N   . THR A 121 ? 0.6414 0.9976 1.0221 -0.1873 -0.1385 -0.1922 658  THR A N   
838  C CA  . THR A 121 ? 0.7055 1.0839 1.0963 -0.1928 -0.1672 -0.1960 658  THR A CA  
839  C C   . THR A 121 ? 0.7462 1.1474 1.1834 -0.2126 -0.1591 -0.2036 658  THR A C   
840  O O   . THR A 121 ? 0.7408 1.1285 1.1874 -0.2265 -0.1307 -0.2068 658  THR A O   
841  C CB  . THR A 121 ? 0.7964 1.1401 1.1302 -0.2014 -0.1819 -0.2029 658  THR A CB  
842  O OG1 . THR A 121 ? 0.8854 1.1906 1.1999 -0.2199 -0.1592 -0.2124 658  THR A OG1 
843  C CG2 . THR A 121 ? 0.7781 1.1026 1.0639 -0.1822 -0.1909 -0.1954 658  THR A CG2 
844  N N   . ASP A 122 ? 0.7760 1.2120 1.2411 -0.2145 -0.1849 -0.2049 659  ASP A N   
845  C CA  . ASP A 122 ? 0.8430 1.3018 1.3497 -0.2356 -0.1818 -0.2138 659  ASP A CA  
846  C C   . ASP A 122 ? 0.9773 1.3959 1.4502 -0.2603 -0.1745 -0.2248 659  ASP A C   
847  O O   . ASP A 122 ? 1.1209 1.5296 1.5683 -0.2689 -0.1980 -0.2313 659  ASP A O   
848  C CB  . ASP A 122 ? 0.9197 1.4218 1.4577 -0.2335 -0.2156 -0.2130 659  ASP A CB  
849  C CG  . ASP A 122 ? 1.0194 1.5278 1.5357 -0.2096 -0.2431 -0.2007 659  ASP A CG  
850  O OD1 . ASP A 122 ? 1.0170 1.5577 1.5714 -0.1897 -0.2467 -0.1913 659  ASP A OD1 
851  O OD2 . ASP A 122 ? 1.1001 1.5786 1.5593 -0.2108 -0.2597 -0.2002 659  ASP A OD2 
852  N N   . ALA A 123 ? 0.9991 1.3923 1.4704 -0.2715 -0.1418 -0.2262 660  ALA A N   
853  C CA  . ALA A 123 ? 1.0211 1.3658 1.4584 -0.2918 -0.1287 -0.2335 660  ALA A CA  
854  C C   . ALA A 123 ? 0.9532 1.2709 1.3831 -0.2929 -0.0937 -0.2262 660  ALA A C   
855  O O   . ALA A 123 ? 0.8844 1.1846 1.3212 -0.3127 -0.0729 -0.2274 660  ALA A O   
856  C CB  . ALA A 123 ? 1.0716 1.3776 1.4505 -0.2875 -0.1450 -0.2383 660  ALA A CB  
857  N N   . ASP A 124 ? 0.8045 1.1180 1.2182 -0.2721 -0.0882 -0.2174 661  ASP A N   
858  C CA  . ASP A 124 ? 0.9176 1.2134 1.3276 -0.2715 -0.0570 -0.2085 661  ASP A CA  
859  C C   . ASP A 124 ? 0.9568 1.2927 1.4178 -0.2758 -0.0403 -0.2064 661  ASP A C   
860  O O   . ASP A 124 ? 1.0339 1.3532 1.4948 -0.2905 -0.0127 -0.2026 661  ASP A O   
861  C CB  . ASP A 124 ? 0.8609 1.1475 1.2449 -0.2482 -0.0579 -0.2008 661  ASP A CB  
862  C CG  . ASP A 124 ? 0.7953 1.0487 1.1301 -0.2418 -0.0752 -0.2045 661  ASP A CG  
863  O OD1 . ASP A 124 ? 0.8078 1.0359 1.1233 -0.2560 -0.0813 -0.2131 661  ASP A OD1 
864  O OD2 . ASP A 124 ? 0.7129 0.9652 1.0279 -0.2223 -0.0818 -0.1995 661  ASP A OD2 
865  N N   . LYS A 125 ? 0.8667 1.2536 1.3699 -0.2630 -0.0567 -0.2082 662  LYS A N   
866  C CA  . LYS A 125 ? 0.8083 1.2366 1.3637 -0.2631 -0.0407 -0.2083 662  LYS A CA  
867  C C   . LYS A 125 ? 0.7964 1.2327 1.3777 -0.2904 -0.0289 -0.2153 662  LYS A C   
868  O O   . LYS A 125 ? 0.7570 1.2011 1.3574 -0.3000 -0.0005 -0.2142 662  LYS A O   
869  C CB  . LYS A 125 ? 0.7726 1.2505 1.3687 -0.2414 -0.0652 -0.2085 662  LYS A CB  
870  C CG  . LYS A 125 ? 0.7618 1.2338 1.3373 -0.2135 -0.0747 -0.1999 662  LYS A CG  
871  C CD  . LYS A 125 ? 0.7538 1.2714 1.3752 -0.1906 -0.0906 -0.1972 662  LYS A CD  
872  C CE  . LYS A 125 ? 0.7181 1.2259 1.3246 -0.1647 -0.0868 -0.1881 662  LYS A CE  
873  N NZ  . LYS A 125 ? 0.7539 1.2823 1.3724 -0.1400 -0.1194 -0.1808 662  LYS A NZ  
874  N N   . ILE A 135 ? 1.1121 1.1099 1.3315 -0.3179 0.0615  -0.1476 672  ILE A N   
875  C CA  . ILE A 135 ? 0.9885 1.0061 1.2043 -0.2953 0.0491  -0.1524 672  ILE A CA  
876  C C   . ILE A 135 ? 0.9910 0.9957 1.1955 -0.2878 0.0270  -0.1670 672  ILE A C   
877  O O   . ILE A 135 ? 1.0949 1.0500 1.2747 -0.2920 0.0263  -0.1673 672  ILE A O   
878  C CB  . ILE A 135 ? 0.9054 0.8911 1.0825 -0.2766 0.0585  -0.1319 672  ILE A CB  
879  C CG1 . ILE A 135 ? 0.9359 0.9481 1.1246 -0.2813 0.0783  -0.1221 672  ILE A CG1 
880  C CG2 . ILE A 135 ? 0.7993 0.7892 0.9584 -0.2447 0.0416  -0.1314 672  ILE A CG2 
881  C CD1 . ILE A 135 ? 0.9633 0.9308 1.1098 -0.2801 0.0932  -0.1003 672  ILE A CD1 
882  N N   . SER A 136 ? 0.8565 0.9046 1.0768 -0.2746 0.0084  -0.1776 673  SER A N   
883  C CA  . SER A 136 ? 0.7529 0.7935 0.9586 -0.2702 -0.0124 -0.1928 673  SER A CA  
884  C C   . SER A 136 ? 0.6041 0.5936 0.7632 -0.2516 -0.0114 -0.1864 673  SER A C   
885  O O   . SER A 136 ? 0.5622 0.5336 0.7028 -0.2356 -0.0006 -0.1686 673  SER A O   
886  C CB  . SER A 136 ? 0.5985 0.6923 0.8213 -0.2562 -0.0337 -0.1992 673  SER A CB  
887  O OG  . SER A 136 ? 0.6075 0.6990 0.8054 -0.2273 -0.0352 -0.1854 673  SER A OG  
888  N N   . ALA A 137 ? 0.6161 0.5834 0.7577 -0.2544 -0.0224 -0.2028 674  ALA A N   
889  C CA  . ALA A 137 ? 0.6842 0.6058 0.7881 -0.2368 -0.0200 -0.2007 674  ALA A CA  
890  C C   . ALA A 137 ? 0.6207 0.5620 0.7073 -0.2086 -0.0260 -0.1916 674  ALA A C   
891  O O   . ALA A 137 ? 0.5785 0.4926 0.6438 -0.1906 -0.0180 -0.1797 674  ALA A O   
892  C CB  . ALA A 137 ? 0.7413 0.6376 0.8312 -0.2453 -0.0285 -0.2226 674  ALA A CB  
893  N N   . ASP A 138 ? 0.6939 0.6823 0.7910 -0.2048 -0.0411 -0.1961 675  ASP A N   
894  C CA  . ASP A 138 ? 0.6328 0.6389 0.7139 -0.1802 -0.0472 -0.1860 675  ASP A CA  
895  C C   . ASP A 138 ? 0.5155 0.5258 0.6040 -0.1672 -0.0344 -0.1646 675  ASP A C   
896  O O   . ASP A 138 ? 0.4562 0.4544 0.5231 -0.1475 -0.0308 -0.1539 675  ASP A O   
897  C CB  . ASP A 138 ? 0.6728 0.7262 0.7660 -0.1803 -0.0685 -0.1923 675  ASP A CB  
898  C CG  . ASP A 138 ? 0.9524 1.0004 1.0222 -0.1883 -0.0839 -0.2120 675  ASP A CG  
899  O OD1 . ASP A 138 ? 1.0436 1.0515 1.0916 -0.1941 -0.0757 -0.2237 675  ASP A OD1 
900  O OD2 . ASP A 138 ? 1.0777 1.1605 1.1500 -0.1887 -0.1049 -0.2162 675  ASP A OD2 
901  N N   . LEU A 139 ? 0.4497 0.4783 0.5684 -0.1794 -0.0264 -0.1597 676  LEU A N   
902  C CA  . LEU A 139 ? 0.4546 0.4883 0.5780 -0.1697 -0.0129 -0.1422 676  LEU A CA  
903  C C   . LEU A 139 ? 0.4663 0.4516 0.5635 -0.1675 0.0017  -0.1304 676  LEU A C   
904  O O   . LEU A 139 ? 0.4768 0.4556 0.5592 -0.1511 0.0070  -0.1164 676  LEU A O   
905  C CB  . LEU A 139 ? 0.5664 0.6342 0.7295 -0.1856 -0.0053 -0.1433 676  LEU A CB  
906  C CG  . LEU A 139 ? 0.6255 0.7034 0.7944 -0.1781 0.0106  -0.1291 676  LEU A CG  
907  C CD1 . LEU A 139 ? 0.5798 0.6744 0.7417 -0.1520 0.0018  -0.1225 676  LEU A CD1 
908  C CD2 . LEU A 139 ? 0.5665 0.6829 0.7795 -0.1955 0.0209  -0.1347 676  LEU A CD2 
909  N N   . LYS A 140 ? 0.4886 0.4383 0.5804 -0.1838 0.0066  -0.1355 677  LYS A N   
910  C CA  . LYS A 140 ? 0.4899 0.3896 0.5571 -0.1794 0.0159  -0.1231 677  LYS A CA  
911  C C   . LYS A 140 ? 0.4803 0.3648 0.5244 -0.1549 0.0094  -0.1220 677  LYS A C   
912  O O   . LYS A 140 ? 0.4721 0.3407 0.5018 -0.1406 0.0140  -0.1067 677  LYS A O   
913  C CB  . LYS A 140 ? 0.5804 0.4403 0.6476 -0.2003 0.0198  -0.1299 677  LYS A CB  
914  C CG  . LYS A 140 ? 0.7267 0.5314 0.7714 -0.1957 0.0272  -0.1142 677  LYS A CG  
915  C CD  . LYS A 140 ? 0.8962 0.6557 0.9416 -0.2160 0.0303  -0.1202 677  LYS A CD  
916  C CE  . LYS A 140 ? 0.9708 0.6727 0.9952 -0.2091 0.0342  -0.1018 677  LYS A CE  
917  N NZ  . LYS A 140 ? 0.9747 0.6281 1.0004 -0.2320 0.0387  -0.1028 677  LYS A NZ  
918  N N   . ARG A 141 ? 0.4972 0.3885 0.5372 -0.1510 -0.0011 -0.1390 678  ARG A N   
919  C CA  . ARG A 141 ? 0.5926 0.4774 0.6124 -0.1293 -0.0048 -0.1402 678  ARG A CA  
920  C C   . ARG A 141 ? 0.5094 0.4206 0.5270 -0.1123 -0.0050 -0.1252 678  ARG A C   
921  O O   . ARG A 141 ? 0.4699 0.3667 0.4746 -0.0959 -0.0015 -0.1160 678  ARG A O   
922  C CB  . ARG A 141 ? 0.5716 0.4694 0.5839 -0.1315 -0.0154 -0.1609 678  ARG A CB  
923  C CG  . ARG A 141 ? 0.8454 0.7062 0.8437 -0.1327 -0.0131 -0.1778 678  ARG A CG  
924  C CD  . ARG A 141 ? 0.8264 0.7049 0.8071 -0.1315 -0.0224 -0.1962 678  ARG A CD  
925  N NE  . ARG A 141 ? 0.7299 0.6073 0.6912 -0.1111 -0.0183 -0.1933 678  ARG A NE  
926  C CZ  . ARG A 141 ? 0.6114 0.5016 0.5498 -0.1084 -0.0229 -0.2060 678  ARG A CZ  
927  N NH1 . ARG A 141 ? 0.5628 0.4677 0.4924 -0.1238 -0.0348 -0.2218 678  ARG A NH1 
928  N NH2 . ARG A 141 ? 0.6436 0.5326 0.5669 -0.0917 -0.0158 -0.2028 678  ARG A NH2 
929  N N   . PHE A 142 ? 0.4599 0.4107 0.4933 -0.1157 -0.0099 -0.1239 679  PHE A N   
930  C CA  . PHE A 142 ? 0.4212 0.3959 0.4544 -0.0998 -0.0109 -0.1119 679  PHE A CA  
931  C C   . PHE A 142 ? 0.4067 0.3658 0.4357 -0.0945 0.0008  -0.0955 679  PHE A C   
932  O O   . PHE A 142 ? 0.3928 0.3481 0.4091 -0.0785 0.0015  -0.0866 679  PHE A O   
933  C CB  . PHE A 142 ? 0.4176 0.4352 0.4757 -0.1044 -0.0186 -0.1144 679  PHE A CB  
934  C CG  . PHE A 142 ? 0.3862 0.4258 0.4467 -0.0878 -0.0205 -0.1035 679  PHE A CG  
935  C CD1 . PHE A 142 ? 0.4227 0.4652 0.4651 -0.0736 -0.0297 -0.1019 679  PHE A CD1 
936  C CD2 . PHE A 142 ? 0.4264 0.4822 0.5065 -0.0878 -0.0117 -0.0959 679  PHE A CD2 
937  C CE1 . PHE A 142 ? 0.3995 0.4575 0.4441 -0.0594 -0.0316 -0.0914 679  PHE A CE1 
938  C CE2 . PHE A 142 ? 0.3624 0.4348 0.4459 -0.0723 -0.0132 -0.0879 679  PHE A CE2 
939  C CZ  . PHE A 142 ? 0.3965 0.4688 0.4631 -0.0581 -0.0240 -0.0849 679  PHE A CZ  
940  N N   . ARG A 143 ? 0.4185 0.3671 0.4555 -0.1096 0.0102  -0.0912 680  ARG A N   
941  C CA  . ARG A 143 ? 0.4579 0.3917 0.4844 -0.1069 0.0202  -0.0750 680  ARG A CA  
942  C C   . ARG A 143 ? 0.4378 0.3318 0.4424 -0.0967 0.0193  -0.0671 680  ARG A C   
943  O O   . ARG A 143 ? 0.4593 0.3467 0.4517 -0.0862 0.0210  -0.0543 680  ARG A O   
944  C CB  . ARG A 143 ? 0.4731 0.4034 0.5083 -0.1286 0.0319  -0.0717 680  ARG A CB  
945  C CG  . ARG A 143 ? 0.4774 0.4523 0.5429 -0.1381 0.0350  -0.0801 680  ARG A CG  
946  C CD  . ARG A 143 ? 0.5395 0.5100 0.6146 -0.1629 0.0496  -0.0789 680  ARG A CD  
947  N NE  . ARG A 143 ? 0.5583 0.5760 0.6688 -0.1709 0.0554  -0.0876 680  ARG A NE  
948  C CZ  . ARG A 143 ? 0.6080 0.6354 0.7366 -0.1942 0.0704  -0.0904 680  ARG A CZ  
949  N NH1 . ARG A 143 ? 0.6432 0.6318 0.7520 -0.2131 0.0804  -0.0827 680  ARG A NH1 
950  N NH2 . ARG A 143 ? 0.6797 0.7554 0.8480 -0.1987 0.0755  -0.1005 680  ARG A NH2 
951  N N   . LYS A 144 ? 0.4493 0.3172 0.4513 -0.0994 0.0160  -0.0760 681  LYS A N   
952  C CA  . LYS A 144 ? 0.4583 0.2867 0.4476 -0.0892 0.0149  -0.0704 681  LYS A CA  
953  C C   . LYS A 144 ? 0.5094 0.3451 0.4950 -0.0685 0.0099  -0.0760 681  LYS A C   
954  O O   . LYS A 144 ? 0.4787 0.3005 0.4586 -0.0545 0.0090  -0.0659 681  LYS A O   
955  C CB  . LYS A 144 ? 0.5483 0.3423 0.5405 -0.1018 0.0154  -0.0797 681  LYS A CB  
956  C CG  . LYS A 144 ? 0.7635 0.5097 0.7484 -0.0933 0.0142  -0.0724 681  LYS A CG  
957  C CD  . LYS A 144 ? 0.9182 0.6268 0.9074 -0.1102 0.0160  -0.0805 681  LYS A CD  
958  C CE  . LYS A 144 ? 1.1123 0.7722 1.1005 -0.0976 0.0128  -0.0783 681  LYS A CE  
959  N NZ  . LYS A 144 ? 1.1742 0.8460 1.1674 -0.0748 0.0101  -0.0917 681  LYS A NZ  
960  N N   . GLU A 145 ? 0.4591 0.3171 0.4471 -0.0676 0.0063  -0.0918 682  GLU A N   
961  C CA  . GLU A 145 ? 0.4534 0.3176 0.4345 -0.0519 0.0044  -0.0989 682  GLU A CA  
962  C C   . GLU A 145 ? 0.4206 0.3161 0.3989 -0.0418 0.0025  -0.0904 682  GLU A C   
963  O O   . GLU A 145 ? 0.4910 0.3891 0.4636 -0.0285 0.0034  -0.0908 682  GLU A O   
964  C CB  . GLU A 145 ? 0.5115 0.3802 0.4882 -0.0581 0.0016  -0.1202 682  GLU A CB  
965  C CG  . GLU A 145 ? 0.7207 0.5548 0.6999 -0.0669 0.0041  -0.1332 682  GLU A CG  
966  C CD  . GLU A 145 ? 0.7425 0.5808 0.7127 -0.0734 0.0016  -0.1572 682  GLU A CD  
967  O OE1 . GLU A 145 ? 0.7623 0.6222 0.7192 -0.0661 0.0001  -0.1628 682  GLU A OE1 
968  O OE2 . GLU A 145 ? 0.9121 0.7306 0.8858 -0.0878 0.0013  -0.1704 682  GLU A OE2 
969  N N   . TYR A 146 ? 0.3875 0.3065 0.3721 -0.0480 0.0010  -0.0838 683  TYR A N   
970  C CA  . TYR A 146 ? 0.3438 0.2898 0.3276 -0.0385 -0.0016 -0.0773 683  TYR A CA  
971  C C   . TYR A 146 ? 0.4009 0.3512 0.3889 -0.0370 0.0028  -0.0632 683  TYR A C   
972  O O   . TYR A 146 ? 0.3709 0.3201 0.3527 -0.0258 0.0036  -0.0550 683  TYR A O   
973  C CB  . TYR A 146 ? 0.3945 0.3687 0.3838 -0.0439 -0.0097 -0.0848 683  TYR A CB  
974  C CG  . TYR A 146 ? 0.3573 0.3520 0.3425 -0.0326 -0.0143 -0.0783 683  TYR A CG  
975  C CD1 . TYR A 146 ? 0.3862 0.3806 0.3539 -0.0259 -0.0170 -0.0817 683  TYR A CD1 
976  C CD2 . TYR A 146 ? 0.3821 0.3941 0.3804 -0.0295 -0.0141 -0.0691 683  TYR A CD2 
977  C CE1 . TYR A 146 ? 0.3443 0.3531 0.3061 -0.0173 -0.0208 -0.0733 683  TYR A CE1 
978  C CE2 . TYR A 146 ? 0.3601 0.3856 0.3558 -0.0192 -0.0186 -0.0626 683  TYR A CE2 
979  C CZ  . TYR A 146 ? 0.4089 0.4315 0.3856 -0.0137 -0.0226 -0.0634 683  TYR A CZ  
980  O OH  . TYR A 146 ? 0.3617 0.3938 0.3338 -0.0054 -0.0269 -0.0550 683  TYR A OH  
981  N N   . VAL A 147 ? 0.3563 0.3121 0.3544 -0.0493 0.0066  -0.0615 684  VAL A N   
982  C CA  . VAL A 147 ? 0.3563 0.3202 0.3560 -0.0494 0.0129  -0.0515 684  VAL A CA  
983  C C   . VAL A 147 ? 0.4263 0.3631 0.4087 -0.0456 0.0160  -0.0396 684  VAL A C   
984  O O   . VAL A 147 ? 0.4085 0.3497 0.3843 -0.0365 0.0159  -0.0326 684  VAL A O   
985  C CB  . VAL A 147 ? 0.3934 0.3696 0.4084 -0.0658 0.0201  -0.0543 684  VAL A CB  
986  C CG1 . VAL A 147 ? 0.3938 0.3766 0.4063 -0.0664 0.0297  -0.0463 684  VAL A CG1 
987  C CG2 . VAL A 147 ? 0.3573 0.3657 0.3954 -0.0677 0.0135  -0.0654 684  VAL A CG2 
988  N N   . GLN A 148 ? 0.4418 0.3493 0.4172 -0.0533 0.0174  -0.0366 685  GLN A N   
989  C CA  . GLN A 148 ? 0.3839 0.2651 0.3428 -0.0497 0.0166  -0.0227 685  GLN A CA  
990  C C   . GLN A 148 ? 0.3949 0.2739 0.3526 -0.0312 0.0092  -0.0213 685  GLN A C   
991  O O   . GLN A 148 ? 0.4224 0.3029 0.3717 -0.0251 0.0072  -0.0118 685  GLN A O   
992  C CB  . GLN A 148 ? 0.5575 0.4027 0.5093 -0.0609 0.0175  -0.0173 685  GLN A CB  
993  C CG  . GLN A 148 ? 0.6071 0.4247 0.5394 -0.0574 0.0133  0.0005  685  GLN A CG  
994  C CD  . GLN A 148 ? 0.8269 0.6055 0.7464 -0.0716 0.0143  0.0113  685  GLN A CD  
995  O OE1 . GLN A 148 ? 0.8528 0.6294 0.7602 -0.0900 0.0235  0.0176  685  GLN A OE1 
996  N NE2 . GLN A 148 ? 0.7995 0.5457 0.7224 -0.0634 0.0057  0.0135  685  GLN A NE2 
997  N N   . PRO A 149 ? 0.3903 0.2682 0.3562 -0.0231 0.0061  -0.0319 686  PRO A N   
998  C CA  . PRO A 149 ? 0.4273 0.3076 0.3956 -0.0069 0.0022  -0.0316 686  PRO A CA  
999  C C   . PRO A 149 ? 0.4506 0.3578 0.4181 -0.0012 0.0024  -0.0289 686  PRO A C   
1000 O O   . PRO A 149 ? 0.4106 0.3174 0.3772 0.0072  -0.0007 -0.0217 686  PRO A O   
1001 C CB  . PRO A 149 ? 0.3972 0.2764 0.3724 -0.0034 0.0033  -0.0475 686  PRO A CB  
1002 C CG  . PRO A 149 ? 0.4305 0.2894 0.4059 -0.0162 0.0045  -0.0525 686  PRO A CG  
1003 C CD  . PRO A 149 ? 0.4111 0.2824 0.3834 -0.0296 0.0068  -0.0456 686  PRO A CD  
1004 N N   . VAL A 150 ? 0.3913 0.3209 0.3610 -0.0056 0.0045  -0.0344 687  VAL A N   
1005 C CA  . VAL A 150 ? 0.3299 0.2802 0.2999 0.0001  0.0042  -0.0313 687  VAL A CA  
1006 C C   . VAL A 150 ? 0.4015 0.3496 0.3658 -0.0019 0.0058  -0.0216 687  VAL A C   
1007 O O   . VAL A 150 ? 0.3818 0.3342 0.3438 0.0046  0.0040  -0.0171 687  VAL A O   
1008 C CB  . VAL A 150 ? 0.3486 0.3204 0.3244 -0.0030 0.0033  -0.0374 687  VAL A CB  
1009 C CG1 . VAL A 150 ? 0.3075 0.2946 0.2855 0.0023  0.0032  -0.0325 687  VAL A CG1 
1010 C CG2 . VAL A 150 ? 0.3217 0.2965 0.2944 -0.0006 0.0003  -0.0461 687  VAL A CG2 
1011 N N   . GLN A 151 ? 0.3761 0.3177 0.3367 -0.0131 0.0100  -0.0192 688  GLN A N   
1012 C CA  . GLN A 151 ? 0.3887 0.3272 0.3375 -0.0179 0.0136  -0.0115 688  GLN A CA  
1013 C C   . GLN A 151 ? 0.4021 0.3213 0.3376 -0.0129 0.0065  -0.0014 688  GLN A C   
1014 O O   . GLN A 151 ? 0.3891 0.3117 0.3156 -0.0110 0.0049  0.0030  688  GLN A O   
1015 C CB  . GLN A 151 ? 0.3455 0.2799 0.2908 -0.0335 0.0222  -0.0113 688  GLN A CB  
1016 C CG  . GLN A 151 ? 0.3418 0.3043 0.3074 -0.0369 0.0283  -0.0219 688  GLN A CG  
1017 C CD  . GLN A 151 ? 0.4134 0.3795 0.3829 -0.0534 0.0396  -0.0244 688  GLN A CD  
1018 O OE1 . GLN A 151 ? 0.3965 0.3402 0.3514 -0.0650 0.0429  -0.0179 688  GLN A OE1 
1019 N NE2 . GLN A 151 ? 0.4056 0.4003 0.3977 -0.0550 0.0458  -0.0336 688  GLN A NE2 
1020 N N   . LEU A 152 ? 0.4328 0.3314 0.3689 -0.0103 0.0010  0.0017  689  LEU A N   
1021 C CA  . LEU A 152 ? 0.4181 0.3001 0.3484 -0.0029 -0.0091 0.0117  689  LEU A CA  
1022 C C   . LEU A 152 ? 0.4312 0.3302 0.3751 0.0105  -0.0137 0.0079  689  LEU A C   
1023 O O   . LEU A 152 ? 0.3955 0.2931 0.3359 0.0149  -0.0219 0.0153  689  LEU A O   
1024 C CB  . LEU A 152 ? 0.4343 0.2887 0.3684 -0.0012 -0.0141 0.0147  689  LEU A CB  
1025 C CG  . LEU A 152 ? 0.4883 0.3184 0.4078 -0.0165 -0.0104 0.0211  689  LEU A CG  
1026 C CD1 . LEU A 152 ? 0.5548 0.3552 0.4831 -0.0129 -0.0155 0.0215  689  LEU A CD1 
1027 C CD2 . LEU A 152 ? 0.6435 0.4599 0.5354 -0.0257 -0.0134 0.0373  689  LEU A CD2 
1028 N N   . ARG A 153 ? 0.3877 0.3027 0.3457 0.0155  -0.0089 -0.0033 690  ARG A N   
1029 C CA  . ARG A 153 ? 0.4078 0.3397 0.3766 0.0248  -0.0101 -0.0065 690  ARG A CA  
1030 C C   . ARG A 153 ? 0.4292 0.3733 0.3907 0.0220  -0.0101 -0.0027 690  ARG A C   
1031 O O   . ARG A 153 ? 0.3782 0.3285 0.3445 0.0267  -0.0148 -0.0001 690  ARG A O   
1032 C CB  . ARG A 153 ? 0.4152 0.3605 0.3914 0.0269  -0.0037 -0.0175 690  ARG A CB  
1033 C CG  . ARG A 153 ? 0.5553 0.4896 0.5367 0.0282  -0.0017 -0.0262 690  ARG A CG  
1034 C CD  . ARG A 153 ? 0.4727 0.4030 0.4693 0.0389  -0.0023 -0.0303 690  ARG A CD  
1035 N NE  . ARG A 153 ? 0.5211 0.4411 0.5214 0.0392  0.0024  -0.0427 690  ARG A NE  
1036 C CZ  . ARG A 153 ? 0.6341 0.5328 0.6456 0.0447  0.0001  -0.0451 690  ARG A CZ  
1037 N NH1 . ARG A 153 ? 0.6559 0.5426 0.6762 0.0513  -0.0090 -0.0336 690  ARG A NH1 
1038 N NH2 . ARG A 153 ? 0.6217 0.5098 0.6353 0.0437  0.0057  -0.0593 690  ARG A NH2 
1039 N N   . ILE A 154 ? 0.3736 0.3225 0.3270 0.0142  -0.0043 -0.0041 691  ILE A N   
1040 C CA  . ILE A 154 ? 0.3411 0.2993 0.2890 0.0118  -0.0023 -0.0035 691  ILE A CA  
1041 C C   . ILE A 154 ? 0.3925 0.3396 0.3248 0.0080  -0.0079 0.0040  691  ILE A C   
1042 O O   . ILE A 154 ? 0.3950 0.3475 0.3255 0.0093  -0.0115 0.0044  691  ILE A O   
1043 C CB  . ILE A 154 ? 0.3162 0.2825 0.2646 0.0054  0.0060  -0.0085 691  ILE A CB  
1044 C CG1 . ILE A 154 ? 0.3410 0.3204 0.3036 0.0099  0.0068  -0.0144 691  ILE A CG1 
1045 C CG2 . ILE A 154 ? 0.3463 0.3176 0.2888 0.0026  0.0099  -0.0100 691  ILE A CG2 
1046 C CD1 . ILE A 154 ? 0.3416 0.3297 0.3119 0.0041  0.0115  -0.0195 691  ILE A CD1 
1047 N N   . LEU A 155 ? 0.3618 0.2918 0.2802 0.0016  -0.0094 0.0104  692  LEU A N   
1048 C CA  . LEU A 155 ? 0.3984 0.3152 0.2953 -0.0033 -0.0174 0.0200  692  LEU A CA  
1049 C C   . LEU A 155 ? 0.4521 0.3686 0.3594 0.0069  -0.0320 0.0249  692  LEU A C   
1050 O O   . LEU A 155 ? 0.4245 0.3403 0.3197 0.0047  -0.0412 0.0297  692  LEU A O   
1051 C CB  . LEU A 155 ? 0.4690 0.3630 0.3461 -0.0132 -0.0170 0.0289  692  LEU A CB  
1052 C CG  . LEU A 155 ? 0.4657 0.3640 0.3341 -0.0263 -0.0006 0.0232  692  LEU A CG  
1053 C CD1 . LEU A 155 ? 0.4888 0.3634 0.3370 -0.0394 0.0019  0.0328  692  LEU A CD1 
1054 C CD2 . LEU A 155 ? 0.4542 0.3641 0.3092 -0.0324 0.0066  0.0179  692  LEU A CD2 
1055 N N   . ASN A 156 ? 0.4090 0.3275 0.3401 0.0174  -0.0342 0.0222  693  ASN A N   
1056 C CA  . ASN A 156 ? 0.4067 0.3311 0.3569 0.0280  -0.0458 0.0241  693  ASN A CA  
1057 C C   . ASN A 156 ? 0.3540 0.3008 0.3141 0.0290  -0.0437 0.0177  693  ASN A C   
1058 O O   . ASN A 156 ? 0.4014 0.3545 0.3672 0.0309  -0.0549 0.0209  693  ASN A O   
1059 C CB  . ASN A 156 ? 0.3611 0.2839 0.3365 0.0387  -0.0444 0.0190  693  ASN A CB  
1060 C CG  . ASN A 156 ? 0.4908 0.4250 0.4941 0.0504  -0.0535 0.0181  693  ASN A CG  
1061 O OD1 . ASN A 156 ? 0.5437 0.4690 0.5504 0.0548  -0.0695 0.0278  693  ASN A OD1 
1062 N ND2 . ASN A 156 ? 0.4360 0.3912 0.4601 0.0549  -0.0440 0.0070  693  ASN A ND2 
1063 N N   . VAL A 157 ? 0.3685 0.3264 0.3311 0.0270  -0.0310 0.0095  694  VAL A N   
1064 C CA  . VAL A 157 ? 0.3425 0.3160 0.3118 0.0261  -0.0283 0.0049  694  VAL A CA  
1065 C C   . VAL A 157 ? 0.3868 0.3570 0.3376 0.0181  -0.0329 0.0070  694  VAL A C   
1066 O O   . VAL A 157 ? 0.3677 0.3460 0.3247 0.0173  -0.0393 0.0061  694  VAL A O   
1067 C CB  . VAL A 157 ? 0.3195 0.3000 0.2912 0.0256  -0.0162 -0.0014 694  VAL A CB  
1068 C CG1 . VAL A 157 ? 0.3259 0.3153 0.3004 0.0231  -0.0136 -0.0040 694  VAL A CG1 
1069 C CG2 . VAL A 157 ? 0.3118 0.2973 0.2978 0.0318  -0.0122 -0.0052 694  VAL A CG2 
1070 N N   . PHE A 158 ? 0.3595 0.3185 0.2873 0.0106  -0.0288 0.0083  695  PHE A N   
1071 C CA  . PHE A 158 ? 0.3520 0.3065 0.2569 0.0013  -0.0310 0.0079  695  PHE A CA  
1072 C C   . PHE A 158 ? 0.3707 0.3203 0.2676 0.0005  -0.0489 0.0161  695  PHE A C   
1073 O O   . PHE A 158 ? 0.4056 0.3592 0.2949 -0.0045 -0.0556 0.0135  695  PHE A O   
1074 C CB  . PHE A 158 ? 0.3400 0.2837 0.2204 -0.0083 -0.0215 0.0077  695  PHE A CB  
1075 C CG  . PHE A 158 ? 0.3957 0.3480 0.2858 -0.0088 -0.0055 -0.0022 695  PHE A CG  
1076 C CD1 . PHE A 158 ? 0.3961 0.3595 0.3045 -0.0033 -0.0017 -0.0096 695  PHE A CD1 
1077 C CD2 . PHE A 158 ? 0.4138 0.3624 0.2957 -0.0154 0.0050  -0.0033 695  PHE A CD2 
1078 C CE1 . PHE A 158 ? 0.3932 0.3635 0.3130 -0.0020 0.0096  -0.0172 695  PHE A CE1 
1079 C CE2 . PHE A 158 ? 0.3947 0.3549 0.2917 -0.0149 0.0177  -0.0128 695  PHE A CE2 
1080 C CZ  . PHE A 158 ? 0.3482 0.3190 0.2648 -0.0069 0.0187  -0.0194 695  PHE A CZ  
1081 N N   A ARG A 159 ? 0.3775 0.3172 0.2769 0.0055  -0.0584 0.0258  696  ARG A N   
1082 N N   B ARG A 159 ? 0.3771 0.3169 0.2766 0.0055  -0.0585 0.0258  696  ARG A N   
1083 C CA  A ARG A 159 ? 0.3820 0.3165 0.2774 0.0071  -0.0794 0.0359  696  ARG A CA  
1084 C CA  B ARG A 159 ? 0.3808 0.3154 0.2759 0.0069  -0.0794 0.0359  696  ARG A CA  
1085 C C   A ARG A 159 ? 0.3994 0.3552 0.3269 0.0143  -0.0881 0.0313  696  ARG A C   
1086 C C   B ARG A 159 ? 0.3981 0.3540 0.3257 0.0143  -0.0881 0.0312  696  ARG A C   
1087 O O   A ARG A 159 ? 0.4124 0.3732 0.3342 0.0100  -0.1025 0.0330  696  ARG A O   
1088 O O   B ARG A 159 ? 0.4141 0.3751 0.3361 0.0100  -0.1026 0.0329  696  ARG A O   
1089 C CB  A ARG A 159 ? 0.4112 0.3283 0.3101 0.0138  -0.0877 0.0473  696  ARG A CB  
1090 C CB  B ARG A 159 ? 0.4210 0.3378 0.3185 0.0133  -0.0882 0.0476  696  ARG A CB  
1091 C CG  A ARG A 159 ? 0.5362 0.4445 0.4318 0.0172  -0.1132 0.0608  696  ARG A CG  
1092 C CG  B ARG A 159 ? 0.5299 0.4384 0.4237 0.0165  -0.1140 0.0610  696  ARG A CG  
1093 C CD  A ARG A 159 ? 0.5823 0.4684 0.4850 0.0256  -0.1214 0.0723  696  ARG A CD  
1094 C CD  B ARG A 159 ? 0.6372 0.5357 0.5584 0.0309  -0.1234 0.0682  696  ARG A CD  
1095 N NE  A ARG A 159 ? 0.6180 0.5160 0.5657 0.0406  -0.1148 0.0630  696  ARG A NE  
1096 N NE  B ARG A 159 ? 0.6342 0.5504 0.5940 0.0412  -0.1084 0.0543  696  ARG A NE  
1097 C CZ  A ARG A 159 ? 0.6202 0.5022 0.5863 0.0515  -0.1200 0.0676  696  ARG A CZ  
1098 C CZ  B ARG A 159 ? 0.5183 0.4606 0.5143 0.0496  -0.1093 0.0454  696  ARG A CZ  
1099 N NH1 A ARG A 159 ? 0.6099 0.5050 0.6149 0.0637  -0.1108 0.0551  696  ARG A NH1 
1100 N NH1 B ARG A 159 ? 0.4253 0.3805 0.4469 0.0558  -0.0929 0.0332  696  ARG A NH1 
1101 N NH2 A ARG A 159 ? 0.4738 0.3244 0.4176 0.0492  -0.1338 0.0844  696  ARG A NH2 
1102 N NH2 B ARG A 159 ? 0.4965 0.4528 0.5018 0.0500  -0.1262 0.0482  696  ARG A NH2 
1103 N N   . HIS A 160 ? 0.3965 0.3658 0.3572 0.0237  -0.0789 0.0246  697  HIS A N   
1104 C CA  . HIS A 160 ? 0.3969 0.3889 0.3905 0.0283  -0.0827 0.0191  697  HIS A CA  
1105 C C   . HIS A 160 ? 0.4081 0.4084 0.3932 0.0180  -0.0787 0.0122  697  HIS A C   
1106 O O   . HIS A 160 ? 0.3663 0.3805 0.3664 0.0157  -0.0892 0.0102  697  HIS A O   
1107 C CB  . HIS A 160 ? 0.3602 0.3632 0.3827 0.0370  -0.0687 0.0121  697  HIS A CB  
1108 C CG  . HIS A 160 ? 0.3888 0.4164 0.4489 0.0414  -0.0702 0.0065  697  HIS A CG  
1109 N ND1 . HIS A 160 ? 0.3897 0.4269 0.4836 0.0530  -0.0771 0.0062  697  HIS A ND1 
1110 C CD2 . HIS A 160 ? 0.3627 0.4072 0.4347 0.0351  -0.0644 0.0003  697  HIS A CD2 
1111 C CE1 . HIS A 160 ? 0.4160 0.4792 0.5426 0.0531  -0.0741 -0.0009 697  HIS A CE1 
1112 N NE2 . HIS A 160 ? 0.3376 0.4044 0.4497 0.0412  -0.0664 -0.0038 697  HIS A NE2 
1113 N N   . TRP A 161 ? 0.3356 0.3271 0.2995 0.0117  -0.0643 0.0076  698  TRP A N   
1114 C CA  . TRP A 161 ? 0.3392 0.3340 0.2974 0.0032  -0.0589 -0.0004 698  TRP A CA  
1115 C C   . TRP A 161 ? 0.3784 0.3685 0.3142 -0.0066 -0.0724 -0.0006 698  TRP A C   
1116 O O   . TRP A 161 ? 0.3579 0.3573 0.3030 -0.0121 -0.0787 -0.0059 698  TRP A O   
1117 C CB  . TRP A 161 ? 0.3327 0.3185 0.2776 0.0014  -0.0420 -0.0052 698  TRP A CB  
1118 C CG  . TRP A 161 ? 0.3328 0.3185 0.2787 -0.0037 -0.0337 -0.0139 698  TRP A CG  
1119 C CD1 . TRP A 161 ? 0.3372 0.3276 0.2913 -0.0094 -0.0383 -0.0186 698  TRP A CD1 
1120 C CD2 . TRP A 161 ? 0.3455 0.3245 0.2873 -0.0032 -0.0201 -0.0190 698  TRP A CD2 
1121 N NE1 . TRP A 161 ? 0.3454 0.3283 0.2987 -0.0124 -0.0276 -0.0259 698  TRP A NE1 
1122 C CE2 . TRP A 161 ? 0.3642 0.3406 0.3113 -0.0074 -0.0171 -0.0260 698  TRP A CE2 
1123 C CE3 . TRP A 161 ? 0.3281 0.3040 0.2660 0.0005  -0.0113 -0.0186 698  TRP A CE3 
1124 C CZ2 . TRP A 161 ? 0.3603 0.3290 0.3097 -0.0057 -0.0062 -0.0318 698  TRP A CZ2 
1125 C CZ3 . TRP A 161 ? 0.3298 0.3029 0.2720 0.0017  -0.0011 -0.0249 698  TRP A CZ3 
1126 C CH2 . TRP A 161 ? 0.3485 0.3170 0.2969 -0.0002 0.0010  -0.0311 698  TRP A CH2 
1127 N N   . VAL A 162 ? 0.3673 0.3423 0.2712 -0.0109 -0.0773 0.0053  699  VAL A N   
1128 C CA  . VAL A 162 ? 0.4226 0.3915 0.2967 -0.0224 -0.0903 0.0050  699  VAL A CA  
1129 C C   . VAL A 162 ? 0.4636 0.4417 0.3507 -0.0196 -0.1157 0.0133  699  VAL A C   
1130 O O   . VAL A 162 ? 0.4468 0.4275 0.3202 -0.0291 -0.1298 0.0105  699  VAL A O   
1131 C CB  . VAL A 162 ? 0.4727 0.4216 0.3016 -0.0314 -0.0862 0.0089  699  VAL A CB  
1132 C CG1 . VAL A 162 ? 0.4383 0.3832 0.2595 -0.0353 -0.0613 -0.0030 699  VAL A CG1 
1133 C CG2 . VAL A 162 ? 0.4154 0.3533 0.2406 -0.0253 -0.0933 0.0246  699  VAL A CG2 
1134 N N   . GLU A 163 ? 0.4124 0.3962 0.3284 -0.0065 -0.1225 0.0220  700  GLU A N   
1135 C CA  . GLU A 163 ? 0.3865 0.3813 0.3232 -0.0010 -0.1481 0.0298  700  GLU A CA  
1136 C C   . GLU A 163 ? 0.3878 0.4102 0.3642 -0.0011 -0.1512 0.0198  700  GLU A C   
1137 O O   . GLU A 163 ? 0.4504 0.4846 0.4334 -0.0054 -0.1732 0.0208  700  GLU A O   
1138 C CB  . GLU A 163 ? 0.4074 0.3987 0.3684 0.0147  -0.1525 0.0397  700  GLU A CB  
1139 C CG  . GLU A 163 ? 0.5530 0.5567 0.5443 0.0240  -0.1806 0.0479  700  GLU A CG  
1140 C CD  . GLU A 163 ? 0.8167 0.8043 0.7683 0.0160  -0.2072 0.0613  700  GLU A CD  
1141 O OE1 . GLU A 163 ? 0.9510 0.9095 0.8614 0.0121  -0.2070 0.0727  700  GLU A OE1 
1142 O OE2 . GLU A 163 ? 0.9417 0.9456 0.9010 0.0115  -0.2283 0.0605  700  GLU A OE2 
1143 N N   . HIS A 164 ? 0.3911 0.4244 0.3940 0.0022  -0.1303 0.0109  701  HIS A N   
1144 C CA  . HIS A 164 ? 0.3989 0.4588 0.4444 0.0020  -0.1298 0.0030  701  HIS A CA  
1145 C C   . HIS A 164 ? 0.3860 0.4461 0.4248 -0.0108 -0.1161 -0.0079 701  HIS A C   
1146 O O   . HIS A 164 ? 0.3187 0.3986 0.3881 -0.0158 -0.1172 -0.0143 701  HIS A O   
1147 C CB  . HIS A 164 ? 0.3395 0.4123 0.4233 0.0150  -0.1167 0.0021  701  HIS A CB  
1148 C CG  . HIS A 164 ? 0.3444 0.4174 0.4452 0.0293  -0.1302 0.0104  701  HIS A CG  
1149 N ND1 . HIS A 164 ? 0.3458 0.4373 0.4792 0.0351  -0.1531 0.0135  701  HIS A ND1 
1150 C CD2 . HIS A 164 ? 0.3438 0.3997 0.4368 0.0393  -0.1251 0.0159  701  HIS A CD2 
1151 C CE1 . HIS A 164 ? 0.4046 0.4878 0.5494 0.0496  -0.1618 0.0214  701  HIS A CE1 
1152 N NE2 . HIS A 164 ? 0.3453 0.4056 0.4646 0.0515  -0.1443 0.0226  701  HIS A NE2 
1153 N N   . HIS A 165 ? 0.3398 0.3783 0.3428 -0.0164 -0.1032 -0.0108 702  HIS A N   
1154 C CA  . HIS A 165 ? 0.3137 0.3475 0.3127 -0.0264 -0.0903 -0.0211 702  HIS A CA  
1155 C C   . HIS A 165 ? 0.3631 0.3762 0.3199 -0.0357 -0.0894 -0.0267 702  HIS A C   
1156 O O   . HIS A 165 ? 0.4036 0.4029 0.3487 -0.0373 -0.0725 -0.0330 702  HIS A O   
1157 C CB  . HIS A 165 ? 0.2981 0.3295 0.3096 -0.0204 -0.0689 -0.0214 702  HIS A CB  
1158 C CG  . HIS A 165 ? 0.3184 0.3693 0.3654 -0.0124 -0.0661 -0.0178 702  HIS A CG  
1159 N ND1 . HIS A 165 ? 0.3762 0.4455 0.4546 -0.0178 -0.0637 -0.0218 702  HIS A ND1 
1160 C CD2 . HIS A 165 ? 0.3721 0.4273 0.4289 -0.0005 -0.0641 -0.0125 702  HIS A CD2 
1161 C CE1 . HIS A 165 ? 0.3664 0.4525 0.4723 -0.0092 -0.0587 -0.0198 702  HIS A CE1 
1162 N NE2 . HIS A 165 ? 0.3059 0.3827 0.3991 0.0019  -0.0592 -0.0147 702  HIS A NE2 
1163 N N   . PHE A 166 ? 0.3793 0.3899 0.3123 -0.0419 -0.1077 -0.0246 703  PHE A N   
1164 C CA  . PHE A 166 ? 0.4779 0.4688 0.3654 -0.0523 -0.1041 -0.0311 703  PHE A CA  
1165 C C   . PHE A 166 ? 0.5047 0.4901 0.3888 -0.0640 -0.0965 -0.0478 703  PHE A C   
1166 O O   . PHE A 166 ? 0.4906 0.4590 0.3447 -0.0703 -0.0843 -0.0578 703  PHE A O   
1167 C CB  . PHE A 166 ? 0.5340 0.5208 0.3887 -0.0589 -0.1266 -0.0238 703  PHE A CB  
1168 C CG  . PHE A 166 ? 0.6019 0.5673 0.4030 -0.0701 -0.1184 -0.0290 703  PHE A CG  
1169 C CD1 . PHE A 166 ? 0.5539 0.5068 0.3382 -0.0658 -0.1019 -0.0240 703  PHE A CD1 
1170 C CD2 . PHE A 166 ? 0.6069 0.5659 0.3755 -0.0865 -0.1252 -0.0411 703  PHE A CD2 
1171 C CE1 . PHE A 166 ? 0.5808 0.5171 0.3186 -0.0776 -0.0904 -0.0305 703  PHE A CE1 
1172 C CE2 . PHE A 166 ? 0.6750 0.6152 0.3925 -0.0982 -0.1138 -0.0485 703  PHE A CE2 
1173 C CZ  . PHE A 166 ? 0.6532 0.5831 0.3566 -0.0937 -0.0953 -0.0431 703  PHE A CZ  
1174 N N   . TYR A 167 ? 0.3966 0.3957 0.3134 -0.0674 -0.1016 -0.0521 704  TYR A N   
1175 C CA  . TYR A 167 ? 0.4093 0.3985 0.3253 -0.0789 -0.0935 -0.0679 704  TYR A CA  
1176 C C   . TYR A 167 ? 0.4290 0.3999 0.3437 -0.0733 -0.0689 -0.0730 704  TYR A C   
1177 O O   . TYR A 167 ? 0.4754 0.4297 0.3790 -0.0814 -0.0604 -0.0875 704  TYR A O   
1178 C CB  . TYR A 167 ? 0.4965 0.5035 0.4528 -0.0842 -0.1003 -0.0696 704  TYR A CB  
1179 C CG  . TYR A 167 ? 0.4720 0.4945 0.4662 -0.0721 -0.0922 -0.0583 704  TYR A CG  
1180 C CD1 . TYR A 167 ? 0.4183 0.4298 0.4217 -0.0671 -0.0714 -0.0573 704  TYR A CD1 
1181 C CD2 . TYR A 167 ? 0.3762 0.4239 0.3963 -0.0655 -0.1059 -0.0491 704  TYR A CD2 
1182 C CE1 . TYR A 167 ? 0.4011 0.4259 0.4320 -0.0583 -0.0634 -0.0479 704  TYR A CE1 
1183 C CE2 . TYR A 167 ? 0.4056 0.4676 0.4583 -0.0554 -0.0958 -0.0421 704  TYR A CE2 
1184 C CZ  . TYR A 167 ? 0.3425 0.3931 0.3975 -0.0530 -0.0741 -0.0417 704  TYR A CZ  
1185 O OH  . TYR A 167 ? 0.3508 0.4152 0.4319 -0.0451 -0.0637 -0.0355 704  TYR A OH  
1186 N N   . ASP A 168 ? 0.4063 0.3797 0.3340 -0.0595 -0.0583 -0.0622 705  ASP A N   
1187 C CA  . ASP A 168 ? 0.4845 0.4424 0.4116 -0.0534 -0.0389 -0.0661 705  ASP A CA  
1188 C C   . ASP A 168 ? 0.5226 0.4655 0.4170 -0.0576 -0.0316 -0.0776 705  ASP A C   
1189 O O   . ASP A 168 ? 0.4497 0.3777 0.3444 -0.0578 -0.0181 -0.0896 705  ASP A O   
1190 C CB  . ASP A 168 ? 0.3327 0.2968 0.2727 -0.0393 -0.0317 -0.0534 705  ASP A CB  
1191 C CG  . ASP A 168 ? 0.3926 0.3669 0.3632 -0.0353 -0.0302 -0.0454 705  ASP A CG  
1192 O OD1 . ASP A 168 ? 0.3524 0.3253 0.3373 -0.0429 -0.0301 -0.0492 705  ASP A OD1 
1193 O OD2 . ASP A 168 ? 0.3505 0.3335 0.3293 -0.0259 -0.0279 -0.0359 705  ASP A OD2 
1194 N N   . PHE A 169 ? 0.4629 0.4088 0.3292 -0.0612 -0.0398 -0.0741 706  PHE A N   
1195 C CA  . PHE A 169 ? 0.4590 0.3932 0.2887 -0.0676 -0.0309 -0.0834 706  PHE A CA  
1196 C C   . PHE A 169 ? 0.5709 0.4956 0.3730 -0.0837 -0.0357 -0.0999 706  PHE A C   
1197 O O   . PHE A 169 ? 0.5998 0.5118 0.3782 -0.0899 -0.0208 -0.1158 706  PHE A O   
1198 C CB  . PHE A 169 ? 0.4933 0.4313 0.3012 -0.0663 -0.0377 -0.0691 706  PHE A CB  
1199 C CG  . PHE A 169 ? 0.4637 0.4088 0.2964 -0.0520 -0.0321 -0.0559 706  PHE A CG  
1200 C CD1 . PHE A 169 ? 0.4988 0.4405 0.3346 -0.0467 -0.0134 -0.0595 706  PHE A CD1 
1201 C CD2 . PHE A 169 ? 0.4543 0.4113 0.3105 -0.0441 -0.0452 -0.0422 706  PHE A CD2 
1202 C CE1 . PHE A 169 ? 0.4648 0.4133 0.3222 -0.0352 -0.0099 -0.0489 706  PHE A CE1 
1203 C CE2 . PHE A 169 ? 0.4150 0.3770 0.2914 -0.0322 -0.0392 -0.0329 706  PHE A CE2 
1204 C CZ  . PHE A 169 ? 0.4655 0.4226 0.3403 -0.0285 -0.0225 -0.0360 706  PHE A CZ  
1205 N N   . GLU A 170 ? 0.5316 0.4639 0.3383 -0.0914 -0.0555 -0.0985 707  GLU A N   
1206 C CA  . GLU A 170 ? 0.5375 0.4609 0.3230 -0.1080 -0.0611 -0.1168 707  GLU A CA  
1207 C C   . GLU A 170 ? 0.5614 0.4709 0.3686 -0.1084 -0.0449 -0.1336 707  GLU A C   
1208 O O   . GLU A 170 ? 0.5920 0.4857 0.3774 -0.1200 -0.0385 -0.1547 707  GLU A O   
1209 C CB  . GLU A 170 ? 0.5706 0.5097 0.3640 -0.1160 -0.0885 -0.1108 707  GLU A CB  
1210 C CG  . GLU A 170 ? 0.5951 0.5467 0.3746 -0.1127 -0.1089 -0.0914 707  GLU A CG  
1211 C CD  . GLU A 170 ? 0.6863 0.6591 0.4894 -0.1160 -0.1371 -0.0845 707  GLU A CD  
1212 O OE1 . GLU A 170 ? 0.6507 0.6352 0.4963 -0.1156 -0.1363 -0.0886 707  GLU A OE1 
1213 O OE2 . GLU A 170 ? 0.7292 0.7071 0.5090 -0.1195 -0.1603 -0.0744 707  GLU A OE2 
1214 N N   . ARG A 171 ? 0.4822 0.3950 0.3305 -0.0967 -0.0389 -0.1248 708  ARG A N   
1215 C CA  . ARG A 171 ? 0.5180 0.4138 0.3882 -0.0970 -0.0268 -0.1366 708  ARG A CA  
1216 C C   . ARG A 171 ? 0.5550 0.4344 0.4239 -0.0872 -0.0052 -0.1457 708  ARG A C   
1217 O O   . ARG A 171 ? 0.6143 0.4733 0.4942 -0.0880 0.0051  -0.1603 708  ARG A O   
1218 C CB  . ARG A 171 ? 0.4951 0.3992 0.4053 -0.0906 -0.0294 -0.1216 708  ARG A CB  
1219 C CG  . ARG A 171 ? 0.4945 0.4153 0.4184 -0.1025 -0.0474 -0.1185 708  ARG A CG  
1220 C CD  . ARG A 171 ? 0.5108 0.4458 0.4718 -0.0957 -0.0465 -0.1019 708  ARG A CD  
1221 N NE  . ARG A 171 ? 0.5305 0.4901 0.5103 -0.1051 -0.0631 -0.0987 708  ARG A NE  
1222 C CZ  . ARG A 171 ? 0.5057 0.4846 0.5187 -0.1022 -0.0629 -0.0869 708  ARG A CZ  
1223 N NH1 . ARG A 171 ? 0.4556 0.4293 0.4796 -0.0915 -0.0479 -0.0763 708  ARG A NH1 
1224 N NH2 . ARG A 171 ? 0.5719 0.5767 0.6072 -0.1106 -0.0778 -0.0867 708  ARG A NH2 
1225 N N   . ASP A 172 ? 0.4784 0.3663 0.3373 -0.0779 0.0015  -0.1380 709  ASP A N   
1226 C CA  . ASP A 172 ? 0.5411 0.4208 0.4075 -0.0670 0.0214  -0.1454 709  ASP A CA  
1227 C C   . ASP A 172 ? 0.5544 0.4414 0.3881 -0.0706 0.0279  -0.1478 709  ASP A C   
1228 O O   . ASP A 172 ? 0.5247 0.4248 0.3593 -0.0639 0.0258  -0.1315 709  ASP A O   
1229 C CB  . ASP A 172 ? 0.4379 0.3231 0.3393 -0.0506 0.0233  -0.1284 709  ASP A CB  
1230 C CG  . ASP A 172 ? 0.5481 0.4277 0.4655 -0.0380 0.0402  -0.1355 709  ASP A CG  
1231 O OD1 . ASP A 172 ? 0.5980 0.4706 0.5029 -0.0415 0.0536  -0.1553 709  ASP A OD1 
1232 O OD2 . ASP A 172 ? 0.5271 0.4104 0.4705 -0.0249 0.0399  -0.1221 709  ASP A OD2 
1233 N N   . LEU A 173 ? 0.5699 0.4465 0.3729 -0.0827 0.0371  -0.1691 710  LEU A N   
1234 C CA  . LEU A 173 ? 0.5794 0.4610 0.3445 -0.0902 0.0453  -0.1715 710  LEU A CA  
1235 C C   . LEU A 173 ? 0.5904 0.4804 0.3759 -0.0774 0.0633  -0.1683 710  LEU A C   
1236 O O   . LEU A 173 ? 0.5983 0.4973 0.3635 -0.0806 0.0653  -0.1582 710  LEU A O   
1237 C CB  . LEU A 173 ? 0.6328 0.5008 0.3601 -0.1065 0.0564  -0.1983 710  LEU A CB  
1238 C CG  . LEU A 173 ? 0.7894 0.6494 0.4883 -0.1235 0.0377  -0.2053 710  LEU A CG  
1239 C CD1 . LEU A 173 ? 0.8411 0.6961 0.5088 -0.1336 0.0475  -0.2204 710  LEU A CD1 
1240 C CD2 . LEU A 173 ? 0.8881 0.7613 0.5713 -0.1278 0.0101  -0.1801 710  LEU A CD2 
1241 N N   . GLU A 174 ? 0.5742 0.4609 0.4009 -0.0634 0.0751  -0.1762 711  GLU A N   
1242 C CA  . GLU A 174 ? 0.6261 0.5248 0.4790 -0.0506 0.0890  -0.1733 711  GLU A CA  
1243 C C   . GLU A 174 ? 0.5000 0.4131 0.3631 -0.0433 0.0759  -0.1467 711  GLU A C   
1244 O O   . GLU A 174 ? 0.5111 0.4365 0.3763 -0.0409 0.0841  -0.1418 711  GLU A O   
1245 C CB  . GLU A 174 ? 0.6555 0.5470 0.5541 -0.0351 0.0984  -0.1842 711  GLU A CB  
1246 C CG  . GLU A 174 ? 0.8033 0.7100 0.7322 -0.0227 0.1137  -0.1871 711  GLU A CG  
1247 C CD  . GLU A 174 ? 0.9154 0.8166 0.8954 -0.0033 0.1140  -0.1886 711  GLU A CD  
1248 O OE1 . GLU A 174 ? 1.0170 0.8973 1.0057 -0.0010 0.1072  -0.1913 711  GLU A OE1 
1249 O OE2 . GLU A 174 ? 0.9012 0.8183 0.9129 0.0090  0.1197  -0.1862 711  GLU A OE2 
1250 N N   . LEU A 175 ? 0.4503 0.3624 0.3208 -0.0408 0.0569  -0.1309 712  LEU A N   
1251 C CA  . LEU A 175 ? 0.4143 0.3389 0.2937 -0.0342 0.0458  -0.1087 712  LEU A CA  
1252 C C   . LEU A 175 ? 0.5090 0.4390 0.3551 -0.0436 0.0424  -0.1007 712  LEU A C   
1253 O O   . LEU A 175 ? 0.4671 0.4058 0.3186 -0.0391 0.0443  -0.0900 712  LEU A O   
1254 C CB  . LEU A 175 ? 0.3804 0.3042 0.2722 -0.0324 0.0290  -0.0969 712  LEU A CB  
1255 C CG  . LEU A 175 ? 0.3888 0.3246 0.2956 -0.0240 0.0201  -0.0774 712  LEU A CG  
1256 C CD1 . LEU A 175 ? 0.4409 0.3787 0.3761 -0.0110 0.0275  -0.0745 712  LEU A CD1 
1257 C CD2 . LEU A 175 ? 0.4063 0.3446 0.3207 -0.0264 0.0057  -0.0690 712  LEU A CD2 
1258 N N   . LEU A 176 ? 0.5229 0.4458 0.3329 -0.0577 0.0359  -0.1052 713  LEU A N   
1259 C CA  . LEU A 176 ? 0.5511 0.4740 0.3236 -0.0678 0.0307  -0.0955 713  LEU A CA  
1260 C C   . LEU A 176 ? 0.5233 0.4467 0.2804 -0.0735 0.0526  -0.1040 713  LEU A C   
1261 O O   . LEU A 176 ? 0.5501 0.4761 0.2965 -0.0756 0.0533  -0.0911 713  LEU A O   
1262 C CB  . LEU A 176 ? 0.4974 0.4121 0.2316 -0.0826 0.0165  -0.0985 713  LEU A CB  
1263 C CG  . LEU A 176 ? 0.6088 0.5191 0.2994 -0.0936 0.0051  -0.0843 713  LEU A CG  
1264 C CD1 . LEU A 176 ? 0.6167 0.5334 0.3277 -0.0824 -0.0095 -0.0608 713  LEU A CD1 
1265 C CD2 . LEU A 176 ? 0.7003 0.6039 0.3554 -0.1077 -0.0135 -0.0875 713  LEU A CD2 
1266 N N   . GLU A 177 ? 0.5873 0.5078 0.3448 -0.0768 0.0720  -0.1267 714  GLU A N   
1267 C CA  . GLU A 177 ? 0.5805 0.5061 0.3301 -0.0824 0.0965  -0.1376 714  GLU A CA  
1268 C C   . GLU A 177 ? 0.5539 0.4943 0.3429 -0.0697 0.1017  -0.1278 714  GLU A C   
1269 O O   . GLU A 177 ? 0.8588 0.8047 0.6354 -0.0769 0.1110  -0.1224 714  GLU A O   
1270 C CB  . GLU A 177 ? 0.6119 0.5343 0.3679 -0.0841 0.1180  -0.1669 714  GLU A CB  
1271 C CG  . GLU A 177 ? 0.8523 0.7622 0.5607 -0.1018 0.1181  -0.1784 714  GLU A CG  
1272 C CD  . GLU A 177 ? 1.0164 0.9229 0.7457 -0.0982 0.1325  -0.2023 714  GLU A CD  
1273 O OE1 . GLU A 177 ? 1.1002 0.9994 0.7977 -0.1111 0.1340  -0.2115 714  GLU A OE1 
1274 O OE2 . GLU A 177 ? 1.0941 1.0041 0.8720 -0.0821 0.1412  -0.2114 714  GLU A OE2 
1275 N N   . ARG A 178 ? 0.5116 0.4574 0.3458 -0.0523 0.0949  -0.1248 715  ARG A N   
1276 C CA  . ARG A 178 ? 0.4558 0.4159 0.3247 -0.0410 0.0961  -0.1151 715  ARG A CA  
1277 C C   . ARG A 178 ? 0.4516 0.4120 0.3035 -0.0449 0.0832  -0.0938 715  ARG A C   
1278 O O   . ARG A 178 ? 0.4554 0.4245 0.3130 -0.0469 0.0906  -0.0895 715  ARG A O   
1279 C CB  . ARG A 178 ? 0.3746 0.3365 0.2852 -0.0236 0.0869  -0.1122 715  ARG A CB  
1280 C CG  . ARG A 178 ? 0.4384 0.3985 0.3777 -0.0152 0.0990  -0.1312 715  ARG A CG  
1281 C CD  . ARG A 178 ? 0.4374 0.3959 0.4129 0.0010  0.0866  -0.1219 715  ARG A CD  
1282 N NE  . ARG A 178 ? 0.4225 0.3973 0.4210 0.0095  0.0827  -0.1102 715  ARG A NE  
1283 C CZ  . ARG A 178 ? 0.4781 0.4535 0.4921 0.0190  0.0677  -0.0947 715  ARG A CZ  
1284 N NH1 . ARG A 178 ? 0.4409 0.4018 0.4518 0.0212  0.0568  -0.0875 715  ARG A NH1 
1285 N NH2 . ARG A 178 ? 0.3658 0.3564 0.3969 0.0244  0.0644  -0.0869 715  ARG A NH2 
1286 N N   . LEU A 179 ? 0.4498 0.4009 0.2844 -0.0461 0.0639  -0.0813 716  LEU A N   
1287 C CA  . LEU A 179 ? 0.4519 0.4015 0.2776 -0.0463 0.0504  -0.0618 716  LEU A CA  
1288 C C   . LEU A 179 ? 0.4407 0.3824 0.2275 -0.0618 0.0561  -0.0574 716  LEU A C   
1289 O O   . LEU A 179 ? 0.5305 0.4726 0.3186 -0.0631 0.0574  -0.0470 716  LEU A O   
1290 C CB  . LEU A 179 ? 0.4178 0.3624 0.2404 -0.0430 0.0289  -0.0515 716  LEU A CB  
1291 C CG  . LEU A 179 ? 0.5201 0.4609 0.3339 -0.0425 0.0142  -0.0329 716  LEU A CG  
1292 C CD1 . LEU A 179 ? 0.4612 0.4092 0.3033 -0.0326 0.0172  -0.0270 716  LEU A CD1 
1293 C CD2 . LEU A 179 ? 0.5172 0.4572 0.3329 -0.0393 -0.0063 -0.0255 716  LEU A CD2 
1294 N N   . GLU A 180 ? 0.4851 0.4176 0.2339 -0.0754 0.0598  -0.0652 717  GLU A N   
1295 C CA  . GLU A 180 ? 0.5870 0.5088 0.2905 -0.0929 0.0656  -0.0592 717  GLU A CA  
1296 C C   . GLU A 180 ? 0.6693 0.6008 0.3826 -0.0986 0.0918  -0.0682 717  GLU A C   
1297 O O   . GLU A 180 ? 0.6381 0.5639 0.3343 -0.1083 0.0954  -0.0564 717  GLU A O   
1298 C CB  . GLU A 180 ? 0.6222 0.5326 0.2783 -0.1080 0.0647  -0.0677 717  GLU A CB  
1299 C CG  . GLU A 180 ? 0.6253 0.5289 0.2728 -0.1046 0.0359  -0.0578 717  GLU A CG  
1300 C CD  . GLU A 180 ? 0.7853 0.6771 0.3804 -0.1220 0.0308  -0.0649 717  GLU A CD  
1301 O OE1 . GLU A 180 ? 0.9049 0.7970 0.4871 -0.1306 0.0510  -0.0875 717  GLU A OE1 
1302 O OE2 . GLU A 180 ? 0.9180 0.8005 0.4855 -0.1268 0.0058  -0.0486 717  GLU A OE2 
1303 N N   . SER A 181 ? 0.6055 0.5514 0.3495 -0.0927 0.1100  -0.0892 718  SER A N   
1304 C CA  . SER A 181 ? 0.6182 0.5800 0.3842 -0.0959 0.1344  -0.0996 718  SER A CA  
1305 C C   . SER A 181 ? 0.5350 0.5057 0.3338 -0.0874 0.1271  -0.0855 718  SER A C   
1306 O O   . SER A 181 ? 0.5539 0.5293 0.3501 -0.0982 0.1396  -0.0827 718  SER A O   
1307 C CB  . SER A 181 ? 0.6298 0.6063 0.4335 -0.0861 0.1508  -0.1245 718  SER A CB  
1308 O OG  . SER A 181 ? 0.6625 0.6603 0.5004 -0.0860 0.1720  -0.1351 718  SER A OG  
1309 N N   . PHE A 182 ? 0.5225 0.4948 0.3496 -0.0702 0.1077  -0.0769 719  PHE A N   
1310 C CA  . PHE A 182 ? 0.5139 0.4945 0.3696 -0.0630 0.1015  -0.0666 719  PHE A CA  
1311 C C   . PHE A 182 ? 0.5648 0.5293 0.3903 -0.0739 0.0939  -0.0486 719  PHE A C   
1312 O O   . PHE A 182 ? 0.5263 0.4950 0.3603 -0.0804 0.1016  -0.0456 719  PHE A O   
1313 C CB  . PHE A 182 ? 0.4534 0.4375 0.3391 -0.0445 0.0839  -0.0614 719  PHE A CB  
1314 C CG  . PHE A 182 ? 0.5114 0.5024 0.4197 -0.0391 0.0771  -0.0524 719  PHE A CG  
1315 C CD1 . PHE A 182 ? 0.4824 0.4929 0.4244 -0.0367 0.0867  -0.0607 719  PHE A CD1 
1316 C CD2 . PHE A 182 ? 0.5106 0.4891 0.4073 -0.0374 0.0615  -0.0374 719  PHE A CD2 
1317 C CE1 . PHE A 182 ? 0.4369 0.4534 0.3965 -0.0341 0.0795  -0.0541 719  PHE A CE1 
1318 C CE2 . PHE A 182 ? 0.4762 0.4588 0.3908 -0.0339 0.0568  -0.0322 719  PHE A CE2 
1319 C CZ  . PHE A 182 ? 0.4864 0.4875 0.4300 -0.0333 0.0653  -0.0405 719  PHE A CZ  
1320 N N   . ILE A 183 ? 0.5423 0.4876 0.3350 -0.0759 0.0773  -0.0363 720  ILE A N   
1321 C CA  . ILE A 183 ? 0.6347 0.5612 0.4028 -0.0832 0.0668  -0.0174 720  ILE A CA  
1322 C C   . ILE A 183 ? 0.6174 0.5340 0.3495 -0.1049 0.0834  -0.0156 720  ILE A C   
1323 O O   . ILE A 183 ? 0.6337 0.5362 0.3549 -0.1128 0.0814  -0.0018 720  ILE A O   
1324 C CB  . ILE A 183 ? 0.5778 0.4883 0.3254 -0.0783 0.0425  -0.0041 720  ILE A CB  
1325 C CG1 . ILE A 183 ? 0.6996 0.6025 0.4072 -0.0894 0.0420  -0.0082 720  ILE A CG1 
1326 C CG2 . ILE A 183 ? 0.5388 0.4609 0.3246 -0.0589 0.0294  -0.0058 720  ILE A CG2 
1327 C CD1 . ILE A 183 ? 0.7291 0.6219 0.4232 -0.0844 0.0154  0.0033  720  ILE A CD1 
1328 N N   A SER A 184 ? 0.5994 0.5216 0.3119 -0.1161 0.1013  -0.0301 721  SER A N   
1329 N N   B SER A 184 ? 0.6005 0.5227 0.3130 -0.1161 0.1014  -0.0301 721  SER A N   
1330 C CA  A SER A 184 ? 0.6246 0.5414 0.3042 -0.1390 0.1229  -0.0314 721  SER A CA  
1331 C CA  B SER A 184 ? 0.6243 0.5405 0.3034 -0.1391 0.1225  -0.0308 721  SER A CA  
1332 C C   A SER A 184 ? 0.6302 0.5650 0.3472 -0.1421 0.1416  -0.0377 721  SER A C   
1333 C C   B SER A 184 ? 0.6296 0.5653 0.3467 -0.1424 0.1427  -0.0387 721  SER A C   
1334 O O   A SER A 184 ? 0.6803 0.6076 0.3741 -0.1623 0.1565  -0.0326 721  SER A O   
1335 O O   B SER A 184 ? 0.6901 0.6202 0.3842 -0.1631 0.1599  -0.0357 721  SER A O   
1336 C CB  A SER A 184 ? 0.6937 0.6162 0.3486 -0.1496 0.1419  -0.0509 721  SER A CB  
1337 C CB  B SER A 184 ? 0.6931 0.6122 0.3418 -0.1508 0.1397  -0.0483 721  SER A CB  
1338 O OG  A SER A 184 ? 0.7189 0.6695 0.4191 -0.1442 0.1653  -0.0745 721  SER A OG  
1339 O OG  B SER A 184 ? 0.7790 0.6787 0.3851 -0.1527 0.1198  -0.0401 721  SER A OG  
1340 N N   . SER A 185 ? 0.6537 0.6119 0.4269 -0.1241 0.1401  -0.0480 722  SER A N   
1341 C CA  . SER A 185 ? 0.6977 0.6778 0.5128 -0.1256 0.1538  -0.0553 722  SER A CA  
1342 C C   . SER A 185 ? 0.6599 0.6294 0.4846 -0.1240 0.1387  -0.0390 722  SER A C   
1343 O O   . SER A 185 ? 0.6145 0.5985 0.4673 -0.1302 0.1488  -0.0432 722  SER A O   
1344 C CB  . SER A 185 ? 0.6163 0.6257 0.4866 -0.1065 0.1557  -0.0730 722  SER A CB  
1345 O OG  . SER A 185 ? 0.6043 0.6115 0.4959 -0.0878 0.1317  -0.0639 722  SER A OG  
1346 N N   . VAL A 186 ? 0.5413 0.4875 0.3474 -0.1156 0.1152  -0.0225 723  VAL A N   
1347 C CA  . VAL A 186 ? 0.5622 0.4969 0.3806 -0.1117 0.1013  -0.0103 723  VAL A CA  
1348 C C   . VAL A 186 ? 0.7471 0.6607 0.5376 -0.1338 0.1103  0.0011  723  VAL A C   
1349 O O   . VAL A 186 ? 0.7435 0.6321 0.4865 -0.1463 0.1094  0.0136  723  VAL A O   
1350 C CB  . VAL A 186 ? 0.5665 0.4837 0.3768 -0.0960 0.0761  0.0019  723  VAL A CB  
1351 C CG1 . VAL A 186 ? 0.6238 0.5227 0.4401 -0.0939 0.0639  0.0140  723  VAL A CG1 
1352 C CG2 . VAL A 186 ? 0.5228 0.4611 0.3647 -0.0763 0.0691  -0.0088 723  VAL A CG2 
1353 N N   . ARG A 187 ? 0.7051 0.6278 0.5236 -0.1404 0.1182  -0.0026 724  ARG A N   
1354 C CA  . ARG A 187 ? 0.7990 0.7008 0.5959 -0.1635 0.1282  0.0078  724  ARG A CA  
1355 C C   . ARG A 187 ? 0.8109 0.6837 0.6080 -0.1588 0.1089  0.0226  724  ARG A C   
1356 O O   . ARG A 187 ? 0.8235 0.7028 0.6491 -0.1394 0.0934  0.0188  724  ARG A O   
1357 C CB  . ARG A 187 ? 0.8426 0.7745 0.6732 -0.1778 0.1520  -0.0079 724  ARG A CB  
1358 C CG  . ARG A 187 ? 0.9579 0.9169 0.7896 -0.1858 0.1766  -0.0242 724  ARG A CG  
1359 C CD  . ARG A 187 ? 1.1636 1.0979 0.9355 -0.2099 0.1917  -0.0143 724  ARG A CD  
1360 N NE  . ARG A 187 ? 1.2879 1.1979 1.0145 -0.2017 0.1754  -0.0035 724  ARG A NE  
1361 C CZ  . ARG A 187 ? 1.2434 1.1643 0.9544 -0.1995 0.1836  -0.0153 724  ARG A CZ  
1362 N NH1 . ARG A 187 ? 1.1644 1.1189 0.9046 -0.2018 0.2074  -0.0387 724  ARG A NH1 
1363 N NH2 . ARG A 187 ? 1.2349 1.1336 0.9057 -0.1935 0.1655  -0.0049 724  ARG A NH2 
1364 N N   . GLY A 188 ? 0.9408 0.7792 0.7043 -0.1776 0.1111  0.0392  725  GLY A N   
1365 C CA  . GLY A 188 ? 0.9792 0.7859 0.7455 -0.1752 0.0957  0.0518  725  GLY A CA  
1366 C C   . GLY A 188 ? 0.9793 0.7431 0.7053 -0.1710 0.0758  0.0750  725  GLY A C   
1367 O O   . GLY A 188 ? 0.8214 0.5883 0.5401 -0.1540 0.0609  0.0772  725  GLY A O   
1368 N N   . LYS A 189 ? 0.7977 0.7109 0.8828 -0.0966 -0.0521 0.0929  726  LYS A N   
1369 C CA  . LYS A 189 ? 0.9298 0.8337 1.0682 -0.1068 -0.0740 0.1248  726  LYS A CA  
1370 C C   . LYS A 189 ? 0.7780 0.6427 0.9438 -0.0833 -0.0707 0.0914  726  LYS A C   
1371 O O   . LYS A 189 ? 0.8958 0.7552 1.0757 -0.0855 -0.0788 0.1059  726  LYS A O   
1372 C CB  . LYS A 189 ? 1.0209 0.9241 1.2384 -0.1269 -0.1042 0.1633  726  LYS A CB  
1373 C CG  . LYS A 189 ? 1.0795 1.0345 1.2875 -0.1620 -0.1188 0.2203  726  LYS A CG  
1374 C CD  . LYS A 189 ? 1.1337 1.0825 1.4328 -0.1824 -0.1535 0.2618  726  LYS A CD  
1375 C CE  . LYS A 189 ? 1.1846 1.1879 1.4943 -0.2234 -0.1777 0.3336  726  LYS A CE  
1376 N NZ  . LYS A 189 ? 1.2133 1.2823 1.4574 -0.2439 -0.1648 0.3466  726  LYS A NZ  
1377 N N   . ALA A 190 ? 0.6432 0.4872 0.8185 -0.0624 -0.0595 0.0465  727  ALA A N   
1378 C CA  . ALA A 190 ? 0.7203 0.5419 0.9254 -0.0424 -0.0563 0.0107  727  ALA A CA  
1379 C C   . ALA A 190 ? 0.7602 0.5854 0.9045 -0.0340 -0.0388 0.0006  727  ALA A C   
1380 O O   . ALA A 190 ? 0.8143 0.6279 0.9840 -0.0243 -0.0407 -0.0144 727  ALA A O   
1381 C CB  . ALA A 190 ? 0.7697 0.5863 0.9878 -0.0249 -0.0453 -0.0372 727  ALA A CB  
1382 N N   . MET A 191 ? 0.6372 0.4802 0.7078 -0.0374 -0.0236 0.0062  728  MET A N   
1383 C CA  . MET A 191 ? 0.6821 0.5272 0.7006 -0.0287 -0.0090 -0.0055 728  MET A CA  
1384 C C   . MET A 191 ? 0.7273 0.5903 0.7205 -0.0428 -0.0138 0.0268  728  MET A C   
1385 O O   . MET A 191 ? 0.5909 0.4550 0.5481 -0.0364 -0.0047 0.0189  728  MET A O   
1386 C CB  . MET A 191 ? 0.5387 0.3906 0.5025 -0.0184 0.0099  -0.0325 728  MET A CB  
1387 C CG  . MET A 191 ? 0.7385 0.5825 0.7263 -0.0069 0.0146  -0.0633 728  MET A CG  
1388 S SD  . MET A 191 ? 0.7911 0.6412 0.7278 0.0072  0.0336  -0.0950 728  MET A SD  
1389 C CE  . MET A 191 ? 0.8958 0.7565 0.7949 0.0034  0.0391  -0.0939 728  MET A CE  
1390 N N   . LYS A 192 ? 0.7228 0.6049 0.7376 -0.0637 -0.0295 0.0643  729  LYS A N   
1391 C CA  . LYS A 192 ? 0.7671 0.6817 0.7559 -0.0804 -0.0337 0.0944  729  LYS A CA  
1392 C C   . LYS A 192 ? 0.6961 0.5955 0.7039 -0.0779 -0.0405 0.1035  729  LYS A C   
1393 O O   . LYS A 192 ? 0.6998 0.6181 0.6697 -0.0801 -0.0345 0.1071  729  LYS A O   
1394 C CB  . LYS A 192 ? 0.7970 0.7468 0.8086 -0.1082 -0.0514 0.1380  729  LYS A CB  
1395 C CG  . LYS A 192 ? 1.0440 1.0247 1.0195 -0.1134 -0.0413 0.1288  729  LYS A CG  
1396 C CD  . LYS A 192 ? 1.2105 1.2327 1.2108 -0.1438 -0.0596 0.1740  729  LYS A CD  
1397 C CE  . LYS A 192 ? 1.2265 1.2797 1.1922 -0.1471 -0.0482 0.1588  729  LYS A CE  
1398 N NZ  . LYS A 192 ? 1.2515 1.3550 1.2390 -0.1802 -0.0661 0.2054  729  LYS A NZ  
1399 N N   . LYS A 193 ? 0.6369 0.5047 0.7077 -0.0723 -0.0538 0.1035  730  LYS A N   
1400 C CA  . LYS A 193 ? 0.6108 0.4650 0.7045 -0.0696 -0.0614 0.1105  730  LYS A CA  
1401 C C   . LYS A 193 ? 0.6066 0.4500 0.6552 -0.0498 -0.0406 0.0748  730  LYS A C   
1402 O O   . LYS A 193 ? 0.5400 0.3864 0.5737 -0.0507 -0.0403 0.0834  730  LYS A O   
1403 C CB  . LYS A 193 ? 0.6754 0.5014 0.8581 -0.0666 -0.0827 0.1114  730  LYS A CB  
1404 C CG  . LYS A 193 ? 0.8016 0.6077 1.0126 -0.0473 -0.0757 0.0659  730  LYS A CG  
1405 C CD  . LYS A 193 ? 0.8380 0.6234 1.1540 -0.0459 -0.1024 0.0644  730  LYS A CD  
1406 C CE  . LYS A 193 ? 0.8890 0.6724 1.2517 -0.0522 -0.1156 0.0687  730  LYS A CE  
1407 N NZ  . LYS A 193 ? 1.0151 0.8008 1.3476 -0.0352 -0.0929 0.0207  730  LYS A NZ  
1408 N N   . TRP A 194 ? 0.5298 0.3645 0.5569 -0.0341 -0.0245 0.0380  731  TRP A N   
1409 C CA  . TRP A 194 ? 0.5396 0.3703 0.5236 -0.0198 -0.0076 0.0115  731  TRP A CA  
1410 C C   . TRP A 194 ? 0.6616 0.5118 0.5874 -0.0246 0.0002  0.0198  731  TRP A C   
1411 O O   . TRP A 194 ? 0.5321 0.3819 0.4366 -0.0208 0.0041  0.0178  731  TRP A O   
1412 C CB  . TRP A 194 ? 0.5949 0.4212 0.5715 -0.0064 0.0047  -0.0235 731  TRP A CB  
1413 C CG  . TRP A 194 ? 0.6417 0.4600 0.6709 0.0031  0.0016  -0.0484 731  TRP A CG  
1414 C CD1 . TRP A 194 ? 0.5853 0.4006 0.6687 0.0042  -0.0070 -0.0598 731  TRP A CD1 
1415 C CD2 . TRP A 194 ? 0.5957 0.4163 0.6323 0.0127  0.0068  -0.0704 731  TRP A CD2 
1416 N NE1 . TRP A 194 ? 0.6539 0.4725 0.7815 0.0152  -0.0075 -0.0927 731  TRP A NE1 
1417 C CE2 . TRP A 194 ? 0.5875 0.4125 0.6844 0.0197  0.0018  -0.0992 731  TRP A CE2 
1418 C CE3 . TRP A 194 ? 0.7078 0.5316 0.7092 0.0152  0.0142  -0.0699 731  TRP A CE3 
1419 C CZ2 . TRP A 194 ? 0.7155 0.5555 0.8367 0.0285  0.0052  -0.1301 731  TRP A CZ2 
1420 C CZ3 . TRP A 194 ? 0.7765 0.6108 0.7987 0.0227  0.0174  -0.0944 731  TRP A CZ3 
1421 C CH2 . TRP A 194 ? 0.7232 0.5693 0.8036 0.0289  0.0137  -0.1255 731  TRP A CH2 
1422 N N   . VAL A 195 ? 0.5175 0.3884 0.4217 -0.0326 0.0019  0.0250  732  VAL A N   
1423 C CA  . VAL A 195 ? 0.5892 0.4879 0.4483 -0.0365 0.0077  0.0242  732  VAL A CA  
1424 C C   . VAL A 195 ? 0.6195 0.5396 0.4794 -0.0490 -0.0004 0.0489  732  VAL A C   
1425 O O   . VAL A 195 ? 0.6147 0.5446 0.4482 -0.0449 0.0043  0.0396  732  VAL A O   
1426 C CB  . VAL A 195 ? 0.5578 0.4849 0.4023 -0.0452 0.0091  0.0241  732  VAL A CB  
1427 C CG1 . VAL A 195 ? 0.5488 0.5193 0.3589 -0.0519 0.0119  0.0202  732  VAL A CG1 
1428 C CG2 . VAL A 195 ? 0.5363 0.4437 0.3724 -0.0310 0.0186  -0.0041 732  VAL A CG2 
1429 N N   . GLU A 196 ? 0.5323 0.4611 0.4275 -0.0652 -0.0151 0.0822  733  GLU A N   
1430 C CA  . GLU A 196 ? 0.5591 0.5157 0.4564 -0.0808 -0.0247 0.1112  733  GLU A CA  
1431 C C   . GLU A 196 ? 0.5616 0.4877 0.4701 -0.0694 -0.0251 0.1064  733  GLU A C   
1432 O O   . GLU A 196 ? 0.6175 0.5646 0.5101 -0.0752 -0.0262 0.1160  733  GLU A O   
1433 C CB  . GLU A 196 ? 0.6634 0.6414 0.6013 -0.1052 -0.0449 0.1557  733  GLU A CB  
1434 C CG  . GLU A 196 ? 0.8380 0.8664 0.7546 -0.1223 -0.0440 0.1649  733  GLU A CG  
1435 C CD  . GLU A 196 ? 1.0583 1.1132 1.0176 -0.1507 -0.0667 0.2153  733  GLU A CD  
1436 O OE1 . GLU A 196 ? 1.0955 1.1124 1.1143 -0.1516 -0.0845 0.2360  733  GLU A OE1 
1437 O OE2 . GLU A 196 ? 1.0782 1.1966 1.0166 -0.1733 -0.0686 0.2337  733  GLU A OE2 
1438 N N   . SER A 197 ? 0.5705 0.4544 0.5054 -0.0535 -0.0233 0.0880  734  SER A N   
1439 C CA  . SER A 197 ? 0.5926 0.4539 0.5348 -0.0423 -0.0215 0.0781  734  SER A CA  
1440 C C   . SER A 197 ? 0.5611 0.4247 0.4538 -0.0311 -0.0065 0.0546  734  SER A C   
1441 O O   . SER A 197 ? 0.5794 0.4437 0.4633 -0.0299 -0.0067 0.0578  734  SER A O   
1442 C CB  . SER A 197 ? 0.6233 0.4542 0.6095 -0.0297 -0.0231 0.0582  734  SER A CB  
1443 O OG  . SER A 197 ? 0.7927 0.6104 0.7817 -0.0189 -0.0190 0.0433  734  SER A OG  
1444 N N   . ILE A 198 ? 0.5715 0.4359 0.4370 -0.0235 0.0039  0.0324  735  ILE A N   
1445 C CA  . ILE A 198 ? 0.5242 0.3902 0.3542 -0.0144 0.0123  0.0133  735  ILE A CA  
1446 C C   . ILE A 198 ? 0.5379 0.4368 0.3478 -0.0229 0.0096  0.0201  735  ILE A C   
1447 O O   . ILE A 198 ? 0.5665 0.4661 0.3657 -0.0186 0.0100  0.0141  735  ILE A O   
1448 C CB  . ILE A 198 ? 0.5002 0.3618 0.3142 -0.0064 0.0196  -0.0084 735  ILE A CB  
1449 C CG1 . ILE A 198 ? 0.5001 0.3408 0.3322 0.0016  0.0235  -0.0198 735  ILE A CG1 
1450 C CG2 . ILE A 198 ? 0.5053 0.3696 0.2946 0.0008  0.0218  -0.0238 735  ILE A CG2 
1451 C CD1 . ILE A 198 ? 0.6013 0.4426 0.4229 0.0062  0.0292  -0.0360 735  ILE A CD1 
1452 N N   . ALA A 199 ? 0.5126 0.4464 0.3197 -0.0364 0.0064  0.0310  736  ALA A N   
1453 C CA  . ALA A 199 ? 0.6068 0.5904 0.3964 -0.0469 0.0044  0.0321  736  ALA A CA  
1454 C C   . ALA A 199 ? 0.6115 0.6050 0.4098 -0.0554 -0.0023 0.0542  736  ALA A C   
1455 O O   . ALA A 199 ? 0.5992 0.6187 0.3833 -0.0553 -0.0016 0.0437  736  ALA A O   
1456 C CB  . ALA A 199 ? 0.5513 0.5829 0.3378 -0.0642 0.0017  0.0432  736  ALA A CB  
1457 N N   . LYS A 200 ? 0.5440 0.5172 0.3719 -0.0621 -0.0107 0.0825  737  LYS A N   
1458 C CA  . LYS A 200 ? 0.6486 0.6276 0.4902 -0.0702 -0.0193 0.1059  737  LYS A CA  
1459 C C   . LYS A 200 ? 0.6786 0.6298 0.5101 -0.0537 -0.0129 0.0855  737  LYS A C   
1460 O O   . LYS A 200 ? 0.6859 0.6593 0.5086 -0.0581 -0.0149 0.0901  737  LYS A O   
1461 C CB  . LYS A 200 ? 0.6140 0.5686 0.5027 -0.0775 -0.0331 0.1358  737  LYS A CB  
1462 C CG  . LYS A 200 ? 0.6499 0.6073 0.5609 -0.0862 -0.0452 0.1627  737  LYS A CG  
1463 C CD  . LYS A 200 ? 0.7218 0.6598 0.6935 -0.0957 -0.0652 0.1941  737  LYS A CD  
1464 C CE  . LYS A 200 ? 0.8457 0.7909 0.8452 -0.1075 -0.0813 0.2264  737  LYS A CE  
1465 N NZ  . LYS A 200 ? 0.8735 0.8252 0.9333 -0.1288 -0.1086 0.2729  737  LYS A NZ  
1466 N N   . ILE A 201 ? 0.5552 0.4638 0.3888 -0.0365 -0.0058 0.0642  738  ILE A N   
1467 C CA  . ILE A 201 ? 0.5162 0.4034 0.3409 -0.0237 -0.0012 0.0486  738  ILE A CA  
1468 C C   . ILE A 201 ? 0.6442 0.5539 0.4427 -0.0207 0.0017  0.0304  738  ILE A C   
1469 O O   . ILE A 201 ? 0.6109 0.5254 0.4057 -0.0192 -0.0001 0.0287  738  ILE A O   
1470 C CB  . ILE A 201 ? 0.5245 0.3777 0.3556 -0.0107 0.0050  0.0315  738  ILE A CB  
1471 C CG1 . ILE A 201 ? 0.6732 0.5096 0.5424 -0.0115 0.0002  0.0405  738  ILE A CG1 
1472 C CG2 . ILE A 201 ? 0.5327 0.3737 0.3503 -0.0012 0.0086  0.0181  738  ILE A CG2 
1473 C CD1 . ILE A 201 ? 0.6789 0.4995 0.5586 -0.0014 0.0066  0.0192  738  ILE A CD1 
1474 N N   . ILE A 202 ? 0.6544 0.5791 0.4404 -0.0192 0.0046  0.0136  739  ILE A N   
1475 C CA  . ILE A 202 ? 0.5486 0.4983 0.3231 -0.0149 0.0038  -0.0108 739  ILE A CA  
1476 C C   . ILE A 202 ? 0.5954 0.5961 0.3669 -0.0270 0.0000  -0.0059 739  ILE A C   
1477 O O   . ILE A 202 ? 0.5939 0.6059 0.3661 -0.0222 -0.0026 -0.0212 739  ILE A O   
1478 C CB  . ILE A 202 ? 0.5672 0.5301 0.3359 -0.0123 0.0058  -0.0307 739  ILE A CB  
1479 C CG1 . ILE A 202 ? 0.5553 0.4731 0.3262 -0.0008 0.0086  -0.0366 739  ILE A CG1 
1480 C CG2 . ILE A 202 ? 0.6176 0.6183 0.3866 -0.0090 0.0018  -0.0615 739  ILE A CG2 
1481 C CD1 . ILE A 202 ? 0.5279 0.4544 0.2946 0.0011  0.0104  -0.0520 739  ILE A CD1 
1482 N N   . ARG A 203 ? 0.6023 0.6392 0.3737 -0.0445 -0.0020 0.0173  740  ARG A N   
1483 C CA  . ARG A 203 ? 0.7295 0.8274 0.4975 -0.0614 -0.0066 0.0293  740  ARG A CA  
1484 C C   . ARG A 203 ? 0.7534 0.8342 0.5273 -0.0584 -0.0097 0.0385  740  ARG A C   
1485 O O   . ARG A 203 ? 0.7617 0.8805 0.5306 -0.0595 -0.0107 0.0228  740  ARG A O   
1486 C CB  . ARG A 203 ? 0.7699 0.8996 0.5445 -0.0844 -0.0128 0.0680  740  ARG A CB  
1487 C CG  . ARG A 203 ? 0.8983 1.1133 0.6598 -0.1032 -0.0133 0.0641  740  ARG A CG  
1488 C CD  . ARG A 203 ? 0.9641 1.2236 0.7358 -0.1331 -0.0246 0.1150  740  ARG A CD  
1489 N NE  . ARG A 203 ? 0.9802 1.1786 0.7791 -0.1333 -0.0322 0.1479  740  ARG A NE  
1490 C CZ  . ARG A 203 ? 0.9790 1.1546 0.7847 -0.1307 -0.0309 0.1468  740  ARG A CZ  
1491 N NH1 . ARG A 203 ? 0.9817 1.1873 0.7655 -0.1276 -0.0216 0.1170  740  ARG A NH1 
1492 N NH2 . ARG A 203 ? 0.9244 1.0488 0.7641 -0.1302 -0.0398 0.1720  740  ARG A NH2 
1493 N N   . ARG A 204 ? 0.6635 0.6912 0.4519 -0.0543 -0.0115 0.0602  741  ARG A N   
1494 C CA  . ARG A 204 ? 0.6645 0.6753 0.4604 -0.0518 -0.0145 0.0698  741  ARG A CA  
1495 C C   . ARG A 204 ? 0.7807 0.7719 0.5688 -0.0349 -0.0104 0.0392  741  ARG A C   
1496 O O   . ARG A 204 ? 0.8770 0.8848 0.6644 -0.0355 -0.0129 0.0359  741  ARG A O   
1497 C CB  . ARG A 204 ? 0.7079 0.6699 0.5284 -0.0493 -0.0181 0.0915  741  ARG A CB  
1498 C CG  . ARG A 204 ? 0.8084 0.7380 0.6359 -0.0389 -0.0176 0.0883  741  ARG A CG  
1499 C CD  . ARG A 204 ? 0.9193 0.8174 0.7807 -0.0393 -0.0241 0.1074  741  ARG A CD  
1500 N NE  . ARG A 204 ? 1.0161 0.8932 0.8953 -0.0360 -0.0236 0.1040  741  ARG A NE  
1501 C CZ  . ARG A 204 ? 0.9304 0.7793 0.8095 -0.0220 -0.0153 0.0804  741  ARG A CZ  
1502 N NH1 . ARG A 204 ? 0.8633 0.7007 0.7255 -0.0117 -0.0081 0.0630  741  ARG A NH1 
1503 N NH2 . ARG A 204 ? 0.9421 0.7794 0.8402 -0.0200 -0.0154 0.0756  741  ARG A NH2 
1504 N N   . LYS A 205 ? 0.6969 0.6549 0.4831 -0.0213 -0.0063 0.0190  742  LYS A N   
1505 C CA  . LYS A 205 ? 0.6470 0.5844 0.4345 -0.0081 -0.0074 -0.0027 742  LYS A CA  
1506 C C   . LYS A 205 ? 0.7152 0.6959 0.5040 -0.0074 -0.0119 -0.0297 742  LYS A C   
1507 O O   . LYS A 205 ? 0.7554 0.7333 0.5534 -0.0013 -0.0169 -0.0415 742  LYS A O   
1508 C CB  . LYS A 205 ? 0.6447 0.5456 0.4332 0.0021  -0.0053 -0.0123 742  LYS A CB  
1509 C CG  . LYS A 205 ? 0.6369 0.5043 0.4292 0.0030  -0.0006 0.0041  742  LYS A CG  
1510 C CD  . LYS A 205 ? 0.7254 0.5697 0.5234 0.0075  -0.0015 0.0088  742  LYS A CD  
1511 C CE  . LYS A 205 ? 0.6843 0.5091 0.4903 0.0086  0.0035  0.0152  742  LYS A CE  
1512 N NZ  . LYS A 205 ? 0.8048 0.6193 0.6186 0.0100  0.0035  0.0203  742  LYS A NZ  
1513 N N   A LYS A 206 ? 0.7102 0.7358 0.4943 -0.0136 -0.0110 -0.0430 743  LYS A N   
1514 N N   B LYS A 206 ? 0.7109 0.7367 0.4951 -0.0136 -0.0110 -0.0430 743  LYS A N   
1515 C CA  A LYS A 206 ? 0.7576 0.8393 0.5496 -0.0133 -0.0155 -0.0775 743  LYS A CA  
1516 C CA  B LYS A 206 ? 0.7578 0.8395 0.5498 -0.0133 -0.0155 -0.0775 743  LYS A CA  
1517 C C   A LYS A 206 ? 0.8486 0.9774 0.6387 -0.0240 -0.0171 -0.0716 743  LYS A C   
1518 C C   B LYS A 206 ? 0.8483 0.9773 0.6384 -0.0240 -0.0171 -0.0716 743  LYS A C   
1519 O O   A LYS A 206 ? 0.8750 1.0336 0.6796 -0.0187 -0.0223 -0.1024 743  LYS A O   
1520 O O   B LYS A 206 ? 0.8745 1.0338 0.6790 -0.0188 -0.0223 -0.1025 743  LYS A O   
1521 C CB  A LYS A 206 ? 0.7322 0.8644 0.5188 -0.0204 -0.0131 -0.0933 743  LYS A CB  
1522 C CB  B LYS A 206 ? 0.7322 0.8644 0.5190 -0.0203 -0.0132 -0.0936 743  LYS A CB  
1523 C CG  A LYS A 206 ? 0.7344 0.8453 0.5344 -0.0061 -0.0162 -0.1238 743  LYS A CG  
1524 C CG  B LYS A 206 ? 0.7367 0.8416 0.5345 -0.0065 -0.0154 -0.1193 743  LYS A CG  
1525 C CD  A LYS A 206 ? 0.7494 0.9175 0.5430 -0.0147 -0.0129 -0.1398 743  LYS A CD  
1526 C CD  B LYS A 206 ? 0.7489 0.9175 0.5441 -0.0139 -0.0134 -0.1422 743  LYS A CD  
1527 C CE  A LYS A 206 ? 0.7364 0.8792 0.5447 -0.0009 -0.0166 -0.1666 743  LYS A CE  
1528 C CE  B LYS A 206 ? 0.7392 0.8736 0.5399 -0.0035 -0.0139 -0.1545 743  LYS A CE  
1529 N NZ  A LYS A 206 ? 0.6829 0.8487 0.4747 -0.0102 -0.0095 -0.1600 743  LYS A NZ  
1530 N NZ  B LYS A 206 ? 0.6800 0.8556 0.5068 0.0050  -0.0217 -0.2058 743  LYS A NZ  
1531 N N   . GLN A 207 ? 0.9233 1.0616 0.7015 -0.0396 -0.0149 -0.0326 744  GLN A N   
1532 C CA  . GLN A 207 ? 0.9510 1.1395 0.7271 -0.0532 -0.0178 -0.0206 744  GLN A CA  
1533 C C   . GLN A 207 ? 0.9452 1.0973 0.7309 -0.0411 -0.0204 -0.0265 744  GLN A C   
1534 O O   . GLN A 207 ? 1.0009 1.1984 0.7921 -0.0425 -0.0235 -0.0467 744  GLN A O   
1535 C CB  . GLN A 207 ? 0.9801 1.1760 0.7514 -0.0730 -0.0199 0.0296  744  GLN A CB  
1536 C CG  . GLN A 207 ? 1.1433 1.4201 0.9059 -0.0965 -0.0217 0.0412  744  GLN A CG  
1537 C CD  . GLN A 207 ? 1.3273 1.6664 1.0891 -0.1218 -0.0292 0.0769  744  GLN A CD  
1538 O OE1 . GLN A 207 ? 1.4594 1.7726 1.2325 -0.1331 -0.0372 0.1240  744  GLN A OE1 
1539 N NE2 . GLN A 207 ? 1.3067 1.7327 1.0607 -0.1313 -0.0287 0.0530  744  GLN A NE2 
1540 N N   . ALA A 208 ? 0.8939 0.9710 0.6834 -0.0301 -0.0194 -0.0111 745  ALA A N   
1541 C CA  . ALA A 208 ? 0.9120 0.9545 0.7098 -0.0211 -0.0220 -0.0108 745  ALA A CA  
1542 C C   . ALA A 208 ? 0.9827 1.0332 0.7964 -0.0089 -0.0278 -0.0497 745  ALA A C   
1543 O O   . ALA A 208 ? 1.0512 1.1084 0.8749 -0.0018 -0.0307 -0.0779 745  ALA A O   
1544 C CB  . ALA A 208 ? 0.7591 0.7326 0.5592 -0.0128 -0.0194 0.0070  745  ALA A CB  
1545 N N   . ILE A 217 ? 0.9915 0.9328 0.8769 -0.0382 -0.0578 0.1595  754  ILE A N   
1546 C CA  . ILE A 217 ? 0.8775 0.7725 0.7832 -0.0284 -0.0571 0.1589  754  ILE A CA  
1547 C C   . ILE A 217 ? 0.8608 0.7562 0.7978 -0.0360 -0.0696 0.1861  754  ILE A C   
1548 O O   . ILE A 217 ? 0.8164 0.7397 0.7520 -0.0447 -0.0758 0.2005  754  ILE A O   
1549 C CB  . ILE A 217 ? 0.8356 0.7126 0.7301 -0.0170 -0.0497 0.1363  754  ILE A CB  
1550 C CG1 . ILE A 217 ? 0.7615 0.6286 0.6393 -0.0098 -0.0425 0.1143  754  ILE A CG1 
1551 C CG2 . ILE A 217 ? 0.7196 0.5671 0.6353 -0.0107 -0.0495 0.1365  754  ILE A CG2 
1552 C CD1 . ILE A 217 ? 0.7849 0.6461 0.6559 -0.0033 -0.0413 0.0972  754  ILE A CD1 
1553 N N   . THR A 218 ? 0.9187 0.7860 0.8900 -0.0328 -0.0749 0.1911  755  THR A N   
1554 C CA  . THR A 218 ? 0.8990 0.7611 0.9163 -0.0387 -0.0918 0.2153  755  THR A CA  
1555 C C   . THR A 218 ? 0.7104 0.5416 0.7550 -0.0249 -0.0897 0.1945  755  THR A C   
1556 O O   . THR A 218 ? 0.6726 0.4880 0.7084 -0.0134 -0.0770 0.1658  755  THR A O   
1557 C CB  . THR A 218 ? 0.9413 0.8027 0.9947 -0.0478 -0.1062 0.2373  755  THR A CB  
1558 O OG1 . THR A 218 ? 1.0170 0.8468 1.0918 -0.0345 -0.1011 0.2119  755  THR A OG1 
1559 C CG2 . THR A 218 ? 0.9466 0.8442 0.9670 -0.0612 -0.1043 0.2511  755  THR A CG2 
1560 N N   . PHE A 219 ? 0.6692 0.4989 0.7495 -0.0278 -0.1033 0.2096  756  PHE A N   
1561 C CA  . PHE A 219 ? 0.6035 0.4132 0.7156 -0.0159 -0.1031 0.1882  756  PHE A CA  
1562 C C   . PHE A 219 ? 0.5508 0.3490 0.7381 -0.0176 -0.1263 0.2008  756  PHE A C   
1563 O O   . PHE A 219 ? 0.6048 0.4127 0.8170 -0.0312 -0.1461 0.2384  756  PHE A O   
1564 C CB  . PHE A 219 ? 0.5653 0.3828 0.6549 -0.0152 -0.0983 0.1877  756  PHE A CB  
1565 C CG  . PHE A 219 ? 0.5725 0.3983 0.6036 -0.0123 -0.0802 0.1724  756  PHE A CG  
1566 C CD1 . PHE A 219 ? 0.5893 0.4040 0.6055 -0.0024 -0.0663 0.1442  756  PHE A CD1 
1567 C CD2 . PHE A 219 ? 0.6384 0.4893 0.6359 -0.0209 -0.0796 0.1856  756  PHE A CD2 
1568 C CE1 . PHE A 219 ? 0.6910 0.5103 0.6650 -0.0011 -0.0554 0.1343  756  PHE A CE1 
1569 C CE2 . PHE A 219 ? 0.6000 0.4571 0.5580 -0.0167 -0.0673 0.1669  756  PHE A CE2 
1570 C CZ  . PHE A 219 ? 0.6226 0.4592 0.5717 -0.0068 -0.0569 0.1438  756  PHE A CZ  
1571 N N   . GLU A 220 ? 0.5555 0.3387 0.7846 -0.0052 -0.1259 0.1689  757  GLU A N   
1572 C CA  . GLU A 220 ? 0.5762 0.3474 0.8935 -0.0033 -0.1510 0.1706  757  GLU A CA  
1573 C C   . GLU A 220 ? 0.6386 0.4086 0.9894 -0.0003 -0.1609 0.1695  757  GLU A C   
1574 O O   . GLU A 220 ? 0.6526 0.4137 1.0791 -0.0032 -0.1887 0.1856  757  GLU A O   
1575 C CB  . GLU A 220 ? 0.6260 0.3919 0.9815 0.0101  -0.1467 0.1267  757  GLU A CB  
1576 C CG  . GLU A 220 ? 0.7066 0.4612 1.1686 0.0150  -0.1750 0.1172  757  GLU A CG  
1577 C CD  . GLU A 220 ? 0.8340 0.5956 1.3436 0.0283  -0.1765 0.0765  757  GLU A CD  
1578 O OE1 . GLU A 220 ? 0.8097 0.5644 1.4110 0.0307  -0.2043 0.0738  757  GLU A OE1 
1579 O OE2 . GLU A 220 ? 0.8617 0.6416 1.3197 0.0346  -0.1512 0.0471  757  GLU A OE2 
1580 N N   . SER A 221 ? 0.6796 0.4581 0.9809 0.0050  -0.1411 0.1519  758  SER A N   
1581 C CA  . SER A 221 ? 0.7583 0.5386 1.0769 0.0071  -0.1466 0.1515  758  SER A CA  
1582 C C   . SER A 221 ? 0.6708 0.4626 0.9120 0.0025  -0.1287 0.1619  758  SER A C   
1583 O O   . SER A 221 ? 0.6389 0.4359 0.8226 0.0033  -0.1094 0.1518  758  SER A O   
1584 C CB  . SER A 221 ? 0.8058 0.5903 1.1649 0.0220  -0.1417 0.1026  758  SER A CB  
1585 O OG  . SER A 221 ? 0.9129 0.7113 1.2246 0.0274  -0.1165 0.0707  758  SER A OG  
1586 N N   . PRO A 222 ? 0.6284 0.4251 0.8725 -0.0025 -0.1371 0.1817  759  PRO A N   
1587 C CA  . PRO A 222 ? 0.5715 0.3831 0.7502 -0.0085 -0.1245 0.1939  759  PRO A CA  
1588 C C   . PRO A 222 ? 0.5985 0.4101 0.7366 0.0011  -0.1023 0.1614  759  PRO A C   
1589 O O   . PRO A 222 ? 0.6208 0.4303 0.7818 0.0090  -0.0999 0.1385  759  PRO A O   
1590 C CB  . PRO A 222 ? 0.5761 0.3946 0.7812 -0.0154 -0.1413 0.2194  759  PRO A CB  
1591 C CG  . PRO A 222 ? 0.7013 0.5079 0.9862 -0.0178 -0.1681 0.2347  759  PRO A CG  
1592 C CD  . PRO A 222 ? 0.6530 0.4435 0.9680 -0.0041 -0.1624 0.1960  759  PRO A CD  
1593 N N   . PRO A 223 ? 0.5878 0.4061 0.6705 -0.0008 -0.0881 0.1592  760  PRO A N   
1594 C CA  . PRO A 223 ? 0.5381 0.3571 0.5886 0.0048  -0.0723 0.1368  760  PRO A CA  
1595 C C   . PRO A 223 ? 0.5632 0.3877 0.6081 0.0042  -0.0733 0.1405  760  PRO A C   
1596 O O   . PRO A 223 ? 0.5473 0.3800 0.5945 -0.0018 -0.0827 0.1615  760  PRO A O   
1597 C CB  . PRO A 223 ? 0.5152 0.3383 0.5216 0.0019  -0.0641 0.1383  760  PRO A CB  
1598 C CG  . PRO A 223 ? 0.6449 0.4811 0.6493 -0.0068 -0.0737 0.1623  760  PRO A CG  
1599 C CD  . PRO A 223 ? 0.6060 0.4368 0.6586 -0.0097 -0.0887 0.1781  760  PRO A CD  
1600 N N   . PRO A 224 ? 0.5293 0.3553 0.5668 0.0083  -0.0644 0.1222  761  PRO A N   
1601 C CA  . PRO A 224 ? 0.5126 0.3434 0.5474 0.0079  -0.0656 0.1248  761  PRO A CA  
1602 C C   . PRO A 224 ? 0.5527 0.3891 0.5539 0.0037  -0.0652 0.1360  761  PRO A C   
1603 O O   . PRO A 224 ? 0.5463 0.3838 0.5234 0.0024  -0.0613 0.1344  761  PRO A O   
1604 C CB  . PRO A 224 ? 0.5080 0.3464 0.5386 0.0100  -0.0556 0.1039  761  PRO A CB  
1605 C CG  . PRO A 224 ? 0.5058 0.3452 0.5176 0.0088  -0.0480 0.0967  761  PRO A CG  
1606 C CD  . PRO A 224 ? 0.5081 0.3388 0.5381 0.0108  -0.0535 0.1008  761  PRO A CD  
1607 N N   . PRO A 225 ? 0.5619 0.4055 0.5652 0.0020  -0.0698 0.1434  762  PRO A N   
1608 C CA  . PRO A 225 ? 0.5268 0.3840 0.5049 -0.0011 -0.0699 0.1461  762  PRO A CA  
1609 C C   . PRO A 225 ? 0.5102 0.3608 0.4703 0.0016  -0.0633 0.1308  762  PRO A C   
1610 O O   . PRO A 225 ? 0.5163 0.3585 0.4805 0.0030  -0.0593 0.1239  762  PRO A O   
1611 C CB  . PRO A 225 ? 0.5926 0.4588 0.5821 -0.0026 -0.0758 0.1538  762  PRO A CB  
1612 C CG  . PRO A 225 ? 0.6237 0.4757 0.6399 0.0019  -0.0756 0.1481  762  PRO A CG  
1613 C CD  . PRO A 225 ? 0.5317 0.3746 0.5650 0.0037  -0.0759 0.1454  762  PRO A CD  
1614 N N   . ILE A 226 ? 0.6031 0.4664 0.4073 -0.0885 -0.1261 0.1518  763  ILE A N   
1615 C CA  . ILE A 226 ? 0.5620 0.4402 0.3655 -0.0835 -0.1087 0.1303  763  ILE A CA  
1616 C C   . ILE A 226 ? 0.5302 0.4175 0.3425 -0.0772 -0.1172 0.1271  763  ILE A C   
1617 O O   . ILE A 226 ? 0.5785 0.4669 0.3782 -0.0858 -0.1326 0.1398  763  ILE A O   
1618 C CB  . ILE A 226 ? 0.6337 0.5212 0.4037 -0.1003 -0.0941 0.1242  763  ILE A CB  
1619 C CG1 . ILE A 226 ? 0.7258 0.6055 0.4872 -0.1087 -0.0865 0.1292  763  ILE A CG1 
1620 C CG2 . ILE A 226 ? 0.5508 0.4516 0.3252 -0.0942 -0.0764 0.1020  763  ILE A CG2 
1621 C CD1 . ILE A 226 ? 0.7310 0.6046 0.5201 -0.0944 -0.0788 0.1207  763  ILE A CD1 
1622 N N   . GLU A 227 ? 0.4658 0.3604 0.2991 -0.0633 -0.1075 0.1105  764  GLU A N   
1623 C CA  . GLU A 227 ? 0.5380 0.4421 0.3838 -0.0567 -0.1139 0.1061  764  GLU A CA  
1624 C C   . GLU A 227 ? 0.5353 0.4529 0.3626 -0.0637 -0.1016 0.0923  764  GLU A C   
1625 O O   . GLU A 227 ? 0.5341 0.4549 0.3576 -0.0634 -0.0840 0.0793  764  GLU A O   
1626 C CB  . GLU A 227 ? 0.4545 0.3585 0.3363 -0.0378 -0.1114 0.0971  764  GLU A CB  
1627 C CG  . GLU A 227 ? 0.5040 0.3949 0.4104 -0.0290 -0.1232 0.1073  764  GLU A CG  
1628 C CD  . GLU A 227 ? 0.5917 0.4825 0.5146 -0.0261 -0.1436 0.1193  764  GLU A CD  
1629 O OE1 . GLU A 227 ? 0.5614 0.4642 0.4805 -0.0286 -0.1476 0.1173  764  GLU A OE1 
1630 O OE2 . GLU A 227 ? 0.5428 0.4215 0.4850 -0.0213 -0.1561 0.1305  764  GLU A OE2 
1631 N N   . TRP A 228 ? 0.4965 0.4220 0.3150 -0.0700 -0.1116 0.0950  765  TRP A N   
1632 C CA  . TRP A 228 ? 0.5013 0.4388 0.3026 -0.0781 -0.1019 0.0818  765  TRP A CA  
1633 C C   . TRP A 228 ? 0.5479 0.4942 0.3681 -0.0706 -0.1088 0.0770  765  TRP A C   
1634 O O   . TRP A 228 ? 0.5425 0.4879 0.3774 -0.0663 -0.1264 0.0884  765  TRP A O   
1635 C CB  . TRP A 228 ? 0.5748 0.5149 0.3378 -0.0990 -0.1060 0.0885  765  TRP A CB  
1636 C CG  . TRP A 228 ? 0.5801 0.5142 0.3228 -0.1088 -0.0959 0.0913  765  TRP A CG  
1637 C CD1 . TRP A 228 ? 0.6615 0.5853 0.3938 -0.1158 -0.1060 0.1096  765  TRP A CD1 
1638 C CD2 . TRP A 228 ? 0.5714 0.5099 0.3052 -0.1126 -0.0738 0.0754  765  TRP A CD2 
1639 N NE1 . TRP A 228 ? 0.6205 0.5428 0.3363 -0.1246 -0.0907 0.1058  765  TRP A NE1 
1640 C CE2 . TRP A 228 ? 0.5972 0.5291 0.3150 -0.1224 -0.0708 0.0845  765  TRP A CE2 
1641 C CE3 . TRP A 228 ? 0.6025 0.5496 0.3430 -0.1087 -0.0568 0.0549  765  TRP A CE3 
1642 C CZ2 . TRP A 228 ? 0.6161 0.5517 0.3253 -0.1281 -0.0508 0.0726  765  TRP A CZ2 
1643 C CZ3 . TRP A 228 ? 0.5916 0.5412 0.3250 -0.1137 -0.0378 0.0436  765  TRP A CZ3 
1644 C CH2 . TRP A 228 ? 0.5787 0.5235 0.2971 -0.1232 -0.0346 0.0520  765  TRP A CH2 
1645 N N   . HIS A 229 ? 0.5029 0.4578 0.3251 -0.0691 -0.0952 0.0601  766  HIS A N   
1646 C CA  . HIS A 229 ? 0.4845 0.4482 0.3267 -0.0621 -0.0987 0.0538  766  HIS A CA  
1647 C C   . HIS A 229 ? 0.5153 0.4881 0.3356 -0.0761 -0.0987 0.0467  766  HIS A C   
1648 O O   . HIS A 229 ? 0.5749 0.5497 0.3759 -0.0881 -0.1131 0.0566  766  HIS A O   
1649 C CB  . HIS A 229 ? 0.4119 0.3768 0.2781 -0.0484 -0.0838 0.0410  766  HIS A CB  
1650 C CG  . HIS A 229 ? 0.4740 0.4482 0.3610 -0.0422 -0.0856 0.0345  766  HIS A CG  
1651 N ND1 . HIS A 229 ? 0.4200 0.3996 0.3190 -0.0413 -0.1022 0.0423  766  HIS A ND1 
1652 C CD2 . HIS A 229 ? 0.4634 0.4429 0.3626 -0.0374 -0.0733 0.0217  766  HIS A CD2 
1653 C CE1 . HIS A 229 ? 0.4825 0.4712 0.4000 -0.0365 -0.0989 0.0336  766  HIS A CE1 
1654 N NE2 . HIS A 229 ? 0.4713 0.4594 0.3883 -0.0344 -0.0815 0.0215  766  HIS A NE2 
1655 N N   . ILE A 230 ? 0.5349 0.5128 0.3574 -0.0755 -0.0832 0.0298  767  ILE A N   
1656 C CA  . ILE A 230 ? 0.4719 0.4576 0.2751 -0.0890 -0.0805 0.0192  767  ILE A CA  
1657 C C   . ILE A 230 ? 0.6516 0.6358 0.4240 -0.1029 -0.0689 0.0134  767  ILE A C   
1658 O O   . ILE A 230 ? 0.6468 0.6351 0.3904 -0.1193 -0.0747 0.0148  767  ILE A O   
1659 C CB  . ILE A 230 ? 0.4650 0.4558 0.2894 -0.0819 -0.0698 0.0037  767  ILE A CB  
1660 C CG1 . ILE A 230 ? 0.5724 0.5680 0.4242 -0.0719 -0.0816 0.0090  767  ILE A CG1 
1661 C CG2 . ILE A 230 ? 0.5592 0.5561 0.3646 -0.0960 -0.0639 -0.0104 767  ILE A CG2 
1662 C CD1 . ILE A 230 ? 0.5171 0.5167 0.3918 -0.0644 -0.0708 -0.0037 767  ILE A CD1 
1663 N N   . SER A 231 ? 0.5220 0.5016 0.2999 -0.0976 -0.0527 0.0067  768  SER A N   
1664 C CA  . SER A 231 ? 0.6797 0.6590 0.4322 -0.1102 -0.0412 0.0019  768  SER A CA  
1665 C C   . SER A 231 ? 0.7215 0.6958 0.4528 -0.1188 -0.0531 0.0204  768  SER A C   
1666 O O   . SER A 231 ? 0.7041 0.6709 0.4500 -0.1090 -0.0631 0.0347  768  SER A O   
1667 C CB  . SER A 231 ? 0.7426 0.7187 0.5112 -0.1013 -0.0230 -0.0078 768  SER A CB  
1668 O OG  . SER A 231 ? 0.5894 0.5695 0.3746 -0.0965 -0.0115 -0.0246 768  SER A OG  
1669 N N   . LYS A 232 ? 0.7230 0.7014 0.4203 -0.1378 -0.0519 0.0200  769  LYS A N   
1670 C CA  . LYS A 232 ? 0.8004 0.7743 0.4734 -0.1493 -0.0643 0.0393  769  LYS A CA  
1671 C C   . LYS A 232 ? 0.8054 0.7779 0.4611 -0.1587 -0.0485 0.0364  769  LYS A C   
1672 O O   . LYS A 232 ? 0.7421 0.7197 0.4010 -0.1590 -0.0281 0.0173  769  LYS A O   
1673 C CB  . LYS A 232 ? 0.8215 0.8024 0.4644 -0.1670 -0.0785 0.0447  769  LYS A CB  
1674 C CG  . LYS A 232 ? 0.8650 0.8478 0.5273 -0.1583 -0.0979 0.0515  769  LYS A CG  
1675 C CD  . LYS A 232 ? 0.9110 0.8839 0.6041 -0.1410 -0.1108 0.0683  769  LYS A CD  
1676 C CE  . LYS A 232 ? 1.0064 0.9832 0.7215 -0.1330 -0.1298 0.0748  769  LYS A CE  
1677 N NZ  . LYS A 232 ? 1.0262 0.9945 0.7748 -0.1157 -0.1406 0.0882  769  LYS A NZ  
1678 N N   . PRO A 233 ? 0.8553 0.8207 0.4962 -0.1659 -0.0572 0.0553  770  PRO A N   
1679 C CA  . PRO A 233 ? 0.8373 0.8019 0.4641 -0.1751 -0.0418 0.0534  770  PRO A CA  
1680 C C   . PRO A 233 ? 0.8509 0.8283 0.4588 -0.1897 -0.0228 0.0335  770  PRO A C   
1681 O O   . PRO A 233 ? 0.8784 0.8635 0.4725 -0.2003 -0.0269 0.0303  770  PRO A O   
1682 C CB  . PRO A 233 ? 0.8950 0.8521 0.5082 -0.1842 -0.0579 0.0776  770  PRO A CB  
1683 C CG  . PRO A 233 ? 0.8331 0.7815 0.4632 -0.1720 -0.0812 0.0939  770  PRO A CG  
1684 C CD  . PRO A 233 ? 0.8152 0.7721 0.4578 -0.1643 -0.0819 0.0797  770  PRO A CD  
1685 N N   . GLY A 234 ? 0.8611 0.8413 0.4763 -0.1880 -0.0015 0.0186  771  GLY A N   
1686 C CA  . GLY A 234 ? 0.9048 0.8973 0.5152 -0.1982 0.0186  -0.0024 771  GLY A CA  
1687 C C   . GLY A 234 ? 0.8612 0.8603 0.4844 -0.1925 0.0291  -0.0255 771  GLY A C   
1688 O O   . GLY A 234 ? 0.9437 0.9516 0.5724 -0.1972 0.0481  -0.0452 771  GLY A O   
1689 N N   . GLN A 235 ? 0.7828 0.7779 0.4170 -0.1816 0.0170  -0.0237 772  GLN A N   
1690 C CA  . GLN A 235 ? 0.8608 0.8610 0.5118 -0.1758 0.0250  -0.0444 772  GLN A CA  
1691 C C   . GLN A 235 ? 0.7961 0.7932 0.4870 -0.1569 0.0374  -0.0545 772  GLN A C   
1692 O O   . GLN A 235 ? 0.7432 0.7373 0.4598 -0.1425 0.0326  -0.0566 772  GLN A O   
1693 C CB  . GLN A 235 ? 0.8234 0.8222 0.4771 -0.1715 0.0056  -0.0369 772  GLN A CB  
1694 C CG  . GLN A 235 ? 0.9219 0.9240 0.5424 -0.1882 -0.0110 -0.0239 772  GLN A CG  
1695 C CD  . GLN A 235 ? 1.0137 1.0151 0.6413 -0.1827 -0.0316 -0.0157 772  GLN A CD  
1696 O OE1 . GLN A 235 ? 0.9866 0.9842 0.6488 -0.1641 -0.0337 -0.0166 772  GLN A OE1 
1697 N NE2 . GLN A 235 ? 0.9906 0.9966 0.5997 -0.1947 -0.0456 -0.0068 772  GLN A NE2 
1698 N N   . PHE A 236 ? 0.7884 0.7870 0.4849 -0.1576 0.0531  -0.0604 773  PHE A N   
1699 C CA  . PHE A 236 ? 0.7525 0.7471 0.4862 -0.1395 0.0601  -0.0637 773  PHE A CA  
1700 C C   . PHE A 236 ? 0.7273 0.7246 0.4873 -0.1310 0.0700  -0.0829 773  PHE A C   
1701 O O   . PHE A 236 ? 0.6858 0.6787 0.4771 -0.1149 0.0707  -0.0824 773  PHE A O   
1702 C CB  . PHE A 236 ? 0.8557 0.8524 0.5910 -0.1430 0.0733  -0.0647 773  PHE A CB  
1703 C CG  . PHE A 236 ? 1.0215 1.0296 0.7485 -0.1567 0.0938  -0.0853 773  PHE A CG  
1704 C CD1 . PHE A 236 ? 1.0330 1.0454 0.7915 -0.1485 0.1098  -0.1042 773  PHE A CD1 
1705 C CD2 . PHE A 236 ? 1.1361 1.1505 0.8297 -0.1765 0.0959  -0.0844 773  PHE A CD2 
1706 C CE1 . PHE A 236 ? 1.0762 1.0995 0.8357 -0.1591 0.1283  -0.1236 773  PHE A CE1 
1707 C CE2 . PHE A 236 ? 1.1231 1.1486 0.8225 -0.1854 0.1124  -0.1018 773  PHE A CE2 
1708 C CZ  . PHE A 236 ? 1.1033 1.1332 0.8363 -0.1765 0.1286  -0.1217 773  PHE A CZ  
1709 N N   . GLU A 237 ? 0.7234 0.7273 0.4718 -0.1421 0.0771  -0.0996 774  GLU A N   
1710 C CA  . GLU A 237 ? 0.7258 0.7303 0.5026 -0.1337 0.0853  -0.1171 774  GLU A CA  
1711 C C   . GLU A 237 ? 0.6316 0.6301 0.4222 -0.1224 0.0702  -0.1090 774  GLU A C   
1712 O O   . GLU A 237 ? 0.7527 0.7488 0.5727 -0.1118 0.0744  -0.1176 774  GLU A O   
1713 C CB  . GLU A 237 ? 0.9078 0.9206 0.6707 -0.1492 0.0986  -0.1402 774  GLU A CB  
1714 C CG  . GLU A 237 ? 1.0593 1.0808 0.8142 -0.1605 0.1126  -0.1464 774  GLU A CG  
1715 C CD  . GLU A 237 ? 1.3328 1.3579 1.0492 -0.1765 0.1032  -0.1324 774  GLU A CD  
1716 O OE1 . GLU A 237 ? 1.4417 1.4738 1.1497 -0.1872 0.1128  -0.1347 774  GLU A OE1 
1717 O OE2 . GLU A 237 ? 1.4000 1.4209 1.0964 -0.1786 0.0854  -0.1185 774  GLU A OE2 
1718 N N   . THR A 238 ? 0.6524 0.6489 0.4249 -0.1246 0.0526  -0.0923 775  THR A N   
1719 C CA  . THR A 238 ? 0.7091 0.7019 0.4967 -0.1140 0.0385  -0.0842 775  THR A CA  
1720 C C   . THR A 238 ? 0.6415 0.6277 0.4499 -0.0976 0.0313  -0.0685 775  THR A C   
1721 O O   . THR A 238 ? 0.5162 0.5003 0.3399 -0.0881 0.0216  -0.0624 775  THR A O   
1722 C CB  . THR A 238 ? 0.7764 0.7721 0.5381 -0.1246 0.0221  -0.0751 775  THR A CB  
1723 O OG1 . THR A 238 ? 0.7306 0.7224 0.4810 -0.1236 0.0093  -0.0543 775  THR A OG1 
1724 C CG2 . THR A 238 ? 0.8318 0.8350 0.5626 -0.1449 0.0285  -0.0883 775  THR A CG2 
1725 N N   . PHE A 239 ? 0.5572 0.5407 0.3663 -0.0950 0.0364  -0.0629 776  PHE A N   
1726 C CA  . PHE A 239 ? 0.4979 0.4751 0.3238 -0.0811 0.0297  -0.0493 776  PHE A CA  
1727 C C   . PHE A 239 ? 0.5002 0.4758 0.3568 -0.0671 0.0329  -0.0540 776  PHE A C   
1728 O O   . PHE A 239 ? 0.4949 0.4722 0.3659 -0.0659 0.0450  -0.0668 776  PHE A O   
1729 C CB  . PHE A 239 ? 0.5277 0.5031 0.3509 -0.0822 0.0367  -0.0458 776  PHE A CB  
1730 C CG  . PHE A 239 ? 0.4779 0.4521 0.2729 -0.0940 0.0302  -0.0344 776  PHE A CG  
1731 C CD1 . PHE A 239 ? 0.5259 0.5020 0.2968 -0.1050 0.0199  -0.0294 776  PHE A CD1 
1732 C CD2 . PHE A 239 ? 0.5074 0.4786 0.3007 -0.0949 0.0335  -0.0277 776  PHE A CD2 
1733 C CE1 . PHE A 239 ? 0.5677 0.5420 0.3123 -0.1169 0.0126  -0.0166 776  PHE A CE1 
1734 C CE2 . PHE A 239 ? 0.5987 0.5677 0.3667 -0.1067 0.0273  -0.0156 776  PHE A CE2 
1735 C CZ  . PHE A 239 ? 0.5922 0.5625 0.3354 -0.1178 0.0165  -0.0093 776  PHE A CZ  
1736 N N   . ASP A 240 ? 0.4188 0.3912 0.2867 -0.0569 0.0223  -0.0433 777  ASP A N   
1737 C CA  . ASP A 240 ? 0.4821 0.4532 0.3759 -0.0449 0.0242  -0.0448 777  ASP A CA  
1738 C C   . ASP A 240 ? 0.4769 0.4454 0.3772 -0.0357 0.0135  -0.0318 777  ASP A C   
1739 O O   . ASP A 240 ? 0.4416 0.4088 0.3297 -0.0381 0.0038  -0.0227 777  ASP A O   
1740 C CB  . ASP A 240 ? 0.6325 0.6066 0.5348 -0.0466 0.0258  -0.0543 777  ASP A CB  
1741 C CG  . ASP A 240 ? 0.7953 0.7676 0.7237 -0.0379 0.0326  -0.0588 777  ASP A CG  
1742 O OD1 . ASP A 240 ? 0.8332 0.8029 0.7722 -0.0300 0.0345  -0.0533 777  ASP A OD1 
1743 O OD2 . ASP A 240 ? 0.8042 0.7773 0.7424 -0.0397 0.0353  -0.0673 777  ASP A OD2 
1744 N N   . LEU A 241 ? 0.3783 0.3462 0.2987 -0.0257 0.0152  -0.0313 778  LEU A N   
1745 C CA  . LEU A 241 ? 0.3676 0.3342 0.2956 -0.0171 0.0079  -0.0219 778  LEU A CA  
1746 C C   . LEU A 241 ? 0.4359 0.4051 0.3611 -0.0181 -0.0032 -0.0169 778  LEU A C   
1747 O O   . LEU A 241 ? 0.3864 0.3537 0.3113 -0.0146 -0.0111 -0.0088 778  LEU A O   
1748 C CB  . LEU A 241 ? 0.3387 0.3062 0.2856 -0.0091 0.0121  -0.0231 778  LEU A CB  
1749 C CG  . LEU A 241 ? 0.4602 0.4285 0.4152 -0.0013 0.0067  -0.0163 778  LEU A CG  
1750 C CD1 . LEU A 241 ? 0.4216 0.3853 0.3734 0.0021  0.0067  -0.0121 778  LEU A CD1 
1751 C CD2 . LEU A 241 ? 0.5276 0.4992 0.4978 0.0031  0.0103  -0.0175 778  LEU A CD2 
1752 N N   . MET A 242 ? 0.4251 0.3989 0.3508 -0.0228 -0.0044 -0.0221 779  MET A N   
1753 C CA  . MET A 242 ? 0.3935 0.3718 0.3217 -0.0230 -0.0156 -0.0174 779  MET A CA  
1754 C C   . MET A 242 ? 0.4454 0.4243 0.3536 -0.0329 -0.0249 -0.0137 779  MET A C   
1755 O O   . MET A 242 ? 0.4651 0.4471 0.3761 -0.0325 -0.0372 -0.0067 779  MET A O   
1756 C CB  . MET A 242 ? 0.3644 0.3484 0.3059 -0.0233 -0.0138 -0.0239 779  MET A CB  
1757 C CG  . MET A 242 ? 0.3685 0.3528 0.3297 -0.0146 -0.0069 -0.0245 779  MET A CG  
1758 S SD  . MET A 242 ? 0.4226 0.4101 0.3966 -0.0047 -0.0134 -0.0157 779  MET A SD  
1759 C CE  . MET A 242 ? 0.3893 0.3871 0.3779 -0.0062 -0.0198 -0.0166 779  MET A CE  
1760 N N   . THR A 243 ? 0.4229 0.3997 0.3113 -0.0423 -0.0195 -0.0178 780  THR A N   
1761 C CA  . THR A 243 ? 0.4478 0.4257 0.3125 -0.0544 -0.0282 -0.0134 780  THR A CA  
1762 C C   . THR A 243 ? 0.4669 0.4387 0.3203 -0.0552 -0.0338 -0.0013 780  THR A C   
1763 O O   . THR A 243 ? 0.4556 0.4273 0.2937 -0.0629 -0.0462 0.0083  780  THR A O   
1764 C CB  . THR A 243 ? 0.4638 0.4445 0.3106 -0.0670 -0.0184 -0.0261 780  THR A CB  
1765 O OG1 . THR A 243 ? 0.5314 0.5086 0.3808 -0.0650 -0.0039 -0.0325 780  THR A OG1 
1766 C CG2 . THR A 243 ? 0.5173 0.5030 0.3744 -0.0683 -0.0157 -0.0377 780  THR A CG2 
1767 N N   . LEU A 244 ? 0.4292 0.3957 0.2898 -0.0485 -0.0258 -0.0010 781  LEU A N   
1768 C CA  . LEU A 244 ? 0.4383 0.3977 0.2924 -0.0484 -0.0312 0.0104  781  LEU A CA  
1769 C C   . LEU A 244 ? 0.4281 0.3846 0.3008 -0.0375 -0.0429 0.0198  781  LEU A C   
1770 O O   . LEU A 244 ? 0.3932 0.3541 0.2849 -0.0291 -0.0434 0.0161  781  LEU A O   
1771 C CB  . LEU A 244 ? 0.4112 0.3669 0.2682 -0.0457 -0.0184 0.0062  781  LEU A CB  
1772 C CG  . LEU A 244 ? 0.4838 0.4422 0.3242 -0.0571 -0.0064 -0.0022 781  LEU A CG  
1773 C CD1 . LEU A 244 ? 0.4197 0.3769 0.2729 -0.0514 0.0060  -0.0081 781  LEU A CD1 
1774 C CD2 . LEU A 244 ? 0.4781 0.4343 0.2923 -0.0705 -0.0117 0.0068  781  LEU A CD2 
1775 N N   . HIS A 245 ? 0.4066 0.3557 0.2753 -0.0381 -0.0518 0.0316  782  HIS A N   
1776 C CA  . HIS A 245 ? 0.3620 0.3076 0.2517 -0.0275 -0.0627 0.0392  782  HIS A CA  
1777 C C   . HIS A 245 ? 0.3994 0.3415 0.3067 -0.0161 -0.0537 0.0341  782  HIS A C   
1778 O O   . HIS A 245 ? 0.3804 0.3172 0.2804 -0.0180 -0.0464 0.0332  782  HIS A O   
1779 C CB  . HIS A 245 ? 0.3664 0.3039 0.2476 -0.0328 -0.0768 0.0544  782  HIS A CB  
1780 C CG  . HIS A 245 ? 0.3825 0.3182 0.2870 -0.0239 -0.0916 0.0626  782  HIS A CG  
1781 N ND1 . HIS A 245 ? 0.3778 0.3101 0.3086 -0.0104 -0.0896 0.0597  782  HIS A ND1 
1782 C CD2 . HIS A 245 ? 0.4134 0.3511 0.3206 -0.0267 -0.1086 0.0730  782  HIS A CD2 
1783 C CE1 . HIS A 245 ? 0.3823 0.3148 0.3336 -0.0046 -0.1035 0.0667  782  HIS A CE1 
1784 N NE2 . HIS A 245 ? 0.4299 0.3655 0.3685 -0.0139 -0.1161 0.0758  782  HIS A NE2 
1785 N N   . PRO A 246 ? 0.3571 0.3031 0.2872 -0.0053 -0.0539 0.0303  783  PRO A N   
1786 C CA  . PRO A 246 ? 0.4139 0.3578 0.3570 0.0037  -0.0451 0.0245  783  PRO A CA  
1787 C C   . PRO A 246 ? 0.3978 0.3308 0.3424 0.0057  -0.0485 0.0302  783  PRO A C   
1788 O O   . PRO A 246 ? 0.3880 0.3178 0.3325 0.0078  -0.0402 0.0259  783  PRO A O   
1789 C CB  . PRO A 246 ? 0.3582 0.3095 0.3237 0.0127  -0.0463 0.0205  783  PRO A CB  
1790 C CG  . PRO A 246 ? 0.3776 0.3320 0.3472 0.0104  -0.0599 0.0274  783  PRO A CG  
1791 C CD  . PRO A 246 ? 0.3333 0.2874 0.2778 -0.0019 -0.0616 0.0303  783  PRO A CD  
1792 N N   . ILE A 247 ? 0.3754 0.3021 0.3229 0.0048  -0.0616 0.0404  784  ILE A N   
1793 C CA  . ILE A 247 ? 0.3819 0.2960 0.3309 0.0053  -0.0655 0.0468  784  ILE A CA  
1794 C C   . ILE A 247 ? 0.4163 0.3263 0.3430 -0.0045 -0.0585 0.0481  784  ILE A C   
1795 O O   . ILE A 247 ? 0.3959 0.3002 0.3248 -0.0028 -0.0526 0.0454  784  ILE A O   
1796 C CB  . ILE A 247 ? 0.3838 0.2907 0.3390 0.0042  -0.0827 0.0603  784  ILE A CB  
1797 C CG1 . ILE A 247 ? 0.4500 0.3619 0.4340 0.0151  -0.0897 0.0581  784  ILE A CG1 
1798 C CG2 . ILE A 247 ? 0.3612 0.2532 0.3174 0.0031  -0.0868 0.0678  784  ILE A CG2 
1799 C CD1 . ILE A 247 ? 0.4166 0.3216 0.4118 0.0147  -0.1090 0.0728  784  ILE A CD1 
1800 N N   . GLU A 248 ? 0.4216 0.3354 0.3271 -0.0157 -0.0588 0.0514  785  GLU A N   
1801 C CA  . GLU A 248 ? 0.4233 0.3345 0.3085 -0.0265 -0.0518 0.0527  785  GLU A CA  
1802 C C   . GLU A 248 ? 0.4411 0.3585 0.3272 -0.0247 -0.0359 0.0398  785  GLU A C   
1803 O O   . GLU A 248 ? 0.3991 0.3136 0.2798 -0.0289 -0.0291 0.0392  785  GLU A O   
1804 C CB  . GLU A 248 ? 0.4444 0.3588 0.3050 -0.0405 -0.0559 0.0587  785  GLU A CB  
1805 C CG  . GLU A 248 ? 0.3974 0.3062 0.2372 -0.0536 -0.0542 0.0663  785  GLU A CG  
1806 C CD  . GLU A 248 ? 0.5075 0.4024 0.3553 -0.0517 -0.0648 0.0794  785  GLU A CD  
1807 O OE1 . GLU A 248 ? 0.4896 0.3789 0.3380 -0.0533 -0.0582 0.0790  785  GLU A OE1 
1808 O OE2 . GLU A 248 ? 0.4787 0.3682 0.3351 -0.0485 -0.0803 0.0898  785  GLU A OE2 
1809 N N   . ILE A 249 ? 0.3475 0.2736 0.2423 -0.0189 -0.0306 0.0305  786  ILE A N   
1810 C CA  . ILE A 249 ? 0.4088 0.3396 0.3097 -0.0156 -0.0179 0.0203  786  ILE A CA  
1811 C C   . ILE A 249 ? 0.4158 0.3409 0.3279 -0.0090 -0.0167 0.0203  786  ILE A C   
1812 O O   . ILE A 249 ? 0.3831 0.3077 0.2933 -0.0116 -0.0097 0.0178  786  ILE A O   
1813 C CB  . ILE A 249 ? 0.3284 0.2674 0.2397 -0.0098 -0.0147 0.0129  786  ILE A CB  
1814 C CG1 . ILE A 249 ? 0.3403 0.2852 0.2404 -0.0178 -0.0133 0.0096  786  ILE A CG1 
1815 C CG2 . ILE A 249 ? 0.3271 0.2690 0.2484 -0.0047 -0.0048 0.0056  786  ILE A CG2 
1816 C CD1 . ILE A 249 ? 0.3681 0.3198 0.2801 -0.0128 -0.0129 0.0042  786  ILE A CD1 
1817 N N   . ALA A 250 ? 0.4036 0.3249 0.3286 -0.0009 -0.0236 0.0224  787  ALA A N   
1818 C CA  . ALA A 250 ? 0.3429 0.2591 0.2780 0.0047  -0.0222 0.0202  787  ALA A CA  
1819 C C   . ALA A 250 ? 0.3759 0.2821 0.3045 -0.0013 -0.0250 0.0267  787  ALA A C   
1820 O O   . ALA A 250 ? 0.3960 0.3004 0.3264 -0.0016 -0.0199 0.0234  787  ALA A O   
1821 C CB  . ALA A 250 ? 0.3474 0.2623 0.2991 0.0140  -0.0275 0.0186  787  ALA A CB  
1822 N N   . ARG A 251 ? 0.3595 0.2591 0.2807 -0.0070 -0.0338 0.0367  788  ARG A N   
1823 C CA  . ARG A 251 ? 0.3477 0.2371 0.2616 -0.0145 -0.0367 0.0448  788  ARG A CA  
1824 C C   . ARG A 251 ? 0.4393 0.3340 0.3401 -0.0235 -0.0259 0.0417  788  ARG A C   
1825 O O   . ARG A 251 ? 0.4106 0.3007 0.3133 -0.0262 -0.0227 0.0419  788  ARG A O   
1826 C CB  . ARG A 251 ? 0.3972 0.2799 0.3021 -0.0213 -0.0487 0.0584  788  ARG A CB  
1827 C CG  . ARG A 251 ? 0.4077 0.2826 0.3308 -0.0129 -0.0618 0.0640  788  ARG A CG  
1828 C CD  . ARG A 251 ? 0.4483 0.3198 0.3606 -0.0208 -0.0749 0.0786  788  ARG A CD  
1829 N NE  . ARG A 251 ? 0.4072 0.2699 0.3405 -0.0134 -0.0895 0.0864  788  ARG A NE  
1830 C CZ  . ARG A 251 ? 0.4452 0.3038 0.3748 -0.0186 -0.1046 0.1011  788  ARG A CZ  
1831 N NH1 . ARG A 251 ? 0.4680 0.3311 0.3692 -0.0325 -0.1061 0.1088  788  ARG A NH1 
1832 N NH2 . ARG A 251 ? 0.4669 0.3174 0.4217 -0.0104 -0.1184 0.1078  788  ARG A NH2 
1833 N N   . GLN A 252 ? 0.3982 0.3024 0.2870 -0.0291 -0.0201 0.0385  789  GLN A N   
1834 C CA  . GLN A 252 ? 0.4047 0.3148 0.2836 -0.0383 -0.0090 0.0345  789  GLN A CA  
1835 C C   . GLN A 252 ? 0.4120 0.3279 0.3054 -0.0318 0.0002  0.0243  789  GLN A C   
1836 O O   . GLN A 252 ? 0.3889 0.3064 0.2830 -0.0368 0.0070  0.0224  789  GLN A O   
1837 C CB  . GLN A 252 ? 0.3750 0.2939 0.2387 -0.0463 -0.0045 0.0313  789  GLN A CB  
1838 C CG  . GLN A 252 ? 0.4060 0.3209 0.2505 -0.0562 -0.0140 0.0425  789  GLN A CG  
1839 C CD  . GLN A 252 ? 0.4821 0.3894 0.3145 -0.0672 -0.0160 0.0531  789  GLN A CD  
1840 O OE1 . GLN A 252 ? 0.5062 0.4170 0.3362 -0.0733 -0.0050 0.0488  789  GLN A OE1 
1841 N NE2 . GLN A 252 ? 0.4912 0.3884 0.3182 -0.0699 -0.0303 0.0677  789  GLN A NE2 
1842 N N   . LEU A 253 ? 0.3795 0.2991 0.2850 -0.0215 0.0001  0.0184  790  LEU A N   
1843 C CA  . LEU A 253 ? 0.4141 0.3383 0.3324 -0.0161 0.0062  0.0114  790  LEU A CA  
1844 C C   . LEU A 253 ? 0.4462 0.3631 0.3711 -0.0140 0.0026  0.0135  790  LEU A C   
1845 O O   . LEU A 253 ? 0.3846 0.3046 0.3159 -0.0149 0.0071  0.0101  790  LEU A O   
1846 C CB  . LEU A 253 ? 0.3602 0.2898 0.2877 -0.0074 0.0064  0.0064  790  LEU A CB  
1847 C CG  . LEU A 253 ? 0.3242 0.2619 0.2507 -0.0093 0.0125  0.0014  790  LEU A CG  
1848 C CD1 . LEU A 253 ? 0.3086 0.2499 0.2431 -0.0018 0.0109  -0.0010 790  LEU A CD1 
1849 C CD2 . LEU A 253 ? 0.3621 0.3058 0.2955 -0.0117 0.0215  -0.0041 790  LEU A CD2 
1850 N N   . THR A 254 ? 0.4227 0.3299 0.3479 -0.0118 -0.0060 0.0189  791  THR A N   
1851 C CA  . THR A 254 ? 0.3922 0.2909 0.3248 -0.0103 -0.0095 0.0195  791  THR A CA  
1852 C C   . THR A 254 ? 0.4605 0.3552 0.3875 -0.0204 -0.0077 0.0243  791  THR A C   
1853 O O   . THR A 254 ? 0.4005 0.2946 0.3343 -0.0212 -0.0055 0.0212  791  THR A O   
1854 C CB  . THR A 254 ? 0.3746 0.2632 0.3132 -0.0051 -0.0190 0.0231  791  THR A CB  
1855 O OG1 . THR A 254 ? 0.3529 0.2477 0.2993 0.0040  -0.0186 0.0167  791  THR A OG1 
1856 C CG2 . THR A 254 ? 0.3675 0.2454 0.3149 -0.0045 -0.0224 0.0226  791  THR A CG2 
1857 N N   . LEU A 255 ? 0.4164 0.3087 0.3302 -0.0293 -0.0087 0.0322  792  LEU A N   
1858 C CA  . LEU A 255 ? 0.4576 0.3480 0.3645 -0.0408 -0.0051 0.0369  792  LEU A CA  
1859 C C   . LEU A 255 ? 0.4004 0.3035 0.3118 -0.0433 0.0066  0.0283  792  LEU A C   
1860 O O   . LEU A 255 ? 0.4280 0.3311 0.3446 -0.0484 0.0099  0.0281  792  LEU A O   
1861 C CB  . LEU A 255 ? 0.4095 0.2980 0.2975 -0.0518 -0.0071 0.0465  792  LEU A CB  
1862 C CG  . LEU A 255 ? 0.4919 0.3666 0.3766 -0.0519 -0.0210 0.0589  792  LEU A CG  
1863 C CD1 . LEU A 255 ? 0.5193 0.3958 0.3824 -0.0630 -0.0236 0.0681  792  LEU A CD1 
1864 C CD2 . LEU A 255 ? 0.5162 0.3774 0.4076 -0.0554 -0.0259 0.0661  792  LEU A CD2 
1865 N N   . LEU A 256 ? 0.3525 0.2664 0.2646 -0.0398 0.0125  0.0212  793  LEU A N   
1866 C CA  . LEU A 256 ? 0.3738 0.2998 0.2950 -0.0410 0.0228  0.0129  793  LEU A CA  
1867 C C   . LEU A 256 ? 0.4540 0.3812 0.3921 -0.0338 0.0210  0.0089  793  LEU A C   
1868 O O   . LEU A 256 ? 0.3898 0.3222 0.3373 -0.0375 0.0255  0.0065  793  LEU A O   
1869 C CB  . LEU A 256 ? 0.3756 0.3106 0.2962 -0.0384 0.0282  0.0064  793  LEU A CB  
1870 C CG  . LEU A 256 ? 0.3897 0.3367 0.3256 -0.0368 0.0378  -0.0030 793  LEU A CG  
1871 C CD1 . LEU A 256 ? 0.5687 0.5212 0.5075 -0.0464 0.0462  -0.0047 793  LEU A CD1 
1872 C CD2 . LEU A 256 ? 0.3958 0.3487 0.3288 -0.0365 0.0430  -0.0090 793  LEU A CD2 
1873 N N   . GLU A 257 ? 0.3603 0.2838 0.3022 -0.0243 0.0144  0.0081  794  GLU A N   
1874 C CA  . GLU A 257 ? 0.3996 0.3252 0.3536 -0.0189 0.0123  0.0041  794  GLU A CA  
1875 C C   . GLU A 257 ? 0.3931 0.3106 0.3494 -0.0225 0.0081  0.0062  794  GLU A C   
1876 O O   . GLU A 257 ? 0.4177 0.3395 0.3837 -0.0232 0.0083  0.0030  794  GLU A O   
1877 C CB  . GLU A 257 ? 0.3240 0.2492 0.2789 -0.0097 0.0080  0.0018  794  GLU A CB  
1878 C CG  . GLU A 257 ? 0.3483 0.2823 0.3044 -0.0068 0.0124  -0.0005 794  GLU A CG  
1879 C CD  . GLU A 257 ? 0.4018 0.3365 0.3581 0.0008  0.0093  -0.0019 794  GLU A CD  
1880 O OE1 . GLU A 257 ? 0.3967 0.3373 0.3549 0.0027  0.0124  -0.0033 794  GLU A OE1 
1881 O OE2 . GLU A 257 ? 0.4337 0.3632 0.3894 0.0042  0.0046  -0.0025 794  GLU A OE2 
1882 N N   . SER A 258 ? 0.3749 0.2803 0.3240 -0.0252 0.0033  0.0120  795  SER A N   
1883 C CA  . SER A 258 ? 0.3956 0.2912 0.3482 -0.0299 -0.0006 0.0146  795  SER A CA  
1884 C C   . SER A 258 ? 0.4790 0.3805 0.4340 -0.0399 0.0057  0.0157  795  SER A C   
1885 O O   . SER A 258 ? 0.3963 0.2972 0.3607 -0.0426 0.0046  0.0136  795  SER A O   
1886 C CB  . SER A 258 ? 0.3931 0.2739 0.3393 -0.0316 -0.0075 0.0228  795  SER A CB  
1887 O OG  . SER A 258 ? 0.4270 0.2970 0.3765 -0.0385 -0.0108 0.0274  795  SER A OG  
1888 N N   . ASP A 259 ? 0.4096 0.3175 0.3566 -0.0464 0.0126  0.0183  796  ASP A N   
1889 C CA  . ASP A 259 ? 0.4901 0.4063 0.4412 -0.0565 0.0209  0.0178  796  ASP A CA  
1890 C C   . ASP A 259 ? 0.4828 0.4124 0.4520 -0.0525 0.0249  0.0094  796  ASP A C   
1891 O O   . ASP A 259 ? 0.4334 0.3671 0.4140 -0.0578 0.0267  0.0083  796  ASP A O   
1892 C CB  . ASP A 259 ? 0.5253 0.4477 0.4633 -0.0647 0.0293  0.0196  796  ASP A CB  
1893 C CG  . ASP A 259 ? 0.6530 0.5633 0.5725 -0.0735 0.0248  0.0309  796  ASP A CG  
1894 O OD1 . ASP A 259 ? 0.6717 0.5684 0.5927 -0.0743 0.0162  0.0378  796  ASP A OD1 
1895 O OD2 . ASP A 259 ? 0.6488 0.5630 0.5525 -0.0803 0.0293  0.0331  796  ASP A OD2 
1896 N N   . LEU A 260 ? 0.3511 0.2880 0.3245 -0.0437 0.0256  0.0043  797  LEU A N   
1897 C CA  . LEU A 260 ? 0.3686 0.3179 0.3607 -0.0399 0.0276  -0.0016 797  LEU A CA  
1898 C C   . LEU A 260 ? 0.4114 0.3576 0.4111 -0.0374 0.0190  -0.0020 797  LEU A C   
1899 O O   . LEU A 260 ? 0.3818 0.3363 0.3969 -0.0402 0.0193  -0.0041 797  LEU A O   
1900 C CB  . LEU A 260 ? 0.3518 0.3069 0.3463 -0.0315 0.0285  -0.0049 797  LEU A CB  
1901 C CG  . LEU A 260 ? 0.3881 0.3481 0.3778 -0.0346 0.0378  -0.0073 797  LEU A CG  
1902 C CD1 . LEU A 260 ? 0.4195 0.3829 0.4131 -0.0261 0.0373  -0.0103 797  LEU A CD1 
1903 C CD2 . LEU A 260 ? 0.4137 0.3852 0.4169 -0.0419 0.0481  -0.0119 797  LEU A CD2 
1904 N N   . TYR A 261 ? 0.3593 0.2943 0.3493 -0.0326 0.0115  -0.0009 798  TYR A N   
1905 C CA  . TYR A 261 ? 0.3811 0.3124 0.3756 -0.0313 0.0040  -0.0034 798  TYR A CA  
1906 C C   . TYR A 261 ? 0.4180 0.3448 0.4179 -0.0402 0.0033  -0.0020 798  TYR A C   
1907 O O   . TYR A 261 ? 0.4066 0.3387 0.4176 -0.0424 0.0001  -0.0052 798  TYR A O   
1908 C CB  . TYR A 261 ? 0.4025 0.3225 0.3866 -0.0252 -0.0016 -0.0044 798  TYR A CB  
1909 C CG  . TYR A 261 ? 0.4498 0.3656 0.4362 -0.0240 -0.0082 -0.0098 798  TYR A CG  
1910 C CD1 . TYR A 261 ? 0.4131 0.3166 0.4010 -0.0285 -0.0118 -0.0105 798  TYR A CD1 
1911 C CD2 . TYR A 261 ? 0.4770 0.4009 0.4632 -0.0195 -0.0109 -0.0144 798  TYR A CD2 
1912 C CE1 . TYR A 261 ? 0.4230 0.3229 0.4131 -0.0282 -0.0172 -0.0179 798  TYR A CE1 
1913 C CE2 . TYR A 261 ? 0.4579 0.3792 0.4432 -0.0201 -0.0164 -0.0209 798  TYR A CE2 
1914 C CZ  . TYR A 261 ? 0.4604 0.3698 0.4479 -0.0243 -0.0191 -0.0238 798  TYR A CZ  
1915 O OH  . TYR A 261 ? 0.4655 0.3725 0.4520 -0.0255 -0.0239 -0.0325 798  TYR A OH  
1916 N N   . ARG A 262 ? 0.3809 0.2981 0.3730 -0.0463 0.0055  0.0035  799  ARG A N   
1917 C CA  . ARG A 262 ? 0.3553 0.2660 0.3519 -0.0559 0.0047  0.0064  799  ARG A CA  
1918 C C   . ARG A 262 ? 0.3878 0.3136 0.3990 -0.0628 0.0108  0.0044  799  ARG A C   
1919 O O   . ARG A 262 ? 0.3872 0.3118 0.4082 -0.0693 0.0084  0.0039  799  ARG A O   
1920 C CB  . ARG A 262 ? 0.4217 0.3202 0.4057 -0.0624 0.0057  0.0154  799  ARG A CB  
1921 C CG  . ARG A 262 ? 0.5787 0.4709 0.5665 -0.0748 0.0062  0.0208  799  ARG A CG  
1922 C CD  . ARG A 262 ? 0.6670 0.5473 0.6401 -0.0827 0.0062  0.0324  799  ARG A CD  
1923 N NE  . ARG A 262 ? 0.8086 0.6985 0.7687 -0.0846 0.0138  0.0346  799  ARG A NE  
1924 C CZ  . ARG A 262 ? 0.8086 0.7122 0.7676 -0.0941 0.0251  0.0340  799  ARG A CZ  
1925 N NH1 . ARG A 262 ? 0.6444 0.5547 0.6164 -0.1024 0.0299  0.0323  799  ARG A NH1 
1926 N NH2 . ARG A 262 ? 0.8321 0.7436 0.7783 -0.0958 0.0320  0.0339  799  ARG A NH2 
1927 N N   . LYS A 263 ? 0.3673 0.3074 0.3829 -0.0618 0.0187  0.0025  800  LYS A N   
1928 C CA  . LYS A 263 ? 0.3235 0.2792 0.3573 -0.0684 0.0260  -0.0002 800  LYS A CA  
1929 C C   . LYS A 263 ? 0.3611 0.3288 0.4154 -0.0635 0.0209  -0.0053 800  LYS A C   
1930 O O   . LYS A 263 ? 0.3743 0.3562 0.4490 -0.0681 0.0256  -0.0077 800  LYS A O   
1931 C CB  . LYS A 263 ? 0.4452 0.4115 0.4781 -0.0703 0.0381  -0.0018 800  LYS A CB  
1932 C CG  . LYS A 263 ? 0.5028 0.4609 0.5151 -0.0794 0.0440  0.0040  800  LYS A CG  
1933 C CD  . LYS A 263 ? 0.5711 0.5411 0.5808 -0.0821 0.0565  -0.0003 800  LYS A CD  
1934 C CE  . LYS A 263 ? 0.7866 0.7501 0.7727 -0.0939 0.0619  0.0061  800  LYS A CE  
1935 N NZ  . LYS A 263 ? 0.8610 0.8374 0.8430 -0.0986 0.0755  -0.0004 800  LYS A NZ  
1936 N N   . VAL A 264 ? 0.3586 0.3224 0.4088 -0.0550 0.0115  -0.0067 801  VAL A N   
1937 C CA  . VAL A 264 ? 0.3161 0.2919 0.3832 -0.0517 0.0050  -0.0096 801  VAL A CA  
1938 C C   . VAL A 264 ? 0.3501 0.3255 0.4261 -0.0588 -0.0014 -0.0109 801  VAL A C   
1939 O O   . VAL A 264 ? 0.3531 0.3143 0.4171 -0.0610 -0.0064 -0.0113 801  VAL A O   
1940 C CB  . VAL A 264 ? 0.3562 0.3290 0.4126 -0.0424 -0.0025 -0.0101 801  VAL A CB  
1941 C CG1 . VAL A 264 ? 0.3137 0.2984 0.3844 -0.0409 -0.0114 -0.0110 801  VAL A CG1 
1942 C CG2 . VAL A 264 ? 0.3539 0.3283 0.4049 -0.0360 0.0037  -0.0090 801  VAL A CG2 
1943 N N   . GLN A 265 ? 0.3094 0.3004 0.4093 -0.0625 -0.0013 -0.0121 802  GLN A N   
1944 C CA  . GLN A 265 ? 0.3145 0.3074 0.4255 -0.0696 -0.0086 -0.0138 802  GLN A CA  
1945 C C   . GLN A 265 ? 0.3160 0.3152 0.4307 -0.0653 -0.0217 -0.0154 802  GLN A C   
1946 O O   . GLN A 265 ? 0.3197 0.3296 0.4421 -0.0587 -0.0239 -0.0138 802  GLN A O   
1947 C CB  . GLN A 265 ? 0.3140 0.3222 0.4516 -0.0775 -0.0019 -0.0142 802  GLN A CB  
1948 C CG  . GLN A 265 ? 0.4019 0.4062 0.5344 -0.0849 0.0120  -0.0124 802  GLN A CG  
1949 C CD  . GLN A 265 ? 0.6183 0.6017 0.7298 -0.0908 0.0099  -0.0091 802  GLN A CD  
1950 O OE1 . GLN A 265 ? 0.5074 0.4850 0.6226 -0.0960 0.0021  -0.0101 802  GLN A OE1 
1951 N NE2 . GLN A 265 ? 0.6012 0.5729 0.6918 -0.0902 0.0158  -0.0051 802  GLN A NE2 
1952 N N   . PRO A 266 ? 0.3289 0.3219 0.4385 -0.0701 -0.0310 -0.0186 803  PRO A N   
1953 C CA  . PRO A 266 ? 0.3586 0.3583 0.4673 -0.0685 -0.0442 -0.0204 803  PRO A CA  
1954 C C   . PRO A 266 ? 0.3666 0.3874 0.5013 -0.0681 -0.0501 -0.0171 803  PRO A C   
1955 O O   . PRO A 266 ? 0.3291 0.3562 0.4604 -0.0634 -0.0590 -0.0146 803  PRO A O   
1956 C CB  . PRO A 266 ? 0.4149 0.4055 0.5190 -0.0770 -0.0508 -0.0262 803  PRO A CB  
1957 C CG  . PRO A 266 ? 0.4878 0.4600 0.5807 -0.0785 -0.0419 -0.0265 803  PRO A CG  
1958 C CD  . PRO A 266 ? 0.4236 0.4010 0.5251 -0.0775 -0.0300 -0.0206 803  PRO A CD  
1959 N N   . SER A 267 ? 0.2897 0.3221 0.4517 -0.0732 -0.0458 -0.0166 804  SER A N   
1960 C CA  . SER A 267 ? 0.3479 0.4011 0.5401 -0.0720 -0.0524 -0.0136 804  SER A CA  
1961 C C   . SER A 267 ? 0.3159 0.3751 0.5147 -0.0618 -0.0488 -0.0095 804  SER A C   
1962 O O   . SER A 267 ? 0.3257 0.3994 0.5469 -0.0586 -0.0579 -0.0054 804  SER A O   
1963 C CB  . SER A 267 ? 0.3235 0.3897 0.5477 -0.0794 -0.0463 -0.0153 804  SER A CB  
1964 O OG  . SER A 267 ? 0.3238 0.3893 0.5519 -0.0785 -0.0287 -0.0162 804  SER A OG  
1965 N N   . GLU A 268 ? 0.2844 0.3327 0.4659 -0.0569 -0.0368 -0.0101 805  GLU A N   
1966 C CA  . GLU A 268 ? 0.2804 0.3323 0.4665 -0.0476 -0.0336 -0.0071 805  GLU A CA  
1967 C C   . GLU A 268 ? 0.3260 0.3757 0.4974 -0.0424 -0.0467 -0.0022 805  GLU A C   
1968 O O   . GLU A 268 ? 0.3294 0.3844 0.5112 -0.0356 -0.0483 0.0022  805  GLU A O   
1969 C CB  . GLU A 268 ? 0.2741 0.3143 0.4418 -0.0452 -0.0188 -0.0094 805  GLU A CB  
1970 C CG  . GLU A 268 ? 0.3005 0.3426 0.4769 -0.0525 -0.0050 -0.0133 805  GLU A CG  
1971 C CD  . GLU A 268 ? 0.3237 0.3565 0.4817 -0.0515 0.0086  -0.0147 805  GLU A CD  
1972 O OE1 . GLU A 268 ? 0.3170 0.3508 0.4745 -0.0442 0.0119  -0.0148 805  GLU A OE1 
1973 O OE2 . GLU A 268 ? 0.3705 0.3951 0.5151 -0.0589 0.0154  -0.0151 805  GLU A OE2 
1974 N N   . LEU A 269 ? 0.3194 0.3609 0.4670 -0.0463 -0.0554 -0.0034 806  LEU A N   
1975 C CA  . LEU A 269 ? 0.3680 0.4075 0.4958 -0.0440 -0.0665 0.0000  806  LEU A CA  
1976 C C   . LEU A 269 ? 0.3879 0.4396 0.5249 -0.0492 -0.0835 0.0036  806  LEU A C   
1977 O O   . LEU A 269 ? 0.4887 0.5430 0.6137 -0.0482 -0.0939 0.0091  806  LEU A O   
1978 C CB  . LEU A 269 ? 0.3707 0.3938 0.4647 -0.0455 -0.0637 -0.0060 806  LEU A CB  
1979 C CG  . LEU A 269 ? 0.4099 0.4213 0.4930 -0.0400 -0.0497 -0.0075 806  LEU A CG  
1980 C CD1 . LEU A 269 ? 0.5068 0.5036 0.5753 -0.0438 -0.0444 -0.0138 806  LEU A CD1 
1981 C CD2 . LEU A 269 ? 0.4922 0.5005 0.5577 -0.0337 -0.0507 -0.0047 806  LEU A CD2 
1982 N N   . VAL A 270 ? 0.3368 0.3967 0.4949 -0.0557 -0.0870 0.0013  807  VAL A N   
1983 C CA  . VAL A 270 ? 0.3190 0.3905 0.4846 -0.0624 -0.1045 0.0039  807  VAL A CA  
1984 C C   . VAL A 270 ? 0.3510 0.4391 0.5467 -0.0582 -0.1144 0.0143  807  VAL A C   
1985 O O   . VAL A 270 ? 0.3640 0.4587 0.5902 -0.0528 -0.1061 0.0157  807  VAL A O   
1986 C CB  . VAL A 270 ? 0.3257 0.4004 0.5061 -0.0714 -0.1047 -0.0026 807  VAL A CB  
1987 C CG1 . VAL A 270 ? 0.3404 0.4299 0.5333 -0.0789 -0.1243 0.0003  807  VAL A CG1 
1988 C CG2 . VAL A 270 ? 0.3293 0.3854 0.4812 -0.0759 -0.0974 -0.0120 807  VAL A CG2 
1989 N N   . GLY A 271 ? 0.4153 0.5104 0.6037 -0.0614 -0.1325 0.0214  808  GLY A N   
1990 C CA  . GLY A 271 ? 0.4731 0.5834 0.6922 -0.0580 -0.1453 0.0336  808  GLY A CA  
1991 C C   . GLY A 271 ? 0.4476 0.5542 0.6725 -0.0475 -0.1387 0.0402  808  GLY A C   
1992 O O   . GLY A 271 ? 0.3573 0.4748 0.6182 -0.0425 -0.1449 0.0487  808  GLY A O   
1993 N N   . SER A 272 ? 0.3647 0.4559 0.5578 -0.0441 -0.1264 0.0361  809  SER A N   
1994 C CA  . SER A 272 ? 0.4456 0.5315 0.6404 -0.0350 -0.1192 0.0411  809  SER A CA  
1995 C C   . SER A 272 ? 0.4677 0.5600 0.7046 -0.0280 -0.1093 0.0397  809  SER A C   
1996 O O   . SER A 272 ? 0.5381 0.6326 0.7945 -0.0211 -0.1105 0.0466  809  SER A O   
1997 C CB  . SER A 272 ? 0.5387 0.6284 0.7268 -0.0349 -0.1357 0.0552  809  SER A CB  
1998 O OG  . SER A 272 ? 0.6715 0.7548 0.8158 -0.0416 -0.1405 0.0543  809  SER A OG  
1999 N N   . VAL A 273 ? 0.4061 0.5015 0.6580 -0.0307 -0.0987 0.0300  810  VAL A N   
2000 C CA  . VAL A 273 ? 0.4035 0.5087 0.6980 -0.0260 -0.0889 0.0269  810  VAL A CA  
2001 C C   . VAL A 273 ? 0.3874 0.4838 0.6789 -0.0184 -0.0729 0.0234  810  VAL A C   
2002 O O   . VAL A 273 ? 0.4047 0.5090 0.7324 -0.0130 -0.0663 0.0214  810  VAL A O   
2003 C CB  . VAL A 273 ? 0.3906 0.5020 0.6999 -0.0324 -0.0792 0.0172  810  VAL A CB  
2004 C CG1 . VAL A 273 ? 0.4056 0.5324 0.7395 -0.0383 -0.0954 0.0209  810  VAL A CG1 
2005 C CG2 . VAL A 273 ? 0.2732 0.3692 0.5425 -0.0379 -0.0692 0.0099  810  VAL A CG2 
2006 N N   . TRP A 274 ? 0.2786 0.3594 0.5300 -0.0178 -0.0667 0.0217  811  TRP A N   
2007 C CA  . TRP A 274 ? 0.2924 0.3657 0.5412 -0.0116 -0.0524 0.0180  811  TRP A CA  
2008 C C   . TRP A 274 ? 0.3416 0.4158 0.6053 -0.0044 -0.0595 0.0266  811  TRP A C   
2009 O O   . TRP A 274 ? 0.3488 0.4183 0.6177 0.0009  -0.0484 0.0230  811  TRP A O   
2010 C CB  . TRP A 274 ? 0.3587 0.4161 0.5639 -0.0131 -0.0443 0.0140  811  TRP A CB  
2011 C CG  . TRP A 274 ? 0.3193 0.3687 0.4954 -0.0119 -0.0538 0.0207  811  TRP A CG  
2012 C CD1 . TRP A 274 ? 0.3841 0.4274 0.5511 -0.0065 -0.0522 0.0246  811  TRP A CD1 
2013 C CD2 . TRP A 274 ? 0.3198 0.3670 0.4710 -0.0174 -0.0649 0.0229  811  TRP A CD2 
2014 N NE1 . TRP A 274 ? 0.3772 0.4158 0.5158 -0.0086 -0.0613 0.0299  811  TRP A NE1 
2015 C CE2 . TRP A 274 ? 0.3784 0.4194 0.5059 -0.0153 -0.0687 0.0281  811  TRP A CE2 
2016 C CE3 . TRP A 274 ? 0.3476 0.3980 0.4948 -0.0248 -0.0717 0.0201  811  TRP A CE3 
2017 C CZ2 . TRP A 274 ? 0.4078 0.4466 0.5070 -0.0204 -0.0778 0.0297  811  TRP A CZ2 
2018 C CZ3 . TRP A 274 ? 0.4508 0.4979 0.5700 -0.0296 -0.0815 0.0210  811  TRP A CZ3 
2019 C CH2 . TRP A 274 ? 0.4611 0.5029 0.5561 -0.0275 -0.0839 0.0253  811  TRP A CH2 
2020 N N   . THR A 275 ? 0.3944 0.4744 0.6646 -0.0050 -0.0784 0.0383  812  THR A N   
2021 C CA  . THR A 275 ? 0.4338 0.5146 0.7216 0.0008  -0.0879 0.0495  812  THR A CA  
2022 C C   . THR A 275 ? 0.4003 0.4956 0.7408 0.0040  -0.0969 0.0543  812  THR A C   
2023 O O   . THR A 275 ? 0.4581 0.5542 0.8206 0.0092  -0.1067 0.0650  812  THR A O   
2024 C CB  . THR A 275 ? 0.3043 0.3810 0.5602 -0.0031 -0.1041 0.0620  812  THR A CB  
2025 O OG1 . THR A 275 ? 0.3902 0.4773 0.6494 -0.0099 -0.1204 0.0674  812  THR A OG1 
2026 C CG2 . THR A 275 ? 0.3628 0.4268 0.5703 -0.0062 -0.0948 0.0555  812  THR A CG2 
2027 N N   . LYS A 276 ? 0.4245 0.5315 0.7884 0.0010  -0.0946 0.0474  813  LYS A N   
2028 C CA  . LYS A 276 ? 0.4422 0.5652 0.8586 0.0035  -0.1055 0.0524  813  LYS A CA  
2029 C C   . LYS A 276 ? 0.4523 0.5825 0.9111 0.0089  -0.0870 0.0392  813  LYS A C   
2030 O O   . LYS A 276 ? 0.4529 0.5754 0.8964 0.0097  -0.0666 0.0271  813  LYS A O   
2031 C CB  . LYS A 276 ? 0.4631 0.5974 0.8800 -0.0049 -0.1190 0.0551  813  LYS A CB  
2032 C CG  . LYS A 276 ? 0.4546 0.5834 0.8292 -0.0116 -0.1372 0.0663  813  LYS A CG  
2033 C CD  . LYS A 276 ? 0.5280 0.6699 0.9100 -0.0202 -0.1529 0.0688  813  LYS A CD  
2034 C CE  . LYS A 276 ? 0.6606 0.7992 1.0023 -0.0281 -0.1720 0.0793  813  LYS A CE  
2035 N NZ  . LYS A 276 ? 0.7575 0.9110 1.1122 -0.0367 -0.1911 0.0836  813  LYS A NZ  
2036 N N   . GLU A 277 ? 0.4241 0.5707 0.9372 0.0119  -0.0947 0.0413  814  GLU A N   
2037 C CA  . GLU A 277 ? 0.5064 0.6624 1.0709 0.0183  -0.0797 0.0297  814  GLU A CA  
2038 C C   . GLU A 277 ? 0.3858 0.5418 0.9379 0.0141  -0.0528 0.0104  814  GLU A C   
2039 O O   . GLU A 277 ? 0.5869 0.7379 1.1431 0.0182  -0.0349 -0.0003 814  GLU A O   
2040 C CB  . GLU A 277 ? 0.6242 0.7984 1.2415 0.0194  -0.0927 0.0340  814  GLU A CB  
2041 C CG  . GLU A 277 ? 0.7993 0.9758 1.4572 0.0248  -0.0772 0.0215  814  GLU A CG  
2042 C CD  . GLU A 277 ? 0.9827 1.1679 1.6742 0.0248  -0.0914 0.0278  814  GLU A CD  
2043 O OE1 . GLU A 277 ? 1.0227 1.2197 1.7402 0.0228  -0.0797 0.0156  814  GLU A OE1 
2044 O OE2 . GLU A 277 ? 1.0252 1.2058 1.7155 0.0259  -0.1145 0.0456  814  GLU A OE2 
2045 N N   . ASP A 278 ? 0.3212 0.4825 0.8571 0.0050  -0.0500 0.0063  815  ASP A N   
2046 C CA  . ASP A 278 ? 0.4024 0.5654 0.9289 -0.0011 -0.0262 -0.0096 815  ASP A CA  
2047 C C   . ASP A 278 ? 0.3439 0.4878 0.8083 -0.0062 -0.0179 -0.0112 815  ASP A C   
2048 O O   . ASP A 278 ? 0.3571 0.5005 0.8027 -0.0146 -0.0061 -0.0185 815  ASP A O   
2049 C CB  . ASP A 278 ? 0.4127 0.5923 0.9615 -0.0090 -0.0270 -0.0129 815  ASP A CB  
2050 C CG  . ASP A 278 ? 0.4783 0.6792 1.0941 -0.0040 -0.0340 -0.0127 815  ASP A CG  
2051 O OD1 . ASP A 278 ? 0.4318 0.6350 1.0788 0.0038  -0.0238 -0.0196 815  ASP A OD1 
2052 O OD2 . ASP A 278 ? 0.4438 0.6565 1.0772 -0.0080 -0.0499 -0.0059 815  ASP A OD2 
2053 N N   . LYS A 279 ? 0.3330 0.4615 0.7679 -0.0014 -0.0240 -0.0041 816  LYS A N   
2054 C CA  . LYS A 279 ? 0.3720 0.4831 0.7511 -0.0053 -0.0195 -0.0041 816  LYS A CA  
2055 C C   . LYS A 279 ? 0.3776 0.4853 0.7425 -0.0097 0.0031  -0.0171 816  LYS A C   
2056 O O   . LYS A 279 ? 0.2922 0.3905 0.6201 -0.0164 0.0070  -0.0181 816  LYS A O   
2057 C CB  . LYS A 279 ? 0.3578 0.4558 0.7162 0.0011  -0.0269 0.0039  816  LYS A CB  
2058 C CG  . LYS A 279 ? 0.4093 0.5068 0.7926 0.0089  -0.0175 -0.0007 816  LYS A CG  
2059 C CD  . LYS A 279 ? 0.4468 0.5302 0.8065 0.0137  -0.0235 0.0073  816  LYS A CD  
2060 C CE  . LYS A 279 ? 0.5968 0.6822 0.9705 0.0172  -0.0454 0.0233  816  LYS A CE  
2061 N NZ  . LYS A 279 ? 0.7472 0.8396 1.1733 0.0248  -0.0480 0.0248  816  LYS A NZ  
2062 N N   . GLU A 280 ? 0.3067 0.4218 0.7004 -0.0067 0.0180  -0.0271 817  GLU A N   
2063 C CA  . GLU A 280 ? 0.3460 0.4577 0.7206 -0.0123 0.0392  -0.0390 817  GLU A CA  
2064 C C   . GLU A 280 ? 0.3347 0.4539 0.7063 -0.0233 0.0475  -0.0436 817  GLU A C   
2065 O O   . GLU A 280 ? 0.3750 0.4859 0.7124 -0.0308 0.0582  -0.0468 817  GLU A O   
2066 C CB  . GLU A 280 ? 0.3853 0.5045 0.7920 -0.0078 0.0542  -0.0511 817  GLU A CB  
2067 C CG  . GLU A 280 ? 0.3552 0.4668 0.7717 0.0027  0.0464  -0.0467 817  GLU A CG  
2068 C CD  . GLU A 280 ? 0.3380 0.4309 0.7065 0.0030  0.0459  -0.0428 817  GLU A CD  
2069 O OE1 . GLU A 280 ? 0.3653 0.4520 0.6976 -0.0043 0.0561  -0.0472 817  GLU A OE1 
2070 O OE2 . GLU A 280 ? 0.3746 0.4594 0.7424 0.0102  0.0344  -0.0343 817  GLU A OE2 
2071 N N   . ILE A 281 ? 0.2644 0.3994 0.6725 -0.0248 0.0418  -0.0430 818  ILE A N   
2072 C CA  . ILE A 281 ? 0.2960 0.4392 0.7053 -0.0361 0.0485  -0.0466 818  ILE A CA  
2073 C C   . ILE A 281 ? 0.2680 0.3993 0.6426 -0.0413 0.0344  -0.0368 818  ILE A C   
2074 O O   . ILE A 281 ? 0.2727 0.3993 0.6252 -0.0513 0.0416  -0.0383 818  ILE A O   
2075 C CB  . ILE A 281 ? 0.2759 0.4425 0.7429 -0.0357 0.0479  -0.0507 818  ILE A CB  
2076 C CG1 . ILE A 281 ? 0.4180 0.5972 0.9217 -0.0319 0.0663  -0.0644 818  ILE A CG1 
2077 C CG2 . ILE A 281 ? 0.3655 0.5413 0.8357 -0.0479 0.0512  -0.0522 818  ILE A CG2 
2078 C CD1 . ILE A 281 ? 0.5869 0.7674 1.0717 -0.0421 0.0914  -0.0769 818  ILE A CD1 
2079 N N   . ASN A 282 ? 0.2850 0.4112 0.6550 -0.0354 0.0142  -0.0268 819  ASN A N   
2080 C CA  . ASN A 282 ? 0.2959 0.4144 0.6408 -0.0409 0.0003  -0.0201 819  ASN A CA  
2081 C C   . ASN A 282 ? 0.2729 0.3699 0.5677 -0.0406 -0.0010 -0.0169 819  ASN A C   
2082 O O   . ASN A 282 ? 0.3358 0.4239 0.6067 -0.0469 -0.0062 -0.0152 819  ASN A O   
2083 C CB  . ASN A 282 ? 0.2636 0.3901 0.6283 -0.0372 -0.0214 -0.0115 819  ASN A CB  
2084 C CG  . ASN A 282 ? 0.2555 0.4041 0.6706 -0.0396 -0.0240 -0.0136 819  ASN A CG  
2085 O OD1 . ASN A 282 ? 0.3349 0.4916 0.7622 -0.0474 -0.0123 -0.0207 819  ASN A OD1 
2086 N ND2 . ASN A 282 ? 0.3741 0.5330 0.8200 -0.0332 -0.0398 -0.0065 819  ASN A ND2 
2087 N N   . SER A 283 ? 0.2557 0.3441 0.5365 -0.0335 0.0037  -0.0168 820  SER A N   
2088 C CA  . SER A 283 ? 0.2549 0.3245 0.4922 -0.0323 0.0018  -0.0138 820  SER A CA  
2089 C C   . SER A 283 ? 0.2555 0.3174 0.4765 -0.0311 0.0172  -0.0187 820  SER A C   
2090 O O   . SER A 283 ? 0.2713 0.3232 0.4729 -0.0253 0.0153  -0.0162 820  SER A O   
2091 C CB  . SER A 283 ? 0.3385 0.4047 0.5694 -0.0252 -0.0135 -0.0060 820  SER A CB  
2092 O OG  . SER A 283 ? 0.3310 0.4061 0.5765 -0.0275 -0.0290 -0.0011 820  SER A OG  
2093 N N   . PRO A 284 ? 0.3248 0.3914 0.5512 -0.0377 0.0326  -0.0256 821  PRO A N   
2094 C CA  . PRO A 284 ? 0.3307 0.3927 0.5438 -0.0373 0.0468  -0.0309 821  PRO A CA  
2095 C C   . PRO A 284 ? 0.3179 0.3617 0.4890 -0.0378 0.0451  -0.0269 821  PRO A C   
2096 O O   . PRO A 284 ? 0.2921 0.3302 0.4511 -0.0333 0.0488  -0.0282 821  PRO A O   
2097 C CB  . PRO A 284 ? 0.3522 0.4249 0.5775 -0.0472 0.0631  -0.0387 821  PRO A CB  
2098 C CG  . PRO A 284 ? 0.3959 0.4705 0.6241 -0.0545 0.0564  -0.0346 821  PRO A CG  
2099 C CD  . PRO A 284 ? 0.3149 0.3918 0.5581 -0.0472 0.0383  -0.0289 821  PRO A CD  
2100 N N   . ASN A 285 ? 0.3039 0.3383 0.4548 -0.0432 0.0394  -0.0225 822  ASN A N   
2101 C CA  . ASN A 285 ? 0.2580 0.2753 0.3738 -0.0430 0.0373  -0.0188 822  ASN A CA  
2102 C C   . ASN A 285 ? 0.3247 0.3350 0.4305 -0.0338 0.0256  -0.0150 822  ASN A C   
2103 O O   . ASN A 285 ? 0.3244 0.3258 0.4108 -0.0299 0.0266  -0.0140 822  ASN A O   
2104 C CB  . ASN A 285 ? 0.3221 0.3309 0.4245 -0.0517 0.0352  -0.0158 822  ASN A CB  
2105 C CG  . ASN A 285 ? 0.4079 0.4245 0.5192 -0.0624 0.0473  -0.0184 822  ASN A CG  
2106 O OD1 . ASN A 285 ? 0.3887 0.4043 0.4879 -0.0669 0.0583  -0.0199 822  ASN A OD1 
2107 N ND2 . ASN A 285 ? 0.3448 0.3706 0.4774 -0.0678 0.0457  -0.0192 822  ASN A ND2 
2108 N N   . LEU A 286 ? 0.2994 0.3149 0.4180 -0.0312 0.0144  -0.0126 823  LEU A N   
2109 C CA  . LEU A 286 ? 0.3181 0.3296 0.4272 -0.0242 0.0040  -0.0087 823  LEU A CA  
2110 C C   . LEU A 286 ? 0.3283 0.3425 0.4444 -0.0172 0.0078  -0.0086 823  LEU A C   
2111 O O   . LEU A 286 ? 0.3175 0.3239 0.4159 -0.0128 0.0058  -0.0065 823  LEU A O   
2112 C CB  . LEU A 286 ? 0.3510 0.3705 0.4740 -0.0247 -0.0087 -0.0058 823  LEU A CB  
2113 C CG  . LEU A 286 ? 0.4012 0.4200 0.5156 -0.0199 -0.0206 -0.0006 823  LEU A CG  
2114 C CD1 . LEU A 286 ? 0.3932 0.3987 0.4766 -0.0189 -0.0207 -0.0015 823  LEU A CD1 
2115 C CD2 . LEU A 286 ? 0.3830 0.4098 0.5071 -0.0237 -0.0338 0.0020  823  LEU A CD2 
2116 N N   . LEU A 287 ? 0.3118 0.3375 0.4565 -0.0164 0.0137  -0.0116 824  LEU A N   
2117 C CA  . LEU A 287 ? 0.3016 0.3291 0.4574 -0.0099 0.0171  -0.0125 824  LEU A CA  
2118 C C   . LEU A 287 ? 0.3347 0.3536 0.4691 -0.0104 0.0277  -0.0168 824  LEU A C   
2119 O O   . LEU A 287 ? 0.3114 0.3252 0.4388 -0.0052 0.0267  -0.0154 824  LEU A O   
2120 C CB  . LEU A 287 ? 0.2642 0.3059 0.4600 -0.0089 0.0221  -0.0169 824  LEU A CB  
2121 C CG  . LEU A 287 ? 0.3213 0.3726 0.5441 -0.0062 0.0084  -0.0105 824  LEU A CG  
2122 C CD1 . LEU A 287 ? 0.2707 0.3374 0.5380 -0.0056 0.0144  -0.0163 824  LEU A CD1 
2123 C CD2 . LEU A 287 ? 0.2910 0.3377 0.5108 0.0004  -0.0037 -0.0016 824  LEU A CD2 
2124 N N   . LYS A 288 ? 0.3374 0.3545 0.4601 -0.0175 0.0372  -0.0211 825  LYS A N   
2125 C CA  . LYS A 288 ? 0.3644 0.3733 0.4634 -0.0195 0.0449  -0.0236 825  LYS A CA  
2126 C C   . LYS A 288 ? 0.3491 0.3454 0.4219 -0.0159 0.0362  -0.0177 825  LYS A C   
2127 O O   . LYS A 288 ? 0.3606 0.3520 0.4216 -0.0131 0.0383  -0.0184 825  LYS A O   
2128 C CB  . LYS A 288 ? 0.3938 0.4027 0.4821 -0.0297 0.0543  -0.0265 825  LYS A CB  
2129 C CG  . LYS A 288 ? 0.4758 0.4986 0.5875 -0.0348 0.0673  -0.0350 825  LYS A CG  
2130 C CD  . LYS A 288 ? 0.6655 0.6872 0.7579 -0.0465 0.0784  -0.0374 825  LYS A CD  
2131 C CE  . LYS A 288 ? 0.8950 0.9048 0.9554 -0.0471 0.0779  -0.0350 825  LYS A CE  
2132 N NZ  . LYS A 288 ? 1.0257 1.0373 1.0686 -0.0591 0.0902  -0.0386 825  LYS A NZ  
2133 N N   A MET A 289 ? 0.3141 0.3059 0.3791 -0.0162 0.0269  -0.0131 826  MET A N   
2134 N N   B MET A 289 ? 0.3205 0.3124 0.3857 -0.0161 0.0268  -0.0131 826  MET A N   
2135 C CA  A MET A 289 ? 0.3175 0.2989 0.3611 -0.0126 0.0197  -0.0095 826  MET A CA  
2136 C CA  B MET A 289 ? 0.3225 0.3040 0.3661 -0.0126 0.0198  -0.0095 826  MET A CA  
2137 C C   A MET A 289 ? 0.3585 0.3422 0.4061 -0.0056 0.0150  -0.0073 826  MET A C   
2138 C C   B MET A 289 ? 0.3399 0.3234 0.3870 -0.0056 0.0147  -0.0072 826  MET A C   
2139 O O   A MET A 289 ? 0.3446 0.3227 0.3791 -0.0024 0.0155  -0.0067 826  MET A O   
2140 O O   B MET A 289 ? 0.3574 0.3350 0.3905 -0.0024 0.0145  -0.0063 826  MET A O   
2141 C CB  A MET A 289 ? 0.3613 0.3386 0.3991 -0.0151 0.0117  -0.0076 826  MET A CB  
2142 C CB  B MET A 289 ? 0.3666 0.3434 0.4035 -0.0154 0.0124  -0.0077 826  MET A CB  
2143 C CG  A MET A 289 ? 0.4386 0.4058 0.4568 -0.0119 0.0058  -0.0065 826  MET A CG  
2144 C CG  B MET A 289 ? 0.4617 0.4325 0.4849 -0.0110 0.0043  -0.0062 826  MET A CG  
2145 S SD  A MET A 289 ? 0.4528 0.4073 0.4527 -0.0140 0.0098  -0.0061 826  MET A SD  
2146 S SD  B MET A 289 ? 0.5210 0.4796 0.5297 -0.0149 0.0007  -0.0074 826  MET A SD  
2147 C CE  A MET A 289 ? 0.5773 0.5224 0.5644 -0.0096 0.0022  -0.0070 826  MET A CE  
2148 C CE  B MET A 289 ? 0.5377 0.4864 0.5320 -0.0141 0.0063  -0.0061 826  MET A CE  
2149 N N   . ILE A 290 ? 0.3095 0.3016 0.3766 -0.0037 0.0098  -0.0051 827  ILE A N   
2150 C CA  . ILE A 290 ? 0.3091 0.3029 0.3805 0.0016  0.0040  -0.0006 827  ILE A CA  
2151 C C   . ILE A 290 ? 0.3979 0.3912 0.4759 0.0048  0.0116  -0.0031 827  ILE A C   
2152 O O   . ILE A 290 ? 0.4243 0.4134 0.4929 0.0080  0.0100  -0.0005 827  ILE A O   
2153 C CB  . ILE A 290 ? 0.3852 0.3884 0.4785 0.0020  -0.0047 0.0041  827  ILE A CB  
2154 C CG1 . ILE A 290 ? 0.3791 0.3824 0.4612 -0.0019 -0.0137 0.0060  827  ILE A CG1 
2155 C CG2 . ILE A 290 ? 0.4643 0.4692 0.5657 0.0067  -0.0107 0.0108  827  ILE A CG2 
2156 C CD1 . ILE A 290 ? 0.4432 0.4573 0.5483 -0.0035 -0.0228 0.0100  827  ILE A CD1 
2157 N N   . ARG A 291 ? 0.3122 0.3103 0.4069 0.0031  0.0207  -0.0092 828  ARG A N   
2158 C CA  . ARG A 291 ? 0.3372 0.3354 0.4407 0.0053  0.0285  -0.0140 828  ARG A CA  
2159 C C   . ARG A 291 ? 0.4079 0.3981 0.4854 0.0036  0.0336  -0.0167 828  ARG A C   
2160 O O   . ARG A 291 ? 0.3526 0.3401 0.4298 0.0063  0.0355  -0.0180 828  ARG A O   
2161 C CB  . ARG A 291 ? 0.3138 0.3208 0.4420 0.0029  0.0385  -0.0224 828  ARG A CB  
2162 C CG  . ARG A 291 ? 0.3329 0.3487 0.4952 0.0066  0.0327  -0.0196 828  ARG A CG  
2163 C CD  . ARG A 291 ? 0.4010 0.4279 0.5900 0.0035  0.0418  -0.0280 828  ARG A CD  
2164 N NE  . ARG A 291 ? 0.4141 0.4496 0.6394 0.0083  0.0335  -0.0238 828  ARG A NE  
2165 C CZ  . ARG A 291 ? 0.4325 0.4802 0.6890 0.0070  0.0369  -0.0285 828  ARG A CZ  
2166 N NH1 . ARG A 291 ? 0.3840 0.4372 0.6380 0.0000  0.0501  -0.0380 828  ARG A NH1 
2167 N NH2 . ARG A 291 ? 0.3695 0.4246 0.6604 0.0120  0.0266  -0.0228 828  ARG A NH2 
2168 N N   . HIS A 292 ? 0.3536 0.3396 0.4111 -0.0013 0.0350  -0.0171 829  HIS A N   
2169 C CA  . HIS A 292 ? 0.3879 0.3662 0.4217 -0.0025 0.0363  -0.0172 829  HIS A CA  
2170 C C   . HIS A 292 ? 0.3994 0.3730 0.4246 0.0030  0.0287  -0.0121 829  HIS A C   
2171 O O   . HIS A 292 ? 0.3428 0.3137 0.3611 0.0045  0.0303  -0.0131 829  HIS A O   
2172 C CB  . HIS A 292 ? 0.3338 0.3070 0.3501 -0.0082 0.0361  -0.0156 829  HIS A CB  
2173 C CG  . HIS A 292 ? 0.3535 0.3180 0.3484 -0.0079 0.0331  -0.0130 829  HIS A CG  
2174 N ND1 . HIS A 292 ? 0.3438 0.3068 0.3277 -0.0116 0.0379  -0.0153 829  HIS A ND1 
2175 C CD2 . HIS A 292 ? 0.3325 0.2904 0.3172 -0.0042 0.0255  -0.0089 829  HIS A CD2 
2176 C CE1 . HIS A 292 ? 0.3733 0.3293 0.3426 -0.0098 0.0321  -0.0113 829  HIS A CE1 
2177 N NE2 . HIS A 292 ? 0.3461 0.2989 0.3170 -0.0050 0.0253  -0.0080 829  HIS A NE2 
2178 N N   . THR A 293 ? 0.3150 0.2886 0.3400 0.0051  0.0209  -0.0074 830  THR A N   
2179 C CA  . THR A 293 ? 0.3651 0.3358 0.3797 0.0088  0.0152  -0.0036 830  THR A CA  
2180 C C   . THR A 293 ? 0.4082 0.3819 0.4340 0.0121  0.0149  -0.0013 830  THR A C   
2181 O O   . THR A 293 ? 0.3582 0.3294 0.3760 0.0139  0.0151  -0.0004 830  THR A O   
2182 C CB  . THR A 293 ? 0.3743 0.3456 0.3847 0.0085  0.0077  -0.0006 830  THR A CB  
2183 O OG1 . THR A 293 ? 0.4021 0.3677 0.4013 0.0058  0.0077  -0.0030 830  THR A OG1 
2184 C CG2 . THR A 293 ? 0.4058 0.3772 0.4072 0.0110  0.0033  0.0026  830  THR A CG2 
2185 N N   . THR A 294 ? 0.3970 0.3761 0.4441 0.0128  0.0143  -0.0002 831  THR A N   
2186 C CA  . THR A 294 ? 0.3965 0.3768 0.4591 0.0158  0.0137  0.0025  831  THR A CA  
2187 C C   . THR A 294 ? 0.4223 0.3993 0.4835 0.0158  0.0216  -0.0037 831  THR A C   
2188 O O   . THR A 294 ? 0.3316 0.3059 0.3903 0.0174  0.0207  -0.0014 831  THR A O   
2189 C CB  . THR A 294 ? 0.3647 0.3511 0.4562 0.0170  0.0122  0.0035  831  THR A CB  
2190 O OG1 . THR A 294 ? 0.4367 0.4269 0.5289 0.0162  0.0025  0.0106  831  THR A OG1 
2191 C CG2 . THR A 294 ? 0.4794 0.4650 0.5916 0.0204  0.0115  0.0061  831  THR A CG2 
2192 N N   . ASN A 295 ? 0.3451 0.3228 0.4068 0.0128  0.0297  -0.0119 832  ASN A N   
2193 C CA  . ASN A 295 ? 0.3293 0.3050 0.3894 0.0113  0.0372  -0.0192 832  ASN A CA  
2194 C C   . ASN A 295 ? 0.2718 0.2426 0.3082 0.0105  0.0353  -0.0177 832  ASN A C   
2195 O O   . ASN A 295 ? 0.3237 0.2927 0.3602 0.0109  0.0368  -0.0196 832  ASN A O   
2196 C CB  . ASN A 295 ? 0.3276 0.3069 0.3903 0.0062  0.0469  -0.0286 832  ASN A CB  
2197 C CG  . ASN A 295 ? 0.5955 0.5802 0.6886 0.0074  0.0529  -0.0354 832  ASN A CG  
2198 O OD1 . ASN A 295 ? 0.6303 0.6134 0.7385 0.0106  0.0535  -0.0373 832  ASN A OD1 
2199 N ND2 . ASN A 295 ? 0.7278 0.7191 0.8328 0.0050  0.0574  -0.0393 832  ASN A ND2 
2200 N N   . LEU A 296 ? 0.3040 0.2726 0.3229 0.0093  0.0317  -0.0145 833  LEU A N   
2201 C CA  . LEU A 296 ? 0.3187 0.2831 0.3197 0.0092  0.0294  -0.0132 833  LEU A CA  
2202 C C   . LEU A 296 ? 0.3843 0.3489 0.3863 0.0134  0.0249  -0.0086 833  LEU A C   
2203 O O   . LEU A 296 ? 0.3349 0.2986 0.3323 0.0136  0.0251  -0.0093 833  LEU A O   
2204 C CB  . LEU A 296 ? 0.3059 0.2669 0.2928 0.0076  0.0262  -0.0110 833  LEU A CB  
2205 C CG  . LEU A 296 ? 0.4877 0.4444 0.4598 0.0069  0.0236  -0.0101 833  LEU A CG  
2206 C CD1 . LEU A 296 ? 0.4177 0.3745 0.3836 0.0017  0.0279  -0.0138 833  LEU A CD1 
2207 C CD2 . LEU A 296 ? 0.4936 0.4452 0.4572 0.0064  0.0192  -0.0071 833  LEU A CD2 
2208 N N   . THR A 297 ? 0.3012 0.2679 0.3091 0.0155  0.0206  -0.0036 834  THR A N   
2209 C CA  . THR A 297 ? 0.3047 0.2727 0.3113 0.0175  0.0171  0.0015  834  THR A CA  
2210 C C   . THR A 297 ? 0.3517 0.3197 0.3705 0.0179  0.0193  0.0020  834  THR A C   
2211 O O   . THR A 297 ? 0.3086 0.2765 0.3234 0.0180  0.0194  0.0031  834  THR A O   
2212 C CB  . THR A 297 ? 0.3424 0.3133 0.3504 0.0176  0.0115  0.0073  834  THR A CB  
2213 O OG1 . THR A 297 ? 0.3651 0.3351 0.3618 0.0168  0.0098  0.0052  834  THR A OG1 
2214 C CG2 . THR A 297 ? 0.3833 0.3566 0.3864 0.0175  0.0087  0.0131  834  THR A CG2 
2215 N N   . LEU A 298 ? 0.3226 0.2908 0.3591 0.0180  0.0213  0.0004  835  LEU A N   
2216 C CA  . LEU A 298 ? 0.3086 0.2752 0.3605 0.0183  0.0238  -0.0010 835  LEU A CA  
2217 C C   . LEU A 298 ? 0.3278 0.2924 0.3719 0.0161  0.0292  -0.0090 835  LEU A C   
2218 O O   . LEU A 298 ? 0.3235 0.2864 0.3731 0.0157  0.0298  -0.0092 835  LEU A O   
2219 C CB  . LEU A 298 ? 0.2937 0.2611 0.3699 0.0194  0.0259  -0.0037 835  LEU A CB  
2220 C CG  . LEU A 298 ? 0.4055 0.3746 0.4976 0.0216  0.0182  0.0064  835  LEU A CG  
2221 C CD1 . LEU A 298 ? 0.3951 0.3663 0.5161 0.0234  0.0206  0.0021  835  LEU A CD1 
2222 C CD2 . LEU A 298 ? 0.3901 0.3562 0.4869 0.0219  0.0137  0.0152  835  LEU A CD2 
2223 N N   . TRP A 299 ? 0.2869 0.2517 0.3187 0.0136  0.0325  -0.0151 836  TRP A N   
2224 C CA  . TRP A 299 ? 0.3155 0.2793 0.3374 0.0101  0.0357  -0.0216 836  TRP A CA  
2225 C C   . TRP A 299 ? 0.3292 0.2928 0.3399 0.0110  0.0312  -0.0173 836  TRP A C   
2226 O O   . TRP A 299 ? 0.3231 0.2867 0.3346 0.0092  0.0320  -0.0203 836  TRP A O   
2227 C CB  . TRP A 299 ? 0.3498 0.3139 0.3583 0.0059  0.0386  -0.0261 836  TRP A CB  
2228 C CG  . TRP A 299 ? 0.3240 0.2878 0.3189 0.0006  0.0403  -0.0315 836  TRP A CG  
2229 C CD1 . TRP A 299 ? 0.3811 0.3457 0.3798 -0.0038 0.0462  -0.0408 836  TRP A CD1 
2230 C CD2 . TRP A 299 ? 0.3758 0.3383 0.3515 -0.0016 0.0353  -0.0280 836  TRP A CD2 
2231 N NE1 . TRP A 299 ? 0.4201 0.3850 0.4001 -0.0095 0.0445  -0.0428 836  TRP A NE1 
2232 C CE2 . TRP A 299 ? 0.3983 0.3618 0.3652 -0.0080 0.0372  -0.0340 836  TRP A CE2 
2233 C CE3 . TRP A 299 ? 0.3783 0.3388 0.3453 0.0011  0.0289  -0.0208 836  TRP A CE3 
2234 C CZ2 . TRP A 299 ? 0.3397 0.3026 0.2893 -0.0117 0.0313  -0.0308 836  TRP A CZ2 
2235 C CZ3 . TRP A 299 ? 0.4064 0.3654 0.3594 -0.0017 0.0239  -0.0183 836  TRP A CZ3 
2236 C CH2 . TRP A 299 ? 0.3362 0.2965 0.2805 -0.0081 0.0244  -0.0223 836  TRP A CH2 
2237 N N   . PHE A 300 ? 0.3071 0.2714 0.3089 0.0134  0.0267  -0.0116 837  PHE A N   
2238 C CA  . PHE A 300 ? 0.2753 0.2413 0.2711 0.0148  0.0237  -0.0088 837  PHE A CA  
2239 C C   . PHE A 300 ? 0.3256 0.2934 0.3320 0.0151  0.0241  -0.0057 837  PHE A C   
2240 O O   . PHE A 300 ? 0.3196 0.2891 0.3268 0.0140  0.0242  -0.0068 837  PHE A O   
2241 C CB  . PHE A 300 ? 0.2691 0.2360 0.2569 0.0173  0.0204  -0.0053 837  PHE A CB  
2242 C CG  . PHE A 300 ? 0.3334 0.2971 0.3112 0.0168  0.0185  -0.0072 837  PHE A CG  
2243 C CD1 . PHE A 300 ? 0.3618 0.3246 0.3341 0.0150  0.0169  -0.0089 837  PHE A CD1 
2244 C CD2 . PHE A 300 ? 0.3007 0.2622 0.2750 0.0173  0.0172  -0.0061 837  PHE A CD2 
2245 C CE1 . PHE A 300 ? 0.3564 0.3152 0.3199 0.0139  0.0137  -0.0081 837  PHE A CE1 
2246 C CE2 . PHE A 300 ? 0.3678 0.3250 0.3343 0.0161  0.0150  -0.0065 837  PHE A CE2 
2247 C CZ  . PHE A 300 ? 0.3482 0.3035 0.3093 0.0144  0.0131  -0.0067 837  PHE A CZ  
2248 N N   . GLU A 301 ? 0.2862 0.2538 0.3021 0.0160  0.0235  -0.0008 838  GLU A N   
2249 C CA  . GLU A 301 ? 0.2824 0.2502 0.3090 0.0152  0.0230  0.0043  838  GLU A CA  
2250 C C   . GLU A 301 ? 0.3117 0.2764 0.3497 0.0133  0.0262  -0.0014 838  GLU A C   
2251 O O   . GLU A 301 ? 0.3189 0.2843 0.3607 0.0115  0.0264  0.0000  838  GLU A O   
2252 C CB  . GLU A 301 ? 0.3661 0.3331 0.4029 0.0159  0.0199  0.0120  838  GLU A CB  
2253 C CG  . GLU A 301 ? 0.5207 0.4914 0.5458 0.0162  0.0160  0.0176  838  GLU A CG  
2254 C CD  . GLU A 301 ? 0.5944 0.5647 0.6303 0.0165  0.0112  0.0245  838  GLU A CD  
2255 O OE1 . GLU A 301 ? 0.3717 0.3393 0.4250 0.0162  0.0094  0.0298  838  GLU A OE1 
2256 O OE2 . GLU A 301 ? 0.5188 0.4913 0.5476 0.0168  0.0085  0.0248  838  GLU A OE2 
2257 N N   . LYS A 302 ? 0.3237 0.2856 0.3684 0.0129  0.0295  -0.0086 839  LYS A N   
2258 C CA  . LYS A 302 ? 0.2996 0.2586 0.3551 0.0103  0.0336  -0.0171 839  LYS A CA  
2259 C C   . LYS A 302 ? 0.3458 0.3068 0.3889 0.0070  0.0337  -0.0217 839  LYS A C   
2260 O O   . LYS A 302 ? 0.3204 0.2801 0.3716 0.0045  0.0344  -0.0242 839  LYS A O   
2261 C CB  . LYS A 302 ? 0.3513 0.3092 0.4128 0.0094  0.0389  -0.0265 839  LYS A CB  
2262 C CG  . LYS A 302 ? 0.3319 0.2870 0.4066 0.0061  0.0450  -0.0384 839  LYS A CG  
2263 C CD  . LYS A 302 ? 0.2952 0.2517 0.3740 0.0044  0.0521  -0.0491 839  LYS A CD  
2264 C CE  . LYS A 302 ? 0.3509 0.3058 0.4386 -0.0004 0.0600  -0.0646 839  LYS A CE  
2265 N NZ  . LYS A 302 ? 0.4582 0.4159 0.5557 -0.0017 0.0687  -0.0756 839  LYS A NZ  
2266 N N   . CYS A 303 ? 0.2917 0.2555 0.3169 0.0066  0.0319  -0.0224 840  CYS A N   
2267 C CA  . CYS A 303 ? 0.3155 0.2819 0.3305 0.0035  0.0298  -0.0256 840  CYS A CA  
2268 C C   . CYS A 303 ? 0.3462 0.3158 0.3669 0.0043  0.0272  -0.0208 840  CYS A C   
2269 O O   . CYS A 303 ? 0.3305 0.3018 0.3536 0.0008  0.0265  -0.0246 840  CYS A O   
2270 C CB  . CYS A 303 ? 0.3514 0.3193 0.3496 0.0040  0.0263  -0.0239 840  CYS A CB  
2271 S SG  . CYS A 303 ? 0.3902 0.3557 0.3780 -0.0005 0.0300  -0.0301 840  CYS A SG  
2272 N N   . ILE A 304 ? 0.3079 0.2793 0.3303 0.0077  0.0262  -0.0128 841  ILE A N   
2273 C CA  . ILE A 304 ? 0.2587 0.2351 0.2856 0.0074  0.0254  -0.0082 841  ILE A CA  
2274 C C   . ILE A 304 ? 0.3202 0.2938 0.3623 0.0042  0.0272  -0.0070 841  ILE A C   
2275 O O   . ILE A 304 ? 0.3514 0.3276 0.3992 0.0010  0.0272  -0.0088 841  ILE A O   
2276 C CB  . ILE A 304 ? 0.2895 0.2694 0.3114 0.0102  0.0249  -0.0012 841  ILE A CB  
2277 C CG1 . ILE A 304 ? 0.2682 0.2502 0.2784 0.0133  0.0229  -0.0035 841  ILE A CG1 
2278 C CG2 . ILE A 304 ? 0.3091 0.2953 0.3358 0.0081  0.0262  0.0034  841  ILE A CG2 
2279 C CD1 . ILE A 304 ? 0.3132 0.2976 0.3173 0.0155  0.0231  0.0004  841  ILE A CD1 
2280 N N   A VAL A 305 ? 0.3069 0.2748 0.3580 0.0050  0.0281  -0.0036 842  VAL A N   
2281 N N   B VAL A 305 ? 0.3145 0.2825 0.3658 0.0050  0.0280  -0.0034 842  VAL A N   
2282 C CA  A VAL A 305 ? 0.3266 0.2902 0.3948 0.0025  0.0285  0.0006  842  VAL A CA  
2283 C CA  B VAL A 305 ? 0.3085 0.2726 0.3765 0.0022  0.0285  0.0004  842  VAL A CA  
2284 C C   A VAL A 305 ? 0.3363 0.2949 0.4162 -0.0005 0.0309  -0.0097 842  VAL A C   
2285 C C   B VAL A 305 ? 0.3405 0.2995 0.4197 -0.0007 0.0309  -0.0101 842  VAL A C   
2286 O O   A VAL A 305 ? 0.3679 0.3237 0.4614 -0.0039 0.0312  -0.0086 842  VAL A O   
2287 O O   B VAL A 305 ? 0.3342 0.2908 0.4264 -0.0043 0.0313  -0.0096 842  VAL A O   
2288 C CB  A VAL A 305 ? 0.3747 0.3339 0.4513 0.0048  0.0266  0.0089  842  VAL A CB  
2289 C CB  B VAL A 305 ? 0.3430 0.3025 0.4207 0.0038  0.0266  0.0098  842  VAL A CB  
2290 C CG1 A VAL A 305 ? 0.3185 0.2710 0.4160 0.0024  0.0256  0.0146  842  VAL A CG1 
2291 C CG1 B VAL A 305 ? 0.3516 0.3171 0.4153 0.0046  0.0241  0.0194  842  VAL A CG1 
2292 C CG2 A VAL A 305 ? 0.3820 0.3472 0.4444 0.0056  0.0240  0.0184  842  VAL A CG2 
2293 C CG2 B VAL A 305 ? 0.3303 0.2852 0.4146 0.0068  0.0278  0.0034  842  VAL A CG2 
2294 N N   . GLU A 306 ? 0.3235 0.2812 0.3976 -0.0004 0.0331  -0.0204 843  GLU A N   
2295 C CA  . GLU A 306 ? 0.3665 0.3206 0.4482 -0.0047 0.0363  -0.0327 843  GLU A CA  
2296 C C   . GLU A 306 ? 0.4084 0.3679 0.4795 -0.0093 0.0343  -0.0376 843  GLU A C   
2297 O O   . GLU A 306 ? 0.3997 0.3573 0.4751 -0.0145 0.0361  -0.0482 843  GLU A O   
2298 C CB  . GLU A 306 ? 0.3679 0.3201 0.4470 -0.0048 0.0408  -0.0432 843  GLU A CB  
2299 C CG  . GLU A 306 ? 0.3758 0.3228 0.4738 -0.0007 0.0431  -0.0413 843  GLU A CG  
2300 C CD  . GLU A 306 ? 0.4522 0.3984 0.5537 -0.0020 0.0500  -0.0551 843  GLU A CD  
2301 O OE1 . GLU A 306 ? 0.4409 0.3915 0.5222 -0.0059 0.0523  -0.0626 843  GLU A OE1 
2302 O OE2 . GLU A 306 ? 0.4480 0.3896 0.5736 0.0005  0.0532  -0.0581 843  GLU A OE2 
2303 N N   . ALA A 307 ? 0.3336 0.3003 0.3928 -0.0078 0.0304  -0.0309 844  ALA A N   
2304 C CA  . ALA A 307 ? 0.3056 0.2788 0.3604 -0.0115 0.0269  -0.0335 844  ALA A CA  
2305 C C   . ALA A 307 ? 0.3117 0.2858 0.3826 -0.0139 0.0272  -0.0292 844  ALA A C   
2306 O O   . ALA A 307 ? 0.3750 0.3544 0.4474 -0.0120 0.0267  -0.0202 844  ALA A O   
2307 C CB  . ALA A 307 ? 0.3395 0.3201 0.3808 -0.0081 0.0226  -0.0285 844  ALA A CB  
2308 N N   . GLU A 308 ? 0.3331 0.3020 0.4165 -0.0191 0.0289  -0.0365 845  GLU A N   
2309 C CA  . GLU A 308 ? 0.2955 0.2629 0.3967 -0.0222 0.0295  -0.0314 845  GLU A CA  
2310 C C   . GLU A 308 ? 0.3197 0.2977 0.4211 -0.0259 0.0264  -0.0303 845  GLU A C   
2311 O O   . GLU A 308 ? 0.3152 0.2972 0.4254 -0.0271 0.0272  -0.0215 845  GLU A O   
2312 C CB  . GLU A 308 ? 0.3344 0.2912 0.4526 -0.0264 0.0323  -0.0404 845  GLU A CB  
2313 C CG  . GLU A 308 ? 0.3364 0.2837 0.4619 -0.0220 0.0356  -0.0410 845  GLU A CG  
2314 C CD  . GLU A 308 ? 0.5582 0.4947 0.7049 -0.0252 0.0392  -0.0519 845  GLU A CD  
2315 O OE1 . GLU A 308 ? 0.5247 0.4600 0.6799 -0.0314 0.0388  -0.0578 845  GLU A OE1 
2316 O OE2 . GLU A 308 ? 0.5081 0.4377 0.6650 -0.0215 0.0424  -0.0553 845  GLU A OE2 
2317 N N   . ASN A 309 ? 0.3543 0.3378 0.4467 -0.0285 0.0227  -0.0387 846  ASN A N   
2318 C CA  . ASN A 309 ? 0.3312 0.3267 0.4262 -0.0311 0.0182  -0.0376 846  ASN A CA  
2319 C C   . ASN A 309 ? 0.3289 0.3332 0.4197 -0.0250 0.0180  -0.0282 846  ASN A C   
2320 O O   . ASN A 309 ? 0.3454 0.3491 0.4227 -0.0195 0.0171  -0.0267 846  ASN A O   
2321 C CB  . ASN A 309 ? 0.3481 0.3475 0.4323 -0.0351 0.0120  -0.0469 846  ASN A CB  
2322 C CG  . ASN A 309 ? 0.3356 0.3487 0.4251 -0.0371 0.0052  -0.0452 846  ASN A CG  
2323 O OD1 . ASN A 309 ? 0.3110 0.3316 0.3947 -0.0322 0.0011  -0.0404 846  ASN A OD1 
2324 N ND2 . ASN A 309 ? 0.3124 0.3288 0.4160 -0.0443 0.0037  -0.0494 846  ASN A ND2 
2325 N N   . PHE A 310 ? 0.3352 0.3478 0.4384 -0.0267 0.0198  -0.0226 847  PHE A N   
2326 C CA  . PHE A 310 ? 0.3553 0.3771 0.4565 -0.0220 0.0221  -0.0156 847  PHE A CA  
2327 C C   . PHE A 310 ? 0.3153 0.3444 0.4089 -0.0168 0.0170  -0.0184 847  PHE A C   
2328 O O   . PHE A 310 ? 0.2912 0.3201 0.3755 -0.0108 0.0182  -0.0157 847  PHE A O   
2329 C CB  . PHE A 310 ? 0.3260 0.3581 0.4430 -0.0269 0.0257  -0.0116 847  PHE A CB  
2330 C CG  . PHE A 310 ? 0.3437 0.3868 0.4596 -0.0237 0.0305  -0.0065 847  PHE A CG  
2331 C CD1 . PHE A 310 ? 0.3596 0.3978 0.4618 -0.0195 0.0338  -0.0016 847  PHE A CD1 
2332 C CD2 . PHE A 310 ? 0.4181 0.4773 0.5474 -0.0255 0.0323  -0.0076 847  PHE A CD2 
2333 C CE1 . PHE A 310 ? 0.3190 0.3676 0.4184 -0.0177 0.0391  0.0010  847  PHE A CE1 
2334 C CE2 . PHE A 310 ? 0.5193 0.5896 0.6481 -0.0230 0.0386  -0.0054 847  PHE A CE2 
2335 C CZ  . PHE A 310 ? 0.3470 0.4115 0.4594 -0.0194 0.0422  -0.0016 847  PHE A CZ  
2336 N N   . GLU A 311 ? 0.3020 0.3378 0.4009 -0.0195 0.0102  -0.0234 848  GLU A N   
2337 C CA  . GLU A 311 ? 0.2782 0.3210 0.3739 -0.0147 0.0034  -0.0239 848  GLU A CA  
2338 C C   . GLU A 311 ? 0.3135 0.3460 0.3894 -0.0116 0.0002  -0.0245 848  GLU A C   
2339 O O   . GLU A 311 ? 0.3164 0.3501 0.3873 -0.0056 -0.0024 -0.0220 848  GLU A O   
2340 C CB  . GLU A 311 ? 0.3028 0.3552 0.4093 -0.0192 -0.0055 -0.0274 848  GLU A CB  
2341 C CG  . GLU A 311 ? 0.3207 0.3871 0.4504 -0.0217 -0.0027 -0.0267 848  GLU A CG  
2342 C CD  . GLU A 311 ? 0.3308 0.3929 0.4672 -0.0288 0.0044  -0.0268 848  GLU A CD  
2343 O OE1 . GLU A 311 ? 0.3160 0.3662 0.4447 -0.0333 0.0039  -0.0303 848  GLU A OE1 
2344 O OE2 . GLU A 311 ? 0.3663 0.4374 0.5172 -0.0306 0.0109  -0.0236 848  GLU A OE2 
2345 N N   . GLU A 312 ? 0.3354 0.3577 0.4016 -0.0161 0.0010  -0.0286 849  GLU A N   
2346 C CA  . GLU A 312 ? 0.3541 0.3675 0.4020 -0.0144 0.0002  -0.0297 849  GLU A CA  
2347 C C   . GLU A 312 ? 0.3615 0.3701 0.4052 -0.0078 0.0061  -0.0247 849  GLU A C   
2348 O O   . GLU A 312 ? 0.3503 0.3565 0.3831 -0.0039 0.0039  -0.0227 849  GLU A O   
2349 C CB  . GLU A 312 ? 0.3456 0.3510 0.3879 -0.0212 0.0025  -0.0374 849  GLU A CB  
2350 C CG  . GLU A 312 ? 0.4127 0.4105 0.4369 -0.0217 0.0034  -0.0405 849  GLU A CG  
2351 C CD  . GLU A 312 ? 0.7364 0.7286 0.7586 -0.0291 0.0073  -0.0512 849  GLU A CD  
2352 O OE1 . GLU A 312 ? 0.7406 0.7366 0.7608 -0.0366 0.0026  -0.0573 849  GLU A OE1 
2353 O OE2 . GLU A 312 ? 0.9308 0.9153 0.9553 -0.0277 0.0149  -0.0541 849  GLU A OE2 
2354 N N   . ARG A 313 ? 0.3035 0.3110 0.3560 -0.0073 0.0128  -0.0217 850  ARG A N   
2355 C CA  . ARG A 313 ? 0.3087 0.3125 0.3562 -0.0025 0.0172  -0.0165 850  ARG A CA  
2356 C C   . ARG A 313 ? 0.3304 0.3418 0.3769 0.0027  0.0165  -0.0137 850  ARG A C   
2357 O O   . ARG A 313 ? 0.3099 0.3178 0.3470 0.0070  0.0167  -0.0122 850  ARG A O   
2358 C CB  . ARG A 313 ? 0.3139 0.3151 0.3705 -0.0047 0.0227  -0.0121 850  ARG A CB  
2359 C CG  . ARG A 313 ? 0.3153 0.3129 0.3659 -0.0013 0.0257  -0.0058 850  ARG A CG  
2360 C CD  . ARG A 313 ? 0.3019 0.2944 0.3616 -0.0046 0.0285  0.0001  850  ARG A CD  
2361 N NE  . ARG A 313 ? 0.3095 0.3092 0.3780 -0.0090 0.0308  0.0049  850  ARG A NE  
2362 C CZ  . ARG A 313 ? 0.3848 0.3836 0.4667 -0.0144 0.0311  0.0039  850  ARG A CZ  
2363 N NH1 . ARG A 313 ? 0.3585 0.3493 0.4461 -0.0158 0.0293  -0.0032 850  ARG A NH1 
2364 N NH2 . ARG A 313 ? 0.3411 0.3474 0.4308 -0.0192 0.0339  0.0093  850  ARG A NH2 
2365 N N   . VAL A 314 ? 0.2749 0.2972 0.3332 0.0023  0.0158  -0.0140 851  VAL A N   
2366 C CA  . VAL A 314 ? 0.2644 0.2947 0.3259 0.0076  0.0157  -0.0138 851  VAL A CA  
2367 C C   . VAL A 314 ? 0.3512 0.3777 0.4061 0.0115  0.0079  -0.0151 851  VAL A C   
2368 O O   . VAL A 314 ? 0.3023 0.3277 0.3542 0.0168  0.0080  -0.0148 851  VAL A O   
2369 C CB  . VAL A 314 ? 0.2568 0.3014 0.3368 0.0062  0.0170  -0.0152 851  VAL A CB  
2370 C CG1 . VAL A 314 ? 0.2699 0.3235 0.3583 0.0125  0.0170  -0.0176 851  VAL A CG1 
2371 C CG2 . VAL A 314 ? 0.3119 0.3602 0.3968 0.0010  0.0255  -0.0122 851  VAL A CG2 
2372 N N   . ALA A 315 ? 0.2684 0.2923 0.3202 0.0079  0.0007  -0.0164 852  ALA A N   
2373 C CA  . ALA A 315 ? 0.3059 0.3257 0.3490 0.0098  -0.0077 -0.0153 852  ALA A CA  
2374 C C   . ALA A 315 ? 0.3353 0.3436 0.3611 0.0106  -0.0050 -0.0143 852  ALA A C   
2375 O O   . ALA A 315 ? 0.3305 0.3349 0.3508 0.0142  -0.0089 -0.0119 852  ALA A O   
2376 C CB  . ALA A 315 ? 0.3315 0.3527 0.3719 0.0035  -0.0164 -0.0165 852  ALA A CB  
2377 N N   . VAL A 316 ? 0.2785 0.2815 0.2988 0.0075  0.0015  -0.0159 853  VAL A N   
2378 C CA  . VAL A 316 ? 0.3092 0.3032 0.3172 0.0084  0.0046  -0.0153 853  VAL A CA  
2379 C C   . VAL A 316 ? 0.3247 0.3187 0.3335 0.0143  0.0073  -0.0124 853  VAL A C   
2380 O O   . VAL A 316 ? 0.3312 0.3202 0.3320 0.0167  0.0054  -0.0112 853  VAL A O   
2381 C CB  . VAL A 316 ? 0.2647 0.2540 0.2730 0.0048  0.0107  -0.0179 853  VAL A CB  
2382 C CG1 . VAL A 316 ? 0.3022 0.2849 0.3037 0.0071  0.0143  -0.0165 853  VAL A CG1 
2383 C CG2 . VAL A 316 ? 0.3262 0.3138 0.3302 -0.0019 0.0090  -0.0238 853  VAL A CG2 
2384 N N   . LEU A 317 ? 0.2949 0.2948 0.3125 0.0156  0.0122  -0.0115 854  LEU A N   
2385 C CA  . LEU A 317 ? 0.3147 0.3161 0.3310 0.0197  0.0153  -0.0105 854  LEU A CA  
2386 C C   . LEU A 317 ? 0.3187 0.3222 0.3384 0.0244  0.0111  -0.0123 854  LEU A C   
2387 O O   . LEU A 317 ? 0.3184 0.3174 0.3327 0.0275  0.0110  -0.0127 854  LEU A O   
2388 C CB  . LEU A 317 ? 0.3086 0.3179 0.3317 0.0181  0.0215  -0.0092 854  LEU A CB  
2389 C CG  . LEU A 317 ? 0.3322 0.3452 0.3514 0.0202  0.0259  -0.0095 854  LEU A CG  
2390 C CD1 . LEU A 317 ? 0.3854 0.3896 0.3922 0.0210  0.0251  -0.0075 854  LEU A CD1 
2391 C CD2 . LEU A 317 ? 0.2939 0.3155 0.3164 0.0159  0.0324  -0.0070 854  LEU A CD2 
2392 N N   . SER A 318 ? 0.2795 0.2895 0.3107 0.0249  0.0067  -0.0135 855  SER A N   
2393 C CA  . SER A 318 ? 0.2555 0.2670 0.2953 0.0301  0.0013  -0.0145 855  SER A CA  
2394 C C   . SER A 318 ? 0.3041 0.3043 0.3325 0.0305  -0.0059 -0.0114 855  SER A C   
2395 O O   . SER A 318 ? 0.3110 0.3071 0.3419 0.0351  -0.0080 -0.0117 855  SER A O   
2396 C CB  . SER A 318 ? 0.3058 0.3270 0.3627 0.0302  -0.0041 -0.0151 855  SER A CB  
2397 O OG  . SER A 318 ? 0.3673 0.3997 0.4352 0.0285  0.0034  -0.0178 855  SER A OG  
2398 N N   . ARG A 319 ? 0.3215 0.3164 0.3376 0.0250  -0.0090 -0.0089 856  ARG A N   
2399 C CA  . ARG A 319 ? 0.2942 0.2793 0.2969 0.0231  -0.0145 -0.0053 856  ARG A CA  
2400 C C   . ARG A 319 ? 0.3322 0.3103 0.3270 0.0250  -0.0092 -0.0057 856  ARG A C   
2401 O O   . ARG A 319 ? 0.3002 0.2712 0.2914 0.0264  -0.0134 -0.0031 856  ARG A O   
2402 C CB  . ARG A 319 ? 0.3228 0.3059 0.3125 0.0152  -0.0158 -0.0051 856  ARG A CB  
2403 C CG  . ARG A 319 ? 0.3075 0.2837 0.2825 0.0106  -0.0228 -0.0007 856  ARG A CG  
2404 C CD  . ARG A 319 ? 0.3139 0.2921 0.2952 0.0112  -0.0356 0.0049  856  ARG A CD  
2405 N NE  . ARG A 319 ? 0.3372 0.3245 0.3252 0.0081  -0.0392 0.0030  856  ARG A NE  
2406 C CZ  . ARG A 319 ? 0.4295 0.4180 0.4044 -0.0010 -0.0438 0.0031  856  ARG A CZ  
2407 N NH1 . ARG A 319 ? 0.3407 0.3226 0.2939 -0.0084 -0.0445 0.0050  856  ARG A NH1 
2408 N NH2 . ARG A 319 ? 0.3691 0.3663 0.3524 -0.0037 -0.0474 0.0005  856  ARG A NH2 
2409 N N   . ILE A 320 ? 0.3380 0.3177 0.3310 0.0243  -0.0011 -0.0081 857  ILE A N   
2410 C CA  . ILE A 320 ? 0.3514 0.3260 0.3380 0.0254  0.0030  -0.0082 857  ILE A CA  
2411 C C   . ILE A 320 ? 0.3651 0.3403 0.3577 0.0307  0.0029  -0.0101 857  ILE A C   
2412 O O   . ILE A 320 ? 0.3222 0.2909 0.3102 0.0317  0.0019  -0.0101 857  ILE A O   
2413 C CB  . ILE A 320 ? 0.3073 0.2844 0.2935 0.0234  0.0096  -0.0087 857  ILE A CB  
2414 C CG1 . ILE A 320 ? 0.3162 0.2906 0.2987 0.0186  0.0104  -0.0090 857  ILE A CG1 
2415 C CG2 . ILE A 320 ? 0.2968 0.2714 0.2788 0.0246  0.0124  -0.0082 857  ILE A CG2 
2416 C CD1 . ILE A 320 ? 0.2856 0.2613 0.2734 0.0171  0.0156  -0.0090 857  ILE A CD1 
2417 N N   . ILE A 321 ? 0.2872 0.2708 0.2917 0.0336  0.0044  -0.0130 858  ILE A N   
2418 C CA  . ILE A 321 ? 0.2722 0.2573 0.2851 0.0386  0.0055  -0.0177 858  ILE A CA  
2419 C C   . ILE A 321 ? 0.3035 0.2809 0.3221 0.0417  -0.0030 -0.0160 858  ILE A C   
2420 O O   . ILE A 321 ? 0.3509 0.3228 0.3723 0.0449  -0.0033 -0.0191 858  ILE A O   
2421 C CB  . ILE A 321 ? 0.2599 0.2577 0.2866 0.0402  0.0105  -0.0223 858  ILE A CB  
2422 C CG1 . ILE A 321 ? 0.2838 0.2877 0.3027 0.0359  0.0187  -0.0222 858  ILE A CG1 
2423 C CG2 . ILE A 321 ? 0.2924 0.2929 0.3330 0.0459  0.0118  -0.0296 858  ILE A CG2 
2424 C CD1 . ILE A 321 ? 0.3344 0.3516 0.3652 0.0345  0.0237  -0.0241 858  ILE A CD1 
2425 N N   . GLU A 322 ? 0.2972 0.2734 0.3177 0.0402  -0.0109 -0.0109 859  GLU A N   
2426 C CA  . GLU A 322 ? 0.3163 0.2840 0.3409 0.0419  -0.0210 -0.0062 859  GLU A CA  
2427 C C   . GLU A 322 ? 0.3578 0.3135 0.3664 0.0384  -0.0221 -0.0024 859  GLU A C   
2428 O O   . GLU A 322 ? 0.3433 0.2903 0.3566 0.0409  -0.0268 -0.0009 859  GLU A O   
2429 C CB  . GLU A 322 ? 0.3424 0.3126 0.3689 0.0390  -0.0305 -0.0001 859  GLU A CB  
2430 C CG  . GLU A 322 ? 0.3975 0.3799 0.4456 0.0430  -0.0317 -0.0033 859  GLU A CG  
2431 C CD  . GLU A 322 ? 0.4658 0.4520 0.5151 0.0389  -0.0421 0.0027  859  GLU A CD  
2432 O OE1 . GLU A 322 ? 0.4122 0.3924 0.4421 0.0318  -0.0468 0.0084  859  GLU A OE1 
2433 O OE2 . GLU A 322 ? 0.4505 0.4471 0.5205 0.0420  -0.0454 0.0011  859  GLU A OE2 
2434 N N   . ILE A 323 ? 0.3467 0.3019 0.3390 0.0325  -0.0178 -0.0011 860  ILE A N   
2435 C CA  . ILE A 323 ? 0.3219 0.2683 0.3013 0.0288  -0.0168 0.0012  860  ILE A CA  
2436 C C   . ILE A 323 ? 0.3769 0.3206 0.3603 0.0326  -0.0127 -0.0035 860  ILE A C   
2437 O O   . ILE A 323 ? 0.3466 0.2811 0.3282 0.0321  -0.0156 -0.0018 860  ILE A O   
2438 C CB  . ILE A 323 ? 0.3270 0.2761 0.2940 0.0228  -0.0110 0.0008  860  ILE A CB  
2439 C CG1 . ILE A 323 ? 0.3245 0.2748 0.2844 0.0170  -0.0153 0.0042  860  ILE A CG1 
2440 C CG2 . ILE A 323 ? 0.3573 0.3003 0.3152 0.0194  -0.0077 0.0015  860  ILE A CG2 
2441 C CD1 . ILE A 323 ? 0.3188 0.2738 0.2726 0.0122  -0.0083 0.0003  860  ILE A CD1 
2442 N N   . LEU A 324 ? 0.3486 0.3003 0.3367 0.0354  -0.0061 -0.0096 861  LEU A N   
2443 C CA  . LEU A 324 ? 0.3612 0.3120 0.3513 0.0379  -0.0023 -0.0155 861  LEU A CA  
2444 C C   . LEU A 324 ? 0.3792 0.3240 0.3820 0.0427  -0.0067 -0.0185 861  LEU A C   
2445 O O   . LEU A 324 ? 0.3572 0.2943 0.3592 0.0428  -0.0072 -0.0210 861  LEU A O   
2446 C CB  . LEU A 324 ? 0.4094 0.3714 0.4011 0.0387  0.0051  -0.0207 861  LEU A CB  
2447 C CG  . LEU A 324 ? 0.3723 0.3357 0.3618 0.0391  0.0097  -0.0277 861  LEU A CG  
2448 C CD1 . LEU A 324 ? 0.3868 0.3599 0.3688 0.0357  0.0158  -0.0279 861  LEU A CD1 
2449 C CD2 . LEU A 324 ? 0.3787 0.3435 0.3821 0.0441  0.0109  -0.0365 861  LEU A CD2 
2450 N N   . GLN A 325 ? 0.3181 0.2665 0.3356 0.0469  -0.0102 -0.0189 862  GLN A N   
2451 C CA  . GLN A 325 ? 0.3418 0.2842 0.3773 0.0524  -0.0152 -0.0217 862  GLN A CA  
2452 C C   . GLN A 325 ? 0.3720 0.2993 0.4034 0.0502  -0.0238 -0.0139 862  GLN A C   
2453 O O   . GLN A 325 ? 0.3539 0.2721 0.3943 0.0529  -0.0255 -0.0175 862  GLN A O   
2454 C CB  . GLN A 325 ? 0.3872 0.3362 0.4418 0.0568  -0.0200 -0.0208 862  GLN A CB  
2455 C CG  . GLN A 325 ? 0.5746 0.5387 0.6381 0.0591  -0.0112 -0.0293 862  GLN A CG  
2456 C CD  . GLN A 325 ? 0.7580 0.7294 0.8451 0.0637  -0.0166 -0.0289 862  GLN A CD  
2457 O OE1 . GLN A 325 ? 0.6475 0.6255 0.7325 0.0610  -0.0196 -0.0233 862  GLN A OE1 
2458 N NE2 . GLN A 325 ? 0.7794 0.7496 0.8915 0.0708  -0.0183 -0.0354 862  GLN A NE2 
2459 N N   . VAL A 326 ? 0.3258 0.2502 0.3439 0.0445  -0.0290 -0.0035 863  VAL A N   
2460 C CA  . VAL A 326 ? 0.4049 0.3157 0.4172 0.0404  -0.0369 0.0054  863  VAL A CA  
2461 C C   . VAL A 326 ? 0.3517 0.2568 0.3530 0.0368  -0.0313 0.0027  863  VAL A C   
2462 O O   . VAL A 326 ? 0.3874 0.2806 0.3926 0.0362  -0.0357 0.0049  863  VAL A O   
2463 C CB  . VAL A 326 ? 0.3733 0.2847 0.3715 0.0333  -0.0427 0.0162  863  VAL A CB  
2464 C CG1 . VAL A 326 ? 0.4038 0.3020 0.3926 0.0269  -0.0499 0.0266  863  VAL A CG1 
2465 C CG2 . VAL A 326 ? 0.3908 0.3078 0.4024 0.0367  -0.0509 0.0195  863  VAL A CG2 
2466 N N   . PHE A 327 ? 0.3587 0.2720 0.3485 0.0342  -0.0226 -0.0016 864  PHE A N   
2467 C CA  . PHE A 327 ? 0.3485 0.2588 0.3320 0.0316  -0.0180 -0.0054 864  PHE A CA  
2468 C C   . PHE A 327 ? 0.4081 0.3132 0.4040 0.0364  -0.0182 -0.0135 864  PHE A C   
2469 O O   . PHE A 327 ? 0.3953 0.2904 0.3914 0.0341  -0.0204 -0.0135 864  PHE A O   
2470 C CB  . PHE A 327 ? 0.2852 0.2066 0.2608 0.0302  -0.0100 -0.0095 864  PHE A CB  
2471 C CG  . PHE A 327 ? 0.3462 0.2704 0.3108 0.0244  -0.0080 -0.0040 864  PHE A CG  
2472 C CD1 . PHE A 327 ? 0.3628 0.2801 0.3205 0.0186  -0.0108 0.0022  864  PHE A CD1 
2473 C CD2 . PHE A 327 ? 0.3380 0.2719 0.3003 0.0241  -0.0027 -0.0058 864  PHE A CD2 
2474 C CE1 . PHE A 327 ? 0.3356 0.2571 0.2845 0.0128  -0.0068 0.0044  864  PHE A CE1 
2475 C CE2 . PHE A 327 ? 0.3534 0.2899 0.3097 0.0194  0.0002  -0.0032 864  PHE A CE2 
2476 C CZ  . PHE A 327 ? 0.3679 0.2989 0.3176 0.0137  -0.0011 0.0008  864  PHE A CZ  
2477 N N   . GLN A 328 ? 0.3846 0.2967 0.3917 0.0423  -0.0152 -0.0217 865  GLN A N   
2478 C CA  . GLN A 328 ? 0.4282 0.3368 0.4482 0.0465  -0.0135 -0.0326 865  GLN A CA  
2479 C C   . GLN A 328 ? 0.4386 0.3322 0.4739 0.0492  -0.0222 -0.0294 865  GLN A C   
2480 O O   . GLN A 328 ? 0.4165 0.3005 0.4572 0.0490  -0.0227 -0.0350 865  GLN A O   
2481 C CB  . GLN A 328 ? 0.4236 0.3443 0.4545 0.0518  -0.0074 -0.0426 865  GLN A CB  
2482 C CG  . GLN A 328 ? 0.7027 0.6359 0.7199 0.0485  0.0017  -0.0484 865  GLN A CG  
2483 C CD  . GLN A 328 ? 0.7370 0.6744 0.7598 0.0501  0.0087  -0.0635 865  GLN A CD  
2484 O OE1 . GLN A 328 ? 0.8761 0.8039 0.9063 0.0512  0.0072  -0.0705 865  GLN A OE1 
2485 N NE2 . GLN A 328 ? 0.6213 0.5732 0.6406 0.0492  0.0168  -0.0691 865  GLN A NE2 
2486 N N   . ASP A 329 ? 0.3764 0.2680 0.4207 0.0514  -0.0299 -0.0205 866  ASP A N   
2487 C CA  . ASP A 329 ? 0.3763 0.2527 0.4363 0.0534  -0.0405 -0.0141 866  ASP A CA  
2488 C C   . ASP A 329 ? 0.3811 0.2441 0.4286 0.0460  -0.0442 -0.0063 866  ASP A C   
2489 O O   . ASP A 329 ? 0.4241 0.2724 0.4853 0.0470  -0.0504 -0.0051 866  ASP A O   
2490 C CB  . ASP A 329 ? 0.4400 0.3174 0.5064 0.0544  -0.0505 -0.0020 866  ASP A CB  
2491 C CG  . ASP A 329 ? 0.6947 0.5852 0.7793 0.0620  -0.0481 -0.0095 866  ASP A CG  
2492 O OD1 . ASP A 329 ? 0.6963 0.5920 0.7952 0.0677  -0.0400 -0.0243 866  ASP A OD1 
2493 O OD2 . ASP A 329 ? 0.8180 0.7145 0.9026 0.0613  -0.0541 -0.0010 866  ASP A OD2 
2494 N N   . LEU A 330 ? 0.4151 0.2828 0.4395 0.0383  -0.0403 -0.0011 867  LEU A N   
2495 C CA  . LEU A 330 ? 0.5147 0.3728 0.5272 0.0300  -0.0421 0.0060  867  LEU A CA  
2496 C C   . LEU A 330 ? 0.5120 0.3701 0.5222 0.0285  -0.0353 -0.0043 867  LEU A C   
2497 O O   . LEU A 330 ? 0.4681 0.3205 0.4699 0.0212  -0.0356 0.0002  867  LEU A O   
2498 C CB  . LEU A 330 ? 0.4500 0.3150 0.4415 0.0221  -0.0402 0.0152  867  LEU A CB  
2499 C CG  . LEU A 330 ? 0.3976 0.2607 0.3858 0.0195  -0.0488 0.0277  867  LEU A CG  
2500 C CD1 . LEU A 330 ? 0.4157 0.2888 0.3831 0.0120  -0.0439 0.0315  867  LEU A CD1 
2501 C CD2 . LEU A 330 ? 0.4145 0.2609 0.4060 0.0150  -0.0592 0.0397  867  LEU A CD2 
2502 N N   . ASN A 331 ? 0.4122 0.2776 0.4287 0.0340  -0.0293 -0.0180 868  ASN A N   
2503 C CA  . ASN A 331 ? 0.4181 0.2862 0.4290 0.0313  -0.0236 -0.0279 868  ASN A CA  
2504 C C   . ASN A 331 ? 0.4252 0.3016 0.4184 0.0245  -0.0200 -0.0229 868  ASN A C   
2505 O O   . ASN A 331 ? 0.4488 0.3239 0.4379 0.0197  -0.0189 -0.0256 868  ASN A O   
2506 C CB  . ASN A 331 ? 0.4565 0.3090 0.4774 0.0295  -0.0277 -0.0311 868  ASN A CB  
2507 C CG  . ASN A 331 ? 0.5695 0.4150 0.6121 0.0370  -0.0291 -0.0417 868  ASN A CG  
2508 O OD1 . ASN A 331 ? 0.5633 0.4193 0.6108 0.0426  -0.0235 -0.0521 868  ASN A OD1 
2509 N ND2 . ASN A 331 ? 0.5964 0.4243 0.6538 0.0369  -0.0360 -0.0395 868  ASN A ND2 
2510 N N   . ASN A 332 ? 0.3748 0.2603 0.3598 0.0240  -0.0182 -0.0164 869  ASN A N   
2511 C CA  . ASN A 332 ? 0.3595 0.2545 0.3327 0.0192  -0.0137 -0.0140 869  ASN A CA  
2512 C C   . ASN A 332 ? 0.4533 0.3609 0.4241 0.0221  -0.0085 -0.0211 869  ASN A C   
2513 O O   . ASN A 332 ? 0.3511 0.2670 0.3197 0.0241  -0.0059 -0.0193 869  ASN A O   
2514 C CB  . ASN A 332 ? 0.3725 0.2700 0.3385 0.0158  -0.0136 -0.0047 869  ASN A CB  
2515 C CG  . ASN A 332 ? 0.3536 0.2610 0.3127 0.0118  -0.0080 -0.0043 869  ASN A CG  
2516 O OD1 . ASN A 332 ? 0.3917 0.3039 0.3518 0.0115  -0.0059 -0.0089 869  ASN A OD1 
2517 N ND2 . ASN A 332 ? 0.3769 0.2880 0.3302 0.0085  -0.0060 0.0008  869  ASN A ND2 
2518 N N   . PHE A 333 ? 0.4431 0.3521 0.4132 0.0211  -0.0073 -0.0288 870  PHE A N   
2519 C CA  . PHE A 333 ? 0.4595 0.3804 0.4244 0.0218  -0.0031 -0.0342 870  PHE A CA  
2520 C C   . PHE A 333 ? 0.4391 0.3688 0.3974 0.0183  -0.0020 -0.0280 870  PHE A C   
2521 O O   . PHE A 333 ? 0.3767 0.3161 0.3309 0.0188  0.0005  -0.0284 870  PHE A O   
2522 C CB  . PHE A 333 ? 0.4653 0.3854 0.4293 0.0204  -0.0028 -0.0451 870  PHE A CB  
2523 C CG  . PHE A 333 ? 0.5019 0.4154 0.4765 0.0251  -0.0021 -0.0542 870  PHE A CG  
2524 C CD1 . PHE A 333 ? 0.6838 0.6046 0.6621 0.0297  0.0025  -0.0596 870  PHE A CD1 
2525 C CD2 . PHE A 333 ? 0.5486 0.4482 0.5324 0.0250  -0.0060 -0.0573 870  PHE A CD2 
2526 C CE1 . PHE A 333 ? 0.6588 0.5746 0.6519 0.0349  0.0036  -0.0691 870  PHE A CE1 
2527 C CE2 . PHE A 333 ? 0.6002 0.4928 0.5986 0.0302  -0.0058 -0.0661 870  PHE A CE2 
2528 C CZ  . PHE A 333 ? 0.6988 0.5999 0.7030 0.0356  -0.0008 -0.0725 870  PHE A CZ  
2529 N N   . ASN A 334 ? 0.3930 0.3198 0.3519 0.0145  -0.0036 -0.0222 871  ASN A N   
2530 C CA  . ASN A 334 ? 0.3482 0.2831 0.3065 0.0125  -0.0019 -0.0168 871  ASN A CA  
2531 C C   . ASN A 334 ? 0.4114 0.3501 0.3696 0.0154  0.0010  -0.0136 871  ASN A C   
2532 O O   . ASN A 334 ? 0.3719 0.3186 0.3301 0.0162  0.0027  -0.0122 871  ASN A O   
2533 C CB  . ASN A 334 ? 0.4181 0.3501 0.3797 0.0077  -0.0022 -0.0130 871  ASN A CB  
2534 C CG  . ASN A 334 ? 0.5284 0.4697 0.4947 0.0060  -0.0002 -0.0098 871  ASN A CG  
2535 O OD1 . ASN A 334 ? 0.5177 0.4648 0.4874 0.0044  -0.0026 -0.0103 871  ASN A OD1 
2536 N ND2 . ASN A 334 ? 0.4295 0.3727 0.3973 0.0061  0.0038  -0.0070 871  ASN A ND2 
2537 N N   . GLY A 335 ? 0.3801 0.3126 0.3386 0.0165  0.0005  -0.0117 872  GLY A N   
2538 C CA  . GLY A 335 ? 0.2974 0.2335 0.2556 0.0185  0.0023  -0.0094 872  GLY A CA  
2539 C C   . GLY A 335 ? 0.3371 0.2790 0.2970 0.0228  0.0035  -0.0129 872  GLY A C   
2540 O O   . GLY A 335 ? 0.3390 0.2875 0.2994 0.0233  0.0061  -0.0113 872  GLY A O   
2541 N N   . VAL A 336 ? 0.3181 0.2577 0.2800 0.0254  0.0026  -0.0184 873  VAL A N   
2542 C CA  . VAL A 336 ? 0.3002 0.2473 0.2639 0.0284  0.0057  -0.0232 873  VAL A CA  
2543 C C   . VAL A 336 ? 0.4019 0.3582 0.3595 0.0256  0.0086  -0.0219 873  VAL A C   
2544 O O   . VAL A 336 ? 0.3638 0.3272 0.3219 0.0260  0.0114  -0.0202 873  VAL A O   
2545 C CB  . VAL A 336 ? 0.3018 0.2458 0.2699 0.0309  0.0059  -0.0322 873  VAL A CB  
2546 C CG1 . VAL A 336 ? 0.3831 0.3380 0.3511 0.0320  0.0117  -0.0389 873  VAL A CG1 
2547 C CG2 . VAL A 336 ? 0.3653 0.3002 0.3440 0.0347  0.0018  -0.0317 873  VAL A CG2 
2548 N N   . LEU A 337 ? 0.3529 0.3090 0.3056 0.0221  0.0069  -0.0217 874  LEU A N   
2549 C CA  . LEU A 337 ? 0.3125 0.2772 0.2597 0.0189  0.0073  -0.0190 874  LEU A CA  
2550 C C   . LEU A 337 ? 0.3458 0.3126 0.2975 0.0181  0.0067  -0.0107 874  LEU A C   
2551 O O   . LEU A 337 ? 0.3676 0.3408 0.3179 0.0162  0.0067  -0.0062 874  LEU A O   
2552 C CB  . LEU A 337 ? 0.4498 0.4150 0.3909 0.0149  0.0041  -0.0217 874  LEU A CB  
2553 C CG  . LEU A 337 ? 0.5120 0.4793 0.4454 0.0133  0.0059  -0.0316 874  LEU A CG  
2554 C CD1 . LEU A 337 ? 0.4999 0.4753 0.4296 0.0139  0.0117  -0.0347 874  LEU A CD1 
2555 C CD2 . LEU A 337 ? 0.6079 0.5657 0.5467 0.0156  0.0056  -0.0398 874  LEU A CD2 
2556 N N   . GLU A 338 ? 0.3442 0.3058 0.3016 0.0188  0.0065  -0.0088 875  GLU A N   
2557 C CA  . GLU A 338 ? 0.3143 0.2780 0.2784 0.0185  0.0079  -0.0040 875  GLU A CA  
2558 C C   . GLU A 338 ? 0.4023 0.3689 0.3674 0.0202  0.0105  -0.0033 875  GLU A C   
2559 O O   . GLU A 338 ? 0.3515 0.3218 0.3217 0.0194  0.0113  0.0008  875  GLU A O   
2560 C CB  . GLU A 338 ? 0.3533 0.3118 0.3205 0.0175  0.0090  -0.0045 875  GLU A CB  
2561 C CG  . GLU A 338 ? 0.4526 0.4102 0.4230 0.0147  0.0075  -0.0042 875  GLU A CG  
2562 C CD  . GLU A 338 ? 0.4745 0.4275 0.4450 0.0120  0.0098  -0.0049 875  GLU A CD  
2563 O OE1 . GLU A 338 ? 0.4549 0.4034 0.4194 0.0122  0.0102  -0.0052 875  GLU A OE1 
2564 O OE2 . GLU A 338 ? 0.5080 0.4627 0.4847 0.0089  0.0110  -0.0048 875  GLU A OE2 
2565 N N   . ILE A 339 ? 0.3622 0.3273 0.3252 0.0224  0.0114  -0.0068 876  ILE A N   
2566 C CA  . ILE A 339 ? 0.3374 0.3068 0.3035 0.0235  0.0137  -0.0065 876  ILE A CA  
2567 C C   . ILE A 339 ? 0.3062 0.2830 0.2697 0.0224  0.0157  -0.0059 876  ILE A C   
2568 O O   . ILE A 339 ? 0.3190 0.3001 0.2856 0.0209  0.0174  -0.0021 876  ILE A O   
2569 C CB  . ILE A 339 ? 0.3138 0.2806 0.2817 0.0263  0.0128  -0.0099 876  ILE A CB  
2570 C CG1 . ILE A 339 ? 0.3142 0.2754 0.2818 0.0249  0.0107  -0.0080 876  ILE A CG1 
2571 C CG2 . ILE A 339 ? 0.3308 0.3047 0.3039 0.0276  0.0151  -0.0111 876  ILE A CG2 
2572 C CD1 . ILE A 339 ? 0.2879 0.2449 0.2565 0.0265  0.0067  -0.0085 876  ILE A CD1 
2573 N N   . VAL A 340 ? 0.3187 0.2972 0.2757 0.0218  0.0158  -0.0097 877  VAL A N   
2574 C CA  . VAL A 340 ? 0.3329 0.3197 0.2832 0.0184  0.0182  -0.0091 877  VAL A CA  
2575 C C   . VAL A 340 ? 0.3268 0.3154 0.2762 0.0145  0.0152  0.0004  877  VAL A C   
2576 O O   . VAL A 340 ? 0.3281 0.3222 0.2766 0.0115  0.0167  0.0057  877  VAL A O   
2577 C CB  . VAL A 340 ? 0.3356 0.3236 0.2773 0.0170  0.0186  -0.0165 877  VAL A CB  
2578 C CG1 . VAL A 340 ? 0.3376 0.3353 0.2675 0.0109  0.0210  -0.0156 877  VAL A CG1 
2579 C CG2 . VAL A 340 ? 0.3258 0.3117 0.2737 0.0216  0.0216  -0.0262 877  VAL A CG2 
2580 N N   . SER A 341 ? 0.3457 0.3298 0.2975 0.0144  0.0107  0.0032  878  SER A N   
2581 C CA  . SER A 341 ? 0.2790 0.2644 0.2360 0.0119  0.0066  0.0125  878  SER A CA  
2582 C C   . SER A 341 ? 0.3096 0.2940 0.2778 0.0131  0.0087  0.0168  878  SER A C   
2583 O O   . SER A 341 ? 0.3419 0.3287 0.3134 0.0103  0.0067  0.0250  878  SER A O   
2584 C CB  . SER A 341 ? 0.3466 0.3282 0.3099 0.0126  0.0026  0.0127  878  SER A CB  
2585 O OG  . SER A 341 ? 0.4977 0.4814 0.4701 0.0108  -0.0025 0.0213  878  SER A OG  
2586 N N   . ALA A 342 ? 0.3774 0.3577 0.3512 0.0163  0.0120  0.0116  879  ALA A N   
2587 C CA  . ALA A 342 ? 0.3440 0.3231 0.3284 0.0166  0.0140  0.0135  879  ALA A CA  
2588 C C   . ALA A 342 ? 0.3218 0.3058 0.3044 0.0145  0.0163  0.0162  879  ALA A C   
2589 O O   . ALA A 342 ? 0.3216 0.3054 0.3124 0.0125  0.0160  0.0223  879  ALA A O   
2590 C CB  . ALA A 342 ? 0.3541 0.3290 0.3408 0.0187  0.0164  0.0068  879  ALA A CB  
2591 N N   . VAL A 343 ? 0.3282 0.3167 0.3024 0.0148  0.0191  0.0115  880  VAL A N   
2592 C CA  . VAL A 343 ? 0.3285 0.3237 0.3029 0.0122  0.0228  0.0130  880  VAL A CA  
2593 C C   . VAL A 343 ? 0.3748 0.3753 0.3412 0.0064  0.0222  0.0207  880  VAL A C   
2594 O O   . VAL A 343 ? 0.3493 0.3548 0.3164 0.0023  0.0250  0.0252  880  VAL A O   
2595 C CB  . VAL A 343 ? 0.3718 0.3718 0.3445 0.0145  0.0267  0.0044  880  VAL A CB  
2596 C CG1 . VAL A 343 ? 0.3678 0.3629 0.3483 0.0188  0.0252  -0.0002 880  VAL A CG1 
2597 C CG2 . VAL A 343 ? 0.3643 0.3659 0.3269 0.0150  0.0271  -0.0010 880  VAL A CG2 
2598 N N   . ASN A 344 ? 0.3488 0.3485 0.3069 0.0050  0.0179  0.0232  881  ASN A N   
2599 C CA  . ASN A 344 ? 0.3251 0.3296 0.2739 -0.0019 0.0149  0.0328  881  ASN A CA  
2600 C C   . ASN A 344 ? 0.3761 0.3758 0.3370 -0.0033 0.0087  0.0453  881  ASN A C   
2601 O O   . ASN A 344 ? 0.3804 0.3833 0.3357 -0.0097 0.0045  0.0566  881  ASN A O   
2602 C CB  . ASN A 344 ? 0.3608 0.3673 0.2963 -0.0039 0.0112  0.0306  881  ASN A CB  
2603 C CG  . ASN A 344 ? 0.4125 0.4255 0.3342 -0.0054 0.0176  0.0194  881  ASN A CG  
2604 O OD1 . ASN A 344 ? 0.4401 0.4588 0.3617 -0.0062 0.0248  0.0155  881  ASN A OD1 
2605 N ND2 . ASN A 344 ? 0.3718 0.3846 0.2842 -0.0060 0.0152  0.0135  881  ASN A ND2 
2606 N N   . SER A 345 ? 0.3275 0.3197 0.3054 0.0020  0.0078  0.0435  882  SER A N   
2607 C CA  . SER A 345 ? 0.3556 0.3428 0.3503 0.0014  0.0028  0.0535  882  SER A CA  
2608 C C   . SER A 345 ? 0.3047 0.2933 0.3013 -0.0036 0.0044  0.0616  882  SER A C   
2609 O O   . SER A 345 ? 0.3691 0.3613 0.3616 -0.0044 0.0110  0.0560  882  SER A O   
2610 C CB  . SER A 345 ? 0.3896 0.3697 0.4021 0.0072  0.0046  0.0464  882  SER A CB  
2611 O OG  . SER A 345 ? 0.4451 0.4243 0.4593 0.0084  0.0109  0.0389  882  SER A OG  
2612 N N   A VAL A 346 ? 0.3588 0.3447 0.3638 -0.0074 -0.0025 0.0756  883  VAL A N   
2613 N N   B VAL A 346 ? 0.3563 0.3424 0.3611 -0.0075 -0.0025 0.0757  883  VAL A N   
2614 C CA  A VAL A 346 ? 0.4218 0.4090 0.4267 -0.0142 -0.0020 0.0861  883  VAL A CA  
2615 C CA  B VAL A 346 ? 0.4265 0.4137 0.4311 -0.0142 -0.0018 0.0858  883  VAL A CA  
2616 C C   A VAL A 346 ? 0.4209 0.4036 0.4410 -0.0119 0.0042  0.0797  883  VAL A C   
2617 C C   B VAL A 346 ? 0.4248 0.4078 0.4445 -0.0117 0.0045  0.0791  883  VAL A C   
2618 O O   A VAL A 346 ? 0.4088 0.3963 0.4239 -0.0166 0.0094  0.0804  883  VAL A O   
2619 O O   B VAL A 346 ? 0.3899 0.3779 0.4040 -0.0161 0.0101  0.0787  883  VAL A O   
2620 C CB  A VAL A 346 ? 0.4473 0.4303 0.4615 -0.0186 -0.0127 0.1045  883  VAL A CB  
2621 C CB  B VAL A 346 ? 0.4422 0.4251 0.4567 -0.0186 -0.0124 0.1042  883  VAL A CB  
2622 C CG1 A VAL A 346 ? 0.5179 0.5083 0.5103 -0.0247 -0.0191 0.1126  883  VAL A CG1 
2623 C CG1 B VAL A 346 ? 0.4438 0.4280 0.4550 -0.0276 -0.0117 0.1166  883  VAL A CG1 
2624 C CG2 A VAL A 346 ? 0.4112 0.3845 0.4538 -0.0114 -0.0180 0.1040  883  VAL A CG2 
2625 C CG2 B VAL A 346 ? 0.5344 0.5224 0.5340 -0.0215 -0.0204 0.1106  883  VAL A CG2 
2626 N N   . SER A 347 ? 0.3396 0.3145 0.3784 -0.0054 0.0042  0.0724  884  SER A N   
2627 C CA  . SER A 347 ? 0.3464 0.3170 0.3991 -0.0043 0.0092  0.0654  884  SER A CA  
2628 C C   . SER A 347 ? 0.3891 0.3667 0.4292 -0.0039 0.0164  0.0541  884  SER A C   
2629 O O   . SER A 347 ? 0.3554 0.3336 0.4018 -0.0063 0.0200  0.0520  884  SER A O   
2630 C CB  . SER A 347 ? 0.4538 0.4160 0.5261 0.0014  0.0089  0.0574  884  SER A CB  
2631 O OG  . SER A 347 ? 0.4543 0.4193 0.5166 0.0059  0.0115  0.0461  884  SER A OG  
2632 N N   . VAL A 348 ? 0.3467 0.3294 0.3715 -0.0009 0.0178  0.0471  885  VAL A N   
2633 C CA  . VAL A 348 ? 0.3152 0.3046 0.3314 0.0002  0.0231  0.0375  885  VAL A CA  
2634 C C   . VAL A 348 ? 0.2943 0.2939 0.2983 -0.0048 0.0265  0.0410  885  VAL A C   
2635 O O   . VAL A 348 ? 0.3461 0.3520 0.3525 -0.0068 0.0314  0.0377  885  VAL A O   
2636 C CB  . VAL A 348 ? 0.3530 0.3416 0.3618 0.0057  0.0229  0.0281  885  VAL A CB  
2637 C CG1 . VAL A 348 ? 0.3275 0.3229 0.3295 0.0072  0.0267  0.0201  885  VAL A CG1 
2638 C CG2 . VAL A 348 ? 0.2896 0.2703 0.3087 0.0090  0.0220  0.0226  885  VAL A CG2 
2639 N N   . TYR A 349 ? 0.3344 0.3370 0.3254 -0.0075 0.0243  0.0468  886  TYR A N   
2640 C CA  . TYR A 349 ? 0.3441 0.3578 0.3196 -0.0135 0.0288  0.0479  886  TYR A CA  
2641 C C   . TYR A 349 ? 0.4155 0.4341 0.3950 -0.0209 0.0327  0.0551  886  TYR A C   
2642 O O   . TYR A 349 ? 0.3662 0.3961 0.3400 -0.0244 0.0404  0.0503  886  TYR A O   
2643 C CB  . TYR A 349 ? 0.3695 0.3843 0.3298 -0.0176 0.0238  0.0554  886  TYR A CB  
2644 C CG  . TYR A 349 ? 0.3729 0.3998 0.3130 -0.0241 0.0293  0.0526  886  TYR A CG  
2645 C CD1 . TYR A 349 ? 0.3779 0.4091 0.3102 -0.0202 0.0336  0.0385  886  TYR A CD1 
2646 C CD2 . TYR A 349 ? 0.4256 0.4599 0.3547 -0.0350 0.0309  0.0633  886  TYR A CD2 
2647 C CE1 . TYR A 349 ? 0.3841 0.4267 0.2995 -0.0262 0.0402  0.0328  886  TYR A CE1 
2648 C CE2 . TYR A 349 ? 0.4558 0.5029 0.3645 -0.0424 0.0379  0.0586  886  TYR A CE2 
2649 C CZ  . TYR A 349 ? 0.4156 0.4670 0.3183 -0.0376 0.0430  0.0420  886  TYR A CZ  
2650 O OH  . TYR A 349 ? 0.4743 0.5386 0.3586 -0.0447 0.0513  0.0340  886  TYR A OH  
2651 N N   . ARG A 350 ? 0.3599 0.3705 0.3519 -0.0234 0.0280  0.0661  887  ARG A N   
2652 C CA  . ARG A 350 ? 0.3557 0.3696 0.3524 -0.0317 0.0310  0.0749  887  ARG A CA  
2653 C C   . ARG A 350 ? 0.4101 0.4266 0.4209 -0.0302 0.0369  0.0658  887  ARG A C   
2654 O O   . ARG A 350 ? 0.3880 0.4076 0.4052 -0.0374 0.0398  0.0722  887  ARG A O   
2655 C CB  . ARG A 350 ? 0.4499 0.4525 0.4587 -0.0351 0.0228  0.0905  887  ARG A CB  
2656 C CG  . ARG A 350 ? 0.3931 0.3828 0.4253 -0.0278 0.0194  0.0857  887  ARG A CG  
2657 C CD  . ARG A 350 ? 0.3801 0.3587 0.4305 -0.0317 0.0126  0.1005  887  ARG A CD  
2658 N NE  . ARG A 350 ? 0.3843 0.3652 0.4383 -0.0407 0.0159  0.1084  887  ARG A NE  
2659 C CZ  . ARG A 350 ? 0.4318 0.4109 0.5008 -0.0410 0.0206  0.1011  887  ARG A CZ  
2660 N NH1 . ARG A 350 ? 0.4610 0.4432 0.5335 -0.0504 0.0235  0.1095  887  ARG A NH1 
2661 N NH2 . ARG A 350 ? 0.3441 0.3191 0.4236 -0.0331 0.0222  0.0856  887  ARG A NH2 
2662 N N   . LEU A 351 ? 0.3410 0.3567 0.3570 -0.0220 0.0379  0.0522  888  LEU A N   
2663 C CA  . LEU A 351 ? 0.3592 0.3773 0.3892 -0.0208 0.0410  0.0443  888  LEU A CA  
2664 C C   . LEU A 351 ? 0.3722 0.4059 0.3987 -0.0226 0.0486  0.0377  888  LEU A C   
2665 O O   . LEU A 351 ? 0.3486 0.3865 0.3777 -0.0165 0.0496  0.0265  888  LEU A O   
2666 C CB  . LEU A 351 ? 0.3201 0.3307 0.3560 -0.0127 0.0374  0.0342  888  LEU A CB  
2667 C CG  . LEU A 351 ? 0.3294 0.3263 0.3728 -0.0108 0.0321  0.0373  888  LEU A CG  
2668 C CD1 . LEU A 351 ? 0.3167 0.3089 0.3613 -0.0045 0.0305  0.0261  888  LEU A CD1 
2669 C CD2 . LEU A 351 ? 0.3225 0.3137 0.3826 -0.0160 0.0316  0.0429  888  LEU A CD2 
2670 N N   . ASP A 352 ? 0.3421 0.3846 0.3643 -0.0316 0.0539  0.0451  889  ASP A N   
2671 C CA  . ASP A 352 ? 0.4080 0.4675 0.4279 -0.0342 0.0632  0.0377  889  ASP A CA  
2672 C C   . ASP A 352 ? 0.3614 0.4271 0.4006 -0.0302 0.0651  0.0274  889  ASP A C   
2673 O O   . ASP A 352 ? 0.3695 0.4451 0.4117 -0.0254 0.0690  0.0163  889  ASP A O   
2674 C CB  . ASP A 352 ? 0.4484 0.5171 0.4613 -0.0468 0.0695  0.0481  889  ASP A CB  
2675 C CG  . ASP A 352 ? 0.6083 0.6756 0.5980 -0.0521 0.0678  0.0573  889  ASP A CG  
2676 O OD1 . ASP A 352 ? 0.6092 0.6784 0.5864 -0.0474 0.0680  0.0495  889  ASP A OD1 
2677 O OD2 . ASP A 352 ? 0.7629 0.8271 0.7476 -0.0617 0.0654  0.0730  889  ASP A OD2 
2678 N N   . HIS A 353 ? 0.3485 0.4083 0.4025 -0.0321 0.0616  0.0305  890  HIS A N   
2679 C CA  . HIS A 353 ? 0.3514 0.4184 0.4235 -0.0297 0.0620  0.0213  890  HIS A CA  
2680 C C   . HIS A 353 ? 0.3393 0.4027 0.4117 -0.0193 0.0563  0.0113  890  HIS A C   
2681 O O   . HIS A 353 ? 0.3271 0.4007 0.4110 -0.0159 0.0569  0.0030  890  HIS A O   
2682 C CB  . HIS A 353 ? 0.3675 0.4273 0.4539 -0.0345 0.0584  0.0255  890  HIS A CB  
2683 C CG  . HIS A 353 ? 0.4477 0.5105 0.5371 -0.0456 0.0633  0.0366  890  HIS A CG  
2684 N ND1 . HIS A 353 ? 0.4685 0.5484 0.5654 -0.0526 0.0717  0.0360  890  HIS A ND1 
2685 C CD2 . HIS A 353 ? 0.4464 0.4973 0.5335 -0.0516 0.0607  0.0494  890  HIS A CD2 
2686 C CE1 . HIS A 353 ? 0.5157 0.5939 0.6119 -0.0634 0.0744  0.0487  890  HIS A CE1 
2687 N NE2 . HIS A 353 ? 0.4584 0.5183 0.5494 -0.0627 0.0670  0.0576  890  HIS A NE2 
2688 N N   . THR A 354 ? 0.3209 0.3706 0.3824 -0.0147 0.0505  0.0126  891  THR A N   
2689 C CA  . THR A 354 ? 0.2943 0.3395 0.3540 -0.0065 0.0450  0.0049  891  THR A CA  
2690 C C   . THR A 354 ? 0.3429 0.3958 0.3972 -0.0016 0.0481  -0.0008 891  THR A C   
2691 O O   . THR A 354 ? 0.3349 0.3917 0.3973 0.0038  0.0454  -0.0079 891  THR A O   
2692 C CB  . THR A 354 ? 0.2942 0.3238 0.3448 -0.0042 0.0396  0.0076  891  THR A CB  
2693 O OG1 . THR A 354 ? 0.3252 0.3475 0.3848 -0.0082 0.0374  0.0100  891  THR A OG1 
2694 C CG2 . THR A 354 ? 0.3072 0.3324 0.3534 0.0026  0.0345  0.0008  891  THR A CG2 
2695 N N   . PHE A 355 ? 0.3149 0.3703 0.3567 -0.0040 0.0532  0.0020  892  PHE A N   
2696 C CA  . PHE A 355 ? 0.3583 0.4210 0.3960 0.0000  0.0572  -0.0059 892  PHE A CA  
2697 C C   . PHE A 355 ? 0.4193 0.4988 0.4725 -0.0009 0.0646  -0.0131 892  PHE A C   
2698 O O   . PHE A 355 ? 0.3522 0.4371 0.4133 0.0053  0.0658  -0.0226 892  PHE A O   
2699 C CB  . PHE A 355 ? 0.3268 0.3887 0.3451 -0.0039 0.0606  -0.0021 892  PHE A CB  
2700 C CG  . PHE A 355 ? 0.3295 0.3770 0.3363 -0.0008 0.0531  0.0020  892  PHE A CG  
2701 C CD1 . PHE A 355 ? 0.3278 0.3701 0.3315 0.0061  0.0499  -0.0049 892  PHE A CD1 
2702 C CD2 . PHE A 355 ? 0.3821 0.4210 0.3845 -0.0048 0.0490  0.0127  892  PHE A CD2 
2703 C CE1 . PHE A 355 ? 0.3598 0.3904 0.3546 0.0083  0.0437  -0.0016 892  PHE A CE1 
2704 C CE2 . PHE A 355 ? 0.3994 0.4267 0.3953 -0.0016 0.0426  0.0155  892  PHE A CE2 
2705 C CZ  . PHE A 355 ? 0.3842 0.4081 0.3756 0.0046  0.0404  0.0082  892  PHE A CZ  
2706 N N   . GLU A 356 ? 0.3504 0.4387 0.4110 -0.0085 0.0697  -0.0090 893  GLU A N   
2707 C CA  . GLU A 356 ? 0.3459 0.4525 0.4244 -0.0098 0.0777  -0.0166 893  GLU A CA  
2708 C C   . GLU A 356 ? 0.3327 0.4414 0.4341 -0.0034 0.0708  -0.0219 893  GLU A C   
2709 O O   . GLU A 356 ? 0.3391 0.4621 0.4599 -0.0004 0.0747  -0.0306 893  GLU A O   
2710 C CB  . GLU A 356 ? 0.4397 0.5557 0.5192 -0.0213 0.0856  -0.0098 893  GLU A CB  
2711 C CG  . GLU A 356 ? 0.5938 0.7110 0.6504 -0.0294 0.0923  -0.0037 893  GLU A CG  
2712 C CD  . GLU A 356 ? 0.7788 0.9123 0.8321 -0.0309 0.1043  -0.0146 893  GLU A CD  
2713 O OE1 . GLU A 356 ? 0.7457 0.8888 0.8183 -0.0237 0.1073  -0.0277 893  GLU A OE1 
2714 O OE2 . GLU A 356 ? 0.7184 0.8553 0.7502 -0.0397 0.1104  -0.0101 893  GLU A OE2 
2715 N N   . ALA A 357 ? 0.2804 0.3759 0.3806 -0.0017 0.0602  -0.0173 894  ALA A N   
2716 C CA  . ALA A 357 ? 0.3497 0.4470 0.4676 0.0025  0.0517  -0.0210 894  ALA A CA  
2717 C C   . ALA A 357 ? 0.3916 0.4837 0.5097 0.0119  0.0446  -0.0259 894  ALA A C   
2718 O O   . ALA A 357 ? 0.3172 0.4137 0.4521 0.0158  0.0372  -0.0288 894  ALA A O   
2719 C CB  . ALA A 357 ? 0.3130 0.3991 0.4277 -0.0015 0.0442  -0.0155 894  ALA A CB  
2720 N N   . LEU A 358 ? 0.3177 0.4007 0.4185 0.0151  0.0458  -0.0259 895  LEU A N   
2721 C CA  . LEU A 358 ? 0.3628 0.4405 0.4652 0.0234  0.0398  -0.0302 895  LEU A CA  
2722 C C   . LEU A 358 ? 0.3769 0.4688 0.5040 0.0283  0.0425  -0.0387 895  LEU A C   
2723 O O   . LEU A 358 ? 0.3583 0.4640 0.4932 0.0257  0.0539  -0.0440 895  LEU A O   
2724 C CB  . LEU A 358 ? 0.3827 0.4513 0.4655 0.0249  0.0430  -0.0306 895  LEU A CB  
2725 C CG  . LEU A 358 ? 0.3663 0.4197 0.4277 0.0227  0.0389  -0.0235 895  LEU A CG  
2726 C CD1 . LEU A 358 ? 0.3574 0.4068 0.4045 0.0238  0.0427  -0.0255 895  LEU A CD1 
2727 C CD2 . LEU A 358 ? 0.3394 0.3822 0.4005 0.0260  0.0279  -0.0216 895  LEU A CD2 
2728 N N   . GLN A 359 ? 0.3582 0.4469 0.4982 0.0351  0.0320  -0.0398 896  GLN A N   
2729 C CA  . GLN A 359 ? 0.4385 0.5372 0.6045 0.0422  0.0331  -0.0483 896  GLN A CA  
2730 C C   . GLN A 359 ? 0.4283 0.5269 0.5872 0.0443  0.0439  -0.0563 896  GLN A C   
2731 O O   . GLN A 359 ? 0.3356 0.4208 0.4707 0.0437  0.0434  -0.0537 896  GLN A O   
2732 C CB  . GLN A 359 ? 0.4270 0.5170 0.6033 0.0491  0.0177  -0.0453 896  GLN A CB  
2733 C CG  . GLN A 359 ? 0.4751 0.5701 0.6655 0.0475  0.0059  -0.0399 896  GLN A CG  
2734 C CD  . GLN A 359 ? 0.6144 0.6989 0.8079 0.0522  -0.0108 -0.0341 896  GLN A CD  
2735 O OE1 . GLN A 359 ? 0.5877 0.6560 0.7584 0.0521  -0.0150 -0.0294 896  GLN A OE1 
2736 N NE2 . GLN A 359 ? 0.6385 0.7325 0.8611 0.0559  -0.0208 -0.0336 896  GLN A NE2 
2737 N N   . GLU A 360 ? 0.4061 0.5207 0.5869 0.0462  0.0540  -0.0672 897  GLU A N   
2738 C CA  . GLU A 360 ? 0.4186 0.5348 0.5938 0.0474  0.0652  -0.0778 897  GLU A CA  
2739 C C   . GLU A 360 ? 0.3563 0.4556 0.5277 0.0549  0.0566  -0.0788 897  GLU A C   
2740 O O   . GLU A 360 ? 0.3846 0.4766 0.5359 0.0533  0.0616  -0.0823 897  GLU A O   
2741 C CB  . GLU A 360 ? 0.4773 0.6144 0.6831 0.0494  0.0771  -0.0918 897  GLU A CB  
2742 C CG  . GLU A 360 ? 0.5412 0.6859 0.7354 0.0453  0.0938  -0.1039 897  GLU A CG  
2743 C CD  . GLU A 360 ? 0.5530 0.7215 0.7765 0.0449  0.1085  -0.1187 897  GLU A CD  
2744 O OE1 . GLU A 360 ? 0.5802 0.7624 0.8213 0.0421  0.1097  -0.1156 897  GLU A OE1 
2745 O OE2 . GLU A 360 ? 0.6566 0.8305 0.8868 0.0472  0.1193  -0.1345 897  GLU A OE2 
2746 N N   . ARG A 361 ? 0.4223 0.5148 0.6121 0.0620  0.0427  -0.0748 898  ARG A N   
2747 C CA  . ARG A 361 ? 0.3851 0.4606 0.5727 0.0682  0.0339  -0.0742 898  ARG A CA  
2748 C C   . ARG A 361 ? 0.4211 0.4803 0.5726 0.0632  0.0303  -0.0651 898  ARG A C   
2749 O O   . ARG A 361 ? 0.4521 0.4999 0.5932 0.0649  0.0303  -0.0678 898  ARG A O   
2750 C CB  . ARG A 361 ? 0.4094 0.4807 0.6217 0.0749  0.0176  -0.0680 898  ARG A CB  
2751 C CG  . ARG A 361 ? 0.4218 0.4866 0.6190 0.0701  0.0046  -0.0531 898  ARG A CG  
2752 C CD  . ARG A 361 ? 0.3316 0.3982 0.5562 0.0750  -0.0114 -0.0474 898  ARG A CD  
2753 N NE  . ARG A 361 ? 0.2972 0.3843 0.5530 0.0766  -0.0072 -0.0537 898  ARG A NE  
2754 C CZ  . ARG A 361 ? 0.4060 0.5003 0.6905 0.0800  -0.0201 -0.0497 898  ARG A CZ  
2755 N NH1 . ARG A 361 ? 0.4032 0.4852 0.6863 0.0815  -0.0387 -0.0381 898  ARG A NH1 
2756 N NH2 . ARG A 361 ? 0.4049 0.5198 0.7199 0.0811  -0.0148 -0.0566 898  ARG A NH2 
2757 N N   . LYS A 362 ? 0.3246 0.3829 0.4590 0.0567  0.0277  -0.0552 899  LYS A N   
2758 C CA  . LYS A 362 ? 0.3294 0.3741 0.4339 0.0521  0.0253  -0.0474 899  LYS A CA  
2759 C C   . LYS A 362 ? 0.3395 0.3866 0.4257 0.0473  0.0369  -0.0513 899  LYS A C   
2760 O O   . LYS A 362 ? 0.3747 0.4112 0.4433 0.0465  0.0361  -0.0502 899  LYS A O   
2761 C CB  . LYS A 362 ? 0.3490 0.3926 0.4452 0.0469  0.0198  -0.0379 899  LYS A CB  
2762 C CG  . LYS A 362 ? 0.4454 0.4757 0.5330 0.0472  0.0075  -0.0301 899  LYS A CG  
2763 C CD  . LYS A 362 ? 0.4990 0.5294 0.6069 0.0525  -0.0034 -0.0291 899  LYS A CD  
2764 C CE  . LYS A 362 ? 0.4721 0.4899 0.5662 0.0500  -0.0155 -0.0199 899  LYS A CE  
2765 N NZ  . LYS A 362 ? 0.3926 0.4096 0.5058 0.0544  -0.0284 -0.0163 899  LYS A NZ  
2766 N N   . ARG A 363 ? 0.4019 0.4641 0.4926 0.0432  0.0473  -0.0554 900  ARG A N   
2767 C CA  . ARG A 363 ? 0.3970 0.4640 0.4696 0.0369  0.0581  -0.0583 900  ARG A CA  
2768 C C   . ARG A 363 ? 0.4374 0.5013 0.5068 0.0398  0.0620  -0.0688 900  ARG A C   
2769 O O   . ARG A 363 ? 0.4028 0.4609 0.4499 0.0357  0.0633  -0.0675 900  ARG A O   
2770 C CB  . ARG A 363 ? 0.3600 0.4457 0.4422 0.0318  0.0692  -0.0622 900  ARG A CB  
2771 C CG  . ARG A 363 ? 0.5686 0.6598 0.6284 0.0222  0.0786  -0.0603 900  ARG A CG  
2772 C CD  . ARG A 363 ? 0.6553 0.7666 0.7258 0.0174  0.0924  -0.0690 900  ARG A CD  
2773 N NE  . ARG A 363 ? 0.7374 0.8582 0.8284 0.0167  0.0922  -0.0657 900  ARG A NE  
2774 C CZ  . ARG A 363 ? 0.8109 0.9510 0.9201 0.0139  0.1035  -0.0739 900  ARG A CZ  
2775 N NH1 . ARG A 363 ? 0.8407 0.9926 0.9489 0.0116  0.1167  -0.0870 900  ARG A NH1 
2776 N NH2 . ARG A 363 ? 0.7602 0.9089 0.8893 0.0128  0.1022  -0.0703 900  ARG A NH2 
2777 N N   . LYS A 364 ? 0.4151 0.4834 0.5088 0.0468  0.0636  -0.0799 901  LYS A N   
2778 C CA  . LYS A 364 ? 0.4115 0.4767 0.5049 0.0493  0.0683  -0.0924 901  LYS A CA  
2779 C C   . LYS A 364 ? 0.3803 0.4258 0.4602 0.0515  0.0578  -0.0867 901  LYS A C   
2780 O O   . LYS A 364 ? 0.4368 0.4777 0.5008 0.0487  0.0611  -0.0919 901  LYS A O   
2781 C CB  . LYS A 364 ? 0.4506 0.5238 0.5794 0.0573  0.0718  -0.1060 901  LYS A CB  
2782 C CG  . LYS A 364 ? 0.5145 0.6102 0.6580 0.0540  0.0849  -0.1139 901  LYS A CG  
2783 C CD  . LYS A 364 ? 0.7381 0.8446 0.9121 0.0598  0.0947  -0.1337 901  LYS A CD  
2784 C CE  . LYS A 364 ? 0.8202 0.9425 0.9804 0.0509  0.1138  -0.1477 901  LYS A CE  
2785 N NZ  . LYS A 364 ? 0.8254 0.9671 0.9844 0.0426  0.1234  -0.1444 901  LYS A NZ  
2786 N N   . ILE A 365 ? 0.3514 0.3859 0.4355 0.0551  0.0453  -0.0756 902  ILE A N   
2787 C CA  . ILE A 365 ? 0.3631 0.3801 0.4340 0.0558  0.0363  -0.0694 902  ILE A CA  
2788 C C   . ILE A 365 ? 0.4231 0.4374 0.4653 0.0483  0.0381  -0.0630 902  ILE A C   
2789 O O   . ILE A 365 ? 0.3686 0.3748 0.3981 0.0467  0.0374  -0.0648 902  ILE A O   
2790 C CB  . ILE A 365 ? 0.4227 0.4307 0.5013 0.0590  0.0234  -0.0583 902  ILE A CB  
2791 C CG1 . ILE A 365 ? 0.5116 0.5192 0.6203 0.0671  0.0181  -0.0630 902  ILE A CG1 
2792 C CG2 . ILE A 365 ? 0.3619 0.3545 0.4217 0.0566  0.0164  -0.0503 902  ILE A CG2 
2793 C CD1 . ILE A 365 ? 0.6609 0.6686 0.7806 0.0686  0.0070  -0.0528 902  ILE A CD1 
2794 N N   . LEU A 366 ? 0.3452 0.3657 0.3794 0.0435  0.0395  -0.0551 903  LEU A N   
2795 C CA  . LEU A 366 ? 0.3943 0.4124 0.4060 0.0369  0.0402  -0.0479 903  LEU A CA  
2796 C C   . LEU A 366 ? 0.3603 0.3843 0.3591 0.0322  0.0478  -0.0548 903  LEU A C   
2797 O O   . LEU A 366 ? 0.3915 0.4090 0.3747 0.0292  0.0452  -0.0524 903  LEU A O   
2798 C CB  . LEU A 366 ? 0.3199 0.3443 0.3303 0.0326  0.0413  -0.0396 903  LEU A CB  
2799 C CG  . LEU A 366 ? 0.4703 0.4928 0.4626 0.0261  0.0414  -0.0313 903  LEU A CG  
2800 C CD1 . LEU A 366 ? 0.4535 0.4627 0.4382 0.0273  0.0339  -0.0264 903  LEU A CD1 
2801 C CD2 . LEU A 366 ? 0.6009 0.6280 0.5968 0.0224  0.0423  -0.0239 903  LEU A CD2 
2802 N N   . ASP A 367 ? 0.3635 0.4010 0.3684 0.0306  0.0575  -0.0637 904  ASP A N   
2803 C CA  . ASP A 367 ? 0.4663 0.5117 0.4542 0.0234  0.0656  -0.0698 904  ASP A CA  
2804 C C   . ASP A 367 ? 0.4609 0.5001 0.4466 0.0255  0.0659  -0.0816 904  ASP A C   
2805 O O   . ASP A 367 ? 0.4743 0.5141 0.4396 0.0188  0.0673  -0.0832 904  ASP A O   
2806 C CB  . ASP A 367 ? 0.4441 0.5074 0.4384 0.0194  0.0776  -0.0768 904  ASP A CB  
2807 C CG  . ASP A 367 ? 0.4809 0.5499 0.4709 0.0138  0.0777  -0.0636 904  ASP A CG  
2808 O OD1 . ASP A 367 ? 0.4374 0.4964 0.4165 0.0122  0.0693  -0.0506 904  ASP A OD1 
2809 O OD2 . ASP A 367 ? 0.4084 0.4913 0.4081 0.0109  0.0862  -0.0666 904  ASP A OD2 
2810 N N   . GLU A 368 ? 0.3846 0.4174 0.3918 0.0342  0.0634  -0.0894 905  GLU A N   
2811 C CA  . GLU A 368 ? 0.5007 0.5243 0.5078 0.0362  0.0622  -0.0997 905  GLU A CA  
2812 C C   . GLU A 368 ? 0.3860 0.3964 0.3754 0.0336  0.0527  -0.0896 905  GLU A C   
2813 O O   . GLU A 368 ? 0.4302 0.4376 0.4071 0.0296  0.0533  -0.0958 905  GLU A O   
2814 C CB  . GLU A 368 ? 0.5863 0.6030 0.6229 0.0463  0.0590  -0.1067 905  GLU A CB  
2815 C CG  . GLU A 368 ? 0.7534 0.7575 0.7931 0.0487  0.0564  -0.1162 905  GLU A CG  
2816 C CD  . GLU A 368 ? 0.9668 0.9727 1.0360 0.0558  0.0617  -0.1330 905  GLU A CD  
2817 O OE1 . GLU A 368 ? 1.0573 1.0527 1.1506 0.0641  0.0531  -0.1297 905  GLU A OE1 
2818 O OE2 . GLU A 368 ? 1.0415 1.0600 1.1104 0.0525  0.0745  -0.1493 905  GLU A OE2 
2819 N N   . ALA A 369 ? 0.4053 0.4088 0.3942 0.0351  0.0444  -0.0749 906  ALA A N   
2820 C CA  . ALA A 369 ? 0.3839 0.3768 0.3595 0.0325  0.0368  -0.0663 906  ALA A CA  
2821 C C   . ALA A 369 ? 0.3855 0.3851 0.3401 0.0242  0.0383  -0.0612 906  ALA A C   
2822 O O   . ALA A 369 ? 0.3918 0.3866 0.3350 0.0207  0.0343  -0.0603 906  ALA A O   
2823 C CB  . ALA A 369 ? 0.3935 0.3784 0.3746 0.0356  0.0291  -0.0541 906  ALA A CB  
2824 N N   . VAL A 370 ? 0.4168 0.4273 0.3673 0.0206  0.0428  -0.0565 907  VAL A N   
2825 C CA  . VAL A 370 ? 0.4343 0.4510 0.3657 0.0120  0.0429  -0.0495 907  VAL A CA  
2826 C C   . VAL A 370 ? 0.4724 0.4943 0.3893 0.0060  0.0467  -0.0600 907  VAL A C   
2827 O O   . VAL A 370 ? 0.4389 0.4603 0.3397 -0.0002 0.0418  -0.0549 907  VAL A O   
2828 C CB  . VAL A 370 ? 0.5038 0.5310 0.4350 0.0083  0.0477  -0.0428 907  VAL A CB  
2829 C CG1 . VAL A 370 ? 0.5369 0.5715 0.4476 -0.0021 0.0480  -0.0355 907  VAL A CG1 
2830 C CG2 . VAL A 370 ? 0.4231 0.4441 0.3656 0.0123  0.0425  -0.0320 907  VAL A CG2 
2831 N N   . GLU A 371 ? 0.4495 0.4765 0.3731 0.0077  0.0552  -0.0756 908  GLU A N   
2832 C CA  . GLU A 371 ? 0.4738 0.5067 0.3828 0.0009  0.0606  -0.0887 908  GLU A CA  
2833 C C   . GLU A 371 ? 0.5051 0.5262 0.4106 0.0016  0.0533  -0.0928 908  GLU A C   
2834 O O   . GLU A 371 ? 0.4695 0.4947 0.3572 -0.0065 0.0542  -0.0996 908  GLU A O   
2835 C CB  . GLU A 371 ? 0.5698 0.6117 0.4916 0.0032  0.0731  -0.1067 908  GLU A CB  
2836 C CG  . GLU A 371 ? 0.7572 0.8156 0.6752 -0.0023 0.0826  -0.1043 908  GLU A CG  
2837 C CD  . GLU A 371 ? 0.8881 0.9553 0.8305 0.0034  0.0937  -0.1188 908  GLU A CD  
2838 O OE1 . GLU A 371 ? 0.7886 0.8673 0.7360 0.0013  0.0996  -0.1144 908  GLU A OE1 
2839 O OE2 . GLU A 371 ? 0.8723 0.9347 0.8314 0.0099  0.0960  -0.1344 908  GLU A OE2 
2840 N N   . LEU A 372 ? 0.4855 0.4926 0.4064 0.0096  0.0458  -0.0883 909  LEU A N   
2841 C CA  . LEU A 372 ? 0.5142 0.5102 0.4322 0.0089  0.0384  -0.0897 909  LEU A CA  
2842 C C   . LEU A 372 ? 0.4987 0.4984 0.3962 0.0001  0.0322  -0.0801 909  LEU A C   
2843 O O   . LEU A 372 ? 0.4247 0.4222 0.3131 -0.0048 0.0288  -0.0859 909  LEU A O   
2844 C CB  . LEU A 372 ? 0.4868 0.4688 0.4214 0.0167  0.0311  -0.0818 909  LEU A CB  
2845 C CG  . LEU A 372 ? 0.5266 0.5021 0.4835 0.0253  0.0331  -0.0889 909  LEU A CG  
2846 C CD1 . LEU A 372 ? 0.6124 0.5758 0.5794 0.0301  0.0248  -0.0770 909  LEU A CD1 
2847 C CD2 . LEU A 372 ? 0.5087 0.4790 0.4716 0.0257  0.0357  -0.1058 909  LEU A CD2 
2848 N N   . SER A 373 ? 0.4894 0.4945 0.3817 -0.0020 0.0298  -0.0652 910  SER A N   
2849 C CA  . SER A 373 ? 0.4634 0.4711 0.3423 -0.0089 0.0218  -0.0531 910  SER A CA  
2850 C C   . SER A 373 ? 0.5060 0.5264 0.3621 -0.0199 0.0237  -0.0545 910  SER A C   
2851 O O   . SER A 373 ? 0.5853 0.6080 0.4291 -0.0269 0.0153  -0.0465 910  SER A O   
2852 C CB  . SER A 373 ? 0.4886 0.4952 0.3755 -0.0060 0.0179  -0.0366 910  SER A CB  
2853 O OG  . SER A 373 ? 0.4627 0.4772 0.3487 -0.0069 0.0244  -0.0340 910  SER A OG  
2854 N N   . GLN A 374 ? 0.4850 0.5146 0.3356 -0.0225 0.0345  -0.0643 911  GLN A N   
2855 C CA  . GLN A 374 ? 0.5655 0.6088 0.3914 -0.0350 0.0376  -0.0637 911  GLN A CA  
2856 C C   . GLN A 374 ? 0.5440 0.5897 0.3517 -0.0434 0.0359  -0.0755 911  GLN A C   
2857 O O   . GLN A 374 ? 0.6030 0.6404 0.4199 -0.0388 0.0358  -0.0888 911  GLN A O   
2858 C CB  . GLN A 374 ? 0.5647 0.6188 0.3912 -0.0361 0.0516  -0.0721 911  GLN A CB  
2859 C CG  . GLN A 374 ? 0.5185 0.5720 0.3601 -0.0306 0.0521  -0.0588 911  GLN A CG  
2860 C CD  . GLN A 374 ? 0.6814 0.7455 0.5301 -0.0302 0.0658  -0.0680 911  GLN A CD  
2861 O OE1 . GLN A 374 ? 0.6251 0.6961 0.4729 -0.0317 0.0763  -0.0865 911  GLN A OE1 
2862 N NE2 . GLN A 374 ? 0.7506 0.8164 0.6090 -0.0283 0.0663  -0.0560 911  GLN A NE2 
2863 N N   . ASP A 375 ? 0.5748 0.6318 0.3561 -0.0568 0.0333  -0.0695 912  ASP A N   
2864 C CA  . ASP A 375 ? 0.5121 0.5739 0.2708 -0.0679 0.0301  -0.0791 912  ASP A CA  
2865 C C   . ASP A 375 ? 0.5890 0.6389 0.3580 -0.0635 0.0182  -0.0786 912  ASP A C   
2866 O O   . ASP A 375 ? 0.6365 0.6820 0.4061 -0.0638 0.0201  -0.0961 912  ASP A O   
2867 C CB  . ASP A 375 ? 0.7116 0.7801 0.4636 -0.0712 0.0454  -0.1051 912  ASP A CB  
2868 C CG  . ASP A 375 ? 1.0545 1.1369 0.7984 -0.0762 0.0590  -0.1069 912  ASP A CG  
2869 O OD1 . ASP A 375 ? 1.1689 1.2607 0.8930 -0.0864 0.0555  -0.0903 912  ASP A OD1 
2870 O OD2 . ASP A 375 ? 1.1671 1.2511 0.9269 -0.0699 0.0729  -0.1243 912  ASP A OD2 
2871 N N   . HIS A 376 ? 0.6336 0.6784 0.4126 -0.0599 0.0062  -0.0586 913  HIS A N   
2872 C CA  . HIS A 376 ? 0.6060 0.6414 0.3969 -0.0565 -0.0051 -0.0556 913  HIS A CA  
2873 C C   . HIS A 376 ? 0.5844 0.6070 0.3961 -0.0460 0.0006  -0.0701 913  HIS A C   
2874 O O   . HIS A 376 ? 0.5346 0.5520 0.3472 -0.0476 -0.0024 -0.0808 913  HIS A O   
2875 C CB  . HIS A 376 ? 0.6692 0.7113 0.4388 -0.0692 -0.0145 -0.0579 913  HIS A CB  
2876 C CG  . HIS A 376 ? 0.8354 0.8904 0.5813 -0.0816 -0.0212 -0.0431 913  HIS A CG  
2877 N ND1 . HIS A 376 ? 0.8953 0.9510 0.6488 -0.0809 -0.0331 -0.0197 913  HIS A ND1 
2878 C CD2 . HIS A 376 ? 0.9209 0.9888 0.6358 -0.0957 -0.0181 -0.0480 913  HIS A CD2 
2879 C CE1 . HIS A 376 ? 0.9275 0.9947 0.6564 -0.0939 -0.0384 -0.0088 913  HIS A CE1 
2880 N NE2 . HIS A 376 ? 0.9383 1.0136 0.6413 -0.1038 -0.0293 -0.0254 913  HIS A NE2 
2881 N N   . PHE A 377 ? 0.5320 0.5496 0.3608 -0.0358 0.0082  -0.0699 914  PHE A N   
2882 C CA  . PHE A 377 ? 0.5086 0.5130 0.3594 -0.0253 0.0113  -0.0782 914  PHE A CA  
2883 C C   . PHE A 377 ? 0.5699 0.5713 0.4202 -0.0264 0.0177  -0.1000 914  PHE A C   
2884 O O   . PHE A 377 ? 0.5582 0.5472 0.4236 -0.0212 0.0157  -0.1064 914  PHE A O   
2885 C CB  . PHE A 377 ? 0.4798 0.4746 0.3437 -0.0218 0.0013  -0.0681 914  PHE A CB  
2886 C CG  . PHE A 377 ? 0.5204 0.5166 0.3912 -0.0188 -0.0032 -0.0497 914  PHE A CG  
2887 C CD1 . PHE A 377 ? 0.5375 0.5413 0.4000 -0.0253 -0.0116 -0.0371 914  PHE A CD1 
2888 C CD2 . PHE A 377 ? 0.5002 0.4904 0.3869 -0.0100 0.0006  -0.0454 914  PHE A CD2 
2889 C CE1 . PHE A 377 ? 0.5820 0.5862 0.4551 -0.0220 -0.0153 -0.0216 914  PHE A CE1 
2890 C CE2 . PHE A 377 ? 0.5056 0.4968 0.3995 -0.0078 -0.0024 -0.0311 914  PHE A CE2 
2891 C CZ  . PHE A 377 ? 0.5293 0.5271 0.4179 -0.0133 -0.0099 -0.0197 914  PHE A CZ  
2892 N N   . LYS A 378 ? 0.5502 0.5629 0.3839 -0.0336 0.0258  -0.1118 915  LYS A N   
2893 C CA  . LYS A 378 ? 0.5826 0.5939 0.4166 -0.0354 0.0337  -0.1357 915  LYS A CA  
2894 C C   . LYS A 378 ? 0.5134 0.5122 0.3770 -0.0225 0.0389  -0.1445 915  LYS A C   
2895 O O   . LYS A 378 ? 0.5413 0.5275 0.4175 -0.0196 0.0363  -0.1541 915  LYS A O   
2896 C CB  . LYS A 378 ? 0.5576 0.5855 0.3710 -0.0447 0.0451  -0.1469 915  LYS A CB  
2897 C CG  . LYS A 378 ? 0.6554 0.6847 0.4656 -0.0492 0.0545  -0.1746 915  LYS A CG  
2898 C CD  . LYS A 378 ? 0.6968 0.7439 0.4908 -0.0572 0.0693  -0.1867 915  LYS A CD  
2899 C CE  . LYS A 378 ? 0.8244 0.8728 0.6210 -0.0602 0.0798  -0.2141 915  LYS A CE  
2900 N NZ  . LYS A 378 ? 0.9076 0.9567 0.6815 -0.0724 0.0720  -0.2175 915  LYS A NZ  
2901 N N   . LYS A 379 ? 0.4922 0.4939 0.3684 -0.0152 0.0449  -0.1400 916  LYS A N   
2902 C CA  . LYS A 379 ? 0.5504 0.5418 0.4554 -0.0035 0.0487  -0.1476 916  LYS A CA  
2903 C C   . LYS A 379 ? 0.5725 0.5472 0.4931 0.0035  0.0378  -0.1353 916  LYS A C   
2904 O O   . LYS A 379 ? 0.5330 0.4947 0.4737 0.0099  0.0369  -0.1430 916  LYS A O   
2905 C CB  . LYS A 379 ? 0.4319 0.4328 0.3463 0.0014  0.0568  -0.1453 916  LYS A CB  
2906 C CG  . LYS A 379 ? 0.5348 0.5515 0.4410 -0.0047 0.0709  -0.1632 916  LYS A CG  
2907 C CD  . LYS A 379 ? 0.5666 0.5952 0.4812 -0.0017 0.0790  -0.1593 916  LYS A CD  
2908 C CE  . LYS A 379 ? 0.6631 0.7081 0.5744 -0.0073 0.0954  -0.1802 916  LYS A CE  
2909 N NZ  . LYS A 379 ? 0.6164 0.6751 0.5342 -0.0065 0.1034  -0.1747 916  LYS A NZ  
2910 N N   . TYR A 380 ? 0.5026 0.4774 0.4150 0.0019  0.0298  -0.1163 917  TYR A N   
2911 C CA  . TYR A 380 ? 0.4837 0.4445 0.4077 0.0062  0.0209  -0.1057 917  TYR A CA  
2912 C C   . TYR A 380 ? 0.4428 0.3937 0.3681 0.0027  0.0165  -0.1146 917  TYR A C   
2913 O O   . TYR A 380 ? 0.4821 0.4187 0.4242 0.0075  0.0133  -0.1152 917  TYR A O   
2914 C CB  . TYR A 380 ? 0.4888 0.4535 0.4047 0.0038  0.0145  -0.0870 917  TYR A CB  
2915 C CG  . TYR A 380 ? 0.4275 0.3808 0.3513 0.0046  0.0065  -0.0793 917  TYR A CG  
2916 C CD1 . TYR A 380 ? 0.4063 0.3483 0.3459 0.0111  0.0053  -0.0750 917  TYR A CD1 
2917 C CD2 . TYR A 380 ? 0.4574 0.4121 0.3730 -0.0023 0.0001  -0.0763 917  TYR A CD2 
2918 C CE1 . TYR A 380 ? 0.4170 0.3494 0.3623 0.0101  -0.0007 -0.0680 917  TYR A CE1 
2919 C CE2 . TYR A 380 ? 0.4138 0.3596 0.3386 -0.0024 -0.0058 -0.0701 917  TYR A CE2 
2920 C CZ  . TYR A 380 ? 0.4766 0.4114 0.4153 0.0035  -0.0054 -0.0661 917  TYR A CZ  
2921 O OH  . TYR A 380 ? 0.4721 0.3989 0.4182 0.0018  -0.0099 -0.0597 917  TYR A OH  
2922 N N   . LEU A 381 ? 0.4554 0.4136 0.3624 -0.0067 0.0153  -0.1205 918  LEU A N   
2923 C CA  . LEU A 381 ? 0.4389 0.3885 0.3467 -0.0114 0.0103  -0.1290 918  LEU A CA  
2924 C C   . LEU A 381 ? 0.5560 0.4954 0.4792 -0.0076 0.0161  -0.1485 918  LEU A C   
2925 O O   . LEU A 381 ? 0.5267 0.4517 0.4625 -0.0070 0.0114  -0.1521 918  LEU A O   
2926 C CB  . LEU A 381 ? 0.5720 0.5335 0.4559 -0.0233 0.0071  -0.1318 918  LEU A CB  
2927 C CG  . LEU A 381 ? 0.5804 0.5496 0.4549 -0.0272 -0.0018 -0.1118 918  LEU A CG  
2928 C CD1 . LEU A 381 ? 0.5828 0.5649 0.4333 -0.0395 -0.0067 -0.1132 918  LEU A CD1 
2929 C CD2 . LEU A 381 ? 0.5255 0.4840 0.4153 -0.0245 -0.0098 -0.1020 918  LEU A CD2 
2930 N N   . VAL A 382 ? 0.5938 0.5403 0.5189 -0.0051 0.0264  -0.1612 919  VAL A N   
2931 C CA  . VAL A 382 ? 0.6390 0.5755 0.5858 0.0005  0.0322  -0.1800 919  VAL A CA  
2932 C C   . VAL A 382 ? 0.5460 0.4664 0.5199 0.0114  0.0270  -0.1697 919  VAL A C   
2933 O O   . VAL A 382 ? 0.6681 0.5723 0.6608 0.0142  0.0238  -0.1764 919  VAL A O   
2934 C CB  . VAL A 382 ? 0.6485 0.5986 0.5948 0.0011  0.0457  -0.1961 919  VAL A CB  
2935 C CG1 . VAL A 382 ? 0.6882 0.6278 0.6660 0.0099  0.0515  -0.2140 919  VAL A CG1 
2936 C CG2 . VAL A 382 ? 0.6599 0.6243 0.5775 -0.0121 0.0510  -0.2096 919  VAL A CG2 
2937 N N   . LYS A 383 ? 0.5364 0.4605 0.5119 0.0164  0.0251  -0.1522 920  LYS A N   
2938 C CA  . LYS A 383 ? 0.5547 0.4654 0.5524 0.0252  0.0196  -0.1414 920  LYS A CA  
2939 C C   . LYS A 383 ? 0.5773 0.4736 0.5757 0.0224  0.0096  -0.1300 920  LYS A C   
2940 O O   . LYS A 383 ? 0.5228 0.4031 0.5406 0.0268  0.0047  -0.1278 920  LYS A O   
2941 C CB  . LYS A 383 ? 0.5285 0.4484 0.5247 0.0294  0.0203  -0.1271 920  LYS A CB  
2942 C CG  . LYS A 383 ? 0.7268 0.6392 0.7482 0.0391  0.0184  -0.1235 920  LYS A CG  
2943 C CD  . LYS A 383 ? 0.7620 0.6885 0.7835 0.0425  0.0230  -0.1184 920  LYS A CD  
2944 C CE  . LYS A 383 ? 0.8188 0.7559 0.8525 0.0456  0.0337  -0.1366 920  LYS A CE  
2945 N NZ  . LYS A 383 ? 0.8132 0.7414 0.8807 0.0553  0.0323  -0.1433 920  LYS A NZ  
2946 N N   . LEU A 384 ? 0.4538 0.3561 0.4329 0.0148  0.0061  -0.1220 921  LEU A N   
2947 C CA  . LEU A 384 ? 0.4920 0.3832 0.4729 0.0112  -0.0020 -0.1121 921  LEU A CA  
2948 C C   . LEU A 384 ? 0.6277 0.5043 0.6202 0.0089  -0.0042 -0.1248 921  LEU A C   
2949 O O   . LEU A 384 ? 0.6200 0.4813 0.6256 0.0096  -0.0100 -0.1177 921  LEU A O   
2950 C CB  . LEU A 384 ? 0.5090 0.4115 0.4713 0.0035  -0.0050 -0.1039 921  LEU A CB  
2951 C CG  . LEU A 384 ? 0.5796 0.4748 0.5445 -0.0015 -0.0121 -0.0946 921  LEU A CG  
2952 C CD1 . LEU A 384 ? 0.5014 0.3887 0.4758 0.0024  -0.0143 -0.0794 921  LEU A CD1 
2953 C CD2 . LEU A 384 ? 0.5749 0.4834 0.5257 -0.0088 -0.0153 -0.0895 921  LEU A CD2 
2954 N N   . LYS A 385 ? 0.5629 0.4440 0.5503 0.0052  0.0004  -0.1438 922  LYS A N   
2955 C CA  . LYS A 385 ? 0.6627 0.5298 0.6608 0.0017  -0.0018 -0.1575 922  LYS A CA  
2956 C C   . LYS A 385 ? 0.6272 0.4770 0.6542 0.0103  -0.0014 -0.1633 922  LYS A C   
2957 O O   . LYS A 385 ? 0.7612 0.5945 0.8026 0.0085  -0.0052 -0.1703 922  LYS A O   
2958 C CB  . LYS A 385 ? 0.7750 0.6523 0.7581 -0.0058 0.0035  -0.1782 922  LYS A CB  
2959 C CG  . LYS A 385 ? 0.9433 0.8193 0.9389 -0.0016 0.0131  -0.2013 922  LYS A CG  
2960 C CD  . LYS A 385 ? 1.0174 0.9096 0.9896 -0.0111 0.0203  -0.2201 922  LYS A CD  
2961 C CE  . LYS A 385 ? 1.1171 1.0014 1.0879 -0.0200 0.0181  -0.2382 922  LYS A CE  
2962 N NZ  . LYS A 385 ? 1.1401 1.0188 1.1280 -0.0171 0.0274  -0.2625 922  LYS A NZ  
2963 N N   . SER A 386 ? 0.6011 0.4536 0.6388 0.0194  0.0018  -0.1595 923  SER A N   
2964 C CA  . SER A 386 ? 0.7270 0.5647 0.7955 0.0284  0.0012  -0.1649 923  SER A CA  
2965 C C   . SER A 386 ? 0.7129 0.5390 0.7939 0.0334  -0.0079 -0.1427 923  SER A C   
2966 O O   . SER A 386 ? 0.8749 0.6852 0.9832 0.0397  -0.0122 -0.1433 923  SER A O   
2967 C CB  . SER A 386 ? 0.7638 0.6140 0.8409 0.0352  0.0114  -0.1793 923  SER A CB  
2968 O OG  . SER A 386 ? 0.8671 0.7293 0.9377 0.0392  0.0119  -0.1643 923  SER A OG  
2969 N N   . ILE A 387 ? 0.7019 0.5351 0.7647 0.0305  -0.0112 -0.1235 924  ILE A N   
2970 C CA  . ILE A 387 ? 0.7834 0.6088 0.8547 0.0344  -0.0184 -0.1039 924  ILE A CA  
2971 C C   . ILE A 387 ? 0.8132 0.6184 0.8937 0.0302  -0.0274 -0.0944 924  ILE A C   
2972 O O   . ILE A 387 ? 0.7678 0.5671 0.8446 0.0232  -0.0280 -0.1002 924  ILE A O   
2973 C CB  . ILE A 387 ? 0.8185 0.6585 0.8685 0.0322  -0.0177 -0.0886 924  ILE A CB  
2974 C CG1 . ILE A 387 ? 0.7563 0.6061 0.7837 0.0235  -0.0155 -0.0882 924  ILE A CG1 
2975 C CG2 . ILE A 387 ? 0.8201 0.6746 0.8709 0.0387  -0.0116 -0.0926 924  ILE A CG2 
2976 C CD1 . ILE A 387 ? 0.7539 0.5924 0.7800 0.0160  -0.0215 -0.0806 924  ILE A CD1 
2977 N N   . ASN A 388 ? 0.7916 0.5861 0.8839 0.0336  -0.0349 -0.0789 925  ASN A N   
2978 C CA  . ASN A 388 ? 0.8151 0.5910 0.9134 0.0280  -0.0438 -0.0660 925  ASN A CA  
2979 C C   . ASN A 388 ? 0.8187 0.5994 0.8971 0.0217  -0.0468 -0.0448 925  ASN A C   
2980 O O   . ASN A 388 ? 0.6947 0.4876 0.7640 0.0249  -0.0453 -0.0380 925  ASN A O   
2981 C CB  . ASN A 388 ? 0.8086 0.5651 0.9374 0.0346  -0.0521 -0.0633 925  ASN A CB  
2982 C CG  . ASN A 388 ? 0.9311 0.6781 1.0836 0.0388  -0.0491 -0.0857 925  ASN A CG  
2983 O OD1 . ASN A 388 ? 1.0156 0.7592 1.1628 0.0323  -0.0462 -0.0968 925  ASN A OD1 
2984 N ND2 . ASN A 388 ? 1.0054 0.7489 1.1852 0.0493  -0.0497 -0.0937 925  ASN A ND2 
2985 N N   . PRO A 389 ? 0.7029 0.4755 0.7746 0.0121  -0.0500 -0.0357 926  PRO A N   
2986 C CA  . PRO A 389 ? 0.6278 0.4067 0.6806 0.0048  -0.0506 -0.0182 926  PRO A CA  
2987 C C   . PRO A 389 ? 0.5683 0.3400 0.6243 0.0064  -0.0581 -0.0013 926  PRO A C   
2988 O O   . PRO A 389 ? 0.5799 0.3365 0.6566 0.0114  -0.0657 0.0004  926  PRO A O   
2989 C CB  . PRO A 389 ? 0.7578 0.5273 0.8093 -0.0061 -0.0524 -0.0143 926  PRO A CB  
2990 C CG  . PRO A 389 ? 0.8301 0.5957 0.8927 -0.0047 -0.0505 -0.0335 926  PRO A CG  
2991 C CD  . PRO A 389 ? 0.7501 0.5097 0.8309 0.0064  -0.0517 -0.0435 926  PRO A CD  
2992 N N   . PRO A 390 ? 0.5312 0.3134 0.5682 0.0019  -0.0567 0.0111  927  PRO A N   
2993 C CA  . PRO A 390 ? 0.5417 0.3414 0.5590 -0.0033 -0.0479 0.0091  927  PRO A CA  
2994 C C   . PRO A 390 ? 0.5067 0.3241 0.5189 0.0041  -0.0409 -0.0019 927  PRO A C   
2995 O O   . PRO A 390 ? 0.5722 0.3918 0.5911 0.0122  -0.0421 -0.0044 927  PRO A O   
2996 C CB  . PRO A 390 ? 0.5585 0.3601 0.5609 -0.0111 -0.0495 0.0261  927  PRO A CB  
2997 C CG  . PRO A 390 ? 0.6394 0.4317 0.6494 -0.0065 -0.0586 0.0353  927  PRO A CG  
2998 C CD  . PRO A 390 ? 0.6311 0.4069 0.6656 -0.0004 -0.0649 0.0292  927  PRO A CD  
2999 N N   . CYS A 391 ? 0.4522 0.2824 0.4541 0.0008  -0.0342 -0.0078 928  CYS A N   
3000 C CA  . CYS A 391 ? 0.5236 0.3702 0.5194 0.0060  -0.0282 -0.0160 928  CYS A CA  
3001 C C   . CYS A 391 ? 0.5584 0.4181 0.5423 0.0002  -0.0233 -0.0131 928  CYS A C   
3002 O O   . CYS A 391 ? 0.5814 0.4386 0.5642 -0.0075 -0.0235 -0.0089 928  CYS A O   
3003 C CB  . CYS A 391 ? 0.5600 0.4079 0.5624 0.0102  -0.0262 -0.0317 928  CYS A CB  
3004 S SG  . CYS A 391 ? 0.5957 0.4431 0.5958 0.0019  -0.0259 -0.0382 928  CYS A SG  
3005 N N   . VAL A 392 ? 0.4050 0.2787 0.3825 0.0038  -0.0188 -0.0154 929  VAL A N   
3006 C CA  . VAL A 392 ? 0.3631 0.2497 0.3345 0.0001  -0.0147 -0.0150 929  VAL A CA  
3007 C C   . VAL A 392 ? 0.4651 0.3615 0.4349 0.0036  -0.0130 -0.0240 929  VAL A C   
3008 O O   . VAL A 392 ? 0.4493 0.3520 0.4166 0.0088  -0.0107 -0.0256 929  VAL A O   
3009 C CB  . VAL A 392 ? 0.3587 0.2528 0.3242 -0.0006 -0.0112 -0.0076 929  VAL A CB  
3010 C CG1 . VAL A 392 ? 0.3911 0.2967 0.3563 -0.0045 -0.0072 -0.0073 929  VAL A CG1 
3011 C CG2 . VAL A 392 ? 0.3914 0.2762 0.3543 -0.0048 -0.0134 0.0015  929  VAL A CG2 
3012 N N   . PRO A 393 ? 0.5140 0.4125 0.4843 -0.0001 -0.0143 -0.0296 930  PRO A N   
3013 C CA  . PRO A 393 ? 0.3941 0.3024 0.3592 0.0012  -0.0136 -0.0372 930  PRO A CA  
3014 C C   . PRO A 393 ? 0.4088 0.3307 0.3696 0.0016  -0.0116 -0.0315 930  PRO A C   
3015 O O   . PRO A 393 ? 0.4171 0.3421 0.3811 -0.0001 -0.0107 -0.0241 930  PRO A O   
3016 C CB  . PRO A 393 ? 0.5336 0.4408 0.4999 -0.0051 -0.0173 -0.0427 930  PRO A CB  
3017 C CG  . PRO A 393 ? 0.5127 0.4063 0.4873 -0.0081 -0.0193 -0.0399 930  PRO A CG  
3018 C CD  . PRO A 393 ? 0.5342 0.4267 0.5093 -0.0069 -0.0171 -0.0289 930  PRO A CD  
3019 N N   . PHE A 394 ? 0.3591 0.2891 0.3133 0.0035  -0.0105 -0.0355 931  PHE A N   
3020 C CA  . PHE A 394 ? 0.3342 0.2762 0.2854 0.0031  -0.0102 -0.0296 931  PHE A CA  
3021 C C   . PHE A 394 ? 0.4637 0.4113 0.4179 -0.0023 -0.0149 -0.0268 931  PHE A C   
3022 O O   . PHE A 394 ? 0.4492 0.3984 0.3989 -0.0065 -0.0189 -0.0322 931  PHE A O   
3023 C CB  . PHE A 394 ? 0.3780 0.3270 0.3198 0.0042  -0.0084 -0.0340 931  PHE A CB  
3024 C CG  . PHE A 394 ? 0.4362 0.3963 0.3746 0.0027  -0.0097 -0.0266 931  PHE A CG  
3025 C CD1 . PHE A 394 ? 0.4702 0.4322 0.4162 0.0052  -0.0085 -0.0181 931  PHE A CD1 
3026 C CD2 . PHE A 394 ? 0.4831 0.4514 0.4106 -0.0020 -0.0125 -0.0281 931  PHE A CD2 
3027 C CE1 . PHE A 394 ? 0.4926 0.4631 0.4391 0.0041  -0.0104 -0.0108 931  PHE A CE1 
3028 C CE2 . PHE A 394 ? 0.5951 0.5726 0.5204 -0.0039 -0.0153 -0.0188 931  PHE A CE2 
3029 C CZ  . PHE A 394 ? 0.4944 0.4721 0.4310 -0.0003 -0.0145 -0.0100 931  PHE A CZ  
3030 N N   . PHE A 395 ? 0.4249 0.3764 0.3880 -0.0025 -0.0145 -0.0193 932  PHE A N   
3031 C CA  . PHE A 395 ? 0.4704 0.4279 0.4424 -0.0071 -0.0188 -0.0166 932  PHE A CA  
3032 C C   . PHE A 395 ? 0.5124 0.4811 0.4830 -0.0087 -0.0246 -0.0131 932  PHE A C   
3033 O O   . PHE A 395 ? 0.4800 0.4537 0.4541 -0.0136 -0.0312 -0.0131 932  PHE A O   
3034 C CB  . PHE A 395 ? 0.6038 0.5628 0.5887 -0.0068 -0.0147 -0.0115 932  PHE A CB  
3035 C CG  . PHE A 395 ? 0.6076 0.5700 0.6050 -0.0120 -0.0167 -0.0109 932  PHE A CG  
3036 C CD1 . PHE A 395 ? 0.7529 0.7073 0.7494 -0.0164 -0.0172 -0.0144 932  PHE A CD1 
3037 C CD2 . PHE A 395 ? 0.6575 0.6310 0.6705 -0.0126 -0.0183 -0.0069 932  PHE A CD2 
3038 C CE1 . PHE A 395 ? 0.7533 0.7117 0.7626 -0.0222 -0.0186 -0.0139 932  PHE A CE1 
3039 C CE2 . PHE A 395 ? 0.7417 0.7202 0.7696 -0.0175 -0.0198 -0.0070 932  PHE A CE2 
3040 C CZ  . PHE A 395 ? 0.7838 0.7552 0.8090 -0.0227 -0.0197 -0.0106 932  PHE A CZ  
3041 N N   . GLY A 396 ? 0.5392 0.5118 0.5049 -0.0055 -0.0232 -0.0093 933  GLY A N   
3042 C CA  . GLY A 396 ? 0.5692 0.5519 0.5350 -0.0077 -0.0297 -0.0026 933  GLY A CA  
3043 C C   . GLY A 396 ? 0.5671 0.5541 0.5192 -0.0140 -0.0367 -0.0058 933  GLY A C   
3044 O O   . GLY A 396 ? 0.5632 0.5587 0.5179 -0.0182 -0.0456 0.0007  933  GLY A O   
3045 N N   . ILE A 397 ? 0.5075 0.4890 0.4459 -0.0152 -0.0333 -0.0162 934  ILE A N   
3046 C CA  . ILE A 397 ? 0.4619 0.4482 0.3848 -0.0224 -0.0387 -0.0218 934  ILE A CA  
3047 C C   . ILE A 397 ? 0.5256 0.5136 0.4558 -0.0280 -0.0470 -0.0226 934  ILE A C   
3048 O O   . ILE A 397 ? 0.4649 0.4614 0.3864 -0.0353 -0.0557 -0.0214 934  ILE A O   
3049 C CB  . ILE A 397 ? 0.6640 0.6439 0.5741 -0.0218 -0.0315 -0.0355 934  ILE A CB  
3050 C CG1 . ILE A 397 ? 0.6283 0.6139 0.5208 -0.0305 -0.0354 -0.0443 934  ILE A CG1 
3051 C CG2 . ILE A 397 ? 0.6356 0.6026 0.5572 -0.0178 -0.0273 -0.0423 934  ILE A CG2 
3052 C CD1 . ILE A 397 ? 0.7166 0.7016 0.5952 -0.0304 -0.0266 -0.0566 934  ILE A CD1 
3053 N N   . TYR A 398 ? 0.5778 0.5591 0.5239 -0.0259 -0.0449 -0.0239 935  TYR A N   
3054 C CA  . TYR A 398 ? 0.5272 0.5114 0.4835 -0.0317 -0.0522 -0.0242 935  TYR A CA  
3055 C C   . TYR A 398 ? 0.3905 0.3872 0.3603 -0.0330 -0.0604 -0.0125 935  TYR A C   
3056 O O   . TYR A 398 ? 0.4344 0.4394 0.4049 -0.0396 -0.0710 -0.0110 935  TYR A O   
3057 C CB  . TYR A 398 ? 0.5645 0.5391 0.5350 -0.0302 -0.0470 -0.0269 935  TYR A CB  
3058 C CG  . TYR A 398 ? 0.4843 0.4449 0.4464 -0.0290 -0.0412 -0.0370 935  TYR A CG  
3059 C CD1 . TYR A 398 ? 0.5227 0.4796 0.4755 -0.0341 -0.0442 -0.0481 935  TYR A CD1 
3060 C CD2 . TYR A 398 ? 0.4192 0.3704 0.3846 -0.0230 -0.0334 -0.0356 935  TYR A CD2 
3061 C CE1 . TYR A 398 ? 0.5630 0.5062 0.5134 -0.0321 -0.0392 -0.0579 935  TYR A CE1 
3062 C CE2 . TYR A 398 ? 0.4945 0.4326 0.4564 -0.0214 -0.0299 -0.0432 935  TYR A CE2 
3063 C CZ  . TYR A 398 ? 0.5444 0.4781 0.5007 -0.0254 -0.0326 -0.0545 935  TYR A CZ  
3064 O OH  . TYR A 398 ? 0.6173 0.5370 0.5749 -0.0229 -0.0293 -0.0628 935  TYR A OH  
3065 N N   . LEU A 399 ? 0.4804 0.4785 0.4632 -0.0267 -0.0562 -0.0044 936  LEU A N   
3066 C CA  . LEU A 399 ? 0.4044 0.4134 0.4053 -0.0262 -0.0634 0.0066  936  LEU A CA  
3067 C C   . LEU A 399 ? 0.4557 0.4729 0.4434 -0.0309 -0.0746 0.0133  936  LEU A C   
3068 O O   . LEU A 399 ? 0.4466 0.4736 0.4455 -0.0350 -0.0866 0.0204  936  LEU A O   
3069 C CB  . LEU A 399 ? 0.4132 0.4204 0.4269 -0.0186 -0.0555 0.0115  936  LEU A CB  
3070 C CG  . LEU A 399 ? 0.5426 0.5435 0.5680 -0.0155 -0.0446 0.0065  936  LEU A CG  
3071 C CD1 . LEU A 399 ? 0.4583 0.4572 0.4903 -0.0092 -0.0364 0.0092  936  LEU A CD1 
3072 C CD2 . LEU A 399 ? 0.6246 0.6324 0.6737 -0.0185 -0.0471 0.0067  936  LEU A CD2 
3073 N N   . THR A 400 ? 0.5031 0.5175 0.4672 -0.0312 -0.0711 0.0115  937  THR A N   
3074 C CA  . THR A 400 ? 0.4042 0.4268 0.3508 -0.0378 -0.0805 0.0181  937  THR A CA  
3075 C C   . THR A 400 ? 0.4093 0.4372 0.3428 -0.0477 -0.0899 0.0125  937  THR A C   
3076 O O   . THR A 400 ? 0.4779 0.5160 0.4102 -0.0543 -0.1037 0.0221  937  THR A O   
3077 C CB  . THR A 400 ? 0.4912 0.5103 0.4155 -0.0367 -0.0717 0.0150  937  THR A CB  
3078 O OG1 . THR A 400 ? 0.5382 0.5549 0.4759 -0.0293 -0.0666 0.0232  937  THR A OG1 
3079 C CG2 . THR A 400 ? 0.5811 0.6089 0.4803 -0.0464 -0.0792 0.0190  937  THR A CG2 
3080 N N   . ASN A 401 ? 0.5190 0.5397 0.4438 -0.0493 -0.0837 -0.0027 938  ASN A N   
3081 C CA  . ASN A 401 ? 0.5077 0.5324 0.4203 -0.0594 -0.0920 -0.0106 938  ASN A CA  
3082 C C   . ASN A 401 ? 0.4581 0.4896 0.3934 -0.0625 -0.1037 -0.0045 938  ASN A C   
3083 O O   . ASN A 401 ? 0.4496 0.4904 0.3770 -0.0721 -0.1167 -0.0031 938  ASN A O   
3084 C CB  . ASN A 401 ? 0.6760 0.6893 0.5800 -0.0595 -0.0821 -0.0289 938  ASN A CB  
3085 C CG  . ASN A 401 ? 0.8940 0.9041 0.7746 -0.0591 -0.0725 -0.0378 938  ASN A CG  
3086 O OD1 . ASN A 401 ? 0.8854 0.9042 0.7486 -0.0631 -0.0748 -0.0322 938  ASN A OD1 
3087 N ND2 . ASN A 401 ? 0.8682 0.8663 0.7500 -0.0547 -0.0619 -0.0513 938  ASN A ND2 
3088 N N   . ILE A 402 ? 0.5206 0.5492 0.4842 -0.0554 -0.0994 -0.0010 939  ILE A N   
3089 C CA  . ILE A 402 ? 0.5249 0.5621 0.5144 -0.0581 -0.1093 0.0044  939  ILE A CA  
3090 C C   . ILE A 402 ? 0.4694 0.5196 0.4695 -0.0590 -0.1229 0.0204  939  ILE A C   
3091 O O   . ILE A 402 ? 0.5094 0.5705 0.5166 -0.0661 -0.1378 0.0251  939  ILE A O   
3092 C CB  . ILE A 402 ? 0.5167 0.5485 0.5328 -0.0513 -0.0989 0.0026  939  ILE A CB  
3093 C CG1 . ILE A 402 ? 0.5465 0.5658 0.5536 -0.0532 -0.0900 -0.0110 939  ILE A CG1 
3094 C CG2 . ILE A 402 ? 0.4465 0.4904 0.4953 -0.0530 -0.1075 0.0094  939  ILE A CG2 
3095 C CD1 . ILE A 402 ? 0.6220 0.6336 0.6460 -0.0477 -0.0779 -0.0122 939  ILE A CD1 
3096 N N   . LEU A 403 ? 0.4848 0.5339 0.4869 -0.0522 -0.1190 0.0296  940  LEU A N   
3097 C CA  . LEU A 403 ? 0.5251 0.5845 0.5382 -0.0530 -0.1329 0.0464  940  LEU A CA  
3098 C C   . LEU A 403 ? 0.4895 0.5563 0.4738 -0.0646 -0.1471 0.0509  940  LEU A C   
3099 O O   . LEU A 403 ? 0.5070 0.5851 0.5019 -0.0698 -0.1647 0.0632  940  LEU A O   
3100 C CB  . LEU A 403 ? 0.5435 0.5978 0.5611 -0.0446 -0.1253 0.0540  940  LEU A CB  
3101 C CG  . LEU A 403 ? 0.5318 0.5824 0.5823 -0.0343 -0.1145 0.0525  940  LEU A CG  
3102 C CD1 . LEU A 403 ? 0.5115 0.5554 0.5609 -0.0273 -0.1058 0.0570  940  LEU A CD1 
3103 C CD2 . LEU A 403 ? 0.5600 0.6213 0.6496 -0.0331 -0.1251 0.0607  940  LEU A CD2 
3104 N N   . LYS A 404 ? 0.5235 0.5851 0.4718 -0.0694 -0.1399 0.0407  941  LYS A N   
3105 C CA  . LYS A 404 ? 0.5431 0.6127 0.4597 -0.0824 -0.1512 0.0420  941  LYS A CA  
3106 C C   . LYS A 404 ? 0.5961 0.6730 0.5162 -0.0914 -0.1640 0.0372  941  LYS A C   
3107 O O   . LYS A 404 ? 0.5543 0.6431 0.4673 -0.1013 -0.1821 0.0477  941  LYS A O   
3108 C CB  . LYS A 404 ? 0.6514 0.7144 0.5326 -0.0855 -0.1377 0.0273  941  LYS A CB  
3109 C CG  . LYS A 404 ? 0.8278 0.8888 0.6957 -0.0824 -0.1300 0.0344  941  LYS A CG  
3110 C CD  . LYS A 404 ? 1.0246 1.0824 0.8593 -0.0871 -0.1174 0.0180  941  LYS A CD  
3111 C CE  . LYS A 404 ? 1.1288 1.1853 0.9524 -0.0840 -0.1076 0.0234  941  LYS A CE  
3112 N NZ  . LYS A 404 ? 1.1868 1.2401 0.9866 -0.0860 -0.0923 0.0045  941  LYS A NZ  
3113 N N   . THR A 405 ? 0.5530 0.6230 0.4841 -0.0889 -0.1555 0.0222  942  THR A N   
3114 C CA  . THR A 405 ? 0.5706 0.6466 0.5064 -0.0980 -0.1664 0.0158  942  THR A CA  
3115 C C   . THR A 405 ? 0.5042 0.5924 0.4754 -0.0974 -0.1820 0.0307  942  THR A C   
3116 O O   . THR A 405 ? 0.5455 0.6452 0.5156 -0.1078 -0.1994 0.0340  942  THR A O   
3117 C CB  . THR A 405 ? 0.5071 0.5709 0.4494 -0.0951 -0.1530 -0.0022 942  THR A CB  
3118 O OG1 . THR A 405 ? 0.6356 0.6878 0.5514 -0.0935 -0.1384 -0.0152 942  THR A OG1 
3119 C CG2 . THR A 405 ? 0.5550 0.6237 0.4979 -0.1063 -0.1635 -0.0112 942  THR A CG2 
3120 N N   . GLU A 406 ? 0.4875 0.5741 0.4919 -0.0857 -0.1760 0.0386  943  GLU A N   
3121 C CA  . GLU A 406 ? 0.5453 0.6445 0.5890 -0.0839 -0.1895 0.0518  943  GLU A CA  
3122 C C   . GLU A 406 ? 0.5140 0.6244 0.5522 -0.0894 -0.2097 0.0703  943  GLU A C   
3123 O O   . GLU A 406 ? 0.5359 0.6597 0.5928 -0.0951 -0.2288 0.0794  943  GLU A O   
3124 C CB  . GLU A 406 ? 0.6149 0.7100 0.6936 -0.0704 -0.1767 0.0545  943  GLU A CB  
3125 C CG  . GLU A 406 ? 0.5598 0.6470 0.6507 -0.0666 -0.1599 0.0399  943  GLU A CG  
3126 C CD  . GLU A 406 ? 0.5434 0.6409 0.6630 -0.0716 -0.1672 0.0370  943  GLU A CD  
3127 O OE1 . GLU A 406 ? 0.5027 0.6149 0.6437 -0.0749 -0.1849 0.0478  943  GLU A OE1 
3128 O OE2 . GLU A 406 ? 0.5157 0.6065 0.6375 -0.0727 -0.1559 0.0248  943  GLU A OE2 
3129 N N   . GLU A 407 ? 0.5910 0.6964 0.6040 -0.0885 -0.2066 0.0770  944  GLU A N   
3130 C CA  . GLU A 407 ? 0.6159 0.7303 0.6232 -0.0941 -0.2256 0.0975  944  GLU A CA  
3131 C C   . GLU A 407 ? 0.5898 0.7130 0.5599 -0.1111 -0.2410 0.0975  944  GLU A C   
3132 O O   . GLU A 407 ? 0.6465 0.7818 0.6205 -0.1187 -0.2635 0.1150  944  GLU A O   
3133 C CB  . GLU A 407 ? 0.7672 0.8731 0.7601 -0.0887 -0.2161 0.1049  944  GLU A CB  
3134 C CG  . GLU A 407 ? 0.9283 1.0341 0.9618 -0.0777 -0.2195 0.1210  944  GLU A CG  
3135 C CD  . GLU A 407 ? 1.1155 1.2312 1.1543 -0.0843 -0.2440 0.1451  944  GLU A CD  
3136 O OE1 . GLU A 407 ? 1.2129 1.3348 1.2144 -0.0984 -0.2562 0.1501  944  GLU A OE1 
3137 O OE2 . GLU A 407 ? 1.1941 1.3115 1.2747 -0.0759 -0.2512 0.1589  944  GLU A OE2 
3138 N N   . GLY A 408 ? 0.6572 0.7611 0.6932 -0.2140 0.0765  0.2778  945  GLY A N   
3139 C CA  . GLY A 408 ? 0.6815 0.8574 0.6721 -0.2142 0.0949  0.2822  945  GLY A CA  
3140 C C   . GLY A 408 ? 0.6004 0.7764 0.5503 -0.1913 0.0987  0.2608  945  GLY A C   
3141 O O   . GLY A 408 ? 0.6120 0.8474 0.5196 -0.1912 0.1114  0.2619  945  GLY A O   
3142 N N   . ASN A 409 ? 0.5626 0.6716 0.5248 -0.1654 0.0842  0.2309  946  ASN A N   
3143 C CA  . ASN A 409 ? 0.6160 0.7168 0.5479 -0.1410 0.0816  0.2043  946  ASN A CA  
3144 C C   . ASN A 409 ? 0.6260 0.6609 0.5774 -0.1319 0.0534  0.2127  946  ASN A C   
3145 O O   . ASN A 409 ? 0.6208 0.6078 0.6112 -0.1267 0.0421  0.2060  946  ASN A O   
3146 C CB  . ASN A 409 ? 0.5228 0.6259 0.4536 -0.1152 0.0958  0.1500  946  ASN A CB  
3147 C CG  . ASN A 409 ? 0.6268 0.7945 0.5460 -0.1149 0.1206  0.1321  946  ASN A CG  
3148 O OD1 . ASN A 409 ? 0.6353 0.8448 0.5179 -0.1042 0.1299  0.1126  946  ASN A OD1 
3149 N ND2 . ASN A 409 ? 0.6466 0.8253 0.5994 -0.1244 0.1293  0.1351  946  ASN A ND2 
3150 N N   A ASN A 410 ? 0.6602 0.6975 0.5852 -0.1272 0.0413  0.2229  947  ASN A N   
3151 N N   B ASN A 410 ? 0.6632 0.7001 0.5887 -0.1276 0.0409  0.2238  947  ASN A N   
3152 C CA  A ASN A 410 ? 0.6508 0.6380 0.5980 -0.1147 0.0137  0.2298  947  ASN A CA  
3153 C CA  B ASN A 410 ? 0.6486 0.6339 0.5980 -0.1151 0.0133  0.2304  947  ASN A CA  
3154 C C   A ASN A 410 ? 0.6023 0.5709 0.5656 -0.0875 0.0168  0.1838  947  ASN A C   
3155 C C   B ASN A 410 ? 0.6022 0.5705 0.5659 -0.0877 0.0167  0.1842  947  ASN A C   
3156 O O   A ASN A 410 ? 0.5449 0.5385 0.4859 -0.0799 0.0324  0.1540  947  ASN A O   
3157 O O   B ASN A 410 ? 0.5432 0.5372 0.4841 -0.0805 0.0325  0.1548  947  ASN A O   
3158 C CB  A ASN A 410 ? 0.6846 0.6888 0.5996 -0.1202 -0.0023 0.2583  947  ASN A CB  
3159 C CB  B ASN A 410 ? 0.6866 0.6847 0.6071 -0.1210 -0.0048 0.2617  947  ASN A CB  
3160 C CG  A ASN A 410 ? 0.7088 0.7306 0.6085 -0.1517 -0.0116 0.3150  947  ASN A CG  
3161 C CG  B ASN A 410 ? 0.7173 0.6630 0.6736 -0.1140 -0.0402 0.2856  947  ASN A CG  
3162 O OD1 A ASN A 410 ? 0.7752 0.7642 0.7084 -0.1670 -0.0254 0.3440  947  ASN A OD1 
3163 O OD1 B ASN A 410 ? 0.6142 0.5371 0.5955 -0.0881 -0.0502 0.2591  947  ASN A OD1 
3164 N ND2 A ASN A 410 ? 0.6968 0.7718 0.5446 -0.1640 -0.0068 0.3323  947  ASN A ND2 
3165 N ND2 B ASN A 410 ? 0.7677 0.6974 0.7297 -0.1374 -0.0615 0.3370  947  ASN A ND2 
3166 N N   . ASP A 411 ? 0.5807 0.5075 0.5837 -0.0729 -0.0004 0.1780  948  ASP A N   
3167 C CA  . ASP A 411 ? 0.5346 0.4588 0.5524 -0.0503 0.0030  0.1399  948  ASP A CA  
3168 C C   . ASP A 411 ? 0.5266 0.4748 0.5247 -0.0437 -0.0026 0.1369  948  ASP A C   
3169 O O   . ASP A 411 ? 0.5553 0.5176 0.5526 -0.0352 0.0049  0.1096  948  ASP A O   
3170 C CB  . ASP A 411 ? 0.5603 0.4487 0.6237 -0.0320 -0.0140 0.1306  948  ASP A CB  
3171 C CG  . ASP A 411 ? 0.6651 0.5314 0.7487 -0.0328 -0.0072 0.1134  948  ASP A CG  
3172 O OD1 . ASP A 411 ? 0.5320 0.4162 0.5985 -0.0437 0.0135  0.1027  948  ASP A OD1 
3173 O OD2 . ASP A 411 ? 0.7689 0.5986 0.8874 -0.0203 -0.0263 0.1081  948  ASP A OD2 
3174 N N   . PHE A 412 ? 0.5345 0.4877 0.5173 -0.0505 -0.0192 0.1677  949  PHE A N   
3175 C CA  . PHE A 412 ? 0.5827 0.5576 0.5500 -0.0453 -0.0305 0.1670  949  PHE A CA  
3176 C C   . PHE A 412 ? 0.6254 0.6292 0.5388 -0.0625 -0.0288 0.1837  949  PHE A C   
3177 O O   . PHE A 412 ? 0.6323 0.6429 0.5264 -0.0790 -0.0250 0.2105  949  PHE A O   
3178 C CB  . PHE A 412 ? 0.5398 0.4992 0.5419 -0.0317 -0.0595 0.1853  949  PHE A CB  
3179 C CG  . PHE A 412 ? 0.5995 0.5462 0.6537 -0.0077 -0.0615 0.1592  949  PHE A CG  
3180 C CD1 . PHE A 412 ? 0.5030 0.4809 0.5722 0.0050  -0.0575 0.1336  949  PHE A CD1 
3181 C CD2 . PHE A 412 ? 0.6135 0.5218 0.7013 0.0009  -0.0689 0.1597  949  PHE A CD2 
3182 C CE1 . PHE A 412 ? 0.5424 0.5261 0.6565 0.0275  -0.0557 0.1081  949  PHE A CE1 
3183 C CE2 . PHE A 412 ? 0.5952 0.4991 0.7267 0.0272  -0.0702 0.1278  949  PHE A CE2 
3184 C CZ  . PHE A 412 ? 0.5750 0.5230 0.7181 0.0413  -0.0611 0.1017  949  PHE A CZ  
3185 N N   . LEU A 413 ? 0.5432 0.5689 0.4323 -0.0599 -0.0330 0.1674  950  LEU A N   
3186 C CA  . LEU A 413 ? 0.6338 0.6888 0.4704 -0.0713 -0.0399 0.1801  950  LEU A CA  
3187 C C   . LEU A 413 ? 0.6985 0.7518 0.5428 -0.0707 -0.0707 0.2112  950  LEU A C   
3188 O O   . LEU A 413 ? 0.6152 0.6626 0.4937 -0.0577 -0.0855 0.2018  950  LEU A O   
3189 C CB  . LEU A 413 ? 0.5752 0.6469 0.3817 -0.0682 -0.0356 0.1420  950  LEU A CB  
3190 C CG  . LEU A 413 ? 0.6379 0.7034 0.4489 -0.0636 -0.0122 0.1083  950  LEU A CG  
3191 C CD1 . LEU A 413 ? 0.6100 0.6761 0.4022 -0.0591 -0.0188 0.0715  950  LEU A CD1 
3192 C CD2 . LEU A 413 ? 0.6589 0.7479 0.4447 -0.0710 0.0087  0.1151  950  LEU A CD2 
3193 N N   . LYS A 414 ? 0.7890 0.8536 0.6036 -0.0858 -0.0814 0.2506  951  LYS A N   
3194 C CA  . LYS A 414 ? 0.8772 0.9340 0.7036 -0.0855 -0.1161 0.2875  951  LYS A CA  
3195 C C   . LYS A 414 ? 0.8898 0.9756 0.6844 -0.0847 -0.1329 0.2778  951  LYS A C   
3196 O O   . LYS A 414 ? 0.9067 1.0245 0.6430 -0.0948 -0.1233 0.2635  951  LYS A O   
3197 C CB  . LYS A 414 ? 0.9872 1.0447 0.7913 -0.1079 -0.1261 0.3411  951  LYS A CB  
3198 C CG  . LYS A 414 ? 1.0685 1.0998 0.9012 -0.1146 -0.1096 0.3486  951  LYS A CG  
3199 C CD  . LYS A 414 ? 1.2235 1.2547 1.0412 -0.1440 -0.1235 0.4096  951  LYS A CD  
3200 C CE  . LYS A 414 ? 1.1860 1.2472 0.9857 -0.1640 -0.0892 0.4072  951  LYS A CE  
3201 N NZ  . LYS A 414 ? 1.1769 1.3105 0.9142 -0.1775 -0.0688 0.4012  951  LYS A NZ  
3202 N N   . LYS A 415 ? 0.9461 1.0242 0.7824 -0.0708 -0.1594 0.2813  952  LYS A N   
3203 C CA  . LYS A 415 ? 0.8894 0.9942 0.7074 -0.0715 -0.1821 0.2757  952  LYS A CA  
3204 C C   . LYS A 415 ? 0.9173 1.0192 0.7622 -0.0663 -0.2214 0.3161  952  LYS A C   
3205 O O   . LYS A 415 ? 0.9064 0.9785 0.7963 -0.0562 -0.2321 0.3401  952  LYS A O   
3206 C CB  . LYS A 415 ? 0.7847 0.8962 0.6375 -0.0606 -0.1769 0.2348  952  LYS A CB  
3207 C CG  . LYS A 415 ? 0.7543 0.8641 0.5808 -0.0658 -0.1485 0.1954  952  LYS A CG  
3208 C CD  . LYS A 415 ? 0.8805 1.0085 0.6324 -0.0789 -0.1494 0.1852  952  LYS A CD  
3209 C CE  . LYS A 415 ? 0.8843 1.0049 0.6197 -0.0778 -0.1282 0.1403  952  LYS A CE  
3210 N NZ  . LYS A 415 ? 0.9117 1.0522 0.5771 -0.0824 -0.1216 0.1213  952  LYS A NZ  
3211 N N   . LYS A 416 ? 0.8253 0.9552 0.6445 -0.0719 -0.2475 0.3215  953  LYS A N   
3212 C CA  . LYS A 416 ? 0.9525 1.0841 0.8032 -0.0644 -0.2898 0.3578  953  LYS A CA  
3213 C C   . LYS A 416 ? 0.9933 1.1188 0.9352 -0.0359 -0.2969 0.3427  953  LYS A C   
3214 O O   . LYS A 416 ? 1.1115 1.2153 1.1034 -0.0185 -0.3204 0.3678  953  LYS A O   
3215 C CB  . LYS A 416 ? 0.9973 1.1652 0.8034 -0.0766 -0.3172 0.3614  953  LYS A CB  
3216 C CG  . LYS A 416 ? 1.0717 1.2432 0.9263 -0.0638 -0.3552 0.3842  953  LYS A CG  
3217 C CD  . LYS A 416 ? 1.1327 1.3285 0.9367 -0.0779 -0.3749 0.3884  953  LYS A CD  
3218 C CE  . LYS A 416 ? 1.2046 1.3936 1.0491 -0.0671 -0.4096 0.4215  953  LYS A CE  
3219 N NZ  . LYS A 416 ? 1.2824 1.4954 1.0780 -0.0808 -0.4315 0.4293  953  LYS A NZ  
3220 N N   . GLY A 417 ? 0.8102 0.9577 0.7757 -0.0304 -0.2790 0.3015  954  GLY A N   
3221 C CA  . GLY A 417 ? 0.7824 0.9418 0.8301 -0.0047 -0.2768 0.2828  954  GLY A CA  
3222 C C   . GLY A 417 ? 0.8444 0.9777 0.9121 0.0050  -0.2415 0.2597  954  GLY A C   
3223 O O   . GLY A 417 ? 1.0082 1.1014 1.0554 0.0015  -0.2336 0.2743  954  GLY A O   
3224 N N   . LYS A 418 ? 0.7693 0.9295 0.8765 0.0140  -0.2219 0.2265  955  LYS A N   
3225 C CA  . LYS A 418 ? 0.7215 0.8626 0.8446 0.0227  -0.1899 0.2023  955  LYS A CA  
3226 C C   . LYS A 418 ? 0.7143 0.8236 0.7731 0.0000  -0.1659 0.1988  955  LYS A C   
3227 O O   . LYS A 418 ? 0.7330 0.8529 0.7456 -0.0200 -0.1618 0.1914  955  LYS A O   
3228 C CB  . LYS A 418 ? 0.7621 0.9510 0.9266 0.0285  -0.1734 0.1721  955  LYS A CB  
3229 C CG  . LYS A 418 ? 0.8434 1.0238 1.0321 0.0425  -0.1445 0.1463  955  LYS A CG  
3230 C CD  . LYS A 418 ? 0.9366 1.1836 1.1788 0.0540  -0.1347 0.1239  955  LYS A CD  
3231 C CE  . LYS A 418 ? 1.0032 1.2893 1.2284 0.0235  -0.1331 0.1245  955  LYS A CE  
3232 N NZ  . LYS A 418 ? 1.0173 1.3873 1.3028 0.0300  -0.1354 0.1183  955  LYS A NZ  
3233 N N   . ASP A 419 ? 0.7316 0.8030 0.7903 0.0044  -0.1534 0.2027  956  ASP A N   
3234 C CA  . ASP A 419 ? 0.6936 0.7459 0.7014 -0.0147 -0.1288 0.1982  956  ASP A CA  
3235 C C   . ASP A 419 ? 0.6251 0.6861 0.6377 -0.0154 -0.1013 0.1616  956  ASP A C   
3236 O O   . ASP A 419 ? 0.6090 0.6830 0.6674 -0.0008 -0.0958 0.1438  956  ASP A O   
3241 N N   . LEU A 420 ? 0.5687 0.6272 0.5334 -0.0319 -0.0858 0.1504  957  LEU A N   
3242 C CA  . LEU A 420 ? 0.4790 0.5400 0.4439 -0.0355 -0.0671 0.1201  957  LEU A CA  
3243 C C   . LEU A 420 ? 0.4594 0.4973 0.4301 -0.0323 -0.0437 0.1108  957  LEU A C   
3244 O O   . LEU A 420 ? 0.5020 0.5237 0.4584 -0.0354 -0.0389 0.1261  957  LEU A O   
3245 C CB  . LEU A 420 ? 0.5661 0.6309 0.4817 -0.0499 -0.0695 0.1064  957  LEU A CB  
3246 C CG  . LEU A 420 ? 0.5866 0.6703 0.4831 -0.0567 -0.0968 0.1149  957  LEU A CG  
3247 C CD1 . LEU A 420 ? 0.6149 0.6949 0.4639 -0.0673 -0.1017 0.0903  957  LEU A CD1 
3248 C CD2 . LEU A 420 ? 0.5094 0.6171 0.4562 -0.0538 -0.1126 0.1188  957  LEU A CD2 
3249 N N   . ILE A 421 ? 0.4248 0.4659 0.4171 -0.0296 -0.0310 0.0890  958  ILE A N   
3250 C CA  . ILE A 421 ? 0.4064 0.4281 0.4001 -0.0288 -0.0109 0.0764  958  ILE A CA  
3251 C C   . ILE A 421 ? 0.4439 0.4573 0.3953 -0.0399 -0.0017 0.0702  958  ILE A C   
3252 O O   . ILE A 421 ? 0.4397 0.4590 0.3678 -0.0463 -0.0074 0.0574  958  ILE A O   
3253 C CB  . ILE A 421 ? 0.4027 0.4377 0.4211 -0.0266 -0.0025 0.0569  958  ILE A CB  
3254 C CG1 . ILE A 421 ? 0.3963 0.4553 0.4592 -0.0101 -0.0078 0.0568  958  ILE A CG1 
3255 C CG2 . ILE A 421 ? 0.3587 0.3741 0.3729 -0.0280 0.0151  0.0431  958  ILE A CG2 
3256 C CD1 . ILE A 421 ? 0.4112 0.5111 0.4950 -0.0127 -0.0021 0.0439  958  ILE A CD1 
3257 N N   . ASN A 422 ? 0.4573 0.4596 0.4018 -0.0416 0.0100  0.0777  959  ASN A N   
3258 C CA  . ASN A 422 ? 0.4322 0.4411 0.3438 -0.0481 0.0228  0.0680  959  ASN A CA  
3259 C C   . ASN A 422 ? 0.4178 0.4167 0.3413 -0.0452 0.0336  0.0423  959  ASN A C   
3260 O O   . ASN A 422 ? 0.4560 0.4453 0.3994 -0.0443 0.0445  0.0420  959  ASN A O   
3261 C CB  . ASN A 422 ? 0.4536 0.4676 0.3591 -0.0558 0.0311  0.0915  959  ASN A CB  
3262 C CG  . ASN A 422 ? 0.5425 0.5829 0.4186 -0.0604 0.0482  0.0796  959  ASN A CG  
3263 O OD1 . ASN A 422 ? 0.5252 0.5701 0.3879 -0.0528 0.0512  0.0486  959  ASN A OD1 
3264 N ND2 . ASN A 422 ? 0.5117 0.5728 0.3805 -0.0728 0.0571  0.1048  959  ASN A ND2 
3265 N N   . PHE A 423 ? 0.4247 0.4221 0.3369 -0.0453 0.0260  0.0226  960  PHE A N   
3266 C CA  . PHE A 423 ? 0.4533 0.4372 0.3780 -0.0446 0.0300  0.0041  960  PHE A CA  
3267 C C   . PHE A 423 ? 0.4559 0.4411 0.3676 -0.0398 0.0411  -0.0115 960  PHE A C   
3268 O O   . PHE A 423 ? 0.4274 0.4039 0.3563 -0.0382 0.0480  -0.0195 960  PHE A O   
3269 C CB  . PHE A 423 ? 0.4417 0.4175 0.3648 -0.0506 0.0115  -0.0058 960  PHE A CB  
3270 C CG  . PHE A 423 ? 0.4040 0.3655 0.3423 -0.0544 0.0107  -0.0147 960  PHE A CG  
3271 C CD1 . PHE A 423 ? 0.4404 0.4122 0.4036 -0.0585 0.0166  -0.0052 960  PHE A CD1 
3272 C CD2 . PHE A 423 ? 0.4096 0.3505 0.3372 -0.0516 0.0026  -0.0339 960  PHE A CD2 
3273 C CE1 . PHE A 423 ? 0.4417 0.4058 0.4131 -0.0649 0.0151  -0.0092 960  PHE A CE1 
3274 C CE2 . PHE A 423 ? 0.4384 0.3635 0.3801 -0.0566 -0.0029 -0.0367 960  PHE A CE2 
3275 C CZ  . PHE A 423 ? 0.4830 0.4210 0.4439 -0.0658 0.0037  -0.0216 960  PHE A CZ  
3276 N N   . SER A 424 ? 0.4651 0.4692 0.3472 -0.0365 0.0429  -0.0172 961  SER A N   
3277 C CA  . SER A 424 ? 0.4945 0.5171 0.3684 -0.0284 0.0562  -0.0353 961  SER A CA  
3278 C C   . SER A 424 ? 0.5147 0.5483 0.4131 -0.0337 0.0748  -0.0188 961  SER A C   
3279 O O   . SER A 424 ? 0.4533 0.4943 0.3654 -0.0279 0.0834  -0.0338 961  SER A O   
3280 C CB  . SER A 424 ? 0.5989 0.6572 0.4335 -0.0240 0.0587  -0.0429 961  SER A CB  
3281 O OG  . SER A 424 ? 0.6755 0.7177 0.4892 -0.0151 0.0377  -0.0718 961  SER A OG  
3282 N N   . LYS A 425 ? 0.4142 0.4461 0.3223 -0.0444 0.0766  0.0118  962  LYS A N   
3283 C CA  . LYS A 425 ? 0.4554 0.4854 0.3913 -0.0520 0.0863  0.0274  962  LYS A CA  
3284 C C   . LYS A 425 ? 0.5087 0.5137 0.4711 -0.0470 0.0850  0.0101  962  LYS A C   
3285 O O   . LYS A 425 ? 0.4259 0.4384 0.4051 -0.0487 0.0934  0.0056  962  LYS A O   
3286 C CB  . LYS A 425 ? 0.4424 0.4573 0.3895 -0.0612 0.0779  0.0594  962  LYS A CB  
3287 C CG  . LYS A 425 ? 0.4650 0.4639 0.4447 -0.0701 0.0790  0.0742  962  LYS A CG  
3288 C CD  . LYS A 425 ? 0.5153 0.4873 0.5099 -0.0749 0.0618  0.1024  962  LYS A CD  
3289 C CE  . LYS A 425 ? 0.4385 0.3863 0.4659 -0.0860 0.0557  0.1171  962  LYS A CE  
3290 N NZ  . LYS A 425 ? 0.4832 0.3942 0.5299 -0.0887 0.0311  0.1438  962  LYS A NZ  
3291 N N   . ARG A 426 ? 0.3878 0.3704 0.3542 -0.0429 0.0737  0.0027  963  ARG A N   
3292 C CA  . ARG A 426 ? 0.4260 0.3926 0.4114 -0.0414 0.0717  -0.0093 963  ARG A CA  
3293 C C   . ARG A 426 ? 0.4256 0.3929 0.4073 -0.0372 0.0706  -0.0288 963  ARG A C   
3294 O O   . ARG A 426 ? 0.4404 0.4031 0.4385 -0.0373 0.0723  -0.0349 963  ARG A O   
3295 C CB  . ARG A 426 ? 0.3898 0.3496 0.3784 -0.0412 0.0615  -0.0092 963  ARG A CB  
3296 C CG  . ARG A 426 ? 0.3945 0.3527 0.4027 -0.0377 0.0613  0.0001  963  ARG A CG  
3297 C CD  . ARG A 426 ? 0.3628 0.3214 0.3684 -0.0370 0.0578  0.0190  963  ARG A CD  
3298 N NE  . ARG A 426 ? 0.3726 0.3235 0.4028 -0.0283 0.0501  0.0243  963  ARG A NE  
3299 C CZ  . ARG A 426 ? 0.4237 0.3731 0.4582 -0.0245 0.0391  0.0413  963  ARG A CZ  
3300 N NH1 . ARG A 426 ? 0.3886 0.3481 0.3980 -0.0322 0.0361  0.0568  963  ARG A NH1 
3301 N NH2 . ARG A 426 ? 0.3972 0.3364 0.4610 -0.0108 0.0283  0.0404  963  ARG A NH2 
3302 N N   . ARG A 427 ? 0.4710 0.4420 0.4323 -0.0316 0.0638  -0.0408 964  ARG A N   
3303 C CA  . ARG A 427 ? 0.4373 0.4042 0.3988 -0.0215 0.0570  -0.0642 964  ARG A CA  
3304 C C   . ARG A 427 ? 0.5156 0.5116 0.4910 -0.0154 0.0732  -0.0700 964  ARG A C   
3305 O O   . ARG A 427 ? 0.4378 0.4290 0.4325 -0.0098 0.0693  -0.0816 964  ARG A O   
3306 C CB  . ARG A 427 ? 0.4792 0.4436 0.4157 -0.0128 0.0437  -0.0821 964  ARG A CB  
3307 C CG  . ARG A 427 ? 0.4732 0.4280 0.4130 0.0044  0.0306  -0.1133 964  ARG A CG  
3308 C CD  . ARG A 427 ? 0.5999 0.5459 0.5136 0.0157  0.0121  -0.1380 964  ARG A CD  
3309 N NE  . ARG A 427 ? 0.6629 0.5727 0.5696 0.0001  -0.0120 -0.1259 964  ARG A NE  
3310 C CZ  . ARG A 427 ? 0.6473 0.5663 0.5339 -0.0089 -0.0132 -0.1146 964  ARG A CZ  
3311 N NH1 . ARG A 427 ? 0.5686 0.5267 0.4350 -0.0043 0.0065  -0.1121 964  ARG A NH1 
3312 N NH2 . ARG A 427 ? 0.6026 0.4963 0.4905 -0.0249 -0.0364 -0.1027 964  ARG A NH2 
3313 N N   . LYS A 428 ? 0.3861 0.4173 0.3538 -0.0191 0.0898  -0.0582 965  LYS A N   
3314 C CA  . LYS A 428 ? 0.4199 0.4927 0.4047 -0.0197 0.1068  -0.0567 965  LYS A CA  
3315 C C   . LYS A 428 ? 0.4028 0.4600 0.4203 -0.0299 0.1068  -0.0454 965  LYS A C   
3316 O O   . LYS A 428 ? 0.3848 0.4627 0.4259 -0.0259 0.1107  -0.0552 965  LYS A O   
3317 C CB  . LYS A 428 ? 0.4684 0.5832 0.4381 -0.0317 0.1220  -0.0331 965  LYS A CB  
3318 C CG  . LYS A 428 ? 0.5792 0.7210 0.5099 -0.0225 0.1231  -0.0451 965  LYS A CG  
3319 C CD  . LYS A 428 ? 0.7573 0.9402 0.6699 -0.0409 0.1352  -0.0109 965  LYS A CD  
3320 C CE  . LYS A 428 ? 0.9504 1.1662 0.8167 -0.0329 0.1354  -0.0229 965  LYS A CE  
3321 N NZ  . LYS A 428 ? 1.0742 1.3353 0.9193 -0.0551 0.1453  0.0174  965  LYS A NZ  
3322 N N   . VAL A 429 ? 0.4223 0.4465 0.4432 -0.0408 0.1006  -0.0281 966  VAL A N   
3323 C CA  . VAL A 429 ? 0.4664 0.4731 0.5134 -0.0480 0.0970  -0.0246 966  VAL A CA  
3324 C C   . VAL A 429 ? 0.4346 0.4247 0.4864 -0.0396 0.0860  -0.0443 966  VAL A C   
3325 O O   . VAL A 429 ? 0.3980 0.3929 0.4711 -0.0409 0.0840  -0.0493 966  VAL A O   
3326 C CB  . VAL A 429 ? 0.4466 0.4241 0.4959 -0.0550 0.0906  -0.0101 966  VAL A CB  
3327 C CG1 . VAL A 429 ? 0.4644 0.4216 0.5339 -0.0575 0.0832  -0.0173 966  VAL A CG1 
3328 C CG2 . VAL A 429 ? 0.4450 0.4316 0.4972 -0.0668 0.0942  0.0161  966  VAL A CG2 
3329 N N   . ALA A 430 ? 0.4001 0.3713 0.4333 -0.0339 0.0752  -0.0520 967  ALA A N   
3330 C CA  . ALA A 430 ? 0.4771 0.4301 0.5132 -0.0309 0.0594  -0.0628 967  ALA A CA  
3331 C C   . ALA A 430 ? 0.4623 0.4270 0.5125 -0.0180 0.0549  -0.0797 967  ALA A C   
3332 O O   . ALA A 430 ? 0.4495 0.4024 0.5131 -0.0168 0.0410  -0.0843 967  ALA A O   
3333 C CB  . ALA A 430 ? 0.4281 0.3610 0.4446 -0.0329 0.0449  -0.0618 967  ALA A CB  
3334 N N   . GLU A 431 ? 0.4103 0.4034 0.4580 -0.0065 0.0650  -0.0905 968  GLU A N   
3335 C CA  . GLU A 431 ? 0.4714 0.4893 0.5391 0.0119  0.0630  -0.1127 968  GLU A CA  
3336 C C   . GLU A 431 ? 0.4766 0.5187 0.5773 0.0055  0.0702  -0.1058 968  GLU A C   
3337 O O   . GLU A 431 ? 0.4130 0.4574 0.5379 0.0169  0.0575  -0.1192 968  GLU A O   
3338 C CB  . GLU A 431 ? 0.5719 0.6362 0.6290 0.0256  0.0787  -0.1275 968  GLU A CB  
3339 C CG  . GLU A 431 ? 0.8815 0.9267 0.9033 0.0317  0.0702  -0.1372 968  GLU A CG  
3340 C CD  . GLU A 431 ? 1.0928 1.1122 1.1137 0.0561  0.0442  -0.1718 968  GLU A CD  
3341 O OE1 . GLU A 431 ? 1.1417 1.1355 1.1356 0.0591  0.0296  -0.1816 968  GLU A OE1 
3342 O OE2 . GLU A 431 ? 1.1546 1.1763 1.2044 0.0725  0.0340  -0.1898 968  GLU A OE2 
3343 N N   . ILE A 432 ? 0.3869 0.4440 0.4917 -0.0132 0.0859  -0.0841 969  ILE A N   
3344 C CA  . ILE A 432 ? 0.3614 0.4402 0.4994 -0.0239 0.0894  -0.0758 969  ILE A CA  
3345 C C   . ILE A 432 ? 0.4054 0.4438 0.5483 -0.0294 0.0703  -0.0759 969  ILE A C   
3346 O O   . ILE A 432 ? 0.3977 0.4476 0.5674 -0.0282 0.0615  -0.0814 969  ILE A O   
3347 C CB  . ILE A 432 ? 0.3957 0.4920 0.5371 -0.0456 0.1041  -0.0500 969  ILE A CB  
3348 C CG1 . ILE A 432 ? 0.4070 0.5554 0.5376 -0.0431 0.1231  -0.0459 969  ILE A CG1 
3349 C CG2 . ILE A 432 ? 0.4425 0.5522 0.6206 -0.0621 0.1014  -0.0393 969  ILE A CG2 
3350 C CD1 . ILE A 432 ? 0.4896 0.6514 0.6189 -0.0686 0.1326  -0.0116 969  ILE A CD1 
3351 N N   . THR A 433 ? 0.4048 0.4037 0.5216 -0.0354 0.0633  -0.0702 970  THR A N   
3352 C CA  . THR A 433 ? 0.3779 0.3516 0.4924 -0.0413 0.0472  -0.0708 970  THR A CA  
3353 C C   . THR A 433 ? 0.3894 0.3522 0.5044 -0.0317 0.0272  -0.0794 970  THR A C   
3354 O O   . THR A 433 ? 0.3983 0.3534 0.5190 -0.0366 0.0115  -0.0784 970  THR A O   
3355 C CB  . THR A 433 ? 0.4386 0.3897 0.5272 -0.0485 0.0473  -0.0645 970  THR A CB  
3356 O OG1 . THR A 433 ? 0.4521 0.3942 0.5194 -0.0439 0.0448  -0.0633 970  THR A OG1 
3357 C CG2 . THR A 433 ? 0.4140 0.3660 0.5074 -0.0544 0.0594  -0.0569 970  THR A CG2 
3358 N N   . GLY A 434 ? 0.3368 0.2962 0.4461 -0.0178 0.0230  -0.0882 971  GLY A N   
3359 C CA  . GLY A 434 ? 0.4074 0.3472 0.5241 -0.0065 -0.0037 -0.0970 971  GLY A CA  
3360 C C   . GLY A 434 ? 0.4480 0.4128 0.6023 0.0059  -0.0097 -0.1082 971  GLY A C   
3361 O O   . GLY A 434 ? 0.4141 0.3600 0.5798 0.0095  -0.0368 -0.1083 971  GLY A O   
3362 N N   . GLU A 435 ? 0.3854 0.3979 0.5619 0.0100  0.0138  -0.1140 972  GLU A N   
3363 C CA  . GLU A 435 ? 0.4449 0.4968 0.6649 0.0194  0.0109  -0.1231 972  GLU A CA  
3364 C C   . GLU A 435 ? 0.3772 0.4194 0.6067 0.0003  -0.0007 -0.1089 972  GLU A C   
3365 O O   . GLU A 435 ? 0.4128 0.4613 0.6700 0.0077  -0.0213 -0.1139 972  GLU A O   
3366 C CB  . GLU A 435 ? 0.4641 0.5821 0.7051 0.0208  0.0407  -0.1258 972  GLU A CB  
3367 C CG  . GLU A 435 ? 0.6003 0.7448 0.8302 0.0423  0.0539  -0.1449 972  GLU A CG  
3368 C CD  . GLU A 435 ? 0.8642 1.0965 1.1219 0.0451  0.0815  -0.1483 972  GLU A CD  
3369 O OE1 . GLU A 435 ? 0.8815 1.1490 1.1724 0.0274  0.0876  -0.1322 972  GLU A OE1 
3370 O OE2 . GLU A 435 ? 0.9642 1.2354 1.2103 0.0632  0.0960  -0.1665 972  GLU A OE2 
3371 N N   . ILE A 436 ? 0.3393 0.3666 0.5472 -0.0221 0.0095  -0.0941 973  ILE A N   
3372 C CA  . ILE A 436 ? 0.3371 0.3540 0.5478 -0.0387 -0.0032 -0.0873 973  ILE A CA  
3373 C C   . ILE A 436 ? 0.3943 0.3822 0.5888 -0.0370 -0.0314 -0.0860 973  ILE A C   
3374 O O   . ILE A 436 ? 0.4070 0.4001 0.6179 -0.0403 -0.0510 -0.0855 973  ILE A O   
3375 C CB  . ILE A 436 ? 0.3640 0.3622 0.5502 -0.0558 0.0083  -0.0796 973  ILE A CB  
3376 C CG1 . ILE A 436 ? 0.4530 0.4754 0.6606 -0.0640 0.0278  -0.0725 973  ILE A CG1 
3377 C CG2 . ILE A 436 ? 0.3821 0.3650 0.5602 -0.0681 -0.0088 -0.0813 973  ILE A CG2 
3378 C CD1 . ILE A 436 ? 0.4470 0.4414 0.6371 -0.0768 0.0317  -0.0663 973  ILE A CD1 
3379 N N   . GLN A 437 ? 0.3576 0.3165 0.5204 -0.0349 -0.0368 -0.0817 974  GLN A N   
3380 C CA  . GLN A 437 ? 0.4018 0.3344 0.5445 -0.0417 -0.0653 -0.0707 974  GLN A CA  
3381 C C   . GLN A 437 ? 0.4478 0.3745 0.6203 -0.0267 -0.0955 -0.0738 974  GLN A C   
3382 O O   . GLN A 437 ? 0.4531 0.3629 0.6162 -0.0361 -0.1248 -0.0598 974  GLN A O   
3383 C CB  . GLN A 437 ? 0.4337 0.3419 0.5419 -0.0477 -0.0656 -0.0606 974  GLN A CB  
3384 C CG  . GLN A 437 ? 0.4692 0.3865 0.5500 -0.0606 -0.0416 -0.0572 974  GLN A CG  
3385 C CD  . GLN A 437 ? 0.5899 0.4947 0.6413 -0.0701 -0.0447 -0.0437 974  GLN A CD  
3386 O OE1 . GLN A 437 ? 0.5458 0.4400 0.5981 -0.0626 -0.0406 -0.0461 974  GLN A OE1 
3387 N NE2 . GLN A 437 ? 0.6183 0.5314 0.6431 -0.0882 -0.0526 -0.0292 974  GLN A NE2 
3388 N N   . GLN A 438 ? 0.4732 0.4180 0.6819 -0.0023 -0.0909 -0.0923 975  GLN A N   
3389 C CA  . GLN A 438 ? 0.5108 0.4505 0.7549 0.0195  -0.1231 -0.1014 975  GLN A CA  
3390 C C   . GLN A 438 ? 0.5103 0.4651 0.7764 0.0120  -0.1426 -0.0934 975  GLN A C   
3391 O O   . GLN A 438 ? 0.4709 0.4061 0.7545 0.0219  -0.1808 -0.0896 975  GLN A O   
3392 C CB  . GLN A 438 ? 0.5650 0.5439 0.8497 0.0513  -0.1091 -0.1304 975  GLN A CB  
3393 C CG  . GLN A 438 ? 0.7263 0.7007 0.9914 0.0630  -0.0905 -0.1447 975  GLN A CG  
3394 C CD  . GLN A 438 ? 0.9528 0.9875 1.2557 0.0939  -0.0720 -0.1758 975  GLN A CD  
3395 O OE1 . GLN A 438 ? 0.9036 0.9789 1.2542 0.1117  -0.0797 -0.1887 975  GLN A OE1 
3396 N NE2 . GLN A 438 ? 1.0425 1.0925 1.3243 0.1004  -0.0473 -0.1879 975  GLN A NE2 
3397 N N   . TYR A 439 ? 0.4329 0.4190 0.7009 -0.0051 -0.1217 -0.0910 976  TYR A N   
3398 C CA  . TYR A 439 ? 0.3925 0.4007 0.6874 -0.0118 -0.1396 -0.0881 976  TYR A CA  
3399 C C   . TYR A 439 ? 0.4011 0.3876 0.6521 -0.0392 -0.1531 -0.0717 976  TYR A C   
3400 O O   . TYR A 439 ? 0.4104 0.4140 0.6755 -0.0488 -0.1680 -0.0708 976  TYR A O   
3401 C CB  . TYR A 439 ? 0.3604 0.4232 0.6964 -0.0135 -0.1137 -0.0980 976  TYR A CB  
3402 C CG  . TYR A 439 ? 0.3675 0.4744 0.7460 0.0131  -0.0962 -0.1153 976  TYR A CG  
3403 C CD1 . TYR A 439 ? 0.3927 0.5337 0.8252 0.0398  -0.1153 -0.1294 976  TYR A CD1 
3404 C CD2 . TYR A 439 ? 0.4017 0.5226 0.7663 0.0135  -0.0616 -0.1193 976  TYR A CD2 
3405 C CE1 . TYR A 439 ? 0.4598 0.6542 0.9302 0.0685  -0.0971 -0.1519 976  TYR A CE1 
3406 C CE2 . TYR A 439 ? 0.3779 0.5503 0.7741 0.0378  -0.0439 -0.1373 976  TYR A CE2 
3407 C CZ  . TYR A 439 ? 0.4502 0.6625 0.8987 0.0664  -0.0601 -0.1561 976  TYR A CZ  
3408 O OH  . TYR A 439 ? 0.4928 0.7692 0.9721 0.0949  -0.0401 -0.1806 976  TYR A OH  
3409 N N   . GLN A 440 ? 0.4901 0.4335 0.5513 -0.1077 -0.0849 -0.0603 977  GLN A N   
3410 C CA  . GLN A 440 ? 0.4614 0.4349 0.5485 -0.1159 -0.0720 -0.0409 977  GLN A CA  
3411 C C   . GLN A 440 ? 0.5488 0.5080 0.6513 -0.1280 -0.0663 -0.0270 977  GLN A C   
3412 O O   . GLN A 440 ? 0.5633 0.5444 0.6810 -0.1331 -0.0529 -0.0103 977  GLN A O   
3413 C CB  . GLN A 440 ? 0.4545 0.4598 0.5692 -0.1274 -0.0798 -0.0380 977  GLN A CB  
3414 C CG  . GLN A 440 ? 0.4384 0.4665 0.5405 -0.1140 -0.0809 -0.0450 977  GLN A CG  
3415 C CD  . GLN A 440 ? 0.4319 0.4936 0.5656 -0.1242 -0.0895 -0.0403 977  GLN A CD  
3416 O OE1 . GLN A 440 ? 0.4534 0.5125 0.6102 -0.1408 -0.1063 -0.0422 977  GLN A OE1 
3417 N NE2 . GLN A 440 ? 0.4038 0.4973 0.5425 -0.1149 -0.0785 -0.0334 977  GLN A NE2 
3418 N N   . ASN A 441 ? 0.5768 0.4985 0.6741 -0.1319 -0.0750 -0.0325 978  ASN A N   
3419 C CA  . ASN A 441 ? 0.7722 0.6805 0.8841 -0.1431 -0.0691 -0.0162 978  ASN A CA  
3420 C C   . ASN A 441 ? 0.7578 0.6381 0.8474 -0.1296 -0.0626 -0.0153 978  ASN A C   
3421 O O   . ASN A 441 ? 0.8444 0.6915 0.9366 -0.1348 -0.0682 -0.0138 978  ASN A O   
3422 C CB  . ASN A 441 ? 0.9030 0.7906 1.0380 -0.1631 -0.0849 -0.0175 978  ASN A CB  
3423 C CG  . ASN A 441 ? 1.0843 0.9992 1.2458 -0.1770 -0.0961 -0.0200 978  ASN A CG  
3424 O OD1 . ASN A 441 ? 1.0586 1.0128 1.2296 -0.1745 -0.0875 -0.0136 978  ASN A OD1 
3425 N ND2 . ASN A 441 ? 1.1629 1.0558 1.3382 -0.1917 -0.1166 -0.0293 978  ASN A ND2 
3426 N N   . GLN A 442 ? 0.6781 0.5715 0.7490 -0.1126 -0.0514 -0.0151 979  GLN A N   
3427 C CA  . GLN A 442 ? 0.6875 0.5585 0.7401 -0.0974 -0.0470 -0.0159 979  GLN A CA  
3428 C C   . GLN A 442 ? 0.5727 0.4626 0.6213 -0.0920 -0.0334 -0.0003 979  GLN A C   
3429 O O   . GLN A 442 ? 0.6173 0.5228 0.6538 -0.0785 -0.0271 -0.0038 979  GLN A O   
3430 C CB  . GLN A 442 ? 0.7267 0.5904 0.7585 -0.0798 -0.0495 -0.0346 979  GLN A CB  
3431 C CG  . GLN A 442 ? 0.7851 0.6306 0.8119 -0.0832 -0.0641 -0.0532 979  GLN A CG  
3432 C CD  . GLN A 442 ? 0.8157 0.6522 0.8155 -0.0634 -0.0634 -0.0704 979  GLN A CD  
3433 O OE1 . GLN A 442 ? 0.7568 0.6049 0.7471 -0.0480 -0.0510 -0.0669 979  GLN A OE1 
3434 N NE2 . GLN A 442 ? 0.7276 0.5424 0.7142 -0.0639 -0.0766 -0.0888 979  GLN A NE2 
3435 N N   . PRO A 443 ? 0.4981 0.3852 0.5549 -0.1023 -0.0291 0.0173  980  PRO A N   
3436 C CA  . PRO A 443 ? 0.4645 0.3667 0.5119 -0.0977 -0.0180 0.0312  980  PRO A CA  
3437 C C   . PRO A 443 ? 0.5345 0.4213 0.5683 -0.0824 -0.0187 0.0309  980  PRO A C   
3438 O O   . PRO A 443 ? 0.5093 0.3684 0.5440 -0.0778 -0.0254 0.0270  980  PRO A O   
3439 C CB  . PRO A 443 ? 0.5716 0.4690 0.6282 -0.1131 -0.0143 0.0502  980  PRO A CB  
3440 C CG  . PRO A 443 ? 0.5903 0.4588 0.6608 -0.1223 -0.0252 0.0473  980  PRO A CG  
3441 C CD  . PRO A 443 ? 0.5682 0.4372 0.6420 -0.1195 -0.0344 0.0260  980  PRO A CD  
3442 N N   . TYR A 444 ? 0.4411 0.3461 0.4642 -0.0743 -0.0121 0.0351  981  TYR A N   
3443 C CA  . TYR A 444 ? 0.4395 0.3366 0.4548 -0.0610 -0.0132 0.0377  981  TYR A CA  
3444 C C   . TYR A 444 ? 0.4555 0.3412 0.4660 -0.0656 -0.0143 0.0560  981  TYR A C   
3445 O O   . TYR A 444 ? 0.5137 0.4084 0.5184 -0.0759 -0.0092 0.0670  981  TYR A O   
3446 C CB  . TYR A 444 ? 0.4275 0.3488 0.4356 -0.0517 -0.0080 0.0335  981  TYR A CB  
3447 C CG  . TYR A 444 ? 0.4008 0.3281 0.4104 -0.0412 -0.0075 0.0177  981  TYR A CG  
3448 C CD1 . TYR A 444 ? 0.3923 0.3335 0.4031 -0.0452 -0.0062 0.0082  981  TYR A CD1 
3449 C CD2 . TYR A 444 ? 0.4020 0.3215 0.4123 -0.0267 -0.0081 0.0135  981  TYR A CD2 
3450 C CE1 . TYR A 444 ? 0.3875 0.3324 0.3947 -0.0352 -0.0062 -0.0051 981  TYR A CE1 
3451 C CE2 . TYR A 444 ? 0.4319 0.3561 0.4398 -0.0162 -0.0053 0.0003  981  TYR A CE2 
3452 C CZ  . TYR A 444 ? 0.4132 0.3491 0.4168 -0.0206 -0.0048 -0.0090 981  TYR A CZ  
3453 O OH  . TYR A 444 ? 0.4186 0.3579 0.4149 -0.0100 -0.0026 -0.0211 981  TYR A OH  
3454 N N   . CYS A 445 ? 0.4724 0.3388 0.4845 -0.0567 -0.0203 0.0600  982  CYS A N   
3455 C CA  . CYS A 445 ? 0.5159 0.3711 0.5215 -0.0588 -0.0240 0.0786  982  CYS A CA  
3456 C C   . CYS A 445 ? 0.5269 0.3998 0.5208 -0.0523 -0.0241 0.0830  982  CYS A C   
3457 O O   . CYS A 445 ? 0.4963 0.3645 0.4932 -0.0424 -0.0310 0.0876  982  CYS A O   
3458 C CB  . CYS A 445 ? 0.5618 0.3883 0.5777 -0.0515 -0.0319 0.0822  982  CYS A CB  
3459 S SG  . CYS A 445 ? 0.6024 0.4115 0.6107 -0.0549 -0.0388 0.1079  982  CYS A SG  
3460 N N   . LEU A 446 ? 0.4560 0.3498 0.4386 -0.0579 -0.0169 0.0810  983  LEU A N   
3461 C CA  . LEU A 446 ? 0.4437 0.3526 0.4131 -0.0533 -0.0172 0.0819  983  LEU A CA  
3462 C C   . LEU A 446 ? 0.4889 0.4048 0.4370 -0.0629 -0.0104 0.0897  983  LEU A C   
3463 O O   . LEU A 446 ? 0.5061 0.4295 0.4563 -0.0710 -0.0007 0.0880  983  LEU A O   
3464 C CB  . LEU A 446 ? 0.4147 0.3423 0.3920 -0.0453 -0.0134 0.0666  983  LEU A CB  
3465 C CG  . LEU A 446 ? 0.4881 0.4122 0.4832 -0.0334 -0.0163 0.0579  983  LEU A CG  
3466 C CD1 . LEU A 446 ? 0.4341 0.3777 0.4327 -0.0274 -0.0100 0.0448  983  LEU A CD1 
3467 C CD2 . LEU A 446 ? 0.4644 0.3820 0.4659 -0.0250 -0.0250 0.0666  983  LEU A CD2 
3468 N N   . ARG A 447 ? 0.4647 0.3786 0.3924 -0.0617 -0.0153 0.0981  984  ARG A N   
3469 C CA  . ARG A 447 ? 0.5040 0.4205 0.4041 -0.0687 -0.0078 0.1055  984  ARG A CA  
3470 C C   . ARG A 447 ? 0.5071 0.4426 0.4000 -0.0659 0.0000  0.0929  984  ARG A C   
3471 O O   . ARG A 447 ? 0.4799 0.4213 0.3773 -0.0586 -0.0065 0.0843  984  ARG A O   
3472 C CB  . ARG A 447 ? 0.6001 0.5017 0.4747 -0.0684 -0.0187 0.1195  984  ARG A CB  
3473 C CG  . ARG A 447 ? 0.8172 0.7154 0.6570 -0.0754 -0.0095 0.1295  984  ARG A CG  
3474 C CD  . ARG A 447 ? 0.8594 0.7386 0.6710 -0.0755 -0.0224 0.1457  984  ARG A CD  
3475 N NE  . ARG A 447 ? 0.9110 0.7737 0.7391 -0.0765 -0.0311 0.1591  984  ARG A NE  
3476 C CZ  . ARG A 447 ? 0.8986 0.7502 0.7263 -0.0845 -0.0231 0.1729  984  ARG A CZ  
3477 N NH1 . ARG A 447 ? 0.8287 0.6873 0.6426 -0.0924 -0.0050 0.1762  984  ARG A NH1 
3478 N NH2 . ARG A 447 ? 0.9496 0.7830 0.7934 -0.0843 -0.0325 0.1844  984  ARG A NH2 
3479 N N   . ILE A 448 ? 0.4770 0.4220 0.3614 -0.0716 0.0147  0.0930  985  ILE A N   
3480 C CA  . ILE A 448 ? 0.4884 0.4491 0.3647 -0.0679 0.0234  0.0821  985  ILE A CA  
3481 C C   . ILE A 448 ? 0.4901 0.4419 0.3325 -0.0649 0.0184  0.0836  985  ILE A C   
3482 O O   . ILE A 448 ? 0.5289 0.4661 0.3447 -0.0684 0.0158  0.0956  985  ILE A O   
3483 C CB  . ILE A 448 ? 0.5124 0.4866 0.3920 -0.0735 0.0414  0.0837  985  ILE A CB  
3484 C CG1 . ILE A 448 ? 0.5500 0.5351 0.4653 -0.0768 0.0427  0.0788  985  ILE A CG1 
3485 C CG2 . ILE A 448 ? 0.5590 0.5459 0.4257 -0.0681 0.0518  0.0745  985  ILE A CG2 
3486 C CD1 . ILE A 448 ? 0.6772 0.6775 0.6045 -0.0846 0.0580  0.0837  985  ILE A CD1 
3487 N N   . GLU A 449 ? 0.4712 0.4296 0.3128 -0.0587 0.0156  0.0716  986  GLU A N   
3488 C CA  . GLU A 449 ? 0.5142 0.4635 0.3222 -0.0567 0.0113  0.0693  986  GLU A CA  
3489 C C   . GLU A 449 ? 0.4967 0.4553 0.2936 -0.0543 0.0284  0.0603  986  GLU A C   
3490 O O   . GLU A 449 ? 0.4729 0.4436 0.2891 -0.0496 0.0310  0.0492  986  GLU A O   
3491 C CB  . GLU A 449 ? 0.4702 0.4174 0.2877 -0.0522 -0.0062 0.0632  986  GLU A CB  
3492 C CG  . GLU A 449 ? 0.5231 0.4528 0.3078 -0.0534 -0.0220 0.0669  986  GLU A CG  
3493 C CD  . GLU A 449 ? 0.5682 0.4896 0.3126 -0.0531 -0.0144 0.0598  986  GLU A CD  
3494 O OE1 . GLU A 449 ? 0.6007 0.5051 0.3045 -0.0556 -0.0186 0.0662  986  GLU A OE1 
3495 O OE2 . GLU A 449 ? 0.5862 0.5164 0.3374 -0.0494 -0.0040 0.0478  986  GLU A OE2 
3496 N N   . PRO A 450 ? 0.5196 0.4728 0.2857 -0.0563 0.0414  0.0655  987  PRO A N   
3497 C CA  . PRO A 450 ? 0.5387 0.5041 0.3018 -0.0526 0.0617  0.0583  987  PRO A CA  
3498 C C   . PRO A 450 ? 0.5113 0.4745 0.2657 -0.0451 0.0593  0.0432  987  PRO A C   
3499 O O   . PRO A 450 ? 0.5296 0.5083 0.3049 -0.0404 0.0701  0.0354  987  PRO A O   
3500 C CB  . PRO A 450 ? 0.5703 0.5262 0.2955 -0.0549 0.0756  0.0685  987  PRO A CB  
3501 C CG  . PRO A 450 ? 0.6527 0.5975 0.3753 -0.0623 0.0651  0.0841  987  PRO A CG  
3502 C CD  . PRO A 450 ? 0.5533 0.4903 0.2880 -0.0612 0.0403  0.0800  987  PRO A CD  
3503 N N   . ASP A 451 ? 0.5363 0.4796 0.2615 -0.0442 0.0442  0.0395  988  ASP A N   
3504 C CA  . ASP A 451 ? 0.5420 0.4797 0.2608 -0.0385 0.0402  0.0250  988  ASP A CA  
3505 C C   . ASP A 451 ? 0.5303 0.4832 0.2936 -0.0365 0.0335  0.0197  988  ASP A C   
3506 O O   . ASP A 451 ? 0.5107 0.4702 0.2848 -0.0309 0.0412  0.0102  988  ASP A O   
3507 C CB  . ASP A 451 ? 0.5780 0.4904 0.2596 -0.0402 0.0209  0.0224  988  ASP A CB  
3508 C CG  . ASP A 451 ? 0.6994 0.5927 0.3253 -0.0393 0.0298  0.0234  988  ASP A CG  
3509 O OD1 . ASP A 451 ? 0.7562 0.6556 0.3730 -0.0344 0.0539  0.0209  988  ASP A OD1 
3510 O OD2 . ASP A 451 ? 0.7276 0.6004 0.3186 -0.0428 0.0131  0.0273  988  ASP A OD2 
3511 N N   . MET A 452 ? 0.4722 0.4293 0.2602 -0.0399 0.0199  0.0263  989  MET A N   
3512 C CA  . MET A 452 ? 0.4372 0.4085 0.2640 -0.0368 0.0162  0.0222  989  MET A CA  
3513 C C   . MET A 452 ? 0.4398 0.4305 0.2896 -0.0341 0.0325  0.0203  989  MET A C   
3514 O O   . MET A 452 ? 0.4138 0.4151 0.2834 -0.0291 0.0354  0.0139  989  MET A O   
3515 C CB  . MET A 452 ? 0.4790 0.4505 0.3263 -0.0391 0.0014  0.0299  989  MET A CB  
3516 C CG  . MET A 452 ? 0.4829 0.4395 0.3165 -0.0415 -0.0182 0.0329  989  MET A CG  
3517 S SD  . MET A 452 ? 0.4360 0.3974 0.3038 -0.0412 -0.0337 0.0426  989  MET A SD  
3518 C CE  . MET A 452 ? 0.3810 0.3616 0.2892 -0.0347 -0.0262 0.0358  989  MET A CE  
3519 N N   . ARG A 453 ? 0.4267 0.4226 0.2755 -0.0379 0.0423  0.0271  990  ARG A N   
3520 C CA  . ARG A 453 ? 0.4103 0.4259 0.2838 -0.0368 0.0548  0.0259  990  ARG A CA  
3521 C C   . ARG A 453 ? 0.4508 0.4740 0.3204 -0.0304 0.0679  0.0184  990  ARG A C   
3522 O O   . ARG A 453 ? 0.4657 0.5039 0.3590 -0.0258 0.0712  0.0137  990  ARG A O   
3523 C CB  . ARG A 453 ? 0.4167 0.4354 0.2920 -0.0440 0.0620  0.0359  990  ARG A CB  
3524 C CG  . ARG A 453 ? 0.5765 0.6164 0.4773 -0.0448 0.0742  0.0358  990  ARG A CG  
3525 C CD  . ARG A 453 ? 0.6685 0.7179 0.5992 -0.0444 0.0655  0.0317  990  ARG A CD  
3526 N NE  . ARG A 453 ? 0.7079 0.7720 0.6615 -0.0504 0.0712  0.0356  990  ARG A NE  
3527 C CZ  . ARG A 453 ? 0.6388 0.6978 0.6033 -0.0586 0.0653  0.0412  990  ARG A CZ  
3528 N NH1 . ARG A 453 ? 0.4605 0.5003 0.4155 -0.0600 0.0545  0.0438  990  ARG A NH1 
3529 N NH2 . ARG A 453 ? 0.5141 0.5870 0.5022 -0.0655 0.0692  0.0443  990  ARG A NH2 
3530 N N   . ARG A 454 ? 0.4581 0.4694 0.2958 -0.0288 0.0753  0.0172  991  ARG A N   
3531 C CA  . ARG A 454 ? 0.4368 0.4516 0.2690 -0.0206 0.0890  0.0092  991  ARG A CA  
3532 C C   . ARG A 454 ? 0.4702 0.4805 0.3109 -0.0150 0.0799  -0.0004 991  ARG A C   
3533 O O   . ARG A 454 ? 0.4703 0.4919 0.3278 -0.0079 0.0883  -0.0051 991  ARG A O   
3534 C CB  . ARG A 454 ? 0.5624 0.5593 0.3513 -0.0188 0.0982  0.0079  991  ARG A CB  
3535 C CG  . ARG A 454 ? 0.7350 0.7412 0.5179 -0.0212 0.1165  0.0179  991  ARG A CG  
3536 C CD  . ARG A 454 ? 0.8144 0.8015 0.5486 -0.0165 0.1289  0.0154  991  ARG A CD  
3537 N NE  . ARG A 454 ? 0.8290 0.7912 0.5247 -0.0222 0.1140  0.0190  991  ARG A NE  
3538 C CZ  . ARG A 454 ? 0.9452 0.9057 0.6307 -0.0298 0.1147  0.0332  991  ARG A CZ  
3539 N NH1 . ARG A 454 ? 0.9015 0.8832 0.6141 -0.0337 0.1298  0.0446  991  ARG A NH1 
3540 N NH2 . ARG A 454 ? 0.9548 0.8921 0.6047 -0.0339 0.0990  0.0369  991  ARG A NH2 
3541 N N   . PHE A 455 ? 0.4849 0.4796 0.3170 -0.0181 0.0624  -0.0017 992  PHE A N   
3542 C CA  . PHE A 455 ? 0.4430 0.4337 0.2872 -0.0145 0.0534  -0.0083 992  PHE A CA  
3543 C C   . PHE A 455 ? 0.4120 0.4239 0.2935 -0.0112 0.0558  -0.0067 992  PHE A C   
3544 O O   . PHE A 455 ? 0.4379 0.4536 0.3305 -0.0047 0.0601  -0.0114 992  PHE A O   
3545 C CB  . PHE A 455 ? 0.4263 0.4021 0.2640 -0.0201 0.0334  -0.0067 992  PHE A CB  
3546 C CG  . PHE A 455 ? 0.4732 0.4473 0.3305 -0.0185 0.0237  -0.0104 992  PHE A CG  
3547 C CD1 . PHE A 455 ? 0.4920 0.4492 0.3348 -0.0163 0.0215  -0.0193 992  PHE A CD1 
3548 C CD2 . PHE A 455 ? 0.4550 0.4428 0.3446 -0.0188 0.0177  -0.0046 992  PHE A CD2 
3549 C CE1 . PHE A 455 ? 0.4612 0.4162 0.3252 -0.0163 0.0126  -0.0207 992  PHE A CE1 
3550 C CE2 . PHE A 455 ? 0.4575 0.4453 0.3670 -0.0174 0.0112  -0.0055 992  PHE A CE2 
3551 C CZ  . PHE A 455 ? 0.4282 0.4000 0.3266 -0.0170 0.0082  -0.0128 992  PHE A CZ  
3552 N N   . PHE A 456 ? 0.3736 0.3973 0.2723 -0.0150 0.0529  -0.0002 993  PHE A N   
3553 C CA  . PHE A 456 ? 0.4037 0.4444 0.3312 -0.0113 0.0536  0.0002  993  PHE A CA  
3554 C C   . PHE A 456 ? 0.3903 0.4482 0.3289 -0.0076 0.0663  -0.0006 993  PHE A C   
3555 O O   . PHE A 456 ? 0.3875 0.4573 0.3442 -0.0021 0.0673  -0.0020 993  PHE A O   
3556 C CB  . PHE A 456 ? 0.3346 0.3783 0.2741 -0.0154 0.0456  0.0053  993  PHE A CB  
3557 C CG  . PHE A 456 ? 0.3390 0.3718 0.2789 -0.0165 0.0331  0.0073  993  PHE A CG  
3558 C CD1 . PHE A 456 ? 0.3790 0.4132 0.3314 -0.0120 0.0299  0.0057  993  PHE A CD1 
3559 C CD2 . PHE A 456 ? 0.3624 0.3844 0.2926 -0.0219 0.0248  0.0125  993  PHE A CD2 
3560 C CE1 . PHE A 456 ? 0.3640 0.3918 0.3234 -0.0134 0.0189  0.0092  993  PHE A CE1 
3561 C CE2 . PHE A 456 ? 0.4368 0.4518 0.3728 -0.0224 0.0123  0.0156  993  PHE A CE2 
3562 C CZ  . PHE A 456 ? 0.3863 0.4056 0.3389 -0.0184 0.0095  0.0139  993  PHE A CZ  
3563 N N   . GLU A 457 ? 0.3873 0.4477 0.3163 -0.0102 0.0761  0.0015  994  GLU A N   
3564 C CA  . GLU A 457 ? 0.3401 0.4198 0.2847 -0.0064 0.0889  0.0020  994  GLU A CA  
3565 C C   . GLU A 457 ? 0.4845 0.5627 0.4259 0.0038  0.0973  -0.0038 994  GLU A C   
3566 O O   . GLU A 457 ? 0.7292 0.8256 0.6913 0.0097  0.1047  -0.0033 994  GLU A O   
3567 C CB  . GLU A 457 ? 0.4479 0.5322 0.3864 -0.0119 0.0998  0.0080  994  GLU A CB  
3568 C CG  . GLU A 457 ? 0.5097 0.5971 0.4579 -0.0222 0.0931  0.0151  994  GLU A CG  
3569 C CD  . GLU A 457 ? 0.4992 0.5912 0.4438 -0.0287 0.1051  0.0237  994  GLU A CD  
3570 O OE1 . GLU A 457 ? 0.4762 0.5597 0.3958 -0.0260 0.1167  0.0246  994  GLU A OE1 
3571 O OE2 . GLU A 457 ? 0.5002 0.6029 0.4661 -0.0366 0.1031  0.0298  994  GLU A OE2 
3572 N N   . ASN A 458 ? 0.4323 0.4883 0.3494 0.0059  0.0950  -0.0094 995  ASN A N   
3573 C CA  . ASN A 458 ? 0.4839 0.5317 0.3935 0.0156  0.1034  -0.0163 995  ASN A CA  
3574 C C   . ASN A 458 ? 0.4646 0.5039 0.3830 0.0195  0.0937  -0.0199 995  ASN A C   
3575 O O   . ASN A 458 ? 0.4947 0.5209 0.4055 0.0268  0.0982  -0.0263 995  ASN A O   
3576 C CB  . ASN A 458 ? 0.6116 0.6359 0.4829 0.0157  0.1085  -0.0217 995  ASN A CB  
3577 C CG  . ASN A 458 ? 0.7928 0.8266 0.6552 0.0147  0.1241  -0.0166 995  ASN A CG  
3578 O OD1 . ASN A 458 ? 0.7967 0.8553 0.6854 0.0176  0.1358  -0.0116 995  ASN A OD1 
3579 N ND2 . ASN A 458 ? 0.7824 0.7977 0.6091 0.0101  0.1240  -0.0165 995  ASN A ND2 
3580 N N   . LEU A 459 ? 0.4001 0.4452 0.3343 0.0152  0.0818  -0.0157 996  LEU A N   
3581 C CA  . LEU A 459 ? 0.4132 0.4517 0.3576 0.0184  0.0745  -0.0164 996  LEU A CA  
3582 C C   . LEU A 459 ? 0.3864 0.4333 0.3457 0.0288  0.0832  -0.0169 996  LEU A C   
3583 O O   . LEU A 459 ? 0.4798 0.5480 0.4547 0.0325  0.0893  -0.0133 996  LEU A O   
3584 C CB  . LEU A 459 ? 0.4406 0.4886 0.4013 0.0145  0.0650  -0.0103 996  LEU A CB  
3585 C CG  . LEU A 459 ? 0.4233 0.4621 0.3764 0.0060  0.0541  -0.0083 996  LEU A CG  
3586 C CD1 . LEU A 459 ? 0.3810 0.4309 0.3534 0.0061  0.0490  -0.0027 996  LEU A CD1 
3587 C CD2 . LEU A 459 ? 0.4857 0.5029 0.4261 0.0031  0.0460  -0.0118 996  LEU A CD2 
3588 N N   . ASN A 460 ? 0.4231 0.4528 0.3797 0.0332  0.0820  -0.0206 997  ASN A N   
3589 C CA  . ASN A 460 ? 0.3520 0.3857 0.3232 0.0442  0.0892  -0.0198 997  ASN A CA  
3590 C C   . ASN A 460 ? 0.3696 0.3891 0.3487 0.0446  0.0815  -0.0177 997  ASN A C   
3591 O O   . ASN A 460 ? 0.4494 0.4467 0.4218 0.0482  0.0824  -0.0232 997  ASN A O   
3592 C CB  . ASN A 460 ? 0.4012 0.4244 0.3591 0.0522  0.1018  -0.0275 997  ASN A CB  
3593 C CG  . ASN A 460 ? 0.3877 0.4143 0.3634 0.0652  0.1093  -0.0260 997  ASN A CG  
3594 O OD1 . ASN A 460 ? 0.4696 0.5195 0.4689 0.0694  0.1094  -0.0177 997  ASN A OD1 
3595 N ND2 . ASN A 460 ? 0.5549 0.5557 0.5178 0.0720  0.1142  -0.0342 997  ASN A ND2 
3596 N N   . PRO A 461 ? 0.3165 0.3473 0.3104 0.0413  0.0747  -0.0095 998  PRO A N   
3597 C CA  . PRO A 461 ? 0.3327 0.3518 0.3371 0.0403  0.0687  -0.0048 998  PRO A CA  
3598 C C   . PRO A 461 ? 0.3297 0.3413 0.3434 0.0500  0.0742  -0.0029 998  PRO A C   
3599 O O   . PRO A 461 ? 0.3790 0.3702 0.3963 0.0481  0.0700  -0.0026 998  PRO A O   
3600 C CB  . PRO A 461 ? 0.3251 0.3633 0.3428 0.0385  0.0657  0.0048  998  PRO A CB  
3601 C CG  . PRO A 461 ? 0.3325 0.3916 0.3483 0.0411  0.0699  0.0042  998  PRO A CG  
3602 C CD  . PRO A 461 ? 0.3421 0.3953 0.3431 0.0384  0.0729  -0.0042 998  PRO A CD  
3603 N N   . MET A 462 ? 0.3666 0.3933 0.3863 0.0600  0.0826  -0.0012 999  MET A N   
3604 C CA  . MET A 462 ? 0.3995 0.4209 0.4312 0.0710  0.0874  0.0032  999  MET A CA  
3605 C C   . MET A 462 ? 0.4337 0.4275 0.4555 0.0756  0.0919  -0.0069 999  MET A C   
3606 O O   . MET A 462 ? 0.3950 0.3764 0.4268 0.0839  0.0945  -0.0038 999  MET A O   
3607 C CB  . MET A 462 ? 0.4101 0.4583 0.4541 0.0808  0.0928  0.0090  999  MET A CB  
3608 C CG  . MET A 462 ? 0.5763 0.6469 0.6264 0.0781  0.0870  0.0181  999  MET A CG  
3609 S SD  . MET A 462 ? 0.6492 0.7461 0.7147 0.0903  0.0880  0.0270  999  MET A SD  
3610 C CE  . MET A 462 ? 0.6513 0.7726 0.7134 0.0822  0.0828  0.0240  999  MET A CE  
3611 N N   . GLY A 463 ? 0.4131 0.3944 0.4133 0.0709  0.0929  -0.0188 1000 GLY A N   
3612 C CA  . GLY A 463 ? 0.4161 0.3697 0.4009 0.0777  0.0991  -0.0305 1000 GLY A CA  
3613 C C   . GLY A 463 ? 0.4317 0.3969 0.4293 0.0940  0.1130  -0.0288 1000 GLY A C   
3614 O O   . GLY A 463 ? 0.4519 0.4466 0.4585 0.0976  0.1200  -0.0247 1000 GLY A O   
3615 N N   . SER A 464 ? 0.4442 0.3864 0.4464 0.1037  0.1162  -0.0309 1001 SER A N   
3616 C CA  . SER A 464 ? 0.4506 0.4018 0.4698 0.1212  0.1286  -0.0275 1001 SER A CA  
3617 C C   . SER A 464 ? 0.4431 0.4096 0.4909 0.1264  0.1240  -0.0111 1001 SER A C   
3618 O O   . SER A 464 ? 0.4378 0.4124 0.5034 0.1415  0.1315  -0.0056 1001 SER A O   
3619 C CB  . SER A 464 ? 0.4956 0.4085 0.5004 0.1314  0.1362  -0.0405 1001 SER A CB  
3620 O OG  . SER A 464 ? 0.6098 0.5123 0.5849 0.1310  0.1444  -0.0552 1001 SER A OG  
3621 N N   . ALA A 465 ? 0.4427 0.4132 0.4948 0.1153  0.1125  -0.0021 1002 ALA A N   
3622 C CA  . ALA A 465 ? 0.4615 0.4458 0.5346 0.1202  0.1090  0.0146  1002 ALA A CA  
3623 C C   . ALA A 465 ? 0.3810 0.4049 0.4649 0.1244  0.1097  0.0225  1002 ALA A C   
3624 O O   . ALA A 465 ? 0.4183 0.4602 0.4951 0.1175  0.1095  0.0173  1002 ALA A O   
3625 C CB  . ALA A 465 ? 0.3926 0.3698 0.4659 0.1076  0.0992  0.0223  1002 ALA A CB  
3626 N N   . SER A 466 ? 0.4408 0.4770 0.5422 0.1354  0.1091  0.0358  1003 SER A N   
3627 C CA  . SER A 466 ? 0.3992 0.4705 0.5089 0.1367  0.1040  0.0450  1003 SER A CA  
3628 C C   . SER A 466 ? 0.4249 0.5010 0.5238 0.1250  0.0957  0.0502  1003 SER A C   
3629 O O   . SER A 466 ? 0.4143 0.4697 0.5062 0.1175  0.0944  0.0505  1003 SER A O   
3630 C CB  . SER A 466 ? 0.4226 0.5040 0.5511 0.1520  0.1031  0.0589  1003 SER A CB  
3631 O OG  . SER A 466 ? 0.5331 0.5975 0.6601 0.1527  0.0996  0.0707  1003 SER A OG  
3632 N N   . GLU A 467 ? 0.4611 0.6173 0.6175 0.1084  0.0122  0.0222  1004 GLU A N   
3633 C CA  . GLU A 467 ? 0.3981 0.5278 0.5327 0.0877  0.0016  0.0166  1004 GLU A CA  
3634 C C   . GLU A 467 ? 0.3670 0.4551 0.4637 0.0881  -0.0071 0.0071  1004 GLU A C   
3635 O O   . GLU A 467 ? 0.4326 0.4949 0.4993 0.0788  -0.0046 -0.0007 1004 GLU A O   
3636 C CB  . GLU A 467 ? 0.5792 0.7257 0.7442 0.0730  -0.0158 0.0264  1004 GLU A CB  
3637 C CG  . GLU A 467 ? 0.7950 0.9192 0.9396 0.0546  -0.0232 0.0196  1004 GLU A CG  
3638 C CD  . GLU A 467 ? 0.9803 1.1203 1.1585 0.0402  -0.0406 0.0282  1004 GLU A CD  
3639 O OE1 . GLU A 467 ? 1.0695 1.2233 1.2760 0.0407  -0.0579 0.0363  1004 GLU A OE1 
3640 O OE2 . GLU A 467 ? 0.9828 1.1194 1.1605 0.0281  -0.0396 0.0270  1004 GLU A OE2 
3641 N N   . LYS A 468 ? 0.4900 0.5731 0.5900 0.0992  -0.0169 0.0098  1005 LYS A N   
3642 C CA  . LYS A 468 ? 0.4861 0.5311 0.5519 0.0998  -0.0248 0.0053  1005 LYS A CA  
3643 C C   . LYS A 468 ? 0.5199 0.5402 0.5609 0.1056  -0.0125 -0.0032 1005 LYS A C   
3644 O O   . LYS A 468 ? 0.4796 0.4717 0.4929 0.0961  -0.0130 -0.0064 1005 LYS A O   
3645 C CB  . LYS A 468 ? 0.5137 0.5592 0.5909 0.1120  -0.0389 0.0119  1005 LYS A CB  
3646 C CG  . LYS A 468 ? 0.6426 0.6496 0.6858 0.1127  -0.0481 0.0118  1005 LYS A CG  
3647 C CD  . LYS A 468 ? 0.7999 0.7888 0.8126 0.0958  -0.0515 0.0104  1005 LYS A CD  
3648 C CE  . LYS A 468 ? 0.9227 0.8817 0.9044 0.0967  -0.0617 0.0163  1005 LYS A CE  
3649 N NZ  . LYS A 468 ? 0.9365 0.8804 0.8852 0.0841  -0.0583 0.0153  1005 LYS A NZ  
3650 N N   . GLU A 469 ? 0.4162 0.4471 0.4677 0.1224  -0.0023 -0.0066 1006 GLU A N   
3651 C CA  . GLU A 469 ? 0.4296 0.4340 0.4569 0.1287  0.0054  -0.0174 1006 GLU A CA  
3652 C C   . GLU A 469 ? 0.4352 0.4340 0.4477 0.1121  0.0126  -0.0220 1006 GLU A C   
3653 O O   . GLU A 469 ? 0.4585 0.4265 0.4486 0.1051  0.0107  -0.0269 1006 GLU A O   
3654 C CB  . GLU A 469 ? 0.4406 0.4613 0.4776 0.1525  0.0159  -0.0225 1006 GLU A CB  
3655 C CG  . GLU A 469 ? 0.4661 0.4801 0.5108 0.1737  0.0086  -0.0220 1006 GLU A CG  
3656 C CD  . GLU A 469 ? 0.4895 0.5289 0.5466 0.2014  0.0217  -0.0261 1006 GLU A CD  
3657 O OE1 . GLU A 469 ? 0.4627 0.5346 0.5285 0.2018  0.0371  -0.0243 1006 GLU A OE1 
3658 O OE2 . GLU A 469 ? 0.5066 0.5336 0.5639 0.2240  0.0171  -0.0305 1006 GLU A OE2 
3659 N N   . PHE A 470 ? 0.3910 0.4202 0.4196 0.1053  0.0200  -0.0186 1007 PHE A N   
3660 C CA  . PHE A 470 ? 0.3775 0.4025 0.3940 0.0918  0.0265  -0.0227 1007 PHE A CA  
3661 C C   . PHE A 470 ? 0.4113 0.4157 0.4131 0.0745  0.0190  -0.0222 1007 PHE A C   
3662 O O   . PHE A 470 ? 0.4137 0.3993 0.3983 0.0669  0.0218  -0.0269 1007 PHE A O   
3663 C CB  . PHE A 470 ? 0.3574 0.4185 0.3969 0.0879  0.0344  -0.0162 1007 PHE A CB  
3664 C CG  . PHE A 470 ? 0.3790 0.4362 0.4067 0.0774  0.0412  -0.0200 1007 PHE A CG  
3665 C CD1 . PHE A 470 ? 0.5195 0.5634 0.5263 0.0854  0.0483  -0.0291 1007 PHE A CD1 
3666 C CD2 . PHE A 470 ? 0.4447 0.5079 0.4804 0.0605  0.0375  -0.0159 1007 PHE A CD2 
3667 C CE1 . PHE A 470 ? 0.4462 0.4862 0.4427 0.0757  0.0522  -0.0321 1007 PHE A CE1 
3668 C CE2 . PHE A 470 ? 0.4195 0.4785 0.4457 0.0519  0.0428  -0.0191 1007 PHE A CE2 
3669 C CZ  . PHE A 470 ? 0.4150 0.4642 0.4228 0.0591  0.0503  -0.0262 1007 PHE A CZ  
3670 N N   . THR A 471 ? 0.4245 0.4333 0.4325 0.0696  0.0089  -0.0161 1008 THR A N   
3671 C CA  . THR A 471 ? 0.4977 0.4882 0.4857 0.0582  0.0030  -0.0156 1008 THR A CA  
3672 C C   . THR A 471 ? 0.4553 0.4171 0.4215 0.0593  0.0031  -0.0149 1008 THR A C   
3673 O O   . THR A 471 ? 0.4758 0.4251 0.4269 0.0500  0.0072  -0.0147 1008 THR A O   
3674 C CB  . THR A 471 ? 0.5631 0.5599 0.5561 0.0574  -0.0113 -0.0107 1008 THR A CB  
3675 O OG1 . THR A 471 ? 0.7111 0.7308 0.7271 0.0515  -0.0146 -0.0100 1008 THR A OG1 
3676 C CG2 . THR A 471 ? 0.7336 0.7096 0.6967 0.0515  -0.0164 -0.0105 1008 THR A CG2 
3677 N N   . ASP A 472 ? 0.4529 0.4045 0.4206 0.0709  -0.0018 -0.0128 1009 ASP A N   
3678 C CA  . ASP A 472 ? 0.4543 0.3756 0.4061 0.0708  -0.0043 -0.0097 1009 ASP A CA  
3679 C C   . ASP A 472 ? 0.5184 0.4271 0.4669 0.0673  0.0022  -0.0167 1009 ASP A C   
3680 O O   . ASP A 472 ? 0.5293 0.4187 0.4684 0.0575  0.0019  -0.0121 1009 ASP A O   
3681 C CB  . ASP A 472 ? 0.5358 0.4458 0.4921 0.0857  -0.0135 -0.0069 1009 ASP A CB  
3682 C CG  . ASP A 472 ? 0.6471 0.5639 0.6038 0.0881  -0.0241 0.0022  1009 ASP A CG  
3683 O OD1 . ASP A 472 ? 0.6771 0.6032 0.6259 0.0786  -0.0256 0.0049  1009 ASP A OD1 
3684 O OD2 . ASP A 472 ? 0.6440 0.5553 0.6079 0.1011  -0.0328 0.0055  1009 ASP A OD2 
3685 N N   . TYR A 473 ? 0.4540 0.3748 0.4107 0.0755  0.0076  -0.0263 1010 TYR A N   
3686 C CA  . TYR A 473 ? 0.4442 0.3523 0.3941 0.0735  0.0109  -0.0349 1010 TYR A CA  
3687 C C   . TYR A 473 ? 0.4594 0.3709 0.4067 0.0556  0.0156  -0.0323 1010 TYR A C   
3688 O O   . TYR A 473 ? 0.4236 0.3157 0.3663 0.0474  0.0130  -0.0320 1010 TYR A O   
3689 C CB  . TYR A 473 ? 0.4277 0.3538 0.3817 0.0875  0.0179  -0.0442 1010 TYR A CB  
3690 C CG  . TYR A 473 ? 0.4378 0.3604 0.3827 0.0832  0.0220  -0.0523 1010 TYR A CG  
3691 C CD1 . TYR A 473 ? 0.6116 0.5027 0.5422 0.0874  0.0139  -0.0619 1010 TYR A CD1 
3692 C CD2 . TYR A 473 ? 0.4610 0.4093 0.4123 0.0749  0.0307  -0.0502 1010 TYR A CD2 
3693 C CE1 . TYR A 473 ? 0.5677 0.4544 0.4888 0.0838  0.0142  -0.0696 1010 TYR A CE1 
3694 C CE2 . TYR A 473 ? 0.5155 0.4606 0.4578 0.0715  0.0329  -0.0565 1010 TYR A CE2 
3695 C CZ  . TYR A 473 ? 0.5736 0.4886 0.5000 0.0763  0.0245  -0.0665 1010 TYR A CZ  
3696 O OH  . TYR A 473 ? 0.6034 0.5141 0.5197 0.0733  0.0235  -0.0732 1010 TYR A OH  
3697 N N   . LEU A 474 ? 0.4482 0.3840 0.4015 0.0496  0.0210  -0.0300 1011 LEU A N   
3698 C CA  . LEU A 474 ? 0.4412 0.3813 0.3925 0.0361  0.0257  -0.0288 1011 LEU A CA  
3699 C C   . LEU A 474 ? 0.4892 0.4151 0.4317 0.0280  0.0247  -0.0200 1011 LEU A C   
3700 O O   . LEU A 474 ? 0.3872 0.3094 0.3301 0.0188  0.0284  -0.0177 1011 LEU A O   
3701 C CB  . LEU A 474 ? 0.4007 0.3638 0.3595 0.0331  0.0279  -0.0285 1011 LEU A CB  
3702 C CG  . LEU A 474 ? 0.5110 0.4952 0.4840 0.0373  0.0315  -0.0314 1011 LEU A CG  
3703 C CD1 . LEU A 474 ? 0.5156 0.5170 0.5002 0.0312  0.0288  -0.0284 1011 LEU A CD1 
3704 C CD2 . LEU A 474 ? 0.5061 0.4881 0.4756 0.0353  0.0371  -0.0366 1011 LEU A CD2 
3705 N N   . PHE A 475 ? 0.4715 0.3924 0.4068 0.0317  0.0200  -0.0128 1012 PHE A N   
3706 C CA  . PHE A 475 ? 0.5154 0.4262 0.4396 0.0253  0.0216  -0.0008 1012 PHE A CA  
3707 C C   . PHE A 475 ? 0.4848 0.3744 0.4142 0.0205  0.0190  0.0056  1012 PHE A C   
3708 O O   . PHE A 475 ? 0.4588 0.3469 0.3903 0.0105  0.0241  0.0157  1012 PHE A O   
3709 C CB  . PHE A 475 ? 0.4666 0.3751 0.3774 0.0315  0.0157  0.0068  1012 PHE A CB  
3710 C CG  . PHE A 475 ? 0.5263 0.4302 0.4200 0.0271  0.0206  0.0210  1012 PHE A CG  
3711 C CD1 . PHE A 475 ? 0.5600 0.4773 0.4430 0.0245  0.0296  0.0203  1012 PHE A CD1 
3712 C CD2 . PHE A 475 ? 0.5789 0.4656 0.4675 0.0269  0.0171  0.0363  1012 PHE A CD2 
3713 C CE1 . PHE A 475 ? 0.6478 0.5655 0.5128 0.0238  0.0378  0.0348  1012 PHE A CE1 
3714 C CE2 . PHE A 475 ? 0.6159 0.5030 0.4890 0.0233  0.0245  0.0537  1012 PHE A CE2 
3715 C CZ  . PHE A 475 ? 0.5641 0.4688 0.4245 0.0227  0.0363  0.0530  1012 PHE A CZ  
3716 N N   . ASN A 476 ? 0.4651 0.3381 0.3989 0.0283  0.0101  0.0003  1013 ASN A N   
3717 C CA  . ASN A 476 ? 0.5335 0.3794 0.4730 0.0237  0.0022  0.0042  1013 ASN A CA  
3718 C C   . ASN A 476 ? 0.4871 0.3339 0.4356 0.0143  0.0039  -0.0016 1013 ASN A C   
3719 O O   . ASN A 476 ? 0.4759 0.3086 0.4346 0.0027  -0.0007 0.0080  1013 ASN A O   
3720 C CB  . ASN A 476 ? 0.5471 0.3719 0.4858 0.0383  -0.0094 -0.0049 1013 ASN A CB  
3721 C CG  . ASN A 476 ? 0.6340 0.4522 0.5680 0.0462  -0.0148 0.0046  1013 ASN A CG  
3722 O OD1 . ASN A 476 ? 0.6306 0.4482 0.5598 0.0382  -0.0134 0.0215  1013 ASN A OD1 
3723 N ND2 . ASN A 476 ? 0.7409 0.5562 0.6756 0.0637  -0.0203 -0.0050 1013 ASN A ND2 
3724 N N   . LYS A 477 ? 0.4380 0.3023 0.3855 0.0184  0.0092  -0.0152 1014 LYS A N   
3725 C CA  . LYS A 477 ? 0.5209 0.3873 0.4752 0.0104  0.0097  -0.0206 1014 LYS A CA  
3726 C C   . LYS A 477 ? 0.4504 0.3329 0.4135 -0.0032 0.0187  -0.0084 1014 LYS A C   
3727 O O   . LYS A 477 ? 0.4255 0.3030 0.4022 -0.0142 0.0156  -0.0029 1014 LYS A O   
3728 C CB  . LYS A 477 ? 0.4385 0.3214 0.3877 0.0193  0.0142  -0.0347 1014 LYS A CB  
3729 C CG  . LYS A 477 ? 0.4625 0.3471 0.4150 0.0133  0.0129  -0.0410 1014 LYS A CG  
3730 C CD  . LYS A 477 ? 0.4816 0.3356 0.4332 0.0125  -0.0025 -0.0465 1014 LYS A CD  
3731 C CE  . LYS A 477 ? 0.6231 0.4600 0.5575 0.0315  -0.0096 -0.0607 1014 LYS A CE  
3732 N NZ  . LYS A 477 ? 0.6260 0.4283 0.5545 0.0324  -0.0287 -0.0708 1014 LYS A NZ  
3733 N N   . SER A 478 ? 0.4174 0.3189 0.3734 -0.0014 0.0286  -0.0039 1015 SER A N   
3734 C CA  . SER A 478 ? 0.4275 0.3441 0.3863 -0.0089 0.0390  0.0074  1015 SER A CA  
3735 C C   . SER A 478 ? 0.4811 0.3878 0.4490 -0.0177 0.0385  0.0264  1015 SER A C   
3736 O O   . SER A 478 ? 0.4259 0.3419 0.4105 -0.0275 0.0436  0.0360  1015 SER A O   
3737 C CB  . SER A 478 ? 0.4358 0.3654 0.3774 -0.0015 0.0451  0.0073  1015 SER A CB  
3738 O OG  . SER A 478 ? 0.3980 0.3419 0.3356 -0.0037 0.0563  0.0155  1015 SER A OG  
3739 N N   . LEU A 479 ? 0.4422 0.3312 0.4033 -0.0147 0.0318  0.0341  1016 LEU A N   
3740 C CA  . LEU A 479 ? 0.4669 0.3445 0.4398 -0.0245 0.0297  0.0561  1016 LEU A CA  
3741 C C   . LEU A 479 ? 0.4860 0.3475 0.4846 -0.0361 0.0177  0.0567  1016 LEU A C   
3742 O O   . LEU A 479 ? 0.5263 0.3905 0.5470 -0.0496 0.0189  0.0771  1016 LEU A O   
3743 C CB  . LEU A 479 ? 0.4918 0.3485 0.4525 -0.0180 0.0211  0.0631  1016 LEU A CB  
3744 C CG  . LEU A 479 ? 0.5224 0.3918 0.4579 -0.0085 0.0292  0.0688  1016 LEU A CG  
3745 C CD1 . LEU A 479 ? 0.5498 0.3967 0.4763 -0.0019 0.0174  0.0761  1016 LEU A CD1 
3746 C CD2 . LEU A 479 ? 0.6077 0.4976 0.5383 -0.0134 0.0453  0.0886  1016 LEU A CD2 
3747 N N   . GLU A 480 ? 0.5040 0.3488 0.5003 -0.0306 0.0051  0.0356  1017 GLU A N   
3748 C CA  . GLU A 480 ? 0.5038 0.3276 0.5185 -0.0394 -0.0112 0.0319  1017 GLU A CA  
3749 C C   . GLU A 480 ? 0.4889 0.3355 0.5228 -0.0506 -0.0052 0.0350  1017 GLU A C   
3750 O O   . GLU A 480 ? 0.5241 0.3641 0.5856 -0.0652 -0.0148 0.0473  1017 GLU A O   
3751 C CB  . GLU A 480 ? 0.5795 0.3816 0.5776 -0.0253 -0.0242 0.0064  1017 GLU A CB  
3752 C CG  . GLU A 480 ? 0.6953 0.4685 0.7033 -0.0306 -0.0459 -0.0027 1017 GLU A CG  
3753 C CD  . GLU A 480 ? 0.7795 0.5344 0.7622 -0.0114 -0.0554 -0.0295 1017 GLU A CD  
3754 O OE1 . GLU A 480 ? 0.6516 0.4233 0.6159 0.0040  -0.0424 -0.0381 1017 GLU A OE1 
3755 O OE2 . GLU A 480 ? 0.7332 0.4579 0.7147 -0.0110 -0.0764 -0.0413 1017 GLU A OE2 
3756 N N   . ILE A 481 ? 0.5067 0.3799 0.5302 -0.0443 0.0088  0.0251  1018 ILE A N   
3757 C CA  . ILE A 481 ? 0.4332 0.3257 0.4741 -0.0519 0.0122  0.0246  1018 ILE A CA  
3758 C C   . ILE A 481 ? 0.4425 0.3628 0.5022 -0.0600 0.0282  0.0466  1018 ILE A C   
3759 O O   . ILE A 481 ? 0.4175 0.3519 0.5045 -0.0698 0.0280  0.0542  1018 ILE A O   
3760 C CB  . ILE A 481 ? 0.4772 0.3831 0.5008 -0.0414 0.0180  0.0056  1018 ILE A CB  
3761 C CG1 . ILE A 481 ? 0.3957 0.3206 0.4023 -0.0325 0.0341  0.0060  1018 ILE A CG1 
3762 C CG2 . ILE A 481 ? 0.4587 0.3423 0.4651 -0.0319 0.0047  -0.0133 1018 ILE A CG2 
3763 C CD1 . ILE A 481 ? 0.3613 0.2993 0.3568 -0.0245 0.0381  -0.0094 1018 ILE A CD1 
3764 N N   . GLU A 482 ? 0.4191 0.3495 0.4643 -0.0544 0.0422  0.0575  1019 GLU A N   
3765 C CA  . GLU A 482 ? 0.4236 0.3803 0.4812 -0.0584 0.0595  0.0809  1019 GLU A CA  
3766 C C   . GLU A 482 ? 0.4759 0.4229 0.5226 -0.0579 0.0619  0.0991  1019 GLU A C   
3767 O O   . GLU A 482 ? 0.4792 0.4316 0.4957 -0.0459 0.0717  0.0978  1019 GLU A O   
3768 C CB  . GLU A 482 ? 0.4064 0.3903 0.4473 -0.0466 0.0774  0.0733  1019 GLU A CB  
3769 C CG  . GLU A 482 ? 0.4508 0.4497 0.5117 -0.0494 0.0775  0.0645  1019 GLU A CG  
3770 C CD  . GLU A 482 ? 0.4103 0.4327 0.4577 -0.0369 0.0934  0.0574  1019 GLU A CD  
3771 O OE1 . GLU A 482 ? 0.3880 0.4228 0.4171 -0.0273 0.1083  0.0655  1019 GLU A OE1 
3772 O OE2 . GLU A 482 ? 0.3573 0.3835 0.4107 -0.0357 0.0894  0.0433  1019 GLU A OE2 
3773 N N   . PRO A 483 ? 0.4707 0.4005 0.5416 -0.0710 0.0501  0.1169  1020 PRO A N   
3774 C CA  . PRO A 483 ? 0.4985 0.4162 0.5600 -0.0711 0.0505  0.1369  1020 PRO A CA  
3775 C C   . PRO A 483 ? 0.5927 0.5439 0.6463 -0.0672 0.0756  0.1608  1020 PRO A C   
3776 O O   . PRO A 483 ? 0.5319 0.5153 0.6015 -0.0689 0.0915  0.1691  1020 PRO A O   
3777 C CB  . PRO A 483 ? 0.5469 0.4404 0.6454 -0.0891 0.0309  0.1532  1020 PRO A CB  
3778 C CG  . PRO A 483 ? 0.5966 0.4743 0.7060 -0.0917 0.0127  0.1276  1020 PRO A CG  
3779 C CD  . PRO A 483 ? 0.5182 0.4313 0.6232 -0.0857 0.0303  0.1166  1020 PRO A CD  
3780 N N   . ARG A 484 ? 0.5399 0.4834 0.5658 -0.0595 0.0791  0.1713  1021 ARG A N   
3781 C CA  . ARG A 484 ? 0.6817 0.6538 0.6904 -0.0523 0.1025  0.1948  1021 ARG A CA  
3782 C C   . ARG A 484 ? 0.6701 0.6680 0.7200 -0.0669 0.1149  0.2296  1021 ARG A C   
3783 O O   . ARG A 484 ? 0.6430 0.6248 0.7305 -0.0851 0.1005  0.2478  1021 ARG A O   
3784 C CB  . ARG A 484 ? 0.7411 0.6949 0.7189 -0.0453 0.0986  0.2061  1021 ARG A CB  
3785 C CG  . ARG A 484 ? 0.7891 0.7465 0.7170 -0.0247 0.1039  0.1866  1021 ARG A CG  
3786 C CD  . ARG A 484 ? 0.8359 0.7620 0.7428 -0.0191 0.0854  0.1795  1021 ARG A CD  
3787 N NE  . ARG A 484 ? 0.9045 0.8310 0.7758 -0.0026 0.0825  0.1528  1021 ARG A NE  
3788 C CZ  . ARG A 484 ? 1.0411 0.9460 0.9035 0.0032  0.0646  0.1356  1021 ARG A CZ  
3789 N NH1 . ARG A 484 ? 1.1592 1.0387 1.0410 -0.0033 0.0492  0.1398  1021 ARG A NH1 
3790 N NH2 . ARG A 484 ? 0.9776 0.8864 0.8143 0.0160  0.0609  0.1147  1021 ARG A NH2 
3791 N N   . ASN A 485 ? 0.6988 0.7369 0.7443 -0.0580 0.1406  0.2384  1022 ASN A N   
3792 C CA  . ASN A 485 ? 0.7132 0.7879 0.7979 -0.0678 0.1590  0.2756  1022 ASN A CA  
3793 C C   . ASN A 485 ? 0.7216 0.7979 0.8681 -0.0894 0.1451  0.2796  1022 ASN A C   
3794 O O   . ASN A 485 ? 0.7120 0.8118 0.9054 -0.1045 0.1521  0.3156  1022 ASN A O   
3795 C CB  . ASN A 485 ? 0.8281 0.9025 0.9138 -0.0741 0.1647  0.3160  1022 ASN A CB  
3796 C CG  . ASN A 485 ? 0.8538 0.9246 0.8750 -0.0522 0.1755  0.3135  1022 ASN A CG  
3797 O OD1 . ASN A 485 ? 0.9410 0.9805 0.9440 -0.0538 0.1607  0.3180  1022 ASN A OD1 
3798 N ND2 . ASN A 485 ? 0.7982 0.8992 0.7839 -0.0305 0.1993  0.3059  1022 ASN A ND2 
3799 N N   . CYS A 486 ? 0.6315 0.6842 0.7809 -0.0916 0.1245  0.2454  1023 CYS A N   
3800 C CA  . CYS A 486 ? 0.6658 0.7226 0.8680 -0.1090 0.1111  0.2469  1023 CYS A CA  
3801 C C   . CYS A 486 ? 0.7036 0.8098 0.9244 -0.1025 0.1350  0.2536  1023 CYS A C   
3802 O O   . CYS A 486 ? 0.8006 0.9202 0.9850 -0.0823 0.1502  0.2328  1023 CYS A O   
3803 C CB  . CYS A 486 ? 0.6756 0.6949 0.8681 -0.1095 0.0839  0.2087  1023 CYS A CB  
3804 S SG  . CYS A 486 ? 0.5719 0.5978 0.7200 -0.0872 0.0926  0.1679  1023 CYS A SG  
3805 N N   . LYS A 487 ? 0.6373 0.7712 0.9173 -0.1192 0.1377  0.2841  1024 LYS A N   
3806 C CA  . LYS A 487 ? 0.6701 0.8550 0.9725 -0.1110 0.1617  0.2924  1024 LYS A CA  
3807 C C   . LYS A 487 ? 0.6840 0.8636 0.9959 -0.1099 0.1470  0.2606  1024 LYS A C   
3808 O O   . LYS A 487 ? 0.7110 0.9247 1.0243 -0.0957 0.1658  0.2553  1024 LYS A O   
3809 C CB  . LYS A 487 ? 0.8630 1.0793 1.2180 -0.1231 0.1653  0.3279  1024 LYS A CB  
3810 C CG  . LYS A 487 ? 0.9909 1.2097 1.3304 -0.1214 0.1759  0.3555  1024 LYS A CG  
3811 C CD  . LYS A 487 ? 1.0470 1.3113 1.3617 -0.0972 0.2113  0.3673  1024 LYS A CD  
3812 C CE  . LYS A 487 ? 1.0968 1.3582 1.3829 -0.0929 0.2213  0.3906  1024 LYS A CE  
3813 N NZ  . LYS A 487 ? 1.1242 1.3960 1.3421 -0.0632 0.2468  0.3788  1024 LYS A NZ  
3814 N N   . GLN A 488 ? 0.5774 0.7139 0.8917 -0.1221 0.1142  0.2388  1025 GLN A N   
3815 C CA  . GLN A 488 ? 0.6354 0.7594 0.9430 -0.1181 0.0990  0.2054  1025 GLN A CA  
3816 C C   . GLN A 488 ? 0.4744 0.5454 0.7455 -0.1182 0.0735  0.1768  1025 GLN A C   
3817 O O   . GLN A 488 ? 0.5288 0.5717 0.8001 -0.1276 0.0600  0.1858  1025 GLN A O   
3818 C CB  . GLN A 488 ? 0.6791 0.8187 1.0483 -0.1352 0.0839  0.2161  1025 GLN A CB  
3819 C CG  . GLN A 488 ? 0.8330 0.9311 1.2260 -0.1565 0.0457  0.2135  1025 GLN A CG  
3820 C CD  . GLN A 488 ? 1.0490 1.1684 1.5137 -0.1771 0.0311  0.2361  1025 GLN A CD  
3821 O OE1 . GLN A 488 ? 1.1624 1.3282 1.6606 -0.1763 0.0515  0.2626  1025 GLN A OE1 
3822 N NE2 . GLN A 488 ? 1.0831 1.1657 1.5605 -0.1899 -0.0067 0.2202  1025 GLN A NE2 
3823 N N   . PRO A 489 ? 0.4540 0.5117 0.6943 -0.1068 0.0674  0.1440  1026 PRO A N   
3824 C CA  . PRO A 489 ? 0.4966 0.5101 0.7043 -0.1044 0.0460  0.1185  1026 PRO A CA  
3825 C C   . PRO A 489 ? 0.5681 0.5527 0.8033 -0.1207 0.0150  0.1173  1026 PRO A C   
3826 O O   . PRO A 489 ? 0.5128 0.5105 0.7861 -0.1314 0.0055  0.1234  1026 PRO A O   
3827 C CB  . PRO A 489 ? 0.4968 0.5137 0.6753 -0.0897 0.0500  0.0906  1026 PRO A CB  
3828 C CG  . PRO A 489 ? 0.4703 0.5257 0.6501 -0.0797 0.0765  0.0995  1026 PRO A CG  
3829 C CD  . PRO A 489 ? 0.4183 0.5018 0.6473 -0.0921 0.0830  0.1302  1026 PRO A CD  
3830 N N   . PRO A 490 ? 0.5717 0.5152 0.7885 -0.1216 -0.0037 0.1085  1027 PRO A N   
3831 C CA  . PRO A 490 ? 0.6515 0.5596 0.8881 -0.1342 -0.0374 0.1031  1027 PRO A CA  
3832 C C   . PRO A 490 ? 0.6009 0.5009 0.8253 -0.1286 -0.0519 0.0761  1027 PRO A C   
3833 O O   . PRO A 490 ? 0.5819 0.4967 0.7774 -0.1142 -0.0372 0.0594  1027 PRO A O   
3834 C CB  . PRO A 490 ? 0.7846 0.6499 0.9916 -0.1281 -0.0501 0.0938  1027 PRO A CB  
3835 C CG  . PRO A 490 ? 0.7162 0.6007 0.9033 -0.1193 -0.0229 0.1065  1027 PRO A CG  
3836 C CD  . PRO A 490 ? 0.6078 0.5340 0.7857 -0.1099 0.0034  0.1033  1027 PRO A CD  
3837 N N   . ARG A 491 ? 0.5819 0.4564 0.8288 -0.1405 -0.0832 0.0728  1028 ARG A N   
3838 C CA  . ARG A 491 ? 0.6386 0.5016 0.8688 -0.1342 -0.1001 0.0475  1028 ARG A CA  
3839 C C   . ARG A 491 ? 0.6421 0.4642 0.8191 -0.1170 -0.1123 0.0181  1028 ARG A C   
3840 O O   . ARG A 491 ? 0.6231 0.4070 0.7936 -0.1178 -0.1306 0.0150  1028 ARG A O   
3841 C CB  . ARG A 491 ? 0.6323 0.4848 0.9059 -0.1525 -0.1319 0.0543  1028 ARG A CB  
3842 C CG  . ARG A 491 ? 0.6973 0.5381 0.9497 -0.1449 -0.1510 0.0288  1028 ARG A CG  
3843 C CD  . ARG A 491 ? 0.8670 0.6937 1.1612 -0.1629 -0.1877 0.0341  1028 ARG A CD  
3844 N NE  . ARG A 491 ? 0.8962 0.6640 1.1737 -0.1641 -0.2261 0.0177  1028 ARG A NE  
3845 C CZ  . ARG A 491 ? 1.1211 0.8734 1.4348 -0.1783 -0.2557 0.0289  1028 ARG A CZ  
3846 N NH1 . ARG A 491 ? 1.0370 0.8301 1.4102 -0.1945 -0.2508 0.0586  1028 ARG A NH1 
3847 N NH2 . ARG A 491 ? 1.2818 0.9842 1.5658 -0.1696 -0.2853 0.0105  1028 ARG A NH2 
3848 N N   . PHE A 492 ? 0.5609 0.3925 0.7017 -0.1006 -0.1012 -0.0016 1029 PHE A N   
3849 C CA  . PHE A 492 ? 0.5082 0.3104 0.6003 -0.0819 -0.1102 -0.0286 1029 PHE A CA  
3850 C C   . PHE A 492 ? 0.6214 0.4241 0.6990 -0.0765 -0.1218 -0.0444 1029 PHE A C   
3851 O O   . PHE A 492 ? 0.5710 0.4056 0.6684 -0.0825 -0.1121 -0.0359 1029 PHE A O   
3852 C CB  . PHE A 492 ? 0.4837 0.3018 0.5448 -0.0657 -0.0825 -0.0333 1029 PHE A CB  
3853 C CG  . PHE A 492 ? 0.5234 0.3374 0.5903 -0.0677 -0.0732 -0.0199 1029 PHE A CG  
3854 C CD1 . PHE A 492 ? 0.5243 0.3695 0.6151 -0.0770 -0.0527 0.0028  1029 PHE A CD1 
3855 C CD2 . PHE A 492 ? 0.6608 0.4396 0.7071 -0.0582 -0.0854 -0.0296 1029 PHE A CD2 
3856 C CE1 . PHE A 492 ? 0.4868 0.3281 0.5788 -0.0779 -0.0448 0.0167  1029 PHE A CE1 
3857 C CE2 . PHE A 492 ? 0.7217 0.4959 0.7735 -0.0599 -0.0785 -0.0157 1029 PHE A CE2 
3858 C CZ  . PHE A 492 ? 0.5952 0.4008 0.6688 -0.0704 -0.0584 0.0082  1029 PHE A CZ  
3859 N N   . PRO A 493 ? 0.6661 0.4334 0.7071 -0.0633 -0.1426 -0.0672 1030 PRO A N   
3860 C CA  . PRO A 493 ? 0.6756 0.4419 0.6952 -0.0559 -0.1542 -0.0818 1030 PRO A CA  
3861 C C   . PRO A 493 ? 0.6180 0.4194 0.6171 -0.0442 -0.1256 -0.0826 1030 PRO A C   
3862 O O   . PRO A 493 ? 0.5560 0.3709 0.5408 -0.0347 -0.1018 -0.0815 1030 PRO A O   
3863 C CB  . PRO A 493 ? 0.7588 0.4773 0.7337 -0.0386 -0.1790 -0.1070 1030 PRO A CB  
3864 C CG  . PRO A 493 ? 0.7483 0.4515 0.7157 -0.0316 -0.1705 -0.1071 1030 PRO A CG  
3865 C CD  . PRO A 493 ? 0.6703 0.3934 0.6883 -0.0537 -0.1599 -0.0804 1030 PRO A CD  
3866 N N   . ARG A 494 ? 0.6118 0.4269 0.6125 -0.0458 -0.1307 -0.0834 1031 ARG A N   
3867 C CA  . ARG A 494 ? 0.6309 0.4754 0.6148 -0.0362 -0.1085 -0.0829 1031 ARG A CA  
3868 C C   . ARG A 494 ? 0.7271 0.5592 0.6585 -0.0137 -0.1037 -0.0990 1031 ARG A C   
3869 O O   . ARG A 494 ? 0.7099 0.5090 0.6105 -0.0025 -0.1237 -0.1154 1031 ARG A O   
3870 C CB  . ARG A 494 ? 0.7686 0.6257 0.7673 -0.0430 -0.1201 -0.0792 1031 ARG A CB  
3871 C CG  . ARG A 494 ? 0.7713 0.6639 0.7770 -0.0415 -0.0983 -0.0699 1031 ARG A CG  
3872 C CD  . ARG A 494 ? 0.6460 0.5686 0.6934 -0.0522 -0.0777 -0.0529 1031 ARG A CD  
3873 N NE  . ARG A 494 ? 0.6037 0.5393 0.6993 -0.0673 -0.0864 -0.0400 1031 ARG A NE  
3874 C CZ  . ARG A 494 ? 0.5418 0.4900 0.6579 -0.0715 -0.0970 -0.0357 1031 ARG A CZ  
3875 N NH1 . ARG A 494 ? 0.4114 0.3570 0.5003 -0.0624 -0.1028 -0.0437 1031 ARG A NH1 
3876 N NH2 . ARG A 494 ? 0.5383 0.5038 0.7047 -0.0846 -0.1023 -0.0213 1031 ARG A NH2 
3877 N N   . LYS A 495 ? 0.8274 0.6864 0.7497 -0.0058 -0.0773 -0.0940 1032 LYS A N   
3878 C CA  . LYS A 495 ? 0.8907 0.7462 0.7708 0.0156  -0.0686 -0.1044 1032 LYS A CA  
3879 C C   . LYS A 495 ? 0.8433 0.7021 0.6919 0.0272  -0.0730 -0.1098 1032 LYS A C   
3880 O O   . LYS A 495 ? 0.9484 0.7922 0.7544 0.0473  -0.0770 -0.1229 1032 LYS A O   
3881 C CB  . LYS A 495 ? 0.8376 0.7209 0.7254 0.0183  -0.0409 -0.0945 1032 LYS A CB  
3882 C CG  . LYS A 495 ? 0.9208 0.7989 0.7795 0.0383  -0.0325 -0.1029 1032 LYS A CG  
3883 C CD  . LYS A 495 ? 1.0915 0.9382 0.9497 0.0400  -0.0453 -0.1115 1032 LYS A CD  
3884 C CE  . LYS A 495 ? 1.1902 1.0103 1.0063 0.0639  -0.0557 -0.1304 1032 LYS A CE  
3885 N NZ  . LYS A 495 ? 1.2453 1.0640 1.0557 0.0780  -0.0446 -0.1329 1032 LYS A NZ  
3886 N N   . SER A 496 ? 0.7929 0.6710 0.6590 0.0170  -0.0722 -0.0994 1033 SER A N   
3887 C CA  . SER A 496 ? 0.7106 0.5919 0.5472 0.0269  -0.0776 -0.1013 1033 SER A CA  
3888 C C   . SER A 496 ? 0.7132 0.5878 0.5692 0.0137  -0.1007 -0.0997 1033 SER A C   
3889 O O   . SER A 496 ? 0.7443 0.6227 0.6443 -0.0040 -0.1057 -0.0926 1033 SER A O   
3890 C CB  . SER A 496 ? 0.7679 0.6827 0.6062 0.0297  -0.0531 -0.0867 1033 SER A CB  
3891 O OG  . SER A 496 ? 0.6537 0.5843 0.5258 0.0145  -0.0539 -0.0745 1033 SER A OG  
3892 N N   . THR A 497 ? 0.6810 0.5478 0.5038 0.0236  -0.1147 -0.1050 1034 THR A N   
3893 C CA  . THR A 497 ? 0.6553 0.5149 0.4938 0.0130  -0.1406 -0.1041 1034 THR A CA  
3894 C C   . THR A 497 ? 0.5951 0.4846 0.4564 0.0060  -0.1305 -0.0871 1034 THR A C   
3895 O O   . THR A 497 ? 0.6488 0.5363 0.5232 -0.0007 -0.1513 -0.0847 1034 THR A O   
3896 C CB  . THR A 497 ? 0.8241 0.6527 0.6102 0.0287  -0.1677 -0.1212 1034 THR A CB  
3897 O OG1 . THR A 497 ? 0.9628 0.8047 0.7027 0.0478  -0.1520 -0.1184 1034 THR A OG1 
3898 C CG2 . THR A 497 ? 0.8063 0.5982 0.5680 0.0380  -0.1818 -0.1411 1034 THR A CG2 
3899 N N   A PHE A 498 ? 0.6236 0.5389 0.4911 0.0077  -0.1021 -0.0752 1035 PHE A N   
3900 N N   B PHE A 498 ? 0.6183 0.5337 0.4873 0.0073  -0.1019 -0.0752 1035 PHE A N   
3901 C CA  A PHE A 498 ? 0.6269 0.5644 0.5146 0.0022  -0.0966 -0.0601 1035 PHE A CA  
3902 C CA  B PHE A 498 ? 0.6233 0.5625 0.5126 0.0021  -0.0933 -0.0596 1035 PHE A CA  
3903 C C   A PHE A 498 ? 0.5125 0.4658 0.4561 -0.0135 -0.0901 -0.0514 1035 PHE A C   
3904 C C   B PHE A 498 ? 0.5017 0.4544 0.4471 -0.0142 -0.0914 -0.0517 1035 PHE A C   
3905 O O   A PHE A 498 ? 0.4414 0.3943 0.4059 -0.0198 -0.0828 -0.0537 1035 PHE A O   
3906 O O   B PHE A 498 ? 0.4486 0.3996 0.4172 -0.0215 -0.0873 -0.0542 1035 PHE A O   
3907 C CB  A PHE A 498 ? 0.7340 0.6896 0.6011 0.0118  -0.0742 -0.0493 1035 PHE A CB  
3908 C CB  B PHE A 498 ? 0.7205 0.6792 0.5991 0.0090  -0.0669 -0.0493 1035 PHE A CB  
3909 C CG  A PHE A 498 ? 0.7887 0.7528 0.6573 0.0147  -0.0513 -0.0490 1035 PHE A CG  
3910 C CG  B PHE A 498 ? 0.8181 0.7739 0.6451 0.0273  -0.0620 -0.0518 1035 PHE A CG  
3911 C CD1 A PHE A 498 ? 0.7696 0.7452 0.6775 0.0034  -0.0389 -0.0437 1035 PHE A CD1 
3912 C CD1 B PHE A 498 ? 0.8691 0.8178 0.6604 0.0371  -0.0762 -0.0518 1035 PHE A CD1 
3913 C CD2 A PHE A 498 ? 0.8635 0.8258 0.6925 0.0310  -0.0421 -0.0534 1035 PHE A CD2 
3914 C CD2 B PHE A 498 ? 0.8716 0.8345 0.6855 0.0365  -0.0422 -0.0525 1035 PHE A CD2 
3915 C CE1 A PHE A 498 ? 0.7952 0.7779 0.7036 0.0063  -0.0210 -0.0432 1035 PHE A CE1 
3916 C CE1 B PHE A 498 ? 0.9571 0.9066 0.6967 0.0574  -0.0684 -0.0527 1035 PHE A CE1 
3917 C CE2 A PHE A 498 ? 0.8731 0.8460 0.7077 0.0342  -0.0224 -0.0517 1035 PHE A CE2 
3918 C CE2 B PHE A 498 ? 0.8995 0.8657 0.6679 0.0562  -0.0341 -0.0528 1035 PHE A CE2 
3919 C CZ  A PHE A 498 ? 0.8124 0.7944 0.6872 0.0207  -0.0134 -0.0466 1035 PHE A CZ  
3920 C CZ  B PHE A 498 ? 0.9549 0.9149 0.6842 0.0675  -0.0459 -0.0528 1035 PHE A CZ  
3921 N N   . SER A 499 ? 0.5139 0.4812 0.4797 -0.0179 -0.0931 -0.0409 1036 SER A N   
3922 C CA  . SER A 499 ? 0.4642 0.4488 0.4795 -0.0278 -0.0859 -0.0329 1036 SER A CA  
3923 C C   . SER A 499 ? 0.4389 0.4334 0.4621 -0.0277 -0.0609 -0.0308 1036 SER A C   
3924 O O   . SER A 499 ? 0.4354 0.4310 0.4349 -0.0213 -0.0485 -0.0294 1036 SER A O   
3925 C CB  . SER A 499 ? 0.5162 0.5124 0.5457 -0.0273 -0.0907 -0.0225 1036 SER A CB  
3926 O OG  . SER A 499 ? 0.4045 0.4176 0.4785 -0.0323 -0.0817 -0.0163 1036 SER A OG  
3927 N N   . LEU A 500 ? 0.4313 0.4342 0.4882 -0.0345 -0.0541 -0.0294 1037 LEU A N   
3928 C CA  . LEU A 500 ? 0.3264 0.3381 0.3906 -0.0335 -0.0331 -0.0278 1037 LEU A CA  
3929 C C   . LEU A 500 ? 0.3609 0.3857 0.4437 -0.0311 -0.0258 -0.0213 1037 LEU A C   
3930 O O   . LEU A 500 ? 0.3416 0.3702 0.4267 -0.0286 -0.0118 -0.0215 1037 LEU A O   
3931 C CB  . LEU A 500 ? 0.3343 0.3493 0.4208 -0.0394 -0.0279 -0.0277 1037 LEU A CB  
3932 C CG  . LEU A 500 ? 0.3690 0.3671 0.4447 -0.0433 -0.0372 -0.0332 1037 LEU A CG  
3933 C CD1 . LEU A 500 ? 0.3258 0.3319 0.4316 -0.0508 -0.0305 -0.0267 1037 LEU A CD1 
3934 C CD2 . LEU A 500 ? 0.4974 0.4822 0.5356 -0.0356 -0.0306 -0.0409 1037 LEU A CD2 
3935 N N   . LYS A 501 ? 0.3359 0.3645 0.4309 -0.0309 -0.0378 -0.0166 1038 LYS A N   
3936 C CA  . LYS A 501 ? 0.3146 0.3526 0.4313 -0.0272 -0.0345 -0.0112 1038 LYS A CA  
3937 C C   . LYS A 501 ? 0.3089 0.3407 0.4071 -0.0236 -0.0286 -0.0082 1038 LYS A C   
3938 O O   . LYS A 501 ? 0.3244 0.3505 0.3977 -0.0233 -0.0332 -0.0042 1038 LYS A O   
3939 C CB  . LYS A 501 ? 0.3929 0.4347 0.5258 -0.0276 -0.0521 -0.0058 1038 LYS A CB  
3940 C CG  . LYS A 501 ? 0.7085 0.7646 0.8797 -0.0234 -0.0510 -0.0015 1038 LYS A CG  
3941 C CD  . LYS A 501 ? 0.8700 0.9338 1.0647 -0.0260 -0.0704 0.0038  1038 LYS A CD  
3942 C CE  . LYS A 501 ? 0.9374 1.0129 1.1582 -0.0333 -0.0723 0.0038  1038 LYS A CE  
3943 N NZ  . LYS A 501 ? 0.9736 1.0441 1.1981 -0.0405 -0.0984 0.0054  1038 LYS A NZ  
3944 N N   . SER A 502 ? 0.3005 0.3339 0.4119 -0.0201 -0.0195 -0.0090 1039 SER A N   
3945 C CA  . SER A 502 ? 0.3016 0.3278 0.4040 -0.0191 -0.0182 -0.0042 1039 SER A CA  
3946 C C   . SER A 502 ? 0.3133 0.3368 0.4255 -0.0177 -0.0304 0.0054  1039 SER A C   
3947 O O   . SER A 502 ? 0.3264 0.3539 0.4598 -0.0143 -0.0371 0.0050  1039 SER A O   
3948 C CB  . SER A 502 ? 0.3384 0.3610 0.4491 -0.0154 -0.0098 -0.0105 1039 SER A CB  
3949 O OG  . SER A 502 ? 0.3741 0.3871 0.4843 -0.0162 -0.0141 -0.0046 1039 SER A OG  
3950 N N   . PRO A 503 ? 0.3237 0.3424 0.4236 -0.0201 -0.0335 0.0167  1040 PRO A N   
3951 C CA  . PRO A 503 ? 0.3857 0.3991 0.4977 -0.0191 -0.0454 0.0284  1040 PRO A CA  
3952 C C   . PRO A 503 ? 0.4342 0.4373 0.5700 -0.0154 -0.0476 0.0251  1040 PRO A C   
3953 O O   . PRO A 503 ? 0.4581 0.4529 0.6079 -0.0133 -0.0593 0.0336  1040 PRO A O   
3954 C CB  . PRO A 503 ? 0.3506 0.3650 0.4426 -0.0233 -0.0448 0.0447  1040 PRO A CB  
3955 C CG  . PRO A 503 ? 0.3554 0.3735 0.4381 -0.0258 -0.0311 0.0398  1040 PRO A CG  
3956 C CD  . PRO A 503 ? 0.3426 0.3633 0.4204 -0.0232 -0.0256 0.0220  1040 PRO A CD  
3957 N N   . GLY A 504 ? 0.3931 0.3935 0.5309 -0.0131 -0.0385 0.0127  1041 GLY A N   
3958 C CA  . GLY A 504 ? 0.4318 0.4179 0.5851 -0.0063 -0.0425 0.0055  1041 GLY A CA  
3959 C C   . GLY A 504 ? 0.4867 0.4576 0.6408 -0.0126 -0.0498 0.0140  1041 GLY A C   
3960 O O   . GLY A 504 ? 0.4136 0.3901 0.5603 -0.0223 -0.0495 0.0294  1041 GLY A O   
3961 N N   . ILE A 505 ? 0.3732 0.3249 0.5376 -0.0061 -0.0572 0.0043  1042 ILE A N   
3962 C CA  . ILE A 505 ? 0.3797 0.3141 0.5502 -0.0137 -0.0681 0.0112  1042 ILE A CA  
3963 C C   . ILE A 505 ? 0.4250 0.3362 0.6161 -0.0122 -0.0880 0.0189  1042 ILE A C   
3964 O O   . ILE A 505 ? 0.4687 0.3584 0.6710 -0.0173 -0.1024 0.0221  1042 ILE A O   
3965 C CB  . ILE A 505 ? 0.4091 0.3329 0.5714 -0.0094 -0.0664 -0.0063 1042 ILE A CB  
3966 C CG1 . ILE A 505 ? 0.5469 0.4572 0.7071 0.0094  -0.0677 -0.0280 1042 ILE A CG1 
3967 C CG2 . ILE A 505 ? 0.3897 0.3351 0.5339 -0.0136 -0.0488 -0.0085 1042 ILE A CG2 
3968 C CD1 . ILE A 505 ? 0.5665 0.4625 0.7117 0.0161  -0.0687 -0.0456 1042 ILE A CD1 
3969 N N   . ARG A 506 ? 0.4322 0.3459 0.6309 -0.0060 -0.0916 0.0229  1043 ARG A N   
3970 C CA  . ARG A 506 ? 0.4986 0.3906 0.7172 -0.0064 -0.1117 0.0355  1043 ARG A CA  
3971 C C   . ARG A 506 ? 0.5036 0.4045 0.7240 -0.0231 -0.1146 0.0656  1043 ARG A C   
3972 O O   . ARG A 506 ? 0.5562 0.4810 0.7618 -0.0261 -0.1039 0.0753  1043 ARG A O   
3973 C CB  . ARG A 506 ? 0.4611 0.3538 0.6896 0.0077  -0.1157 0.0305  1043 ARG A CB  
3974 C CG  . ARG A 506 ? 0.7315 0.5959 0.9815 0.0100  -0.1387 0.0408  1043 ARG A CG  
3975 C CD  . ARG A 506 ? 0.8339 0.7005 1.0975 0.0241  -0.1448 0.0395  1043 ARG A CD  
3976 N NE  . ARG A 506 ? 0.9171 0.7493 1.2015 0.0292  -0.1687 0.0453  1043 ARG A NE  
3977 C CZ  . ARG A 506 ? 0.9073 0.7332 1.2093 0.0422  -0.1801 0.0471  1043 ARG A CZ  
3978 N NH1 . ARG A 506 ? 0.7746 0.6296 1.0784 0.0503  -0.1700 0.0443  1043 ARG A NH1 
3979 N NH2 . ARG A 506 ? 0.7685 0.5580 1.0892 0.0467  -0.2040 0.0523  1043 ARG A NH2 
3980 N N   . PRO A 507 ? 0.5786 0.4614 0.8163 -0.0335 -0.1293 0.0819  1044 PRO A N   
3981 C CA  . PRO A 507 ? 0.6747 0.5708 0.9163 -0.0485 -0.1295 0.1159  1044 PRO A CA  
3982 C C   . PRO A 507 ? 0.8156 0.7132 1.0568 -0.0448 -0.1361 0.1309  1044 PRO A C   
3983 O O   . PRO A 507 ? 0.7922 0.6708 1.0447 -0.0337 -0.1489 0.1202  1044 PRO A O   
3984 C CB  . PRO A 507 ? 0.6192 0.4911 0.8897 -0.0602 -0.1486 0.1297  1044 PRO A CB  
3985 C CG  . PRO A 507 ? 0.7123 0.5581 0.9852 -0.0510 -0.1572 0.0979  1044 PRO A CG  
3986 C CD  . PRO A 507 ? 0.6890 0.5365 0.9444 -0.0311 -0.1486 0.0710  1044 PRO A CD  
3987 N N   . ASN A 508 ? 0.8282 0.7492 1.0547 -0.0522 -0.1273 0.1559  1045 ASN A N   
3988 C CA  . ASN A 508 ? 0.9230 0.8466 1.1430 -0.0485 -0.1345 0.1719  1045 ASN A CA  
3989 C C   . ASN A 508 ? 0.9168 0.8254 1.1587 -0.0582 -0.1511 0.2051  1045 ASN A C   
3990 O O   . ASN A 508 ? 0.9984 0.9242 1.2352 -0.0690 -0.1439 0.2351  1045 ASN A O   
3991 C CB  . ASN A 508 ? 1.0405 0.9944 1.2241 -0.0474 -0.1183 0.1794  1045 ASN A CB  
3992 C CG  . ASN A 508 ? 1.1221 1.0863 1.2871 -0.0377 -0.1081 0.1487  1045 ASN A CG  
3993 O OD1 . ASN A 508 ? 1.2126 1.1786 1.3703 -0.0299 -0.1142 0.1420  1045 ASN A OD1 
3994 N ND2 . ASN A 508 ? 1.0013 0.9723 1.1615 -0.0389 -0.0943 0.1321  1045 ASN A ND2 
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