data_9BVE
# 
_entry.id   9BVE 
# 
_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   9BVE         pdb_00009bve 10.2210/pdb9bve/pdb 
WWPDB D_1000283497 ?            ?                   
# 
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                        9BVE 
_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 'N-(1H-indol-5-yl)-4-[4-(propan-2-yl)piperazin-1-yl]-5,6,7,8-tetrahydroquinazolin-2-amine' 390.525   1   ? ? ? ? 
3 water       nat water                                                                                      18.015    252 ? ? ? ? 
# 
_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 'N-(1H-indol-5-yl)-4-[4-(propan-2-yl)piperazin-1-yl]-5,6,7,8-tetrahydroquinazolin-2-amine' A1ASY 
3 water                                                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   TYR n 
1 4   TYR n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  LEU n 
1 12  GLU n 
1 13  SER n 
1 14  THR n 
1 15  SER n 
1 16  LEU n 
1 17  TYR n 
1 18  LYS n 
1 19  LYS n 
1 20  ALA n 
1 21  GLY n 
1 22  PHE n 
1 23  GLU n 
1 24  ASN n 
1 25  LEU n 
1 26  TYR n 
1 27  PHE n 
1 28  GLN n 
1 29  GLU n 
1 30  GLN n 
1 31  PRO n 
1 32  LEU n 
1 33  ARG n 
1 34  LEU n 
1 35  PRO n 
1 36  SER n 
1 37  PRO n 
1 38  GLU n 
1 39  VAL n 
1 40  TYR n 
1 41  ARG n 
1 42  PHE n 
1 43  VAL n 
1 44  VAL n 
1 45  LYS n 
1 46  ASP n 
1 47  SER n 
1 48  GLU n 
1 49  GLU n 
1 50  ASN n 
1 51  ILE n 
1 52  VAL n 
1 53  PHE n 
1 54  GLU n 
1 55  ASP n 
1 56  ASN n 
1 57  LEU n 
1 58  GLN n 
1 59  SER n 
1 60  ARG n 
1 61  SER n 
1 62  GLY n 
1 63  ILE n 
1 64  PRO n 
1 65  ILE n 
1 66  ILE n 
1 67  LYS n 
1 68  GLY n 
1 69  GLY n 
1 70  THR n 
1 71  VAL n 
1 72  VAL n 
1 73  LYS n 
1 74  LEU n 
1 75  ILE n 
1 76  GLU n 
1 77  ARG n 
1 78  LEU n 
1 79  THR n 
1 80  TYR n 
1 81  HIS n 
1 82  MET n 
1 83  TYR n 
1 84  ALA n 
1 85  ASP n 
1 86  PRO n 
1 87  ASN n 
1 88  PHE n 
1 89  VAL n 
1 90  ARG n 
1 91  THR n 
1 92  PHE n 
1 93  LEU n 
1 94  THR n 
1 95  THR n 
1 96  TYR n 
1 97  ARG n 
1 98  SER n 
1 99  PHE n 
1 100 CYS n 
1 101 LYS n 
1 102 PRO n 
1 103 GLN n 
1 104 GLU n 
1 105 LEU n 
1 106 LEU n 
1 107 SER n 
1 108 LEU n 
1 109 LEU n 
1 110 ILE n 
1 111 GLU n 
1 112 ARG n 
1 113 PHE n 
1 114 GLU n 
1 115 ILE n 
1 116 PRO n 
1 117 GLU n 
1 118 PRO n 
1 119 GLU n 
1 120 PRO n 
1 121 THR n 
1 122 ASP n 
1 123 ALA n 
1 124 ASP n 
1 125 LYS n 
1 126 LEU n 
1 127 ALA n 
1 128 ILE n 
1 129 GLU n 
1 130 LYS n 
1 131 GLY n 
1 132 GLU n 
1 133 GLN n 
1 134 PRO n 
1 135 ILE n 
1 136 SER n 
1 137 ALA n 
1 138 ASP n 
1 139 LEU n 
1 140 LYS n 
1 141 ARG n 
1 142 PHE n 
1 143 ARG n 
1 144 LYS n 
1 145 GLU n 
1 146 TYR n 
1 147 VAL n 
1 148 GLN n 
1 149 PRO n 
1 150 VAL n 
1 151 GLN n 
1 152 LEU n 
1 153 ARG n 
1 154 ILE n 
1 155 LEU n 
1 156 ASN n 
1 157 VAL n 
1 158 PHE n 
1 159 ARG n 
1 160 HIS n 
1 161 TRP n 
1 162 VAL n 
1 163 GLU n 
1 164 HIS n 
1 165 HIS n 
1 166 PHE n 
1 167 TYR n 
1 168 ASP n 
1 169 PHE n 
1 170 GLU n 
1 171 ARG n 
1 172 ASP n 
1 173 LEU n 
1 174 GLU n 
1 175 LEU n 
1 176 LEU n 
1 177 GLU n 
1 178 ARG n 
1 179 LEU n 
1 180 GLU n 
1 181 SER n 
1 182 PHE n 
1 183 ILE n 
1 184 SER n 
1 185 SER n 
1 186 VAL n 
1 187 ARG n 
1 188 GLY n 
1 189 LYS n 
1 190 ALA n 
1 191 MET n 
1 192 LYS n 
1 193 LYS n 
1 194 TRP n 
1 195 VAL n 
1 196 GLU n 
1 197 SER n 
1 198 ILE n 
1 199 ALA n 
1 200 LYS n 
1 201 ILE n 
1 202 ILE n 
1 203 ARG n 
1 204 ARG n 
1 205 LYS n 
1 206 LYS n 
1 207 GLN n 
1 208 ALA n 
1 209 GLN n 
1 210 ALA n 
1 211 ASN n 
1 212 GLY n 
1 213 VAL n 
1 214 SER n 
1 215 HIS n 
1 216 ASN n 
1 217 ILE n 
1 218 THR n 
1 219 PHE n 
1 220 GLU n 
1 221 SER n 
1 222 PRO n 
1 223 PRO n 
1 224 PRO n 
1 225 PRO n 
1 226 ILE n 
1 227 GLU n 
1 228 TRP n 
1 229 HIS n 
1 230 ILE n 
1 231 SER n 
1 232 LYS n 
1 233 PRO n 
1 234 GLY n 
1 235 GLN n 
1 236 PHE n 
1 237 GLU n 
1 238 THR n 
1 239 PHE n 
1 240 ASP n 
1 241 LEU n 
1 242 MET n 
1 243 THR n 
1 244 LEU n 
1 245 HIS n 
1 246 PRO n 
1 247 ILE n 
1 248 GLU n 
1 249 ILE n 
1 250 ALA n 
1 251 ARG n 
1 252 GLN n 
1 253 LEU n 
1 254 THR n 
1 255 LEU n 
1 256 LEU n 
1 257 GLU n 
1 258 SER n 
1 259 ASP n 
1 260 LEU n 
1 261 TYR n 
1 262 ARG n 
1 263 LYS n 
1 264 VAL n 
1 265 GLN n 
1 266 PRO n 
1 267 SER n 
1 268 GLU n 
1 269 LEU n 
1 270 VAL n 
1 271 GLY n 
1 272 SER n 
1 273 VAL n 
1 274 TRP n 
1 275 THR n 
1 276 LYS n 
1 277 GLU n 
1 278 ASP n 
1 279 LYS n 
1 280 GLU n 
1 281 ILE n 
1 282 ASN n 
1 283 SER n 
1 284 PRO n 
1 285 ASN n 
1 286 LEU n 
1 287 LEU n 
1 288 LYS n 
1 289 MET n 
1 290 ILE n 
1 291 ARG n 
1 292 HIS n 
1 293 THR n 
1 294 THR n 
1 295 ASN n 
1 296 LEU n 
1 297 THR n 
1 298 LEU n 
1 299 TRP n 
1 300 PHE n 
1 301 GLU n 
1 302 LYS n 
1 303 CYS n 
1 304 ILE n 
1 305 VAL n 
1 306 GLU n 
1 307 ALA n 
1 308 GLU n 
1 309 ASN n 
1 310 PHE n 
1 311 GLU n 
1 312 GLU n 
1 313 ARG n 
1 314 VAL n 
1 315 ALA n 
1 316 VAL n 
1 317 LEU n 
1 318 SER n 
1 319 ARG n 
1 320 ILE n 
1 321 ILE n 
1 322 GLU n 
1 323 ILE n 
1 324 LEU n 
1 325 GLN n 
1 326 VAL n 
1 327 PHE n 
1 328 GLN n 
1 329 ASP n 
1 330 LEU n 
1 331 ASN n 
1 332 ASN n 
1 333 PHE n 
1 334 ASN n 
1 335 GLY n 
1 336 VAL n 
1 337 LEU n 
1 338 GLU n 
1 339 ILE n 
1 340 VAL n 
1 341 SER n 
1 342 ALA n 
1 343 VAL n 
1 344 ASN n 
1 345 SER n 
1 346 VAL n 
1 347 SER n 
1 348 VAL n 
1 349 TYR n 
1 350 ARG n 
1 351 LEU n 
1 352 ASP n 
1 353 HIS n 
1 354 THR n 
1 355 PHE n 
1 356 GLU n 
1 357 ALA n 
1 358 LEU n 
1 359 GLN n 
1 360 GLU n 
1 361 ARG n 
1 362 LYS n 
1 363 ARG n 
1 364 LYS n 
1 365 ILE n 
1 366 LEU n 
1 367 ASP n 
1 368 GLU n 
1 369 ALA n 
1 370 VAL n 
1 371 GLU n 
1 372 LEU n 
1 373 SER n 
1 374 GLN n 
1 375 ASP n 
1 376 HIS n 
1 377 PHE n 
1 378 LYS n 
1 379 LYS n 
1 380 TYR n 
1 381 LEU n 
1 382 VAL n 
1 383 LYS n 
1 384 LEU n 
1 385 LYS n 
1 386 SER n 
1 387 ILE n 
1 388 ASN n 
1 389 PRO n 
1 390 PRO n 
1 391 CYS n 
1 392 VAL n 
1 393 PRO n 
1 394 PHE n 
1 395 PHE n 
1 396 GLY n 
1 397 ILE n 
1 398 TYR n 
1 399 LEU n 
1 400 THR n 
1 401 ASN n 
1 402 ILE n 
1 403 LEU n 
1 404 LYS n 
1 405 THR n 
1 406 GLU n 
1 407 GLU n 
1 408 GLY n 
1 409 ASN n 
1 410 ASN n 
1 411 ASP n 
1 412 PHE n 
1 413 LEU n 
1 414 LYS n 
1 415 LYS n 
1 416 LYS n 
1 417 GLY n 
1 418 LYS n 
1 419 ASP n 
1 420 LEU n 
1 421 ILE n 
1 422 ASN n 
1 423 PHE n 
1 424 SER n 
1 425 LYS n 
1 426 ARG n 
1 427 ARG n 
1 428 LYS n 
1 429 VAL n 
1 430 ALA n 
1 431 GLU n 
1 432 ILE n 
1 433 THR n 
1 434 GLY n 
1 435 GLU n 
1 436 ILE n 
1 437 GLN n 
1 438 GLN n 
1 439 TYR n 
1 440 GLN n 
1 441 ASN n 
1 442 GLN n 
1 443 PRO n 
1 444 TYR n 
1 445 CYS n 
1 446 LEU n 
1 447 ARG n 
1 448 ILE n 
1 449 GLU n 
1 450 PRO n 
1 451 ASP n 
1 452 MET n 
1 453 ARG n 
1 454 ARG n 
1 455 PHE n 
1 456 PHE n 
1 457 GLU n 
1 458 ASN n 
1 459 LEU n 
1 460 ASN n 
1 461 PRO n 
1 462 MET n 
1 463 GLY n 
1 464 SER n 
1 465 ALA n 
1 466 SER n 
1 467 GLU n 
1 468 LYS n 
1 469 GLU n 
1 470 PHE n 
1 471 THR n 
1 472 ASP n 
1 473 TYR n 
1 474 LEU n 
1 475 PHE n 
1 476 ASN n 
1 477 LYS n 
1 478 SER n 
1 479 LEU n 
1 480 GLU n 
1 481 ILE n 
1 482 GLU n 
1 483 PRO n 
1 484 ARG n 
1 485 ASN n 
1 486 CYS n 
1 487 LYS n 
1 488 GLN n 
1 489 PRO n 
1 490 PRO n 
1 491 ARG n 
1 492 PHE n 
1 493 PRO n 
1 494 ARG n 
1 495 LYS n 
1 496 SER n 
1 497 THR n 
1 498 PHE n 
1 499 SER n 
1 500 LEU n 
1 501 LYS n 
1 502 SER n 
1 503 PRO n 
1 504 GLY n 
1 505 ILE n 
1 506 ARG n 
1 507 PRO n 
1 508 ASN n 
1 509 THR n 
1 510 GLY n 
1 511 ARG n 
1 512 HIS n 
1 513 GLY n 
1 514 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   514 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOS2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ASY non-polymer         . 'N-(1H-indol-5-yl)-4-[4-(propan-2-yl)piperazin-1-yl]-5,6,7,8-tetrahydroquinazolin-2-amine' ? 
'C23 H30 N6'     390.525 
ALA   'L-peptide linking' y ALANINE                                                                                    ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                   ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                 ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                            ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                   ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                  ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                            ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                    ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                  ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                      ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                 ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                    ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                     ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                 ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                              ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                    ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                     ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                  ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                 ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                   ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                     ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -28  ?    ?   ?   A . n 
A 1 2   SER 2   -27  ?    ?   ?   A . n 
A 1 3   TYR 3   -26  ?    ?   ?   A . n 
A 1 4   TYR 4   -25  ?    ?   ?   A . n 
A 1 5   HIS 5   -24  ?    ?   ?   A . n 
A 1 6   HIS 6   -23  ?    ?   ?   A . n 
A 1 7   HIS 7   -22  ?    ?   ?   A . n 
A 1 8   HIS 8   -21  ?    ?   ?   A . n 
A 1 9   HIS 9   -20  ?    ?   ?   A . n 
A 1 10  HIS 10  -19  ?    ?   ?   A . n 
A 1 11  LEU 11  -18  ?    ?   ?   A . n 
A 1 12  GLU 12  -17  ?    ?   ?   A . n 
A 1 13  SER 13  -16  ?    ?   ?   A . n 
A 1 14  THR 14  -15  ?    ?   ?   A . n 
A 1 15  SER 15  -14  ?    ?   ?   A . n 
A 1 16  LEU 16  -13  ?    ?   ?   A . n 
A 1 17  TYR 17  -12  ?    ?   ?   A . n 
A 1 18  LYS 18  -11  ?    ?   ?   A . n 
A 1 19  LYS 19  -10  ?    ?   ?   A . n 
A 1 20  ALA 20  -9   ?    ?   ?   A . n 
A 1 21  GLY 21  -8   ?    ?   ?   A . n 
A 1 22  PHE 22  -7   ?    ?   ?   A . n 
A 1 23  GLU 23  -6   ?    ?   ?   A . n 
A 1 24  ASN 24  -5   ?    ?   ?   A . n 
A 1 25  LEU 25  -4   -4   LEU LEU A . n 
A 1 26  TYR 26  -3   -3   TYR TYR A . n 
A 1 27  PHE 27  -2   -2   PHE PHE A . n 
A 1 28  GLN 28  -1   -1   GLN GLN A . n 
A 1 29  GLU 29  566  566  GLU GLU A . n 
A 1 30  GLN 30  567  567  GLN GLN A . n 
A 1 31  PRO 31  568  568  PRO PRO A . n 
A 1 32  LEU 32  569  569  LEU LEU A . n 
A 1 33  ARG 33  570  570  ARG ARG A . n 
A 1 34  LEU 34  571  571  LEU LEU A . n 
A 1 35  PRO 35  572  572  PRO PRO A . n 
A 1 36  SER 36  573  573  SER SER A . n 
A 1 37  PRO 37  574  574  PRO PRO A . n 
A 1 38  GLU 38  575  575  GLU GLU A . n 
A 1 39  VAL 39  576  576  VAL VAL A . n 
A 1 40  TYR 40  577  577  TYR TYR A . n 
A 1 41  ARG 41  578  578  ARG ARG A . n 
A 1 42  PHE 42  579  579  PHE PHE A . n 
A 1 43  VAL 43  580  580  VAL VAL A . n 
A 1 44  VAL 44  581  581  VAL VAL A . n 
A 1 45  LYS 45  582  582  LYS LYS A . n 
A 1 46  ASP 46  583  583  ASP ASP A . n 
A 1 47  SER 47  584  584  SER SER A . n 
A 1 48  GLU 48  585  585  GLU GLU A . n 
A 1 49  GLU 49  586  586  GLU GLU A . n 
A 1 50  ASN 50  587  587  ASN ASN A . n 
A 1 51  ILE 51  588  588  ILE ILE A . n 
A 1 52  VAL 52  589  589  VAL VAL A . n 
A 1 53  PHE 53  590  590  PHE PHE A . n 
A 1 54  GLU 54  591  591  GLU GLU A . n 
A 1 55  ASP 55  592  592  ASP ASP A . n 
A 1 56  ASN 56  593  ?    ?   ?   A . n 
A 1 57  LEU 57  594  ?    ?   ?   A . n 
A 1 58  GLN 58  595  ?    ?   ?   A . n 
A 1 59  SER 59  596  ?    ?   ?   A . n 
A 1 60  ARG 60  597  ?    ?   ?   A . n 
A 1 61  SER 61  598  ?    ?   ?   A . n 
A 1 62  GLY 62  599  599  GLY GLY A . n 
A 1 63  ILE 63  600  600  ILE ILE A . n 
A 1 64  PRO 64  601  601  PRO PRO A . n 
A 1 65  ILE 65  602  602  ILE ILE A . n 
A 1 66  ILE 66  603  603  ILE ILE A . n 
A 1 67  LYS 67  604  604  LYS LYS A . n 
A 1 68  GLY 68  605  605  GLY GLY A . n 
A 1 69  GLY 69  606  606  GLY GLY A . n 
A 1 70  THR 70  607  607  THR THR A . n 
A 1 71  VAL 71  608  608  VAL VAL A . n 
A 1 72  VAL 72  609  609  VAL VAL A . n 
A 1 73  LYS 73  610  610  LYS LYS A . n 
A 1 74  LEU 74  611  611  LEU LEU A . n 
A 1 75  ILE 75  612  612  ILE ILE A . n 
A 1 76  GLU 76  613  613  GLU GLU A . n 
A 1 77  ARG 77  614  614  ARG ARG A . n 
A 1 78  LEU 78  615  615  LEU LEU A . n 
A 1 79  THR 79  616  616  THR THR A . n 
A 1 80  TYR 80  617  617  TYR TYR A . n 
A 1 81  HIS 81  618  618  HIS HIS A . n 
A 1 82  MET 82  619  619  MET MET A . n 
A 1 83  TYR 83  620  620  TYR TYR A . n 
A 1 84  ALA 84  621  621  ALA ALA A . n 
A 1 85  ASP 85  622  622  ASP ASP A . n 
A 1 86  PRO 86  623  623  PRO PRO A . n 
A 1 87  ASN 87  624  624  ASN ASN A . n 
A 1 88  PHE 88  625  625  PHE PHE A . n 
A 1 89  VAL 89  626  626  VAL VAL A . n 
A 1 90  ARG 90  627  627  ARG ARG A . n 
A 1 91  THR 91  628  628  THR THR A . n 
A 1 92  PHE 92  629  629  PHE PHE A . n 
A 1 93  LEU 93  630  630  LEU LEU A . n 
A 1 94  THR 94  631  631  THR THR A . n 
A 1 95  THR 95  632  632  THR THR A . n 
A 1 96  TYR 96  633  633  TYR TYR A . n 
A 1 97  ARG 97  634  634  ARG ARG A . n 
A 1 98  SER 98  635  635  SER SER A . n 
A 1 99  PHE 99  636  636  PHE PHE A . n 
A 1 100 CYS 100 637  637  CYS CYS A . n 
A 1 101 LYS 101 638  638  LYS LYS A . n 
A 1 102 PRO 102 639  639  PRO PRO A . n 
A 1 103 GLN 103 640  640  GLN GLN A . n 
A 1 104 GLU 104 641  641  GLU GLU A . n 
A 1 105 LEU 105 642  642  LEU LEU A . n 
A 1 106 LEU 106 643  643  LEU LEU A . n 
A 1 107 SER 107 644  644  SER SER A . n 
A 1 108 LEU 108 645  645  LEU LEU A . n 
A 1 109 LEU 109 646  646  LEU LEU A . n 
A 1 110 ILE 110 647  647  ILE ILE A . n 
A 1 111 GLU 111 648  648  GLU GLU A . n 
A 1 112 ARG 112 649  649  ARG ARG A . n 
A 1 113 PHE 113 650  650  PHE PHE A . n 
A 1 114 GLU 114 651  651  GLU GLU A . n 
A 1 115 ILE 115 652  652  ILE ILE A . n 
A 1 116 PRO 116 653  653  PRO PRO A . n 
A 1 117 GLU 117 654  654  GLU GLU A . n 
A 1 118 PRO 118 655  655  PRO PRO A . n 
A 1 119 GLU 119 656  656  GLU GLU A . n 
A 1 120 PRO 120 657  657  PRO PRO A . n 
A 1 121 THR 121 658  658  THR THR A . n 
A 1 122 ASP 122 659  659  ASP ASP A . n 
A 1 123 ALA 123 660  660  ALA ALA A . n 
A 1 124 ASP 124 661  661  ASP ASP A . n 
A 1 125 LYS 125 662  662  LYS LYS A . n 
A 1 126 LEU 126 663  663  LEU LEU A . n 
A 1 127 ALA 127 664  664  ALA ALA A . n 
A 1 128 ILE 128 665  665  ILE ILE A . n 
A 1 129 GLU 129 666  666  GLU GLU A . n 
A 1 130 LYS 130 667  667  LYS LYS A . n 
A 1 131 GLY 131 668  668  GLY GLY A . n 
A 1 132 GLU 132 669  669  GLU GLU A . n 
A 1 133 GLN 133 670  670  GLN GLN A . n 
A 1 134 PRO 134 671  671  PRO PRO A . n 
A 1 135 ILE 135 672  672  ILE ILE A . n 
A 1 136 SER 136 673  673  SER SER A . n 
A 1 137 ALA 137 674  674  ALA ALA A . n 
A 1 138 ASP 138 675  675  ASP ASP A . n 
A 1 139 LEU 139 676  676  LEU LEU A . n 
A 1 140 LYS 140 677  677  LYS LYS A . n 
A 1 141 ARG 141 678  678  ARG ARG A . n 
A 1 142 PHE 142 679  679  PHE PHE A . n 
A 1 143 ARG 143 680  680  ARG ARG A . n 
A 1 144 LYS 144 681  681  LYS LYS A . n 
A 1 145 GLU 145 682  682  GLU GLU A . n 
A 1 146 TYR 146 683  683  TYR TYR A . n 
A 1 147 VAL 147 684  684  VAL VAL A . n 
A 1 148 GLN 148 685  685  GLN GLN A . n 
A 1 149 PRO 149 686  686  PRO PRO A . n 
A 1 150 VAL 150 687  687  VAL VAL A . n 
A 1 151 GLN 151 688  688  GLN GLN A . n 
A 1 152 LEU 152 689  689  LEU LEU A . n 
A 1 153 ARG 153 690  690  ARG ARG A . n 
A 1 154 ILE 154 691  691  ILE ILE A . n 
A 1 155 LEU 155 692  692  LEU LEU A . n 
A 1 156 ASN 156 693  693  ASN ASN A . n 
A 1 157 VAL 157 694  694  VAL VAL A . n 
A 1 158 PHE 158 695  695  PHE PHE A . n 
A 1 159 ARG 159 696  696  ARG ARG A . n 
A 1 160 HIS 160 697  697  HIS HIS A . n 
A 1 161 TRP 161 698  698  TRP TRP A . n 
A 1 162 VAL 162 699  699  VAL VAL A . n 
A 1 163 GLU 163 700  700  GLU GLU A . n 
A 1 164 HIS 164 701  701  HIS HIS A . n 
A 1 165 HIS 165 702  702  HIS HIS A . n 
A 1 166 PHE 166 703  703  PHE PHE A . n 
A 1 167 TYR 167 704  704  TYR TYR A . n 
A 1 168 ASP 168 705  705  ASP ASP A . n 
A 1 169 PHE 169 706  706  PHE PHE A . n 
A 1 170 GLU 170 707  707  GLU GLU A . n 
A 1 171 ARG 171 708  708  ARG ARG A . n 
A 1 172 ASP 172 709  709  ASP ASP A . n 
A 1 173 LEU 173 710  710  LEU LEU A . n 
A 1 174 GLU 174 711  711  GLU GLU A . n 
A 1 175 LEU 175 712  712  LEU LEU A . n 
A 1 176 LEU 176 713  713  LEU LEU A . n 
A 1 177 GLU 177 714  714  GLU GLU A . n 
A 1 178 ARG 178 715  715  ARG ARG A . n 
A 1 179 LEU 179 716  716  LEU LEU A . n 
A 1 180 GLU 180 717  717  GLU GLU A . n 
A 1 181 SER 181 718  718  SER SER A . n 
A 1 182 PHE 182 719  719  PHE PHE A . n 
A 1 183 ILE 183 720  720  ILE ILE A . n 
A 1 184 SER 184 721  721  SER SER A . n 
A 1 185 SER 185 722  722  SER SER A . n 
A 1 186 VAL 186 723  723  VAL VAL A . n 
A 1 187 ARG 187 724  724  ARG ARG A . n 
A 1 188 GLY 188 725  725  GLY GLY A . n 
A 1 189 LYS 189 726  726  LYS LYS A . n 
A 1 190 ALA 190 727  727  ALA ALA A . n 
A 1 191 MET 191 728  728  MET MET A . n 
A 1 192 LYS 192 729  729  LYS LYS A . n 
A 1 193 LYS 193 730  730  LYS LYS A . n 
A 1 194 TRP 194 731  731  TRP TRP A . n 
A 1 195 VAL 195 732  732  VAL VAL A . n 
A 1 196 GLU 196 733  733  GLU GLU A . n 
A 1 197 SER 197 734  734  SER SER A . n 
A 1 198 ILE 198 735  735  ILE ILE A . n 
A 1 199 ALA 199 736  736  ALA ALA A . n 
A 1 200 LYS 200 737  737  LYS LYS A . n 
A 1 201 ILE 201 738  738  ILE ILE A . n 
A 1 202 ILE 202 739  739  ILE ILE A . n 
A 1 203 ARG 203 740  740  ARG ARG A . n 
A 1 204 ARG 204 741  741  ARG ARG A . n 
A 1 205 LYS 205 742  742  LYS LYS A . n 
A 1 206 LYS 206 743  743  LYS LYS A . n 
A 1 207 GLN 207 744  744  GLN GLN A . n 
A 1 208 ALA 208 745  745  ALA ALA A . n 
A 1 209 GLN 209 746  ?    ?   ?   A . n 
A 1 210 ALA 210 747  ?    ?   ?   A . n 
A 1 211 ASN 211 748  ?    ?   ?   A . n 
A 1 212 GLY 212 749  ?    ?   ?   A . n 
A 1 213 VAL 213 750  ?    ?   ?   A . n 
A 1 214 SER 214 751  ?    ?   ?   A . n 
A 1 215 HIS 215 752  ?    ?   ?   A . n 
A 1 216 ASN 216 753  ?    ?   ?   A . n 
A 1 217 ILE 217 754  754  ILE ILE A . n 
A 1 218 THR 218 755  755  THR THR A . n 
A 1 219 PHE 219 756  756  PHE PHE A . n 
A 1 220 GLU 220 757  757  GLU GLU A . n 
A 1 221 SER 221 758  758  SER SER A . n 
A 1 222 PRO 222 759  759  PRO PRO A . n 
A 1 223 PRO 223 760  760  PRO PRO A . n 
A 1 224 PRO 224 761  761  PRO PRO A . n 
A 1 225 PRO 225 762  762  PRO PRO A . n 
A 1 226 ILE 226 763  763  ILE ILE A . n 
A 1 227 GLU 227 764  764  GLU GLU A . n 
A 1 228 TRP 228 765  765  TRP TRP A . n 
A 1 229 HIS 229 766  766  HIS HIS A . n 
A 1 230 ILE 230 767  767  ILE ILE A . n 
A 1 231 SER 231 768  768  SER SER A . n 
A 1 232 LYS 232 769  769  LYS LYS A . n 
A 1 233 PRO 233 770  770  PRO PRO A . n 
A 1 234 GLY 234 771  771  GLY GLY A . n 
A 1 235 GLN 235 772  772  GLN GLN A . n 
A 1 236 PHE 236 773  773  PHE PHE A . n 
A 1 237 GLU 237 774  774  GLU GLU A . n 
A 1 238 THR 238 775  775  THR THR A . n 
A 1 239 PHE 239 776  776  PHE PHE A . n 
A 1 240 ASP 240 777  777  ASP ASP A . n 
A 1 241 LEU 241 778  778  LEU LEU A . n 
A 1 242 MET 242 779  779  MET MET A . n 
A 1 243 THR 243 780  780  THR THR A . n 
A 1 244 LEU 244 781  781  LEU LEU A . n 
A 1 245 HIS 245 782  782  HIS HIS A . n 
A 1 246 PRO 246 783  783  PRO PRO A . n 
A 1 247 ILE 247 784  784  ILE ILE A . n 
A 1 248 GLU 248 785  785  GLU GLU A . n 
A 1 249 ILE 249 786  786  ILE ILE A . n 
A 1 250 ALA 250 787  787  ALA ALA A . n 
A 1 251 ARG 251 788  788  ARG ARG A . n 
A 1 252 GLN 252 789  789  GLN GLN A . n 
A 1 253 LEU 253 790  790  LEU LEU A . n 
A 1 254 THR 254 791  791  THR THR A . n 
A 1 255 LEU 255 792  792  LEU LEU A . n 
A 1 256 LEU 256 793  793  LEU LEU A . n 
A 1 257 GLU 257 794  794  GLU GLU A . n 
A 1 258 SER 258 795  795  SER SER A . n 
A 1 259 ASP 259 796  796  ASP ASP A . n 
A 1 260 LEU 260 797  797  LEU LEU A . n 
A 1 261 TYR 261 798  798  TYR TYR A . n 
A 1 262 ARG 262 799  799  ARG ARG A . n 
A 1 263 LYS 263 800  800  LYS LYS A . n 
A 1 264 VAL 264 801  801  VAL VAL A . n 
A 1 265 GLN 265 802  802  GLN GLN A . n 
A 1 266 PRO 266 803  803  PRO PRO A . n 
A 1 267 SER 267 804  804  SER SER A . n 
A 1 268 GLU 268 805  805  GLU GLU A . n 
A 1 269 LEU 269 806  806  LEU LEU A . n 
A 1 270 VAL 270 807  807  VAL VAL A . n 
A 1 271 GLY 271 808  808  GLY GLY A . n 
A 1 272 SER 272 809  809  SER SER A . n 
A 1 273 VAL 273 810  810  VAL VAL A . n 
A 1 274 TRP 274 811  811  TRP TRP A . n 
A 1 275 THR 275 812  812  THR THR A . n 
A 1 276 LYS 276 813  813  LYS LYS A . n 
A 1 277 GLU 277 814  814  GLU GLU A . n 
A 1 278 ASP 278 815  815  ASP ASP A . n 
A 1 279 LYS 279 816  816  LYS LYS A . n 
A 1 280 GLU 280 817  817  GLU GLU A . n 
A 1 281 ILE 281 818  818  ILE ILE A . n 
A 1 282 ASN 282 819  819  ASN ASN A . n 
A 1 283 SER 283 820  820  SER SER A . n 
A 1 284 PRO 284 821  821  PRO PRO A . n 
A 1 285 ASN 285 822  822  ASN ASN A . n 
A 1 286 LEU 286 823  823  LEU LEU A . n 
A 1 287 LEU 287 824  824  LEU LEU A . n 
A 1 288 LYS 288 825  825  LYS LYS A . n 
A 1 289 MET 289 826  826  MET MET A . n 
A 1 290 ILE 290 827  827  ILE ILE A . n 
A 1 291 ARG 291 828  828  ARG ARG A . n 
A 1 292 HIS 292 829  829  HIS HIS A . n 
A 1 293 THR 293 830  830  THR THR A . n 
A 1 294 THR 294 831  831  THR THR A . n 
A 1 295 ASN 295 832  832  ASN ASN A . n 
A 1 296 LEU 296 833  833  LEU LEU A . n 
A 1 297 THR 297 834  834  THR THR A . n 
A 1 298 LEU 298 835  835  LEU LEU A . n 
A 1 299 TRP 299 836  836  TRP TRP A . n 
A 1 300 PHE 300 837  837  PHE PHE A . n 
A 1 301 GLU 301 838  838  GLU GLU A . n 
A 1 302 LYS 302 839  839  LYS LYS A . n 
A 1 303 CYS 303 840  840  CYS CYS A . n 
A 1 304 ILE 304 841  841  ILE ILE A . n 
A 1 305 VAL 305 842  842  VAL VAL A . n 
A 1 306 GLU 306 843  843  GLU GLU A . n 
A 1 307 ALA 307 844  844  ALA ALA A . n 
A 1 308 GLU 308 845  845  GLU GLU A . n 
A 1 309 ASN 309 846  846  ASN ASN A . n 
A 1 310 PHE 310 847  847  PHE PHE A . n 
A 1 311 GLU 311 848  848  GLU GLU A . n 
A 1 312 GLU 312 849  849  GLU GLU A . n 
A 1 313 ARG 313 850  850  ARG ARG A . n 
A 1 314 VAL 314 851  851  VAL VAL A . n 
A 1 315 ALA 315 852  852  ALA ALA A . n 
A 1 316 VAL 316 853  853  VAL VAL A . n 
A 1 317 LEU 317 854  854  LEU LEU A . n 
A 1 318 SER 318 855  855  SER SER A . n 
A 1 319 ARG 319 856  856  ARG ARG A . n 
A 1 320 ILE 320 857  857  ILE ILE A . n 
A 1 321 ILE 321 858  858  ILE ILE A . n 
A 1 322 GLU 322 859  859  GLU GLU A . n 
A 1 323 ILE 323 860  860  ILE ILE A . n 
A 1 324 LEU 324 861  861  LEU LEU A . n 
A 1 325 GLN 325 862  862  GLN GLN A . n 
A 1 326 VAL 326 863  863  VAL VAL A . n 
A 1 327 PHE 327 864  864  PHE PHE A . n 
A 1 328 GLN 328 865  865  GLN GLN A . n 
A 1 329 ASP 329 866  866  ASP ASP A . n 
A 1 330 LEU 330 867  867  LEU LEU A . n 
A 1 331 ASN 331 868  868  ASN ASN A . n 
A 1 332 ASN 332 869  869  ASN ASN A . n 
A 1 333 PHE 333 870  870  PHE PHE A . n 
A 1 334 ASN 334 871  871  ASN ASN A . n 
A 1 335 GLY 335 872  872  GLY GLY A . n 
A 1 336 VAL 336 873  873  VAL VAL A . n 
A 1 337 LEU 337 874  874  LEU LEU A . n 
A 1 338 GLU 338 875  875  GLU GLU A . n 
A 1 339 ILE 339 876  876  ILE ILE A . n 
A 1 340 VAL 340 877  877  VAL VAL A . n 
A 1 341 SER 341 878  878  SER SER A . n 
A 1 342 ALA 342 879  879  ALA ALA A . n 
A 1 343 VAL 343 880  880  VAL VAL A . n 
A 1 344 ASN 344 881  881  ASN ASN A . n 
A 1 345 SER 345 882  882  SER SER A . n 
A 1 346 VAL 346 883  883  VAL VAL A . n 
A 1 347 SER 347 884  884  SER SER A . n 
A 1 348 VAL 348 885  885  VAL VAL A . n 
A 1 349 TYR 349 886  886  TYR TYR A . n 
A 1 350 ARG 350 887  887  ARG ARG A . n 
A 1 351 LEU 351 888  888  LEU LEU A . n 
A 1 352 ASP 352 889  889  ASP ASP A . n 
A 1 353 HIS 353 890  890  HIS HIS A . n 
A 1 354 THR 354 891  891  THR THR A . n 
A 1 355 PHE 355 892  892  PHE PHE A . n 
A 1 356 GLU 356 893  893  GLU GLU A . n 
A 1 357 ALA 357 894  894  ALA ALA A . n 
A 1 358 LEU 358 895  895  LEU LEU A . n 
A 1 359 GLN 359 896  896  GLN GLN A . n 
A 1 360 GLU 360 897  897  GLU GLU A . n 
A 1 361 ARG 361 898  898  ARG ARG A . n 
A 1 362 LYS 362 899  899  LYS LYS A . n 
A 1 363 ARG 363 900  900  ARG ARG A . n 
A 1 364 LYS 364 901  901  LYS LYS A . n 
A 1 365 ILE 365 902  902  ILE ILE A . n 
A 1 366 LEU 366 903  903  LEU LEU A . n 
A 1 367 ASP 367 904  904  ASP ASP A . n 
A 1 368 GLU 368 905  905  GLU GLU A . n 
A 1 369 ALA 369 906  906  ALA ALA A . n 
A 1 370 VAL 370 907  907  VAL VAL A . n 
A 1 371 GLU 371 908  908  GLU GLU A . n 
A 1 372 LEU 372 909  909  LEU LEU A . n 
A 1 373 SER 373 910  910  SER SER A . n 
A 1 374 GLN 374 911  911  GLN GLN A . n 
A 1 375 ASP 375 912  912  ASP ASP A . n 
A 1 376 HIS 376 913  913  HIS HIS A . n 
A 1 377 PHE 377 914  914  PHE PHE A . n 
A 1 378 LYS 378 915  915  LYS LYS A . n 
A 1 379 LYS 379 916  916  LYS LYS A . n 
A 1 380 TYR 380 917  917  TYR TYR A . n 
A 1 381 LEU 381 918  918  LEU LEU A . n 
A 1 382 VAL 382 919  919  VAL VAL A . n 
A 1 383 LYS 383 920  920  LYS LYS A . n 
A 1 384 LEU 384 921  921  LEU LEU A . n 
A 1 385 LYS 385 922  922  LYS LYS A . n 
A 1 386 SER 386 923  923  SER SER A . n 
A 1 387 ILE 387 924  924  ILE ILE A . n 
A 1 388 ASN 388 925  925  ASN ASN A . n 
A 1 389 PRO 389 926  926  PRO PRO A . n 
A 1 390 PRO 390 927  927  PRO PRO A . n 
A 1 391 CYS 391 928  928  CYS CYS A . n 
A 1 392 VAL 392 929  929  VAL VAL A . n 
A 1 393 PRO 393 930  930  PRO PRO A . n 
A 1 394 PHE 394 931  931  PHE PHE A . n 
A 1 395 PHE 395 932  932  PHE PHE A . n 
A 1 396 GLY 396 933  933  GLY GLY A . n 
A 1 397 ILE 397 934  934  ILE ILE A . n 
A 1 398 TYR 398 935  935  TYR TYR A . n 
A 1 399 LEU 399 936  936  LEU LEU A . n 
A 1 400 THR 400 937  937  THR THR A . n 
A 1 401 ASN 401 938  938  ASN ASN A . n 
A 1 402 ILE 402 939  939  ILE ILE A . n 
A 1 403 LEU 403 940  940  LEU LEU A . n 
A 1 404 LYS 404 941  941  LYS LYS A . n 
A 1 405 THR 405 942  942  THR THR A . n 
A 1 406 GLU 406 943  943  GLU GLU A . n 
A 1 407 GLU 407 944  944  GLU GLU A . n 
A 1 408 GLY 408 945  945  GLY GLY A . n 
A 1 409 ASN 409 946  946  ASN ASN A . n 
A 1 410 ASN 410 947  947  ASN ASN A . n 
A 1 411 ASP 411 948  948  ASP ASP A . n 
A 1 412 PHE 412 949  949  PHE PHE A . n 
A 1 413 LEU 413 950  950  LEU LEU A . n 
A 1 414 LYS 414 951  951  LYS LYS A . n 
A 1 415 LYS 415 952  952  LYS LYS A . n 
A 1 416 LYS 416 953  953  LYS LYS A . n 
A 1 417 GLY 417 954  954  GLY GLY A . n 
A 1 418 LYS 418 955  955  LYS LYS A . n 
A 1 419 ASP 419 956  956  ASP ASP A . n 
A 1 420 LEU 420 957  957  LEU LEU A . n 
A 1 421 ILE 421 958  958  ILE ILE A . n 
A 1 422 ASN 422 959  959  ASN ASN A . n 
A 1 423 PHE 423 960  960  PHE PHE A . n 
A 1 424 SER 424 961  961  SER SER A . n 
A 1 425 LYS 425 962  962  LYS LYS A . n 
A 1 426 ARG 426 963  963  ARG ARG A . n 
A 1 427 ARG 427 964  964  ARG ARG A . n 
A 1 428 LYS 428 965  965  LYS LYS A . n 
A 1 429 VAL 429 966  966  VAL VAL A . n 
A 1 430 ALA 430 967  967  ALA ALA A . n 
A 1 431 GLU 431 968  968  GLU GLU A . n 
A 1 432 ILE 432 969  969  ILE ILE A . n 
A 1 433 THR 433 970  970  THR THR A . n 
A 1 434 GLY 434 971  971  GLY GLY A . n 
A 1 435 GLU 435 972  972  GLU GLU A . n 
A 1 436 ILE 436 973  973  ILE ILE A . n 
A 1 437 GLN 437 974  974  GLN GLN A . n 
A 1 438 GLN 438 975  975  GLN GLN A . n 
A 1 439 TYR 439 976  976  TYR TYR A . n 
A 1 440 GLN 440 977  977  GLN GLN A . n 
A 1 441 ASN 441 978  978  ASN ASN A . n 
A 1 442 GLN 442 979  979  GLN GLN A . n 
A 1 443 PRO 443 980  980  PRO PRO A . n 
A 1 444 TYR 444 981  981  TYR TYR A . n 
A 1 445 CYS 445 982  982  CYS CYS A . n 
A 1 446 LEU 446 983  983  LEU LEU A . n 
A 1 447 ARG 447 984  984  ARG ARG A . n 
A 1 448 ILE 448 985  985  ILE ILE A . n 
A 1 449 GLU 449 986  986  GLU GLU A . n 
A 1 450 PRO 450 987  987  PRO PRO A . n 
A 1 451 ASP 451 988  988  ASP ASP A . n 
A 1 452 MET 452 989  989  MET MET A . n 
A 1 453 ARG 453 990  990  ARG ARG A . n 
A 1 454 ARG 454 991  991  ARG ARG A . n 
A 1 455 PHE 455 992  992  PHE PHE A . n 
A 1 456 PHE 456 993  993  PHE PHE A . n 
A 1 457 GLU 457 994  994  GLU GLU A . n 
A 1 458 ASN 458 995  995  ASN ASN A . n 
A 1 459 LEU 459 996  996  LEU LEU A . n 
A 1 460 ASN 460 997  997  ASN ASN A . n 
A 1 461 PRO 461 998  998  PRO PRO A . n 
A 1 462 MET 462 999  999  MET MET A . n 
A 1 463 GLY 463 1000 1000 GLY GLY A . n 
A 1 464 SER 464 1001 1001 SER SER A . n 
A 1 465 ALA 465 1002 1002 ALA ALA A . n 
A 1 466 SER 466 1003 1003 SER SER A . n 
A 1 467 GLU 467 1004 1004 GLU GLU A . n 
A 1 468 LYS 468 1005 1005 LYS LYS A . n 
A 1 469 GLU 469 1006 1006 GLU GLU A . n 
A 1 470 PHE 470 1007 1007 PHE PHE A . n 
A 1 471 THR 471 1008 1008 THR THR A . n 
A 1 472 ASP 472 1009 1009 ASP ASP A . n 
A 1 473 TYR 473 1010 1010 TYR TYR A . n 
A 1 474 LEU 474 1011 1011 LEU LEU A . n 
A 1 475 PHE 475 1012 1012 PHE PHE A . n 
A 1 476 ASN 476 1013 1013 ASN ASN A . n 
A 1 477 LYS 477 1014 1014 LYS LYS A . n 
A 1 478 SER 478 1015 1015 SER SER A . n 
A 1 479 LEU 479 1016 1016 LEU LEU A . n 
A 1 480 GLU 480 1017 1017 GLU GLU A . n 
A 1 481 ILE 481 1018 1018 ILE ILE A . n 
A 1 482 GLU 482 1019 1019 GLU GLU A . n 
A 1 483 PRO 483 1020 1020 PRO PRO A . n 
A 1 484 ARG 484 1021 1021 ARG ARG A . n 
A 1 485 ASN 485 1022 1022 ASN ASN A . n 
A 1 486 CYS 486 1023 1023 CYS CYS A . n 
A 1 487 LYS 487 1024 1024 LYS LYS A . n 
A 1 488 GLN 488 1025 1025 GLN GLN A . n 
A 1 489 PRO 489 1026 1026 PRO PRO A . n 
A 1 490 PRO 490 1027 1027 PRO PRO A . n 
A 1 491 ARG 491 1028 1028 ARG ARG A . n 
A 1 492 PHE 492 1029 1029 PHE PHE A . n 
A 1 493 PRO 493 1030 1030 PRO PRO A . n 
A 1 494 ARG 494 1031 1031 ARG ARG A . n 
A 1 495 LYS 495 1032 1032 LYS LYS A . n 
A 1 496 SER 496 1033 1033 SER SER A . n 
A 1 497 THR 497 1034 1034 THR THR A . n 
A 1 498 PHE 498 1035 1035 PHE PHE A . n 
A 1 499 SER 499 1036 1036 SER SER A . n 
A 1 500 LEU 500 1037 1037 LEU LEU A . n 
A 1 501 LYS 501 1038 1038 LYS LYS A . n 
A 1 502 SER 502 1039 1039 SER SER A . n 
A 1 503 PRO 503 1040 1040 PRO PRO A . n 
A 1 504 GLY 504 1041 1041 GLY GLY A . n 
A 1 505 ILE 505 1042 1042 ILE ILE A . n 
A 1 506 ARG 506 1043 1043 ARG ARG A . n 
A 1 507 PRO 507 1044 1044 PRO PRO A . n 
A 1 508 ASN 508 1045 1045 ASN ASN A . n 
A 1 509 THR 509 1046 ?    ?   ?   A . n 
A 1 510 GLY 510 1047 ?    ?   ?   A . n 
A 1 511 ARG 511 1048 ?    ?   ?   A . n 
A 1 512 HIS 512 1049 ?    ?   ?   A . n 
A 1 513 GLY 513 1050 ?    ?   ?   A . n 
A 1 514 SER 514 1051 ?    ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ASY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ASY 
_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 A1ASY 1   1101 1101 A1ASY LIG A . 
C 3 HOH   1   1201 224  HOH   HOH A . 
C 3 HOH   2   1202 3    HOH   HOH A . 
C 3 HOH   3   1203 163  HOH   HOH A . 
C 3 HOH   4   1204 226  HOH   HOH A . 
C 3 HOH   5   1205 225  HOH   HOH A . 
C 3 HOH   6   1206 246  HOH   HOH A . 
C 3 HOH   7   1207 54   HOH   HOH A . 
C 3 HOH   8   1208 235  HOH   HOH A . 
C 3 HOH   9   1209 177  HOH   HOH A . 
C 3 HOH   10  1210 221  HOH   HOH A . 
C 3 HOH   11  1211 45   HOH   HOH A . 
C 3 HOH   12  1212 229  HOH   HOH A . 
C 3 HOH   13  1213 197  HOH   HOH A . 
C 3 HOH   14  1214 81   HOH   HOH A . 
C 3 HOH   15  1215 13   HOH   HOH A . 
C 3 HOH   16  1216 7    HOH   HOH A . 
C 3 HOH   17  1217 193  HOH   HOH A . 
C 3 HOH   18  1218 114  HOH   HOH A . 
C 3 HOH   19  1219 179  HOH   HOH A . 
C 3 HOH   20  1220 157  HOH   HOH A . 
C 3 HOH   21  1221 100  HOH   HOH A . 
C 3 HOH   22  1222 208  HOH   HOH A . 
C 3 HOH   23  1223 201  HOH   HOH A . 
C 3 HOH   24  1224 148  HOH   HOH A . 
C 3 HOH   25  1225 22   HOH   HOH A . 
C 3 HOH   26  1226 39   HOH   HOH A . 
C 3 HOH   27  1227 243  HOH   HOH A . 
C 3 HOH   28  1228 36   HOH   HOH A . 
C 3 HOH   29  1229 136  HOH   HOH A . 
C 3 HOH   30  1230 222  HOH   HOH A . 
C 3 HOH   31  1231 194  HOH   HOH A . 
C 3 HOH   32  1232 59   HOH   HOH A . 
C 3 HOH   33  1233 145  HOH   HOH A . 
C 3 HOH   34  1234 126  HOH   HOH A . 
C 3 HOH   35  1235 116  HOH   HOH A . 
C 3 HOH   36  1236 20   HOH   HOH A . 
C 3 HOH   37  1237 83   HOH   HOH A . 
C 3 HOH   38  1238 52   HOH   HOH A . 
C 3 HOH   39  1239 84   HOH   HOH A . 
C 3 HOH   40  1240 51   HOH   HOH A . 
C 3 HOH   41  1241 5    HOH   HOH A . 
C 3 HOH   42  1242 168  HOH   HOH A . 
C 3 HOH   43  1243 79   HOH   HOH A . 
C 3 HOH   44  1244 14   HOH   HOH A . 
C 3 HOH   45  1245 213  HOH   HOH A . 
C 3 HOH   46  1246 73   HOH   HOH A . 
C 3 HOH   47  1247 122  HOH   HOH A . 
C 3 HOH   48  1248 206  HOH   HOH A . 
C 3 HOH   49  1249 70   HOH   HOH A . 
C 3 HOH   50  1250 16   HOH   HOH A . 
C 3 HOH   51  1251 139  HOH   HOH A . 
C 3 HOH   52  1252 241  HOH   HOH A . 
C 3 HOH   53  1253 150  HOH   HOH A . 
C 3 HOH   54  1254 217  HOH   HOH A . 
C 3 HOH   55  1255 2    HOH   HOH A . 
C 3 HOH   56  1256 75   HOH   HOH A . 
C 3 HOH   57  1257 27   HOH   HOH A . 
C 3 HOH   58  1258 195  HOH   HOH A . 
C 3 HOH   59  1259 40   HOH   HOH A . 
C 3 HOH   60  1260 72   HOH   HOH A . 
C 3 HOH   61  1261 9    HOH   HOH A . 
C 3 HOH   62  1262 152  HOH   HOH A . 
C 3 HOH   63  1263 140  HOH   HOH A . 
C 3 HOH   64  1264 24   HOH   HOH A . 
C 3 HOH   65  1265 25   HOH   HOH A . 
C 3 HOH   66  1266 219  HOH   HOH A . 
C 3 HOH   67  1267 92   HOH   HOH A . 
C 3 HOH   68  1268 4    HOH   HOH A . 
C 3 HOH   69  1269 216  HOH   HOH A . 
C 3 HOH   70  1270 191  HOH   HOH A . 
C 3 HOH   71  1271 91   HOH   HOH A . 
C 3 HOH   72  1272 103  HOH   HOH A . 
C 3 HOH   73  1273 64   HOH   HOH A . 
C 3 HOH   74  1274 35   HOH   HOH A . 
C 3 HOH   75  1275 203  HOH   HOH A . 
C 3 HOH   76  1276 65   HOH   HOH A . 
C 3 HOH   77  1277 253  HOH   HOH A . 
C 3 HOH   78  1278 143  HOH   HOH A . 
C 3 HOH   79  1279 123  HOH   HOH A . 
C 3 HOH   80  1280 99   HOH   HOH A . 
C 3 HOH   81  1281 204  HOH   HOH A . 
C 3 HOH   82  1282 248  HOH   HOH A . 
C 3 HOH   83  1283 205  HOH   HOH A . 
C 3 HOH   84  1284 56   HOH   HOH A . 
C 3 HOH   85  1285 33   HOH   HOH A . 
C 3 HOH   86  1286 141  HOH   HOH A . 
C 3 HOH   87  1287 17   HOH   HOH A . 
C 3 HOH   88  1288 47   HOH   HOH A . 
C 3 HOH   89  1289 66   HOH   HOH A . 
C 3 HOH   90  1290 124  HOH   HOH A . 
C 3 HOH   91  1291 37   HOH   HOH A . 
C 3 HOH   92  1292 176  HOH   HOH A . 
C 3 HOH   93  1293 223  HOH   HOH A . 
C 3 HOH   94  1294 158  HOH   HOH A . 
C 3 HOH   95  1295 142  HOH   HOH A . 
C 3 HOH   96  1296 252  HOH   HOH A . 
C 3 HOH   97  1297 29   HOH   HOH A . 
C 3 HOH   98  1298 164  HOH   HOH A . 
C 3 HOH   99  1299 41   HOH   HOH A . 
C 3 HOH   100 1300 95   HOH   HOH A . 
C 3 HOH   101 1301 53   HOH   HOH A . 
C 3 HOH   102 1302 18   HOH   HOH A . 
C 3 HOH   103 1303 239  HOH   HOH A . 
C 3 HOH   104 1304 88   HOH   HOH A . 
C 3 HOH   105 1305 162  HOH   HOH A . 
C 3 HOH   106 1306 58   HOH   HOH A . 
C 3 HOH   107 1307 49   HOH   HOH A . 
C 3 HOH   108 1308 106  HOH   HOH A . 
C 3 HOH   109 1309 117  HOH   HOH A . 
C 3 HOH   110 1310 146  HOH   HOH A . 
C 3 HOH   111 1311 71   HOH   HOH A . 
C 3 HOH   112 1312 78   HOH   HOH A . 
C 3 HOH   113 1313 178  HOH   HOH A . 
C 3 HOH   114 1314 120  HOH   HOH A . 
C 3 HOH   115 1315 8    HOH   HOH A . 
C 3 HOH   116 1316 172  HOH   HOH A . 
C 3 HOH   117 1317 94   HOH   HOH A . 
C 3 HOH   118 1318 12   HOH   HOH A . 
C 3 HOH   119 1319 151  HOH   HOH A . 
C 3 HOH   120 1320 200  HOH   HOH A . 
C 3 HOH   121 1321 153  HOH   HOH A . 
C 3 HOH   122 1322 173  HOH   HOH A . 
C 3 HOH   123 1323 30   HOH   HOH A . 
C 3 HOH   124 1324 44   HOH   HOH A . 
C 3 HOH   125 1325 184  HOH   HOH A . 
C 3 HOH   126 1326 42   HOH   HOH A . 
C 3 HOH   127 1327 6    HOH   HOH A . 
C 3 HOH   128 1328 110  HOH   HOH A . 
C 3 HOH   129 1329 209  HOH   HOH A . 
C 3 HOH   130 1330 86   HOH   HOH A . 
C 3 HOH   131 1331 85   HOH   HOH A . 
C 3 HOH   132 1332 96   HOH   HOH A . 
C 3 HOH   133 1333 169  HOH   HOH A . 
C 3 HOH   134 1334 46   HOH   HOH A . 
C 3 HOH   135 1335 190  HOH   HOH A . 
C 3 HOH   136 1336 192  HOH   HOH A . 
C 3 HOH   137 1337 102  HOH   HOH A . 
C 3 HOH   138 1338 138  HOH   HOH A . 
C 3 HOH   139 1339 189  HOH   HOH A . 
C 3 HOH   140 1340 154  HOH   HOH A . 
C 3 HOH   141 1341 26   HOH   HOH A . 
C 3 HOH   142 1342 1    HOH   HOH A . 
C 3 HOH   143 1343 149  HOH   HOH A . 
C 3 HOH   144 1344 238  HOH   HOH A . 
C 3 HOH   145 1345 77   HOH   HOH A . 
C 3 HOH   146 1346 82   HOH   HOH A . 
C 3 HOH   147 1347 62   HOH   HOH A . 
C 3 HOH   148 1348 127  HOH   HOH A . 
C 3 HOH   149 1349 11   HOH   HOH A . 
C 3 HOH   150 1350 48   HOH   HOH A . 
C 3 HOH   151 1351 215  HOH   HOH A . 
C 3 HOH   152 1352 133  HOH   HOH A . 
C 3 HOH   153 1353 19   HOH   HOH A . 
C 3 HOH   154 1354 97   HOH   HOH A . 
C 3 HOH   155 1355 160  HOH   HOH A . 
C 3 HOH   156 1356 68   HOH   HOH A . 
C 3 HOH   157 1357 212  HOH   HOH A . 
C 3 HOH   158 1358 23   HOH   HOH A . 
C 3 HOH   159 1359 10   HOH   HOH A . 
C 3 HOH   160 1360 166  HOH   HOH A . 
C 3 HOH   161 1361 55   HOH   HOH A . 
C 3 HOH   162 1362 43   HOH   HOH A . 
C 3 HOH   163 1363 254  HOH   HOH A . 
C 3 HOH   164 1364 128  HOH   HOH A . 
C 3 HOH   165 1365 21   HOH   HOH A . 
C 3 HOH   166 1366 129  HOH   HOH A . 
C 3 HOH   167 1367 60   HOH   HOH A . 
C 3 HOH   168 1368 69   HOH   HOH A . 
C 3 HOH   169 1369 109  HOH   HOH A . 
C 3 HOH   170 1370 34   HOH   HOH A . 
C 3 HOH   171 1371 188  HOH   HOH A . 
C 3 HOH   172 1372 93   HOH   HOH A . 
C 3 HOH   173 1373 181  HOH   HOH A . 
C 3 HOH   174 1374 119  HOH   HOH A . 
C 3 HOH   175 1375 255  HOH   HOH A . 
C 3 HOH   176 1376 90   HOH   HOH A . 
C 3 HOH   177 1377 170  HOH   HOH A . 
C 3 HOH   178 1378 220  HOH   HOH A . 
C 3 HOH   179 1379 242  HOH   HOH A . 
C 3 HOH   180 1380 137  HOH   HOH A . 
C 3 HOH   181 1381 67   HOH   HOH A . 
C 3 HOH   182 1382 80   HOH   HOH A . 
C 3 HOH   183 1383 101  HOH   HOH A . 
C 3 HOH   184 1384 87   HOH   HOH A . 
C 3 HOH   185 1385 210  HOH   HOH A . 
C 3 HOH   186 1386 115  HOH   HOH A . 
C 3 HOH   187 1387 156  HOH   HOH A . 
C 3 HOH   188 1388 104  HOH   HOH A . 
C 3 HOH   189 1389 31   HOH   HOH A . 
C 3 HOH   190 1390 232  HOH   HOH A . 
C 3 HOH   191 1391 230  HOH   HOH A . 
C 3 HOH   192 1392 112  HOH   HOH A . 
C 3 HOH   193 1393 236  HOH   HOH A . 
C 3 HOH   194 1394 198  HOH   HOH A . 
C 3 HOH   195 1395 134  HOH   HOH A . 
C 3 HOH   196 1396 244  HOH   HOH A . 
C 3 HOH   197 1397 182  HOH   HOH A . 
C 3 HOH   198 1398 245  HOH   HOH A . 
C 3 HOH   199 1399 32   HOH   HOH A . 
C 3 HOH   200 1400 237  HOH   HOH A . 
C 3 HOH   201 1401 247  HOH   HOH A . 
C 3 HOH   202 1402 196  HOH   HOH A . 
C 3 HOH   203 1403 50   HOH   HOH A . 
C 3 HOH   204 1404 118  HOH   HOH A . 
C 3 HOH   205 1405 233  HOH   HOH A . 
C 3 HOH   206 1406 105  HOH   HOH A . 
C 3 HOH   207 1407 57   HOH   HOH A . 
C 3 HOH   208 1408 38   HOH   HOH A . 
C 3 HOH   209 1409 231  HOH   HOH A . 
C 3 HOH   210 1410 15   HOH   HOH A . 
C 3 HOH   211 1411 113  HOH   HOH A . 
C 3 HOH   212 1412 63   HOH   HOH A . 
C 3 HOH   213 1413 207  HOH   HOH A . 
C 3 HOH   214 1414 76   HOH   HOH A . 
C 3 HOH   215 1415 98   HOH   HOH A . 
C 3 HOH   216 1416 250  HOH   HOH A . 
C 3 HOH   217 1417 121  HOH   HOH A . 
C 3 HOH   218 1418 187  HOH   HOH A . 
C 3 HOH   219 1419 186  HOH   HOH A . 
C 3 HOH   220 1420 111  HOH   HOH A . 
C 3 HOH   221 1421 214  HOH   HOH A . 
C 3 HOH   222 1422 74   HOH   HOH A . 
C 3 HOH   223 1423 202  HOH   HOH A . 
C 3 HOH   224 1424 185  HOH   HOH A . 
C 3 HOH   225 1425 144  HOH   HOH A . 
C 3 HOH   226 1426 159  HOH   HOH A . 
C 3 HOH   227 1427 28   HOH   HOH A . 
C 3 HOH   228 1428 174  HOH   HOH A . 
C 3 HOH   229 1429 125  HOH   HOH A . 
C 3 HOH   230 1430 155  HOH   HOH A . 
C 3 HOH   231 1431 240  HOH   HOH A . 
C 3 HOH   232 1432 147  HOH   HOH A . 
C 3 HOH   233 1433 167  HOH   HOH A . 
C 3 HOH   234 1434 199  HOH   HOH A . 
C 3 HOH   235 1435 171  HOH   HOH A . 
C 3 HOH   236 1436 251  HOH   HOH A . 
C 3 HOH   237 1437 165  HOH   HOH A . 
C 3 HOH   238 1438 132  HOH   HOH A . 
C 3 HOH   239 1439 61   HOH   HOH A . 
C 3 HOH   240 1440 175  HOH   HOH A . 
C 3 HOH   241 1441 183  HOH   HOH A . 
C 3 HOH   242 1442 108  HOH   HOH A . 
C 3 HOH   243 1443 89   HOH   HOH A . 
C 3 HOH   244 1444 218  HOH   HOH A . 
C 3 HOH   245 1445 161  HOH   HOH A . 
C 3 HOH   246 1446 234  HOH   HOH A . 
C 3 HOH   247 1447 249  HOH   HOH A . 
C 3 HOH   248 1448 135  HOH   HOH A . 
C 3 HOH   249 1449 211  HOH   HOH A . 
C 3 HOH   250 1450 130  HOH   HOH A . 
C 3 HOH   251 1451 131  HOH   HOH A . 
C 3 HOH   252 1452 107  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 ? ? ? '(1.15.2_3472: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .                    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                     9BVE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.234 
_cell.length_a_esd                 ? 
_cell.length_b                     86.349 
_cell.length_b_esd                 ? 
_cell.length_c                     106.587 
_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                         9BVE 
_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                   9BVE 
_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             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.66 
_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                                       9BVE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.83 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     28277 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.099 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_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                        ? 
# 
_reflns_shell.d_res_high                                    1.83 
_reflns_shell.d_res_low                                     1.86 
_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                             2621 
_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                               1.9 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.66 
_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               ? 
# 
_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                                 9BVE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.400 
_refine.ls_d_res_low                             17.939 
_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                     22815 
_refine.ls_number_reflns_R_free                  1143 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.99 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2565 
_refine.ls_R_factor_R_free                       0.3053 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2540 
_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                 32.44 
_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                            0.38 
_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        3912 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             255 
_refine_hist.number_atoms_total               4196 
_refine_hist.d_res_high                       2.400 
_refine_hist.d_res_low                        17.939 
# 
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' ? 0.004  ? 4084 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.608  ? 5524 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.137 ? 2535 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.040  ? 596  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 713  ? 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' 2.4000 2.5090  . . 129 2449 89.00 . . . . 0.3227 . . . . . . . . . . . 0.3727 
'X-RAY DIFFRACTION' 2.5090 2.6408  . . 142 2698 97.00 . . . . 0.3187 . . . . . . . . . . . 0.3866 
'X-RAY DIFFRACTION' 2.6408 2.8057  . . 143 2702 97.00 . . . . 0.3112 . . . . . . . . . . . 0.3473 
'X-RAY DIFFRACTION' 2.8057 3.0214  . . 145 2745 99.00 . . . . 0.3072 . . . . . . . . . . . 0.3641 
'X-RAY DIFFRACTION' 3.0214 3.3237  . . 144 2741 98.00 . . . . 0.3104 . . . . . . . . . . . 0.3450 
'X-RAY DIFFRACTION' 3.3237 3.8007  . . 138 2641 93.00 . . . . 0.2778 . . . . . . . . . . . 0.2978 
'X-RAY DIFFRACTION' 3.8007 4.7735  . . 145 2758 97.00 . . . . 0.2054 . . . . . . . . . . . 0.2760 
'X-RAY DIFFRACTION' 4.7735 17.9390 . . 157 2938 99.00 . . . . 0.1813 . . . . . . . . . . . 0.2404 
# 
_struct.entry_id                     9BVE 
_struct.title                        'Identification of multiple ligand hotspots on SOS2, compound 9' 
_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        9BVE 
_struct_keywords.text            
;small molecule complex crystal structure, SOS2, guanosine nucleotide exchange factor, RAS-activator, SIGNALING PROTEIN, oncogenes, inhibitor of SOS-mediated guanosine nucleotide exchange
;
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SOS2_HUMAN 
_struct_ref.pdbx_db_accession          Q07890 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EQPLRLPSPEVYRFVVKDSEENIVFEDNLQSRSGIPIIKGGTVVKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSL
LIERFEIPEPEPTDADKLAIEKGEQPISADLKRFRKEYVQPVQLRILNVFRHWVEHHFYDFERDLELLERLESFISSVRG
KAMKKWVESIAKIIRRKKQAQANGVSHNITFESPPPPIEWHISKPGQFETFDLMTLHPIEIARQLTLLESDLYRKVQPSE
LVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVEAENFEERVAVLSRIIEILQVFQDLNNFNGVLEIVSAVNSVSV
YRLDHTFEALQERKRKILDEAVELSQDHFKKYLVKLKSINPPCVPFFGIYLTNILKTEEGNNDFLKKKGKDLINFSKRRK
VAEITGEIQQYQNQPYCLRIEPDMRRFFENLNPMGSASEKEFTDYLFNKSLEIEPRNCKQPPRFPRKSTFSLKSPGIRPN
TGRHGS
;
_struct_ref.pdbx_align_begin           562 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BVE 
_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 9BVE MET A 1  ? UNP Q07890 ? ? 'expression tag' -28 1  
1 9BVE SER A 2  ? UNP Q07890 ? ? 'expression tag' -27 2  
1 9BVE TYR A 3  ? UNP Q07890 ? ? 'expression tag' -26 3  
1 9BVE TYR A 4  ? UNP Q07890 ? ? 'expression tag' -25 4  
1 9BVE HIS A 5  ? UNP Q07890 ? ? 'expression tag' -24 5  
1 9BVE HIS A 6  ? UNP Q07890 ? ? 'expression tag' -23 6  
1 9BVE HIS A 7  ? UNP Q07890 ? ? 'expression tag' -22 7  
1 9BVE HIS A 8  ? UNP Q07890 ? ? 'expression tag' -21 8  
1 9BVE HIS A 9  ? UNP Q07890 ? ? 'expression tag' -20 9  
1 9BVE HIS A 10 ? UNP Q07890 ? ? 'expression tag' -19 10 
1 9BVE LEU A 11 ? UNP Q07890 ? ? 'expression tag' -18 11 
1 9BVE GLU A 12 ? UNP Q07890 ? ? 'expression tag' -17 12 
1 9BVE SER A 13 ? UNP Q07890 ? ? 'expression tag' -16 13 
1 9BVE THR A 14 ? UNP Q07890 ? ? 'expression tag' -15 14 
1 9BVE SER A 15 ? UNP Q07890 ? ? 'expression tag' -14 15 
1 9BVE LEU A 16 ? UNP Q07890 ? ? 'expression tag' -13 16 
1 9BVE TYR A 17 ? UNP Q07890 ? ? 'expression tag' -12 17 
1 9BVE LYS A 18 ? UNP Q07890 ? ? 'expression tag' -11 18 
1 9BVE LYS A 19 ? UNP Q07890 ? ? 'expression tag' -10 19 
1 9BVE ALA A 20 ? UNP Q07890 ? ? 'expression tag' -9  20 
1 9BVE GLY A 21 ? UNP Q07890 ? ? 'expression tag' -8  21 
1 9BVE PHE A 22 ? UNP Q07890 ? ? 'expression tag' -7  22 
1 9BVE GLU A 23 ? UNP Q07890 ? ? 'expression tag' -6  23 
1 9BVE ASN A 24 ? UNP Q07890 ? ? 'expression tag' -5  24 
1 9BVE LEU A 25 ? UNP Q07890 ? ? 'expression tag' -4  25 
1 9BVE TYR A 26 ? UNP Q07890 ? ? 'expression tag' -3  26 
1 9BVE PHE A 27 ? UNP Q07890 ? ? 'expression tag' -2  27 
1 9BVE GLN A 28 ? UNP Q07890 ? ? 'expression tag' -1  28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  25700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TYR A 40  ? VAL A 44  ? TYR A 577  VAL A 581  5 ? 5  
HELX_P HELX_P2  AA2 THR A 70  ? THR A 79  ? THR A 607  THR A 616  1 ? 10 
HELX_P HELX_P3  AA3 ASP A 85  ? TYR A 96  ? ASP A 622  TYR A 633  1 ? 12 
HELX_P HELX_P4  AA4 ARG A 97  ? PHE A 99  ? ARG A 634  PHE A 636  5 ? 3  
HELX_P HELX_P5  AA5 LYS A 101 ? GLU A 114 ? LYS A 638  GLU A 651  1 ? 14 
HELX_P HELX_P6  AA6 THR A 121 ? GLY A 131 ? THR A 658  GLY A 668  1 ? 11 
HELX_P HELX_P7  AA7 SER A 136 ? TYR A 146 ? SER A 673  TYR A 683  1 ? 11 
HELX_P HELX_P8  AA8 TYR A 146 ? HIS A 165 ? TYR A 683  HIS A 702  1 ? 20 
HELX_P HELX_P9  AA9 PHE A 166 ? ASP A 172 ? PHE A 703  ASP A 709  1 ? 7  
HELX_P HELX_P10 AB1 ASP A 172 ? SER A 184 ? ASP A 709  SER A 721  1 ? 13 
HELX_P HELX_P11 AB2 GLY A 188 ? ALA A 208 ? GLY A 725  ALA A 745  1 ? 21 
HELX_P HELX_P12 AB3 GLN A 235 ? PHE A 239 ? GLN A 772  PHE A 776  5 ? 5  
HELX_P HELX_P13 AB4 HIS A 245 ? LYS A 263 ? HIS A 782  LYS A 800  1 ? 19 
HELX_P HELX_P14 AB5 GLN A 265 ? LYS A 276 ? GLN A 802  LYS A 813  5 ? 12 
HELX_P HELX_P15 AB6 ASP A 278 ? SER A 283 ? ASP A 815  SER A 820  1 ? 6  
HELX_P HELX_P16 AB7 SER A 283 ? GLU A 306 ? SER A 820  GLU A 843  1 ? 24 
HELX_P HELX_P17 AB8 ASN A 309 ? LEU A 330 ? ASN A 846  LEU A 867  1 ? 22 
HELX_P HELX_P18 AB9 ASN A 332 ? SER A 345 ? ASN A 869  SER A 882  1 ? 14 
HELX_P HELX_P19 AC1 SER A 345 ? ARG A 350 ? SER A 882  ARG A 887  1 ? 6  
HELX_P HELX_P20 AC2 LEU A 351 ? LEU A 358 ? LEU A 888  LEU A 895  1 ? 8  
HELX_P HELX_P21 AC3 GLN A 359 ? SER A 373 ? GLN A 896  SER A 910  1 ? 15 
HELX_P HELX_P22 AC4 SER A 373 ? LYS A 385 ? SER A 910  LYS A 922  1 ? 13 
HELX_P HELX_P23 AC5 PHE A 395 ? ASN A 409 ? PHE A 932  ASN A 946  1 ? 15 
HELX_P HELX_P24 AC6 PHE A 423 ? GLN A 438 ? PHE A 960  GLN A 975  1 ? 16 
HELX_P HELX_P25 AC7 GLU A 449 ? ASN A 458 ? GLU A 986  ASN A 995  1 ? 10 
HELX_P HELX_P26 AC8 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       -3.45 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   4 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 51  ? PHE A 53  ? ILE A 588 PHE A 590 
AA1 2 ILE A 66  ? GLY A 69  ? ILE A 603 GLY A 606 
AA1 3 LEU A 420 ? ASN A 422 ? LEU A 957 ASN A 959 
AA1 4 PHE A 412 ? LEU A 413 ? PHE A 949 LEU A 950 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 52  ? N VAL A 589 O GLY A 68  ? O GLY A 605 
AA1 2 3 N GLY A 69  ? N GLY A 606 O ILE A 421 ? O ILE A 958 
AA1 3 4 O LEU A 420 ? O LEU A 957 N LEU A 413 ? N LEU A 950 
# 
_pdbx_entry_details.entry_id                   9BVE 
_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 O   A HOH 1441 ? ? O A HOH 1447 ? ? 2.00 
2  1 O   A LYS 951  ? ? O A HOH 1201 ? ? 2.00 
3  1 O   A HOH 1304 ? ? O A HOH 1421 ? ? 2.05 
4  1 O   A LEU 781  ? ? O A HOH 1202 ? ? 2.05 
5  1 OE1 A GLU 905  ? ? O A HOH 1203 ? ? 2.06 
6  1 ND2 A ASN 1022 ? ? O A HOH 1204 ? ? 2.08 
7  1 O   A HOH 1405 ? ? O A HOH 1420 ? ? 2.10 
8  1 OE1 A GLU 908  ? ? O A HOH 1205 ? ? 2.11 
9  1 O   A HOH 1380 ? ? O A HOH 1421 ? ? 2.12 
10 1 OH  A TYR 1010 ? ? O A HOH 1206 ? ? 2.14 
11 1 OE2 A GLU 849  ? ? O A HOH 1207 ? ? 2.14 
12 1 OD1 A ASN 997  ? ? O A HOH 1208 ? ? 2.15 
13 1 NZ  A LYS 681  ? ? O A HOH 1209 ? ? 2.15 
14 1 OE1 A GLU 943  ? ? O A HOH 1210 ? ? 2.15 
15 1 OE1 A GLU 654  ? ? O A HOH 1211 ? ? 2.16 
16 1 O   A HOH 1262 ? ? O A HOH 1333 ? ? 2.16 
# 
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 TYR A 683 ? ? -127.41 -62.26  
2 1 HIS A 766 ? ? -109.39 -106.19 
3 1 ASP A 815 ? ? -95.45  44.74   
4 1 CYS A 982 ? ? -91.78  58.75   
# 
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 -17.6463 -16.0572 -27.5865 0.2682 ? 0.0315  ? -0.0419 ? 0.3901 ? -0.0331 ? 0.2811 ? 0.2120 ? 
0.1233  ? 0.5915  ? 1.1642 ? 0.7486  ? 1.3882 ? -0.0013 ? 0.0877  ? -0.0275 ? -0.3226 ? -0.1428 ? 0.1215  ? -0.0222 ? 0.0506  ? 
0.1592  ? 
2 'X-RAY DIFFRACTION' ? refined -21.8107 -17.0962 -15.6277 0.2476 ? 0.0133  ? 0.0217  ? 0.2124 ? -0.0233 ? 0.2081 ? 1.6490 ? 
0.5312  ? 0.2736  ? 2.3173 ? 0.2864  ? 2.5589 ? 0.0794  ? -0.0856 ? 0.0136  ? 0.0019  ? -0.1487 ? 0.1468  ? 0.2757  ? -0.2622 ? 
0.0067  ? 
3 'X-RAY DIFFRACTION' ? refined -8.3809  -11.5282 0.2530   0.5374 ? -0.0623 ? 0.0373  ? 0.3087 ? 0.0229  ? 0.3341 ? 1.9033 ? 
0.1625  ? 0.9912  ? 0.3609 ? 0.2225  ? 0.2235 ? 0.2615  ? -0.3978 ? -0.3447 ? 0.6282  ? -0.2852 ? 0.1587  ? -0.0072 ? -0.1013 ? 
-0.0062 ? 
4 'X-RAY DIFFRACTION' ? refined 22.4243  8.3785   -4.6854  0.2061 ? 0.0064  ? 0.0134  ? 0.1748 ? -0.0204 ? 0.1873 ? 3.1894 ? 
1.3985  ? 0.2940  ? 2.2622 ? -0.2044 ? 0.8397 ? 0.0338  ? -0.0351 ? 0.0679  ? 0.1121  ? 0.0080  ? 0.0977  ? 0.0253  ? -0.0446 ? 
-0.0384 ? 
5 'X-RAY DIFFRACTION' ? refined 22.4328  0.1627   -18.0965 0.3762 ? 0.0153  ? 0.0236  ? 0.3101 ? -0.0303 ? 0.2545 ? 2.4277 ? 
0.3897  ? 0.3392  ? 1.9067 ? -0.3856 ? 1.2590 ? 0.0054  ? 0.7258  ? -0.0929 ? -0.1448 ? 0.1007  ? 0.0630  ? 0.4981  ? 0.0067  ? 
-0.0524 ? 
6 'X-RAY DIFFRACTION' ? refined -2.4681  -3.0923  -24.9248 0.3894 ? -0.0491 ? 0.0901  ? 0.4374 ? 0.0589  ? 0.3918 ? 2.7920 ? 
0.8320  ? 1.2293  ? 3.3431 ? 1.2384  ? 4.1249 ? 0.2670  ? 1.1442  ? 0.5605  ? -0.6408 ? -0.1237 ? -0.5789 ? -0.0569 ? 0.6372  ? 
-0.3332 ? 
7 'X-RAY DIFFRACTION' ? refined 17.4662  4.8470   2.7865   0.2725 ? -0.0281 ? -0.0085 ? 0.3818 ? -0.0041 ? 0.2929 ? 1.3816 ? 
-0.5322 ? -0.1941 ? 3.2182 ? 0.1729  ? 0.9522 ? 0.1547  ? 0.0391  ? -0.3961 ? 0.2068  ? -0.1629 ? 0.3654  ? 0.1105  ? -0.2018 ? 
0.0356  ? 
8 'X-RAY DIFFRACTION' ? refined 33.1191  21.3517  -5.1895  0.3455 ? -0.0857 ? 0.0694  ? 0.3451 ? 0.0517  ? 0.3324 ? 1.9033 ? 
-0.5515 ? 0.5742  ? 1.8595 ? 0.0642  ? 1.9459 ? 0.0759  ? -0.0874 ? 0.4400  ? -0.0108 ? -0.0809 ? -0.4185 ? -0.2764 ? -0.0436 ? 
0.0183  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid -4 through 622 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 623 through 701 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 702 through 762 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 763 through 896 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 897 through 945 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 946 through 976 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 977 through 1003 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1004 through 1045 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -28  ? A MET 1   
2  1 Y 1 A SER -27  ? A SER 2   
3  1 Y 1 A TYR -26  ? A TYR 3   
4  1 Y 1 A TYR -25  ? A TYR 4   
5  1 Y 1 A HIS -24  ? A HIS 5   
6  1 Y 1 A HIS -23  ? A HIS 6   
7  1 Y 1 A HIS -22  ? A HIS 7   
8  1 Y 1 A HIS -21  ? A HIS 8   
9  1 Y 1 A HIS -20  ? A HIS 9   
10 1 Y 1 A HIS -19  ? A HIS 10  
11 1 Y 1 A LEU -18  ? A LEU 11  
12 1 Y 1 A GLU -17  ? A GLU 12  
13 1 Y 1 A SER -16  ? A SER 13  
14 1 Y 1 A THR -15  ? A THR 14  
15 1 Y 1 A SER -14  ? A SER 15  
16 1 Y 1 A LEU -13  ? A LEU 16  
17 1 Y 1 A TYR -12  ? A TYR 17  
18 1 Y 1 A LYS -11  ? A LYS 18  
19 1 Y 1 A LYS -10  ? A LYS 19  
20 1 Y 1 A ALA -9   ? A ALA 20  
21 1 Y 1 A GLY -8   ? A GLY 21  
22 1 Y 1 A PHE -7   ? A PHE 22  
23 1 Y 1 A GLU -6   ? A GLU 23  
24 1 Y 1 A ASN -5   ? A ASN 24  
25 1 Y 1 A ASN 593  ? A ASN 56  
26 1 Y 1 A LEU 594  ? A LEU 57  
27 1 Y 1 A GLN 595  ? A GLN 58  
28 1 Y 1 A SER 596  ? A SER 59  
29 1 Y 1 A ARG 597  ? A ARG 60  
30 1 Y 1 A SER 598  ? A SER 61  
31 1 Y 1 A GLN 746  ? A GLN 209 
32 1 Y 1 A ALA 747  ? A ALA 210 
33 1 Y 1 A ASN 748  ? A ASN 211 
34 1 Y 1 A GLY 749  ? A GLY 212 
35 1 Y 1 A VAL 750  ? A VAL 213 
36 1 Y 1 A SER 751  ? A SER 214 
37 1 Y 1 A HIS 752  ? A HIS 215 
38 1 Y 1 A ASN 753  ? A ASN 216 
39 1 Y 1 A THR 1046 ? A THR 509 
40 1 Y 1 A GLY 1047 ? A GLY 510 
41 1 Y 1 A ARG 1048 ? A ARG 511 
42 1 Y 1 A HIS 1049 ? A HIS 512 
43 1 Y 1 A GLY 1050 ? A GLY 513 
44 1 Y 1 A SER 1051 ? A SER 514 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ASY N1   N N N 1   
A1ASY N3   N Y N 2   
A1ASY C4   C N N 3   
A1ASY C5   C N N 4   
A1ASY C6   C N N 5   
A1ASY C7   C N N 6   
A1ASY C8   C Y N 7   
A1ASY C10  C Y N 8   
A1ASY C13  C Y N 9   
A1ASY C15  C Y N 10  
A1ASY C17  C Y N 11  
A1ASY C20  C N N 12  
A1ASY C21  C N N 13  
A1ASY C22  C N N 14  
A1ASY C1   C N N 15  
A1ASY C11  C Y N 16  
A1ASY C12  C Y N 17  
A1ASY C14  C Y N 18  
A1ASY C16  C Y N 19  
A1ASY C18  C Y N 20  
A1ASY C19  C N N 21  
A1ASY C2   C N N 22  
A1ASY C23  C Y N 23  
A1ASY C3   C N N 24  
A1ASY C9   C Y N 25  
A1ASY N2   N N N 26  
A1ASY N4   N N N 27  
A1ASY N5   N Y N 28  
A1ASY N6   N Y N 29  
A1ASY H2   H N N 30  
A1ASY H3   H N N 31  
A1ASY H4   H N N 32  
A1ASY H5   H N N 33  
A1ASY H6   H N N 34  
A1ASY H7   H N N 35  
A1ASY H8   H N N 36  
A1ASY H9   H N N 37  
A1ASY H10  H N N 38  
A1ASY H11  H N N 39  
A1ASY H12  H N N 40  
A1ASY H13  H N N 41  
A1ASY H14  H N N 42  
A1ASY H15  H N N 43  
A1ASY H16  H N N 44  
A1ASY H17  H N N 45  
A1ASY H18  H N N 46  
A1ASY H19  H N N 47  
A1ASY H20  H N N 48  
A1ASY H21  H N N 49  
A1ASY H22  H N N 50  
A1ASY H23  H N N 51  
A1ASY H24  H N N 52  
A1ASY H25  H N N 53  
A1ASY H26  H N N 54  
A1ASY H27  H N N 55  
A1ASY H28  H N N 56  
A1ASY H29  H N N 57  
A1ASY H30  H N N 58  
A1ASY H31  H N N 59  
ALA   N    N N N 60  
ALA   CA   C N S 61  
ALA   C    C N N 62  
ALA   O    O N N 63  
ALA   CB   C N N 64  
ALA   OXT  O N N 65  
ALA   H    H N N 66  
ALA   H2   H N N 67  
ALA   HA   H N N 68  
ALA   HB1  H N N 69  
ALA   HB2  H N N 70  
ALA   HB3  H N N 71  
ALA   HXT  H N N 72  
ARG   N    N N N 73  
ARG   CA   C N S 74  
ARG   C    C N N 75  
ARG   O    O N N 76  
ARG   CB   C N N 77  
ARG   CG   C N N 78  
ARG   CD   C N N 79  
ARG   NE   N N N 80  
ARG   CZ   C N N 81  
ARG   NH1  N N N 82  
ARG   NH2  N N N 83  
ARG   OXT  O N N 84  
ARG   H    H N N 85  
ARG   H2   H N N 86  
ARG   HA   H N N 87  
ARG   HB2  H N N 88  
ARG   HB3  H N N 89  
ARG   HG2  H N N 90  
ARG   HG3  H N N 91  
ARG   HD2  H N N 92  
ARG   HD3  H N N 93  
ARG   HE   H N N 94  
ARG   HH11 H N N 95  
ARG   HH12 H N N 96  
ARG   HH21 H N N 97  
ARG   HH22 H N N 98  
ARG   HXT  H N N 99  
ASN   N    N N N 100 
ASN   CA   C N S 101 
ASN   C    C N N 102 
ASN   O    O N N 103 
ASN   CB   C N N 104 
ASN   CG   C N N 105 
ASN   OD1  O N N 106 
ASN   ND2  N N N 107 
ASN   OXT  O N N 108 
ASN   H    H N N 109 
ASN   H2   H N N 110 
ASN   HA   H N N 111 
ASN   HB2  H N N 112 
ASN   HB3  H N N 113 
ASN   HD21 H N N 114 
ASN   HD22 H N N 115 
ASN   HXT  H N N 116 
ASP   N    N N N 117 
ASP   CA   C N S 118 
ASP   C    C N N 119 
ASP   O    O N N 120 
ASP   CB   C N N 121 
ASP   CG   C N N 122 
ASP   OD1  O N N 123 
ASP   OD2  O N N 124 
ASP   OXT  O N N 125 
ASP   H    H N N 126 
ASP   H2   H N N 127 
ASP   HA   H N N 128 
ASP   HB2  H N N 129 
ASP   HB3  H N N 130 
ASP   HD2  H N N 131 
ASP   HXT  H N N 132 
CYS   N    N N N 133 
CYS   CA   C N R 134 
CYS   C    C N N 135 
CYS   O    O N N 136 
CYS   CB   C N N 137 
CYS   SG   S N N 138 
CYS   OXT  O N N 139 
CYS   H    H N N 140 
CYS   H2   H N N 141 
CYS   HA   H N N 142 
CYS   HB2  H N N 143 
CYS   HB3  H N N 144 
CYS   HG   H N N 145 
CYS   HXT  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 
THR   N    N N N 363 
THR   CA   C N S 364 
THR   C    C N N 365 
THR   O    O N N 366 
THR   CB   C N R 367 
THR   OG1  O N N 368 
THR   CG2  C N N 369 
THR   OXT  O N N 370 
THR   H    H N N 371 
THR   H2   H N N 372 
THR   HA   H N N 373 
THR   HB   H N N 374 
THR   HG1  H N N 375 
THR   HG21 H N N 376 
THR   HG22 H N N 377 
THR   HG23 H N N 378 
THR   HXT  H N N 379 
TRP   N    N N N 380 
TRP   CA   C N S 381 
TRP   C    C N N 382 
TRP   O    O N N 383 
TRP   CB   C N N 384 
TRP   CG   C Y N 385 
TRP   CD1  C Y N 386 
TRP   CD2  C Y N 387 
TRP   NE1  N Y N 388 
TRP   CE2  C Y N 389 
TRP   CE3  C Y N 390 
TRP   CZ2  C Y N 391 
TRP   CZ3  C Y N 392 
TRP   CH2  C Y N 393 
TRP   OXT  O N N 394 
TRP   H    H N N 395 
TRP   H2   H N N 396 
TRP   HA   H N N 397 
TRP   HB2  H N N 398 
TRP   HB3  H N N 399 
TRP   HD1  H N N 400 
TRP   HE1  H N N 401 
TRP   HE3  H N N 402 
TRP   HZ2  H N N 403 
TRP   HZ3  H N N 404 
TRP   HH2  H N N 405 
TRP   HXT  H N N 406 
TYR   N    N N N 407 
TYR   CA   C N S 408 
TYR   C    C N N 409 
TYR   O    O N N 410 
TYR   CB   C N N 411 
TYR   CG   C Y N 412 
TYR   CD1  C Y N 413 
TYR   CD2  C Y N 414 
TYR   CE1  C Y N 415 
TYR   CE2  C Y N 416 
TYR   CZ   C Y N 417 
TYR   OH   O N N 418 
TYR   OXT  O N N 419 
TYR   H    H N N 420 
TYR   H2   H N N 421 
TYR   HA   H N N 422 
TYR   HB2  H N N 423 
TYR   HB3  H N N 424 
TYR   HD1  H N N 425 
TYR   HD2  H N N 426 
TYR   HE1  H N N 427 
TYR   HE2  H N N 428 
TYR   HH   H N N 429 
TYR   HXT  H N N 430 
VAL   N    N N N 431 
VAL   CA   C N S 432 
VAL   C    C N N 433 
VAL   O    O N N 434 
VAL   CB   C N N 435 
VAL   CG1  C N N 436 
VAL   CG2  C N N 437 
VAL   OXT  O N N 438 
VAL   H    H N N 439 
VAL   H2   H N N 440 
VAL   HA   H N N 441 
VAL   HB   H N N 442 
VAL   HG11 H N N 443 
VAL   HG12 H N N 444 
VAL   HG13 H N N 445 
VAL   HG21 H N N 446 
VAL   HG22 H N N 447 
VAL   HG23 H N N 448 
VAL   HXT  H N N 449 
# 
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 
A1ASY C1  C2   sing N N 1   
A1ASY C3  C2   sing N N 2   
A1ASY C2  N1   sing N N 3   
A1ASY N1  C7   sing N N 4   
A1ASY N1  C4   sing N N 5   
A1ASY C15 C14  doub Y N 6   
A1ASY C15 C16  sing Y N 7   
A1ASY C7  C6   sing N N 8   
A1ASY C4  C5   sing N N 9   
A1ASY C14 N5   sing Y N 10  
A1ASY C16 C17  doub Y N 11  
A1ASY C16 C13  sing Y N 12  
A1ASY C17 C10  sing Y N 13  
A1ASY N5  C13  sing Y N 14  
A1ASY C6  N2   sing N N 15  
A1ASY C13 C12  doub Y N 16  
A1ASY C5  N2   sing N N 17  
A1ASY C10 N4   sing N N 18  
A1ASY C10 C11  doub Y N 19  
A1ASY N2  C8   sing N N 20  
A1ASY N4  C9   sing N N 21  
A1ASY N3  C9   doub Y N 22  
A1ASY N3  C8   sing Y N 23  
A1ASY C9  N6   sing Y N 24  
A1ASY C8  C23  doub Y N 25  
A1ASY N6  C18  doub Y N 26  
A1ASY C23 C18  sing Y N 27  
A1ASY C23 C22  sing N N 28  
A1ASY C18 C19  sing N N 29  
A1ASY C22 C21  sing N N 30  
A1ASY C12 C11  sing Y N 31  
A1ASY C20 C19  sing N N 32  
A1ASY C20 C21  sing N N 33  
A1ASY C4  H2   sing N N 34  
A1ASY C4  H3   sing N N 35  
A1ASY C5  H4   sing N N 36  
A1ASY C5  H5   sing N N 37  
A1ASY C6  H6   sing N N 38  
A1ASY C6  H7   sing N N 39  
A1ASY C7  H8   sing N N 40  
A1ASY C7  H9   sing N N 41  
A1ASY C15 H10  sing N N 42  
A1ASY C17 H11  sing N N 43  
A1ASY C20 H12  sing N N 44  
A1ASY C20 H13  sing N N 45  
A1ASY C21 H14  sing N N 46  
A1ASY C21 H15  sing N N 47  
A1ASY C22 H16  sing N N 48  
A1ASY C22 H17  sing N N 49  
A1ASY C1  H18  sing N N 50  
A1ASY C1  H19  sing N N 51  
A1ASY C1  H20  sing N N 52  
A1ASY C11 H21  sing N N 53  
A1ASY C12 H22  sing N N 54  
A1ASY C14 H23  sing N N 55  
A1ASY C19 H24  sing N N 56  
A1ASY C19 H25  sing N N 57  
A1ASY C2  H26  sing N N 58  
A1ASY C3  H27  sing N N 59  
A1ASY C3  H28  sing N N 60  
A1ASY C3  H29  sing N N 61  
A1ASY N4  H30  sing N N 62  
A1ASY N5  H31  sing N N 63  
ALA   N   CA   sing N N 64  
ALA   N   H    sing N N 65  
ALA   N   H2   sing N N 66  
ALA   CA  C    sing N N 67  
ALA   CA  CB   sing N N 68  
ALA   CA  HA   sing N N 69  
ALA   C   O    doub N N 70  
ALA   C   OXT  sing N N 71  
ALA   CB  HB1  sing N N 72  
ALA   CB  HB2  sing N N 73  
ALA   CB  HB3  sing N N 74  
ALA   OXT HXT  sing N N 75  
ARG   N   CA   sing N N 76  
ARG   N   H    sing N N 77  
ARG   N   H2   sing N N 78  
ARG   CA  C    sing N N 79  
ARG   CA  CB   sing N N 80  
ARG   CA  HA   sing N N 81  
ARG   C   O    doub N N 82  
ARG   C   OXT  sing N N 83  
ARG   CB  CG   sing N N 84  
ARG   CB  HB2  sing N N 85  
ARG   CB  HB3  sing N N 86  
ARG   CG  CD   sing N N 87  
ARG   CG  HG2  sing N N 88  
ARG   CG  HG3  sing N N 89  
ARG   CD  NE   sing N N 90  
ARG   CD  HD2  sing N N 91  
ARG   CD  HD3  sing N N 92  
ARG   NE  CZ   sing N N 93  
ARG   NE  HE   sing N N 94  
ARG   CZ  NH1  sing N N 95  
ARG   CZ  NH2  doub N N 96  
ARG   NH1 HH11 sing N N 97  
ARG   NH1 HH12 sing N N 98  
ARG   NH2 HH21 sing N N 99  
ARG   NH2 HH22 sing N N 100 
ARG   OXT HXT  sing N N 101 
ASN   N   CA   sing N N 102 
ASN   N   H    sing N N 103 
ASN   N   H2   sing N N 104 
ASN   CA  C    sing N N 105 
ASN   CA  CB   sing N N 106 
ASN   CA  HA   sing N N 107 
ASN   C   O    doub N N 108 
ASN   C   OXT  sing N N 109 
ASN   CB  CG   sing N N 110 
ASN   CB  HB2  sing N N 111 
ASN   CB  HB3  sing N N 112 
ASN   CG  OD1  doub N N 113 
ASN   CG  ND2  sing N N 114 
ASN   ND2 HD21 sing N N 115 
ASN   ND2 HD22 sing N N 116 
ASN   OXT HXT  sing N N 117 
ASP   N   CA   sing N N 118 
ASP   N   H    sing N N 119 
ASP   N   H2   sing N N 120 
ASP   CA  C    sing N N 121 
ASP   CA  CB   sing N N 122 
ASP   CA  HA   sing N N 123 
ASP   C   O    doub N N 124 
ASP   C   OXT  sing N N 125 
ASP   CB  CG   sing N N 126 
ASP   CB  HB2  sing N N 127 
ASP   CB  HB3  sing N N 128 
ASP   CG  OD1  doub N N 129 
ASP   CG  OD2  sing N N 130 
ASP   OD2 HD2  sing N N 131 
ASP   OXT HXT  sing N N 132 
CYS   N   CA   sing N N 133 
CYS   N   H    sing N N 134 
CYS   N   H2   sing N N 135 
CYS   CA  C    sing N N 136 
CYS   CA  CB   sing N N 137 
CYS   CA  HA   sing N N 138 
CYS   C   O    doub N N 139 
CYS   C   OXT  sing N N 140 
CYS   CB  SG   sing N N 141 
CYS   CB  HB2  sing N N 142 
CYS   CB  HB3  sing N N 143 
CYS   SG  HG   sing N N 144 
CYS   OXT HXT  sing N N 145 
GLN   N   CA   sing N N 146 
GLN   N   H    sing N N 147 
GLN   N   H2   sing N N 148 
GLN   CA  C    sing N N 149 
GLN   CA  CB   sing N N 150 
GLN   CA  HA   sing N N 151 
GLN   C   O    doub N N 152 
GLN   C   OXT  sing N N 153 
GLN   CB  CG   sing N N 154 
GLN   CB  HB2  sing N N 155 
GLN   CB  HB3  sing N N 156 
GLN   CG  CD   sing N N 157 
GLN   CG  HG2  sing N N 158 
GLN   CG  HG3  sing N N 159 
GLN   CD  OE1  doub N N 160 
GLN   CD  NE2  sing N N 161 
GLN   NE2 HE21 sing N N 162 
GLN   NE2 HE22 sing N N 163 
GLN   OXT HXT  sing N N 164 
GLU   N   CA   sing N N 165 
GLU   N   H    sing N N 166 
GLU   N   H2   sing N N 167 
GLU   CA  C    sing N N 168 
GLU   CA  CB   sing N N 169 
GLU   CA  HA   sing N N 170 
GLU   C   O    doub N N 171 
GLU   C   OXT  sing N N 172 
GLU   CB  CG   sing N N 173 
GLU   CB  HB2  sing N N 174 
GLU   CB  HB3  sing N N 175 
GLU   CG  CD   sing N N 176 
GLU   CG  HG2  sing N N 177 
GLU   CG  HG3  sing N N 178 
GLU   CD  OE1  doub N N 179 
GLU   CD  OE2  sing N N 180 
GLU   OE2 HE2  sing N N 181 
GLU   OXT HXT  sing N N 182 
GLY   N   CA   sing N N 183 
GLY   N   H    sing N N 184 
GLY   N   H2   sing N N 185 
GLY   CA  C    sing N N 186 
GLY   CA  HA2  sing N N 187 
GLY   CA  HA3  sing N N 188 
GLY   C   O    doub N N 189 
GLY   C   OXT  sing N N 190 
GLY   OXT HXT  sing N N 191 
HIS   N   CA   sing N N 192 
HIS   N   H    sing N N 193 
HIS   N   H2   sing N N 194 
HIS   CA  C    sing N N 195 
HIS   CA  CB   sing N N 196 
HIS   CA  HA   sing N N 197 
HIS   C   O    doub N N 198 
HIS   C   OXT  sing N N 199 
HIS   CB  CG   sing N N 200 
HIS   CB  HB2  sing N N 201 
HIS   CB  HB3  sing N N 202 
HIS   CG  ND1  sing Y N 203 
HIS   CG  CD2  doub Y N 204 
HIS   ND1 CE1  doub Y N 205 
HIS   ND1 HD1  sing N N 206 
HIS   CD2 NE2  sing Y N 207 
HIS   CD2 HD2  sing N N 208 
HIS   CE1 NE2  sing Y N 209 
HIS   CE1 HE1  sing N N 210 
HIS   NE2 HE2  sing N N 211 
HIS   OXT HXT  sing N N 212 
HOH   O   H1   sing N N 213 
HOH   O   H2   sing N N 214 
ILE   N   CA   sing N N 215 
ILE   N   H    sing N N 216 
ILE   N   H2   sing N N 217 
ILE   CA  C    sing N N 218 
ILE   CA  CB   sing N N 219 
ILE   CA  HA   sing N N 220 
ILE   C   O    doub N N 221 
ILE   C   OXT  sing N N 222 
ILE   CB  CG1  sing N N 223 
ILE   CB  CG2  sing N N 224 
ILE   CB  HB   sing N N 225 
ILE   CG1 CD1  sing N N 226 
ILE   CG1 HG12 sing N N 227 
ILE   CG1 HG13 sing N N 228 
ILE   CG2 HG21 sing N N 229 
ILE   CG2 HG22 sing N N 230 
ILE   CG2 HG23 sing N N 231 
ILE   CD1 HD11 sing N N 232 
ILE   CD1 HD12 sing N N 233 
ILE   CD1 HD13 sing N N 234 
ILE   OXT HXT  sing N N 235 
LEU   N   CA   sing N N 236 
LEU   N   H    sing N N 237 
LEU   N   H2   sing N N 238 
LEU   CA  C    sing N N 239 
LEU   CA  CB   sing N N 240 
LEU   CA  HA   sing N N 241 
LEU   C   O    doub N N 242 
LEU   C   OXT  sing N N 243 
LEU   CB  CG   sing N N 244 
LEU   CB  HB2  sing N N 245 
LEU   CB  HB3  sing N N 246 
LEU   CG  CD1  sing N N 247 
LEU   CG  CD2  sing N N 248 
LEU   CG  HG   sing N N 249 
LEU   CD1 HD11 sing N N 250 
LEU   CD1 HD12 sing N N 251 
LEU   CD1 HD13 sing N N 252 
LEU   CD2 HD21 sing N N 253 
LEU   CD2 HD22 sing N N 254 
LEU   CD2 HD23 sing N N 255 
LEU   OXT HXT  sing N N 256 
LYS   N   CA   sing N N 257 
LYS   N   H    sing N N 258 
LYS   N   H2   sing N N 259 
LYS   CA  C    sing N N 260 
LYS   CA  CB   sing N N 261 
LYS   CA  HA   sing N N 262 
LYS   C   O    doub N N 263 
LYS   C   OXT  sing N N 264 
LYS   CB  CG   sing N N 265 
LYS   CB  HB2  sing N N 266 
LYS   CB  HB3  sing N N 267 
LYS   CG  CD   sing N N 268 
LYS   CG  HG2  sing N N 269 
LYS   CG  HG3  sing N N 270 
LYS   CD  CE   sing N N 271 
LYS   CD  HD2  sing N N 272 
LYS   CD  HD3  sing N N 273 
LYS   CE  NZ   sing N N 274 
LYS   CE  HE2  sing N N 275 
LYS   CE  HE3  sing N N 276 
LYS   NZ  HZ1  sing N N 277 
LYS   NZ  HZ2  sing N N 278 
LYS   NZ  HZ3  sing N N 279 
LYS   OXT HXT  sing N N 280 
MET   N   CA   sing N N 281 
MET   N   H    sing N N 282 
MET   N   H2   sing N N 283 
MET   CA  C    sing N N 284 
MET   CA  CB   sing N N 285 
MET   CA  HA   sing N N 286 
MET   C   O    doub N N 287 
MET   C   OXT  sing N N 288 
MET   CB  CG   sing N N 289 
MET   CB  HB2  sing N N 290 
MET   CB  HB3  sing N N 291 
MET   CG  SD   sing N N 292 
MET   CG  HG2  sing N N 293 
MET   CG  HG3  sing N N 294 
MET   SD  CE   sing N N 295 
MET   CE  HE1  sing N N 296 
MET   CE  HE2  sing N N 297 
MET   CE  HE3  sing N N 298 
MET   OXT HXT  sing N N 299 
PHE   N   CA   sing N N 300 
PHE   N   H    sing N N 301 
PHE   N   H2   sing N N 302 
PHE   CA  C    sing N N 303 
PHE   CA  CB   sing N N 304 
PHE   CA  HA   sing N N 305 
PHE   C   O    doub N N 306 
PHE   C   OXT  sing N N 307 
PHE   CB  CG   sing N N 308 
PHE   CB  HB2  sing N N 309 
PHE   CB  HB3  sing N N 310 
PHE   CG  CD1  doub Y N 311 
PHE   CG  CD2  sing Y N 312 
PHE   CD1 CE1  sing Y N 313 
PHE   CD1 HD1  sing N N 314 
PHE   CD2 CE2  doub Y N 315 
PHE   CD2 HD2  sing N N 316 
PHE   CE1 CZ   doub Y N 317 
PHE   CE1 HE1  sing N N 318 
PHE   CE2 CZ   sing Y N 319 
PHE   CE2 HE2  sing N N 320 
PHE   CZ  HZ   sing N N 321 
PHE   OXT HXT  sing N N 322 
PRO   N   CA   sing N N 323 
PRO   N   CD   sing N N 324 
PRO   N   H    sing N N 325 
PRO   CA  C    sing N N 326 
PRO   CA  CB   sing N N 327 
PRO   CA  HA   sing N N 328 
PRO   C   O    doub N N 329 
PRO   C   OXT  sing N N 330 
PRO   CB  CG   sing N N 331 
PRO   CB  HB2  sing N N 332 
PRO   CB  HB3  sing N N 333 
PRO   CG  CD   sing N N 334 
PRO   CG  HG2  sing N N 335 
PRO   CG  HG3  sing N N 336 
PRO   CD  HD2  sing N N 337 
PRO   CD  HD3  sing N N 338 
PRO   OXT HXT  sing N N 339 
SER   N   CA   sing N N 340 
SER   N   H    sing N N 341 
SER   N   H2   sing N N 342 
SER   CA  C    sing N N 343 
SER   CA  CB   sing N N 344 
SER   CA  HA   sing N N 345 
SER   C   O    doub N N 346 
SER   C   OXT  sing N N 347 
SER   CB  OG   sing N N 348 
SER   CB  HB2  sing N N 349 
SER   CB  HB3  sing N N 350 
SER   OG  HG   sing N N 351 
SER   OXT HXT  sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TRP   N   CA   sing N N 369 
TRP   N   H    sing N N 370 
TRP   N   H2   sing N N 371 
TRP   CA  C    sing N N 372 
TRP   CA  CB   sing N N 373 
TRP   CA  HA   sing N N 374 
TRP   C   O    doub N N 375 
TRP   C   OXT  sing N N 376 
TRP   CB  CG   sing N N 377 
TRP   CB  HB2  sing N N 378 
TRP   CB  HB3  sing N N 379 
TRP   CG  CD1  doub Y N 380 
TRP   CG  CD2  sing Y N 381 
TRP   CD1 NE1  sing Y N 382 
TRP   CD1 HD1  sing N N 383 
TRP   CD2 CE2  doub Y N 384 
TRP   CD2 CE3  sing Y N 385 
TRP   NE1 CE2  sing Y N 386 
TRP   NE1 HE1  sing N N 387 
TRP   CE2 CZ2  sing Y N 388 
TRP   CE3 CZ3  doub Y N 389 
TRP   CE3 HE3  sing N N 390 
TRP   CZ2 CH2  doub Y N 391 
TRP   CZ2 HZ2  sing N N 392 
TRP   CZ3 CH2  sing Y N 393 
TRP   CZ3 HZ3  sing N N 394 
TRP   CH2 HH2  sing N N 395 
TRP   OXT HXT  sing N N 396 
TYR   N   CA   sing N N 397 
TYR   N   H    sing N N 398 
TYR   N   H2   sing N N 399 
TYR   CA  C    sing N N 400 
TYR   CA  CB   sing N N 401 
TYR   CA  HA   sing N N 402 
TYR   C   O    doub N N 403 
TYR   C   OXT  sing N N 404 
TYR   CB  CG   sing N N 405 
TYR   CB  HB2  sing N N 406 
TYR   CB  HB3  sing N N 407 
TYR   CG  CD1  doub Y N 408 
TYR   CG  CD2  sing Y N 409 
TYR   CD1 CE1  sing Y N 410 
TYR   CD1 HD1  sing N N 411 
TYR   CD2 CE2  doub Y N 412 
TYR   CD2 HD2  sing N N 413 
TYR   CE1 CZ   doub Y N 414 
TYR   CE1 HE1  sing N N 415 
TYR   CE2 CZ   sing Y N 416 
TYR   CE2 HE2  sing N N 417 
TYR   CZ  OH   sing N N 418 
TYR   OH  HH   sing N N 419 
TYR   OXT HXT  sing N N 420 
VAL   N   CA   sing N N 421 
VAL   N   H    sing N N 422 
VAL   N   H2   sing N N 423 
VAL   CA  C    sing N N 424 
VAL   CA  CB   sing N N 425 
VAL   CA  HA   sing N N 426 
VAL   C   O    doub N N 427 
VAL   C   OXT  sing N N 428 
VAL   CB  CG1  sing N N 429 
VAL   CB  CG2  sing N N 430 
VAL   CB  HB   sing N N 431 
VAL   CG1 HG11 sing N N 432 
VAL   CG1 HG12 sing N N 433 
VAL   CG1 HG13 sing N N 434 
VAL   CG2 HG21 sing N N 435 
VAL   CG2 HG22 sing N N 436 
VAL   CG2 HG23 sing N N 437 
VAL   OXT HXT  sing N N 438 
# 
_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                    9BVE 
_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]   0.015568 
_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]   0.011581 
_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]   0.009382 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU   A 1 25  ? -14.928 -31.002 -34.242 1.00 43.09  ? -4   LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 25  ? -13.880 -30.815 -35.243 1.00 43.53  ? -4   LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 25  ? -14.137 -31.684 -36.475 1.00 43.45  ? -4   LEU   A C   1 
ATOM   4    O O   . LEU   A 1 25  ? -14.076 -31.198 -37.605 1.00 43.96  ? -4   LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 25  ? -12.505 -31.119 -34.636 1.00 44.28  ? -4   LEU   A CB  1 
ATOM   6    C CG  . LEU   A 1 25  ? -11.219 -31.026 -35.470 1.00 45.72  ? -4   LEU   A CG  1 
ATOM   7    C CD1 . LEU   A 1 25  ? -11.294 -29.999 -36.598 1.00 46.03  ? -4   LEU   A CD1 1 
ATOM   8    C CD2 . LEU   A 1 25  ? -10.046 -30.702 -34.555 1.00 45.56  ? -4   LEU   A CD2 1 
ATOM   9    N N   . TYR   A 1 26  ? -14.423 -32.969 -36.257 1.00 42.82  ? -3   TYR   A N   1 
ATOM   10   C CA  . TYR   A 1 26  ? -14.752 -33.895 -37.335 1.00 41.64  ? -3   TYR   A CA  1 
ATOM   11   C C   . TYR   A 1 26  ? -16.238 -34.221 -37.381 1.00 39.43  ? -3   TYR   A C   1 
ATOM   12   O O   . TYR   A 1 26  ? -16.645 -35.129 -38.112 1.00 39.73  ? -3   TYR   A O   1 
ATOM   13   C CB  . TYR   A 1 26  ? -13.921 -35.172 -37.201 1.00 43.02  ? -3   TYR   A CB  1 
ATOM   14   C CG  . TYR   A 1 26  ? -12.441 -34.885 -37.264 1.00 44.51  ? -3   TYR   A CG  1 
ATOM   15   C CD1 . TYR   A 1 26  ? -11.854 -34.472 -38.452 1.00 45.61  ? -3   TYR   A CD1 1 
ATOM   16   C CD2 . TYR   A 1 26  ? -11.637 -34.990 -36.134 1.00 44.31  ? -3   TYR   A CD2 1 
ATOM   17   C CE1 . TYR   A 1 26  ? -10.509 -34.187 -38.524 1.00 46.32  ? -3   TYR   A CE1 1 
ATOM   18   C CE2 . TYR   A 1 26  ? -10.282 -34.705 -36.196 1.00 44.89  ? -3   TYR   A CE2 1 
ATOM   19   C CZ  . TYR   A 1 26  ? -9.727  -34.303 -37.399 1.00 46.14  ? -3   TYR   A CZ  1 
ATOM   20   O OH  . TYR   A 1 26  ? -8.386  -34.011 -37.500 1.00 47.50  ? -3   TYR   A OH  1 
ATOM   21   N N   . PHE   A 1 27  ? -17.052 -33.489 -36.625 1.00 38.42  ? -2   PHE   A N   1 
ATOM   22   C CA  . PHE   A 1 27  ? -18.496 -33.657 -36.578 1.00 37.89  ? -2   PHE   A CA  1 
ATOM   23   C C   . PHE   A 1 27  ? -19.074 -32.465 -35.840 1.00 37.50  ? -2   PHE   A C   1 
ATOM   24   O O   . PHE   A 1 27  ? -18.490 -32.006 -34.858 1.00 37.23  ? -2   PHE   A O   1 
ATOM   25   C CB  . PHE   A 1 27  ? -18.889 -34.966 -35.878 1.00 38.69  ? -2   PHE   A CB  1 
ATOM   26   C CG  . PHE   A 1 27  ? -20.367 -35.108 -35.643 1.00 39.08  ? -2   PHE   A CG  1 
ATOM   27   C CD1 . PHE   A 1 27  ? -21.213 -35.484 -36.673 1.00 39.53  ? -2   PHE   A CD1 1 
ATOM   28   C CD2 . PHE   A 1 27  ? -20.912 -34.863 -34.395 1.00 38.97  ? -2   PHE   A CD2 1 
ATOM   29   C CE1 . PHE   A 1 27  ? -22.576 -35.610 -36.465 1.00 39.57  ? -2   PHE   A CE1 1 
ATOM   30   C CE2 . PHE   A 1 27  ? -22.279 -34.988 -34.180 1.00 38.97  ? -2   PHE   A CE2 1 
ATOM   31   C CZ  . PHE   A 1 27  ? -23.109 -35.360 -35.217 1.00 39.05  ? -2   PHE   A CZ  1 
ATOM   32   N N   . GLN   A 1 28  ? -20.209 -31.964 -36.316 1.00 38.45  ? -1   GLN   A N   1 
ATOM   33   C CA  . GLN   A 1 28  ? -20.848 -30.809 -35.700 1.00 39.84  ? -1   GLN   A CA  1 
ATOM   34   C C   . GLN   A 1 28  ? -21.937 -31.294 -34.748 1.00 40.00  ? -1   GLN   A C   1 
ATOM   35   O O   . GLN   A 1 28  ? -22.867 -31.998 -35.160 1.00 39.91  ? -1   GLN   A O   1 
ATOM   36   C CB  . GLN   A 1 28  ? -21.409 -29.871 -36.770 1.00 42.77  ? -1   GLN   A CB  1 
ATOM   37   C CG  . GLN   A 1 28  ? -20.382 -29.537 -37.860 1.00 46.94  ? -1   GLN   A CG  1 
ATOM   38   C CD  . GLN   A 1 28  ? -20.874 -28.508 -38.871 1.00 50.28  ? -1   GLN   A CD  1 
ATOM   39   O OE1 . GLN   A 1 28  ? -20.146 -27.583 -39.224 1.00 51.79  ? -1   GLN   A OE1 1 
ATOM   40   N NE2 . GLN   A 1 28  ? -22.103 -28.675 -39.351 1.00 51.36  ? -1   GLN   A NE2 1 
ATOM   41   N N   . GLU   A 1 29  ? -21.801 -30.941 -33.475 1.00 40.74  ? 566  GLU   A N   1 
ATOM   42   C CA  . GLU   A 1 29  ? -22.761 -31.357 -32.469 1.00 41.17  ? 566  GLU   A CA  1 
ATOM   43   C C   . GLU   A 1 29  ? -23.954 -30.406 -32.451 1.00 37.42  ? 566  GLU   A C   1 
ATOM   44   O O   . GLU   A 1 29  ? -23.928 -29.316 -33.029 1.00 33.05  ? 566  GLU   A O   1 
ATOM   45   C CB  . GLU   A 1 29  ? -22.107 -31.411 -31.087 1.00 44.92  ? 566  GLU   A CB  1 
ATOM   46   C CG  . GLU   A 1 29  ? -20.894 -32.330 -30.992 1.00 48.95  ? 566  GLU   A CG  1 
ATOM   47   C CD  . GLU   A 1 29  ? -20.333 -32.418 -29.577 1.00 52.11  ? 566  GLU   A CD  1 
ATOM   48   O OE1 . GLU   A 1 29  ? -20.471 -31.439 -28.810 1.00 52.63  ? 566  GLU   A OE1 1 
ATOM   49   O OE2 . GLU   A 1 29  ? -19.755 -33.469 -29.227 1.00 53.57  ? 566  GLU   A OE2 1 
ATOM   50   N N   . GLN   A 1 30  ? -25.008 -30.837 -31.765 1.00 41.50  ? 567  GLN   A N   1 
ATOM   51   C CA  . GLN   A 1 30  ? -26.198 -30.012 -31.601 1.00 47.22  ? 567  GLN   A CA  1 
ATOM   52   C C   . GLN   A 1 30  ? -25.849 -28.703 -30.888 1.00 52.91  ? 567  GLN   A C   1 
ATOM   53   O O   . GLN   A 1 30  ? -25.141 -28.724 -29.870 1.00 55.81  ? 567  GLN   A O   1 
ATOM   54   C CB  . GLN   A 1 30  ? -27.257 -30.782 -30.809 1.00 42.17  ? 567  GLN   A CB  1 
ATOM   55   C CG  . GLN   A 1 30  ? -28.447 -29.950 -30.373 1.00 39.84  ? 567  GLN   A CG  1 
ATOM   56   C CD  . GLN   A 1 30  ? -29.412 -30.719 -29.491 1.00 39.73  ? 567  GLN   A CD  1 
ATOM   57   O OE1 . GLN   A 1 30  ? -29.070 -31.122 -28.380 1.00 39.38  ? 567  GLN   A OE1 1 
ATOM   58   N NE2 . GLN   A 1 30  ? -30.630 -30.926 -29.984 1.00 40.39  ? 567  GLN   A NE2 1 
ATOM   59   N N   . PRO   A 1 31  ? -26.309 -27.556 -31.386 1.00 43.08  ? 568  PRO   A N   1 
ATOM   60   C CA  . PRO   A 1 31  ? -25.932 -26.277 -30.774 1.00 36.70  ? 568  PRO   A CA  1 
ATOM   61   C C   . PRO   A 1 31  ? -26.527 -26.095 -29.386 1.00 33.10  ? 568  PRO   A C   1 
ATOM   62   O O   . PRO   A 1 31  ? -27.591 -26.624 -29.062 1.00 31.27  ? 568  PRO   A O   1 
ATOM   63   C CB  . PRO   A 1 31  ? -26.495 -25.235 -31.749 1.00 28.82  ? 568  PRO   A CB  1 
ATOM   64   C CG  . PRO   A 1 31  ? -26.707 -25.967 -33.023 1.00 29.39  ? 568  PRO   A CG  1 
ATOM   65   C CD  . PRO   A 1 31  ? -27.052 -27.368 -32.639 1.00 37.44  ? 568  PRO   A CD  1 
ATOM   66   N N   . LEU   A 1 32  ? -25.814 -25.324 -28.568 1.00 34.41  ? 569  LEU   A N   1 
ATOM   67   C CA  . LEU   A 1 32  ? -26.256 -24.993 -27.219 1.00 35.03  ? 569  LEU   A CA  1 
ATOM   68   C C   . LEU   A 1 32  ? -27.312 -23.893 -27.280 1.00 36.56  ? 569  LEU   A C   1 
ATOM   69   O O   . LEU   A 1 32  ? -27.117 -22.877 -27.952 1.00 36.62  ? 569  LEU   A O   1 
ATOM   70   C CB  . LEU   A 1 32  ? -25.059 -24.537 -26.381 1.00 33.95  ? 569  LEU   A CB  1 
ATOM   71   C CG  . LEU   A 1 32  ? -25.020 -24.808 -24.878 1.00 35.49  ? 569  LEU   A CG  1 
ATOM   72   C CD1 . LEU   A 1 32  ? -24.829 -26.294 -24.596 1.00 36.65  ? 569  LEU   A CD1 1 
ATOM   73   C CD2 . LEU   A 1 32  ? -23.917 -23.988 -24.215 1.00 35.04  ? 569  LEU   A CD2 1 
ATOM   74   N N   . ARG   A 1 33  ? -28.430 -24.093 -26.583 1.00 38.66  ? 570  ARG   A N   1 
ATOM   75   C CA  . ARG   A 1 33  ? -29.511 -23.112 -26.563 1.00 40.21  ? 570  ARG   A CA  1 
ATOM   76   C C   . ARG   A 1 33  ? -29.237 -22.063 -25.489 1.00 39.61  ? 570  ARG   A C   1 
ATOM   77   O O   . ARG   A 1 33  ? -29.022 -22.404 -24.320 1.00 40.34  ? 570  ARG   A O   1 
ATOM   78   C CB  . ARG   A 1 33  ? -30.860 -23.787 -26.314 1.00 43.73  ? 570  ARG   A CB  1 
ATOM   79   C CG  . ARG   A 1 33  ? -32.045 -22.922 -26.725 1.00 46.03  ? 570  ARG   A CG  1 
ATOM   80   C CD  . ARG   A 1 33  ? -33.356 -23.423 -26.146 1.00 47.66  ? 570  ARG   A CD  1 
ATOM   81   N NE  . ARG   A 1 33  ? -34.427 -22.467 -26.400 1.00 48.82  ? 570  ARG   A NE  1 
ATOM   82   C CZ  . ARG   A 1 33  ? -35.595 -22.466 -25.770 1.00 51.29  ? 570  ARG   A CZ  1 
ATOM   83   N NH1 . ARG   A 1 33  ? -35.854 -23.375 -24.838 1.00 52.55  ? 570  ARG   A NH1 1 
ATOM   84   N NH2 . ARG   A 1 33  ? -36.505 -21.551 -26.072 1.00 52.44  ? 570  ARG   A NH2 1 
ATOM   85   N N   . LEU   A 1 34  ? -29.256 -20.793 -25.887 1.00 37.71  ? 571  LEU   A N   1 
ATOM   86   C CA  . LEU   A 1 34  ? -28.874 -19.675 -25.041 1.00 36.05  ? 571  LEU   A CA  1 
ATOM   87   C C   . LEU   A 1 34  ? -30.017 -18.674 -24.904 1.00 36.69  ? 571  LEU   A C   1 
ATOM   88   O O   . LEU   A 1 34  ? -30.918 -18.627 -25.749 1.00 37.68  ? 571  LEU   A O   1 
ATOM   89   C CB  . LEU   A 1 34  ? -27.634 -18.965 -25.608 1.00 33.60  ? 571  LEU   A CB  1 
ATOM   90   C CG  . LEU   A 1 34  ? -26.301 -19.720 -25.579 1.00 30.65  ? 571  LEU   A CG  1 
ATOM   91   C CD1 . LEU   A 1 34  ? -25.247 -18.942 -26.341 1.00 29.73  ? 571  LEU   A CD1 1 
ATOM   92   C CD2 . LEU   A 1 34  ? -25.843 -19.979 -24.149 1.00 29.26  ? 571  LEU   A CD2 1 
ATOM   93   N N   . PRO   A 1 35  ? -30.015 -17.862 -23.846 1.00 36.36  ? 572  PRO   A N   1 
ATOM   94   C CA  . PRO   A 1 35  ? -31.041 -16.821 -23.714 1.00 36.16  ? 572  PRO   A CA  1 
ATOM   95   C C   . PRO   A 1 35  ? -30.862 -15.723 -24.751 1.00 35.84  ? 572  PRO   A C   1 
ATOM   96   O O   . PRO   A 1 35  ? -29.852 -15.630 -25.453 1.00 34.66  ? 572  PRO   A O   1 
ATOM   97   C CB  . PRO   A 1 35  ? -30.833 -16.286 -22.294 1.00 35.73  ? 572  PRO   A CB  1 
ATOM   98   C CG  . PRO   A 1 35  ? -29.415 -16.603 -21.981 1.00 35.24  ? 572  PRO   A CG  1 
ATOM   99   C CD  . PRO   A 1 35  ? -29.147 -17.922 -22.658 1.00 35.52  ? 572  PRO   A CD  1 
ATOM   100  N N   . SER   A 1 36  ? -31.877 -14.874 -24.829 1.00 37.49  ? 573  SER   A N   1 
ATOM   101  C CA  . SER   A 1 36  ? -31.880 -13.807 -25.812 1.00 38.43  ? 573  SER   A CA  1 
ATOM   102  C C   . SER   A 1 36  ? -30.875 -12.723 -25.427 1.00 39.84  ? 573  SER   A C   1 
ATOM   103  O O   . SER   A 1 36  ? -30.738 -12.387 -24.244 1.00 39.72  ? 573  SER   A O   1 
ATOM   104  C CB  . SER   A 1 36  ? -33.273 -13.203 -25.924 1.00 39.60  ? 573  SER   A CB  1 
ATOM   105  O OG  . SER   A 1 36  ? -33.198 -11.804 -26.117 1.00 39.92  ? 573  SER   A OG  1 
ATOM   106  N N   . PRO   A 1 37  ? -30.159 -12.150 -26.399 1.00 40.85  ? 574  PRO   A N   1 
ATOM   107  C CA  . PRO   A 1 37  ? -29.308 -10.989 -26.104 1.00 41.30  ? 574  PRO   A CA  1 
ATOM   108  C C   . PRO   A 1 37  ? -30.068 -9.760  -25.626 1.00 44.13  ? 574  PRO   A C   1 
ATOM   109  O O   . PRO   A 1 37  ? -29.429 -8.754  -25.307 1.00 44.73  ? 574  PRO   A O   1 
ATOM   110  C CB  . PRO   A 1 37  ? -28.615 -10.716 -27.445 1.00 40.45  ? 574  PRO   A CB  1 
ATOM   111  C CG  . PRO   A 1 37  ? -29.469 -11.394 -28.472 1.00 40.94  ? 574  PRO   A CG  1 
ATOM   112  C CD  . PRO   A 1 37  ? -30.016 -12.602 -27.793 1.00 40.42  ? 574  PRO   A CD  1 
ATOM   113  N N   . GLU   A 1 38  ? -31.403 -9.793  -25.554 1.00 46.63  ? 575  GLU   A N   1 
ATOM   114  C CA  . GLU   A 1 38  ? -32.148 -8.690  -24.954 1.00 49.26  ? 575  GLU   A CA  1 
ATOM   115  C C   . GLU   A 1 38  ? -32.245 -8.813  -23.440 1.00 46.12  ? 575  GLU   A C   1 
ATOM   116  O O   . GLU   A 1 38  ? -32.613 -7.839  -22.776 1.00 46.52  ? 575  GLU   A O   1 
ATOM   117  C CB  . GLU   A 1 38  ? -33.565 -8.592  -25.543 1.00 54.65  ? 575  GLU   A CB  1 
ATOM   118  C CG  . GLU   A 1 38  ? -33.662 -7.942  -26.926 1.00 58.30  ? 575  GLU   A CG  1 
ATOM   119  C CD  . GLU   A 1 38  ? -33.171 -8.840  -28.055 1.00 60.40  ? 575  GLU   A CD  1 
ATOM   120  O OE1 . GLU   A 1 38  ? -33.467 -10.055 -28.035 1.00 61.47  ? 575  GLU   A OE1 1 
ATOM   121  O OE2 . GLU   A 1 38  ? -32.484 -8.328  -28.966 1.00 60.53  ? 575  GLU   A OE2 1 
ATOM   122  N N   . VAL   A 1 39  ? -31.943 -9.986  -22.885 1.00 43.00  ? 576  VAL   A N   1 
ATOM   123  C CA  . VAL   A 1 39  ? -31.912 -10.193 -21.444 1.00 40.03  ? 576  VAL   A CA  1 
ATOM   124  C C   . VAL   A 1 39  ? -30.535 -10.591 -20.943 1.00 37.81  ? 576  VAL   A C   1 
ATOM   125  O O   . VAL   A 1 39  ? -30.332 -10.671 -19.723 1.00 38.32  ? 576  VAL   A O   1 
ATOM   126  C CB  . VAL   A 1 39  ? -32.959 -11.233 -20.998 1.00 40.01  ? 576  VAL   A CB  1 
ATOM   127  C CG1 . VAL   A 1 39  ? -34.358 -10.715 -21.271 1.00 41.09  ? 576  VAL   A CG1 1 
ATOM   128  C CG2 . VAL   A 1 39  ? -32.735 -12.563 -21.705 1.00 39.97  ? 576  VAL   A CG2 1 
ATOM   129  N N   . TYR   A 1 40  ? -29.575 -10.818 -21.840 1.00 34.90  ? 577  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 40  ? -28.231 -11.204 -21.415 1.00 33.75  ? 577  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 40  ? -27.283 -10.821 -22.555 1.00 34.66  ? 577  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 40  ? -27.056 -11.608 -23.474 1.00 35.86  ? 577  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 40  ? -28.164 -12.679 -21.082 1.00 32.55  ? 577  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 40  ? -26.892 -13.126 -20.399 1.00 30.80  ? 577  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 40  ? -26.567 -12.675 -19.127 1.00 29.80  ? 577  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 40  ? -26.035 -14.032 -21.014 1.00 29.77  ? 577  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 40  ? -25.409 -13.094 -18.492 1.00 28.03  ? 577  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 40  ? -24.877 -14.461 -20.388 1.00 28.72  ? 577  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 40  ? -24.566 -13.986 -19.128 1.00 28.49  ? 577  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 40  ? -23.412 -14.407 -18.503 1.00 28.83  ? 577  TYR   A OH  1 
ATOM   141  N N   . ARG   A 1 41  ? -26.743 -9.604  -22.482 1.00 34.07  ? 578  ARG   A N   1 
ATOM   142  C CA  . ARG   A 1 41  ? -26.016 -9.076  -23.631 1.00 33.91  ? 578  ARG   A CA  1 
ATOM   143  C C   . ARG   A 1 41  ? -24.699 -9.798  -23.906 1.00 33.33  ? 578  ARG   A C   1 
ATOM   144  O O   . ARG   A 1 41  ? -24.048 -9.485  -24.908 1.00 33.82  ? 578  ARG   A O   1 
ATOM   145  C CB  . ARG   A 1 41  ? -25.769 -7.581  -23.444 1.00 33.13  ? 578  ARG   A CB  1 
ATOM   146  C CG  . ARG   A 1 41  ? -25.234 -7.174  -22.091 1.00 31.79  ? 578  ARG   A CG  1 
ATOM   147  C CD  . ARG   A 1 41  ? -24.961 -5.678  -22.078 1.00 31.68  ? 578  ARG   A CD  1 
ATOM   148  N NE  . ARG   A 1 41  ? -24.337 -5.222  -20.843 1.00 30.99  ? 578  ARG   A NE  1 
ATOM   149  C CZ  . ARG   A 1 41  ? -23.577 -4.137  -20.760 1.00 31.74  ? 578  ARG   A CZ  1 
ATOM   150  N NH1 . ARG   A 1 41  ? -23.039 -3.783  -19.599 1.00 30.81  ? 578  ARG   A NH1 1 
ATOM   151  N NH2 . ARG   A 1 41  ? -23.347 -3.409  -21.846 1.00 33.12  ? 578  ARG   A NH2 1 
ATOM   152  N N   . PHE   A 1 42  ? -24.300 -10.760 -23.072 1.00 32.27  ? 579  PHE   A N   1 
ATOM   153  C CA  . PHE   A 1 42  ? -23.066 -11.501 -23.303 1.00 30.69  ? 579  PHE   A CA  1 
ATOM   154  C C   . PHE   A 1 42  ? -23.204 -12.584 -24.369 1.00 32.40  ? 579  PHE   A C   1 
ATOM   155  O O   . PHE   A 1 42  ? -22.189 -13.169 -24.760 1.00 33.01  ? 579  PHE   A O   1 
ATOM   156  C CB  . PHE   A 1 42  ? -22.578 -12.135 -21.998 1.00 28.03  ? 579  PHE   A CB  1 
ATOM   157  C CG  . PHE   A 1 42  ? -22.209 -11.137 -20.931 1.00 26.81  ? 579  PHE   A CG  1 
ATOM   158  C CD1 . PHE   A 1 42  ? -21.019 -10.439 -20.996 1.00 24.04  ? 579  PHE   A CD1 1 
ATOM   159  C CD2 . PHE   A 1 42  ? -23.053 -10.904 -19.855 1.00 26.61  ? 579  PHE   A CD2 1 
ATOM   160  C CE1 . PHE   A 1 42  ? -20.685 -9.524  -20.011 1.00 23.62  ? 579  PHE   A CE1 1 
ATOM   161  C CE2 . PHE   A 1 42  ? -22.718 -9.990  -18.866 1.00 25.07  ? 579  PHE   A CE2 1 
ATOM   162  C CZ  . PHE   A 1 42  ? -21.537 -9.302  -18.944 1.00 23.08  ? 579  PHE   A CZ  1 
ATOM   163  N N   . VAL   A 1 43  ? -24.418 -12.872 -24.849 1.00 33.15  ? 580  VAL   A N   1 
ATOM   164  C CA  . VAL   A 1 43  ? -24.608 -13.891 -25.876 1.00 34.62  ? 580  VAL   A CA  1 
ATOM   165  C C   . VAL   A 1 43  ? -24.728 -13.300 -27.269 1.00 36.24  ? 580  VAL   A C   1 
ATOM   166  O O   . VAL   A 1 43  ? -24.917 -14.053 -28.238 1.00 35.91  ? 580  VAL   A O   1 
ATOM   167  C CB  . VAL   A 1 43  ? -25.833 -14.780 -25.580 1.00 34.73  ? 580  VAL   A CB  1 
ATOM   168  C CG1 . VAL   A 1 43  ? -25.623 -15.553 -24.294 1.00 34.57  ? 580  VAL   A CG1 1 
ATOM   169  C CG2 . VAL   A 1 43  ? -27.097 -13.948 -25.515 1.00 35.54  ? 580  VAL   A CG2 1 
ATOM   170  N N   . VAL   A 1 44  ? -24.639 -11.974 -27.401 1.00 38.07  ? 581  VAL   A N   1 
ATOM   171  C CA  . VAL   A 1 44  ? -24.614 -11.347 -28.716 1.00 39.95  ? 581  VAL   A CA  1 
ATOM   172  C C   . VAL   A 1 44  ? -23.561 -12.022 -29.575 1.00 40.99  ? 581  VAL   A C   1 
ATOM   173  O O   . VAL   A 1 44  ? -22.437 -12.264 -29.121 1.00 40.03  ? 581  VAL   A O   1 
ATOM   174  C CB  . VAL   A 1 44  ? -24.351 -9.838  -28.584 1.00 40.72  ? 581  VAL   A CB  1 
ATOM   175  C CG1 . VAL   A 1 44  ? -24.162 -9.213  -29.954 1.00 42.06  ? 581  VAL   A CG1 1 
ATOM   176  C CG2 . VAL   A 1 44  ? -25.494 -9.168  -27.842 1.00 40.95  ? 581  VAL   A CG2 1 
ATOM   177  N N   . LYS   A 1 45  ? -23.933 -12.350 -30.813 1.00 43.58  ? 582  LYS   A N   1 
ATOM   178  C CA  . LYS   A 1 45  ? -23.059 -13.106 -31.703 1.00 44.76  ? 582  LYS   A CA  1 
ATOM   179  C C   . LYS   A 1 45  ? -21.728 -12.391 -31.894 1.00 44.97  ? 582  LYS   A C   1 
ATOM   180  O O   . LYS   A 1 45  ? -21.680 -11.174 -32.094 1.00 45.36  ? 582  LYS   A O   1 
ATOM   181  C CB  . LYS   A 1 45  ? -23.737 -13.310 -33.061 1.00 46.22  ? 582  LYS   A CB  1 
ATOM   182  C CG  . LYS   A 1 45  ? -22.956 -14.183 -34.055 1.00 46.89  ? 582  LYS   A CG  1 
ATOM   183  C CD  . LYS   A 1 45  ? -23.147 -15.660 -33.731 1.00 48.23  ? 582  LYS   A CD  1 
ATOM   184  C CE  . LYS   A 1 45  ? -22.511 -16.582 -34.757 1.00 49.68  ? 582  LYS   A CE  1 
ATOM   185  N NZ  . LYS   A 1 45  ? -23.073 -17.950 -34.568 1.00 49.82  ? 582  LYS   A NZ  1 
ATOM   186  N N   . ASP   A 1 46  ? -20.644 -13.160 -31.822 1.00 45.15  ? 583  ASP   A N   1 
ATOM   187  C CA  . ASP   A 1 46  ? -19.327 -12.625 -32.136 1.00 46.75  ? 583  ASP   A CA  1 
ATOM   188  C C   . ASP   A 1 46  ? -19.301 -12.105 -33.565 1.00 48.60  ? 583  ASP   A C   1 
ATOM   189  O O   . ASP   A 1 46  ? -19.932 -12.670 -34.463 1.00 49.29  ? 583  ASP   A O   1 
ATOM   190  C CB  . ASP   A 1 46  ? -18.252 -13.699 -31.962 1.00 47.65  ? 583  ASP   A CB  1 
ATOM   191  C CG  . ASP   A 1 46  ? -17.773 -13.826 -30.531 1.00 48.30  ? 583  ASP   A CG  1 
ATOM   192  O OD1 . ASP   A 1 46  ? -18.337 -13.150 -29.642 1.00 48.90  ? 583  ASP   A OD1 1 
ATOM   193  O OD2 . ASP   A 1 46  ? -16.825 -14.607 -30.300 1.00 47.59  ? 583  ASP   A OD2 1 
ATOM   194  N N   . SER   A 1 47  ? -18.572 -11.015 -33.770 1.00 49.36  ? 584  SER   A N   1 
ATOM   195  C CA  . SER   A 1 47  ? -18.379 -10.456 -35.099 1.00 50.62  ? 584  SER   A CA  1 
ATOM   196  C C   . SER   A 1 47  ? -17.155 -9.557  -35.049 1.00 51.78  ? 584  SER   A C   1 
ATOM   197  O O   . SER   A 1 47  ? -16.569 -9.330  -33.986 1.00 51.08  ? 584  SER   A O   1 
ATOM   198  C CB  . SER   A 1 47  ? -19.609 -9.679  -35.573 1.00 50.38  ? 584  SER   A CB  1 
ATOM   199  O OG  . SER   A 1 47  ? -19.613 -8.376  -35.018 1.00 49.49  ? 584  SER   A OG  1 
ATOM   200  N N   . GLU   A 1 48  ? -16.780 -9.034  -36.212 1.00 53.53  ? 585  GLU   A N   1 
ATOM   201  C CA  . GLU   A 1 48  ? -15.660 -8.109  -36.292 1.00 53.88  ? 585  GLU   A CA  1 
ATOM   202  C C   . GLU   A 1 48  ? -16.008 -6.730  -35.757 1.00 52.49  ? 585  GLU   A C   1 
ATOM   203  O O   . GLU   A 1 48  ? -15.119 -5.876  -35.670 1.00 52.30  ? 585  GLU   A O   1 
ATOM   204  C CB  . GLU   A 1 48  ? -15.164 -7.998  -37.739 1.00 56.32  ? 585  GLU   A CB  1 
ATOM   205  C CG  . GLU   A 1 48  ? -14.915 -9.342  -38.440 1.00 57.70  ? 585  GLU   A CG  1 
ATOM   206  C CD  . GLU   A 1 48  ? -13.807 -10.178 -37.799 1.00 58.32  ? 585  GLU   A CD  1 
ATOM   207  O OE1 . GLU   A 1 48  ? -12.961 -9.617  -37.068 1.00 58.60  ? 585  GLU   A OE1 1 
ATOM   208  O OE2 . GLU   A 1 48  ? -13.782 -11.406 -38.033 1.00 58.45  ? 585  GLU   A OE2 1 
ATOM   209  N N   . GLU   A 1 49  ? -17.269 -6.495  -35.394 1.00 52.11  ? 586  GLU   A N   1 
ATOM   210  C CA  . GLU   A 1 49  ? -17.692 -5.213  -34.845 1.00 51.68  ? 586  GLU   A CA  1 
ATOM   211  C C   . GLU   A 1 49  ? -17.635 -5.168  -33.326 1.00 47.99  ? 586  GLU   A C   1 
ATOM   212  O O   . GLU   A 1 49  ? -17.726 -4.076  -32.753 1.00 47.61  ? 586  GLU   A O   1 
ATOM   213  C CB  . GLU   A 1 49  ? -19.116 -4.874  -35.305 1.00 53.48  ? 586  GLU   A CB  1 
ATOM   214  C CG  . GLU   A 1 49  ? -19.335 -4.979  -36.803 1.00 55.15  ? 586  GLU   A CG  1 
ATOM   215  C CD  . GLU   A 1 49  ? -18.393 -4.095  -37.593 1.00 57.15  ? 586  GLU   A CD  1 
ATOM   216  O OE1 . GLU   A 1 49  ? -17.982 -3.035  -37.071 1.00 57.72  ? 586  GLU   A OE1 1 
ATOM   217  O OE2 . GLU   A 1 49  ? -18.059 -4.464  -38.737 1.00 58.53  ? 586  GLU   A OE2 1 
ATOM   218  N N   . ASN   A 1 50  ? -17.486 -6.314  -32.656 1.00 44.84  ? 587  ASN   A N   1 
ATOM   219  C CA  . ASN   A 1 50  ? -17.390 -6.320  -31.204 1.00 42.16  ? 587  ASN   A CA  1 
ATOM   220  C C   . ASN   A 1 50  ? -16.207 -7.108  -30.642 1.00 40.43  ? 587  ASN   A C   1 
ATOM   221  O O   . ASN   A 1 50  ? -15.927 -6.970  -29.447 1.00 38.69  ? 587  ASN   A O   1 
ATOM   222  C CB  . ASN   A 1 50  ? -18.698 -6.843  -30.577 1.00 39.61  ? 587  ASN   A CB  1 
ATOM   223  C CG  . ASN   A 1 50  ? -19.126 -8.184  -31.136 1.00 38.60  ? 587  ASN   A CG  1 
ATOM   224  O OD1 . ASN   A 1 50  ? -18.295 -9.044  -31.432 1.00 38.25  ? 587  ASN   A OD1 1 
ATOM   225  N ND2 . ASN   A 1 50  ? -20.434 -8.373  -31.278 1.00 37.98  ? 587  ASN   A ND2 1 
ATOM   226  N N   . ILE   A 1 51  ? -15.502 -7.904  -31.443 1.00 40.07  ? 588  ILE   A N   1 
ATOM   227  C CA  . ILE   A 1 51  ? -14.325 -8.618  -30.954 1.00 39.15  ? 588  ILE   A CA  1 
ATOM   228  C C   . ILE   A 1 51  ? -13.447 -8.984  -32.144 1.00 40.95  ? 588  ILE   A C   1 
ATOM   229  O O   . ILE   A 1 51  ? -13.942 -9.343  -33.215 1.00 42.81  ? 588  ILE   A O   1 
ATOM   230  C CB  . ILE   A 1 51  ? -14.721 -9.863  -30.123 1.00 38.24  ? 588  ILE   A CB  1 
ATOM   231  C CG1 . ILE   A 1 51  ? -13.487 -10.486 -29.461 1.00 37.15  ? 588  ILE   A CG1 1 
ATOM   232  C CG2 . ILE   A 1 51  ? -15.468 -10.890 -30.979 1.00 38.82  ? 588  ILE   A CG2 1 
ATOM   233  C CD1 . ILE   A 1 51  ? -13.808 -11.615 -28.500 1.00 36.35  ? 588  ILE   A CD1 1 
ATOM   234  N N   . VAL   A 1 52  ? -12.131 -8.871  -31.949 1.00 40.99  ? 589  VAL   A N   1 
ATOM   235  C CA  . VAL   A 1 52  ? -11.131 -9.207  -32.955 1.00 40.97  ? 589  VAL   A CA  1 
ATOM   236  C C   . VAL   A 1 52  ? -10.054 -10.047 -32.283 1.00 40.96  ? 589  VAL   A C   1 
ATOM   237  O O   . VAL   A 1 52  ? -9.775  -9.894  -31.089 1.00 39.36  ? 589  VAL   A O   1 
ATOM   238  C CB  . VAL   A 1 52  ? -10.532 -7.937  -33.612 1.00 40.90  ? 589  VAL   A CB  1 
ATOM   239  C CG1 . VAL   A 1 52  ? -9.490  -8.283  -34.669 1.00 41.10  ? 589  VAL   A CG1 1 
ATOM   240  C CG2 . VAL   A 1 52  ? -11.631 -7.101  -34.234 1.00 41.77  ? 589  VAL   A CG2 1 
ATOM   241  N N   . PHE   A 1 53  ? -9.474  -10.963 -33.052 1.00 42.77  ? 590  PHE   A N   1 
ATOM   242  C CA  . PHE   A 1 53  ? -8.408  -11.829 -32.586 1.00 45.67  ? 590  PHE   A CA  1 
ATOM   243  C C   . PHE   A 1 53  ? -7.180  -11.635 -33.458 1.00 48.38  ? 590  PHE   A C   1 
ATOM   244  O O   . PHE   A 1 53  ? -7.246  -11.067 -34.554 1.00 49.49  ? 590  PHE   A O   1 
ATOM   245  C CB  . PHE   A 1 53  ? -8.812  -13.307 -32.618 1.00 46.55  ? 590  PHE   A CB  1 
ATOM   246  C CG  . PHE   A 1 53  ? -10.059 -13.613 -31.850 1.00 46.52  ? 590  PHE   A CG  1 
ATOM   247  C CD1 . PHE   A 1 53  ? -11.306 -13.355 -32.400 1.00 46.91  ? 590  PHE   A CD1 1 
ATOM   248  C CD2 . PHE   A 1 53  ? -9.989  -14.176 -30.586 1.00 45.46  ? 590  PHE   A CD2 1 
ATOM   249  C CE1 . PHE   A 1 53  ? -12.459 -13.638 -31.700 1.00 46.30  ? 590  PHE   A CE1 1 
ATOM   250  C CE2 . PHE   A 1 53  ? -11.135 -14.466 -29.881 1.00 45.25  ? 590  PHE   A CE2 1 
ATOM   251  C CZ  . PHE   A 1 53  ? -12.374 -14.197 -30.438 1.00 45.66  ? 590  PHE   A CZ  1 
ATOM   252  N N   . GLU   A 1 54  ? -6.057  -12.141 -32.967 1.00 49.27  ? 591  GLU   A N   1 
ATOM   253  C CA  . GLU   A 1 54  ? -4.806  -12.027 -33.705 1.00 52.05  ? 591  GLU   A CA  1 
ATOM   254  C C   . GLU   A 1 54  ? -4.659  -13.196 -34.668 1.00 55.17  ? 591  GLU   A C   1 
ATOM   255  O O   . GLU   A 1 54  ? -4.696  -14.358 -34.252 1.00 55.00  ? 591  GLU   A O   1 
ATOM   256  C CB  . GLU   A 1 54  ? -3.620  -11.979 -32.753 1.00 50.79  ? 591  GLU   A CB  1 
ATOM   257  C CG  . GLU   A 1 54  ? -3.599  -10.773 -31.859 1.00 49.40  ? 591  GLU   A CG  1 
ATOM   258  C CD  . GLU   A 1 54  ? -2.866  -9.646  -32.480 1.00 49.08  ? 591  GLU   A CD  1 
ATOM   259  O OE1 . GLU   A 1 54  ? -2.508  -8.726  -31.701 1.00 48.21  ? 591  GLU   A OE1 1 
ATOM   260  O OE2 . GLU   A 1 54  ? -2.677  -9.669  -33.729 1.00 49.63  ? 591  GLU   A OE2 1 
ATOM   261  N N   . ASP   A 1 55  ? -4.568  -12.889 -35.957 1.00 58.33  ? 592  ASP   A N   1 
ATOM   262  C CA  . ASP   A 1 55  ? -4.416  -13.908 -36.991 1.00 61.54  ? 592  ASP   A CA  1 
ATOM   263  C C   . ASP   A 1 55  ? -2.957  -14.352 -37.096 1.00 61.57  ? 592  ASP   A C   1 
ATOM   264  O O   . ASP   A 1 55  ? -2.075  -13.702 -36.531 1.00 61.36  ? 592  ASP   A O   1 
ATOM   265  C CB  . ASP   A 1 55  ? -4.938  -13.371 -38.326 1.00 65.36  ? 592  ASP   A CB  1 
ATOM   266  C CG  . ASP   A 1 55  ? -6.428  -13.062 -38.282 1.00 67.43  ? 592  ASP   A CG  1 
ATOM   267  O OD1 . ASP   A 1 55  ? -7.121  -13.579 -37.372 1.00 67.49  ? 592  ASP   A OD1 1 
ATOM   268  O OD2 . ASP   A 1 55  ? -6.913  -12.318 -39.161 1.00 68.64  ? 592  ASP   A OD2 1 
ATOM   269  N N   . GLY   A 1 62  ? -3.977  -24.472 -28.212 1.00 55.24  ? 599  GLY   A N   1 
ATOM   270  C CA  . GLY   A 1 62  ? -3.772  -23.035 -28.152 1.00 55.16  ? 599  GLY   A CA  1 
ATOM   271  C C   . GLY   A 1 62  ? -5.027  -22.205 -28.369 1.00 54.33  ? 599  GLY   A C   1 
ATOM   272  O O   . GLY   A 1 62  ? -5.553  -22.135 -29.480 1.00 54.53  ? 599  GLY   A O   1 
ATOM   273  N N   . ILE   A 1 63  ? -5.500  -21.565 -27.303 1.00 52.65  ? 600  ILE   A N   1 
ATOM   274  C CA  . ILE   A 1 63  ? -6.691  -20.719 -27.345 1.00 49.57  ? 600  ILE   A CA  1 
ATOM   275  C C   . ILE   A 1 63  ? -6.367  -19.439 -28.106 1.00 48.97  ? 600  ILE   A C   1 
ATOM   276  O O   . ILE   A 1 63  ? -5.202  -19.016 -28.136 1.00 49.66  ? 600  ILE   A O   1 
ATOM   277  C CB  . ILE   A 1 63  ? -7.199  -20.411 -25.928 1.00 47.63  ? 600  ILE   A CB  1 
ATOM   278  C CG1 . ILE   A 1 63  ? -6.121  -19.685 -25.126 1.00 46.93  ? 600  ILE   A CG1 1 
ATOM   279  C CG2 . ILE   A 1 63  ? -7.622  -21.689 -25.225 1.00 47.39  ? 600  ILE   A CG2 1 
ATOM   280  C CD1 . ILE   A 1 63  ? -6.275  -19.834 -23.642 1.00 46.14  ? 600  ILE   A CD1 1 
ATOM   281  N N   . PRO   A 1 64  ? -7.348  -18.794 -28.733 1.00 48.13  ? 601  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 64  ? -7.043  -17.611 -29.546 1.00 47.87  ? 601  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 64  ? -6.616  -16.420 -28.700 1.00 46.28  ? 601  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 64  ? -7.053  -16.242 -27.559 1.00 46.07  ? 601  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 64  ? -8.364  -17.331 -30.273 1.00 47.89  ? 601  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 64  ? -9.410  -17.967 -29.415 1.00 46.94  ? 601  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 64  ? -8.766  -19.185 -28.833 1.00 46.93  ? 601  PRO   A CD  1 
ATOM   288  N N   . ILE   A 1 65  ? -5.744  -15.600 -29.283 1.00 44.61  ? 602  ILE   A N   1 
ATOM   289  C CA  . ILE   A 1 65  ? -5.252  -14.385 -28.642 1.00 41.62  ? 602  ILE   A CA  1 
ATOM   290  C C   . ILE   A 1 65  ? -6.170  -13.233 -29.030 1.00 39.35  ? 602  ILE   A C   1 
ATOM   291  O O   . ILE   A 1 65  ? -6.393  -12.977 -30.219 1.00 39.45  ? 602  ILE   A O   1 
ATOM   292  C CB  . ILE   A 1 65  ? -3.801  -14.085 -29.048 1.00 42.03  ? 602  ILE   A CB  1 
ATOM   293  C CG1 . ILE   A 1 65  ? -2.988  -15.375 -29.184 1.00 41.35  ? 602  ILE   A CG1 1 
ATOM   294  C CG2 . ILE   A 1 65  ? -3.153  -13.159 -28.030 1.00 41.86  ? 602  ILE   A CG2 1 
ATOM   295  C CD1 . ILE   A 1 65  ? -2.522  -15.957 -27.871 1.00 40.12  ? 602  ILE   A CD1 1 
ATOM   296  N N   . ILE   A 1 66  ? -6.689  -12.528 -28.033 1.00 36.97  ? 603  ILE   A N   1 
ATOM   297  C CA  . ILE   A 1 66  ? -7.654  -11.463 -28.280 1.00 34.98  ? 603  ILE   A CA  1 
ATOM   298  C C   . ILE   A 1 66  ? -6.915  -10.183 -28.638 1.00 35.20  ? 603  ILE   A C   1 
ATOM   299  O O   . ILE   A 1 66  ? -6.032  -9.730  -27.900 1.00 34.58  ? 603  ILE   A O   1 
ATOM   300  C CB  . ILE   A 1 66  ? -8.554  -11.249 -27.057 1.00 32.63  ? 603  ILE   A CB  1 
ATOM   301  C CG1 . ILE   A 1 66  ? -9.327  -12.526 -26.735 1.00 30.50  ? 603  ILE   A CG1 1 
ATOM   302  C CG2 . ILE   A 1 66  ? -9.501  -10.082 -27.302 1.00 32.28  ? 603  ILE   A CG2 1 
ATOM   303  C CD1 . ILE   A 1 66  ? -10.061 -12.447 -25.436 1.00 28.59  ? 603  ILE   A CD1 1 
ATOM   304  N N   . LYS   A 1 67  ? -7.284  -9.589  -29.768 1.00 36.30  ? 604  LYS   A N   1 
ATOM   305  C CA  . LYS   A 1 67  ? -6.691  -8.329  -30.194 1.00 37.23  ? 604  LYS   A CA  1 
ATOM   306  C C   . LYS   A 1 67  ? -7.448  -7.132  -29.638 1.00 38.11  ? 604  LYS   A C   1 
ATOM   307  O O   . LYS   A 1 67  ? -6.837  -6.112  -29.302 1.00 38.82  ? 604  LYS   A O   1 
ATOM   308  C CB  . LYS   A 1 67  ? -6.646  -8.269  -31.719 1.00 38.10  ? 604  LYS   A CB  1 
ATOM   309  C CG  . LYS   A 1 67  ? -6.012  -7.028  -32.295 1.00 39.56  ? 604  LYS   A CG  1 
ATOM   310  C CD  . LYS   A 1 67  ? -5.945  -7.160  -33.808 1.00 41.58  ? 604  LYS   A CD  1 
ATOM   311  C CE  . LYS   A 1 67  ? -5.340  -5.935  -34.475 1.00 43.97  ? 604  LYS   A CE  1 
ATOM   312  N NZ  . LYS   A 1 67  ? -5.182  -6.145  -35.945 1.00 45.52  ? 604  LYS   A NZ  1 
ATOM   313  N N   . GLY   A 1 68  ? -8.764  -7.241  -29.519 1.00 37.27  ? 605  GLY   A N   1 
ATOM   314  C CA  . GLY   A 1 68  ? -9.542  -6.188  -28.898 1.00 35.96  ? 605  GLY   A CA  1 
ATOM   315  C C   . GLY   A 1 68  ? -11.012 -6.527  -28.934 1.00 35.63  ? 605  GLY   A C   1 
ATOM   316  O O   . GLY   A 1 68  ? -11.418 -7.595  -29.404 1.00 36.78  ? 605  GLY   A O   1 
ATOM   317  N N   . GLY   A 1 69  ? -11.813 -5.599  -28.422 1.00 33.57  ? 606  GLY   A N   1 
ATOM   318  C CA  . GLY   A 1 69  ? -13.250 -5.759  -28.482 1.00 31.86  ? 606  GLY   A CA  1 
ATOM   319  C C   . GLY   A 1 69  ? -13.945 -4.794  -27.546 1.00 30.11  ? 606  GLY   A C   1 
ATOM   320  O O   . GLY   A 1 69  ? -13.325 -3.893  -26.980 1.00 30.13  ? 606  GLY   A O   1 
ATOM   321  N N   . THR   A 1 70  ? -15.255 -4.988  -27.415 1.00 29.70  ? 607  THR   A N   1 
ATOM   322  C CA  . THR   A 1 70  ? -16.008 -4.263  -26.405 1.00 29.32  ? 607  THR   A CA  1 
ATOM   323  C C   . THR   A 1 70  ? -15.687 -4.825  -25.021 1.00 28.49  ? 607  THR   A C   1 
ATOM   324  O O   . THR   A 1 70  ? -15.244 -5.968  -24.875 1.00 27.69  ? 607  THR   A O   1 
ATOM   325  C CB  . THR   A 1 70  ? -17.513 -4.346  -26.677 1.00 29.70  ? 607  THR   A CB  1 
ATOM   326  O OG1 . THR   A 1 70  ? -17.972 -5.684  -26.452 1.00 29.92  ? 607  THR   A OG1 1 
ATOM   327  C CG2 . THR   A 1 70  ? -17.829 -3.940  -28.118 1.00 30.07  ? 607  THR   A CG2 1 
ATOM   328  N N   . VAL   A 1 71  ? -15.896 -3.999  -23.993 1.00 24.65  ? 608  VAL   A N   1 
ATOM   329  C CA  . VAL   A 1 71  ? -15.603 -4.470  -22.643 1.00 23.92  ? 608  VAL   A CA  1 
ATOM   330  C C   . VAL   A 1 71  ? -16.552 -5.597  -22.266 1.00 23.59  ? 608  VAL   A C   1 
ATOM   331  O O   . VAL   A 1 71  ? -16.198 -6.472  -21.467 1.00 23.10  ? 608  VAL   A O   1 
ATOM   332  C CB  . VAL   A 1 71  ? -15.647 -3.310  -21.627 1.00 29.48  ? 608  VAL   A CB  1 
ATOM   333  C CG1 . VAL   A 1 71  ? -17.075 -2.818  -21.402 1.00 28.53  ? 608  VAL   A CG1 1 
ATOM   334  C CG2 . VAL   A 1 71  ? -14.995 -3.731  -20.311 1.00 23.10  ? 608  VAL   A CG2 1 
ATOM   335  N N   . VAL   A 1 72  ? -17.748 -5.622  -22.860 1.00 26.19  ? 609  VAL   A N   1 
ATOM   336  C CA  . VAL   A 1 72  ? -18.667 -6.739  -22.654 1.00 25.95  ? 609  VAL   A CA  1 
ATOM   337  C C   . VAL   A 1 72  ? -18.071 -8.025  -23.214 1.00 25.26  ? 609  VAL   A C   1 
ATOM   338  O O   . VAL   A 1 72  ? -18.105 -9.080  -22.567 1.00 25.47  ? 609  VAL   A O   1 
ATOM   339  C CB  . VAL   A 1 72  ? -20.036 -6.433  -23.288 1.00 28.17  ? 609  VAL   A CB  1 
ATOM   340  C CG1 . VAL   A 1 72  ? -20.898 -7.691  -23.332 1.00 28.81  ? 609  VAL   A CG1 1 
ATOM   341  C CG2 . VAL   A 1 72  ? -20.741 -5.326  -22.524 1.00 28.35  ? 609  VAL   A CG2 1 
ATOM   342  N N   . LYS   A 1 73  ? -17.515 -7.957  -24.428 1.00 24.12  ? 610  LYS   A N   1 
ATOM   343  C CA  . LYS   A 1 73  ? -16.939 -9.152  -25.037 1.00 24.49  ? 610  LYS   A CA  1 
ATOM   344  C C   . LYS   A 1 73  ? -15.657 -9.580  -24.329 1.00 23.73  ? 610  LYS   A C   1 
ATOM   345  O O   . LYS   A 1 73  ? -15.361 -10.779 -24.254 1.00 23.57  ? 610  LYS   A O   1 
ATOM   346  C CB  . LYS   A 1 73  ? -16.686 -8.913  -26.527 1.00 27.40  ? 610  LYS   A CB  1 
ATOM   347  C CG  . LYS   A 1 73  ? -17.916 -9.112  -27.414 1.00 26.52  ? 610  LYS   A CG  1 
ATOM   348  C CD  . LYS   A 1 73  ? -18.333 -10.578 -27.442 1.00 25.08  ? 610  LYS   A CD  1 
ATOM   349  C CE  . LYS   A 1 73  ? -19.691 -10.765 -28.090 1.00 27.48  ? 610  LYS   A CE  1 
ATOM   350  N NZ  . LYS   A 1 73  ? -20.156 -12.183 -28.022 1.00 25.39  ? 610  LYS   A NZ  1 
ATOM   351  N N   . LEU   A 1 74  ? -14.892 -8.625  -23.797 1.00 24.07  ? 611  LEU   A N   1 
ATOM   352  C CA  . LEU   A 1 74  ? -13.707 -8.983  -23.025 1.00 24.54  ? 611  LEU   A CA  1 
ATOM   353  C C   . LEU   A 1 74  ? -14.093 -9.688  -21.729 1.00 23.79  ? 611  LEU   A C   1 
ATOM   354  O O   . LEU   A 1 74  ? -13.428 -10.644 -21.314 1.00 23.92  ? 611  LEU   A O   1 
ATOM   355  C CB  . LEU   A 1 74  ? -12.866 -7.737  -22.742 1.00 23.38  ? 611  LEU   A CB  1 
ATOM   356  C CG  . LEU   A 1 74  ? -12.306 -7.009  -23.969 1.00 26.91  ? 611  LEU   A CG  1 
ATOM   357  C CD1 . LEU   A 1 74  ? -11.667 -5.691  -23.567 1.00 24.21  ? 611  LEU   A CD1 1 
ATOM   358  C CD2 . LEU   A 1 74  ? -11.306 -7.880  -24.723 1.00 24.41  ? 611  LEU   A CD2 1 
ATOM   359  N N   . ILE   A 1 75  ? -15.174 -9.238  -21.087 1.00 23.61  ? 612  ILE   A N   1 
ATOM   360  C CA  . ILE   A 1 75  ? -15.679 -9.904  -19.887 1.00 24.16  ? 612  ILE   A CA  1 
ATOM   361  C C   . ILE   A 1 75  ? -16.145 -11.322 -20.209 1.00 25.59  ? 612  ILE   A C   1 
ATOM   362  O O   . ILE   A 1 75  ? -15.926 -12.257 -19.427 1.00 25.18  ? 612  ILE   A O   1 
ATOM   363  C CB  . ILE   A 1 75  ? -16.806 -9.062  -19.255 1.00 24.45  ? 612  ILE   A CB  1 
ATOM   364  C CG1 . ILE   A 1 75  ? -16.237 -7.772  -18.657 1.00 24.12  ? 612  ILE   A CG1 1 
ATOM   365  C CG2 . ILE   A 1 75  ? -17.577 -9.862  -18.204 1.00 21.91  ? 612  ILE   A CG2 1 
ATOM   366  C CD1 . ILE   A 1 75  ? -15.236 -7.996  -17.543 1.00 21.57  ? 612  ILE   A CD1 1 
ATOM   367  N N   . GLU   A 1 76  ? -16.797 -11.506 -21.361 1.00 27.23  ? 613  GLU   A N   1 
ATOM   368  C CA  . GLU   A 1 76  ? -17.254 -12.836 -21.753 1.00 27.81  ? 613  GLU   A CA  1 
ATOM   369  C C   . GLU   A 1 76  ? -16.077 -13.788 -21.933 1.00 27.12  ? 613  GLU   A C   1 
ATOM   370  O O   . GLU   A 1 76  ? -16.055 -14.885 -21.364 1.00 26.86  ? 613  GLU   A O   1 
ATOM   371  C CB  . GLU   A 1 76  ? -18.083 -12.753 -23.036 1.00 29.44  ? 613  GLU   A CB  1 
ATOM   372  C CG  . GLU   A 1 76  ? -18.927 -13.991 -23.302 1.00 30.69  ? 613  GLU   A CG  1 
ATOM   373  C CD  . GLU   A 1 76  ? -19.238 -14.197 -24.773 1.00 32.85  ? 613  GLU   A CD  1 
ATOM   374  O OE1 . GLU   A 1 76  ? -19.340 -13.195 -25.512 1.00 33.33  ? 613  GLU   A OE1 1 
ATOM   375  O OE2 . GLU   A 1 76  ? -19.376 -15.367 -25.191 1.00 33.74  ? 613  GLU   A OE2 1 
ATOM   376  N N   . ARG   A 1 77  ? -15.082 -13.384 -22.721 1.00 27.34  ? 614  ARG   A N   1 
ATOM   377  C CA  . ARG   A 1 77  ? -13.910 -14.231 -22.916 1.00 26.48  ? 614  ARG   A CA  1 
ATOM   378  C C   . ARG   A 1 77  ? -13.088 -14.360 -21.638 1.00 25.65  ? 614  ARG   A C   1 
ATOM   379  O O   . ARG   A 1 77  ? -12.361 -15.348 -21.465 1.00 23.92  ? 614  ARG   A O   1 
ATOM   380  C CB  . ARG   A 1 77  ? -13.056 -13.665 -24.048 1.00 27.35  ? 614  ARG   A CB  1 
ATOM   381  C CG  . ARG   A 1 77  ? -13.730 -13.723 -25.403 1.00 28.05  ? 614  ARG   A CG  1 
ATOM   382  C CD  . ARG   A 1 77  ? -13.551 -15.091 -26.022 1.00 28.64  ? 614  ARG   A CD  1 
ATOM   383  N NE  . ARG   A 1 77  ? -14.393 -15.272 -27.194 1.00 29.43  ? 614  ARG   A NE  1 
ATOM   384  C CZ  . ARG   A 1 77  ? -14.199 -16.213 -28.110 1.00 29.44  ? 614  ARG   A CZ  1 
ATOM   385  N NH1 . ARG   A 1 77  ? -15.021 -16.306 -29.147 1.00 30.77  ? 614  ARG   A NH1 1 
ATOM   386  N NH2 . ARG   A 1 77  ? -13.179 -17.054 -27.991 1.00 28.15  ? 614  ARG   A NH2 1 
ATOM   387  N N   . LEU   A 1 78  ? -13.178 -13.366 -20.743 1.00 25.74  ? 615  LEU   A N   1 
ATOM   388  C CA  . LEU   A 1 78  ? -12.549 -13.480 -19.433 1.00 25.48  ? 615  LEU   A CA  1 
ATOM   389  C C   . LEU   A 1 78  ? -13.146 -14.627 -18.636 1.00 26.40  ? 615  LEU   A C   1 
ATOM   390  O O   . LEU   A 1 78  ? -12.468 -15.220 -17.790 1.00 21.72  ? 615  LEU   A O   1 
ATOM   391  C CB  . LEU   A 1 78  ? -12.700 -12.165 -18.667 1.00 25.24  ? 615  LEU   A CB  1 
ATOM   392  C CG  . LEU   A 1 78  ? -12.004 -12.034 -17.308 1.00 26.05  ? 615  LEU   A CG  1 
ATOM   393  C CD1 . LEU   A 1 78  ? -10.486 -12.122 -17.453 1.00 26.11  ? 615  LEU   A CD1 1 
ATOM   394  C CD2 . LEU   A 1 78  ? -12.400 -10.729 -16.644 1.00 25.65  ? 615  LEU   A CD2 1 
ATOM   395  N N   . THR   A 1 79  ? -14.408 -14.951 -18.895 1.00 25.75  ? 616  THR   A N   1 
ATOM   396  C CA  . THR   A 1 79  ? -15.148 -15.978 -18.180 1.00 24.82  ? 616  THR   A CA  1 
ATOM   397  C C   . THR   A 1 79  ? -15.798 -16.934 -19.169 1.00 25.62  ? 616  THR   A C   1 
ATOM   398  O O   . THR   A 1 79  ? -16.954 -17.337 -19.012 1.00 25.83  ? 616  THR   A O   1 
ATOM   399  C CB  . THR   A 1 79  ? -16.177 -15.337 -17.248 1.00 24.97  ? 616  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 79  ? -16.991 -14.412 -17.980 1.00 21.86  ? 616  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 79  ? -15.468 -14.578 -16.135 1.00 21.38  ? 616  THR   A CG2 1 
ATOM   402  N N   . TYR   A 1 80  ? -15.045 -17.307 -20.205 1.00 26.44  ? 617  TYR   A N   1 
ATOM   403  C CA  . TYR   A 1 80  ? -15.559 -18.153 -21.274 1.00 27.98  ? 617  TYR   A CA  1 
ATOM   404  C C   . TYR   A 1 80  ? -15.925 -19.532 -20.740 1.00 30.19  ? 617  TYR   A C   1 
ATOM   405  O O   . TYR   A 1 80  ? -15.235 -20.085 -19.878 1.00 30.27  ? 617  TYR   A O   1 
ATOM   406  C CB  . TYR   A 1 80  ? -14.508 -18.277 -22.376 1.00 29.72  ? 617  TYR   A CB  1 
ATOM   407  C CG  . TYR   A 1 80  ? -15.050 -18.509 -23.765 1.00 30.02  ? 617  TYR   A CG  1 
ATOM   408  C CD1 . TYR   A 1 80  ? -16.028 -17.682 -24.298 1.00 30.86  ? 617  TYR   A CD1 1 
ATOM   409  C CD2 . TYR   A 1 80  ? -14.557 -19.532 -24.553 1.00 30.63  ? 617  TYR   A CD2 1 
ATOM   410  C CE1 . TYR   A 1 80  ? -16.519 -17.888 -25.573 1.00 32.32  ? 617  TYR   A CE1 1 
ATOM   411  C CE2 . TYR   A 1 80  ? -15.035 -19.743 -25.827 1.00 32.32  ? 617  TYR   A CE2 1 
ATOM   412  C CZ  . TYR   A 1 80  ? -16.016 -18.921 -26.334 1.00 33.28  ? 617  TYR   A CZ  1 
ATOM   413  O OH  . TYR   A 1 80  ? -16.487 -19.142 -27.609 1.00 34.56  ? 617  TYR   A OH  1 
ATOM   414  N N   . HIS   A 1 81  ? -17.022 -20.088 -21.260 1.00 32.62  ? 618  HIS   A N   1 
ATOM   415  C CA  . HIS   A 1 81  ? -17.530 -21.366 -20.773 1.00 33.46  ? 618  HIS   A CA  1 
ATOM   416  C C   . HIS   A 1 81  ? -16.828 -22.567 -21.389 1.00 33.38  ? 618  HIS   A C   1 
ATOM   417  O O   . HIS   A 1 81  ? -16.840 -23.644 -20.785 1.00 33.62  ? 618  HIS   A O   1 
ATOM   418  C CB  . HIS   A 1 81  ? -19.033 -21.480 -21.045 1.00 35.90  ? 618  HIS   A CB  1 
ATOM   419  C CG  . HIS   A 1 81  ? -19.383 -21.641 -22.494 1.00 37.74  ? 618  HIS   A CG  1 
ATOM   420  N ND1 . HIS   A 1 81  ? -19.422 -20.580 -23.374 1.00 37.90  ? 618  HIS   A ND1 1 
ATOM   421  C CD2 . HIS   A 1 81  ? -19.734 -22.736 -23.211 1.00 38.46  ? 618  HIS   A CD2 1 
ATOM   422  C CE1 . HIS   A 1 81  ? -19.772 -21.016 -24.571 1.00 38.03  ? 618  HIS   A CE1 1 
ATOM   423  N NE2 . HIS   A 1 81  ? -19.966 -22.320 -24.499 1.00 38.56  ? 618  HIS   A NE2 1 
ATOM   424  N N   A MET   A 1 82  ? -16.214 -22.410 -22.564 0.55 33.44  ? 619  MET   A N   1 
ATOM   425  N N   B MET   A 1 82  ? -16.231 -22.411 -22.573 0.45 33.43  ? 619  MET   A N   1 
ATOM   426  C CA  A MET   A 1 82  ? -15.635 -23.555 -23.257 0.55 34.16  ? 619  MET   A CA  1 
ATOM   427  C CA  B MET   A 1 82  ? -15.624 -23.551 -23.252 0.45 34.57  ? 619  MET   A CA  1 
ATOM   428  C C   A MET   A 1 82  ? -14.307 -23.997 -22.655 0.55 33.96  ? 619  MET   A C   1 
ATOM   429  C C   B MET   A 1 82  ? -14.360 -24.017 -22.542 0.45 33.94  ? 619  MET   A C   1 
ATOM   430  O O   A MET   A 1 82  ? -13.971 -25.184 -22.733 0.55 35.11  ? 619  MET   A O   1 
ATOM   431  O O   B MET   A 1 82  ? -14.119 -25.224 -22.425 0.45 35.06  ? 619  MET   A O   1 
ATOM   432  C CB  A MET   A 1 82  ? -15.457 -23.237 -24.741 0.55 34.24  ? 619  MET   A CB  1 
ATOM   433  C CB  B MET   A 1 82  ? -15.320 -23.194 -24.705 0.45 34.22  ? 619  MET   A CB  1 
ATOM   434  C CG  A MET   A 1 82  ? -16.681 -23.558 -25.588 0.55 35.33  ? 619  MET   A CG  1 
ATOM   435  C CG  B MET   A 1 82  ? -16.554 -23.041 -25.578 0.45 35.12  ? 619  MET   A CG  1 
ATOM   436  S SD  A MET   A 1 82  ? -16.444 -23.239 -27.349 0.55 35.73  ? 619  MET   A SD  1 
ATOM   437  S SD  B MET   A 1 82  ? -17.466 -24.589 -25.757 0.45 35.62  ? 619  MET   A SD  1 
ATOM   438  C CE  A MET   A 1 82  ? -17.860 -24.097 -28.037 0.55 36.97  ? 619  MET   A CE  1 
ATOM   439  C CE  B MET   A 1 82  ? -16.240 -25.615 -26.563 0.45 34.37  ? 619  MET   A CE  1 
ATOM   440  N N   . TYR   A 1 83  ? -13.548 -23.083 -22.057 1.00 33.46  ? 620  TYR   A N   1 
ATOM   441  C CA  . TYR   A 1 83  ? -12.255 -23.423 -21.472 1.00 32.85  ? 620  TYR   A CA  1 
ATOM   442  C C   . TYR   A 1 83  ? -11.809 -22.294 -20.551 1.00 32.78  ? 620  TYR   A C   1 
ATOM   443  O O   . TYR   A 1 83  ? -12.336 -21.179 -20.596 1.00 31.86  ? 620  TYR   A O   1 
ATOM   444  C CB  . TYR   A 1 83  ? -11.209 -23.665 -22.564 1.00 32.48  ? 620  TYR   A CB  1 
ATOM   445  C CG  . TYR   A 1 83  ? -11.220 -22.579 -23.617 1.00 31.65  ? 620  TYR   A CG  1 
ATOM   446  C CD1 . TYR   A 1 83  ? -10.700 -21.317 -23.350 1.00 30.89  ? 620  TYR   A CD1 1 
ATOM   447  C CD2 . TYR   A 1 83  ? -11.764 -22.808 -24.868 1.00 31.43  ? 620  TYR   A CD2 1 
ATOM   448  C CE1 . TYR   A 1 83  ? -10.721 -20.321 -24.298 1.00 30.32  ? 620  TYR   A CE1 1 
ATOM   449  C CE2 . TYR   A 1 83  ? -11.787 -21.818 -25.823 1.00 31.63  ? 620  TYR   A CE2 1 
ATOM   450  C CZ  . TYR   A 1 83  ? -11.262 -20.576 -25.534 1.00 30.85  ? 620  TYR   A CZ  1 
ATOM   451  O OH  . TYR   A 1 83  ? -11.281 -19.581 -26.484 1.00 30.70  ? 620  TYR   A OH  1 
ATOM   452  N N   . ALA   A 1 84  ? -10.803 -22.596 -19.731 1.00 33.19  ? 621  ALA   A N   1 
ATOM   453  C CA  . ALA   A 1 84  ? -10.131 -21.584 -18.933 1.00 32.78  ? 621  ALA   A CA  1 
ATOM   454  C C   . ALA   A 1 84  ? -9.046  -20.892 -19.755 1.00 32.89  ? 621  ALA   A C   1 
ATOM   455  O O   . ALA   A 1 84  ? -8.579  -21.401 -20.777 1.00 33.46  ? 621  ALA   A O   1 
ATOM   456  C CB  . ALA   A 1 84  ? -9.521  -22.201 -17.675 1.00 32.98  ? 621  ALA   A CB  1 
ATOM   457  N N   . ASP   A 1 85  ? -8.647  -19.711 -19.292 1.00 32.25  ? 622  ASP   A N   1 
ATOM   458  C CA  . ASP   A 1 85  ? -7.683  -18.870 -19.999 1.00 30.39  ? 622  ASP   A CA  1 
ATOM   459  C C   . ASP   A 1 85  ? -6.855  -18.134 -18.957 1.00 29.25  ? 622  ASP   A C   1 
ATOM   460  O O   . ASP   A 1 85  ? -7.040  -16.935 -18.719 1.00 28.29  ? 622  ASP   A O   1 
ATOM   461  C CB  . ASP   A 1 85  ? -8.404  -17.906 -20.945 1.00 29.52  ? 622  ASP   A CB  1 
ATOM   462  C CG  . ASP   A 1 85  ? -7.471  -17.251 -21.936 1.00 30.64  ? 622  ASP   A CG  1 
ATOM   463  O OD1 . ASP   A 1 85  ? -6.244  -17.335 -21.743 1.00 31.76  ? 622  ASP   A OD1 1 
ATOM   464  O OD2 . ASP   A 1 85  ? -7.963  -16.656 -22.923 1.00 31.79  ? 622  ASP   A OD2 1 
ATOM   465  N N   . PRO   A 1 86  ? -5.917  -18.833 -18.312 1.00 27.91  ? 623  PRO   A N   1 
ATOM   466  C CA  . PRO   A 1 86  ? -5.147  -18.201 -17.223 1.00 27.17  ? 623  PRO   A CA  1 
ATOM   467  C C   . PRO   A 1 86  ? -4.284  -17.021 -17.651 1.00 26.69  ? 623  PRO   A C   1 
ATOM   468  O O   . PRO   A 1 86  ? -4.069  -16.110 -16.847 1.00 25.90  ? 623  PRO   A O   1 
ATOM   469  C CB  . PRO   A 1 86  ? -4.278  -19.353 -16.695 1.00 28.75  ? 623  PRO   A CB  1 
ATOM   470  C CG  . PRO   A 1 86  ? -4.247  -20.377 -17.816 1.00 28.62  ? 623  PRO   A CG  1 
ATOM   471  C CD  . PRO   A 1 86  ? -5.571  -20.256 -18.500 1.00 28.76  ? 623  PRO   A CD  1 
ATOM   472  N N   . ASN   A 1 87  ? -3.770  -16.998 -18.880 1.00 27.48  ? 624  ASN   A N   1 
ATOM   473  C CA  . ASN   A 1 87  ? -2.952  -15.861 -19.304 1.00 28.83  ? 624  ASN   A CA  1 
ATOM   474  C C   . ASN   A 1 87  ? -3.810  -14.626 -19.557 1.00 26.92  ? 624  ASN   A C   1 
ATOM   475  O O   . ASN   A 1 87  ? -3.392  -13.500 -19.257 1.00 27.07  ? 624  ASN   A O   1 
ATOM   476  C CB  . ASN   A 1 87  ? -2.127  -16.230 -20.544 1.00 31.20  ? 624  ASN   A CB  1 
ATOM   477  C CG  . ASN   A 1 87  ? -1.163  -17.381 -20.272 1.00 33.57  ? 624  ASN   A CG  1 
ATOM   478  O OD1 . ASN   A 1 87  ? -0.617  -17.499 -19.170 1.00 32.69  ? 624  ASN   A OD1 1 
ATOM   479  N ND2 . ASN   A 1 87  ? -0.956  -18.236 -21.267 1.00 35.85  ? 624  ASN   A ND2 1 
ATOM   480  N N   . PHE   A 1 88  ? -5.028  -14.815 -20.066 1.00 24.66  ? 625  PHE   A N   1 
ATOM   481  C CA  . PHE   A 1 88  ? -5.897  -13.662 -20.291 1.00 23.73  ? 625  PHE   A CA  1 
ATOM   482  C C   . PHE   A 1 88  ? -6.411  -13.087 -18.972 1.00 22.07  ? 625  PHE   A C   1 
ATOM   483  O O   . PHE   A 1 88  ? -6.551  -11.865 -18.837 1.00 21.74  ? 625  PHE   A O   1 
ATOM   484  C CB  . PHE   A 1 88  ? -7.054  -14.044 -21.217 1.00 22.48  ? 625  PHE   A CB  1 
ATOM   485  C CG  . PHE   A 1 88  ? -7.973  -12.904 -21.538 1.00 23.95  ? 625  PHE   A CG  1 
ATOM   486  C CD1 . PHE   A 1 88  ? -7.472  -11.708 -22.029 1.00 25.00  ? 625  PHE   A CD1 1 
ATOM   487  C CD2 . PHE   A 1 88  ? -9.341  -13.029 -21.358 1.00 23.03  ? 625  PHE   A CD2 1 
ATOM   488  C CE1 . PHE   A 1 88  ? -8.323  -10.655 -22.324 1.00 24.50  ? 625  PHE   A CE1 1 
ATOM   489  C CE2 . PHE   A 1 88  ? -10.191 -11.985 -21.651 1.00 22.71  ? 625  PHE   A CE2 1 
ATOM   490  C CZ  . PHE   A 1 88  ? -9.684  -10.794 -22.135 1.00 23.01  ? 625  PHE   A CZ  1 
ATOM   491  N N   . VAL   A 1 89  ? -6.679  -13.951 -17.987 1.00 20.46  ? 626  VAL   A N   1 
ATOM   492  C CA  . VAL   A 1 89  ? -7.129  -13.498 -16.671 1.00 19.65  ? 626  VAL   A CA  1 
ATOM   493  C C   . VAL   A 1 89  ? -6.049  -12.664 -15.991 1.00 21.39  ? 626  VAL   A C   1 
ATOM   494  O O   . VAL   A 1 89  ? -6.319  -11.584 -15.452 1.00 20.80  ? 626  VAL   A O   1 
ATOM   495  C CB  . VAL   A 1 89  ? -7.532  -14.703 -15.799 1.00 19.78  ? 626  VAL   A CB  1 
ATOM   496  C CG1 . VAL   A 1 89  ? -7.726  -14.280 -14.345 1.00 19.36  ? 626  VAL   A CG1 1 
ATOM   497  C CG2 . VAL   A 1 89  ? -8.792  -15.363 -16.341 1.00 19.06  ? 626  VAL   A CG2 1 
ATOM   498  N N   . ARG   A 1 90  ? -4.811  -13.159 -15.986 1.00 24.63  ? 627  ARG   A N   1 
ATOM   499  C CA  . ARG   A 1 90  ? -3.734  -12.422 -15.329 1.00 26.42  ? 627  ARG   A CA  1 
ATOM   500  C C   . ARG   A 1 90  ? -3.516  -11.067 -15.995 1.00 26.45  ? 627  ARG   A C   1 
ATOM   501  O O   . ARG   A 1 90  ? -3.489  -10.030 -15.325 1.00 22.69  ? 627  ARG   A O   1 
ATOM   502  C CB  . ARG   A 1 90  ? -2.447  -13.246 -15.349 1.00 28.28  ? 627  ARG   A CB  1 
ATOM   503  C CG  . ARG   A 1 90  ? -1.317  -12.677 -14.503 1.00 29.66  ? 627  ARG   A CG  1 
ATOM   504  C CD  . ARG   A 1 90  ? 0.040   -12.987 -15.115 1.00 31.84  ? 627  ARG   A CD  1 
ATOM   505  N NE  . ARG   A 1 90  ? 0.126   -14.354 -15.618 1.00 34.35  ? 627  ARG   A NE  1 
ATOM   506  C CZ  . ARG   A 1 90  ? 0.191   -14.676 -16.908 1.00 36.04  ? 627  ARG   A CZ  1 
ATOM   507  N NH1 . ARG   A 1 90  ? 0.262   -15.951 -17.275 1.00 37.03  ? 627  ARG   A NH1 1 
ATOM   508  N NH2 . ARG   A 1 90  ? 0.190   -13.722 -17.831 1.00 35.47  ? 627  ARG   A NH2 1 
ATOM   509  N N   . THR   A 1 91  ? -3.380  -11.060 -17.324 1.00 25.17  ? 628  THR   A N   1 
ATOM   510  C CA  . THR   A 1 91  ? -3.120  -9.817  -18.041 1.00 25.17  ? 628  THR   A CA  1 
ATOM   511  C C   . THR   A 1 91  ? -4.282  -8.840  -17.908 1.00 25.07  ? 628  THR   A C   1 
ATOM   512  O O   . THR   A 1 91  ? -4.068  -7.634  -17.719 1.00 24.71  ? 628  THR   A O   1 
ATOM   513  C CB  . THR   A 1 91  ? -2.842  -10.116 -19.509 1.00 25.43  ? 628  THR   A CB  1 
ATOM   514  O OG1 . THR   A 1 91  ? -1.824  -11.117 -19.599 1.00 27.77  ? 628  THR   A OG1 1 
ATOM   515  C CG2 . THR   A 1 91  ? -2.378  -8.866  -20.225 1.00 26.40  ? 628  THR   A CG2 1 
ATOM   516  N N   . PHE   A 1 92  ? -5.518  -9.337  -18.015 1.00 24.42  ? 629  PHE   A N   1 
ATOM   517  C CA  . PHE   A 1 92  ? -6.680  -8.473  -17.823 1.00 23.95  ? 629  PHE   A CA  1 
ATOM   518  C C   . PHE   A 1 92  ? -6.630  -7.793  -16.462 1.00 23.97  ? 629  PHE   A C   1 
ATOM   519  O O   . PHE   A 1 92  ? -6.746  -6.567  -16.362 1.00 23.18  ? 629  PHE   A O   1 
ATOM   520  C CB  . PHE   A 1 92  ? -7.966  -9.287  -17.973 1.00 23.81  ? 629  PHE   A CB  1 
ATOM   521  C CG  . PHE   A 1 92  ? -9.224  -8.470  -17.885 1.00 24.17  ? 629  PHE   A CG  1 
ATOM   522  C CD1 . PHE   A 1 92  ? -9.834  -8.241  -16.665 1.00 23.52  ? 629  PHE   A CD1 1 
ATOM   523  C CD2 . PHE   A 1 92  ? -9.809  -7.945  -19.027 1.00 24.56  ? 629  PHE   A CD2 1 
ATOM   524  C CE1 . PHE   A 1 92  ? -10.991 -7.493  -16.584 1.00 22.67  ? 629  PHE   A CE1 1 
ATOM   525  C CE2 . PHE   A 1 92  ? -10.969 -7.197  -18.948 1.00 23.74  ? 629  PHE   A CE2 1 
ATOM   526  C CZ  . PHE   A 1 92  ? -11.558 -6.974  -17.725 1.00 22.92  ? 629  PHE   A CZ  1 
ATOM   527  N N   . LEU   A 1 93  ? -6.429  -8.575  -15.400 1.00 20.33  ? 630  LEU   A N   1 
ATOM   528  C CA  . LEU   A 1 93  ? -6.499  -8.020  -14.055 1.00 20.44  ? 630  LEU   A CA  1 
ATOM   529  C C   . LEU   A 1 93  ? -5.325  -7.100  -13.728 1.00 26.76  ? 630  LEU   A C   1 
ATOM   530  O O   . LEU   A 1 93  ? -5.426  -6.295  -12.797 1.00 26.43  ? 630  LEU   A O   1 
ATOM   531  C CB  . LEU   A 1 93  ? -6.615  -9.161  -13.049 1.00 23.92  ? 630  LEU   A CB  1 
ATOM   532  C CG  . LEU   A 1 93  ? -8.059  -9.687  -13.098 1.00 23.80  ? 630  LEU   A CG  1 
ATOM   533  C CD1 . LEU   A 1 93  ? -8.282  -10.912 -12.229 1.00 24.26  ? 630  LEU   A CD1 1 
ATOM   534  C CD2 . LEU   A 1 93  ? -9.042  -8.575  -12.723 1.00 18.86  ? 630  LEU   A CD2 1 
ATOM   535  N N   . THR   A 1 94  ? -4.231  -7.181  -14.483 1.00 26.98  ? 631  THR   A N   1 
ATOM   536  C CA  . THR   A 1 94  ? -3.141  -6.226  -14.328 1.00 28.57  ? 631  THR   A CA  1 
ATOM   537  C C   . THR   A 1 94  ? -3.408  -4.927  -15.086 1.00 28.59  ? 631  THR   A C   1 
ATOM   538  O O   . THR   A 1 94  ? -3.008  -3.851  -14.626 1.00 32.13  ? 631  THR   A O   1 
ATOM   539  C CB  . THR   A 1 94  ? -1.831  -6.876  -14.790 1.00 30.93  ? 631  THR   A CB  1 
ATOM   540  O OG1 . THR   A 1 94  ? -1.408  -7.833  -13.808 1.00 32.54  ? 631  THR   A OG1 1 
ATOM   541  C CG2 . THR   A 1 94  ? -0.728  -5.849  -15.005 1.00 31.25  ? 631  THR   A CG2 1 
ATOM   542  N N   . THR   A 1 95  ? -4.124  -4.992  -16.209 1.00 27.02  ? 632  THR   A N   1 
ATOM   543  C CA  . THR   A 1 95  ? -4.215  -3.869  -17.131 1.00 27.71  ? 632  THR   A CA  1 
ATOM   544  C C   . THR   A 1 95  ? -5.598  -3.232  -17.231 1.00 27.70  ? 632  THR   A C   1 
ATOM   545  O O   . THR   A 1 95  ? -5.716  -2.175  -17.864 1.00 28.14  ? 632  THR   A O   1 
ATOM   546  C CB  . THR   A 1 95  ? -3.791  -4.320  -18.535 1.00 30.28  ? 632  THR   A CB  1 
ATOM   547  O OG1 . THR   A 1 95  ? -4.679  -5.351  -18.984 1.00 23.25  ? 632  THR   A OG1 1 
ATOM   548  C CG2 . THR   A 1 95  ? -2.358  -4.850  -18.519 1.00 25.59  ? 632  THR   A CG2 1 
ATOM   549  N N   . TYR   A 1 96  ? -6.639  -3.829  -16.633 1.00 26.24  ? 633  TYR   A N   1 
ATOM   550  C CA  . TYR   A 1 96  ? -8.010  -3.430  -16.958 1.00 26.14  ? 633  TYR   A CA  1 
ATOM   551  C C   . TYR   A 1 96  ? -8.285  -1.971  -16.616 1.00 26.69  ? 633  TYR   A C   1 
ATOM   552  O O   . TYR   A 1 96  ? -9.087  -1.315  -17.293 1.00 27.51  ? 633  TYR   A O   1 
ATOM   553  C CB  . TYR   A 1 96  ? -9.024  -4.334  -16.246 1.00 25.52  ? 633  TYR   A CB  1 
ATOM   554  C CG  . TYR   A 1 96  ? -9.236  -4.024  -14.779 1.00 20.25  ? 633  TYR   A CG  1 
ATOM   555  C CD1 . TYR   A 1 96  ? -10.179 -3.088  -14.369 1.00 26.61  ? 633  TYR   A CD1 1 
ATOM   556  C CD2 . TYR   A 1 96  ? -8.510  -4.687  -13.801 1.00 23.60  ? 633  TYR   A CD2 1 
ATOM   557  C CE1 . TYR   A 1 96  ? -10.372 -2.811  -13.025 1.00 28.00  ? 633  TYR   A CE1 1 
ATOM   558  C CE2 . TYR   A 1 96  ? -8.699  -4.418  -12.459 1.00 20.54  ? 633  TYR   A CE2 1 
ATOM   559  C CZ  . TYR   A 1 96  ? -9.625  -3.482  -12.077 1.00 20.64  ? 633  TYR   A CZ  1 
ATOM   560  O OH  . TYR   A 1 96  ? -9.801  -3.219  -10.742 1.00 21.03  ? 633  TYR   A OH  1 
ATOM   561  N N   . ARG   A 1 97  ? -7.631  -1.445  -15.581 1.00 26.05  ? 634  ARG   A N   1 
ATOM   562  C CA  . ARG   A 1 97  ? -7.882  -0.084  -15.129 1.00 26.46  ? 634  ARG   A CA  1 
ATOM   563  C C   . ARG   A 1 97  ? -7.633  0.956   -16.213 1.00 27.74  ? 634  ARG   A C   1 
ATOM   564  O O   . ARG   A 1 97  ? -8.080  2.097   -16.068 1.00 30.34  ? 634  ARG   A O   1 
ATOM   565  C CB  . ARG   A 1 97  ? -7.026  0.191   -13.892 1.00 26.60  ? 634  ARG   A CB  1 
ATOM   566  C CG  . ARG   A 1 97  ? -7.314  -0.808  -12.780 1.00 25.63  ? 634  ARG   A CG  1 
ATOM   567  C CD  . ARG   A 1 97  ? -6.244  -0.820  -11.711 1.00 26.65  ? 634  ARG   A CD  1 
ATOM   568  N NE  . ARG   A 1 97  ? -6.372  -1.975  -10.822 1.00 25.49  ? 634  ARG   A NE  1 
ATOM   569  C CZ  . ARG   A 1 97  ? -5.894  -3.186  -11.095 1.00 24.63  ? 634  ARG   A CZ  1 
ATOM   570  N NH1 . ARG   A 1 97  ? -5.263  -3.410  -12.239 1.00 25.22  ? 634  ARG   A NH1 1 
ATOM   571  N NH2 . ARG   A 1 97  ? -6.048  -4.176  -10.227 1.00 22.83  ? 634  ARG   A NH2 1 
ATOM   572  N N   . SER   A 1 98  ? -6.960  0.597   -17.298 1.00 27.18  ? 635  SER   A N   1 
ATOM   573  C CA  . SER   A 1 98  ? -6.771  1.520   -18.406 1.00 28.66  ? 635  SER   A CA  1 
ATOM   574  C C   . SER   A 1 98  ? -7.985  1.606   -19.323 1.00 30.95  ? 635  SER   A C   1 
ATOM   575  O O   . SER   A 1 98  ? -7.972  2.412   -20.261 1.00 33.14  ? 635  SER   A O   1 
ATOM   576  C CB  . SER   A 1 98  ? -5.542  1.112   -19.220 1.00 29.18  ? 635  SER   A CB  1 
ATOM   577  O OG  . SER   A 1 98  ? -5.736  -0.151  -19.825 1.00 25.78  ? 635  SER   A OG  1 
ATOM   578  N N   . PHE   A 1 99  ? -9.027  0.797   -19.089 1.00 30.18  ? 636  PHE   A N   1 
ATOM   579  C CA  . PHE   A 1 99  ? -10.222 0.873   -19.920 1.00 30.08  ? 636  PHE   A CA  1 
ATOM   580  C C   . PHE   A 1 99  ? -11.511 0.597   -19.154 1.00 28.41  ? 636  PHE   A C   1 
ATOM   581  O O   . PHE   A 1 99  ? -12.569 0.494   -19.786 1.00 28.44  ? 636  PHE   A O   1 
ATOM   582  C CB  . PHE   A 1 99  ? -10.128 -0.091  -21.126 1.00 30.29  ? 636  PHE   A CB  1 
ATOM   583  C CG  . PHE   A 1 99  ? -9.906  -1.546  -20.753 1.00 30.26  ? 636  PHE   A CG  1 
ATOM   584  C CD1 . PHE   A 1 99  ? -10.937 -2.320  -20.238 1.00 28.19  ? 636  PHE   A CD1 1 
ATOM   585  C CD2 . PHE   A 1 99  ? -8.671  -2.146  -20.956 1.00 30.51  ? 636  PHE   A CD2 1 
ATOM   586  C CE1 . PHE   A 1 99  ? -10.729 -3.646  -19.908 1.00 27.52  ? 636  PHE   A CE1 1 
ATOM   587  C CE2 . PHE   A 1 99  ? -8.459  -3.478  -20.629 1.00 29.28  ? 636  PHE   A CE2 1 
ATOM   588  C CZ  . PHE   A 1 99  ? -9.490  -4.226  -20.106 1.00 28.23  ? 636  PHE   A CZ  1 
ATOM   589  N N   . CYS   A 1 100 ? -11.467 0.485   -17.827 1.00 26.72  ? 637  CYS   A N   1 
ATOM   590  C CA  . CYS   A 1 100 ? -12.638 0.063   -17.074 1.00 25.41  ? 637  CYS   A CA  1 
ATOM   591  C C   . CYS   A 1 100 ? -12.407 0.329   -15.596 1.00 27.22  ? 637  CYS   A C   1 
ATOM   592  O O   . CYS   A 1 100 ? -11.309 0.102   -15.086 1.00 29.45  ? 637  CYS   A O   1 
ATOM   593  C CB  . CYS   A 1 100 ? -12.925 -1.426  -17.305 1.00 23.83  ? 637  CYS   A CB  1 
ATOM   594  S SG  . CYS   A 1 100 ? -14.335 -2.038  -16.383 1.00 24.38  ? 637  CYS   A SG  1 
ATOM   595  N N   . LYS   A 1 101 ? -13.441 0.793   -14.920 1.00 27.79  ? 638  LYS   A N   1 
ATOM   596  C CA  . LYS   A 1 101 ? -13.292 1.128   -13.514 1.00 28.06  ? 638  LYS   A CA  1 
ATOM   597  C C   . LYS   A 1 101 ? -13.449 -0.114  -12.639 1.00 25.16  ? 638  LYS   A C   1 
ATOM   598  O O   . LYS   A 1 101 ? -14.152 -1.057  -13.010 1.00 24.06  ? 638  LYS   A O   1 
ATOM   599  C CB  . LYS   A 1 101 ? -14.322 2.173   -13.099 1.00 31.37  ? 638  LYS   A CB  1 
ATOM   600  C CG  . LYS   A 1 101 ? -13.964 3.597   -13.464 1.00 34.70  ? 638  LYS   A CG  1 
ATOM   601  C CD  . LYS   A 1 101 ? -14.982 4.567   -12.896 1.00 38.52  ? 638  LYS   A CD  1 
ATOM   602  C CE  . LYS   A 1 101 ? -14.692 6.000   -13.335 1.00 43.48  ? 638  LYS   A CE  1 
ATOM   603  N NZ  . LYS   A 1 101 ? -15.771 6.948   -12.920 1.00 46.00  ? 638  LYS   A NZ  1 
ATOM   604  N N   . PRO   A 1 102 ? -12.790 -0.133  -11.474 1.00 24.64  ? 639  PRO   A N   1 
ATOM   605  C CA  . PRO   A 1 102 ? -12.986 -1.255  -10.537 1.00 25.36  ? 639  PRO   A CA  1 
ATOM   606  C C   . PRO   A 1 102 ? -14.449 -1.551  -10.227 1.00 27.71  ? 639  PRO   A C   1 
ATOM   607  O O   . PRO   A 1 102 ? -14.860 -2.718  -10.242 1.00 28.18  ? 639  PRO   A O   1 
ATOM   608  C CB  . PRO   A 1 102 ? -12.211 -0.791  -9.295  1.00 24.04  ? 639  PRO   A CB  1 
ATOM   609  C CG  . PRO   A 1 102 ? -11.149 0.104   -9.822  1.00 23.11  ? 639  PRO   A CG  1 
ATOM   610  C CD  . PRO   A 1 102 ? -11.720 0.785   -11.035 1.00 23.55  ? 639  PRO   A CD  1 
ATOM   611  N N   . GLN   A 1 103 ? -15.250 -0.521  -9.948  1.00 29.61  ? 640  GLN   A N   1 
ATOM   612  C CA  . GLN   A 1 103 ? -16.681 -0.719  -9.742  1.00 31.08  ? 640  GLN   A CA  1 
ATOM   613  C C   . GLN   A 1 103 ? -17.360 -1.191  -11.020 1.00 31.32  ? 640  GLN   A C   1 
ATOM   614  O O   . GLN   A 1 103 ? -18.285 -2.012  -10.977 1.00 32.22  ? 640  GLN   A O   1 
ATOM   615  C CB  . GLN   A 1 103 ? -17.317 0.581   -9.250  1.00 33.36  ? 640  GLN   A CB  1 
ATOM   616  C CG  . GLN   A 1 103 ? -16.776 1.067   -7.912  1.00 34.63  ? 640  GLN   A CG  1 
ATOM   617  C CD  . GLN   A 1 103 ? -17.486 0.430   -6.732  1.00 35.36  ? 640  GLN   A CD  1 
ATOM   618  O OE1 . GLN   A 1 103 ? -18.526 -0.210  -6.894  1.00 36.11  ? 640  GLN   A OE1 1 
ATOM   619  N NE2 . GLN   A 1 103 ? -16.932 0.609   -5.538  1.00 35.14  ? 640  GLN   A NE2 1 
ATOM   620  N N   . GLU   A 1 104 ? -16.921 -0.661  -12.165 1.00 31.55  ? 641  GLU   A N   1 
ATOM   621  C CA  . GLU   A 1 104 ? -17.457 -1.085  -13.454 1.00 31.23  ? 641  GLU   A CA  1 
ATOM   622  C C   . GLU   A 1 104 ? -17.184 -2.562  -13.698 1.00 28.43  ? 641  GLU   A C   1 
ATOM   623  O O   . GLU   A 1 104 ? -18.024 -3.273  -14.259 1.00 29.65  ? 641  GLU   A O   1 
ATOM   624  C CB  . GLU   A 1 104 ? -16.840 -0.231  -14.560 1.00 33.68  ? 641  GLU   A CB  1 
ATOM   625  C CG  . GLU   A 1 104 ? -17.573 -0.227  -15.882 1.00 35.72  ? 641  GLU   A CG  1 
ATOM   626  C CD  . GLU   A 1 104 ? -16.793 0.516   -16.952 1.00 38.03  ? 641  GLU   A CD  1 
ATOM   627  O OE1 . GLU   A 1 104 ? -16.617 -0.040  -18.058 1.00 38.49  ? 641  GLU   A OE1 1 
ATOM   628  O OE2 . GLU   A 1 104 ? -16.331 1.646   -16.682 1.00 39.17  ? 641  GLU   A OE2 1 
ATOM   629  N N   . LEU   A 1 105 ? -16.014 -3.041  -13.272 1.00 24.77  ? 642  LEU   A N   1 
ATOM   630  C CA  . LEU   A 1 105 ? -15.650 -4.437  -13.489 1.00 22.49  ? 642  LEU   A CA  1 
ATOM   631  C C   . LEU   A 1 105 ? -16.452 -5.363  -12.582 1.00 20.82  ? 642  LEU   A C   1 
ATOM   632  O O   . LEU   A 1 105 ? -16.939 -6.411  -13.022 1.00 19.19  ? 642  LEU   A O   1 
ATOM   633  C CB  . LEU   A 1 105 ? -14.149 -4.624  -13.255 1.00 21.48  ? 642  LEU   A CB  1 
ATOM   634  C CG  . LEU   A 1 105 ? -13.657 -6.068  -13.182 1.00 20.56  ? 642  LEU   A CG  1 
ATOM   635  C CD1 . LEU   A 1 105 ? -13.833 -6.745  -14.524 1.00 17.53  ? 642  LEU   A CD1 1 
ATOM   636  C CD2 . LEU   A 1 105 ? -12.206 -6.122  -12.726 1.00 18.34  ? 642  LEU   A CD2 1 
ATOM   637  N N   . LEU   A 1 106 ? -16.586 -4.996  -11.305 1.00 21.11  ? 643  LEU   A N   1 
ATOM   638  C CA  . LEU   A 1 106 ? -17.388 -5.798  -10.386 1.00 22.01  ? 643  LEU   A CA  1 
ATOM   639  C C   . LEU   A 1 106 ? -18.821 -5.939  -10.888 1.00 23.63  ? 643  LEU   A C   1 
ATOM   640  O O   . LEU   A 1 106 ? -19.381 -7.042  -10.894 1.00 18.51  ? 643  LEU   A O   1 
ATOM   641  C CB  . LEU   A 1 106 ? -17.362 -5.176  -8.989  1.00 21.13  ? 643  LEU   A CB  1 
ATOM   642  C CG  . LEU   A 1 106 ? -18.176 -5.924  -7.932  1.00 20.85  ? 643  LEU   A CG  1 
ATOM   643  C CD1 . LEU   A 1 106 ? -17.776 -7.391  -7.914  1.00 20.50  ? 643  LEU   A CD1 1 
ATOM   644  C CD2 . LEU   A 1 106 ? -17.996 -5.303  -6.560  1.00 21.35  ? 643  LEU   A CD2 1 
ATOM   645  N N   . SER   A 1 107 ? -19.420 -4.832  -11.337 1.00 23.18  ? 644  SER   A N   1 
ATOM   646  C CA  . SER   A 1 107 ? -20.786 -4.886  -11.848 1.00 23.46  ? 644  SER   A CA  1 
ATOM   647  C C   . SER   A 1 107 ? -20.884 -5.730  -13.112 1.00 22.73  ? 644  SER   A C   1 
ATOM   648  O O   . SER   A 1 107 ? -21.908 -6.380  -13.339 1.00 22.77  ? 644  SER   A O   1 
ATOM   649  C CB  . SER   A 1 107 ? -21.310 -3.474  -12.108 1.00 24.03  ? 644  SER   A CB  1 
ATOM   650  O OG  . SER   A 1 107 ? -21.328 -2.710  -10.917 1.00 24.86  ? 644  SER   A OG  1 
ATOM   651  N N   . LEU   A 1 108 ? -19.843 -5.734  -13.949 1.00 22.59  ? 645  LEU   A N   1 
ATOM   652  C CA  . LEU   A 1 108 ? -19.875 -6.576  -15.141 1.00 22.93  ? 645  LEU   A CA  1 
ATOM   653  C C   . LEU   A 1 108 ? -19.813 -8.053  -14.771 1.00 22.91  ? 645  LEU   A C   1 
ATOM   654  O O   . LEU   A 1 108 ? -20.539 -8.875  -15.343 1.00 23.37  ? 645  LEU   A O   1 
ATOM   655  C CB  . LEU   A 1 108 ? -18.732 -6.206  -16.086 1.00 25.38  ? 645  LEU   A CB  1 
ATOM   656  C CG  . LEU   A 1 108 ? -18.903 -4.930  -16.923 1.00 27.61  ? 645  LEU   A CG  1 
ATOM   657  C CD1 . LEU   A 1 108 ? -17.559 -4.422  -17.433 1.00 28.03  ? 645  LEU   A CD1 1 
ATOM   658  C CD2 . LEU   A 1 108 ? -19.845 -5.164  -18.088 1.00 28.13  ? 645  LEU   A CD2 1 
ATOM   659  N N   . LEU   A 1 109 ? -18.967 -8.408  -13.801 1.00 23.02  ? 646  LEU   A N   1 
ATOM   660  C CA  . LEU   A 1 109 ? -18.858 -9.803  -13.382 1.00 22.41  ? 646  LEU   A CA  1 
ATOM   661  C C   . LEU   A 1 109 ? -20.144 -10.298 -12.729 1.00 24.25  ? 646  LEU   A C   1 
ATOM   662  O O   . LEU   A 1 109 ? -20.496 -11.477 -12.866 1.00 24.28  ? 646  LEU   A O   1 
ATOM   663  C CB  . LEU   A 1 109 ? -17.676 -9.967  -12.426 1.00 21.48  ? 646  LEU   A CB  1 
ATOM   664  C CG  . LEU   A 1 109 ? -16.347 -9.619  -13.083 1.00 21.50  ? 646  LEU   A CG  1 
ATOM   665  C CD1 . LEU   A 1 109 ? -15.215 -9.662  -12.078 1.00 21.86  ? 646  LEU   A CD1 1 
ATOM   666  C CD2 . LEU   A 1 109 ? -16.085 -10.575 -14.220 1.00 21.75  ? 646  LEU   A CD2 1 
ATOM   667  N N   . ILE   A 1 110 ? -20.846 -9.420  -12.008 1.00 25.42  ? 647  ILE   A N   1 
ATOM   668  C CA  . ILE   A 1 110 ? -22.132 -9.784  -11.423 1.00 27.56  ? 647  ILE   A CA  1 
ATOM   669  C C   . ILE   A 1 110 ? -23.189 -9.921  -12.515 1.00 28.45  ? 647  ILE   A C   1 
ATOM   670  O O   . ILE   A 1 110 ? -24.044 -10.818 -12.469 1.00 28.81  ? 647  ILE   A O   1 
ATOM   671  C CB  . ILE   A 1 110 ? -22.530 -8.747  -10.355 1.00 28.46  ? 647  ILE   A CB  1 
ATOM   672  C CG1 . ILE   A 1 110 ? -21.560 -8.819  -9.167  1.00 28.31  ? 647  ILE   A CG1 1 
ATOM   673  C CG2 . ILE   A 1 110 ? -23.979 -8.944  -9.917  1.00 29.12  ? 647  ILE   A CG2 1 
ATOM   674  C CD1 . ILE   A 1 110 ? -21.763 -7.742  -8.119  1.00 29.07  ? 647  ILE   A CD1 1 
ATOM   675  N N   . GLU   A 1 111 ? -23.137 -9.043  -13.518 1.00 27.50  ? 648  GLU   A N   1 
ATOM   676  C CA  . GLU   A 1 111 ? -23.985 -9.195  -14.693 1.00 27.83  ? 648  GLU   A CA  1 
ATOM   677  C C   . GLU   A 1 111 ? -23.769 -10.556 -15.340 1.00 26.65  ? 648  GLU   A C   1 
ATOM   678  O O   . GLU   A 1 111 ? -24.728 -11.267 -15.662 1.00 27.30  ? 648  GLU   A O   1 
ATOM   679  C CB  . GLU   A 1 111 ? -23.680 -8.076  -15.684 1.00 29.40  ? 648  GLU   A CB  1 
ATOM   680  C CG  . GLU   A 1 111 ? -24.882 -7.429  -16.313 1.00 31.99  ? 648  GLU   A CG  1 
ATOM   681  C CD  . GLU   A 1 111 ? -24.486 -6.611  -17.515 1.00 33.54  ? 648  GLU   A CD  1 
ATOM   682  O OE1 . GLU   A 1 111 ? -25.089 -6.799  -18.593 1.00 32.76  ? 648  GLU   A OE1 1 
ATOM   683  O OE2 . GLU   A 1 111 ? -23.543 -5.803  -17.381 1.00 34.87  ? 648  GLU   A OE2 1 
ATOM   684  N N   . ARG   A 1 112 ? -22.503 -10.938 -15.527 1.00 25.19  ? 649  ARG   A N   1 
ATOM   685  C CA  . ARG   A 1 112 ? -22.180 -12.216 -16.151 1.00 24.24  ? 649  ARG   A CA  1 
ATOM   686  C C   . ARG   A 1 112 ? -22.699 -13.386 -15.329 1.00 21.99  ? 649  ARG   A C   1 
ATOM   687  O O   . ARG   A 1 112 ? -23.076 -14.420 -15.892 1.00 20.15  ? 649  ARG   A O   1 
ATOM   688  C CB  . ARG   A 1 112 ? -20.663 -12.333 -16.339 1.00 23.91  ? 649  ARG   A CB  1 
ATOM   689  C CG  . ARG   A 1 112 ? -20.197 -13.571 -17.101 1.00 23.71  ? 649  ARG   A CG  1 
ATOM   690  C CD  . ARG   A 1 112 ? -20.242 -13.354 -18.605 1.00 24.41  ? 649  ARG   A CD  1 
ATOM   691  N NE  . ARG   A 1 112 ? -19.518 -14.399 -19.322 1.00 25.15  ? 649  ARG   A NE  1 
ATOM   692  C CZ  . ARG   A 1 112 ? -20.087 -15.288 -20.129 1.00 26.80  ? 649  ARG   A CZ  1 
ATOM   693  N NH1 . ARG   A 1 112 ? -21.398 -15.261 -20.342 1.00 28.55  ? 649  ARG   A NH1 1 
ATOM   694  N NH2 . ARG   A 1 112 ? -19.342 -16.198 -20.736 1.00 26.38  ? 649  ARG   A NH2 1 
ATOM   695  N N   . PHE   A 1 113 ? -22.747 -13.227 -14.004 1.00 21.38  ? 650  PHE   A N   1 
ATOM   696  C CA  . PHE   A 1 113 ? -23.073 -14.322 -13.098 1.00 20.57  ? 650  PHE   A CA  1 
ATOM   697  C C   . PHE   A 1 113 ? -24.563 -14.630 -13.096 1.00 22.95  ? 650  PHE   A C   1 
ATOM   698  O O   . PHE   A 1 113 ? -24.955 -15.794 -12.968 1.00 23.38  ? 650  PHE   A O   1 
ATOM   699  C CB  . PHE   A 1 113 ? -22.601 -13.974 -11.683 1.00 19.56  ? 650  PHE   A CB  1 
ATOM   700  C CG  . PHE   A 1 113 ? -22.555 -15.147 -10.747 1.00 19.52  ? 650  PHE   A CG  1 
ATOM   701  C CD1 . PHE   A 1 113 ? -23.683 -15.544 -10.053 1.00 20.03  ? 650  PHE   A CD1 1 
ATOM   702  C CD2 . PHE   A 1 113 ? -21.376 -15.842 -10.550 1.00 19.76  ? 650  PHE   A CD2 1 
ATOM   703  C CE1 . PHE   A 1 113 ? -23.635 -16.619 -9.195  1.00 20.95  ? 650  PHE   A CE1 1 
ATOM   704  C CE2 . PHE   A 1 113 ? -21.324 -16.914 -9.686  1.00 18.95  ? 650  PHE   A CE2 1 
ATOM   705  C CZ  . PHE   A 1 113 ? -22.451 -17.303 -9.012  1.00 20.64  ? 650  PHE   A CZ  1 
ATOM   706  N N   . GLU   A 1 114 ? -25.405 -13.604 -13.229 1.00 25.20  ? 651  GLU   A N   1 
ATOM   707  C CA  . GLU   A 1 114 ? -26.857 -13.764 -13.126 1.00 29.44  ? 651  GLU   A CA  1 
ATOM   708  C C   . GLU   A 1 114 ? -27.398 -14.087 -14.511 1.00 28.96  ? 651  GLU   A C   1 
ATOM   709  O O   . GLU   A 1 114 ? -27.858 -13.216 -15.252 1.00 28.70  ? 651  GLU   A O   1 
ATOM   710  C CB  . GLU   A 1 114 ? -27.496 -12.513 -12.533 1.00 33.66  ? 651  GLU   A CB  1 
ATOM   711  C CG  . GLU   A 1 114 ? -27.078 -12.276 -11.086 1.00 37.81  ? 651  GLU   A CG  1 
ATOM   712  C CD  . GLU   A 1 114 ? -27.522 -10.928 -10.542 1.00 41.64  ? 651  GLU   A CD  1 
ATOM   713  O OE1 . GLU   A 1 114 ? -28.013 -10.087 -11.328 1.00 42.74  ? 651  GLU   A OE1 1 
ATOM   714  O OE2 . GLU   A 1 114 ? -27.375 -10.711 -9.319  1.00 42.82  ? 651  GLU   A OE2 1 
ATOM   715  N N   . ILE   A 1 115 ? -27.359 -15.365 -14.855 1.00 20.73  ? 652  ILE   A N   1 
ATOM   716  C CA  . ILE   A 1 115 ? -27.669 -15.839 -16.199 1.00 20.89  ? 652  ILE   A CA  1 
ATOM   717  C C   . ILE   A 1 115 ? -29.138 -16.251 -16.234 1.00 35.20  ? 652  ILE   A C   1 
ATOM   718  O O   . ILE   A 1 115 ? -29.542 -17.125 -15.451 1.00 22.85  ? 652  ILE   A O   1 
ATOM   719  C CB  . ILE   A 1 115 ? -26.757 -17.008 -16.595 1.00 25.15  ? 652  ILE   A CB  1 
ATOM   720  C CG1 . ILE   A 1 115 ? -25.290 -16.557 -16.575 1.00 22.00  ? 652  ILE   A CG1 1 
ATOM   721  C CG2 . ILE   A 1 115 ? -27.152 -17.556 -17.952 1.00 20.73  ? 652  ILE   A CG2 1 
ATOM   722  C CD1 . ILE   A 1 115 ? -24.288 -17.689 -16.662 1.00 20.01  ? 652  ILE   A CD1 1 
ATOM   723  N N   . PRO   A 1 116 ? -29.961 -15.656 -17.089 1.00 32.95  ? 653  PRO   A N   1 
ATOM   724  C CA  . PRO   A 1 116 ? -31.331 -16.147 -17.240 1.00 32.97  ? 653  PRO   A CA  1 
ATOM   725  C C   . PRO   A 1 116 ? -31.348 -17.419 -18.067 1.00 33.61  ? 653  PRO   A C   1 
ATOM   726  O O   . PRO   A 1 116 ? -30.476 -17.656 -18.906 1.00 32.33  ? 653  PRO   A O   1 
ATOM   727  C CB  . PRO   A 1 116 ? -32.043 -14.994 -17.959 1.00 32.83  ? 653  PRO   A CB  1 
ATOM   728  C CG  . PRO   A 1 116 ? -30.960 -14.327 -18.746 1.00 31.63  ? 653  PRO   A CG  1 
ATOM   729  C CD  . PRO   A 1 116 ? -29.702 -14.464 -17.919 1.00 31.31  ? 653  PRO   A CD  1 
ATOM   730  N N   . GLU   A 1 117 ? -32.340 -18.254 -17.799 1.00 35.71  ? 654  GLU   A N   1 
ATOM   731  C CA  . GLU   A 1 117 ? -32.475 -19.457 -18.604 1.00 36.87  ? 654  GLU   A CA  1 
ATOM   732  C C   . GLU   A 1 117 ? -33.268 -19.145 -19.874 1.00 39.32  ? 654  GLU   A C   1 
ATOM   733  O O   . GLU   A 1 117 ? -34.027 -18.171 -19.916 1.00 41.07  ? 654  GLU   A O   1 
ATOM   734  C CB  . GLU   A 1 117 ? -33.170 -20.556 -17.803 1.00 37.24  ? 654  GLU   A CB  1 
ATOM   735  C CG  . GLU   A 1 117 ? -32.409 -20.953 -16.558 1.00 36.18  ? 654  GLU   A CG  1 
ATOM   736  C CD  . GLU   A 1 117 ? -33.020 -22.129 -15.830 1.00 37.04  ? 654  GLU   A CD  1 
ATOM   737  O OE1 . GLU   A 1 117 ? -34.233 -22.378 -16.000 1.00 37.84  ? 654  GLU   A OE1 1 
ATOM   738  O OE2 . GLU   A 1 117 ? -32.277 -22.806 -15.087 1.00 36.49  ? 654  GLU   A OE2 1 
ATOM   739  N N   . PRO   A 1 118 ? -33.094 -19.936 -20.934 1.00 40.61  ? 655  PRO   A N   1 
ATOM   740  C CA  . PRO   A 1 118 ? -33.891 -19.709 -22.145 1.00 43.40  ? 655  PRO   A CA  1 
ATOM   741  C C   . PRO   A 1 118 ? -35.376 -19.859 -21.852 1.00 47.06  ? 655  PRO   A C   1 
ATOM   742  O O   . PRO   A 1 118 ? -35.778 -20.546 -20.912 1.00 47.68  ? 655  PRO   A O   1 
ATOM   743  C CB  . PRO   A 1 118 ? -33.394 -20.793 -23.111 1.00 42.72  ? 655  PRO   A CB  1 
ATOM   744  C CG  . PRO   A 1 118 ? -32.055 -21.183 -22.591 1.00 41.08  ? 655  PRO   A CG  1 
ATOM   745  C CD  . PRO   A 1 118 ? -32.142 -21.047 -21.102 1.00 40.12  ? 655  PRO   A CD  1 
ATOM   746  N N   . GLU   A 1 119 ? -36.190 -19.196 -22.660 1.00 50.05  ? 656  GLU   A N   1 
ATOM   747  C CA  . GLU   A 1 119 ? -37.634 -19.293 -22.503 1.00 54.58  ? 656  GLU   A CA  1 
ATOM   748  C C   . GLU   A 1 119 ? -38.081 -20.729 -22.751 1.00 55.87  ? 656  GLU   A C   1 
ATOM   749  O O   . GLU   A 1 119 ? -37.845 -21.259 -23.847 1.00 55.78  ? 656  GLU   A O   1 
ATOM   750  C CB  . GLU   A 1 119 ? -38.352 -18.354 -23.467 1.00 58.20  ? 656  GLU   A CB  1 
ATOM   751  C CG  . GLU   A 1 119 ? -39.712 -17.895 -22.977 1.00 62.15  ? 656  GLU   A CG  1 
ATOM   752  C CD  . GLU   A 1 119 ? -39.613 -16.678 -22.089 1.00 63.13  ? 656  GLU   A CD  1 
ATOM   753  O OE1 . GLU   A 1 119 ? -39.973 -15.577 -22.559 1.00 65.06  ? 656  GLU   A OE1 1 
ATOM   754  O OE2 . GLU   A 1 119 ? -39.153 -16.818 -20.935 1.00 61.86  ? 656  GLU   A OE2 1 
ATOM   755  N N   . PRO   A 1 120 ? -38.707 -21.393 -21.781 1.00 57.33  ? 657  PRO   A N   1 
ATOM   756  C CA  . PRO   A 1 120 ? -39.162 -22.768 -22.012 1.00 59.57  ? 657  PRO   A CA  1 
ATOM   757  C C   . PRO   A 1 120 ? -40.114 -22.831 -23.196 1.00 62.69  ? 657  PRO   A C   1 
ATOM   758  O O   . PRO   A 1 120 ? -40.868 -21.894 -23.461 1.00 63.64  ? 657  PRO   A O   1 
ATOM   759  C CB  . PRO   A 1 120 ? -39.870 -23.133 -20.701 1.00 60.30  ? 657  PRO   A CB  1 
ATOM   760  C CG  . PRO   A 1 120 ? -39.293 -22.200 -19.683 1.00 58.28  ? 657  PRO   A CG  1 
ATOM   761  C CD  . PRO   A 1 120 ? -39.006 -20.927 -20.417 1.00 57.02  ? 657  PRO   A CD  1 
ATOM   762  N N   . THR   A 1 121 ? -40.053 -23.942 -23.927 1.00 65.08  ? 658  THR   A N   1 
ATOM   763  C CA  . THR   A 1 121 ? -40.974 -24.139 -25.037 1.00 68.62  ? 658  THR   A CA  1 
ATOM   764  C C   . THR   A 1 121 ? -42.331 -24.617 -24.523 1.00 72.47  ? 658  THR   A C   1 
ATOM   765  O O   . THR   A 1 121 ? -42.477 -25.046 -23.375 1.00 72.90  ? 658  THR   A O   1 
ATOM   766  C CB  . THR   A 1 121 ? -40.410 -25.136 -26.056 1.00 68.11  ? 658  THR   A CB  1 
ATOM   767  O OG1 . THR   A 1 121 ? -41.301 -25.231 -27.174 1.00 70.63  ? 658  THR   A OG1 1 
ATOM   768  C CG2 . THR   A 1 121 ? -40.250 -26.513 -25.445 1.00 67.92  ? 658  THR   A CG2 1 
ATOM   769  N N   . ASP   A 1 122 ? -43.340 -24.521 -25.395 1.00 75.52  ? 659  ASP   A N   1 
ATOM   770  C CA  . ASP   A 1 122 ? -44.691 -24.913 -25.005 1.00 79.40  ? 659  ASP   A CA  1 
ATOM   771  C C   . ASP   A 1 122 ? -44.731 -26.357 -24.524 1.00 81.49  ? 659  ASP   A C   1 
ATOM   772  O O   . ASP   A 1 122 ? -45.428 -26.676 -23.553 1.00 83.06  ? 659  ASP   A O   1 
ATOM   773  C CB  . ASP   A 1 122 ? -45.656 -24.708 -26.171 1.00 81.53  ? 659  ASP   A CB  1 
ATOM   774  C CG  . ASP   A 1 122 ? -45.947 -23.246 -26.433 1.00 81.62  ? 659  ASP   A CG  1 
ATOM   775  O OD1 . ASP   A 1 122 ? -46.347 -22.539 -25.484 1.00 81.77  ? 659  ASP   A OD1 1 
ATOM   776  O OD2 . ASP   A 1 122 ? -45.761 -22.801 -27.584 1.00 81.69  ? 659  ASP   A OD2 1 
ATOM   777  N N   . ALA   A 1 123 ? -43.975 -27.241 -25.180 1.00 81.72  ? 660  ALA   A N   1 
ATOM   778  C CA  . ALA   A 1 123 ? -43.920 -28.636 -24.754 1.00 83.08  ? 660  ALA   A CA  1 
ATOM   779  C C   . ALA   A 1 123 ? -43.170 -28.795 -23.438 1.00 81.77  ? 660  ALA   A C   1 
ATOM   780  O O   . ALA   A 1 123 ? -43.450 -29.729 -22.677 1.00 82.94  ? 660  ALA   A O   1 
ATOM   781  C CB  . ALA   A 1 123 ? -43.276 -29.495 -25.842 1.00 82.95  ? 660  ALA   A CB  1 
ATOM   782  N N   . ASP   A 1 124 ? -42.216 -27.904 -23.151 1.00 79.57  ? 661  ASP   A N   1 
ATOM   783  C CA  . ASP   A 1 124 ? -41.522 -27.957 -21.868 1.00 78.57  ? 661  ASP   A CA  1 
ATOM   784  C C   . ASP   A 1 124 ? -42.444 -27.556 -20.725 1.00 80.72  ? 661  ASP   A C   1 
ATOM   785  O O   . ASP   A 1 124 ? -42.424 -28.179 -19.656 1.00 80.89  ? 661  ASP   A O   1 
ATOM   786  C CB  . ASP   A 1 124 ? -40.287 -27.058 -21.890 1.00 75.38  ? 661  ASP   A CB  1 
ATOM   787  C CG  . ASP   A 1 124 ? -39.096 -27.724 -22.533 1.00 73.38  ? 661  ASP   A CG  1 
ATOM   788  O OD1 . ASP   A 1 124 ? -39.187 -28.931 -22.847 1.00 74.79  ? 661  ASP   A OD1 1 
ATOM   789  O OD2 . ASP   A 1 124 ? -38.072 -27.037 -22.728 1.00 70.85  ? 661  ASP   A OD2 1 
ATOM   790  N N   . LYS   A 1 125 ? -43.255 -26.513 -20.930 1.00 82.41  ? 662  LYS   A N   1 
ATOM   791  C CA  . LYS   A 1 125 ? -44.180 -26.072 -19.890 1.00 84.35  ? 662  LYS   A CA  1 
ATOM   792  C C   . LYS   A 1 125 ? -45.186 -27.163 -19.548 1.00 88.42  ? 662  LYS   A C   1 
ATOM   793  O O   . LYS   A 1 125 ? -45.520 -27.367 -18.374 1.00 89.00  ? 662  LYS   A O   1 
ATOM   794  C CB  . LYS   A 1 125 ? -44.908 -24.801 -20.333 1.00 84.18  ? 662  LYS   A CB  1 
ATOM   795  C CG  . LYS   A 1 125 ? -43.985 -23.681 -20.776 1.00 81.03  ? 662  LYS   A CG  1 
ATOM   796  C CD  . LYS   A 1 125 ? -44.755 -22.406 -21.081 1.00 81.67  ? 662  LYS   A CD  1 
ATOM   797  C CE  . LYS   A 1 125 ? -43.800 -21.236 -21.273 1.00 79.18  ? 662  LYS   A CE  1 
ATOM   798  N NZ  . LYS   A 1 125 ? -44.507 -19.965 -21.593 1.00 80.29  ? 662  LYS   A NZ  1 
ATOM   799  N N   . LEU   A 1 126 ? -45.674 -27.878 -20.566 1.00 91.59  ? 663  LEU   A N   1 
ATOM   800  C CA  . LEU   A 1 126 ? -46.633 -28.953 -20.335 1.00 96.01  ? 663  LEU   A CA  1 
ATOM   801  C C   . LEU   A 1 126 ? -46.051 -30.028 -19.427 1.00 97.53  ? 663  LEU   A C   1 
ATOM   802  O O   . LEU   A 1 126 ? -46.749 -30.556 -18.553 1.00 99.47  ? 663  LEU   A O   1 
ATOM   803  C CB  . LEU   A 1 126 ? -47.071 -29.556 -21.669 1.00 97.51  ? 663  LEU   A CB  1 
ATOM   804  C CG  . LEU   A 1 126 ? -47.786 -28.617 -22.642 1.00 98.73  ? 663  LEU   A CG  1 
ATOM   805  C CD1 . LEU   A 1 126 ? -47.918 -29.260 -24.014 1.00 99.99  ? 663  LEU   A CD1 1 
ATOM   806  C CD2 . LEU   A 1 126 ? -49.151 -28.223 -22.100 1.00 101.52 ? 663  LEU   A CD2 1 
ATOM   807  N N   . ALA   A 1 127 ? -44.768 -30.355 -19.612 1.00 96.95  ? 664  ALA   A N   1 
ATOM   808  C CA  . ALA   A 1 127 ? -44.130 -31.385 -18.797 1.00 98.45  ? 664  ALA   A CA  1 
ATOM   809  C C   . ALA   A 1 127 ? -44.092 -30.977 -17.329 1.00 100.28 ? 664  ALA   A C   1 
ATOM   810  O O   . ALA   A 1 127 ? -44.410 -31.777 -16.440 1.00 101.80 ? 664  ALA   A O   1 
ATOM   811  C CB  . ALA   A 1 127 ? -42.720 -31.669 -19.317 1.00 95.75  ? 664  ALA   A CB  1 
ATOM   812  N N   . ILE   A 1 128 ? -43.705 -29.729 -17.056 1.00 100.42 ? 665  ILE   A N   1 
ATOM   813  C CA  . ILE   A 1 128 ? -43.712 -29.224 -15.683 1.00 101.66 ? 665  ILE   A CA  1 
ATOM   814  C C   . ILE   A 1 128 ? -45.118 -29.302 -15.096 1.00 106.43 ? 665  ILE   A C   1 
ATOM   815  O O   . ILE   A 1 128 ? -45.315 -29.754 -13.961 1.00 107.85 ? 665  ILE   A O   1 
ATOM   816  C CB  . ILE   A 1 128 ? -43.154 -27.788 -15.639 1.00 98.34  ? 665  ILE   A CB  1 
ATOM   817  C CG1 . ILE   A 1 128 ? -41.623 -27.810 -15.652 1.00 94.48  ? 665  ILE   A CG1 1 
ATOM   818  C CG2 . ILE   A 1 128 ? -43.689 -27.029 -14.429 1.00 98.99  ? 665  ILE   A CG2 1 
ATOM   819  C CD1 . ILE   A 1 128 ? -41.012 -27.106 -16.838 1.00 92.15  ? 665  ILE   A CD1 1 
ATOM   820  N N   . GLU   A 1 129 ? -46.119 -28.879 -15.874 1.00 109.04 ? 666  GLU   A N   1 
ATOM   821  C CA  . GLU   A 1 129 ? -47.501 -28.892 -15.401 1.00 113.10 ? 666  GLU   A CA  1 
ATOM   822  C C   . GLU   A 1 129 ? -47.953 -30.303 -15.046 1.00 115.94 ? 666  GLU   A C   1 
ATOM   823  O O   . GLU   A 1 129 ? -48.658 -30.507 -14.050 1.00 118.46 ? 666  GLU   A O   1 
ATOM   824  C CB  . GLU   A 1 129 ? -48.413 -28.287 -16.465 1.00 114.90 ? 666  GLU   A CB  1 
ATOM   825  C CG  . GLU   A 1 129 ? -49.801 -27.930 -15.986 1.00 118.89 ? 666  GLU   A CG  1 
ATOM   826  C CD  . GLU   A 1 129 ? -50.450 -26.900 -16.881 1.00 120.83 ? 666  GLU   A CD  1 
ATOM   827  O OE1 . GLU   A 1 129 ? -51.537 -27.178 -17.430 1.00 124.10 ? 666  GLU   A OE1 1 
ATOM   828  O OE2 . GLU   A 1 129 ? -49.854 -25.815 -17.049 1.00 119.25 ? 666  GLU   A OE2 1 
ATOM   829  N N   . LYS   A 1 130 ? -47.549 -31.289 -15.849 1.00 115.72 ? 667  LYS   A N   1 
ATOM   830  C CA  . LYS   A 1 130 ? -47.889 -32.680 -15.567 1.00 117.76 ? 667  LYS   A CA  1 
ATOM   831  C C   . LYS   A 1 130 ? -47.320 -33.124 -14.224 1.00 116.62 ? 667  LYS   A C   1 
ATOM   832  O O   . LYS   A 1 130 ? -48.037 -33.688 -13.388 1.00 119.22 ? 667  LYS   A O   1 
ATOM   833  C CB  . LYS   A 1 130 ? -47.377 -33.573 -16.697 1.00 117.55 ? 667  LYS   A CB  1 
ATOM   834  C CG  . LYS   A 1 130 ? -47.597 -35.055 -16.481 1.00 119.99 ? 667  LYS   A CG  1 
ATOM   835  C CD  . LYS   A 1 130 ? -47.049 -35.846 -17.654 1.00 119.57 ? 667  LYS   A CD  1 
ATOM   836  C CE  . LYS   A 1 130 ? -47.352 -37.321 -17.502 1.00 122.15 ? 667  LYS   A CE  1 
ATOM   837  N NZ  . LYS   A 1 130 ? -46.352 -38.162 -18.211 1.00 120.97 ? 667  LYS   A NZ  1 
ATOM   838  N N   . GLY   A 1 131 ? -46.039 -32.877 -14.000 1.00 112.62 ? 668  GLY   A N   1 
ATOM   839  C CA  . GLY   A 1 131 ? -45.406 -33.215 -12.743 1.00 111.01 ? 668  GLY   A CA  1 
ATOM   840  C C   . GLY   A 1 131 ? -44.576 -34.483 -12.836 1.00 109.72 ? 668  GLY   A C   1 
ATOM   841  O O   . GLY   A 1 131 ? -44.898 -35.423 -13.573 1.00 111.36 ? 668  GLY   A O   1 
ATOM   842  N N   . GLU   A 1 132 ? -43.481 -34.509 -12.071 1.00 106.69 ? 669  GLU   A N   1 
ATOM   843  C CA  . GLU   A 1 132 ? -42.578 -35.660 -12.001 1.00 105.02 ? 669  GLU   A CA  1 
ATOM   844  C C   . GLU   A 1 132 ? -41.969 -35.970 -13.369 1.00 101.63 ? 669  GLU   A C   1 
ATOM   845  O O   . GLU   A 1 132 ? -41.905 -37.122 -13.804 1.00 102.76 ? 669  GLU   A O   1 
ATOM   846  C CB  . GLU   A 1 132 ? -43.292 -36.886 -11.422 1.00 108.75 ? 669  GLU   A CB  1 
ATOM   847  C CG  . GLU   A 1 132 ? -43.749 -36.718 -9.980  1.00 110.86 ? 669  GLU   A CG  1 
ATOM   848  C CD  . GLU   A 1 132 ? -44.562 -37.898 -9.478  1.00 115.39 ? 669  GLU   A CD  1 
ATOM   849  O OE1 . GLU   A 1 132 ? -45.802 -37.882 -9.638  1.00 118.19 ? 669  GLU   A OE1 1 
ATOM   850  O OE2 . GLU   A 1 132 ? -43.958 -38.844 -8.928  1.00 116.23 ? 669  GLU   A OE2 1 
ATOM   851  N N   . GLN   A 1 133 ? -41.517 -34.920 -14.052 1.00 97.10  ? 670  GLN   A N   1 
ATOM   852  C CA  . GLN   A 1 133 ? -40.942 -35.045 -15.380 1.00 93.90  ? 670  GLN   A CA  1 
ATOM   853  C C   . GLN   A 1 133 ? -39.534 -34.466 -15.386 1.00 89.53  ? 670  GLN   A C   1 
ATOM   854  O O   . GLN   A 1 133 ? -39.340 -33.320 -14.952 1.00 88.00  ? 670  GLN   A O   1 
ATOM   855  C CB  . GLN   A 1 133 ? -41.810 -34.328 -16.427 1.00 93.67  ? 670  GLN   A CB  1 
ATOM   856  C CG  . GLN   A 1 133 ? -43.285 -34.695 -16.374 1.00 96.26  ? 670  GLN   A CG  1 
ATOM   857  C CD  . GLN   A 1 133 ? -43.535 -36.175 -16.583 1.00 97.93  ? 670  GLN   A CD  1 
ATOM   858  O OE1 . GLN   A 1 133 ? -42.920 -36.807 -17.441 1.00 97.32  ? 670  GLN   A OE1 1 
ATOM   859  N NE2 . GLN   A 1 133 ? -44.444 -36.736 -15.795 1.00 100.28 ? 670  GLN   A NE2 1 
ATOM   860  N N   . PRO   A 1 134 ? -38.532 -35.213 -15.852 1.00 87.07  ? 671  PRO   A N   1 
ATOM   861  C CA  . PRO   A 1 134 ? -37.175 -34.658 -15.924 1.00 82.11  ? 671  PRO   A CA  1 
ATOM   862  C C   . PRO   A 1 134 ? -37.114 -33.491 -16.898 1.00 77.66  ? 671  PRO   A C   1 
ATOM   863  O O   . PRO   A 1 134 ? -37.745 -33.510 -17.957 1.00 78.97  ? 671  PRO   A O   1 
ATOM   864  C CB  . PRO   A 1 134 ? -36.328 -35.844 -16.404 1.00 82.85  ? 671  PRO   A CB  1 
ATOM   865  C CG  . PRO   A 1 134 ? -37.302 -36.782 -17.056 1.00 86.04  ? 671  PRO   A CG  1 
ATOM   866  C CD  . PRO   A 1 134 ? -38.587 -36.618 -16.298 1.00 88.44  ? 671  PRO   A CD  1 
ATOM   867  N N   . ILE   A 1 135 ? -36.347 -32.464 -16.520 1.00 71.88  ? 672  ILE   A N   1 
ATOM   868  C CA  . ILE   A 1 135 ? -36.293 -31.246 -17.316 1.00 66.65  ? 672  ILE   A CA  1 
ATOM   869  C C   . ILE   A 1 135 ? -35.747 -31.553 -18.709 1.00 62.64  ? 672  ILE   A C   1 
ATOM   870  O O   . ILE   A 1 135 ? -35.118 -32.590 -18.952 1.00 62.63  ? 672  ILE   A O   1 
ATOM   871  C CB  . ILE   A 1 135 ? -35.443 -30.174 -16.619 1.00 64.23  ? 672  ILE   A CB  1 
ATOM   872  C CG1 . ILE   A 1 135 ? -34.029 -30.701 -16.395 1.00 62.54  ? 672  ILE   A CG1 1 
ATOM   873  C CG2 . ILE   A 1 135 ? -36.087 -29.761 -15.302 1.00 65.00  ? 672  ILE   A CG2 1 
ATOM   874  C CD1 . ILE   A 1 135 ? -33.091 -29.684 -15.830 1.00 60.37  ? 672  ILE   A CD1 1 
ATOM   875  N N   . SER   A 1 136 ? -35.998 -30.629 -19.635 1.00 59.01  ? 673  SER   A N   1 
ATOM   876  C CA  . SER   A 1 136 ? -35.640 -30.851 -21.029 1.00 56.33  ? 673  SER   A CA  1 
ATOM   877  C C   . SER   A 1 136 ? -34.137 -31.053 -21.174 1.00 52.56  ? 673  SER   A C   1 
ATOM   878  O O   . SER   A 1 136 ? -33.340 -30.466 -20.436 1.00 50.44  ? 673  SER   A O   1 
ATOM   879  C CB  . SER   A 1 136 ? -36.093 -29.675 -21.896 1.00 55.17  ? 673  SER   A CB  1 
ATOM   880  O OG  . SER   A 1 136 ? -35.203 -28.580 -21.776 1.00 51.81  ? 673  SER   A OG  1 
ATOM   881  N N   . ALA   A 1 137 ? -33.761 -31.904 -22.134 1.00 51.68  ? 674  ALA   A N   1 
ATOM   882  C CA  . ALA   A 1 137 ? -32.352 -32.163 -22.406 1.00 48.53  ? 674  ALA   A CA  1 
ATOM   883  C C   . ALA   A 1 137 ? -31.594 -30.873 -22.689 1.00 45.37  ? 674  ALA   A C   1 
ATOM   884  O O   . ALA   A 1 137 ? -30.439 -30.718 -22.276 1.00 43.33  ? 674  ALA   A O   1 
ATOM   885  C CB  . ALA   A 1 137 ? -32.221 -33.135 -23.580 1.00 49.70  ? 674  ALA   A CB  1 
ATOM   886  N N   . ASP   A 1 138 ? -32.238 -29.931 -23.383 1.00 44.83  ? 675  ASP   A N   1 
ATOM   887  C CA  . ASP   A 1 138 ? -31.612 -28.642 -23.661 1.00 42.62  ? 675  ASP   A CA  1 
ATOM   888  C C   . ASP   A 1 138 ? -31.321 -27.878 -22.375 1.00 40.90  ? 675  ASP   A C   1 
ATOM   889  O O   . ASP   A 1 138 ? -30.233 -27.313 -22.211 1.00 38.30  ? 675  ASP   A O   1 
ATOM   890  C CB  . ASP   A 1 138 ? -32.504 -27.808 -24.583 1.00 42.98  ? 675  ASP   A CB  1 
ATOM   891  C CG  . ASP   A 1 138 ? -32.568 -28.360 -25.989 1.00 44.15  ? 675  ASP   A CG  1 
ATOM   892  O OD1 . ASP   A 1 138 ? -31.919 -29.392 -26.251 1.00 44.25  ? 675  ASP   A OD1 1 
ATOM   893  O OD2 . ASP   A 1 138 ? -33.267 -27.759 -26.832 1.00 45.35  ? 675  ASP   A OD2 1 
ATOM   894  N N   . LEU   A 1 139 ? -32.288 -27.839 -21.453 1.00 41.82  ? 676  LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 139 ? -32.089 -27.089 -20.217 1.00 40.87  ? 676  LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 139 ? -31.014 -27.733 -19.348 1.00 40.73  ? 676  LEU   A C   1 
ATOM   897  O O   . LEU   A 1 139 ? -30.242 -27.028 -18.685 1.00 38.40  ? 676  LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 139 ? -33.409 -26.970 -19.452 1.00 42.16  ? 676  LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 139 ? -33.409 -26.054 -18.221 1.00 41.92  ? 676  LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 139 ? -32.930 -24.656 -18.590 1.00 40.93  ? 676  LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 139 ? -34.789 -25.991 -17.582 1.00 43.50  ? 676  LEU   A CD2 1 
ATOM   902  N N   . LYS   A 1 140 ? -30.944 -29.070 -19.342 1.00 42.11  ? 677  LYS   A N   1 
ATOM   903  C CA  . LYS   A 1 140 ? -29.877 -29.744 -18.613 1.00 41.09  ? 677  LYS   A CA  1 
ATOM   904  C C   . LYS   A 1 140 ? -28.516 -29.427 -19.219 1.00 37.77  ? 677  LYS   A C   1 
ATOM   905  O O   . LYS   A 1 140 ? -27.558 -29.151 -18.489 1.00 37.36  ? 677  LYS   A O   1 
ATOM   906  C CB  . LYS   A 1 140 ? -30.117 -31.252 -18.599 1.00 44.57  ? 677  LYS   A CB  1 
ATOM   907  C CG  . LYS   A 1 140 ? -29.020 -32.031 -17.874 1.00 46.26  ? 677  LYS   A CG  1 
ATOM   908  C CD  . LYS   A 1 140 ? -29.247 -33.531 -17.956 1.00 50.19  ? 677  LYS   A CD  1 
ATOM   909  C CE  . LYS   A 1 140 ? -28.143 -34.303 -17.249 1.00 51.40  ? 677  LYS   A CE  1 
ATOM   910  N NZ  . LYS   A 1 140 ? -28.414 -35.769 -17.269 1.00 54.30  ? 677  LYS   A NZ  1 
ATOM   911  N N   . ARG   A 1 141 ? -28.409 -29.479 -20.550 1.00 36.29  ? 678  ARG   A N   1 
ATOM   912  C CA  . ARG   A 1 141 ? -27.173 -29.071 -21.214 1.00 34.20  ? 678  ARG   A CA  1 
ATOM   913  C C   . ARG   A 1 141 ? -26.798 -27.644 -20.844 1.00 30.49  ? 678  ARG   A C   1 
ATOM   914  O O   . ARG   A 1 141 ? -25.634 -27.354 -20.543 1.00 29.35  ? 678  ARG   A O   1 
ATOM   915  C CB  . ARG   A 1 141 ? -27.322 -29.188 -22.731 1.00 35.96  ? 678  ARG   A CB  1 
ATOM   916  C CG  . ARG   A 1 141 ? -27.018 -30.550 -23.312 1.00 39.32  ? 678  ARG   A CG  1 
ATOM   917  C CD  . ARG   A 1 141 ? -26.800 -30.440 -24.819 1.00 40.86  ? 678  ARG   A CD  1 
ATOM   918  N NE  . ARG   A 1 141 ? -25.570 -29.724 -25.152 1.00 40.12  ? 678  ARG   A NE  1 
ATOM   919  C CZ  . ARG   A 1 141 ? -25.214 -29.390 -26.390 1.00 40.81  ? 678  ARG   A CZ  1 
ATOM   920  N NH1 . ARG   A 1 141 ? -26.001 -29.699 -27.411 1.00 42.53  ? 678  ARG   A NH1 1 
ATOM   921  N NH2 . ARG   A 1 141 ? -24.076 -28.745 -26.611 1.00 39.77  ? 678  ARG   A NH2 1 
ATOM   922  N N   . PHE   A 1 142 ? -27.780 -26.739 -20.875 1.00 29.03  ? 679  PHE   A N   1 
ATOM   923  C CA  . PHE   A 1 142 ? -27.529 -25.319 -20.638 1.00 27.44  ? 679  PHE   A CA  1 
ATOM   924  C C   . PHE   A 1 142 ? -26.959 -25.080 -19.244 1.00 28.66  ? 679  PHE   A C   1 
ATOM   925  O O   . PHE   A 1 142 ? -25.994 -24.326 -19.076 1.00 27.54  ? 679  PHE   A O   1 
ATOM   926  C CB  . PHE   A 1 142 ? -28.830 -24.535 -20.848 1.00 26.45  ? 679  PHE   A CB  1 
ATOM   927  C CG  . PHE   A 1 142 ? -28.750 -23.086 -20.457 1.00 25.14  ? 679  PHE   A CG  1 
ATOM   928  C CD1 . PHE   A 1 142 ? -28.089 -22.167 -21.262 1.00 25.02  ? 679  PHE   A CD1 1 
ATOM   929  C CD2 . PHE   A 1 142 ? -29.359 -22.635 -19.300 1.00 24.58  ? 679  PHE   A CD2 1 
ATOM   930  C CE1 . PHE   A 1 142 ? -28.017 -20.820 -20.905 1.00 23.65  ? 679  PHE   A CE1 1 
ATOM   931  C CE2 . PHE   A 1 142 ? -29.295 -21.299 -18.942 1.00 23.84  ? 679  PHE   A CE2 1 
ATOM   932  C CZ  . PHE   A 1 142 ? -28.618 -20.390 -19.746 1.00 22.94  ? 679  PHE   A CZ  1 
ATOM   933  N N   . ARG   A 1 143 ? -27.541 -25.719 -18.228 1.00 31.44  ? 680  ARG   A N   1 
ATOM   934  C CA  . ARG   A 1 143 ? -27.059 -25.515 -16.867 1.00 31.90  ? 680  ARG   A CA  1 
ATOM   935  C C   . ARG   A 1 143 ? -25.689 -26.152 -16.663 1.00 32.77  ? 680  ARG   A C   1 
ATOM   936  O O   . ARG   A 1 143 ? -24.853 -25.622 -15.922 1.00 31.80  ? 680  ARG   A O   1 
ATOM   937  C CB  . ARG   A 1 143 ? -28.061 -26.080 -15.864 1.00 32.40  ? 680  ARG   A CB  1 
ATOM   938  C CG  . ARG   A 1 143 ? -29.427 -25.404 -15.874 1.00 33.55  ? 680  ARG   A CG  1 
ATOM   939  C CD  . ARG   A 1 143 ? -30.328 -26.027 -14.818 1.00 35.28  ? 680  ARG   A CD  1 
ATOM   940  N NE  . ARG   A 1 143 ? -31.660 -25.433 -14.768 1.00 37.30  ? 680  ARG   A NE  1 
ATOM   941  C CZ  . ARG   A 1 143 ? -32.664 -25.926 -14.046 1.00 39.00  ? 680  ARG   A CZ  1 
ATOM   942  N NH1 . ARG   A 1 143 ? -32.484 -27.021 -13.320 1.00 39.24  ? 680  ARG   A NH1 1 
ATOM   943  N NH2 . ARG   A 1 143 ? -33.850 -25.333 -14.050 1.00 40.13  ? 680  ARG   A NH2 1 
ATOM   944  N N   . LYS   A 1 144 ? -25.436 -27.285 -17.311 1.00 34.55  ? 681  LYS   A N   1 
ATOM   945  C CA  . LYS   A 1 144 ? -24.207 -28.011 -17.029 1.00 36.64  ? 681  LYS   A CA  1 
ATOM   946  C C   . LYS   A 1 144 ? -23.048 -27.545 -17.899 1.00 35.93  ? 681  LYS   A C   1 
ATOM   947  O O   . LYS   A 1 144 ? -21.901 -27.525 -17.437 1.00 36.55  ? 681  LYS   A O   1 
ATOM   948  C CB  . LYS   A 1 144 ? -24.435 -29.515 -17.207 1.00 40.25  ? 681  LYS   A CB  1 
ATOM   949  C CG  . LYS   A 1 144 ? -23.409 -30.392 -16.495 1.00 42.48  ? 681  LYS   A CG  1 
ATOM   950  C CD  . LYS   A 1 144 ? -23.869 -31.845 -16.431 1.00 45.02  ? 681  LYS   A CD  1 
ATOM   951  C CE  . LYS   A 1 144 ? -23.905 -32.473 -17.818 1.00 45.56  ? 681  LYS   A CE  1 
ATOM   952  N NZ  . LYS   A 1 144 ? -22.560 -32.466 -18.455 1.00 45.11  ? 681  LYS   A NZ  1 
ATOM   953  N N   . GLU   A 1 145 ? -23.319 -27.169 -19.148 1.00 34.67  ? 682  GLU   A N   1 
ATOM   954  C CA  . GLU   A 1 145 ? -22.260 -26.749 -20.053 1.00 33.78  ? 682  GLU   A CA  1 
ATOM   955  C C   . GLU   A 1 145 ? -22.074 -25.239 -20.102 1.00 31.04  ? 682  GLU   A C   1 
ATOM   956  O O   . GLU   A 1 145 ? -21.076 -24.776 -20.665 1.00 31.65  ? 682  GLU   A O   1 
ATOM   957  C CB  . GLU   A 1 145 ? -22.526 -27.271 -21.469 1.00 35.89  ? 682  GLU   A CB  1 
ATOM   958  C CG  . GLU   A 1 145 ? -22.646 -28.779 -21.562 1.00 38.82  ? 682  GLU   A CG  1 
ATOM   959  C CD  . GLU   A 1 145 ? -22.920 -29.255 -22.977 1.00 40.22  ? 682  GLU   A CD  1 
ATOM   960  O OE1 . GLU   A 1 145 ? -22.246 -28.774 -23.908 1.00 39.81  ? 682  GLU   A OE1 1 
ATOM   961  O OE2 . GLU   A 1 145 ? -23.821 -30.099 -23.161 1.00 41.44  ? 682  GLU   A OE2 1 
ATOM   962  N N   . TYR   A 1 146 ? -22.987 -24.460 -19.525 1.00 28.50  ? 683  TYR   A N   1 
ATOM   963  C CA  . TYR   A 1 146 ? -22.860 -23.012 -19.631 1.00 25.95  ? 683  TYR   A CA  1 
ATOM   964  C C   . TYR   A 1 146 ? -22.916 -22.314 -18.279 1.00 25.40  ? 683  TYR   A C   1 
ATOM   965  O O   . TYR   A 1 146 ? -21.946 -21.664 -17.875 1.00 24.15  ? 683  TYR   A O   1 
ATOM   966  C CB  . TYR   A 1 146 ? -23.943 -22.452 -20.552 1.00 24.95  ? 683  TYR   A CB  1 
ATOM   967  C CG  . TYR   A 1 146 ? -23.686 -21.033 -20.976 1.00 23.04  ? 683  TYR   A CG  1 
ATOM   968  C CD1 . TYR   A 1 146 ? -22.782 -20.745 -21.995 1.00 22.25  ? 683  TYR   A CD1 1 
ATOM   969  C CD2 . TYR   A 1 146 ? -24.338 -19.974 -20.356 1.00 22.60  ? 683  TYR   A CD2 1 
ATOM   970  C CE1 . TYR   A 1 146 ? -22.541 -19.438 -22.386 1.00 20.98  ? 683  TYR   A CE1 1 
ATOM   971  C CE2 . TYR   A 1 146 ? -24.102 -18.668 -20.740 1.00 20.79  ? 683  TYR   A CE2 1 
ATOM   972  C CZ  . TYR   A 1 146 ? -23.205 -18.407 -21.754 1.00 19.89  ? 683  TYR   A CZ  1 
ATOM   973  O OH  . TYR   A 1 146 ? -22.965 -17.112 -22.136 1.00 18.98  ? 683  TYR   A OH  1 
ATOM   974  N N   . VAL   A 1 147 ? -24.045 -22.440 -17.576 1.00 27.35  ? 684  VAL   A N   1 
ATOM   975  C CA  . VAL   A 1 147 ? -24.257 -21.667 -16.353 1.00 26.91  ? 684  VAL   A CA  1 
ATOM   976  C C   . VAL   A 1 147 ? -23.189 -21.995 -15.319 1.00 29.35  ? 684  VAL   A C   1 
ATOM   977  O O   . VAL   A 1 147 ? -22.503 -21.101 -14.807 1.00 29.72  ? 684  VAL   A O   1 
ATOM   978  C CB  . VAL   A 1 147 ? -25.672 -21.910 -15.799 1.00 25.93  ? 684  VAL   A CB  1 
ATOM   979  C CG1 . VAL   A 1 147 ? -25.855 -21.193 -14.472 1.00 24.67  ? 684  VAL   A CG1 1 
ATOM   980  C CG2 . VAL   A 1 147 ? -26.704 -21.438 -16.796 1.00 26.06  ? 684  VAL   A CG2 1 
ATOM   981  N N   . GLN   A 1 148 ? -23.024 -23.281 -15.003 1.00 31.39  ? 685  GLN   A N   1 
ATOM   982  C CA  . GLN   A 1 148 ? -22.029 -23.655 -13.999 1.00 33.97  ? 685  GLN   A CA  1 
ATOM   983  C C   . GLN   A 1 148 ? -20.609 -23.277 -14.405 1.00 31.20  ? 685  GLN   A C   1 
ATOM   984  O O   . GLN   A 1 148 ? -19.920 -22.625 -13.601 1.00 30.35  ? 685  GLN   A O   1 
ATOM   985  C CB  . GLN   A 1 148 ? -22.138 -25.147 -13.664 1.00 38.68  ? 685  GLN   A CB  1 
ATOM   986  C CG  . GLN   A 1 148 ? -21.087 -25.596 -12.658 1.00 41.84  ? 685  GLN   A CG  1 
ATOM   987  C CD  . GLN   A 1 148 ? -21.473 -26.863 -11.929 1.00 46.33  ? 685  GLN   A CD  1 
ATOM   988  O OE1 . GLN   A 1 148 ? -22.182 -26.823 -10.922 1.00 47.45  ? 685  GLN   A OE1 1 
ATOM   989  N NE2 . GLN   A 1 148 ? -21.004 -28.001 -12.431 1.00 48.35  ? 685  GLN   A NE2 1 
ATOM   990  N N   . PRO   A 1 149 ? -20.107 -23.631 -15.597 1.00 29.73  ? 686  PRO   A N   1 
ATOM   991  C CA  . PRO   A 1 149 ? -18.728 -23.231 -15.928 1.00 27.77  ? 686  PRO   A CA  1 
ATOM   992  C C   . PRO   A 1 149 ? -18.513 -21.725 -15.895 1.00 26.77  ? 686  PRO   A C   1 
ATOM   993  O O   . PRO   A 1 149 ? -17.506 -21.268 -15.343 1.00 26.39  ? 686  PRO   A O   1 
ATOM   994  C CB  . PRO   A 1 149 ? -18.521 -23.814 -17.334 1.00 27.57  ? 686  PRO   A CB  1 
ATOM   995  C CG  . PRO   A 1 149 ? -19.510 -24.923 -17.437 1.00 28.74  ? 686  PRO   A CG  1 
ATOM   996  C CD  . PRO   A 1 149 ? -20.698 -24.470 -16.658 1.00 29.81  ? 686  PRO   A CD  1 
ATOM   997  N N   . VAL   A 1 150 ? -19.443 -20.936 -16.446 1.00 26.39  ? 687  VAL   A N   1 
ATOM   998  C CA  . VAL   A 1 150 ? -19.276 -19.483 -16.462 1.00 24.58  ? 687  VAL   A CA  1 
ATOM   999  C C   . VAL   A 1 150 ? -19.211 -18.936 -15.041 1.00 23.89  ? 687  VAL   A C   1 
ATOM   1000 O O   . VAL   A 1 150 ? -18.322 -18.147 -14.701 1.00 23.82  ? 687  VAL   A O   1 
ATOM   1001 C CB  . VAL   A 1 150 ? -20.409 -18.815 -17.263 1.00 24.18  ? 687  VAL   A CB  1 
ATOM   1002 C CG1 . VAL   A 1 150 ? -20.424 -17.303 -17.001 1.00 24.21  ? 687  VAL   A CG1 1 
ATOM   1003 C CG2 . VAL   A 1 150 ? -20.242 -19.085 -18.738 1.00 23.82  ? 687  VAL   A CG2 1 
ATOM   1004 N N   . GLN   A 1 151 ? -20.159 -19.345 -14.192 1.00 23.99  ? 688  GLN   A N   1 
ATOM   1005 C CA  . GLN   A 1 151 ? -20.172 -18.868 -12.813 1.00 23.95  ? 688  GLN   A CA  1 
ATOM   1006 C C   . GLN   A 1 151 ? -18.903 -19.270 -12.068 1.00 24.32  ? 688  GLN   A C   1 
ATOM   1007 O O   . GLN   A 1 151 ? -18.420 -18.512 -11.220 1.00 24.90  ? 688  GLN   A O   1 
ATOM   1008 C CB  . GLN   A 1 151 ? -21.422 -19.383 -12.092 1.00 24.84  ? 688  GLN   A CB  1 
ATOM   1009 C CG  . GLN   A 1 151 ? -22.725 -18.780 -12.630 1.00 24.83  ? 688  GLN   A CG  1 
ATOM   1010 C CD  . GLN   A 1 151 ? -23.973 -19.284 -11.910 1.00 25.35  ? 688  GLN   A CD  1 
ATOM   1011 O OE1 . GLN   A 1 151 ? -23.981 -20.374 -11.339 1.00 25.65  ? 688  GLN   A OE1 1 
ATOM   1012 N NE2 . GLN   A 1 151 ? -25.037 -18.486 -11.944 1.00 24.84  ? 688  GLN   A NE2 1 
ATOM   1013 N N   . LEU   A 1 152 ? -18.334 -20.437 -12.380 1.00 24.85  ? 689  LEU   A N   1 
ATOM   1014 C CA  . LEU   A 1 152 ? -17.076 -20.831 -11.747 1.00 26.49  ? 689  LEU   A CA  1 
ATOM   1015 C C   . LEU   A 1 152 ? -15.911 -19.984 -12.250 1.00 27.18  ? 689  LEU   A C   1 
ATOM   1016 O O   . LEU   A 1 152 ? -15.009 -19.630 -11.477 1.00 27.42  ? 689  LEU   A O   1 
ATOM   1017 C CB  . LEU   A 1 152 ? -16.793 -22.314 -11.995 1.00 28.10  ? 689  LEU   A CB  1 
ATOM   1018 C CG  . LEU   A 1 152 ? -17.737 -23.331 -11.351 1.00 29.87  ? 689  LEU   A CG  1 
ATOM   1019 C CD1 . LEU   A 1 152 ? -17.347 -24.740 -11.757 1.00 30.92  ? 689  LEU   A CD1 1 
ATOM   1020 C CD2 . LEU   A 1 152 ? -17.745 -23.193 -9.837  1.00 30.49  ? 689  LEU   A CD2 1 
ATOM   1021 N N   . ARG   A 1 153 ? -15.909 -19.648 -13.543 1.00 26.92  ? 690  ARG   A N   1 
ATOM   1022 C CA  . ARG   A 1 153 ? -14.855 -18.784 -14.066 1.00 27.71  ? 690  ARG   A CA  1 
ATOM   1023 C C   . ARG   A 1 153 ? -14.902 -17.406 -13.423 1.00 25.30  ? 690  ARG   A C   1 
ATOM   1024 O O   . ARG   A 1 153 ? -13.855 -16.786 -13.202 1.00 23.46  ? 690  ARG   A O   1 
ATOM   1025 C CB  . ARG   A 1 153 ? -14.973 -18.668 -15.585 1.00 29.52  ? 690  ARG   A CB  1 
ATOM   1026 C CG  . ARG   A 1 153 ? -14.955 -20.010 -16.292 1.00 33.06  ? 690  ARG   A CG  1 
ATOM   1027 C CD  . ARG   A 1 153 ? -13.679 -20.271 -17.071 1.00 34.79  ? 690  ARG   A CD  1 
ATOM   1028 N NE  . ARG   A 1 153 ? -13.887 -21.378 -17.998 1.00 36.63  ? 690  ARG   A NE  1 
ATOM   1029 C CZ  . ARG   A 1 153 ? -13.618 -22.647 -17.717 1.00 39.28  ? 690  ARG   A CZ  1 
ATOM   1030 N NH1 . ARG   A 1 153 ? -13.104 -22.972 -16.539 1.00 40.13  ? 690  ARG   A NH1 1 
ATOM   1031 N NH2 . ARG   A 1 153 ? -13.851 -23.590 -18.621 1.00 40.91  ? 690  ARG   A NH2 1 
ATOM   1032 N N   . ILE   A 1 154 ? -16.103 -16.911 -13.118 1.00 24.66  ? 691  ILE   A N   1 
ATOM   1033 C CA  . ILE   A 1 154 ? -16.231 -15.640 -12.411 1.00 23.38  ? 691  ILE   A CA  1 
ATOM   1034 C C   . ILE   A 1 154 ? -15.648 -15.747 -11.011 1.00 24.14  ? 691  ILE   A C   1 
ATOM   1035 O O   . ILE   A 1 154 ? -14.920 -14.855 -10.556 1.00 24.26  ? 691  ILE   A O   1 
ATOM   1036 C CB  . ILE   A 1 154 ? -17.703 -15.203 -12.366 1.00 21.52  ? 691  ILE   A CB  1 
ATOM   1037 C CG1 . ILE   A 1 154 ? -18.230 -15.023 -13.786 1.00 20.22  ? 691  ILE   A CG1 1 
ATOM   1038 C CG2 . ILE   A 1 154 ? -17.870 -13.947 -11.516 1.00 16.92  ? 691  ILE   A CG2 1 
ATOM   1039 C CD1 . ILE   A 1 154 ? -19.701 -14.829 -13.834 1.00 20.70  ? 691  ILE   A CD1 1 
ATOM   1040 N N   . LEU   A 1 155 ? -15.964 -16.831 -10.301 1.00 24.57  ? 692  LEU   A N   1 
ATOM   1041 C CA  . LEU   A 1 155 ? -15.394 -17.018 -8.972  1.00 25.09  ? 692  LEU   A CA  1 
ATOM   1042 C C   . LEU   A 1 155 ? -13.877 -17.133 -9.040  1.00 23.55  ? 692  LEU   A C   1 
ATOM   1043 O O   . LEU   A 1 155 ? -13.173 -16.662 -8.139  1.00 23.44  ? 692  LEU   A O   1 
ATOM   1044 C CB  . LEU   A 1 155 ? -16.009 -18.247 -8.301  1.00 26.71  ? 692  LEU   A CB  1 
ATOM   1045 C CG  . LEU   A 1 155 ? -17.505 -18.132 -7.975  1.00 27.96  ? 692  LEU   A CG  1 
ATOM   1046 C CD1 . LEU   A 1 155 ? -18.064 -19.446 -7.449  1.00 29.22  ? 692  LEU   A CD1 1 
ATOM   1047 C CD2 . LEU   A 1 155 ? -17.756 -17.013 -6.981  1.00 28.30  ? 692  LEU   A CD2 1 
ATOM   1048 N N   . ASN   A 1 156 ? -13.356 -17.742 -10.107 1.00 22.22  ? 693  ASN   A N   1 
ATOM   1049 C CA  . ASN   A 1 156 ? -11.911 -17.780 -10.294 1.00 22.55  ? 693  ASN   A CA  1 
ATOM   1050 C C   . ASN   A 1 156 ? -11.347 -16.380 -10.503 1.00 21.64  ? 693  ASN   A C   1 
ATOM   1051 O O   . ASN   A 1 156 ? -10.275 -16.051 -9.983  1.00 19.29  ? 693  ASN   A O   1 
ATOM   1052 C CB  . ASN   A 1 156 ? -11.563 -18.691 -11.467 1.00 22.73  ? 693  ASN   A CB  1 
ATOM   1053 C CG  . ASN   A 1 156 ? -10.080 -18.910 -11.601 1.00 24.70  ? 693  ASN   A CG  1 
ATOM   1054 O OD1 . ASN   A 1 156 ? -9.437  -19.405 -10.677 1.00 27.33  ? 693  ASN   A OD1 1 
ATOM   1055 N ND2 . ASN   A 1 156 ? -9.523  -18.546 -12.750 1.00 23.53  ? 693  ASN   A ND2 1 
ATOM   1056 N N   . VAL   A 1 157 ? -12.062 -15.539 -11.251 1.00 17.96  ? 694  VAL   A N   1 
ATOM   1057 C CA  . VAL   A 1 157 ? -11.625 -14.159 -11.453 1.00 24.53  ? 694  VAL   A CA  1 
ATOM   1058 C C   . VAL   A 1 157 ? -11.614 -13.395 -10.128 1.00 26.67  ? 694  VAL   A C   1 
ATOM   1059 O O   . VAL   A 1 157 ? -10.633 -12.714 -9.801  1.00 25.28  ? 694  VAL   A O   1 
ATOM   1060 C CB  . VAL   A 1 157 ? -12.511 -13.468 -12.508 1.00 23.68  ? 694  VAL   A CB  1 
ATOM   1061 C CG1 . VAL   A 1 157 ? -12.225 -11.966 -12.560 1.00 17.15  ? 694  VAL   A CG1 1 
ATOM   1062 C CG2 . VAL   A 1 157 ? -12.290 -14.107 -13.880 1.00 17.03  ? 694  VAL   A CG2 1 
ATOM   1063 N N   . PHE   A 1 158 ? -12.701 -13.491 -9.348  1.00 18.10  ? 695  PHE   A N   1 
ATOM   1064 C CA  . PHE   A 1 158 ? -12.730 -12.871 -8.022  1.00 19.45  ? 695  PHE   A CA  1 
ATOM   1065 C C   . PHE   A 1 158 ? -11.533 -13.303 -7.178  1.00 24.02  ? 695  PHE   A C   1 
ATOM   1066 O O   . PHE   A 1 158 ? -10.922 -12.484 -6.481  1.00 24.53  ? 695  PHE   A O   1 
ATOM   1067 C CB  . PHE   A 1 158 ? -14.025 -13.232 -7.282  1.00 18.88  ? 695  PHE   A CB  1 
ATOM   1068 C CG  . PHE   A 1 158 ? -15.262 -12.549 -7.803  1.00 20.26  ? 695  PHE   A CG  1 
ATOM   1069 C CD1 . PHE   A 1 158 ? -15.185 -11.357 -8.510  1.00 21.00  ? 695  PHE   A CD1 1 
ATOM   1070 C CD2 . PHE   A 1 158 ? -16.517 -13.102 -7.563  1.00 21.97  ? 695  PHE   A CD2 1 
ATOM   1071 C CE1 . PHE   A 1 158 ? -16.338 -10.734 -8.972  1.00 17.82  ? 695  PHE   A CE1 1 
ATOM   1072 C CE2 . PHE   A 1 158 ? -17.671 -12.488 -8.023  1.00 18.76  ? 695  PHE   A CE2 1 
ATOM   1073 C CZ  . PHE   A 1 158 ? -17.583 -11.303 -8.732  1.00 17.98  ? 695  PHE   A CZ  1 
ATOM   1074 N N   . ARG   A 1 159 ? -11.185 -14.594 -7.235  1.00 26.66  ? 696  ARG   A N   1 
ATOM   1075 C CA  . ARG   A 1 159 ? -10.095 -15.123 -6.419  1.00 28.40  ? 696  ARG   A CA  1 
ATOM   1076 C C   . ARG   A 1 159 ? -8.743  -14.575 -6.869  1.00 27.47  ? 696  ARG   A C   1 
ATOM   1077 O O   . ARG   A 1 159 ? -7.893  -14.241 -6.038  1.00 27.34  ? 696  ARG   A O   1 
ATOM   1078 C CB  . ARG   A 1 159 ? -10.096 -16.652 -6.476  1.00 31.32  ? 696  ARG   A CB  1 
ATOM   1079 C CG  . ARG   A 1 159 ? -8.984  -17.302 -5.665  1.00 35.77  ? 696  ARG   A CG  1 
ATOM   1080 C CD  . ARG   A 1 159 ? -9.033  -18.825 -5.744  1.00 39.28  ? 696  ARG   A CD  1 
ATOM   1081 N NE  . ARG   A 1 159 ? -8.684  -19.329 -7.070  1.00 41.69  ? 696  ARG   A NE  1 
ATOM   1082 C CZ  . ARG   A 1 159 ? -8.665  -20.618 -7.394  1.00 43.54  ? 696  ARG   A CZ  1 
ATOM   1083 N NH1 . ARG   A 1 159 ? -8.337  -20.997 -8.622  1.00 43.49  ? 696  ARG   A NH1 1 
ATOM   1084 N NH2 . ARG   A 1 159 ? -8.981  -21.530 -6.486  1.00 44.79  ? 696  ARG   A NH2 1 
ATOM   1085 N N   . HIS   A 1 160 ? -8.518  -14.493 -8.182  1.00 26.07  ? 697  HIS   A N   1 
ATOM   1086 C CA  . HIS   A 1 160 ? -7.297  -13.881 -8.699  1.00 25.39  ? 697  HIS   A CA  1 
ATOM   1087 C C   . HIS   A 1 160 ? -7.249  -12.398 -8.355  1.00 23.98  ? 697  HIS   A C   1 
ATOM   1088 O O   . HIS   A 1 160 ? -6.174  -11.852 -8.089  1.00 23.70  ? 697  HIS   A O   1 
ATOM   1089 C CB  . HIS   A 1 160 ? -7.225  -14.104 -10.210 1.00 27.07  ? 697  HIS   A CB  1 
ATOM   1090 C CG  . HIS   A 1 160 ? -5.931  -13.684 -10.842 1.00 31.39  ? 697  HIS   A CG  1 
ATOM   1091 N ND1 . HIS   A 1 160 ? -5.005  -14.588 -11.318 1.00 33.24  ? 697  HIS   A ND1 1 
ATOM   1092 C CD2 . HIS   A 1 160 ? -5.430  -12.457 -11.122 1.00 32.17  ? 697  HIS   A CD2 1 
ATOM   1093 C CE1 . HIS   A 1 160 ? -3.978  -13.937 -11.837 1.00 33.38  ? 697  HIS   A CE1 1 
ATOM   1094 N NE2 . HIS   A 1 160 ? -4.209  -12.642 -11.726 1.00 32.77  ? 697  HIS   A NE2 1 
ATOM   1095 N N   . TRP   A 1 161 ? -8.412  -11.743 -8.325  1.00 23.46  ? 698  TRP   A N   1 
ATOM   1096 C CA  . TRP   A 1 161 ? -8.480  -10.306 -8.073  1.00 22.33  ? 698  TRP   A CA  1 
ATOM   1097 C C   . TRP   A 1 161 ? -7.988  -9.977  -6.666  1.00 23.21  ? 698  TRP   A C   1 
ATOM   1098 O O   . TRP   A 1 161 ? -7.030  -9.216  -6.486  1.00 23.41  ? 698  TRP   A O   1 
ATOM   1099 C CB  . TRP   A 1 161 ? -9.923  -9.835  -8.287  1.00 21.18  ? 698  TRP   A CB  1 
ATOM   1100 C CG  . TRP   A 1 161 ? -10.158 -8.353  -8.434  1.00 21.47  ? 698  TRP   A CG  1 
ATOM   1101 C CD1 . TRP   A 1 161 ? -9.255  -7.339  -8.266  1.00 21.49  ? 698  TRP   A CD1 1 
ATOM   1102 C CD2 . TRP   A 1 161 ? -11.401 -7.727  -8.783  1.00 21.80  ? 698  TRP   A CD2 1 
ATOM   1103 N NE1 . TRP   A 1 161 ? -9.862  -6.122  -8.489  1.00 20.44  ? 698  TRP   A NE1 1 
ATOM   1104 C CE2 . TRP   A 1 161 ? -11.180 -6.335  -8.804  1.00 23.74  ? 698  TRP   A CE2 1 
ATOM   1105 C CE3 . TRP   A 1 161 ? -12.681 -8.211  -9.074  1.00 19.38  ? 698  TRP   A CE3 1 
ATOM   1106 C CZ2 . TRP   A 1 161 ? -12.194 -5.425  -9.110  1.00 23.50  ? 698  TRP   A CZ2 1 
ATOM   1107 C CZ3 . TRP   A 1 161 ? -13.680 -7.312  -9.380  1.00 19.44  ? 698  TRP   A CZ3 1 
ATOM   1108 C CH2 . TRP   A 1 161 ? -13.435 -5.933  -9.396  1.00 21.07  ? 698  TRP   A CH2 1 
ATOM   1109 N N   . VAL   A 1 162 ? -8.609  -10.587 -5.652  1.00 23.43  ? 699  VAL   A N   1 
ATOM   1110 C CA  . VAL   A 1 162 ? -8.249  -10.300 -4.267  1.00 25.18  ? 699  VAL   A CA  1 
ATOM   1111 C C   . VAL   A 1 162 ? -6.887  -10.871 -3.890  1.00 23.92  ? 699  VAL   A C   1 
ATOM   1112 O O   . VAL   A 1 162 ? -6.261  -10.378 -2.944  1.00 25.09  ? 699  VAL   A O   1 
ATOM   1113 C CB  . VAL   A 1 162 ? -9.341  -10.824 -3.314  1.00 26.13  ? 699  VAL   A CB  1 
ATOM   1114 C CG1 . VAL   A 1 162 ? -10.665 -10.138 -3.601  1.00 22.14  ? 699  VAL   A CG1 1 
ATOM   1115 C CG2 . VAL   A 1 162 ? -9.489  -12.335 -3.453  1.00 22.78  ? 699  VAL   A CG2 1 
ATOM   1116 N N   . GLU   A 1 163 ? -6.403  -11.895 -4.601  1.00 23.80  ? 700  GLU   A N   1 
ATOM   1117 C CA  . GLU   A 1 163 ? -5.081  -12.438 -4.296  1.00 31.52  ? 700  GLU   A CA  1 
ATOM   1118 C C   . GLU   A 1 163 ? -3.960  -11.527 -4.787  1.00 31.50  ? 700  GLU   A C   1 
ATOM   1119 O O   . GLU   A 1 163 ? -2.988  -11.294 -4.063  1.00 31.93  ? 700  GLU   A O   1 
ATOM   1120 C CB  . GLU   A 1 163 ? -4.912  -13.829 -4.904  1.00 31.08  ? 700  GLU   A CB  1 
ATOM   1121 C CG  . GLU   A 1 163 ? -3.551  -14.443 -4.625  1.00 33.47  ? 700  GLU   A CG  1 
ATOM   1122 C CD  . GLU   A 1 163 ? -3.330  -14.738 -3.147  1.00 36.50  ? 700  GLU   A CD  1 
ATOM   1123 O OE1 . GLU   A 1 163 ? -3.911  -15.716 -2.631  1.00 37.41  ? 700  GLU   A OE1 1 
ATOM   1124 O OE2 . GLU   A 1 163 ? -2.580  -13.986 -2.492  1.00 38.38  ? 700  GLU   A OE2 1 
ATOM   1125 N N   . HIS   A 1 164 ? -4.071  -11.000 -6.005  1.00 24.79  ? 701  HIS   A N   1 
ATOM   1126 C CA  . HIS   A 1 164 ? -2.960  -10.295 -6.620  1.00 28.02  ? 701  HIS   A CA  1 
ATOM   1127 C C   . HIS   A 1 164 ? -3.217  -8.813  -6.845  1.00 28.45  ? 701  HIS   A C   1 
ATOM   1128 O O   . HIS   A 1 164 ? -2.300  -8.102  -7.272  1.00 26.03  ? 701  HIS   A O   1 
ATOM   1129 C CB  . HIS   A 1 164 ? -2.599  -10.950 -7.960  1.00 27.14  ? 701  HIS   A CB  1 
ATOM   1130 C CG  . HIS   A 1 164 ? -2.236  -12.399 -7.853  1.00 28.86  ? 701  HIS   A CG  1 
ATOM   1131 N ND1 . HIS   A 1 164 ? -0.940  -12.826 -7.667  1.00 31.27  ? 701  HIS   A ND1 1 
ATOM   1132 C CD2 . HIS   A 1 164 ? -2.996  -13.519 -7.932  1.00 28.83  ? 701  HIS   A CD2 1 
ATOM   1133 C CE1 . HIS   A 1 164 ? -0.918  -14.147 -7.629  1.00 31.69  ? 701  HIS   A CE1 1 
ATOM   1134 N NE2 . HIS   A 1 164 ? -2.152  -14.592 -7.789  1.00 29.92  ? 701  HIS   A NE2 1 
ATOM   1135 N N   . HIS   A 1 165 ? -4.426  -8.328  -6.580  1.00 26.91  ? 702  HIS   A N   1 
ATOM   1136 C CA  . HIS   A 1 165 ? -4.741  -6.921  -6.784  1.00 26.56  ? 702  HIS   A CA  1 
ATOM   1137 C C   . HIS   A 1 165 ? -5.601  -6.401  -5.641  1.00 27.94  ? 702  HIS   A C   1 
ATOM   1138 O O   . HIS   A 1 165 ? -6.534  -5.619  -5.848  1.00 24.60  ? 702  HIS   A O   1 
ATOM   1139 C CB  . HIS   A 1 165 ? -5.413  -6.705  -8.142  1.00 25.39  ? 702  HIS   A CB  1 
ATOM   1140 C CG  . HIS   A 1 165 ? -4.596  -7.208  -9.293  1.00 23.64  ? 702  HIS   A CG  1 
ATOM   1141 N ND1 . HIS   A 1 165 ? -3.461  -6.563  -9.736  1.00 22.37  ? 702  HIS   A ND1 1 
ATOM   1142 C CD2 . HIS   A 1 165 ? -4.721  -8.315  -10.064 1.00 23.26  ? 702  HIS   A CD2 1 
ATOM   1143 C CE1 . HIS   A 1 165 ? -2.934  -7.239  -10.741 1.00 21.77  ? 702  HIS   A CE1 1 
ATOM   1144 N NE2 . HIS   A 1 165 ? -3.679  -8.306  -10.960 1.00 22.58  ? 702  HIS   A NE2 1 
ATOM   1145 N N   . PHE   A 1 166 ? -5.286  -6.819  -4.411  1.00 29.00  ? 703  PHE   A N   1 
ATOM   1146 C CA  . PHE   A 1 166 ? -6.067  -6.400  -3.255  1.00 30.18  ? 703  PHE   A CA  1 
ATOM   1147 C C   . PHE   A 1 166 ? -5.951  -4.908  -2.967  1.00 29.84  ? 703  PHE   A C   1 
ATOM   1148 O O   . PHE   A 1 166 ? -6.732  -4.391  -2.162  1.00 30.30  ? 703  PHE   A O   1 
ATOM   1149 C CB  . PHE   A 1 166 ? -5.655  -7.201  -2.015  1.00 31.97  ? 703  PHE   A CB  1 
ATOM   1150 C CG  . PHE   A 1 166 ? -6.651  -7.122  -0.891  1.00 33.91  ? 703  PHE   A CG  1 
ATOM   1151 C CD1 . PHE   A 1 166 ? -7.817  -7.872  -0.927  1.00 34.45  ? 703  PHE   A CD1 1 
ATOM   1152 C CD2 . PHE   A 1 166 ? -6.431  -6.289  0.194   1.00 35.27  ? 703  PHE   A CD2 1 
ATOM   1153 C CE1 . PHE   A 1 166 ? -8.744  -7.800  0.101   1.00 35.91  ? 703  PHE   A CE1 1 
ATOM   1154 C CE2 . PHE   A 1 166 ? -7.352  -6.213  1.225   1.00 36.54  ? 703  PHE   A CE2 1 
ATOM   1155 C CZ  . PHE   A 1 166 ? -8.510  -6.972  1.180   1.00 36.89  ? 703  PHE   A CZ  1 
ATOM   1156 N N   . TYR   A 1 167 ? -5.009  -4.204  -3.596  1.00 28.98  ? 704  TYR   A N   1 
ATOM   1157 C CA  . TYR   A 1 167 ? -4.940  -2.759  -3.423  1.00 29.52  ? 704  TYR   A CA  1 
ATOM   1158 C C   . TYR   A 1 167 ? -6.176  -2.063  -3.978  1.00 30.16  ? 704  TYR   A C   1 
ATOM   1159 O O   . TYR   A 1 167 ? -6.496  -0.952  -3.544  1.00 31.37  ? 704  TYR   A O   1 
ATOM   1160 C CB  . TYR   A 1 167 ? -3.676  -2.214  -4.085  1.00 29.78  ? 704  TYR   A CB  1 
ATOM   1161 C CG  . TYR   A 1 167 ? -3.466  -2.704  -5.497  1.00 29.36  ? 704  TYR   A CG  1 
ATOM   1162 C CD1 . TYR   A 1 167 ? -4.141  -2.119  -6.563  1.00 27.87  ? 704  TYR   A CD1 1 
ATOM   1163 C CD2 . TYR   A 1 167 ? -2.596  -3.757  -5.766  1.00 28.26  ? 704  TYR   A CD2 1 
ATOM   1164 C CE1 . TYR   A 1 167 ? -3.954  -2.567  -7.857  1.00 27.01  ? 704  TYR   A CE1 1 
ATOM   1165 C CE2 . TYR   A 1 167 ? -2.401  -4.209  -7.057  1.00 27.17  ? 704  TYR   A CE2 1 
ATOM   1166 C CZ  . TYR   A 1 167 ? -3.084  -3.612  -8.099  1.00 26.48  ? 704  TYR   A CZ  1 
ATOM   1167 O OH  . TYR   A 1 167 ? -2.900  -4.054  -9.387  1.00 25.83  ? 704  TYR   A OH  1 
ATOM   1168 N N   . ASP   A 1 168 ? -6.870  -2.689  -4.940  1.00 29.79  ? 705  ASP   A N   1 
ATOM   1169 C CA  . ASP   A 1 168 ? -8.144  -2.154  -5.413  1.00 30.24  ? 705  ASP   A CA  1 
ATOM   1170 C C   . ASP   A 1 168 ? -9.143  -2.040  -4.269  1.00 32.35  ? 705  ASP   A C   1 
ATOM   1171 O O   . ASP   A 1 168 ? -9.943  -1.101  -4.225  1.00 32.39  ? 705  ASP   A O   1 
ATOM   1172 C CB  . ASP   A 1 168 ? -8.729  -3.046  -6.511  1.00 29.60  ? 705  ASP   A CB  1 
ATOM   1173 C CG  . ASP   A 1 168 ? -8.057  -2.862  -7.861  1.00 27.59  ? 705  ASP   A CG  1 
ATOM   1174 O OD1 . ASP   A 1 168 ? -7.247  -1.930  -8.026  1.00 27.09  ? 705  ASP   A OD1 1 
ATOM   1175 O OD2 . ASP   A 1 168 ? -8.357  -3.670  -8.764  1.00 26.49  ? 705  ASP   A OD2 1 
ATOM   1176 N N   . PHE   A 1 169 ? -9.119  -2.999  -3.344  1.00 33.63  ? 706  PHE   A N   1 
ATOM   1177 C CA  . PHE   A 1 169 ? -10.046 -3.021  -2.224  1.00 36.57  ? 706  PHE   A CA  1 
ATOM   1178 C C   . PHE   A 1 169 ? -9.549  -2.220  -1.027  1.00 38.38  ? 706  PHE   A C   1 
ATOM   1179 O O   . PHE   A 1 169 ? -10.365 -1.803  -0.197  1.00 39.29  ? 706  PHE   A O   1 
ATOM   1180 C CB  . PHE   A 1 169 ? -10.328 -4.476  -1.830  1.00 37.65  ? 706  PHE   A CB  1 
ATOM   1181 C CG  . PHE   A 1 169 ? -10.839 -5.315  -2.975  1.00 37.12  ? 706  PHE   A CG  1 
ATOM   1182 C CD1 . PHE   A 1 169 ? -12.176 -5.266  -3.343  1.00 37.88  ? 706  PHE   A CD1 1 
ATOM   1183 C CD2 . PHE   A 1 169 ? -9.980  -6.128  -3.698  1.00 35.62  ? 706  PHE   A CD2 1 
ATOM   1184 C CE1 . PHE   A 1 169 ? -12.649 -6.020  -4.403  1.00 37.30  ? 706  PHE   A CE1 1 
ATOM   1185 C CE2 . PHE   A 1 169 ? -10.445 -6.881  -4.760  1.00 35.39  ? 706  PHE   A CE2 1 
ATOM   1186 C CZ  . PHE   A 1 169 ? -11.783 -6.829  -5.112  1.00 36.46  ? 706  PHE   A CZ  1 
ATOM   1187 N N   . GLU   A 1 170 ? -8.240  -1.978  -0.926  1.00 39.44  ? 707  GLU   A N   1 
ATOM   1188 C CA  . GLU   A 1 170 ? -7.741  -1.073  0.106   1.00 41.21  ? 707  GLU   A CA  1 
ATOM   1189 C C   . GLU   A 1 170 ? -8.102  0.372   -0.216  1.00 41.94  ? 707  GLU   A C   1 
ATOM   1190 O O   . GLU   A 1 170 ? -8.421  1.154   0.687   1.00 43.52  ? 707  GLU   A O   1 
ATOM   1191 C CB  . GLU   A 1 170 ? -6.226  -1.226  0.259   1.00 41.45  ? 707  GLU   A CB  1 
ATOM   1192 C CG  . GLU   A 1 170 ? -5.797  -2.556  0.870   1.00 42.98  ? 707  GLU   A CG  1 
ATOM   1193 C CD  . GLU   A 1 170 ? -4.325  -2.871  0.647   1.00 43.05  ? 707  GLU   A CD  1 
ATOM   1194 O OE1 . GLU   A 1 170 ? -3.615  -2.031  0.059   1.00 42.51  ? 707  GLU   A OE1 1 
ATOM   1195 O OE2 . GLU   A 1 170 ? -3.876  -3.965  1.057   1.00 43.48  ? 707  GLU   A OE2 1 
ATOM   1196 N N   . ARG   A 1 171 ? -8.069  0.736   -1.502  1.00 40.72  ? 708  ARG   A N   1 
ATOM   1197 C CA  . ARG   A 1 171 ? -8.360  2.104   -1.916  1.00 41.31  ? 708  ARG   A CA  1 
ATOM   1198 C C   . ARG   A 1 171 ? -9.852  2.393   -1.952  1.00 41.95  ? 708  ARG   A C   1 
ATOM   1199 O O   . ARG   A 1 171 ? -10.263 3.535   -1.724  1.00 43.77  ? 708  ARG   A O   1 
ATOM   1200 C CB  . ARG   A 1 171 ? -7.759  2.378   -3.294  1.00 41.33  ? 708  ARG   A CB  1 
ATOM   1201 C CG  . ARG   A 1 171 ? -6.257  2.187   -3.363  1.00 41.66  ? 708  ARG   A CG  1 
ATOM   1202 C CD  . ARG   A 1 171 ? -5.797  2.038   -4.800  1.00 41.41  ? 708  ARG   A CD  1 
ATOM   1203 N NE  . ARG   A 1 171 ? -4.360  1.798   -4.901  1.00 41.88  ? 708  ARG   A NE  1 
ATOM   1204 C CZ  . ARG   A 1 171 ? -3.730  1.529   -6.041  1.00 41.01  ? 708  ARG   A CZ  1 
ATOM   1205 N NH1 . ARG   A 1 171 ? -4.412  1.462   -7.178  1.00 40.75  ? 708  ARG   A NH1 1 
ATOM   1206 N NH2 . ARG   A 1 171 ? -2.420  1.326   -6.045  1.00 40.04  ? 708  ARG   A NH2 1 
ATOM   1207 N N   . ASP   A 1 172 ? -10.669 1.382   -2.235  1.00 41.49  ? 709  ASP   A N   1 
ATOM   1208 C CA  . ASP   A 1 172 ? -12.112 1.539   -2.383  1.00 41.53  ? 709  ASP   A CA  1 
ATOM   1209 C C   . ASP   A 1 172 ? -12.803 0.575   -1.426  1.00 43.52  ? 709  ASP   A C   1 
ATOM   1210 O O   . ASP   A 1 172 ? -12.749 -0.645  -1.624  1.00 42.28  ? 709  ASP   A O   1 
ATOM   1211 C CB  . ASP   A 1 172 ? -12.531 1.282   -3.830  1.00 39.64  ? 709  ASP   A CB  1 
ATOM   1212 C CG  . ASP   A 1 172 ? -13.880 1.859   -4.154  1.00 38.09  ? 709  ASP   A CG  1 
ATOM   1213 O OD1 . ASP   A 1 172 ? -14.690 2.005   -3.215  1.00 38.82  ? 709  ASP   A OD1 1 
ATOM   1214 O OD2 . ASP   A 1 172 ? -14.126 2.168   -5.338  1.00 36.46  ? 709  ASP   A OD2 1 
ATOM   1215 N N   . LEU   A 1 173 ? -13.465 1.122   -0.399  1.00 45.78  ? 710  LEU   A N   1 
ATOM   1216 C CA  . LEU   A 1 173 ? -14.124 0.298   0.610   1.00 47.22  ? 710  LEU   A CA  1 
ATOM   1217 C C   . LEU   A 1 173 ? -15.508 -0.178  0.190   1.00 47.39  ? 710  LEU   A C   1 
ATOM   1218 O O   . LEU   A 1 173 ? -15.906 -1.291  0.553   1.00 47.66  ? 710  LEU   A O   1 
ATOM   1219 C CB  . LEU   A 1 173 ? -14.238 1.057   1.931   1.00 48.49  ? 710  LEU   A CB  1 
ATOM   1220 C CG  . LEU   A 1 173 ? -12.949 1.208   2.719   1.00 49.50  ? 710  LEU   A CG  1 
ATOM   1221 C CD1 . LEU   A 1 173 ? -13.255 1.299   4.206   1.00 51.07  ? 710  LEU   A CD1 1 
ATOM   1222 C CD2 . LEU   A 1 173 ? -11.993 0.052   2.429   1.00 49.51  ? 710  LEU   A CD2 1 
ATOM   1223 N N   . GLU   A 1 174 ? -16.264 0.643   -0.547  1.00 47.31  ? 711  GLU   A N   1 
ATOM   1224 C CA  . GLU   A 1 174 ? -17.535 0.170   -1.090  1.00 46.76  ? 711  GLU   A CA  1 
ATOM   1225 C C   . GLU   A 1 174 ? -17.309 -0.945  -2.099  1.00 41.72  ? 711  GLU   A C   1 
ATOM   1226 O O   . GLU   A 1 174 ? -18.161 -1.826  -2.249  1.00 42.18  ? 711  GLU   A O   1 
ATOM   1227 C CB  . GLU   A 1 174 ? -18.323 1.323   -1.734  1.00 48.86  ? 711  GLU   A CB  1 
ATOM   1228 C CG  . GLU   A 1 174 ? -19.862 1.251   -1.566  1.00 51.91  ? 711  GLU   A CG  1 
ATOM   1229 C CD  . GLU   A 1 174 ? -20.633 1.151   -2.890  1.00 53.30  ? 711  GLU   A CD  1 
ATOM   1230 O OE1 . GLU   A 1 174 ? -20.124 1.626   -3.929  1.00 54.23  ? 711  GLU   A OE1 1 
ATOM   1231 O OE2 . GLU   A 1 174 ? -21.754 0.590   -2.889  1.00 52.79  ? 711  GLU   A OE2 1 
ATOM   1232 N N   . LEU   A 1 175 ? -16.168 -0.930  -2.791  1.00 37.60  ? 712  LEU   A N   1 
ATOM   1233 C CA  . LEU   A 1 175 ? -15.854 -2.009  -3.724  1.00 34.16  ? 712  LEU   A CA  1 
ATOM   1234 C C   . LEU   A 1 175 ? -15.782 -3.347  -3.001  1.00 32.39  ? 712  LEU   A C   1 
ATOM   1235 O O   . LEU   A 1 175 ? -16.387 -4.336  -3.432  1.00 30.66  ? 712  LEU   A O   1 
ATOM   1236 C CB  . LEU   A 1 175 ? -14.535 -1.718  -4.445  1.00 32.28  ? 712  LEU   A CB  1 
ATOM   1237 C CG  . LEU   A 1 175 ? -14.110 -2.695  -5.546  1.00 28.61  ? 712  LEU   A CG  1 
ATOM   1238 C CD1 . LEU   A 1 175 ? -15.030 -2.579  -6.752  1.00 26.67  ? 712  LEU   A CD1 1 
ATOM   1239 C CD2 . LEU   A 1 175 ? -12.670 -2.451  -5.950  1.00 27.81  ? 712  LEU   A CD2 1 
ATOM   1240 N N   . LEU   A 1 176 ? -15.051 -3.388  -1.885  1.00 33.72  ? 713  LEU   A N   1 
ATOM   1241 C CA  . LEU   A 1 176 ? -14.915 -4.622  -1.121  1.00 35.38  ? 713  LEU   A CA  1 
ATOM   1242 C C   . LEU   A 1 176 ? -16.258 -5.074  -0.559  1.00 37.12  ? 713  LEU   A C   1 
ATOM   1243 O O   . LEU   A 1 176 ? -16.627 -6.250  -0.671  1.00 36.32  ? 713  LEU   A O   1 
ATOM   1244 C CB  . LEU   A 1 176 ? -13.890 -4.424  -0.002  1.00 36.00  ? 713  LEU   A CB  1 
ATOM   1245 C CG  . LEU   A 1 176 ? -13.522 -5.624  0.876   1.00 36.53  ? 713  LEU   A CG  1 
ATOM   1246 C CD1 . LEU   A 1 176 ? -13.075 -6.793  0.015   1.00 35.33  ? 713  LEU   A CD1 1 
ATOM   1247 C CD2 . LEU   A 1 176 ? -12.428 -5.238  1.859   1.00 36.62  ? 713  LEU   A CD2 1 
ATOM   1248 N N   . GLU   A 1 177 ? -17.014 -4.146  0.037   1.00 38.46  ? 714  GLU   A N   1 
ATOM   1249 C CA  . GLU   A 1 177 ? -18.295 -4.512  0.637   1.00 40.56  ? 714  GLU   A CA  1 
ATOM   1250 C C   . GLU   A 1 177 ? -19.273 -5.050  -0.402  1.00 37.68  ? 714  GLU   A C   1 
ATOM   1251 O O   . GLU   A 1 177 ? -20.053 -5.961  -0.109  1.00 39.35  ? 714  GLU   A O   1 
ATOM   1252 C CB  . GLU   A 1 177 ? -18.901 -3.318  1.372   1.00 44.58  ? 714  GLU   A CB  1 
ATOM   1253 C CG  . GLU   A 1 177 ? -18.291 -3.045  2.734   1.00 48.61  ? 714  GLU   A CG  1 
ATOM   1254 C CD  . GLU   A 1 177 ? -18.866 -1.804  3.376   1.00 53.01  ? 714  GLU   A CD  1 
ATOM   1255 O OE1 . GLU   A 1 177 ? -20.009 -1.442  3.025   1.00 54.65  ? 714  GLU   A OE1 1 
ATOM   1256 O OE2 . GLU   A 1 177 ? -18.176 -1.186  4.217   1.00 54.71  ? 714  GLU   A OE2 1 
ATOM   1257 N N   . ARG   A 1 178 ? -19.255 -4.502  -1.620  1.00 33.19  ? 715  ARG   A N   1 
ATOM   1258 C CA  . ARG   A 1 178 ? -20.108 -5.050  -2.671  1.00 30.92  ? 715  ARG   A CA  1 
ATOM   1259 C C   . ARG   A 1 178 ? -19.722 -6.489  -2.990  1.00 30.76  ? 715  ARG   A C   1 
ATOM   1260 O O   . ARG   A 1 178 ? -20.582 -7.376  -3.062  1.00 32.53  ? 715  ARG   A O   1 
ATOM   1261 C CB  . ARG   A 1 178 ? -20.032 -4.186  -3.929  1.00 30.64  ? 715  ARG   A CB  1 
ATOM   1262 C CG  . ARG   A 1 178 ? -20.826 -2.896  -3.872  1.00 29.37  ? 715  ARG   A CG  1 
ATOM   1263 C CD  . ARG   A 1 178 ? -20.729 -2.178  -5.201  1.00 28.13  ? 715  ARG   A CD  1 
ATOM   1264 N NE  . ARG   A 1 178 ? -21.334 -2.966  -6.269  1.00 27.31  ? 715  ARG   A NE  1 
ATOM   1265 C CZ  . ARG   A 1 178 ? -21.031 -2.846  -7.557  1.00 26.13  ? 715  ARG   A CZ  1 
ATOM   1266 N NH1 . ARG   A 1 178 ? -20.114 -1.974  -7.952  1.00 25.63  ? 715  ARG   A NH1 1 
ATOM   1267 N NH2 . ARG   A 1 178 ? -21.642 -3.610  -8.450  1.00 25.52  ? 715  ARG   A NH2 1 
ATOM   1268 N N   . LEU   A 1 179 ? -18.424 -6.736  -3.182  1.00 30.05  ? 716  LEU   A N   1 
ATOM   1269 C CA  . LEU   A 1 179 ? -17.947 -8.086  -3.471  1.00 30.14  ? 716  LEU   A CA  1 
ATOM   1270 C C   . LEU   A 1 179 ? -18.320 -9.053  -2.355  1.00 31.89  ? 716  LEU   A C   1 
ATOM   1271 O O   . LEU   A 1 179 ? -18.807 -10.160 -2.611  1.00 31.51  ? 716  LEU   A O   1 
ATOM   1272 C CB  . LEU   A 1 179 ? -16.432 -8.066  -3.675  1.00 28.62  ? 716  LEU   A CB  1 
ATOM   1273 C CG  . LEU   A 1 179 ? -15.745 -9.421  -3.838  1.00 30.10  ? 716  LEU   A CG  1 
ATOM   1274 C CD1 . LEU   A 1 179 ? -16.246 -10.145 -5.086  1.00 27.71  ? 716  LEU   A CD1 1 
ATOM   1275 C CD2 . LEU   A 1 179 ? -14.240 -9.240  -3.888  1.00 28.09  ? 716  LEU   A CD2 1 
ATOM   1276 N N   . GLU   A 1 180 ? -18.093 -8.647  -1.103  1.00 33.84  ? 717  GLU   A N   1 
ATOM   1277 C CA  . GLU   A 1 180 ? -18.415 -9.509  0.027   1.00 35.54  ? 717  GLU   A CA  1 
ATOM   1278 C C   . GLU   A 1 180 ? -19.915 -9.713  0.154   1.00 35.95  ? 717  GLU   A C   1 
ATOM   1279 O O   . GLU   A 1 180 ? -20.372 -10.802 0.523   1.00 36.65  ? 717  GLU   A O   1 
ATOM   1280 C CB  . GLU   A 1 180 ? -17.843 -8.919  1.310   1.00 37.46  ? 717  GLU   A CB  1 
ATOM   1281 C CG  . GLU   A 1 180 ? -16.338 -8.850  1.309   1.00 38.93  ? 717  GLU   A CG  1 
ATOM   1282 C CD  . GLU   A 1 180 ? -15.775 -8.443  2.649   1.00 42.39  ? 717  GLU   A CD  1 
ATOM   1283 O OE1 . GLU   A 1 180 ? -16.379 -7.570  3.313   1.00 42.57  ? 717  GLU   A OE1 1 
ATOM   1284 O OE2 . GLU   A 1 180 ? -14.731 -9.008  3.038   1.00 44.52  ? 717  GLU   A OE2 1 
ATOM   1285 N N   . SER   A 1 181 ? -20.699 -8.676  -0.141  1.00 35.22  ? 718  SER   A N   1 
ATOM   1286 C CA  . SER   A 1 181 ? -22.145 -8.842  -0.156  1.00 34.77  ? 718  SER   A CA  1 
ATOM   1287 C C   . SER   A 1 181 ? -22.560 -9.844  -1.222  1.00 34.09  ? 718  SER   A C   1 
ATOM   1288 O O   . SER   A 1 181 ? -23.391 -10.724 -0.966  1.00 35.37  ? 718  SER   A O   1 
ATOM   1289 C CB  . SER   A 1 181 ? -22.825 -7.492  -0.380  1.00 34.46  ? 718  SER   A CB  1 
ATOM   1290 O OG  . SER   A 1 181 ? -24.225 -7.644  -0.544  1.00 35.45  ? 718  SER   A OG  1 
ATOM   1291 N N   . PHE   A 1 182 ? -21.968 -9.747  -2.416  1.00 32.62  ? 719  PHE   A N   1 
ATOM   1292 C CA  . PHE   A 1 182 ? -22.378 -10.620 -3.511  1.00 33.26  ? 719  PHE   A CA  1 
ATOM   1293 C C   . PHE   A 1 182 ? -22.033 -12.079 -3.227  1.00 33.52  ? 719  PHE   A C   1 
ATOM   1294 O O   . PHE   A 1 182 ? -22.868 -12.972 -3.423  1.00 32.99  ? 719  PHE   A O   1 
ATOM   1295 C CB  . PHE   A 1 182 ? -21.739 -10.177 -4.826  1.00 32.57  ? 719  PHE   A CB  1 
ATOM   1296 C CG  . PHE   A 1 182 ? -21.997 -11.132 -5.957  1.00 33.13  ? 719  PHE   A CG  1 
ATOM   1297 C CD1 . PHE   A 1 182 ? -23.206 -11.111 -6.634  1.00 33.63  ? 719  PHE   A CD1 1 
ATOM   1298 C CD2 . PHE   A 1 182 ? -21.051 -12.076 -6.316  1.00 33.06  ? 719  PHE   A CD2 1 
ATOM   1299 C CE1 . PHE   A 1 182 ? -23.458 -11.999 -7.659  1.00 32.80  ? 719  PHE   A CE1 1 
ATOM   1300 C CE2 . PHE   A 1 182 ? -21.300 -12.965 -7.337  1.00 33.07  ? 719  PHE   A CE2 1 
ATOM   1301 C CZ  . PHE   A 1 182 ? -22.505 -12.928 -8.010  1.00 32.52  ? 719  PHE   A CZ  1 
ATOM   1302 N N   . ILE   A 1 183 ? -20.797 -12.349 -2.794  1.00 34.02  ? 720  ILE   A N   1 
ATOM   1303 C CA  . ILE   A 1 183 ? -20.398 -13.737 -2.566  1.00 35.07  ? 720  ILE   A CA  1 
ATOM   1304 C C   . ILE   A 1 183 ? -21.234 -14.355 -1.457  1.00 37.82  ? 720  ILE   A C   1 
ATOM   1305 O O   . ILE   A 1 183 ? -21.458 -15.572 -1.441  1.00 38.91  ? 720  ILE   A O   1 
ATOM   1306 C CB  . ILE   A 1 183 ? -18.883 -13.838 -2.273  1.00 34.37  ? 720  ILE   A CB  1 
ATOM   1307 C CG1 . ILE   A 1 183 ? -18.521 -13.096 -0.986  1.00 35.83  ? 720  ILE   A CG1 1 
ATOM   1308 C CG2 . ILE   A 1 183 ? -18.068 -13.314 -3.456  1.00 31.51  ? 720  ILE   A CG2 1 
ATOM   1309 C CD1 . ILE   A 1 183 ? -17.046 -13.107 -0.678  1.00 36.22  ? 720  ILE   A CD1 1 
ATOM   1310 N N   . SER   A 1 184 ? -21.736 -13.534 -0.534  1.00 39.86  ? 721  SER   A N   1 
ATOM   1311 C CA  . SER   A 1 184 ? -22.658 -14.025 0.480   1.00 42.95  ? 721  SER   A CA  1 
ATOM   1312 C C   . SER   A 1 184 ? -24.049 -14.309 -0.073  1.00 43.82  ? 721  SER   A C   1 
ATOM   1313 O O   . SER   A 1 184 ? -24.848 -14.947 0.617   1.00 46.37  ? 721  SER   A O   1 
ATOM   1314 C CB  . SER   A 1 184 ? -22.759 -13.023 1.627   1.00 45.21  ? 721  SER   A CB  1 
ATOM   1315 O OG  . SER   A 1 184 ? -24.066 -12.483 1.709   1.00 47.10  ? 721  SER   A OG  1 
ATOM   1316 N N   . SER   A 1 185 ? -24.357 -13.860 -1.288  1.00 42.25  ? 722  SER   A N   1 
ATOM   1317 C CA  . SER   A 1 185 ? -25.626 -14.179 -1.928  1.00 42.30  ? 722  SER   A CA  1 
ATOM   1318 C C   . SER   A 1 185 ? -25.551 -15.421 -2.802  1.00 43.10  ? 722  SER   A C   1 
ATOM   1319 O O   . SER   A 1 185 ? -26.579 -15.839 -3.345  1.00 42.95  ? 722  SER   A O   1 
ATOM   1320 C CB  . SER   A 1 185 ? -26.107 -13.005 -2.785  1.00 41.20  ? 722  SER   A CB  1 
ATOM   1321 O OG  . SER   A 1 185 ? -25.402 -12.950 -4.015  1.00 39.40  ? 722  SER   A OG  1 
ATOM   1322 N N   . VAL   A 1 186 ? -24.368 -16.008 -2.965  1.00 43.87  ? 723  VAL   A N   1 
ATOM   1323 C CA  . VAL   A 1 186 ? -24.201 -17.169 -3.832  1.00 45.08  ? 723  VAL   A CA  1 
ATOM   1324 C C   . VAL   A 1 186 ? -24.721 -18.407 -3.111  1.00 49.08  ? 723  VAL   A C   1 
ATOM   1325 O O   . VAL   A 1 186 ? -24.272 -18.729 -2.006  1.00 48.71  ? 723  VAL   A O   1 
ATOM   1326 C CB  . VAL   A 1 186 ? -22.733 -17.346 -4.245  1.00 42.96  ? 723  VAL   A CB  1 
ATOM   1327 C CG1 . VAL   A 1 186 ? -22.581 -18.556 -5.140  1.00 42.50  ? 723  VAL   A CG1 1 
ATOM   1328 C CG2 . VAL   A 1 186 ? -22.229 -16.102 -4.946  1.00 41.13  ? 723  VAL   A CG2 1 
ATOM   1329 N N   . ARG   A 1 187 ? -25.675 -19.095 -3.732  1.00 53.24  ? 724  ARG   A N   1 
ATOM   1330 C CA  . ARG   A 1 187 ? -26.213 -20.344 -3.216  1.00 59.03  ? 724  ARG   A CA  1 
ATOM   1331 C C   . ARG   A 1 187 ? -25.698 -21.507 -4.054  1.00 60.23  ? 724  ARG   A C   1 
ATOM   1332 O O   . ARG   A 1 187 ? -25.468 -21.369 -5.260  1.00 59.59  ? 724  ARG   A O   1 
ATOM   1333 C CB  . ARG   A 1 187 ? -27.746 -20.340 -3.227  1.00 61.31  ? 724  ARG   A CB  1 
ATOM   1334 C CG  . ARG   A 1 187 ? -28.396 -19.220 -2.423  1.00 63.70  ? 724  ARG   A CG  1 
ATOM   1335 C CD  . ARG   A 1 187 ? -28.328 -19.470 -0.920  1.00 67.04  ? 724  ARG   A CD  1 
ATOM   1336 N NE  . ARG   A 1 187 ? -27.095 -18.965 -0.320  1.00 68.36  ? 724  ARG   A NE  1 
ATOM   1337 C CZ  . ARG   A 1 187 ? -26.942 -17.730 0.151   1.00 69.00  ? 724  ARG   A CZ  1 
ATOM   1338 N NH1 . ARG   A 1 187 ? -27.945 -16.863 0.091   1.00 69.07  ? 724  ARG   A NH1 1 
ATOM   1339 N NH2 . ARG   A 1 187 ? -25.783 -17.361 0.681   1.00 69.14  ? 724  ARG   A NH2 1 
ATOM   1340 N N   . GLY   A 1 188 ? -25.515 -22.654 -3.405  1.00 62.43  ? 725  GLY   A N   1 
ATOM   1341 C CA  . GLY   A 1 188 ? -25.089 -23.847 -4.111  1.00 63.24  ? 725  GLY   A CA  1 
ATOM   1342 C C   . GLY   A 1 188 ? -23.914 -24.539 -3.457  1.00 65.02  ? 725  GLY   A C   1 
ATOM   1343 O O   . GLY   A 1 188 ? -22.906 -23.896 -3.149  1.00 65.37  ? 725  GLY   A O   1 
ATOM   1344 N N   . LYS   A 1 189 ? -24.032 -25.850 -3.237  1.00 66.41  ? 726  LYS   A N   1 
ATOM   1345 C CA  . LYS   A 1 189 ? -22.952 -26.589 -2.593  1.00 67.90  ? 726  LYS   A CA  1 
ATOM   1346 C C   . LYS   A 1 189 ? -21.691 -26.579 -3.445  1.00 66.63  ? 726  LYS   A C   1 
ATOM   1347 O O   . LYS   A 1 189 ? -20.576 -26.496 -2.915  1.00 66.87  ? 726  LYS   A O   1 
ATOM   1348 C CB  . LYS   A 1 189 ? -23.388 -28.029 -2.314  1.00 69.87  ? 726  LYS   A CB  1 
ATOM   1349 C CG  . LYS   A 1 189 ? -24.549 -28.159 -1.351  1.00 72.16  ? 726  LYS   A CG  1 
ATOM   1350 C CD  . LYS   A 1 189 ? -24.924 -29.618 -1.144  1.00 74.17  ? 726  LYS   A CD  1 
ATOM   1351 C CE  . LYS   A 1 189 ? -26.126 -29.759 -0.221  1.00 76.23  ? 726  LYS   A CE  1 
ATOM   1352 N NZ  . LYS   A 1 189 ? -26.545 -31.182 -0.061  1.00 78.24  ? 726  LYS   A NZ  1 
ATOM   1353 N N   . ALA   A 1 190 ? -21.846 -26.649 -4.770  1.00 65.37  ? 727  ALA   A N   1 
ATOM   1354 C CA  . ALA   A 1 190 ? -20.693 -26.768 -5.654  1.00 64.57  ? 727  ALA   A CA  1 
ATOM   1355 C C   . ALA   A 1 190 ? -19.804 -25.534 -5.624  1.00 63.40  ? 727  ALA   A C   1 
ATOM   1356 O O   . ALA   A 1 190 ? -18.653 -25.605 -6.066  1.00 62.53  ? 727  ALA   A O   1 
ATOM   1357 C CB  . ALA   A 1 190 ? -21.155 -27.048 -7.086  1.00 63.88  ? 727  ALA   A CB  1 
ATOM   1358 N N   . MET   A 1 191 ? -20.306 -24.413 -5.111  1.00 63.15  ? 728  MET   A N   1 
ATOM   1359 C CA  . MET   A 1 191 ? -19.571 -23.160 -5.104  1.00 61.61  ? 728  MET   A CA  1 
ATOM   1360 C C   . MET   A 1 191 ? -19.143 -22.732 -3.709  1.00 62.02  ? 728  MET   A C   1 
ATOM   1361 O O   . MET   A 1 191 ? -18.431 -21.729 -3.578  1.00 61.24  ? 728  MET   A O   1 
ATOM   1362 C CB  . MET   A 1 191 ? -20.421 -22.064 -5.755  1.00 60.70  ? 728  MET   A CB  1 
ATOM   1363 C CG  . MET   A 1 191 ? -21.162 -22.553 -6.982  1.00 60.61  ? 728  MET   A CG  1 
ATOM   1364 S SD  . MET   A 1 191 ? -21.194 -21.374 -8.338  1.00 59.46  ? 728  MET   A SD  1 
ATOM   1365 C CE  . MET   A 1 191 ? -22.865 -20.739 -8.199  1.00 59.73  ? 728  MET   A CE  1 
ATOM   1366 N N   . LYS   A 1 192 ? -19.550 -23.465 -2.667  1.00 63.02  ? 729  LYS   A N   1 
ATOM   1367 C CA  . LYS   A 1 192 ? -19.192 -23.072 -1.308  1.00 63.10  ? 729  LYS   A CA  1 
ATOM   1368 C C   . LYS   A 1 192 ? -17.694 -23.187 -1.065  1.00 61.63  ? 729  LYS   A C   1 
ATOM   1369 O O   . LYS   A 1 192 ? -17.139 -22.414 -0.277  1.00 61.31  ? 729  LYS   A O   1 
ATOM   1370 C CB  . LYS   A 1 192 ? -19.972 -23.907 -0.294  1.00 65.25  ? 729  LYS   A CB  1 
ATOM   1371 C CG  . LYS   A 1 192 ? -21.424 -23.481 -0.165  1.00 66.34  ? 729  LYS   A CG  1 
ATOM   1372 C CD  . LYS   A 1 192 ? -21.527 -22.010 0.212   1.00 66.62  ? 729  LYS   A CD  1 
ATOM   1373 C CE  . LYS   A 1 192 ? -22.853 -21.420 -0.236  1.00 67.22  ? 729  LYS   A CE  1 
ATOM   1374 N NZ  . LYS   A 1 192 ? -22.964 -21.417 -1.721  1.00 65.98  ? 729  LYS   A NZ  1 
ATOM   1375 N N   . LYS   A 1 193 ? -17.025 -24.129 -1.736  1.00 60.52  ? 730  LYS   A N   1 
ATOM   1376 C CA  . LYS   A 1 193 ? -15.572 -24.218 -1.635  1.00 58.62  ? 730  LYS   A CA  1 
ATOM   1377 C C   . LYS   A 1 193 ? -14.908 -22.966 -2.187  1.00 53.92  ? 730  LYS   A C   1 
ATOM   1378 O O   . LYS   A 1 193 ? -13.918 -22.478 -1.626  1.00 52.86  ? 730  LYS   A O   1 
ATOM   1379 C CB  . LYS   A 1 193 ? -15.072 -25.456 -2.372  1.00 60.13  ? 730  LYS   A CB  1 
ATOM   1380 C CG  . LYS   A 1 193 ? -15.668 -26.734 -1.842  1.00 64.89  ? 730  LYS   A CG  1 
ATOM   1381 C CD  . LYS   A 1 193 ? -14.986 -27.961 -2.424  1.00 68.12  ? 730  LYS   A CD  1 
ATOM   1382 C CE  . LYS   A 1 193 ? -15.974 -28.878 -3.133  1.00 70.89  ? 730  LYS   A CE  1 
ATOM   1383 N NZ  . LYS   A 1 193 ? -16.072 -28.565 -4.586  1.00 70.41  ? 730  LYS   A NZ  1 
ATOM   1384 N N   . TRP   A 1 194 ? -15.437 -22.437 -3.291  1.00 49.82  ? 731  TRP   A N   1 
ATOM   1385 C CA  . TRP   A 1 194 ? -14.901 -21.206 -3.861  1.00 45.09  ? 731  TRP   A CA  1 
ATOM   1386 C C   . TRP   A 1 194 ? -15.206 -20.008 -2.969  1.00 42.67  ? 731  TRP   A C   1 
ATOM   1387 O O   . TRP   A 1 194 ? -14.318 -19.200 -2.673  1.00 40.11  ? 731  TRP   A O   1 
ATOM   1388 C CB  . TRP   A 1 194 ? -15.472 -20.987 -5.260  1.00 42.95  ? 731  TRP   A CB  1 
ATOM   1389 C CG  . TRP   A 1 194 ? -14.911 -21.892 -6.313  1.00 41.47  ? 731  TRP   A CG  1 
ATOM   1390 C CD1 . TRP   A 1 194 ? -15.394 -23.112 -6.692  1.00 41.40  ? 731  TRP   A CD1 1 
ATOM   1391 C CD2 . TRP   A 1 194 ? -13.773 -21.636 -7.143  1.00 40.37  ? 731  TRP   A CD2 1 
ATOM   1392 N NE1 . TRP   A 1 194 ? -14.620 -23.634 -7.699  1.00 40.95  ? 731  TRP   A NE1 1 
ATOM   1393 C CE2 . TRP   A 1 194 ? -13.619 -22.746 -7.995  1.00 40.72  ? 731  TRP   A CE2 1 
ATOM   1394 C CE3 . TRP   A 1 194 ? -12.867 -20.576 -7.245  1.00 39.55  ? 731  TRP   A CE3 1 
ATOM   1395 C CZ2 . TRP   A 1 194 ? -12.596 -22.827 -8.935  1.00 40.14  ? 731  TRP   A CZ2 1 
ATOM   1396 C CZ3 . TRP   A 1 194 ? -11.856 -20.657 -8.177  1.00 39.09  ? 731  TRP   A CZ3 1 
ATOM   1397 C CH2 . TRP   A 1 194 ? -11.727 -21.775 -9.009  1.00 39.56  ? 731  TRP   A CH2 1 
ATOM   1398 N N   . VAL   A 1 195 ? -16.465 -19.874 -2.537  1.00 43.74  ? 732  VAL   A N   1 
ATOM   1399 C CA  . VAL   A 1 195 ? -16.866 -18.721 -1.734  1.00 44.71  ? 732  VAL   A CA  1 
ATOM   1400 C C   . VAL   A 1 195 ? -16.023 -18.632 -0.471  1.00 45.36  ? 732  VAL   A C   1 
ATOM   1401 O O   . VAL   A 1 195 ? -15.589 -17.546 -0.068  1.00 45.49  ? 732  VAL   A O   1 
ATOM   1402 C CB  . VAL   A 1 195 ? -18.371 -18.792 -1.410  1.00 46.53  ? 732  VAL   A CB  1 
ATOM   1403 C CG1 . VAL   A 1 195 ? -18.721 -17.842 -0.275  1.00 48.00  ? 732  VAL   A CG1 1 
ATOM   1404 C CG2 . VAL   A 1 195 ? -19.191 -18.462 -2.644  1.00 45.73  ? 732  VAL   A CG2 1 
ATOM   1405 N N   . GLU   A 1 196 ? -15.757 -19.773 0.159   1.00 46.17  ? 733  GLU   A N   1 
ATOM   1406 C CA  . GLU   A 1 196 ? -14.964 -19.781 1.378   1.00 47.50  ? 733  GLU   A CA  1 
ATOM   1407 C C   . GLU   A 1 196 ? -13.474 -19.627 1.105   1.00 45.06  ? 733  GLU   A C   1 
ATOM   1408 O O   . GLU   A 1 196 ? -12.736 -19.208 2.002   1.00 46.77  ? 733  GLU   A O   1 
ATOM   1409 C CB  . GLU   A 1 196 ? -15.248 -21.062 2.165   1.00 51.54  ? 733  GLU   A CB  1 
ATOM   1410 C CG  . GLU   A 1 196 ? -16.661 -21.076 2.747   1.00 54.76  ? 733  GLU   A CG  1 
ATOM   1411 C CD  . GLU   A 1 196 ? -17.219 -22.472 2.955   1.00 57.27  ? 733  GLU   A CD  1 
ATOM   1412 O OE1 . GLU   A 1 196 ? -16.506 -23.454 2.650   1.00 57.72  ? 733  GLU   A OE1 1 
ATOM   1413 O OE2 . GLU   A 1 196 ? -18.376 -22.583 3.419   1.00 58.53  ? 733  GLU   A OE2 1 
ATOM   1414 N N   . SER   A 1 197 ? -13.020 -19.934 -0.111  1.00 41.75  ? 734  SER   A N   1 
ATOM   1415 C CA  . SER   A 1 197 ? -11.636 -19.651 -0.472  1.00 40.90  ? 734  SER   A CA  1 
ATOM   1416 C C   . SER   A 1 197 ? -11.426 -18.157 -0.704  1.00 39.05  ? 734  SER   A C   1 
ATOM   1417 O O   . SER   A 1 197 ? -10.387 -17.601 -0.325  1.00 37.67  ? 734  SER   A O   1 
ATOM   1418 C CB  . SER   A 1 197 ? -11.250 -20.453 -1.717  1.00 42.26  ? 734  SER   A CB  1 
ATOM   1419 O OG  . SER   A 1 197 ? -9.908  -20.213 -2.108  1.00 42.63  ? 734  SER   A OG  1 
ATOM   1420 N N   . ILE   A 1 198 ? -12.401 -17.494 -1.332  1.00 38.39  ? 735  ILE   A N   1 
ATOM   1421 C CA  . ILE   A 1 198 ? -12.325 -16.047 -1.518  1.00 36.55  ? 735  ILE   A CA  1 
ATOM   1422 C C   . ILE   A 1 198 ? -12.303 -15.334 -0.170  1.00 37.82  ? 735  ILE   A C   1 
ATOM   1423 O O   . ILE   A 1 198 ? -11.511 -14.410 0.046   1.00 36.75  ? 735  ILE   A O   1 
ATOM   1424 C CB  . ILE   A 1 198 ? -13.494 -15.566 -2.399  1.00 33.20  ? 735  ILE   A CB  1 
ATOM   1425 C CG1 . ILE   A 1 198 ? -13.263 -15.987 -3.854  1.00 30.18  ? 735  ILE   A CG1 1 
ATOM   1426 C CG2 . ILE   A 1 198 ? -13.695 -14.053 -2.252  1.00 31.01  ? 735  ILE   A CG2 1 
ATOM   1427 C CD1 . ILE   A 1 198 ? -14.520 -16.394 -4.584  1.00 29.85  ? 735  ILE   A CD1 1 
ATOM   1428 N N   . ALA   A 1 199 ? -13.168 -15.757 0.758   1.00 39.87  ? 736  ALA   A N   1 
ATOM   1429 C CA  . ALA   A 1 199 ? -13.211 -15.125 2.076   1.00 40.71  ? 736  ALA   A CA  1 
ATOM   1430 C C   . ALA   A 1 199 ? -11.918 -15.363 2.846   1.00 40.73  ? 736  ALA   A C   1 
ATOM   1431 O O   . ALA   A 1 199 ? -11.452 -14.485 3.580   1.00 40.45  ? 736  ALA   A O   1 
ATOM   1432 C CB  . ALA   A 1 199 ? -14.411 -15.640 2.871   1.00 41.25  ? 736  ALA   A CB  1 
ATOM   1433 N N   . LYS   A 1 200 ? -11.323 -16.547 2.683   1.00 41.96  ? 737  LYS   A N   1 
ATOM   1434 C CA  . LYS   A 1 200 ? -10.070 -16.860 3.361   1.00 43.51  ? 737  LYS   A CA  1 
ATOM   1435 C C   . LYS   A 1 200 ? -8.933  -15.987 2.847   1.00 44.17  ? 737  LYS   A C   1 
ATOM   1436 O O   . LYS   A 1 200 ? -8.063  -15.570 3.623   1.00 45.40  ? 737  LYS   A O   1 
ATOM   1437 C CB  . LYS   A 1 200 ? -9.749  -18.343 3.180   1.00 44.22  ? 737  LYS   A CB  1 
ATOM   1438 C CG  . LYS   A 1 200 ? -8.405  -18.783 3.724   1.00 45.11  ? 737  LYS   A CG  1 
ATOM   1439 C CD  . LYS   A 1 200 ? -8.167  -20.261 3.439   1.00 45.78  ? 737  LYS   A CD  1 
ATOM   1440 C CE  . LYS   A 1 200 ? -6.691  -20.549 3.206   1.00 45.71  ? 737  LYS   A CE  1 
ATOM   1441 N NZ  . LYS   A 1 200 ? -6.134  -21.507 4.205   1.00 47.70  ? 737  LYS   A NZ  1 
ATOM   1442 N N   . ILE   A 1 201 ? -8.928  -15.690 1.546   1.00 42.93  ? 738  ILE   A N   1 
ATOM   1443 C CA  . ILE   A 1 201 ? -7.919  -14.788 0.998   1.00 42.10  ? 738  ILE   A CA  1 
ATOM   1444 C C   . ILE   A 1 201 ? -8.124  -13.375 1.531   1.00 42.30  ? 738  ILE   A C   1 
ATOM   1445 O O   . ILE   A 1 201 ? -7.173  -12.719 1.974   1.00 42.11  ? 738  ILE   A O   1 
ATOM   1446 C CB  . ILE   A 1 201 ? -7.945  -14.820 -0.540  1.00 40.31  ? 738  ILE   A CB  1 
ATOM   1447 C CG1 . ILE   A 1 201 ? -7.443  -16.175 -1.042  1.00 40.34  ? 738  ILE   A CG1 1 
ATOM   1448 C CG2 . ILE   A 1 201 ? -7.110  -13.674 -1.111  1.00 39.15  ? 738  ILE   A CG2 1 
ATOM   1449 C CD1 . ILE   A 1 201 ? -7.375  -16.288 -2.548  1.00 38.77  ? 738  ILE   A CD1 1 
ATOM   1450 N N   . ILE   A 1 202 ? -9.369  -12.890 1.503   1.00 42.26  ? 739  ILE   A N   1 
ATOM   1451 C CA  . ILE   A 1 202 ? -9.653  -11.540 1.981   1.00 43.28  ? 739  ILE   A CA  1 
ATOM   1452 C C   . ILE   A 1 202 ? -9.265  -11.398 3.446   1.00 47.80  ? 739  ILE   A C   1 
ATOM   1453 O O   . ILE   A 1 202 ? -8.678  -10.387 3.852   1.00 47.98  ? 739  ILE   A O   1 
ATOM   1454 C CB  . ILE   A 1 202 ? -11.136 -11.191 1.758   1.00 42.18  ? 739  ILE   A CB  1 
ATOM   1455 C CG1 . ILE   A 1 202 ? -11.481 -11.233 0.271   1.00 39.57  ? 739  ILE   A CG1 1 
ATOM   1456 C CG2 . ILE   A 1 202 ? -11.450 -9.817  2.339   1.00 42.29  ? 739  ILE   A CG2 1 
ATOM   1457 C CD1 . ILE   A 1 202 ? -12.945 -11.006 -0.004  1.00 39.40  ? 739  ILE   A CD1 1 
ATOM   1458 N N   . ARG   A 1 203 ? -9.579  -12.411 4.260   1.00 51.44  ? 740  ARG   A N   1 
ATOM   1459 C CA  . ARG   A 1 203 ? -9.215  -12.360 5.673   1.00 54.60  ? 740  ARG   A CA  1 
ATOM   1460 C C   . ARG   A 1 203 ? -7.701  -12.302 5.855   1.00 54.41  ? 740  ARG   A C   1 
ATOM   1461 O O   . ARG   A 1 203 ? -7.201  -11.549 6.699   1.00 55.00  ? 740  ARG   A O   1 
ATOM   1462 C CB  . ARG   A 1 203 ? -9.803  -13.559 6.418   1.00 57.67  ? 740  ARG   A CB  1 
ATOM   1463 C CG  . ARG   A 1 203 ? -11.324 -13.538 6.548   1.00 60.05  ? 740  ARG   A CG  1 
ATOM   1464 C CD  . ARG   A 1 203 ? -11.814 -14.580 7.549   1.00 63.09  ? 740  ARG   A CD  1 
ATOM   1465 N NE  . ARG   A 1 203 ? -11.206 -15.886 7.307   1.00 64.78  ? 740  ARG   A NE  1 
ATOM   1466 C CZ  . ARG   A 1 203 ? -11.799 -16.891 6.667   1.00 65.40  ? 740  ARG   A CZ  1 
ATOM   1467 N NH1 . ARG   A 1 203 ? -13.037 -16.754 6.208   1.00 65.21  ? 740  ARG   A NH1 1 
ATOM   1468 N NH2 . ARG   A 1 203 ? -11.155 -18.038 6.492   1.00 65.71  ? 740  ARG   A NH2 1 
ATOM   1469 N N   . ARG   A 1 204 ? -6.952  -13.088 5.074   1.00 53.00  ? 741  ARG   A N   1 
ATOM   1470 C CA  . ARG   A 1 204 ? -5.495  -13.020 5.157   1.00 52.85  ? 741  ARG   A CA  1 
ATOM   1471 C C   . ARG   A 1 204 ? -4.985  -11.636 4.778   1.00 52.43  ? 741  ARG   A C   1 
ATOM   1472 O O   . ARG   A 1 204 ? -4.003  -11.152 5.353   1.00 53.32  ? 741  ARG   A O   1 
ATOM   1473 C CB  . ARG   A 1 204 ? -4.859  -14.088 4.264   1.00 52.39  ? 741  ARG   A CB  1 
ATOM   1474 C CG  . ARG   A 1 204 ? -3.400  -13.812 3.880   1.00 51.28  ? 741  ARG   A CG  1 
ATOM   1475 C CD  . ARG   A 1 204 ? -2.756  -15.034 3.235   1.00 51.18  ? 741  ARG   A CD  1 
ATOM   1476 N NE  . ARG   A 1 204 ? -3.584  -15.601 2.172   1.00 50.99  ? 741  ARG   A NE  1 
ATOM   1477 C CZ  . ARG   A 1 204 ? -3.348  -15.452 0.871   1.00 49.24  ? 741  ARG   A CZ  1 
ATOM   1478 N NH1 . ARG   A 1 204 ? -2.299  -14.757 0.454   1.00 47.87  ? 741  ARG   A NH1 1 
ATOM   1479 N NH2 . ARG   A 1 204 ? -4.163  -16.006 -0.018  1.00 49.12  ? 741  ARG   A NH2 1 
ATOM   1480 N N   . LYS   A 1 205 ? -5.652  -10.976 3.827   1.00 50.50  ? 742  LYS   A N   1 
ATOM   1481 C CA  . LYS   A 1 205 ? -5.221  -9.650  3.398   1.00 48.29  ? 742  LYS   A CA  1 
ATOM   1482 C C   . LYS   A 1 205 ? -5.571  -8.591  4.437   1.00 51.62  ? 742  LYS   A C   1 
ATOM   1483 O O   . LYS   A 1 205 ? -4.735  -7.746  4.775   1.00 51.69  ? 742  LYS   A O   1 
ATOM   1484 C CB  . LYS   A 1 205 ? -5.851  -9.310  2.047   1.00 43.28  ? 742  LYS   A CB  1 
ATOM   1485 C CG  . LYS   A 1 205 ? -5.462  -10.248 0.918   1.00 39.44  ? 742  LYS   A CG  1 
ATOM   1486 C CD  . LYS   A 1 205 ? -4.060  -9.965  0.414   1.00 37.15  ? 742  LYS   A CD  1 
ATOM   1487 C CE  . LYS   A 1 205 ? -3.712  -10.854 -0.764  1.00 35.07  ? 742  LYS   A CE  1 
ATOM   1488 N NZ  . LYS   A 1 205 ? -2.446  -10.442 -1.424  1.00 33.67  ? 742  LYS   A NZ  1 
ATOM   1489 N N   . LYS   A 1 206 ? -6.802  -8.631  4.966   1.00 54.84  ? 743  LYS   A N   1 
ATOM   1490 C CA  . LYS   A 1 206 ? -7.267  -7.574  5.863   1.00 58.21  ? 743  LYS   A CA  1 
ATOM   1491 C C   . LYS   A 1 206 ? -6.384  -7.438  7.098   1.00 63.28  ? 743  LYS   A C   1 
ATOM   1492 O O   . LYS   A 1 206 ? -6.271  -6.341  7.657   1.00 64.29  ? 743  LYS   A O   1 
ATOM   1493 C CB  . LYS   A 1 206 ? -8.717  -7.830  6.280   1.00 57.65  ? 743  LYS   A CB  1 
ATOM   1494 C CG  . LYS   A 1 206 ? -9.762  -7.177  5.381   1.00 55.81  ? 743  LYS   A CG  1 
ATOM   1495 C CD  . LYS   A 1 206 ? -11.132 -7.166  6.051   1.00 56.34  ? 743  LYS   A CD  1 
ATOM   1496 C CE  . LYS   A 1 206 ? -12.197 -6.563  5.148   1.00 55.11  ? 743  LYS   A CE  1 
ATOM   1497 N NZ  . LYS   A 1 206 ? -13.532 -6.478  5.808   1.00 55.82  ? 743  LYS   A NZ  1 
ATOM   1498 N N   . GLN   A 1 207 ? -5.745  -8.525  7.534   1.00 66.90  ? 744  GLN   A N   1 
ATOM   1499 C CA  . GLN   A 1 207 ? -4.922  -8.449  8.735   1.00 71.47  ? 744  GLN   A CA  1 
ATOM   1500 C C   . GLN   A 1 207 ? -3.547  -7.854  8.447   1.00 71.82  ? 744  GLN   A C   1 
ATOM   1501 O O   . GLN   A 1 207 ? -3.029  -7.074  9.255   1.00 73.15  ? 744  GLN   A O   1 
ATOM   1502 C CB  . GLN   A 1 207 ? -4.791  -9.833  9.373   1.00 74.24  ? 744  GLN   A CB  1 
ATOM   1503 C CG  . GLN   A 1 207 ? -6.076  -10.324 10.022  1.00 77.23  ? 744  GLN   A CG  1 
ATOM   1504 C CD  . GLN   A 1 207 ? -5.826  -11.202 11.235  1.00 80.45  ? 744  GLN   A CD  1 
ATOM   1505 O OE1 . GLN   A 1 207 ? -4.791  -11.862 11.336  1.00 81.23  ? 744  GLN   A OE1 1 
ATOM   1506 N NE2 . GLN   A 1 207 ? -6.771  -11.204 12.169  1.00 82.06  ? 744  GLN   A NE2 1 
ATOM   1507 N N   . ALA   A 1 208 ? -2.953  -8.196  7.306   1.00 70.64  ? 745  ALA   A N   1 
ATOM   1508 C CA  . ALA   A 1 208 ? -1.609  -7.735  6.955   1.00 69.70  ? 745  ALA   A CA  1 
ATOM   1509 C C   . ALA   A 1 208 ? -1.497  -6.209  6.923   1.00 69.09  ? 745  ALA   A C   1 
ATOM   1510 O O   . ALA   A 1 208 ? -2.492  -5.499  6.768   1.00 69.02  ? 745  ALA   A O   1 
ATOM   1511 C CB  . ALA   A 1 208 ? -1.195  -8.320  5.611   1.00 68.53  ? 745  ALA   A CB  1 
ATOM   1512 N N   . ILE   A 1 217 ? 13.251  -9.735  10.214  1.00 57.69  ? 754  ILE   A N   1 
ATOM   1513 C CA  . ILE   A 1 217 ? 13.966  -10.224 9.041   1.00 56.56  ? 754  ILE   A CA  1 
ATOM   1514 C C   . ILE   A 1 217 ? 14.916  -11.350 9.441   1.00 56.44  ? 754  ILE   A C   1 
ATOM   1515 O O   . ILE   A 1 217 ? 15.713  -11.200 10.367  1.00 56.37  ? 754  ILE   A O   1 
ATOM   1516 C CB  . ILE   A 1 217 ? 14.731  -9.087  8.337   1.00 55.90  ? 754  ILE   A CB  1 
ATOM   1517 C CG1 . ILE   A 1 217 ? 13.800  -7.903  8.068   1.00 55.82  ? 754  ILE   A CG1 1 
ATOM   1518 C CG2 . ILE   A 1 217 ? 15.358  -9.584  7.039   1.00 54.68  ? 754  ILE   A CG2 1 
ATOM   1519 C CD1 . ILE   A 1 217 ? 14.474  -6.739  7.362   1.00 54.86  ? 754  ILE   A CD1 1 
ATOM   1520 N N   . THR   A 1 218 ? 14.823  -12.476 8.736   1.00 56.38  ? 755  THR   A N   1 
ATOM   1521 C CA  . THR   A 1 218 ? 15.660  -13.639 8.989   1.00 57.22  ? 755  THR   A CA  1 
ATOM   1522 C C   . THR   A 1 218 ? 16.853  -13.647 8.044   1.00 53.49  ? 755  THR   A C   1 
ATOM   1523 O O   . THR   A 1 218 ? 16.766  -13.206 6.895   1.00 51.94  ? 755  THR   A O   1 
ATOM   1524 C CB  . THR   A 1 218 ? 14.875  -14.946 8.821   1.00 59.83  ? 755  THR   A CB  1 
ATOM   1525 O OG1 . THR   A 1 218 ? 14.388  -15.045 7.475   1.00 59.65  ? 755  THR   A OG1 1 
ATOM   1526 C CG2 . THR   A 1 218 ? 13.702  -15.008 9.789   1.00 61.55  ? 755  THR   A CG2 1 
ATOM   1527 N N   . PHE   A 1 219 ? 17.968  -14.178 8.537   1.00 52.06  ? 756  PHE   A N   1 
ATOM   1528 C CA  . PHE   A 1 219 ? 19.205  -14.252 7.773   1.00 48.35  ? 756  PHE   A CA  1 
ATOM   1529 C C   . PHE   A 1 219 ? 19.689  -15.693 7.740   1.00 47.33  ? 756  PHE   A C   1 
ATOM   1530 O O   . PHE   A 1 219 ? 19.925  -16.299 8.791   1.00 47.46  ? 756  PHE   A O   1 
ATOM   1531 C CB  . PHE   A 1 219 ? 20.263  -13.324 8.367   1.00 46.55  ? 756  PHE   A CB  1 
ATOM   1532 C CG  . PHE   A 1 219 ? 19.966  -11.872 8.145   1.00 45.05  ? 756  PHE   A CG  1 
ATOM   1533 C CD1 . PHE   A 1 219 ? 20.245  -11.277 6.923   1.00 43.37  ? 756  PHE   A CD1 1 
ATOM   1534 C CD2 . PHE   A 1 219 ? 19.392  -11.105 9.143   1.00 45.43  ? 756  PHE   A CD2 1 
ATOM   1535 C CE1 . PHE   A 1 219 ? 19.967  -9.936  6.701   1.00 42.34  ? 756  PHE   A CE1 1 
ATOM   1536 C CE2 . PHE   A 1 219 ? 19.111  -9.763  8.928   1.00 44.67  ? 756  PHE   A CE2 1 
ATOM   1537 C CZ  . PHE   A 1 219 ? 19.400  -9.178  7.703   1.00 42.97  ? 756  PHE   A CZ  1 
ATOM   1538 N N   . GLU   A 1 220 ? 19.825  -16.238 6.527   1.00 46.19  ? 757  GLU   A N   1 
ATOM   1539 C CA  . GLU   A 1 220 ? 20.280  -17.615 6.362   1.00 46.95  ? 757  GLU   A CA  1 
ATOM   1540 C C   . GLU   A 1 220 ? 21.759  -17.751 6.707   1.00 45.77  ? 757  GLU   A C   1 
ATOM   1541 O O   . GLU   A 1 220 ? 22.177  -18.758 7.293   1.00 46.40  ? 757  GLU   A O   1 
ATOM   1542 C CB  . GLU   A 1 220 ? 19.995  -18.074 4.929   1.00 48.11  ? 757  GLU   A CB  1 
ATOM   1543 C CG  . GLU   A 1 220 ? 20.470  -19.476 4.585   1.00 50.85  ? 757  GLU   A CG  1 
ATOM   1544 C CD  . GLU   A 1 220 ? 21.862  -19.492 3.978   1.00 51.97  ? 757  GLU   A CD  1 
ATOM   1545 O OE1 . GLU   A 1 220 ? 22.464  -20.587 3.896   1.00 53.03  ? 757  GLU   A OE1 1 
ATOM   1546 O OE2 . GLU   A 1 220 ? 22.351  -18.409 3.583   1.00 51.27  ? 757  GLU   A OE2 1 
ATOM   1547 N N   . SER   A 1 221 ? 22.563  -16.756 6.350   1.00 43.86  ? 758  SER   A N   1 
ATOM   1548 C CA  . SER   A 1 221 ? 23.942  -16.631 6.793   1.00 43.09  ? 758  SER   A CA  1 
ATOM   1549 C C   . SER   A 1 221 ? 24.151  -15.239 7.374   1.00 41.01  ? 758  SER   A C   1 
ATOM   1550 O O   . SER   A 1 221 ? 23.511  -14.277 6.936   1.00 39.11  ? 758  SER   A O   1 
ATOM   1551 C CB  . SER   A 1 221 ? 24.930  -16.881 5.643   1.00 43.17  ? 758  SER   A CB  1 
ATOM   1552 O OG  . SER   A 1 221 ? 24.980  -15.777 4.758   1.00 43.22  ? 758  SER   A OG  1 
ATOM   1553 N N   . PRO   A 1 222 ? 25.020  -15.107 8.373   1.00 41.42  ? 759  PRO   A N   1 
ATOM   1554 C CA  . PRO   A 1 222 ? 25.123  -13.841 9.125   1.00 41.33  ? 759  PRO   A CA  1 
ATOM   1555 C C   . PRO   A 1 222 ? 25.539  -12.679 8.239   1.00 39.94  ? 759  PRO   A C   1 
ATOM   1556 O O   . PRO   A 1 222 ? 26.542  -12.759 7.512   1.00 38.46  ? 759  PRO   A O   1 
ATOM   1557 C CB  . PRO   A 1 222 ? 26.196  -14.148 10.180  1.00 42.38  ? 759  PRO   A CB  1 
ATOM   1558 C CG  . PRO   A 1 222 ? 26.099  -15.627 10.373  1.00 43.24  ? 759  PRO   A CG  1 
ATOM   1559 C CD  . PRO   A 1 222 ? 25.780  -16.193 9.015   1.00 42.01  ? 759  PRO   A CD  1 
ATOM   1560 N N   . PRO   A 1 223 ? 24.794  -11.569 8.284   1.00 38.79  ? 760  PRO   A N   1 
ATOM   1561 C CA  . PRO   A 1 223 ? 25.179  -10.405 7.490   1.00 36.23  ? 760  PRO   A CA  1 
ATOM   1562 C C   . PRO   A 1 223 ? 26.413  -9.744  8.069   1.00 33.91  ? 760  PRO   A C   1 
ATOM   1563 O O   . PRO   A 1 223 ? 26.651  -9.794  9.288   1.00 33.55  ? 760  PRO   A O   1 
ATOM   1564 C CB  . PRO   A 1 223 ? 23.946  -9.487  7.593   1.00 37.06  ? 760  PRO   A CB  1 
ATOM   1565 C CG  . PRO   A 1 223 ? 23.328  -9.854  8.899   1.00 39.15  ? 760  PRO   A CG  1 
ATOM   1566 C CD  . PRO   A 1 223 ? 23.554  -11.339 9.049   1.00 39.17  ? 760  PRO   A CD  1 
ATOM   1567 N N   . PRO   A 1 224 ? 27.227  -9.098  7.237   1.00 33.08  ? 761  PRO   A N   1 
ATOM   1568 C CA  . PRO   A 1 224 ? 28.484  -8.501  7.721   1.00 33.06  ? 761  PRO   A CA  1 
ATOM   1569 C C   . PRO   A 1 224 ? 28.220  -7.377  8.709   1.00 36.20  ? 761  PRO   A C   1 
ATOM   1570 O O   . PRO   A 1 224 ? 27.122  -6.799  8.735   1.00 36.37  ? 761  PRO   A O   1 
ATOM   1571 C CB  . PRO   A 1 224 ? 29.143  -7.981  6.433   1.00 30.88  ? 761  PRO   A CB  1 
ATOM   1572 C CG  . PRO   A 1 224 ? 28.006  -7.788  5.470   1.00 30.56  ? 761  PRO   A CG  1 
ATOM   1573 C CD  . PRO   A 1 224 ? 27.015  -8.869  5.794   1.00 31.39  ? 761  PRO   A CD  1 
ATOM   1574 N N   . PRO   A 1 225 ? 29.193  -7.041  9.554   1.00 37.37  ? 762  PRO   A N   1 
ATOM   1575 C CA  . PRO   A 1 225 ? 28.967  -5.985  10.548  1.00 36.53  ? 762  PRO   A CA  1 
ATOM   1576 C C   . PRO   A 1 225 ? 28.852  -4.612  9.906   1.00 33.06  ? 762  PRO   A C   1 
ATOM   1577 O O   . PRO   A 1 225 ? 29.446  -4.337  8.862   1.00 31.78  ? 762  PRO   A O   1 
ATOM   1578 C CB  . PRO   A 1 225 ? 30.204  -6.073  11.451  1.00 33.81  ? 762  PRO   A CB  1 
ATOM   1579 C CG  . PRO   A 1 225 ? 31.256  -6.676  10.581  1.00 41.79  ? 762  PRO   A CG  1 
ATOM   1580 C CD  . PRO   A 1 225 ? 30.535  -7.637  9.671   1.00 32.89  ? 762  PRO   A CD  1 
ATOM   1581 N N   . ILE   A 1 226 ? 28.068  -3.744  10.557  1.00 32.89  ? 763  ILE   A N   1 
ATOM   1582 C CA  . ILE   A 1 226 ? 27.883  -2.385  10.062  1.00 30.72  ? 763  ILE   A CA  1 
ATOM   1583 C C   . ILE   A 1 226 ? 29.219  -1.659  10.079  1.00 32.12  ? 763  ILE   A C   1 
ATOM   1584 O O   . ILE   A 1 226 ? 30.015  -1.793  11.019  1.00 34.98  ? 763  ILE   A O   1 
ATOM   1585 C CB  . ILE   A 1 226 ? 26.837  -1.622  10.895  1.00 31.40  ? 763  ILE   A CB  1 
ATOM   1586 C CG1 . ILE   A 1 226 ? 25.560  -2.447  11.081  1.00 33.32  ? 763  ILE   A CG1 1 
ATOM   1587 C CG2 . ILE   A 1 226 ? 26.486  -0.294  10.226  1.00 29.38  ? 763  ILE   A CG2 1 
ATOM   1588 C CD1 . ILE   A 1 226 ? 24.756  -2.629  9.826   1.00 29.32  ? 763  ILE   A CD1 1 
ATOM   1589 N N   . GLU   A 1 227 ? 29.472  -0.890  9.029   1.00 30.80  ? 764  GLU   A N   1 
ATOM   1590 C CA  . GLU   A 1 227 ? 30.692  -0.113  8.904   1.00 31.38  ? 764  GLU   A CA  1 
ATOM   1591 C C   . GLU   A 1 227 ? 30.425  1.333   9.300   1.00 31.97  ? 764  GLU   A C   1 
ATOM   1592 O O   . GLU   A 1 227 ? 29.423  1.930   8.891   1.00 31.06  ? 764  GLU   A O   1 
ATOM   1593 C CB  . GLU   A 1 227 ? 31.231  -0.182  7.473   1.00 29.40  ? 764  GLU   A CB  1 
ATOM   1594 C CG  . GLU   A 1 227 ? 31.670  -1.575  7.037   1.00 30.28  ? 764  GLU   A CG  1 
ATOM   1595 C CD  . GLU   A 1 227 ? 32.976  -2.005  7.685   1.00 32.47  ? 764  GLU   A CD  1 
ATOM   1596 O OE1 . GLU   A 1 227 ? 33.692  -1.134  8.216   1.00 33.33  ? 764  GLU   A OE1 1 
ATOM   1597 O OE2 . GLU   A 1 227 ? 33.290  -3.213  7.665   1.00 33.89  ? 764  GLU   A OE2 1 
ATOM   1598 N N   . TRP   A 1 228 ? 31.322  1.888   10.108  1.00 33.42  ? 765  TRP   A N   1 
ATOM   1599 C CA  . TRP   A 1 228 ? 31.247  3.282   10.514  1.00 32.99  ? 765  TRP   A CA  1 
ATOM   1600 C C   . TRP   A 1 228 ? 32.582  3.949   10.242  1.00 32.24  ? 765  TRP   A C   1 
ATOM   1601 O O   . TRP   A 1 228 ? 33.636  3.321   10.353  1.00 32.42  ? 765  TRP   A O   1 
ATOM   1602 C CB  . TRP   A 1 228 ? 30.880  3.430   11.993  1.00 35.20  ? 765  TRP   A CB  1 
ATOM   1603 C CG  . TRP   A 1 228 ? 29.553  2.846   12.327  1.00 36.08  ? 765  TRP   A CG  1 
ATOM   1604 C CD1 . TRP   A 1 228 ? 29.305  1.590   12.809  1.00 36.85  ? 765  TRP   A CD1 1 
ATOM   1605 C CD2 . TRP   A 1 228 ? 28.281  3.488   12.201  1.00 35.51  ? 765  TRP   A CD2 1 
ATOM   1606 N NE1 . TRP   A 1 228 ? 27.954  1.414   12.995  1.00 37.42  ? 765  TRP   A NE1 1 
ATOM   1607 C CE2 . TRP   A 1 228 ? 27.303  2.564   12.628  1.00 36.92  ? 765  TRP   A CE2 1 
ATOM   1608 C CE3 . TRP   A 1 228 ? 27.873  4.756   11.772  1.00 33.42  ? 765  TRP   A CE3 1 
ATOM   1609 C CZ2 . TRP   A 1 228 ? 25.940  2.871   12.636  1.00 36.48  ? 765  TRP   A CZ2 1 
ATOM   1610 C CZ3 . TRP   A 1 228 ? 26.522  5.059   11.783  1.00 33.22  ? 765  TRP   A CZ3 1 
ATOM   1611 C CH2 . TRP   A 1 228 ? 25.572  4.121   12.210  1.00 34.94  ? 765  TRP   A CH2 1 
ATOM   1612 N N   . HIS   A 1 229 ? 32.517  5.227   9.866   1.00 33.38  ? 766  HIS   A N   1 
ATOM   1613 C CA  . HIS   A 1 229 ? 33.703  6.015   9.557   1.00 35.05  ? 766  HIS   A CA  1 
ATOM   1614 C C   . HIS   A 1 229 ? 33.924  7.055   10.652  1.00 36.76  ? 766  HIS   A C   1 
ATOM   1615 O O   . HIS   A 1 229 ? 34.326  6.723   11.774  1.00 38.66  ? 766  HIS   A O   1 
ATOM   1616 C CB  . HIS   A 1 229 ? 33.560  6.691   8.187   1.00 34.59  ? 766  HIS   A CB  1 
ATOM   1617 C CG  . HIS   A 1 229 ? 34.745  7.521   7.783   1.00 35.34  ? 766  HIS   A CG  1 
ATOM   1618 N ND1 . HIS   A 1 229 ? 36.028  7.273   8.227   1.00 36.64  ? 766  HIS   A ND1 1 
ATOM   1619 C CD2 . HIS   A 1 229 ? 34.829  8.614   6.990   1.00 33.96  ? 766  HIS   A CD2 1 
ATOM   1620 C CE1 . HIS   A 1 229 ? 36.852  8.172   7.718   1.00 35.97  ? 766  HIS   A CE1 1 
ATOM   1621 N NE2 . HIS   A 1 229 ? 36.149  8.999   6.966   1.00 35.06  ? 766  HIS   A NE2 1 
ATOM   1622 N N   . ILE   A 1 230 ? 33.636  8.315   10.348  1.00 37.40  ? 767  ILE   A N   1 
ATOM   1623 C CA  . ILE   A 1 230 ? 33.786  9.392   11.320  1.00 40.24  ? 767  ILE   A CA  1 
ATOM   1624 C C   . ILE   A 1 230 ? 32.549  9.516   12.196  1.00 41.71  ? 767  ILE   A C   1 
ATOM   1625 O O   . ILE   A 1 230 ? 32.652  9.554   13.425  1.00 43.72  ? 767  ILE   A O   1 
ATOM   1626 C CB  . ILE   A 1 230 ? 34.101  10.718  10.602  1.00 38.92  ? 767  ILE   A CB  1 
ATOM   1627 C CG1 . ILE   A 1 230 ? 35.370  10.586  9.761   1.00 38.26  ? 767  ILE   A CG1 1 
ATOM   1628 C CG2 . ILE   A 1 230 ? 34.274  11.821  11.618  1.00 39.95  ? 767  ILE   A CG2 1 
ATOM   1629 C CD1 . ILE   A 1 230 ? 35.636  11.788  8.889   1.00 37.59  ? 767  ILE   A CD1 1 
ATOM   1630 N N   . SER   A 1 231 ? 31.364  9.566   11.585  1.00 40.48  ? 768  SER   A N   1 
ATOM   1631 C CA  . SER   A 1 231 ? 30.137  9.538   12.367  1.00 42.44  ? 768  SER   A CA  1 
ATOM   1632 C C   . SER   A 1 231 ? 30.026  8.206   13.094  1.00 45.11  ? 768  SER   A C   1 
ATOM   1633 O O   . SER   A 1 231 ? 30.482  7.165   12.610  1.00 44.10  ? 768  SER   A O   1 
ATOM   1634 C CB  . SER   A 1 231 ? 28.909  9.757   11.479  1.00 41.43  ? 768  SER   A CB  1 
ATOM   1635 O OG  . SER   A 1 231 ? 28.781  11.111  11.081  1.00 40.93  ? 768  SER   A OG  1 
ATOM   1636 N N   . LYS   A 1 232 ? 29.424  8.249   14.273  1.00 48.92  ? 769  LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 232 ? 29.296  7.094   15.143  1.00 51.73  ? 769  LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 232 ? 27.825  6.749   15.340  1.00 51.20  ? 769  LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 232 ? 26.947  7.585   15.094  1.00 50.75  ? 769  LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 232 ? 29.974  7.364   16.495  1.00 55.51  ? 769  LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 232 ? 31.490  7.498   16.388  1.00 57.51  ? 769  LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 232 ? 32.086  6.374   15.538  1.00 58.40  ? 769  LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 232 ? 33.592  6.532   15.355  1.00 59.91  ? 769  LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 232 ? 34.163  5.428   14.528  1.00 60.00  ? 769  LYS   A NZ  1 
ATOM   1645 N N   . PRO   A 1 233 ? 27.517  5.517   15.750  1.00 51.48  ? 770  PRO   A N   1 
ATOM   1646 C CA  . PRO   A 1 233 ? 26.108  5.129   15.902  1.00 50.95  ? 770  PRO   A CA  1 
ATOM   1647 C C   . PRO   A 1 233 ? 25.375  6.057   16.858  1.00 52.53  ? 770  PRO   A C   1 
ATOM   1648 O O   . PRO   A 1 233 ? 25.840  6.325   17.967  1.00 54.81  ? 770  PRO   A O   1 
ATOM   1649 C CB  . PRO   A 1 233 ? 26.194  3.701   16.454  1.00 52.10  ? 770  PRO   A CB  1 
ATOM   1650 C CG  . PRO   A 1 233 ? 27.510  3.197   15.978  1.00 51.97  ? 770  PRO   A CG  1 
ATOM   1651 C CD  . PRO   A 1 233 ? 28.428  4.381   15.986  1.00 52.15  ? 770  PRO   A CD  1 
ATOM   1652 N N   . GLY   A 1 234 ? 24.225  6.560   16.410  1.00 52.01  ? 771  GLY   A N   1 
ATOM   1653 C CA  . GLY   A 1 234 ? 23.386  7.424   17.208  1.00 54.20  ? 771  GLY   A CA  1 
ATOM   1654 C C   . GLY   A 1 234 ? 23.528  8.902   16.907  1.00 54.60  ? 771  GLY   A C   1 
ATOM   1655 O O   . GLY   A 1 234 ? 22.583  9.663   17.149  1.00 55.77  ? 771  GLY   A O   1 
ATOM   1656 N N   . GLN   A 1 235 ? 24.675  9.327   16.386  1.00 54.23  ? 772  GLN   A N   1 
ATOM   1657 C CA  . GLN   A 1 235 ? 24.891  10.727  16.025  1.00 55.17  ? 772  GLN   A CA  1 
ATOM   1658 C C   . GLN   A 1 235 ? 24.343  11.024  14.629  1.00 51.33  ? 772  GLN   A C   1 
ATOM   1659 O O   . GLN   A 1 235 ? 25.072  11.447  13.734  1.00 49.24  ? 772  GLN   A O   1 
ATOM   1660 C CB  . GLN   A 1 235 ? 26.374  11.066  16.089  1.00 57.87  ? 772  GLN   A CB  1 
ATOM   1661 C CG  . GLN   A 1 235 ? 26.983  11.081  17.468  1.00 62.94  ? 772  GLN   A CG  1 
ATOM   1662 C CD  . GLN   A 1 235 ? 28.464  11.382  17.404  1.00 64.30  ? 772  GLN   A CD  1 
ATOM   1663 O OE1 . GLN   A 1 235 ? 29.106  11.154  16.379  1.00 62.36  ? 772  GLN   A OE1 1 
ATOM   1664 N NE2 . GLN   A 1 235 ? 29.013  11.909  18.492  1.00 67.24  ? 772  GLN   A NE2 1 
ATOM   1665 N N   . PHE   A 1 236 ? 23.035  10.811  14.449  1.00 50.99  ? 773  PHE   A N   1 
ATOM   1666 C CA  . PHE   A 1 236 ? 22.462  11.002  13.121  1.00 49.35  ? 773  PHE   A CA  1 
ATOM   1667 C C   . PHE   A 1 236 ? 22.471  12.463  12.688  1.00 49.75  ? 773  PHE   A C   1 
ATOM   1668 O O   . PHE   A 1 236 ? 22.354  12.738  11.488  1.00 47.42  ? 773  PHE   A O   1 
ATOM   1669 C CB  . PHE   A 1 236 ? 21.038  10.428  13.040  1.00 49.85  ? 773  PHE   A CB  1 
ATOM   1670 C CG  . PHE   A 1 236 ? 20.062  11.019  14.026  1.00 52.75  ? 773  PHE   A CG  1 
ATOM   1671 C CD1 . PHE   A 1 236 ? 19.435  12.233  13.772  1.00 53.00  ? 773  PHE   A CD1 1 
ATOM   1672 C CD2 . PHE   A 1 236 ? 19.735  10.332  15.190  1.00 54.88  ? 773  PHE   A CD2 1 
ATOM   1673 C CE1 . PHE   A 1 236 ? 18.527  12.765  14.678  1.00 55.40  ? 773  PHE   A CE1 1 
ATOM   1674 C CE2 . PHE   A 1 236 ? 18.827  10.858  16.098  1.00 56.87  ? 773  PHE   A CE2 1 
ATOM   1675 C CZ  . PHE   A 1 236 ? 18.223  12.074  15.842  1.00 57.13  ? 773  PHE   A CZ  1 
ATOM   1676 N N   . GLU   A 1 237 ? 22.633  13.401  13.627  1.00 52.50  ? 774  GLU   A N   1 
ATOM   1677 C CA  . GLU   A 1 237 ? 22.691  14.815  13.274  1.00 53.86  ? 774  GLU   A CA  1 
ATOM   1678 C C   . GLU   A 1 237 ? 23.952  15.171  12.498  1.00 49.78  ? 774  GLU   A C   1 
ATOM   1679 O O   . GLU   A 1 237 ? 23.979  16.209  11.830  1.00 49.08  ? 774  GLU   A O   1 
ATOM   1680 C CB  . GLU   A 1 237 ? 22.605  15.688  14.530  1.00 59.72  ? 774  GLU   A CB  1 
ATOM   1681 C CG  . GLU   A 1 237 ? 21.353  15.480  15.368  1.00 64.34  ? 774  GLU   A CG  1 
ATOM   1682 C CD  . GLU   A 1 237 ? 21.524  14.398  16.421  1.00 68.43  ? 774  GLU   A CD  1 
ATOM   1683 O OE1 . GLU   A 1 237 ? 20.725  14.368  17.381  1.00 71.57  ? 774  GLU   A OE1 1 
ATOM   1684 O OE2 . GLU   A 1 237 ? 22.461  13.580  16.296  1.00 68.55  ? 774  GLU   A OE2 1 
ATOM   1685 N N   . THR   A 1 238 ? 24.992  14.342  12.568  1.00 47.45  ? 775  THR   A N   1 
ATOM   1686 C CA  . THR   A 1 238 ? 26.249  14.604  11.882  1.00 45.83  ? 775  THR   A CA  1 
ATOM   1687 C C   . THR   A 1 238 ? 26.430  13.762  10.623  1.00 41.71  ? 775  THR   A C   1 
ATOM   1688 O O   . THR   A 1 238 ? 27.507  13.798  10.020  1.00 40.99  ? 775  THR   A O   1 
ATOM   1689 C CB  . THR   A 1 238 ? 27.431  14.367  12.825  1.00 48.29  ? 775  THR   A CB  1 
ATOM   1690 O OG1 . THR   A 1 238 ? 27.667  12.959  12.948  1.00 48.51  ? 775  THR   A OG1 1 
ATOM   1691 C CG2 . THR   A 1 238 ? 27.134  14.949  14.200  1.00 51.25  ? 775  THR   A CG2 1 
ATOM   1692 N N   . PHE   A 1 239 ? 25.413  13.008  10.213  1.00 38.32  ? 776  PHE   A N   1 
ATOM   1693 C CA  . PHE   A 1 239 ? 25.541  12.202  9.008   1.00 33.80  ? 776  PHE   A CA  1 
ATOM   1694 C C   . PHE   A 1 239 ? 25.728  13.099  7.790   1.00 31.79  ? 776  PHE   A C   1 
ATOM   1695 O O   . PHE   A 1 239 ? 25.116  14.164  7.677   1.00 31.60  ? 776  PHE   A O   1 
ATOM   1696 C CB  . PHE   A 1 239 ? 24.316  11.304  8.815   1.00 32.16  ? 776  PHE   A CB  1 
ATOM   1697 C CG  . PHE   A 1 239 ? 24.213  10.177  9.814   1.00 31.43  ? 776  PHE   A CG  1 
ATOM   1698 C CD1 . PHE   A 1 239 ? 25.190  9.981   10.772  1.00 31.83  ? 776  PHE   A CD1 1 
ATOM   1699 C CD2 . PHE   A 1 239 ? 23.133  9.310   9.784   1.00 29.65  ? 776  PHE   A CD2 1 
ATOM   1700 C CE1 . PHE   A 1 239 ? 25.086  8.951   11.686  1.00 32.51  ? 776  PHE   A CE1 1 
ATOM   1701 C CE2 . PHE   A 1 239 ? 23.027  8.277   10.694  1.00 30.84  ? 776  PHE   A CE2 1 
ATOM   1702 C CZ  . PHE   A 1 239 ? 24.004  8.097   11.646  1.00 32.04  ? 776  PHE   A CZ  1 
ATOM   1703 N N   . ASP   A 1 240 ? 26.599  12.665  6.886   1.00 30.30  ? 777  ASP   A N   1 
ATOM   1704 C CA  . ASP   A 1 240 ? 26.877  13.374  5.645   1.00 29.79  ? 777  ASP   A CA  1 
ATOM   1705 C C   . ASP   A 1 240 ? 27.679  12.430  4.762   1.00 28.02  ? 777  ASP   A C   1 
ATOM   1706 O O   . ASP   A 1 240 ? 28.126  11.367  5.205   1.00 28.25  ? 777  ASP   A O   1 
ATOM   1707 C CB  . ASP   A 1 240 ? 27.636  14.683  5.890   1.00 32.25  ? 777  ASP   A CB  1 
ATOM   1708 C CG  . ASP   A 1 240 ? 27.354  15.727  4.825   1.00 33.82  ? 777  ASP   A CG  1 
ATOM   1709 O OD1 . ASP   A 1 240 ? 26.973  15.341  3.697   1.00 33.06  ? 777  ASP   A OD1 1 
ATOM   1710 O OD2 . ASP   A 1 240 ? 27.510  16.934  5.118   1.00 34.64  ? 777  ASP   A OD2 1 
ATOM   1711 N N   . LEU   A 1 241 ? 27.858  12.835  3.503   1.00 25.82  ? 778  LEU   A N   1 
ATOM   1712 C CA  . LEU   A 1 241 ? 28.536  11.981  2.533   1.00 23.10  ? 778  LEU   A CA  1 
ATOM   1713 C C   . LEU   A 1 241 ? 29.911  11.546  3.035   1.00 23.23  ? 778  LEU   A C   1 
ATOM   1714 O O   . LEU   A 1 241 ? 30.248  10.358  3.005   1.00 22.77  ? 778  LEU   A O   1 
ATOM   1715 C CB  . LEU   A 1 241 ? 28.660  12.710  1.196   1.00 21.25  ? 778  LEU   A CB  1 
ATOM   1716 C CG  . LEU   A 1 241 ? 29.360  11.928  0.083   1.00 21.48  ? 778  LEU   A CG  1 
ATOM   1717 C CD1 . LEU   A 1 241 ? 28.414  10.924  -0.550  1.00 21.05  ? 778  LEU   A CD1 1 
ATOM   1718 C CD2 . LEU   A 1 241 ? 29.935  12.864  -0.966  1.00 21.30  ? 778  LEU   A CD2 1 
ATOM   1719 N N   . MET   A 1 242 ? 30.716  12.493  3.513   1.00 23.56  ? 779  MET   A N   1 
ATOM   1720 C CA  . MET   A 1 242 ? 32.093  12.200  3.889   1.00 24.85  ? 779  MET   A CA  1 
ATOM   1721 C C   . MET   A 1 242 ? 32.253  11.697  5.323   1.00 27.63  ? 779  MET   A C   1 
ATOM   1722 O O   . MET   A 1 242 ? 33.348  11.245  5.675   1.00 28.11  ? 779  MET   A O   1 
ATOM   1723 C CB  . MET   A 1 242 ? 32.968  13.444  3.694   1.00 24.20  ? 779  MET   A CB  1 
ATOM   1724 C CG  . MET   A 1 242 ? 32.957  13.997  2.278   1.00 23.53  ? 779  MET   A CG  1 
ATOM   1725 S SD  . MET   A 1 242 ? 33.723  12.908  1.056   1.00 23.85  ? 779  MET   A SD  1 
ATOM   1726 C CE  . MET   A 1 242 ? 35.457  13.127  1.444   1.00 22.69  ? 779  MET   A CE  1 
ATOM   1727 N N   . THR   A 1 243 ? 31.215  11.769  6.163   1.00 28.79  ? 780  THR   A N   1 
ATOM   1728 C CA  . THR   A 1 243 ? 31.313  11.286  7.541   1.00 30.44  ? 780  THR   A CA  1 
ATOM   1729 C C   . THR   A 1 243 ? 30.765  9.875   7.735   1.00 30.30  ? 780  THR   A C   1 
ATOM   1730 O O   . THR   A 1 243 ? 31.231  9.160   8.629   1.00 32.10  ? 780  THR   A O   1 
ATOM   1731 C CB  . THR   A 1 243 ? 30.594  12.240  8.503   1.00 32.41  ? 780  THR   A CB  1 
ATOM   1732 O OG1 . THR   A 1 243 ? 29.248  12.446  8.064   1.00 33.00  ? 780  THR   A OG1 1 
ATOM   1733 C CG2 . THR   A 1 243 ? 31.315  13.579  8.568   1.00 33.60  ? 780  THR   A CG2 1 
ATOM   1734 N N   . LEU   A 1 244 ? 29.792  9.456   6.936   1.00 26.67  ? 781  LEU   A N   1 
ATOM   1735 C CA  . LEU   A 1 244 ? 29.416  8.054   6.926   1.00 25.73  ? 781  LEU   A CA  1 
ATOM   1736 C C   . LEU   A 1 244 ? 30.481  7.235   6.195   1.00 24.75  ? 781  LEU   A C   1 
ATOM   1737 O O   . LEU   A 1 244 ? 31.332  7.771   5.481   1.00 23.89  ? 781  LEU   A O   1 
ATOM   1738 C CB  . LEU   A 1 244 ? 28.040  7.874   6.275   1.00 24.84  ? 781  LEU   A CB  1 
ATOM   1739 C CG  . LEU   A 1 244 ? 26.859  8.476   7.044   1.00 25.58  ? 781  LEU   A CG  1 
ATOM   1740 C CD1 . LEU   A 1 244 ? 25.648  8.658   6.151   1.00 24.12  ? 781  LEU   A CD1 1 
ATOM   1741 C CD2 . LEU   A 1 244 ? 26.504  7.609   8.248   1.00 27.43  ? 781  LEU   A CD2 1 
ATOM   1742 N N   . HIS   A 1 245 ? 30.436  5.911   6.397   1.00 24.87  ? 782  HIS   A N   1 
ATOM   1743 C CA  . HIS   A 1 245 ? 31.386  5.017   5.744   1.00 24.45  ? 782  HIS   A CA  1 
ATOM   1744 C C   . HIS   A 1 245 ? 30.913  4.708   4.325   1.00 22.98  ? 782  HIS   A C   1 
ATOM   1745 O O   . HIS   A 1 245 ? 29.724  4.463   4.109   1.00 23.26  ? 782  HIS   A O   1 
ATOM   1746 C CB  . HIS   A 1 245 ? 31.532  3.718   6.538   1.00 27.01  ? 782  HIS   A CB  1 
ATOM   1747 C CG  . HIS   A 1 245 ? 32.764  2.931   6.205   1.00 28.67  ? 782  HIS   A CG  1 
ATOM   1748 N ND1 . HIS   A 1 245 ? 32.921  2.259   5.012   1.00 27.51  ? 782  HIS   A ND1 1 
ATOM   1749 C CD2 . HIS   A 1 245 ? 33.888  2.692   6.923   1.00 29.79  ? 782  HIS   A CD2 1 
ATOM   1750 C CE1 . HIS   A 1 245 ? 34.093  1.650   5.004   1.00 28.35  ? 782  HIS   A CE1 1 
ATOM   1751 N NE2 . HIS   A 1 245 ? 34.700  1.896   6.152   1.00 29.81  ? 782  HIS   A NE2 1 
ATOM   1752 N N   . PRO   A 1 246 ? 31.816  4.718   3.340   1.00 20.43  ? 783  PRO   A N   1 
ATOM   1753 C CA  . PRO   A 1 246 ? 31.363  4.529   1.950   1.00 19.33  ? 783  PRO   A CA  1 
ATOM   1754 C C   . PRO   A 1 246 ? 30.748  3.167   1.694   1.00 19.52  ? 783  PRO   A C   1 
ATOM   1755 O O   . PRO   A 1 246 ? 29.812  3.064   0.897   1.00 20.57  ? 783  PRO   A O   1 
ATOM   1756 C CB  . PRO   A 1 246 ? 32.641  4.746   1.127   1.00 19.24  ? 783  PRO   A CB  1 
ATOM   1757 C CG  . PRO   A 1 246 ? 33.769  4.538   2.096   1.00 22.88  ? 783  PRO   A CG  1 
ATOM   1758 C CD  . PRO   A 1 246 ? 33.254  5.018   3.421   1.00 23.22  ? 783  PRO   A CD  1 
ATOM   1759 N N   . ILE   A 1 247 ? 31.243  2.116   2.346   1.00 20.67  ? 784  ILE   A N   1 
ATOM   1760 C CA  . ILE   A 1 247 ? 30.632  0.795   2.205   1.00 34.43  ? 784  ILE   A CA  1 
ATOM   1761 C C   . ILE   A 1 247 ? 29.182  0.826   2.678   1.00 33.28  ? 784  ILE   A C   1 
ATOM   1762 O O   . ILE   A 1 247 ? 28.284  0.277   2.026   1.00 20.42  ? 784  ILE   A O   1 
ATOM   1763 C CB  . ILE   A 1 247 ? 31.442  -0.258  2.982   1.00 22.68  ? 784  ILE   A CB  1 
ATOM   1764 C CG1 . ILE   A 1 247 ? 32.864  -0.376  2.439   1.00 23.11  ? 784  ILE   A CG1 1 
ATOM   1765 C CG2 . ILE   A 1 247 ? 30.743  -1.611  2.937   1.00 23.30  ? 784  ILE   A CG2 1 
ATOM   1766 C CD1 . ILE   A 1 247 ? 33.716  -1.347  3.251   1.00 24.94  ? 784  ILE   A CD1 1 
ATOM   1767 N N   . GLU   A 1 248 ? 28.939  1.464   3.833   1.00 30.59  ? 785  GLU   A N   1 
ATOM   1768 C CA  . GLU   A 1 248 ? 27.611  1.448   4.441   1.00 27.05  ? 785  GLU   A CA  1 
ATOM   1769 C C   . GLU   A 1 248 ? 26.642  2.355   3.697   1.00 23.38  ? 785  GLU   A C   1 
ATOM   1770 O O   . GLU   A 1 248 ? 25.450  2.047   3.614   1.00 24.03  ? 785  GLU   A O   1 
ATOM   1771 C CB  . GLU   A 1 248 ? 27.698  1.859   5.912   1.00 26.18  ? 785  GLU   A CB  1 
ATOM   1772 C CG  . GLU   A 1 248 ? 26.670  1.182   6.807   1.00 28.18  ? 785  GLU   A CG  1 
ATOM   1773 C CD  . GLU   A 1 248 ? 26.722  -0.343  6.728   1.00 30.24  ? 785  GLU   A CD  1 
ATOM   1774 O OE1 . GLU   A 1 248 ? 25.696  -0.963  6.360   1.00 29.54  ? 785  GLU   A OE1 1 
ATOM   1775 O OE2 . GLU   A 1 248 ? 27.788  -0.920  7.025   1.00 25.44  ? 785  GLU   A OE2 1 
ATOM   1776 N N   . ILE   A 1 249 ? 27.129  3.468   3.148   1.00 21.26  ? 786  ILE   A N   1 
ATOM   1777 C CA  . ILE   A 1 249 ? 26.283  4.298   2.293   1.00 20.63  ? 786  ILE   A CA  1 
ATOM   1778 C C   . ILE   A 1 249 ? 25.749  3.472   1.134   1.00 18.89  ? 786  ILE   A C   1 
ATOM   1779 O O   . ILE   A 1 249 ? 24.549  3.485   0.834   1.00 19.13  ? 786  ILE   A O   1 
ATOM   1780 C CB  . ILE   A 1 249 ? 27.059  5.531   1.800   1.00 21.98  ? 786  ILE   A CB  1 
ATOM   1781 C CG1 . ILE   A 1 249 ? 27.252  6.524   2.947   1.00 18.50  ? 786  ILE   A CG1 1 
ATOM   1782 C CG2 . ILE   A 1 249 ? 26.353  6.194   0.627   1.00 16.90  ? 786  ILE   A CG2 1 
ATOM   1783 C CD1 . ILE   A 1 249 ? 28.135  7.665   2.582   1.00 18.18  ? 786  ILE   A CD1 1 
ATOM   1784 N N   . ALA   A 1 250 ? 26.630  2.707   0.491   1.00 18.56  ? 787  ALA   A N   1 
ATOM   1785 C CA  . ALA   A 1 250 ? 26.196  1.838   -0.594  1.00 18.92  ? 787  ALA   A CA  1 
ATOM   1786 C C   . ALA   A 1 250 ? 25.278  0.732   -0.084  1.00 18.72  ? 787  ALA   A C   1 
ATOM   1787 O O   . ALA   A 1 250 ? 24.256  0.430   -0.709  1.00 18.17  ? 787  ALA   A O   1 
ATOM   1788 C CB  . ALA   A 1 250 ? 27.409  1.250   -1.312  1.00 18.18  ? 787  ALA   A CB  1 
ATOM   1789 N N   . ARG   A 1 251 ? 25.612  0.130   1.060   1.00 19.23  ? 788  ARG   A N   1 
ATOM   1790 C CA  . ARG   A 1 251 ? 24.773  -0.938  1.600   1.00 22.71  ? 788  ARG   A CA  1 
ATOM   1791 C C   . ARG   A 1 251 ? 23.369  -0.433  1.900   1.00 20.85  ? 788  ARG   A C   1 
ATOM   1792 O O   . ARG   A 1 251 ? 22.375  -1.065  1.523   1.00 20.64  ? 788  ARG   A O   1 
ATOM   1793 C CB  . ARG   A 1 251 ? 25.397  -1.522  2.865   1.00 24.04  ? 788  ARG   A CB  1 
ATOM   1794 C CG  . ARG   A 1 251 ? 26.521  -2.503  2.637   1.00 23.70  ? 788  ARG   A CG  1 
ATOM   1795 C CD  . ARG   A 1 251 ? 27.117  -2.887  3.978   1.00 24.40  ? 788  ARG   A CD  1 
ATOM   1796 N NE  . ARG   A 1 251 ? 28.316  -3.709  3.856   1.00 25.25  ? 788  ARG   A NE  1 
ATOM   1797 C CZ  . ARG   A 1 251 ? 29.068  -4.072  4.891   1.00 27.43  ? 788  ARG   A CZ  1 
ATOM   1798 N NH1 . ARG   A 1 251 ? 28.737  -3.678  6.112   1.00 26.86  ? 788  ARG   A NH1 1 
ATOM   1799 N NH2 . ARG   A 1 251 ? 30.148  -4.819  4.708   1.00 27.20  ? 788  ARG   A NH2 1 
ATOM   1800 N N   . GLN   A 1 252 ? 23.273  0.714   2.574   1.00 20.01  ? 789  GLN   A N   1 
ATOM   1801 C CA  . GLN   A 1 252 ? 21.980  1.186   3.050   1.00 22.12  ? 789  GLN   A CA  1 
ATOM   1802 C C   . GLN   A 1 252 ? 21.122  1.718   1.906   1.00 22.34  ? 789  GLN   A C   1 
ATOM   1803 O O   . GLN   A 1 252 ? 19.900  1.529   1.905   1.00 19.02  ? 789  GLN   A O   1 
ATOM   1804 C CB  . GLN   A 1 252 ? 22.186  2.250   4.129   1.00 20.35  ? 789  GLN   A CB  1 
ATOM   1805 C CG  . GLN   A 1 252 ? 22.888  1.734   5.381   1.00 21.68  ? 789  GLN   A CG  1 
ATOM   1806 C CD  . GLN   A 1 252 ? 22.115  0.628   6.065   1.00 22.83  ? 789  GLN   A CD  1 
ATOM   1807 O OE1 . GLN   A 1 252 ? 20.889  0.691   6.179   1.00 22.99  ? 789  GLN   A OE1 1 
ATOM   1808 N NE2 . GLN   A 1 252 ? 22.826  -0.401  6.518   1.00 23.79  ? 789  GLN   A NE2 1 
ATOM   1809 N N   . LEU   A 1 253 ? 21.741  2.393   0.930   1.00 19.44  ? 790  LEU   A N   1 
ATOM   1810 C CA  . LEU   A 1 253 ? 21.000  2.820   -0.252  1.00 17.91  ? 790  LEU   A CA  1 
ATOM   1811 C C   . LEU   A 1 253 ? 20.526  1.620   -1.055  1.00 17.58  ? 790  LEU   A C   1 
ATOM   1812 O O   . LEU   A 1 253 ? 19.430  1.643   -1.624  1.00 17.12  ? 790  LEU   A O   1 
ATOM   1813 C CB  . LEU   A 1 253 ? 21.857  3.742   -1.122  1.00 16.48  ? 790  LEU   A CB  1 
ATOM   1814 C CG  . LEU   A 1 253 ? 22.015  5.188   -0.630  1.00 20.52  ? 790  LEU   A CG  1 
ATOM   1815 C CD1 . LEU   A 1 253 ? 23.004  5.979   -1.493  1.00 17.43  ? 790  LEU   A CD1 1 
ATOM   1816 C CD2 . LEU   A 1 253 ? 20.656  5.885   -0.562  1.00 16.57  ? 790  LEU   A CD2 1 
ATOM   1817 N N   . THR   A 1 254 ? 21.337  0.561   -1.109  1.00 17.64  ? 791  THR   A N   1 
ATOM   1818 C CA  . THR   A 1 254 ? 20.905  -0.650  -1.791  1.00 17.94  ? 791  THR   A CA  1 
ATOM   1819 C C   . THR   A 1 254 ? 19.711  -1.270  -1.086  1.00 18.93  ? 791  THR   A C   1 
ATOM   1820 O O   . THR   A 1 254 ? 18.742  -1.676  -1.736  1.00 19.33  ? 791  THR   A O   1 
ATOM   1821 C CB  . THR   A 1 254 ? 22.058  -1.645  -1.876  1.00 18.41  ? 791  THR   A CB  1 
ATOM   1822 O OG1 . THR   A 1 254 ? 23.099  -1.094  -2.694  1.00 17.92  ? 791  THR   A OG1 1 
ATOM   1823 C CG2 . THR   A 1 254 ? 21.581  -2.956  -2.493  1.00 19.01  ? 791  THR   A CG2 1 
ATOM   1824 N N   . LEU   A 1 255 ? 19.757  -1.353  0.245   1.00 19.21  ? 792  LEU   A N   1 
ATOM   1825 C CA  . LEU   A 1 255 ? 18.619  -1.895  0.981   1.00 20.02  ? 792  LEU   A CA  1 
ATOM   1826 C C   . LEU   A 1 255 ? 17.368  -1.053  0.750   1.00 23.19  ? 792  LEU   A C   1 
ATOM   1827 O O   . LEU   A 1 255 ? 16.282  -1.590  0.507   1.00 20.00  ? 792  LEU   A O   1 
ATOM   1828 C CB  . LEU   A 1 255 ? 18.948  -1.986  2.470   1.00 21.04  ? 792  LEU   A CB  1 
ATOM   1829 C CG  . LEU   A 1 255 ? 19.969  -3.049  2.874   1.00 21.92  ? 792  LEU   A CG  1 
ATOM   1830 C CD1 . LEU   A 1 255 ? 20.328  -2.884  4.334   1.00 22.99  ? 792  LEU   A CD1 1 
ATOM   1831 C CD2 . LEU   A 1 255 ? 19.441  -4.464  2.614   1.00 22.64  ? 792  LEU   A CD2 1 
ATOM   1832 N N   . LEU   A 1 256 ? 17.508  0.273   0.790   1.00 22.34  ? 793  LEU   A N   1 
ATOM   1833 C CA  . LEU   A 1 256 ? 16.358  1.141   0.561   1.00 22.08  ? 793  LEU   A CA  1 
ATOM   1834 C C   . LEU   A 1 256 ? 15.839  1.006   -0.869  1.00 20.98  ? 793  LEU   A C   1 
ATOM   1835 O O   . LEU   A 1 256 ? 14.637  0.823   -1.092  1.00 21.43  ? 793  LEU   A O   1 
ATOM   1836 C CB  . LEU   A 1 256 ? 16.735  2.586   0.870   1.00 23.06  ? 793  LEU   A CB  1 
ATOM   1837 C CG  . LEU   A 1 256 ? 15.874  3.697   0.274   1.00 24.15  ? 793  LEU   A CG  1 
ATOM   1838 C CD1 . LEU   A 1 256 ? 14.459  3.637   0.824   1.00 26.84  ? 793  LEU   A CD1 1 
ATOM   1839 C CD2 . LEU   A 1 256 ? 16.524  5.036   0.576   1.00 22.90  ? 793  LEU   A CD2 1 
ATOM   1840 N N   . GLU   A 1 257 ? 16.734  1.087   -1.853  1.00 20.78  ? 794  GLU   A N   1 
ATOM   1841 C CA  . GLU   A 1 257 ? 16.331  0.964   -3.248  1.00 17.44  ? 794  GLU   A CA  1 
ATOM   1842 C C   . GLU   A 1 257 ? 15.791  -0.423  -3.576  1.00 22.57  ? 794  GLU   A C   1 
ATOM   1843 O O   . GLU   A 1 257 ? 15.020  -0.560  -4.531  1.00 22.01  ? 794  GLU   A O   1 
ATOM   1844 C CB  . GLU   A 1 257 ? 17.512  1.305   -4.156  1.00 16.84  ? 794  GLU   A CB  1 
ATOM   1845 C CG  . GLU   A 1 257 ? 17.823  2.795   -4.193  1.00 16.37  ? 794  GLU   A CG  1 
ATOM   1846 C CD  . GLU   A 1 257 ? 19.168  3.121   -4.839  1.00 21.85  ? 794  GLU   A CD  1 
ATOM   1847 O OE1 . GLU   A 1 257 ? 19.850  4.058   -4.361  1.00 20.31  ? 794  GLU   A OE1 1 
ATOM   1848 O OE2 . GLU   A 1 257 ? 19.541  2.449   -5.826  1.00 15.97  ? 794  GLU   A OE2 1 
ATOM   1849 N N   . SER   A 1 258 ? 16.171  -1.449  -2.806  1.00 23.86  ? 795  SER   A N   1 
ATOM   1850 C CA  . SER   A 1 258 ? 15.627  -2.785  -3.026  1.00 25.09  ? 795  SER   A CA  1 
ATOM   1851 C C   . SER   A 1 258 ? 14.174  -2.865  -2.584  1.00 27.39  ? 795  SER   A C   1 
ATOM   1852 O O   . SER   A 1 258 ? 13.338  -3.436  -3.293  1.00 20.11  ? 795  SER   A O   1 
ATOM   1853 C CB  . SER   A 1 258 ? 16.465  -3.829  -2.288  1.00 24.49  ? 795  SER   A CB  1 
ATOM   1854 O OG  . SER   A 1 258 ? 15.932  -5.136  -2.451  1.00 23.91  ? 795  SER   A OG  1 
ATOM   1855 N N   . ASP   A 1 259 ? 13.854  -2.291  -1.418  1.00 28.35  ? 796  ASP   A N   1 
ATOM   1856 C CA  . ASP   A 1 259 ? 12.476  -2.311  -0.933  1.00 30.84  ? 796  ASP   A CA  1 
ATOM   1857 C C   . ASP   A 1 259 ? 11.561  -1.484  -1.825  1.00 30.04  ? 796  ASP   A C   1 
ATOM   1858 O O   . ASP   A 1 259 ? 10.420  -1.880  -2.093  1.00 32.28  ? 796  ASP   A O   1 
ATOM   1859 C CB  . ASP   A 1 259 ? 12.412  -1.806  0.507   1.00 32.32  ? 796  ASP   A CB  1 
ATOM   1860 C CG  . ASP   A 1 259 ? 13.058  -2.758  1.475   1.00 35.57  ? 796  ASP   A CG  1 
ATOM   1861 O OD1 . ASP   A 1 259 ? 13.239  -3.941  1.110   1.00 38.70  ? 796  ASP   A OD1 1 
ATOM   1862 O OD2 . ASP   A 1 259 ? 13.379  -2.330  2.602   1.00 36.42  ? 796  ASP   A OD2 1 
ATOM   1863 N N   . LEU   A 1 260 ? 12.041  -0.333  -2.291  1.00 26.31  ? 797  LEU   A N   1 
ATOM   1864 C CA  . LEU   A 1 260 ? 11.230  0.478   -3.186  1.00 25.84  ? 797  LEU   A CA  1 
ATOM   1865 C C   . LEU   A 1 260 ? 10.959  -0.255  -4.492  1.00 26.09  ? 797  LEU   A C   1 
ATOM   1866 O O   . LEU   A 1 260 ? 9.829   -0.247  -4.992  1.00 26.47  ? 797  LEU   A O   1 
ATOM   1867 C CB  . LEU   A 1 260 ? 11.920  1.814   -3.444  1.00 24.87  ? 797  LEU   A CB  1 
ATOM   1868 C CG  . LEU   A 1 260 ? 12.188  2.640   -2.186  1.00 25.67  ? 797  LEU   A CG  1 
ATOM   1869 C CD1 . LEU   A 1 260 ? 13.018  3.869   -2.522  1.00 25.06  ? 797  LEU   A CD1 1 
ATOM   1870 C CD2 . LEU   A 1 260 ? 10.873  3.030   -1.505  1.00 26.47  ? 797  LEU   A CD2 1 
ATOM   1871 N N   . TYR   A 1 261 ? 11.980  -0.912  -5.048  1.00 25.81  ? 798  TYR   A N   1 
ATOM   1872 C CA  . TYR   A 1 261 ? 11.792  -1.618  -6.312  1.00 25.40  ? 798  TYR   A CA  1 
ATOM   1873 C C   . TYR   A 1 261 ? 10.838  -2.796  -6.149  1.00 25.41  ? 798  TYR   A C   1 
ATOM   1874 O O   . TYR   A 1 261 ? 10.042  -3.086  -7.050  1.00 20.87  ? 798  TYR   A O   1 
ATOM   1875 C CB  . TYR   A 1 261 ? 13.143  -2.088  -6.857  1.00 23.51  ? 798  TYR   A CB  1 
ATOM   1876 C CG  . TYR   A 1 261 ? 13.052  -2.858  -8.160  1.00 24.15  ? 798  TYR   A CG  1 
ATOM   1877 C CD1 . TYR   A 1 261 ? 13.007  -2.192  -9.382  1.00 24.20  ? 798  TYR   A CD1 1 
ATOM   1878 C CD2 . TYR   A 1 261 ? 13.016  -4.248  -8.169  1.00 25.24  ? 798  TYR   A CD2 1 
ATOM   1879 C CE1 . TYR   A 1 261 ? 12.928  -2.888  -10.575 1.00 24.72  ? 798  TYR   A CE1 1 
ATOM   1880 C CE2 . TYR   A 1 261 ? 12.931  -4.956  -9.360  1.00 26.36  ? 798  TYR   A CE2 1 
ATOM   1881 C CZ  . TYR   A 1 261 ? 12.890  -4.270  -10.559 1.00 26.47  ? 798  TYR   A CZ  1 
ATOM   1882 O OH  . TYR   A 1 261 ? 12.810  -4.971  -11.746 1.00 28.29  ? 798  TYR   A OH  1 
ATOM   1883 N N   A ARG   A 1 262 ? 10.902  -3.487  -5.008  0.48 24.90  ? 799  ARG   A N   1 
ATOM   1884 N N   B ARG   A 1 262 ? 10.896  -3.472  -4.997  0.52 24.89  ? 799  ARG   A N   1 
ATOM   1885 C CA  A ARG   A 1 262 ? 10.075  -4.674  -4.809  0.48 26.40  ? 799  ARG   A CA  1 
ATOM   1886 C CA  B ARG   A 1 262 ? 10.096  -4.673  -4.770  0.52 26.31  ? 799  ARG   A CA  1 
ATOM   1887 C C   A ARG   A 1 262 ? 8.593   -4.330  -4.723  0.48 25.44  ? 799  ARG   A C   1 
ATOM   1888 C C   B ARG   A 1 262 ? 8.608   -4.359  -4.647  0.52 25.45  ? 799  ARG   A C   1 
ATOM   1889 O O   A ARG   A 1 262 ? 7.750   -5.117  -5.166  0.48 26.59  ? 799  ARG   A O   1 
ATOM   1890 O O   B ARG   A 1 262 ? 7.771   -5.194  -5.007  0.52 26.60  ? 799  ARG   A O   1 
ATOM   1891 C CB  A ARG   A 1 262 ? 10.518  -5.412  -3.545  0.48 25.56  ? 799  ARG   A CB  1 
ATOM   1892 C CB  B ARG   A 1 262 ? 10.611  -5.398  -3.520  0.52 25.53  ? 799  ARG   A CB  1 
ATOM   1893 C CG  A ARG   A 1 262 ? 9.638   -6.586  -3.172  0.48 27.33  ? 799  ARG   A CG  1 
ATOM   1894 C CG  B ARG   A 1 262 ? 9.600   -6.265  -2.802  0.52 27.20  ? 799  ARG   A CG  1 
ATOM   1895 C CD  A ARG   A 1 262 ? 10.066  -7.200  -1.851  0.48 28.16  ? 799  ARG   A CD  1 
ATOM   1896 C CD  B ARG   A 1 262 ? 10.223  -7.017  -1.630  0.52 28.06  ? 799  ARG   A CD  1 
ATOM   1897 N NE  A ARG   A 1 262 ? 10.257  -6.189  -0.814  0.48 27.86  ? 799  ARG   A NE  1 
ATOM   1898 N NE  B ARG   A 1 262 ? 11.429  -6.371  -1.115  0.52 27.88  ? 799  ARG   A NE  1 
ATOM   1899 C CZ  A ARG   A 1 262 ? 9.273   -5.646  -0.107  0.48 28.61  ? 799  ARG   A CZ  1 
ATOM   1900 C CZ  B ARG   A 1 262 ? 12.607  -6.979  -0.996  0.52 28.51  ? 799  ARG   A CZ  1 
ATOM   1901 N NH1 A ARG   A 1 262 ? 8.014   -6.007  -0.325  0.48 29.42  ? 799  ARG   A NH1 1 
ATOM   1902 N NH1 B ARG   A 1 262 ? 12.734  -8.254  -1.340  0.52 29.37  ? 799  ARG   A NH1 1 
ATOM   1903 N NH2 A ARG   A 1 262 ? 9.547   -4.738  0.818   0.48 28.72  ? 799  ARG   A NH2 1 
ATOM   1904 N NH2 B ARG   A 1 262 ? 13.654  -6.319  -0.517  0.52 27.63  ? 799  ARG   A NH2 1 
ATOM   1905 N N   . LYS   A 1 263 ? 8.257   -3.165  -4.174  1.00 25.29  ? 800  LYS   A N   1 
ATOM   1906 C CA  . LYS   A 1 263 ? 6.866   -2.824  -3.910  1.00 25.78  ? 800  LYS   A CA  1 
ATOM   1907 C C   . LYS   A 1 263 ? 6.129   -2.245  -5.110  1.00 25.55  ? 800  LYS   A C   1 
ATOM   1908 O O   . LYS   A 1 263 ? 4.952   -1.905  -4.974  1.00 27.41  ? 800  LYS   A O   1 
ATOM   1909 C CB  . LYS   A 1 263 ? 6.781   -1.839  -2.740  1.00 27.09  ? 800  LYS   A CB  1 
ATOM   1910 C CG  . LYS   A 1 263 ? 7.230   -2.420  -1.412  1.00 28.39  ? 800  LYS   A CG  1 
ATOM   1911 C CD  . LYS   A 1 263 ? 7.182   -1.376  -0.309  1.00 30.31  ? 800  LYS   A CD  1 
ATOM   1912 C CE  . LYS   A 1 263 ? 7.634   -1.964  1.019   1.00 32.35  ? 800  LYS   A CE  1 
ATOM   1913 N NZ  . LYS   A 1 263 ? 7.696   -0.934  2.092   1.00 33.72  ? 800  LYS   A NZ  1 
ATOM   1914 N N   . VAL   A 1 264 ? 6.766   -2.122  -6.271  1.00 24.69  ? 801  VAL   A N   1 
ATOM   1915 C CA  . VAL   A 1 264 ? 6.078   -1.597  -7.449  1.00 25.03  ? 801  VAL   A CA  1 
ATOM   1916 C C   . VAL   A 1 264 ? 5.196   -2.687  -8.041  1.00 25.49  ? 801  VAL   A C   1 
ATOM   1917 O O   . VAL   A 1 264 ? 5.658   -3.803  -8.308  1.00 25.75  ? 801  VAL   A O   1 
ATOM   1918 C CB  . VAL   A 1 264 ? 7.080   -1.076  -8.491  1.00 24.88  ? 801  VAL   A CB  1 
ATOM   1919 C CG1 . VAL   A 1 264 ? 6.350   -0.645  -9.752  1.00 25.64  ? 801  VAL   A CG1 1 
ATOM   1920 C CG2 . VAL   A 1 264 ? 7.893   0.076   -7.926  1.00 23.75  ? 801  VAL   A CG2 1 
ATOM   1921 N N   . GLN   A 1 265 ? 3.928   -2.366  -8.251  1.00 27.19  ? 802  GLN   A N   1 
ATOM   1922 C CA  . GLN   A 1 265 ? 2.994   -3.290  -8.874  1.00 28.54  ? 802  GLN   A CA  1 
ATOM   1923 C C   . GLN   A 1 265 ? 2.844   -2.975  -10.355 1.00 29.00  ? 802  GLN   A C   1 
ATOM   1924 O O   . GLN   A 1 265 ? 2.832   -1.804  -10.736 1.00 31.54  ? 802  GLN   A O   1 
ATOM   1925 C CB  . GLN   A 1 265 ? 1.626   -3.209  -8.198  1.00 29.68  ? 802  GLN   A CB  1 
ATOM   1926 C CG  . GLN   A 1 265 ? 1.679   -3.457  -6.707  1.00 29.99  ? 802  GLN   A CG  1 
ATOM   1927 C CD  . GLN   A 1 265 ? 2.196   -4.841  -6.364  1.00 29.49  ? 802  GLN   A CD  1 
ATOM   1928 O OE1 . GLN   A 1 265 ? 1.969   -5.805  -7.099  1.00 30.80  ? 802  GLN   A OE1 1 
ATOM   1929 N NE2 . GLN   A 1 265 ? 2.896   -4.947  -5.245  1.00 27.37  ? 802  GLN   A NE2 1 
ATOM   1930 N N   . PRO   A 1 266 ? 2.731   -4.001  -11.199 1.00 29.09  ? 803  PRO   A N   1 
ATOM   1931 C CA  . PRO   A 1 266 ? 2.622   -3.763  -12.650 1.00 29.70  ? 803  PRO   A CA  1 
ATOM   1932 C C   . PRO   A 1 266 ? 1.530   -2.783  -13.056 1.00 31.19  ? 803  PRO   A C   1 
ATOM   1933 O O   . PRO   A 1 266 ? 1.709   -2.049  -14.038 1.00 31.43  ? 803  PRO   A O   1 
ATOM   1934 C CB  . PRO   A 1 266 ? 2.335   -5.164  -13.205 1.00 31.26  ? 803  PRO   A CB  1 
ATOM   1935 C CG  . PRO   A 1 266 ? 2.916   -6.096  -12.206 1.00 30.84  ? 803  PRO   A CG  1 
ATOM   1936 C CD  . PRO   A 1 266 ? 2.779   -5.435  -10.868 1.00 30.15  ? 803  PRO   A CD  1 
ATOM   1937 N N   . SER   A 1 267 ? 0.398   -2.755  -12.347 1.00 32.15  ? 804  SER   A N   1 
ATOM   1938 C CA  . SER   A 1 267 ? -0.678  -1.843  -12.717 1.00 33.69  ? 804  SER   A CA  1 
ATOM   1939 C C   . SER   A 1 267 ? -0.236  -0.386  -12.643 1.00 34.22  ? 804  SER   A C   1 
ATOM   1940 O O   . SER   A 1 267 ? -0.735  0.453   -13.405 1.00 30.34  ? 804  SER   A O   1 
ATOM   1941 C CB  . SER   A 1 267 ? -1.892  -2.071  -11.818 1.00 34.39  ? 804  SER   A CB  1 
ATOM   1942 O OG  . SER   A 1 267 ? -1.578  -1.804  -10.463 1.00 30.10  ? 804  SER   A OG  1 
ATOM   1943 N N   . GLU   A 1 268 ? 0.699   -0.065  -11.741 1.00 32.78  ? 805  GLU   A N   1 
ATOM   1944 C CA  . GLU   A 1 268 ? 1.154   1.312   -11.584 1.00 31.75  ? 805  GLU   A CA  1 
ATOM   1945 C C   . GLU   A 1 268 ? 1.860   1.837   -12.825 1.00 32.69  ? 805  GLU   A C   1 
ATOM   1946 O O   . GLU   A 1 268 ? 2.102   3.045   -12.913 1.00 27.36  ? 805  GLU   A O   1 
ATOM   1947 C CB  . GLU   A 1 268 ? 2.084   1.432   -10.371 1.00 29.33  ? 805  GLU   A CB  1 
ATOM   1948 C CG  . GLU   A 1 268 ? 1.502   0.868   -9.096  1.00 30.18  ? 805  GLU   A CG  1 
ATOM   1949 C CD  . GLU   A 1 268 ? 2.379   1.108   -7.886  1.00 30.28  ? 805  GLU   A CD  1 
ATOM   1950 O OE1 . GLU   A 1 268 ? 2.952   2.211   -7.769  1.00 30.78  ? 805  GLU   A OE1 1 
ATOM   1951 O OE2 . GLU   A 1 268 ? 2.495   0.191   -7.046  1.00 30.63  ? 805  GLU   A OE2 1 
ATOM   1952 N N   . LEU   A 1 269 ? 2.189   0.963   -13.779 1.00 33.80  ? 806  LEU   A N   1 
ATOM   1953 C CA  . LEU   A 1 269 ? 2.881   1.347   -14.999 1.00 34.30  ? 806  LEU   A CA  1 
ATOM   1954 C C   . LEU   A 1 269 ? 2.000   1.314   -16.239 1.00 34.57  ? 806  LEU   A C   1 
ATOM   1955 O O   . LEU   A 1 269 ? 2.352   1.948   -17.238 1.00 34.37  ? 806  LEU   A O   1 
ATOM   1956 C CB  . LEU   A 1 269 ? 4.096   0.432   -15.226 1.00 34.38  ? 806  LEU   A CB  1 
ATOM   1957 C CG  . LEU   A 1 269 ? 5.145   0.434   -14.113 1.00 33.89  ? 806  LEU   A CG  1 
ATOM   1958 C CD1 . LEU   A 1 269 ? 5.325   -0.953  -13.524 1.00 33.99  ? 806  LEU   A CD1 1 
ATOM   1959 C CD2 . LEU   A 1 269 ? 6.463   0.958   -14.639 1.00 34.45  ? 806  LEU   A CD2 1 
ATOM   1960 N N   . VAL   A 1 270 ? 0.875   0.592   -16.203 1.00 35.52  ? 807  VAL   A N   1 
ATOM   1961 C CA  . VAL   A 1 270 ? -0.006  0.507   -17.361 1.00 36.72  ? 807  VAL   A CA  1 
ATOM   1962 C C   . VAL   A 1 270 ? -0.654  1.861   -17.609 1.00 38.95  ? 807  VAL   A C   1 
ATOM   1963 O O   . VAL   A 1 270 ? -1.031  2.572   -16.669 1.00 38.13  ? 807  VAL   A O   1 
ATOM   1964 C CB  . VAL   A 1 270 ? -1.074  -0.582  -17.157 1.00 36.69  ? 807  VAL   A CB  1 
ATOM   1965 C CG1 . VAL   A 1 270 ? -1.887  -0.777  -18.434 1.00 38.03  ? 807  VAL   A CG1 1 
ATOM   1966 C CG2 . VAL   A 1 270 ? -0.441  -1.892  -16.724 1.00 35.45  ? 807  VAL   A CG2 1 
ATOM   1967 N N   . GLY   A 1 271 ? -0.779  2.227   -18.882 1.00 43.40  ? 808  GLY   A N   1 
ATOM   1968 C CA  . GLY   A 1 271 ? -1.478  3.443   -19.251 1.00 47.07  ? 808  GLY   A CA  1 
ATOM   1969 C C   . GLY   A 1 271 ? -0.785  4.731   -18.876 1.00 48.18  ? 808  GLY   A C   1 
ATOM   1970 O O   . GLY   A 1 271 ? -1.408  5.795   -18.941 1.00 49.87  ? 808  GLY   A O   1 
ATOM   1971 N N   . SER   A 1 272 ? 0.489   4.669   -18.487 1.00 47.77  ? 809  SER   A N   1 
ATOM   1972 C CA  . SER   A 1 272 ? 1.228   5.843   -18.018 1.00 48.60  ? 809  SER   A CA  1 
ATOM   1973 C C   . SER   A 1 272 ? 0.450   6.586   -16.937 1.00 48.11  ? 809  SER   A C   1 
ATOM   1974 O O   . SER   A 1 272 ? 0.468   7.816   -16.863 1.00 48.82  ? 809  SER   A O   1 
ATOM   1975 C CB  . SER   A 1 272 ? 1.578   6.777   -19.176 1.00 51.51  ? 809  SER   A CB  1 
ATOM   1976 O OG  . SER   A 1 272 ? 2.548   6.190   -20.025 1.00 52.56  ? 809  SER   A OG  1 
ATOM   1977 N N   . VAL   A 1 273 ? -0.246  5.823   -16.088 1.00 46.74  ? 810  VAL   A N   1 
ATOM   1978 C CA  . VAL   A 1 273 ? -1.065  6.414   -15.036 1.00 45.60  ? 810  VAL   A CA  1 
ATOM   1979 C C   . VAL   A 1 273 ? -0.225  7.151   -14.006 1.00 43.52  ? 810  VAL   A C   1 
ATOM   1980 O O   . VAL   A 1 273 ? -0.761  7.952   -13.233 1.00 43.42  ? 810  VAL   A O   1 
ATOM   1981 C CB  . VAL   A 1 273 ? -1.925  5.330   -14.358 1.00 44.75  ? 810  VAL   A CB  1 
ATOM   1982 C CG1 . VAL   A 1 273 ? -2.963  4.805   -15.325 1.00 46.55  ? 810  VAL   A CG1 1 
ATOM   1983 C CG2 . VAL   A 1 273 ? -1.036  4.202   -13.846 1.00 42.81  ? 810  VAL   A CG2 1 
ATOM   1984 N N   . TRP   A 1 274 ? 1.086   6.899   -13.963 1.00 42.40  ? 811  TRP   A N   1 
ATOM   1985 C CA  . TRP   A 1 274 ? 1.934   7.661   -13.057 1.00 41.81  ? 811  TRP   A CA  1 
ATOM   1986 C C   . TRP   A 1 274 ? 2.229   9.059   -13.585 1.00 42.32  ? 811  TRP   A C   1 
ATOM   1987 O O   . TRP   A 1 274 ? 2.705   9.903   -12.821 1.00 42.20  ? 811  TRP   A O   1 
ATOM   1988 C CB  . TRP   A 1 274 ? 3.237   6.901   -12.772 1.00 40.73  ? 811  TRP   A CB  1 
ATOM   1989 C CG  . TRP   A 1 274 ? 4.338   7.079   -13.776 1.00 40.90  ? 811  TRP   A CG  1 
ATOM   1990 C CD1 . TRP   A 1 274 ? 5.362   7.973   -13.710 1.00 40.61  ? 811  TRP   A CD1 1 
ATOM   1991 C CD2 . TRP   A 1 274 ? 4.542   6.324   -14.983 1.00 42.03  ? 811  TRP   A CD2 1 
ATOM   1992 N NE1 . TRP   A 1 274 ? 6.186   7.834   -14.802 1.00 40.92  ? 811  TRP   A NE1 1 
ATOM   1993 C CE2 . TRP   A 1 274 ? 5.704   6.829   -15.599 1.00 41.20  ? 811  TRP   A CE2 1 
ATOM   1994 C CE3 . TRP   A 1 274 ? 3.851   5.276   -15.604 1.00 43.36  ? 811  TRP   A CE3 1 
ATOM   1995 C CZ2 . TRP   A 1 274 ? 6.192   6.325   -16.804 1.00 41.09  ? 811  TRP   A CZ2 1 
ATOM   1996 C CZ3 . TRP   A 1 274 ? 4.340   4.776   -16.804 1.00 43.45  ? 811  TRP   A CZ3 1 
ATOM   1997 C CH2 . TRP   A 1 274 ? 5.498   5.303   -17.389 1.00 42.51  ? 811  TRP   A CH2 1 
ATOM   1998 N N   . THR   A 1 275 ? 1.945   9.327   -14.860 1.00 44.09  ? 812  THR   A N   1 
ATOM   1999 C CA  . THR   A 1 275 ? 2.029   10.667  -15.434 1.00 46.13  ? 812  THR   A CA  1 
ATOM   2000 C C   . THR   A 1 275 ? 0.647   11.195  -15.796 1.00 50.20  ? 812  THR   A C   1 
ATOM   2001 O O   . THR   A 1 275 ? 0.472   11.848  -16.827 1.00 52.39  ? 812  THR   A O   1 
ATOM   2002 C CB  . THR   A 1 275 ? 2.912   10.692  -16.678 1.00 46.38  ? 812  THR   A CB  1 
ATOM   2003 O OG1 . THR   A 1 275 ? 2.178   10.169  -17.793 1.00 48.45  ? 812  THR   A OG1 1 
ATOM   2004 C CG2 . THR   A 1 275 ? 4.174   9.873   -16.474 1.00 44.64  ? 812  THR   A CG2 1 
ATOM   2005 N N   . LYS   A 1 276 ? -0.357  10.904  -14.968 1.00 51.65  ? 813  LYS   A N   1 
ATOM   2006 C CA  . LYS   A 1 276 ? -1.727  11.292  -15.268 1.00 54.40  ? 813  LYS   A CA  1 
ATOM   2007 C C   . LYS   A 1 276 ? -2.391  11.837  -14.010 1.00 55.16  ? 813  LYS   A C   1 
ATOM   2008 O O   . LYS   A 1 276 ? -1.764  11.960  -12.952 1.00 53.10  ? 813  LYS   A O   1 
ATOM   2009 C CB  . LYS   A 1 276 ? -2.514  10.122  -15.868 1.00 55.81  ? 813  LYS   A CB  1 
ATOM   2010 C CG  . LYS   A 1 276 ? -2.220  9.908   -17.343 1.00 57.02  ? 813  LYS   A CG  1 
ATOM   2011 C CD  . LYS   A 1 276 ? -3.037  8.777   -17.930 1.00 58.33  ? 813  LYS   A CD  1 
ATOM   2012 C CE  . LYS   A 1 276 ? -2.786  8.656   -19.425 1.00 59.83  ? 813  LYS   A CE  1 
ATOM   2013 N NZ  . LYS   A 1 276 ? -3.576  7.557   -20.045 1.00 61.24  ? 813  LYS   A NZ  1 
ATOM   2014 N N   . GLU   A 1 277 ? -3.688  12.139  -14.139 1.00 58.52  ? 814  GLU   A N   1 
ATOM   2015 C CA  . GLU   A 1 277 ? -4.382  12.998  -13.180 1.00 60.90  ? 814  GLU   A CA  1 
ATOM   2016 C C   . GLU   A 1 277 ? -4.324  12.430  -11.766 1.00 60.29  ? 814  GLU   A C   1 
ATOM   2017 O O   . GLU   A 1 277 ? -3.938  13.127  -10.819 1.00 59.91  ? 814  GLU   A O   1 
ATOM   2018 C CB  . GLU   A 1 277 ? -5.831  13.199  -13.631 1.00 64.17  ? 814  GLU   A CB  1 
ATOM   2019 C CG  . GLU   A 1 277 ? -6.442  14.534  -13.222 1.00 68.02  ? 814  GLU   A CG  1 
ATOM   2020 C CD  . GLU   A 1 277 ? -7.824  14.766  -13.826 1.00 73.24  ? 814  GLU   A CD  1 
ATOM   2021 O OE1 . GLU   A 1 277 ? -8.768  14.015  -13.489 1.00 74.37  ? 814  GLU   A OE1 1 
ATOM   2022 O OE2 . GLU   A 1 277 ? -7.964  15.699  -14.647 1.00 75.75  ? 814  GLU   A OE2 1 
ATOM   2023 N N   . ASP   A 1 278 ? -4.702  11.165  -11.602 1.00 60.15  ? 815  ASP   A N   1 
ATOM   2024 C CA  . ASP   A 1 278 ? -4.707  10.508  -10.296 1.00 59.30  ? 815  ASP   A CA  1 
ATOM   2025 C C   . ASP   A 1 278 ? -3.428  9.717   -10.054 1.00 54.22  ? 815  ASP   A C   1 
ATOM   2026 O O   . ASP   A 1 278 ? -3.481  8.581   -9.577  1.00 53.59  ? 815  ASP   A O   1 
ATOM   2027 C CB  . ASP   A 1 278 ? -5.932  9.605   -10.169 1.00 62.85  ? 815  ASP   A CB  1 
ATOM   2028 C CG  . ASP   A 1 278 ? -7.235  10.373  -10.294 1.00 66.74  ? 815  ASP   A CG  1 
ATOM   2029 O OD1 . ASP   A 1 278 ? -7.199  11.530  -10.761 1.00 68.21  ? 815  ASP   A OD1 1 
ATOM   2030 O OD2 . ASP   A 1 278 ? -8.289  9.823   -9.911  1.00 68.11  ? 815  ASP   A OD2 1 
ATOM   2031 N N   . LYS   A 1 279 ? -2.265  10.296  -10.369 1.00 50.45  ? 816  LYS   A N   1 
ATOM   2032 C CA  . LYS   A 1 279 ? -1.011  9.551   -10.271 1.00 46.20  ? 816  LYS   A CA  1 
ATOM   2033 C C   . LYS   A 1 279 ? -0.712  9.139   -8.834  1.00 44.54  ? 816  LYS   A C   1 
ATOM   2034 O O   . LYS   A 1 279 ? -0.183  8.047   -8.592  1.00 42.80  ? 816  LYS   A O   1 
ATOM   2035 C CB  . LYS   A 1 279 ? 0.145   10.383  -10.840 1.00 44.44  ? 816  LYS   A CB  1 
ATOM   2036 C CG  . LYS   A 1 279 ? 0.331   11.747  -10.181 1.00 44.04  ? 816  LYS   A CG  1 
ATOM   2037 C CD  . LYS   A 1 279 ? 1.685   12.363  -10.508 1.00 42.17  ? 816  LYS   A CD  1 
ATOM   2038 C CE  . LYS   A 1 279 ? 1.714   12.997  -11.892 1.00 43.09  ? 816  LYS   A CE  1 
ATOM   2039 N NZ  . LYS   A 1 279 ? 1.099   14.357  -11.918 1.00 45.31  ? 816  LYS   A NZ  1 
ATOM   2040 N N   . GLU   A 1 280 ? -1.049  9.995   -7.865  1.00 45.05  ? 817  GLU   A N   1 
ATOM   2041 C CA  . GLU   A 1 280 ? -0.681  9.722   -6.480  1.00 43.19  ? 817  GLU   A CA  1 
ATOM   2042 C C   . GLU   A 1 280 ? -1.442  8.529   -5.923  1.00 44.91  ? 817  GLU   A C   1 
ATOM   2043 O O   . GLU   A 1 280 ? -0.926  7.820   -5.052  1.00 45.60  ? 817  GLU   A O   1 
ATOM   2044 C CB  . GLU   A 1 280 ? -0.926  10.959  -5.612  1.00 43.07  ? 817  GLU   A CB  1 
ATOM   2045 C CG  . GLU   A 1 280 ? -0.296  12.253  -6.137  1.00 42.74  ? 817  GLU   A CG  1 
ATOM   2046 C CD  . GLU   A 1 280 ? 1.226   12.287  -6.025  1.00 40.88  ? 817  GLU   A CD  1 
ATOM   2047 O OE1 . GLU   A 1 280 ? 1.791   11.592  -5.155  1.00 39.74  ? 817  GLU   A OE1 1 
ATOM   2048 O OE2 . GLU   A 1 280 ? 1.857   13.019  -6.814  1.00 40.26  ? 817  GLU   A OE2 1 
ATOM   2049 N N   . ILE   A 1 281 ? -2.652  8.285   -6.417  1.00 46.03  ? 818  ILE   A N   1 
ATOM   2050 C CA  . ILE   A 1 281 ? -3.469  7.177   -5.931  1.00 46.43  ? 818  ILE   A CA  1 
ATOM   2051 C C   . ILE   A 1 281 ? -3.135  5.876   -6.652  1.00 43.15  ? 818  ILE   A C   1 
ATOM   2052 O O   . ILE   A 1 281 ? -3.054  4.818   -6.023  1.00 42.55  ? 818  ILE   A O   1 
ATOM   2053 C CB  . ILE   A 1 281 ? -4.962  7.539   -6.075  1.00 50.96  ? 818  ILE   A CB  1 
ATOM   2054 C CG1 . ILE   A 1 281 ? -5.349  8.614   -5.057  1.00 53.28  ? 818  ILE   A CG1 1 
ATOM   2055 C CG2 . ILE   A 1 281 ? -5.843  6.314   -5.913  1.00 52.34  ? 818  ILE   A CG2 1 
ATOM   2056 C CD1 . ILE   A 1 281 ? -5.236  8.156   -3.619  1.00 53.43  ? 818  ILE   A CD1 1 
ATOM   2057 N N   . ASN   A 1 282 ? -2.925  5.933   -7.971  1.00 40.52  ? 819  ASN   A N   1 
ATOM   2058 C CA  . ASN   A 1 282 ? -2.761  4.733   -8.783  1.00 36.92  ? 819  ASN   A CA  1 
ATOM   2059 C C   . ASN   A 1 282 ? -1.320  4.251   -8.869  1.00 33.46  ? 819  ASN   A C   1 
ATOM   2060 O O   . ASN   A 1 282 ? -1.093  3.093   -9.242  1.00 32.36  ? 819  ASN   A O   1 
ATOM   2061 C CB  . ASN   A 1 282 ? -3.291  4.970   -10.206 1.00 37.45  ? 819  ASN   A CB  1 
ATOM   2062 C CG  . ASN   A 1 282 ? -4.764  5.350   -10.232 1.00 40.76  ? 819  ASN   A CG  1 
ATOM   2063 O OD1 . ASN   A 1 282 ? -5.553  4.885   -9.409  1.00 42.12  ? 819  ASN   A OD1 1 
ATOM   2064 N ND2 . ASN   A 1 282 ? -5.140  6.199   -11.183 1.00 42.18  ? 819  ASN   A ND2 1 
ATOM   2065 N N   . SER   A 1 283 ? -0.344  5.095   -8.541  1.00 32.62  ? 820  SER   A N   1 
ATOM   2066 C CA  . SER   A 1 283 ? 1.051   4.680   -8.658  1.00 29.86  ? 820  SER   A CA  1 
ATOM   2067 C C   . SER   A 1 283 ? 1.881   5.127   -7.458  1.00 28.76  ? 820  SER   A C   1 
ATOM   2068 O O   . SER   A 1 283 ? 2.945   5.731   -7.636  1.00 26.72  ? 820  SER   A O   1 
ATOM   2069 C CB  . SER   A 1 283 ? 1.652   5.233   -9.951  1.00 29.30  ? 820  SER   A CB  1 
ATOM   2070 O OG  . SER   A 1 283 ? 0.991   4.710   -11.088 1.00 29.94  ? 820  SER   A OG  1 
ATOM   2071 N N   . PRO   A 1 284 ? 1.457   4.828   -6.226  1.00 29.18  ? 821  PRO   A N   1 
ATOM   2072 C CA  . PRO   A 1 284 ? 2.220   5.334   -5.074  1.00 27.96  ? 821  PRO   A CA  1 
ATOM   2073 C C   . PRO   A 1 284 ? 3.618   4.747   -4.966  1.00 26.77  ? 821  PRO   A C   1 
ATOM   2074 O O   . PRO   A 1 284 ? 4.571   5.494   -4.710  1.00 27.13  ? 821  PRO   A O   1 
ATOM   2075 C CB  . PRO   A 1 284 ? 1.340   4.948   -3.881  1.00 29.19  ? 821  PRO   A CB  1 
ATOM   2076 C CG  . PRO   A 1 284 ? 0.607   3.742   -4.342  1.00 30.10  ? 821  PRO   A CG  1 
ATOM   2077 C CD  . PRO   A 1 284 ? 0.343   3.958   -5.804  1.00 29.91  ? 821  PRO   A CD  1 
ATOM   2078 N N   . ASN   A 1 285 ? 3.777   3.435   -5.161  1.00 26.18  ? 822  ASN   A N   1 
ATOM   2079 C CA  . ASN   A 1 285 ? 5.093   2.823   -4.985  1.00 24.44  ? 822  ASN   A CA  1 
ATOM   2080 C C   . ASN   A 1 285 ? 6.048   3.224   -6.103  1.00 24.43  ? 822  ASN   A C   1 
ATOM   2081 O O   . ASN   A 1 285 ? 7.226   3.505   -5.848  1.00 21.44  ? 822  ASN   A O   1 
ATOM   2082 C CB  . ASN   A 1 285 ? 4.959   1.304   -4.910  1.00 24.46  ? 822  ASN   A CB  1 
ATOM   2083 C CG  . ASN   A 1 285 ? 3.974   0.859   -3.841  1.00 26.55  ? 822  ASN   A CG  1 
ATOM   2084 O OD1 . ASN   A 1 285 ? 4.318   0.790   -2.659  1.00 24.53  ? 822  ASN   A OD1 1 
ATOM   2085 N ND2 . ASN   A 1 285 ? 2.748   0.553   -4.251  1.00 25.47  ? 822  ASN   A ND2 1 
ATOM   2086 N N   . LEU   A 1 286 ? 5.555   3.259   -7.347  1.00 24.51  ? 823  LEU   A N   1 
ATOM   2087 C CA  . LEU   A 1 286 ? 6.380   3.685   -8.472  1.00 22.18  ? 823  LEU   A CA  1 
ATOM   2088 C C   . LEU   A 1 286 ? 6.831   5.134   -8.314  1.00 21.97  ? 823  LEU   A C   1 
ATOM   2089 O O   . LEU   A 1 286 ? 7.966   5.479   -8.660  1.00 25.64  ? 823  LEU   A O   1 
ATOM   2090 C CB  . LEU   A 1 286 ? 5.608   3.485   -9.782  1.00 23.04  ? 823  LEU   A CB  1 
ATOM   2091 C CG  . LEU   A 1 286 ? 5.965   4.280   -11.045 1.00 26.59  ? 823  LEU   A CG  1 
ATOM   2092 C CD1 . LEU   A 1 286 ? 7.401   4.116   -11.387 1.00 22.19  ? 823  LEU   A CD1 1 
ATOM   2093 C CD2 . LEU   A 1 286 ? 5.107   3.865   -12.242 1.00 27.49  ? 823  LEU   A CD2 1 
ATOM   2094 N N   . LEU   A 1 287 ? 5.959   6.002   -7.802  1.00 22.85  ? 824  LEU   A N   1 
ATOM   2095 C CA  . LEU   A 1 287 ? 6.360   7.392   -7.622  1.00 28.36  ? 824  LEU   A CA  1 
ATOM   2096 C C   . LEU   A 1 287 ? 7.403   7.528   -6.521  1.00 27.56  ? 824  LEU   A C   1 
ATOM   2097 O O   . LEU   A 1 287 ? 8.278   8.396   -6.607  1.00 26.02  ? 824  LEU   A O   1 
ATOM   2098 C CB  . LEU   A 1 287 ? 5.144   8.268   -7.322  1.00 24.32  ? 824  LEU   A CB  1 
ATOM   2099 C CG  . LEU   A 1 287 ? 4.173   8.492   -8.479  1.00 29.40  ? 824  LEU   A CG  1 
ATOM   2100 C CD1 . LEU   A 1 287 ? 2.946   9.219   -7.973  1.00 31.38  ? 824  LEU   A CD1 1 
ATOM   2101 C CD2 . LEU   A 1 287 ? 4.829   9.269   -9.611  1.00 28.79  ? 824  LEU   A CD2 1 
ATOM   2102 N N   . LYS   A 1 288 ? 7.331   6.684   -5.486  1.00 28.46  ? 825  LYS   A N   1 
ATOM   2103 C CA  . LYS   A 1 288 ? 8.352   6.721   -4.446  1.00 28.99  ? 825  LYS   A CA  1 
ATOM   2104 C C   . LYS   A 1 288 ? 9.701   6.275   -4.984  1.00 27.18  ? 825  LYS   A C   1 
ATOM   2105 O O   . LYS   A 1 288 ? 10.742  6.729   -4.497  1.00 26.27  ? 825  LYS   A O   1 
ATOM   2106 C CB  . LYS   A 1 288 ? 7.949   5.849   -3.258  1.00 30.66  ? 825  LYS   A CB  1 
ATOM   2107 C CG  . LYS   A 1 288 ? 6.983   6.504   -2.287  1.00 33.70  ? 825  LYS   A CG  1 
ATOM   2108 C CD  . LYS   A 1 288 ? 6.978   5.763   -0.960  1.00 35.74  ? 825  LYS   A CD  1 
ATOM   2109 C CE  . LYS   A 1 288 ? 8.387   5.671   -0.393  1.00 36.37  ? 825  LYS   A CE  1 
ATOM   2110 N NZ  . LYS   A 1 288 ? 8.444   4.858   0.852   1.00 38.02  ? 825  LYS   A NZ  1 
ATOM   2111 N N   . MET   A 1 289 ? 9.701   5.398   -5.989  1.00 26.89  ? 826  MET   A N   1 
ATOM   2112 C CA  . MET   A 1 289 ? 10.940  4.958   -6.616  1.00 26.98  ? 826  MET   A CA  1 
ATOM   2113 C C   . MET   A 1 289 ? 11.532  6.062   -7.481  1.00 25.81  ? 826  MET   A C   1 
ATOM   2114 O O   . MET   A 1 289 ? 12.735  6.329   -7.414  1.00 25.44  ? 826  MET   A O   1 
ATOM   2115 C CB  . MET   A 1 289 ? 10.685  3.693   -7.443  1.00 29.78  ? 826  MET   A CB  1 
ATOM   2116 C CG  . MET   A 1 289 ? 11.931  2.989   -7.985  1.00 32.46  ? 826  MET   A CG  1 
ATOM   2117 S SD  . MET   A 1 289 ? 12.958  2.230   -6.694  1.00 34.90  ? 826  MET   A SD  1 
ATOM   2118 C CE  . MET   A 1 289 ? 14.143  1.305   -7.665  1.00 33.85  ? 826  MET   A CE  1 
ATOM   2119 N N   . ILE   A 1 290 ? 10.701  6.729   -8.282  1.00 25.80  ? 827  ILE   A N   1 
ATOM   2120 C CA  . ILE   A 1 290 ? 11.191  7.819   -9.124  1.00 24.93  ? 827  ILE   A CA  1 
ATOM   2121 C C   . ILE   A 1 290 ? 11.719  8.965   -8.271  1.00 24.45  ? 827  ILE   A C   1 
ATOM   2122 O O   . ILE   A 1 290 ? 12.773  9.545   -8.562  1.00 23.28  ? 827  ILE   A O   1 
ATOM   2123 C CB  . ILE   A 1 290 ? 10.075  8.303   -10.069 1.00 25.73  ? 827  ILE   A CB  1 
ATOM   2124 C CG1 . ILE   A 1 290 ? 9.642   7.183   -11.016 1.00 26.50  ? 827  ILE   A CG1 1 
ATOM   2125 C CG2 . ILE   A 1 290 ? 10.521  9.538   -10.837 1.00 24.69  ? 827  ILE   A CG2 1 
ATOM   2126 C CD1 . ILE   A 1 290 ? 8.428   7.555   -11.839 1.00 28.78  ? 827  ILE   A CD1 1 
ATOM   2127 N N   . ARG   A 1 291 ? 10.989  9.319   -7.211  1.00 23.55  ? 828  ARG   A N   1 
ATOM   2128 C CA  . ARG   A 1 291 ? 11.363  10.484  -6.422  1.00 23.09  ? 828  ARG   A CA  1 
ATOM   2129 C C   . ARG   A 1 291 ? 12.610  10.219  -5.598  1.00 22.06  ? 828  ARG   A C   1 
ATOM   2130 O O   . ARG   A 1 291 ? 13.423  11.129  -5.398  1.00 22.39  ? 828  ARG   A O   1 
ATOM   2131 C CB  . ARG   A 1 291 ? 10.191  10.912  -5.538  1.00 25.28  ? 828  ARG   A CB  1 
ATOM   2132 C CG  . ARG   A 1 291 ? 9.058   11.522  -6.345  1.00 26.72  ? 828  ARG   A CG  1 
ATOM   2133 C CD  . ARG   A 1 291 ? 7.744   11.495  -5.607  1.00 30.68  ? 828  ARG   A CD  1 
ATOM   2134 N NE  . ARG   A 1 291 ? 6.675   11.993  -6.467  1.00 34.05  ? 828  ARG   A NE  1 
ATOM   2135 C CZ  . ARG   A 1 291 ? 5.385   11.971  -6.160  1.00 35.11  ? 828  ARG   A CZ  1 
ATOM   2136 N NH1 . ARG   A 1 291 ? 4.983   11.471  -5.000  1.00 35.55  ? 828  ARG   A NH1 1 
ATOM   2137 N NH2 . ARG   A 1 291 ? 4.496   12.448  -7.020  1.00 36.40  ? 828  ARG   A NH2 1 
ATOM   2138 N N   . HIS   A 1 292 ? 12.794  8.987   -5.124  1.00 21.26  ? 829  HIS   A N   1 
ATOM   2139 C CA  . HIS   A 1 292 ? 14.052  8.665   -4.467  1.00 20.99  ? 829  HIS   A CA  1 
ATOM   2140 C C   . HIS   A 1 292 ? 15.222  8.879   -5.416  1.00 20.16  ? 829  HIS   A C   1 
ATOM   2141 O O   . HIS   A 1 292 ? 16.242  9.464   -5.036  1.00 19.61  ? 829  HIS   A O   1 
ATOM   2142 C CB  . HIS   A 1 292 ? 14.053  7.228   -3.953  1.00 21.99  ? 829  HIS   A CB  1 
ATOM   2143 C CG  . HIS   A 1 292 ? 15.427  6.723   -3.651  1.00 21.93  ? 829  HIS   A CG  1 
ATOM   2144 N ND1 . HIS   A 1 292 ? 16.058  6.959   -2.449  1.00 22.33  ? 829  HIS   A ND1 1 
ATOM   2145 C CD2 . HIS   A 1 292 ? 16.317  6.048   -4.417  1.00 21.50  ? 829  HIS   A CD2 1 
ATOM   2146 C CE1 . HIS   A 1 292 ? 17.267  6.427   -2.478  1.00 22.34  ? 829  HIS   A CE1 1 
ATOM   2147 N NE2 . HIS   A 1 292 ? 17.450  5.871   -3.662  1.00 20.83  ? 829  HIS   A NE2 1 
ATOM   2148 N N   . THR   A 1 293 ? 15.082  8.414   -6.664  1.00 19.92  ? 830  THR   A N   1 
ATOM   2149 C CA  . THR   A 1 293 ? 16.134  8.564   -7.667  1.00 18.85  ? 830  THR   A CA  1 
ATOM   2150 C C   . THR   A 1 293 ? 16.421  10.031  -7.966  1.00 20.76  ? 830  THR   A C   1 
ATOM   2151 O O   . THR   A 1 293 ? 17.585  10.435  -8.070  1.00 22.45  ? 830  THR   A O   1 
ATOM   2152 C CB  . THR   A 1 293 ? 15.733  7.824   -8.945  1.00 19.25  ? 830  THR   A CB  1 
ATOM   2153 O OG1 . THR   A 1 293 ? 15.639  6.421   -8.666  1.00 19.36  ? 830  THR   A OG1 1 
ATOM   2154 C CG2 . THR   A 1 293 ? 16.749  8.053   -10.068 1.00 18.98  ? 830  THR   A CG2 1 
ATOM   2155 N N   . THR   A 1 294 ? 15.371  10.842  -8.115  1.00 21.75  ? 831  THR   A N   1 
ATOM   2156 C CA  . THR   A 1 294 ? 15.555  12.274  -8.324  1.00 21.53  ? 831  THR   A CA  1 
ATOM   2157 C C   . THR   A 1 294 ? 16.328  12.901  -7.170  1.00 21.93  ? 831  THR   A C   1 
ATOM   2158 O O   . THR   A 1 294 ? 17.310  13.621  -7.384  1.00 22.57  ? 831  THR   A O   1 
ATOM   2159 C CB  . THR   A 1 294 ? 14.193  12.961  -8.491  1.00 21.78  ? 831  THR   A CB  1 
ATOM   2160 O OG1 . THR   A 1 294 ? 13.511  12.418  -9.628  1.00 23.65  ? 831  THR   A OG1 1 
ATOM   2161 C CG2 . THR   A 1 294 ? 14.364  14.465  -8.675  1.00 20.14  ? 831  THR   A CG2 1 
ATOM   2162 N N   . ASN   A 1 295 ? 15.905  12.629  -5.932  1.00 21.31  ? 832  ASN   A N   1 
ATOM   2163 C CA  . ASN   A 1 295 ? 16.531  13.280  -4.787  1.00 21.26  ? 832  ASN   A CA  1 
ATOM   2164 C C   . ASN   A 1 295 ? 17.974  12.839  -4.612  1.00 18.47  ? 832  ASN   A C   1 
ATOM   2165 O O   . ASN   A 1 295 ? 18.845  13.660  -4.305  1.00 17.88  ? 832  ASN   A O   1 
ATOM   2166 C CB  . ASN   A 1 295 ? 15.737  12.994  -3.520  1.00 26.61  ? 832  ASN   A CB  1 
ATOM   2167 C CG  . ASN   A 1 295 ? 14.634  13.988  -3.307  1.00 32.22  ? 832  ASN   A CG  1 
ATOM   2168 O OD1 . ASN   A 1 295 ? 14.817  15.188  -3.511  1.00 32.73  ? 832  ASN   A OD1 1 
ATOM   2169 N ND2 . ASN   A 1 295 ? 13.472  13.501  -2.912  1.00 36.53  ? 832  ASN   A ND2 1 
ATOM   2170 N N   . LEU   A 1 296 ? 18.244  11.547  -4.806  1.00 17.60  ? 833  LEU   A N   1 
ATOM   2171 C CA  . LEU   A 1 296 ? 19.592  11.041  -4.602  1.00 17.11  ? 833  LEU   A CA  1 
ATOM   2172 C C   . LEU   A 1 296 ? 20.541  11.553  -5.681  1.00 18.36  ? 833  LEU   A C   1 
ATOM   2173 O O   . LEU   A 1 296 ? 21.698  11.881  -5.391  1.00 19.09  ? 833  LEU   A O   1 
ATOM   2174 C CB  . LEU   A 1 296 ? 19.575  9.515   -4.559  1.00 18.16  ? 833  LEU   A CB  1 
ATOM   2175 C CG  . LEU   A 1 296 ? 20.914  8.906   -4.139  1.00 18.73  ? 833  LEU   A CG  1 
ATOM   2176 C CD1 . LEU   A 1 296 ? 21.266  9.307   -2.695  1.00 17.13  ? 833  LEU   A CD1 1 
ATOM   2177 C CD2 . LEU   A 1 296 ? 20.917  7.390   -4.315  1.00 19.74  ? 833  LEU   A CD2 1 
ATOM   2178 N N   . THR   A 1 297 ? 20.062  11.664  -6.923  1.00 18.35  ? 834  THR   A N   1 
ATOM   2179 C CA  . THR   A 1 297 ? 20.899  12.192  -8.000  1.00 19.00  ? 834  THR   A CA  1 
ATOM   2180 C C   . THR   A 1 297 ? 21.214  13.671  -7.782  1.00 19.93  ? 834  THR   A C   1 
ATOM   2181 O O   . THR   A 1 297 ? 22.364  14.105  -7.944  1.00 18.86  ? 834  THR   A O   1 
ATOM   2182 C CB  . THR   A 1 297 ? 20.206  11.982  -9.348  1.00 20.56  ? 834  THR   A CB  1 
ATOM   2183 O OG1 . THR   A 1 297 ? 19.926  10.591  -9.536  1.00 16.08  ? 834  THR   A OG1 1 
ATOM   2184 C CG2 . THR   A 1 297 ? 21.080  12.473  -10.490 1.00 16.57  ? 834  THR   A CG2 1 
ATOM   2185 N N   . LEU   A 1 298 ? 20.201  14.467  -7.430  1.00 20.51  ? 835  LEU   A N   1 
ATOM   2186 C CA  . LEU   A 1 298 ? 20.462  15.858  -7.085  1.00 20.12  ? 835  LEU   A CA  1 
ATOM   2187 C C   . LEU   A 1 298 ? 21.360  15.965  -5.856  1.00 20.59  ? 835  LEU   A C   1 
ATOM   2188 O O   . LEU   A 1 298 ? 22.124  16.925  -5.734  1.00 20.92  ? 835  LEU   A O   1 
ATOM   2189 C CB  . LEU   A 1 298 ? 19.142  16.605  -6.862  1.00 21.76  ? 835  LEU   A CB  1 
ATOM   2190 C CG  . LEU   A 1 298 ? 18.328  16.998  -8.108  1.00 24.07  ? 835  LEU   A CG  1 
ATOM   2191 C CD1 . LEU   A 1 298 ? 17.078  17.795  -7.753  1.00 23.58  ? 835  LEU   A CD1 1 
ATOM   2192 C CD2 . LEU   A 1 298 ? 19.184  17.784  -9.101  1.00 25.28  ? 835  LEU   A CD2 1 
ATOM   2193 N N   . TRP   A 1 299 ? 21.295  14.991  -4.942  1.00 21.64  ? 836  TRP   A N   1 
ATOM   2194 C CA  . TRP   A 1 299 ? 22.113  15.058  -3.734  1.00 23.13  ? 836  TRP   A CA  1 
ATOM   2195 C C   . TRP   A 1 299 ? 23.595  14.873  -4.052  1.00 23.60  ? 836  TRP   A C   1 
ATOM   2196 O O   . TRP   A 1 299 ? 24.445  15.605  -3.529  1.00 16.66  ? 836  TRP   A O   1 
ATOM   2197 C CB  . TRP   A 1 299 ? 21.646  14.013  -2.725  1.00 16.89  ? 836  TRP   A CB  1 
ATOM   2198 C CG  . TRP   A 1 299 ? 22.410  14.052  -1.446  1.00 19.22  ? 836  TRP   A CG  1 
ATOM   2199 C CD1 . TRP   A 1 299 ? 22.373  15.034  -0.499  1.00 21.58  ? 836  TRP   A CD1 1 
ATOM   2200 C CD2 . TRP   A 1 299 ? 23.319  13.057  -0.957  1.00 19.11  ? 836  TRP   A CD2 1 
ATOM   2201 N NE1 . TRP   A 1 299 ? 23.209  14.716  0.547   1.00 22.13  ? 836  TRP   A NE1 1 
ATOM   2202 C CE2 . TRP   A 1 299 ? 23.802  13.508  0.288   1.00 20.68  ? 836  TRP   A CE2 1 
ATOM   2203 C CE3 . TRP   A 1 299 ? 23.773  11.831  -1.452  1.00 19.27  ? 836  TRP   A CE3 1 
ATOM   2204 C CZ2 . TRP   A 1 299 ? 24.717  12.776  1.044   1.00 21.16  ? 836  TRP   A CZ2 1 
ATOM   2205 C CZ3 . TRP   A 1 299 ? 24.678  11.103  -0.698  1.00 20.56  ? 836  TRP   A CZ3 1 
ATOM   2206 C CH2 . TRP   A 1 299 ? 25.139  11.578  0.536   1.00 21.19  ? 836  TRP   A CH2 1 
ATOM   2207 N N   . PHE   A 1 300 ? 23.927  13.887  -4.897  1.00 21.56  ? 837  PHE   A N   1 
ATOM   2208 C CA  . PHE   A 1 300 ? 25.317  13.703  -5.311  1.00 15.49  ? 837  PHE   A CA  1 
ATOM   2209 C C   . PHE   A 1 300 ? 25.845  14.950  -6.014  1.00 22.79  ? 837  PHE   A C   1 
ATOM   2210 O O   . PHE   A 1 300 ? 26.948  15.427  -5.714  1.00 15.94  ? 837  PHE   A O   1 
ATOM   2211 C CB  . PHE   A 1 300 ? 25.447  12.483  -6.225  1.00 16.31  ? 837  PHE   A CB  1 
ATOM   2212 C CG  . PHE   A 1 300 ? 25.336  11.162  -5.510  1.00 14.88  ? 837  PHE   A CG  1 
ATOM   2213 C CD1 . PHE   A 1 300 ? 26.225  10.823  -4.505  1.00 18.91  ? 837  PHE   A CD1 1 
ATOM   2214 C CD2 . PHE   A 1 300 ? 24.362  10.242  -5.870  1.00 14.80  ? 837  PHE   A CD2 1 
ATOM   2215 C CE1 . PHE   A 1 300 ? 26.130  9.599   -3.849  1.00 17.02  ? 837  PHE   A CE1 1 
ATOM   2216 C CE2 . PHE   A 1 300 ? 24.261  9.015   -5.223  1.00 15.80  ? 837  PHE   A CE2 1 
ATOM   2217 C CZ  . PHE   A 1 300 ? 25.146  8.694   -4.208  1.00 15.87  ? 837  PHE   A CZ  1 
ATOM   2218 N N   . GLU   A 1 301 ? 25.065  15.497  -6.954  1.00 21.17  ? 838  GLU   A N   1 
ATOM   2219 C CA  . GLU   A 1 301 ? 25.453  16.744  -7.607  1.00 20.51  ? 838  GLU   A CA  1 
ATOM   2220 C C   . GLU   A 1 301 ? 25.717  17.837  -6.579  1.00 21.33  ? 838  GLU   A C   1 
ATOM   2221 O O   . GLU   A 1 301 ? 26.740  18.527  -6.640  1.00 17.47  ? 838  GLU   A O   1 
ATOM   2222 C CB  . GLU   A 1 301 ? 24.370  17.188  -8.593  1.00 21.94  ? 838  GLU   A CB  1 
ATOM   2223 C CG  . GLU   A 1 301 ? 24.147  16.212  -9.736  1.00 24.96  ? 838  GLU   A CG  1 
ATOM   2224 C CD  . GLU   A 1 301 ? 22.922  16.537  -10.578 1.00 26.36  ? 838  GLU   A CD  1 
ATOM   2225 O OE1 . GLU   A 1 301 ? 22.575  17.736  -10.696 1.00 26.71  ? 838  GLU   A OE1 1 
ATOM   2226 O OE2 . GLU   A 1 301 ? 22.317  15.584  -11.123 1.00 25.87  ? 838  GLU   A OE2 1 
ATOM   2227 N N   . LYS   A 1 302 ? 24.800  18.004  -5.623  1.00 17.53  ? 839  LYS   A N   1 
ATOM   2228 C CA  . LYS   A 1 302 ? 24.954  19.035  -4.602  1.00 18.28  ? 839  LYS   A CA  1 
ATOM   2229 C C   . LYS   A 1 302 ? 26.276  18.877  -3.851  1.00 18.04  ? 839  LYS   A C   1 
ATOM   2230 O O   . LYS   A 1 302 ? 26.999  19.856  -3.631  1.00 18.61  ? 839  LYS   A O   1 
ATOM   2231 C CB  . LYS   A 1 302 ? 23.761  18.978  -3.644  1.00 18.77  ? 839  LYS   A CB  1 
ATOM   2232 C CG  . LYS   A 1 302 ? 23.717  20.071  -2.585  1.00 19.91  ? 839  LYS   A CG  1 
ATOM   2233 C CD  . LYS   A 1 302 ? 22.406  19.991  -1.797  1.00 20.64  ? 839  LYS   A CD  1 
ATOM   2234 C CE  . LYS   A 1 302 ? 22.328  21.048  -0.716  1.00 22.07  ? 839  LYS   A CE  1 
ATOM   2235 N NZ  . LYS   A 1 302 ? 23.428  20.864  0.259   1.00 22.01  ? 839  LYS   A NZ  1 
ATOM   2236 N N   . CYS   A 1 303 ? 26.625  17.640  -3.477  1.00 17.34  ? 840  CYS   A N   1 
ATOM   2237 C CA  . CYS   A 1 303 ? 27.824  17.414  -2.670  1.00 20.50  ? 840  CYS   A CA  1 
ATOM   2238 C C   . CYS   A 1 303 ? 29.097  17.773  -3.434  1.00 19.42  ? 840  CYS   A C   1 
ATOM   2239 O O   . CYS   A 1 303 ? 30.079  18.234  -2.836  1.00 17.63  ? 840  CYS   A O   1 
ATOM   2240 C CB  . CYS   A 1 303 ? 27.868  15.957  -2.198  1.00 16.81  ? 840  CYS   A CB  1 
ATOM   2241 S SG  . CYS   A 1 303 ? 26.540  15.465  -1.032  1.00 17.17  ? 840  CYS   A SG  1 
ATOM   2242 N N   . ILE   A 1 304 ? 29.093  17.586  -4.754  1.00 20.17  ? 841  ILE   A N   1 
ATOM   2243 C CA  . ILE   A 1 304 ? 30.279  17.879  -5.554  1.00 20.62  ? 841  ILE   A CA  1 
ATOM   2244 C C   . ILE   A 1 304 ? 30.457  19.381  -5.717  1.00 21.19  ? 841  ILE   A C   1 
ATOM   2245 O O   . ILE   A 1 304 ? 31.540  19.926  -5.470  1.00 22.01  ? 841  ILE   A O   1 
ATOM   2246 C CB  . ILE   A 1 304 ? 30.191  17.183  -6.925  1.00 20.85  ? 841  ILE   A CB  1 
ATOM   2247 C CG1 . ILE   A 1 304 ? 30.197  15.663  -6.754  1.00 16.10  ? 841  ILE   A CG1 1 
ATOM   2248 C CG2 . ILE   A 1 304 ? 31.318  17.654  -7.842  1.00 17.10  ? 841  ILE   A CG2 1 
ATOM   2249 C CD1 . ILE   A 1 304 ? 29.642  14.929  -7.941  1.00 15.95  ? 841  ILE   A CD1 1 
ATOM   2250 N N   A VAL   A 1 305 ? 29.389  20.069  -6.122  0.60 20.86  ? 842  VAL   A N   1 
ATOM   2251 N N   B VAL   A 1 305 ? 29.406  20.079  -6.148  0.40 20.98  ? 842  VAL   A N   1 
ATOM   2252 C CA  A VAL   A 1 305 ? 29.504  21.475  -6.490  0.60 19.13  ? 842  VAL   A CA  1 
ATOM   2253 C CA  B VAL   A 1 305 ? 29.590  21.488  -6.485  0.40 19.13  ? 842  VAL   A CA  1 
ATOM   2254 C C   A VAL   A 1 305 ? 29.647  22.345  -5.248  0.60 22.11  ? 842  VAL   A C   1 
ATOM   2255 C C   B VAL   A 1 305 ? 29.665  22.357  -5.233  0.40 22.21  ? 842  VAL   A C   1 
ATOM   2256 O O   A VAL   A 1 305 ? 30.413  23.316  -5.239  0.60 20.54  ? 842  VAL   A O   1 
ATOM   2257 O O   B VAL   A 1 305 ? 30.398  23.352  -5.211  0.40 25.05  ? 842  VAL   A O   1 
ATOM   2258 C CB  A VAL   A 1 305 ? 28.298  21.888  -7.357  0.60 46.86  ? 842  VAL   A CB  1 
ATOM   2259 C CB  B VAL   A 1 305 ? 28.485  21.971  -7.443  0.40 47.35  ? 842  VAL   A CB  1 
ATOM   2260 C CG1 A VAL   A 1 305 ? 28.531  23.240  -7.981  0.60 20.73  ? 842  VAL   A CG1 1 
ATOM   2261 C CG1 B VAL   A 1 305 ? 28.570  21.223  -8.764  0.40 19.27  ? 842  VAL   A CG1 1 
ATOM   2262 C CG2 A VAL   A 1 305 ? 28.059  20.853  -8.440  0.60 19.00  ? 842  VAL   A CG2 1 
ATOM   2263 C CG2 B VAL   A 1 305 ? 27.123  21.796  -6.816  0.40 19.68  ? 842  VAL   A CG2 1 
ATOM   2264 N N   . GLU   A 1 306 ? 28.938  22.002  -4.174  1.00 23.08  ? 843  GLU   A N   1 
ATOM   2265 C CA  . GLU   A 1 306 ? 29.000  22.776  -2.941  1.00 25.07  ? 843  GLU   A CA  1 
ATOM   2266 C C   . GLU   A 1 306 ? 30.288  22.554  -2.155  1.00 25.23  ? 843  GLU   A C   1 
ATOM   2267 O O   . GLU   A 1 306 ? 30.479  23.200  -1.119  1.00 27.01  ? 843  GLU   A O   1 
ATOM   2268 C CB  . GLU   A 1 306 ? 27.792  22.459  -2.064  1.00 25.54  ? 843  GLU   A CB  1 
ATOM   2269 C CG  . GLU   A 1 306 ? 26.481  22.948  -2.650  1.00 27.85  ? 843  GLU   A CG  1 
ATOM   2270 C CD  . GLU   A 1 306 ? 25.392  23.063  -1.601  1.00 30.49  ? 843  GLU   A CD  1 
ATOM   2271 O OE1 . GLU   A 1 306 ? 25.554  22.471  -0.514  1.00 31.00  ? 843  GLU   A OE1 1 
ATOM   2272 O OE2 . GLU   A 1 306 ? 24.382  23.748  -1.860  1.00 31.56  ? 843  GLU   A OE2 1 
ATOM   2273 N N   . ALA   A 1 307 ? 31.165  21.662  -2.607  1.00 24.03  ? 844  ALA   A N   1 
ATOM   2274 C CA  . ALA   A 1 307 ? 32.486  21.491  -2.008  1.00 24.59  ? 844  ALA   A CA  1 
ATOM   2275 C C   . ALA   A 1 307 ? 33.421  22.428  -2.754  1.00 26.13  ? 844  ALA   A C   1 
ATOM   2276 O O   . ALA   A 1 307 ? 33.973  22.085  -3.801  1.00 26.48  ? 844  ALA   A O   1 
ATOM   2277 C CB  . ALA   A 1 307 ? 32.944  20.041  -2.093  1.00 23.92  ? 844  ALA   A CB  1 
ATOM   2278 N N   . GLU   A 1 308 ? 33.596  23.633  -2.207  1.00 26.75  ? 845  GLU   A N   1 
ATOM   2279 C CA  . GLU   A 1 308 ? 34.259  24.693  -2.957  1.00 27.36  ? 845  GLU   A CA  1 
ATOM   2280 C C   . GLU   A 1 308 ? 35.775  24.525  -2.954  1.00 27.27  ? 845  GLU   A C   1 
ATOM   2281 O O   . GLU   A 1 308 ? 36.422  24.742  -3.986  1.00 24.96  ? 845  GLU   A O   1 
ATOM   2282 C CB  . GLU   A 1 308 ? 33.829  26.053  -2.405  1.00 29.71  ? 845  GLU   A CB  1 
ATOM   2283 C CG  . GLU   A 1 308 ? 32.318  26.284  -2.573  1.00 30.53  ? 845  GLU   A CG  1 
ATOM   2284 C CD  . GLU   A 1 308 ? 31.816  27.586  -1.975  1.00 32.51  ? 845  GLU   A CD  1 
ATOM   2285 O OE1 . GLU   A 1 308 ? 32.646  28.421  -1.561  1.00 34.13  ? 845  GLU   A OE1 1 
ATOM   2286 O OE2 . GLU   A 1 308 ? 30.583  27.777  -1.924  1.00 32.91  ? 845  GLU   A OE2 1 
ATOM   2287 N N   . ASN   A 1 309 ? 36.353  24.106  -1.827  1.00 28.45  ? 846  ASN   A N   1 
ATOM   2288 C CA  . ASN   A 1 309 ? 37.781  23.808  -1.784  1.00 27.69  ? 846  ASN   A CA  1 
ATOM   2289 C C   . ASN   A 1 309 ? 38.112  22.703  -2.777  1.00 24.36  ? 846  ASN   A C   1 
ATOM   2290 O O   . ASN   A 1 309 ? 37.437  21.672  -2.822  1.00 23.79  ? 846  ASN   A O   1 
ATOM   2291 C CB  . ASN   A 1 309 ? 38.204  23.394  -0.374  1.00 28.84  ? 846  ASN   A CB  1 
ATOM   2292 C CG  . ASN   A 1 309 ? 39.700  23.114  -0.272  1.00 31.05  ? 846  ASN   A CG  1 
ATOM   2293 O OD1 . ASN   A 1 309 ? 40.146  21.970  -0.417  1.00 31.21  ? 846  ASN   A OD1 1 
ATOM   2294 N ND2 . ASN   A 1 309 ? 40.482  24.162  -0.020  1.00 31.37  ? 846  ASN   A ND2 1 
ATOM   2295 N N   . PHE   A 1 310 ? 39.166  22.920  -3.567  1.00 23.63  ? 847  PHE   A N   1 
ATOM   2296 C CA  . PHE   A 1 310 ? 39.467  22.029  -4.685  1.00 23.07  ? 847  PHE   A CA  1 
ATOM   2297 C C   . PHE   A 1 310 ? 39.834  20.629  -4.204  1.00 23.41  ? 847  PHE   A C   1 
ATOM   2298 O O   . PHE   A 1 310 ? 39.294  19.630  -4.700  1.00 22.74  ? 847  PHE   A O   1 
ATOM   2299 C CB  . PHE   A 1 310 ? 40.591  22.628  -5.535  1.00 22.92  ? 847  PHE   A CB  1 
ATOM   2300 C CG  . PHE   A 1 310 ? 41.030  21.747  -6.671  1.00 23.42  ? 847  PHE   A CG  1 
ATOM   2301 C CD1 . PHE   A 1 310 ? 40.101  21.199  -7.538  1.00 21.23  ? 847  PHE   A CD1 1 
ATOM   2302 C CD2 . PHE   A 1 310 ? 42.377  21.481  -6.882  1.00 24.36  ? 847  PHE   A CD2 1 
ATOM   2303 C CE1 . PHE   A 1 310 ? 40.497  20.391  -8.587  1.00 21.29  ? 847  PHE   A CE1 1 
ATOM   2304 C CE2 . PHE   A 1 310 ? 42.783  20.674  -7.935  1.00 25.10  ? 847  PHE   A CE2 1 
ATOM   2305 C CZ  . PHE   A 1 310 ? 41.840  20.124  -8.787  1.00 24.76  ? 847  PHE   A CZ  1 
ATOM   2306 N N   . GLU   A 1 311 ? 40.760  20.534  -3.244  1.00 24.26  ? 848  GLU   A N   1 
ATOM   2307 C CA  . GLU   A 1 311 ? 41.165  19.225  -2.744  1.00 26.62  ? 848  GLU   A CA  1 
ATOM   2308 C C   . GLU   A 1 311 ? 39.996  18.494  -2.098  1.00 28.32  ? 848  GLU   A C   1 
ATOM   2309 O O   . GLU   A 1 311 ? 39.843  17.279  -2.268  1.00 28.41  ? 848  GLU   A O   1 
ATOM   2310 C CB  . GLU   A 1 311 ? 42.322  19.373  -1.757  1.00 29.01  ? 848  GLU   A CB  1 
ATOM   2311 C CG  . GLU   A 1 311 ? 43.653  19.734  -2.409  1.00 32.02  ? 848  GLU   A CG  1 
ATOM   2312 C CD  . GLU   A 1 311 ? 43.692  21.174  -2.901  1.00 34.35  ? 848  GLU   A CD  1 
ATOM   2313 O OE1 . GLU   A 1 311 ? 42.880  21.987  -2.416  1.00 35.22  ? 848  GLU   A OE1 1 
ATOM   2314 O OE2 . GLU   A 1 311 ? 44.526  21.492  -3.775  1.00 35.33  ? 848  GLU   A OE2 1 
ATOM   2315 N N   . GLU   A 1 312 ? 39.160  19.217  -1.355  1.00 31.13  ? 849  GLU   A N   1 
ATOM   2316 C CA  . GLU   A 1 312 ? 37.990  18.595  -0.749  1.00 32.95  ? 849  GLU   A CA  1 
ATOM   2317 C C   . GLU   A 1 312 ? 37.029  18.082  -1.814  1.00 27.83  ? 849  GLU   A C   1 
ATOM   2318 O O   . GLU   A 1 312 ? 36.420  17.017  -1.647  1.00 26.74  ? 849  GLU   A O   1 
ATOM   2319 C CB  . GLU   A 1 312 ? 37.302  19.597  0.180   1.00 39.64  ? 849  GLU   A CB  1 
ATOM   2320 C CG  . GLU   A 1 312 ? 36.005  19.120  0.815   1.00 45.02  ? 849  GLU   A CG  1 
ATOM   2321 C CD  . GLU   A 1 312 ? 35.491  20.089  1.861   1.00 50.56  ? 849  GLU   A CD  1 
ATOM   2322 O OE1 . GLU   A 1 312 ? 36.150  20.226  2.916   1.00 52.59  ? 849  GLU   A OE1 1 
ATOM   2323 O OE2 . GLU   A 1 312 ? 34.443  20.729  1.616   1.00 52.17  ? 849  GLU   A OE2 1 
ATOM   2324 N N   . ARG   A 1 313 ? 36.899  18.811  -2.926  1.00 24.03  ? 850  ARG   A N   1 
ATOM   2325 C CA  . ARG   A 1 313 ? 35.964  18.406  -3.969  1.00 21.53  ? 850  ARG   A CA  1 
ATOM   2326 C C   . ARG   A 1 313 ? 36.432  17.132  -4.667  1.00 20.88  ? 850  ARG   A C   1 
ATOM   2327 O O   . ARG   A 1 313 ? 35.626  16.228  -4.920  1.00 20.44  ? 850  ARG   A O   1 
ATOM   2328 C CB  . ARG   A 1 313 ? 35.768  19.545  -4.969  1.00 20.07  ? 850  ARG   A CB  1 
ATOM   2329 C CG  . ARG   A 1 313 ? 34.786  19.207  -6.070  1.00 18.82  ? 850  ARG   A CG  1 
ATOM   2330 C CD  . ARG   A 1 313 ? 34.386  20.417  -6.881  1.00 19.48  ? 850  ARG   A CD  1 
ATOM   2331 N NE  . ARG   A 1 313 ? 35.502  21.038  -7.589  1.00 20.59  ? 850  ARG   A NE  1 
ATOM   2332 C CZ  . ARG   A 1 313 ? 36.142  22.123  -7.164  1.00 21.59  ? 850  ARG   A CZ  1 
ATOM   2333 N NH1 . ARG   A 1 313 ? 35.785  22.702  -6.020  1.00 20.46  ? 850  ARG   A NH1 1 
ATOM   2334 N NH2 . ARG   A 1 313 ? 37.135  22.629  -7.882  1.00 21.71  ? 850  ARG   A NH2 1 
ATOM   2335 N N   . VAL   A 1 314 ? 37.730  17.032  -4.969  1.00 21.76  ? 851  VAL   A N   1 
ATOM   2336 C CA  . VAL   A 1 314 ? 38.265  15.810  -5.565  1.00 18.52  ? 851  VAL   A CA  1 
ATOM   2337 C C   . VAL   A 1 314 ? 38.031  14.621  -4.637  1.00 19.95  ? 851  VAL   A C   1 
ATOM   2338 O O   . VAL   A 1 314 ? 37.733  13.507  -5.091  1.00 18.05  ? 851  VAL   A O   1 
ATOM   2339 C CB  . VAL   A 1 314 ? 39.758  15.998  -5.903  1.00 19.34  ? 851  VAL   A CB  1 
ATOM   2340 C CG1 . VAL   A 1 314 ? 40.401  14.687  -6.333  1.00 19.63  ? 851  VAL   A CG1 1 
ATOM   2341 C CG2 . VAL   A 1 314 ? 39.923  17.039  -6.997  1.00 19.69  ? 851  VAL   A CG2 1 
ATOM   2342 N N   . ALA   A 1 315 ? 38.129  14.843  -3.322  1.00 20.18  ? 852  ALA   A N   1 
ATOM   2343 C CA  . ALA   A 1 315 ? 37.881  13.763  -2.369  1.00 22.07  ? 852  ALA   A CA  1 
ATOM   2344 C C   . ALA   A 1 315 ? 36.412  13.353  -2.357  1.00 21.36  ? 852  ALA   A C   1 
ATOM   2345 O O   . ALA   A 1 315 ? 36.099  12.168  -2.179  1.00 21.36  ? 852  ALA   A O   1 
ATOM   2346 C CB  . ALA   A 1 315 ? 38.329  14.177  -0.967  1.00 23.69  ? 852  ALA   A CB  1 
ATOM   2347 N N   . VAL   A 1 316 ? 35.501  14.318  -2.527  1.00 20.51  ? 853  VAL   A N   1 
ATOM   2348 C CA  . VAL   A 1 316 ? 34.077  14.003  -2.606  1.00 18.91  ? 853  VAL   A CA  1 
ATOM   2349 C C   . VAL   A 1 316 ? 33.793  13.142  -3.831  1.00 18.81  ? 853  VAL   A C   1 
ATOM   2350 O O   . VAL   A 1 316 ? 33.138  12.095  -3.742  1.00 17.14  ? 853  VAL   A O   1 
ATOM   2351 C CB  . VAL   A 1 316 ? 33.241  15.296  -2.622  1.00 19.19  ? 853  VAL   A CB  1 
ATOM   2352 C CG1 . VAL   A 1 316 ? 31.821  15.007  -3.079  1.00 18.37  ? 853  VAL   A CG1 1 
ATOM   2353 C CG2 . VAL   A 1 316 ? 33.238  15.950  -1.246  1.00 19.59  ? 853  VAL   A CG2 1 
ATOM   2354 N N   . LEU   A 1 317 ? 34.282  13.573  -4.996  1.00 20.86  ? 854  LEU   A N   1 
ATOM   2355 C CA  . LEU   A 1 317 ? 34.074  12.803  -6.217  1.00 20.26  ? 854  LEU   A CA  1 
ATOM   2356 C C   . LEU   A 1 317 ? 34.660  11.404  -6.088  1.00 21.92  ? 854  LEU   A C   1 
ATOM   2357 O O   . LEU   A 1 317 ? 34.046  10.424  -6.526  1.00 22.07  ? 854  LEU   A O   1 
ATOM   2358 C CB  . LEU   A 1 317 ? 34.685  13.539  -7.407  1.00 18.24  ? 854  LEU   A CB  1 
ATOM   2359 C CG  . LEU   A 1 317 ? 34.452  12.934  -8.790  1.00 18.35  ? 854  LEU   A CG  1 
ATOM   2360 C CD1 . LEU   A 1 317 ? 32.974  12.633  -9.025  1.00 17.95  ? 854  LEU   A CD1 1 
ATOM   2361 C CD2 . LEU   A 1 317 ? 34.976  13.878  -9.860  1.00 19.56  ? 854  LEU   A CD2 1 
ATOM   2362 N N   . SER   A 1 318 ? 35.841  11.290  -5.474  1.00 22.35  ? 855  SER   A N   1 
ATOM   2363 C CA  . SER   A 1 318 ? 36.456  9.978   -5.318  1.00 23.42  ? 855  SER   A CA  1 
ATOM   2364 C C   . SER   A 1 318 ? 35.659  9.112   -4.352  1.00 22.37  ? 855  SER   A C   1 
ATOM   2365 O O   . SER   A 1 318 ? 35.566  7.893   -4.535  1.00 22.46  ? 855  SER   A O   1 
ATOM   2366 C CB  . SER   A 1 318 ? 37.899  10.131  -4.845  1.00 25.44  ? 855  SER   A CB  1 
ATOM   2367 O OG  . SER   A 1 318 ? 38.512  11.230  -5.489  1.00 28.43  ? 855  SER   A OG  1 
ATOM   2368 N N   . ARG   A 1 319 ? 35.083  9.725   -3.315  1.00 20.90  ? 856  ARG   A N   1 
ATOM   2369 C CA  . ARG   A 1 319 ? 34.210  8.983   -2.414  1.00 20.74  ? 856  ARG   A CA  1 
ATOM   2370 C C   . ARG   A 1 319 ? 33.006  8.431   -3.164  1.00 16.58  ? 856  ARG   A C   1 
ATOM   2371 O O   . ARG   A 1 319 ? 32.631  7.269   -2.985  1.00 16.73  ? 856  ARG   A O   1 
ATOM   2372 C CB  . ARG   A 1 319 ? 33.760  9.883   -1.265  1.00 20.29  ? 856  ARG   A CB  1 
ATOM   2373 C CG  . ARG   A 1 319 ? 33.125  9.144   -0.101  1.00 20.18  ? 856  ARG   A CG  1 
ATOM   2374 C CD  . ARG   A 1 319 ? 34.154  8.277   0.637   1.00 22.15  ? 856  ARG   A CD  1 
ATOM   2375 N NE  . ARG   A 1 319 ? 35.334  9.037   1.053   1.00 22.39  ? 856  ARG   A NE  1 
ATOM   2376 C CZ  . ARG   A 1 319 ? 35.488  9.588   2.254   1.00 23.77  ? 856  ARG   A CZ  1 
ATOM   2377 N NH1 . ARG   A 1 319 ? 34.536  9.467   3.171   1.00 24.48  ? 856  ARG   A NH1 1 
ATOM   2378 N NH2 . ARG   A 1 319 ? 36.596  10.259  2.542   1.00 22.47  ? 856  ARG   A NH2 1 
ATOM   2379 N N   . ILE   A 1 320 ? 32.404  9.250   -4.028  1.00 19.25  ? 857  ILE   A N   1 
ATOM   2380 C CA  . ILE   A 1 320 ? 31.222  8.830   -4.777  1.00 19.22  ? 857  ILE   A CA  1 
ATOM   2381 C C   . ILE   A 1 320 ? 31.559  7.666   -5.700  1.00 19.51  ? 857  ILE   A C   1 
ATOM   2382 O O   . ILE   A 1 320 ? 30.749  6.748   -5.885  1.00 15.87  ? 857  ILE   A O   1 
ATOM   2383 C CB  . ILE   A 1 320 ? 30.637  10.031  -5.548  1.00 15.35  ? 857  ILE   A CB  1 
ATOM   2384 C CG1 . ILE   A 1 320 ? 30.024  11.035  -4.564  1.00 15.29  ? 857  ILE   A CG1 1 
ATOM   2385 C CG2 . ILE   A 1 320 ? 29.626  9.577   -6.582  1.00 15.16  ? 857  ILE   A CG2 1 
ATOM   2386 C CD1 . ILE   A 1 320 ? 29.592  12.337  -5.195  1.00 19.48  ? 857  ILE   A CD1 1 
ATOM   2387 N N   . ILE   A 1 321 ? 32.764  7.674   -6.278  1.00 16.39  ? 858  ILE   A N   1 
ATOM   2388 C CA  . ILE   A 1 321 ? 33.191  6.553   -7.109  1.00 19.76  ? 858  ILE   A CA  1 
ATOM   2389 C C   . ILE   A 1 321 ? 33.394  5.302   -6.258  1.00 17.45  ? 858  ILE   A C   1 
ATOM   2390 O O   . ILE   A 1 321 ? 33.116  4.182   -6.701  1.00 24.41  ? 858  ILE   A O   1 
ATOM   2391 C CB  . ILE   A 1 321 ? 34.463  6.921   -7.894  1.00 24.43  ? 858  ILE   A CB  1 
ATOM   2392 C CG1 . ILE   A 1 321 ? 34.229  8.174   -8.745  1.00 20.18  ? 858  ILE   A CG1 1 
ATOM   2393 C CG2 . ILE   A 1 321 ? 34.902  5.755   -8.770  1.00 18.50  ? 858  ILE   A CG2 1 
ATOM   2394 C CD1 . ILE   A 1 321 ? 35.448  8.618   -9.557  1.00 19.59  ? 858  ILE   A CD1 1 
ATOM   2395 N N   . GLU   A 1 322 ? 33.883  5.469   -5.028  1.00 17.61  ? 859  GLU   A N   1 
ATOM   2396 C CA  . GLU   A 1 322 ? 33.979  4.336   -4.114  1.00 18.23  ? 859  GLU   A CA  1 
ATOM   2397 C C   . GLU   A 1 322 ? 32.599  3.777   -3.786  1.00 22.53  ? 859  GLU   A C   1 
ATOM   2398 O O   . GLU   A 1 322 ? 32.423  2.557   -3.676  1.00 22.56  ? 859  GLU   A O   1 
ATOM   2399 C CB  . GLU   A 1 322 ? 34.711  4.748   -2.837  1.00 19.24  ? 859  GLU   A CB  1 
ATOM   2400 C CG  . GLU   A 1 322 ? 36.177  5.107   -3.042  1.00 19.30  ? 859  GLU   A CG  1 
ATOM   2401 C CD  . GLU   A 1 322 ? 36.882  5.469   -1.743  1.00 27.56  ? 859  GLU   A CD  1 
ATOM   2402 O OE1 . GLU   A 1 322 ? 36.192  5.833   -0.772  1.00 34.43  ? 859  GLU   A OE1 1 
ATOM   2403 O OE2 . GLU   A 1 322 ? 38.124  5.385   -1.684  1.00 35.16  ? 859  GLU   A OE2 1 
ATOM   2404 N N   . ILE   A 1 323 ? 31.604  4.652   -3.632  1.00 17.05  ? 860  ILE   A N   1 
ATOM   2405 C CA  . ILE   A 1 323 ? 30.239  4.179   -3.432  1.00 21.22  ? 860  ILE   A CA  1 
ATOM   2406 C C   . ILE   A 1 323 ? 29.742  3.457   -4.680  1.00 22.54  ? 860  ILE   A C   1 
ATOM   2407 O O   . ILE   A 1 323 ? 29.030  2.446   -4.593  1.00 23.31  ? 860  ILE   A O   1 
ATOM   2408 C CB  . ILE   A 1 323 ? 29.325  5.355   -3.050  1.00 18.38  ? 860  ILE   A CB  1 
ATOM   2409 C CG1 . ILE   A 1 323 ? 29.791  5.975   -1.734  1.00 18.01  ? 860  ILE   A CG1 1 
ATOM   2410 C CG2 . ILE   A 1 323 ? 27.879  4.903   -2.951  1.00 18.34  ? 860  ILE   A CG2 1 
ATOM   2411 C CD1 . ILE   A 1 323 ? 29.208  7.354   -1.476  1.00 18.52  ? 860  ILE   A CD1 1 
ATOM   2412 N N   . LEU   A 1 324 ? 30.124  3.955   -5.860  1.00 20.42  ? 861  LEU   A N   1 
ATOM   2413 C CA  . LEU   A 1 324 ? 29.728  3.297   -7.100  1.00 20.45  ? 861  LEU   A CA  1 
ATOM   2414 C C   . LEU   A 1 324 ? 30.282  1.877   -7.175  1.00 22.69  ? 861  LEU   A C   1 
ATOM   2415 O O   . LEU   A 1 324 ? 29.598  0.964   -7.648  1.00 22.80  ? 861  LEU   A O   1 
ATOM   2416 C CB  . LEU   A 1 324 ? 30.188  4.135   -8.293  1.00 18.87  ? 861  LEU   A CB  1 
ATOM   2417 C CG  . LEU   A 1 324 ? 29.956  3.606   -9.707  1.00 20.03  ? 861  LEU   A CG  1 
ATOM   2418 C CD1 . LEU   A 1 324 ? 29.739  4.772   -10.662 1.00 19.90  ? 861  LEU   A CD1 1 
ATOM   2419 C CD2 . LEU   A 1 324 ? 31.124  2.741   -10.185 1.00 20.92  ? 861  LEU   A CD2 1 
ATOM   2420 N N   . GLN   A 1 325 ? 31.521  1.670   -6.714  1.00 24.72  ? 862  GLN   A N   1 
ATOM   2421 C CA  . GLN   A 1 325 ? 32.137  0.353   -6.846  1.00 28.95  ? 862  GLN   A CA  1 
ATOM   2422 C C   . GLN   A 1 325 ? 31.443  -0.671  -5.955  1.00 29.59  ? 862  GLN   A C   1 
ATOM   2423 O O   . GLN   A 1 325 ? 31.287  -1.835  -6.347  1.00 28.99  ? 862  GLN   A O   1 
ATOM   2424 C CB  . GLN   A 1 325 ? 33.633  0.434   -6.534  1.00 32.90  ? 862  GLN   A CB  1 
ATOM   2425 C CG  . GLN   A 1 325 ? 34.390  -0.905  -6.620  1.00 37.65  ? 862  GLN   A CG  1 
ATOM   2426 C CD  . GLN   A 1 325 ? 34.603  -1.412  -8.052  1.00 40.46  ? 862  GLN   A CD  1 
ATOM   2427 O OE1 . GLN   A 1 325 ? 35.153  -0.707  -8.901  1.00 41.43  ? 862  GLN   A OE1 1 
ATOM   2428 N NE2 . GLN   A 1 325 ? 34.178  -2.646  -8.314  1.00 40.92  ? 862  GLN   A NE2 1 
ATOM   2429 N N   . VAL   A 1 326 ? 30.995  -0.259  -4.765  1.00 19.39  ? 863  VAL   A N   1 
ATOM   2430 C CA  . VAL   A 1 326 ? 30.256  -1.192  -3.917  1.00 25.05  ? 863  VAL   A CA  1 
ATOM   2431 C C   . VAL   A 1 326 ? 28.861  -1.443  -4.489  1.00 23.83  ? 863  VAL   A C   1 
ATOM   2432 O O   . VAL   A 1 326 ? 28.341  -2.564  -4.410  1.00 24.54  ? 863  VAL   A O   1 
ATOM   2433 C CB  . VAL   A 1 326 ? 30.201  -0.687  -2.463  1.00 19.69  ? 863  VAL   A CB  1 
ATOM   2434 C CG1 . VAL   A 1 326 ? 29.586  -1.750  -1.561  1.00 20.48  ? 863  VAL   A CG1 1 
ATOM   2435 C CG2 . VAL   A 1 326 ? 31.596  -0.322  -1.963  1.00 20.24  ? 863  VAL   A CG2 1 
ATOM   2436 N N   . PHE   A 1 327 ? 28.232  -0.410  -5.067  1.00 18.31  ? 864  PHE   A N   1 
ATOM   2437 C CA  . PHE   A 1 327 ? 27.002  -0.610  -5.831  1.00 18.02  ? 864  PHE   A CA  1 
ATOM   2438 C C   . PHE   A 1 327 ? 27.171  -1.741  -6.840  1.00 25.53  ? 864  PHE   A C   1 
ATOM   2439 O O   . PHE   A 1 327 ? 26.321  -2.634  -6.942  1.00 19.31  ? 864  PHE   A O   1 
ATOM   2440 C CB  . PHE   A 1 327 ? 26.604  0.681   -6.557  1.00 18.48  ? 864  PHE   A CB  1 
ATOM   2441 C CG  . PHE   A 1 327 ? 25.822  1.660   -5.716  1.00 18.05  ? 864  PHE   A CG  1 
ATOM   2442 C CD1 . PHE   A 1 327 ? 25.139  1.252   -4.578  1.00 21.12  ? 864  PHE   A CD1 1 
ATOM   2443 C CD2 . PHE   A 1 327 ? 25.759  2.994   -6.082  1.00 16.86  ? 864  PHE   A CD2 1 
ATOM   2444 C CE1 . PHE   A 1 327 ? 24.418  2.159   -3.822  1.00 16.20  ? 864  PHE   A CE1 1 
ATOM   2445 C CE2 . PHE   A 1 327 ? 25.039  3.909   -5.330  1.00 16.35  ? 864  PHE   A CE2 1 
ATOM   2446 C CZ  . PHE   A 1 327 ? 24.368  3.488   -4.198  1.00 17.03  ? 864  PHE   A CZ  1 
ATOM   2447 N N   . GLN   A 1 328 ? 28.278  -1.722  -7.592  1.00 25.56  ? 865  GLN   A N   1 
ATOM   2448 C CA  . GLN   A 1 328 ? 28.508  -2.765  -8.591  1.00 28.33  ? 865  GLN   A CA  1 
ATOM   2449 C C   . GLN   A 1 328 ? 28.819  -4.108  -7.941  1.00 27.80  ? 865  GLN   A C   1 
ATOM   2450 O O   . GLN   A 1 328 ? 28.450  -5.157  -8.483  1.00 29.09  ? 865  GLN   A O   1 
ATOM   2451 C CB  . GLN   A 1 328 ? 29.648  -2.370  -9.533  1.00 32.71  ? 865  GLN   A CB  1 
ATOM   2452 C CG  . GLN   A 1 328 ? 29.471  -1.032  -10.250 1.00 35.48  ? 865  GLN   A CG  1 
ATOM   2453 C CD  . GLN   A 1 328 ? 29.434  -1.161  -11.780 1.00 39.60  ? 865  GLN   A CD  1 
ATOM   2454 O OE1 . GLN   A 1 328 ? 30.345  -0.711  -12.470 1.00 42.40  ? 865  GLN   A OE1 1 
ATOM   2455 N NE2 . GLN   A 1 328 ? 28.382  -1.774  -12.294 1.00 40.33  ? 865  GLN   A NE2 1 
ATOM   2456 N N   . ASP   A 1 329 ? 29.499  -4.104  -6.791  1.00 26.86  ? 866  ASP   A N   1 
ATOM   2457 C CA  . ASP   A 1 329 ? 29.745  -5.358  -6.088  1.00 28.40  ? 866  ASP   A CA  1 
ATOM   2458 C C   . ASP   A 1 329 ? 28.451  -5.976  -5.584  1.00 27.37  ? 866  ASP   A C   1 
ATOM   2459 O O   . ASP   A 1 329 ? 28.356  -7.202  -5.477  1.00 28.74  ? 866  ASP   A O   1 
ATOM   2460 C CB  . ASP   A 1 329 ? 30.706  -5.148  -4.917  1.00 29.47  ? 866  ASP   A CB  1 
ATOM   2461 C CG  . ASP   A 1 329 ? 32.089  -4.726  -5.364  1.00 30.46  ? 866  ASP   A CG  1 
ATOM   2462 O OD1 . ASP   A 1 329 ? 32.484  -5.074  -6.497  1.00 31.52  ? 866  ASP   A OD1 1 
ATOM   2463 O OD2 . ASP   A 1 329 ? 32.786  -4.053  -4.578  1.00 30.64  ? 866  ASP   A OD2 1 
ATOM   2464 N N   . LEU   A 1 330 ? 27.455  -5.148  -5.272  1.00 25.02  ? 867  LEU   A N   1 
ATOM   2465 C CA  . LEU   A 1 330 ? 26.154  -5.610  -4.813  1.00 22.58  ? 867  LEU   A CA  1 
ATOM   2466 C C   . LEU   A 1 330 ? 25.152  -5.783  -5.946  1.00 22.15  ? 867  LEU   A C   1 
ATOM   2467 O O   . LEU   A 1 330 ? 23.975  -6.043  -5.672  1.00 22.94  ? 867  LEU   A O   1 
ATOM   2468 C CB  . LEU   A 1 330 ? 25.581  -4.634  -3.784  1.00 21.59  ? 867  LEU   A CB  1 
ATOM   2469 C CG  . LEU   A 1 330 ? 26.399  -4.383  -2.520  1.00 23.60  ? 867  LEU   A CG  1 
ATOM   2470 C CD1 . LEU   A 1 330 ? 25.887  -3.144  -1.811  1.00 23.41  ? 867  LEU   A CD1 1 
ATOM   2471 C CD2 . LEU   A 1 330 ? 26.349  -5.590  -1.600  1.00 22.44  ? 867  LEU   A CD2 1 
ATOM   2472 N N   . ASN   A 1 331 ? 25.580  -5.629  -7.200  1.00 21.66  ? 868  ASN   A N   1 
ATOM   2473 C CA  . ASN   A 1 331 ? 24.662  -5.637  -8.341  1.00 24.60  ? 868  ASN   A CA  1 
ATOM   2474 C C   . ASN   A 1 331 ? 23.517  -4.640  -8.167  1.00 23.49  ? 868  ASN   A C   1 
ATOM   2475 O O   . ASN   A 1 331 ? 22.361  -4.948  -8.460  1.00 25.01  ? 868  ASN   A O   1 
ATOM   2476 C CB  . ASN   A 1 331 ? 24.087  -7.032  -8.586  1.00 27.50  ? 868  ASN   A CB  1 
ATOM   2477 C CG  . ASN   A 1 331 ? 25.092  -7.991  -9.156  1.00 29.43  ? 868  ASN   A CG  1 
ATOM   2478 O OD1 . ASN   A 1 331 ? 26.075  -7.588  -9.773  1.00 30.72  ? 868  ASN   A OD1 1 
ATOM   2479 N ND2 . ASN   A 1 331 ? 24.843  -9.282  -8.964  1.00 30.04  ? 868  ASN   A ND2 1 
ATOM   2480 N N   . ASN   A 1 332 ? 23.823  -3.435  -7.679  1.00 22.10  ? 869  ASN   A N   1 
ATOM   2481 C CA  . ASN   A 1 332 ? 22.817  -2.370  -7.593  1.00 21.58  ? 869  ASN   A CA  1 
ATOM   2482 C C   . ASN   A 1 332 ? 23.063  -1.417  -8.754  1.00 21.05  ? 869  ASN   A C   1 
ATOM   2483 O O   . ASN   A 1 332 ? 23.746  -0.404  -8.612  1.00 17.51  ? 869  ASN   A O   1 
ATOM   2484 C CB  . ASN   A 1 332 ? 22.862  -1.639  -6.253  1.00 21.34  ? 869  ASN   A CB  1 
ATOM   2485 C CG  . ASN   A 1 332 ? 21.795  -0.550  -6.140  1.00 17.08  ? 869  ASN   A CG  1 
ATOM   2486 O OD1 . ASN   A 1 332 ? 20.985  -0.345  -7.054  1.00 17.00  ? 869  ASN   A OD1 1 
ATOM   2487 N ND2 . ASN   A 1 332 ? 21.788  0.148   -5.010  1.00 16.76  ? 869  ASN   A ND2 1 
ATOM   2488 N N   . PHE   A 1 333 ? 22.474  -1.739  -9.905  1.00 20.79  ? 870  PHE   A N   1 
ATOM   2489 C CA  . PHE   A 1 333 ? 22.673  -0.920  -11.091 1.00 22.81  ? 870  PHE   A CA  1 
ATOM   2490 C C   . PHE   A 1 333 ? 21.845  0.355   -11.049 1.00 22.30  ? 870  PHE   A C   1 
ATOM   2491 O O   . PHE   A 1 333 ? 22.208  1.344   -11.689 1.00 23.54  ? 870  PHE   A O   1 
ATOM   2492 C CB  . PHE   A 1 333 ? 22.359  -1.740  -12.342 1.00 25.37  ? 870  PHE   A CB  1 
ATOM   2493 C CG  . PHE   A 1 333 ? 23.286  -2.904  -12.533 1.00 26.58  ? 870  PHE   A CG  1 
ATOM   2494 C CD1 . PHE   A 1 333 ? 24.596  -2.697  -12.927 1.00 26.64  ? 870  PHE   A CD1 1 
ATOM   2495 C CD2 . PHE   A 1 333 ? 22.858  -4.198  -12.291 1.00 27.75  ? 870  PHE   A CD2 1 
ATOM   2496 C CE1 . PHE   A 1 333 ? 25.456  -3.755  -13.090 1.00 28.92  ? 870  PHE   A CE1 1 
ATOM   2497 C CE2 . PHE   A 1 333 ? 23.716  -5.270  -12.456 1.00 29.65  ? 870  PHE   A CE2 1 
ATOM   2498 C CZ  . PHE   A 1 333 ? 25.016  -5.049  -12.854 1.00 30.17  ? 870  PHE   A CZ  1 
ATOM   2499 N N   . ASN   A 1 334 ? 20.743  0.359   -10.307 1.00 21.53  ? 871  ASN   A N   1 
ATOM   2500 C CA  . ASN   A 1 334 ? 20.049  1.613   -10.057 1.00 20.76  ? 871  ASN   A CA  1 
ATOM   2501 C C   . ASN   A 1 334 ? 20.978  2.597   -9.360  1.00 20.66  ? 871  ASN   A C   1 
ATOM   2502 O O   . ASN   A 1 334 ? 21.131  3.745   -9.793  1.00 20.06  ? 871  ASN   A O   1 
ATOM   2503 C CB  . ASN   A 1 334 ? 18.794  1.356   -9.226  1.00 21.90  ? 871  ASN   A CB  1 
ATOM   2504 C CG  . ASN   A 1 334 ? 17.909  2.567   -9.133  1.00 22.60  ? 871  ASN   A CG  1 
ATOM   2505 O OD1 . ASN   A 1 334 ? 17.199  2.900   -10.081 1.00 23.87  ? 871  ASN   A OD1 1 
ATOM   2506 N ND2 . ASN   A 1 334 ? 17.948  3.244   -7.991  1.00 22.46  ? 871  ASN   A ND2 1 
ATOM   2507 N N   . GLY   A 1 335 ? 21.640  2.145   -8.293  1.00 20.43  ? 872  GLY   A N   1 
ATOM   2508 C CA  . GLY   A 1 335 ? 22.592  3.001   -7.606  1.00 17.62  ? 872  GLY   A CA  1 
ATOM   2509 C C   . GLY   A 1 335 ? 23.739  3.433   -8.497  1.00 17.39  ? 872  GLY   A C   1 
ATOM   2510 O O   . GLY   A 1 335 ? 24.175  4.585   -8.440  1.00 15.45  ? 872  GLY   A O   1 
ATOM   2511 N N   . VAL   A 1 336 ? 24.242  2.517   -9.337  1.00 16.36  ? 873  VAL   A N   1 
ATOM   2512 C CA  . VAL   A 1 336 ? 25.323  2.858   -10.262 1.00 16.69  ? 873  VAL   A CA  1 
ATOM   2513 C C   . VAL   A 1 336 ? 24.902  3.990   -11.193 1.00 25.61  ? 873  VAL   A C   1 
ATOM   2514 O O   . VAL   A 1 336 ? 25.609  4.995   -11.339 1.00 16.48  ? 873  VAL   A O   1 
ATOM   2515 C CB  . VAL   A 1 336 ? 25.758  1.627   -11.071 1.00 17.67  ? 873  VAL   A CB  1 
ATOM   2516 C CG1 . VAL   A 1 336 ? 26.781  2.042   -12.128 1.00 18.25  ? 873  VAL   A CG1 1 
ATOM   2517 C CG2 . VAL   A 1 336 ? 26.322  0.551   -10.159 1.00 27.33  ? 873  VAL   A CG2 1 
ATOM   2518 N N   . LEU   A 1 337 ? 23.746  3.836   -11.846 1.00 22.88  ? 874  LEU   A N   1 
ATOM   2519 C CA  . LEU   A 1 337 ? 23.329  4.780   -12.875 1.00 21.76  ? 874  LEU   A CA  1 
ATOM   2520 C C   . LEU   A 1 337 ? 22.793  6.089   -12.301 1.00 20.12  ? 874  LEU   A C   1 
ATOM   2521 O O   . LEU   A 1 337 ? 22.742  7.088   -13.025 1.00 19.50  ? 874  LEU   A O   1 
ATOM   2522 C CB  . LEU   A 1 337 ? 22.285  4.129   -13.789 1.00 23.17  ? 874  LEU   A CB  1 
ATOM   2523 C CG  . LEU   A 1 337 ? 22.795  3.241   -14.944 1.00 25.23  ? 874  LEU   A CG  1 
ATOM   2524 C CD1 . LEU   A 1 337 ? 23.759  3.996   -15.856 1.00 24.28  ? 874  LEU   A CD1 1 
ATOM   2525 C CD2 . LEU   A 1 337 ? 23.432  1.949   -14.456 1.00 25.20  ? 874  LEU   A CD2 1 
ATOM   2526 N N   . GLU   A 1 338 ? 22.392  6.111   -11.027 1.00 20.15  ? 875  GLU   A N   1 
ATOM   2527 C CA  . GLU   A 1 338 ? 22.130  7.388   -10.366 1.00 21.02  ? 875  GLU   A CA  1 
ATOM   2528 C C   . GLU   A 1 338 ? 23.411  8.208   -10.254 1.00 19.29  ? 875  GLU   A C   1 
ATOM   2529 O O   . GLU   A 1 338 ? 23.394  9.437   -10.393 1.00 18.06  ? 875  GLU   A O   1 
ATOM   2530 C CB  . GLU   A 1 338 ? 21.527  7.160   -8.976  1.00 22.95  ? 875  GLU   A CB  1 
ATOM   2531 C CG  . GLU   A 1 338 ? 20.105  6.629   -8.960  1.00 26.12  ? 875  GLU   A CG  1 
ATOM   2532 C CD  . GLU   A 1 338 ? 19.682  6.116   -7.583  1.00 29.64  ? 875  GLU   A CD  1 
ATOM   2533 O OE1 . GLU   A 1 338 ? 20.539  5.554   -6.867  1.00 30.67  ? 875  GLU   A OE1 1 
ATOM   2534 O OE2 . GLU   A 1 338 ? 18.494  6.278   -7.212  1.00 30.46  ? 875  GLU   A OE2 1 
ATOM   2535 N N   . ILE   A 1 339 ? 24.534  7.541   -10.002 1.00 19.47  ? 876  ILE   A N   1 
ATOM   2536 C CA  . ILE   A 1 339 ? 25.806  8.246   -9.909  1.00 19.93  ? 876  ILE   A CA  1 
ATOM   2537 C C   . ILE   A 1 339 ? 26.271  8.697   -11.289 1.00 18.32  ? 876  ILE   A C   1 
ATOM   2538 O O   . ILE   A 1 339 ? 26.739  9.830   -11.461 1.00 17.07  ? 876  ILE   A O   1 
ATOM   2539 C CB  . ILE   A 1 339 ? 26.844  7.356   -9.205  1.00 21.64  ? 876  ILE   A CB  1 
ATOM   2540 C CG1 . ILE   A 1 339 ? 26.480  7.218   -7.724  1.00 15.00  ? 876  ILE   A CG1 1 
ATOM   2541 C CG2 . ILE   A 1 339 ? 28.246  7.905   -9.400  1.00 15.56  ? 876  ILE   A CG2 1 
ATOM   2542 C CD1 . ILE   A 1 339 ? 27.383  6.282   -6.947  1.00 24.78  ? 876  ILE   A CD1 1 
ATOM   2543 N N   . VAL   A 1 340 ? 26.152  7.822   -12.292 1.00 19.02  ? 877  VAL   A N   1 
ATOM   2544 C CA  . VAL   A 1 340 ? 26.438  8.217   -13.670 1.00 20.33  ? 877  VAL   A CA  1 
ATOM   2545 C C   . VAL   A 1 340 ? 25.573  9.409   -14.062 1.00 22.41  ? 877  VAL   A C   1 
ATOM   2546 O O   . VAL   A 1 340 ? 26.031  10.348  -14.730 1.00 22.73  ? 877  VAL   A O   1 
ATOM   2547 C CB  . VAL   A 1 340 ? 26.218  7.022   -14.619 1.00 19.34  ? 877  VAL   A CB  1 
ATOM   2548 C CG1 . VAL   A 1 340 ? 26.301  7.464   -16.071 1.00 19.26  ? 877  VAL   A CG1 1 
ATOM   2549 C CG2 . VAL   A 1 340 ? 27.225  5.916   -14.330 1.00 18.32  ? 877  VAL   A CG2 1 
ATOM   2550 N N   . SER   A 1 341 ? 24.310  9.394   -13.634 1.00 23.32  ? 878  SER   A N   1 
ATOM   2551 C CA  . SER   A 1 341 ? 23.401  10.491  -13.932 1.00 25.20  ? 878  SER   A CA  1 
ATOM   2552 C C   . SER   A 1 341 ? 23.900  11.800  -13.326 1.00 23.88  ? 878  SER   A C   1 
ATOM   2553 O O   . SER   A 1 341 ? 23.870  12.848  -13.981 1.00 23.94  ? 878  SER   A O   1 
ATOM   2554 C CB  . SER   A 1 341 ? 22.004  10.139  -13.421 1.00 28.24  ? 878  SER   A CB  1 
ATOM   2555 O OG  . SER   A 1 341 ? 21.033  11.056  -13.881 1.00 31.46  ? 878  SER   A OG  1 
ATOM   2556 N N   . ALA   A 1 342 ? 24.393  11.753  -12.084 1.00 22.23  ? 879  ALA   A N   1 
ATOM   2557 C CA  . ALA   A 1 342 ? 24.852  12.969  -11.414 1.00 20.63  ? 879  ALA   A CA  1 
ATOM   2558 C C   . ALA   A 1 342 ? 26.067  13.578  -12.116 1.00 19.52  ? 879  ALA   A C   1 
ATOM   2559 O O   . ALA   A 1 342 ? 26.118  14.790  -12.366 1.00 18.55  ? 879  ALA   A O   1 
ATOM   2560 C CB  . ALA   A 1 342 ? 25.172  12.668  -9.949  1.00 19.67  ? 879  ALA   A CB  1 
ATOM   2561 N N   . VAL   A 1 343 ? 27.062  12.753  -12.444 1.00 16.86  ? 880  VAL   A N   1 
ATOM   2562 C CA  . VAL   A 1 343 ? 28.254  13.296  -13.079 1.00 19.74  ? 880  VAL   A CA  1 
ATOM   2563 C C   . VAL   A 1 343 ? 27.986  13.735  -14.513 1.00 20.98  ? 880  VAL   A C   1 
ATOM   2564 O O   . VAL   A 1 343 ? 28.776  14.501  -15.079 1.00 21.49  ? 880  VAL   A O   1 
ATOM   2565 C CB  . VAL   A 1 343 ? 29.411  12.281  -13.039 1.00 19.96  ? 880  VAL   A CB  1 
ATOM   2566 C CG1 . VAL   A 1 343 ? 29.835  12.013  -11.601 1.00 18.83  ? 880  VAL   A CG1 1 
ATOM   2567 C CG2 . VAL   A 1 343 ? 29.010  10.995  -13.741 1.00 20.74  ? 880  VAL   A CG2 1 
ATOM   2568 N N   . ASN   A 1 344 ? 26.899  13.267  -15.131 1.00 21.67  ? 881  ASN   A N   1 
ATOM   2569 C CA  . ASN   A 1 344 ? 26.567  13.765  -16.458 1.00 22.25  ? 881  ASN   A CA  1 
ATOM   2570 C C   . ASN   A 1 344 ? 25.843  15.106  -16.410 1.00 22.75  ? 881  ASN   A C   1 
ATOM   2571 O O   . ASN   A 1 344 ? 25.729  15.761  -17.452 1.00 24.21  ? 881  ASN   A O   1 
ATOM   2572 C CB  . ASN   A 1 344 ? 25.731  12.734  -17.229 1.00 23.46  ? 881  ASN   A CB  1 
ATOM   2573 C CG  . ASN   A 1 344 ? 26.585  11.617  -17.853 1.00 25.51  ? 881  ASN   A CG  1 
ATOM   2574 O OD1 . ASN   A 1 344 ? 27.807  11.726  -17.942 1.00 26.64  ? 881  ASN   A OD1 1 
ATOM   2575 N ND2 . ASN   A 1 344 ? 25.932  10.550  -18.298 1.00 21.25  ? 881  ASN   A ND2 1 
ATOM   2576 N N   . SER   A 1 345 ? 25.374  15.540  -15.238 1.00 21.57  ? 882  SER   A N   1 
ATOM   2577 C CA  . SER   A 1 345 ? 24.720  16.841  -15.137 1.00 22.33  ? 882  SER   A CA  1 
ATOM   2578 C C   . SER   A 1 345 ? 25.693  17.955  -15.523 1.00 24.35  ? 882  SER   A C   1 
ATOM   2579 O O   . SER   A 1 345 ? 26.902  17.869  -15.276 1.00 24.26  ? 882  SER   A O   1 
ATOM   2580 C CB  . SER   A 1 345 ? 24.167  17.068  -13.723 1.00 19.86  ? 882  SER   A CB  1 
ATOM   2581 O OG  . SER   A 1 345 ? 25.145  17.572  -12.829 1.00 18.97  ? 882  SER   A OG  1 
ATOM   2582 N N   A VAL   A 1 346 ? 25.139  19.012  -16.127 0.30 26.05  ? 883  VAL   A N   1 
ATOM   2583 N N   B VAL   A 1 346 ? 25.156  19.006  -16.150 0.70 26.10  ? 883  VAL   A N   1 
ATOM   2584 C CA  A VAL   A 1 346 ? 25.957  20.070  -16.722 0.30 26.12  ? 883  VAL   A CA  1 
ATOM   2585 C CA  B VAL   A 1 346 ? 26.012  20.046  -16.721 0.70 25.66  ? 883  VAL   A CA  1 
ATOM   2586 C C   A VAL   A 1 346 ? 26.847  20.730  -15.675 0.30 26.65  ? 883  VAL   A C   1 
ATOM   2587 C C   B VAL   A 1 346 ? 26.887  20.681  -15.648 0.70 26.60  ? 883  VAL   A C   1 
ATOM   2588 O O   A VAL   A 1 346 ? 28.009  21.055  -15.946 0.30 26.57  ? 883  VAL   A O   1 
ATOM   2589 O O   B VAL   A 1 346 ? 28.078  20.938  -15.871 0.70 26.66  ? 883  VAL   A O   1 
ATOM   2590 C CB  A VAL   A 1 346 ? 25.060  21.100  -17.439 0.30 28.40  ? 883  VAL   A CB  1 
ATOM   2591 C CB  B VAL   A 1 346 ? 25.165  21.102  -17.454 0.70 28.88  ? 883  VAL   A CB  1 
ATOM   2592 C CG1 A VAL   A 1 346 ? 24.433  20.486  -18.683 0.30 28.78  ? 883  VAL   A CG1 1 
ATOM   2593 C CG1 B VAL   A 1 346 ? 26.066  22.172  -18.041 0.70 28.39  ? 883  VAL   A CG1 1 
ATOM   2594 C CG2 A VAL   A 1 346 ? 23.975  21.624  -16.503 0.30 27.47  ? 883  VAL   A CG2 1 
ATOM   2595 C CG2 B VAL   A 1 346 ? 24.333  20.447  -18.545 0.70 28.67  ? 883  VAL   A CG2 1 
ATOM   2596 N N   . SER   A 1 347 ? 26.324  20.931  -14.464 1.00 25.09  ? 884  SER   A N   1 
ATOM   2597 C CA  . SER   A 1 347 ? 27.097  21.594  -13.416 1.00 26.08  ? 884  SER   A CA  1 
ATOM   2598 C C   . SER   A 1 347 ? 28.296  20.756  -12.961 1.00 27.02  ? 884  SER   A C   1 
ATOM   2599 O O   . SER   A 1 347 ? 29.327  21.315  -12.565 1.00 27.72  ? 884  SER   A O   1 
ATOM   2600 C CB  . SER   A 1 347 ? 26.184  21.933  -12.234 1.00 24.63  ? 884  SER   A CB  1 
ATOM   2601 O OG  . SER   A 1 347 ? 25.600  20.766  -11.690 1.00 25.20  ? 884  SER   A OG  1 
ATOM   2602 N N   . VAL   A 1 348 ? 28.193  19.430  -13.023 1.00 26.75  ? 885  VAL   A N   1 
ATOM   2603 C CA  . VAL   A 1 348 ? 29.317  18.571  -12.653 1.00 27.08  ? 885  VAL   A CA  1 
ATOM   2604 C C   . VAL   A 1 348 ? 30.212  18.267  -13.849 1.00 29.32  ? 885  VAL   A C   1 
ATOM   2605 O O   . VAL   A 1 348 ? 31.438  18.302  -13.732 1.00 30.10  ? 885  VAL   A O   1 
ATOM   2606 C CB  . VAL   A 1 348 ? 28.801  17.272  -12.003 1.00 27.75  ? 885  VAL   A CB  1 
ATOM   2607 C CG1 . VAL   A 1 348 ? 29.947  16.311  -11.764 1.00 27.39  ? 885  VAL   A CG1 1 
ATOM   2608 C CG2 . VAL   A 1 348 ? 28.081  17.577  -10.694 1.00 27.69  ? 885  VAL   A CG2 1 
ATOM   2609 N N   . TYR   A 1 349 ? 29.615  17.976  -15.010 1.00 30.21  ? 886  TYR   A N   1 
ATOM   2610 C CA  . TYR   A 1 349 ? 30.382  17.526  -16.172 1.00 30.02  ? 886  TYR   A CA  1 
ATOM   2611 C C   . TYR   A 1 349 ? 31.473  18.518  -16.568 1.00 32.22  ? 886  TYR   A C   1 
ATOM   2612 O O   . TYR   A 1 349 ? 32.533  18.111  -17.056 1.00 32.91  ? 886  TYR   A O   1 
ATOM   2613 C CB  . TYR   A 1 349 ? 29.429  17.281  -17.348 1.00 29.75  ? 886  TYR   A CB  1 
ATOM   2614 C CG  . TYR   A 1 349 ? 30.032  16.592  -18.558 1.00 29.59  ? 886  TYR   A CG  1 
ATOM   2615 C CD1 . TYR   A 1 349 ? 30.051  15.207  -18.653 1.00 28.47  ? 886  TYR   A CD1 1 
ATOM   2616 C CD2 . TYR   A 1 349 ? 30.553  17.326  -19.617 1.00 31.02  ? 886  TYR   A CD2 1 
ATOM   2617 C CE1 . TYR   A 1 349 ? 30.584  14.568  -19.758 1.00 28.52  ? 886  TYR   A CE1 1 
ATOM   2618 C CE2 . TYR   A 1 349 ? 31.091  16.696  -20.730 1.00 31.22  ? 886  TYR   A CE2 1 
ATOM   2619 C CZ  . TYR   A 1 349 ? 31.103  15.314  -20.794 1.00 29.42  ? 886  TYR   A CZ  1 
ATOM   2620 O OH  . TYR   A 1 349 ? 31.635  14.676  -21.897 1.00 29.16  ? 886  TYR   A OH  1 
ATOM   2621 N N   . ARG   A 1 350 ? 31.243  19.816  -16.367 1.00 32.48  ? 887  ARG   A N   1 
ATOM   2622 C CA  . ARG   A 1 350 ? 32.207  20.823  -16.798 1.00 34.15  ? 887  ARG   A CA  1 
ATOM   2623 C C   . ARG   A 1 350 ? 33.417  20.947  -15.877 1.00 33.50  ? 887  ARG   A C   1 
ATOM   2624 O O   . ARG   A 1 350 ? 34.353  21.680  -16.215 1.00 34.14  ? 887  ARG   A O   1 
ATOM   2625 C CB  . ARG   A 1 350 ? 31.521  22.186  -16.912 1.00 35.66  ? 887  ARG   A CB  1 
ATOM   2626 C CG  . ARG   A 1 350 ? 30.909  22.681  -15.610 1.00 35.08  ? 887  ARG   A CG  1 
ATOM   2627 C CD  . ARG   A 1 350 ? 30.306  24.061  -15.786 1.00 36.57  ? 887  ARG   A CD  1 
ATOM   2628 N NE  . ARG   A 1 350 ? 31.269  24.987  -16.376 1.00 38.29  ? 887  ARG   A NE  1 
ATOM   2629 C CZ  . ARG   A 1 350 ? 32.228  25.604  -15.690 1.00 37.18  ? 887  ARG   A CZ  1 
ATOM   2630 N NH1 . ARG   A 1 350 ? 33.069  26.422  -16.310 1.00 37.89  ? 887  ARG   A NH1 1 
ATOM   2631 N NH2 . ARG   A 1 350 ? 32.347  25.403  -14.384 1.00 34.93  ? 887  ARG   A NH2 1 
ATOM   2632 N N   . LEU   A 1 351 ? 33.430  20.256  -14.735 1.00 31.22  ? 888  LEU   A N   1 
ATOM   2633 C CA  . LEU   A 1 351 ? 34.478  20.435  -13.729 1.00 30.34  ? 888  LEU   A CA  1 
ATOM   2634 C C   . LEU   A 1 351 ? 35.737  19.667  -14.136 1.00 28.61  ? 888  LEU   A C   1 
ATOM   2635 O O   . LEU   A 1 351 ? 36.161  18.710  -13.486 1.00 25.94  ? 888  LEU   A O   1 
ATOM   2636 C CB  . LEU   A 1 351 ? 33.978  19.994  -12.360 1.00 29.75  ? 888  LEU   A CB  1 
ATOM   2637 C CG  . LEU   A 1 351 ? 32.846  20.825  -11.756 1.00 29.29  ? 888  LEU   A CG  1 
ATOM   2638 C CD1 . LEU   A 1 351 ? 32.434  20.258  -10.412 1.00 28.02  ? 888  LEU   A CD1 1 
ATOM   2639 C CD2 . LEU   A 1 351 ? 33.273  22.274  -11.619 1.00 28.92  ? 888  LEU   A CD2 1 
ATOM   2640 N N   . ASP   A 1 352 ? 36.360  20.141  -15.224 1.00 29.27  ? 889  ASP   A N   1 
ATOM   2641 C CA  . ASP   A 1 352 ? 37.472  19.410  -15.833 1.00 27.80  ? 889  ASP   A CA  1 
ATOM   2642 C C   . ASP   A 1 352 ? 38.654  19.276  -14.884 1.00 27.61  ? 889  ASP   A C   1 
ATOM   2643 O O   . ASP   A 1 352 ? 39.292  18.221  -14.827 1.00 27.96  ? 889  ASP   A O   1 
ATOM   2644 C CB  . ASP   A 1 352 ? 37.921  20.095  -17.124 1.00 28.04  ? 889  ASP   A CB  1 
ATOM   2645 C CG  . ASP   A 1 352 ? 36.972  19.850  -18.271 1.00 28.20  ? 889  ASP   A CG  1 
ATOM   2646 O OD1 . ASP   A 1 352 ? 36.194  18.873  -18.205 1.00 26.53  ? 889  ASP   A OD1 1 
ATOM   2647 O OD2 . ASP   A 1 352 ? 37.016  20.634  -19.243 1.00 30.67  ? 889  ASP   A OD2 1 
ATOM   2648 N N   . HIS   A 1 353 ? 38.977  20.337  -14.145 1.00 29.37  ? 890  HIS   A N   1 
ATOM   2649 C CA  . HIS   A 1 353 ? 40.116  20.264  -13.238 1.00 31.16  ? 890  HIS   A CA  1 
ATOM   2650 C C   . HIS   A 1 353 ? 39.873  19.262  -12.118 1.00 30.06  ? 890  HIS   A C   1 
ATOM   2651 O O   . HIS   A 1 353 ? 40.826  18.658  -11.609 1.00 30.12  ? 890  HIS   A O   1 
ATOM   2652 C CB  . HIS   A 1 353 ? 40.428  21.644  -12.657 1.00 32.55  ? 890  HIS   A CB  1 
ATOM   2653 C CG  . HIS   A 1 353 ? 40.906  22.639  -13.671 1.00 35.28  ? 890  HIS   A CG  1 
ATOM   2654 N ND1 . HIS   A 1 353 ? 42.146  22.560  -14.267 1.00 36.84  ? 890  HIS   A ND1 1 
ATOM   2655 C CD2 . HIS   A 1 353 ? 40.315  23.746  -14.180 1.00 36.47  ? 890  HIS   A CD2 1 
ATOM   2656 C CE1 . HIS   A 1 353 ? 42.295  23.569  -15.106 1.00 37.72  ? 890  HIS   A CE1 1 
ATOM   2657 N NE2 . HIS   A 1 353 ? 41.199  24.305  -15.070 1.00 37.55  ? 890  HIS   A NE2 1 
ATOM   2658 N N   . THR   A 1 354 ? 38.613  19.063  -11.726 1.00 27.88  ? 891  THR   A N   1 
ATOM   2659 C CA  . THR   A 1 354 ? 38.314  18.072  -10.698 1.00 26.32  ? 891  THR   A CA  1 
ATOM   2660 C C   . THR   A 1 354 ? 38.472  16.655  -11.242 1.00 26.84  ? 891  THR   A C   1 
ATOM   2661 O O   . THR   A 1 354 ? 39.107  15.806  -10.606 1.00 26.22  ? 891  THR   A O   1 
ATOM   2662 C CB  . THR   A 1 354 ? 36.903  18.291  -10.148 1.00 23.89  ? 891  THR   A CB  1 
ATOM   2663 O OG1 . THR   A 1 354 ? 36.825  19.587  -9.543  1.00 23.29  ? 891  THR   A OG1 1 
ATOM   2664 C CG2 . THR   A 1 354 ? 36.562  17.228  -9.110  1.00 22.51  ? 891  THR   A CG2 1 
ATOM   2665 N N   . PHE   A 1 355 ? 37.916  16.385  -12.427 1.00 28.75  ? 892  PHE   A N   1 
ATOM   2666 C CA  . PHE   A 1 355 ? 38.061  15.059  -13.023 1.00 30.50  ? 892  PHE   A CA  1 
ATOM   2667 C C   . PHE   A 1 355 ? 39.516  14.755  -13.356 1.00 32.13  ? 892  PHE   A C   1 
ATOM   2668 O O   . PHE   A 1 355 ? 39.967  13.613  -13.211 1.00 31.76  ? 892  PHE   A O   1 
ATOM   2669 C CB  . PHE   A 1 355 ? 37.187  14.940  -14.276 1.00 30.58  ? 892  PHE   A CB  1 
ATOM   2670 C CG  . PHE   A 1 355 ? 35.726  14.771  -13.979 1.00 29.63  ? 892  PHE   A CG  1 
ATOM   2671 C CD1 . PHE   A 1 355 ? 35.205  13.519  -13.694 1.00 28.84  ? 892  PHE   A CD1 1 
ATOM   2672 C CD2 . PHE   A 1 355 ? 34.874  15.865  -13.973 1.00 28.80  ? 892  PHE   A CD2 1 
ATOM   2673 C CE1 . PHE   A 1 355 ? 33.862  13.360  -13.412 1.00 28.06  ? 892  PHE   A CE1 1 
ATOM   2674 C CE2 . PHE   A 1 355 ? 33.529  15.715  -13.693 1.00 28.56  ? 892  PHE   A CE2 1 
ATOM   2675 C CZ  . PHE   A 1 355 ? 33.021  14.460  -13.410 1.00 28.59  ? 892  PHE   A CZ  1 
ATOM   2676 N N   . GLU   A 1 356 ? 40.268  15.764  -13.799 1.00 34.22  ? 893  GLU   A N   1 
ATOM   2677 C CA  . GLU   A 1 356 ? 41.666  15.540  -14.159 1.00 37.45  ? 893  GLU   A CA  1 
ATOM   2678 C C   . GLU   A 1 356 ? 42.518  15.201  -12.940 1.00 34.47  ? 893  GLU   A C   1 
ATOM   2679 O O   . GLU   A 1 356 ? 43.495  14.451  -13.055 1.00 35.24  ? 893  GLU   A O   1 
ATOM   2680 C CB  . GLU   A 1 356 ? 42.227  16.768  -14.873 1.00 41.82  ? 893  GLU   A CB  1 
ATOM   2681 C CG  . GLU   A 1 356 ? 43.623  16.566  -15.419 1.00 47.31  ? 893  GLU   A CG  1 
ATOM   2682 C CD  . GLU   A 1 356 ? 43.697  15.395  -16.381 1.00 51.26  ? 893  GLU   A CD  1 
ATOM   2683 O OE1 . GLU   A 1 356 ? 42.820  15.303  -17.267 1.00 52.37  ? 893  GLU   A OE1 1 
ATOM   2684 O OE2 . GLU   A 1 356 ? 44.622  14.561  -16.248 1.00 52.62  ? 893  GLU   A OE2 1 
ATOM   2685 N N   . ALA   A 1 357 ? 42.161  15.733  -11.769 1.00 29.72  ? 894  ALA   A N   1 
ATOM   2686 C CA  . ALA   A 1 357 ? 42.916  15.445  -10.559 1.00 26.51  ? 894  ALA   A CA  1 
ATOM   2687 C C   . ALA   A 1 357 ? 42.667  14.037  -10.032 1.00 26.59  ? 894  ALA   A C   1 
ATOM   2688 O O   . ALA   A 1 357 ? 43.447  13.560  -9.202  1.00 27.21  ? 894  ALA   A O   1 
ATOM   2689 C CB  . ALA   A 1 357 ? 42.576  16.471  -9.482  1.00 24.02  ? 894  ALA   A CB  1 
ATOM   2690 N N   . LEU   A 1 358 ? 41.604  13.370  -10.486 1.00 27.43  ? 895  LEU   A N   1 
ATOM   2691 C CA  . LEU   A 1 358 ? 41.293  12.025  -10.017 1.00 27.99  ? 895  LEU   A CA  1 
ATOM   2692 C C   . LEU   A 1 358 ? 42.425  11.057  -10.328 1.00 30.94  ? 895  LEU   A C   1 
ATOM   2693 O O   . LEU   A 1 358 ? 43.015  11.096  -11.410 1.00 32.04  ? 895  LEU   A O   1 
ATOM   2694 C CB  . LEU   A 1 358 ? 40.010  11.519  -10.671 1.00 27.08  ? 895  LEU   A CB  1 
ATOM   2695 C CG  . LEU   A 1 358 ? 38.681  12.027  -10.138 1.00 25.42  ? 895  LEU   A CG  1 
ATOM   2696 C CD1 . LEU   A 1 358 ? 37.573  11.533  -11.047 1.00 26.10  ? 895  LEU   A CD1 1 
ATOM   2697 C CD2 . LEU   A 1 358 ? 38.479  11.540  -8.716  1.00 23.63  ? 895  LEU   A CD2 1 
ATOM   2698 N N   . GLN   A 1 359 ? 42.722  10.175  -9.376  1.00 32.31  ? 896  GLN   A N   1 
ATOM   2699 C CA  . GLN   A 1 359 ? 43.703  9.139   -9.649  1.00 35.48  ? 896  GLN   A CA  1 
ATOM   2700 C C   . GLN   A 1 359 ? 43.184  8.237   -10.759 1.00 36.52  ? 896  GLN   A C   1 
ATOM   2701 O O   . GLN   A 1 359 ? 41.977  8.022   -10.904 1.00 36.41  ? 896  GLN   A O   1 
ATOM   2702 C CB  . GLN   A 1 359 ? 44.026  8.329   -8.390  1.00 38.67  ? 896  GLN   A CB  1 
ATOM   2703 C CG  . GLN   A 1 359 ? 42.830  7.954   -7.532  1.00 40.32  ? 896  GLN   A CG  1 
ATOM   2704 C CD  . GLN   A 1 359 ? 43.197  6.982   -6.419  1.00 43.11  ? 896  GLN   A CD  1 
ATOM   2705 O OE1 . GLN   A 1 359 ? 42.654  5.877   -6.340  1.00 43.97  ? 896  GLN   A OE1 1 
ATOM   2706 N NE2 . GLN   A 1 359 ? 44.123  7.389   -5.553  1.00 43.59  ? 896  GLN   A NE2 1 
ATOM   2707 N N   . GLU   A 1 360 ? 44.121  7.722   -11.555 1.00 41.09  ? 897  GLU   A N   1 
ATOM   2708 C CA  . GLU   A 1 360 ? 43.774  7.032   -12.793 1.00 41.28  ? 897  GLU   A CA  1 
ATOM   2709 C C   . GLU   A 1 360 ? 42.848  5.844   -12.556 1.00 37.69  ? 897  GLU   A C   1 
ATOM   2710 O O   . GLU   A 1 360 ? 42.003  5.543   -13.403 1.00 36.85  ? 897  GLU   A O   1 
ATOM   2711 C CB  . GLU   A 1 360 ? 45.056  6.582   -13.494 1.00 44.68  ? 897  GLU   A CB  1 
ATOM   2712 C CG  . GLU   A 1 360 ? 44.957  6.452   -15.003 1.00 46.60  ? 897  GLU   A CG  1 
ATOM   2713 C CD  . GLU   A 1 360 ? 46.328  6.409   -15.651 1.00 49.78  ? 897  GLU   A CD  1 
ATOM   2714 O OE1 . GLU   A 1 360 ? 47.020  7.452   -15.655 1.00 50.00  ? 897  GLU   A OE1 1 
ATOM   2715 O OE2 . GLU   A 1 360 ? 46.721  5.328   -16.143 1.00 51.92  ? 897  GLU   A OE2 1 
ATOM   2716 N N   . ARG   A 1 361 ? 42.975  5.165   -11.418 1.00 35.71  ? 898  ARG   A N   1 
ATOM   2717 C CA  . ARG   A 1 361 ? 42.196  3.948   -11.211 1.00 33.16  ? 898  ARG   A CA  1 
ATOM   2718 C C   . ARG   A 1 361 ? 40.720  4.260   -10.978 1.00 30.53  ? 898  ARG   A C   1 
ATOM   2719 O O   . ARG   A 1 361 ? 39.834  3.607   -11.546 1.00 25.42  ? 898  ARG   A O   1 
ATOM   2720 C CB  . ARG   A 1 361 ? 42.766  3.152   -10.040 1.00 34.48  ? 898  ARG   A CB  1 
ATOM   2721 C CG  . ARG   A 1 361 ? 41.819  2.086   -9.536  1.00 36.69  ? 898  ARG   A CG  1 
ATOM   2722 C CD  . ARG   A 1 361 ? 42.457  1.281   -8.401  1.00 40.31  ? 898  ARG   A CD  1 
ATOM   2723 N NE  . ARG   A 1 361 ? 41.429  0.868   -7.451  1.00 41.25  ? 898  ARG   A NE  1 
ATOM   2724 C CZ  . ARG   A 1 361 ? 40.614  -0.176  -7.582  1.00 42.88  ? 898  ARG   A CZ  1 
ATOM   2725 N NH1 . ARG   A 1 361 ? 40.637  -0.953  -8.655  1.00 43.55  ? 898  ARG   A NH1 1 
ATOM   2726 N NH2 . ARG   A 1 361 ? 39.742  -0.422  -6.621  1.00 42.99  ? 898  ARG   A NH2 1 
ATOM   2727 N N   . LYS   A 1 362 ? 40.433  5.237   -10.118 1.00 29.75  ? 899  LYS   A N   1 
ATOM   2728 C CA  . LYS   A 1 362 ? 39.041  5.595   -9.872  1.00 30.97  ? 899  LYS   A CA  1 
ATOM   2729 C C   . LYS   A 1 362 ? 38.410  6.228   -11.106 1.00 31.11  ? 899  LYS   A C   1 
ATOM   2730 O O   . LYS   A 1 362 ? 37.209  6.056   -11.348 1.00 30.68  ? 899  LYS   A O   1 
ATOM   2731 C CB  . LYS   A 1 362 ? 38.942  6.531   -8.665  1.00 31.24  ? 899  LYS   A CB  1 
ATOM   2732 C CG  . LYS   A 1 362 ? 39.541  5.954   -7.399  1.00 32.27  ? 899  LYS   A CG  1 
ATOM   2733 C CD  . LYS   A 1 362 ? 38.789  6.417   -6.172  1.00 33.10  ? 899  LYS   A CD  1 
ATOM   2734 C CE  . LYS   A 1 362 ? 38.993  5.460   -5.006  1.00 34.16  ? 899  LYS   A CE  1 
ATOM   2735 N NZ  . LYS   A 1 362 ? 40.371  5.494   -4.440  1.00 35.76  ? 899  LYS   A NZ  1 
ATOM   2736 N N   . ARG   A 1 363 ? 39.207  6.948   -11.900 1.00 31.06  ? 900  ARG   A N   1 
ATOM   2737 C CA  . ARG   A 1 363 ? 38.721  7.465   -13.174 1.00 30.59  ? 900  ARG   A CA  1 
ATOM   2738 C C   . ARG   A 1 363 ? 38.301  6.332   -14.107 1.00 29.79  ? 900  ARG   A C   1 
ATOM   2739 O O   . ARG   A 1 363 ? 37.280  6.434   -14.797 1.00 29.45  ? 900  ARG   A O   1 
ATOM   2740 C CB  . ARG   A 1 363 ? 39.800  8.334   -13.821 1.00 33.30  ? 900  ARG   A CB  1 
ATOM   2741 C CG  . ARG   A 1 363 ? 39.539  8.709   -15.268 1.00 36.61  ? 900  ARG   A CG  1 
ATOM   2742 C CD  . ARG   A 1 363 ? 40.841  8.762   -16.068 1.00 40.42  ? 900  ARG   A CD  1 
ATOM   2743 N NE  . ARG   A 1 363 ? 41.823  9.649   -15.451 1.00 42.43  ? 900  ARG   A NE  1 
ATOM   2744 C CZ  . ARG   A 1 363 ? 43.012  9.924   -15.977 1.00 44.95  ? 900  ARG   A CZ  1 
ATOM   2745 N NH1 . ARG   A 1 363 ? 43.369  9.381   -17.137 1.00 46.97  ? 900  ARG   A NH1 1 
ATOM   2746 N NH2 . ARG   A 1 363 ? 43.844  10.746  -15.350 1.00 45.11  ? 900  ARG   A NH2 1 
ATOM   2747 N N   . LYS   A 1 364 ? 39.067  5.237   -14.134 1.00 29.76  ? 901  LYS   A N   1 
ATOM   2748 C CA  . LYS   A 1 364 ? 38.743  4.133   -15.036 1.00 30.34  ? 901  LYS   A CA  1 
ATOM   2749 C C   . LYS   A 1 364 ? 37.485  3.399   -14.591 1.00 30.02  ? 901  LYS   A C   1 
ATOM   2750 O O   . LYS   A 1 364 ? 36.677  2.981   -15.429 1.00 30.30  ? 901  LYS   A O   1 
ATOM   2751 C CB  . LYS   A 1 364 ? 39.921  3.165   -15.138 1.00 31.13  ? 901  LYS   A CB  1 
ATOM   2752 C CG  . LYS   A 1 364 ? 41.074  3.686   -15.984 1.00 33.26  ? 901  LYS   A CG  1 
ATOM   2753 C CD  . LYS   A 1 364 ? 42.252  2.714   -16.022 1.00 33.75  ? 901  LYS   A CD  1 
ATOM   2754 C CE  . LYS   A 1 364 ? 42.752  2.545   -17.449 1.00 34.97  ? 901  LYS   A CE  1 
ATOM   2755 N NZ  . LYS   A 1 364 ? 44.073  1.862   -17.516 1.00 36.88  ? 901  LYS   A NZ  1 
ATOM   2756 N N   . ILE   A 1 365 ? 37.310  3.220   -13.280 1.00 28.38  ? 902  ILE   A N   1 
ATOM   2757 C CA  . ILE   A 1 365 ? 36.083  2.620   -12.761 1.00 26.15  ? 902  ILE   A CA  1 
ATOM   2758 C C   . ILE   A 1 365 ? 34.875  3.436   -13.193 1.00 24.57  ? 902  ILE   A C   1 
ATOM   2759 O O   . ILE   A 1 365 ? 33.909  2.901   -13.751 1.00 23.23  ? 902  ILE   A O   1 
ATOM   2760 C CB  . ILE   A 1 365 ? 36.153  2.498   -11.229 1.00 25.63  ? 902  ILE   A CB  1 
ATOM   2761 C CG1 . ILE   A 1 365 ? 37.185  1.442   -10.825 1.00 25.93  ? 902  ILE   A CG1 1 
ATOM   2762 C CG2 . ILE   A 1 365 ? 34.766  2.200   -10.645 1.00 24.70  ? 902  ILE   A CG2 1 
ATOM   2763 C CD1 . ILE   A 1 365 ? 37.495  1.440   -9.345  1.00 25.67  ? 902  ILE   A CD1 1 
ATOM   2764 N N   . LEU   A 1 366 ? 34.921  4.750   -12.948 1.00 26.54  ? 903  LEU   A N   1 
ATOM   2765 C CA  . LEU   A 1 366 ? 33.817  5.624   -13.326 1.00 21.83  ? 903  LEU   A CA  1 
ATOM   2766 C C   . LEU   A 1 366 ? 33.521  5.543   -14.819 1.00 25.51  ? 903  LEU   A C   1 
ATOM   2767 O O   . LEU   A 1 366 ? 32.352  5.494   -15.222 1.00 24.53  ? 903  LEU   A O   1 
ATOM   2768 C CB  . LEU   A 1 366 ? 34.134  7.061   -12.923 1.00 31.95  ? 903  LEU   A CB  1 
ATOM   2769 C CG  . LEU   A 1 366 ? 33.181  8.122   -13.474 1.00 21.16  ? 903  LEU   A CG  1 
ATOM   2770 C CD1 . LEU   A 1 366 ? 31.766  7.936   -12.920 1.00 20.38  ? 903  LEU   A CD1 1 
ATOM   2771 C CD2 . LEU   A 1 366 ? 33.704  9.512   -13.172 1.00 21.14  ? 903  LEU   A CD2 1 
ATOM   2772 N N   . ASP   A 1 367 ? 34.563  5.519   -15.657 1.00 23.58  ? 904  ASP   A N   1 
ATOM   2773 C CA  . ASP   A 1 367 ? 34.339  5.559   -17.100 1.00 28.30  ? 904  ASP   A CA  1 
ATOM   2774 C C   . ASP   A 1 367 ? 33.711  4.268   -17.601 1.00 29.65  ? 904  ASP   A C   1 
ATOM   2775 O O   . ASP   A 1 367 ? 32.851  4.295   -18.489 1.00 29.72  ? 904  ASP   A O   1 
ATOM   2776 C CB  . ASP   A 1 367 ? 35.645  5.857   -17.832 1.00 28.25  ? 904  ASP   A CB  1 
ATOM   2777 C CG  . ASP   A 1 367 ? 35.908  7.343   -17.933 1.00 27.86  ? 904  ASP   A CG  1 
ATOM   2778 O OD1 . ASP   A 1 367 ? 34.922  8.109   -17.854 1.00 26.39  ? 904  ASP   A OD1 1 
ATOM   2779 O OD2 . ASP   A 1 367 ? 37.078  7.748   -18.084 1.00 27.98  ? 904  ASP   A OD2 1 
ATOM   2780 N N   . GLU   A 1 368 ? 34.112  3.130   -17.038 1.00 31.50  ? 905  GLU   A N   1 
ATOM   2781 C CA  . GLU   A 1 368 ? 33.418  1.887   -17.345 1.00 33.59  ? 905  GLU   A CA  1 
ATOM   2782 C C   . GLU   A 1 368 ? 31.940  1.980   -16.986 1.00 31.27  ? 905  GLU   A C   1 
ATOM   2783 O O   . GLU   A 1 368 ? 31.081  1.535   -17.755 1.00 32.30  ? 905  GLU   A O   1 
ATOM   2784 C CB  . GLU   A 1 368 ? 34.075  0.727   -16.608 1.00 36.82  ? 905  GLU   A CB  1 
ATOM   2785 C CG  . GLU   A 1 368 ? 33.324  -0.578  -16.721 1.00 40.25  ? 905  GLU   A CG  1 
ATOM   2786 C CD  . GLU   A 1 368 ? 34.203  -1.761  -16.411 1.00 44.31  ? 905  GLU   A CD  1 
ATOM   2787 O OE1 . GLU   A 1 368 ? 34.469  -2.040  -15.218 1.00 45.07  ? 905  GLU   A OE1 1 
ATOM   2788 O OE2 . GLU   A 1 368 ? 34.645  -2.400  -17.383 1.00 46.20  ? 905  GLU   A OE2 1 
ATOM   2789 N N   . ALA   A 1 369 ? 31.626  2.554   -15.821 1.00 28.37  ? 906  ALA   A N   1 
ATOM   2790 C CA  . ALA   A 1 369 ? 30.231  2.705   -15.413 1.00 26.43  ? 906  ALA   A CA  1 
ATOM   2791 C C   . ALA   A 1 369 ? 29.469  3.601   -16.383 1.00 27.30  ? 906  ALA   A C   1 
ATOM   2792 O O   . ALA   A 1 369 ? 28.334  3.295   -16.766 1.00 27.94  ? 906  ALA   A O   1 
ATOM   2793 C CB  . ALA   A 1 369 ? 30.153  3.263   -13.990 1.00 23.65  ? 906  ALA   A CB  1 
ATOM   2794 N N   . VAL   A 1 370 ? 30.083  4.716   -16.789 1.00 28.21  ? 907  VAL   A N   1 
ATOM   2795 C CA  . VAL   A 1 370 ? 29.427  5.638   -17.715 1.00 29.91  ? 907  VAL   A CA  1 
ATOM   2796 C C   . VAL   A 1 370 ? 29.128  4.940   -19.032 1.00 32.87  ? 907  VAL   A C   1 
ATOM   2797 O O   . VAL   A 1 370 ? 28.079  5.163   -19.652 1.00 32.22  ? 907  VAL   A O   1 
ATOM   2798 C CB  . VAL   A 1 370 ? 30.300  6.890   -17.929 1.00 29.94  ? 907  VAL   A CB  1 
ATOM   2799 C CG1 . VAL   A 1 370 ? 29.799  7.700   -19.120 1.00 30.87  ? 907  VAL   A CG1 1 
ATOM   2800 C CG2 . VAL   A 1 370 ? 30.313  7.745   -16.672 1.00 28.85  ? 907  VAL   A CG2 1 
ATOM   2801 N N   . GLU   A 1 371 ? 30.040  4.075   -19.476 1.00 36.41  ? 908  GLU   A N   1 
ATOM   2802 C CA  . GLU   A 1 371 ? 29.861  3.379   -20.740 1.00 39.27  ? 908  GLU   A CA  1 
ATOM   2803 C C   . GLU   A 1 371 ? 28.736  2.355   -20.685 1.00 37.09  ? 908  GLU   A C   1 
ATOM   2804 O O   . GLU   A 1 371 ? 28.251  1.943   -21.742 1.00 37.89  ? 908  GLU   A O   1 
ATOM   2805 C CB  . GLU   A 1 371 ? 31.174  2.713   -21.156 1.00 44.50  ? 908  GLU   A CB  1 
ATOM   2806 C CG  . GLU   A 1 371 ? 32.276  3.709   -21.523 1.00 50.82  ? 908  GLU   A CG  1 
ATOM   2807 C CD  . GLU   A 1 371 ? 33.652  3.075   -21.535 1.00 57.37  ? 908  GLU   A CD  1 
ATOM   2808 O OE1 . GLU   A 1 371 ? 34.652  3.796   -21.746 1.00 58.64  ? 908  GLU   A OE1 1 
ATOM   2809 O OE2 . GLU   A 1 371 ? 33.729  1.848   -21.325 1.00 61.92  ? 908  GLU   A OE2 1 
ATOM   2810 N N   . LEU   A 1 372 ? 28.307  1.937   -19.489 1.00 35.24  ? 909  LEU   A N   1 
ATOM   2811 C CA  . LEU   A 1 372 ? 27.129  1.076   -19.394 1.00 35.07  ? 909  LEU   A CA  1 
ATOM   2812 C C   . LEU   A 1 372 ? 25.941  1.687   -20.115 1.00 25.88  ? 909  LEU   A C   1 
ATOM   2813 O O   . LEU   A 1 372 ? 25.144  0.972   -20.726 1.00 26.74  ? 909  LEU   A O   1 
ATOM   2814 C CB  . LEU   A 1 372 ? 26.759  0.812   -17.929 1.00 29.90  ? 909  LEU   A CB  1 
ATOM   2815 C CG  . LEU   A 1 372 ? 27.542  -0.248  -17.150 1.00 27.07  ? 909  LEU   A CG  1 
ATOM   2816 C CD1 . LEU   A 1 372 ? 27.095  -0.249  -15.704 1.00 25.71  ? 909  LEU   A CD1 1 
ATOM   2817 C CD2 . LEU   A 1 372 ? 27.382  -1.625  -17.765 1.00 26.93  ? 909  LEU   A CD2 1 
ATOM   2818 N N   . SER   A 1 373 ? 25.808  3.009   -20.060 1.00 25.22  ? 910  SER   A N   1 
ATOM   2819 C CA  . SER   A 1 373 ? 24.629  3.681   -20.587 1.00 29.29  ? 910  SER   A CA  1 
ATOM   2820 C C   . SER   A 1 373 ? 24.718  3.989   -22.072 1.00 31.23  ? 910  SER   A C   1 
ATOM   2821 O O   . SER   A 1 373 ? 23.688  4.278   -22.688 1.00 32.69  ? 910  SER   A O   1 
ATOM   2822 C CB  . SER   A 1 373 ? 24.379  4.985   -19.823 1.00 28.12  ? 910  SER   A CB  1 
ATOM   2823 O OG  . SER   A 1 373 ? 25.507  5.840   -19.901 1.00 27.58  ? 910  SER   A OG  1 
ATOM   2824 N N   . GLN   A 1 374 ? 25.906  3.938   -22.662 1.00 32.47  ? 911  GLN   A N   1 
ATOM   2825 C CA  . GLN   A 1 374 ? 26.057  4.385   -24.037 1.00 36.23  ? 911  GLN   A CA  1 
ATOM   2826 C C   . GLN   A 1 374 ? 25.401  3.402   -24.999 1.00 38.04  ? 911  GLN   A C   1 
ATOM   2827 O O   . GLN   A 1 374 ? 25.255  2.211   -24.702 1.00 37.88  ? 911  GLN   A O   1 
ATOM   2828 C CB  . GLN   A 1 374 ? 27.538  4.573   -24.373 1.00 39.46  ? 911  GLN   A CB  1 
ATOM   2829 C CG  . GLN   A 1 374 ? 28.171  5.774   -23.673 1.00 41.05  ? 911  GLN   A CG  1 
ATOM   2830 C CD  . GLN   A 1 374 ? 29.669  5.618   -23.466 1.00 44.07  ? 911  GLN   A CD  1 
ATOM   2831 O OE1 . GLN   A 1 374 ? 30.274  4.642   -23.911 1.00 46.04  ? 911  GLN   A OE1 1 
ATOM   2832 N NE2 . GLN   A 1 374 ? 30.273  6.580   -22.778 1.00 44.30  ? 911  GLN   A NE2 1 
ATOM   2833 N N   A ASP   A 1 375 ? 25.000  3.921   -26.164 0.49 39.12  ? 912  ASP   A N   1 
ATOM   2834 N N   B ASP   A 1 375 ? 25.014  3.921   -26.170 0.51 39.15  ? 912  ASP   A N   1 
ATOM   2835 C CA  A ASP   A 1 375 ? 24.325  3.133   -27.197 0.49 40.61  ? 912  ASP   A CA  1 
ATOM   2836 C CA  B ASP   A 1 375 ? 24.317  3.150   -27.202 0.51 40.81  ? 912  ASP   A CA  1 
ATOM   2837 C C   A ASP   A 1 375 ? 23.036  2.513   -26.657 0.49 40.28  ? 912  ASP   A C   1 
ATOM   2838 C C   B ASP   A 1 375 ? 23.045  2.513   -26.641 0.51 40.26  ? 912  ASP   A C   1 
ATOM   2839 O O   A ASP   A 1 375 ? 22.794  1.312   -26.792 0.49 41.23  ? 912  ASP   A O   1 
ATOM   2840 O O   B ASP   A 1 375 ? 22.824  1.305   -26.746 0.51 41.16  ? 912  ASP   A O   1 
ATOM   2841 C CB  A ASP   A 1 375 ? 25.254  2.058   -27.771 0.49 41.67  ? 912  ASP   A CB  1 
ATOM   2842 C CB  B ASP   A 1 375 ? 25.235  2.095   -27.828 0.51 41.73  ? 912  ASP   A CB  1 
ATOM   2843 C CG  A ASP   A 1 375 ? 26.483  2.642   -28.441 0.49 42.58  ? 912  ASP   A CG  1 
ATOM   2844 C CG  B ASP   A 1 375 ? 24.675  1.527   -29.117 0.51 43.41  ? 912  ASP   A CG  1 
ATOM   2845 O OD1 A ASP   A 1 375 ? 26.327  3.576   -29.255 0.49 43.26  ? 912  ASP   A OD1 1 
ATOM   2846 O OD1 B ASP   A 1 375 ? 23.756  2.148   -29.689 0.51 43.39  ? 912  ASP   A OD1 1 
ATOM   2847 O OD2 A ASP   A 1 375 ? 27.605  2.171   -28.153 0.49 42.44  ? 912  ASP   A OD2 1 
ATOM   2848 O OD2 B ASP   A 1 375 ? 25.149  0.455   -29.552 0.51 44.16  ? 912  ASP   A OD2 1 
ATOM   2849 N N   . HIS   A 1 376 ? 22.209  3.350   -26.030 1.00 39.48  ? 913  HIS   A N   1 
ATOM   2850 C CA  . HIS   A 1 376 ? 20.919  2.932   -25.480 1.00 40.38  ? 913  HIS   A CA  1 
ATOM   2851 C C   . HIS   A 1 376 ? 21.079  1.771   -24.499 1.00 39.04  ? 913  HIS   A C   1 
ATOM   2852 O O   . HIS   A 1 376 ? 20.344  0.783   -24.539 1.00 40.31  ? 913  HIS   A O   1 
ATOM   2853 C CB  . HIS   A 1 376 ? 19.934  2.587   -26.600 1.00 45.11  ? 913  HIS   A CB  1 
ATOM   2854 C CG  . HIS   A 1 376 ? 19.652  3.731   -27.524 1.00 48.18  ? 913  HIS   A CG  1 
ATOM   2855 N ND1 . HIS   A 1 376 ? 18.917  4.833   -27.140 1.00 47.90  ? 913  HIS   A ND1 1 
ATOM   2856 C CD2 . HIS   A 1 376 ? 20.005  3.946   -28.814 1.00 50.58  ? 913  HIS   A CD2 1 
ATOM   2857 C CE1 . HIS   A 1 376 ? 18.833  5.677   -28.152 1.00 49.63  ? 913  HIS   A CE1 1 
ATOM   2858 N NE2 . HIS   A 1 376 ? 19.484  5.163   -29.180 1.00 50.71  ? 913  HIS   A NE2 1 
ATOM   2859 N N   . PHE   A 1 377 ? 22.075  1.895   -23.619 1.00 37.33  ? 914  PHE   A N   1 
ATOM   2860 C CA  . PHE   A 1 377 ? 22.324  0.924   -22.548 1.00 36.23  ? 914  PHE   A CA  1 
ATOM   2861 C C   . PHE   A 1 377 ? 22.606  -0.469  -23.105 1.00 37.64  ? 914  PHE   A C   1 
ATOM   2862 O O   . PHE   A 1 377 ? 22.183  -1.480  -22.541 1.00 37.34  ? 914  PHE   A O   1 
ATOM   2863 C CB  . PHE   A 1 377 ? 21.166  0.892   -21.550 1.00 34.13  ? 914  PHE   A CB  1 
ATOM   2864 C CG  . PHE   A 1 377 ? 21.002  2.170   -20.784 1.00 32.24  ? 914  PHE   A CG  1 
ATOM   2865 C CD1 . PHE   A 1 377 ? 20.416  3.278   -21.376 1.00 31.71  ? 914  PHE   A CD1 1 
ATOM   2866 C CD2 . PHE   A 1 377 ? 21.434  2.265   -19.473 1.00 29.94  ? 914  PHE   A CD2 1 
ATOM   2867 C CE1 . PHE   A 1 377 ? 20.265  4.456   -20.674 1.00 30.26  ? 914  PHE   A CE1 1 
ATOM   2868 C CE2 . PHE   A 1 377 ? 21.287  3.439   -18.768 1.00 28.72  ? 914  PHE   A CE2 1 
ATOM   2869 C CZ  . PHE   A 1 377 ? 20.701  4.538   -19.369 1.00 28.66  ? 914  PHE   A CZ  1 
ATOM   2870 N N   . LYS   A 1 378 ? 23.337  -0.518  -24.219 1.00 39.90  ? 915  LYS   A N   1 
ATOM   2871 C CA  . LYS   A 1 378 ? 23.683  -1.797  -24.828 1.00 42.59  ? 915  LYS   A CA  1 
ATOM   2872 C C   . LYS   A 1 378 ? 24.504  -2.656  -23.872 1.00 41.47  ? 915  LYS   A C   1 
ATOM   2873 O O   . LYS   A 1 378 ? 24.183  -3.828  -23.642 1.00 42.53  ? 915  LYS   A O   1 
ATOM   2874 C CB  . LYS   A 1 378 ? 24.438  -1.561  -26.138 1.00 45.84  ? 915  LYS   A CB  1 
ATOM   2875 C CG  . LYS   A 1 378 ? 25.077  -2.809  -26.738 1.00 48.99  ? 915  LYS   A CG  1 
ATOM   2876 C CD  . LYS   A 1 378 ? 26.069  -2.431  -27.830 1.00 50.86  ? 915  LYS   A CD  1 
ATOM   2877 C CE  . LYS   A 1 378 ? 26.883  -3.626  -28.296 1.00 52.72  ? 915  LYS   A CE  1 
ATOM   2878 N NZ  . LYS   A 1 378 ? 26.083  -4.561  -29.133 1.00 54.64  ? 915  LYS   A NZ  1 
ATOM   2879 N N   . LYS   A 1 379 ? 25.564  -2.085  -23.292 1.00 39.00  ? 916  LYS   A N   1 
ATOM   2880 C CA  . LYS   A 1 379 ? 26.404  -2.859  -22.383 1.00 37.84  ? 916  LYS   A CA  1 
ATOM   2881 C C   . LYS   A 1 379 ? 25.693  -3.157  -21.069 1.00 36.24  ? 916  LYS   A C   1 
ATOM   2882 O O   . LYS   A 1 379 ? 25.917  -4.216  -20.471 1.00 37.18  ? 916  LYS   A O   1 
ATOM   2883 C CB  . LYS   A 1 379 ? 27.715  -2.123  -22.120 1.00 37.80  ? 916  LYS   A CB  1 
ATOM   2884 C CG  . LYS   A 1 379 ? 28.723  -2.225  -23.250 1.00 40.30  ? 916  LYS   A CG  1 
ATOM   2885 C CD  . LYS   A 1 379 ? 29.933  -1.341  -22.971 1.00 40.73  ? 916  LYS   A CD  1 
ATOM   2886 C CE  . LYS   A 1 379 ? 31.013  -1.519  -24.026 1.00 42.31  ? 916  LYS   A CE  1 
ATOM   2887 N NZ  . LYS   A 1 379 ? 32.179  -0.627  -23.769 1.00 41.41  ? 916  LYS   A NZ  1 
ATOM   2888 N N   . TYR   A 1 380 ? 24.844  -2.241  -20.598 1.00 33.73  ? 917  TYR   A N   1 
ATOM   2889 C CA  . TYR   A 1 380 ? 24.104  -2.502  -19.368 1.00 32.56  ? 917  TYR   A CA  1 
ATOM   2890 C C   . TYR   A 1 380 ? 23.198  -3.713  -19.519 1.00 34.03  ? 917  TYR   A C   1 
ATOM   2891 O O   . TYR   A 1 380 ? 23.065  -4.519  -18.590 1.00 33.66  ? 917  TYR   A O   1 
ATOM   2892 C CB  . TYR   A 1 380 ? 23.276  -1.283  -18.964 1.00 31.43  ? 917  TYR   A CB  1 
ATOM   2893 C CG  . TYR   A 1 380 ? 22.180  -1.622  -17.977 1.00 30.25  ? 917  TYR   A CG  1 
ATOM   2894 C CD1 . TYR   A 1 380 ? 22.486  -2.016  -16.681 1.00 28.27  ? 917  TYR   A CD1 1 
ATOM   2895 C CD2 . TYR   A 1 380 ? 20.842  -1.557  -18.345 1.00 26.11  ? 917  TYR   A CD2 1 
ATOM   2896 C CE1 . TYR   A 1 380 ? 21.497  -2.332  -15.779 1.00 24.67  ? 917  TYR   A CE1 1 
ATOM   2897 C CE2 . TYR   A 1 380 ? 19.844  -1.869  -17.449 1.00 25.76  ? 917  TYR   A CE2 1 
ATOM   2898 C CZ  . TYR   A 1 380 ? 20.179  -2.259  -16.165 1.00 29.08  ? 917  TYR   A CZ  1 
ATOM   2899 O OH  . TYR   A 1 380 ? 19.194  -2.578  -15.259 1.00 24.86  ? 917  TYR   A OH  1 
ATOM   2900 N N   . LEU   A 1 381 ? 22.572  -3.864  -20.686 1.00 36.64  ? 918  LEU   A N   1 
ATOM   2901 C CA  . LEU   A 1 381 ? 21.574  -4.912  -20.851 1.00 39.55  ? 918  LEU   A CA  1 
ATOM   2902 C C   . LEU   A 1 381 ? 22.204  -6.298  -20.890 1.00 42.65  ? 918  LEU   A C   1 
ATOM   2903 O O   . LEU   A 1 381 ? 21.588  -7.267  -20.429 1.00 43.05  ? 918  LEU   A O   1 
ATOM   2904 C CB  . LEU   A 1 381 ? 20.748  -4.651  -22.110 1.00 41.21  ? 918  LEU   A CB  1 
ATOM   2905 C CG  . LEU   A 1 381 ? 19.722  -3.524  -21.953 1.00 40.76  ? 918  LEU   A CG  1 
ATOM   2906 C CD1 . LEU   A 1 381 ? 19.166  -3.088  -23.299 1.00 42.55  ? 918  LEU   A CD1 1 
ATOM   2907 C CD2 . LEU   A 1 381 ? 18.598  -3.953  -21.022 1.00 39.98  ? 918  LEU   A CD2 1 
ATOM   2908 N N   . VAL   A 1 382 ? 23.423  -6.417  -21.420 1.00 44.44  ? 919  VAL   A N   1 
ATOM   2909 C CA  . VAL   A 1 382 ? 24.067  -7.726  -21.426 1.00 46.51  ? 919  VAL   A CA  1 
ATOM   2910 C C   . VAL   A 1 382 ? 24.593  -8.073  -20.037 1.00 45.64  ? 919  VAL   A C   1 
ATOM   2911 O O   . VAL   A 1 382 ? 24.688  -9.254  -19.686 1.00 47.35  ? 919  VAL   A O   1 
ATOM   2912 C CB  . VAL   A 1 382 ? 25.179  -7.799  -22.492 1.00 47.48  ? 919  VAL   A CB  1 
ATOM   2913 C CG1 . VAL   A 1 382 ? 24.718  -7.152  -23.791 1.00 48.43  ? 919  VAL   A CG1 1 
ATOM   2914 C CG2 . VAL   A 1 382 ? 26.474  -7.167  -21.997 1.00 46.30  ? 919  VAL   A CG2 1 
ATOM   2915 N N   . LYS   A 1 383 ? 24.920  -7.069  -19.218 1.00 43.41  ? 920  LYS   A N   1 
ATOM   2916 C CA  . LYS   A 1 383 ? 25.407  -7.359  -17.873 1.00 42.67  ? 920  LYS   A CA  1 
ATOM   2917 C C   . LYS   A 1 383 ? 24.269  -7.678  -16.915 1.00 42.03  ? 920  LYS   A C   1 
ATOM   2918 O O   . LYS   A 1 383 ? 24.457  -8.460  -15.976 1.00 41.78  ? 920  LYS   A O   1 
ATOM   2919 C CB  . LYS   A 1 383 ? 26.228  -6.190  -17.331 1.00 41.73  ? 920  LYS   A CB  1 
ATOM   2920 C CG  . LYS   A 1 383 ? 27.057  -6.578  -16.122 1.00 42.65  ? 920  LYS   A CG  1 
ATOM   2921 C CD  . LYS   A 1 383 ? 27.905  -5.432  -15.618 1.00 42.57  ? 920  LYS   A CD  1 
ATOM   2922 C CE  . LYS   A 1 383 ? 28.787  -5.878  -14.464 1.00 43.45  ? 920  LYS   A CE  1 
ATOM   2923 N NZ  . LYS   A 1 383 ? 29.447  -4.719  -13.801 1.00 43.38  ? 920  LYS   A NZ  1 
ATOM   2924 N N   . LEU   A 1 384 ? 23.092  -7.085  -17.131 1.00 40.89  ? 921  LEU   A N   1 
ATOM   2925 C CA  . LEU   A 1 384 ? 21.931  -7.451  -16.329 1.00 39.96  ? 921  LEU   A CA  1 
ATOM   2926 C C   . LEU   A 1 384 ? 21.556  -8.913  -16.544 1.00 42.57  ? 921  LEU   A C   1 
ATOM   2927 O O   . LEU   A 1 384 ? 21.226  -9.625  -15.589 1.00 42.59  ? 921  LEU   A O   1 
ATOM   2928 C CB  . LEU   A 1 384 ? 20.753  -6.539  -16.666 1.00 37.31  ? 921  LEU   A CB  1 
ATOM   2929 C CG  . LEU   A 1 384 ? 19.429  -6.910  -16.000 1.00 36.68  ? 921  LEU   A CG  1 
ATOM   2930 C CD1 . LEU   A 1 384 ? 19.572  -6.841  -14.494 1.00 35.26  ? 921  LEU   A CD1 1 
ATOM   2931 C CD2 . LEU   A 1 384 ? 18.289  -6.016  -16.483 1.00 36.65  ? 921  LEU   A CD2 1 
ATOM   2932 N N   . LYS   A 1 385 ? 21.617  -9.383  -17.791 1.00 45.37  ? 922  LYS   A N   1 
ATOM   2933 C CA  . LYS   A 1 385 ? 21.233  -10.753 -18.102 1.00 48.02  ? 922  LYS   A CA  1 
ATOM   2934 C C   . LYS   A 1 385 ? 22.206  -11.786 -17.554 1.00 47.64  ? 922  LYS   A C   1 
ATOM   2935 O O   . LYS   A 1 385 ? 21.892  -12.980 -17.596 1.00 49.74  ? 922  LYS   A O   1 
ATOM   2936 C CB  . LYS   A 1 385 ? 21.103  -10.936 -19.616 1.00 51.88  ? 922  LYS   A CB  1 
ATOM   2937 C CG  . LYS   A 1 385 ? 19.936  -10.184 -20.241 1.00 54.45  ? 922  LYS   A CG  1 
ATOM   2938 C CD  . LYS   A 1 385 ? 19.746  -10.545 -21.715 1.00 58.54  ? 922  LYS   A CD  1 
ATOM   2939 C CE  . LYS   A 1 385 ? 18.511  -9.861  -22.290 1.00 60.16  ? 922  LYS   A CE  1 
ATOM   2940 N NZ  . LYS   A 1 385 ? 18.330  -10.125 -23.745 1.00 63.18  ? 922  LYS   A NZ  1 
ATOM   2941 N N   . SER   A 1 386 ? 23.364  -11.370 -17.040 1.00 45.38  ? 923  SER   A N   1 
ATOM   2942 C CA  . SER   A 1 386 ? 24.407  -12.308 -16.644 1.00 45.93  ? 923  SER   A CA  1 
ATOM   2943 C C   . SER   A 1 386 ? 24.728  -12.263 -15.156 1.00 45.70  ? 923  SER   A C   1 
ATOM   2944 O O   . SER   A 1 386 ? 25.679  -12.922 -14.722 1.00 46.80  ? 923  SER   A O   1 
ATOM   2945 C CB  . SER   A 1 386 ? 25.684  -12.058 -17.455 1.00 45.43  ? 923  SER   A CB  1 
ATOM   2946 O OG  . SER   A 1 386 ? 26.449  -10.994 -16.912 1.00 43.33  ? 923  SER   A OG  1 
ATOM   2947 N N   . ILE   A 1 387 ? 23.975  -11.524 -14.361 1.00 44.96  ? 924  ILE   A N   1 
ATOM   2948 C CA  . ILE   A 1 387 ? 24.261  -11.430 -12.935 1.00 45.39  ? 924  ILE   A CA  1 
ATOM   2949 C C   . ILE   A 1 387 ? 23.286  -12.307 -12.167 1.00 45.57  ? 924  ILE   A C   1 
ATOM   2950 O O   . ILE   A 1 387 ? 22.124  -12.477 -12.553 1.00 45.16  ? 924  ILE   A O   1 
ATOM   2951 C CB  . ILE   A 1 387 ? 24.215  -9.971  -12.431 1.00 44.78  ? 924  ILE   A CB  1 
ATOM   2952 C CG1 . ILE   A 1 387 ? 22.982  -9.247  -12.973 1.00 44.76  ? 924  ILE   A CG1 1 
ATOM   2953 C CG2 . ILE   A 1 387 ? 25.506  -9.239  -12.786 1.00 44.83  ? 924  ILE   A CG2 1 
ATOM   2954 C CD1 . ILE   A 1 387 ? 21.773  -9.335  -12.070 1.00 44.39  ? 924  ILE   A CD1 1 
ATOM   2955 N N   . ASN   A 1 388 ? 23.777  -12.877 -11.060 1.00 46.03  ? 925  ASN   A N   1 
ATOM   2956 C CA  . ASN   A 1 388 ? 22.987  -13.669 -10.136 1.00 46.74  ? 925  ASN   A CA  1 
ATOM   2957 C C   . ASN   A 1 388 ? 22.355  -12.770 -9.078  1.00 46.21  ? 925  ASN   A C   1 
ATOM   2958 O O   . ASN   A 1 388 ? 22.926  -11.736 -8.709  1.00 44.76  ? 925  ASN   A O   1 
ATOM   2959 C CB  . ASN   A 1 388 ? 23.856  -14.723 -9.453  1.00 47.73  ? 925  ASN   A CB  1 
ATOM   2960 C CG  . ASN   A 1 388 ? 24.450  -15.719 -10.432 1.00 49.64  ? 925  ASN   A CG  1 
ATOM   2961 O OD1 . ASN   A 1 388 ? 23.800  -16.134 -11.392 1.00 50.83  ? 925  ASN   A OD1 1 
ATOM   2962 N ND2 . ASN   A 1 388 ? 25.696  -16.109 -10.189 1.00 49.98  ? 925  ASN   A ND2 1 
ATOM   2963 N N   . PRO   A 1 389 ? 21.175  -13.135 -8.588  1.00 46.76  ? 926  PRO   A N   1 
ATOM   2964 C CA  . PRO   A 1 389 ? 20.545  -12.370 -7.507  1.00 44.22  ? 926  PRO   A CA  1 
ATOM   2965 C C   . PRO   A 1 389 ? 21.396  -12.404 -6.250  1.00 42.64  ? 926  PRO   A C   1 
ATOM   2966 O O   . PRO   A 1 389 ? 22.259  -13.284 -6.100  1.00 43.88  ? 926  PRO   A O   1 
ATOM   2967 C CB  . PRO   A 1 389 ? 19.209  -13.099 -7.296  1.00 46.80  ? 926  PRO   A CB  1 
ATOM   2968 C CG  . PRO   A 1 389 ? 18.950  -13.802 -8.596  1.00 48.99  ? 926  PRO   A CG  1 
ATOM   2969 C CD  . PRO   A 1 389 ? 20.301  -14.206 -9.097  1.00 49.15  ? 926  PRO   A CD  1 
ATOM   2970 N N   . PRO   A 1 390 ? 21.193  -11.455 -5.316  1.00 39.94  ? 927  PRO   A N   1 
ATOM   2971 C CA  . PRO   A 1 390 ? 20.261  -10.319 -5.412  1.00 38.18  ? 927  PRO   A CA  1 
ATOM   2972 C C   . PRO   A 1 390 ? 20.774  -9.168  -6.285  1.00 36.36  ? 927  PRO   A C   1 
ATOM   2973 O O   . PRO   A 1 390 ? 21.981  -9.033  -6.493  1.00 37.26  ? 927  PRO   A O   1 
ATOM   2974 C CB  . PRO   A 1 390 ? 20.115  -9.863  -3.955  1.00 37.71  ? 927  PRO   A CB  1 
ATOM   2975 C CG  . PRO   A 1 390 ? 21.390  -10.272 -3.302  1.00 38.24  ? 927  PRO   A CG  1 
ATOM   2976 C CD  . PRO   A 1 390 ? 21.809  -11.555 -3.980  1.00 39.84  ? 927  PRO   A CD  1 
ATOM   2977 N N   . CYS   A 1 391 ? 19.862  -8.342  -6.790  1.00 34.20  ? 928  CYS   A N   1 
ATOM   2978 C CA  . CYS   A 1 391 ? 20.261  -7.201  -7.603  1.00 33.56  ? 928  CYS   A CA  1 
ATOM   2979 C C   . CYS   A 1 391 ? 19.151  -6.162  -7.578  1.00 32.94  ? 928  CYS   A C   1 
ATOM   2980 O O   . CYS   A 1 391 ? 18.005  -6.463  -7.231  1.00 34.31  ? 928  CYS   A O   1 
ATOM   2981 C CB  . CYS   A 1 391 ? 20.571  -7.623  -9.041  1.00 37.43  ? 928  CYS   A CB  1 
ATOM   2982 S SG  . CYS   A 1 391 ? 19.120  -7.759  -10.101 1.00 40.45  ? 928  CYS   A SG  1 
ATOM   2983 N N   . VAL   A 1 392 ? 19.499  -4.936  -7.947  1.00 31.04  ? 929  VAL   A N   1 
ATOM   2984 C CA  . VAL   A 1 392 ? 18.530  -3.862  -8.126  1.00 30.52  ? 929  VAL   A CA  1 
ATOM   2985 C C   . VAL   A 1 392 ? 18.681  -3.309  -9.539  1.00 23.16  ? 929  VAL   A C   1 
ATOM   2986 O O   . VAL   A 1 392 ? 19.628  -2.578  -9.835  1.00 22.52  ? 929  VAL   A O   1 
ATOM   2987 C CB  . VAL   A 1 392 ? 18.704  -2.751  -7.075  1.00 22.50  ? 929  VAL   A CB  1 
ATOM   2988 C CG1 . VAL   A 1 392 ? 17.700  -1.642  -7.336  1.00 22.17  ? 929  VAL   A CG1 1 
ATOM   2989 C CG2 . VAL   A 1 392 ? 18.533  -3.308  -5.670  1.00 22.93  ? 929  VAL   A CG2 1 
ATOM   2990 N N   . PRO   A 1 393 ? 17.768  -3.652  -10.448 1.00 33.99  ? 930  PRO   A N   1 
ATOM   2991 C CA  . PRO   A 1 393 ? 17.901  -3.202  -11.838 1.00 23.96  ? 930  PRO   A CA  1 
ATOM   2992 C C   . PRO   A 1 393 ? 17.708  -1.700  -11.964 1.00 28.67  ? 930  PRO   A C   1 
ATOM   2993 O O   . PRO   A 1 393 ? 17.139  -1.038  -11.093 1.00 22.65  ? 930  PRO   A O   1 
ATOM   2994 C CB  . PRO   A 1 393 ? 16.790  -3.962  -12.567 1.00 25.13  ? 930  PRO   A CB  1 
ATOM   2995 C CG  . PRO   A 1 393 ? 16.519  -5.161  -11.693 1.00 25.79  ? 930  PRO   A CG  1 
ATOM   2996 C CD  . PRO   A 1 393 ? 16.703  -4.658  -10.295 1.00 24.91  ? 930  PRO   A CD  1 
ATOM   2997 N N   . PHE   A 1 394 ? 18.216  -1.168  -13.071 1.00 28.08  ? 931  PHE   A N   1 
ATOM   2998 C CA  . PHE   A 1 394 ? 17.990  0.228   -13.411 1.00 28.59  ? 931  PHE   A CA  1 
ATOM   2999 C C   . PHE   A 1 394 ? 16.534  0.413   -13.813 1.00 31.21  ? 931  PHE   A C   1 
ATOM   3000 O O   . PHE   A 1 394 ? 16.057  -0.214  -14.766 1.00 31.92  ? 931  PHE   A O   1 
ATOM   3001 C CB  . PHE   A 1 394 ? 18.930  0.659   -14.535 1.00 27.89  ? 931  PHE   A CB  1 
ATOM   3002 C CG  . PHE   A 1 394 ? 18.635  2.027   -15.089 1.00 28.09  ? 931  PHE   A CG  1 
ATOM   3003 C CD1 . PHE   A 1 394 ? 18.620  3.142   -14.259 1.00 27.69  ? 931  PHE   A CD1 1 
ATOM   3004 C CD2 . PHE   A 1 394 ? 18.387  2.199   -16.442 1.00 28.64  ? 931  PHE   A CD2 1 
ATOM   3005 C CE1 . PHE   A 1 394 ? 18.353  4.408   -14.769 1.00 26.78  ? 931  PHE   A CE1 1 
ATOM   3006 C CE2 . PHE   A 1 394 ? 18.120  3.455   -16.965 1.00 28.51  ? 931  PHE   A CE2 1 
ATOM   3007 C CZ  . PHE   A 1 394 ? 18.104  4.565   -16.127 1.00 28.20  ? 931  PHE   A CZ  1 
ATOM   3008 N N   . PHE   A 1 395 ? 15.826  1.273   -13.085 1.00 32.70  ? 932  PHE   A N   1 
ATOM   3009 C CA  . PHE   A 1 395 ? 14.390  1.395   -13.285 1.00 36.26  ? 932  PHE   A CA  1 
ATOM   3010 C C   . PHE   A 1 395 ? 14.037  2.257   -14.491 1.00 36.99  ? 932  PHE   A C   1 
ATOM   3011 O O   . PHE   A 1 395 ? 12.956  2.089   -15.065 1.00 38.67  ? 932  PHE   A O   1 
ATOM   3012 C CB  . PHE   A 1 395 ? 13.745  1.956   -12.021 1.00 38.95  ? 932  PHE   A CB  1 
ATOM   3013 C CG  . PHE   A 1 395 ? 12.307  1.594   -11.874 1.00 43.05  ? 932  PHE   A CG  1 
ATOM   3014 C CD1 . PHE   A 1 395 ? 11.931  0.277   -11.685 1.00 44.74  ? 932  PHE   A CD1 1 
ATOM   3015 C CD2 . PHE   A 1 395 ? 11.329  2.563   -11.924 1.00 45.28  ? 932  PHE   A CD2 1 
ATOM   3016 C CE1 . PHE   A 1 395 ? 10.604  -0.066  -11.553 1.00 46.88  ? 932  PHE   A CE1 1 
ATOM   3017 C CE2 . PHE   A 1 395 ? 10.008  2.225   -11.790 1.00 47.38  ? 932  PHE   A CE2 1 
ATOM   3018 C CZ  . PHE   A 1 395 ? 9.639   0.910   -11.604 1.00 47.98  ? 932  PHE   A CZ  1 
ATOM   3019 N N   . GLY   A 1 396 ? 14.933  3.162   -14.898 1.00 35.96  ? 933  GLY   A N   1 
ATOM   3020 C CA  . GLY   A 1 396 ? 14.603  4.109   -15.952 1.00 35.45  ? 933  GLY   A CA  1 
ATOM   3021 C C   . GLY   A 1 396 ? 14.373  3.480   -17.314 1.00 36.27  ? 933  GLY   A C   1 
ATOM   3022 O O   . GLY   A 1 396 ? 13.671  4.050   -18.152 1.00 38.66  ? 933  GLY   A O   1 
ATOM   3023 N N   . ILE   A 1 397 ? 14.954  2.306   -17.561 1.00 35.49  ? 934  ILE   A N   1 
ATOM   3024 C CA  . ILE   A 1 397 ? 14.809  1.710   -18.884 1.00 36.91  ? 934  ILE   A CA  1 
ATOM   3025 C C   . ILE   A 1 397 ? 13.410  1.132   -19.069 1.00 38.68  ? 934  ILE   A C   1 
ATOM   3026 O O   . ILE   A 1 397 ? 12.890  1.091   -20.192 1.00 40.11  ? 934  ILE   A O   1 
ATOM   3027 C CB  . ILE   A 1 397 ? 15.908  0.657   -19.119 1.00 36.78  ? 934  ILE   A CB  1 
ATOM   3028 C CG1 . ILE   A 1 397 ? 15.745  0.018   -20.497 1.00 37.58  ? 934  ILE   A CG1 1 
ATOM   3029 C CG2 . ILE   A 1 397 ? 15.893  -0.395  -18.023 1.00 36.65  ? 934  ILE   A CG2 1 
ATOM   3030 C CD1 . ILE   A 1 397 ? 17.052  -0.310  -21.163 1.00 37.53  ? 934  ILE   A CD1 1 
ATOM   3031 N N   . TYR   A 1 398 ? 12.772  0.685   -17.988 1.00 38.48  ? 935  TYR   A N   1 
ATOM   3032 C CA  . TYR   A 1 398 ? 11.401  0.203   -18.100 1.00 39.71  ? 935  TYR   A CA  1 
ATOM   3033 C C   . TYR   A 1 398 ? 10.438  1.360   -18.316 1.00 41.23  ? 935  TYR   A C   1 
ATOM   3034 O O   . TYR   A 1 398 ? 9.570   1.305   -19.196 1.00 43.71  ? 935  TYR   A O   1 
ATOM   3035 C CB  . TYR   A 1 398 ? 11.011  -0.591  -16.853 1.00 39.30  ? 935  TYR   A CB  1 
ATOM   3036 C CG  . TYR   A 1 398 ? 11.907  -1.771  -16.572 1.00 38.98  ? 935  TYR   A CG  1 
ATOM   3037 C CD1 . TYR   A 1 398 ? 11.992  -2.830  -17.468 1.00 40.02  ? 935  TYR   A CD1 1 
ATOM   3038 C CD2 . TYR   A 1 398 ? 12.659  -1.833  -15.406 1.00 37.30  ? 935  TYR   A CD2 1 
ATOM   3039 C CE1 . TYR   A 1 398 ? 12.809  -3.909  -17.215 1.00 39.87  ? 935  TYR   A CE1 1 
ATOM   3040 C CE2 . TYR   A 1 398 ? 13.476  -2.911  -15.143 1.00 37.41  ? 935  TYR   A CE2 1 
ATOM   3041 C CZ  . TYR   A 1 398 ? 13.549  -3.946  -16.051 1.00 39.00  ? 935  TYR   A CZ  1 
ATOM   3042 O OH  . TYR   A 1 398 ? 14.366  -5.022  -15.796 1.00 40.21  ? 935  TYR   A OH  1 
ATOM   3043 N N   . LEU   A 1 399 ? 10.580  2.420   -17.517 1.00 40.53  ? 936  LEU   A N   1 
ATOM   3044 C CA  . LEU   A 1 399 ? 9.704   3.579   -17.653 1.00 41.36  ? 936  LEU   A CA  1 
ATOM   3045 C C   . LEU   A 1 399 ? 9.812   4.194   -19.042 1.00 40.81  ? 936  LEU   A C   1 
ATOM   3046 O O   . LEU   A 1 399 ? 8.811   4.639   -19.614 1.00 41.99  ? 936  LEU   A O   1 
ATOM   3047 C CB  . LEU   A 1 399 ? 10.045  4.611   -16.581 1.00 41.60  ? 936  LEU   A CB  1 
ATOM   3048 C CG  . LEU   A 1 399 ? 9.830   4.181   -15.134 1.00 41.43  ? 936  LEU   A CG  1 
ATOM   3049 C CD1 . LEU   A 1 399 ? 10.533  5.147   -14.208 1.00 40.54  ? 936  LEU   A CD1 1 
ATOM   3050 C CD2 . LEU   A 1 399 ? 8.346   4.135   -14.828 1.00 43.35  ? 936  LEU   A CD2 1 
ATOM   3051 N N   . THR   A 1 400 ? 11.021  4.224   -19.603 1.00 38.72  ? 937  THR   A N   1 
ATOM   3052 C CA  . THR   A 1 400 ? 11.198  4.787   -20.936 1.00 38.21  ? 937  THR   A CA  1 
ATOM   3053 C C   . THR   A 1 400 ? 10.576  3.890   -21.999 1.00 39.15  ? 937  THR   A C   1 
ATOM   3054 O O   . THR   A 1 400 ? 9.890   4.378   -22.905 1.00 39.96  ? 937  THR   A O   1 
ATOM   3055 C CB  . THR   A 1 400 ? 12.686  5.005   -21.217 1.00 37.79  ? 937  THR   A CB  1 
ATOM   3056 O OG1 . THR   A 1 400 ? 13.228  5.919   -20.253 1.00 36.58  ? 937  THR   A OG1 1 
ATOM   3057 C CG2 . THR   A 1 400 ? 12.890  5.569   -22.616 1.00 38.73  ? 937  THR   A CG2 1 
ATOM   3058 N N   . ASN   A 1 401 ? 10.798  2.574   -21.900 1.00 39.81  ? 938  ASN   A N   1 
ATOM   3059 C CA  . ASN   A 1 401 ? 10.271  1.652   -22.902 1.00 42.56  ? 938  ASN   A CA  1 
ATOM   3060 C C   . ASN   A 1 401 ? 8.754   1.565   -22.834 1.00 44.31  ? 938  ASN   A C   1 
ATOM   3061 O O   . ASN   A 1 401 ? 8.100   1.346   -23.860 1.00 47.00  ? 938  ASN   A O   1 
ATOM   3062 C CB  . ASN   A 1 401 ? 10.889  0.261   -22.726 1.00 43.86  ? 938  ASN   A CB  1 
ATOM   3063 C CG  . ASN   A 1 401 ? 12.383  0.222   -23.056 1.00 43.85  ? 938  ASN   A CG  1 
ATOM   3064 O OD1 . ASN   A 1 401 ? 13.056  1.251   -23.097 1.00 43.10  ? 938  ASN   A OD1 1 
ATOM   3065 N ND2 . ASN   A 1 401 ? 12.902  -0.981  -23.281 1.00 44.53  ? 938  ASN   A ND2 1 
ATOM   3066 N N   . ILE   A 1 402 ? 8.177   1.740   -21.643 1.00 43.07  ? 939  ILE   A N   1 
ATOM   3067 C CA  . ILE   A 1 402 ? 6.724   1.724   -21.512 1.00 43.81  ? 939  ILE   A CA  1 
ATOM   3068 C C   . ILE   A 1 402 ? 6.113   2.970   -22.148 1.00 45.77  ? 939  ILE   A C   1 
ATOM   3069 O O   . ILE   A 1 402 ? 5.073   2.894   -22.812 1.00 47.13  ? 939  ILE   A O   1 
ATOM   3070 C CB  . ILE   A 1 402 ? 6.329   1.571   -20.030 1.00 40.61  ? 939  ILE   A CB  1 
ATOM   3071 C CG1 . ILE   A 1 402 ? 6.357   0.095   -19.634 1.00 39.40  ? 939  ILE   A CG1 1 
ATOM   3072 C CG2 . ILE   A 1 402 ? 4.958   2.172   -19.757 1.00 41.46  ? 939  ILE   A CG2 1 
ATOM   3073 C CD1 . ILE   A 1 402 ? 6.513   -0.136  -18.154 1.00 37.98  ? 939  ILE   A CD1 1 
ATOM   3074 N N   . LEU   A 1 403 ? 6.755   4.130   -21.978 1.00 46.88  ? 940  LEU   A N   1 
ATOM   3075 C CA  . LEU   A 1 403 ? 6.231   5.355   -22.576 1.00 50.40  ? 940  LEU   A CA  1 
ATOM   3076 C C   . LEU   A 1 403 ? 6.200   5.274   -24.097 1.00 54.94  ? 940  LEU   A C   1 
ATOM   3077 O O   . LEU   A 1 403 ? 5.312   5.856   -24.731 1.00 56.82  ? 940  LEU   A O   1 
ATOM   3078 C CB  . LEU   A 1 403 ? 7.057   6.559   -22.130 1.00 49.33  ? 940  LEU   A CB  1 
ATOM   3079 C CG  . LEU   A 1 403 ? 6.776   7.062   -20.714 1.00 49.27  ? 940  LEU   A CG  1 
ATOM   3080 C CD1 . LEU   A 1 403 ? 7.713   8.202   -20.360 1.00 48.81  ? 940  LEU   A CD1 1 
ATOM   3081 C CD2 . LEU   A 1 403 ? 5.332   7.510   -20.594 1.00 50.86  ? 940  LEU   A CD2 1 
ATOM   3082 N N   . LYS   A 1 404 ? 7.149   4.556   -24.698 1.00 57.32  ? 941  LYS   A N   1 
ATOM   3083 C CA  . LYS   A 1 404 ? 7.149   4.411   -26.148 1.00 61.25  ? 941  LYS   A CA  1 
ATOM   3084 C C   . LYS   A 1 404 ? 6.008   3.518   -26.612 1.00 63.68  ? 941  LYS   A C   1 
ATOM   3085 O O   . LYS   A 1 404 ? 5.372   3.798   -27.635 1.00 65.62  ? 941  LYS   A O   1 
ATOM   3086 C CB  . LYS   A 1 404 ? 8.491   3.857   -26.616 1.00 62.73  ? 941  LYS   A CB  1 
ATOM   3087 C CG  . LYS   A 1 404 ? 9.666   4.749   -26.274 1.00 62.74  ? 941  LYS   A CG  1 
ATOM   3088 C CD  . LYS   A 1 404 ? 10.959  4.189   -26.835 1.00 63.90  ? 941  LYS   A CD  1 
ATOM   3089 C CE  . LYS   A 1 404 ? 12.111  5.152   -26.613 1.00 63.60  ? 941  LYS   A CE  1 
ATOM   3090 N NZ  . LYS   A 1 404 ? 13.387  4.618   -27.163 1.00 64.38  ? 941  LYS   A NZ  1 
ATOM   3091 N N   . THR   A 1 405 ? 5.738   2.437   -25.876 1.00 64.36  ? 942  THR   A N   1 
ATOM   3092 C CA  . THR   A 1 405 ? 4.583   1.600   -26.185 1.00 67.13  ? 942  THR   A CA  1 
ATOM   3093 C C   . THR   A 1 405 ? 3.287   2.386   -26.042 1.00 69.23  ? 942  THR   A C   1 
ATOM   3094 O O   . THR   A 1 405 ? 2.337   2.179   -26.806 1.00 72.22  ? 942  THR   A O   1 
ATOM   3095 C CB  . THR   A 1 405 ? 4.564   0.373   -25.272 1.00 66.05  ? 942  THR   A CB  1 
ATOM   3096 O OG1 . THR   A 1 405 ? 5.897   -0.132  -25.120 1.00 64.22  ? 942  THR   A OG1 1 
ATOM   3097 C CG2 . THR   A 1 405 ? 3.675   -0.722  -25.860 1.00 68.07  ? 942  THR   A CG2 1 
ATOM   3098 N N   . GLU   A 1 406 ? 3.232   3.298   -25.068 1.00 68.53  ? 943  GLU   A N   1 
ATOM   3099 C CA  . GLU   A 1 406 ? 2.034   4.104   -24.863 1.00 70.93  ? 943  GLU   A CA  1 
ATOM   3100 C C   . GLU   A 1 406 ? 1.753   4.997   -26.065 1.00 72.01  ? 943  GLU   A C   1 
ATOM   3101 O O   . GLU   A 1 406 ? 0.612   5.085   -26.536 1.00 74.63  ? 943  GLU   A O   1 
ATOM   3102 C CB  . GLU   A 1 406 ? 2.180   4.940   -23.592 1.00 71.36  ? 943  GLU   A CB  1 
ATOM   3103 C CG  . GLU   A 1 406 ? 1.993   4.137   -22.325 1.00 73.05  ? 943  GLU   A CG  1 
ATOM   3104 C CD  . GLU   A 1 406 ? 0.601   3.552   -22.219 1.00 77.49  ? 943  GLU   A CD  1 
ATOM   3105 O OE1 . GLU   A 1 406 ? -0.348  4.192   -22.723 1.00 80.36  ? 943  GLU   A OE1 1 
ATOM   3106 O OE2 . GLU   A 1 406 ? 0.456   2.453   -21.638 1.00 78.14  ? 943  GLU   A OE2 1 
ATOM   3107 N N   . GLU   A 1 407 ? 2.786   5.667   -26.578 1.00 69.95  ? 944  GLU   A N   1 
ATOM   3108 C CA  . GLU   A 1 407 ? 2.610   6.568   -27.710 1.00 70.05  ? 944  GLU   A CA  1 
ATOM   3109 C C   . GLU   A 1 407 ? 2.565   5.835   -29.044 1.00 67.42  ? 944  GLU   A C   1 
ATOM   3110 O O   . GLU   A 1 407 ? 2.053   6.389   -30.023 1.00 68.63  ? 944  GLU   A O   1 
ATOM   3111 C CB  . GLU   A 1 407 ? 3.735   7.605   -27.732 1.00 71.73  ? 944  GLU   A CB  1 
ATOM   3112 C CG  . GLU   A 1 407 ? 3.920   8.339   -26.413 1.00 72.54  ? 944  GLU   A CG  1 
ATOM   3113 C CD  . GLU   A 1 407 ? 3.576   9.813   -26.510 1.00 75.25  ? 944  GLU   A CD  1 
ATOM   3114 O OE1 . GLU   A 1 407 ? 3.310   10.288  -27.635 1.00 77.16  ? 944  GLU   A OE1 1 
ATOM   3115 O OE2 . GLU   A 1 407 ? 3.577   10.496  -25.462 1.00 75.13  ? 944  GLU   A OE2 1 
ATOM   3116 N N   . GLY   A 1 408 ? 3.081   4.609   -29.101 1.00 63.94  ? 945  GLY   A N   1 
ATOM   3117 C CA  . GLY   A 1 408 ? 3.133   3.825   -30.314 1.00 63.34  ? 945  GLY   A CA  1 
ATOM   3118 C C   . GLY   A 1 408 ? 1.931   2.953   -30.588 1.00 63.34  ? 945  GLY   A C   1 
ATOM   3119 O O   . GLY   A 1 408 ? 1.845   2.356   -31.665 1.00 65.21  ? 945  GLY   A O   1 
ATOM   3120 N N   . ASN   A 1 409 ? 0.992   2.859   -29.649 1.00 63.54  ? 946  ASN   A N   1 
ATOM   3121 C CA  . ASN   A 1 409 ? -0.208  2.053   -29.819 1.00 59.10  ? 946  ASN   A CA  1 
ATOM   3122 C C   . ASN   A 1 409 ? -1.420  2.866   -29.392 1.00 54.82  ? 946  ASN   A C   1 
ATOM   3123 O O   . ASN   A 1 409 ? -1.410  3.483   -28.323 1.00 50.99  ? 946  ASN   A O   1 
ATOM   3124 C CB  . ASN   A 1 409 ? -0.122  0.755   -29.009 1.00 57.12  ? 946  ASN   A CB  1 
ATOM   3125 C CG  . ASN   A 1 409 ? 0.883   -0.229  -29.581 1.00 59.21  ? 946  ASN   A CG  1 
ATOM   3126 O OD1 . ASN   A 1 409 ? 0.510   -1.198  -30.242 1.00 59.64  ? 946  ASN   A OD1 1 
ATOM   3127 N ND2 . ASN   A 1 409 ? 2.163   0.013   -29.323 1.00 60.95  ? 946  ASN   A ND2 1 
ATOM   3128 N N   . ASN   A 1 410 ? -2.454  2.870   -30.230 1.00 56.07  ? 947  ASN   A N   1 
ATOM   3129 C CA  . ASN   A 1 410 ? -3.682  3.587   -29.920 1.00 55.43  ? 947  ASN   A CA  1 
ATOM   3130 C C   . ASN   A 1 410 ? -4.490  2.814   -28.883 1.00 50.82  ? 947  ASN   A C   1 
ATOM   3131 O O   . ASN   A 1 410 ? -4.430  1.584   -28.810 1.00 48.73  ? 947  ASN   A O   1 
ATOM   3132 C CB  . ASN   A 1 410 ? -4.512  3.800   -31.190 1.00 58.25  ? 947  ASN   A CB  1 
ATOM   3133 C CG  . ASN   A 1 410 ? -5.409  5.030   -31.114 1.00 58.87  ? 947  ASN   A CG  1 
ATOM   3134 O OD1 . ASN   A 1 410 ? -6.611  4.930   -30.857 1.00 57.10  ? 947  ASN   A OD1 1 
ATOM   3135 N ND2 . ASN   A 1 410 ? -4.822  6.199   -31.341 1.00 60.94  ? 947  ASN   A ND2 1 
ATOM   3136 N N   . ASP   A 1 411 ? -5.244  3.551   -28.065 1.00 49.51  ? 948  ASP   A N   1 
ATOM   3137 C CA  . ASP   A 1 411 ? -6.073  2.899   -27.056 1.00 46.63  ? 948  ASP   A CA  1 
ATOM   3138 C C   . ASP   A 1 411 ? -7.230  2.133   -27.683 1.00 46.37  ? 948  ASP   A C   1 
ATOM   3139 O O   . ASP   A 1 411 ? -7.709  1.156   -27.097 1.00 43.66  ? 948  ASP   A O   1 
ATOM   3140 C CB  . ASP   A 1 411 ? -6.606  3.926   -26.056 1.00 46.85  ? 948  ASP   A CB  1 
ATOM   3141 C CG  . ASP   A 1 411 ? -5.528  4.452   -25.128 1.00 47.32  ? 948  ASP   A CG  1 
ATOM   3142 O OD1 . ASP   A 1 411 ? -4.548  3.715   -24.879 1.00 45.97  ? 948  ASP   A OD1 1 
ATOM   3143 O OD2 . ASP   A 1 411 ? -5.662  5.597   -24.644 1.00 48.70  ? 948  ASP   A OD2 1 
ATOM   3144 N N   . PHE   A 1 412 ? -7.682  2.547   -28.864 1.00 48.97  ? 949  PHE   A N   1 
ATOM   3145 C CA  . PHE   A 1 412 ? -8.841  1.956   -29.511 1.00 49.95  ? 949  PHE   A CA  1 
ATOM   3146 C C   . PHE   A 1 412 ? -8.495  1.458   -30.907 1.00 53.35  ? 949  PHE   A C   1 
ATOM   3147 O O   . PHE   A 1 412 ? -7.501  1.865   -31.511 1.00 55.88  ? 949  PHE   A O   1 
ATOM   3148 C CB  . PHE   A 1 412 ? -9.994  2.959   -29.620 1.00 51.70  ? 949  PHE   A CB  1 
ATOM   3149 C CG  . PHE   A 1 412 ? -10.565 3.379   -28.300 1.00 50.10  ? 949  PHE   A CG  1 
ATOM   3150 C CD1 . PHE   A 1 412 ? -11.459 2.563   -27.624 1.00 47.62  ? 949  PHE   A CD1 1 
ATOM   3151 C CD2 . PHE   A 1 412 ? -10.226 4.601   -27.744 1.00 51.10  ? 949  PHE   A CD2 1 
ATOM   3152 C CE1 . PHE   A 1 412 ? -11.997 2.953   -26.408 1.00 45.98  ? 949  PHE   A CE1 1 
ATOM   3153 C CE2 . PHE   A 1 412 ? -10.761 4.997   -26.529 1.00 49.62  ? 949  PHE   A CE2 1 
ATOM   3154 C CZ  . PHE   A 1 412 ? -11.648 4.171   -25.859 1.00 46.77  ? 949  PHE   A CZ  1 
ATOM   3155 N N   . LEU   A 1 413 ? -9.351  0.575   -31.409 1.00 54.88  ? 950  LEU   A N   1 
ATOM   3156 C CA  . LEU   A 1 413 ? -9.371  0.181   -32.810 1.00 59.15  ? 950  LEU   A CA  1 
ATOM   3157 C C   . LEU   A 1 413 ? -10.550 0.867   -33.491 1.00 64.60  ? 950  LEU   A C   1 
ATOM   3158 O O   . LEU   A 1 413 ? -11.632 0.981   -32.908 1.00 63.57  ? 950  LEU   A O   1 
ATOM   3159 C CB  . LEU   A 1 413 ? -9.485  -1.340  -32.943 1.00 55.55  ? 950  LEU   A CB  1 
ATOM   3160 C CG  . LEU   A 1 413 ? -8.597  -2.137  -31.987 1.00 50.65  ? 950  LEU   A CG  1 
ATOM   3161 C CD1 . LEU   A 1 413 ? -8.859  -3.629  -32.113 1.00 48.51  ? 950  LEU   A CD1 1 
ATOM   3162 C CD2 . LEU   A 1 413 ? -7.138  -1.819  -32.245 1.00 51.94  ? 950  LEU   A CD2 1 
ATOM   3163 N N   . LYS   A 1 414 ? -10.340 1.334   -34.721 1.00 70.99  ? 951  LYS   A N   1 
ATOM   3164 C CA  . LYS   A 1 414 ? -11.343 2.145   -35.402 1.00 76.31  ? 951  LYS   A CA  1 
ATOM   3165 C C   . LYS   A 1 414 ? -12.382 1.261   -36.083 1.00 77.64  ? 951  LYS   A C   1 
ATOM   3166 O O   . LYS   A 1 414 ? -12.033 0.340   -36.832 1.00 78.86  ? 951  LYS   A O   1 
ATOM   3167 C CB  . LYS   A 1 414 ? -10.682 3.063   -36.430 1.00 82.25  ? 951  LYS   A CB  1 
ATOM   3168 C CG  . LYS   A 1 414 ? -9.640  4.001   -35.847 1.00 84.14  ? 951  LYS   A CG  1 
ATOM   3169 C CD  . LYS   A 1 414 ? -9.065  4.927   -36.910 1.00 90.14  ? 951  LYS   A CD  1 
ATOM   3170 C CE  . LYS   A 1 414 ? -8.129  5.958   -36.296 1.00 91.27  ? 951  LYS   A CE  1 
ATOM   3171 N NZ  . LYS   A 1 414 ? -7.487  6.811   -37.335 1.00 96.95  ? 951  LYS   A NZ  1 
ATOM   3172 N N   . LYS   A 1 415 ? -13.661 1.556   -35.834 1.00 77.47  ? 952  LYS   A N   1 
ATOM   3173 C CA  . LYS   A 1 415 ? -14.765 0.812   -36.426 1.00 77.71  ? 952  LYS   A CA  1 
ATOM   3174 C C   . LYS   A 1 415 ? -15.804 1.785   -36.969 1.00 80.94  ? 952  LYS   A C   1 
ATOM   3175 O O   . LYS   A 1 415 ? -15.743 2.993   -36.730 1.00 82.02  ? 952  LYS   A O   1 
ATOM   3176 C CB  . LYS   A 1 415 ? -15.405 -0.143  -35.409 1.00 73.14  ? 952  LYS   A CB  1 
ATOM   3177 C CG  . LYS   A 1 415 ? -14.443 -1.158  -34.817 1.00 69.53  ? 952  LYS   A CG  1 
ATOM   3178 C CD  . LYS   A 1 415 ? -14.574 -2.516  -35.484 1.00 69.05  ? 952  LYS   A CD  1 
ATOM   3179 C CE  . LYS   A 1 415 ? -13.241 -2.985  -36.037 1.00 69.59  ? 952  LYS   A CE  1 
ATOM   3180 N NZ  . LYS   A 1 415 ? -13.138 -4.471  -36.053 1.00 68.30  ? 952  LYS   A NZ  1 
ATOM   3181 N N   . LYS   A 1 416 ? -16.767 1.238   -37.717 1.00 82.88  ? 953  LYS   A N   1 
ATOM   3182 C CA  . LYS   A 1 416 ? -17.888 2.046   -38.189 1.00 86.54  ? 953  LYS   A CA  1 
ATOM   3183 C C   . LYS   A 1 416 ? -18.696 2.586   -37.019 1.00 84.58  ? 953  LYS   A C   1 
ATOM   3184 O O   . LYS   A 1 416 ? -18.961 3.791   -36.932 1.00 86.83  ? 953  LYS   A O   1 
ATOM   3185 C CB  . LYS   A 1 416 ? -18.788 1.223   -39.113 1.00 89.17  ? 953  LYS   A CB  1 
ATOM   3186 C CG  . LYS   A 1 416 ? -18.223 0.928   -40.488 1.00 92.83  ? 953  LYS   A CG  1 
ATOM   3187 C CD  . LYS   A 1 416 ? -19.241 0.157   -41.312 1.00 95.11  ? 953  LYS   A CD  1 
ATOM   3188 C CE  . LYS   A 1 416 ? -18.705 -0.205  -42.686 1.00 98.93  ? 953  LYS   A CE  1 
ATOM   3189 N NZ  . LYS   A 1 416 ? -19.707 -0.978  -43.473 1.00 101.07 ? 953  LYS   A NZ  1 
ATOM   3190 N N   . GLY   A 1 417 ? -19.103 1.705   -36.110 1.00 80.38  ? 954  GLY   A N   1 
ATOM   3191 C CA  . GLY   A 1 417 ? -19.868 2.120   -34.953 1.00 78.19  ? 954  GLY   A CA  1 
ATOM   3192 C C   . GLY   A 1 417 ? -18.999 2.334   -33.733 1.00 74.51  ? 954  GLY   A C   1 
ATOM   3193 O O   . GLY   A 1 417 ? -18.082 3.161   -33.754 1.00 75.50  ? 954  GLY   A O   1 
ATOM   3194 N N   . LYS   A 1 418 ? -19.276 1.593   -32.664 1.00 70.02  ? 955  LYS   A N   1 
ATOM   3195 C CA  . LYS   A 1 418 ? -18.499 1.739   -31.444 1.00 65.62  ? 955  LYS   A CA  1 
ATOM   3196 C C   . LYS   A 1 418 ? -17.079 1.242   -31.678 1.00 62.92  ? 955  LYS   A C   1 
ATOM   3197 O O   . LYS   A 1 418 ? -16.869 0.199   -32.305 1.00 63.39  ? 955  LYS   A O   1 
ATOM   3198 C CB  . LYS   A 1 418 ? -19.158 0.975   -30.295 1.00 63.03  ? 955  LYS   A CB  1 
ATOM   3199 C CG  . LYS   A 1 418 ? -18.587 1.314   -28.926 1.00 61.14  ? 955  LYS   A CG  1 
ATOM   3200 C CD  . LYS   A 1 418 ? -18.720 2.808   -28.634 1.00 64.07  ? 955  LYS   A CD  1 
ATOM   3201 C CE  . LYS   A 1 418 ? -17.831 3.246   -27.471 1.00 63.02  ? 955  LYS   A CE  1 
ATOM   3202 N NZ  . LYS   A 1 418 ? -18.342 2.818   -26.135 1.00 61.16  ? 955  LYS   A NZ  1 
ATOM   3203 N N   . ASP   A 1 419 ? -16.102 2.007   -31.203 1.00 59.62  ? 956  ASP   A N   1 
ATOM   3204 C CA  . ASP   A 1 419 ? -14.707 1.620   -31.347 1.00 56.00  ? 956  ASP   A CA  1 
ATOM   3205 C C   . ASP   A 1 419 ? -14.339 0.587   -30.293 1.00 50.10  ? 956  ASP   A C   1 
ATOM   3206 O O   . ASP   A 1 419 ? -14.811 0.644   -29.154 1.00 47.35  ? 956  ASP   A O   1 
ATOM   3207 C CB  . ASP   A 1 419 ? -13.792 2.842   -31.239 1.00 30.00  ? 956  ASP   A CB  1 
ATOM   3208 C CG  . ASP   A 1 419 ? -13.886 3.748   -32.451 1.00 30.00  ? 956  ASP   A CG  1 
ATOM   3209 O OD1 . ASP   A 1 419 ? -14.427 3.305   -33.486 1.00 30.00  ? 956  ASP   A OD1 1 
ATOM   3210 O OD2 . ASP   A 1 419 ? -13.446 4.917   -32.461 1.00 30.00  ? 956  ASP   A OD2 1 
ATOM   3211 N N   . LEU   A 1 420 ? -13.492 -0.358  -30.678 1.00 47.97  ? 957  LEU   A N   1 
ATOM   3212 C CA  . LEU   A 1 420 ? -13.124 -1.459  -29.805 1.00 44.11  ? 957  LEU   A CA  1 
ATOM   3213 C C   . LEU   A 1 420 ? -11.921 -1.094  -28.945 1.00 41.60  ? 957  LEU   A C   1 
ATOM   3214 O O   . LEU   A 1 420 ? -11.060 -0.306  -29.343 1.00 43.57  ? 957  LEU   A O   1 
ATOM   3215 C CB  . LEU   A 1 420 ? -12.814 -2.712  -30.627 1.00 44.53  ? 957  LEU   A CB  1 
ATOM   3216 C CG  . LEU   A 1 420 ? -13.891 -3.211  -31.592 1.00 45.55  ? 957  LEU   A CG  1 
ATOM   3217 C CD1 . LEU   A 1 420 ? -13.494 -4.562  -32.162 1.00 45.39  ? 957  LEU   A CD1 1 
ATOM   3218 C CD2 . LEU   A 1 420 ? -15.246 -3.290  -30.905 1.00 44.56  ? 957  LEU   A CD2 1 
ATOM   3219 N N   . ILE   A 1 421 ? -11.872 -1.681  -27.752 1.00 37.53  ? 958  ILE   A N   1 
ATOM   3220 C CA  . ILE   A 1 421 ? -10.712 -1.528  -26.884 1.00 36.13  ? 958  ILE   A CA  1 
ATOM   3221 C C   . ILE   A 1 421 ? -9.532  -2.278  -27.488 1.00 37.17  ? 958  ILE   A C   1 
ATOM   3222 O O   . ILE   A 1 421 ? -9.655  -3.446  -27.871 1.00 37.14  ? 958  ILE   A O   1 
ATOM   3223 C CB  . ILE   A 1 421 ? -11.037 -2.038  -25.472 1.00 32.28  ? 958  ILE   A CB  1 
ATOM   3224 C CG1 . ILE   A 1 421 ? -12.235 -1.278  -24.904 1.00 31.27  ? 958  ILE   A CG1 1 
ATOM   3225 C CG2 . ILE   A 1 421 ? -9.822  -1.918  -24.560 1.00 31.15  ? 958  ILE   A CG2 1 
ATOM   3226 C CD1 . ILE   A 1 421 ? -12.802 -1.886  -23.648 1.00 29.66  ? 958  ILE   A CD1 1 
ATOM   3227 N N   . ASN   A 1 422 ? -8.383  -1.609  -27.589 1.00 37.90  ? 959  ASN   A N   1 
ATOM   3228 C CA  . ASN   A 1 422 ? -7.164  -2.245  -28.092 1.00 37.59  ? 959  ASN   A CA  1 
ATOM   3229 C C   . ASN   A 1 422 ? -6.508  -2.990  -26.937 1.00 35.62  ? 959  ASN   A C   1 
ATOM   3230 O O   . ASN   A 1 422 ? -5.808  -2.393  -26.115 1.00 35.61  ? 959  ASN   A O   1 
ATOM   3231 C CB  . ASN   A 1 422 ? -6.220  -1.211  -28.696 1.00 39.52  ? 959  ASN   A CB  1 
ATOM   3232 C CG  . ASN   A 1 422 ? -4.916  -1.823  -29.208 1.00 38.37  ? 959  ASN   A CG  1 
ATOM   3233 O OD1 . ASN   A 1 422 ? -4.700  -3.032  -29.118 1.00 37.47  ? 959  ASN   A OD1 1 
ATOM   3234 N ND2 . ASN   A 1 422 ? -4.049  -0.984  -29.758 1.00 41.07  ? 959  ASN   A ND2 1 
ATOM   3235 N N   . PHE   A 1 423 ? -6.724  -4.307  -26.873 1.00 34.29  ? 960  PHE   A N   1 
ATOM   3236 C CA  . PHE   A 1 423 ? -6.169  -5.091  -25.775 1.00 31.94  ? 960  PHE   A CA  1 
ATOM   3237 C C   . PHE   A 1 423 ? -4.765  -5.596  -26.058 1.00 32.35  ? 960  PHE   A C   1 
ATOM   3238 O O   . PHE   A 1 423 ? -4.011  -5.841  -25.111 1.00 31.60  ? 960  PHE   A O   1 
ATOM   3239 C CB  . PHE   A 1 423 ? -7.069  -6.284  -25.439 1.00 30.66  ? 960  PHE   A CB  1 
ATOM   3240 C CG  . PHE   A 1 423 ? -6.651  -7.020  -24.190 1.00 28.64  ? 960  PHE   A CG  1 
ATOM   3241 C CD1 . PHE   A 1 423 ? -7.068  -6.582  -22.940 1.00 26.39  ? 960  PHE   A CD1 1 
ATOM   3242 C CD2 . PHE   A 1 423 ? -5.834  -8.139  -24.266 1.00 28.76  ? 960  PHE   A CD2 1 
ATOM   3243 C CE1 . PHE   A 1 423 ? -6.682  -7.245  -21.797 1.00 24.92  ? 960  PHE   A CE1 1 
ATOM   3244 C CE2 . PHE   A 1 423 ? -5.445  -8.807  -23.127 1.00 27.93  ? 960  PHE   A CE2 1 
ATOM   3245 C CZ  . PHE   A 1 423 ? -5.870  -8.360  -21.891 1.00 26.77  ? 960  PHE   A CZ  1 
ATOM   3246 N N   . SER   A 1 424 ? -4.402  -5.773  -27.331 1.00 34.64  ? 961  SER   A N   1 
ATOM   3247 C CA  . SER   A 1 424 ? -3.028  -6.149  -27.654 1.00 37.42  ? 961  SER   A CA  1 
ATOM   3248 C C   . SER   A 1 424 ? -2.041  -5.132  -27.099 1.00 37.54  ? 961  SER   A C   1 
ATOM   3249 O O   . SER   A 1 424 ? -0.961  -5.498  -26.619 1.00 35.79  ? 961  SER   A O   1 
ATOM   3250 C CB  . SER   A 1 424 ? -2.859  -6.293  -29.166 1.00 40.78  ? 961  SER   A CB  1 
ATOM   3251 O OG  . SER   A 1 424 ? -3.540  -7.440  -29.644 1.00 41.61  ? 961  SER   A OG  1 
ATOM   3252 N N   . LYS   A 1 425 ? -2.402  -3.849  -27.144 1.00 36.16  ? 962  LYS   A N   1 
ATOM   3253 C CA  . LYS   A 1 425 ? -1.568  -2.822  -26.534 1.00 36.62  ? 962  LYS   A CA  1 
ATOM   3254 C C   . LYS   A 1 425 ? -1.341  -3.109  -25.056 1.00 35.11  ? 962  LYS   A C   1 
ATOM   3255 O O   . LYS   A 1 425 ? -0.207  -3.051  -24.568 1.00 37.18  ? 962  LYS   A O   1 
ATOM   3256 C CB  . LYS   A 1 425 ? -2.207  -1.447  -26.726 1.00 37.11  ? 962  LYS   A CB  1 
ATOM   3257 C CG  . LYS   A 1 425 ? -1.639  -0.373  -25.818 1.00 36.53  ? 962  LYS   A CG  1 
ATOM   3258 C CD  . LYS   A 1 425 ? -2.288  0.973   -26.078 1.00 37.54  ? 962  LYS   A CD  1 
ATOM   3259 C CE  . LYS   A 1 425 ? -1.520  2.081   -25.375 1.00 40.49  ? 962  LYS   A CE  1 
ATOM   3260 N NZ  . LYS   A 1 425 ? -1.903  3.443   -25.838 1.00 40.42  ? 962  LYS   A NZ  1 
ATOM   3261 N N   . ARG   A 1 426 ? -2.411  -3.435  -24.326 1.00 32.65  ? 963  ARG   A N   1 
ATOM   3262 C CA  . ARG   A 1 426 ? -2.268  -3.726  -22.901 1.00 30.25  ? 963  ARG   A CA  1 
ATOM   3263 C C   . ARG   A 1 426 ? -1.406  -4.963  -22.674 1.00 30.38  ? 963  ARG   A C   1 
ATOM   3264 O O   . ARG   A 1 426 ? -0.601  -5.003  -21.738 1.00 29.41  ? 963  ARG   A O   1 
ATOM   3265 C CB  . ARG   A 1 426 ? -3.641  -3.909  -22.255 1.00 28.02  ? 963  ARG   A CB  1 
ATOM   3266 C CG  . ARG   A 1 426 ? -4.309  -2.618  -21.812 1.00 28.54  ? 963  ARG   A CG  1 
ATOM   3267 C CD  . ARG   A 1 426 ? -4.801  -1.779  -22.990 1.00 31.28  ? 963  ARG   A CD  1 
ATOM   3268 N NE  . ARG   A 1 426 ? -5.671  -0.696  -22.538 1.00 31.34  ? 963  ARG   A NE  1 
ATOM   3269 C CZ  . ARG   A 1 426 ? -6.338  0.123   -23.345 1.00 32.69  ? 963  ARG   A CZ  1 
ATOM   3270 N NH1 . ARG   A 1 426 ? -6.242  -0.009  -24.661 1.00 34.31  ? 963  ARG   A NH1 1 
ATOM   3271 N NH2 . ARG   A 1 426 ? -7.106  1.075   -22.832 1.00 32.56  ? 963  ARG   A NH2 1 
ATOM   3272 N N   . ARG   A 1 427 ? -1.568  -5.984  -23.519 1.00 32.42  ? 964  ARG   A N   1 
ATOM   3273 C CA  . ARG   A 1 427 ? -0.720  -7.166  -23.426 1.00 33.23  ? 964  ARG   A CA  1 
ATOM   3274 C C   . ARG   A 1 427 ? 0.749   -6.806  -23.606 1.00 36.49  ? 964  ARG   A C   1 
ATOM   3275 O O   . ARG   A 1 427 ? 1.610   -7.304  -22.872 1.00 36.79  ? 964  ARG   A O   1 
ATOM   3276 C CB  . ARG   A 1 427 ? -1.141  -8.200  -24.466 1.00 33.14  ? 964  ARG   A CB  1 
ATOM   3277 C CG  . ARG   A 1 427 ? -0.248  -9.422  -24.499 1.00 34.77  ? 964  ARG   A CG  1 
ATOM   3278 C CD  . ARG   A 1 427 ? -0.748  -10.455 -25.490 1.00 36.48  ? 964  ARG   A CD  1 
ATOM   3279 N NE  . ARG   A 1 427 ? -2.133  -10.844 -25.237 1.00 35.53  ? 964  ARG   A NE  1 
ATOM   3280 C CZ  . ARG   A 1 427 ? -3.167  -10.442 -25.968 1.00 35.84  ? 964  ARG   A CZ  1 
ATOM   3281 N NH1 . ARG   A 1 427 ? -2.978  -9.638  -27.008 1.00 36.99  ? 964  ARG   A NH1 1 
ATOM   3282 N NH2 . ARG   A 1 427 ? -4.389  -10.853 -25.666 1.00 34.85  ? 964  ARG   A NH2 1 
ATOM   3283 N N   . LYS   A 1 428 ? 1.051   -5.935  -24.578 1.00 38.55  ? 965  LYS   A N   1 
ATOM   3284 C CA  . LYS   A 1 428 ? 2.437   -5.547  -24.835 1.00 40.37  ? 965  LYS   A CA  1 
ATOM   3285 C C   . LYS   A 1 428 ? 3.055   -4.864  -23.622 1.00 39.58  ? 965  LYS   A C   1 
ATOM   3286 O O   . LYS   A 1 428 ? 4.198   -5.156  -23.249 1.00 40.88  ? 965  LYS   A O   1 
ATOM   3287 C CB  . LYS   A 1 428 ? 2.513   -4.629  -26.056 1.00 42.75  ? 965  LYS   A CB  1 
ATOM   3288 C CG  . LYS   A 1 428 ? 2.275   -5.329  -27.386 1.00 45.10  ? 965  LYS   A CG  1 
ATOM   3289 C CD  . LYS   A 1 428 ? 2.487   -4.377  -28.554 1.00 48.57  ? 965  LYS   A CD  1 
ATOM   3290 C CE  . LYS   A 1 428 ? 2.514   -5.118  -29.884 1.00 51.25  ? 965  LYS   A CE  1 
ATOM   3291 N NZ  . LYS   A 1 428 ? 2.785   -4.194  -31.022 1.00 54.61  ? 965  LYS   A NZ  1 
ATOM   3292 N N   . VAL   A 1 429 ? 2.317   -3.947  -22.994 1.00 37.71  ? 966  VAL   A N   1 
ATOM   3293 C CA  . VAL   A 1 429 ? 2.815   -3.316  -21.778 1.00 37.31  ? 966  VAL   A CA  1 
ATOM   3294 C C   . VAL   A 1 429 ? 2.939   -4.342  -20.658 1.00 35.93  ? 966  VAL   A C   1 
ATOM   3295 O O   . VAL   A 1 429 ? 3.866   -4.283  -19.843 1.00 36.38  ? 966  VAL   A O   1 
ATOM   3296 C CB  . VAL   A 1 429 ? 1.908   -2.143  -21.372 1.00 36.54  ? 966  VAL   A CB  1 
ATOM   3297 C CG1 . VAL   A 1 429 ? 2.524   -1.383  -20.213 1.00 36.01  ? 966  VAL   A CG1 1 
ATOM   3298 C CG2 . VAL   A 1 429 ? 1.662   -1.226  -22.560 1.00 38.94  ? 966  VAL   A CG2 1 
ATOM   3299 N N   . ALA   A 1 430 ? 2.010   -5.299  -20.596 1.00 34.20  ? 967  ALA   A N   1 
ATOM   3300 C CA  . ALA   A 1 430 ? 2.092   -6.323  -19.560 1.00 32.64  ? 967  ALA   A CA  1 
ATOM   3301 C C   . ALA   A 1 430 ? 3.333   -7.193  -19.732 1.00 36.08  ? 967  ALA   A C   1 
ATOM   3302 O O   . ALA   A 1 430 ? 3.895   -7.668  -18.739 1.00 35.30  ? 967  ALA   A O   1 
ATOM   3303 C CB  . ALA   A 1 430 ? 0.827   -7.183  -19.561 1.00 28.86  ? 967  ALA   A CB  1 
ATOM   3304 N N   . GLU   A 1 431 ? 3.770   -7.409  -20.979 1.00 40.36  ? 968  GLU   A N   1 
ATOM   3305 C CA  . GLU   A 1 431 ? 5.006   -8.149  -21.224 1.00 44.47  ? 968  GLU   A CA  1 
ATOM   3306 C C   . GLU   A 1 431 ? 6.185   -7.477  -20.535 1.00 43.85  ? 968  GLU   A C   1 
ATOM   3307 O O   . GLU   A 1 431 ? 7.033   -8.150  -19.937 1.00 44.94  ? 968  GLU   A O   1 
ATOM   3308 C CB  . GLU   A 1 431 ? 5.274   -8.264  -22.728 1.00 50.24  ? 968  GLU   A CB  1 
ATOM   3309 C CG  . GLU   A 1 431 ? 4.134   -8.843  -23.562 1.00 52.75  ? 968  GLU   A CG  1 
ATOM   3310 C CD  . GLU   A 1 431 ? 4.046   -10.359 -23.501 1.00 56.18  ? 968  GLU   A CD  1 
ATOM   3311 O OE1 . GLU   A 1 431 ? 4.554   -11.025 -24.432 1.00 60.21  ? 968  GLU   A OE1 1 
ATOM   3312 O OE2 . GLU   A 1 431 ? 3.467   -10.884 -22.523 1.00 54.38  ? 968  GLU   A OE2 1 
ATOM   3313 N N   . ILE   A 1 432 ? 6.247   -6.147  -20.600 1.00 42.75  ? 969  ILE   A N   1 
ATOM   3314 C CA  . ILE   A 1 432 ? 7.362   -5.421  -20.006 1.00 43.23  ? 969  ILE   A CA  1 
ATOM   3315 C C   . ILE   A 1 432 ? 7.254   -5.421  -18.486 1.00 41.49  ? 969  ILE   A C   1 
ATOM   3316 O O   . ILE   A 1 432 ? 8.262   -5.544  -17.782 1.00 43.32  ? 969  ILE   A O   1 
ATOM   3317 C CB  . ILE   A 1 432 ? 7.425   -3.991  -20.575 1.00 42.94  ? 969  ILE   A CB  1 
ATOM   3318 C CG1 . ILE   A 1 432 ? 7.327   -4.026  -22.104 1.00 44.25  ? 969  ILE   A CG1 1 
ATOM   3319 C CG2 . ILE   A 1 432 ? 8.713   -3.305  -20.144 1.00 44.51  ? 969  ILE   A CG2 1 
ATOM   3320 C CD1 . ILE   A 1 432 ? 7.163   -2.661  -22.747 1.00 44.81  ? 969  ILE   A CD1 1 
ATOM   3321 N N   . THR   A 1 433 ? 6.036   -5.286  -17.952 1.00 39.06  ? 970  THR   A N   1 
ATOM   3322 C CA  . THR   A 1 433 ? 5.883   -5.272  -16.499 1.00 37.00  ? 970  THR   A CA  1 
ATOM   3323 C C   . THR   A 1 433 ? 6.214   -6.624  -15.891 1.00 36.50  ? 970  THR   A C   1 
ATOM   3324 O O   . THR   A 1 433 ? 6.583   -6.697  -14.714 1.00 36.43  ? 970  THR   A O   1 
ATOM   3325 C CB  . THR   A 1 433 ? 4.468   -4.867  -16.104 1.00 35.09  ? 970  THR   A CB  1 
ATOM   3326 O OG1 . THR   A 1 433 ? 3.530   -5.740  -16.746 1.00 35.29  ? 970  THR   A OG1 1 
ATOM   3327 C CG2 . THR   A 1 433 ? 4.195   -3.421  -16.505 1.00 35.19  ? 970  THR   A CG2 1 
ATOM   3328 N N   . GLY   A 1 434 ? 6.073   -7.701  -16.666 1.00 37.03  ? 971  GLY   A N   1 
ATOM   3329 C CA  . GLY   A 1 434 ? 6.527   -8.998  -16.202 1.00 39.04  ? 971  GLY   A CA  1 
ATOM   3330 C C   . GLY   A 1 434 ? 8.033   -9.076  -16.048 1.00 43.67  ? 971  GLY   A C   1 
ATOM   3331 O O   . GLY   A 1 434 ? 8.536   -9.849  -15.230 1.00 43.94  ? 971  GLY   A O   1 
ATOM   3332 N N   . GLU   A 1 435 ? 8.772   -8.277  -16.824 1.00 46.94  ? 972  GLU   A N   1 
ATOM   3333 C CA  . GLU   A 1 435 ? 10.223  -8.265  -16.695 1.00 52.41  ? 972  GLU   A CA  1 
ATOM   3334 C C   . GLU   A 1 435 ? 10.661  -7.626  -15.385 1.00 50.82  ? 972  GLU   A C   1 
ATOM   3335 O O   . GLU   A 1 435 ? 11.739  -7.944  -14.869 1.00 52.76  ? 972  GLU   A O   1 
ATOM   3336 C CB  . GLU   A 1 435 ? 10.850  -7.523  -17.874 1.00 58.88  ? 972  GLU   A CB  1 
ATOM   3337 C CG  . GLU   A 1 435 ? 10.464  -8.072  -19.234 1.00 63.05  ? 972  GLU   A CG  1 
ATOM   3338 C CD  . GLU   A 1 435 ? 11.146  -7.331  -20.368 1.00 69.44  ? 972  GLU   A CD  1 
ATOM   3339 O OE1 . GLU   A 1 435 ? 10.883  -6.120  -20.536 1.00 70.51  ? 972  GLU   A OE1 1 
ATOM   3340 O OE2 . GLU   A 1 435 ? 11.956  -7.959  -21.083 1.00 73.29  ? 972  GLU   A OE2 1 
ATOM   3341 N N   . ILE   A 1 436 ? 9.848   -6.718  -14.844 1.00 47.68  ? 973  ILE   A N   1 
ATOM   3342 C CA  . ILE   A 1 436 ? 10.189  -6.058  -13.589 1.00 47.45  ? 973  ILE   A CA  1 
ATOM   3343 C C   . ILE   A 1 436 ? 10.020  -7.020  -12.418 1.00 47.82  ? 973  ILE   A C   1 
ATOM   3344 O O   . ILE   A 1 436 ? 10.825  -7.027  -11.477 1.00 48.67  ? 973  ILE   A O   1 
ATOM   3345 C CB  . ILE   A 1 436 ? 9.338   -4.783  -13.419 1.00 43.71  ? 973  ILE   A CB  1 
ATOM   3346 C CG1 . ILE   A 1 436 ? 9.742   -3.727  -14.459 1.00 44.64  ? 973  ILE   A CG1 1 
ATOM   3347 C CG2 . ILE   A 1 436 ? 9.443   -4.240  -12.000 1.00 42.17  ? 973  ILE   A CG2 1 
ATOM   3348 C CD1 . ILE   A 1 436 ? 8.998   -2.407  -14.341 1.00 42.62  ? 973  ILE   A CD1 1 
ATOM   3349 N N   . GLN   A 1 437 ? 8.997   -7.875  -12.475 1.00 47.55  ? 974  GLN   A N   1 
ATOM   3350 C CA  . GLN   A 1 437 ? 8.657   -8.720  -11.337 1.00 47.94  ? 974  GLN   A CA  1 
ATOM   3351 C C   . GLN   A 1 437 ? 9.652   -9.850  -11.110 1.00 50.56  ? 974  GLN   A C   1 
ATOM   3352 O O   . GLN   A 1 437 ? 9.746   -10.354 -9.986  1.00 50.94  ? 974  GLN   A O   1 
ATOM   3353 C CB  . GLN   A 1 437 ? 7.251   -9.291  -11.519 1.00 46.52  ? 974  GLN   A CB  1 
ATOM   3354 C CG  . GLN   A 1 437 ? 6.176   -8.214  -11.556 1.00 45.29  ? 974  GLN   A CG  1 
ATOM   3355 C CD  . GLN   A 1 437 ? 4.778   -8.777  -11.439 1.00 43.84  ? 974  GLN   A CD  1 
ATOM   3356 O OE1 . GLN   A 1 437 ? 4.229   -9.314  -12.405 1.00 43.87  ? 974  GLN   A OE1 1 
ATOM   3357 N NE2 . GLN   A 1 437 ? 4.186   -8.649  -10.252 1.00 41.84  ? 974  GLN   A NE2 1 
ATOM   3358 N N   . GLN   A 1 438 ? 10.399  -10.255 -12.137 1.00 52.65  ? 975  GLN   A N   1 
ATOM   3359 C CA  . GLN   A 1 438 ? 11.294  -11.398 -11.998 1.00 55.13  ? 975  GLN   A CA  1 
ATOM   3360 C C   . GLN   A 1 438 ? 12.479  -11.117 -11.082 1.00 56.38  ? 975  GLN   A C   1 
ATOM   3361 O O   . GLN   A 1 438 ? 13.188  -12.058 -10.712 1.00 57.34  ? 975  GLN   A O   1 
ATOM   3362 C CB  . GLN   A 1 438 ? 11.792  -11.841 -13.376 1.00 58.86  ? 975  GLN   A CB  1 
ATOM   3363 C CG  . GLN   A 1 438 ? 12.890  -10.968 -13.966 1.00 62.67  ? 975  GLN   A CG  1 
ATOM   3364 C CD  . GLN   A 1 438 ? 13.225  -11.350 -15.395 1.00 65.88  ? 975  GLN   A CD  1 
ATOM   3365 O OE1 . GLN   A 1 438 ? 12.340  -11.440 -16.247 1.00 64.07  ? 975  GLN   A OE1 1 
ATOM   3366 N NE2 . GLN   A 1 438 ? 14.506  -11.587 -15.664 1.00 70.43  ? 975  GLN   A NE2 1 
ATOM   3367 N N   . TYR   A 1 439 ? 12.700  -9.860  -10.697 1.00 56.97  ? 976  TYR   A N   1 
ATOM   3368 C CA  . TYR   A 1 439 ? 13.823  -9.482  -9.850  1.00 60.72  ? 976  TYR   A CA  1 
ATOM   3369 C C   . TYR   A 1 439 ? 13.408  -9.084  -8.441  1.00 59.75  ? 976  TYR   A C   1 
ATOM   3370 O O   . TYR   A 1 439 ? 14.275  -8.756  -7.625  1.00 61.56  ? 976  TYR   A O   1 
ATOM   3371 C CB  . TYR   A 1 439 ? 14.598  -8.320  -10.484 1.00 62.24  ? 976  TYR   A CB  1 
ATOM   3372 C CG  . TYR   A 1 439 ? 15.191  -8.609  -11.845 1.00 64.99  ? 976  TYR   A CG  1 
ATOM   3373 C CD1 . TYR   A 1 439 ? 16.256  -9.491  -11.989 1.00 69.02  ? 976  TYR   A CD1 1 
ATOM   3374 C CD2 . TYR   A 1 439 ? 14.703  -7.979  -12.985 1.00 63.70  ? 976  TYR   A CD2 1 
ATOM   3375 C CE1 . TYR   A 1 439 ? 16.809  -9.750  -13.230 1.00 72.01  ? 976  TYR   A CE1 1 
ATOM   3376 C CE2 . TYR   A 1 439 ? 15.252  -8.233  -14.232 1.00 66.85  ? 976  TYR   A CE2 1 
ATOM   3377 C CZ  . TYR   A 1 439 ? 16.305  -9.119  -14.347 1.00 70.77  ? 976  TYR   A CZ  1 
ATOM   3378 O OH  . TYR   A 1 439 ? 16.854  -9.374  -15.583 1.00 73.84  ? 976  TYR   A OH  1 
ATOM   3379 N N   . GLN   A 1 440 ? 12.117  -9.100  -8.131  1.00 54.04  ? 977  GLN   A N   1 
ATOM   3380 C CA  . GLN   A 1 440 ? 11.626  -8.474  -6.913  1.00 53.24  ? 977  GLN   A CA  1 
ATOM   3381 C C   . GLN   A 1 440 ? 11.651  -9.387  -5.693  1.00 55.19  ? 977  GLN   A C   1 
ATOM   3382 O O   . GLN   A 1 440 ? 11.338  -8.922  -4.592  1.00 55.36  ? 977  GLN   A O   1 
ATOM   3383 C CB  . GLN   A 1 440 ? 10.199  -7.955  -7.133  1.00 52.72  ? 977  GLN   A CB  1 
ATOM   3384 C CG  . GLN   A 1 440 ? 10.112  -6.713  -8.010  1.00 50.56  ? 977  GLN   A CG  1 
ATOM   3385 C CD  . GLN   A 1 440 ? 8.681   -6.270  -8.236  1.00 51.81  ? 977  GLN   A CD  1 
ATOM   3386 O OE1 . GLN   A 1 440 ? 7.790   -7.096  -8.436  1.00 54.07  ? 977  GLN   A OE1 1 
ATOM   3387 N NE2 . GLN   A 1 440 ? 8.450   -4.962  -8.197  1.00 50.46  ? 977  GLN   A NE2 1 
ATOM   3388 N N   . ASN   A 1 441 ? 12.014  -10.657 -5.841  1.00 57.30  ? 978  ASN   A N   1 
ATOM   3389 C CA  . ASN   A 1 441 ? 12.008  -11.605 -4.729  1.00 59.57  ? 978  ASN   A CA  1 
ATOM   3390 C C   . ASN   A 1 441 ? 13.426  -12.012 -4.333  1.00 58.40  ? 978  ASN   A C   1 
ATOM   3391 O O   . ASN   A 1 441 ? 13.708  -13.187 -4.087  1.00 59.91  ? 978  ASN   A O   1 
ATOM   3392 C CB  . ASN   A 1 441 ? 11.167  -12.835 -5.072  1.00 63.51  ? 978  ASN   A CB  1 
ATOM   3393 C CG  . ASN   A 1 441 ? 9.712   -12.485 -5.388  1.00 65.78  ? 978  ASN   A CG  1 
ATOM   3394 O OD1 . ASN   A 1 441 ? 9.155   -11.531 -4.840  1.00 65.10  ? 978  ASN   A OD1 1 
ATOM   3395 N ND2 . ASN   A 1 441 ? 9.095   -13.261 -6.278  1.00 67.73  ? 978  ASN   A ND2 1 
ATOM   3396 N N   . GLN   A 1 442 ? 14.330  -11.036 -4.247  1.00 55.56  ? 979  GLN   A N   1 
ATOM   3397 C CA  . GLN   A 1 442 ? 15.757  -11.284 -4.044  1.00 53.11  ? 979  GLN   A CA  1 
ATOM   3398 C C   . GLN   A 1 442 ? 16.267  -10.422 -2.897  1.00 46.60  ? 979  GLN   A C   1 
ATOM   3399 O O   . GLN   A 1 442 ? 16.787  -9.317  -3.116  1.00 45.31  ? 979  GLN   A O   1 
ATOM   3400 C CB  . GLN   A 1 442 ? 16.549  -10.993 -5.317  1.00 56.27  ? 979  GLN   A CB  1 
ATOM   3401 C CG  . GLN   A 1 442 ? 15.911  -11.508 -6.603  1.00 60.76  ? 979  GLN   A CG  1 
ATOM   3402 C CD  . GLN   A 1 442 ? 16.623  -10.993 -7.841  1.00 62.66  ? 979  GLN   A CD  1 
ATOM   3403 O OE1 . GLN   A 1 442 ? 17.446  -10.080 -7.762  1.00 61.96  ? 979  GLN   A OE1 1 
ATOM   3404 N NE2 . GLN   A 1 442 ? 16.317  -11.583 -8.990  1.00 65.04  ? 979  GLN   A NE2 1 
ATOM   3405 N N   . PRO   A 1 443 ? 16.149  -10.897 -1.661  1.00 41.95  ? 980  PRO   A N   1 
ATOM   3406 C CA  . PRO   A 1 443 ? 16.593  -10.100 -0.516  1.00 38.58  ? 980  PRO   A CA  1 
ATOM   3407 C C   . PRO   A 1 443 ? 18.106  -10.085 -0.392  1.00 37.45  ? 980  PRO   A C   1 
ATOM   3408 O O   . PRO   A 1 443 ? 18.797  -11.061 -0.692  1.00 38.32  ? 980  PRO   A O   1 
ATOM   3409 C CB  . PRO   A 1 443 ? 15.959  -10.824 0.675   1.00 38.59  ? 980  PRO   A CB  1 
ATOM   3410 C CG  . PRO   A 1 443 ? 15.917  -12.244 0.226   1.00 40.22  ? 980  PRO   A CG  1 
ATOM   3411 C CD  . PRO   A 1 443 ? 15.612  -12.203 -1.249  1.00 41.79  ? 980  PRO   A CD  1 
ATOM   3412 N N   . TYR   A 1 444 ? 18.616  -8.951  0.067   1.00 36.20  ? 981  TYR   A N   1 
ATOM   3413 C CA  . TYR   A 1 444 ? 20.039  -8.799  0.319   1.00 35.53  ? 981  TYR   A CA  1 
ATOM   3414 C C   . TYR   A 1 444 ? 20.388  -9.302  1.713   1.00 33.50  ? 981  TYR   A C   1 
ATOM   3415 O O   . TYR   A 1 444 ? 19.573  -9.250  2.639   1.00 33.98  ? 981  TYR   A O   1 
ATOM   3416 C CB  . TYR   A 1 444 ? 20.460  -7.339  0.171   1.00 31.54  ? 981  TYR   A CB  1 
ATOM   3417 C CG  . TYR   A 1 444 ? 20.735  -6.923  -1.252  1.00 32.62  ? 981  TYR   A CG  1 
ATOM   3418 C CD1 . TYR   A 1 444 ? 19.725  -6.412  -2.062  1.00 31.25  ? 981  TYR   A CD1 1 
ATOM   3419 C CD2 . TYR   A 1 444 ? 22.010  -7.041  -1.788  1.00 30.82  ? 981  TYR   A CD2 1 
ATOM   3420 C CE1 . TYR   A 1 444 ? 19.981  -6.030  -3.363  1.00 31.09  ? 981  TYR   A CE1 1 
ATOM   3421 C CE2 . TYR   A 1 444 ? 22.276  -6.665  -3.084  1.00 30.65  ? 981  TYR   A CE2 1 
ATOM   3422 C CZ  . TYR   A 1 444 ? 21.262  -6.157  -3.871  1.00 42.46  ? 981  TYR   A CZ  1 
ATOM   3423 O OH  . TYR   A 1 444 ? 21.542  -5.777  -5.165  1.00 30.82  ? 981  TYR   A OH  1 
ATOM   3424 N N   . CYS   A 1 445 ? 21.615  -9.798  1.853   1.00 33.49  ? 982  CYS   A N   1 
ATOM   3425 C CA  . CYS   A 1 445 ? 22.117  -10.266 3.146   1.00 36.63  ? 982  CYS   A CA  1 
ATOM   3426 C C   . CYS   A 1 445 ? 22.837  -9.129  3.876   1.00 32.89  ? 982  CYS   A C   1 
ATOM   3427 O O   . CYS   A 1 445 ? 24.016  -9.207  4.213   1.00 32.78  ? 982  CYS   A O   1 
ATOM   3428 C CB  . CYS   A 1 445 ? 23.029  -11.474 2.952   1.00 34.91  ? 982  CYS   A CB  1 
ATOM   3429 S SG  . CYS   A 1 445 ? 23.510  -12.321 4.484   1.00 36.10  ? 982  CYS   A SG  1 
ATOM   3430 N N   . LEU   A 1 446 ? 22.091  -8.049  4.110   1.00 37.14  ? 983  LEU   A N   1 
ATOM   3431 C CA  . LEU   A 1 446 ? 22.616  -6.831  4.712   1.00 34.34  ? 983  LEU   A CA  1 
ATOM   3432 C C   . LEU   A 1 446 ? 21.667  -6.351  5.799   1.00 34.19  ? 983  LEU   A C   1 
ATOM   3433 O O   . LEU   A 1 446 ? 20.445  -6.364  5.617   1.00 35.60  ? 983  LEU   A O   1 
ATOM   3434 C CB  . LEU   A 1 446 ? 22.796  -5.723  3.663   1.00 31.93  ? 983  LEU   A CB  1 
ATOM   3435 C CG  . LEU   A 1 446 ? 23.716  -6.025  2.481   1.00 30.78  ? 983  LEU   A CG  1 
ATOM   3436 C CD1 . LEU   A 1 446 ? 23.491  -5.024  1.358   1.00 29.59  ? 983  LEU   A CD1 1 
ATOM   3437 C CD2 . LEU   A 1 446 ? 25.173  -6.010  2.927   1.00 29.51  ? 983  LEU   A CD2 1 
ATOM   3438 N N   . ARG   A 1 447 ? 22.230  -5.909  6.920   1.00 33.40  ? 984  ARG   A N   1 
ATOM   3439 C CA  . ARG   A 1 447 ? 21.431  -5.463  8.051   1.00 34.21  ? 984  ARG   A CA  1 
ATOM   3440 C C   . ARG   A 1 447 ? 21.075  -3.987  7.912   1.00 32.60  ? 984  ARG   A C   1 
ATOM   3441 O O   . ARG   A 1 447 ? 21.900  -3.171  7.486   1.00 31.45  ? 984  ARG   A O   1 
ATOM   3442 C CB  . ARG   A 1 447 ? 22.181  -5.703  9.360   1.00 35.77  ? 984  ARG   A CB  1 
ATOM   3443 C CG  . ARG   A 1 447 ? 21.327  -5.512  10.591  1.00 37.79  ? 984  ARG   A CG  1 
ATOM   3444 C CD  . ARG   A 1 447 ? 22.107  -5.843  11.847  1.00 40.75  ? 984  ARG   A CD  1 
ATOM   3445 N NE  . ARG   A 1 447 ? 22.633  -7.205  11.817  1.00 43.31  ? 984  ARG   A NE  1 
ATOM   3446 C CZ  . ARG   A 1 447 ? 21.911  -8.292  12.077  1.00 45.55  ? 984  ARG   A CZ  1 
ATOM   3447 N NH1 . ARG   A 1 447 ? 20.624  -8.181  12.379  1.00 46.73  ? 984  ARG   A NH1 1 
ATOM   3448 N NH2 . ARG   A 1 447 ? 22.474  -9.492  12.028  1.00 46.82  ? 984  ARG   A NH2 1 
ATOM   3449 N N   . ILE   A 1 448 ? 19.839  -3.655  8.279   1.00 32.88  ? 985  ILE   A N   1 
ATOM   3450 C CA  . ILE   A 1 448 ? 19.328  -2.293  8.162   1.00 31.47  ? 985  ILE   A CA  1 
ATOM   3451 C C   . ILE   A 1 448 ? 19.902  -1.440  9.285   1.00 31.25  ? 985  ILE   A C   1 
ATOM   3452 O O   . ILE   A 1 448 ? 19.902  -1.847  10.453  1.00 32.77  ? 985  ILE   A O   1 
ATOM   3453 C CB  . ILE   A 1 448 ? 17.789  -2.291  8.191   1.00 33.41  ? 985  ILE   A CB  1 
ATOM   3454 C CG1 . ILE   A 1 448 ? 17.222  -2.366  6.772   1.00 33.62  ? 985  ILE   A CG1 1 
ATOM   3455 C CG2 . ILE   A 1 448 ? 17.245  -1.065  8.922   1.00 33.61  ? 985  ILE   A CG2 1 
ATOM   3456 C CD1 . ILE   A 1 448 ? 15.726  -2.604  6.730   1.00 31.80  ? 985  ILE   A CD1 1 
ATOM   3457 N N   . GLU   A 1 449 ? 20.404  -0.256  8.932   1.00 30.30  ? 986  GLU   A N   1 
ATOM   3458 C CA  . GLU   A 1 449 ? 20.833  0.731   9.913   1.00 30.46  ? 986  GLU   A CA  1 
ATOM   3459 C C   . GLU   A 1 449 ? 19.751  1.800   9.980   1.00 30.80  ? 986  GLU   A C   1 
ATOM   3460 O O   . GLU   A 1 449 ? 19.656  2.635   9.066   1.00 28.73  ? 986  GLU   A O   1 
ATOM   3461 C CB  . GLU   A 1 449 ? 22.180  1.344   9.523   1.00 30.58  ? 986  GLU   A CB  1 
ATOM   3462 C CG  . GLU   A 1 449 ? 23.059  1.771   10.697  1.00 31.38  ? 986  GLU   A CG  1 
ATOM   3463 C CD  . GLU   A 1 449 ? 22.358  2.711   11.660  1.00 31.77  ? 986  GLU   A CD  1 
ATOM   3464 O OE1 . GLU   A 1 449 ? 22.368  2.426   12.877  1.00 33.59  ? 986  GLU   A OE1 1 
ATOM   3465 O OE2 . GLU   A 1 449 ? 21.796  3.728   11.206  1.00 27.85  ? 986  GLU   A OE2 1 
ATOM   3466 N N   . PRO   A 1 450 ? 18.918  1.823   11.027  1.00 32.49  ? 987  PRO   A N   1 
ATOM   3467 C CA  . PRO   A 1 450 ? 17.714  2.675   10.991  1.00 31.31  ? 987  PRO   A CA  1 
ATOM   3468 C C   . PRO   A 1 450 ? 18.000  4.161   10.833  1.00 30.40  ? 987  PRO   A C   1 
ATOM   3469 O O   . PRO   A 1 450 ? 17.274  4.848   10.102  1.00 29.37  ? 987  PRO   A O   1 
ATOM   3470 C CB  . PRO   A 1 450 ? 17.038  2.368   12.334  1.00 31.32  ? 987  PRO   A CB  1 
ATOM   3471 C CG  . PRO   A 1 450 ? 17.573  1.035   12.736  1.00 32.21  ? 987  PRO   A CG  1 
ATOM   3472 C CD  . PRO   A 1 450 ? 18.980  0.999   12.244  1.00 31.14  ? 987  PRO   A CD  1 
ATOM   3473 N N   . ASP   A 1 451 ? 19.037  4.680   11.497  1.00 30.65  ? 988  ASP   A N   1 
ATOM   3474 C CA  . ASP   A 1 451 ? 19.314  6.112   11.424  1.00 29.52  ? 988  ASP   A CA  1 
ATOM   3475 C C   . ASP   A 1 451 ? 19.796  6.519   10.035  1.00 28.08  ? 988  ASP   A C   1 
ATOM   3476 O O   . ASP   A 1 451 ? 19.374  7.552   9.500   1.00 25.99  ? 988  ASP   A O   1 
ATOM   3477 C CB  . ASP   A 1 451 ? 20.336  6.502   12.491  1.00 30.32  ? 988  ASP   A CB  1 
ATOM   3478 C CG  . ASP   A 1 451 ? 19.740  6.534   13.879  1.00 32.69  ? 988  ASP   A CG  1 
ATOM   3479 O OD1 . ASP   A 1 451 ? 18.542  6.853   13.999  1.00 34.34  ? 988  ASP   A OD1 1 
ATOM   3480 O OD2 . ASP   A 1 451 ? 20.463  6.237   14.850  1.00 34.16  ? 988  ASP   A OD2 1 
ATOM   3481 N N   . MET   A 1 452 ? 20.686  5.729   9.437   1.00 28.61  ? 989  MET   A N   1 
ATOM   3482 C CA  . MET   A 1 452 ? 21.095  6.023   8.070   1.00 29.35  ? 989  MET   A CA  1 
ATOM   3483 C C   . MET   A 1 452 ? 19.935  5.846   7.099   1.00 30.91  ? 989  MET   A C   1 
ATOM   3484 O O   . MET   A 1 452 ? 19.843  6.571   6.101   1.00 24.09  ? 989  MET   A O   1 
ATOM   3485 C CB  . MET   A 1 452 ? 22.274  5.133   7.677   1.00 28.36  ? 989  MET   A CB  1 
ATOM   3486 C CG  . MET   A 1 452 ? 23.481  5.274   8.594   1.00 27.81  ? 989  MET   A CG  1 
ATOM   3487 S SD  . MET   A 1 452 ? 24.813  4.179   8.088   1.00 28.24  ? 989  MET   A SD  1 
ATOM   3488 C CE  . MET   A 1 452 ? 24.997  4.671   6.373   1.00 27.38  ? 989  MET   A CE  1 
ATOM   3489 N N   . ARG   A 1 453 ? 19.037  4.901   7.391   1.00 25.68  ? 990  ARG   A N   1 
ATOM   3490 C CA  . ARG   A 1 453 ? 17.849  4.695   6.571   1.00 33.78  ? 990  ARG   A CA  1 
ATOM   3491 C C   . ARG   A 1 453 ? 16.941  5.924   6.577   1.00 33.71  ? 990  ARG   A C   1 
ATOM   3492 O O   . ARG   A 1 453 ? 16.416  6.323   5.528   1.00 25.53  ? 990  ARG   A O   1 
ATOM   3493 C CB  . ARG   A 1 453 ? 17.096  3.464   7.074   1.00 27.16  ? 990  ARG   A CB  1 
ATOM   3494 C CG  . ARG   A 1 453 ? 15.794  3.189   6.371   1.00 27.76  ? 990  ARG   A CG  1 
ATOM   3495 C CD  . ARG   A 1 453 ? 16.008  2.947   4.900   1.00 38.52  ? 990  ARG   A CD  1 
ATOM   3496 N NE  . ARG   A 1 453 ? 14.963  2.091   4.363   1.00 38.42  ? 990  ARG   A NE  1 
ATOM   3497 C CZ  . ARG   A 1 453 ? 15.130  0.808   4.068   1.00 37.21  ? 990  ARG   A CZ  1 
ATOM   3498 N NH1 . ARG   A 1 453 ? 16.312  0.236   4.242   1.00 36.18  ? 990  ARG   A NH1 1 
ATOM   3499 N NH2 . ARG   A 1 453 ? 14.119  0.103   3.584   1.00 38.34  ? 990  ARG   A NH2 1 
ATOM   3500 N N   . ARG   A 1 454 ? 16.727  6.526   7.754   1.00 33.62  ? 991  ARG   A N   1 
ATOM   3501 C CA  . ARG   A 1 454 ? 15.952  7.763   7.822   1.00 32.81  ? 991  ARG   A CA  1 
ATOM   3502 C C   . ARG   A 1 454 ? 16.661  8.897   7.097   1.00 25.05  ? 991  ARG   A C   1 
ATOM   3503 O O   . ARG   A 1 454 ? 16.013  9.739   6.465   1.00 31.80  ? 991  ARG   A O   1 
ATOM   3504 C CB  . ARG   A 1 454 ? 15.693  8.149   9.279   1.00 32.68  ? 991  ARG   A CB  1 
ATOM   3505 C CG  . ARG   A 1 454 ? 14.615  7.323   9.946   1.00 35.09  ? 991  ARG   A CG  1 
ATOM   3506 C CD  . ARG   A 1 454 ? 14.424  7.707   11.406  1.00 36.57  ? 991  ARG   A CD  1 
ATOM   3507 N NE  . ARG   A 1 454 ? 15.389  7.049   12.283  1.00 37.60  ? 991  ARG   A NE  1 
ATOM   3508 C CZ  . ARG   A 1 454 ? 15.251  5.808   12.747  1.00 39.35  ? 991  ARG   A CZ  1 
ATOM   3509 N NH1 . ARG   A 1 454 ? 14.191  5.081   12.413  1.00 40.19  ? 991  ARG   A NH1 1 
ATOM   3510 N NH2 . ARG   A 1 454 ? 16.175  5.292   13.547  1.00 39.80  ? 991  ARG   A NH2 1 
ATOM   3511 N N   . PHE   A 1 455 ? 17.993  8.937   7.187   1.00 24.44  ? 992  PHE   A N   1 
ATOM   3512 C CA  . PHE   A 1 455 ? 18.772  9.980   6.530   1.00 26.19  ? 992  PHE   A CA  1 
ATOM   3513 C C   . PHE   A 1 455 ? 18.477  10.023  5.035   1.00 27.52  ? 992  PHE   A C   1 
ATOM   3514 O O   . PHE   A 1 455 ? 18.065  11.056  4.496   1.00 25.67  ? 992  PHE   A O   1 
ATOM   3515 C CB  . PHE   A 1 455 ? 20.262  9.741   6.793   1.00 28.53  ? 992  PHE   A CB  1 
ATOM   3516 C CG  . PHE   A 1 455 ? 21.171  10.782  6.196   1.00 26.77  ? 992  PHE   A CG  1 
ATOM   3517 C CD1 . PHE   A 1 455 ? 21.289  12.037  6.775   1.00 26.05  ? 992  PHE   A CD1 1 
ATOM   3518 C CD2 . PHE   A 1 455 ? 21.927  10.497  5.073   1.00 25.10  ? 992  PHE   A CD2 1 
ATOM   3519 C CE1 . PHE   A 1 455 ? 22.132  12.995  6.234   1.00 25.38  ? 992  PHE   A CE1 1 
ATOM   3520 C CE2 . PHE   A 1 455 ? 22.772  11.450  4.529   1.00 25.07  ? 992  PHE   A CE2 1 
ATOM   3521 C CZ  . PHE   A 1 455 ? 22.873  12.701  5.111   1.00 24.96  ? 992  PHE   A CZ  1 
ATOM   3522 N N   . PHE   A 1 456 ? 18.644  8.884   4.356   1.00 23.15  ? 993  PHE   A N   1 
ATOM   3523 C CA  . PHE   A 1 456 ? 18.449  8.849   2.910   1.00 33.88  ? 993  PHE   A CA  1 
ATOM   3524 C C   . PHE   A 1 456 ? 16.977  8.959   2.525   1.00 23.54  ? 993  PHE   A C   1 
ATOM   3525 O O   . PHE   A 1 456 ? 16.661  9.421   1.424   1.00 23.48  ? 993  PHE   A O   1 
ATOM   3526 C CB  . PHE   A 1 456 ? 19.077  7.581   2.333   1.00 23.02  ? 993  PHE   A CB  1 
ATOM   3527 C CG  . PHE   A 1 456 ? 20.573  7.513   2.518   1.00 26.74  ? 993  PHE   A CG  1 
ATOM   3528 C CD1 . PHE   A 1 456 ? 21.407  8.433   1.892   1.00 25.70  ? 993  PHE   A CD1 1 
ATOM   3529 C CD2 . PHE   A 1 456 ? 21.148  6.536   3.316   1.00 26.98  ? 993  PHE   A CD2 1 
ATOM   3530 C CE1 . PHE   A 1 456 ? 22.784  8.376   2.063   1.00 25.42  ? 993  PHE   A CE1 1 
ATOM   3531 C CE2 . PHE   A 1 456 ? 22.522  6.478   3.487   1.00 26.01  ? 993  PHE   A CE2 1 
ATOM   3532 C CZ  . PHE   A 1 456 ? 23.337  7.400   2.860   1.00 25.08  ? 993  PHE   A CZ  1 
ATOM   3533 N N   . GLU   A 1 457 ? 16.062  8.561   3.405   1.00 30.99  ? 994  GLU   A N   1 
ATOM   3534 C CA  . GLU   A 1 457 ? 14.651  8.812   3.134   1.00 30.61  ? 994  GLU   A CA  1 
ATOM   3535 C C   . GLU   A 1 457 ? 14.289  10.286  3.261   1.00 29.61  ? 994  GLU   A C   1 
ATOM   3536 O O   . GLU   A 1 457 ? 13.286  10.716  2.683   1.00 30.93  ? 994  GLU   A O   1 
ATOM   3537 C CB  . GLU   A 1 457 ? 13.769  7.987   4.071   1.00 26.17  ? 994  GLU   A CB  1 
ATOM   3538 C CG  . GLU   A 1 457 ? 13.710  6.526   3.709   1.00 30.24  ? 994  GLU   A CG  1 
ATOM   3539 C CD  . GLU   A 1 457 ? 12.997  5.695   4.747   1.00 31.29  ? 994  GLU   A CD  1 
ATOM   3540 O OE1 . GLU   A 1 457 ? 12.970  6.086   5.936   1.00 31.26  ? 994  GLU   A OE1 1 
ATOM   3541 O OE2 . GLU   A 1 457 ? 12.461  4.638   4.361   1.00 32.74  ? 994  GLU   A OE2 1 
ATOM   3542 N N   . ASN   A 1 458 ? 15.077  11.075  3.990   1.00 28.27  ? 995  ASN   A N   1 
ATOM   3543 C CA  . ASN   A 1 458 ? 14.720  12.461  4.263   1.00 29.11  ? 995  ASN   A CA  1 
ATOM   3544 C C   . ASN   A 1 458 ? 15.613  13.466  3.546   1.00 27.17  ? 995  ASN   A C   1 
ATOM   3545 O O   . ASN   A 1 458 ? 15.510  14.666  3.822   1.00 26.66  ? 995  ASN   A O   1 
ATOM   3546 C CB  . ASN   A 1 458 ? 14.742  12.721  5.773   1.00 31.50  ? 995  ASN   A CB  1 
ATOM   3547 C CG  . ASN   A 1 458 ? 13.771  11.834  6.531   1.00 33.45  ? 995  ASN   A CG  1 
ATOM   3548 O OD1 . ASN   A 1 458 ? 12.645  11.591  6.083   1.00 35.04  ? 995  ASN   A OD1 1 
ATOM   3549 N ND2 . ASN   A 1 458 ? 14.207  11.337  7.680   1.00 33.08  ? 995  ASN   A ND2 1 
ATOM   3550 N N   . LEU   A 1 459 ? 16.477  13.013  2.639   1.00 23.66  ? 996  LEU   A N   1 
ATOM   3551 C CA  . LEU   A 1 459 ? 17.302  13.935  1.866   1.00 26.42  ? 996  LEU   A CA  1 
ATOM   3552 C C   . LEU   A 1 459 ? 16.433  14.941  1.126   1.00 27.74  ? 996  LEU   A C   1 
ATOM   3553 O O   . LEU   A 1 459 ? 15.517  14.561  0.396   1.00 27.44  ? 996  LEU   A O   1 
ATOM   3554 C CB  . LEU   A 1 459 ? 18.166  13.172  0.863   1.00 25.54  ? 996  LEU   A CB  1 
ATOM   3555 C CG  . LEU   A 1 459 ? 19.320  12.334  1.399   1.00 24.83  ? 996  LEU   A CG  1 
ATOM   3556 C CD1 . LEU   A 1 459 ? 19.939  11.516  0.276   1.00 25.62  ? 996  LEU   A CD1 1 
ATOM   3557 C CD2 . LEU   A 1 459 ? 20.356  13.234  2.046   1.00 23.91  ? 996  LEU   A CD2 1 
ATOM   3558 N N   . ASN   A 1 460 ? 16.730  16.228  1.312   1.00 28.19  ? 997  ASN   A N   1 
ATOM   3559 C CA  . ASN   A 1 460 ? 16.059  17.319  0.604   1.00 28.14  ? 997  ASN   A CA  1 
ATOM   3560 C C   . ASN   A 1 460 ? 17.133  18.243  0.045   1.00 29.08  ? 997  ASN   A C   1 
ATOM   3561 O O   . ASN   A 1 460 ? 17.373  19.333  0.584   1.00 27.22  ? 997  ASN   A O   1 
ATOM   3562 C CB  . ASN   A 1 460 ? 15.101  18.079  1.523   1.00 28.00  ? 997  ASN   A CB  1 
ATOM   3563 C CG  . ASN   A 1 460 ? 14.259  19.104  0.774   1.00 29.79  ? 997  ASN   A CG  1 
ATOM   3564 O OD1 . ASN   A 1 460 ? 13.873  18.889  -0.372  1.00 31.09  ? 997  ASN   A OD1 1 
ATOM   3565 N ND2 . ASN   A 1 460 ? 13.965  20.217  1.425   1.00 30.73  ? 997  ASN   A ND2 1 
ATOM   3566 N N   . PRO   A 1 461 ? 17.803  17.841  -1.037  1.00 21.99  ? 998  PRO   A N   1 
ATOM   3567 C CA  . PRO   A 1 461 ? 18.865  18.698  -1.583  1.00 26.72  ? 998  PRO   A CA  1 
ATOM   3568 C C   . PRO   A 1 461 ? 18.368  20.047  -2.085  1.00 27.41  ? 998  PRO   A C   1 
ATOM   3569 O O   . PRO   A 1 461 ? 19.104  21.032  -1.982  1.00 24.66  ? 998  PRO   A O   1 
ATOM   3570 C CB  . PRO   A 1 461 ? 19.457  17.845  -2.716  1.00 21.79  ? 998  PRO   A CB  1 
ATOM   3571 C CG  . PRO   A 1 461 ? 18.400  16.875  -3.067  1.00 22.22  ? 998  PRO   A CG  1 
ATOM   3572 C CD  . PRO   A 1 461 ? 17.678  16.580  -1.786  1.00 22.17  ? 998  PRO   A CD  1 
ATOM   3573 N N   . MET   A 1 462 ? 17.138  20.137  -2.598  1.00 30.93  ? 999  MET   A N   1 
ATOM   3574 C CA  . MET   A 1 462 ? 16.665  21.403  -3.158  1.00 32.42  ? 999  MET   A CA  1 
ATOM   3575 C C   . MET   A 1 462 ? 16.382  22.447  -2.082  1.00 32.12  ? 999  MET   A C   1 
ATOM   3576 O O   . MET   A 1 462 ? 16.443  23.650  -2.362  1.00 33.58  ? 999  MET   A O   1 
ATOM   3577 C CB  . MET   A 1 462 ? 15.408  21.180  -3.998  1.00 34.74  ? 999  MET   A CB  1 
ATOM   3578 C CG  . MET   A 1 462 ? 15.673  20.649  -5.382  1.00 37.05  ? 999  MET   A CG  1 
ATOM   3579 S SD  . MET   A 1 462 ? 14.156  20.468  -6.332  1.00 41.72  ? 999  MET   A SD  1 
ATOM   3580 C CE  . MET   A 1 462 ? 13.860  18.709  -6.161  1.00 42.81  ? 999  MET   A CE  1 
ATOM   3581 N N   . GLY   A 1 463 ? 16.060  22.022  -0.865  1.00 30.15  ? 1000 GLY   A N   1 
ATOM   3582 C CA  . GLY   A 1 463 ? 15.715  22.976  0.173   1.00 29.66  ? 1000 GLY   A CA  1 
ATOM   3583 C C   . GLY   A 1 463 ? 14.360  23.616  -0.055  1.00 29.29  ? 1000 GLY   A C   1 
ATOM   3584 O O   . GLY   A 1 463 ? 13.350  22.914  -0.151  1.00 24.76  ? 1000 GLY   A O   1 
ATOM   3585 N N   . SER   A 1 464 ? 14.321  24.946  -0.135  1.00 27.02  ? 1001 SER   A N   1 
ATOM   3586 C CA  . SER   A 1 464 ? 13.106  25.663  -0.500  1.00 26.87  ? 1001 SER   A CA  1 
ATOM   3587 C C   . SER   A 1 464 ? 13.077  26.066  -1.966  1.00 29.49  ? 1001 SER   A C   1 
ATOM   3588 O O   . SER   A 1 464 ? 12.070  26.612  -2.423  1.00 31.76  ? 1001 SER   A O   1 
ATOM   3589 C CB  . SER   A 1 464 ? 12.942  26.918  0.361   1.00 25.99  ? 1001 SER   A CB  1 
ATOM   3590 O OG  . SER   A 1 464 ? 12.775  26.584  1.721   1.00 36.94  ? 1001 SER   A OG  1 
ATOM   3591 N N   . ALA   A 1 465 ? 14.152  25.821  -2.705  1.00 29.08  ? 1002 ALA   A N   1 
ATOM   3592 C CA  . ALA   A 1 465 ? 14.193  26.185  -4.108  1.00 30.46  ? 1002 ALA   A CA  1 
ATOM   3593 C C   . ALA   A 1 465 ? 13.317  25.249  -4.931  1.00 31.78  ? 1002 ALA   A C   1 
ATOM   3594 O O   . ALA   A 1 465 ? 12.994  24.129  -4.521  1.00 31.46  ? 1002 ALA   A O   1 
ATOM   3595 C CB  . ALA   A 1 465 ? 15.630  26.139  -4.628  1.00 30.68  ? 1002 ALA   A CB  1 
ATOM   3596 N N   . SER   A 1 466 ? 12.926  25.730  -6.109  1.00 33.64  ? 1003 SER   A N   1 
ATOM   3597 C CA  . SER   A 1 466 ? 12.311  24.867  -7.104  1.00 35.53  ? 1003 SER   A CA  1 
ATOM   3598 C C   . SER   A 1 466 ? 13.392  24.136  -7.893  1.00 36.00  ? 1003 SER   A C   1 
ATOM   3599 O O   . SER   A 1 466 ? 14.563  24.519  -7.881  1.00 34.25  ? 1003 SER   A O   1 
ATOM   3600 C CB  . SER   A 1 466 ? 11.430  25.680  -8.049  1.00 36.99  ? 1003 SER   A CB  1 
ATOM   3601 O OG  . SER   A 1 466 ? 12.217  26.608  -8.774  1.00 37.31  ? 1003 SER   A OG  1 
ATOM   3602 N N   . GLU   A 1 467 ? 12.984  23.062  -8.576  1.00 43.98  ? 1004 GLU   A N   1 
ATOM   3603 C CA  . GLU   A 1 467 ? 13.913  22.323  -9.426  1.00 45.16  ? 1004 GLU   A CA  1 
ATOM   3604 C C   . GLU   A 1 467 ? 14.622  23.265  -10.390 1.00 43.32  ? 1004 GLU   A C   1 
ATOM   3605 O O   . GLU   A 1 467 ? 15.842  23.184  -10.577 1.00 42.12  ? 1004 GLU   A O   1 
ATOM   3606 C CB  . GLU   A 1 467 ? 13.173  21.219  -10.188 1.00 50.15  ? 1004 GLU   A CB  1 
ATOM   3607 C CG  . GLU   A 1 467 ? 14.087  20.163  -10.813 1.00 53.26  ? 1004 GLU   A CG  1 
ATOM   3608 C CD  . GLU   A 1 467 ? 13.590  18.739  -10.591 1.00 56.78  ? 1004 GLU   A CD  1 
ATOM   3609 O OE1 . GLU   A 1 467 ? 13.916  17.857  -11.417 1.00 57.37  ? 1004 GLU   A OE1 1 
ATOM   3610 O OE2 . GLU   A 1 467 ? 12.878  18.499  -9.589  1.00 58.27  ? 1004 GLU   A OE2 1 
ATOM   3611 N N   . LYS   A 1 468 ? 13.870  24.192  -10.987 1.00 42.90  ? 1005 LYS   A N   1 
ATOM   3612 C CA  . LYS   A 1 468 ? 14.478  25.193  -11.856 1.00 41.30  ? 1005 LYS   A CA  1 
ATOM   3613 C C   . LYS   A 1 468 ? 15.448  26.073  -11.080 1.00 38.94  ? 1005 LYS   A C   1 
ATOM   3614 O O   . LYS   A 1 468 ? 16.590  26.286  -11.505 1.00 37.48  ? 1005 LYS   A O   1 
ATOM   3615 C CB  . LYS   A 1 468 ? 13.395  26.046  -12.514 1.00 43.99  ? 1005 LYS   A CB  1 
ATOM   3616 C CG  . LYS   A 1 468 ? 13.956  27.112  -13.422 1.00 46.00  ? 1005 LYS   A CG  1 
ATOM   3617 C CD  . LYS   A 1 468 ? 14.824  26.470  -14.480 1.00 46.91  ? 1005 LYS   A CD  1 
ATOM   3618 C CE  . LYS   A 1 468 ? 15.751  27.476  -15.117 1.00 48.73  ? 1005 LYS   A CE  1 
ATOM   3619 N NZ  . LYS   A 1 468 ? 16.768  26.788  -15.951 1.00 48.12  ? 1005 LYS   A NZ  1 
ATOM   3620 N N   . GLU   A 1 469 ? 15.006  26.598  -9.934  1.00 38.54  ? 1006 GLU   A N   1 
ATOM   3621 C CA  . GLU   A 1 469 ? 15.877  27.451  -9.134  1.00 37.08  ? 1006 GLU   A CA  1 
ATOM   3622 C C   . GLU   A 1 469 ? 17.124  26.700  -8.684  1.00 35.05  ? 1006 GLU   A C   1 
ATOM   3623 O O   . GLU   A 1 469 ? 18.234  27.243  -8.732  1.00 34.64  ? 1006 GLU   A O   1 
ATOM   3624 C CB  . GLU   A 1 469 ? 15.115  27.999  -7.928  1.00 37.03  ? 1006 GLU   A CB  1 
ATOM   3625 C CG  . GLU   A 1 469 ? 14.129  29.104  -8.264  1.00 37.79  ? 1006 GLU   A CG  1 
ATOM   3626 C CD  . GLU   A 1 469 ? 13.442  29.658  -7.036  1.00 37.88  ? 1006 GLU   A CD  1 
ATOM   3627 O OE1 . GLU   A 1 469 ? 13.456  28.978  -5.991  1.00 37.51  ? 1006 GLU   A OE1 1 
ATOM   3628 O OE2 . GLU   A 1 469 ? 12.897  30.777  -7.111  1.00 39.33  ? 1006 GLU   A OE2 1 
ATOM   3629 N N   . PHE   A 1 470 ? 16.965  25.447  -8.254  1.00 34.02  ? 1007 PHE   A N   1 
ATOM   3630 C CA  . PHE   A 1 470 ? 18.113  24.684  -7.773  1.00 32.65  ? 1007 PHE   A CA  1 
ATOM   3631 C C   . PHE   A 1 470 ? 19.088  24.384  -8.904  1.00 31.05  ? 1007 PHE   A C   1 
ATOM   3632 O O   . PHE   A 1 470 ? 20.309  24.421  -8.704  1.00 30.78  ? 1007 PHE   A O   1 
ATOM   3633 C CB  . PHE   A 1 470 ? 17.646  23.392  -7.105  1.00 31.09  ? 1007 PHE   A CB  1 
ATOM   3634 C CG  . PHE   A 1 470 ? 18.707  22.717  -6.285  1.00 33.65  ? 1007 PHE   A CG  1 
ATOM   3635 C CD1 . PHE   A 1 470 ? 19.266  23.357  -5.185  1.00 34.16  ? 1007 PHE   A CD1 1 
ATOM   3636 C CD2 . PHE   A 1 470 ? 19.139  21.437  -6.600  1.00 32.86  ? 1007 PHE   A CD2 1 
ATOM   3637 C CE1 . PHE   A 1 470 ? 20.249  22.736  -4.421  1.00 33.39  ? 1007 PHE   A CE1 1 
ATOM   3638 C CE2 . PHE   A 1 470 ? 20.122  20.807  -5.837  1.00 32.70  ? 1007 PHE   A CE2 1 
ATOM   3639 C CZ  . PHE   A 1 470 ? 20.677  21.459  -4.748  1.00 33.18  ? 1007 PHE   A CZ  1 
ATOM   3640 N N   . THR   A 1 471 ? 18.568  24.101  -10.101 1.00 29.99  ? 1008 THR   A N   1 
ATOM   3641 C CA  . THR   A 1 471 ? 19.432  23.825  -11.246 1.00 30.10  ? 1008 THR   A CA  1 
ATOM   3642 C C   . THR   A 1 471 ? 20.305  25.031  -11.578 1.00 31.54  ? 1008 THR   A C   1 
ATOM   3643 O O   . THR   A 1 471 ? 21.523  24.903  -11.749 1.00 29.55  ? 1008 THR   A O   1 
ATOM   3644 C CB  . THR   A 1 471 ? 18.583  23.421  -12.452 1.00 29.71  ? 1008 THR   A CB  1 
ATOM   3645 O OG1 . THR   A 1 471 ? 17.763  22.299  -12.103 1.00 29.42  ? 1008 THR   A OG1 1 
ATOM   3646 C CG2 . THR   A 1 471 ? 19.467  23.053  -13.637 1.00 29.42  ? 1008 THR   A CG2 1 
ATOM   3647 N N   . ASP   A 1 472 ? 19.694  26.218  -11.670 1.00 32.05  ? 1009 ASP   A N   1 
ATOM   3648 C CA  . ASP   A 1 472 ? 20.467  27.429  -11.926 1.00 33.22  ? 1009 ASP   A CA  1 
ATOM   3649 C C   . ASP   A 1 472 ? 21.497  27.670  -10.830 1.00 34.29  ? 1009 ASP   A C   1 
ATOM   3650 O O   . ASP   A 1 472 ? 22.635  28.064  -11.112 1.00 31.96  ? 1009 ASP   A O   1 
ATOM   3651 C CB  . ASP   A 1 472 ? 19.534  28.632  -12.053 1.00 34.88  ? 1009 ASP   A CB  1 
ATOM   3652 C CG  . ASP   A 1 472 ? 18.803  28.660  -13.373 1.00 36.51  ? 1009 ASP   A CG  1 
ATOM   3653 O OD1 . ASP   A 1 472 ? 19.178  27.871  -14.267 1.00 36.18  ? 1009 ASP   A OD1 1 
ATOM   3654 O OD2 . ASP   A 1 472 ? 17.855  29.462  -13.516 1.00 38.38  ? 1009 ASP   A OD2 1 
ATOM   3655 N N   . TYR   A 1 473 ? 21.118  27.433  -9.572  1.00 34.75  ? 1010 TYR   A N   1 
ATOM   3656 C CA  . TYR   A 1 473 ? 22.045  27.653  -8.468  1.00 33.89  ? 1010 TYR   A CA  1 
ATOM   3657 C C   . TYR   A 1 473 ? 23.256  26.735  -8.569  1.00 32.67  ? 1010 TYR   A C   1 
ATOM   3658 O O   . TYR   A 1 473 ? 24.391  27.165  -8.321  1.00 30.50  ? 1010 TYR   A O   1 
ATOM   3659 C CB  . TYR   A 1 473 ? 21.328  27.449  -7.134  1.00 33.77  ? 1010 TYR   A CB  1 
ATOM   3660 C CG  . TYR   A 1 473 ? 22.258  27.074  -6.004  1.00 30.89  ? 1010 TYR   A CG  1 
ATOM   3661 C CD1 . TYR   A 1 473 ? 23.003  28.041  -5.336  1.00 31.72  ? 1010 TYR   A CD1 1 
ATOM   3662 C CD2 . TYR   A 1 473 ? 22.395  25.749  -5.607  1.00 30.21  ? 1010 TYR   A CD2 1 
ATOM   3663 C CE1 . TYR   A 1 473 ? 23.860  27.695  -4.295  1.00 31.40  ? 1010 TYR   A CE1 1 
ATOM   3664 C CE2 . TYR   A 1 473 ? 23.246  25.393  -4.575  1.00 29.41  ? 1010 TYR   A CE2 1 
ATOM   3665 C CZ  . TYR   A 1 473 ? 23.976  26.367  -3.921  1.00 33.46  ? 1010 TYR   A CZ  1 
ATOM   3666 O OH  . TYR   A 1 473 ? 24.818  25.998  -2.892  1.00 30.03  ? 1010 TYR   A OH  1 
ATOM   3667 N N   . LEU   A 1 474 ? 23.034  25.464  -8.920  1.00 31.48  ? 1011 LEU   A N   1 
ATOM   3668 C CA  . LEU   A 1 474 ? 24.145  24.526  -9.064  1.00 31.53  ? 1011 LEU   A CA  1 
ATOM   3669 C C   . LEU   A 1 474 ? 25.116  24.993  -10.138 1.00 32.14  ? 1011 LEU   A C   1 
ATOM   3670 O O   . LEU   A 1 474 ? 26.326  25.080  -9.902  1.00 28.71  ? 1011 LEU   A O   1 
ATOM   3671 C CB  . LEU   A 1 474 ? 23.626  23.125  -9.397  1.00 30.61  ? 1011 LEU   A CB  1 
ATOM   3672 C CG  . LEU   A 1 474 ? 22.792  22.394  -8.346  1.00 30.54  ? 1011 LEU   A CG  1 
ATOM   3673 C CD1 . LEU   A 1 474 ? 22.115  21.171  -8.956  1.00 30.20  ? 1011 LEU   A CD1 1 
ATOM   3674 C CD2 . LEU   A 1 474 ? 23.656  21.996  -7.169  1.00 30.05  ? 1011 LEU   A CD2 1 
ATOM   3675 N N   . PHE   A 1 475 ? 24.606  25.300  -11.331 1.00 32.24  ? 1012 PHE   A N   1 
ATOM   3676 C CA  . PHE   A 1 475 ? 25.517  25.722  -12.386 1.00 33.24  ? 1012 PHE   A CA  1 
ATOM   3677 C C   . PHE   A 1 475 ? 26.234  27.008  -12.013 1.00 35.10  ? 1012 PHE   A C   1 
ATOM   3678 O O   . PHE   A 1 475 ? 27.417  27.181  -12.331 1.00 35.56  ? 1012 PHE   A O   1 
ATOM   3679 C CB  . PHE   A 1 475 ? 24.789  25.913  -13.704 1.00 35.13  ? 1012 PHE   A CB  1 
ATOM   3680 C CG  . PHE   A 1 475 ? 25.680  26.384  -14.795 1.00 37.03  ? 1012 PHE   A CG  1 
ATOM   3681 C CD1 . PHE   A 1 475 ? 26.715  25.589  -15.242 1.00 37.30  ? 1012 PHE   A CD1 1 
ATOM   3682 C CD2 . PHE   A 1 475 ? 25.479  27.615  -15.387 1.00 38.83  ? 1012 PHE   A CD2 1 
ATOM   3683 C CE1 . PHE   A 1 475 ? 27.548  26.027  -16.245 1.00 38.81  ? 1012 PHE   A CE1 1 
ATOM   3684 C CE2 . PHE   A 1 475 ? 26.287  28.033  -16.419 1.00 40.67  ? 1012 PHE   A CE2 1 
ATOM   3685 C CZ  . PHE   A 1 475 ? 27.343  27.229  -16.828 1.00 40.36  ? 1012 PHE   A CZ  1 
ATOM   3686 N N   . ASN   A 1 476 ? 25.524  27.945  -11.383 1.00 36.48  ? 1013 ASN   A N   1 
ATOM   3687 C CA  . ASN   A 1 476 ? 26.181  29.166  -10.932 1.00 38.05  ? 1013 ASN   A CA  1 
ATOM   3688 C C   . ASN   A 1 476 ? 27.300  28.854  -9.950  1.00 35.65  ? 1013 ASN   A C   1 
ATOM   3689 O O   . ASN   A 1 476 ? 28.371  29.468  -10.006 1.00 35.79  ? 1013 ASN   A O   1 
ATOM   3690 C CB  . ASN   A 1 476 ? 25.173  30.125  -10.296 1.00 39.01  ? 1013 ASN   A CB  1 
ATOM   3691 C CG  . ASN   A 1 476 ? 24.295  30.810  -11.318 1.00 38.48  ? 1013 ASN   A CG  1 
ATOM   3692 O OD1 . ASN   A 1 476 ? 24.681  30.974  -12.470 1.00 38.47  ? 1013 ASN   A OD1 1 
ATOM   3693 N ND2 . ASN   A 1 476 ? 23.103  31.210  -10.901 1.00 39.10  ? 1013 ASN   A ND2 1 
ATOM   3694 N N   . LYS   A 1 477 ? 27.067  27.913  -9.028  1.00 33.52  ? 1014 LYS   A N   1 
ATOM   3695 C CA  . LYS   A 1 477 ? 28.122  27.524  -8.098  1.00 33.51  ? 1014 LYS   A CA  1 
ATOM   3696 C C   . LYS   A 1 477 ? 29.256  26.811  -8.819  1.00 32.98  ? 1014 LYS   A C   1 
ATOM   3697 O O   . LYS   A 1 477 ? 30.420  26.941  -8.426  1.00 33.48  ? 1014 LYS   A O   1 
ATOM   3698 C CB  . LYS   A 1 477 ? 27.553  26.641  -6.986  1.00 32.82  ? 1014 LYS   A CB  1 
ATOM   3699 C CG  . LYS   A 1 477 ? 28.585  26.160  -5.974  1.00 31.40  ? 1014 LYS   A CG  1 
ATOM   3700 C CD  . LYS   A 1 477 ? 29.196  27.320  -5.221  1.00 31.93  ? 1014 LYS   A CD  1 
ATOM   3701 C CE  . LYS   A 1 477 ? 28.145  28.044  -4.391  1.00 32.12  ? 1014 LYS   A CE  1 
ATOM   3702 N NZ  . LYS   A 1 477 ? 28.761  28.995  -3.425  1.00 32.81  ? 1014 LYS   A NZ  1 
ATOM   3703 N N   . SER   A 1 478 ? 28.936  26.069  -9.880  1.00 31.82  ? 1015 SER   A N   1 
ATOM   3704 C CA  . SER   A 1 478 ? 29.972  25.422  -10.678 1.00 31.84  ? 1015 SER   A CA  1 
ATOM   3705 C C   . SER   A 1 478 ? 30.849  26.453  -11.374 1.00 33.50  ? 1015 SER   A C   1 
ATOM   3706 O O   . SER   A 1 478 ? 32.080  26.336  -11.375 1.00 33.69  ? 1015 SER   A O   1 
ATOM   3707 C CB  . SER   A 1 478 ? 29.335  24.483  -11.702 1.00 31.26  ? 1015 SER   A CB  1 
ATOM   3708 O OG  . SER   A 1 478 ? 30.319  23.869  -12.514 1.00 30.92  ? 1015 SER   A OG  1 
ATOM   3709 N N   . LEU   A 1 479 ? 30.228  27.462  -11.993 1.00 35.12  ? 1016 LEU   A N   1 
ATOM   3710 C CA  . LEU   A 1 479 ? 31.001  28.531  -12.616 1.00 37.08  ? 1016 LEU   A CA  1 
ATOM   3711 C C   . LEU   A 1 479 ? 31.924  29.194  -11.603 1.00 39.35  ? 1016 LEU   A C   1 
ATOM   3712 O O   . LEU   A 1 479 ? 33.048  29.586  -11.936 1.00 35.36  ? 1016 LEU   A O   1 
ATOM   3713 C CB  . LEU   A 1 479 ? 30.063  29.568  -13.241 1.00 36.98  ? 1016 LEU   A CB  1 
ATOM   3714 C CG  . LEU   A 1 479 ? 29.339  29.192  -14.534 1.00 36.03  ? 1016 LEU   A CG  1 
ATOM   3715 C CD1 . LEU   A 1 479 ? 28.456  30.336  -14.989 1.00 36.93  ? 1016 LEU   A CD1 1 
ATOM   3716 C CD2 . LEU   A 1 479 ? 30.340  28.825  -15.616 1.00 35.81  ? 1016 LEU   A CD2 1 
ATOM   3717 N N   . GLU   A 1 480 ? 31.469  29.301  -10.353 1.00 39.00  ? 1017 GLU   A N   1 
ATOM   3718 C CA  . GLU   A 1 480 ? 32.246  29.974  -9.318  1.00 39.36  ? 1017 GLU   A CA  1 
ATOM   3719 C C   . GLU   A 1 480 ? 33.470  29.158  -8.913  1.00 38.78  ? 1017 GLU   A C   1 
ATOM   3720 O O   . GLU   A 1 480 ? 34.546  29.719  -8.678  1.00 35.45  ? 1017 GLU   A O   1 
ATOM   3721 C CB  . GLU   A 1 480 ? 31.351  30.246  -8.106  1.00 38.30  ? 1017 GLU   A CB  1 
ATOM   3722 C CG  . GLU   A 1 480 ? 32.036  30.917  -6.934  1.00 38.70  ? 1017 GLU   A CG  1 
ATOM   3723 C CD  . GLU   A 1 480 ? 31.084  31.180  -5.779  1.00 39.07  ? 1017 GLU   A CD  1 
ATOM   3724 O OE1 . GLU   A 1 480 ? 29.878  30.883  -5.920  1.00 38.80  ? 1017 GLU   A OE1 1 
ATOM   3725 O OE2 . GLU   A 1 480 ? 31.539  31.683  -4.730  1.00 40.01  ? 1017 GLU   A OE2 1 
ATOM   3726 N N   . ILE   A 1 481 ? 33.330  27.836  -8.816  1.00 36.92  ? 1018 ILE   A N   1 
ATOM   3727 C CA  . ILE   A 1 481 ? 34.420  27.040  -8.266  1.00 34.95  ? 1018 ILE   A CA  1 
ATOM   3728 C C   . ILE   A 1 481 ? 35.445  26.678  -9.336  1.00 34.78  ? 1018 ILE   A C   1 
ATOM   3729 O O   . ILE   A 1 481 ? 36.618  26.450  -9.014  1.00 35.56  ? 1018 ILE   A O   1 
ATOM   3730 C CB  . ILE   A 1 481 ? 33.863  25.789  -7.567  1.00 32.91  ? 1018 ILE   A CB  1 
ATOM   3731 C CG1 . ILE   A 1 481 ? 33.125  24.876  -8.553  1.00 31.42  ? 1018 ILE   A CG1 1 
ATOM   3732 C CG2 . ILE   A 1 481 ? 32.951  26.180  -6.411  1.00 33.38  ? 1018 ILE   A CG2 1 
ATOM   3733 C CD1 . ILE   A 1 481 ? 32.557  23.609  -7.915  1.00 29.95  ? 1018 ILE   A CD1 1 
ATOM   3734 N N   . GLU   A 1 482 ? 35.037  26.626  -10.607 1.00 32.74  ? 1019 GLU   A N   1 
ATOM   3735 C CA  . GLU   A 1 482 ? 35.960  26.451  -11.732 1.00 33.47  ? 1019 GLU   A CA  1 
ATOM   3736 C C   . GLU   A 1 482 ? 35.513  27.370  -12.858 1.00 37.99  ? 1019 GLU   A C   1 
ATOM   3737 O O   . GLU   A 1 482 ? 34.791  26.956  -13.773 1.00 36.83  ? 1019 GLU   A O   1 
ATOM   3738 C CB  . GLU   A 1 482 ? 36.022  24.991  -12.193 1.00 32.28  ? 1019 GLU   A CB  1 
ATOM   3739 C CG  . GLU   A 1 482 ? 36.590  24.033  -11.156 1.00 36.22  ? 1019 GLU   A CG  1 
ATOM   3740 C CD  . GLU   A 1 482 ? 36.945  22.671  -11.731 1.00 34.54  ? 1019 GLU   A CD  1 
ATOM   3741 O OE1 . GLU   A 1 482 ? 36.882  22.510  -12.965 1.00 34.34  ? 1019 GLU   A OE1 1 
ATOM   3742 O OE2 . GLU   A 1 482 ? 37.293  21.760  -10.946 1.00 32.89  ? 1019 GLU   A OE2 1 
ATOM   3743 N N   . PRO   A 1 483 ? 35.903  28.646  -12.804 1.00 39.56  ? 1020 PRO   A N   1 
ATOM   3744 C CA  . PRO   A 1 483 ? 35.471  29.599  -13.836 1.00 41.55  ? 1020 PRO   A CA  1 
ATOM   3745 C C   . PRO   A 1 483 ? 35.944  29.193  -15.223 1.00 41.78  ? 1020 PRO   A C   1 
ATOM   3746 O O   . PRO   A 1 483 ? 36.939  28.481  -15.377 1.00 40.60  ? 1020 PRO   A O   1 
ATOM   3747 C CB  . PRO   A 1 483 ? 36.114  30.921  -13.394 1.00 43.32  ? 1020 PRO   A CB  1 
ATOM   3748 C CG  . PRO   A 1 483 ? 36.349  30.760  -11.928 1.00 42.23  ? 1020 PRO   A CG  1 
ATOM   3749 C CD  . PRO   A 1 483 ? 36.646  29.300  -11.716 1.00 40.14  ? 1020 PRO   A CD  1 
ATOM   3750 N N   . ARG   A 1 484 ? 35.201  29.650  -16.235 1.00 44.00  ? 1021 ARG   A N   1 
ATOM   3751 C CA  . ARG   A 1 484 ? 35.535  29.381  -17.631 1.00 48.02  ? 1021 ARG   A CA  1 
ATOM   3752 C C   . ARG   A 1 484 ? 36.988  29.749  -17.930 1.00 51.45  ? 1021 ARG   A C   1 
ATOM   3753 O O   . ARG   A 1 484 ? 37.473  30.811  -17.526 1.00 53.49  ? 1021 ARG   A O   1 
ATOM   3754 C CB  . ARG   A 1 484 ? 34.588  30.158  -18.561 1.00 49.65  ? 1021 ARG   A CB  1 
ATOM   3755 C CG  . ARG   A 1 484 ? 33.276  29.441  -18.939 1.00 48.39  ? 1021 ARG   A CG  1 
ATOM   3756 C CD  . ARG   A 1 484 ? 32.439  30.261  -19.929 1.00 50.19  ? 1021 ARG   A CD  1 
ATOM   3757 N NE  . ARG   A 1 484 ? 32.681  29.913  -21.332 1.00 52.09  ? 1021 ARG   A NE  1 
ATOM   3758 C CZ  . ARG   A 1 484 ? 32.472  30.730  -22.365 1.00 54.11  ? 1021 ARG   A CZ  1 
ATOM   3759 N NH1 . ARG   A 1 484 ? 32.056  31.977  -22.166 1.00 55.38  ? 1021 ARG   A NH1 1 
ATOM   3760 N NH2 . ARG   A 1 484 ? 32.706  30.303  -23.603 1.00 54.81  ? 1021 ARG   A NH2 1 
ATOM   3761 N N   . ASN   A 1 485 ? 37.686  28.839  -18.614 1.00 51.99  ? 1022 ASN   A N   1 
ATOM   3762 C CA  . ASN   A 1 485 ? 39.019  29.090  -19.157 1.00 55.42  ? 1022 ASN   A CA  1 
ATOM   3763 C C   . ASN   A 1 485 ? 40.050  29.387  -18.069 1.00 58.49  ? 1022 ASN   A C   1 
ATOM   3764 O O   . ASN   A 1 485 ? 41.064  30.040  -18.330 1.00 60.33  ? 1022 ASN   A O   1 
ATOM   3765 C CB  . ASN   A 1 485 ? 38.983  30.220  -20.188 1.00 56.76  ? 1022 ASN   A CB  1 
ATOM   3766 C CG  . ASN   A 1 485 ? 37.965  29.973  -21.279 1.00 56.36  ? 1022 ASN   A CG  1 
ATOM   3767 O OD1 . ASN   A 1 485 ? 37.020  30.742  -21.445 1.00 57.28  ? 1022 ASN   A OD1 1 
ATOM   3768 N ND2 . ASN   A 1 485 ? 38.154  28.894  -22.030 1.00 55.00  ? 1022 ASN   A ND2 1 
ATOM   3769 N N   . CYS   A 1 486 ? 39.804  28.920  -16.845 1.00 59.13  ? 1023 CYS   A N   1 
ATOM   3770 C CA  . CYS   A 1 486 ? 40.817  28.977  -15.802 1.00 60.97  ? 1023 CYS   A CA  1 
ATOM   3771 C C   . CYS   A 1 486 ? 41.775  27.809  -15.984 1.00 61.85  ? 1023 CYS   A C   1 
ATOM   3772 O O   . CYS   A 1 486 ? 41.376  26.717  -16.400 1.00 60.71  ? 1023 CYS   A O   1 
ATOM   3773 C CB  . CYS   A 1 486 ? 40.180  28.945  -14.407 1.00 59.50  ? 1023 CYS   A CB  1 
ATOM   3774 S SG  . CYS   A 1 486 ? 40.060  27.319  -13.561 1.00 57.81  ? 1023 CYS   A SG  1 
ATOM   3775 N N   . LYS   A 1 487 ? 43.053  28.056  -15.703 1.00 64.06  ? 1024 LYS   A N   1 
ATOM   3776 C CA  . LYS   A 1 487 ? 44.064  27.011  -15.771 1.00 64.98  ? 1024 LYS   A CA  1 
ATOM   3777 C C   . LYS   A 1 487 ? 44.389  26.416  -14.408 1.00 63.78  ? 1024 LYS   A C   1 
ATOM   3778 O O   . LYS   A 1 487 ? 45.025  25.359  -14.346 1.00 63.90  ? 1024 LYS   A O   1 
ATOM   3779 C CB  . LYS   A 1 487 ? 45.341  27.551  -16.423 1.00 68.28  ? 1024 LYS   A CB  1 
ATOM   3780 C CG  . LYS   A 1 487 ? 45.155  27.921  -17.882 1.00 70.30  ? 1024 LYS   A CG  1 
ATOM   3781 C CD  . LYS   A 1 487 ? 46.423  28.490  -18.476 1.00 73.70  ? 1024 LYS   A CD  1 
ATOM   3782 C CE  . LYS   A 1 487 ? 46.230  28.852  -19.936 1.00 75.38  ? 1024 LYS   A CE  1 
ATOM   3783 N NZ  . LYS   A 1 487 ? 47.454  29.484  -20.498 1.00 78.76  ? 1024 LYS   A NZ  1 
ATOM   3784 N N   . GLN   A 1 488 ? 43.964  27.059  -13.330 1.00 62.91  ? 1025 GLN   A N   1 
ATOM   3785 C CA  . GLN   A 1 488 ? 44.129  26.535  -11.982 1.00 62.71  ? 1025 GLN   A CA  1 
ATOM   3786 C C   . GLN   A 1 488 ? 42.877  26.860  -11.181 1.00 61.70  ? 1025 GLN   A C   1 
ATOM   3787 O O   . GLN   A 1 488 ? 42.494  28.034  -11.091 1.00 63.32  ? 1025 GLN   A O   1 
ATOM   3788 C CB  . GLN   A 1 488 ? 45.369  27.128  -11.311 1.00 66.21  ? 1025 GLN   A CB  1 
ATOM   3789 C CG  . GLN   A 1 488 ? 45.482  26.828  -9.819  1.00 66.65  ? 1025 GLN   A CG  1 
ATOM   3790 C CD  . GLN   A 1 488 ? 46.627  27.577  -9.162  1.00 70.18  ? 1025 GLN   A CD  1 
ATOM   3791 O OE1 . GLN   A 1 488 ? 47.376  28.292  -9.829  1.00 72.70  ? 1025 GLN   A OE1 1 
ATOM   3792 N NE2 . GLN   A 1 488 ? 46.766  27.422  -7.848  1.00 70.24  ? 1025 GLN   A NE2 1 
ATOM   3793 N N   . PRO   A 1 489 ? 42.207  25.862  -10.607 1.00 58.69  ? 1026 PRO   A N   1 
ATOM   3794 C CA  . PRO   A 1 489 ? 40.980  26.124  -9.845  1.00 56.08  ? 1026 PRO   A CA  1 
ATOM   3795 C C   . PRO   A 1 489 ? 41.234  27.122  -8.730  1.00 55.58  ? 1026 PRO   A C   1 
ATOM   3796 O O   . PRO   A 1 489 ? 42.241  27.023  -8.014  1.00 55.28  ? 1026 PRO   A O   1 
ATOM   3797 C CB  . PRO   A 1 489 ? 40.604  24.742  -9.286  1.00 54.84  ? 1026 PRO   A CB  1 
ATOM   3798 C CG  . PRO   A 1 489 ? 41.841  23.906  -9.430  1.00 55.53  ? 1026 PRO   A CG  1 
ATOM   3799 C CD  . PRO   A 1 489 ? 42.539  24.430  -10.639 1.00 57.47  ? 1026 PRO   A CD  1 
ATOM   3800 N N   . PRO   A 1 490 ? 40.357  28.114  -8.574  1.00 55.45  ? 1027 PRO   A N   1 
ATOM   3801 C CA  . PRO   A 1 490 ? 40.573  29.140  -7.548  1.00 55.43  ? 1027 PRO   A CA  1 
ATOM   3802 C C   . PRO   A 1 490 ? 40.602  28.541  -6.151  1.00 53.75  ? 1027 PRO   A C   1 
ATOM   3803 O O   . PRO   A 1 490 ? 40.017  27.490  -5.879  1.00 51.15  ? 1027 PRO   A O   1 
ATOM   3804 C CB  . PRO   A 1 490 ? 39.376  30.082  -7.727  1.00 55.58  ? 1027 PRO   A CB  1 
ATOM   3805 C CG  . PRO   A 1 490 ? 38.935  29.866  -9.131  1.00 55.76  ? 1027 PRO   A CG  1 
ATOM   3806 C CD  . PRO   A 1 490 ? 39.190  28.414  -9.421  1.00 55.04  ? 1027 PRO   A CD  1 
ATOM   3807 N N   . ARG   A 1 491 ? 41.287  29.246  -5.253  1.00 53.92  ? 1028 ARG   A N   1 
ATOM   3808 C CA  . ARG   A 1 491 ? 41.536  28.759  -3.903  1.00 51.91  ? 1028 ARG   A CA  1 
ATOM   3809 C C   . ARG   A 1 491 ? 40.385  29.170  -2.984  1.00 48.46  ? 1028 ARG   A C   1 
ATOM   3810 O O   . ARG   A 1 491 ? 40.084  30.362  -2.851  1.00 50.05  ? 1028 ARG   A O   1 
ATOM   3811 C CB  . ARG   A 1 491 ? 42.871  29.298  -3.388  1.00 54.67  ? 1028 ARG   A CB  1 
ATOM   3812 C CG  . ARG   A 1 491 ? 43.485  28.459  -2.277  1.00 55.34  ? 1028 ARG   A CG  1 
ATOM   3813 C CD  . ARG   A 1 491 ? 43.420  29.217  -0.961  1.00 57.76  ? 1028 ARG   A CD  1 
ATOM   3814 N NE  . ARG   A 1 491 ? 44.560  30.114  -0.795  1.00 61.34  ? 1028 ARG   A NE  1 
ATOM   3815 C CZ  . ARG   A 1 491 ? 44.527  31.278  -0.151  1.00 63.93  ? 1028 ARG   A CZ  1 
ATOM   3816 N NH1 . ARG   A 1 491 ? 43.388  31.708  0.372   1.00 64.04  ? 1028 ARG   A NH1 1 
ATOM   3817 N NH2 . ARG   A 1 491 ? 45.612  32.028  -0.072  1.00 66.19  ? 1028 ARG   A NH2 1 
ATOM   3818 N N   . PHE   A 1 492 ? 39.753  28.186  -2.350  1.00 44.04  ? 1029 PHE   A N   1 
ATOM   3819 C CA  . PHE   A 1 492 ? 38.650  28.380  -1.421  1.00 41.92  ? 1029 PHE   A CA  1 
ATOM   3820 C C   . PHE   A 1 492 ? 38.967  27.705  -0.094  1.00 41.17  ? 1029 PHE   A C   1 
ATOM   3821 O O   . PHE   A 1 492 ? 39.628  26.662  -0.067  1.00 39.40  ? 1029 PHE   A O   1 
ATOM   3822 C CB  . PHE   A 1 492 ? 37.334  27.803  -1.973  1.00 38.84  ? 1029 PHE   A CB  1 
ATOM   3823 C CG  . PHE   A 1 492 ? 36.743  28.592  -3.110  1.00 37.26  ? 1029 PHE   A CG  1 
ATOM   3824 C CD1 . PHE   A 1 492 ? 35.873  29.643  -2.864  1.00 36.82  ? 1029 PHE   A CD1 1 
ATOM   3825 C CD2 . PHE   A 1 492 ? 37.039  28.269  -4.425  1.00 36.11  ? 1029 PHE   A CD2 1 
ATOM   3826 C CE1 . PHE   A 1 492 ? 35.322  30.363  -3.905  1.00 36.59  ? 1029 PHE   A CE1 1 
ATOM   3827 C CE2 . PHE   A 1 492 ? 36.492  28.985  -5.469  1.00 36.21  ? 1029 PHE   A CE2 1 
ATOM   3828 C CZ  . PHE   A 1 492 ? 35.629  30.033  -5.208  1.00 36.57  ? 1029 PHE   A CZ  1 
ATOM   3829 N N   . PRO   A 1 493 ? 38.500  28.267  1.020   1.00 42.24  ? 1030 PRO   A N   1 
ATOM   3830 C CA  . PRO   A 1 493 ? 38.807  27.671  2.326   1.00 42.48  ? 1030 PRO   A CA  1 
ATOM   3831 C C   . PRO   A 1 493 ? 38.198  26.283  2.494   1.00 41.25  ? 1030 PRO   A C   1 
ATOM   3832 O O   . PRO   A 1 493 ? 37.120  25.977  1.978   1.00 38.02  ? 1030 PRO   A O   1 
ATOM   3833 C CB  . PRO   A 1 493 ? 38.210  28.672  3.323   1.00 42.72  ? 1030 PRO   A CB  1 
ATOM   3834 C CG  . PRO   A 1 493 ? 37.207  29.446  2.541   1.00 42.58  ? 1030 PRO   A CG  1 
ATOM   3835 C CD  . PRO   A 1 493 ? 37.758  29.532  1.155   1.00 43.03  ? 1030 PRO   A CD  1 
ATOM   3836 N N   . ARG   A 1 494 ? 38.916  25.440  3.233   1.00 43.56  ? 1031 ARG   A N   1 
ATOM   3837 C CA  . ARG   A 1 494 ? 38.457  24.086  3.514   1.00 44.18  ? 1031 ARG   A CA  1 
ATOM   3838 C C   . ARG   A 1 494 ? 37.240  24.119  4.438   1.00 47.12  ? 1031 ARG   A C   1 
ATOM   3839 O O   . ARG   A 1 494 ? 37.177  24.909  5.384   1.00 47.49  ? 1031 ARG   A O   1 
ATOM   3840 C CB  . ARG   A 1 494 ? 39.595  23.279  4.145   1.00 42.93  ? 1031 ARG   A CB  1 
ATOM   3841 C CG  . ARG   A 1 494 ? 39.365  21.776  4.236   1.00 41.20  ? 1031 ARG   A CG  1 
ATOM   3842 C CD  . ARG   A 1 494 ? 39.854  21.029  2.992   1.00 39.94  ? 1031 ARG   A CD  1 
ATOM   3843 N NE  . ARG   A 1 494 ? 41.282  21.219  2.705   1.00 40.11  ? 1031 ARG   A NE  1 
ATOM   3844 C CZ  . ARG   A 1 494 ? 42.265  20.464  3.198   1.00 39.10  ? 1031 ARG   A CZ  1 
ATOM   3845 N NH1 . ARG   A 1 494 ? 41.992  19.467  4.025   1.00 39.29  ? 1031 ARG   A NH1 1 
ATOM   3846 N NH2 . ARG   A 1 494 ? 43.526  20.708  2.870   1.00 38.57  ? 1031 ARG   A NH2 1 
ATOM   3847 N N   . LYS   A 1 495 ? 36.261  23.257  4.157   1.00 49.35  ? 1032 LYS   A N   1 
ATOM   3848 C CA  . LYS   A 1 495 ? 35.010  23.273  4.907   1.00 52.20  ? 1032 LYS   A CA  1 
ATOM   3849 C C   . LYS   A 1 495 ? 35.072  22.471  6.199   1.00 53.67  ? 1032 LYS   A C   1 
ATOM   3850 O O   . LYS   A 1 495 ? 34.375  22.812  7.162   1.00 55.07  ? 1032 LYS   A O   1 
ATOM   3851 C CB  . LYS   A 1 495 ? 33.864  22.749  4.037   1.00 52.90  ? 1032 LYS   A CB  1 
ATOM   3852 C CG  . LYS   A 1 495 ? 32.497  22.848  4.692   1.00 56.08  ? 1032 LYS   A CG  1 
ATOM   3853 C CD  . LYS   A 1 495 ? 31.388  22.417  3.749   1.00 57.83  ? 1032 LYS   A CD  1 
ATOM   3854 C CE  . LYS   A 1 495 ? 30.048  22.356  4.467   1.00 60.10  ? 1032 LYS   A CE  1 
ATOM   3855 N NZ  . LYS   A 1 495 ? 28.955  21.934  3.546   1.00 60.33  ? 1032 LYS   A NZ  1 
ATOM   3856 N N   . SER   A 1 496 ? 35.887  21.421  6.257   1.00 53.82  ? 1033 SER   A N   1 
ATOM   3857 C CA  . SER   A 1 496 ? 35.982  20.587  7.447   1.00 54.82  ? 1033 SER   A CA  1 
ATOM   3858 C C   . SER   A 1 496 ? 37.428  20.505  7.916   1.00 55.85  ? 1033 SER   A C   1 
ATOM   3859 O O   . SER   A 1 496 ? 38.364  20.831  7.182   1.00 56.54  ? 1033 SER   A O   1 
ATOM   3860 C CB  . SER   A 1 496 ? 35.437  19.176  7.195   1.00 54.10  ? 1033 SER   A CB  1 
ATOM   3861 O OG  . SER   A 1 496 ? 36.134  18.541  6.135   1.00 54.14  ? 1033 SER   A OG  1 
ATOM   3862 N N   . THR   A 1 497 ? 37.597  20.061  9.159   1.00 56.28  ? 1034 THR   A N   1 
ATOM   3863 C CA  . THR   A 1 497 ? 38.918  19.879  9.738   1.00 56.96  ? 1034 THR   A CA  1 
ATOM   3864 C C   . THR   A 1 497 ? 39.373  18.426  9.755   1.00 54.94  ? 1034 THR   A C   1 
ATOM   3865 O O   . THR   A 1 497 ? 40.530  18.165  10.102  1.00 55.66  ? 1034 THR   A O   1 
ATOM   3866 C CB  . THR   A 1 497 ? 38.961  20.441  11.168  1.00 59.47  ? 1034 THR   A CB  1 
ATOM   3867 O OG1 . THR   A 1 497 ? 37.702  20.211  11.816  1.00 59.70  ? 1034 THR   A OG1 1 
ATOM   3868 C CG2 . THR   A 1 497 ? 39.258  21.932  11.149  1.00 60.76  ? 1034 THR   A CG2 1 
ATOM   3869 N N   . PHE   A 1 498 ? 38.509  17.479  9.392   1.00 51.83  ? 1035 PHE   A N   1 
ATOM   3870 C CA  . PHE   A 1 498 ? 38.951  16.096  9.418   1.00 50.16  ? 1035 PHE   A CA  1 
ATOM   3871 C C   . PHE   A 1 498 ? 39.676  15.742  8.124   1.00 46.74  ? 1035 PHE   A C   1 
ATOM   3872 O O   . PHE   A 1 498 ? 39.693  16.501  7.150   1.00 46.49  ? 1035 PHE   A O   1 
ATOM   3873 C CB  . PHE   A 1 498 ? 37.787  15.131  9.672   1.00 51.13  ? 1035 PHE   A CB  1 
ATOM   3874 C CG  . PHE   A 1 498 ? 36.520  15.461  8.928   1.00 52.06  ? 1035 PHE   A CG  1 
ATOM   3875 C CD1 . PHE   A 1 498 ? 36.431  15.289  7.554   1.00 52.23  ? 1035 PHE   A CD1 1 
ATOM   3876 C CD2 . PHE   A 1 498 ? 35.396  15.892  9.619   1.00 53.38  ? 1035 PHE   A CD2 1 
ATOM   3877 C CE1 . PHE   A 1 498 ? 35.251  15.577  6.878   1.00 52.45  ? 1035 PHE   A CE1 1 
ATOM   3878 C CE2 . PHE   A 1 498 ? 34.214  16.181  8.955   1.00 53.39  ? 1035 PHE   A CE2 1 
ATOM   3879 C CZ  . PHE   A 1 498 ? 34.140  16.022  7.581   1.00 53.15  ? 1035 PHE   A CZ  1 
ATOM   3880 N N   . SER   A 1 499 ? 40.297  14.568  8.138   1.00 43.14  ? 1036 SER   A N   1 
ATOM   3881 C CA  . SER   A 1 499 ? 41.113  14.126  7.022   1.00 37.79  ? 1036 SER   A CA  1 
ATOM   3882 C C   . SER   A 1 499 ? 40.252  13.842  5.797   1.00 36.71  ? 1036 SER   A C   1 
ATOM   3883 O O   . SER   A 1 499 ? 39.101  13.410  5.902   1.00 35.95  ? 1036 SER   A O   1 
ATOM   3884 C CB  . SER   A 1 499 ? 41.903  12.880  7.415   1.00 34.98  ? 1036 SER   A CB  1 
ATOM   3885 O OG  . SER   A 1 499 ? 42.287  12.136  6.276   1.00 32.79  ? 1036 SER   A OG  1 
ATOM   3886 N N   . LEU   A 1 500 ? 40.823  14.112  4.622   1.00 37.55  ? 1037 LEU   A N   1 
ATOM   3887 C CA  . LEU   A 1 500 ? 40.189  13.782  3.352   1.00 34.96  ? 1037 LEU   A CA  1 
ATOM   3888 C C   . LEU   A 1 500 ? 40.376  12.324  2.968   1.00 35.19  ? 1037 LEU   A C   1 
ATOM   3889 O O   . LEU   A 1 500 ? 39.699  11.852  2.047   1.00 34.08  ? 1037 LEU   A O   1 
ATOM   3890 C CB  . LEU   A 1 500 ? 40.741  14.671  2.231   1.00 33.53  ? 1037 LEU   A CB  1 
ATOM   3891 C CG  . LEU   A 1 500 ? 40.616  16.189  2.370   1.00 33.83  ? 1037 LEU   A CG  1 
ATOM   3892 C CD1 . LEU   A 1 500 ? 41.144  16.860  1.117   1.00 33.27  ? 1037 LEU   A CD1 1 
ATOM   3893 C CD2 . LEU   A 1 500 ? 39.177  16.607  2.632   1.00 33.94  ? 1037 LEU   A CD2 1 
ATOM   3894 N N   . LYS   A 1 501 ? 41.268  11.606  3.648   1.00 37.04  ? 1038 LYS   A N   1 
ATOM   3895 C CA  . LYS   A 1 501 ? 41.536  10.217  3.298   1.00 38.23  ? 1038 LYS   A CA  1 
ATOM   3896 C C   . LYS   A 1 501 ? 40.298  9.353   3.506   1.00 36.10  ? 1038 LYS   A C   1 
ATOM   3897 O O   . LYS   A 1 501 ? 39.688  9.356   4.581   1.00 37.01  ? 1038 LYS   A O   1 
ATOM   3898 C CB  . LYS   A 1 501 ? 42.706  9.677   4.120   1.00 41.59  ? 1038 LYS   A CB  1 
ATOM   3899 C CG  . LYS   A 1 501 ? 44.045  9.829   3.420   1.00 46.02  ? 1038 LYS   A CG  1 
ATOM   3900 C CD  . LYS   A 1 501 ? 45.221  9.558   4.354   1.00 50.83  ? 1038 LYS   A CD  1 
ATOM   3901 C CE  . LYS   A 1 501 ? 45.208  8.128   4.887   1.00 53.54  ? 1038 LYS   A CE  1 
ATOM   3902 N NZ  . LYS   A 1 501 ? 45.350  7.105   3.804   1.00 54.14  ? 1038 LYS   A NZ  1 
ATOM   3903 N N   . SER   A 1 502 ? 39.920  8.627   2.460   1.00 32.86  ? 1039 SER   A N   1 
ATOM   3904 C CA  . SER   A 1 502 ? 38.857  7.653   2.580   1.00 31.86  ? 1039 SER   A CA  1 
ATOM   3905 C C   . SER   A 1 502 ? 39.318  6.488   3.450   1.00 33.50  ? 1039 SER   A C   1 
ATOM   3906 O O   . SER   A 1 502 ? 40.511  6.176   3.494   1.00 35.13  ? 1039 SER   A O   1 
ATOM   3907 C CB  . SER   A 1 502 ? 38.450  7.134   1.205   1.00 30.75  ? 1039 SER   A CB  1 
ATOM   3908 O OG  . SER   A 1 502 ? 37.456  6.134   1.316   1.00 31.75  ? 1039 SER   A OG  1 
ATOM   3909 N N   . PRO   A 1 503 ? 38.396  5.835   4.166   1.00 29.08  ? 1040 PRO   A N   1 
ATOM   3910 C CA  . PRO   A 1 503 ? 38.739  4.559   4.806   1.00 30.01  ? 1040 PRO   A CA  1 
ATOM   3911 C C   . PRO   A 1 503 ? 38.737  3.388   3.840   1.00 32.90  ? 1040 PRO   A C   1 
ATOM   3912 O O   . PRO   A 1 503 ? 39.139  2.285   4.231   1.00 33.85  ? 1040 PRO   A O   1 
ATOM   3913 C CB  . PRO   A 1 503 ? 37.651  4.402   5.876   1.00 30.35  ? 1040 PRO   A CB  1 
ATOM   3914 C CG  . PRO   A 1 503 ? 36.472  5.094   5.293   1.00 29.30  ? 1040 PRO   A CG  1 
ATOM   3915 C CD  . PRO   A 1 503 ? 37.018  6.254   4.482   1.00 34.57  ? 1040 PRO   A CD  1 
ATOM   3916 N N   . GLY   A 1 504 ? 38.301  3.592   2.598   1.00 28.91  ? 1041 GLY   A N   1 
ATOM   3917 C CA  . GLY   A 1 504 ? 38.347  2.562   1.584   1.00 30.70  ? 1041 GLY   A CA  1 
ATOM   3918 C C   . GLY   A 1 504 ? 37.129  1.656   1.605   1.00 31.06  ? 1041 GLY   A C   1 
ATOM   3919 O O   . GLY   A 1 504 ? 36.271  1.723   2.487   1.00 31.68  ? 1041 GLY   A O   1 
ATOM   3920 N N   . ILE   A 1 505 ? 37.067  0.779   0.603   1.00 32.66  ? 1042 ILE   A N   1 
ATOM   3921 C CA  . ILE   A 1 505 ? 35.926  -0.111  0.429   1.00 35.99  ? 1042 ILE   A CA  1 
ATOM   3922 C C   . ILE   A 1 505 ? 36.236  -1.534  0.885   1.00 38.45  ? 1042 ILE   A C   1 
ATOM   3923 O O   . ILE   A 1 505 ? 35.500  -2.459  0.549   1.00 39.80  ? 1042 ILE   A O   1 
ATOM   3924 C CB  . ILE   A 1 505 ? 35.423  -0.095  -1.025  1.00 37.29  ? 1042 ILE   A CB  1 
ATOM   3925 C CG1 . ILE   A 1 505 ? 36.515  -0.591  -1.975  1.00 38.25  ? 1042 ILE   A CG1 1 
ATOM   3926 C CG2 . ILE   A 1 505 ? 34.975  1.307   -1.420  1.00 36.14  ? 1042 ILE   A CG2 1 
ATOM   3927 C CD1 . ILE   A 1 505 ? 36.092  -0.596  -3.432  1.00 37.95  ? 1042 ILE   A CD1 1 
ATOM   3928 N N   . ARG   A 1 506 ? 37.306  -1.727  1.648   1.00 40.61  ? 1043 ARG   A N   1 
ATOM   3929 C CA  . ARG   A 1 506 ? 37.635  -3.042  2.179   1.00 42.27  ? 1043 ARG   A CA  1 
ATOM   3930 C C   . ARG   A 1 506 ? 37.004  -3.202  3.557   1.00 43.97  ? 1043 ARG   A C   1 
ATOM   3931 O O   . ARG   A 1 506 ? 37.308  -2.409  4.457   1.00 43.92  ? 1043 ARG   A O   1 
ATOM   3932 C CB  . ARG   A 1 506 ? 39.143  -3.216  2.269   1.00 43.11  ? 1043 ARG   A CB  1 
ATOM   3933 C CG  . ARG   A 1 506 ? 39.685  -4.441  1.541   1.00 45.30  ? 1043 ARG   A CG  1 
ATOM   3934 C CD  . ARG   A 1 506 ? 40.364  -4.083  0.217   1.00 45.33  ? 1043 ARG   A CD  1 
ATOM   3935 N NE  . ARG   A 1 506 ? 41.611  -3.341  0.408   1.00 45.92  ? 1043 ARG   A NE  1 
ATOM   3936 C CZ  . ARG   A 1 506 ? 41.824  -2.102  -0.026  1.00 45.50  ? 1043 ARG   A CZ  1 
ATOM   3937 N NH1 . ARG   A 1 506 ? 40.879  -1.453  -0.693  1.00 44.51  ? 1043 ARG   A NH1 1 
ATOM   3938 N NH2 . ARG   A 1 506 ? 42.989  -1.513  0.199   1.00 46.12  ? 1043 ARG   A NH2 1 
ATOM   3939 N N   . PRO   A 1 507 ? 36.128  -4.181  3.767   1.00 46.47  ? 1044 PRO   A N   1 
ATOM   3940 C CA  . PRO   A 1 507 ? 35.548  -4.371  5.100   1.00 49.19  ? 1044 PRO   A CA  1 
ATOM   3941 C C   . PRO   A 1 507 ? 36.612  -4.776  6.109   1.00 52.81  ? 1044 PRO   A C   1 
ATOM   3942 O O   . PRO   A 1 507 ? 37.699  -5.239  5.760   1.00 53.01  ? 1044 PRO   A O   1 
ATOM   3943 C CB  . PRO   A 1 507 ? 34.523  -5.496  4.894   1.00 48.88  ? 1044 PRO   A CB  1 
ATOM   3944 C CG  . PRO   A 1 507 ? 34.306  -5.573  3.419   1.00 47.67  ? 1044 PRO   A CG  1 
ATOM   3945 C CD  . PRO   A 1 507 ? 35.607  -5.156  2.797   1.00 47.19  ? 1044 PRO   A CD  1 
ATOM   3946 N N   . ASN   A 1 508 ? 36.285  -4.586  7.384   1.00 56.76  ? 1045 ASN   A N   1 
ATOM   3947 C CA  . ASN   A 1 508 ? 37.204  -4.961  8.457   1.00 61.88  ? 1045 ASN   A CA  1 
ATOM   3948 C C   . ASN   A 1 508 ? 36.641  -6.113  9.284   1.00 64.18  ? 1045 ASN   A C   1 
ATOM   3949 O O   . ASN   A 1 508 ? 36.492  -7.230  8.790   1.00 65.47  ? 1045 ASN   A O   1 
ATOM   3950 C CB  . ASN   A 1 508 ? 37.506  -3.762  9.361   1.00 64.10  ? 1045 ASN   A CB  1 
ATOM   3951 C CG  . ASN   A 1 508 ? 36.461  -3.568  10.443  1.00 67.17  ? 1045 ASN   A CG  1 
ATOM   3952 O OD1 . ASN   A 1 508 ? 35.257  -3.606  10.180  1.00 68.36  ? 1045 ASN   A OD1 1 
ATOM   3953 N ND2 . ASN   A 1 508 ? 36.919  -3.365  11.674  1.00 68.58  ? 1045 ASN   A ND2 1 
HETATM 3954 N N1  . A1ASY B 2 .   ? 35.841  16.888  -19.757 1.00 33.25  ? 1101 A1ASY A N1  1 
HETATM 3955 N N3  . A1ASY B 2 .   ? 36.322  12.786  -17.763 1.00 27.15  ? 1101 A1ASY A N3  1 
HETATM 3956 C C4  . A1ASY B 2 .   ? 36.855  15.900  -19.387 1.00 32.43  ? 1101 A1ASY A C4  1 
HETATM 3957 C C5  . A1ASY B 2 .   ? 36.682  15.452  -17.952 1.00 31.21  ? 1101 A1ASY A C5  1 
HETATM 3958 C C6  . A1ASY B 2 .   ? 34.323  15.848  -18.124 1.00 30.94  ? 1101 A1ASY A C6  1 
HETATM 3959 C C7  . A1ASY B 2 .   ? 34.505  16.330  -19.546 1.00 31.54  ? 1101 A1ASY A C7  1 
HETATM 3960 C C8  . A1ASY B 2 .   ? 35.201  13.503  -17.589 1.00 28.35  ? 1101 A1ASY A C8  1 
HETATM 3961 C C10 . A1ASY B 2 .   ? 38.767  11.255  -17.858 1.00 28.66  ? 1101 A1ASY A C10 1 
HETATM 3962 C C13 . A1ASY B 2 .   ? 41.318  12.242  -17.966 1.00 28.97  ? 1101 A1ASY A C13 1 
HETATM 3963 C C15 . A1ASY B 2 .   ? 42.034  11.013  -19.757 1.00 29.55  ? 1101 A1ASY A C15 1 
HETATM 3964 C C17 . A1ASY B 2 .   ? 39.596  10.775  -18.843 1.00 29.16  ? 1101 A1ASY A C17 1 
HETATM 3965 C C20 . A1ASY B 2 .   ? 31.527  11.360  -16.863 1.00 26.57  ? 1101 A1ASY A C20 1 
HETATM 3966 C C21 . A1ASY B 2 .   ? 31.678  12.696  -16.206 1.00 26.42  ? 1101 A1ASY A C21 1 
HETATM 3967 C C22 . A1ASY B 2 .   ? 32.671  13.531  -16.984 1.00 26.74  ? 1101 A1ASY A C22 1 
HETATM 3968 C C1  . A1ASY B 2 .   ? 35.468  16.293  -22.136 1.00 34.53  ? 1101 A1ASY A C1  1 
HETATM 3969 C C11 . A1ASY B 2 .   ? 39.187  12.227  -16.945 1.00 29.60  ? 1101 A1ASY A C11 1 
HETATM 3970 C C12 . A1ASY B 2 .   ? 40.462  12.724  -16.981 1.00 29.60  ? 1101 A1ASY A C12 1 
HETATM 3971 C C14 . A1ASY B 2 .   ? 43.044  11.811  -19.318 1.00 29.12  ? 1101 A1ASY A C14 1 
HETATM 3972 C C16 . A1ASY B 2 .   ? 40.906  11.269  -18.904 1.00 29.53  ? 1101 A1ASY A C16 1 
HETATM 3973 C C18 . A1ASY B 2 .   ? 34.041  11.441  -17.080 1.00 26.76  ? 1101 A1ASY A C18 1 
HETATM 3974 C C19 . A1ASY B 2 .   ? 32.841  10.617  -16.696 1.00 26.90  ? 1101 A1ASY A C19 1 
HETATM 3975 C C2  . A1ASY B 2 .   ? 36.007  17.325  -21.163 1.00 35.09  ? 1101 A1ASY A C2  1 
HETATM 3976 C C23 . A1ASY B 2 .   ? 33.993  12.833  -17.216 1.00 26.99  ? 1101 A1ASY A C23 1 
HETATM 3977 C C3  . A1ASY B 2 .   ? 37.446  17.706  -21.470 1.00 34.98  ? 1101 A1ASY A C3  1 
HETATM 3978 C C9  . A1ASY B 2 .   ? 36.284  11.456  -17.604 1.00 26.77  ? 1101 A1ASY A C9  1 
HETATM 3979 N N2  . A1ASY B 2 .   ? 35.356  14.865  -17.804 1.00 30.52  ? 1101 A1ASY A N2  1 
HETATM 3980 N N4  . A1ASY B 2 .   ? 37.439  10.775  -17.797 1.00 27.12  ? 1101 A1ASY A N4  1 
HETATM 3981 N N5  . A1ASY B 2 .   ? 42.626  12.553  -18.245 1.00 28.76  ? 1101 A1ASY A N5  1 
HETATM 3982 N N6  . A1ASY B 2 .   ? 35.190  10.763  -17.264 1.00 26.76  ? 1101 A1ASY A N6  1 
HETATM 3983 O O   . HOH   C 3 .   ? -10.324 -0.596  -36.381 1.00 41.90  ? 1201 HOH   A O   1 
HETATM 3984 O O   . HOH   C 3 .   ? 31.899  8.303   3.580   1.00 24.74  ? 1202 HOH   A O   1 
HETATM 3985 O O   . HOH   C 3 .   ? 33.543  -3.690  -14.404 1.00 41.14  ? 1203 HOH   A O   1 
HETATM 3986 O O   . HOH   C 3 .   ? 39.268  27.218  -22.554 1.00 49.44  ? 1204 HOH   A O   1 
HETATM 3987 O O   . HOH   C 3 .   ? 36.691  4.216   -22.065 1.00 40.57  ? 1205 HOH   A O   1 
HETATM 3988 O O   . HOH   C 3 .   ? 24.867  26.830  -0.923  1.00 39.72  ? 1206 HOH   A O   1 
HETATM 3989 O O   . HOH   C 3 .   ? 34.386  22.752  0.909   1.00 49.97  ? 1207 HOH   A O   1 
HETATM 3990 O O   . HOH   C 3 .   ? 14.701  18.608  -2.335  1.00 28.36  ? 1208 HOH   A O   1 
HETATM 3991 O O   . HOH   C 3 .   ? -21.762 -33.702 -20.024 1.00 38.45  ? 1209 HOH   A O   1 
HETATM 3992 O O   . HOH   C 3 .   ? -0.618  6.159   -23.554 1.00 46.36  ? 1210 HOH   A O   1 
HETATM 3993 O O   . HOH   C 3 .   ? -35.957 -22.852 -17.215 1.00 44.65  ? 1211 HOH   A O   1 
HETATM 3994 O O   . HOH   C 3 .   ? -22.951 -28.576 -29.818 1.00 36.50  ? 1212 HOH   A O   1 
HETATM 3995 O O   . HOH   C 3 .   ? 20.962  13.034  19.118  1.00 37.04  ? 1213 HOH   A O   1 
HETATM 3996 O O   . HOH   C 3 .   ? -39.515 -31.499 -16.211 1.00 46.60  ? 1214 HOH   A O   1 
HETATM 3997 O O   . HOH   C 3 .   ? 18.355  13.106  5.354   1.00 33.84  ? 1215 HOH   A O   1 
HETATM 3998 O O   . HOH   C 3 .   ? -19.050 -17.685 -22.404 1.00 36.70  ? 1216 HOH   A O   1 
HETATM 3999 O O   . HOH   C 3 .   ? -15.389 -0.229  -19.968 1.00 47.43  ? 1217 HOH   A O   1 
HETATM 4000 O O   . HOH   C 3 .   ? -22.428 -17.558 -0.861  1.00 38.69  ? 1218 HOH   A O   1 
HETATM 4001 O O   . HOH   C 3 .   ? 13.890  -8.341  -3.329  1.00 32.29  ? 1219 HOH   A O   1 
HETATM 4002 O O   . HOH   C 3 .   ? 32.712  -4.797  -2.369  1.00 30.07  ? 1220 HOH   A O   1 
HETATM 4003 O O   . HOH   C 3 .   ? -23.950 -22.710 -11.544 1.00 41.93  ? 1221 HOH   A O   1 
HETATM 4004 O O   . HOH   C 3 .   ? 41.701  11.541  -14.064 1.00 37.48  ? 1222 HOH   A O   1 
HETATM 4005 O O   . HOH   C 3 .   ? 34.824  26.454  1.666   1.00 35.23  ? 1223 HOH   A O   1 
HETATM 4006 O O   . HOH   C 3 .   ? -0.755  -0.361  -6.293  1.00 38.57  ? 1224 HOH   A O   1 
HETATM 4007 O O   . HOH   C 3 .   ? -21.424 -16.335 -24.432 1.00 43.00  ? 1225 HOH   A O   1 
HETATM 4008 O O   . HOH   C 3 .   ? 0.679   -7.383  -8.349  1.00 29.26  ? 1226 HOH   A O   1 
HETATM 4009 O O   . HOH   C 3 .   ? -0.005  -9.531  -14.744 1.00 44.76  ? 1227 HOH   A O   1 
HETATM 4010 O O   . HOH   C 3 .   ? -10.852 -17.334 -25.659 1.00 30.39  ? 1228 HOH   A O   1 
HETATM 4011 O O   . HOH   C 3 .   ? 26.833  -4.900  12.310  1.00 34.80  ? 1229 HOH   A O   1 
HETATM 4012 O O   . HOH   C 3 .   ? -42.881 -26.844 -28.171 1.00 41.83  ? 1230 HOH   A O   1 
HETATM 4013 O O   . HOH   C 3 .   ? -30.956 -28.948 -13.538 1.00 38.91  ? 1231 HOH   A O   1 
HETATM 4014 O O   . HOH   C 3 .   ? 25.729  -6.881  10.777  1.00 34.29  ? 1232 HOH   A O   1 
HETATM 4015 O O   . HOH   C 3 .   ? -32.015 -5.504  -23.369 1.00 38.72  ? 1233 HOH   A O   1 
HETATM 4016 O O   . HOH   C 3 .   ? 43.385  33.490  -1.358  1.00 43.15  ? 1234 HOH   A O   1 
HETATM 4017 O O   . HOH   C 3 .   ? 7.092   -10.584 -19.438 1.00 32.47  ? 1235 HOH   A O   1 
HETATM 4018 O O   . HOH   C 3 .   ? -29.857 -22.214 -15.153 1.00 37.86  ? 1236 HOH   A O   1 
HETATM 4019 O O   . HOH   C 3 .   ? -5.045  6.026   -27.833 1.00 38.21  ? 1237 HOH   A O   1 
HETATM 4020 O O   . HOH   C 3 .   ? 43.192  18.872  -12.375 1.00 20.31  ? 1238 HOH   A O   1 
HETATM 4021 O O   . HOH   C 3 .   ? 8.057   2.399   1.042   1.00 35.08  ? 1239 HOH   A O   1 
HETATM 4022 O O   . HOH   C 3 .   ? 5.877   9.863   -3.296  1.00 35.74  ? 1240 HOH   A O   1 
HETATM 4023 O O   . HOH   C 3 .   ? 8.119   2.125   -3.943  1.00 8.78   ? 1241 HOH   A O   1 
HETATM 4024 O O   . HOH   C 3 .   ? -18.514 -6.860  4.474   1.00 34.12  ? 1242 HOH   A O   1 
HETATM 4025 O O   . HOH   C 3 .   ? 27.500  30.687  -6.818  1.00 34.03  ? 1243 HOH   A O   1 
HETATM 4026 O O   . HOH   C 3 .   ? -26.817 -8.439  -19.509 1.00 27.80  ? 1244 HOH   A O   1 
HETATM 4027 O O   . HOH   C 3 .   ? -6.675  2.764   -10.291 1.00 35.81  ? 1245 HOH   A O   1 
HETATM 4028 O O   . HOH   C 3 .   ? -11.074 -17.362 -17.902 1.00 34.83  ? 1246 HOH   A O   1 
HETATM 4029 O O   . HOH   C 3 .   ? -16.091 -15.706 -32.497 1.00 40.97  ? 1247 HOH   A O   1 
HETATM 4030 O O   . HOH   C 3 .   ? 22.599  18.620  -16.379 1.00 26.09  ? 1248 HOH   A O   1 
HETATM 4031 O O   . HOH   C 3 .   ? -8.995  2.322   -24.143 1.00 25.33  ? 1249 HOH   A O   1 
HETATM 4032 O O   . HOH   C 3 .   ? 23.601  16.531  -18.767 1.00 18.43  ? 1250 HOH   A O   1 
HETATM 4033 O O   . HOH   C 3 .   ? -14.617 3.381   -17.640 1.00 43.80  ? 1251 HOH   A O   1 
HETATM 4034 O O   . HOH   C 3 .   ? 23.074  5.042   14.610  1.00 49.09  ? 1252 HOH   A O   1 
HETATM 4035 O O   . HOH   C 3 .   ? 27.213  29.076  -1.308  1.00 33.45  ? 1253 HOH   A O   1 
HETATM 4036 O O   . HOH   C 3 .   ? 39.285  -0.132  3.216   1.00 39.03  ? 1254 HOH   A O   1 
HETATM 4037 O O   . HOH   C 3 .   ? 18.837  0.904   4.552   1.00 16.49  ? 1255 HOH   A O   1 
HETATM 4038 O O   . HOH   C 3 .   ? 4.956   -7.021  -8.330  1.00 38.63  ? 1256 HOH   A O   1 
HETATM 4039 O O   . HOH   C 3 .   ? -4.081  -18.760 -20.815 1.00 37.37  ? 1257 HOH   A O   1 
HETATM 4040 O O   . HOH   C 3 .   ? 16.786  -11.739 4.685   1.00 35.37  ? 1258 HOH   A O   1 
HETATM 4041 O O   . HOH   C 3 .   ? 15.060  4.245   -7.260  1.00 24.06  ? 1259 HOH   A O   1 
HETATM 4042 O O   . HOH   C 3 .   ? 33.032  -0.707  -21.113 1.00 21.16  ? 1260 HOH   A O   1 
HETATM 4043 O O   . HOH   C 3 .   ? 16.700  -2.979  -16.087 1.00 33.92  ? 1261 HOH   A O   1 
HETATM 4044 O O   . HOH   C 3 .   ? -12.098 5.178   -2.742  1.00 52.55  ? 1262 HOH   A O   1 
HETATM 4045 O O   . HOH   C 3 .   ? 28.395  1.281   -25.764 1.00 31.34  ? 1263 HOH   A O   1 
HETATM 4046 O O   . HOH   C 3 .   ? 36.031  23.555  -15.275 1.00 25.88  ? 1264 HOH   A O   1 
HETATM 4047 O O   . HOH   C 3 .   ? -2.748  -10.460 -12.791 1.00 22.05  ? 1265 HOH   A O   1 
HETATM 4048 O O   . HOH   C 3 .   ? 28.371  32.124  -10.378 1.00 44.72  ? 1266 HOH   A O   1 
HETATM 4049 O O   . HOH   C 3 .   ? -28.585 -28.746 -27.186 1.00 42.38  ? 1267 HOH   A O   1 
HETATM 4050 O O   . HOH   C 3 .   ? -4.491  -1.590  -14.539 1.00 26.86  ? 1268 HOH   A O   1 
HETATM 4051 O O   . HOH   C 3 .   ? 31.520  -5.957  -8.869  1.00 24.04  ? 1269 HOH   A O   1 
HETATM 4052 O O   . HOH   C 3 .   ? -3.299  1.004   -14.098 1.00 22.45  ? 1270 HOH   A O   1 
HETATM 4053 O O   . HOH   C 3 .   ? 18.620  25.171  -1.809  1.00 19.67  ? 1271 HOH   A O   1 
HETATM 4054 O O   . HOH   C 3 .   ? 28.513  -4.956  -20.097 1.00 37.99  ? 1272 HOH   A O   1 
HETATM 4055 O O   . HOH   C 3 .   ? -10.919 -16.948 -23.136 1.00 18.91  ? 1273 HOH   A O   1 
HETATM 4056 O O   . HOH   C 3 .   ? 33.010  0.391   -13.154 1.00 30.17  ? 1274 HOH   A O   1 
HETATM 4057 O O   . HOH   C 3 .   ? -9.234  9.585   -7.354  1.00 40.80  ? 1275 HOH   A O   1 
HETATM 4058 O O   . HOH   C 3 .   ? -40.088 -29.602 -19.467 1.00 50.50  ? 1276 HOH   A O   1 
HETATM 4059 O O   . HOH   C 3 .   ? -6.054  1.296   -33.773 1.00 41.32  ? 1277 HOH   A O   1 
HETATM 4060 O O   . HOH   C 3 .   ? 24.359  -9.600  -5.239  1.00 36.06  ? 1278 HOH   A O   1 
HETATM 4061 O O   . HOH   C 3 .   ? 10.806  28.190  -10.529 1.00 34.92  ? 1279 HOH   A O   1 
HETATM 4062 O O   . HOH   C 3 .   ? -34.910 -15.707 -20.769 1.00 35.86  ? 1280 HOH   A O   1 
HETATM 4063 O O   . HOH   C 3 .   ? -1.958  -10.680 8.008   1.00 44.98  ? 1281 HOH   A O   1 
HETATM 4064 O O   . HOH   C 3 .   ? 11.944  -3.789  -21.584 1.00 40.54  ? 1282 HOH   A O   1 
HETATM 4065 O O   . HOH   C 3 .   ? 11.471  2.239   5.337   1.00 27.00  ? 1283 HOH   A O   1 
HETATM 4066 O O   . HOH   C 3 .   ? -2.650  0.649   -9.709  1.00 10.25  ? 1284 HOH   A O   1 
HETATM 4067 O O   . HOH   C 3 .   ? -16.778 -13.848 -27.344 1.00 29.14  ? 1285 HOH   A O   1 
HETATM 4068 O O   . HOH   C 3 .   ? -14.047 -18.869 4.702   1.00 33.09  ? 1286 HOH   A O   1 
HETATM 4069 O O   . HOH   C 3 .   ? 31.841  -5.523  7.086   1.00 23.31  ? 1287 HOH   A O   1 
HETATM 4070 O O   . HOH   C 3 .   ? 4.154   7.709   -3.063  1.00 30.10  ? 1288 HOH   A O   1 
HETATM 4071 O O   . HOH   C 3 .   ? 10.725  8.311   -2.185  1.00 19.30  ? 1289 HOH   A O   1 
HETATM 4072 O O   . HOH   C 3 .   ? -7.017  -18.260 -13.976 1.00 26.77  ? 1290 HOH   A O   1 
HETATM 4073 O O   . HOH   C 3 .   ? -30.058 -32.022 -25.914 1.00 26.14  ? 1291 HOH   A O   1 
HETATM 4074 O O   . HOH   C 3 .   ? 26.704  -4.893  -31.850 1.00 44.18  ? 1292 HOH   A O   1 
HETATM 4075 O O   . HOH   C 3 .   ? 39.288  0.884   -1.121  1.00 30.89  ? 1293 HOH   A O   1 
HETATM 4076 O O   . HOH   C 3 .   ? 11.267  4.654   1.813   1.00 33.17  ? 1294 HOH   A O   1 
HETATM 4077 O O   . HOH   C 3 .   ? -7.934  -32.147 -39.585 1.00 36.75  ? 1295 HOH   A O   1 
HETATM 4078 O O   . HOH   C 3 .   ? -15.280 4.644   -2.334  1.00 30.57  ? 1296 HOH   A O   1 
HETATM 4079 O O   . HOH   C 3 .   ? 29.431  11.359  -20.259 1.00 34.62  ? 1297 HOH   A O   1 
HETATM 4080 O O   . HOH   C 3 .   ? -14.807 -11.864 3.147   1.00 35.91  ? 1298 HOH   A O   1 
HETATM 4081 O O   . HOH   C 3 .   ? 14.636  8.104   -0.247  1.00 27.11  ? 1299 HOH   A O   1 
HETATM 4082 O O   . HOH   C 3 .   ? 23.475  -9.936  -0.317  1.00 24.64  ? 1300 HOH   A O   1 
HETATM 4083 O O   . HOH   C 3 .   ? 30.626  25.366  -19.143 1.00 27.38  ? 1301 HOH   A O   1 
HETATM 4084 O O   . HOH   C 3 .   ? -28.612 -26.558 -25.103 1.00 26.56  ? 1302 HOH   A O   1 
HETATM 4085 O O   . HOH   C 3 .   ? -7.070  1.137   -8.257  1.00 39.05  ? 1303 HOH   A O   1 
HETATM 4086 O O   . HOH   C 3 .   ? 41.599  8.704   0.109   1.00 23.98  ? 1304 HOH   A O   1 
HETATM 4087 O O   . HOH   C 3 .   ? -32.563 -33.070 -29.817 1.00 38.17  ? 1305 HOH   A O   1 
HETATM 4088 O O   . HOH   C 3 .   ? 19.017  29.961  -8.127  1.00 29.22  ? 1306 HOH   A O   1 
HETATM 4089 O O   . HOH   C 3 .   ? -4.309  -16.721 -14.023 1.00 40.03  ? 1307 HOH   A O   1 
HETATM 4090 O O   . HOH   C 3 .   ? 43.075  18.863  11.312  1.00 20.01  ? 1308 HOH   A O   1 
HETATM 4091 O O   . HOH   C 3 .   ? 28.672  -2.685  13.439  1.00 38.06  ? 1309 HOH   A O   1 
HETATM 4092 O O   . HOH   C 3 .   ? -24.684 -31.999 -21.134 1.00 22.96  ? 1310 HOH   A O   1 
HETATM 4093 O O   . HOH   C 3 .   ? 39.411  6.009   -18.250 1.00 29.42  ? 1311 HOH   A O   1 
HETATM 4094 O O   . HOH   C 3 .   ? 17.203  9.373   13.381  1.00 31.04  ? 1312 HOH   A O   1 
HETATM 4095 O O   . HOH   C 3 .   ? 6.793   -8.532  -6.097  1.00 36.73  ? 1313 HOH   A O   1 
HETATM 4096 O O   . HOH   C 3 .   ? 40.551  25.490  -3.468  1.00 18.64  ? 1314 HOH   A O   1 
HETATM 4097 O O   . HOH   C 3 .   ? -27.473 -10.271 -15.804 1.00 26.78  ? 1315 HOH   A O   1 
HETATM 4098 O O   . HOH   C 3 .   ? 26.679  30.999  -2.976  1.00 40.85  ? 1316 HOH   A O   1 
HETATM 4099 O O   . HOH   C 3 .   ? -14.222 -11.774 -34.818 1.00 52.79  ? 1317 HOH   A O   1 
HETATM 4100 O O   . HOH   C 3 .   ? 24.628  -3.682  6.111   1.00 15.22  ? 1318 HOH   A O   1 
HETATM 4101 O O   . HOH   C 3 .   ? -32.321 -21.930 -12.285 1.00 30.50  ? 1319 HOH   A O   1 
HETATM 4102 O O   . HOH   C 3 .   ? 14.734  -7.047  -17.890 1.00 38.69  ? 1320 HOH   A O   1 
HETATM 4103 O O   . HOH   C 3 .   ? 16.637  26.750  0.071   1.00 23.93  ? 1321 HOH   A O   1 
HETATM 4104 O O   . HOH   C 3 .   ? 34.550  28.905  0.633   1.00 22.99  ? 1322 HOH   A O   1 
HETATM 4105 O O   . HOH   C 3 .   ? -23.163 -24.677 -29.681 1.00 39.06  ? 1323 HOH   A O   1 
HETATM 4106 O O   . HOH   C 3 .   ? 43.014  22.443  0.493   1.00 33.27  ? 1324 HOH   A O   1 
HETATM 4107 O O   . HOH   C 3 .   ? -1.459  0.212   -21.797 1.00 11.71  ? 1325 HOH   A O   1 
HETATM 4108 O O   . HOH   C 3 .   ? 27.004  20.011  0.236   1.00 33.07  ? 1326 HOH   A O   1 
HETATM 4109 O O   . HOH   C 3 .   ? -0.247  -4.939  -10.467 1.00 42.11  ? 1327 HOH   A O   1 
HETATM 4110 O O   . HOH   C 3 .   ? 13.372  -5.727  -5.156  1.00 37.62  ? 1328 HOH   A O   1 
HETATM 4111 O O   . HOH   C 3 .   ? -5.867  -17.288 -10.474 1.00 26.99  ? 1329 HOH   A O   1 
HETATM 4112 O O   . HOH   C 3 .   ? 17.493  -6.196  5.465   1.00 35.31  ? 1330 HOH   A O   1 
HETATM 4113 O O   . HOH   C 3 .   ? 44.126  20.360  -14.083 1.00 32.43  ? 1331 HOH   A O   1 
HETATM 4114 O O   . HOH   C 3 .   ? -35.296 -23.466 -20.714 1.00 35.05  ? 1332 HOH   A O   1 
HETATM 4115 O O   . HOH   C 3 .   ? -12.031 5.655   -0.634  1.00 50.95  ? 1333 HOH   A O   1 
HETATM 4116 O O   . HOH   C 3 .   ? -2.837  -8.222  -3.489  1.00 25.48  ? 1334 HOH   A O   1 
HETATM 4117 O O   . HOH   C 3 .   ? -23.093 -6.513  -4.396  1.00 26.00  ? 1335 HOH   A O   1 
HETATM 4118 O O   . HOH   C 3 .   ? 29.552  33.887  -4.511  1.00 25.07  ? 1336 HOH   A O   1 
HETATM 4119 O O   . HOH   C 3 .   ? -26.954 -4.548  -19.166 1.00 26.90  ? 1337 HOH   A O   1 
HETATM 4120 O O   . HOH   C 3 .   ? -1.904  1.308   -3.109  1.00 41.80  ? 1338 HOH   A O   1 
HETATM 4121 O O   . HOH   C 3 .   ? 1.231   -3.130  -3.563  1.00 51.71  ? 1339 HOH   A O   1 
HETATM 4122 O O   . HOH   C 3 .   ? 26.291  -11.828 -9.830  1.00 31.72  ? 1340 HOH   A O   1 
HETATM 4123 O O   . HOH   C 3 .   ? -22.388 -7.282  -35.273 1.00 45.46  ? 1341 HOH   A O   1 
HETATM 4124 O O   . HOH   C 3 .   ? 22.813  23.246  -13.884 1.00 32.90  ? 1342 HOH   A O   1 
HETATM 4125 O O   . HOH   C 3 .   ? 18.148  21.393  2.619   1.00 36.08  ? 1343 HOH   A O   1 
HETATM 4126 O O   . HOH   C 3 .   ? -18.330 -16.458 -28.483 1.00 40.89  ? 1344 HOH   A O   1 
HETATM 4127 O O   . HOH   C 3 .   ? 16.605  -6.906  0.950   1.00 28.89  ? 1345 HOH   A O   1 
HETATM 4128 O O   . HOH   C 3 .   ? -9.950  0.989   -6.389  1.00 29.82  ? 1346 HOH   A O   1 
HETATM 4129 O O   . HOH   C 3 .   ? 29.016  -5.329  1.413   1.00 18.57  ? 1347 HOH   A O   1 
HETATM 4130 O O   . HOH   C 3 .   ? 37.155  5.062   9.951   1.00 27.17  ? 1348 HOH   A O   1 
HETATM 4131 O O   . HOH   C 3 .   ? -26.590 -12.163 -32.242 1.00 41.67  ? 1349 HOH   A O   1 
HETATM 4132 O O   . HOH   C 3 .   ? -22.386 -3.892  -15.338 1.00 34.63  ? 1350 HOH   A O   1 
HETATM 4133 O O   . HOH   C 3 .   ? -24.456 -33.644 -30.766 1.00 31.35  ? 1351 HOH   A O   1 
HETATM 4134 O O   . HOH   C 3 .   ? -24.247 -4.828  -9.412  1.00 29.42  ? 1352 HOH   A O   1 
HETATM 4135 O O   . HOH   C 3 .   ? -23.072 -9.542  -34.239 1.00 26.66  ? 1353 HOH   A O   1 
HETATM 4136 O O   . HOH   C 3 .   ? 14.696  3.397   9.424   1.00 37.36  ? 1354 HOH   A O   1 
HETATM 4137 O O   . HOH   C 3 .   ? 10.519  19.615  -11.139 1.00 31.00  ? 1355 HOH   A O   1 
HETATM 4138 O O   . HOH   C 3 .   ? -3.357  4.351   -3.039  1.00 43.02  ? 1356 HOH   A O   1 
HETATM 4139 O O   . HOH   C 3 .   ? -5.708  -18.353 1.146   1.00 33.89  ? 1357 HOH   A O   1 
HETATM 4140 O O   . HOH   C 3 .   ? 28.191  4.594   8.071   1.00 19.53  ? 1358 HOH   A O   1 
HETATM 4141 O O   . HOH   C 3 .   ? 37.578  9.839   -0.872  1.00 24.33  ? 1359 HOH   A O   1 
HETATM 4142 O O   . HOH   C 3 .   ? 40.273  12.996  10.762  1.00 27.41  ? 1360 HOH   A O   1 
HETATM 4143 O O   . HOH   C 3 .   ? 22.913  31.359  -7.849  1.00 45.62  ? 1361 HOH   A O   1 
HETATM 4144 O O   . HOH   C 3 .   ? 30.324  -0.880  -19.480 1.00 46.41  ? 1362 HOH   A O   1 
HETATM 4145 O O   . HOH   C 3 .   ? -9.115  4.317   -17.913 1.00 33.99  ? 1363 HOH   A O   1 
HETATM 4146 O O   . HOH   C 3 .   ? 11.765  32.345  -9.492  1.00 45.35  ? 1364 HOH   A O   1 
HETATM 4147 O O   . HOH   C 3 .   ? 34.321  23.301  -18.825 1.00 27.91  ? 1365 HOH   A O   1 
HETATM 4148 O O   . HOH   C 3 .   ? -17.186 -30.909 -38.290 1.00 37.82  ? 1366 HOH   A O   1 
HETATM 4149 O O   . HOH   C 3 .   ? 19.019  17.448  2.964   1.00 19.36  ? 1367 HOH   A O   1 
HETATM 4150 O O   . HOH   C 3 .   ? 2.961   -8.355  -15.043 1.00 36.64  ? 1368 HOH   A O   1 
HETATM 4151 O O   . HOH   C 3 .   ? 20.479  -14.405 4.122   1.00 19.60  ? 1369 HOH   A O   1 
HETATM 4152 O O   . HOH   C 3 .   ? 36.396  11.779  5.237   1.00 23.89  ? 1370 HOH   A O   1 
HETATM 4153 O O   . HOH   C 3 .   ? 17.805  32.477  -14.255 1.00 42.70  ? 1371 HOH   A O   1 
HETATM 4154 O O   . HOH   C 3 .   ? -34.473 -17.992 -15.558 1.00 31.98  ? 1372 HOH   A O   1 
HETATM 4155 O O   . HOH   C 3 .   ? -12.205 -24.687 -0.269  1.00 36.32  ? 1373 HOH   A O   1 
HETATM 4156 O O   . HOH   C 3 .   ? 7.053   -10.051 -7.812  1.00 38.93  ? 1374 HOH   A O   1 
HETATM 4157 O O   . HOH   C 3 .   ? 32.614  -1.981  12.717  1.00 41.27  ? 1375 HOH   A O   1 
HETATM 4158 O O   . HOH   C 3 .   ? 17.745  -5.914  8.748   1.00 21.42  ? 1376 HOH   A O   1 
HETATM 4159 O O   . HOH   C 3 .   ? 45.938  14.909  -7.894  1.00 24.33  ? 1377 HOH   A O   1 
HETATM 4160 O O   . HOH   C 3 .   ? 45.717  4.714   -9.983  1.00 32.74  ? 1378 HOH   A O   1 
HETATM 4161 O O   . HOH   C 3 .   ? -23.226 -9.800  3.087   1.00 38.03  ? 1379 HOH   A O   1 
HETATM 4162 O O   . HOH   C 3 .   ? 39.022  8.306   -2.424  1.00 25.01  ? 1380 HOH   A O   1 
HETATM 4163 O O   . HOH   C 3 .   ? 42.149  15.166  -2.608  1.00 40.15  ? 1381 HOH   A O   1 
HETATM 4164 O O   . HOH   C 3 .   ? -28.835 -8.810  -17.675 1.00 22.35  ? 1382 HOH   A O   1 
HETATM 4165 O O   . HOH   C 3 .   ? 37.470  1.969   -18.302 1.00 37.26  ? 1383 HOH   A O   1 
HETATM 4166 O O   . HOH   C 3 .   ? -12.016 -18.093 -19.811 1.00 22.00  ? 1384 HOH   A O   1 
HETATM 4167 O O   . HOH   C 3 .   ? 1.097   -9.297  -10.118 1.00 37.87  ? 1385 HOH   A O   1 
HETATM 4168 O O   . HOH   C 3 .   ? -9.072  -25.183 -20.271 1.00 32.66  ? 1386 HOH   A O   1 
HETATM 4169 O O   . HOH   C 3 .   ? 9.939   22.225  -8.667  1.00 36.35  ? 1387 HOH   A O   1 
HETATM 4170 O O   . HOH   C 3 .   ? 18.558  10.315  10.830  1.00 25.10  ? 1388 HOH   A O   1 
HETATM 4171 O O   . HOH   C 3 .   ? -21.040 -6.280  -27.013 1.00 23.11  ? 1389 HOH   A O   1 
HETATM 4172 O O   . HOH   C 3 .   ? 48.855  27.609  -22.664 1.00 36.94  ? 1390 HOH   A O   1 
HETATM 4173 O O   . HOH   C 3 .   ? 43.116  25.168  -2.383  1.00 37.16  ? 1391 HOH   A O   1 
HETATM 4174 O O   . HOH   C 3 .   ? -11.221 -20.882 -15.034 1.00 40.78  ? 1392 HOH   A O   1 
HETATM 4175 O O   . HOH   C 3 .   ? 32.744  -4.326  -10.628 1.00 34.44  ? 1393 HOH   A O   1 
HETATM 4176 O O   . HOH   C 3 .   ? -19.353 -1.093  -19.353 1.00 46.16  ? 1394 HOH   A O   1 
HETATM 4177 O O   . HOH   C 3 .   ? 24.949  18.051  0.695   1.00 45.28  ? 1395 HOH   A O   1 
HETATM 4178 O O   . HOH   C 3 .   ? 18.684  -12.298 3.245   1.00 41.26  ? 1396 HOH   A O   1 
HETATM 4179 O O   . HOH   C 3 .   ? 17.260  -9.985  -18.734 1.00 36.98  ? 1397 HOH   A O   1 
HETATM 4180 O O   . HOH   C 3 .   ? 43.513  -1.297  -17.065 1.00 40.56  ? 1398 HOH   A O   1 
HETATM 4181 O O   . HOH   C 3 .   ? 6.783   1.854   -0.835  1.00 39.10  ? 1399 HOH   A O   1 
HETATM 4182 O O   . HOH   C 3 .   ? -8.296  -19.355 -16.076 1.00 50.96  ? 1400 HOH   A O   1 
HETATM 4183 O O   . HOH   C 3 .   ? 33.176  31.783  -14.810 1.00 45.90  ? 1401 HOH   A O   1 
HETATM 4184 O O   . HOH   C 3 .   ? 32.699  32.803  -12.499 1.00 27.25  ? 1402 HOH   A O   1 
HETATM 4185 O O   . HOH   C 3 .   ? 5.376   11.825  -12.798 1.00 30.61  ? 1403 HOH   A O   1 
HETATM 4186 O O   . HOH   C 3 .   ? -7.140  5.585   -20.549 1.00 34.74  ? 1404 HOH   A O   1 
HETATM 4187 O O   . HOH   C 3 .   ? -24.871 -5.620  -12.070 1.00 28.36  ? 1405 HOH   A O   1 
HETATM 4188 O O   . HOH   C 3 .   ? -28.472 -7.080  -21.204 1.00 33.86  ? 1406 HOH   A O   1 
HETATM 4189 O O   . HOH   C 3 .   ? 40.983  11.377  -0.985  1.00 33.93  ? 1407 HOH   A O   1 
HETATM 4190 O O   . HOH   C 3 .   ? -20.654 -16.429 -31.025 1.00 43.23  ? 1408 HOH   A O   1 
HETATM 4191 O O   . HOH   C 3 .   ? 0.035   -11.619 0.553   1.00 41.79  ? 1409 HOH   A O   1 
HETATM 4192 O O   . HOH   C 3 .   ? -17.150 -0.918  -24.735 1.00 32.30  ? 1410 HOH   A O   1 
HETATM 4193 O O   . HOH   C 3 .   ? -11.514 -17.628 -15.565 1.00 34.78  ? 1411 HOH   A O   1 
HETATM 4194 O O   . HOH   C 3 .   ? 35.909  32.854  -8.366  1.00 27.71  ? 1412 HOH   A O   1 
HETATM 4195 O O   . HOH   C 3 .   ? 34.466  33.152  -5.973  1.00 41.63  ? 1413 HOH   A O   1 
HETATM 4196 O O   . HOH   C 3 .   ? -21.026 -3.894  -26.450 1.00 23.97  ? 1414 HOH   A O   1 
HETATM 4197 O O   . HOH   C 3 .   ? 4.944   -7.669  -4.253  1.00 32.54  ? 1415 HOH   A O   1 
HETATM 4198 O O   . HOH   C 3 .   ? -0.217  -10.501 -11.675 1.00 42.62  ? 1416 HOH   A O   1 
HETATM 4199 O O   . HOH   C 3 .   ? -31.914 -33.094 -32.590 1.00 30.33  ? 1417 HOH   A O   1 
HETATM 4200 O O   . HOH   C 3 .   ? 27.099  33.696  -12.565 1.00 32.61  ? 1418 HOH   A O   1 
HETATM 4201 O O   . HOH   C 3 .   ? 23.443  16.428  3.998   1.00 34.05  ? 1419 HOH   A O   1 
HETATM 4202 O O   . HOH   C 3 .   ? -24.840 -4.082  -13.497 1.00 24.68  ? 1420 HOH   A O   1 
HETATM 4203 O O   . HOH   C 3 .   ? 40.982  7.945   -1.691  1.00 32.71  ? 1421 HOH   A O   1 
HETATM 4204 O O   . HOH   C 3 .   ? 21.081  18.100  1.167   1.00 7.51   ? 1422 HOH   A O   1 
HETATM 4205 O O   . HOH   C 3 .   ? -5.843  -17.347 -5.587  1.00 33.74  ? 1423 HOH   A O   1 
HETATM 4206 O O   . HOH   C 3 .   ? -5.728  -17.082 -7.805  1.00 31.94  ? 1424 HOH   A O   1 
HETATM 4207 O O   . HOH   C 3 .   ? 33.142  -7.834  7.035   1.00 27.06  ? 1425 HOH   A O   1 
HETATM 4208 O O   . HOH   C 3 .   ? 17.763  -7.649  -20.116 1.00 38.68  ? 1426 HOH   A O   1 
HETATM 4209 O O   . HOH   C 3 .   ? -19.660 -2.296  -23.327 1.00 47.88  ? 1427 HOH   A O   1 
HETATM 4210 O O   . HOH   C 3 .   ? -11.203 -22.770 2.057   1.00 30.23  ? 1428 HOH   A O   1 
HETATM 4211 O O   . HOH   C 3 .   ? -1.460  -5.674  -2.731  1.00 30.05  ? 1429 HOH   A O   1 
HETATM 4212 O O   . HOH   C 3 .   ? -29.839 -23.415 -30.760 1.00 23.00  ? 1430 HOH   A O   1 
HETATM 4213 O O   . HOH   C 3 .   ? 30.333  32.981  -11.251 1.00 40.60  ? 1431 HOH   A O   1 
HETATM 4214 O O   . HOH   C 3 .   ? -22.476 -20.001 -31.180 1.00 42.34  ? 1432 HOH   A O   1 
HETATM 4215 O O   . HOH   C 3 .   ? 20.870  27.060  -2.803  1.00 37.43  ? 1433 HOH   A O   1 
HETATM 4216 O O   . HOH   C 3 .   ? 23.292  19.382  4.108   1.00 36.89  ? 1434 HOH   A O   1 
HETATM 4217 O O   . HOH   C 3 .   ? 45.821  21.484  -15.902 1.00 30.07  ? 1435 HOH   A O   1 
HETATM 4218 O O   . HOH   C 3 .   ? -16.312 0.999   -22.119 1.00 36.33  ? 1436 HOH   A O   1 
HETATM 4219 O O   . HOH   C 3 .   ? 12.588  6.528   -0.083  1.00 34.88  ? 1437 HOH   A O   1 
HETATM 4220 O O   . HOH   C 3 .   ? -35.237 -14.126 -19.025 1.00 22.22  ? 1438 HOH   A O   1 
HETATM 4221 O O   . HOH   C 3 .   ? -21.964 -25.619 -31.959 1.00 39.95  ? 1439 HOH   A O   1 
HETATM 4222 O O   . HOH   C 3 .   ? 32.016  -4.374  -26.033 1.00 33.57  ? 1440 HOH   A O   1 
HETATM 4223 O O   . HOH   C 3 .   ? -20.064 -20.213 -31.807 1.00 40.54  ? 1441 HOH   A O   1 
HETATM 4224 O O   . HOH   C 3 .   ? 19.894  15.815  4.962   1.00 44.79  ? 1442 HOH   A O   1 
HETATM 4225 O O   . HOH   C 3 .   ? 27.101  33.715  -8.456  1.00 28.16  ? 1443 HOH   A O   1 
HETATM 4226 O O   . HOH   C 3 .   ? -22.184 -20.458 -28.218 1.00 39.12  ? 1444 HOH   A O   1 
HETATM 4227 O O   . HOH   C 3 .   ? 32.614  19.815  -21.678 1.00 33.88  ? 1445 HOH   A O   1 
HETATM 4228 O O   . HOH   C 3 .   ? -29.431 -21.577 -31.972 1.00 28.36  ? 1446 HOH   A O   1 
HETATM 4229 O O   . HOH   C 3 .   ? -20.196 -18.569 -30.684 1.00 49.20  ? 1447 HOH   A O   1 
HETATM 4230 O O   . HOH   C 3 .   ? 26.679  34.533  -15.308 1.00 44.16  ? 1448 HOH   A O   1 
HETATM 4231 O O   . HOH   C 3 .   ? 28.072  26.065  -20.184 1.00 21.75  ? 1449 HOH   A O   1 
HETATM 4232 O O   . HOH   C 3 .   ? 28.112  -7.890  0.921   1.00 23.07  ? 1450 HOH   A O   1 
HETATM 4233 O O   . HOH   C 3 .   ? -23.057 -22.108 -31.434 1.00 31.35  ? 1451 HOH   A O   1 
HETATM 4234 O O   . HOH   C 3 .   ? 23.825  35.142  -15.319 1.00 41.70  ? 1452 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LEU A 25  ? 0.5661 0.5975 0.4737 0.0894  -0.0421 -0.0617 -4   LEU A N   
2    C CA  . LEU A 25  ? 0.5733 0.6093 0.4714 0.0971  -0.0369 -0.0622 -4   LEU A CA  
3    C C   . LEU A 25  ? 0.5830 0.6039 0.4643 0.1040  -0.0415 -0.0666 -4   LEU A C   
4    O O   . LEU A 25  ? 0.5933 0.6125 0.4645 0.1065  -0.0399 -0.0670 -4   LEU A O   
5    C CB  . LEU A 25  ? 0.5776 0.6247 0.4801 0.1020  -0.0314 -0.0620 -4   LEU A CB  
6    C CG  . LEU A 25  ? 0.5946 0.6516 0.4908 0.1098  -0.0243 -0.0639 -4   LEU A CG  
7    C CD1 . LEU A 25  ? 0.6004 0.6597 0.4889 0.1076  -0.0200 -0.0624 -4   LEU A CD1 
8    C CD2 . LEU A 25  ? 0.5825 0.6573 0.4914 0.1103  -0.0181 -0.0626 -4   LEU A CD2 
9    N N   . TYR A 26  ? 0.5808 0.5889 0.4572 0.1069  -0.0477 -0.0698 -3   TYR A N   
10   C CA  . TYR A 26  ? 0.5768 0.5685 0.4370 0.1134  -0.0536 -0.0741 -3   TYR A CA  
11   C C   . TYR A 26  ? 0.5536 0.5313 0.4132 0.1073  -0.0623 -0.0757 -3   TYR A C   
12   O O   . TYR A 26  ? 0.5669 0.5288 0.4138 0.1116  -0.0688 -0.0794 -3   TYR A O   
13   C CB  . TYR A 26  ? 0.5989 0.5846 0.4512 0.1223  -0.0553 -0.0776 -3   TYR A CB  
14   C CG  . TYR A 26  ? 0.6116 0.6135 0.4659 0.1293  -0.0468 -0.0780 -3   TYR A CG  
15   C CD1 . TYR A 26  ? 0.6265 0.6342 0.4721 0.1347  -0.0412 -0.0797 -3   TYR A CD1 
16   C CD2 . TYR A 26  ? 0.6023 0.6142 0.4671 0.1298  -0.0444 -0.0772 -3   TYR A CD2 
17   C CE1 . TYR A 26  ? 0.6286 0.6539 0.4775 0.1399  -0.0325 -0.0811 -3   TYR A CE1 
18   C CE2 . TYR A 26  ? 0.6025 0.6317 0.4714 0.1361  -0.0368 -0.0788 -3   TYR A CE2 
19   C CZ  . TYR A 26  ? 0.6181 0.6551 0.4798 0.1408  -0.0304 -0.0809 -3   TYR A CZ  
20   O OH  . TYR A 26  ? 0.6272 0.6837 0.4940 0.1460  -0.0219 -0.0835 -3   TYR A OH  
21   N N   . PHE A 27  ? 0.5340 0.5180 0.4077 0.0975  -0.0628 -0.0735 -2   PHE A N   
22   C CA  . PHE A 27  ? 0.5289 0.5045 0.4063 0.0905  -0.0702 -0.0761 -2   PHE A CA  
23   C C   . PHE A 27  ? 0.5137 0.5028 0.4082 0.0816  -0.0680 -0.0739 -2   PHE A C   
24   O O   . PHE A 27  ? 0.5029 0.5041 0.4074 0.0785  -0.0622 -0.0703 -2   PHE A O   
25   C CB  . PHE A 27  ? 0.5437 0.5073 0.4191 0.0872  -0.0753 -0.0781 -2   PHE A CB  
26   C CG  . PHE A 27  ? 0.5480 0.5066 0.4304 0.0776  -0.0815 -0.0812 -2   PHE A CG  
27   C CD1 . PHE A 27  ? 0.5602 0.5069 0.4348 0.0793  -0.0890 -0.0857 -2   PHE A CD1 
28   C CD2 . PHE A 27  ? 0.5390 0.5057 0.4360 0.0666  -0.0798 -0.0804 -2   PHE A CD2 
29   C CE1 . PHE A 27  ? 0.5585 0.5032 0.4418 0.0701  -0.0947 -0.0898 -2   PHE A CE1 
30   C CE2 . PHE A 27  ? 0.5367 0.5018 0.4419 0.0570  -0.0846 -0.0845 -2   PHE A CE2 
31   C CZ  . PHE A 27  ? 0.5432 0.4981 0.4425 0.0588  -0.0922 -0.0895 -2   PHE A CZ  
32   N N   . GLN A 28  ? 0.5254 0.5124 0.4233 0.0781  -0.0735 -0.0768 -1   GLN A N   
33   C CA  . GLN A 28  ? 0.5334 0.5329 0.4474 0.0709  -0.0728 -0.0762 -1   GLN A CA  
34   C C   . GLN A 28  ? 0.5307 0.5315 0.4575 0.0614  -0.0763 -0.0797 -1   GLN A C   
35   O O   . GLN A 28  ? 0.5336 0.5247 0.4581 0.0597  -0.0832 -0.0849 -1   GLN A O   
36   C CB  . GLN A 28  ? 0.5728 0.5696 0.4828 0.0734  -0.0775 -0.0783 -1   GLN A CB  
37   C CG  . GLN A 28  ? 0.6330 0.6249 0.5256 0.0816  -0.0740 -0.0754 -1   GLN A CG  
38   C CD  . GLN A 28  ? 0.6797 0.6659 0.5648 0.0835  -0.0788 -0.0766 -1   GLN A CD  
39   O OE1 . GLN A 28  ? 0.7003 0.6892 0.5783 0.0849  -0.0740 -0.0727 -1   GLN A OE1 
40   N NE2 . GLN A 28  ? 0.6963 0.6733 0.5819 0.0832  -0.0888 -0.0824 -1   GLN A NE2 
41   N N   . GLU A 29  ? 0.5319 0.5444 0.4716 0.0547  -0.0712 -0.0771 566  GLU A N   
42   C CA  . GLU A 29  ? 0.5327 0.5476 0.4840 0.0442  -0.0726 -0.0803 566  GLU A CA  
43   C C   . GLU A 29  ? 0.4765 0.5021 0.4432 0.0390  -0.0760 -0.0852 566  GLU A C   
44   O O   . GLU A 29  ? 0.4189 0.4496 0.3872 0.0436  -0.0772 -0.0849 566  GLU A O   
45   C CB  . GLU A 29  ? 0.5763 0.5976 0.5329 0.0393  -0.0658 -0.0757 566  GLU A CB  
46   C CG  . GLU A 29  ? 0.6354 0.6466 0.5779 0.0453  -0.0636 -0.0720 566  GLU A CG  
47   C CD  . GLU A 29  ? 0.6726 0.6878 0.6197 0.0403  -0.0586 -0.0682 566  GLU A CD  
48   O OE1 . GLU A 29  ? 0.6701 0.6991 0.6307 0.0350  -0.0546 -0.0665 566  GLU A OE1 
49   O OE2 . GLU A 29  ? 0.6989 0.7017 0.6347 0.0421  -0.0595 -0.0673 566  GLU A OE2 
50   N N   . GLN A 30  ? 0.5236 0.5522 0.5010 0.0292  -0.0778 -0.0902 567  GLN A N   
51   C CA  . GLN A 30  ? 0.5858 0.6275 0.5809 0.0239  -0.0811 -0.0968 567  GLN A CA  
52   C C   . GLN A 30  ? 0.6489 0.7060 0.6553 0.0234  -0.0762 -0.0935 567  GLN A C   
53   O O   . GLN A 30  ? 0.6839 0.7450 0.6915 0.0200  -0.0690 -0.0881 567  GLN A O   
54   C CB  . GLN A 30  ? 0.5174 0.5621 0.5227 0.0116  -0.0815 -0.1028 567  GLN A CB  
55   C CG  . GLN A 30  ? 0.4746 0.5375 0.5018 0.0049  -0.0831 -0.1108 567  GLN A CG  
56   C CD  . GLN A 30  ? 0.4681 0.5362 0.5054 -0.0092 -0.0813 -0.1169 567  GLN A CD  
57   O OE1 . GLN A 30  ? 0.4641 0.5322 0.4999 -0.0174 -0.0741 -0.1130 567  GLN A OE1 
58   N NE2 . GLN A 30  ? 0.4718 0.5438 0.5189 -0.0127 -0.0879 -0.1269 567  GLN A NE2 
59   N N   . PRO A 31  ? 0.5198 0.5838 0.5331 0.0271  -0.0807 -0.0967 568  PRO A N   
60   C CA  . PRO A 31  ? 0.4322 0.5085 0.4539 0.0273  -0.0770 -0.0933 568  PRO A CA  
61   C C   . PRO A 31  ? 0.3754 0.4669 0.4153 0.0173  -0.0731 -0.0963 568  PRO A C   
62   O O   . PRO A 31  ? 0.3472 0.4434 0.3974 0.0100  -0.0750 -0.1039 568  PRO A O   
63   C CB  . PRO A 31  ? 0.3323 0.4082 0.3545 0.0336  -0.0855 -0.0978 568  PRO A CB  
64   C CG  . PRO A 31  ? 0.3492 0.4096 0.3577 0.0391  -0.0920 -0.1005 568  PRO A CG  
65   C CD  . PRO A 31  ? 0.4517 0.5091 0.4617 0.0328  -0.0904 -0.1029 568  PRO A CD  
66   N N   . LEU A 32  ? 0.3882 0.4877 0.4317 0.0167  -0.0672 -0.0906 569  LEU A N   
67   C CA  . LEU A 32  ? 0.3860 0.4998 0.4453 0.0080  -0.0628 -0.0927 569  LEU A CA  
68   C C   . LEU A 32  ? 0.3957 0.5226 0.4709 0.0083  -0.0686 -0.1010 569  LEU A C   
69   O O   . LEU A 32  ? 0.3979 0.5235 0.4700 0.0160  -0.0735 -0.1000 569  LEU A O   
70   C CB  . LEU A 32  ? 0.3725 0.4886 0.4289 0.0084  -0.0554 -0.0835 569  LEU A CB  
71   C CG  . LEU A 32  ? 0.3875 0.5102 0.4509 -0.0010 -0.0483 -0.0822 569  LEU A CG  
72   C CD1 . LEU A 32  ? 0.4097 0.5201 0.4626 -0.0059 -0.0457 -0.0807 569  LEU A CD1 
73   C CD2 . LEU A 32  ? 0.3807 0.5075 0.4433 0.0015  -0.0434 -0.0741 569  LEU A CD2 
74   N N   . ARG A 33  ? 0.4128 0.5519 0.5042 -0.0003 -0.0684 -0.1098 570  ARG A N   
75   C CA  . ARG A 33  ? 0.4216 0.5756 0.5307 0.0003  -0.0745 -0.1199 570  ARG A CA  
76   C C   . ARG A 33  ? 0.4067 0.5733 0.5250 -0.0013 -0.0699 -0.1176 570  ARG A C   
77   O O   . ARG A 33  ? 0.4130 0.5850 0.5347 -0.0097 -0.0613 -0.1148 570  ARG A O   
78   C CB  . ARG A 33  ? 0.4575 0.6221 0.5819 -0.0085 -0.0759 -0.1319 570  ARG A CB  
79   C CG  . ARG A 33  ? 0.4763 0.6545 0.6181 -0.0047 -0.0855 -0.1449 570  ARG A CG  
80   C CD  . ARG A 33  ? 0.4843 0.6801 0.6466 -0.0155 -0.0844 -0.1580 570  ARG A CD  
81   N NE  . ARG A 33  ? 0.4871 0.6990 0.6687 -0.0107 -0.0937 -0.1715 570  ARG A NE  
82   C CZ  . ARG A 33  ? 0.5031 0.7375 0.7081 -0.0187 -0.0929 -0.1852 570  ARG A CZ  
83   N NH1 . ARG A 33  ? 0.5148 0.7569 0.7250 -0.0334 -0.0823 -0.1864 570  ARG A NH1 
84   N NH2 . ARG A 33  ? 0.5071 0.7558 0.7295 -0.0120 -0.1029 -0.1982 570  ARG A NH2 
85   N N   . LEU A 34  ? 0.3811 0.5502 0.5015 0.0067  -0.0765 -0.1188 571  LEU A N   
86   C CA  . LEU A 34  ? 0.3553 0.5330 0.4812 0.0072  -0.0738 -0.1156 571  LEU A CA  
87   C C   . LEU A 34  ? 0.3527 0.5452 0.4964 0.0092  -0.0816 -0.1277 571  LEU A C   
88   O O   . LEU A 34  ? 0.3634 0.5563 0.5119 0.0134  -0.0912 -0.1373 571  LEU A O   
89   C CB  . LEU A 34  ? 0.3345 0.4991 0.4431 0.0151  -0.0747 -0.1045 571  LEU A CB  
90   C CG  . LEU A 34  ? 0.3060 0.4596 0.3991 0.0143  -0.0664 -0.0927 571  LEU A CG  
91   C CD1 . LEU A 34  ? 0.3029 0.4460 0.3807 0.0218  -0.0680 -0.0844 571  LEU A CD1 
92   C CD2 . LEU A 34  ? 0.2839 0.4450 0.3826 0.0068  -0.0568 -0.0883 571  LEU A CD2 
93   N N   . PRO A 35  ? 0.3409 0.5458 0.4948 0.0069  -0.0784 -0.1282 572  PRO A N   
94   C CA  . PRO A 35  ? 0.3281 0.5473 0.4987 0.0106  -0.0867 -0.1404 572  PRO A CA  
95   C C   . PRO A 35  ? 0.3316 0.5385 0.4917 0.0225  -0.0989 -0.1395 572  PRO A C   
96   O O   . PRO A 35  ? 0.3294 0.5183 0.4692 0.0269  -0.0991 -0.1285 572  PRO A O   
97   C CB  . PRO A 35  ? 0.3153 0.5474 0.4950 0.0053  -0.0790 -0.1386 572  PRO A CB  
98   C CG  . PRO A 35  ? 0.3190 0.5382 0.4818 0.0032  -0.0702 -0.1229 572  PRO A CG  
99   C CD  . PRO A 35  ? 0.3303 0.5373 0.4819 0.0009  -0.0674 -0.1191 572  PRO A CD  
100  N N   . SER A 36  ? 0.3447 0.5616 0.5183 0.0276  -0.1092 -0.1522 573  SER A N   
101  C CA  . SER A 36  ? 0.3649 0.5679 0.5273 0.0390  -0.1231 -0.1533 573  SER A CA  
102  C C   . SER A 36  ? 0.3894 0.5845 0.5399 0.0416  -0.1219 -0.1426 573  SER A C   
103  O O   . SER A 36  ? 0.3801 0.5883 0.5409 0.0372  -0.1152 -0.1417 573  SER A O   
104  C CB  . SER A 36  ? 0.3691 0.5853 0.5502 0.0446  -0.1359 -0.1712 573  SER A CB  
105  O OG  . SER A 36  ? 0.3780 0.5863 0.5524 0.0540  -0.1471 -0.1721 573  SER A OG  
106  N N   . PRO A 37  ? 0.4170 0.5903 0.5449 0.0480  -0.1282 -0.1346 574  PRO A N   
107  C CA  . PRO A 37  ? 0.4292 0.5944 0.5455 0.0502  -0.1290 -0.1259 574  PRO A CA  
108  C C   . PRO A 37  ? 0.4588 0.6317 0.5861 0.0555  -0.1396 -0.1358 574  PRO A C   
109  O O   . PRO A 37  ? 0.4717 0.6377 0.5899 0.0571  -0.1410 -0.1291 574  PRO A O   
110  C CB  . PRO A 37  ? 0.4363 0.5755 0.5252 0.0553  -0.1348 -0.1179 574  PRO A CB  
111  C CG  . PRO A 37  ? 0.4443 0.5784 0.5330 0.0591  -0.1425 -0.1268 574  PRO A CG  
112  C CD  . PRO A 37  ? 0.4239 0.5779 0.5338 0.0523  -0.1336 -0.1323 574  PRO A CD  
113  N N   . GLU A 38  ? 0.4791 0.6666 0.6262 0.0585  -0.1473 -0.1520 575  GLU A N   
114  C CA  . GLU A 38  ? 0.5061 0.7011 0.6643 0.0633  -0.1537 -0.1610 575  GLU A CA  
115  C C   . GLU A 38  ? 0.4526 0.6699 0.6297 0.0556  -0.1410 -0.1621 575  GLU A C   
116  O O   . GLU A 38  ? 0.4558 0.6750 0.6369 0.0587  -0.1418 -0.1653 575  GLU A O   
117  C CB  . GLU A 38  ? 0.5726 0.7655 0.7382 0.0698  -0.1609 -0.1743 575  GLU A CB  
118  C CG  . GLU A 38  ? 0.6349 0.8006 0.7795 0.0801  -0.1758 -0.1744 575  GLU A CG  
119  C CD  . GLU A 38  ? 0.6704 0.8240 0.8005 0.0794  -0.1790 -0.1698 575  GLU A CD  
120  O OE1 . GLU A 38  ? 0.6753 0.8424 0.8181 0.0739  -0.1729 -0.1736 575  GLU A OE1 
121  O OE2 . GLU A 38  ? 0.6888 0.8180 0.7931 0.0840  -0.1875 -0.1625 575  GLU A OE2 
122  N N   . VAL A 39  ? 0.4050 0.6371 0.5919 0.0458  -0.1294 -0.1598 576  VAL A N   
123  C CA  . VAL A 39  ? 0.3566 0.6069 0.5576 0.0371  -0.1166 -0.1594 576  VAL A CA  
124  C C   . VAL A 39  ? 0.3359 0.5774 0.5231 0.0304  -0.1040 -0.1423 576  VAL A C   
125  O O   . VAL A 39  ? 0.3360 0.5889 0.5311 0.0237  -0.0942 -0.1401 576  VAL A O   
126  C CB  . VAL A 39  ? 0.3449 0.6119 0.5635 0.0292  -0.1079 -0.1693 576  VAL A CB  
127  C CG1 . VAL A 39  ? 0.3550 0.6241 0.5822 0.0357  -0.1141 -0.1827 576  VAL A CG1 
128  C CG2 . VAL A 39  ? 0.3470 0.6101 0.5614 0.0242  -0.1052 -0.1666 576  VAL A CG2 
129  N N   . TYR A 40  ? 0.3128 0.5341 0.4792 0.0323  -0.1039 -0.1303 577  TYR A N   
130  C CA  . TYR A 40  ? 0.3049 0.5184 0.4590 0.0269  -0.0924 -0.1149 577  TYR A CA  
131  C C   . TYR A 40  ? 0.3313 0.5231 0.4625 0.0323  -0.0970 -0.1048 577  TYR A C   
132  O O   . TYR A 40  ? 0.3531 0.5351 0.4743 0.0326  -0.0962 -0.1018 577  TYR A O   
133  C CB  . TYR A 40  ? 0.2869 0.5053 0.4446 0.0183  -0.0810 -0.1131 577  TYR A CB  
134  C CG  . TYR A 40  ? 0.2695 0.4828 0.4180 0.0129  -0.0695 -0.0997 577  TYR A CG  
135  C CD1 . TYR A 40  ? 0.2523 0.4735 0.4065 0.0091  -0.0639 -0.0968 577  TYR A CD1 
136  C CD2 . TYR A 40  ? 0.2653 0.4661 0.3997 0.0121  -0.0649 -0.0909 577  TYR A CD2 
137  C CE1 . TYR A 40  ? 0.2344 0.4504 0.3804 0.0048  -0.0546 -0.0854 577  TYR A CE1 
138  C CE2 . TYR A 40  ? 0.2557 0.4525 0.3828 0.0083  -0.0556 -0.0801 577  TYR A CE2 
139  C CZ  . TYR A 40  ? 0.2485 0.4527 0.3815 0.0047  -0.0508 -0.0774 577  TYR A CZ  
140  O OH  . TYR A 40  ? 0.2567 0.4563 0.3825 0.0015  -0.0428 -0.0674 577  TYR A OH  
141  N N   . ARG A 41  ? 0.3293 0.5136 0.4517 0.0359  -0.1019 -0.0997 578  ARG A N   
142  C CA  . ARG A 41  ? 0.3419 0.5050 0.4415 0.0404  -0.1077 -0.0920 578  ARG A CA  
143  C C   . ARG A 41  ? 0.3417 0.4968 0.4277 0.0360  -0.0968 -0.0789 578  ARG A C   
144  O O   . ARG A 41  ? 0.3599 0.4985 0.4264 0.0384  -0.0996 -0.0726 578  ARG A O   
145  C CB  . ARG A 41  ? 0.3370 0.4926 0.4290 0.0441  -0.1158 -0.0898 578  ARG A CB  
146  C CG  . ARG A 41  ? 0.3138 0.4799 0.4140 0.0397  -0.1085 -0.0849 578  ARG A CG  
147  C CD  . ARG A 41  ? 0.3199 0.4748 0.4091 0.0437  -0.1180 -0.0823 578  ARG A CD  
148  N NE  . ARG A 41  ? 0.3067 0.4693 0.4015 0.0397  -0.1117 -0.0765 578  ARG A NE  
149  C CZ  . ARG A 41  ? 0.3244 0.4755 0.4060 0.0400  -0.1154 -0.0689 578  ARG A CZ  
150  N NH1 . ARG A 41  ? 0.3080 0.4667 0.3958 0.0365  -0.1098 -0.0640 578  ARG A NH1 
151  N NH2 . ARG A 41  ? 0.3557 0.4863 0.4165 0.0433  -0.1249 -0.0659 578  ARG A NH2 
152  N N   . PHE A 42  ? 0.3219 0.4876 0.4165 0.0299  -0.0848 -0.0753 579  PHE A N   
153  C CA  . PHE A 42  ? 0.3077 0.4672 0.3911 0.0270  -0.0753 -0.0645 579  PHE A CA  
154  C C   . PHE A 42  ? 0.3342 0.4865 0.4104 0.0284  -0.0750 -0.0660 579  PHE A C   
155  O O   . PHE A 42  ? 0.3477 0.4937 0.4128 0.0275  -0.0685 -0.0582 579  PHE A O   
156  C CB  . PHE A 42  ? 0.2670 0.4375 0.3603 0.0208  -0.0644 -0.0606 579  PHE A CB  
157  C CG  . PHE A 42  ? 0.2481 0.4243 0.3464 0.0193  -0.0634 -0.0573 579  PHE A CG  
158  C CD1 . PHE A 42  ? 0.2189 0.3883 0.3062 0.0196  -0.0619 -0.0475 579  PHE A CD1 
159  C CD2 . PHE A 42  ? 0.2361 0.4249 0.3499 0.0172  -0.0638 -0.0644 579  PHE A CD2 
160  C CE1 . PHE A 42  ? 0.2107 0.3844 0.3021 0.0181  -0.0617 -0.0445 579  PHE A CE1 
161  C CE2 . PHE A 42  ? 0.2140 0.4070 0.3314 0.0162  -0.0633 -0.0615 579  PHE A CE2 
162  C CZ  . PHE A 42  ? 0.1953 0.3801 0.3014 0.0169  -0.0627 -0.0514 579  PHE A CZ  
163  N N   . VAL A 43  ? 0.3412 0.4947 0.4236 0.0307  -0.0822 -0.0765 580  VAL A N   
164  C CA  . VAL A 43  ? 0.3649 0.5105 0.4401 0.0323  -0.0829 -0.0783 580  VAL A CA  
165  C C   . VAL A 43  ? 0.3965 0.5255 0.4551 0.0389  -0.0931 -0.0793 580  VAL A C   
166  O O   . VAL A 43  ? 0.3979 0.5182 0.4484 0.0412  -0.0951 -0.0812 580  VAL A O   
167  C CB  . VAL A 43  ? 0.3572 0.5136 0.4488 0.0296  -0.0837 -0.0892 580  VAL A CB  
168  C CG1 . VAL A 43  ? 0.3475 0.5158 0.4501 0.0216  -0.0727 -0.0871 580  VAL A CG1 
169  C CG2 . VAL A 43  ? 0.3605 0.5248 0.4652 0.0328  -0.0943 -0.1012 580  VAL A CG2 
170  N N   . VAL A 44  ? 0.4243 0.5466 0.4757 0.0421  -0.1003 -0.0782 581  VAL A N   
171  C CA  . VAL A 44  ? 0.4617 0.5639 0.4921 0.0475  -0.1100 -0.0777 581  VAL A CA  
172  C C   . VAL A 44  ? 0.4849 0.5758 0.4967 0.0463  -0.1025 -0.0689 581  VAL A C   
173  O O   . VAL A 44  ? 0.4717 0.5672 0.4819 0.0420  -0.0913 -0.0599 581  VAL A O   
174  C CB  . VAL A 44  ? 0.4772 0.5714 0.4985 0.0491  -0.1166 -0.0748 581  VAL A CB  
175  C CG1 . VAL A 44  ? 0.5116 0.5808 0.5058 0.0531  -0.1257 -0.0725 581  VAL A CG1 
176  C CG2 . VAL A 44  ? 0.4706 0.5756 0.5099 0.0521  -0.1258 -0.0856 581  VAL A CG2 
177  N N   . LYS A 45  ? 0.5269 0.6035 0.5254 0.0506  -0.1090 -0.0722 582  LYS A N   
178  C CA  . LYS A 45  ? 0.5509 0.6174 0.5322 0.0502  -0.1022 -0.0656 582  LYS A CA  
179  C C   . LYS A 45  ? 0.5620 0.6209 0.5257 0.0473  -0.0960 -0.0549 582  LYS A C   
180  O O   . LYS A 45  ? 0.5744 0.6227 0.5265 0.0476  -0.1026 -0.0532 582  LYS A O   
181  C CB  . LYS A 45  ? 0.5802 0.6292 0.5467 0.0558  -0.1123 -0.0713 582  LYS A CB  
182  C CG  . LYS A 45  ? 0.5983 0.6367 0.5467 0.0562  -0.1058 -0.0661 582  LYS A CG  
183  C CD  . LYS A 45  ? 0.6066 0.6566 0.5692 0.0552  -0.0995 -0.0689 582  LYS A CD  
184  C CE  . LYS A 45  ? 0.6345 0.6735 0.5797 0.0572  -0.0949 -0.0656 582  LYS A CE  
185  N NZ  . LYS A 45  ? 0.6299 0.6756 0.5875 0.0574  -0.0937 -0.0709 582  LYS A NZ  
186  N N   . ASP A 46  ? 0.5631 0.6275 0.5248 0.0443  -0.0836 -0.0481 583  ASP A N   
187  C CA  . ASP A 46  ? 0.5905 0.6498 0.5360 0.0410  -0.0765 -0.0389 583  ASP A CA  
188  C C   . ASP A 46  ? 0.6306 0.6673 0.5487 0.0428  -0.0826 -0.0382 583  ASP A C   
189  O O   . ASP A 46  ? 0.6455 0.6717 0.5557 0.0473  -0.0882 -0.0432 583  ASP A O   
190  C CB  . ASP A 46  ? 0.5973 0.6670 0.5461 0.0391  -0.0632 -0.0342 583  ASP A CB  
191  C CG  . ASP A 46  ? 0.5928 0.6809 0.5614 0.0356  -0.0559 -0.0314 583  ASP A CG  
192  O OD1 . ASP A 46  ? 0.5946 0.6883 0.5752 0.0342  -0.0602 -0.0332 583  ASP A OD1 
193  O OD2 . ASP A 46  ? 0.5803 0.6765 0.5516 0.0346  -0.0462 -0.0279 583  ASP A OD2 
194  N N   . SER A 47  ? 0.6485 0.6763 0.5506 0.0389  -0.0819 -0.0318 584  SER A N   
195  C CA  . SER A 47  ? 0.6826 0.6866 0.5542 0.0387  -0.0863 -0.0298 584  SER A CA  
196  C C   . SER A 47  ? 0.7024 0.7042 0.5607 0.0310  -0.0789 -0.0208 584  SER A C   
197  O O   . SER A 47  ? 0.6828 0.7012 0.5569 0.0270  -0.0722 -0.0170 584  SER A O   
198  C CB  . SER A 47  ? 0.6891 0.6741 0.5511 0.0437  -0.1037 -0.0363 584  SER A CB  
199  O OG  . SER A 47  ? 0.6798 0.6607 0.5397 0.0412  -0.1096 -0.0342 584  SER A OG  
200  N N   . GLU A 48  ? 0.7420 0.7221 0.5699 0.0283  -0.0803 -0.0176 585  GLU A N   
201  C CA  . GLU A 48  ? 0.7533 0.7288 0.5650 0.0193  -0.0736 -0.0094 585  GLU A CA  
202  C C   . GLU A 48  ? 0.7402 0.7058 0.5481 0.0171  -0.0840 -0.0080 585  GLU A C   
203  O O   . GLU A 48  ? 0.7431 0.7050 0.5390 0.0087  -0.0793 -0.0011 585  GLU A O   
204  C CB  . GLU A 48  ? 0.8029 0.7566 0.5804 0.0157  -0.0712 -0.0067 585  GLU A CB  
205  C CG  . GLU A 48  ? 0.8184 0.7782 0.5958 0.0193  -0.0628 -0.0092 585  GLU A CG  
206  C CD  . GLU A 48  ? 0.8097 0.7982 0.6078 0.0168  -0.0463 -0.0067 585  GLU A CD  
207  O OE1 . GLU A 48  ? 0.8065 0.8077 0.6124 0.0102  -0.0391 -0.0017 585  GLU A OE1 
208  O OE2 . GLU A 48  ? 0.8058 0.8031 0.6118 0.0220  -0.0414 -0.0102 585  GLU A OE2 
209  N N   . GLU A 49  ? 0.7333 0.6951 0.5514 0.0243  -0.0980 -0.0150 586  GLU A N   
210  C CA  . GLU A 49  ? 0.7317 0.6845 0.5475 0.0240  -0.1095 -0.0153 586  GLU A CA  
211  C C   . GLU A 49  ? 0.6662 0.6444 0.5128 0.0235  -0.1053 -0.0151 586  GLU A C   
212  O O   . GLU A 49  ? 0.6635 0.6368 0.5087 0.0221  -0.1123 -0.0138 586  GLU A O   
213  C CB  . GLU A 49  ? 0.7626 0.6972 0.5721 0.0330  -0.1285 -0.0245 586  GLU A CB  
214  C CG  . GLU A 49  ? 0.8031 0.7103 0.5819 0.0350  -0.1348 -0.0259 586  GLU A CG  
215  C CD  . GLU A 49  ? 0.8489 0.7315 0.5910 0.0261  -0.1327 -0.0171 586  GLU A CD  
216  O OE1 . GLU A 49  ? 0.8596 0.7378 0.5958 0.0205  -0.1343 -0.0122 586  GLU A OE1 
217  O OE2 . GLU A 49  ? 0.8795 0.7468 0.5976 0.0241  -0.1291 -0.0152 586  GLU A OE2 
218  N N   . ASN A 50  ? 0.6094 0.6126 0.4818 0.0247  -0.0948 -0.0164 587  ASN A N   
219  C CA  . ASN A 50  ? 0.5590 0.5845 0.4583 0.0236  -0.0904 -0.0160 587  ASN A CA  
220  C C   . ASN A 50  ? 0.5261 0.5719 0.4382 0.0189  -0.0740 -0.0103 587  ASN A C   
221  O O   . ASN A 50  ? 0.4928 0.5542 0.4230 0.0169  -0.0701 -0.0084 587  ASN A O   
222  C CB  . ASN A 50  ? 0.5153 0.5519 0.4379 0.0307  -0.0972 -0.0258 587  ASN A CB  
223  C CG  . ASN A 50  ? 0.4995 0.5399 0.4272 0.0345  -0.0945 -0.0308 587  ASN A CG  
224  O OD1 . ASN A 50  ? 0.4940 0.5397 0.4195 0.0321  -0.0833 -0.0266 587  ASN A OD1 
225  N ND2 . ASN A 50  ? 0.4898 0.5282 0.4250 0.0407  -0.1052 -0.0405 587  ASN A ND2 
226  N N   . ILE A 51  ? 0.5245 0.5703 0.4275 0.0175  -0.0649 -0.0080 588  ILE A N   
227  C CA  . ILE A 51  ? 0.5026 0.5676 0.4173 0.0140  -0.0505 -0.0036 588  ILE A CA  
228  C C   . ILE A 51  ? 0.5339 0.5928 0.4293 0.0114  -0.0425 -0.0008 588  ILE A C   
229  O O   . ILE A 51  ? 0.5671 0.6120 0.4476 0.0148  -0.0465 -0.0040 588  ILE A O   
230  C CB  . ILE A 51  ? 0.4770 0.5594 0.4166 0.0187  -0.0473 -0.0082 588  ILE A CB  
231  C CG1 . ILE A 51  ? 0.4530 0.5538 0.4047 0.0160  -0.0345 -0.0041 588  ILE A CG1 
232  C CG2 . ILE A 51  ? 0.4877 0.5637 0.4234 0.0244  -0.0502 -0.0142 588  ILE A CG2 
233  C CD1 . ILE A 51  ? 0.4310 0.5458 0.4043 0.0196  -0.0321 -0.0077 588  ILE A CD1 
234  N N   . VAL A 52  ? 0.5304 0.6005 0.4265 0.0052  -0.0313 0.0047  589  VAL A N   
235  C CA  . VAL A 52  ? 0.5354 0.6050 0.4162 0.0016  -0.0213 0.0068  589  VAL A CA  
236  C C   . VAL A 52  ? 0.5202 0.6150 0.4209 0.0015  -0.0089 0.0074  589  VAL A C   
237  O O   . VAL A 52  ? 0.4890 0.5979 0.4088 0.0005  -0.0075 0.0090  589  VAL A O   
238  C CB  . VAL A 52  ? 0.5478 0.6027 0.4034 -0.0079 -0.0206 0.0124  589  VAL A CB  
239  C CG1 . VAL A 52  ? 0.5555 0.6114 0.3947 -0.0128 -0.0087 0.0138  589  VAL A CG1 
240  C CG2 . VAL A 52  ? 0.5753 0.6022 0.4095 -0.0066 -0.0351 0.0113  589  VAL A CG2 
241  N N   . PHE A 53  ? 0.5432 0.6428 0.4390 0.0034  -0.0008 0.0053  590  PHE A N   
242  C CA  . PHE A 53  ? 0.5669 0.6891 0.4793 0.0047  0.0101  0.0044  590  PHE A CA  
243  C C   . PHE A 53  ? 0.6040 0.7312 0.5030 -0.0015 0.0212  0.0059  590  PHE A C   
244  O O   . PHE A 53  ? 0.6319 0.7425 0.5060 -0.0063 0.0210  0.0074  590  PHE A O   
245  C CB  . PHE A 53  ? 0.5735 0.6998 0.4953 0.0142  0.0096  -0.0013 590  PHE A CB  
246  C CG  . PHE A 53  ? 0.5706 0.6924 0.5046 0.0192  -0.0002 -0.0038 590  PHE A CG  
247  C CD1 . PHE A 53  ? 0.5851 0.6888 0.5083 0.0211  -0.0103 -0.0060 590  PHE A CD1 
248  C CD2 . PHE A 53  ? 0.5451 0.6809 0.5011 0.0216  0.0007  -0.0046 590  PHE A CD2 
249  C CE1 . PHE A 53  ? 0.5734 0.6760 0.5097 0.0249  -0.0186 -0.0095 590  PHE A CE1 
250  C CE2 . PHE A 53  ? 0.5402 0.6725 0.5066 0.0246  -0.0071 -0.0073 590  PHE A CE2 
251  C CZ  . PHE A 53  ? 0.5533 0.6706 0.5110 0.0260  -0.0162 -0.0101 590  PHE A CZ  
252  N N   . GLU A 54  ? 0.6024 0.7523 0.5175 -0.0014 0.0309  0.0049  591  GLU A N   
253  C CA  . GLU A 54  ? 0.6368 0.7971 0.5435 -0.0076 0.0430  0.0048  591  GLU A CA  
254  C C   . GLU A 54  ? 0.6781 0.8398 0.5782 -0.0008 0.0478  -0.0010 591  GLU A C   
255  O O   . GLU A 54  ? 0.6675 0.8390 0.5832 0.0088  0.0473  -0.0057 591  GLU A O   
256  C CB  . GLU A 54  ? 0.6050 0.7911 0.5336 -0.0103 0.0507  0.0049  591  GLU A CB  
257  C CG  . GLU A 54  ? 0.5860 0.7712 0.5196 -0.0179 0.0470  0.0108  591  GLU A CG  
258  C CD  . GLU A 54  ? 0.5884 0.7711 0.5051 -0.0309 0.0533  0.0149  591  GLU A CD  
259  O OE1 . GLU A 54  ? 0.5737 0.7609 0.4972 -0.0379 0.0526  0.0193  591  GLU A OE1 
260  O OE2 . GLU A 54  ? 0.6052 0.7800 0.5007 -0.0347 0.0587  0.0139  591  GLU A OE2 
261  N N   . ASP A 55  ? 0.7308 0.8798 0.6054 -0.0056 0.0514  -0.0008 592  ASP A N   
262  C CA  . ASP A 55  ? 0.7749 0.9234 0.6397 0.0004  0.0562  -0.0063 592  ASP A CA  
263  C C   . ASP A 55  ? 0.7632 0.9384 0.6378 -0.0010 0.0704  -0.0104 592  ASP A C   
264  O O   . ASP A 55  ? 0.7515 0.9432 0.6367 -0.0086 0.0768  -0.0084 592  ASP A O   
265  C CB  . ASP A 55  ? 0.8434 0.9654 0.6748 -0.0044 0.0539  -0.0045 592  ASP A CB  
266  C CG  . ASP A 55  ? 0.8807 0.9772 0.7041 -0.0007 0.0384  -0.0026 592  ASP A CG  
267  O OD1 . ASP A 55  ? 0.8733 0.9741 0.7171 0.0069  0.0308  -0.0042 592  ASP A OD1 
268  O OD2 . ASP A 55  ? 0.9134 0.9853 0.7094 -0.0055 0.0336  -0.0001 592  ASP A OD2 
269  N N   . GLY A 62  ? 0.6277 0.8295 0.6419 0.0828  0.0193  -0.0419 599  GLY A N   
270  C CA  . GLY A 62  ? 0.6213 0.8338 0.6408 0.0735  0.0248  -0.0365 599  GLY A CA  
271  C C   . GLY A 62  ? 0.6176 0.8171 0.6295 0.0654  0.0223  -0.0307 599  GLY A C   
272  O O   . GLY A 62  ? 0.6273 0.8184 0.6262 0.0647  0.0227  -0.0310 599  GLY A O   
273  N N   . ILE A 63  ? 0.5944 0.7919 0.6142 0.0598  0.0191  -0.0261 600  ILE A N   
274  C CA  . ILE A 63  ? 0.5605 0.7473 0.5757 0.0528  0.0156  -0.0217 600  ILE A CA  
275  C C   . ILE A 63  ? 0.5531 0.7450 0.5627 0.0465  0.0205  -0.0183 600  ILE A C   
276  O O   . ILE A 63  ? 0.5554 0.7619 0.5696 0.0450  0.0270  -0.0179 600  ILE A O   
277  C CB  . ILE A 63  ? 0.5330 0.7181 0.5588 0.0490  0.0113  -0.0187 600  ILE A CB  
278  C CG1 . ILE A 63  ? 0.5154 0.7152 0.5527 0.0465  0.0151  -0.0160 600  ILE A CG1 
279  C CG2 . ILE A 63  ? 0.5324 0.7086 0.5596 0.0534  0.0064  -0.0218 600  ILE A CG2 
280  C CD1 . ILE A 63  ? 0.5025 0.7009 0.5498 0.0458  0.0113  -0.0147 600  ILE A CD1 
281  N N   . PRO A 64  ? 0.5500 0.7298 0.5490 0.0425  0.0171  -0.0162 601  PRO A N   
282  C CA  . PRO A 64  ? 0.5500 0.7301 0.5388 0.0362  0.0209  -0.0129 601  PRO A CA  
283  C C   . PRO A 64  ? 0.5244 0.7125 0.5217 0.0292  0.0222  -0.0079 601  PRO A C   
284  O O   . PRO A 64  ? 0.5179 0.7062 0.5264 0.0284  0.0177  -0.0063 601  PRO A O   
285  C CB  . PRO A 64  ? 0.5609 0.7223 0.5362 0.0353  0.0139  -0.0128 601  PRO A CB  
286  C CG  . PRO A 64  ? 0.5475 0.7036 0.5325 0.0382  0.0067  -0.0148 601  PRO A CG  
287  C CD  . PRO A 64  ? 0.5414 0.7057 0.5358 0.0438  0.0094  -0.0177 601  PRO A CD  
288  N N   . ILE A 65  ? 0.5032 0.6977 0.4940 0.0235  0.0287  -0.0057 602  ILE A N   
289  C CA  . ILE A 65  ? 0.4613 0.6625 0.4575 0.0157  0.0302  -0.0007 602  ILE A CA  
290  C C   . ILE A 65  ? 0.4431 0.6271 0.4250 0.0098  0.0242  0.0034  602  ILE A C   
291  O O   . ILE A 65  ? 0.4545 0.6268 0.4174 0.0078  0.0245  0.0034  602  ILE A O   
292  C CB  . ILE A 65  ? 0.4609 0.6785 0.4576 0.0113  0.0405  -0.0009 602  ILE A CB  
293  C CG1 . ILE A 65  ? 0.4446 0.6766 0.4500 0.0193  0.0460  -0.0075 602  ILE A CG1 
294  C CG2 . ILE A 65  ? 0.4509 0.6795 0.4599 0.0050  0.0417  0.0032  602  ILE A CG2 
295  C CD1 . ILE A 65  ? 0.4178 0.6622 0.4441 0.0246  0.0443  -0.0094 602  ILE A CD1 
296  N N   . ILE A 66  ? 0.4113 0.5926 0.4009 0.0075  0.0181  0.0064  603  ILE A N   
297  C CA  . ILE A 66  ? 0.3957 0.5601 0.3731 0.0037  0.0102  0.0090  603  ILE A CA  
298  C C   . ILE A 66  ? 0.4030 0.5657 0.3688 -0.0056 0.0133  0.0142  603  ILE A C   
299  O O   . ILE A 66  ? 0.3875 0.5629 0.3636 -0.0101 0.0175  0.0170  603  ILE A O   
300  C CB  . ILE A 66  ? 0.3620 0.5251 0.3528 0.0055  0.0024  0.0090  603  ILE A CB  
301  C CG1 . ILE A 66  ? 0.3318 0.4952 0.3318 0.0128  -0.0002 0.0039  603  ILE A CG1 
302  C CG2 . ILE A 66  ? 0.3669 0.5138 0.3459 0.0026  -0.0067 0.0105  603  ILE A CG2 
303  C CD1 . ILE A 66  ? 0.3022 0.4675 0.3164 0.0134  -0.0054 0.0033  603  ILE A CD1 
304  N N   . LYS A 67  ? 0.4303 0.5756 0.3733 -0.0090 0.0106  0.0153  604  LYS A N   
305  C CA  . LYS A 67  ? 0.4498 0.5882 0.3766 -0.0193 0.0126  0.0204  604  LYS A CA  
306  C C   . LYS A 67  ? 0.4670 0.5914 0.3896 -0.0220 0.0016  0.0237  604  LYS A C   
307  O O   . LYS A 67  ? 0.4769 0.6017 0.3964 -0.0301 0.0027  0.0285  604  LYS A O   
308  C CB  . LYS A 67  ? 0.4747 0.5983 0.3748 -0.0225 0.0150  0.0201  604  LYS A CB  
309  C CG  . LYS A 67  ? 0.5037 0.6172 0.3822 -0.0347 0.0178  0.0254  604  LYS A CG  
310  C CD  . LYS A 67  ? 0.5434 0.6422 0.3945 -0.0376 0.0214  0.0245  604  LYS A CD  
311  C CE  . LYS A 67  ? 0.5871 0.6720 0.4116 -0.0515 0.0245  0.0299  604  LYS A CE  
312  N NZ  . LYS A 67  ? 0.6206 0.6918 0.4172 -0.0550 0.0297  0.0287  604  LYS A NZ  
313  N N   . GLY A 68  ? 0.4600 0.5727 0.3833 -0.0152 -0.0091 0.0205  605  GLY A N   
314  C CA  . GLY A 68  ? 0.4474 0.5492 0.3699 -0.0157 -0.0201 0.0218  605  GLY A CA  
315  C C   . GLY A 68  ? 0.4455 0.5377 0.3703 -0.0073 -0.0309 0.0159  605  GLY A C   
316  O O   . GLY A 68  ? 0.4589 0.5526 0.3861 -0.0016 -0.0296 0.0113  605  GLY A O   
317  N N   . GLY A 69  ? 0.4227 0.5056 0.3473 -0.0064 -0.0418 0.0153  606  GLY A N   
318  C CA  . GLY A 69  ? 0.4029 0.4775 0.3301 0.0012  -0.0529 0.0084  606  GLY A CA  
319  C C   . GLY A 69  ? 0.3790 0.4514 0.3136 0.0025  -0.0630 0.0070  606  GLY A C   
320  O O   . GLY A 69  ? 0.3797 0.4523 0.3128 -0.0027 -0.0625 0.0122  606  GLY A O   
321  N N   . THR A 70  ? 0.3719 0.4421 0.3143 0.0096  -0.0723 -0.0008 607  THR A N   
322  C CA  . THR A 70  ? 0.3623 0.4352 0.3166 0.0123  -0.0809 -0.0043 607  THR A CA  
323  C C   . THR A 70  ? 0.3360 0.4313 0.3152 0.0113  -0.0724 -0.0035 607  THR A C   
324  O O   . THR A 70  ? 0.3183 0.4263 0.3076 0.0109  -0.0623 -0.0028 607  THR A O   
325  C CB  . THR A 70  ? 0.3679 0.4350 0.3254 0.0201  -0.0930 -0.0145 607  THR A CB  
326  O OG1 . THR A 70  ? 0.3596 0.4418 0.3353 0.0231  -0.0873 -0.0198 607  THR A OG1 
327  C CG2 . THR A 70  ? 0.3896 0.4323 0.3208 0.0220  -0.1021 -0.0158 607  THR A CG2 
328  N N   . VAL A 71  ? 0.2834 0.3821 0.2710 0.0111  -0.0770 -0.0037 608  VAL A N   
329  C CA  . VAL A 71  ? 0.2609 0.3783 0.2696 0.0100  -0.0696 -0.0028 608  VAL A CA  
330  C C   . VAL A 71  ? 0.2474 0.3760 0.2730 0.0142  -0.0681 -0.0107 608  VAL A C   
331  O O   . VAL A 71  ? 0.2321 0.3740 0.2714 0.0127  -0.0594 -0.0097 608  VAL A O   
332  C CB  . VAL A 71  ? 0.3300 0.4474 0.3426 0.0091  -0.0752 -0.0015 608  VAL A CB  
333  C CG1 . VAL A 71  ? 0.3174 0.4317 0.3350 0.0153  -0.0872 -0.0109 608  VAL A CG1 
334  C CG2 . VAL A 71  ? 0.2380 0.3719 0.2678 0.0064  -0.0662 0.0017  608  VAL A CG2 
335  N N   . VAL A 72  ? 0.2829 0.4054 0.3069 0.0191  -0.0768 -0.0188 609  VAL A N   
336  C CA  . VAL A 72  ? 0.2714 0.4041 0.3103 0.0217  -0.0751 -0.0267 609  VAL A CA  
337  C C   . VAL A 72  ? 0.2629 0.3976 0.2993 0.0204  -0.0658 -0.0239 609  VAL A C   
338  O O   . VAL A 72  ? 0.2576 0.4034 0.3067 0.0193  -0.0589 -0.0253 609  VAL A O   
339  C CB  . VAL A 72  ? 0.3023 0.4281 0.3398 0.0275  -0.0874 -0.0368 609  VAL A CB  
340  C CG1 . VAL A 72  ? 0.3029 0.4383 0.3535 0.0290  -0.0850 -0.0447 609  VAL A CG1 
341  C CG2 . VAL A 72  ? 0.3016 0.4295 0.3462 0.0300  -0.0966 -0.0420 609  VAL A CG2 
342  N N   . LYS A 73  ? 0.2586 0.3812 0.2769 0.0204  -0.0658 -0.0200 610  LYS A N   
343  C CA  . LYS A 73  ? 0.2637 0.3879 0.2787 0.0201  -0.0575 -0.0181 610  LYS A CA  
344  C C   . LYS A 73  ? 0.2485 0.3837 0.2696 0.0164  -0.0464 -0.0114 610  LYS A C   
345  O O   . LYS A 73  ? 0.2425 0.3841 0.2691 0.0171  -0.0397 -0.0119 610  LYS A O   
346  C CB  . LYS A 73  ? 0.3133 0.4216 0.3062 0.0209  -0.0601 -0.0163 610  LYS A CB  
347  C CG  . LYS A 73  ? 0.3075 0.4051 0.2948 0.0261  -0.0697 -0.0242 610  LYS A CG  
348  C CD  . LYS A 73  ? 0.2832 0.3887 0.2811 0.0283  -0.0656 -0.0290 610  LYS A CD  
349  C CE  . LYS A 73  ? 0.3160 0.4143 0.3136 0.0332  -0.0759 -0.0382 610  LYS A CE  
350  N NZ  . LYS A 73  ? 0.2833 0.3893 0.2919 0.0342  -0.0722 -0.0430 610  LYS A NZ  
351  N N   . LEU A 74  ? 0.2525 0.3893 0.2726 0.0128  -0.0452 -0.0056 611  LEU A N   
352  C CA  . LEU A 74  ? 0.2520 0.4004 0.2801 0.0098  -0.0358 -0.0003 611  LEU A CA  
353  C C   . LEU A 74  ? 0.2330 0.3920 0.2788 0.0107  -0.0338 -0.0032 611  LEU A C   
354  O O   . LEU A 74  ? 0.2302 0.3964 0.2820 0.0106  -0.0268 -0.0019 611  LEU A O   
355  C CB  . LEU A 74  ? 0.2393 0.3865 0.2624 0.0052  -0.0359 0.0061  611  LEU A CB  
356  C CG  . LEU A 74  ? 0.2947 0.4302 0.2973 0.0019  -0.0365 0.0100  611  LEU A CG  
357  C CD1 . LEU A 74  ? 0.2632 0.3959 0.2607 -0.0037 -0.0382 0.0158  611  LEU A CD1 
358  C CD2 . LEU A 74  ? 0.2628 0.4035 0.2610 0.0009  -0.0267 0.0118  611  LEU A CD2 
359  N N   . ILE A 75  ? 0.2282 0.3875 0.2813 0.0114  -0.0401 -0.0078 612  ILE A N   
360  C CA  . ILE A 75  ? 0.2272 0.3955 0.2952 0.0110  -0.0378 -0.0114 612  ILE A CA  
361  C C   . ILE A 75  ? 0.2444 0.4133 0.3146 0.0123  -0.0349 -0.0159 612  ILE A C   
362  O O   . ILE A 75  ? 0.2354 0.4092 0.3122 0.0109  -0.0295 -0.0158 612  ILE A O   
363  C CB  . ILE A 75  ? 0.2281 0.3978 0.3033 0.0114  -0.0450 -0.0168 612  ILE A CB  
364  C CG1 . ILE A 75  ? 0.2245 0.3936 0.2983 0.0099  -0.0475 -0.0118 612  ILE A CG1 
365  C CG2 . ILE A 75  ? 0.1883 0.3669 0.2773 0.0100  -0.0422 -0.0225 612  ILE A CG2 
366  C CD1 . ILE A 75  ? 0.1877 0.3639 0.2679 0.0068  -0.0403 -0.0060 612  ILE A CD1 
367  N N   . GLU A 76  ? 0.2698 0.4320 0.3329 0.0150  -0.0391 -0.0200 613  GLU A N   
368  C CA  . GLU A 76  ? 0.2771 0.4385 0.3411 0.0162  -0.0372 -0.0244 613  GLU A CA  
369  C C   . GLU A 76  ? 0.2699 0.4314 0.3291 0.0166  -0.0296 -0.0195 613  GLU A C   
370  O O   . GLU A 76  ? 0.2642 0.4280 0.3282 0.0158  -0.0258 -0.0207 613  GLU A O   
371  C CB  . GLU A 76  ? 0.3033 0.4562 0.3593 0.0196  -0.0441 -0.0294 613  GLU A CB  
372  C CG  . GLU A 76  ? 0.3179 0.4706 0.3776 0.0204  -0.0444 -0.0360 613  GLU A CG  
373  C CD  . GLU A 76  ? 0.3528 0.4948 0.4003 0.0244  -0.0491 -0.0385 613  GLU A CD  
374  O OE1 . GLU A 76  ? 0.3647 0.4989 0.4028 0.0267  -0.0554 -0.0383 613  GLU A OE1 
375  O OE2 . GLU A 76  ? 0.3656 0.5052 0.4113 0.0253  -0.0471 -0.0408 613  GLU A OE2 
376  N N   . ARG A 77  ? 0.2771 0.4357 0.3260 0.0175  -0.0276 -0.0145 614  ARG A N   
377  C CA  . ARG A 77  ? 0.2664 0.4275 0.3122 0.0187  -0.0205 -0.0112 614  ARG A CA  
378  C C   . ARG A 77  ? 0.2499 0.4194 0.3052 0.0170  -0.0159 -0.0078 614  ARG A C   
379  O O   . ARG A 77  ? 0.2269 0.3988 0.2831 0.0189  -0.0115 -0.0074 614  ARG A O   
380  C CB  . ARG A 77  ? 0.2827 0.4407 0.3158 0.0190  -0.0186 -0.0076 614  ARG A CB  
381  C CG  . ARG A 77  ? 0.2996 0.4465 0.3198 0.0214  -0.0229 -0.0108 614  ARG A CG  
382  C CD  . ARG A 77  ? 0.3087 0.4543 0.3253 0.0252  -0.0195 -0.0134 614  ARG A CD  
383  N NE  . ARG A 77  ? 0.3262 0.4603 0.3317 0.0279  -0.0247 -0.0174 614  ARG A NE  
384  C CZ  . ARG A 77  ? 0.3308 0.4602 0.3276 0.0314  -0.0227 -0.0192 614  ARG A CZ  
385  N NH1 . ARG A 77  ? 0.3550 0.4728 0.3414 0.0339  -0.0285 -0.0230 614  ARG A NH1 
386  N NH2 . ARG A 77  ? 0.3117 0.4477 0.3100 0.0332  -0.0156 -0.0179 614  ARG A NH2 
387  N N   . LEU A 78  ? 0.2478 0.4208 0.3095 0.0140  -0.0178 -0.0058 615  LEU A N   
388  C CA  . LEU A 78  ? 0.2396 0.4188 0.3100 0.0123  -0.0146 -0.0031 615  LEU A CA  
389  C C   . LEU A 78  ? 0.2500 0.4279 0.3254 0.0122  -0.0139 -0.0069 615  LEU A C   
390  O O   . LEU A 78  ? 0.1892 0.3685 0.2675 0.0122  -0.0109 -0.0052 615  LEU A O   
391  C CB  . LEU A 78  ? 0.2342 0.4157 0.3092 0.0093  -0.0177 -0.0008 615  LEU A CB  
392  C CG  . LEU A 78  ? 0.2400 0.4269 0.3229 0.0075  -0.0153 0.0025  615  LEU A CG  
393  C CD1 . LEU A 78  ? 0.2393 0.4313 0.3213 0.0082  -0.0107 0.0071  615  LEU A CD1 
394  C CD2 . LEU A 78  ? 0.2337 0.4212 0.3198 0.0050  -0.0196 0.0037  615  LEU A CD2 
395  N N   . THR A 79  ? 0.2429 0.4171 0.3185 0.0116  -0.0171 -0.0124 616  THR A N   
396  C CA  . THR A 79  ? 0.2306 0.4028 0.3098 0.0093  -0.0163 -0.0165 616  THR A CA  
397  C C   . THR A 79  ? 0.2444 0.4108 0.3183 0.0110  -0.0177 -0.0212 616  THR A C   
398  O O   . THR A 79  ? 0.2463 0.4117 0.3236 0.0082  -0.0196 -0.0269 616  THR A O   
399  C CB  . THR A 79  ? 0.2282 0.4045 0.3160 0.0051  -0.0185 -0.0199 616  THR A CB  
400  O OG1 . THR A 79  ? 0.1880 0.3657 0.2770 0.0064  -0.0239 -0.0234 616  THR A OG1 
401  C CG2 . THR A 79  ? 0.1801 0.3604 0.2720 0.0035  -0.0170 -0.0151 616  THR A CG2 
402  N N   . TYR A 80  ? 0.2586 0.4219 0.3243 0.0154  -0.0166 -0.0193 617  TYR A N   
403  C CA  . TYR A 80  ? 0.2826 0.4392 0.3415 0.0179  -0.0184 -0.0233 617  TYR A CA  
404  C C   . TYR A 80  ? 0.3125 0.4637 0.3709 0.0162  -0.0175 -0.0263 617  TYR A C   
405  O O   . TYR A 80  ? 0.3140 0.4640 0.3722 0.0156  -0.0146 -0.0239 617  TYR A O   
406  C CB  . TYR A 80  ? 0.3084 0.4633 0.3578 0.0230  -0.0163 -0.0205 617  TYR A CB  
407  C CG  . TYR A 80  ? 0.3175 0.4654 0.3579 0.0260  -0.0194 -0.0238 617  TYR A CG  
408  C CD1 . TYR A 80  ? 0.3292 0.4746 0.3689 0.0252  -0.0249 -0.0265 617  TYR A CD1 
409  C CD2 . TYR A 80  ? 0.3298 0.4727 0.3615 0.0303  -0.0176 -0.0246 617  TYR A CD2 
410  C CE1 . TYR A 80  ? 0.3535 0.4908 0.3837 0.0283  -0.0287 -0.0297 617  TYR A CE1 
411  C CE2 . TYR A 80  ? 0.3568 0.4922 0.3790 0.0332  -0.0206 -0.0276 617  TYR A CE2 
412  C CZ  . TYR A 80  ? 0.3704 0.5024 0.3915 0.0321  -0.0262 -0.0299 617  TYR A CZ  
413  O OH  . TYR A 80  ? 0.3933 0.5160 0.4037 0.0354  -0.0301 -0.0330 617  TYR A OH  
414  N N   . HIS A 81  ? 0.3453 0.4919 0.4024 0.0151  -0.0206 -0.0319 618  HIS A N   
415  C CA  . HIS A 81  ? 0.3587 0.4986 0.4140 0.0115  -0.0202 -0.0352 618  HIS A CA  
416  C C   . HIS A 81  ? 0.3647 0.4949 0.4086 0.0163  -0.0198 -0.0343 618  HIS A C   
417  O O   . HIS A 81  ? 0.3721 0.4941 0.4114 0.0139  -0.0193 -0.0352 618  HIS A O   
418  C CB  . HIS A 81  ? 0.3879 0.5282 0.4479 0.0074  -0.0238 -0.0424 618  HIS A CB  
419  C CG  . HIS A 81  ? 0.4147 0.5503 0.4689 0.0123  -0.0280 -0.0454 618  HIS A CG  
420  N ND1 . HIS A 81  ? 0.4159 0.5543 0.4698 0.0166  -0.0314 -0.0453 618  HIS A ND1 
421  C CD2 . HIS A 81  ? 0.4293 0.5559 0.4763 0.0135  -0.0301 -0.0487 618  HIS A CD2 
422  C CE1 . HIS A 81  ? 0.4225 0.5535 0.4688 0.0203  -0.0352 -0.0483 618  HIS A CE1 
423  N NE2 . HIS A 81  ? 0.4325 0.5571 0.4754 0.0187  -0.0345 -0.0505 618  HIS A NE2 
424  N N   A MET A 82  ? 0.3676 0.4975 0.4054 0.0230  -0.0202 -0.0331 619  MET A N   
425  N N   B MET A 82  ? 0.3676 0.4974 0.4054 0.0229  -0.0202 -0.0331 619  MET A N   
426  C CA  A MET A 82  ? 0.3832 0.5045 0.4103 0.0285  -0.0202 -0.0337 619  MET A CA  
427  C CA  B MET A 82  ? 0.3883 0.5097 0.4154 0.0285  -0.0202 -0.0336 619  MET A CA  
428  C C   A MET A 82  ? 0.3813 0.5029 0.4062 0.0321  -0.0172 -0.0304 619  MET A C   
429  C C   B MET A 82  ? 0.3811 0.5024 0.4063 0.0315  -0.0173 -0.0304 619  MET A C   
430  O O   A MET A 82  ? 0.4017 0.5140 0.4184 0.0356  -0.0184 -0.0320 619  MET A O   
431  O O   B MET A 82  ? 0.4010 0.5124 0.4186 0.0338  -0.0186 -0.0320 619  MET A O   
432  C CB  A MET A 82  ? 0.3866 0.5075 0.4069 0.0341  -0.0212 -0.0342 619  MET A CB  
433  C CB  B MET A 82  ? 0.3860 0.5077 0.4064 0.0343  -0.0207 -0.0337 619  MET A CB  
434  C CG  A MET A 82  ? 0.4040 0.5177 0.4207 0.0335  -0.0262 -0.0393 619  MET A CG  
435  C CG  B MET A 82  ? 0.3996 0.5168 0.4182 0.0333  -0.0256 -0.0381 619  MET A CG  
436  S SD  A MET A 82  ? 0.4144 0.5238 0.4192 0.0402  -0.0278 -0.0398 619  MET A SD  
437  S SD  B MET A 82  ? 0.4118 0.5167 0.4251 0.0322  -0.0295 -0.0437 619  MET A SD  
438  C CE  A MET A 82  ? 0.4352 0.5335 0.4361 0.0397  -0.0348 -0.0467 619  MET A CE  
439  C CE  B MET A 82  ? 0.4032 0.5003 0.4023 0.0411  -0.0279 -0.0424 619  MET A CE  
440  N N   . TYR A 83  ? 0.3694 0.5008 0.4012 0.0317  -0.0142 -0.0264 620  TYR A N   
441  C CA  . TYR A 83  ? 0.3610 0.4944 0.3927 0.0356  -0.0121 -0.0241 620  TYR A CA  
442  C C   . TYR A 83  ? 0.3535 0.4970 0.3950 0.0324  -0.0098 -0.0200 620  TYR A C   
443  O O   . TYR A 83  ? 0.3380 0.4875 0.3849 0.0284  -0.0096 -0.0187 620  TYR A O   
444  C CB  . TYR A 83  ? 0.3568 0.4938 0.3834 0.0436  -0.0102 -0.0247 620  TYR A CB  
445  C CG  . TYR A 83  ? 0.3437 0.4884 0.3705 0.0433  -0.0080 -0.0234 620  TYR A CG  
446  C CD1 . TYR A 83  ? 0.3281 0.4838 0.3618 0.0405  -0.0050 -0.0194 620  TYR A CD1 
447  C CD2 . TYR A 83  ? 0.3457 0.4846 0.3639 0.0453  -0.0095 -0.0260 620  TYR A CD2 
448  C CE1 . TYR A 83  ? 0.3208 0.4801 0.3512 0.0392  -0.0037 -0.0179 620  TYR A CE1 
449  C CE2 . TYR A 83  ? 0.3482 0.4906 0.3632 0.0447  -0.0083 -0.0246 620  TYR A CE2 
450  C CZ  . TYR A 83  ? 0.3333 0.4852 0.3536 0.0413  -0.0054 -0.0205 620  TYR A CZ  
451  O OH  . TYR A 83  ? 0.3335 0.4856 0.3473 0.0398  -0.0048 -0.0189 620  TYR A OH  
452  N N   . ALA A 84  ? 0.3579 0.5024 0.4009 0.0348  -0.0090 -0.0185 621  ALA A N   
453  C CA  . ALA A 84  ? 0.3464 0.5008 0.3982 0.0331  -0.0070 -0.0146 621  ALA A CA  
454  C C   . ALA A 84  ? 0.3425 0.5096 0.3974 0.0369  -0.0036 -0.0131 621  ALA A C   
455  O O   . ALA A 84  ? 0.3511 0.5193 0.4010 0.0422  -0.0023 -0.0155 621  ALA A O   
456  C CB  . ALA A 84  ? 0.3509 0.4998 0.4026 0.0341  -0.0086 -0.0142 621  ALA A CB  
457  N N   . ASP A 85  ? 0.3288 0.5053 0.3914 0.0337  -0.0019 -0.0093 622  ASP A N   
458  C CA  . ASP A 85  ? 0.3002 0.4890 0.3654 0.0345  0.0020  -0.0074 622  ASP A CA  
459  C C   . ASP A 85  ? 0.2798 0.4772 0.3545 0.0325  0.0029  -0.0041 622  ASP A C   
460  O O   . ASP A 85  ? 0.2653 0.4663 0.3434 0.0273  0.0029  -0.0004 622  ASP A O   
461  C CB  . ASP A 85  ? 0.2909 0.4792 0.3517 0.0305  0.0022  -0.0060 622  ASP A CB  
462  C CG  . ASP A 85  ? 0.3030 0.5002 0.3611 0.0305  0.0067  -0.0045 622  ASP A CG  
463  O OD1 . ASP A 85  ? 0.3118 0.5197 0.3754 0.0325  0.0104  -0.0045 622  ASP A OD1 
464  O OD2 . ASP A 85  ? 0.3216 0.5149 0.3715 0.0282  0.0065  -0.0039 622  ASP A OD2 
465  N N   . PRO A 86  ? 0.3402 0.3360 0.3841 0.1095  0.0422  0.0068  623  PRO A N   
466  C CA  . PRO A 86  ? 0.3172 0.3339 0.3814 0.1066  0.0342  0.0112  623  PRO A CA  
467  C C   . PRO A 86  ? 0.2951 0.3388 0.3802 0.1012  0.0411  0.0114  623  PRO A C   
468  O O   . PRO A 86  ? 0.2778 0.3338 0.3724 0.0922  0.0347  0.0141  623  PRO A O   
469  C CB  . PRO A 86  ? 0.3327 0.3511 0.4086 0.1208  0.0277  0.0127  623  PRO A CB  
470  C CG  . PRO A 86  ? 0.3380 0.3428 0.4068 0.1329  0.0373  0.0074  623  PRO A CG  
471  C CD  . PRO A 86  ? 0.3562 0.3390 0.3975 0.1238  0.0424  0.0045  623  PRO A CD  
472  N N   . ASN A 87  ? 0.3003 0.3526 0.3911 0.1053  0.0543  0.0084  624  ASN A N   
473  C CA  . ASN A 87  ? 0.3029 0.3802 0.4122 0.0976  0.0620  0.0095  624  ASN A CA  
474  C C   . ASN A 87  ? 0.2874 0.3545 0.3809 0.0827  0.0632  0.0113  624  ASN A C   
475  O O   . ASN A 87  ? 0.2808 0.3615 0.3863 0.0722  0.0622  0.0139  624  ASN A O   
476  C CB  . ASN A 87  ? 0.3254 0.4159 0.4441 0.1056  0.0777  0.0056  624  ASN A CB  
477  C CG  . ASN A 87  ? 0.3440 0.4476 0.4840 0.1227  0.0765  0.0029  624  ASN A CG  
478  O OD1 . ASN A 87  ? 0.3220 0.4387 0.4812 0.1257  0.0643  0.0060  624  ASN A OD1 
479  N ND2 . ASN A 87  ? 0.3760 0.4747 0.5115 0.1346  0.0882  -0.0031 624  ASN A ND2 
480  N N   . PHE A 88  ? 0.2758 0.3181 0.3429 0.0818  0.0640  0.0099  625  PHE A N   
481  C CA  . PHE A 88  ? 0.2720 0.3039 0.3256 0.0702  0.0634  0.0117  625  PHE A CA  
482  C C   . PHE A 88  ? 0.2515 0.2805 0.3066 0.0635  0.0516  0.0130  625  PHE A C   
483  O O   . PHE A 88  ? 0.2468 0.2762 0.3029 0.0539  0.0504  0.0146  625  PHE A O   
484  C CB  . PHE A 88  ? 0.2723 0.2819 0.2999 0.0717  0.0660  0.0096  625  PHE A CB  
485  C CG  . PHE A 88  ? 0.2987 0.2976 0.3135 0.0625  0.0642  0.0118  625  PHE A CG  
486  C CD1 . PHE A 88  ? 0.3086 0.3139 0.3276 0.0547  0.0693  0.0157  625  PHE A CD1 
487  C CD2 . PHE A 88  ? 0.2976 0.2801 0.2972 0.0617  0.0570  0.0102  625  PHE A CD2 
488  C CE1 . PHE A 88  ? 0.3109 0.3025 0.3174 0.0479  0.0661  0.0184  625  PHE A CE1 
489  C CE2 . PHE A 88  ? 0.2994 0.2732 0.2902 0.0557  0.0542  0.0120  625  PHE A CE2 
490  C CZ  . PHE A 88  ? 0.3014 0.2779 0.2949 0.0497  0.0582  0.0163  625  PHE A CZ  
491  N N   . VAL A 89  ? 0.2335 0.2574 0.2866 0.0682  0.0430  0.0121  626  VAL A N   
492  C CA  . VAL A 89  ? 0.2244 0.2460 0.2761 0.0616  0.0329  0.0124  626  VAL A CA  
493  C C   . VAL A 89  ? 0.2334 0.2745 0.3049 0.0558  0.0293  0.0142  626  VAL A C   
494  O O   . VAL A 89  ? 0.2268 0.2665 0.2971 0.0461  0.0258  0.0135  626  VAL A O   
495  C CB  . VAL A 89  ? 0.2325 0.2439 0.2752 0.0668  0.0254  0.0124  626  VAL A CB  
496  C CG1 . VAL A 89  ? 0.2273 0.2398 0.2684 0.0596  0.0157  0.0129  626  VAL A CG1 
497  C CG2 . VAL A 89  ? 0.2369 0.2281 0.2592 0.0681  0.0278  0.0100  626  VAL A CG2 
498  N N   . ARG A 90  ? 0.2617 0.3216 0.3525 0.0617  0.0295  0.0157  627  ARG A N   
499  C CA  . ARG A 90  ? 0.2697 0.3519 0.3822 0.0552  0.0247  0.0171  627  ARG A CA  
500  C C   . ARG A 90  ? 0.2666 0.3542 0.3843 0.0436  0.0322  0.0174  627  ARG A C   
501  O O   . ARG A 90  ? 0.2182 0.3064 0.3377 0.0323  0.0267  0.0171  627  ARG A O   
502  C CB  . ARG A 90  ? 0.2774 0.3828 0.4141 0.0654  0.0241  0.0184  627  ARG A CB  
503  C CG  . ARG A 90  ? 0.2777 0.4097 0.4395 0.0593  0.0155  0.0200  627  ARG A CG  
504  C CD  . ARG A 90  ? 0.2844 0.4477 0.4778 0.0663  0.0219  0.0202  627  ARG A CD  
505  N NE  . ARG A 90  ? 0.3172 0.4769 0.5111 0.0845  0.0260  0.0191  627  ARG A NE  
506  C CZ  . ARG A 90  ? 0.3388 0.4983 0.5322 0.0909  0.0417  0.0163  627  ARG A CZ  
507  N NH1 . ARG A 90  ? 0.3540 0.5069 0.5462 0.1078  0.0444  0.0140  627  ARG A NH1 
508  N NH2 . ARG A 90  ? 0.3308 0.4945 0.5225 0.0799  0.0545  0.0158  627  ARG A NH2 
509  N N   . THR A 91  ? 0.2503 0.3388 0.3673 0.0456  0.0449  0.0179  628  THR A N   
510  C CA  . THR A 91  ? 0.2487 0.3397 0.3678 0.0338  0.0526  0.0199  628  THR A CA  
511  C C   . THR A 91  ? 0.2628 0.3286 0.3612 0.0258  0.0488  0.0199  628  THR A C   
512  O O   . THR A 91  ? 0.2574 0.3222 0.3592 0.0139  0.0476  0.0210  628  THR A O   
513  C CB  . THR A 91  ? 0.2519 0.3459 0.3682 0.0377  0.0674  0.0207  628  THR A CB  
514  O OG1 . THR A 91  ? 0.2671 0.3843 0.4039 0.0481  0.0715  0.0190  628  THR A OG1 
515  C CG2 . THR A 91  ? 0.2620 0.3602 0.3808 0.0238  0.0760  0.0244  628  THR A CG2 
516  N N   . PHE A 92  ? 0.2682 0.3136 0.3462 0.0323  0.0469  0.0181  629  PHE A N   
517  C CA  . PHE A 92  ? 0.2744 0.2990 0.3366 0.0274  0.0427  0.0170  629  PHE A CA  
518  C C   . PHE A 92  ? 0.2724 0.2981 0.3402 0.0203  0.0335  0.0143  629  PHE A C   
519  O O   . PHE A 92  ? 0.2659 0.2829 0.3320 0.0116  0.0323  0.0140  629  PHE A O   
520  C CB  . PHE A 92  ? 0.2834 0.2928 0.3283 0.0355  0.0409  0.0145  629  PHE A CB  
521  C CG  . PHE A 92  ? 0.2981 0.2899 0.3304 0.0328  0.0372  0.0127  629  PHE A CG  
522  C CD1 . PHE A 92  ? 0.2914 0.2797 0.3228 0.0309  0.0302  0.0082  629  PHE A CD1 
523  C CD2 . PHE A 92  ? 0.3110 0.2901 0.3320 0.0328  0.0406  0.0151  629  PHE A CD2 
524  C CE1 . PHE A 92  ? 0.2878 0.2624 0.3110 0.0303  0.0278  0.0051  629  PHE A CE1 
525  C CE2 . PHE A 92  ? 0.3083 0.2727 0.3210 0.0327  0.0359  0.0133  629  PHE A CE2 
526  C CZ  . PHE A 92  ? 0.2973 0.2606 0.3130 0.0321  0.0300  0.0078  629  PHE A CZ  
527  N N   . LEU A 93  ? 0.2219 0.2561 0.2944 0.0237  0.0265  0.0123  630  LEU A N   
528  C CA  . LEU A 93  ? 0.2238 0.2569 0.2958 0.0168  0.0174  0.0089  630  LEU A CA  
529  C C   . LEU A 93  ? 0.2938 0.3407 0.3822 0.0061  0.0148  0.0096  630  LEU A C   
530  O O   . LEU A 93  ? 0.2927 0.3340 0.3776 -0.0023 0.0082  0.0057  630  LEU A O   
531  C CB  . LEU A 93  ? 0.2682 0.3044 0.3362 0.0225  0.0101  0.0080  630  LEU A CB  
532  C CG  . LEU A 93  ? 0.2790 0.2974 0.3277 0.0275  0.0118  0.0056  630  LEU A CG  
533  C CD1 . LEU A 93  ? 0.2882 0.3051 0.3286 0.0319  0.0061  0.0060  630  LEU A CD1 
534  C CD2 . LEU A 93  ? 0.2240 0.2293 0.2630 0.0213  0.0115  0.0003  630  LEU A CD2 
535  N N   . THR A 94  ? 0.2846 0.3499 0.3906 0.0053  0.0204  0.0136  631  THR A N   
536  C CA  . THR A 94  ? 0.2940 0.3740 0.4174 -0.0074 0.0193  0.0145  631  THR A CA  
537  C C   . THR A 94  ? 0.3026 0.3656 0.4181 -0.0178 0.0258  0.0158  631  THR A C   
538  O O   . THR A 94  ? 0.3467 0.4076 0.4665 -0.0311 0.0219  0.0145  631  THR A O   
539  C CB  . THR A 94  ? 0.3050 0.4160 0.4540 -0.0042 0.0237  0.0179  631  THR A CB  
540  O OG1 . THR A 94  ? 0.3172 0.4434 0.4760 0.0034  0.0132  0.0171  631  THR A OG1 
541  C CG2 . THR A 94  ? 0.2966 0.4252 0.4654 -0.0194 0.0266  0.0196  631  THR A CG2 
542  N N   . THR A 95  ? 0.2924 0.3401 0.3940 -0.0123 0.0343  0.0185  632  THR A N   
543  C CA  . THR A 95  ? 0.3091 0.3412 0.4027 -0.0212 0.0408  0.0223  632  THR A CA  
544  C C   . THR A 95  ? 0.3269 0.3271 0.3983 -0.0186 0.0378  0.0208  632  THR A C   
545  O O   . THR A 95  ? 0.3414 0.3235 0.4043 -0.0260 0.0405  0.0245  632  THR A O   
546  C CB  . THR A 95  ? 0.3385 0.3792 0.4329 -0.0184 0.0534  0.0279  632  THR A CB  
547  O OG1 . THR A 95  ? 0.2567 0.2896 0.3372 -0.0041 0.0549  0.0268  632  THR A OG1 
548  C CG2 . THR A 95  ? 0.2585 0.3342 0.3796 -0.0204 0.0581  0.0286  632  THR A CG2 
549  N N   . TYR A 96  ? 0.3139 0.3068 0.3762 -0.0085 0.0325  0.0158  633  TYR A N   
550  C CA  . TYR A 96  ? 0.3265 0.2950 0.3716 -0.0029 0.0311  0.0144  633  TYR A CA  
551  C C   . TYR A 96  ? 0.3422 0.2896 0.3824 -0.0105 0.0272  0.0122  633  TYR A C   
552  O O   . TYR A 96  ? 0.3637 0.2895 0.3922 -0.0076 0.0273  0.0143  633  TYR A O   
553  C CB  . TYR A 96  ? 0.3203 0.2895 0.3600 0.0071  0.0269  0.0085  633  TYR A CB  
554  C CG  . TYR A 96  ? 0.2536 0.2217 0.2941 0.0039  0.0201  0.0009  633  TYR A CG  
555  C CD1 . TYR A 96  ? 0.3429 0.2925 0.3755 0.0039  0.0174  -0.0050 633  TYR A CD1 
556  C CD2 . TYR A 96  ? 0.2880 0.2729 0.3359 0.0016  0.0162  -0.0008 633  TYR A CD2 
557  C CE1 . TYR A 96  ? 0.3616 0.3099 0.3922 0.0006  0.0128  -0.0134 633  TYR A CE1 
558  C CE2 . TYR A 96  ? 0.2512 0.2340 0.2952 -0.0024 0.0099  -0.0077 633  TYR A CE2 
559  C CZ  . TYR A 96  ? 0.2617 0.2263 0.2963 -0.0034 0.0091  -0.0145 633  TYR A CZ  
560  O OH  . TYR A 96  ? 0.2695 0.2317 0.2977 -0.0078 0.0043  -0.0227 633  TYR A OH  
561  N N   . ARG A 97  ? 0.3300 0.2816 0.3782 -0.0199 0.0227  0.0080  634  ARG A N   
562  C CA  . ARG A 97  ? 0.3449 0.2733 0.3872 -0.0272 0.0185  0.0039  634  ARG A CA  
563  C C   . ARG A 97  ? 0.3693 0.2785 0.4061 -0.0347 0.0222  0.0116  634  ARG A C   
564  O O   . ARG A 97  ? 0.4142 0.2961 0.4423 -0.0377 0.0187  0.0092  634  ARG A O   
565  C CB  . ARG A 97  ? 0.3404 0.2791 0.3914 -0.0383 0.0128  -0.0020 634  ARG A CB  
566  C CG  . ARG A 97  ? 0.3229 0.2767 0.3742 -0.0316 0.0082  -0.0084 634  ARG A CG  
567  C CD  . ARG A 97  ? 0.3271 0.2977 0.3878 -0.0422 0.0014  -0.0115 634  ARG A CD  
568  N NE  . ARG A 97  ? 0.3076 0.2938 0.3671 -0.0355 -0.0031 -0.0141 634  ARG A NE  
569  C CZ  . ARG A 97  ? 0.2863 0.2940 0.3555 -0.0288 -0.0023 -0.0082 634  ARG A CZ  
570  N NH1 . ARG A 97  ? 0.2859 0.3047 0.3677 -0.0275 0.0043  -0.0008 634  ARG A NH1 
571  N NH2 . ARG A 97  ? 0.2621 0.2784 0.3268 -0.0234 -0.0077 -0.0099 634  ARG A NH2 
572  N N   . SER A 98  ? 0.3574 0.2780 0.3973 -0.0375 0.0296  0.0207  635  SER A N   
573  C CA  . SER A 98  ? 0.3860 0.2868 0.4162 -0.0455 0.0340  0.0296  635  SER A CA  
574  C C   . SER A 98  ? 0.4290 0.3065 0.4404 -0.0338 0.0333  0.0336  635  SER A C   
575  O O   . SER A 98  ? 0.4685 0.3240 0.4668 -0.0394 0.0353  0.0421  635  SER A O   
576  C CB  . SER A 98  ? 0.3816 0.3058 0.4213 -0.0543 0.0440  0.0372  635  SER A CB  
577  O OG  . SER A 98  ? 0.3329 0.2742 0.3722 -0.0421 0.0493  0.0385  635  SER A OG  
578  N N   . PHE A 99  ? 0.4185 0.3003 0.4277 -0.0188 0.0300  0.0282  636  PHE A N   
579  C CA  . PHE A 99  ? 0.4285 0.2917 0.4228 -0.0077 0.0274  0.0313  636  PHE A CA  
580  C C   . PHE A 99  ? 0.4072 0.2690 0.4033 0.0054  0.0208  0.0217  636  PHE A C   
581  O O   . PHE A 99  ? 0.4133 0.2661 0.4013 0.0159  0.0175  0.0232  636  PHE A O   
582  C CB  . PHE A 99  ? 0.4298 0.3044 0.4167 -0.0039 0.0337  0.0383  636  PHE A CB  
583  C CG  . PHE A 99  ? 0.4162 0.3196 0.4137 0.0016  0.0371  0.0332  636  PHE A CG  
584  C CD1 . PHE A 99  ? 0.3882 0.2963 0.3866 0.0129  0.0323  0.0263  636  PHE A CD1 
585  C CD2 . PHE A 99  ? 0.4091 0.3343 0.4160 -0.0043 0.0453  0.0356  636  PHE A CD2 
586  C CE1 . PHE A 99  ? 0.3704 0.2995 0.3755 0.0171  0.0348  0.0227  636  PHE A CE1 
587  C CE2 . PHE A 99  ? 0.3829 0.3305 0.3989 0.0025  0.0474  0.0314  636  PHE A CE2 
588  C CZ  . PHE A 99  ? 0.3707 0.3178 0.3841 0.0129  0.0417  0.0254  636  PHE A CZ  
589  N N   . CYS A 100 ? 0.3793 0.2507 0.3853 0.0046  0.0187  0.0119  637  CYS A N   
590  C CA  . CYS A 100 ? 0.3608 0.2361 0.3687 0.0155  0.0152  0.0024  637  CYS A CA  
591  C C   . CYS A 100 ? 0.3807 0.2595 0.3942 0.0105  0.0134  -0.0078 637  CYS A C   
592  O O   . CYS A 100 ? 0.4026 0.2944 0.4218 0.0008  0.0144  -0.0075 637  CYS A O   
593  C CB  . CYS A 100 ? 0.3331 0.2299 0.3424 0.0220  0.0178  0.0030  637  CYS A CB  
594  S SG  . CYS A 100 ? 0.3365 0.2412 0.3485 0.0319  0.0152  -0.0079 637  CYS A SG  
595  N N   . LYS A 101 ? 0.3916 0.2603 0.4039 0.0174  0.0106  -0.0174 638  LYS A N   
596  C CA  . LYS A 101 ? 0.3947 0.2636 0.4079 0.0123  0.0094  -0.0284 638  LYS A CA  
597  C C   . LYS A 101 ? 0.3493 0.2423 0.3642 0.0136  0.0110  -0.0333 638  LYS A C   
598  O O   . LYS A 101 ? 0.3313 0.2358 0.3471 0.0215  0.0129  -0.0315 638  LYS A O   
599  C CB  . LYS A 101 ? 0.4447 0.2921 0.4552 0.0197  0.0075  -0.0385 638  LYS A CB  
600  C CG  . LYS A 101 ? 0.4987 0.3153 0.5045 0.0150  0.0044  -0.0365 638  LYS A CG  
601  C CD  . LYS A 101 ? 0.5548 0.3498 0.5589 0.0245  0.0025  -0.0488 638  LYS A CD  
602  C CE  . LYS A 101 ? 0.6323 0.3901 0.6296 0.0210  -0.0017 -0.0459 638  LYS A CE  
603  N NZ  . LYS A 101 ? 0.6723 0.4061 0.6692 0.0341  -0.0039 -0.0580 638  LYS A NZ  
604  N N   . PRO A 102 ? 0.3411 0.2404 0.3547 0.0049  0.0093  -0.0390 639  PRO A N   
605  C CA  . PRO A 102 ? 0.3450 0.2628 0.3559 0.0055  0.0099  -0.0430 639  PRO A CA  
606  C C   . PRO A 102 ? 0.3754 0.2942 0.3831 0.0149  0.0134  -0.0507 639  PRO A C   
607  O O   . PRO A 102 ? 0.3768 0.3100 0.3840 0.0182  0.0154  -0.0483 639  PRO A O   
608  C CB  . PRO A 102 ? 0.3302 0.2469 0.3362 -0.0057 0.0058  -0.0497 639  PRO A CB  
609  C CG  . PRO A 102 ? 0.3194 0.2274 0.3311 -0.0145 0.0031  -0.0446 639  PRO A CG  
610  C CD  . PRO A 102 ? 0.3304 0.2208 0.3437 -0.0078 0.0059  -0.0403 639  PRO A CD  
611  N N   . GLN A 103 ? 0.4048 0.3087 0.4114 0.0192  0.0145  -0.0604 640  GLN A N   
612  C CA  . GLN A 103 ? 0.4212 0.3300 0.4298 0.0291  0.0188  -0.0685 640  GLN A CA  
613  C C   . GLN A 103 ? 0.4197 0.3336 0.4365 0.0385  0.0186  -0.0605 640  GLN A C   
614  O O   . GLN A 103 ? 0.4253 0.3540 0.4452 0.0431  0.0216  -0.0628 640  GLN A O   
615  C CB  . GLN A 103 ? 0.4559 0.3471 0.4644 0.0338  0.0199  -0.0813 640  GLN A CB  
616  C CG  . GLN A 103 ? 0.4781 0.3626 0.4750 0.0241  0.0202  -0.0918 640  GLN A CG  
617  C CD  . GLN A 103 ? 0.4847 0.3844 0.4743 0.0234  0.0265  -0.1025 640  GLN A CD  
618  O OE1 . GLN A 103 ? 0.4872 0.4015 0.4833 0.0308  0.0316  -0.1039 640  GLN A OE1 
619  N NE2 . GLN A 103 ? 0.4879 0.3844 0.4627 0.0130  0.0261  -0.1102 640  GLN A NE2 
620  N N   . GLU A 104 ? 0.4263 0.3274 0.4450 0.0399  0.0151  -0.0513 641  GLU A N   
621  C CA  . GLU A 104 ? 0.4202 0.3241 0.4424 0.0475  0.0136  -0.0430 641  GLU A CA  
622  C C   . GLU A 104 ? 0.3790 0.3016 0.3995 0.0445  0.0155  -0.0368 641  GLU A C   
623  O O   . GLU A 104 ? 0.3908 0.3223 0.4136 0.0503  0.0156  -0.0354 641  GLU A O   
624  C CB  . GLU A 104 ? 0.4588 0.3431 0.4779 0.0466  0.0100  -0.0332 641  GLU A CB  
625  C CG  . GLU A 104 ? 0.4864 0.3656 0.5054 0.0557  0.0065  -0.0260 641  GLU A CG  
626  C CD  . GLU A 104 ? 0.5251 0.3841 0.5357 0.0516  0.0040  -0.0144 641  GLU A CD  
627  O OE1 . GLU A 104 ? 0.5319 0.3941 0.5365 0.0515  0.0040  -0.0046 641  GLU A OE1 
628  O OE2 . GLU A 104 ? 0.5471 0.3859 0.5552 0.0473  0.0027  -0.0153 641  GLU A OE2 
629  N N   . LEU A 105 ? 0.3319 0.2604 0.3490 0.0357  0.0164  -0.0334 642  LEU A N   
630  C CA  . LEU A 105 ? 0.2988 0.2416 0.3141 0.0342  0.0177  -0.0276 642  LEU A CA  
631  C C   . LEU A 105 ? 0.2747 0.2290 0.2875 0.0346  0.0197  -0.0337 642  LEU A C   
632  O O   . LEU A 105 ? 0.2521 0.2136 0.2636 0.0370  0.0207  -0.0310 642  LEU A O   
633  C CB  . LEU A 105 ? 0.2845 0.2317 0.3001 0.0265  0.0171  -0.0224 642  LEU A CB  
634  C CG  . LEU A 105 ? 0.2686 0.2293 0.2832 0.0262  0.0176  -0.0180 642  LEU A CG  
635  C CD1 . LEU A 105 ? 0.2304 0.1914 0.2441 0.0318  0.0200  -0.0117 642  LEU A CD1 
636  C CD2 . LEU A 105 ? 0.2364 0.2046 0.2556 0.0198  0.0154  -0.0146 642  LEU A CD2 
637  N N   . LEU A 106 ? 0.2791 0.2339 0.2889 0.0306  0.0206  -0.0423 643  LEU A N   
638  C CA  . LEU A 106 ? 0.2888 0.2538 0.2936 0.0290  0.0239  -0.0481 643  LEU A CA  
639  C C   . LEU A 106 ? 0.3050 0.2759 0.3169 0.0359  0.0268  -0.0520 643  LEU A C   
640  O O   . LEU A 106 ? 0.2375 0.2182 0.2475 0.0345  0.0288  -0.0507 643  LEU A O   
641  C CB  . LEU A 106 ? 0.2807 0.2435 0.2785 0.0235  0.0254  -0.0580 643  LEU A CB  
642  C CG  . LEU A 106 ? 0.2768 0.2496 0.2658 0.0197  0.0306  -0.0644 643  LEU A CG  
643  C CD1 . LEU A 106 ? 0.2730 0.2518 0.2541 0.0152  0.0288  -0.0550 643  LEU A CD1 
644  C CD2 . LEU A 106 ? 0.2884 0.2574 0.2656 0.0131  0.0321  -0.0742 643  LEU A CD2 
645  N N   . SER A 107 ? 0.2985 0.2629 0.3193 0.0433  0.0261  -0.0564 644  SER A N   
646  C CA  . SER A 107 ? 0.2956 0.2687 0.3272 0.0512  0.0269  -0.0601 644  SER A CA  
647  C C   . SER A 107 ? 0.2850 0.2613 0.3173 0.0531  0.0233  -0.0505 644  SER A C   
648  O O   . SER A 107 ? 0.2792 0.2685 0.3174 0.0548  0.0239  -0.0527 644  SER A O   
649  C CB  . SER A 107 ? 0.3029 0.2656 0.3443 0.0609  0.0247  -0.0658 644  SER A CB  
650  O OG  . SER A 107 ? 0.3155 0.2739 0.3552 0.0596  0.0290  -0.0772 644  SER A OG  
651  N N   . LEU A 108 ? 0.2888 0.2545 0.3149 0.0521  0.0199  -0.0407 645  LEU A N   
652  C CA  . LEU A 108 ? 0.2938 0.2609 0.3167 0.0534  0.0175  -0.0328 645  LEU A CA  
653  C C   . LEU A 108 ? 0.2925 0.2688 0.3091 0.0475  0.0202  -0.0319 645  LEU A C   
654  O O   . LEU A 108 ? 0.2965 0.2785 0.3128 0.0480  0.0192  -0.0312 645  LEU A O   
655  C CB  . LEU A 108 ? 0.3311 0.2854 0.3478 0.0531  0.0156  -0.0235 645  LEU A CB  
656  C CG  . LEU A 108 ? 0.3635 0.3038 0.3817 0.0586  0.0113  -0.0206 645  LEU A CG  
657  C CD1 . LEU A 108 ? 0.3752 0.3033 0.3865 0.0538  0.0122  -0.0125 645  LEU A CD1 
658  C CD2 . LEU A 108 ? 0.3701 0.3111 0.3875 0.0650  0.0063  -0.0175 645  LEU A CD2 
659  N N   . LEU A 109 ? 0.2959 0.2723 0.3066 0.0415  0.0226  -0.0317 646  LEU A N   
660  C CA  . LEU A 109 ? 0.2895 0.2700 0.2921 0.0363  0.0241  -0.0296 646  LEU A CA  
661  C C   . LEU A 109 ? 0.3092 0.2997 0.3126 0.0328  0.0272  -0.0362 646  LEU A C   
662  O O   . LEU A 109 ? 0.3109 0.3031 0.3087 0.0290  0.0277  -0.0341 646  LEU A O   
663  C CB  . LEU A 109 ? 0.2805 0.2588 0.2768 0.0315  0.0237  -0.0273 646  LEU A CB  
664  C CG  . LEU A 109 ? 0.2815 0.2550 0.2804 0.0336  0.0215  -0.0208 646  LEU A CG  
665  C CD1 . LEU A 109 ? 0.2861 0.2614 0.2829 0.0289  0.0193  -0.0193 646  LEU A CD1 
666  C CD2 . LEU A 109 ? 0.2862 0.2577 0.2826 0.0371  0.0218  -0.0146 646  LEU A CD2 
667  N N   . ILE A 110 ? 0.3196 0.3164 0.3300 0.0334  0.0301  -0.0448 647  ILE A N   
668  C CA  . ILE A 110 ? 0.3406 0.3514 0.3552 0.0299  0.0350  -0.0523 647  ILE A CA  
669  C C   . ILE A 110 ? 0.3448 0.3644 0.3720 0.0347  0.0325  -0.0529 647  ILE A C   
670  O O   . ILE A 110 ? 0.3451 0.3757 0.3738 0.0291  0.0347  -0.0546 647  ILE A O   
671  C CB  . ILE A 110 ? 0.3488 0.3647 0.3680 0.0306  0.0402  -0.0630 647  ILE A CB  
672  C CG1 . ILE A 110 ? 0.3549 0.3632 0.3575 0.0229  0.0417  -0.0627 647  ILE A CG1 
673  C CG2 . ILE A 110 ? 0.3473 0.3825 0.3766 0.0287  0.0470  -0.0724 647  ILE A CG2 
674  C CD1 . ILE A 110 ? 0.3645 0.3733 0.3667 0.0229  0.0464  -0.0741 647  ILE A CD1 
675  N N   . GLU A 111 ? 0.3320 0.3460 0.3670 0.0442  0.0270  -0.0509 648  GLU A N   
676  C CA  . GLU A 111 ? 0.3312 0.3512 0.3749 0.0490  0.0215  -0.0495 648  GLU A CA  
677  C C   . GLU A 111 ? 0.3214 0.3379 0.3532 0.0427  0.0197  -0.0430 648  GLU A C   
678  O O   . GLU A 111 ? 0.3244 0.3520 0.3608 0.0393  0.0183  -0.0451 648  GLU A O   
679  C CB  . GLU A 111 ? 0.3542 0.3620 0.4007 0.0589  0.0148  -0.0453 648  GLU A CB  
680  C CG  . GLU A 111 ? 0.3786 0.3955 0.4414 0.0682  0.0088  -0.0489 648  GLU A CG  
681  C CD  . GLU A 111 ? 0.4056 0.4052 0.4635 0.0760  0.0004  -0.0409 648  GLU A CD  
682  O OE1 . GLU A 111 ? 0.3945 0.3967 0.4536 0.0796  -0.0076 -0.0373 648  GLU A OE1 
683  O OE2 . GLU A 111 ? 0.4304 0.4129 0.4814 0.0770  0.0016  -0.0378 648  GLU A OE2 
684  N N   . ARG A 112 ? 0.3126 0.3143 0.3302 0.0411  0.0197  -0.0359 649  ARG A N   
685  C CA  . ARG A 112 ? 0.3070 0.3016 0.3122 0.0371  0.0185  -0.0307 649  ARG A CA  
686  C C   . ARG A 112 ? 0.2784 0.2780 0.2789 0.0274  0.0221  -0.0332 649  ARG A C   
687  O O   . ARG A 112 ? 0.2583 0.2551 0.2524 0.0231  0.0203  -0.0321 649  ARG A O   
688  C CB  . ARG A 112 ? 0.3109 0.2918 0.3056 0.0388  0.0193  -0.0240 649  ARG A CB  
689  C CG  . ARG A 112 ? 0.3159 0.2869 0.2979 0.0376  0.0188  -0.0196 649  ARG A CG  
690  C CD  . ARG A 112 ? 0.3279 0.2937 0.3061 0.0425  0.0155  -0.0171 649  ARG A CD  
691  N NE  . ARG A 112 ? 0.3455 0.2998 0.3101 0.0428  0.0169  -0.0140 649  ARG A NE  
692  C CZ  . ARG A 112 ? 0.3716 0.3204 0.3263 0.0407  0.0146  -0.0155 649  ARG A CZ  
693  N NH1 . ARG A 112 ? 0.3897 0.3463 0.3486 0.0374  0.0097  -0.0193 649  ARG A NH1 
694  N NH2 . ARG A 112 ? 0.3749 0.3109 0.3163 0.0422  0.0170  -0.0141 649  ARG A NH2 
695  N N   . PHE A 113 ? 0.2687 0.2738 0.2698 0.0228  0.0271  -0.0368 650  PHE A N   
696  C CA  . PHE A 113 ? 0.2613 0.2674 0.2529 0.0119  0.0312  -0.0373 650  PHE A CA  
697  C C   . PHE A 113 ? 0.2824 0.3056 0.2841 0.0054  0.0336  -0.0435 650  PHE A C   
698  O O   . PHE A 113 ? 0.2915 0.3123 0.2845 -0.0049 0.0348  -0.0421 650  PHE A O   
699  C CB  . PHE A 113 ? 0.2505 0.2565 0.2361 0.0082  0.0356  -0.0389 650  PHE A CB  
700  C CG  . PHE A 113 ? 0.2580 0.2575 0.2263 -0.0030 0.0382  -0.0357 650  PHE A CG  
701  C CD1 . PHE A 113 ? 0.2608 0.2717 0.2285 -0.0137 0.0446  -0.0406 650  PHE A CD1 
702  C CD2 . PHE A 113 ? 0.2719 0.2540 0.2249 -0.0030 0.0343  -0.0275 650  PHE A CD2 
703  C CE1 . PHE A 113 ? 0.2822 0.2836 0.2303 -0.0257 0.0470  -0.0363 650  PHE A CE1 
704  C CE2 . PHE A 113 ? 0.2710 0.2431 0.2059 -0.0126 0.0351  -0.0232 650  PHE A CE2 
705  C CZ  . PHE A 113 ? 0.2914 0.2712 0.2217 -0.0247 0.0414  -0.0270 650  PHE A CZ  
706  N N   . GLU A 114 ? 0.2986 0.3392 0.3198 0.0112  0.0339  -0.0505 651  GLU A N   
707  C CA  . GLU A 114 ? 0.3391 0.4030 0.3764 0.0060  0.0367  -0.0579 651  GLU A CA  
708  C C   . GLU A 114 ? 0.3298 0.3966 0.3740 0.0084  0.0280  -0.0561 651  GLU A C   
709  O O   . GLU A 114 ? 0.3181 0.3941 0.3782 0.0187  0.0221  -0.0584 651  GLU A O   
710  C CB  . GLU A 114 ? 0.3800 0.4622 0.4368 0.0130  0.0413  -0.0675 651  GLU A CB  
711  C CG  . GLU A 114 ? 0.4367 0.5165 0.4832 0.0081  0.0507  -0.0710 651  GLU A CG  
712  C CD  . GLU A 114 ? 0.4757 0.5678 0.5385 0.0172  0.0554  -0.0817 651  GLU A CD  
713  O OE1 . GLU A 114 ? 0.4807 0.5799 0.5633 0.0295  0.0500  -0.0848 651  GLU A OE1 
714  O OE2 . GLU A 114 ? 0.4933 0.5861 0.5474 0.0122  0.0640  -0.0871 651  GLU A OE2 
715  N N   . ILE A 115 ? 0.2335 0.2905 0.2637 -0.0014 0.0263  -0.0520 652  ILE A N   
716  C CA  . ILE A 115 ? 0.2371 0.2907 0.2661 -0.0010 0.0174  -0.0500 652  ILE A CA  
717  C C   . ILE A 115 ? 0.4043 0.4829 0.4503 -0.0106 0.0167  -0.0565 652  ILE A C   
718  O O   . ILE A 115 ? 0.2479 0.3305 0.2898 -0.0250 0.0234  -0.0581 652  ILE A O   
719  C CB  . ILE A 115 ? 0.3086 0.3347 0.3121 -0.0057 0.0160  -0.0434 652  ILE A CB  
720  C CG1 . ILE A 115 ? 0.2788 0.2862 0.2710 0.0044  0.0169  -0.0375 652  ILE A CG1 
721  C CG2 . ILE A 115 ? 0.2557 0.2772 0.2547 -0.0069 0.0075  -0.0432 652  ILE A CG2 
722  C CD1 . ILE A 115 ? 0.2691 0.2518 0.2395 0.0017  0.0174  -0.0319 652  ILE A CD1 
723  N N   . PRO A 116 ? 0.3635 0.4599 0.4287 -0.0038 0.0085  -0.0599 653  PRO A N   
724  C CA  . PRO A 116 ? 0.3488 0.4717 0.4323 -0.0139 0.0061  -0.0660 653  PRO A CA  
725  C C   . PRO A 116 ? 0.3680 0.4757 0.4334 -0.0256 -0.0003 -0.0628 653  PRO A C   
726  O O   . PRO A 116 ? 0.3680 0.4488 0.4116 -0.0208 -0.0059 -0.0571 653  PRO A O   
727  C CB  . PRO A 116 ? 0.3314 0.4754 0.4406 0.0005  -0.0034 -0.0694 653  PRO A CB  
728  C CG  . PRO A 116 ? 0.3308 0.4479 0.4232 0.0143  -0.0099 -0.0620 653  PRO A CG  
729  C CD  . PRO A 116 ? 0.3415 0.4351 0.4131 0.0129  0.0004  -0.0579 653  PRO A CD  
730  N N   . GLU A 117 ? 0.3861 0.5108 0.4600 -0.0421 0.0015  -0.0673 654  GLU A N   
731  C CA  . GLU A 117 ? 0.4114 0.5209 0.4685 -0.0547 -0.0055 -0.0659 654  GLU A CA  
732  C C   . GLU A 117 ? 0.4320 0.5583 0.5035 -0.0506 -0.0204 -0.0688 654  GLU A C   
733  O O   . GLU A 117 ? 0.4339 0.5914 0.5351 -0.0416 -0.0242 -0.0729 654  GLU A O   
734  C CB  . GLU A 117 ? 0.4138 0.5304 0.4707 -0.0772 0.0021  -0.0686 654  GLU A CB  
735  C CG  . GLU A 117 ? 0.4133 0.5100 0.4512 -0.0825 0.0150  -0.0642 654  GLU A CG  
736  C CD  . GLU A 117 ? 0.4268 0.5231 0.4575 -0.1066 0.0221  -0.0648 654  GLU A CD  
737  O OE1 . GLU A 117 ? 0.4207 0.5453 0.4717 -0.1198 0.0207  -0.0708 654  GLU A OE1 
738  O OE2 . GLU A 117 ? 0.4380 0.5056 0.4427 -0.1127 0.0284  -0.0587 654  GLU A OE2 
739  N N   . PRO A 118 ? 0.4626 0.5677 0.5126 -0.0559 -0.0297 -0.0671 655  PRO A N   
740  C CA  . PRO A 118 ? 0.4893 0.6101 0.5497 -0.0540 -0.0457 -0.0697 655  PRO A CA  
741  C C   . PRO A 118 ? 0.5105 0.6732 0.6044 -0.0665 -0.0485 -0.0772 655  PRO A C   
742  O O   . PRO A 118 ? 0.5133 0.6852 0.6132 -0.0828 -0.0379 -0.0803 655  PRO A O   
743  C CB  . PRO A 118 ? 0.5039 0.5901 0.5293 -0.0621 -0.0518 -0.0681 655  PRO A CB  
744  C CG  . PRO A 118 ? 0.5038 0.5546 0.5026 -0.0589 -0.0400 -0.0629 655  PRO A CG  
745  C CD  . PRO A 118 ? 0.4819 0.5464 0.4962 -0.0626 -0.0268 -0.0630 655  PRO A CD  
746  N N   . GLU A 119 ? 0.5322 0.7212 0.6483 -0.0590 -0.0629 -0.0798 656  GLU A N   
747  C CA  . GLU A 119 ? 0.5619 0.7966 0.7152 -0.0695 -0.0675 -0.0875 656  GLU A CA  
748  C C   . GLU A 119 ? 0.5845 0.8133 0.7249 -0.0953 -0.0702 -0.0905 656  GLU A C   
749  O O   . GLU A 119 ? 0.6000 0.8047 0.7146 -0.0988 -0.0827 -0.0889 656  GLU A O   
750  C CB  . GLU A 119 ? 0.5910 0.8518 0.7684 -0.0549 -0.0863 -0.0886 656  GLU A CB  
751  C CG  . GLU A 119 ? 0.6052 0.9221 0.8342 -0.0552 -0.0874 -0.0969 656  GLU A CG  
752  C CD  . GLU A 119 ? 0.6049 0.9365 0.8574 -0.0359 -0.0765 -0.0984 656  GLU A CD  
753  O OE1 . GLU A 119 ? 0.6164 0.9645 0.8911 -0.0157 -0.0883 -0.0985 656  GLU A OE1 
754  O OE2 . GLU A 119 ? 0.5934 0.9172 0.8397 -0.0406 -0.0569 -0.0994 656  GLU A OE2 
755  N N   . PRO A 120 ? 0.5919 0.8397 0.7468 -0.1146 -0.0586 -0.0950 657  PRO A N   
756  C CA  . PRO A 120 ? 0.6273 0.8669 0.7692 -0.1414 -0.0615 -0.0977 657  PRO A CA  
757  C C   . PRO A 120 ? 0.6537 0.9170 0.8111 -0.1463 -0.0824 -0.1024 657  PRO A C   
758  O O   . PRO A 120 ? 0.6398 0.9443 0.8337 -0.1342 -0.0918 -0.1056 657  PRO A O   
759  C CB  . PRO A 120 ? 0.6196 0.8874 0.7840 -0.1596 -0.0450 -0.1017 657  PRO A CB  
760  C CG  . PRO A 120 ? 0.5913 0.8615 0.7618 -0.1423 -0.0301 -0.0994 657  PRO A CG  
761  C CD  . PRO A 120 ? 0.5703 0.8454 0.7509 -0.1143 -0.0413 -0.0981 657  PRO A CD  
762  N N   . THR A 121 ? 0.7031 0.9383 0.8313 -0.1633 -0.0908 -0.1032 658  THR A N   
763  C CA  . THR A 121 ? 0.7374 0.9934 0.8765 -0.1720 -0.1119 -0.1084 658  THR A CA  
764  C C   . THR A 121 ? 0.7574 1.0609 0.9352 -0.1961 -0.1110 -0.1160 658  THR A C   
765  O O   . THR A 121 ? 0.7579 1.0681 0.9437 -0.2104 -0.0928 -0.1168 658  THR A O   
766  C CB  . THR A 121 ? 0.7634 0.9700 0.8545 -0.1817 -0.1215 -0.1080 658  THR A CB  
767  O OG1 . THR A 121 ? 0.7854 1.0128 0.8852 -0.1895 -0.1440 -0.1133 658  THR A OG1 
768  C CG2 . THR A 121 ? 0.7787 0.9552 0.8466 -0.2069 -0.1095 -0.1094 658  THR A CG2 
769  N N   . ASP A 122 ? 0.7763 1.1147 0.9783 -0.2011 -0.1312 -0.1213 659  ASP A N   
770  C CA  . ASP A 122 ? 0.7935 1.1847 1.0385 -0.2241 -0.1320 -0.1293 659  ASP A CA  
771  C C   . ASP A 122 ? 0.8360 1.2024 1.0579 -0.2576 -0.1212 -0.1311 659  ASP A C   
772  O O   . ASP A 122 ? 0.8385 1.2317 1.0857 -0.2732 -0.1064 -0.1329 659  ASP A O   
773  C CB  . ASP A 122 ? 0.8009 1.2274 1.0696 -0.2252 -0.1593 -0.1343 659  ASP A CB  
774  C CG  . ASP A 122 ? 0.7776 1.2415 1.0823 -0.1943 -0.1698 -0.1330 659  ASP A CG  
775  O OD1 . ASP A 122 ? 0.7524 1.2558 1.0986 -0.1846 -0.1565 -0.1353 659  ASP A OD1 
776  O OD2 . ASP A 122 ? 0.7879 1.2388 1.0770 -0.1794 -0.1910 -0.1297 659  ASP A OD2 
777  N N   . ALA A 123 ? 0.8756 1.1834 1.0459 -0.2653 -0.1265 -0.1287 660  ALA A N   
778  C CA  . ALA A 123 ? 0.9133 1.1873 1.0562 -0.2952 -0.1171 -0.1295 660  ALA A CA  
779  C C   . ALA A 123 ? 0.9096 1.1591 1.0381 -0.2944 -0.0922 -0.1231 660  ALA A C   
780  O O   . ALA A 123 ? 0.9300 1.1692 1.0520 -0.3183 -0.0801 -0.1222 660  ALA A O   
781  C CB  . ALA A 123 ? 0.9485 1.1637 1.0394 -0.3000 -0.1296 -0.1299 660  ALA A CB  
782  N N   . ASP A 124 ? 0.8888 1.1250 1.0097 -0.2653 -0.0845 -0.1170 661  ASP A N   
783  C CA  . ASP A 124 ? 0.8866 1.1033 0.9955 -0.2632 -0.0625 -0.1108 661  ASP A CA  
784  C C   . ASP A 124 ? 0.8812 1.1524 1.0335 -0.2724 -0.0484 -0.1139 661  ASP A C   
785  O O   . ASP A 124 ? 0.8899 1.1510 1.0326 -0.2903 -0.0316 -0.1112 661  ASP A O   
786  C CB  . ASP A 124 ? 0.8600 1.0521 0.9521 -0.2308 -0.0593 -0.1043 661  ASP A CB  
787  C CG  . ASP A 124 ? 0.8727 1.0012 0.9142 -0.2254 -0.0630 -0.0999 661  ASP A CG  
788  O OD1 . ASP A 124 ? 0.9090 1.0074 0.9254 -0.2464 -0.0667 -0.1018 661  ASP A OD1 
789  O OD2 . ASP A 124 ? 0.8517 0.9609 0.8794 -0.2004 -0.0619 -0.0950 661  ASP A OD2 
790  N N   . LYS A 125 ? 0.8679 1.1962 1.0671 -0.2598 -0.0548 -0.1195 662  LYS A N   
791  C CA  . LYS A 125 ? 0.8585 1.2435 1.1031 -0.2664 -0.0403 -0.1247 662  LYS A CA  
792  C C   . LYS A 125 ? 0.9043 1.3002 1.1552 -0.2970 -0.0350 -0.1261 662  LYS A C   
793  O O   . LYS A 125 ? 0.9060 1.3126 1.1631 -0.3073 -0.0150 -0.1246 662  LYS A O   
794  C CB  . LYS A 125 ? 0.8208 1.2623 1.1154 -0.2442 -0.0512 -0.1309 662  LYS A CB  
795  C CG  . LYS A 125 ? 0.7918 1.2121 1.0748 -0.2084 -0.0579 -0.1259 662  LYS A CG  
796  C CD  . LYS A 125 ? 0.7652 1.2395 1.0985 -0.1862 -0.0678 -0.1314 662  LYS A CD  
797  C CE  . LYS A 125 ? 0.7459 1.1961 1.0664 -0.1523 -0.0701 -0.1257 662  LYS A CE  
798  N NZ  . LYS A 125 ? 0.7296 1.2253 1.0959 -0.1286 -0.0811 -0.1302 662  LYS A NZ  
799  N N   . LEU A 126 ? 0.9492 1.3367 1.1941 -0.3089 -0.0525 -0.1275 663  LEU A N   
800  C CA  . LEU A 126 ? 1.0027 1.3943 1.2510 -0.3355 -0.0488 -0.1276 663  LEU A CA  
801  C C   . LEU A 126 ? 1.0523 1.3949 1.2584 -0.3549 -0.0314 -0.1208 663  LEU A C   
802  O O   . LEU A 126 ? 1.0698 1.4255 1.2840 -0.3728 -0.0172 -0.1194 663  LEU A O   
803  C CB  . LEU A 126 ? 1.0269 1.4090 1.2690 -0.3440 -0.0721 -0.1305 663  LEU A CB  
804  C CG  . LEU A 126 ? 1.0135 1.4424 1.2955 -0.3269 -0.0929 -0.1358 663  LEU A CG  
805  C CD1 . LEU A 126 ? 1.0442 1.4496 1.3056 -0.3346 -0.1168 -0.1381 663  LEU A CD1 
806  C CD2 . LEU A 126 ? 1.0088 1.5017 1.3468 -0.3293 -0.0872 -0.1394 663  LEU A CD2 
807  N N   . ALA A 127 ? 1.0797 1.3646 1.2395 -0.3507 -0.0328 -0.1160 664  ALA A N   
808  C CA  . ALA A 127 ? 1.1306 1.3627 1.2474 -0.3660 -0.0189 -0.1080 664  ALA A CA  
809  C C   . ALA A 127 ? 1.1450 1.3946 1.2705 -0.3656 0.0036  -0.1042 664  ALA A C   
810  O O   . ALA A 127 ? 1.1726 1.4105 1.2848 -0.3845 0.0169  -0.0993 664  ALA A O   
811  C CB  . ALA A 127 ? 1.1333 1.3020 1.2027 -0.3564 -0.0256 -0.1041 664  ALA A CB  
812  N N   . ILE A 128 ? 1.1309 1.4075 1.2770 -0.3438 0.0081  -0.1065 665  ILE A N   
813  C CA  . ILE A 128 ? 1.1369 1.4332 1.2923 -0.3413 0.0295  -0.1045 665  ILE A CA  
814  C C   . ILE A 128 ? 1.1697 1.5146 1.3593 -0.3541 0.0393  -0.1087 665  ILE A C   
815  O O   . ILE A 128 ? 1.1937 1.5335 1.3707 -0.3681 0.0568  -0.1046 665  ILE A O   
816  C CB  . ILE A 128 ? 1.0798 1.4004 1.2561 -0.3137 0.0306  -0.1085 665  ILE A CB  
817  C CG1 . ILE A 128 ? 1.0666 1.3260 1.1971 -0.2964 0.0291  -0.0993 665  ILE A CG1 
818  C CG2 . ILE A 128 ? 1.0649 1.4276 1.2688 -0.3079 0.0501  -0.1115 665  ILE A CG2 
819  C CD1 . ILE A 128 ? 1.0413 1.2892 1.1706 -0.2671 0.0115  -0.0996 665  ILE A CD1 
820  N N   . GLU A 129 ? 1.1731 1.5648 1.4052 -0.3494 0.0273  -0.1165 666  GLU A N   
821  C CA  . GLU A 129 ? 1.1952 1.6372 1.4651 -0.3602 0.0356  -0.1213 666  GLU A CA  
822  C C   . GLU A 129 ? 1.2470 1.6651 1.4930 -0.3916 0.0413  -0.1166 666  GLU A C   
823  O O   . GLU A 129 ? 1.2684 1.7083 1.5241 -0.4050 0.0583  -0.1168 666  GLU A O   
824  C CB  . GLU A 129 ? 1.1865 1.6761 1.5031 -0.3492 0.0172  -0.1292 666  GLU A CB  
825  C CG  . GLU A 129 ? 1.2002 1.7511 1.5662 -0.3519 0.0254  -0.1355 666  GLU A CG  
826  C CD  . GLU A 129 ? 1.1928 1.7912 1.6071 -0.3297 0.0081  -0.1423 666  GLU A CD  
827  O OE1 . GLU A 129 ? 1.2136 1.8438 1.6580 -0.3394 -0.0029 -0.1457 666  GLU A OE1 
828  O OE2 . GLU A 129 ? 1.1692 1.7712 1.5904 -0.3024 0.0043  -0.1436 666  GLU A OE2 
829  N N   . LYS A 130 ? 1.2708 1.6421 1.4838 -0.4034 0.0276  -0.1127 667  LYS A N   
830  C CA  . LYS A 130 ? 1.3158 1.6566 1.5019 -0.4324 0.0317  -0.1078 667  LYS A CA  
831  C C   . LYS A 130 ? 1.3247 1.6320 1.4744 -0.4413 0.0519  -0.0990 667  LYS A C   
832  O O   . LYS A 130 ? 1.3542 1.6715 1.5041 -0.4614 0.0651  -0.0971 667  LYS A O   
833  C CB  . LYS A 130 ? 1.3417 1.6307 1.4941 -0.4383 0.0130  -0.1059 667  LYS A CB  
834  C CG  . LYS A 130 ? 1.3971 1.6452 1.5166 -0.4662 0.0157  -0.1007 667  LYS A CG  
835  C CD  . LYS A 130 ? 1.4204 1.6162 1.5067 -0.4680 -0.0029 -0.1007 667  LYS A CD  
836  C CE  . LYS A 130 ? 1.4762 1.6323 1.5325 -0.4951 -0.0013 -0.0964 667  LYS A CE  
837  N NZ  . LYS A 130 ? 1.5016 1.5861 1.5086 -0.4924 -0.0123 -0.0934 667  LYS A NZ  
838  N N   . GLY A 131 ? 1.2981 1.5655 1.4157 -0.4268 0.0538  -0.0933 668  GLY A N   
839  C CA  . GLY A 131 ? 1.3007 1.5348 1.3823 -0.4323 0.0704  -0.0841 668  GLY A CA  
840  C C   . GLY A 131 ? 1.3273 1.4875 1.3540 -0.4435 0.0650  -0.0739 668  GLY A C   
841  O O   . GLY A 131 ? 1.3586 1.4973 1.3753 -0.4574 0.0540  -0.0742 668  GLY A O   
842  N N   . GLU A 132 ? 1.3147 1.4341 1.3052 -0.4361 0.0723  -0.0649 669  GLU A N   
843  C CA  . GLU A 132 ? 1.3357 1.3819 1.2728 -0.4422 0.0678  -0.0540 669  GLU A CA  
844  C C   . GLU A 132 ? 1.3085 1.3197 1.2334 -0.4327 0.0490  -0.0564 669  GLU A C   
845  O O   . GLU A 132 ? 1.3469 1.3138 1.2439 -0.4439 0.0411  -0.0533 669  GLU A O   
846  C CB  . GLU A 132 ? 1.3947 1.4242 1.3130 -0.4696 0.0737  -0.0487 669  GLU A CB  
847  C CG  . GLU A 132 ? 1.4133 1.4663 1.3325 -0.4799 0.0928  -0.0452 669  GLU A CG  
848  C CD  . GLU A 132 ? 1.4800 1.5209 1.3835 -0.5090 0.0983  -0.0408 669  GLU A CD  
849  O OE1 . GLU A 132 ? 1.4879 1.5763 1.4263 -0.5236 0.1016  -0.0486 669  GLU A OE1 
850  O OE2 . GLU A 132 ? 1.5252 1.5091 1.3820 -0.5170 0.0987  -0.0295 669  GLU A OE2 
851  N N   . GLN A 133 ? 1.2381 1.2685 1.1828 -0.4114 0.0420  -0.0625 670  GLN A N   
852  C CA  . GLN A 133 ? 1.2106 1.2126 1.1445 -0.4003 0.0246  -0.0664 670  GLN A CA  
853  C C   . GLN A 133 ? 1.1720 1.1435 1.0861 -0.3775 0.0235  -0.0626 670  GLN A C   
854  O O   . GLN A 133 ? 1.1341 1.1394 1.0700 -0.3648 0.0303  -0.0643 670  GLN A O   
855  C CB  . GLN A 133 ? 1.1754 1.2311 1.1527 -0.3963 0.0134  -0.0784 670  GLN A CB  
856  C CG  . GLN A 133 ? 1.1844 1.2819 1.1911 -0.4170 0.0148  -0.0829 670  GLN A CG  
857  C CD  . GLN A 133 ? 1.2302 1.2844 1.2065 -0.4387 0.0106  -0.0796 670  GLN A CD  
858  O OE1 . GLN A 133 ? 1.2484 1.2545 1.1948 -0.4354 -0.0016 -0.0796 670  GLN A OE1 
859  N NE2 . GLN A 133 ? 1.2521 1.3226 1.2353 -0.4606 0.0213  -0.0773 670  GLN A NE2 
860  N N   . PRO A 134 ? 1.1753 1.0838 1.0494 -0.3708 0.0155  -0.0582 671  PRO A N   
861  C CA  . PRO A 134 ? 1.1278 1.0075 0.9846 -0.3481 0.0138  -0.0552 671  PRO A CA  
862  C C   . PRO A 134 ? 1.0496 0.9660 0.9351 -0.3227 0.0052  -0.0636 671  PRO A C   
863  O O   . PRO A 134 ? 1.0561 0.9892 0.9554 -0.3276 -0.0062 -0.0724 671  PRO A O   
864  C CB  . PRO A 134 ? 1.1754 0.9842 0.9881 -0.3440 0.0059  -0.0507 671  PRO A CB  
865  C CG  . PRO A 134 ? 1.2161 1.0240 1.0291 -0.3624 -0.0010 -0.0556 671  PRO A CG  
866  C CD  . PRO A 134 ? 1.2189 1.0791 1.0622 -0.3828 0.0084  -0.0560 671  PRO A CD  
867  N N   . ILE A 135 ? 0.9700 0.8980 0.8631 -0.2954 0.0101  -0.0600 672  ILE A N   
868  C CA  . ILE A 135 ? 0.8830 0.8461 0.8033 -0.2705 0.0032  -0.0661 672  ILE A CA  
869  C C   . ILE A 135 ? 0.8492 0.7805 0.7504 -0.2588 -0.0112 -0.0696 672  ILE A C   
870  O O   . ILE A 135 ? 0.8788 0.7568 0.7442 -0.2628 -0.0140 -0.0670 672  ILE A O   
871  C CB  . ILE A 135 ? 0.8474 0.8196 0.7735 -0.2451 0.0112  -0.0611 672  ILE A CB  
872  C CG1 . ILE A 135 ? 0.8577 0.7734 0.7452 -0.2327 0.0119  -0.0522 672  ILE A CG1 
873  C CG2 . ILE A 135 ? 0.8385 0.8469 0.7844 -0.2564 0.0258  -0.0602 672  ILE A CG2 
874  C CD1 . ILE A 135 ? 0.8267 0.7487 0.7183 -0.2081 0.0173  -0.0475 672  ILE A CD1 
875  N N   . SER A 136 ? 0.7848 0.7483 0.7089 -0.2437 -0.0203 -0.0757 673  SER A N   
876  C CA  . SER A 136 ? 0.7649 0.7042 0.6711 -0.2350 -0.0340 -0.0801 673  SER A CA  
877  C C   . SER A 136 ? 0.7450 0.6345 0.6175 -0.2145 -0.0315 -0.0748 673  SER A C   
878  O O   . SER A 136 ? 0.7178 0.6069 0.5920 -0.1979 -0.0227 -0.0681 673  SER A O   
879  C CB  . SER A 136 ? 0.7261 0.7087 0.6612 -0.2201 -0.0440 -0.0853 673  SER A CB  
880  O OG  . SER A 136 ? 0.6808 0.6676 0.6203 -0.1922 -0.0399 -0.0806 673  SER A OG  
881  N N   . ALA A 137 ? 0.7577 0.6059 0.6000 -0.2161 -0.0393 -0.0786 674  ALA A N   
882  C CA  . ALA A 137 ? 0.7429 0.5456 0.5553 -0.1959 -0.0369 -0.0755 674  ALA A CA  
883  C C   . ALA A 137 ? 0.6919 0.5149 0.5170 -0.1677 -0.0356 -0.0731 674  ALA A C   
884  O O   . ALA A 137 ? 0.6757 0.4796 0.4910 -0.1503 -0.0285 -0.0671 674  ALA A O   
885  C CB  . ALA A 137 ? 0.7817 0.5437 0.5629 -0.2011 -0.0458 -0.0833 674  ALA A CB  
886  N N   . ASP A 138 ? 0.6646 0.5266 0.5121 -0.1634 -0.0431 -0.0772 675  ASP A N   
887  C CA  . ASP A 138 ? 0.6264 0.5072 0.4859 -0.1388 -0.0424 -0.0742 675  ASP A CA  
888  C C   . ASP A 138 ? 0.5910 0.4920 0.4708 -0.1306 -0.0314 -0.0673 675  ASP A C   
889  O O   . ASP A 138 ? 0.5626 0.4545 0.4380 -0.1114 -0.0261 -0.0623 675  ASP A O   
890  C CB  . ASP A 138 ? 0.6119 0.5294 0.4916 -0.1375 -0.0544 -0.0790 675  ASP A CB  
891  C CG  . ASP A 138 ? 0.6424 0.5382 0.4969 -0.1411 -0.0662 -0.0855 675  ASP A CG  
892  O OD1 . ASP A 138 ? 0.6693 0.5209 0.4913 -0.1442 -0.0638 -0.0877 675  ASP A OD1 
893  O OD2 . ASP A 138 ? 0.6451 0.5669 0.5112 -0.1404 -0.0786 -0.0888 675  ASP A OD2 
894  N N   . LEU A 139 ? 0.5857 0.5154 0.4879 -0.1458 -0.0275 -0.0675 676  LEU A N   
895  C CA  . LEU A 139 ? 0.5613 0.5110 0.4807 -0.1392 -0.0167 -0.0624 676  LEU A CA  
896  C C   . LEU A 139 ? 0.5804 0.4924 0.4748 -0.1371 -0.0080 -0.0551 676  LEU A C   
897  O O   . LEU A 139 ? 0.5486 0.4637 0.4467 -0.1226 -0.0018 -0.0501 676  LEU A O   
898  C CB  . LEU A 139 ? 0.5548 0.5446 0.5024 -0.1571 -0.0128 -0.0657 676  LEU A CB  
899  C CG  . LEU A 139 ? 0.5359 0.5530 0.5039 -0.1507 -0.0012 -0.0633 676  LEU A CG  
900  C CD1 . LEU A 139 ? 0.5128 0.5464 0.4961 -0.1252 -0.0039 -0.0633 676  LEU A CD1 
901  C CD2 . LEU A 139 ? 0.5319 0.5917 0.5291 -0.1690 0.0040  -0.0686 676  LEU A CD2 
902  N N   . LYS A 140 ? 0.6189 0.4938 0.4873 -0.1515 -0.0088 -0.0543 677  LYS A N   
903  C CA  . LYS A 140 ? 0.6277 0.4627 0.4709 -0.1472 -0.0032 -0.0466 677  LYS A CA  
904  C C   . LYS A 140 ? 0.5961 0.4107 0.4282 -0.1219 -0.0047 -0.0449 677  LYS A C   
905  O O   . LYS A 140 ? 0.5944 0.4015 0.4236 -0.1092 0.0004  -0.0382 677  LYS A O   
906  C CB  . LYS A 140 ? 0.6940 0.4889 0.5105 -0.1671 -0.0052 -0.0464 677  LYS A CB  
907  C CG  . LYS A 140 ? 0.7397 0.4890 0.5288 -0.1613 -0.0016 -0.0377 677  LYS A CG  
908  C CD  . LYS A 140 ? 0.8146 0.5177 0.5749 -0.1799 -0.0048 -0.0375 677  LYS A CD  
909  C CE  . LYS A 140 ? 0.8548 0.5103 0.5881 -0.1716 -0.0031 -0.0281 677  LYS A CE  
910  N NZ  . LYS A 140 ? 0.9179 0.5238 0.6215 -0.1905 -0.0065 -0.0273 677  LYS A NZ  
911  N N   . ARG A 141 ? 0.5826 0.3889 0.4075 -0.1152 -0.0116 -0.0511 678  ARG A N   
912  C CA  . ARG A 141 ? 0.5632 0.3564 0.3800 -0.0920 -0.0112 -0.0504 678  ARG A CA  
913  C C   . ARG A 141 ? 0.4975 0.3236 0.3375 -0.0768 -0.0075 -0.0465 678  ARG A C   
914  O O   . ARG A 141 ? 0.4870 0.3039 0.3241 -0.0611 -0.0030 -0.0416 678  ARG A O   
915  C CB  . ARG A 141 ? 0.5915 0.3774 0.3973 -0.0898 -0.0185 -0.0584 678  ARG A CB  
916  C CG  . ARG A 141 ? 0.6598 0.3997 0.4343 -0.0948 -0.0207 -0.0632 678  ARG A CG  
917  C CD  . ARG A 141 ? 0.6866 0.4189 0.4470 -0.0865 -0.0256 -0.0710 678  ARG A CD  
918  N NE  . ARG A 141 ? 0.6770 0.4101 0.4373 -0.0632 -0.0197 -0.0684 678  ARG A NE  
919  C CZ  . ARG A 141 ? 0.6904 0.4211 0.4389 -0.0536 -0.0213 -0.0734 678  ARG A CZ  
920  N NH1 . ARG A 141 ? 0.7182 0.4449 0.4529 -0.0646 -0.0300 -0.0814 678  ARG A NH1 
921  N NH2 . ARG A 141 ? 0.6760 0.4091 0.4258 -0.0345 -0.0143 -0.0704 678  ARG A NH2 
922  N N   . PHE A 142 ? 0.4581 0.3226 0.3223 -0.0810 -0.0099 -0.0490 679  PHE A N   
923  C CA  . PHE A 142 ? 0.4212 0.3146 0.3069 -0.0667 -0.0075 -0.0466 679  PHE A CA  
924  C C   . PHE A 142 ? 0.4347 0.3295 0.3248 -0.0637 0.0010  -0.0405 679  PHE A C   
925  O O   . PHE A 142 ? 0.4191 0.3149 0.3123 -0.0484 0.0039  -0.0368 679  PHE A O   
926  C CB  . PHE A 142 ? 0.3868 0.3194 0.2986 -0.0724 -0.0124 -0.0512 679  PHE A CB  
927  C CG  . PHE A 142 ? 0.3531 0.3139 0.2882 -0.0591 -0.0098 -0.0495 679  PHE A CG  
928  C CD1 . PHE A 142 ? 0.3518 0.3121 0.2866 -0.0422 -0.0131 -0.0477 679  PHE A CD1 
929  C CD2 . PHE A 142 ? 0.3306 0.3171 0.2863 -0.0644 -0.0036 -0.0501 679  PHE A CD2 
930  C CE1 . PHE A 142 ? 0.3207 0.3026 0.2754 -0.0306 -0.0113 -0.0461 679  PHE A CE1 
931  C CE2 . PHE A 142 ? 0.3069 0.3160 0.2827 -0.0517 -0.0012 -0.0500 679  PHE A CE2 
932  C CZ  . PHE A 142 ? 0.2971 0.3024 0.2723 -0.0348 -0.0057 -0.0478 679  PHE A CZ  
933  N N   . ARG A 143 ? 0.4705 0.3648 0.3591 -0.0798 0.0050  -0.0392 680  ARG A N   
934  C CA  . ARG A 143 ? 0.4762 0.3710 0.3649 -0.0788 0.0123  -0.0333 680  ARG A CA  
935  C C   . ARG A 143 ? 0.5067 0.3653 0.3731 -0.0691 0.0125  -0.0267 680  ARG A C   
936  O O   . ARG A 143 ? 0.4932 0.3537 0.3615 -0.0591 0.0155  -0.0218 680  ARG A O   
937  C CB  . ARG A 143 ? 0.4798 0.3822 0.3690 -0.1004 0.0172  -0.0332 680  ARG A CB  
938  C CG  . ARG A 143 ? 0.4707 0.4159 0.3880 -0.1094 0.0187  -0.0403 680  ARG A CG  
939  C CD  . ARG A 143 ? 0.4901 0.4434 0.4068 -0.1324 0.0262  -0.0400 680  ARG A CD  
940  N NE  . ARG A 143 ? 0.4903 0.4890 0.4379 -0.1411 0.0290  -0.0479 680  ARG A NE  
941  C CZ  . ARG A 143 ? 0.5046 0.5194 0.4578 -0.1634 0.0363  -0.0498 680  ARG A CZ  
942  N NH1 . ARG A 143 ? 0.5268 0.5116 0.4527 -0.1802 0.0410  -0.0432 680  ARG A NH1 
943  N NH2 . ARG A 143 ? 0.4926 0.5534 0.4789 -0.1691 0.0390  -0.0581 680  ARG A NH2 
944  N N   . LYS A 144 ? 0.5471 0.3728 0.3930 -0.0714 0.0088  -0.0272 681  LYS A N   
945  C CA  . LYS A 144 ? 0.5915 0.3824 0.4180 -0.0617 0.0087  -0.0212 681  LYS A CA  
946  C C   . LYS A 144 ? 0.5830 0.3706 0.4116 -0.0401 0.0080  -0.0224 681  LYS A C   
947  O O   . LYS A 144 ? 0.5949 0.3727 0.4212 -0.0273 0.0092  -0.0170 681  LYS A O   
948  C CB  . LYS A 144 ? 0.6585 0.4105 0.4604 -0.0737 0.0058  -0.0214 681  LYS A CB  
949  C CG  . LYS A 144 ? 0.7058 0.4205 0.4877 -0.0674 0.0052  -0.0133 681  LYS A CG  
950  C CD  . LYS A 144 ? 0.7597 0.4345 0.5164 -0.0835 0.0024  -0.0124 681  LYS A CD  
951  C CE  . LYS A 144 ? 0.7775 0.4303 0.5232 -0.0811 -0.0012 -0.0216 681  LYS A CE  
952  N NZ  . LYS A 144 ? 0.7781 0.4154 0.5205 -0.0559 -0.0013 -0.0231 681  LYS A NZ  
953  N N   . GLU A 145 ? 0.5626 0.3594 0.3953 -0.0365 0.0058  -0.0290 682  GLU A N   
954  C CA  . GLU A 145 ? 0.5526 0.3463 0.3847 -0.0182 0.0068  -0.0303 682  GLU A CA  
955  C C   . GLU A 145 ? 0.5001 0.3263 0.3532 -0.0092 0.0086  -0.0290 682  GLU A C   
956  O O   . GLU A 145 ? 0.5074 0.3334 0.3616 0.0049  0.0109  -0.0284 682  GLU A O   
957  C CB  . GLU A 145 ? 0.5891 0.3679 0.4065 -0.0193 0.0037  -0.0380 682  GLU A CB  
958  C CG  . GLU A 145 ? 0.6467 0.3875 0.4406 -0.0277 0.0017  -0.0409 682  GLU A CG  
959  C CD  . GLU A 145 ? 0.6753 0.4007 0.4522 -0.0295 -0.0017 -0.0502 682  GLU A CD  
960  O OE1 . GLU A 145 ? 0.6699 0.3983 0.4444 -0.0160 0.0006  -0.0531 682  GLU A OE1 
961  O OE2 . GLU A 145 ? 0.6998 0.4102 0.4644 -0.0460 -0.0065 -0.0547 682  GLU A OE2 
962  N N   . TYR A 146 ? 0.4532 0.3065 0.3231 -0.0170 0.0081  -0.0289 683  TYR A N   
963  C CA  . TYR A 146 ? 0.4060 0.2855 0.2943 -0.0080 0.0089  -0.0283 683  TYR A CA  
964  C C   . TYR A 146 ? 0.3884 0.2856 0.2910 -0.0096 0.0124  -0.0252 683  TYR A C   
965  O O   . TYR A 146 ? 0.3700 0.2700 0.2775 0.0003  0.0149  -0.0215 683  TYR A O   
966  C CB  . TYR A 146 ? 0.3846 0.2821 0.2813 -0.0116 0.0037  -0.0332 683  TYR A CB  
967  C CG  . TYR A 146 ? 0.3501 0.2654 0.2601 -0.0002 0.0031  -0.0319 683  TYR A CG  
968  C CD1 . TYR A 146 ? 0.3466 0.2517 0.2470 0.0104  0.0034  -0.0305 683  TYR A CD1 
969  C CD2 . TYR A 146 ? 0.3289 0.2697 0.2601 -0.0003 0.0029  -0.0323 683  TYR A CD2 
970  C CE1 . TYR A 146 ? 0.3231 0.2410 0.2330 0.0190  0.0028  -0.0280 683  TYR A CE1 
971  C CE2 . TYR A 146 ? 0.2988 0.2508 0.2403 0.0101  0.0016  -0.0308 683  TYR A CE2 
972  C CZ  . TYR A 146 ? 0.2954 0.2349 0.2254 0.0189  0.0011  -0.0279 683  TYR A CZ  
973  O OH  . TYR A 146 ? 0.2787 0.2260 0.2164 0.0274  -0.0002 -0.0251 683  TYR A OH  
974  N N   . VAL A 147 ? 0.4067 0.3168 0.3157 -0.0228 0.0131  -0.0273 684  VAL A N   
975  C CA  . VAL A 147 ? 0.3904 0.3200 0.3123 -0.0249 0.0177  -0.0266 684  VAL A CA  
976  C C   . VAL A 147 ? 0.4304 0.3441 0.3406 -0.0224 0.0203  -0.0202 684  VAL A C   
977  O O   . VAL A 147 ? 0.4299 0.3521 0.3474 -0.0142 0.0219  -0.0184 684  VAL A O   
978  C CB  . VAL A 147 ? 0.3695 0.3164 0.2994 -0.0410 0.0199  -0.0308 684  VAL A CB  
979  C CG1 . VAL A 147 ? 0.3442 0.3094 0.2838 -0.0434 0.0267  -0.0313 684  VAL A CG1 
980  C CG2 . VAL A 147 ? 0.3585 0.3265 0.3051 -0.0413 0.0152  -0.0371 684  VAL A CG2 
981  N N   . GLN A 148 ? 0.4708 0.3597 0.3621 -0.0296 0.0196  -0.0165 685  GLN A N   
982  C CA  . GLN A 148 ? 0.5129 0.3855 0.3921 -0.0267 0.0198  -0.0093 685  GLN A CA  
983  C C   . GLN A 148 ? 0.4786 0.3460 0.3609 -0.0090 0.0176  -0.0065 685  GLN A C   
984  O O   . GLN A 148 ? 0.4634 0.3391 0.3508 -0.0041 0.0179  -0.0033 685  GLN A O   
985  C CB  . GLN A 148 ? 0.5903 0.4324 0.4468 -0.0370 0.0181  -0.0049 685  GLN A CB  
986  C CG  . GLN A 148 ? 0.6416 0.4642 0.4841 -0.0325 0.0157  0.0039  685  GLN A CG  
987  C CD  . GLN A 148 ? 0.7156 0.5106 0.5343 -0.0470 0.0145  0.0098  685  GLN A CD  
988  O OE1 . GLN A 148 ? 0.7292 0.5316 0.5421 -0.0621 0.0183  0.0117  685  GLN A OE1 
989  N NE2 . GLN A 148 ? 0.7577 0.5187 0.5608 -0.0429 0.0098  0.0125  685  GLN A NE2 
990  N N   . PRO A 149 ? 0.4649 0.3202 0.3445 0.0001  0.0160  -0.0081 686  PRO A N   
991  C CA  . PRO A 149 ? 0.4382 0.2934 0.3237 0.0161  0.0159  -0.0058 686  PRO A CA  
992  C C   . PRO A 149 ? 0.4107 0.2921 0.3144 0.0210  0.0178  -0.0068 686  PRO A C   
993  O O   . PRO A 149 ? 0.4021 0.2886 0.3122 0.0278  0.0175  -0.0031 686  PRO A O   
994  C CB  . PRO A 149 ? 0.4430 0.2836 0.3211 0.0224  0.0162  -0.0098 686  PRO A CB  
995  C CG  . PRO A 149 ? 0.4692 0.2912 0.3317 0.0101  0.0142  -0.0122 686  PRO A CG  
996  C CD  . PRO A 149 ? 0.4743 0.3148 0.3437 -0.0042 0.0145  -0.0126 686  PRO A CD  
997  N N   . VAL A 150 ? 0.3976 0.2950 0.3102 0.0174  0.0187  -0.0115 687  VAL A N   
998  C CA  . VAL A 150 ? 0.3628 0.2801 0.2910 0.0225  0.0199  -0.0123 687  VAL A CA  
999  C C   . VAL A 150 ? 0.3490 0.2761 0.2825 0.0188  0.0209  -0.0110 687  VAL A C   
1000 O O   . VAL A 150 ? 0.3437 0.2769 0.2843 0.0245  0.0209  -0.0090 687  VAL A O   
1001 C CB  . VAL A 150 ? 0.3508 0.2810 0.2868 0.0202  0.0188  -0.0172 687  VAL A CB  
1002 C CG1 . VAL A 150 ? 0.3402 0.2878 0.2918 0.0243  0.0195  -0.0180 687  VAL A CG1 
1003 C CG2 . VAL A 150 ? 0.3519 0.2728 0.2803 0.0251  0.0172  -0.0180 687  VAL A CG2 
1004 N N   . GLN A 151 ? 0.3512 0.2802 0.2801 0.0077  0.0220  -0.0125 688  GLN A N   
1005 C CA  . GLN A 151 ? 0.3477 0.2851 0.2772 0.0028  0.0240  -0.0123 688  GLN A CA  
1006 C C   . GLN A 151 ? 0.3597 0.2846 0.2795 0.0063  0.0209  -0.0055 688  GLN A C   
1007 O O   . GLN A 151 ? 0.3635 0.2963 0.2863 0.0070  0.0205  -0.0052 688  GLN A O   
1008 C CB  . GLN A 151 ? 0.3594 0.3009 0.2833 -0.0113 0.0276  -0.0150 688  GLN A CB  
1009 C CG  . GLN A 151 ? 0.3471 0.3090 0.2872 -0.0141 0.0301  -0.0228 688  GLN A CG  
1010 C CD  . GLN A 151 ? 0.3511 0.3225 0.2896 -0.0292 0.0353  -0.0264 688  GLN A CD  
1011 O OE1 . GLN A 151 ? 0.3659 0.3222 0.2867 -0.0397 0.0362  -0.0219 688  GLN A OE1 
1012 N NE2 . GLN A 151 ? 0.3298 0.3264 0.2874 -0.0304 0.0388  -0.0343 688  GLN A NE2 
1013 N N   . LEU A 152 ? 0.3768 0.2819 0.2854 0.0092  0.0177  -0.0006 689  LEU A N   
1014 C CA  . LEU A 152 ? 0.4029 0.2977 0.3057 0.0153  0.0128  0.0062  689  LEU A CA  
1015 C C   . LEU A 152 ? 0.4025 0.3087 0.3214 0.0274  0.0118  0.0063  689  LEU A C   
1016 O O   . LEU A 152 ? 0.4027 0.3140 0.3249 0.0301  0.0080  0.0098  689  LEU A O   
1017 C CB  . LEU A 152 ? 0.4371 0.3057 0.3250 0.0174  0.0095  0.0108  689  LEU A CB  
1018 C CG  . LEU A 152 ? 0.4719 0.3233 0.3399 0.0035  0.0094  0.0132  689  LEU A CG  
1019 C CD1 . LEU A 152 ? 0.5003 0.3209 0.3537 0.0076  0.0053  0.0173  689  LEU A CD1 
1020 C CD2 . LEU A 152 ? 0.4828 0.3356 0.3401 -0.0051 0.0078  0.0180  689  LEU A CD2 
1021 N N   . ARG A 153 ? 0.3948 0.3053 0.3228 0.0334  0.0150  0.0029  690  ARG A N   
1022 C CA  . ARG A 153 ? 0.3960 0.3182 0.3387 0.0423  0.0158  0.0032  690  ARG A CA  
1023 C C   . ARG A 153 ? 0.3568 0.2953 0.3094 0.0385  0.0160  0.0014  690  ARG A C   
1024 O O   . ARG A 153 ? 0.3273 0.2744 0.2899 0.0422  0.0144  0.0034  690  ARG A O   
1025 C CB  . ARG A 153 ? 0.4183 0.3399 0.3636 0.0472  0.0200  0.0002  690  ARG A CB  
1026 C CG  . ARG A 153 ? 0.4732 0.3763 0.4065 0.0509  0.0204  -0.0002 690  ARG A CG  
1027 C CD  . ARG A 153 ? 0.4939 0.3955 0.4323 0.0628  0.0231  0.0006  690  ARG A CD  
1028 N NE  . ARG A 153 ? 0.5281 0.4106 0.4529 0.0660  0.0250  -0.0026 690  ARG A NE  
1029 C CZ  . ARG A 153 ? 0.5716 0.4342 0.4867 0.0699  0.0225  -0.0016 690  ARG A CZ  
1030 N NH1 . ARG A 153 ? 0.5825 0.4426 0.4999 0.0714  0.0172  0.0040  690  ARG A NH1 
1031 N NH2 . ARG A 153 ? 0.6036 0.4463 0.5047 0.0722  0.0246  -0.0060 690  ARG A NH2 
1032 N N   . ILE A 154 ? 0.3474 0.2908 0.2986 0.0311  0.0180  -0.0031 691  ILE A N   
1033 C CA  . ILE A 154 ? 0.3248 0.2803 0.2835 0.0280  0.0186  -0.0065 691  ILE A CA  
1034 C C   . ILE A 154 ? 0.3368 0.2918 0.2887 0.0238  0.0151  -0.0041 691  ILE A C   
1035 O O   . ILE A 154 ? 0.3337 0.2958 0.2921 0.0243  0.0130  -0.0045 691  ILE A O   
1036 C CB  . ILE A 154 ? 0.2985 0.2605 0.2588 0.0226  0.0222  -0.0130 691  ILE A CB  
1037 C CG1 . ILE A 154 ? 0.2795 0.2424 0.2462 0.0272  0.0229  -0.0146 691  ILE A CG1 
1038 C CG2 . ILE A 154 ? 0.2350 0.2065 0.2013 0.0204  0.0236  -0.0182 691  ILE A CG2 
1039 C CD1 . ILE A 154 ? 0.2813 0.2527 0.2524 0.0231  0.0246  -0.0205 691  ILE A CD1 
1040 N N   . LEU A 155 ? 0.3505 0.2958 0.2872 0.0185  0.0136  -0.0012 692  LEU A N   
1041 C CA  . LEU A 155 ? 0.3618 0.3041 0.2875 0.0143  0.0086  0.0025  692  LEU A CA  
1042 C C   . LEU A 155 ? 0.3398 0.2823 0.2727 0.0228  0.0014  0.0085  692  LEU A C   
1043 O O   . LEU A 155 ? 0.3367 0.2849 0.2692 0.0210  -0.0041 0.0098  692  LEU A O   
1044 C CB  . LEU A 155 ? 0.3941 0.3218 0.2989 0.0063  0.0080  0.0064  692  LEU A CB  
1045 C CG  . LEU A 155 ? 0.4102 0.3428 0.3092 -0.0050 0.0160  0.0002  692  LEU A CG  
1046 C CD1 . LEU A 155 ? 0.4388 0.3551 0.3165 -0.0149 0.0162  0.0052  692  LEU A CD1 
1047 C CD2 . LEU A 155 ? 0.4103 0.3560 0.3092 -0.0105 0.0191  -0.0061 692  LEU A CD2 
1048 N N   . ASN A 156 ? 0.3220 0.2601 0.2622 0.0322  0.0014  0.0112  693  ASN A N   
1049 C CA  . ASN A 156 ? 0.3199 0.2639 0.2729 0.0416  -0.0036 0.0154  693  ASN A CA  
1050 C C   . ASN A 156 ? 0.2965 0.2586 0.2670 0.0414  -0.0020 0.0121  693  ASN A C   
1051 O O   . ASN A 156 ? 0.2602 0.2326 0.2401 0.0427  -0.0081 0.0147  693  ASN A O   
1052 C CB  . ASN A 156 ? 0.3236 0.2595 0.2805 0.0519  -0.0011 0.0168  693  ASN A CB  
1053 C CG  . ASN A 156 ? 0.3408 0.2848 0.3130 0.0629  -0.0053 0.0206  693  ASN A CG  
1054 O OD1 . ASN A 156 ? 0.3755 0.3173 0.3455 0.0653  -0.0144 0.0260  693  ASN A OD1 
1055 N ND2 . ASN A 156 ? 0.3173 0.2718 0.3051 0.0696  0.0011  0.0181  693  ASN A ND2 
1056 N N   . VAL A 157 ? 0.2471 0.2128 0.2223 0.0393  0.0050  0.0069  694  VAL A N   
1057 C CA  . VAL A 157 ? 0.3219 0.2996 0.3106 0.0377  0.0064  0.0042  694  VAL A CA  
1058 C C   . VAL A 157 ? 0.3490 0.3306 0.3338 0.0297  0.0020  0.0016  694  VAL A C   
1059 O O   . VAL A 157 ? 0.3250 0.3158 0.3196 0.0281  -0.0021 0.0022  694  VAL A O   
1060 C CB  . VAL A 157 ? 0.3110 0.2870 0.3018 0.0378  0.0132  0.0002  694  VAL A CB  
1061 C CG1 . VAL A 157 ? 0.2228 0.2053 0.2236 0.0347  0.0140  -0.0023 694  VAL A CG1 
1062 C CG2 . VAL A 157 ? 0.2272 0.1999 0.2200 0.0451  0.0172  0.0026  694  VAL A CG2 
1063 N N   . PHE A 158 ? 0.2473 0.2227 0.2176 0.0235  0.0032  -0.0021 695  PHE A N   
1064 C CA  . PHE A 158 ? 0.2667 0.2440 0.2285 0.0155  0.0000  -0.0058 695  PHE A CA  
1065 C C   . PHE A 158 ? 0.3248 0.3044 0.2835 0.0148  -0.0102 0.0001  695  PHE A C   
1066 O O   . PHE A 158 ? 0.3286 0.3144 0.2891 0.0099  -0.0153 -0.0022 695  PHE A O   
1067 C CB  . PHE A 158 ? 0.2672 0.2385 0.2116 0.0089  0.0042  -0.0099 695  PHE A CB  
1068 C CG  . PHE A 158 ? 0.2818 0.2558 0.2320 0.0088  0.0128  -0.0179 695  PHE A CG  
1069 C CD1 . PHE A 158 ? 0.2851 0.2628 0.2500 0.0128  0.0146  -0.0219 695  PHE A CD1 
1070 C CD2 . PHE A 158 ? 0.3068 0.2798 0.2482 0.0044  0.0185  -0.0210 695  PHE A CD2 
1071 C CE1 . PHE A 158 ? 0.2422 0.2217 0.2133 0.0147  0.0205  -0.0286 695  PHE A CE1 
1072 C CE2 . PHE A 158 ? 0.2609 0.2403 0.2116 0.0055  0.0252  -0.0286 695  PHE A CE2 
1073 C CZ  . PHE A 158 ? 0.2451 0.2273 0.2107 0.0118  0.0255  -0.0324 695  PHE A CZ  
1074 N N   . ARG A 159 ? 0.3617 0.3355 0.3158 0.0199  -0.0144 0.0077  696  ARG A N   
1075 C CA  . ARG A 159 ? 0.3841 0.3595 0.3355 0.0212  -0.0263 0.0144  696  ARG A CA  
1076 C C   . ARG A 159 ? 0.3584 0.3508 0.3346 0.0266  -0.0307 0.0159  696  ARG A C   
1077 O O   . ARG A 159 ? 0.3528 0.3542 0.3317 0.0232  -0.0407 0.0174  696  ARG A O   
1078 C CB  . ARG A 159 ? 0.4293 0.3904 0.3703 0.0274  -0.0297 0.0222  696  ARG A CB  
1079 C CG  . ARG A 159 ? 0.4866 0.4475 0.4252 0.0314  -0.0440 0.0306  696  ARG A CG  
1080 C CD  . ARG A 159 ? 0.5416 0.4827 0.4681 0.0385  -0.0478 0.0385  696  ARG A CD  
1081 N NE  . ARG A 159 ? 0.5659 0.5075 0.5107 0.0514  -0.0425 0.0383  696  ARG A NE  
1082 C CZ  . ARG A 159 ? 0.5980 0.5207 0.5356 0.0598  -0.0444 0.0432  696  ARG A CZ  
1083 N NH1 . ARG A 159 ? 0.5919 0.5155 0.5450 0.0714  -0.0384 0.0409  696  ARG A NH1 
1084 N NH2 . ARG A 159 ? 0.6295 0.5303 0.5420 0.0560  -0.0520 0.0502  696  ARG A NH2 
1085 N N   . HIS A 160 ? 0.3329 0.3308 0.3269 0.0338  -0.0235 0.0154  697  HIS A N   
1086 C CA  . HIS A 160 ? 0.3097 0.3263 0.3286 0.0368  -0.0246 0.0161  697  HIS A CA  
1087 C C   . HIS A 160 ? 0.2882 0.3118 0.3111 0.0261  -0.0244 0.0106  697  HIS A C   
1088 O O   . HIS A 160 ? 0.2745 0.3135 0.3125 0.0230  -0.0305 0.0113  697  HIS A O   
1089 C CB  . HIS A 160 ? 0.3262 0.3447 0.3575 0.0451  -0.0145 0.0162  697  HIS A CB  
1090 C CG  . HIS A 160 ? 0.3654 0.4047 0.4226 0.0483  -0.0132 0.0175  697  HIS A CG  
1091 N ND1 . HIS A 160 ? 0.3806 0.4296 0.4528 0.0599  -0.0136 0.0211  697  HIS A ND1 
1092 C CD2 . HIS A 160 ? 0.3663 0.4186 0.4376 0.0411  -0.0104 0.0154  697  HIS A CD2 
1093 C CE1 . HIS A 160 ? 0.3670 0.4380 0.4632 0.0591  -0.0103 0.0208  697  HIS A CE1 
1094 N NE2 . HIS A 160 ? 0.3591 0.4316 0.4543 0.0467  -0.0086 0.0180  697  HIS A NE2 
1095 N N   . TRP A 161 ? 0.2896 0.3019 0.2998 0.0205  -0.0180 0.0045  698  TRP A N   
1096 C CA  . TRP A 161 ? 0.2743 0.2876 0.2866 0.0117  -0.0169 -0.0019 698  TRP A CA  
1097 C C   . TRP A 161 ? 0.2869 0.3035 0.2913 0.0032  -0.0273 -0.0039 698  TRP A C   
1098 O O   . TRP A 161 ? 0.2820 0.3090 0.2986 -0.0024 -0.0327 -0.0047 698  TRP A O   
1099 C CB  . TRP A 161 ? 0.2679 0.2681 0.2688 0.0106  -0.0084 -0.0084 698  TRP A CB  
1100 C CG  . TRP A 161 ? 0.2717 0.2677 0.2764 0.0055  -0.0052 -0.0151 698  TRP A CG  
1101 C CD1 . TRP A 161 ? 0.2676 0.2677 0.2813 -0.0011 -0.0090 -0.0165 698  TRP A CD1 
1102 C CD2 . TRP A 161 ? 0.2809 0.2664 0.2809 0.0070  0.0018  -0.0213 698  TRP A CD2 
1103 N NE1 . TRP A 161 ? 0.2586 0.2470 0.2709 -0.0039 -0.0046 -0.0230 698  TRP A NE1 
1104 C CE2 . TRP A 161 ? 0.3057 0.2858 0.3105 0.0023  0.0017  -0.0260 698  TRP A CE2 
1105 C CE3 . TRP A 161 ? 0.2541 0.2348 0.2476 0.0117  0.0074  -0.0235 698  TRP A CE3 
1106 C CZ2 . TRP A 161 ? 0.3072 0.2754 0.3103 0.0045  0.0066  -0.0325 698  TRP A CZ2 
1107 C CZ3 . TRP A 161 ? 0.2567 0.2306 0.2514 0.0135  0.0122  -0.0301 698  TRP A CZ3 
1108 C CH2 . TRP A 161 ? 0.2781 0.2449 0.2774 0.0111  0.0115  -0.0344 698  TRP A CH2 
1109 N N   . VAL A 162 ? 0.3000 0.3077 0.2824 0.0007  -0.0305 -0.0045 699  VAL A N   
1110 C CA  . VAL A 162 ? 0.3267 0.3348 0.2951 -0.0084 -0.0405 -0.0067 699  VAL A CA  
1111 C C   . VAL A 162 ? 0.3032 0.3245 0.2812 -0.0065 -0.0546 0.0014  699  VAL A C   
1112 O O   . VAL A 162 ? 0.3177 0.3444 0.2911 -0.0148 -0.0652 -0.0004 699  VAL A O   
1113 C CB  . VAL A 162 ? 0.3530 0.3476 0.2921 -0.0127 -0.0384 -0.0091 699  VAL A CB  
1114 C CG1 . VAL A 162 ? 0.3067 0.2935 0.2412 -0.0143 -0.0250 -0.0188 699  VAL A CG1 
1115 C CG2 . VAL A 162 ? 0.3148 0.3038 0.2468 -0.0059 -0.0399 0.0004  699  VAL A CG2 
1116 N N   . GLU A 163 ? 0.2952 0.3221 0.2868 0.0048  -0.0555 0.0096  700  GLU A N   
1117 C CA  . GLU A 163 ? 0.3831 0.4254 0.3890 0.0094  -0.0693 0.0170  700  GLU A CA  
1118 C C   . GLU A 163 ? 0.3652 0.4304 0.4014 0.0069  -0.0709 0.0152  700  GLU A C   
1119 O O   . GLU A 163 ? 0.3628 0.4431 0.4074 0.0022  -0.0843 0.0166  700  GLU A O   
1120 C CB  . GLU A 163 ? 0.3765 0.4161 0.3883 0.0240  -0.0691 0.0250  700  GLU A CB  
1121 C CG  . GLU A 163 ? 0.3949 0.4516 0.4252 0.0321  -0.0837 0.0324  700  GLU A CG  
1122 C CD  . GLU A 163 ? 0.4420 0.4936 0.4513 0.0268  -0.1012 0.0369  700  GLU A CD  
1123 O OE1 . GLU A 163 ? 0.4692 0.4996 0.4526 0.0292  -0.1046 0.0424  700  GLU A OE1 
1124 O OE2 . GLU A 163 ? 0.4580 0.5257 0.4748 0.0187  -0.1120 0.0352  700  GLU A OE2 
1125 N N   . HIS A 164 ? 0.2737 0.3422 0.3259 0.0088  -0.0578 0.0125  701  HIS A N   
1126 C CA  . HIS A 164 ? 0.2973 0.3881 0.3792 0.0061  -0.0573 0.0125  701  HIS A CA  
1127 C C   . HIS A 164 ? 0.3045 0.3903 0.3862 -0.0065 -0.0507 0.0056  701  HIS A C   
1128 O O   . HIS A 164 ? 0.2608 0.3634 0.3649 -0.0125 -0.0503 0.0056  701  HIS A O   
1129 C CB  . HIS A 164 ? 0.2762 0.3766 0.3783 0.0186  -0.0474 0.0166  701  HIS A CB  
1130 C CG  . HIS A 164 ? 0.2958 0.3995 0.4012 0.0329  -0.0535 0.0229  701  HIS A CG  
1131 N ND1 . HIS A 164 ? 0.3094 0.4382 0.4403 0.0392  -0.0634 0.0271  701  HIS A ND1 
1132 C CD2 . HIS A 164 ? 0.3080 0.3921 0.3952 0.0425  -0.0515 0.0255  701  HIS A CD2 
1133 C CE1 . HIS A 164 ? 0.3182 0.4402 0.4456 0.0537  -0.0675 0.0322  701  HIS A CE1 
1134 N NE2 . HIS A 164 ? 0.3145 0.4079 0.4142 0.0549  -0.0602 0.0314  701  HIS A NE2 
1135 N N   . HIS A 165 ? 0.4308 0.2780 0.3138 -0.0035 -0.0120 -0.0050 702  HIS A N   
1136 C CA  . HIS A 165 ? 0.4288 0.2765 0.3039 -0.0025 -0.0070 -0.0101 702  HIS A CA  
1137 C C   . HIS A 165 ? 0.4601 0.2886 0.3127 -0.0102 0.0052  -0.0126 702  HIS A C   
1138 O O   . HIS A 165 ? 0.4164 0.2461 0.2723 -0.0081 0.0144  -0.0214 702  HIS A O   
1139 C CB  . HIS A 165 ? 0.3974 0.2663 0.3008 0.0076  -0.0037 -0.0191 702  HIS A CB  
1140 C CG  . HIS A 165 ? 0.3600 0.2524 0.2860 0.0155  -0.0153 -0.0180 702  HIS A CG  
1141 N ND1 . HIS A 165 ? 0.3415 0.2444 0.2642 0.0163  -0.0265 -0.0130 702  HIS A ND1 
1142 C CD2 . HIS A 165 ? 0.3407 0.2498 0.2933 0.0228  -0.0178 -0.0217 702  HIS A CD2 
1143 C CE1 . HIS A 165 ? 0.3183 0.2451 0.2640 0.0237  -0.0347 -0.0142 702  HIS A CE1 
1144 N NE2 . HIS A 165 ? 0.3209 0.2518 0.2854 0.0281  -0.0300 -0.0201 702  HIS A NE2 
1145 N N   . PHE A 166 ? 0.4868 0.2986 0.3164 -0.0195 0.0048  -0.0054 703  PHE A N   
1146 C CA  . PHE A 166 ? 0.5142 0.3112 0.3212 -0.0274 0.0164  -0.0080 703  PHE A CA  
1147 C C   . PHE A 166 ? 0.5176 0.3087 0.3076 -0.0287 0.0169  -0.0129 703  PHE A C   
1148 O O   . PHE A 166 ? 0.5311 0.3138 0.3062 -0.0334 0.0272  -0.0191 703  PHE A O   
1149 C CB  . PHE A 166 ? 0.5488 0.3317 0.3343 -0.0377 0.0145  0.0024  703  PHE A CB  
1150 C CG  . PHE A 166 ? 0.5828 0.3561 0.3496 -0.0460 0.0281  -0.0003 703  PHE A CG  
1151 C CD1 . PHE A 166 ? 0.5837 0.3612 0.3642 -0.0462 0.0390  -0.0034 703  PHE A CD1 
1152 C CD2 . PHE A 166 ? 0.6139 0.3760 0.3502 -0.0535 0.0299  -0.0003 703  PHE A CD2 
1153 C CE1 . PHE A 166 ? 0.6097 0.3816 0.3731 -0.0543 0.0521  -0.0059 703  PHE A CE1 
1154 C CE2 . PHE A 166 ? 0.6373 0.3946 0.3564 -0.0611 0.0428  -0.0039 703  PHE A CE2 
1155 C CZ  . PHE A 166 ? 0.6355 0.3983 0.3678 -0.0618 0.0541  -0.0064 703  PHE A CZ  
1156 N N   . TYR A 167 ? 0.5037 0.3004 0.2970 -0.0248 0.0056  -0.0105 704  TYR A N   
1157 C CA  . TYR A 167 ? 0.5158 0.3076 0.2982 -0.0254 0.0045  -0.0151 704  TYR A CA  
1158 C C   . TYR A 167 ? 0.5166 0.3147 0.3146 -0.0205 0.0141  -0.0276 704  TYR A C   
1159 O O   . TYR A 167 ? 0.5377 0.3285 0.3259 -0.0223 0.0164  -0.0345 704  TYR A O   
1160 C CB  . TYR A 167 ? 0.5156 0.3142 0.3019 -0.0225 -0.0106 -0.0083 704  TYR A CB  
1161 C CG  . TYR A 167 ? 0.4935 0.3136 0.3085 -0.0142 -0.0158 -0.0069 704  TYR A CG  
1162 C CD1 . TYR A 167 ? 0.4625 0.2971 0.2992 -0.0075 -0.0130 -0.0139 704  TYR A CD1 
1163 C CD2 . TYR A 167 ? 0.4752 0.3024 0.2962 -0.0132 -0.0242 0.0007  704  TYR A CD2 
1164 C CE1 . TYR A 167 ? 0.4356 0.2929 0.2978 0.0001  -0.0177 -0.0132 704  TYR A CE1 
1165 C CE2 . TYR A 167 ? 0.4448 0.2950 0.2927 -0.0051 -0.0291 0.0000  704  TYR A CE2 
1166 C CZ  . TYR A 167 ? 0.4242 0.2902 0.2919 0.0015  -0.0255 -0.0068 704  TYR A CZ  
1167 O OH  . TYR A 167 ? 0.3987 0.2903 0.2925 0.0095  -0.0303 -0.0079 704  TYR A OH  
1168 N N   . ASP A 168 ? 0.4989 0.3105 0.3223 -0.0139 0.0190  -0.0314 705  ASP A N   
1169 C CA  . ASP A 168 ? 0.4980 0.3144 0.3365 -0.0095 0.0291  -0.0436 705  ASP A CA  
1170 C C   . ASP A 168 ? 0.5343 0.3380 0.3567 -0.0155 0.0424  -0.0514 705  ASP A C   
1171 O O   . ASP A 168 ? 0.5348 0.3367 0.3593 -0.0144 0.0483  -0.0625 705  ASP A O   
1172 C CB  . ASP A 168 ? 0.4751 0.3074 0.3423 -0.0019 0.0326  -0.0460 705  ASP A CB  
1173 C CG  . ASP A 168 ? 0.4364 0.2876 0.3242 0.0056  0.0216  -0.0428 705  ASP A CG  
1174 O OD1 . ASP A 168 ? 0.4316 0.2840 0.3136 0.0048  0.0118  -0.0386 705  ASP A OD1 
1175 O OD2 . ASP A 168 ? 0.4098 0.2762 0.3207 0.0122  0.0226  -0.0446 705  ASP A OD2 
1176 N N   . PHE A 169 ? 0.5581 0.3542 0.3653 -0.0221 0.0467  -0.0459 706  PHE A N   
1177 C CA  . PHE A 169 ? 0.6035 0.3914 0.3945 -0.0288 0.0597  -0.0520 706  PHE A CA  
1178 C C   . PHE A 169 ? 0.6406 0.4165 0.4013 -0.0363 0.0576  -0.0521 706  PHE A C   
1179 O O   . PHE A 169 ? 0.6574 0.4298 0.4057 -0.0405 0.0680  -0.0615 706  PHE A O   
1180 C CB  . PHE A 169 ? 0.6172 0.4049 0.4085 -0.0331 0.0651  -0.0447 706  PHE A CB  
1181 C CG  . PHE A 169 ? 0.5959 0.3955 0.4188 -0.0252 0.0666  -0.0459 706  PHE A CG  
1182 C CD1 . PHE A 169 ? 0.5983 0.4035 0.4375 -0.0213 0.0789  -0.0570 706  PHE A CD1 
1183 C CD2 . PHE A 169 ? 0.5699 0.3761 0.4072 -0.0210 0.0552  -0.0370 706  PHE A CD2 
1184 C CE1 . PHE A 169 ? 0.5773 0.3937 0.4462 -0.0134 0.0799  -0.0588 706  PHE A CE1 
1185 C CE2 . PHE A 169 ? 0.5527 0.3718 0.4203 -0.0129 0.0559  -0.0398 706  PHE A CE2 
1186 C CZ  . PHE A 169 ? 0.5595 0.3832 0.4426 -0.0090 0.0683  -0.0504 706  PHE A CZ  
1187 N N   . GLU A 170 ? 0.6594 0.4304 0.4088 -0.0377 0.0442  -0.0428 707  GLU A N   
1188 C CA  . GLU A 170 ? 0.6941 0.4542 0.4173 -0.0434 0.0407  -0.0442 707  GLU A CA  
1189 C C   . GLU A 170 ? 0.7006 0.4615 0.4313 -0.0387 0.0396  -0.0568 707  GLU A C   
1190 O O   . GLU A 170 ? 0.7280 0.4827 0.4427 -0.0423 0.0433  -0.0661 707  GLU A O   
1191 C CB  . GLU A 170 ? 0.7033 0.4575 0.4141 -0.0459 0.0260  -0.0306 707  GLU A CB  
1192 C CG  . GLU A 170 ? 0.7280 0.4780 0.4271 -0.0524 0.0253  -0.0183 707  GLU A CG  
1193 C CD  . GLU A 170 ? 0.7307 0.4779 0.4271 -0.0525 0.0096  -0.0053 707  GLU A CD  
1194 O OE1 . GLU A 170 ? 0.7213 0.4707 0.4232 -0.0479 -0.0002 -0.0053 707  GLU A OE1 
1195 O OE2 . GLU A 170 ? 0.7395 0.4830 0.4297 -0.0574 0.0065  0.0051  707  GLU A OE2 
1196 N N   . ARG A 171 ? 0.6736 0.4436 0.4298 -0.0308 0.0338  -0.0575 708  ARG A N   
1197 C CA  . ARG A 171 ? 0.6771 0.4480 0.4444 -0.0267 0.0301  -0.0674 708  ARG A CA  
1198 C C   . ARG A 171 ? 0.6803 0.4542 0.4593 -0.0243 0.0434  -0.0833 708  ARG A C   
1199 O O   . ARG A 171 ? 0.7041 0.4746 0.4844 -0.0235 0.0427  -0.0950 708  ARG A O   
1200 C CB  . ARG A 171 ? 0.6661 0.4477 0.4564 -0.0202 0.0184  -0.0605 708  ARG A CB  
1201 C CG  . ARG A 171 ? 0.6735 0.4545 0.4550 -0.0219 0.0045  -0.0457 708  ARG A CG  
1202 C CD  . ARG A 171 ? 0.6565 0.4544 0.4624 -0.0156 -0.0038 -0.0385 708  ARG A CD  
1203 N NE  . ARG A 171 ? 0.6642 0.4641 0.4631 -0.0171 -0.0168 -0.0250 708  ARG A NE  
1204 C CZ  . ARG A 171 ? 0.6414 0.4587 0.4581 -0.0126 -0.0251 -0.0174 708  ARG A CZ  
1205 N NH1 . ARG A 171 ? 0.6241 0.4582 0.4661 -0.0063 -0.0218 -0.0215 708  ARG A NH1 
1206 N NH2 . ARG A 171 ? 0.6309 0.4501 0.4404 -0.0144 -0.0367 -0.0062 708  ARG A NH2 
1207 N N   . ASP A 172 ? 0.6690 0.4494 0.4582 -0.0230 0.0546  -0.0844 709  ASP A N   
1208 C CA  . ASP A 172 ? 0.6635 0.4479 0.4664 -0.0203 0.0675  -0.0990 709  ASP A CA  
1209 C C   . ASP A 172 ? 0.6939 0.4768 0.4827 -0.0264 0.0817  -0.1004 709  ASP A C   
1210 O O   . ASP A 172 ? 0.6759 0.4622 0.4685 -0.0271 0.0843  -0.0909 709  ASP A O   
1211 C CB  . ASP A 172 ? 0.6252 0.4214 0.4593 -0.0120 0.0671  -0.0990 709  ASP A CB  
1212 C CG  . ASP A 172 ? 0.5988 0.3980 0.4504 -0.0080 0.0763  -0.1150 709  ASP A CG  
1213 O OD1 . ASP A 172 ? 0.6134 0.4079 0.4538 -0.0119 0.0873  -0.1261 709  ASP A OD1 
1214 O OD2 . ASP A 172 ? 0.5670 0.3746 0.4436 -0.0011 0.0724  -0.1168 709  ASP A OD2 
1215 N N   . LEU A 173 ? 0.7288 0.5082 0.5026 -0.0309 0.0903  -0.1124 710  LEU A N   
1216 C CA  . LEU A 173 ? 0.7519 0.5323 0.5098 -0.0383 0.1040  -0.1133 710  LEU A CA  
1217 C C   . LEU A 173 ? 0.7448 0.5333 0.5224 -0.0354 0.1180  -0.1221 710  LEU A C   
1218 O O   . LEU A 173 ? 0.7484 0.5399 0.5224 -0.0401 0.1267  -0.1159 710  LEU A O   
1219 C CB  . LEU A 173 ? 0.7776 0.5547 0.5100 -0.0447 0.1078  -0.1232 710  LEU A CB  
1220 C CG  . LEU A 173 ? 0.8019 0.5707 0.5081 -0.0503 0.0970  -0.1130 710  LEU A CG  
1221 C CD1 . LEU A 173 ? 0.8310 0.6008 0.5086 -0.0592 0.1057  -0.1195 710  LEU A CD1 
1222 C CD2 . LEU A 173 ? 0.8037 0.5696 0.5076 -0.0524 0.0898  -0.0924 710  LEU A CD2 
1223 N N   . GLU A 174 ? 0.7355 0.5274 0.5347 -0.0281 0.1197  -0.1361 711  GLU A N   
1224 C CA  . GLU A 174 ? 0.7189 0.5181 0.5396 -0.0243 0.1318  -0.1440 711  GLU A CA  
1225 C C   . GLU A 174 ? 0.6475 0.4510 0.4867 -0.0199 0.1289  -0.1313 711  GLU A C   
1226 O O   . GLU A 174 ? 0.6478 0.4564 0.4985 -0.0195 0.1392  -0.1321 711  GLU A O   
1227 C CB  . GLU A 174 ? 0.7372 0.5396 0.5798 -0.0171 0.1314  -0.1604 711  GLU A CB  
1228 C CG  . GLU A 174 ? 0.7646 0.5828 0.6252 -0.0153 0.1397  -0.1673 711  GLU A CG  
1229 C CD  . GLU A 174 ? 0.7661 0.5967 0.6623 -0.0061 0.1349  -0.1645 711  GLU A CD  
1230 O OE1 . GLU A 174 ? 0.7730 0.6039 0.6836 0.0002  0.1231  -0.1608 711  GLU A OE1 
1231 O OE2 . GLU A 174 ? 0.7525 0.5927 0.6607 -0.0057 0.1427  -0.1655 711  GLU A OE2 
1232 N N   . LEU A 175 ? 0.5941 0.3970 0.4375 -0.0165 0.1146  -0.1201 712  LEU A N   
1233 C CA  . LEU A 175 ? 0.5425 0.3519 0.4036 -0.0119 0.1105  -0.1092 712  LEU A CA  
1234 C C   . LEU A 175 ? 0.5244 0.3320 0.3745 -0.0186 0.1152  -0.0987 712  LEU A C   
1235 O O   . LEU A 175 ? 0.4946 0.3079 0.3623 -0.0161 0.1207  -0.0972 712  LEU A O   
1236 C CB  . LEU A 175 ? 0.5171 0.3282 0.3811 -0.0082 0.0939  -0.0993 712  LEU A CB  
1237 C CG  . LEU A 175 ? 0.4601 0.2818 0.3451 -0.0020 0.0876  -0.0903 712  LEU A CG  
1238 C CD1 . LEU A 175 ? 0.4218 0.2547 0.3368 0.0071  0.0916  -0.0995 712  LEU A CD1 
1239 C CD2 . LEU A 175 ? 0.4504 0.2745 0.3316 -0.0009 0.0716  -0.0796 712  LEU A CD2 
1240 N N   . LEU A 176 ? 0.5532 0.3530 0.3751 -0.0274 0.1122  -0.0910 713  LEU A N   
1241 C CA  . LEU A 176 ? 0.5788 0.3764 0.3891 -0.0354 0.1149  -0.0791 713  LEU A CA  
1242 C C   . LEU A 176 ? 0.5993 0.4005 0.4105 -0.0398 0.1313  -0.0854 713  LEU A C   
1243 O O   . LEU A 176 ? 0.5841 0.3886 0.4072 -0.0411 0.1347  -0.0783 713  LEU A O   
1244 C CB  . LEU A 176 ? 0.6003 0.3890 0.3787 -0.0444 0.1084  -0.0704 713  LEU A CB  
1245 C CG  . LEU A 176 ? 0.6132 0.3983 0.3765 -0.0542 0.1079  -0.0553 713  LEU A CG  
1246 C CD1 . LEU A 176 ? 0.5897 0.3775 0.3754 -0.0498 0.0994  -0.0442 713  LEU A CD1 
1247 C CD2 . LEU A 176 ? 0.6277 0.4038 0.3600 -0.0617 0.0998  -0.0479 713  LEU A CD2 
1248 N N   . GLU A 177 ? 0.6196 0.4214 0.4204 -0.0421 0.1410  -0.0994 714  GLU A N   
1249 C CA  . GLU A 177 ? 0.6444 0.4520 0.4447 -0.0470 0.1572  -0.1063 714  GLU A CA  
1250 C C   . GLU A 177 ? 0.5949 0.4090 0.4277 -0.0392 0.1634  -0.1112 714  GLU A C   
1251 O O   . GLU A 177 ? 0.6129 0.4315 0.4509 -0.0434 0.1731  -0.1083 714  GLU A O   
1252 C CB  . GLU A 177 ? 0.6996 0.5089 0.4855 -0.0493 0.1654  -0.1235 714  GLU A CB  
1253 C CG  . GLU A 177 ? 0.7631 0.5698 0.5142 -0.0596 0.1644  -0.1199 714  GLU A CG  
1254 C CD  . GLU A 177 ? 0.8211 0.6314 0.5616 -0.0601 0.1710  -0.1398 714  GLU A CD  
1255 O OE1 . GLU A 177 ? 0.8339 0.6506 0.5918 -0.0556 0.1806  -0.1555 714  GLU A OE1 
1256 O OE2 . GLU A 177 ? 0.8518 0.6589 0.5679 -0.0647 0.1658  -0.1406 714  GLU A OE2 
1257 N N   . ARG A 178 ? 0.5301 0.3455 0.3855 -0.0282 0.1576  -0.1182 715  ARG A N   
1258 C CA  . ARG A 178 ? 0.4886 0.3106 0.3755 -0.0201 0.1622  -0.1224 715  ARG A CA  
1259 C C   . ARG A 178 ? 0.4822 0.3060 0.3804 -0.0200 0.1572  -0.1074 715  ARG A C   
1260 O O   . ARG A 178 ? 0.4984 0.3263 0.4115 -0.0203 0.1654  -0.1070 715  ARG A O   
1261 C CB  . ARG A 178 ? 0.4774 0.3019 0.3850 -0.0089 0.1550  -0.1308 715  ARG A CB  
1262 C CG  . ARG A 178 ? 0.4572 0.2883 0.3703 -0.0069 0.1547  -0.1425 715  ARG A CG  
1263 C CD  . ARG A 178 ? 0.4296 0.2713 0.3678 0.0031  0.1396  -0.1409 715  ARG A CD  
1264 N NE  . ARG A 178 ? 0.4058 0.2604 0.3714 0.0098  0.1369  -0.1358 715  ARG A NE  
1265 C CZ  . ARG A 178 ? 0.3813 0.2457 0.3657 0.0177  0.1250  -0.1311 715  ARG A CZ  
1266 N NH1 . ARG A 178 ? 0.3771 0.2390 0.3578 0.0200  0.1157  -0.1306 715  ARG A NH1 
1267 N NH2 . ARG A 178 ? 0.3624 0.2393 0.3681 0.0229  0.1223  -0.1268 715  ARG A NH2 
1268 N N   . LEU A 179 ? 0.4759 0.2970 0.3688 -0.0197 0.1430  -0.0953 716  LEU A N   
1269 C CA  . LEU A 179 ? 0.4724 0.2953 0.3776 -0.0193 0.1359  -0.0819 716  LEU A CA  
1270 C C   . LEU A 179 ? 0.4995 0.3194 0.3929 -0.0306 0.1427  -0.0726 716  LEU A C   
1271 O O   . LEU A 179 ? 0.4868 0.3103 0.4002 -0.0298 0.1444  -0.0679 716  LEU A O   
1272 C CB  . LEU A 179 ? 0.4565 0.2769 0.3539 -0.0185 0.1195  -0.0715 716  LEU A CB  
1273 C CG  . LEU A 179 ? 0.4713 0.2930 0.3794 -0.0189 0.1094  -0.0579 716  LEU A CG  
1274 C CD1 . LEU A 179 ? 0.4249 0.2578 0.3700 -0.0079 0.1082  -0.0623 716  LEU A CD1 
1275 C CD2 . LEU A 179 ? 0.4507 0.2696 0.3472 -0.0191 0.0940  -0.0491 716  LEU A CD2 
1276 N N   . GLU A 180 ? 0.5368 0.3509 0.3983 -0.0415 0.1460  -0.0695 717  GLU A N   
1277 C CA  . GLU A 180 ? 0.5631 0.3765 0.4107 -0.0539 0.1522  -0.0591 717  GLU A CA  
1278 C C   . GLU A 180 ? 0.5621 0.3827 0.4210 -0.0552 0.1685  -0.0676 717  GLU A C   
1279 O O   . GLU A 180 ? 0.5681 0.3913 0.4334 -0.0616 0.1722  -0.0578 717  GLU A O   
1280 C CB  . GLU A 180 ? 0.6017 0.4100 0.4116 -0.0648 0.1524  -0.0555 717  GLU A CB  
1281 C CG  . GLU A 180 ? 0.6271 0.4273 0.4249 -0.0649 0.1361  -0.0450 717  GLU A CG  
1282 C CD  . GLU A 180 ? 0.6849 0.4799 0.4457 -0.0764 0.1358  -0.0397 717  GLU A CD  
1283 O OE1 . GLU A 180 ? 0.6917 0.4899 0.4358 -0.0798 0.1464  -0.0514 717  GLU A OE1 
1284 O OE2 . GLU A 180 ? 0.7180 0.5063 0.4672 -0.0820 0.1244  -0.0246 717  GLU A OE2 
1285 N N   . SER A 181 ? 0.5505 0.3746 0.4132 -0.0495 0.1777  -0.0856 718  SER A N   
1286 C CA  . SER A 181 ? 0.5375 0.3691 0.4144 -0.0493 0.1929  -0.0955 718  SER A CA  
1287 C C   . SER A 181 ? 0.5162 0.3507 0.4285 -0.0412 0.1908  -0.0924 718  SER A C   
1288 O O   . SER A 181 ? 0.5275 0.3663 0.4502 -0.0456 0.1988  -0.0884 718  SER A O   
1289 C CB  . SER A 181 ? 0.5325 0.3664 0.4102 -0.0435 0.2007  -0.1166 718  SER A CB  
1290 O OG  . SER A 181 ? 0.5369 0.3780 0.4321 -0.0417 0.2147  -0.1274 718  SER A OG  
1291 N N   . PHE A 182 ? 0.4915 0.3250 0.4230 -0.0296 0.1795  -0.0940 719  PHE A N   
1292 C CA  . PHE A 182 ? 0.4862 0.3247 0.4530 -0.0203 0.1771  -0.0940 719  PHE A CA  
1293 C C   . PHE A 182 ? 0.4873 0.3250 0.4615 -0.0256 0.1704  -0.0769 719  PHE A C   
1294 O O   . PHE A 182 ? 0.4717 0.3133 0.4683 -0.0248 0.1752  -0.0756 719  PHE A O   
1295 C CB  . PHE A 182 ? 0.4707 0.3120 0.4548 -0.0072 0.1658  -0.0992 719  PHE A CB  
1296 C CG  . PHE A 182 ? 0.4634 0.3121 0.4833 0.0029  0.1613  -0.0992 719  PHE A CG  
1297 C CD1 . PHE A 182 ? 0.4599 0.3141 0.5039 0.0102  0.1707  -0.1114 719  PHE A CD1 
1298 C CD2 . PHE A 182 ? 0.4584 0.3089 0.4889 0.0052  0.1472  -0.0878 719  PHE A CD2 
1299 C CE1 . PHE A 182 ? 0.4349 0.3000 0.5113 0.0189  0.1628  -0.1094 719  PHE A CE1 
1300 C CE2 . PHE A 182 ? 0.4441 0.3031 0.5092 0.0151  0.1424  -0.0896 719  PHE A CE2 
1301 C CZ  . PHE A 182 ? 0.4275 0.2923 0.5159 0.0226  0.1520  -0.1017 719  PHE A CZ  
1302 N N   . ILE A 183 ? 0.5008 0.3331 0.4588 -0.0309 0.1581  -0.0636 720  ILE A N   
1303 C CA  . ILE A 183 ? 0.5113 0.3420 0.4792 -0.0358 0.1490  -0.0472 720  ILE A CA  
1304 C C   . ILE A 183 ? 0.5490 0.3797 0.5082 -0.0490 0.1597  -0.0390 720  ILE A C   
1305 O O   . ILE A 183 ? 0.5561 0.3878 0.5346 -0.0518 0.1558  -0.0282 720  ILE A O   
1306 C CB  . ILE A 183 ? 0.5101 0.3344 0.4613 -0.0393 0.1333  -0.0351 720  ILE A CB  
1307 C CG1 . ILE A 183 ? 0.5444 0.3622 0.4548 -0.0516 0.1376  -0.0310 720  ILE A CG1 
1308 C CG2 . ILE A 183 ? 0.4687 0.2964 0.4320 -0.0262 0.1225  -0.0424 720  ILE A CG2 
1309 C CD1 . ILE A 183 ? 0.5576 0.3682 0.4504 -0.0551 0.1226  -0.0198 720  ILE A CD1 
1310 N N   . SER A 184 ? 0.5837 0.4151 0.5155 -0.0573 0.1728  -0.0443 721  SER A N   
1311 C CA  . SER A 184 ? 0.6241 0.4601 0.5476 -0.0699 0.1850  -0.0382 721  SER A CA  
1312 C C   . SER A 184 ? 0.6233 0.4667 0.5749 -0.0644 0.1968  -0.0480 721  SER A C   
1313 O O   . SER A 184 ? 0.6537 0.5024 0.6057 -0.0743 0.2056  -0.0409 721  SER A O   
1314 C CB  . SER A 184 ? 0.6647 0.5027 0.5505 -0.0797 0.1954  -0.0432 721  SER A CB  
1315 O OG  . SER A 184 ? 0.6846 0.5312 0.5736 -0.0790 0.2126  -0.0587 721  SER A OG  
1316 N N   . SER A 185 ? 0.5953 0.4399 0.5703 -0.0496 0.1969  -0.0632 722  SER A N   
1317 C CA  . SER A 185 ? 0.5840 0.4346 0.5887 -0.0430 0.2065  -0.0726 722  SER A CA  
1318 C C   . SER A 185 ? 0.5819 0.4329 0.6227 -0.0357 0.1958  -0.0651 722  SER A C   
1319 O O   . SER A 185 ? 0.5693 0.4250 0.6375 -0.0301 0.2023  -0.0714 722  SER A O   
1320 C CB  . SER A 185 ? 0.5668 0.4193 0.5791 -0.0309 0.2126  -0.0940 722  SER A CB  
1321 O OG  . SER A 185 ? 0.5381 0.3894 0.5695 -0.0177 0.1996  -0.0969 722  SER A OG  
1322 N N   . VAL A 186 ? 0.5924 0.4391 0.6354 -0.0350 0.1790  -0.0530 723  VAL A N   
1323 C CA  . VAL A 186 ? 0.5950 0.4434 0.6745 -0.0268 0.1666  -0.0479 723  VAL A CA  
1324 C C   . VAL A 186 ? 0.6422 0.4904 0.7321 -0.0377 0.1671  -0.0325 723  VAL A C   
1325 O O   . VAL A 186 ? 0.6465 0.4906 0.7138 -0.0521 0.1644  -0.0166 723  VAL A O   
1326 C CB  . VAL A 186 ? 0.5691 0.4147 0.6485 -0.0222 0.1477  -0.0418 723  VAL A CB  
1327 C CG1 . VAL A 186 ? 0.5486 0.3982 0.6681 -0.0130 0.1343  -0.0390 723  VAL A CG1 
1328 C CG2 . VAL A 186 ? 0.5487 0.3961 0.6181 -0.0126 0.1470  -0.0553 723  VAL A CG2 
1329 N N   . ARG A 187 ? 0.6819 0.5347 0.8063 -0.0313 0.1700  -0.0366 724  ARG A N   
1330 C CA  . ARG A 187 ? 0.7492 0.6025 0.8910 -0.0404 0.1686  -0.0216 724  ARG A CA  
1331 C C   . ARG A 187 ? 0.7518 0.6047 0.9321 -0.0313 0.1495  -0.0164 724  ARG A C   
1332 O O   . ARG A 187 ? 0.7351 0.5918 0.9373 -0.0151 0.1431  -0.0298 724  ARG A O   
1333 C CB  . ARG A 187 ? 0.7716 0.6310 0.9270 -0.0406 0.1857  -0.0296 724  ARG A CB  
1334 C CG  . ARG A 187 ? 0.8119 0.6746 0.9338 -0.0488 0.2052  -0.0376 724  ARG A CG  
1335 C CD  . ARG A 187 ? 0.8638 0.7277 0.9557 -0.0690 0.2094  -0.0199 724  ARG A CD  
1336 N NE  . ARG A 187 ? 0.8937 0.7520 0.9516 -0.0750 0.2018  -0.0134 724  ARG A NE  
1337 C CZ  . ARG A 187 ? 0.9128 0.7720 0.9370 -0.0774 0.2108  -0.0236 724  ARG A CZ  
1338 N NH1 . ARG A 187 ? 0.9127 0.7782 0.9333 -0.0743 0.2275  -0.0413 724  ARG A NH1 
1339 N NH2 . ARG A 187 ? 0.9260 0.7794 0.9216 -0.0826 0.2024  -0.0166 724  ARG A NH2 
1340 N N   . GLY A 188 ? 0.7776 0.6273 0.9670 -0.0420 0.1396  0.0030  725  GLY A N   
1341 C CA  . GLY A 188 ? 0.7746 0.6241 1.0041 -0.0341 0.1201  0.0078  725  GLY A CA  
1342 C C   . GLY A 188 ? 0.8019 0.6444 1.0240 -0.0438 0.1020  0.0267  725  GLY A C   
1343 O O   . GLY A 188 ? 0.8178 0.6562 1.0096 -0.0466 0.0985  0.0280  725  GLY A O   
1344 N N   . LYS A 189 ? 0.8105 0.6512 1.0616 -0.0494 0.0896  0.0418  726  LYS A N   
1345 C CA  . LYS A 189 ? 0.8332 0.6663 1.0806 -0.0595 0.0707  0.0609  726  LYS A CA  
1346 C C   . LYS A 189 ? 0.8136 0.6465 1.0717 -0.0461 0.0531  0.0521  726  LYS A C   
1347 O O   . LYS A 189 ? 0.8261 0.6525 1.0619 -0.0529 0.0430  0.0615  726  LYS A O   
1348 C CB  . LYS A 189 ? 0.8465 0.6781 1.1300 -0.0668 0.0587  0.0780  726  LYS A CB  
1349 C CG  . LYS A 189 ? 0.8784 0.7121 1.1511 -0.0829 0.0744  0.0909  726  LYS A CG  
1350 C CD  . LYS A 189 ? 0.8912 0.7236 1.2035 -0.0901 0.0600  0.1092  726  LYS A CD  
1351 C CE  . LYS A 189 ? 0.9186 0.7561 1.2218 -0.1066 0.0760  0.1227  726  LYS A CE  
1352 N NZ  . LYS A 189 ? 0.9304 0.7671 1.2755 -0.1138 0.0613  0.1417  726  LYS A NZ  
1353 N N   . ALA A 190 ? 0.7837 0.6250 1.0752 -0.0269 0.0494  0.0336  727  ALA A N   
1354 C CA  . ALA A 190 ? 0.7670 0.6125 1.0740 -0.0137 0.0318  0.0246  727  ALA A CA  
1355 C C   . ALA A 190 ? 0.7656 0.6105 1.0327 -0.0127 0.0365  0.0183  727  ALA A C   
1356 O O   . ALA A 190 ? 0.7523 0.5997 1.0238 -0.0061 0.0213  0.0154  727  ALA A O   
1357 C CB  . ALA A 190 ? 0.7396 0.5979 1.0897 0.0065  0.0287  0.0051  727  ALA A CB  
1358 N N   . MET A 191 ? 0.7755 0.6180 1.0057 -0.0190 0.0565  0.0157  728  MET A N   
1359 C CA  . MET A 191 ? 0.7682 0.6101 0.9626 -0.0177 0.0614  0.0088  728  MET A CA  
1360 C C   . MET A 191 ? 0.7918 0.6229 0.9419 -0.0356 0.0657  0.0238  728  MET A C   
1361 O O   . MET A 191 ? 0.7928 0.6218 0.9124 -0.0358 0.0678  0.0199  728  MET A O   
1362 C CB  . MET A 191 ? 0.7559 0.6050 0.9453 -0.0084 0.0793  -0.0096 728  MET A CB  
1363 C CG  . MET A 191 ? 0.7367 0.5966 0.9696 0.0071  0.0783  -0.0231 728  MET A CG  
1364 S SD  . MET A 191 ? 0.7170 0.5895 0.9525 0.0247  0.0846  -0.0461 728  MET A SD  
1365 C CE  . MET A 191 ? 0.7222 0.5938 0.9536 0.0231  0.1083  -0.0551 728  MET A CE  
1366 N N   . LYS A 192 ? 0.8076 0.6328 0.9541 -0.0508 0.0663  0.0412  729  LYS A N   
1367 C CA  . LYS A 192 ? 0.8256 0.6429 0.9291 -0.0684 0.0709  0.0556  729  LYS A CA  
1368 C C   . LYS A 192 ? 0.8137 0.6237 0.9044 -0.0711 0.0532  0.0644  729  LYS A C   
1369 O O   . LYS A 192 ? 0.8247 0.6293 0.8756 -0.0798 0.0572  0.0686  729  LYS A O   
1370 C CB  . LYS A 192 ? 0.8528 0.6687 0.9577 -0.0848 0.0746  0.0737  729  LYS A CB  
1371 C CG  . LYS A 192 ? 0.8651 0.6883 0.9671 -0.0865 0.0967  0.0660  729  LYS A CG  
1372 C CD  . LYS A 192 ? 0.8819 0.7067 0.9427 -0.0880 0.1140  0.0543  729  LYS A CD  
1373 C CE  . LYS A 192 ? 0.8841 0.7171 0.9527 -0.0811 0.1332  0.0372  729  LYS A CE  
1374 N NZ  . LYS A 192 ? 0.8558 0.6920 0.9594 -0.0612 0.1288  0.0203  729  LYS A NZ  
1375 N N   . LYS A 193 ? 0.7881 0.5984 0.9128 -0.0633 0.0331  0.0660  730  LYS A N   
1376 C CA  . LYS A 193 ? 0.7690 0.5735 0.8848 -0.0640 0.0156  0.0718  730  LYS A CA  
1377 C C   . LYS A 193 ? 0.7155 0.5234 0.8098 -0.0542 0.0199  0.0567  730  LYS A C   
1378 O O   . LYS A 193 ? 0.7145 0.5154 0.7787 -0.0604 0.0152  0.0626  730  LYS A O   
1379 C CB  . LYS A 193 ? 0.7719 0.5790 0.9335 -0.0554 -0.0067 0.0726  730  LYS A CB  
1380 C CG  . LYS A 193 ? 0.8253 0.6281 1.0121 -0.0653 -0.0141 0.0888  730  LYS A CG  
1381 C CD  . LYS A 193 ? 0.8512 0.6548 1.0825 -0.0582 -0.0398 0.0905  730  LYS A CD  
1382 C CE  . LYS A 193 ? 0.8673 0.6784 1.1476 -0.0497 -0.0427 0.0852  730  LYS A CE  
1383 N NZ  . LYS A 193 ? 0.8480 0.6738 1.1534 -0.0279 -0.0412 0.0602  730  LYS A NZ  
1384 N N   . TRP A 194 ? 0.6546 0.4736 0.7648 -0.0393 0.0281  0.0380  731  TRP A N   
1385 C CA  . TRP A 194 ? 0.5992 0.4229 0.6911 -0.0306 0.0323  0.0247  731  TRP A CA  
1386 C C   . TRP A 194 ? 0.5854 0.4025 0.6335 -0.0404 0.0492  0.0252  731  TRP A C   
1387 O O   . TRP A 194 ? 0.5638 0.3766 0.5834 -0.0427 0.0470  0.0258  731  TRP A O   
1388 C CB  . TRP A 194 ? 0.5574 0.3956 0.6789 -0.0131 0.0364  0.0058  731  TRP A CB  
1389 C CG  . TRP A 194 ? 0.5217 0.3708 0.6834 -0.0004 0.0186  0.0004  731  TRP A CG  
1390 C CD1 . TRP A 194 ? 0.5059 0.3592 0.7077 0.0041  0.0105  0.0007  731  TRP A CD1 
1391 C CD2 . TRP A 194 ? 0.5025 0.3617 0.6696 0.0100  0.0062  -0.0073 731  TRP A CD2 
1392 N NE1 . TRP A 194 ? 0.4858 0.3518 0.7181 0.0172  -0.0063 -0.0077 731  TRP A NE1 
1393 C CE2 . TRP A 194 ? 0.4885 0.3593 0.6996 0.0208  -0.0088 -0.0126 731  TRP A CE2 
1394 C CE3 . TRP A 194 ? 0.5005 0.3615 0.6408 0.0111  0.0059  -0.0103 731  TRP A CE3 
1395 C CZ2 . TRP A 194 ? 0.4706 0.3564 0.6983 0.0325  -0.0232 -0.0217 731  TRP A CZ2 
1396 C CZ3 . TRP A 194 ? 0.4847 0.3597 0.6411 0.0220  -0.0082 -0.0175 731  TRP A CZ3 
1397 C CH2 . TRP A 194 ? 0.4718 0.3602 0.6711 0.0326  -0.0222 -0.0236 731  TRP A CH2 
1398 N N   . VAL A 195 ? 0.6003 0.4177 0.6439 -0.0458 0.0658  0.0241  732  VAL A N   
1399 C CA  . VAL A 195 ? 0.6263 0.4405 0.6318 -0.0538 0.0824  0.0213  732  VAL A CA  
1400 C C   . VAL A 195 ? 0.6499 0.4540 0.6196 -0.0687 0.0777  0.0364  732  VAL A C   
1401 O O   . VAL A 195 ? 0.6632 0.4642 0.6011 -0.0711 0.0824  0.0325  732  VAL A O   
1402 C CB  . VAL A 195 ? 0.6467 0.4647 0.6565 -0.0583 0.0999  0.0185  732  VAL A CB  
1403 C CG1 . VAL A 195 ? 0.6797 0.4953 0.6489 -0.0702 0.1150  0.0187  732  VAL A CG1 
1404 C CG2 . VAL A 195 ? 0.6244 0.4515 0.6616 -0.0428 0.1072  0.0000  732  VAL A CG2 
1405 N N   . GLU A 196 ? 0.6598 0.4588 0.6356 -0.0789 0.0673  0.0541  733  GLU A N   
1406 C CA  . GLU A 196 ? 0.6908 0.4806 0.6335 -0.0938 0.0619  0.0700  733  GLU A CA  
1407 C C   . GLU A 196 ? 0.6637 0.4476 0.6008 -0.0893 0.0451  0.0713  733  GLU A C   
1408 O O   . GLU A 196 ? 0.6991 0.4752 0.6028 -0.0990 0.0427  0.0795  733  GLU A O   
1409 C CB  . GLU A 196 ? 0.7397 0.5266 0.6920 -0.1075 0.0559  0.0901  733  GLU A CB  
1410 C CG  . GLU A 196 ? 0.7798 0.5734 0.7274 -0.1162 0.0743  0.0916  733  GLU A CG  
1411 C CD  . GLU A 196 ? 0.8017 0.5963 0.7780 -0.1238 0.0679  0.1074  733  GLU A CD  
1412 O OE1 . GLU A 196 ? 0.8008 0.5900 0.8024 -0.1220 0.0479  0.1167  733  GLU A OE1 
1413 O OE2 . GLU A 196 ? 0.8157 0.6173 0.7909 -0.1315 0.0822  0.1102  733  GLU A OE2 
1414 N N   . SER A 197 ? 0.6096 0.3985 0.5783 -0.0747 0.0336  0.0627  734  SER A N   
1415 C CA  . SER A 197 ? 0.6013 0.3879 0.5648 -0.0692 0.0192  0.0614  734  SER A CA  
1416 C C   . SER A 197 ? 0.5856 0.3743 0.5239 -0.0638 0.0287  0.0487  734  SER A C   
1417 O O   . SER A 197 ? 0.5785 0.3608 0.4921 -0.0669 0.0223  0.0522  734  SER A O   
1418 C CB  . SER A 197 ? 0.6012 0.3967 0.6077 -0.0551 0.0042  0.0548  734  SER A CB  
1419 O OG  . SER A 197 ? 0.6067 0.4029 0.6101 -0.0496 -0.0097 0.0529  734  SER A OG  
1420 N N   . ILE A 198 ? 0.5720 0.3691 0.5176 -0.0556 0.0429  0.0341  735  ILE A N   
1421 C CA  . ILE A 198 ? 0.5553 0.3540 0.4794 -0.0513 0.0516  0.0224  735  ILE A CA  
1422 C C   . ILE A 198 ? 0.5885 0.3775 0.4708 -0.0649 0.0599  0.0283  735  ILE A C   
1423 O O   . ILE A 198 ? 0.5844 0.3691 0.4429 -0.0654 0.0572  0.0266  735  ILE A O   
1424 C CB  . ILE A 198 ? 0.5032 0.3122 0.4459 -0.0410 0.0648  0.0064  735  ILE A CB  
1425 C CG1 . ILE A 198 ? 0.4485 0.2699 0.4284 -0.0258 0.0552  -0.0018 735  ILE A CG1 
1426 C CG2 . ILE A 198 ? 0.4843 0.2925 0.4016 -0.0406 0.0760  -0.0041 735  ILE A CG2 
1427 C CD1 . ILE A 198 ? 0.4311 0.2615 0.4416 -0.0180 0.0638  -0.0112 735  ILE A CD1 
1428 N N   . ALA A 199 ? 0.6181 0.4051 0.4916 -0.0762 0.0698  0.0352  736  ALA A N   
1429 C CA  . ALA A 199 ? 0.6438 0.4252 0.4777 -0.0893 0.0783  0.0399  736  ALA A CA  
1430 C C   . ALA A 199 ? 0.6547 0.4259 0.4668 -0.0982 0.0644  0.0547  736  ALA A C   
1431 O O   . ALA A 199 ? 0.6638 0.4301 0.4429 -0.1037 0.0666  0.0542  736  ALA A O   
1432 C CB  . ALA A 199 ? 0.6502 0.4355 0.4815 -0.1001 0.0914  0.0452  736  ALA A CB  
1433 N N   . LYS A 200 ? 0.6650 0.4329 0.4965 -0.0994 0.0491  0.0671  737  LYS A N   
1434 C CA  . LYS A 200 ? 0.6938 0.4513 0.5079 -0.1076 0.0341  0.0814  737  LYS A CA  
1435 C C   . LYS A 200 ? 0.7061 0.4608 0.5114 -0.0989 0.0258  0.0739  737  LYS A C   
1436 O O   . LYS A 200 ? 0.7343 0.4802 0.5105 -0.1061 0.0206  0.0805  737  LYS A O   
1437 C CB  . LYS A 200 ? 0.6940 0.4491 0.5372 -0.1094 0.0182  0.0945  737  LYS A CB  
1438 C CG  . LYS A 200 ? 0.7126 0.4566 0.5446 -0.1164 0.0000  0.1087  737  LYS A CG  
1439 C CD  . LYS A 200 ? 0.7098 0.4524 0.5771 -0.1169 -0.0170 0.1195  737  LYS A CD  
1440 C CE  . LYS A 200 ? 0.7095 0.4456 0.5818 -0.1137 -0.0379 0.1234  737  LYS A CE  
1441 N NZ  . LYS A 200 ? 0.7404 0.4648 0.6073 -0.1284 -0.0523 0.1443  737  LYS A NZ  
1442 N N   . ILE A 201 ? 0.6792 0.4425 0.5095 -0.0838 0.0244  0.0604  738  ILE A N   
1443 C CA  . ILE A 201 ? 0.6710 0.4346 0.4941 -0.0758 0.0173  0.0535  738  ILE A CA  
1444 C C   . ILE A 201 ? 0.6851 0.4458 0.4764 -0.0785 0.0292  0.0461  738  ILE A C   
1445 O O   . ILE A 201 ? 0.6930 0.4464 0.4604 -0.0815 0.0231  0.0488  738  ILE A O   
1446 C CB  . ILE A 201 ? 0.6321 0.4092 0.4902 -0.0597 0.0135  0.0414  738  ILE A CB  
1447 C CG1 . ILE A 201 ? 0.6209 0.4015 0.5102 -0.0563 -0.0022 0.0475  738  ILE A CG1 
1448 C CG2 . ILE A 201 ? 0.6193 0.3998 0.4683 -0.0523 0.0095  0.0338  738  ILE A CG2 
1449 C CD1 . ILE A 201 ? 0.5839 0.3812 0.5081 -0.0403 -0.0074 0.0352  738  ILE A CD1 
1450 N N   . ILE A 202 ? 0.6825 0.4488 0.4745 -0.0772 0.0456  0.0359  739  ILE A N   
1451 C CA  . ILE A 202 ? 0.7046 0.4694 0.4705 -0.0789 0.0563  0.0264  739  ILE A CA  
1452 C C   . ILE A 202 ? 0.7772 0.5326 0.5063 -0.0929 0.0567  0.0360  739  ILE A C   
1453 O O   . ILE A 202 ? 0.7891 0.5395 0.4944 -0.0940 0.0552  0.0325  739  ILE A O   
1454 C CB  . ILE A 202 ? 0.6847 0.4577 0.4603 -0.0759 0.0735  0.0135  739  ILE A CB  
1455 C CG1 . ILE A 202 ? 0.6366 0.4194 0.4477 -0.0615 0.0725  0.0034  739  ILE A CG1 
1456 C CG2 . ILE A 202 ? 0.6950 0.4669 0.4451 -0.0780 0.0835  0.0024  739  ILE A CG2 
1457 C CD1 . ILE A 202 ? 0.6277 0.4179 0.4516 -0.0581 0.0885  -0.0088 739  ILE A CD1 
1458 N N   . ARG A 203 ? 0.8254 0.5790 0.5499 -0.1042 0.0581  0.0488  740  ARG A N   
1459 C CA  . ARG A 203 ? 0.8795 0.6264 0.5688 -0.1185 0.0582  0.0594  740  ARG A CA  
1460 C C   . ARG A 203 ? 0.8851 0.6211 0.5611 -0.1197 0.0413  0.0682  740  ARG A C   
1461 O O   . ARG A 203 ? 0.9049 0.6352 0.5496 -0.1255 0.0413  0.0686  740  ARG A O   
1462 C CB  . ARG A 203 ? 0.9173 0.6660 0.6078 -0.1309 0.0609  0.0740  740  ARG A CB  
1463 C CG  . ARG A 203 ? 0.9418 0.7019 0.6379 -0.1329 0.0793  0.0665  740  ARG A CG  
1464 C CD  . ARG A 203 ? 0.9816 0.7445 0.6710 -0.1486 0.0821  0.0835  740  ARG A CD  
1465 N NE  . ARG A 203 ? 0.9980 0.7542 0.7090 -0.1508 0.0655  0.1004  740  ARG A NE  
1466 C CZ  . ARG A 203 ? 0.9930 0.7529 0.7389 -0.1477 0.0636  0.1039  740  ARG A CZ  
1467 N NH1 . ARG A 203 ? 0.9819 0.7520 0.7439 -0.1424 0.0781  0.0925  740  ARG A NH1 
1468 N NH2 . ARG A 203 ? 0.9923 0.7458 0.7585 -0.1495 0.0463  0.1183  740  ARG A NH2 
1469 N N   . ARG A 204 ? 0.8599 0.5935 0.5602 -0.1140 0.0265  0.0744  741  ARG A N   
1470 C CA  . ARG A 204 ? 0.8645 0.5888 0.5549 -0.1142 0.0102  0.0814  741  ARG A CA  
1471 C C   . ARG A 204 ? 0.8630 0.5871 0.5420 -0.1062 0.0105  0.0694  741  ARG A C   
1472 O O   . ARG A 204 ? 0.8851 0.6001 0.5405 -0.1101 0.0027  0.0738  741  ARG A O   
1473 C CB  . ARG A 204 ? 0.8473 0.5727 0.5705 -0.1078 -0.0054 0.0869  741  ARG A CB  
1474 C CG  . ARG A 204 ? 0.8354 0.5561 0.5571 -0.1027 -0.0215 0.0881  741  ARG A CG  
1475 C CD  . ARG A 204 ? 0.8233 0.5456 0.5758 -0.0987 -0.0380 0.0943  741  ARG A CD  
1476 N NE  . ARG A 204 ? 0.8040 0.5396 0.5936 -0.0890 -0.0346 0.0862  741  ARG A NE  
1477 C CZ  . ARG A 204 ? 0.7690 0.5172 0.5848 -0.0749 -0.0389 0.0749  741  ARG A CZ  
1478 N NH1 . ARG A 204 ? 0.7530 0.5031 0.5626 -0.0694 -0.0468 0.0714  741  ARG A NH1 
1479 N NH2 . ARG A 204 ? 0.7524 0.5129 0.6010 -0.0666 -0.0354 0.0675  741  ARG A NH2 
1480 N N   . LYS A 205 ? 0.8296 0.5633 0.5258 -0.0952 0.0186  0.0546  742  LYS A N   
1481 C CA  . LYS A 205 ? 0.8037 0.5381 0.4930 -0.0878 0.0177  0.0440  742  LYS A CA  
1482 C C   . LYS A 205 ? 0.8580 0.5878 0.5155 -0.0943 0.0276  0.0383  742  LYS A C   
1483 O O   . LYS A 205 ? 0.8675 0.5905 0.5059 -0.0949 0.0212  0.0377  742  LYS A O   
1484 C CB  . LYS A 205 ? 0.7262 0.4730 0.4452 -0.0748 0.0224  0.0312  742  LYS A CB  
1485 C CG  . LYS A 205 ? 0.6639 0.4189 0.4157 -0.0666 0.0121  0.0339  742  LYS A CG  
1486 C CD  . LYS A 205 ? 0.6345 0.3896 0.3872 -0.0619 -0.0034 0.0370  742  LYS A CD  
1487 C CE  . LYS A 205 ? 0.5926 0.3602 0.3797 -0.0527 -0.0133 0.0370  742  LYS A CE  
1488 N NZ  . LYS A 205 ? 0.5719 0.3449 0.3625 -0.0469 -0.0268 0.0374  742  LYS A NZ  
1489 N N   . LYS A 206 ? 0.8988 0.6334 0.5514 -0.0991 0.0427  0.0334  743  LYS A N   
1490 C CA  . LYS A 206 ? 0.9504 0.6848 0.5766 -0.1037 0.0531  0.0239  743  LYS A CA  
1491 C C   . LYS A 206 ? 1.0291 0.7540 0.6212 -0.1141 0.0468  0.0331  743  LYS A C   
1492 O O   . LYS A 206 ? 1.0494 0.7724 0.6207 -0.1148 0.0490  0.0243  743  LYS A O   
1493 C CB  . LYS A 206 ? 0.9400 0.6835 0.5671 -0.1083 0.0702  0.0183  743  LYS A CB  
1494 C CG  . LYS A 206 ? 0.9063 0.6587 0.5554 -0.0980 0.0805  0.0009  743  LYS A CG  
1495 C CD  . LYS A 206 ? 0.9122 0.6736 0.5549 -0.1038 0.0981  -0.0069 743  LYS A CD  
1496 C CE  . LYS A 206 ? 0.8861 0.6555 0.5524 -0.0935 0.1079  -0.0244 743  LYS A CE  
1497 N NZ  . LYS A 206 ? 0.8938 0.6730 0.5541 -0.0989 0.1252  -0.0338 743  LYS A NZ  
1498 N N   . GLN A 207 ? 1.0785 0.7974 0.6658 -0.1220 0.0379  0.0503  744  GLN A N   
1499 C CA  . GLN A 207 ? 1.1504 0.8603 0.7049 -0.1326 0.0316  0.0599  744  GLN A CA  
1500 C C   . GLN A 207 ? 1.1598 0.8596 0.7093 -0.1273 0.0165  0.0611  744  GLN A C   
1501 O O   . GLN A 207 ? 1.1877 0.8816 0.7101 -0.1312 0.0144  0.0594  744  GLN A O   
1502 C CB  . GLN A 207 ? 1.1876 0.8946 0.7388 -0.1444 0.0270  0.0790  744  GLN A CB  
1503 C CG  . GLN A 207 ? 1.2233 0.9408 0.7704 -0.1535 0.0420  0.0805  744  GLN A CG  
1504 C CD  . GLN A 207 ? 1.2722 0.9868 0.7979 -0.1698 0.0382  0.0996  744  GLN A CD  
1505 O OE1 . GLN A 207 ? 1.2857 0.9894 0.8112 -0.1735 0.0226  0.1142  744  GLN A OE1 
1506 N NE2 . GLN A 207 ? 1.2949 1.0205 0.8026 -0.1802 0.0521  0.0997  744  GLN A NE2 
1507 N N   . ALA A 208 ? 1.1362 0.8355 0.7121 -0.1184 0.0060  0.0632  745  ALA A N   
1508 C CA  . ALA A 208 ? 1.1275 0.8193 0.7015 -0.1136 -0.0089 0.0656  745  ALA A CA  
1509 C C   . ALA A 208 ? 1.1236 0.8149 0.6866 -0.1082 -0.0069 0.0528  745  ALA A C   
1510 O O   . ALA A 208 ? 1.1191 0.8177 0.6858 -0.1046 0.0050  0.0395  745  ALA A O   
1511 C CB  . ALA A 208 ? 1.0995 0.7969 0.7074 -0.1038 -0.0182 0.0670  745  ALA A CB  
1512 N N   . ILE A 217 ? 0.9788 0.6327 0.5806 -0.1233 -0.1494 0.1148  754  ILE A N   
1513 C CA  . ILE A 217 ? 0.9527 0.6151 0.5811 -0.1168 -0.1581 0.1126  754  ILE A CA  
1514 C C   . ILE A 217 ? 0.9492 0.6080 0.5873 -0.1219 -0.1703 0.1174  754  ILE A C   
1515 O O   . ILE A 217 ? 0.9537 0.6057 0.5826 -0.1265 -0.1737 0.1187  754  ILE A O   
1516 C CB  . ILE A 217 ? 0.9391 0.6088 0.5760 -0.1088 -0.1580 0.1049  754  ILE A CB  
1517 C CG1 . ILE A 217 ? 0.9410 0.6126 0.5673 -0.1048 -0.1474 0.1004  754  ILE A CG1 
1518 C CG2 . ILE A 217 ? 0.9105 0.5924 0.5745 -0.1021 -0.1655 0.1024  754  ILE A CG2 
1519 C CD1 . ILE A 217 ? 0.9228 0.6026 0.5591 -0.0974 -0.1478 0.0943  754  ILE A CD1 
1520 N N   . THR A 218 ? 0.9407 0.6034 0.5980 -0.1209 -0.1777 0.1199  755  THR A N   
1521 C CA  . THR A 218 ? 0.9482 0.6075 0.6182 -0.1256 -0.1914 0.1242  755  THR A CA  
1522 C C   . THR A 218 ? 0.8914 0.5582 0.5829 -0.1190 -0.2004 0.1178  755  THR A C   
1523 O O   . THR A 218 ? 0.8641 0.5419 0.5677 -0.1103 -0.1977 0.1121  755  THR A O   
1524 C CB  . THR A 218 ? 0.9777 0.6364 0.6591 -0.1290 -0.1965 0.1311  755  THR A CB  
1525 O OG1 . THR A 218 ? 0.9662 0.6344 0.6657 -0.1203 -0.1963 0.1269  755  THR A OG1 
1526 C CG2 . THR A 218 ? 1.0084 0.6610 0.6691 -0.1367 -0.1868 0.1385  755  THR A CG2 
1527 N N   . PHE A 219 ? 0.8734 0.5349 0.5698 -0.1235 -0.2111 0.1192  756  PHE A N   
1528 C CA  . PHE A 219 ? 0.8179 0.4853 0.5339 -0.1188 -0.2198 0.1135  756  PHE A CA  
1529 C C   . PHE A 219 ? 0.8001 0.4639 0.5344 -0.1230 -0.2358 0.1166  756  PHE A C   
1530 O O   . PHE A 219 ? 0.8077 0.4610 0.5347 -0.1320 -0.2422 0.1225  756  PHE A O   
1531 C CB  . PHE A 219 ? 0.7999 0.4634 0.5054 -0.1197 -0.2177 0.1105  756  PHE A CB  
1532 C CG  . PHE A 219 ? 0.7823 0.4516 0.4777 -0.1138 -0.2050 0.1060  756  PHE A CG  
1533 C CD1 . PHE A 219 ? 0.7512 0.4345 0.4620 -0.1048 -0.2023 0.1002  756  PHE A CD1 
1534 C CD2 . PHE A 219 ? 0.7976 0.4592 0.4694 -0.1174 -0.1963 0.1079  756  PHE A CD2 
1535 C CE1 . PHE A 219 ? 0.7386 0.4278 0.4424 -0.0999 -0.1921 0.0968  756  PHE A CE1 
1536 C CE2 . PHE A 219 ? 0.7889 0.4549 0.4534 -0.1121 -0.1865 0.1034  756  PHE A CE2 
1537 C CZ  . PHE A 219 ? 0.7573 0.4369 0.4385 -0.1036 -0.1849 0.0981  756  PHE A CZ  
1538 N N   . GLU A 220 ? 0.7741 0.4474 0.5336 -0.1163 -0.2427 0.1125  757  GLU A N   
1539 C CA  . GLU A 220 ? 0.7772 0.4476 0.5593 -0.1192 -0.2596 0.1139  757  GLU A CA  
1540 C C   . GLU A 220 ? 0.7627 0.4270 0.5495 -0.1225 -0.2688 0.1116  757  GLU A C   
1541 O O   . GLU A 220 ? 0.7712 0.4264 0.5653 -0.1301 -0.2824 0.1155  757  GLU A O   
1542 C CB  . GLU A 220 ? 0.7784 0.4617 0.5879 -0.1092 -0.2636 0.1086  757  GLU A CB  
1543 C CG  . GLU A 220 ? 0.8038 0.4852 0.6431 -0.1098 -0.2817 0.1078  757  GLU A CG  
1544 C CD  . GLU A 220 ? 0.8111 0.4963 0.6672 -0.1042 -0.2870 0.1004  757  GLU A CD  
1545 O OE1 . GLU A 220 ? 0.8189 0.4984 0.6977 -0.1054 -0.3015 0.0994  757  GLU A OE1 
1546 O OE2 . GLU A 220 ? 0.8020 0.4962 0.6498 -0.0982 -0.2761 0.0960  757  GLU A OE2 
1547 N N   . SER A 221 ? 0.7376 0.4072 0.5215 -0.1171 -0.2621 0.1058  758  SER A N   
1548 C CA  . SER A 221 ? 0.7303 0.3931 0.5139 -0.1203 -0.2675 0.1039  758  SER A CA  
1549 C C   . SER A 221 ? 0.7116 0.3737 0.4728 -0.1202 -0.2549 0.1030  758  SER A C   
1550 O O   . SER A 221 ? 0.6867 0.3581 0.4413 -0.1141 -0.2425 0.1009  758  SER A O   
1551 C CB  . SER A 221 ? 0.7200 0.3914 0.5290 -0.1123 -0.2728 0.0976  758  SER A CB  
1552 O OG  . SER A 221 ? 0.7150 0.4027 0.5245 -0.1023 -0.2602 0.0929  758  SER A OG  
1553 N N   . PRO A 222 ? 0.7241 0.3751 0.4746 -0.1267 -0.2587 0.1043  759  PRO A N   
1554 C CA  . PRO A 222 ? 0.7311 0.3792 0.4600 -0.1272 -0.2481 0.1039  759  PRO A CA  
1555 C C   . PRO A 222 ? 0.7074 0.3678 0.4424 -0.1180 -0.2392 0.0979  759  PRO A C   
1556 O O   . PRO A 222 ? 0.6810 0.3473 0.4328 -0.1141 -0.2434 0.0944  759  PRO A O   
1557 C CB  . PRO A 222 ? 0.7509 0.3857 0.4738 -0.1352 -0.2573 0.1057  759  PRO A CB  
1558 C CG  . PRO A 222 ? 0.7605 0.3890 0.4934 -0.1420 -0.2711 0.1102  759  PRO A CG  
1559 C CD  . PRO A 222 ? 0.7335 0.3727 0.4901 -0.1351 -0.2740 0.1071  759  PRO A CD  
1560 N N   . PRO A 223 ? 0.6956 0.3606 0.4178 -0.1146 -0.2270 0.0972  760  PRO A N   
1561 C CA  . PRO A 223 ? 0.6567 0.3344 0.3856 -0.1066 -0.2195 0.0926  760  PRO A CA  
1562 C C   . PRO A 223 ? 0.6305 0.3024 0.3554 -0.1084 -0.2211 0.0912  760  PRO A C   
1563 O O   . PRO A 223 ? 0.6360 0.2932 0.3456 -0.1153 -0.2243 0.0934  760  PRO A O   
1564 C CB  . PRO A 223 ? 0.6709 0.3512 0.3858 -0.1043 -0.2082 0.0929  760  PRO A CB  
1565 C CG  . PRO A 223 ? 0.7095 0.3744 0.4037 -0.1123 -0.2087 0.0975  760  PRO A CG  
1566 C CD  . PRO A 223 ? 0.7090 0.3681 0.4111 -0.1179 -0.2200 0.1009  760  PRO A CD  
1567 N N   . PRO A 224 ? 0.6116 0.2955 0.3499 -0.1024 -0.2190 0.0878  761  PRO A N   
1568 C CA  . PRO A 224 ? 0.6166 0.2893 0.3501 -0.1066 -0.2246 0.0870  761  PRO A CA  
1569 C C   . PRO A 224 ? 0.6670 0.3288 0.3796 -0.1096 -0.2203 0.0873  761  PRO A C   
1570 O O   . PRO A 224 ? 0.6703 0.3367 0.3749 -0.1066 -0.2116 0.0875  761  PRO A O   
1571 C CB  . PRO A 224 ? 0.5780 0.2664 0.3291 -0.1001 -0.2232 0.0847  761  PRO A CB  
1572 C CG  . PRO A 224 ? 0.5653 0.2725 0.3236 -0.0925 -0.2142 0.0841  761  PRO A CG  
1573 C CD  . PRO A 224 ? 0.5775 0.2821 0.3332 -0.0936 -0.2141 0.0856  761  PRO A CD  
1574 N N   . PRO A 225 ? 0.6899 0.3368 0.3931 -0.1151 -0.2265 0.0872  762  PRO A N   
1575 C CA  . PRO A 225 ? 0.6896 0.3255 0.3728 -0.1174 -0.2231 0.0873  762  PRO A CA  
1576 C C   . PRO A 225 ? 0.6417 0.2863 0.3282 -0.1117 -0.2171 0.0851  762  PRO A C   
1577 O O   . PRO A 225 ? 0.6161 0.2721 0.3192 -0.1080 -0.2179 0.0838  762  PRO A O   
1578 C CB  . PRO A 225 ? 0.6632 0.2822 0.3392 -0.1243 -0.2327 0.0875  762  PRO A CB  
1579 C CG  . PRO A 225 ? 0.7559 0.3801 0.4519 -0.1236 -0.2396 0.0862  762  PRO A CG  
1580 C CD  . PRO A 225 ? 0.6336 0.2722 0.3440 -0.1195 -0.2371 0.0869  762  PRO A CD  
1581 N N   . ILE A 226 ? 0.4622 0.4142 0.3734 -0.1108 -0.1345 0.1761  763  ILE A N   
1582 C CA  . ILE A 226 ? 0.4393 0.3951 0.3326 -0.1031 -0.1162 0.1491  763  ILE A CA  
1583 C C   . ILE A 226 ? 0.4549 0.4126 0.3528 -0.1000 -0.1250 0.1459  763  ILE A C   
1584 O O   . ILE A 226 ? 0.4923 0.4544 0.3825 -0.1123 -0.1427 0.1633  763  ILE A O   
1585 C CB  . ILE A 226 ? 0.4599 0.4261 0.3073 -0.1168 -0.1018 0.1414  763  ILE A CB  
1586 C CG1 . ILE A 226 ? 0.4853 0.4523 0.3285 -0.1233 -0.0953 0.1493  763  ILE A CG1 
1587 C CG2 . ILE A 226 ? 0.4365 0.4042 0.2754 -0.1063 -0.0819 0.1131  763  ILE A CG2 
1588 C CD1 . ILE A 226 ? 0.4288 0.3888 0.2966 -0.1072 -0.0816 0.1348  763  ILE A CD1 
1589 N N   . GLU A 227 ? 0.4347 0.3898 0.3457 -0.0847 -0.1136 0.1249  764  GLU A N   
1590 C CA  . GLU A 227 ? 0.4391 0.3964 0.3570 -0.0807 -0.1195 0.1195  764  GLU A CA  
1591 C C   . GLU A 227 ? 0.4565 0.4201 0.3380 -0.0865 -0.1077 0.1028  764  GLU A C   
1592 O O   . GLU A 227 ? 0.4491 0.4126 0.3183 -0.0824 -0.0893 0.0860  764  GLU A O   
1593 C CB  . GLU A 227 ? 0.4029 0.3543 0.3599 -0.0615 -0.1144 0.1077  764  GLU A CB  
1594 C CG  . GLU A 227 ? 0.4022 0.3467 0.4017 -0.0547 -0.1254 0.1204  764  GLU A CG  
1595 C CD  . GLU A 227 ? 0.4221 0.3688 0.4430 -0.0594 -0.1474 0.1397  764  GLU A CD  
1596 O OE1 . GLU A 227 ? 0.4357 0.3894 0.4413 -0.0654 -0.1531 0.1399  764  GLU A OE1 
1597 O OE2 . GLU A 227 ? 0.4303 0.3714 0.4860 -0.0573 -0.1597 0.1550  764  GLU A OE2 
1598 N N   . TRP A 228 ? 0.4779 0.4470 0.3449 -0.0966 -0.1191 0.1075  765  TRP A N   
1599 C CA  . TRP A 228 ? 0.4812 0.4550 0.3173 -0.1027 -0.1096 0.0903  765  TRP A CA  
1600 C C   . TRP A 228 ? 0.4662 0.4405 0.3182 -0.0981 -0.1185 0.0871  765  TRP A C   
1601 O O   . TRP A 228 ? 0.4608 0.4359 0.3353 -0.0985 -0.1369 0.1037  765  TRP A O   
1602 C CB  . TRP A 228 ? 0.5211 0.5031 0.3132 -0.1252 -0.1132 0.0965  765  TRP A CB  
1603 C CG  . TRP A 228 ? 0.5372 0.5211 0.3124 -0.1316 -0.1028 0.0994  765  TRP A CG  
1604 C CD1 . TRP A 228 ? 0.5463 0.5312 0.3228 -0.1403 -0.1140 0.1225  765  TRP A CD1 
1605 C CD2 . TRP A 228 ? 0.5351 0.5208 0.2933 -0.1301 -0.0794 0.0795  765  TRP A CD2 
1606 N NE1 . TRP A 228 ? 0.5583 0.5462 0.3173 -0.1450 -0.0982 0.1179  765  TRP A NE1 
1607 C CE2 . TRP A 228 ? 0.5551 0.5441 0.3038 -0.1385 -0.0767 0.0912  765  TRP A CE2 
1608 C CE3 . TRP A 228 ? 0.5103 0.4952 0.2643 -0.1227 -0.0611 0.0538  765  TRP A CE3 
1609 C CZ2 . TRP A 228 ? 0.5526 0.5455 0.2880 -0.1393 -0.0553 0.0771  765  TRP A CZ2 
1610 C CZ3 . TRP A 228 ? 0.5104 0.4983 0.2534 -0.1229 -0.0409 0.0403  765  TRP A CZ3 
1611 C CH2 . TRP A 228 ? 0.5336 0.5262 0.2676 -0.1311 -0.0377 0.0515  765  TRP A CH2 
1612 N N   . HIS A 229 ? 0.4836 0.4574 0.3274 -0.0935 -0.1054 0.0662  766  HIS A N   
1613 C CA  . HIS A 229 ? 0.4997 0.4743 0.3578 -0.0895 -0.1114 0.0611  766  HIS A CA  
1614 C C   . HIS A 229 ? 0.5314 0.5106 0.3549 -0.1056 -0.1141 0.0541  766  HIS A C   
1615 O O   . HIS A 229 ? 0.5600 0.5448 0.3639 -0.1221 -0.1296 0.0678  766  HIS A O   
1616 C CB  . HIS A 229 ? 0.4882 0.4583 0.3676 -0.0725 -0.0958 0.0440  766  HIS A CB  
1617 C CG  . HIS A 229 ? 0.4918 0.4634 0.3877 -0.0685 -0.1004 0.0390  766  HIS A CG  
1618 N ND1 . HIS A 229 ? 0.5023 0.4786 0.4111 -0.0737 -0.1190 0.0521  766  HIS A ND1 
1619 C CD2 . HIS A 229 ? 0.4724 0.4422 0.3757 -0.0608 -0.0895 0.0238  766  HIS A CD2 
1620 C CE1 . HIS A 229 ? 0.4886 0.4663 0.4118 -0.0691 -0.1182 0.0440  766  HIS A CE1 
1621 N NE2 . HIS A 229 ? 0.4798 0.4533 0.3990 -0.0616 -0.1005 0.0272  766  HIS A NE2 
1622 N N   . ILE A 230 ? 0.5430 0.5197 0.3585 -0.1022 -0.0995 0.0326  767  ILE A N   
1623 C CA  . ILE A 230 ? 0.5884 0.5678 0.3728 -0.1170 -0.0994 0.0210  767  ILE A CA  
1624 C C   . ILE A 230 ? 0.6185 0.6004 0.3658 -0.1291 -0.0866 0.0117  767  ILE A C   
1625 O O   . ILE A 230 ? 0.6532 0.6415 0.3666 -0.1488 -0.0937 0.0144  767  ILE A O   
1626 C CB  . ILE A 230 ? 0.5686 0.5431 0.3669 -0.1080 -0.0903 0.0022  767  ILE A CB  
1627 C CG1 . ILE A 230 ? 0.5481 0.5229 0.3827 -0.0977 -0.1019 0.0116  767  ILE A CG1 
1628 C CG2 . ILE A 230 ? 0.5912 0.5670 0.3597 -0.1237 -0.0903 -0.0119 767  ILE A CG2 
1629 C CD1 . ILE A 230 ? 0.5354 0.5059 0.3870 -0.0883 -0.0925 -0.0036 767  ILE A CD1 
1630 N N   . SER A 231 ? 0.6021 0.5806 0.3553 -0.1189 -0.0676 0.0010  768  SER A N   
1631 C CA  . SER A 231 ? 0.6354 0.6182 0.3588 -0.1296 -0.0540 -0.0066 768  SER A CA  
1632 C C   . SER A 231 ? 0.6721 0.6613 0.3808 -0.1414 -0.0658 0.0161  768  SER A C   
1633 O O   . SER A 231 ? 0.6520 0.6390 0.3847 -0.1343 -0.0790 0.0358  768  SER A O   
1634 C CB  . SER A 231 ? 0.6183 0.5972 0.3585 -0.1151 -0.0334 -0.0195 768  SER A CB  
1635 O OG  . SER A 231 ? 0.6108 0.5850 0.3593 -0.1085 -0.0210 -0.0413 768  SER A OG  
1636 N N   . LYS A 232 ? 0.7305 0.7278 0.4004 -0.1605 -0.0606 0.0131  769  LYS A N   
1637 C CA  . LYS A 232 ? 0.7703 0.7754 0.4198 -0.1765 -0.0723 0.0359  769  LYS A CA  
1638 C C   . LYS A 232 ? 0.7664 0.7761 0.4027 -0.1797 -0.0533 0.0310  769  LYS A C   
1639 O O   . LYS A 232 ? 0.7611 0.7704 0.3968 -0.1739 -0.0310 0.0071  769  LYS A O   
1640 C CB  . LYS A 232 ? 0.8227 0.8361 0.4503 -0.1951 -0.0816 0.0392  769  LYS A CB  
1641 C CG  . LYS A 232 ? 0.8441 0.8548 0.4862 -0.1943 -0.1038 0.0496  769  LYS A CG  
1642 C CD  . LYS A 232 ? 0.8462 0.8519 0.5210 -0.1832 -0.1228 0.0744  769  LYS A CD  
1643 C CE  . LYS A 232 ? 0.8582 0.8627 0.5554 -0.1804 -0.1436 0.0836  769  LYS A CE  
1644 N NZ  . LYS A 232 ? 0.8466 0.8468 0.5864 -0.1669 -0.1589 0.1051  769  LYS A NZ  
1645 N N   . PRO A 233 ? 0.7685 0.7828 0.4047 -0.1867 -0.0610 0.0535  770  PRO A N   
1646 C CA  . PRO A 233 ? 0.7622 0.7819 0.3916 -0.1891 -0.0431 0.0501  770  PRO A CA  
1647 C C   . PRO A 233 ? 0.7865 0.8162 0.3933 -0.1996 -0.0226 0.0270  770  PRO A C   
1648 O O   . PRO A 233 ? 0.8194 0.8562 0.4070 -0.2146 -0.0278 0.0269  770  PRO A O   
1649 C CB  . PRO A 233 ? 0.7745 0.7980 0.4072 -0.1988 -0.0597 0.0801  770  PRO A CB  
1650 C CG  . PRO A 233 ? 0.7679 0.7833 0.4234 -0.1924 -0.0848 0.0993  770  PRO A CG  
1651 C CD  . PRO A 233 ? 0.7726 0.7865 0.4222 -0.1909 -0.0868 0.0836  770  PRO A CD  
1652 N N   . GLY A 234 ? 0.7780 0.8082 0.3900 -0.1915 0.0007  0.0072  771  GLY A N   
1653 C CA  . GLY A 234 ? 0.8070 0.8462 0.4063 -0.1986 0.0222  -0.0161 771  GLY A CA  
1654 C C   . GLY A 234 ? 0.8114 0.8450 0.4182 -0.1899 0.0345  -0.0443 771  GLY A C   
1655 O O   . GLY A 234 ? 0.8235 0.8617 0.4339 -0.1888 0.0561  -0.0664 771  GLY A O   
1656 N N   . GLN A 235 ? 0.8079 0.8317 0.4211 -0.1836 0.0208  -0.0438 772  GLN A N   
1657 C CA  . GLN A 235 ? 0.8183 0.8351 0.4428 -0.1749 0.0302  -0.0688 772  GLN A CA  
1658 C C   . GLN A 235 ? 0.7632 0.7708 0.4163 -0.1554 0.0408  -0.0785 772  GLN A C   
1659 O O   . GLN A 235 ? 0.7333 0.7305 0.4072 -0.1429 0.0328  -0.0793 772  GLN A O   
1660 C CB  . GLN A 235 ? 0.8558 0.8670 0.4761 -0.1778 0.0104  -0.0635 772  GLN A CB  
1661 C CG  . GLN A 235 ? 0.9258 0.9455 0.5202 -0.1971 0.0011  -0.0584 772  GLN A CG  
1662 C CD  . GLN A 235 ? 0.9443 0.9586 0.5403 -0.1985 -0.0195 -0.0516 772  GLN A CD  
1663 O OE1 . GLN A 235 ? 0.9160 0.9222 0.5312 -0.1868 -0.0317 -0.0423 772  GLN A OE1 
1664 N NE2 . GLN A 235 ? 0.9862 1.0058 0.5629 -0.2133 -0.0235 -0.0565 772  GLN A NE2 
1665 N N   . PHE A 236 ? 0.7541 0.7665 0.4169 -0.1511 0.0583  -0.0838 773  PHE A N   
1666 C CA  . PHE A 236 ? 0.7233 0.7282 0.4237 -0.1305 0.0659  -0.0882 773  PHE A CA  
1667 C C   . PHE A 236 ? 0.7238 0.7213 0.4451 -0.1205 0.0765  -0.1121 773  PHE A C   
1668 O O   . PHE A 236 ? 0.6850 0.6746 0.4421 -0.1025 0.0760  -0.1111 773  PHE A O   
1669 C CB  . PHE A 236 ? 0.7240 0.7371 0.4330 -0.1289 0.0812  -0.0873 773  PHE A CB  
1670 C CG  . PHE A 236 ? 0.7601 0.7842 0.4601 -0.1384 0.1020  -0.1063 773  PHE A CG  
1671 C CD1 . PHE A 236 ? 0.7548 0.7770 0.4819 -0.1284 0.1186  -0.1298 773  PHE A CD1 
1672 C CD2 . PHE A 236 ? 0.7912 0.8277 0.4664 -0.1550 0.1023  -0.0976 773  PHE A CD2 
1673 C CE1 . PHE A 236 ? 0.7814 0.8135 0.5100 -0.1348 0.1358  -0.1456 773  PHE A CE1 
1674 C CE2 . PHE A 236 ? 0.8134 0.8606 0.4867 -0.1623 0.1203  -0.1142 773  PHE A CE2 
1675 C CZ  . PHE A 236 ? 0.8085 0.8535 0.5086 -0.1520 0.1374  -0.1388 773  PHE A CZ  
1676 N N   . GLU A 237 ? 0.7624 0.7623 0.4700 -0.1303 0.0831  -0.1297 774  GLU A N   
1677 C CA  . GLU A 237 ? 0.7741 0.7656 0.5066 -0.1208 0.0911  -0.1506 774  GLU A CA  
1678 C C   . GLU A 237 ? 0.7244 0.7035 0.4635 -0.1148 0.0754  -0.1471 774  GLU A C   
1679 O O   . GLU A 237 ? 0.7090 0.6790 0.4768 -0.1036 0.0800  -0.1595 774  GLU A O   
1680 C CB  . GLU A 237 ? 0.8505 0.8474 0.5714 -0.1322 0.0999  -0.1677 774  GLU A CB  
1681 C CG  . GLU A 237 ? 0.9063 0.9163 0.6219 -0.1397 0.1172  -0.1745 774  GLU A CG  
1682 C CD  . GLU A 237 ? 0.9671 0.9889 0.6441 -0.1582 0.1096  -0.1588 774  GLU A CD  
1683 O OE1 . GLU A 237 ? 1.0067 1.0402 0.6724 -0.1691 0.1226  -0.1664 774  GLU A OE1 
1684 O OE2 . GLU A 237 ? 0.9750 0.9945 0.6350 -0.1623 0.0900  -0.1382 774  GLU A OE2 
1685 N N   . THR A 238 ? 0.7000 0.6795 0.4233 -0.1199 0.0548  -0.1260 775  THR A N   
1686 C CA  . THR A 238 ? 0.6771 0.6479 0.4162 -0.1123 0.0377  -0.1173 775  THR A CA  
1687 C C   . THR A 238 ? 0.6167 0.5844 0.3836 -0.0963 0.0277  -0.0963 775  THR A C   
1688 O O   . THR A 238 ? 0.6047 0.5676 0.3851 -0.0905 0.0137  -0.0870 775  THR A O   
1689 C CB  . THR A 238 ? 0.7175 0.6917 0.4257 -0.1290 0.0205  -0.1094 775  THR A CB  
1690 O OG1 . THR A 238 ? 0.7215 0.7016 0.4199 -0.1328 0.0065  -0.0838 775  THR A OG1 
1691 C CG2 . THR A 238 ? 0.7621 0.7431 0.4422 -0.1457 0.0302  -0.1258 775  THR A CG2 
1692 N N   . PHE A 239 ? 0.5697 0.5407 0.3456 -0.0901 0.0350  -0.0897 776  PHE A N   
1693 C CA  . PHE A 239 ? 0.5052 0.4732 0.3059 -0.0763 0.0265  -0.0726 776  PHE A CA  
1694 C C   . PHE A 239 ? 0.4717 0.4323 0.3038 -0.0617 0.0281  -0.0785 776  PHE A C   
1695 O O   . PHE A 239 ? 0.4662 0.4242 0.3101 -0.0582 0.0404  -0.0943 776  PHE A O   
1696 C CB  . PHE A 239 ? 0.4815 0.4543 0.2863 -0.0737 0.0347  -0.0666 776  PHE A CB  
1697 C CG  . PHE A 239 ? 0.4788 0.4588 0.2567 -0.0876 0.0297  -0.0540 776  PHE A CG  
1698 C CD1 . PHE A 239 ? 0.4917 0.4740 0.2438 -0.1015 0.0170  -0.0470 776  PHE A CD1 
1699 C CD2 . PHE A 239 ? 0.4540 0.4390 0.2336 -0.0879 0.0365  -0.0473 776  PHE A CD2 
1700 C CE1 . PHE A 239 ? 0.5059 0.4955 0.2338 -0.1158 0.0107  -0.0324 776  PHE A CE1 
1701 C CE2 . PHE A 239 ? 0.4746 0.4663 0.2307 -0.1018 0.0312  -0.0335 776  PHE A CE2 
1702 C CZ  . PHE A 239 ? 0.4978 0.4918 0.2278 -0.1160 0.0180  -0.0253 776  PHE A CZ  
1703 N N   . ASP A 240 ? 0.4488 0.4065 0.2959 -0.0538 0.0157  -0.0652 777  ASP A N   
1704 C CA  . ASP A 240 ? 0.4350 0.3876 0.3094 -0.0418 0.0155  -0.0668 777  ASP A CA  
1705 C C   . ASP A 240 ? 0.4086 0.3617 0.2944 -0.0355 0.0039  -0.0510 777  ASP A C   
1706 O O   . ASP A 240 ? 0.4138 0.3696 0.2898 -0.0401 -0.0051 -0.0400 777  ASP A O   
1707 C CB  . ASP A 240 ? 0.4671 0.4150 0.3434 -0.0447 0.0143  -0.0779 777  ASP A CB  
1708 C CG  . ASP A 240 ? 0.4792 0.4220 0.3838 -0.0345 0.0200  -0.0836 777  ASP A CG  
1709 O OD1 . ASP A 240 ? 0.4634 0.4073 0.3853 -0.0251 0.0202  -0.0748 777  ASP A OD1 
1710 O OD2 . ASP A 240 ? 0.4896 0.4272 0.3994 -0.0368 0.0235  -0.0964 777  ASP A OD2 
1711 N N   . LEU A 241 ? 0.3739 0.3250 0.2823 -0.0257 0.0042  -0.0500 778  LEU A N   
1712 C CA  . LEU A 241 ? 0.3346 0.2874 0.2556 -0.0196 -0.0034 -0.0386 778  LEU A CA  
1713 C C   . LEU A 241 ? 0.3371 0.2914 0.2543 -0.0242 -0.0157 -0.0315 778  LEU A C   
1714 O O   . LEU A 241 ? 0.3296 0.2859 0.2496 -0.0236 -0.0225 -0.0214 778  LEU A O   
1715 C CB  . LEU A 241 ? 0.3047 0.2569 0.2459 -0.0118 -0.0009 -0.0397 778  LEU A CB  
1716 C CG  . LEU A 241 ? 0.3021 0.2578 0.2560 -0.0065 -0.0056 -0.0313 778  LEU A CG  
1717 C CD1 . LEU A 241 ? 0.2956 0.2527 0.2517 -0.0026 -0.0020 -0.0281 778  LEU A CD1 
1718 C CD2 . LEU A 241 ? 0.2946 0.2517 0.2632 -0.0032 -0.0051 -0.0318 778  LEU A CD2 
1719 N N   . MET A 242 ? 0.3425 0.2958 0.2567 -0.0290 -0.0196 -0.0363 779  MET A N   
1720 C CA  . MET A 242 ? 0.3575 0.3135 0.2733 -0.0332 -0.0327 -0.0286 779  MET A CA  
1721 C C   . MET A 242 ? 0.3997 0.3575 0.2925 -0.0454 -0.0411 -0.0242 779  MET A C   
1722 O O   . MET A 242 ? 0.4034 0.3646 0.3000 -0.0493 -0.0546 -0.0143 779  MET A O   
1723 C CB  . MET A 242 ? 0.3466 0.3014 0.2714 -0.0341 -0.0347 -0.0344 779  MET A CB  
1724 C CG  . MET A 242 ? 0.3310 0.2855 0.2776 -0.0246 -0.0283 -0.0357 779  MET A CG  
1725 S SD  . MET A 242 ? 0.3256 0.2871 0.2936 -0.0165 -0.0316 -0.0248 779  MET A SD  
1726 C CE  . MET A 242 ? 0.3055 0.2720 0.2847 -0.0211 -0.0439 -0.0200 779  MET A CE  
1727 N N   . THR A 243 ? 0.4222 0.3795 0.2924 -0.0524 -0.0338 -0.0305 780  THR A N   
1728 C CA  . THR A 243 ? 0.4507 0.4116 0.2943 -0.0668 -0.0414 -0.0253 780  THR A CA  
1729 C C   . THR A 243 ? 0.4494 0.4130 0.2888 -0.0681 -0.0442 -0.0117 780  THR A C   
1730 O O   . THR A 243 ? 0.4753 0.4427 0.3015 -0.0788 -0.0570 0.0010  780  THR A O   
1731 C CB  . THR A 243 ? 0.4843 0.4450 0.3022 -0.0773 -0.0309 -0.0420 780  THR A CB  
1732 O OG1 . THR A 243 ? 0.4906 0.4496 0.3137 -0.0703 -0.0139 -0.0518 780  THR A OG1 
1733 C CG2 . THR A 243 ? 0.4997 0.4567 0.3204 -0.0794 -0.0317 -0.0547 780  THR A CG2 
1734 N N   . LEU A 244 ? 0.4002 0.3619 0.2511 -0.0585 -0.0341 -0.0128 781  LEU A N   
1735 C CA  . LEU A 244 ? 0.3868 0.3496 0.2410 -0.0583 -0.0383 0.0011  781  LEU A CA  
1736 C C   . LEU A 244 ? 0.3660 0.3274 0.2469 -0.0505 -0.0506 0.0131  781  LEU A C   
1737 O O   . LEU A 244 ? 0.3496 0.3105 0.2477 -0.0436 -0.0522 0.0093  781  LEU A O   
1738 C CB  . LEU A 244 ? 0.3741 0.3358 0.2339 -0.0512 -0.0242 -0.0046 781  LEU A CB  
1739 C CG  . LEU A 244 ? 0.3894 0.3542 0.2282 -0.0587 -0.0105 -0.0158 781  LEU A CG  
1740 C CD1 . LEU A 244 ? 0.3661 0.3301 0.2200 -0.0490 0.0031  -0.0235 781  LEU A CD1 
1741 C CD2 . LEU A 244 ? 0.4191 0.3891 0.2338 -0.0729 -0.0140 -0.0058 781  LEU A CD2 
1742 N N   . HIS A 245 ? 0.3657 0.3270 0.2524 -0.0522 -0.0588 0.0277  782  HIS A N   
1743 C CA  . HIS A 245 ? 0.3506 0.3103 0.2680 -0.0446 -0.0693 0.0377  782  HIS A CA  
1744 C C   . HIS A 245 ? 0.3259 0.2822 0.2650 -0.0311 -0.0588 0.0303  782  HIS A C   
1745 O O   . HIS A 245 ? 0.3323 0.2869 0.2646 -0.0301 -0.0496 0.0269  782  HIS A O   
1746 C CB  . HIS A 245 ? 0.3823 0.3420 0.3020 -0.0521 -0.0835 0.0570  782  HIS A CB  
1747 C CG  . HIS A 245 ? 0.3921 0.3511 0.3463 -0.0466 -0.0975 0.0683  782  HIS A CG  
1748 N ND1 . HIS A 245 ? 0.3675 0.3227 0.3551 -0.0334 -0.0935 0.0649  782  HIS A ND1 
1749 C CD2 . HIS A 245 ? 0.4022 0.3646 0.3650 -0.0531 -0.1154 0.0826  782  HIS A CD2 
1750 C CE1 . HIS A 245 ? 0.3676 0.3238 0.3858 -0.0308 -0.1067 0.0751  782  HIS A CE1 
1751 N NE2 . HIS A 245 ? 0.3888 0.3495 0.3943 -0.0424 -0.1211 0.0873  782  HIS A NE2 
1752 N N   . PRO A 246 ? 0.2849 0.2416 0.2497 -0.0219 -0.0596 0.0273  783  PRO A N   
1753 C CA  . PRO A 246 ? 0.2664 0.2216 0.2465 -0.0116 -0.0488 0.0184  783  PRO A CA  
1754 C C   . PRO A 246 ? 0.2665 0.2174 0.2576 -0.0094 -0.0494 0.0234  783  PRO A C   
1755 O O   . PRO A 246 ? 0.2806 0.2300 0.2711 -0.0054 -0.0397 0.0162  783  PRO A O   
1756 C CB  . PRO A 246 ? 0.2561 0.2149 0.2602 -0.0050 -0.0503 0.0151  783  PRO A CB  
1757 C CG  . PRO A 246 ? 0.2989 0.2600 0.3104 -0.0102 -0.0650 0.0263  783  PRO A CG  
1758 C CD  . PRO A 246 ? 0.3141 0.2745 0.2937 -0.0217 -0.0693 0.0306  783  PRO A CD  
1759 N N   . ILE A 247 ? 0.2777 0.2265 0.2811 -0.0125 -0.0617 0.0366  784  ILE A N   
1760 C CA  . ILE A 247 ? 0.4497 0.3928 0.4657 -0.0115 -0.0634 0.0425  784  ILE A CA  
1761 C C   . ILE A 247 ? 0.4441 0.3862 0.4342 -0.0179 -0.0571 0.0432  784  ILE A C   
1762 O O   . ILE A 247 ? 0.2805 0.2194 0.2760 -0.0147 -0.0505 0.0390  784  ILE A O   
1763 C CB  . ILE A 247 ? 0.2950 0.2357 0.3309 -0.0152 -0.0803 0.0599  784  ILE A CB  
1764 C CG1 . ILE A 247 ? 0.2885 0.2311 0.3584 -0.0075 -0.0854 0.0584  784  ILE A CG1 
1765 C CG2 . ILE A 247 ? 0.3008 0.2340 0.3507 -0.0154 -0.0830 0.0674  784  ILE A CG2 
1766 C CD1 . ILE A 247 ? 0.3037 0.2447 0.3991 -0.0110 -0.1043 0.0777  784  ILE A CD1 
1767 N N   . GLU A 248 ? 0.4179 0.3640 0.3803 -0.0281 -0.0588 0.0476  785  GLU A N   
1768 C CA  . GLU A 248 ? 0.3803 0.3278 0.3196 -0.0357 -0.0520 0.0486  785  GLU A CA  
1769 C C   . GLU A 248 ? 0.3356 0.2850 0.2678 -0.0304 -0.0361 0.0327  785  GLU A C   
1770 O O   . GLU A 248 ? 0.3450 0.2947 0.2733 -0.0316 -0.0288 0.0317  785  GLU A O   
1771 C CB  . GLU A 248 ? 0.3771 0.3299 0.2878 -0.0498 -0.0571 0.0561  785  GLU A CB  
1772 C CG  . GLU A 248 ? 0.4074 0.3625 0.3006 -0.0614 -0.0564 0.0663  785  GLU A CG  
1773 C CD  . GLU A 248 ? 0.4282 0.3775 0.3434 -0.0615 -0.0678 0.0831  785  GLU A CD  
1774 O OE1 . GLU A 248 ? 0.4182 0.3651 0.3393 -0.0600 -0.0613 0.0830  785  GLU A OE1 
1775 O OE2 . GLU A 248 ? 0.3631 0.3101 0.2933 -0.0631 -0.0837 0.0967  785  GLU A OE2 
1776 N N   . ILE A 249 ? 0.3078 0.2588 0.2411 -0.0248 -0.0314 0.0217  786  ILE A N   
1777 C CA  . ILE A 249 ? 0.2995 0.2518 0.2325 -0.0192 -0.0188 0.0092  786  ILE A CA  
1778 C C   . ILE A 249 ? 0.2725 0.2224 0.2226 -0.0126 -0.0163 0.0081  786  ILE A C   
1779 O O   . ILE A 249 ? 0.2760 0.2271 0.2239 -0.0124 -0.0089 0.0048  786  ILE A O   
1780 C CB  . ILE A 249 ? 0.3151 0.2689 0.2510 -0.0148 -0.0169 0.0006  786  ILE A CB  
1781 C CG1 . ILE A 249 ? 0.2768 0.2326 0.1935 -0.0224 -0.0167 -0.0023 786  ILE A CG1 
1782 C CG2 . ILE A 249 ? 0.2480 0.2028 0.1913 -0.0081 -0.0073 -0.0084 786  ILE A CG2 
1783 C CD1 . ILE A 249 ? 0.2710 0.2270 0.1926 -0.0194 -0.0169 -0.0091 786  ILE A CD1 
1784 N N   . ALA A 250 ? 0.2632 0.2101 0.2321 -0.0078 -0.0224 0.0101  787  ALA A N   
1785 C CA  . ALA A 250 ? 0.2635 0.2076 0.2478 -0.0030 -0.0200 0.0068  787  ALA A CA  
1786 C C   . ALA A 250 ? 0.2622 0.2025 0.2466 -0.0078 -0.0224 0.0147  787  ALA A C   
1787 O O   . ALA A 250 ? 0.2546 0.1945 0.2411 -0.0071 -0.0171 0.0109  787  ALA A O   
1788 C CB  . ALA A 250 ? 0.2473 0.1894 0.2540 0.0026  -0.0242 0.0046  787  ALA A CB  
1789 N N   . ARG A 251 ? 0.2701 0.2083 0.2524 -0.0139 -0.0312 0.0272  788  ARG A N   
1790 C CA  . ARG A 251 ? 0.3150 0.2500 0.2980 -0.0200 -0.0343 0.0374  788  ARG A CA  
1791 C C   . ARG A 251 ? 0.2958 0.2363 0.2600 -0.0249 -0.0243 0.0348  788  ARG A C   
1792 O O   . ARG A 251 ? 0.2915 0.2307 0.2621 -0.0255 -0.0212 0.0350  788  ARG A O   
1793 C CB  . ARG A 251 ? 0.3330 0.2667 0.3137 -0.0282 -0.0469 0.0543  788  ARG A CB  
1794 C CG  . ARG A 251 ? 0.3211 0.2479 0.3316 -0.0240 -0.0589 0.0613  788  ARG A CG  
1795 C CD  . ARG A 251 ? 0.3311 0.2585 0.3373 -0.0339 -0.0735 0.0810  788  ARG A CD  
1796 N NE  . ARG A 251 ? 0.3325 0.2544 0.3727 -0.0295 -0.0868 0.0893  788  ARG A NE  
1797 C CZ  . ARG A 251 ? 0.3584 0.2811 0.4025 -0.0372 -0.1031 0.1084  788  ARG A CZ  
1798 N NH1 . ARG A 251 ? 0.3603 0.2894 0.3707 -0.0512 -0.1072 0.1199  788  ARG A NH1 
1799 N NH2 . ARG A 251 ? 0.3444 0.2623 0.4269 -0.0318 -0.1152 0.1158  788  ARG A NH2 
1800 N N   . GLN A 252 ? 0.2899 0.2369 0.2336 -0.0286 -0.0188 0.0311  789  GLN A N   
1801 C CA  . GLN A 252 ? 0.3193 0.2728 0.2485 -0.0340 -0.0082 0.0282  789  GLN A CA  
1802 C C   . GLN A 252 ? 0.3180 0.2735 0.2573 -0.0264 0.0011  0.0169  789  GLN A C   
1803 O O   . GLN A 252 ? 0.2742 0.2336 0.2149 -0.0289 0.0075  0.0169  789  GLN A O   
1804 C CB  . GLN A 252 ? 0.3024 0.2618 0.2089 -0.0406 -0.0042 0.0249  789  GLN A CB  
1805 C CG  . GLN A 252 ? 0.3241 0.2840 0.2156 -0.0518 -0.0146 0.0381  789  GLN A CG  
1806 C CD  . GLN A 252 ? 0.3396 0.3013 0.2264 -0.0617 -0.0166 0.0517  789  GLN A CD  
1807 O OE1 . GLN A 252 ? 0.3414 0.3087 0.2233 -0.0649 -0.0053 0.0481  789  GLN A OE1 
1808 N NE2 . GLN A 252 ? 0.3516 0.3091 0.2431 -0.0670 -0.0316 0.0686  789  GLN A NE2 
1809 N N   . LEU A 253 ? 0.2791 0.2333 0.2262 -0.0183 0.0013  0.0087  790  LEU A N   
1810 C CA  . LEU A 253 ? 0.2557 0.2122 0.2127 -0.0128 0.0070  0.0011  790  LEU A CA  
1811 C C   . LEU A 253 ? 0.2484 0.2016 0.2181 -0.0120 0.0038  0.0034  790  LEU A C   
1812 O O   . LEU A 253 ? 0.2395 0.1962 0.2146 -0.0120 0.0078  0.0012  790  LEU A O   
1813 C CB  . LEU A 253 ? 0.2363 0.1928 0.1971 -0.0065 0.0067  -0.0058 790  LEU A CB  
1814 C CG  . LEU A 253 ? 0.2890 0.2487 0.2420 -0.0065 0.0115  -0.0109 790  LEU A CG  
1815 C CD1 . LEU A 253 ? 0.2483 0.2075 0.2067 -0.0014 0.0096  -0.0150 790  LEU A CD1 
1816 C CD2 . LEU A 253 ? 0.2364 0.2012 0.1919 -0.0070 0.0204  -0.0147 790  LEU A CD2 
1817 N N   . THR A 254 ? 0.2488 0.1952 0.2263 -0.0117 -0.0039 0.0075  791  THR A N   
1818 C CA  . THR A 254 ? 0.2495 0.1910 0.2410 -0.0117 -0.0069 0.0079  791  THR A CA  
1819 C C   . THR A 254 ? 0.2623 0.2048 0.2521 -0.0186 -0.0059 0.0160  791  THR A C   
1820 O O   . THR A 254 ? 0.2645 0.2079 0.2619 -0.0195 -0.0041 0.0138  791  THR A O   
1821 C CB  . THR A 254 ? 0.2535 0.1867 0.2594 -0.0096 -0.0148 0.0100  791  THR A CB  
1822 O OG1 . THR A 254 ? 0.2456 0.1799 0.2555 -0.0034 -0.0136 0.0009  791  THR A OG1 
1823 C CG2 . THR A 254 ? 0.2577 0.1840 0.2805 -0.0104 -0.0176 0.0090  791  THR A CG2 
1824 N N   . LEU A 255 ? 0.2689 0.2128 0.2481 -0.0250 -0.0073 0.0259  792  LEU A N   
1825 C CA  . LEU A 255 ? 0.2792 0.2264 0.2551 -0.0334 -0.0049 0.0343  792  LEU A CA  
1826 C C   . LEU A 255 ? 0.3170 0.2741 0.2902 -0.0333 0.0063  0.0273  792  LEU A C   
1827 O O   . LEU A 255 ? 0.2727 0.2323 0.2550 -0.0362 0.0083  0.0295  792  LEU A O   
1828 C CB  . LEU A 255 ? 0.2967 0.2462 0.2566 -0.0425 -0.0076 0.0460  792  LEU A CB  
1829 C CG  . LEU A 255 ? 0.3081 0.2486 0.2761 -0.0451 -0.0214 0.0587  792  LEU A CG  
1830 C CD1 . LEU A 255 ? 0.3271 0.2726 0.2739 -0.0560 -0.0251 0.0707  792  LEU A CD1 
1831 C CD2 . LEU A 255 ? 0.3132 0.2463 0.3008 -0.0477 -0.0273 0.0672  792  LEU A CD2 
1832 N N   . LEU A 256 ? 0.3071 0.2697 0.2719 -0.0298 0.0129  0.0191  793  LEU A N   
1833 C CA  . LEU A 256 ? 0.2993 0.2712 0.2684 -0.0286 0.0230  0.0127  793  LEU A CA  
1834 C C   . LEU A 256 ? 0.2800 0.2515 0.2657 -0.0235 0.0205  0.0090  793  LEU A C   
1835 O O   . LEU A 256 ? 0.2802 0.2577 0.2764 -0.0258 0.0237  0.0103  793  LEU A O   
1836 C CB  . LEU A 256 ? 0.3132 0.2888 0.2743 -0.0256 0.0294  0.0043  793  LEU A CB  
1837 C CG  . LEU A 256 ? 0.3204 0.3029 0.2944 -0.0207 0.0371  -0.0035 793  LEU A CG  
1838 C CD1 . LEU A 256 ? 0.3487 0.3410 0.3300 -0.0255 0.0469  -0.0030 793  LEU A CD1 
1839 C CD2 . LEU A 256 ? 0.3065 0.2890 0.2747 -0.0177 0.0412  -0.0116 793  LEU A CD2 
1840 N N   . GLU A 257 ? 0.2786 0.2445 0.2665 -0.0179 0.0147  0.0046  794  GLU A N   
1841 C CA  . GLU A 257 ? 0.2324 0.1991 0.2310 -0.0155 0.0117  0.0008  794  GLU A CA  
1842 C C   . GLU A 257 ? 0.2958 0.2585 0.3031 -0.0197 0.0070  0.0038  794  GLU A C   
1843 O O   . GLU A 257 ? 0.2850 0.2509 0.3005 -0.0209 0.0053  0.0016  794  GLU A O   
1844 C CB  . GLU A 257 ? 0.2269 0.1900 0.2229 -0.0107 0.0081  -0.0052 794  GLU A CB  
1845 C CG  . GLU A 257 ? 0.2207 0.1886 0.2127 -0.0070 0.0119  -0.0082 794  GLU A CG  
1846 C CD  . GLU A 257 ? 0.2924 0.2574 0.2806 -0.0034 0.0090  -0.0125 794  GLU A CD  
1847 O OE1 . GLU A 257 ? 0.2744 0.2397 0.2577 -0.0012 0.0109  -0.0134 794  GLU A OE1 
1848 O OE2 . GLU A 257 ? 0.2176 0.1807 0.2084 -0.0035 0.0057  -0.0160 794  GLU A OE2 
1849 N N   . SER A 258 ? 0.3148 0.2702 0.3216 -0.0230 0.0036  0.0097  795  SER A N   
1850 C CA  . SER A 258 ? 0.3282 0.2783 0.3466 -0.0276 -0.0012 0.0133  795  SER A CA  
1851 C C   . SER A 258 ? 0.3531 0.3115 0.3759 -0.0336 0.0031  0.0193  795  SER A C   
1852 O O   . SER A 258 ? 0.2569 0.2159 0.2913 -0.0364 0.0005  0.0185  795  SER A O   
1853 C CB  . SER A 258 ? 0.3232 0.2628 0.3445 -0.0296 -0.0075 0.0205  795  SER A CB  
1854 O OG  . SER A 258 ? 0.3133 0.2460 0.3493 -0.0344 -0.0126 0.0245  795  SER A OG  
1855 N N   . ASP A 259 ? 0.3658 0.3317 0.3799 -0.0365 0.0102  0.0244  796  ASP A N   
1856 C CA  . ASP A 259 ? 0.3917 0.3681 0.4121 -0.0425 0.0169  0.0291  796  ASP A CA  
1857 C C   . ASP A 259 ? 0.3743 0.3602 0.4068 -0.0388 0.0205  0.0228  796  ASP A C   
1858 O O   . ASP A 259 ? 0.3958 0.3879 0.4428 -0.0428 0.0208  0.0259  796  ASP A O   
1859 C CB  . ASP A 259 ? 0.4126 0.3965 0.4189 -0.0473 0.0261  0.0330  796  ASP A CB  
1860 C CG  . ASP A 259 ? 0.4596 0.4368 0.4552 -0.0546 0.0205  0.0442  796  ASP A CG  
1861 O OD1 . ASP A 259 ? 0.4991 0.4663 0.5050 -0.0562 0.0106  0.0504  796  ASP A OD1 
1862 O OD2 . ASP A 259 ? 0.4747 0.4565 0.4525 -0.0595 0.0253  0.0469  796  ASP A OD2 
1863 N N   . LEU A 260 ? 0.3277 0.3153 0.3568 -0.0319 0.0221  0.0156  797  LEU A N   
1864 C CA  . LEU A 260 ? 0.3141 0.3104 0.3575 -0.0290 0.0228  0.0125  797  LEU A CA  
1865 C C   . LEU A 260 ? 0.3155 0.3091 0.3668 -0.0308 0.0127  0.0124  797  LEU A C   
1866 O O   . LEU A 260 ? 0.3122 0.3143 0.3791 -0.0336 0.0112  0.0149  797  LEU A O   
1867 C CB  . LEU A 260 ? 0.3030 0.2999 0.3419 -0.0221 0.0248  0.0067  797  LEU A CB  
1868 C CG  . LEU A 260 ? 0.3151 0.3145 0.3460 -0.0211 0.0350  0.0039  797  LEU A CG  
1869 C CD1 . LEU A 260 ? 0.3091 0.3063 0.3367 -0.0147 0.0349  -0.0019 797  LEU A CD1 
1870 C CD2 . LEU A 260 ? 0.3161 0.3279 0.3618 -0.0236 0.0460  0.0039  797  LEU A CD2 
1871 N N   . TYR A 261 ? 0.3187 0.3013 0.3606 -0.0301 0.0060  0.0087  798  TYR A N   
1872 C CA  . TYR A 261 ? 0.3130 0.2928 0.3594 -0.0333 -0.0023 0.0050  798  TYR A CA  
1873 C C   . TYR A 261 ? 0.3095 0.2882 0.3676 -0.0404 -0.0051 0.0096  798  TYR A C   
1874 O O   . TYR A 261 ? 0.2478 0.2306 0.3147 -0.0450 -0.0108 0.0086  798  TYR A O   
1875 C CB  . TYR A 261 ? 0.2961 0.2648 0.3323 -0.0309 -0.0060 -0.0028 798  TYR A CB  
1876 C CG  . TYR A 261 ? 0.3046 0.2702 0.3428 -0.0355 -0.0127 -0.0104 798  TYR A CG  
1877 C CD1 . TYR A 261 ? 0.3048 0.2777 0.3370 -0.0370 -0.0157 -0.0151 798  TYR A CD1 
1878 C CD2 . TYR A 261 ? 0.3192 0.2747 0.3651 -0.0397 -0.0163 -0.0130 798  TYR A CD2 
1879 C CE1 . TYR A 261 ? 0.3126 0.2842 0.3423 -0.0436 -0.0212 -0.0237 798  TYR A CE1 
1880 C CE2 . TYR A 261 ? 0.3340 0.2864 0.3813 -0.0449 -0.0214 -0.0231 798  TYR A CE2 
1881 C CZ  . TYR A 261 ? 0.3359 0.2969 0.3729 -0.0474 -0.0234 -0.0292 798  TYR A CZ  
1882 O OH  . TYR A 261 ? 0.3606 0.3197 0.3946 -0.0549 -0.0280 -0.0409 798  TYR A OH  
1883 N N   A ARG A 262 ? 0.3047 0.2785 0.3631 -0.0427 -0.0023 0.0157  799  ARG A N   
1884 N N   B ARG A 262 ? 0.3045 0.2785 0.3628 -0.0426 -0.0022 0.0157  799  ARG A N   
1885 C CA  A ARG A 262 ? 0.3201 0.2918 0.3910 -0.0503 -0.0055 0.0215  799  ARG A CA  
1886 C CA  B ARG A 262 ? 0.3192 0.2908 0.3898 -0.0503 -0.0054 0.0217  799  ARG A CA  
1887 C C   A ARG A 262 ? 0.2984 0.2850 0.3832 -0.0545 -0.0019 0.0269  799  ARG A C   
1888 C C   B ARG A 262 ? 0.2987 0.2851 0.3833 -0.0546 -0.0016 0.0273  799  ARG A C   
1889 O O   A ARG A 262 ? 0.3082 0.2957 0.4065 -0.0610 -0.0073 0.0291  799  ARG A O   
1890 O O   B ARG A 262 ? 0.3086 0.2955 0.4067 -0.0613 -0.0067 0.0300  799  ARG A O   
1891 C CB  A ARG A 262 ? 0.3131 0.2775 0.3806 -0.0532 -0.0042 0.0301  799  ARG A CB  
1892 C CB  B ARG A 262 ? 0.3132 0.2770 0.3797 -0.0528 -0.0042 0.0299  799  ARG A CB  
1893 C CG  A ARG A 262 ? 0.3314 0.2942 0.4128 -0.0623 -0.0070 0.0392  799  ARG A CG  
1894 C CG  B ARG A 262 ? 0.3297 0.2964 0.4075 -0.0620 -0.0036 0.0411  799  ARG A CG  
1895 C CD  A ARG A 262 ? 0.3453 0.3029 0.4218 -0.0669 -0.0065 0.0513  799  ARG A CD  
1896 C CD  B ARG A 262 ? 0.3450 0.3035 0.4174 -0.0662 -0.0051 0.0520  799  ARG A CD  
1897 N NE  A ARG A 262 ? 0.3437 0.3113 0.4035 -0.0659 0.0030  0.0544  799  ARG A NE  
1898 N NE  B ARG A 262 ? 0.3494 0.3051 0.4048 -0.0607 -0.0034 0.0505  799  ARG A NE  
1899 C CZ  A ARG A 262 ? 0.3483 0.3315 0.4073 -0.0705 0.0135  0.0582  799  ARG A CZ  
1900 C CZ  B ARG A 262 ? 0.3621 0.3043 0.4169 -0.0587 -0.0111 0.0523  799  ARG A CZ  
1901 N NH1 A ARG A 262 ? 0.3503 0.3416 0.4261 -0.0759 0.0152  0.0615  799  ARG A NH1 
1902 N NH1 B ARG A 262 ? 0.3717 0.3009 0.4434 -0.0613 -0.0201 0.0548  799  ARG A NH1 
1903 N NH2 A ARG A 262 ? 0.3526 0.3436 0.3952 -0.0701 0.0228  0.0577  799  ARG A NH2 
1904 N NH2 B ARG A 262 ? 0.3559 0.2976 0.3963 -0.0544 -0.0100 0.0516  799  ARG A NH2 
1905 N N   . LYS A 263 ? 0.2925 0.2911 0.3774 -0.0511 0.0071  0.0282  800  LYS A N   
1906 C CA  . LYS A 263 ? 0.2873 0.3015 0.3909 -0.0544 0.0129  0.0331  800  LYS A CA  
1907 C C   . LYS A 263 ? 0.2760 0.2992 0.3955 -0.0532 0.0068  0.0314  800  LYS A C   
1908 O O   . LYS A 263 ? 0.2876 0.3250 0.4287 -0.0552 0.0107  0.0358  800  LYS A O   
1909 C CB  . LYS A 263 ? 0.3016 0.3253 0.4024 -0.0517 0.0270  0.0331  800  LYS A CB  
1910 C CG  . LYS A 263 ? 0.3247 0.3443 0.4096 -0.0568 0.0330  0.0378  800  LYS A CG  
1911 C CD  . LYS A 263 ? 0.3480 0.3778 0.4259 -0.0557 0.0478  0.0345  800  LYS A CD  
1912 C CE  . LYS A 263 ? 0.3814 0.4089 0.4390 -0.0638 0.0523  0.0408  800  LYS A CE  
1913 N NZ  . LYS A 263 ? 0.3995 0.4367 0.4450 -0.0645 0.0671  0.0347  800  LYS A NZ  
1914 N N   . VAL A 264 ? 0.2702 0.2870 0.3808 -0.0511 -0.0027 0.0259  801  VAL A N   
1915 C CA  . VAL A 264 ? 0.2672 0.2935 0.3903 -0.0526 -0.0109 0.0269  801  VAL A CA  
1916 C C   . VAL A 264 ? 0.2688 0.2964 0.4033 -0.0621 -0.0201 0.0295  801  VAL A C   
1917 O O   . VAL A 264 ? 0.2796 0.2947 0.4040 -0.0665 -0.0251 0.0247  801  VAL A O   
1918 C CB  . VAL A 264 ? 0.2729 0.2939 0.3787 -0.0497 -0.0175 0.0208  801  VAL A CB  
1919 C CG1 . VAL A 264 ? 0.2756 0.3072 0.3915 -0.0544 -0.0287 0.0245  801  VAL A CG1 
1920 C CG2 . VAL A 264 ? 0.2614 0.2817 0.3594 -0.0409 -0.0093 0.0191  801  VAL A CG2 
1921 N N   . GLN A 265 ? 0.2773 0.3199 0.4361 -0.0654 -0.0225 0.0365  802  GLN A N   
1922 C CA  . GLN A 265 ? 0.2887 0.3347 0.4609 -0.0755 -0.0327 0.0396  802  GLN A CA  
1923 C C   . GLN A 265 ? 0.2937 0.3444 0.4638 -0.0802 -0.0474 0.0388  802  GLN A C   
1924 O O   . GLN A 265 ? 0.3215 0.3811 0.4959 -0.0759 -0.0492 0.0425  802  GLN A O   
1925 C CB  . GLN A 265 ? 0.2875 0.3494 0.4909 -0.0780 -0.0272 0.0491  802  GLN A CB  
1926 C CG  . GLN A 265 ? 0.2917 0.3526 0.4950 -0.0761 -0.0116 0.0507  802  GLN A CG  
1927 C CD  . GLN A 265 ? 0.2958 0.3408 0.4841 -0.0818 -0.0136 0.0496  802  GLN A CD  
1928 O OE1 . GLN A 265 ? 0.3136 0.3522 0.5047 -0.0893 -0.0249 0.0488  802  GLN A OE1 
1929 N NE2 . GLN A 265 ? 0.2761 0.3142 0.4498 -0.0790 -0.0034 0.0499  802  GLN A NE2 
1930 N N   . PRO A 266 ? 0.2990 0.3439 0.4625 -0.0902 -0.0585 0.0343  803  PRO A N   
1931 C CA  . PRO A 266 ? 0.3075 0.3580 0.4631 -0.0979 -0.0731 0.0329  803  PRO A CA  
1932 C C   . PRO A 266 ? 0.3114 0.3819 0.4917 -0.0998 -0.0811 0.0463  803  PRO A C   
1933 O O   . PRO A 266 ? 0.3153 0.3920 0.4869 -0.1025 -0.0909 0.0489  803  PRO A O   
1934 C CB  . PRO A 266 ? 0.3309 0.3736 0.4831 -0.1100 -0.0818 0.0258  803  PRO A CB  
1935 C CG  . PRO A 266 ? 0.3320 0.3584 0.4812 -0.1058 -0.0714 0.0201  803  PRO A CG  
1936 C CD  . PRO A 266 ? 0.3172 0.3492 0.4790 -0.0958 -0.0582 0.0296  803  PRO A CD  
1937 N N   . SER A 267 ? 0.3089 0.3907 0.5220 -0.0991 -0.0776 0.0558  804  SER A N   
1938 C CA  . SER A 267 ? 0.3111 0.4129 0.5560 -0.1002 -0.0855 0.0691  804  SER A CA  
1939 C C   . SER A 267 ? 0.3151 0.4214 0.5636 -0.0896 -0.0812 0.0729  804  SER A C   
1940 O O   . SER A 267 ? 0.2560 0.3750 0.5217 -0.0918 -0.0934 0.0836  804  SER A O   
1941 C CB  . SER A 267 ? 0.3033 0.4171 0.5861 -0.1000 -0.0783 0.0766  804  SER A CB  
1942 O OG  . SER A 267 ? 0.2493 0.3600 0.5345 -0.0896 -0.0579 0.0732  804  SER A OG  
1943 N N   . GLU A 268 ? 0.3054 0.4011 0.5391 -0.0789 -0.0653 0.0653  805  GLU A N   
1944 C CA  . GLU A 268 ? 0.2900 0.3882 0.5284 -0.0689 -0.0603 0.0674  805  GLU A CA  
1945 C C   . GLU A 268 ? 0.3096 0.4058 0.5267 -0.0724 -0.0738 0.0691  805  GLU A C   
1946 O O   . GLU A 268 ? 0.2380 0.3378 0.4638 -0.0660 -0.0737 0.0743  805  GLU A O   
1947 C CB  . GLU A 268 ? 0.2686 0.3551 0.4909 -0.0590 -0.0417 0.0576  805  GLU A CB  
1948 C CG  . GLU A 268 ? 0.2740 0.3629 0.5100 -0.0579 -0.0274 0.0561  805  GLU A CG  
1949 C CD  . GLU A 268 ? 0.2839 0.3637 0.5029 -0.0502 -0.0105 0.0481  805  GLU A CD  
1950 O OE1 . GLU A 268 ? 0.2913 0.3700 0.5082 -0.0424 -0.0061 0.0454  805  GLU A OE1 
1951 O OE2 . GLU A 268 ? 0.2939 0.3679 0.5020 -0.0530 -0.0028 0.0454  805  GLU A OE2 
1952 N N   . LEU A 269 ? 0.3345 0.4252 0.5245 -0.0832 -0.0847 0.0643  806  LEU A N   
1953 C CA  . LEU A 269 ? 0.3494 0.4400 0.5139 -0.0896 -0.0962 0.0646  806  LEU A CA  
1954 C C   . LEU A 269 ? 0.3459 0.4505 0.5171 -0.1041 -0.1170 0.0755  806  LEU A C   
1955 O O   . LEU A 269 ? 0.3466 0.4564 0.5031 -0.1104 -0.1282 0.0814  806  LEU A O   
1956 C CB  . LEU A 269 ? 0.3690 0.4436 0.4937 -0.0922 -0.0914 0.0478  806  LEU A CB  
1957 C CG  . LEU A 269 ? 0.3707 0.4315 0.4853 -0.0796 -0.0739 0.0382  806  LEU A CG  
1958 C CD1 . LEU A 269 ? 0.3786 0.4267 0.4862 -0.0805 -0.0673 0.0274  806  LEU A CD1 
1959 C CD2 . LEU A 269 ? 0.3889 0.4441 0.4759 -0.0777 -0.0725 0.0322  806  LEU A CD2 
1960 N N   . VAL A 270 ? 0.3487 0.4601 0.5410 -0.1108 -0.1231 0.0793  807  VAL A N   
1961 C CA  . VAL A 270 ? 0.3568 0.4824 0.5560 -0.1263 -0.1447 0.0903  807  VAL A CA  
1962 C C   . VAL A 270 ? 0.3683 0.5105 0.6012 -0.1237 -0.1549 0.1108  807  VAL A C   
1963 O O   . VAL A 270 ? 0.3447 0.4906 0.6135 -0.1103 -0.1444 0.1163  807  VAL A O   
1964 C CB  . VAL A 270 ? 0.3488 0.4779 0.5673 -0.1337 -0.1484 0.0898  807  VAL A CB  
1965 C CG1 . VAL A 270 ? 0.3607 0.5037 0.5806 -0.1523 -0.1726 0.0995  807  VAL A CG1 
1966 C CG2 . VAL A 270 ? 0.3477 0.4583 0.5410 -0.1341 -0.1370 0.0708  807  VAL A CG2 
1967 N N   . GLY A 271 ? 0.4246 0.5772 0.6472 -0.1373 -0.1756 0.1222  808  GLY A N   
1968 C CA  . GLY A 271 ? 0.4534 0.6226 0.7125 -0.1372 -0.1900 0.1453  808  GLY A CA  
1969 C C   . GLY A 271 ? 0.4659 0.6315 0.7333 -0.1236 -0.1816 0.1500  808  GLY A C   
1970 O O   . GLY A 271 ? 0.4715 0.6463 0.7772 -0.1188 -0.1888 0.1677  808  GLY A O   
1971 N N   . SER A 272 ? 0.4778 0.6272 0.7102 -0.1162 -0.1652 0.1338  809  SER A N   
1972 C CA  . SER A 272 ? 0.4878 0.6318 0.7269 -0.1030 -0.1555 0.1357  809  SER A CA  
1973 C C   . SER A 272 ? 0.4620 0.6104 0.7556 -0.0880 -0.1458 0.1413  809  SER A C   
1974 O O   . SER A 272 ? 0.4608 0.6123 0.7816 -0.0806 -0.1473 0.1518  809  SER A O   
1975 C CB  . SER A 272 ? 0.5256 0.6771 0.7546 -0.1122 -0.1732 0.1521  809  SER A CB  
1976 O OG  . SER A 272 ? 0.5589 0.7053 0.7330 -0.1245 -0.1757 0.1422  809  SER A OG  
1977 N N   . VAL A 273 ? 0.4387 0.5876 0.7497 -0.0841 -0.1350 0.1334  810  VAL A N   
1978 C CA  . VAL A 273 ? 0.4047 0.5604 0.7674 -0.0716 -0.1230 0.1358  810  VAL A CA  
1979 C C   . VAL A 273 ? 0.3830 0.5271 0.7435 -0.0566 -0.1023 0.1244  810  VAL A C   
1980 O O   . VAL A 273 ? 0.3655 0.5150 0.7691 -0.0460 -0.0920 0.1254  810  VAL A O   
1981 C CB  . VAL A 273 ? 0.3882 0.5480 0.7642 -0.0732 -0.1147 0.1294  810  VAL A CB  
1982 C CG1 . VAL A 273 ? 0.4011 0.5753 0.7921 -0.0876 -0.1365 0.1429  810  VAL A CG1 
1983 C CG2 . VAL A 273 ? 0.3848 0.5277 0.7139 -0.0738 -0.1013 0.1108  810  VAL A CG2 
1984 N N   . TRP A 274 ? 0.3898 0.5184 0.7027 -0.0558 -0.0954 0.1123  811  TRP A N   
1985 C CA  . TRP A 274 ? 0.3870 0.5050 0.6966 -0.0432 -0.0784 0.1025  811  TRP A CA  
1986 C C   . TRP A 274 ? 0.3873 0.5071 0.7137 -0.0399 -0.0870 0.1139  811  TRP A C   
1987 O O   . TRP A 274 ? 0.3846 0.4976 0.7210 -0.0291 -0.0741 0.1074  811  TRP A O   
1988 C CB  . TRP A 274 ? 0.3959 0.4977 0.6539 -0.0433 -0.0686 0.0867  811  TRP A CB  
1989 C CG  . TRP A 274 ? 0.4120 0.5078 0.6344 -0.0489 -0.0783 0.0880  811  TRP A CG  
1990 C CD1 . TRP A 274 ? 0.4142 0.5028 0.6258 -0.0431 -0.0742 0.0862  811  TRP A CD1 
1991 C CD2 . TRP A 274 ? 0.4358 0.5333 0.6280 -0.0626 -0.0924 0.0897  811  TRP A CD2 
1992 N NE1 . TRP A 274 ? 0.4301 0.5170 0.6077 -0.0522 -0.0842 0.0879  811  TRP A NE1 
1993 C CE2 . TRP A 274 ? 0.4363 0.5287 0.6003 -0.0645 -0.0949 0.0891  811  TRP A CE2 
1994 C CE3 . TRP A 274 ? 0.4526 0.5558 0.6389 -0.0744 -0.1028 0.0907  811  TRP A CE3 
1995 C CZ2 . TRP A 274 ? 0.4460 0.5402 0.5752 -0.0780 -0.1056 0.0884  811  TRP A CZ2 
1996 C CZ3 . TRP A 274 ? 0.4655 0.5689 0.6166 -0.0879 -0.1143 0.0890  811  TRP A CZ3 
1997 C CH2 . TRP A 274 ? 0.4644 0.5639 0.5868 -0.0897 -0.1148 0.0874  811  TRP A CH2 
1998 N N   . THR A 275 ? 0.4054 0.5344 0.7354 -0.0503 -0.1092 0.1314  812  THR A N   
1999 C CA  . THR A 275 ? 0.4221 0.5549 0.7759 -0.0491 -0.1211 0.1477  812  THR A CA  
2000 C C   . THR A 275 ? 0.4487 0.5983 0.8604 -0.0508 -0.1362 0.1675  812  THR A C   
2001 O O   . THR A 275 ? 0.4720 0.6268 0.8917 -0.0585 -0.1561 0.1875  812  THR A O   
2002 C CB  . THR A 275 ? 0.4398 0.5713 0.7510 -0.0618 -0.1366 0.1557  812  THR A CB  
2003 O OG1 . THR A 275 ? 0.4628 0.6078 0.7703 -0.0778 -0.1579 0.1698  812  THR A OG1 
2004 C CG2 . THR A 275 ? 0.4410 0.5587 0.6962 -0.0624 -0.1233 0.1356  812  THR A CG2 
2005 N N   . LYS A 276 ? 0.4524 0.6087 0.9013 -0.0443 -0.1257 0.1622  813  LYS A N   
2006 C CA  . LYS A 276 ? 0.4704 0.6339 0.9628 -0.0447 -0.1346 0.1767  813  LYS A CA  
2007 C C   . LYS A 276 ? 0.4647 0.6271 1.0041 -0.0295 -0.1131 0.1662  813  LYS A C   
2008 O O   . LYS A 276 ? 0.4397 0.5987 0.9794 -0.0197 -0.0929 0.1490  813  LYS A O   
2009 C CB  . LYS A 276 ? 0.4899 0.6616 0.9689 -0.0576 -0.1465 0.1815  813  LYS A CB  
2010 C CG  . LYS A 276 ? 0.5183 0.6902 0.9579 -0.0744 -0.1699 0.1952  813  LYS A CG  
2011 C CD  . LYS A 276 ? 0.5370 0.7157 0.9637 -0.0874 -0.1810 0.1979  813  LYS A CD  
2012 C CE  . LYS A 276 ? 0.5695 0.7484 0.9554 -0.1052 -0.2023 0.2101  813  LYS A CE  
2013 N NZ  . LYS A 276 ? 0.5902 0.7747 0.9618 -0.1188 -0.2132 0.2112  813  LYS A NZ  
2014 N N   . GLU A 277 ? 0.4933 0.6589 1.0711 -0.0288 -0.1171 0.1758  814  GLU A N   
2015 C CA  . GLU A 277 ? 0.5081 0.6709 1.1347 -0.0158 -0.0994 0.1682  814  GLU A CA  
2016 C C   . GLU A 277 ? 0.4991 0.6656 1.1263 -0.0079 -0.0722 0.1447  814  GLU A C   
2017 O O   . GLU A 277 ? 0.4926 0.6525 1.1311 0.0025  -0.0527 0.1295  814  GLU A O   
2018 C CB  . GLU A 277 ? 0.5346 0.7023 1.2012 -0.0187 -0.1099 0.1831  814  GLU A CB  
2019 C CG  . GLU A 277 ? 0.5680 0.7288 1.2876 -0.0090 -0.1020 0.1837  814  GLU A CG  
2020 C CD  . GLU A 277 ? 0.6188 0.7841 1.3797 -0.0134 -0.1159 0.2019  814  GLU A CD  
2021 O OE1 . GLU A 277 ? 0.6249 0.8006 1.4001 -0.0137 -0.1107 0.1987  814  GLU A OE1 
2022 O OE2 . GLU A 277 ? 0.6464 0.8052 1.4265 -0.0173 -0.1324 0.2205  814  GLU A OE2 
2023 N N   . ASP A 278 ? 0.4986 0.6749 1.1119 -0.0143 -0.0702 0.1412  815  ASP A N   
2024 C CA  . ASP A 278 ? 0.4871 0.6681 1.0980 -0.0101 -0.0448 0.1217  815  ASP A CA  
2025 C C   . ASP A 278 ? 0.4385 0.6171 1.0046 -0.0142 -0.0401 0.1121  815  ASP A C   
2026 O O   . ASP A 278 ? 0.4394 0.6176 0.9793 -0.0195 -0.0314 0.1041  815  ASP A O   
2027 C CB  . ASP A 278 ? 0.5231 0.7155 1.1495 -0.0156 -0.0440 0.1244  815  ASP A CB  
2028 C CG  . ASP A 278 ? 0.5549 0.7503 1.2306 -0.0111 -0.0465 0.1327  815  ASP A CG  
2029 O OD1 . ASP A 278 ? 0.5696 0.7571 1.2649 -0.0066 -0.0549 0.1409  815  ASP A OD1 
2030 O OD2 . ASP A 278 ? 0.5620 0.7675 1.2584 -0.0127 -0.0400 0.1316  815  ASP A OD2 
2031 N N   . LYS A 279 ? 0.4054 0.5699 0.9414 -0.0118 -0.0442 0.1107  816  LYS A N   
2032 C CA  . LYS A 279 ? 0.3796 0.5272 0.8486 -0.0155 -0.0402 0.0998  816  LYS A CA  
2033 C C   . LYS A 279 ? 0.3665 0.5078 0.8181 -0.0104 -0.0139 0.0799  816  LYS A C   
2034 O O   . LYS A 279 ? 0.3618 0.4950 0.7696 -0.0159 -0.0103 0.0730  816  LYS A O   
2035 C CB  . LYS A 279 ? 0.3689 0.5043 0.8151 -0.0135 -0.0482 0.1024  816  LYS A CB  
2036 C CG  . LYS A 279 ? 0.3543 0.4862 0.8327 -0.0013 -0.0363 0.0967  816  LYS A CG  
2037 C CD  . LYS A 279 ? 0.3466 0.4636 0.7920 0.0001  -0.0401 0.0955  816  LYS A CD  
2038 C CE  . LYS A 279 ? 0.3536 0.4743 0.8093 -0.0058 -0.0653 0.1174  816  LYS A CE  
2039 N NZ  . LYS A 279 ? 0.3589 0.4853 0.8775 0.0017  -0.0693 0.1277  816  LYS A NZ  
2040 N N   . GLU A 280 ? 0.3598 0.5054 0.8463 -0.0010 0.0045  0.0705  817  GLU A N   
2041 C CA  . GLU A 280 ? 0.3451 0.4856 0.8102 0.0018  0.0295  0.0515  817  GLU A CA  
2042 C C   . GLU A 280 ? 0.3646 0.5147 0.8271 -0.0050 0.0380  0.0497  817  GLU A C   
2043 O O   . GLU A 280 ? 0.3880 0.5314 0.8132 -0.0081 0.0511  0.0393  817  GLU A O   
2044 C CB  . GLU A 280 ? 0.3293 0.4736 0.8337 0.0120  0.0481  0.0395  817  GLU A CB  
2045 C CG  . GLU A 280 ? 0.3237 0.4587 0.8414 0.0191  0.0395  0.0425  817  GLU A CG  
2046 C CD  . GLU A 280 ? 0.3252 0.4410 0.7872 0.0189  0.0397  0.0350  817  GLU A CD  
2047 O OE1 . GLU A 280 ? 0.3263 0.4360 0.7474 0.0161  0.0531  0.0223  817  GLU A OE1 
2048 O OE2 . GLU A 280 ? 0.3202 0.4281 0.7813 0.0208  0.0257  0.0432  817  GLU A OE2 
2049 N N   . ILE A 281 ? 0.3602 0.5263 0.8626 -0.0085 0.0294  0.0612  818  ILE A N   
2050 C CA  . ILE A 281 ? 0.3605 0.5374 0.8663 -0.0159 0.0367  0.0612  818  ILE A CA  
2051 C C   . ILE A 281 ? 0.3354 0.5040 0.8002 -0.0266 0.0196  0.0687  818  ILE A C   
2052 O O   . ILE A 281 ? 0.3375 0.5029 0.7765 -0.0327 0.0280  0.0640  818  ILE A O   
2053 C CB  . ILE A 281 ? 0.3877 0.5873 0.9613 -0.0147 0.0363  0.0694  818  ILE A CB  
2054 C CG1 . ILE A 281 ? 0.4081 0.6087 1.0076 -0.0043 0.0591  0.0549  818  ILE A CG1 
2055 C CG2 . ILE A 281 ? 0.4003 0.6110 0.9772 -0.0245 0.0369  0.0741  818  ILE A CG2 
2056 C CD1 . ILE A 281 ? 0.4150 0.6193 0.9956 -0.0064 0.0872  0.0378  818  ILE A CD1 
2057 N N   . ASN A 282 ? 0.3055 0.4703 0.7639 -0.0301 -0.0042 0.0803  819  ASN A N   
2058 C CA  . ASN A 282 ? 0.2725 0.4314 0.6987 -0.0414 -0.0208 0.0858  819  ASN A CA  
2059 C C   . ASN A 282 ? 0.2550 0.3931 0.6231 -0.0426 -0.0215 0.0772  819  ASN A C   
2060 O O   . ASN A 282 ? 0.2529 0.3838 0.5928 -0.0512 -0.0292 0.0765  819  ASN A O   
2061 C CB  . ASN A 282 ? 0.2700 0.4376 0.7154 -0.0477 -0.0465 0.1018  819  ASN A CB  
2062 C CG  . ASN A 282 ? 0.2835 0.4731 0.7918 -0.0475 -0.0496 0.1130  819  ASN A CG  
2063 O OD1 . ASN A 282 ? 0.2899 0.4895 0.8211 -0.0478 -0.0358 0.1094  819  ASN A OD1 
2064 N ND2 . ASN A 282 ? 0.2894 0.4869 0.8264 -0.0476 -0.0680 0.1276  819  ASN A ND2 
2065 N N   . SER A 283 ? 0.2528 0.3812 0.6055 -0.0342 -0.0137 0.0701  820  SER A N   
2066 C CA  . SER A 283 ? 0.2408 0.3509 0.5429 -0.0350 -0.0148 0.0626  820  SER A CA  
2067 C C   . SER A 283 ? 0.2350 0.3363 0.5216 -0.0270 0.0040  0.0505  820  SER A C   
2068 O O   . SER A 283 ? 0.2193 0.3104 0.4854 -0.0227 0.0029  0.0468  820  SER A O   
2069 C CB  . SER A 283 ? 0.2390 0.3454 0.5290 -0.0367 -0.0324 0.0691  820  SER A CB  
2070 O OG  . SER A 283 ? 0.2427 0.3569 0.5381 -0.0470 -0.0511 0.0794  820  SER A OG  
2071 N N   . PRO A 284 ? 0.2365 0.3423 0.5299 -0.0265 0.0214  0.0443  821  PRO A N   
2072 C CA  . PRO A 284 ? 0.2288 0.3278 0.5058 -0.0209 0.0387  0.0326  821  PRO A CA  
2073 C C   . PRO A 284 ? 0.2353 0.3169 0.4648 -0.0223 0.0363  0.0279  821  PRO A C   
2074 O O   . PRO A 284 ? 0.2477 0.3210 0.4622 -0.0169 0.0402  0.0215  821  PRO A O   
2075 C CB  . PRO A 284 ? 0.2356 0.3461 0.5274 -0.0239 0.0564  0.0287  821  PRO A CB  
2076 C CG  . PRO A 284 ? 0.2439 0.3594 0.5404 -0.0326 0.0468  0.0381  821  PRO A CG  
2077 C CD  . PRO A 284 ? 0.2358 0.3530 0.5476 -0.0329 0.0261  0.0477  821  PRO A CD  
2078 N N   . ASN A 285 ? 0.2368 0.3123 0.4455 -0.0295 0.0295  0.0308  822  ASN A N   
2079 C CA  . ASN A 285 ? 0.2330 0.2925 0.4032 -0.0303 0.0278  0.0264  822  ASN A CA  
2080 C C   . ASN A 285 ? 0.2407 0.2914 0.3961 -0.0274 0.0157  0.0257  822  ASN A C   
2081 O O   . ASN A 285 ? 0.2135 0.2542 0.3467 -0.0237 0.0182  0.0202  822  ASN A O   
2082 C CB  . ASN A 285 ? 0.2386 0.2932 0.3978 -0.0384 0.0236  0.0296  822  ASN A CB  
2083 C CG  . ASN A 285 ? 0.2567 0.3216 0.4302 -0.0434 0.0353  0.0324  822  ASN A CG  
2084 O OD1 . ASN A 285 ? 0.2363 0.2999 0.3959 -0.0444 0.0473  0.0296  822  ASN A OD1 
2085 N ND2 . ASN A 285 ? 0.2300 0.3067 0.4309 -0.0478 0.0317  0.0386  822  ASN A ND2 
2086 N N   . LEU A 286 ? 0.2360 0.2919 0.4032 -0.0305 0.0022  0.0319  823  LEU A N   
2087 C CA  . LEU A 286 ? 0.2131 0.2640 0.3655 -0.0302 -0.0088 0.0323  823  LEU A CA  
2088 C C   . LEU A 286 ? 0.2080 0.2595 0.3674 -0.0224 -0.0046 0.0318  823  LEU A C   
2089 O O   . LEU A 286 ? 0.2641 0.3075 0.4028 -0.0204 -0.0070 0.0287  823  LEU A O   
2090 C CB  . LEU A 286 ? 0.2176 0.2769 0.3811 -0.0377 -0.0246 0.0405  823  LEU A CB  
2091 C CG  . LEU A 286 ? 0.2631 0.3253 0.4221 -0.0399 -0.0374 0.0462  823  LEU A CG  
2092 C CD1 . LEU A 286 ? 0.2228 0.2733 0.3470 -0.0397 -0.0371 0.0382  823  LEU A CD1 
2093 C CD2 . LEU A 286 ? 0.2688 0.3407 0.4350 -0.0508 -0.0539 0.0547  823  LEU A CD2 
2094 N N   . LEU A 287 ? 0.2050 0.2662 0.3968 -0.0180 0.0020  0.0341  824  LEU A N   
2095 C CA  . LEU A 287 ? 0.2715 0.3316 0.4745 -0.0105 0.0062  0.0324  824  LEU A CA  
2096 C C   . LEU A 287 ? 0.2727 0.3223 0.4521 -0.0063 0.0193  0.0208  824  LEU A C   
2097 O O   . LEU A 287 ? 0.2576 0.3008 0.4302 -0.0022 0.0191  0.0182  824  LEU A O   
2098 C CB  . LEU A 287 ? 0.2007 0.2734 0.4501 -0.0064 0.0112  0.0357  824  LEU A CB  
2099 C CG  . LEU A 287 ? 0.2509 0.3352 0.5310 -0.0098 -0.0050 0.0504  824  LEU A CG  
2100 C CD1 . LEU A 287 ? 0.2542 0.3516 0.5863 -0.0047 0.0026  0.0521  824  LEU A CD1 
2101 C CD2 . LEU A 287 ? 0.2461 0.3271 0.5206 -0.0106 -0.0201 0.0593  824  LEU A CD2 
2102 N N   . LYS A 288 ? 0.2888 0.3370 0.4557 -0.0087 0.0297  0.0150  825  LYS A N   
2103 C CA  . LYS A 288 ? 0.3069 0.3460 0.4483 -0.0070 0.0396  0.0060  825  LYS A CA  
2104 C C   . LYS A 288 ? 0.2984 0.3254 0.4091 -0.0078 0.0306  0.0058  825  LYS A C   
2105 O O   . LYS A 288 ? 0.2947 0.3143 0.3892 -0.0050 0.0343  0.0002  825  LYS A O   
2106 C CB  . LYS A 288 ? 0.3298 0.3716 0.4634 -0.0119 0.0507  0.0031  825  LYS A CB  
2107 C CG  . LYS A 288 ? 0.3566 0.4101 0.5137 -0.0109 0.0667  -0.0026 825  LYS A CG  
2108 C CD  . LYS A 288 ? 0.3885 0.4436 0.5258 -0.0177 0.0789  -0.0063 825  LYS A CD  
2109 C CE  . LYS A 288 ? 0.4129 0.4554 0.5137 -0.0187 0.0781  -0.0103 825  LYS A CE  
2110 N NZ  . LYS A 288 ? 0.4406 0.4848 0.5193 -0.0276 0.0864  -0.0101 825  LYS A NZ  
2111 N N   . MET A 289 ? 0.2974 0.3229 0.4014 -0.0121 0.0192  0.0108  826  MET A N   
2112 C CA  . MET A 289 ? 0.3101 0.3258 0.3893 -0.0129 0.0121  0.0088  826  MET A CA  
2113 C C   . MET A 289 ? 0.2949 0.3110 0.3746 -0.0100 0.0066  0.0102  826  MET A C   
2114 O O   . MET A 289 ? 0.2981 0.3071 0.3613 -0.0076 0.0075  0.0060  826  MET A O   
2115 C CB  . MET A 289 ? 0.3477 0.3624 0.4215 -0.0193 0.0033  0.0107  826  MET A CB  
2116 C CG  . MET A 289 ? 0.3925 0.3971 0.4437 -0.0206 -0.0012 0.0054  826  MET A CG  
2117 S SD  . MET A 289 ? 0.4322 0.4251 0.4685 -0.0183 0.0055  0.0009  826  MET A SD  
2118 C CE  . MET A 289 ? 0.4266 0.4102 0.4491 -0.0198 -0.0010 -0.0058 826  MET A CE  
2119 N N   . ILE A 290 ? 0.2850 0.3100 0.3854 -0.0110 0.0000  0.0176  827  ILE A N   
2120 C CA  . ILE A 290 ? 0.2727 0.2988 0.3757 -0.0099 -0.0067 0.0222  827  ILE A CA  
2121 C C   . ILE A 290 ? 0.2658 0.2876 0.3755 -0.0027 0.0020  0.0178  827  ILE A C   
2122 O O   . ILE A 290 ? 0.2566 0.2734 0.3546 -0.0015 0.0001  0.0170  827  ILE A O   
2123 C CB  . ILE A 290 ? 0.2705 0.3081 0.3990 -0.0134 -0.0174 0.0343  827  ILE A CB  
2124 C CG1 . ILE A 290 ? 0.2825 0.3243 0.4002 -0.0227 -0.0276 0.0376  827  ILE A CG1 
2125 C CG2 . ILE A 290 ? 0.2548 0.2939 0.3896 -0.0130 -0.0250 0.0423  827  ILE A CG2 
2126 C CD1 . ILE A 290 ? 0.2983 0.3530 0.4422 -0.0277 -0.0398 0.0509  827  ILE A CD1 
2127 N N   . ARG A 291 ? 0.2472 0.2715 0.3762 0.0012  0.0124  0.0138  828  ARG A N   
2128 C CA  . ARG A 291 ? 0.2395 0.2600 0.3778 0.0071  0.0211  0.0073  828  ARG A CA  
2129 C C   . ARG A 291 ? 0.2398 0.2505 0.3479 0.0075  0.0274  -0.0021 828  ARG A C   
2130 O O   . ARG A 291 ? 0.2466 0.2517 0.3524 0.0104  0.0290  -0.0059 828  ARG A O   
2131 C CB  . ARG A 291 ? 0.2548 0.2824 0.4232 0.0101  0.0325  0.0028  828  ARG A CB  
2132 C CG  . ARG A 291 ? 0.2566 0.2939 0.4648 0.0114  0.0251  0.0132  828  ARG A CG  
2133 C CD  . ARG A 291 ? 0.2930 0.3406 0.5322 0.0130  0.0361  0.0094  828  ARG A CD  
2134 N NE  . ARG A 291 ? 0.3183 0.3762 0.5993 0.0140  0.0262  0.0218  828  ARG A NE  
2135 C CZ  . ARG A 291 ? 0.3155 0.3856 0.6329 0.0150  0.0320  0.0224  828  ARG A CZ  
2136 N NH1 . ARG A 291 ? 0.3207 0.3947 0.6352 0.0146  0.0494  0.0107  828  ARG A NH1 
2137 N NH2 . ARG A 291 ? 0.3152 0.3949 0.6729 0.0156  0.0200  0.0360  828  ARG A NH2 
2138 N N   . HIS A 292 ? 0.2376 0.2460 0.3244 0.0040  0.0296  -0.0045 829  HIS A N   
2139 C CA  . HIS A 292 ? 0.2459 0.2456 0.3062 0.0035  0.0319  -0.0102 829  HIS A CA  
2140 C C   . HIS A 292 ? 0.2408 0.2355 0.2897 0.0043  0.0233  -0.0080 829  HIS A C   
2141 O O   . HIS A 292 ? 0.2386 0.2280 0.2786 0.0062  0.0250  -0.0122 829  HIS A O   
2142 C CB  . HIS A 292 ? 0.2646 0.2623 0.3085 -0.0009 0.0326  -0.0098 829  HIS A CB  
2143 C CG  . HIS A 292 ? 0.2744 0.2634 0.2953 -0.0016 0.0299  -0.0118 829  HIS A CG  
2144 N ND1 . HIS A 292 ? 0.2849 0.2704 0.2930 -0.0024 0.0355  -0.0163 829  HIS A ND1 
2145 C CD2 . HIS A 292 ? 0.2740 0.2580 0.2849 -0.0019 0.0222  -0.0104 829  HIS A CD2 
2146 C CE1 . HIS A 292 ? 0.2921 0.2710 0.2856 -0.0027 0.0297  -0.0154 829  HIS A CE1 
2147 N NE2 . HIS A 292 ? 0.2724 0.2502 0.2690 -0.0018 0.0226  -0.0127 829  HIS A NE2 
2148 N N   . THR A 293 ? 0.2368 0.2345 0.2855 0.0016  0.0144  -0.0021 830  THR A N   
2149 C CA  . THR A 293 ? 0.2277 0.2237 0.2649 0.0004  0.0078  -0.0006 830  THR A CA  
2150 C C   . THR A 293 ? 0.2478 0.2448 0.2962 0.0028  0.0062  0.0028  830  THR A C   
2151 O O   . THR A 293 ? 0.2738 0.2671 0.3121 0.0034  0.0058  0.0009  830  THR A O   
2152 C CB  . THR A 293 ? 0.2320 0.2332 0.2660 -0.0053 -0.0004 0.0038  830  THR A CB  
2153 O OG1 . THR A 293 ? 0.2376 0.2354 0.2625 -0.0075 0.0008  -0.0006 830  THR A OG1 
2154 C CG2 . THR A 293 ? 0.2325 0.2349 0.2536 -0.0085 -0.0055 0.0046  830  THR A CG2 
2155 N N   . THR A 294 ? 0.2504 0.2527 0.3235 0.0039  0.0049  0.0084  831  THR A N   
2156 C CA  . THR A 294 ? 0.2419 0.2438 0.3323 0.0064  0.0028  0.0125  831  THR A CA  
2157 C C   . THR A 294 ? 0.2508 0.2444 0.3381 0.0108  0.0117  0.0023  831  THR A C   
2158 O O   . THR A 294 ? 0.2615 0.2511 0.3450 0.0111  0.0094  0.0029  831  THR A O   
2159 C CB  . THR A 294 ? 0.2313 0.2397 0.3564 0.0080  0.0005  0.0196  831  THR A CB  
2160 O OG1 . THR A 294 ? 0.2515 0.2686 0.3784 0.0021  -0.0104 0.0307  831  THR A OG1 
2161 C CG2 . THR A 294 ? 0.2033 0.2095 0.3525 0.0110  -0.0024 0.0246  831  THR A CG2 
2162 N N   . ASN A 295 ? 0.2435 0.2353 0.3310 0.0128  0.0219  -0.0070 832  ASN A N   
2163 C CA  . ASN A 295 ? 0.2464 0.2316 0.3299 0.0150  0.0302  -0.0178 832  ASN A CA  
2164 C C   . ASN A 295 ? 0.2224 0.2018 0.2777 0.0130  0.0279  -0.0203 832  ASN A C   
2165 O O   . ASN A 295 ? 0.2172 0.1913 0.2708 0.0138  0.0285  -0.0244 832  ASN A O   
2166 C CB  . ASN A 295 ? 0.3129 0.3001 0.3981 0.0148  0.0422  -0.0273 832  ASN A CB  
2167 C CG  . ASN A 295 ? 0.3711 0.3622 0.4910 0.0184  0.0490  -0.0309 832  ASN A CG  
2168 O OD1 . ASN A 295 ? 0.3722 0.3595 0.5121 0.0217  0.0479  -0.0319 832  ASN A OD1 
2169 N ND2 . ASN A 295 ? 0.4193 0.4180 0.5505 0.0178  0.0560  -0.0325 832  ASN A ND2 
2170 N N   . LEU A 296 ? 0.2172 0.1974 0.2540 0.0104  0.0250  -0.0180 833  LEU A N   
2171 C CA  . LEU A 296 ? 0.2195 0.1950 0.2357 0.0091  0.0227  -0.0201 833  LEU A CA  
2172 C C   . LEU A 296 ? 0.2351 0.2109 0.2514 0.0092  0.0164  -0.0159 833  LEU A C   
2173 O O   . LEU A 296 ? 0.2480 0.2202 0.2571 0.0093  0.0159  -0.0186 833  LEU A O   
2174 C CB  . LEU A 296 ? 0.2371 0.2127 0.2404 0.0068  0.0211  -0.0188 833  LEU A CB  
2175 C CG  . LEU A 296 ? 0.2509 0.2217 0.2391 0.0061  0.0187  -0.0206 833  LEU A CG  
2176 C CD1 . LEU A 296 ? 0.2346 0.2020 0.2145 0.0046  0.0226  -0.0251 833  LEU A CD1 
2177 C CD2 . LEU A 296 ? 0.2658 0.2355 0.2485 0.0044  0.0157  -0.0185 833  LEU A CD2 
2178 N N   . THR A 297 ? 0.2305 0.2118 0.2548 0.0078  0.0113  -0.0086 834  THR A N   
2179 C CA  . THR A 297 ? 0.2384 0.2224 0.2611 0.0055  0.0059  -0.0034 834  THR A CA  
2180 C C   . THR A 297 ? 0.2466 0.2275 0.2832 0.0072  0.0058  -0.0018 834  THR A C   
2181 O O   . THR A 297 ? 0.2352 0.2147 0.2667 0.0062  0.0045  -0.0018 834  THR A O   
2182 C CB  . THR A 297 ? 0.2546 0.2468 0.2799 0.0010  -0.0004 0.0052  834  THR A CB  
2183 O OG1 . THR A 297 ? 0.2013 0.1950 0.2148 -0.0011 -0.0001 0.0017  834  THR A OG1 
2184 C CG2 . THR A 297 ? 0.2043 0.2016 0.2238 -0.0040 -0.0051 0.0112  834  THR A CG2 
2185 N N   . LEU A 298 ? 0.2472 0.2270 0.3049 0.0098  0.0073  -0.0010 835  LEU A N   
2186 C CA  . LEU A 298 ? 0.2382 0.2127 0.3133 0.0118  0.0080  -0.0020 835  LEU A CA  
2187 C C   . LEU A 298 ? 0.2507 0.2178 0.3138 0.0130  0.0142  -0.0142 835  LEU A C   
2188 O O   . LEU A 298 ? 0.2545 0.2168 0.3236 0.0128  0.0130  -0.0155 835  LEU A O   
2189 C CB  . LEU A 298 ? 0.2488 0.2235 0.3543 0.0152  0.0100  -0.0013 835  LEU A CB  
2190 C CG  . LEU A 298 ? 0.2686 0.2503 0.3957 0.0134  0.0002  0.0145  835  LEU A CG  
2191 C CD1 . LEU A 298 ? 0.2497 0.2312 0.4149 0.0180  0.0026  0.0145  835  LEU A CD1 
2192 C CD2 . LEU A 298 ? 0.2833 0.2654 0.4117 0.0092  -0.0090 0.0263  835  LEU A CD2 
2193 N N   . TRP A 299 ? 0.2699 0.2362 0.3162 0.0129  0.0195  -0.0219 836  TRP A N   
2194 C CA  . TRP A 299 ? 0.2952 0.2558 0.3278 0.0118  0.0235  -0.0318 836  TRP A CA  
2195 C C   . TRP A 299 ? 0.3057 0.2656 0.3254 0.0099  0.0177  -0.0290 836  TRP A C   
2196 O O   . TRP A 299 ? 0.2195 0.1750 0.2386 0.0087  0.0173  -0.0335 836  TRP A O   
2197 C CB  . TRP A 299 ? 0.2209 0.1826 0.2383 0.0101  0.0289  -0.0372 836  TRP A CB  
2198 C CG  . TRP A 299 ? 0.2574 0.2149 0.2580 0.0065  0.0314  -0.0455 836  TRP A CG  
2199 C CD1 . TRP A 299 ? 0.2877 0.2413 0.2908 0.0048  0.0375  -0.0565 836  TRP A CD1 
2200 C CD2 . TRP A 299 ? 0.2630 0.2202 0.2427 0.0031  0.0271  -0.0435 836  TRP A CD2 
2201 N NE1 . TRP A 299 ? 0.3028 0.2545 0.2834 -0.0009 0.0365  -0.0611 836  TRP A NE1 
2202 C CE2 . TRP A 299 ? 0.2880 0.2420 0.2556 -0.0017 0.0293  -0.0517 836  TRP A CE2 
2203 C CE3 . TRP A 299 ? 0.2668 0.2260 0.2392 0.0033  0.0212  -0.0359 836  TRP A CE3 
2204 C CZ2 . TRP A 299 ? 0.3006 0.2544 0.2489 -0.0069 0.0238  -0.0495 836  TRP A CZ2 
2205 C CZ3 . TRP A 299 ? 0.2884 0.2462 0.2465 -0.0002 0.0168  -0.0346 836  TRP A CZ3 
2206 C CH2 . TRP A 299 ? 0.3011 0.2567 0.2472 -0.0055 0.0171  -0.0398 836  TRP A CH2 
2207 N N   . PHE A 300 ? 0.2811 0.2459 0.2922 0.0092  0.0138  -0.0229 837  PHE A N   
2208 C CA  . PHE A 300 ? 0.2060 0.1724 0.2102 0.0078  0.0100  -0.0210 837  PHE A CA  
2209 C C   . PHE A 300 ? 0.2943 0.2614 0.3101 0.0066  0.0072  -0.0165 837  PHE A C   
2210 O O   . PHE A 300 ? 0.2084 0.1736 0.2238 0.0054  0.0058  -0.0182 837  PHE A O   
2211 C CB  . PHE A 300 ? 0.2169 0.1889 0.2141 0.0072  0.0085  -0.0178 837  PHE A CB  
2212 C CG  . PHE A 300 ? 0.2026 0.1725 0.1904 0.0078  0.0094  -0.0211 837  PHE A CG  
2213 C CD1 . PHE A 300 ? 0.2568 0.2233 0.2385 0.0075  0.0081  -0.0238 837  PHE A CD1 
2214 C CD2 . PHE A 300 ? 0.2014 0.1731 0.1880 0.0077  0.0101  -0.0200 837  PHE A CD2 
2215 C CE1 . PHE A 300 ? 0.2356 0.2000 0.2109 0.0070  0.0071  -0.0237 837  PHE A CE1 
2216 C CE2 . PHE A 300 ? 0.2170 0.1859 0.1976 0.0076  0.0101  -0.0215 837  PHE A CE2 
2217 C CZ  . PHE A 300 ? 0.2209 0.1860 0.1962 0.0072  0.0084  -0.0225 837  PHE A CZ  
2218 N N   . GLU A 301 ? 0.2688 0.2391 0.2965 0.0060  0.0053  -0.0091 838  GLU A N   
2219 C CA  . GLU A 301 ? 0.2556 0.2264 0.2971 0.0038  0.0014  -0.0018 838  GLU A CA  
2220 C C   . GLU A 301 ? 0.2654 0.2267 0.3183 0.0054  0.0029  -0.0085 838  GLU A C   
2221 O O   . GLU A 301 ? 0.2160 0.1757 0.2722 0.0030  0.0004  -0.0072 838  GLU A O   
2222 C CB  . GLU A 301 ? 0.2676 0.2426 0.3234 0.0024  -0.0029 0.0092  838  GLU A CB  
2223 C CG  . GLU A 301 ? 0.3069 0.2921 0.3492 -0.0018 -0.0055 0.0155  838  GLU A CG  
2224 C CD  . GLU A 301 ? 0.3186 0.3090 0.3741 -0.0043 -0.0115 0.0270  838  GLU A CD  
2225 O OE1 . GLU A 301 ? 0.3163 0.3042 0.3945 -0.0043 -0.0161 0.0353  838  GLU A OE1 
2226 O OE2 . GLU A 301 ? 0.3136 0.3103 0.3589 -0.0068 -0.0127 0.0282  838  GLU A OE2 
2227 N N   . LYS A 302 ? 0.2171 0.1726 0.2764 0.0085  0.0078  -0.0170 839  LYS A N   
2228 C CA  . LYS A 302 ? 0.2262 0.1726 0.2957 0.0089  0.0110  -0.0271 839  LYS A CA  
2229 C C   . LYS A 302 ? 0.2298 0.1737 0.2819 0.0058  0.0102  -0.0337 839  LYS A C   
2230 O O   . LYS A 302 ? 0.2360 0.1745 0.2966 0.0037  0.0081  -0.0363 839  LYS A O   
2231 C CB  . LYS A 302 ? 0.2317 0.1752 0.3062 0.0116  0.0193  -0.0380 839  LYS A CB  
2232 C CG  . LYS A 302 ? 0.2451 0.1796 0.3317 0.0114  0.0253  -0.0524 839  LYS A CG  
2233 C CD  . LYS A 302 ? 0.2516 0.1865 0.3461 0.0136  0.0359  -0.0635 839  LYS A CD  
2234 C CE  . LYS A 302 ? 0.2686 0.1952 0.3746 0.0126  0.0444  -0.0818 839  LYS A CE  
2235 N NZ  . LYS A 302 ? 0.2788 0.2024 0.3549 0.0059  0.0445  -0.0914 839  LYS A NZ  
2236 N N   . CYS A 303 ? 0.2270 0.1748 0.2573 0.0050  0.0106  -0.0352 840  CYS A N   
2237 C CA  . CYS A 303 ? 0.2721 0.2185 0.2883 0.0016  0.0081  -0.0398 840  CYS A CA  
2238 C C   . CYS A 303 ? 0.2555 0.2050 0.2775 -0.0001 0.0023  -0.0328 840  CYS A C   
2239 O O   . CYS A 303 ? 0.2341 0.1809 0.2550 -0.0034 -0.0008 -0.0365 840  CYS A O   
2240 C CB  . CYS A 303 ? 0.2304 0.1805 0.2278 0.0012  0.0080  -0.0397 840  CYS A CB  
2241 S SG  . CYS A 303 ? 0.2394 0.1875 0.2257 0.0003  0.0153  -0.0477 840  CYS A SG  
2242 N N   . ILE A 304 ? 0.2607 0.2172 0.2885 0.0008  0.0010  -0.0230 841  ILE A N   
2243 C CA  . ILE A 304 ? 0.2628 0.2252 0.2956 -0.0021 -0.0025 -0.0163 841  ILE A CA  
2244 C C   . ILE A 304 ? 0.2659 0.2233 0.3160 -0.0046 -0.0051 -0.0134 841  ILE A C   
2245 O O   . ILE A 304 ? 0.2751 0.2316 0.3295 -0.0078 -0.0080 -0.0140 841  ILE A O   
2246 C CB  . ILE A 304 ? 0.2631 0.2361 0.2930 -0.0026 -0.0016 -0.0082 841  ILE A CB  
2247 C CG1 . ILE A 304 ? 0.2062 0.1827 0.2230 -0.0002 0.0006  -0.0125 841  ILE A CG1 
2248 C CG2 . ILE A 304 ? 0.2108 0.1920 0.2468 -0.0073 -0.0031 -0.0012 841  ILE A CG2 
2249 C CD1 . ILE A 304 ? 0.2032 0.1874 0.2155 -0.0009 0.0027  -0.0086 841  ILE A CD1 
2250 N N   A VAL A 305 ? 0.2584 0.2124 0.3220 -0.0034 -0.0048 -0.0095 842  VAL A N   
2251 N N   B VAL A 305 ? 0.2597 0.2139 0.3236 -0.0035 -0.0049 -0.0092 842  VAL A N   
2252 C CA  A VAL A 305 ? 0.2306 0.1798 0.3164 -0.0059 -0.0087 -0.0034 842  VAL A CA  
2253 C CA  B VAL A 305 ? 0.2307 0.1800 0.3162 -0.0062 -0.0088 -0.0034 842  VAL A CA  
2254 C C   A VAL A 305 ? 0.2696 0.2062 0.3642 -0.0057 -0.0076 -0.0163 842  VAL A C   
2255 C C   B VAL A 305 ? 0.2709 0.2073 0.3655 -0.0057 -0.0076 -0.0165 842  VAL A C   
2256 O O   A VAL A 305 ? 0.2470 0.1791 0.3545 -0.0093 -0.0114 -0.0150 842  VAL A O   
2257 O O   B VAL A 305 ? 0.3040 0.2356 0.4121 -0.0093 -0.0113 -0.0153 842  VAL A O   
2258 C CB  A VAL A 305 ? 0.5761 0.5263 0.6781 -0.0049 -0.0107 0.0071  842  VAL A CB  
2259 C CB  B VAL A 305 ? 0.5820 0.5327 0.6844 -0.0057 -0.0114 0.0083  842  VAL A CB  
2260 C CG1 A VAL A 305 ? 0.2380 0.1850 0.3646 -0.0088 -0.0170 0.0186  842  VAL A CG1 
2261 C CG1 B VAL A 305 ? 0.2259 0.1906 0.3158 -0.0095 -0.0134 0.0209  842  VAL A CG1 
2262 C CG2 A VAL A 305 ? 0.2241 0.1870 0.3108 -0.0066 -0.0113 0.0163  842  VAL A CG2 
2263 C CG2 B VAL A 305 ? 0.2315 0.1767 0.3395 -0.0001 -0.0071 0.0004  842  VAL A CG2 
2264 N N   . GLU A 306 ? 0.2864 0.2176 0.3731 -0.0028 -0.0020 -0.0297 843  GLU A N   
2265 C CA  . GLU A 306 ? 0.3137 0.2339 0.4048 -0.0043 0.0008  -0.0453 843  GLU A CA  
2266 C C   . GLU A 306 ? 0.3217 0.2421 0.3949 -0.0095 -0.0024 -0.0514 843  GLU A C   
2267 O O   . GLU A 306 ? 0.3472 0.2591 0.4200 -0.0131 -0.0011 -0.0650 843  GLU A O   
2268 C CB  . GLU A 306 ? 0.3223 0.2395 0.4087 -0.0013 0.0095  -0.0580 843  GLU A CB  
2269 C CG  . GLU A 306 ? 0.3431 0.2588 0.4563 0.0039  0.0124  -0.0542 843  GLU A CG  
2270 C CD  . GLU A 306 ? 0.3765 0.2878 0.4944 0.0060  0.0232  -0.0712 843  GLU A CD  
2271 O OE1 . GLU A 306 ? 0.3913 0.3033 0.4833 0.0026  0.0285  -0.0836 843  GLU A OE1 
2272 O OE2 . GLU A 306 ? 0.3808 0.2888 0.5294 0.0104  0.0263  -0.0717 843  GLU A OE2 
2273 N N   . ALA A 307 ? 0.3076 0.2378 0.3677 -0.0105 -0.0065 -0.0424 844  ALA A N   
2274 C CA  . ALA A 307 ? 0.3173 0.2495 0.3675 -0.0155 -0.0117 -0.0448 844  ALA A CA  
2275 C C   . ALA A 307 ? 0.3303 0.2634 0.3992 -0.0187 -0.0167 -0.0367 844  ALA A C   
2276 O O   . ALA A 307 ? 0.3301 0.2735 0.4025 -0.0186 -0.0182 -0.0248 844  ALA A O   
2277 C CB  . ALA A 307 ? 0.3109 0.2533 0.3447 -0.0143 -0.0131 -0.0396 844  ALA A CB  
2278 N N   . GLU A 308 ? 0.3374 0.2600 0.4189 -0.0225 -0.0186 -0.0442 845  GLU A N   
2279 C CA  . GLU A 308 ? 0.3380 0.2595 0.4421 -0.0259 -0.0233 -0.0353 845  GLU A CA  
2280 C C   . GLU A 308 ? 0.3349 0.2646 0.4365 -0.0313 -0.0293 -0.0308 845  GLU A C   
2281 O O   . GLU A 308 ? 0.2989 0.2370 0.4126 -0.0334 -0.0314 -0.0176 845  GLU A O   
2282 C CB  . GLU A 308 ? 0.3665 0.2721 0.4903 -0.0276 -0.0230 -0.0457 845  GLU A CB  
2283 C CG  . GLU A 308 ? 0.3750 0.2743 0.5106 -0.0214 -0.0168 -0.0483 845  GLU A CG  
2284 C CD  . GLU A 308 ? 0.3972 0.2802 0.5578 -0.0219 -0.0147 -0.0615 845  GLU A CD  
2285 O OE1 . GLU A 308 ? 0.4172 0.2925 0.5870 -0.0279 -0.0189 -0.0676 845  GLU A OE1 
2286 O OE2 . GLU A 308 ? 0.3994 0.2773 0.5735 -0.0165 -0.0086 -0.0667 845  GLU A OE2 
2287 N N   . ASN A 309 ? 0.3551 0.2842 0.4416 -0.0345 -0.0323 -0.0405 846  ASN A N   
2288 C CA  . ASN A 309 ? 0.3419 0.2808 0.4292 -0.0391 -0.0391 -0.0352 846  ASN A CA  
2289 C C   . ASN A 309 ? 0.2951 0.2496 0.3810 -0.0348 -0.0365 -0.0233 846  ASN A C   
2290 O O   . ASN A 309 ? 0.2914 0.2488 0.3636 -0.0295 -0.0323 -0.0240 846  ASN A O   
2291 C CB  . ASN A 309 ? 0.3631 0.3000 0.4327 -0.0439 -0.0446 -0.0455 846  ASN A CB  
2292 C CG  . ASN A 309 ? 0.3855 0.3330 0.4611 -0.0488 -0.0536 -0.0389 846  ASN A CG  
2293 O OD1 . ASN A 309 ? 0.3850 0.3441 0.4569 -0.0460 -0.0550 -0.0321 846  ASN A OD1 
2294 N ND2 . ASN A 309 ? 0.3866 0.3301 0.4753 -0.0563 -0.0599 -0.0410 846  ASN A ND2 
2295 N N   . PHE A 310 ? 0.2772 0.2423 0.3784 -0.0379 -0.0384 -0.0137 847  PHE A N   
2296 C CA  . PHE A 310 ? 0.2642 0.2451 0.3670 -0.0350 -0.0331 -0.0046 847  PHE A CA  
2297 C C   . PHE A 310 ? 0.2692 0.2574 0.3627 -0.0313 -0.0337 -0.0077 847  PHE A C   
2298 O O   . PHE A 310 ? 0.2619 0.2548 0.3472 -0.0260 -0.0279 -0.0071 847  PHE A O   
2299 C CB  . PHE A 310 ? 0.2522 0.2444 0.3743 -0.0408 -0.0336 0.0051  847  PHE A CB  
2300 C CG  . PHE A 310 ? 0.2517 0.2625 0.3759 -0.0395 -0.0261 0.0116  847  PHE A CG  
2301 C CD1 . PHE A 310 ? 0.2267 0.2407 0.3393 -0.0361 -0.0188 0.0136  847  PHE A CD1 
2302 C CD2 . PHE A 310 ? 0.2536 0.2794 0.3927 -0.0424 -0.0258 0.0144  847  PHE A CD2 
2303 C CE1 . PHE A 310 ? 0.2218 0.2529 0.3344 -0.0364 -0.0106 0.0165  847  PHE A CE1 
2304 C CE2 . PHE A 310 ? 0.2557 0.2995 0.3985 -0.0416 -0.0163 0.0172  847  PHE A CE2 
2305 C CZ  . PHE A 310 ? 0.2556 0.3016 0.3835 -0.0389 -0.0083 0.0173  847  PHE A CZ  
2306 N N   . GLU A 311 ? 0.2788 0.2677 0.3753 -0.0347 -0.0419 -0.0103 848  GLU A N   
2307 C CA  . GLU A 311 ? 0.3077 0.3033 0.4005 -0.0318 -0.0450 -0.0104 848  GLU A CA  
2308 C C   . GLU A 311 ? 0.3396 0.3262 0.4104 -0.0280 -0.0437 -0.0158 848  GLU A C   
2309 O O   . GLU A 311 ? 0.3398 0.3316 0.4081 -0.0229 -0.0414 -0.0140 848  GLU A O   
2310 C CB  . GLU A 311 ? 0.3346 0.3325 0.4353 -0.0380 -0.0569 -0.0100 848  GLU A CB  
2311 C CG  . GLU A 311 ? 0.3593 0.3707 0.4868 -0.0410 -0.0581 -0.0033 848  GLU A CG  
2312 C CD  . GLU A 311 ? 0.3875 0.3947 0.5229 -0.0464 -0.0563 -0.0022 848  GLU A CD  
2313 O OE1 . GLU A 311 ? 0.4077 0.3994 0.5309 -0.0485 -0.0576 -0.0084 848  GLU A OE1 
2314 O OE2 . GLU A 311 ? 0.3890 0.4086 0.5446 -0.0487 -0.0532 0.0047  848  GLU A OE2 
2315 N N   . GLU A 312 ? 0.3842 0.3577 0.4409 -0.0307 -0.0442 -0.0231 849  GLU A N   
2316 C CA  . GLU A 312 ? 0.4163 0.3829 0.4528 -0.0281 -0.0412 -0.0284 849  GLU A CA  
2317 C C   . GLU A 312 ? 0.3509 0.3196 0.3871 -0.0208 -0.0318 -0.0256 849  GLU A C   
2318 O O   . GLU A 312 ? 0.3405 0.3096 0.3660 -0.0172 -0.0298 -0.0257 849  GLU A O   
2319 C CB  . GLU A 312 ? 0.5090 0.4627 0.5342 -0.0329 -0.0409 -0.0394 849  GLU A CB  
2320 C CG  . GLU A 312 ? 0.5857 0.5335 0.5912 -0.0313 -0.0354 -0.0463 849  GLU A CG  
2321 C CD  . GLU A 312 ? 0.6629 0.5999 0.6584 -0.0375 -0.0337 -0.0603 849  GLU A CD  
2322 O OE1 . GLU A 312 ? 0.6927 0.6288 0.6766 -0.0464 -0.0411 -0.0653 849  GLU A OE1 
2323 O OE2 . GLU A 312 ? 0.6838 0.6136 0.6847 -0.0342 -0.0250 -0.0669 849  GLU A OE2 
2324 N N   . ARG A 313 ? 0.2982 0.2686 0.3463 -0.0198 -0.0271 -0.0218 850  ARG A N   
2325 C CA  . ARG A 313 ? 0.2662 0.2394 0.3124 -0.0151 -0.0197 -0.0184 850  ARG A CA  
2326 C C   . ARG A 313 ? 0.2537 0.2388 0.3011 -0.0120 -0.0171 -0.0147 850  ARG A C   
2327 O O   . ARG A 313 ? 0.2508 0.2361 0.2895 -0.0081 -0.0131 -0.0157 850  ARG A O   
2328 C CB  . ARG A 313 ? 0.2436 0.2170 0.3021 -0.0171 -0.0177 -0.0125 850  ARG A CB  
2329 C CG  . ARG A 313 ? 0.2275 0.2048 0.2829 -0.0144 -0.0123 -0.0073 850  ARG A CG  
2330 C CD  . ARG A 313 ? 0.2322 0.2078 0.3000 -0.0176 -0.0130 0.0008  850  ARG A CD  
2331 N NE  . ARG A 313 ? 0.2397 0.2236 0.3192 -0.0235 -0.0146 0.0090  850  ARG A NE  
2332 C CZ  . ARG A 313 ? 0.2497 0.2278 0.3428 -0.0275 -0.0193 0.0095  850  ARG A CZ  
2333 N NH1 . ARG A 313 ? 0.2395 0.2030 0.3350 -0.0263 -0.0223 0.0001  850  ARG A NH1 
2334 N NH2 . ARG A 313 ? 0.2444 0.2317 0.3488 -0.0337 -0.0203 0.0184  850  ARG A NH2 
2335 N N   . VAL A 314 ? 0.2569 0.2521 0.3176 -0.0139 -0.0186 -0.0116 851  VAL A N   
2336 C CA  . VAL A 314 ? 0.2099 0.2165 0.2772 -0.0106 -0.0148 -0.0110 851  VAL A CA  
2337 C C   . VAL A 314 ? 0.2317 0.2337 0.2925 -0.0068 -0.0188 -0.0139 851  VAL A C   
2338 O O   . VAL A 314 ? 0.2065 0.2117 0.2674 -0.0026 -0.0143 -0.0153 851  VAL A O   
2339 C CB  . VAL A 314 ? 0.2093 0.2284 0.2972 -0.0134 -0.0154 -0.0080 851  VAL A CB  
2340 C CG1 . VAL A 314 ? 0.2048 0.2354 0.3057 -0.0093 -0.0109 -0.0101 851  VAL A CG1 
2341 C CG2 . VAL A 314 ? 0.2098 0.2355 0.3029 -0.0184 -0.0102 -0.0032 851  VAL A CG2 
2342 N N   . ALA A 315 ? 0.2393 0.2336 0.2937 -0.0096 -0.0276 -0.0145 852  ALA A N   
2343 C CA  . ALA A 315 ? 0.2673 0.2577 0.3135 -0.0083 -0.0329 -0.0143 852  ALA A CA  
2344 C C   . ALA A 315 ? 0.2667 0.2497 0.2953 -0.0057 -0.0275 -0.0173 852  ALA A C   
2345 O O   . ALA A 315 ? 0.2675 0.2501 0.2941 -0.0030 -0.0282 -0.0158 852  ALA A O   
2346 C CB  . ALA A 315 ? 0.2918 0.2776 0.3306 -0.0150 -0.0441 -0.0139 852  ALA A CB  
2347 N N   . VAL A 316 ? 0.2608 0.2380 0.2804 -0.0066 -0.0227 -0.0207 853  VAL A N   
2348 C CA  . VAL A 316 ? 0.2464 0.2184 0.2539 -0.0041 -0.0171 -0.0231 853  VAL A CA  
2349 C C   . VAL A 316 ? 0.2413 0.2194 0.2540 0.0003  -0.0115 -0.0211 853  VAL A C   
2350 O O   . VAL A 316 ? 0.2225 0.1991 0.2296 0.0027  -0.0103 -0.0214 853  VAL A O   
2351 C CB  . VAL A 316 ? 0.2529 0.2184 0.2580 -0.0054 -0.0134 -0.0268 853  VAL A CB  
2352 C CG1 . VAL A 316 ? 0.2445 0.2082 0.2451 -0.0020 -0.0072 -0.0273 853  VAL A CG1 
2353 C CG2 . VAL A 316 ? 0.2635 0.2215 0.2595 -0.0105 -0.0167 -0.0333 853  VAL A CG2 
2354 N N   . LEU A 317 ? 0.2613 0.2470 0.2841 0.0001  -0.0079 -0.0192 854  LEU A N   
2355 C CA  . LEU A 317 ? 0.2506 0.2436 0.2753 0.0020  -0.0017 -0.0193 854  LEU A CA  
2356 C C   . LEU A 317 ? 0.2682 0.2644 0.3004 0.0052  -0.0021 -0.0217 854  LEU A C   
2357 O O   . LEU A 317 ? 0.2710 0.2671 0.3004 0.0074  0.0015  -0.0244 854  LEU A O   
2358 C CB  . LEU A 317 ? 0.2193 0.2223 0.2516 -0.0015 0.0023  -0.0165 854  LEU A CB  
2359 C CG  . LEU A 317 ? 0.2183 0.2310 0.2480 -0.0027 0.0096  -0.0177 854  LEU A CG  
2360 C CD1 . LEU A 317 ? 0.2192 0.2266 0.2360 -0.0020 0.0102  -0.0176 854  LEU A CD1 
2361 C CD2 . LEU A 317 ? 0.2290 0.2522 0.2620 -0.0090 0.0129  -0.0125 854  LEU A CD2 
2362 N N   . SER A 318 ? 0.2686 0.2674 0.3133 0.0051  -0.0072 -0.0204 855  SER A N   
2363 C CA  . SER A 318 ? 0.2764 0.2779 0.3357 0.0087  -0.0090 -0.0213 855  SER A CA  
2364 C C   . SER A 318 ? 0.2694 0.2612 0.3193 0.0099  -0.0146 -0.0193 855  SER A C   
2365 O O   . SER A 318 ? 0.2678 0.2590 0.3266 0.0132  -0.0137 -0.0205 855  SER A O   
2366 C CB  . SER A 318 ? 0.2934 0.3010 0.3723 0.0078  -0.0152 -0.0181 855  SER A CB  
2367 O OG  . SER A 318 ? 0.3271 0.3424 0.4108 0.0047  -0.0114 -0.0182 855  SER A OG  
2368 N N   . ARG A 319 ? 0.2590 0.2432 0.2917 0.0063  -0.0197 -0.0167 856  ARG A N   
2369 C CA  . ARG A 319 ? 0.2637 0.2404 0.2840 0.0055  -0.0233 -0.0143 856  ARG A CA  
2370 C C   . ARG A 319 ? 0.2136 0.1882 0.2280 0.0083  -0.0157 -0.0176 856  ARG A C   
2371 O O   . ARG A 319 ? 0.2158 0.1873 0.2325 0.0097  -0.0173 -0.0158 856  ARG A O   
2372 C CB  . ARG A 319 ? 0.2662 0.2374 0.2672 -0.0003 -0.0268 -0.0141 856  ARG A CB  
2373 C CG  . ARG A 319 ? 0.2712 0.2375 0.2579 -0.0041 -0.0316 -0.0102 856  ARG A CG  
2374 C CD  . ARG A 319 ? 0.2923 0.2604 0.2887 -0.0066 -0.0438 -0.0012 856  ARG A CD  
2375 N NE  . ARG A 319 ? 0.2924 0.2642 0.2940 -0.0105 -0.0512 0.0003  856  ARG A NE  
2376 C CZ  . ARG A 319 ? 0.3161 0.2865 0.3005 -0.0195 -0.0588 0.0019  856  ARG A CZ  
2377 N NH1 . ARG A 319 ? 0.3346 0.3009 0.2945 -0.0258 -0.0583 0.0017  856  ARG A NH1 
2378 N NH2 . ARG A 319 ? 0.2962 0.2703 0.2875 -0.0234 -0.0663 0.0030  856  ARG A NH2 
2379 N N   . ILE A 320 ? 0.2487 0.2250 0.2575 0.0084  -0.0088 -0.0211 857  ILE A N   
2380 C CA  . ILE A 320 ? 0.2505 0.2261 0.2537 0.0097  -0.0031 -0.0233 857  ILE A CA  
2381 C C   . ILE A 320 ? 0.2491 0.2288 0.2634 0.0122  -0.0001 -0.0267 857  ILE A C   
2382 O O   . ILE A 320 ? 0.2047 0.1813 0.2169 0.0130  0.0012  -0.0282 857  ILE A O   
2383 C CB  . ILE A 320 ? 0.2023 0.1802 0.2008 0.0082  0.0012  -0.0237 857  ILE A CB  
2384 C CG1 . ILE A 320 ? 0.2061 0.1777 0.1971 0.0066  -0.0002 -0.0232 857  ILE A CG1 
2385 C CG2 . ILE A 320 ? 0.2002 0.1805 0.1954 0.0083  0.0054  -0.0247 857  ILE A CG2 
2386 C CD1 . ILE A 320 ? 0.2579 0.2304 0.2520 0.0055  0.0022  -0.0222 857  ILE A CD1 
2387 N N   . ILE A 321 ? 0.2025 0.1895 0.2307 0.0130  0.0017  -0.0291 858  ILE A N   
2388 C CA  . ILE A 321 ? 0.2390 0.2305 0.2815 0.0154  0.0066  -0.0357 858  ILE A CA  
2389 C C   . ILE A 321 ? 0.2074 0.1921 0.2635 0.0186  0.0004  -0.0337 858  ILE A C   
2390 O O   . ILE A 321 ? 0.2933 0.2758 0.3581 0.0206  0.0032  -0.0390 858  ILE A O   
2391 C CB  . ILE A 321 ? 0.2895 0.2926 0.3462 0.0149  0.0120  -0.0396 858  ILE A CB  
2392 C CG1 . ILE A 321 ? 0.2380 0.2478 0.2808 0.0099  0.0166  -0.0384 858  ILE A CG1 
2393 C CG2 . ILE A 321 ? 0.2070 0.2155 0.2804 0.0171  0.0197  -0.0501 858  ILE A CG2 
2394 C CD1 . ILE A 321 ? 0.2221 0.2454 0.2768 0.0075  0.0229  -0.0411 858  ILE A CD1 
2395 N N   . GLU A 322 ? 0.2097 0.1910 0.2684 0.0182  -0.0090 -0.0256 859  GLU A N   
2396 C CA  . GLU A 322 ? 0.2160 0.1908 0.2860 0.0193  -0.0177 -0.0194 859  GLU A CA  
2397 C C   . GLU A 322 ? 0.2783 0.2449 0.3327 0.0176  -0.0181 -0.0173 859  GLU A C   
2398 O O   . GLU A 322 ? 0.2763 0.2377 0.3433 0.0191  -0.0210 -0.0156 859  GLU A O   
2399 C CB  . GLU A 322 ? 0.2288 0.2032 0.2990 0.0161  -0.0292 -0.0094 859  GLU A CB  
2400 C CG  . GLU A 322 ? 0.2193 0.2024 0.3117 0.0176  -0.0310 -0.0096 859  GLU A CG  
2401 C CD  . GLU A 322 ? 0.3241 0.3070 0.4161 0.0128  -0.0448 0.0011  859  GLU A CD  
2402 O OE1 . GLU A 322 ? 0.4215 0.3988 0.4880 0.0069  -0.0500 0.0059  859  GLU A OE1 
2403 O OE2 . GLU A 322 ? 0.4097 0.3992 0.5271 0.0141  -0.0503 0.0042  859  GLU A OE2 
2404 N N   . ILE A 323 ? 0.2173 0.1827 0.2479 0.0144  -0.0151 -0.0172 860  ILE A N   
2405 C CA  . ILE A 323 ? 0.2760 0.2359 0.2942 0.0127  -0.0138 -0.0159 860  ILE A CA  
2406 C C   . ILE A 323 ? 0.2903 0.2508 0.3155 0.0150  -0.0074 -0.0235 860  ILE A C   
2407 O O   . ILE A 323 ? 0.3009 0.2560 0.3287 0.0146  -0.0086 -0.0226 860  ILE A O   
2408 C CB  . ILE A 323 ? 0.2469 0.2070 0.2443 0.0094  -0.0107 -0.0157 860  ILE A CB  
2409 C CG1 . ILE A 323 ? 0.2457 0.2048 0.2339 0.0053  -0.0166 -0.0108 860  ILE A CG1 
2410 C CG2 . ILE A 323 ? 0.2505 0.2074 0.2390 0.0078  -0.0079 -0.0150 860  ILE A CG2 
2411 C CD1 . ILE A 323 ? 0.2567 0.2162 0.2306 0.0029  -0.0118 -0.0147 860  ILE A CD1 
2412 N N   . LEU A 324 ? 0.2603 0.2278 0.2877 0.0160  -0.0007 -0.0312 861  LEU A N   
2413 C CA  . LEU A 324 ? 0.2589 0.2286 0.2894 0.0160  0.0057  -0.0402 861  LEU A CA  
2414 C C   . LEU A 324 ? 0.2812 0.2468 0.3342 0.0190  0.0050  -0.0450 861  LEU A C   
2415 O O   . LEU A 324 ? 0.2830 0.2446 0.3386 0.0183  0.0069  -0.0505 861  LEU A O   
2416 C CB  . LEU A 324 ? 0.2367 0.2169 0.2634 0.0141  0.0127  -0.0462 861  LEU A CB  
2417 C CG  . LEU A 324 ? 0.2499 0.2358 0.2753 0.0112  0.0203  -0.0571 861  LEU A CG  
2418 C CD1 . LEU A 324 ? 0.2504 0.2462 0.2597 0.0057  0.0239  -0.0560 861  LEU A CD1 
2419 C CD2 . LEU A 324 ? 0.2529 0.2424 0.2997 0.0137  0.0259  -0.0681 861  LEU A CD2 
2420 N N   . GLN A 325 ? 0.2999 0.2664 0.3729 0.0223  0.0016  -0.0431 862  GLN A N   
2421 C CA  . GLN A 325 ? 0.3448 0.3077 0.4474 0.0262  0.0011  -0.0482 862  GLN A CA  
2422 C C   . GLN A 325 ? 0.3552 0.3062 0.4629 0.0258  -0.0078 -0.0394 862  GLN A C   
2423 O O   . GLN A 325 ? 0.3434 0.2885 0.4696 0.0275  -0.0066 -0.0458 862  GLN A O   
2424 C CB  . GLN A 325 ? 0.3848 0.3529 0.5126 0.0299  -0.0017 -0.0463 862  GLN A CB  
2425 C CG  . GLN A 325 ? 0.4326 0.3972 0.6006 0.0352  -0.0028 -0.0511 862  GLN A CG  
2426 C CD  . GLN A 325 ? 0.4620 0.4320 0.6435 0.0368  0.0121  -0.0719 862  GLN A CD  
2427 O OE1 . GLN A 325 ? 0.4716 0.4540 0.6486 0.0356  0.0224  -0.0812 862  GLN A OE1 
2428 N NE2 . GLN A 325 ? 0.4652 0.4263 0.6633 0.0384  0.0133  -0.0795 862  GLN A NE2 
2429 N N   . VAL A 326 ? 0.2326 0.1803 0.3238 0.0225  -0.0162 -0.0254 863  VAL A N   
2430 C CA  . VAL A 326 ? 0.3070 0.2453 0.3996 0.0199  -0.0241 -0.0154 863  VAL A CA  
2431 C C   . VAL A 326 ? 0.2973 0.2327 0.3755 0.0174  -0.0182 -0.0208 863  VAL A C   
2432 O O   . VAL A 326 ? 0.3051 0.2326 0.3948 0.0165  -0.0212 -0.0191 863  VAL A O   
2433 C CB  . VAL A 326 ? 0.2447 0.1826 0.3209 0.0148  -0.0335 0.0002  863  VAL A CB  
2434 C CG1 . VAL A 326 ? 0.2563 0.1861 0.3357 0.0104  -0.0422 0.0129  863  VAL A CG1 
2435 C CG2 . VAL A 326 ? 0.2459 0.1881 0.3349 0.0160  -0.0405 0.0055  863  VAL A CG2 
2436 N N   . PHE A 327 ? 0.2326 0.1745 0.2884 0.0157  -0.0110 -0.0262 864  PHE A N   
2437 C CA  . PHE A 327 ? 0.2324 0.1738 0.2784 0.0132  -0.0060 -0.0321 864  PHE A CA  
2438 C C   . PHE A 327 ? 0.3225 0.2607 0.3869 0.0145  -0.0028 -0.0442 864  PHE A C   
2439 O O   . PHE A 327 ? 0.2446 0.1764 0.3127 0.0121  -0.0041 -0.0451 864  PHE A O   
2440 C CB  . PHE A 327 ? 0.2416 0.1919 0.2685 0.0116  0.0001  -0.0362 864  PHE A CB  
2441 C CG  . PHE A 327 ? 0.2414 0.1931 0.2513 0.0094  -0.0011 -0.0275 864  PHE A CG  
2442 C CD1 . PHE A 327 ? 0.2830 0.2299 0.2894 0.0069  -0.0050 -0.0189 864  PHE A CD1 
2443 C CD2 . PHE A 327 ? 0.2277 0.1861 0.2269 0.0090  0.0023  -0.0285 864  PHE A CD2 
2444 C CE1 . PHE A 327 ? 0.2247 0.1742 0.2166 0.0043  -0.0034 -0.0142 864  PHE A CE1 
2445 C CE2 . PHE A 327 ? 0.2245 0.1837 0.2131 0.0075  0.0026  -0.0233 864  PHE A CE2 
2446 C CZ  . PHE A 327 ? 0.2357 0.1908 0.2204 0.0053  0.0007  -0.0175 864  PHE A CZ  
2447 N N   . GLN A 328 ? 0.3170 0.2599 0.3943 0.0176  0.0024  -0.0547 865  GLN A N   
2448 C CA  . GLN A 328 ? 0.3467 0.2874 0.4424 0.0184  0.0081  -0.0704 865  GLN A CA  
2449 C C   . GLN A 328 ? 0.3335 0.2622 0.4604 0.0218  0.0015  -0.0674 865  GLN A C   
2450 O O   . GLN A 328 ? 0.3475 0.2694 0.4884 0.0210  0.0036  -0.0775 865  GLN A O   
2451 C CB  . GLN A 328 ? 0.3963 0.3476 0.4990 0.0201  0.0176  -0.0835 865  GLN A CB  
2452 C CG  . GLN A 328 ? 0.4366 0.4003 0.5112 0.0156  0.0232  -0.0845 865  GLN A CG  
2453 C CD  . GLN A 328 ? 0.4885 0.4609 0.5554 0.0101  0.0341  -0.1021 865  GLN A CD  
2454 O OE1 . GLN A 328 ? 0.5197 0.5033 0.5880 0.0091  0.0424  -0.1100 865  GLN A OE1 
2455 N NE2 . GLN A 328 ? 0.5019 0.4704 0.5598 0.0051  0.0341  -0.1079 865  GLN A NE2 
2456 N N   . ASP A 329 ? 0.3183 0.2442 0.4579 0.0247  -0.0075 -0.0530 866  ASP A N   
2457 C CA  . ASP A 329 ? 0.3313 0.2457 0.5023 0.0268  -0.0168 -0.0454 866  ASP A CA  
2458 C C   . ASP A 329 ? 0.3244 0.2297 0.4859 0.0216  -0.0227 -0.0361 866  ASP A C   
2459 O O   . ASP A 329 ? 0.3365 0.2308 0.5247 0.0220  -0.0276 -0.0351 866  ASP A O   
2460 C CB  . ASP A 329 ? 0.3405 0.2557 0.5236 0.0287  -0.0278 -0.0286 866  ASP A CB  
2461 C CG  . ASP A 329 ? 0.3437 0.2678 0.5458 0.0342  -0.0231 -0.0369 866  ASP A CG  
2462 O OD1 . ASP A 329 ? 0.3504 0.2772 0.5699 0.0377  -0.0120 -0.0560 866  ASP A OD1 
2463 O OD2 . ASP A 329 ? 0.3452 0.2744 0.5447 0.0340  -0.0302 -0.0249 866  ASP A OD2 
2464 N N   . LEU A 330 ? 0.3044 0.2142 0.4319 0.0165  -0.0220 -0.0292 867  LEU A N   
2465 C CA  . LEU A 330 ? 0.2788 0.1831 0.3962 0.0107  -0.0258 -0.0206 867  LEU A CA  
2466 C C   . LEU A 330 ? 0.2759 0.1807 0.3850 0.0082  -0.0184 -0.0344 867  LEU A C   
2467 O O   . LEU A 330 ? 0.2898 0.1922 0.3898 0.0030  -0.0205 -0.0280 867  LEU A O   
2468 C CB  . LEU A 330 ? 0.2738 0.1841 0.3623 0.0062  -0.0280 -0.0066 867  LEU A CB  
2469 C CG  . LEU A 330 ? 0.2990 0.2100 0.3876 0.0052  -0.0367 0.0084  867  LEU A CG  
2470 C CD1 . LEU A 330 ? 0.3046 0.2238 0.3610 0.0008  -0.0341 0.0139  867  LEU A CD1 
2471 C CD2 . LEU A 330 ? 0.2816 0.1835 0.3877 0.0012  -0.0482 0.0242  867  LEU A CD2 
2472 N N   . ASN A 331 ? 0.2675 0.1769 0.3785 0.0103  -0.0099 -0.0525 868  ASN A N   
2473 C CA  . ASN A 331 ? 0.3082 0.2208 0.4057 0.0056  -0.0039 -0.0651 868  ASN A CA  
2474 C C   . ASN A 331 ? 0.3010 0.2213 0.3700 0.0011  -0.0042 -0.0561 868  ASN A C   
2475 O O   . ASN A 331 ? 0.3225 0.2420 0.3857 -0.0041 -0.0052 -0.0564 868  ASN A O   
2476 C CB  . ASN A 331 ? 0.3424 0.2434 0.4589 0.0028  -0.0064 -0.0710 868  ASN A CB  
2477 C CG  . ASN A 331 ? 0.3589 0.2530 0.5063 0.0068  -0.0029 -0.0870 868  ASN A CG  
2478 O OD1 . ASN A 331 ? 0.3719 0.2732 0.5220 0.0102  0.0047  -0.0989 868  ASN A OD1 
2479 N ND2 . ASN A 331 ? 0.3625 0.2427 0.5364 0.0062  -0.0079 -0.0879 868  ASN A ND2 
2480 N N   . ASN A 332 ? 0.2858 0.2137 0.3403 0.0030  -0.0035 -0.0483 869  ASN A N   
2481 C CA  . ASN A 332 ? 0.2838 0.2195 0.3168 -0.0001 -0.0025 -0.0419 869  ASN A CA  
2482 C C   . ASN A 332 ? 0.2776 0.2234 0.2987 -0.0008 0.0029  -0.0505 869  ASN A C   
2483 O O   . ASN A 332 ? 0.2331 0.1843 0.2480 0.0017  0.0046  -0.0481 869  ASN A O   
2484 C CB  . ASN A 332 ? 0.2829 0.2196 0.3082 0.0010  -0.0049 -0.0287 869  ASN A CB  
2485 C CG  . ASN A 332 ? 0.2317 0.1760 0.2412 -0.0014 -0.0022 -0.0243 869  ASN A CG  
2486 O OD1 . ASN A 332 ? 0.2304 0.1795 0.2362 -0.0039 -0.0005 -0.0283 869  ASN A OD1 
2487 N ND2 . ASN A 332 ? 0.2298 0.1756 0.2316 -0.0013 -0.0022 -0.0164 869  ASN A ND2 
2488 N N   . PHE A 333 ? 0.2748 0.2235 0.2917 -0.0058 0.0046  -0.0595 870  PHE A N   
2489 C CA  . PHE A 333 ? 0.3011 0.2608 0.3045 -0.0093 0.0086  -0.0660 870  PHE A CA  
2490 C C   . PHE A 333 ? 0.2965 0.2642 0.2866 -0.0113 0.0062  -0.0550 870  PHE A C   
2491 O O   . PHE A 333 ? 0.3125 0.2889 0.2932 -0.0130 0.0080  -0.0546 870  PHE A O   
2492 C CB  . PHE A 333 ? 0.3339 0.2951 0.3351 -0.0163 0.0106  -0.0800 870  PHE A CB  
2493 C CG  . PHE A 333 ? 0.3459 0.2996 0.3646 -0.0139 0.0150  -0.0946 870  PHE A CG  
2494 C CD1 . PHE A 333 ? 0.3434 0.3020 0.3669 -0.0110 0.0222  -0.1039 870  PHE A CD1 
2495 C CD2 . PHE A 333 ? 0.3592 0.3012 0.3940 -0.0142 0.0122  -0.0988 870  PHE A CD2 
2496 C CE1 . PHE A 333 ? 0.3668 0.3192 0.4128 -0.0079 0.0272  -0.1183 870  PHE A CE1 
2497 C CE2 . PHE A 333 ? 0.3784 0.3124 0.4359 -0.0112 0.0161  -0.1127 870  PHE A CE2 
2498 C CZ  . PHE A 333 ? 0.3809 0.3203 0.4452 -0.0076 0.0240  -0.1230 870  PHE A CZ  
2499 N N   . ASN A 334 ? 0.2869 0.2522 0.2789 -0.0115 0.0026  -0.0457 871  ASN A N   
2500 C CA  . ASN A 334 ? 0.2767 0.2487 0.2636 -0.0114 0.0015  -0.0359 871  ASN A CA  
2501 C C   . ASN A 334 ? 0.2759 0.2479 0.2613 -0.0061 0.0040  -0.0325 871  ASN A C   
2502 O O   . ASN A 334 ? 0.2675 0.2461 0.2485 -0.0064 0.0043  -0.0299 871  ASN A O   
2503 C CB  . ASN A 334 ? 0.2897 0.2597 0.2827 -0.0121 -0.0003 -0.0284 871  ASN A CB  
2504 C CG  . ASN A 334 ? 0.2956 0.2735 0.2897 -0.0122 -0.0005 -0.0205 871  ASN A CG  
2505 O OD1 . ASN A 334 ? 0.3090 0.2944 0.3035 -0.0166 -0.0041 -0.0185 871  ASN A OD1 
2506 N ND2 . ASN A 334 ? 0.2935 0.2703 0.2897 -0.0080 0.0030  -0.0163 871  ASN A ND2 
2507 N N   . GLY A 335 ? 0.2738 0.2386 0.2639 -0.0021 0.0044  -0.0317 872  GLY A N   
2508 C CA  . GLY A 335 ? 0.2388 0.2035 0.2270 0.0016  0.0055  -0.0293 872  GLY A CA  
2509 C C   . GLY A 335 ? 0.2347 0.2041 0.2221 0.0023  0.0075  -0.0349 872  GLY A C   
2510 O O   . GLY A 335 ? 0.2099 0.1831 0.1941 0.0033  0.0083  -0.0321 872  GLY A O   
2511 N N   . VAL A 336 ? 0.2201 0.1897 0.2119 0.0012  0.0092  -0.0437 873  VAL A N   
2512 C CA  . VAL A 336 ? 0.2222 0.1987 0.2134 0.0005  0.0135  -0.0506 873  VAL A CA  
2513 C C   . VAL A 336 ? 0.3361 0.3225 0.3146 -0.0047 0.0139  -0.0473 873  VAL A C   
2514 O O   . VAL A 336 ? 0.2193 0.2111 0.1957 -0.0046 0.0152  -0.0444 873  VAL A O   
2515 C CB  . VAL A 336 ? 0.2322 0.2081 0.2311 -0.0009 0.0174  -0.0638 873  VAL A CB  
2516 C CG1 . VAL A 336 ? 0.2369 0.2234 0.2330 -0.0036 0.0244  -0.0724 873  VAL A CG1 
2517 C CG2 . VAL A 336 ? 0.3515 0.3171 0.3697 0.0047  0.0155  -0.0650 873  VAL A CG2 
2518 N N   . LEU A 337 ? 0.3028 0.2920 0.2745 -0.0101 0.0115  -0.0463 874  LEU A N   
2519 C CA  . LEU A 337 ? 0.2886 0.2883 0.2498 -0.0170 0.0096  -0.0413 874  LEU A CA  
2520 C C   . LEU A 337 ? 0.2666 0.2666 0.2314 -0.0145 0.0056  -0.0285 874  LEU A C   
2521 O O   . LEU A 337 ? 0.2573 0.2652 0.2182 -0.0191 0.0031  -0.0216 874  LEU A O   
2522 C CB  . LEU A 337 ? 0.3077 0.3111 0.2617 -0.0249 0.0065  -0.0438 874  LEU A CB  
2523 C CG  . LEU A 337 ? 0.3352 0.3435 0.2801 -0.0322 0.0112  -0.0584 874  LEU A CG  
2524 C CD1 . LEU A 337 ? 0.3229 0.3430 0.2568 -0.0377 0.0157  -0.0599 874  LEU A CD1 
2525 C CD2 . LEU A 337 ? 0.3340 0.3323 0.2913 -0.0265 0.0165  -0.0715 874  LEU A CD2 
2526 N N   . GLU A 338 ? 0.2669 0.2589 0.2398 -0.0084 0.0052  -0.0253 875  GLU A N   
2527 C CA  . GLU A 338 ? 0.2761 0.2676 0.2549 -0.0054 0.0041  -0.0175 875  GLU A CA  
2528 C C   . GLU A 338 ? 0.2542 0.2461 0.2327 -0.0035 0.0059  -0.0177 875  GLU A C   
2529 O O   . GLU A 338 ? 0.2364 0.2308 0.2190 -0.0041 0.0042  -0.0114 875  GLU A O   
2530 C CB  . GLU A 338 ? 0.3011 0.2853 0.2855 -0.0009 0.0056  -0.0170 875  GLU A CB  
2531 C CG  . GLU A 338 ? 0.3393 0.3247 0.3284 -0.0028 0.0042  -0.0145 875  GLU A CG  
2532 C CD  . GLU A 338 ? 0.3851 0.3646 0.3766 -0.0003 0.0073  -0.0151 875  GLU A CD  
2533 O OE1 . GLU A 338 ? 0.4017 0.3754 0.3883 0.0013  0.0084  -0.0179 875  GLU A OE1 
2534 O OE2 . GLU A 338 ? 0.3921 0.3740 0.3914 -0.0008 0.0085  -0.0119 875  GLU A OE2 
2535 N N   . ILE A 339 ? 0.2577 0.2471 0.2348 -0.0014 0.0088  -0.0244 876  ILE A N   
2536 C CA  . ILE A 339 ? 0.2624 0.2535 0.2415 -0.0002 0.0102  -0.0245 876  ILE A CA  
2537 C C   . ILE A 339 ? 0.2400 0.2416 0.2144 -0.0062 0.0115  -0.0238 876  ILE A C   
2538 O O   . ILE A 339 ? 0.2223 0.2275 0.1986 -0.0077 0.0107  -0.0181 876  ILE A O   
2539 C CB  . ILE A 339 ? 0.2839 0.2704 0.2678 0.0037  0.0116  -0.0304 876  ILE A CB  
2540 C CG1 . ILE A 339 ? 0.2024 0.1801 0.1874 0.0070  0.0089  -0.0276 876  ILE A CG1 
2541 C CG2 . ILE A 339 ? 0.2037 0.1951 0.1922 0.0039  0.0134  -0.0315 876  ILE A CG2 
2542 C CD1 . ILE A 339 ? 0.3258 0.2990 0.3169 0.0096  0.0071  -0.0295 876  ILE A CD1 
2543 N N   . VAL A 340 ? 0.2493 0.2566 0.2169 -0.0109 0.0138  -0.0297 877  VAL A N   
2544 C CA  . VAL A 340 ? 0.2650 0.2846 0.2230 -0.0198 0.0155  -0.0289 877  VAL A CA  
2545 C C   . VAL A 340 ? 0.2906 0.3141 0.2466 -0.0245 0.0085  -0.0149 877  VAL A C   
2546 O O   . VAL A 340 ? 0.2930 0.3246 0.2462 -0.0303 0.0076  -0.0076 877  VAL A O   
2547 C CB  . VAL A 340 ? 0.2539 0.2784 0.2026 -0.0257 0.0191  -0.0398 877  VAL A CB  
2548 C CG1 . VAL A 340 ? 0.2532 0.2925 0.1861 -0.0381 0.0202  -0.0380 877  VAL A CG1 
2549 C CG2 . VAL A 340 ? 0.2391 0.2601 0.1969 -0.0206 0.0265  -0.0540 877  VAL A CG2 
2550 N N   . SER A 341 ? 0.3024 0.3206 0.2630 -0.0223 0.0033  -0.0100 878  SER A N   
2551 C CA  . SER A 341 ? 0.3232 0.3444 0.2897 -0.0255 -0.0041 0.0038  878  SER A CA  
2552 C C   . SER A 341 ? 0.3037 0.3210 0.2827 -0.0213 -0.0049 0.0104  878  SER A C   
2553 O O   . SER A 341 ? 0.3013 0.3241 0.2843 -0.0266 -0.0100 0.0220  878  SER A O   
2554 C CB  . SER A 341 ? 0.3605 0.3770 0.3354 -0.0224 -0.0077 0.0057  878  SER A CB  
2555 O OG  . SER A 341 ? 0.3963 0.4176 0.3813 -0.0261 -0.0158 0.0193  878  SER A OG  
2556 N N   . ALA A 342 ? 0.2840 0.2917 0.2689 -0.0131 -0.0007 0.0035  879  ALA A N   
2557 C CA  . ALA A 342 ? 0.2616 0.2643 0.2580 -0.0098 -0.0013 0.0071  879  ALA A CA  
2558 C C   . ALA A 342 ? 0.2461 0.2555 0.2400 -0.0147 -0.0010 0.0106  879  ALA A C   
2559 O O   . ALA A 342 ? 0.2304 0.2405 0.2341 -0.0174 -0.0051 0.0203  879  ALA A O   
2560 C CB  . ALA A 342 ? 0.2521 0.2449 0.2505 -0.0026 0.0027  -0.0018 879  ALA A CB  
2561 N N   . VAL A 343 ? 0.2140 0.2285 0.1980 -0.0163 0.0042  0.0029  880  VAL A N   
2562 C CA  . VAL A 343 ? 0.2480 0.2709 0.2311 -0.0214 0.0063  0.0055  880  VAL A CA  
2563 C C   . VAL A 343 ? 0.2624 0.2978 0.2370 -0.0326 0.0036  0.0156  880  VAL A C   
2564 O O   . VAL A 343 ? 0.2661 0.3093 0.2412 -0.0389 0.0039  0.0224  880  VAL A O   
2565 C CB  . VAL A 343 ? 0.2506 0.2772 0.2307 -0.0197 0.0139  -0.0066 880  VAL A CB  
2566 C CG1 . VAL A 343 ? 0.2369 0.2524 0.2262 -0.0107 0.0136  -0.0124 880  VAL A CG1 
2567 C CG2 . VAL A 343 ? 0.2625 0.2938 0.2318 -0.0223 0.0178  -0.0151 880  VAL A CG2 
2568 N N   . ASN A 344 ? 0.2729 0.3116 0.2390 -0.0369 0.0002  0.0181  881  ASN A N   
2569 C CA  . ASN A 344 ? 0.2792 0.3306 0.2358 -0.0497 -0.0051 0.0306  881  ASN A CA  
2570 C C   . ASN A 344 ? 0.2810 0.3291 0.2543 -0.0506 -0.0159 0.0488  881  ASN A C   
2571 O O   . ASN A 344 ? 0.2974 0.3560 0.2665 -0.0621 -0.0226 0.0638  881  ASN A O   
2572 C CB  . ASN A 344 ? 0.2978 0.3555 0.2382 -0.0561 -0.0060 0.0264  881  ASN A CB  
2573 C CG  . ASN A 344 ? 0.3266 0.3930 0.2495 -0.0610 0.0049  0.0100  881  ASN A CG  
2574 O OD1 . ASN A 344 ? 0.3393 0.4108 0.2620 -0.0617 0.0128  0.0048  881  ASN A OD1 
2575 N ND2 . ASN A 344 ? 0.2761 0.3444 0.1870 -0.0648 0.0056  0.0012  881  ASN A ND2 
2576 N N   . SER A 345 ? 0.2640 0.2984 0.2571 -0.0396 -0.0176 0.0478  882  SER A N   
2577 C CA  . SER A 345 ? 0.2675 0.2975 0.2834 -0.0392 -0.0265 0.0626  882  SER A CA  
2578 C C   . SER A 345 ? 0.2901 0.3230 0.3120 -0.0450 -0.0288 0.0730  882  SER A C   
2579 O O   . SER A 345 ? 0.2910 0.3244 0.3065 -0.0442 -0.0218 0.0650  882  SER A O   
2580 C CB  . SER A 345 ? 0.2346 0.2497 0.2702 -0.0267 -0.0243 0.0547  882  SER A CB  
2581 O OG  . SER A 345 ? 0.2241 0.2309 0.2657 -0.0216 -0.0195 0.0473  882  SER A OG  
2582 N N   A VAL A 346 ? 0.3057 0.3410 0.3433 -0.0511 -0.0398 0.0924  883  VAL A N   
2583 N N   B VAL A 346 ? 0.3064 0.3420 0.3435 -0.0513 -0.0397 0.0925  883  VAL A N   
2584 C CA  A VAL A 346 ? 0.3030 0.3432 0.3462 -0.0598 -0.0441 0.1068  883  VAL A CA  
2585 C CA  B VAL A 346 ? 0.2975 0.3379 0.3398 -0.0598 -0.0436 0.1062  883  VAL A CA  
2586 C C   A VAL A 346 ? 0.3085 0.3365 0.3676 -0.0516 -0.0391 0.0986  883  VAL A C   
2587 C C   B VAL A 346 ? 0.3082 0.3362 0.3663 -0.0514 -0.0385 0.0976  883  VAL A C   
2588 O O   A VAL A 346 ? 0.3074 0.3406 0.3614 -0.0572 -0.0363 0.1006  883  VAL A O   
2589 O O   B VAL A 346 ? 0.3092 0.3422 0.3614 -0.0564 -0.0350 0.0982  883  VAL A O   
2590 C CB  A VAL A 346 ? 0.3242 0.3669 0.3879 -0.0671 -0.0593 0.1314  883  VAL A CB  
2591 C CB  B VAL A 346 ? 0.3306 0.3737 0.3930 -0.0675 -0.0587 0.1311  883  VAL A CB  
2592 C CG1 A VAL A 346 ? 0.3311 0.3900 0.3726 -0.0801 -0.0659 0.1422  883  VAL A CG1 
2593 C CG1 B VAL A 346 ? 0.3207 0.3686 0.3892 -0.0776 -0.0635 0.1475  883  VAL A CG1 
2594 C CG2 A VAL A 346 ? 0.3060 0.3337 0.4042 -0.0549 -0.0634 0.1305  883  VAL A CG2 
2595 C CG2 B VAL A 346 ? 0.3294 0.3866 0.3732 -0.0782 -0.0656 0.1405  883  VAL A CG2 
2596 N N   . SER A 347 ? 0.2876 0.3003 0.3655 -0.0396 -0.0375 0.0885  884  SER A N   
2597 C CA  . SER A 347 ? 0.2995 0.3002 0.3912 -0.0334 -0.0337 0.0795  884  SER A CA  
2598 C C   . SER A 347 ? 0.3175 0.3207 0.3884 -0.0316 -0.0243 0.0643  884  SER A C   
2599 O O   . SER A 347 ? 0.3254 0.3253 0.4024 -0.0320 -0.0230 0.0619  884  SER A O   
2600 C CB  . SER A 347 ? 0.2789 0.2646 0.3922 -0.0227 -0.0326 0.0698  884  SER A CB  
2601 O OG  . SER A 347 ? 0.2912 0.2767 0.3895 -0.0168 -0.0263 0.0566  884  SER A OG  
2602 N N   . VAL A 348 ? 0.3192 0.3281 0.3689 -0.0299 -0.0186 0.0546  885  VAL A N   
2603 C CA  . VAL A 348 ? 0.3271 0.3390 0.3628 -0.0279 -0.0107 0.0416  885  VAL A CA  
2604 C C   . VAL A 348 ? 0.3546 0.3828 0.3768 -0.0375 -0.0074 0.0460  885  VAL A C   
2605 O O   . VAL A 348 ? 0.3628 0.3950 0.3860 -0.0385 -0.0030 0.0420  885  VAL A O   
2606 C CB  . VAL A 348 ? 0.3405 0.3486 0.3651 -0.0208 -0.0060 0.0283  885  VAL A CB  
2607 C CG1 . VAL A 348 ? 0.3380 0.3501 0.3527 -0.0192 0.0005  0.0174  885  VAL A CG1 
2608 C CG2 . VAL A 348 ? 0.3408 0.3347 0.3765 -0.0128 -0.0067 0.0221  885  VAL A CG2 
2609 N N   . TYR A 349 ? 0.3663 0.4055 0.3762 -0.0456 -0.0092 0.0538  886  TYR A N   
2610 C CA  . TYR A 349 ? 0.3638 0.4207 0.3563 -0.0563 -0.0035 0.0544  886  TYR A CA  
2611 C C   . TYR A 349 ? 0.3869 0.4512 0.3863 -0.0641 -0.0034 0.0642  886  TYR A C   
2612 O O   . TYR A 349 ? 0.3941 0.4714 0.3848 -0.0694 0.0056  0.0584  886  TYR A O   
2613 C CB  . TYR A 349 ? 0.3622 0.4294 0.3389 -0.0667 -0.0081 0.0635  886  TYR A CB  
2614 C CG  . TYR A 349 ? 0.3617 0.4481 0.3144 -0.0792 -0.0001 0.0594  886  TYR A CG  
2615 C CD1 . TYR A 349 ? 0.3512 0.4406 0.2898 -0.0770 0.0090  0.0410  886  TYR A CD1 
2616 C CD2 . TYR A 349 ? 0.3773 0.4792 0.3222 -0.0943 -0.0011 0.0735  886  TYR A CD2 
2617 C CE1 . TYR A 349 ? 0.3530 0.4600 0.2708 -0.0888 0.0183  0.0336  886  TYR A CE1 
2618 C CE2 . TYR A 349 ? 0.3814 0.5029 0.3020 -0.1075 0.0083  0.0676  886  TYR A CE2 
2619 C CZ  . TYR A 349 ? 0.3623 0.4861 0.2696 -0.1044 0.0188  0.0460  886  TYR A CZ  
2620 O OH  . TYR A 349 ? 0.3601 0.5034 0.2445 -0.1177 0.0302  0.0364  886  TYR A OH  
2621 N N   . ARG A 350 ? 0.3865 0.4431 0.4045 -0.0650 -0.0126 0.0786  887  ARG A N   
2622 C CA  . ARG A 350 ? 0.4026 0.4660 0.4291 -0.0739 -0.0140 0.0907  887  ARG A CA  
2623 C C   . ARG A 350 ? 0.3922 0.4504 0.4304 -0.0676 -0.0085 0.0798  887  ARG A C   
2624 O O   . ARG A 350 ? 0.3953 0.4606 0.4412 -0.0752 -0.0084 0.0883  887  ARG A O   
2625 C CB  . ARG A 350 ? 0.4174 0.4726 0.4648 -0.0773 -0.0272 0.1108  887  ARG A CB  
2626 C CG  . ARG A 350 ? 0.4093 0.4427 0.4807 -0.0639 -0.0315 0.1041  887  ARG A CG  
2627 C CD  . ARG A 350 ? 0.4218 0.4470 0.5208 -0.0672 -0.0439 0.1232  887  ARG A CD  
2628 N NE  . ARG A 350 ? 0.4387 0.4705 0.5457 -0.0783 -0.0473 0.1383  887  ARG A NE  
2629 C CZ  . ARG A 350 ? 0.4223 0.4464 0.5440 -0.0760 -0.0453 0.1330  887  ARG A CZ  
2630 N NH1 . ARG A 350 ? 0.4262 0.4577 0.5557 -0.0874 -0.0487 0.1485  887  ARG A NH1 
2631 N NH2 . ARG A 350 ? 0.3966 0.4063 0.5244 -0.0637 -0.0406 0.1128  887  ARG A NH2 
2632 N N   . LEU A 351 ? 0.3663 0.4135 0.4063 -0.0552 -0.0050 0.0628  888  LEU A N   
2633 C CA  . LEU A 351 ? 0.3531 0.3942 0.4054 -0.0498 -0.0031 0.0541  888  LEU A CA  
2634 C C   . LEU A 351 ? 0.3278 0.3849 0.3743 -0.0529 0.0066  0.0469  888  LEU A C   
2635 O O   . LEU A 351 ? 0.2946 0.3505 0.3405 -0.0454 0.0113  0.0331  888  LEU A O   
2636 C CB  . LEU A 351 ? 0.3504 0.3753 0.4047 -0.0379 -0.0043 0.0408  888  LEU A CB  
2637 C CG  . LEU A 351 ? 0.3462 0.3551 0.4117 -0.0339 -0.0113 0.0439  888  LEU A CG  
2638 C CD1 . LEU A 351 ? 0.3351 0.3317 0.3978 -0.0243 -0.0098 0.0290  888  LEU A CD1 
2639 C CD2 . LEU A 351 ? 0.3367 0.3392 0.4230 -0.0379 -0.0172 0.0523  888  LEU A CD2 
2640 N N   . ASP A 352 ? 0.3312 0.4043 0.3765 -0.0648 0.0095  0.0575  889  ASP A N   
2641 C CA  . ASP A 352 ? 0.3077 0.4000 0.3485 -0.0693 0.0215  0.0500  889  ASP A CA  
2642 C C   . ASP A 352 ? 0.2998 0.3902 0.3590 -0.0626 0.0237  0.0407  889  ASP A C   
2643 O O   . ASP A 352 ? 0.3009 0.3995 0.3618 -0.0585 0.0324  0.0277  889  ASP A O   
2644 C CB  . ASP A 352 ? 0.3062 0.4173 0.3419 -0.0854 0.0245  0.0645  889  ASP A CB  
2645 C CG  . ASP A 352 ? 0.3130 0.4332 0.3252 -0.0951 0.0245  0.0714  889  ASP A CG  
2646 O OD1 . ASP A 352 ? 0.2975 0.4134 0.2969 -0.0892 0.0262  0.0606  889  ASP A OD1 
2647 O OD2 . ASP A 352 ? 0.3423 0.4744 0.3486 -0.1099 0.0220  0.0889  889  ASP A OD2 
2648 N N   . HIS A 353 ? 0.3201 0.4000 0.3957 -0.0619 0.0152  0.0472  890  HIS A N   
2649 C CA  . HIS A 353 ? 0.3374 0.4164 0.4303 -0.0573 0.0151  0.0398  890  HIS A CA  
2650 C C   . HIS A 353 ? 0.3278 0.3954 0.4188 -0.0454 0.0134  0.0260  890  HIS A C   
2651 O O   . HIS A 353 ? 0.3231 0.3956 0.4257 -0.0416 0.0154  0.0185  890  HIS A O   
2652 C CB  . HIS A 353 ? 0.3529 0.4215 0.4623 -0.0604 0.0053  0.0485  890  HIS A CB  
2653 C CG  . HIS A 353 ? 0.3812 0.4618 0.4976 -0.0733 0.0059  0.0641  890  HIS A CG  
2654 N ND1 . HIS A 353 ? 0.3913 0.4923 0.5162 -0.0806 0.0141  0.0660  890  HIS A ND1 
2655 C CD2 . HIS A 353 ? 0.3971 0.4726 0.5159 -0.0807 -0.0009 0.0799  890  HIS A CD2 
2656 C CE1 . HIS A 353 ? 0.3986 0.5073 0.5272 -0.0931 0.0126  0.0827  890  HIS A CE1 
2657 N NE2 . HIS A 353 ? 0.4028 0.4955 0.5284 -0.0934 0.0025  0.0923  890  HIS A NE2 
2658 N N   . THR A 354 ? 0.3092 0.3627 0.3876 -0.0400 0.0093  0.0237  891  THR A N   
2659 C CA  . THR A 354 ? 0.2939 0.3377 0.3683 -0.0304 0.0078  0.0125  891  THR A CA  
2660 C C   . THR A 354 ? 0.2985 0.3533 0.3681 -0.0277 0.0167  0.0043  891  THR A C   
2661 O O   . THR A 354 ? 0.2875 0.3428 0.3661 -0.0222 0.0171  -0.0033 891  THR A O   
2662 C CB  . THR A 354 ? 0.2720 0.2994 0.3361 -0.0264 0.0025  0.0123  891  THR A CB  
2663 O OG1 . THR A 354 ? 0.2651 0.2813 0.3385 -0.0282 -0.0046 0.0165  891  THR A OG1 
2664 C CG2 . THR A 354 ? 0.2595 0.2787 0.3172 -0.0184 0.0015  0.0023  891  THR A CG2 
2665 N N   . PHE A 355 ? 0.3240 0.3877 0.3808 -0.0324 0.0232  0.0057  892  PHE A N   
2666 C CA  . PHE A 355 ? 0.3441 0.4178 0.3968 -0.0310 0.0330  -0.0050 892  PHE A CA  
2667 C C   . PHE A 355 ? 0.3535 0.4435 0.4237 -0.0328 0.0417  -0.0103 892  PHE A C   
2668 O O   . PHE A 355 ? 0.3442 0.4377 0.4248 -0.0271 0.0473  -0.0216 892  PHE A O   
2669 C CB  . PHE A 355 ? 0.3493 0.4305 0.3819 -0.0384 0.0377  -0.0027 892  PHE A CB  
2670 C CG  . PHE A 355 ? 0.3463 0.4137 0.3659 -0.0347 0.0309  -0.0011 892  PHE A CG  
2671 C CD1 . PHE A 355 ? 0.3397 0.4016 0.3546 -0.0283 0.0330  -0.0119 892  PHE A CD1 
2672 C CD2 . PHE A 355 ? 0.3394 0.3993 0.3556 -0.0377 0.0223  0.0116  892  PHE A CD2 
2673 C CE1 . PHE A 355 ? 0.3369 0.3876 0.3418 -0.0254 0.0272  -0.0100 892  PHE A CE1 
2674 C CE2 . PHE A 355 ? 0.3425 0.3915 0.3514 -0.0340 0.0169  0.0128  892  PHE A CE2 
2675 C CZ  . PHE A 355 ? 0.3464 0.3914 0.3485 -0.0282 0.0196  0.0020  892  PHE A CZ  
2676 N N   . GLU A 356 ? 0.3741 0.4745 0.4515 -0.0409 0.0430  -0.0018 893  GLU A N   
2677 C CA  . GLU A 356 ? 0.4024 0.5210 0.4994 -0.0435 0.0526  -0.0066 893  GLU A CA  
2678 C C   . GLU A 356 ? 0.3582 0.4712 0.4802 -0.0345 0.0466  -0.0107 893  GLU A C   
2679 O O   . GLU A 356 ? 0.3567 0.4824 0.5000 -0.0320 0.0545  -0.0191 893  GLU A O   
2680 C CB  . GLU A 356 ? 0.4529 0.5840 0.5520 -0.0556 0.0543  0.0058  893  GLU A CB  
2681 C CG  . GLU A 356 ? 0.5083 0.6622 0.6272 -0.0602 0.0670  0.0009  893  GLU A CG  
2682 C CD  . GLU A 356 ? 0.5549 0.7248 0.6681 -0.0618 0.0839  -0.0140 893  GLU A CD  
2683 O OE1 . GLU A 356 ? 0.5772 0.7497 0.6630 -0.0689 0.0878  -0.0135 893  GLU A OE1 
2684 O OE2 . GLU A 356 ? 0.5607 0.7403 0.6983 -0.0563 0.0928  -0.0266 893  GLU A OE2 
2685 N N   . ALA A 357 ? 0.3044 0.3995 0.4253 -0.0305 0.0327  -0.0053 894  ALA A N   
2686 C CA  . ALA A 357 ? 0.2590 0.3489 0.3994 -0.0244 0.0244  -0.0073 894  ALA A CA  
2687 C C   . ALA A 357 ? 0.2608 0.3453 0.4041 -0.0153 0.0238  -0.0160 894  ALA A C   
2688 O O   . ALA A 357 ? 0.2618 0.3463 0.4256 -0.0110 0.0177  -0.0168 894  ALA A O   
2689 C CB  . ALA A 357 ? 0.2351 0.3082 0.3694 -0.0252 0.0105  -0.0007 894  ALA A CB  
2690 N N   . LEU A 358 ? 0.2793 0.3589 0.4042 -0.0131 0.0287  -0.0210 895  LEU A N   
2691 C CA  . LEU A 358 ? 0.2873 0.3603 0.4159 -0.0052 0.0278  -0.0283 895  LEU A CA  
2692 C C   . LEU A 358 ? 0.3100 0.3967 0.4688 -0.0017 0.0355  -0.0363 895  LEU A C   
2693 O O   . LEU A 358 ? 0.3156 0.4192 0.4827 -0.0060 0.0487  -0.0417 895  LEU A O   
2694 C CB  . LEU A 358 ? 0.2851 0.3532 0.3907 -0.0052 0.0331  -0.0328 895  LEU A CB  
2695 C CG  . LEU A 358 ? 0.2771 0.3294 0.3592 -0.0052 0.0248  -0.0269 895  LEU A CG  
2696 C CD1 . LEU A 358 ? 0.2918 0.3442 0.3557 -0.0069 0.0311  -0.0309 895  LEU A CD1 
2697 C CD2 . LEU A 358 ? 0.2583 0.2968 0.3428 0.0007  0.0144  -0.0260 895  LEU A CD2 
2698 N N   . GLN A 359 ? 0.3234 0.4036 0.5006 0.0053  0.0275  -0.0370 896  GLN A N   
2699 C CA  . GLN A 359 ? 0.3479 0.4395 0.5605 0.0102  0.0344  -0.0451 896  GLN A CA  
2700 C C   . GLN A 359 ? 0.3614 0.4572 0.5691 0.0111  0.0497  -0.0591 896  GLN A C   
2701 O O   . GLN A 359 ? 0.3728 0.4577 0.5531 0.0106  0.0492  -0.0605 896  GLN A O   
2702 C CB  . GLN A 359 ? 0.3839 0.4665 0.6188 0.0170  0.0200  -0.0400 896  GLN A CB  
2703 C CG  . GLN A 359 ? 0.4196 0.4828 0.6297 0.0188  0.0091  -0.0352 896  GLN A CG  
2704 C CD  . GLN A 359 ? 0.4491 0.5059 0.6829 0.0239  -0.0046 -0.0289 896  GLN A CD  
2705 O OE1 . GLN A 359 ? 0.4614 0.5102 0.6992 0.0284  -0.0049 -0.0317 896  GLN A OE1 
2706 N NE2 . GLN A 359 ? 0.4487 0.5087 0.6989 0.0220  -0.0173 -0.0190 896  GLN A NE2 
2707 N N   . GLU A 360 ? 0.4368 0.4989 0.6255 0.1343  -0.0014 0.0502  897  GLU A N   
2708 C CA  . GLU A 360 ? 0.4372 0.5171 0.6142 0.1398  0.0132  0.0434  897  GLU A CA  
2709 C C   . GLU A 360 ? 0.4143 0.4610 0.5569 0.1432  0.0134  0.0280  897  GLU A C   
2710 O O   . GLU A 360 ? 0.4083 0.4595 0.5323 0.1415  0.0230  0.0229  897  GLU A O   
2711 C CB  . GLU A 360 ? 0.4613 0.5742 0.6621 0.1515  0.0201  0.0424  897  GLU A CB  
2712 C CG  . GLU A 360 ? 0.4749 0.6226 0.6732 0.1539  0.0373  0.0412  897  GLU A CG  
2713 C CD  . GLU A 360 ? 0.4914 0.6792 0.7209 0.1632  0.0452  0.0447  897  GLU A CD  
2714 O OE1 . GLU A 360 ? 0.4759 0.6886 0.7354 0.1576  0.0433  0.0607  897  GLU A OE1 
2715 O OE2 . GLU A 360 ? 0.5177 0.7119 0.7432 0.1760  0.0533  0.0310  897  GLU A OE2 
2716 N N   . ARG A 361 ? 0.4033 0.4167 0.5368 0.1471  0.0022  0.0215  898  ARG A N   
2717 C CA  . ARG A 361 ? 0.3913 0.3736 0.4949 0.1505  0.0023  0.0079  898  ARG A CA  
2718 C C   . ARG A 361 ? 0.3736 0.3348 0.4517 0.1386  0.0029  0.0080  898  ARG A C   
2719 O O   . ARG A 361 ? 0.3180 0.2725 0.3754 0.1379  0.0097  -0.0003 898  ARG A O   
2720 C CB  . ARG A 361 ? 0.4183 0.3715 0.5203 0.1574  -0.0107 0.0037  898  ARG A CB  
2721 C CG  . ARG A 361 ? 0.4697 0.3842 0.5401 0.1571  -0.0134 -0.0065 898  ARG A CG  
2722 C CD  . ARG A 361 ? 0.5249 0.4118 0.5948 0.1640  -0.0272 -0.0083 898  ARG A CD  
2723 N NE  . ARG A 361 ? 0.5602 0.4075 0.5994 0.1565  -0.0335 -0.0105 898  ARG A NE  
2724 C CZ  . ARG A 361 ? 0.5959 0.4207 0.6127 0.1572  -0.0302 -0.0196 898  ARG A CZ  
2725 N NH1 . ARG A 361 ? 0.6003 0.4353 0.6189 0.1653  -0.0210 -0.0298 898  ARG A NH1 
2726 N NH2 . ARG A 361 ? 0.6141 0.4117 0.6076 0.1447  -0.0344 -0.0180 898  ARG A NH2 
2727 N N   . LYS A 362 ? 0.3668 0.3167 0.4468 0.1292  -0.0042 0.0165  899  LYS A N   
2728 C CA  . LYS A 362 ? 0.3950 0.3270 0.4547 0.1187  -0.0025 0.0168  899  LYS A CA  
2729 C C   . LYS A 362 ? 0.3859 0.3458 0.4502 0.1134  0.0085  0.0221  899  LYS A C   
2730 O O   . LYS A 362 ? 0.3897 0.3404 0.4357 0.1079  0.0128  0.0190  899  LYS A O   
2731 C CB  . LYS A 362 ? 0.4038 0.3178 0.4655 0.1108  -0.0117 0.0230  899  LYS A CB  
2732 C CG  . LYS A 362 ? 0.4285 0.3153 0.4825 0.1145  -0.0242 0.0192  899  LYS A CG  
2733 C CD  . LYS A 362 ? 0.4549 0.3119 0.4909 0.1053  -0.0303 0.0192  899  LYS A CD  
2734 C CE  . LYS A 362 ? 0.4858 0.3107 0.5014 0.1081  -0.0407 0.0140  899  LYS A CE  
2735 N NZ  . LYS A 362 ? 0.4995 0.3277 0.5316 0.1133  -0.0535 0.0175  899  LYS A NZ  
2736 N N   . ARG A 363 ? 0.3652 0.3603 0.4545 0.1146  0.0125  0.0312  900  ARG A N   
2737 C CA  . ARG A 363 ? 0.3482 0.3732 0.4411 0.1101  0.0226  0.0378  900  ARG A CA  
2738 C C   . ARG A 363 ? 0.3433 0.3730 0.4157 0.1148  0.0308  0.0260  900  ARG A C   
2739 O O   . ARG A 363 ? 0.3412 0.3769 0.4009 0.1085  0.0360  0.0269  900  ARG A O   
2740 C CB  . ARG A 363 ? 0.3596 0.4223 0.4833 0.1108  0.0256  0.0505  900  ARG A CB  
2741 C CG  . ARG A 363 ? 0.3884 0.4874 0.5152 0.1075  0.0366  0.0581  900  ARG A CG  
2742 C CD  . ARG A 363 ? 0.4166 0.5537 0.5654 0.1139  0.0432  0.0632  900  ARG A CD  
2743 N NE  . ARG A 363 ? 0.4293 0.5734 0.6093 0.1124  0.0363  0.0748  900  ARG A NE  
2744 C CZ  . ARG A 363 ? 0.4411 0.6193 0.6476 0.1161  0.0406  0.0829  900  ARG A CZ  
2745 N NH1 . ARG A 363 ? 0.4572 0.6663 0.6611 0.1223  0.0534  0.0797  900  ARG A NH1 
2746 N NH2 . ARG A 363 ? 0.4320 0.6143 0.6679 0.1131  0.0324  0.0937  900  ARG A NH2 
2747 N N   . LYS A 364 ? 0.3450 0.3711 0.4145 0.1260  0.0314  0.0145  901  LYS A N   
2748 C CA  . LYS A 364 ? 0.3578 0.3868 0.4082 0.1312  0.0391  0.0009  901  LYS A CA  
2749 C C   . LYS A 364 ? 0.3747 0.3686 0.3973 0.1265  0.0357  -0.0085 901  LYS A C   
2750 O O   . LYS A 364 ? 0.3824 0.3808 0.3879 0.1233  0.0413  -0.0148 901  LYS A O   
2751 C CB  . LYS A 364 ? 0.3640 0.3966 0.4224 0.1456  0.0408  -0.0097 901  LYS A CB  
2752 C CG  . LYS A 364 ? 0.3678 0.4438 0.4519 0.1509  0.0489  -0.0028 901  LYS A CG  
2753 C CD  . LYS A 364 ? 0.3689 0.4488 0.4648 0.1666  0.0511  -0.0139 901  LYS A CD  
2754 C CE  . LYS A 364 ? 0.3695 0.4896 0.4698 0.1728  0.0666  -0.0185 901  LYS A CE  
2755 N NZ  . LYS A 364 ? 0.3825 0.5149 0.5040 0.1887  0.0705  -0.0264 901  LYS A NZ  
2756 N N   . ILE A 365 ? 0.3672 0.3268 0.3845 0.1252  0.0263  -0.0092 902  ILE A N   
2757 C CA  . ILE A 365 ? 0.3579 0.2850 0.3506 0.1191  0.0234  -0.0155 902  ILE A CA  
2758 C C   . ILE A 365 ? 0.3360 0.2731 0.3244 0.1073  0.0274  -0.0081 902  ILE A C   
2759 O O   . ILE A 365 ? 0.3257 0.2594 0.2974 0.1031  0.0307  -0.0142 902  ILE A O   
2760 C CB  . ILE A 365 ? 0.3642 0.2570 0.3526 0.1184  0.0132  -0.0144 902  ILE A CB  
2761 C CG1 . ILE A 365 ? 0.3720 0.2510 0.3622 0.1303  0.0078  -0.0222 902  ILE A CG1 
2762 C CG2 . ILE A 365 ? 0.3696 0.2337 0.3353 0.1092  0.0120  -0.0168 902  ILE A CG2 
2763 C CD1 . ILE A 365 ? 0.3789 0.2297 0.3670 0.1299  -0.0039 -0.0183 902  ILE A CD1 
2764 N N   . LEU A 366 ? 0.3512 0.3006 0.3565 0.1017  0.0263  0.0055  903  LEU A N   
2765 C CA  . LEU A 366 ? 0.2879 0.2473 0.2943 0.0913  0.0294  0.0143  903  LEU A CA  
2766 C C   . LEU A 366 ? 0.3253 0.3150 0.3290 0.0899  0.0367  0.0150  903  LEU A C   
2767 O O   . LEU A 366 ? 0.3167 0.3060 0.3094 0.0827  0.0383  0.0151  903  LEU A O   
2768 C CB  . LEU A 366 ? 0.4051 0.3744 0.4347 0.0873  0.0270  0.0284  903  LEU A CB  
2769 C CG  . LEU A 366 ? 0.2598 0.2454 0.2987 0.0781  0.0303  0.0403  903  LEU A CG  
2770 C CD1 . LEU A 366 ? 0.2631 0.2244 0.2868 0.0716  0.0300  0.0365  903  LEU A CD1 
2771 C CD2 . LEU A 366 ? 0.2472 0.2432 0.3128 0.0753  0.0275  0.0538  903  LEU A CD2 
2772 N N   . ASP A 367 ? 0.2883 0.3059 0.3017 0.0964  0.0411  0.0155  904  ASP A N   
2773 C CA  . ASP A 367 ? 0.3388 0.3887 0.3478 0.0943  0.0485  0.0174  904  ASP A CA  
2774 C C   . ASP A 367 ? 0.3685 0.4071 0.3508 0.0955  0.0505  0.0006  904  ASP A C   
2775 O O   . ASP A 367 ? 0.3685 0.4210 0.3396 0.0885  0.0529  0.0017  904  ASP A O   
2776 C CB  . ASP A 367 ? 0.3211 0.4052 0.3469 0.1008  0.0543  0.0221  904  ASP A CB  
2777 C CG  . ASP A 367 ? 0.2998 0.4075 0.3514 0.0946  0.0540  0.0430  904  ASP A CG  
2778 O OD1 . ASP A 367 ? 0.2815 0.3861 0.3350 0.0851  0.0512  0.0532  904  ASP A OD1 
2779 O OD2 . ASP A 367 ? 0.2873 0.4164 0.3593 0.0992  0.0563  0.0495  904  ASP A OD2 
2780 N N   . GLU A 368 ? 0.4038 0.4164 0.3765 0.1037  0.0483  -0.0144 905  GLU A N   
2781 C CA  . GLU A 368 ? 0.4445 0.4389 0.3928 0.1037  0.0484  -0.0308 905  GLU A CA  
2782 C C   . GLU A 368 ? 0.4250 0.4011 0.3620 0.0918  0.0441  -0.0277 905  GLU A C   
2783 O O   . GLU A 368 ? 0.4419 0.4220 0.3634 0.0860  0.0453  -0.0336 905  GLU A O   
2784 C CB  . GLU A 368 ? 0.4967 0.4614 0.4407 0.1142  0.0450  -0.0448 905  GLU A CB  
2785 C CG  . GLU A 368 ? 0.5567 0.4951 0.4776 0.1134  0.0433  -0.0612 905  GLU A CG  
2786 C CD  . GLU A 368 ? 0.6152 0.5331 0.5352 0.1263  0.0418  -0.0758 905  GLU A CD  
2787 O OE1 . GLU A 368 ? 0.6331 0.5225 0.5571 0.1295  0.0346  -0.0739 905  GLU A OE1 
2788 O OE2 . GLU A 368 ? 0.6363 0.5675 0.5516 0.1337  0.0480  -0.0890 905  GLU A OE2 
2789 N N   . ALA A 369 ? 0.3920 0.3490 0.3370 0.0878  0.0393  -0.0189 906  ALA A N   
2790 C CA  . ALA A 369 ? 0.3749 0.3166 0.3127 0.0771  0.0369  -0.0153 906  ALA A CA  
2791 C C   . ALA A 369 ? 0.3739 0.3455 0.3181 0.0685  0.0396  -0.0040 906  ALA A C   
2792 O O   . ALA A 369 ? 0.3860 0.3561 0.3197 0.0607  0.0388  -0.0060 906  ALA A O   
2793 C CB  . ALA A 369 ? 0.3448 0.2635 0.2903 0.0753  0.0330  -0.0085 906  ALA A CB  
2794 N N   . VAL A 370 ? 0.3697 0.3694 0.3329 0.0693  0.0419  0.0091  907  VAL A N   
2795 C CA  . VAL A 370 ? 0.3785 0.4078 0.3502 0.0613  0.0435  0.0229  907  VAL A CA  
2796 C C   . VAL A 370 ? 0.4157 0.4641 0.3692 0.0593  0.0458  0.0156  907  VAL A C   
2797 O O   . VAL A 370 ? 0.4046 0.4650 0.3545 0.0503  0.0442  0.0215  907  VAL A O   
2798 C CB  . VAL A 370 ? 0.3620 0.4172 0.3582 0.0629  0.0452  0.0388  907  VAL A CB  
2799 C CG1 . VAL A 370 ? 0.3599 0.4499 0.3632 0.0554  0.0468  0.0538  907  VAL A CG1 
2800 C CG2 . VAL A 370 ? 0.3487 0.3847 0.3627 0.0619  0.0417  0.0464  907  VAL A CG2 
2801 N N   . GLU A 371 ? 0.4632 0.5150 0.4053 0.0677  0.0493  0.0021  908  GLU A N   
2802 C CA  . GLU A 371 ? 0.5001 0.5697 0.4222 0.0666  0.0523  -0.0078 908  GLU A CA  
2803 C C   . GLU A 371 ? 0.4876 0.5328 0.3889 0.0608  0.0476  -0.0212 908  GLU A C   
2804 O O   . GLU A 371 ? 0.4984 0.5584 0.3828 0.0559  0.0478  -0.0274 908  GLU A O   
2805 C CB  . GLU A 371 ? 0.5651 0.6431 0.4826 0.0786  0.0586  -0.0207 908  GLU A CB  
2806 C CG  . GLU A 371 ? 0.6272 0.7386 0.5651 0.0827  0.0644  -0.0065 908  GLU A CG  
2807 C CD  . GLU A 371 ? 0.7081 0.8222 0.6494 0.0963  0.0704  -0.0185 908  GLU A CD  
2808 O OE1 . GLU A 371 ? 0.7089 0.8495 0.6695 0.1003  0.0753  -0.0077 908  GLU A OE1 
2809 O OE2 . GLU A 371 ? 0.7788 0.8684 0.7056 0.1031  0.0699  -0.0383 908  GLU A OE2 
2810 N N   . LEU A 372 ? 0.4762 0.4852 0.3777 0.0603  0.0433  -0.0253 909  LEU A N   
2811 C CA  . LEU A 372 ? 0.4866 0.4737 0.3722 0.0526  0.0386  -0.0346 909  LEU A CA  
2812 C C   . LEU A 372 ? 0.3624 0.3713 0.2494 0.0402  0.0361  -0.0235 909  LEU A C   
2813 O O   . LEU A 372 ? 0.3792 0.3868 0.2501 0.0334  0.0327  -0.0323 909  LEU A O   
2814 C CB  . LEU A 372 ? 0.4325 0.3821 0.3216 0.0520  0.0352  -0.0350 909  LEU A CB  
2815 C CG  . LEU A 372 ? 0.4098 0.3278 0.2911 0.0614  0.0341  -0.0487 909  LEU A CG  
2816 C CD1 . LEU A 372 ? 0.4021 0.2885 0.2864 0.0585  0.0308  -0.0441 909  LEU A CD1 
2817 C CD2 . LEU A 372 ? 0.4188 0.3241 0.2802 0.0622  0.0327  -0.0677 909  LEU A CD2 
2818 N N   . SER A 373 ? 0.3407 0.3693 0.2482 0.0371  0.0367  -0.0040 910  SER A N   
2819 C CA  . SER A 373 ? 0.3837 0.4311 0.2982 0.0259  0.0332  0.0095  910  SER A CA  
2820 C C   . SER A 373 ? 0.3976 0.4836 0.3054 0.0224  0.0334  0.0151  910  SER A C   
2821 O O   . SER A 373 ? 0.4106 0.5126 0.3190 0.0123  0.0285  0.0238  910  SER A O   
2822 C CB  . SER A 373 ? 0.3592 0.4081 0.3011 0.0244  0.0335  0.0281  910  SER A CB  
2823 O OG  . SER A 373 ? 0.3421 0.4074 0.2982 0.0309  0.0371  0.0374  910  SER A OG  
2824 N N   . GLN A 374 ? 0.4097 0.5125 0.3116 0.0300  0.0389  0.0112  911  GLN A N   
2825 C CA  . GLN A 374 ? 0.4460 0.5888 0.3417 0.0263  0.0403  0.0196  911  GLN A CA  
2826 C C   . GLN A 374 ? 0.4770 0.6244 0.3438 0.0200  0.0369  0.0049  911  GLN A C   
2827 O O   . GLN A 374 ? 0.4898 0.6093 0.3400 0.0220  0.0356  -0.0160 911  GLN A O   
2828 C CB  . GLN A 374 ? 0.4801 0.6411 0.3781 0.0363  0.0489  0.0190  911  GLN A CB  
2829 C CG  . GLN A 374 ? 0.4885 0.6539 0.4173 0.0397  0.0507  0.0375  911  GLN A CG  
2830 C CD  . GLN A 374 ? 0.5243 0.6918 0.4585 0.0516  0.0580  0.0312  911  GLN A CD  
2831 O OE1 . GLN A 374 ? 0.5549 0.7233 0.4709 0.0585  0.0629  0.0134  911  GLN A OE1 
2832 N NE2 . GLN A 374 ? 0.5181 0.6863 0.4790 0.0542  0.0583  0.0453  911  GLN A NE2 
2833 N N   A ASP A 375 ? 0.4811 0.6634 0.3420 0.0116  0.0344  0.0167  912  ASP A N   
2834 N N   B ASP A 375 ? 0.4813 0.6639 0.3422 0.0117  0.0345  0.0166  912  ASP A N   
2835 C CA  A ASP A 375 ? 0.5064 0.6980 0.3386 0.0035  0.0294  0.0047  912  ASP A CA  
2836 C CA  B ASP A 375 ? 0.5087 0.7007 0.3412 0.0034  0.0293  0.0050  912  ASP A CA  
2837 C C   A ASP A 375 ? 0.5119 0.6759 0.3428 -0.0047 0.0202  -0.0022 912  ASP A C   
2838 C C   B ASP A 375 ? 0.5117 0.6753 0.3428 -0.0045 0.0202  -0.0022 912  ASP A C   
2839 O O   A ASP A 375 ? 0.5377 0.6826 0.3463 -0.0060 0.0177  -0.0241 912  ASP A O   
2840 O O   B ASP A 375 ? 0.5370 0.6808 0.3462 -0.0055 0.0179  -0.0243 912  ASP A O   
2841 C CB  A ASP A 375 ? 0.5295 0.7197 0.3341 0.0117  0.0365  -0.0204 912  ASP A CB  
2842 C CB  B ASP A 375 ? 0.5297 0.7219 0.3340 0.0112  0.0363  -0.0196 912  ASP A CB  
2843 C CG  A ASP A 375 ? 0.5296 0.7530 0.3350 0.0187  0.0468  -0.0134 912  ASP A CG  
2844 C CG  B ASP A 375 ? 0.5553 0.7661 0.3281 0.0021  0.0318  -0.0299 912  ASP A CG  
2845 O OD1 A ASP A 375 ? 0.5254 0.7850 0.3334 0.0115  0.0458  0.0069  912  ASP A OD1 
2846 O OD1 B ASP A 375 ? 0.5472 0.7801 0.3212 -0.0102 0.0235  -0.0131 912  ASP A OD1 
2847 O OD2 A ASP A 375 ? 0.5311 0.7454 0.3361 0.0313  0.0557  -0.0269 912  ASP A OD2 
2848 O OD2 B ASP A 375 ? 0.5759 0.7788 0.3232 0.0073  0.0360  -0.0553 912  ASP A OD2 
2849 N N   . HIS A 376 ? 0.4938 0.6557 0.3507 -0.0102 0.0155  0.0168  913  HIS A N   
2850 C CA  . HIS A 376 ? 0.5107 0.6512 0.3724 -0.0188 0.0078  0.0145  913  HIS A CA  
2851 C C   . HIS A 376 ? 0.5108 0.6091 0.3636 -0.0134 0.0100  -0.0068 913  HIS A C   
2852 O O   . HIS A 376 ? 0.5372 0.6184 0.3761 -0.0201 0.0043  -0.0205 913  HIS A O   
2853 C CB  . HIS A 376 ? 0.5696 0.7297 0.4147 -0.0317 -0.0020 0.0135  913  HIS A CB  
2854 C CG  . HIS A 376 ? 0.5915 0.7927 0.4464 -0.0383 -0.0062 0.0375  913  HIS A CG  
2855 N ND1 . HIS A 376 ? 0.5739 0.7844 0.4616 -0.0424 -0.0099 0.0616  913  HIS A ND1 
2856 C CD2 . HIS A 376 ? 0.6166 0.8523 0.4531 -0.0414 -0.0073 0.0418  913  HIS A CD2 
2857 C CE1 . HIS A 376 ? 0.5824 0.8302 0.4731 -0.0477 -0.0142 0.0810  913  HIS A CE1 
2858 N NE2 . HIS A 376 ? 0.6012 0.8657 0.4598 -0.0478 -0.0127 0.0700  913  HIS A NE2 
2859 N N   . PHE A 377 ? 0.4918 0.5733 0.3532 -0.0018 0.0175  -0.0088 914  PHE A N   
2860 C CA  . PHE A 377 ? 0.4931 0.5342 0.3494 0.0041  0.0192  -0.0250 914  PHE A CA  
2861 C C   . PHE A 377 ? 0.5246 0.5525 0.3532 0.0060  0.0182  -0.0495 914  PHE A C   
2862 O O   . PHE A 377 ? 0.5341 0.5297 0.3549 0.0041  0.0148  -0.0627 914  PHE A O   
2863 C CB  . PHE A 377 ? 0.4698 0.4881 0.3387 -0.0034 0.0152  -0.0196 914  PHE A CB  
2864 C CG  . PHE A 377 ? 0.4348 0.4587 0.3314 -0.0026 0.0180  0.0003  914  PHE A CG  
2865 C CD1 . PHE A 377 ? 0.4121 0.4668 0.3258 -0.0088 0.0157  0.0193  914  PHE A CD1 
2866 C CD2 . PHE A 377 ? 0.4115 0.4090 0.3170 0.0042  0.0223  -0.0001 914  PHE A CD2 
2867 C CE1 . PHE A 377 ? 0.3837 0.4413 0.3247 -0.0074 0.0183  0.0361  914  PHE A CE1 
2868 C CE2 . PHE A 377 ? 0.3869 0.3880 0.3164 0.0049  0.0250  0.0157  914  PHE A CE2 
2869 C CZ  . PHE A 377 ? 0.3702 0.4005 0.3184 -0.0005 0.0233  0.0332  914  PHE A CZ  
2870 N N   . LYS A 378 ? 0.5499 0.6026 0.3636 0.0099  0.0216  -0.0559 915  LYS A N   
2871 C CA  . LYS A 378 ? 0.5964 0.6380 0.3836 0.0131  0.0219  -0.0814 915  LYS A CA  
2872 C C   . LYS A 378 ? 0.5942 0.5992 0.3823 0.0254  0.0258  -0.0964 915  LYS A C   
2873 O O   . LYS A 378 ? 0.6220 0.5961 0.3979 0.0242  0.0216  -0.1141 915  LYS A O   
2874 C CB  . LYS A 378 ? 0.6304 0.7087 0.4026 0.0165  0.0276  -0.0845 915  LYS A CB  
2875 C CG  . LYS A 378 ? 0.6824 0.7503 0.4288 0.0238  0.0313  -0.1132 915  LYS A CG  
2876 C CD  . LYS A 378 ? 0.6968 0.8029 0.4326 0.0302  0.0410  -0.1144 915  LYS A CD  
2877 C CE  . LYS A 378 ? 0.7313 0.8261 0.4457 0.0409  0.0477  -0.1443 915  LYS A CE  
2878 N NZ  . LYS A 378 ? 0.7677 0.8562 0.4522 0.0315  0.0408  -0.1648 915  LYS A NZ  
2879 N N   . LYS A 379 ? 0.5566 0.5643 0.3607 0.0368  0.0326  -0.0887 916  LYS A N   
2880 C CA  . LYS A 379 ? 0.5520 0.5272 0.3586 0.0488  0.0350  -0.1009 916  LYS A CA  
2881 C C   . LYS A 379 ? 0.5415 0.4796 0.3558 0.0443  0.0291  -0.0973 916  LYS A C   
2882 O O   . LYS A 379 ? 0.5667 0.4709 0.3751 0.0494  0.0271  -0.1111 916  LYS A O   
2883 C CB  . LYS A 379 ? 0.5408 0.5313 0.3641 0.0610  0.0424  -0.0922 916  LYS A CB  
2884 C CG  . LYS A 379 ? 0.5657 0.5851 0.3805 0.0694  0.0507  -0.1015 916  LYS A CG  
2885 C CD  . LYS A 379 ? 0.5574 0.5961 0.3939 0.0791  0.0575  -0.0887 916  LYS A CD  
2886 C CE  . LYS A 379 ? 0.5699 0.6377 0.3999 0.0886  0.0676  -0.0985 916  LYS A CE  
2887 N NZ  . LYS A 379 ? 0.5433 0.6325 0.3978 0.0968  0.0740  -0.0842 916  LYS A NZ  
2888 N N   . TYR A 380 ? 0.5031 0.4473 0.3312 0.0352  0.0266  -0.0786 917  TYR A N   
2889 C CA  . TYR A 380 ? 0.4970 0.4091 0.3310 0.0301  0.0227  -0.0751 917  TYR A CA  
2890 C C   . TYR A 380 ? 0.5284 0.4176 0.3468 0.0216  0.0165  -0.0889 917  TYR A C   
2891 O O   . TYR A 380 ? 0.5363 0.3903 0.3525 0.0219  0.0141  -0.0947 917  TYR A O   
2892 C CB  . TYR A 380 ? 0.4720 0.3980 0.3243 0.0220  0.0225  -0.0542 917  TYR A CB  
2893 C CG  . TYR A 380 ? 0.4649 0.3642 0.3202 0.0133  0.0192  -0.0516 917  TYR A CG  
2894 C CD1 . TYR A 380 ? 0.4506 0.3171 0.3063 0.0178  0.0202  -0.0536 917  TYR A CD1 
2895 C CD2 . TYR A 380 ? 0.4086 0.3170 0.2666 0.0002  0.0152  -0.0465 917  TYR A CD2 
2896 C CE1 . TYR A 380 ? 0.4120 0.2560 0.2692 0.0094  0.0186  -0.0505 917  TYR A CE1 
2897 C CE2 . TYR A 380 ? 0.4098 0.2964 0.2725 -0.0079 0.0136  -0.0436 917  TYR A CE2 
2898 C CZ  . TYR A 380 ? 0.4630 0.3174 0.3244 -0.0033 0.0161  -0.0456 917  TYR A CZ  
2899 O OH  . TYR A 380 ? 0.4152 0.2494 0.2800 -0.0119 0.0158  -0.0420 917  TYR A OH  
2900 N N   . LEU A 381 ? 0.5586 0.4676 0.3661 0.0132  0.0131  -0.0939 918  LEU A N   
2901 C CA  . LEU A 381 ? 0.6060 0.4952 0.4013 0.0024  0.0057  -0.1055 918  LEU A CA  
2902 C C   . LEU A 381 ? 0.6607 0.5198 0.4398 0.0097  0.0047  -0.1290 918  LEU A C   
2903 O O   . LEU A 381 ? 0.6779 0.5053 0.4525 0.0034  -0.0011 -0.1370 918  LEU A O   
2904 C CB  . LEU A 381 ? 0.6193 0.5394 0.4070 -0.0093 0.0006  -0.1041 918  LEU A CB  
2905 C CG  . LEU A 381 ? 0.5998 0.5417 0.4072 -0.0196 -0.0016 -0.0809 918  LEU A CG  
2906 C CD1 . LEU A 381 ? 0.6122 0.5912 0.4131 -0.0289 -0.0069 -0.0763 918  LEU A CD1 
2907 C CD2 . LEU A 381 ? 0.5954 0.5116 0.4122 -0.0296 -0.0060 -0.0776 918  LEU A CD2 
2908 N N   . VAL A 382 ? 0.6827 0.5509 0.4549 0.0230  0.0105  -0.1398 919  VAL A N   
2909 C CA  . VAL A 382 ? 0.7227 0.5612 0.4831 0.0319  0.0101  -0.1627 919  VAL A CA  
2910 C C   . VAL A 382 ? 0.7192 0.5233 0.4915 0.0403  0.0103  -0.1592 919  VAL A C   
2911 O O   . VAL A 382 ? 0.7546 0.5231 0.5213 0.0432  0.0064  -0.1734 919  VAL A O   
2912 C CB  . VAL A 382 ? 0.7309 0.5921 0.4809 0.0439  0.0174  -0.1769 919  VAL A CB  
2913 C CG1 . VAL A 382 ? 0.7331 0.6354 0.4715 0.0349  0.0178  -0.1739 919  VAL A CG1 
2914 C CG2 . VAL A 382 ? 0.7073 0.5785 0.4734 0.0592  0.0258  -0.1683 919  VAL A CG2 
2915 N N   . LYS A 383 ? 0.6826 0.4953 0.4713 0.0438  0.0139  -0.1402 920  LYS A N   
2916 C CA  . LYS A 383 ? 0.6808 0.4621 0.4782 0.0507  0.0129  -0.1359 920  LYS A CA  
2917 C C   . LYS A 383 ? 0.6818 0.4356 0.4797 0.0383  0.0073  -0.1284 920  LYS A C   
2918 O O   . LYS A 383 ? 0.6906 0.4092 0.4878 0.0412  0.0040  -0.1307 920  LYS A O   
2919 C CB  . LYS A 383 ? 0.6576 0.4571 0.4708 0.0586  0.0181  -0.1201 920  LYS A CB  
2920 C CG  . LYS A 383 ? 0.6768 0.4472 0.4964 0.0686  0.0164  -0.1190 920  LYS A CG  
2921 C CD  . LYS A 383 ? 0.6645 0.4531 0.4996 0.0756  0.0201  -0.1047 920  LYS A CD  
2922 C CE  . LYS A 383 ? 0.6833 0.4440 0.5236 0.0855  0.0166  -0.1042 920  LYS A CE  
2923 N NZ  . LYS A 383 ? 0.6729 0.4478 0.5278 0.0892  0.0181  -0.0892 920  LYS A NZ  
2924 N N   . LEU A 384 ? 0.6610 0.4312 0.4614 0.0244  0.0062  -0.1182 921  LEU A N   
2925 C CA  . LEU A 384 ? 0.6564 0.4037 0.4582 0.0116  0.0020  -0.1118 921  LEU A CA  
2926 C C   . LEU A 384 ? 0.7037 0.4208 0.4931 0.0067  -0.0049 -0.1285 921  LEU A C   
2927 O O   . LEU A 384 ? 0.7150 0.3989 0.5044 0.0027  -0.0082 -0.1267 921  LEU A O   
2928 C CB  . LEU A 384 ? 0.6108 0.3857 0.4212 -0.0014 0.0022  -0.0986 921  LEU A CB  
2929 C CG  . LEU A 384 ? 0.6073 0.3648 0.4217 -0.0160 -0.0012 -0.0922 921  LEU A CG  
2930 C CD1 . LEU A 384 ? 0.5957 0.3286 0.4153 -0.0134 0.0023  -0.0824 921  LEU A CD1 
2931 C CD2 . LEU A 384 ? 0.5924 0.3813 0.4189 -0.0277 -0.0014 -0.0798 921  LEU A CD2 
2932 N N   . LYS A 385 ? 0.7394 0.4670 0.5176 0.0066  -0.0072 -0.1448 922  LYS A N   
2933 C CA  . LYS A 385 ? 0.7864 0.4852 0.5530 0.0011  -0.0145 -0.1628 922  LYS A CA  
2934 C C   . LYS A 385 ? 0.7947 0.4567 0.5588 0.0139  -0.0154 -0.1749 922  LYS A C   
2935 O O   . LYS A 385 ? 0.8295 0.4676 0.5928 0.0091  -0.0213 -0.1862 922  LYS A O   
2936 C CB  . LYS A 385 ? 0.8325 0.5534 0.5851 -0.0019 -0.0166 -0.1791 922  LYS A CB  
2937 C CG  . LYS A 385 ? 0.8539 0.6066 0.6082 -0.0176 -0.0198 -0.1682 922  LYS A CG  
2938 C CD  . LYS A 385 ? 0.9060 0.6763 0.6419 -0.0226 -0.0243 -0.1858 922  LYS A CD  
2939 C CE  . LYS A 385 ? 0.9153 0.7159 0.6545 -0.0394 -0.0300 -0.1732 922  LYS A CE  
2940 N NZ  . LYS A 385 ? 0.9536 0.7748 0.6721 -0.0453 -0.0354 -0.1889 922  LYS A NZ  
2941 N N   . SER A 386 ? 0.7630 0.4273 0.5340 0.0291  -0.0098 -0.1700 923  SER A N   
2942 C CA  . SER A 386 ? 0.7695 0.4212 0.5545 0.0405  -0.0093 -0.1757 923  SER A CA  
2943 C C   . SER A 386 ? 0.7660 0.4039 0.5664 0.0428  -0.0099 -0.1576 923  SER A C   
2944 O O   . SER A 386 ? 0.7780 0.4085 0.5916 0.0520  -0.0097 -0.1586 923  SER A O   
2945 C CB  . SER A 386 ? 0.7556 0.4297 0.5409 0.0563  -0.0023 -0.1864 923  SER A CB  
2946 O OG  . SER A 386 ? 0.7224 0.4096 0.5144 0.0660  0.0023  -0.1730 923  SER A OG  
2947 N N   . ILE A 387 ? 0.7584 0.3930 0.5569 0.0342  -0.0103 -0.1413 924  ILE A N   
2948 C CA  . ILE A 387 ? 0.7632 0.3883 0.5732 0.0354  -0.0107 -0.1244 924  ILE A CA  
2949 C C   . ILE A 387 ? 0.7720 0.3751 0.5843 0.0227  -0.0155 -0.1181 924  ILE A C   
2950 O O   . ILE A 387 ? 0.7710 0.3686 0.5762 0.0099  -0.0175 -0.1207 924  ILE A O   
2951 C CB  . ILE A 387 ? 0.7518 0.3898 0.5597 0.0356  -0.0059 -0.1100 924  ILE A CB  
2952 C CG1 . ILE A 387 ? 0.7514 0.3990 0.5502 0.0232  -0.0036 -0.1077 924  ILE A CG1 
2953 C CG2 . ILE A 387 ? 0.7447 0.4018 0.5567 0.0508  -0.0018 -0.1122 924  ILE A CG2 
2954 C CD1 . ILE A 387 ? 0.7518 0.3838 0.5509 0.0085  -0.0044 -0.0959 924  ILE A CD1 
2955 N N   . ASN A 388 ? 0.7787 0.3694 0.6008 0.0258  -0.0177 -0.1093 925  ASN A N   
2956 C CA  . ASN A 388 ? 0.7937 0.3642 0.6179 0.0150  -0.0215 -0.1003 925  ASN A CA  
2957 C C   . ASN A 388 ? 0.7872 0.3610 0.6074 0.0075  -0.0183 -0.0824 925  ASN A C   
2958 O O   . ASN A 388 ? 0.7645 0.3520 0.5843 0.0138  -0.0146 -0.0755 925  ASN A O   
2959 C CB  . ASN A 388 ? 0.8081 0.3630 0.6422 0.0221  -0.0253 -0.0990 925  ASN A CB  
2960 C CG  . ASN A 388 ? 0.8324 0.3813 0.6725 0.0293  -0.0268 -0.1173 925  ASN A CG  
2961 O OD1 . ASN A 388 ? 0.8496 0.3962 0.6856 0.0234  -0.0276 -0.1305 925  ASN A OD1 
2962 N ND2 . ASN A 388 ? 0.8344 0.3805 0.6840 0.0418  -0.0270 -0.1188 925  ASN A ND2 
2963 N N   . PRO A 389 ? 0.7989 0.3609 0.6169 -0.0063 -0.0191 -0.0751 926  PRO A N   
2964 C CA  . PRO A 389 ? 0.7671 0.3318 0.5814 -0.0137 -0.0143 -0.0589 926  PRO A CA  
2965 C C   . PRO A 389 ? 0.7482 0.3090 0.5630 -0.0069 -0.0152 -0.0486 926  PRO A C   
2966 O O   . PRO A 389 ? 0.7656 0.3162 0.5854 0.0005  -0.0206 -0.0518 926  PRO A O   
2967 C CB  . PRO A 389 ? 0.8044 0.3551 0.6187 -0.0296 -0.0155 -0.0548 926  PRO A CB  
2968 C CG  . PRO A 389 ? 0.8329 0.3794 0.6489 -0.0322 -0.0206 -0.0707 926  PRO A CG  
2969 C CD  . PRO A 389 ? 0.8338 0.3810 0.6529 -0.0167 -0.0236 -0.0826 926  PRO A CD  
2970 N N   . PRO A 390 ? 0.7133 0.2815 0.5227 -0.0095 -0.0099 -0.0366 927  PRO A N   
2971 C CA  . PRO A 390 ? 0.6878 0.2687 0.4942 -0.0170 -0.0018 -0.0323 927  PRO A CA  
2972 C C   . PRO A 390 ? 0.6576 0.2575 0.4663 -0.0089 0.0015  -0.0381 927  PRO A C   
2973 O O   . PRO A 390 ? 0.6660 0.2723 0.4777 0.0033  -0.0013 -0.0425 927  PRO A O   
2974 C CB  . PRO A 390 ? 0.6845 0.2640 0.4844 -0.0202 0.0024  -0.0190 927  PRO A CB  
2975 C CG  . PRO A 390 ? 0.6939 0.2671 0.4920 -0.0102 -0.0041 -0.0177 927  PRO A CG  
2976 C CD  . PRO A 390 ? 0.7157 0.2771 0.5209 -0.0064 -0.0118 -0.0263 927  PRO A CD  
2977 N N   . CYS A 391 ? 0.6274 0.2361 0.4360 -0.0161 0.0078  -0.0372 928  CYS A N   
2978 C CA  . CYS A 391 ? 0.6133 0.2382 0.4235 -0.0095 0.0116  -0.0410 928  CYS A CA  
2979 C C   . CYS A 391 ? 0.5988 0.2378 0.4150 -0.0189 0.0202  -0.0331 928  CYS A C   
2980 O O   . CYS A 391 ? 0.6175 0.2511 0.4351 -0.0314 0.0229  -0.0278 928  CYS A O   
2981 C CB  . CYS A 391 ? 0.6631 0.2889 0.4703 -0.0055 0.0072  -0.0555 928  CYS A CB  
2982 S SG  . CYS A 391 ? 0.6930 0.3369 0.5071 -0.0204 0.0069  -0.0581 928  CYS A SG  
2983 N N   . VAL A 392 ? 0.5618 0.2286 0.3888 -0.0126 0.0242  -0.0306 929  VAL A N   
2984 C CA  . VAL A 392 ? 0.5410 0.2347 0.3838 -0.0190 0.0312  -0.0226 929  VAL A CA  
2985 C C   . VAL A 392 ? 0.4335 0.1587 0.2880 -0.0157 0.0291  -0.0258 929  VAL A C   
2986 O O   . VAL A 392 ? 0.4193 0.1585 0.2778 -0.0057 0.0294  -0.0258 929  VAL A O   
2987 C CB  . VAL A 392 ? 0.4374 0.1337 0.2839 -0.0155 0.0386  -0.0143 929  VAL A CB  
2988 C CG1 . VAL A 392 ? 0.4171 0.1412 0.2841 -0.0208 0.0459  -0.0069 929  VAL A CG1 
2989 C CG2 . VAL A 392 ? 0.4579 0.1245 0.2888 -0.0198 0.0409  -0.0108 929  VAL A CG2 
2990 N N   . PRO A 393 ? 0.5646 0.3023 0.4243 -0.0247 0.0265  -0.0277 930  PRO A N   
2991 C CA  . PRO A 393 ? 0.4252 0.1932 0.2920 -0.0226 0.0235  -0.0303 930  PRO A CA  
2992 C C   . PRO A 393 ? 0.4684 0.2664 0.3547 -0.0210 0.0289  -0.0184 930  PRO A C   
2993 O O   . PRO A 393 ? 0.3888 0.1862 0.2859 -0.0237 0.0352  -0.0093 930  PRO A O   
2994 C CB  . PRO A 393 ? 0.4389 0.2100 0.3058 -0.0353 0.0183  -0.0340 930  PRO A CB  
2995 C CG  . PRO A 393 ? 0.4631 0.1981 0.3185 -0.0409 0.0167  -0.0380 930  PRO A CG  
2996 C CD  . PRO A 393 ? 0.4560 0.1780 0.3124 -0.0374 0.0242  -0.0289 930  PRO A CD  
2997 N N   . PHE A 394 ? 0.4508 0.2748 0.3415 -0.0162 0.0266  -0.0187 931  PHE A N   
2998 C CA  . PHE A 394 ? 0.4402 0.2945 0.3515 -0.0156 0.0298  -0.0063 931  PHE A CA  
2999 C C   . PHE A 394 ? 0.4628 0.3341 0.3889 -0.0274 0.0289  0.0012  931  PHE A C   
3000 O O   . PHE A 394 ? 0.4706 0.3510 0.3914 -0.0344 0.0223  -0.0033 931  PHE A O   
3001 C CB  . PHE A 394 ? 0.4235 0.3018 0.3343 -0.0085 0.0273  -0.0072 931  PHE A CB  
3002 C CG  . PHE A 394 ? 0.4078 0.3189 0.3407 -0.0094 0.0287  0.0073  931  PHE A CG  
3003 C CD1 . PHE A 394 ? 0.3963 0.3082 0.3476 -0.0063 0.0343  0.0177  931  PHE A CD1 
3004 C CD2 . PHE A 394 ? 0.4043 0.3448 0.3392 -0.0134 0.0240  0.0105  931  PHE A CD2 
3005 C CE1 . PHE A 394 ? 0.3676 0.3077 0.3422 -0.0068 0.0350  0.0317  931  PHE A CE1 
3006 C CE2 . PHE A 394 ? 0.3854 0.3560 0.3419 -0.0144 0.0242  0.0261  931  PHE A CE2 
3007 C CZ  . PHE A 394 ? 0.3746 0.3442 0.3527 -0.0108 0.0296  0.0370  931  PHE A CZ  
3008 N N   . PHE A 395 ? 0.4737 0.3496 0.4192 -0.0296 0.0352  0.0120  932  PHE A N   
3009 C CA  . PHE A 395 ? 0.5080 0.3984 0.4713 -0.0406 0.0352  0.0197  932  PHE A CA  
3010 C C   . PHE A 395 ? 0.4988 0.4260 0.4808 -0.0424 0.0305  0.0296  932  PHE A C   
3011 O O   . PHE A 395 ? 0.5113 0.4541 0.5041 -0.0524 0.0259  0.0341  932  PHE A O   
3012 C CB  . PHE A 395 ? 0.5400 0.4218 0.5182 -0.0414 0.0453  0.0265  932  PHE A CB  
3013 C CG  . PHE A 395 ? 0.5862 0.4721 0.5776 -0.0533 0.0468  0.0309  932  PHE A CG  
3014 C CD1 . PHE A 395 ? 0.6194 0.4854 0.5951 -0.0618 0.0437  0.0237  932  PHE A CD1 
3015 C CD2 . PHE A 395 ? 0.5962 0.5059 0.6184 -0.0560 0.0511  0.0428  932  PHE A CD2 
3016 C CE1 . PHE A 395 ? 0.6398 0.5111 0.6301 -0.0738 0.0449  0.0287  932  PHE A CE1 
3017 C CE2 . PHE A 395 ? 0.6155 0.5315 0.6532 -0.0668 0.0528  0.0474  932  PHE A CE2 
3018 C CZ  . PHE A 395 ? 0.6346 0.5322 0.6564 -0.0763 0.0498  0.0406  932  PHE A CZ  
3019 N N   . GLY A 396 ? 0.4793 0.4213 0.4657 -0.0337 0.0308  0.0342  933  GLY A N   
3020 C CA  . GLY A 396 ? 0.4546 0.4316 0.4606 -0.0355 0.0266  0.0471  933  GLY A CA  
3021 C C   . GLY A 396 ? 0.4630 0.4583 0.4569 -0.0427 0.0165  0.0442  933  GLY A C   
3022 O O   . GLY A 396 ? 0.4781 0.5023 0.4884 -0.0484 0.0111  0.0561  933  GLY A O   
3023 N N   . ILE A 397 ? 0.4681 0.4470 0.4333 -0.0424 0.0133  0.0283  934  ILE A N   
3024 C CA  . ILE A 397 ? 0.4855 0.4811 0.4358 -0.0489 0.0040  0.0227  934  ILE A CA  
3025 C C   . ILE A 397 ? 0.5052 0.5031 0.4615 -0.0628 -0.0027 0.0233  934  ILE A C   
3026 O O   . ILE A 397 ? 0.5157 0.5377 0.4708 -0.0709 -0.0119 0.0261  934  ILE A O   
3027 C CB  . ILE A 397 ? 0.5003 0.4772 0.4199 -0.0429 0.0034  0.0036  934  ILE A CB  
3028 C CG1 . ILE A 397 ? 0.5112 0.5044 0.4123 -0.0497 -0.0056 -0.0049 934  ILE A CG1 
3029 C CG2 . ILE A 397 ? 0.5152 0.4529 0.4245 -0.0427 0.0059  -0.0083 934  ILE A CG2 
3030 C CD1 . ILE A 397 ? 0.5174 0.5128 0.3958 -0.0404 -0.0040 -0.0173 934  ILE A CD1 
3031 N N   . TYR A 398 ? 0.5082 0.4826 0.4711 -0.0665 0.0015  0.0216  935  TYR A N   
3032 C CA  . TYR A 398 ? 0.5187 0.4974 0.4925 -0.0805 -0.0042 0.0242  935  TYR A CA  
3033 C C   . TYR A 398 ? 0.5161 0.5266 0.5241 -0.0843 -0.0046 0.0437  935  TYR A C   
3034 O O   . TYR A 398 ? 0.5368 0.5704 0.5536 -0.0948 -0.0146 0.0493  935  TYR A O   
3035 C CB  . TYR A 398 ? 0.5249 0.4710 0.4971 -0.0838 0.0017  0.0186  935  TYR A CB  
3036 C CG  . TYR A 398 ? 0.5423 0.4546 0.4842 -0.0800 0.0011  0.0010  935  TYR A CG  
3037 C CD1 . TYR A 398 ? 0.5640 0.4710 0.4854 -0.0855 -0.0089 -0.0129 935  TYR A CD1 
3038 C CD2 . TYR A 398 ? 0.5325 0.4178 0.4669 -0.0708 0.0099  -0.0019 935  TYR A CD2 
3039 C CE1 . TYR A 398 ? 0.5810 0.4559 0.4780 -0.0809 -0.0095 -0.0292 935  TYR A CE1 
3040 C CE2 . TYR A 398 ? 0.5523 0.4069 0.4622 -0.0667 0.0083  -0.0163 935  TYR A CE2 
3041 C CZ  . TYR A 398 ? 0.5800 0.4291 0.4727 -0.0713 -0.0011 -0.0299 935  TYR A CZ  
3042 O OH  . TYR A 398 ? 0.6130 0.4304 0.4844 -0.0661 -0.0027 -0.0446 935  TYR A OH  
3043 N N   . LEU A 399 ? 0.4999 0.5117 0.5284 -0.0759 0.0054  0.0539  936  LEU A N   
3044 C CA  . LEU A 399 ? 0.4889 0.5288 0.5539 -0.0776 0.0059  0.0723  936  LEU A CA  
3045 C C   . LEU A 399 ? 0.4692 0.5429 0.5383 -0.0789 -0.0046 0.0824  936  LEU A C   
3046 O O   . LEU A 399 ? 0.4671 0.5677 0.5607 -0.0862 -0.0115 0.0960  936  LEU A O   
3047 C CB  . LEU A 399 ? 0.4888 0.5204 0.5713 -0.0666 0.0188  0.0783  936  LEU A CB  
3048 C CG  . LEU A 399 ? 0.4975 0.4993 0.5775 -0.0658 0.0302  0.0710  936  LEU A CG  
3049 C CD1 . LEU A 399 ? 0.4875 0.4787 0.5740 -0.0539 0.0411  0.0727  936  LEU A CD1 
3050 C CD2 . LEU A 399 ? 0.5096 0.5212 0.6165 -0.0753 0.0326  0.0786  936  LEU A CD2 
3051 N N   . THR A 400 ? 0.4504 0.5247 0.4962 -0.0720 -0.0060 0.0769  937  THR A N   
3052 C CA  . THR A 400 ? 0.4329 0.5402 0.4786 -0.0738 -0.0151 0.0871  937  THR A CA  
3053 C C   . THR A 400 ? 0.4462 0.5662 0.4752 -0.0865 -0.0282 0.0815  937  THR A C   
3054 O O   . THR A 400 ? 0.4414 0.5927 0.4841 -0.0939 -0.0382 0.0957  937  THR A O   
3055 C CB  . THR A 400 ? 0.4352 0.5406 0.4603 -0.0634 -0.0114 0.0822  937  THR A CB  
3056 O OG1 . THR A 400 ? 0.4174 0.5123 0.4602 -0.0528 -0.0010 0.0883  937  THR A OG1 
3057 C CG2 . THR A 400 ? 0.4361 0.5772 0.4584 -0.0660 -0.0199 0.0938  937  THR A CG2 
3058 N N   . ASN A 401 ? 0.4724 0.5677 0.4723 -0.0896 -0.0294 0.0611  938  ASN A N   
3059 C CA  . ASN A 401 ? 0.5108 0.6144 0.4919 -0.1020 -0.0424 0.0524  938  ASN A CA  
3060 C C   . ASN A 401 ? 0.5210 0.6350 0.5278 -0.1153 -0.0498 0.0617  938  ASN A C   
3061 O O   . ASN A 401 ? 0.5486 0.6848 0.5522 -0.1269 -0.0636 0.0643  938  ASN A O   
3062 C CB  . ASN A 401 ? 0.5497 0.6201 0.4967 -0.1012 -0.0414 0.0273  938  ASN A CB  
3063 C CG  . ASN A 401 ? 0.5599 0.6255 0.4807 -0.0889 -0.0360 0.0166  938  ASN A CG  
3064 O OD1 . ASN A 401 ? 0.5423 0.6232 0.4720 -0.0798 -0.0303 0.0280  938  ASN A OD1 
3065 N ND2 . ASN A 401 ? 0.5859 0.6299 0.4764 -0.0886 -0.0378 -0.0056 938  ASN A ND2 
3066 N N   . ILE A 402 ? 0.5014 0.6012 0.5337 -0.1141 -0.0409 0.0670  939  ILE A N   
3067 C CA  . ILE A 402 ? 0.4967 0.6091 0.5588 -0.1260 -0.0460 0.0774  939  ILE A CA  
3068 C C   . ILE A 402 ? 0.4974 0.6493 0.5924 -0.1270 -0.0518 0.1003  939  ILE A C   
3069 O O   . ILE A 402 ? 0.5017 0.6771 0.6121 -0.1392 -0.0644 0.1090  939  ILE A O   
3070 C CB  . ILE A 402 ? 0.4588 0.5462 0.5379 -0.1238 -0.0324 0.0763  939  ILE A CB  
3071 C CG1 . ILE A 402 ? 0.4630 0.5176 0.5164 -0.1306 -0.0333 0.0576  939  ILE A CG1 
3072 C CG2 . ILE A 402 ? 0.4476 0.5569 0.5707 -0.1302 -0.0320 0.0936  939  ILE A CG2 
3073 C CD1 . ILE A 402 ? 0.4550 0.4781 0.5099 -0.1251 -0.0184 0.0536  939  ILE A CD1 
3074 N N   . LEU A 403 ? 0.5047 0.6644 0.6120 -0.1146 -0.0440 0.1113  940  LEU A N   
3075 C CA  . LEU A 403 ? 0.5264 0.7217 0.6670 -0.1147 -0.0500 0.1346  940  LEU A CA  
3076 C C   . LEU A 403 ? 0.5796 0.8041 0.7039 -0.1235 -0.0672 0.1399  940  LEU A C   
3077 O O   . LEU A 403 ? 0.5840 0.8399 0.7352 -0.1303 -0.0782 0.1586  940  LEU A O   
3078 C CB  . LEU A 403 ? 0.5087 0.7029 0.6628 -0.1000 -0.0390 0.1437  940  LEU A CB  
3079 C CG  . LEU A 403 ? 0.5046 0.6806 0.6869 -0.0920 -0.0236 0.1452  940  LEU A CG  
3080 C CD1 . LEU A 403 ? 0.4969 0.6696 0.6881 -0.0784 -0.0147 0.1516  940  LEU A CD1 
3081 C CD2 . LEU A 403 ? 0.5031 0.6994 0.7299 -0.0979 -0.0259 0.1604  940  LEU A CD2 
3082 N N   . LYS A 404 ? 0.6272 0.8429 0.7079 -0.1233 -0.0699 0.1237  941  LYS A N   
3083 C CA  . LYS A 404 ? 0.6750 0.9181 0.7342 -0.1323 -0.0854 0.1262  941  LYS A CA  
3084 C C   . LYS A 404 ? 0.7043 0.9539 0.7615 -0.1489 -0.1001 0.1214  941  LYS A C   
3085 O O   . LYS A 404 ? 0.7162 0.9983 0.7790 -0.1590 -0.1156 0.1346  941  LYS A O   
3086 C CB  . LYS A 404 ? 0.7129 0.9443 0.7262 -0.1266 -0.0819 0.1078  941  LYS A CB  
3087 C CG  . LYS A 404 ? 0.7130 0.9418 0.7289 -0.1115 -0.0691 0.1138  941  LYS A CG  
3088 C CD  . LYS A 404 ? 0.7440 0.9665 0.7175 -0.1062 -0.0658 0.0965  941  LYS A CD  
3089 C CE  . LYS A 404 ? 0.7372 0.9628 0.7165 -0.0928 -0.0548 0.1053  941  LYS A CE  
3090 N NZ  . LYS A 404 ? 0.7608 0.9834 0.7021 -0.0871 -0.0503 0.0891  941  LYS A NZ  
3091 N N   . THR A 405 ? 0.7255 0.9447 0.7751 -0.1528 -0.0963 0.1034  942  THR A N   
3092 C CA  . THR A 405 ? 0.7579 0.9814 0.8115 -0.1696 -0.1100 0.0997  942  THR A CA  
3093 C C   . THR A 405 ? 0.7586 1.0093 0.8625 -0.1755 -0.1151 0.1238  942  THR A C   
3094 O O   . THR A 405 ? 0.7858 1.0600 0.8984 -0.1900 -0.1322 0.1306  942  THR A O   
3095 C CB  . THR A 405 ? 0.7617 0.9452 0.8028 -0.1719 -0.1032 0.0786  942  THR A CB  
3096 O OG1 . THR A 405 ? 0.7603 0.9159 0.7639 -0.1613 -0.0943 0.0591  942  THR A OG1 
3097 C CG2 . THR A 405 ? 0.7901 0.9742 0.8220 -0.1905 -0.1198 0.0688  942  THR A CG2 
3098 N N   . GLU A 406 ? 0.7390 0.9872 0.8775 -0.1643 -0.1008 0.1365  943  GLU A N   
3099 C CA  . GLU A 406 ? 0.7435 1.0171 0.9342 -0.1673 -0.1032 0.1589  943  GLU A CA  
3100 C C   . GLU A 406 ? 0.7389 1.0538 0.9434 -0.1708 -0.1190 0.1806  943  GLU A C   
3101 O O   . GLU A 406 ? 0.7538 1.0957 0.9861 -0.1822 -0.1330 0.1945  943  GLU A O   
3102 C CB  . GLU A 406 ? 0.7436 1.0038 0.9642 -0.1527 -0.0831 0.1652  943  GLU A CB  
3103 C CG  . GLU A 406 ? 0.7764 1.0035 0.9956 -0.1528 -0.0692 0.1503  943  GLU A CG  
3104 C CD  . GLU A 406 ? 0.8206 1.0577 1.0659 -0.1674 -0.0759 0.1540  943  GLU A CD  
3105 O OE1 . GLU A 406 ? 0.8330 1.1044 1.1160 -0.1726 -0.0855 0.1732  943  GLU A OE1 
3106 O OE2 . GLU A 406 ? 0.8424 1.0539 1.0725 -0.1741 -0.0722 0.1390  943  GLU A OE2 
3107 N N   . GLU A 407 ? 0.7167 1.0381 0.9030 -0.1617 -0.1174 0.1850  944  GLU A N   
3108 C CA  . GLU A 407 ? 0.7012 1.0616 0.8989 -0.1648 -0.1319 0.2079  944  GLU A CA  
3109 C C   . GLU A 407 ? 0.6748 1.0525 0.8342 -0.1793 -0.1514 0.2019  944  GLU A C   
3110 O O   . GLU A 407 ? 0.6744 1.0879 0.8453 -0.1869 -0.1680 0.2222  944  GLU A O   
3111 C CB  . GLU A 407 ? 0.7231 1.0846 0.9178 -0.1504 -0.1223 0.2169  944  GLU A CB  
3112 C CG  . GLU A 407 ? 0.7291 1.0705 0.9564 -0.1357 -0.1030 0.2197  944  GLU A CG  
3113 C CD  . GLU A 407 ? 0.7395 1.1057 1.0141 -0.1294 -0.1045 0.2481  944  GLU A CD  
3114 O OE1 . GLU A 407 ? 0.7507 1.1501 1.0308 -0.1360 -0.1208 0.2675  944  GLU A OE1 
3115 O OE2 . GLU A 407 ? 0.7324 1.0842 1.0382 -0.1180 -0.0899 0.2511  944  GLU A OE2 
3116 N N   . GLY A 408 ? 0.6541 1.0068 0.7684 -0.1832 -0.1502 0.1745  945  GLY A N   
3117 C CA  . GLY A 408 ? 0.6566 1.0207 0.7291 -0.1962 -0.1668 0.1634  945  GLY A CA  
3118 C C   . GLY A 408 ? 0.6532 1.0225 0.7310 -0.2143 -0.1835 0.1584  945  GLY A C   
3119 O O   . GLY A 408 ? 0.6838 1.0655 0.7285 -0.2269 -0.2001 0.1500  945  GLY A O   
3120 N N   . ASN A 409 ? 0.7485 0.9025 0.7633 -0.1347 0.2232  0.2458  946  ASN A N   
3121 C CA  . ASN A 409 ? 0.7129 0.8454 0.6871 -0.1095 0.2011  0.2299  946  ASN A CA  
3122 C C   . ASN A 409 ? 0.6788 0.7537 0.6504 -0.1106 0.1767  0.2446  946  ASN A C   
3123 O O   . ASN A 409 ? 0.6244 0.6736 0.6393 -0.1215 0.1678  0.2434  946  ASN A O   
3124 C CB  . ASN A 409 ? 0.6775 0.8227 0.6699 -0.0914 0.1888  0.1872  946  ASN A CB  
3125 C CG  . ASN A 409 ? 0.6873 0.8878 0.6747 -0.0810 0.2082  0.1673  946  ASN A CG  
3126 O OD1 . ASN A 409 ? 0.7035 0.9137 0.6489 -0.0609 0.2051  0.1511  946  ASN A OD1 
3127 N ND2 . ASN A 409 ? 0.6814 0.9201 0.7142 -0.0940 0.2277  0.1661  946  ASN A ND2 
3128 N N   . ASN A 410 ? 0.7173 0.7738 0.6392 -0.0984 0.1654  0.2568  947  ASN A N   
3129 C CA  . ASN A 410 ? 0.7261 0.7335 0.6466 -0.0945 0.1404  0.2679  947  ASN A CA  
3130 C C   . ASN A 410 ? 0.6653 0.6612 0.6046 -0.0805 0.1182  0.2322  947  ASN A C   
3131 O O   . ASN A 410 ? 0.6346 0.6534 0.5633 -0.0689 0.1169  0.2035  947  ASN A O   
3132 C CB  . ASN A 410 ? 0.7853 0.7811 0.6470 -0.0846 0.1328  0.2917  947  ASN A CB  
3133 C CG  . ASN A 410 ? 0.8090 0.7542 0.6735 -0.0860 0.1129  0.3179  947  ASN A CG  
3134 O OD1 . ASN A 410 ? 0.7938 0.7185 0.6573 -0.0695 0.0874  0.3064  947  ASN A OD1 
3135 N ND2 . ASN A 410 ? 0.8410 0.7644 0.7099 -0.1044 0.1220  0.3439  947  ASN A ND2 
3136 N N   . ASP A 411 ? 0.6520 0.6106 0.6184 -0.0827 0.1007  0.2334  948  ASP A N   
3137 C CA  . ASP A 411 ? 0.6136 0.5621 0.5962 -0.0735 0.0816  0.2005  948  ASP A CA  
3138 C C   . ASP A 411 ? 0.6223 0.5747 0.5647 -0.0548 0.0655  0.1896  948  ASP A C   
3139 O O   . ASP A 411 ? 0.5865 0.5433 0.5293 -0.0487 0.0548  0.1588  948  ASP A O   
3140 C CB  . ASP A 411 ? 0.6155 0.5274 0.6372 -0.0804 0.0694  0.2022  948  ASP A CB  
3141 C CG  . ASP A 411 ? 0.6083 0.5155 0.6739 -0.0999 0.0809  0.2019  948  ASP A CG  
3142 O OD1 . ASP A 411 ? 0.5792 0.5142 0.6533 -0.1052 0.0926  0.1879  948  ASP A OD1 
3143 O OD2 . ASP A 411 ? 0.6275 0.5028 0.7200 -0.1090 0.0766  0.2143  948  ASP A OD2 
3144 N N   . PHE A 412 ? 0.6686 0.6181 0.5738 -0.0473 0.0625  0.2147  949  PHE A N   
3145 C CA  . PHE A 412 ? 0.6922 0.6452 0.5604 -0.0302 0.0440  0.2065  949  PHE A CA  
3146 C C   . PHE A 412 ? 0.7462 0.7223 0.5585 -0.0241 0.0540  0.2187  949  PHE A C   
3147 O O   . PHE A 412 ? 0.7789 0.7651 0.5791 -0.0337 0.0752  0.2414  949  PHE A O   
3148 C CB  . PHE A 412 ? 0.7220 0.6467 0.5957 -0.0226 0.0226  0.2230  949  PHE A CB  
3149 C CG  . PHE A 412 ? 0.6910 0.5963 0.6163 -0.0249 0.0112  0.2051  949  PHE A CG  
3150 C CD1 . PHE A 412 ? 0.6528 0.5676 0.5888 -0.0192 -0.0024 0.1709  949  PHE A CD1 
3151 C CD2 . PHE A 412 ? 0.7012 0.5781 0.6621 -0.0346 0.0145  0.2217  949  PHE A CD2 
3152 C CE1 . PHE A 412 ? 0.6218 0.5224 0.6027 -0.0230 -0.0103 0.1528  949  PHE A CE1 
3153 C CE2 . PHE A 412 ? 0.6732 0.5329 0.6794 -0.0361 0.0049  0.2023  949  PHE A CE2 
3154 C CZ  . PHE A 412 ? 0.6291 0.5029 0.6451 -0.0301 -0.0065 0.1674  949  PHE A CZ  
3155 N N   . LEU A 413 ? 0.7740 0.7598 0.5516 -0.0098 0.0389  0.2022  950  LEU A N   
3156 C CA  . LEU A 413 ? 0.8427 0.8450 0.5597 -0.0014 0.0415  0.2131  950  LEU A CA  
3157 C C   . LEU A 413 ? 0.9259 0.9095 0.6191 0.0083  0.0176  0.2343  950  LEU A C   
3158 O O   . LEU A 413 ? 0.9086 0.8797 0.6272 0.0153  -0.0056 0.2220  950  LEU A O   
3159 C CB  . LEU A 413 ? 0.7986 0.8225 0.4897 0.0082  0.0386  0.1778  950  LEU A CB  
3160 C CG  . LEU A 413 ? 0.7226 0.7567 0.4450 0.0030  0.0514  0.1495  950  LEU A CG  
3161 C CD1 . LEU A 413 ? 0.7019 0.7460 0.3951 0.0136  0.0428  0.1150  950  LEU A CD1 
3162 C CD2 . LEU A 413 ? 0.7299 0.7840 0.4596 -0.0054 0.0810  0.1637  950  LEU A CD2 
3163 N N   . LYS A 414 ? 1.0233 1.0063 0.6677 0.0086  0.0228  0.2658  951  LYS A N   
3164 C CA  . LYS A 414 ? 1.1066 1.0660 0.7268 0.0180  -0.0022 0.2922  951  LYS A CA  
3165 C C   . LYS A 414 ? 1.1320 1.1062 0.7119 0.0346  -0.0252 0.2745  951  LYS A C   
3166 O O   . LYS A 414 ? 1.1551 1.1530 0.6880 0.0364  -0.0151 0.2640  951  LYS A O   
3167 C CB  . LYS A 414 ? 1.2004 1.1464 0.7784 0.0082  0.0111  0.3370  951  LYS A CB  
3168 C CG  . LYS A 414 ? 1.2169 1.1475 0.8326 -0.0121 0.0336  0.3572  951  LYS A CG  
3169 C CD  . LYS A 414 ? 1.3143 1.2226 0.8880 -0.0257 0.0449  0.3911  951  LYS A CD  
3170 C CE  . LYS A 414 ? 1.3220 1.2087 0.9371 -0.0476 0.0631  0.4056  951  LYS A CE  
3171 N NZ  . LYS A 414 ? 1.4162 1.2795 0.9879 -0.0639 0.0768  0.4320  951  LYS A NZ  
3172 N N   . LYS A 415 ? 1.1273 1.0894 0.7270 0.0470  -0.0565 0.2696  952  LYS A N   
3173 C CA  . LYS A 415 ? 1.1353 1.1130 0.7042 0.0615  -0.0825 0.2526  952  LYS A CA  
3174 C C   . LYS A 415 ? 1.1852 1.1432 0.7469 0.0756  -0.1143 0.2779  952  LYS A C   
3175 O O   . LYS A 415 ? 1.2006 1.1287 0.7870 0.0753  -0.1176 0.3046  952  LYS A O   
3176 C CB  . LYS A 415 ? 1.0584 1.0530 0.6677 0.0621  -0.0911 0.2081  952  LYS A CB  
3177 C CG  . LYS A 415 ? 1.0062 1.0138 0.6216 0.0506  -0.0656 0.1819  952  LYS A CG  
3178 C CD  . LYS A 415 ? 1.0099 1.0377 0.5761 0.0550  -0.0689 0.1576  952  LYS A CD  
3179 C CE  . LYS A 415 ? 1.0253 1.0633 0.5555 0.0511  -0.0400 0.1606  952  LYS A CE  
3180 N NZ  . LYS A 415 ? 1.0122 1.0637 0.5190 0.0534  -0.0388 0.1235  952  LYS A NZ  
3181 N N   . LYS A 416 ? 1.2163 1.1896 0.7433 0.0888  -0.1402 0.2686  953  LYS A N   
3182 C CA  . LYS A 416 ? 1.2678 1.2272 0.7932 0.1061  -0.1769 0.2870  953  LYS A CA  
3183 C C   . LYS A 416 ? 1.2178 1.1732 0.8227 0.1134  -0.1926 0.2705  953  LYS A C   
3184 O O   . LYS A 416 ? 1.2485 1.1745 0.8763 0.1225  -0.2069 0.2948  953  LYS A O   
3185 C CB  . LYS A 416 ? 1.3079 1.2903 0.7897 0.1162  -0.2025 0.2719  953  LYS A CB  
3186 C CG  . LYS A 416 ? 1.3811 1.3530 0.7929 0.1034  -0.1922 0.2822  953  LYS A CG  
3187 C CD  . LYS A 416 ? 1.4109 1.4032 0.7996 0.1059  -0.2192 0.2623  953  LYS A CD  
3188 C CE  . LYS A 416 ? 1.4865 1.4689 0.8036 0.0931  -0.2093 0.2699  953  LYS A CE  
3189 N NZ  . LYS A 416 ? 1.5129 1.5164 0.8108 0.0934  -0.2352 0.2513  953  LYS A NZ  
3190 N N   . GLY A 417 ? 1.1419 1.1249 0.7874 0.1090  -0.1904 0.2283  954  GLY A N   
3191 C CA  . GLY A 417 ? 1.0884 1.0746 0.8079 0.1133  -0.2012 0.2076  954  GLY A CA  
3192 C C   . GLY A 417 ? 1.0317 1.0043 0.7952 0.0971  -0.1722 0.2000  954  GLY A C   
3193 O O   . GLY A 417 ? 1.0553 0.9980 0.8155 0.0913  -0.1564 0.2289  954  GLY A O   
3194 N N   . LYS A 418 ? 0.9548 0.9483 0.7572 0.0875  -0.1657 0.1617  955  LYS A N   
3195 C CA  . LYS A 418 ? 0.8902 0.8710 0.7322 0.0717  -0.1411 0.1520  955  LYS A CA  
3196 C C   . LYS A 418 ? 0.8704 0.8445 0.6760 0.0575  -0.1128 0.1622  955  LYS A C   
3197 O O   . LYS A 418 ? 0.8855 0.8764 0.6468 0.0557  -0.1091 0.1534  955  LYS A O   
3198 C CB  . LYS A 418 ? 0.8363 0.8402 0.7184 0.0625  -0.1418 0.1092  955  LYS A CB  
3199 C CG  . LYS A 418 ? 0.8022 0.7910 0.7300 0.0481  -0.1224 0.0983  955  LYS A CG  
3200 C CD  . LYS A 418 ? 0.8341 0.7983 0.8018 0.0583  -0.1281 0.1169  955  LYS A CD  
3201 C CE  . LYS A 418 ? 0.8171 0.7591 0.8182 0.0425  -0.1063 0.1138  955  LYS A CE  
3202 N NZ  . LYS A 418 ? 0.7750 0.7322 0.8166 0.0313  -0.1027 0.0750  955  LYS A NZ  
3203 N N   . ASP A 419 ? 0.8294 0.7804 0.6552 0.0482  -0.0937 0.1796  956  ASP A N   
3204 C CA  . ASP A 419 ? 0.7915 0.7426 0.5937 0.0348  -0.0659 0.1876  956  ASP A CA  
3205 C C   . ASP A 419 ? 0.7056 0.6692 0.5287 0.0226  -0.0535 0.1524  956  ASP A C   
3206 O O   . ASP A 419 ? 0.6573 0.6176 0.5241 0.0176  -0.0582 0.1310  956  ASP A O   
3211 N N   . LEU A 420 ? 0.6854 0.6623 0.4749 0.0182  -0.0382 0.1459  957  LEU A N   
3212 C CA  . LEU A 420 ? 0.6308 0.6147 0.4306 0.0091  -0.0306 0.1135  957  LEU A CA  
3213 C C   . LEU A 420 ? 0.5910 0.5655 0.4240 -0.0036 -0.0100 0.1171  957  LEU A C   
3214 O O   . LEU A 420 ? 0.6168 0.5879 0.4508 -0.0066 0.0049  0.1440  957  LEU A O   
3215 C CB  . LEU A 420 ? 0.6477 0.6481 0.3964 0.0140  -0.0274 0.1008  957  LEU A CB  
3216 C CG  . LEU A 420 ? 0.6704 0.6818 0.3784 0.0251  -0.0480 0.0956  957  LEU A CG  
3217 C CD1 . LEU A 420 ? 0.6803 0.7028 0.3416 0.0280  -0.0438 0.0755  957  LEU A CD1 
3218 C CD2 . LEU A 420 ? 0.6482 0.6603 0.3846 0.0236  -0.0704 0.0756  957  LEU A CD2 
3219 N N   . ILE A 421 ? 0.5323 0.5024 0.3911 -0.0130 -0.0102 0.0898  958  ILE A N   
3220 C CA  . ILE A 421 ? 0.5071 0.4704 0.3952 -0.0248 0.0059  0.0884  958  ILE A CA  
3221 C C   . ILE A 421 ? 0.5234 0.5034 0.3853 -0.0221 0.0215  0.0881  958  ILE A C   
3222 O O   . ILE A 421 ? 0.5313 0.5202 0.3596 -0.0150 0.0166  0.0691  958  ILE A O   
3223 C CB  . ILE A 421 ? 0.4536 0.4055 0.3673 -0.0358 -0.0014 0.0589  958  ILE A CB  
3224 C CG1 . ILE A 421 ? 0.4343 0.3771 0.3766 -0.0375 -0.0140 0.0556  958  ILE A CG1 
3225 C CG2 . ILE A 421 ? 0.4325 0.3768 0.3743 -0.0474 0.0117  0.0566  958  ILE A CG2 
3226 C CD1 . ILE A 421 ? 0.4110 0.3475 0.3684 -0.0501 -0.0211 0.0244  958  ILE A CD1 
3227 N N   . ASN A 422 ? 0.5254 0.5110 0.4038 -0.0279 0.0403  0.1075  959  ASN A N   
3228 C CA  . ASN A 422 ? 0.5184 0.5280 0.3820 -0.0252 0.0581  0.1047  959  ASN A CA  
3229 C C   . ASN A 422 ? 0.4854 0.4923 0.3755 -0.0300 0.0575  0.0780  959  ASN A C   
3230 O O   . ASN A 422 ? 0.4731 0.4760 0.4040 -0.0417 0.0645  0.0823  959  ASN A O   
3231 C CB  . ASN A 422 ? 0.5359 0.5579 0.4079 -0.0326 0.0796  0.1364  959  ASN A CB  
3232 C CG  . ASN A 422 ? 0.5125 0.5693 0.3762 -0.0304 0.1013  0.1309  959  ASN A CG  
3233 O OD1 . ASN A 422 ? 0.5014 0.5694 0.3530 -0.0198 0.0983  0.1026  959  ASN A OD1 
3234 N ND2 . ASN A 422 ? 0.5387 0.6126 0.4091 -0.0407 0.1231  0.1573  959  ASN A ND2 
3235 N N   . PHE A 423 ? 0.4774 0.4833 0.3421 -0.0215 0.0471  0.0504  960  PHE A N   
3236 C CA  . PHE A 423 ? 0.4451 0.4407 0.3277 -0.0251 0.0415  0.0256  960  PHE A CA  
3237 C C   . PHE A 423 ? 0.4404 0.4610 0.3278 -0.0168 0.0559  0.0192  960  PHE A C   
3238 O O   . PHE A 423 ? 0.4227 0.4388 0.3390 -0.0208 0.0537  0.0067  960  PHE A O   
3239 C CB  . PHE A 423 ? 0.4459 0.4202 0.2987 -0.0226 0.0207  -0.0015 960  PHE A CB  
3240 C CG  . PHE A 423 ? 0.4233 0.3758 0.2891 -0.0293 0.0106  -0.0240 960  PHE A CG  
3241 C CD1 . PHE A 423 ? 0.3936 0.3236 0.2854 -0.0465 0.0027  -0.0270 960  PHE A CD1 
3242 C CD2 . PHE A 423 ? 0.4299 0.3829 0.2800 -0.0177 0.0080  -0.0428 960  PHE A CD2 
3243 C CE1 . PHE A 423 ? 0.3812 0.2879 0.2779 -0.0544 -0.0081 -0.0456 960  PHE A CE1 
3244 C CE2 . PHE A 423 ? 0.4253 0.3527 0.2834 -0.0229 -0.0052 -0.0613 960  PHE A CE2 
3245 C CZ  . PHE A 423 ? 0.4116 0.3150 0.2906 -0.0426 -0.0135 -0.0615 960  PHE A CZ  
3246 N N   . SER A 424 ? 0.4692 0.5179 0.3288 -0.0048 0.0698  0.0258  961  SER A N   
3247 C CA  . SER A 424 ? 0.4896 0.5718 0.3603 0.0037  0.0873  0.0186  961  SER A CA  
3248 C C   . SER A 424 ? 0.4681 0.5661 0.3921 -0.0108 0.1025  0.0349  961  SER A C   
3249 O O   . SER A 424 ? 0.4296 0.5458 0.3843 -0.0079 0.1070  0.0206  961  SER A O   
3250 C CB  . SER A 424 ? 0.5351 0.6486 0.3658 0.0154  0.1041  0.0259  961  SER A CB  
3251 O OG  . SER A 424 ? 0.5656 0.6671 0.3484 0.0306  0.0894  0.0038  961  SER A OG  
3252 N N   . LYS A 425 ? 0.4491 0.5390 0.3860 -0.0262 0.1082  0.0640  962  LYS A N   
3253 C CA  . LYS A 425 ? 0.4357 0.5328 0.4228 -0.0437 0.1198  0.0796  962  LYS A CA  
3254 C C   . LYS A 425 ? 0.4111 0.4883 0.4344 -0.0492 0.1041  0.0590  962  LYS A C   
3255 O O   . LYS A 425 ? 0.4177 0.5155 0.4796 -0.0541 0.1113  0.0538  962  LYS A O   
3256 C CB  . LYS A 425 ? 0.4480 0.5244 0.4375 -0.0580 0.1219  0.1119  962  LYS A CB  
3257 C CG  . LYS A 425 ? 0.4267 0.4936 0.4676 -0.0783 0.1261  0.1242  962  LYS A CG  
3258 C CD  . LYS A 425 ? 0.4489 0.4888 0.4887 -0.0897 0.1260  0.1555  962  LYS A CD  
3259 C CE  . LYS A 425 ? 0.4726 0.5054 0.5606 -0.1118 0.1340  0.1697  962  LYS A CE  
3260 N NZ  . LYS A 425 ? 0.4818 0.4880 0.5659 -0.1234 0.1369  0.2044  962  LYS A NZ  
3261 N N   . ARG A 426 ? 0.3970 0.4361 0.4074 -0.0496 0.0821  0.0464  963  ARG A N   
3262 C CA  . ARG A 426 ? 0.3660 0.3818 0.4014 -0.0573 0.0665  0.0275  963  ARG A CA  
3263 C C   . ARG A 426 ? 0.3645 0.3915 0.3983 -0.0442 0.0603  0.0022  963  ARG A C   
3264 O O   . ARG A 426 ? 0.3414 0.3678 0.4082 -0.0496 0.0548  -0.0070 963  ARG A O   
3265 C CB  . ARG A 426 ? 0.3573 0.3343 0.3731 -0.0621 0.0469  0.0178  963  ARG A CB  
3266 C CG  . ARG A 426 ? 0.3623 0.3215 0.4005 -0.0767 0.0473  0.0343  963  ARG A CG  
3267 C CD  . ARG A 426 ? 0.3978 0.3667 0.4239 -0.0724 0.0573  0.0605  963  ARG A CD  
3268 N NE  . ARG A 426 ? 0.4007 0.3455 0.4444 -0.0814 0.0515  0.0710  963  ARG A NE  
3269 C CZ  . ARG A 426 ? 0.4218 0.3635 0.4566 -0.0772 0.0529  0.0928  963  ARG A CZ  
3270 N NH1 . ARG A 426 ? 0.4465 0.4071 0.4498 -0.0669 0.0606  0.1085  963  ARG A NH1 
3271 N NH2 . ARG A 426 ? 0.4212 0.3393 0.4768 -0.0823 0.0452  0.0980  963  ARG A NH2 
3272 N N   . ARG A 427 ? 0.4005 0.4358 0.3954 -0.0257 0.0589  -0.0104 964  ARG A N   
3273 C CA  . ARG A 427 ? 0.4083 0.4531 0.4011 -0.0087 0.0523  -0.0357 964  ARG A CA  
3274 C C   . ARG A 427 ? 0.4190 0.5114 0.4562 -0.0057 0.0710  -0.0324 964  ARG A C   
3275 O O   . ARG A 427 ? 0.4125 0.5086 0.4768 0.0001  0.0610  -0.0499 964  ARG A O   
3276 C CB  . ARG A 427 ? 0.4233 0.4701 0.3657 0.0111  0.0502  -0.0491 964  ARG A CB  
3277 C CG  . ARG A 427 ? 0.4421 0.4977 0.3813 0.0331  0.0434  -0.0770 964  ARG A CG  
3278 C CD  . ARG A 427 ? 0.4834 0.5337 0.3688 0.0519  0.0393  -0.0928 964  ARG A CD  
3279 N NE  . ARG A 427 ? 0.5007 0.5037 0.3455 0.0430  0.0188  -0.0960 964  ARG A NE  
3280 C CZ  . ARG A 427 ? 0.5141 0.5173 0.3305 0.0369  0.0232  -0.0820 964  ARG A CZ  
3281 N NH1 . ARG A 427 ? 0.5155 0.5570 0.3330 0.0386  0.0462  -0.0614 964  ARG A NH1 
3282 N NH2 . ARG A 427 ? 0.5241 0.4900 0.3102 0.0280  0.0037  -0.0885 964  ARG A NH2 
3283 N N   . LYS A 428 ? 0.4300 0.5596 0.4749 -0.0107 0.0973  -0.0097 965  LYS A N   
3284 C CA  . LYS A 428 ? 0.4209 0.6035 0.5093 -0.0121 0.1192  -0.0059 965  LYS A CA  
3285 C C   . LYS A 428 ? 0.3940 0.5725 0.5373 -0.0301 0.1133  -0.0025 965  LYS A C   
3286 O O   . LYS A 428 ? 0.3866 0.5966 0.5700 -0.0247 0.1140  -0.0171 965  LYS A O   
3287 C CB  . LYS A 428 ? 0.4434 0.6587 0.5224 -0.0214 0.1487  0.0225  965  LYS A CB  
3288 C CG  . LYS A 428 ? 0.4835 0.7186 0.5116 -0.0027 0.1594  0.0166  965  LYS A CG  
3289 C CD  . LYS A 428 ? 0.5203 0.7885 0.5368 -0.0154 0.1895  0.0469  965  LYS A CD  
3290 C CE  . LYS A 428 ? 0.5604 0.8585 0.5283 0.0032  0.2038  0.0373  965  LYS A CE  
3291 N NZ  . LYS A 428 ? 0.5980 0.9282 0.5486 -0.0122 0.2343  0.0684  965  LYS A NZ  
3292 N N   . VAL A 429 ? 0.3814 0.5227 0.5287 -0.0505 0.1064  0.0149  966  VAL A N   
3293 C CA  . VAL A 429 ? 0.3641 0.4952 0.5582 -0.0683 0.0982  0.0157  966  VAL A CA  
3294 C C   . VAL A 429 ? 0.3546 0.4608 0.5498 -0.0591 0.0706  -0.0128 966  VAL A C   
3295 O O   . VAL A 429 ? 0.3427 0.4604 0.5792 -0.0640 0.0634  -0.0214 966  VAL A O   
3296 C CB  . VAL A 429 ? 0.3673 0.4601 0.5611 -0.0895 0.0962  0.0370  966  VAL A CB  
3297 C CG1 . VAL A 429 ? 0.3470 0.4323 0.5891 -0.1097 0.0908  0.0382  966  VAL A CG1 
3298 C CG2 . VAL A 429 ? 0.3972 0.5040 0.5785 -0.0959 0.1186  0.0668  966  VAL A CG2 
3299 N N   . ALA A 430 ? 0.3604 0.4305 0.5085 -0.0471 0.0530  -0.0272 967  ALA A N   
3300 C CA  . ALA A 430 ? 0.3540 0.3924 0.4938 -0.0403 0.0250  -0.0521 967  ALA A CA  
3301 C C   . ALA A 430 ? 0.3797 0.4517 0.5394 -0.0182 0.0218  -0.0716 967  ALA A C   
3302 O O   . ALA A 430 ? 0.3693 0.4266 0.5454 -0.0156 0.0000  -0.0873 967  ALA A O   
3303 C CB  . ALA A 430 ? 0.3404 0.3336 0.4227 -0.0354 0.0086  -0.0624 967  ALA A CB  
3304 N N   . GLU A 431 ? 0.4193 0.5370 0.5772 -0.0014 0.0426  -0.0720 968  GLU A N   
3305 C CA  . GLU A 431 ? 0.4482 0.6084 0.6331 0.0219  0.0434  -0.0931 968  GLU A CA  
3306 C C   . GLU A 431 ? 0.4062 0.6020 0.6581 0.0110  0.0461  -0.0910 968  GLU A C   
3307 O O   . GLU A 431 ? 0.4081 0.6125 0.6867 0.0262  0.0274  -0.1127 968  GLU A O   
3308 C CB  . GLU A 431 ? 0.5078 0.7193 0.6819 0.0370  0.0722  -0.0921 968  GLU A CB  
3309 C CG  . GLU A 431 ? 0.5714 0.7540 0.6790 0.0467  0.0712  -0.0932 968  GLU A CG  
3310 C CD  . GLU A 431 ? 0.6354 0.7896 0.7095 0.0741  0.0469  -0.1249 968  GLU A CD  
3311 O OE1 . GLU A 431 ? 0.6778 0.8664 0.7434 0.0985  0.0578  -0.1420 968  GLU A OE1 
3312 O OE2 . GLU A 431 ? 0.6390 0.7346 0.6928 0.0703  0.0170  -0.1333 968  GLU A OE2 
3313 N N   . ILE A 432 ? 0.3767 0.5911 0.6563 -0.0153 0.0668  -0.0652 969  ILE A N   
3314 C CA  . ILE A 432 ? 0.3491 0.5997 0.6938 -0.0300 0.0709  -0.0621 969  ILE A CA  
3315 C C   . ILE A 432 ? 0.3399 0.5425 0.6939 -0.0409 0.0390  -0.0694 969  ILE A C   
3316 O O   . ILE A 432 ? 0.3411 0.5650 0.7400 -0.0387 0.0257  -0.0825 969  ILE A O   
3317 C CB  . ILE A 432 ? 0.3297 0.6067 0.6951 -0.0575 0.1019  -0.0310 969  ILE A CB  
3318 C CG1 . ILE A 432 ? 0.3429 0.6565 0.6819 -0.0488 0.1319  -0.0210 969  ILE A CG1 
3319 C CG2 . ILE A 432 ? 0.3098 0.6354 0.7459 -0.0735 0.1097  -0.0295 969  ILE A CG2 
3320 C CD1 . ILE A 432 ? 0.3459 0.6695 0.6874 -0.0765 0.1593  0.0140  969  ILE A CD1 
3321 N N   . THR A 433 ? 0.3442 0.4839 0.6560 -0.0530 0.0260  -0.0622 970  THR A N   
3322 C CA  . THR A 433 ? 0.3331 0.4263 0.6466 -0.0661 -0.0022 -0.0695 970  THR A CA  
3323 C C   . THR A 433 ? 0.3390 0.4110 0.6369 -0.0446 -0.0335 -0.0958 970  THR A C   
3324 O O   . THR A 433 ? 0.3412 0.3904 0.6523 -0.0520 -0.0582 -0.1044 970  THR A O   
3325 C CB  . THR A 433 ? 0.3417 0.3784 0.6133 -0.0834 -0.0062 -0.0591 970  THR A CB  
3326 O OG1 . THR A 433 ? 0.3695 0.3846 0.5869 -0.0680 -0.0084 -0.0647 970  THR A OG1 
3327 C CG2 . THR A 433 ? 0.3323 0.3809 0.6240 -0.1046 0.0185  -0.0333 970  THR A CG2 
3328 N N   . GLY A 434 ? 0.3556 0.4297 0.6218 -0.0181 -0.0351 -0.1088 971  GLY A N   
3329 C CA  . GLY A 434 ? 0.3917 0.4457 0.6460 0.0059  -0.0658 -0.1341 971  GLY A CA  
3330 C C   . GLY A 434 ? 0.4113 0.5193 0.7286 0.0207  -0.0704 -0.1473 971  GLY A C   
3331 O O   . GLY A 434 ? 0.4212 0.5068 0.7415 0.0343  -0.1035 -0.1654 971  GLY A O   
3332 N N   . GLU A 435 ? 0.4116 0.5917 0.7800 0.0174  -0.0385 -0.1384 972  GLU A N   
3333 C CA  . GLU A 435 ? 0.4370 0.6800 0.8744 0.0284  -0.0401 -0.1519 972  GLU A CA  
3334 C C   . GLU A 435 ? 0.4089 0.6394 0.8824 0.0060  -0.0605 -0.1482 972  GLU A C   
3335 O O   . GLU A 435 ? 0.4080 0.6683 0.9283 0.0188  -0.0800 -0.1654 972  GLU A O   
3336 C CB  . GLU A 435 ? 0.4774 0.8025 0.9571 0.0241  0.0030  -0.1417 972  GLU A CB  
3337 C CG  . GLU A 435 ? 0.5369 0.8796 0.9790 0.0445  0.0259  -0.1450 972  GLU A CG  
3338 C CD  . GLU A 435 ? 0.5779 1.0028 1.0578 0.0369  0.0694  -0.1343 972  GLU A CD  
3339 O OE1 . GLU A 435 ? 0.5880 1.0172 1.0738 0.0044  0.0917  -0.1052 972  GLU A OE1 
3340 O OE2 . GLU A 435 ? 0.5990 1.0837 1.1021 0.0629  0.0813  -0.1556 972  GLU A OE2 
3341 N N   . ILE A 436 ? 0.3898 0.5782 0.8435 -0.0263 -0.0574 -0.1277 973  ILE A N   
3342 C CA  . ILE A 436 ? 0.3830 0.5551 0.8650 -0.0499 -0.0762 -0.1250 973  ILE A CA  
3343 C C   . ILE A 436 ? 0.4200 0.5302 0.8666 -0.0406 -0.1205 -0.1420 973  ILE A C   
3344 O O   . ILE A 436 ? 0.4189 0.5326 0.8977 -0.0428 -0.1462 -0.1517 973  ILE A O   
3345 C CB  . ILE A 436 ? 0.3486 0.4933 0.8187 -0.0850 -0.0580 -0.1005 973  ILE A CB  
3346 C CG1 . ILE A 436 ? 0.3267 0.5314 0.8379 -0.0979 -0.0185 -0.0814 973  ILE A CG1 
3347 C CG2 . ILE A 436 ? 0.3426 0.4492 0.8105 -0.1053 -0.0792 -0.0986 973  ILE A CG2 
3348 C CD1 . ILE A 436 ? 0.3142 0.4895 0.8158 -0.1295 -0.0026 -0.0566 973  ILE A CD1 
3349 N N   . GLN A 437 ? 0.4587 0.5111 0.8369 -0.0311 -0.1314 -0.1456 974  GLN A N   
3350 C CA  . GLN A 437 ? 0.5028 0.4845 0.8342 -0.0300 -0.1718 -0.1570 974  GLN A CA  
3351 C C   . GLN A 437 ? 0.5294 0.5170 0.8747 0.0025  -0.2044 -0.1795 974  GLN A C   
3352 O O   . GLN A 437 ? 0.5614 0.5009 0.8731 0.0048  -0.2325 -0.1784 974  GLN A O   
3353 C CB  . GLN A 437 ? 0.5316 0.4557 0.7802 -0.0305 -0.1666 -0.1486 974  GLN A CB  
3354 C CG  . GLN A 437 ? 0.5274 0.4443 0.7492 -0.0565 -0.1344 -0.1225 974  GLN A CG  
3355 C CD  . GLN A 437 ? 0.5507 0.4259 0.6892 -0.0581 -0.1249 -0.1098 974  GLN A CD  
3356 O OE1 . GLN A 437 ? 0.5583 0.4277 0.6810 -0.0491 -0.1227 -0.1171 974  GLN A OE1 
3357 N NE2 . GLN A 437 ? 0.5473 0.4034 0.6392 -0.0703 -0.1151 -0.0950 974  GLN A NE2 
3358 N N   . GLN A 438 ? 0.5238 0.5714 0.9053 0.0327  -0.1912 -0.1910 975  GLN A N   
3359 C CA  . GLN A 438 ? 0.5490 0.6015 0.9443 0.0696  -0.2233 -0.2159 975  GLN A CA  
3360 C C   . GLN A 438 ? 0.5346 0.6167 0.9909 0.0695  -0.2482 -0.2241 975  GLN A C   
3361 O O   . GLN A 438 ? 0.5462 0.6208 1.0116 0.0995  -0.2845 -0.2448 975  GLN A O   
3362 C CB  . GLN A 438 ? 0.5657 0.6827 0.9880 0.1025  -0.1988 -0.2294 975  GLN A CB  
3363 C CG  . GLN A 438 ? 0.5510 0.7709 1.0594 0.1012  -0.1673 -0.2290 975  GLN A CG  
3364 C CD  . GLN A 438 ? 0.5652 0.8483 1.0896 0.1289  -0.1364 -0.2411 975  GLN A CD  
3365 O OE1 . GLN A 438 ? 0.5644 0.8303 1.0398 0.1274  -0.1136 -0.2325 975  GLN A OE1 
3366 N NE2 . GLN A 438 ? 0.5743 0.9338 1.1680 0.1546  -0.1359 -0.2630 975  GLN A NE2 
3367 N N   . TYR A 439 ? 0.5184 0.6305 1.0156 0.0371  -0.2325 -0.2092 976  TYR A N   
3368 C CA  . TYR A 439 ? 0.5342 0.6799 1.0931 0.0327  -0.2548 -0.2166 976  TYR A CA  
3369 C C   . TYR A 439 ? 0.5680 0.6357 1.0665 0.0069  -0.2659 -0.1970 976  TYR A C   
3370 O O   . TYR A 439 ? 0.5789 0.6577 1.1025 0.0034  -0.2777 -0.1965 976  TYR A O   
3371 C CB  . TYR A 439 ? 0.4953 0.7346 1.1350 0.0175  -0.2163 -0.2091 976  TYR A CB  
3372 C CG  . TYR A 439 ? 0.4897 0.8091 1.1705 0.0447  -0.1857 -0.2194 976  TYR A CG  
3373 C CD1 . TYR A 439 ? 0.5117 0.8765 1.2343 0.0834  -0.2042 -0.2463 976  TYR A CD1 
3374 C CD2 . TYR A 439 ? 0.4657 0.8146 1.1402 0.0316  -0.1376 -0.2024 976  TYR A CD2 
3375 C CE1 . TYR A 439 ? 0.5137 0.9530 1.2692 0.1073  -0.1726 -0.2578 976  TYR A CE1 
3376 C CE2 . TYR A 439 ? 0.4701 0.8934 1.1767 0.0539  -0.1077 -0.2122 976  TYR A CE2 
3377 C CZ  . TYR A 439 ? 0.4879 0.9612 1.2399 0.0920  -0.1246 -0.2421 976  TYR A CZ  
3378 O OH  . TYR A 439 ? 0.4932 1.0406 1.2717 0.1135  -0.0918 -0.2536 976  TYR A OH  
3379 N N   . GLN A 440 ? 0.5584 0.6534 0.8417 -0.0352 -0.1609 -0.1846 977  GLN A N   
3380 C CA  . GLN A 440 ? 0.5379 0.6462 0.8388 -0.0444 -0.1452 -0.1677 977  GLN A CA  
3381 C C   . GLN A 440 ? 0.5577 0.6552 0.8840 -0.0593 -0.1295 -0.1553 977  GLN A C   
3382 O O   . GLN A 440 ? 0.5546 0.6587 0.8899 -0.0667 -0.1137 -0.1399 977  GLN A O   
3383 C CB  . GLN A 440 ? 0.5132 0.6440 0.8458 -0.0469 -0.1549 -0.1766 977  GLN A CB  
3384 C CG  . GLN A 440 ? 0.4911 0.6345 0.7953 -0.0321 -0.1660 -0.1819 977  GLN A CG  
3385 C CD  . GLN A 440 ? 0.4875 0.6533 0.8276 -0.0338 -0.1778 -0.1913 977  GLN A CD  
3386 O OE1 . GLN A 440 ? 0.5007 0.6706 0.8831 -0.0419 -0.1893 -0.2046 977  GLN A OE1 
3387 N NE2 . GLN A 440 ? 0.4702 0.6506 0.7966 -0.0264 -0.1752 -0.1846 977  GLN A NE2 
3388 N N   . ASN A 441 ? 0.5874 0.6663 0.9233 -0.0632 -0.1325 -0.1611 978  ASN A N   
3389 C CA  . ASN A 441 ? 0.6129 0.6781 0.9725 -0.0769 -0.1182 -0.1492 978  ASN A CA  
3390 C C   . ASN A 441 ? 0.6151 0.6589 0.9447 -0.0729 -0.1096 -0.1370 978  ASN A C   
3391 O O   . ASN A 441 ? 0.6363 0.6609 0.9790 -0.0787 -0.1074 -0.1363 978  ASN A O   
3392 C CB  . ASN A 441 ? 0.6499 0.7096 1.0536 -0.0868 -0.1277 -0.1645 978  ASN A CB  
3393 C CG  . ASN A 441 ? 0.6582 0.7407 1.1004 -0.0919 -0.1371 -0.1767 978  ASN A CG  
3394 O OD1 . ASN A 441 ? 0.6418 0.7422 1.0896 -0.0936 -0.1283 -0.1674 978  ASN A OD1 
3395 N ND2 . ASN A 441 ? 0.6737 0.7554 1.1442 -0.0941 -0.1559 -0.1982 978  ASN A ND2 
3396 N N   . GLN A 442 ? 0.5909 0.6377 0.8824 -0.0629 -0.1048 -0.1270 979  GLN A N   
3397 C CA  . GLN A 442 ? 0.5747 0.6046 0.8386 -0.0566 -0.0995 -0.1175 979  GLN A CA  
3398 C C   . GLN A 442 ? 0.4981 0.5304 0.7423 -0.0575 -0.0854 -0.0962 979  GLN A C   
3399 O O   . GLN A 442 ? 0.4875 0.5293 0.7048 -0.0484 -0.0850 -0.0931 979  GLN A O   
3400 C CB  . GLN A 442 ? 0.6243 0.6536 0.8603 -0.0415 -0.1098 -0.1298 979  GLN A CB  
3401 C CG  . GLN A 442 ? 0.6776 0.7070 0.9239 -0.0380 -0.1266 -0.1535 979  GLN A CG  
3402 C CD  . GLN A 442 ? 0.7139 0.7423 0.9245 -0.0216 -0.1342 -0.1641 979  GLN A CD  
3403 O OE1 . GLN A 442 ? 0.7133 0.7454 0.8956 -0.0136 -0.1263 -0.1536 979  GLN A OE1 
3404 N NE2 . GLN A 442 ? 0.7463 0.7678 0.9572 -0.0166 -0.1491 -0.1850 979  GLN A NE2 
3405 N N   . PRO A 443 ? 0.4391 0.4607 0.6941 -0.0680 -0.0736 -0.0813 980  PRO A N   
3406 C CA  . PRO A 443 ? 0.4040 0.4249 0.6370 -0.0689 -0.0615 -0.0618 980  PRO A CA  
3407 C C   . PRO A 443 ? 0.4027 0.4117 0.6083 -0.0603 -0.0622 -0.0535 980  PRO A C   
3408 O O   . PRO A 443 ? 0.4176 0.4116 0.6267 -0.0577 -0.0667 -0.0564 980  PRO A O   
3409 C CB  . PRO A 443 ? 0.4019 0.4102 0.6540 -0.0824 -0.0492 -0.0499 980  PRO A CB  
3410 C CG  . PRO A 443 ? 0.4194 0.4130 0.6957 -0.0861 -0.0552 -0.0589 980  PRO A CG  
3411 C CD  . PRO A 443 ? 0.4316 0.4385 0.7176 -0.0795 -0.0707 -0.0814 980  PRO A CD  
3412 N N   . TYR A 444 ? 0.3930 0.4089 0.5736 -0.0559 -0.0578 -0.0433 981  TYR A N   
3413 C CA  . TYR A 444 ? 0.3949 0.4019 0.5533 -0.0486 -0.0584 -0.0342 981  TYR A CA  
3414 C C   . TYR A 444 ? 0.3770 0.3653 0.5305 -0.0552 -0.0517 -0.0164 981  TYR A C   
3415 O O   . TYR A 444 ? 0.3833 0.3684 0.5393 -0.0643 -0.0429 -0.0078 981  TYR A O   
3416 C CB  . TYR A 444 ? 0.3471 0.3688 0.4826 -0.0413 -0.0577 -0.0320 981  TYR A CB  
3417 C CG  . TYR A 444 ? 0.3587 0.3915 0.4890 -0.0305 -0.0647 -0.0465 981  TYR A CG  
3418 C CD1 . TYR A 444 ? 0.3350 0.3826 0.4699 -0.0291 -0.0683 -0.0585 981  TYR A CD1 
3419 C CD2 . TYR A 444 ? 0.3411 0.3684 0.4615 -0.0211 -0.0673 -0.0477 981  TYR A CD2 
3420 C CE1 . TYR A 444 ? 0.3344 0.3884 0.4583 -0.0181 -0.0747 -0.0709 981  TYR A CE1 
3421 C CE2 . TYR A 444 ? 0.3397 0.3738 0.4512 -0.0106 -0.0710 -0.0600 981  TYR A CE2 
3422 C CZ  . TYR A 444 ? 0.4856 0.5318 0.5959 -0.0090 -0.0749 -0.0713 981  TYR A CZ  
3423 O OH  . TYR A 444 ? 0.3419 0.3915 0.4375 0.0026  -0.0786 -0.0828 981  TYR A OH  
3424 N N   . CYS A 445 ? 0.3839 0.3587 0.5299 -0.0497 -0.0557 -0.0106 982  CYS A N   
3425 C CA  . CYS A 445 ? 0.4334 0.3881 0.5701 -0.0535 -0.0525 0.0070  982  CYS A CA  
3426 C C   . CYS A 445 ? 0.3937 0.3520 0.5038 -0.0498 -0.0523 0.0183  982  CYS A C   
3427 O O   . CYS A 445 ? 0.3984 0.3481 0.4990 -0.0441 -0.0580 0.0258  982  CYS A O   
3428 C CB  . CYS A 445 ? 0.4143 0.3515 0.5606 -0.0492 -0.0587 0.0072  982  CYS A CB  
3429 S SG  . CYS A 445 ? 0.4424 0.3499 0.5794 -0.0535 -0.0567 0.0288  982  CYS A SG  
3430 N N   . LEU A 446 ? 0.4465 0.4180 0.5468 -0.0530 -0.0462 0.0186  983  LEU A N   
3431 C CA  . LEU A 446 ? 0.4176 0.3939 0.4931 -0.0500 -0.0458 0.0266  983  LEU A CA  
3432 C C   . LEU A 446 ? 0.4214 0.3936 0.4841 -0.0583 -0.0350 0.0356  983  LEU A C   
3433 O O   . LEU A 446 ? 0.4319 0.4119 0.5087 -0.0642 -0.0273 0.0302  983  LEU A O   
3434 C CB  . LEU A 446 ? 0.3803 0.3787 0.4542 -0.0426 -0.0486 0.0156  983  LEU A CB  
3435 C CG  . LEU A 446 ? 0.3611 0.3641 0.4443 -0.0332 -0.0560 0.0059  983  LEU A CG  
3436 C CD1 . LEU A 446 ? 0.3403 0.3628 0.4210 -0.0270 -0.0558 -0.0057 983  LEU A CD1 
3437 C CD2 . LEU A 446 ? 0.3503 0.3452 0.4259 -0.0278 -0.0614 0.0147  983  LEU A CD2 
3438 N N   . ARG A 447 ? 0.4243 0.3842 0.4607 -0.0584 -0.0347 0.0487  984  ARG A N   
3439 C CA  . ARG A 447 ? 0.4436 0.3949 0.4613 -0.0652 -0.0231 0.0581  984  ARG A CA  
3440 C C   . ARG A 447 ? 0.4205 0.3901 0.4280 -0.0635 -0.0192 0.0533  984  ARG A C   
3441 O O   . ARG A 447 ? 0.4050 0.3849 0.4053 -0.0566 -0.0274 0.0497  984  ARG A O   
3442 C CB  . ARG A 447 ? 0.4818 0.4070 0.4703 -0.0654 -0.0257 0.0741  984  ARG A CB  
3443 C CG  . ARG A 447 ? 0.5204 0.4297 0.4859 -0.0725 -0.0113 0.0850  984  ARG A CG  
3444 C CD  . ARG A 447 ? 0.5791 0.4586 0.5107 -0.0713 -0.0161 0.1008  984  ARG A CD  
3445 N NE  . ARG A 447 ? 0.6133 0.4761 0.5563 -0.0704 -0.0231 0.1060  984  ARG A NE  
3446 C CZ  . ARG A 447 ? 0.6436 0.4905 0.5967 -0.0769 -0.0124 0.1115  984  ARG A CZ  
3447 N NH1 . ARG A 447 ? 0.6575 0.5045 0.6134 -0.0852 0.0065  0.1123  984  ARG A NH1 
3448 N NH2 . ARG A 447 ? 0.6617 0.4924 0.6249 -0.0752 -0.0197 0.1161  984  ARG A NH2 
3449 N N   . ILE A 448 ? 0.4224 0.3954 0.4315 -0.0697 -0.0057 0.0536  985  ILE A N   
3450 C CA  . ILE A 448 ? 0.4012 0.3908 0.4035 -0.0681 -0.0004 0.0489  985  ILE A CA  
3451 C C   . ILE A 448 ? 0.4152 0.3915 0.3806 -0.0670 0.0008  0.0590  985  ILE A C   
3452 O O   . ILE A 448 ? 0.4494 0.4025 0.3934 -0.0712 0.0063  0.0708  985  ILE A O   
3453 C CB  . ILE A 448 ? 0.4165 0.4146 0.4382 -0.0748 0.0140  0.0454  985  ILE A CB  
3454 C CG1 . ILE A 448 ? 0.4001 0.4219 0.4555 -0.0723 0.0082  0.0299  985  ILE A CG1 
3455 C CG2 . ILE A 448 ? 0.4249 0.4250 0.4270 -0.0755 0.0257  0.0490  985  ILE A CG2 
3456 C CD1 . ILE A 448 ? 0.3642 0.3953 0.4486 -0.0794 0.0194  0.0254  985  ILE A CD1 
3457 N N   . GLU A 449 ? 0.4021 0.3909 0.3582 -0.0612 -0.0048 0.0544  986  GLU A N   
3458 C CA  . GLU A 449 ? 0.4187 0.3969 0.3417 -0.0603 -0.0042 0.0611  986  GLU A CA  
3459 C C   . GLU A 449 ? 0.4202 0.4093 0.3408 -0.0617 0.0090  0.0570  986  GLU A C   
3460 O O   . GLU A 449 ? 0.3831 0.3925 0.3159 -0.0571 0.0068  0.0480  986  GLU A O   
3461 C CB  . GLU A 449 ? 0.4202 0.4037 0.3378 -0.0534 -0.0189 0.0587  986  GLU A CB  
3462 C CG  . GLU A 449 ? 0.4477 0.4118 0.3327 -0.0531 -0.0258 0.0676  986  GLU A CG  
3463 C CD  . GLU A 449 ? 0.4651 0.4201 0.3217 -0.0561 -0.0148 0.0707  986  GLU A CD  
3464 O OE1 . GLU A 449 ? 0.5062 0.4366 0.3334 -0.0591 -0.0128 0.0803  986  GLU A OE1 
3465 O OE2 . GLU A 449 ? 0.4085 0.3794 0.2705 -0.0549 -0.0077 0.0636  986  GLU A OE2 
3466 N N   . PRO A 450 ? 0.4513 0.4267 0.3564 -0.0672 0.0237  0.0638  987  PRO A N   
3467 C CA  . PRO A 450 ? 0.4297 0.4178 0.3420 -0.0685 0.0386  0.0590  987  PRO A CA  
3468 C C   . PRO A 450 ? 0.4198 0.4172 0.3182 -0.0629 0.0358  0.0543  987  PRO A C   
3469 O O   . PRO A 450 ? 0.3935 0.4113 0.3111 -0.0604 0.0402  0.0461  987  PRO A O   
3470 C CB  . PRO A 450 ? 0.4447 0.4097 0.3357 -0.0749 0.0559  0.0695  987  PRO A CB  
3471 C CG  . PRO A 450 ? 0.4643 0.4092 0.3502 -0.0780 0.0508  0.0782  987  PRO A CG  
3472 C CD  . PRO A 450 ? 0.4515 0.3982 0.3334 -0.0720 0.0290  0.0764  987  PRO A CD  
3473 N N   . ASP A 451 ? 0.4384 0.4209 0.3053 -0.0607 0.0278  0.0589  988  ASP A N   
3474 C CA  . ASP A 451 ? 0.4262 0.4150 0.2804 -0.0563 0.0260  0.0545  988  ASP A CA  
3475 C C   . ASP A 451 ? 0.3923 0.4040 0.2707 -0.0503 0.0155  0.0457  988  ASP A C   
3476 O O   . ASP A 451 ? 0.3590 0.3848 0.2435 -0.0467 0.0196  0.0396  988  ASP A O   
3477 C CB  . ASP A 451 ? 0.4564 0.4225 0.2730 -0.0561 0.0178  0.0607  988  ASP A CB  
3478 C CG  . ASP A 451 ? 0.5060 0.4474 0.2885 -0.0602 0.0310  0.0680  988  ASP A CG  
3479 O OD1 . ASP A 451 ? 0.5240 0.4698 0.3112 -0.0620 0.0492  0.0664  988  ASP A OD1 
3480 O OD2 . ASP A 451 ? 0.5435 0.4601 0.2942 -0.0610 0.0234  0.0755  988  ASP A OD2 
3481 N N   . MET A 452 ? 0.3940 0.4080 0.2849 -0.0485 0.0028  0.0454  989  MET A N   
3482 C CA  . MET A 452 ? 0.3899 0.4235 0.3019 -0.0423 -0.0044 0.0374  989  MET A CA  
3483 C C   . MET A 452 ? 0.3953 0.4468 0.3322 -0.0411 0.0017  0.0297  989  MET A C   
3484 O O   . MET A 452 ? 0.3008 0.3677 0.2468 -0.0351 0.0002  0.0228  989  MET A O   
3485 C CB  . MET A 452 ? 0.3754 0.4061 0.2960 -0.0403 -0.0171 0.0385  989  MET A CB  
3486 C CG  . MET A 452 ? 0.3804 0.3950 0.2813 -0.0407 -0.0265 0.0455  989  MET A CG  
3487 S SD  . MET A 452 ? 0.3803 0.3938 0.2988 -0.0374 -0.0407 0.0466  989  MET A SD  
3488 C CE  . MET A 452 ? 0.3536 0.3907 0.2962 -0.0301 -0.0397 0.0360  989  MET A CE  
3489 N N   . ARG A 453 ? 0.3263 0.3749 0.2745 -0.0466 0.0082  0.0310  990  ARG A N   
3490 C CA  . ARG A 453 ? 0.4140 0.4796 0.3897 -0.0464 0.0126  0.0231  990  ARG A CA  
3491 C C   . ARG A 453 ? 0.4097 0.4861 0.3852 -0.0441 0.0217  0.0199  990  ARG A C   
3492 O O   . ARG A 453 ? 0.2942 0.3886 0.2873 -0.0388 0.0188  0.0115  990  ARG A O   
3493 C CB  . ARG A 453 ? 0.3280 0.3861 0.3178 -0.0543 0.0193  0.0262  990  ARG A CB  
3494 C CG  . ARG A 453 ? 0.3188 0.3942 0.3419 -0.0557 0.0233  0.0177  990  ARG A CG  
3495 C CD  . ARG A 453 ? 0.4441 0.5344 0.4853 -0.0493 0.0094  0.0067  990  ARG A CD  
3496 N NE  . ARG A 453 ? 0.4283 0.5283 0.5031 -0.0529 0.0090  -0.0009 990  ARG A NE  
3497 C CZ  . ARG A 453 ? 0.4101 0.5042 0.4996 -0.0562 0.0030  -0.0032 990  ARG A CZ  
3498 N NH1 . ARG A 453 ? 0.4072 0.4865 0.4808 -0.0555 -0.0025 0.0020  990  ARG A NH1 
3499 N NH2 . ARG A 453 ? 0.4102 0.5136 0.5329 -0.0601 0.0020  -0.0114 990  ARG A NH2 
3500 N N   . ARG A 454 ? 0.4196 0.4838 0.3739 -0.0474 0.0325  0.0263  991  ARG A N   
3501 C CA  . ARG A 454 ? 0.4070 0.4796 0.3599 -0.0445 0.0419  0.0233  991  ARG A CA  
3502 C C   . ARG A 454 ? 0.3092 0.3892 0.2536 -0.0365 0.0336  0.0194  991  ARG A C   
3503 O O   . ARG A 454 ? 0.3863 0.4805 0.3414 -0.0311 0.0361  0.0139  991  ARG A O   
3504 C CB  . ARG A 454 ? 0.4204 0.4742 0.3471 -0.0492 0.0559  0.0307  991  ARG A CB  
3505 C CG  . ARG A 454 ? 0.4486 0.4974 0.3871 -0.0563 0.0709  0.0344  991  ARG A CG  
3506 C CD  . ARG A 454 ? 0.4860 0.5120 0.3915 -0.0599 0.0865  0.0422  991  ARG A CD  
3507 N NE  . ARG A 454 ? 0.5183 0.5184 0.3918 -0.0633 0.0812  0.0513  991  ARG A NE  
3508 C CZ  . ARG A 454 ? 0.5443 0.5314 0.4194 -0.0692 0.0855  0.0582  991  ARG A CZ  
3509 N NH1 . ARG A 454 ? 0.5396 0.5379 0.4495 -0.0735 0.0958  0.0564  991  ARG A NH1 
3510 N NH2 . ARG A 454 ? 0.5689 0.5311 0.4121 -0.0707 0.0788  0.0669  991  ARG A NH2 
3511 N N   . PHE A 455 ? 0.3105 0.3806 0.2376 -0.0355 0.0240  0.0226  992  PHE A N   
3512 C CA  . PHE A 455 ? 0.3329 0.4082 0.2540 -0.0288 0.0178  0.0198  992  PHE A CA  
3513 C C   . PHE A 455 ? 0.3366 0.4305 0.2787 -0.0216 0.0132  0.0123  992  PHE A C   
3514 O O   . PHE A 455 ? 0.3097 0.4126 0.2530 -0.0157 0.0159  0.0088  992  PHE A O   
3515 C CB  . PHE A 455 ? 0.3706 0.4344 0.2792 -0.0296 0.0075  0.0240  992  PHE A CB  
3516 C CG  . PHE A 455 ? 0.3481 0.4158 0.2534 -0.0239 0.0026  0.0220  992  PHE A CG  
3517 C CD1 . PHE A 455 ? 0.3468 0.4077 0.2353 -0.0238 0.0064  0.0228  992  PHE A CD1 
3518 C CD2 . PHE A 455 ? 0.3196 0.3958 0.2383 -0.0189 -0.0044 0.0192  992  PHE A CD2 
3519 C CE1 . PHE A 455 ? 0.3374 0.4009 0.2258 -0.0194 0.0031  0.0214  992  PHE A CE1 
3520 C CE2 . PHE A 455 ? 0.3190 0.3975 0.2362 -0.0141 -0.0061 0.0184  992  PHE A CE2 
3521 C CZ  . PHE A 455 ? 0.3242 0.3966 0.2276 -0.0147 -0.0025 0.0197  992  PHE A CZ  
3522 N N   . PHE A 456 ? 0.2748 0.3730 0.2318 -0.0215 0.0060  0.0097  993  PHE A N   
3523 C CA  . PHE A 456 ? 0.4012 0.5136 0.3726 -0.0139 0.0000  0.0019  993  PHE A CA  
3524 C C   . PHE A 456 ? 0.2599 0.3857 0.2490 -0.0124 0.0031  -0.0041 993  PHE A C   
3525 O O   . PHE A 456 ? 0.2536 0.3904 0.2482 -0.0042 -0.0016 -0.0102 993  PHE A O   
3526 C CB  . PHE A 456 ? 0.2612 0.3718 0.2417 -0.0140 -0.0086 -0.0003 993  PHE A CB  
3527 C CG  . PHE A 456 ? 0.3156 0.4160 0.2846 -0.0136 -0.0128 0.0046  993  PHE A CG  
3528 C CD1 . PHE A 456 ? 0.3043 0.4069 0.2655 -0.0068 -0.0138 0.0042  993  PHE A CD1 
3529 C CD2 . PHE A 456 ? 0.3228 0.4114 0.2910 -0.0197 -0.0156 0.0099  993  PHE A CD2 
3530 C CE1 . PHE A 456 ? 0.3045 0.3996 0.2617 -0.0068 -0.0174 0.0083  993  PHE A CE1 
3531 C CE2 . PHE A 456 ? 0.3150 0.3958 0.2773 -0.0186 -0.0211 0.0140  993  PHE A CE2 
3532 C CZ  . PHE A 456 ? 0.3029 0.3882 0.2619 -0.0125 -0.0219 0.0128  993  PHE A CZ  
3533 N N   . GLU A 457 ? 0.3514 0.4761 0.3501 -0.0197 0.0110  -0.0021 994  GLU A N   
3534 C CA  . GLU A 457 ? 0.3345 0.4735 0.3549 -0.0183 0.0151  -0.0076 994  GLU A CA  
3535 C C   . GLU A 457 ? 0.3236 0.4665 0.3351 -0.0128 0.0218  -0.0070 994  GLU A C   
3536 O O   . GLU A 457 ? 0.3295 0.4868 0.3590 -0.0077 0.0214  -0.0126 994  GLU A O   
3537 C CB  . GLU A 457 ? 0.2738 0.4102 0.3104 -0.0281 0.0251  -0.0051 994  GLU A CB  
3538 C CG  . GLU A 457 ? 0.3186 0.4555 0.3750 -0.0328 0.0182  -0.0083 994  GLU A CG  
3539 C CD  . GLU A 457 ? 0.3298 0.4596 0.3994 -0.0434 0.0305  -0.0035 994  GLU A CD  
3540 O OE1 . GLU A 457 ? 0.3397 0.4570 0.3912 -0.0476 0.0441  0.0050  994  GLU A OE1 
3541 O OE2 . GLU A 457 ? 0.3371 0.4722 0.4345 -0.0475 0.0269  -0.0083 994  GLU A OE2 
3542 N N   . ASN A 458 ? 0.3196 0.4495 0.3049 -0.0134 0.0269  -0.0008 995  ASN A N   
3543 C CA  . ASN A 458 ? 0.3332 0.4634 0.3093 -0.0092 0.0348  -0.0002 995  ASN A CA  
3544 C C   . ASN A 458 ? 0.3144 0.4430 0.2749 -0.0012 0.0290  -0.0003 995  ASN A C   
3545 O O   . ASN A 458 ? 0.3126 0.4379 0.2626 0.0020  0.0353  0.0009  995  ASN A O   
3546 C CB  . ASN A 458 ? 0.3753 0.4891 0.3324 -0.0163 0.0472  0.0060  995  ASN A CB  
3547 C CG  . ASN A 458 ? 0.3956 0.5087 0.3668 -0.0238 0.0574  0.0075  995  ASN A CG  
3548 O OD1 . ASN A 458 ? 0.4006 0.5294 0.4013 -0.0228 0.0601  0.0028  995  ASN A OD1 
3549 N ND2 . ASN A 458 ? 0.4040 0.4981 0.3548 -0.0313 0.0629  0.0143  995  ASN A ND2 
3550 N N   . LEU A 459 ? 0.2699 0.3997 0.2294 0.0020  0.0186  -0.0016 996  LEU A N   
3551 C CA  . LEU A 459 ? 0.3095 0.4376 0.2566 0.0098  0.0155  -0.0012 996  LEU A CA  
3552 C C   . LEU A 459 ? 0.3218 0.4591 0.2731 0.0193  0.0170  -0.0045 996  LEU A C   
3553 O O   . LEU A 459 ? 0.3085 0.4581 0.2760 0.0237  0.0119  -0.0099 996  LEU A O   
3554 C CB  . LEU A 459 ? 0.2977 0.4267 0.2461 0.0131  0.0063  -0.0031 996  LEU A CB  
3555 C CG  . LEU A 459 ? 0.2934 0.4126 0.2376 0.0063  0.0034  0.0007  996  LEU A CG  
3556 C CD1 . LEU A 459 ? 0.3007 0.4226 0.2503 0.0110  -0.0041 -0.0028 996  LEU A CD1 
3557 C CD2 . LEU A 459 ? 0.2902 0.3986 0.2195 0.0045  0.0063  0.0062  996  LEU A CD2 
3558 N N   . ASN A 460 ? 0.3342 0.4649 0.2720 0.0226  0.0227  -0.0014 997  ASN A N   
3559 C CA  . ASN A 460 ? 0.3314 0.4677 0.2702 0.0329  0.0242  -0.0030 997  ASN A CA  
3560 C C   . ASN A 460 ? 0.3521 0.4789 0.2739 0.0384  0.0249  0.0006  997  ASN A C   
3561 O O   . ASN A 460 ? 0.3349 0.4527 0.2468 0.0381  0.0321  0.0037  997  ASN A O   
3562 C CB  . ASN A 460 ? 0.3283 0.4646 0.2709 0.0315  0.0343  -0.0028 997  ASN A CB  
3563 C CG  . ASN A 460 ? 0.3466 0.4902 0.2951 0.0431  0.0346  -0.0047 997  ASN A CG  
3564 O OD1 . ASN A 460 ? 0.3571 0.5105 0.3137 0.0514  0.0253  -0.0080 997  ASN A OD1 
3565 N ND2 . ASN A 460 ? 0.3624 0.4997 0.3055 0.0443  0.0446  -0.0029 997  ASN A ND2 
3566 N N   . PRO A 461 ? 0.2634 0.3907 0.1815 0.0435  0.0187  0.0002  998  PRO A N   
3567 C CA  . PRO A 461 ? 0.3313 0.4487 0.2354 0.0484  0.0222  0.0045  998  PRO A CA  
3568 C C   . PRO A 461 ? 0.3432 0.4581 0.2400 0.0582  0.0267  0.0063  998  PRO A C   
3569 O O   . PRO A 461 ? 0.3151 0.4192 0.2027 0.0587  0.0336  0.0109  998  PRO A O   
3570 C CB  . PRO A 461 ? 0.2689 0.3879 0.1711 0.0531  0.0161  0.0028  998  PRO A CB  
3571 C CG  . PRO A 461 ? 0.2669 0.3972 0.1800 0.0547  0.0075  -0.0038 998  PRO A CG  
3572 C CD  . PRO A 461 ? 0.2604 0.3952 0.1867 0.0448  0.0095  -0.0045 998  PRO A CD  
3573 N N   . MET A 462 ? 0.3826 0.5069 0.2855 0.0661  0.0226  0.0028  999  MET A N   
3574 C CA  . MET A 462 ? 0.4051 0.5260 0.3007 0.0773  0.0256  0.0051  999  MET A CA  
3575 C C   . MET A 462 ? 0.4027 0.5181 0.2997 0.0735  0.0354  0.0073  999  MET A C   
3576 O O   . MET A 462 ? 0.4271 0.5337 0.3151 0.0806  0.0408  0.0110  999  MET A O   
3577 C CB  . MET A 462 ? 0.4276 0.5606 0.3317 0.0876  0.0157  0.0001  999  MET A CB  
3578 C CG  . MET A 462 ? 0.4610 0.5933 0.3533 0.0969  0.0061  -0.0017 999  MET A CG  
3579 S SD  . MET A 462 ? 0.5126 0.6581 0.4146 0.1096  -0.0096 -0.0089 999  MET A SD  
3580 C CE  . MET A 462 ? 0.5150 0.6739 0.4378 0.0999  -0.0199 -0.0181 999  MET A CE  
3581 N N   . GLY A 463 ? 0.3736 0.4919 0.2800 0.0631  0.0385  0.0050  1000 GLY A N   
3582 C CA  . GLY A 463 ? 0.3703 0.4815 0.2750 0.0603  0.0485  0.0059  1000 GLY A CA  
3583 C C   . GLY A 463 ? 0.3590 0.4784 0.2754 0.0696  0.0503  0.0037  1000 GLY A C   
3584 O O   . GLY A 463 ? 0.2904 0.4248 0.2254 0.0707  0.0459  -0.0005 1000 GLY A O   
3585 N N   . SER A 464 ? 0.3361 0.4459 0.2447 0.0765  0.0567  0.0064  1001 SER A N   
3586 C CA  . SER A 464 ? 0.3280 0.4448 0.2482 0.0879  0.0574  0.0052  1001 SER A CA  
3587 C C   . SER A 464 ? 0.3633 0.4802 0.2771 0.1023  0.0489  0.0079  1001 SER A C   
3588 O O   . SER A 464 ? 0.3866 0.5098 0.3102 0.1137  0.0460  0.0072  1001 SER A O   
3589 C CB  . SER A 464 ? 0.3226 0.4267 0.2381 0.0881  0.0702  0.0062  1001 SER A CB  
3590 O OG  . SER A 464 ? 0.4612 0.5633 0.3791 0.0768  0.0786  0.0031  1001 SER A OG  
3591 N N   . ALA A 465 ? 0.3661 0.4755 0.2633 0.1027  0.0452  0.0114  1002 ALA A N   
3592 C CA  . ALA A 465 ? 0.3892 0.4946 0.2736 0.1169  0.0389  0.0148  1002 ALA A CA  
3593 C C   . ALA A 465 ? 0.3972 0.5187 0.2916 0.1238  0.0237  0.0092  1002 ALA A C   
3594 O O   . ALA A 465 ? 0.3831 0.5180 0.2940 0.1155  0.0186  0.0032  1002 ALA A O   
3595 C CB  . ALA A 465 ? 0.4032 0.4948 0.2676 0.1148  0.0423  0.0200  1002 ALA A CB  
3596 N N   . SER A 466 ? 0.4254 0.5439 0.3090 0.1395  0.0159  0.0112  1003 SER A N   
3597 C CA  . SER A 466 ? 0.4448 0.5744 0.3309 0.1475  -0.0014 0.0055  1003 SER A CA  
3598 C C   . SER A 466 ? 0.4615 0.5820 0.3245 0.1470  -0.0040 0.0064  1003 SER A C   
3599 O O   . SER A 466 ? 0.4504 0.5556 0.2953 0.1438  0.0078  0.0131  1003 SER A O   
3600 C CB  . SER A 466 ? 0.4656 0.5937 0.3462 0.1660  -0.0110 0.0071  1003 SER A CB  
3601 O OG  . SER A 466 ? 0.4879 0.5938 0.3360 0.1754  -0.0044 0.0165  1003 SER A OG  
3602 N N   . GLU A 467 ? 0.5139 0.7307 0.4265 0.0447  0.0536  0.0229  1004 GLU A N   
3603 C CA  . GLU A 467 ? 0.5396 0.7342 0.4422 0.0342  0.0519  0.0322  1004 GLU A CA  
3604 C C   . GLU A 467 ? 0.5319 0.6903 0.4237 0.0449  0.0521  0.0378  1004 GLU A C   
3605 O O   . GLU A 467 ? 0.5279 0.6600 0.4124 0.0375  0.0554  0.0431  1004 GLU A O   
3606 C CB  . GLU A 467 ? 0.5951 0.8105 0.5001 0.0288  0.0454  0.0360  1004 GLU A CB  
3607 C CG  . GLU A 467 ? 0.6435 0.8414 0.5386 0.0158  0.0438  0.0432  1004 GLU A CG  
3608 C CD  . GLU A 467 ? 0.6779 0.9000 0.5797 0.0005  0.0396  0.0435  1004 GLU A CD  
3609 O OE1 . GLU A 467 ? 0.6911 0.9032 0.5854 -0.0058 0.0347  0.0479  1004 GLU A OE1 
3610 O OE2 . GLU A 467 ? 0.6831 0.9336 0.5973 -0.0052 0.0413  0.0394  1004 GLU A OE2 
3611 N N   . LYS A 468 ? 0.5271 0.6843 0.4186 0.0625  0.0487  0.0371  1005 LYS A N   
3612 C CA  . LYS A 468 ? 0.5224 0.6438 0.4029 0.0732  0.0492  0.0438  1005 LYS A CA  
3613 C C   . LYS A 468 ? 0.5009 0.5965 0.3822 0.0717  0.0551  0.0412  1005 LYS A C   
3614 O O   . LYS A 468 ? 0.4946 0.5604 0.3690 0.0667  0.0587  0.0488  1005 LYS A O   
3615 C CB  . LYS A 468 ? 0.5552 0.6808 0.4353 0.0938  0.0432  0.0431  1005 LYS A CB  
3616 C CG  . LYS A 468 ? 0.5980 0.6848 0.4650 0.1053  0.0437  0.0520  1005 LYS A CG  
3617 C CD  . LYS A 468 ? 0.6203 0.6892 0.4727 0.0969  0.0454  0.0639  1005 LYS A CD  
3618 C CE  . LYS A 468 ? 0.6609 0.6890 0.5018 0.1023  0.0501  0.0744  1005 LYS A CE  
3619 N NZ  . LYS A 468 ? 0.6621 0.6759 0.4904 0.0921  0.0549  0.0852  1005 LYS A NZ  
3620 N N   . GLU A 469 ? 0.4887 0.5964 0.3790 0.0761  0.0559  0.0300  1006 GLU A N   
3621 C CA  . GLU A 469 ? 0.4782 0.5613 0.3694 0.0750  0.0594  0.0252  1006 GLU A CA  
3622 C C   . GLU A 469 ? 0.4554 0.5303 0.3460 0.0557  0.0633  0.0279  1006 GLU A C   
3623 O O   . GLU A 469 ? 0.4606 0.5055 0.3500 0.0517  0.0656  0.0312  1006 GLU A O   
3624 C CB  . GLU A 469 ? 0.4689 0.5705 0.3676 0.0837  0.0593  0.0106  1006 GLU A CB  
3625 C CG  . GLU A 469 ? 0.4784 0.5785 0.3788 0.1060  0.0554  0.0063  1006 GLU A CG  
3626 C CD  . GLU A 469 ? 0.4713 0.5897 0.3784 0.1161  0.0562  -0.0096 1006 GLU A CD  
3627 O OE1 . GLU A 469 ? 0.4576 0.5997 0.3678 0.1054  0.0599  -0.0161 1006 GLU A OE1 
3628 O OE2 . GLU A 469 ? 0.4926 0.6009 0.4008 0.1355  0.0530  -0.0156 1006 GLU A OE2 
3629 N N   . PHE A 470 ? 0.4329 0.5341 0.3256 0.0433  0.0636  0.0271  1007 PHE A N   
3630 C CA  . PHE A 470 ? 0.4180 0.5125 0.3102 0.0263  0.0661  0.0293  1007 PHE A CA  
3631 C C   . PHE A 470 ? 0.4072 0.4789 0.2939 0.0210  0.0675  0.0411  1007 PHE A C   
3632 O O   . PHE A 470 ? 0.4093 0.4625 0.2975 0.0124  0.0703  0.0434  1007 PHE A O   
3633 C CB  . PHE A 470 ? 0.3870 0.5129 0.2815 0.0150  0.0655  0.0272  1007 PHE A CB  
3634 C CG  . PHE A 470 ? 0.4211 0.5421 0.3151 -0.0002 0.0669  0.0272  1007 PHE A CG  
3635 C CD1 . PHE A 470 ? 0.4300 0.5427 0.3253 -0.0009 0.0680  0.0193  1007 PHE A CD1 
3636 C CD2 . PHE A 470 ? 0.4109 0.5350 0.3027 -0.0129 0.0659  0.0342  1007 PHE A CD2 
3637 C CE1 . PHE A 470 ? 0.4216 0.5307 0.3163 -0.0140 0.0678  0.0191  1007 PHE A CE1 
3638 C CE2 . PHE A 470 ? 0.4105 0.5299 0.3020 -0.0255 0.0662  0.0344  1007 PHE A CE2 
3639 C CZ  . PHE A 470 ? 0.4183 0.5310 0.3114 -0.0261 0.0670  0.0272  1007 PHE A CZ  
3640 N N   . THR A 471 ? 0.3949 0.4691 0.2753 0.0268  0.0656  0.0481  1008 THR A N   
3641 C CA  . THR A 471 ? 0.4058 0.4599 0.2779 0.0240  0.0679  0.0591  1008 THR A CA  
3642 C C   . THR A 471 ? 0.4350 0.4570 0.3063 0.0287  0.0724  0.0644  1008 THR A C   
3643 O O   . THR A 471 ? 0.4150 0.4207 0.2872 0.0199  0.0773  0.0702  1008 THR A O   
3644 C CB  . THR A 471 ? 0.4012 0.4639 0.2639 0.0320  0.0636  0.0641  1008 THR A CB  
3645 O OG1 . THR A 471 ? 0.3862 0.4788 0.2529 0.0256  0.0587  0.0592  1008 THR A OG1 
3646 C CG2 . THR A 471 ? 0.4078 0.4516 0.2585 0.0301  0.0667  0.0748  1008 THR A CG2 
3647 N N   . ASP A 472 ? 0.4447 0.4573 0.3157 0.0425  0.0708  0.0627  1009 ASP A N   
3648 C CA  . ASP A 472 ? 0.4706 0.4499 0.3419 0.0461  0.0743  0.0681  1009 ASP A CA  
3649 C C   . ASP A 472 ? 0.4835 0.4530 0.3665 0.0345  0.0766  0.0621  1009 ASP A C   
3650 O O   . ASP A 472 ? 0.4606 0.4067 0.3471 0.0281  0.0812  0.0694  1009 ASP A O   
3651 C CB  . ASP A 472 ? 0.4951 0.4656 0.3645 0.0638  0.0703  0.0654  1009 ASP A CB  
3652 C CG  . ASP A 472 ? 0.5202 0.4904 0.3766 0.0764  0.0678  0.0747  1009 ASP A CG  
3653 O OD1 . ASP A 472 ? 0.5188 0.4901 0.3659 0.0712  0.0702  0.0839  1009 ASP A OD1 
3654 O OD2 . ASP A 472 ? 0.5448 0.5138 0.3996 0.0926  0.0628  0.0720  1009 ASP A OD2 
3655 N N   . TYR A 473 ? 0.4809 0.4693 0.3703 0.0317  0.0734  0.0491  1010 TYR A N   
3656 C CA  . TYR A 473 ? 0.4697 0.4499 0.3682 0.0217  0.0736  0.0420  1010 TYR A CA  
3657 C C   . TYR A 473 ? 0.4533 0.4326 0.3553 0.0061  0.0769  0.0484  1010 TYR A C   
3658 O O   . TYR A 473 ? 0.4290 0.3901 0.3399 -0.0015 0.0785  0.0494  1010 TYR A O   
3659 C CB  . TYR A 473 ? 0.4596 0.4636 0.3599 0.0228  0.0700  0.0274  1010 TYR A CB  
3660 C CG  . TYR A 473 ? 0.4209 0.4263 0.3265 0.0096  0.0692  0.0210  1010 TYR A CG  
3661 C CD1 . TYR A 473 ? 0.4366 0.4202 0.3485 0.0086  0.0670  0.0140  1010 TYR A CD1 
3662 C CD2 . TYR A 473 ? 0.4056 0.4327 0.3097 -0.0017 0.0693  0.0220  1010 TYR A CD2 
3663 C CE1 . TYR A 473 ? 0.4304 0.4160 0.3467 -0.0029 0.0645  0.0075  1010 TYR A CE1 
3664 C CE2 . TYR A 473 ? 0.3940 0.4221 0.3015 -0.0126 0.0674  0.0167  1010 TYR A CE2 
3665 C CZ  . TYR A 473 ? 0.4498 0.4583 0.3633 -0.0129 0.0648  0.0092  1010 TYR A CZ  
3666 O OH  . TYR A 473 ? 0.4048 0.4153 0.3211 -0.0232 0.0612  0.0035  1010 TYR A OH  
3667 N N   . LEU A 474 ? 0.4334 0.4326 0.3301 0.0013  0.0773  0.0523  1011 LEU A N   
3668 C CA  . LEU A 474 ? 0.4333 0.4320 0.3328 -0.0115 0.0799  0.0579  1011 LEU A CA  
3669 C C   . LEU A 474 ? 0.4483 0.4239 0.3490 -0.0118 0.0862  0.0696  1011 LEU A C   
3670 O O   . LEU A 474 ? 0.4047 0.3700 0.3161 -0.0209 0.0890  0.0715  1011 LEU A O   
3671 C CB  . LEU A 474 ? 0.4171 0.4371 0.3089 -0.0146 0.0782  0.0600  1011 LEU A CB  
3672 C CG  . LEU A 474 ? 0.4077 0.4533 0.2995 -0.0183 0.0734  0.0514  1011 LEU A CG  
3673 C CD1 . LEU A 474 ? 0.4000 0.4626 0.2849 -0.0203 0.0710  0.0551  1011 LEU A CD1 
3674 C CD2 . LEU A 474 ? 0.3988 0.4460 0.2968 -0.0297 0.0722  0.0465  1011 LEU A CD2 
3675 N N   . PHE A 475 ? 0.4555 0.4239 0.3455 -0.0018 0.0886  0.0781  1012 PHE A N   
3676 C CA  . PHE A 475 ? 0.4755 0.4231 0.3643 -0.0020 0.0962  0.0910  1012 PHE A CA  
3677 C C   . PHE A 475 ? 0.5027 0.4266 0.4043 -0.0044 0.0984  0.0919  1012 PHE A C   
3678 O O   . PHE A 475 ? 0.5097 0.4212 0.4203 -0.0124 0.1050  0.1000  1012 PHE A O   
3679 C CB  . PHE A 475 ? 0.5068 0.4493 0.3786 0.0106  0.0976  0.1003  1012 PHE A CB  
3680 C CG  . PHE A 475 ? 0.5392 0.4608 0.4068 0.0109  0.1068  0.1150  1012 PHE A CG  
3681 C CD1 . PHE A 475 ? 0.5412 0.4660 0.4100 0.0028  0.1139  0.1212  1012 PHE A CD1 
3682 C CD2 . PHE A 475 ? 0.5714 0.4702 0.4337 0.0200  0.1090  0.1234  1012 PHE A CD2 
3683 C CE1 . PHE A 475 ? 0.5668 0.4754 0.4322 0.0031  0.1243  0.1356  1012 PHE A CE1 
3684 C CE2 . PHE A 475 ? 0.6026 0.4827 0.4598 0.0197  0.1188  0.1392  1012 PHE A CE2 
3685 C CZ  . PHE A 475 ? 0.5959 0.4826 0.4552 0.0107  0.1273  0.1452  1012 PHE A CZ  
3686 N N   . ASN A 476 ? 0.5218 0.4390 0.4251 0.0028  0.0930  0.0837  1013 ASN A N   
3687 C CA  . ASN A 476 ? 0.5459 0.4380 0.4617 0.0000  0.0929  0.0824  1013 ASN A CA  
3688 C C   . ASN A 476 ? 0.5088 0.4045 0.4414 -0.0149 0.0919  0.0759  1013 ASN A C   
3689 O O   . ASN A 476 ? 0.5121 0.3892 0.4585 -0.0231 0.0950  0.0808  1013 ASN A O   
3690 C CB  . ASN A 476 ? 0.5608 0.4466 0.4747 0.0119  0.0857  0.0714  1013 ASN A CB  
3691 C CG  . ASN A 476 ? 0.5626 0.4358 0.4637 0.0275  0.0860  0.0795  1013 ASN A CG  
3692 O OD1 . ASN A 476 ? 0.5695 0.4279 0.4644 0.0282  0.0921  0.0950  1013 ASN A OD1 
3693 N ND2 . ASN A 476 ? 0.5696 0.4499 0.4661 0.0410  0.0795  0.0693  1013 ASN A ND2 
3694 N N   . LYS A 477 ? 0.4740 0.3937 0.4061 -0.0189 0.0872  0.0651  1014 LYS A N   
3695 C CA  . LYS A 477 ? 0.4677 0.3919 0.4136 -0.0321 0.0848  0.0592  1014 LYS A CA  
3696 C C   . LYS A 477 ? 0.4579 0.3840 0.4110 -0.0415 0.0917  0.0706  1014 LYS A C   
3697 O O   . LYS A 477 ? 0.4604 0.3812 0.4306 -0.0519 0.0917  0.0702  1014 LYS A O   
3698 C CB  . LYS A 477 ? 0.4527 0.4015 0.3929 -0.0334 0.0784  0.0472  1014 LYS A CB  
3699 C CG  . LYS A 477 ? 0.4291 0.3836 0.3805 -0.0456 0.0743  0.0410  1014 LYS A CG  
3700 C CD  . LYS A 477 ? 0.4378 0.3736 0.4018 -0.0483 0.0695  0.0327  1014 LYS A CD  
3701 C CE  . LYS A 477 ? 0.4435 0.3786 0.3984 -0.0381 0.0637  0.0192  1014 LYS A CE  
3702 N NZ  . LYS A 477 ? 0.4544 0.3728 0.4196 -0.0412 0.0563  0.0072  1014 LYS A NZ  
3703 N N   . SER A 478 ? 0.4448 0.3789 0.3854 -0.0372 0.0970  0.0800  1015 SER A N   
3704 C CA  . SER A 478 ? 0.4429 0.3788 0.3882 -0.0433 0.1047  0.0905  1015 SER A CA  
3705 C C   . SER A 478 ? 0.4673 0.3820 0.4237 -0.0459 0.1130  0.1018  1015 SER A C   
3706 O O   . SER A 478 ? 0.4639 0.3787 0.4374 -0.0557 0.1176  0.1059  1015 SER A O   
3707 C CB  . SER A 478 ? 0.4383 0.3849 0.3646 -0.0362 0.1076  0.0966  1015 SER A CB  
3708 O OG  . SER A 478 ? 0.4327 0.3808 0.3612 -0.0399 0.1157  0.1058  1015 SER A OG  
3709 N N   . LEU A 479 ? 0.4968 0.3935 0.4443 -0.0371 0.1150  0.1078  1016 LEU A N   
3710 C CA  . LEU A 479 ? 0.5260 0.3993 0.4836 -0.0404 0.1228  0.1201  1016 LEU A CA  
3711 C C   . LEU A 479 ? 0.5492 0.4133 0.5326 -0.0526 0.1189  0.1134  1016 LEU A C   
3712 O O   . LEU A 479 ? 0.4956 0.3508 0.4970 -0.0623 0.1260  0.1229  1016 LEU A O   
3713 C CB  . LEU A 479 ? 0.5365 0.3891 0.4794 -0.0280 0.1227  0.1261  1016 LEU A CB  
3714 C CG  . LEU A 479 ? 0.5317 0.3874 0.4497 -0.0158 0.1276  0.1369  1016 LEU A CG  
3715 C CD1 . LEU A 479 ? 0.5546 0.3880 0.4604 -0.0031 0.1252  0.1419  1016 LEU A CD1 
3716 C CD2 . LEU A 479 ? 0.5293 0.3850 0.4464 -0.0206 0.1408  0.1527  1016 LEU A CD2 
3717 N N   . GLU A 480 ? 0.5428 0.4104 0.5287 -0.0523 0.1074  0.0968  1017 GLU A N   
3718 C CA  . GLU A 480 ? 0.5434 0.4010 0.5512 -0.0625 0.1008  0.0876  1017 GLU A CA  
3719 C C   . GLU A 480 ? 0.5242 0.3986 0.5507 -0.0757 0.1013  0.0865  1017 GLU A C   
3720 O O   . GLU A 480 ? 0.4770 0.3422 0.5275 -0.0869 0.1012  0.0877  1017 GLU A O   
3721 C CB  . GLU A 480 ? 0.5320 0.3907 0.5324 -0.0561 0.0886  0.0692  1017 GLU A CB  
3722 C CG  . GLU A 480 ? 0.5345 0.3827 0.5532 -0.0647 0.0793  0.0564  1017 GLU A CG  
3723 C CD  . GLU A 480 ? 0.5424 0.3928 0.5494 -0.0559 0.0685  0.0378  1017 GLU A CD  
3724 O OE1 . GLU A 480 ? 0.5417 0.4031 0.5293 -0.0436 0.0692  0.0359  1017 GLU A OE1 
3725 O OE2 . GLU A 480 ? 0.5533 0.3958 0.5709 -0.0609 0.0591  0.0245  1017 GLU A OE2 
3726 N N   . ILE A 481 ? 0.4955 0.3944 0.5128 -0.0746 0.1010  0.0840  1018 ILE A N   
3727 C CA  . ILE A 481 ? 0.4596 0.3744 0.4938 -0.0852 0.0988  0.0807  1018 ILE A CA  
3728 C C   . ILE A 481 ? 0.4520 0.3716 0.4980 -0.0900 0.1111  0.0954  1018 ILE A C   
3729 O O   . ILE A 481 ? 0.4513 0.3793 0.5206 -0.1000 0.1109  0.0950  1018 ILE A O   
3730 C CB  . ILE A 481 ? 0.4314 0.3678 0.4512 -0.0823 0.0918  0.0713  1018 ILE A CB  
3731 C CG1 . ILE A 481 ? 0.4162 0.3626 0.4151 -0.0740 0.0981  0.0790  1018 ILE A CG1 
3732 C CG2 . ILE A 481 ? 0.4411 0.3761 0.4510 -0.0782 0.0810  0.0567  1018 ILE A CG2 
3733 C CD1 . ILE A 481 ? 0.3954 0.3612 0.3812 -0.0729 0.0912  0.0714  1018 ILE A CD1 
3734 N N   . GLU A 482 ? 0.4326 0.3484 0.4630 -0.0824 0.1218  0.1081  1019 GLU A N   
3735 C CA  . GLU A 482 ? 0.4381 0.3569 0.4768 -0.0852 0.1359  0.1233  1019 GLU A CA  
3736 C C   . GLU A 482 ? 0.5062 0.4052 0.5321 -0.0788 0.1454  0.1372  1019 GLU A C   
3737 O O   . GLU A 482 ? 0.4993 0.4000 0.5002 -0.0679 0.1502  0.1435  1019 GLU A O   
3738 C CB  . GLU A 482 ? 0.4199 0.3598 0.4467 -0.0806 0.1393  0.1241  1019 GLU A CB  
3739 C CG  . GLU A 482 ? 0.4595 0.4175 0.4993 -0.0868 0.1303  0.1128  1019 GLU A CG  
3740 C CD  . GLU A 482 ? 0.4346 0.4099 0.4679 -0.0830 0.1349  0.1154  1019 GLU A CD  
3741 O OE1 . GLU A 482 ? 0.4366 0.4110 0.4571 -0.0763 0.1462  0.1259  1019 GLU A OE1 
3742 O OE2 . GLU A 482 ? 0.4072 0.3957 0.4469 -0.0861 0.1267  0.1069  1019 GLU A OE2 
3743 N N   . PRO A 483 ? 0.5278 0.4057 0.5697 -0.0852 0.1470  0.1424  1020 PRO A N   
3744 C CA  . PRO A 483 ? 0.5650 0.4200 0.5937 -0.0789 0.1552  0.1571  1020 PRO A CA  
3745 C C   . PRO A 483 ? 0.5685 0.4302 0.5888 -0.0764 0.1719  0.1751  1020 PRO A C   
3746 O O   . PRO A 483 ? 0.5423 0.4234 0.5769 -0.0829 0.1787  0.1775  1020 PRO A O   
3747 C CB  . PRO A 483 ? 0.5865 0.4186 0.6411 -0.0903 0.1534  0.1591  1020 PRO A CB  
3748 C CG  . PRO A 483 ? 0.5641 0.4044 0.6362 -0.0976 0.1389  0.1394  1020 PRO A CG  
3749 C CD  . PRO A 483 ? 0.5275 0.3992 0.5984 -0.0978 0.1388  0.1336  1020 PRO A CD  
3750 N N   . ARG A 484 ? 0.6101 0.4564 0.6054 -0.0654 0.1774  0.1869  1021 ARG A N   
3751 C CA  . ARG A 484 ? 0.6631 0.5179 0.6436 -0.0598 0.1865  0.1982  1021 ARG A CA  
3752 C C   . ARG A 484 ? 0.6959 0.5569 0.7020 -0.0722 0.1930  0.2043  1021 ARG A C   
3753 O O   . ARG A 484 ? 0.7200 0.5643 0.7479 -0.0829 0.1926  0.2082  1021 ARG A O   
3754 C CB  . ARG A 484 ? 0.7001 0.5331 0.6533 -0.0474 0.1878  0.2090  1021 ARG A CB  
3755 C CG  . ARG A 484 ? 0.6935 0.5319 0.6134 -0.0310 0.1835  0.2053  1021 ARG A CG  
3756 C CD  . ARG A 484 ? 0.7318 0.5493 0.6260 -0.0181 0.1839  0.2168  1021 ARG A CD  
3757 N NE  . ARG A 484 ? 0.7584 0.5861 0.6346 -0.0118 0.1888  0.2237  1021 ARG A NE  
3758 C CZ  . ARG A 484 ? 0.7950 0.6061 0.6549 -0.0050 0.1920  0.2368  1021 ARG A CZ  
3759 N NH1 . ARG A 484 ? 0.8207 0.6026 0.6811 -0.0037 0.1901  0.2449  1021 ARG A NH1 
3760 N NH2 . ARG A 484 ? 0.8061 0.6280 0.6485 0.0008  0.1969  0.2418  1021 ARG A NH2 
3761 N N   . ASN A 485 ? 0.6954 0.5805 0.6994 -0.0706 0.1986  0.2045  1022 ASN A N   
3762 C CA  . ASN A 485 ? 0.7293 0.6239 0.7525 -0.0795 0.2077  0.2122  1022 ASN A CA  
3763 C C   . ASN A 485 ? 0.7534 0.6529 0.8161 -0.0960 0.2048  0.2071  1022 ASN A C   
3764 O O   . ASN A 485 ? 0.7695 0.6696 0.8532 -0.1063 0.2107  0.2148  1022 ASN A O   
3765 C CB  . ASN A 485 ? 0.7564 0.6315 0.7689 -0.0783 0.2147  0.2280  1022 ASN A CB  
3766 C CG  . ASN A 485 ? 0.7660 0.6361 0.7395 -0.0616 0.2161  0.2328  1022 ASN A CG  
3767 O OD1 . ASN A 485 ? 0.7910 0.6377 0.7478 -0.0552 0.2126  0.2383  1022 ASN A OD1 
3768 N ND2 . ASN A 485 ? 0.7465 0.6378 0.7056 -0.0538 0.2206  0.2303  1022 ASN A ND2 
3769 N N   . CYS A 486 ? 0.7565 0.6602 0.8301 -0.0990 0.1953  0.1942  1023 CYS A N   
3770 C CA  . CYS A 486 ? 0.7643 0.6773 0.8750 -0.1136 0.1908  0.1871  1023 CYS A CA  
3771 C C   . CYS A 486 ? 0.7615 0.7060 0.8824 -0.1135 0.1950  0.1836  1023 CYS A C   
3772 O O   . CYS A 486 ? 0.7503 0.7073 0.8492 -0.1022 0.1965  0.1806  1023 CYS A O   
3773 C CB  . CYS A 486 ? 0.7462 0.6506 0.8639 -0.1167 0.1789  0.1744  1023 CYS A CB  
3774 S SG  . CYS A 486 ? 0.7166 0.6471 0.8328 -0.1134 0.1726  0.1602  1023 CYS A SG  
3775 N N   . LYS A 487 ? 0.7743 0.7307 0.9291 -0.1259 0.1966  0.1841  1024 LYS A N   
3776 C CA  . LYS A 487 ? 0.7708 0.7573 0.9408 -0.1260 0.2006  0.1807  1024 LYS A CA  
3777 C C   . LYS A 487 ? 0.7435 0.7423 0.9374 -0.1324 0.1891  0.1672  1024 LYS A C   
3778 O O   . LYS A 487 ? 0.7340 0.7569 0.9372 -0.1298 0.1905  0.1630  1024 LYS A O   
3779 C CB  . LYS A 487 ? 0.8012 0.7984 0.9946 -0.1344 0.2112  0.1905  1024 LYS A CB  
3780 C CG  . LYS A 487 ? 0.8374 0.8277 1.0061 -0.1271 0.2243  0.2045  1024 LYS A CG  
3781 C CD  . LYS A 487 ? 0.8686 0.8703 1.0615 -0.1370 0.2358  0.2151  1024 LYS A CD  
3782 C CE  . LYS A 487 ? 0.9010 0.8957 1.0675 -0.1299 0.2492  0.2297  1024 LYS A CE  
3783 N NZ  . LYS A 487 ? 0.9322 0.9375 1.1227 -0.1411 0.2615  0.2415  1024 LYS A NZ  
3784 N N   . GLN A 488 ? 0.7348 0.7171 0.9385 -0.1401 0.1775  0.1604  1025 GLN A N   
3785 C CA  . GLN A 488 ? 0.7227 0.7142 0.9458 -0.1459 0.1648  0.1469  1025 GLN A CA  
3786 C C   . GLN A 488 ? 0.7225 0.6918 0.9302 -0.1446 0.1556  0.1399  1025 GLN A C   
3787 O O   . GLN A 488 ? 0.7509 0.6955 0.9594 -0.1488 0.1537  0.1421  1025 GLN A O   
3788 C CB  . GLN A 488 ? 0.7504 0.7496 1.0156 -0.1611 0.1587  0.1432  1025 GLN A CB  
3789 C CG  . GLN A 488 ? 0.7474 0.7517 1.0332 -0.1682 0.1420  0.1279  1025 GLN A CG  
3790 C CD  . GLN A 488 ? 0.7774 0.7858 1.1031 -0.1832 0.1332  0.1230  1025 GLN A CD  
3791 O OE1 . GLN A 488 ? 0.8046 0.8134 1.1443 -0.1893 0.1410  0.1320  1025 GLN A OE1 
3792 N NE2 . GLN A 488 ? 0.7711 0.7829 1.1148 -0.1896 0.1160  0.1084  1025 GLN A NE2 
3793 N N   . PRO A 489 ? 0.6889 0.6661 0.8750 -0.1359 0.1455  0.1280  1026 PRO A N   
3794 C CA  . PRO A 489 ? 0.6695 0.6305 0.8309 -0.1304 0.1320  0.1163  1026 PRO A CA  
3795 C C   . PRO A 489 ? 0.6606 0.6088 0.8424 -0.1405 0.1187  0.1058  1026 PRO A C   
3796 O O   . PRO A 489 ? 0.6432 0.6033 0.8537 -0.1503 0.1114  0.0994  1026 PRO A O   
3797 C CB  . PRO A 489 ? 0.6537 0.6319 0.7979 -0.1233 0.1231  0.1057  1026 PRO A CB  
3798 C CG  . PRO A 489 ? 0.6472 0.6483 0.8145 -0.1270 0.1272  0.1083  1026 PRO A CG  
3799 C CD  . PRO A 489 ? 0.6666 0.6681 0.8491 -0.1300 0.1456  0.1246  1026 PRO A CD  
3800 N N   . PRO A 490 ? 0.6717 0.5952 0.8399 -0.1378 0.1145  0.1031  1027 PRO A N   
3801 C CA  . PRO A 490 ? 0.6709 0.5784 0.8567 -0.1463 0.1012  0.0918  1027 PRO A CA  
3802 C C   . PRO A 490 ? 0.6455 0.5659 0.8308 -0.1468 0.0840  0.0728  1027 PRO A C   
3803 O O   . PRO A 490 ? 0.6153 0.5502 0.7781 -0.1383 0.0810  0.0677  1027 PRO A O   
3804 C CB  . PRO A 490 ? 0.6898 0.5698 0.8521 -0.1378 0.1003  0.0915  1027 PRO A CB  
3805 C CG  . PRO A 490 ? 0.6986 0.5777 0.8424 -0.1295 0.1167  0.1090  1027 PRO A CG  
3806 C CD  . PRO A 490 ? 0.6818 0.5899 0.8196 -0.1262 0.1219  0.1109  1027 PRO A CD  
3807 N N   . ARG A 491 ? 0.6418 0.5553 0.8517 -0.1572 0.0719  0.0627  1028 ARG A N   
3808 C CA  . ARG A 491 ? 0.6113 0.5372 0.8238 -0.1590 0.0546  0.0453  1028 ARG A CA  
3809 C C   . ARG A 491 ? 0.5819 0.4928 0.7667 -0.1504 0.0428  0.0299  1028 ARG A C   
3810 O O   . ARG A 491 ? 0.6099 0.4958 0.7961 -0.1511 0.0390  0.0255  1028 ARG A O   
3811 C CB  . ARG A 491 ? 0.6320 0.5597 0.8853 -0.1742 0.0460  0.0408  1028 ARG A CB  
3812 C CG  . ARG A 491 ? 0.6307 0.5801 0.8917 -0.1763 0.0309  0.0277  1028 ARG A CG  
3813 C CD  . ARG A 491 ? 0.6660 0.6010 0.9276 -0.1793 0.0107  0.0081  1028 ARG A CD  
3814 N NE  . ARG A 491 ? 0.6995 0.6285 1.0027 -0.1947 0.0039  0.0059  1028 ARG A NE  
3815 C CZ  . ARG A 491 ? 0.7380 0.6427 1.0482 -0.1999 -0.0090 -0.0064 1028 ARG A CZ  
3816 N NH1 . ARG A 491 ? 0.7572 0.6420 1.0342 -0.1892 -0.0152 -0.0179 1028 ARG A NH1 
3817 N NH2 . ARG A 491 ? 0.7544 0.6546 1.1058 -0.2157 -0.0152 -0.0073 1028 ARG A NH2 
3818 N N   . PHE A 492 ? 0.5292 0.4552 0.6889 -0.1420 0.0371  0.0220  1029 PHE A N   
3819 C CA  . PHE A 492 ? 0.5139 0.4330 0.6460 -0.1329 0.0274  0.0077  1029 PHE A CA  
3820 C C   . PHE A 492 ? 0.5005 0.4349 0.6290 -0.1344 0.0125  -0.0063 1029 PHE A C   
3821 O O   . PHE A 492 ? 0.4690 0.4232 0.6048 -0.1377 0.0120  -0.0021 1029 PHE A O   
3822 C CB  . PHE A 492 ? 0.4839 0.4079 0.5841 -0.1204 0.0367  0.0136  1029 PHE A CB  
3823 C CG  . PHE A 492 ? 0.4714 0.3774 0.5671 -0.1154 0.0484  0.0244  1029 PHE A CG  
3824 C CD1 . PHE A 492 ? 0.4764 0.3621 0.5606 -0.1082 0.0447  0.0169  1029 PHE A CD1 
3825 C CD2 . PHE A 492 ? 0.4538 0.3633 0.5549 -0.1164 0.0627  0.0420  1029 PHE A CD2 
3826 C CE1 . PHE A 492 ? 0.4812 0.3491 0.5601 -0.1024 0.0542  0.0276  1029 PHE A CE1 
3827 C CE2 . PHE A 492 ? 0.4632 0.3555 0.5571 -0.1110 0.0727  0.0529  1029 PHE A CE2 
3828 C CZ  . PHE A 492 ? 0.4785 0.3495 0.5616 -0.1041 0.0680  0.0461  1029 PHE A CZ  
3829 N N   . PRO A 493 ? 0.5213 0.4466 0.6369 -0.1308 -0.0002 -0.0231 1030 PRO A N   
3830 C CA  . PRO A 493 ? 0.5221 0.4610 0.6308 -0.1316 -0.0151 -0.0362 1030 PRO A CA  
3831 C C   . PRO A 493 ? 0.5081 0.4682 0.5910 -0.1250 -0.0119 -0.0319 1030 PRO A C   
3832 O O   . PRO A 493 ? 0.4735 0.4358 0.5353 -0.1171 -0.0017 -0.0255 1030 PRO A O   
3833 C CB  . PRO A 493 ? 0.5356 0.4578 0.6298 -0.1261 -0.0265 -0.0546 1030 PRO A CB  
3834 C CG  . PRO A 493 ? 0.5429 0.4479 0.6270 -0.1184 -0.0155 -0.0500 1030 PRO A CG  
3835 C CD  . PRO A 493 ? 0.5423 0.4430 0.6494 -0.1253 -0.0023 -0.0314 1030 PRO A CD  
3836 N N   . ARG A 494 ? 0.5312 0.5066 0.6173 -0.1287 -0.0219 -0.0352 1031 ARG A N   
3837 C CA  . ARG A 494 ? 0.5409 0.5340 0.6037 -0.1240 -0.0212 -0.0309 1031 ARG A CA  
3838 C C   . ARG A 494 ? 0.5894 0.5829 0.6179 -0.1156 -0.0248 -0.0407 1031 ARG A C   
3839 O O   . ARG A 494 ? 0.5987 0.5842 0.6214 -0.1139 -0.0353 -0.0557 1031 ARG A O   
3840 C CB  . ARG A 494 ? 0.5164 0.5230 0.5918 -0.1294 -0.0329 -0.0324 1031 ARG A CB  
3841 C CG  . ARG A 494 ? 0.4954 0.5175 0.5524 -0.1261 -0.0318 -0.0245 1031 ARG A CG  
3842 C CD  . ARG A 494 ? 0.4717 0.5006 0.5452 -0.1277 -0.0204 -0.0095 1031 ARG A CD  
3843 N NE  . ARG A 494 ? 0.4601 0.4934 0.5706 -0.1346 -0.0233 -0.0082 1031 ARG A NE  
3844 C CZ  . ARG A 494 ? 0.4388 0.4848 0.5620 -0.1366 -0.0338 -0.0093 1031 ARG A CZ  
3845 N NH1 . ARG A 494 ? 0.4470 0.4993 0.5464 -0.1324 -0.0430 -0.0110 1031 ARG A NH1 
3846 N NH2 . ARG A 494 ? 0.4174 0.4703 0.5779 -0.1428 -0.0352 -0.0080 1031 ARG A NH2 
3847 N N   . LYS A 495 ? 0.6217 0.6255 0.6278 -0.1102 -0.0161 -0.0327 1032 LYS A N   
3848 C CA  . LYS A 495 ? 0.6665 0.6747 0.6421 -0.1022 -0.0163 -0.0398 1032 LYS A CA  
3849 C C   . LYS A 495 ? 0.6874 0.7082 0.6434 -0.1023 -0.0270 -0.0454 1032 LYS A C   
3850 O O   . LYS A 495 ? 0.7119 0.7348 0.6459 -0.0964 -0.0310 -0.0563 1032 LYS A O   
3851 C CB  . LYS A 495 ? 0.6776 0.6927 0.6398 -0.0974 -0.0026 -0.0286 1032 LYS A CB  
3852 C CG  . LYS A 495 ? 0.7241 0.7471 0.6594 -0.0892 -0.0005 -0.0351 1032 LYS A CG  
3853 C CD  . LYS A 495 ? 0.7465 0.7771 0.6738 -0.0851 0.0120  -0.0245 1032 LYS A CD  
3854 C CE  . LYS A 495 ? 0.7785 0.8232 0.6818 -0.0779 0.0144  -0.0299 1032 LYS A CE  
3855 N NZ  . LYS A 495 ? 0.7797 0.8340 0.6785 -0.0746 0.0251  -0.0201 1032 LYS A NZ  
3856 N N   . SER A 496 ? 0.6844 0.7136 0.6468 -0.1077 -0.0317 -0.0381 1033 SER A N   
3857 C CA  . SER A 496 ? 0.7003 0.7399 0.6426 -0.1075 -0.0424 -0.0409 1033 SER A CA  
3858 C C   . SER A 496 ? 0.7072 0.7460 0.6687 -0.1128 -0.0569 -0.0452 1033 SER A C   
3859 O O   . SER A 496 ? 0.7069 0.7412 0.6999 -0.1178 -0.0564 -0.0428 1033 SER A O   
3860 C CB  . SER A 496 ? 0.6927 0.7436 0.6191 -0.1078 -0.0360 -0.0268 1033 SER A CB  
3861 O OG  . SER A 496 ? 0.6865 0.7366 0.6340 -0.1117 -0.0318 -0.0154 1033 SER A OG  
3862 N N   . THR A 497 ? 0.7170 0.7619 0.6595 -0.1115 -0.0699 -0.0513 1034 THR A N   
3863 C CA  . THR A 497 ? 0.7198 0.7665 0.6778 -0.1153 -0.0863 -0.0559 1034 THR A CA  
3864 C C   . THR A 497 ? 0.6920 0.7483 0.6470 -0.1164 -0.0897 -0.0435 1034 THR A C   
3865 O O   . THR A 497 ? 0.6945 0.7541 0.6660 -0.1187 -0.1031 -0.0458 1034 THR A O   
3866 C CB  . THR A 497 ? 0.7587 0.8036 0.6974 -0.1120 -0.1020 -0.0728 1034 THR A CB  
3867 O OG1 . THR A 497 ? 0.7731 0.8226 0.6725 -0.1054 -0.0966 -0.0735 1034 THR A OG1 
3868 C CG2 . THR A 497 ? 0.7730 0.8047 0.7309 -0.1132 -0.1065 -0.0879 1034 THR A CG2 
3869 N N   . PHE A 498 ? 0.6579 0.7181 0.5936 -0.1148 -0.0790 -0.0310 1035 PHE A N   
3870 C CA  . PHE A 498 ? 0.6361 0.7014 0.5685 -0.1155 -0.0836 -0.0196 1035 PHE A CA  
3871 C C   . PHE A 498 ? 0.5823 0.6474 0.5463 -0.1178 -0.0767 -0.0108 1035 PHE A C   
3872 O O   . PHE A 498 ? 0.5734 0.6350 0.5582 -0.1193 -0.0662 -0.0112 1035 PHE A O   
3873 C CB  . PHE A 498 ? 0.6585 0.7270 0.5571 -0.1141 -0.0771 -0.0095 1035 PHE A CB  
3874 C CG  . PHE A 498 ? 0.6726 0.7412 0.5642 -0.1135 -0.0601 -0.0062 1035 PHE A CG  
3875 C CD1 . PHE A 498 ? 0.6698 0.7356 0.5793 -0.1147 -0.0484 0.0020  1035 PHE A CD1 
3876 C CD2 . PHE A 498 ? 0.6966 0.7696 0.5622 -0.1106 -0.0561 -0.0113 1035 PHE A CD2 
3877 C CE1 . PHE A 498 ? 0.6746 0.7412 0.5771 -0.1133 -0.0345 0.0049  1035 PHE A CE1 
3878 C CE2 . PHE A 498 ? 0.6973 0.7729 0.5583 -0.1091 -0.0415 -0.0086 1035 PHE A CE2 
3879 C CZ  . PHE A 498 ? 0.6892 0.7612 0.5688 -0.1107 -0.0314 -0.0004 1035 PHE A CZ  
3880 N N   . SER A 499 ? 0.5348 0.6033 0.5010 -0.1172 -0.0831 -0.0027 1036 SER A N   
3881 C CA  . SER A 499 ? 0.4567 0.5270 0.4520 -0.1174 -0.0780 0.0043  1036 SER A CA  
3882 C C   . SER A 499 ? 0.4458 0.5123 0.4367 -0.1168 -0.0603 0.0138  1036 SER A C   
3883 O O   . SER A 499 ? 0.4461 0.5100 0.4096 -0.1162 -0.0551 0.0185  1036 SER A O   
3884 C CB  . SER A 499 ? 0.4201 0.4937 0.4154 -0.1147 -0.0904 0.0098  1036 SER A CB  
3885 O OG  . SER A 499 ? 0.3865 0.4607 0.3986 -0.1126 -0.0824 0.0186  1036 SER A OG  
3886 N N   . LEU A 500 ? 0.4468 0.5143 0.4655 -0.1169 -0.0510 0.0165  1037 LEU A N   
3887 C CA  . LEU A 500 ? 0.4161 0.4803 0.4321 -0.1151 -0.0355 0.0252  1037 LEU A CA  
3888 C C   . LEU A 500 ? 0.4209 0.4847 0.4315 -0.1116 -0.0368 0.0340  1037 LEU A C   
3889 O O   . LEU A 500 ? 0.4113 0.4709 0.4129 -0.1097 -0.0265 0.0406  1037 LEU A O   
3890 C CB  . LEU A 500 ? 0.3881 0.4530 0.4331 -0.1160 -0.0242 0.0255  1037 LEU A CB  
3891 C CG  . LEU A 500 ? 0.3901 0.4509 0.4445 -0.1196 -0.0218 0.0180  1037 LEU A CG  
3892 C CD1 . LEU A 500 ? 0.3741 0.4344 0.4555 -0.1210 -0.0089 0.0225  1037 LEU A CD1 
3893 C CD2 . LEU A 500 ? 0.4031 0.4572 0.4291 -0.1182 -0.0176 0.0158  1037 LEU A CD2 
3894 N N   . LYS A 501 ? 0.4415 0.5086 0.4573 -0.1101 -0.0502 0.0336  1038 LYS A N   
3895 C CA  . LYS A 501 ? 0.4589 0.5230 0.4709 -0.1055 -0.0530 0.0411  1038 LYS A CA  
3896 C C   . LYS A 501 ? 0.4463 0.5009 0.4244 -0.1065 -0.0524 0.0479  1038 LYS A C   
3897 O O   . LYS A 501 ? 0.4658 0.5192 0.4214 -0.1097 -0.0590 0.0474  1038 LYS A O   
3898 C CB  . LYS A 501 ? 0.4960 0.5649 0.5192 -0.1027 -0.0696 0.0390  1038 LYS A CB  
3899 C CG  . LYS A 501 ? 0.5357 0.6156 0.5974 -0.0992 -0.0681 0.0369  1038 LYS A CG  
3900 C CD  . LYS A 501 ? 0.5886 0.6770 0.6658 -0.0967 -0.0863 0.0326  1038 LYS A CD  
3901 C CE  . LYS A 501 ? 0.6328 0.7127 0.6888 -0.0908 -0.0987 0.0386  1038 LYS A CE  
3902 N NZ  . LYS A 501 ? 0.6405 0.7158 0.7009 -0.0835 -0.0914 0.0451  1038 LYS A NZ  
3903 N N   . SER A 502 ? 0.4085 0.4569 0.3831 -0.1040 -0.0441 0.0542  1039 SER A N   
3904 C CA  . SER A 502 ? 0.4082 0.4472 0.3551 -0.1061 -0.0450 0.0614  1039 SER A CA  
3905 C C   . SER A 502 ? 0.4347 0.4669 0.3712 -0.1048 -0.0602 0.0659  1039 SER A C   
3906 O O   . SER A 502 ? 0.4490 0.4828 0.4030 -0.0993 -0.0682 0.0642  1039 SER A O   
3907 C CB  . SER A 502 ? 0.3961 0.4287 0.3434 -0.1032 -0.0349 0.0654  1039 SER A CB  
3908 O OG  . SER A 502 ? 0.4200 0.4428 0.3435 -0.1065 -0.0374 0.0722  1039 SER A OG  
3909 N N   . PRO A 503 ? 0.3902 0.4156 0.2991 -0.1097 -0.0645 0.0724  1040 PRO A N   
3910 C CA  . PRO A 503 ? 0.4100 0.4240 0.3063 -0.1085 -0.0782 0.0797  1040 PRO A CA  
3911 C C   . PRO A 503 ? 0.4511 0.4508 0.3482 -0.1050 -0.0777 0.0854  1040 PRO A C   
3912 O O   . PRO A 503 ? 0.4699 0.4569 0.3594 -0.1024 -0.0898 0.0913  1040 PRO A O   
3913 C CB  . PRO A 503 ? 0.4248 0.4376 0.2907 -0.1165 -0.0803 0.0859  1040 PRO A CB  
3914 C CG  . PRO A 503 ? 0.4102 0.4300 0.2730 -0.1213 -0.0653 0.0842  1040 PRO A CG  
3915 C CD  . PRO A 503 ? 0.4654 0.4941 0.3539 -0.1167 -0.0571 0.0740  1040 PRO A CD  
3916 N N   . GLY A 504 ? 0.3979 0.3979 0.3025 -0.1042 -0.0652 0.0835  1041 GLY A N   
3917 C CA  . GLY A 504 ? 0.4249 0.4112 0.3304 -0.0994 -0.0648 0.0863  1041 GLY A CA  
3918 C C   . GLY A 504 ? 0.4420 0.4143 0.3238 -0.1069 -0.0663 0.0945  1041 GLY A C   
3919 O O   . GLY A 504 ? 0.4549 0.4293 0.3193 -0.1162 -0.0675 0.0997  1041 GLY A O   
3920 N N   . ILE A 505 ? 0.4671 0.4252 0.3488 -0.1029 -0.0663 0.0953  1042 ILE A N   
3921 C CA  . ILE A 505 ? 0.5202 0.4637 0.3834 -0.1107 -0.0682 0.1021  1042 ILE A CA  
3922 C C   . ILE A 505 ? 0.5628 0.4830 0.4153 -0.1102 -0.0832 0.1094  1042 ILE A C   
3923 O O   . ILE A 505 ? 0.5896 0.4925 0.4303 -0.1155 -0.0867 0.1144  1042 ILE A O   
3924 C CB  . ILE A 505 ? 0.5363 0.4775 0.4032 -0.1078 -0.0591 0.0973  1042 ILE A CB  
3925 C CG1 . ILE A 505 ? 0.5474 0.4795 0.4265 -0.0938 -0.0607 0.0914  1042 ILE A CG1 
3926 C CG2 . ILE A 505 ? 0.5124 0.4742 0.3867 -0.1089 -0.0450 0.0922  1042 ILE A CG2 
3927 C CD1 . ILE A 505 ? 0.5444 0.4737 0.4237 -0.0890 -0.0522 0.0860  1042 ILE A CD1 
3928 N N   . ARG A 506 ? 0.5893 0.5077 0.4461 -0.1041 -0.0932 0.1101  1043 ARG A N   
3929 C CA  . ARG A 506 ? 0.6220 0.5167 0.4674 -0.1026 -0.1088 0.1181  1043 ARG A CA  
3930 C C   . ARG A 506 ? 0.6513 0.5442 0.4750 -0.1146 -0.1147 0.1296  1043 ARG A C   
3931 O O   . ARG A 506 ? 0.6453 0.5547 0.4689 -0.1150 -0.1149 0.1285  1043 ARG A O   
3932 C CB  . ARG A 506 ? 0.6272 0.5218 0.4890 -0.0880 -0.1176 0.1130  1043 ARG A CB  
3933 C CG  . ARG A 506 ? 0.6619 0.5329 0.5264 -0.0769 -0.1261 0.1120  1043 ARG A CG  
3934 C CD  . ARG A 506 ? 0.6513 0.5327 0.5384 -0.0639 -0.1162 0.0997  1043 ARG A CD  
3935 N NE  . ARG A 506 ? 0.6432 0.5469 0.5546 -0.0545 -0.1150 0.0932  1043 ARG A NE  
3936 C CZ  . ARG A 506 ? 0.6234 0.5524 0.5529 -0.0545 -0.1011 0.0863  1043 ARG A CZ  
3937 N NH1 . ARG A 506 ? 0.6107 0.5454 0.5350 -0.0617 -0.0873 0.0850  1043 ARG A NH1 
3938 N NH2 . ARG A 506 ? 0.6167 0.5651 0.5706 -0.0473 -0.1018 0.0811  1043 ARG A NH2 
3939 N N   . PRO A 507 ? 0.6956 0.5693 0.5006 -0.1246 -0.1196 0.1408  1044 PRO A N   
3940 C CA  . PRO A 507 ? 0.7377 0.6107 0.5206 -0.1361 -0.1239 0.1538  1044 PRO A CA  
3941 C C   . PRO A 507 ? 0.7887 0.6527 0.5653 -0.1287 -0.1389 0.1584  1044 PRO A C   
3942 O O   . PRO A 507 ? 0.7910 0.6437 0.5796 -0.1156 -0.1483 0.1537  1044 PRO A O   
3943 C CB  . PRO A 507 ? 0.7459 0.5966 0.5148 -0.1481 -0.1267 0.1653  1044 PRO A CB  
3944 C CG  . PRO A 507 ? 0.7272 0.5737 0.5106 -0.1444 -0.1210 0.1555  1044 PRO A CG  
3945 C CD  . PRO A 507 ? 0.7128 0.5645 0.5156 -0.1265 -0.1213 0.1423  1044 PRO A CD  
3946 N N   . ASN A 508 ? 0.8430 0.7137 0.5999 -0.1361 -0.1411 0.1673  1045 ASN A N   
3947 C CA  . ASN A 508 ? 0.9141 0.7765 0.6605 -0.1295 -0.1567 0.1729  1045 ASN A CA  
3948 C C   . ASN A 508 ? 0.9608 0.7993 0.6784 -0.1392 -0.1657 0.1925  1045 ASN A C   
3949 O O   . ASN A 508 ? 0.9870 0.7981 0.7024 -0.1410 -0.1719 0.1997  1045 ASN A O   
3950 C CB  . ASN A 508 ? 0.9340 0.8229 0.6786 -0.1276 -0.1545 0.1664  1045 ASN A CB  
3951 C CG  . ASN A 508 ? 0.9798 0.8766 0.6958 -0.1403 -0.1495 0.1770  1045 ASN A CG  
3952 O OD1 . ASN A 508 ? 0.9961 0.8961 0.7054 -0.1522 -0.1376 0.1824  1045 ASN A OD1 
3953 N ND2 . ASN A 508 ? 1.0017 0.9033 0.7007 -0.1372 -0.1587 0.1798  1045 ASN A ND2 
# 
