data_8XM4
# 
_entry.id   8XM4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8XM4         pdb_00008xm4 10.2210/pdb8xm4/pdb 
WWPDB D_1300043761 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XM4 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              zhuihao@mail.sysu.edu.cn 
_pdbx_contact_author.name_first         Huihao 
_pdbx_contact_author.name_last          Zhou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9675-5007 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lu, F.'   1 ? 
'Xia, K.'  2 ? 
'Yi, J.'   3 ? 
'Chen, B.' 4 ? 
'Luo, Z.'  5 ? 
'Xu, J.'   6 ? 
'Gu, Q.'   7 ? 
'Zhou, H.' 8 ? 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            268 
_citation.language                  ? 
_citation.page_first                116303 
_citation.page_last                 116303 
_citation.title                     
;Biochemical and structural characterization of chlorhexidine as an ATP-assisted inhibitor against type 1 methionyl-tRNA synthetase from Gram-positive bacteria.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116303 
_citation.pdbx_database_id_PubMed   38458107 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lu, F.'   1 ? 
primary 'Xia, K.'  2 ? 
primary 'Su, J.'   3 ? 
primary 'Yi, J.'   4 ? 
primary 'Luo, Z.'  5 ? 
primary 'Xu, J.'   6 ? 
primary 'Gu, Q.'   7 ? 
primary 'Chen, B.' 8 ? 
primary 'Zhou, H.' 9 ? 
# 
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 'Methionine--tRNA ligase' 61103.969 1   6.1.1.10 ? ? ? 
2 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE" 507.181   1   ?        ? ? ? 
3 non-polymer syn 
;1-[6-[azanylidene-[[azanylidene-[[(4-chlorophenyl)amino]methyl]-$l^{4}-azanyl]methyl]-$l^{4}-azanyl]hexyl]-3-[~{N}-(4-chlorophenyl)carbamimidoyl]guanidine
;
505.447   1   ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL 62.068    4   ?        ? ? ? 
5 water       nat water 18.015    312 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Methionyl-tRNA synthetase,MetRS' 
# 
_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       
;MGSSHHHHHHSAKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIE
YLDEMIAGIKQLWAKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDPQYENGKI
IGGKSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMINNFIKPGLADLAVSRTSFNWGVHVPSNP
KHVVYVWIDALVNYISALGYLSDDESLFNKYWPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWILMKDGKMS
KSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVNKYFDGELPAYQGPL
HELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKDDSQKDMLGNVMAHLVENIRYAAVL
LRPFLTHAPKEIFEQLNINNPQFMEFSSLEQYGVLNESIMVTGQPKPIFP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSAKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIE
YLDEMIAGIKQLWAKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDPQYENGKI
IGGKSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMINNFIKPGLADLAVSRTSFNWGVHVPSNP
KHVVYVWIDALVNYISALGYLSDDESLFNKYWPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWILMKDGKMS
KSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVNKYFDGELPAYQGPL
HELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKDDSQKDMLGNVMAHLVENIRYAAVL
LRPFLTHAPKEIFEQLNINNPQFMEFSSLEQYGVLNESIMVTGQPKPIFP
;
_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 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
3 
;1-[6-[azanylidene-[[azanylidene-[[(4-chlorophenyl)amino]methyl]-$l^{4}-azanyl]methyl]-$l^{4}-azanyl]hexyl]-3-[~{N}-(4-chlorophenyl)carbamimidoyl]guanidine
;
XC9 
4 1,2-ETHANEDIOL EDO 
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER 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  SER n 
1 12  ALA n 
1 13  LYS n 
1 14  GLU n 
1 15  THR n 
1 16  PHE n 
1 17  TYR n 
1 18  ILE n 
1 19  THR n 
1 20  THR n 
1 21  PRO n 
1 22  ILE n 
1 23  TYR n 
1 24  TYR n 
1 25  PRO n 
1 26  SER n 
1 27  GLY n 
1 28  ASN n 
1 29  LEU n 
1 30  HIS n 
1 31  ILE n 
1 32  GLY n 
1 33  HIS n 
1 34  ALA n 
1 35  TYR n 
1 36  SER n 
1 37  THR n 
1 38  VAL n 
1 39  ALA n 
1 40  GLY n 
1 41  ASP n 
1 42  VAL n 
1 43  ILE n 
1 44  ALA n 
1 45  ARG n 
1 46  TYR n 
1 47  LYS n 
1 48  ARG n 
1 49  MET n 
1 50  GLN n 
1 51  GLY n 
1 52  TYR n 
1 53  ASP n 
1 54  VAL n 
1 55  ARG n 
1 56  TYR n 
1 57  LEU n 
1 58  THR n 
1 59  GLY n 
1 60  THR n 
1 61  ASP n 
1 62  GLU n 
1 63  HIS n 
1 64  GLY n 
1 65  GLN n 
1 66  LYS n 
1 67  ILE n 
1 68  GLN n 
1 69  GLU n 
1 70  LYS n 
1 71  ALA n 
1 72  GLN n 
1 73  LYS n 
1 74  ALA n 
1 75  GLY n 
1 76  LYS n 
1 77  THR n 
1 78  GLU n 
1 79  ILE n 
1 80  GLU n 
1 81  TYR n 
1 82  LEU n 
1 83  ASP n 
1 84  GLU n 
1 85  MET n 
1 86  ILE n 
1 87  ALA n 
1 88  GLY n 
1 89  ILE n 
1 90  LYS n 
1 91  GLN n 
1 92  LEU n 
1 93  TRP n 
1 94  ALA n 
1 95  LYS n 
1 96  LEU n 
1 97  GLU n 
1 98  ILE n 
1 99  SER n 
1 100 ASN n 
1 101 ASP n 
1 102 ASP n 
1 103 PHE n 
1 104 ILE n 
1 105 ARG n 
1 106 THR n 
1 107 THR n 
1 108 GLU n 
1 109 GLU n 
1 110 ARG n 
1 111 HIS n 
1 112 LYS n 
1 113 HIS n 
1 114 VAL n 
1 115 VAL n 
1 116 GLU n 
1 117 GLN n 
1 118 VAL n 
1 119 PHE n 
1 120 GLU n 
1 121 ARG n 
1 122 LEU n 
1 123 LEU n 
1 124 LYS n 
1 125 GLN n 
1 126 GLY n 
1 127 ASP n 
1 128 ILE n 
1 129 TYR n 
1 130 LEU n 
1 131 GLY n 
1 132 GLU n 
1 133 TYR n 
1 134 GLU n 
1 135 GLY n 
1 136 TRP n 
1 137 TYR n 
1 138 SER n 
1 139 VAL n 
1 140 PRO n 
1 141 ASP n 
1 142 GLU n 
1 143 THR n 
1 144 TYR n 
1 145 TYR n 
1 146 THR n 
1 147 GLU n 
1 148 SER n 
1 149 GLN n 
1 150 LEU n 
1 151 VAL n 
1 152 ASP n 
1 153 PRO n 
1 154 GLN n 
1 155 TYR n 
1 156 GLU n 
1 157 ASN n 
1 158 GLY n 
1 159 LYS n 
1 160 ILE n 
1 161 ILE n 
1 162 GLY n 
1 163 GLY n 
1 164 LYS n 
1 165 SER n 
1 166 PRO n 
1 167 ASP n 
1 168 SER n 
1 169 GLY n 
1 170 HIS n 
1 171 GLU n 
1 172 VAL n 
1 173 GLU n 
1 174 LEU n 
1 175 VAL n 
1 176 LYS n 
1 177 GLU n 
1 178 GLU n 
1 179 SER n 
1 180 TYR n 
1 181 PHE n 
1 182 PHE n 
1 183 ASN n 
1 184 ILE n 
1 185 SER n 
1 186 LYS n 
1 187 TYR n 
1 188 THR n 
1 189 ASP n 
1 190 ARG n 
1 191 LEU n 
1 192 LEU n 
1 193 GLU n 
1 194 PHE n 
1 195 TYR n 
1 196 ASP n 
1 197 GLN n 
1 198 ASN n 
1 199 PRO n 
1 200 ASP n 
1 201 PHE n 
1 202 ILE n 
1 203 GLN n 
1 204 PRO n 
1 205 PRO n 
1 206 SER n 
1 207 ARG n 
1 208 LYS n 
1 209 ASN n 
1 210 GLU n 
1 211 MET n 
1 212 ILE n 
1 213 ASN n 
1 214 ASN n 
1 215 PHE n 
1 216 ILE n 
1 217 LYS n 
1 218 PRO n 
1 219 GLY n 
1 220 LEU n 
1 221 ALA n 
1 222 ASP n 
1 223 LEU n 
1 224 ALA n 
1 225 VAL n 
1 226 SER n 
1 227 ARG n 
1 228 THR n 
1 229 SER n 
1 230 PHE n 
1 231 ASN n 
1 232 TRP n 
1 233 GLY n 
1 234 VAL n 
1 235 HIS n 
1 236 VAL n 
1 237 PRO n 
1 238 SER n 
1 239 ASN n 
1 240 PRO n 
1 241 LYS n 
1 242 HIS n 
1 243 VAL n 
1 244 VAL n 
1 245 TYR n 
1 246 VAL n 
1 247 TRP n 
1 248 ILE n 
1 249 ASP n 
1 250 ALA n 
1 251 LEU n 
1 252 VAL n 
1 253 ASN n 
1 254 TYR n 
1 255 ILE n 
1 256 SER n 
1 257 ALA n 
1 258 LEU n 
1 259 GLY n 
1 260 TYR n 
1 261 LEU n 
1 262 SER n 
1 263 ASP n 
1 264 ASP n 
1 265 GLU n 
1 266 SER n 
1 267 LEU n 
1 268 PHE n 
1 269 ASN n 
1 270 LYS n 
1 271 TYR n 
1 272 TRP n 
1 273 PRO n 
1 274 ALA n 
1 275 ASP n 
1 276 ILE n 
1 277 HIS n 
1 278 LEU n 
1 279 MET n 
1 280 ALA n 
1 281 LYS n 
1 282 GLU n 
1 283 ILE n 
1 284 VAL n 
1 285 ARG n 
1 286 PHE n 
1 287 HIS n 
1 288 SER n 
1 289 ILE n 
1 290 ILE n 
1 291 TRP n 
1 292 PRO n 
1 293 ILE n 
1 294 LEU n 
1 295 LEU n 
1 296 MET n 
1 297 ALA n 
1 298 LEU n 
1 299 ASP n 
1 300 LEU n 
1 301 PRO n 
1 302 LEU n 
1 303 PRO n 
1 304 LYS n 
1 305 LYS n 
1 306 VAL n 
1 307 PHE n 
1 308 ALA n 
1 309 HIS n 
1 310 GLY n 
1 311 TRP n 
1 312 ILE n 
1 313 LEU n 
1 314 MET n 
1 315 LYS n 
1 316 ASP n 
1 317 GLY n 
1 318 LYS n 
1 319 MET n 
1 320 SER n 
1 321 LYS n 
1 322 SER n 
1 323 LYS n 
1 324 GLY n 
1 325 ASN n 
1 326 VAL n 
1 327 VAL n 
1 328 ASP n 
1 329 PRO n 
1 330 ASN n 
1 331 ILE n 
1 332 LEU n 
1 333 ILE n 
1 334 ASP n 
1 335 ARG n 
1 336 TYR n 
1 337 GLY n 
1 338 LEU n 
1 339 ASP n 
1 340 ALA n 
1 341 THR n 
1 342 ARG n 
1 343 TYR n 
1 344 TYR n 
1 345 LEU n 
1 346 MET n 
1 347 ARG n 
1 348 GLU n 
1 349 LEU n 
1 350 PRO n 
1 351 PHE n 
1 352 GLY n 
1 353 SER n 
1 354 ASP n 
1 355 GLY n 
1 356 VAL n 
1 357 PHE n 
1 358 THR n 
1 359 PRO n 
1 360 GLU n 
1 361 ALA n 
1 362 PHE n 
1 363 VAL n 
1 364 GLU n 
1 365 ARG n 
1 366 THR n 
1 367 ASN n 
1 368 PHE n 
1 369 ASP n 
1 370 LEU n 
1 371 ALA n 
1 372 ASN n 
1 373 ASP n 
1 374 LEU n 
1 375 GLY n 
1 376 ASN n 
1 377 LEU n 
1 378 VAL n 
1 379 ASN n 
1 380 ARG n 
1 381 THR n 
1 382 ILE n 
1 383 SER n 
1 384 MET n 
1 385 VAL n 
1 386 ASN n 
1 387 LYS n 
1 388 TYR n 
1 389 PHE n 
1 390 ASP n 
1 391 GLY n 
1 392 GLU n 
1 393 LEU n 
1 394 PRO n 
1 395 ALA n 
1 396 TYR n 
1 397 GLN n 
1 398 GLY n 
1 399 PRO n 
1 400 LEU n 
1 401 HIS n 
1 402 GLU n 
1 403 LEU n 
1 404 ASP n 
1 405 GLU n 
1 406 GLU n 
1 407 MET n 
1 408 GLU n 
1 409 ALA n 
1 410 MET n 
1 411 ALA n 
1 412 LEU n 
1 413 GLU n 
1 414 THR n 
1 415 VAL n 
1 416 LYS n 
1 417 SER n 
1 418 TYR n 
1 419 THR n 
1 420 GLU n 
1 421 SER n 
1 422 MET n 
1 423 GLU n 
1 424 SER n 
1 425 LEU n 
1 426 GLN n 
1 427 PHE n 
1 428 SER n 
1 429 VAL n 
1 430 ALA n 
1 431 LEU n 
1 432 SER n 
1 433 THR n 
1 434 VAL n 
1 435 TRP n 
1 436 LYS n 
1 437 PHE n 
1 438 ILE n 
1 439 SER n 
1 440 ARG n 
1 441 THR n 
1 442 ASN n 
1 443 LYS n 
1 444 TYR n 
1 445 ILE n 
1 446 ASP n 
1 447 GLU n 
1 448 THR n 
1 449 THR n 
1 450 PRO n 
1 451 TRP n 
1 452 VAL n 
1 453 LEU n 
1 454 ALA n 
1 455 LYS n 
1 456 ASP n 
1 457 ASP n 
1 458 SER n 
1 459 GLN n 
1 460 LYS n 
1 461 ASP n 
1 462 MET n 
1 463 LEU n 
1 464 GLY n 
1 465 ASN n 
1 466 VAL n 
1 467 MET n 
1 468 ALA n 
1 469 HIS n 
1 470 LEU n 
1 471 VAL n 
1 472 GLU n 
1 473 ASN n 
1 474 ILE n 
1 475 ARG n 
1 476 TYR n 
1 477 ALA n 
1 478 ALA n 
1 479 VAL n 
1 480 LEU n 
1 481 LEU n 
1 482 ARG n 
1 483 PRO n 
1 484 PHE n 
1 485 LEU n 
1 486 THR n 
1 487 HIS n 
1 488 ALA n 
1 489 PRO n 
1 490 LYS n 
1 491 GLU n 
1 492 ILE n 
1 493 PHE n 
1 494 GLU n 
1 495 GLN n 
1 496 LEU n 
1 497 ASN n 
1 498 ILE n 
1 499 ASN n 
1 500 ASN n 
1 501 PRO n 
1 502 GLN n 
1 503 PHE n 
1 504 MET n 
1 505 GLU n 
1 506 PHE n 
1 507 SER n 
1 508 SER n 
1 509 LEU n 
1 510 GLU n 
1 511 GLN n 
1 512 TYR n 
1 513 GLY n 
1 514 VAL n 
1 515 LEU n 
1 516 ASN n 
1 517 GLU n 
1 518 SER n 
1 519 ILE n 
1 520 MET n 
1 521 VAL n 
1 522 THR n 
1 523 GLY n 
1 524 GLN n 
1 525 PRO n 
1 526 LYS n 
1 527 PRO n 
1 528 ILE n 
1 529 PHE n 
1 530 PRO 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                   530 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 metG 
_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      'Staphylococcus aureus subsp. aureus COL' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     93062 
_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 
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 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ?                 'C10 H16 N5 O13 P3' 507.181 
EDO non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'          62.068  
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 
XC9 non-polymer         . 
;1-[6-[azanylidene-[[azanylidene-[[(4-chlorophenyl)amino]methyl]-$l^{4}-azanyl]methyl]-$l^{4}-azanyl]hexyl]-3-[~{N}-(4-chlorophenyl)carbamimidoyl]guanidine
;
?                 'C22 H30 Cl2 N10'   505.447 
# 
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   -9  ?   ?   ?   A . n 
A 1 2   GLY 2   -8  ?   ?   ?   A . n 
A 1 3   SER 3   -7  ?   ?   ?   A . n 
A 1 4   SER 4   -6  ?   ?   ?   A . n 
A 1 5   HIS 5   -5  ?   ?   ?   A . n 
A 1 6   HIS 6   -4  ?   ?   ?   A . n 
A 1 7   HIS 7   -3  ?   ?   ?   A . n 
A 1 8   HIS 8   -2  ?   ?   ?   A . n 
A 1 9   HIS 9   -1  ?   ?   ?   A . n 
A 1 10  HIS 10  0   ?   ?   ?   A . n 
A 1 11  SER 11  1   ?   ?   ?   A . n 
A 1 12  ALA 12  2   2   ALA ALA A . n 
A 1 13  LYS 13  3   3   LYS LYS A . n 
A 1 14  GLU 14  4   4   GLU GLU A . n 
A 1 15  THR 15  5   5   THR THR A . n 
A 1 16  PHE 16  6   6   PHE PHE A . n 
A 1 17  TYR 17  7   7   TYR TYR A . n 
A 1 18  ILE 18  8   8   ILE ILE A . n 
A 1 19  THR 19  9   9   THR THR A . n 
A 1 20  THR 20  10  10  THR THR A . n 
A 1 21  PRO 21  11  11  PRO PRO A . n 
A 1 22  ILE 22  12  12  ILE ILE A . n 
A 1 23  TYR 23  13  13  TYR TYR A . n 
A 1 24  TYR 24  14  14  TYR TYR A . n 
A 1 25  PRO 25  15  15  PRO PRO A . n 
A 1 26  SER 26  16  16  SER SER A . n 
A 1 27  GLY 27  17  17  GLY GLY A . n 
A 1 28  ASN 28  18  18  ASN ASN A . n 
A 1 29  LEU 29  19  19  LEU LEU A . n 
A 1 30  HIS 30  20  20  HIS HIS A . n 
A 1 31  ILE 31  21  21  ILE ILE A . n 
A 1 32  GLY 32  22  22  GLY GLY A . n 
A 1 33  HIS 33  23  23  HIS HIS A . n 
A 1 34  ALA 34  24  24  ALA ALA A . n 
A 1 35  TYR 35  25  25  TYR TYR A . n 
A 1 36  SER 36  26  26  SER SER A . n 
A 1 37  THR 37  27  27  THR THR A . n 
A 1 38  VAL 38  28  28  VAL VAL A . n 
A 1 39  ALA 39  29  29  ALA ALA A . n 
A 1 40  GLY 40  30  30  GLY GLY A . n 
A 1 41  ASP 41  31  31  ASP ASP A . n 
A 1 42  VAL 42  32  32  VAL VAL A . n 
A 1 43  ILE 43  33  33  ILE ILE A . n 
A 1 44  ALA 44  34  34  ALA ALA A . n 
A 1 45  ARG 45  35  35  ARG ARG A . n 
A 1 46  TYR 46  36  36  TYR TYR A . n 
A 1 47  LYS 47  37  37  LYS LYS A . n 
A 1 48  ARG 48  38  38  ARG ARG A . n 
A 1 49  MET 49  39  39  MET MET A . n 
A 1 50  GLN 50  40  40  GLN GLN A . n 
A 1 51  GLY 51  41  41  GLY GLY A . n 
A 1 52  TYR 52  42  42  TYR TYR A . n 
A 1 53  ASP 53  43  43  ASP ASP A . n 
A 1 54  VAL 54  44  44  VAL VAL A . n 
A 1 55  ARG 55  45  45  ARG ARG A . n 
A 1 56  TYR 56  46  46  TYR TYR A . n 
A 1 57  LEU 57  47  47  LEU LEU A . n 
A 1 58  THR 58  48  48  THR THR A . n 
A 1 59  GLY 59  49  49  GLY GLY A . n 
A 1 60  THR 60  50  50  THR THR A . n 
A 1 61  ASP 61  51  51  ASP ASP A . n 
A 1 62  GLU 62  52  52  GLU GLU A . n 
A 1 63  HIS 63  53  53  HIS HIS A . n 
A 1 64  GLY 64  54  54  GLY GLY A . n 
A 1 65  GLN 65  55  55  GLN GLN A . n 
A 1 66  LYS 66  56  56  LYS LYS A . n 
A 1 67  ILE 67  57  57  ILE ILE A . n 
A 1 68  GLN 68  58  58  GLN GLN A . n 
A 1 69  GLU 69  59  59  GLU GLU A . n 
A 1 70  LYS 70  60  60  LYS LYS A . n 
A 1 71  ALA 71  61  61  ALA ALA A . n 
A 1 72  GLN 72  62  62  GLN GLN A . n 
A 1 73  LYS 73  63  63  LYS LYS A . n 
A 1 74  ALA 74  64  64  ALA ALA A . n 
A 1 75  GLY 75  65  65  GLY GLY A . n 
A 1 76  LYS 76  66  66  LYS LYS A . n 
A 1 77  THR 77  67  67  THR THR A . n 
A 1 78  GLU 78  68  68  GLU GLU A . n 
A 1 79  ILE 79  69  69  ILE ILE A . n 
A 1 80  GLU 80  70  70  GLU GLU A . n 
A 1 81  TYR 81  71  71  TYR TYR A . n 
A 1 82  LEU 82  72  72  LEU LEU A . n 
A 1 83  ASP 83  73  73  ASP ASP A . n 
A 1 84  GLU 84  74  74  GLU GLU A . n 
A 1 85  MET 85  75  75  MET MET A . n 
A 1 86  ILE 86  76  76  ILE ILE A . n 
A 1 87  ALA 87  77  77  ALA ALA A . n 
A 1 88  GLY 88  78  78  GLY GLY A . n 
A 1 89  ILE 89  79  79  ILE ILE A . n 
A 1 90  LYS 90  80  80  LYS LYS A . n 
A 1 91  GLN 91  81  81  GLN GLN A . n 
A 1 92  LEU 92  82  82  LEU LEU A . n 
A 1 93  TRP 93  83  83  TRP TRP A . n 
A 1 94  ALA 94  84  84  ALA ALA A . n 
A 1 95  LYS 95  85  85  LYS LYS A . n 
A 1 96  LEU 96  86  86  LEU LEU A . n 
A 1 97  GLU 97  87  87  GLU GLU A . n 
A 1 98  ILE 98  88  88  ILE ILE A . n 
A 1 99  SER 99  89  89  SER SER A . n 
A 1 100 ASN 100 90  90  ASN ASN A . n 
A 1 101 ASP 101 91  91  ASP ASP A . n 
A 1 102 ASP 102 92  92  ASP ASP A . n 
A 1 103 PHE 103 93  93  PHE PHE A . n 
A 1 104 ILE 104 94  94  ILE ILE A . n 
A 1 105 ARG 105 95  95  ARG ARG A . n 
A 1 106 THR 106 96  96  THR THR A . n 
A 1 107 THR 107 97  97  THR THR A . n 
A 1 108 GLU 108 98  98  GLU GLU A . n 
A 1 109 GLU 109 99  99  GLU GLU A . n 
A 1 110 ARG 110 100 100 ARG ARG A . n 
A 1 111 HIS 111 101 101 HIS HIS A . n 
A 1 112 LYS 112 102 102 LYS LYS A . n 
A 1 113 HIS 113 103 103 HIS HIS A . n 
A 1 114 VAL 114 104 104 VAL VAL A . n 
A 1 115 VAL 115 105 105 VAL VAL A . n 
A 1 116 GLU 116 106 106 GLU GLU A . n 
A 1 117 GLN 117 107 107 GLN GLN A . n 
A 1 118 VAL 118 108 108 VAL VAL A . n 
A 1 119 PHE 119 109 109 PHE PHE A . n 
A 1 120 GLU 120 110 110 GLU GLU A . n 
A 1 121 ARG 121 111 111 ARG ARG A . n 
A 1 122 LEU 122 112 112 LEU LEU A . n 
A 1 123 LEU 123 113 113 LEU LEU A . n 
A 1 124 LYS 124 114 114 LYS LYS A . n 
A 1 125 GLN 125 115 115 GLN GLN A . n 
A 1 126 GLY 126 116 116 GLY GLY A . n 
A 1 127 ASP 127 117 117 ASP ASP A . n 
A 1 128 ILE 128 118 118 ILE ILE A . n 
A 1 129 TYR 129 119 119 TYR TYR A . n 
A 1 130 LEU 130 120 120 LEU LEU A . n 
A 1 131 GLY 131 121 121 GLY GLY A . n 
A 1 132 GLU 132 122 122 GLU GLU A . n 
A 1 133 TYR 133 123 123 TYR TYR A . n 
A 1 134 GLU 134 124 124 GLU GLU A . n 
A 1 135 GLY 135 125 125 GLY GLY A . n 
A 1 136 TRP 136 126 126 TRP TRP A . n 
A 1 137 TYR 137 127 127 TYR TYR A . n 
A 1 138 SER 138 128 128 SER SER A . n 
A 1 139 VAL 139 129 129 VAL VAL A . n 
A 1 140 PRO 140 130 130 PRO PRO A . n 
A 1 141 ASP 141 131 131 ASP ASP A . n 
A 1 142 GLU 142 132 132 GLU GLU A . n 
A 1 143 THR 143 133 133 THR THR A . n 
A 1 144 TYR 144 134 134 TYR TYR A . n 
A 1 145 TYR 145 135 135 TYR TYR A . n 
A 1 146 THR 146 136 136 THR THR A . n 
A 1 147 GLU 147 137 137 GLU GLU A . n 
A 1 148 SER 148 138 138 SER SER A . n 
A 1 149 GLN 149 139 139 GLN GLN A . n 
A 1 150 LEU 150 140 140 LEU LEU A . n 
A 1 151 VAL 151 141 141 VAL VAL A . n 
A 1 152 ASP 152 142 142 ASP ASP A . n 
A 1 153 PRO 153 143 143 PRO PRO A . n 
A 1 154 GLN 154 144 144 GLN GLN A . n 
A 1 155 TYR 155 145 145 TYR TYR A . n 
A 1 156 GLU 156 146 146 GLU GLU A . n 
A 1 157 ASN 157 147 147 ASN ASN A . n 
A 1 158 GLY 158 148 148 GLY GLY A . n 
A 1 159 LYS 159 149 149 LYS LYS A . n 
A 1 160 ILE 160 150 150 ILE ILE A . n 
A 1 161 ILE 161 151 151 ILE ILE A . n 
A 1 162 GLY 162 152 152 GLY GLY A . n 
A 1 163 GLY 163 153 153 GLY GLY A . n 
A 1 164 LYS 164 154 154 LYS LYS A . n 
A 1 165 SER 165 155 155 SER SER A . n 
A 1 166 PRO 166 156 156 PRO PRO A . n 
A 1 167 ASP 167 157 157 ASP ASP A . n 
A 1 168 SER 168 158 158 SER SER A . n 
A 1 169 GLY 169 159 159 GLY GLY A . n 
A 1 170 HIS 170 160 160 HIS HIS A . n 
A 1 171 GLU 171 161 161 GLU GLU A . n 
A 1 172 VAL 172 162 162 VAL VAL A . n 
A 1 173 GLU 173 163 163 GLU GLU A . n 
A 1 174 LEU 174 164 164 LEU LEU A . n 
A 1 175 VAL 175 165 165 VAL VAL A . n 
A 1 176 LYS 176 166 166 LYS LYS A . n 
A 1 177 GLU 177 167 167 GLU GLU A . n 
A 1 178 GLU 178 168 168 GLU GLU A . n 
A 1 179 SER 179 169 169 SER SER A . n 
A 1 180 TYR 180 170 170 TYR TYR A . n 
A 1 181 PHE 181 171 171 PHE PHE A . n 
A 1 182 PHE 182 172 172 PHE PHE A . n 
A 1 183 ASN 183 173 173 ASN ASN A . n 
A 1 184 ILE 184 174 174 ILE ILE A . n 
A 1 185 SER 185 175 175 SER SER A . n 
A 1 186 LYS 186 176 176 LYS LYS A . n 
A 1 187 TYR 187 177 177 TYR TYR A . n 
A 1 188 THR 188 178 178 THR THR A . n 
A 1 189 ASP 189 179 179 ASP ASP A . n 
A 1 190 ARG 190 180 180 ARG ARG A . n 
A 1 191 LEU 191 181 181 LEU LEU A . n 
A 1 192 LEU 192 182 182 LEU LEU A . n 
A 1 193 GLU 193 183 183 GLU GLU A . n 
A 1 194 PHE 194 184 184 PHE PHE A . n 
A 1 195 TYR 195 185 185 TYR TYR A . n 
A 1 196 ASP 196 186 186 ASP ASP A . n 
A 1 197 GLN 197 187 187 GLN GLN A . n 
A 1 198 ASN 198 188 188 ASN ASN A . n 
A 1 199 PRO 199 189 189 PRO PRO A . n 
A 1 200 ASP 200 190 190 ASP ASP A . n 
A 1 201 PHE 201 191 191 PHE PHE A . n 
A 1 202 ILE 202 192 192 ILE ILE A . n 
A 1 203 GLN 203 193 193 GLN GLN A . n 
A 1 204 PRO 204 194 194 PRO PRO A . n 
A 1 205 PRO 205 195 195 PRO PRO A . n 
A 1 206 SER 206 196 196 SER SER A . n 
A 1 207 ARG 207 197 197 ARG ARG A . n 
A 1 208 LYS 208 198 198 LYS LYS A . n 
A 1 209 ASN 209 199 199 ASN ASN A . n 
A 1 210 GLU 210 200 200 GLU GLU A . n 
A 1 211 MET 211 201 201 MET MET A . n 
A 1 212 ILE 212 202 202 ILE ILE A . n 
A 1 213 ASN 213 203 203 ASN ASN A . n 
A 1 214 ASN 214 204 204 ASN ASN A . n 
A 1 215 PHE 215 205 205 PHE PHE A . n 
A 1 216 ILE 216 206 206 ILE ILE A . n 
A 1 217 LYS 217 207 207 LYS LYS A . n 
A 1 218 PRO 218 208 208 PRO PRO A . n 
A 1 219 GLY 219 209 209 GLY GLY A . n 
A 1 220 LEU 220 210 210 LEU LEU A . n 
A 1 221 ALA 221 211 211 ALA ALA A . n 
A 1 222 ASP 222 212 212 ASP ASP A . n 
A 1 223 LEU 223 213 213 LEU LEU A . n 
A 1 224 ALA 224 214 214 ALA ALA A . n 
A 1 225 VAL 225 215 215 VAL VAL A . n 
A 1 226 SER 226 216 216 SER SER A . n 
A 1 227 ARG 227 217 217 ARG ARG A . n 
A 1 228 THR 228 218 218 THR THR A . n 
A 1 229 SER 229 219 219 SER SER A . n 
A 1 230 PHE 230 220 220 PHE PHE A . n 
A 1 231 ASN 231 221 221 ASN ASN A . n 
A 1 232 TRP 232 222 222 TRP TRP A . n 
A 1 233 GLY 233 223 223 GLY GLY A . n 
A 1 234 VAL 234 224 224 VAL VAL A . n 
A 1 235 HIS 235 225 225 HIS HIS A . n 
A 1 236 VAL 236 226 226 VAL VAL A . n 
A 1 237 PRO 237 227 227 PRO PRO A . n 
A 1 238 SER 238 228 228 SER SER A . n 
A 1 239 ASN 239 229 229 ASN ASN A . n 
A 1 240 PRO 240 230 230 PRO PRO A . n 
A 1 241 LYS 241 231 231 LYS LYS A . n 
A 1 242 HIS 242 232 232 HIS HIS A . n 
A 1 243 VAL 243 233 233 VAL VAL A . n 
A 1 244 VAL 244 234 234 VAL VAL A . n 
A 1 245 TYR 245 235 235 TYR TYR A . n 
A 1 246 VAL 246 236 236 VAL VAL A . n 
A 1 247 TRP 247 237 237 TRP TRP A . n 
A 1 248 ILE 248 238 238 ILE ILE A . n 
A 1 249 ASP 249 239 239 ASP ASP A . n 
A 1 250 ALA 250 240 240 ALA ALA A . n 
A 1 251 LEU 251 241 241 LEU LEU A . n 
A 1 252 VAL 252 242 242 VAL VAL A . n 
A 1 253 ASN 253 243 243 ASN ASN A . n 
A 1 254 TYR 254 244 244 TYR TYR A . n 
A 1 255 ILE 255 245 245 ILE ILE A . n 
A 1 256 SER 256 246 246 SER SER A . n 
A 1 257 ALA 257 247 247 ALA ALA A . n 
A 1 258 LEU 258 248 248 LEU LEU A . n 
A 1 259 GLY 259 249 249 GLY GLY A . n 
A 1 260 TYR 260 250 250 TYR TYR A . n 
A 1 261 LEU 261 251 251 LEU LEU A . n 
A 1 262 SER 262 252 252 SER SER A . n 
A 1 263 ASP 263 253 253 ASP ASP A . n 
A 1 264 ASP 264 254 254 ASP ASP A . n 
A 1 265 GLU 265 255 255 GLU GLU A . n 
A 1 266 SER 266 256 256 SER SER A . n 
A 1 267 LEU 267 257 257 LEU LEU A . n 
A 1 268 PHE 268 258 258 PHE PHE A . n 
A 1 269 ASN 269 259 259 ASN ASN A . n 
A 1 270 LYS 270 260 260 LYS LYS A . n 
A 1 271 TYR 271 261 261 TYR TYR A . n 
A 1 272 TRP 272 262 262 TRP TRP A . n 
A 1 273 PRO 273 263 263 PRO PRO A . n 
A 1 274 ALA 274 264 264 ALA ALA A . n 
A 1 275 ASP 275 265 265 ASP ASP A . n 
A 1 276 ILE 276 266 266 ILE ILE A . n 
A 1 277 HIS 277 267 267 HIS HIS A . n 
A 1 278 LEU 278 268 268 LEU LEU A . n 
A 1 279 MET 279 269 269 MET MET A . n 
A 1 280 ALA 280 270 270 ALA ALA A . n 
A 1 281 LYS 281 271 271 LYS LYS A . n 
A 1 282 GLU 282 272 272 GLU GLU A . n 
A 1 283 ILE 283 273 273 ILE ILE A . n 
A 1 284 VAL 284 274 274 VAL VAL A . n 
A 1 285 ARG 285 275 275 ARG ARG A . n 
A 1 286 PHE 286 276 276 PHE PHE A . n 
A 1 287 HIS 287 277 277 HIS HIS A . n 
A 1 288 SER 288 278 278 SER SER A . n 
A 1 289 ILE 289 279 279 ILE ILE A . n 
A 1 290 ILE 290 280 280 ILE ILE A . n 
A 1 291 TRP 291 281 281 TRP TRP A . n 
A 1 292 PRO 292 282 282 PRO PRO A . n 
A 1 293 ILE 293 283 283 ILE ILE A . n 
A 1 294 LEU 294 284 284 LEU LEU A . n 
A 1 295 LEU 295 285 285 LEU LEU A . n 
A 1 296 MET 296 286 286 MET MET A . n 
A 1 297 ALA 297 287 287 ALA ALA A . n 
A 1 298 LEU 298 288 288 LEU LEU A . n 
A 1 299 ASP 299 289 289 ASP ASP A . n 
A 1 300 LEU 300 290 290 LEU LEU A . n 
A 1 301 PRO 301 291 291 PRO PRO A . n 
A 1 302 LEU 302 292 292 LEU LEU A . n 
A 1 303 PRO 303 293 293 PRO PRO A . n 
A 1 304 LYS 304 294 294 LYS LYS A . n 
A 1 305 LYS 305 295 295 LYS LYS A . n 
A 1 306 VAL 306 296 296 VAL VAL A . n 
A 1 307 PHE 307 297 297 PHE PHE A . n 
A 1 308 ALA 308 298 298 ALA ALA A . n 
A 1 309 HIS 309 299 299 HIS HIS A . n 
A 1 310 GLY 310 300 300 GLY GLY A . n 
A 1 311 TRP 311 301 301 TRP TRP A . n 
A 1 312 ILE 312 302 302 ILE ILE A . n 
A 1 313 LEU 313 303 303 LEU LEU A . n 
A 1 314 MET 314 304 304 MET MET A . n 
A 1 315 LYS 315 305 305 LYS LYS A . n 
A 1 316 ASP 316 306 306 ASP ASP A . n 
A 1 317 GLY 317 307 307 GLY GLY A . n 
A 1 318 LYS 318 308 308 LYS LYS A . n 
A 1 319 MET 319 309 309 MET MET A . n 
A 1 320 SER 320 310 310 SER SER A . n 
A 1 321 LYS 321 311 311 LYS LYS A . n 
A 1 322 SER 322 312 312 SER SER A . n 
A 1 323 LYS 323 313 313 LYS LYS A . n 
A 1 324 GLY 324 314 314 GLY GLY A . n 
A 1 325 ASN 325 315 315 ASN ASN A . n 
A 1 326 VAL 326 316 316 VAL VAL A . n 
A 1 327 VAL 327 317 317 VAL VAL A . n 
A 1 328 ASP 328 318 318 ASP ASP A . n 
A 1 329 PRO 329 319 319 PRO PRO A . n 
A 1 330 ASN 330 320 320 ASN ASN A . n 
A 1 331 ILE 331 321 321 ILE ILE A . n 
A 1 332 LEU 332 322 322 LEU LEU A . n 
A 1 333 ILE 333 323 323 ILE ILE A . n 
A 1 334 ASP 334 324 324 ASP ASP A . n 
A 1 335 ARG 335 325 325 ARG ARG A . n 
A 1 336 TYR 336 326 326 TYR TYR A . n 
A 1 337 GLY 337 327 327 GLY GLY A . n 
A 1 338 LEU 338 328 328 LEU LEU A . n 
A 1 339 ASP 339 329 329 ASP ASP A . n 
A 1 340 ALA 340 330 330 ALA ALA A . n 
A 1 341 THR 341 331 331 THR THR A . n 
A 1 342 ARG 342 332 332 ARG ARG A . n 
A 1 343 TYR 343 333 333 TYR TYR A . n 
A 1 344 TYR 344 334 334 TYR TYR A . n 
A 1 345 LEU 345 335 335 LEU LEU A . n 
A 1 346 MET 346 336 336 MET MET A . n 
A 1 347 ARG 347 337 337 ARG ARG A . n 
A 1 348 GLU 348 338 338 GLU GLU A . n 
A 1 349 LEU 349 339 339 LEU LEU A . n 
A 1 350 PRO 350 340 340 PRO PRO A . n 
A 1 351 PHE 351 341 341 PHE PHE A . n 
A 1 352 GLY 352 342 342 GLY GLY A . n 
A 1 353 SER 353 343 343 SER SER A . n 
A 1 354 ASP 354 344 344 ASP ASP A . n 
A 1 355 GLY 355 345 345 GLY GLY A . n 
A 1 356 VAL 356 346 346 VAL VAL A . n 
A 1 357 PHE 357 347 347 PHE PHE A . n 
A 1 358 THR 358 348 348 THR THR A . n 
A 1 359 PRO 359 349 349 PRO PRO A . n 
A 1 360 GLU 360 350 350 GLU GLU A . n 
A 1 361 ALA 361 351 351 ALA ALA A . n 
A 1 362 PHE 362 352 352 PHE PHE A . n 
A 1 363 VAL 363 353 353 VAL VAL A . n 
A 1 364 GLU 364 354 354 GLU GLU A . n 
A 1 365 ARG 365 355 355 ARG ARG A . n 
A 1 366 THR 366 356 356 THR THR A . n 
A 1 367 ASN 367 357 357 ASN ASN A . n 
A 1 368 PHE 368 358 358 PHE PHE A . n 
A 1 369 ASP 369 359 359 ASP ASP A . n 
A 1 370 LEU 370 360 360 LEU LEU A . n 
A 1 371 ALA 371 361 361 ALA ALA A . n 
A 1 372 ASN 372 362 362 ASN ASN A . n 
A 1 373 ASP 373 363 363 ASP ASP A . n 
A 1 374 LEU 374 364 364 LEU LEU A . n 
A 1 375 GLY 375 365 365 GLY GLY A . n 
A 1 376 ASN 376 366 366 ASN ASN A . n 
A 1 377 LEU 377 367 367 LEU LEU A . n 
A 1 378 VAL 378 368 368 VAL VAL A . n 
A 1 379 ASN 379 369 369 ASN ASN A . n 
A 1 380 ARG 380 370 370 ARG ARG A . n 
A 1 381 THR 381 371 371 THR THR A . n 
A 1 382 ILE 382 372 372 ILE ILE A . n 
A 1 383 SER 383 373 373 SER SER A . n 
A 1 384 MET 384 374 374 MET MET A . n 
A 1 385 VAL 385 375 375 VAL VAL A . n 
A 1 386 ASN 386 376 376 ASN ASN A . n 
A 1 387 LYS 387 377 377 LYS LYS A . n 
A 1 388 TYR 388 378 378 TYR TYR A . n 
A 1 389 PHE 389 379 379 PHE PHE A . n 
A 1 390 ASP 390 380 380 ASP ASP A . n 
A 1 391 GLY 391 381 381 GLY GLY A . n 
A 1 392 GLU 392 382 382 GLU GLU A . n 
A 1 393 LEU 393 383 383 LEU LEU A . n 
A 1 394 PRO 394 384 384 PRO PRO A . n 
A 1 395 ALA 395 385 385 ALA ALA A . n 
A 1 396 TYR 396 386 386 TYR TYR A . n 
A 1 397 GLN 397 387 387 GLN GLN A . n 
A 1 398 GLY 398 388 388 GLY GLY A . n 
A 1 399 PRO 399 389 389 PRO PRO A . n 
A 1 400 LEU 400 390 390 LEU LEU A . n 
A 1 401 HIS 401 391 391 HIS HIS A . n 
A 1 402 GLU 402 392 392 GLU GLU A . n 
A 1 403 LEU 403 393 393 LEU LEU A . n 
A 1 404 ASP 404 394 394 ASP ASP A . n 
A 1 405 GLU 405 395 395 GLU GLU A . n 
A 1 406 GLU 406 396 396 GLU GLU A . n 
A 1 407 MET 407 397 397 MET MET A . n 
A 1 408 GLU 408 398 398 GLU GLU A . n 
A 1 409 ALA 409 399 399 ALA ALA A . n 
A 1 410 MET 410 400 400 MET MET A . n 
A 1 411 ALA 411 401 401 ALA ALA A . n 
A 1 412 LEU 412 402 402 LEU LEU A . n 
A 1 413 GLU 413 403 403 GLU GLU A . n 
A 1 414 THR 414 404 404 THR THR A . n 
A 1 415 VAL 415 405 405 VAL VAL A . n 
A 1 416 LYS 416 406 406 LYS LYS A . n 
A 1 417 SER 417 407 407 SER SER A . n 
A 1 418 TYR 418 408 408 TYR TYR A . n 
A 1 419 THR 419 409 409 THR THR A . n 
A 1 420 GLU 420 410 410 GLU GLU A . n 
A 1 421 SER 421 411 411 SER SER A . n 
A 1 422 MET 422 412 412 MET MET A . n 
A 1 423 GLU 423 413 413 GLU GLU A . n 
A 1 424 SER 424 414 414 SER SER A . n 
A 1 425 LEU 425 415 415 LEU LEU A . n 
A 1 426 GLN 426 416 416 GLN GLN A . n 
A 1 427 PHE 427 417 417 PHE PHE A . n 
A 1 428 SER 428 418 418 SER SER A . n 
A 1 429 VAL 429 419 419 VAL VAL A . n 
A 1 430 ALA 430 420 420 ALA ALA A . n 
A 1 431 LEU 431 421 421 LEU LEU A . n 
A 1 432 SER 432 422 422 SER SER A . n 
A 1 433 THR 433 423 423 THR THR A . n 
A 1 434 VAL 434 424 424 VAL VAL A . n 
A 1 435 TRP 435 425 425 TRP TRP A . n 
A 1 436 LYS 436 426 426 LYS LYS A . n 
A 1 437 PHE 437 427 427 PHE PHE A . n 
A 1 438 ILE 438 428 428 ILE ILE A . n 
A 1 439 SER 439 429 429 SER SER A . n 
A 1 440 ARG 440 430 430 ARG ARG A . n 
A 1 441 THR 441 431 431 THR THR A . n 
A 1 442 ASN 442 432 432 ASN ASN A . n 
A 1 443 LYS 443 433 433 LYS LYS A . n 
A 1 444 TYR 444 434 434 TYR TYR A . n 
A 1 445 ILE 445 435 435 ILE ILE A . n 
A 1 446 ASP 446 436 436 ASP ASP A . n 
A 1 447 GLU 447 437 437 GLU GLU A . n 
A 1 448 THR 448 438 438 THR THR A . n 
A 1 449 THR 449 439 439 THR THR A . n 
A 1 450 PRO 450 440 440 PRO PRO A . n 
A 1 451 TRP 451 441 441 TRP TRP A . n 
A 1 452 VAL 452 442 442 VAL VAL A . n 
A 1 453 LEU 453 443 443 LEU LEU A . n 
A 1 454 ALA 454 444 444 ALA ALA A . n 
A 1 455 LYS 455 445 445 LYS LYS A . n 
A 1 456 ASP 456 446 446 ASP ASP A . n 
A 1 457 ASP 457 447 447 ASP ASP A . n 
A 1 458 SER 458 448 448 SER SER A . n 
A 1 459 GLN 459 449 449 GLN GLN A . n 
A 1 460 LYS 460 450 450 LYS LYS A . n 
A 1 461 ASP 461 451 451 ASP ASP A . n 
A 1 462 MET 462 452 452 MET MET A . n 
A 1 463 LEU 463 453 453 LEU LEU A . n 
A 1 464 GLY 464 454 454 GLY GLY A . n 
A 1 465 ASN 465 455 455 ASN ASN A . n 
A 1 466 VAL 466 456 456 VAL VAL A . n 
A 1 467 MET 467 457 457 MET MET A . n 
A 1 468 ALA 468 458 458 ALA ALA A . n 
A 1 469 HIS 469 459 459 HIS HIS A . n 
A 1 470 LEU 470 460 460 LEU LEU A . n 
A 1 471 VAL 471 461 461 VAL VAL A . n 
A 1 472 GLU 472 462 462 GLU GLU A . n 
A 1 473 ASN 473 463 463 ASN ASN A . n 
A 1 474 ILE 474 464 464 ILE ILE A . n 
A 1 475 ARG 475 465 465 ARG ARG A . n 
A 1 476 TYR 476 466 466 TYR TYR A . n 
A 1 477 ALA 477 467 467 ALA ALA A . n 
A 1 478 ALA 478 468 468 ALA ALA A . n 
A 1 479 VAL 479 469 469 VAL VAL A . n 
A 1 480 LEU 480 470 470 LEU LEU A . n 
A 1 481 LEU 481 471 471 LEU LEU A . n 
A 1 482 ARG 482 472 472 ARG ARG A . n 
A 1 483 PRO 483 473 473 PRO PRO A . n 
A 1 484 PHE 484 474 474 PHE PHE A . n 
A 1 485 LEU 485 475 475 LEU LEU A . n 
A 1 486 THR 486 476 476 THR THR A . n 
A 1 487 HIS 487 477 477 HIS HIS A . n 
A 1 488 ALA 488 478 478 ALA ALA A . n 
A 1 489 PRO 489 479 479 PRO PRO A . n 
A 1 490 LYS 490 480 480 LYS LYS A . n 
A 1 491 GLU 491 481 481 GLU GLU A . n 
A 1 492 ILE 492 482 482 ILE ILE A . n 
A 1 493 PHE 493 483 483 PHE PHE A . n 
A 1 494 GLU 494 484 484 GLU GLU A . n 
A 1 495 GLN 495 485 485 GLN GLN A . n 
A 1 496 LEU 496 486 486 LEU LEU A . n 
A 1 497 ASN 497 487 487 ASN ASN A . n 
A 1 498 ILE 498 488 488 ILE ILE A . n 
A 1 499 ASN 499 489 489 ASN ASN A . n 
A 1 500 ASN 500 490 490 ASN ASN A . n 
A 1 501 PRO 501 491 491 PRO PRO A . n 
A 1 502 GLN 502 492 492 GLN GLN A . n 
A 1 503 PHE 503 493 493 PHE PHE A . n 
A 1 504 MET 504 494 494 MET MET A . n 
A 1 505 GLU 505 495 495 GLU GLU A . n 
A 1 506 PHE 506 496 496 PHE PHE A . n 
A 1 507 SER 507 497 497 SER SER A . n 
A 1 508 SER 508 498 498 SER SER A . n 
A 1 509 LEU 509 499 499 LEU LEU A . n 
A 1 510 GLU 510 500 500 GLU GLU A . n 
A 1 511 GLN 511 501 501 GLN GLN A . n 
A 1 512 TYR 512 502 502 TYR TYR A . n 
A 1 513 GLY 513 503 503 GLY GLY A . n 
A 1 514 VAL 514 504 504 VAL VAL A . n 
A 1 515 LEU 515 505 505 LEU LEU A . n 
A 1 516 ASN 516 506 506 ASN ASN A . n 
A 1 517 GLU 517 507 507 GLU GLU A . n 
A 1 518 SER 518 508 508 SER SER A . n 
A 1 519 ILE 519 509 509 ILE ILE A . n 
A 1 520 MET 520 510 510 MET MET A . n 
A 1 521 VAL 521 511 511 VAL VAL A . n 
A 1 522 THR 522 512 512 THR THR A . n 
A 1 523 GLY 523 513 513 GLY GLY A . n 
A 1 524 GLN 524 514 514 GLN GLN A . n 
A 1 525 PRO 525 515 515 PRO PRO A . n 
A 1 526 LYS 526 516 516 LYS LYS A . n 
A 1 527 PRO 527 517 517 PRO PRO A . n 
A 1 528 ILE 528 518 518 ILE ILE A . n 
A 1 529 PHE 529 519 519 PHE PHE A . n 
A 1 530 PRO 530 520 520 PRO PRO A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        XC9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XC9 
_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 ATP 1   601  601 ATP ATP A . 
C 3 XC9 1   602  1   XC9 C6  A . 
D 4 EDO 1   603  1   EDO EDO A . 
E 4 EDO 1   604  2   EDO EDO A . 
F 4 EDO 1   605  3   EDO EDO A . 
G 4 EDO 1   606  7   EDO EDO A . 
H 5 HOH 1   701  254 HOH HOH A . 
H 5 HOH 2   702  95  HOH HOH A . 
H 5 HOH 3   703  259 HOH HOH A . 
H 5 HOH 4   704  60  HOH HOH A . 
H 5 HOH 5   705  273 HOH HOH A . 
H 5 HOH 6   706  36  HOH HOH A . 
H 5 HOH 7   707  142 HOH HOH A . 
H 5 HOH 8   708  283 HOH HOH A . 
H 5 HOH 9   709  164 HOH HOH A . 
H 5 HOH 10  710  62  HOH HOH A . 
H 5 HOH 11  711  71  HOH HOH A . 
H 5 HOH 12  712  136 HOH HOH A . 
H 5 HOH 13  713  31  HOH HOH A . 
H 5 HOH 14  714  276 HOH HOH A . 
H 5 HOH 15  715  235 HOH HOH A . 
H 5 HOH 16  716  197 HOH HOH A . 
H 5 HOH 17  717  15  HOH HOH A . 
H 5 HOH 18  718  61  HOH HOH A . 
H 5 HOH 19  719  43  HOH HOH A . 
H 5 HOH 20  720  127 HOH HOH A . 
H 5 HOH 21  721  105 HOH HOH A . 
H 5 HOH 22  722  123 HOH HOH A . 
H 5 HOH 23  723  287 HOH HOH A . 
H 5 HOH 24  724  195 HOH HOH A . 
H 5 HOH 25  725  205 HOH HOH A . 
H 5 HOH 26  726  12  HOH HOH A . 
H 5 HOH 27  727  284 HOH HOH A . 
H 5 HOH 28  728  70  HOH HOH A . 
H 5 HOH 29  729  88  HOH HOH A . 
H 5 HOH 30  730  247 HOH HOH A . 
H 5 HOH 31  731  25  HOH HOH A . 
H 5 HOH 32  732  288 HOH HOH A . 
H 5 HOH 33  733  89  HOH HOH A . 
H 5 HOH 34  734  271 HOH HOH A . 
H 5 HOH 35  735  45  HOH HOH A . 
H 5 HOH 36  736  295 HOH HOH A . 
H 5 HOH 37  737  318 HOH HOH A . 
H 5 HOH 38  738  76  HOH HOH A . 
H 5 HOH 39  739  58  HOH HOH A . 
H 5 HOH 40  740  27  HOH HOH A . 
H 5 HOH 41  741  108 HOH HOH A . 
H 5 HOH 42  742  280 HOH HOH A . 
H 5 HOH 43  743  222 HOH HOH A . 
H 5 HOH 44  744  191 HOH HOH A . 
H 5 HOH 45  745  225 HOH HOH A . 
H 5 HOH 46  746  13  HOH HOH A . 
H 5 HOH 47  747  170 HOH HOH A . 
H 5 HOH 48  748  174 HOH HOH A . 
H 5 HOH 49  749  114 HOH HOH A . 
H 5 HOH 50  750  320 HOH HOH A . 
H 5 HOH 51  751  92  HOH HOH A . 
H 5 HOH 52  752  166 HOH HOH A . 
H 5 HOH 53  753  181 HOH HOH A . 
H 5 HOH 54  754  21  HOH HOH A . 
H 5 HOH 55  755  278 HOH HOH A . 
H 5 HOH 56  756  73  HOH HOH A . 
H 5 HOH 57  757  291 HOH HOH A . 
H 5 HOH 58  758  59  HOH HOH A . 
H 5 HOH 59  759  55  HOH HOH A . 
H 5 HOH 60  760  90  HOH HOH A . 
H 5 HOH 61  761  133 HOH HOH A . 
H 5 HOH 62  762  304 HOH HOH A . 
H 5 HOH 63  763  37  HOH HOH A . 
H 5 HOH 64  764  96  HOH HOH A . 
H 5 HOH 65  765  153 HOH HOH A . 
H 5 HOH 66  766  99  HOH HOH A . 
H 5 HOH 67  767  217 HOH HOH A . 
H 5 HOH 68  768  117 HOH HOH A . 
H 5 HOH 69  769  24  HOH HOH A . 
H 5 HOH 70  770  35  HOH HOH A . 
H 5 HOH 71  771  239 HOH HOH A . 
H 5 HOH 72  772  115 HOH HOH A . 
H 5 HOH 73  773  116 HOH HOH A . 
H 5 HOH 74  774  219 HOH HOH A . 
H 5 HOH 75  775  297 HOH HOH A . 
H 5 HOH 76  776  325 HOH HOH A . 
H 5 HOH 77  777  94  HOH HOH A . 
H 5 HOH 78  778  78  HOH HOH A . 
H 5 HOH 79  779  194 HOH HOH A . 
H 5 HOH 80  780  102 HOH HOH A . 
H 5 HOH 81  781  234 HOH HOH A . 
H 5 HOH 82  782  66  HOH HOH A . 
H 5 HOH 83  783  130 HOH HOH A . 
H 5 HOH 84  784  101 HOH HOH A . 
H 5 HOH 85  785  157 HOH HOH A . 
H 5 HOH 86  786  213 HOH HOH A . 
H 5 HOH 87  787  146 HOH HOH A . 
H 5 HOH 88  788  67  HOH HOH A . 
H 5 HOH 89  789  19  HOH HOH A . 
H 5 HOH 90  790  148 HOH HOH A . 
H 5 HOH 91  791  50  HOH HOH A . 
H 5 HOH 92  792  330 HOH HOH A . 
H 5 HOH 93  793  69  HOH HOH A . 
H 5 HOH 94  794  16  HOH HOH A . 
H 5 HOH 95  795  175 HOH HOH A . 
H 5 HOH 96  796  17  HOH HOH A . 
H 5 HOH 97  797  216 HOH HOH A . 
H 5 HOH 98  798  260 HOH HOH A . 
H 5 HOH 99  799  75  HOH HOH A . 
H 5 HOH 100 800  144 HOH HOH A . 
H 5 HOH 101 801  184 HOH HOH A . 
H 5 HOH 102 802  134 HOH HOH A . 
H 5 HOH 103 803  139 HOH HOH A . 
H 5 HOH 104 804  159 HOH HOH A . 
H 5 HOH 105 805  237 HOH HOH A . 
H 5 HOH 106 806  10  HOH HOH A . 
H 5 HOH 107 807  81  HOH HOH A . 
H 5 HOH 108 808  196 HOH HOH A . 
H 5 HOH 109 809  8   HOH HOH A . 
H 5 HOH 110 810  180 HOH HOH A . 
H 5 HOH 111 811  112 HOH HOH A . 
H 5 HOH 112 812  56  HOH HOH A . 
H 5 HOH 113 813  214 HOH HOH A . 
H 5 HOH 114 814  218 HOH HOH A . 
H 5 HOH 115 815  161 HOH HOH A . 
H 5 HOH 116 816  29  HOH HOH A . 
H 5 HOH 117 817  163 HOH HOH A . 
H 5 HOH 118 818  160 HOH HOH A . 
H 5 HOH 119 819  41  HOH HOH A . 
H 5 HOH 120 820  277 HOH HOH A . 
H 5 HOH 121 821  107 HOH HOH A . 
H 5 HOH 122 822  80  HOH HOH A . 
H 5 HOH 123 823  106 HOH HOH A . 
H 5 HOH 124 824  4   HOH HOH A . 
H 5 HOH 125 825  319 HOH HOH A . 
H 5 HOH 126 826  152 HOH HOH A . 
H 5 HOH 127 827  1   HOH HOH A . 
H 5 HOH 128 828  210 HOH HOH A . 
H 5 HOH 129 829  103 HOH HOH A . 
H 5 HOH 130 830  202 HOH HOH A . 
H 5 HOH 131 831  292 HOH HOH A . 
H 5 HOH 132 832  156 HOH HOH A . 
H 5 HOH 133 833  299 HOH HOH A . 
H 5 HOH 134 834  227 HOH HOH A . 
H 5 HOH 135 835  298 HOH HOH A . 
H 5 HOH 136 836  281 HOH HOH A . 
H 5 HOH 137 837  2   HOH HOH A . 
H 5 HOH 138 838  296 HOH HOH A . 
H 5 HOH 139 839  91  HOH HOH A . 
H 5 HOH 140 840  131 HOH HOH A . 
H 5 HOH 141 841  64  HOH HOH A . 
H 5 HOH 142 842  3   HOH HOH A . 
H 5 HOH 143 843  120 HOH HOH A . 
H 5 HOH 144 844  32  HOH HOH A . 
H 5 HOH 145 845  272 HOH HOH A . 
H 5 HOH 146 846  269 HOH HOH A . 
H 5 HOH 147 847  5   HOH HOH A . 
H 5 HOH 148 848  147 HOH HOH A . 
H 5 HOH 149 849  68  HOH HOH A . 
H 5 HOH 150 850  236 HOH HOH A . 
H 5 HOH 151 851  188 HOH HOH A . 
H 5 HOH 152 852  199 HOH HOH A . 
H 5 HOH 153 853  82  HOH HOH A . 
H 5 HOH 154 854  155 HOH HOH A . 
H 5 HOH 155 855  128 HOH HOH A . 
H 5 HOH 156 856  286 HOH HOH A . 
H 5 HOH 157 857  53  HOH HOH A . 
H 5 HOH 158 858  138 HOH HOH A . 
H 5 HOH 159 859  122 HOH HOH A . 
H 5 HOH 160 860  182 HOH HOH A . 
H 5 HOH 161 861  20  HOH HOH A . 
H 5 HOH 162 862  98  HOH HOH A . 
H 5 HOH 163 863  39  HOH HOH A . 
H 5 HOH 164 864  74  HOH HOH A . 
H 5 HOH 165 865  132 HOH HOH A . 
H 5 HOH 166 866  187 HOH HOH A . 
H 5 HOH 167 867  6   HOH HOH A . 
H 5 HOH 168 868  293 HOH HOH A . 
H 5 HOH 169 869  255 HOH HOH A . 
H 5 HOH 170 870  243 HOH HOH A . 
H 5 HOH 171 871  279 HOH HOH A . 
H 5 HOH 172 872  11  HOH HOH A . 
H 5 HOH 173 873  51  HOH HOH A . 
H 5 HOH 174 874  44  HOH HOH A . 
H 5 HOH 175 875  221 HOH HOH A . 
H 5 HOH 176 876  309 HOH HOH A . 
H 5 HOH 177 877  40  HOH HOH A . 
H 5 HOH 178 878  33  HOH HOH A . 
H 5 HOH 179 879  224 HOH HOH A . 
H 5 HOH 180 880  165 HOH HOH A . 
H 5 HOH 181 881  141 HOH HOH A . 
H 5 HOH 182 882  124 HOH HOH A . 
H 5 HOH 183 883  84  HOH HOH A . 
H 5 HOH 184 884  121 HOH HOH A . 
H 5 HOH 185 885  312 HOH HOH A . 
H 5 HOH 186 886  256 HOH HOH A . 
H 5 HOH 187 887  23  HOH HOH A . 
H 5 HOH 188 888  49  HOH HOH A . 
H 5 HOH 189 889  323 HOH HOH A . 
H 5 HOH 190 890  177 HOH HOH A . 
H 5 HOH 191 891  151 HOH HOH A . 
H 5 HOH 192 892  307 HOH HOH A . 
H 5 HOH 193 893  328 HOH HOH A . 
H 5 HOH 194 894  83  HOH HOH A . 
H 5 HOH 195 895  110 HOH HOH A . 
H 5 HOH 196 896  226 HOH HOH A . 
H 5 HOH 197 897  208 HOH HOH A . 
H 5 HOH 198 898  223 HOH HOH A . 
H 5 HOH 199 899  14  HOH HOH A . 
H 5 HOH 200 900  109 HOH HOH A . 
H 5 HOH 201 901  22  HOH HOH A . 
H 5 HOH 202 902  47  HOH HOH A . 
H 5 HOH 203 903  190 HOH HOH A . 
H 5 HOH 204 904  34  HOH HOH A . 
H 5 HOH 205 905  48  HOH HOH A . 
H 5 HOH 206 906  79  HOH HOH A . 
H 5 HOH 207 907  212 HOH HOH A . 
H 5 HOH 208 908  28  HOH HOH A . 
H 5 HOH 209 909  233 HOH HOH A . 
H 5 HOH 210 910  26  HOH HOH A . 
H 5 HOH 211 911  125 HOH HOH A . 
H 5 HOH 212 912  100 HOH HOH A . 
H 5 HOH 213 913  104 HOH HOH A . 
H 5 HOH 214 914  42  HOH HOH A . 
H 5 HOH 215 915  87  HOH HOH A . 
H 5 HOH 216 916  65  HOH HOH A . 
H 5 HOH 217 917  7   HOH HOH A . 
H 5 HOH 218 918  162 HOH HOH A . 
H 5 HOH 219 919  9   HOH HOH A . 
H 5 HOH 220 920  46  HOH HOH A . 
H 5 HOH 221 921  301 HOH HOH A . 
H 5 HOH 222 922  176 HOH HOH A . 
H 5 HOH 223 923  204 HOH HOH A . 
H 5 HOH 224 924  54  HOH HOH A . 
H 5 HOH 225 925  145 HOH HOH A . 
H 5 HOH 226 926  85  HOH HOH A . 
H 5 HOH 227 927  303 HOH HOH A . 
H 5 HOH 228 928  308 HOH HOH A . 
H 5 HOH 229 929  313 HOH HOH A . 
H 5 HOH 230 930  57  HOH HOH A . 
H 5 HOH 231 931  63  HOH HOH A . 
H 5 HOH 232 932  38  HOH HOH A . 
H 5 HOH 233 933  135 HOH HOH A . 
H 5 HOH 234 934  228 HOH HOH A . 
H 5 HOH 235 935  52  HOH HOH A . 
H 5 HOH 236 936  241 HOH HOH A . 
H 5 HOH 237 937  30  HOH HOH A . 
H 5 HOH 238 938  251 HOH HOH A . 
H 5 HOH 239 939  18  HOH HOH A . 
H 5 HOH 240 940  314 HOH HOH A . 
H 5 HOH 241 941  231 HOH HOH A . 
H 5 HOH 242 942  230 HOH HOH A . 
H 5 HOH 243 943  149 HOH HOH A . 
H 5 HOH 244 944  154 HOH HOH A . 
H 5 HOH 245 945  173 HOH HOH A . 
H 5 HOH 246 946  282 HOH HOH A . 
H 5 HOH 247 947  232 HOH HOH A . 
H 5 HOH 248 948  285 HOH HOH A . 
H 5 HOH 249 949  137 HOH HOH A . 
H 5 HOH 250 950  200 HOH HOH A . 
H 5 HOH 251 951  93  HOH HOH A . 
H 5 HOH 252 952  206 HOH HOH A . 
H 5 HOH 253 953  240 HOH HOH A . 
H 5 HOH 254 954  209 HOH HOH A . 
H 5 HOH 255 955  198 HOH HOH A . 
H 5 HOH 256 956  270 HOH HOH A . 
H 5 HOH 257 957  249 HOH HOH A . 
H 5 HOH 258 958  306 HOH HOH A . 
H 5 HOH 259 959  238 HOH HOH A . 
H 5 HOH 260 960  111 HOH HOH A . 
H 5 HOH 261 961  126 HOH HOH A . 
H 5 HOH 262 962  97  HOH HOH A . 
H 5 HOH 263 963  86  HOH HOH A . 
H 5 HOH 264 964  229 HOH HOH A . 
H 5 HOH 265 965  178 HOH HOH A . 
H 5 HOH 266 966  150 HOH HOH A . 
H 5 HOH 267 967  329 HOH HOH A . 
H 5 HOH 268 968  186 HOH HOH A . 
H 5 HOH 269 969  250 HOH HOH A . 
H 5 HOH 270 970  72  HOH HOH A . 
H 5 HOH 271 971  220 HOH HOH A . 
H 5 HOH 272 972  171 HOH HOH A . 
H 5 HOH 273 973  289 HOH HOH A . 
H 5 HOH 274 974  169 HOH HOH A . 
H 5 HOH 275 975  113 HOH HOH A . 
H 5 HOH 276 976  119 HOH HOH A . 
H 5 HOH 277 977  211 HOH HOH A . 
H 5 HOH 278 978  143 HOH HOH A . 
H 5 HOH 279 979  203 HOH HOH A . 
H 5 HOH 280 980  326 HOH HOH A . 
H 5 HOH 281 981  305 HOH HOH A . 
H 5 HOH 282 982  246 HOH HOH A . 
H 5 HOH 283 983  290 HOH HOH A . 
H 5 HOH 284 984  183 HOH HOH A . 
H 5 HOH 285 985  311 HOH HOH A . 
H 5 HOH 286 986  215 HOH HOH A . 
H 5 HOH 287 987  253 HOH HOH A . 
H 5 HOH 288 988  248 HOH HOH A . 
H 5 HOH 289 989  77  HOH HOH A . 
H 5 HOH 290 990  327 HOH HOH A . 
H 5 HOH 291 991  168 HOH HOH A . 
H 5 HOH 292 992  316 HOH HOH A . 
H 5 HOH 293 993  185 HOH HOH A . 
H 5 HOH 294 994  201 HOH HOH A . 
H 5 HOH 295 995  244 HOH HOH A . 
H 5 HOH 296 996  317 HOH HOH A . 
H 5 HOH 297 997  172 HOH HOH A . 
H 5 HOH 298 998  179 HOH HOH A . 
H 5 HOH 299 999  140 HOH HOH A . 
H 5 HOH 300 1000 322 HOH HOH A . 
H 5 HOH 301 1001 129 HOH HOH A . 
H 5 HOH 302 1002 193 HOH HOH A . 
H 5 HOH 303 1003 294 HOH HOH A . 
H 5 HOH 304 1004 245 HOH HOH A . 
H 5 HOH 305 1005 252 HOH HOH A . 
H 5 HOH 306 1006 242 HOH HOH A . 
H 5 HOH 307 1007 158 HOH HOH A . 
H 5 HOH 308 1008 207 HOH HOH A . 
H 5 HOH 309 1009 321 HOH HOH A . 
H 5 HOH 310 1010 167 HOH HOH A . 
H 5 HOH 311 1011 189 HOH HOH A . 
H 5 HOH 312 1012 302 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A VAL 141 ? CG1 ? A VAL 151 CG1 
2  1 Y 1 A VAL 141 ? CG2 ? A VAL 151 CG2 
3  1 Y 1 A ASN 147 ? CG  ? A ASN 157 CG  
4  1 Y 1 A ASN 147 ? OD1 ? A ASN 157 OD1 
5  1 Y 1 A ASN 147 ? ND2 ? A ASN 157 ND2 
6  1 Y 1 A LYS 149 ? CG  ? A LYS 159 CG  
7  1 Y 1 A LYS 149 ? CD  ? A LYS 159 CD  
8  1 Y 1 A LYS 149 ? CE  ? A LYS 159 CE  
9  1 Y 1 A LYS 149 ? NZ  ? A LYS 159 NZ  
10 1 Y 1 A LYS 154 ? CG  ? A LYS 164 CG  
11 1 Y 1 A LYS 154 ? CD  ? A LYS 164 CD  
12 1 Y 1 A LYS 154 ? CE  ? A LYS 164 CE  
13 1 Y 1 A LYS 154 ? NZ  ? A LYS 164 NZ  
14 1 Y 1 A LYS 207 ? CG  ? A LYS 217 CG  
15 1 Y 1 A LYS 207 ? CD  ? A LYS 217 CD  
16 1 Y 1 A LYS 207 ? CE  ? A LYS 217 CE  
17 1 Y 1 A LYS 207 ? NZ  ? A LYS 217 NZ  
# 
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        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0158 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? autoPROC    ? ? ? .        3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        4 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? autoPROC    ? ? ? .        5 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? autoPROC    ? ? ? .        6 
# 
_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                     8XM4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.409 
_cell.length_a_esd                 ? 
_cell.length_b                     76.059 
_cell.length_b_esd                 ? 
_cell.length_c                     119.046 
_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                         8XM4 
_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                   8XM4 
_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             2.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.31 
_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, SITTING 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    '0.10 M magnesium acetate, 0.1 M Bis-Tris pH 7.0, 20% w/v PEG 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-27 
_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   0.9785 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XM4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.67 
_reflns.d_resolution_low                               64.09 
_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                                     66315 
_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                           96.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          25.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.83 
_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                                0.038 
_reflns.pdbx_Rpim_I_all                                0.016 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       384951 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.034 
_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                                    1.67 
_reflns_shell.d_res_low                                     1.76 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           58515 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9828 
_reflns_shell.percent_possible_obs                          98.6 
_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                               6.0 
_reflns_shell.pdbx_chi_squared                              0.65 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.6 
_reflns_shell.pdbx_Rrim_I_all                               0.703 
_reflns_shell.pdbx_Rpim_I_all                               0.283 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.880 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.642 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.07 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            1.54 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.61 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.846 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8XM4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.67 
_refine.ls_d_res_low                             64.09 
_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                     62873 
_refine.ls_number_reflns_R_free                  3394 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.71 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18945 
_refine.ls_R_factor_R_free                       0.21427 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18811 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.106 
_refine.pdbx_overall_ESU_R_Free                  0.101 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_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                             4.303 
_refine.overall_SU_ML                            0.075 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.67 
_refine_hist.d_res_low                        64.09 
_refine_hist.number_atoms_solvent             312 
_refine_hist.number_atoms_total               4597 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4204 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         81 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  0.019  4469 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  3994 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.291  1.970  6076 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.915  3.000  9295 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.379  5.000  526  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 35.717 24.744 215  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.782 15.000 737  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.024 15.000 18   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.074  0.200  643  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.021  4993 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  919  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.016  2.808  2095 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.015  2.807  2094 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.710  4.203  2624 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.710  4.204  2625 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.032  2.874  2374 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.031  2.874  2374 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.772  4.264  3453 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.415  32.193 5105 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.240  31.908 5031 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.673 
_refine_ls_shell.d_res_low                        1.717 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             262 
_refine_ls_shell.number_reflns_R_work             4667 
_refine_ls_shell.percent_reflns_obs               98.13 
_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                  0.284 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.320 
# 
_struct.entry_id                     8XM4 
_struct.title                        'Methionyl-tRNA synthetase from Staphylococcus aureus in complex with chlorhexidine and ATP' 
_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        8XM4 
_struct_keywords.text            'MetRS, methionyl-tRNA synthetase, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SYM_STAAC 
_struct_ref.pdbx_db_accession          Q5HII6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQ
LWAKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDPQYENGKIIGGKSPDSGHE
VELVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMINNFIKPGLADLAVSRTSFNWGVHVPSNPKHVVYVWIDAL
VNYISALGYLSDDESLFNKYWPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWILMKDGKMSKSKGNVVDPNI
LIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVNKYFDGELPAYQGPLHELDEEMEAMA
LETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKDDSQKDMLGNVMAHLVENIRYAAVLLRPFLTHAPKE
IFEQLNINNPQFMEFSSLEQYGVLNESIMVTGQPKPIFP
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XM4 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 12 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 530 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q5HII6 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  520 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       520 
# 
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 8XM4 MET A 1  ? UNP Q5HII6 ? ? 'initiating methionine' -9 1  
1 8XM4 GLY A 2  ? UNP Q5HII6 ? ? 'expression tag'        -8 2  
1 8XM4 SER A 3  ? UNP Q5HII6 ? ? 'expression tag'        -7 3  
1 8XM4 SER A 4  ? UNP Q5HII6 ? ? 'expression tag'        -6 4  
1 8XM4 HIS A 5  ? UNP Q5HII6 ? ? 'expression tag'        -5 5  
1 8XM4 HIS A 6  ? UNP Q5HII6 ? ? 'expression tag'        -4 6  
1 8XM4 HIS A 7  ? UNP Q5HII6 ? ? 'expression tag'        -3 7  
1 8XM4 HIS A 8  ? UNP Q5HII6 ? ? 'expression tag'        -2 8  
1 8XM4 HIS A 9  ? UNP Q5HII6 ? ? 'expression tag'        -1 9  
1 8XM4 HIS A 10 ? UNP Q5HII6 ? ? 'expression tag'        0  10 
1 8XM4 SER A 11 ? UNP Q5HII6 ? ? 'expression tag'        1  11 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 30  ? GLN A 50  ? HIS A 20  GLN A 40  1 ? 21 
HELX_P HELX_P2  AA2 GLY A 64  ? ALA A 74  ? GLY A 54  ALA A 64  1 ? 11 
HELX_P HELX_P3  AA3 THR A 77  ? LEU A 96  ? THR A 67  LEU A 86  1 ? 20 
HELX_P HELX_P4  AA4 GLU A 108 ? GLN A 125 ? GLU A 98  GLN A 115 1 ? 18 
HELX_P HELX_P5  AA5 THR A 146 ? LEU A 150 ? THR A 136 LEU A 140 5 ? 5  
HELX_P HELX_P6  AA6 ILE A 184 ? LYS A 186 ? ILE A 174 LYS A 176 5 ? 3  
HELX_P HELX_P7  AA7 TYR A 187 ? ASN A 198 ? TYR A 177 ASN A 188 1 ? 12 
HELX_P HELX_P8  AA8 PRO A 204 ? PHE A 215 ? PRO A 194 PHE A 205 1 ? 12 
HELX_P HELX_P9  AA9 TYR A 245 ? VAL A 252 ? TYR A 235 VAL A 242 1 ? 8  
HELX_P HELX_P10 AB1 VAL A 252 ? ALA A 257 ? VAL A 242 ALA A 247 1 ? 6  
HELX_P HELX_P11 AB2 GLU A 265 ? TRP A 272 ? GLU A 255 TRP A 262 1 ? 8  
HELX_P HELX_P12 AB3 ILE A 283 ? ILE A 289 ? ILE A 273 ILE A 279 1 ? 7  
HELX_P HELX_P13 AB4 ILE A 289 ? LEU A 298 ? ILE A 279 LEU A 288 1 ? 10 
HELX_P HELX_P14 AB5 ASP A 328 ? GLY A 337 ? ASP A 318 GLY A 327 1 ? 10 
HELX_P HELX_P15 AB6 GLY A 337 ? LEU A 349 ? GLY A 327 LEU A 339 1 ? 13 
HELX_P HELX_P16 AB7 THR A 358 ? LEU A 370 ? THR A 348 LEU A 360 1 ? 13 
HELX_P HELX_P17 AB8 ASN A 372 ? ASP A 390 ? ASN A 362 ASP A 380 1 ? 19 
HELX_P HELX_P18 AB9 LEU A 403 ? SER A 424 ? LEU A 393 SER A 414 1 ? 22 
HELX_P HELX_P19 AC1 GLN A 426 ? THR A 449 ? GLN A 416 THR A 439 1 ? 24 
HELX_P HELX_P20 AC2 THR A 449 ? ALA A 454 ? THR A 439 ALA A 444 1 ? 6  
HELX_P HELX_P21 AC3 LYS A 455 ? SER A 458 ? LYS A 445 SER A 448 5 ? 4  
HELX_P HELX_P22 AC4 GLN A 459 ? ARG A 482 ? GLN A 449 ARG A 472 1 ? 24 
HELX_P HELX_P23 AC5 HIS A 487 ? ASN A 497 ? HIS A 477 ASN A 487 1 ? 11 
HELX_P HELX_P24 AC6 ASN A 500 ? GLU A 510 ? ASN A 490 GLU A 500 5 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLN 203 A . ? GLN 193 A PRO 204 A ? PRO 194 A 1 -7.47 
2 TRP 272 A . ? TRP 262 A PRO 273 A ? PRO 263 A 1 7.62  
3 PHE 529 A . ? PHE 519 A PRO 530 A ? PRO 520 A 1 4.55  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA6 1 2 ? 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 ASP A 102 ? ARG A 105 ? ASP A 92  ARG A 95  
AA1 2 ASP A 53  ? THR A 60  ? ASP A 43  THR A 50  
AA1 3 THR A 15  ? TYR A 23  ? THR A 5   TYR A 13  
AA1 4 ILE A 276 ? ALA A 280 ? ILE A 266 ALA A 270 
AA1 5 VAL A 306 ? HIS A 309 ? VAL A 296 HIS A 299 
AA2 1 THR A 143 ? TYR A 145 ? THR A 133 TYR A 135 
AA2 2 ILE A 128 ? SER A 138 ? ILE A 118 SER A 128 
AA2 3 GLU A 173 ? PHE A 182 ? GLU A 163 PHE A 172 
AA2 4 LEU A 223 ? ALA A 224 ? LEU A 213 ALA A 214 
AA3 1 VAL A 151 ? TYR A 155 ? VAL A 141 TYR A 145 
AA3 2 ILE A 160 ? LYS A 164 ? ILE A 150 LYS A 154 
AA4 1 SER A 226 ? ARG A 227 ? SER A 216 ARG A 217 
AA4 2 ASN A 239 ? VAL A 244 ? ASN A 229 VAL A 234 
AA4 3 HIS A 235 ? VAL A 236 ? HIS A 225 VAL A 226 
AA5 1 GLY A 317 ? LYS A 318 ? GLY A 307 LYS A 308 
AA5 2 ILE A 312 ? MET A 314 ? ILE A 302 MET A 304 
AA5 3 GLY A 355 ? VAL A 356 ? GLY A 345 VAL A 346 
AA6 1 GLU A 392 ? LEU A 393 ? GLU A 382 LEU A 383 
AA6 2 ILE A 519 ? MET A 520 ? ILE A 509 MET A 510 
# 
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 O ILE A 104 ? O ILE A 94  N THR A 60  ? N THR A 50  
AA1 2 3 O ARG A 55  ? O ARG A 45  N ILE A 18  ? N ILE A 8   
AA1 3 4 N THR A 19  ? N THR A 9   O LEU A 278 ? O LEU A 268 
AA1 4 5 N HIS A 277 ? N HIS A 267 O PHE A 307 ? O PHE A 297 
AA2 1 2 O TYR A 145 ? O TYR A 135 N TRP A 136 ? N TRP A 126 
AA2 2 3 N TYR A 129 ? N TYR A 119 O PHE A 181 ? O PHE A 171 
AA2 3 4 N PHE A 182 ? N PHE A 172 O LEU A 223 ? O LEU A 213 
AA3 1 2 N GLN A 154 ? N GLN A 144 O ILE A 161 ? O ILE A 151 
AA4 1 2 N ARG A 227 ? N ARG A 217 O VAL A 243 ? O VAL A 233 
AA4 2 3 O HIS A 242 ? O HIS A 232 N VAL A 236 ? N VAL A 226 
AA5 1 2 O GLY A 317 ? O GLY A 307 N MET A 314 ? N MET A 304 
AA5 2 3 N LEU A 313 ? N LEU A 303 O GLY A 355 ? O GLY A 345 
AA6 1 2 N LEU A 393 ? N LEU A 383 O ILE A 519 ? O ILE A 509 
# 
_pdbx_entry_details.entry_id                   8XM4 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 SER A 89  ? ? -93.86  33.54  
2 1 ASN A 229 ? ? -151.60 77.52  
3 1 LYS A 305 ? ? -92.50  57.10  
4 1 ASP A 306 ? ? -174.28 27.58  
5 1 GLN A 387 ? ? -121.34 -53.53 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -18.7807 
_pdbx_refine_tls.origin_y         2.8697 
_pdbx_refine_tls.origin_z         -13.0090 
_pdbx_refine_tls.T[1][1]          0.0327 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0126 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0064 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0218 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0260 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0473 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.3572 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0662 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.1475 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.0185 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0737 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.5274 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0370 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0384 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0763 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0003 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0003 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0105 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0098 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0483 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0372 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
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 ? ? A 2   ? ? ? A 115 ? ? ? 
2 'X-RAY DIFFRACTION' 1 ? ? A 116 ? ? ? A 152 ? ? ? 
3 'X-RAY DIFFRACTION' 1 ? ? A 153 ? ? ? A 248 ? ? ? 
4 'X-RAY DIFFRACTION' 1 ? ? A 249 ? ? ? A 318 ? ? ? 
5 'X-RAY DIFFRACTION' 1 ? ? A 319 ? ? ? A 416 ? ? ? 
6 'X-RAY DIFFRACTION' 1 ? ? A 417 ? ? ? A 520 ? ? ? 
# 
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 -9 ? A MET 1  
2  1 Y 1 A GLY -8 ? A GLY 2  
3  1 Y 1 A SER -7 ? A SER 3  
4  1 Y 1 A SER -6 ? A SER 4  
5  1 Y 1 A HIS -5 ? A HIS 5  
6  1 Y 1 A HIS -4 ? A HIS 6  
7  1 Y 1 A HIS -3 ? A HIS 7  
8  1 Y 1 A HIS -2 ? A HIS 8  
9  1 Y 1 A HIS -1 ? A HIS 9  
10 1 Y 1 A HIS 0  ? A HIS 10 
11 1 Y 1 A SER 1  ? A SER 11 
# 
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 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
EDO C1     C  N N 121 
EDO O1     O  N N 122 
EDO C2     C  N N 123 
EDO O2     O  N N 124 
EDO H11    H  N N 125 
EDO H12    H  N N 126 
EDO HO1    H  N N 127 
EDO H21    H  N N 128 
EDO H22    H  N N 129 
EDO HO2    H  N N 130 
GLN N      N  N N 131 
GLN CA     C  N S 132 
GLN C      C  N N 133 
GLN O      O  N N 134 
GLN CB     C  N N 135 
GLN CG     C  N N 136 
GLN CD     C  N N 137 
GLN OE1    O  N N 138 
GLN NE2    N  N N 139 
GLN OXT    O  N N 140 
GLN H      H  N N 141 
GLN H2     H  N N 142 
GLN HA     H  N N 143 
GLN HB2    H  N N 144 
GLN HB3    H  N N 145 
GLN HG2    H  N N 146 
GLN HG3    H  N N 147 
GLN HE21   H  N N 148 
GLN HE22   H  N N 149 
GLN HXT    H  N N 150 
GLU N      N  N N 151 
GLU CA     C  N S 152 
GLU C      C  N N 153 
GLU O      O  N N 154 
GLU CB     C  N N 155 
GLU CG     C  N N 156 
GLU CD     C  N N 157 
GLU OE1    O  N N 158 
GLU OE2    O  N N 159 
GLU OXT    O  N N 160 
GLU H      H  N N 161 
GLU H2     H  N N 162 
GLU HA     H  N N 163 
GLU HB2    H  N N 164 
GLU HB3    H  N N 165 
GLU HG2    H  N N 166 
GLU HG3    H  N N 167 
GLU HE2    H  N N 168 
GLU HXT    H  N N 169 
GLY N      N  N N 170 
GLY CA     C  N N 171 
GLY C      C  N N 172 
GLY O      O  N N 173 
GLY OXT    O  N N 174 
GLY H      H  N N 175 
GLY H2     H  N N 176 
GLY HA2    H  N N 177 
GLY HA3    H  N N 178 
GLY HXT    H  N N 179 
HIS N      N  N N 180 
HIS CA     C  N S 181 
HIS C      C  N N 182 
HIS O      O  N N 183 
HIS CB     C  N N 184 
HIS CG     C  Y N 185 
HIS ND1    N  Y N 186 
HIS CD2    C  Y N 187 
HIS CE1    C  Y N 188 
HIS NE2    N  Y N 189 
HIS OXT    O  N N 190 
HIS H      H  N N 191 
HIS H2     H  N N 192 
HIS HA     H  N N 193 
HIS HB2    H  N N 194 
HIS HB3    H  N N 195 
HIS HD1    H  N N 196 
HIS HD2    H  N N 197 
HIS HE1    H  N N 198 
HIS HE2    H  N N 199 
HIS HXT    H  N N 200 
HOH O      O  N N 201 
HOH H1     H  N N 202 
HOH H2     H  N N 203 
ILE N      N  N N 204 
ILE CA     C  N S 205 
ILE C      C  N N 206 
ILE O      O  N N 207 
ILE CB     C  N S 208 
ILE CG1    C  N N 209 
ILE CG2    C  N N 210 
ILE CD1    C  N N 211 
ILE OXT    O  N N 212 
ILE H      H  N N 213 
ILE H2     H  N N 214 
ILE HA     H  N N 215 
ILE HB     H  N N 216 
ILE HG12   H  N N 217 
ILE HG13   H  N N 218 
ILE HG21   H  N N 219 
ILE HG22   H  N N 220 
ILE HG23   H  N N 221 
ILE HD11   H  N N 222 
ILE HD12   H  N N 223 
ILE HD13   H  N N 224 
ILE HXT    H  N N 225 
LEU N      N  N N 226 
LEU CA     C  N S 227 
LEU C      C  N N 228 
LEU O      O  N N 229 
LEU CB     C  N N 230 
LEU CG     C  N N 231 
LEU CD1    C  N N 232 
LEU CD2    C  N N 233 
LEU OXT    O  N N 234 
LEU H      H  N N 235 
LEU H2     H  N N 236 
LEU HA     H  N N 237 
LEU HB2    H  N N 238 
LEU HB3    H  N N 239 
LEU HG     H  N N 240 
LEU HD11   H  N N 241 
LEU HD12   H  N N 242 
LEU HD13   H  N N 243 
LEU HD21   H  N N 244 
LEU HD22   H  N N 245 
LEU HD23   H  N N 246 
LEU HXT    H  N N 247 
LYS N      N  N N 248 
LYS CA     C  N S 249 
LYS C      C  N N 250 
LYS O      O  N N 251 
LYS CB     C  N N 252 
LYS CG     C  N N 253 
LYS CD     C  N N 254 
LYS CE     C  N N 255 
LYS NZ     N  N N 256 
LYS OXT    O  N N 257 
LYS H      H  N N 258 
LYS H2     H  N N 259 
LYS HA     H  N N 260 
LYS HB2    H  N N 261 
LYS HB3    H  N N 262 
LYS HG2    H  N N 263 
LYS HG3    H  N N 264 
LYS HD2    H  N N 265 
LYS HD3    H  N N 266 
LYS HE2    H  N N 267 
LYS HE3    H  N N 268 
LYS HZ1    H  N N 269 
LYS HZ2    H  N N 270 
LYS HZ3    H  N N 271 
LYS HXT    H  N N 272 
MET N      N  N N 273 
MET CA     C  N S 274 
MET C      C  N N 275 
MET O      O  N N 276 
MET CB     C  N N 277 
MET CG     C  N N 278 
MET SD     S  N N 279 
MET CE     C  N N 280 
MET OXT    O  N N 281 
MET H      H  N N 282 
MET H2     H  N N 283 
MET HA     H  N N 284 
MET HB2    H  N N 285 
MET HB3    H  N N 286 
MET HG2    H  N N 287 
MET HG3    H  N N 288 
MET HE1    H  N N 289 
MET HE2    H  N N 290 
MET HE3    H  N N 291 
MET HXT    H  N N 292 
PHE N      N  N N 293 
PHE CA     C  N S 294 
PHE C      C  N N 295 
PHE O      O  N N 296 
PHE CB     C  N N 297 
PHE CG     C  Y N 298 
PHE CD1    C  Y N 299 
PHE CD2    C  Y N 300 
PHE CE1    C  Y N 301 
PHE CE2    C  Y N 302 
PHE CZ     C  Y N 303 
PHE OXT    O  N N 304 
PHE H      H  N N 305 
PHE H2     H  N N 306 
PHE HA     H  N N 307 
PHE HB2    H  N N 308 
PHE HB3    H  N N 309 
PHE HD1    H  N N 310 
PHE HD2    H  N N 311 
PHE HE1    H  N N 312 
PHE HE2    H  N N 313 
PHE HZ     H  N N 314 
PHE HXT    H  N N 315 
PRO N      N  N N 316 
PRO CA     C  N S 317 
PRO C      C  N N 318 
PRO O      O  N N 319 
PRO CB     C  N N 320 
PRO CG     C  N N 321 
PRO CD     C  N N 322 
PRO OXT    O  N N 323 
PRO H      H  N N 324 
PRO HA     H  N N 325 
PRO HB2    H  N N 326 
PRO HB3    H  N N 327 
PRO HG2    H  N N 328 
PRO HG3    H  N N 329 
PRO HD2    H  N N 330 
PRO HD3    H  N N 331 
PRO HXT    H  N N 332 
SER N      N  N N 333 
SER CA     C  N S 334 
SER C      C  N N 335 
SER O      O  N N 336 
SER CB     C  N N 337 
SER OG     O  N N 338 
SER OXT    O  N N 339 
SER H      H  N N 340 
SER H2     H  N N 341 
SER HA     H  N N 342 
SER HB2    H  N N 343 
SER HB3    H  N N 344 
SER HG     H  N N 345 
SER HXT    H  N N 346 
THR N      N  N N 347 
THR CA     C  N S 348 
THR C      C  N N 349 
THR O      O  N N 350 
THR CB     C  N R 351 
THR OG1    O  N N 352 
THR CG2    C  N N 353 
THR OXT    O  N N 354 
THR H      H  N N 355 
THR H2     H  N N 356 
THR HA     H  N N 357 
THR HB     H  N N 358 
THR HG1    H  N N 359 
THR HG21   H  N N 360 
THR HG22   H  N N 361 
THR HG23   H  N N 362 
THR HXT    H  N N 363 
TRP N      N  N N 364 
TRP CA     C  N S 365 
TRP C      C  N N 366 
TRP O      O  N N 367 
TRP CB     C  N N 368 
TRP CG     C  Y N 369 
TRP CD1    C  Y N 370 
TRP CD2    C  Y N 371 
TRP NE1    N  Y N 372 
TRP CE2    C  Y N 373 
TRP CE3    C  Y N 374 
TRP CZ2    C  Y N 375 
TRP CZ3    C  Y N 376 
TRP CH2    C  Y N 377 
TRP OXT    O  N N 378 
TRP H      H  N N 379 
TRP H2     H  N N 380 
TRP HA     H  N N 381 
TRP HB2    H  N N 382 
TRP HB3    H  N N 383 
TRP HD1    H  N N 384 
TRP HE1    H  N N 385 
TRP HE3    H  N N 386 
TRP HZ2    H  N N 387 
TRP HZ3    H  N N 388 
TRP HH2    H  N N 389 
TRP HXT    H  N N 390 
TYR N      N  N N 391 
TYR CA     C  N S 392 
TYR C      C  N N 393 
TYR O      O  N N 394 
TYR CB     C  N N 395 
TYR CG     C  Y N 396 
TYR CD1    C  Y N 397 
TYR CD2    C  Y N 398 
TYR CE1    C  Y N 399 
TYR CE2    C  Y N 400 
TYR CZ     C  Y N 401 
TYR OH     O  N N 402 
TYR OXT    O  N N 403 
TYR H      H  N N 404 
TYR H2     H  N N 405 
TYR HA     H  N N 406 
TYR HB2    H  N N 407 
TYR HB3    H  N N 408 
TYR HD1    H  N N 409 
TYR HD2    H  N N 410 
TYR HE1    H  N N 411 
TYR HE2    H  N N 412 
TYR HH     H  N N 413 
TYR HXT    H  N N 414 
VAL N      N  N N 415 
VAL CA     C  N S 416 
VAL C      C  N N 417 
VAL O      O  N N 418 
VAL CB     C  N N 419 
VAL CG1    C  N N 420 
VAL CG2    C  N N 421 
VAL OXT    O  N N 422 
VAL H      H  N N 423 
VAL H2     H  N N 424 
VAL HA     H  N N 425 
VAL HB     H  N N 426 
VAL HG11   H  N N 427 
VAL HG12   H  N N 428 
VAL HG13   H  N N 429 
VAL HG21   H  N N 430 
VAL HG22   H  N N 431 
VAL HG23   H  N N 432 
VAL HXT    H  N N 433 
XC9 CL2    CL N N 434 
XC9 C10    C  N N 435 
XC9 C11    C  N N 436 
XC9 C12    C  N N 437 
XC9 N6     N  N N 438 
XC9 C13    C  N N 439 
XC9 N7     N  N N 440 
XC9 N8     N  N N 441 
XC9 C14    C  N N 442 
XC9 N9     N  N N 443 
XC9 N10    N  N N 444 
XC9 C15    C  Y N 445 
XC9 C16    C  Y N 446 
XC9 C17    C  Y N 447 
XC9 C18    C  Y N 448 
XC9 C19    C  Y N 449 
XC9 C20    C  Y N 450 
XC9 H1     H  N N 451 
XC9 H2     H  N N 452 
XC9 H4     H  N N 453 
XC9 H5     H  N N 454 
XC9 H6     H  N N 455 
XC9 H7     H  N N 456 
XC9 H8     H  N N 457 
XC9 H9     H  N N 458 
XC9 H10    H  N N 459 
XC9 H11    H  N N 460 
XC9 H12    H  N N 461 
XC9 H13    H  N N 462 
XC9 H14    H  N N 463 
XC9 H15    H  N N 464 
XC9 H16    H  N N 465 
XC9 C1     C  N N 466 
XC9 C2     C  N N 467 
XC9 C3     C  N N 468 
XC9 N1     N  N N 469 
XC9 C4     C  N N 470 
XC9 N2     N  N N 471 
XC9 C5     C  N N 472 
XC9 N3     N  N N 473 
XC9 C6     C  Y N 474 
XC9 C7     C  Y N 475 
XC9 C8     C  Y N 476 
XC9 C9     C  Y N 477 
XC9 C21    C  Y N 478 
XC9 C22    C  Y N 479 
XC9 CL1    CL N N 480 
XC9 H3     H  N N 481 
XC9 H17    H  N N 482 
XC9 H18    H  N N 483 
XC9 H19    H  N N 484 
XC9 H20    H  N N 485 
XC9 H21    H  N N 486 
XC9 H26    H  N N 487 
XC9 H27    H  N N 488 
XC9 H28    H  N N 489 
XC9 H29    H  N N 490 
XC9 H30    H  N N 491 
XC9 N4     N  N N 492 
XC9 N5     N  N N 493 
XC9 H31    H  N N 494 
XC9 H22    H  N N 495 
XC9 H23    H  N N 496 
XC9 H24    H  N N 497 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
EDO C1    O1     sing N N 119 
EDO C1    C2     sing N N 120 
EDO C1    H11    sing N N 121 
EDO C1    H12    sing N N 122 
EDO O1    HO1    sing N N 123 
EDO C2    O2     sing N N 124 
EDO C2    H21    sing N N 125 
EDO C2    H22    sing N N 126 
EDO O2    HO2    sing N N 127 
GLN N     CA     sing N N 128 
GLN N     H      sing N N 129 
GLN N     H2     sing N N 130 
GLN CA    C      sing N N 131 
GLN CA    CB     sing N N 132 
GLN CA    HA     sing N N 133 
GLN C     O      doub N N 134 
GLN C     OXT    sing N N 135 
GLN CB    CG     sing N N 136 
GLN CB    HB2    sing N N 137 
GLN CB    HB3    sing N N 138 
GLN CG    CD     sing N N 139 
GLN CG    HG2    sing N N 140 
GLN CG    HG3    sing N N 141 
GLN CD    OE1    doub N N 142 
GLN CD    NE2    sing N N 143 
GLN NE2   HE21   sing N N 144 
GLN NE2   HE22   sing N N 145 
GLN OXT   HXT    sing N N 146 
GLU N     CA     sing N N 147 
GLU N     H      sing N N 148 
GLU N     H2     sing N N 149 
GLU CA    C      sing N N 150 
GLU CA    CB     sing N N 151 
GLU CA    HA     sing N N 152 
GLU C     O      doub N N 153 
GLU C     OXT    sing N N 154 
GLU CB    CG     sing N N 155 
GLU CB    HB2    sing N N 156 
GLU CB    HB3    sing N N 157 
GLU CG    CD     sing N N 158 
GLU CG    HG2    sing N N 159 
GLU CG    HG3    sing N N 160 
GLU CD    OE1    doub N N 161 
GLU CD    OE2    sing N N 162 
GLU OE2   HE2    sing N N 163 
GLU OXT   HXT    sing N N 164 
GLY N     CA     sing N N 165 
GLY N     H      sing N N 166 
GLY N     H2     sing N N 167 
GLY CA    C      sing N N 168 
GLY CA    HA2    sing N N 169 
GLY CA    HA3    sing N N 170 
GLY C     O      doub N N 171 
GLY C     OXT    sing N N 172 
GLY OXT   HXT    sing N N 173 
HIS N     CA     sing N N 174 
HIS N     H      sing N N 175 
HIS N     H2     sing N N 176 
HIS CA    C      sing N N 177 
HIS CA    CB     sing N N 178 
HIS CA    HA     sing N N 179 
HIS C     O      doub N N 180 
HIS C     OXT    sing N N 181 
HIS CB    CG     sing N N 182 
HIS CB    HB2    sing N N 183 
HIS CB    HB3    sing N N 184 
HIS CG    ND1    sing Y N 185 
HIS CG    CD2    doub Y N 186 
HIS ND1   CE1    doub Y N 187 
HIS ND1   HD1    sing N N 188 
HIS CD2   NE2    sing Y N 189 
HIS CD2   HD2    sing N N 190 
HIS CE1   NE2    sing Y N 191 
HIS CE1   HE1    sing N N 192 
HIS NE2   HE2    sing N N 193 
HIS OXT   HXT    sing N N 194 
HOH O     H1     sing N N 195 
HOH O     H2     sing N N 196 
ILE N     CA     sing N N 197 
ILE N     H      sing N N 198 
ILE N     H2     sing N N 199 
ILE CA    C      sing N N 200 
ILE CA    CB     sing N N 201 
ILE CA    HA     sing N N 202 
ILE C     O      doub N N 203 
ILE C     OXT    sing N N 204 
ILE CB    CG1    sing N N 205 
ILE CB    CG2    sing N N 206 
ILE CB    HB     sing N N 207 
ILE CG1   CD1    sing N N 208 
ILE CG1   HG12   sing N N 209 
ILE CG1   HG13   sing N N 210 
ILE CG2   HG21   sing N N 211 
ILE CG2   HG22   sing N N 212 
ILE CG2   HG23   sing N N 213 
ILE CD1   HD11   sing N N 214 
ILE CD1   HD12   sing N N 215 
ILE CD1   HD13   sing N N 216 
ILE OXT   HXT    sing N N 217 
LEU N     CA     sing N N 218 
LEU N     H      sing N N 219 
LEU N     H2     sing N N 220 
LEU CA    C      sing N N 221 
LEU CA    CB     sing N N 222 
LEU CA    HA     sing N N 223 
LEU C     O      doub N N 224 
LEU C     OXT    sing N N 225 
LEU CB    CG     sing N N 226 
LEU CB    HB2    sing N N 227 
LEU CB    HB3    sing N N 228 
LEU CG    CD1    sing N N 229 
LEU CG    CD2    sing N N 230 
LEU CG    HG     sing N N 231 
LEU CD1   HD11   sing N N 232 
LEU CD1   HD12   sing N N 233 
LEU CD1   HD13   sing N N 234 
LEU CD2   HD21   sing N N 235 
LEU CD2   HD22   sing N N 236 
LEU CD2   HD23   sing N N 237 
LEU OXT   HXT    sing N N 238 
LYS N     CA     sing N N 239 
LYS N     H      sing N N 240 
LYS N     H2     sing N N 241 
LYS CA    C      sing N N 242 
LYS CA    CB     sing N N 243 
LYS CA    HA     sing N N 244 
LYS C     O      doub N N 245 
LYS C     OXT    sing N N 246 
LYS CB    CG     sing N N 247 
LYS CB    HB2    sing N N 248 
LYS CB    HB3    sing N N 249 
LYS CG    CD     sing N N 250 
LYS CG    HG2    sing N N 251 
LYS CG    HG3    sing N N 252 
LYS CD    CE     sing N N 253 
LYS CD    HD2    sing N N 254 
LYS CD    HD3    sing N N 255 
LYS CE    NZ     sing N N 256 
LYS CE    HE2    sing N N 257 
LYS CE    HE3    sing N N 258 
LYS NZ    HZ1    sing N N 259 
LYS NZ    HZ2    sing N N 260 
LYS NZ    HZ3    sing N N 261 
LYS OXT   HXT    sing N N 262 
MET N     CA     sing N N 263 
MET N     H      sing N N 264 
MET N     H2     sing N N 265 
MET CA    C      sing N N 266 
MET CA    CB     sing N N 267 
MET CA    HA     sing N N 268 
MET C     O      doub N N 269 
MET C     OXT    sing N N 270 
MET CB    CG     sing N N 271 
MET CB    HB2    sing N N 272 
MET CB    HB3    sing N N 273 
MET CG    SD     sing N N 274 
MET CG    HG2    sing N N 275 
MET CG    HG3    sing N N 276 
MET SD    CE     sing N N 277 
MET CE    HE1    sing N N 278 
MET CE    HE2    sing N N 279 
MET CE    HE3    sing N N 280 
MET OXT   HXT    sing N N 281 
PHE N     CA     sing N N 282 
PHE N     H      sing N N 283 
PHE N     H2     sing N N 284 
PHE CA    C      sing N N 285 
PHE CA    CB     sing N N 286 
PHE CA    HA     sing N N 287 
PHE C     O      doub N N 288 
PHE C     OXT    sing N N 289 
PHE CB    CG     sing N N 290 
PHE CB    HB2    sing N N 291 
PHE CB    HB3    sing N N 292 
PHE CG    CD1    doub Y N 293 
PHE CG    CD2    sing Y N 294 
PHE CD1   CE1    sing Y N 295 
PHE CD1   HD1    sing N N 296 
PHE CD2   CE2    doub Y N 297 
PHE CD2   HD2    sing N N 298 
PHE CE1   CZ     doub Y N 299 
PHE CE1   HE1    sing N N 300 
PHE CE2   CZ     sing Y N 301 
PHE CE2   HE2    sing N N 302 
PHE CZ    HZ     sing N N 303 
PHE OXT   HXT    sing N N 304 
PRO N     CA     sing N N 305 
PRO N     CD     sing N N 306 
PRO N     H      sing N N 307 
PRO CA    C      sing N N 308 
PRO CA    CB     sing N N 309 
PRO CA    HA     sing N N 310 
PRO C     O      doub N N 311 
PRO C     OXT    sing N N 312 
PRO CB    CG     sing N N 313 
PRO CB    HB2    sing N N 314 
PRO CB    HB3    sing N N 315 
PRO CG    CD     sing N N 316 
PRO CG    HG2    sing N N 317 
PRO CG    HG3    sing N N 318 
PRO CD    HD2    sing N N 319 
PRO CD    HD3    sing N N 320 
PRO OXT   HXT    sing N N 321 
SER N     CA     sing N N 322 
SER N     H      sing N N 323 
SER N     H2     sing N N 324 
SER CA    C      sing N N 325 
SER CA    CB     sing N N 326 
SER CA    HA     sing N N 327 
SER C     O      doub N N 328 
SER C     OXT    sing N N 329 
SER CB    OG     sing N N 330 
SER CB    HB2    sing N N 331 
SER CB    HB3    sing N N 332 
SER OG    HG     sing N N 333 
SER OXT   HXT    sing N N 334 
THR N     CA     sing N N 335 
THR N     H      sing N N 336 
THR N     H2     sing N N 337 
THR CA    C      sing N N 338 
THR CA    CB     sing N N 339 
THR CA    HA     sing N N 340 
THR C     O      doub N N 341 
THR C     OXT    sing N N 342 
THR CB    OG1    sing N N 343 
THR CB    CG2    sing N N 344 
THR CB    HB     sing N N 345 
THR OG1   HG1    sing N N 346 
THR CG2   HG21   sing N N 347 
THR CG2   HG22   sing N N 348 
THR CG2   HG23   sing N N 349 
THR OXT   HXT    sing N N 350 
TRP N     CA     sing N N 351 
TRP N     H      sing N N 352 
TRP N     H2     sing N N 353 
TRP CA    C      sing N N 354 
TRP CA    CB     sing N N 355 
TRP CA    HA     sing N N 356 
TRP C     O      doub N N 357 
TRP C     OXT    sing N N 358 
TRP CB    CG     sing N N 359 
TRP CB    HB2    sing N N 360 
TRP CB    HB3    sing N N 361 
TRP CG    CD1    doub Y N 362 
TRP CG    CD2    sing Y N 363 
TRP CD1   NE1    sing Y N 364 
TRP CD1   HD1    sing N N 365 
TRP CD2   CE2    doub Y N 366 
TRP CD2   CE3    sing Y N 367 
TRP NE1   CE2    sing Y N 368 
TRP NE1   HE1    sing N N 369 
TRP CE2   CZ2    sing Y N 370 
TRP CE3   CZ3    doub Y N 371 
TRP CE3   HE3    sing N N 372 
TRP CZ2   CH2    doub Y N 373 
TRP CZ2   HZ2    sing N N 374 
TRP CZ3   CH2    sing Y N 375 
TRP CZ3   HZ3    sing N N 376 
TRP CH2   HH2    sing N N 377 
TRP OXT   HXT    sing N N 378 
TYR N     CA     sing N N 379 
TYR N     H      sing N N 380 
TYR N     H2     sing N N 381 
TYR CA    C      sing N N 382 
TYR CA    CB     sing N N 383 
TYR CA    HA     sing N N 384 
TYR C     O      doub N N 385 
TYR C     OXT    sing N N 386 
TYR CB    CG     sing N N 387 
TYR CB    HB2    sing N N 388 
TYR CB    HB3    sing N N 389 
TYR CG    CD1    doub Y N 390 
TYR CG    CD2    sing Y N 391 
TYR CD1   CE1    sing Y N 392 
TYR CD1   HD1    sing N N 393 
TYR CD2   CE2    doub Y N 394 
TYR CD2   HD2    sing N N 395 
TYR CE1   CZ     doub Y N 396 
TYR CE1   HE1    sing N N 397 
TYR CE2   CZ     sing Y N 398 
TYR CE2   HE2    sing N N 399 
TYR CZ    OH     sing N N 400 
TYR OH    HH     sing N N 401 
TYR OXT   HXT    sing N N 402 
VAL N     CA     sing N N 403 
VAL N     H      sing N N 404 
VAL N     H2     sing N N 405 
VAL CA    C      sing N N 406 
VAL CA    CB     sing N N 407 
VAL CA    HA     sing N N 408 
VAL C     O      doub N N 409 
VAL C     OXT    sing N N 410 
VAL CB    CG1    sing N N 411 
VAL CB    CG2    sing N N 412 
VAL CB    HB     sing N N 413 
VAL CG1   HG11   sing N N 414 
VAL CG1   HG12   sing N N 415 
VAL CG1   HG13   sing N N 416 
VAL CG2   HG21   sing N N 417 
VAL CG2   HG22   sing N N 418 
VAL CG2   HG23   sing N N 419 
VAL OXT   HXT    sing N N 420 
XC9 CL2   C18    sing N N 421 
XC9 C18   C19    doub Y N 422 
XC9 C18   C17    sing Y N 423 
XC9 C19   C20    sing Y N 424 
XC9 C17   C16    doub Y N 425 
XC9 C20   C15    doub Y N 426 
XC9 C16   C15    sing Y N 427 
XC9 C15   N10    sing N N 428 
XC9 C12   C11    sing N N 429 
XC9 C12   N6     sing N N 430 
XC9 N10   C14    sing N N 431 
XC9 C11   C10    sing N N 432 
XC9 N8    C14    sing N N 433 
XC9 N8    C13    sing N N 434 
XC9 N6    C13    sing N N 435 
XC9 C14   N9     doub N N 436 
XC9 C13   N7     doub N N 437 
XC9 C10   H1     sing N N 438 
XC9 C10   H2     sing N N 439 
XC9 C11   H4     sing N N 440 
XC9 C11   H5     sing N N 441 
XC9 C12   H6     sing N N 442 
XC9 C12   H7     sing N N 443 
XC9 N6    H8     sing N N 444 
XC9 N7    H9     sing N N 445 
XC9 N8    H10    sing N N 446 
XC9 N9    H11    sing N N 447 
XC9 N10   H12    sing N N 448 
XC9 C16   H13    sing N N 449 
XC9 C17   H14    sing N N 450 
XC9 C19   H15    sing N N 451 
XC9 C20   H16    sing N N 452 
XC9 C10   C1     sing N N 453 
XC9 C1    C2     sing N N 454 
XC9 C2    C3     sing N N 455 
XC9 C3    N1     sing N N 456 
XC9 N1    C4     sing N N 457 
XC9 C4    N2     sing N N 458 
XC9 N2    C5     sing N N 459 
XC9 C5    N3     sing N N 460 
XC9 N3    C6     sing N N 461 
XC9 C6    C7     sing Y N 462 
XC9 C7    C8     doub Y N 463 
XC9 C8    C9     sing Y N 464 
XC9 C9    C21    doub Y N 465 
XC9 C21   C22    sing Y N 466 
XC9 C22   C6     doub Y N 467 
XC9 C9    CL1    sing N N 468 
XC9 C1    H3     sing N N 469 
XC9 C1    H17    sing N N 470 
XC9 C2    H18    sing N N 471 
XC9 C2    H19    sing N N 472 
XC9 C3    H20    sing N N 473 
XC9 C3    H21    sing N N 474 
XC9 N3    H26    sing N N 475 
XC9 C7    H27    sing N N 476 
XC9 C8    H28    sing N N 477 
XC9 C21   H29    sing N N 478 
XC9 C22   H30    sing N N 479 
XC9 C4    N4     doub N N 480 
XC9 C5    N5     doub N N 481 
XC9 N1    H31    sing N N 482 
XC9 N2    H22    sing N N 483 
XC9 N4    H23    sing N N 484 
XC9 N5    H24    sing N N 485 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 2217714  1 
'National Natural Science Foundation of China (NSFC)' China 22207133 2 
# 
_atom_sites.entry_id                    8XM4 
_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]   0.015288 
_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]   0.013148 
_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]   0.008400 
_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  
CL 
N  
O  
P  
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     . ALA A 1 12  ? -38.901 12.335  2.829   1.00 41.16 ? 2    ALA A N     1 
ATOM   2    C  CA    . ALA A 1 12  ? -37.847 12.739  1.835   1.00 39.33 ? 2    ALA A CA    1 
ATOM   3    C  C     . ALA A 1 12  ? -37.365 11.549  0.999   1.00 37.02 ? 2    ALA A C     1 
ATOM   4    O  O     . ALA A 1 12  ? -37.568 10.399  1.370   1.00 37.58 ? 2    ALA A O     1 
ATOM   5    C  CB    . ALA A 1 12  ? -36.678 13.422  2.545   1.00 40.63 ? 2    ALA A CB    1 
ATOM   6    N  N     . LYS A 1 13  ? -36.765 11.838  -0.153  1.00 33.18 ? 3    LYS A N     1 
ATOM   7    C  CA    . LYS A 1 13  ? -36.150 10.814  -0.985  1.00 30.60 ? 3    LYS A CA    1 
ATOM   8    C  C     . LYS A 1 13  ? -35.012 10.130  -0.224  1.00 28.62 ? 3    LYS A C     1 
ATOM   9    O  O     . LYS A 1 13  ? -34.234 10.797  0.463   1.00 27.38 ? 3    LYS A O     1 
ATOM   10   C  CB    . LYS A 1 13  ? -35.581 11.450  -2.253  1.00 30.35 ? 3    LYS A CB    1 
ATOM   11   C  CG    . LYS A 1 13  ? -36.620 11.983  -3.224  1.00 30.48 ? 3    LYS A CG    1 
ATOM   12   C  CD    . LYS A 1 13  ? -35.976 12.442  -4.527  1.00 30.73 ? 3    LYS A CD    1 
ATOM   13   C  CE    . LYS A 1 13  ? -37.031 12.701  -5.585  1.00 31.36 ? 3    LYS A CE    1 
ATOM   14   N  NZ    . LYS A 1 13  ? -36.447 13.276  -6.824  1.00 31.86 ? 3    LYS A NZ    1 
ATOM   15   N  N     . GLU A 1 14  ? -34.918 8.806   -0.346  1.00 27.50 ? 4    GLU A N     1 
ATOM   16   C  CA    . GLU A 1 14  ? -33.794 8.070   0.248   1.00 26.70 ? 4    GLU A CA    1 
ATOM   17   C  C     . GLU A 1 14  ? -32.506 8.418   -0.499  1.00 24.04 ? 4    GLU A C     1 
ATOM   18   O  O     . GLU A 1 14  ? -32.527 8.574   -1.713  1.00 22.40 ? 4    GLU A O     1 
ATOM   19   C  CB    . GLU A 1 14  ? -34.024 6.555   0.184   1.00 29.05 ? 4    GLU A CB    1 
ATOM   20   C  CG    . GLU A 1 14  ? -35.208 6.066   1.014   1.00 31.98 ? 4    GLU A CG    1 
ATOM   21   C  CD    . GLU A 1 14  ? -35.069 6.324   2.514   1.00 34.91 ? 4    GLU A CD    1 
ATOM   22   O  OE1   . GLU A 1 14  ? -33.944 6.236   3.063   1.00 37.62 ? 4    GLU A OE1   1 
ATOM   23   O  OE2   . GLU A 1 14  ? -36.110 6.604   3.161   1.00 37.52 ? 4    GLU A OE2   1 
ATOM   24   N  N     . THR A 1 15  ? -31.406 8.535   0.235   1.00 21.97 ? 5    THR A N     1 
ATOM   25   C  CA    . THR A 1 15  ? -30.116 8.896   -0.372  1.00 21.45 ? 5    THR A CA    1 
ATOM   26   C  C     . THR A 1 15  ? -29.459 7.658   -0.976  1.00 20.81 ? 5    THR A C     1 
ATOM   27   O  O     . THR A 1 15  ? -29.659 6.531   -0.500  1.00 20.51 ? 5    THR A O     1 
ATOM   28   C  CB    . THR A 1 15  ? -29.142 9.563   0.621   1.00 21.77 ? 5    THR A CB    1 
ATOM   29   O  OG1   . THR A 1 15  ? -28.780 8.651   1.660   1.00 21.02 ? 5    THR A OG1   1 
ATOM   30   C  CG2   . THR A 1 15  ? -29.757 10.813  1.242   1.00 22.26 ? 5    THR A CG2   1 
ATOM   31   N  N     . PHE A 1 16  ? -28.673 7.883   -2.029  1.00 20.07 ? 6    PHE A N     1 
ATOM   32   C  CA    . PHE A 1 16  ? -27.867 6.840   -2.637  1.00 19.74 ? 6    PHE A CA    1 
ATOM   33   C  C     . PHE A 1 16  ? -26.547 7.460   -3.044  1.00 18.99 ? 6    PHE A C     1 
ATOM   34   O  O     . PHE A 1 16  ? -26.531 8.381   -3.850  1.00 19.43 ? 6    PHE A O     1 
ATOM   35   C  CB    . PHE A 1 16  ? -28.562 6.236   -3.858  1.00 20.07 ? 6    PHE A CB    1 
ATOM   36   C  CG    . PHE A 1 16  ? -27.808 5.089   -4.470  1.00 20.42 ? 6    PHE A CG    1 
ATOM   37   C  CD1   . PHE A 1 16  ? -26.915 5.306   -5.507  1.00 20.87 ? 6    PHE A CD1   1 
ATOM   38   C  CD2   . PHE A 1 16  ? -27.977 3.789   -3.993  1.00 21.63 ? 6    PHE A CD2   1 
ATOM   39   C  CE1   . PHE A 1 16  ? -26.220 4.247   -6.072  1.00 20.79 ? 6    PHE A CE1   1 
ATOM   40   C  CE2   . PHE A 1 16  ? -27.274 2.730   -4.552  1.00 21.70 ? 6    PHE A CE2   1 
ATOM   41   C  CZ    . PHE A 1 16  ? -26.388 2.967   -5.577  1.00 20.97 ? 6    PHE A CZ    1 
ATOM   42   N  N     . TYR A 1 17  ? -25.457 6.957   -2.469  1.00 18.20 ? 7    TYR A N     1 
ATOM   43   C  CA    . TYR A 1 17  ? -24.124 7.484   -2.710  1.00 17.79 ? 7    TYR A CA    1 
ATOM   44   C  C     . TYR A 1 17  ? -23.268 6.428   -3.388  1.00 17.28 ? 7    TYR A C     1 
ATOM   45   O  O     . TYR A 1 17  ? -23.091 5.322   -2.858  1.00 16.82 ? 7    TYR A O     1 
ATOM   46   C  CB    . TYR A 1 17  ? -23.513 7.948   -1.389  1.00 17.48 ? 7    TYR A CB    1 
ATOM   47   C  CG    . TYR A 1 17  ? -22.117 8.538   -1.458  1.00 16.97 ? 7    TYR A CG    1 
ATOM   48   C  CD1   . TYR A 1 17  ? -21.707 9.322   -2.549  1.00 17.00 ? 7    TYR A CD1   1 
ATOM   49   C  CD2   . TYR A 1 17  ? -21.210 8.348   -0.418  1.00 17.22 ? 7    TYR A CD2   1 
ATOM   50   C  CE1   . TYR A 1 17  ? -20.453 9.886   -2.587  1.00 17.03 ? 7    TYR A CE1   1 
ATOM   51   C  CE2   . TYR A 1 17  ? -19.949 8.910   -0.459  1.00 16.78 ? 7    TYR A CE2   1 
ATOM   52   C  CZ    . TYR A 1 17  ? -19.575 9.658   -1.554  1.00 17.20 ? 7    TYR A CZ    1 
ATOM   53   O  OH    . TYR A 1 17  ? -18.346 10.233  -1.615  1.00 17.62 ? 7    TYR A OH    1 
ATOM   54   N  N     . ILE A 1 18  ? -22.741 6.772   -4.563  1.00 17.39 ? 8    ILE A N     1 
ATOM   55   C  CA    . ILE A 1 18  ? -21.895 5.856   -5.359  1.00 17.80 ? 8    ILE A CA    1 
ATOM   56   C  C     . ILE A 1 18  ? -20.608 6.552   -5.779  1.00 16.93 ? 8    ILE A C     1 
ATOM   57   O  O     . ILE A 1 18  ? -20.618 7.745   -6.079  1.00 16.17 ? 8    ILE A O     1 
ATOM   58   C  CB    . ILE A 1 18  ? -22.651 5.264   -6.574  1.00 18.48 ? 8    ILE A CB    1 
ATOM   59   C  CG1   . ILE A 1 18  ? -21.732 4.367   -7.406  1.00 19.63 ? 8    ILE A CG1   1 
ATOM   60   C  CG2   . ILE A 1 18  ? -23.304 6.341   -7.417  1.00 18.47 ? 8    ILE A CG2   1 
ATOM   61   C  CD1   . ILE A 1 18  ? -22.479 3.448   -8.319  1.00 20.68 ? 8    ILE A CD1   1 
ATOM   62   N  N     . THR A 1 19  ? -19.492 5.816   -5.743  1.00 16.02 ? 9    THR A N     1 
ATOM   63   C  CA    . THR A 1 19  ? -18.187 6.363   -6.064  1.00 16.35 ? 9    THR A CA    1 
ATOM   64   C  C     . THR A 1 19  ? -17.476 5.496   -7.095  1.00 16.58 ? 9    THR A C     1 
ATOM   65   O  O     . THR A 1 19  ? -17.690 4.260   -7.149  1.00 17.26 ? 9    THR A O     1 
ATOM   66   C  CB    . THR A 1 19  ? -17.291 6.462   -4.803  1.00 15.80 ? 9    THR A CB    1 
ATOM   67   O  OG1   . THR A 1 19  ? -16.956 5.141   -4.391  1.00 16.33 ? 9    THR A OG1   1 
ATOM   68   C  CG2   . THR A 1 19  ? -17.973 7.199   -3.642  1.00 15.52 ? 9    THR A CG2   1 
ATOM   69   N  N     . THR A 1 20  ? -16.635 6.129   -7.913  1.00 16.85 ? 10   THR A N     1 
ATOM   70   C  CA    . THR A 1 20  ? -15.611 5.414   -8.674  1.00 16.98 ? 10   THR A CA    1 
ATOM   71   C  C     . THR A 1 20  ? -14.327 5.477   -7.865  1.00 16.93 ? 10   THR A C     1 
ATOM   72   O  O     . THR A 1 20  ? -14.236 6.254   -6.910  1.00 17.46 ? 10   THR A O     1 
ATOM   73   C  CB    . THR A 1 20  ? -15.301 6.055   -10.053 1.00 17.09 ? 10   THR A CB    1 
ATOM   74   O  OG1   . THR A 1 20  ? -14.523 7.243   -9.868  1.00 17.85 ? 10   THR A OG1   1 
ATOM   75   C  CG2   . THR A 1 20  ? -16.526 6.398   -10.823 1.00 17.28 ? 10   THR A CG2   1 
ATOM   76   N  N     . PRO A 1 21  ? -13.293 4.726   -8.274  1.00 16.86 ? 11   PRO A N     1 
ATOM   77   C  CA    . PRO A 1 21  ? -11.977 4.997   -7.710  1.00 17.43 ? 11   PRO A CA    1 
ATOM   78   C  C     . PRO A 1 21  ? -11.490 6.352   -8.192  1.00 17.44 ? 11   PRO A C     1 
ATOM   79   O  O     . PRO A 1 21  ? -11.952 6.853   -9.225  1.00 18.26 ? 11   PRO A O     1 
ATOM   80   C  CB    . PRO A 1 21  ? -11.096 3.893   -8.307  1.00 17.54 ? 11   PRO A CB    1 
ATOM   81   C  CG    . PRO A 1 21  ? -12.052 2.872   -8.823  1.00 17.35 ? 11   PRO A CG    1 
ATOM   82   C  CD    . PRO A 1 21  ? -13.198 3.698   -9.321  1.00 17.43 ? 11   PRO A CD    1 
ATOM   83   N  N     . ILE A 1 22  ? -10.578 6.940   -7.442  1.00 17.20 ? 12   ILE A N     1 
ATOM   84   C  CA    . ILE A 1 22  ? -9.905  8.148   -7.906  1.00 17.21 ? 12   ILE A CA    1 
ATOM   85   C  C     . ILE A 1 22  ? -8.732  7.663   -8.747  1.00 17.21 ? 12   ILE A C     1 
ATOM   86   O  O     . ILE A 1 22  ? -7.978  6.777   -8.328  1.00 18.78 ? 12   ILE A O     1 
ATOM   87   C  CB    . ILE A 1 22  ? -9.553  9.163   -6.790  1.00 17.22 ? 12   ILE A CB    1 
ATOM   88   C  CG1   . ILE A 1 22  ? -8.748  8.532   -5.642  1.00 17.35 ? 12   ILE A CG1   1 
ATOM   89   C  CG2   . ILE A 1 22  ? -10.848 9.805   -6.268  1.00 17.37 ? 12   ILE A CG2   1 
ATOM   90   C  CD1   . ILE A 1 22  ? -8.101  9.561   -4.727  1.00 17.94 ? 12   ILE A CD1   1 
ATOM   91   N  N     . TYR A 1 23  ? -8.651  8.164   -9.971  1.00 17.31 ? 13   TYR A N     1 
ATOM   92   C  CA    . TYR A 1 23  ? -7.682  7.664   -10.957 1.00 17.86 ? 13   TYR A CA    1 
ATOM   93   C  C     . TYR A 1 23  ? -6.336  8.373   -10.845 1.00 18.20 ? 13   TYR A C     1 
ATOM   94   O  O     . TYR A 1 23  ? -6.267  9.526   -10.420 1.00 17.90 ? 13   TYR A O     1 
ATOM   95   C  CB    . TYR A 1 23  ? -8.268  7.785   -12.351 1.00 18.20 ? 13   TYR A CB    1 
ATOM   96   C  CG    . TYR A 1 23  ? -9.624  7.140   -12.479 1.00 18.13 ? 13   TYR A CG    1 
ATOM   97   C  CD1   . TYR A 1 23  ? -9.801  5.795   -12.205 1.00 17.81 ? 13   TYR A CD1   1 
ATOM   98   C  CD2   . TYR A 1 23  ? -10.743 7.890   -12.847 1.00 18.49 ? 13   TYR A CD2   1 
ATOM   99   C  CE1   . TYR A 1 23  ? -11.047 5.196   -12.329 1.00 18.61 ? 13   TYR A CE1   1 
ATOM   100  C  CE2   . TYR A 1 23  ? -12.000 7.307   -12.960 1.00 18.45 ? 13   TYR A CE2   1 
ATOM   101  C  CZ    . TYR A 1 23  ? -12.142 5.954   -12.703 1.00 18.17 ? 13   TYR A CZ    1 
ATOM   102  O  OH    . TYR A 1 23  ? -13.375 5.346   -12.794 1.00 18.89 ? 13   TYR A OH    1 
ATOM   103  N  N     . TYR A 1 24  ? -5.267  7.666   -11.221 1.00 18.45 ? 14   TYR A N     1 
ATOM   104  C  CA    . TYR A 1 24  ? -3.898  8.149   -11.024 1.00 19.33 ? 14   TYR A CA    1 
ATOM   105  C  C     . TYR A 1 24  ? -3.371  8.730   -12.331 1.00 20.40 ? 14   TYR A C     1 
ATOM   106  O  O     . TYR A 1 24  ? -3.103  7.972   -13.271 1.00 21.45 ? 14   TYR A O     1 
ATOM   107  C  CB    . TYR A 1 24  ? -3.006  7.005   -10.537 1.00 19.75 ? 14   TYR A CB    1 
ATOM   108  C  CG    . TYR A 1 24  ? -1.740  7.466   -9.853  1.00 19.98 ? 14   TYR A CG    1 
ATOM   109  C  CD1   . TYR A 1 24  ? -1.789  8.103   -8.624  1.00 19.42 ? 14   TYR A CD1   1 
ATOM   110  C  CD2   . TYR A 1 24  ? -0.489  7.260   -10.433 1.00 20.61 ? 14   TYR A CD2   1 
ATOM   111  C  CE1   . TYR A 1 24  ? -0.645  8.531   -7.994  1.00 19.75 ? 14   TYR A CE1   1 
ATOM   112  C  CE2   . TYR A 1 24  ? 0.667   7.672   -9.799  1.00 20.60 ? 14   TYR A CE2   1 
ATOM   113  C  CZ    . TYR A 1 24  ? 0.590   8.304   -8.570  1.00 20.39 ? 14   TYR A CZ    1 
ATOM   114  O  OH    . TYR A 1 24  ? 1.737   8.741   -7.924  1.00 21.07 ? 14   TYR A OH    1 
ATOM   115  N  N     . PRO A 1 25  ? -3.221  10.067  -12.421 1.00 20.75 ? 15   PRO A N     1 
ATOM   116  C  CA    . PRO A 1 25  ? -2.940  10.679  -13.723 1.00 21.56 ? 15   PRO A CA    1 
ATOM   117  C  C     . PRO A 1 25  ? -1.451  10.663  -14.122 1.00 22.50 ? 15   PRO A C     1 
ATOM   118  O  O     . PRO A 1 25  ? -0.879  11.709  -14.467 1.00 23.10 ? 15   PRO A O     1 
ATOM   119  C  CB    . PRO A 1 25  ? -3.487  12.100  -13.543 1.00 21.61 ? 15   PRO A CB    1 
ATOM   120  C  CG    . PRO A 1 25  ? -3.235  12.389  -12.111 1.00 21.44 ? 15   PRO A CG    1 
ATOM   121  C  CD    . PRO A 1 25  ? -3.470  11.095  -11.393 1.00 21.04 ? 15   PRO A CD    1 
ATOM   122  N  N     . SER A 1 26  ? -0.843  9.480   -14.083 1.00 23.08 ? 16   SER A N     1 
ATOM   123  C  CA    . SER A 1 26  ? 0.552   9.280   -14.505 1.00 24.36 ? 16   SER A CA    1 
ATOM   124  C  C     . SER A 1 26  ? 0.624   9.104   -16.026 1.00 25.47 ? 16   SER A C     1 
ATOM   125  O  O     . SER A 1 26  ? 1.717   9.056   -16.625 1.00 27.28 ? 16   SER A O     1 
ATOM   126  C  CB    . SER A 1 26  ? 1.133   8.060   -13.801 1.00 24.90 ? 16   SER A CB    1 
ATOM   127  O  OG    . SER A 1 26  ? 0.349   6.927   -14.085 1.00 25.18 ? 16   SER A OG    1 
ATOM   128  N  N     . GLY A 1 27  ? -0.542  8.930   -16.631 1.00 25.60 ? 17   GLY A N     1 
ATOM   129  C  CA    . GLY A 1 27  ? -0.714  8.953   -18.077 1.00 25.63 ? 17   GLY A CA    1 
ATOM   130  C  C     . GLY A 1 27  ? -2.174  9.210   -18.405 1.00 25.47 ? 17   GLY A C     1 
ATOM   131  O  O     . GLY A 1 27  ? -2.999  9.364   -17.500 1.00 24.73 ? 17   GLY A O     1 
ATOM   132  N  N     . ASN A 1 28  ? -2.498  9.263   -19.693 1.00 26.10 ? 18   ASN A N     1 
ATOM   133  C  CA    . ASN A 1 28  ? -3.882  9.510   -20.127 1.00 26.53 ? 18   ASN A CA    1 
ATOM   134  C  C     . ASN A 1 28  ? -4.779  8.347   -19.727 1.00 25.13 ? 18   ASN A C     1 
ATOM   135  O  O     . ASN A 1 28  ? -4.334  7.193   -19.689 1.00 24.22 ? 18   ASN A O     1 
ATOM   136  C  CB    . ASN A 1 28  ? -3.966  9.673   -21.644 1.00 28.40 ? 18   ASN A CB    1 
ATOM   137  C  CG    . ASN A 1 28  ? -3.287  10.929  -22.148 1.00 30.29 ? 18   ASN A CG    1 
ATOM   138  O  OD1   . ASN A 1 28  ? -3.117  11.895  -21.429 1.00 32.46 ? 18   ASN A OD1   1 
ATOM   139  N  ND2   . ASN A 1 28  ? -2.906  10.912  -23.419 1.00 33.92 ? 18   ASN A ND2   1 
ATOM   140  N  N     . LEU A 1 29  ? -6.041  8.651   -19.430 1.00 23.39 ? 19   LEU A N     1 
ATOM   141  C  CA    . LEU A 1 29  ? -7.008  7.591   -19.147 1.00 23.00 ? 19   LEU A CA    1 
ATOM   142  C  C     . LEU A 1 29  ? -7.413  6.901   -20.453 1.00 22.82 ? 19   LEU A C     1 
ATOM   143  O  O     . LEU A 1 29  ? -7.302  7.468   -21.547 1.00 24.23 ? 19   LEU A O     1 
ATOM   144  C  CB    . LEU A 1 29  ? -8.214  8.147   -18.373 1.00 22.64 ? 19   LEU A CB    1 
ATOM   145  C  CG    . LEU A 1 29  ? -7.840  8.891   -17.079 1.00 22.92 ? 19   LEU A CG    1 
ATOM   146  C  CD1   . LEU A 1 29  ? -9.096  9.164   -16.262 1.00 23.08 ? 19   LEU A CD1   1 
ATOM   147  C  CD2   . LEU A 1 29  ? -6.825  8.160   -16.207 1.00 23.05 ? 19   LEU A CD2   1 
ATOM   148  N  N     . HIS A 1 30  ? -7.848  5.653   -20.323 1.00 22.30 ? 20   HIS A N     1 
ATOM   149  C  CA    . HIS A 1 30  ? -8.201  4.810   -21.453 1.00 22.35 ? 20   HIS A CA    1 
ATOM   150  C  C     . HIS A 1 30  ? -9.595  4.216   -21.227 1.00 22.06 ? 20   HIS A C     1 
ATOM   151  O  O     . HIS A 1 30  ? -10.278 4.576   -20.253 1.00 21.16 ? 20   HIS A O     1 
ATOM   152  C  CB    . HIS A 1 30  ? -7.118  3.758   -21.702 1.00 22.86 ? 20   HIS A CB    1 
ATOM   153  C  CG    . HIS A 1 30  ? -6.787  2.912   -20.519 1.00 22.84 ? 20   HIS A CG    1 
ATOM   154  N  ND1   . HIS A 1 30  ? -7.688  2.045   -19.943 1.00 23.39 ? 20   HIS A ND1   1 
ATOM   155  C  CD2   . HIS A 1 30  ? -5.627  2.757   -19.836 1.00 23.33 ? 20   HIS A CD2   1 
ATOM   156  C  CE1   . HIS A 1 30  ? -7.106  1.416   -18.939 1.00 23.73 ? 20   HIS A CE1   1 
ATOM   157  N  NE2   . HIS A 1 30  ? -5.853  1.826   -18.856 1.00 23.14 ? 20   HIS A NE2   1 
ATOM   158  N  N     . ILE A 1 31  ? -10.046 3.347   -22.124 1.00 21.99 ? 21   ILE A N     1 
ATOM   159  C  CA    . ILE A 1 31  ? -11.427 2.818   -22.020 1.00 22.21 ? 21   ILE A CA    1 
ATOM   160  C  C     . ILE A 1 31  ? -11.723 1.994   -20.759 1.00 21.55 ? 21   ILE A C     1 
ATOM   161  O  O     . ILE A 1 31  ? -12.888 1.841   -20.390 1.00 21.03 ? 21   ILE A O     1 
ATOM   162  C  CB    . ILE A 1 31  ? -11.904 2.059   -23.288 1.00 23.56 ? 21   ILE A CB    1 
ATOM   163  C  CG1   . ILE A 1 31  ? -11.020 0.850   -23.587 1.00 24.76 ? 21   ILE A CG1   1 
ATOM   164  C  CG2   . ILE A 1 31  ? -11.981 3.020   -24.466 1.00 24.16 ? 21   ILE A CG2   1 
ATOM   165  C  CD1   . ILE A 1 31  ? -11.656 -0.097  -24.599 1.00 25.33 ? 21   ILE A CD1   1 
ATOM   166  N  N     . GLY A 1 32  ? -10.690 1.445   -20.124 1.00 20.42 ? 22   GLY A N     1 
ATOM   167  C  CA    . GLY A 1 32  ? -10.801 0.860   -18.774 1.00 20.19 ? 22   GLY A CA    1 
ATOM   168  C  C     . GLY A 1 32  ? -11.356 1.821   -17.727 1.00 19.55 ? 22   GLY A C     1 
ATOM   169  O  O     . GLY A 1 32  ? -12.297 1.504   -16.973 1.00 19.07 ? 22   GLY A O     1 
ATOM   170  N  N     . HIS A 1 33  ? -10.788 3.017   -17.705 1.00 19.63 ? 23   HIS A N     1 
ATOM   171  C  CA    . HIS A 1 33  ? -11.283 4.094   -16.853 1.00 19.14 ? 23   HIS A CA    1 
ATOM   172  C  C     . HIS A 1 33  ? -12.676 4.545   -17.266 1.00 19.12 ? 23   HIS A C     1 
ATOM   173  O  O     . HIS A 1 33  ? -13.524 4.786   -16.405 1.00 19.42 ? 23   HIS A O     1 
ATOM   174  C  CB    . HIS A 1 33  ? -10.298 5.267   -16.837 1.00 19.38 ? 23   HIS A CB    1 
ATOM   175  C  CG    . HIS A 1 33  ? -8.907  4.853   -16.474 1.00 19.29 ? 23   HIS A CG    1 
ATOM   176  N  ND1   . HIS A 1 33  ? -7.923  4.648   -17.420 1.00 19.71 ? 23   HIS A ND1   1 
ATOM   177  C  CD2   . HIS A 1 33  ? -8.353  4.536   -15.280 1.00 19.50 ? 23   HIS A CD2   1 
ATOM   178  C  CE1   . HIS A 1 33  ? -6.817  4.246   -16.818 1.00 19.89 ? 23   HIS A CE1   1 
ATOM   179  N  NE2   . HIS A 1 33  ? -7.054  4.161   -15.521 1.00 19.68 ? 23   HIS A NE2   1 
ATOM   180  N  N     . ALA A 1 34  ? -12.919 4.642   -18.571 1.00 19.02 ? 24   ALA A N     1 
ATOM   181  C  CA    . ALA A 1 34  ? -14.249 5.014   -19.067 1.00 19.50 ? 24   ALA A CA    1 
ATOM   182  C  C     . ALA A 1 34  ? -15.310 3.984   -18.683 1.00 19.27 ? 24   ALA A C     1 
ATOM   183  O  O     . ALA A 1 34  ? -16.437 4.348   -18.356 1.00 18.65 ? 24   ALA A O     1 
ATOM   184  C  CB    . ALA A 1 34  ? -14.230 5.231   -20.572 1.00 19.82 ? 24   ALA A CB    1 
ATOM   185  N  N     . TYR A 1 35  ? -14.929 2.701   -18.701 1.00 20.10 ? 25   TYR A N     1 
ATOM   186  C  CA    . TYR A 1 35  ? -15.808 1.591   -18.321 1.00 20.61 ? 25   TYR A CA    1 
ATOM   187  C  C     . TYR A 1 35  ? -16.337 1.775   -16.893 1.00 19.96 ? 25   TYR A C     1 
ATOM   188  O  O     . TYR A 1 35  ? -17.542 1.773   -16.675 1.00 19.46 ? 25   TYR A O     1 
ATOM   189  C  CB    . TYR A 1 35  ? -15.005 0.297   -18.456 1.00 22.12 ? 25   TYR A CB    1 
ATOM   190  C  CG    . TYR A 1 35  ? -15.688 -1.006  -18.186 1.00 23.33 ? 25   TYR A CG    1 
ATOM   191  C  CD1   . TYR A 1 35  ? -16.821 -1.393  -18.889 1.00 23.95 ? 25   TYR A CD1   1 
ATOM   192  C  CD2   . TYR A 1 35  ? -15.123 -1.920  -17.295 1.00 24.68 ? 25   TYR A CD2   1 
ATOM   193  C  CE1   . TYR A 1 35  ? -17.409 -2.631  -18.666 1.00 25.12 ? 25   TYR A CE1   1 
ATOM   194  C  CE2   . TYR A 1 35  ? -15.700 -3.155  -17.069 1.00 25.26 ? 25   TYR A CE2   1 
ATOM   195  C  CZ    . TYR A 1 35  ? -16.836 -3.509  -17.759 1.00 25.41 ? 25   TYR A CZ    1 
ATOM   196  O  OH    . TYR A 1 35  ? -17.378 -4.744  -17.538 1.00 26.84 ? 25   TYR A OH    1 
ATOM   197  N  N     . SER A 1 36  ? -15.438 1.984   -15.929 1.00 19.28 ? 26   SER A N     1 
ATOM   198  C  CA    . SER A 1 36  ? -15.850 2.219   -14.545 1.00 18.71 ? 26   SER A CA    1 
ATOM   199  C  C     . SER A 1 36  ? -16.743 3.445   -14.398 1.00 18.04 ? 26   SER A C     1 
ATOM   200  O  O     . SER A 1 36  ? -17.776 3.407   -13.708 1.00 18.30 ? 26   SER A O     1 
ATOM   201  C  CB    . SER A 1 36  ? -14.645 2.377   -13.626 1.00 19.10 ? 26   SER A CB    1 
ATOM   202  O  OG    . SER A 1 36  ? -13.945 1.152   -13.508 1.00 20.46 ? 26   SER A OG    1 
ATOM   203  N  N     . THR A 1 37  ? -16.348 4.535   -15.042 1.00 17.56 ? 27   THR A N     1 
ATOM   204  C  CA    . THR A 1 37  ? -17.050 5.806   -14.884 1.00 17.65 ? 27   THR A CA    1 
ATOM   205  C  C     . THR A 1 37  ? -18.405 5.800   -15.572 1.00 18.01 ? 27   THR A C     1 
ATOM   206  O  O     . THR A 1 37  ? -19.373 6.333   -15.019 1.00 17.75 ? 27   THR A O     1 
ATOM   207  C  CB    . THR A 1 37  ? -16.175 6.971   -15.344 1.00 18.15 ? 27   THR A CB    1 
ATOM   208  O  OG1   . THR A 1 37  ? -14.922 6.850   -14.693 1.00 18.81 ? 27   THR A OG1   1 
ATOM   209  C  CG2   . THR A 1 37  ? -16.782 8.311   -14.945 1.00 18.29 ? 27   THR A CG2   1 
ATOM   210  N  N     . VAL A 1 38  ? -18.497 5.164   -16.744 1.00 18.16 ? 28   VAL A N     1 
ATOM   211  C  CA    . VAL A 1 38  ? -19.810 4.968   -17.389 1.00 18.54 ? 28   VAL A CA    1 
ATOM   212  C  C     . VAL A 1 38  ? -20.704 4.031   -16.544 1.00 18.25 ? 28   VAL A C     1 
ATOM   213  O  O     . VAL A 1 38  ? -21.893 4.310   -16.363 1.00 18.61 ? 28   VAL A O     1 
ATOM   214  C  CB    . VAL A 1 38  ? -19.663 4.500   -18.854 1.00 18.66 ? 28   VAL A CB    1 
ATOM   215  C  CG1   . VAL A 1 38  ? -21.010 4.091   -19.451 1.00 19.17 ? 28   VAL A CG1   1 
ATOM   216  C  CG2   . VAL A 1 38  ? -19.048 5.606   -19.701 1.00 18.65 ? 28   VAL A CG2   1 
ATOM   217  N  N     . ALA A 1 39  ? -20.128 2.937   -16.029 1.00 18.17 ? 29   ALA A N     1 
ATOM   218  C  CA    . ALA A 1 39  ? -20.852 2.021   -15.155 1.00 18.25 ? 29   ALA A CA    1 
ATOM   219  C  C     . ALA A 1 39  ? -21.456 2.752   -13.955 1.00 17.89 ? 29   ALA A C     1 
ATOM   220  O  O     . ALA A 1 39  ? -22.644 2.579   -13.646 1.00 18.21 ? 29   ALA A O     1 
ATOM   221  C  CB    . ALA A 1 39  ? -19.953 0.877   -14.705 1.00 18.43 ? 29   ALA A CB    1 
ATOM   222  N  N     . GLY A 1 40  ? -20.645 3.568   -13.282 1.00 17.63 ? 30   GLY A N     1 
ATOM   223  C  CA    . GLY A 1 40  ? -21.124 4.344   -12.137 1.00 17.82 ? 30   GLY A CA    1 
ATOM   224  C  C     . GLY A 1 40  ? -22.194 5.325   -12.560 1.00 17.79 ? 30   GLY A C     1 
ATOM   225  O  O     . GLY A 1 40  ? -23.167 5.544   -11.829 1.00 17.99 ? 30   GLY A O     1 
ATOM   226  N  N     . ASP A 1 41  ? -22.028 5.905   -13.748 1.00 17.69 ? 31   ASP A N     1 
ATOM   227  C  CA    . ASP A 1 41  ? -23.023 6.825   -14.299 1.00 18.06 ? 31   ASP A CA    1 
ATOM   228  C  C     . ASP A 1 41  ? -24.378 6.168   -14.575 1.00 18.09 ? 31   ASP A C     1 
ATOM   229  O  O     . ASP A 1 41  ? -25.438 6.750   -14.245 1.00 18.22 ? 31   ASP A O     1 
ATOM   230  C  CB    . ASP A 1 41  ? -22.501 7.490   -15.574 1.00 18.37 ? 31   ASP A CB    1 
ATOM   231  C  CG    . ASP A 1 41  ? -23.371 8.608   -16.028 1.00 18.71 ? 31   ASP A CG    1 
ATOM   232  O  OD1   . ASP A 1 41  ? -23.550 9.561   -15.237 1.00 19.75 ? 31   ASP A OD1   1 
ATOM   233  O  OD2   . ASP A 1 41  ? -23.896 8.555   -17.157 1.00 19.27 ? 31   ASP A OD2   1 
ATOM   234  N  N     . VAL A 1 42  ? -24.356 4.962   -15.133 1.00 17.98 ? 32   VAL A N     1 
ATOM   235  C  CA    . VAL A 1 42  ? -25.597 4.205   -15.378 1.00 18.63 ? 32   VAL A CA    1 
ATOM   236  C  C     . VAL A 1 42  ? -26.314 3.925   -14.043 1.00 18.48 ? 32   VAL A C     1 
ATOM   237  O  O     . VAL A 1 42  ? -27.527 4.115   -13.938 1.00 19.83 ? 32   VAL A O     1 
ATOM   238  C  CB    . VAL A 1 42  ? -25.315 2.895   -16.134 1.00 18.76 ? 32   VAL A CB    1 
ATOM   239  C  CG1   . VAL A 1 42  ? -26.563 2.037   -16.222 1.00 19.08 ? 32   VAL A CG1   1 
ATOM   240  C  CG2   . VAL A 1 42  ? -24.798 3.184   -17.541 1.00 18.88 ? 32   VAL A CG2   1 
ATOM   241  N  N     . ILE A 1 43  ? -25.559 3.511   -13.026 1.00 18.89 ? 33   ILE A N     1 
ATOM   242  C  CA    . ILE A 1 43  ? -26.136 3.260   -11.703 1.00 19.57 ? 33   ILE A CA    1 
ATOM   243  C  C     . ILE A 1 43  ? -26.761 4.548   -11.178 1.00 19.39 ? 33   ILE A C     1 
ATOM   244  O  O     . ILE A 1 43  ? -27.906 4.540   -10.717 1.00 20.01 ? 33   ILE A O     1 
ATOM   245  C  CB    . ILE A 1 43  ? -25.099 2.712   -10.704 1.00 19.97 ? 33   ILE A CB    1 
ATOM   246  C  CG1   . ILE A 1 43  ? -24.562 1.344   -11.169 1.00 20.32 ? 33   ILE A CG1   1 
ATOM   247  C  CG2   . ILE A 1 43  ? -25.729 2.561   -9.329  1.00 20.62 ? 33   ILE A CG2   1 
ATOM   248  C  CD1   . ILE A 1 43  ? -23.315 0.877   -10.445 1.00 21.08 ? 33   ILE A CD1   1 
ATOM   249  N  N     . ALA A 1 44  ? -26.008 5.643   -11.228 1.00 19.05 ? 34   ALA A N     1 
ATOM   250  C  CA    . ALA A 1 44  ? -26.491 6.940   -10.752 1.00 19.30 ? 34   ALA A CA    1 
ATOM   251  C  C     . ALA A 1 44  ? -27.770 7.389   -11.475 1.00 19.73 ? 34   ALA A C     1 
ATOM   252  O  O     . ALA A 1 44  ? -28.744 7.770   -10.830 1.00 19.73 ? 34   ALA A O     1 
ATOM   253  C  CB    . ALA A 1 44  ? -25.394 7.992   -10.887 1.00 19.40 ? 34   ALA A CB    1 
ATOM   254  N  N     . ARG A 1 45  ? -27.766 7.304   -12.800 1.00 19.20 ? 35   ARG A N     1 
ATOM   255  C  CA    . ARG A 1 45  ? -28.914 7.706   -13.605 1.00 20.18 ? 35   ARG A CA    1 
ATOM   256  C  C     . ARG A 1 45  ? -30.126 6.827   -13.320 1.00 20.60 ? 35   ARG A C     1 
ATOM   257  O  O     . ARG A 1 45  ? -31.250 7.330   -13.211 1.00 21.27 ? 35   ARG A O     1 
ATOM   258  C  CB    . ARG A 1 45  ? -28.560 7.689   -15.092 1.00 20.62 ? 35   ARG A CB    1 
ATOM   259  C  CG    . ARG A 1 45  ? -27.608 8.798   -15.515 1.00 20.92 ? 35   ARG A CG    1 
ATOM   260  C  CD    . ARG A 1 45  ? -27.187 8.661   -16.971 1.00 21.39 ? 35   ARG A CD    1 
ATOM   261  N  NE    . ARG A 1 45  ? -26.352 9.790   -17.399 1.00 21.80 ? 35   ARG A NE    1 
ATOM   262  C  CZ    . ARG A 1 45  ? -26.791 11.009  -17.738 1.00 22.91 ? 35   ARG A CZ    1 
ATOM   263  N  NH1   . ARG A 1 45  ? -28.089 11.293  -17.776 1.00 23.76 ? 35   ARG A NH1   1 
ATOM   264  N  NH2   . ARG A 1 45  ? -25.917 11.951  -18.085 1.00 22.72 ? 35   ARG A NH2   1 
ATOM   265  N  N     . TYR A 1 46  ? -29.901 5.525   -13.164 1.00 20.43 ? 36   TYR A N     1 
ATOM   266  C  CA    . TYR A 1 46  ? -30.970 4.586   -12.842 1.00 21.46 ? 36   TYR A CA    1 
ATOM   267  C  C     . TYR A 1 46  ? -31.581 4.908   -11.484 1.00 21.28 ? 36   TYR A C     1 
ATOM   268  O  O     . TYR A 1 46  ? -32.806 5.011   -11.343 1.00 21.24 ? 36   TYR A O     1 
ATOM   269  C  CB    . TYR A 1 46  ? -30.426 3.156   -12.865 1.00 21.96 ? 36   TYR A CB    1 
ATOM   270  C  CG    . TYR A 1 46  ? -31.372 2.092   -12.380 1.00 22.83 ? 36   TYR A CG    1 
ATOM   271  C  CD1   . TYR A 1 46  ? -32.435 1.669   -13.165 1.00 23.26 ? 36   TYR A CD1   1 
ATOM   272  C  CD2   . TYR A 1 46  ? -31.170 1.462   -11.149 1.00 23.92 ? 36   TYR A CD2   1 
ATOM   273  C  CE1   . TYR A 1 46  ? -33.299 0.678   -12.726 1.00 24.45 ? 36   TYR A CE1   1 
ATOM   274  C  CE2   . TYR A 1 46  ? -32.020 0.461   -10.707 1.00 24.48 ? 36   TYR A CE2   1 
ATOM   275  C  CZ    . TYR A 1 46  ? -33.088 0.076   -11.498 1.00 25.15 ? 36   TYR A CZ    1 
ATOM   276  O  OH    . TYR A 1 46  ? -33.956 -0.913  -11.076 1.00 27.66 ? 36   TYR A OH    1 
ATOM   277  N  N     . LYS A 1 47  ? -30.726 5.108   -10.488 1.00 21.38 ? 37   LYS A N     1 
ATOM   278  C  CA    . LYS A 1 47  ? -31.218 5.435   -9.153  1.00 22.34 ? 37   LYS A CA    1 
ATOM   279  C  C     . LYS A 1 47  ? -31.977 6.766   -9.101  1.00 22.29 ? 37   LYS A C     1 
ATOM   280  O  O     . LYS A 1 47  ? -32.981 6.868   -8.384  1.00 23.18 ? 37   LYS A O     1 
ATOM   281  C  CB    . LYS A 1 47  ? -30.066 5.384   -8.143  1.00 22.91 ? 37   LYS A CB    1 
ATOM   282  C  CG    . LYS A 1 47  ? -29.574 3.966   -7.895  1.00 24.22 ? 37   LYS A CG    1 
ATOM   283  C  CD    . LYS A 1 47  ? -30.534 3.213   -6.995  1.00 26.62 ? 37   LYS A CD    1 
ATOM   284  C  CE    . LYS A 1 47  ? -30.196 1.751   -6.850  1.00 29.15 ? 37   LYS A CE    1 
ATOM   285  N  NZ    . LYS A 1 47  ? -31.092 1.186   -5.789  1.00 30.92 ? 37   LYS A NZ    1 
ATOM   286  N  N     . ARG A 1 48  ? -31.539 7.769   -9.865  1.00 21.78 ? 38   ARG A N     1 
ATOM   287  C  CA    . ARG A 1 48  ? -32.278 9.041   -9.950  1.00 22.59 ? 38   ARG A CA    1 
ATOM   288  C  C     . ARG A 1 48  ? -33.675 8.807   -10.539 1.00 23.27 ? 38   ARG A C     1 
ATOM   289  O  O     . ARG A 1 48  ? -34.675 9.327   -10.026 1.00 23.33 ? 38   ARG A O     1 
ATOM   290  C  CB    . ARG A 1 48  ? -31.506 10.095  -10.780 1.00 22.46 ? 38   ARG A CB    1 
ATOM   291  C  CG    . ARG A 1 48  ? -30.248 10.626  -10.090 1.00 21.78 ? 38   ARG A CG    1 
ATOM   292  C  CD    . ARG A 1 48  ? -29.748 11.954  -10.666 1.00 21.75 ? 38   ARG A CD    1 
ATOM   293  N  NE    . ARG A 1 48  ? -28.350 12.211  -10.320 1.00 21.60 ? 38   ARG A NE    1 
ATOM   294  C  CZ    . ARG A 1 48  ? -27.274 11.820  -11.019 1.00 21.54 ? 38   ARG A CZ    1 
ATOM   295  N  NH1   . ARG A 1 48  ? -27.373 11.131  -12.159 1.00 21.54 ? 38   ARG A NH1   1 
ATOM   296  N  NH2   . ARG A 1 48  ? -26.066 12.108  -10.544 1.00 21.36 ? 38   ARG A NH2   1 
ATOM   297  N  N     . MET A 1 49  ? -33.742 7.995   -11.590 1.00 23.26 ? 39   MET A N     1 
ATOM   298  C  CA    . MET A 1 49  ? -35.032 7.615   -12.188 1.00 24.24 ? 39   MET A CA    1 
ATOM   299  C  C     . MET A 1 49  ? -35.942 6.794   -11.249 1.00 24.78 ? 39   MET A C     1 
ATOM   300  O  O     . MET A 1 49  ? -37.185 6.866   -11.369 1.00 24.60 ? 39   MET A O     1 
ATOM   301  C  CB    . MET A 1 49  ? -34.811 6.890   -13.514 1.00 24.71 ? 39   MET A CB    1 
ATOM   302  C  CG    . MET A 1 49  ? -34.447 7.832   -14.642 1.00 25.13 ? 39   MET A CG    1 
ATOM   303  S  SD    . MET A 1 49  ? -34.172 6.947   -16.190 1.00 26.77 ? 39   MET A SD    1 
ATOM   304  C  CE    . MET A 1 49  ? -35.851 6.448   -16.593 1.00 27.36 ? 39   MET A CE    1 
ATOM   305  N  N     A GLN A 1 50  ? -35.338 6.025   -10.342 0.50 24.34 ? 40   GLN A N     1 
ATOM   306  N  N     B GLN A 1 50  ? -35.331 6.021   -10.348 0.50 24.66 ? 40   GLN A N     1 
ATOM   307  C  CA    A GLN A 1 50  ? -36.090 5.300   -9.304  0.50 24.86 ? 40   GLN A CA    1 
ATOM   308  C  CA    B GLN A 1 50  ? -36.067 5.295   -9.302  0.50 25.39 ? 40   GLN A CA    1 
ATOM   309  C  C     A GLN A 1 50  ? -36.453 6.158   -8.084  0.50 25.01 ? 40   GLN A C     1 
ATOM   310  C  C     B GLN A 1 50  ? -36.560 6.187   -8.154  0.50 25.36 ? 40   GLN A C     1 
ATOM   311  O  O     A GLN A 1 50  ? -36.992 5.638   -7.105  0.50 25.13 ? 40   GLN A O     1 
ATOM   312  O  O     B GLN A 1 50  ? -37.325 5.724   -7.304  0.50 25.49 ? 40   GLN A O     1 
ATOM   313  C  CB    A GLN A 1 50  ? -35.318 4.059   -8.843  0.50 25.00 ? 40   GLN A CB    1 
ATOM   314  C  CB    B GLN A 1 50  ? -35.225 4.147   -8.724  0.50 25.96 ? 40   GLN A CB    1 
ATOM   315  C  CG    A GLN A 1 50  ? -35.187 2.974   -9.904  0.50 25.27 ? 40   GLN A CG    1 
ATOM   316  C  CG    B GLN A 1 50  ? -35.125 2.919   -9.618  0.50 26.67 ? 40   GLN A CG    1 
ATOM   317  C  CD    A GLN A 1 50  ? -36.521 2.379   -10.305 0.50 25.65 ? 40   GLN A CD    1 
ATOM   318  C  CD    B GLN A 1 50  ? -34.654 1.677   -8.873  0.50 27.08 ? 40   GLN A CD    1 
ATOM   319  O  OE1   A GLN A 1 50  ? -37.556 3.039   -10.226 0.50 25.70 ? 40   GLN A OE1   1 
ATOM   320  O  OE1   B GLN A 1 50  ? -33.746 1.734   -8.036  0.50 28.15 ? 40   GLN A OE1   1 
ATOM   321  N  NE2   A GLN A 1 50  ? -36.499 1.130   -10.761 0.50 25.78 ? 40   GLN A NE2   1 
ATOM   322  N  NE2   B GLN A 1 50  ? -35.272 0.541   -9.178  0.50 27.58 ? 40   GLN A NE2   1 
ATOM   323  N  N     . GLY A 1 51  ? -36.130 7.449   -8.131  1.00 24.70 ? 41   GLY A N     1 
ATOM   324  C  CA    . GLY A 1 51  ? -36.564 8.419   -7.128  1.00 24.29 ? 41   GLY A CA    1 
ATOM   325  C  C     . GLY A 1 51  ? -35.646 8.606   -5.942  1.00 23.81 ? 41   GLY A C     1 
ATOM   326  O  O     . GLY A 1 51  ? -36.085 9.134   -4.916  1.00 24.11 ? 41   GLY A O     1 
ATOM   327  N  N     . TYR A 1 52  ? -34.386 8.174   -6.073  1.00 22.73 ? 42   TYR A N     1 
ATOM   328  C  CA    . TYR A 1 52  ? -33.389 8.372   -5.023  1.00 22.60 ? 42   TYR A CA    1 
ATOM   329  C  C     . TYR A 1 52  ? -32.750 9.756   -5.139  1.00 22.16 ? 42   TYR A C     1 
ATOM   330  O  O     . TYR A 1 52  ? -32.690 10.342  -6.218  1.00 22.75 ? 42   TYR A O     1 
ATOM   331  C  CB    . TYR A 1 52  ? -32.296 7.293   -5.079  1.00 22.91 ? 42   TYR A CB    1 
ATOM   332  C  CG    . TYR A 1 52  ? -32.757 5.928   -4.620  1.00 23.70 ? 42   TYR A CG    1 
ATOM   333  C  CD1   . TYR A 1 52  ? -32.546 5.495   -3.313  1.00 24.33 ? 42   TYR A CD1   1 
ATOM   334  C  CD2   . TYR A 1 52  ? -33.417 5.072   -5.492  1.00 24.59 ? 42   TYR A CD2   1 
ATOM   335  C  CE1   . TYR A 1 52  ? -32.976 4.247   -2.891  1.00 25.25 ? 42   TYR A CE1   1 
ATOM   336  C  CE2   . TYR A 1 52  ? -33.853 3.826   -5.078  1.00 26.04 ? 42   TYR A CE2   1 
ATOM   337  C  CZ    . TYR A 1 52  ? -33.627 3.419   -3.777  1.00 26.33 ? 42   TYR A CZ    1 
ATOM   338  O  OH    . TYR A 1 52  ? -34.059 2.184   -3.371  1.00 28.02 ? 42   TYR A OH    1 
ATOM   339  N  N     . ASP A 1 53  ? -32.268 10.247  -4.007  1.00 21.96 ? 43   ASP A N     1 
ATOM   340  C  CA    . ASP A 1 53  ? -31.466 11.456  -3.918  1.00 22.13 ? 43   ASP A CA    1 
ATOM   341  C  C     . ASP A 1 53  ? -30.013 10.987  -4.038  1.00 21.40 ? 43   ASP A C     1 
ATOM   342  O  O     . ASP A 1 53  ? -29.406 10.516  -3.069  1.00 20.55 ? 43   ASP A O     1 
ATOM   343  C  CB    . ASP A 1 53  ? -31.767 12.140  -2.574  1.00 23.07 ? 43   ASP A CB    1 
ATOM   344  C  CG    . ASP A 1 53  ? -30.818 13.276  -2.239  1.00 24.35 ? 43   ASP A CG    1 
ATOM   345  O  OD1   . ASP A 1 53  ? -29.914 13.622  -3.031  1.00 23.35 ? 43   ASP A OD1   1 
ATOM   346  O  OD2   . ASP A 1 53  ? -30.976 13.815  -1.129  1.00 26.15 ? 43   ASP A OD2   1 
ATOM   347  N  N     . VAL A 1 54  ? -29.473 11.140  -5.242  1.00 20.16 ? 44   VAL A N     1 
ATOM   348  C  CA    . VAL A 1 54  ? -28.211 10.519  -5.639  1.00 19.68 ? 44   VAL A CA    1 
ATOM   349  C  C     . VAL A 1 54  ? -27.054 11.485  -5.518  1.00 19.58 ? 44   VAL A C     1 
ATOM   350  O  O     . VAL A 1 54  ? -27.188 12.655  -5.866  1.00 19.48 ? 44   VAL A O     1 
ATOM   351  C  CB    . VAL A 1 54  ? -28.296 9.995   -7.080  1.00 19.86 ? 44   VAL A CB    1 
ATOM   352  C  CG1   . VAL A 1 54  ? -26.937 9.528   -7.609  1.00 19.67 ? 44   VAL A CG1   1 
ATOM   353  C  CG2   . VAL A 1 54  ? -29.296 8.847   -7.130  1.00 20.30 ? 44   VAL A CG2   1 
ATOM   354  N  N     . ARG A 1 55  ? -25.928 10.987  -5.003  1.00 19.26 ? 45   ARG A N     1 
ATOM   355  C  CA    . ARG A 1 55  ? -24.652 11.664  -5.184  1.00 19.18 ? 45   ARG A CA    1 
ATOM   356  C  C     . ARG A 1 55  ? -23.675 10.686  -5.819  1.00 18.13 ? 45   ARG A C     1 
ATOM   357  O  O     . ARG A 1 55  ? -23.532 9.553   -5.346  1.00 17.79 ? 45   ARG A O     1 
ATOM   358  C  CB    . ARG A 1 55  ? -24.104 12.245  -3.884  1.00 19.60 ? 45   ARG A CB    1 
ATOM   359  C  CG    . ARG A 1 55  ? -22.973 13.229  -4.131  1.00 20.01 ? 45   ARG A CG    1 
ATOM   360  C  CD    . ARG A 1 55  ? -22.693 14.101  -2.926  1.00 21.17 ? 45   ARG A CD    1 
ATOM   361  N  NE    . ARG A 1 55  ? -21.850 15.259  -3.241  1.00 21.41 ? 45   ARG A NE    1 
ATOM   362  C  CZ    . ARG A 1 55  ? -22.271 16.400  -3.790  1.00 22.46 ? 45   ARG A CZ    1 
ATOM   363  N  NH1   . ARG A 1 55  ? -23.535 16.574  -4.167  1.00 23.05 ? 45   ARG A NH1   1 
ATOM   364  N  NH2   . ARG A 1 55  ? -21.403 17.387  -3.994  1.00 23.36 ? 45   ARG A NH2   1 
ATOM   365  N  N     . TYR A 1 56  ? -23.029 11.121  -6.904  1.00 17.51 ? 46   TYR A N     1 
ATOM   366  C  CA    . TYR A 1 56  ? -22.053 10.318  -7.654  1.00 16.94 ? 46   TYR A CA    1 
ATOM   367  C  C     . TYR A 1 56  ? -20.720 11.056  -7.706  1.00 16.86 ? 46   TYR A C     1 
ATOM   368  O  O     . TYR A 1 56  ? -20.643 12.180  -8.229  1.00 16.77 ? 46   TYR A O     1 
ATOM   369  C  CB    . TYR A 1 56  ? -22.588 10.021  -9.045  1.00 17.18 ? 46   TYR A CB    1 
ATOM   370  C  CG    . TYR A 1 56  ? -21.664 9.233   -9.962  1.00 16.90 ? 46   TYR A CG    1 
ATOM   371  C  CD1   . TYR A 1 56  ? -20.785 8.267   -9.462  1.00 17.09 ? 46   TYR A CD1   1 
ATOM   372  C  CD2   . TYR A 1 56  ? -21.701 9.425   -11.347 1.00 17.35 ? 46   TYR A CD2   1 
ATOM   373  C  CE1   . TYR A 1 56  ? -19.954 7.542   -10.303 1.00 17.48 ? 46   TYR A CE1   1 
ATOM   374  C  CE2   . TYR A 1 56  ? -20.883 8.701   -12.184 1.00 16.63 ? 46   TYR A CE2   1 
ATOM   375  C  CZ    . TYR A 1 56  ? -20.011 7.758   -11.663 1.00 17.30 ? 46   TYR A CZ    1 
ATOM   376  O  OH    . TYR A 1 56  ? -19.168 7.036   -12.492 1.00 18.30 ? 46   TYR A OH    1 
ATOM   377  N  N     . LEU A 1 57  ? -19.703 10.445  -7.095  1.00 16.06 ? 47   LEU A N     1 
ATOM   378  C  CA    . LEU A 1 57  ? -18.362 11.021  -7.005  1.00 16.31 ? 47   LEU A CA    1 
ATOM   379  C  C     . LEU A 1 57  ? -17.349 10.290  -7.874  1.00 15.77 ? 47   LEU A C     1 
ATOM   380  O  O     . LEU A 1 57  ? -17.378 9.061   -7.985  1.00 16.39 ? 47   LEU A O     1 
ATOM   381  C  CB    . LEU A 1 57  ? -17.868 10.945  -5.574  1.00 16.19 ? 47   LEU A CB    1 
ATOM   382  C  CG    . LEU A 1 57  ? -16.488 11.558  -5.295  1.00 16.63 ? 47   LEU A CG    1 
ATOM   383  C  CD1   . LEU A 1 57  ? -16.516 13.058  -5.484  1.00 16.53 ? 47   LEU A CD1   1 
ATOM   384  C  CD2   . LEU A 1 57  ? -16.035 11.204  -3.891  1.00 16.82 ? 47   LEU A CD2   1 
ATOM   385  N  N     . THR A 1 58  ? -16.450 11.062  -8.472  1.00 15.91 ? 48   THR A N     1 
ATOM   386  C  CA    . THR A 1 58  ? -15.236 10.543  -9.101  1.00 16.17 ? 48   THR A CA    1 
ATOM   387  C  C     . THR A 1 58  ? -14.138 11.560  -8.806  1.00 16.29 ? 48   THR A C     1 
ATOM   388  O  O     . THR A 1 58  ? -14.393 12.625  -8.219  1.00 16.73 ? 48   THR A O     1 
ATOM   389  C  CB    . THR A 1 58  ? -15.423 10.298  -10.623 1.00 16.44 ? 48   THR A CB    1 
ATOM   390  O  OG1   . THR A 1 58  ? -14.306 9.563   -11.153 1.00 17.74 ? 48   THR A OG1   1 
ATOM   391  C  CG2   . THR A 1 58  ? -15.619 11.613  -11.398 1.00 16.91 ? 48   THR A CG2   1 
ATOM   392  N  N     . GLY A 1 59  ? -12.924 11.249  -9.230  1.00 15.97 ? 49   GLY A N     1 
ATOM   393  C  CA    . GLY A 1 59  ? -11.844 12.184  -9.070  1.00 16.79 ? 49   GLY A CA    1 
ATOM   394  C  C     . GLY A 1 59  ? -10.486 11.633  -9.386  1.00 16.40 ? 49   GLY A C     1 
ATOM   395  O  O     . GLY A 1 59  ? -10.364 10.644  -10.120 1.00 16.70 ? 49   GLY A O     1 
ATOM   396  N  N     . THR A 1 60  ? -9.475  12.280  -8.801  1.00 16.74 ? 50   THR A N     1 
ATOM   397  C  CA    . THR A 1 60  ? -8.070  11.986  -9.098  1.00 17.16 ? 50   THR A CA    1 
ATOM   398  C  C     . THR A 1 60  ? -7.158  11.938  -7.872  1.00 16.72 ? 50   THR A C     1 
ATOM   399  O  O     . THR A 1 60  ? -7.264  12.762  -6.953  1.00 16.42 ? 50   THR A O     1 
ATOM   400  C  CB    . THR A 1 60  ? -7.486  12.969  -10.120 1.00 17.57 ? 50   THR A CB    1 
ATOM   401  O  OG1   . THR A 1 60  ? -7.846  14.316  -9.776  1.00 18.37 ? 50   THR A OG1   1 
ATOM   402  C  CG2   . THR A 1 60  ? -7.969  12.650  -11.549 1.00 18.14 ? 50   THR A CG2   1 
ATOM   403  N  N     . ASP A 1 61  ? -6.241  10.967  -7.926  1.00 17.13 ? 51   ASP A N     1 
ATOM   404  C  CA    . ASP A 1 61  ? -5.265  10.623  -6.910  1.00 17.93 ? 51   ASP A CA    1 
ATOM   405  C  C     . ASP A 1 61  ? -3.953  11.200  -7.410  1.00 18.04 ? 51   ASP A C     1 
ATOM   406  O  O     . ASP A 1 61  ? -3.402  10.678  -8.366  1.00 19.07 ? 51   ASP A O     1 
ATOM   407  C  CB    . ASP A 1 61  ? -5.247  9.093   -6.848  1.00 18.58 ? 51   ASP A CB    1 
ATOM   408  C  CG    . ASP A 1 61  ? -4.335  8.526   -5.787  1.00 19.61 ? 51   ASP A CG    1 
ATOM   409  O  OD1   . ASP A 1 61  ? -3.705  9.262   -5.015  1.00 21.81 ? 51   ASP A OD1   1 
ATOM   410  O  OD2   . ASP A 1 61  ? -4.287  7.281   -5.710  1.00 20.96 ? 51   ASP A OD2   1 
ATOM   411  N  N     . GLU A 1 62  ? -3.475  12.287  -6.806  1.00 17.83 ? 52   GLU A N     1 
ATOM   412  C  CA    . GLU A 1 62  ? -2.464  13.165  -7.430  1.00 18.10 ? 52   GLU A CA    1 
ATOM   413  C  C     . GLU A 1 62  ? -1.078  13.209  -6.786  1.00 18.15 ? 52   GLU A C     1 
ATOM   414  O  O     . GLU A 1 62  ? -0.172  13.849  -7.333  1.00 18.66 ? 52   GLU A O     1 
ATOM   415  C  CB    . GLU A 1 62  ? -3.032  14.591  -7.526  1.00 18.13 ? 52   GLU A CB    1 
ATOM   416  C  CG    . GLU A 1 62  ? -4.284  14.644  -8.395  1.00 18.45 ? 52   GLU A CG    1 
ATOM   417  C  CD    . GLU A 1 62  ? -4.808  16.026  -8.670  1.00 18.77 ? 52   GLU A CD    1 
ATOM   418  O  OE1   . GLU A 1 62  ? -4.089  17.027  -8.495  1.00 19.51 ? 52   GLU A OE1   1 
ATOM   419  O  OE2   . GLU A 1 62  ? -5.982  16.109  -9.085  1.00 19.54 ? 52   GLU A OE2   1 
ATOM   420  N  N     . HIS A 1 63  ? -0.898  12.532  -5.655  1.00 17.94 ? 53   HIS A N     1 
ATOM   421  C  CA    . HIS A 1 63  ? 0.379   12.560  -4.929  1.00 18.42 ? 53   HIS A CA    1 
ATOM   422  C  C     . HIS A 1 63  ? 1.275   11.377  -5.288  1.00 18.77 ? 53   HIS A C     1 
ATOM   423  O  O     . HIS A 1 63  ? 0.878   10.478  -6.024  1.00 18.43 ? 53   HIS A O     1 
ATOM   424  C  CB    . HIS A 1 63  ? 0.125   12.664  -3.426  1.00 18.44 ? 53   HIS A CB    1 
ATOM   425  C  CG    . HIS A 1 63  ? -0.547  13.939  -3.037  1.00 18.95 ? 53   HIS A CG    1 
ATOM   426  N  ND1   . HIS A 1 63  ? -1.655  13.974  -2.214  1.00 19.34 ? 53   HIS A ND1   1 
ATOM   427  C  CD2   . HIS A 1 63  ? -0.283  15.219  -3.373  1.00 19.67 ? 53   HIS A CD2   1 
ATOM   428  C  CE1   . HIS A 1 63  ? -2.039  15.229  -2.067  1.00 20.03 ? 53   HIS A CE1   1 
ATOM   429  N  NE2   . HIS A 1 63  ? -1.223  16.006  -2.756  1.00 20.78 ? 53   HIS A NE2   1 
ATOM   430  N  N     . GLY A 1 64  ? 2.509   11.418  -4.798  1.00 19.31 ? 54   GLY A N     1 
ATOM   431  C  CA    . GLY A 1 64  ? 3.439   10.313  -4.946  1.00 20.35 ? 54   GLY A CA    1 
ATOM   432  C  C     . GLY A 1 64  ? 4.579   10.559  -5.924  1.00 21.91 ? 54   GLY A C     1 
ATOM   433  O  O     . GLY A 1 64  ? 4.554   11.485  -6.739  1.00 21.09 ? 54   GLY A O     1 
ATOM   434  N  N     . GLN A 1 65  ? 5.581   9.696   -5.818  1.00 23.98 ? 55   GLN A N     1 
ATOM   435  C  CA    . GLN A 1 65  ? 6.804   9.784   -6.611  1.00 26.23 ? 55   GLN A CA    1 
ATOM   436  C  C     . GLN A 1 65  ? 6.574   9.756   -8.101  1.00 26.74 ? 55   GLN A C     1 
ATOM   437  O  O     . GLN A 1 65  ? 7.198   10.517  -8.837  1.00 26.14 ? 55   GLN A O     1 
ATOM   438  C  CB    . GLN A 1 65  ? 7.754   8.653   -6.234  1.00 28.94 ? 55   GLN A CB    1 
ATOM   439  C  CG    . GLN A 1 65  ? 8.343   8.821   -4.865  1.00 31.81 ? 55   GLN A CG    1 
ATOM   440  C  CD    . GLN A 1 65  ? 9.393   7.777   -4.550  1.00 33.54 ? 55   GLN A CD    1 
ATOM   441  O  OE1   . GLN A 1 65  ? 10.584  8.066   -4.551  1.00 37.30 ? 55   GLN A OE1   1 
ATOM   442  N  NE2   . GLN A 1 65  ? 8.950   6.557   -4.296  1.00 35.37 ? 55   GLN A NE2   1 
ATOM   443  N  N     . LYS A 1 66  ? 5.678   8.882   -8.555  1.00 26.73 ? 56   LYS A N     1 
ATOM   444  C  CA    . LYS A 1 66  ? 5.472   8.719   -9.987  1.00 28.17 ? 56   LYS A CA    1 
ATOM   445  C  C     . LYS A 1 66  ? 4.973   10.011  -10.641 1.00 27.54 ? 56   LYS A C     1 
ATOM   446  O  O     . LYS A 1 66  ? 5.429   10.369  -11.719 1.00 26.82 ? 56   LYS A O     1 
ATOM   447  C  CB    . LYS A 1 66  ? 4.535   7.546   -10.265 1.00 29.66 ? 56   LYS A CB    1 
ATOM   448  C  CG    . LYS A 1 66  ? 4.257   7.274   -11.735 1.00 32.42 ? 56   LYS A CG    1 
ATOM   449  C  CD    . LYS A 1 66  ? 5.518   6.888   -12.485 1.00 34.87 ? 56   LYS A CD    1 
ATOM   450  C  CE    . LYS A 1 66  ? 5.194   6.249   -13.827 1.00 37.53 ? 56   LYS A CE    1 
ATOM   451  N  NZ    . LYS A 1 66  ? 6.440   5.792   -14.508 1.00 38.73 ? 56   LYS A NZ    1 
ATOM   452  N  N     . ILE A 1 67  ? 4.055   10.711  -9.982  1.00 25.85 ? 57   ILE A N     1 
ATOM   453  C  CA    . ILE A 1 67  ? 3.567   11.992  -10.484 1.00 26.35 ? 57   ILE A CA    1 
ATOM   454  C  C     . ILE A 1 67  ? 4.677   13.034  -10.525 1.00 26.31 ? 57   ILE A C     1 
ATOM   455  O  O     . ILE A 1 67  ? 4.819   13.734  -11.515 1.00 26.23 ? 57   ILE A O     1 
ATOM   456  C  CB    . ILE A 1 67  ? 2.371   12.521  -9.652  1.00 26.18 ? 57   ILE A CB    1 
ATOM   457  C  CG1   . ILE A 1 67  ? 1.178   11.573  -9.744  1.00 26.32 ? 57   ILE A CG1   1 
ATOM   458  C  CG2   . ILE A 1 67  ? 1.963   13.935  -10.074 1.00 25.94 ? 57   ILE A CG2   1 
ATOM   459  C  CD1   . ILE A 1 67  ? 0.669   11.265  -11.127 1.00 26.52 ? 57   ILE A CD1   1 
ATOM   460  N  N     . GLN A 1 68  ? 5.471   13.122  -9.462  1.00 26.22 ? 58   GLN A N     1 
ATOM   461  C  CA    . GLN A 1 68  ? 6.574   14.064  -9.417  1.00 26.84 ? 58   GLN A CA    1 
ATOM   462  C  C     . GLN A 1 68  ? 7.547   13.798  -10.565 1.00 27.31 ? 58   GLN A C     1 
ATOM   463  O  O     . GLN A 1 68  ? 8.000   14.727  -11.222 1.00 27.01 ? 58   GLN A O     1 
ATOM   464  C  CB    . GLN A 1 68  ? 7.284   13.990  -8.071  1.00 27.41 ? 58   GLN A CB    1 
ATOM   465  C  CG    . GLN A 1 68  ? 8.534   14.850  -7.962  1.00 28.17 ? 58   GLN A CG    1 
ATOM   466  C  CD    . GLN A 1 68  ? 9.774   14.182  -8.514  1.00 29.10 ? 58   GLN A CD    1 
ATOM   467  O  OE1   . GLN A 1 68  ? 10.003  12.997  -8.292  1.00 30.73 ? 58   GLN A OE1   1 
ATOM   468  N  NE2   . GLN A 1 68  ? 10.576  14.936  -9.259  1.00 31.33 ? 58   GLN A NE2   1 
ATOM   469  N  N     . GLU A 1 69  ? 7.863   12.523  -10.782 1.00 27.59 ? 59   GLU A N     1 
ATOM   470  C  CA    . GLU A 1 69  ? 8.748   12.120  -11.878 1.00 30.13 ? 59   GLU A CA    1 
ATOM   471  C  C     . GLU A 1 69  ? 8.207   12.525  -13.244 1.00 29.37 ? 59   GLU A C     1 
ATOM   472  O  O     . GLU A 1 69  ? 8.953   13.028  -14.094 1.00 28.54 ? 59   GLU A O     1 
ATOM   473  C  CB    . GLU A 1 69  ? 8.975   10.614  -11.846 1.00 32.70 ? 59   GLU A CB    1 
ATOM   474  C  CG    . GLU A 1 69  ? 10.014  10.194  -10.821 1.00 36.44 ? 59   GLU A CG    1 
ATOM   475  C  CD    . GLU A 1 69  ? 10.020  8.701   -10.554 1.00 39.17 ? 59   GLU A CD    1 
ATOM   476  O  OE1   . GLU A 1 69  ? 9.435   7.931   -11.356 1.00 43.23 ? 59   GLU A OE1   1 
ATOM   477  O  OE2   . GLU A 1 69  ? 10.604  8.306   -9.525  1.00 41.32 ? 59   GLU A OE2   1 
ATOM   478  N  N     . LYS A 1 70  ? 6.912   12.289  -13.457 1.00 27.58 ? 60   LYS A N     1 
ATOM   479  C  CA    . LYS A 1 70  ? 6.271   12.640  -14.723 1.00 27.98 ? 60   LYS A CA    1 
ATOM   480  C  C     . LYS A 1 70  ? 6.303   14.137  -14.991 1.00 27.13 ? 60   LYS A C     1 
ATOM   481  O  O     . LYS A 1 70  ? 6.594   14.579  -16.106 1.00 27.17 ? 60   LYS A O     1 
ATOM   482  C  CB    . LYS A 1 70  ? 4.820   12.136  -14.769 1.00 28.38 ? 60   LYS A CB    1 
ATOM   483  C  CG    . LYS A 1 70  ? 4.687   10.641  -14.984 1.00 30.17 ? 60   LYS A CG    1 
ATOM   484  C  CD    . LYS A 1 70  ? 5.022   10.231  -16.408 1.00 31.59 ? 60   LYS A CD    1 
ATOM   485  C  CE    . LYS A 1 70  ? 5.037   8.722   -16.564 1.00 33.00 ? 60   LYS A CE    1 
ATOM   486  N  NZ    . LYS A 1 70  ? 5.326   8.332   -17.974 1.00 34.31 ? 60   LYS A NZ    1 
ATOM   487  N  N     . ALA A 1 71  ? 6.010   14.910  -13.953 1.00 26.05 ? 61   ALA A N     1 
ATOM   488  C  CA    . ALA A 1 71  ? 6.045   16.354  -14.032 1.00 26.55 ? 61   ALA A CA    1 
ATOM   489  C  C     . ALA A 1 71  ? 7.454   16.840  -14.354 1.00 27.40 ? 61   ALA A C     1 
ATOM   490  O  O     . ALA A 1 71  ? 7.649   17.617  -15.287 1.00 27.85 ? 61   ALA A O     1 
ATOM   491  C  CB    . ALA A 1 71  ? 5.550   16.960  -12.733 1.00 26.63 ? 61   ALA A CB    1 
ATOM   492  N  N     . GLN A 1 72  ? 8.431   16.380  -13.581 1.00 28.95 ? 62   GLN A N     1 
ATOM   493  C  CA    . GLN A 1 72  ? 9.824   16.770  -13.813 1.00 30.17 ? 62   GLN A CA    1 
ATOM   494  C  C     . GLN A 1 72  ? 10.313  16.397  -15.230 1.00 31.91 ? 62   GLN A C     1 
ATOM   495  O  O     . GLN A 1 72  ? 10.977  17.202  -15.891 1.00 31.84 ? 62   GLN A O     1 
ATOM   496  C  CB    . GLN A 1 72  ? 10.740  16.177  -12.741 1.00 30.93 ? 62   GLN A CB    1 
ATOM   497  C  CG    . GLN A 1 72  ? 12.172  16.694  -12.784 1.00 32.35 ? 62   GLN A CG    1 
ATOM   498  C  CD    . GLN A 1 72  ? 13.066  16.031  -11.745 1.00 33.99 ? 62   GLN A CD    1 
ATOM   499  O  OE1   . GLN A 1 72  ? 13.058  14.815  -11.599 1.00 35.66 ? 62   GLN A OE1   1 
ATOM   500  N  NE2   . GLN A 1 72  ? 13.855  16.829  -11.034 1.00 33.46 ? 62   GLN A NE2   1 
ATOM   501  N  N     . LYS A 1 73  ? 9.962   15.202  -15.697 1.00 32.71 ? 63   LYS A N     1 
ATOM   502  C  CA    . LYS A 1 73  ? 10.306  14.776  -17.071 1.00 35.21 ? 63   LYS A CA    1 
ATOM   503  C  C     . LYS A 1 73  ? 9.729   15.721  -18.128 1.00 35.39 ? 63   LYS A C     1 
ATOM   504  O  O     . LYS A 1 73  ? 10.384  16.017  -19.130 1.00 36.15 ? 63   LYS A O     1 
ATOM   505  C  CB    . LYS A 1 73  ? 9.823   13.345  -17.340 1.00 37.17 ? 63   LYS A CB    1 
ATOM   506  C  CG    . LYS A 1 73  ? 10.207  12.825  -18.721 1.00 39.78 ? 63   LYS A CG    1 
ATOM   507  C  CD    . LYS A 1 73  ? 10.125  11.312  -18.823 1.00 41.44 ? 63   LYS A CD    1 
ATOM   508  C  CE    . LYS A 1 73  ? 10.446  10.831  -20.230 1.00 43.57 ? 63   LYS A CE    1 
ATOM   509  N  NZ    . LYS A 1 73  ? 11.799  11.238  -20.722 1.00 45.12 ? 63   LYS A NZ    1 
ATOM   510  N  N     . ALA A 1 74  ? 8.511   16.202  -17.887 1.00 34.77 ? 64   ALA A N     1 
ATOM   511  C  CA    . ALA A 1 74  ? 7.826   17.134  -18.787 1.00 34.88 ? 64   ALA A CA    1 
ATOM   512  C  C     . ALA A 1 74  ? 8.289   18.598  -18.693 1.00 35.24 ? 64   ALA A C     1 
ATOM   513  O  O     . ALA A 1 74  ? 7.786   19.446  -19.434 1.00 34.91 ? 64   ALA A O     1 
ATOM   514  C  CB    . ALA A 1 74  ? 6.324   17.053  -18.555 1.00 34.72 ? 64   ALA A CB    1 
ATOM   515  N  N     . GLY A 1 75  ? 9.221   18.902  -17.788 1.00 35.03 ? 65   GLY A N     1 
ATOM   516  C  CA    . GLY A 1 75  ? 9.677   20.275  -17.579 1.00 35.24 ? 65   GLY A CA    1 
ATOM   517  C  C     . GLY A 1 75  ? 8.635   21.179  -16.937 1.00 34.80 ? 65   GLY A C     1 
ATOM   518  O  O     . GLY A 1 75  ? 8.652   22.394  -17.139 1.00 34.06 ? 65   GLY A O     1 
ATOM   519  N  N     . LYS A 1 76  ? 7.749   20.577  -16.136 1.00 33.11 ? 66   LYS A N     1 
ATOM   520  C  CA    . LYS A 1 76  ? 6.639   21.281  -15.503 1.00 32.38 ? 66   LYS A CA    1 
ATOM   521  C  C     . LYS A 1 76  ? 6.666   21.079  -13.996 1.00 29.89 ? 66   LYS A C     1 
ATOM   522  O  O     . LYS A 1 76  ? 7.215   20.091  -13.505 1.00 28.84 ? 66   LYS A O     1 
ATOM   523  C  CB    . LYS A 1 76  ? 5.312   20.760  -16.063 1.00 33.29 ? 66   LYS A CB    1 
ATOM   524  C  CG    . LYS A 1 76  ? 5.137   21.048  -17.545 1.00 34.82 ? 66   LYS A CG    1 
ATOM   525  C  CD    . LYS A 1 76  ? 3.891   20.395  -18.116 1.00 35.80 ? 66   LYS A CD    1 
ATOM   526  C  CE    . LYS A 1 76  ? 3.818   20.618  -19.624 1.00 36.78 ? 66   LYS A CE    1 
ATOM   527  N  NZ    . LYS A 1 76  ? 2.934   19.630  -20.280 1.00 37.90 ? 66   LYS A NZ    1 
ATOM   528  N  N     . THR A 1 77  ? 6.060   22.011  -13.270 1.00 28.35 ? 67   THR A N     1 
ATOM   529  C  CA    . THR A 1 77  ? 5.862   21.827  -11.827 1.00 27.34 ? 67   THR A CA    1 
ATOM   530  C  C     . THR A 1 77  ? 4.823   20.733  -11.645 1.00 26.23 ? 67   THR A C     1 
ATOM   531  O  O     . THR A 1 77  ? 4.073   20.387  -12.577 1.00 24.60 ? 67   THR A O     1 
ATOM   532  C  CB    . THR A 1 77  ? 5.402   23.101  -11.091 1.00 28.07 ? 67   THR A CB    1 
ATOM   533  O  OG1   . THR A 1 77  ? 4.072   23.455  -11.493 1.00 28.56 ? 67   THR A OG1   1 
ATOM   534  C  CG2   . THR A 1 77  ? 6.367   24.282  -11.362 1.00 28.59 ? 67   THR A CG2   1 
ATOM   535  N  N     . GLU A 1 78  ? 4.768   20.202  -10.436 1.00 24.79 ? 68   GLU A N     1 
ATOM   536  C  CA    . GLU A 1 78  ? 3.830   19.127  -10.145 1.00 24.66 ? 68   GLU A CA    1 
ATOM   537  C  C     . GLU A 1 78  ? 2.402   19.604  -10.413 1.00 23.82 ? 68   GLU A C     1 
ATOM   538  O  O     . GLU A 1 78  ? 1.632   18.926  -11.113 1.00 22.45 ? 68   GLU A O     1 
ATOM   539  C  CB    . GLU A 1 78  ? 3.983   18.652  -8.708  1.00 25.01 ? 68   GLU A CB    1 
ATOM   540  C  CG    . GLU A 1 78  ? 5.239   17.830  -8.473  1.00 26.10 ? 68   GLU A CG    1 
ATOM   541  C  CD    . GLU A 1 78  ? 6.540   18.627  -8.530  1.00 27.44 ? 68   GLU A CD    1 
ATOM   542  O  OE1   . GLU A 1 78  ? 6.549   19.886  -8.396  1.00 26.66 ? 68   GLU A OE1   1 
ATOM   543  O  OE2   . GLU A 1 78  ? 7.585   17.977  -8.716  1.00 30.12 ? 68   GLU A OE2   1 
ATOM   544  N  N     . ILE A 1 79  ? 2.056   20.774  -9.876  1.00 24.18 ? 69   ILE A N     1 
ATOM   545  C  CA    . ILE A 1 79  ? 0.685   21.275  -10.043 1.00 25.12 ? 69   ILE A CA    1 
ATOM   546  C  C     . ILE A 1 79  ? 0.358   21.690  -11.491 1.00 25.72 ? 69   ILE A C     1 
ATOM   547  O  O     . ILE A 1 79  ? -0.785  21.540  -11.923 1.00 25.33 ? 69   ILE A O     1 
ATOM   548  C  CB    . ILE A 1 79  ? 0.316   22.343  -8.986  1.00 26.06 ? 69   ILE A CB    1 
ATOM   549  C  CG1   . ILE A 1 79  ? -1.212  22.421  -8.794  1.00 26.20 ? 69   ILE A CG1   1 
ATOM   550  C  CG2   . ILE A 1 79  ? 0.899   23.694  -9.331  1.00 26.53 ? 69   ILE A CG2   1 
ATOM   551  C  CD1   . ILE A 1 79  ? -1.843  21.184  -8.158  1.00 26.52 ? 69   ILE A CD1   1 
ATOM   552  N  N     A GLU A 1 80  ? 1.355   22.204  -12.216 0.50 26.00 ? 70   GLU A N     1 
ATOM   553  N  N     B GLU A 1 80  ? 1.347   22.197  -12.225 0.50 25.90 ? 70   GLU A N     1 
ATOM   554  C  CA    A GLU A 1 80  ? 1.231   22.520  -13.654 0.50 26.52 ? 70   GLU A CA    1 
ATOM   555  C  CA    B GLU A 1 80  ? 1.170   22.510  -13.654 0.50 26.34 ? 70   GLU A CA    1 
ATOM   556  C  C     A GLU A 1 80  ? 0.869   21.277  -14.467 0.50 25.77 ? 70   GLU A C     1 
ATOM   557  C  C     B GLU A 1 80  ? 0.849   21.262  -14.470 0.50 25.67 ? 70   GLU A C     1 
ATOM   558  O  O     A GLU A 1 80  ? -0.078  21.288  -15.255 0.50 25.84 ? 70   GLU A O     1 
ATOM   559  O  O     B GLU A 1 80  ? -0.087  21.256  -15.271 0.50 25.71 ? 70   GLU A O     1 
ATOM   560  C  CB    A GLU A 1 80  ? 2.546   23.121  -14.177 0.50 27.69 ? 70   GLU A CB    1 
ATOM   561  C  CB    B GLU A 1 80  ? 2.415   23.187  -14.226 0.50 27.39 ? 70   GLU A CB    1 
ATOM   562  C  CG    A GLU A 1 80  ? 2.569   23.514  -15.649 0.50 28.45 ? 70   GLU A CG    1 
ATOM   563  C  CG    B GLU A 1 80  ? 2.498   24.673  -13.914 0.50 27.98 ? 70   GLU A CG    1 
ATOM   564  C  CD    A GLU A 1 80  ? 3.892   24.155  -16.049 0.50 29.55 ? 70   GLU A CD    1 
ATOM   565  C  CD    B GLU A 1 80  ? 3.840   25.275  -14.290 0.50 28.85 ? 70   GLU A CD    1 
ATOM   566  O  OE1   A GLU A 1 80  ? 3.993   24.673  -17.184 0.50 29.95 ? 70   GLU A OE1   1 
ATOM   567  O  OE1   B GLU A 1 80  ? 4.798   24.504  -14.524 0.50 28.64 ? 70   GLU A OE1   1 
ATOM   568  O  OE2   A GLU A 1 80  ? 4.834   24.143  -15.220 0.50 29.40 ? 70   GLU A OE2   1 
ATOM   569  O  OE2   B GLU A 1 80  ? 3.935   26.520  -14.347 0.50 29.66 ? 70   GLU A OE2   1 
ATOM   570  N  N     . TYR A 1 81  ? 1.630   20.211  -14.245 1.00 25.06 ? 71   TYR A N     1 
ATOM   571  C  CA    . TYR A 1 81  ? 1.404   18.909  -14.861 1.00 24.26 ? 71   TYR A CA    1 
ATOM   572  C  C     . TYR A 1 81  ? -0.003  18.380  -14.535 1.00 23.21 ? 71   TYR A C     1 
ATOM   573  O  O     . TYR A 1 81  ? -0.788  18.036  -15.437 1.00 22.83 ? 71   TYR A O     1 
ATOM   574  C  CB    . TYR A 1 81  ? 2.486   17.917  -14.376 1.00 23.96 ? 71   TYR A CB    1 
ATOM   575  C  CG    . TYR A 1 81  ? 2.195   16.479  -14.783 1.00 24.07 ? 71   TYR A CG    1 
ATOM   576  C  CD1   . TYR A 1 81  ? 2.540   16.003  -16.050 1.00 24.20 ? 71   TYR A CD1   1 
ATOM   577  C  CD2   . TYR A 1 81  ? 1.525   15.613  -13.918 1.00 23.62 ? 71   TYR A CD2   1 
ATOM   578  C  CE1   . TYR A 1 81  ? 2.246   14.710  -16.436 1.00 24.20 ? 71   TYR A CE1   1 
ATOM   579  C  CE2   . TYR A 1 81  ? 1.233   14.316  -14.288 1.00 23.46 ? 71   TYR A CE2   1 
ATOM   580  C  CZ    . TYR A 1 81  ? 1.583   13.863  -15.548 1.00 24.09 ? 71   TYR A CZ    1 
ATOM   581  O  OH    . TYR A 1 81  ? 1.274   12.567  -15.911 1.00 24.15 ? 71   TYR A OH    1 
ATOM   582  N  N     . LEU A 1 82  ? -0.324  18.377  -13.244 1.00 22.55 ? 72   LEU A N     1 
ATOM   583  C  CA    . LEU A 1 82  ? -1.618  17.852  -12.776 1.00 22.08 ? 72   LEU A CA    1 
ATOM   584  C  C     . LEU A 1 82  ? -2.815  18.638  -13.298 1.00 22.41 ? 72   LEU A C     1 
ATOM   585  O  O     . LEU A 1 82  ? -3.814  18.046  -13.728 1.00 21.93 ? 72   LEU A O     1 
ATOM   586  C  CB    . LEU A 1 82  ? -1.664  17.774  -11.250 1.00 21.71 ? 72   LEU A CB    1 
ATOM   587  C  CG    . LEU A 1 82  ? -0.786  16.671  -10.658 1.00 21.62 ? 72   LEU A CG    1 
ATOM   588  C  CD1   . LEU A 1 82  ? -0.550  16.947  -9.185  1.00 21.52 ? 72   LEU A CD1   1 
ATOM   589  C  CD2   . LEU A 1 82  ? -1.391  15.288  -10.870 1.00 21.47 ? 72   LEU A CD2   1 
ATOM   590  N  N     . ASP A 1 83  ? -2.721  19.961  -13.269 1.00 23.69 ? 73   ASP A N     1 
ATOM   591  C  CA    . ASP A 1 83  ? -3.815  20.797  -13.756 1.00 24.71 ? 73   ASP A CA    1 
ATOM   592  C  C     . ASP A 1 83  ? -4.127  20.486  -15.213 1.00 25.12 ? 73   ASP A C     1 
ATOM   593  O  O     . ASP A 1 83  ? -5.296  20.434  -15.595 1.00 24.87 ? 73   ASP A O     1 
ATOM   594  C  CB    . ASP A 1 83  ? -3.509  22.292  -13.576 1.00 25.41 ? 73   ASP A CB    1 
ATOM   595  C  CG    . ASP A 1 83  ? -3.568  22.746  -12.116 1.00 25.64 ? 73   ASP A CG    1 
ATOM   596  O  OD1   . ASP A 1 83  ? -4.075  22.005  -11.239 1.00 24.81 ? 73   ASP A OD1   1 
ATOM   597  O  OD2   . ASP A 1 83  ? -3.094  23.873  -11.844 1.00 26.04 ? 73   ASP A OD2   1 
ATOM   598  N  N     . GLU A 1 84  ? -3.091  20.249  -16.015 1.00 25.80 ? 74   GLU A N     1 
ATOM   599  C  CA    . GLU A 1 84  ? -3.276  19.891  -17.424 1.00 27.15 ? 74   GLU A CA    1 
ATOM   600  C  C     . GLU A 1 84  ? -3.920  18.518  -17.558 1.00 25.02 ? 74   GLU A C     1 
ATOM   601  O  O     . GLU A 1 84  ? -4.875  18.361  -18.320 1.00 25.45 ? 74   GLU A O     1 
ATOM   602  C  CB    . GLU A 1 84  ? -1.946  19.936  -18.182 1.00 30.10 ? 74   GLU A CB    1 
ATOM   603  C  CG    . GLU A 1 84  ? -1.519  21.358  -18.533 1.00 33.28 ? 74   GLU A CG    1 
ATOM   604  C  CD    . GLU A 1 84  ? -0.100  21.453  -19.073 1.00 36.29 ? 74   GLU A CD    1 
ATOM   605  O  OE1   . GLU A 1 84  ? 0.362   22.596  -19.273 1.00 39.73 ? 74   GLU A OE1   1 
ATOM   606  O  OE2   . GLU A 1 84  ? 0.558   20.404  -19.290 1.00 37.96 ? 74   GLU A OE2   1 
ATOM   607  N  N     . MET A 1 85  ? -3.410  17.535  -16.813 1.00 23.58 ? 75   MET A N     1 
ATOM   608  C  CA    . MET A 1 85  ? -3.961  16.166  -16.844 1.00 22.90 ? 75   MET A CA    1 
ATOM   609  C  C     . MET A 1 85  ? -5.428  16.170  -16.429 1.00 21.82 ? 75   MET A C     1 
ATOM   610  O  O     . MET A 1 85  ? -6.287  15.532  -17.068 1.00 21.16 ? 75   MET A O     1 
ATOM   611  C  CB    . MET A 1 85  ? -3.185  15.222  -15.917 1.00 22.97 ? 75   MET A CB    1 
ATOM   612  C  CG    . MET A 1 85  ? -1.756  14.918  -16.349 1.00 23.66 ? 75   MET A CG    1 
ATOM   613  S  SD    . MET A 1 85  ? -1.618  14.309  -18.056 1.00 25.06 ? 75   MET A SD    1 
ATOM   614  C  CE    . MET A 1 85  ? -2.403  12.710  -17.918 1.00 24.84 ? 75   MET A CE    1 
ATOM   615  N  N     . ILE A 1 86  ? -5.708  16.890  -15.349 1.00 21.01 ? 76   ILE A N     1 
ATOM   616  C  CA    . ILE A 1 86  ? -7.075  16.947  -14.803 1.00 20.83 ? 76   ILE A CA    1 
ATOM   617  C  C     . ILE A 1 86  ? -8.037  17.653  -15.759 1.00 20.95 ? 76   ILE A C     1 
ATOM   618  O  O     . ILE A 1 86  ? -9.187  17.237  -15.899 1.00 20.15 ? 76   ILE A O     1 
ATOM   619  C  CB    . ILE A 1 86  ? -7.102  17.536  -13.364 1.00 20.43 ? 76   ILE A CB    1 
ATOM   620  C  CG1   . ILE A 1 86  ? -6.922  16.409  -12.339 1.00 20.17 ? 76   ILE A CG1   1 
ATOM   621  C  CG2   . ILE A 1 86  ? -8.429  18.225  -13.046 1.00 20.86 ? 76   ILE A CG2   1 
ATOM   622  C  CD1   . ILE A 1 86  ? -5.654  15.577  -12.474 1.00 20.02 ? 76   ILE A CD1   1 
ATOM   623  N  N     . ALA A 1 87  ? -7.577  18.718  -16.418 1.00 22.24 ? 77   ALA A N     1 
ATOM   624  C  CA    . ALA A 1 87  ? -8.419  19.389  -17.419 1.00 23.12 ? 77   ALA A CA    1 
ATOM   625  C  C     . ALA A 1 87  ? -8.862  18.390  -18.500 1.00 23.16 ? 77   ALA A C     1 
ATOM   626  O  O     . ALA A 1 87  ? -10.040 18.338  -18.868 1.00 22.93 ? 77   ALA A O     1 
ATOM   627  C  CB    . ALA A 1 87  ? -7.685  20.576  -18.021 1.00 23.70 ? 77   ALA A CB    1 
ATOM   628  N  N     . GLY A 1 88  ? -7.923  17.559  -18.957 1.00 22.44 ? 78   GLY A N     1 
ATOM   629  C  CA    . GLY A 1 88  ? -8.205  16.517  -19.947 1.00 21.79 ? 78   GLY A CA    1 
ATOM   630  C  C     . GLY A 1 88  ? -9.158  15.441  -19.427 1.00 21.23 ? 78   GLY A C     1 
ATOM   631  O  O     . GLY A 1 88  ? -10.015 14.958  -20.162 1.00 21.21 ? 78   GLY A O     1 
ATOM   632  N  N     . ILE A 1 89  ? -9.012  15.065  -18.158 1.00 20.51 ? 79   ILE A N     1 
ATOM   633  C  CA    . ILE A 1 89  ? -9.912  14.061  -17.557 1.00 20.03 ? 79   ILE A CA    1 
ATOM   634  C  C     . ILE A 1 89  ? -11.330 14.621  -17.440 1.00 20.70 ? 79   ILE A C     1 
ATOM   635  O  O     . ILE A 1 89  ? -12.305 13.948  -17.799 1.00 21.10 ? 79   ILE A O     1 
ATOM   636  C  CB    . ILE A 1 89  ? -9.366  13.550  -16.205 1.00 19.84 ? 79   ILE A CB    1 
ATOM   637  C  CG1   . ILE A 1 89  ? -8.106  12.707  -16.462 1.00 19.65 ? 79   ILE A CG1   1 
ATOM   638  C  CG2   . ILE A 1 89  ? -10.397 12.699  -15.450 1.00 19.86 ? 79   ILE A CG2   1 
ATOM   639  C  CD1   . ILE A 1 89  ? -7.245  12.441  -15.246 1.00 19.96 ? 79   ILE A CD1   1 
ATOM   640  N  N     . LYS A 1 90  ? -11.442 15.851  -16.950 1.00 21.30 ? 80   LYS A N     1 
ATOM   641  C  CA    . LYS A 1 90  ? -12.748 16.501  -16.835 1.00 22.43 ? 80   LYS A CA    1 
ATOM   642  C  C     . LYS A 1 90  ? -13.417 16.688  -18.196 1.00 22.75 ? 80   LYS A C     1 
ATOM   643  O  O     . LYS A 1 90  ? -14.635 16.529  -18.312 1.00 22.96 ? 80   LYS A O     1 
ATOM   644  C  CB    . LYS A 1 90  ? -12.611 17.829  -16.103 1.00 23.65 ? 80   LYS A CB    1 
ATOM   645  C  CG    . LYS A 1 90  ? -12.322 17.643  -14.619 1.00 24.62 ? 80   LYS A CG    1 
ATOM   646  C  CD    . LYS A 1 90  ? -12.352 18.953  -13.855 1.00 25.93 ? 80   LYS A CD    1 
ATOM   647  C  CE    . LYS A 1 90  ? -12.278 18.696  -12.359 1.00 27.58 ? 80   LYS A CE    1 
ATOM   648  N  NZ    . LYS A 1 90  ? -12.041 19.906  -11.539 1.00 29.22 ? 80   LYS A NZ    1 
ATOM   649  N  N     . GLN A 1 91  ? -12.623 17.031  -19.211 1.00 23.27 ? 81   GLN A N     1 
ATOM   650  C  CA    . GLN A 1 91  ? -13.115 17.138  -20.593 1.00 24.21 ? 81   GLN A CA    1 
ATOM   651  C  C     . GLN A 1 91  ? -13.655 15.788  -21.064 1.00 22.80 ? 81   GLN A C     1 
ATOM   652  O  O     . GLN A 1 91  ? -14.711 15.722  -21.692 1.00 23.25 ? 81   GLN A O     1 
ATOM   653  C  CB    . GLN A 1 91  ? -12.002 17.635  -21.536 1.00 26.20 ? 81   GLN A CB    1 
ATOM   654  C  CG    . GLN A 1 91  ? -11.830 19.150  -21.520 1.00 28.79 ? 81   GLN A CG    1 
ATOM   655  C  CD    . GLN A 1 91  ? -10.422 19.632  -21.861 1.00 31.91 ? 81   GLN A CD    1 
ATOM   656  O  OE1   . GLN A 1 91  ? -9.656  18.950  -22.557 1.00 33.96 ? 81   GLN A OE1   1 
ATOM   657  N  NE2   . GLN A 1 91  ? -10.069 20.821  -21.354 1.00 33.42 ? 81   GLN A NE2   1 
ATOM   658  N  N     . LEU A 1 92  ? -12.940 14.713  -20.746 1.00 21.69 ? 82   LEU A N     1 
ATOM   659  C  CA    . LEU A 1 92  ? -13.393 13.376  -21.114 1.00 21.35 ? 82   LEU A CA    1 
ATOM   660  C  C     . LEU A 1 92  ? -14.738 13.031  -20.458 1.00 20.65 ? 82   LEU A C     1 
ATOM   661  O  O     . LEU A 1 92  ? -15.641 12.539  -21.141 1.00 20.74 ? 82   LEU A O     1 
ATOM   662  C  CB    . LEU A 1 92  ? -12.358 12.311  -20.760 1.00 21.52 ? 82   LEU A CB    1 
ATOM   663  C  CG    . LEU A 1 92  ? -12.785 10.859  -21.017 1.00 21.17 ? 82   LEU A CG    1 
ATOM   664  C  CD1   . LEU A 1 92  ? -13.138 10.606  -22.471 1.00 21.95 ? 82   LEU A CD1   1 
ATOM   665  C  CD2   . LEU A 1 92  ? -11.700 9.915   -20.552 1.00 21.30 ? 82   LEU A CD2   1 
ATOM   666  N  N     . TRP A 1 93  ? -14.871 13.277  -19.156 1.00 20.22 ? 83   TRP A N     1 
ATOM   667  C  CA    . TRP A 1 93  ? -16.154 13.017  -18.472 1.00 19.91 ? 83   TRP A CA    1 
ATOM   668  C  C     . TRP A 1 93  ? -17.296 13.881  -19.027 1.00 20.65 ? 83   TRP A C     1 
ATOM   669  O  O     . TRP A 1 93  ? -18.422 13.395  -19.180 1.00 20.93 ? 83   TRP A O     1 
ATOM   670  C  CB    . TRP A 1 93  ? -16.060 13.121  -16.943 1.00 19.57 ? 83   TRP A CB    1 
ATOM   671  C  CG    . TRP A 1 93  ? -15.008 12.257  -16.280 1.00 18.93 ? 83   TRP A CG    1 
ATOM   672  C  CD1   . TRP A 1 93  ? -14.344 12.559  -15.128 1.00 19.24 ? 83   TRP A CD1   1 
ATOM   673  C  CD2   . TRP A 1 93  ? -14.500 10.970  -16.700 1.00 18.98 ? 83   TRP A CD2   1 
ATOM   674  N  NE1   . TRP A 1 93  ? -13.473 11.562  -14.805 1.00 18.99 ? 83   TRP A NE1   1 
ATOM   675  C  CE2   . TRP A 1 93  ? -13.544 10.573  -15.741 1.00 18.95 ? 83   TRP A CE2   1 
ATOM   676  C  CE3   . TRP A 1 93  ? -14.762 10.110  -17.782 1.00 19.13 ? 83   TRP A CE3   1 
ATOM   677  C  CZ2   . TRP A 1 93  ? -12.826 9.371   -15.836 1.00 19.03 ? 83   TRP A CZ2   1 
ATOM   678  C  CZ3   . TRP A 1 93  ? -14.050 8.903   -17.872 1.00 19.73 ? 83   TRP A CZ3   1 
ATOM   679  C  CH2   . TRP A 1 93  ? -13.078 8.561   -16.908 1.00 20.02 ? 83   TRP A CH2   1 
ATOM   680  N  N     . ALA A 1 94  ? -17.008 15.137  -19.360 1.00 21.28 ? 84   ALA A N     1 
ATOM   681  C  CA    . ALA A 1 94  ? -18.007 15.983  -20.010 1.00 22.97 ? 84   ALA A CA    1 
ATOM   682  C  C     . ALA A 1 94  ? -18.420 15.411  -21.378 1.00 23.19 ? 84   ALA A C     1 
ATOM   683  O  O     . ALA A 1 94  ? -19.604 15.397  -21.730 1.00 23.49 ? 84   ALA A O     1 
ATOM   684  C  CB    . ALA A 1 94  ? -17.499 17.417  -20.145 1.00 23.54 ? 84   ALA A CB    1 
ATOM   685  N  N     . LYS A 1 95  ? -17.449 14.921  -22.134 1.00 23.25 ? 85   LYS A N     1 
ATOM   686  C  CA    . LYS A 1 95  ? -17.717 14.343  -23.449 1.00 24.03 ? 85   LYS A CA    1 
ATOM   687  C  C     . LYS A 1 95  ? -18.514 13.033  -23.371 1.00 23.06 ? 85   LYS A C     1 
ATOM   688  O  O     . LYS A 1 95  ? -19.354 12.751  -24.247 1.00 22.74 ? 85   LYS A O     1 
ATOM   689  C  CB    . LYS A 1 95  ? -16.408 14.130  -24.215 1.00 26.13 ? 85   LYS A CB    1 
ATOM   690  C  CG    . LYS A 1 95  ? -16.642 13.712  -25.660 1.00 28.52 ? 85   LYS A CG    1 
ATOM   691  C  CD    . LYS A 1 95  ? -15.356 13.383  -26.381 1.00 30.66 ? 85   LYS A CD    1 
ATOM   692  C  CE    . LYS A 1 95  ? -14.713 14.617  -26.976 1.00 32.83 ? 85   LYS A CE    1 
ATOM   693  N  NZ    . LYS A 1 95  ? -13.559 14.199  -27.819 1.00 34.51 ? 85   LYS A NZ    1 
ATOM   694  N  N     . LEU A 1 96  ? -18.263 12.257  -22.318 1.00 21.76 ? 86   LEU A N     1 
ATOM   695  C  CA    . LEU A 1 96  ? -19.046 11.057  -22.021 1.00 21.46 ? 86   LEU A CA    1 
ATOM   696  C  C     . LEU A 1 96  ? -20.394 11.331  -21.342 1.00 21.40 ? 86   LEU A C     1 
ATOM   697  O  O     . LEU A 1 96  ? -21.162 10.394  -21.117 1.00 20.91 ? 86   LEU A O     1 
ATOM   698  C  CB    . LEU A 1 96  ? -18.222 10.068  -21.175 1.00 21.44 ? 86   LEU A CB    1 
ATOM   699  C  CG    . LEU A 1 96  ? -17.228 9.224   -21.977 1.00 21.97 ? 86   LEU A CG    1 
ATOM   700  C  CD1   . LEU A 1 96  ? -16.163 8.614   -21.080 1.00 21.89 ? 86   LEU A CD1   1 
ATOM   701  C  CD2   . LEU A 1 96  ? -17.951 8.137   -22.748 1.00 22.08 ? 86   LEU A CD2   1 
ATOM   702  N  N     . GLU A 1 97  ? -20.674 12.599  -21.042 1.00 21.11 ? 87   GLU A N     1 
ATOM   703  C  CA    . GLU A 1 97  ? -21.889 13.039  -20.351 1.00 22.11 ? 87   GLU A CA    1 
ATOM   704  C  C     . GLU A 1 97  ? -22.100 12.271  -19.040 1.00 21.16 ? 87   GLU A C     1 
ATOM   705  O  O     . GLU A 1 97  ? -23.185 11.772  -18.734 1.00 21.50 ? 87   GLU A O     1 
ATOM   706  C  CB    . GLU A 1 97  ? -23.094 13.025  -21.303 1.00 23.68 ? 87   GLU A CB    1 
ATOM   707  C  CG    . GLU A 1 97  ? -22.882 14.050  -22.424 1.00 25.18 ? 87   GLU A CG    1 
ATOM   708  C  CD    . GLU A 1 97  ? -24.010 14.156  -23.429 1.00 27.40 ? 87   GLU A CD    1 
ATOM   709  O  OE1   . GLU A 1 97  ? -25.127 13.680  -23.162 1.00 28.14 ? 87   GLU A OE1   1 
ATOM   710  O  OE2   . GLU A 1 97  ? -23.754 14.730  -24.521 1.00 29.67 ? 87   GLU A OE2   1 
ATOM   711  N  N     . ILE A 1 98  ? -21.013 12.186  -18.275 1.00 20.67 ? 88   ILE A N     1 
ATOM   712  C  CA    . ILE A 1 98  ? -21.047 11.622  -16.931 1.00 20.17 ? 88   ILE A CA    1 
ATOM   713  C  C     . ILE A 1 98  ? -21.770 12.611  -16.000 1.00 19.89 ? 88   ILE A C     1 
ATOM   714  O  O     . ILE A 1 98  ? -21.479 13.815  -15.998 1.00 20.08 ? 88   ILE A O     1 
ATOM   715  C  CB    . ILE A 1 98  ? -19.625 11.313  -16.398 1.00 19.92 ? 88   ILE A CB    1 
ATOM   716  C  CG1   . ILE A 1 98  ? -18.838 10.427  -17.381 1.00 19.86 ? 88   ILE A CG1   1 
ATOM   717  C  CG2   . ILE A 1 98  ? -19.677 10.633  -15.026 1.00 20.17 ? 88   ILE A CG2   1 
ATOM   718  C  CD1   . ILE A 1 98  ? -19.468 9.085   -17.730 1.00 20.51 ? 88   ILE A CD1   1 
ATOM   719  N  N     . SER A 1 99  ? -22.693 12.079  -15.200 1.00 19.31 ? 89   SER A N     1 
ATOM   720  C  CA    . SER A 1 99  ? -23.520 12.863  -14.282 1.00 19.36 ? 89   SER A CA    1 
ATOM   721  C  C     . SER A 1 99  ? -22.926 12.939  -12.866 1.00 19.00 ? 89   SER A C     1 
ATOM   722  O  O     . SER A 1 99  ? -23.662 12.991  -11.869 1.00 19.53 ? 89   SER A O     1 
ATOM   723  C  CB    . SER A 1 99  ? -24.947 12.287  -14.253 1.00 19.76 ? 89   SER A CB    1 
ATOM   724  O  OG    . SER A 1 99  ? -24.988 11.004  -13.635 1.00 19.94 ? 89   SER A OG    1 
ATOM   725  N  N     . ASN A 1 100 ? -21.596 12.957  -12.772 1.00 18.86 ? 90   ASN A N     1 
ATOM   726  C  CA    . ASN A 1 100 ? -20.939 13.091  -11.466 1.00 18.50 ? 90   ASN A CA    1 
ATOM   727  C  C     . ASN A 1 100 ? -21.300 14.444  -10.838 1.00 19.33 ? 90   ASN A C     1 
ATOM   728  O  O     . ASN A 1 100 ? -21.344 15.490  -11.520 1.00 19.11 ? 90   ASN A O     1 
ATOM   729  C  CB    . ASN A 1 100 ? -19.406 12.920  -11.530 1.00 18.84 ? 90   ASN A CB    1 
ATOM   730  C  CG    . ASN A 1 100 ? -18.738 13.860  -12.515 1.00 18.69 ? 90   ASN A CG    1 
ATOM   731  O  OD1   . ASN A 1 100 ? -19.062 13.841  -13.712 1.00 18.79 ? 90   ASN A OD1   1 
ATOM   732  N  ND2   . ASN A 1 100 ? -17.791 14.676  -12.027 1.00 18.69 ? 90   ASN A ND2   1 
ATOM   733  N  N     . ASP A 1 101 ? -21.571 14.414  -9.547  1.00 19.19 ? 91   ASP A N     1 
ATOM   734  C  CA    . ASP A 1 101 ? -21.950 15.587  -8.801  1.00 20.20 ? 91   ASP A CA    1 
ATOM   735  C  C     . ASP A 1 101 ? -20.775 16.381  -8.237  1.00 20.41 ? 91   ASP A C     1 
ATOM   736  O  O     . ASP A 1 101 ? -20.943 17.454  -7.781  1.00 21.09 ? 91   ASP A O     1 
ATOM   737  C  CB    . ASP A 1 101 ? -22.866 15.191  -7.661  1.00 20.74 ? 91   ASP A CB    1 
ATOM   738  C  CG    . ASP A 1 101 ? -24.151 14.599  -8.147  1.00 21.48 ? 91   ASP A CG    1 
ATOM   739  O  OD1   . ASP A 1 101 ? -25.016 15.356  -8.536  1.00 23.28 ? 91   ASP A OD1   1 
ATOM   740  O  OD2   . ASP A 1 101 ? -24.280 13.391  -8.155  1.00 21.32 ? 91   ASP A OD2   1 
ATOM   741  N  N     . ASP A 1 102 ? -19.603 15.758  -8.271  1.00 19.69 ? 92   ASP A N     1 
ATOM   742  C  CA    . ASP A 1 102 ? -18.381 16.359  -7.770  1.00 19.57 ? 92   ASP A CA    1 
ATOM   743  C  C     . ASP A 1 102 ? -17.169 15.612  -8.312  1.00 18.59 ? 92   ASP A C     1 
ATOM   744  O  O     . ASP A 1 102 ? -17.257 14.448  -8.704  1.00 18.34 ? 92   ASP A O     1 
ATOM   745  C  CB    . ASP A 1 102 ? -18.366 16.348  -6.240  1.00 20.24 ? 92   ASP A CB    1 
ATOM   746  C  CG    . ASP A 1 102 ? -17.324 17.285  -5.662  1.00 20.89 ? 92   ASP A CG    1 
ATOM   747  O  OD1   . ASP A 1 102 ? -16.706 18.042  -6.439  1.00 21.08 ? 92   ASP A OD1   1 
ATOM   748  O  OD2   . ASP A 1 102 ? -17.123 17.264  -4.429  1.00 22.89 ? 92   ASP A OD2   1 
ATOM   749  N  N     . PHE A 1 103 ? -16.040 16.304  -8.327  1.00 18.16 ? 93   PHE A N     1 
ATOM   750  C  CA    . PHE A 1 103 ? -14.802 15.780  -8.802  1.00 18.03 ? 93   PHE A CA    1 
ATOM   751  C  C     . PHE A 1 103 ? -13.789 16.136  -7.699  1.00 17.73 ? 93   PHE A C     1 
ATOM   752  O  O     . PHE A 1 103 ? -13.514 17.247  -7.477  1.00 18.37 ? 93   PHE A O     1 
ATOM   753  C  CB    . PHE A 1 103 ? -14.432 16.409  -10.131 1.00 18.06 ? 93   PHE A CB    1 
ATOM   754  C  CG    . PHE A 1 103 ? -13.244 15.797  -10.795 1.00 18.11 ? 93   PHE A CG    1 
ATOM   755  C  CD1   . PHE A 1 103 ? -13.393 14.974  -11.866 1.00 17.89 ? 93   PHE A CD1   1 
ATOM   756  C  CD2   . PHE A 1 103 ? -11.988 16.064  -10.361 1.00 18.21 ? 93   PHE A CD2   1 
ATOM   757  C  CE1   . PHE A 1 103 ? -12.298 14.448  -12.506 1.00 18.21 ? 93   PHE A CE1   1 
ATOM   758  C  CE2   . PHE A 1 103 ? -10.887 15.518  -10.975 1.00 18.64 ? 93   PHE A CE2   1 
ATOM   759  C  CZ    . PHE A 1 103 ? -11.041 14.712  -12.056 1.00 18.13 ? 93   PHE A CZ    1 
ATOM   760  N  N     . ILE A 1 104 ? -13.319 15.132  -7.004  1.00 17.23 ? 94   ILE A N     1 
ATOM   761  C  CA    . ILE A 1 104 ? -12.384 15.314  -5.903  1.00 17.41 ? 94   ILE A CA    1 
ATOM   762  C  C     . ILE A 1 104 ? -10.939 15.170  -6.380  1.00 17.51 ? 94   ILE A C     1 
ATOM   763  O  O     . ILE A 1 104 ? -10.592 14.201  -7.038  1.00 18.08 ? 94   ILE A O     1 
ATOM   764  C  CB    . ILE A 1 104 ? -12.711 14.370  -4.717  1.00 17.80 ? 94   ILE A CB    1 
ATOM   765  C  CG1   . ILE A 1 104 ? -11.804 14.659  -3.506  1.00 17.79 ? 94   ILE A CG1   1 
ATOM   766  C  CG2   . ILE A 1 104 ? -12.623 12.895  -5.100  1.00 17.72 ? 94   ILE A CG2   1 
ATOM   767  C  CD1   . ILE A 1 104 ? -11.986 16.024  -2.885  1.00 18.28 ? 94   ILE A CD1   1 
ATOM   768  N  N     . ARG A 1 105 ? -10.114 16.157  -6.058  1.00 17.19 ? 95   ARG A N     1 
ATOM   769  C  CA    . ARG A 1 105 ? -8.669  16.119  -6.319  1.00 17.51 ? 95   ARG A CA    1 
ATOM   770  C  C     . ARG A 1 105 ? -7.937  16.059  -4.998  1.00 17.52 ? 95   ARG A C     1 
ATOM   771  O  O     . ARG A 1 105 ? -8.228  16.837  -4.083  1.00 18.02 ? 95   ARG A O     1 
ATOM   772  C  CB    . ARG A 1 105 ? -8.238  17.356  -7.085  1.00 17.98 ? 95   ARG A CB    1 
ATOM   773  C  CG    . ARG A 1 105 ? -8.976  17.569  -8.405  1.00 18.45 ? 95   ARG A CG    1 
ATOM   774  C  CD    . ARG A 1 105 ? -8.433  18.803  -9.133  1.00 19.36 ? 95   ARG A CD    1 
ATOM   775  N  NE    . ARG A 1 105 ? -6.994  18.692  -9.416  1.00 19.65 ? 95   ARG A NE    1 
ATOM   776  C  CZ    . ARG A 1 105 ? -6.244  19.622  -10.018 1.00 21.05 ? 95   ARG A CZ    1 
ATOM   777  N  NH1   . ARG A 1 105 ? -6.782  20.762  -10.460 1.00 21.42 ? 95   ARG A NH1   1 
ATOM   778  N  NH2   . ARG A 1 105 ? -4.943  19.412  -10.187 1.00 21.30 ? 95   ARG A NH2   1 
ATOM   779  N  N     . THR A 1 106 ? -6.990  15.136  -4.858  1.00 17.06 ? 96   THR A N     1 
ATOM   780  C  CA    . THR A 1 106 ? -6.296  15.024  -3.563  1.00 17.43 ? 96   THR A CA    1 
ATOM   781  C  C     . THR A 1 106 ? -5.348  16.190  -3.238  1.00 17.67 ? 96   THR A C     1 
ATOM   782  O  O     . THR A 1 106 ? -4.908  16.324  -2.094  1.00 18.09 ? 96   THR A O     1 
ATOM   783  C  CB    . THR A 1 106 ? -5.568  13.685  -3.390  1.00 17.34 ? 96   THR A CB    1 
ATOM   784  O  OG1   . THR A 1 106 ? -4.552  13.553  -4.387  1.00 18.01 ? 96   THR A OG1   1 
ATOM   785  C  CG2   . THR A 1 106 ? -6.543  12.530  -3.449  1.00 17.73 ? 96   THR A CG2   1 
ATOM   786  N  N     . THR A 1 107 ? -5.049  17.035  -4.238  1.00 18.28 ? 97   THR A N     1 
ATOM   787  C  CA    . THR A 1 107 ? -4.355  18.307  -4.041  1.00 18.97 ? 97   THR A CA    1 
ATOM   788  C  C     . THR A 1 107 ? -5.219  19.435  -3.444  1.00 19.84 ? 97   THR A C     1 
ATOM   789  O  O     . THR A 1 107 ? -4.682  20.435  -3.001  1.00 20.26 ? 97   THR A O     1 
ATOM   790  C  CB    . THR A 1 107 ? -3.753  18.800  -5.377  1.00 19.04 ? 97   THR A CB    1 
ATOM   791  O  OG1   . THR A 1 107 ? -4.728  18.638  -6.419  1.00 18.42 ? 97   THR A OG1   1 
ATOM   792  C  CG2   . THR A 1 107 ? -2.518  18.015  -5.713  1.00 19.08 ? 97   THR A CG2   1 
ATOM   793  N  N     . GLU A 1 108 ? -6.543  19.286  -3.439  1.00 20.12 ? 98   GLU A N     1 
ATOM   794  C  CA    . GLU A 1 108 ? -7.435  20.307  -2.865  1.00 21.19 ? 98   GLU A CA    1 
ATOM   795  C  C     . GLU A 1 108 ? -7.334  20.360  -1.348  1.00 20.94 ? 98   GLU A C     1 
ATOM   796  O  O     . GLU A 1 108 ? -7.186  19.334  -0.693  1.00 19.04 ? 98   GLU A O     1 
ATOM   797  C  CB    . GLU A 1 108 ? -8.876  20.043  -3.311  1.00 22.16 ? 98   GLU A CB    1 
ATOM   798  C  CG    . GLU A 1 108 ? -9.093  20.431  -4.757  1.00 23.81 ? 98   GLU A CG    1 
ATOM   799  C  CD    . GLU A 1 108 ? -10.368 19.909  -5.389  1.00 25.12 ? 98   GLU A CD    1 
ATOM   800  O  OE1   . GLU A 1 108 ? -10.682 20.414  -6.493  1.00 28.30 ? 98   GLU A OE1   1 
ATOM   801  O  OE2   . GLU A 1 108 ? -11.038 18.988  -4.861  1.00 25.61 ? 98   GLU A OE2   1 
ATOM   802  N  N     . GLU A 1 109 ? -7.380  21.566  -0.783  1.00 21.37 ? 99   GLU A N     1 
ATOM   803  C  CA    . GLU A 1 109 ? -7.240  21.715  0.669   1.00 22.16 ? 99   GLU A CA    1 
ATOM   804  C  C     . GLU A 1 109 ? -8.353  20.961  1.410   1.00 20.84 ? 99   GLU A C     1 
ATOM   805  O  O     . GLU A 1 109 ? -8.121  20.411  2.465   1.00 20.28 ? 99   GLU A O     1 
ATOM   806  C  CB    . GLU A 1 109 ? -7.221  23.200  1.059   1.00 23.78 ? 99   GLU A CB    1 
ATOM   807  C  CG    . GLU A 1 109 ? -7.253  23.491  2.563   1.00 25.14 ? 99   GLU A CG    1 
ATOM   808  C  CD    . GLU A 1 109 ? -6.162  22.819  3.388   1.00 26.58 ? 99   GLU A CD    1 
ATOM   809  O  OE1   . GLU A 1 109 ? -5.075  22.476  2.859   1.00 28.29 ? 99   GLU A OE1   1 
ATOM   810  O  OE2   . GLU A 1 109 ? -6.385  22.643  4.607   1.00 28.25 ? 99   GLU A OE2   1 
ATOM   811  N  N     . ARG A 1 110 ? -9.559  20.921  0.847   1.00 20.64 ? 100  ARG A N     1 
ATOM   812  C  CA    . ARG A 1 110 ? -10.653 20.174  1.490   1.00 20.08 ? 100  ARG A CA    1 
ATOM   813  C  C     . ARG A 1 110 ? -10.302 18.697  1.724   1.00 19.32 ? 100  ARG A C     1 
ATOM   814  O  O     . ARG A 1 110 ? -10.752 18.081  2.704   1.00 19.93 ? 100  ARG A O     1 
ATOM   815  C  CB    . ARG A 1 110 ? -11.953 20.308  0.714   1.00 20.99 ? 100  ARG A CB    1 
ATOM   816  C  CG    . ARG A 1 110 ? -11.910 19.760  -0.699  1.00 21.09 ? 100  ARG A CG    1 
ATOM   817  C  CD    . ARG A 1 110 ? -13.294 19.744  -1.294  1.00 21.64 ? 100  ARG A CD    1 
ATOM   818  N  NE    . ARG A 1 110 ? -13.241 19.399  -2.717  1.00 21.37 ? 100  ARG A NE    1 
ATOM   819  C  CZ    . ARG A 1 110 ? -14.246 18.865  -3.416  1.00 21.47 ? 100  ARG A CZ    1 
ATOM   820  N  NH1   . ARG A 1 110 ? -15.419 18.589  -2.855  1.00 21.67 ? 100  ARG A NH1   1 
ATOM   821  N  NH2   . ARG A 1 110 ? -14.053 18.584  -4.692  1.00 20.76 ? 100  ARG A NH2   1 
ATOM   822  N  N     . HIS A 1 111 ? -9.485  18.142  0.831   1.00 18.28 ? 101  HIS A N     1 
ATOM   823  C  CA    . HIS A 1 111 ? -8.991  16.797  0.981   1.00 17.88 ? 101  HIS A CA    1 
ATOM   824  C  C     . HIS A 1 111 ? -7.800  16.735  1.926   1.00 18.53 ? 101  HIS A C     1 
ATOM   825  O  O     . HIS A 1 111 ? -7.784  15.935  2.866   1.00 18.89 ? 101  HIS A O     1 
ATOM   826  C  CB    . HIS A 1 111 ? -8.603  16.195  -0.360  1.00 17.40 ? 101  HIS A CB    1 
ATOM   827  C  CG    . HIS A 1 111 ? -8.113  14.793  -0.242  1.00 17.10 ? 101  HIS A CG    1 
ATOM   828  N  ND1   . HIS A 1 111 ? -8.963  13.734  -0.012  1.00 17.65 ? 101  HIS A ND1   1 
ATOM   829  C  CD2   . HIS A 1 111 ? -6.859  14.285  -0.222  1.00 17.26 ? 101  HIS A CD2   1 
ATOM   830  C  CE1   . HIS A 1 111 ? -8.254  12.625  0.093   1.00 17.06 ? 101  HIS A CE1   1 
ATOM   831  N  NE2   . HIS A 1 111 ? -6.974  12.930  -0.031  1.00 16.82 ? 101  HIS A NE2   1 
ATOM   832  N  N     . LYS A 1 112 ? -6.794  17.563  1.670   1.00 18.76 ? 102  LYS A N     1 
ATOM   833  C  CA    . LYS A 1 112 ? -5.580  17.527  2.480   1.00 19.97 ? 102  LYS A CA    1 
ATOM   834  C  C     . LYS A 1 112 ? -5.878  17.741  3.961   1.00 19.56 ? 102  LYS A C     1 
ATOM   835  O  O     . LYS A 1 112 ? -5.267  17.110  4.824   1.00 19.37 ? 102  LYS A O     1 
ATOM   836  C  CB    . LYS A 1 112 ? -4.589  18.576  1.994   1.00 21.09 ? 102  LYS A CB    1 
ATOM   837  C  CG    . LYS A 1 112 ? -4.067  18.297  0.595   1.00 22.03 ? 102  LYS A CG    1 
ATOM   838  C  CD    . LYS A 1 112 ? -3.037  19.321  0.165   1.00 23.92 ? 102  LYS A CD    1 
ATOM   839  C  CE    . LYS A 1 112 ? -1.760  19.173  0.982   1.00 25.40 ? 102  LYS A CE    1 
ATOM   840  N  NZ    . LYS A 1 112 ? -0.662  19.970  0.370   1.00 27.36 ? 102  LYS A NZ    1 
ATOM   841  N  N     . HIS A 1 113 ? -6.828  18.615  4.255   1.00 20.14 ? 103  HIS A N     1 
ATOM   842  C  CA    . HIS A 1 113 ? -7.225  18.856  5.653   1.00 21.40 ? 103  HIS A CA    1 
ATOM   843  C  C     . HIS A 1 113 ? -7.684  17.563  6.347   1.00 20.24 ? 103  HIS A C     1 
ATOM   844  O  O     . HIS A 1 113 ? -7.316  17.295  7.500   1.00 20.58 ? 103  HIS A O     1 
ATOM   845  C  CB    . HIS A 1 113 ? -8.325  19.922  5.739   1.00 23.37 ? 103  HIS A CB    1 
ATOM   846  C  CG    . HIS A 1 113 ? -8.762  20.210  7.144   1.00 25.00 ? 103  HIS A CG    1 
ATOM   847  N  ND1   . HIS A 1 113 ? -7.982  20.913  8.037   1.00 26.38 ? 103  HIS A ND1   1 
ATOM   848  C  CD2   . HIS A 1 113 ? -9.883  19.859  7.821   1.00 27.08 ? 103  HIS A CD2   1 
ATOM   849  C  CE1   . HIS A 1 113 ? -8.605  20.990  9.200   1.00 27.36 ? 103  HIS A CE1   1 
ATOM   850  N  NE2   . HIS A 1 113 ? -9.759  20.356  9.097   1.00 27.51 ? 103  HIS A NE2   1 
ATOM   851  N  N     . VAL A 1 114 ? -8.483  16.766  5.641   1.00 19.11 ? 104  VAL A N     1 
ATOM   852  C  CA    . VAL A 1 114 ? -8.963  15.500  6.168   1.00 18.63 ? 104  VAL A CA    1 
ATOM   853  C  C     . VAL A 1 114 ? -7.840  14.486  6.355   1.00 18.38 ? 104  VAL A C     1 
ATOM   854  O  O     . VAL A 1 114 ? -7.774  13.812  7.375   1.00 18.89 ? 104  VAL A O     1 
ATOM   855  C  CB    . VAL A 1 114 ? -10.079 14.913  5.273   1.00 18.55 ? 104  VAL A CB    1 
ATOM   856  C  CG1   . VAL A 1 114 ? -10.470 13.501  5.700   1.00 18.85 ? 104  VAL A CG1   1 
ATOM   857  C  CG2   . VAL A 1 114 ? -11.278 15.824  5.297   1.00 19.05 ? 104  VAL A CG2   1 
ATOM   858  N  N     . VAL A 1 115 ? -6.940  14.402  5.385   1.00 18.33 ? 105  VAL A N     1 
ATOM   859  C  CA    . VAL A 1 115 ? -5.815  13.489  5.468   1.00 18.53 ? 105  VAL A CA    1 
ATOM   860  C  C     . VAL A 1 115 ? -4.986  13.842  6.709   1.00 19.30 ? 105  VAL A C     1 
ATOM   861  O  O     . VAL A 1 115 ? -4.626  12.955  7.486   1.00 19.68 ? 105  VAL A O     1 
ATOM   862  C  CB    . VAL A 1 115 ? -4.931  13.544  4.205   1.00 18.07 ? 105  VAL A CB    1 
ATOM   863  C  CG1   . VAL A 1 115 ? -3.702  12.657  4.353   1.00 18.44 ? 105  VAL A CG1   1 
ATOM   864  C  CG2   . VAL A 1 115 ? -5.715  13.135  2.954   1.00 18.15 ? 105  VAL A CG2   1 
ATOM   865  N  N     . GLU A 1 116 ? -4.710  15.134  6.897   1.00 19.84 ? 106  GLU A N     1 
ATOM   866  C  CA    . GLU A 1 116 ? -3.973  15.616  8.066   1.00 21.07 ? 106  GLU A CA    1 
ATOM   867  C  C     . GLU A 1 116 ? -4.684  15.251  9.376   1.00 20.69 ? 106  GLU A C     1 
ATOM   868  O  O     . GLU A 1 116 ? -4.065  14.722  10.302  1.00 20.81 ? 106  GLU A O     1 
ATOM   869  C  CB    . GLU A 1 116 ? -3.792  17.135  8.005   1.00 21.78 ? 106  GLU A CB    1 
ATOM   870  C  CG    . GLU A 1 116 ? -2.806  17.586  6.930   1.00 23.27 ? 106  GLU A CG    1 
ATOM   871  C  CD    . GLU A 1 116 ? -2.960  19.049  6.531   1.00 25.84 ? 106  GLU A CD    1 
ATOM   872  O  OE1   . GLU A 1 116 ? -3.717  19.813  7.173   1.00 26.85 ? 106  GLU A OE1   1 
ATOM   873  O  OE2   . GLU A 1 116 ? -2.336  19.436  5.521   1.00 28.58 ? 106  GLU A OE2   1 
ATOM   874  N  N     . GLN A 1 117 ? -5.975  15.538  9.443   1.00 21.03 ? 107  GLN A N     1 
ATOM   875  C  CA    . GLN A 1 117 ? -6.735  15.348  10.689  1.00 22.27 ? 107  GLN A CA    1 
ATOM   876  C  C     . GLN A 1 117 ? -6.931  13.879  11.043  1.00 21.64 ? 107  GLN A C     1 
ATOM   877  O  O     . GLN A 1 117 ? -6.853  13.502  12.223  1.00 21.26 ? 107  GLN A O     1 
ATOM   878  C  CB    . GLN A 1 117 ? -8.081  16.090  10.642  1.00 24.06 ? 107  GLN A CB    1 
ATOM   879  C  CG    . GLN A 1 117 ? -7.963  17.615  10.744  1.00 26.51 ? 107  GLN A CG    1 
ATOM   880  C  CD    . GLN A 1 117 ? -7.263  18.045  12.031  1.00 29.39 ? 107  GLN A CD    1 
ATOM   881  O  OE1   . GLN A 1 117 ? -7.793  17.851  13.131  1.00 32.83 ? 107  GLN A OE1   1 
ATOM   882  N  NE2   . GLN A 1 117 ? -6.058  18.598  11.901  1.00 31.08 ? 107  GLN A NE2   1 
ATOM   883  N  N     . VAL A 1 118 ? -7.202  13.056  10.031  1.00 20.57 ? 108  VAL A N     1 
ATOM   884  C  CA    . VAL A 1 118 ? -7.295  11.605  10.202  1.00 20.03 ? 108  VAL A CA    1 
ATOM   885  C  C     . VAL A 1 118 ? -5.975  11.037  10.710  1.00 20.07 ? 108  VAL A C     1 
ATOM   886  O  O     . VAL A 1 118 ? -5.945  10.276  11.679  1.00 20.47 ? 108  VAL A O     1 
ATOM   887  C  CB    . VAL A 1 118 ? -7.716  10.924  8.888   1.00 20.00 ? 108  VAL A CB    1 
ATOM   888  C  CG1   . VAL A 1 118 ? -7.493  9.420   8.913   1.00 19.79 ? 108  VAL A CG1   1 
ATOM   889  C  CG2   . VAL A 1 118 ? -9.178  11.238  8.592   1.00 19.88 ? 108  VAL A CG2   1 
ATOM   890  N  N     . PHE A 1 119 ? -4.875  11.399  10.057  1.00 18.94 ? 109  PHE A N     1 
ATOM   891  C  CA    . PHE A 1 119 ? -3.577  10.913  10.471  1.00 19.59 ? 109  PHE A CA    1 
ATOM   892  C  C     . PHE A 1 119 ? -3.266  11.315  11.926  1.00 20.31 ? 109  PHE A C     1 
ATOM   893  O  O     . PHE A 1 119 ? -2.860  10.485  12.746  1.00 20.63 ? 109  PHE A O     1 
ATOM   894  C  CB    . PHE A 1 119 ? -2.480  11.414  9.514   1.00 19.63 ? 109  PHE A CB    1 
ATOM   895  C  CG    . PHE A 1 119 ? -1.229  10.599  9.567   1.00 20.23 ? 109  PHE A CG    1 
ATOM   896  C  CD1   . PHE A 1 119 ? -0.944  9.667   8.562   1.00 20.38 ? 109  PHE A CD1   1 
ATOM   897  C  CD2   . PHE A 1 119 ? -0.320  10.756  10.605  1.00 20.66 ? 109  PHE A CD2   1 
ATOM   898  C  CE1   . PHE A 1 119 ? 0.197   8.898   8.612   1.00 20.44 ? 109  PHE A CE1   1 
ATOM   899  C  CE2   . PHE A 1 119 ? 0.829   9.979   10.661  1.00 20.81 ? 109  PHE A CE2   1 
ATOM   900  C  CZ    . PHE A 1 119 ? 1.086   9.054   9.661   1.00 21.17 ? 109  PHE A CZ    1 
ATOM   901  N  N     . GLU A 1 120 ? -3.477  12.582  12.248  1.00 21.05 ? 110  GLU A N     1 
ATOM   902  C  CA    . GLU A 1 120 ? -3.201  13.092  13.593  1.00 21.89 ? 110  GLU A CA    1 
ATOM   903  C  C     . GLU A 1 120 ? -4.081  12.432  14.657  1.00 22.25 ? 110  GLU A C     1 
ATOM   904  O  O     . GLU A 1 120 ? -3.614  12.188  15.767  1.00 22.69 ? 110  GLU A O     1 
ATOM   905  C  CB    . GLU A 1 120 ? -3.363  14.614  13.635  1.00 23.56 ? 110  GLU A CB    1 
ATOM   906  C  CG    . GLU A 1 120 ? -2.261  15.383  12.904  1.00 24.30 ? 110  GLU A CG    1 
ATOM   907  C  CD    . GLU A 1 120 ? -0.886  15.223  13.531  1.00 26.82 ? 110  GLU A CD    1 
ATOM   908  O  OE1   . GLU A 1 120 ? -0.766  15.299  14.771  1.00 29.53 ? 110  GLU A OE1   1 
ATOM   909  O  OE2   . GLU A 1 120 ? 0.094   15.028  12.786  1.00 28.82 ? 110  GLU A OE2   1 
ATOM   910  N  N     . ARG A 1 121 ? -5.335  12.148  14.311  1.00 22.12 ? 111  ARG A N     1 
ATOM   911  C  CA    . ARG A 1 121 ? -6.256  11.451  15.220  1.00 22.34 ? 111  ARG A CA    1 
ATOM   912  C  C     . ARG A 1 121 ? -5.760  10.044  15.520  1.00 22.54 ? 111  ARG A C     1 
ATOM   913  O  O     . ARG A 1 121 ? -5.760  9.623   16.674  1.00 22.96 ? 111  ARG A O     1 
ATOM   914  C  CB    . ARG A 1 121 ? -7.676  11.394  14.664  1.00 23.16 ? 111  ARG A CB    1 
ATOM   915  C  CG    . ARG A 1 121 ? -8.624  10.529  15.493  1.00 23.96 ? 111  ARG A CG    1 
ATOM   916  C  CD    . ARG A 1 121 ? -10.052 10.704  15.050  1.00 24.70 ? 111  ARG A CD    1 
ATOM   917  N  NE    . ARG A 1 121 ? -10.923 9.800   15.786  1.00 25.44 ? 111  ARG A NE    1 
ATOM   918  C  CZ    . ARG A 1 121 ? -12.241 9.717   15.650  1.00 26.51 ? 111  ARG A CZ    1 
ATOM   919  N  NH1   . ARG A 1 121 ? -12.881 10.470  14.759  1.00 27.35 ? 111  ARG A NH1   1 
ATOM   920  N  NH2   . ARG A 1 121 ? -12.919 8.856   16.412  1.00 26.94 ? 111  ARG A NH2   1 
ATOM   921  N  N     . LEU A 1 122 ? -5.331  9.319   14.490  1.00 21.86 ? 112  LEU A N     1 
ATOM   922  C  CA    . LEU A 1 122 ? -4.850  7.958   14.679  1.00 22.89 ? 112  LEU A CA    1 
ATOM   923  C  C     . LEU A 1 122 ? -3.540  7.933   15.490  1.00 23.26 ? 112  LEU A C     1 
ATOM   924  O  O     . LEU A 1 122 ? -3.330  7.035   16.315  1.00 23.28 ? 112  LEU A O     1 
ATOM   925  C  CB    . LEU A 1 122 ? -4.709  7.217   13.335  1.00 23.61 ? 112  LEU A CB    1 
ATOM   926  C  CG    . LEU A 1 122 ? -5.964  6.426   12.944  1.00 25.06 ? 112  LEU A CG    1 
ATOM   927  C  CD1   . LEU A 1 122 ? -7.206  7.292   12.839  1.00 26.47 ? 112  LEU A CD1   1 
ATOM   928  C  CD2   . LEU A 1 122 ? -5.718  5.674   11.636  1.00 26.06 ? 112  LEU A CD2   1 
ATOM   929  N  N     . LEU A 1 123 ? -2.685  8.931   15.272  1.00 23.55 ? 113  LEU A N     1 
ATOM   930  C  CA    . LEU A 1 123 ? -1.466  9.100   16.065  1.00 24.81 ? 113  LEU A CA    1 
ATOM   931  C  C     . LEU A 1 123 ? -1.796  9.355   17.534  1.00 25.11 ? 113  LEU A C     1 
ATOM   932  O  O     . LEU A 1 123 ? -1.237  8.705   18.415  1.00 24.89 ? 113  LEU A O     1 
ATOM   933  C  CB    . LEU A 1 123 ? -0.636  10.265  15.516  1.00 26.65 ? 113  LEU A CB    1 
ATOM   934  C  CG    . LEU A 1 123 ? 0.822   10.354  15.973  1.00 28.79 ? 113  LEU A CG    1 
ATOM   935  C  CD1   . LEU A 1 123 ? 1.624   9.214   15.371  1.00 29.60 ? 113  LEU A CD1   1 
ATOM   936  C  CD2   . LEU A 1 123 ? 1.429   11.693  15.568  1.00 29.64 ? 113  LEU A CD2   1 
ATOM   937  N  N     . LYS A 1 124 ? -2.702  10.296  17.774  1.00 25.26 ? 114  LYS A N     1 
ATOM   938  C  CA    . LYS A 1 124 ? -3.152  10.633  19.140  1.00 26.74 ? 114  LYS A CA    1 
ATOM   939  C  C     . LYS A 1 124 ? -3.749  9.426   19.870  1.00 25.81 ? 114  LYS A C     1 
ATOM   940  O  O     . LYS A 1 124 ? -3.475  9.218   21.054  1.00 26.09 ? 114  LYS A O     1 
ATOM   941  C  CB    . LYS A 1 124 ? -4.173  11.784  19.100  1.00 28.75 ? 114  LYS A CB    1 
ATOM   942  C  CG    . LYS A 1 124 ? -4.565  12.334  20.465  1.00 31.13 ? 114  LYS A CG    1 
ATOM   943  C  CD    . LYS A 1 124 ? -5.409  13.598  20.331  1.00 33.96 ? 114  LYS A CD    1 
ATOM   944  C  CE    . LYS A 1 124 ? -6.122  13.950  21.636  1.00 36.27 ? 114  LYS A CE    1 
ATOM   945  N  NZ    . LYS A 1 124 ? -5.186  14.226  22.759  1.00 38.21 ? 114  LYS A NZ    1 
ATOM   946  N  N     . GLN A 1 125 ? -4.570  8.648   19.162  1.00 24.69 ? 115  GLN A N     1 
ATOM   947  C  CA    . GLN A 1 125 ? -5.211  7.444   19.720  1.00 24.50 ? 115  GLN A CA    1 
ATOM   948  C  C     . GLN A 1 125 ? -4.215  6.332   20.014  1.00 24.53 ? 115  GLN A C     1 
ATOM   949  O  O     . GLN A 1 125 ? -4.436  5.509   20.905  1.00 25.12 ? 115  GLN A O     1 
ATOM   950  C  CB    . GLN A 1 125 ? -6.307  6.928   18.764  1.00 23.72 ? 115  GLN A CB    1 
ATOM   951  C  CG    . GLN A 1 125 ? -7.489  7.871   18.679  1.00 23.69 ? 115  GLN A CG    1 
ATOM   952  C  CD    . GLN A 1 125 ? -8.585  7.442   17.726  1.00 23.65 ? 115  GLN A CD    1 
ATOM   953  O  OE1   . GLN A 1 125 ? -9.676  8.018   17.749  1.00 24.06 ? 115  GLN A OE1   1 
ATOM   954  N  NE2   . GLN A 1 125 ? -8.326  6.416   16.899  1.00 23.45 ? 115  GLN A NE2   1 
ATOM   955  N  N     . GLY A 1 126 ? -3.113  6.324   19.271  1.00 24.06 ? 116  GLY A N     1 
ATOM   956  C  CA    . GLY A 1 126 ? -2.123  5.264   19.344  1.00 24.06 ? 116  GLY A CA    1 
ATOM   957  C  C     . GLY A 1 126 ? -2.298  4.148   18.332  1.00 23.37 ? 116  GLY A C     1 
ATOM   958  O  O     . GLY A 1 126 ? -1.638  3.128   18.434  1.00 23.68 ? 116  GLY A O     1 
ATOM   959  N  N     . ASP A 1 127 ? -3.190  4.332   17.352  1.00 23.13 ? 117  ASP A N     1 
ATOM   960  C  CA    . ASP A 1 127 ? -3.357  3.376   16.248  1.00 23.28 ? 117  ASP A CA    1 
ATOM   961  C  C     . ASP A 1 127 ? -2.138  3.381   15.326  1.00 23.08 ? 117  ASP A C     1 
ATOM   962  O  O     . ASP A 1 127 ? -1.818  2.370   14.715  1.00 23.02 ? 117  ASP A O     1 
ATOM   963  C  CB    . ASP A 1 127 ? -4.606  3.718   15.422  1.00 23.32 ? 117  ASP A CB    1 
ATOM   964  C  CG    . ASP A 1 127 ? -5.888  3.268   16.089  1.00 23.92 ? 117  ASP A CG    1 
ATOM   965  O  OD1   . ASP A 1 127 ? -6.203  2.056   16.002  1.00 24.56 ? 117  ASP A OD1   1 
ATOM   966  O  OD2   . ASP A 1 127 ? -6.589  4.126   16.683  1.00 24.78 ? 117  ASP A OD2   1 
ATOM   967  N  N     . ILE A 1 128 ? -1.486  4.538   15.229  1.00 23.75 ? 118  ILE A N     1 
ATOM   968  C  CA    . ILE A 1 128 ? -0.280  4.719   14.425  1.00 23.39 ? 118  ILE A CA    1 
ATOM   969  C  C     . ILE A 1 128 ? 0.925   4.963   15.322  1.00 24.04 ? 118  ILE A C     1 
ATOM   970  O  O     . ILE A 1 128 ? 0.844   5.731   16.281  1.00 24.01 ? 118  ILE A O     1 
ATOM   971  C  CB    . ILE A 1 128 ? -0.452  5.897   13.439  1.00 23.47 ? 118  ILE A CB    1 
ATOM   972  C  CG1   . ILE A 1 128 ? -1.455  5.510   12.340  1.00 23.41 ? 118  ILE A CG1   1 
ATOM   973  C  CG2   . ILE A 1 128 ? 0.887   6.277   12.805  1.00 24.39 ? 118  ILE A CG2   1 
ATOM   974  C  CD1   . ILE A 1 128 ? -1.864  6.657   11.427  1.00 22.77 ? 118  ILE A CD1   1 
ATOM   975  N  N     . TYR A 1 129 ? 2.048   4.339   14.982  1.00 24.86 ? 119  TYR A N     1 
ATOM   976  C  CA    . TYR A 1 129 ? 3.309   4.569   15.687  1.00 25.76 ? 119  TYR A CA    1 
ATOM   977  C  C     . TYR A 1 129 ? 4.484   4.518   14.736  1.00 25.81 ? 119  TYR A C     1 
ATOM   978  O  O     . TYR A 1 129 ? 4.404   3.925   13.665  1.00 24.70 ? 119  TYR A O     1 
ATOM   979  C  CB    . TYR A 1 129 ? 3.511   3.552   16.797  1.00 27.12 ? 119  TYR A CB    1 
ATOM   980  C  CG    . TYR A 1 129 ? 3.241   2.129   16.401  1.00 28.85 ? 119  TYR A CG    1 
ATOM   981  C  CD1   . TYR A 1 129 ? 2.014   1.536   16.710  1.00 30.17 ? 119  TYR A CD1   1 
ATOM   982  C  CD2   . TYR A 1 129 ? 4.201   1.358   15.738  1.00 30.09 ? 119  TYR A CD2   1 
ATOM   983  C  CE1   . TYR A 1 129 ? 1.745   0.221   16.376  1.00 31.28 ? 119  TYR A CE1   1 
ATOM   984  C  CE2   . TYR A 1 129 ? 3.932   0.038   15.387  1.00 31.23 ? 119  TYR A CE2   1 
ATOM   985  C  CZ    . TYR A 1 129 ? 2.699   -0.520  15.713  1.00 31.91 ? 119  TYR A CZ    1 
ATOM   986  O  OH    . TYR A 1 129 ? 2.384   -1.825  15.408  1.00 33.97 ? 119  TYR A OH    1 
ATOM   987  N  N     . LEU A 1 130 ? 5.576   5.140   15.168  1.00 25.37 ? 120  LEU A N     1 
ATOM   988  C  CA    . LEU A 1 130 ? 6.757   5.325   14.341  1.00 25.93 ? 120  LEU A CA    1 
ATOM   989  C  C     . LEU A 1 130 ? 7.596   4.062   14.285  1.00 26.44 ? 120  LEU A C     1 
ATOM   990  O  O     . LEU A 1 130 ? 7.854   3.439   15.312  1.00 26.59 ? 120  LEU A O     1 
ATOM   991  C  CB    . LEU A 1 130 ? 7.596   6.488   14.885  1.00 26.39 ? 120  LEU A CB    1 
ATOM   992  C  CG    . LEU A 1 130 ? 8.700   7.010   13.953  1.00 27.02 ? 120  LEU A CG    1 
ATOM   993  C  CD1   . LEU A 1 130 ? 8.139   7.650   12.691  1.00 26.77 ? 120  LEU A CD1   1 
ATOM   994  C  CD2   . LEU A 1 130 ? 9.576   8.000   14.701  1.00 27.86 ? 120  LEU A CD2   1 
ATOM   995  N  N     . GLY A 1 131 ? 8.031   3.708   13.079  1.00 26.12 ? 121  GLY A N     1 
ATOM   996  C  CA    . GLY A 1 131 ? 8.901   2.556   12.843  1.00 26.55 ? 121  GLY A CA    1 
ATOM   997  C  C     . GLY A 1 131 ? 9.802   2.767   11.632  1.00 26.83 ? 121  GLY A C     1 
ATOM   998  O  O     . GLY A 1 131 ? 10.080  3.902   11.253  1.00 26.62 ? 121  GLY A O     1 
ATOM   999  N  N     . GLU A 1 132 ? 10.268  1.662   11.056  1.00 27.71 ? 122  GLU A N     1 
ATOM   1000 C  CA    . GLU A 1 132 ? 11.027  1.653   9.802   1.00 29.17 ? 122  GLU A CA    1 
ATOM   1001 C  C     . GLU A 1 132 ? 10.380  0.708   8.796   1.00 28.68 ? 122  GLU A C     1 
ATOM   1002 O  O     . GLU A 1 132 ? 10.225  -0.485  9.054   1.00 28.63 ? 122  GLU A O     1 
ATOM   1003 C  CB    . GLU A 1 132 ? 12.478  1.212   10.033  1.00 30.72 ? 122  GLU A CB    1 
ATOM   1004 C  CG    . GLU A 1 132 ? 13.362  1.268   8.785   1.00 31.98 ? 122  GLU A CG    1 
ATOM   1005 C  CD    . GLU A 1 132 ? 14.786  0.797   9.053   1.00 34.05 ? 122  GLU A CD    1 
ATOM   1006 O  OE1   . GLU A 1 132 ? 15.724  1.577   8.833   1.00 36.57 ? 122  GLU A OE1   1 
ATOM   1007 O  OE2   . GLU A 1 132 ? 14.961  -0.357  9.487   1.00 35.82 ? 122  GLU A OE2   1 
ATOM   1008 N  N     . TYR A 1 133 ? 10.019  1.250   7.639   1.00 29.35 ? 123  TYR A N     1 
ATOM   1009 C  CA    . TYR A 1 133 ? 9.545   0.449   6.524   1.00 29.86 ? 123  TYR A CA    1 
ATOM   1010 C  C     . TYR A 1 133 ? 10.734  -0.256  5.885   1.00 31.33 ? 123  TYR A C     1 
ATOM   1011 O  O     . TYR A 1 133 ? 11.783  0.353   5.714   1.00 30.73 ? 123  TYR A O     1 
ATOM   1012 C  CB    . TYR A 1 133 ? 8.846   1.340   5.490   1.00 29.56 ? 123  TYR A CB    1 
ATOM   1013 C  CG    . TYR A 1 133 ? 8.515   0.624   4.205   1.00 29.58 ? 123  TYR A CG    1 
ATOM   1014 C  CD1   . TYR A 1 133 ? 7.467   -0.285  4.147   1.00 29.26 ? 123  TYR A CD1   1 
ATOM   1015 C  CD2   . TYR A 1 133 ? 9.270   0.833   3.050   1.00 30.00 ? 123  TYR A CD2   1 
ATOM   1016 C  CE1   . TYR A 1 133 ? 7.168   -0.958  2.972   1.00 29.87 ? 123  TYR A CE1   1 
ATOM   1017 C  CE2   . TYR A 1 133 ? 8.986   0.160   1.876   1.00 29.83 ? 123  TYR A CE2   1 
ATOM   1018 C  CZ    . TYR A 1 133 ? 7.940   -0.730  1.835   1.00 29.86 ? 123  TYR A CZ    1 
ATOM   1019 O  OH    . TYR A 1 133 ? 7.671   -1.383  0.661   1.00 30.47 ? 123  TYR A OH    1 
ATOM   1020 N  N     . GLU A 1 134 ? 10.558  -1.533  5.557   1.00 33.15 ? 124  GLU A N     1 
ATOM   1021 C  CA    . GLU A 1 134 ? 11.505  -2.288  4.728   1.00 35.81 ? 124  GLU A CA    1 
ATOM   1022 C  C     . GLU A 1 134 ? 10.744  -2.923  3.586   1.00 34.94 ? 124  GLU A C     1 
ATOM   1023 O  O     . GLU A 1 134 ? 9.722   -3.565  3.807   1.00 34.20 ? 124  GLU A O     1 
ATOM   1024 C  CB    . GLU A 1 134 ? 12.198  -3.416  5.492   1.00 39.01 ? 124  GLU A CB    1 
ATOM   1025 C  CG    . GLU A 1 134 ? 12.931  -3.022  6.760   1.00 41.75 ? 124  GLU A CG    1 
ATOM   1026 C  CD    . GLU A 1 134 ? 13.955  -4.072  7.177   1.00 44.09 ? 124  GLU A CD    1 
ATOM   1027 O  OE1   . GLU A 1 134 ? 14.893  -3.738  7.930   1.00 48.13 ? 124  GLU A OE1   1 
ATOM   1028 O  OE2   . GLU A 1 134 ? 13.831  -5.235  6.742   1.00 46.31 ? 124  GLU A OE2   1 
ATOM   1029 N  N     . GLY A 1 135 ? 11.252  -2.753  2.370   1.00 34.93 ? 125  GLY A N     1 
ATOM   1030 C  CA    . GLY A 1 135 ? 10.658  -3.350  1.184   1.00 35.19 ? 125  GLY A CA    1 
ATOM   1031 C  C     . GLY A 1 135 ? 11.727  -3.762  0.195   1.00 35.74 ? 125  GLY A C     1 
ATOM   1032 O  O     . GLY A 1 135 ? 12.895  -3.417  0.352   1.00 34.48 ? 125  GLY A O     1 
ATOM   1033 N  N     . TRP A 1 136 ? 11.306  -4.502  -0.819  1.00 36.18 ? 126  TRP A N     1 
ATOM   1034 C  CA    . TRP A 1 136 ? 12.191  -4.954  -1.886  1.00 37.59 ? 126  TRP A CA    1 
ATOM   1035 C  C     . TRP A 1 136 ? 11.682  -4.415  -3.213  1.00 38.26 ? 126  TRP A C     1 
ATOM   1036 O  O     . TRP A 1 136 ? 10.643  -4.857  -3.709  1.00 38.02 ? 126  TRP A O     1 
ATOM   1037 C  CB    . TRP A 1 136 ? 12.252  -6.479  -1.886  1.00 38.87 ? 126  TRP A CB    1 
ATOM   1038 C  CG    . TRP A 1 136 ? 12.758  -7.000  -0.585  1.00 39.83 ? 126  TRP A CG    1 
ATOM   1039 C  CD1   . TRP A 1 136 ? 12.018  -7.311  0.517   1.00 40.17 ? 126  TRP A CD1   1 
ATOM   1040 C  CD2   . TRP A 1 136 ? 14.120  -7.228  -0.229  1.00 40.55 ? 126  TRP A CD2   1 
ATOM   1041 N  NE1   . TRP A 1 136 ? 12.832  -7.738  1.533   1.00 40.72 ? 126  TRP A NE1   1 
ATOM   1042 C  CE2   . TRP A 1 136 ? 14.130  -7.695  1.104   1.00 40.74 ? 126  TRP A CE2   1 
ATOM   1043 C  CE3   . TRP A 1 136 ? 15.336  -7.096  -0.910  1.00 41.64 ? 126  TRP A CE3   1 
ATOM   1044 C  CZ2   . TRP A 1 136 ? 15.310  -8.034  1.773   1.00 41.87 ? 126  TRP A CZ2   1 
ATOM   1045 C  CZ3   . TRP A 1 136 ? 16.514  -7.431  -0.245  1.00 42.26 ? 126  TRP A CZ3   1 
ATOM   1046 C  CH2   . TRP A 1 136 ? 16.490  -7.893  1.084   1.00 42.12 ? 126  TRP A CH2   1 
ATOM   1047 N  N     . TYR A 1 137 ? 12.405  -3.438  -3.768  1.00 39.56 ? 127  TYR A N     1 
ATOM   1048 C  CA    . TYR A 1 137 ? 11.957  -2.710  -4.955  1.00 41.21 ? 127  TYR A CA    1 
ATOM   1049 C  C     . TYR A 1 137 ? 12.473  -3.337  -6.240  1.00 42.42 ? 127  TYR A C     1 
ATOM   1050 O  O     . TYR A 1 137 ? 13.656  -3.671  -6.340  1.00 42.42 ? 127  TYR A O     1 
ATOM   1051 C  CB    . TYR A 1 137 ? 12.418  -1.243  -4.902  1.00 41.18 ? 127  TYR A CB    1 
ATOM   1052 C  CG    . TYR A 1 137 ? 11.802  -0.369  -5.986  1.00 40.95 ? 127  TYR A CG    1 
ATOM   1053 C  CD1   . TYR A 1 137 ? 10.416  -0.217  -6.080  1.00 40.49 ? 127  TYR A CD1   1 
ATOM   1054 C  CD2   . TYR A 1 137 ? 12.599  0.307   -6.913  1.00 41.76 ? 127  TYR A CD2   1 
ATOM   1055 C  CE1   . TYR A 1 137 ? 9.841   0.574   -7.061  1.00 40.70 ? 127  TYR A CE1   1 
ATOM   1056 C  CE2   . TYR A 1 137 ? 12.030  1.106   -7.905  1.00 41.65 ? 127  TYR A CE2   1 
ATOM   1057 C  CZ    . TYR A 1 137 ? 10.652  1.236   -7.969  1.00 42.02 ? 127  TYR A CZ    1 
ATOM   1058 O  OH    . TYR A 1 137 ? 10.064  2.014   -8.934  1.00 41.88 ? 127  TYR A OH    1 
ATOM   1059 N  N     . SER A 1 138 ? 11.572  -3.470  -7.209  1.00 44.13 ? 128  SER A N     1 
ATOM   1060 C  CA    . SER A 1 138 ? 11.903  -3.870  -8.577  1.00 46.84 ? 128  SER A CA    1 
ATOM   1061 C  C     . SER A 1 138 ? 11.649  -2.697  -9.530  1.00 47.91 ? 128  SER A C     1 
ATOM   1062 O  O     . SER A 1 138 ? 10.532  -2.185  -9.610  1.00 45.72 ? 128  SER A O     1 
ATOM   1063 C  CB    . SER A 1 138 ? 11.054  -5.070  -8.986  1.00 47.52 ? 128  SER A CB    1 
ATOM   1064 O  OG    . SER A 1 138 ? 11.312  -5.448  -10.325 1.00 48.89 ? 128  SER A OG    1 
ATOM   1065 N  N     . VAL A 1 139 ? 12.687  -2.296  -10.259 1.00 51.09 ? 129  VAL A N     1 
ATOM   1066 C  CA    . VAL A 1 139 ? 12.626  -1.138  -11.166 1.00 53.66 ? 129  VAL A CA    1 
ATOM   1067 C  C     . VAL A 1 139 ? 11.553  -1.282  -12.267 1.00 54.51 ? 129  VAL A C     1 
ATOM   1068 O  O     . VAL A 1 139 ? 10.672  -0.424  -12.356 1.00 54.51 ? 129  VAL A O     1 
ATOM   1069 C  CB    . VAL A 1 139 ? 14.016  -0.810  -11.778 1.00 55.30 ? 129  VAL A CB    1 
ATOM   1070 C  CG1   . VAL A 1 139 ? 13.921  0.305   -12.819 1.00 55.92 ? 129  VAL A CG1   1 
ATOM   1071 C  CG2   . VAL A 1 139 ? 14.995  -0.401  -10.684 1.00 55.85 ? 129  VAL A CG2   1 
ATOM   1072 N  N     . PRO A 1 140 ? 11.608  -2.360  -13.090 1.00 55.86 ? 130  PRO A N     1 
ATOM   1073 C  CA    . PRO A 1 140 ? 10.639  -2.478  -14.195 1.00 55.24 ? 130  PRO A CA    1 
ATOM   1074 C  C     . PRO A 1 140 ? 9.198   -2.732  -13.750 1.00 54.49 ? 130  PRO A C     1 
ATOM   1075 O  O     . PRO A 1 140 ? 8.263   -2.269  -14.408 1.00 54.59 ? 130  PRO A O     1 
ATOM   1076 C  CB    . PRO A 1 140 ? 11.165  -3.671  -14.997 1.00 56.63 ? 130  PRO A CB    1 
ATOM   1077 C  CG    . PRO A 1 140 ? 11.884  -4.501  -14.001 1.00 57.07 ? 130  PRO A CG    1 
ATOM   1078 C  CD    . PRO A 1 140 ? 12.509  -3.530  -13.043 1.00 56.87 ? 130  PRO A CD    1 
ATOM   1079 N  N     . ASP A 1 141 ? 9.028   -3.458  -12.646 1.00 53.03 ? 131  ASP A N     1 
ATOM   1080 C  CA    . ASP A 1 141 ? 7.700   -3.708  -12.071 1.00 51.68 ? 131  ASP A CA    1 
ATOM   1081 C  C     . ASP A 1 141 ? 7.096   -2.482  -11.368 1.00 50.16 ? 131  ASP A C     1 
ATOM   1082 O  O     . ASP A 1 141 ? 5.882   -2.422  -11.172 1.00 50.06 ? 131  ASP A O     1 
ATOM   1083 C  CB    . ASP A 1 141 ? 7.771   -4.872  -11.082 1.00 51.71 ? 131  ASP A CB    1 
ATOM   1084 C  CG    . ASP A 1 141 ? 8.205   -6.168  -11.737 1.00 53.03 ? 131  ASP A CG    1 
ATOM   1085 O  OD1   . ASP A 1 141 ? 7.455   -6.669  -12.600 1.00 54.16 ? 131  ASP A OD1   1 
ATOM   1086 O  OD2   . ASP A 1 141 ? 9.287   -6.685  -11.386 1.00 51.88 ? 131  ASP A OD2   1 
ATOM   1087 N  N     . GLU A 1 142 ? 7.945   -1.523  -10.986 1.00 49.37 ? 132  GLU A N     1 
ATOM   1088 C  CA    . GLU A 1 142 ? 7.553   -0.355  -10.181 1.00 48.53 ? 132  GLU A CA    1 
ATOM   1089 C  C     . GLU A 1 142 ? 6.732   -0.783  -8.967  1.00 46.77 ? 132  GLU A C     1 
ATOM   1090 O  O     . GLU A 1 142 ? 5.694   -0.189  -8.652  1.00 45.43 ? 132  GLU A O     1 
ATOM   1091 C  CB    . GLU A 1 142 ? 6.801   0.676   -11.030 1.00 49.71 ? 132  GLU A CB    1 
ATOM   1092 C  CG    . GLU A 1 142 ? 7.673   1.361   -12.073 1.00 51.33 ? 132  GLU A CG    1 
ATOM   1093 C  CD    . GLU A 1 142 ? 7.026   2.606   -12.665 1.00 52.52 ? 132  GLU A CD    1 
ATOM   1094 O  OE1   . GLU A 1 142 ? 5.774   2.694   -12.673 1.00 52.32 ? 132  GLU A OE1   1 
ATOM   1095 O  OE2   . GLU A 1 142 ? 7.772   3.499   -13.126 1.00 52.57 ? 132  GLU A OE2   1 
ATOM   1096 N  N     . THR A 1 143 ? 7.211   -1.841  -8.316  1.00 45.11 ? 133  THR A N     1 
ATOM   1097 C  CA    . THR A 1 143 ? 6.515   -2.483  -7.209  1.00 44.25 ? 133  THR A CA    1 
ATOM   1098 C  C     . THR A 1 143 ? 7.511   -2.780  -6.091  1.00 41.93 ? 133  THR A C     1 
ATOM   1099 O  O     . THR A 1 143 ? 8.686   -3.085  -6.342  1.00 39.69 ? 133  THR A O     1 
ATOM   1100 C  CB    . THR A 1 143 ? 5.827   -3.797  -7.654  1.00 45.12 ? 133  THR A CB    1 
ATOM   1101 O  OG1   . THR A 1 143 ? 5.031   -3.551  -8.818  1.00 44.95 ? 133  THR A OG1   1 
ATOM   1102 C  CG2   . THR A 1 143 ? 4.920   -4.361  -6.552  1.00 45.31 ? 133  THR A CG2   1 
ATOM   1103 N  N     . TYR A 1 144 ? 7.020   -2.654  -4.862  1.00 40.20 ? 134  TYR A N     1 
ATOM   1104 C  CA    . TYR A 1 144 ? 7.729   -3.078  -3.666  1.00 40.48 ? 134  TYR A CA    1 
ATOM   1105 C  C     . TYR A 1 144 ? 7.137   -4.406  -3.195  1.00 41.06 ? 134  TYR A C     1 
ATOM   1106 O  O     . TYR A 1 144 ? 5.927   -4.515  -3.004  1.00 40.95 ? 134  TYR A O     1 
ATOM   1107 C  CB    . TYR A 1 144 ? 7.579   -2.041  -2.559  1.00 39.89 ? 134  TYR A CB    1 
ATOM   1108 C  CG    . TYR A 1 144 ? 8.166   -0.690  -2.896  1.00 39.57 ? 134  TYR A CG    1 
ATOM   1109 C  CD1   . TYR A 1 144 ? 9.430   -0.316  -2.431  1.00 39.56 ? 134  TYR A CD1   1 
ATOM   1110 C  CD2   . TYR A 1 144 ? 7.457   0.223   -3.682  1.00 39.40 ? 134  TYR A CD2   1 
ATOM   1111 C  CE1   . TYR A 1 144 ? 9.967   0.932   -2.742  1.00 40.20 ? 134  TYR A CE1   1 
ATOM   1112 C  CE2   . TYR A 1 144 ? 7.988   1.469   -3.992  1.00 39.85 ? 134  TYR A CE2   1 
ATOM   1113 C  CZ    . TYR A 1 144 ? 9.244   1.820   -3.519  1.00 40.18 ? 134  TYR A CZ    1 
ATOM   1114 O  OH    . TYR A 1 144 ? 9.792   3.053   -3.819  1.00 40.60 ? 134  TYR A OH    1 
ATOM   1115 N  N     . TYR A 1 145 ? 7.996   -5.403  -3.019  1.00 42.27 ? 135  TYR A N     1 
ATOM   1116 C  CA    . TYR A 1 145 ? 7.587   -6.736  -2.563  1.00 43.44 ? 135  TYR A CA    1 
ATOM   1117 C  C     . TYR A 1 145 ? 8.039   -6.986  -1.132  1.00 44.03 ? 135  TYR A C     1 
ATOM   1118 O  O     . TYR A 1 145 ? 9.013   -6.394  -0.662  1.00 42.48 ? 135  TYR A O     1 
ATOM   1119 C  CB    . TYR A 1 145 ? 8.196   -7.812  -3.466  1.00 44.40 ? 135  TYR A CB    1 
ATOM   1120 C  CG    . TYR A 1 145 ? 7.791   -7.688  -4.913  1.00 44.48 ? 135  TYR A CG    1 
ATOM   1121 C  CD1   . TYR A 1 145 ? 8.626   -7.066  -5.839  1.00 45.17 ? 135  TYR A CD1   1 
ATOM   1122 C  CD2   . TYR A 1 145 ? 6.567   -8.186  -5.358  1.00 45.17 ? 135  TYR A CD2   1 
ATOM   1123 C  CE1   . TYR A 1 145 ? 8.256   -6.947  -7.171  1.00 45.82 ? 135  TYR A CE1   1 
ATOM   1124 C  CE2   . TYR A 1 145 ? 6.182   -8.072  -6.685  1.00 45.74 ? 135  TYR A CE2   1 
ATOM   1125 C  CZ    . TYR A 1 145 ? 7.030   -7.453  -7.589  1.00 46.12 ? 135  TYR A CZ    1 
ATOM   1126 O  OH    . TYR A 1 145 ? 6.654   -7.334  -8.905  1.00 46.89 ? 135  TYR A OH    1 
ATOM   1127 N  N     . THR A 1 146 ? 7.327   -7.881  -0.452  1.00 45.04 ? 136  THR A N     1 
ATOM   1128 C  CA    . THR A 1 146 ? 7.777   -8.422  0.829   1.00 46.70 ? 136  THR A CA    1 
ATOM   1129 C  C     . THR A 1 146 ? 8.811   -9.506  0.543   1.00 48.95 ? 136  THR A C     1 
ATOM   1130 O  O     . THR A 1 146 ? 8.896   -10.014 -0.580  1.00 49.45 ? 136  THR A O     1 
ATOM   1131 C  CB    . THR A 1 146 ? 6.623   -9.023  1.662   1.00 46.60 ? 136  THR A CB    1 
ATOM   1132 O  OG1   . THR A 1 146 ? 6.067   -10.162 0.987   1.00 46.44 ? 136  THR A OG1   1 
ATOM   1133 C  CG2   . THR A 1 146 ? 5.530   -7.986  1.905   1.00 45.83 ? 136  THR A CG2   1 
ATOM   1134 N  N     . GLU A 1 147 ? 9.592   -9.853  1.559   1.00 51.91 ? 137  GLU A N     1 
ATOM   1135 C  CA    . GLU A 1 147 ? 10.635  -10.880 1.422   1.00 54.43 ? 137  GLU A CA    1 
ATOM   1136 C  C     . GLU A 1 147 ? 10.081  -12.268 1.054   1.00 55.34 ? 137  GLU A C     1 
ATOM   1137 O  O     . GLU A 1 147 ? 10.716  -13.008 0.302   1.00 54.81 ? 137  GLU A O     1 
ATOM   1138 C  CB    . GLU A 1 147 ? 11.516  -10.949 2.677   1.00 56.22 ? 137  GLU A CB    1 
ATOM   1139 C  CG    . GLU A 1 147 ? 10.827  -11.413 3.955   1.00 57.73 ? 137  GLU A CG    1 
ATOM   1140 C  CD    . GLU A 1 147 ? 11.779  -11.472 5.138   1.00 59.31 ? 137  GLU A CD    1 
ATOM   1141 O  OE1   . GLU A 1 147 ? 12.710  -10.642 5.218   1.00 60.39 ? 137  GLU A OE1   1 
ATOM   1142 O  OE2   . GLU A 1 147 ? 11.597  -12.357 5.993   1.00 60.76 ? 137  GLU A OE2   1 
ATOM   1143 N  N     . SER A 1 148 ? 8.891   -12.594 1.563   1.00 57.48 ? 138  SER A N     1 
ATOM   1144 C  CA    . SER A 1 148 ? 8.225   -13.882 1.274   1.00 58.94 ? 138  SER A CA    1 
ATOM   1145 C  C     . SER A 1 148 ? 7.722   -14.020 -0.172  1.00 59.69 ? 138  SER A C     1 
ATOM   1146 O  O     . SER A 1 148 ? 7.499   -15.133 -0.644  1.00 59.94 ? 138  SER A O     1 
ATOM   1147 C  CB    . SER A 1 148 ? 7.062   -14.126 2.249   1.00 58.74 ? 138  SER A CB    1 
ATOM   1148 O  OG    . SER A 1 148 ? 6.026   -13.173 2.081   1.00 58.48 ? 138  SER A OG    1 
ATOM   1149 N  N     . GLN A 1 149 ? 7.528   -12.895 -0.856  1.00 60.10 ? 139  GLN A N     1 
ATOM   1150 C  CA    . GLN A 1 149 ? 7.136   -12.885 -2.270  1.00 60.98 ? 139  GLN A CA    1 
ATOM   1151 C  C     . GLN A 1 149 ? 8.287   -13.122 -3.261  1.00 62.47 ? 139  GLN A C     1 
ATOM   1152 O  O     . GLN A 1 149 ? 8.036   -13.428 -4.430  1.00 63.17 ? 139  GLN A O     1 
ATOM   1153 C  CB    . GLN A 1 149 ? 6.448   -11.566 -2.604  1.00 59.72 ? 139  GLN A CB    1 
ATOM   1154 C  CG    . GLN A 1 149 ? 5.083   -11.404 -1.959  1.00 59.20 ? 139  GLN A CG    1 
ATOM   1155 C  CD    . GLN A 1 149 ? 4.482   -10.034 -2.209  1.00 58.57 ? 139  GLN A CD    1 
ATOM   1156 O  OE1   . GLN A 1 149 ? 5.172   -9.013  -2.141  1.00 57.61 ? 139  GLN A OE1   1 
ATOM   1157 N  NE2   . GLN A 1 149 ? 3.189   -10.005 -2.505  1.00 58.47 ? 139  GLN A NE2   1 
ATOM   1158 N  N     . LEU A 1 150 ? 9.482   -12.942 -2.763  1.00 64.20 ? 140  LEU A N     1 
ATOM   1159 C  CA    . LEU A 1 150 ? 10.622  -13.077 -3.600  1.00 66.37 ? 140  LEU A CA    1 
ATOM   1160 C  C     . LEU A 1 150 ? 10.830  -14.500 -4.001  1.00 69.43 ? 140  LEU A C     1 
ATOM   1161 O  O     . LEU A 1 150 ? 10.657  -15.417 -3.217  1.00 68.54 ? 140  LEU A O     1 
ATOM   1162 C  CB    . LEU A 1 150 ? 11.863  -12.587 -2.901  1.00 65.90 ? 140  LEU A CB    1 
ATOM   1163 C  CG    . LEU A 1 150 ? 11.917  -11.117 -2.497  1.00 64.88 ? 140  LEU A CG    1 
ATOM   1164 C  CD1   . LEU A 1 150 ? 13.294  -10.811 -1.982  1.00 64.85 ? 140  LEU A CD1   1 
ATOM   1165 C  CD2   . LEU A 1 150 ? 11.538  -10.234 -3.656  1.00 63.70 ? 140  LEU A CD2   1 
ATOM   1166 N  N     . VAL A 1 151 ? 11.218  -14.619 -5.249  1.00 73.01 ? 141  VAL A N     1 
ATOM   1167 C  CA    . VAL A 1 151 ? 11.549  -15.857 -5.927  1.00 76.82 ? 141  VAL A CA    1 
ATOM   1168 C  C     . VAL A 1 151 ? 13.058  -15.937 -5.894  1.00 78.73 ? 141  VAL A C     1 
ATOM   1169 O  O     . VAL A 1 151 ? 13.712  -14.921 -5.957  1.00 80.11 ? 141  VAL A O     1 
ATOM   1170 C  CB    . VAL A 1 151 ? 11.028  -15.769 -7.364  1.00 78.33 ? 141  VAL A CB    1 
ATOM   1171 N  N     . ASP A 1 152 ? 13.614  -17.137 -5.750  1.00 79.92 ? 142  ASP A N     1 
ATOM   1172 C  CA    . ASP A 1 152 ? 15.075  -17.339 -5.692  1.00 80.52 ? 142  ASP A CA    1 
ATOM   1173 C  C     . ASP A 1 152 ? 15.767  -16.552 -4.583  1.00 79.91 ? 142  ASP A C     1 
ATOM   1174 O  O     . ASP A 1 152 ? 16.783  -15.927 -4.805  1.00 78.55 ? 142  ASP A O     1 
ATOM   1175 C  CB    . ASP A 1 152 ? 15.770  -17.105 -7.049  1.00 80.70 ? 142  ASP A CB    1 
ATOM   1176 C  CG    . ASP A 1 152 ? 15.453  -18.180 -8.066  1.00 81.46 ? 142  ASP A CG    1 
ATOM   1177 O  OD1   . ASP A 1 152 ? 14.567  -19.023 -7.809  1.00 80.99 ? 142  ASP A OD1   1 
ATOM   1178 O  OD2   . ASP A 1 152 ? 16.113  -18.177 -9.124  1.00 80.99 ? 142  ASP A OD2   1 
ATOM   1179 N  N     . PRO A 1 153 ? 15.227  -16.630 -3.378  1.00 80.29 ? 143  PRO A N     1 
ATOM   1180 C  CA    . PRO A 1 153 ? 15.742  -15.895 -2.238  1.00 80.61 ? 143  PRO A CA    1 
ATOM   1181 C  C     . PRO A 1 153 ? 17.143  -16.262 -1.874  1.00 81.67 ? 143  PRO A C     1 
ATOM   1182 O  O     . PRO A 1 153 ? 17.451  -17.437 -1.801  1.00 82.15 ? 143  PRO A O     1 
ATOM   1183 C  CB    . PRO A 1 153 ? 14.798  -16.288 -1.108  1.00 80.51 ? 143  PRO A CB    1 
ATOM   1184 C  CG    . PRO A 1 153 ? 14.163  -17.550 -1.546  1.00 80.77 ? 143  PRO A CG    1 
ATOM   1185 C  CD    . PRO A 1 153 ? 14.064  -17.450 -3.023  1.00 80.85 ? 143  PRO A CD    1 
ATOM   1186 N  N     . GLN A 1 154 ? 17.985  -15.257 -1.726  1.00 81.45 ? 144  GLN A N     1 
ATOM   1187 C  CA    . GLN A 1 154 ? 19.372  -15.407 -1.293  1.00 82.05 ? 144  GLN A CA    1 
ATOM   1188 C  C     . GLN A 1 154 ? 19.427  -15.186 0.215   1.00 81.92 ? 144  GLN A C     1 
ATOM   1189 O  O     . GLN A 1 154 ? 18.871  -14.205 0.719   1.00 82.36 ? 144  GLN A O     1 
ATOM   1190 C  CB    . GLN A 1 154 ? 20.271  -14.387 -2.001  1.00 81.65 ? 144  GLN A CB    1 
ATOM   1191 C  CG    . GLN A 1 154 ? 20.162  -14.384 -3.519  1.00 81.66 ? 144  GLN A CG    1 
ATOM   1192 C  CD    . GLN A 1 154 ? 20.612  -15.691 -4.136  1.00 82.79 ? 144  GLN A CD    1 
ATOM   1193 O  OE1   . GLN A 1 154 ? 21.740  -16.131 -3.920  1.00 82.58 ? 144  GLN A OE1   1 
ATOM   1194 N  NE2   . GLN A 1 154 ? 19.733  -16.317 -4.912  1.00 82.86 ? 144  GLN A NE2   1 
ATOM   1195 N  N     . TYR A 1 155 ? 20.101  -16.090 0.924   1.00 81.08 ? 145  TYR A N     1 
ATOM   1196 C  CA    . TYR A 1 155 ? 20.161  -16.061 2.391   1.00 80.96 ? 145  TYR A CA    1 
ATOM   1197 C  C     . TYR A 1 155 ? 21.565  -15.758 2.920   1.00 83.01 ? 145  TYR A C     1 
ATOM   1198 O  O     . TYR A 1 155 ? 22.565  -15.950 2.227   1.00 82.37 ? 145  TYR A O     1 
ATOM   1199 C  CB    . TYR A 1 155 ? 19.662  -17.389 2.974   1.00 79.33 ? 145  TYR A CB    1 
ATOM   1200 C  CG    . TYR A 1 155 ? 18.157  -17.524 3.002   1.00 76.65 ? 145  TYR A CG    1 
ATOM   1201 C  CD1   . TYR A 1 155 ? 17.450  -17.899 1.862   1.00 75.31 ? 145  TYR A CD1   1 
ATOM   1202 C  CD2   . TYR A 1 155 ? 17.437  -17.282 4.172   1.00 75.58 ? 145  TYR A CD2   1 
ATOM   1203 C  CE1   . TYR A 1 155 ? 16.067  -18.030 1.885   1.00 74.51 ? 145  TYR A CE1   1 
ATOM   1204 C  CE2   . TYR A 1 155 ? 16.054  -17.408 4.206   1.00 75.01 ? 145  TYR A CE2   1 
ATOM   1205 C  CZ    . TYR A 1 155 ? 15.373  -17.783 3.060   1.00 74.13 ? 145  TYR A CZ    1 
ATOM   1206 O  OH    . TYR A 1 155 ? 14.004  -17.905 3.091   1.00 72.43 ? 145  TYR A OH    1 
ATOM   1207 N  N     . GLU A 1 156 ? 21.608  -15.267 4.156   1.00 85.52 ? 146  GLU A N     1 
ATOM   1208 C  CA    . GLU A 1 156 ? 22.859  -15.061 4.890   1.00 87.90 ? 146  GLU A CA    1 
ATOM   1209 C  C     . GLU A 1 156 ? 22.568  -15.035 6.389   1.00 87.74 ? 146  GLU A C     1 
ATOM   1210 O  O     . GLU A 1 156 ? 21.812  -14.185 6.860   1.00 87.34 ? 146  GLU A O     1 
ATOM   1211 C  CB    . GLU A 1 156 ? 23.536  -13.757 4.469   1.00 88.93 ? 146  GLU A CB    1 
ATOM   1212 C  CG    . GLU A 1 156 ? 24.917  -13.544 5.076   1.00 90.35 ? 146  GLU A CG    1 
ATOM   1213 C  CD    . GLU A 1 156 ? 25.632  -12.326 4.524   1.00 91.25 ? 146  GLU A CD    1 
ATOM   1214 O  OE1   . GLU A 1 156 ? 26.871  -12.262 4.665   1.00 92.72 ? 146  GLU A OE1   1 
ATOM   1215 O  OE2   . GLU A 1 156 ? 24.971  -11.432 3.953   1.00 91.75 ? 146  GLU A OE2   1 
ATOM   1216 N  N     . ASN A 1 157 ? 23.168  -15.975 7.119   1.00 87.93 ? 147  ASN A N     1 
ATOM   1217 C  CA    . ASN A 1 157 ? 22.961  -16.130 8.567   1.00 88.01 ? 147  ASN A CA    1 
ATOM   1218 C  C     . ASN A 1 157 ? 21.480  -16.324 8.959   1.00 87.68 ? 147  ASN A C     1 
ATOM   1219 O  O     . ASN A 1 157 ? 21.043  -15.864 10.017  1.00 87.97 ? 147  ASN A O     1 
ATOM   1220 C  CB    . ASN A 1 157 ? 23.573  -14.942 9.323   1.00 87.12 ? 147  ASN A CB    1 
ATOM   1221 N  N     . GLY A 1 158 ? 20.730  -17.022 8.104   1.00 86.80 ? 148  GLY A N     1 
ATOM   1222 C  CA    . GLY A 1 158 ? 19.303  -17.288 8.325   1.00 85.81 ? 148  GLY A CA    1 
ATOM   1223 C  C     . GLY A 1 158 ? 18.412  -16.067 8.180   1.00 84.49 ? 148  GLY A C     1 
ATOM   1224 O  O     . GLY A 1 158 ? 17.516  -15.849 8.999   1.00 85.75 ? 148  GLY A O     1 
ATOM   1225 N  N     . LYS A 1 159 ? 18.655  -15.281 7.131   1.00 81.13 ? 149  LYS A N     1 
ATOM   1226 C  CA    . LYS A 1 159 ? 17.903  -14.048 6.868   1.00 77.74 ? 149  LYS A CA    1 
ATOM   1227 C  C     . LYS A 1 159 ? 18.002  -13.677 5.389   1.00 74.93 ? 149  LYS A C     1 
ATOM   1228 O  O     . LYS A 1 159 ? 19.091  -13.714 4.810   1.00 73.91 ? 149  LYS A O     1 
ATOM   1229 C  CB    . LYS A 1 159 ? 18.434  -12.901 7.732   1.00 76.81 ? 149  LYS A CB    1 
ATOM   1230 N  N     . ILE A 1 160 ? 16.868  -13.308 4.793   1.00 71.64 ? 150  ILE A N     1 
ATOM   1231 C  CA    . ILE A 1 160 ? 16.795  -13.015 3.356   1.00 69.34 ? 150  ILE A CA    1 
ATOM   1232 C  C     . ILE A 1 160 ? 17.514  -11.689 3.083   1.00 66.98 ? 150  ILE A C     1 
ATOM   1233 O  O     . ILE A 1 160 ? 17.200  -10.672 3.697   1.00 65.64 ? 150  ILE A O     1 
ATOM   1234 C  CB    . ILE A 1 160 ? 15.333  -12.972 2.838   1.00 69.00 ? 150  ILE A CB    1 
ATOM   1235 C  CG1   . ILE A 1 160 ? 14.650  -14.333 3.046   1.00 69.53 ? 150  ILE A CG1   1 
ATOM   1236 C  CG2   . ILE A 1 160 ? 15.285  -12.610 1.353   1.00 68.54 ? 150  ILE A CG2   1 
ATOM   1237 C  CD1   . ILE A 1 160 ? 13.138  -14.302 2.974   1.00 69.01 ? 150  ILE A CD1   1 
ATOM   1238 N  N     . ILE A 1 161 ? 18.486  -11.734 2.173   1.00 65.87 ? 151  ILE A N     1 
ATOM   1239 C  CA    . ILE A 1 161 ? 19.347  -10.586 1.818   1.00 65.84 ? 151  ILE A CA    1 
ATOM   1240 C  C     . ILE A 1 161 ? 19.138  -10.101 0.367   1.00 64.61 ? 151  ILE A C     1 
ATOM   1241 O  O     . ILE A 1 161 ? 19.597  -9.018  -0.012  1.00 62.54 ? 151  ILE A O     1 
ATOM   1242 C  CB    . ILE A 1 161 ? 20.830  -10.966 2.104   1.00 67.08 ? 151  ILE A CB    1 
ATOM   1243 C  CG1   . ILE A 1 161 ? 21.082  -10.951 3.624   1.00 67.58 ? 151  ILE A CG1   1 
ATOM   1244 C  CG2   . ILE A 1 161 ? 21.845  -10.085 1.366   1.00 67.79 ? 151  ILE A CG2   1 
ATOM   1245 C  CD1   . ILE A 1 161 ? 21.566  -9.637  4.215   1.00 67.38 ? 151  ILE A CD1   1 
ATOM   1246 N  N     . GLY A 1 162 ? 18.419  -10.882 -0.431  1.00 64.23 ? 152  GLY A N     1 
ATOM   1247 C  CA    . GLY A 1 162 ? 18.225  -10.568 -1.837  1.00 64.11 ? 152  GLY A CA    1 
ATOM   1248 C  C     . GLY A 1 162 ? 17.246  -11.512 -2.493  1.00 63.85 ? 152  GLY A C     1 
ATOM   1249 O  O     . GLY A 1 162 ? 16.741  -12.450 -1.864  1.00 63.22 ? 152  GLY A O     1 
ATOM   1250 N  N     . GLY A 1 163 ? 16.969  -11.249 -3.764  1.00 62.65 ? 153  GLY A N     1 
ATOM   1251 C  CA    . GLY A 1 163 ? 16.067  -12.088 -4.538  1.00 62.33 ? 153  GLY A CA    1 
ATOM   1252 C  C     . GLY A 1 163 ? 15.711  -11.513 -5.889  1.00 61.77 ? 153  GLY A C     1 
ATOM   1253 O  O     . GLY A 1 163 ? 16.381  -10.612 -6.398  1.00 61.14 ? 153  GLY A O     1 
ATOM   1254 N  N     . LYS A 1 164 ? 14.643  -12.057 -6.464  1.00 61.62 ? 154  LYS A N     1 
ATOM   1255 C  CA    . LYS A 1 164 ? 14.133  -11.636 -7.767  1.00 61.40 ? 154  LYS A CA    1 
ATOM   1256 C  C     . LYS A 1 164 ? 12.623  -11.451 -7.689  1.00 60.77 ? 154  LYS A C     1 
ATOM   1257 O  O     . LYS A 1 164 ? 11.956  -12.034 -6.831  1.00 60.17 ? 154  LYS A O     1 
ATOM   1258 C  CB    . LYS A 1 164 ? 14.493  -12.662 -8.847  1.00 61.71 ? 154  LYS A CB    1 
ATOM   1259 N  N     . SER A 1 165 ? 12.092  -10.628 -8.586  1.00 61.00 ? 155  SER A N     1 
ATOM   1260 C  CA    . SER A 1 165 ? 10.658  -10.337 -8.623  1.00 61.83 ? 155  SER A CA    1 
ATOM   1261 C  C     . SER A 1 165 ? 9.856   -11.566 -9.082  1.00 63.25 ? 155  SER A C     1 
ATOM   1262 O  O     . SER A 1 165 ? 10.245  -12.216 -10.047 1.00 63.56 ? 155  SER A O     1 
ATOM   1263 C  CB    . SER A 1 165 ? 10.396  -9.147  -9.553  1.00 61.04 ? 155  SER A CB    1 
ATOM   1264 O  OG    . SER A 1 165 ? 9.020   -9.014  -9.865  1.00 59.85 ? 155  SER A OG    1 
ATOM   1265 N  N     . PRO A 1 166 ? 8.733   -11.886 -8.400  1.00 65.05 ? 156  PRO A N     1 
ATOM   1266 C  CA    . PRO A 1 166 ? 7.911   -13.016 -8.853  1.00 66.45 ? 156  PRO A CA    1 
ATOM   1267 C  C     . PRO A 1 166 ? 7.169   -12.756 -10.173 1.00 67.91 ? 156  PRO A C     1 
ATOM   1268 O  O     . PRO A 1 166 ? 6.818   -13.708 -10.872 1.00 68.57 ? 156  PRO A O     1 
ATOM   1269 C  CB    . PRO A 1 166 ? 6.914   -13.204 -7.705  1.00 66.17 ? 156  PRO A CB    1 
ATOM   1270 C  CG    . PRO A 1 166 ? 6.773   -11.849 -7.113  1.00 65.37 ? 156  PRO A CG    1 
ATOM   1271 C  CD    . PRO A 1 166 ? 8.133   -11.217 -7.230  1.00 65.16 ? 156  PRO A CD    1 
ATOM   1272 N  N     . ASP A 1 167 ? 6.934   -11.484 -10.497 1.00 69.00 ? 157  ASP A N     1 
ATOM   1273 C  CA    . ASP A 1 167 ? 6.230   -11.094 -11.721 1.00 69.20 ? 157  ASP A CA    1 
ATOM   1274 C  C     . ASP A 1 167 ? 7.137   -11.115 -12.950 1.00 69.89 ? 157  ASP A C     1 
ATOM   1275 O  O     . ASP A 1 167 ? 6.868   -11.849 -13.899 1.00 72.23 ? 157  ASP A O     1 
ATOM   1276 C  CB    . ASP A 1 167 ? 5.602   -9.710  -11.547 1.00 68.80 ? 157  ASP A CB    1 
ATOM   1277 C  CG    . ASP A 1 167 ? 4.516   -9.693  -10.478 1.00 68.78 ? 157  ASP A CG    1 
ATOM   1278 O  OD1   . ASP A 1 167 ? 4.604   -8.863  -9.548  1.00 68.03 ? 157  ASP A OD1   1 
ATOM   1279 O  OD2   . ASP A 1 167 ? 3.578   -10.516 -10.558 1.00 68.55 ? 157  ASP A OD2   1 
ATOM   1280 N  N     . SER A 1 168 ? 8.200   -10.312 -12.924 1.00 69.35 ? 158  SER A N     1 
ATOM   1281 C  CA    . SER A 1 168 ? 9.120   -10.165 -14.073 1.00 69.62 ? 158  SER A CA    1 
ATOM   1282 C  C     . SER A 1 168 ? 10.403  -10.999 -13.984 1.00 70.62 ? 158  SER A C     1 
ATOM   1283 O  O     . SER A 1 168 ? 10.942  -11.417 -15.011 1.00 72.60 ? 158  SER A O     1 
ATOM   1284 C  CB    . SER A 1 168 ? 9.513   -8.699  -14.252 1.00 69.15 ? 158  SER A CB    1 
ATOM   1285 O  OG    . SER A 1 168 ? 10.378  -8.270  -13.212 1.00 68.62 ? 158  SER A OG    1 
ATOM   1286 N  N     . GLY A 1 169 ? 10.899  -11.211 -12.768 1.00 70.40 ? 159  GLY A N     1 
ATOM   1287 C  CA    . GLY A 1 169 ? 12.187  -11.877 -12.537 1.00 70.44 ? 159  GLY A CA    1 
ATOM   1288 C  C     . GLY A 1 169 ? 13.380  -10.940 -12.422 1.00 69.87 ? 159  GLY A C     1 
ATOM   1289 O  O     . GLY A 1 169 ? 14.520  -11.399 -12.398 1.00 70.17 ? 159  GLY A O     1 
ATOM   1290 N  N     . HIS A 1 170 ? 13.126  -9.634  -12.342 1.00 69.28 ? 160  HIS A N     1 
ATOM   1291 C  CA    . HIS A 1 170 ? 14.195  -8.635  -12.205 1.00 68.47 ? 160  HIS A CA    1 
ATOM   1292 C  C     . HIS A 1 170 ? 14.763  -8.630  -10.777 1.00 66.48 ? 160  HIS A C     1 
ATOM   1293 O  O     . HIS A 1 170 ? 14.048  -8.910  -9.809  1.00 63.83 ? 160  HIS A O     1 
ATOM   1294 C  CB    . HIS A 1 170 ? 13.676  -7.241  -12.580 1.00 69.68 ? 160  HIS A CB    1 
ATOM   1295 C  CG    . HIS A 1 170 ? 14.755  -6.215  -12.780 1.00 71.48 ? 160  HIS A CG    1 
ATOM   1296 N  ND1   . HIS A 1 170 ? 15.428  -6.062  -13.974 1.00 72.56 ? 160  HIS A ND1   1 
ATOM   1297 C  CD2   . HIS A 1 170 ? 15.260  -5.275  -11.943 1.00 71.78 ? 160  HIS A CD2   1 
ATOM   1298 C  CE1   . HIS A 1 170 ? 16.306  -5.081  -13.862 1.00 72.11 ? 160  HIS A CE1   1 
ATOM   1299 N  NE2   . HIS A 1 170 ? 16.223  -4.586  -12.640 1.00 71.93 ? 160  HIS A NE2   1 
ATOM   1300 N  N     . GLU A 1 171 ? 16.051  -8.305  -10.669 1.00 64.72 ? 161  GLU A N     1 
ATOM   1301 C  CA    . GLU A 1 171 ? 16.767  -8.276  -9.391  1.00 64.26 ? 161  GLU A CA    1 
ATOM   1302 C  C     . GLU A 1 171 ? 16.233  -7.138  -8.515  1.00 62.12 ? 161  GLU A C     1 
ATOM   1303 O  O     . GLU A 1 171 ? 16.318  -5.971  -8.899  1.00 62.03 ? 161  GLU A O     1 
ATOM   1304 C  CB    . GLU A 1 171 ? 18.274  -8.090  -9.642  1.00 65.87 ? 161  GLU A CB    1 
ATOM   1305 C  CG    . GLU A 1 171 ? 19.176  -8.122  -8.404  1.00 66.93 ? 161  GLU A CG    1 
ATOM   1306 C  CD    . GLU A 1 171 ? 19.405  -9.511  -7.816  1.00 68.12 ? 161  GLU A CD    1 
ATOM   1307 O  OE1   . GLU A 1 171 ? 20.121  -9.596  -6.794  1.00 68.03 ? 161  GLU A OE1   1 
ATOM   1308 O  OE2   . GLU A 1 171 ? 18.887  -10.516 -8.353  1.00 69.06 ? 161  GLU A OE2   1 
ATOM   1309 N  N     . VAL A 1 172 ? 15.679  -7.486  -7.352  1.00 58.85 ? 162  VAL A N     1 
ATOM   1310 C  CA    . VAL A 1 172 ? 15.163  -6.479  -6.406  1.00 55.46 ? 162  VAL A CA    1 
ATOM   1311 C  C     . VAL A 1 172 ? 16.274  -5.813  -5.600  1.00 52.48 ? 162  VAL A C     1 
ATOM   1312 O  O     . VAL A 1 172 ? 17.373  -6.354  -5.473  1.00 51.85 ? 162  VAL A O     1 
ATOM   1313 C  CB    . VAL A 1 172 ? 14.106  -7.042  -5.422  1.00 55.62 ? 162  VAL A CB    1 
ATOM   1314 C  CG1   . VAL A 1 172 ? 12.911  -7.590  -6.185  1.00 55.67 ? 162  VAL A CG1   1 
ATOM   1315 C  CG2   . VAL A 1 172 ? 14.692  -8.094  -4.478  1.00 55.74 ? 162  VAL A CG2   1 
ATOM   1316 N  N     . GLU A 1 173 ? 15.953  -4.650  -5.039  1.00 48.36 ? 163  GLU A N     1 
ATOM   1317 C  CA    . GLU A 1 173 ? 16.878  -3.898  -4.186  1.00 45.44 ? 163  GLU A CA    1 
ATOM   1318 C  C     . GLU A 1 173 ? 16.209  -3.534  -2.860  1.00 45.38 ? 163  GLU A C     1 
ATOM   1319 O  O     . GLU A 1 173 ? 15.044  -3.121  -2.827  1.00 44.38 ? 163  GLU A O     1 
ATOM   1320 C  CB    . GLU A 1 173 ? 17.390  -2.642  -4.899  1.00 42.13 ? 163  GLU A CB    1 
ATOM   1321 C  CG    . GLU A 1 173 ? 16.345  -1.561  -5.153  1.00 40.88 ? 163  GLU A CG    1 
ATOM   1322 C  CD    . GLU A 1 173 ? 16.845  -0.479  -6.098  1.00 40.87 ? 163  GLU A CD    1 
ATOM   1323 O  OE1   . GLU A 1 173 ? 17.944  0.071   -5.854  1.00 41.51 ? 163  GLU A OE1   1 
ATOM   1324 O  OE2   . GLU A 1 173 ? 16.134  -0.181  -7.096  1.00 40.92 ? 163  GLU A OE2   1 
ATOM   1325 N  N     . LEU A 1 174 ? 16.961  -3.687  -1.778  1.00 44.78 ? 164  LEU A N     1 
ATOM   1326 C  CA    . LEU A 1 174 ? 16.457  -3.458  -0.437  1.00 44.65 ? 164  LEU A CA    1 
ATOM   1327 C  C     . LEU A 1 174 ? 16.288  -1.965  -0.193  1.00 42.63 ? 164  LEU A C     1 
ATOM   1328 O  O     . LEU A 1 174 ? 17.210  -1.194  -0.427  1.00 40.65 ? 164  LEU A O     1 
ATOM   1329 C  CB    . LEU A 1 174 ? 17.435  -4.031  0.582   1.00 46.08 ? 164  LEU A CB    1 
ATOM   1330 C  CG    . LEU A 1 174 ? 17.133  -3.858  2.071   1.00 47.09 ? 164  LEU A CG    1 
ATOM   1331 C  CD1   . LEU A 1 174 ? 15.736  -4.332  2.448   1.00 47.13 ? 164  LEU A CD1   1 
ATOM   1332 C  CD2   . LEU A 1 174 ? 18.185  -4.605  2.874   1.00 48.14 ? 164  LEU A CD2   1 
ATOM   1333 N  N     . VAL A 1 175 ? 15.109  -1.574  0.280   1.00 40.12 ? 165  VAL A N     1 
ATOM   1334 C  CA    . VAL A 1 175 ? 14.837  -0.176  0.625   1.00 39.21 ? 165  VAL A CA    1 
ATOM   1335 C  C     . VAL A 1 175 ? 14.354  -0.097  2.072   1.00 37.15 ? 165  VAL A C     1 
ATOM   1336 O  O     . VAL A 1 175 ? 13.510  -0.878  2.490   1.00 35.92 ? 165  VAL A O     1 
ATOM   1337 C  CB    . VAL A 1 175 ? 13.831  0.482   -0.345  1.00 40.26 ? 165  VAL A CB    1 
ATOM   1338 C  CG1   . VAL A 1 175 ? 14.448  0.612   -1.737  1.00 41.08 ? 165  VAL A CG1   1 
ATOM   1339 C  CG2   . VAL A 1 175 ? 12.536  -0.304  -0.432  1.00 40.98 ? 165  VAL A CG2   1 
ATOM   1340 N  N     . LYS A 1 176 ? 14.942  0.822   2.829   1.00 35.90 ? 166  LYS A N     1 
ATOM   1341 C  CA    . LYS A 1 176 ? 14.570  1.073   4.218   1.00 35.57 ? 166  LYS A CA    1 
ATOM   1342 C  C     . LYS A 1 176 ? 14.387  2.565   4.407   1.00 33.70 ? 166  LYS A C     1 
ATOM   1343 O  O     . LYS A 1 176 ? 15.174  3.355   3.895   1.00 32.70 ? 166  LYS A O     1 
ATOM   1344 C  CB    . LYS A 1 176 ? 15.656  0.594   5.180   1.00 37.34 ? 166  LYS A CB    1 
ATOM   1345 C  CG    . LYS A 1 176 ? 15.898  -0.904  5.167   1.00 39.39 ? 166  LYS A CG    1 
ATOM   1346 C  CD    . LYS A 1 176 ? 16.854  -1.284  6.288   1.00 41.36 ? 166  LYS A CD    1 
ATOM   1347 C  CE    . LYS A 1 176 ? 17.352  -2.707  6.141   1.00 43.49 ? 166  LYS A CE    1 
ATOM   1348 N  NZ    . LYS A 1 176 ? 18.096  -3.146  7.355   1.00 44.87 ? 166  LYS A NZ    1 
ATOM   1349 N  N     . GLU A 1 177 ? 13.350  2.947   5.143   1.00 30.99 ? 167  GLU A N     1 
ATOM   1350 C  CA    . GLU A 1 177 ? 13.160  4.347   5.512   1.00 29.87 ? 167  GLU A CA    1 
ATOM   1351 C  C     . GLU A 1 177 ? 12.212  4.459   6.691   1.00 28.37 ? 167  GLU A C     1 
ATOM   1352 O  O     . GLU A 1 177 ? 11.319  3.630   6.846   1.00 27.63 ? 167  GLU A O     1 
ATOM   1353 C  CB    . GLU A 1 177 ? 12.628  5.164   4.336   1.00 29.71 ? 167  GLU A CB    1 
ATOM   1354 C  CG    . GLU A 1 177 ? 11.254  4.749   3.829   1.00 29.58 ? 167  GLU A CG    1 
ATOM   1355 C  CD    . GLU A 1 177 ? 10.837  5.550   2.624   1.00 30.10 ? 167  GLU A CD    1 
ATOM   1356 O  OE1   . GLU A 1 177 ? 10.096  6.544   2.797   1.00 29.40 ? 167  GLU A OE1   1 
ATOM   1357 O  OE2   . GLU A 1 177 ? 11.275  5.207   1.507   1.00 30.88 ? 167  GLU A OE2   1 
ATOM   1358 N  N     . GLU A 1 178 ? 12.408  5.500   7.492   1.00 27.64 ? 168  GLU A N     1 
ATOM   1359 C  CA    . GLU A 1 178 ? 11.537  5.793   8.615   1.00 27.12 ? 168  GLU A CA    1 
ATOM   1360 C  C     . GLU A 1 178 ? 10.114  5.952   8.101   1.00 26.16 ? 168  GLU A C     1 
ATOM   1361 O  O     . GLU A 1 178 ? 9.893   6.560   7.049   1.00 25.24 ? 168  GLU A O     1 
ATOM   1362 C  CB    . GLU A 1 178 ? 11.988  7.062   9.335   1.00 27.61 ? 168  GLU A CB    1 
ATOM   1363 C  CG    . GLU A 1 178 ? 11.187  7.359   10.588  1.00 27.78 ? 168  GLU A CG    1 
ATOM   1364 C  CD    . GLU A 1 178 ? 11.680  8.568   11.328  1.00 28.35 ? 168  GLU A CD    1 
ATOM   1365 O  OE1   . GLU A 1 178 ? 12.788  8.483   11.905  1.00 30.17 ? 168  GLU A OE1   1 
ATOM   1366 O  OE2   . GLU A 1 178 ? 10.965  9.591   11.351  1.00 28.50 ? 168  GLU A OE2   1 
ATOM   1367 N  N     . SER A 1 179 ? 9.164   5.385   8.845   1.00 25.11 ? 169  SER A N     1 
ATOM   1368 C  CA    . SER A 1 179 ? 7.779   5.286   8.406   1.00 24.24 ? 169  SER A CA    1 
ATOM   1369 C  C     . SER A 1 179 ? 6.857   5.076   9.612   1.00 23.92 ? 169  SER A C     1 
ATOM   1370 O  O     . SER A 1 179 ? 7.195   4.345   10.546  1.00 23.71 ? 169  SER A O     1 
ATOM   1371 C  CB    . SER A 1 179 ? 7.630   4.116   7.431   1.00 24.73 ? 169  SER A CB    1 
ATOM   1372 O  OG    . SER A 1 179 ? 6.302   3.980   6.949   1.00 24.96 ? 169  SER A OG    1 
ATOM   1373 N  N     . TYR A 1 180 ? 5.697   5.723   9.566   1.00 22.78 ? 170  TYR A N     1 
ATOM   1374 C  CA    . TYR A 1 180 ? 4.620   5.455   10.512  1.00 23.11 ? 170  TYR A CA    1 
ATOM   1375 C  C     . TYR A 1 180 ? 3.832   4.217   10.095  1.00 22.93 ? 170  TYR A C     1 
ATOM   1376 O  O     . TYR A 1 180 ? 3.535   4.017   8.907   1.00 22.39 ? 170  TYR A O     1 
ATOM   1377 C  CB    . TYR A 1 180 ? 3.682   6.658   10.611  1.00 22.86 ? 170  TYR A CB    1 
ATOM   1378 C  CG    . TYR A 1 180 ? 4.181   7.768   11.499  1.00 22.86 ? 170  TYR A CG    1 
ATOM   1379 C  CD1   . TYR A 1 180 ? 4.639   8.964   10.956  1.00 23.01 ? 170  TYR A CD1   1 
ATOM   1380 C  CD2   . TYR A 1 180 ? 4.189   7.632   12.900  1.00 23.26 ? 170  TYR A CD2   1 
ATOM   1381 C  CE1   . TYR A 1 180 ? 5.103   9.991   11.768  1.00 23.51 ? 170  TYR A CE1   1 
ATOM   1382 C  CE2   . TYR A 1 180 ? 4.641   8.650   13.711  1.00 23.30 ? 170  TYR A CE2   1 
ATOM   1383 C  CZ    . TYR A 1 180 ? 5.091   9.831   13.142  1.00 23.50 ? 170  TYR A CZ    1 
ATOM   1384 O  OH    . TYR A 1 180 ? 5.554   10.847  13.931  1.00 24.37 ? 170  TYR A OH    1 
ATOM   1385 N  N     . PHE A 1 181 ? 3.453   3.411   11.086  1.00 23.16 ? 171  PHE A N     1 
ATOM   1386 C  CA    . PHE A 1 181 ? 2.684   2.181   10.869  1.00 23.17 ? 171  PHE A CA    1 
ATOM   1387 C  C     . PHE A 1 181 ? 1.355   2.219   11.588  1.00 22.77 ? 171  PHE A C     1 
ATOM   1388 O  O     . PHE A 1 181 ? 1.305   2.646   12.721  1.00 22.95 ? 171  PHE A O     1 
ATOM   1389 C  CB    . PHE A 1 181 ? 3.443   0.985   11.415  1.00 24.29 ? 171  PHE A CB    1 
ATOM   1390 C  CG    . PHE A 1 181 ? 4.556   0.541   10.534  1.00 25.13 ? 171  PHE A CG    1 
ATOM   1391 C  CD1   . PHE A 1 181 ? 5.824   1.057   10.697  1.00 26.16 ? 171  PHE A CD1   1 
ATOM   1392 C  CD2   . PHE A 1 181 ? 4.321   -0.365  9.513   1.00 25.67 ? 171  PHE A CD2   1 
ATOM   1393 C  CE1   . PHE A 1 181 ? 6.859   0.660   9.868   1.00 26.66 ? 171  PHE A CE1   1 
ATOM   1394 C  CE2   . PHE A 1 181 ? 5.355   -0.784  8.694   1.00 26.22 ? 171  PHE A CE2   1 
ATOM   1395 C  CZ    . PHE A 1 181 ? 6.621   -0.263  8.873   1.00 26.73 ? 171  PHE A CZ    1 
ATOM   1396 N  N     . PHE A 1 182 ? 0.316   1.726   10.921  1.00 21.81 ? 172  PHE A N     1 
ATOM   1397 C  CA    . PHE A 1 182 ? -1.048  1.601   11.457  1.00 21.58 ? 172  PHE A CA    1 
ATOM   1398 C  C     . PHE A 1 182 ? -1.247  0.124   11.809  1.00 22.26 ? 172  PHE A C     1 
ATOM   1399 O  O     . PHE A 1 182 ? -1.102  -0.750  10.952  1.00 22.55 ? 172  PHE A O     1 
ATOM   1400 C  CB    . PHE A 1 182 ? -2.009  2.105   10.370  1.00 20.90 ? 172  PHE A CB    1 
ATOM   1401 C  CG    . PHE A 1 182 ? -3.496  1.991   10.666  1.00 20.40 ? 172  PHE A CG    1 
ATOM   1402 C  CD1   . PHE A 1 182 ? -4.019  1.850   11.947  1.00 20.70 ? 172  PHE A CD1   1 
ATOM   1403 C  CD2   . PHE A 1 182 ? -4.392  2.103   9.602   1.00 20.61 ? 172  PHE A CD2   1 
ATOM   1404 C  CE1   . PHE A 1 182 ? -5.398  1.774   12.143  1.00 20.43 ? 172  PHE A CE1   1 
ATOM   1405 C  CE2   . PHE A 1 182 ? -5.768  2.026   9.791   1.00 20.15 ? 172  PHE A CE2   1 
ATOM   1406 C  CZ    . PHE A 1 182 ? -6.271  1.881   11.066  1.00 20.28 ? 172  PHE A CZ    1 
ATOM   1407 N  N     . ASN A 1 183 ? -1.566  -0.148  13.077  1.00 23.18 ? 173  ASN A N     1 
ATOM   1408 C  CA    . ASN A 1 183 ? -1.805  -1.518  13.535  1.00 23.77 ? 173  ASN A CA    1 
ATOM   1409 C  C     . ASN A 1 183 ? -3.235  -1.906  13.149  1.00 23.97 ? 173  ASN A C     1 
ATOM   1410 O  O     . ASN A 1 183 ? -4.182  -1.697  13.910  1.00 24.69 ? 173  ASN A O     1 
ATOM   1411 C  CB    . ASN A 1 183 ? -1.573  -1.658  15.051  1.00 25.46 ? 173  ASN A CB    1 
ATOM   1412 C  CG    . ASN A 1 183 ? -1.893  -3.058  15.579  1.00 26.25 ? 173  ASN A CG    1 
ATOM   1413 O  OD1   . ASN A 1 183 ? -2.148  -3.991  14.816  1.00 27.73 ? 173  ASN A OD1   1 
ATOM   1414 N  ND2   . ASN A 1 183 ? -1.868  -3.209  16.899  1.00 28.06 ? 173  ASN A ND2   1 
ATOM   1415 N  N     . ILE A 1 184 ? -3.365  -2.462  11.954  1.00 23.60 ? 174  ILE A N     1 
ATOM   1416 C  CA    . ILE A 1 184 ? -4.665  -2.863  11.426  1.00 24.09 ? 174  ILE A CA    1 
ATOM   1417 C  C     . ILE A 1 184 ? -5.140  -4.198  12.000  1.00 25.11 ? 174  ILE A C     1 
ATOM   1418 O  O     . ILE A 1 184 ? -6.345  -4.431  12.079  1.00 25.30 ? 174  ILE A O     1 
ATOM   1419 C  CB    . ILE A 1 184 ? -4.702  -2.870  9.877   1.00 23.94 ? 174  ILE A CB    1 
ATOM   1420 C  CG1   . ILE A 1 184 ? -3.609  -3.753  9.257   1.00 24.21 ? 174  ILE A CG1   1 
ATOM   1421 C  CG2   . ILE A 1 184 ? -4.589  -1.433  9.381   1.00 23.41 ? 174  ILE A CG2   1 
ATOM   1422 C  CD1   . ILE A 1 184 ? -3.813  -4.002  7.771   1.00 24.40 ? 174  ILE A CD1   1 
ATOM   1423 N  N     . SER A 1 185 ? -4.211  -5.047  12.441  1.00 26.25 ? 175  SER A N     1 
ATOM   1424 C  CA    . SER A 1 185 ? -4.582  -6.396  12.915  1.00 27.17 ? 175  SER A CA    1 
ATOM   1425 C  C     . SER A 1 185 ? -5.461  -6.394  14.167  1.00 26.77 ? 175  SER A C     1 
ATOM   1426 O  O     . SER A 1 185 ? -6.206  -7.357  14.392  1.00 26.99 ? 175  SER A O     1 
ATOM   1427 C  CB    . SER A 1 185 ? -3.348  -7.267  13.161  1.00 28.84 ? 175  SER A CB    1 
ATOM   1428 O  OG    . SER A 1 185 ? -2.579  -6.773  14.241  1.00 30.31 ? 175  SER A OG    1 
ATOM   1429 N  N     . LYS A 1 186 ? -5.384  -5.329  14.969  1.00 26.24 ? 176  LYS A N     1 
ATOM   1430 C  CA    . LYS A 1 186 ? -6.263  -5.170  16.148  1.00 26.84 ? 176  LYS A CA    1 
ATOM   1431 C  C     . LYS A 1 186 ? -7.747  -5.288  15.780  1.00 26.66 ? 176  LYS A C     1 
ATOM   1432 O  O     . LYS A 1 186 ? -8.559  -5.774  16.570  1.00 26.70 ? 176  LYS A O     1 
ATOM   1433 C  CB    . LYS A 1 186 ? -6.024  -3.813  16.844  1.00 27.53 ? 176  LYS A CB    1 
ATOM   1434 C  CG    . LYS A 1 186 ? -6.836  -3.621  18.123  1.00 28.51 ? 176  LYS A CG    1 
ATOM   1435 C  CD    . LYS A 1 186 ? -6.566  -2.278  18.773  1.00 28.64 ? 176  LYS A CD    1 
ATOM   1436 C  CE    . LYS A 1 186 ? -7.292  -1.130  18.093  1.00 28.45 ? 176  LYS A CE    1 
ATOM   1437 N  NZ    . LYS A 1 186 ? -7.350  0.066   18.979  1.00 27.95 ? 176  LYS A NZ    1 
ATOM   1438 N  N     . TYR A 1 187 ? -8.081  -4.842  14.571  1.00 25.91 ? 177  TYR A N     1 
ATOM   1439 C  CA    . TYR A 1 187 ? -9.449  -4.805  14.086  1.00 25.72 ? 177  TYR A CA    1 
ATOM   1440 C  C     . TYR A 1 187 ? -9.907  -6.081  13.367  1.00 26.24 ? 177  TYR A C     1 
ATOM   1441 O  O     . TYR A 1 187 ? -11.023 -6.117  12.866  1.00 26.48 ? 177  TYR A O     1 
ATOM   1442 C  CB    . TYR A 1 187 ? -9.606  -3.585  13.158  1.00 24.63 ? 177  TYR A CB    1 
ATOM   1443 C  CG    . TYR A 1 187 ? -9.375  -2.276  13.874  1.00 24.15 ? 177  TYR A CG    1 
ATOM   1444 C  CD1   . TYR A 1 187 ? -8.112  -1.692  13.922  1.00 24.22 ? 177  TYR A CD1   1 
ATOM   1445 C  CD2   . TYR A 1 187 ? -10.420 -1.634  14.529  1.00 24.25 ? 177  TYR A CD2   1 
ATOM   1446 C  CE1   . TYR A 1 187 ? -7.899  -0.501  14.594  1.00 23.60 ? 177  TYR A CE1   1 
ATOM   1447 C  CE2   . TYR A 1 187 ? -10.220 -0.448  15.204  1.00 24.25 ? 177  TYR A CE2   1 
ATOM   1448 C  CZ    . TYR A 1 187 ? -8.964  0.118   15.237  1.00 23.98 ? 177  TYR A CZ    1 
ATOM   1449 O  OH    . TYR A 1 187 ? -8.793  1.296   15.914  1.00 24.18 ? 177  TYR A OH    1 
ATOM   1450 N  N     . THR A 1 188 ? -9.077  -7.126  13.343  1.00 27.56 ? 178  THR A N     1 
ATOM   1451 C  CA    . THR A 1 188 ? -9.367  -8.338  12.567  1.00 29.32 ? 178  THR A CA    1 
ATOM   1452 C  C     . THR A 1 188 ? -10.722 -8.965  12.932  1.00 29.53 ? 178  THR A C     1 
ATOM   1453 O  O     . THR A 1 188 ? -11.554 -9.196  12.056  1.00 27.92 ? 178  THR A O     1 
ATOM   1454 C  CB    . THR A 1 188 ? -8.235  -9.382  12.710  1.00 30.27 ? 178  THR A CB    1 
ATOM   1455 O  OG1   . THR A 1 188 ? -7.007  -8.814  12.240  1.00 30.81 ? 178  THR A OG1   1 
ATOM   1456 C  CG2   . THR A 1 188 ? -8.526  -10.641 11.899  1.00 31.00 ? 178  THR A CG2   1 
ATOM   1457 N  N     . ASP A 1 189 ? -10.934 -9.234  14.218  1.00 31.28 ? 179  ASP A N     1 
ATOM   1458 C  CA    . ASP A 1 189 ? -12.196 -9.853  14.669  1.00 32.50 ? 179  ASP A CA    1 
ATOM   1459 C  C     . ASP A 1 189 ? -13.421 -8.995  14.366  1.00 31.26 ? 179  ASP A C     1 
ATOM   1460 O  O     . ASP A 1 189 ? -14.460 -9.520  13.971  1.00 29.17 ? 179  ASP A O     1 
ATOM   1461 C  CB    . ASP A 1 189 ? -12.149 -10.181 16.165  1.00 34.55 ? 179  ASP A CB    1 
ATOM   1462 C  CG    . ASP A 1 189 ? -11.156 -11.289 16.498  1.00 37.42 ? 179  ASP A CG    1 
ATOM   1463 O  OD1   . ASP A 1 189 ? -10.748 -12.050 15.595  1.00 38.74 ? 179  ASP A OD1   1 
ATOM   1464 O  OD2   . ASP A 1 189 ? -10.784 -11.403 17.683  1.00 39.79 ? 179  ASP A OD2   1 
ATOM   1465 N  N     . ARG A 1 190 ? -13.287 -7.680  14.546  1.00 29.74 ? 180  ARG A N     1 
ATOM   1466 C  CA    . ARG A 1 190 ? -14.368 -6.760  14.211  1.00 30.25 ? 180  ARG A CA    1 
ATOM   1467 C  C     . ARG A 1 190 ? -14.681 -6.775  12.723  1.00 28.80 ? 180  ARG A C     1 
ATOM   1468 O  O     . ARG A 1 190 ? -15.842 -6.685  12.344  1.00 28.11 ? 180  ARG A O     1 
ATOM   1469 C  CB    . ARG A 1 190 ? -14.058 -5.331  14.659  1.00 31.08 ? 180  ARG A CB    1 
ATOM   1470 C  CG    . ARG A 1 190 ? -14.216 -5.122  16.158  1.00 33.04 ? 180  ARG A CG    1 
ATOM   1471 C  CD    . ARG A 1 190 ? -13.968 -3.677  16.552  1.00 33.79 ? 180  ARG A CD    1 
ATOM   1472 N  NE    . ARG A 1 190 ? -14.961 -2.772  15.966  1.00 34.43 ? 180  ARG A NE    1 
ATOM   1473 C  CZ    . ARG A 1 190 ? -14.919 -1.438  16.034  1.00 34.50 ? 180  ARG A CZ    1 
ATOM   1474 N  NH1   . ARG A 1 190 ? -13.930 -0.815  16.674  1.00 34.62 ? 180  ARG A NH1   1 
ATOM   1475 N  NH2   . ARG A 1 190 ? -15.876 -0.718  15.451  1.00 35.61 ? 180  ARG A NH2   1 
ATOM   1476 N  N     . LEU A 1 191 ? -13.650 -6.883  11.887  1.00 27.68 ? 181  LEU A N     1 
ATOM   1477 C  CA    . LEU A 1 191 ? -13.859 -6.950  10.437  1.00 28.09 ? 181  LEU A CA    1 
ATOM   1478 C  C     . LEU A 1 191 ? -14.582 -8.234  10.030  1.00 29.16 ? 181  LEU A C     1 
ATOM   1479 O  O     . LEU A 1 191 ? -15.524 -8.197  9.233   1.00 28.76 ? 181  LEU A O     1 
ATOM   1480 C  CB    . LEU A 1 191 ? -12.537 -6.845  9.691   1.00 27.75 ? 181  LEU A CB    1 
ATOM   1481 C  CG    . LEU A 1 191 ? -12.584 -6.864  8.162   1.00 27.41 ? 181  LEU A CG    1 
ATOM   1482 C  CD1   . LEU A 1 191 ? -13.418 -5.720  7.603   1.00 27.29 ? 181  LEU A CD1   1 
ATOM   1483 C  CD2   . LEU A 1 191 ? -11.163 -6.798  7.626   1.00 26.90 ? 181  LEU A CD2   1 
ATOM   1484 N  N     . LEU A 1 192 ? -14.148 -9.368  10.579  1.00 30.58 ? 182  LEU A N     1 
ATOM   1485 C  CA    . LEU A 1 192 ? -14.798 -10.645 10.269  1.00 32.26 ? 182  LEU A CA    1 
ATOM   1486 C  C     . LEU A 1 192 ? -16.259 -10.648 10.733  1.00 32.55 ? 182  LEU A C     1 
ATOM   1487 O  O     . LEU A 1 192 ? -17.137 -11.135 10.020  1.00 32.54 ? 182  LEU A O     1 
ATOM   1488 C  CB    . LEU A 1 192 ? -14.013 -11.823 10.853  1.00 33.53 ? 182  LEU A CB    1 
ATOM   1489 C  CG    . LEU A 1 192 ? -12.592 -12.025 10.302  1.00 34.50 ? 182  LEU A CG    1 
ATOM   1490 C  CD1   . LEU A 1 192 ? -11.842 -13.071 11.115  1.00 35.53 ? 182  LEU A CD1   1 
ATOM   1491 C  CD2   . LEU A 1 192 ? -12.591 -12.422 8.835   1.00 34.24 ? 182  LEU A CD2   1 
ATOM   1492 N  N     . GLU A 1 193 ? -16.513 -10.059 11.895  1.00 33.18 ? 183  GLU A N     1 
ATOM   1493 C  CA    . GLU A 1 193 ? -17.880 -9.864  12.395  1.00 35.06 ? 183  GLU A CA    1 
ATOM   1494 C  C     . GLU A 1 193 ? -18.710 -9.006  11.427  1.00 33.45 ? 183  GLU A C     1 
ATOM   1495 O  O     . GLU A 1 193 ? -19.863 -9.323  11.135  1.00 31.67 ? 183  GLU A O     1 
ATOM   1496 C  CB    . GLU A 1 193 ? -17.849 -9.222  13.788  1.00 37.87 ? 183  GLU A CB    1 
ATOM   1497 C  CG    . GLU A 1 193 ? -19.214 -8.970  14.415  1.00 40.32 ? 183  GLU A CG    1 
ATOM   1498 C  CD    . GLU A 1 193 ? -19.119 -8.431  15.838  1.00 43.33 ? 183  GLU A CD    1 
ATOM   1499 O  OE1   . GLU A 1 193 ? -18.378 -7.442  16.064  1.00 44.90 ? 183  GLU A OE1   1 
ATOM   1500 O  OE2   . GLU A 1 193 ? -19.791 -8.993  16.734  1.00 46.65 ? 183  GLU A OE2   1 
ATOM   1501 N  N     . PHE A 1 194 ? -18.111 -7.927  10.926  1.00 31.84 ? 184  PHE A N     1 
ATOM   1502 C  CA    . PHE A 1 194 ? -18.754 -7.087  9.918   1.00 31.04 ? 184  PHE A CA    1 
ATOM   1503 C  C     . PHE A 1 194 ? -19.146 -7.890  8.669   1.00 30.83 ? 184  PHE A C     1 
ATOM   1504 O  O     . PHE A 1 194 ? -20.281 -7.783  8.202   1.00 29.86 ? 184  PHE A O     1 
ATOM   1505 C  CB    . PHE A 1 194 ? -17.855 -5.898  9.547   1.00 30.31 ? 184  PHE A CB    1 
ATOM   1506 C  CG    . PHE A 1 194 ? -18.401 -5.052  8.437   1.00 29.94 ? 184  PHE A CG    1 
ATOM   1507 C  CD1   . PHE A 1 194 ? -19.502 -4.237  8.657   1.00 30.22 ? 184  PHE A CD1   1 
ATOM   1508 C  CD2   . PHE A 1 194 ? -17.827 -5.076  7.166   1.00 29.52 ? 184  PHE A CD2   1 
ATOM   1509 C  CE1   . PHE A 1 194 ? -20.020 -3.455  7.635   1.00 30.16 ? 184  PHE A CE1   1 
ATOM   1510 C  CE2   . PHE A 1 194 ? -18.345 -4.297  6.143   1.00 29.77 ? 184  PHE A CE2   1 
ATOM   1511 C  CZ    . PHE A 1 194 ? -19.441 -3.490  6.378   1.00 29.89 ? 184  PHE A CZ    1 
ATOM   1512 N  N     . TYR A 1 195 ? -18.224 -8.695  8.139   1.00 30.37 ? 185  TYR A N     1 
ATOM   1513 C  CA    . TYR A 1 195 ? -18.533 -9.560  6.993   1.00 31.22 ? 185  TYR A CA    1 
ATOM   1514 C  C     . TYR A 1 195 ? -19.719 -10.493 7.270   1.00 33.53 ? 185  TYR A C     1 
ATOM   1515 O  O     . TYR A 1 195 ? -20.563 -10.699 6.401   1.00 33.30 ? 185  TYR A O     1 
ATOM   1516 C  CB    . TYR A 1 195 ? -17.334 -10.418 6.590   1.00 30.64 ? 185  TYR A CB    1 
ATOM   1517 C  CG    . TYR A 1 195 ? -16.121 -9.694  6.039   1.00 29.54 ? 185  TYR A CG    1 
ATOM   1518 C  CD1   . TYR A 1 195 ? -14.899 -10.343 5.986   1.00 29.71 ? 185  TYR A CD1   1 
ATOM   1519 C  CD2   . TYR A 1 195 ? -16.180 -8.372  5.569   1.00 28.97 ? 185  TYR A CD2   1 
ATOM   1520 C  CE1   . TYR A 1 195 ? -13.770 -9.721  5.490   1.00 29.00 ? 185  TYR A CE1   1 
ATOM   1521 C  CE2   . TYR A 1 195 ? -15.050 -7.741  5.069   1.00 28.21 ? 185  TYR A CE2   1 
ATOM   1522 C  CZ    . TYR A 1 195 ? -13.850 -8.422  5.027   1.00 28.59 ? 185  TYR A CZ    1 
ATOM   1523 O  OH    . TYR A 1 195 ? -12.710 -7.836  4.532   1.00 27.82 ? 185  TYR A OH    1 
ATOM   1524 N  N     . ASP A 1 196 ? -19.775 -11.041 8.482   1.00 36.47 ? 186  ASP A N     1 
ATOM   1525 C  CA    . ASP A 1 196 ? -20.883 -11.918 8.896   1.00 39.57 ? 186  ASP A CA    1 
ATOM   1526 C  C     . ASP A 1 196 ? -22.236 -11.206 8.928   1.00 39.73 ? 186  ASP A C     1 
ATOM   1527 O  O     . ASP A 1 196 ? -23.241 -11.754 8.473   1.00 39.64 ? 186  ASP A O     1 
ATOM   1528 C  CB    . ASP A 1 196 ? -20.598 -12.525 10.274  1.00 43.07 ? 186  ASP A CB    1 
ATOM   1529 C  CG    . ASP A 1 196 ? -19.476 -13.534 10.244  1.00 45.71 ? 186  ASP A CG    1 
ATOM   1530 O  OD1   . ASP A 1 196 ? -18.647 -13.534 11.180  1.00 49.26 ? 186  ASP A OD1   1 
ATOM   1531 O  OD2   . ASP A 1 196 ? -19.425 -14.337 9.289   1.00 49.28 ? 186  ASP A OD2   1 
ATOM   1532 N  N     . GLN A 1 197 ? -22.247 -9.986  9.458   1.00 39.52 ? 187  GLN A N     1 
ATOM   1533 C  CA    . GLN A 1 197 ? -23.460 -9.165  9.507   1.00 40.88 ? 187  GLN A CA    1 
ATOM   1534 C  C     . GLN A 1 197 ? -23.853 -8.560  8.154   1.00 40.14 ? 187  GLN A C     1 
ATOM   1535 O  O     . GLN A 1 197 ? -24.983 -8.109  7.999   1.00 40.12 ? 187  GLN A O     1 
ATOM   1536 C  CB    . GLN A 1 197 ? -23.298 -8.030  10.523  1.00 42.54 ? 187  GLN A CB    1 
ATOM   1537 C  CG    . GLN A 1 197 ? -23.177 -8.479  11.971  1.00 44.67 ? 187  GLN A CG    1 
ATOM   1538 C  CD    . GLN A 1 197 ? -22.712 -7.365  12.897  1.00 46.58 ? 187  GLN A CD    1 
ATOM   1539 O  OE1   . GLN A 1 197 ? -22.714 -6.183  12.533  1.00 48.34 ? 187  GLN A OE1   1 
ATOM   1540 N  NE2   . GLN A 1 197 ? -22.307 -7.739  14.106  1.00 48.45 ? 187  GLN A NE2   1 
ATOM   1541 N  N     . ASN A 1 198 ? -22.923 -8.527  7.200   1.00 38.55 ? 188  ASN A N     1 
ATOM   1542 C  CA    . ASN A 1 198 ? -23.134 -7.893  5.889   1.00 38.51 ? 188  ASN A CA    1 
ATOM   1543 C  C     . ASN A 1 198 ? -22.699 -8.833  4.767   1.00 38.20 ? 188  ASN A C     1 
ATOM   1544 O  O     . ASN A 1 198 ? -21.681 -8.601  4.108   1.00 35.44 ? 188  ASN A O     1 
ATOM   1545 C  CB    . ASN A 1 198 ? -22.365 -6.574  5.813   1.00 38.38 ? 188  ASN A CB    1 
ATOM   1546 C  CG    . ASN A 1 198 ? -22.808 -5.594  6.867   1.00 38.84 ? 188  ASN A CG    1 
ATOM   1547 O  OD1   . ASN A 1 198 ? -22.375 -5.670  8.014   1.00 39.19 ? 188  ASN A OD1   1 
ATOM   1548 N  ND2   . ASN A 1 198 ? -23.684 -4.677  6.491   1.00 39.54 ? 188  ASN A ND2   1 
ATOM   1549 N  N     . PRO A 1 199 ? -23.492 -9.896  4.523   1.00 38.99 ? 189  PRO A N     1 
ATOM   1550 C  CA    . PRO A 1 199 ? -23.080 -10.980 3.621   1.00 39.35 ? 189  PRO A CA    1 
ATOM   1551 C  C     . PRO A 1 199 ? -22.884 -10.584 2.154   1.00 39.11 ? 189  PRO A C     1 
ATOM   1552 O  O     . PRO A 1 199 ? -22.212 -11.306 1.420   1.00 39.70 ? 189  PRO A O     1 
ATOM   1553 C  CB    . PRO A 1 199 ? -24.233 -11.989 3.749   1.00 40.67 ? 189  PRO A CB    1 
ATOM   1554 C  CG    . PRO A 1 199 ? -25.415 -11.152 4.092   1.00 40.37 ? 189  PRO A CG    1 
ATOM   1555 C  CD    . PRO A 1 199 ? -24.877 -10.087 5.000   1.00 39.89 ? 189  PRO A CD    1 
ATOM   1556 N  N     . ASP A 1 200 ? -23.463 -9.456  1.744   1.00 38.18 ? 190  ASP A N     1 
ATOM   1557 C  CA    . ASP A 1 200 ? -23.356 -8.956  0.372   1.00 38.24 ? 190  ASP A CA    1 
ATOM   1558 C  C     . ASP A 1 200 ? -22.388 -7.769  0.219   1.00 34.93 ? 190  ASP A C     1 
ATOM   1559 O  O     . ASP A 1 200 ? -22.378 -7.110  -0.821  1.00 34.56 ? 190  ASP A O     1 
ATOM   1560 C  CB    . ASP A 1 200 ? -24.754 -8.583  -0.138  1.00 40.39 ? 190  ASP A CB    1 
ATOM   1561 C  CG    . ASP A 1 200 ? -25.752 -9.742  -0.030  1.00 42.27 ? 190  ASP A CG    1 
ATOM   1562 O  OD1   . ASP A 1 200 ? -25.342 -10.916 -0.200  1.00 44.00 ? 190  ASP A OD1   1 
ATOM   1563 O  OD2   . ASP A 1 200 ? -26.948 -9.474  0.222   1.00 44.19 ? 190  ASP A OD2   1 
ATOM   1564 N  N     . PHE A 1 201 ? -21.565 -7.522  1.241   1.00 32.48 ? 191  PHE A N     1 
ATOM   1565 C  CA    . PHE A 1 201 ? -20.559 -6.458  1.209   1.00 31.29 ? 191  PHE A CA    1 
ATOM   1566 C  C     . PHE A 1 201 ? -19.532 -6.727  0.101   1.00 32.53 ? 191  PHE A C     1 
ATOM   1567 O  O     . PHE A 1 201 ? -19.224 -5.841  -0.705  1.00 30.92 ? 191  PHE A O     1 
ATOM   1568 C  CB    . PHE A 1 201 ? -19.864 -6.347  2.577   1.00 29.91 ? 191  PHE A CB    1 
ATOM   1569 C  CG    . PHE A 1 201 ? -18.731 -5.353  2.604   1.00 28.46 ? 191  PHE A CG    1 
ATOM   1570 C  CD1   . PHE A 1 201 ? -18.976 -4.003  2.396   1.00 27.59 ? 191  PHE A CD1   1 
ATOM   1571 C  CD2   . PHE A 1 201 ? -17.427 -5.762  2.843   1.00 27.61 ? 191  PHE A CD2   1 
ATOM   1572 C  CE1   . PHE A 1 201 ? -17.935 -3.077  2.406   1.00 27.22 ? 191  PHE A CE1   1 
ATOM   1573 C  CE2   . PHE A 1 201 ? -16.385 -4.849  2.864   1.00 27.32 ? 191  PHE A CE2   1 
ATOM   1574 C  CZ    . PHE A 1 201 ? -16.637 -3.499  2.636   1.00 27.06 ? 191  PHE A CZ    1 
ATOM   1575 N  N     . ILE A 1 202 ? -19.013 -7.957  0.085   1.00 33.96 ? 192  ILE A N     1 
ATOM   1576 C  CA    . ILE A 1 202 ? -18.135 -8.459  -0.985  1.00 36.31 ? 192  ILE A CA    1 
ATOM   1577 C  C     . ILE A 1 202 ? -18.844 -9.611  -1.705  1.00 38.30 ? 192  ILE A C     1 
ATOM   1578 O  O     . ILE A 1 202 ? -19.340 -10.547 -1.060  1.00 38.51 ? 192  ILE A O     1 
ATOM   1579 C  CB    . ILE A 1 202 ? -16.798 -9.031  -0.453  1.00 37.97 ? 192  ILE A CB    1 
ATOM   1580 C  CG1   . ILE A 1 202 ? -16.061 -8.045  0.450   1.00 39.08 ? 192  ILE A CG1   1 
ATOM   1581 C  CG2   . ILE A 1 202 ? -15.874 -9.407  -1.609  1.00 38.74 ? 192  ILE A CG2   1 
ATOM   1582 C  CD1   . ILE A 1 202 ? -15.115 -8.734  1.419   1.00 39.48 ? 192  ILE A CD1   1 
ATOM   1583 N  N     . GLN A 1 203 ? -18.864 -9.544  -3.031  1.00 39.02 ? 193  GLN A N     1 
ATOM   1584 C  CA    . GLN A 1 203 ? -19.422 -10.609 -3.874  1.00 40.61 ? 193  GLN A CA    1 
ATOM   1585 C  C     . GLN A 1 203 ? -18.471 -10.922 -5.028  1.00 40.07 ? 193  GLN A C     1 
ATOM   1586 O  O     . GLN A 1 203 ? -17.677 -10.067 -5.407  1.00 38.67 ? 193  GLN A O     1 
ATOM   1587 C  CB    . GLN A 1 203 ? -20.785 -10.194 -4.421  1.00 41.76 ? 193  GLN A CB    1 
ATOM   1588 C  CG    . GLN A 1 203 ? -21.852 -10.071 -3.347  1.00 43.27 ? 193  GLN A CG    1 
ATOM   1589 C  CD    . GLN A 1 203 ? -23.182 -9.594  -3.895  1.00 44.87 ? 193  GLN A CD    1 
ATOM   1590 O  OE1   . GLN A 1 203 ? -23.250 -8.584  -4.601  1.00 46.40 ? 193  GLN A OE1   1 
ATOM   1591 N  NE2   . GLN A 1 203 ? -24.254 -10.308 -3.556  1.00 45.93 ? 193  GLN A NE2   1 
ATOM   1592 N  N     . PRO A 1 204 ? -18.508 -12.137 -5.579  1.00 41.24 ? 194  PRO A N     1 
ATOM   1593 C  CA    . PRO A 1 204 ? -19.287 -13.285 -5.077  1.00 41.66 ? 194  PRO A CA    1 
ATOM   1594 C  C     . PRO A 1 204 ? -18.636 -13.940 -3.831  1.00 42.21 ? 194  PRO A C     1 
ATOM   1595 O  O     . PRO A 1 204 ? -17.563 -13.501 -3.400  1.00 40.02 ? 194  PRO A O     1 
ATOM   1596 C  CB    . PRO A 1 204 ? -19.277 -14.248 -6.275  1.00 42.13 ? 194  PRO A CB    1 
ATOM   1597 C  CG    . PRO A 1 204 ? -18.003 -13.937 -6.988  1.00 42.33 ? 194  PRO A CG    1 
ATOM   1598 C  CD    . PRO A 1 204 ? -17.787 -12.456 -6.826  1.00 42.06 ? 194  PRO A CD    1 
ATOM   1599 N  N     . PRO A 1 205 ? -19.279 -14.977 -3.248  1.00 43.19 ? 195  PRO A N     1 
ATOM   1600 C  CA    . PRO A 1 205 ? -18.713 -15.671 -2.078  1.00 43.40 ? 195  PRO A CA    1 
ATOM   1601 C  C     . PRO A 1 205 ? -17.247 -16.104 -2.207  1.00 42.76 ? 195  PRO A C     1 
ATOM   1602 O  O     . PRO A 1 205 ? -16.499 -16.027 -1.229  1.00 42.59 ? 195  PRO A O     1 
ATOM   1603 C  CB    . PRO A 1 205 ? -19.627 -16.891 -1.937  1.00 44.56 ? 195  PRO A CB    1 
ATOM   1604 C  CG    . PRO A 1 205 ? -20.950 -16.388 -2.394  1.00 44.29 ? 195  PRO A CG    1 
ATOM   1605 C  CD    . PRO A 1 205 ? -20.648 -15.455 -3.537  1.00 44.11 ? 195  PRO A CD    1 
ATOM   1606 N  N     . SER A 1 206 ? -16.848 -16.539 -3.399  1.00 43.04 ? 196  SER A N     1 
ATOM   1607 C  CA    . SER A 1 206 ? -15.445 -16.874 -3.679  1.00 43.81 ? 196  SER A CA    1 
ATOM   1608 C  C     . SER A 1 206 ? -14.491 -15.698 -3.428  1.00 43.29 ? 196  SER A C     1 
ATOM   1609 O  O     . SER A 1 206 ? -13.408 -15.888 -2.875  1.00 43.34 ? 196  SER A O     1 
ATOM   1610 C  CB    . SER A 1 206 ? -15.288 -17.370 -5.116  1.00 44.41 ? 196  SER A CB    1 
ATOM   1611 O  OG    . SER A 1 206 ? -15.723 -16.398 -6.042  1.00 44.62 ? 196  SER A OG    1 
ATOM   1612 N  N     . ARG A 1 207 ? -14.909 -14.496 -3.825  1.00 41.89 ? 197  ARG A N     1 
ATOM   1613 C  CA    . ARG A 1 207 ? -14.122 -13.273 -3.585  1.00 41.98 ? 197  ARG A CA    1 
ATOM   1614 C  C     . ARG A 1 207 ? -13.993 -12.951 -2.096  1.00 41.64 ? 197  ARG A C     1 
ATOM   1615 O  O     . ARG A 1 207 ? -12.918 -12.578 -1.648  1.00 41.13 ? 197  ARG A O     1 
ATOM   1616 C  CB    . ARG A 1 207 ? -14.718 -12.073 -4.335  1.00 41.42 ? 197  ARG A CB    1 
ATOM   1617 C  CG    . ARG A 1 207 ? -13.735 -10.921 -4.556  1.00 41.44 ? 197  ARG A CG    1 
ATOM   1618 C  CD    . ARG A 1 207 ? -14.424 -9.666  -5.085  1.00 41.19 ? 197  ARG A CD    1 
ATOM   1619 N  NE    . ARG A 1 207 ? -15.116 -9.869  -6.366  1.00 41.76 ? 197  ARG A NE    1 
ATOM   1620 C  CZ    . ARG A 1 207 ? -14.537 -9.878  -7.568  1.00 41.94 ? 197  ARG A CZ    1 
ATOM   1621 N  NH1   . ARG A 1 207 ? -13.227 -9.716  -7.703  1.00 41.75 ? 197  ARG A NH1   1 
ATOM   1622 N  NH2   . ARG A 1 207 ? -15.282 -10.069 -8.653  1.00 43.46 ? 197  ARG A NH2   1 
ATOM   1623 N  N     . LYS A 1 208 ? -15.078 -13.089 -1.336  1.00 43.18 ? 198  LYS A N     1 
ATOM   1624 C  CA    . LYS A 1 208 ? -15.022 -12.912 0.126   1.00 45.34 ? 198  LYS A CA    1 
ATOM   1625 C  C     . LYS A 1 208 ? -14.050 -13.911 0.771   1.00 46.53 ? 198  LYS A C     1 
ATOM   1626 O  O     . LYS A 1 208 ? -13.201 -13.518 1.571   1.00 45.53 ? 198  LYS A O     1 
ATOM   1627 C  CB    . LYS A 1 208 ? -16.405 -13.059 0.774   1.00 47.06 ? 198  LYS A CB    1 
ATOM   1628 C  CG    . LYS A 1 208 ? -16.414 -12.704 2.263   1.00 48.54 ? 198  LYS A CG    1 
ATOM   1629 C  CD    . LYS A 1 208 ? -17.448 -13.476 3.070   1.00 50.70 ? 198  LYS A CD    1 
ATOM   1630 C  CE    . LYS A 1 208 ? -18.816 -12.824 3.011   1.00 52.25 ? 198  LYS A CE    1 
ATOM   1631 N  NZ    . LYS A 1 208 ? -19.800 -13.529 3.880   1.00 53.97 ? 198  LYS A NZ    1 
ATOM   1632 N  N     . ASN A 1 209 ? -14.185 -15.191 0.426   1.00 47.69 ? 199  ASN A N     1 
ATOM   1633 C  CA    . ASN A 1 209 ? -13.262 -16.233 0.918   1.00 50.06 ? 199  ASN A CA    1 
ATOM   1634 C  C     . ASN A 1 209 ? -11.812 -15.931 0.546   1.00 50.50 ? 199  ASN A C     1 
ATOM   1635 O  O     . ASN A 1 209 ? -10.900 -16.145 1.342   1.00 50.58 ? 199  ASN A O     1 
ATOM   1636 C  CB    . ASN A 1 209 ? -13.639 -17.607 0.360   1.00 51.23 ? 199  ASN A CB    1 
ATOM   1637 C  CG    . ASN A 1 209 ? -12.704 -18.706 0.843   1.00 52.63 ? 199  ASN A CG    1 
ATOM   1638 O  OD1   . ASN A 1 209 ? -12.040 -19.373 0.041   1.00 54.84 ? 199  ASN A OD1   1 
ATOM   1639 N  ND2   . ASN A 1 209 ? -12.632 -18.885 2.158   1.00 51.60 ? 199  ASN A ND2   1 
ATOM   1640 N  N     . GLU A 1 210 ? -11.631 -15.440 -0.677  1.00 51.68 ? 200  GLU A N     1 
ATOM   1641 C  CA    . GLU A 1 210 ? -10.335 -14.982 -1.189  1.00 53.19 ? 200  GLU A CA    1 
ATOM   1642 C  C     . GLU A 1 210 ? -9.697  -13.931 -0.272  1.00 51.69 ? 200  GLU A C     1 
ATOM   1643 O  O     . GLU A 1 210 ? -8.537  -14.067 0.107   1.00 52.74 ? 200  GLU A O     1 
ATOM   1644 C  CB    . GLU A 1 210 ? -10.518 -14.389 -2.587  1.00 54.96 ? 200  GLU A CB    1 
ATOM   1645 C  CG    . GLU A 1 210 ? -9.292  -14.400 -3.470  1.00 57.02 ? 200  GLU A CG    1 
ATOM   1646 C  CD    . GLU A 1 210 ? -9.510  -13.548 -4.705  1.00 58.39 ? 200  GLU A CD    1 
ATOM   1647 O  OE1   . GLU A 1 210 ? -10.443 -13.861 -5.485  1.00 59.32 ? 200  GLU A OE1   1 
ATOM   1648 O  OE2   . GLU A 1 210 ? -8.768  -12.556 -4.874  1.00 59.10 ? 200  GLU A OE2   1 
ATOM   1649 N  N     . MET A 1 211 ? -10.466 -12.896 0.074   1.00 50.15 ? 201  MET A N     1 
ATOM   1650 C  CA    . MET A 1 211 ? -10.017 -11.847 1.007   1.00 49.31 ? 201  MET A CA    1 
ATOM   1651 C  C     . MET A 1 211 ? -9.591  -12.451 2.344   1.00 49.59 ? 201  MET A C     1 
ATOM   1652 O  O     . MET A 1 211 ? -8.507  -12.153 2.850   1.00 50.02 ? 201  MET A O     1 
ATOM   1653 C  CB    . MET A 1 211 ? -11.119 -10.805 1.272   1.00 48.44 ? 201  MET A CB    1 
ATOM   1654 C  CG    . MET A 1 211 ? -11.518 -9.925  0.097   1.00 47.43 ? 201  MET A CG    1 
ATOM   1655 S  SD    . MET A 1 211 ? -10.153 -9.051  -0.685  1.00 46.59 ? 201  MET A SD    1 
ATOM   1656 C  CE    . MET A 1 211 ? -9.835  -10.033 -2.151  1.00 47.26 ? 201  MET A CE    1 
ATOM   1657 N  N     . ILE A 1 212 ? -10.444 -13.313 2.889   1.00 49.96 ? 202  ILE A N     1 
ATOM   1658 C  CA    . ILE A 1 212 ? -10.245 -13.882 4.224   1.00 50.69 ? 202  ILE A CA    1 
ATOM   1659 C  C     . ILE A 1 212 ? -9.021  -14.812 4.239   1.00 51.76 ? 202  ILE A C     1 
ATOM   1660 O  O     . ILE A 1 212 ? -8.131  -14.647 5.074   1.00 50.65 ? 202  ILE A O     1 
ATOM   1661 C  CB    . ILE A 1 212 ? -11.528 -14.588 4.742   1.00 51.32 ? 202  ILE A CB    1 
ATOM   1662 C  CG1   . ILE A 1 212 ? -12.673 -13.567 4.878   1.00 50.57 ? 202  ILE A CG1   1 
ATOM   1663 C  CG2   . ILE A 1 212 ? -11.294 -15.251 6.100   1.00 51.20 ? 202  ILE A CG2   1 
ATOM   1664 C  CD1   . ILE A 1 212 ? -14.059 -14.169 4.969   1.00 50.89 ? 202  ILE A CD1   1 
ATOM   1665 N  N     . ASN A 1 213 ? -8.970  -15.754 3.298   1.00 52.70 ? 203  ASN A N     1 
ATOM   1666 C  CA    . ASN A 1 213 ? -7.923  -16.790 3.277   1.00 54.05 ? 203  ASN A CA    1 
ATOM   1667 C  C     . ASN A 1 213 ? -6.534  -16.285 2.889   1.00 52.70 ? 203  ASN A C     1 
ATOM   1668 O  O     . ASN A 1 213 ? -5.554  -16.639 3.536   1.00 52.35 ? 203  ASN A O     1 
ATOM   1669 C  CB    . ASN A 1 213 ? -8.324  -17.946 2.344   1.00 55.58 ? 203  ASN A CB    1 
ATOM   1670 C  CG    . ASN A 1 213 ? -9.415  -18.839 2.926   1.00 56.48 ? 203  ASN A CG    1 
ATOM   1671 O  OD1   . ASN A 1 213 ? -9.852  -19.781 2.270   1.00 58.88 ? 203  ASN A OD1   1 
ATOM   1672 N  ND2   . ASN A 1 213 ? -9.853  -18.560 4.151   1.00 56.76 ? 203  ASN A ND2   1 
ATOM   1673 N  N     . ASN A 1 214 ? -6.452  -15.475 1.837   1.00 51.51 ? 204  ASN A N     1 
ATOM   1674 C  CA    . ASN A 1 214 ? -5.161  -14.983 1.339   1.00 51.36 ? 204  ASN A CA    1 
ATOM   1675 C  C     . ASN A 1 214 ? -4.529  -13.887 2.200   1.00 49.53 ? 204  ASN A C     1 
ATOM   1676 O  O     . ASN A 1 214 ? -3.307  -13.818 2.288   1.00 48.90 ? 204  ASN A O     1 
ATOM   1677 C  CB    . ASN A 1 214 ? -5.293  -14.455 -0.095  1.00 52.55 ? 204  ASN A CB    1 
ATOM   1678 C  CG    . ASN A 1 214 ? -5.656  -15.537 -1.096  1.00 53.47 ? 204  ASN A CG    1 
ATOM   1679 O  OD1   . ASN A 1 214 ? -5.807  -16.710 -0.746  1.00 55.04 ? 204  ASN A OD1   1 
ATOM   1680 N  ND2   . ASN A 1 214 ? -5.795  -15.142 -2.358  1.00 52.88 ? 204  ASN A ND2   1 
ATOM   1681 N  N     . PHE A 1 215 ? -5.354  -13.031 2.808   1.00 47.71 ? 205  PHE A N     1 
ATOM   1682 C  CA    . PHE A 1 215 ? -4.867  -11.799 3.453   1.00 46.68 ? 205  PHE A CA    1 
ATOM   1683 C  C     . PHE A 1 215 ? -5.139  -11.686 4.946   1.00 45.72 ? 205  PHE A C     1 
ATOM   1684 O  O     . PHE A 1 215 ? -4.240  -11.330 5.707   1.00 47.75 ? 205  PHE A O     1 
ATOM   1685 C  CB    . PHE A 1 215 ? -5.443  -10.577 2.740   1.00 47.04 ? 205  PHE A CB    1 
ATOM   1686 C  CG    . PHE A 1 215 ? -5.213  -10.586 1.255   1.00 47.13 ? 205  PHE A CG    1 
ATOM   1687 C  CD1   . PHE A 1 215 ? -6.282  -10.492 0.368   1.00 47.68 ? 205  PHE A CD1   1 
ATOM   1688 C  CD2   . PHE A 1 215 ? -3.923  -10.709 0.739   1.00 47.28 ? 205  PHE A CD2   1 
ATOM   1689 C  CE1   . PHE A 1 215 ? -6.069  -10.502 -1.005  1.00 48.18 ? 205  PHE A CE1   1 
ATOM   1690 C  CE2   . PHE A 1 215 ? -3.702  -10.727 -0.631  1.00 47.56 ? 205  PHE A CE2   1 
ATOM   1691 C  CZ    . PHE A 1 215 ? -4.775  -10.625 -1.506  1.00 48.41 ? 205  PHE A CZ    1 
ATOM   1692 N  N     . ILE A 1 216 ? -6.366  -11.976 5.365   1.00 43.44 ? 206  ILE A N     1 
ATOM   1693 C  CA    . ILE A 1 216 ? -6.758  -11.797 6.767   1.00 42.61 ? 206  ILE A CA    1 
ATOM   1694 C  C     . ILE A 1 216 ? -6.264  -12.958 7.637   1.00 44.05 ? 206  ILE A C     1 
ATOM   1695 O  O     . ILE A 1 216 ? -5.654  -12.733 8.685   1.00 42.56 ? 206  ILE A O     1 
ATOM   1696 C  CB    . ILE A 1 216 ? -8.283  -11.613 6.923   1.00 41.49 ? 206  ILE A CB    1 
ATOM   1697 C  CG1   . ILE A 1 216 ? -8.754  -10.396 6.112   1.00 40.00 ? 206  ILE A CG1   1 
ATOM   1698 C  CG2   . ILE A 1 216 ? -8.644  -11.411 8.391   1.00 41.26 ? 206  ILE A CG2   1 
ATOM   1699 C  CD1   . ILE A 1 216 ? -10.256 -10.250 5.995   1.00 39.72 ? 206  ILE A CD1   1 
ATOM   1700 N  N     . LYS A 1 217 ? -6.538  -14.182 7.185   1.00 44.95 ? 207  LYS A N     1 
ATOM   1701 C  CA    . LYS A 1 217 ? -6.221  -15.416 7.919   1.00 45.78 ? 207  LYS A CA    1 
ATOM   1702 C  C     . LYS A 1 217 ? -4.760  -15.536 8.368   1.00 45.03 ? 207  LYS A C     1 
ATOM   1703 O  O     . LYS A 1 217 ? -4.512  -15.701 9.560   1.00 45.83 ? 207  LYS A O     1 
ATOM   1704 C  CB    . LYS A 1 217 ? -6.622  -16.649 7.096   1.00 46.31 ? 207  LYS A CB    1 
ATOM   1705 N  N     . PRO A 1 218 ? -3.790  -15.437 7.432   1.00 45.17 ? 208  PRO A N     1 
ATOM   1706 C  CA    . PRO A 1 218 ? -2.382  -15.525 7.869   1.00 44.63 ? 208  PRO A CA    1 
ATOM   1707 C  C     . PRO A 1 218 ? -1.900  -14.394 8.794   1.00 42.61 ? 208  PRO A C     1 
ATOM   1708 O  O     . PRO A 1 218 ? -0.852  -14.536 9.426   1.00 42.98 ? 208  PRO A O     1 
ATOM   1709 C  CB    . PRO A 1 218 ? -1.593  -15.541 6.551   1.00 45.15 ? 208  PRO A CB    1 
ATOM   1710 C  CG    . PRO A 1 218 ? -2.521  -15.012 5.518   1.00 45.29 ? 208  PRO A CG    1 
ATOM   1711 C  CD    . PRO A 1 218 ? -3.899  -15.378 5.963   1.00 45.35 ? 208  PRO A CD    1 
ATOM   1712 N  N     . GLY A 1 219 ? -2.658  -13.298 8.867   1.00 38.73 ? 209  GLY A N     1 
ATOM   1713 C  CA    . GLY A 1 219 ? -2.389  -12.199 9.793   1.00 37.14 ? 209  GLY A CA    1 
ATOM   1714 C  C     . GLY A 1 219 ? -2.116  -10.930 9.011   1.00 34.42 ? 209  GLY A C     1 
ATOM   1715 O  O     . GLY A 1 219 ? -1.290  -10.930 8.105   1.00 33.95 ? 209  GLY A O     1 
ATOM   1716 N  N     . LEU A 1 220 ? -2.821  -9.856  9.355   1.00 32.34 ? 210  LEU A N     1 
ATOM   1717 C  CA    . LEU A 1 220 ? -2.639  -8.566  8.687   1.00 30.65 ? 210  LEU A CA    1 
ATOM   1718 C  C     . LEU A 1 220 ? -1.394  -7.888  9.251   1.00 29.63 ? 210  LEU A C     1 
ATOM   1719 O  O     . LEU A 1 220 ? -1.359  -7.525  10.421  1.00 30.06 ? 210  LEU A O     1 
ATOM   1720 C  CB    . LEU A 1 220 ? -3.863  -7.673  8.900   1.00 30.08 ? 210  LEU A CB    1 
ATOM   1721 C  CG    . LEU A 1 220 ? -5.172  -8.150  8.260   1.00 30.07 ? 210  LEU A CG    1 
ATOM   1722 C  CD1   . LEU A 1 220 ? -6.344  -7.340  8.787   1.00 29.60 ? 210  LEU A CD1   1 
ATOM   1723 C  CD2   . LEU A 1 220 ? -5.103  -8.101  6.740   1.00 29.79 ? 210  LEU A CD2   1 
ATOM   1724 N  N     . ALA A 1 221 ? -0.367  -7.726  8.426   1.00 29.04 ? 211  ALA A N     1 
ATOM   1725 C  CA    . ALA A 1 221 ? 0.839   -7.000  8.843   1.00 28.60 ? 211  ALA A CA    1 
ATOM   1726 C  C     . ALA A 1 221 ? 0.520   -5.530  9.092   1.00 27.32 ? 211  ALA A C     1 
ATOM   1727 O  O     . ALA A 1 221 ? -0.410  -4.980  8.484   1.00 26.62 ? 211  ALA A O     1 
ATOM   1728 C  CB    . ALA A 1 221 ? 1.922   -7.117  7.785   1.00 29.10 ? 211  ALA A CB    1 
ATOM   1729 N  N     . ASP A 1 222 ? 1.292   -4.895  9.969   1.00 26.32 ? 212  ASP A N     1 
ATOM   1730 C  CA    . ASP A 1 222 ? 1.164   -3.451  10.180  1.00 25.86 ? 212  ASP A CA    1 
ATOM   1731 C  C     . ASP A 1 222 ? 1.315   -2.737  8.846   1.00 24.65 ? 212  ASP A C     1 
ATOM   1732 O  O     . ASP A 1 222 ? 2.128   -3.133  8.005   1.00 24.57 ? 212  ASP A O     1 
ATOM   1733 C  CB    . ASP A 1 222 ? 2.229   -2.925  11.138  1.00 26.65 ? 212  ASP A CB    1 
ATOM   1734 C  CG    . ASP A 1 222 ? 2.002   -3.350  12.576  1.00 28.11 ? 212  ASP A CG    1 
ATOM   1735 O  OD1   . ASP A 1 222 ? 0.916   -3.888  12.924  1.00 28.13 ? 212  ASP A OD1   1 
ATOM   1736 O  OD2   . ASP A 1 222 ? 2.955   -3.128  13.363  1.00 29.87 ? 212  ASP A OD2   1 
ATOM   1737 N  N     . LEU A 1 223 ? 0.540   -1.676  8.676   1.00 23.07 ? 213  LEU A N     1 
ATOM   1738 C  CA    . LEU A 1 223 ? 0.460   -0.973  7.405   1.00 22.23 ? 213  LEU A CA    1 
ATOM   1739 C  C     . LEU A 1 223 ? 1.322   0.289   7.446   1.00 21.28 ? 213  LEU A C     1 
ATOM   1740 O  O     . LEU A 1 223 ? 1.107   1.170   8.272   1.00 20.30 ? 213  LEU A O     1 
ATOM   1741 C  CB    . LEU A 1 223 ? -1.002  -0.622  7.135   1.00 22.18 ? 213  LEU A CB    1 
ATOM   1742 C  CG    . LEU A 1 223 ? -1.318  -0.020  5.767   1.00 22.52 ? 213  LEU A CG    1 
ATOM   1743 C  CD1   . LEU A 1 223 ? -1.087  -1.022  4.641   1.00 23.06 ? 213  LEU A CD1   1 
ATOM   1744 C  CD2   . LEU A 1 223 ? -2.752  0.449   5.766   1.00 22.53 ? 213  LEU A CD2   1 
ATOM   1745 N  N     . ALA A 1 224 ? 2.302   0.374   6.550   1.00 21.23 ? 214  ALA A N     1 
ATOM   1746 C  CA    . ALA A 1 224 ? 3.205   1.524   6.488   1.00 21.50 ? 214  ALA A CA    1 
ATOM   1747 C  C     . ALA A 1 224 ? 2.471   2.666   5.802   1.00 20.52 ? 214  ALA A C     1 
ATOM   1748 O  O     . ALA A 1 224 ? 2.286   2.648   4.564   1.00 20.68 ? 214  ALA A O     1 
ATOM   1749 C  CB    . ALA A 1 224 ? 4.478   1.164   5.730   1.00 21.73 ? 214  ALA A CB    1 
ATOM   1750 N  N     . VAL A 1 225 ? 2.048   3.643   6.608   1.00 20.04 ? 215  VAL A N     1 
ATOM   1751 C  CA    . VAL A 1 225 ? 1.104   4.679   6.173   1.00 19.76 ? 215  VAL A CA    1 
ATOM   1752 C  C     . VAL A 1 225 ? 1.770   6.034   5.911   1.00 19.89 ? 215  VAL A C     1 
ATOM   1753 O  O     . VAL A 1 225 ? 1.090   6.983   5.533   1.00 19.32 ? 215  VAL A O     1 
ATOM   1754 C  CB    . VAL A 1 225 ? -0.104  4.841   7.151   1.00 19.71 ? 215  VAL A CB    1 
ATOM   1755 C  CG1   . VAL A 1 225 ? -1.055  3.650   7.045   1.00 19.95 ? 215  VAL A CG1   1 
ATOM   1756 C  CG2   . VAL A 1 225 ? 0.340   5.066   8.598   1.00 19.87 ? 215  VAL A CG2   1 
ATOM   1757 N  N     . SER A 1 226 ? 3.091   6.123   6.095   1.00 20.02 ? 216  SER A N     1 
ATOM   1758 C  CA    . SER A 1 226 ? 3.847   7.304   5.674   1.00 20.25 ? 216  SER A CA    1 
ATOM   1759 C  C     . SER A 1 226 ? 5.156   6.893   5.005   1.00 21.26 ? 216  SER A C     1 
ATOM   1760 O  O     . SER A 1 226 ? 5.568   5.732   5.056   1.00 20.96 ? 216  SER A O     1 
ATOM   1761 C  CB    . SER A 1 226 ? 4.146   8.235   6.846   1.00 20.49 ? 216  SER A CB    1 
ATOM   1762 O  OG    . SER A 1 226 ? 5.151   7.689   7.671   1.00 20.90 ? 216  SER A OG    1 
ATOM   1763 N  N     . ARG A 1 227 ? 5.791   7.873   4.374   1.00 21.71 ? 217  ARG A N     1 
ATOM   1764 C  CA    . ARG A 1 227 ? 7.120   7.710   3.776   1.00 22.31 ? 217  ARG A CA    1 
ATOM   1765 C  C     . ARG A 1 227 ? 7.918   8.969   4.082   1.00 23.56 ? 217  ARG A C     1 
ATOM   1766 O  O     . ARG A 1 227 ? 7.342   10.020  4.325   1.00 22.81 ? 217  ARG A O     1 
ATOM   1767 C  CB    . ARG A 1 227 ? 7.011   7.481   2.260   1.00 22.75 ? 217  ARG A CB    1 
ATOM   1768 C  CG    . ARG A 1 227 ? 6.334   6.173   1.845   1.00 23.14 ? 217  ARG A CG    1 
ATOM   1769 C  CD    . ARG A 1 227 ? 7.146   4.955   2.257   1.00 23.97 ? 217  ARG A CD    1 
ATOM   1770 N  NE    . ARG A 1 227 ? 6.584   3.698   1.774   1.00 24.46 ? 217  ARG A NE    1 
ATOM   1771 C  CZ    . ARG A 1 227 ? 5.511   3.074   2.276   1.00 24.37 ? 217  ARG A CZ    1 
ATOM   1772 N  NH1   . ARG A 1 227 ? 4.814   3.587   3.294   1.00 23.95 ? 217  ARG A NH1   1 
ATOM   1773 N  NH2   . ARG A 1 227 ? 5.098   1.934   1.719   1.00 24.44 ? 217  ARG A NH2   1 
ATOM   1774 N  N     . THR A 1 228 ? 9.241   8.824   4.123   1.00 24.34 ? 218  THR A N     1 
ATOM   1775 C  CA    . THR A 1 228 ? 10.177  9.932   4.342   1.00 25.21 ? 218  THR A CA    1 
ATOM   1776 C  C     . THR A 1 228 ? 11.106  10.192  3.154   1.00 26.03 ? 218  THR A C     1 
ATOM   1777 O  O     . THR A 1 228 ? 11.842  11.175  3.168   1.00 28.51 ? 218  THR A O     1 
ATOM   1778 C  CB    . THR A 1 228 ? 11.029  9.668   5.600   1.00 25.21 ? 218  THR A CB    1 
ATOM   1779 O  OG1   . THR A 1 228 ? 11.490  8.309   5.585   1.00 25.56 ? 218  THR A OG1   1 
ATOM   1780 C  CG2   . THR A 1 228 ? 10.197  9.882   6.848   1.00 25.10 ? 218  THR A CG2   1 
ATOM   1781 N  N     . SER A 1 229 ? 11.050  9.355   2.126   1.00 26.33 ? 219  SER A N     1 
ATOM   1782 C  CA    . SER A 1 229 ? 12.020  9.408   1.010   1.00 26.80 ? 219  SER A CA    1 
ATOM   1783 C  C     . SER A 1 229 ? 11.641  10.343  -0.154  1.00 26.67 ? 219  SER A C     1 
ATOM   1784 O  O     . SER A 1 229 ? 12.428  10.503  -1.088  1.00 27.23 ? 219  SER A O     1 
ATOM   1785 C  CB    . SER A 1 229 ? 12.286  7.998   0.480   1.00 27.11 ? 219  SER A CB    1 
ATOM   1786 O  OG    . SER A 1 229 ? 11.121  7.410   -0.066  1.00 28.47 ? 219  SER A OG    1 
ATOM   1787 N  N     . PHE A 1 230 ? 10.441  10.928  -0.117  1.00 25.55 ? 220  PHE A N     1 
ATOM   1788 C  CA    . PHE A 1 230 ? 10.015  11.894  -1.136  1.00 25.26 ? 220  PHE A CA    1 
ATOM   1789 C  C     . PHE A 1 230 ? 9.084   12.941  -0.527  1.00 24.45 ? 220  PHE A C     1 
ATOM   1790 O  O     . PHE A 1 230 ? 8.610   12.777  0.596   1.00 24.62 ? 220  PHE A O     1 
ATOM   1791 C  CB    . PHE A 1 230 ? 9.383   11.181  -2.334  1.00 25.53 ? 220  PHE A CB    1 
ATOM   1792 C  CG    . PHE A 1 230 ? 8.123   10.433  -2.006  1.00 24.87 ? 220  PHE A CG    1 
ATOM   1793 C  CD1   . PHE A 1 230 ? 8.171   9.110   -1.555  1.00 25.38 ? 220  PHE A CD1   1 
ATOM   1794 C  CD2   . PHE A 1 230 ? 6.886   11.030  -2.173  1.00 24.30 ? 220  PHE A CD2   1 
ATOM   1795 C  CE1   . PHE A 1 230 ? 7.004   8.422   -1.261  1.00 25.07 ? 220  PHE A CE1   1 
ATOM   1796 C  CE2   . PHE A 1 230 ? 5.719   10.351  -1.864  1.00 24.70 ? 220  PHE A CE2   1 
ATOM   1797 C  CZ    . PHE A 1 230 ? 5.776   9.043   -1.414  1.00 24.58 ? 220  PHE A CZ    1 
ATOM   1798 N  N     . ASN A 1 231 ? 8.856   14.027  -1.262  1.00 23.84 ? 221  ASN A N     1 
ATOM   1799 C  CA    . ASN A 1 231 ? 8.146   15.202  -0.729  1.00 24.19 ? 221  ASN A CA    1 
ATOM   1800 C  C     . ASN A 1 231 ? 6.757   15.468  -1.290  1.00 23.21 ? 221  ASN A C     1 
ATOM   1801 O  O     . ASN A 1 231 ? 5.997   16.214  -0.673  1.00 22.83 ? 221  ASN A O     1 
ATOM   1802 C  CB    . ASN A 1 231 ? 8.993   16.464  -0.922  1.00 25.42 ? 221  ASN A CB    1 
ATOM   1803 C  CG    . ASN A 1 231 ? 10.254  16.455  -0.086  1.00 27.05 ? 221  ASN A CG    1 
ATOM   1804 O  OD1   . ASN A 1 231 ? 11.351  16.637  -0.612  1.00 29.73 ? 221  ASN A OD1   1 
ATOM   1805 N  ND2   . ASN A 1 231 ? 10.103  16.277  1.216   1.00 27.28 ? 221  ASN A ND2   1 
ATOM   1806 N  N     . TRP A 1 232 ? 6.440   14.904  -2.454  1.00 21.57 ? 222  TRP A N     1 
ATOM   1807 C  CA    . TRP A 1 232 ? 5.182   15.200  -3.115  1.00 20.83 ? 222  TRP A CA    1 
ATOM   1808 C  C     . TRP A 1 232 ? 4.027   14.374  -2.524  1.00 20.64 ? 222  TRP A C     1 
ATOM   1809 O  O     . TRP A 1 232 ? 3.713   13.264  -2.973  1.00 20.70 ? 222  TRP A O     1 
ATOM   1810 C  CB    . TRP A 1 232 ? 5.299   15.065  -4.638  1.00 20.16 ? 222  TRP A CB    1 
ATOM   1811 C  CG    . TRP A 1 232 ? 4.038   15.465  -5.324  1.00 19.87 ? 222  TRP A CG    1 
ATOM   1812 C  CD1   . TRP A 1 232 ? 3.201   14.653  -6.002  1.00 19.67 ? 222  TRP A CD1   1 
ATOM   1813 C  CD2   . TRP A 1 232 ? 3.446   16.775  -5.353  1.00 19.18 ? 222  TRP A CD2   1 
ATOM   1814 N  NE1   . TRP A 1 232 ? 2.110   15.357  -6.453  1.00 19.37 ? 222  TRP A NE1   1 
ATOM   1815 C  CE2   . TRP A 1 232 ? 2.238   16.664  -6.073  1.00 19.29 ? 222  TRP A CE2   1 
ATOM   1816 C  CE3   . TRP A 1 232 ? 3.817   18.027  -4.833  1.00 19.87 ? 222  TRP A CE3   1 
ATOM   1817 C  CZ2   . TRP A 1 232 ? 1.393   17.745  -6.299  1.00 19.71 ? 222  TRP A CZ2   1 
ATOM   1818 C  CZ3   . TRP A 1 232 ? 2.972   19.117  -5.057  1.00 19.92 ? 222  TRP A CZ3   1 
ATOM   1819 C  CH2   . TRP A 1 232 ? 1.770   18.964  -5.796  1.00 19.93 ? 222  TRP A CH2   1 
ATOM   1820 N  N     . GLY A 1 233 ? 3.435   14.943  -1.482  1.00 20.19 ? 223  GLY A N     1 
ATOM   1821 C  CA    . GLY A 1 233 ? 2.264   14.386  -0.815  1.00 20.20 ? 223  GLY A CA    1 
ATOM   1822 C  C     . GLY A 1 233 ? 1.853   15.237  0.363   1.00 20.33 ? 223  GLY A C     1 
ATOM   1823 O  O     . GLY A 1 233 ? 2.391   16.329  0.574   1.00 20.72 ? 223  GLY A O     1 
ATOM   1824 N  N     . VAL A 1 234 ? 0.879   14.749  1.116   1.00 20.47 ? 224  VAL A N     1 
ATOM   1825 C  CA    . VAL A 1 234 ? 0.383   15.449  2.292   1.00 20.60 ? 224  VAL A CA    1 
ATOM   1826 C  C     . VAL A 1 234 ? 1.365   15.219  3.437   1.00 21.50 ? 224  VAL A C     1 
ATOM   1827 O  O     . VAL A 1 234 ? 1.656   14.082  3.774   1.00 21.60 ? 224  VAL A O     1 
ATOM   1828 C  CB    . VAL A 1 234 ? -1.012  14.949  2.721   1.00 20.68 ? 224  VAL A CB    1 
ATOM   1829 C  CG1   . VAL A 1 234 ? -1.522  15.771  3.909   1.00 21.11 ? 224  VAL A CG1   1 
ATOM   1830 C  CG2   . VAL A 1 234 ? -2.003  15.028  1.573   1.00 20.99 ? 224  VAL A CG2   1 
ATOM   1831 N  N     . HIS A 1 235 ? 1.878   16.294  4.024   1.00 22.07 ? 225  HIS A N     1 
ATOM   1832 C  CA    . HIS A 1 235 ? 2.845   16.183  5.117   1.00 23.22 ? 225  HIS A CA    1 
ATOM   1833 C  C     . HIS A 1 235 ? 2.120   16.046  6.451   1.00 22.67 ? 225  HIS A C     1 
ATOM   1834 O  O     . HIS A 1 235 ? 1.052   16.619  6.641   1.00 22.31 ? 225  HIS A O     1 
ATOM   1835 C  CB    . HIS A 1 235 ? 3.822   17.357  5.088   1.00 25.08 ? 225  HIS A CB    1 
ATOM   1836 C  CG    . HIS A 1 235 ? 4.776   17.296  3.934   1.00 26.78 ? 225  HIS A CG    1 
ATOM   1837 N  ND1   . HIS A 1 235 ? 6.102   16.946  4.075   1.00 28.42 ? 225  HIS A ND1   1 
ATOM   1838 C  CD2   . HIS A 1 235 ? 4.574   17.467  2.604   1.00 27.96 ? 225  HIS A CD2   1 
ATOM   1839 C  CE1   . HIS A 1 235 ? 6.686   16.946  2.886   1.00 29.01 ? 225  HIS A CE1   1 
ATOM   1840 N  NE2   . HIS A 1 235 ? 5.777   17.244  1.977   1.00 28.76 ? 225  HIS A NE2   1 
ATOM   1841 N  N     . VAL A 1 236 ? 2.684   15.234  7.346   1.00 22.51 ? 226  VAL A N     1 
ATOM   1842 C  CA    . VAL A 1 236 ? 2.074   14.967  8.663   1.00 23.23 ? 226  VAL A CA    1 
ATOM   1843 C  C     . VAL A 1 236 ? 2.321   16.207  9.542   1.00 24.01 ? 226  VAL A C     1 
ATOM   1844 O  O     . VAL A 1 236 ? 3.483   16.555  9.762   1.00 24.41 ? 226  VAL A O     1 
ATOM   1845 C  CB    . VAL A 1 236 ? 2.703   13.720  9.326   1.00 23.33 ? 226  VAL A CB    1 
ATOM   1846 C  CG1   . VAL A 1 236 ? 2.163   13.497  10.744  1.00 24.01 ? 226  VAL A CG1   1 
ATOM   1847 C  CG2   . VAL A 1 236 ? 2.472   12.470  8.472   1.00 23.13 ? 226  VAL A CG2   1 
ATOM   1848 N  N     . PRO A 1 237 ? 1.252   16.867  10.045  1.00 25.00 ? 227  PRO A N     1 
ATOM   1849 C  CA    . PRO A 1 237 ? 1.475   18.128  10.785  1.00 26.16 ? 227  PRO A CA    1 
ATOM   1850 C  C     . PRO A 1 237 ? 2.454   18.026  11.961  1.00 26.88 ? 227  PRO A C     1 
ATOM   1851 O  O     . PRO A 1 237 ? 3.293   18.910  12.132  1.00 27.41 ? 227  PRO A O     1 
ATOM   1852 C  CB    . PRO A 1 237 ? 0.065   18.493  11.273  1.00 26.43 ? 227  PRO A CB    1 
ATOM   1853 C  CG    . PRO A 1 237 ? -0.830  17.954  10.202  1.00 26.31 ? 227  PRO A CG    1 
ATOM   1854 C  CD    . PRO A 1 237 ? -0.189  16.643  9.808   1.00 25.57 ? 227  PRO A CD    1 
ATOM   1855 N  N     . SER A 1 238 ? 2.363   16.943  12.729  1.00 27.95 ? 228  SER A N     1 
ATOM   1856 C  CA    . SER A 1 238 ? 3.218   16.754  13.908  1.00 28.74 ? 228  SER A CA    1 
ATOM   1857 C  C     . SER A 1 238 ? 4.612   16.189  13.603  1.00 29.12 ? 228  SER A C     1 
ATOM   1858 O  O     . SER A 1 238 ? 5.460   16.125  14.502  1.00 29.04 ? 228  SER A O     1 
ATOM   1859 C  CB    . SER A 1 238 ? 2.520   15.869  14.945  1.00 29.74 ? 228  SER A CB    1 
ATOM   1860 O  OG    . SER A 1 238 ? 2.395   14.555  14.472  1.00 31.00 ? 228  SER A OG    1 
ATOM   1861 N  N     . ASN A 1 239 ? 4.858   15.776  12.361  1.00 28.76 ? 229  ASN A N     1 
ATOM   1862 C  CA    . ASN A 1 239 ? 6.189   15.310  11.941  1.00 29.23 ? 229  ASN A CA    1 
ATOM   1863 C  C     . ASN A 1 239 ? 6.365   15.583  10.435  1.00 29.89 ? 229  ASN A C     1 
ATOM   1864 O  O     . ASN A 1 239 ? 6.245   14.662  9.619   1.00 28.32 ? 229  ASN A O     1 
ATOM   1865 C  CB    . ASN A 1 239 ? 6.367   13.830  12.287  1.00 29.11 ? 229  ASN A CB    1 
ATOM   1866 C  CG    . ASN A 1 239 ? 7.826   13.374  12.259  1.00 29.76 ? 229  ASN A CG    1 
ATOM   1867 O  OD1   . ASN A 1 239 ? 8.707   14.045  11.713  1.00 30.63 ? 229  ASN A OD1   1 
ATOM   1868 N  ND2   . ASN A 1 239 ? 8.077   12.198  12.827  1.00 28.68 ? 229  ASN A ND2   1 
ATOM   1869 N  N     . PRO A 1 240 ? 6.645   16.860  10.076  1.00 30.94 ? 230  PRO A N     1 
ATOM   1870 C  CA    . PRO A 1 240 ? 6.726   17.407  8.704   1.00 32.40 ? 230  PRO A CA    1 
ATOM   1871 C  C     . PRO A 1 240 ? 7.525   16.629  7.675   1.00 30.91 ? 230  PRO A C     1 
ATOM   1872 O  O     . PRO A 1 240 ? 7.199   16.692  6.491   1.00 30.95 ? 230  PRO A O     1 
ATOM   1873 C  CB    . PRO A 1 240 ? 7.425   18.755  8.911   1.00 33.29 ? 230  PRO A CB    1 
ATOM   1874 C  CG    . PRO A 1 240 ? 6.995   19.187  10.257  1.00 33.18 ? 230  PRO A CG    1 
ATOM   1875 C  CD    . PRO A 1 240 ? 6.925   17.922  11.073  1.00 32.61 ? 230  PRO A CD    1 
ATOM   1876 N  N     . LYS A 1 241 ? 8.567   15.926  8.105   1.00 30.13 ? 231  LYS A N     1 
ATOM   1877 C  CA    . LYS A 1 241 ? 9.394   15.171  7.169   1.00 29.87 ? 231  LYS A CA    1 
ATOM   1878 C  C     . LYS A 1 241 ? 8.716   13.902  6.637   1.00 26.89 ? 231  LYS A C     1 
ATOM   1879 O  O     . LYS A 1 241 ? 9.220   13.299  5.692   1.00 26.34 ? 231  LYS A O     1 
ATOM   1880 C  CB    . LYS A 1 241 ? 10.771  14.877  7.753   1.00 32.61 ? 231  LYS A CB    1 
ATOM   1881 C  CG    . LYS A 1 241 ? 10.807  13.867  8.873   1.00 34.68 ? 231  LYS A CG    1 
ATOM   1882 C  CD    . LYS A 1 241 ? 12.056  14.082  9.720   1.00 36.30 ? 231  LYS A CD    1 
ATOM   1883 C  CE    . LYS A 1 241 ? 12.147  13.076  10.851  1.00 38.70 ? 231  LYS A CE    1 
ATOM   1884 N  NZ    . LYS A 1 241 ? 12.715  11.791  10.351  1.00 40.92 ? 231  LYS A NZ    1 
ATOM   1885 N  N     . HIS A 1 242 ? 7.578   13.525  7.228   1.00 24.32 ? 232  HIS A N     1 
ATOM   1886 C  CA    . HIS A 1 242 ? 6.774   12.407  6.759   1.00 22.86 ? 232  HIS A CA    1 
ATOM   1887 C  C     . HIS A 1 242 ? 5.681   12.874  5.824   1.00 22.06 ? 232  HIS A C     1 
ATOM   1888 O  O     . HIS A 1 242 ? 5.004   13.860  6.111   1.00 22.11 ? 232  HIS A O     1 
ATOM   1889 C  CB    . HIS A 1 242 ? 6.122   11.683  7.937   1.00 22.66 ? 232  HIS A CB    1 
ATOM   1890 C  CG    . HIS A 1 242 ? 7.058   10.787  8.681   1.00 23.11 ? 232  HIS A CG    1 
ATOM   1891 N  ND1   . HIS A 1 242 ? 7.040   9.416   8.540   1.00 22.85 ? 232  HIS A ND1   1 
ATOM   1892 C  CD2   . HIS A 1 242 ? 8.047   11.064  9.565   1.00 23.20 ? 232  HIS A CD2   1 
ATOM   1893 C  CE1   . HIS A 1 242 ? 7.984   8.888   9.299   1.00 23.10 ? 232  HIS A CE1   1 
ATOM   1894 N  NE2   . HIS A 1 242 ? 8.605   9.866   9.936   1.00 23.11 ? 232  HIS A NE2   1 
ATOM   1895 N  N     A VAL A 1 243 ? 5.514   12.152  4.719   0.50 21.57 ? 233  VAL A N     1 
ATOM   1896 N  N     B VAL A 1 243 ? 5.524   12.173  4.701   0.50 21.51 ? 233  VAL A N     1 
ATOM   1897 C  CA    A VAL A 1 243 ? 4.398   12.340  3.808   0.50 21.45 ? 233  VAL A CA    1 
ATOM   1898 C  CA    B VAL A 1 243 ? 4.382   12.358  3.815   0.50 21.36 ? 233  VAL A CA    1 
ATOM   1899 C  C     A VAL A 1 243 ? 3.436   11.166  3.956   0.50 21.33 ? 233  VAL A C     1 
ATOM   1900 C  C     B VAL A 1 243 ? 3.435   11.174  3.968   0.50 21.28 ? 233  VAL A C     1 
ATOM   1901 O  O     A VAL A 1 243 ? 3.865   10.025  4.091   0.50 21.02 ? 233  VAL A O     1 
ATOM   1902 O  O     B VAL A 1 243 ? 3.874   10.040  4.118   0.50 20.99 ? 233  VAL A O     1 
ATOM   1903 C  CB    A VAL A 1 243 ? 4.886   12.476  2.353   0.50 21.82 ? 233  VAL A CB    1 
ATOM   1904 C  CB    B VAL A 1 243 ? 4.803   12.532  2.338   0.50 21.64 ? 233  VAL A CB    1 
ATOM   1905 C  CG1   A VAL A 1 243 ? 3.798   12.091  1.371   0.50 21.71 ? 233  VAL A CG1   1 
ATOM   1906 C  CG1   B VAL A 1 243 ? 5.809   13.666  2.227   0.50 22.11 ? 233  VAL A CG1   1 
ATOM   1907 C  CG2   A VAL A 1 243 ? 5.340   13.905  2.104   0.50 22.12 ? 233  VAL A CG2   1 
ATOM   1908 C  CG2   B VAL A 1 243 ? 5.378   11.245  1.769   0.50 21.45 ? 233  VAL A CG2   1 
ATOM   1909 N  N     . VAL A 1 244 ? 2.138   11.449  3.945   1.00 21.03 ? 234  VAL A N     1 
ATOM   1910 C  CA    . VAL A 1 244 ? 1.126   10.392  4.099   1.00 20.73 ? 234  VAL A CA    1 
ATOM   1911 C  C     . VAL A 1 244 ? 1.089   9.585   2.812   1.00 20.55 ? 234  VAL A C     1 
ATOM   1912 O  O     . VAL A 1 244 ? 0.986   10.153  1.732   1.00 21.91 ? 234  VAL A O     1 
ATOM   1913 C  CB    . VAL A 1 244 ? -0.263  10.966  4.427   1.00 19.93 ? 234  VAL A CB    1 
ATOM   1914 C  CG1   . VAL A 1 244 ? -1.288  9.854   4.582   1.00 19.97 ? 234  VAL A CG1   1 
ATOM   1915 C  CG2   . VAL A 1 244 ? -0.201  11.812  5.686   1.00 20.04 ? 234  VAL A CG2   1 
ATOM   1916 N  N     . TYR A 1 245 ? 1.186   8.261   2.926   1.00 20.41 ? 235  TYR A N     1 
ATOM   1917 C  CA    . TYR A 1 245 ? 1.241   7.394   1.752   1.00 20.28 ? 235  TYR A CA    1 
ATOM   1918 C  C     . TYR A 1 245 ? -0.176  7.117   1.210   1.00 19.67 ? 235  TYR A C     1 
ATOM   1919 O  O     . TYR A 1 245 ? -1.175  7.632   1.741   1.00 19.56 ? 235  TYR A O     1 
ATOM   1920 C  CB    . TYR A 1 245 ? 2.023   6.116   2.095   1.00 21.29 ? 235  TYR A CB    1 
ATOM   1921 C  CG    . TYR A 1 245 ? 2.506   5.299   0.899   1.00 22.40 ? 235  TYR A CG    1 
ATOM   1922 C  CD1   . TYR A 1 245 ? 3.220   5.889   -0.152  1.00 23.83 ? 235  TYR A CD1   1 
ATOM   1923 C  CD2   . TYR A 1 245 ? 2.242   3.933   0.817   1.00 23.57 ? 235  TYR A CD2   1 
ATOM   1924 C  CE1   . TYR A 1 245 ? 3.643   5.135   -1.246  1.00 25.13 ? 235  TYR A CE1   1 
ATOM   1925 C  CE2   . TYR A 1 245 ? 2.671   3.176   -0.263  1.00 24.62 ? 235  TYR A CE2   1 
ATOM   1926 C  CZ    . TYR A 1 245 ? 3.371   3.774   -1.290  1.00 25.25 ? 235  TYR A CZ    1 
ATOM   1927 O  OH    . TYR A 1 245 ? 3.780   2.997   -2.366  1.00 26.94 ? 235  TYR A OH    1 
ATOM   1928 N  N     . VAL A 1 246 ? -0.262  6.307   0.166   1.00 19.63 ? 236  VAL A N     1 
ATOM   1929 C  CA    . VAL A 1 246 ? -1.495  6.076   -0.572  1.00 19.64 ? 236  VAL A CA    1 
ATOM   1930 C  C     . VAL A 1 246 ? -2.696  5.651   0.285   1.00 19.30 ? 236  VAL A C     1 
ATOM   1931 O  O     . VAL A 1 246 ? -3.807  6.099   0.040   1.00 19.62 ? 236  VAL A O     1 
ATOM   1932 C  CB    . VAL A 1 246 ? -1.283  5.084   -1.742  1.00 20.51 ? 236  VAL A CB    1 
ATOM   1933 C  CG1   . VAL A 1 246 ? -0.940  3.677   -1.270  1.00 21.02 ? 236  VAL A CG1   1 
ATOM   1934 C  CG2   . VAL A 1 246 ? -2.504  5.055   -2.653  1.00 20.50 ? 236  VAL A CG2   1 
ATOM   1935 N  N     . TRP A 1 247 ? -2.463  4.802   1.285   1.00 19.43 ? 237  TRP A N     1 
ATOM   1936 C  CA    . TRP A 1 247 ? -3.555  4.100   1.960   1.00 19.91 ? 237  TRP A CA    1 
ATOM   1937 C  C     . TRP A 1 247 ? -4.560  5.105   2.539   1.00 19.71 ? 237  TRP A C     1 
ATOM   1938 O  O     . TRP A 1 247 ? -5.740  5.098   2.163   1.00 20.58 ? 237  TRP A O     1 
ATOM   1939 C  CB    . TRP A 1 247 ? -3.024  3.133   3.029   1.00 20.75 ? 237  TRP A CB    1 
ATOM   1940 C  CG    . TRP A 1 247 ? -1.892  2.268   2.535   1.00 21.38 ? 237  TRP A CG    1 
ATOM   1941 C  CD1   . TRP A 1 247 ? -0.596  2.270   2.973   1.00 21.89 ? 237  TRP A CD1   1 
ATOM   1942 C  CD2   . TRP A 1 247 ? -1.948  1.333   1.457   1.00 22.19 ? 237  TRP A CD2   1 
ATOM   1943 N  NE1   . TRP A 1 247 ? 0.149   1.370   2.251   1.00 21.84 ? 237  TRP A NE1   1 
ATOM   1944 C  CE2   . TRP A 1 247 ? -0.655  0.783   1.313   1.00 22.45 ? 237  TRP A CE2   1 
ATOM   1945 C  CE3   . TRP A 1 247 ? -2.967  0.894   0.604   1.00 22.92 ? 237  TRP A CE3   1 
ATOM   1946 C  CZ2   . TRP A 1 247 ? -0.356  -0.175  0.350   1.00 23.29 ? 237  TRP A CZ2   1 
ATOM   1947 C  CZ3   . TRP A 1 247 ? -2.668  -0.069  -0.347  1.00 23.37 ? 237  TRP A CZ3   1 
ATOM   1948 C  CH2   . TRP A 1 247 ? -1.370  -0.581  -0.474  1.00 23.82 ? 237  TRP A CH2   1 
ATOM   1949 N  N     . ILE A 1 248 ? -4.084  5.992   3.402   1.00 19.40 ? 238  ILE A N     1 
ATOM   1950 C  CA    . ILE A 1 248 ? -4.928  7.018   4.013   1.00 19.05 ? 238  ILE A CA    1 
ATOM   1951 C  C     . ILE A 1 248 ? -5.295  8.126   3.017   1.00 18.80 ? 238  ILE A C     1 
ATOM   1952 O  O     . ILE A 1 248 ? -6.451  8.534   2.939   1.00 19.09 ? 238  ILE A O     1 
ATOM   1953 C  CB    . ILE A 1 248 ? -4.299  7.582   5.307   1.00 19.48 ? 238  ILE A CB    1 
ATOM   1954 C  CG1   . ILE A 1 248 ? -4.254  6.473   6.372   1.00 20.14 ? 238  ILE A CG1   1 
ATOM   1955 C  CG2   . ILE A 1 248 ? -5.127  8.738   5.860   1.00 19.85 ? 238  ILE A CG2   1 
ATOM   1956 C  CD1   . ILE A 1 248 ? -3.419  6.801   7.599   1.00 20.67 ? 238  ILE A CD1   1 
ATOM   1957 N  N     . ASP A 1 249 ? -4.317  8.600   2.243   1.00 18.43 ? 239  ASP A N     1 
ATOM   1958 C  CA    . ASP A 1 249 ? -4.532  9.742   1.355   1.00 18.03 ? 239  ASP A CA    1 
ATOM   1959 C  C     . ASP A 1 249 ? -5.641  9.431   0.356   1.00 17.78 ? 239  ASP A C     1 
ATOM   1960 O  O     . ASP A 1 249 ? -6.615  10.165  0.270   1.00 18.42 ? 239  ASP A O     1 
ATOM   1961 C  CB    . ASP A 1 249 ? -3.225  10.065  0.638   1.00 18.56 ? 239  ASP A CB    1 
ATOM   1962 C  CG    . ASP A 1 249 ? -3.309  11.284  -0.272  1.00 18.77 ? 239  ASP A CG    1 
ATOM   1963 O  OD1   . ASP A 1 249 ? -4.308  12.040  -0.254  1.00 19.50 ? 239  ASP A OD1   1 
ATOM   1964 O  OD2   . ASP A 1 249 ? -2.338  11.489  -1.025  1.00 19.29 ? 239  ASP A OD2   1 
ATOM   1965 N  N     . ALA A 1 250 ? -5.512  8.332   -0.378  1.00 17.24 ? 240  ALA A N     1 
ATOM   1966 C  CA    . ALA A 1 250 ? -6.487  8.027   -1.424  1.00 17.49 ? 240  ALA A CA    1 
ATOM   1967 C  C     . ALA A 1 250 ? -7.852  7.626   -0.869  1.00 17.35 ? 240  ALA A C     1 
ATOM   1968 O  O     . ALA A 1 250 ? -8.871  8.118   -1.338  1.00 18.19 ? 240  ALA A O     1 
ATOM   1969 C  CB    . ALA A 1 250 ? -5.938  6.968   -2.367  1.00 17.75 ? 240  ALA A CB    1 
ATOM   1970 N  N     . LEU A 1 251 ? -7.882  6.758   0.144   1.00 17.17 ? 241  LEU A N     1 
ATOM   1971 C  CA    . LEU A 1 251 ? -9.147  6.218   0.624   1.00 17.69 ? 241  LEU A CA    1 
ATOM   1972 C  C     . LEU A 1 251 ? -10.072 7.268   1.227   1.00 16.93 ? 241  LEU A C     1 
ATOM   1973 O  O     . LEU A 1 251 ? -11.298 7.229   1.004   1.00 17.25 ? 241  LEU A O     1 
ATOM   1974 C  CB    . LEU A 1 251 ? -8.930  5.063   1.605   1.00 17.79 ? 241  LEU A CB    1 
ATOM   1975 C  CG    . LEU A 1 251 ? -8.464  3.726   1.032   1.00 18.53 ? 241  LEU A CG    1 
ATOM   1976 C  CD1   . LEU A 1 251 ? -8.101  2.752   2.144   1.00 19.20 ? 241  LEU A CD1   1 
ATOM   1977 C  CD2   . LEU A 1 251 ? -9.522  3.124   0.131   1.00 19.16 ? 241  LEU A CD2   1 
ATOM   1978 N  N     . VAL A 1 252 ? -9.510  8.268   1.908   1.00 16.43 ? 242  VAL A N     1 
ATOM   1979 C  CA    . VAL A 1 252 ? -10.381 9.279   2.539   1.00 16.09 ? 242  VAL A CA    1 
ATOM   1980 C  C     . VAL A 1 252 ? -11.037 10.255  1.552   1.00 15.96 ? 242  VAL A C     1 
ATOM   1981 O  O     . VAL A 1 252 ? -11.885 11.038  1.964   1.00 16.30 ? 242  VAL A O     1 
ATOM   1982 C  CB    . VAL A 1 252 ? -9.712  10.037  3.698   1.00 16.28 ? 242  VAL A CB    1 
ATOM   1983 C  CG1   . VAL A 1 252 ? -9.215  9.076   4.777   1.00 16.24 ? 242  VAL A CG1   1 
ATOM   1984 C  CG2   . VAL A 1 252 ? -8.631  10.963  3.207   1.00 16.19 ? 242  VAL A CG2   1 
ATOM   1985 N  N     . ASN A 1 253 ? -10.696 10.199  0.253   1.00 15.34 ? 243  ASN A N     1 
ATOM   1986 C  CA    . ASN A 1 253 ? -11.403 11.010  -0.769  1.00 15.50 ? 243  ASN A CA    1 
ATOM   1987 C  C     . ASN A 1 253 ? -12.936 10.853  -0.672  1.00 15.25 ? 243  ASN A C     1 
ATOM   1988 O  O     . ASN A 1 253 ? -13.683 11.819  -0.885  1.00 15.65 ? 243  ASN A O     1 
ATOM   1989 C  CB    . ASN A 1 253 ? -10.926 10.700  -2.202  1.00 15.25 ? 243  ASN A CB    1 
ATOM   1990 C  CG    . ASN A 1 253 ? -11.737 9.616   -2.892  1.00 14.66 ? 243  ASN A CG    1 
ATOM   1991 O  OD1   . ASN A 1 253 ? -12.779 9.889   -3.468  1.00 15.41 ? 243  ASN A OD1   1 
ATOM   1992 N  ND2   . ASN A 1 253 ? -11.282 8.378   -2.804  1.00 15.32 ? 243  ASN A ND2   1 
ATOM   1993 N  N     . TYR A 1 254 ? -13.391 9.638   -0.348  1.00 15.27 ? 244  TYR A N     1 
ATOM   1994 C  CA    . TYR A 1 254 ? -14.815 9.327   -0.343  1.00 15.41 ? 244  TYR A CA    1 
ATOM   1995 C  C     . TYR A 1 254 ? -15.576 10.084  0.741   1.00 15.40 ? 244  TYR A C     1 
ATOM   1996 O  O     . TYR A 1 254 ? -16.797 10.276  0.629   1.00 16.28 ? 244  TYR A O     1 
ATOM   1997 C  CB    . TYR A 1 254 ? -15.040 7.818   -0.183  1.00 15.57 ? 244  TYR A CB    1 
ATOM   1998 C  CG    . TYR A 1 254 ? -14.379 6.926   -1.219  1.00 15.95 ? 244  TYR A CG    1 
ATOM   1999 C  CD1   . TYR A 1 254 ? -13.625 5.811   -0.822  1.00 16.18 ? 244  TYR A CD1   1 
ATOM   2000 C  CD2   . TYR A 1 254 ? -14.552 7.143   -2.582  1.00 15.93 ? 244  TYR A CD2   1 
ATOM   2001 C  CE1   . TYR A 1 254 ? -13.042 4.967   -1.755  1.00 16.15 ? 244  TYR A CE1   1 
ATOM   2002 C  CE2   . TYR A 1 254 ? -13.970 6.308   -3.522  1.00 16.26 ? 244  TYR A CE2   1 
ATOM   2003 C  CZ    . TYR A 1 254 ? -13.218 5.206   -3.106  1.00 16.48 ? 244  TYR A CZ    1 
ATOM   2004 O  OH    . TYR A 1 254 ? -12.637 4.353   -4.047  1.00 17.13 ? 244  TYR A OH    1 
ATOM   2005 N  N     . ILE A 1 255 ? -14.870 10.495  1.787   1.00 15.80 ? 245  ILE A N     1 
ATOM   2006 C  CA    . ILE A 1 255 ? -15.461 11.297  2.882   1.00 16.19 ? 245  ILE A CA    1 
ATOM   2007 C  C     . ILE A 1 255 ? -15.024 12.777  2.850   1.00 16.36 ? 245  ILE A C     1 
ATOM   2008 O  O     . ILE A 1 255 ? -15.826 13.671  3.201   1.00 16.64 ? 245  ILE A O     1 
ATOM   2009 C  CB    . ILE A 1 255 ? -15.288 10.623  4.269   1.00 17.08 ? 245  ILE A CB    1 
ATOM   2010 C  CG1   . ILE A 1 255 ? -13.815 10.434  4.651   1.00 17.29 ? 245  ILE A CG1   1 
ATOM   2011 C  CG2   . ILE A 1 255 ? -16.019 9.282   4.285   1.00 17.78 ? 245  ILE A CG2   1 
ATOM   2012 C  CD1   . ILE A 1 255 ? -13.609 9.853   6.040   1.00 17.59 ? 245  ILE A CD1   1 
ATOM   2013 N  N     . SER A 1 256 ? -13.801 13.059  2.392   1.00 15.85 ? 246  SER A N     1 
ATOM   2014 C  CA    . SER A 1 256 ? -13.357 14.455  2.271   1.00 16.52 ? 246  SER A CA    1 
ATOM   2015 C  C     . SER A 1 256 ? -14.183 15.251  1.250   1.00 16.90 ? 246  SER A C     1 
ATOM   2016 O  O     . SER A 1 256 ? -14.497 16.424  1.495   1.00 18.00 ? 246  SER A O     1 
ATOM   2017 C  CB    . SER A 1 256 ? -11.870 14.530  1.963   1.00 16.76 ? 246  SER A CB    1 
ATOM   2018 O  OG    . SER A 1 256 ? -11.635 14.210  0.618   1.00 16.70 ? 246  SER A OG    1 
ATOM   2019 N  N     . ALA A 1 257 ? -14.587 14.604  0.149   1.00 17.38 ? 247  ALA A N     1 
ATOM   2020 C  CA    . ALA A 1 257 ? -15.437 15.245  -0.870  1.00 17.50 ? 247  ALA A CA    1 
ATOM   2021 C  C     . ALA A 1 257 ? -16.804 15.665  -0.306  1.00 18.27 ? 247  ALA A C     1 
ATOM   2022 O  O     . ALA A 1 257 ? -17.437 16.578  -0.832  1.00 18.56 ? 247  ALA A O     1 
ATOM   2023 C  CB    . ALA A 1 257 ? -15.612 14.326  -2.069  1.00 17.46 ? 247  ALA A CB    1 
ATOM   2024 N  N     . LEU A 1 258 ? -17.251 14.992  0.756   1.00 17.81 ? 248  LEU A N     1 
ATOM   2025 C  CA    . LEU A 1 258 ? -18.518 15.315  1.416   1.00 18.51 ? 248  LEU A CA    1 
ATOM   2026 C  C     . LEU A 1 258 ? -18.390 16.357  2.514   1.00 19.78 ? 248  LEU A C     1 
ATOM   2027 O  O     . LEU A 1 258 ? -19.368 16.632  3.225   1.00 21.54 ? 248  LEU A O     1 
ATOM   2028 C  CB    . LEU A 1 258 ? -19.134 14.047  2.004   1.00 18.18 ? 248  LEU A CB    1 
ATOM   2029 C  CG    . LEU A 1 258 ? -19.335 12.881  1.029   1.00 17.90 ? 248  LEU A CG    1 
ATOM   2030 C  CD1   . LEU A 1 258 ? -19.857 11.679  1.812   1.00 18.07 ? 248  LEU A CD1   1 
ATOM   2031 C  CD2   . LEU A 1 258 ? -20.246 13.226  -0.135  1.00 18.35 ? 248  LEU A CD2   1 
ATOM   2032 N  N     . GLY A 1 259 ? -17.205 16.936  2.679   1.00 19.63 ? 249  GLY A N     1 
ATOM   2033 C  CA    . GLY A 1 259 ? -17.019 17.992  3.680   1.00 20.17 ? 249  GLY A CA    1 
ATOM   2034 C  C     . GLY A 1 259 ? -16.779 17.469  5.087   1.00 20.54 ? 249  GLY A C     1 
ATOM   2035 O  O     . GLY A 1 259 ? -16.930 18.222  6.056   1.00 21.50 ? 249  GLY A O     1 
ATOM   2036 N  N     . TYR A 1 260 ? -16.398 16.195  5.222   1.00 20.95 ? 250  TYR A N     1 
ATOM   2037 C  CA    . TYR A 1 260 ? -16.026 15.625  6.524   1.00 21.58 ? 250  TYR A CA    1 
ATOM   2038 C  C     . TYR A 1 260 ? -14.939 16.494  7.163   1.00 22.46 ? 250  TYR A C     1 
ATOM   2039 O  O     . TYR A 1 260 ? -14.003 16.900  6.486   1.00 21.92 ? 250  TYR A O     1 
ATOM   2040 C  CB    . TYR A 1 260 ? -15.573 14.168  6.370   1.00 21.37 ? 250  TYR A CB    1 
ATOM   2041 C  CG    . TYR A 1 260 ? -15.089 13.481  7.627   1.00 21.56 ? 250  TYR A CG    1 
ATOM   2042 C  CD1   . TYR A 1 260 ? -15.932 13.305  8.732   1.00 22.28 ? 250  TYR A CD1   1 
ATOM   2043 C  CD2   . TYR A 1 260 ? -13.793 12.971  7.706   1.00 21.41 ? 250  TYR A CD2   1 
ATOM   2044 C  CE1   . TYR A 1 260 ? -15.478 12.673  9.886   1.00 22.77 ? 250  TYR A CE1   1 
ATOM   2045 C  CE2   . TYR A 1 260 ? -13.337 12.331  8.858   1.00 21.75 ? 250  TYR A CE2   1 
ATOM   2046 C  CZ    . TYR A 1 260 ? -14.186 12.174  9.935   1.00 22.60 ? 250  TYR A CZ    1 
ATOM   2047 O  OH    . TYR A 1 260 ? -13.723 11.550  11.073  1.00 24.01 ? 250  TYR A OH    1 
ATOM   2048 N  N     . LEU A 1 261 ? -15.137 16.840  8.436   1.00 23.09 ? 251  LEU A N     1 
ATOM   2049 C  CA    . LEU A 1 261 ? -14.211 17.697  9.206   1.00 24.47 ? 251  LEU A CA    1 
ATOM   2050 C  C     . LEU A 1 261 ? -13.981 19.107  8.674   1.00 26.07 ? 251  LEU A C     1 
ATOM   2051 O  O     . LEU A 1 261 ? -12.974 19.741  9.006   1.00 27.92 ? 251  LEU A O     1 
ATOM   2052 C  CB    . LEU A 1 261 ? -12.863 16.981  9.404   1.00 24.23 ? 251  LEU A CB    1 
ATOM   2053 C  CG    . LEU A 1 261 ? -12.945 15.611  10.047  1.00 24.65 ? 251  LEU A CG    1 
ATOM   2054 C  CD1   . LEU A 1 261 ? -11.545 15.027  10.168  1.00 24.43 ? 251  LEU A CD1   1 
ATOM   2055 C  CD2   . LEU A 1 261 ? -13.622 15.659  11.411  1.00 25.12 ? 251  LEU A CD2   1 
ATOM   2056 N  N     . SER A 1 262 ? -14.916 19.609  7.873   1.00 25.75 ? 252  SER A N     1 
ATOM   2057 C  CA    . SER A 1 262 ? -14.862 20.967  7.354   1.00 26.62 ? 252  SER A CA    1 
ATOM   2058 C  C     . SER A 1 262 ? -15.851 21.821  8.148   1.00 27.73 ? 252  SER A C     1 
ATOM   2059 O  O     . SER A 1 262 ? -16.536 21.323  9.035   1.00 27.48 ? 252  SER A O     1 
ATOM   2060 C  CB    . SER A 1 262 ? -15.235 20.977  5.866   1.00 26.57 ? 252  SER A CB    1 
ATOM   2061 O  OG    . SER A 1 262 ? -16.641 20.858  5.669   1.00 25.79 ? 252  SER A OG    1 
ATOM   2062 N  N     . ASP A 1 263 ? -15.951 23.093  7.781   1.00 29.96 ? 253  ASP A N     1 
ATOM   2063 C  CA    . ASP A 1 263 ? -16.986 23.978  8.335   1.00 31.44 ? 253  ASP A CA    1 
ATOM   2064 C  C     . ASP A 1 263 ? -18.421 23.682  7.842   1.00 29.97 ? 253  ASP A C     1 
ATOM   2065 O  O     . ASP A 1 263 ? -19.361 24.321  8.288   1.00 30.99 ? 253  ASP A O     1 
ATOM   2066 C  CB    . ASP A 1 263 ? -16.619 25.465  8.108   1.00 34.40 ? 253  ASP A CB    1 
ATOM   2067 C  CG    . ASP A 1 263 ? -16.554 25.864  6.640   1.00 36.43 ? 253  ASP A CG    1 
ATOM   2068 O  OD1   . ASP A 1 263 ? -16.235 27.045  6.386   1.00 41.07 ? 253  ASP A OD1   1 
ATOM   2069 O  OD2   . ASP A 1 263 ? -16.798 25.032  5.736   1.00 38.47 ? 253  ASP A OD2   1 
ATOM   2070 N  N     . ASP A 1 264 ? -18.591 22.730  6.925   1.00 28.02 ? 254  ASP A N     1 
ATOM   2071 C  CA    . ASP A 1 264 ? -19.915 22.348  6.442   1.00 26.76 ? 254  ASP A CA    1 
ATOM   2072 C  C     . ASP A 1 264 ? -19.923 20.846  6.144   1.00 25.25 ? 254  ASP A C     1 
ATOM   2073 O  O     . ASP A 1 264 ? -19.491 20.421  5.072   1.00 24.20 ? 254  ASP A O     1 
ATOM   2074 C  CB    . ASP A 1 264 ? -20.260 23.169  5.199   1.00 27.37 ? 254  ASP A CB    1 
ATOM   2075 C  CG    . ASP A 1 264 ? -21.545 22.700  4.500   1.00 28.11 ? 254  ASP A CG    1 
ATOM   2076 O  OD1   . ASP A 1 264 ? -22.349 21.937  5.100   1.00 27.07 ? 254  ASP A OD1   1 
ATOM   2077 O  OD2   . ASP A 1 264 ? -21.733 23.115  3.340   1.00 28.02 ? 254  ASP A OD2   1 
ATOM   2078 N  N     . GLU A 1 265 ? -20.412 20.065  7.105   1.00 23.91 ? 255  GLU A N     1 
ATOM   2079 C  CA    . GLU A 1 265 ? -20.489 18.599  6.969   1.00 23.53 ? 255  GLU A CA    1 
ATOM   2080 C  C     . GLU A 1 265 ? -21.859 18.094  6.482   1.00 22.43 ? 255  GLU A C     1 
ATOM   2081 O  O     . GLU A 1 265 ? -22.148 16.903  6.605   1.00 21.96 ? 255  GLU A O     1 
ATOM   2082 C  CB    . GLU A 1 265 ? -20.140 17.924  8.299   1.00 24.52 ? 255  GLU A CB    1 
ATOM   2083 C  CG    . GLU A 1 265 ? -18.706 18.154  8.763   1.00 25.42 ? 255  GLU A CG    1 
ATOM   2084 C  CD    . GLU A 1 265 ? -18.379 17.475  10.083  1.00 26.52 ? 255  GLU A CD    1 
ATOM   2085 O  OE1   . GLU A 1 265 ? -19.138 17.647  11.061  1.00 29.20 ? 255  GLU A OE1   1 
ATOM   2086 O  OE2   . GLU A 1 265 ? -17.345 16.770  10.152  1.00 26.27 ? 255  GLU A OE2   1 
ATOM   2087 N  N     . SER A 1 266 ? -22.695 18.975  5.926   1.00 22.11 ? 256  SER A N     1 
ATOM   2088 C  CA    . SER A 1 266 ? -24.068 18.595  5.564   1.00 22.21 ? 256  SER A CA    1 
ATOM   2089 C  C     . SER A 1 266 ? -24.128 17.461  4.519   1.00 22.05 ? 256  SER A C     1 
ATOM   2090 O  O     . SER A 1 266 ? -24.941 16.542  4.647   1.00 21.94 ? 256  SER A O     1 
ATOM   2091 C  CB    . SER A 1 266 ? -24.886 19.824  5.122   1.00 23.17 ? 256  SER A CB    1 
ATOM   2092 O  OG    . SER A 1 266 ? -24.314 20.434  3.983   1.00 23.37 ? 256  SER A OG    1 
ATOM   2093 N  N     . LEU A 1 267 ? -23.241 17.483  3.525   1.00 20.58 ? 257  LEU A N     1 
ATOM   2094 C  CA    . LEU A 1 267 ? -23.191 16.378  2.558   1.00 20.56 ? 257  LEU A CA    1 
ATOM   2095 C  C     . LEU A 1 267 ? -22.792 15.070  3.228   1.00 19.57 ? 257  LEU A C     1 
ATOM   2096 O  O     . LEU A 1 267 ? -23.379 14.039  2.950   1.00 20.43 ? 257  LEU A O     1 
ATOM   2097 C  CB    . LEU A 1 267 ? -22.248 16.658  1.387   1.00 20.52 ? 257  LEU A CB    1 
ATOM   2098 C  CG    . LEU A 1 267 ? -22.580 17.832  0.464   1.00 21.36 ? 257  LEU A CG    1 
ATOM   2099 C  CD1   . LEU A 1 267 ? -21.428 18.020  -0.503  1.00 21.66 ? 257  LEU A CD1   1 
ATOM   2100 C  CD2   . LEU A 1 267 ? -23.887 17.658  -0.304  1.00 21.67 ? 257  LEU A CD2   1 
ATOM   2101 N  N     . PHE A 1 268 ? -21.797 15.125  4.106   1.00 19.46 ? 258  PHE A N     1 
ATOM   2102 C  CA    . PHE A 1 268 ? -21.331 13.950  4.834   1.00 19.85 ? 258  PHE A CA    1 
ATOM   2103 C  C     . PHE A 1 268 ? -22.451 13.353  5.699   1.00 20.43 ? 258  PHE A C     1 
ATOM   2104 O  O     . PHE A 1 268 ? -22.674 12.154  5.689   1.00 19.93 ? 258  PHE A O     1 
ATOM   2105 C  CB    . PHE A 1 268 ? -20.113 14.317  5.692   1.00 19.99 ? 258  PHE A CB    1 
ATOM   2106 C  CG    . PHE A 1 268 ? -19.621 13.188  6.541   1.00 20.26 ? 258  PHE A CG    1 
ATOM   2107 C  CD1   . PHE A 1 268 ? -18.822 12.192  5.989   1.00 20.72 ? 258  PHE A CD1   1 
ATOM   2108 C  CD2   . PHE A 1 268 ? -19.998 13.084  7.884   1.00 21.43 ? 258  PHE A CD2   1 
ATOM   2109 C  CE1   . PHE A 1 268 ? -18.384 11.133  6.763   1.00 20.54 ? 258  PHE A CE1   1 
ATOM   2110 C  CE2   . PHE A 1 268 ? -19.556 12.023  8.659   1.00 21.43 ? 258  PHE A CE2   1 
ATOM   2111 C  CZ    . PHE A 1 268 ? -18.753 11.054  8.097   1.00 21.29 ? 258  PHE A CZ    1 
ATOM   2112 N  N     . ASN A 1 269 ? -23.142 14.213  6.434   1.00 20.80 ? 259  ASN A N     1 
ATOM   2113 C  CA    . ASN A 1 269 ? -24.265 13.801  7.291   1.00 21.66 ? 259  ASN A CA    1 
ATOM   2114 C  C     . ASN A 1 269 ? -25.427 13.152  6.518   1.00 22.47 ? 259  ASN A C     1 
ATOM   2115 O  O     . ASN A 1 269 ? -26.168 12.333  7.064   1.00 23.50 ? 259  ASN A O     1 
ATOM   2116 C  CB    . ASN A 1 269 ? -24.772 15.016  8.076   1.00 22.42 ? 259  ASN A CB    1 
ATOM   2117 C  CG    . ASN A 1 269 ? -23.775 15.509  9.121   1.00 22.76 ? 259  ASN A CG    1 
ATOM   2118 O  OD1   . ASN A 1 269 ? -22.906 14.754  9.588   1.00 23.44 ? 259  ASN A OD1   1 
ATOM   2119 N  ND2   . ASN A 1 269 ? -23.904 16.784  9.512   1.00 22.77 ? 259  ASN A ND2   1 
ATOM   2120 N  N     . LYS A 1 270 ? -25.581 13.529  5.255   1.00 22.10 ? 260  LYS A N     1 
ATOM   2121 C  CA    . LYS A 1 270 ? -26.626 12.977  4.390   1.00 23.54 ? 260  LYS A CA    1 
ATOM   2122 C  C     . LYS A 1 270 ? -26.247 11.687  3.686   1.00 22.36 ? 260  LYS A C     1 
ATOM   2123 O  O     . LYS A 1 270 ? -27.020 10.736  3.683   1.00 22.89 ? 260  LYS A O     1 
ATOM   2124 C  CB    . LYS A 1 270 ? -26.999 13.992  3.314   1.00 25.85 ? 260  LYS A CB    1 
ATOM   2125 C  CG    . LYS A 1 270 ? -28.219 14.823  3.628   1.00 28.58 ? 260  LYS A CG    1 
ATOM   2126 C  CD    . LYS A 1 270 ? -28.569 15.714  2.442   1.00 29.06 ? 260  LYS A CD    1 
ATOM   2127 C  CE    . LYS A 1 270 ? -29.224 14.950  1.306   1.00 29.37 ? 260  LYS A CE    1 
ATOM   2128 N  NZ    . LYS A 1 270 ? -29.875 15.871  0.325   1.00 29.97 ? 260  LYS A NZ    1 
ATOM   2129 N  N     . TYR A 1 271 ? -25.074 11.685  3.041   1.00 20.29 ? 261  TYR A N     1 
ATOM   2130 C  CA    . TYR A 1 271 ? -24.711 10.622  2.102   1.00 19.53 ? 261  TYR A CA    1 
ATOM   2131 C  C     . TYR A 1 271 ? -23.862 9.500   2.663   1.00 19.31 ? 261  TYR A C     1 
ATOM   2132 O  O     . TYR A 1 271 ? -23.963 8.374   2.172   1.00 18.88 ? 261  TYR A O     1 
ATOM   2133 C  CB    . TYR A 1 271 ? -24.059 11.224  0.839   1.00 19.51 ? 261  TYR A CB    1 
ATOM   2134 C  CG    . TYR A 1 271 ? -25.033 12.104  0.063   1.00 19.34 ? 261  TYR A CG    1 
ATOM   2135 C  CD1   . TYR A 1 271 ? -24.929 13.498  0.089   1.00 19.57 ? 261  TYR A CD1   1 
ATOM   2136 C  CD2   . TYR A 1 271 ? -26.069 11.551  -0.675  1.00 19.47 ? 261  TYR A CD2   1 
ATOM   2137 C  CE1   . TYR A 1 271 ? -25.815 14.294  -0.618  1.00 20.26 ? 261  TYR A CE1   1 
ATOM   2138 C  CE2   . TYR A 1 271 ? -26.969 12.345  -1.374  1.00 19.73 ? 261  TYR A CE2   1 
ATOM   2139 C  CZ    . TYR A 1 271 ? -26.833 13.718  -1.329  1.00 20.21 ? 261  TYR A CZ    1 
ATOM   2140 O  OH    . TYR A 1 271 ? -27.718 14.505  -2.016  1.00 21.28 ? 261  TYR A OH    1 
ATOM   2141 N  N     . TRP A 1 272 ? -23.035 9.784   3.669   1.00 18.53 ? 262  TRP A N     1 
ATOM   2142 C  CA    . TRP A 1 272 ? -22.162 8.756   4.245   1.00 18.87 ? 262  TRP A CA    1 
ATOM   2143 C  C     . TRP A 1 272 ? -23.019 7.876   5.179   1.00 19.14 ? 262  TRP A C     1 
ATOM   2144 O  O     . TRP A 1 272 ? -23.764 8.427   5.988   1.00 19.26 ? 262  TRP A O     1 
ATOM   2145 C  CB    . TRP A 1 272 ? -20.941 9.356   4.989   1.00 18.58 ? 262  TRP A CB    1 
ATOM   2146 C  CG    . TRP A 1 272 ? -20.004 8.237   5.298   1.00 18.55 ? 262  TRP A CG    1 
ATOM   2147 C  CD1   . TRP A 1 272 ? -19.845 7.606   6.488   1.00 18.84 ? 262  TRP A CD1   1 
ATOM   2148 C  CD2   . TRP A 1 272 ? -19.207 7.516   4.347   1.00 17.88 ? 262  TRP A CD2   1 
ATOM   2149 N  NE1   . TRP A 1 272 ? -18.990 6.539   6.352   1.00 18.96 ? 262  TRP A NE1   1 
ATOM   2150 C  CE2   . TRP A 1 272 ? -18.578 6.464   5.048   1.00 18.31 ? 262  TRP A CE2   1 
ATOM   2151 C  CE3   . TRP A 1 272 ? -18.982 7.652   2.970   1.00 17.55 ? 262  TRP A CE3   1 
ATOM   2152 C  CZ2   . TRP A 1 272 ? -17.736 5.552   4.426   1.00 18.25 ? 262  TRP A CZ2   1 
ATOM   2153 C  CZ3   . TRP A 1 272 ? -18.122 6.768   2.353   1.00 17.71 ? 262  TRP A CZ3   1 
ATOM   2154 C  CH2   . TRP A 1 272 ? -17.522 5.712   3.075   1.00 18.00 ? 262  TRP A CH2   1 
ATOM   2155 N  N     . PRO A 1 273 ? -22.952 6.535   5.108   1.00 19.14 ? 263  PRO A N     1 
ATOM   2156 C  CA    . PRO A 1 273 ? -22.007 5.730   4.311   1.00 18.73 ? 263  PRO A CA    1 
ATOM   2157 C  C     . PRO A 1 273 ? -22.405 5.457   2.866   1.00 18.51 ? 263  PRO A C     1 
ATOM   2158 O  O     . PRO A 1 273 ? -23.599 5.348   2.528   1.00 18.56 ? 263  PRO A O     1 
ATOM   2159 C  CB    . PRO A 1 273 ? -21.935 4.412   5.096   1.00 19.16 ? 263  PRO A CB    1 
ATOM   2160 C  CG    . PRO A 1 273 ? -23.305 4.297   5.700   1.00 19.33 ? 263  PRO A CG    1 
ATOM   2161 C  CD    . PRO A 1 273 ? -23.707 5.703   6.059   1.00 19.63 ? 263  PRO A CD    1 
ATOM   2162 N  N     . ALA A 1 274 ? -21.386 5.281   2.022   1.00 18.10 ? 264  ALA A N     1 
ATOM   2163 C  CA    . ALA A 1 274 ? -21.579 4.970   0.623   1.00 17.93 ? 264  ALA A CA    1 
ATOM   2164 C  C     . ALA A 1 274 ? -22.398 3.694   0.458   1.00 18.67 ? 264  ALA A C     1 
ATOM   2165 O  O     . ALA A 1 274 ? -22.217 2.721   1.180   1.00 19.05 ? 264  ALA A O     1 
ATOM   2166 C  CB    . ALA A 1 274 ? -20.246 4.813   -0.087  1.00 18.07 ? 264  ALA A CB    1 
ATOM   2167 N  N     . ASP A 1 275 ? -23.306 3.730   -0.500  1.00 18.93 ? 265  ASP A N     1 
ATOM   2168 C  CA    . ASP A 1 275 ? -24.080 2.559   -0.867  1.00 19.75 ? 265  ASP A CA    1 
ATOM   2169 C  C     . ASP A 1 275 ? -23.245 1.620   -1.712  1.00 19.63 ? 265  ASP A C     1 
ATOM   2170 O  O     . ASP A 1 275 ? -23.319 0.416   -1.533  1.00 19.58 ? 265  ASP A O     1 
ATOM   2171 C  CB    . ASP A 1 275 ? -25.341 2.968   -1.610  1.00 20.42 ? 265  ASP A CB    1 
ATOM   2172 C  CG    . ASP A 1 275 ? -26.296 3.708   -0.719  1.00 21.34 ? 265  ASP A CG    1 
ATOM   2173 O  OD1   . ASP A 1 275 ? -27.128 3.026   -0.078  1.00 22.96 ? 265  ASP A OD1   1 
ATOM   2174 O  OD2   . ASP A 1 275 ? -26.143 4.951   -0.569  1.00 20.61 ? 265  ASP A OD2   1 
ATOM   2175 N  N     . ILE A 1 276 ? -22.475 2.178   -2.646  1.00 19.12 ? 266  ILE A N     1 
ATOM   2176 C  CA    . ILE A 1 276 ? -21.597 1.385   -3.514  1.00 19.44 ? 266  ILE A CA    1 
ATOM   2177 C  C     . ILE A 1 276 ? -20.297 2.116   -3.779  1.00 18.76 ? 266  ILE A C     1 
ATOM   2178 O  O     . ILE A 1 276 ? -20.319 3.261   -4.230  1.00 18.75 ? 266  ILE A O     1 
ATOM   2179 C  CB    . ILE A 1 276 ? -22.227 1.059   -4.886  1.00 19.88 ? 266  ILE A CB    1 
ATOM   2180 C  CG1   . ILE A 1 276 ? -23.492 0.211   -4.719  1.00 20.54 ? 266  ILE A CG1   1 
ATOM   2181 C  CG2   . ILE A 1 276 ? -21.203 0.335   -5.766  1.00 20.54 ? 266  ILE A CG2   1 
ATOM   2182 C  CD1   . ILE A 1 276 ? -24.186 -0.124  -6.025  1.00 21.03 ? 266  ILE A CD1   1 
ATOM   2183 N  N     . HIS A 1 277 ? -19.178 1.440   -3.496  1.00 18.43 ? 267  HIS A N     1 
ATOM   2184 C  CA    . HIS A 1 277 ? -17.873 1.796   -4.033  1.00 18.34 ? 267  HIS A CA    1 
ATOM   2185 C  C     . HIS A 1 277 ? -17.594 0.866   -5.220  1.00 18.90 ? 267  HIS A C     1 
ATOM   2186 O  O     . HIS A 1 277 ? -17.559 -0.366  -5.064  1.00 19.36 ? 267  HIS A O     1 
ATOM   2187 C  CB    . HIS A 1 277 ? -16.744 1.615   -3.005  1.00 17.90 ? 267  HIS A CB    1 
ATOM   2188 C  CG    . HIS A 1 277 ? -16.789 2.549   -1.835  1.00 17.86 ? 267  HIS A CG    1 
ATOM   2189 N  ND1   . HIS A 1 277 ? -16.842 3.920   -1.963  1.00 17.01 ? 267  HIS A ND1   1 
ATOM   2190 C  CD2   . HIS A 1 277 ? -16.688 2.301   -0.506  1.00 17.57 ? 267  HIS A CD2   1 
ATOM   2191 C  CE1   . HIS A 1 277 ? -16.797 4.474   -0.761  1.00 17.26 ? 267  HIS A CE1   1 
ATOM   2192 N  NE2   . HIS A 1 277 ? -16.732 3.510   0.142   1.00 17.68 ? 267  HIS A NE2   1 
ATOM   2193 N  N     . LEU A 1 278 ? -17.407 1.439   -6.400  1.00 18.82 ? 268  LEU A N     1 
ATOM   2194 C  CA    . LEU A 1 278 ? -17.143 0.662   -7.605  1.00 19.94 ? 268  LEU A CA    1 
ATOM   2195 C  C     . LEU A 1 278 ? -15.647 0.693   -7.925  1.00 19.22 ? 268  LEU A C     1 
ATOM   2196 O  O     . LEU A 1 278 ? -14.982 1.689   -7.688  1.00 18.64 ? 268  LEU A O     1 
ATOM   2197 C  CB    . LEU A 1 278 ? -17.960 1.257   -8.746  1.00 21.24 ? 268  LEU A CB    1 
ATOM   2198 C  CG    . LEU A 1 278 ? -17.865 0.629   -10.133 1.00 22.84 ? 268  LEU A CG    1 
ATOM   2199 C  CD1   . LEU A 1 278 ? -19.218 0.705   -10.850 1.00 24.17 ? 268  LEU A CD1   1 
ATOM   2200 C  CD2   . LEU A 1 278 ? -16.771 1.291   -10.957 1.00 23.18 ? 268  LEU A CD2   1 
ATOM   2201 N  N     . MET A 1 279 ? -15.129 -0.402  -8.481  1.00 18.89 ? 269  MET A N     1 
ATOM   2202 C  CA    . MET A 1 279 ? -13.718 -0.513  -8.857  1.00 19.58 ? 269  MET A CA    1 
ATOM   2203 C  C     . MET A 1 279 ? -13.503 -1.769  -9.691  1.00 20.42 ? 269  MET A C     1 
ATOM   2204 O  O     . MET A 1 279 ? -14.379 -2.622  -9.755  1.00 21.19 ? 269  MET A O     1 
ATOM   2205 C  CB    . MET A 1 279 ? -12.849 -0.642  -7.603  1.00 19.35 ? 269  MET A CB    1 
ATOM   2206 C  CG    . MET A 1 279 ? -13.155 -1.900  -6.776  1.00 20.12 ? 269  MET A CG    1 
ATOM   2207 S  SD    . MET A 1 279 ? -12.904 -1.728  -5.007  1.00 20.80 ? 269  MET A SD    1 
ATOM   2208 C  CE    . MET A 1 279 ? -14.218 -0.556  -4.635  1.00 20.42 ? 269  MET A CE    1 
ATOM   2209 N  N     . ALA A 1 280 ? -12.315 -1.913  -10.255 1.00 21.36 ? 270  ALA A N     1 
ATOM   2210 C  CA    . ALA A 1 280 ? -11.890 -3.209  -10.777 1.00 22.31 ? 270  ALA A CA    1 
ATOM   2211 C  C     . ALA A 1 280 ? -11.298 -4.081  -9.688  1.00 23.36 ? 270  ALA A C     1 
ATOM   2212 O  O     . ALA A 1 280 ? -10.936 -3.619  -8.603  1.00 22.90 ? 270  ALA A O     1 
ATOM   2213 C  CB    . ALA A 1 280 ? -10.904 -3.052  -11.919 1.00 22.70 ? 270  ALA A CB    1 
ATOM   2214 N  N     . LYS A 1 281 ? -11.190 -5.361  -10.006 1.00 24.70 ? 271  LYS A N     1 
ATOM   2215 C  CA    . LYS A 1 281 ? -10.852 -6.380  -9.018  1.00 27.02 ? 271  LYS A CA    1 
ATOM   2216 C  C     . LYS A 1 281 ? -9.549  -6.209  -8.219  1.00 26.94 ? 271  LYS A C     1 
ATOM   2217 O  O     . LYS A 1 281 ? -9.485  -6.652  -7.077  1.00 27.58 ? 271  LYS A O     1 
ATOM   2218 C  CB    . LYS A 1 281 ? -10.894 -7.772  -9.665  1.00 28.55 ? 271  LYS A CB    1 
ATOM   2219 C  CG    . LYS A 1 281 ? -9.900  -7.986  -10.794 1.00 29.59 ? 271  LYS A CG    1 
ATOM   2220 C  CD    . LYS A 1 281 ? -10.128 -9.345  -11.446 1.00 31.38 ? 271  LYS A CD    1 
ATOM   2221 C  CE    . LYS A 1 281 ? -9.560  -9.385  -12.847 1.00 32.78 ? 271  LYS A CE    1 
ATOM   2222 N  NZ    . LYS A 1 281 ? -9.564  -10.773 -13.391 1.00 33.84 ? 271  LYS A NZ    1 
ATOM   2223 N  N     A GLU A 1 282 ? -8.542  -5.562  -8.803  0.50 27.57 ? 272  GLU A N     1 
ATOM   2224 N  N     B GLU A 1 282 ? -8.546  -5.557  -8.805  0.50 27.42 ? 272  GLU A N     1 
ATOM   2225 C  CA    A GLU A 1 282 ? -7.210  -5.487  -8.181  0.50 27.97 ? 272  GLU A CA    1 
ATOM   2226 C  CA    B GLU A 1 282 ? -7.211  -5.475  -8.191  0.50 27.73 ? 272  GLU A CA    1 
ATOM   2227 C  C     A GLU A 1 282 ? -7.123  -4.596  -6.927  0.50 27.09 ? 272  GLU A C     1 
ATOM   2228 C  C     B GLU A 1 282 ? -7.125  -4.598  -6.929  0.50 26.96 ? 272  GLU A C     1 
ATOM   2229 O  O     A GLU A 1 282 ? -6.167  -4.715  -6.157  0.50 27.47 ? 272  GLU A O     1 
ATOM   2230 O  O     B GLU A 1 282 ? -6.174  -4.728  -6.155  0.50 27.36 ? 272  GLU A O     1 
ATOM   2231 C  CB    A GLU A 1 282 ? -6.131  -5.103  -9.214  0.50 29.12 ? 272  GLU A CB    1 
ATOM   2232 C  CB    B GLU A 1 282 ? -6.151  -5.058  -9.232  0.50 28.65 ? 272  GLU A CB    1 
ATOM   2233 C  CG    A GLU A 1 282 ? -6.041  -3.635  -9.596  0.50 29.96 ? 272  GLU A CG    1 
ATOM   2234 C  CG    B GLU A 1 282 ? -6.034  -3.570  -9.530  0.50 29.29 ? 272  GLU A CG    1 
ATOM   2235 C  CD    A GLU A 1 282 ? -7.194  -3.171  -10.472 0.50 31.14 ? 272  GLU A CD    1 
ATOM   2236 C  CD    B GLU A 1 282 ? -7.270  -2.987  -10.202 0.50 30.26 ? 272  GLU A CD    1 
ATOM   2237 O  OE1   A GLU A 1 282 ? -7.366  -1.933  -10.619 0.50 32.05 ? 272  GLU A OE1   1 
ATOM   2238 O  OE1   B GLU A 1 282 ? -7.953  -3.747  -10.936 0.50 31.18 ? 272  GLU A OE1   1 
ATOM   2239 O  OE2   A GLU A 1 282 ? -7.935  -4.044  -10.994 0.50 31.68 ? 272  GLU A OE2   1 
ATOM   2240 O  OE2   B GLU A 1 282 ? -7.558  -1.773  -9.983  0.50 29.46 ? 272  GLU A OE2   1 
ATOM   2241 N  N     . ILE A 1 283 ? -8.113  -3.730  -6.714  1.00 25.72 ? 273  ILE A N     1 
ATOM   2242 C  CA    . ILE A 1 283 ? -8.146  -2.880  -5.513  1.00 24.51 ? 273  ILE A CA    1 
ATOM   2243 C  C     . ILE A 1 283 ? -9.279  -3.221  -4.540  1.00 23.59 ? 273  ILE A C     1 
ATOM   2244 O  O     . ILE A 1 283 ? -9.490  -2.495  -3.577  1.00 22.04 ? 273  ILE A O     1 
ATOM   2245 C  CB    . ILE A 1 283 ? -8.088  -1.368  -5.852  1.00 23.62 ? 273  ILE A CB    1 
ATOM   2246 C  CG1   . ILE A 1 283 ? -9.315  -0.898  -6.655  1.00 23.28 ? 273  ILE A CG1   1 
ATOM   2247 C  CG2   . ILE A 1 283 ? -6.793  -1.069  -6.590  1.00 24.13 ? 273  ILE A CG2   1 
ATOM   2248 C  CD1   . ILE A 1 283 ? -9.283  0.587   -6.998  1.00 22.45 ? 273  ILE A CD1   1 
ATOM   2249 N  N     . VAL A 1 284 ? -9.935  -4.371  -4.740  1.00 23.96 ? 274  VAL A N     1 
ATOM   2250 C  CA    . VAL A 1 284 ? -10.949 -4.849  -3.790  1.00 24.87 ? 274  VAL A CA    1 
ATOM   2251 C  C     . VAL A 1 284 ? -10.383 -5.062  -2.399  1.00 24.72 ? 274  VAL A C     1 
ATOM   2252 O  O     . VAL A 1 284 ? -11.031 -4.716  -1.411  1.00 23.04 ? 274  VAL A O     1 
ATOM   2253 C  CB    . VAL A 1 284 ? -11.621 -6.162  -4.225  1.00 26.90 ? 274  VAL A CB    1 
ATOM   2254 C  CG1   . VAL A 1 284 ? -12.547 -6.721  -3.132  1.00 27.79 ? 274  VAL A CG1   1 
ATOM   2255 C  CG2   . VAL A 1 284 ? -12.430 -5.907  -5.453  1.00 27.75 ? 274  VAL A CG2   1 
ATOM   2256 N  N     . ARG A 1 285 ? -9.197  -5.652  -2.324  1.00 25.54 ? 275  ARG A N     1 
ATOM   2257 C  CA    . ARG A 1 285 ? -8.577  -5.912  -1.027  1.00 27.83 ? 275  ARG A CA    1 
ATOM   2258 C  C     . ARG A 1 285 ? -8.417  -4.636  -0.211  1.00 25.96 ? 275  ARG A C     1 
ATOM   2259 O  O     . ARG A 1 285 ? -8.684  -4.629  0.985   1.00 25.79 ? 275  ARG A O     1 
ATOM   2260 C  CB    . ARG A 1 285 ? -7.246  -6.659  -1.169  1.00 31.21 ? 275  ARG A CB    1 
ATOM   2261 C  CG    . ARG A 1 285 ? -6.170  -5.913  -1.937  1.00 34.11 ? 275  ARG A CG    1 
ATOM   2262 C  CD    . ARG A 1 285 ? -4.950  -6.783  -2.196  1.00 37.90 ? 275  ARG A CD    1 
ATOM   2263 N  NE    . ARG A 1 285 ? -4.128  -6.924  -0.990  1.00 40.39 ? 275  ARG A NE    1 
ATOM   2264 C  CZ    . ARG A 1 285 ? -2.887  -7.405  -0.972  1.00 43.09 ? 275  ARG A CZ    1 
ATOM   2265 N  NH1   . ARG A 1 285 ? -2.230  -7.478  0.181   1.00 44.04 ? 275  ARG A NH1   1 
ATOM   2266 N  NH2   . ARG A 1 285 ? -2.297  -7.819  -2.096  1.00 44.23 ? 275  ARG A NH2   1 
ATOM   2267 N  N     . PHE A 1 286 ? -8.025  -3.551  -0.870  1.00 23.99 ? 276  PHE A N     1 
ATOM   2268 C  CA    . PHE A 1 286 ? -7.802  -2.280  -0.176  1.00 23.27 ? 276  PHE A CA    1 
ATOM   2269 C  C     . PHE A 1 286 ? -9.115  -1.672  0.305   1.00 21.76 ? 276  PHE A C     1 
ATOM   2270 O  O     . PHE A 1 286 ? -9.190  -1.118  1.412   1.00 22.40 ? 276  PHE A O     1 
ATOM   2271 C  CB    . PHE A 1 286 ? -7.009  -1.308  -1.058  1.00 24.00 ? 276  PHE A CB    1 
ATOM   2272 C  CG    . PHE A 1 286 ? -5.764  -1.926  -1.663  1.00 25.07 ? 276  PHE A CG    1 
ATOM   2273 C  CD1   . PHE A 1 286 ? -4.885  -2.676  -0.876  1.00 26.30 ? 276  PHE A CD1   1 
ATOM   2274 C  CD2   . PHE A 1 286 ? -5.494  -1.795  -3.013  1.00 26.01 ? 276  PHE A CD2   1 
ATOM   2275 C  CE1   . PHE A 1 286 ? -3.754  -3.264  -1.428  1.00 26.55 ? 276  PHE A CE1   1 
ATOM   2276 C  CE2   . PHE A 1 286 ? -4.359  -2.375  -3.576  1.00 26.63 ? 276  PHE A CE2   1 
ATOM   2277 C  CZ    . PHE A 1 286 ? -3.494  -3.117  -2.784  1.00 26.81 ? 276  PHE A CZ    1 
ATOM   2278 N  N     . HIS A 1 287 ? -10.156 -1.799  -0.508  1.00 20.94 ? 277  HIS A N     1 
ATOM   2279 C  CA    . HIS A 1 287 ? -11.488 -1.313  -0.149  1.00 21.01 ? 277  HIS A CA    1 
ATOM   2280 C  C     . HIS A 1 287 ? -12.285 -2.172  0.810   1.00 21.04 ? 277  HIS A C     1 
ATOM   2281 O  O     . HIS A 1 287 ? -13.215 -1.681  1.454   1.00 20.93 ? 277  HIS A O     1 
ATOM   2282 C  CB    . HIS A 1 287 ? -12.320 -1.095  -1.410  1.00 20.53 ? 277  HIS A CB    1 
ATOM   2283 C  CG    . HIS A 1 287 ? -11.903 0.110   -2.178  1.00 19.86 ? 277  HIS A CG    1 
ATOM   2284 N  ND1   . HIS A 1 287 ? -10.805 0.116   -3.006  1.00 19.99 ? 277  HIS A ND1   1 
ATOM   2285 C  CD2   . HIS A 1 287 ? -12.416 1.363   -2.217  1.00 20.06 ? 277  HIS A CD2   1 
ATOM   2286 C  CE1   . HIS A 1 287 ? -10.672 1.318   -3.540  1.00 19.85 ? 277  HIS A CE1   1 
ATOM   2287 N  NE2   . HIS A 1 287 ? -11.634 2.092   -3.074  1.00 19.39 ? 277  HIS A NE2   1 
ATOM   2288 N  N     . SER A 1 288 ? -11.958 -3.455  0.879   1.00 21.55 ? 278  SER A N     1 
ATOM   2289 C  CA    . SER A 1 288 ? -12.723 -4.379  1.707   1.00 22.63 ? 278  SER A CA    1 
ATOM   2290 C  C     . SER A 1 288 ? -12.032 -4.755  3.021   1.00 22.46 ? 278  SER A C     1 
ATOM   2291 O  O     . SER A 1 288 ? -12.681 -5.322  3.891   1.00 22.69 ? 278  SER A O     1 
ATOM   2292 C  CB    . SER A 1 288 ? -13.080 -5.622  0.897   1.00 23.69 ? 278  SER A CB    1 
ATOM   2293 O  OG    . SER A 1 288 ? -11.948 -6.426  0.641   1.00 26.16 ? 278  SER A OG    1 
ATOM   2294 N  N     . ILE A 1 289 ? -10.743 -4.435  3.155   1.00 22.05 ? 279  ILE A N     1 
ATOM   2295 C  CA    . ILE A 1 289 ? -9.980  -4.674  4.387   1.00 22.05 ? 279  ILE A CA    1 
ATOM   2296 C  C     . ILE A 1 289 ? -9.483  -3.359  4.997   1.00 21.71 ? 279  ILE A C     1 
ATOM   2297 O  O     . ILE A 1 289 ? -9.918  -2.982  6.090   1.00 22.48 ? 279  ILE A O     1 
ATOM   2298 C  CB    . ILE A 1 289 ? -8.812  -5.650  4.149   1.00 22.70 ? 279  ILE A CB    1 
ATOM   2299 C  CG1   . ILE A 1 289 ? -9.363  -7.009  3.679   1.00 23.35 ? 279  ILE A CG1   1 
ATOM   2300 C  CG2   . ILE A 1 289 ? -7.969  -5.804  5.412   1.00 22.91 ? 279  ILE A CG2   1 
ATOM   2301 C  CD1   . ILE A 1 289 ? -8.325  -7.953  3.103   1.00 23.83 ? 279  ILE A CD1   1 
ATOM   2302 N  N     . ILE A 1 290 ? -8.600  -2.651  4.292   1.00 20.98 ? 280  ILE A N     1 
ATOM   2303 C  CA    . ILE A 1 290 ? -7.977  -1.432  4.844   1.00 20.20 ? 280  ILE A CA    1 
ATOM   2304 C  C     . ILE A 1 290 ? -9.022  -0.359  5.120   1.00 19.13 ? 280  ILE A C     1 
ATOM   2305 O  O     . ILE A 1 290 ? -9.034  0.230   6.202   1.00 18.82 ? 280  ILE A O     1 
ATOM   2306 C  CB    . ILE A 1 290 ? -6.873  -0.848  3.927   1.00 20.71 ? 280  ILE A CB    1 
ATOM   2307 C  CG1   . ILE A 1 290 ? -5.739  -1.857  3.746   1.00 21.27 ? 280  ILE A CG1   1 
ATOM   2308 C  CG2   . ILE A 1 290 ? -6.299  0.456   4.502   1.00 20.26 ? 280  ILE A CG2   1 
ATOM   2309 C  CD1   . ILE A 1 290 ? -4.710  -1.448  2.711   1.00 21.97 ? 280  ILE A CD1   1 
ATOM   2310 N  N     . TRP A 1 291 ? -9.902  -0.122  4.152   1.00 18.15 ? 281  TRP A N     1 
ATOM   2311 C  CA    . TRP A 1 291 ? -10.875 0.958   4.259   1.00 18.09 ? 281  TRP A CA    1 
ATOM   2312 C  C     . TRP A 1 291 ? -11.855 0.759   5.425   1.00 18.62 ? 281  TRP A C     1 
ATOM   2313 O  O     . TRP A 1 291 ? -11.992 1.670   6.248   1.00 18.85 ? 281  TRP A O     1 
ATOM   2314 C  CB    . TRP A 1 291 ? -11.570 1.154   2.910   1.00 17.39 ? 281  TRP A CB    1 
ATOM   2315 C  CG    . TRP A 1 291 ? -12.612 2.255   2.790   1.00 16.55 ? 281  TRP A CG    1 
ATOM   2316 C  CD1   . TRP A 1 291 ? -13.786 2.156   2.122   1.00 17.17 ? 281  TRP A CD1   1 
ATOM   2317 C  CD2   . TRP A 1 291 ? -12.548 3.607   3.279   1.00 16.56 ? 281  TRP A CD2   1 
ATOM   2318 N  NE1   . TRP A 1 291 ? -14.457 3.350   2.150   1.00 16.93 ? 281  TRP A NE1   1 
ATOM   2319 C  CE2   . TRP A 1 291 ? -13.732 4.260   2.854   1.00 15.96 ? 281  TRP A CE2   1 
ATOM   2320 C  CE3   . TRP A 1 291 ? -11.613 4.336   4.018   1.00 16.14 ? 281  TRP A CE3   1 
ATOM   2321 C  CZ2   . TRP A 1 291 ? -14.002 5.597   3.154   1.00 15.80 ? 281  TRP A CZ2   1 
ATOM   2322 C  CZ3   . TRP A 1 291 ? -11.890 5.671   4.322   1.00 15.96 ? 281  TRP A CZ3   1 
ATOM   2323 C  CH2   . TRP A 1 291 ? -13.066 6.285   3.880   1.00 15.80 ? 281  TRP A CH2   1 
ATOM   2324 N  N     . PRO A 1 292 ? -12.494 -0.426  5.544   1.00 19.85 ? 282  PRO A N     1 
ATOM   2325 C  CA    . PRO A 1 292 ? -13.329 -0.601  6.743   1.00 20.42 ? 282  PRO A CA    1 
ATOM   2326 C  C     . PRO A 1 292 ? -12.547 -0.484  8.062   1.00 20.16 ? 282  PRO A C     1 
ATOM   2327 O  O     . PRO A 1 292 ? -13.066 0.065   9.033   1.00 19.78 ? 282  PRO A O     1 
ATOM   2328 C  CB    . PRO A 1 292 ? -13.930 -2.005  6.590   1.00 21.24 ? 282  PRO A CB    1 
ATOM   2329 C  CG    . PRO A 1 292 ? -13.304 -2.607  5.386   1.00 21.88 ? 282  PRO A CG    1 
ATOM   2330 C  CD    . PRO A 1 292 ? -12.633 -1.536  4.591   1.00 20.33 ? 282  PRO A CD    1 
ATOM   2331 N  N     . ILE A 1 293 ? -11.303 -0.952  8.087   1.00 19.76 ? 283  ILE A N     1 
ATOM   2332 C  CA    . ILE A 1 293 ? -10.512 -0.855  9.322   1.00 20.15 ? 283  ILE A CA    1 
ATOM   2333 C  C     . ILE A 1 293 ? -10.211 0.612   9.681   1.00 19.73 ? 283  ILE A C     1 
ATOM   2334 O  O     . ILE A 1 293 ? -10.347 1.028   10.840  1.00 18.84 ? 283  ILE A O     1 
ATOM   2335 C  CB    . ILE A 1 293 ? -9.240  -1.731  9.245   1.00 20.54 ? 283  ILE A CB    1 
ATOM   2336 C  CG1   . ILE A 1 293 ? -9.662  -3.206  9.318   1.00 21.34 ? 283  ILE A CG1   1 
ATOM   2337 C  CG2   . ILE A 1 293 ? -8.274  -1.392  10.369  1.00 20.77 ? 283  ILE A CG2   1 
ATOM   2338 C  CD1   . ILE A 1 293 ? -8.545  -4.210  9.108   1.00 21.77 ? 283  ILE A CD1   1 
ATOM   2339 N  N     . LEU A 1 294 ? -9.817  1.399   8.682   1.00 19.52 ? 284  LEU A N     1 
ATOM   2340 C  CA    . LEU A 1 294 ? -9.619  2.837   8.865   1.00 19.06 ? 284  LEU A CA    1 
ATOM   2341 C  C     . LEU A 1 294 ? -10.887 3.514   9.415   1.00 19.15 ? 284  LEU A C     1 
ATOM   2342 O  O     . LEU A 1 294 ? -10.815 4.337   10.328  1.00 19.11 ? 284  LEU A O     1 
ATOM   2343 C  CB    . LEU A 1 294 ? -9.162  3.485   7.554   1.00 19.02 ? 284  LEU A CB    1 
ATOM   2344 C  CG    . LEU A 1 294 ? -8.908  5.004   7.560   1.00 19.51 ? 284  LEU A CG    1 
ATOM   2345 C  CD1   . LEU A 1 294 ? -7.927  5.422   8.640   1.00 19.70 ? 284  LEU A CD1   1 
ATOM   2346 C  CD2   . LEU A 1 294 ? -8.376  5.451   6.211   1.00 20.00 ? 284  LEU A CD2   1 
ATOM   2347 N  N     . LEU A 1 295 ? -12.036 3.142   8.867   1.00 19.34 ? 285  LEU A N     1 
ATOM   2348 C  CA    . LEU A 1 295 ? -13.314 3.709   9.294   1.00 19.46 ? 285  LEU A CA    1 
ATOM   2349 C  C     . LEU A 1 295 ? -13.646 3.312   10.735  1.00 20.12 ? 285  LEU A C     1 
ATOM   2350 O  O     . LEU A 1 295 ? -14.128 4.148   11.533  1.00 20.26 ? 285  LEU A O     1 
ATOM   2351 C  CB    . LEU A 1 295 ? -14.414 3.292   8.320   1.00 19.22 ? 285  LEU A CB    1 
ATOM   2352 C  CG    . LEU A 1 295 ? -14.350 3.958   6.939   1.00 18.79 ? 285  LEU A CG    1 
ATOM   2353 C  CD1   . LEU A 1 295 ? -15.246 3.217   5.984   1.00 19.26 ? 285  LEU A CD1   1 
ATOM   2354 C  CD2   . LEU A 1 295 ? -14.738 5.436   7.005   1.00 18.95 ? 285  LEU A CD2   1 
ATOM   2355 N  N     . MET A 1 296 ? -13.345 2.068   11.093  1.00 20.77 ? 286  MET A N     1 
ATOM   2356 C  CA    . MET A 1 296 ? -13.508 1.631   12.491  1.00 22.36 ? 286  MET A CA    1 
ATOM   2357 C  C     . MET A 1 296 ? -12.645 2.459   13.436  1.00 21.95 ? 286  MET A C     1 
ATOM   2358 O  O     . MET A 1 296 ? -13.109 2.908   14.476  1.00 21.71 ? 286  MET A O     1 
ATOM   2359 C  CB    . MET A 1 296 ? -13.160 0.157   12.632  1.00 24.00 ? 286  MET A CB    1 
ATOM   2360 C  CG    . MET A 1 296 ? -14.214 -0.746  12.059  1.00 26.09 ? 286  MET A CG    1 
ATOM   2361 S  SD    . MET A 1 296 ? -13.626 -2.443  12.184  1.00 29.56 ? 286  MET A SD    1 
ATOM   2362 C  CE    . MET A 1 296 ? -15.055 -3.300  11.557  1.00 30.03 ? 286  MET A CE    1 
ATOM   2363 N  N     . ALA A 1 297 ? -11.394 2.699   13.042  1.00 22.43 ? 287  ALA A N     1 
ATOM   2364 C  CA    . ALA A 1 297 ? -10.483 3.493   13.863  1.00 22.61 ? 287  ALA A CA    1 
ATOM   2365 C  C     . ALA A 1 297 ? -10.954 4.946   14.032  1.00 22.57 ? 287  ALA A C     1 
ATOM   2366 O  O     . ALA A 1 297 ? -10.654 5.582   15.048  1.00 22.97 ? 287  ALA A O     1 
ATOM   2367 C  CB    . ALA A 1 297 ? -9.070  3.440   13.299  1.00 22.77 ? 287  ALA A CB    1 
ATOM   2368 N  N     . LEU A 1 298 ? -11.723 5.438   13.060  1.00 22.07 ? 288  LEU A N     1 
ATOM   2369 C  CA    . LEU A 1 298 ? -12.353 6.757   13.101  1.00 22.75 ? 288  LEU A CA    1 
ATOM   2370 C  C     . LEU A 1 298 ? -13.778 6.780   13.684  1.00 22.87 ? 288  LEU A C     1 
ATOM   2371 O  O     . LEU A 1 298 ? -14.400 7.835   13.720  1.00 22.84 ? 288  LEU A O     1 
ATOM   2372 C  CB    . LEU A 1 298 ? -12.383 7.360   11.686  1.00 23.40 ? 288  LEU A CB    1 
ATOM   2373 C  CG    . LEU A 1 298 ? -11.010 7.621   11.068  1.00 23.59 ? 288  LEU A CG    1 
ATOM   2374 C  CD1   . LEU A 1 298 ? -11.114 7.976   9.591   1.00 23.33 ? 288  LEU A CD1   1 
ATOM   2375 C  CD2   . LEU A 1 298 ? -10.273 8.712   11.843  1.00 24.32 ? 288  LEU A CD2   1 
ATOM   2376 N  N     . ASP A 1 299 ? -14.266 5.627   14.141  1.00 23.40 ? 289  ASP A N     1 
ATOM   2377 C  CA    . ASP A 1 299 ? -15.619 5.462   14.689  1.00 24.19 ? 289  ASP A CA    1 
ATOM   2378 C  C     . ASP A 1 299 ? -16.689 5.946   13.694  1.00 23.39 ? 289  ASP A C     1 
ATOM   2379 O  O     . ASP A 1 299 ? -17.620 6.675   14.065  1.00 23.23 ? 289  ASP A O     1 
ATOM   2380 C  CB    . ASP A 1 299 ? -15.718 6.189   16.046  1.00 25.87 ? 289  ASP A CB    1 
ATOM   2381 C  CG    . ASP A 1 299 ? -16.957 5.803   16.847  1.00 27.63 ? 289  ASP A CG    1 
ATOM   2382 O  OD1   . ASP A 1 299 ? -17.526 4.716   16.633  1.00 28.31 ? 289  ASP A OD1   1 
ATOM   2383 O  OD2   . ASP A 1 299 ? -17.360 6.605   17.713  1.00 30.25 ? 289  ASP A OD2   1 
ATOM   2384 N  N     . LEU A 1 300 ? -16.506 5.573   12.428  1.00 22.17 ? 290  LEU A N     1 
ATOM   2385 C  CA    . LEU A 1 300 ? -17.428 5.949   11.339  1.00 22.36 ? 290  LEU A CA    1 
ATOM   2386 C  C     . LEU A 1 300 ? -18.144 4.726   10.778  1.00 22.19 ? 290  LEU A C     1 
ATOM   2387 O  O     . LEU A 1 300 ? -17.559 3.632   10.740  1.00 21.85 ? 290  LEU A O     1 
ATOM   2388 C  CB    . LEU A 1 300 ? -16.683 6.661   10.198  1.00 22.39 ? 290  LEU A CB    1 
ATOM   2389 C  CG    . LEU A 1 300 ? -16.046 8.025   10.493  1.00 22.96 ? 290  LEU A CG    1 
ATOM   2390 C  CD1   . LEU A 1 300 ? -15.313 8.529   9.263   1.00 22.57 ? 290  LEU A CD1   1 
ATOM   2391 C  CD2   . LEU A 1 300 ? -17.058 9.063   10.940  1.00 23.77 ? 290  LEU A CD2   1 
ATOM   2392 N  N     . PRO A 1 301 ? -19.384 4.911   10.271  1.00 22.68 ? 291  PRO A N     1 
ATOM   2393 C  CA    . PRO A 1 301 ? -20.082 3.817   9.585   1.00 23.27 ? 291  PRO A CA    1 
ATOM   2394 C  C     . PRO A 1 301 ? -19.324 3.305   8.368   1.00 22.65 ? 291  PRO A C     1 
ATOM   2395 O  O     . PRO A 1 301 ? -18.635 4.080   7.695   1.00 22.45 ? 291  PRO A O     1 
ATOM   2396 C  CB    . PRO A 1 301 ? -21.401 4.460   9.115   1.00 24.28 ? 291  PRO A CB    1 
ATOM   2397 C  CG    . PRO A 1 301 ? -21.569 5.685   9.930   1.00 24.79 ? 291  PRO A CG    1 
ATOM   2398 C  CD    . PRO A 1 301 ? -20.197 6.142   10.321  1.00 23.43 ? 291  PRO A CD    1 
ATOM   2399 N  N     . LEU A 1 302 ? -19.479 2.016   8.097   1.00 22.46 ? 292  LEU A N     1 
ATOM   2400 C  CA    . LEU A 1 302 ? -18.799 1.358   6.984   1.00 22.72 ? 292  LEU A CA    1 
ATOM   2401 C  C     . LEU A 1 302 ? -19.685 1.402   5.738   1.00 21.94 ? 292  LEU A C     1 
ATOM   2402 O  O     . LEU A 1 302 ? -20.922 1.455   5.848   1.00 21.64 ? 292  LEU A O     1 
ATOM   2403 C  CB    . LEU A 1 302 ? -18.435 -0.093  7.346   1.00 23.53 ? 292  LEU A CB    1 
ATOM   2404 C  CG    . LEU A 1 302 ? -17.086 -0.270  8.084   1.00 24.60 ? 292  LEU A CG    1 
ATOM   2405 C  CD1   . LEU A 1 302 ? -16.900 0.674   9.262   1.00 24.73 ? 292  LEU A CD1   1 
ATOM   2406 C  CD2   . LEU A 1 302 ? -16.948 -1.714  8.544   1.00 25.55 ? 292  LEU A CD2   1 
ATOM   2407 N  N     . PRO A 1 303 ? -19.059 1.351   4.543   1.00 22.04 ? 293  PRO A N     1 
ATOM   2408 C  CA    . PRO A 1 303 ? -19.847 1.311   3.317   1.00 22.02 ? 293  PRO A CA    1 
ATOM   2409 C  C     . PRO A 1 303 ? -20.670 0.028   3.206   1.00 23.11 ? 293  PRO A C     1 
ATOM   2410 O  O     . PRO A 1 303 ? -20.321 -1.003  3.796   1.00 23.74 ? 293  PRO A O     1 
ATOM   2411 C  CB    . PRO A 1 303 ? -18.790 1.379   2.202   1.00 22.40 ? 293  PRO A CB    1 
ATOM   2412 C  CG    . PRO A 1 303 ? -17.498 0.984   2.822   1.00 22.17 ? 293  PRO A CG    1 
ATOM   2413 C  CD    . PRO A 1 303 ? -17.614 1.180   4.296   1.00 22.04 ? 293  PRO A CD    1 
ATOM   2414 N  N     . LYS A 1 304 ? -21.760 0.104   2.462   1.00 23.58 ? 294  LYS A N     1 
ATOM   2415 C  CA    . LYS A 1 304 ? -22.702 -1.010  2.345   1.00 24.72 ? 294  LYS A CA    1 
ATOM   2416 C  C     . LYS A 1 304 ? -22.251 -2.097  1.370   1.00 24.43 ? 294  LYS A C     1 
ATOM   2417 O  O     . LYS A 1 304 ? -22.547 -3.281  1.589   1.00 23.90 ? 294  LYS A O     1 
ATOM   2418 C  CB    . LYS A 1 304 ? -24.081 -0.478  1.962   1.00 25.78 ? 294  LYS A CB    1 
ATOM   2419 C  CG    . LYS A 1 304 ? -24.684 0.380   3.069   1.00 27.65 ? 294  LYS A CG    1 
ATOM   2420 C  CD    . LYS A 1 304 ? -26.141 0.757   2.818   1.00 29.23 ? 294  LYS A CD    1 
ATOM   2421 C  CE    . LYS A 1 304 ? -26.765 1.344   4.084   1.00 30.32 ? 294  LYS A CE    1 
ATOM   2422 N  NZ    . LYS A 1 304 ? -28.178 1.768   3.860   1.00 31.53 ? 294  LYS A NZ    1 
ATOM   2423 N  N     . LYS A 1 305 ? -21.529 -1.707  0.319   1.00 23.95 ? 295  LYS A N     1 
ATOM   2424 C  CA    . LYS A 1 305 ? -21.137 -2.635  -0.742  1.00 24.58 ? 295  LYS A CA    1 
ATOM   2425 C  C     . LYS A 1 305 ? -19.899 -2.176  -1.487  1.00 23.89 ? 295  LYS A C     1 
ATOM   2426 O  O     . LYS A 1 305 ? -19.788 -1.012  -1.878  1.00 22.11 ? 295  LYS A O     1 
ATOM   2427 C  CB    . LYS A 1 305 ? -22.284 -2.809  -1.742  1.00 26.02 ? 295  LYS A CB    1 
ATOM   2428 C  CG    . LYS A 1 305 ? -22.042 -3.866  -2.817  1.00 28.26 ? 295  LYS A CG    1 
ATOM   2429 C  CD    . LYS A 1 305 ? -23.176 -3.960  -3.840  1.00 30.39 ? 295  LYS A CD    1 
ATOM   2430 C  CE    . LYS A 1 305 ? -24.496 -4.426  -3.251  1.00 33.20 ? 295  LYS A CE    1 
ATOM   2431 N  NZ    . LYS A 1 305 ? -24.449 -5.805  -2.686  1.00 35.90 ? 295  LYS A NZ    1 
ATOM   2432 N  N     . VAL A 1 306 ? -18.988 -3.117  -1.697  1.00 23.49 ? 296  VAL A N     1 
ATOM   2433 C  CA    . VAL A 1 306 ? -17.905 -2.965  -2.653  1.00 24.72 ? 296  VAL A CA    1 
ATOM   2434 C  C     . VAL A 1 306 ? -18.297 -3.758  -3.892  1.00 24.96 ? 296  VAL A C     1 
ATOM   2435 O  O     . VAL A 1 306 ? -18.516 -4.970  -3.815  1.00 25.24 ? 296  VAL A O     1 
ATOM   2436 C  CB    . VAL A 1 306 ? -16.598 -3.490  -2.048  1.00 25.81 ? 296  VAL A CB    1 
ATOM   2437 C  CG1   . VAL A 1 306 ? -15.497 -3.586  -3.095  1.00 26.57 ? 296  VAL A CG1   1 
ATOM   2438 C  CG2   . VAL A 1 306 ? -16.174 -2.568  -0.917  1.00 26.35 ? 296  VAL A CG2   1 
ATOM   2439 N  N     . PHE A 1 307 ? -18.402 -3.070  -5.024  1.00 25.29 ? 297  PHE A N     1 
ATOM   2440 C  CA    . PHE A 1 307 ? -18.696 -3.706  -6.288  1.00 25.78 ? 297  PHE A CA    1 
ATOM   2441 C  C     . PHE A 1 307 ? -17.450 -3.718  -7.159  1.00 25.01 ? 297  PHE A C     1 
ATOM   2442 O  O     . PHE A 1 307 ? -16.943 -2.662  -7.529  1.00 23.81 ? 297  PHE A O     1 
ATOM   2443 C  CB    . PHE A 1 307 ? -19.826 -3.018  -7.031  1.00 27.73 ? 297  PHE A CB    1 
ATOM   2444 C  CG    . PHE A 1 307 ? -20.179 -3.710  -8.314  1.00 30.18 ? 297  PHE A CG    1 
ATOM   2445 C  CD1   . PHE A 1 307 ? -20.712 -5.002  -8.284  1.00 32.33 ? 297  PHE A CD1   1 
ATOM   2446 C  CD2   . PHE A 1 307 ? -19.939 -3.111  -9.546  1.00 31.95 ? 297  PHE A CD2   1 
ATOM   2447 C  CE1   . PHE A 1 307 ? -21.012 -5.676  -9.460  1.00 33.65 ? 297  PHE A CE1   1 
ATOM   2448 C  CE2   . PHE A 1 307 ? -20.240 -3.780  -10.729 1.00 32.46 ? 297  PHE A CE2   1 
ATOM   2449 C  CZ    . PHE A 1 307 ? -20.778 -5.064  -10.682 1.00 33.63 ? 297  PHE A CZ    1 
ATOM   2450 N  N     . ALA A 1 308 ? -16.984 -4.915  -7.507  1.00 25.10 ? 298  ALA A N     1 
ATOM   2451 C  CA    . ALA A 1 308 ? -15.804 -5.076  -8.349  1.00 26.01 ? 298  ALA A CA    1 
ATOM   2452 C  C     . ALA A 1 308 ? -16.158 -5.683  -9.689  1.00 26.29 ? 298  ALA A C     1 
ATOM   2453 O  O     . ALA A 1 308 ? -16.787 -6.733  -9.743  1.00 27.88 ? 298  ALA A O     1 
ATOM   2454 C  CB    . ALA A 1 308 ? -14.777 -5.951  -7.665  1.00 26.98 ? 298  ALA A CB    1 
ATOM   2455 N  N     . HIS A 1 309 ? -15.727 -5.027  -10.760 1.00 24.90 ? 299  HIS A N     1 
ATOM   2456 C  CA    . HIS A 1 309 ? -15.872 -5.573  -12.099 1.00 24.48 ? 299  HIS A CA    1 
ATOM   2457 C  C     . HIS A 1 309 ? -14.516 -6.095  -12.588 1.00 25.11 ? 299  HIS A C     1 
ATOM   2458 O  O     . HIS A 1 309 ? -13.493 -5.973  -11.902 1.00 24.87 ? 299  HIS A O     1 
ATOM   2459 C  CB    . HIS A 1 309 ? -16.473 -4.547  -13.074 1.00 24.01 ? 299  HIS A CB    1 
ATOM   2460 C  CG    . HIS A 1 309 ? -15.689 -3.283  -13.198 1.00 23.35 ? 299  HIS A CG    1 
ATOM   2461 N  ND1   . HIS A 1 309 ? -14.467 -3.215  -13.835 1.00 23.10 ? 299  HIS A ND1   1 
ATOM   2462 C  CD2   . HIS A 1 309 ? -15.967 -2.027  -12.777 1.00 22.54 ? 299  HIS A CD2   1 
ATOM   2463 C  CE1   . HIS A 1 309 ? -14.028 -1.969  -13.793 1.00 22.90 ? 299  HIS A CE1   1 
ATOM   2464 N  NE2   . HIS A 1 309 ? -14.920 -1.229  -13.157 1.00 22.51 ? 299  HIS A NE2   1 
ATOM   2465 N  N     . GLY A 1 310 ? -14.541 -6.691  -13.769 1.00 25.74 ? 300  GLY A N     1 
ATOM   2466 C  CA    . GLY A 1 310 ? -13.348 -7.235  -14.395 1.00 26.31 ? 300  GLY A CA    1 
ATOM   2467 C  C     . GLY A 1 310 ? -12.552 -6.239  -15.208 1.00 26.59 ? 300  GLY A C     1 
ATOM   2468 O  O     . GLY A 1 310 ? -12.725 -5.024  -15.102 1.00 25.36 ? 300  GLY A O     1 
ATOM   2469 N  N     . TRP A 1 311 ? -11.654 -6.785  -16.015 1.00 26.91 ? 301  TRP A N     1 
ATOM   2470 C  CA    . TRP A 1 311 ? -10.742 -6.000  -16.819 1.00 27.71 ? 301  TRP A CA    1 
ATOM   2471 C  C     . TRP A 1 311 ? -11.102 -6.043  -18.290 1.00 28.11 ? 301  TRP A C     1 
ATOM   2472 O  O     . TRP A 1 311 ? -11.461 -7.096  -18.834 1.00 28.20 ? 301  TRP A O     1 
ATOM   2473 C  CB    . TRP A 1 311 ? -9.310  -6.515  -16.686 1.00 28.96 ? 301  TRP A CB    1 
ATOM   2474 C  CG    . TRP A 1 311 ? -8.681  -6.341  -15.351 1.00 30.14 ? 301  TRP A CG    1 
ATOM   2475 C  CD1   . TRP A 1 311 ? -8.882  -5.321  -14.452 1.00 30.15 ? 301  TRP A CD1   1 
ATOM   2476 C  CD2   . TRP A 1 311 ? -7.685  -7.188  -14.782 1.00 31.32 ? 301  TRP A CD2   1 
ATOM   2477 N  NE1   . TRP A 1 311 ? -8.094  -5.510  -13.343 1.00 30.35 ? 301  TRP A NE1   1 
ATOM   2478 C  CE2   . TRP A 1 311 ? -7.343  -6.645  -13.520 1.00 31.54 ? 301  TRP A CE2   1 
ATOM   2479 C  CE3   . TRP A 1 311 ? -7.055  -8.369  -15.208 1.00 32.95 ? 301  TRP A CE3   1 
ATOM   2480 C  CZ2   . TRP A 1 311 ? -6.398  -7.246  -12.677 1.00 32.45 ? 301  TRP A CZ2   1 
ATOM   2481 C  CZ3   . TRP A 1 311 ? -6.114  -8.967  -14.373 1.00 33.57 ? 301  TRP A CZ3   1 
ATOM   2482 C  CH2   . TRP A 1 311 ? -5.796  -8.404  -13.118 1.00 33.41 ? 301  TRP A CH2   1 
ATOM   2483 N  N     . ILE A 1 312 ? -10.988 -4.889  -18.925 1.00 27.83 ? 302  ILE A N     1 
ATOM   2484 C  CA    . ILE A 1 312 ? -10.892 -4.812  -20.370 1.00 28.43 ? 302  ILE A CA    1 
ATOM   2485 C  C     . ILE A 1 312 ? -9.460  -5.207  -20.702 1.00 30.69 ? 302  ILE A C     1 
ATOM   2486 O  O     . ILE A 1 312 ? -8.504  -4.628  -20.172 1.00 29.22 ? 302  ILE A O     1 
ATOM   2487 C  CB    . ILE A 1 312 ? -11.211 -3.409  -20.913 1.00 27.50 ? 302  ILE A CB    1 
ATOM   2488 C  CG1   . ILE A 1 312 ? -12.654 -3.045  -20.541 1.00 27.29 ? 302  ILE A CG1   1 
ATOM   2489 C  CG2   . ILE A 1 312 ? -11.009 -3.363  -22.424 1.00 27.58 ? 302  ILE A CG2   1 
ATOM   2490 C  CD1   . ILE A 1 312 ? -13.136 -1.696  -21.047 1.00 26.42 ? 302  ILE A CD1   1 
ATOM   2491 N  N     . LEU A 1 313 ? -9.344  -6.223  -21.557 1.00 32.21 ? 303  LEU A N     1 
ATOM   2492 C  CA    . LEU A 1 313 ? -8.071  -6.765  -21.997 1.00 34.96 ? 303  LEU A CA    1 
ATOM   2493 C  C     . LEU A 1 313 ? -7.811  -6.379  -23.446 1.00 36.40 ? 303  LEU A C     1 
ATOM   2494 O  O     . LEU A 1 313 ? -8.728  -6.036  -24.192 1.00 34.24 ? 303  LEU A O     1 
ATOM   2495 C  CB    . LEU A 1 313 ? -8.080  -8.295  -21.902 1.00 36.10 ? 303  LEU A CB    1 
ATOM   2496 C  CG    . LEU A 1 313 ? -8.429  -8.952  -20.570 1.00 36.96 ? 303  LEU A CG    1 
ATOM   2497 C  CD1   . LEU A 1 313 ? -8.485  -10.467 -20.731 1.00 37.67 ? 303  LEU A CD1   1 
ATOM   2498 C  CD2   . LEU A 1 313 ? -7.441  -8.565  -19.484 1.00 37.06 ? 303  LEU A CD2   1 
ATOM   2499 N  N     . MET A 1 314 ? -6.540  -6.427  -23.821 1.00 38.87 ? 304  MET A N     1 
ATOM   2500 C  CA    . MET A 1 314 ? -6.126  -6.430  -25.221 1.00 42.49 ? 304  MET A CA    1 
ATOM   2501 C  C     . MET A 1 314 ? -5.448  -7.780  -25.477 1.00 46.41 ? 304  MET A C     1 
ATOM   2502 O  O     . MET A 1 314 ? -5.470  -8.671  -24.615 1.00 46.33 ? 304  MET A O     1 
ATOM   2503 C  CB    . MET A 1 314 ? -5.189  -5.250  -25.505 1.00 42.30 ? 304  MET A CB    1 
ATOM   2504 C  CG    . MET A 1 314 ? -5.874  -3.895  -25.463 1.00 41.87 ? 304  MET A CG    1 
ATOM   2505 S  SD    . MET A 1 314 ? -7.196  -3.677  -26.671 1.00 40.82 ? 304  MET A SD    1 
ATOM   2506 C  CE    . MET A 1 314 ? -6.393  -2.719  -27.953 1.00 41.75 ? 304  MET A CE    1 
ATOM   2507 N  N     . LYS A 1 315 ? -4.851  -7.953  -26.653 1.00 50.75 ? 305  LYS A N     1 
ATOM   2508 C  CA    . LYS A 1 315 ? -4.138  -9.200  -26.971 1.00 53.81 ? 305  LYS A CA    1 
ATOM   2509 C  C     . LYS A 1 315 ? -2.654  -9.081  -26.613 1.00 55.19 ? 305  LYS A C     1 
ATOM   2510 O  O     . LYS A 1 315 ? -1.761  -9.216  -27.450 1.00 58.62 ? 305  LYS A O     1 
ATOM   2511 C  CB    . LYS A 1 315 ? -4.383  -9.576  -28.425 1.00 55.75 ? 305  LYS A CB    1 
ATOM   2512 C  CG    . LYS A 1 315 ? -5.797  -10.097 -28.662 1.00 56.42 ? 305  LYS A CG    1 
ATOM   2513 C  CD    . LYS A 1 315 ? -6.432  -9.555  -29.938 1.00 57.18 ? 305  LYS A CD    1 
ATOM   2514 C  CE    . LYS A 1 315 ? -5.728  -10.036 -31.201 1.00 58.63 ? 305  LYS A CE    1 
ATOM   2515 N  NZ    . LYS A 1 315 ? -4.540  -9.228  -31.609 1.00 59.56 ? 305  LYS A NZ    1 
ATOM   2516 N  N     . ASP A 1 316 ? -2.459  -8.773  -25.333 1.00 54.43 ? 306  ASP A N     1 
ATOM   2517 C  CA    . ASP A 1 316 ? -1.191  -8.830  -24.589 1.00 55.06 ? 306  ASP A CA    1 
ATOM   2518 C  C     . ASP A 1 316 ? -1.440  -8.525  -23.090 1.00 54.00 ? 306  ASP A C     1 
ATOM   2519 O  O     . ASP A 1 316 ? -0.542  -8.043  -22.388 1.00 54.69 ? 306  ASP A O     1 
ATOM   2520 C  CB    . ASP A 1 316 ? -0.090  -7.915  -25.190 1.00 56.92 ? 306  ASP A CB    1 
ATOM   2521 C  CG    . ASP A 1 316 ? -0.393  -6.417  -25.064 1.00 57.56 ? 306  ASP A CG    1 
ATOM   2522 O  OD1   . ASP A 1 316 ? -1.579  -6.012  -25.014 1.00 57.13 ? 306  ASP A OD1   1 
ATOM   2523 O  OD2   . ASP A 1 316 ? 0.586   -5.638  -25.035 1.00 57.89 ? 306  ASP A OD2   1 
ATOM   2524 N  N     . GLY A 1 317 ? -2.654  -8.827  -22.610 1.00 50.85 ? 307  GLY A N     1 
ATOM   2525 C  CA    . GLY A 1 317 ? -3.045  -8.588  -21.233 1.00 47.77 ? 307  GLY A CA    1 
ATOM   2526 C  C     . GLY A 1 317 ? -3.897  -7.358  -20.984 1.00 45.35 ? 307  GLY A C     1 
ATOM   2527 O  O     . GLY A 1 317 ? -4.301  -6.634  -21.900 1.00 42.74 ? 307  GLY A O     1 
ATOM   2528 N  N     . LYS A 1 318 ? -4.155  -7.160  -19.697 1.00 43.28 ? 308  LYS A N     1 
ATOM   2529 C  CA    . LYS A 1 318 ? -4.949  -6.057  -19.166 1.00 41.34 ? 308  LYS A CA    1 
ATOM   2530 C  C     . LYS A 1 318 ? -4.560  -4.723  -19.782 1.00 38.70 ? 308  LYS A C     1 
ATOM   2531 O  O     . LYS A 1 318 ? -3.374  -4.412  -19.899 1.00 38.56 ? 308  LYS A O     1 
ATOM   2532 C  CB    . LYS A 1 318 ? -4.752  -5.994  -17.651 1.00 42.14 ? 308  LYS A CB    1 
ATOM   2533 C  CG    . LYS A 1 318 ? -5.634  -4.988  -16.942 1.00 42.40 ? 308  LYS A CG    1 
ATOM   2534 C  CD    . LYS A 1 318 ? -5.023  -4.585  -15.616 1.00 42.99 ? 308  LYS A CD    1 
ATOM   2535 C  CE    . LYS A 1 318 ? -5.705  -3.365  -15.054 1.00 42.42 ? 308  LYS A CE    1 
ATOM   2536 N  NZ    . LYS A 1 318 ? -5.231  -2.097  -15.672 1.00 42.45 ? 308  LYS A NZ    1 
ATOM   2537 N  N     . MET A 1 319 ? -5.560  -3.947  -20.185 1.00 35.20 ? 309  MET A N     1 
ATOM   2538 C  CA    . MET A 1 319 ? -5.304  -2.600  -20.675 1.00 34.69 ? 309  MET A CA    1 
ATOM   2539 C  C     . MET A 1 319 ? -4.723  -1.759  -19.529 1.00 35.00 ? 309  MET A C     1 
ATOM   2540 O  O     . MET A 1 319 ? -5.300  -1.699  -18.431 1.00 33.15 ? 309  MET A O     1 
ATOM   2541 C  CB    . MET A 1 319 ? -6.564  -1.957  -21.238 1.00 33.50 ? 309  MET A CB    1 
ATOM   2542 C  CG    . MET A 1 319 ? -6.279  -0.661  -21.973 1.00 33.11 ? 309  MET A CG    1 
ATOM   2543 S  SD    . MET A 1 319 ? -7.705  0.023   -22.810 1.00 31.42 ? 309  MET A SD    1 
ATOM   2544 C  CE    . MET A 1 319 ? -7.918  -1.187  -24.128 1.00 32.31 ? 309  MET A CE    1 
ATOM   2545 N  N     . SER A 1 320 ? -3.573  -1.139  -19.800 1.00 35.40 ? 310  SER A N     1 
ATOM   2546 C  CA    . SER A 1 320 ? -2.798  -0.417  -18.793 1.00 36.93 ? 310  SER A CA    1 
ATOM   2547 C  C     . SER A 1 320 ? -2.175  0.826   -19.435 1.00 38.59 ? 310  SER A C     1 
ATOM   2548 O  O     . SER A 1 320 ? -1.546  0.722   -20.495 1.00 38.19 ? 310  SER A O     1 
ATOM   2549 C  CB    . SER A 1 320 ? -1.718  -1.344  -18.225 1.00 37.52 ? 310  SER A CB    1 
ATOM   2550 O  OG    . SER A 1 320 ? -0.734  -0.632  -17.500 1.00 37.05 ? 310  SER A OG    1 
ATOM   2551 N  N     . LYS A 1 321 ? -2.362  1.992   -18.808 1.00 39.67 ? 311  LYS A N     1 
ATOM   2552 C  CA    . LYS A 1 321 ? -1.798  3.250   -19.343 1.00 41.92 ? 311  LYS A CA    1 
ATOM   2553 C  C     . LYS A 1 321 ? -0.259  3.293   -19.305 1.00 43.74 ? 311  LYS A C     1 
ATOM   2554 O  O     . LYS A 1 321 ? 0.366   3.889   -20.188 1.00 43.87 ? 311  LYS A O     1 
ATOM   2555 C  CB    . LYS A 1 321 ? -2.410  4.496   -18.676 1.00 42.23 ? 311  LYS A CB    1 
ATOM   2556 C  CG    . LYS A 1 321 ? -2.161  4.670   -17.185 1.00 42.95 ? 311  LYS A CG    1 
ATOM   2557 C  CD    . LYS A 1 321 ? -2.932  5.871   -16.633 1.00 42.27 ? 311  LYS A CD    1 
ATOM   2558 C  CE    . LYS A 1 321 ? -3.715  5.534   -15.368 1.00 43.33 ? 311  LYS A CE    1 
ATOM   2559 N  NZ    . LYS A 1 321 ? -2.866  5.209   -14.197 1.00 43.67 ? 311  LYS A NZ    1 
ATOM   2560 N  N     . SER A 1 322 ? 0.336   2.657   -18.296 1.00 44.90 ? 312  SER A N     1 
ATOM   2561 C  CA    . SER A 1 322 ? 1.800   2.540   -18.200 1.00 47.28 ? 312  SER A CA    1 
ATOM   2562 C  C     . SER A 1 322 ? 2.387   1.569   -19.245 1.00 47.91 ? 312  SER A C     1 
ATOM   2563 O  O     . SER A 1 322 ? 3.514   1.760   -19.691 1.00 47.96 ? 312  SER A O     1 
ATOM   2564 C  CB    . SER A 1 322 ? 2.217   2.110   -16.786 1.00 47.28 ? 312  SER A CB    1 
ATOM   2565 O  OG    . SER A 1 322 ? 1.829   0.777   -16.520 1.00 47.61 ? 312  SER A OG    1 
ATOM   2566 N  N     . LYS A 1 323 ? 1.626   0.536   -19.613 1.00 48.60 ? 313  LYS A N     1 
ATOM   2567 C  CA    . LYS A 1 323 ? 2.037   -0.428  -20.655 1.00 49.74 ? 313  LYS A CA    1 
ATOM   2568 C  C     . LYS A 1 323 ? 1.894   0.123   -22.080 1.00 49.89 ? 313  LYS A C     1 
ATOM   2569 O  O     . LYS A 1 323 ? 2.686   -0.220  -22.962 1.00 50.50 ? 313  LYS A O     1 
ATOM   2570 C  CB    . LYS A 1 323 ? 1.228   -1.724  -20.540 1.00 50.61 ? 313  LYS A CB    1 
ATOM   2571 C  CG    . LYS A 1 323 ? 1.690   -2.836  -21.481 1.00 51.88 ? 313  LYS A CG    1 
ATOM   2572 C  CD    . LYS A 1 323 ? 0.855   -4.098  -21.337 1.00 53.04 ? 313  LYS A CD    1 
ATOM   2573 C  CE    . LYS A 1 323 ? 1.315   -4.975  -20.181 1.00 54.37 ? 313  LYS A CE    1 
ATOM   2574 N  NZ    . LYS A 1 323 ? 0.639   -6.306  -20.228 1.00 55.04 ? 313  LYS A NZ    1 
ATOM   2575 N  N     . GLY A 1 324 ? 0.868   0.941   -22.304 1.00 48.30 ? 314  GLY A N     1 
ATOM   2576 C  CA    . GLY A 1 324 ? 0.609   1.535   -23.619 1.00 48.05 ? 314  GLY A CA    1 
ATOM   2577 C  C     . GLY A 1 324 ? -0.217  0.705   -24.594 1.00 47.22 ? 314  GLY A C     1 
ATOM   2578 O  O     . GLY A 1 324 ? -0.383  1.106   -25.749 1.00 49.06 ? 314  GLY A O     1 
ATOM   2579 N  N     . ASN A 1 325 ? -0.754  -0.432  -24.142 1.00 46.16 ? 315  ASN A N     1 
ATOM   2580 C  CA    . ASN A 1 325 ? -1.698  -1.244  -24.945 1.00 42.90 ? 315  ASN A CA    1 
ATOM   2581 C  C     . ASN A 1 325 ? -3.134  -0.676  -24.867 1.00 41.10 ? 315  ASN A C     1 
ATOM   2582 O  O     . ASN A 1 325 ? -4.062  -1.374  -24.464 1.00 41.34 ? 315  ASN A O     1 
ATOM   2583 C  CB    . ASN A 1 325 ? -1.658  -2.724  -24.497 1.00 42.70 ? 315  ASN A CB    1 
ATOM   2584 C  CG    . ASN A 1 325 ? -2.110  -2.940  -23.039 1.00 42.14 ? 315  ASN A CG    1 
ATOM   2585 O  OD1   . ASN A 1 325 ? -2.041  -2.030  -22.192 1.00 38.84 ? 315  ASN A OD1   1 
ATOM   2586 N  ND2   . ASN A 1 325 ? -2.566  -4.162  -22.742 1.00 41.23 ? 315  ASN A ND2   1 
ATOM   2587 N  N     . VAL A 1 326 ? -3.317  0.575   -25.289 1.00 37.69 ? 316  VAL A N     1 
ATOM   2588 C  CA    . VAL A 1 326 ? -4.520  1.337   -24.920 1.00 35.59 ? 316  VAL A CA    1 
ATOM   2589 C  C     . VAL A 1 326 ? -5.437  1.711   -26.078 1.00 33.90 ? 316  VAL A C     1 
ATOM   2590 O  O     . VAL A 1 326 ? -4.995  1.897   -27.212 1.00 33.44 ? 316  VAL A O     1 
ATOM   2591 C  CB    . VAL A 1 326 ? -4.177  2.634   -24.136 1.00 35.61 ? 316  VAL A CB    1 
ATOM   2592 C  CG1   . VAL A 1 326 ? -3.488  2.291   -22.824 1.00 35.88 ? 316  VAL A CG1   1 
ATOM   2593 C  CG2   . VAL A 1 326 ? -3.333  3.593   -24.967 1.00 35.56 ? 316  VAL A CG2   1 
ATOM   2594 N  N     . VAL A 1 327 ? -6.722  1.833   -25.745 1.00 31.45 ? 317  VAL A N     1 
ATOM   2595 C  CA    . VAL A 1 327 ? -7.723  2.423   -26.615 1.00 30.55 ? 317  VAL A CA    1 
ATOM   2596 C  C     . VAL A 1 327 ? -8.194  3.696   -25.921 1.00 30.18 ? 317  VAL A C     1 
ATOM   2597 O  O     . VAL A 1 327 ? -8.579  3.674   -24.739 1.00 27.89 ? 317  VAL A O     1 
ATOM   2598 C  CB    . VAL A 1 327 ? -8.909  1.470   -26.863 1.00 31.32 ? 317  VAL A CB    1 
ATOM   2599 C  CG1   . VAL A 1 327 ? -9.958  2.116   -27.769 1.00 31.00 ? 317  VAL A CG1   1 
ATOM   2600 C  CG2   . VAL A 1 327 ? -8.420  0.164   -27.475 1.00 31.98 ? 317  VAL A CG2   1 
ATOM   2601 N  N     . ASP A 1 328 ? -8.170  4.791   -26.673 1.00 29.88 ? 318  ASP A N     1 
ATOM   2602 C  CA    . ASP A 1 328 ? -8.530  6.108   -26.179 1.00 29.89 ? 318  ASP A CA    1 
ATOM   2603 C  C     . ASP A 1 328 ? -10.027 6.334   -26.401 1.00 28.11 ? 318  ASP A C     1 
ATOM   2604 O  O     . ASP A 1 328 ? -10.483 6.334   -27.558 1.00 27.62 ? 318  ASP A O     1 
ATOM   2605 C  CB    . ASP A 1 328 ? -7.723  7.158   -26.941 1.00 31.63 ? 318  ASP A CB    1 
ATOM   2606 C  CG    . ASP A 1 328 ? -7.883  8.554   -26.387 1.00 32.32 ? 318  ASP A CG    1 
ATOM   2607 O  OD1   . ASP A 1 328 ? -8.809  8.824   -25.571 1.00 32.00 ? 318  ASP A OD1   1 
ATOM   2608 O  OD2   . ASP A 1 328 ? -7.060  9.408   -26.781 1.00 34.29 ? 318  ASP A OD2   1 
ATOM   2609 N  N     . PRO A 1 329 ? -10.804 6.538   -25.308 1.00 26.70 ? 319  PRO A N     1 
ATOM   2610 C  CA    . PRO A 1 329 ? -12.239 6.759   -25.524 1.00 26.76 ? 319  PRO A CA    1 
ATOM   2611 C  C     . PRO A 1 329 ? -12.570 7.990   -26.356 1.00 26.69 ? 319  PRO A C     1 
ATOM   2612 O  O     . PRO A 1 329 ? -13.597 8.003   -27.013 1.00 26.80 ? 319  PRO A O     1 
ATOM   2613 C  CB    . PRO A 1 329 ? -12.802 6.906   -24.101 1.00 26.20 ? 319  PRO A CB    1 
ATOM   2614 C  CG    . PRO A 1 329 ? -11.640 7.264   -23.255 1.00 26.57 ? 319  PRO A CG    1 
ATOM   2615 C  CD    . PRO A 1 329 ? -10.457 6.586   -23.871 1.00 26.89 ? 319  PRO A CD    1 
ATOM   2616 N  N     . ASN A 1 330 ? -11.718 9.013   -26.328 1.00 27.14 ? 320  ASN A N     1 
ATOM   2617 C  CA    . ASN A 1 330 ? -11.930 10.194  -27.167 1.00 28.21 ? 320  ASN A CA    1 
ATOM   2618 C  C     . ASN A 1 330 ? -12.002 9.840   -28.645 1.00 28.96 ? 320  ASN A C     1 
ATOM   2619 O  O     . ASN A 1 330 ? -12.833 10.390  -29.378 1.00 29.10 ? 320  ASN A O     1 
ATOM   2620 C  CB    . ASN A 1 330 ? -10.826 11.231  -26.949 1.00 28.47 ? 320  ASN A CB    1 
ATOM   2621 C  CG    . ASN A 1 330 ? -11.056 12.072  -25.710 1.00 28.60 ? 320  ASN A CG    1 
ATOM   2622 O  OD1   . ASN A 1 330 ? -12.159 12.574  -25.493 1.00 29.83 ? 320  ASN A OD1   1 
ATOM   2623 N  ND2   . ASN A 1 330 ? -10.018 12.245  -24.901 1.00 27.91 ? 320  ASN A ND2   1 
ATOM   2624 N  N     . ILE A 1 331 ? -11.150 8.907   -29.065 1.00 29.59 ? 321  ILE A N     1 
ATOM   2625 C  CA    . ILE A 1 331 ? -11.094 8.481   -30.461 1.00 30.66 ? 321  ILE A CA    1 
ATOM   2626 C  C     . ILE A 1 331 ? -12.392 7.762   -30.845 1.00 29.78 ? 321  ILE A C     1 
ATOM   2627 O  O     . ILE A 1 331 ? -12.942 8.016   -31.923 1.00 28.80 ? 321  ILE A O     1 
ATOM   2628 C  CB    . ILE A 1 331 ? -9.834  7.629   -30.754 1.00 32.75 ? 321  ILE A CB    1 
ATOM   2629 C  CG1   . ILE A 1 331 ? -8.583  8.508   -30.555 1.00 34.42 ? 321  ILE A CG1   1 
ATOM   2630 C  CG2   . ILE A 1 331 ? -9.877  7.057   -32.173 1.00 33.02 ? 321  ILE A CG2   1 
ATOM   2631 C  CD1   . ILE A 1 331 ? -7.247  7.798   -30.679 1.00 35.71 ? 321  ILE A CD1   1 
ATOM   2632 N  N     . LEU A 1 332 ? -12.878 6.898   -29.952 1.00 27.77 ? 322  LEU A N     1 
ATOM   2633 C  CA    . LEU A 1 332 ? -14.144 6.185   -30.163 1.00 27.31 ? 322  LEU A CA    1 
ATOM   2634 C  C     . LEU A 1 332 ? -15.337 7.120   -30.256 1.00 27.25 ? 322  LEU A C     1 
ATOM   2635 O  O     . LEU A 1 332 ? -16.192 6.945   -31.134 1.00 27.44 ? 322  LEU A O     1 
ATOM   2636 C  CB    . LEU A 1 332 ? -14.377 5.144   -29.065 1.00 26.98 ? 322  LEU A CB    1 
ATOM   2637 C  CG    . LEU A 1 332 ? -13.405 3.963   -29.032 1.00 27.98 ? 322  LEU A CG    1 
ATOM   2638 C  CD1   . LEU A 1 332 ? -13.700 3.071   -27.838 1.00 27.93 ? 322  LEU A CD1   1 
ATOM   2639 C  CD2   . LEU A 1 332 ? -13.441 3.158   -30.327 1.00 28.62 ? 322  LEU A CD2   1 
ATOM   2640 N  N     . ILE A 1 333 ? -15.401 8.099   -29.355 1.00 26.49 ? 323  ILE A N     1 
ATOM   2641 C  CA    . ILE A 1 333 ? -16.506 9.053   -29.349 1.00 26.64 ? 323  ILE A CA    1 
ATOM   2642 C  C     . ILE A 1 333 ? -16.479 9.907   -30.617 1.00 28.59 ? 323  ILE A C     1 
ATOM   2643 O  O     . ILE A 1 333 ? -17.505 10.035  -31.288 1.00 27.75 ? 323  ILE A O     1 
ATOM   2644 C  CB    . ILE A 1 333 ? -16.516 9.949   -28.093 1.00 26.14 ? 323  ILE A CB    1 
ATOM   2645 C  CG1   . ILE A 1 333 ? -16.737 9.087   -26.849 1.00 26.13 ? 323  ILE A CG1   1 
ATOM   2646 C  CG2   . ILE A 1 333 ? -17.617 10.997  -28.200 1.00 26.30 ? 323  ILE A CG2   1 
ATOM   2647 C  CD1   . ILE A 1 333 ? -16.273 9.730   -25.570 1.00 25.93 ? 323  ILE A CD1   1 
ATOM   2648 N  N     . ASP A 1 334 ? -15.312 10.470  -30.931 1.00 29.68 ? 324  ASP A N     1 
ATOM   2649 C  CA    . ASP A 1 334 ? -15.138 11.296  -32.136 1.00 32.32 ? 324  ASP A CA    1 
ATOM   2650 C  C     . ASP A 1 334 ? -15.514 10.566  -33.422 1.00 32.86 ? 324  ASP A C     1 
ATOM   2651 O  O     . ASP A 1 334 ? -16.156 11.145  -34.295 1.00 33.88 ? 324  ASP A O     1 
ATOM   2652 C  CB    . ASP A 1 334 ? -13.691 11.804  -32.248 1.00 33.47 ? 324  ASP A CB    1 
ATOM   2653 C  CG    . ASP A 1 334 ? -13.342 12.847  -31.202 1.00 35.06 ? 324  ASP A CG    1 
ATOM   2654 O  OD1   . ASP A 1 334 ? -14.224 13.271  -30.421 1.00 37.39 ? 324  ASP A OD1   1 
ATOM   2655 O  OD2   . ASP A 1 334 ? -12.159 13.238  -31.145 1.00 36.12 ? 324  ASP A OD2   1 
ATOM   2656 N  N     . ARG A 1 335 ? -15.131 9.297   -33.528 1.00 32.94 ? 325  ARG A N     1 
ATOM   2657 C  CA    . ARG A 1 335 ? -15.406 8.524   -34.748 1.00 34.16 ? 325  ARG A CA    1 
ATOM   2658 C  C     . ARG A 1 335 ? -16.824 7.957   -34.817 1.00 33.25 ? 325  ARG A C     1 
ATOM   2659 O  O     . ARG A 1 335 ? -17.483 8.065   -35.859 1.00 31.90 ? 325  ARG A O     1 
ATOM   2660 C  CB    . ARG A 1 335 ? -14.400 7.388   -34.912 1.00 36.46 ? 325  ARG A CB    1 
ATOM   2661 C  CG    . ARG A 1 335 ? -14.524 6.697   -36.265 1.00 39.84 ? 325  ARG A CG    1 
ATOM   2662 C  CD    . ARG A 1 335 ? -13.306 5.861   -36.590 1.00 43.25 ? 325  ARG A CD    1 
ATOM   2663 N  NE    . ARG A 1 335 ? -13.525 5.070   -37.806 1.00 46.25 ? 325  ARG A NE    1 
ATOM   2664 C  CZ    . ARG A 1 335 ? -12.701 4.125   -38.269 1.00 48.57 ? 325  ARG A CZ    1 
ATOM   2665 N  NH1   . ARG A 1 335 ? -11.566 3.827   -37.631 1.00 49.26 ? 325  ARG A NH1   1 
ATOM   2666 N  NH2   . ARG A 1 335 ? -13.017 3.468   -39.387 1.00 49.67 ? 325  ARG A NH2   1 
ATOM   2667 N  N     . TYR A 1 336 ? -17.265 7.316   -33.731 1.00 31.75 ? 326  TYR A N     1 
ATOM   2668 C  CA    . TYR A 1 336 ? -18.529 6.549   -33.715 1.00 31.24 ? 326  TYR A CA    1 
ATOM   2669 C  C     . TYR A 1 336 ? -19.699 7.176   -32.948 1.00 30.38 ? 326  TYR A C     1 
ATOM   2670 O  O     . TYR A 1 336 ? -20.838 6.718   -33.081 1.00 30.32 ? 326  TYR A O     1 
ATOM   2671 C  CB    . TYR A 1 336 ? -18.270 5.141   -33.189 1.00 32.13 ? 326  TYR A CB    1 
ATOM   2672 C  CG    . TYR A 1 336 ? -17.276 4.365   -34.029 1.00 33.75 ? 326  TYR A CG    1 
ATOM   2673 C  CD1   . TYR A 1 336 ? -17.635 3.868   -35.286 1.00 35.35 ? 326  TYR A CD1   1 
ATOM   2674 C  CD2   . TYR A 1 336 ? -15.983 4.116   -33.565 1.00 34.96 ? 326  TYR A CD2   1 
ATOM   2675 C  CE1   . TYR A 1 336 ? -16.723 3.155   -36.063 1.00 36.38 ? 326  TYR A CE1   1 
ATOM   2676 C  CE2   . TYR A 1 336 ? -15.071 3.395   -34.332 1.00 36.13 ? 326  TYR A CE2   1 
ATOM   2677 C  CZ    . TYR A 1 336 ? -15.451 2.920   -35.575 1.00 36.86 ? 326  TYR A CZ    1 
ATOM   2678 O  OH    . TYR A 1 336 ? -14.548 2.217   -36.331 1.00 39.94 ? 326  TYR A OH    1 
ATOM   2679 N  N     . GLY A 1 337 ? -19.420 8.207   -32.159 1.00 28.44 ? 327  GLY A N     1 
ATOM   2680 C  CA    . GLY A 1 337 ? -20.423 8.899   -31.364 1.00 28.43 ? 327  GLY A CA    1 
ATOM   2681 C  C     . GLY A 1 337 ? -20.491 8.410   -29.930 1.00 27.43 ? 327  GLY A C     1 
ATOM   2682 O  O     . GLY A 1 337 ? -19.963 7.351   -29.577 1.00 25.82 ? 327  GLY A O     1 
ATOM   2683 N  N     . LEU A 1 338 ? -21.178 9.197   -29.115 1.00 27.05 ? 328  LEU A N     1 
ATOM   2684 C  CA    . LEU A 1 338 ? -21.257 8.975   -27.679 1.00 26.62 ? 328  LEU A CA    1 
ATOM   2685 C  C     . LEU A 1 338 ? -22.135 7.780   -27.306 1.00 25.72 ? 328  LEU A C     1 
ATOM   2686 O  O     . LEU A 1 338 ? -21.732 6.938   -26.502 1.00 24.07 ? 328  LEU A O     1 
ATOM   2687 C  CB    . LEU A 1 338 ? -21.760 10.245  -26.980 1.00 26.95 ? 328  LEU A CB    1 
ATOM   2688 C  CG    . LEU A 1 338 ? -22.026 10.106  -25.476 1.00 26.81 ? 328  LEU A CG    1 
ATOM   2689 C  CD1   . LEU A 1 338 ? -20.764 9.637   -24.769 1.00 27.04 ? 328  LEU A CD1   1 
ATOM   2690 C  CD2   . LEU A 1 338 ? -22.532 11.384  -24.835 1.00 27.56 ? 328  LEU A CD2   1 
ATOM   2691 N  N     . ASP A 1 339 ? -23.335 7.711   -27.873 1.00 25.65 ? 329  ASP A N     1 
ATOM   2692 C  CA    . ASP A 1 339 ? -24.236 6.584   -27.596 1.00 25.52 ? 329  ASP A CA    1 
ATOM   2693 C  C     . ASP A 1 339 ? -23.559 5.245   -27.932 1.00 23.97 ? 329  ASP A C     1 
ATOM   2694 O  O     . ASP A 1 339 ? -23.630 4.307   -27.146 1.00 23.18 ? 329  ASP A O     1 
ATOM   2695 C  CB    . ASP A 1 339 ? -25.569 6.709   -28.355 1.00 26.43 ? 329  ASP A CB    1 
ATOM   2696 C  CG    . ASP A 1 339 ? -26.582 7.620   -27.655 1.00 27.61 ? 329  ASP A CG    1 
ATOM   2697 O  OD1   . ASP A 1 339 ? -26.294 8.203   -26.600 1.00 28.01 ? 329  ASP A OD1   1 
ATOM   2698 O  OD2   . ASP A 1 339 ? -27.705 7.747   -28.190 1.00 29.65 ? 329  ASP A OD2   1 
ATOM   2699 N  N     . ALA A 1 340 ? -22.860 5.184   -29.065 1.00 23.87 ? 330  ALA A N     1 
ATOM   2700 C  CA    . ALA A 1 340 ? -22.188 3.967   -29.481 1.00 23.42 ? 330  ALA A CA    1 
ATOM   2701 C  C     . ALA A 1 340 ? -21.138 3.528   -28.462 1.00 22.61 ? 330  ALA A C     1 
ATOM   2702 O  O     . ALA A 1 340 ? -21.030 2.354   -28.147 1.00 22.43 ? 330  ALA A O     1 
ATOM   2703 C  CB    . ALA A 1 340 ? -21.522 4.171   -30.835 1.00 24.26 ? 330  ALA A CB    1 
ATOM   2704 N  N     . THR A 1 341 ? -20.363 4.485   -27.977 1.00 22.20 ? 331  THR A N     1 
ATOM   2705 C  CA    . THR A 1 341 ? -19.284 4.212   -27.034 1.00 21.90 ? 331  THR A CA    1 
ATOM   2706 C  C     . THR A 1 341 ? -19.821 3.741   -25.682 1.00 21.50 ? 331  THR A C     1 
ATOM   2707 O  O     . THR A 1 341 ? -19.355 2.733   -25.137 1.00 20.97 ? 331  THR A O     1 
ATOM   2708 C  CB    . THR A 1 341 ? -18.402 5.458   -26.851 1.00 22.58 ? 331  THR A CB    1 
ATOM   2709 O  OG1   . THR A 1 341 ? -17.891 5.861   -28.132 1.00 23.54 ? 331  THR A OG1   1 
ATOM   2710 C  CG2   . THR A 1 341 ? -17.241 5.185   -25.899 1.00 22.59 ? 331  THR A CG2   1 
ATOM   2711 N  N     . ARG A 1 342 ? -20.806 4.459   -25.147 1.00 21.38 ? 332  ARG A N     1 
ATOM   2712 C  CA    . ARG A 1 342 ? -21.436 4.036   -23.891 1.00 21.05 ? 332  ARG A CA    1 
ATOM   2713 C  C     . ARG A 1 342 ? -22.137 2.673   -24.020 1.00 21.24 ? 332  ARG A C     1 
ATOM   2714 O  O     . ARG A 1 342 ? -22.011 1.814   -23.133 1.00 21.31 ? 332  ARG A O     1 
ATOM   2715 C  CB    . ARG A 1 342 ? -22.417 5.109   -23.392 1.00 21.18 ? 332  ARG A CB    1 
ATOM   2716 C  CG    . ARG A 1 342 ? -21.727 6.362   -22.867 1.00 20.61 ? 332  ARG A CG    1 
ATOM   2717 C  CD    . ARG A 1 342 ? -22.738 7.459   -22.604 1.00 20.52 ? 332  ARG A CD    1 
ATOM   2718 N  NE    . ARG A 1 342 ? -23.669 7.041   -21.552 1.00 20.31 ? 332  ARG A NE    1 
ATOM   2719 C  CZ    . ARG A 1 342 ? -23.652 7.450   -20.285 1.00 20.02 ? 332  ARG A CZ    1 
ATOM   2720 N  NH1   . ARG A 1 342 ? -22.758 8.342   -19.851 1.00 20.63 ? 332  ARG A NH1   1 
ATOM   2721 N  NH2   . ARG A 1 342 ? -24.556 6.962   -19.439 1.00 19.87 ? 332  ARG A NH2   1 
ATOM   2722 N  N     . TYR A 1 343 ? -22.887 2.486   -25.114 1.00 21.80 ? 333  TYR A N     1 
ATOM   2723 C  CA    . TYR A 1 343 ? -23.549 1.201   -25.399 1.00 22.55 ? 333  TYR A CA    1 
ATOM   2724 C  C     . TYR A 1 343 ? -22.567 0.022   -25.458 1.00 23.13 ? 333  TYR A C     1 
ATOM   2725 O  O     . TYR A 1 343 ? -22.785 -1.004  -24.827 1.00 22.92 ? 333  TYR A O     1 
ATOM   2726 C  CB    . TYR A 1 343 ? -24.364 1.271   -26.699 1.00 22.77 ? 333  TYR A CB    1 
ATOM   2727 C  CG    . TYR A 1 343 ? -25.093 -0.032  -26.997 1.00 23.12 ? 333  TYR A CG    1 
ATOM   2728 C  CD1   . TYR A 1 343 ? -24.737 -0.826  -28.084 1.00 23.76 ? 333  TYR A CD1   1 
ATOM   2729 C  CD2   . TYR A 1 343 ? -26.132 -0.470  -26.168 1.00 23.27 ? 333  TYR A CD2   1 
ATOM   2730 C  CE1   . TYR A 1 343 ? -25.387 -2.020  -28.335 1.00 24.19 ? 333  TYR A CE1   1 
ATOM   2731 C  CE2   . TYR A 1 343 ? -26.787 -1.661  -26.415 1.00 24.14 ? 333  TYR A CE2   1 
ATOM   2732 C  CZ    . TYR A 1 343 ? -26.421 -2.429  -27.501 1.00 23.99 ? 333  TYR A CZ    1 
ATOM   2733 O  OH    . TYR A 1 343 ? -27.075 -3.615  -27.757 1.00 24.95 ? 333  TYR A OH    1 
ATOM   2734 N  N     . TYR A 1 344 ? -21.474 0.180   -26.194 1.00 23.25 ? 334  TYR A N     1 
ATOM   2735 C  CA    . TYR A 1 344 ? -20.501 -0.907  -26.309 1.00 24.39 ? 334  TYR A CA    1 
ATOM   2736 C  C     . TYR A 1 344 ? -19.965 -1.298  -24.927 1.00 23.55 ? 334  TYR A C     1 
ATOM   2737 O  O     . TYR A 1 344 ? -19.922 -2.469  -24.579 1.00 23.55 ? 334  TYR A O     1 
ATOM   2738 C  CB    . TYR A 1 344 ? -19.330 -0.518  -27.218 1.00 25.30 ? 334  TYR A CB    1 
ATOM   2739 C  CG    . TYR A 1 344 ? -18.197 -1.496  -27.070 1.00 26.59 ? 334  TYR A CG    1 
ATOM   2740 C  CD1   . TYR A 1 344 ? -18.183 -2.687  -27.795 1.00 27.03 ? 334  TYR A CD1   1 
ATOM   2741 C  CD2   . TYR A 1 344 ? -17.162 -1.261  -26.158 1.00 27.16 ? 334  TYR A CD2   1 
ATOM   2742 C  CE1   . TYR A 1 344 ? -17.150 -3.599  -27.642 1.00 28.49 ? 334  TYR A CE1   1 
ATOM   2743 C  CE2   . TYR A 1 344 ? -16.139 -2.173  -25.992 1.00 28.05 ? 334  TYR A CE2   1 
ATOM   2744 C  CZ    . TYR A 1 344 ? -16.138 -3.341  -26.734 1.00 28.62 ? 334  TYR A CZ    1 
ATOM   2745 O  OH    . TYR A 1 344 ? -15.123 -4.246  -26.553 1.00 30.28 ? 334  TYR A OH    1 
ATOM   2746 N  N     . LEU A 1 345 ? -19.574 -0.300  -24.139 1.00 23.75 ? 335  LEU A N     1 
ATOM   2747 C  CA    . LEU A 1 345 ? -18.972 -0.554  -22.833 1.00 23.67 ? 335  LEU A CA    1 
ATOM   2748 C  C     . LEU A 1 345 ? -19.898 -1.342  -21.918 1.00 23.70 ? 335  LEU A C     1 
ATOM   2749 O  O     . LEU A 1 345 ? -19.463 -2.278  -21.260 1.00 25.03 ? 335  LEU A O     1 
ATOM   2750 C  CB    . LEU A 1 345 ? -18.543 0.756   -22.155 1.00 23.95 ? 335  LEU A CB    1 
ATOM   2751 C  CG    . LEU A 1 345 ? -17.367 1.500   -22.793 1.00 23.92 ? 335  LEU A CG    1 
ATOM   2752 C  CD1   . LEU A 1 345 ? -17.271 2.912   -22.245 1.00 23.59 ? 335  LEU A CD1   1 
ATOM   2753 C  CD2   . LEU A 1 345 ? -16.050 0.755   -22.600 1.00 24.67 ? 335  LEU A CD2   1 
ATOM   2754 N  N     . MET A 1 346 ? -21.183 -0.995  -21.913 1.00 23.55 ? 336  MET A N     1 
ATOM   2755 C  CA    . MET A 1 346 ? -22.148 -1.644  -21.035 1.00 23.58 ? 336  MET A CA    1 
ATOM   2756 C  C     . MET A 1 346 ? -22.704 -2.960  -21.565 1.00 24.70 ? 336  MET A C     1 
ATOM   2757 O  O     . MET A 1 346 ? -23.011 -3.844  -20.776 1.00 24.57 ? 336  MET A O     1 
ATOM   2758 C  CB    . MET A 1 346 ? -23.277 -0.670  -20.695 1.00 22.97 ? 336  MET A CB    1 
ATOM   2759 C  CG    . MET A 1 346 ? -22.796 0.589   -19.969 1.00 22.59 ? 336  MET A CG    1 
ATOM   2760 S  SD    . MET A 1 346 ? -22.055 0.266   -18.350 1.00 22.71 ? 336  MET A SD    1 
ATOM   2761 C  CE    . MET A 1 346 ? -20.293 0.174   -18.689 1.00 23.11 ? 336  MET A CE    1 
ATOM   2762 N  N     . ARG A 1 347 ? -22.838 -3.088  -22.886 1.00 24.83 ? 337  ARG A N     1 
ATOM   2763 C  CA    . ARG A 1 347 ? -23.414 -4.295  -23.493 1.00 26.19 ? 337  ARG A CA    1 
ATOM   2764 C  C     . ARG A 1 347 ? -22.413 -5.431  -23.710 1.00 27.51 ? 337  ARG A C     1 
ATOM   2765 O  O     . ARG A 1 347 ? -22.742 -6.592  -23.501 1.00 27.04 ? 337  ARG A O     1 
ATOM   2766 C  CB    . ARG A 1 347 ? -24.073 -3.942  -24.842 1.00 26.36 ? 337  ARG A CB    1 
ATOM   2767 C  CG    . ARG A 1 347 ? -24.653 -5.130  -25.618 1.00 27.01 ? 337  ARG A CG    1 
ATOM   2768 C  CD    . ARG A 1 347 ? -25.734 -5.845  -24.834 1.00 27.73 ? 337  ARG A CD    1 
ATOM   2769 N  NE    . ARG A 1 347 ? -26.231 -7.024  -25.542 1.00 28.26 ? 337  ARG A NE    1 
ATOM   2770 C  CZ    . ARG A 1 347 ? -25.700 -8.246  -25.490 1.00 29.89 ? 337  ARG A CZ    1 
ATOM   2771 N  NH1   . ARG A 1 347 ? -24.607 -8.516  -24.761 1.00 29.49 ? 337  ARG A NH1   1 
ATOM   2772 N  NH2   . ARG A 1 347 ? -26.275 -9.227  -26.192 1.00 30.69 ? 337  ARG A NH2   1 
ATOM   2773 N  N     . GLU A 1 348 ? -21.224 -5.102  -24.194 1.00 29.56 ? 338  GLU A N     1 
ATOM   2774 C  CA    . GLU A 1 348 ? -20.282 -6.134  -24.644 1.00 31.78 ? 338  GLU A CA    1 
ATOM   2775 C  C     . GLU A 1 348 ? -19.473 -6.764  -23.512 1.00 32.37 ? 338  GLU A C     1 
ATOM   2776 O  O     . GLU A 1 348 ? -18.960 -7.873  -23.676 1.00 33.47 ? 338  GLU A O     1 
ATOM   2777 C  CB    . GLU A 1 348 ? -19.344 -5.561  -25.715 1.00 33.65 ? 338  GLU A CB    1 
ATOM   2778 C  CG    . GLU A 1 348 ? -18.583 -6.595  -26.542 1.00 35.62 ? 338  GLU A CG    1 
ATOM   2779 C  CD    . GLU A 1 348 ? -19.466 -7.418  -27.467 1.00 37.92 ? 338  GLU A CD    1 
ATOM   2780 O  OE1   . GLU A 1 348 ? -18.948 -8.401  -28.023 1.00 39.79 ? 338  GLU A OE1   1 
ATOM   2781 O  OE2   . GLU A 1 348 ? -20.660 -7.106  -27.638 1.00 38.99 ? 338  GLU A OE2   1 
ATOM   2782 N  N     . LEU A 1 349 ? -19.369 -6.077  -22.374 1.00 32.23 ? 339  LEU A N     1 
ATOM   2783 C  CA    . LEU A 1 349 ? -18.433 -6.454  -21.309 1.00 33.08 ? 339  LEU A CA    1 
ATOM   2784 C  C     . LEU A 1 349 ? -19.160 -6.627  -19.980 1.00 33.42 ? 339  LEU A C     1 
ATOM   2785 O  O     . LEU A 1 349 ? -19.279 -5.664  -19.216 1.00 33.19 ? 339  LEU A O     1 
ATOM   2786 C  CB    . LEU A 1 349 ? -17.341 -5.384  -21.173 1.00 34.14 ? 339  LEU A CB    1 
ATOM   2787 C  CG    . LEU A 1 349 ? -16.545 -5.106  -22.455 1.00 35.22 ? 339  LEU A CG    1 
ATOM   2788 C  CD1   . LEU A 1 349 ? -15.904 -3.731  -22.421 1.00 35.58 ? 339  LEU A CD1   1 
ATOM   2789 C  CD2   . LEU A 1 349 ? -15.502 -6.186  -22.683 1.00 35.68 ? 339  LEU A CD2   1 
ATOM   2790 N  N     . PRO A 1 350 ? -19.650 -7.851  -19.689 1.00 33.11 ? 340  PRO A N     1 
ATOM   2791 C  CA    . PRO A 1 350 ? -20.259 -8.106  -18.381 1.00 32.80 ? 340  PRO A CA    1 
ATOM   2792 C  C     . PRO A 1 350 ? -19.262 -7.904  -17.241 1.00 32.14 ? 340  PRO A C     1 
ATOM   2793 O  O     . PRO A 1 350 ? -18.071 -8.197  -17.406 1.00 31.23 ? 340  PRO A O     1 
ATOM   2794 C  CB    . PRO A 1 350 ? -20.696 -9.583  -18.463 1.00 33.76 ? 340  PRO A CB    1 
ATOM   2795 C  CG    . PRO A 1 350 ? -20.683 -9.926  -19.910 1.00 34.50 ? 340  PRO A CG    1 
ATOM   2796 C  CD    . PRO A 1 350 ? -19.632 -9.066  -20.531 1.00 33.96 ? 340  PRO A CD    1 
ATOM   2797 N  N     . PHE A 1 351 ? -19.744 -7.397  -16.104 1.00 31.72 ? 341  PHE A N     1 
ATOM   2798 C  CA    . PHE A 1 351 ? -18.871 -7.060  -14.967 1.00 31.46 ? 341  PHE A CA    1 
ATOM   2799 C  C     . PHE A 1 351 ? -18.209 -8.260  -14.295 1.00 32.74 ? 341  PHE A C     1 
ATOM   2800 O  O     . PHE A 1 351 ? -17.152 -8.120  -13.670 1.00 31.93 ? 341  PHE A O     1 
ATOM   2801 C  CB    . PHE A 1 351 ? -19.642 -6.249  -13.907 1.00 31.08 ? 341  PHE A CB    1 
ATOM   2802 C  CG    . PHE A 1 351 ? -20.210 -4.944  -14.416 1.00 29.92 ? 341  PHE A CG    1 
ATOM   2803 C  CD1   . PHE A 1 351 ? -19.447 -4.067  -15.188 1.00 29.46 ? 341  PHE A CD1   1 
ATOM   2804 C  CD2   . PHE A 1 351 ? -21.510 -4.585  -14.103 1.00 30.00 ? 341  PHE A CD2   1 
ATOM   2805 C  CE1   . PHE A 1 351 ? -19.986 -2.869  -15.644 1.00 29.11 ? 341  PHE A CE1   1 
ATOM   2806 C  CE2   . PHE A 1 351 ? -22.058 -3.391  -14.551 1.00 29.91 ? 341  PHE A CE2   1 
ATOM   2807 C  CZ    . PHE A 1 351 ? -21.294 -2.527  -15.320 1.00 29.58 ? 341  PHE A CZ    1 
ATOM   2808 N  N     . GLY A 1 352 ? -18.821 -9.437  -14.426 1.00 34.82 ? 342  GLY A N     1 
ATOM   2809 C  CA    . GLY A 1 352 ? -18.294 -10.670 -13.832 1.00 36.23 ? 342  GLY A CA    1 
ATOM   2810 C  C     . GLY A 1 352 ? -17.206 -11.379 -14.619 1.00 37.62 ? 342  GLY A C     1 
ATOM   2811 O  O     . GLY A 1 352 ? -16.748 -12.445 -14.198 1.00 38.64 ? 342  GLY A O     1 
ATOM   2812 N  N     . SER A 1 353 ? -16.791 -10.802 -15.749 1.00 37.74 ? 343  SER A N     1 
ATOM   2813 C  CA    . SER A 1 353 ? -15.786 -11.401 -16.626 1.00 38.80 ? 343  SER A CA    1 
ATOM   2814 C  C     . SER A 1 353 ? -14.766 -10.374 -17.076 1.00 37.11 ? 343  SER A C     1 
ATOM   2815 O  O     . SER A 1 353 ? -15.028 -9.171  -17.053 1.00 34.59 ? 343  SER A O     1 
ATOM   2816 C  CB    . SER A 1 353 ? -16.452 -11.986 -17.872 1.00 39.70 ? 343  SER A CB    1 
ATOM   2817 O  OG    . SER A 1 353 ? -17.453 -12.921 -17.522 1.00 42.51 ? 343  SER A OG    1 
ATOM   2818 N  N     . ASP A 1 354 ? -13.599 -10.873 -17.478 1.00 37.10 ? 344  ASP A N     1 
ATOM   2819 C  CA    . ASP A 1 354 ? -12.631 -10.088 -18.223 1.00 37.73 ? 344  ASP A CA    1 
ATOM   2820 C  C     . ASP A 1 354 ? -12.981 -10.272 -19.691 1.00 38.89 ? 344  ASP A C     1 
ATOM   2821 O  O     . ASP A 1 354 ? -13.348 -11.367 -20.112 1.00 40.34 ? 344  ASP A O     1 
ATOM   2822 C  CB    . ASP A 1 354 ? -11.199 -10.560 -17.956 1.00 38.12 ? 344  ASP A CB    1 
ATOM   2823 C  CG    . ASP A 1 354 ? -10.761 -10.356 -16.515 1.00 38.62 ? 344  ASP A CG    1 
ATOM   2824 O  OD1   . ASP A 1 354 ? -11.454 -9.648  -15.739 1.00 37.95 ? 344  ASP A OD1   1 
ATOM   2825 O  OD2   . ASP A 1 354 ? -9.700  -10.901 -16.148 1.00 38.88 ? 344  ASP A OD2   1 
ATOM   2826 N  N     . GLY A 1 355 ? -12.878 -9.198  -20.462 1.00 37.74 ? 345  GLY A N     1 
ATOM   2827 C  CA    . GLY A 1 355 ? -13.243 -9.212  -21.883 1.00 37.80 ? 345  GLY A CA    1 
ATOM   2828 C  C     . GLY A 1 355 ? -12.195 -8.529  -22.741 1.00 37.27 ? 345  GLY A C     1 
ATOM   2829 O  O     . GLY A 1 355 ? -11.593 -7.544  -22.327 1.00 35.97 ? 345  GLY A O     1 
ATOM   2830 N  N     . VAL A 1 356 ? -11.982 -9.056  -23.942 1.00 36.52 ? 346  VAL A N     1 
ATOM   2831 C  CA    . VAL A 1 356 ? -11.050 -8.473  -24.900 1.00 36.93 ? 346  VAL A CA    1 
ATOM   2832 C  C     . VAL A 1 356 ? -11.774 -7.455  -25.786 1.00 35.94 ? 346  VAL A C     1 
ATOM   2833 O  O     . VAL A 1 356 ? -12.779 -7.777  -26.416 1.00 36.90 ? 346  VAL A O     1 
ATOM   2834 C  CB    . VAL A 1 356 ? -10.408 -9.568  -25.794 1.00 38.21 ? 346  VAL A CB    1 
ATOM   2835 C  CG1   . VAL A 1 356 ? -9.368  -8.967  -26.729 1.00 38.71 ? 346  VAL A CG1   1 
ATOM   2836 C  CG2   . VAL A 1 356 ? -9.763  -10.652 -24.938 1.00 38.95 ? 346  VAL A CG2   1 
ATOM   2837 N  N     . PHE A 1 357 ? -11.255 -6.230  -25.834 1.00 35.05 ? 347  PHE A N     1 
ATOM   2838 C  CA    . PHE A 1 357 ? -11.703 -5.238  -26.803 1.00 34.16 ? 347  PHE A CA    1 
ATOM   2839 C  C     . PHE A 1 357 ? -11.186 -5.609  -28.187 1.00 35.44 ? 347  PHE A C     1 
ATOM   2840 O  O     . PHE A 1 357 ? -10.008 -5.915  -28.334 1.00 34.92 ? 347  PHE A O     1 
ATOM   2841 C  CB    . PHE A 1 357 ? -11.181 -3.834  -26.464 1.00 33.79 ? 347  PHE A CB    1 
ATOM   2842 C  CG    . PHE A 1 357 ? -11.537 -2.792  -27.498 1.00 33.10 ? 347  PHE A CG    1 
ATOM   2843 C  CD1   . PHE A 1 357 ? -12.745 -2.115  -27.429 1.00 33.15 ? 347  PHE A CD1   1 
ATOM   2844 C  CD2   . PHE A 1 357 ? -10.682 -2.507  -28.555 1.00 33.33 ? 347  PHE A CD2   1 
ATOM   2845 C  CE1   . PHE A 1 357 ? -13.087 -1.167  -28.385 1.00 32.55 ? 347  PHE A CE1   1 
ATOM   2846 C  CE2   . PHE A 1 357 ? -11.018 -1.561  -29.515 1.00 33.27 ? 347  PHE A CE2   1 
ATOM   2847 C  CZ    . PHE A 1 357 ? -12.225 -0.889  -29.425 1.00 33.30 ? 347  PHE A CZ    1 
ATOM   2848 N  N     . THR A 1 358 ? -12.064 -5.554  -29.186 1.00 35.81 ? 348  THR A N     1 
ATOM   2849 C  CA    . THR A 1 358 ? -11.647 -5.535  -30.600 1.00 37.56 ? 348  THR A CA    1 
ATOM   2850 C  C     . THR A 1 358 ? -12.457 -4.479  -31.355 1.00 37.25 ? 348  THR A C     1 
ATOM   2851 O  O     . THR A 1 358 ? -13.648 -4.320  -31.082 1.00 36.20 ? 348  THR A O     1 
ATOM   2852 C  CB    . THR A 1 358 ? -11.842 -6.897  -31.312 1.00 38.94 ? 348  THR A CB    1 
ATOM   2853 O  OG1   . THR A 1 358 ? -13.227 -7.097  -31.628 1.00 38.44 ? 348  THR A OG1   1 
ATOM   2854 C  CG2   . THR A 1 358 ? -11.323 -8.066  -30.456 1.00 39.83 ? 348  THR A CG2   1 
ATOM   2855 N  N     . PRO A 1 359 ? -11.825 -3.758  -32.307 1.00 38.41 ? 349  PRO A N     1 
ATOM   2856 C  CA    . PRO A 1 359 ? -12.591 -2.790  -33.116 1.00 38.58 ? 349  PRO A CA    1 
ATOM   2857 C  C     . PRO A 1 359 ? -13.729 -3.412  -33.935 1.00 39.12 ? 349  PRO A C     1 
ATOM   2858 O  O     . PRO A 1 359 ? -14.731 -2.754  -34.176 1.00 37.80 ? 349  PRO A O     1 
ATOM   2859 C  CB    . PRO A 1 359 ? -11.540 -2.162  -34.048 1.00 39.03 ? 349  PRO A CB    1 
ATOM   2860 C  CG    . PRO A 1 359 ? -10.296 -2.960  -33.885 1.00 39.50 ? 349  PRO A CG    1 
ATOM   2861 C  CD    . PRO A 1 359 ? -10.377 -3.712  -32.599 1.00 39.07 ? 349  PRO A CD    1 
ATOM   2862 N  N     . GLU A 1 360 ? -13.564 -4.669  -34.342 1.00 41.06 ? 350  GLU A N     1 
ATOM   2863 C  CA    . GLU A 1 360 ? -14.581 -5.382  -35.122 1.00 42.41 ? 350  GLU A CA    1 
ATOM   2864 C  C     . GLU A 1 360 ? -15.852 -5.619  -34.294 1.00 40.48 ? 350  GLU A C     1 
ATOM   2865 O  O     . GLU A 1 360 ? -16.966 -5.452  -34.797 1.00 40.45 ? 350  GLU A O     1 
ATOM   2866 C  CB    . GLU A 1 360 ? -14.028 -6.718  -35.655 1.00 44.57 ? 350  GLU A CB    1 
ATOM   2867 C  CG    . GLU A 1 360 ? -12.954 -6.581  -36.742 1.00 46.90 ? 350  GLU A CG    1 
ATOM   2868 C  CD    . GLU A 1 360 ? -11.558 -6.238  -36.222 1.00 48.94 ? 350  GLU A CD    1 
ATOM   2869 O  OE1   . GLU A 1 360 ? -11.281 -6.446  -35.017 1.00 48.94 ? 350  GLU A OE1   1 
ATOM   2870 O  OE2   . GLU A 1 360 ? -10.721 -5.751  -37.024 1.00 50.77 ? 350  GLU A OE2   1 
ATOM   2871 N  N     . ALA A 1 361 ? -15.670 -6.001  -33.029 1.00 38.28 ? 351  ALA A N     1 
ATOM   2872 C  CA    . ALA A 1 361 ? -16.783 -6.205  -32.097 1.00 36.76 ? 351  ALA A CA    1 
ATOM   2873 C  C     . ALA A 1 361 ? -17.500 -4.889  -31.758 1.00 34.65 ? 351  ALA A C     1 
ATOM   2874 O  O     . ALA A 1 361 ? -18.726 -4.849  -31.673 1.00 34.33 ? 351  ALA A O     1 
ATOM   2875 C  CB    . ALA A 1 361 ? -16.289 -6.883  -30.828 1.00 37.20 ? 351  ALA A CB    1 
ATOM   2876 N  N     . PHE A 1 362 ? -16.727 -3.821  -31.571 1.00 32.60 ? 352  PHE A N     1 
ATOM   2877 C  CA    . PHE A 1 362 ? -17.281 -2.468  -31.381 1.00 31.03 ? 352  PHE A CA    1 
ATOM   2878 C  C     . PHE A 1 362 ? -18.169 -2.015  -32.549 1.00 31.30 ? 352  PHE A C     1 
ATOM   2879 O  O     . PHE A 1 362 ? -19.285 -1.527  -32.351 1.00 29.71 ? 352  PHE A O     1 
ATOM   2880 C  CB    . PHE A 1 362 ? -16.153 -1.454  -31.194 1.00 30.08 ? 352  PHE A CB    1 
ATOM   2881 C  CG    . PHE A 1 362 ? -16.636 -0.090  -30.794 1.00 28.73 ? 352  PHE A CG    1 
ATOM   2882 C  CD1   . PHE A 1 362 ? -16.650 0.287   -29.456 1.00 28.27 ? 352  PHE A CD1   1 
ATOM   2883 C  CD2   . PHE A 1 362 ? -17.100 0.812   -31.746 1.00 28.60 ? 352  PHE A CD2   1 
ATOM   2884 C  CE1   . PHE A 1 362 ? -17.111 1.540   -29.077 1.00 28.14 ? 352  PHE A CE1   1 
ATOM   2885 C  CE2   . PHE A 1 362 ? -17.560 2.062   -31.377 1.00 28.94 ? 352  PHE A CE2   1 
ATOM   2886 C  CZ    . PHE A 1 362 ? -17.559 2.432   -30.036 1.00 28.23 ? 352  PHE A CZ    1 
ATOM   2887 N  N     . VAL A 1 363 ? -17.649 -2.161  -33.764 1.00 30.89 ? 353  VAL A N     1 
ATOM   2888 C  CA    . VAL A 1 363 ? -18.371 -1.756  -34.969 1.00 32.67 ? 353  VAL A CA    1 
ATOM   2889 C  C     . VAL A 1 363 ? -19.653 -2.566  -35.181 1.00 32.69 ? 353  VAL A C     1 
ATOM   2890 O  O     . VAL A 1 363 ? -20.698 -1.994  -35.513 1.00 31.76 ? 353  VAL A O     1 
ATOM   2891 C  CB    . VAL A 1 363 ? -17.468 -1.852  -36.227 1.00 33.27 ? 353  VAL A CB    1 
ATOM   2892 C  CG1   . VAL A 1 363 ? -18.266 -1.658  -37.513 1.00 34.66 ? 353  VAL A CG1   1 
ATOM   2893 C  CG2   . VAL A 1 363 ? -16.379 -0.793  -36.155 1.00 34.49 ? 353  VAL A CG2   1 
ATOM   2894 N  N     . GLU A 1 364 ? -19.566 -3.883  -35.010 1.00 34.81 ? 354  GLU A N     1 
ATOM   2895 C  CA    . GLU A 1 364 ? -20.727 -4.751  -35.206 1.00 37.17 ? 354  GLU A CA    1 
ATOM   2896 C  C     . GLU A 1 364 ? -21.801 -4.428  -34.168 1.00 36.12 ? 354  GLU A C     1 
ATOM   2897 O  O     . GLU A 1 364 ? -22.975 -4.246  -34.494 1.00 34.38 ? 354  GLU A O     1 
ATOM   2898 C  CB    . GLU A 1 364 ? -20.333 -6.236  -35.133 1.00 40.88 ? 354  GLU A CB    1 
ATOM   2899 C  CG    . GLU A 1 364 ? -19.650 -6.769  -36.393 1.00 43.96 ? 354  GLU A CG    1 
ATOM   2900 C  CD    . GLU A 1 364 ? -19.868 -8.266  -36.628 1.00 47.01 ? 354  GLU A CD    1 
ATOM   2901 O  OE1   . GLU A 1 364 ? -19.872 -8.694  -37.812 1.00 50.19 ? 354  GLU A OE1   1 
ATOM   2902 O  OE2   . GLU A 1 364 ? -20.048 -9.021  -35.647 1.00 48.69 ? 354  GLU A OE2   1 
ATOM   2903 N  N     . ARG A 1 365 ? -21.376 -4.325  -32.917 1.00 35.22 ? 355  ARG A N     1 
ATOM   2904 C  CA    . ARG A 1 365 ? -22.303 -4.113  -31.831 1.00 35.20 ? 355  ARG A CA    1 
ATOM   2905 C  C     . ARG A 1 365 ? -23.096 -2.825  -32.029 1.00 35.17 ? 355  ARG A C     1 
ATOM   2906 O  O     . ARG A 1 365 ? -24.320 -2.835  -31.943 1.00 36.16 ? 355  ARG A O     1 
ATOM   2907 C  CB    . ARG A 1 365 ? -21.556 -4.138  -30.492 1.00 34.99 ? 355  ARG A CB    1 
ATOM   2908 C  CG    . ARG A 1 365 ? -22.409 -3.983  -29.253 1.00 34.53 ? 355  ARG A CG    1 
ATOM   2909 C  CD    . ARG A 1 365 ? -23.519 -5.015  -29.179 1.00 34.28 ? 355  ARG A CD    1 
ATOM   2910 N  NE    . ARG A 1 365 ? -23.058 -6.337  -28.770 1.00 33.86 ? 355  ARG A NE    1 
ATOM   2911 C  CZ    . ARG A 1 365 ? -23.829 -7.422  -28.715 1.00 34.29 ? 355  ARG A CZ    1 
ATOM   2912 N  NH1   . ARG A 1 365 ? -25.117 -7.374  -29.065 1.00 34.08 ? 355  ARG A NH1   1 
ATOM   2913 N  NH2   . ARG A 1 365 ? -23.307 -8.574  -28.305 1.00 34.93 ? 355  ARG A NH2   1 
ATOM   2914 N  N     . THR A 1 366 ? -22.405 -1.743  -32.368 1.00 34.70 ? 356  THR A N     1 
ATOM   2915 C  CA    . THR A 1 366 ? -23.043 -0.436  -32.524 1.00 35.57 ? 356  THR A CA    1 
ATOM   2916 C  C     . THR A 1 366 ? -23.806 -0.231  -33.848 1.00 36.02 ? 356  THR A C     1 
ATOM   2917 O  O     . THR A 1 366 ? -24.841 0.431   -33.853 1.00 36.53 ? 356  THR A O     1 
ATOM   2918 C  CB    . THR A 1 366 ? -22.039 0.693   -32.278 1.00 36.96 ? 356  THR A CB    1 
ATOM   2919 O  OG1   . THR A 1 366 ? -20.994 0.632   -33.249 1.00 36.36 ? 356  THR A OG1   1 
ATOM   2920 C  CG2   . THR A 1 366 ? -21.458 0.560   -30.846 1.00 37.07 ? 356  THR A CG2   1 
ATOM   2921 N  N     . ASN A 1 367 ? -23.341 -0.820  -34.951 1.00 33.83 ? 357  ASN A N     1 
ATOM   2922 C  CA    . ASN A 1 367 ? -24.109 -0.765  -36.208 1.00 34.29 ? 357  ASN A CA    1 
ATOM   2923 C  C     . ASN A 1 367 ? -25.348 -1.650  -36.200 1.00 32.46 ? 357  ASN A C     1 
ATOM   2924 O  O     . ASN A 1 367 ? -26.417 -1.215  -36.628 1.00 33.16 ? 357  ASN A O     1 
ATOM   2925 C  CB    . ASN A 1 367 ? -23.247 -1.102  -37.422 1.00 35.16 ? 357  ASN A CB    1 
ATOM   2926 C  CG    . ASN A 1 367 ? -22.512 0.102   -37.941 1.00 36.63 ? 357  ASN A CG    1 
ATOM   2927 O  OD1   . ASN A 1 367 ? -21.340 0.289   -37.653 1.00 37.69 ? 357  ASN A OD1   1 
ATOM   2928 N  ND2   . ASN A 1 367 ? -23.217 0.955   -38.675 1.00 37.87 ? 357  ASN A ND2   1 
ATOM   2929 N  N     . PHE A 1 368 ? -25.204 -2.893  -35.748 1.00 31.20 ? 358  PHE A N     1 
ATOM   2930 C  CA    . PHE A 1 368 ? -26.315 -3.855  -35.807 1.00 30.69 ? 358  PHE A CA    1 
ATOM   2931 C  C     . PHE A 1 368 ? -27.416 -3.546  -34.802 1.00 29.76 ? 358  PHE A C     1 
ATOM   2932 O  O     . PHE A 1 368 ? -28.592 -3.615  -35.142 1.00 28.76 ? 358  PHE A O     1 
ATOM   2933 C  CB    . PHE A 1 368 ? -25.847 -5.298  -35.594 1.00 31.31 ? 358  PHE A CB    1 
ATOM   2934 C  CG    . PHE A 1 368 ? -24.821 -5.780  -36.596 1.00 31.35 ? 358  PHE A CG    1 
ATOM   2935 C  CD1   . PHE A 1 368 ? -24.505 -5.050  -37.742 1.00 31.42 ? 358  PHE A CD1   1 
ATOM   2936 C  CD2   . PHE A 1 368 ? -24.176 -6.991  -36.388 1.00 32.23 ? 358  PHE A CD2   1 
ATOM   2937 C  CE1   . PHE A 1 368 ? -23.550 -5.505  -38.633 1.00 31.83 ? 358  PHE A CE1   1 
ATOM   2938 C  CE2   . PHE A 1 368 ? -23.221 -7.452  -37.285 1.00 32.31 ? 358  PHE A CE2   1 
ATOM   2939 C  CZ    . PHE A 1 368 ? -22.917 -6.710  -38.409 1.00 32.12 ? 358  PHE A CZ    1 
ATOM   2940 N  N     . ASP A 1 369 ? -27.037 -3.229  -33.568 1.00 28.95 ? 359  ASP A N     1 
ATOM   2941 C  CA    . ASP A 1 369 ? -28.026 -2.972  -32.514 1.00 28.59 ? 359  ASP A CA    1 
ATOM   2942 C  C     . ASP A 1 369 ? -28.572 -1.551  -32.540 1.00 27.59 ? 359  ASP A C     1 
ATOM   2943 O  O     . ASP A 1 369 ? -29.774 -1.363  -32.402 1.00 27.89 ? 359  ASP A O     1 
ATOM   2944 C  CB    . ASP A 1 369 ? -27.425 -3.250  -31.136 1.00 29.31 ? 359  ASP A CB    1 
ATOM   2945 C  CG    . ASP A 1 369 ? -27.165 -4.726  -30.889 1.00 30.87 ? 359  ASP A CG    1 
ATOM   2946 O  OD1   . ASP A 1 369 ? -27.613 -5.577  -31.693 1.00 32.55 ? 359  ASP A OD1   1 
ATOM   2947 O  OD2   . ASP A 1 369 ? -26.525 -5.038  -29.866 1.00 30.73 ? 359  ASP A OD2   1 
ATOM   2948 N  N     . LEU A 1 370 ? -27.694 -0.552  -32.658 1.00 26.02 ? 360  LEU A N     1 
ATOM   2949 C  CA    . LEU A 1 370 ? -28.138 0.847   -32.590 1.00 25.84 ? 360  LEU A CA    1 
ATOM   2950 C  C     . LEU A 1 370 ? -28.694 1.345   -33.918 1.00 26.62 ? 360  LEU A C     1 
ATOM   2951 O  O     . LEU A 1 370 ? -29.890 1.551   -34.032 1.00 26.23 ? 360  LEU A O     1 
ATOM   2952 C  CB    . LEU A 1 370 ? -27.044 1.778   -32.056 1.00 25.44 ? 360  LEU A CB    1 
ATOM   2953 C  CG    . LEU A 1 370 ? -26.470 1.359   -30.707 1.00 25.14 ? 360  LEU A CG    1 
ATOM   2954 C  CD1   . LEU A 1 370 ? -25.341 2.295   -30.325 1.00 24.90 ? 360  LEU A CD1   1 
ATOM   2955 C  CD2   . LEU A 1 370 ? -27.513 1.378   -29.602 1.00 25.28 ? 360  LEU A CD2   1 
ATOM   2956 N  N     . ALA A 1 371 ? -27.832 1.515   -34.920 1.00 26.99 ? 361  ALA A N     1 
ATOM   2957 C  CA    . ALA A 1 371 ? -28.265 2.089   -36.194 1.00 28.26 ? 361  ALA A CA    1 
ATOM   2958 C  C     . ALA A 1 371 ? -29.312 1.219   -36.882 1.00 28.90 ? 361  ALA A C     1 
ATOM   2959 O  O     . ALA A 1 371 ? -30.345 1.718   -37.337 1.00 29.11 ? 361  ALA A O     1 
ATOM   2960 C  CB    . ALA A 1 371 ? -27.069 2.298   -37.111 1.00 28.34 ? 361  ALA A CB    1 
ATOM   2961 N  N     . ASN A 1 372 ? -29.056 -0.084  -36.930 1.00 29.04 ? 362  ASN A N     1 
ATOM   2962 C  CA    . ASN A 1 372 ? -29.927 -0.989  -37.690 1.00 30.09 ? 362  ASN A CA    1 
ATOM   2963 C  C     . ASN A 1 372 ? -31.206 -1.309  -36.927 1.00 31.16 ? 362  ASN A C     1 
ATOM   2964 O  O     . ASN A 1 372 ? -32.283 -0.947  -37.374 1.00 33.54 ? 362  ASN A O     1 
ATOM   2965 C  CB    . ASN A 1 372 ? -29.176 -2.256  -38.082 1.00 29.63 ? 362  ASN A CB    1 
ATOM   2966 C  CG    . ASN A 1 372 ? -28.059 -1.987  -39.078 1.00 30.24 ? 362  ASN A CG    1 
ATOM   2967 O  OD1   . ASN A 1 372 ? -27.829 -0.843  -39.485 1.00 29.98 ? 362  ASN A OD1   1 
ATOM   2968 N  ND2   . ASN A 1 372 ? -27.343 -3.045  -39.460 1.00 29.61 ? 362  ASN A ND2   1 
ATOM   2969 N  N     . ASP A 1 373 ? -31.092 -1.949  -35.770 1.00 29.89 ? 363  ASP A N     1 
ATOM   2970 C  CA    . ASP A 1 373 ? -32.277 -2.462  -35.070 1.00 30.18 ? 363  ASP A CA    1 
ATOM   2971 C  C     . ASP A 1 373 ? -33.147 -1.317  -34.529 1.00 29.24 ? 363  ASP A C     1 
ATOM   2972 O  O     . ASP A 1 373 ? -34.292 -1.152  -34.940 1.00 28.18 ? 363  ASP A O     1 
ATOM   2973 C  CB    . ASP A 1 373 ? -31.872 -3.427  -33.945 1.00 31.83 ? 363  ASP A CB    1 
ATOM   2974 C  CG    . ASP A 1 373 ? -32.885 -4.534  -33.700 1.00 34.17 ? 363  ASP A CG    1 
ATOM   2975 O  OD1   . ASP A 1 373 ? -34.053 -4.433  -34.129 1.00 36.86 ? 363  ASP A OD1   1 
ATOM   2976 O  OD2   . ASP A 1 373 ? -32.494 -5.533  -33.060 1.00 35.69 ? 363  ASP A OD2   1 
ATOM   2977 N  N     . LEU A 1 374 ? -32.593 -0.513  -33.627 1.00 27.30 ? 364  LEU A N     1 
ATOM   2978 C  CA    . LEU A 1 374 ? -33.371 0.579   -33.023 1.00 27.45 ? 364  LEU A CA    1 
ATOM   2979 C  C     . LEU A 1 374 ? -33.606 1.731   -33.992 1.00 27.38 ? 364  LEU A C     1 
ATOM   2980 O  O     . LEU A 1 374 ? -34.716 2.241   -34.086 1.00 27.59 ? 364  LEU A O     1 
ATOM   2981 C  CB    . LEU A 1 374 ? -32.708 1.103   -31.740 1.00 27.42 ? 364  LEU A CB    1 
ATOM   2982 C  CG    . LEU A 1 374 ? -33.453 2.210   -30.978 1.00 27.59 ? 364  LEU A CG    1 
ATOM   2983 C  CD1   . LEU A 1 374 ? -34.903 1.870   -30.661 1.00 27.95 ? 364  LEU A CD1   1 
ATOM   2984 C  CD2   . LEU A 1 374 ? -32.703 2.496   -29.687 1.00 27.67 ? 364  LEU A CD2   1 
ATOM   2985 N  N     . GLY A 1 375 ? -32.558 2.149   -34.699 1.00 27.69 ? 365  GLY A N     1 
ATOM   2986 C  CA    . GLY A 1 375 ? -32.648 3.304   -35.596 1.00 27.81 ? 365  GLY A CA    1 
ATOM   2987 C  C     . GLY A 1 375 ? -33.656 3.107   -36.724 1.00 28.20 ? 365  GLY A C     1 
ATOM   2988 O  O     . GLY A 1 375 ? -34.456 3.988   -37.004 1.00 28.06 ? 365  GLY A O     1 
ATOM   2989 N  N     . ASN A 1 376 ? -33.603 1.956   -37.385 1.00 28.58 ? 366  ASN A N     1 
ATOM   2990 C  CA    . ASN A 1 376 ? -34.593 1.646   -38.432 1.00 29.41 ? 366  ASN A CA    1 
ATOM   2991 C  C     . ASN A 1 376 ? -36.004 1.457   -37.887 1.00 29.25 ? 366  ASN A C     1 
ATOM   2992 O  O     . ASN A 1 376 ? -36.968 1.807   -38.566 1.00 28.97 ? 366  ASN A O     1 
ATOM   2993 C  CB    . ASN A 1 376 ? -34.200 0.417   -39.253 1.00 29.82 ? 366  ASN A CB    1 
ATOM   2994 C  CG    . ASN A 1 376 ? -32.977 0.663   -40.118 1.00 30.07 ? 366  ASN A CG    1 
ATOM   2995 O  OD1   . ASN A 1 376 ? -32.738 1.783   -40.562 1.00 31.02 ? 366  ASN A OD1   1 
ATOM   2996 N  ND2   . ASN A 1 376 ? -32.207 -0.382  -40.367 1.00 29.23 ? 366  ASN A ND2   1 
ATOM   2997 N  N     . LEU A 1 377 ? -36.135 0.896   -36.688 1.00 29.29 ? 367  LEU A N     1 
ATOM   2998 C  CA    . LEU A 1 377 ? -37.468 0.748   -36.081 1.00 29.87 ? 367  LEU A CA    1 
ATOM   2999 C  C     . LEU A 1 377 ? -38.168 2.098   -35.977 1.00 30.22 ? 367  LEU A C     1 
ATOM   3000 O  O     . LEU A 1 377 ? -39.332 2.232   -36.356 1.00 30.30 ? 367  LEU A O     1 
ATOM   3001 C  CB    . LEU A 1 377 ? -37.401 0.075   -34.711 1.00 29.65 ? 367  LEU A CB    1 
ATOM   3002 C  CG    . LEU A 1 377 ? -38.693 0.102   -33.872 1.00 30.51 ? 367  LEU A CG    1 
ATOM   3003 C  CD1   . LEU A 1 377 ? -39.834 -0.596  -34.601 1.00 30.65 ? 367  LEU A CD1   1 
ATOM   3004 C  CD2   . LEU A 1 377 ? -38.449 -0.530  -32.509 1.00 30.01 ? 367  LEU A CD2   1 
ATOM   3005 N  N     . VAL A 1 378 ? -37.447 3.099   -35.485 1.00 30.32 ? 368  VAL A N     1 
ATOM   3006 C  CA    . VAL A 1 378 ? -38.021 4.429   -35.288 1.00 31.31 ? 368  VAL A CA    1 
ATOM   3007 C  C     . VAL A 1 378 ? -38.341 5.072   -36.640 1.00 32.44 ? 368  VAL A C     1 
ATOM   3008 O  O     . VAL A 1 378 ? -39.446 5.591   -36.842 1.00 33.56 ? 368  VAL A O     1 
ATOM   3009 C  CB    . VAL A 1 378 ? -37.107 5.338   -34.436 1.00 30.99 ? 368  VAL A CB    1 
ATOM   3010 C  CG1   . VAL A 1 378 ? -37.690 6.738   -34.309 1.00 30.96 ? 368  VAL A CG1   1 
ATOM   3011 C  CG2   . VAL A 1 378 ? -36.922 4.742   -33.045 1.00 31.09 ? 368  VAL A CG2   1 
ATOM   3012 N  N     . ASN A 1 379 ? -37.401 5.004   -37.576 1.00 32.50 ? 369  ASN A N     1 
ATOM   3013 C  CA    . ASN A 1 379 ? -37.618 5.637   -38.872 1.00 33.78 ? 369  ASN A CA    1 
ATOM   3014 C  C     . ASN A 1 379 ? -38.743 4.970   -39.667 1.00 33.19 ? 369  ASN A C     1 
ATOM   3015 O  O     . ASN A 1 379 ? -39.542 5.658   -40.290 1.00 33.01 ? 369  ASN A O     1 
ATOM   3016 C  CB    . ASN A 1 379 ? -36.346 5.680   -39.714 1.00 35.01 ? 369  ASN A CB    1 
ATOM   3017 C  CG    . ASN A 1 379 ? -36.409 6.765   -40.770 1.00 37.11 ? 369  ASN A CG    1 
ATOM   3018 O  OD1   . ASN A 1 379 ? -36.385 7.960   -40.452 1.00 39.48 ? 369  ASN A OD1   1 
ATOM   3019 N  ND2   . ASN A 1 379 ? -36.516 6.361   -42.025 1.00 37.83 ? 369  ASN A ND2   1 
ATOM   3020 N  N     . ARG A 1 380 ? -38.795 3.641   -39.643 1.00 32.60 ? 370  ARG A N     1 
ATOM   3021 C  CA    . ARG A 1 380 ? -39.882 2.908   -40.313 1.00 33.05 ? 370  ARG A CA    1 
ATOM   3022 C  C     . ARG A 1 380 ? -41.243 3.318   -39.755 1.00 33.56 ? 370  ARG A C     1 
ATOM   3023 O  O     . ARG A 1 380 ? -42.191 3.534   -40.505 1.00 32.98 ? 370  ARG A O     1 
ATOM   3024 C  CB    . ARG A 1 380 ? -39.725 1.407   -40.129 1.00 33.28 ? 370  ARG A CB    1 
ATOM   3025 C  CG    . ARG A 1 380 ? -38.608 0.786   -40.943 1.00 33.65 ? 370  ARG A CG    1 
ATOM   3026 C  CD    . ARG A 1 380 ? -38.322 -0.617  -40.443 1.00 33.33 ? 370  ARG A CD    1 
ATOM   3027 N  NE    . ARG A 1 380 ? -39.179 -1.633  -41.061 1.00 33.11 ? 370  ARG A NE    1 
ATOM   3028 C  CZ    . ARG A 1 380 ? -39.261 -2.902  -40.664 1.00 33.82 ? 370  ARG A CZ    1 
ATOM   3029 N  NH1   . ARG A 1 380 ? -38.576 -3.340  -39.604 1.00 33.61 ? 370  ARG A NH1   1 
ATOM   3030 N  NH2   . ARG A 1 380 ? -40.044 -3.754  -41.327 1.00 33.67 ? 370  ARG A NH2   1 
ATOM   3031 N  N     . THR A 1 381 ? -41.310 3.425   -38.432 1.00 32.44 ? 371  THR A N     1 
ATOM   3032 C  CA    . THR A 1 381 ? -42.563 3.708   -37.728 1.00 33.43 ? 371  THR A CA    1 
ATOM   3033 C  C     . THR A 1 381 ? -43.057 5.114   -38.045 1.00 34.53 ? 371  THR A C     1 
ATOM   3034 O  O     . THR A 1 381 ? -44.196 5.289   -38.465 1.00 34.47 ? 371  THR A O     1 
ATOM   3035 C  CB    . THR A 1 381 ? -42.401 3.521   -36.208 1.00 32.44 ? 371  THR A CB    1 
ATOM   3036 O  OG1   . THR A 1 381 ? -42.103 2.150   -35.938 1.00 30.84 ? 371  THR A OG1   1 
ATOM   3037 C  CG2   . THR A 1 381 ? -43.682 3.885   -35.453 1.00 32.43 ? 371  THR A CG2   1 
ATOM   3038 N  N     . ILE A 1 382 ? -42.191 6.100   -37.853 1.00 35.72 ? 372  ILE A N     1 
ATOM   3039 C  CA    . ILE A 1 382 ? -42.533 7.495   -38.145 1.00 37.46 ? 372  ILE A CA    1 
ATOM   3040 C  C     . ILE A 1 382 ? -42.896 7.685   -39.620 1.00 38.85 ? 372  ILE A C     1 
ATOM   3041 O  O     . ILE A 1 382 ? -43.852 8.391   -39.931 1.00 38.82 ? 372  ILE A O     1 
ATOM   3042 C  CB    . ILE A 1 382 ? -41.416 8.467   -37.715 1.00 38.43 ? 372  ILE A CB    1 
ATOM   3043 C  CG1   . ILE A 1 382 ? -41.309 8.475   -36.180 1.00 38.52 ? 372  ILE A CG1   1 
ATOM   3044 C  CG2   . ILE A 1 382 ? -41.697 9.885   -38.212 1.00 38.84 ? 372  ILE A CG2   1 
ATOM   3045 C  CD1   . ILE A 1 382 ? -40.070 9.155   -35.634 1.00 38.54 ? 372  ILE A CD1   1 
ATOM   3046 N  N     . SER A 1 383 ? -42.137 7.055   -40.514 1.00 38.96 ? 373  SER A N     1 
ATOM   3047 C  CA    . SER A 1 383 ? -42.415 7.123   -41.960 1.00 39.98 ? 373  SER A CA    1 
ATOM   3048 C  C     . SER A 1 383 ? -43.819 6.632   -42.291 1.00 40.56 ? 373  SER A C     1 
ATOM   3049 O  O     . SER A 1 383 ? -44.528 7.255   -43.083 1.00 40.60 ? 373  SER A O     1 
ATOM   3050 C  CB    . SER A 1 383 ? -41.385 6.316   -42.761 1.00 40.26 ? 373  SER A CB    1 
ATOM   3051 O  OG    . SER A 1 383 ? -40.110 6.928   -42.703 1.00 40.06 ? 373  SER A OG    1 
ATOM   3052 N  N     . MET A 1 384 ? -44.215 5.527   -41.668 1.00 40.57 ? 374  MET A N     1 
ATOM   3053 C  CA    . MET A 1 384 ? -45.557 4.973   -41.857 1.00 41.04 ? 374  MET A CA    1 
ATOM   3054 C  C     . MET A 1 384 ? -46.669 5.868   -41.288 1.00 42.47 ? 374  MET A C     1 
ATOM   3055 O  O     . MET A 1 384 ? -47.730 5.982   -41.894 1.00 41.90 ? 374  MET A O     1 
ATOM   3056 C  CB    . MET A 1 384 ? -45.642 3.559   -41.279 1.00 40.86 ? 374  MET A CB    1 
ATOM   3057 C  CG    . MET A 1 384 ? -44.974 2.511   -42.161 1.00 40.73 ? 374  MET A CG    1 
ATOM   3058 S  SD    . MET A 1 384 ? -45.219 0.818   -41.598 1.00 39.82 ? 374  MET A SD    1 
ATOM   3059 C  CE    . MET A 1 384 ? -44.381 0.848   -40.004 1.00 40.40 ? 374  MET A CE    1 
ATOM   3060 N  N     . VAL A 1 385 ? -46.426 6.504   -40.141 1.00 42.22 ? 375  VAL A N     1 
ATOM   3061 C  CA    . VAL A 1 385 ? -47.394 7.457   -39.568 1.00 43.60 ? 375  VAL A CA    1 
ATOM   3062 C  C     . VAL A 1 385 ? -47.582 8.650   -40.516 1.00 44.10 ? 375  VAL A C     1 
ATOM   3063 O  O     . VAL A 1 385 ? -48.712 9.078   -40.760 1.00 43.50 ? 375  VAL A O     1 
ATOM   3064 C  CB    . VAL A 1 385 ? -46.979 7.943   -38.156 1.00 43.29 ? 375  VAL A CB    1 
ATOM   3065 C  CG1   . VAL A 1 385 ? -47.918 9.026   -37.639 1.00 43.83 ? 375  VAL A CG1   1 
ATOM   3066 C  CG2   . VAL A 1 385 ? -46.984 6.783   -37.177 1.00 43.10 ? 375  VAL A CG2   1 
ATOM   3067 N  N     . ASN A 1 386 ? -46.475 9.170   -41.044 1.00 44.66 ? 376  ASN A N     1 
ATOM   3068 C  CA    . ASN A 1 386 ? -46.512 10.266  -42.018 1.00 46.62 ? 376  ASN A CA    1 
ATOM   3069 C  C     . ASN A 1 386 ? -47.203 9.873   -43.327 1.00 48.29 ? 376  ASN A C     1 
ATOM   3070 O  O     . ASN A 1 386 ? -47.975 10.659  -43.873 1.00 48.30 ? 376  ASN A O     1 
ATOM   3071 C  CB    . ASN A 1 386 ? -45.103 10.798  -42.308 1.00 46.72 ? 376  ASN A CB    1 
ATOM   3072 C  CG    . ASN A 1 386 ? -44.601 11.742  -41.230 1.00 46.95 ? 376  ASN A CG    1 
ATOM   3073 O  OD1   . ASN A 1 386 ? -45.370 12.509  -40.651 1.00 47.86 ? 376  ASN A OD1   1 
ATOM   3074 N  ND2   . ASN A 1 386 ? -43.303 11.703  -40.969 1.00 45.79 ? 376  ASN A ND2   1 
ATOM   3075 N  N     . LYS A 1 387 ? -46.928 8.665   -43.812 1.00 49.18 ? 377  LYS A N     1 
ATOM   3076 C  CA    . LYS A 1 387 ? -47.498 8.186   -45.079 1.00 51.13 ? 377  LYS A CA    1 
ATOM   3077 C  C     . LYS A 1 387 ? -49.001 7.894   -44.992 1.00 51.85 ? 377  LYS A C     1 
ATOM   3078 O  O     . LYS A 1 387 ? -49.762 8.320   -45.859 1.00 51.17 ? 377  LYS A O     1 
ATOM   3079 C  CB    . LYS A 1 387 ? -46.757 6.939   -45.576 1.00 51.87 ? 377  LYS A CB    1 
ATOM   3080 C  CG    . LYS A 1 387 ? -47.278 6.419   -46.911 1.00 52.89 ? 377  LYS A CG    1 
ATOM   3081 C  CD    . LYS A 1 387 ? -46.294 5.496   -47.607 1.00 53.92 ? 377  LYS A CD    1 
ATOM   3082 C  CE    . LYS A 1 387 ? -46.742 5.197   -49.027 1.00 54.84 ? 377  LYS A CE    1 
ATOM   3083 N  NZ    . LYS A 1 387 ? -46.516 6.356   -49.936 1.00 55.80 ? 377  LYS A NZ    1 
ATOM   3084 N  N     . TYR A 1 388 ? -49.408 7.163   -43.957 1.00 51.92 ? 378  TYR A N     1 
ATOM   3085 C  CA    . TYR A 1 388 ? -50.796 6.704   -43.807 1.00 53.04 ? 378  TYR A CA    1 
ATOM   3086 C  C     . TYR A 1 388 ? -51.759 7.659   -43.086 1.00 53.02 ? 378  TYR A C     1 
ATOM   3087 O  O     . TYR A 1 388 ? -52.950 7.648   -43.383 1.00 51.74 ? 378  TYR A O     1 
ATOM   3088 C  CB    . TYR A 1 388 ? -50.837 5.351   -43.092 1.00 53.39 ? 378  TYR A CB    1 
ATOM   3089 C  CG    . TYR A 1 388 ? -49.946 4.270   -43.677 1.00 53.24 ? 378  TYR A CG    1 
ATOM   3090 C  CD1   . TYR A 1 388 ? -49.259 3.393   -42.840 1.00 52.60 ? 378  TYR A CD1   1 
ATOM   3091 C  CD2   . TYR A 1 388 ? -49.792 4.115   -45.061 1.00 53.25 ? 378  TYR A CD2   1 
ATOM   3092 C  CE1   . TYR A 1 388 ? -48.445 2.398   -43.352 1.00 52.89 ? 378  TYR A CE1   1 
ATOM   3093 C  CE2   . TYR A 1 388 ? -48.977 3.120   -45.581 1.00 53.41 ? 378  TYR A CE2   1 
ATOM   3094 C  CZ    . TYR A 1 388 ? -48.307 2.265   -44.722 1.00 53.17 ? 378  TYR A CZ    1 
ATOM   3095 O  OH    . TYR A 1 388 ? -47.500 1.276   -45.223 1.00 53.89 ? 378  TYR A OH    1 
ATOM   3096 N  N     . PHE A 1 389 ? -51.263 8.448   -42.132 1.00 52.79 ? 379  PHE A N     1 
ATOM   3097 C  CA    . PHE A 1 389 ? -52.120 9.357   -41.338 1.00 52.84 ? 379  PHE A CA    1 
ATOM   3098 C  C     . PHE A 1 389 ? -51.697 10.832  -41.394 1.00 53.08 ? 379  PHE A C     1 
ATOM   3099 O  O     . PHE A 1 389 ? -52.167 11.641  -40.593 1.00 51.78 ? 379  PHE A O     1 
ATOM   3100 C  CB    . PHE A 1 389 ? -52.184 8.873   -39.883 1.00 52.48 ? 379  PHE A CB    1 
ATOM   3101 C  CG    . PHE A 1 389 ? -52.764 7.494   -39.728 1.00 52.44 ? 379  PHE A CG    1 
ATOM   3102 C  CD1   . PHE A 1 389 ? -51.938 6.390   -39.568 1.00 52.01 ? 379  PHE A CD1   1 
ATOM   3103 C  CD2   . PHE A 1 389 ? -54.143 7.295   -39.749 1.00 53.08 ? 379  PHE A CD2   1 
ATOM   3104 C  CE1   . PHE A 1 389 ? -52.470 5.118   -39.430 1.00 51.98 ? 379  PHE A CE1   1 
ATOM   3105 C  CE2   . PHE A 1 389 ? -54.680 6.022   -39.610 1.00 52.85 ? 379  PHE A CE2   1 
ATOM   3106 C  CZ    . PHE A 1 389 ? -53.843 4.932   -39.452 1.00 52.72 ? 379  PHE A CZ    1 
ATOM   3107 N  N     . ASP A 1 390 ? -50.830 11.174  -42.351 1.00 54.06 ? 380  ASP A N     1 
ATOM   3108 C  CA    . ASP A 1 390 ? -50.296 12.541  -42.526 1.00 55.75 ? 380  ASP A CA    1 
ATOM   3109 C  C     . ASP A 1 390 ? -49.694 13.141  -41.236 1.00 55.58 ? 380  ASP A C     1 
ATOM   3110 O  O     . ASP A 1 390 ? -49.823 14.338  -40.962 1.00 55.27 ? 380  ASP A O     1 
ATOM   3111 C  CB    . ASP A 1 390 ? -51.361 13.463  -43.151 1.00 58.12 ? 380  ASP A CB    1 
ATOM   3112 C  CG    . ASP A 1 390 ? -51.649 13.124  -44.615 1.00 59.49 ? 380  ASP A CG    1 
ATOM   3113 O  OD1   . ASP A 1 390 ? -51.991 14.048  -45.381 1.00 61.36 ? 380  ASP A OD1   1 
ATOM   3114 O  OD2   . ASP A 1 390 ? -51.532 11.943  -45.006 1.00 59.29 ? 380  ASP A OD2   1 
ATOM   3115 N  N     . GLY A 1 391 ? -49.039 12.287  -40.451 1.00 54.65 ? 381  GLY A N     1 
ATOM   3116 C  CA    . GLY A 1 391 ? -48.346 12.702  -39.231 1.00 54.06 ? 381  GLY A CA    1 
ATOM   3117 C  C     . GLY A 1 391 ? -49.138 12.574  -37.942 1.00 53.62 ? 381  GLY A C     1 
ATOM   3118 O  O     . GLY A 1 391 ? -48.554 12.611  -36.862 1.00 51.62 ? 381  GLY A O     1 
ATOM   3119 N  N     . GLU A 1 392 ? -50.459 12.429  -38.046 1.00 53.79 ? 382  GLU A N     1 
ATOM   3120 C  CA    . GLU A 1 392 ? -51.326 12.355  -36.870 1.00 53.66 ? 382  GLU A CA    1 
ATOM   3121 C  C     . GLU A 1 392 ? -51.471 10.915  -36.383 1.00 51.45 ? 382  GLU A C     1 
ATOM   3122 O  O     . GLU A 1 392 ? -52.290 10.154  -36.889 1.00 49.96 ? 382  GLU A O     1 
ATOM   3123 C  CB    . GLU A 1 392 ? -52.700 12.967  -37.164 1.00 55.79 ? 382  GLU A CB    1 
ATOM   3124 C  CG    . GLU A 1 392 ? -53.562 13.124  -35.917 1.00 57.26 ? 382  GLU A CG    1 
ATOM   3125 C  CD    . GLU A 1 392 ? -54.654 14.159  -36.078 1.00 58.49 ? 382  GLU A CD    1 
ATOM   3126 O  OE1   . GLU A 1 392 ? -54.850 14.962  -35.144 1.00 59.71 ? 382  GLU A OE1   1 
ATOM   3127 O  OE2   . GLU A 1 392 ? -55.308 14.175  -37.139 1.00 59.81 ? 382  GLU A OE2   1 
ATOM   3128 N  N     . LEU A 1 393 ? -50.664 10.562  -35.386 1.00 49.95 ? 383  LEU A N     1 
ATOM   3129 C  CA    . LEU A 1 393 ? -50.681 9.233   -34.781 1.00 49.80 ? 383  LEU A CA    1 
ATOM   3130 C  C     . LEU A 1 393 ? -52.004 9.005   -34.052 1.00 50.58 ? 383  LEU A C     1 
ATOM   3131 O  O     . LEU A 1 393 ? -52.305 9.741   -33.112 1.00 49.99 ? 383  LEU A O     1 
ATOM   3132 C  CB    . LEU A 1 393 ? -49.526 9.099   -33.776 1.00 48.74 ? 383  LEU A CB    1 
ATOM   3133 C  CG    . LEU A 1 393 ? -49.418 7.783   -32.999 1.00 48.33 ? 383  LEU A CG    1 
ATOM   3134 C  CD1   . LEU A 1 393 ? -49.044 6.632   -33.918 1.00 48.06 ? 383  LEU A CD1   1 
ATOM   3135 C  CD2   . LEU A 1 393 ? -48.401 7.923   -31.880 1.00 47.39 ? 383  LEU A CD2   1 
ATOM   3136 N  N     . PRO A 1 394 ? -52.793 7.995   -34.474 1.00 51.73 ? 384  PRO A N     1 
ATOM   3137 C  CA    . PRO A 1 394 ? -54.031 7.714   -33.742 1.00 52.02 ? 384  PRO A CA    1 
ATOM   3138 C  C     . PRO A 1 394 ? -53.800 7.268   -32.295 1.00 51.40 ? 384  PRO A C     1 
ATOM   3139 O  O     . PRO A 1 394 ? -52.835 6.547   -32.001 1.00 47.89 ? 384  PRO A O     1 
ATOM   3140 C  CB    . PRO A 1 394 ? -54.672 6.585   -34.555 1.00 52.97 ? 384  PRO A CB    1 
ATOM   3141 C  CG    . PRO A 1 394 ? -54.125 6.765   -35.926 1.00 53.05 ? 384  PRO A CG    1 
ATOM   3142 C  CD    . PRO A 1 394 ? -52.703 7.174   -35.696 1.00 52.54 ? 384  PRO A CD    1 
ATOM   3143 N  N     . ALA A 1 395 ? -54.698 7.703   -31.415 1.00 49.89 ? 385  ALA A N     1 
ATOM   3144 C  CA    . ALA A 1 395 ? -54.631 7.389   -29.996 1.00 49.52 ? 385  ALA A CA    1 
ATOM   3145 C  C     . ALA A 1 395 ? -54.713 5.891   -29.762 1.00 48.53 ? 385  ALA A C     1 
ATOM   3146 O  O     . ALA A 1 395 ? -55.414 5.185   -30.485 1.00 46.97 ? 385  ALA A O     1 
ATOM   3147 C  CB    . ALA A 1 395 ? -55.765 8.077   -29.255 1.00 50.12 ? 385  ALA A CB    1 
ATOM   3148 N  N     . TYR A 1 396 ? -53.987 5.422   -28.748 1.00 46.78 ? 386  TYR A N     1 
ATOM   3149 C  CA    . TYR A 1 396 ? -54.113 4.049   -28.270 1.00 46.69 ? 386  TYR A CA    1 
ATOM   3150 C  C     . TYR A 1 396 ? -55.535 3.837   -27.755 1.00 47.92 ? 386  TYR A C     1 
ATOM   3151 O  O     . TYR A 1 396 ? -56.095 4.721   -27.111 1.00 47.79 ? 386  TYR A O     1 
ATOM   3152 C  CB    . TYR A 1 396 ? -53.108 3.757   -27.144 1.00 44.99 ? 386  TYR A CB    1 
ATOM   3153 C  CG    . TYR A 1 396 ? -53.250 2.369   -26.548 1.00 44.03 ? 386  TYR A CG    1 
ATOM   3154 C  CD1   . TYR A 1 396 ? -52.584 1.275   -27.103 1.00 43.73 ? 386  TYR A CD1   1 
ATOM   3155 C  CD2   . TYR A 1 396 ? -54.072 2.142   -25.442 1.00 44.15 ? 386  TYR A CD2   1 
ATOM   3156 C  CE1   . TYR A 1 396 ? -52.721 -0.001  -26.569 1.00 43.48 ? 386  TYR A CE1   1 
ATOM   3157 C  CE2   . TYR A 1 396 ? -54.215 0.873   -24.902 1.00 44.06 ? 386  TYR A CE2   1 
ATOM   3158 C  CZ    . TYR A 1 396 ? -53.542 -0.196  -25.462 1.00 43.98 ? 386  TYR A CZ    1 
ATOM   3159 O  OH    . TYR A 1 396 ? -53.686 -1.452  -24.918 1.00 43.98 ? 386  TYR A OH    1 
ATOM   3160 N  N     . GLN A 1 397 ? -56.091 2.666   -28.048 1.00 49.64 ? 387  GLN A N     1 
ATOM   3161 C  CA    . GLN A 1 397 ? -57.431 2.276   -27.597 1.00 51.98 ? 387  GLN A CA    1 
ATOM   3162 C  C     . GLN A 1 397 ? -57.398 1.000   -26.762 1.00 51.66 ? 387  GLN A C     1 
ATOM   3163 O  O     . GLN A 1 397 ? -57.927 0.967   -25.652 1.00 51.47 ? 387  GLN A O     1 
ATOM   3164 C  CB    . GLN A 1 397 ? -58.361 2.079   -28.794 1.00 53.35 ? 387  GLN A CB    1 
ATOM   3165 C  CG    . GLN A 1 397 ? -58.660 3.352   -29.568 1.00 54.63 ? 387  GLN A CG    1 
ATOM   3166 C  CD    . GLN A 1 397 ? -59.548 3.100   -30.777 1.00 56.44 ? 387  GLN A CD    1 
ATOM   3167 O  OE1   . GLN A 1 397 ? -60.579 2.435   -30.677 1.00 57.09 ? 387  GLN A OE1   1 
ATOM   3168 N  NE2   . GLN A 1 397 ? -59.153 3.636   -31.928 1.00 56.60 ? 387  GLN A NE2   1 
ATOM   3169 N  N     . GLY A 1 398 ? -56.798 -0.051  -27.312 1.00 51.38 ? 388  GLY A N     1 
ATOM   3170 C  CA    . GLY A 1 398 ? -56.685 -1.342  -26.625 1.00 51.99 ? 388  GLY A CA    1 
ATOM   3171 C  C     . GLY A 1 398 ? -55.934 -2.358  -27.465 1.00 51.69 ? 388  GLY A C     1 
ATOM   3172 O  O     . GLY A 1 398 ? -55.410 -2.005  -28.513 1.00 51.22 ? 388  GLY A O     1 
ATOM   3173 N  N     . PRO A 1 399 ? -55.864 -3.625  -27.004 1.00 53.03 ? 389  PRO A N     1 
ATOM   3174 C  CA    . PRO A 1 399 ? -55.203 -4.697  -27.758 1.00 54.02 ? 389  PRO A CA    1 
ATOM   3175 C  C     . PRO A 1 399 ? -56.109 -5.258  -28.863 1.00 55.00 ? 389  PRO A C     1 
ATOM   3176 O  O     . PRO A 1 399 ? -56.732 -6.306  -28.692 1.00 55.09 ? 389  PRO A O     1 
ATOM   3177 C  CB    . PRO A 1 399 ? -54.902 -5.741  -26.675 1.00 53.91 ? 389  PRO A CB    1 
ATOM   3178 C  CG    . PRO A 1 399 ? -56.015 -5.574  -25.701 1.00 53.70 ? 389  PRO A CG    1 
ATOM   3179 C  CD    . PRO A 1 399 ? -56.339 -4.102  -25.691 1.00 53.23 ? 389  PRO A CD    1 
ATOM   3180 N  N     . LEU A 1 400 ? -56.158 -4.554  -29.991 1.00 56.49 ? 390  LEU A N     1 
ATOM   3181 C  CA    . LEU A 1 400 ? -57.102 -4.866  -31.077 1.00 58.19 ? 390  LEU A CA    1 
ATOM   3182 C  C     . LEU A 1 400 ? -56.629 -5.982  -32.007 1.00 57.86 ? 390  LEU A C     1 
ATOM   3183 O  O     . LEU A 1 400 ? -57.433 -6.824  -32.422 1.00 57.45 ? 390  LEU A O     1 
ATOM   3184 C  CB    . LEU A 1 400 ? -57.427 -3.612  -31.893 1.00 59.33 ? 390  LEU A CB    1 
ATOM   3185 C  CG    . LEU A 1 400 ? -57.936 -2.379  -31.132 1.00 61.02 ? 390  LEU A CG    1 
ATOM   3186 C  CD1   . LEU A 1 400 ? -58.445 -1.340  -32.119 1.00 61.87 ? 390  LEU A CD1   1 
ATOM   3187 C  CD2   . LEU A 1 400 ? -59.033 -2.709  -30.123 1.00 61.90 ? 390  LEU A CD2   1 
ATOM   3188 N  N     . HIS A 1 401 ? -55.340 -5.985  -32.344 1.00 55.93 ? 391  HIS A N     1 
ATOM   3189 C  CA    . HIS A 1 401 ? -54.762 -7.041  -33.182 1.00 55.51 ? 391  HIS A CA    1 
ATOM   3190 C  C     . HIS A 1 401 ? -54.594 -8.314  -32.355 1.00 55.92 ? 391  HIS A C     1 
ATOM   3191 O  O     . HIS A 1 401 ? -54.458 -8.251  -31.133 1.00 53.99 ? 391  HIS A O     1 
ATOM   3192 C  CB    . HIS A 1 401 ? -53.413 -6.597  -33.765 1.00 54.64 ? 391  HIS A CB    1 
ATOM   3193 C  CG    . HIS A 1 401 ? -52.998 -7.361  -34.984 1.00 53.75 ? 391  HIS A CG    1 
ATOM   3194 N  ND1   . HIS A 1 401 ? -52.339 -8.569  -34.917 1.00 53.13 ? 391  HIS A ND1   1 
ATOM   3195 C  CD2   . HIS A 1 401 ? -53.143 -7.087  -36.302 1.00 53.31 ? 391  HIS A CD2   1 
ATOM   3196 C  CE1   . HIS A 1 401 ? -52.104 -9.010  -36.139 1.00 53.36 ? 391  HIS A CE1   1 
ATOM   3197 N  NE2   . HIS A 1 401 ? -52.581 -8.128  -36.998 1.00 53.23 ? 391  HIS A NE2   1 
ATOM   3198 N  N     . GLU A 1 402 ? -54.606 -9.461  -33.030 1.00 57.18 ? 392  GLU A N     1 
ATOM   3199 C  CA    . GLU A 1 402 ? -54.453 -10.776 -32.383 1.00 59.43 ? 392  GLU A CA    1 
ATOM   3200 C  C     . GLU A 1 402 ? -53.157 -10.900 -31.570 1.00 57.09 ? 392  GLU A C     1 
ATOM   3201 O  O     . GLU A 1 402 ? -53.145 -11.487 -30.492 1.00 56.23 ? 392  GLU A O     1 
ATOM   3202 C  CB    . GLU A 1 402 ? -54.509 -11.891 -33.440 1.00 62.63 ? 392  GLU A CB    1 
ATOM   3203 C  CG    . GLU A 1 402 ? -54.796 -13.293 -32.895 1.00 65.63 ? 392  GLU A CG    1 
ATOM   3204 C  CD    . GLU A 1 402 ? -53.557 -14.139 -32.627 1.00 67.62 ? 392  GLU A CD    1 
ATOM   3205 O  OE1   . GLU A 1 402 ? -53.562 -14.882 -31.620 1.00 69.26 ? 392  GLU A OE1   1 
ATOM   3206 O  OE2   . GLU A 1 402 ? -52.590 -14.085 -33.419 1.00 68.95 ? 392  GLU A OE2   1 
ATOM   3207 N  N     . LEU A 1 403 ? -52.078 -10.340 -32.106 1.00 55.44 ? 393  LEU A N     1 
ATOM   3208 C  CA    . LEU A 1 403 ? -50.758 -10.379 -31.475 1.00 54.26 ? 393  LEU A CA    1 
ATOM   3209 C  C     . LEU A 1 403 ? -50.594 -9.437  -30.274 1.00 52.51 ? 393  LEU A C     1 
ATOM   3210 O  O     . LEU A 1 403 ? -49.691 -9.642  -29.466 1.00 51.71 ? 393  LEU A O     1 
ATOM   3211 C  CB    . LEU A 1 403 ? -49.681 -10.059 -32.519 1.00 53.94 ? 393  LEU A CB    1 
ATOM   3212 C  CG    . LEU A 1 403 ? -49.542 -11.039 -33.689 1.00 54.35 ? 393  LEU A CG    1 
ATOM   3213 C  CD1   . LEU A 1 403 ? -48.727 -10.416 -34.811 1.00 54.50 ? 393  LEU A CD1   1 
ATOM   3214 C  CD2   . LEU A 1 403 ? -48.920 -12.351 -33.238 1.00 54.36 ? 393  LEU A CD2   1 
ATOM   3215 N  N     . ASP A 1 404 ? -51.456 -8.423  -30.164 1.00 51.46 ? 394  ASP A N     1 
ATOM   3216 C  CA    . ASP A 1 404 ? -51.315 -7.353  -29.164 1.00 51.18 ? 394  ASP A CA    1 
ATOM   3217 C  C     . ASP A 1 404 ? -51.300 -7.795  -27.706 1.00 52.39 ? 394  ASP A C     1 
ATOM   3218 O  O     . ASP A 1 404 ? -50.466 -7.324  -26.939 1.00 50.59 ? 394  ASP A O     1 
ATOM   3219 C  CB    . ASP A 1 404 ? -52.410 -6.293  -29.342 1.00 50.15 ? 394  ASP A CB    1 
ATOM   3220 C  CG    . ASP A 1 404 ? -52.225 -5.455  -30.588 1.00 48.53 ? 394  ASP A CG    1 
ATOM   3221 O  OD1   . ASP A 1 404 ? -51.169 -5.558  -31.244 1.00 47.27 ? 394  ASP A OD1   1 
ATOM   3222 O  OD2   . ASP A 1 404 ? -53.144 -4.680  -30.910 1.00 46.68 ? 394  ASP A OD2   1 
ATOM   3223 N  N     . GLU A 1 405 ? -52.217 -8.683  -27.328 1.00 54.13 ? 395  GLU A N     1 
ATOM   3224 C  CA    . GLU A 1 405 ? -52.318 -9.156  -25.940 1.00 55.69 ? 395  GLU A CA    1 
ATOM   3225 C  C     . GLU A 1 405 ? -50.968 -9.678  -25.444 1.00 53.50 ? 395  GLU A C     1 
ATOM   3226 O  O     . GLU A 1 405 ? -50.441 -9.212  -24.431 1.00 51.56 ? 395  GLU A O     1 
ATOM   3227 C  CB    . GLU A 1 405 ? -53.390 -10.246 -25.826 1.00 58.69 ? 395  GLU A CB    1 
ATOM   3228 C  CG    . GLU A 1 405 ? -53.694 -10.709 -24.409 1.00 60.56 ? 395  GLU A CG    1 
ATOM   3229 C  CD    . GLU A 1 405 ? -54.820 -11.729 -24.371 1.00 62.96 ? 395  GLU A CD    1 
ATOM   3230 O  OE1   . GLU A 1 405 ? -55.984 -11.344 -24.624 1.00 63.92 ? 395  GLU A OE1   1 
ATOM   3231 O  OE2   . GLU A 1 405 ? -54.540 -12.916 -24.096 1.00 63.38 ? 395  GLU A OE2   1 
ATOM   3232 N  N     . GLU A 1 406 ? -50.410 -10.622 -26.188 1.00 52.20 ? 396  GLU A N     1 
ATOM   3233 C  CA    . GLU A 1 406 ? -49.115 -11.212 -25.861 1.00 52.23 ? 396  GLU A CA    1 
ATOM   3234 C  C     . GLU A 1 406 ? -47.943 -10.216 -25.936 1.00 49.07 ? 396  GLU A C     1 
ATOM   3235 O  O     . GLU A 1 406 ? -46.984 -10.344 -25.173 1.00 47.16 ? 396  GLU A O     1 
ATOM   3236 C  CB    . GLU A 1 406 ? -48.854 -12.405 -26.775 1.00 54.29 ? 396  GLU A CB    1 
ATOM   3237 C  CG    . GLU A 1 406 ? -47.659 -13.259 -26.389 1.00 56.17 ? 396  GLU A CG    1 
ATOM   3238 C  CD    . GLU A 1 406 ? -47.369 -14.328 -27.424 1.00 58.13 ? 396  GLU A CD    1 
ATOM   3239 O  OE1   . GLU A 1 406 ? -48.299 -15.094 -27.762 1.00 58.72 ? 396  GLU A OE1   1 
ATOM   3240 O  OE2   . GLU A 1 406 ? -46.213 -14.398 -27.900 1.00 59.08 ? 396  GLU A OE2   1 
ATOM   3241 N  N     . MET A 1 407 ? -48.024 -9.243  -26.845 1.00 46.48 ? 397  MET A N     1 
ATOM   3242 C  CA    . MET A 1 407 ? -46.957 -8.235  -27.008 1.00 44.89 ? 397  MET A CA    1 
ATOM   3243 C  C     . MET A 1 407 ? -46.976 -7.179  -25.902 1.00 43.89 ? 397  MET A C     1 
ATOM   3244 O  O     . MET A 1 407 ? -45.919 -6.728  -25.449 1.00 42.62 ? 397  MET A O     1 
ATOM   3245 C  CB    . MET A 1 407 ? -47.023 -7.555  -28.379 1.00 43.34 ? 397  MET A CB    1 
ATOM   3246 C  CG    . MET A 1 407 ? -45.800 -6.689  -28.662 1.00 42.03 ? 397  MET A CG    1 
ATOM   3247 S  SD    . MET A 1 407 ? -45.651 -6.127  -30.368 1.00 39.54 ? 397  MET A SD    1 
ATOM   3248 C  CE    . MET A 1 407 ? -46.776 -4.737  -30.392 1.00 40.28 ? 397  MET A CE    1 
ATOM   3249 N  N     . GLU A 1 408 ? -48.172 -6.771  -25.490 1.00 43.39 ? 398  GLU A N     1 
ATOM   3250 C  CA    . GLU A 1 408 ? -48.333 -5.896  -24.326 1.00 43.48 ? 398  GLU A CA    1 
ATOM   3251 C  C     . GLU A 1 408 ? -47.832 -6.572  -23.047 1.00 43.42 ? 398  GLU A C     1 
ATOM   3252 O  O     . GLU A 1 408 ? -47.268 -5.913  -22.181 1.00 42.38 ? 398  GLU A O     1 
ATOM   3253 C  CB    . GLU A 1 408 ? -49.792 -5.461  -24.168 1.00 43.75 ? 398  GLU A CB    1 
ATOM   3254 C  CG    . GLU A 1 408 ? -50.255 -4.496  -25.253 1.00 43.50 ? 398  GLU A CG    1 
ATOM   3255 C  CD    . GLU A 1 408 ? -51.669 -3.961  -25.060 1.00 43.70 ? 398  GLU A CD    1 
ATOM   3256 O  OE1   . GLU A 1 408 ? -52.236 -3.435  -26.038 1.00 42.72 ? 398  GLU A OE1   1 
ATOM   3257 O  OE2   . GLU A 1 408 ? -52.219 -4.047  -23.943 1.00 43.33 ? 398  GLU A OE2   1 
ATOM   3258 N  N     . ALA A 1 409 ? -48.043 -7.883  -22.947 1.00 43.58 ? 399  ALA A N     1 
ATOM   3259 C  CA    . ALA A 1 409 ? -47.504 -8.701  -21.856 1.00 43.71 ? 399  ALA A CA    1 
ATOM   3260 C  C     . ALA A 1 409 ? -45.974 -8.792  -21.911 1.00 42.64 ? 399  ALA A C     1 
ATOM   3261 O  O     . ALA A 1 409 ? -45.313 -8.768  -20.871 1.00 43.03 ? 399  ALA A O     1 
ATOM   3262 C  CB    . ALA A 1 409 ? -48.110 -10.094 -21.896 1.00 43.95 ? 399  ALA A CB    1 
ATOM   3263 N  N     . MET A 1 410 ? -45.428 -8.920  -23.120 1.00 40.89 ? 400  MET A N     1 
ATOM   3264 C  CA    . MET A 1 410 ? -43.974 -8.869  -23.327 1.00 39.93 ? 400  MET A CA    1 
ATOM   3265 C  C     . MET A 1 410 ? -43.364 -7.523  -22.904 1.00 38.38 ? 400  MET A C     1 
ATOM   3266 O  O     . MET A 1 410 ? -42.278 -7.502  -22.329 1.00 36.76 ? 400  MET A O     1 
ATOM   3267 C  CB    . MET A 1 410 ? -43.612 -9.170  -24.785 1.00 40.23 ? 400  MET A CB    1 
ATOM   3268 C  CG    . MET A 1 410 ? -42.138 -9.494  -24.995 1.00 40.08 ? 400  MET A CG    1 
ATOM   3269 S  SD    . MET A 1 410 ? -41.659 -9.534  -26.738 1.00 39.14 ? 400  MET A SD    1 
ATOM   3270 C  CE    . MET A 1 410 ? -39.912 -9.922  -26.581 1.00 39.57 ? 400  MET A CE    1 
ATOM   3271 N  N     . ALA A 1 411 ? -44.050 -6.418  -23.194 1.00 37.44 ? 401  ALA A N     1 
ATOM   3272 C  CA    . ALA A 1 411 ? -43.602 -5.084  -22.757 1.00 37.82 ? 401  ALA A CA    1 
ATOM   3273 C  C     . ALA A 1 411 ? -43.458 -5.007  -21.233 1.00 38.23 ? 401  ALA A C     1 
ATOM   3274 O  O     . ALA A 1 411 ? -42.420 -4.594  -20.713 1.00 35.64 ? 401  ALA A O     1 
ATOM   3275 C  CB    . ALA A 1 411 ? -44.546 -4.005  -23.254 1.00 37.51 ? 401  ALA A CB    1 
ATOM   3276 N  N     . LEU A 1 412 ? -44.490 -5.439  -20.517 1.00 38.88 ? 402  LEU A N     1 
ATOM   3277 C  CA    . LEU A 1 412 ? -44.438 -5.448  -19.050 1.00 40.11 ? 402  LEU A CA    1 
ATOM   3278 C  C     . LEU A 1 412 ? -43.409 -6.432  -18.492 1.00 38.89 ? 402  LEU A C     1 
ATOM   3279 O  O     . LEU A 1 412 ? -42.713 -6.114  -17.531 1.00 38.17 ? 402  LEU A O     1 
ATOM   3280 C  CB    . LEU A 1 412 ? -45.822 -5.727  -18.460 1.00 42.13 ? 402  LEU A CB    1 
ATOM   3281 C  CG    . LEU A 1 412 ? -46.903 -4.699  -18.804 1.00 44.61 ? 402  LEU A CG    1 
ATOM   3282 C  CD1   . LEU A 1 412 ? -48.224 -5.144  -18.191 1.00 45.94 ? 402  LEU A CD1   1 
ATOM   3283 C  CD2   . LEU A 1 412 ? -46.553 -3.287  -18.332 1.00 45.52 ? 402  LEU A CD2   1 
ATOM   3284 N  N     . GLU A 1 413 ? -43.302 -7.610  -19.099 1.00 38.82 ? 403  GLU A N     1 
ATOM   3285 C  CA    . GLU A 1 413 ? -42.287 -8.592  -18.698 1.00 39.69 ? 403  GLU A CA    1 
ATOM   3286 C  C     . GLU A 1 413 ? -40.865 -8.082  -18.958 1.00 37.45 ? 403  GLU A C     1 
ATOM   3287 O  O     . GLU A 1 413 ? -39.942 -8.405  -18.210 1.00 36.22 ? 403  GLU A O     1 
ATOM   3288 C  CB    . GLU A 1 413 ? -42.505 -9.932  -19.417 1.00 41.69 ? 403  GLU A CB    1 
ATOM   3289 C  CG    . GLU A 1 413 ? -41.616 -11.080 -18.940 1.00 43.62 ? 403  GLU A CG    1 
ATOM   3290 C  CD    . GLU A 1 413 ? -41.780 -11.412 -17.458 1.00 46.11 ? 403  GLU A CD    1 
ATOM   3291 O  OE1   . GLU A 1 413 ? -40.788 -11.864 -16.842 1.00 48.67 ? 403  GLU A OE1   1 
ATOM   3292 O  OE2   . GLU A 1 413 ? -42.885 -11.216 -16.900 1.00 47.26 ? 403  GLU A OE2   1 
ATOM   3293 N  N     . THR A 1 414 ? -40.707 -7.301  -20.024 1.00 35.56 ? 404  THR A N     1 
ATOM   3294 C  CA    . THR A 1 414 ? -39.427 -6.692  -20.370 1.00 34.36 ? 404  THR A CA    1 
ATOM   3295 C  C     . THR A 1 414 ? -38.992 -5.739  -19.247 1.00 33.52 ? 404  THR A C     1 
ATOM   3296 O  O     . THR A 1 414 ? -37.842 -5.779  -18.803 1.00 32.02 ? 404  THR A O     1 
ATOM   3297 C  CB    . THR A 1 414 ? -39.515 -5.960  -21.732 1.00 33.93 ? 404  THR A CB    1 
ATOM   3298 O  OG1   . THR A 1 414 ? -39.789 -6.911  -22.774 1.00 33.29 ? 404  THR A OG1   1 
ATOM   3299 C  CG2   . THR A 1 414 ? -38.226 -5.230  -22.066 1.00 33.04 ? 404  THR A CG2   1 
ATOM   3300 N  N     . VAL A 1 415 ? -39.925 -4.907  -18.784 1.00 33.23 ? 405  VAL A N     1 
ATOM   3301 C  CA    . VAL A 1 415 ? -39.658 -3.969  -17.685 1.00 33.96 ? 405  VAL A CA    1 
ATOM   3302 C  C     . VAL A 1 415 ? -39.290 -4.714  -16.395 1.00 34.66 ? 405  VAL A C     1 
ATOM   3303 O  O     . VAL A 1 415 ? -38.356 -4.310  -15.694 1.00 32.91 ? 405  VAL A O     1 
ATOM   3304 C  CB    . VAL A 1 415 ? -40.843 -2.991  -17.454 1.00 34.23 ? 405  VAL A CB    1 
ATOM   3305 C  CG1   . VAL A 1 415 ? -40.601 -2.070  -16.261 1.00 34.30 ? 405  VAL A CG1   1 
ATOM   3306 C  CG2   . VAL A 1 415 ? -41.067 -2.137  -18.692 1.00 34.17 ? 405  VAL A CG2   1 
ATOM   3307 N  N     . LYS A 1 416 ? -40.015 -5.794  -16.094 1.00 35.88 ? 406  LYS A N     1 
ATOM   3308 C  CA    . LYS A 1 416 ? -39.784 -6.584  -14.878 1.00 36.89 ? 406  LYS A CA    1 
ATOM   3309 C  C     . LYS A 1 416 ? -38.400 -7.245  -14.884 1.00 35.52 ? 406  LYS A C     1 
ATOM   3310 O  O     . LYS A 1 416 ? -37.656 -7.149  -13.907 1.00 34.24 ? 406  LYS A O     1 
ATOM   3311 C  CB    . LYS A 1 416 ? -40.864 -7.667  -14.715 1.00 39.54 ? 406  LYS A CB    1 
ATOM   3312 C  CG    . LYS A 1 416 ? -40.813 -8.391  -13.372 1.00 42.03 ? 406  LYS A CG    1 
ATOM   3313 C  CD    . LYS A 1 416 ? -41.796 -9.553  -13.292 1.00 44.54 ? 406  LYS A CD    1 
ATOM   3314 C  CE    . LYS A 1 416 ? -41.555 -10.380 -12.035 1.00 46.20 ? 406  LYS A CE    1 
ATOM   3315 N  NZ    . LYS A 1 416 ? -42.428 -11.585 -11.988 1.00 47.91 ? 406  LYS A NZ    1 
ATOM   3316 N  N     . SER A 1 417 ? -38.089 -7.930  -15.983 1.00 34.03 ? 407  SER A N     1 
ATOM   3317 C  CA    . SER A 1 417 ? -36.787 -8.575  -16.181 1.00 33.53 ? 407  SER A CA    1 
ATOM   3318 C  C     . SER A 1 417 ? -35.631 -7.571  -16.143 1.00 31.36 ? 407  SER A C     1 
ATOM   3319 O  O     . SER A 1 417 ? -34.607 -7.821  -15.504 1.00 30.98 ? 407  SER A O     1 
ATOM   3320 C  CB    . SER A 1 417 ? -36.776 -9.320  -17.517 1.00 34.30 ? 407  SER A CB    1 
ATOM   3321 O  OG    . SER A 1 417 ? -35.531 -9.954  -17.756 1.00 34.81 ? 407  SER A OG    1 
ATOM   3322 N  N     . TYR A 1 418 ? -35.803 -6.460  -16.855 1.00 29.75 ? 408  TYR A N     1 
ATOM   3323 C  CA    . TYR A 1 418 ? -34.825 -5.358  -16.880 1.00 29.46 ? 408  TYR A CA    1 
ATOM   3324 C  C     . TYR A 1 418 ? -34.522 -4.884  -15.463 1.00 29.49 ? 408  TYR A C     1 
ATOM   3325 O  O     . TYR A 1 418 ? -33.359 -4.726  -15.075 1.00 29.14 ? 408  TYR A O     1 
ATOM   3326 C  CB    . TYR A 1 418 ? -35.395 -4.211  -17.728 1.00 28.31 ? 408  TYR A CB    1 
ATOM   3327 C  CG    . TYR A 1 418 ? -34.746 -2.839  -17.619 1.00 27.12 ? 408  TYR A CG    1 
ATOM   3328 C  CD1   . TYR A 1 418 ? -33.811 -2.407  -18.567 1.00 26.86 ? 408  TYR A CD1   1 
ATOM   3329 C  CD2   . TYR A 1 418 ? -35.106 -1.945  -16.606 1.00 26.82 ? 408  TYR A CD2   1 
ATOM   3330 C  CE1   . TYR A 1 418 ? -33.252 -1.142  -18.491 1.00 25.84 ? 408  TYR A CE1   1 
ATOM   3331 C  CE2   . TYR A 1 418 ? -34.549 -0.679  -16.528 1.00 25.70 ? 408  TYR A CE2   1 
ATOM   3332 C  CZ    . TYR A 1 418 ? -33.621 -0.283  -17.471 1.00 25.60 ? 408  TYR A CZ    1 
ATOM   3333 O  OH    . TYR A 1 418 ? -33.059 0.966   -17.405 1.00 24.46 ? 408  TYR A OH    1 
ATOM   3334 N  N     . THR A 1 419 ? -35.582 -4.665  -14.694 1.00 30.12 ? 409  THR A N     1 
ATOM   3335 C  CA    . THR A 1 419 ? -35.444 -4.196  -13.312 1.00 30.93 ? 409  THR A CA    1 
ATOM   3336 C  C     . THR A 1 419 ? -34.624 -5.195  -12.473 1.00 31.76 ? 409  THR A C     1 
ATOM   3337 O  O     . THR A 1 419 ? -33.708 -4.792  -11.764 1.00 29.58 ? 409  THR A O     1 
ATOM   3338 C  CB    . THR A 1 419 ? -36.827 -3.895  -12.691 1.00 31.32 ? 409  THR A CB    1 
ATOM   3339 O  OG1   . THR A 1 419 ? -37.522 -2.967  -13.535 1.00 31.38 ? 409  THR A OG1   1 
ATOM   3340 C  CG2   . THR A 1 419 ? -36.698 -3.280  -11.301 1.00 31.69 ? 409  THR A CG2   1 
ATOM   3341 N  N     . GLU A 1 420 ? -34.919 -6.488  -12.595 1.00 32.82 ? 410  GLU A N     1 
ATOM   3342 C  CA    . GLU A 1 420 ? -34.143 -7.526  -11.898 1.00 34.54 ? 410  GLU A CA    1 
ATOM   3343 C  C     . GLU A 1 420 ? -32.658 -7.474  -12.269 1.00 32.88 ? 410  GLU A C     1 
ATOM   3344 O  O     . GLU A 1 420 ? -31.784 -7.539  -11.396 1.00 31.70 ? 410  GLU A O     1 
ATOM   3345 C  CB    . GLU A 1 420 ? -34.718 -8.928  -12.166 1.00 37.59 ? 410  GLU A CB    1 
ATOM   3346 C  CG    . GLU A 1 420 ? -36.075 -9.161  -11.506 1.00 40.63 ? 410  GLU A CG    1 
ATOM   3347 C  CD    . GLU A 1 420 ? -36.737 -10.485 -11.881 1.00 43.90 ? 410  GLU A CD    1 
ATOM   3348 O  OE1   . GLU A 1 420 ? -37.937 -10.662 -11.550 1.00 47.35 ? 410  GLU A OE1   1 
ATOM   3349 O  OE2   . GLU A 1 420 ? -36.078 -11.348 -12.504 1.00 46.14 ? 410  GLU A OE2   1 
ATOM   3350 N  N     . SER A 1 421 ? -32.380 -7.335  -13.565 1.00 30.85 ? 411  SER A N     1 
ATOM   3351 C  CA    . SER A 1 421 ? -31.002 -7.222  -14.046 1.00 29.43 ? 411  SER A CA    1 
ATOM   3352 C  C     . SER A 1 421 ? -30.308 -5.962  -13.521 1.00 28.39 ? 411  SER A C     1 
ATOM   3353 O  O     . SER A 1 421 ? -29.162 -6.030  -13.082 1.00 27.65 ? 411  SER A O     1 
ATOM   3354 C  CB    . SER A 1 421 ? -30.971 -7.241  -15.569 1.00 29.50 ? 411  SER A CB    1 
ATOM   3355 O  OG    . SER A 1 421 ? -31.425 -8.488  -16.052 1.00 29.54 ? 411  SER A OG    1 
ATOM   3356 N  N     . MET A 1 422 ? -31.005 -4.827  -13.568 1.00 27.52 ? 412  MET A N     1 
ATOM   3357 C  CA    . MET A 1 422 ? -30.439 -3.556  -13.082 1.00 26.97 ? 412  MET A CA    1 
ATOM   3358 C  C     . MET A 1 422 ? -30.157 -3.626  -11.587 1.00 27.72 ? 412  MET A C     1 
ATOM   3359 O  O     . MET A 1 422 ? -29.105 -3.197  -11.140 1.00 27.32 ? 412  MET A O     1 
ATOM   3360 C  CB    . MET A 1 422 ? -31.366 -2.367  -13.368 1.00 26.18 ? 412  MET A CB    1 
ATOM   3361 C  CG    . MET A 1 422 ? -31.588 -2.054  -14.838 1.00 25.86 ? 412  MET A CG    1 
ATOM   3362 S  SD    . MET A 1 422 ? -30.088 -1.653  -15.761 1.00 24.92 ? 412  MET A SD    1 
ATOM   3363 C  CE    . MET A 1 422 ? -29.805 0.035   -15.221 1.00 24.86 ? 412  MET A CE    1 
ATOM   3364 N  N     . GLU A 1 423 ? -31.092 -4.185  -10.817 1.00 29.51 ? 413  GLU A N     1 
ATOM   3365 C  CA    . GLU A 1 423 ? -30.896 -4.320  -9.365  1.00 30.85 ? 413  GLU A CA    1 
ATOM   3366 C  C     . GLU A 1 423 ? -29.696 -5.200  -9.000  1.00 31.32 ? 413  GLU A C     1 
ATOM   3367 O  O     . GLU A 1 423 ? -29.066 -4.969  -7.974  1.00 30.09 ? 413  GLU A O     1 
ATOM   3368 C  CB    . GLU A 1 423 ? -32.172 -4.844  -8.692  1.00 32.27 ? 413  GLU A CB    1 
ATOM   3369 C  CG    . GLU A 1 423 ? -33.335 -3.859  -8.733  1.00 33.78 ? 413  GLU A CG    1 
ATOM   3370 C  CD    . GLU A 1 423 ? -33.060 -2.563  -7.985  1.00 34.46 ? 413  GLU A CD    1 
ATOM   3371 O  OE1   . GLU A 1 423 ? -32.442 -2.617  -6.907  1.00 36.23 ? 413  GLU A OE1   1 
ATOM   3372 O  OE2   . GLU A 1 423 ? -33.481 -1.496  -8.467  1.00 34.57 ? 413  GLU A OE2   1 
ATOM   3373 N  N     . SER A 1 424 ? -29.388 -6.191  -9.843  1.00 31.15 ? 414  SER A N     1 
ATOM   3374 C  CA    . SER A 1 424 ? -28.225 -7.066  -9.652  1.00 31.49 ? 414  SER A CA    1 
ATOM   3375 C  C     . SER A 1 424 ? -26.973 -6.623  -10.440 1.00 30.35 ? 414  SER A C     1 
ATOM   3376 O  O     . SER A 1 424 ? -25.992 -7.353  -10.488 1.00 29.56 ? 414  SER A O     1 
ATOM   3377 C  CB    . SER A 1 424 ? -28.600 -8.521  -9.988  1.00 33.35 ? 414  SER A CB    1 
ATOM   3378 O  OG    . SER A 1 424 ? -29.058 -8.653  -11.321 1.00 34.02 ? 414  SER A OG    1 
ATOM   3379 N  N     . LEU A 1 425 ? -27.016 -5.421  -11.031 1.00 29.25 ? 415  LEU A N     1 
ATOM   3380 C  CA    . LEU A 1 425 ? -25.901 -4.831  -11.789 1.00 29.19 ? 415  LEU A CA    1 
ATOM   3381 C  C     . LEU A 1 425 ? -25.471 -5.672  -12.993 1.00 29.20 ? 415  LEU A C     1 
ATOM   3382 O  O     . LEU A 1 425 ? -24.315 -5.640  -13.417 1.00 29.58 ? 415  LEU A O     1 
ATOM   3383 C  CB    . LEU A 1 425 ? -24.715 -4.519  -10.865 1.00 29.31 ? 415  LEU A CB    1 
ATOM   3384 C  CG    . LEU A 1 425 ? -25.052 -3.652  -9.649  1.00 29.39 ? 415  LEU A CG    1 
ATOM   3385 C  CD1   . LEU A 1 425 ? -23.820 -3.507  -8.776  1.00 29.26 ? 415  LEU A CD1   1 
ATOM   3386 C  CD2   . LEU A 1 425 ? -25.581 -2.278  -10.052 1.00 29.59 ? 415  LEU A CD2   1 
ATOM   3387 N  N     . GLN A 1 426 ? -26.422 -6.407  -13.559 1.00 29.42 ? 416  GLN A N     1 
ATOM   3388 C  CA    . GLN A 1 426 ? -26.186 -7.194  -14.767 1.00 29.89 ? 416  GLN A CA    1 
ATOM   3389 C  C     . GLN A 1 426 ? -26.638 -6.365  -15.966 1.00 28.72 ? 416  GLN A C     1 
ATOM   3390 O  O     . GLN A 1 426 ? -27.659 -6.626  -16.585 1.00 28.50 ? 416  GLN A O     1 
ATOM   3391 C  CB    . GLN A 1 426 ? -26.921 -8.531  -14.676 1.00 31.39 ? 416  GLN A CB    1 
ATOM   3392 C  CG    . GLN A 1 426 ? -26.304 -9.432  -13.617 1.00 33.18 ? 416  GLN A CG    1 
ATOM   3393 C  CD    . GLN A 1 426 ? -26.932 -10.803 -13.561 1.00 35.21 ? 416  GLN A CD    1 
ATOM   3394 O  OE1   . GLN A 1 426 ? -27.583 -11.153 -12.582 1.00 38.13 ? 416  GLN A OE1   1 
ATOM   3395 N  NE2   . GLN A 1 426 ? -26.744 -11.584 -14.611 1.00 36.76 ? 416  GLN A NE2   1 
ATOM   3396 N  N     . PHE A 1 427 ? -25.855 -5.343  -16.276 1.00 28.12 ? 417  PHE A N     1 
ATOM   3397 C  CA    . PHE A 1 427 ? -26.241 -4.376  -17.302 1.00 27.63 ? 417  PHE A CA    1 
ATOM   3398 C  C     . PHE A 1 427 ? -26.256 -4.943  -18.713 1.00 27.20 ? 417  PHE A C     1 
ATOM   3399 O  O     . PHE A 1 427 ? -27.135 -4.586  -19.506 1.00 26.50 ? 417  PHE A O     1 
ATOM   3400 C  CB    . PHE A 1 427 ? -25.342 -3.150  -17.238 1.00 27.51 ? 417  PHE A CB    1 
ATOM   3401 C  CG    . PHE A 1 427 ? -25.518 -2.314  -15.991 1.00 28.16 ? 417  PHE A CG    1 
ATOM   3402 C  CD1   . PHE A 1 427 ? -26.616 -2.471  -15.129 1.00 28.46 ? 417  PHE A CD1   1 
ATOM   3403 C  CD2   . PHE A 1 427 ? -24.594 -1.322  -15.703 1.00 28.44 ? 417  PHE A CD2   1 
ATOM   3404 C  CE1   . PHE A 1 427 ? -26.753 -1.680  -14.002 1.00 29.08 ? 417  PHE A CE1   1 
ATOM   3405 C  CE2   . PHE A 1 427 ? -24.733 -0.526  -14.578 1.00 28.61 ? 417  PHE A CE2   1 
ATOM   3406 C  CZ    . PHE A 1 427 ? -25.820 -0.701  -13.732 1.00 28.57 ? 417  PHE A CZ    1 
ATOM   3407 N  N     . SER A 1 428 ? -25.310 -5.827  -19.017 1.00 26.74 ? 418  SER A N     1 
ATOM   3408 C  CA    . SER A 1 428 ? -25.290 -6.489  -20.333 1.00 27.56 ? 418  SER A CA    1 
ATOM   3409 C  C     . SER A 1 428 ? -26.576 -7.290  -20.575 1.00 28.07 ? 418  SER A C     1 
ATOM   3410 O  O     . SER A 1 428 ? -27.111 -7.300  -21.679 1.00 27.46 ? 418  SER A O     1 
ATOM   3411 C  CB    . SER A 1 428 ? -24.043 -7.366  -20.506 1.00 28.39 ? 418  SER A CB    1 
ATOM   3412 O  OG    . SER A 1 428 ? -24.012 -8.456  -19.605 1.00 29.98 ? 418  SER A OG    1 
ATOM   3413 N  N     . VAL A 1 429 ? -27.076 -7.920  -19.518 1.00 27.72 ? 419  VAL A N     1 
ATOM   3414 C  CA    . VAL A 1 429 ? -28.316 -8.695  -19.563 1.00 28.52 ? 419  VAL A CA    1 
ATOM   3415 C  C     . VAL A 1 429 ? -29.532 -7.774  -19.680 1.00 28.06 ? 419  VAL A C     1 
ATOM   3416 O  O     . VAL A 1 429 ? -30.438 -8.048  -20.464 1.00 28.13 ? 419  VAL A O     1 
ATOM   3417 C  CB    . VAL A 1 429 ? -28.446 -9.620  -18.332 1.00 29.77 ? 419  VAL A CB    1 
ATOM   3418 C  CG1   . VAL A 1 429 ? -29.740 -10.439 -18.376 1.00 30.10 ? 419  VAL A CG1   1 
ATOM   3419 C  CG2   . VAL A 1 429 ? -27.250 -10.566 -18.252 1.00 30.30 ? 419  VAL A CG2   1 
ATOM   3420 N  N     . ALA A 1 430 ? -29.556 -6.688  -18.905 1.00 27.46 ? 420  ALA A N     1 
ATOM   3421 C  CA    . ALA A 1 430 ? -30.639 -5.698  -19.022 1.00 27.22 ? 420  ALA A CA    1 
ATOM   3422 C  C     . ALA A 1 430 ? -30.747 -5.199  -20.469 1.00 26.69 ? 420  ALA A C     1 
ATOM   3423 O  O     . ALA A 1 430 ? -31.847 -5.122  -21.028 1.00 26.77 ? 420  ALA A O     1 
ATOM   3424 C  CB    . ALA A 1 430 ? -30.427 -4.529  -18.065 1.00 27.42 ? 420  ALA A CB    1 
ATOM   3425 N  N     . LEU A 1 431 ? -29.596 -4.903  -21.075 1.00 25.98 ? 421  LEU A N     1 
ATOM   3426 C  CA    . LEU A 1 431 ? -29.554 -4.379  -22.438 1.00 25.66 ? 421  LEU A CA    1 
ATOM   3427 C  C     . LEU A 1 431 ? -29.998 -5.422  -23.462 1.00 26.40 ? 421  LEU A C     1 
ATOM   3428 O  O     . LEU A 1 431 ? -30.802 -5.113  -24.334 1.00 25.70 ? 421  LEU A O     1 
ATOM   3429 C  CB    . LEU A 1 431 ? -28.170 -3.813  -22.780 1.00 25.38 ? 421  LEU A CB    1 
ATOM   3430 C  CG    . LEU A 1 431 ? -27.837 -2.499  -22.053 1.00 24.40 ? 421  LEU A CG    1 
ATOM   3431 C  CD1   . LEU A 1 431 ? -26.366 -2.126  -22.208 1.00 24.25 ? 421  LEU A CD1   1 
ATOM   3432 C  CD2   . LEU A 1 431 ? -28.716 -1.354  -22.543 1.00 24.46 ? 421  LEU A CD2   1 
ATOM   3433 N  N     . SER A 1 432 ? -29.502 -6.651  -23.344 1.00 27.09 ? 422  SER A N     1 
ATOM   3434 C  CA    . SER A 1 432 ? -29.957 -7.725  -24.243 1.00 29.12 ? 422  SER A CA    1 
ATOM   3435 C  C     . SER A 1 432 ? -31.474 -7.950  -24.132 1.00 29.10 ? 422  SER A C     1 
ATOM   3436 O  O     . SER A 1 432 ? -32.150 -8.170  -25.136 1.00 28.58 ? 422  SER A O     1 
ATOM   3437 C  CB    . SER A 1 432 ? -29.189 -9.031  -24.005 1.00 30.95 ? 422  SER A CB    1 
ATOM   3438 O  OG    . SER A 1 432 ? -29.317 -9.453  -22.667 1.00 33.90 ? 422  SER A OG    1 
ATOM   3439 N  N     . THR A 1 433 ? -32.002 -7.837  -22.915 1.00 28.77 ? 423  THR A N     1 
ATOM   3440 C  CA    . THR A 1 433 ? -33.452 -7.945  -22.676 1.00 29.43 ? 423  THR A CA    1 
ATOM   3441 C  C     . THR A 1 433 ? -34.234 -6.830  -23.376 1.00 28.42 ? 423  THR A C     1 
ATOM   3442 O  O     . THR A 1 433 ? -35.246 -7.095  -24.032 1.00 28.70 ? 423  THR A O     1 
ATOM   3443 C  CB    . THR A 1 433 ? -33.732 -7.997  -21.166 1.00 29.71 ? 423  THR A CB    1 
ATOM   3444 O  OG1   . THR A 1 433 ? -33.249 -9.247  -20.668 1.00 30.09 ? 423  THR A OG1   1 
ATOM   3445 C  CG2   . THR A 1 433 ? -35.227 -7.855  -20.832 1.00 30.37 ? 423  THR A CG2   1 
ATOM   3446 N  N     . VAL A 1 434 ? -33.758 -5.591  -23.266 1.00 27.14 ? 424  VAL A N     1 
ATOM   3447 C  CA    . VAL A 1 434 ? -34.379 -4.478  -24.008 1.00 26.86 ? 424  VAL A CA    1 
ATOM   3448 C  C     . VAL A 1 434 ? -34.330 -4.745  -25.526 1.00 26.92 ? 424  VAL A C     1 
ATOM   3449 O  O     . VAL A 1 434 ? -35.310 -4.496  -26.241 1.00 27.42 ? 424  VAL A O     1 
ATOM   3450 C  CB    . VAL A 1 434 ? -33.727 -3.110  -23.685 1.00 26.46 ? 424  VAL A CB    1 
ATOM   3451 C  CG1   . VAL A 1 434 ? -34.270 -2.003  -24.597 1.00 26.31 ? 424  VAL A CG1   1 
ATOM   3452 C  CG2   . VAL A 1 434 ? -33.981 -2.738  -22.231 1.00 25.66 ? 424  VAL A CG2   1 
ATOM   3453 N  N     . TRP A 1 435 ? -33.204 -5.262  -26.006 1.00 27.05 ? 425  TRP A N     1 
ATOM   3454 C  CA    . TRP A 1 435 ? -33.061 -5.507  -27.450 1.00 27.77 ? 425  TRP A CA    1 
ATOM   3455 C  C     . TRP A 1 435 ? -33.956 -6.634  -27.971 1.00 28.83 ? 425  TRP A C     1 
ATOM   3456 O  O     . TRP A 1 435 ? -34.407 -6.580  -29.111 1.00 28.86 ? 425  TRP A O     1 
ATOM   3457 C  CB    . TRP A 1 435 ? -31.596 -5.646  -27.899 1.00 27.25 ? 425  TRP A CB    1 
ATOM   3458 C  CG    . TRP A 1 435 ? -31.213 -4.409  -28.649 1.00 26.39 ? 425  TRP A CG    1 
ATOM   3459 C  CD1   . TRP A 1 435 ? -31.246 -4.234  -30.004 1.00 26.71 ? 425  TRP A CD1   1 
ATOM   3460 C  CD2   . TRP A 1 435 ? -30.859 -3.139  -28.088 1.00 25.77 ? 425  TRP A CD2   1 
ATOM   3461 N  NE1   . TRP A 1 435 ? -30.905 -2.946  -30.320 1.00 26.44 ? 425  TRP A NE1   1 
ATOM   3462 C  CE2   . TRP A 1 435 ? -30.645 -2.256  -29.164 1.00 26.06 ? 425  TRP A CE2   1 
ATOM   3463 C  CE3   . TRP A 1 435 ? -30.667 -2.672  -26.785 1.00 25.27 ? 425  TRP A CE3   1 
ATOM   3464 C  CZ2   . TRP A 1 435 ? -30.268 -0.926  -28.978 1.00 25.97 ? 425  TRP A CZ2   1 
ATOM   3465 C  CZ3   . TRP A 1 435 ? -30.292 -1.343  -26.599 1.00 25.53 ? 425  TRP A CZ3   1 
ATOM   3466 C  CH2   . TRP A 1 435 ? -30.097 -0.487  -27.686 1.00 25.87 ? 425  TRP A CH2   1 
ATOM   3467 N  N     . LYS A 1 436 ? -34.235 -7.631  -27.136 1.00 30.17 ? 426  LYS A N     1 
ATOM   3468 C  CA    . LYS A 1 436 ? -35.237 -8.654  -27.488 1.00 32.24 ? 426  LYS A CA    1 
ATOM   3469 C  C     . LYS A 1 436 ? -36.576 -8.007  -27.799 1.00 32.12 ? 426  LYS A C     1 
ATOM   3470 O  O     . LYS A 1 436 ? -37.275 -8.433  -28.719 1.00 32.29 ? 426  LYS A O     1 
ATOM   3471 C  CB    . LYS A 1 436 ? -35.410 -9.690  -26.373 1.00 34.17 ? 426  LYS A CB    1 
ATOM   3472 C  CG    . LYS A 1 436 ? -34.272 -10.682 -26.277 1.00 36.39 ? 426  LYS A CG    1 
ATOM   3473 C  CD    . LYS A 1 436 ? -34.395 -11.559 -25.041 1.00 38.84 ? 426  LYS A CD    1 
ATOM   3474 C  CE    . LYS A 1 436 ? -33.153 -12.423 -24.865 1.00 40.71 ? 426  LYS A CE    1 
ATOM   3475 N  NZ    . LYS A 1 436 ? -33.190 -13.203 -23.595 1.00 41.79 ? 426  LYS A NZ    1 
ATOM   3476 N  N     . PHE A 1 437 ? -36.927 -6.979  -27.031 1.00 31.38 ? 427  PHE A N     1 
ATOM   3477 C  CA    . PHE A 1 437 ? -38.182 -6.252  -27.220 1.00 31.58 ? 427  PHE A CA    1 
ATOM   3478 C  C     . PHE A 1 437 ? -38.137 -5.350  -28.459 1.00 30.97 ? 427  PHE A C     1 
ATOM   3479 O  O     . PHE A 1 437 ? -39.094 -5.297  -29.229 1.00 31.05 ? 427  PHE A O     1 
ATOM   3480 C  CB    . PHE A 1 437 ? -38.524 -5.453  -25.962 1.00 31.61 ? 427  PHE A CB    1 
ATOM   3481 C  CG    . PHE A 1 437 ? -39.884 -4.819  -25.994 1.00 32.15 ? 427  PHE A CG    1 
ATOM   3482 C  CD1   . PHE A 1 437 ? -41.031 -5.606  -26.092 1.00 32.96 ? 427  PHE A CD1   1 
ATOM   3483 C  CD2   . PHE A 1 437 ? -40.029 -3.438  -25.914 1.00 32.33 ? 427  PHE A CD2   1 
ATOM   3484 C  CE1   . PHE A 1 437 ? -42.287 -5.027  -26.116 1.00 32.96 ? 427  PHE A CE1   1 
ATOM   3485 C  CE2   . PHE A 1 437 ? -41.287 -2.854  -25.936 1.00 32.56 ? 427  PHE A CE2   1 
ATOM   3486 C  CZ    . PHE A 1 437 ? -42.417 -3.650  -26.033 1.00 33.23 ? 427  PHE A CZ    1 
ATOM   3487 N  N     . ILE A 1 438 ? -37.015 -4.661  -28.661 1.00 29.63 ? 428  ILE A N     1 
ATOM   3488 C  CA    . ILE A 1 438 ? -36.811 -3.852  -29.873 1.00 29.12 ? 428  ILE A CA    1 
ATOM   3489 C  C     . ILE A 1 438 ? -36.902 -4.714  -31.141 1.00 29.39 ? 428  ILE A C     1 
ATOM   3490 O  O     . ILE A 1 438 ? -37.590 -4.356  -32.092 1.00 29.05 ? 428  ILE A O     1 
ATOM   3491 C  CB    . ILE A 1 438 ? -35.455 -3.107  -29.824 1.00 28.12 ? 428  ILE A CB    1 
ATOM   3492 C  CG1   . ILE A 1 438 ? -35.503 -2.029  -28.735 1.00 27.82 ? 428  ILE A CG1   1 
ATOM   3493 C  CG2   . ILE A 1 438 ? -35.105 -2.468  -31.174 1.00 27.93 ? 428  ILE A CG2   1 
ATOM   3494 C  CD1   . ILE A 1 438 ? -34.135 -1.530  -28.317 1.00 27.06 ? 428  ILE A CD1   1 
ATOM   3495 N  N     . SER A 1 439 ? -36.202 -5.842  -31.137 1.00 30.02 ? 429  SER A N     1 
ATOM   3496 C  CA    . SER A 1 439 ? -36.216 -6.760  -32.279 1.00 31.52 ? 429  SER A CA    1 
ATOM   3497 C  C     . SER A 1 439 ? -37.619 -7.295  -32.545 1.00 32.51 ? 429  SER A C     1 
ATOM   3498 O  O     . SER A 1 439 ? -38.033 -7.397  -33.693 1.00 32.03 ? 429  SER A O     1 
ATOM   3499 C  CB    . SER A 1 439 ? -35.245 -7.909  -32.060 1.00 32.57 ? 429  SER A CB    1 
ATOM   3500 O  OG    . SER A 1 439 ? -33.920 -7.419  -31.966 1.00 32.75 ? 429  SER A OG    1 
ATOM   3501 N  N     . ARG A 1 440 ? -38.349 -7.608  -31.481 1.00 32.56 ? 430  ARG A N     1 
ATOM   3502 C  CA    . ARG A 1 440 ? -39.728 -8.082  -31.624 1.00 34.09 ? 430  ARG A CA    1 
ATOM   3503 C  C     . ARG A 1 440 ? -40.656 -7.008  -32.192 1.00 33.80 ? 430  ARG A C     1 
ATOM   3504 O  O     . ARG A 1 440 ? -41.623 -7.333  -32.884 1.00 33.41 ? 430  ARG A O     1 
ATOM   3505 C  CB    . ARG A 1 440 ? -40.258 -8.623  -30.294 1.00 35.18 ? 430  ARG A CB    1 
ATOM   3506 C  CG    . ARG A 1 440 ? -41.514 -9.487  -30.429 1.00 36.08 ? 430  ARG A CG    1 
ATOM   3507 C  CD    . ARG A 1 440 ? -42.791 -8.696  -30.178 1.00 36.97 ? 430  ARG A CD    1 
ATOM   3508 N  NE    . ARG A 1 440 ? -43.986 -9.447  -30.575 1.00 37.39 ? 430  ARG A NE    1 
ATOM   3509 C  CZ    . ARG A 1 440 ? -44.390 -9.646  -31.831 1.00 38.62 ? 430  ARG A CZ    1 
ATOM   3510 N  NH1   . ARG A 1 440 ? -43.714 -9.150  -32.874 1.00 37.47 ? 430  ARG A NH1   1 
ATOM   3511 N  NH2   . ARG A 1 440 ? -45.496 -10.353 -32.049 1.00 38.95 ? 430  ARG A NH2   1 
ATOM   3512 N  N     . THR A 1 441 ? -40.366 -5.743  -31.902 1.00 32.68 ? 431  THR A N     1 
ATOM   3513 C  CA    . THR A 1 441 ? -41.165 -4.631  -32.412 1.00 32.61 ? 431  THR A CA    1 
ATOM   3514 C  C     . THR A 1 441 ? -40.956 -4.478  -33.923 1.00 32.93 ? 431  THR A C     1 
ATOM   3515 O  O     . THR A 1 441 ? -41.912 -4.247  -34.658 1.00 31.94 ? 431  THR A O     1 
ATOM   3516 C  CB    . THR A 1 441 ? -40.858 -3.326  -31.662 1.00 32.12 ? 431  THR A CB    1 
ATOM   3517 O  OG1   . THR A 1 441 ? -41.002 -3.555  -30.252 1.00 31.15 ? 431  THR A OG1   1 
ATOM   3518 C  CG2   . THR A 1 441 ? -41.812 -2.218  -32.070 1.00 31.86 ? 431  THR A CG2   1 
ATOM   3519 N  N     . ASN A 1 442 ? -39.716 -4.623  -34.378 1.00 32.38 ? 432  ASN A N     1 
ATOM   3520 C  CA    . ASN A 1 442 ? -39.444 -4.718  -35.820 1.00 33.32 ? 432  ASN A CA    1 
ATOM   3521 C  C     . ASN A 1 442 ? -40.205 -5.890  -36.459 1.00 34.37 ? 432  ASN A C     1 
ATOM   3522 O  O     . ASN A 1 442 ? -40.800 -5.737  -37.520 1.00 34.92 ? 432  ASN A O     1 
ATOM   3523 C  CB    . ASN A 1 442 ? -37.936 -4.844  -36.098 1.00 32.56 ? 432  ASN A CB    1 
ATOM   3524 C  CG    . ASN A 1 442 ? -37.244 -3.498  -36.167 1.00 31.69 ? 432  ASN A CG    1 
ATOM   3525 O  OD1   . ASN A 1 442 ? -37.697 -2.588  -36.862 1.00 30.51 ? 432  ASN A OD1   1 
ATOM   3526 N  ND2   . ASN A 1 442 ? -36.127 -3.371  -35.458 1.00 30.93 ? 432  ASN A ND2   1 
ATOM   3527 N  N     . LYS A 1 443 ? -40.185 -7.042  -35.798 1.00 36.56 ? 433  LYS A N     1 
ATOM   3528 C  CA    . LYS A 1 443 ? -40.896 -8.241  -36.274 1.00 38.55 ? 433  LYS A CA    1 
ATOM   3529 C  C     . LYS A 1 443 ? -42.419 -8.034  -36.369 1.00 38.58 ? 433  LYS A C     1 
ATOM   3530 O  O     . LYS A 1 443 ? -43.061 -8.601  -37.254 1.00 37.36 ? 433  LYS A O     1 
ATOM   3531 C  CB    . LYS A 1 443 ? -40.562 -9.449  -35.384 1.00 40.65 ? 433  LYS A CB    1 
ATOM   3532 C  CG    . LYS A 1 443 ? -41.177 -10.770 -35.832 1.00 43.17 ? 433  LYS A CG    1 
ATOM   3533 C  CD    . LYS A 1 443 ? -40.545 -11.960 -35.116 1.00 45.15 ? 433  LYS A CD    1 
ATOM   3534 C  CE    . LYS A 1 443 ? -41.420 -13.209 -35.181 1.00 47.08 ? 433  LYS A CE    1 
ATOM   3535 N  NZ    . LYS A 1 443 ? -41.779 -13.615 -36.570 1.00 48.22 ? 433  LYS A NZ    1 
ATOM   3536 N  N     . TYR A 1 444 ? -42.974 -7.224  -35.466 1.00 37.88 ? 434  TYR A N     1 
ATOM   3537 C  CA    . TYR A 1 444 ? -44.403 -6.846  -35.474 1.00 38.63 ? 434  TYR A CA    1 
ATOM   3538 C  C     . TYR A 1 444 ? -44.796 -6.077  -36.741 1.00 38.99 ? 434  TYR A C     1 
ATOM   3539 O  O     . TYR A 1 444 ? -45.892 -6.273  -37.257 1.00 38.24 ? 434  TYR A O     1 
ATOM   3540 C  CB    . TYR A 1 444 ? -44.720 -6.020  -34.221 1.00 37.93 ? 434  TYR A CB    1 
ATOM   3541 C  CG    . TYR A 1 444 ? -46.157 -5.551  -33.997 1.00 37.81 ? 434  TYR A CG    1 
ATOM   3542 C  CD1   . TYR A 1 444 ? -47.133 -6.411  -33.485 1.00 39.10 ? 434  TYR A CD1   1 
ATOM   3543 C  CD2   . TYR A 1 444 ? -46.514 -4.222  -34.214 1.00 37.37 ? 434  TYR A CD2   1 
ATOM   3544 C  CE1   . TYR A 1 444 ? -48.429 -5.963  -33.232 1.00 38.51 ? 434  TYR A CE1   1 
ATOM   3545 C  CE2   . TYR A 1 444 ? -47.804 -3.763  -33.963 1.00 37.90 ? 434  TYR A CE2   1 
ATOM   3546 C  CZ    . TYR A 1 444 ? -48.757 -4.637  -33.473 1.00 38.28 ? 434  TYR A CZ    1 
ATOM   3547 O  OH    . TYR A 1 444 ? -50.028 -4.169  -33.228 1.00 38.19 ? 434  TYR A OH    1 
ATOM   3548 N  N     . ILE A 1 445 ? -43.903 -5.217  -37.241 1.00 38.79 ? 435  ILE A N     1 
ATOM   3549 C  CA    . ILE A 1 445 ? -44.119 -4.551  -38.542 1.00 39.65 ? 435  ILE A CA    1 
ATOM   3550 C  C     . ILE A 1 445 ? -44.308 -5.616  -39.632 1.00 40.41 ? 435  ILE A C     1 
ATOM   3551 O  O     . ILE A 1 445 ? -45.273 -5.574  -40.391 1.00 40.09 ? 435  ILE A O     1 
ATOM   3552 C  CB    . ILE A 1 445 ? -42.964 -3.590  -38.955 1.00 38.69 ? 435  ILE A CB    1 
ATOM   3553 C  CG1   . ILE A 1 445 ? -42.798 -2.447  -37.936 1.00 38.29 ? 435  ILE A CG1   1 
ATOM   3554 C  CG2   . ILE A 1 445 ? -43.230 -2.991  -40.340 1.00 38.72 ? 435  ILE A CG2   1 
ATOM   3555 C  CD1   . ILE A 1 445 ? -41.595 -1.545  -38.171 1.00 37.27 ? 435  ILE A CD1   1 
ATOM   3556 N  N     . ASP A 1 446 ? -43.389 -6.572  -39.678 1.00 41.70 ? 436  ASP A N     1 
ATOM   3557 C  CA    . ASP A 1 446 ? -43.387 -7.612  -40.713 1.00 43.61 ? 436  ASP A CA    1 
ATOM   3558 C  C     . ASP A 1 446 ? -44.594 -8.545  -40.596 1.00 45.07 ? 436  ASP A C     1 
ATOM   3559 O  O     . ASP A 1 446 ? -45.178 -8.936  -41.606 1.00 44.72 ? 436  ASP A O     1 
ATOM   3560 C  CB    . ASP A 1 446 ? -42.114 -8.451  -40.634 1.00 44.25 ? 436  ASP A CB    1 
ATOM   3561 C  CG    . ASP A 1 446 ? -40.837 -7.632  -40.814 1.00 44.26 ? 436  ASP A CG    1 
ATOM   3562 O  OD1   . ASP A 1 446 ? -40.887 -6.404  -41.029 1.00 43.02 ? 436  ASP A OD1   1 
ATOM   3563 O  OD2   . ASP A 1 446 ? -39.766 -8.246  -40.718 1.00 47.20 ? 436  ASP A OD2   1 
ATOM   3564 N  N     . GLU A 1 447 ? -44.949 -8.897  -39.363 1.00 45.49 ? 437  GLU A N     1 
ATOM   3565 C  CA    . GLU A 1 447 ? -46.110 -9.752  -39.084 1.00 47.38 ? 437  GLU A CA    1 
ATOM   3566 C  C     . GLU A 1 447 ? -47.448 -9.099  -39.444 1.00 47.96 ? 437  GLU A C     1 
ATOM   3567 O  O     . GLU A 1 447 ? -48.333 -9.759  -39.991 1.00 47.16 ? 437  GLU A O     1 
ATOM   3568 C  CB    . GLU A 1 447 ? -46.133 -10.158 -37.607 1.00 47.57 ? 437  GLU A CB    1 
ATOM   3569 C  CG    . GLU A 1 447 ? -45.087 -11.190 -37.213 1.00 47.77 ? 437  GLU A CG    1 
ATOM   3570 C  CD    . GLU A 1 447 ? -45.022 -11.431 -35.711 1.00 48.50 ? 437  GLU A CD    1 
ATOM   3571 O  OE1   . GLU A 1 447 ? -45.229 -10.481 -34.924 1.00 46.53 ? 437  GLU A OE1   1 
ATOM   3572 O  OE2   . GLU A 1 447 ? -44.750 -12.580 -35.313 1.00 50.47 ? 437  GLU A OE2   1 
ATOM   3573 N  N     . THR A 1 448 ? -47.597 -7.816  -39.128 1.00 47.81 ? 438  THR A N     1 
ATOM   3574 C  CA    . THR A 1 448 ? -48.865 -7.103  -39.341 1.00 48.36 ? 438  THR A CA    1 
ATOM   3575 C  C     . THR A 1 448 ? -49.031 -6.518  -40.749 1.00 48.68 ? 438  THR A C     1 
ATOM   3576 O  O     . THR A 1 448 ? -50.149 -6.220  -41.150 1.00 48.96 ? 438  THR A O     1 
ATOM   3577 C  CB    . THR A 1 448 ? -49.064 -5.968  -38.315 1.00 48.38 ? 438  THR A CB    1 
ATOM   3578 O  OG1   . THR A 1 448 ? -48.030 -4.983  -38.458 1.00 46.74 ? 438  THR A OG1   1 
ATOM   3579 C  CG2   . THR A 1 448 ? -49.064 -6.521  -36.893 1.00 48.64 ? 438  THR A CG2   1 
ATOM   3580 N  N     . THR A 1 449 ? -47.926 -6.352  -41.479 1.00 48.70 ? 439  THR A N     1 
ATOM   3581 C  CA    . THR A 1 449 ? -47.910 -5.741  -42.831 1.00 48.91 ? 439  THR A CA    1 
ATOM   3582 C  C     . THR A 1 449 ? -48.836 -4.515  -42.974 1.00 48.49 ? 439  THR A C     1 
ATOM   3583 O  O     . THR A 1 449 ? -49.836 -4.586  -43.689 1.00 47.52 ? 439  THR A O     1 
ATOM   3584 C  CB    . THR A 1 449 ? -48.280 -6.767  -43.934 1.00 49.58 ? 439  THR A CB    1 
ATOM   3585 O  OG1   . THR A 1 449 ? -49.595 -7.275  -43.697 1.00 49.81 ? 439  THR A OG1   1 
ATOM   3586 C  CG2   . THR A 1 449 ? -47.303 -7.924  -43.967 1.00 49.73 ? 439  THR A CG2   1 
ATOM   3587 N  N     . PRO A 1 450 ? -48.518 -3.397  -42.286 1.00 47.43 ? 440  PRO A N     1 
ATOM   3588 C  CA    . PRO A 1 450 ? -49.342 -2.174  -42.311 1.00 47.79 ? 440  PRO A CA    1 
ATOM   3589 C  C     . PRO A 1 450 ? -49.755 -1.683  -43.706 1.00 48.46 ? 440  PRO A C     1 
ATOM   3590 O  O     . PRO A 1 450 ? -50.870 -1.197  -43.879 1.00 48.19 ? 440  PRO A O     1 
ATOM   3591 C  CB    . PRO A 1 450 ? -48.433 -1.135  -41.647 1.00 47.89 ? 440  PRO A CB    1 
ATOM   3592 C  CG    . PRO A 1 450 ? -47.581 -1.928  -40.727 1.00 46.95 ? 440  PRO A CG    1 
ATOM   3593 C  CD    . PRO A 1 450 ? -47.336 -3.229  -41.417 1.00 47.04 ? 440  PRO A CD    1 
ATOM   3594 N  N     . TRP A 1 451 ? -48.833 -1.791  -44.658 1.00 48.09 ? 441  TRP A N     1 
ATOM   3595 C  CA    . TRP A 1 451 ? -49.070 -1.464  -46.079 1.00 48.97 ? 441  TRP A CA    1 
ATOM   3596 C  C     . TRP A 1 451 ? -50.289 -2.170  -46.692 1.00 50.05 ? 441  TRP A C     1 
ATOM   3597 O  O     . TRP A 1 451 ? -51.002 -1.569  -47.493 1.00 50.39 ? 441  TRP A O     1 
ATOM   3598 C  CB    . TRP A 1 451 ? -47.809 -1.703  -46.947 1.00 48.18 ? 441  TRP A CB    1 
ATOM   3599 C  CG    . TRP A 1 451 ? -47.116 -3.026  -46.748 1.00 47.45 ? 441  TRP A CG    1 
ATOM   3600 C  CD1   . TRP A 1 451 ? -47.358 -4.188  -47.415 1.00 47.39 ? 441  TRP A CD1   1 
ATOM   3601 C  CD2   . TRP A 1 451 ? -46.055 -3.309  -45.820 1.00 46.40 ? 441  TRP A CD2   1 
ATOM   3602 N  NE1   . TRP A 1 451 ? -46.524 -5.181  -46.957 1.00 46.84 ? 441  TRP A NE1   1 
ATOM   3603 C  CE2   . TRP A 1 451 ? -45.718 -4.670  -45.975 1.00 46.19 ? 441  TRP A CE2   1 
ATOM   3604 C  CE3   . TRP A 1 451 ? -45.370 -2.544  -44.860 1.00 45.54 ? 441  TRP A CE3   1 
ATOM   3605 C  CZ2   . TRP A 1 451 ? -44.720 -5.287  -45.211 1.00 45.82 ? 441  TRP A CZ2   1 
ATOM   3606 C  CZ3   . TRP A 1 451 ? -44.381 -3.157  -44.098 1.00 45.00 ? 441  TRP A CZ3   1 
ATOM   3607 C  CH2   . TRP A 1 451 ? -44.062 -4.515  -44.283 1.00 45.50 ? 441  TRP A CH2   1 
ATOM   3608 N  N     . VAL A 1 452 ? -50.518 -3.426  -46.311 1.00 51.07 ? 442  VAL A N     1 
ATOM   3609 C  CA    . VAL A 1 452 ? -51.712 -4.183  -46.742 1.00 53.68 ? 442  VAL A CA    1 
ATOM   3610 C  C     . VAL A 1 452 ? -52.984 -3.595  -46.120 1.00 54.39 ? 442  VAL A C     1 
ATOM   3611 O  O     . VAL A 1 452 ? -53.997 -3.445  -46.799 1.00 54.36 ? 442  VAL A O     1 
ATOM   3612 C  CB    . VAL A 1 452 ? -51.610 -5.687  -46.381 1.00 54.95 ? 442  VAL A CB    1 
ATOM   3613 C  CG1   . VAL A 1 452 ? -52.898 -6.442  -46.711 1.00 55.74 ? 442  VAL A CG1   1 
ATOM   3614 C  CG2   . VAL A 1 452 ? -50.444 -6.333  -47.112 1.00 55.31 ? 442  VAL A CG2   1 
ATOM   3615 N  N     . LEU A 1 453 ? -52.915 -3.269  -44.832 1.00 54.14 ? 443  LEU A N     1 
ATOM   3616 C  CA    . LEU A 1 453 ? -54.043 -2.681  -44.106 1.00 55.60 ? 443  LEU A CA    1 
ATOM   3617 C  C     . LEU A 1 453 ? -54.400 -1.276  -44.613 1.00 56.50 ? 443  LEU A C     1 
ATOM   3618 O  O     . LEU A 1 453 ? -55.558 -0.863  -44.541 1.00 56.13 ? 443  LEU A O     1 
ATOM   3619 C  CB    . LEU A 1 453 ? -53.752 -2.633  -42.598 1.00 55.09 ? 443  LEU A CB    1 
ATOM   3620 C  CG    . LEU A 1 453 ? -53.426 -3.948  -41.882 1.00 55.62 ? 443  LEU A CG    1 
ATOM   3621 C  CD1   . LEU A 1 453 ? -53.069 -3.662  -40.432 1.00 55.54 ? 443  LEU A CD1   1 
ATOM   3622 C  CD2   . LEU A 1 453 ? -54.567 -4.951  -41.952 1.00 56.74 ? 443  LEU A CD2   1 
ATOM   3623 N  N     . ALA A 1 454 ? -53.406 -0.562  -45.141 1.00 57.23 ? 444  ALA A N     1 
ATOM   3624 C  CA    . ALA A 1 454 ? -53.598 0.776   -45.714 1.00 59.23 ? 444  ALA A CA    1 
ATOM   3625 C  C     . ALA A 1 454 ? -54.329 0.801   -47.070 1.00 61.98 ? 444  ALA A C     1 
ATOM   3626 O  O     . ALA A 1 454 ? -54.656 1.878   -47.560 1.00 61.30 ? 444  ALA A O     1 
ATOM   3627 C  CB    . ALA A 1 454 ? -52.252 1.473   -45.849 1.00 59.28 ? 444  ALA A CB    1 
ATOM   3628 N  N     . LYS A 1 455 ? -54.560 -0.367  -47.672 1.00 66.04 ? 445  LYS A N     1 
ATOM   3629 C  CA    . LYS A 1 455 ? -55.216 -0.481  -48.987 1.00 69.97 ? 445  LYS A CA    1 
ATOM   3630 C  C     . LYS A 1 455 ? -56.703 -0.145  -48.971 1.00 72.95 ? 445  LYS A C     1 
ATOM   3631 O  O     . LYS A 1 455 ? -57.209 0.459   -49.917 1.00 73.10 ? 445  LYS A O     1 
ATOM   3632 C  CB    . LYS A 1 455 ? -55.049 -1.897  -49.550 1.00 70.44 ? 445  LYS A CB    1 
ATOM   3633 C  CG    . LYS A 1 455 ? -53.611 -2.317  -49.807 1.00 70.96 ? 445  LYS A CG    1 
ATOM   3634 C  CD    . LYS A 1 455 ? -53.023 -1.644  -51.037 1.00 71.76 ? 445  LYS A CD    1 
ATOM   3635 C  CE    . LYS A 1 455 ? -51.536 -1.930  -51.171 1.00 71.92 ? 445  LYS A CE    1 
ATOM   3636 N  NZ    . LYS A 1 455 ? -51.239 -3.352  -51.501 1.00 72.52 ? 445  LYS A NZ    1 
ATOM   3637 N  N     . ASP A 1 456 ? -57.394 -0.553  -47.909 1.00 76.38 ? 446  ASP A N     1 
ATOM   3638 C  CA    . ASP A 1 456 ? -58.847 -0.364  -47.796 1.00 79.61 ? 446  ASP A CA    1 
ATOM   3639 C  C     . ASP A 1 456 ? -59.230 0.408   -46.531 1.00 80.34 ? 446  ASP A C     1 
ATOM   3640 O  O     . ASP A 1 456 ? -58.661 0.183   -45.460 1.00 79.86 ? 446  ASP A O     1 
ATOM   3641 C  CB    . ASP A 1 456 ? -59.599 -1.708  -47.881 1.00 81.16 ? 446  ASP A CB    1 
ATOM   3642 C  CG    . ASP A 1 456 ? -59.121 -2.736  -46.863 1.00 81.16 ? 446  ASP A CG    1 
ATOM   3643 O  OD1   . ASP A 1 456 ? -57.914 -2.762  -46.544 1.00 82.37 ? 446  ASP A OD1   1 
ATOM   3644 O  OD2   . ASP A 1 456 ? -59.958 -3.540  -46.400 1.00 81.27 ? 446  ASP A OD2   1 
ATOM   3645 N  N     . ASP A 1 457 ? -60.205 1.309   -46.670 1.00 81.96 ? 447  ASP A N     1 
ATOM   3646 C  CA    . ASP A 1 457 ? -60.690 2.147   -45.557 1.00 83.10 ? 447  ASP A CA    1 
ATOM   3647 C  C     . ASP A 1 457 ? -61.398 1.366   -44.445 1.00 82.29 ? 447  ASP A C     1 
ATOM   3648 O  O     . ASP A 1 457 ? -61.616 1.907   -43.359 1.00 82.24 ? 447  ASP A O     1 
ATOM   3649 C  CB    . ASP A 1 457 ? -61.644 3.238   -46.061 1.00 84.67 ? 447  ASP A CB    1 
ATOM   3650 C  CG    . ASP A 1 457 ? -60.995 4.183   -47.058 1.00 85.95 ? 447  ASP A CG    1 
ATOM   3651 O  OD1   . ASP A 1 457 ? -59.855 3.922   -47.502 1.00 86.23 ? 447  ASP A OD1   1 
ATOM   3652 O  OD2   . ASP A 1 457 ? -61.642 5.193   -47.405 1.00 87.12 ? 447  ASP A OD2   1 
ATOM   3653 N  N     . SER A 1 458 ? -61.768 0.114   -44.721 1.00 80.82 ? 448  SER A N     1 
ATOM   3654 C  CA    . SER A 1 458 ? -62.325 -0.787  -43.708 1.00 79.58 ? 448  SER A CA    1 
ATOM   3655 C  C     . SER A 1 458 ? -61.338 -1.144  -42.582 1.00 77.32 ? 448  SER A C     1 
ATOM   3656 O  O     . SER A 1 458 ? -61.763 -1.528  -41.493 1.00 75.62 ? 448  SER A O     1 
ATOM   3657 C  CB    . SER A 1 458 ? -62.853 -2.065  -44.377 1.00 79.80 ? 448  SER A CB    1 
ATOM   3658 O  OG    . SER A 1 458 ? -61.822 -3.004  -44.625 1.00 78.75 ? 448  SER A OG    1 
ATOM   3659 N  N     . GLN A 1 459 ? -60.037 -1.019  -42.855 1.00 75.85 ? 449  GLN A N     1 
ATOM   3660 C  CA    . GLN A 1 459 ? -58.976 -1.369  -41.906 1.00 74.33 ? 449  GLN A CA    1 
ATOM   3661 C  C     . GLN A 1 459 ? -58.198 -0.164  -41.353 1.00 72.53 ? 449  GLN A C     1 
ATOM   3662 O  O     . GLN A 1 459 ? -57.118 -0.338  -40.785 1.00 71.05 ? 449  GLN A O     1 
ATOM   3663 C  CB    . GLN A 1 459 ? -58.000 -2.328  -42.593 1.00 74.68 ? 449  GLN A CB    1 
ATOM   3664 C  CG    . GLN A 1 459 ? -58.608 -3.656  -43.017 1.00 75.34 ? 449  GLN A CG    1 
ATOM   3665 C  CD    . GLN A 1 459 ? -58.601 -4.693  -41.908 1.00 75.29 ? 449  GLN A CD    1 
ATOM   3666 O  OE1   . GLN A 1 459 ? -58.884 -4.388  -40.751 1.00 74.41 ? 449  GLN A OE1   1 
ATOM   3667 N  NE2   . GLN A 1 459 ? -58.277 -5.933  -42.261 1.00 75.45 ? 449  GLN A NE2   1 
ATOM   3668 N  N     . LYS A 1 460 ? -58.741 1.044   -41.497 1.00 71.16 ? 450  LYS A N     1 
ATOM   3669 C  CA    . LYS A 1 460 ? -58.060 2.254   -41.015 1.00 71.21 ? 450  LYS A CA    1 
ATOM   3670 C  C     . LYS A 1 460 ? -57.934 2.275   -39.485 1.00 70.28 ? 450  LYS A C     1 
ATOM   3671 O  O     . LYS A 1 460 ? -56.951 2.785   -38.936 1.00 68.89 ? 450  LYS A O     1 
ATOM   3672 C  CB    . LYS A 1 460 ? -58.776 3.509   -41.515 1.00 71.74 ? 450  LYS A CB    1 
ATOM   3673 C  CG    . LYS A 1 460 ? -58.110 4.821   -41.098 1.00 72.54 ? 450  LYS A CG    1 
ATOM   3674 C  CD    . LYS A 1 460 ? -58.087 5.866   -42.213 1.00 73.32 ? 450  LYS A CD    1 
ATOM   3675 C  CE    . LYS A 1 460 ? -58.402 7.275   -41.720 1.00 73.93 ? 450  LYS A CE    1 
ATOM   3676 N  NZ    . LYS A 1 460 ? -57.320 7.914   -40.920 1.00 73.49 ? 450  LYS A NZ    1 
ATOM   3677 N  N     . ASP A 1 461 ? -58.932 1.704   -38.820 1.00 69.35 ? 451  ASP A N     1 
ATOM   3678 C  CA    . ASP A 1 461 ? -58.961 1.583   -37.366 1.00 68.83 ? 451  ASP A CA    1 
ATOM   3679 C  C     . ASP A 1 461 ? -57.859 0.647   -36.856 1.00 65.53 ? 451  ASP A C     1 
ATOM   3680 O  O     . ASP A 1 461 ? -57.109 0.998   -35.942 1.00 64.40 ? 451  ASP A O     1 
ATOM   3681 C  CB    . ASP A 1 461 ? -60.338 1.068   -36.940 1.00 70.67 ? 451  ASP A CB    1 
ATOM   3682 C  CG    . ASP A 1 461 ? -60.549 1.111   -35.445 1.00 72.05 ? 451  ASP A CG    1 
ATOM   3683 O  OD1   . ASP A 1 461 ? -60.357 2.187   -34.843 1.00 73.01 ? 451  ASP A OD1   1 
ATOM   3684 O  OD2   . ASP A 1 461 ? -60.927 0.068   -34.873 1.00 74.20 ? 451  ASP A OD2   1 
ATOM   3685 N  N     . MET A 1 462 ? -57.780 -0.538  -37.457 1.00 62.74 ? 452  MET A N     1 
ATOM   3686 C  CA    . MET A 1 462 ? -56.743 -1.527  -37.146 1.00 61.00 ? 452  MET A CA    1 
ATOM   3687 C  C     . MET A 1 462 ? -55.335 -1.028  -37.486 1.00 58.78 ? 452  MET A C     1 
ATOM   3688 O  O     . MET A 1 462 ? -54.385 -1.333  -36.766 1.00 57.26 ? 452  MET A O     1 
ATOM   3689 C  CB    . MET A 1 462 ? -57.017 -2.839  -37.893 1.00 61.62 ? 452  MET A CB    1 
ATOM   3690 C  CG    . MET A 1 462 ? -56.010 -3.965  -37.651 1.00 61.60 ? 452  MET A CG    1 
ATOM   3691 S  SD    . MET A 1 462 ? -55.857 -4.510  -35.938 1.00 60.63 ? 452  MET A SD    1 
ATOM   3692 C  CE    . MET A 1 462 ? -57.487 -5.204  -35.656 1.00 62.54 ? 452  MET A CE    1 
ATOM   3693 N  N     . LEU A 1 463 ? -55.206 -0.282  -38.582 1.00 56.43 ? 453  LEU A N     1 
ATOM   3694 C  CA    . LEU A 1 463 ? -53.920 0.308   -38.967 1.00 55.19 ? 453  LEU A CA    1 
ATOM   3695 C  C     . LEU A 1 463 ? -53.449 1.291   -37.899 1.00 53.27 ? 453  LEU A C     1 
ATOM   3696 O  O     . LEU A 1 463 ? -52.277 1.269   -37.503 1.00 50.43 ? 453  LEU A O     1 
ATOM   3697 C  CB    . LEU A 1 463 ? -54.020 1.007   -40.326 1.00 55.67 ? 453  LEU A CB    1 
ATOM   3698 C  CG    . LEU A 1 463 ? -52.755 1.664   -40.897 1.00 55.90 ? 453  LEU A CG    1 
ATOM   3699 C  CD1   . LEU A 1 463 ? -51.610 0.674   -41.070 1.00 55.25 ? 453  LEU A CD1   1 
ATOM   3700 C  CD2   . LEU A 1 463 ? -53.077 2.336   -42.223 1.00 56.42 ? 453  LEU A CD2   1 
ATOM   3701 N  N     . GLY A 1 464 ? -54.372 2.137   -37.439 1.00 51.16 ? 454  GLY A N     1 
ATOM   3702 C  CA    . GLY A 1 464 ? -54.125 3.071   -36.335 1.00 49.77 ? 454  GLY A CA    1 
ATOM   3703 C  C     . GLY A 1 464 ? -53.643 2.389   -35.065 1.00 48.57 ? 454  GLY A C     1 
ATOM   3704 O  O     . GLY A 1 464 ? -52.753 2.895   -34.381 1.00 47.61 ? 454  GLY A O     1 
ATOM   3705 N  N     . ASN A 1 465 ? -54.234 1.236   -34.764 1.00 46.97 ? 455  ASN A N     1 
ATOM   3706 C  CA    . ASN A 1 465 ? -53.838 0.407   -33.630 1.00 46.55 ? 455  ASN A CA    1 
ATOM   3707 C  C     . ASN A 1 465 ? -52.415 -0.147  -33.752 1.00 45.65 ? 455  ASN A C     1 
ATOM   3708 O  O     . ASN A 1 465 ? -51.686 -0.200  -32.763 1.00 43.77 ? 455  ASN A O     1 
ATOM   3709 C  CB    . ASN A 1 465 ? -54.807 -0.754  -33.490 1.00 47.06 ? 455  ASN A CB    1 
ATOM   3710 C  CG    . ASN A 1 465 ? -54.387 -1.736  -32.427 1.00 46.54 ? 455  ASN A CG    1 
ATOM   3711 O  OD1   . ASN A 1 465 ? -54.515 -1.459  -31.243 1.00 47.19 ? 455  ASN A OD1   1 
ATOM   3712 N  ND2   . ASN A 1 465 ? -53.884 -2.888  -32.844 1.00 45.35 ? 455  ASN A ND2   1 
ATOM   3713 N  N     . VAL A 1 466 ? -52.054 -0.602  -34.949 1.00 44.36 ? 456  VAL A N     1 
ATOM   3714 C  CA    . VAL A 1 466 ? -50.705 -1.103  -35.221 1.00 43.98 ? 456  VAL A CA    1 
ATOM   3715 C  C     . VAL A 1 466 ? -49.676 0.018   -35.010 1.00 41.94 ? 456  VAL A C     1 
ATOM   3716 O  O     . VAL A 1 466 ? -48.682 -0.185  -34.305 1.00 40.77 ? 456  VAL A O     1 
ATOM   3717 C  CB    . VAL A 1 466 ? -50.623 -1.749  -36.629 1.00 45.14 ? 456  VAL A CB    1 
ATOM   3718 C  CG1   . VAL A 1 466 ? -49.187 -2.047  -37.055 1.00 45.05 ? 456  VAL A CG1   1 
ATOM   3719 C  CG2   . VAL A 1 466 ? -51.434 -3.037  -36.648 1.00 45.71 ? 456  VAL A CG2   1 
ATOM   3720 N  N     . MET A 1 467 ? -49.941 1.194   -35.580 1.00 40.44 ? 457  MET A N     1 
ATOM   3721 C  CA    . MET A 1 467 ? -49.089 2.378   -35.386 1.00 40.33 ? 457  MET A CA    1 
ATOM   3722 C  C     . MET A 1 467 ? -48.972 2.755   -33.902 1.00 39.66 ? 457  MET A C     1 
ATOM   3723 O  O     . MET A 1 467 ? -47.889 3.090   -33.422 1.00 37.33 ? 457  MET A O     1 
ATOM   3724 C  CB    . MET A 1 467 ? -49.618 3.586   -36.165 1.00 40.81 ? 457  MET A CB    1 
ATOM   3725 C  CG    . MET A 1 467 ? -49.657 3.452   -37.684 1.00 41.77 ? 457  MET A CG    1 
ATOM   3726 S  SD    . MET A 1 467 ? -48.086 3.087   -38.492 1.00 41.44 ? 457  MET A SD    1 
ATOM   3727 C  CE    . MET A 1 467 ? -48.169 1.310   -38.595 1.00 40.89 ? 457  MET A CE    1 
ATOM   3728 N  N     . ALA A 1 468 ? -50.092 2.708   -33.187 1.00 38.75 ? 458  ALA A N     1 
ATOM   3729 C  CA    . ALA A 1 468 ? -50.102 3.000   -31.753 1.00 38.76 ? 458  ALA A CA    1 
ATOM   3730 C  C     . ALA A 1 468 ? -49.220 2.042   -30.960 1.00 37.42 ? 458  ALA A C     1 
ATOM   3731 O  O     . ALA A 1 468 ? -48.510 2.461   -30.041 1.00 37.75 ? 458  ALA A O     1 
ATOM   3732 C  CB    . ALA A 1 468 ? -51.527 2.968   -31.216 1.00 39.31 ? 458  ALA A CB    1 
ATOM   3733 N  N     . HIS A 1 469 ? -49.268 0.763   -31.317 1.00 37.09 ? 459  HIS A N     1 
ATOM   3734 C  CA    . HIS A 1 469 ? -48.452 -0.249  -30.647 1.00 37.74 ? 459  HIS A CA    1 
ATOM   3735 C  C     . HIS A 1 469 ? -46.958 -0.124  -30.940 1.00 37.28 ? 459  HIS A C     1 
ATOM   3736 O  O     . HIS A 1 469 ? -46.134 -0.379  -30.055 1.00 35.73 ? 459  HIS A O     1 
ATOM   3737 C  CB    . HIS A 1 469 ? -48.948 -1.656  -30.955 1.00 38.84 ? 459  HIS A CB    1 
ATOM   3738 C  CG    . HIS A 1 469 ? -50.067 -2.085  -30.063 1.00 40.37 ? 459  HIS A CG    1 
ATOM   3739 N  ND1   . HIS A 1 469 ? -51.383 -1.760  -30.312 1.00 41.40 ? 459  HIS A ND1   1 
ATOM   3740 C  CD2   . HIS A 1 469 ? -50.060 -2.769  -28.896 1.00 41.14 ? 459  HIS A CD2   1 
ATOM   3741 C  CE1   . HIS A 1 469 ? -52.142 -2.246  -29.346 1.00 41.82 ? 459  HIS A CE1   1 
ATOM   3742 N  NE2   . HIS A 1 469 ? -51.365 -2.864  -28.475 1.00 41.45 ? 459  HIS A NE2   1 
ATOM   3743 N  N     . LEU A 1 470 ? -46.618 0.253   -32.170 1.00 35.98 ? 460  LEU A N     1 
ATOM   3744 C  CA    . LEU A 1 470 ? -45.216 0.476   -32.532 1.00 35.68 ? 460  LEU A CA    1 
ATOM   3745 C  C     . LEU A 1 470 ? -44.633 1.626   -31.715 1.00 34.58 ? 460  LEU A C     1 
ATOM   3746 O  O     . LEU A 1 470 ? -43.554 1.491   -31.135 1.00 33.82 ? 460  LEU A O     1 
ATOM   3747 C  CB    . LEU A 1 470 ? -45.062 0.757   -34.029 1.00 36.10 ? 460  LEU A CB    1 
ATOM   3748 C  CG    . LEU A 1 470 ? -45.294 -0.422  -34.981 1.00 36.39 ? 460  LEU A CG    1 
ATOM   3749 C  CD1   . LEU A 1 470 ? -45.366 0.088   -36.414 1.00 36.32 ? 460  LEU A CD1   1 
ATOM   3750 C  CD2   . LEU A 1 470 ? -44.198 -1.469  -34.850 1.00 36.17 ? 460  LEU A CD2   1 
ATOM   3751 N  N     . VAL A 1 471 ? -45.364 2.736   -31.662 1.00 34.45 ? 461  VAL A N     1 
ATOM   3752 C  CA    . VAL A 1 471 ? -44.934 3.917   -30.921 1.00 34.85 ? 461  VAL A CA    1 
ATOM   3753 C  C     . VAL A 1 471 ? -44.843 3.645   -29.417 1.00 34.74 ? 461  VAL A C     1 
ATOM   3754 O  O     . VAL A 1 471 ? -43.867 4.058   -28.782 1.00 33.05 ? 461  VAL A O     1 
ATOM   3755 C  CB    . VAL A 1 471 ? -45.837 5.138   -31.217 1.00 35.46 ? 461  VAL A CB    1 
ATOM   3756 C  CG1   . VAL A 1 471 ? -45.496 6.326   -30.321 1.00 35.03 ? 461  VAL A CG1   1 
ATOM   3757 C  CG2   . VAL A 1 471 ? -45.686 5.548   -32.674 1.00 35.48 ? 461  VAL A CG2   1 
ATOM   3758 N  N     . GLU A 1 472 ? -45.836 2.958   -28.851 1.00 34.20 ? 462  GLU A N     1 
ATOM   3759 C  CA    . GLU A 1 472 ? -45.811 2.664   -27.407 1.00 34.64 ? 462  GLU A CA    1 
ATOM   3760 C  C     . GLU A 1 472 ? -44.657 1.707   -27.057 1.00 33.81 ? 462  GLU A C     1 
ATOM   3761 O  O     . GLU A 1 472 ? -43.978 1.909   -26.055 1.00 33.03 ? 462  GLU A O     1 
ATOM   3762 C  CB    . GLU A 1 472 ? -47.171 2.157   -26.893 1.00 35.27 ? 462  GLU A CB    1 
ATOM   3763 C  CG    . GLU A 1 472 ? -47.242 1.871   -25.387 1.00 35.60 ? 462  GLU A CG    1 
ATOM   3764 C  CD    . GLU A 1 472 ? -47.249 3.108   -24.491 1.00 36.04 ? 462  GLU A CD    1 
ATOM   3765 O  OE1   . GLU A 1 472 ? -46.935 4.231   -24.936 1.00 36.18 ? 462  GLU A OE1   1 
ATOM   3766 O  OE2   . GLU A 1 472 ? -47.595 2.963   -23.296 1.00 36.34 ? 462  GLU A OE2   1 
ATOM   3767 N  N     . ASN A 1 473 ? -44.418 0.698   -27.894 1.00 32.82 ? 463  ASN A N     1 
ATOM   3768 C  CA    . ASN A 1 473 ? -43.217 -0.155  -27.759 1.00 32.30 ? 463  ASN A CA    1 
ATOM   3769 C  C     . ASN A 1 473 ? -41.916 0.660   -27.790 1.00 31.41 ? 463  ASN A C     1 
ATOM   3770 O  O     . ASN A 1 473 ? -41.031 0.449   -26.957 1.00 29.89 ? 463  ASN A O     1 
ATOM   3771 C  CB    . ASN A 1 473 ? -43.155 -1.216  -28.872 1.00 32.56 ? 463  ASN A CB    1 
ATOM   3772 C  CG    . ASN A 1 473 ? -44.087 -2.396  -28.629 1.00 32.57 ? 463  ASN A CG    1 
ATOM   3773 O  OD1   . ASN A 1 473 ? -45.071 -2.301  -27.882 1.00 32.26 ? 463  ASN A OD1   1 
ATOM   3774 N  ND2   . ASN A 1 473 ? -43.770 -3.522  -29.250 1.00 31.51 ? 463  ASN A ND2   1 
ATOM   3775 N  N     . ILE A 1 474 ? -41.809 1.578   -28.753 1.00 30.54 ? 464  ILE A N     1 
ATOM   3776 C  CA    . ILE A 1 474 ? -40.622 2.439   -28.892 1.00 30.90 ? 464  ILE A CA    1 
ATOM   3777 C  C     . ILE A 1 474 ? -40.440 3.268   -27.613 1.00 30.37 ? 464  ILE A C     1 
ATOM   3778 O  O     . ILE A 1 474 ? -39.326 3.391   -27.088 1.00 28.84 ? 464  ILE A O     1 
ATOM   3779 C  CB    . ILE A 1 474 ? -40.715 3.349   -30.143 1.00 31.28 ? 464  ILE A CB    1 
ATOM   3780 C  CG1   . ILE A 1 474 ? -40.506 2.506   -31.417 1.00 31.90 ? 464  ILE A CG1   1 
ATOM   3781 C  CG2   . ILE A 1 474 ? -39.679 4.476   -30.101 1.00 31.42 ? 464  ILE A CG2   1 
ATOM   3782 C  CD1   . ILE A 1 474 ? -40.980 3.172   -32.694 1.00 31.96 ? 464  ILE A CD1   1 
ATOM   3783 N  N     . ARG A 1 475 ? -41.545 3.818   -27.116 1.00 29.70 ? 465  ARG A N     1 
ATOM   3784 C  CA    . ARG A 1 475 ? -41.527 4.617   -25.889 1.00 29.56 ? 465  ARG A CA    1 
ATOM   3785 C  C     . ARG A 1 475 ? -40.957 3.834   -24.713 1.00 29.07 ? 465  ARG A C     1 
ATOM   3786 O  O     . ARG A 1 475 ? -40.102 4.353   -23.997 1.00 27.86 ? 465  ARG A O     1 
ATOM   3787 C  CB    . ARG A 1 475 ? -42.926 5.138   -25.540 1.00 30.47 ? 465  ARG A CB    1 
ATOM   3788 C  CG    . ARG A 1 475 ? -42.906 6.275   -24.517 1.00 30.97 ? 465  ARG A CG    1 
ATOM   3789 C  CD    . ARG A 1 475 ? -44.323 6.703   -24.145 1.00 31.67 ? 465  ARG A CD    1 
ATOM   3790 N  NE    . ARG A 1 475 ? -45.049 5.646   -23.439 1.00 32.28 ? 465  ARG A NE    1 
ATOM   3791 C  CZ    . ARG A 1 475 ? -44.939 5.362   -22.137 1.00 32.76 ? 465  ARG A CZ    1 
ATOM   3792 N  NH1   . ARG A 1 475 ? -44.112 6.054   -21.350 1.00 32.25 ? 465  ARG A NH1   1 
ATOM   3793 N  NH2   . ARG A 1 475 ? -45.657 4.373   -21.614 1.00 32.43 ? 465  ARG A NH2   1 
ATOM   3794 N  N     . TYR A 1 476 ? -41.413 2.592   -24.547 1.00 28.38 ? 466  TYR A N     1 
ATOM   3795 C  CA    . TYR A 1 476 ? -40.889 1.695   -23.505 1.00 28.76 ? 466  TYR A CA    1 
ATOM   3796 C  C     . TYR A 1 476 ? -39.377 1.537   -23.627 1.00 27.65 ? 466  TYR A C     1 
ATOM   3797 O  O     . TYR A 1 476 ? -38.648 1.733   -22.658 1.00 26.34 ? 466  TYR A O     1 
ATOM   3798 C  CB    . TYR A 1 476 ? -41.534 0.314   -23.565 1.00 29.68 ? 466  TYR A CB    1 
ATOM   3799 C  CG    . TYR A 1 476 ? -42.780 0.175   -22.712 1.00 30.81 ? 466  TYR A CG    1 
ATOM   3800 C  CD1   . TYR A 1 476 ? -43.914 0.954   -22.959 1.00 31.52 ? 466  TYR A CD1   1 
ATOM   3801 C  CD2   . TYR A 1 476 ? -42.830 -0.750  -21.673 1.00 31.27 ? 466  TYR A CD2   1 
ATOM   3802 C  CE1   . TYR A 1 476 ? -45.057 0.823   -22.178 1.00 32.38 ? 466  TYR A CE1   1 
ATOM   3803 C  CE2   . TYR A 1 476 ? -43.971 -0.887  -20.886 1.00 31.75 ? 466  TYR A CE2   1 
ATOM   3804 C  CZ    . TYR A 1 476 ? -45.080 -0.107  -21.147 1.00 32.41 ? 466  TYR A CZ    1 
ATOM   3805 O  OH    . TYR A 1 476 ? -46.206 -0.253  -20.357 1.00 32.88 ? 466  TYR A OH    1 
ATOM   3806 N  N     . ALA A 1 477 ? -38.920 1.189   -24.825 1.00 26.98 ? 467  ALA A N     1 
ATOM   3807 C  CA    . ALA A 1 477 ? -37.475 1.047   -25.069 1.00 26.11 ? 467  ALA A CA    1 
ATOM   3808 C  C     . ALA A 1 477 ? -36.717 2.327   -24.723 1.00 26.15 ? 467  ALA A C     1 
ATOM   3809 O  O     . ALA A 1 477 ? -35.678 2.280   -24.064 1.00 25.62 ? 467  ALA A O     1 
ATOM   3810 C  CB    . ALA A 1 477 ? -37.205 0.645   -26.515 1.00 26.62 ? 467  ALA A CB    1 
ATOM   3811 N  N     . ALA A 1 478 ? -37.247 3.469   -25.145 1.00 25.34 ? 468  ALA A N     1 
ATOM   3812 C  CA    . ALA A 1 478 ? -36.575 4.740   -24.923 1.00 26.20 ? 468  ALA A CA    1 
ATOM   3813 C  C     . ALA A 1 478 ? -36.443 5.061   -23.427 1.00 25.70 ? 468  ALA A C     1 
ATOM   3814 O  O     . ALA A 1 478 ? -35.384 5.496   -22.970 1.00 26.18 ? 468  ALA A O     1 
ATOM   3815 C  CB    . ALA A 1 478 ? -37.293 5.851   -25.661 1.00 26.44 ? 468  ALA A CB    1 
ATOM   3816 N  N     . VAL A 1 479 ? -37.502 4.812   -22.661 1.00 25.73 ? 469  VAL A N     1 
ATOM   3817 C  CA    . VAL A 1 479 ? -37.450 5.042   -21.213 1.00 25.87 ? 469  VAL A CA    1 
ATOM   3818 C  C     . VAL A 1 479 ? -36.407 4.138   -20.562 1.00 25.68 ? 469  VAL A C     1 
ATOM   3819 O  O     . VAL A 1 479 ? -35.590 4.609   -19.764 1.00 25.13 ? 469  VAL A O     1 
ATOM   3820 C  CB    . VAL A 1 479 ? -38.818 4.840   -20.527 1.00 26.70 ? 469  VAL A CB    1 
ATOM   3821 C  CG1   . VAL A 1 479 ? -38.687 4.962   -19.010 1.00 26.84 ? 469  VAL A CG1   1 
ATOM   3822 C  CG2   . VAL A 1 479 ? -39.807 5.881   -21.029 1.00 27.46 ? 469  VAL A CG2   1 
ATOM   3823 N  N     . LEU A 1 480 ? -36.431 2.856   -20.909 1.00 25.15 ? 470  LEU A N     1 
ATOM   3824 C  CA    . LEU A 1 480 ? -35.500 1.879   -20.333 1.00 25.35 ? 470  LEU A CA    1 
ATOM   3825 C  C     . LEU A 1 480 ? -34.041 2.166   -20.685 1.00 24.63 ? 470  LEU A C     1 
ATOM   3826 O  O     . LEU A 1 480 ? -33.143 1.778   -19.940 1.00 23.73 ? 470  LEU A O     1 
ATOM   3827 C  CB    . LEU A 1 480 ? -35.861 0.467   -20.782 1.00 26.19 ? 470  LEU A CB    1 
ATOM   3828 C  CG    . LEU A 1 480 ? -37.223 -0.073  -20.317 1.00 26.97 ? 470  LEU A CG    1 
ATOM   3829 C  CD1   . LEU A 1 480 ? -37.470 -1.435  -20.936 1.00 27.55 ? 470  LEU A CD1   1 
ATOM   3830 C  CD2   . LEU A 1 480 ? -37.348 -0.166  -18.806 1.00 27.14 ? 470  LEU A CD2   1 
ATOM   3831 N  N     . LEU A 1 481 ? -33.816 2.840   -21.809 1.00 24.05 ? 471  LEU A N     1 
ATOM   3832 C  CA    . LEU A 1 481 ? -32.463 3.202   -22.226 1.00 23.98 ? 471  LEU A CA    1 
ATOM   3833 C  C     . LEU A 1 481 ? -31.938 4.517   -21.633 1.00 23.77 ? 471  LEU A C     1 
ATOM   3834 O  O     . LEU A 1 481 ? -30.758 4.809   -21.781 1.00 22.71 ? 471  LEU A O     1 
ATOM   3835 C  CB    . LEU A 1 481 ? -32.364 3.218   -23.756 1.00 24.84 ? 471  LEU A CB    1 
ATOM   3836 C  CG    . LEU A 1 481 ? -32.514 1.827   -24.387 1.00 25.65 ? 471  LEU A CG    1 
ATOM   3837 C  CD1   . LEU A 1 481 ? -32.620 1.939   -25.905 1.00 25.96 ? 471  LEU A CD1   1 
ATOM   3838 C  CD2   . LEU A 1 481 ? -31.371 0.879   -24.018 1.00 25.90 ? 471  LEU A CD2   1 
ATOM   3839 N  N     . ARG A 1 482 ? -32.789 5.288   -20.959 1.00 23.62 ? 472  ARG A N     1 
ATOM   3840 C  CA    . ARG A 1 482 ? -32.360 6.575   -20.380 1.00 24.14 ? 472  ARG A CA    1 
ATOM   3841 C  C     . ARG A 1 482 ? -31.157 6.511   -19.412 1.00 23.35 ? 472  ARG A C     1 
ATOM   3842 O  O     . ARG A 1 482 ? -30.364 7.436   -19.407 1.00 24.13 ? 472  ARG A O     1 
ATOM   3843 C  CB    . ARG A 1 482 ? -33.522 7.313   -19.720 1.00 24.99 ? 472  ARG A CB    1 
ATOM   3844 C  CG    . ARG A 1 482 ? -34.499 7.929   -20.717 1.00 26.07 ? 472  ARG A CG    1 
ATOM   3845 C  CD    . ARG A 1 482 ? -35.578 8.728   -20.007 1.00 27.28 ? 472  ARG A CD    1 
ATOM   3846 N  NE    . ARG A 1 482 ? -34.990 9.835   -19.264 1.00 28.39 ? 472  ARG A NE    1 
ATOM   3847 C  CZ    . ARG A 1 482 ? -35.445 10.343  -18.118 1.00 29.22 ? 472  ARG A CZ    1 
ATOM   3848 N  NH1   . ARG A 1 482 ? -36.544 9.886   -17.538 1.00 28.82 ? 472  ARG A NH1   1 
ATOM   3849 N  NH2   . ARG A 1 482 ? -34.772 11.336  -17.546 1.00 30.55 ? 472  ARG A NH2   1 
ATOM   3850 N  N     . PRO A 1 483 ? -31.011 5.434   -18.620 1.00 22.83 ? 473  PRO A N     1 
ATOM   3851 C  CA    . PRO A 1 483 ? -29.772 5.348   -17.814 1.00 22.25 ? 473  PRO A CA    1 
ATOM   3852 C  C     . PRO A 1 483 ? -28.489 5.100   -18.634 1.00 22.57 ? 473  PRO A C     1 
ATOM   3853 O  O     . PRO A 1 483 ? -27.402 5.475   -18.195 1.00 22.66 ? 473  PRO A O     1 
ATOM   3854 C  CB    . PRO A 1 483 ? -30.041 4.163   -16.882 1.00 22.45 ? 473  PRO A CB    1 
ATOM   3855 C  CG    . PRO A 1 483 ? -31.532 4.082   -16.805 1.00 22.94 ? 473  PRO A CG    1 
ATOM   3856 C  CD    . PRO A 1 483 ? -31.976 4.404   -18.208 1.00 22.88 ? 473  PRO A CD    1 
ATOM   3857 N  N     . PHE A 1 484 ? -28.634 4.486   -19.811 1.00 21.76 ? 474  PHE A N     1 
ATOM   3858 C  CA    . PHE A 1 484 ? -27.504 4.071   -20.629 1.00 22.61 ? 474  PHE A CA    1 
ATOM   3859 C  C     . PHE A 1 484 ? -27.089 5.079   -21.698 1.00 22.94 ? 474  PHE A C     1 
ATOM   3860 O  O     . PHE A 1 484 ? -25.902 5.381   -21.857 1.00 23.17 ? 474  PHE A O     1 
ATOM   3861 C  CB    . PHE A 1 484 ? -27.862 2.754   -21.305 1.00 22.14 ? 474  PHE A CB    1 
ATOM   3862 C  CG    . PHE A 1 484 ? -27.969 1.604   -20.355 1.00 21.78 ? 474  PHE A CG    1 
ATOM   3863 C  CD1   . PHE A 1 484 ? -29.208 1.202   -19.842 1.00 22.24 ? 474  PHE A CD1   1 
ATOM   3864 C  CD2   . PHE A 1 484 ? -26.835 0.909   -19.969 1.00 21.56 ? 474  PHE A CD2   1 
ATOM   3865 C  CE1   . PHE A 1 484 ? -29.303 0.130   -18.969 1.00 22.05 ? 474  PHE A CE1   1 
ATOM   3866 C  CE2   . PHE A 1 484 ? -26.922 -0.159  -19.092 1.00 21.47 ? 474  PHE A CE2   1 
ATOM   3867 C  CZ    . PHE A 1 484 ? -28.156 -0.553  -18.590 1.00 21.87 ? 474  PHE A CZ    1 
ATOM   3868 N  N     . LEU A 1 485 ? -28.069 5.546   -22.461 1.00 23.30 ? 475  LEU A N     1 
ATOM   3869 C  CA    . LEU A 1 485 ? -27.845 6.392   -23.644 1.00 23.55 ? 475  LEU A CA    1 
ATOM   3870 C  C     . LEU A 1 485 ? -28.378 7.783   -23.355 1.00 24.45 ? 475  LEU A C     1 
ATOM   3871 O  O     . LEU A 1 485 ? -29.544 7.930   -22.977 1.00 25.47 ? 475  LEU A O     1 
ATOM   3872 C  CB    . LEU A 1 485 ? -28.556 5.805   -24.874 1.00 23.91 ? 475  LEU A CB    1 
ATOM   3873 C  CG    . LEU A 1 485 ? -28.377 4.313   -25.146 1.00 24.31 ? 475  LEU A CG    1 
ATOM   3874 C  CD1   . LEU A 1 485 ? -29.082 3.904   -26.436 1.00 24.90 ? 475  LEU A CD1   1 
ATOM   3875 C  CD2   . LEU A 1 485 ? -26.896 3.963   -25.210 1.00 24.48 ? 475  LEU A CD2   1 
ATOM   3876 N  N     . THR A 1 486 ? -27.529 8.796   -23.538 1.00 24.82 ? 476  THR A N     1 
ATOM   3877 C  CA    . THR A 1 486 ? -27.890 10.181  -23.214 1.00 26.47 ? 476  THR A CA    1 
ATOM   3878 C  C     . THR A 1 486 ? -28.430 10.989  -24.391 1.00 27.14 ? 476  THR A C     1 
ATOM   3879 O  O     . THR A 1 486 ? -29.042 12.036  -24.174 1.00 28.31 ? 476  THR A O     1 
ATOM   3880 C  CB    . THR A 1 486 ? -26.706 10.952  -22.594 1.00 26.58 ? 476  THR A CB    1 
ATOM   3881 O  OG1   . THR A 1 486 ? -25.623 11.028  -23.534 1.00 27.25 ? 476  THR A OG1   1 
ATOM   3882 C  CG2   . THR A 1 486 ? -26.230 10.269  -21.331 1.00 26.63 ? 476  THR A CG2   1 
ATOM   3883 N  N     . HIS A 1 487 ? -28.208 10.527  -25.623 1.00 28.13 ? 477  HIS A N     1 
ATOM   3884 C  CA    . HIS A 1 487 ? -28.725 11.234  -26.802 1.00 29.02 ? 477  HIS A CA    1 
ATOM   3885 C  C     . HIS A 1 487 ? -29.980 10.593  -27.383 1.00 28.33 ? 477  HIS A C     1 
ATOM   3886 O  O     . HIS A 1 487 ? -30.981 11.283  -27.569 1.00 27.96 ? 477  HIS A O     1 
ATOM   3887 C  CB    . HIS A 1 487 ? -27.656 11.376  -27.885 1.00 31.16 ? 477  HIS A CB    1 
ATOM   3888 C  CG    . HIS A 1 487 ? -26.546 12.313  -27.518 1.00 32.79 ? 477  HIS A CG    1 
ATOM   3889 N  ND1   . HIS A 1 487 ? -25.421 12.475  -28.302 1.00 35.16 ? 477  HIS A ND1   1 
ATOM   3890 C  CD2   . HIS A 1 487 ? -26.378 13.123  -26.446 1.00 33.76 ? 477  HIS A CD2   1 
ATOM   3891 C  CE1   . HIS A 1 487 ? -24.614 13.354  -27.732 1.00 35.10 ? 477  HIS A CE1   1 
ATOM   3892 N  NE2   . HIS A 1 487 ? -25.169 13.760  -26.604 1.00 34.47 ? 477  HIS A NE2   1 
ATOM   3893 N  N     . ALA A 1 488 ? -29.931 9.289   -27.663 1.00 27.70 ? 478  ALA A N     1 
ATOM   3894 C  CA    . ALA A 1 488 ? -31.023 8.611   -28.400 1.00 27.77 ? 478  ALA A CA    1 
ATOM   3895 C  C     . ALA A 1 488 ? -32.429 8.739   -27.775 1.00 28.20 ? 478  ALA A C     1 
ATOM   3896 O  O     . ALA A 1 488 ? -33.402 9.025   -28.497 1.00 27.44 ? 478  ALA A O     1 
ATOM   3897 C  CB    . ALA A 1 488 ? -30.691 7.146   -28.643 1.00 27.98 ? 478  ALA A CB    1 
ATOM   3898 N  N     . PRO A 1 489 ? -32.563 8.512   -26.451 1.00 27.74 ? 479  PRO A N     1 
ATOM   3899 C  CA    . PRO A 1 489 ? -33.925 8.593   -25.904 1.00 28.46 ? 479  PRO A CA    1 
ATOM   3900 C  C     . PRO A 1 489 ? -34.568 9.962   -26.104 1.00 30.12 ? 479  PRO A C     1 
ATOM   3901 O  O     . PRO A 1 489 ? -35.705 10.037  -26.562 1.00 29.68 ? 479  PRO A O     1 
ATOM   3902 C  CB    . PRO A 1 489 ? -33.735 8.270   -24.420 1.00 27.99 ? 479  PRO A CB    1 
ATOM   3903 C  CG    . PRO A 1 489 ? -32.510 7.432   -24.384 1.00 27.70 ? 479  PRO A CG    1 
ATOM   3904 C  CD    . PRO A 1 489 ? -31.610 8.043   -25.430 1.00 27.56 ? 479  PRO A CD    1 
ATOM   3905 N  N     . LYS A 1 490 ? -33.822 11.022  -25.797 1.00 31.41 ? 480  LYS A N     1 
ATOM   3906 C  CA    . LYS A 1 490 ? -34.285 12.400  -25.994 1.00 33.75 ? 480  LYS A CA    1 
ATOM   3907 C  C     . LYS A 1 490 ? -34.691 12.655  -27.445 1.00 33.78 ? 480  LYS A C     1 
ATOM   3908 O  O     . LYS A 1 490 ? -35.763 13.198  -27.716 1.00 33.41 ? 480  LYS A O     1 
ATOM   3909 C  CB    . LYS A 1 490 ? -33.184 13.383  -25.582 1.00 36.76 ? 480  LYS A CB    1 
ATOM   3910 C  CG    . LYS A 1 490 ? -33.556 14.850  -25.686 1.00 39.37 ? 480  LYS A CG    1 
ATOM   3911 C  CD    . LYS A 1 490 ? -32.531 15.717  -24.965 1.00 42.08 ? 480  LYS A CD    1 
ATOM   3912 C  CE    . LYS A 1 490 ? -32.878 17.197  -25.068 1.00 44.47 ? 480  LYS A CE    1 
ATOM   3913 N  NZ    . LYS A 1 490 ? -32.514 17.762  -26.398 1.00 45.84 ? 480  LYS A NZ    1 
ATOM   3914 N  N     . GLU A 1 491 ? -33.816 12.257  -28.364 1.00 32.46 ? 481  GLU A N     1 
ATOM   3915 C  CA    . GLU A 1 491 ? -34.085 12.363  -29.792 1.00 32.89 ? 481  GLU A CA    1 
ATOM   3916 C  C     . GLU A 1 491 ? -35.338 11.590  -30.192 1.00 31.86 ? 481  GLU A C     1 
ATOM   3917 O  O     . GLU A 1 491 ? -36.136 12.099  -30.968 1.00 31.25 ? 481  GLU A O     1 
ATOM   3918 C  CB    . GLU A 1 491 ? -32.884 11.876  -30.608 1.00 34.35 ? 481  GLU A CB    1 
ATOM   3919 C  CG    . GLU A 1 491 ? -33.012 12.094  -32.114 1.00 36.22 ? 481  GLU A CG    1 
ATOM   3920 C  CD    . GLU A 1 491 ? -33.126 13.561  -32.509 1.00 37.82 ? 481  GLU A CD    1 
ATOM   3921 O  OE1   . GLU A 1 491 ? -32.465 14.414  -31.882 1.00 39.45 ? 481  GLU A OE1   1 
ATOM   3922 O  OE2   . GLU A 1 491 ? -33.877 13.862  -33.458 1.00 39.55 ? 481  GLU A OE2   1 
ATOM   3923 N  N     . ILE A 1 492 ? -35.514 10.383  -29.652 1.00 30.87 ? 482  ILE A N     1 
ATOM   3924 C  CA    . ILE A 1 492 ? -36.703 9.565   -29.954 1.00 31.66 ? 482  ILE A CA    1 
ATOM   3925 C  C     . ILE A 1 492 ? -37.984 10.254  -29.472 1.00 32.52 ? 482  ILE A C     1 
ATOM   3926 O  O     . ILE A 1 492 ? -38.970 10.318  -30.212 1.00 31.71 ? 482  ILE A O     1 
ATOM   3927 C  CB    . ILE A 1 492 ? -36.587 8.135   -29.381 1.00 31.06 ? 482  ILE A CB    1 
ATOM   3928 C  CG1   . ILE A 1 492 ? -35.552 7.344   -30.192 1.00 31.20 ? 482  ILE A CG1   1 
ATOM   3929 C  CG2   . ILE A 1 492 ? -37.928 7.402   -29.415 1.00 31.32 ? 482  ILE A CG2   1 
ATOM   3930 C  CD1   . ILE A 1 492 ? -35.068 6.075   -29.523 1.00 31.31 ? 482  ILE A CD1   1 
ATOM   3931 N  N     . PHE A 1 493 ? -37.965 10.773  -28.247 1.00 32.91 ? 483  PHE A N     1 
ATOM   3932 C  CA    . PHE A 1 493 ? -39.128 11.502  -27.731 1.00 34.68 ? 483  PHE A CA    1 
ATOM   3933 C  C     . PHE A 1 493 ? -39.441 12.741  -28.575 1.00 35.85 ? 483  PHE A C     1 
ATOM   3934 O  O     . PHE A 1 493 ? -40.612 13.019  -28.851 1.00 36.80 ? 483  PHE A O     1 
ATOM   3935 C  CB    . PHE A 1 493 ? -38.939 11.912  -26.267 1.00 34.79 ? 483  PHE A CB    1 
ATOM   3936 C  CG    . PHE A 1 493 ? -38.781 10.756  -25.312 1.00 35.06 ? 483  PHE A CG    1 
ATOM   3937 C  CD1   . PHE A 1 493 ? -37.690 10.698  -24.449 1.00 35.02 ? 483  PHE A CD1   1 
ATOM   3938 C  CD2   . PHE A 1 493 ? -39.727 9.744   -25.250 1.00 36.22 ? 483  PHE A CD2   1 
ATOM   3939 C  CE1   . PHE A 1 493 ? -37.540 9.644   -23.563 1.00 35.11 ? 483  PHE A CE1   1 
ATOM   3940 C  CE2   . PHE A 1 493 ? -39.585 8.687   -24.360 1.00 36.08 ? 483  PHE A CE2   1 
ATOM   3941 C  CZ    . PHE A 1 493 ? -38.489 8.637   -23.516 1.00 35.31 ? 483  PHE A CZ    1 
ATOM   3942 N  N     . GLU A 1 494 ? -38.405 13.466  -28.994 1.00 37.04 ? 484  GLU A N     1 
ATOM   3943 C  CA    . GLU A 1 494 ? -38.574 14.675  -29.811 1.00 39.49 ? 484  GLU A CA    1 
ATOM   3944 C  C     . GLU A 1 494 ? -39.209 14.393  -31.172 1.00 39.47 ? 484  GLU A C     1 
ATOM   3945 O  O     . GLU A 1 494 ? -40.093 15.135  -31.599 1.00 39.68 ? 484  GLU A O     1 
ATOM   3946 C  CB    . GLU A 1 494 ? -37.243 15.407  -30.011 1.00 41.61 ? 484  GLU A CB    1 
ATOM   3947 C  CG    . GLU A 1 494 ? -36.846 16.299  -28.837 1.00 44.21 ? 484  GLU A CG    1 
ATOM   3948 C  CD    . GLU A 1 494 ? -35.446 16.890  -28.963 1.00 46.31 ? 484  GLU A CD    1 
ATOM   3949 O  OE1   . GLU A 1 494 ? -34.886 17.310  -27.919 1.00 47.70 ? 484  GLU A OE1   1 
ATOM   3950 O  OE2   . GLU A 1 494 ? -34.906 16.942  -30.095 1.00 47.49 ? 484  GLU A OE2   1 
ATOM   3951 N  N     . GLN A 1 495 ? -38.766 13.328  -31.840 1.00 38.30 ? 485  GLN A N     1 
ATOM   3952 C  CA    . GLN A 1 495 ? -39.318 12.956  -33.160 1.00 38.41 ? 485  GLN A CA    1 
ATOM   3953 C  C     . GLN A 1 495 ? -40.744 12.415  -33.089 1.00 39.11 ? 485  GLN A C     1 
ATOM   3954 O  O     . GLN A 1 495 ? -41.545 12.672  -33.986 1.00 38.86 ? 485  GLN A O     1 
ATOM   3955 C  CB    . GLN A 1 495 ? -38.410 11.957  -33.882 1.00 38.08 ? 485  GLN A CB    1 
ATOM   3956 C  CG    . GLN A 1 495 ? -37.069 12.556  -34.280 1.00 38.06 ? 485  GLN A CG    1 
ATOM   3957 C  CD    . GLN A 1 495 ? -36.312 11.725  -35.292 1.00 38.17 ? 485  GLN A CD    1 
ATOM   3958 O  OE1   . GLN A 1 495 ? -36.905 11.009  -36.104 1.00 39.16 ? 485  GLN A OE1   1 
ATOM   3959 N  NE2   . GLN A 1 495 ? -34.989 11.839  -35.269 1.00 37.07 ? 485  GLN A NE2   1 
ATOM   3960 N  N     . LEU A 1 496 ? -41.048 11.660  -32.037 1.00 39.03 ? 486  LEU A N     1 
ATOM   3961 C  CA    . LEU A 1 496 ? -42.420 11.212  -31.761 1.00 40.17 ? 486  LEU A CA    1 
ATOM   3962 C  C     . LEU A 1 496 ? -43.317 12.307  -31.171 1.00 41.49 ? 486  LEU A C     1 
ATOM   3963 O  O     . LEU A 1 496 ? -44.524 12.108  -31.056 1.00 42.46 ? 486  LEU A O     1 
ATOM   3964 C  CB    . LEU A 1 496 ? -42.412 10.007  -30.817 1.00 39.47 ? 486  LEU A CB    1 
ATOM   3965 C  CG    . LEU A 1 496 ? -41.714 8.742   -31.322 1.00 39.31 ? 486  LEU A CG    1 
ATOM   3966 C  CD1   . LEU A 1 496 ? -41.633 7.719   -30.202 1.00 39.06 ? 486  LEU A CD1   1 
ATOM   3967 C  CD2   . LEU A 1 496 ? -42.407 8.146   -32.534 1.00 39.25 ? 486  LEU A CD2   1 
ATOM   3968 N  N     . ASN A 1 497 ? -42.718 13.431  -30.781 1.00 42.93 ? 487  ASN A N     1 
ATOM   3969 C  CA    . ASN A 1 497 ? -43.413 14.583  -30.208 1.00 45.13 ? 487  ASN A CA    1 
ATOM   3970 C  C     . ASN A 1 497 ? -44.182 14.186  -28.942 1.00 45.57 ? 487  ASN A C     1 
ATOM   3971 O  O     . ASN A 1 497 ? -45.346 14.545  -28.757 1.00 45.18 ? 487  ASN A O     1 
ATOM   3972 C  CB    . ASN A 1 497 ? -44.319 15.255  -31.252 1.00 46.29 ? 487  ASN A CB    1 
ATOM   3973 C  CG    . ASN A 1 497 ? -44.709 16.674  -30.869 1.00 47.44 ? 487  ASN A CG    1 
ATOM   3974 O  OD1   . ASN A 1 497 ? -43.911 17.426  -30.307 1.00 47.86 ? 487  ASN A OD1   1 
ATOM   3975 N  ND2   . ASN A 1 497 ? -45.943 17.049  -31.181 1.00 48.36 ? 487  ASN A ND2   1 
ATOM   3976 N  N     . ILE A 1 498 ? -43.508 13.402  -28.102 1.00 46.06 ? 488  ILE A N     1 
ATOM   3977 C  CA    . ILE A 1 498 ? -43.962 13.088  -26.749 1.00 46.95 ? 488  ILE A CA    1 
ATOM   3978 C  C     . ILE A 1 498 ? -43.290 14.126  -25.851 1.00 47.38 ? 488  ILE A C     1 
ATOM   3979 O  O     . ILE A 1 498 ? -42.088 14.035  -25.572 1.00 45.57 ? 488  ILE A O     1 
ATOM   3980 C  CB    . ILE A 1 498 ? -43.605 11.637  -26.350 1.00 47.18 ? 488  ILE A CB    1 
ATOM   3981 C  CG1   . ILE A 1 498 ? -44.317 10.652  -27.294 1.00 46.99 ? 488  ILE A CG1   1 
ATOM   3982 C  CG2   . ILE A 1 498 ? -43.999 11.354  -24.901 1.00 46.88 ? 488  ILE A CG2   1 
ATOM   3983 C  CD1   . ILE A 1 498 ? -43.825 9.221   -27.219 1.00 47.12 ? 488  ILE A CD1   1 
ATOM   3984 N  N     . ASN A 1 499 ? -44.075 15.124  -25.446 1.00 48.02 ? 489  ASN A N     1 
ATOM   3985 C  CA    . ASN A 1 499 ? -43.593 16.293  -24.693 1.00 49.55 ? 489  ASN A CA    1 
ATOM   3986 C  C     . ASN A 1 499 ? -43.822 16.217  -23.183 1.00 48.91 ? 489  ASN A C     1 
ATOM   3987 O  O     . ASN A 1 499 ? -43.110 16.874  -22.424 1.00 49.05 ? 489  ASN A O     1 
ATOM   3988 C  CB    . ASN A 1 499 ? -44.256 17.560  -25.231 1.00 50.94 ? 489  ASN A CB    1 
ATOM   3989 C  CG    . ASN A 1 499 ? -43.862 17.854  -26.661 1.00 51.40 ? 489  ASN A CG    1 
ATOM   3990 O  OD1   . ASN A 1 499 ? -42.700 18.131  -26.946 1.00 52.53 ? 489  ASN A OD1   1 
ATOM   3991 N  ND2   . ASN A 1 499 ? -44.826 17.786  -27.570 1.00 52.28 ? 489  ASN A ND2   1 
ATOM   3992 N  N     . ASN A 1 500 ? -44.820 15.443  -22.760 1.00 47.57 ? 490  ASN A N     1 
ATOM   3993 C  CA    . ASN A 1 500 ? -45.112 15.229  -21.345 1.00 47.48 ? 490  ASN A CA    1 
ATOM   3994 C  C     . ASN A 1 500 ? -43.916 14.561  -20.633 1.00 46.16 ? 490  ASN A C     1 
ATOM   3995 O  O     . ASN A 1 500 ? -43.648 13.386  -20.877 1.00 44.24 ? 490  ASN A O     1 
ATOM   3996 C  CB    . ASN A 1 500 ? -46.366 14.352  -21.223 1.00 48.05 ? 490  ASN A CB    1 
ATOM   3997 C  CG    . ASN A 1 500 ? -46.837 14.167  -19.785 1.00 48.89 ? 490  ASN A CG    1 
ATOM   3998 O  OD1   . ASN A 1 500 ? -46.251 14.696  -18.841 1.00 49.00 ? 490  ASN A OD1   1 
ATOM   3999 N  ND2   . ASN A 1 500 ? -47.909 13.398  -19.620 1.00 48.88 ? 490  ASN A ND2   1 
ATOM   4000 N  N     . PRO A 1 501 ? -43.207 15.297  -19.738 1.00 45.86 ? 491  PRO A N     1 
ATOM   4001 C  CA    . PRO A 1 501 ? -42.040 14.695  -19.053 1.00 44.14 ? 491  PRO A CA    1 
ATOM   4002 C  C     . PRO A 1 501 ? -42.345 13.404  -18.276 1.00 42.73 ? 491  PRO A C     1 
ATOM   4003 O  O     . PRO A 1 501 ? -41.467 12.556  -18.117 1.00 39.75 ? 491  PRO A O     1 
ATOM   4004 C  CB    . PRO A 1 501 ? -41.584 15.801  -18.088 1.00 45.29 ? 491  PRO A CB    1 
ATOM   4005 C  CG    . PRO A 1 501 ? -42.141 17.062  -18.642 1.00 46.35 ? 491  PRO A CG    1 
ATOM   4006 C  CD    . PRO A 1 501 ? -43.455 16.671  -19.254 1.00 46.47 ? 491  PRO A CD    1 
ATOM   4007 N  N     . GLN A 1 502 ? -43.581 13.276  -17.798 1.00 42.52 ? 492  GLN A N     1 
ATOM   4008 C  CA    . GLN A 1 502 ? -44.052 12.076  -17.109 1.00 43.40 ? 492  GLN A CA    1 
ATOM   4009 C  C     . GLN A 1 502 ? -43.990 10.800  -17.950 1.00 41.35 ? 492  GLN A C     1 
ATOM   4010 O  O     . GLN A 1 502 ? -43.751 9.717   -17.414 1.00 39.27 ? 492  GLN A O     1 
ATOM   4011 C  CB    . GLN A 1 502 ? -45.490 12.290  -16.625 1.00 47.06 ? 492  GLN A CB    1 
ATOM   4012 C  CG    . GLN A 1 502 ? -46.101 11.113  -15.862 1.00 49.99 ? 492  GLN A CG    1 
ATOM   4013 C  CD    . GLN A 1 502 ? -45.266 10.669  -14.670 1.00 52.00 ? 492  GLN A CD    1 
ATOM   4014 O  OE1   . GLN A 1 502 ? -45.103 11.413  -13.698 1.00 55.74 ? 492  GLN A OE1   1 
ATOM   4015 N  NE2   . GLN A 1 502 ? -44.736 9.446   -14.738 1.00 53.08 ? 492  GLN A NE2   1 
ATOM   4016 N  N     . PHE A 1 503 ? -44.208 10.930  -19.257 1.00 39.33 ? 493  PHE A N     1 
ATOM   4017 C  CA    . PHE A 1 503 ? -44.143 9.781   -20.167 1.00 38.59 ? 493  PHE A CA    1 
ATOM   4018 C  C     . PHE A 1 503 ? -42.712 9.345   -20.519 1.00 36.77 ? 493  PHE A C     1 
ATOM   4019 O  O     . PHE A 1 503 ? -42.530 8.458   -21.348 1.00 34.58 ? 493  PHE A O     1 
ATOM   4020 C  CB    . PHE A 1 503 ? -44.930 10.068  -21.455 1.00 39.39 ? 493  PHE A CB    1 
ATOM   4021 C  CG    . PHE A 1 503 ? -46.415 10.274  -21.253 1.00 40.89 ? 493  PHE A CG    1 
ATOM   4022 C  CD1   . PHE A 1 503 ? -47.148 10.958  -22.221 1.00 41.73 ? 493  PHE A CD1   1 
ATOM   4023 C  CD2   . PHE A 1 503 ? -47.095 9.780   -20.134 1.00 41.27 ? 493  PHE A CD2   1 
ATOM   4024 C  CE1   . PHE A 1 503 ? -48.513 11.152  -22.082 1.00 42.45 ? 493  PHE A CE1   1 
ATOM   4025 C  CE2   . PHE A 1 503 ? -48.462 9.978   -19.991 1.00 42.22 ? 493  PHE A CE2   1 
ATOM   4026 C  CZ    . PHE A 1 503 ? -49.171 10.661  -20.965 1.00 42.78 ? 493  PHE A CZ    1 
ATOM   4027 N  N     . MET A 1 504 ? -41.716 9.970   -19.893 1.00 35.81 ? 494  MET A N     1 
ATOM   4028 C  CA    . MET A 1 504 ? -40.304 9.570   -20.024 1.00 35.79 ? 494  MET A CA    1 
ATOM   4029 C  C     . MET A 1 504 ? -39.775 8.863   -18.761 1.00 34.78 ? 494  MET A C     1 
ATOM   4030 O  O     . MET A 1 504 ? -38.602 8.498   -18.712 1.00 32.01 ? 494  MET A O     1 
ATOM   4031 C  CB    . MET A 1 504 ? -39.451 10.806  -20.317 1.00 36.91 ? 494  MET A CB    1 
ATOM   4032 C  CG    . MET A 1 504 ? -39.958 11.644  -21.490 1.00 38.34 ? 494  MET A CG    1 
ATOM   4033 S  SD    . MET A 1 504 ? -39.117 13.228  -21.673 1.00 40.62 ? 494  MET A SD    1 
ATOM   4034 C  CE    . MET A 1 504 ? -40.112 13.963  -22.968 1.00 41.03 ? 494  MET A CE    1 
ATOM   4035 N  N     . GLU A 1 505 ? -40.643 8.661   -17.762 1.00 34.00 ? 495  GLU A N     1 
ATOM   4036 C  CA    . GLU A 1 505 ? -40.268 8.078   -16.461 1.00 34.13 ? 495  GLU A CA    1 
ATOM   4037 C  C     . GLU A 1 505 ? -40.741 6.630   -16.302 1.00 32.36 ? 495  GLU A C     1 
ATOM   4038 O  O     . GLU A 1 505 ? -41.682 6.204   -16.973 1.00 31.74 ? 495  GLU A O     1 
ATOM   4039 C  CB    . GLU A 1 505 ? -40.850 8.923   -15.321 1.00 35.58 ? 495  GLU A CB    1 
ATOM   4040 C  CG    . GLU A 1 505 ? -40.475 10.402  -15.357 1.00 36.49 ? 495  GLU A CG    1 
ATOM   4041 C  CD    . GLU A 1 505 ? -38.992 10.667  -15.151 1.00 37.68 ? 495  GLU A CD    1 
ATOM   4042 O  OE1   . GLU A 1 505 ? -38.269 9.780   -14.650 1.00 38.83 ? 495  GLU A OE1   1 
ATOM   4043 O  OE2   . GLU A 1 505 ? -38.541 11.778  -15.491 1.00 39.63 ? 495  GLU A OE2   1 
ATOM   4044 N  N     . PHE A 1 506 ? -40.094 5.894   -15.395 1.00 31.16 ? 496  PHE A N     1 
ATOM   4045 C  CA    . PHE A 1 506 ? -40.387 4.461   -15.176 1.00 31.24 ? 496  PHE A CA    1 
ATOM   4046 C  C     . PHE A 1 506 ? -41.826 4.207   -14.741 1.00 32.23 ? 496  PHE A C     1 
ATOM   4047 O  O     . PHE A 1 506 ? -42.402 3.201   -15.112 1.00 31.85 ? 496  PHE A O     1 
ATOM   4048 C  CB    . PHE A 1 506 ? -39.489 3.844   -14.093 1.00 30.55 ? 496  PHE A CB    1 
ATOM   4049 C  CG    . PHE A 1 506 ? -38.072 3.549   -14.525 1.00 29.52 ? 496  PHE A CG    1 
ATOM   4050 C  CD1   . PHE A 1 506 ? -37.018 3.800   -13.646 1.00 29.15 ? 496  PHE A CD1   1 
ATOM   4051 C  CD2   . PHE A 1 506 ? -37.780 2.978   -15.766 1.00 29.15 ? 496  PHE A CD2   1 
ATOM   4052 C  CE1   . PHE A 1 506 ? -35.708 3.514   -13.997 1.00 28.47 ? 496  PHE A CE1   1 
ATOM   4053 C  CE2   . PHE A 1 506 ? -36.467 2.700   -16.124 1.00 28.64 ? 496  PHE A CE2   1 
ATOM   4054 C  CZ    . PHE A 1 506 ? -35.430 2.972   -15.239 1.00 28.33 ? 496  PHE A CZ    1 
ATOM   4055 N  N     . SER A 1 507 ? -42.376 5.105   -13.926 1.00 34.32 ? 497  SER A N     1 
ATOM   4056 C  CA    . SER A 1 507 ? -43.766 4.986   -13.471 1.00 36.07 ? 497  SER A CA    1 
ATOM   4057 C  C     . SER A 1 507 ? -44.785 4.957   -14.627 1.00 36.64 ? 497  SER A C     1 
ATOM   4058 O  O     . SER A 1 507 ? -45.843 4.339   -14.499 1.00 37.58 ? 497  SER A O     1 
ATOM   4059 C  CB    . SER A 1 507 ? -44.111 6.114   -12.497 1.00 37.29 ? 497  SER A CB    1 
ATOM   4060 O  OG    . SER A 1 507 ? -43.977 7.380   -13.118 1.00 39.13 ? 497  SER A OG    1 
ATOM   4061 N  N     . SER A 1 508 ? -44.458 5.600   -15.751 1.00 36.05 ? 498  SER A N     1 
ATOM   4062 C  CA    . SER A 1 508 ? -45.318 5.568   -16.951 1.00 35.58 ? 498  SER A CA    1 
ATOM   4063 C  C     . SER A 1 508 ? -45.317 4.241   -17.732 1.00 36.32 ? 498  SER A C     1 
ATOM   4064 O  O     . SER A 1 508 ? -46.069 4.113   -18.698 1.00 35.61 ? 498  SER A O     1 
ATOM   4065 C  CB    . SER A 1 508 ? -44.968 6.721   -17.895 1.00 35.43 ? 498  SER A CB    1 
ATOM   4066 O  OG    . SER A 1 508 ? -43.770 6.489   -18.624 1.00 34.05 ? 498  SER A OG    1 
ATOM   4067 N  N     . LEU A 1 509 ? -44.483 3.280   -17.327 1.00 36.41 ? 499  LEU A N     1 
ATOM   4068 C  CA    . LEU A 1 509 ? -44.473 1.931   -17.893 1.00 37.64 ? 499  LEU A CA    1 
ATOM   4069 C  C     . LEU A 1 509 ? -45.339 0.911   -17.143 1.00 39.32 ? 499  LEU A C     1 
ATOM   4070 O  O     . LEU A 1 509 ? -45.401 -0.249  -17.545 1.00 38.77 ? 499  LEU A O     1 
ATOM   4071 C  CB    . LEU A 1 509 ? -43.029 1.415   -17.976 1.00 37.51 ? 499  LEU A CB    1 
ATOM   4072 C  CG    . LEU A 1 509 ? -42.004 2.380   -18.594 1.00 37.42 ? 499  LEU A CG    1 
ATOM   4073 C  CD1   . LEU A 1 509 ? -40.630 1.726   -18.683 1.00 37.22 ? 499  LEU A CD1   1 
ATOM   4074 C  CD2   . LEU A 1 509 ? -42.446 2.861   -19.970 1.00 37.31 ? 499  LEU A CD2   1 
ATOM   4075 N  N     . GLU A 1 510 ? -46.010 1.334   -16.070 1.00 41.45 ? 500  GLU A N     1 
ATOM   4076 C  CA    . GLU A 1 510 ? -46.825 0.427   -15.253 1.00 44.17 ? 500  GLU A CA    1 
ATOM   4077 C  C     . GLU A 1 510 ? -47.990 -0.193  -16.032 1.00 43.90 ? 500  GLU A C     1 
ATOM   4078 O  O     . GLU A 1 510 ? -48.281 -1.377  -15.876 1.00 42.64 ? 500  GLU A O     1 
ATOM   4079 C  CB    . GLU A 1 510 ? -47.362 1.163   -14.023 1.00 46.51 ? 500  GLU A CB    1 
ATOM   4080 C  CG    . GLU A 1 510 ? -46.301 1.439   -12.965 1.00 49.14 ? 500  GLU A CG    1 
ATOM   4081 C  CD    . GLU A 1 510 ? -46.829 2.216   -11.763 1.00 50.78 ? 500  GLU A CD    1 
ATOM   4082 O  OE1   . GLU A 1 510 ? -48.053 2.470   -11.690 1.00 52.14 ? 500  GLU A OE1   1 
ATOM   4083 O  OE2   . GLU A 1 510 ? -46.010 2.572   -10.886 1.00 51.64 ? 500  GLU A OE2   1 
ATOM   4084 N  N     . GLN A 1 511 ? -48.634 0.621   -16.865 1.00 43.82 ? 501  GLN A N     1 
ATOM   4085 C  CA    . GLN A 1 511 ? -49.757 0.175   -17.690 1.00 45.27 ? 501  GLN A CA    1 
ATOM   4086 C  C     . GLN A 1 511 ? -49.565 0.607   -19.145 1.00 43.46 ? 501  GLN A C     1 
ATOM   4087 O  O     . GLN A 1 511 ? -49.441 1.797   -19.438 1.00 42.86 ? 501  GLN A O     1 
ATOM   4088 C  CB    . GLN A 1 511 ? -51.076 0.727   -17.142 1.00 47.05 ? 501  GLN A CB    1 
ATOM   4089 C  CG    . GLN A 1 511 ? -52.308 0.045   -17.727 1.00 49.15 ? 501  GLN A CG    1 
ATOM   4090 C  CD    . GLN A 1 511 ? -53.587 0.349   -16.964 1.00 50.36 ? 501  GLN A CD    1 
ATOM   4091 O  OE1   . GLN A 1 511 ? -53.597 1.131   -16.010 1.00 50.17 ? 501  GLN A OE1   1 
ATOM   4092 N  NE2   . GLN A 1 511 ? -54.679 -0.277  -17.385 1.00 51.20 ? 501  GLN A NE2   1 
ATOM   4093 N  N     . TYR A 1 512 ? -49.554 -0.375  -20.039 1.00 42.31 ? 502  TYR A N     1 
ATOM   4094 C  CA    . TYR A 1 512 ? -49.327 -0.154  -21.464 1.00 42.44 ? 502  TYR A CA    1 
ATOM   4095 C  C     . TYR A 1 512 ? -50.445 0.687   -22.075 1.00 42.42 ? 502  TYR A C     1 
ATOM   4096 O  O     . TYR A 1 512 ? -51.622 0.436   -21.828 1.00 40.94 ? 502  TYR A O     1 
ATOM   4097 C  CB    . TYR A 1 512 ? -49.234 -1.505  -22.180 1.00 41.88 ? 502  TYR A CB    1 
ATOM   4098 C  CG    . TYR A 1 512 ? -48.748 -1.451  -23.618 1.00 41.87 ? 502  TYR A CG    1 
ATOM   4099 C  CD1   . TYR A 1 512 ? -47.421 -1.757  -23.943 1.00 41.11 ? 502  TYR A CD1   1 
ATOM   4100 C  CD2   . TYR A 1 512 ? -49.617 -1.114  -24.658 1.00 41.41 ? 502  TYR A CD2   1 
ATOM   4101 C  CE1   . TYR A 1 512 ? -46.977 -1.721  -25.261 1.00 40.82 ? 502  TYR A CE1   1 
ATOM   4102 C  CE2   . TYR A 1 512 ? -49.180 -1.074  -25.977 1.00 41.42 ? 502  TYR A CE2   1 
ATOM   4103 C  CZ    . TYR A 1 512 ? -47.867 -1.376  -26.276 1.00 40.78 ? 502  TYR A CZ    1 
ATOM   4104 O  OH    . TYR A 1 512 ? -47.464 -1.334  -27.591 1.00 39.08 ? 502  TYR A OH    1 
ATOM   4105 N  N     . GLY A 1 513 ? -50.056 1.704   -22.834 1.00 42.01 ? 503  GLY A N     1 
ATOM   4106 C  CA    . GLY A 1 513 ? -50.978 2.477   -23.670 1.00 43.32 ? 503  GLY A CA    1 
ATOM   4107 C  C     . GLY A 1 513 ? -51.342 3.846   -23.133 1.00 43.65 ? 503  GLY A C     1 
ATOM   4108 O  O     . GLY A 1 513 ? -52.515 4.213   -23.113 1.00 43.10 ? 503  GLY A O     1 
ATOM   4109 N  N     . VAL A 1 514 ? -50.331 4.607   -22.723 1.00 43.27 ? 504  VAL A N     1 
ATOM   4110 C  CA    . VAL A 1 514 ? -50.533 5.944   -22.137 1.00 43.27 ? 504  VAL A CA    1 
ATOM   4111 C  C     . VAL A 1 514 ? -50.960 7.030   -23.134 1.00 43.61 ? 504  VAL A C     1 
ATOM   4112 O  O     . VAL A 1 514 ? -51.568 8.021   -22.736 1.00 43.81 ? 504  VAL A O     1 
ATOM   4113 C  CB    . VAL A 1 514 ? -49.288 6.436   -21.351 1.00 42.62 ? 504  VAL A CB    1 
ATOM   4114 C  CG1   . VAL A 1 514 ? -48.953 5.469   -20.220 1.00 42.33 ? 504  VAL A CG1   1 
ATOM   4115 C  CG2   . VAL A 1 514 ? -48.085 6.660   -22.267 1.00 41.94 ? 504  VAL A CG2   1 
ATOM   4116 N  N     . LEU A 1 515 ? -50.635 6.853   -24.415 1.00 43.42 ? 505  LEU A N     1 
ATOM   4117 C  CA    . LEU A 1 515 ? -50.936 7.861   -25.433 1.00 44.49 ? 505  LEU A CA    1 
ATOM   4118 C  C     . LEU A 1 515 ? -52.372 7.696   -25.918 1.00 46.35 ? 505  LEU A C     1 
ATOM   4119 O  O     . LEU A 1 515 ? -52.634 7.105   -26.969 1.00 45.89 ? 505  LEU A O     1 
ATOM   4120 C  CB    . LEU A 1 515 ? -49.946 7.784   -26.600 1.00 44.35 ? 505  LEU A CB    1 
ATOM   4121 C  CG    . LEU A 1 515 ? -48.469 7.920   -26.214 1.00 44.31 ? 505  LEU A CG    1 
ATOM   4122 C  CD1   . LEU A 1 515 ? -47.595 7.618   -27.422 1.00 44.02 ? 505  LEU A CD1   1 
ATOM   4123 C  CD2   . LEU A 1 515 ? -48.141 9.299   -25.661 1.00 44.27 ? 505  LEU A CD2   1 
ATOM   4124 N  N     . ASN A 1 516 ? -53.295 8.235   -25.134 1.00 47.34 ? 506  ASN A N     1 
ATOM   4125 C  CA    . ASN A 1 516 ? -54.729 8.077   -25.407 1.00 48.62 ? 506  ASN A CA    1 
ATOM   4126 C  C     . ASN A 1 516 ? -55.349 9.297   -26.115 1.00 51.38 ? 506  ASN A C     1 
ATOM   4127 O  O     . ASN A 1 516 ? -56.556 9.335   -26.345 1.00 51.46 ? 506  ASN A O     1 
ATOM   4128 C  CB    . ASN A 1 516 ? -55.476 7.700   -24.118 1.00 45.31 ? 506  ASN A CB    1 
ATOM   4129 C  CG    . ASN A 1 516 ? -55.284 8.699   -23.024 1.00 45.06 ? 506  ASN A CG    1 
ATOM   4130 O  OD1   . ASN A 1 516 ? -55.107 9.895   -23.285 1.00 45.44 ? 506  ASN A OD1   1 
ATOM   4131 N  ND2   . ASN A 1 516 ? -55.328 8.233   -21.770 1.00 46.35 ? 506  ASN A ND2   1 
ATOM   4132 N  N     . GLU A 1 517 ? -54.515 10.280  -26.445 1.00 54.77 ? 507  GLU A N     1 
ATOM   4133 C  CA    . GLU A 1 517 ? -54.862 11.349  -27.378 1.00 58.43 ? 507  GLU A CA    1 
ATOM   4134 C  C     . GLU A 1 517 ? -53.972 11.230  -28.618 1.00 58.12 ? 507  GLU A C     1 
ATOM   4135 O  O     . GLU A 1 517 ? -52.899 10.623  -28.564 1.00 56.56 ? 507  GLU A O     1 
ATOM   4136 C  CB    . GLU A 1 517 ? -54.657 12.709  -26.716 1.00 62.05 ? 507  GLU A CB    1 
ATOM   4137 C  CG    . GLU A 1 517 ? -55.535 12.948  -25.491 1.00 65.55 ? 507  GLU A CG    1 
ATOM   4138 C  CD    . GLU A 1 517 ? -55.017 14.066  -24.598 1.00 68.51 ? 507  GLU A CD    1 
ATOM   4139 O  OE1   . GLU A 1 517 ? -55.150 13.950  -23.358 1.00 70.97 ? 507  GLU A OE1   1 
ATOM   4140 O  OE2   . GLU A 1 517 ? -54.469 15.058  -25.129 1.00 70.67 ? 507  GLU A OE2   1 
ATOM   4141 N  N     . SER A 1 518 ? -54.426 11.801  -29.732 1.00 57.48 ? 508  SER A N     1 
ATOM   4142 C  CA    . SER A 1 518 ? -53.634 11.836  -30.959 1.00 57.03 ? 508  SER A CA    1 
ATOM   4143 C  C     . SER A 1 518 ? -52.469 12.814  -30.816 1.00 56.48 ? 508  SER A C     1 
ATOM   4144 O  O     . SER A 1 518 ? -52.571 13.808  -30.097 1.00 55.08 ? 508  SER A O     1 
ATOM   4145 C  CB    . SER A 1 518 ? -54.504 12.220  -32.161 1.00 57.67 ? 508  SER A CB    1 
ATOM   4146 O  OG    . SER A 1 518 ? -54.883 13.583  -32.112 1.00 57.86 ? 508  SER A OG    1 
ATOM   4147 N  N     . ILE A 1 519 ? -51.359 12.514  -31.490 1.00 55.40 ? 509  ILE A N     1 
ATOM   4148 C  CA    . ILE A 1 519 ? -50.186 13.398  -31.501 1.00 54.63 ? 509  ILE A CA    1 
ATOM   4149 C  C     . ILE A 1 519 ? -49.623 13.537  -32.910 1.00 52.91 ? 509  ILE A C     1 
ATOM   4150 O  O     . ILE A 1 519 ? -49.672 12.599  -33.703 1.00 50.40 ? 509  ILE A O     1 
ATOM   4151 C  CB    . ILE A 1 519 ? -49.072 12.930  -30.524 1.00 55.19 ? 509  ILE A CB    1 
ATOM   4152 C  CG1   . ILE A 1 519 ? -48.757 11.441  -30.706 1.00 55.55 ? 509  ILE A CG1   1 
ATOM   4153 C  CG2   . ILE A 1 519 ? -49.485 13.222  -29.087 1.00 55.97 ? 509  ILE A CG2   1 
ATOM   4154 C  CD1   . ILE A 1 519 ? -47.600 10.935  -29.865 1.00 55.91 ? 509  ILE A CD1   1 
ATOM   4155 N  N     . MET A 1 520 ? -49.101 14.725  -33.200 1.00 52.08 ? 510  MET A N     1 
ATOM   4156 C  CA    . MET A 1 520 ? -48.458 15.012  -34.471 1.00 52.70 ? 510  MET A CA    1 
ATOM   4157 C  C     . MET A 1 520 ? -46.976 14.684  -34.348 1.00 50.30 ? 510  MET A C     1 
ATOM   4158 O  O     . MET A 1 520 ? -46.224 15.430  -33.721 1.00 48.25 ? 510  MET A O     1 
ATOM   4159 C  CB    . MET A 1 520 ? -48.634 16.487  -34.854 1.00 54.68 ? 510  MET A CB    1 
ATOM   4160 C  CG    . MET A 1 520 ? -50.053 16.878  -35.257 1.00 56.70 ? 510  MET A CG    1 
ATOM   4161 S  SD    . MET A 1 520 ? -50.656 16.093  -36.771 1.00 59.35 ? 510  MET A SD    1 
ATOM   4162 C  CE    . MET A 1 520 ? -49.501 16.721  -37.989 1.00 58.34 ? 510  MET A CE    1 
ATOM   4163 N  N     . VAL A 1 521 ? -46.566 13.568  -34.948 1.00 48.86 ? 511  VAL A N     1 
ATOM   4164 C  CA    . VAL A 1 521 ? -45.141 13.202  -35.008 1.00 47.63 ? 511  VAL A CA    1 
ATOM   4165 C  C     . VAL A 1 521 ? -44.407 14.154  -35.953 1.00 46.81 ? 511  VAL A C     1 
ATOM   4166 O  O     . VAL A 1 521 ? -45.037 14.918  -36.689 1.00 46.71 ? 511  VAL A O     1 
ATOM   4167 C  CB    . VAL A 1 521 ? -44.899 11.726  -35.434 1.00 47.66 ? 511  VAL A CB    1 
ATOM   4168 C  CG1   . VAL A 1 521 ? -45.600 10.758  -34.488 1.00 46.94 ? 511  VAL A CG1   1 
ATOM   4169 C  CG2   . VAL A 1 521 ? -45.313 11.459  -36.882 1.00 47.95 ? 511  VAL A CG2   1 
ATOM   4170 N  N     . THR A 1 522 ? -43.078 14.108  -35.934 1.00 45.32 ? 512  THR A N     1 
ATOM   4171 C  CA    . THR A 1 522 ? -42.288 14.960  -36.829 1.00 45.74 ? 512  THR A CA    1 
ATOM   4172 C  C     . THR A 1 522 ? -42.589 14.639  -38.296 1.00 46.42 ? 512  THR A C     1 
ATOM   4173 O  O     . THR A 1 522 ? -42.836 13.484  -38.651 1.00 43.87 ? 512  THR A O     1 
ATOM   4174 C  CB    . THR A 1 522 ? -40.762 14.866  -36.598 1.00 45.18 ? 512  THR A CB    1 
ATOM   4175 O  OG1   . THR A 1 522 ? -40.099 15.804  -37.457 1.00 44.74 ? 512  THR A OG1   1 
ATOM   4176 C  CG2   . THR A 1 522 ? -40.211 13.451  -36.880 1.00 44.32 ? 512  THR A CG2   1 
ATOM   4177 N  N     . GLY A 1 523 ? -42.581 15.681  -39.120 1.00 48.47 ? 513  GLY A N     1 
ATOM   4178 C  CA    . GLY A 1 523 ? -42.726 15.549  -40.571 1.00 50.46 ? 513  GLY A CA    1 
ATOM   4179 C  C     . GLY A 1 523 ? -41.400 15.329  -41.284 1.00 51.47 ? 513  GLY A C     1 
ATOM   4180 O  O     . GLY A 1 523 ? -41.382 14.931  -42.451 1.00 51.12 ? 513  GLY A O     1 
ATOM   4181 N  N     . GLN A 1 524 ? -40.295 15.606  -40.590 1.00 52.11 ? 514  GLN A N     1 
ATOM   4182 C  CA    . GLN A 1 524 ? -38.950 15.470  -41.142 1.00 53.33 ? 514  GLN A CA    1 
ATOM   4183 C  C     . GLN A 1 524 ? -38.116 14.572  -40.222 1.00 51.34 ? 514  GLN A C     1 
ATOM   4184 O  O     . GLN A 1 524 ? -37.220 15.052  -39.521 1.00 49.18 ? 514  GLN A O     1 
ATOM   4185 C  CB    . GLN A 1 524 ? -38.291 16.849  -41.318 1.00 56.27 ? 514  GLN A CB    1 
ATOM   4186 C  CG    . GLN A 1 524 ? -38.870 17.693  -42.452 1.00 59.06 ? 514  GLN A CG    1 
ATOM   4187 C  CD    . GLN A 1 524 ? -40.226 18.317  -42.134 1.00 61.44 ? 514  GLN A CD    1 
ATOM   4188 O  OE1   . GLN A 1 524 ? -40.526 18.653  -40.985 1.00 63.03 ? 514  GLN A OE1   1 
ATOM   4189 N  NE2   . GLN A 1 524 ? -41.054 18.477  -43.163 1.00 63.42 ? 514  GLN A NE2   1 
ATOM   4190 N  N     . PRO A 1 525 ? -38.410 13.256  -40.220 1.00 50.13 ? 515  PRO A N     1 
ATOM   4191 C  CA    . PRO A 1 525 ? -37.604 12.358  -39.391 1.00 49.35 ? 515  PRO A CA    1 
ATOM   4192 C  C     . PRO A 1 525 ? -36.156 12.303  -39.875 1.00 47.90 ? 515  PRO A C     1 
ATOM   4193 O  O     . PRO A 1 525 ? -35.880 12.523  -41.056 1.00 47.65 ? 515  PRO A O     1 
ATOM   4194 C  CB    . PRO A 1 525 ? -38.293 11.001  -39.558 1.00 49.67 ? 515  PRO A CB    1 
ATOM   4195 C  CG    . PRO A 1 525 ? -38.995 11.088  -40.870 1.00 50.58 ? 515  PRO A CG    1 
ATOM   4196 C  CD    . PRO A 1 525 ? -39.411 12.521  -41.015 1.00 50.65 ? 515  PRO A CD    1 
ATOM   4197 N  N     . LYS A 1 526 ? -35.249 12.037  -38.949 1.00 45.29 ? 516  LYS A N     1 
ATOM   4198 C  CA    . LYS A 1 526 ? -33.836 11.939  -39.258 1.00 44.03 ? 516  LYS A CA    1 
ATOM   4199 C  C     . LYS A 1 526 ? -33.216 10.814  -38.425 1.00 40.35 ? 516  LYS A C     1 
ATOM   4200 O  O     . LYS A 1 526 ? -33.824 10.361  -37.456 1.00 37.42 ? 516  LYS A O     1 
ATOM   4201 C  CB    . LYS A 1 526 ? -33.151 13.283  -39.004 1.00 46.66 ? 516  LYS A CB    1 
ATOM   4202 C  CG    . LYS A 1 526 ? -33.335 13.839  -37.602 1.00 48.81 ? 516  LYS A CG    1 
ATOM   4203 C  CD    . LYS A 1 526 ? -32.496 15.092  -37.392 1.00 50.89 ? 516  LYS A CD    1 
ATOM   4204 C  CE    . LYS A 1 526 ? -32.372 15.434  -35.915 1.00 51.82 ? 516  LYS A CE    1 
ATOM   4205 N  NZ    . LYS A 1 526 ? -31.314 16.454  -35.688 1.00 53.60 ? 516  LYS A NZ    1 
ATOM   4206 N  N     . PRO A 1 527 ? -32.011 10.350  -38.802 1.00 37.89 ? 517  PRO A N     1 
ATOM   4207 C  CA    . PRO A 1 527 ? -31.451 9.209   -38.082 1.00 37.09 ? 517  PRO A CA    1 
ATOM   4208 C  C     . PRO A 1 527 ? -31.203 9.475   -36.595 1.00 35.62 ? 517  PRO A C     1 
ATOM   4209 O  O     . PRO A 1 527 ? -30.655 10.512  -36.237 1.00 33.45 ? 517  PRO A O     1 
ATOM   4210 C  CB    . PRO A 1 527 ? -30.119 8.956   -38.803 1.00 37.90 ? 517  PRO A CB    1 
ATOM   4211 C  CG    . PRO A 1 527 ? -30.337 9.501   -40.173 1.00 38.71 ? 517  PRO A CG    1 
ATOM   4212 C  CD    . PRO A 1 527 ? -31.165 10.728  -39.950 1.00 38.56 ? 517  PRO A CD    1 
ATOM   4213 N  N     . ILE A 1 528 ? -31.607 8.517   -35.764 1.00 35.06 ? 518  ILE A N     1 
ATOM   4214 C  CA    . ILE A 1 528 ? -31.394 8.567   -34.311 1.00 34.87 ? 518  ILE A CA    1 
ATOM   4215 C  C     . ILE A 1 528 ? -29.894 8.481   -33.994 1.00 34.87 ? 518  ILE A C     1 
ATOM   4216 O  O     . ILE A 1 528 ? -29.425 9.104   -33.042 1.00 34.05 ? 518  ILE A O     1 
ATOM   4217 C  CB    . ILE A 1 528 ? -32.168 7.426   -33.586 1.00 34.99 ? 518  ILE A CB    1 
ATOM   4218 C  CG1   . ILE A 1 528 ? -33.679 7.484   -33.892 1.00 35.36 ? 518  ILE A CG1   1 
ATOM   4219 C  CG2   . ILE A 1 528 ? -31.964 7.460   -32.073 1.00 35.19 ? 518  ILE A CG2   1 
ATOM   4220 C  CD1   . ILE A 1 528 ? -34.370 8.792   -33.555 1.00 35.83 ? 518  ILE A CD1   1 
ATOM   4221 N  N     . PHE A 1 529 ? -29.164 7.703   -34.791 1.00 34.68 ? 519  PHE A N     1 
ATOM   4222 C  CA    . PHE A 1 529 ? -27.731 7.485   -34.607 1.00 35.75 ? 519  PHE A CA    1 
ATOM   4223 C  C     . PHE A 1 529 ? -26.950 7.992   -35.843 1.00 39.27 ? 519  PHE A C     1 
ATOM   4224 O  O     . PHE A 1 529 ? -27.503 8.007   -36.941 1.00 40.49 ? 519  PHE A O     1 
ATOM   4225 C  CB    . PHE A 1 529 ? -27.487 5.995   -34.347 1.00 33.78 ? 519  PHE A CB    1 
ATOM   4226 C  CG    . PHE A 1 529 ? -28.195 5.482   -33.116 1.00 32.22 ? 519  PHE A CG    1 
ATOM   4227 C  CD1   . PHE A 1 529 ? -29.367 4.747   -33.220 1.00 31.53 ? 519  PHE A CD1   1 
ATOM   4228 C  CD2   . PHE A 1 529 ? -27.699 5.771   -31.844 1.00 31.27 ? 519  PHE A CD2   1 
ATOM   4229 C  CE1   . PHE A 1 529 ? -30.019 4.282   -32.088 1.00 31.30 ? 519  PHE A CE1   1 
ATOM   4230 C  CE2   . PHE A 1 529 ? -28.347 5.309   -30.706 1.00 30.65 ? 519  PHE A CE2   1 
ATOM   4231 C  CZ    . PHE A 1 529 ? -29.509 4.567   -30.827 1.00 30.61 ? 519  PHE A CZ    1 
ATOM   4232 N  N     . PRO A 1 530 ? -25.682 8.402   -35.698 1.00 44.59 ? 520  PRO A N     1 
ATOM   4233 C  CA    . PRO A 1 530 ? -24.892 8.334   -34.455 1.00 45.75 ? 520  PRO A CA    1 
ATOM   4234 C  C     . PRO A 1 530 ? -25.131 9.503   -33.500 1.00 46.77 ? 520  PRO A C     1 
ATOM   4235 O  O     . PRO A 1 530 ? -26.122 10.222  -33.642 1.00 49.52 ? 520  PRO A O     1 
ATOM   4236 C  CB    . PRO A 1 530 ? -23.447 8.364   -34.971 1.00 46.58 ? 520  PRO A CB    1 
ATOM   4237 C  CG    . PRO A 1 530 ? -23.523 9.117   -36.263 1.00 46.73 ? 520  PRO A CG    1 
ATOM   4238 C  CD    . PRO A 1 530 ? -24.859 8.796   -36.860 1.00 46.72 ? 520  PRO A CD    1 
HETATM 4239 P  PG    A ATP B 2 .   ? -4.756  3.520   -9.627  0.42 33.18 ? 601  ATP A PG    1 
HETATM 4240 P  PG    B ATP B 2 .   ? -1.176  1.762   -14.581 0.58 32.72 ? 601  ATP A PG    1 
HETATM 4241 O  O1G   A ATP B 2 .   ? -5.366  2.296   -8.983  0.42 33.90 ? 601  ATP A O1G   1 
HETATM 4242 O  O1G   B ATP B 2 .   ? -0.615  3.069   -14.079 0.58 32.82 ? 601  ATP A O1G   1 
HETATM 4243 O  O2G   A ATP B 2 .   ? -3.346  3.820   -9.167  0.42 33.01 ? 601  ATP A O2G   1 
HETATM 4244 O  O2G   B ATP B 2 .   ? -0.835  0.574   -13.714 0.58 31.79 ? 601  ATP A O2G   1 
HETATM 4245 O  O3G   A ATP B 2 .   ? -5.682  4.708   -9.674  0.42 34.22 ? 601  ATP A O3G   1 
HETATM 4246 O  O3G   B ATP B 2 .   ? -0.979  1.566   -16.063 0.58 32.82 ? 601  ATP A O3G   1 
HETATM 4247 P  PB    A ATP B 2 .   ? -5.763  3.715   -12.183 0.42 29.37 ? 601  ATP A PB    1 
HETATM 4248 P  PB    B ATP B 2 .   ? -3.836  0.984   -15.137 0.58 30.43 ? 601  ATP A PB    1 
HETATM 4249 O  O1B   A ATP B 2 .   ? -7.117  3.221   -11.728 0.42 29.43 ? 601  ATP A O1B   1 
HETATM 4250 O  O1B   B ATP B 2 .   ? -4.450  1.690   -16.321 0.58 29.11 ? 601  ATP A O1B   1 
HETATM 4251 O  O2B   A ATP B 2 .   ? -5.553  5.192   -12.373 0.42 27.67 ? 601  ATP A O2B   1 
HETATM 4252 O  O2B   B ATP B 2 .   ? -3.202  -0.364  -15.379 0.58 30.48 ? 601  ATP A O2B   1 
HETATM 4253 O  O3B   A ATP B 2 .   ? -4.633  3.157   -11.184 0.42 31.57 ? 601  ATP A O3B   1 
HETATM 4254 O  O3B   B ATP B 2 .   ? -2.768  1.960   -14.427 0.58 31.64 ? 601  ATP A O3B   1 
HETATM 4255 P  PA    A ATP B 2 .   ? -5.472  1.313   -13.537 0.42 32.52 ? 601  ATP A PA    1 
HETATM 4256 P  PA    B ATP B 2 .   ? -5.304  1.895   -12.835 0.58 29.19 ? 601  ATP A PA    1 
HETATM 4257 O  O1A   A ATP B 2 .   ? -4.484  0.788   -12.518 0.42 33.04 ? 601  ATP A O1A   1 
HETATM 4258 O  O1A   B ATP B 2 .   ? -5.371  3.262   -13.474 0.58 29.15 ? 601  ATP A O1A   1 
HETATM 4259 O  O2A   A ATP B 2 .   ? -5.396  0.840   -14.968 0.42 32.61 ? 601  ATP A O2A   1 
HETATM 4260 O  O2A   B ATP B 2 .   ? -4.451  1.664   -11.608 0.58 27.98 ? 601  ATP A O2A   1 
HETATM 4261 O  O3A   A ATP B 2 .   ? -5.406  2.925   -13.536 0.42 31.16 ? 601  ATP A O3A   1 
HETATM 4262 O  O3A   B ATP B 2 .   ? -4.931  0.784   -13.962 0.58 29.40 ? 601  ATP A O3A   1 
HETATM 4263 O  "O5'" A ATP B 2 .   ? -6.957  1.017   -12.979 0.42 30.16 ? 601  ATP A "O5'" 1 
HETATM 4264 O  "O5'" B ATP B 2 .   ? -6.804  1.429   -12.475 0.58 26.39 ? 601  ATP A "O5'" 1 
HETATM 4265 C  "C5'" A ATP B 2 .   ? -7.404  1.566   -11.738 0.42 27.70 ? 601  ATP A "C5'" 1 
HETATM 4266 C  "C5'" B ATP B 2 .   ? -7.598  2.097   -11.499 0.58 23.64 ? 601  ATP A "C5'" 1 
HETATM 4267 C  "C4'" A ATP B 2 .   ? -8.923  1.666   -11.744 0.42 26.27 ? 601  ATP A "C4'" 1 
HETATM 4268 C  "C4'" B ATP B 2 .   ? -9.083  1.896   -11.798 0.58 22.03 ? 601  ATP A "C4'" 1 
HETATM 4269 O  "O4'" A ATP B 2 .   ? -9.362  2.247   -12.978 0.42 25.49 ? 601  ATP A "O4'" 1 
HETATM 4270 O  "O4'" B ATP B 2 .   ? -9.414  2.295   -13.140 0.58 21.08 ? 601  ATP A "O4'" 1 
HETATM 4271 C  "C3'" A ATP B 2 .   ? -9.595  0.304   -11.629 0.42 25.76 ? 601  ATP A "C3'" 1 
HETATM 4272 C  "C3'" B ATP B 2 .   ? -9.547  0.450   -11.688 0.58 21.49 ? 601  ATP A "C3'" 1 
HETATM 4273 O  "O3'" A ATP B 2 .   ? -10.013 -0.018  -10.301 0.42 25.72 ? 601  ATP A "O3'" 1 
HETATM 4274 O  "O3'" B ATP B 2 .   ? -9.852  0.003   -10.365 0.58 21.11 ? 601  ATP A "O3'" 1 
HETATM 4275 C  "C2'" A ATP B 2 .   ? -10.769 0.429   -12.569 0.42 25.45 ? 601  ATP A "C2'" 1 
HETATM 4276 C  "C2'" B ATP B 2 .   ? -10.759 0.484   -12.584 0.58 21.13 ? 601  ATP A "C2'" 1 
HETATM 4277 O  "O2'" A ATP B 2 .   ? -11.879 1.007   -11.875 0.42 25.16 ? 601  ATP A "O2'" 1 
HETATM 4278 O  "O2'" B ATP B 2 .   ? -11.852 1.124   -11.914 0.58 20.37 ? 601  ATP A "O2'" 1 
HETATM 4279 C  "C1'" A ATP B 2 .   ? -10.267 1.368   -13.639 0.42 25.31 ? 601  ATP A "C1'" 1 
HETATM 4280 C  "C1'" B ATP B 2 .   ? -10.303 1.350   -13.742 0.58 21.11 ? 601  ATP A "C1'" 1 
HETATM 4281 N  N9    A ATP B 2 .   ? -9.513  0.614   -14.667 0.42 25.46 ? 601  ATP A N9    1 
HETATM 4282 N  N9    B ATP B 2 .   ? -9.570  0.570   -14.782 0.58 21.42 ? 601  ATP A N9    1 
HETATM 4283 C  C8    A ATP B 2 .   ? -8.242  0.874   -15.021 0.42 25.34 ? 601  ATP A C8    1 
HETATM 4284 C  C8    B ATP B 2 .   ? -8.310  0.822   -15.198 0.58 21.39 ? 601  ATP A C8    1 
HETATM 4285 N  N7    A ATP B 2 .   ? -7.825  0.011   -15.983 0.42 25.46 ? 601  ATP A N7    1 
HETATM 4286 N  N7    B ATP B 2 .   ? -7.917  -0.056  -16.149 0.58 21.60 ? 601  ATP A N7    1 
HETATM 4287 C  C5    A ATP B 2 .   ? -8.848  -0.819  -16.253 0.42 25.26 ? 601  ATP A C5    1 
HETATM 4288 C  C5    B ATP B 2 .   ? -8.941  -0.892  -16.367 0.58 21.34 ? 601  ATP A C5    1 
HETATM 4289 C  C6    A ATP B 2 .   ? -9.082  -1.957  -17.165 0.42 25.36 ? 601  ATP A C6    1 
HETATM 4290 C  C6    B ATP B 2 .   ? -9.191  -2.051  -17.252 0.58 21.67 ? 601  ATP A C6    1 
HETATM 4291 N  N6    A ATP B 2 .   ? -8.110  -2.388  -18.007 0.42 25.97 ? 601  ATP A N6    1 
HETATM 4292 N  N6    B ATP B 2 .   ? -8.236  -2.483  -18.112 0.58 22.41 ? 601  ATP A N6    1 
HETATM 4293 N  N1    A ATP B 2 .   ? -10.295 -2.545  -17.136 0.42 25.45 ? 601  ATP A N1    1 
HETATM 4294 N  N1    B ATP B 2 .   ? -10.404 -2.647  -17.180 0.58 21.76 ? 601  ATP A N1    1 
HETATM 4295 C  C2    A ATP B 2 .   ? -11.274 -2.132  -16.307 0.42 25.16 ? 601  ATP A C2    1 
HETATM 4296 C  C2    B ATP B 2 .   ? -11.366 -2.226  -16.324 0.58 21.36 ? 601  ATP A C2    1 
HETATM 4297 N  N3    A ATP B 2 .   ? -11.120 -1.104  -15.455 0.42 25.07 ? 601  ATP A N3    1 
HETATM 4298 N  N3    B ATP B 2 .   ? -11.192 -1.176  -15.495 0.58 21.17 ? 601  ATP A N3    1 
HETATM 4299 C  C4    A ATP B 2 .   ? -9.956  -0.421  -15.378 0.42 25.02 ? 601  ATP A C4    1 
HETATM 4300 C  C4    B ATP B 2 .   ? -10.027 -0.480  -15.463 0.58 21.15 ? 601  ATP A C4    1 
HETATM 4301 CL CL2   . XC9 C 3 .   ? 2.245   9.761   -1.146  1.00 24.35 ? 602  XC9 A CL2   1 
HETATM 4302 C  C10   . XC9 C 3 .   ? 0.825   1.198   -3.484  1.00 38.94 ? 602  XC9 A C10   1 
HETATM 4303 C  C11   . XC9 C 3 .   ? 0.529   2.141   -4.655  1.00 37.30 ? 602  XC9 A C11   1 
HETATM 4304 C  C12   . XC9 C 3 .   ? 1.668   2.966   -5.234  1.00 35.14 ? 602  XC9 A C12   1 
HETATM 4305 N  N6    . XC9 C 3 .   ? 1.300   3.385   -6.579  1.00 33.43 ? 602  XC9 A N6    1 
HETATM 4306 C  C13   . XC9 C 3 .   ? 0.368   4.291   -6.868  1.00 31.04 ? 602  XC9 A C13   1 
HETATM 4307 N  N7    . XC9 C 3 .   ? -0.017  4.438   -8.091  1.00 32.46 ? 602  XC9 A N7    1 
HETATM 4308 N  N8    . XC9 C 3 .   ? -0.068  5.147   -5.881  1.00 28.42 ? 602  XC9 A N8    1 
HETATM 4309 C  C14   . XC9 C 3 .   ? -1.150  5.995   -5.931  1.00 25.85 ? 602  XC9 A C14   1 
HETATM 4310 N  N9    . XC9 C 3 .   ? -2.111  5.725   -6.744  1.00 26.90 ? 602  XC9 A N9    1 
HETATM 4311 N  N10   . XC9 C 3 .   ? -1.285  6.985   -4.984  1.00 24.74 ? 602  XC9 A N10   1 
HETATM 4312 C  C15   . XC9 C 3 .   ? -0.402  7.568   -4.048  1.00 22.98 ? 602  XC9 A C15   1 
HETATM 4313 C  C16   . XC9 C 3 .   ? 0.971   7.325   -4.023  1.00 22.94 ? 602  XC9 A C16   1 
HETATM 4314 C  C17   . XC9 C 3 .   ? 1.785   7.997   -3.129  1.00 22.66 ? 602  XC9 A C17   1 
HETATM 4315 C  C18   . XC9 C 3 .   ? 1.224   8.911   -2.264  1.00 22.73 ? 602  XC9 A C18   1 
HETATM 4316 C  C19   . XC9 C 3 .   ? -0.130  9.169   -2.270  1.00 22.76 ? 602  XC9 A C19   1 
HETATM 4317 C  C20   . XC9 C 3 .   ? -0.942  8.496   -3.164  1.00 22.58 ? 602  XC9 A C20   1 
HETATM 4318 C  C1    . XC9 C 3 .   ? 1.047   -0.290  -3.789  1.00 40.55 ? 602  XC9 A C1    1 
HETATM 4319 C  C2    . XC9 C 3 .   ? 0.275   -0.884  -4.960  1.00 41.47 ? 602  XC9 A C2    1 
HETATM 4320 C  C3    . XC9 C 3 .   ? -0.806  -1.909  -4.652  1.00 41.78 ? 602  XC9 A C3    1 
HETATM 4321 N  N1    . XC9 C 3 .   ? -1.369  -2.399  -5.904  1.00 41.96 ? 602  XC9 A N1    1 
HETATM 4322 C  C4    . XC9 C 3 .   ? -2.028  -1.651  -6.792  1.00 43.05 ? 602  XC9 A C4    1 
HETATM 4323 N  N2    . XC9 C 3 .   ? -2.505  -0.412  -6.405  1.00 41.49 ? 602  XC9 A N2    1 
HETATM 4324 C  C5    . XC9 C 3 .   ? -3.011  0.588   -7.211  1.00 41.70 ? 602  XC9 A C5    1 
HETATM 4325 N  N3    . XC9 C 3 .   ? -3.623  1.674   -6.620  1.00 40.85 ? 602  XC9 A N3    1 
HETATM 4326 C  C6    . XC9 C 3 .   ? -4.127  1.853   -5.311  1.00 39.05 ? 602  XC9 A C6    1 
HETATM 4327 C  C7    . XC9 C 3 .   ? -5.437  2.313   -5.250  1.00 40.80 ? 602  XC9 A C7    1 
HETATM 4328 C  C8    . XC9 C 3 .   ? -6.063  2.484   -4.028  1.00 40.78 ? 602  XC9 A C8    1 
HETATM 4329 C  C9    . XC9 C 3 .   ? -5.374  2.203   -2.873  1.00 38.54 ? 602  XC9 A C9    1 
HETATM 4330 C  C21   . XC9 C 3 .   ? -4.078  1.743   -2.906  1.00 37.84 ? 602  XC9 A C21   1 
HETATM 4331 C  C22   . XC9 C 3 .   ? -3.451  1.570   -4.128  1.00 39.19 ? 602  XC9 A C22   1 
HETATM 4332 CL CL1   . XC9 C 3 .   ? -6.092  2.609   -1.343  1.00 37.24 ? 602  XC9 A CL1   1 
HETATM 4333 N  N4    . XC9 C 3 .   ? -2.284  -2.146  -7.952  1.00 44.78 ? 602  XC9 A N4    1 
HETATM 4334 N  N5    . XC9 C 3 .   ? -2.827  0.562   -8.484  1.00 43.39 ? 602  XC9 A N5    1 
HETATM 4335 C  C1    . EDO D 4 .   ? -9.515  5.349   -3.835  1.00 26.87 ? 603  EDO A C1    1 
HETATM 4336 O  O1    . EDO D 4 .   ? -10.520 5.731   -4.767  1.00 24.73 ? 603  EDO A O1    1 
HETATM 4337 C  C2    . EDO D 4 .   ? -8.341  4.866   -4.661  1.00 28.67 ? 603  EDO A C2    1 
HETATM 4338 O  O2    . EDO D 4 .   ? -8.666  3.627   -5.325  1.00 30.00 ? 603  EDO A O2    1 
HETATM 4339 C  C1    . EDO E 4 .   ? 8.250   -3.400  7.754   1.00 34.35 ? 604  EDO A C1    1 
HETATM 4340 O  O1    . EDO E 4 .   ? 7.970   -2.645  6.567   1.00 31.45 ? 604  EDO A O1    1 
HETATM 4341 C  C2    . EDO E 4 .   ? 8.142   -4.888  7.439   1.00 35.16 ? 604  EDO A C2    1 
HETATM 4342 O  O2    . EDO E 4 .   ? 9.075   -5.263  6.415   1.00 36.87 ? 604  EDO A O2    1 
HETATM 4343 C  C1    . EDO F 4 .   ? -7.993  11.697  -20.327 1.00 25.00 ? 605  EDO A C1    1 
HETATM 4344 O  O1    . EDO F 4 .   ? -6.757  11.389  -19.691 1.00 22.96 ? 605  EDO A O1    1 
HETATM 4345 C  C2    . EDO F 4 .   ? -7.769  12.421  -21.644 1.00 25.95 ? 605  EDO A C2    1 
HETATM 4346 O  O2    . EDO F 4 .   ? -6.849  11.707  -22.480 1.00 26.79 ? 605  EDO A O2    1 
HETATM 4347 C  C1    . EDO G 4 .   ? -36.397 6.468   -3.170  1.00 45.95 ? 606  EDO A C1    1 
HETATM 4348 O  O1    . EDO G 4 .   ? -36.692 7.490   -2.210  1.00 43.94 ? 606  EDO A O1    1 
HETATM 4349 C  C2    . EDO G 4 .   ? -36.854 5.113   -2.641  1.00 46.69 ? 606  EDO A C2    1 
HETATM 4350 O  O2    . EDO G 4 .   ? -38.264 4.912   -2.817  1.00 48.72 ? 606  EDO A O2    1 
HETATM 4351 O  O     . HOH H 5 .   ? -29.603 7.851   3.667   1.00 14.36 ? 701  HOH A O     1 
HETATM 4352 O  O     . HOH H 5 .   ? -40.422 14.210  2.407   1.00 26.89 ? 702  HOH A O     1 
HETATM 4353 O  O     . HOH H 5 .   ? -5.572  5.809   -7.482  1.00 29.65 ? 703  HOH A O     1 
HETATM 4354 O  O     . HOH H 5 .   ? -25.022 8.579   -24.488 1.00 27.79 ? 704  HOH A O     1 
HETATM 4355 O  O     . HOH H 5 .   ? 15.650  3.872   7.747   1.00 41.90 ? 705  HOH A O     1 
HETATM 4356 O  O     . HOH H 5 .   ? -24.312 -8.521  -17.060 1.00 27.84 ? 706  HOH A O     1 
HETATM 4357 O  O     . HOH H 5 .   ? 9.521   12.126  -5.915  1.00 30.18 ? 707  HOH A O     1 
HETATM 4358 O  O     . HOH H 5 .   ? -38.946 13.365  -17.485 1.00 40.15 ? 708  HOH A O     1 
HETATM 4359 O  O     . HOH H 5 .   ? 11.643  13.325  4.780   1.00 36.64 ? 709  HOH A O     1 
HETATM 4360 O  O     . HOH H 5 .   ? -22.914 0.836   7.389   1.00 27.31 ? 710  HOH A O     1 
HETATM 4361 O  O     . HOH H 5 .   ? 10.118  17.820  -9.288  1.00 29.85 ? 711  HOH A O     1 
HETATM 4362 O  O     . HOH H 5 .   ? -33.041 -8.474  -18.098 1.00 31.55 ? 712  HOH A O     1 
HETATM 4363 O  O     . HOH H 5 .   ? -27.880 3.965   2.245   1.00 23.19 ? 713  HOH A O     1 
HETATM 4364 O  O     . HOH H 5 .   ? -19.782 -10.285 1.508   1.00 45.84 ? 714  HOH A O     1 
HETATM 4365 O  O     . HOH H 5 .   ? -32.110 4.416   2.634   1.00 34.52 ? 715  HOH A O     1 
HETATM 4366 O  O     . HOH H 5 .   ? 5.750   10.175  16.458  1.00 36.62 ? 716  HOH A O     1 
HETATM 4367 O  O     . HOH H 5 .   ? -3.009  11.454  -3.752  1.00 16.19 ? 717  HOH A O     1 
HETATM 4368 O  O     . HOH H 5 .   ? -21.778 -4.435  -18.534 1.00 30.34 ? 718  HOH A O     1 
HETATM 4369 O  O     . HOH H 5 .   ? -4.538  -0.071  15.943  1.00 22.60 ? 719  HOH A O     1 
HETATM 4370 O  O     . HOH H 5 .   ? -38.286 7.304   -13.769 1.00 27.33 ? 720  HOH A O     1 
HETATM 4371 O  O     . HOH H 5 .   ? -14.893 -6.579  -27.758 1.00 34.80 ? 721  HOH A O     1 
HETATM 4372 O  O     . HOH H 5 .   ? 4.474   -4.290  7.669   1.00 30.46 ? 722  HOH A O     1 
HETATM 4373 O  O     . HOH H 5 .   ? -1.194  25.151  -13.153 1.00 39.90 ? 723  HOH A O     1 
HETATM 4374 O  O     . HOH H 5 .   ? -5.171  -0.291  -9.471  1.00 41.47 ? 724  HOH A O     1 
HETATM 4375 O  O     . HOH H 5 .   ? 0.261   18.948  5.513   1.00 37.11 ? 725  HOH A O     1 
HETATM 4376 O  O     . HOH H 5 .   ? 5.618   21.150  -6.263  1.00 22.64 ? 726  HOH A O     1 
HETATM 4377 O  O     . HOH H 5 .   ? -51.954 14.449  -27.602 1.00 54.86 ? 727  HOH A O     1 
HETATM 4378 O  O     . HOH H 5 .   ? -3.801  23.455  0.752   1.00 25.57 ? 728  HOH A O     1 
HETATM 4379 O  O     . HOH H 5 .   ? -12.386 14.834  -24.125 1.00 31.27 ? 729  HOH A O     1 
HETATM 4380 O  O     . HOH H 5 .   ? -5.461  21.855  6.965   1.00 28.85 ? 730  HOH A O     1 
HETATM 4381 O  O     . HOH H 5 .   ? -29.307 10.064  4.859   1.00 24.12 ? 731  HOH A O     1 
HETATM 4382 O  O     . HOH H 5 .   ? -7.590  11.947  -26.195 1.00 40.39 ? 732  HOH A O     1 
HETATM 4383 O  O     . HOH H 5 .   ? -27.644 0.470   -0.600  1.00 27.66 ? 733  HOH A O     1 
HETATM 4384 O  O     . HOH H 5 .   ? -8.414  23.836  5.852   1.00 37.82 ? 734  HOH A O     1 
HETATM 4385 O  O     . HOH H 5 .   ? 3.379   25.804  -10.442 1.00 27.82 ? 735  HOH A O     1 
HETATM 4386 O  O     . HOH H 5 .   ? -2.862  21.688  4.196   1.00 33.25 ? 736  HOH A O     1 
HETATM 4387 O  O     . HOH H 5 .   ? -1.326  -5.478  -18.567 1.00 45.99 ? 737  HOH A O     1 
HETATM 4388 O  O     . HOH H 5 .   ? 1.056   -5.142  15.273  1.00 35.37 ? 738  HOH A O     1 
HETATM 4389 O  O     . HOH H 5 .   ? -12.232 19.529  -8.475  1.00 27.10 ? 739  HOH A O     1 
HETATM 4390 O  O     . HOH H 5 .   ? -37.897 -6.880  -42.044 1.00 29.46 ? 740  HOH A O     1 
HETATM 4391 O  O     . HOH H 5 .   ? -17.883 -5.564  13.646  1.00 32.50 ? 741  HOH A O     1 
HETATM 4392 O  O     . HOH H 5 .   ? 15.082  7.301   11.224  1.00 47.44 ? 742  HOH A O     1 
HETATM 4393 O  O     . HOH H 5 .   ? -1.769  13.827  16.787  1.00 34.26 ? 743  HOH A O     1 
HETATM 4394 O  O     . HOH H 5 .   ? -6.990  18.775  -22.537 1.00 37.78 ? 744  HOH A O     1 
HETATM 4395 O  O     . HOH H 5 .   ? -38.695 9.170   -4.344  1.00 33.73 ? 745  HOH A O     1 
HETATM 4396 O  O     . HOH H 5 .   ? -26.007 5.522   3.674   1.00 22.19 ? 746  HOH A O     1 
HETATM 4397 O  O     . HOH H 5 .   ? -24.301 -4.333  3.319   1.00 36.14 ? 747  HOH A O     1 
HETATM 4398 O  O     . HOH H 5 .   ? -33.534 6.494   -37.235 1.00 38.93 ? 748  HOH A O     1 
HETATM 4399 O  O     . HOH H 5 .   ? -31.573 -10.824 -22.046 1.00 35.43 ? 749  HOH A O     1 
HETATM 4400 O  O     . HOH H 5 .   ? -3.371  25.592  -9.800  1.00 43.80 ? 750  HOH A O     1 
HETATM 4401 O  O     . HOH H 5 .   ? -5.079  -10.332 11.148  1.00 33.70 ? 751  HOH A O     1 
HETATM 4402 O  O     . HOH H 5 .   ? -2.059  21.014  -2.982  1.00 30.42 ? 752  HOH A O     1 
HETATM 4403 O  O     . HOH H 5 .   ? 19.856  -7.919  -2.453  1.00 47.23 ? 753  HOH A O     1 
HETATM 4404 O  O     . HOH H 5 .   ? -0.079  12.252  0.429   1.00 18.85 ? 754  HOH A O     1 
HETATM 4405 O  O     . HOH H 5 .   ? -54.657 -9.549  -28.784 1.00 37.99 ? 755  HOH A O     1 
HETATM 4406 O  O     . HOH H 5 .   ? -20.272 14.200  -26.321 1.00 31.77 ? 756  HOH A O     1 
HETATM 4407 O  O     . HOH H 5 .   ? -20.946 14.657  11.430  1.00 36.44 ? 757  HOH A O     1 
HETATM 4408 O  O     . HOH H 5 .   ? -30.990 -9.192  -27.341 1.00 26.68 ? 758  HOH A O     1 
HETATM 4409 O  O     . HOH H 5 .   ? -10.349 10.061  19.370  1.00 29.24 ? 759  HOH A O     1 
HETATM 4410 O  O     . HOH H 5 .   ? -37.578 -8.427  -23.823 1.00 30.26 ? 760  HOH A O     1 
HETATM 4411 O  O     . HOH H 5 .   ? -11.625 12.187  12.638  1.00 33.80 ? 761  HOH A O     1 
HETATM 4412 O  O     . HOH H 5 .   ? -50.200 0.433   -49.110 1.00 52.92 ? 762  HOH A O     1 
HETATM 4413 O  O     . HOH H 5 .   ? -16.361 16.840  -16.263 1.00 23.50 ? 763  HOH A O     1 
HETATM 4414 O  O     . HOH H 5 .   ? -36.803 -10.774 -29.974 1.00 32.61 ? 764  HOH A O     1 
HETATM 4415 O  O     . HOH H 5 .   ? -24.552 -10.541 -21.230 1.00 37.09 ? 765  HOH A O     1 
HETATM 4416 O  O     . HOH H 5 .   ? -46.427 -9.561  -18.542 1.00 38.06 ? 766  HOH A O     1 
HETATM 4417 O  O     . HOH H 5 .   ? 11.621  12.617  -14.007 1.00 35.02 ? 767  HOH A O     1 
HETATM 4418 O  O     . HOH H 5 .   ? -7.136  22.028  -14.425 1.00 34.44 ? 768  HOH A O     1 
HETATM 4419 O  O     . HOH H 5 .   ? -27.555 13.964  -8.202  1.00 22.19 ? 769  HOH A O     1 
HETATM 4420 O  O     . HOH H 5 .   ? -34.592 11.175  -7.949  1.00 24.07 ? 770  HOH A O     1 
HETATM 4421 O  O     . HOH H 5 .   ? -41.167 11.011  3.481   1.00 50.05 ? 771  HOH A O     1 
HETATM 4422 O  O     . HOH H 5 .   ? -5.139  19.555  -20.734 1.00 32.92 ? 772  HOH A O     1 
HETATM 4423 O  O     . HOH H 5 .   ? -16.068 9.709   14.735  1.00 36.47 ? 773  HOH A O     1 
HETATM 4424 O  O     . HOH H 5 .   ? -51.633 -12.201 -28.362 1.00 42.05 ? 774  HOH A O     1 
HETATM 4425 O  O     . HOH H 5 .   ? 5.199   19.759  13.861  1.00 34.73 ? 775  HOH A O     1 
HETATM 4426 O  O     . HOH H 5 .   ? -19.546 23.891  1.937   1.00 35.72 ? 776  HOH A O     1 
HETATM 4427 O  O     . HOH H 5 .   ? -15.471 17.930  -23.076 1.00 30.59 ? 777  HOH A O     1 
HETATM 4428 O  O     . HOH H 5 .   ? -32.228 -8.557  -8.918  1.00 32.93 ? 778  HOH A O     1 
HETATM 4429 O  O     . HOH H 5 .   ? 10.333  3.176   -0.033  1.00 45.33 ? 779  HOH A O     1 
HETATM 4430 O  O     . HOH H 5 .   ? 8.265   1.008   16.455  1.00 29.09 ? 780  HOH A O     1 
HETATM 4431 O  O     . HOH H 5 .   ? -34.209 1.884   -0.674  1.00 40.92 ? 781  HOH A O     1 
HETATM 4432 O  O     . HOH H 5 .   ? -21.755 16.024  -14.153 1.00 24.31 ? 782  HOH A O     1 
HETATM 4433 O  O     . HOH H 5 .   ? -30.596 13.948  -27.947 1.00 36.00 ? 783  HOH A O     1 
HETATM 4434 O  O     . HOH H 5 .   ? -10.354 17.050  13.575  1.00 39.54 ? 784  HOH A O     1 
HETATM 4435 O  O     . HOH H 5 .   ? -34.385 -6.823  -35.385 1.00 35.36 ? 785  HOH A O     1 
HETATM 4436 O  O     . HOH H 5 .   ? 12.367  19.404  -15.104 1.00 36.30 ? 786  HOH A O     1 
HETATM 4437 O  O     . HOH H 5 .   ? -51.346 9.127   -30.224 1.00 40.08 ? 787  HOH A O     1 
HETATM 4438 O  O     . HOH H 5 .   ? -0.630  -4.752  5.781   1.00 30.00 ? 788  HOH A O     1 
HETATM 4439 O  O     . HOH H 5 .   ? -17.165 1.914   12.815  1.00 25.96 ? 789  HOH A O     1 
HETATM 4440 O  O     . HOH H 5 .   ? -45.742 14.877  -39.360 1.00 38.75 ? 790  HOH A O     1 
HETATM 4441 O  O     . HOH H 5 .   ? -4.803  23.015  -8.817  1.00 25.20 ? 791  HOH A O     1 
HETATM 4442 O  O     . HOH H 5 .   ? -34.797 -11.421 -21.210 1.00 40.28 ? 792  HOH A O     1 
HETATM 4443 O  O     . HOH H 5 .   ? -25.123 15.342  -11.258 1.00 26.89 ? 793  HOH A O     1 
HETATM 4444 O  O     . HOH H 5 .   ? -29.891 5.839   2.125   1.00 23.40 ? 794  HOH A O     1 
HETATM 4445 O  O     . HOH H 5 .   ? -1.003  5.296   -22.079 1.00 38.76 ? 795  HOH A O     1 
HETATM 4446 O  O     . HOH H 5 .   ? -5.647  13.805  -19.089 1.00 23.98 ? 796  HOH A O     1 
HETATM 4447 O  O     . HOH H 5 .   ? -6.083  -11.166 -23.703 1.00 41.90 ? 797  HOH A O     1 
HETATM 4448 O  O     . HOH H 5 .   ? -7.635  3.665   -8.083  1.00 49.54 ? 798  HOH A O     1 
HETATM 4449 O  O     . HOH H 5 .   ? 10.804  11.437  13.351  1.00 29.33 ? 799  HOH A O     1 
HETATM 4450 O  O     . HOH H 5 .   ? -22.943 10.499  7.840   1.00 30.59 ? 800  HOH A O     1 
HETATM 4451 O  O     . HOH H 5 .   ? -21.772 18.311  11.309  1.00 36.26 ? 801  HOH A O     1 
HETATM 4452 O  O     . HOH H 5 .   ? -30.830 9.562   -21.209 1.00 31.69 ? 802  HOH A O     1 
HETATM 4453 O  O     . HOH H 5 .   ? -48.421 3.420   -17.495 1.00 35.71 ? 803  HOH A O     1 
HETATM 4454 O  O     . HOH H 5 .   ? -28.379 -5.735  -26.632 1.00 34.41 ? 804  HOH A O     1 
HETATM 4455 O  O     . HOH H 5 .   ? -16.967 -9.738  -23.566 1.00 40.08 ? 805  HOH A O     1 
HETATM 4456 O  O     . HOH H 5 .   ? -1.385  -4.986  11.942  1.00 23.95 ? 806  HOH A O     1 
HETATM 4457 O  O     . HOH H 5 .   ? -8.049  2.877   18.626  1.00 27.21 ? 807  HOH A O     1 
HETATM 4458 O  O     . HOH H 5 .   ? -3.410  -8.290  16.359  1.00 44.51 ? 808  HOH A O     1 
HETATM 4459 O  O     . HOH H 5 .   ? -12.226 10.806  -12.424 1.00 16.15 ? 809  HOH A O     1 
HETATM 4460 O  O     . HOH H 5 .   ? -51.033 6.470   -29.943 1.00 41.16 ? 810  HOH A O     1 
HETATM 4461 O  O     . HOH H 5 .   ? -1.123  23.713  -15.990 1.00 33.82 ? 811  HOH A O     1 
HETATM 4462 O  O     . HOH H 5 .   ? -7.134  15.326  14.255  1.00 30.23 ? 812  HOH A O     1 
HETATM 4463 O  O     . HOH H 5 .   ? 13.893  10.103  8.534   1.00 44.17 ? 813  HOH A O     1 
HETATM 4464 O  O     . HOH H 5 .   ? -36.674 -8.439  -35.840 1.00 41.00 ? 814  HOH A O     1 
HETATM 4465 O  O     . HOH H 5 .   ? -27.305 8.973   -30.615 1.00 34.57 ? 815  HOH A O     1 
HETATM 4466 O  O     . HOH H 5 .   ? -29.768 3.810   -0.874  1.00 21.60 ? 816  HOH A O     1 
HETATM 4467 O  O     . HOH H 5 .   ? -8.192  -6.715  19.127  1.00 32.24 ? 817  HOH A O     1 
HETATM 4468 O  O     . HOH H 5 .   ? -20.719 15.842  -17.701 1.00 37.41 ? 818  HOH A O     1 
HETATM 4469 O  O     . HOH H 5 .   ? 4.282   0.294   -2.152  1.00 25.33 ? 819  HOH A O     1 
HETATM 4470 O  O     . HOH H 5 .   ? -20.898 19.257  3.000   1.00 18.49 ? 820  HOH A O     1 
HETATM 4471 O  O     . HOH H 5 .   ? -32.989 13.271  0.685   1.00 26.25 ? 821  HOH A O     1 
HETATM 4472 O  O     . HOH H 5 .   ? -47.430 -11.133 -30.018 1.00 41.73 ? 822  HOH A O     1 
HETATM 4473 O  O     . HOH H 5 .   ? -13.116 -10.917 -13.928 1.00 36.90 ? 823  HOH A O     1 
HETATM 4474 O  O     . HOH H 5 .   ? -19.119 15.845  -2.903  1.00 21.57 ? 824  HOH A O     1 
HETATM 4475 O  O     . HOH H 5 .   ? -5.594  -6.388  -28.813 1.00 44.03 ? 825  HOH A O     1 
HETATM 4476 O  O     . HOH H 5 .   ? -15.541 -6.499  -16.428 1.00 29.74 ? 826  HOH A O     1 
HETATM 4477 O  O     . HOH H 5 .   ? -25.667 -1.059  -1.503  1.00 24.09 ? 827  HOH A O     1 
HETATM 4478 O  O     . HOH H 5 .   ? -55.418 0.913   -30.089 1.00 38.17 ? 828  HOH A O     1 
HETATM 4479 O  O     . HOH H 5 .   ? -0.396  -9.523  12.092  1.00 38.61 ? 829  HOH A O     1 
HETATM 4480 O  O     . HOH H 5 .   ? -30.024 -10.588 -14.893 1.00 35.90 ? 830  HOH A O     1 
HETATM 4481 O  O     . HOH H 5 .   ? -18.212 14.748  11.848  1.00 44.17 ? 831  HOH A O     1 
HETATM 4482 O  O     . HOH H 5 .   ? -33.539 10.486  3.137   1.00 33.29 ? 832  HOH A O     1 
HETATM 4483 O  O     . HOH H 5 .   ? 9.977   20.364  -13.676 1.00 33.37 ? 833  HOH A O     1 
HETATM 4484 O  O     . HOH H 5 .   ? 6.304   19.116  -21.765 1.00 43.31 ? 834  HOH A O     1 
HETATM 4485 O  O     . HOH H 5 .   ? 3.351   21.526  11.186  1.00 37.38 ? 835  HOH A O     1 
HETATM 4486 O  O     . HOH H 5 .   ? -49.603 4.694   -25.835 1.00 33.13 ? 836  HOH A O     1 
HETATM 4487 O  O     . HOH H 5 .   ? -0.429  18.648  -2.390  1.00 22.84 ? 837  HOH A O     1 
HETATM 4488 O  O     . HOH H 5 .   ? 5.232   17.818  16.699  1.00 43.50 ? 838  HOH A O     1 
HETATM 4489 O  O     . HOH H 5 .   ? -35.990 8.612   -37.370 1.00 36.87 ? 839  HOH A O     1 
HETATM 4490 O  O     . HOH H 5 .   ? -43.408 9.000   -44.943 1.00 36.28 ? 840  HOH A O     1 
HETATM 4491 O  O     . HOH H 5 .   ? -1.236  6.208   4.135   1.00 21.31 ? 841  HOH A O     1 
HETATM 4492 O  O     . HOH H 5 .   ? -26.376 7.462   0.898   1.00 18.45 ? 842  HOH A O     1 
HETATM 4493 O  O     . HOH H 5 .   ? -38.345 -6.112  -39.411 1.00 35.46 ? 843  HOH A O     1 
HETATM 4494 O  O     . HOH H 5 .   ? 5.383   -2.892  5.547   1.00 23.86 ? 844  HOH A O     1 
HETATM 4495 O  O     . HOH H 5 .   ? -4.969  19.909  9.673   1.00 32.03 ? 845  HOH A O     1 
HETATM 4496 O  O     . HOH H 5 .   ? -7.348  -1.734  -13.410 1.00 34.03 ? 846  HOH A O     1 
HETATM 4497 O  O     . HOH H 5 .   ? -14.997 3.442   -5.449  1.00 15.13 ? 847  HOH A O     1 
HETATM 4498 O  O     . HOH H 5 .   ? 1.379   11.856  -18.623 1.00 30.69 ? 848  HOH A O     1 
HETATM 4499 O  O     . HOH H 5 .   ? -11.198 -6.702  16.340  1.00 25.76 ? 849  HOH A O     1 
HETATM 4500 O  O     . HOH H 5 .   ? 5.798   -3.471  0.767   1.00 45.05 ? 850  HOH A O     1 
HETATM 4501 O  O     . HOH H 5 .   ? -31.652 11.108  -23.716 1.00 34.69 ? 851  HOH A O     1 
HETATM 4502 O  O     . HOH H 5 .   ? -38.432 -6.695  -11.245 1.00 36.18 ? 852  HOH A O     1 
HETATM 4503 O  O     . HOH H 5 .   ? 7.750   3.316   -0.754  1.00 32.30 ? 853  HOH A O     1 
HETATM 4504 O  O     . HOH H 5 .   ? -45.270 -10.693 -28.406 1.00 34.82 ? 854  HOH A O     1 
HETATM 4505 O  O     . HOH H 5 .   ? 6.145   13.349  -18.595 1.00 31.74 ? 855  HOH A O     1 
HETATM 4506 O  O     . HOH H 5 .   ? -12.019 19.393  4.845   1.00 31.23 ? 856  HOH A O     1 
HETATM 4507 O  O     . HOH H 5 .   ? -18.592 15.319  -16.059 1.00 23.01 ? 857  HOH A O     1 
HETATM 4508 O  O     . HOH H 5 .   ? -9.373  21.858  -10.452 1.00 35.05 ? 858  HOH A O     1 
HETATM 4509 O  O     . HOH H 5 .   ? -11.650 20.602  -18.409 1.00 35.73 ? 859  HOH A O     1 
HETATM 4510 O  O     . HOH H 5 .   ? -17.079 -7.362  -4.192  1.00 36.86 ? 860  HOH A O     1 
HETATM 4511 O  O     . HOH H 5 .   ? -9.940  14.642  -22.963 1.00 24.57 ? 861  HOH A O     1 
HETATM 4512 O  O     . HOH H 5 .   ? -5.550  6.468   -23.521 1.00 30.70 ? 862  HOH A O     1 
HETATM 4513 O  O     . HOH H 5 .   ? -28.833 12.967  7.756   1.00 26.54 ? 863  HOH A O     1 
HETATM 4514 O  O     . HOH H 5 .   ? -40.941 6.904   -12.286 1.00 29.77 ? 864  HOH A O     1 
HETATM 4515 O  O     . HOH H 5 .   ? -34.132 3.966   -41.695 1.00 34.33 ? 865  HOH A O     1 
HETATM 4516 O  O     . HOH H 5 .   ? -16.613 19.174  -0.066  1.00 35.49 ? 866  HOH A O     1 
HETATM 4517 O  O     . HOH H 5 .   ? -6.036  21.092  -6.941  1.00 22.57 ? 867  HOH A O     1 
HETATM 4518 O  O     . HOH H 5 .   ? -13.854 18.041  3.901   1.00 31.26 ? 868  HOH A O     1 
HETATM 4519 O  O     . HOH H 5 .   ? -10.365 0.810   18.216  1.00 35.83 ? 869  HOH A O     1 
HETATM 4520 O  O     . HOH H 5 .   ? 2.885   9.383   -19.183 1.00 39.73 ? 870  HOH A O     1 
HETATM 4521 O  O     . HOH H 5 .   ? -21.345 -10.552 -15.078 1.00 40.02 ? 871  HOH A O     1 
HETATM 4522 O  O     . HOH H 5 .   ? -31.541 9.727   -14.709 1.00 24.79 ? 872  HOH A O     1 
HETATM 4523 O  O     . HOH H 5 .   ? -29.462 0.545   -41.355 1.00 25.58 ? 873  HOH A O     1 
HETATM 4524 O  O     . HOH H 5 .   ? -16.143 16.490  -13.471 1.00 23.78 ? 874  HOH A O     1 
HETATM 4525 O  O     . HOH H 5 .   ? -16.582 -13.422 8.420   1.00 43.53 ? 875  HOH A O     1 
HETATM 4526 O  O     . HOH H 5 .   ? -28.205 -8.078  -30.467 1.00 42.20 ? 876  HOH A O     1 
HETATM 4527 O  O     . HOH H 5 .   ? 3.003   -1.648  4.670   1.00 22.66 ? 877  HOH A O     1 
HETATM 4528 O  O     . HOH H 5 .   ? 6.435   0.888   -0.571  1.00 26.81 ? 878  HOH A O     1 
HETATM 4529 O  O     . HOH H 5 .   ? -7.191  4.594   -29.347 1.00 42.19 ? 879  HOH A O     1 
HETATM 4530 O  O     . HOH H 5 .   ? -27.017 -11.109 -22.324 1.00 37.80 ? 880  HOH A O     1 
HETATM 4531 O  O     . HOH H 5 .   ? -49.707 4.554   -28.511 1.00 36.51 ? 881  HOH A O     1 
HETATM 4532 O  O     . HOH H 5 .   ? -2.956  6.136   23.272  1.00 34.10 ? 882  HOH A O     1 
HETATM 4533 O  O     . HOH H 5 .   ? 3.313   -6.320  11.418  1.00 27.24 ? 883  HOH A O     1 
HETATM 4534 O  O     . HOH H 5 .   ? -15.632 11.820  13.194  1.00 33.01 ? 884  HOH A O     1 
HETATM 4535 O  O     . HOH H 5 .   ? -15.143 -9.701  -12.368 1.00 42.39 ? 885  HOH A O     1 
HETATM 4536 O  O     . HOH H 5 .   ? -22.031 11.665  -30.320 1.00 34.88 ? 886  HOH A O     1 
HETATM 4537 O  O     . HOH H 5 .   ? -25.953 14.949  -4.646  1.00 24.17 ? 887  HOH A O     1 
HETATM 4538 O  O     . HOH H 5 .   ? 8.357   13.889  -4.347  1.00 24.16 ? 888  HOH A O     1 
HETATM 4539 O  O     . HOH H 5 .   ? 7.286   -11.459 4.025   1.00 40.24 ? 889  HOH A O     1 
HETATM 4540 O  O     . HOH H 5 .   ? -38.695 13.649  -8.598  1.00 42.87 ? 890  HOH A O     1 
HETATM 4541 O  O     . HOH H 5 .   ? 5.654   -2.453  12.585  1.00 40.65 ? 891  HOH A O     1 
HETATM 4542 O  O     . HOH H 5 .   ? -17.566 21.712  3.068   1.00 27.28 ? 892  HOH A O     1 
HETATM 4543 O  O     . HOH H 5 .   ? -1.846  10.665  22.955  1.00 43.72 ? 893  HOH A O     1 
HETATM 4544 O  O     . HOH H 5 .   ? 9.749   -0.729  12.620  1.00 28.18 ? 894  HOH A O     1 
HETATM 4545 O  O     . HOH H 5 .   ? -0.581  -8.111  5.549   1.00 31.30 ? 895  HOH A O     1 
HETATM 4546 O  O     . HOH H 5 .   ? -22.613 19.847  -4.981  1.00 30.71 ? 896  HOH A O     1 
HETATM 4547 O  O     . HOH H 5 .   ? 14.064  4.731   0.810   1.00 40.40 ? 897  HOH A O     1 
HETATM 4548 O  O     . HOH H 5 .   ? -37.064 14.821  -25.673 1.00 50.17 ? 898  HOH A O     1 
HETATM 4549 O  O     . HOH H 5 .   ? -29.551 11.458  -14.071 1.00 22.26 ? 899  HOH A O     1 
HETATM 4550 O  O     . HOH H 5 .   ? 14.699  7.176   6.822   1.00 34.28 ? 900  HOH A O     1 
HETATM 4551 O  O     . HOH H 5 .   ? 3.863   6.975   -6.986  1.00 24.00 ? 901  HOH A O     1 
HETATM 4552 O  O     . HOH H 5 .   ? -21.143 0.469   9.935   1.00 26.38 ? 902  HOH A O     1 
HETATM 4553 O  O     . HOH H 5 .   ? 1.216   18.937  2.962   1.00 38.30 ? 903  HOH A O     1 
HETATM 4554 O  O     . HOH H 5 .   ? -24.473 9.579   -29.814 1.00 30.27 ? 904  HOH A O     1 
HETATM 4555 O  O     . HOH H 5 .   ? -30.635 12.877  -7.290  1.00 22.39 ? 905  HOH A O     1 
HETATM 4556 O  O     . HOH H 5 .   ? -7.924  -7.011  -4.626  1.00 26.21 ? 906  HOH A O     1 
HETATM 4557 O  O     . HOH H 5 .   ? -54.097 5.509   -45.021 1.00 47.74 ? 907  HOH A O     1 
HETATM 4558 O  O     . HOH H 5 .   ? -31.883 8.358   3.120   1.00 22.09 ? 908  HOH A O     1 
HETATM 4559 O  O     . HOH H 5 .   ? -51.911 -7.859  -22.279 1.00 41.45 ? 909  HOH A O     1 
HETATM 4560 O  O     . HOH H 5 .   ? -18.446 -7.324  -6.675  1.00 26.58 ? 910  HOH A O     1 
HETATM 4561 O  O     . HOH H 5 .   ? -23.341 6.958   -31.365 1.00 29.63 ? 911  HOH A O     1 
HETATM 4562 O  O     . HOH H 5 .   ? -0.500  8.293   -21.631 1.00 32.74 ? 912  HOH A O     1 
HETATM 4563 O  O     . HOH H 5 .   ? -32.473 -9.037  -29.970 1.00 28.64 ? 913  HOH A O     1 
HETATM 4564 O  O     . HOH H 5 .   ? -14.417 9.019   -5.897  1.00 19.82 ? 914  HOH A O     1 
HETATM 4565 O  O     . HOH H 5 .   ? -30.693 1.760   -2.914  1.00 31.21 ? 915  HOH A O     1 
HETATM 4566 O  O     . HOH H 5 .   ? -8.847  -8.943  16.298  1.00 30.09 ? 916  HOH A O     1 
HETATM 4567 O  O     . HOH H 5 .   ? 2.855   0.070   2.278   1.00 19.09 ? 917  HOH A O     1 
HETATM 4568 O  O     . HOH H 5 .   ? -19.787 -7.524  -30.910 1.00 43.62 ? 918  HOH A O     1 
HETATM 4569 O  O     . HOH H 5 .   ? -27.166 7.830   4.316   1.00 21.96 ? 919  HOH A O     1 
HETATM 4570 O  O     . HOH H 5 .   ? 5.036   7.205   -4.272  1.00 21.93 ? 920  HOH A O     1 
HETATM 4571 O  O     . HOH H 5 .   ? -15.692 9.540   17.270  1.00 45.48 ? 921  HOH A O     1 
HETATM 4572 O  O     . HOH H 5 .   ? -0.236  12.483  -20.923 1.00 36.57 ? 922  HOH A O     1 
HETATM 4573 O  O     . HOH H 5 .   ? -16.302 -8.315  -19.809 1.00 32.81 ? 923  HOH A O     1 
HETATM 4574 O  O     . HOH H 5 .   ? -30.142 5.727   -36.809 1.00 28.09 ? 924  HOH A O     1 
HETATM 4575 O  O     . HOH H 5 .   ? -41.910 10.515  -43.336 1.00 46.37 ? 925  HOH A O     1 
HETATM 4576 O  O     . HOH H 5 .   ? -38.411 -0.194  -12.840 1.00 42.06 ? 926  HOH A O     1 
HETATM 4577 O  O     . HOH H 5 .   ? -51.275 11.311  -26.135 1.00 47.05 ? 927  HOH A O     1 
HETATM 4578 O  O     . HOH H 5 .   ? -28.564 -8.154  -27.811 1.00 36.48 ? 928  HOH A O     1 
HETATM 4579 O  O     . HOH H 5 .   ? 0.445   17.524  -18.449 1.00 41.22 ? 929  HOH A O     1 
HETATM 4580 O  O     . HOH H 5 .   ? -24.774 -7.148  3.156   1.00 32.34 ? 930  HOH A O     1 
HETATM 4581 O  O     . HOH H 5 .   ? -14.410 -6.556  -19.173 1.00 31.38 ? 931  HOH A O     1 
HETATM 4582 O  O     . HOH H 5 .   ? -10.483 22.883  -1.256  1.00 24.29 ? 932  HOH A O     1 
HETATM 4583 O  O     . HOH H 5 .   ? 9.364   -7.863  3.822   1.00 32.02 ? 933  HOH A O     1 
HETATM 4584 O  O     . HOH H 5 .   ? -19.865 -7.253  -40.481 1.00 44.70 ? 934  HOH A O     1 
HETATM 4585 O  O     . HOH H 5 .   ? -30.651 9.642   -17.304 1.00 26.38 ? 935  HOH A O     1 
HETATM 4586 O  O     . HOH H 5 .   ? -36.464 -2.043  -7.981  1.00 39.03 ? 936  HOH A O     1 
HETATM 4587 O  O     . HOH H 5 .   ? 3.519   22.272  -7.609  1.00 30.12 ? 937  HOH A O     1 
HETATM 4588 O  O     . HOH H 5 .   ? -19.030 19.478  -3.406  1.00 43.04 ? 938  HOH A O     1 
HETATM 4589 O  O     . HOH H 5 .   ? -4.180  14.795  -21.177 1.00 36.49 ? 939  HOH A O     1 
HETATM 4590 O  O     . HOH H 5 .   ? 2.625   16.645  -19.487 1.00 42.55 ? 940  HOH A O     1 
HETATM 4591 O  O     . HOH H 5 .   ? -39.570 15.699  -26.315 1.00 41.72 ? 941  HOH A O     1 
HETATM 4592 O  O     . HOH H 5 .   ? -18.559 -9.092  -8.662  1.00 40.57 ? 942  HOH A O     1 
HETATM 4593 O  O     . HOH H 5 .   ? -31.911 11.425  -18.854 1.00 40.56 ? 943  HOH A O     1 
HETATM 4594 O  O     . HOH H 5 .   ? -22.835 -6.110  -16.784 1.00 38.02 ? 944  HOH A O     1 
HETATM 4595 O  O     . HOH H 5 .   ? -39.372 -10.971 -39.158 1.00 44.32 ? 945  HOH A O     1 
HETATM 4596 O  O     . HOH H 5 .   ? -46.961 14.043  -24.725 1.00 34.64 ? 946  HOH A O     1 
HETATM 4597 O  O     . HOH H 5 .   ? -61.598 0.716   -49.482 1.00 56.76 ? 947  HOH A O     1 
HETATM 4598 O  O     . HOH H 5 .   ? -29.506 13.251  -31.421 1.00 51.90 ? 948  HOH A O     1 
HETATM 4599 O  O     . HOH H 5 .   ? 11.830  10.993  -5.028  1.00 34.02 ? 949  HOH A O     1 
HETATM 4600 O  O     . HOH H 5 .   ? 6.240   19.089  -2.097  1.00 32.19 ? 950  HOH A O     1 
HETATM 4601 O  O     . HOH H 5 .   ? -18.035 -0.656  13.056  1.00 44.15 ? 951  HOH A O     1 
HETATM 4602 O  O     . HOH H 5 .   ? 14.008  17.207  1.167   1.00 36.07 ? 952  HOH A O     1 
HETATM 4603 O  O     . HOH H 5 .   ? 16.959  -20.426 -3.027  1.00 43.89 ? 953  HOH A O     1 
HETATM 4604 O  O     . HOH H 5 .   ? -4.198  8.361   -25.005 1.00 38.43 ? 954  HOH A O     1 
HETATM 4605 O  O     . HOH H 5 .   ? -5.665  22.852  -4.976  1.00 32.54 ? 955  HOH A O     1 
HETATM 4606 O  O     . HOH H 5 .   ? -40.461 11.125  -0.254  1.00 38.60 ? 956  HOH A O     1 
HETATM 4607 O  O     . HOH H 5 .   ? -20.744 4.073   13.307  1.00 45.81 ? 957  HOH A O     1 
HETATM 4608 O  O     . HOH H 5 .   ? -37.772 15.953  -33.993 1.00 51.31 ? 958  HOH A O     1 
HETATM 4609 O  O     . HOH H 5 .   ? -11.927 11.982  18.251  1.00 43.18 ? 959  HOH A O     1 
HETATM 4610 O  O     . HOH H 5 .   ? 1.666   -4.022  4.706   1.00 36.11 ? 960  HOH A O     1 
HETATM 4611 O  O     . HOH H 5 .   ? -14.445 19.983  -18.681 1.00 35.37 ? 961  HOH A O     1 
HETATM 4612 O  O     . HOH H 5 .   ? -38.322 -10.954 -32.448 1.00 35.30 ? 962  HOH A O     1 
HETATM 4613 O  O     . HOH H 5 .   ? -27.094 4.367   5.975   1.00 27.20 ? 963  HOH A O     1 
HETATM 4614 O  O     . HOH H 5 .   ? -36.462 -6.279  -9.420  1.00 45.29 ? 964  HOH A O     1 
HETATM 4615 O  O     . HOH H 5 .   ? -3.846  23.570  -16.969 1.00 43.40 ? 965  HOH A O     1 
HETATM 4616 O  O     . HOH H 5 .   ? -17.869 17.607  -24.432 1.00 51.07 ? 966  HOH A O     1 
HETATM 4617 O  O     . HOH H 5 .   ? -32.299 -9.348  -34.488 1.00 48.05 ? 967  HOH A O     1 
HETATM 4618 O  O     . HOH H 5 .   ? 2.645   -3.422  -3.945  1.00 50.30 ? 968  HOH A O     1 
HETATM 4619 O  O     . HOH H 5 .   ? -33.020 6.482   -40.291 1.00 38.49 ? 969  HOH A O     1 
HETATM 4620 O  O     . HOH H 5 .   ? -33.743 11.157  -13.569 1.00 35.67 ? 970  HOH A O     1 
HETATM 4621 O  O     . HOH H 5 .   ? 7.347   14.158  -20.794 1.00 38.71 ? 971  HOH A O     1 
HETATM 4622 O  O     . HOH H 5 .   ? -22.211 -8.205  -31.960 1.00 44.02 ? 972  HOH A O     1 
HETATM 4623 O  O     . HOH H 5 .   ? -27.460 15.164  -12.586 1.00 38.55 ? 973  HOH A O     1 
HETATM 4624 O  O     . HOH H 5 .   ? -6.503  14.715  16.904  1.00 40.31 ? 974  HOH A O     1 
HETATM 4625 O  O     . HOH H 5 .   ? -16.440 19.562  -16.804 1.00 28.72 ? 975  HOH A O     1 
HETATM 4626 O  O     . HOH H 5 .   ? -34.200 -11.038 -30.662 1.00 32.11 ? 976  HOH A O     1 
HETATM 4627 O  O     . HOH H 5 .   ? -24.069 -12.294 -19.220 1.00 48.12 ? 977  HOH A O     1 
HETATM 4628 O  O     . HOH H 5 .   ? -26.083 -3.275  0.003   1.00 35.54 ? 978  HOH A O     1 
HETATM 4629 O  O     . HOH H 5 .   ? -13.806 14.248  14.815  1.00 39.83 ? 979  HOH A O     1 
HETATM 4630 O  O     . HOH H 5 .   ? -30.398 -9.055  -31.733 1.00 51.09 ? 980  HOH A O     1 
HETATM 4631 O  O     . HOH H 5 .   ? -54.558 -12.691 -36.489 1.00 48.21 ? 981  HOH A O     1 
HETATM 4632 O  O     . HOH H 5 .   ? -10.726 3.358   18.671  1.00 37.54 ? 982  HOH A O     1 
HETATM 4633 O  O     . HOH H 5 .   ? -28.774 13.907  -14.627 1.00 45.68 ? 983  HOH A O     1 
HETATM 4634 O  O     . HOH H 5 .   ? -32.757 13.210  -9.031  1.00 32.98 ? 984  HOH A O     1 
HETATM 4635 O  O     . HOH H 5 .   ? -9.628  21.536  -14.319 1.00 36.67 ? 985  HOH A O     1 
HETATM 4636 O  O     . HOH H 5 .   ? -2.323  -10.754 13.487  1.00 43.15 ? 986  HOH A O     1 
HETATM 4637 O  O     . HOH H 5 .   ? -3.587  15.693  17.822  1.00 38.29 ? 987  HOH A O     1 
HETATM 4638 O  O     . HOH H 5 .   ? 0.193   13.031  18.650  1.00 40.61 ? 988  HOH A O     1 
HETATM 4639 O  O     . HOH H 5 .   ? 3.299   -1.286  -0.140  1.00 29.06 ? 989  HOH A O     1 
HETATM 4640 O  O     . HOH H 5 .   ? -34.043 -11.320 -33.378 1.00 43.34 ? 990  HOH A O     1 
HETATM 4641 O  O     . HOH H 5 .   ? -12.420 -7.465  18.638  1.00 43.14 ? 991  HOH A O     1 
HETATM 4642 O  O     . HOH H 5 .   ? -29.630 15.885  -8.683  1.00 35.71 ? 992  HOH A O     1 
HETATM 4643 O  O     . HOH H 5 .   ? -0.012  5.264   -24.617 1.00 43.28 ? 993  HOH A O     1 
HETATM 4644 O  O     . HOH H 5 .   ? -28.049 7.856   6.758   1.00 37.23 ? 994  HOH A O     1 
HETATM 4645 O  O     . HOH H 5 .   ? -21.436 9.021   9.607   1.00 29.63 ? 995  HOH A O     1 
HETATM 4646 O  O     . HOH H 5 .   ? -21.168 13.533  -28.693 1.00 44.07 ? 996  HOH A O     1 
HETATM 4647 O  O     . HOH H 5 .   ? -30.504 12.093  5.946   1.00 37.09 ? 997  HOH A O     1 
HETATM 4648 O  O     . HOH H 5 .   ? -22.222 2.065   12.085  1.00 42.60 ? 998  HOH A O     1 
HETATM 4649 O  O     . HOH H 5 .   ? -15.366 20.143  -21.439 1.00 34.56 ? 999  HOH A O     1 
HETATM 4650 O  O     . HOH H 5 .   ? -1.324  22.780  -4.831  1.00 39.46 ? 1000 HOH A O     1 
HETATM 4651 O  O     . HOH H 5 .   ? -11.102 14.520  13.940  1.00 34.34 ? 1001 HOH A O     1 
HETATM 4652 O  O     . HOH H 5 .   ? -33.129 13.255  -11.855 1.00 34.57 ? 1002 HOH A O     1 
HETATM 4653 O  O     . HOH H 5 .   ? -11.575 21.977  5.075   1.00 44.28 ? 1003 HOH A O     1 
HETATM 4654 O  O     . HOH H 5 .   ? -30.114 6.625   5.734   1.00 26.41 ? 1004 HOH A O     1 
HETATM 4655 O  O     . HOH H 5 .   ? -14.804 -15.378 9.150   1.00 40.94 ? 1005 HOH A O     1 
HETATM 4656 O  O     . HOH H 5 .   ? 5.475   16.047  -22.039 1.00 45.90 ? 1006 HOH A O     1 
HETATM 4657 O  O     . HOH H 5 .   ? -26.846 -1.628  -4.162  1.00 36.97 ? 1007 HOH A O     1 
HETATM 4658 O  O     . HOH H 5 .   ? 1.496   22.735  -5.450  1.00 32.98 ? 1008 HOH A O     1 
HETATM 4659 O  O     . HOH H 5 .   ? -3.282  23.762  -6.326  1.00 39.02 ? 1009 HOH A O     1 
HETATM 4660 O  O     . HOH H 5 .   ? 1.418   -2.915  -1.546  1.00 38.77 ? 1010 HOH A O     1 
HETATM 4661 O  O     . HOH H 5 .   ? -16.048 20.877  -14.489 1.00 36.14 ? 1011 HOH A O     1 
HETATM 4662 O  O     . HOH H 5 .   ? -20.441 10.245  11.784  1.00 38.29 ? 1012 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   . ALA A 12  ? 0.4878 0.5985 0.4774 0.0340  -0.0123 -0.0521 2   ALA A N   
2    C CA  . ALA A 12  ? 0.4702 0.5659 0.4583 0.0344  -0.0132 -0.0503 2   ALA A CA  
3    C C   . ALA A 12  ? 0.4414 0.5328 0.4322 0.0284  -0.0106 -0.0471 2   ALA A C   
4    O O   . ALA A 12  ? 0.4456 0.5428 0.4394 0.0235  -0.0081 -0.0456 2   ALA A O   
5    C CB  . ALA A 12  ? 0.4905 0.5764 0.4767 0.0358  -0.0146 -0.0490 2   ALA A CB  
6    N N   . LYS A 13  ? 0.3966 0.4779 0.3862 0.0288  -0.0113 -0.0463 3   LYS A N   
7    C CA  . LYS A 13  ? 0.3648 0.4408 0.3568 0.0235  -0.0090 -0.0436 3   LYS A CA  
8    C C   . LYS A 13  ? 0.3410 0.4116 0.3348 0.0196  -0.0074 -0.0402 3   LYS A C   
9    O O   . LYS A 13  ? 0.3277 0.3928 0.3198 0.0214  -0.0087 -0.0395 3   LYS A O   
10   C CB  . LYS A 13  ? 0.3656 0.4317 0.3555 0.0252  -0.0104 -0.0434 3   LYS A CB  
11   C CG  . LYS A 13  ? 0.3664 0.4369 0.3548 0.0286  -0.0119 -0.0462 3   LYS A CG  
12   C CD  . LYS A 13  ? 0.3735 0.4341 0.3600 0.0291  -0.0130 -0.0453 3   LYS A CD  
13   C CE  . LYS A 13  ? 0.3800 0.4458 0.3655 0.0314  -0.0139 -0.0477 3   LYS A CE  
14   N NZ  . LYS A 13  ? 0.3902 0.4467 0.3734 0.0323  -0.0154 -0.0468 3   LYS A NZ  
15   N N   . GLU A 14  ? 0.3252 0.3971 0.3222 0.0141  -0.0048 -0.0381 4   GLU A N   
16   C CA  . GLU A 14  ? 0.3165 0.3825 0.3153 0.0104  -0.0033 -0.0347 4   GLU A CA  
17   C C   . GLU A 14  ? 0.2872 0.3410 0.2851 0.0107  -0.0039 -0.0332 4   GLU A C   
18   O O   . GLU A 14  ? 0.2676 0.3182 0.2650 0.0111  -0.0042 -0.0340 4   GLU A O   
19   C CB  . GLU A 14  ? 0.3440 0.4134 0.3462 0.0047  -0.0006 -0.0330 4   GLU A CB  
20   C CG  . GLU A 14  ? 0.3766 0.4585 0.3799 0.0031  0.0001  -0.0338 4   GLU A CG  
21   C CD  . GLU A 14  ? 0.4127 0.4982 0.4154 0.0039  -0.0003 -0.0331 4   GLU A CD  
22   O OE1 . GLU A 14  ? 0.4494 0.5277 0.4523 0.0030  -0.0002 -0.0305 4   GLU A OE1 
23   O OE2 . GLU A 14  ? 0.4422 0.5387 0.4443 0.0053  -0.0008 -0.0351 4   GLU A OE2 
24   N N   . THR A 15  ? 0.2631 0.3109 0.2607 0.0103  -0.0040 -0.0311 5   THR A N   
25   C CA  . THR A 15  ? 0.2604 0.2974 0.2571 0.0104  -0.0046 -0.0297 5   THR A CA  
26   C C   . THR A 15  ? 0.2526 0.2858 0.2524 0.0059  -0.0023 -0.0274 5   THR A C   
27   O O   . THR A 15  ? 0.2466 0.2835 0.2492 0.0025  -0.0005 -0.0262 5   THR A O   
28   C CB  . THR A 15  ? 0.2665 0.2987 0.2616 0.0118  -0.0057 -0.0284 5   THR A CB  
29   O OG1 . THR A 15  ? 0.2554 0.2899 0.2530 0.0088  -0.0041 -0.0261 5   THR A OG1 
30   C CG2 . THR A 15  ? 0.2729 0.3082 0.2647 0.0165  -0.0082 -0.0309 5   THR A CG2 
31   N N   . PHE A 16  ? 0.2458 0.2717 0.2449 0.0058  -0.0027 -0.0271 6   PHE A N   
32   C CA  . PHE A 16  ? 0.2422 0.2637 0.2441 0.0022  -0.0008 -0.0253 6   PHE A CA  
33   C C   . PHE A 16  ? 0.2360 0.2490 0.2363 0.0029  -0.0018 -0.0242 6   PHE A C   
34   O O   . PHE A 16  ? 0.2435 0.2537 0.2411 0.0050  -0.0033 -0.0253 6   PHE A O   
35   C CB  . PHE A 16  ? 0.2451 0.2691 0.2484 0.0007  0.0001  -0.0267 6   PHE A CB  
36   C CG  . PHE A 16  ? 0.2499 0.2698 0.2562 -0.0028 0.0020  -0.0254 6   PHE A CG  
37   C CD1 . PHE A 16  ? 0.2577 0.2715 0.2635 -0.0028 0.0017  -0.0253 6   PHE A CD1 
38   C CD2 . PHE A 16  ? 0.2634 0.2855 0.2728 -0.0062 0.0038  -0.0242 6   PHE A CD2 
39   C CE1 . PHE A 16  ? 0.2568 0.2675 0.2655 -0.0058 0.0034  -0.0245 6   PHE A CE1 
40   C CE2 . PHE A 16  ? 0.2649 0.2826 0.2769 -0.0091 0.0053  -0.0232 6   PHE A CE2 
41   C CZ  . PHE A 16  ? 0.2576 0.2698 0.2694 -0.0087 0.0051  -0.0235 6   PHE A CZ  
42   N N   . TYR A 17  ? 0.2268 0.2360 0.2287 0.0012  -0.0009 -0.0219 7   TYR A N   
43   C CA  . TYR A 17  ? 0.2243 0.2264 0.2249 0.0014  -0.0017 -0.0207 7   TYR A CA  
44   C C   . TYR A 17  ? 0.2180 0.2169 0.2216 -0.0014 0.0000  -0.0195 7   TYR A C   
45   O O   . TYR A 17  ? 0.2108 0.2106 0.2174 -0.0035 0.0015  -0.0181 7   TYR A O   
46   C CB  . TYR A 17  ? 0.2212 0.2222 0.2207 0.0024  -0.0025 -0.0193 7   TYR A CB  
47   C CG  . TYR A 17  ? 0.2175 0.2118 0.2154 0.0025  -0.0034 -0.0180 7   TYR A CG  
48   C CD1 . TYR A 17  ? 0.2202 0.2100 0.2157 0.0031  -0.0046 -0.0186 7   TYR A CD1 
49   C CD2 . TYR A 17  ? 0.2208 0.2137 0.2195 0.0018  -0.0031 -0.0160 7   TYR A CD2 
50   C CE1 . TYR A 17  ? 0.2229 0.2072 0.2166 0.0028  -0.0055 -0.0174 7   TYR A CE1 
51   C CE2 . TYR A 17  ? 0.2175 0.2052 0.2147 0.0017  -0.0039 -0.0149 7   TYR A CE2 
52   C CZ  . TYR A 17  ? 0.2251 0.2086 0.2198 0.0020  -0.0050 -0.0156 7   TYR A CZ  
53   O OH  . TYR A 17  ? 0.2325 0.2113 0.2254 0.0015  -0.0059 -0.0145 7   TYR A OH  
54   N N   . ILE A 18  ? 0.2210 0.2162 0.2236 -0.0014 -0.0004 -0.0200 8   ILE A N   
55   C CA  . ILE A 18  ? 0.2261 0.2186 0.2314 -0.0038 0.0010  -0.0194 8   ILE A CA  
56   C C   . ILE A 18  ? 0.2173 0.2048 0.2208 -0.0036 0.0001  -0.0186 8   ILE A C   
57   O O   . ILE A 18  ? 0.2096 0.1953 0.2094 -0.0020 -0.0017 -0.0191 8   ILE A O   
58   C CB  . ILE A 18  ? 0.2334 0.2284 0.2401 -0.0050 0.0020  -0.0213 8   ILE A CB  
59   C CG1 . ILE A 18  ? 0.2480 0.2403 0.2574 -0.0071 0.0034  -0.0211 8   ILE A CG1 
60   C CG2 . ILE A 18  ? 0.2341 0.2300 0.2376 -0.0031 0.0004  -0.0229 8   ILE A CG2 
61   C CD1 . ILE A 18  ? 0.2596 0.2546 0.2714 -0.0088 0.0048  -0.0228 8   ILE A CD1 
62   N N   . THR A 19  ? 0.2057 0.1910 0.2117 -0.0052 0.0012  -0.0173 9   THR A N   
63   C CA  . THR A 19  ? 0.2117 0.1932 0.2162 -0.0054 0.0005  -0.0165 9   THR A CA  
64   C C   . THR A 19  ? 0.2139 0.1949 0.2212 -0.0072 0.0019  -0.0169 9   THR A C   
65   O O   . THR A 19  ? 0.2208 0.2030 0.2318 -0.0083 0.0035  -0.0172 9   THR A O   
66   C CB  . THR A 19  ? 0.2052 0.1851 0.2098 -0.0052 0.0002  -0.0144 9   THR A CB  
67   O OG1 . THR A 19  ? 0.2103 0.1910 0.2190 -0.0064 0.0020  -0.0135 9   THR A OG1 
68   C CG2 . THR A 19  ? 0.2021 0.1832 0.2044 -0.0034 -0.0009 -0.0142 9   THR A CG2 
69   N N   . THR A 20  ? 0.2185 0.1976 0.2240 -0.0076 0.0011  -0.0170 10  THR A N   
70   C CA  . THR A 20  ? 0.2193 0.1983 0.2274 -0.0091 0.0023  -0.0172 10  THR A CA  
71   C C   . THR A 20  ? 0.2192 0.1965 0.2275 -0.0091 0.0021  -0.0154 10  THR A C   
72   O O   . THR A 20  ? 0.2271 0.2031 0.2330 -0.0083 0.0009  -0.0141 10  THR A O   
73   C CB  . THR A 20  ? 0.2214 0.2004 0.2273 -0.0099 0.0016  -0.0182 10  THR A CB  
74   O OG1 . THR A 20  ? 0.2332 0.2098 0.2352 -0.0099 0.0000  -0.0169 10  THR A OG1 
75   C CG2 . THR A 20  ? 0.2239 0.2044 0.2282 -0.0095 0.0011  -0.0197 10  THR A CG2 
76   N N   . PRO A 21  ? 0.2173 0.1949 0.2283 -0.0100 0.0032  -0.0155 11  PRO A N   
77   C CA  . PRO A 21  ? 0.2248 0.2016 0.2355 -0.0101 0.0028  -0.0139 11  PRO A CA  
78   C C   . PRO A 21  ? 0.2268 0.2027 0.2330 -0.0108 0.0011  -0.0136 11  PRO A C   
79   O O   . PRO A 21  ? 0.2377 0.2138 0.2420 -0.0114 0.0006  -0.0147 11  PRO A O   
80   C CB  . PRO A 21  ? 0.2245 0.2027 0.2390 -0.0107 0.0042  -0.0148 11  PRO A CB  
81   C CG  . PRO A 21  ? 0.2210 0.1998 0.2383 -0.0108 0.0054  -0.0164 11  PRO A CG  
82   C CD  . PRO A 21  ? 0.2229 0.2021 0.2372 -0.0109 0.0046  -0.0173 11  PRO A CD  
83   N N   . ILE A 22  ? 0.2247 0.1995 0.2292 -0.0109 0.0003  -0.0120 12  ILE A N   
84   C CA  . ILE A 22  ? 0.2266 0.2002 0.2269 -0.0122 -0.0012 -0.0115 12  ILE A CA  
85   C C   . ILE A 22  ? 0.2251 0.2015 0.2273 -0.0138 -0.0003 -0.0120 12  ILE A C   
86   O O   . ILE A 22  ? 0.2431 0.2214 0.2490 -0.0134 0.0008  -0.0117 12  ILE A O   
87   C CB  . ILE A 22  ? 0.2287 0.1998 0.2255 -0.0119 -0.0028 -0.0098 12  ILE A CB  
88   C CG1 . ILE A 22  ? 0.2290 0.2013 0.2286 -0.0115 -0.0019 -0.0086 12  ILE A CG1 
89   C CG2 . ILE A 22  ? 0.2323 0.2011 0.2266 -0.0102 -0.0040 -0.0101 12  ILE A CG2 
90   C CD1 . ILE A 22  ? 0.2383 0.2089 0.2344 -0.0118 -0.0035 -0.0071 12  ILE A CD1 
91   N N   . TYR A 23  ? 0.2268 0.2039 0.2269 -0.0153 -0.0008 -0.0128 13  TYR A N   
92   C CA  . TYR A 23  ? 0.2317 0.2127 0.2339 -0.0168 0.0000  -0.0137 13  TYR A CA  
93   C C   . TYR A 23  ? 0.2365 0.2185 0.2363 -0.0186 -0.0008 -0.0124 13  TYR A C   
94   O O   . TYR A 23  ? 0.2352 0.2141 0.2305 -0.0195 -0.0026 -0.0109 13  TYR A O   
95   C CB  . TYR A 23  ? 0.2359 0.2182 0.2371 -0.0178 0.0000  -0.0153 13  TYR A CB  
96   C CG  . TYR A 23  ? 0.2345 0.2163 0.2378 -0.0163 0.0008  -0.0167 13  TYR A CG  
97   C CD1 . TYR A 23  ? 0.2284 0.2115 0.2367 -0.0151 0.0027  -0.0178 13  TYR A CD1 
98   C CD2 . TYR A 23  ? 0.2408 0.2207 0.2408 -0.0160 -0.0003 -0.0168 13  TYR A CD2 
99   C CE1 . TYR A 23  ? 0.2380 0.2209 0.2480 -0.0142 0.0034  -0.0190 13  TYR A CE1 
100  C CE2 . TYR A 23  ? 0.2395 0.2198 0.2414 -0.0148 0.0004  -0.0182 13  TYR A CE2 
101  C CZ  . TYR A 23  ? 0.2338 0.2158 0.2407 -0.0141 0.0024  -0.0193 13  TYR A CZ  
102  O OH  . TYR A 23  ? 0.2421 0.2247 0.2507 -0.0134 0.0031  -0.0206 13  TYR A OH  
103  N N   . TYR A 24  ? 0.2371 0.2237 0.2399 -0.0193 0.0003  -0.0132 14  TYR A N   
104  C CA  . TYR A 24  ? 0.2480 0.2370 0.2494 -0.0210 -0.0001 -0.0120 14  TYR A CA  
105  C C   . TYR A 24  ? 0.2613 0.2535 0.2602 -0.0239 -0.0007 -0.0125 14  TYR A C   
106  O O   . TYR A 24  ? 0.2721 0.2690 0.2739 -0.0241 0.0005  -0.0145 14  TYR A O   
107  C CB  . TYR A 24  ? 0.2504 0.2431 0.2568 -0.0195 0.0013  -0.0126 14  TYR A CB  
108  C CG  . TYR A 24  ? 0.2530 0.2478 0.2582 -0.0205 0.0007  -0.0110 14  TYR A CG  
109  C CD1 . TYR A 24  ? 0.2479 0.2391 0.2507 -0.0202 -0.0002 -0.0090 14  TYR A CD1 
110  C CD2 . TYR A 24  ? 0.2586 0.2596 0.2649 -0.0218 0.0012  -0.0118 14  TYR A CD2 
111  C CE1 . TYR A 24  ? 0.2518 0.2451 0.2533 -0.0214 -0.0008 -0.0076 14  TYR A CE1 
112  C CE2 . TYR A 24  ? 0.2578 0.2615 0.2631 -0.0229 0.0007  -0.0105 14  TYR A CE2 
113  C CZ  . TYR A 24  ? 0.2574 0.2571 0.2602 -0.0228 -0.0003 -0.0083 14  TYR A CZ  
114  O OH  . TYR A 24  ? 0.2654 0.2680 0.2670 -0.0241 -0.0008 -0.0070 14  TYR A OH  
115  N N   . PRO A 25  ? 0.2685 0.2582 0.2616 -0.0264 -0.0027 -0.0109 15  PRO A N   
116  C CA  . PRO A 25  ? 0.2790 0.2710 0.2690 -0.0296 -0.0035 -0.0110 15  PRO A CA  
117  C C   . PRO A 25  ? 0.2885 0.2872 0.2788 -0.0322 -0.0031 -0.0110 15  PRO A C   
118  O O   . PRO A 25  ? 0.2977 0.2965 0.2832 -0.0358 -0.0047 -0.0095 15  PRO A O   
119  C CB  . PRO A 25  ? 0.2840 0.2694 0.2676 -0.0308 -0.0061 -0.0090 15  PRO A CB  
120  C CG  . PRO A 25  ? 0.2832 0.2652 0.2661 -0.0297 -0.0066 -0.0076 15  PRO A CG  
121  C CD  . PRO A 25  ? 0.2755 0.2593 0.2644 -0.0264 -0.0045 -0.0088 15  PRO A CD  
122  N N   . SER A 26  ? 0.2922 0.2965 0.2881 -0.0306 -0.0012 -0.0127 16  SER A N   
123  C CA  . SER A 26  ? 0.3054 0.3176 0.3024 -0.0325 -0.0006 -0.0134 16  SER A CA  
124  C C   . SER A 26  ? 0.3174 0.3353 0.3148 -0.0344 -0.0001 -0.0153 16  SER A C   
125  O O   . SER A 26  ? 0.3377 0.3634 0.3355 -0.0365 0.0002  -0.0160 16  SER A O   
126  C CB  . SER A 26  ? 0.3092 0.3247 0.3121 -0.0293 0.0010  -0.0146 16  SER A CB  
127  O OG  . SER A 26  ? 0.3115 0.3264 0.3189 -0.0263 0.0024  -0.0168 16  SER A OG  
128  N N   . GLY A 27  ? 0.3200 0.3350 0.3176 -0.0334 0.0000  -0.0162 17  GLY A N   
129  C CA  . GLY A 27  ? 0.3191 0.3385 0.3161 -0.0354 0.0002  -0.0177 17  GLY A CA  
130  C C   . GLY A 27  ? 0.3196 0.3331 0.3148 -0.0346 -0.0003 -0.0176 17  GLY A C   
131  O O   . GLY A 27  ? 0.3127 0.3194 0.3073 -0.0325 -0.0009 -0.0165 17  GLY A O   
132  N N   . ASN A 28  ? 0.3268 0.3437 0.3212 -0.0363 -0.0003 -0.0187 18  ASN A N   
133  C CA  . ASN A 28  ? 0.3342 0.3467 0.3269 -0.0355 -0.0009 -0.0188 18  ASN A CA  
134  C C   . ASN A 28  ? 0.3154 0.3261 0.3132 -0.0317 0.0007  -0.0209 18  ASN A C   
135  O O   . ASN A 28  ? 0.3008 0.3155 0.3038 -0.0301 0.0026  -0.0232 18  ASN A O   
136  C CB  . ASN A 28  ? 0.3566 0.3744 0.3480 -0.0381 -0.0010 -0.0198 18  ASN A CB  
137  C CG  . ASN A 28  ? 0.3823 0.4009 0.3675 -0.0425 -0.0030 -0.0172 18  ASN A CG  
138  O OD1 . ASN A 28  ? 0.4131 0.4260 0.3940 -0.0436 -0.0049 -0.0144 18  ASN A OD1 
139  N ND2 . ASN A 28  ? 0.4260 0.4519 0.4108 -0.0454 -0.0028 -0.0182 18  ASN A ND2 
140  N N   . LEU A 29  ? 0.2958 0.3007 0.2920 -0.0302 0.0000  -0.0202 19  LEU A N   
141  C CA  . LEU A 29  ? 0.2898 0.2935 0.2905 -0.0272 0.0015  -0.0222 19  LEU A CA  
142  C C   . LEU A 29  ? 0.2851 0.2937 0.2881 -0.0276 0.0027  -0.0250 19  LEU A C   
143  O O   . LEU A 29  ? 0.3027 0.3147 0.3031 -0.0301 0.0020  -0.0250 19  LEU A O   
144  C CB  . LEU A 29  ? 0.2883 0.2853 0.2865 -0.0255 0.0003  -0.0207 19  LEU A CB  
145  C CG  . LEU A 29  ? 0.2944 0.2865 0.2899 -0.0250 -0.0010 -0.0181 19  LEU A CG  
146  C CD1 . LEU A 29  ? 0.2986 0.2853 0.2929 -0.0227 -0.0017 -0.0175 19  LEU A CD1 
147  C CD2 . LEU A 29  ? 0.2943 0.2880 0.2935 -0.0242 0.0002  -0.0181 19  LEU A CD2 
148  N N   . HIS A 30  ? 0.2767 0.2859 0.2847 -0.0255 0.0045  -0.0274 20  HIS A N   
149  C CA  . HIS A 30  ? 0.2746 0.2886 0.2858 -0.0256 0.0059  -0.0306 20  HIS A CA  
150  C C   . HIS A 30  ? 0.2715 0.2822 0.2844 -0.0238 0.0065  -0.0316 20  HIS A C   
151  O O   . HIS A 30  ? 0.2624 0.2678 0.2738 -0.0226 0.0058  -0.0298 20  HIS A O   
152  C CB  . HIS A 30  ? 0.2778 0.2969 0.2936 -0.0252 0.0075  -0.0331 20  HIS A CB  
153  C CG  . HIS A 30  ? 0.2775 0.2934 0.2968 -0.0227 0.0082  -0.0331 20  HIS A CG  
154  N ND1 . HIS A 30  ? 0.2849 0.2967 0.3071 -0.0206 0.0091  -0.0338 20  HIS A ND1 
155  C CD2 . HIS A 30  ? 0.2830 0.2998 0.3036 -0.0220 0.0083  -0.0324 20  HIS A CD2 
156  C CE1 . HIS A 30  ? 0.2890 0.2987 0.3138 -0.0188 0.0095  -0.0334 20  HIS A CE1 
157  N NE2 . HIS A 30  ? 0.2807 0.2935 0.3048 -0.0194 0.0090  -0.0325 20  HIS A NE2 
158  N N   . ILE A 31  ? 0.2684 0.2826 0.2843 -0.0238 0.0079  -0.0347 21  ILE A N   
159  C CA  . ILE A 31  ? 0.2716 0.2834 0.2889 -0.0227 0.0085  -0.0358 21  ILE A CA  
160  C C   . ILE A 31  ? 0.2638 0.2709 0.2840 -0.0206 0.0092  -0.0355 21  ILE A C   
161  O O   . ILE A 31  ? 0.2580 0.2627 0.2783 -0.0199 0.0093  -0.0354 21  ILE A O   
162  C CB  . ILE A 31  ? 0.2862 0.3028 0.3059 -0.0235 0.0097  -0.0393 21  ILE A CB  
163  C CG1 . ILE A 31  ? 0.2987 0.3185 0.3233 -0.0230 0.0113  -0.0424 21  ILE A CG1 
164  C CG2 . ILE A 31  ? 0.2937 0.3145 0.3097 -0.0256 0.0087  -0.0390 21  ILE A CG2 
165  C CD1 . ILE A 31  ? 0.3038 0.3270 0.3314 -0.0234 0.0126  -0.0462 21  ILE A CD1 
166  N N   . GLY A 32  ? 0.2488 0.2554 0.2716 -0.0197 0.0097  -0.0354 22  GLY A N   
167  C CA  . GLY A 32  ? 0.2469 0.2486 0.2716 -0.0179 0.0100  -0.0341 22  GLY A CA  
168  C C   . GLY A 32  ? 0.2413 0.2389 0.2625 -0.0175 0.0087  -0.0309 22  GLY A C   
169  O O   . GLY A 32  ? 0.2361 0.2307 0.2578 -0.0166 0.0088  -0.0304 22  GLY A O   
170  N N   . HIS A 33  ? 0.2436 0.2413 0.2609 -0.0183 0.0073  -0.0290 23  HIS A N   
171  C CA  . HIS A 33  ? 0.2399 0.2339 0.2532 -0.0179 0.0057  -0.0263 23  HIS A CA  
172  C C   . HIS A 33  ? 0.2406 0.2340 0.2517 -0.0179 0.0051  -0.0266 23  HIS A C   
173  O O   . HIS A 33  ? 0.2457 0.2362 0.2557 -0.0166 0.0045  -0.0256 23  HIS A O   
174  C CB  . HIS A 33  ? 0.2444 0.2382 0.2538 -0.0192 0.0042  -0.0243 23  HIS A CB  
175  C CG  . HIS A 33  ? 0.2420 0.2375 0.2535 -0.0193 0.0048  -0.0240 23  HIS A CG  
176  N ND1 . HIS A 33  ? 0.2452 0.2457 0.2577 -0.0207 0.0053  -0.0254 23  HIS A ND1 
177  C CD2 . HIS A 33  ? 0.2447 0.2383 0.2578 -0.0180 0.0050  -0.0228 23  HIS A CD2 
178  C CE1 . HIS A 33  ? 0.2464 0.2480 0.2610 -0.0201 0.0058  -0.0251 23  HIS A CE1 
179  N NE2 . HIS A 33  ? 0.2452 0.2425 0.2602 -0.0185 0.0056  -0.0234 23  HIS A NE2 
180  N N   . ALA A 34  ? 0.2385 0.2353 0.2489 -0.0191 0.0052  -0.0282 24  ALA A N   
181  C CA  . ALA A 34  ? 0.2451 0.2422 0.2536 -0.0189 0.0046  -0.0288 24  ALA A CA  
182  C C   . ALA A 34  ? 0.2410 0.2381 0.2530 -0.0179 0.0060  -0.0303 24  ALA A C   
183  O O   . ALA A 34  ? 0.2340 0.2300 0.2443 -0.0169 0.0053  -0.0299 24  ALA A O   
184  C CB  . ALA A 34  ? 0.2480 0.2494 0.2554 -0.0207 0.0045  -0.0302 24  ALA A CB  
185  N N   . TYR A 35  ? 0.2496 0.2477 0.2661 -0.0180 0.0077  -0.0320 25  TYR A N   
186  C CA  . TYR A 35  ? 0.2553 0.2527 0.2751 -0.0176 0.0090  -0.0334 25  TYR A CA  
187  C C   . TYR A 35  ? 0.2484 0.2424 0.2675 -0.0163 0.0085  -0.0312 25  TYR A C   
188  O O   . TYR A 35  ? 0.2421 0.2365 0.2606 -0.0160 0.0085  -0.0314 25  TYR A O   
189  C CB  . TYR A 35  ? 0.2727 0.2704 0.2971 -0.0178 0.0106  -0.0352 25  TYR A CB  
190  C CG  . TYR A 35  ? 0.2873 0.2837 0.3153 -0.0178 0.0119  -0.0367 25  TYR A CG  
191  C CD1 . TYR A 35  ? 0.2943 0.2928 0.3227 -0.0188 0.0125  -0.0388 25  TYR A CD1 
192  C CD2 . TYR A 35  ? 0.3046 0.2976 0.3354 -0.0170 0.0124  -0.0361 25  TYR A CD2 
193  C CE1 . TYR A 35  ? 0.3085 0.3056 0.3401 -0.0193 0.0136  -0.0402 25  TYR A CE1 
194  C CE2 . TYR A 35  ? 0.3115 0.3026 0.3453 -0.0173 0.0134  -0.0374 25  TYR A CE2 
195  C CZ  . TYR A 35  ? 0.3127 0.3057 0.3468 -0.0186 0.0140  -0.0394 25  TYR A CZ  
196  O OH  . TYR A 35  ? 0.3306 0.3213 0.3675 -0.0194 0.0149  -0.0406 25  TYR A OH  
197  N N   . SER A 36  ? 0.2408 0.2321 0.2596 -0.0156 0.0080  -0.0291 26  SER A N   
198  C CA  . SER A 36  ? 0.2348 0.2233 0.2526 -0.0144 0.0075  -0.0270 26  SER A CA  
199  C C   . SER A 36  ? 0.2278 0.2162 0.2414 -0.0137 0.0059  -0.0261 26  SER A C   
200  O O   . SER A 36  ? 0.2311 0.2195 0.2445 -0.0129 0.0058  -0.0259 26  SER A O   
201  C CB  . SER A 36  ? 0.2405 0.2267 0.2584 -0.0138 0.0071  -0.0250 26  SER A CB  
202  O OG  . SER A 36  ? 0.2564 0.2423 0.2784 -0.0139 0.0084  -0.0257 26  SER A OG  
203  N N   . THR A 37  ? 0.2229 0.2113 0.2330 -0.0139 0.0045  -0.0256 27  THR A N   
204  C CA  . THR A 37  ? 0.2259 0.2131 0.2315 -0.0128 0.0025  -0.0247 27  THR A CA  
205  C C   . THR A 37  ? 0.2297 0.2197 0.2349 -0.0125 0.0025  -0.0263 27  THR A C   
206  O O   . THR A 37  ? 0.2271 0.2169 0.2303 -0.0109 0.0015  -0.0260 27  THR A O   
207  C CB  . THR A 37  ? 0.2341 0.2196 0.2356 -0.0135 0.0008  -0.0234 27  THR A CB  
208  O OG1 . THR A 37  ? 0.2428 0.2267 0.2452 -0.0139 0.0010  -0.0221 27  THR A OG1 
209  C CG2 . THR A 37  ? 0.2385 0.2211 0.2351 -0.0120 -0.0015 -0.0221 27  THR A CG2 
210  N N   . VAL A 38  ? 0.2298 0.2230 0.2369 -0.0139 0.0037  -0.0283 28  VAL A N   
211  C CA  . VAL A 38  ? 0.2335 0.2301 0.2408 -0.0138 0.0040  -0.0301 28  VAL A CA  
212  C C   . VAL A 38  ? 0.2285 0.2261 0.2387 -0.0135 0.0052  -0.0308 28  VAL A C   
213  O O   . VAL A 38  ? 0.2328 0.2324 0.2418 -0.0125 0.0047  -0.0312 28  VAL A O   
214  C CB  . VAL A 38  ? 0.2334 0.2336 0.2421 -0.0156 0.0049  -0.0322 28  VAL A CB  
215  C CG1 . VAL A 38  ? 0.2381 0.2423 0.2477 -0.0157 0.0056  -0.0343 28  VAL A CG1 
216  C CG2 . VAL A 38  ? 0.2346 0.2346 0.2394 -0.0161 0.0033  -0.0312 28  VAL A CG2 
217  N N   . ALA A 39  ? 0.2267 0.2230 0.2406 -0.0143 0.0068  -0.0308 29  ALA A N   
218  C CA  . ALA A 39  ? 0.2268 0.2233 0.2432 -0.0145 0.0078  -0.0309 29  ALA A CA  
219  C C   . ALA A 39  ? 0.2231 0.2191 0.2372 -0.0128 0.0066  -0.0292 29  ALA A C   
220  O O   . ALA A 39  ? 0.2262 0.2251 0.2404 -0.0127 0.0068  -0.0298 29  ALA A O   
221  C CB  . ALA A 39  ? 0.2286 0.2226 0.2487 -0.0154 0.0091  -0.0306 29  ALA A CB  
222  N N   . GLY A 40  ? 0.2216 0.2145 0.2336 -0.0116 0.0054  -0.0272 30  GLY A N   
223  C CA  . GLY A 40  ? 0.2250 0.2173 0.2345 -0.0098 0.0041  -0.0258 30  GLY A CA  
224  C C   . GLY A 40  ? 0.2250 0.2196 0.2312 -0.0083 0.0026  -0.0267 30  GLY A C   
225  O O   . GLY A 40  ? 0.2270 0.2238 0.2324 -0.0069 0.0021  -0.0269 30  GLY A O   
226  N N   . ASP A 41  ? 0.2244 0.2189 0.2286 -0.0084 0.0018  -0.0274 31  ASP A N   
227  C CA  . ASP A 41  ? 0.2295 0.2260 0.2304 -0.0068 0.0002  -0.0283 31  ASP A CA  
228  C C   . ASP A 41  ? 0.2274 0.2295 0.2302 -0.0070 0.0013  -0.0303 31  ASP A C   
229  O O   . ASP A 41  ? 0.2288 0.2335 0.2297 -0.0049 0.0001  -0.0308 31  ASP A O   
230  C CB  . ASP A 41  ? 0.2346 0.2300 0.2331 -0.0074 -0.0007 -0.0283 31  ASP A CB  
231  C CG  . ASP A 41  ? 0.2401 0.2361 0.2345 -0.0053 -0.0030 -0.0286 31  ASP A CG  
232  O OD1 . ASP A 41  ? 0.2553 0.2485 0.2465 -0.0030 -0.0049 -0.0277 31  ASP A OD1 
233  O OD2 . ASP A 41  ? 0.2463 0.2454 0.2404 -0.0058 -0.0029 -0.0299 31  ASP A OD2 
234  N N   . VAL A 42  ? 0.2241 0.2283 0.2307 -0.0094 0.0034  -0.0315 32  VAL A N   
235  C CA  . VAL A 42  ? 0.2299 0.2394 0.2384 -0.0102 0.0046  -0.0335 32  VAL A CA  
236  C C   . VAL A 42  ? 0.2272 0.2384 0.2365 -0.0097 0.0048  -0.0329 32  VAL A C   
237  O O   . VAL A 42  ? 0.2429 0.2590 0.2513 -0.0088 0.0045  -0.0340 32  VAL A O   
238  C CB  . VAL A 42  ? 0.2300 0.2404 0.2424 -0.0132 0.0067  -0.0349 32  VAL A CB  
239  C CG1 . VAL A 42  ? 0.2317 0.2471 0.2461 -0.0146 0.0080  -0.0368 32  VAL A CG1 
240  C CG2 . VAL A 42  ? 0.2317 0.2423 0.2433 -0.0138 0.0065  -0.0359 32  VAL A CG2 
241  N N   . ILE A 43  ? 0.2330 0.2407 0.2437 -0.0102 0.0053  -0.0312 33  ILE A N   
242  C CA  . ILE A 43  ? 0.2409 0.2503 0.2521 -0.0099 0.0055  -0.0304 33  ILE A CA  
243  C C   . ILE A 43  ? 0.2393 0.2505 0.2469 -0.0067 0.0035  -0.0303 33  ILE A C   
244  O O   . ILE A 43  ? 0.2454 0.2619 0.2528 -0.0061 0.0034  -0.0312 33  ILE A O   
245  C CB  . ILE A 43  ? 0.2469 0.2519 0.2599 -0.0108 0.0062  -0.0282 33  ILE A CB  
246  C CG1 . ILE A 43  ? 0.2507 0.2539 0.2674 -0.0136 0.0080  -0.0286 33  ILE A CG1 
247  C CG2 . ILE A 43  ? 0.2542 0.2617 0.2674 -0.0105 0.0062  -0.0272 33  ILE A CG2 
248  C CD1 . ILE A 43  ? 0.2614 0.2597 0.2798 -0.0139 0.0084  -0.0266 33  ILE A CD1 
249  N N   . ALA A 44  ? 0.2373 0.2442 0.2420 -0.0048 0.0017  -0.0293 34  ALA A N   
250  C CA  . ALA A 44  ? 0.2418 0.2489 0.2425 -0.0014 -0.0005 -0.0294 34  ALA A CA  
251  C C   . ALA A 44  ? 0.2460 0.2582 0.2452 0.0001  -0.0014 -0.0315 34  ALA A C   
252  O O   . ALA A 44  ? 0.2450 0.2614 0.2430 0.0023  -0.0022 -0.0323 34  ALA A O   
253  C CB  . ALA A 44  ? 0.2462 0.2470 0.2438 -0.0003 -0.0023 -0.0280 34  ALA A CB  
254  N N   . ARG A 45  ? 0.2393 0.2518 0.2384 -0.0008 -0.0012 -0.0323 35  ARG A N   
255  C CA  . ARG A 45  ? 0.2505 0.2680 0.2481 0.0006  -0.0020 -0.0342 35  ARG A CA  
256  C C   . ARG A 45  ? 0.2524 0.2775 0.2527 -0.0003 -0.0005 -0.0359 35  ARG A C   
257  O O   . ARG A 45  ? 0.2596 0.2901 0.2584 0.0020  -0.0016 -0.0372 35  ARG A O   
258  C CB  . ARG A 45  ? 0.2565 0.2731 0.2538 -0.0007 -0.0019 -0.0347 35  ARG A CB  
259  C CG  . ARG A 45  ? 0.2636 0.2738 0.2572 0.0003  -0.0040 -0.0331 35  ARG A CG  
260  C CD  . ARG A 45  ? 0.2695 0.2797 0.2632 -0.0016 -0.0036 -0.0335 35  ARG A CD  
261  N NE  . ARG A 45  ? 0.2780 0.2825 0.2675 -0.0009 -0.0059 -0.0318 35  ARG A NE  
262  C CZ  . ARG A 45  ? 0.2941 0.2971 0.2790 0.0017  -0.0087 -0.0315 35  ARG A CZ  
263  N NH1 . ARG A 45  ? 0.3038 0.3112 0.2877 0.0043  -0.0097 -0.0330 35  ARG A NH1 
264  N NH2 . ARG A 45  ? 0.2950 0.2921 0.2761 0.0016  -0.0107 -0.0296 35  ARG A NH2 
265  N N   . TYR A 46  ? 0.2487 0.2744 0.2528 -0.0038 0.0019  -0.0357 36  TYR A N   
266  C CA  . TYR A 46  ? 0.2588 0.2913 0.2654 -0.0056 0.0034  -0.0369 36  TYR A CA  
267  C C   . TYR A 46  ? 0.2556 0.2914 0.2614 -0.0039 0.0027  -0.0365 36  TYR A C   
268  O O   . TYR A 46  ? 0.2528 0.2960 0.2581 -0.0029 0.0025  -0.0381 36  TYR A O   
269  C CB  . TYR A 46  ? 0.2645 0.2950 0.2750 -0.0098 0.0058  -0.0364 36  TYR A CB  
270  C CG  . TYR A 46  ? 0.2729 0.3088 0.2857 -0.0125 0.0074  -0.0371 36  TYR A CG  
271  C CD1 . TYR A 46  ? 0.2759 0.3182 0.2895 -0.0139 0.0081  -0.0393 36  TYR A CD1 
272  C CD2 . TYR A 46  ? 0.2866 0.3213 0.3009 -0.0140 0.0081  -0.0354 36  TYR A CD2 
273  C CE1 . TYR A 46  ? 0.2886 0.3361 0.3042 -0.0170 0.0095  -0.0399 36  TYR A CE1 
274  C CE2 . TYR A 46  ? 0.2914 0.3310 0.3076 -0.0170 0.0095  -0.0357 36  TYR A CE2 
275  C CZ  . TYR A 46  ? 0.2975 0.3434 0.3143 -0.0187 0.0102  -0.0380 36  TYR A CZ  
276  O OH  . TYR A 46  ? 0.3272 0.3781 0.3456 -0.0222 0.0115  -0.0383 36  TYR A OH  
277  N N   . LYS A 47  ? 0.2586 0.2896 0.2641 -0.0033 0.0024  -0.0346 37  LYS A N   
278  C CA  . LYS A 47  ? 0.2700 0.3042 0.2746 -0.0016 0.0017  -0.0342 37  LYS A CA  
279  C C   . LYS A 47  ? 0.2695 0.3068 0.2705 0.0028  -0.0007 -0.0357 37  LYS A C   
280  O O   . LYS A 47  ? 0.2784 0.3228 0.2792 0.0041  -0.0009 -0.0368 37  LYS A O   
281  C CB  . LYS A 47  ? 0.2790 0.3072 0.2840 -0.0020 0.0017  -0.0318 37  LYS A CB  
282  C CG  . LYS A 47  ? 0.2949 0.3215 0.3035 -0.0061 0.0040  -0.0304 37  LYS A CG  
283  C CD  . LYS A 47  ? 0.3227 0.3559 0.3329 -0.0080 0.0051  -0.0304 37  LYS A CD  
284  C CE  . LYS A 47  ? 0.3542 0.3855 0.3677 -0.0123 0.0071  -0.0290 37  LYS A CE  
285  N NZ  . LYS A 47  ? 0.3743 0.4119 0.3886 -0.0142 0.0077  -0.0285 37  LYS A NZ  
286  N N   . ARG A 48  ? 0.2656 0.2981 0.2638 0.0053  -0.0025 -0.0358 38  ARG A N   
287  C CA  . ARG A 48  ? 0.2764 0.3108 0.2708 0.0099  -0.0052 -0.0373 38  ARG A CA  
288  C C   . ARG A 48  ? 0.2819 0.3254 0.2769 0.0104  -0.0049 -0.0397 38  ARG A C   
289  O O   . ARG A 48  ? 0.2809 0.3306 0.2746 0.0135  -0.0061 -0.0414 38  ARG A O   
290  C CB  . ARG A 48  ? 0.2786 0.3052 0.2696 0.0118  -0.0073 -0.0366 38  ARG A CB  
291  C CG  . ARG A 48  ? 0.2732 0.2916 0.2626 0.0121  -0.0083 -0.0345 38  ARG A CG  
292  C CD  . ARG A 48  ? 0.2767 0.2880 0.2614 0.0146  -0.0112 -0.0339 38  ARG A CD  
293  N NE  . ARG A 48  ? 0.2778 0.2812 0.2616 0.0133  -0.0115 -0.0317 38  ARG A NE  
294  C CZ  . ARG A 48  ? 0.2781 0.2773 0.2629 0.0101  -0.0104 -0.0302 38  ARG A CZ  
295  N NH1 . ARG A 48  ? 0.2766 0.2782 0.2634 0.0078  -0.0090 -0.0307 38  ARG A NH1 
296  N NH2 . ARG A 48  ? 0.2781 0.2712 0.2620 0.0092  -0.0108 -0.0283 38  ARG A NH2 
297  N N   . MET A 49  ? 0.2805 0.3255 0.2776 0.0072  -0.0032 -0.0401 39  MET A N   
298  C CA  . MET A 49  ? 0.2895 0.3436 0.2876 0.0069  -0.0026 -0.0424 39  MET A CA  
299  C C   . MET A 49  ? 0.2928 0.3554 0.2933 0.0051  -0.0010 -0.0432 39  MET A C   
300  O O   . MET A 49  ? 0.2875 0.3593 0.2878 0.0063  -0.0012 -0.0454 39  MET A O   
301  C CB  . MET A 49  ? 0.2952 0.3486 0.2951 0.0036  -0.0010 -0.0427 39  MET A CB  
302  C CG  . MET A 49  ? 0.3028 0.3520 0.2997 0.0058  -0.0029 -0.0427 39  MET A CG  
303  S SD  . MET A 49  ? 0.3229 0.3723 0.3220 0.0017  -0.0010 -0.0433 39  MET A SD  
304  C CE  . MET A 49  ? 0.3259 0.3874 0.3263 0.0013  -0.0002 -0.0462 39  MET A CE  
305  N N   A GLN A 50  ? 0.2874 0.3474 0.2900 0.0022  0.0005  -0.0414 40  GLN A N   
306  N N   B GLN A 50  ? 0.2915 0.3514 0.2941 0.0021  0.0005  -0.0414 40  GLN A N   
307  C CA  A GLN A 50  ? 0.2909 0.3583 0.2954 0.0001  0.0017  -0.0416 40  GLN A CA  
308  C CA  B GLN A 50  ? 0.2977 0.3649 0.3021 0.0001  0.0017  -0.0416 40  GLN A CA  
309  C C   A GLN A 50  ? 0.2923 0.3630 0.2947 0.0039  0.0001  -0.0419 40  GLN A C   
310  C C   B GLN A 50  ? 0.2965 0.3680 0.2989 0.0041  0.0000  -0.0422 40  GLN A C   
311  O O   A GLN A 50  ? 0.2912 0.3683 0.2950 0.0023  0.0010  -0.0418 40  GLN A O   
312  O O   B GLN A 50  ? 0.2951 0.3745 0.2986 0.0028  0.0008  -0.0426 40  GLN A O   
313  C CB  A GLN A 50  ? 0.2931 0.3561 0.3006 -0.0046 0.0039  -0.0394 40  GLN A CB  
314  C CB  B GLN A 50  ? 0.3055 0.3679 0.3128 -0.0043 0.0038  -0.0392 40  GLN A CB  
315  C CG  A GLN A 50  ? 0.2962 0.3577 0.3061 -0.0087 0.0058  -0.0397 40  GLN A CG  
316  C CG  B GLN A 50  ? 0.3140 0.3752 0.3240 -0.0089 0.0058  -0.0393 40  GLN A CG  
317  C CD  A GLN A 50  ? 0.2974 0.3686 0.3084 -0.0109 0.0068  -0.0418 40  GLN A CD  
318  C CD  B GLN A 50  ? 0.3192 0.3777 0.3319 -0.0133 0.0077  -0.0372 40  GLN A CD  
319  O OE1 A GLN A 50  ? 0.2959 0.3751 0.3053 -0.0082 0.0057  -0.0436 40  GLN A OE1 
320  O OE1 B GLN A 50  ? 0.3345 0.3875 0.3473 -0.0129 0.0074  -0.0351 40  GLN A OE1 
321  N NE2 A GLN A 50  ? 0.2984 0.3690 0.3120 -0.0157 0.0088  -0.0418 40  GLN A NE2 
322  N NE2 B GLN A 50  ? 0.3235 0.3858 0.3384 -0.0176 0.0093  -0.0379 40  GLN A NE2 
323  N N   . GLY A 51  ? 0.2909 0.3573 0.2902 0.0087  -0.0023 -0.0422 41  GLY A N   
324  C CA  . GLY A 51  ? 0.2853 0.3550 0.2823 0.0131  -0.0043 -0.0433 41  GLY A CA  
325  C C   . GLY A 51  ? 0.2812 0.3455 0.2778 0.0132  -0.0046 -0.0413 41  GLY A C   
326  O O   . GLY A 51  ? 0.2838 0.3527 0.2793 0.0160  -0.0057 -0.0423 41  GLY A O   
327  N N   . TYR A 52  ? 0.2701 0.3255 0.2678 0.0105  -0.0036 -0.0388 42  TYR A N   
328  C CA  . TYR A 52  ? 0.2705 0.3203 0.2679 0.0106  -0.0039 -0.0367 42  TYR A CA  
329  C C   . TYR A 52  ? 0.2686 0.3109 0.2622 0.0147  -0.0066 -0.0368 42  TYR A C   
330  O O   . TYR A 52  ? 0.2780 0.3167 0.2696 0.0163  -0.0079 -0.0375 42  TYR A O   
331  C CB  . TYR A 52  ? 0.2755 0.3193 0.2756 0.0059  -0.0017 -0.0341 42  TYR A CB  
332  C CG  . TYR A 52  ? 0.2825 0.3318 0.2860 0.0016  0.0005  -0.0334 42  TYR A CG  
333  C CD1 . TYR A 52  ? 0.2896 0.3404 0.2942 0.0002  0.0012  -0.0316 42  TYR A CD1 
334  C CD2 . TYR A 52  ? 0.2919 0.3451 0.2973 -0.0011 0.0020  -0.0343 42  TYR A CD2 
335  C CE1 . TYR A 52  ? 0.2989 0.3543 0.3062 -0.0040 0.0032  -0.0307 42  TYR A CE1 
336  C CE2 . TYR A 52  ? 0.3078 0.3654 0.3159 -0.0054 0.0040  -0.0336 42  TYR A CE2 
337  C CZ  . TYR A 52  ? 0.3109 0.3693 0.3199 -0.0069 0.0045  -0.0317 42  TYR A CZ  
338  O OH  . TYR A 52  ? 0.3303 0.3926 0.3416 -0.0115 0.0063  -0.0306 42  TYR A OH  
339  N N   . ASP A 53  ? 0.2672 0.3074 0.2596 0.0162  -0.0075 -0.0361 43  ASP A N   
340  C CA  . ASP A 53  ? 0.2733 0.3052 0.2621 0.0193  -0.0100 -0.0357 43  ASP A CA  
341  C C   . ASP A 53  ? 0.2664 0.2901 0.2564 0.0159  -0.0088 -0.0328 43  ASP A C   
342  O O   . ASP A 53  ? 0.2552 0.2783 0.2469 0.0141  -0.0077 -0.0311 43  ASP A O   
343  C CB  . ASP A 53  ? 0.2848 0.3198 0.2720 0.0225  -0.0114 -0.0368 43  ASP A CB  
344  C CG  . ASP A 53  ? 0.3051 0.3312 0.2888 0.0250  -0.0138 -0.0362 43  ASP A CG  
345  O OD1 . ASP A 53  ? 0.2958 0.3132 0.2779 0.0242  -0.0145 -0.0348 43  ASP A OD1 
346  O OD2 . ASP A 53  ? 0.3276 0.3559 0.3101 0.0274  -0.0149 -0.0372 43  ASP A OD2 
347  N N   . VAL A 54  ? 0.2529 0.2709 0.2421 0.0151  -0.0091 -0.0323 44  VAL A N   
348  C CA  . VAL A 54  ? 0.2483 0.2602 0.2392 0.0116  -0.0076 -0.0300 44  VAL A CA  
349  C C   . VAL A 54  ? 0.2508 0.2543 0.2386 0.0126  -0.0094 -0.0286 44  VAL A C   
350  O O   . VAL A 54  ? 0.2520 0.2523 0.2359 0.0156  -0.0120 -0.0295 44  VAL A O   
351  C CB  . VAL A 54  ? 0.2501 0.2620 0.2423 0.0096  -0.0066 -0.0303 44  VAL A CB  
352  C CG1 . VAL A 54  ? 0.2494 0.2550 0.2429 0.0065  -0.0055 -0.0284 44  VAL A CG1 
353  C CG2 . VAL A 54  ? 0.2519 0.2716 0.2475 0.0075  -0.0044 -0.0314 44  VAL A CG2 
354  N N   . ARG A 55  ? 0.2474 0.2474 0.2369 0.0102  -0.0082 -0.0265 45  ARG A N   
355  C CA  . ARG A 55  ? 0.2496 0.2419 0.2368 0.0099  -0.0094 -0.0250 45  ARG A CA  
356  C C   . ARG A 55  ? 0.2360 0.2263 0.2263 0.0062  -0.0073 -0.0234 45  ARG A C   
357  O O   . ARG A 55  ? 0.2297 0.2224 0.2237 0.0041  -0.0051 -0.0226 45  ARG A O   
358  C CB  . ARG A 55  ? 0.2563 0.2463 0.2419 0.0111  -0.0105 -0.0242 45  ARG A CB  
359  C CG  . ARG A 55  ? 0.2654 0.2474 0.2475 0.0111  -0.0124 -0.0231 45  ARG A CG  
360  C CD  . ARG A 55  ? 0.2816 0.2614 0.2611 0.0131  -0.0141 -0.0230 45  ARG A CD  
361  N NE  . ARG A 55  ? 0.2888 0.2608 0.2638 0.0135  -0.0166 -0.0224 45  ARG A NE  
362  C CZ  . ARG A 55  ? 0.3049 0.2729 0.2754 0.0160  -0.0194 -0.0235 45  ARG A CZ  
363  N NH1 . ARG A 55  ? 0.3115 0.2830 0.2814 0.0187  -0.0202 -0.0256 45  ARG A NH1 
364  N NH2 . ARG A 55  ? 0.3203 0.2805 0.2865 0.0156  -0.0216 -0.0225 45  ARG A NH2 
365  N N   . TYR A 56  ? 0.2303 0.2161 0.2187 0.0055  -0.0081 -0.0231 46  TYR A N   
366  C CA  . TYR A 56  ? 0.2228 0.2069 0.2137 0.0023  -0.0064 -0.0220 46  TYR A CA  
367  C C   . TYR A 56  ? 0.2246 0.2028 0.2130 0.0017  -0.0076 -0.0204 46  TYR A C   
368  O O   . TYR A 56  ? 0.2261 0.2006 0.2102 0.0027  -0.0099 -0.0205 46  TYR A O   
369  C CB  . TYR A 56  ? 0.2250 0.2112 0.2166 0.0015  -0.0058 -0.0233 46  TYR A CB  
370  C CG  . TYR A 56  ? 0.2209 0.2062 0.2150 -0.0013 -0.0042 -0.0228 46  TYR A CG  
371  C CD1 . TYR A 56  ? 0.2223 0.2070 0.2198 -0.0032 -0.0024 -0.0217 46  TYR A CD1 
372  C CD2 . TYR A 56  ? 0.2269 0.2122 0.2199 -0.0021 -0.0045 -0.0236 46  TYR A CD2 
373  C CE1 . TYR A 56  ? 0.2266 0.2109 0.2265 -0.0055 -0.0010 -0.0217 46  TYR A CE1 
374  C CE2 . TYR A 56  ? 0.2170 0.2024 0.2124 -0.0046 -0.0030 -0.0235 46  TYR A CE2 
375  C CZ  . TYR A 56  ? 0.2245 0.2094 0.2234 -0.0062 -0.0012 -0.0228 46  TYR A CZ  
376  O OH  . TYR A 56  ? 0.2363 0.2213 0.2375 -0.0083 0.0001  -0.0231 46  TYR A OH  
377  N N   . LEU A 57  ? 0.2140 0.1913 0.2048 0.0000  -0.0063 -0.0189 47  LEU A N   
378  C CA  . LEU A 57  ? 0.2193 0.1921 0.2082 -0.0010 -0.0072 -0.0174 47  LEU A CA  
379  C C   . LEU A 57  ? 0.2117 0.1843 0.2029 -0.0036 -0.0056 -0.0168 47  LEU A C   
380  O O   . LEU A 57  ? 0.2171 0.1926 0.2127 -0.0047 -0.0034 -0.0171 47  LEU A O   
381  C CB  . LEU A 57  ? 0.2176 0.1900 0.2072 -0.0006 -0.0070 -0.0161 47  LEU A CB  
382  C CG  . LEU A 57  ? 0.2253 0.1937 0.2128 -0.0017 -0.0079 -0.0145 47  LEU A CG  
383  C CD1 . LEU A 57  ? 0.2275 0.1913 0.2093 -0.0006 -0.0108 -0.0147 47  LEU A CD1 
384  C CD2 . LEU A 57  ? 0.2268 0.1961 0.2160 -0.0016 -0.0072 -0.0133 47  LEU A CD2 
385  N N   . THR A 58  ? 0.2155 0.1849 0.2039 -0.0047 -0.0069 -0.0160 48  THR A N   
386  C CA  . THR A 58  ? 0.2181 0.1877 0.2083 -0.0072 -0.0057 -0.0153 48  THR A CA  
387  C C   . THR A 58  ? 0.2222 0.1881 0.2087 -0.0081 -0.0074 -0.0138 48  THR A C   
388  O O   . THR A 58  ? 0.2302 0.1926 0.2126 -0.0068 -0.0096 -0.0133 48  THR A O   
389  C CB  . THR A 58  ? 0.2208 0.1922 0.2114 -0.0085 -0.0052 -0.0165 48  THR A CB  
390  O OG1 . THR A 58  ? 0.2358 0.2088 0.2291 -0.0107 -0.0037 -0.0164 48  THR A OG1 
391  C CG2 . THR A 58  ? 0.2296 0.1981 0.2148 -0.0085 -0.0077 -0.0163 48  THR A CG2 
392  N N   . GLY A 59  ? 0.2175 0.1840 0.2051 -0.0103 -0.0066 -0.0130 49  GLY A N   
393  C CA  . GLY A 59  ? 0.2300 0.1937 0.2141 -0.0118 -0.0082 -0.0116 49  GLY A CA  
394  C C   . GLY A 59  ? 0.2236 0.1897 0.2098 -0.0141 -0.0069 -0.0110 49  GLY A C   
395  O O   . GLY A 59  ? 0.2249 0.1947 0.2149 -0.0147 -0.0051 -0.0120 49  GLY A O   
396  N N   . THR A 60  ? 0.2291 0.1936 0.2131 -0.0153 -0.0079 -0.0095 50  THR A N   
397  C CA  . THR A 60  ? 0.2332 0.2005 0.2184 -0.0177 -0.0071 -0.0089 50  THR A CA  
398  C C   . THR A 60  ? 0.2272 0.1948 0.2132 -0.0177 -0.0069 -0.0076 50  THR A C   
399  O O   . THR A 60  ? 0.2255 0.1896 0.2084 -0.0171 -0.0085 -0.0067 50  THR A O   
400  C CB  . THR A 60  ? 0.2402 0.2063 0.2208 -0.0206 -0.0087 -0.0082 50  THR A CB  
401  O OG1 . THR A 60  ? 0.2543 0.2145 0.2291 -0.0206 -0.0115 -0.0072 50  THR A OG1 
402  C CG2 . THR A 60  ? 0.2464 0.2149 0.2278 -0.0213 -0.0082 -0.0095 50  THR A CG2 
403  N N   . ASP A 61  ? 0.2295 0.2015 0.2196 -0.0182 -0.0051 -0.0077 51  ASP A N   
404  C CA  . ASP A 61  ? 0.2384 0.2123 0.2304 -0.0181 -0.0045 -0.0067 51  ASP A CA  
405  C C   . ASP A 61  ? 0.2399 0.2158 0.2296 -0.0210 -0.0052 -0.0060 51  ASP A C   
406  O O   . ASP A 61  ? 0.2508 0.2309 0.2426 -0.0221 -0.0042 -0.0069 51  ASP A O   
407  C CB  . ASP A 61  ? 0.2434 0.2207 0.2415 -0.0164 -0.0022 -0.0076 51  ASP A CB  
408  C CG  . ASP A 61  ? 0.2548 0.2343 0.2557 -0.0157 -0.0015 -0.0065 51  ASP A CG  
409  O OD1 . ASP A 61  ? 0.2837 0.2627 0.2820 -0.0164 -0.0026 -0.0051 51  ASP A OD1 
410  O OD2 . ASP A 61  ? 0.2697 0.2512 0.2753 -0.0142 0.0000  -0.0070 51  ASP A OD2 
411  N N   . GLU A 62  ? 0.2396 0.2129 0.2250 -0.0225 -0.0069 -0.0046 52  GLU A N   
412  C CA  . GLU A 62  ? 0.2440 0.2181 0.2255 -0.0261 -0.0082 -0.0038 52  GLU A CA  
413  C C   . GLU A 62  ? 0.2434 0.2211 0.2251 -0.0277 -0.0080 -0.0028 52  GLU A C   
414  O O   . GLU A 62  ? 0.2502 0.2296 0.2289 -0.0312 -0.0089 -0.0021 52  GLU A O   
415  C CB  . GLU A 62  ? 0.2489 0.2162 0.2238 -0.0273 -0.0109 -0.0030 52  GLU A CB  
416  C CG  . GLU A 62  ? 0.2541 0.2188 0.2282 -0.0261 -0.0113 -0.0040 52  GLU A CG  
417  C CD  . GLU A 62  ? 0.2626 0.2205 0.2301 -0.0271 -0.0142 -0.0033 52  GLU A CD  
418  O OE1 . GLU A 62  ? 0.2745 0.2295 0.2373 -0.0297 -0.0161 -0.0020 52  GLU A OE1 
419  O OE2 . GLU A 62  ? 0.2733 0.2287 0.2402 -0.0252 -0.0147 -0.0042 52  GLU A OE2 
420  N N   . HIS A 63  ? 0.2390 0.2183 0.2242 -0.0255 -0.0070 -0.0025 53  HIS A N   
421  C CA  . HIS A 63  ? 0.2437 0.2267 0.2292 -0.0267 -0.0068 -0.0015 53  HIS A CA  
422  C C   . HIS A 63  ? 0.2439 0.2343 0.2348 -0.0261 -0.0049 -0.0022 53  HIS A C   
423  O O   . HIS A 63  ? 0.2379 0.2299 0.2323 -0.0246 -0.0035 -0.0037 53  HIS A O   
424  C CB  . HIS A 63  ? 0.2448 0.2254 0.2304 -0.0247 -0.0072 -0.0005 53  HIS A CB  
425  C CG  . HIS A 63  ? 0.2553 0.2293 0.2353 -0.0254 -0.0094 -0.0001 53  HIS A CG  
426  N ND1 . HIS A 63  ? 0.2615 0.2317 0.2416 -0.0226 -0.0097 -0.0003 53  HIS A ND1 
427  C CD2 . HIS A 63  ? 0.2676 0.2379 0.2417 -0.0284 -0.0116 0.0004  53  HIS A CD2 
428  C CE1 . HIS A 63  ? 0.2739 0.2385 0.2484 -0.0235 -0.0120 -0.0002 53  HIS A CE1 
429  N NE2 . HIS A 63  ? 0.2849 0.2488 0.2556 -0.0270 -0.0132 0.0003  53  HIS A NE2 
430  N N   . GLY A 64  ? 0.2492 0.2441 0.2403 -0.0273 -0.0048 -0.0015 54  GLY A N   
431  C CA  . GLY A 64  ? 0.2583 0.2604 0.2544 -0.0261 -0.0031 -0.0023 54  GLY A CA  
432  C C   . GLY A 64  ? 0.2762 0.2848 0.2713 -0.0293 -0.0032 -0.0029 54  GLY A C   
433  O O   . GLY A 64  ? 0.2677 0.2751 0.2585 -0.0327 -0.0043 -0.0027 54  GLY A O   
434  N N   . GLN A 65  ? 0.2986 0.3144 0.2979 -0.0280 -0.0020 -0.0035 55  GLN A N   
435  C CA  . GLN A 65  ? 0.3244 0.3485 0.3236 -0.0306 -0.0018 -0.0043 55  GLN A CA  
436  C C   . GLN A 65  ? 0.3303 0.3563 0.3292 -0.0322 -0.0015 -0.0060 55  GLN A C   
437  O O   . GLN A 65  ? 0.3226 0.3523 0.3180 -0.0363 -0.0022 -0.0058 55  GLN A O   
438  C CB  . GLN A 65  ? 0.3544 0.3859 0.3590 -0.0277 -0.0004 -0.0052 55  GLN A CB  
439  C CG  . GLN A 65  ? 0.3906 0.4228 0.3950 -0.0271 -0.0009 -0.0035 55  GLN A CG  
440  C CD  . GLN A 65  ? 0.4082 0.4484 0.4177 -0.0243 0.0001  -0.0043 55  GLN A CD  
441  O OE1 . GLN A 65  ? 0.4535 0.5014 0.4623 -0.0262 0.0000  -0.0043 55  GLN A OE1 
442  N NE2 . GLN A 65  ? 0.4302 0.4687 0.4447 -0.0197 0.0011  -0.0050 55  GLN A NE2 
443  N N   . LYS A 66  ? 0.3298 0.3535 0.3321 -0.0292 -0.0004 -0.0075 56  LYS A N   
444  C CA  . LYS A 66  ? 0.3471 0.3735 0.3497 -0.0304 0.0000  -0.0094 56  LYS A CA  
445  C C   . LYS A 66  ? 0.3425 0.3648 0.3389 -0.0344 -0.0016 -0.0082 56  LYS A C   
446  O O   . LYS A 66  ? 0.3324 0.3594 0.3270 -0.0376 -0.0018 -0.0088 56  LYS A O   
447  C CB  . LYS A 66  ? 0.3652 0.3892 0.3725 -0.0265 0.0013  -0.0113 56  LYS A CB  
448  C CG  . LYS A 66  ? 0.3989 0.4260 0.4070 -0.0274 0.0019  -0.0136 56  LYS A CG  
449  C CD  . LYS A 66  ? 0.4258 0.4631 0.4359 -0.0283 0.0026  -0.0155 56  LYS A CD  
450  C CE  . LYS A 66  ? 0.4575 0.4984 0.4701 -0.0280 0.0036  -0.0185 56  LYS A CE  
451  N NZ  . LYS A 66  ? 0.4681 0.5200 0.4832 -0.0283 0.0044  -0.0207 56  LYS A NZ  
452  N N   . ILE A 67  ? 0.3251 0.3387 0.3182 -0.0343 -0.0028 -0.0066 57  ILE A N   
453  C CA  . ILE A 67  ? 0.3353 0.3438 0.3221 -0.0377 -0.0047 -0.0053 57  ILE A CA  
454  C C   . ILE A 67  ? 0.3355 0.3466 0.3175 -0.0424 -0.0062 -0.0037 57  ILE A C   
455  O O   . ILE A 67  ? 0.3354 0.3474 0.3135 -0.0462 -0.0072 -0.0033 57  ILE A O   
456  C CB  . ILE A 67  ? 0.3372 0.3361 0.3215 -0.0359 -0.0059 -0.0041 57  ILE A CB  
457  C CG1 . ILE A 67  ? 0.3383 0.3348 0.3267 -0.0319 -0.0046 -0.0056 57  ILE A CG1 
458  C CG2 . ILE A 67  ? 0.3384 0.3313 0.3157 -0.0391 -0.0084 -0.0027 57  ILE A CG2 
459  C CD1 . ILE A 67  ? 0.3400 0.3383 0.3292 -0.0324 -0.0041 -0.0072 57  ILE A CD1 
460  N N   . GLN A 68  ? 0.3337 0.3465 0.3159 -0.0424 -0.0063 -0.0027 58  GLN A N   
461  C CA  . GLN A 68  ? 0.3419 0.3578 0.3197 -0.0472 -0.0075 -0.0013 58  GLN A CA  
462  C C   . GLN A 68  ? 0.3443 0.3703 0.3231 -0.0500 -0.0068 -0.0024 58  GLN A C   
463  O O   . GLN A 68  ? 0.3416 0.3688 0.3154 -0.0551 -0.0081 -0.0013 58  GLN A O   
464  C CB  . GLN A 68  ? 0.3483 0.3659 0.3273 -0.0462 -0.0074 -0.0005 58  GLN A CB  
465  C CG  . GLN A 68  ? 0.3577 0.3798 0.3326 -0.0512 -0.0085 0.0007  58  GLN A CG  
466  C CD  . GLN A 68  ? 0.3642 0.3987 0.3426 -0.0522 -0.0071 -0.0004 58  GLN A CD  
467  O OE1 . GLN A 68  ? 0.3811 0.4209 0.3656 -0.0480 -0.0053 -0.0020 58  GLN A OE1 
468  N NE2 . GLN A 68  ? 0.3922 0.4314 0.3664 -0.0577 -0.0080 0.0001  58  GLN A NE2 
469  N N   . GLU A 69  ? 0.3432 0.3764 0.3285 -0.0467 -0.0046 -0.0046 59  GLU A N   
470  C CA  . GLU A 69  ? 0.3712 0.4151 0.3583 -0.0485 -0.0037 -0.0063 59  GLU A CA  
471  C C   . GLU A 69  ? 0.3628 0.4060 0.3471 -0.0513 -0.0042 -0.0067 59  GLU A C   
472  O O   . GLU A 69  ? 0.3511 0.4008 0.3325 -0.0559 -0.0047 -0.0065 59  GLU A O   
473  C CB  . GLU A 69  ? 0.3992 0.4491 0.3938 -0.0435 -0.0015 -0.0090 59  GLU A CB  
474  C CG  . GLU A 69  ? 0.4439 0.4992 0.4412 -0.0418 -0.0010 -0.0089 59  GLU A CG  
475  C CD  . GLU A 69  ? 0.4752 0.5333 0.4797 -0.0359 0.0006  -0.0111 59  GLU A CD  
476  O OE1 . GLU A 69  ? 0.5256 0.5836 0.5333 -0.0337 0.0016  -0.0133 59  GLU A OE1 
477  O OE2 . GLU A 69  ? 0.5010 0.5610 0.5079 -0.0335 0.0009  -0.0106 59  GLU A OE2 
478  N N   . LYS A 70  ? 0.3423 0.3782 0.3273 -0.0487 -0.0041 -0.0071 60  LYS A N   
479  C CA  . LYS A 70  ? 0.3486 0.3834 0.3311 -0.0508 -0.0047 -0.0074 60  LYS A CA  
480  C C   . LYS A 70  ? 0.3420 0.3722 0.3165 -0.0562 -0.0072 -0.0046 60  LYS A C   
481  O O   . LYS A 70  ? 0.3421 0.3765 0.3138 -0.0604 -0.0078 -0.0044 60  LYS A O   
482  C CB  . LYS A 70  ? 0.3553 0.3829 0.3399 -0.0468 -0.0042 -0.0084 60  LYS A CB  
483  C CG  . LYS A 70  ? 0.3740 0.4063 0.3659 -0.0424 -0.0018 -0.0115 60  LYS A CG  
484  C CD  . LYS A 70  ? 0.3887 0.4294 0.3821 -0.0439 -0.0009 -0.0137 60  LYS A CD  
485  C CE  . LYS A 70  ? 0.4026 0.4480 0.4032 -0.0395 0.0012  -0.0171 60  LYS A CE  
486  N NZ  . LYS A 70  ? 0.4159 0.4698 0.4180 -0.0408 0.0020  -0.0197 60  LYS A NZ  
487  N N   . ALA A 71  ? 0.3324 0.3540 0.3034 -0.0563 -0.0088 -0.0025 61  ALA A N   
488  C CA  . ALA A 71  ? 0.3433 0.3589 0.3065 -0.0611 -0.0115 0.0001  61  ALA A CA  
489  C C   . ALA A 71  ? 0.3523 0.3760 0.3127 -0.0667 -0.0120 0.0010  61  ALA A C   
490  O O   . ALA A 71  ? 0.3594 0.3837 0.3148 -0.0717 -0.0135 0.0024  61  ALA A O   
491  C CB  . ALA A 71  ? 0.3484 0.3541 0.3090 -0.0594 -0.0129 0.0015  61  ALA A CB  
492  N N   . GLN A 72  ? 0.3686 0.3988 0.3323 -0.0660 -0.0108 0.0005  62  GLN A N   
493  C CA  . GLN A 72  ? 0.3818 0.4211 0.3433 -0.0712 -0.0111 0.0012  62  GLN A CA  
494  C C   . GLN A 72  ? 0.3999 0.4499 0.3626 -0.0737 -0.0102 -0.0002 62  GLN A C   
495  O O   . GLN A 72  ? 0.3993 0.4532 0.3571 -0.0799 -0.0114 0.0012  62  GLN A O   
496  C CB  . GLN A 72  ? 0.3879 0.4334 0.3535 -0.0690 -0.0098 0.0004  62  GLN A CB  
497  C CG  . GLN A 72  ? 0.4038 0.4585 0.3667 -0.0745 -0.0103 0.0013  62  GLN A CG  
498  C CD  . GLN A 72  ? 0.4207 0.4824 0.3881 -0.0718 -0.0089 0.0004  62  GLN A CD  
499  O OE1 . GLN A 72  ? 0.4381 0.5044 0.4123 -0.0664 -0.0069 -0.0018 62  GLN A OE1 
500  N NE2 . GLN A 72  ? 0.4151 0.4775 0.3786 -0.0757 -0.0102 0.0022  62  GLN A NE2 
501  N N   . LYS A 73  ? 0.4063 0.4609 0.3754 -0.0691 -0.0080 -0.0030 63  LYS A N   
502  C CA  . LYS A 73  ? 0.4340 0.4988 0.4048 -0.0709 -0.0070 -0.0049 63  LYS A CA  
503  C C   . LYS A 73  ? 0.4398 0.5003 0.4045 -0.0755 -0.0088 -0.0031 63  LYS A C   
504  O O   . LYS A 73  ? 0.4473 0.5162 0.4097 -0.0804 -0.0091 -0.0029 63  LYS A O   
505  C CB  . LYS A 73  ? 0.4552 0.5232 0.4336 -0.0648 -0.0046 -0.0084 63  LYS A CB  
506  C CG  . LYS A 73  ? 0.4838 0.5631 0.4644 -0.0661 -0.0034 -0.0110 63  LYS A CG  
507  C CD  . LYS A 73  ? 0.5004 0.5848 0.4890 -0.0600 -0.0010 -0.0150 63  LYS A CD  
508  C CE  . LYS A 73  ? 0.5230 0.6186 0.5137 -0.0613 0.0000  -0.0178 63  LYS A CE  
509  N NZ  . LYS A 73  ? 0.5390 0.6474 0.5278 -0.0662 -0.0002 -0.0178 63  LYS A NZ  
510  N N   . ALA A 74  ? 0.4372 0.4849 0.3990 -0.0740 -0.0102 -0.0016 64  ALA A N   
511  C CA  . ALA A 74  ? 0.4425 0.4842 0.3983 -0.0776 -0.0123 0.0003  64  ALA A CA  
512  C C   . ALA A 74  ? 0.4515 0.4884 0.3988 -0.0841 -0.0152 0.0039  64  ALA A C   
513  O O   . ALA A 74  ? 0.4511 0.4824 0.3926 -0.0875 -0.0174 0.0060  64  ALA A O   
514  C CB  . ALA A 74  ? 0.4441 0.4746 0.4004 -0.0730 -0.0126 0.0001  64  ALA A CB  
515  N N   . GLY A 75  ? 0.4488 0.4872 0.3949 -0.0859 -0.0156 0.0049  65  GLY A N   
516  C CA  . GLY A 75  ? 0.4559 0.4889 0.3939 -0.0922 -0.0185 0.0083  65  GLY A CA  
517  C C   . GLY A 75  ? 0.4574 0.4742 0.3904 -0.0910 -0.0211 0.0103  65  GLY A C   
518  O O   . GLY A 75  ? 0.4530 0.4627 0.3782 -0.0960 -0.0240 0.0132  65  GLY A O   
519  N N   . LYS A 76  ? 0.4364 0.4476 0.3738 -0.0842 -0.0200 0.0087  66  LYS A N   
520  C CA  . LYS A 76  ? 0.4331 0.4301 0.3669 -0.0818 -0.0221 0.0098  66  LYS A CA  
521  C C   . LYS A 76  ? 0.4018 0.3955 0.3381 -0.0780 -0.0216 0.0092  66  LYS A C   
522  O O   . LYS A 76  ? 0.3837 0.3856 0.3262 -0.0754 -0.0190 0.0075  66  LYS A O   
523  C CB  . LYS A 76  ? 0.4450 0.4384 0.3815 -0.0771 -0.0214 0.0084  66  LYS A CB  
524  C CG  . LYS A 76  ? 0.4646 0.4603 0.3981 -0.0807 -0.0223 0.0092  66  LYS A CG  
525  C CD  . LYS A 76  ? 0.4763 0.4704 0.4134 -0.0759 -0.0212 0.0074  66  LYS A CD  
526  C CE  . LYS A 76  ? 0.4884 0.4863 0.4228 -0.0797 -0.0219 0.0081  66  LYS A CE  
527  N NZ  . LYS A 76  ? 0.4995 0.5008 0.4394 -0.0754 -0.0198 0.0056  66  LYS A NZ  
528  N N   . THR A 77  ? 0.3879 0.3697 0.3193 -0.0776 -0.0240 0.0106  67  THR A N   
529  C CA  . THR A 77  ? 0.3757 0.3536 0.3094 -0.0735 -0.0236 0.0099  67  THR A CA  
530  C C   . THR A 77  ? 0.3594 0.3375 0.2998 -0.0666 -0.0214 0.0076  67  THR A C   
531  O O   . THR A 77  ? 0.3383 0.3164 0.2799 -0.0652 -0.0209 0.0069  67  THR A O   
532  C CB  . THR A 77  ? 0.3915 0.3566 0.3184 -0.0743 -0.0269 0.0115  67  THR A CB  
533  O OG1 . THR A 77  ? 0.4014 0.3574 0.3261 -0.0716 -0.0284 0.0114  67  THR A OG1 
534  C CG2 . THR A 77  ? 0.4012 0.3645 0.3204 -0.0818 -0.0295 0.0139  67  THR A CG2 
535  N N   . GLU A 78  ? 0.3398 0.3180 0.2841 -0.0627 -0.0201 0.0067  68  GLU A N   
536  C CA  . GLU A 78  ? 0.3360 0.3144 0.2865 -0.0566 -0.0181 0.0047  68  GLU A CA  
537  C C   . GLU A 78  ? 0.3293 0.2984 0.2771 -0.0543 -0.0197 0.0047  68  GLU A C   
538  O O   . GLU A 78  ? 0.3104 0.2809 0.2614 -0.0518 -0.0184 0.0034  68  GLU A O   
539  C CB  . GLU A 78  ? 0.3390 0.3181 0.2932 -0.0533 -0.0170 0.0042  68  GLU A CB  
540  C CG  . GLU A 78  ? 0.3477 0.3373 0.3064 -0.0538 -0.0149 0.0037  68  GLU A CG  
541  C CD  . GLU A 78  ? 0.3649 0.3582 0.3193 -0.0595 -0.0161 0.0052  68  GLU A CD  
542  O OE1 . GLU A 78  ? 0.3596 0.3459 0.3072 -0.0631 -0.0187 0.0068  68  GLU A OE1 
543  O OE2 . GLU A 78  ? 0.3943 0.3978 0.3522 -0.0605 -0.0144 0.0046  68  GLU A OE2 
544  N N   . ILE A 79  ? 0.3390 0.2987 0.2808 -0.0552 -0.0225 0.0060  69  ILE A N   
545  C CA  . ILE A 79  ? 0.3548 0.3056 0.2939 -0.0525 -0.0243 0.0058  69  ILE A CA  
546  C C   . ILE A 79  ? 0.3640 0.3133 0.2996 -0.0550 -0.0255 0.0065  69  ILE A C   
547  O O   . ILE A 79  ? 0.3598 0.3062 0.2962 -0.0519 -0.0257 0.0057  69  ILE A O   
548  C CB  . ILE A 79  ? 0.3717 0.3126 0.3058 -0.0517 -0.0270 0.0064  69  ILE A CB  
549  C CG1 . ILE A 79  ? 0.3757 0.3100 0.3098 -0.0466 -0.0278 0.0052  69  ILE A CG1 
550  C CG2 . ILE A 79  ? 0.3824 0.3173 0.3083 -0.0571 -0.0303 0.0085  69  ILE A CG2 
551  C CD1 . ILE A 79  ? 0.3757 0.3148 0.3172 -0.0414 -0.0249 0.0033  69  ILE A CD1 
552  N N   A GLU A 80  ? 0.3679 0.3199 0.2998 -0.0607 -0.0265 0.0082  70  GLU A N   
553  N N   B GLU A 80  ? 0.3667 0.3186 0.2986 -0.0607 -0.0265 0.0082  70  GLU A N   
554  C CA  A GLU A 80  ? 0.3755 0.3280 0.3042 -0.0639 -0.0275 0.0092  70  GLU A CA  
555  C CA  B GLU A 80  ? 0.3732 0.3255 0.3021 -0.0637 -0.0275 0.0091  70  GLU A CA  
556  C C   A GLU A 80  ? 0.3609 0.3217 0.2962 -0.0614 -0.0245 0.0071  70  GLU A C   
557  C C   B GLU A 80  ? 0.3596 0.3204 0.2950 -0.0613 -0.0245 0.0071  70  GLU A C   
558  O O   A GLU A 80  ? 0.3629 0.3213 0.2976 -0.0599 -0.0250 0.0068  70  GLU A O   
559  O O   B GLU A 80  ? 0.3611 0.3197 0.2961 -0.0599 -0.0249 0.0068  70  GLU A O   
560  C CB  A GLU A 80  ? 0.3904 0.3467 0.3149 -0.0709 -0.0285 0.0112  70  GLU A CB  
561  C CB  B GLU A 80  ? 0.3871 0.3424 0.3111 -0.0708 -0.0288 0.0113  70  GLU A CB  
562  C CG  A GLU A 80  ? 0.4008 0.3585 0.3215 -0.0752 -0.0298 0.0126  70  GLU A CG  
563  C CG  B GLU A 80  ? 0.4011 0.3455 0.3164 -0.0743 -0.0328 0.0137  70  GLU A CG  
564  C CD  A GLU A 80  ? 0.4149 0.3767 0.3309 -0.0826 -0.0309 0.0148  70  GLU A CD  
565  C CD  B GLU A 80  ? 0.4124 0.3605 0.3232 -0.0818 -0.0338 0.0159  70  GLU A CD  
566  O OE1 A GLU A 80  ? 0.4214 0.3835 0.3330 -0.0871 -0.0324 0.0166  70  GLU A OE1 
567  O OE1 B GLU A 80  ? 0.4043 0.3644 0.3194 -0.0836 -0.0312 0.0151  70  GLU A OE1 
568  O OE2 A GLU A 80  ? 0.4117 0.3767 0.3284 -0.0842 -0.0303 0.0148  70  GLU A OE2 
569  O OE2 B GLU A 80  ? 0.4283 0.3674 0.3311 -0.0858 -0.0374 0.0183  70  GLU A OE2 
570  N N   . TYR A 81  ? 0.3466 0.3172 0.2882 -0.0607 -0.0216 0.0057  71  TYR A N   
571  C CA  . TYR A 81  ? 0.3315 0.3101 0.2800 -0.0580 -0.0186 0.0033  71  TYR A CA  
572  C C   . TYR A 81  ? 0.3187 0.2927 0.2703 -0.0522 -0.0179 0.0018  71  TYR A C   
573  O O   . TYR A 81  ? 0.3132 0.2881 0.2662 -0.0510 -0.0174 0.0008  71  TYR A O   
574  C CB  . TYR A 81  ? 0.3226 0.3108 0.2769 -0.0574 -0.0159 0.0020  71  TYR A CB  
575  C CG  . TYR A 81  ? 0.3192 0.3143 0.2810 -0.0537 -0.0129 -0.0006 71  TYR A CG  
576  C CD1 . TYR A 81  ? 0.3175 0.3206 0.2811 -0.0555 -0.0118 -0.0018 71  TYR A CD1 
577  C CD2 . TYR A 81  ? 0.3124 0.3056 0.2792 -0.0484 -0.0114 -0.0021 71  TYR A CD2 
578  C CE1 . TYR A 81  ? 0.3136 0.3222 0.2837 -0.0521 -0.0093 -0.0046 71  TYR A CE1 
579  C CE2 . TYR A 81  ? 0.3066 0.3049 0.2798 -0.0452 -0.0089 -0.0045 71  TYR A CE2 
580  C CZ  . TYR A 81  ? 0.3115 0.3172 0.2864 -0.0469 -0.0079 -0.0059 71  TYR A CZ  
581  O OH  . TYR A 81  ? 0.3087 0.3189 0.2898 -0.0437 -0.0056 -0.0086 71  TYR A OH  
582  N N   . LEU A 82  ? 0.3115 0.2809 0.2641 -0.0491 -0.0179 0.0016  72  LEU A N   
583  C CA  . LEU A 82  ? 0.3057 0.2716 0.2615 -0.0438 -0.0172 0.0002  72  LEU A CA  
584  C C   . LEU A 82  ? 0.3138 0.2722 0.2651 -0.0430 -0.0194 0.0006  72  LEU A C   
585  O O   . LEU A 82  ? 0.3066 0.2658 0.2608 -0.0400 -0.0184 -0.0008 72  LEU A O   
586  C CB  . LEU A 82  ? 0.3015 0.2646 0.2588 -0.0410 -0.0170 0.0001  72  LEU A CB  
587  C CG  . LEU A 82  ? 0.2958 0.2664 0.2590 -0.0401 -0.0143 -0.0006 72  LEU A CG  
588  C CD1 . LEU A 82  ? 0.2957 0.2634 0.2584 -0.0389 -0.0149 0.0000  72  LEU A CD1 
589  C CD2 . LEU A 82  ? 0.2903 0.2652 0.2602 -0.0365 -0.0117 -0.0026 72  LEU A CD2 
590  N N   . ASP A 83  ? 0.3348 0.2861 0.2791 -0.0455 -0.0226 0.0025  73  ASP A N   
591  C CA  . ASP A 83  ? 0.3519 0.2955 0.2914 -0.0445 -0.0252 0.0030  73  ASP A CA  
592  C C   . ASP A 83  ? 0.3556 0.3033 0.2956 -0.0457 -0.0247 0.0028  73  ASP A C   
593  O O   . ASP A 83  ? 0.3531 0.2984 0.2934 -0.0427 -0.0250 0.0019  73  ASP A O   
594  C CB  . ASP A 83  ? 0.3665 0.3012 0.2977 -0.0475 -0.0290 0.0053  73  ASP A CB  
595  C CG  . ASP A 83  ? 0.3717 0.3006 0.3017 -0.0453 -0.0301 0.0051  73  ASP A CG  
596  O OD1 . ASP A 83  ? 0.3589 0.2898 0.2939 -0.0410 -0.0282 0.0034  73  ASP A OD1 
597  O OD2 . ASP A 83  ? 0.3811 0.3034 0.3048 -0.0483 -0.0329 0.0068  73  ASP A OD2 
598  N N   . GLU A 84  ? 0.3616 0.3162 0.3021 -0.0499 -0.0237 0.0033  74  GLU A N   
599  C CA  . GLU A 84  ? 0.3767 0.3367 0.3181 -0.0514 -0.0230 0.0029  74  GLU A CA  
600  C C   . GLU A 84  ? 0.3452 0.3111 0.2941 -0.0473 -0.0198 0.0000  74  GLU A C   
601  O O   . GLU A 84  ? 0.3505 0.3164 0.2998 -0.0458 -0.0198 -0.0007 74  GLU A O   
602  C CB  . GLU A 84  ? 0.4119 0.3791 0.3523 -0.0570 -0.0226 0.0039  74  GLU A CB  
603  C CG  . GLU A 84  ? 0.4572 0.4184 0.3889 -0.0621 -0.0261 0.0071  74  GLU A CG  
604  C CD  . GLU A 84  ? 0.4931 0.4620 0.4235 -0.0681 -0.0258 0.0083  74  GLU A CD  
605  O OE1 . GLU A 84  ? 0.5407 0.5048 0.4639 -0.0729 -0.0287 0.0111  74  GLU A OE1 
606  O OE2 . GLU A 84  ? 0.5088 0.4884 0.4451 -0.0681 -0.0228 0.0064  74  GLU A OE2 
607  N N   . MET A 85  ? 0.3233 0.2943 0.2781 -0.0456 -0.0172 -0.0014 75  MET A N   
608  C CA  . MET A 85  ? 0.3107 0.2867 0.2726 -0.0419 -0.0142 -0.0041 75  MET A CA  
609  C C   . MET A 85  ? 0.2988 0.2690 0.2610 -0.0377 -0.0147 -0.0049 75  MET A C   
610  O O   . MET A 85  ? 0.2888 0.2612 0.2537 -0.0358 -0.0136 -0.0065 75  MET A O   
611  C CB  . MET A 85  ? 0.3083 0.2887 0.2756 -0.0405 -0.0120 -0.0052 75  MET A CB  
612  C CG  . MET A 85  ? 0.3139 0.3024 0.2825 -0.0437 -0.0109 -0.0052 75  MET A CG  
613  S SD  . MET A 85  ? 0.3281 0.3252 0.2988 -0.0457 -0.0095 -0.0070 75  MET A SD  
614  C CE  . MET A 85  ? 0.3217 0.3215 0.3005 -0.0406 -0.0066 -0.0103 75  MET A CE  
615  N N   . ILE A 86  ? 0.2919 0.2550 0.2511 -0.0362 -0.0164 -0.0038 76  ILE A N   
616  C CA  . ILE A 86  ? 0.2913 0.2495 0.2506 -0.0320 -0.0170 -0.0046 76  ILE A CA  
617  C C   . ILE A 86  ? 0.2954 0.2501 0.2506 -0.0319 -0.0191 -0.0043 76  ILE A C   
618  O O   . ILE A 86  ? 0.2843 0.2393 0.2416 -0.0288 -0.0185 -0.0058 76  ILE A O   
619  C CB  . ILE A 86  ? 0.2887 0.2412 0.2461 -0.0303 -0.0183 -0.0038 76  ILE A CB  
620  C CG1 . ILE A 86  ? 0.2821 0.2386 0.2457 -0.0280 -0.0157 -0.0050 76  ILE A CG1 
621  C CG2 . ILE A 86  ? 0.2974 0.2433 0.2517 -0.0270 -0.0204 -0.0042 76  ILE A CG2 
622  C CD1 . ILE A 86  ? 0.2765 0.2400 0.2440 -0.0301 -0.0135 -0.0051 76  ILE A CD1 
623  N N   . ALA A 87  ? 0.3147 0.2661 0.2639 -0.0354 -0.0216 -0.0023 77  ALA A N   
624  C CA  . ALA A 87  ? 0.3284 0.2765 0.2734 -0.0354 -0.0237 -0.0017 77  ALA A CA  
625  C C   . ALA A 87  ? 0.3248 0.2806 0.2743 -0.0351 -0.0214 -0.0035 77  ALA A C   
626  O O   . ALA A 87  ? 0.3222 0.2771 0.2719 -0.0324 -0.0217 -0.0045 77  ALA A O   
627  C CB  . ALA A 87  ? 0.3395 0.2836 0.2774 -0.0401 -0.0267 0.0010  77  ALA A CB  
628  N N   . GLY A 88  ? 0.3118 0.2754 0.2652 -0.0376 -0.0190 -0.0042 78  GLY A N   
629  C CA  . GLY A 88  ? 0.2995 0.2708 0.2576 -0.0374 -0.0165 -0.0063 78  GLY A CA  
630  C C   . GLY A 88  ? 0.2899 0.2627 0.2538 -0.0330 -0.0143 -0.0089 78  GLY A C   
631  O O   . GLY A 88  ? 0.2880 0.2637 0.2539 -0.0318 -0.0134 -0.0105 78  GLY A O   
632  N N   . ILE A 89  ? 0.2804 0.2517 0.2470 -0.0309 -0.0134 -0.0092 79  ILE A N   
633  C CA  . ILE A 89  ? 0.2722 0.2447 0.2440 -0.0271 -0.0114 -0.0113 79  ILE A CA  
634  C C   . ILE A 89  ? 0.2831 0.2510 0.2523 -0.0243 -0.0130 -0.0114 79  ILE A C   
635  O O   . ILE A 89  ? 0.2862 0.2569 0.2584 -0.0225 -0.0118 -0.0132 79  ILE A O   
636  C CB  . ILE A 89  ? 0.2689 0.2410 0.2439 -0.0258 -0.0102 -0.0113 79  ILE A CB  
637  C CG1 . ILE A 89  ? 0.2631 0.2413 0.2419 -0.0278 -0.0081 -0.0119 79  ILE A CG1 
638  C CG2 . ILE A 89  ? 0.2678 0.2399 0.2470 -0.0222 -0.0087 -0.0128 79  ILE A CG2 
639  C CD1 . ILE A 89  ? 0.2665 0.2445 0.2472 -0.0273 -0.0074 -0.0112 79  ILE A CD1 
640  N N   . LYS A 90  ? 0.2948 0.2559 0.2585 -0.0240 -0.0159 -0.0097 80  LYS A N   
641  C CA  . LYS A 90  ? 0.3115 0.2682 0.2723 -0.0209 -0.0179 -0.0099 80  LYS A CA  
642  C C   . LYS A 90  ? 0.3156 0.2739 0.2746 -0.0215 -0.0187 -0.0102 80  LYS A C   
643  O O   . LYS A 90  ? 0.3178 0.2768 0.2776 -0.0186 -0.0187 -0.0116 80  LYS A O   
644  C CB  . LYS A 90  ? 0.3317 0.2803 0.2864 -0.0205 -0.0212 -0.0081 80  LYS A CB  
645  C CG  . LYS A 90  ? 0.3438 0.2910 0.3005 -0.0189 -0.0205 -0.0082 80  LYS A CG  
646  C CD  . LYS A 90  ? 0.3651 0.3041 0.3158 -0.0180 -0.0238 -0.0070 80  LYS A CD  
647  C CE  . LYS A 90  ? 0.3854 0.3240 0.3385 -0.0159 -0.0229 -0.0076 80  LYS A CE  
648  N NZ  . LYS A 90  ? 0.4104 0.3416 0.3581 -0.0156 -0.0259 -0.0066 80  LYS A NZ  
649  N N   . GLN A 91  ? 0.3227 0.2822 0.2791 -0.0253 -0.0194 -0.0088 81  GLN A N   
650  C CA  . GLN A 91  ? 0.3341 0.2963 0.2891 -0.0264 -0.0199 -0.0090 81  GLN A CA  
651  C C   . GLN A 91  ? 0.3116 0.2815 0.2730 -0.0253 -0.0167 -0.0118 81  GLN A C   
652  O O   . GLN A 91  ? 0.3167 0.2882 0.2782 -0.0237 -0.0169 -0.0128 81  GLN A O   
653  C CB  . GLN A 91  ? 0.3601 0.3236 0.3117 -0.0313 -0.0209 -0.0070 81  GLN A CB  
654  C CG  . GLN A 91  ? 0.3985 0.3534 0.3420 -0.0327 -0.0249 -0.0039 81  GLN A CG  
655  C CD  . GLN A 91  ? 0.4388 0.3941 0.3792 -0.0380 -0.0257 -0.0017 81  GLN A CD  
656  O OE1 . GLN A 91  ? 0.4612 0.4244 0.4046 -0.0410 -0.0235 -0.0022 81  GLN A OE1 
657  N NE2 . GLN A 91  ? 0.4629 0.4098 0.3971 -0.0392 -0.0288 0.0007  81  GLN A NE2 
658  N N   . LEU A 92  ? 0.2942 0.2688 0.2610 -0.0260 -0.0138 -0.0131 82  LEU A N   
659  C CA  . LEU A 92  ? 0.2856 0.2667 0.2586 -0.0251 -0.0108 -0.0159 82  LEU A CA  
660  C C   . LEU A 92  ? 0.2766 0.2564 0.2515 -0.0213 -0.0104 -0.0173 82  LEU A C   
661  O O   . LEU A 92  ? 0.2759 0.2594 0.2526 -0.0205 -0.0095 -0.0191 82  LEU A O   
662  C CB  . LEU A 92  ? 0.2848 0.2699 0.2629 -0.0261 -0.0082 -0.0170 82  LEU A CB  
663  C CG  . LEU A 92  ? 0.2764 0.2670 0.2609 -0.0249 -0.0052 -0.0200 82  LEU A CG  
664  C CD1 . LEU A 92  ? 0.2843 0.2802 0.2693 -0.0264 -0.0047 -0.0215 82  LEU A CD1 
665  C CD2 . LEU A 92  ? 0.2756 0.2688 0.2646 -0.0254 -0.0032 -0.0208 82  LEU A CD2 
666  N N   . TRP A 93  ? 0.2727 0.2481 0.2472 -0.0191 -0.0110 -0.0167 83  TRP A N   
667  C CA  . TRP A 93  ? 0.2684 0.2434 0.2445 -0.0157 -0.0108 -0.0179 83  TRP A CA  
668  C C   . TRP A 93  ? 0.2797 0.2530 0.2517 -0.0140 -0.0131 -0.0179 83  TRP A C   
669  O O   . TRP A 93  ? 0.2814 0.2580 0.2555 -0.0121 -0.0123 -0.0197 83  TRP A O   
670  C CB  . TRP A 93  ? 0.2652 0.2366 0.2416 -0.0138 -0.0110 -0.0173 83  TRP A CB  
671  C CG  . TRP A 93  ? 0.2553 0.2282 0.2358 -0.0150 -0.0088 -0.0172 83  TRP A CG  
672  C CD1 . TRP A 93  ? 0.2605 0.2302 0.2402 -0.0147 -0.0093 -0.0159 83  TRP A CD1 
673  C CD2 . TRP A 93  ? 0.2524 0.2304 0.2382 -0.0164 -0.0060 -0.0186 83  TRP A CD2 
674  N NE1 . TRP A 93  ? 0.2549 0.2274 0.2391 -0.0157 -0.0071 -0.0161 83  TRP A NE1 
675  C CE2 . TRP A 93  ? 0.2515 0.2288 0.2394 -0.0166 -0.0051 -0.0178 83  TRP A CE2 
676  C CE3 . TRP A 93  ? 0.2516 0.2345 0.2405 -0.0173 -0.0043 -0.0205 83  TRP A CE3 
677  C CZ2 . TRP A 93  ? 0.2496 0.2307 0.2425 -0.0175 -0.0027 -0.0189 83  TRP A CZ2 
678  C CZ3 . TRP A 93  ? 0.2564 0.2429 0.2503 -0.0183 -0.0019 -0.0218 83  TRP A CZ3 
679  C CH2 . TRP A 93  ? 0.2598 0.2452 0.2556 -0.0183 -0.0012 -0.0209 83  TRP A CH2 
680  N N   . ALA A 94  ? 0.2913 0.2597 0.2573 -0.0147 -0.0161 -0.0159 84  ALA A N   
681  C CA  . ALA A 94  ? 0.3147 0.2813 0.2765 -0.0130 -0.0186 -0.0157 84  ALA A CA  
682  C C   . ALA A 94  ? 0.3148 0.2877 0.2784 -0.0144 -0.0173 -0.0169 84  ALA A C   
683  O O   . ALA A 94  ? 0.3179 0.2929 0.2815 -0.0121 -0.0177 -0.0182 84  ALA A O   
684  C CB  . ALA A 94  ? 0.3268 0.2860 0.2815 -0.0140 -0.0222 -0.0130 84  ALA A CB  
685  N N   . LYS A 95  ? 0.3137 0.2904 0.2790 -0.0180 -0.0158 -0.0168 85  LYS A N   
686  C CA  . LYS A 95  ? 0.3208 0.3040 0.2880 -0.0196 -0.0145 -0.0181 85  LYS A CA  
687  C C   . LYS A 95  ? 0.3046 0.2936 0.2779 -0.0181 -0.0115 -0.0213 85  LYS A C   
688  O O   . LYS A 95  ? 0.2988 0.2923 0.2729 -0.0178 -0.0111 -0.0227 85  LYS A O   
689  C CB  . LYS A 95  ? 0.3463 0.3327 0.3139 -0.0238 -0.0136 -0.0175 85  LYS A CB  
690  C CG  . LYS A 95  ? 0.3738 0.3671 0.3425 -0.0256 -0.0127 -0.0188 85  LYS A CG  
691  C CD  . LYS A 95  ? 0.3990 0.3970 0.3688 -0.0296 -0.0115 -0.0187 85  LYS A CD  
692  C CE  . LYS A 95  ? 0.4296 0.4248 0.3929 -0.0326 -0.0143 -0.0155 85  LYS A CE  
693  N NZ  . LYS A 95  ? 0.4481 0.4501 0.4128 -0.0366 -0.0129 -0.0159 85  LYS A NZ  
694  N N   . LEU A 96  ? 0.2868 0.2757 0.2642 -0.0173 -0.0096 -0.0221 86  LEU A N   
695  C CA  . LEU A 96  ? 0.2799 0.2728 0.2627 -0.0160 -0.0071 -0.0247 86  LEU A CA  
696  C C   . LEU A 96  ? 0.2798 0.2716 0.2617 -0.0126 -0.0080 -0.0252 86  LEU A C   
697  O O   . LEU A 96  ? 0.2709 0.2665 0.2568 -0.0118 -0.0061 -0.0272 86  LEU A O   
698  C CB  . LEU A 96  ? 0.2781 0.2711 0.2654 -0.0166 -0.0048 -0.0252 86  LEU A CB  
699  C CG  . LEU A 96  ? 0.2822 0.2794 0.2728 -0.0193 -0.0028 -0.0263 86  LEU A CG  
700  C CD1 . LEU A 96  ? 0.2807 0.2765 0.2742 -0.0197 -0.0015 -0.0260 86  LEU A CD1 
701  C CD2 . LEU A 96  ? 0.2804 0.2832 0.2750 -0.0196 -0.0007 -0.0293 86  LEU A CD2 
702  N N   . GLU A 97  ? 0.2795 0.2664 0.2562 -0.0107 -0.0110 -0.0235 87  GLU A N   
703  C CA  . GLU A 97  ? 0.2930 0.2788 0.2682 -0.0070 -0.0124 -0.0240 87  GLU A CA  
704  C C   . GLU A 97  ? 0.2794 0.2660 0.2585 -0.0058 -0.0106 -0.0249 87  GLU A C   
705  O O   . GLU A 97  ? 0.2817 0.2721 0.2631 -0.0041 -0.0097 -0.0266 87  GLU A O   
706  C CB  . GLU A 97  ? 0.3114 0.3019 0.2863 -0.0059 -0.0127 -0.0255 87  GLU A CB  
707  C CG  . GLU A 97  ? 0.3329 0.3212 0.3026 -0.0068 -0.0153 -0.0239 87  GLU A CG  
708  C CD  . GLU A 97  ? 0.3597 0.3526 0.3285 -0.0056 -0.0160 -0.0251 87  GLU A CD  
709  O OE1 . GLU A 97  ? 0.3668 0.3641 0.3380 -0.0034 -0.0151 -0.0271 87  GLU A OE1 
710  O OE2 . GLU A 97  ? 0.3898 0.3823 0.3552 -0.0072 -0.0176 -0.0238 87  GLU A OE2 
711  N N   . ILE A 98  ? 0.2740 0.2572 0.2539 -0.0069 -0.0101 -0.0237 88  ILE A N   
712  C CA  . ILE A 98  ? 0.2668 0.2498 0.2496 -0.0058 -0.0088 -0.0239 88  ILE A CA  
713  C C   . ILE A 98  ? 0.2655 0.2454 0.2448 -0.0024 -0.0112 -0.0235 88  ILE A C   
714  O O   . ILE A 98  ? 0.2713 0.2459 0.2456 -0.0015 -0.0140 -0.0221 88  ILE A O   
715  C CB  . ILE A 98  ? 0.2640 0.2445 0.2482 -0.0078 -0.0078 -0.0225 88  ILE A CB  
716  C CG1 . ILE A 98  ? 0.2611 0.2449 0.2485 -0.0108 -0.0058 -0.0232 88  ILE A CG1 
717  C CG2 . ILE A 98  ? 0.2660 0.2467 0.2535 -0.0068 -0.0065 -0.0226 88  ILE A CG2 
718  C CD1 . ILE A 98  ? 0.2659 0.2549 0.2583 -0.0113 -0.0032 -0.0255 88  ILE A CD1 
719  N N   . SER A 99  ? 0.2562 0.2394 0.2380 -0.0006 -0.0102 -0.0249 89  SER A N   
720  C CA  . SER A 99  ? 0.2581 0.2401 0.2373 0.0029  -0.0122 -0.0252 89  SER A CA  
721  C C   . SER A 99  ? 0.2544 0.2335 0.2339 0.0034  -0.0121 -0.0242 89  SER A C   
722  O O   . SER A 99  ? 0.2604 0.2413 0.2402 0.0057  -0.0124 -0.0250 89  SER A O   
723  C CB  . SER A 99  ? 0.2601 0.2489 0.2417 0.0045  -0.0111 -0.0274 89  SER A CB  
724  O OG  . SER A 99  ? 0.2594 0.2521 0.2459 0.0028  -0.0083 -0.0279 89  SER A OG  
725  N N   . ASN A 100 ? 0.2540 0.2292 0.2333 0.0011  -0.0119 -0.0225 90  ASN A N   
726  C CA  . ASN A 100 ? 0.2503 0.2228 0.2297 0.0014  -0.0120 -0.0214 90  ASN A CA  
727  C C   . ASN A 100 ? 0.2639 0.2321 0.2383 0.0045  -0.0151 -0.0213 90  ASN A C   
728  O O   . ASN A 100 ? 0.2640 0.2281 0.2338 0.0053  -0.0177 -0.0209 90  ASN A O   
729  C CB  . ASN A 100 ? 0.2553 0.2250 0.2353 -0.0014 -0.0112 -0.0196 90  ASN A CB  
730  C CG  . ASN A 100 ? 0.2563 0.2219 0.2320 -0.0028 -0.0132 -0.0185 90  ASN A CG  
731  O OD1 . ASN A 100 ? 0.2571 0.2243 0.2323 -0.0036 -0.0133 -0.0190 90  ASN A OD1 
732  N ND2 . ASN A 100 ? 0.2591 0.2196 0.2315 -0.0035 -0.0148 -0.0168 90  ASN A ND2 
733  N N   . ASP A 101 ? 0.2616 0.2307 0.2368 0.0063  -0.0150 -0.0216 91  ASP A N   
734  C CA  . ASP A 101 ? 0.2769 0.2426 0.2478 0.0096  -0.0179 -0.0221 91  ASP A CA  
735  C C   . ASP A 101 ? 0.2828 0.2419 0.2506 0.0087  -0.0194 -0.0204 91  ASP A C   
736  O O   . ASP A 101 ? 0.2944 0.2489 0.2579 0.0111  -0.0222 -0.0207 91  ASP A O   
737  C CB  . ASP A 101 ? 0.2811 0.2522 0.2545 0.0118  -0.0170 -0.0235 91  ASP A CB  
738  C CG  . ASP A 101 ? 0.2876 0.2654 0.2632 0.0129  -0.0160 -0.0254 91  ASP A CG  
739  O OD1 . ASP A 101 ? 0.3114 0.2892 0.2839 0.0159  -0.0182 -0.0268 91  ASP A OD1 
740  O OD2 . ASP A 101 ? 0.2823 0.2651 0.2625 0.0107  -0.0131 -0.0255 91  ASP A OD2 
741  N N   . ASP A 102 ? 0.2731 0.2318 0.2432 0.0053  -0.0176 -0.0188 92  ASP A N   
742  C CA  . ASP A 102 ? 0.2741 0.2276 0.2417 0.0039  -0.0187 -0.0171 92  ASP A CA  
743  C C   . ASP A 102 ? 0.2606 0.2149 0.2307 0.0000  -0.0168 -0.0157 92  ASP A C   
744  O O   . ASP A 102 ? 0.2545 0.2134 0.2287 -0.0011 -0.0144 -0.0162 92  ASP A O   
745  C CB  . ASP A 102 ? 0.2818 0.2364 0.2507 0.0052  -0.0183 -0.0173 92  ASP A CB  
746  C CG  . ASP A 102 ? 0.2932 0.2420 0.2584 0.0045  -0.0202 -0.0160 92  ASP A CG  
747  O OD1 . ASP A 102 ? 0.2989 0.2420 0.2600 0.0030  -0.0221 -0.0149 92  ASP A OD1 
748  O OD2 . ASP A 102 ? 0.3177 0.2679 0.2841 0.0053  -0.0197 -0.0160 92  ASP A OD2 
749  N N   . PHE A 103 ? 0.2576 0.2074 0.2248 -0.0018 -0.0180 -0.0141 93  PHE A N   
750  C CA  . PHE A 103 ? 0.2550 0.2058 0.2240 -0.0054 -0.0165 -0.0127 93  PHE A CA  
751  C C   . PHE A 103 ? 0.2523 0.2008 0.2203 -0.0062 -0.0169 -0.0115 93  PHE A C   
752  O O   . PHE A 103 ? 0.2639 0.2069 0.2269 -0.0064 -0.0195 -0.0107 93  PHE A O   
753  C CB  . PHE A 103 ? 0.2575 0.2058 0.2229 -0.0076 -0.0179 -0.0120 93  PHE A CB  
754  C CG  . PHE A 103 ? 0.2563 0.2075 0.2240 -0.0112 -0.0162 -0.0111 93  PHE A CG  
755  C CD1 . PHE A 103 ? 0.2511 0.2068 0.2219 -0.0122 -0.0143 -0.0119 93  PHE A CD1 
756  C CD2 . PHE A 103 ? 0.2585 0.2082 0.2251 -0.0135 -0.0164 -0.0096 93  PHE A CD2 
757  C CE1 . PHE A 103 ? 0.2533 0.2123 0.2263 -0.0153 -0.0128 -0.0115 93  PHE A CE1 
758  C CE2 . PHE A 103 ? 0.2620 0.2154 0.2309 -0.0166 -0.0147 -0.0090 93  PHE A CE2 
759  C CZ  . PHE A 103 ? 0.2529 0.2109 0.2249 -0.0173 -0.0130 -0.0101 93  PHE A CZ  
760  N N   . ILE A 104 ? 0.2431 0.1956 0.2158 -0.0068 -0.0145 -0.0112 94  ILE A N   
761  C CA  . ILE A 104 ? 0.2458 0.1973 0.2182 -0.0074 -0.0146 -0.0100 94  ILE A CA  
762  C C   . ILE A 104 ? 0.2468 0.1989 0.2196 -0.0109 -0.0140 -0.0086 94  ILE A C   
763  O O   . ILE A 104 ? 0.2514 0.2074 0.2279 -0.0121 -0.0119 -0.0088 94  ILE A O   
764  C CB  . ILE A 104 ? 0.2479 0.2035 0.2248 -0.0058 -0.0127 -0.0103 94  ILE A CB  
765  C CG1 . ILE A 104 ? 0.2484 0.2030 0.2246 -0.0063 -0.0131 -0.0091 94  ILE A CG1 
766  C CG2 . ILE A 104 ? 0.2434 0.2038 0.2261 -0.0066 -0.0098 -0.0104 94  ILE A CG2 
767  C CD1 . ILE A 104 ? 0.2579 0.2076 0.2288 -0.0051 -0.0159 -0.0093 94  ILE A CD1 
768  N N   . ARG A 105 ? 0.2454 0.1936 0.2139 -0.0124 -0.0158 -0.0075 95  ARG A N   
769  C CA  . ARG A 105 ? 0.2491 0.1986 0.2176 -0.0158 -0.0154 -0.0061 95  ARG A CA  
770  C C   . ARG A 105 ? 0.2487 0.1989 0.2181 -0.0158 -0.0150 -0.0053 95  ARG A C   
771  O O   . ARG A 105 ? 0.2572 0.2038 0.2236 -0.0145 -0.0167 -0.0054 95  ARG A O   
772  C CB  . ARG A 105 ? 0.2587 0.2033 0.2211 -0.0184 -0.0180 -0.0052 95  ARG A CB  
773  C CG  . ARG A 105 ? 0.2656 0.2090 0.2262 -0.0184 -0.0188 -0.0057 95  ARG A CG  
774  C CD  . ARG A 105 ? 0.2811 0.2193 0.2352 -0.0215 -0.0216 -0.0043 95  ARG A CD  
775  N NE  . ARG A 105 ? 0.2836 0.2249 0.2379 -0.0257 -0.0208 -0.0029 95  ARG A NE  
776  C CZ  . ARG A 105 ? 0.3041 0.2424 0.2531 -0.0295 -0.0229 -0.0013 95  ARG A CZ  
777  N NH1 . ARG A 105 ? 0.3133 0.2444 0.2562 -0.0298 -0.0260 -0.0007 95  ARG A NH1 
778  N NH2 . ARG A 105 ? 0.3056 0.2483 0.2554 -0.0332 -0.0219 -0.0004 95  ARG A NH2 
779  N N   . THR A 106 ? 0.2398 0.1949 0.2133 -0.0170 -0.0129 -0.0047 96  THR A N   
780  C CA  . THR A 106 ? 0.2437 0.2001 0.2183 -0.0168 -0.0126 -0.0039 96  THR A CA  
781  C C   . THR A 106 ? 0.2494 0.2027 0.2190 -0.0193 -0.0146 -0.0028 96  THR A C   
782  O O   . THR A 106 ? 0.2546 0.2084 0.2242 -0.0190 -0.0148 -0.0022 96  THR A O   
783  C CB  . THR A 106 ? 0.2386 0.2011 0.2191 -0.0169 -0.0099 -0.0035 96  THR A CB  
784  O OG1 . THR A 106 ? 0.2461 0.2111 0.2268 -0.0195 -0.0095 -0.0033 96  THR A OG1 
785  C CG2 . THR A 106 ? 0.2413 0.2059 0.2264 -0.0145 -0.0081 -0.0045 96  THR A CG2 
786  N N   . THR A 107 ? 0.2596 0.2098 0.2248 -0.0219 -0.0163 -0.0024 97  THR A N   
787  C CA  . THR A 107 ? 0.2719 0.2176 0.2312 -0.0246 -0.0188 -0.0014 97  THR A CA  
788  C C   . THR A 107 ? 0.2870 0.2253 0.2414 -0.0227 -0.0215 -0.0019 97  THR A C   
789  O O   . THR A 107 ? 0.2953 0.2293 0.2450 -0.0245 -0.0236 -0.0013 97  THR A O   
790  C CB  . THR A 107 ? 0.2741 0.2190 0.2301 -0.0284 -0.0198 -0.0005 97  THR A CB  
791  O OG1 . THR A 107 ? 0.2666 0.2105 0.2228 -0.0272 -0.0198 -0.0013 97  THR A OG1 
792  C CG2 . THR A 107 ? 0.2709 0.2232 0.2305 -0.0309 -0.0177 0.0000  97  THR A CG2 
793  N N   . GLU A 108 ? 0.2907 0.2277 0.2460 -0.0191 -0.0216 -0.0033 98  GLU A N   
794  C CA  . GLU A 108 ? 0.3078 0.2384 0.2587 -0.0166 -0.0243 -0.0043 98  GLU A CA  
795  C C   . GLU A 108 ? 0.3042 0.2356 0.2558 -0.0151 -0.0242 -0.0047 98  GLU A C   
796  O O   . GLU A 108 ? 0.2763 0.2139 0.2332 -0.0142 -0.0217 -0.0046 98  GLU A O   
797  C CB  . GLU A 108 ? 0.3197 0.2503 0.2719 -0.0132 -0.0242 -0.0058 98  GLU A CB  
798  C CG  . GLU A 108 ? 0.3425 0.2702 0.2919 -0.0145 -0.0254 -0.0055 98  GLU A CG  
799  C CD  . GLU A 108 ? 0.3576 0.2874 0.3094 -0.0117 -0.0246 -0.0069 98  GLU A CD  
800  O OE1 . GLU A 108 ? 0.3999 0.3266 0.3485 -0.0124 -0.0261 -0.0067 98  GLU A OE1 
801  O OE2 . GLU A 108 ? 0.3605 0.2952 0.3170 -0.0092 -0.0225 -0.0080 98  GLU A OE2 
802  N N   . GLU A 109 ? 0.3134 0.2386 0.2597 -0.0148 -0.0271 -0.0051 99  GLU A N   
803  C CA  . GLU A 109 ? 0.3230 0.2491 0.2696 -0.0135 -0.0272 -0.0056 99  GLU A CA  
804  C C   . GLU A 109 ? 0.3033 0.2341 0.2542 -0.0093 -0.0257 -0.0071 99  GLU A C   
805  O O   . GLU A 109 ? 0.2936 0.2291 0.2476 -0.0087 -0.0242 -0.0070 99  GLU A O   
806  C CB  . GLU A 109 ? 0.3487 0.2665 0.2883 -0.0136 -0.0309 -0.0063 99  GLU A CB  
807  C CG  . GLU A 109 ? 0.3658 0.2841 0.3051 -0.0118 -0.0314 -0.0075 99  GLU A CG  
808  C CD  . GLU A 109 ? 0.3807 0.3055 0.3236 -0.0139 -0.0292 -0.0062 99  GLU A CD  
809  O OE1 . GLU A 109 ? 0.4013 0.3283 0.3451 -0.0176 -0.0280 -0.0043 99  GLU A OE1 
810  O OE2 . GLU A 109 ? 0.4002 0.3282 0.3448 -0.0118 -0.0286 -0.0071 99  GLU A OE2 
811  N N   . ARG A 110 ? 0.3011 0.2310 0.2521 -0.0066 -0.0260 -0.0084 100 ARG A N   
812  C CA  . ARG A 110 ? 0.2909 0.2260 0.2460 -0.0030 -0.0245 -0.0098 100 ARG A CA  
813  C C   . ARG A 110 ? 0.2764 0.2193 0.2381 -0.0039 -0.0210 -0.0086 100 ARG A C   
814  O O   . ARG A 110 ? 0.2815 0.2291 0.2464 -0.0021 -0.0197 -0.0090 100 ARG A O   
815  C CB  . ARG A 110 ? 0.3030 0.2368 0.2573 -0.0003 -0.0253 -0.0114 100 ARG A CB  
816  C CG  . ARG A 110 ? 0.3036 0.2382 0.2595 -0.0021 -0.0242 -0.0105 100 ARG A CG  
817  C CD  . ARG A 110 ? 0.3104 0.2454 0.2663 0.0008  -0.0246 -0.0122 100 ARG A CD  
818  N NE  . ARG A 110 ? 0.3068 0.2418 0.2633 -0.0009 -0.0240 -0.0115 100 ARG A NE  
819  C CZ  . ARG A 110 ? 0.3063 0.2443 0.2650 0.0005  -0.0231 -0.0125 100 ARG A CZ  
820  N NH1 . ARG A 110 ? 0.3071 0.2486 0.2676 0.0039  -0.0227 -0.0143 100 ARG A NH1 
821  N NH2 . ARG A 110 ? 0.2971 0.2353 0.2563 -0.0014 -0.0224 -0.0119 100 ARG A NH2 
822  N N   . HIS A 111 ? 0.2624 0.2063 0.2258 -0.0067 -0.0196 -0.0072 101 HIS A N   
823  C CA  . HIS A 111 ? 0.2533 0.2035 0.2225 -0.0076 -0.0166 -0.0061 101 HIS A CA  
824  C C   . HIS A 111 ? 0.2607 0.2128 0.2305 -0.0092 -0.0162 -0.0047 101 HIS A C   
825  O O   . HIS A 111 ? 0.2625 0.2192 0.2361 -0.0082 -0.0146 -0.0042 101 HIS A O   
826  C CB  . HIS A 111 ? 0.2463 0.1975 0.2174 -0.0095 -0.0154 -0.0055 101 HIS A CB  
827  C CG  . HIS A 111 ? 0.2385 0.1955 0.2155 -0.0100 -0.0125 -0.0046 101 HIS A CG  
828  N ND1 . HIS A 111 ? 0.2429 0.2033 0.2242 -0.0081 -0.0108 -0.0051 101 HIS A ND1 
829  C CD2 . HIS A 111 ? 0.2389 0.1987 0.2180 -0.0120 -0.0114 -0.0034 101 HIS A CD2 
830  C CE1 . HIS A 111 ? 0.2327 0.1969 0.2184 -0.0089 -0.0087 -0.0041 101 HIS A CE1 
831  N NE2 . HIS A 111 ? 0.2301 0.1943 0.2147 -0.0110 -0.0090 -0.0031 101 HIS A NE2 
832  N N   . LYS A 112 ? 0.2659 0.2148 0.2320 -0.0118 -0.0176 -0.0040 102 LYS A N   
833  C CA  . LYS A 112 ? 0.2802 0.2316 0.2468 -0.0137 -0.0172 -0.0027 102 LYS A CA  
834  C C   . LYS A 112 ? 0.2748 0.2271 0.2412 -0.0117 -0.0177 -0.0031 102 LYS A C   
835  O O   . LYS A 112 ? 0.2698 0.2269 0.2392 -0.0120 -0.0162 -0.0021 102 LYS A O   
836  C CB  . LYS A 112 ? 0.2974 0.2448 0.2590 -0.0171 -0.0191 -0.0020 102 LYS A CB  
837  C CG  . LYS A 112 ? 0.3089 0.2570 0.2709 -0.0196 -0.0185 -0.0013 102 LYS A CG  
838  C CD  . LYS A 112 ? 0.3356 0.2805 0.2925 -0.0237 -0.0204 -0.0004 102 LYS A CD  
839  C CE  . LYS A 112 ? 0.3527 0.3018 0.3106 -0.0257 -0.0196 0.0006  102 LYS A CE  
840  N NZ  . LYS A 112 ? 0.3794 0.3271 0.3330 -0.0304 -0.0210 0.0016  102 LYS A NZ  
841  N N   . HIS A 113 ? 0.2847 0.2329 0.2475 -0.0097 -0.0197 -0.0048 103 HIS A N   
842  C CA  . HIS A 113 ? 0.3002 0.2499 0.2628 -0.0076 -0.0202 -0.0056 103 HIS A CA  
843  C C   . HIS A 113 ? 0.2812 0.2381 0.2496 -0.0058 -0.0176 -0.0051 103 HIS A C   
844  O O   . HIS A 113 ? 0.2836 0.2445 0.2536 -0.0057 -0.0170 -0.0045 103 HIS A O   
845  C CB  . HIS A 113 ? 0.3283 0.2729 0.2865 -0.0049 -0.0228 -0.0080 103 HIS A CB  
846  C CG  . HIS A 113 ? 0.3483 0.2952 0.3062 -0.0026 -0.0234 -0.0093 103 HIS A CG  
847  N ND1 . HIS A 113 ? 0.3672 0.3128 0.3224 -0.0038 -0.0246 -0.0094 103 HIS A ND1 
848  C CD2 . HIS A 113 ? 0.3726 0.3236 0.3326 0.0005  -0.0228 -0.0108 103 HIS A CD2 
849  C CE1 . HIS A 113 ? 0.3783 0.3271 0.3340 -0.0012 -0.0248 -0.0109 103 HIS A CE1 
850  N NE2 . HIS A 113 ? 0.3780 0.3304 0.3366 0.0013  -0.0238 -0.0117 103 HIS A NE2 
851  N N   . VAL A 114 ? 0.2654 0.2239 0.2368 -0.0047 -0.0163 -0.0054 104 VAL A N   
852  C CA  . VAL A 114 ? 0.2555 0.2200 0.2321 -0.0035 -0.0140 -0.0047 104 VAL A CA  
853  C C   . VAL A 114 ? 0.2497 0.2180 0.2303 -0.0054 -0.0120 -0.0024 104 VAL A C   
854  O O   . VAL A 114 ? 0.2538 0.2265 0.2372 -0.0048 -0.0109 -0.0013 104 VAL A O   
855  C CB  . VAL A 114 ? 0.2537 0.2187 0.2323 -0.0023 -0.0131 -0.0056 104 VAL A CB  
856  C CG1 . VAL A 114 ? 0.2538 0.2245 0.2378 -0.0019 -0.0107 -0.0046 104 VAL A CG1 
857  C CG2 . VAL A 114 ? 0.2619 0.2246 0.2371 0.0001  -0.0150 -0.0079 104 VAL A CG2 
858  N N   . VAL A 115 ? 0.2496 0.2164 0.2302 -0.0074 -0.0117 -0.0017 105 VAL A N   
859  C CA  . VAL A 115 ? 0.2498 0.2203 0.2339 -0.0088 -0.0100 0.0000  105 VAL A CA  
860  C C   . VAL A 115 ? 0.2591 0.2316 0.2423 -0.0094 -0.0105 0.0010  105 VAL A C   
861  O O   . VAL A 115 ? 0.2612 0.2382 0.2481 -0.0090 -0.0092 0.0025  105 VAL A O   
862  C CB  . VAL A 115 ? 0.2445 0.2136 0.2282 -0.0110 -0.0099 0.0002  105 VAL A CB  
863  C CG1 . VAL A 115 ? 0.2465 0.2202 0.2338 -0.0121 -0.0084 0.0018  105 VAL A CG1 
864  C CG2 . VAL A 115 ? 0.2456 0.2134 0.2304 -0.0106 -0.0093 -0.0007 105 VAL A CG2 
865  N N   . GLU A 116 ? 0.2687 0.2378 0.2470 -0.0103 -0.0126 0.0003  106 GLU A N   
866  C CA  . GLU A 116 ? 0.2843 0.2550 0.2611 -0.0111 -0.0133 0.0009  106 GLU A CA  
867  C C   . GLU A 116 ? 0.2776 0.2521 0.2563 -0.0088 -0.0128 0.0009  106 GLU A C   
868  O O   . GLU A 116 ? 0.2767 0.2559 0.2577 -0.0090 -0.0119 0.0024  106 GLU A O   
869  C CB  . GLU A 116 ? 0.2972 0.2624 0.2679 -0.0124 -0.0159 -0.0003 106 GLU A CB  
870  C CG  . GLU A 116 ? 0.3178 0.2802 0.2860 -0.0156 -0.0165 0.0001  106 GLU A CG  
871  C CD  . GLU A 116 ? 0.3550 0.3099 0.3167 -0.0168 -0.0194 -0.0010 106 GLU A CD  
872  O OE1 . GLU A 116 ? 0.3700 0.3215 0.3287 -0.0150 -0.0211 -0.0026 106 GLU A OE1 
873  O OE2 . GLU A 116 ? 0.3913 0.3436 0.3506 -0.0196 -0.0201 -0.0005 106 GLU A OE2 
874  N N   . GLN A 117 ? 0.2828 0.2557 0.2604 -0.0067 -0.0135 -0.0007 107 GLN A N   
875  C CA  . GLN A 117 ? 0.2968 0.2737 0.2755 -0.0047 -0.0133 -0.0011 107 GLN A CA  
876  C C   . GLN A 117 ? 0.2852 0.2676 0.2693 -0.0042 -0.0110 0.0007  107 GLN A C   
877  O O   . GLN A 117 ? 0.2782 0.2655 0.2639 -0.0039 -0.0104 0.0018  107 GLN A O   
878  C CB  . GLN A 117 ? 0.3212 0.2957 0.2971 -0.0024 -0.0148 -0.0037 107 GLN A CB  
879  C CG  . GLN A 117 ? 0.3560 0.3250 0.3261 -0.0023 -0.0176 -0.0058 107 GLN A CG  
880  C CD  . GLN A 117 ? 0.3921 0.3635 0.3610 -0.0029 -0.0182 -0.0056 107 GLN A CD  
881  O OE1 . GLN A 117 ? 0.4336 0.4099 0.4037 -0.0013 -0.0178 -0.0061 107 GLN A OE1 
882  N NE2 . GLN A 117 ? 0.4152 0.3838 0.3817 -0.0055 -0.0190 -0.0048 107 GLN A NE2 
883  N N   . VAL A 118 ? 0.2710 0.2527 0.2577 -0.0043 -0.0097 0.0011  108 VAL A N   
884  C CA  . VAL A 118 ? 0.2612 0.2468 0.2530 -0.0042 -0.0077 0.0031  108 VAL A CA  
885  C C   . VAL A 118 ? 0.2600 0.2483 0.2539 -0.0053 -0.0069 0.0054  108 VAL A C   
886  O O   . VAL A 118 ? 0.2629 0.2553 0.2594 -0.0049 -0.0061 0.0072  108 VAL A O   
887  C CB  . VAL A 118 ? 0.2608 0.2443 0.2546 -0.0043 -0.0067 0.0027  108 VAL A CB  
888  C CG1 . VAL A 118 ? 0.2557 0.2418 0.2544 -0.0045 -0.0048 0.0047  108 VAL A CG1 
889  C CG2 . VAL A 118 ? 0.2601 0.2427 0.2526 -0.0029 -0.0072 0.0006  108 VAL A CG2 
890  N N   . PHE A 119 ? 0.2467 0.2331 0.2395 -0.0067 -0.0072 0.0055  109 PHE A N   
891  C CA  . PHE A 119 ? 0.2533 0.2429 0.2481 -0.0076 -0.0066 0.0075  109 PHE A CA  
892  C C   . PHE A 119 ? 0.2616 0.2546 0.2552 -0.0076 -0.0072 0.0083  109 PHE A C   
893  O O   . PHE A 119 ? 0.2633 0.2606 0.2599 -0.0072 -0.0063 0.0104  109 PHE A O   
894  C CB  . PHE A 119 ? 0.2550 0.2427 0.2481 -0.0094 -0.0070 0.0071  109 PHE A CB  
895  C CG  . PHE A 119 ? 0.2602 0.2518 0.2565 -0.0099 -0.0060 0.0088  109 PHE A CG  
896  C CD1 . PHE A 119 ? 0.2609 0.2527 0.2605 -0.0097 -0.0048 0.0090  109 PHE A CD1 
897  C CD2 . PHE A 119 ? 0.2644 0.2598 0.2605 -0.0104 -0.0062 0.0102  109 PHE A CD2 
898  C CE1 . PHE A 119 ? 0.2594 0.2550 0.2620 -0.0096 -0.0040 0.0103  109 PHE A CE1 
899  C CE2 . PHE A 119 ? 0.2640 0.2635 0.2631 -0.0105 -0.0054 0.0117  109 PHE A CE2 
900  C CZ  . PHE A 119 ? 0.2674 0.2670 0.2698 -0.0099 -0.0043 0.0118  109 PHE A CZ  
901  N N   . GLU A 120 ? 0.2731 0.2641 0.2624 -0.0079 -0.0088 0.0066  110 GLU A N   
902  C CA  . GLU A 120 ? 0.2832 0.2774 0.2709 -0.0079 -0.0096 0.0069  110 GLU A CA  
903  C C   . GLU A 120 ? 0.2855 0.2842 0.2756 -0.0063 -0.0089 0.0077  110 GLU A C   
904  O O   . GLU A 120 ? 0.2891 0.2925 0.2802 -0.0064 -0.0086 0.0092  110 GLU A O   
905  C CB  . GLU A 120 ? 0.3075 0.2976 0.2898 -0.0084 -0.0117 0.0044  110 GLU A CB  
906  C CG  . GLU A 120 ? 0.3190 0.3057 0.2983 -0.0108 -0.0127 0.0041  110 GLU A CG  
907  C CD  . GLU A 120 ? 0.3492 0.3403 0.3294 -0.0125 -0.0123 0.0059  110 GLU A CD  
908  O OE1 . GLU A 120 ? 0.3822 0.3773 0.3625 -0.0122 -0.0124 0.0063  110 GLU A OE1 
909  O OE2 . GLU A 120 ? 0.3743 0.3656 0.3551 -0.0143 -0.0119 0.0068  110 GLU A OE2 
910  N N   . ARG A 121 ? 0.2840 0.2815 0.2747 -0.0050 -0.0086 0.0067  111 ARG A N   
911  C CA  . ARG A 121 ? 0.2845 0.2868 0.2775 -0.0039 -0.0078 0.0075  111 ARG A CA  
912  C C   . ARG A 121 ? 0.2844 0.2900 0.2818 -0.0044 -0.0062 0.0109  111 ARG A C   
913  O O   . ARG A 121 ? 0.2877 0.2982 0.2863 -0.0043 -0.0059 0.0126  111 ARG A O   
914  C CB  . ARG A 121 ? 0.2954 0.2962 0.2883 -0.0027 -0.0077 0.0058  111 ARG A CB  
915  C CG  . ARG A 121 ? 0.3029 0.3092 0.2983 -0.0022 -0.0068 0.0069  111 ARG A CG  
916  C CD  . ARG A 121 ? 0.3126 0.3185 0.3072 -0.0010 -0.0070 0.0046  111 ARG A CD  
917  N NE  . ARG A 121 ? 0.3193 0.3309 0.3163 -0.0010 -0.0060 0.0060  111 ARG A NE  
918  C CZ  . ARG A 121 ? 0.3321 0.3458 0.3291 -0.0003 -0.0059 0.0044  111 ARG A CZ  
919  N NH1 . ARG A 121 ? 0.3447 0.3550 0.3395 0.0009  -0.0067 0.0014  111 ARG A NH1 
920  N NH2 . ARG A 121 ? 0.3349 0.3545 0.3341 -0.0010 -0.0049 0.0061  111 ARG A NH2 
921  N N   . LEU A 122 ? 0.2760 0.2789 0.2757 -0.0047 -0.0053 0.0117  112 LEU A N   
922  C CA  . LEU A 122 ? 0.2869 0.2918 0.2907 -0.0048 -0.0041 0.0146  112 LEU A CA  
923  C C   . LEU A 122 ? 0.2904 0.2987 0.2946 -0.0052 -0.0042 0.0166  112 LEU A C   
924  O O   . LEU A 122 ? 0.2886 0.3004 0.2953 -0.0049 -0.0037 0.0193  112 LEU A O   
925  C CB  . LEU A 122 ? 0.2966 0.2977 0.3026 -0.0048 -0.0032 0.0144  112 LEU A CB  
926  C CG  . LEU A 122 ? 0.3148 0.3147 0.3226 -0.0044 -0.0024 0.0143  112 LEU A CG  
927  C CD1 . LEU A 122 ? 0.3338 0.3331 0.3388 -0.0041 -0.0031 0.0118  112 LEU A CD1 
928  C CD2 . LEU A 122 ? 0.3279 0.3243 0.3380 -0.0045 -0.0016 0.0140  112 LEU A CD2 
929  N N   . LEU A 123 ? 0.2952 0.3026 0.2968 -0.0060 -0.0051 0.0153  113 LEU A N   
930  C CA  . LEU A 123 ? 0.3099 0.3211 0.3113 -0.0066 -0.0054 0.0167  113 LEU A CA  
931  C C   . LEU A 123 ? 0.3125 0.3283 0.3130 -0.0064 -0.0058 0.0174  113 LEU A C   
932  O O   . LEU A 123 ? 0.3076 0.3279 0.3100 -0.0063 -0.0054 0.0200  113 LEU A O   
933  C CB  . LEU A 123 ? 0.3352 0.3443 0.3331 -0.0080 -0.0064 0.0149  113 LEU A CB  
934  C CG  . LEU A 123 ? 0.3609 0.3740 0.3590 -0.0091 -0.0065 0.0162  113 LEU A CG  
935  C CD1 . LEU A 123 ? 0.3693 0.3837 0.3714 -0.0085 -0.0054 0.0179  113 LEU A CD1 
936  C CD2 . LEU A 123 ? 0.3738 0.3846 0.3675 -0.0111 -0.0078 0.0142  113 LEU A CD2 
937  N N   . LYS A 124 ? 0.3158 0.3306 0.3132 -0.0062 -0.0067 0.0151  114 LYS A N   
938  C CA  . LYS A 124 ? 0.3334 0.3530 0.3296 -0.0059 -0.0072 0.0151  114 LYS A CA  
939  C C   . LYS A 124 ? 0.3190 0.3431 0.3186 -0.0054 -0.0062 0.0178  114 LYS A C   
940  O O   . LYS A 124 ? 0.3205 0.3501 0.3206 -0.0056 -0.0062 0.0196  114 LYS A O   
941  C CB  . LYS A 124 ? 0.3608 0.3781 0.3533 -0.0053 -0.0085 0.0116  114 LYS A CB  
942  C CG  . LYS A 124 ? 0.3897 0.4123 0.3806 -0.0049 -0.0092 0.0108  114 LYS A CG  
943  C CD  . LYS A 124 ? 0.4280 0.4475 0.4148 -0.0038 -0.0108 0.0068  114 LYS A CD  
944  C CE  . LYS A 124 ? 0.4555 0.4811 0.4413 -0.0028 -0.0113 0.0056  114 LYS A CE  
945  N NZ  . LYS A 124 ? 0.4787 0.5090 0.4639 -0.0038 -0.0117 0.0065  114 LYS A NZ  
946  N N   . GLN A 125 ? 0.3049 0.3265 0.3065 -0.0050 -0.0054 0.0181  115 GLN A N   
947  C CA  . GLN A 125 ? 0.3006 0.3253 0.3050 -0.0049 -0.0045 0.0208  115 GLN A CA  
948  C C   . GLN A 125 ? 0.2995 0.3256 0.3070 -0.0051 -0.0038 0.0245  115 GLN A C   
949  O O   . GLN A 125 ? 0.3051 0.3350 0.3143 -0.0054 -0.0035 0.0274  115 GLN A O   
950  C CB  . GLN A 125 ? 0.2914 0.3126 0.2970 -0.0047 -0.0038 0.0199  115 GLN A CB  
951  C CG  . GLN A 125 ? 0.2920 0.3133 0.2947 -0.0041 -0.0045 0.0165  115 GLN A CG  
952  C CD  . GLN A 125 ? 0.2921 0.3106 0.2957 -0.0040 -0.0039 0.0154  115 GLN A CD  
953  O OE1 . GLN A 125 ? 0.2975 0.3172 0.2994 -0.0033 -0.0044 0.0130  115 GLN A OE1 
954  N NE2 . GLN A 125 ? 0.2898 0.3049 0.2962 -0.0044 -0.0030 0.0169  115 GLN A NE2 
955  N N   . GLY A 126 ? 0.2942 0.3175 0.3024 -0.0050 -0.0038 0.0245  116 GLY A N   
956  C CA  . GLY A 126 ? 0.2929 0.3168 0.3041 -0.0046 -0.0034 0.0275  116 GLY A CA  
957  C C   . GLY A 126 ? 0.2848 0.3042 0.2990 -0.0040 -0.0026 0.0282  116 GLY A C   
958  O O   . GLY A 126 ? 0.2878 0.3073 0.3046 -0.0033 -0.0024 0.0308  116 GLY A O   
959  N N   . ASP A 127 ? 0.2833 0.2986 0.2968 -0.0042 -0.0023 0.0258  117 ASP A N   
960  C CA  . ASP A 127 ? 0.2858 0.2965 0.3019 -0.0038 -0.0016 0.0258  117 ASP A CA  
961  C C   . ASP A 127 ? 0.2837 0.2925 0.3006 -0.0032 -0.0015 0.0250  117 ASP A C   
962  O O   . ASP A 127 ? 0.2827 0.2892 0.3024 -0.0023 -0.0010 0.0258  117 ASP A O   
963  C CB  . ASP A 127 ? 0.2878 0.2954 0.3027 -0.0042 -0.0014 0.0232  117 ASP A CB  
964  C CG  . ASP A 127 ? 0.2947 0.3041 0.3097 -0.0048 -0.0011 0.0242  117 ASP A CG  
965  O OD1 . ASP A 127 ? 0.3025 0.3105 0.3201 -0.0050 -0.0006 0.0262  117 ASP A OD1 
966  O OD2 . ASP A 127 ? 0.3054 0.3178 0.3180 -0.0050 -0.0016 0.0229  117 ASP A OD2 
967  N N   . ILE A 128 ? 0.2926 0.3026 0.3070 -0.0037 -0.0021 0.0233  118 ILE A N   
968  C CA  . ILE A 128 ? 0.2881 0.2977 0.3027 -0.0036 -0.0021 0.0224  118 ILE A CA  
969  C C   . ILE A 128 ? 0.2947 0.3093 0.3091 -0.0036 -0.0026 0.0239  118 ILE A C   
970  O O   . ILE A 128 ? 0.2942 0.3115 0.3063 -0.0044 -0.0032 0.0240  118 ILE A O   
971  C CB  . ILE A 128 ? 0.2911 0.2978 0.3025 -0.0047 -0.0025 0.0192  118 ILE A CB  
972  C CG1 . ILE A 128 ? 0.2916 0.2938 0.3038 -0.0045 -0.0020 0.0177  118 ILE A CG1 
973  C CG2 . ILE A 128 ? 0.3025 0.3104 0.3135 -0.0054 -0.0027 0.0185  118 ILE A CG2 
974  C CD1 . ILE A 128 ? 0.2857 0.2848 0.2945 -0.0055 -0.0025 0.0148  118 ILE A CD1 
975  N N   . TYR A 129 ? 0.3039 0.3199 0.3207 -0.0027 -0.0024 0.0247  119 TYR A N   
976  C CA  . TYR A 129 ? 0.3136 0.3349 0.3303 -0.0027 -0.0028 0.0259  119 TYR A CA  
977  C C   . TYR A 129 ? 0.3135 0.3359 0.3311 -0.0025 -0.0026 0.0248  119 TYR A C   
978  O O   . TYR A 129 ? 0.2997 0.3192 0.3193 -0.0017 -0.0021 0.0238  119 TYR A O   
979  C CB  . TYR A 129 ? 0.3290 0.3533 0.3482 -0.0012 -0.0028 0.0294  119 TYR A CB  
980  C CG  . TYR A 129 ? 0.3508 0.3718 0.3736 0.0005  -0.0024 0.0308  119 TYR A CG  
981  C CD1 . TYR A 129 ? 0.3682 0.3862 0.3916 0.0004  -0.0022 0.0320  119 TYR A CD1 
982  C CD2 . TYR A 129 ? 0.3655 0.3866 0.3911 0.0023  -0.0022 0.0309  119 TYR A CD2 
983  C CE1 . TYR A 129 ? 0.3826 0.3969 0.4089 0.0018  -0.0019 0.0334  119 TYR A CE1 
984  C CE2 . TYR A 129 ? 0.3801 0.3974 0.4089 0.0042  -0.0020 0.0320  119 TYR A CE2 
985  C CZ  . TYR A 129 ? 0.3899 0.4034 0.4189 0.0037  -0.0019 0.0334  119 TYR A CZ  
986  O OH  . TYR A 129 ? 0.4165 0.4255 0.4483 0.0051  -0.0019 0.0346  119 TYR A OH  
987  N N   . LEU A 130 ? 0.3066 0.3341 0.3230 -0.0034 -0.0031 0.0250  120 LEU A N   
988  C CA  . LEU A 130 ? 0.3128 0.3429 0.3294 -0.0038 -0.0031 0.0237  120 LEU A CA  
989  C C   . LEU A 130 ? 0.3168 0.3499 0.3377 -0.0010 -0.0027 0.0251  120 LEU A C   
990  O O   . LEU A 130 ? 0.3171 0.3531 0.3398 0.0004  -0.0030 0.0277  120 LEU A O   
991  C CB  . LEU A 130 ? 0.3182 0.3529 0.3315 -0.0061 -0.0038 0.0233  120 LEU A CB  
992  C CG  . LEU A 130 ? 0.3256 0.3631 0.3379 -0.0078 -0.0039 0.0215  120 LEU A CG  
993  C CD1 . LEU A 130 ? 0.3250 0.3572 0.3350 -0.0096 -0.0039 0.0191  120 LEU A CD1 
994  C CD2 . LEU A 130 ? 0.3354 0.3781 0.3448 -0.0102 -0.0046 0.0217  120 LEU A CD2 
995  N N   . GLY A 131 ? 0.3124 0.3451 0.3349 -0.0004 -0.0023 0.0234  121 GLY A N   
996  C CA  . GLY A 131 ? 0.3154 0.3510 0.3421 0.0025  -0.0021 0.0240  121 GLY A CA  
997  C C   . GLY A 131 ? 0.3179 0.3566 0.3448 0.0021  -0.0019 0.0214  121 GLY A C   
998  O O   . GLY A 131 ? 0.3158 0.3562 0.3395 -0.0009 -0.0020 0.0198  121 GLY A O   
999  N N   . GLU A 132 ? 0.3275 0.3670 0.3582 0.0051  -0.0016 0.0209  122 GLU A N   
1000 C CA  . GLU A 132 ? 0.3446 0.3874 0.3764 0.0052  -0.0013 0.0182  122 GLU A CA  
1001 C C   . GLU A 132 ? 0.3392 0.3766 0.3737 0.0072  -0.0008 0.0166  122 GLU A C   
1002 O O   . GLU A 132 ? 0.3384 0.3732 0.3761 0.0105  -0.0009 0.0177  122 GLU A O   
1003 C CB  . GLU A 132 ? 0.3606 0.4118 0.3947 0.0074  -0.0016 0.0184  122 GLU A CB  
1004 C CG  . GLU A 132 ? 0.3744 0.4310 0.4095 0.0073  -0.0012 0.0153  122 GLU A CG  
1005 C CD  . GLU A 132 ? 0.3967 0.4626 0.4344 0.0099  -0.0016 0.0154  122 GLU A CD  
1006 O OE1 . GLU A 132 ? 0.4266 0.5002 0.4625 0.0075  -0.0016 0.0143  122 GLU A OE1 
1007 O OE2 . GLU A 132 ? 0.4180 0.4835 0.4592 0.0143  -0.0020 0.0166  122 GLU A OE2 
1008 N N   . TYR A 133 ? 0.3488 0.3844 0.3817 0.0050  -0.0003 0.0141  123 TYR A N   
1009 C CA  . TYR A 133 ? 0.3558 0.3875 0.3911 0.0066  0.0002  0.0121  123 TYR A CA  
1010 C C   . TYR A 133 ? 0.3712 0.4090 0.4098 0.0092  0.0002  0.0103  123 TYR A C   
1011 O O   . TYR A 133 ? 0.3614 0.4067 0.3991 0.0080  0.0001  0.0094  123 TYR A O   
1012 C CB  . TYR A 133 ? 0.3540 0.3828 0.3863 0.0033  0.0006  0.0100  123 TYR A CB  
1013 C CG  . TYR A 133 ? 0.3541 0.3807 0.3888 0.0045  0.0012  0.0074  123 TYR A CG  
1014 C CD1 . TYR A 133 ? 0.3518 0.3715 0.3884 0.0062  0.0015  0.0076  123 TYR A CD1 
1015 C CD2 . TYR A 133 ? 0.3578 0.3894 0.3927 0.0037  0.0015  0.0047  123 TYR A CD2 
1016 C CE1 . TYR A 133 ? 0.3594 0.3771 0.3982 0.0073  0.0020  0.0051  123 TYR A CE1 
1017 C CE2 . TYR A 133 ? 0.3554 0.3855 0.3925 0.0049  0.0021  0.0021  123 TYR A CE2 
1018 C CZ  . TYR A 133 ? 0.3574 0.3804 0.3965 0.0067  0.0024  0.0022  123 TYR A CZ  
1019 O OH  . TYR A 133 ? 0.3649 0.3865 0.4062 0.0078  0.0029  -0.0005 123 TYR A OH  
1020 N N   . GLU A 134 ? 0.3941 0.4288 0.4365 0.0129  0.0003  0.0097  124 GLU A N   
1021 C CA  . GLU A 134 ? 0.4251 0.4645 0.4708 0.0159  0.0004  0.0071  124 GLU A CA  
1022 C C   . GLU A 134 ? 0.4153 0.4494 0.4627 0.0166  0.0009  0.0045  124 GLU A C   
1023 O O   . GLU A 134 ? 0.4084 0.4344 0.4564 0.0175  0.0009  0.0056  124 GLU A O   
1024 C CB  . GLU A 134 ? 0.4640 0.5049 0.5132 0.0206  -0.0004 0.0085  124 GLU A CB  
1025 C CG  . GLU A 134 ? 0.4972 0.5434 0.5455 0.0206  -0.0010 0.0114  124 GLU A CG  
1026 C CD  . GLU A 134 ? 0.5243 0.5746 0.5763 0.0256  -0.0019 0.0119  124 GLU A CD  
1027 O OE1 . GLU A 134 ? 0.5732 0.6308 0.6247 0.0259  -0.0024 0.0132  124 GLU A OE1 
1028 O OE2 . GLU A 134 ? 0.5527 0.5989 0.6078 0.0294  -0.0022 0.0108  124 GLU A OE2 
1029 N N   . GLY A 135 ? 0.4135 0.4523 0.4613 0.0161  0.0014  0.0012  125 GLY A N   
1030 C CA  . GLY A 135 ? 0.4175 0.4525 0.4670 0.0169  0.0020  -0.0016 125 GLY A CA  
1031 C C   . GLY A 135 ? 0.4210 0.4637 0.4732 0.0191  0.0021  -0.0052 125 GLY A C   
1032 O O   . GLY A 135 ? 0.4020 0.4536 0.4542 0.0193  0.0019  -0.0055 125 GLY A O   
1033 N N   . TRP A 136 ? 0.4267 0.4665 0.4811 0.0206  0.0025  -0.0081 126 TRP A N   
1034 C CA  . TRP A 136 ? 0.4413 0.4883 0.4984 0.0228  0.0027  -0.0121 126 TRP A CA  
1035 C C   . TRP A 136 ? 0.4501 0.4978 0.5056 0.0195  0.0037  -0.0149 126 TRP A C   
1036 O O   . TRP A 136 ? 0.4494 0.4898 0.5054 0.0194  0.0040  -0.0158 126 TRP A O   
1037 C CB  . TRP A 136 ? 0.4573 0.5003 0.5189 0.0285  0.0021  -0.0135 126 TRP A CB  
1038 C CG  . TRP A 136 ? 0.4694 0.5117 0.5323 0.0318  0.0010  -0.0105 126 TRP A CG  
1039 C CD1 . TRP A 136 ? 0.4768 0.5105 0.5390 0.0320  0.0004  -0.0066 126 TRP A CD1 
1040 C CD2 . TRP A 136 ? 0.4750 0.5259 0.5398 0.0351  0.0002  -0.0109 126 TRP A CD2 
1041 N NE1 . TRP A 136 ? 0.4825 0.5187 0.5460 0.0353  -0.0006 -0.0045 126 TRP A NE1 
1042 C CE2 . TRP A 136 ? 0.4786 0.5253 0.5438 0.0374  -0.0007 -0.0071 126 TRP A CE2 
1043 C CE3 . TRP A 136 ? 0.4844 0.5470 0.5506 0.0364  0.0004  -0.0142 126 TRP A CE3 
1044 C CZ2 . TRP A 136 ? 0.4901 0.5435 0.5572 0.0412  -0.0017 -0.0064 126 TRP A CZ2 
1045 C CZ3 . TRP A 136 ? 0.4893 0.5590 0.5574 0.0401  -0.0005 -0.0137 126 TRP A CZ3 
1046 C CH2 . TRP A 136 ? 0.4890 0.5539 0.5575 0.0426  -0.0016 -0.0098 126 TRP A CH2 
1047 N N   . TYR A 137 ? 0.4643 0.5209 0.5177 0.0163  0.0040  -0.0160 127 TYR A N   
1048 C CA  . TYR A 137 ? 0.4855 0.5433 0.5366 0.0123  0.0047  -0.0179 127 TYR A CA  
1049 C C   . TYR A 137 ? 0.4977 0.5619 0.5518 0.0142  0.0052  -0.0225 127 TYR A C   
1050 O O   . TYR A 137 ? 0.4940 0.5672 0.5504 0.0166  0.0050  -0.0243 127 TYR A O   
1051 C CB  . TYR A 137 ? 0.4849 0.5483 0.5314 0.0072  0.0046  -0.0164 127 TYR A CB  
1052 C CG  . TYR A 137 ? 0.4833 0.5461 0.5265 0.0026  0.0051  -0.0174 127 TYR A CG  
1053 C CD1 . TYR A 137 ? 0.4812 0.5343 0.5227 0.0013  0.0052  -0.0165 127 TYR A CD1 
1054 C CD2 . TYR A 137 ? 0.4909 0.5631 0.5325 -0.0004 0.0052  -0.0192 127 TYR A CD2 
1055 C CE1 . TYR A 137 ? 0.4853 0.5375 0.5236 -0.0025 0.0054  -0.0173 127 TYR A CE1 
1056 C CE2 . TYR A 137 ? 0.4909 0.5621 0.5291 -0.0047 0.0054  -0.0198 127 TYR A CE2 
1057 C CZ  . TYR A 137 ? 0.4995 0.5606 0.5362 -0.0056 0.0055  -0.0188 127 TYR A CZ  
1058 O OH  . TYR A 137 ? 0.4993 0.5592 0.5326 -0.0095 0.0055  -0.0193 127 TYR A OH  
1059 N N   . SER A 138 ? 0.5208 0.5808 0.5748 0.0130  0.0058  -0.0244 128 SER A N   
1060 C CA  . SER A 138 ? 0.5524 0.6187 0.6085 0.0138  0.0064  -0.0289 128 SER A CA  
1061 C C   . SER A 138 ? 0.5661 0.6359 0.6183 0.0081  0.0069  -0.0293 128 SER A C   
1062 O O   . SER A 138 ? 0.5417 0.6041 0.5911 0.0053  0.0070  -0.0277 128 SER A O   
1063 C CB  . SER A 138 ? 0.5625 0.6210 0.6218 0.0171  0.0066  -0.0311 128 SER A CB  
1064 O OG  . SER A 138 ? 0.5772 0.6417 0.6385 0.0178  0.0072  -0.0358 128 SER A OG  
1065 N N   . VAL A 139 ? 0.6026 0.6839 0.6544 0.0066  0.0071  -0.0314 129 VAL A N   
1066 C CA  . VAL A 139 ? 0.6350 0.7209 0.6828 0.0009  0.0073  -0.0315 129 VAL A CA  
1067 C C   . VAL A 139 ? 0.6473 0.7287 0.6949 -0.0002 0.0080  -0.0334 129 VAL A C   
1068 O O   . VAL A 139 ? 0.6506 0.7262 0.6941 -0.0041 0.0078  -0.0312 129 VAL A O   
1069 C CB  . VAL A 139 ? 0.6509 0.7514 0.6988 -0.0004 0.0074  -0.0336 129 VAL A CB  
1070 C CG1 . VAL A 139 ? 0.6587 0.7635 0.7022 -0.0066 0.0076  -0.0336 129 VAL A CG1 
1071 C CG2 . VAL A 139 ? 0.6567 0.7616 0.7036 -0.0006 0.0068  -0.0311 129 VAL A CG2 
1072 N N   . PRO A 140 ? 0.6622 0.7462 0.7139 0.0032  0.0085  -0.0377 130 PRO A N   
1073 C CA  . PRO A 140 ? 0.6553 0.7363 0.7069 0.0018  0.0092  -0.0398 130 PRO A CA  
1074 C C   . PRO A 140 ? 0.6505 0.7182 0.7015 0.0022  0.0092  -0.0379 130 PRO A C   
1075 O O   . PRO A 140 ? 0.6536 0.7180 0.7023 -0.0007 0.0095  -0.0378 130 PRO A O   
1076 C CB  . PRO A 140 ? 0.6693 0.7564 0.7259 0.0060  0.0096  -0.0449 130 PRO A CB  
1077 C CG  . PRO A 140 ? 0.6738 0.7606 0.7338 0.0112  0.0090  -0.0448 130 PRO A CG  
1078 C CD  . PRO A 140 ? 0.6715 0.7609 0.7284 0.0087  0.0085  -0.0408 130 PRO A CD  
1079 N N   . ASP A 141 ? 0.6336 0.6943 0.6868 0.0059  0.0088  -0.0363 131 ASP A N   
1080 C CA  . ASP A 141 ? 0.6207 0.6695 0.6733 0.0061  0.0087  -0.0342 131 ASP A CA  
1081 C C   . ASP A 141 ? 0.6046 0.6489 0.6524 0.0022  0.0083  -0.0299 131 ASP A C   
1082 O O   . ASP A 141 ? 0.6065 0.6425 0.6529 0.0013  0.0084  -0.0285 131 ASP A O   
1083 C CB  . ASP A 141 ? 0.6217 0.6650 0.6779 0.0109  0.0083  -0.0336 131 ASP A CB  
1084 C CG  . ASP A 141 ? 0.6361 0.6816 0.6970 0.0153  0.0084  -0.0380 131 ASP A CG  
1085 O OD1 . ASP A 141 ? 0.6510 0.6935 0.7131 0.0153  0.0089  -0.0407 131 ASP A OD1 
1086 O OD2 . ASP A 141 ? 0.6191 0.6694 0.6826 0.0189  0.0079  -0.0390 131 ASP A OD2 
1087 N N   . GLU A 142 ? 0.5936 0.6433 0.6386 0.0000  0.0078  -0.0280 132 GLU A N   
1088 C CA  . GLU A 142 ? 0.5859 0.6315 0.6263 -0.0032 0.0072  -0.0240 132 GLU A CA  
1089 C C   . GLU A 142 ? 0.5666 0.6028 0.6077 -0.0011 0.0069  -0.0215 132 GLU A C   
1090 O O   . GLU A 142 ? 0.5527 0.5824 0.5908 -0.0031 0.0067  -0.0194 132 GLU A O   
1091 C CB  . GLU A 142 ? 0.6028 0.6470 0.6390 -0.0077 0.0071  -0.0238 132 GLU A CB  
1092 C CG  . GLU A 142 ? 0.6207 0.6744 0.6550 -0.0109 0.0071  -0.0253 132 GLU A CG  
1093 C CD  . GLU A 142 ? 0.6383 0.6898 0.6673 -0.0157 0.0066  -0.0239 132 GLU A CD  
1094 O OE1 . GLU A 142 ? 0.6388 0.6823 0.6666 -0.0158 0.0065  -0.0231 132 GLU A OE1 
1095 O OE2 . GLU A 142 ? 0.6379 0.6957 0.6637 -0.0194 0.0061  -0.0235 132 GLU A OE2 
1096 N N   . THR A 143 ? 0.5442 0.5802 0.5892 0.0029  0.0068  -0.0217 133 THR A N   
1097 C CA  . THR A 143 ? 0.5357 0.5635 0.5819 0.0052  0.0066  -0.0194 133 THR A CA  
1098 C C   . THR A 143 ? 0.5050 0.5353 0.5526 0.0077  0.0060  -0.0176 133 THR A C   
1099 O O   . THR A 143 ? 0.4734 0.5113 0.5232 0.0096  0.0059  -0.0194 133 THR A O   
1100 C CB  . THR A 143 ? 0.5473 0.5698 0.5971 0.0081  0.0070  -0.0216 133 THR A CB  
1101 O OG1 . THR A 143 ? 0.5458 0.5675 0.5945 0.0058  0.0076  -0.0238 133 THR A OG1 
1102 C CG2 . THR A 143 ? 0.5526 0.5660 0.6029 0.0093  0.0067  -0.0189 133 THR A CG2 
1103 N N   . TYR A 144 ? 0.4854 0.5101 0.5318 0.0077  0.0055  -0.0142 134 TYR A N   
1104 C CA  . TYR A 144 ? 0.4882 0.5137 0.5361 0.0104  0.0048  -0.0120 134 TYR A CA  
1105 C C   . TYR A 144 ? 0.4969 0.5151 0.5480 0.0139  0.0046  -0.0115 134 TYR A C   
1106 O O   . TYR A 144 ? 0.4983 0.5091 0.5484 0.0128  0.0048  -0.0103 134 TYR A O   
1107 C CB  . TYR A 144 ? 0.4823 0.5068 0.5265 0.0078  0.0044  -0.0084 134 TYR A CB  
1108 C CG  . TYR A 144 ? 0.4775 0.5080 0.5180 0.0040  0.0043  -0.0085 134 TYR A CG  
1109 C CD1 . TYR A 144 ? 0.4749 0.5130 0.5151 0.0040  0.0038  -0.0078 134 TYR A CD1 
1110 C CD2 . TYR A 144 ? 0.4770 0.5058 0.5141 0.0004  0.0045  -0.0091 134 TYR A CD2 
1111 C CE1 . TYR A 144 ? 0.4825 0.5258 0.5189 0.0000  0.0036  -0.0077 134 TYR A CE1 
1112 C CE2 . TYR A 144 ? 0.4824 0.5158 0.5156 -0.0033 0.0041  -0.0089 134 TYR A CE2 
1113 C CZ  . TYR A 144 ? 0.4844 0.5250 0.5172 -0.0037 0.0037  -0.0082 134 TYR A CZ  
1114 O OH  . TYR A 144 ? 0.4896 0.5346 0.5183 -0.0080 0.0032  -0.0079 134 TYR A OH  
1115 N N   . TYR A 145 ? 0.5103 0.5306 0.5649 0.0180  0.0041  -0.0124 135 TYR A N   
1116 C CA  . TYR A 145 ? 0.5266 0.5396 0.5842 0.0216  0.0036  -0.0118 135 TYR A CA  
1117 C C   . TYR A 145 ? 0.5342 0.5464 0.5921 0.0235  0.0026  -0.0081 135 TYR A C   
1118 O O   . TYR A 145 ? 0.5125 0.5316 0.5697 0.0235  0.0024  -0.0071 135 TYR A O   
1119 C CB  . TYR A 145 ? 0.5368 0.5517 0.5983 0.0255  0.0035  -0.0158 135 TYR A CB  
1120 C CG  . TYR A 145 ? 0.5373 0.5537 0.5989 0.0238  0.0044  -0.0197 135 TYR A CG  
1121 C CD1 . TYR A 145 ? 0.5429 0.5690 0.6042 0.0228  0.0050  -0.0225 135 TYR A CD1 
1122 C CD2 . TYR A 145 ? 0.5486 0.5570 0.6104 0.0230  0.0048  -0.0205 135 TYR A CD2 
1123 C CE1 . TYR A 145 ? 0.5506 0.5785 0.6118 0.0211  0.0058  -0.0260 135 TYR A CE1 
1124 C CE2 . TYR A 145 ? 0.5553 0.5654 0.6171 0.0214  0.0057  -0.0241 135 TYR A CE2 
1125 C CZ  . TYR A 145 ? 0.5570 0.5768 0.6185 0.0205  0.0062  -0.0268 135 TYR A CZ  
1126 O OH  . TYR A 145 ? 0.5659 0.5879 0.6274 0.0188  0.0070  -0.0302 135 TYR A OH  
1127 N N   . THR A 146 ? 0.5495 0.5533 0.6084 0.0250  0.0020  -0.0060 136 THR A N   
1128 C CA  . THR A 146 ? 0.5707 0.5731 0.6306 0.0277  0.0009  -0.0026 136 THR A CA  
1129 C C   . THR A 146 ? 0.5972 0.6015 0.6609 0.0329  0.0000  -0.0048 136 THR A C   
1130 O O   . THR A 146 ? 0.6028 0.6074 0.6685 0.0344  0.0003  -0.0088 136 THR A O   
1131 C CB  . THR A 146 ? 0.5728 0.5655 0.6322 0.0271  0.0004  0.0005  136 THR A CB  
1132 O OG1 . THR A 146 ? 0.5723 0.5581 0.6339 0.0287  0.0003  -0.0014 136 THR A OG1 
1133 C CG2 . THR A 146 ? 0.5648 0.5560 0.6205 0.0223  0.0013  0.0022  136 THR A CG2 
1134 N N   . GLU A 147 ? 0.6338 0.6399 0.6985 0.0357  -0.0010 -0.0023 137 GLU A N   
1135 C CA  . GLU A 147 ? 0.6639 0.6720 0.7321 0.0413  -0.0022 -0.0042 137 GLU A CA  
1136 C C   . GLU A 147 ? 0.6778 0.6761 0.7485 0.0444  -0.0031 -0.0055 137 GLU A C   
1137 O O   . GLU A 147 ? 0.6696 0.6696 0.7432 0.0484  -0.0036 -0.0093 137 GLU A O   
1138 C CB  . GLU A 147 ? 0.6852 0.6969 0.7538 0.0438  -0.0034 -0.0008 137 GLU A CB  
1139 C CG  . GLU A 147 ? 0.7074 0.7107 0.7750 0.0436  -0.0044 0.0041  137 GLU A CG  
1140 C CD  . GLU A 147 ? 0.7259 0.7338 0.7938 0.0462  -0.0056 0.0073  137 GLU A CD  
1141 O OE1 . GLU A 147 ? 0.7364 0.7544 0.8038 0.0457  -0.0052 0.0067  137 GLU A OE1 
1142 O OE2 . GLU A 147 ? 0.7462 0.7474 0.8148 0.0485  -0.0070 0.0105  137 GLU A OE2 
1143 N N   . SER A 148 ? 0.7086 0.6972 0.7779 0.0423  -0.0032 -0.0026 138 SER A N   
1144 C CA  . SER A 148 ? 0.7301 0.7081 0.8011 0.0442  -0.0041 -0.0034 138 SER A CA  
1145 C C   . SER A 148 ? 0.7396 0.7165 0.8115 0.0433  -0.0030 -0.0083 138 SER A C   
1146 O O   . SER A 148 ? 0.7445 0.7146 0.8184 0.0458  -0.0039 -0.0104 138 SER A O   
1147 C CB  . SER A 148 ? 0.7312 0.7002 0.8002 0.0414  -0.0045 0.0012  138 SER A CB  
1148 O OG  . SER A 148 ? 0.7288 0.6981 0.7950 0.0361  -0.0029 0.0017  138 SER A OG  
1149 N N   . GLN A 149 ? 0.7434 0.7266 0.8135 0.0395  -0.0014 -0.0100 139 GLN A N   
1150 C CA  . GLN A 149 ? 0.7541 0.7380 0.8249 0.0384  -0.0003 -0.0147 139 GLN A CA  
1151 C C   . GLN A 149 ? 0.7694 0.7611 0.8430 0.0420  -0.0003 -0.0196 139 GLN A C   
1152 O O   . GLN A 149 ? 0.7779 0.7695 0.8527 0.0421  0.0002  -0.0239 139 GLN A O   
1153 C CB  . GLN A 149 ? 0.7380 0.7253 0.8055 0.0330  0.0012  -0.0143 139 GLN A CB  
1154 C CG  . GLN A 149 ? 0.7347 0.7144 0.7998 0.0294  0.0015  -0.0108 139 GLN A CG  
1155 C CD  . GLN A 149 ? 0.7267 0.7100 0.7884 0.0246  0.0028  -0.0104 139 GLN A CD  
1156 O OE1 . GLN A 149 ? 0.7125 0.7034 0.7727 0.0236  0.0031  -0.0102 139 GLN A OE1 
1157 N NE2 . GLN A 149 ? 0.7276 0.7057 0.7880 0.0218  0.0034  -0.0104 139 GLN A NE2 
1158 N N   . LEU A 150 ? 0.7884 0.7876 0.8630 0.0449  -0.0010 -0.0192 140 LEU A N   
1159 C CA  . LEU A 150 ? 0.8119 0.8206 0.8889 0.0482  -0.0010 -0.0239 140 LEU A CA  
1160 C C   . LEU A 150 ? 0.8511 0.8550 0.9318 0.0537  -0.0023 -0.0275 140 LEU A C   
1161 O O   . LEU A 150 ? 0.8426 0.8373 0.9242 0.0565  -0.0038 -0.0253 140 LEU A O   
1162 C CB  . LEU A 150 ? 0.8027 0.8211 0.8799 0.0498  -0.0015 -0.0223 140 LEU A CB  
1163 C CG  . LEU A 150 ? 0.7892 0.8132 0.8627 0.0447  -0.0005 -0.0192 140 LEU A CG  
1164 C CD1 . LEU A 150 ? 0.7855 0.8189 0.8595 0.0468  -0.0012 -0.0179 140 LEU A CD1 
1165 C CD2 . LEU A 150 ? 0.7729 0.8028 0.8445 0.0401  0.0010  -0.0218 140 LEU A CD2 
1166 N N   . VAL A 151 ? 0.8936 0.9039 0.9763 0.0551  -0.0017 -0.0330 141 VAL A N   
1167 C CA  . VAL A 151 ? 0.9426 0.9477 1.0285 0.0597  -0.0027 -0.0374 141 VAL A CA  
1168 C C   . VAL A 151 ? 0.9645 0.9729 1.0537 0.0668  -0.0045 -0.0393 141 VAL A C   
1169 O O   . VAL A 151 ? 0.9847 0.9833 1.0757 0.0711  -0.0063 -0.0396 141 VAL A O   
1170 C CB  . VAL A 151 ? 0.9600 0.9696 1.0465 0.0578  -0.0012 -0.0428 141 VAL A CB  
1171 N N   . ASP A 152 ? 0.9749 0.9966 1.0648 0.0681  -0.0043 -0.0406 142 ASP A N   
1172 C CA  . ASP A 152 ? 0.9797 1.0069 1.0727 0.0751  -0.0060 -0.0427 142 ASP A CA  
1173 C C   . ASP A 152 ? 0.9706 1.0030 1.0624 0.0751  -0.0065 -0.0379 142 ASP A C   
1174 O O   . ASP A 152 ? 0.9487 0.9948 1.0409 0.0755  -0.0060 -0.0393 142 ASP A O   
1175 C CB  . ASP A 152 ? 0.9766 1.0172 1.0721 0.0772  -0.0053 -0.0492 142 ASP A CB  
1176 C CG  . ASP A 152 ? 0.9871 1.0226 1.0852 0.0803  -0.0057 -0.0549 142 ASP A CG  
1177 O OD1 . ASP A 152 ? 0.9860 1.0071 1.0840 0.0809  -0.0066 -0.0539 142 ASP A OD1 
1178 O OD2 . ASP A 152 ? 0.9769 1.0233 1.0770 0.0820  -0.0051 -0.0605 142 ASP A OD2 
1179 N N   . PRO A 153 ? 0.9794 1.0015 1.0697 0.0744  -0.0074 -0.0323 143 PRO A N   
1180 C CA  . PRO A 153 ? 0.9825 1.0093 1.0710 0.0732  -0.0076 -0.0275 143 PRO A CA  
1181 C C   . PRO A 153 ? 0.9922 1.0276 1.0832 0.0794  -0.0091 -0.0285 143 PRO A C   
1182 O O   . PRO A 153 ? 0.9994 1.0288 1.0928 0.0855  -0.0112 -0.0291 143 PRO A O   
1183 C CB  . PRO A 153 ? 0.9864 0.9992 1.0731 0.0719  -0.0085 -0.0219 143 PRO A CB  
1184 C CG  . PRO A 153 ? 0.9929 0.9943 1.0816 0.0755  -0.0098 -0.0242 143 PRO A CG  
1185 C CD  . PRO A 153 ? 0.9920 0.9980 1.0819 0.0747  -0.0085 -0.0303 143 PRO A CD  
1186 N N   . GLN A 154 ? 0.9850 1.0344 1.0753 0.0776  -0.0081 -0.0287 144 GLN A N   
1187 C CA  . GLN A 154 ? 0.9883 1.0484 1.0807 0.0826  -0.0093 -0.0294 144 GLN A CA  
1188 C C   . GLN A 154 ? 0.9882 1.0456 1.0787 0.0820  -0.0102 -0.0231 144 GLN A C   
1189 O O   . GLN A 154 ? 0.9952 1.0518 1.0823 0.0758  -0.0089 -0.0193 144 GLN A O   
1190 C CB  . GLN A 154 ? 0.9777 1.0547 1.0698 0.0801  -0.0078 -0.0325 144 GLN A CB  
1191 C CG  . GLN A 154 ? 0.9760 1.0573 1.0693 0.0793  -0.0066 -0.0384 144 GLN A CG  
1192 C CD  . GLN A 154 ? 0.9892 1.0698 1.0867 0.0869  -0.0081 -0.0435 144 GLN A CD  
1193 O OE1 . GLN A 154 ? 0.9828 1.0715 1.0830 0.0927  -0.0094 -0.0453 144 GLN A OE1 
1194 N NE2 . GLN A 154 ? 0.9930 1.0639 1.0913 0.0872  -0.0080 -0.0462 144 GLN A NE2 
1195 N N   . TYR A 155 ? 0.9772 1.0333 1.0699 0.0884  -0.0124 -0.0221 145 TYR A N   
1196 C CA  . TYR A 155 ? 0.9772 1.0303 1.0686 0.0886  -0.0136 -0.0160 145 TYR A CA  
1197 C C   . TYR A 155 ? 0.9981 1.0652 1.0904 0.0916  -0.0142 -0.0159 145 TYR A C   
1198 O O   . TYR A 155 ? 0.9856 1.0634 1.0807 0.0957  -0.0145 -0.0207 145 TYR A O   
1199 C CB  . TYR A 155 ? 0.9611 0.9992 1.0535 0.0931  -0.0159 -0.0137 145 TYR A CB  
1200 C CG  . TYR A 155 ? 0.9328 0.9564 1.0229 0.0885  -0.0154 -0.0112 145 TYR A CG  
1201 C CD1 . TYR A 155 ? 0.9176 0.9351 1.0084 0.0878  -0.0147 -0.0152 145 TYR A CD1 
1202 C CD2 . TYR A 155 ? 0.9225 0.9391 1.0098 0.0849  -0.0155 -0.0049 145 TYR A CD2 
1203 C CE1 . TYR A 155 ? 0.9124 0.9173 1.0012 0.0835  -0.0142 -0.0130 145 TYR A CE1 
1204 C CE2 . TYR A 155 ? 0.9201 0.9245 1.0054 0.0806  -0.0150 -0.0028 145 TYR A CE2 
1205 C CZ  . TYR A 155 ? 0.9107 0.9092 0.9967 0.0799  -0.0143 -0.0068 145 TYR A CZ  
1206 O OH  . TYR A 155 ? 0.8935 0.8807 0.9775 0.0755  -0.0138 -0.0047 145 TYR A OH  
1207 N N   . GLU A 156 ? 1.0304 1.0982 1.1207 0.0894  -0.0144 -0.0105 146 GLU A N   
1208 C CA  . GLU A 156 ? 1.0562 1.1360 1.1473 0.0924  -0.0153 -0.0094 146 GLU A CA  
1209 C C   . GLU A 156 ? 1.0568 1.1309 1.1459 0.0913  -0.0162 -0.0028 146 GLU A C   
1210 O O   . GLU A 156 ? 1.0538 1.1249 1.1395 0.0849  -0.0149 0.0005  146 GLU A O   
1211 C CB  . GLU A 156 ? 1.0646 1.1601 1.1543 0.0877  -0.0132 -0.0114 146 GLU A CB  
1212 C CG  . GLU A 156 ? 1.0773 1.1872 1.1681 0.0906  -0.0140 -0.0112 146 GLU A CG  
1213 C CD  . GLU A 156 ? 1.0839 1.2096 1.1734 0.0859  -0.0121 -0.0137 146 GLU A CD  
1214 O OE1 . GLU A 156 ? 1.0974 1.2370 1.1885 0.0889  -0.0127 -0.0152 146 GLU A OE1 
1215 O OE2 . GLU A 156 ? 1.0916 1.2160 1.1784 0.0791  -0.0102 -0.0141 146 GLU A OE2 
1216 N N   . ASN A 157 ? 1.0590 1.1317 1.1500 0.0979  -0.0187 -0.0011 147 ASN A N   
1217 C CA  . ASN A 157 ? 1.0624 1.1296 1.1518 0.0978  -0.0200 0.0052  147 ASN A CA  
1218 C C   . ASN A 157 ? 1.0644 1.1156 1.1513 0.0937  -0.0199 0.0093  147 ASN A C   
1219 O O   . ASN A 157 ? 1.0696 1.1187 1.1539 0.0898  -0.0197 0.0144  147 ASN A O   
1220 C CB  . ASN A 157 ? 1.0475 1.1275 1.1349 0.0939  -0.0189 0.0076  147 ASN A CB  
1221 N N   . GLY A 158 ? 1.0565 1.0972 1.1443 0.0945  -0.0200 0.0067  148 GLY A N   
1222 C CA  . GLY A 158 ? 1.0495 1.0754 1.1352 0.0906  -0.0199 0.0099  148 GLY A CA  
1223 C C   . GLY A 158 ? 1.0335 1.0604 1.1160 0.0823  -0.0172 0.0106  148 GLY A C   
1224 O O   . GLY A 158 ? 1.0527 1.0728 1.1326 0.0782  -0.0169 0.0153  148 GLY A O   
1225 N N   . LYS A 159 ? 0.9881 1.0235 1.0708 0.0800  -0.0152 0.0061  149 LYS A N   
1226 C CA  . LYS A 159 ? 0.9457 0.9827 1.0254 0.0725  -0.0128 0.0063  149 LYS A CA  
1227 C C   . LYS A 159 ? 0.9080 0.9502 0.9885 0.0713  -0.0112 0.0005  149 LYS A C   
1228 O O   . LYS A 159 ? 0.8910 0.9433 0.9737 0.0747  -0.0113 -0.0032 149 LYS A O   
1229 C CB  . LYS A 159 ? 0.9313 0.9783 1.0087 0.0692  -0.0120 0.0090  149 LYS A CB  
1230 N N   . ILE A 160 ? 0.8692 0.9049 0.9479 0.0666  -0.0098 -0.0001 150 ILE A N   
1231 C CA  . ILE A 160 ? 0.8386 0.8779 0.9180 0.0651  -0.0083 -0.0053 150 ILE A CA  
1232 C C   . ILE A 160 ? 0.8048 0.8576 0.8825 0.0614  -0.0068 -0.0066 150 ILE A C   
1233 O O   . ILE A 160 ? 0.7885 0.8425 0.8629 0.0564  -0.0060 -0.0035 150 ILE A O   
1234 C CB  . ILE A 160 ? 0.8384 0.8670 0.9160 0.0609  -0.0073 -0.0054 150 ILE A CB  
1235 C CG1 . ILE A 160 ? 0.8490 0.8643 0.9282 0.0642  -0.0088 -0.0043 150 ILE A CG1 
1236 C CG2 . ILE A 160 ? 0.8309 0.8641 0.9090 0.0592  -0.0058 -0.0106 150 ILE A CG2 
1237 C CD1 . ILE A 160 ? 0.8469 0.8513 0.9239 0.0597  -0.0080 -0.0027 150 ILE A CD1 
1238 N N   . ILE A 161 ? 0.7866 0.8496 0.8665 0.0639  -0.0067 -0.0113 151 ILE A N   
1239 C CA  . ILE A 161 ? 0.7819 0.8590 0.8605 0.0607  -0.0055 -0.0129 151 ILE A CA  
1240 C C   . ILE A 161 ? 0.7653 0.8462 0.8434 0.0575  -0.0040 -0.0173 151 ILE A C   
1241 O O   . ILE A 161 ? 0.7364 0.8272 0.8125 0.0532  -0.0028 -0.0182 151 ILE A O   
1242 C CB  . ILE A 161 ? 0.7928 0.8815 0.8741 0.0661  -0.0067 -0.0142 151 ILE A CB  
1243 C CG1 . ILE A 161 ? 0.7997 0.8875 0.8802 0.0670  -0.0078 -0.0090 151 ILE A CG1 
1244 C CG2 . ILE A 161 ? 0.7966 0.9012 0.8776 0.0638  -0.0056 -0.0176 151 ILE A CG2 
1245 C CD1 . ILE A 161 ? 0.7951 0.8925 0.8724 0.0619  -0.0069 -0.0068 151 ILE A CD1 
1246 N N   . GLY A 162 ? 0.7626 0.8354 0.8423 0.0592  -0.0039 -0.0199 152 GLY A N   
1247 C CA  . GLY A 162 ? 0.7599 0.8364 0.8396 0.0567  -0.0026 -0.0243 152 GLY A CA  
1248 C C   . GLY A 162 ? 0.7597 0.8250 0.8411 0.0585  -0.0028 -0.0264 152 GLY A C   
1249 O O   . GLY A 162 ? 0.7550 0.8093 0.8375 0.0616  -0.0040 -0.0244 152 GLY A O   
1250 N N   . GLY A 163 ? 0.7437 0.8117 0.8250 0.0562  -0.0015 -0.0302 153 GLY A N   
1251 C CA  . GLY A 163 ? 0.7423 0.8009 0.8250 0.0574  -0.0015 -0.0329 153 GLY A CA  
1252 C C   . GLY A 163 ? 0.7340 0.7970 0.8158 0.0534  0.0000  -0.0365 153 GLY A C   
1253 O O   . GLY A 163 ? 0.7225 0.7972 0.8031 0.0507  0.0009  -0.0379 153 GLY A O   
1254 N N   . LYS A 164 ? 0.7352 0.7885 0.8174 0.0530  0.0003  -0.0378 154 LYS A N   
1255 C CA  . LYS A 164 ? 0.7319 0.7877 0.8132 0.0494  0.0017  -0.0412 154 LYS A CA  
1256 C C   . LYS A 164 ? 0.7286 0.7726 0.8074 0.0453  0.0023  -0.0386 154 LYS A C   
1257 O O   . LYS A 164 ? 0.7247 0.7578 0.8035 0.0464  0.0015  -0.0356 154 LYS A O   
1258 C CB  . LYS A 164 ? 0.7337 0.7920 0.8188 0.0541  0.0014  -0.0473 154 LYS A CB  
1259 N N   . SER A 165 ? 0.7314 0.7781 0.8079 0.0404  0.0037  -0.0398 155 SER A N   
1260 C CA  . SER A 165 ? 0.7460 0.7832 0.8200 0.0363  0.0043  -0.0377 155 SER A CA  
1261 C C   . SER A 165 ? 0.7663 0.7941 0.8428 0.0389  0.0041  -0.0402 155 SER A C   
1262 O O   . SER A 165 ? 0.7681 0.7995 0.8474 0.0416  0.0041  -0.0451 155 SER A O   
1263 C CB  . SER A 165 ? 0.7349 0.7783 0.8060 0.0309  0.0057  -0.0386 155 SER A CB  
1264 O OG  . SER A 165 ? 0.7232 0.7583 0.7925 0.0277  0.0063  -0.0379 155 SER A OG  
1265 N N   . PRO A 166 ? 0.7933 0.8094 0.8686 0.0377  0.0038  -0.0370 156 PRO A N   
1266 C CA  . PRO A 166 ? 0.8136 0.8204 0.8908 0.0393  0.0035  -0.0392 156 PRO A CA  
1267 C C   . PRO A 166 ? 0.8317 0.8399 0.9084 0.0362  0.0048  -0.0427 156 PRO A C   
1268 O O   . PRO A 166 ? 0.8408 0.8447 0.9196 0.0381  0.0047  -0.0463 156 PRO A O   
1269 C CB  . PRO A 166 ? 0.8143 0.8100 0.8898 0.0378  0.0030  -0.0342 156 PRO A CB  
1270 C CG  . PRO A 166 ? 0.8041 0.8037 0.8760 0.0335  0.0037  -0.0303 156 PRO A CG  
1271 C CD  . PRO A 166 ? 0.7974 0.8086 0.8696 0.0346  0.0037  -0.0314 156 PRO A CD  
1272 N N   . ASP A 167 ? 0.8447 0.8585 0.9183 0.0314  0.0060  -0.0416 157 ASP A N   
1273 C CA  . ASP A 167 ? 0.8470 0.8627 0.9195 0.0281  0.0072  -0.0444 157 ASP A CA  
1274 C C   . ASP A 167 ? 0.8515 0.8780 0.9259 0.0294  0.0076  -0.0496 157 ASP A C   
1275 O O   . ASP A 167 ? 0.8806 0.9064 0.9572 0.0307  0.0079  -0.0539 157 ASP A O   
1276 C CB  . ASP A 167 ? 0.8430 0.8597 0.9111 0.0227  0.0079  -0.0409 157 ASP A CB  
1277 C CG  . ASP A 167 ? 0.8468 0.8534 0.9131 0.0212  0.0076  -0.0365 157 ASP A CG  
1278 O OD1 . ASP A 167 ? 0.8380 0.8450 0.9017 0.0195  0.0074  -0.0325 157 ASP A OD1 
1279 O OD2 . ASP A 167 ? 0.8462 0.8448 0.9135 0.0215  0.0076  -0.0370 157 ASP A OD2 
1280 N N   . SER A 168 ? 0.8415 0.8783 0.9150 0.0288  0.0077  -0.0492 158 SER A N   
1281 C CA  . SER A 168 ? 0.8404 0.8895 0.9153 0.0292  0.0082  -0.0538 158 SER A CA  
1282 C C   . SER A 168 ? 0.8497 0.9049 0.9285 0.0350  0.0074  -0.0568 158 SER A C   
1283 O O   . SER A 168 ? 0.8714 0.9342 0.9527 0.0370  0.0076  -0.0620 158 SER A O   
1284 C CB  . SER A 168 ? 0.8326 0.8908 0.9039 0.0243  0.0088  -0.0518 158 SER A CB  
1285 O OG  . SER A 168 ? 0.8251 0.8865 0.8956 0.0250  0.0082  -0.0487 158 SER A OG  
1286 N N   . GLY A 169 ? 0.8476 0.9001 0.9269 0.0377  0.0063  -0.0537 159 GLY A N   
1287 C CA  . GLY A 169 ? 0.8450 0.9039 0.9276 0.0433  0.0053  -0.0560 159 GLY A CA  
1288 C C   . GLY A 169 ? 0.8335 0.9059 0.9150 0.0420  0.0055  -0.0553 159 GLY A C   
1289 O O   . GLY A 169 ? 0.8338 0.9142 0.9181 0.0464  0.0048  -0.0578 159 GLY A O   
1290 N N   . HIS A 170 ? 0.8266 0.9016 0.9039 0.0359  0.0063  -0.0520 160 HIS A N   
1291 C CA  . HIS A 170 ? 0.8129 0.9001 0.8884 0.0336  0.0065  -0.0509 160 HIS A CA  
1292 C C   . HIS A 170 ? 0.7882 0.8739 0.8636 0.0357  0.0055  -0.0470 160 HIS A C   
1293 O O   . HIS A 170 ? 0.7587 0.8330 0.8336 0.0364  0.0049  -0.0435 160 HIS A O   
1294 C CB  . HIS A 170 ? 0.8293 0.9181 0.9000 0.0264  0.0074  -0.0486 160 HIS A CB  
1295 C CG  . HIS A 170 ? 0.8484 0.9505 0.9170 0.0231  0.0076  -0.0484 160 HIS A CG  
1296 N ND1 . HIS A 170 ? 0.8577 0.9722 0.9270 0.0220  0.0082  -0.0525 160 HIS A ND1 
1297 C CD2 . HIS A 170 ? 0.8521 0.9572 0.9177 0.0203  0.0073  -0.0445 160 HIS A CD2 
1298 C CE1 . HIS A 170 ? 0.8495 0.9740 0.9161 0.0185  0.0082  -0.0510 160 HIS A CE1 
1299 N NE2 . HIS A 170 ? 0.8499 0.9687 0.9142 0.0174  0.0076  -0.0462 160 HIS A NE2 
1300 N N   . GLU A 171 ? 0.7616 0.8597 0.8375 0.0365  0.0052  -0.0478 161 GLU A N   
1301 C CA  . GLU A 171 ? 0.7554 0.8546 0.8314 0.0386  0.0043  -0.0445 161 GLU A CA  
1302 C C   . GLU A 171 ? 0.7315 0.8258 0.8028 0.0332  0.0045  -0.0390 161 GLU A C   
1303 O O   . GLU A 171 ? 0.7296 0.8296 0.7974 0.0276  0.0052  -0.0382 161 GLU A O   
1304 C CB  . GLU A 171 ? 0.7699 0.8855 0.8473 0.0401  0.0042  -0.0471 161 GLU A CB  
1305 C CG  . GLU A 171 ? 0.7819 0.9010 0.8599 0.0428  0.0031  -0.0444 161 GLU A CG  
1306 C CD  . GLU A 171 ? 0.7973 0.9111 0.8795 0.0507  0.0017  -0.0453 161 GLU A CD  
1307 O OE1 . GLU A 171 ? 0.7952 0.9117 0.8780 0.0532  0.0008  -0.0430 161 GLU A OE1 
1308 O OE2 . GLU A 171 ? 0.8107 0.9176 0.8956 0.0543  0.0014  -0.0483 161 GLU A OE2 
1309 N N   . VAL A 172 ? 0.6937 0.7774 0.7649 0.0348  0.0038  -0.0352 162 VAL A N   
1310 C CA  . VAL A 172 ? 0.6537 0.7327 0.7208 0.0302  0.0039  -0.0301 162 VAL A CA  
1311 C C   . VAL A 172 ? 0.6134 0.7013 0.6792 0.0295  0.0034  -0.0280 162 VAL A C   
1312 O O   . VAL A 172 ? 0.6018 0.6977 0.6705 0.0336  0.0029  -0.0297 162 VAL A O   
1313 C CB  . VAL A 172 ? 0.6603 0.7254 0.7273 0.0316  0.0033  -0.0267 162 VAL A CB  
1314 C CG1 . VAL A 172 ? 0.6637 0.7198 0.7314 0.0314  0.0038  -0.0285 162 VAL A CG1 
1315 C CG2 . VAL A 172 ? 0.6613 0.7248 0.7316 0.0375  0.0020  -0.0258 162 VAL A CG2 
1316 N N   . GLU A 173 ? 0.5632 0.6495 0.6247 0.0244  0.0036  -0.0244 163 GLU A N   
1317 C CA  . GLU A 173 ? 0.5244 0.6180 0.5840 0.0228  0.0032  -0.0220 163 GLU A CA  
1318 C C   . GLU A 173 ? 0.5274 0.6121 0.5846 0.0214  0.0028  -0.0172 163 GLU A C   
1319 O O   . GLU A 173 ? 0.5185 0.5942 0.5732 0.0185  0.0031  -0.0155 163 GLU A O   
1320 C CB  . GLU A 173 ? 0.4805 0.5835 0.5366 0.0170  0.0038  -0.0227 163 GLU A CB  
1321 C CG  . GLU A 173 ? 0.4686 0.5647 0.5199 0.0110  0.0042  -0.0208 163 GLU A CG  
1322 C CD  . GLU A 173 ? 0.4666 0.5716 0.5146 0.0055  0.0046  -0.0221 163 GLU A CD  
1323 O OE1 . GLU A 173 ? 0.4718 0.5867 0.5186 0.0037  0.0043  -0.0217 163 GLU A OE1 
1324 O OE2 . GLU A 173 ? 0.4687 0.5708 0.5151 0.0028  0.0051  -0.0233 163 GLU A OE2 
1325 N N   . LEU A 174 ? 0.5183 0.6065 0.5763 0.0237  0.0020  -0.0151 164 LEU A N   
1326 C CA  . LEU A 174 ? 0.5196 0.6008 0.5758 0.0230  0.0015  -0.0107 164 LEU A CA  
1327 C C   . LEU A 174 ? 0.4954 0.5777 0.5465 0.0167  0.0018  -0.0086 164 LEU A C   
1328 O O   . LEU A 174 ? 0.4676 0.5596 0.5170 0.0140  0.0019  -0.0093 164 LEU A O   
1329 C CB  . LEU A 174 ? 0.5353 0.6214 0.5940 0.0273  0.0006  -0.0093 164 LEU A CB  
1330 C CG  . LEU A 174 ? 0.5503 0.6313 0.6074 0.0270  0.0000  -0.0047 164 LEU A CG  
1331 C CD1 . LEU A 174 ? 0.5553 0.6230 0.6122 0.0273  0.0000  -0.0027 164 LEU A CD1 
1332 C CD2 . LEU A 174 ? 0.5607 0.6475 0.6208 0.0320  -0.0010 -0.0040 164 LEU A CD2 
1333 N N   . VAL A 175 ? 0.4678 0.5401 0.5163 0.0144  0.0019  -0.0061 165 VAL A N   
1334 C CA  . VAL A 175 ? 0.4582 0.5297 0.5016 0.0089  0.0018  -0.0041 165 VAL A CA  
1335 C C   . VAL A 175 ? 0.4344 0.5002 0.4767 0.0092  0.0013  -0.0003 165 VAL A C   
1336 O O   . VAL A 175 ? 0.4209 0.4788 0.4650 0.0118  0.0012  0.0008  165 VAL A O   
1337 C CB  . VAL A 175 ? 0.4743 0.5405 0.5148 0.0050  0.0023  -0.0051 165 VAL A CB  
1338 C CG1 . VAL A 175 ? 0.4820 0.5558 0.5230 0.0037  0.0028  -0.0086 165 VAL A CG1 
1339 C CG2 . VAL A 175 ? 0.4864 0.5421 0.5285 0.0072  0.0026  -0.0051 165 VAL A CG2 
1340 N N   . LYS A 176 ? 0.4180 0.4884 0.4575 0.0065  0.0009  0.0014  166 LYS A N   
1341 C CA  . LYS A 176 ? 0.4156 0.4821 0.4536 0.0063  0.0003  0.0048  166 LYS A CA  
1342 C C   . LYS A 176 ? 0.3939 0.4599 0.4265 0.0008  0.0001  0.0057  166 LYS A C   
1343 O O   . LYS A 176 ? 0.3797 0.4524 0.4101 -0.0023 0.0001  0.0045  166 LYS A O   
1344 C CB  . LYS A 176 ? 0.4350 0.5083 0.4752 0.0093  -0.0001 0.0062  166 LYS A CB  
1345 C CG  . LYS A 176 ? 0.4593 0.5324 0.5046 0.0153  -0.0003 0.0056  166 LYS A CG  
1346 C CD  . LYS A 176 ? 0.4818 0.5609 0.5288 0.0182  -0.0011 0.0076  166 LYS A CD  
1347 C CE  . LYS A 176 ? 0.5067 0.5870 0.5586 0.0244  -0.0016 0.0065  166 LYS A CE  
1348 N NZ  . LYS A 176 ? 0.5223 0.6068 0.5758 0.0276  -0.0026 0.0091  166 LYS A NZ  
1349 N N   . GLU A 177 ? 0.3629 0.4212 0.3933 -0.0003 0.0000  0.0077  167 GLU A N   
1350 C CA  . GLU A 177 ? 0.3508 0.4080 0.3760 -0.0049 -0.0005 0.0087  167 GLU A CA  
1351 C C   . GLU A 177 ? 0.3344 0.3850 0.3584 -0.0045 -0.0009 0.0111  167 GLU A C   
1352 O O   . GLU A 177 ? 0.3261 0.3710 0.3524 -0.0019 -0.0006 0.0117  167 GLU A O   
1353 C CB  . GLU A 177 ? 0.3509 0.4048 0.3729 -0.0085 -0.0004 0.0069  167 GLU A CB  
1354 C CG  . GLU A 177 ? 0.3520 0.3971 0.3748 -0.0073 0.0000  0.0063  167 GLU A CG  
1355 C CD  . GLU A 177 ? 0.3604 0.4032 0.3800 -0.0108 0.0000  0.0046  167 GLU A CD  
1356 O OE1 . GLU A 177 ? 0.3548 0.3921 0.3701 -0.0135 -0.0007 0.0053  167 GLU A OE1 
1357 O OE2 . GLU A 177 ? 0.3685 0.4152 0.3896 -0.0107 0.0004  0.0025  167 GLU A OE2 
1358 N N   . GLU A 178 ? 0.3260 0.3779 0.3463 -0.0074 -0.0015 0.0123  168 GLU A N   
1359 C CA  . GLU A 178 ? 0.3216 0.3684 0.3403 -0.0075 -0.0020 0.0142  168 GLU A CA  
1360 C C   . GLU A 178 ? 0.3128 0.3508 0.3301 -0.0081 -0.0018 0.0135  168 GLU A C   
1361 O O   . GLU A 178 ? 0.3026 0.3386 0.3177 -0.0104 -0.0019 0.0117  168 GLU A O   
1362 C CB  . GLU A 178 ? 0.3284 0.3778 0.3427 -0.0111 -0.0028 0.0148  168 GLU A CB  
1363 C CG  . GLU A 178 ? 0.3324 0.3778 0.3451 -0.0110 -0.0033 0.0166  168 GLU A CG  
1364 C CD  . GLU A 178 ? 0.3402 0.3882 0.3486 -0.0143 -0.0042 0.0169  168 GLU A CD  
1365 O OE1 . GLU A 178 ? 0.3604 0.4160 0.3697 -0.0143 -0.0043 0.0178  168 GLU A OE1 
1366 O OE2 . GLU A 178 ? 0.3453 0.3880 0.3496 -0.0168 -0.0049 0.0163  168 GLU A OE2 
1367 N N   . SER A 179 ? 0.3006 0.3340 0.3193 -0.0060 -0.0017 0.0150  169 SER A N   
1368 C CA  . SER A 179 ? 0.2922 0.3181 0.3104 -0.0058 -0.0015 0.0143  169 SER A CA  
1369 C C   . SER A 179 ? 0.2892 0.3120 0.3075 -0.0047 -0.0016 0.0164  169 SER A C   
1370 O O   . SER A 179 ? 0.2849 0.3104 0.3056 -0.0027 -0.0016 0.0184  169 SER A O   
1371 C CB  . SER A 179 ? 0.2975 0.3221 0.3197 -0.0034 -0.0006 0.0132  169 SER A CB  
1372 O OG  . SER A 179 ? 0.3028 0.3208 0.3247 -0.0034 -0.0003 0.0125  169 SER A OG  
1373 N N   . TYR A 180 ? 0.2774 0.2951 0.2929 -0.0061 -0.0019 0.0157  170 TYR A N   
1374 C CA  . TYR A 180 ? 0.2824 0.2972 0.2981 -0.0051 -0.0019 0.0172  170 TYR A CA  
1375 C C   . TYR A 180 ? 0.2802 0.2914 0.2994 -0.0030 -0.0011 0.0174  170 TYR A C   
1376 O O   . TYR A 180 ? 0.2741 0.2826 0.2939 -0.0031 -0.0007 0.0156  170 TYR A O   
1377 C CB  . TYR A 180 ? 0.2819 0.2931 0.2933 -0.0071 -0.0026 0.0161  170 TYR A CB  
1378 C CG  . TYR A 180 ? 0.2822 0.2960 0.2901 -0.0088 -0.0036 0.0164  170 TYR A CG  
1379 C CD1 . TYR A 180 ? 0.2856 0.2989 0.2896 -0.0114 -0.0044 0.0148  170 TYR A CD1 
1380 C CD2 . TYR A 180 ? 0.2862 0.3030 0.2945 -0.0081 -0.0038 0.0183  170 TYR A CD2 
1381 C CE1 . TYR A 180 ? 0.2925 0.3076 0.2930 -0.0133 -0.0054 0.0149  170 TYR A CE1 
1382 C CE2 . TYR A 180 ? 0.2869 0.3062 0.2920 -0.0097 -0.0047 0.0183  170 TYR A CE2 
1383 C CZ  . TYR A 180 ? 0.2912 0.3093 0.2923 -0.0123 -0.0055 0.0165  170 TYR A CZ  
1384 O OH  . TYR A 180 ? 0.3027 0.3228 0.3004 -0.0142 -0.0066 0.0163  170 TYR A OH  
1385 N N   . PHE A 181 ? 0.2825 0.2937 0.3036 -0.0015 -0.0011 0.0198  171 PHE A N   
1386 C CA  . PHE A 181 ? 0.2829 0.2903 0.3070 0.0000  -0.0005 0.0204  171 PHE A CA  
1387 C C   . PHE A 181 ? 0.2790 0.2840 0.3020 -0.0005 -0.0006 0.0215  171 PHE A C   
1388 O O   . PHE A 181 ? 0.2809 0.2884 0.3024 -0.0010 -0.0010 0.0230  171 PHE A O   
1389 C CB  . PHE A 181 ? 0.2953 0.3046 0.3229 0.0024  -0.0006 0.0227  171 PHE A CB  
1390 C CG  . PHE A 181 ? 0.3045 0.3158 0.3344 0.0039  -0.0004 0.0214  171 PHE A CG  
1391 C CD1 . PHE A 181 ? 0.3158 0.3329 0.3452 0.0038  -0.0007 0.0212  171 PHE A CD1 
1392 C CD2 . PHE A 181 ? 0.3117 0.3194 0.3442 0.0053  0.0000  0.0199  171 PHE A CD2 
1393 C CE1 . PHE A 181 ? 0.3204 0.3405 0.3520 0.0052  -0.0006 0.0197  171 PHE A CE1 
1394 C CE2 . PHE A 181 ? 0.3170 0.3273 0.3517 0.0069  0.0001  0.0183  171 PHE A CE2 
1395 C CZ  . PHE A 181 ? 0.3214 0.3382 0.3557 0.0069  -0.0001 0.0182  171 PHE A CZ  
1396 N N   . PHE A 182 ? 0.2680 0.2687 0.2918 -0.0005 0.0000  0.0205  172 PHE A N   
1397 C CA  . PHE A 182 ? 0.2660 0.2648 0.2891 -0.0011 0.0000  0.0213  172 PHE A CA  
1398 C C   . PHE A 182 ? 0.2740 0.2711 0.3004 0.0000  0.0002  0.0237  172 PHE A C   
1399 O O   . PHE A 182 ? 0.2779 0.2720 0.3067 0.0009  0.0006  0.0231  172 PHE A O   
1400 C CB  . PHE A 182 ? 0.2590 0.2545 0.2806 -0.0021 0.0002  0.0185  172 PHE A CB  
1401 C CG  . PHE A 182 ? 0.2534 0.2474 0.2743 -0.0027 0.0004  0.0186  172 PHE A CG  
1402 C CD1 . PHE A 182 ? 0.2565 0.2528 0.2771 -0.0030 0.0002  0.0208  172 PHE A CD1 
1403 C CD2 . PHE A 182 ? 0.2572 0.2482 0.2776 -0.0032 0.0008  0.0162  172 PHE A CD2 
1404 C CE1 . PHE A 182 ? 0.2534 0.2493 0.2733 -0.0038 0.0004  0.0205  172 PHE A CE1 
1405 C CE2 . PHE A 182 ? 0.2517 0.2421 0.2715 -0.0038 0.0010  0.0160  172 PHE A CE2 
1406 C CZ  . PHE A 182 ? 0.2526 0.2457 0.2721 -0.0041 0.0008  0.0181  172 PHE A CZ  
1407 N N   . ASN A 183 ? 0.2851 0.2840 0.3114 -0.0002 0.0000  0.0265  173 ASN A N   
1408 C CA  . ASN A 183 ? 0.2924 0.2893 0.3212 0.0004  -0.0001 0.0294  173 ASN A CA  
1409 C C   . ASN A 183 ? 0.2962 0.2896 0.3250 -0.0009 0.0003  0.0288  173 ASN A C   
1410 O O   . ASN A 183 ? 0.3052 0.3004 0.3325 -0.0023 0.0003  0.0298  173 ASN A O   
1411 C CB  . ASN A 183 ? 0.3126 0.3134 0.3412 0.0003  -0.0007 0.0329  173 ASN A CB  
1412 C CG  . ASN A 183 ? 0.3228 0.3210 0.3534 0.0006  -0.0010 0.0363  173 ASN A CG  
1413 O OD1 . ASN A 183 ? 0.3427 0.3358 0.3752 0.0011  -0.0008 0.0360  173 ASN A OD1 
1414 N ND2 . ASN A 183 ? 0.3447 0.3463 0.3749 0.0001  -0.0016 0.0397  173 ASN A ND2 
1415 N N   . ILE A 184 ? 0.2924 0.2816 0.3228 -0.0004 0.0008  0.0269  174 ILE A N   
1416 C CA  . ILE A 184 ? 0.2997 0.2855 0.3301 -0.0018 0.0013  0.0259  174 ILE A CA  
1417 C C   . ILE A 184 ? 0.3129 0.2961 0.3450 -0.0022 0.0011  0.0290  174 ILE A C   
1418 O O   . ILE A 184 ? 0.3158 0.2981 0.3473 -0.0041 0.0014  0.0292  174 ILE A O   
1419 C CB  . ILE A 184 ? 0.2986 0.2813 0.3298 -0.0014 0.0019  0.0225  174 ILE A CB  
1420 C CG1 . ILE A 184 ? 0.3018 0.2822 0.3359 0.0005  0.0018  0.0222  174 ILE A CG1 
1421 C CG2 . ILE A 184 ? 0.2919 0.2771 0.3205 -0.0018 0.0019  0.0198  174 ILE A CG2 
1422 C CD1 . ILE A 184 ? 0.3049 0.2821 0.3401 0.0007  0.0024  0.0189  174 ILE A CD1 
1423 N N   . SER A 185 ? 0.3271 0.3091 0.3612 -0.0007 0.0004  0.0315  175 SER A N   
1424 C CA  . SER A 185 ? 0.3396 0.3176 0.3750 -0.0011 0.0000  0.0346  175 SER A CA  
1425 C C   . SER A 185 ? 0.3342 0.3150 0.3680 -0.0035 -0.0002 0.0378  175 SER A C   
1426 O O   . SER A 185 ? 0.3379 0.3154 0.3721 -0.0051 -0.0005 0.0399  175 SER A O   
1427 C CB  . SER A 185 ? 0.3607 0.3367 0.3983 0.0014  -0.0009 0.0367  175 SER A CB  
1428 O OG  . SER A 185 ? 0.3778 0.3591 0.4147 0.0021  -0.0015 0.0389  175 SER A OG  
1429 N N   . LYS A 186 ? 0.3260 0.3130 0.3578 -0.0039 -0.0002 0.0380  176 LYS A N   
1430 C CA  . LYS A 186 ? 0.3328 0.3241 0.3629 -0.0061 -0.0004 0.0404  176 LYS A CA  
1431 C C   . LYS A 186 ? 0.3310 0.3214 0.3603 -0.0086 0.0001  0.0392  176 LYS A C   
1432 O O   . LYS A 186 ? 0.3312 0.3232 0.3599 -0.0108 0.0000  0.0418  176 LYS A O   
1433 C CB  . LYS A 186 ? 0.3400 0.3380 0.3679 -0.0060 -0.0004 0.0394  176 LYS A CB  
1434 C CG  . LYS A 186 ? 0.3511 0.3546 0.3773 -0.0080 -0.0006 0.0416  176 LYS A CG  
1435 C CD  . LYS A 186 ? 0.3514 0.3612 0.3754 -0.0075 -0.0008 0.0402  176 LYS A CD  
1436 C CE  . LYS A 186 ? 0.3494 0.3600 0.3714 -0.0077 -0.0003 0.0359  176 LYS A CE  
1437 N NZ  . LYS A 186 ? 0.3418 0.3585 0.3613 -0.0077 -0.0007 0.0349  176 LYS A NZ  
1438 N N   . TYR A 187 ? 0.3222 0.3106 0.3514 -0.0082 0.0008  0.0353  177 TYR A N   
1439 C CA  . TYR A 187 ? 0.3202 0.3084 0.3485 -0.0102 0.0015  0.0335  177 TYR A CA  
1440 C C   . TYR A 187 ? 0.3282 0.3103 0.3583 -0.0114 0.0017  0.0339  177 TYR A C   
1441 O O   . TYR A 187 ? 0.3315 0.3135 0.3610 -0.0131 0.0023  0.0323  177 TYR A O   
1442 C CB  . TYR A 187 ? 0.3064 0.2959 0.3335 -0.0093 0.0020  0.0291  177 TYR A CB  
1443 C CG  . TYR A 187 ? 0.2993 0.2942 0.3240 -0.0086 0.0016  0.0284  177 TYR A CG  
1444 C CD1 . TYR A 187 ? 0.3001 0.2955 0.3247 -0.0069 0.0012  0.0281  177 TYR A CD1 
1445 C CD2 . TYR A 187 ? 0.2995 0.2995 0.3222 -0.0098 0.0016  0.0279  177 TYR A CD2 
1446 C CE1 . TYR A 187 ? 0.2915 0.2914 0.3137 -0.0065 0.0008  0.0274  177 TYR A CE1 
1447 C CE2 . TYR A 187 ? 0.2987 0.3033 0.3192 -0.0090 0.0011  0.0270  177 TYR A CE2 
1448 C CZ  . TYR A 187 ? 0.2956 0.2997 0.3157 -0.0075 0.0007  0.0268  177 TYR A CZ  
1449 O OH  . TYR A 187 ? 0.2975 0.3058 0.3152 -0.0070 0.0001  0.0257  177 TYR A OH  
1450 N N   . THR A 188 ? 0.3460 0.3231 0.3781 -0.0103 0.0011  0.0360  178 THR A N   
1451 C CA  . THR A 188 ? 0.3699 0.3401 0.4037 -0.0110 0.0011  0.0359  178 THR A CA  
1452 C C   . THR A 188 ? 0.3730 0.3429 0.4059 -0.0147 0.0011  0.0377  178 THR A C   
1453 O O   . THR A 188 ? 0.3533 0.3211 0.3864 -0.0161 0.0018  0.0354  178 THR A O   
1454 C CB  . THR A 188 ? 0.3830 0.3479 0.4189 -0.0089 0.0000  0.0383  178 THR A CB  
1455 O OG1 . THR A 188 ? 0.3892 0.3551 0.4260 -0.0056 0.0001  0.0362  178 THR A OG1 
1456 C CG2 . THR A 188 ? 0.3944 0.3513 0.4319 -0.0094 -0.0001 0.0379  178 THR A CG2 
1457 N N   . ASP A 189 ? 0.3945 0.3673 0.4264 -0.0164 0.0005  0.0417  179 ASP A N   
1458 C CA  . ASP A 189 ? 0.4101 0.3835 0.4409 -0.0204 0.0005  0.0438  179 ASP A CA  
1459 C C   . ASP A 189 ? 0.3931 0.3724 0.4223 -0.0221 0.0016  0.0407  179 ASP A C   
1460 O O   . ASP A 189 ? 0.3670 0.3452 0.3960 -0.0250 0.0020  0.0403  179 ASP A O   
1461 C CB  . ASP A 189 ? 0.4354 0.4121 0.4651 -0.0220 -0.0003 0.0488  179 ASP A CB  
1462 C CG  . ASP A 189 ? 0.4736 0.4435 0.5046 -0.0208 -0.0017 0.0525  179 ASP A CG  
1463 O OD1 . ASP A 189 ? 0.4925 0.4544 0.5251 -0.0195 -0.0020 0.0515  179 ASP A OD1 
1464 O OD2 . ASP A 189 ? 0.5029 0.4757 0.5332 -0.0211 -0.0026 0.0565  179 ASP A OD2 
1465 N N   . ARG A 190 ? 0.3720 0.3575 0.4002 -0.0204 0.0020  0.0385  180 ARG A N   
1466 C CA  . ARG A 190 ? 0.3772 0.3681 0.4038 -0.0212 0.0027  0.0352  180 ARG A CA  
1467 C C   . ARG A 190 ? 0.3600 0.3467 0.3874 -0.0207 0.0035  0.0314  180 ARG A C   
1468 O O   . ARG A 190 ? 0.3507 0.3399 0.3774 -0.0225 0.0040  0.0296  180 ARG A O   
1469 C CB  . ARG A 190 ? 0.3862 0.3832 0.4113 -0.0190 0.0027  0.0334  180 ARG A CB  
1470 C CG  . ARG A 190 ? 0.4092 0.4131 0.4330 -0.0202 0.0022  0.0363  180 ARG A CG  
1471 C CD  . ARG A 190 ? 0.4174 0.4269 0.4394 -0.0180 0.0021  0.0340  180 ARG A CD  
1472 N NE  . ARG A 190 ? 0.4249 0.4376 0.4455 -0.0177 0.0025  0.0299  180 ARG A NE  
1473 C CZ  . ARG A 190 ? 0.4252 0.4414 0.4440 -0.0157 0.0022  0.0270  180 ARG A CZ  
1474 N NH1 . ARG A 190 ? 0.4266 0.4440 0.4448 -0.0141 0.0017  0.0276  180 ARG A NH1 
1475 N NH2 . ARG A 190 ? 0.4390 0.4575 0.4565 -0.0152 0.0024  0.0234  180 ARG A NH2 
1476 N N   . LEU A 191 ? 0.3471 0.3283 0.3761 -0.0182 0.0034  0.0300  181 LEU A N   
1477 C CA  . LEU A 191 ? 0.3533 0.3307 0.3832 -0.0177 0.0041  0.0264  181 LEU A CA  
1478 C C   . LEU A 191 ? 0.3680 0.3408 0.3989 -0.0204 0.0042  0.0272  181 LEU A C   
1479 O O   . LEU A 191 ? 0.3628 0.3362 0.3935 -0.0218 0.0049  0.0246  181 LEU A O   
1480 C CB  . LEU A 191 ? 0.3498 0.3232 0.3812 -0.0147 0.0039  0.0250  181 LEU A CB  
1481 C CG  . LEU A 191 ? 0.3463 0.3164 0.3787 -0.0139 0.0046  0.0211  181 LEU A CG  
1482 C CD1 . LEU A 191 ? 0.3440 0.3183 0.3745 -0.0142 0.0052  0.0179  181 LEU A CD1 
1483 C CD2 . LEU A 191 ? 0.3402 0.3076 0.3741 -0.0110 0.0043  0.0202  181 LEU A CD2 
1484 N N   . LEU A 192 ? 0.3872 0.3553 0.4191 -0.0212 0.0034  0.0307  182 LEU A N   
1485 C CA  . LEU A 192 ? 0.4101 0.3729 0.4427 -0.0241 0.0033  0.0318  182 LEU A CA  
1486 C C   . LEU A 192 ? 0.4126 0.3806 0.4434 -0.0282 0.0037  0.0326  182 LEU A C   
1487 O O   . LEU A 192 ? 0.4130 0.3793 0.4439 -0.0305 0.0042  0.0310  182 LEU A O   
1488 C CB  . LEU A 192 ? 0.4280 0.3842 0.4617 -0.0239 0.0020  0.0357  182 LEU A CB  
1489 C CG  . LEU A 192 ? 0.4413 0.3922 0.4771 -0.0198 0.0015  0.0347  182 LEU A CG  
1490 C CD1 . LEU A 192 ? 0.4560 0.4015 0.4924 -0.0192 0.0000  0.0391  182 LEU A CD1 
1491 C CD2 . LEU A 192 ? 0.4393 0.3849 0.4767 -0.0189 0.0020  0.0308  182 LEU A CD2 
1492 N N   . GLU A 193 ? 0.4187 0.3938 0.4479 -0.0289 0.0035  0.0346  183 GLU A N   
1493 C CA  . GLU A 193 ? 0.4408 0.4231 0.4683 -0.0324 0.0040  0.0349  183 GLU A CA  
1494 C C   . GLU A 193 ? 0.4191 0.4055 0.4461 -0.0318 0.0050  0.0301  183 GLU A C   
1495 O O   . GLU A 193 ? 0.3961 0.3847 0.4225 -0.0349 0.0055  0.0293  183 GLU A O   
1496 C CB  . GLU A 193 ? 0.4743 0.4643 0.5002 -0.0324 0.0036  0.0373  183 GLU A CB  
1497 C CG  . GLU A 193 ? 0.5029 0.5020 0.5270 -0.0358 0.0040  0.0375  183 GLU A CG  
1498 C CD  . GLU A 193 ? 0.5389 0.5458 0.5617 -0.0358 0.0035  0.0400  183 GLU A CD  
1499 O OE1 . GLU A 193 ? 0.5581 0.5671 0.5807 -0.0323 0.0034  0.0386  183 GLU A OE1 
1500 O OE2 . GLU A 193 ? 0.5799 0.5910 0.6016 -0.0396 0.0032  0.0432  183 GLU A OE2 
1501 N N   . PHE A 194 ? 0.3985 0.3858 0.4255 -0.0281 0.0052  0.0271  184 PHE A N   
1502 C CA  . PHE A 194 ? 0.3876 0.3776 0.4141 -0.0271 0.0060  0.0226  184 PHE A CA  
1503 C C   . PHE A 194 ? 0.3862 0.3710 0.4141 -0.0285 0.0065  0.0207  184 PHE A C   
1504 O O   . PHE A 194 ? 0.3730 0.3614 0.4002 -0.0302 0.0071  0.0186  184 PHE A O   
1505 C CB  . PHE A 194 ? 0.3784 0.3685 0.4046 -0.0230 0.0058  0.0202  184 PHE A CB  
1506 C CG  . PHE A 194 ? 0.3733 0.3651 0.3989 -0.0218 0.0063  0.0159  184 PHE A CG  
1507 C CD1 . PHE A 194 ? 0.3752 0.3741 0.3988 -0.0221 0.0064  0.0142  184 PHE A CD1 
1508 C CD2 . PHE A 194 ? 0.3694 0.3559 0.3961 -0.0203 0.0066  0.0136  184 PHE A CD2 
1509 C CE1 . PHE A 194 ? 0.3742 0.3744 0.3970 -0.0208 0.0066  0.0104  184 PHE A CE1 
1510 C CE2 . PHE A 194 ? 0.3723 0.3605 0.3982 -0.0193 0.0069  0.0099  184 PHE A CE2 
1511 C CZ  . PHE A 194 ? 0.3723 0.3670 0.3962 -0.0195 0.0069  0.0084  184 PHE A CZ  
1512 N N   . TYR A 195 ? 0.3825 0.3592 0.4122 -0.0276 0.0063  0.0212  185 TYR A N   
1513 C CA  . TYR A 195 ? 0.3946 0.3659 0.4257 -0.0289 0.0067  0.0194  185 TYR A CA  
1514 C C   . TYR A 195 ? 0.4239 0.3957 0.4544 -0.0336 0.0068  0.0210  185 TYR A C   
1515 O O   . TYR A 195 ? 0.4208 0.3928 0.4513 -0.0354 0.0075  0.0185  185 TYR A O   
1516 C CB  . TYR A 195 ? 0.3895 0.3521 0.4226 -0.0272 0.0062  0.0201  185 TYR A CB  
1517 C CG  . TYR A 195 ? 0.3756 0.3371 0.4096 -0.0230 0.0062  0.0180  185 TYR A CG  
1518 C CD1 . TYR A 195 ? 0.3790 0.3346 0.4149 -0.0209 0.0055  0.0190  185 TYR A CD1 
1519 C CD2 . TYR A 195 ? 0.3670 0.3336 0.4000 -0.0212 0.0067  0.0151  185 TYR A CD2 
1520 C CE1 . TYR A 195 ? 0.3699 0.3254 0.4066 -0.0173 0.0055  0.0172  185 TYR A CE1 
1521 C CE2 . TYR A 195 ? 0.3575 0.3232 0.3910 -0.0179 0.0066  0.0135  185 TYR A CE2 
1522 C CZ  . TYR A 195 ? 0.3633 0.3239 0.3988 -0.0162 0.0061  0.0145  185 TYR A CZ  
1523 O OH  . TYR A 195 ? 0.3535 0.3140 0.3895 -0.0132 0.0060  0.0129  185 TYR A OH  
1524 N N   . ASP A 196 ? 0.4612 0.4334 0.4909 -0.0358 0.0061  0.0253  186 ASP A N   
1525 C CA  . ASP A 196 ? 0.5004 0.4737 0.5291 -0.0409 0.0061  0.0274  186 ASP A CA  
1526 C C   . ASP A 196 ? 0.4996 0.4829 0.5268 -0.0429 0.0069  0.0254  186 ASP A C   
1527 O O   . ASP A 196 ? 0.4983 0.4824 0.5252 -0.0464 0.0074  0.0245  186 ASP A O   
1528 C CB  . ASP A 196 ? 0.5452 0.5178 0.5732 -0.0428 0.0050  0.0327  186 ASP A CB  
1529 C CG  . ASP A 196 ? 0.5818 0.5438 0.6112 -0.0416 0.0039  0.0351  186 ASP A CG  
1530 O OD1 . ASP A 196 ? 0.6270 0.5884 0.6563 -0.0401 0.0030  0.0384  186 ASP A OD1 
1531 O OD2 . ASP A 196 ? 0.6292 0.5835 0.6598 -0.0421 0.0038  0.0336  186 ASP A OD2 
1532 N N   . GLN A 197 ? 0.4947 0.4857 0.5209 -0.0405 0.0070  0.0245  187 GLN A N   
1533 C CA  . GLN A 197 ? 0.5091 0.5102 0.5338 -0.0413 0.0076  0.0222  187 GLN A CA  
1534 C C   . GLN A 197 ? 0.4994 0.5011 0.5245 -0.0394 0.0084  0.0173  187 GLN A C   
1535 O O   . GLN A 197 ? 0.4971 0.5062 0.5211 -0.0404 0.0089  0.0151  187 GLN A O   
1536 C CB  . GLN A 197 ? 0.5280 0.5366 0.5514 -0.0389 0.0073  0.0225  187 GLN A CB  
1537 C CG  . GLN A 197 ? 0.5544 0.5656 0.5771 -0.0412 0.0067  0.0271  187 GLN A CG  
1538 C CD  . GLN A 197 ? 0.5770 0.5940 0.5986 -0.0381 0.0062  0.0272  187 GLN A CD  
1539 O OE1 . GLN A 197 ? 0.5984 0.6186 0.6195 -0.0347 0.0064  0.0237  187 GLN A OE1 
1540 N NE2 . GLN A 197 ? 0.6005 0.6186 0.6217 -0.0394 0.0056  0.0314  187 GLN A NE2 
1541 N N   . ASN A 198 ? 0.4813 0.4757 0.5077 -0.0366 0.0084  0.0156  188 ASN A N   
1542 C CA  . ASN A 198 ? 0.4806 0.4752 0.5073 -0.0345 0.0090  0.0112  188 ASN A CA  
1543 C C   . ASN A 198 ? 0.4788 0.4650 0.5075 -0.0350 0.0093  0.0101  188 ASN A C   
1544 O O   . ASN A 198 ? 0.4451 0.4264 0.4748 -0.0320 0.0092  0.0088  188 ASN A O   
1545 C CB  . ASN A 198 ? 0.4788 0.4745 0.5048 -0.0299 0.0086  0.0095  188 ASN A CB  
1546 C CG  . ASN A 198 ? 0.4825 0.4864 0.5066 -0.0291 0.0082  0.0099  188 ASN A CG  
1547 O OD1 . ASN A 198 ? 0.4868 0.4916 0.5105 -0.0293 0.0077  0.0129  188 ASN A OD1 
1548 N ND2 . ASN A 198 ? 0.4899 0.4999 0.5126 -0.0280 0.0083  0.0068  188 ASN A ND2 
1549 N N   . PRO A 199 ? 0.4892 0.4738 0.5182 -0.0391 0.0096  0.0105  189 PRO A N   
1550 C CA  . PRO A 199 ? 0.4961 0.4719 0.5269 -0.0400 0.0097  0.0098  189 PRO A CA  
1551 C C   . PRO A 199 ? 0.4932 0.4675 0.5250 -0.0376 0.0103  0.0054  189 PRO A C   
1552 O O   . PRO A 199 ? 0.5026 0.4696 0.5361 -0.0370 0.0102  0.0046  189 PRO A O   
1553 C CB  . PRO A 199 ? 0.5129 0.4893 0.5431 -0.0454 0.0099  0.0109  189 PRO A CB  
1554 C CG  . PRO A 199 ? 0.5059 0.4934 0.5344 -0.0465 0.0104  0.0099  189 PRO A CG  
1555 C CD  . PRO A 199 ? 0.4987 0.4905 0.5263 -0.0431 0.0099  0.0111  189 PRO A CD  
1556 N N   . ASP A 200 ? 0.4795 0.4608 0.5102 -0.0361 0.0108  0.0027  190 ASP A N   
1557 C CA  . ASP A 200 ? 0.4803 0.4612 0.5115 -0.0340 0.0113  -0.0011 190 ASP A CA  
1558 C C   . ASP A 200 ? 0.4383 0.4196 0.4692 -0.0295 0.0109  -0.0021 190 ASP A C   
1559 O O   . ASP A 200 ? 0.4334 0.4157 0.4640 -0.0278 0.0111  -0.0051 190 ASP A O   
1560 C CB  . ASP A 200 ? 0.5055 0.4936 0.5356 -0.0356 0.0119  -0.0037 190 ASP A CB  
1561 C CG  . ASP A 200 ? 0.5291 0.5175 0.5594 -0.0406 0.0123  -0.0029 190 ASP A CG  
1562 O OD1 . ASP A 200 ? 0.5530 0.5339 0.5848 -0.0425 0.0122  -0.0018 190 ASP A OD1 
1563 O OD2 . ASP A 200 ? 0.5512 0.5474 0.5802 -0.0426 0.0126  -0.0034 190 ASP A OD2 
1564 N N   . PHE A 201 ? 0.4078 0.3880 0.4383 -0.0280 0.0102  0.0005  191 PHE A N   
1565 C CA  . PHE A 201 ? 0.3929 0.3731 0.4229 -0.0243 0.0097  0.0000  191 PHE A CA  
1566 C C   . PHE A 201 ? 0.4099 0.3845 0.4416 -0.0226 0.0099  -0.0016 191 PHE A C   
1567 O O   . PHE A 201 ? 0.3893 0.3650 0.4204 -0.0206 0.0099  -0.0040 191 PHE A O   
1568 C CB  . PHE A 201 ? 0.3756 0.3557 0.4051 -0.0235 0.0090  0.0035  191 PHE A CB  
1569 C CG  . PHE A 201 ? 0.3575 0.3371 0.3865 -0.0201 0.0085  0.0032  191 PHE A CG  
1570 C CD1 . PHE A 201 ? 0.3458 0.3296 0.3727 -0.0183 0.0082  0.0012  191 PHE A CD1 
1571 C CD2 . PHE A 201 ? 0.3479 0.3228 0.3782 -0.0188 0.0081  0.0049  191 PHE A CD2 
1572 C CE1 . PHE A 201 ? 0.3417 0.3246 0.3676 -0.0157 0.0076  0.0010  191 PHE A CE1 
1573 C CE2 . PHE A 201 ? 0.3444 0.3195 0.3741 -0.0161 0.0077  0.0046  191 PHE A CE2 
1574 C CZ  . PHE A 201 ? 0.3405 0.3194 0.3679 -0.0148 0.0074  0.0027  191 PHE A CZ  
1575 N N   . ILE A 202 ? 0.4293 0.3979 0.4631 -0.0236 0.0099  -0.0005 192 ILE A N   
1576 C CA  . ILE A 202 ? 0.4600 0.4235 0.4958 -0.0222 0.0101  -0.0025 192 ILE A CA  
1577 C C   . ILE A 202 ? 0.4858 0.4462 0.5229 -0.0249 0.0106  -0.0040 192 ILE A C   
1578 O O   . ILE A 202 ? 0.4892 0.4473 0.5265 -0.0276 0.0104  -0.0018 192 ILE A O   
1579 C CB  . ILE A 202 ? 0.4823 0.4407 0.5197 -0.0204 0.0094  -0.0003 192 ILE A CB  
1580 C CG1 . ILE A 202 ? 0.4958 0.4570 0.5318 -0.0183 0.0088  0.0015  192 ILE A CG1 
1581 C CG2 . ILE A 202 ? 0.4926 0.4472 0.5321 -0.0186 0.0096  -0.0030 192 ILE A CG2 
1582 C CD1 . ILE A 202 ? 0.5017 0.4592 0.5389 -0.0174 0.0081  0.0048  192 ILE A CD1 
1583 N N   . GLN A 203 ? 0.4947 0.4550 0.5326 -0.0244 0.0112  -0.0076 193 GLN A N   
1584 C CA  . GLN A 203 ? 0.5155 0.4727 0.5547 -0.0267 0.0117  -0.0096 193 GLN A CA  
1585 C C   . GLN A 203 ? 0.5091 0.4627 0.5504 -0.0246 0.0119  -0.0126 193 GLN A C   
1586 O O   . GLN A 203 ? 0.4907 0.4464 0.5319 -0.0219 0.0118  -0.0136 193 GLN A O   
1587 C CB  . GLN A 203 ? 0.5286 0.4915 0.5665 -0.0289 0.0124  -0.0117 193 GLN A CB  
1588 C CG  . GLN A 203 ? 0.5469 0.5141 0.5830 -0.0313 0.0123  -0.0092 193 GLN A CG  
1589 C CD  . GLN A 203 ? 0.5653 0.5393 0.6002 -0.0330 0.0130  -0.0115 193 GLN A CD  
1590 O OE1 . GLN A 203 ? 0.5837 0.5616 0.6178 -0.0309 0.0131  -0.0138 193 GLN A OE1 
1591 N NE2 . GLN A 203 ? 0.5783 0.5538 0.6128 -0.0368 0.0132  -0.0107 193 GLN A NE2 
1592 N N   . PRO A 204 ? 0.5251 0.4734 0.5682 -0.0259 0.0119  -0.0140 194 PRO A N   
1593 C CA  . PRO A 204 ? 0.5318 0.4760 0.5750 -0.0295 0.0117  -0.0124 194 PRO A CA  
1594 C C   . PRO A 204 ? 0.5405 0.4792 0.5839 -0.0291 0.0106  -0.0082 194 PRO A C   
1595 O O   . PRO A 204 ? 0.5127 0.4513 0.5565 -0.0259 0.0101  -0.0069 194 PRO A O   
1596 C CB  . PRO A 204 ? 0.5386 0.4783 0.5837 -0.0301 0.0120  -0.0160 194 PRO A CB  
1597 C CG  . PRO A 204 ? 0.5408 0.4799 0.5875 -0.0261 0.0120  -0.0182 194 PRO A CG  
1598 C CD  . PRO A 204 ? 0.5355 0.4816 0.5807 -0.0242 0.0122  -0.0176 194 PRO A CD  
1599 N N   . PRO A 205 ? 0.5545 0.4890 0.5975 -0.0326 0.0101  -0.0060 195 PRO A N   
1600 C CA  . PRO A 205 ? 0.5591 0.4879 0.6021 -0.0325 0.0088  -0.0018 195 PRO A CA  
1601 C C   . PRO A 205 ? 0.5523 0.4749 0.5974 -0.0284 0.0079  -0.0020 195 PRO A C   
1602 O O   . PRO A 205 ? 0.5505 0.4720 0.5954 -0.0266 0.0070  0.0011  195 PRO A O   
1603 C CB  . PRO A 205 ? 0.5756 0.4993 0.6181 -0.0372 0.0084  -0.0007 195 PRO A CB  
1604 C CG  . PRO A 205 ? 0.5702 0.5012 0.6113 -0.0403 0.0096  -0.0026 195 PRO A CG  
1605 C CD  . PRO A 205 ? 0.5660 0.5017 0.6081 -0.0371 0.0106  -0.0069 195 PRO A CD  
1606 N N   . SER A 206 ? 0.5563 0.4756 0.6032 -0.0269 0.0081  -0.0060 196 SER A N   
1607 C CA  . SER A 206 ? 0.5668 0.4818 0.6159 -0.0226 0.0073  -0.0071 196 SER A CA  
1608 C C   . SER A 206 ? 0.5583 0.4792 0.6074 -0.0190 0.0076  -0.0067 196 SER A C   
1609 O O   . SER A 206 ? 0.5595 0.4778 0.6095 -0.0160 0.0066  -0.0049 196 SER A O   
1610 C CB  . SER A 206 ? 0.5745 0.4872 0.6256 -0.0216 0.0078  -0.0123 196 SER A CB  
1611 O OG  . SER A 206 ? 0.5748 0.4950 0.6254 -0.0219 0.0092  -0.0154 196 SER A OG  
1612 N N   . ARG A 207 ? 0.5383 0.4670 0.5862 -0.0193 0.0087  -0.0081 197 ARG A N   
1613 C CA  . ARG A 207 ? 0.5378 0.4721 0.5851 -0.0165 0.0088  -0.0076 197 ARG A CA  
1614 C C   . ARG A 207 ? 0.5336 0.4689 0.5795 -0.0166 0.0081  -0.0030 197 ARG A C   
1615 O O   . ARG A 207 ? 0.5267 0.4628 0.5730 -0.0138 0.0076  -0.0018 197 ARG A O   
1616 C CB  . ARG A 207 ? 0.5288 0.4702 0.5747 -0.0171 0.0099  -0.0101 197 ARG A CB  
1617 C CG  . ARG A 207 ? 0.5276 0.4736 0.5731 -0.0142 0.0100  -0.0108 197 ARG A CG  
1618 C CD  . ARG A 207 ? 0.5230 0.4753 0.5664 -0.0150 0.0107  -0.0124 197 ARG A CD  
1619 N NE  . ARG A 207 ? 0.5298 0.4830 0.5737 -0.0163 0.0115  -0.0160 197 ARG A NE  
1620 C CZ  . ARG A 207 ? 0.5315 0.4852 0.5766 -0.0151 0.0118  -0.0193 197 ARG A CZ  
1621 N NH1 . ARG A 207 ? 0.5287 0.4825 0.5749 -0.0124 0.0115  -0.0197 197 ARG A NH1 
1622 N NH2 . ARG A 207 ? 0.5502 0.5052 0.5957 -0.0166 0.0126  -0.0224 197 ARG A NH2 
1623 N N   . LYS A 208 ? 0.5534 0.4894 0.5977 -0.0198 0.0081  -0.0005 198 LYS A N   
1624 C CA  . LYS A 208 ? 0.5809 0.5180 0.6238 -0.0203 0.0074  0.0039  198 LYS A CA  
1625 C C   . LYS A 208 ? 0.5978 0.5281 0.6420 -0.0187 0.0061  0.0065  198 LYS A C   
1626 O O   . LYS A 208 ? 0.5846 0.5163 0.6288 -0.0165 0.0055  0.0088  198 LYS A O   
1627 C CB  . LYS A 208 ? 0.6025 0.5418 0.6436 -0.0245 0.0076  0.0059  198 LYS A CB  
1628 C CG  . LYS A 208 ? 0.6208 0.5631 0.6603 -0.0250 0.0070  0.0102  198 LYS A CG  
1629 C CD  . LYS A 208 ? 0.6489 0.5903 0.6871 -0.0293 0.0066  0.0133  198 LYS A CD  
1630 C CE  . LYS A 208 ? 0.6666 0.6156 0.7031 -0.0321 0.0076  0.0121  198 LYS A CE  
1631 N NZ  . LYS A 208 ? 0.6886 0.6381 0.7237 -0.0367 0.0073  0.0153  198 LYS A NZ  
1632 N N   . ASN A 209 ? 0.6145 0.5374 0.6599 -0.0198 0.0055  0.0062  199 ASN A N   
1633 C CA  . ASN A 209 ? 0.6466 0.5619 0.6933 -0.0179 0.0040  0.0083  199 ASN A CA  
1634 C C   . ASN A 209 ? 0.6514 0.5673 0.7000 -0.0129 0.0037  0.0066  199 ASN A C   
1635 O O   . ASN A 209 ? 0.6529 0.5669 0.7020 -0.0106 0.0026  0.0093  199 ASN A O   
1636 C CB  . ASN A 209 ? 0.6641 0.5707 0.7117 -0.0196 0.0033  0.0072  199 ASN A CB  
1637 C CG  . ASN A 209 ? 0.6843 0.5821 0.7330 -0.0173 0.0014  0.0094  199 ASN A CG  
1638 O OD1 . ASN A 209 ? 0.7134 0.6059 0.7642 -0.0145 0.0008  0.0064  199 ASN A OD1 
1639 N ND2 . ASN A 209 ? 0.6721 0.5688 0.7196 -0.0181 0.0003  0.0145  199 ASN A ND2 
1640 N N   . GLU A 210 ? 0.6650 0.5839 0.7146 -0.0115 0.0048  0.0021  200 GLU A N   
1641 C CA  . GLU A 210 ? 0.6827 0.6043 0.7340 -0.0073 0.0048  -0.0001 200 GLU A CA  
1642 C C   . GLU A 210 ? 0.6621 0.5894 0.7122 -0.0059 0.0047  0.0025  200 GLU A C   
1643 O O   . GLU A 210 ? 0.6752 0.6019 0.7265 -0.0028 0.0039  0.0035  200 GLU A O   
1644 C CB  . GLU A 210 ? 0.7035 0.6293 0.7552 -0.0073 0.0061  -0.0049 200 GLU A CB  
1645 C CG  . GLU A 210 ? 0.7286 0.6554 0.7825 -0.0035 0.0061  -0.0083 200 GLU A CG  
1646 C CD  . GLU A 210 ? 0.7440 0.6767 0.7977 -0.0040 0.0074  -0.0122 200 GLU A CD  
1647 O OE1 . GLU A 210 ? 0.7562 0.6877 0.8098 -0.0063 0.0081  -0.0146 200 GLU A OE1 
1648 O OE2 . GLU A 210 ? 0.7512 0.6897 0.8045 -0.0024 0.0077  -0.0128 200 GLU A OE2 
1649 N N   . MET A 211 ? 0.6415 0.5744 0.6893 -0.0081 0.0055  0.0034  201 MET A N   
1650 C CA  . MET A 211 ? 0.6296 0.5679 0.6759 -0.0073 0.0054  0.0059  201 MET A CA  
1651 C C   . MET A 211 ? 0.6341 0.5696 0.6805 -0.0068 0.0042  0.0103  201 MET A C   
1652 O O   . MET A 211 ? 0.6388 0.5760 0.6856 -0.0042 0.0036  0.0116  201 MET A O   
1653 C CB  . MET A 211 ? 0.6177 0.5614 0.6614 -0.0099 0.0062  0.0062  201 MET A CB  
1654 C CG  . MET A 211 ? 0.6037 0.5514 0.6467 -0.0101 0.0072  0.0024  201 MET A CG  
1655 S SD  . MET A 211 ? 0.5919 0.5428 0.6354 -0.0070 0.0073  -0.0001 201 MET A SD  
1656 C CE  . MET A 211 ? 0.6006 0.5479 0.6470 -0.0060 0.0077  -0.0041 201 MET A CE  
1657 N N   . ILE A 212 ? 0.6404 0.5716 0.6862 -0.0095 0.0037  0.0127  202 ILE A N   
1658 C CA  . ILE A 212 ? 0.6506 0.5793 0.6959 -0.0098 0.0024  0.0175  202 ILE A CA  
1659 C C   . ILE A 212 ? 0.6654 0.5882 0.7129 -0.0063 0.0011  0.0181  202 ILE A C   
1660 O O   . ILE A 212 ? 0.6508 0.5751 0.6985 -0.0041 0.0003  0.0206  202 ILE A O   
1661 C CB  . ILE A 212 ? 0.6600 0.5858 0.7039 -0.0142 0.0022  0.0200  202 ILE A CB  
1662 C CG1 . ILE A 212 ? 0.6487 0.5820 0.6905 -0.0171 0.0034  0.0196  202 ILE A CG1 
1663 C CG2 . ILE A 212 ? 0.6597 0.5826 0.7030 -0.0148 0.0008  0.0253  202 ILE A CG2 
1664 C CD1 . ILE A 212 ? 0.6536 0.5856 0.6942 -0.0217 0.0036  0.0204  202 ILE A CD1 
1665 N N   . ASN A 213 ? 0.6788 0.5953 0.7281 -0.0056 0.0008  0.0155  203 ASN A N   
1666 C CA  . ASN A 213 ? 0.6974 0.6073 0.7487 -0.0020 -0.0006 0.0157  203 ASN A CA  
1667 C C   . ASN A 213 ? 0.6784 0.5924 0.7315 0.0025  -0.0006 0.0134  203 ASN A C   
1668 O O   . ASN A 213 ? 0.6741 0.5867 0.7280 0.0056  -0.0019 0.0155  203 ASN A O   
1669 C CB  . ASN A 213 ? 0.7191 0.6209 0.7716 -0.0026 -0.0011 0.0130  203 ASN A CB  
1670 C CG  . ASN A 213 ? 0.7333 0.6285 0.7841 -0.0069 -0.0019 0.0163  203 ASN A CG  
1671 O OD1 . ASN A 213 ? 0.7658 0.6540 0.8172 -0.0081 -0.0023 0.0144  203 ASN A OD1 
1672 N ND2 . ASN A 213 ? 0.7366 0.6344 0.7854 -0.0095 -0.0021 0.0210  203 ASN A ND2 
1673 N N   . ASN A 214 ? 0.6614 0.5807 0.7149 0.0030  0.0007  0.0092  204 ASN A N   
1674 C CA  . ASN A 214 ? 0.6574 0.5814 0.7126 0.0069  0.0009  0.0067  204 ASN A CA  
1675 C C   . ASN A 214 ? 0.6323 0.5634 0.6862 0.0076  0.0010  0.0091  204 ASN A C   
1676 O O   . ASN A 214 ? 0.6231 0.5566 0.6783 0.0110  0.0004  0.0088  204 ASN A O   
1677 C CB  . ASN A 214 ? 0.6710 0.5987 0.7267 0.0067  0.0023  0.0016  204 ASN A CB  
1678 C CG  . ASN A 214 ? 0.6842 0.6057 0.7417 0.0068  0.0021  -0.0016 204 ASN A CG  
1679 O OD1 . ASN A 214 ? 0.7065 0.6201 0.7646 0.0070  0.0009  -0.0001 204 ASN A OD1 
1680 N ND2 . ASN A 214 ? 0.6754 0.6003 0.7334 0.0065  0.0033  -0.0060 204 ASN A ND2 
1681 N N   . PHE A 215 ? 0.6088 0.5435 0.6602 0.0045  0.0017  0.0111  205 PHE A N   
1682 C CA  . PHE A 215 ? 0.5939 0.5358 0.6437 0.0047  0.0020  0.0125  205 PHE A CA  
1683 C C   . PHE A 215 ? 0.5821 0.5247 0.6303 0.0034  0.0013  0.0173  205 PHE A C   
1684 O O   . PHE A 215 ? 0.6068 0.5527 0.6548 0.0051  0.0008  0.0192  205 PHE A O   
1685 C CB  . PHE A 215 ? 0.5973 0.5444 0.6455 0.0028  0.0033  0.0098  205 PHE A CB  
1686 C CG  . PHE A 215 ? 0.5978 0.5452 0.6474 0.0037  0.0040  0.0052  205 PHE A CG  
1687 C CD1 . PHE A 215 ? 0.6053 0.5520 0.6542 0.0014  0.0049  0.0028  205 PHE A CD1 
1688 C CD2 . PHE A 215 ? 0.5985 0.5476 0.6500 0.0069  0.0038  0.0033  205 PHE A CD2 
1689 C CE1 . PHE A 215 ? 0.6110 0.5585 0.6611 0.0022  0.0056  -0.0014 205 PHE A CE1 
1690 C CE2 . PHE A 215 ? 0.6014 0.5516 0.6541 0.0077  0.0044  -0.0010 205 PHE A CE2 
1691 C CZ  . PHE A 215 ? 0.6126 0.5620 0.6647 0.0053  0.0053  -0.0033 205 PHE A CZ  
1692 N N   . ILE A 216 ? 0.5545 0.4948 0.6012 0.0001  0.0014  0.0191  206 ILE A N   
1693 C CA  . ILE A 216 ? 0.5439 0.4861 0.5888 -0.0016 0.0010  0.0235  206 ILE A CA  
1694 C C   . ILE A 216 ? 0.5635 0.5005 0.6094 -0.0005 -0.0005 0.0273  206 ILE A C   
1695 O O   . ILE A 216 ? 0.5439 0.4838 0.5893 0.0004  -0.0012 0.0304  206 ILE A O   
1696 C CB  . ILE A 216 ? 0.5301 0.4732 0.5730 -0.0057 0.0017  0.0239  206 ILE A CB  
1697 C CG1 . ILE A 216 ? 0.5098 0.4582 0.5516 -0.0063 0.0030  0.0203  206 ILE A CG1 
1698 C CG2 . ILE A 216 ? 0.5267 0.4730 0.5678 -0.0075 0.0012  0.0283  206 ILE A CG2 
1699 C CD1 . ILE A 216 ? 0.5064 0.4560 0.5466 -0.0098 0.0037  0.0197  206 ILE A CD1 
1700 N N   . LYS A 217 ? 0.5771 0.5064 0.6242 -0.0007 -0.0012 0.0271  207 LYS A N   
1701 C CA  . LYS A 217 ? 0.5897 0.5121 0.6373 0.0000  -0.0030 0.0308  207 LYS A CA  
1702 C C   . LYS A 217 ? 0.5795 0.5026 0.6286 0.0044  -0.0042 0.0321  207 LYS A C   
1703 O O   . LYS A 217 ? 0.5897 0.5133 0.6380 0.0044  -0.0053 0.0365  207 LYS A O   
1704 C CB  . LYS A 217 ? 0.5992 0.5124 0.6479 -0.0004 -0.0036 0.0292  207 LYS A CB  
1705 N N   . PRO A 218 ? 0.5803 0.5043 0.6316 0.0082  -0.0040 0.0282  208 PRO A N   
1706 C CA  . PRO A 218 ? 0.5724 0.4982 0.6250 0.0125  -0.0051 0.0292  208 PRO A CA  
1707 C C   . PRO A 218 ? 0.5443 0.4788 0.5956 0.0124  -0.0047 0.0313  208 PRO A C   
1708 O O   . PRO A 218 ? 0.5482 0.4844 0.6003 0.0154  -0.0058 0.0332  208 PRO A O   
1709 C CB  . PRO A 218 ? 0.5779 0.5045 0.6330 0.0159  -0.0047 0.0240  208 PRO A CB  
1710 C CG  . PRO A 218 ? 0.5795 0.5073 0.6340 0.0130  -0.0030 0.0204  208 PRO A CG  
1711 C CD  . PRO A 218 ? 0.5823 0.5057 0.6348 0.0087  -0.0030 0.0229  208 PRO A CD  
1712 N N   . GLY A 219 ? 0.4940 0.4340 0.5433 0.0092  -0.0033 0.0308  209 GLY A N   
1713 C CA  . GLY A 219 ? 0.4719 0.4196 0.5195 0.0086  -0.0029 0.0327  209 GLY A CA  
1714 C C   . GLY A 219 ? 0.4356 0.3895 0.4827 0.0087  -0.0016 0.0288  209 GLY A C   
1715 O O   . GLY A 219 ? 0.4288 0.3834 0.4776 0.0112  -0.0014 0.0257  209 GLY A O   
1716 N N   . LEU A 220 ? 0.4085 0.3670 0.4532 0.0060  -0.0007 0.0289  210 LEU A N   
1717 C CA  . LEU A 220 ? 0.3857 0.3495 0.4292 0.0057  0.0003  0.0256  210 LEU A CA  
1718 C C   . LEU A 220 ? 0.3710 0.3405 0.4143 0.0075  0.0000  0.0264  210 LEU A C   
1719 O O   . LEU A 220 ? 0.3758 0.3484 0.4177 0.0068  -0.0004 0.0293  210 LEU A O   
1720 C CB  . LEU A 220 ? 0.3786 0.3448 0.4195 0.0025  0.0010  0.0254  210 LEU A CB  
1721 C CG  . LEU A 220 ? 0.3799 0.3420 0.4206 0.0003  0.0016  0.0242  210 LEU A CG  
1722 C CD1 . LEU A 220 ? 0.3736 0.3391 0.4117 -0.0024 0.0021  0.0247  210 LEU A CD1 
1723 C CD2 . LEU A 220 ? 0.3764 0.3370 0.4183 0.0010  0.0023  0.0199  210 LEU A CD2 
1724 N N   . ALA A 221 ? 0.3624 0.3338 0.4071 0.0097  0.0000  0.0237  211 ALA A N   
1725 C CA  . ALA A 221 ? 0.3548 0.3325 0.3992 0.0111  -0.0002 0.0240  211 ALA A CA  
1726 C C   . ALA A 221 ? 0.3381 0.3205 0.3793 0.0085  0.0003  0.0235  211 ALA A C   
1727 O O   . ALA A 221 ? 0.3301 0.3114 0.3698 0.0065  0.0010  0.0216  211 ALA A O   
1728 C CB  . ALA A 221 ? 0.3599 0.3393 0.4062 0.0135  -0.0001 0.0208  211 ALA A CB  
1729 N N   . ASP A 222 ? 0.3241 0.3116 0.3642 0.0088  0.0000  0.0251  212 ASP A N   
1730 C CA  . ASP A 222 ? 0.3179 0.3096 0.3549 0.0067  0.0002  0.0243  212 ASP A CA  
1731 C C   . ASP A 222 ? 0.3026 0.2949 0.3388 0.0060  0.0008  0.0205  212 ASP A C   
1732 O O   . ASP A 222 ? 0.3008 0.2937 0.3389 0.0076  0.0009  0.0187  212 ASP A O   
1733 C CB  . ASP A 222 ? 0.3263 0.3237 0.3625 0.0072  -0.0003 0.0260  212 ASP A CB  
1734 C CG  . ASP A 222 ? 0.3446 0.3426 0.3807 0.0073  -0.0009 0.0300  212 ASP A CG  
1735 O OD1 . ASP A 222 ? 0.3460 0.3404 0.3821 0.0063  -0.0009 0.0315  212 ASP A OD1 
1736 O OD2 . ASP A 222 ? 0.3653 0.3681 0.4014 0.0081  -0.0015 0.0315  212 ASP A OD2 
1737 N N   . LEU A 223 ? 0.2836 0.2760 0.3168 0.0037  0.0011  0.0192  213 LEU A N   
1738 C CA  . LEU A 223 ? 0.2735 0.2657 0.3055 0.0026  0.0016  0.0159  213 LEU A CA  
1739 C C   . LEU A 223 ? 0.2609 0.2575 0.2902 0.0016  0.0012  0.0152  213 LEU A C   
1740 O O   . LEU A 223 ? 0.2488 0.2469 0.2754 0.0003  0.0007  0.0162  213 LEU A O   
1741 C CB  . LEU A 223 ? 0.2745 0.2634 0.3046 0.0009  0.0019  0.0150  213 LEU A CB  
1742 C CG  . LEU A 223 ? 0.2796 0.2675 0.3085 0.0000  0.0023  0.0118  213 LEU A CG  
1743 C CD1 . LEU A 223 ? 0.2860 0.2721 0.3180 0.0010  0.0029  0.0100  213 LEU A CD1 
1744 C CD2 . LEU A 223 ? 0.2812 0.2669 0.3080 -0.0015 0.0024  0.0113  213 LEU A CD2 
1745 N N   . ALA A 224 ? 0.2591 0.2582 0.2892 0.0020  0.0013  0.0134  214 ALA A N   
1746 C CA  . ALA A 224 ? 0.2619 0.2655 0.2895 0.0005  0.0009  0.0127  214 ALA A CA  
1747 C C   . ALA A 224 ? 0.2514 0.2528 0.2753 -0.0020 0.0008  0.0109  214 ALA A C   
1748 O O   . ALA A 224 ? 0.2538 0.2539 0.2779 -0.0024 0.0012  0.0087  214 ALA A O   
1749 C CB  . ALA A 224 ? 0.2627 0.2703 0.2923 0.0016  0.0011  0.0113  214 ALA A CB  
1750 N N   . VAL A 225 ? 0.2467 0.2476 0.2672 -0.0034 0.0002  0.0118  215 VAL A N   
1751 C CA  . VAL A 225 ? 0.2454 0.2431 0.2623 -0.0052 -0.0001 0.0104  215 VAL A CA  
1752 C C   . VAL A 225 ? 0.2478 0.2470 0.2607 -0.0075 -0.0010 0.0095  215 VAL A C   
1753 O O   . VAL A 225 ? 0.2429 0.2390 0.2522 -0.0090 -0.0017 0.0083  215 VAL A O   
1754 C CB  . VAL A 225 ? 0.2459 0.2414 0.2615 -0.0051 -0.0004 0.0114  215 VAL A CB  
1755 C CG1 . VAL A 225 ? 0.2488 0.2418 0.2675 -0.0037 0.0003  0.0118  215 VAL A CG1 
1756 C CG2 . VAL A 225 ? 0.2470 0.2456 0.2620 -0.0049 -0.0009 0.0135  215 VAL A CG2 
1757 N N   . SER A 226 ? 0.2478 0.2516 0.2610 -0.0080 -0.0011 0.0100  216 SER A N   
1758 C CA  . SER A 226 ? 0.2515 0.2570 0.2609 -0.0107 -0.0020 0.0091  216 SER A CA  
1759 C C   . SER A 226 ? 0.2617 0.2726 0.2732 -0.0108 -0.0015 0.0086  216 SER A C   
1760 O O   . SER A 226 ? 0.2557 0.2692 0.2715 -0.0083 -0.0007 0.0089  216 SER A O   
1761 C CB  . SER A 226 ? 0.2551 0.2618 0.2614 -0.0120 -0.0030 0.0103  216 SER A CB  
1762 O OG  . SER A 226 ? 0.2578 0.2698 0.2664 -0.0109 -0.0027 0.0118  216 SER A OG  
1763 N N   . ARG A 227 ? 0.2679 0.2805 0.2761 -0.0138 -0.0021 0.0076  217 ARG A N   
1764 C CA  . ARG A 227 ? 0.2730 0.2922 0.2824 -0.0146 -0.0018 0.0070  217 ARG A CA  
1765 C C   . ARG A 227 ? 0.2895 0.3111 0.2944 -0.0182 -0.0029 0.0074  217 ARG A C   
1766 O O   . ARG A 227 ? 0.2830 0.2999 0.2835 -0.0202 -0.0040 0.0076  217 ARG A O   
1767 C CB  . ARG A 227 ? 0.2783 0.2974 0.2885 -0.0151 -0.0013 0.0049  217 ARG A CB  
1768 C CG  . ARG A 227 ? 0.2825 0.2994 0.2972 -0.0118 -0.0002 0.0041  217 ARG A CG  
1769 C CD  . ARG A 227 ? 0.2898 0.3114 0.3094 -0.0085 0.0004  0.0045  217 ARG A CD  
1770 N NE  . ARG A 227 ? 0.2954 0.3145 0.3191 -0.0056 0.0013  0.0035  217 ARG A NE  
1771 C CZ  . ARG A 227 ? 0.2957 0.3092 0.3209 -0.0038 0.0015  0.0044  217 ARG A CZ  
1772 N NH1 . ARG A 227 ? 0.2923 0.3025 0.3151 -0.0045 0.0010  0.0063  217 ARG A NH1 
1773 N NH2 . ARG A 227 ? 0.2962 0.3075 0.3249 -0.0015 0.0022  0.0033  217 ARG A NH2 
1774 N N   . THR A 228 ? 0.2964 0.3257 0.3025 -0.0187 -0.0028 0.0075  218 THR A N   
1775 C CA  . THR A 228 ? 0.3075 0.3405 0.3095 -0.0226 -0.0037 0.0079  218 THR A CA  
1776 C C   . THR A 228 ? 0.3164 0.3549 0.3175 -0.0254 -0.0037 0.0066  218 THR A C   
1777 O O   . THR A 228 ? 0.3482 0.3895 0.3454 -0.0294 -0.0046 0.0068  218 THR A O   
1778 C CB  . THR A 228 ? 0.3052 0.3439 0.3088 -0.0214 -0.0037 0.0094  218 THR A CB  
1779 O OG1 . THR A 228 ? 0.3060 0.3496 0.3153 -0.0175 -0.0026 0.0093  218 THR A OG1 
1780 C CG2 . THR A 228 ? 0.3058 0.3395 0.3083 -0.0203 -0.0042 0.0108  218 THR A CG2 
1781 N N   . SER A 229 ? 0.3186 0.3588 0.3231 -0.0237 -0.0027 0.0051  219 SER A N   
1782 C CA  . SER A 229 ? 0.3220 0.3695 0.3266 -0.0259 -0.0024 0.0036  219 SER A CA  
1783 C C   . SER A 229 ? 0.3230 0.3671 0.3231 -0.0300 -0.0031 0.0028  219 SER A C   
1784 O O   . SER A 229 ? 0.3281 0.3786 0.3276 -0.0325 -0.0030 0.0018  219 SER A O   
1785 C CB  . SER A 229 ? 0.3224 0.3746 0.3330 -0.0217 -0.0011 0.0021  219 SER A CB  
1786 O OG  . SER A 229 ? 0.3413 0.3868 0.3537 -0.0194 -0.0005 0.0012  219 SER A OG  
1787 N N   . PHE A 230 ? 0.3130 0.3477 0.3100 -0.0306 -0.0039 0.0033  220 PHE A N   
1788 C CA  . PHE A 230 ? 0.3123 0.3428 0.3046 -0.0344 -0.0049 0.0029  220 PHE A CA  
1789 C C   . PHE A 230 ? 0.3068 0.3279 0.2942 -0.0356 -0.0064 0.0041  220 PHE A C   
1790 O O   . PHE A 230 ? 0.3097 0.3276 0.2980 -0.0331 -0.0064 0.0048  220 PHE A O   
1791 C CB  . PHE A 230 ? 0.3151 0.3448 0.3101 -0.0327 -0.0039 0.0013  220 PHE A CB  
1792 C CG  . PHE A 230 ? 0.3079 0.3312 0.3058 -0.0285 -0.0032 0.0011  220 PHE A CG  
1793 C CD1 . PHE A 230 ? 0.3116 0.3374 0.3153 -0.0241 -0.0019 0.0007  220 PHE A CD1 
1794 C CD2 . PHE A 230 ? 0.3044 0.3194 0.2993 -0.0289 -0.0041 0.0012  220 PHE A CD2 
1795 C CE1 . PHE A 230 ? 0.3087 0.3287 0.3148 -0.0208 -0.0013 0.0007  220 PHE A CE1 
1796 C CE2 . PHE A 230 ? 0.3103 0.3202 0.3077 -0.0254 -0.0034 0.0010  220 PHE A CE2 
1797 C CZ  . PHE A 230 ? 0.3061 0.3186 0.3092 -0.0216 -0.0020 0.0008  220 PHE A CZ  
1798 N N   . ASN A 231 ? 0.3023 0.3191 0.2843 -0.0395 -0.0079 0.0041  221 ASN A N   
1799 C CA  . ASN A 231 ? 0.3116 0.3195 0.2880 -0.0411 -0.0098 0.0050  221 ASN A CA  
1800 C C   . ASN A 231 ? 0.3026 0.3020 0.2772 -0.0399 -0.0105 0.0045  221 ASN A C   
1801 O O   . ASN A 231 ? 0.3013 0.2933 0.2725 -0.0396 -0.0120 0.0049  221 ASN A O   
1802 C CB  . ASN A 231 ? 0.3291 0.3372 0.2994 -0.0468 -0.0117 0.0059  221 ASN A CB  
1803 C CG  . ASN A 231 ? 0.3470 0.3626 0.3179 -0.0482 -0.0114 0.0065  221 ASN A CG  
1804 O OD1 . ASN A 231 ? 0.3790 0.4015 0.3489 -0.0519 -0.0114 0.0066  221 ASN A OD1 
1805 N ND2 . ASN A 231 ? 0.3498 0.3645 0.3222 -0.0456 -0.0112 0.0070  221 ASN A ND2 
1806 N N   . TRP A 232 ? 0.2806 0.2813 0.2575 -0.0393 -0.0096 0.0035  222 TRP A N   
1807 C CA  . TRP A 232 ? 0.2742 0.2677 0.2492 -0.0386 -0.0103 0.0030  222 TRP A CA  
1808 C C   . TRP A 232 ? 0.2716 0.2621 0.2505 -0.0336 -0.0092 0.0023  222 TRP A C   
1809 O O   . TRP A 232 ? 0.2699 0.2629 0.2536 -0.0311 -0.0075 0.0013  222 TRP A O   
1810 C CB  . TRP A 232 ? 0.2649 0.2611 0.2397 -0.0405 -0.0099 0.0022  222 TRP A CB  
1811 C CG  . TRP A 232 ? 0.2644 0.2534 0.2368 -0.0400 -0.0109 0.0018  222 TRP A CG  
1812 C CD1 . TRP A 232 ? 0.2608 0.2498 0.2367 -0.0373 -0.0096 0.0005  222 TRP A CD1 
1813 C CD2 . TRP A 232 ? 0.2607 0.2413 0.2266 -0.0420 -0.0134 0.0026  222 TRP A CD2 
1814 N NE1 . TRP A 232 ? 0.2606 0.2425 0.2328 -0.0374 -0.0111 0.0005  222 TRP A NE1 
1815 C CE2 . TRP A 232 ? 0.2634 0.2398 0.2294 -0.0401 -0.0135 0.0018  222 TRP A CE2 
1816 C CE3 . TRP A 232 ? 0.2730 0.2490 0.2329 -0.0451 -0.0158 0.0039  222 TRP A CE3 
1817 C CZ2 . TRP A 232 ? 0.2735 0.2415 0.2339 -0.0408 -0.0159 0.0023  222 TRP A CZ2 
1818 C CZ3 . TRP A 232 ? 0.2786 0.2454 0.2328 -0.0459 -0.0183 0.0043  222 TRP A CZ3 
1819 C CH2 . TRP A 232 ? 0.2799 0.2429 0.2344 -0.0435 -0.0183 0.0035  222 TRP A CH2 
1820 N N   . GLY A 233 ? 0.2685 0.2536 0.2451 -0.0326 -0.0104 0.0029  223 GLY A N   
1821 C CA  . GLY A 233 ? 0.2687 0.2506 0.2479 -0.0285 -0.0097 0.0025  223 GLY A CA  
1822 C C   . GLY A 233 ? 0.2730 0.2503 0.2489 -0.0281 -0.0113 0.0030  223 GLY A C   
1823 O O   . GLY A 233 ? 0.2804 0.2555 0.2514 -0.0310 -0.0131 0.0036  223 GLY A O   
1824 N N   . VAL A 234 ? 0.2745 0.2503 0.2527 -0.0246 -0.0107 0.0027  224 VAL A N   
1825 C CA  . VAL A 234 ? 0.2783 0.2505 0.2538 -0.0237 -0.0120 0.0028  224 VAL A CA  
1826 C C   . VAL A 234 ? 0.2875 0.2646 0.2646 -0.0239 -0.0115 0.0039  224 VAL A C   
1827 O O   . VAL A 234 ? 0.2854 0.2676 0.2676 -0.0222 -0.0097 0.0045  224 VAL A O   
1828 C CB  . VAL A 234 ? 0.2792 0.2496 0.2570 -0.0200 -0.0115 0.0021  224 VAL A CB  
1829 C CG1 . VAL A 234 ? 0.2866 0.2540 0.2613 -0.0190 -0.0130 0.0019  224 VAL A CG1 
1830 C CG2 . VAL A 234 ? 0.2846 0.2513 0.2615 -0.0195 -0.0118 0.0010  224 VAL A CG2 
1831 N N   . HIS A 235 ? 0.2968 0.2721 0.2694 -0.0261 -0.0132 0.0042  225 HIS A N   
1832 C CA  . HIS A 235 ? 0.3094 0.2896 0.2831 -0.0267 -0.0129 0.0052  225 HIS A CA  
1833 C C   . HIS A 235 ? 0.3023 0.2821 0.2770 -0.0238 -0.0128 0.0052  225 HIS A C   
1834 O O   . HIS A 235 ? 0.3002 0.2749 0.2725 -0.0225 -0.0140 0.0042  225 HIS A O   
1835 C CB  . HIS A 235 ? 0.3350 0.3142 0.3034 -0.0309 -0.0146 0.0055  225 HIS A CB  
1836 C CG  . HIS A 235 ? 0.3556 0.3380 0.3238 -0.0340 -0.0143 0.0059  225 HIS A CG  
1837 N ND1 . HIS A 235 ? 0.3733 0.3633 0.3432 -0.0358 -0.0134 0.0067  225 HIS A ND1 
1838 C CD2 . HIS A 235 ? 0.3718 0.3518 0.3385 -0.0355 -0.0146 0.0054  225 HIS A CD2 
1839 C CE1 . HIS A 235 ? 0.3801 0.3725 0.3496 -0.0384 -0.0132 0.0066  225 HIS A CE1 
1840 N NE2 . HIS A 235 ? 0.3796 0.3659 0.3471 -0.0384 -0.0139 0.0059  225 HIS A NE2 
1841 N N   . VAL A 236 ? 0.2969 0.2828 0.2755 -0.0227 -0.0115 0.0064  226 VAL A N   
1842 C CA  . VAL A 236 ? 0.3051 0.2921 0.2852 -0.0201 -0.0113 0.0067  226 VAL A CA  
1843 C C   . VAL A 236 ? 0.3172 0.3024 0.2924 -0.0218 -0.0132 0.0062  226 VAL A C   
1844 O O   . VAL A 236 ? 0.3218 0.3099 0.2957 -0.0243 -0.0135 0.0069  226 VAL A O   
1845 C CB  . VAL A 236 ? 0.3023 0.2963 0.2877 -0.0186 -0.0095 0.0084  226 VAL A CB  
1846 C CG1 . VAL A 236 ? 0.3099 0.3057 0.2964 -0.0166 -0.0094 0.0091  226 VAL A CG1 
1847 C CG2 . VAL A 236 ? 0.2978 0.2929 0.2879 -0.0169 -0.0078 0.0087  226 VAL A CG2 
1848 N N   . PRO A 237 ? 0.3321 0.3129 0.3047 -0.0203 -0.0144 0.0049  227 PRO A N   
1849 C CA  . PRO A 237 ? 0.3494 0.3275 0.3169 -0.0219 -0.0165 0.0040  227 PRO A CA  
1850 C C   . PRO A 237 ? 0.3562 0.3404 0.3246 -0.0228 -0.0161 0.0051  227 PRO A C   
1851 O O   . PRO A 237 ? 0.3644 0.3478 0.3290 -0.0258 -0.0175 0.0049  227 PRO A O   
1852 C CB  . PRO A 237 ? 0.3545 0.3289 0.3207 -0.0189 -0.0175 0.0023  227 PRO A CB  
1853 C CG  . PRO A 237 ? 0.3532 0.3252 0.3213 -0.0173 -0.0167 0.0019  227 PRO A CG  
1854 C CD  . PRO A 237 ? 0.3402 0.3178 0.3136 -0.0175 -0.0143 0.0038  227 PRO A CD  
1855 N N   . SER A 238 ? 0.3661 0.3563 0.3393 -0.0205 -0.0144 0.0064  228 SER A N   
1856 C CA  . SER A 238 ? 0.3736 0.3703 0.3481 -0.0210 -0.0140 0.0076  228 SER A CA  
1857 C C   . SER A 238 ? 0.3758 0.3780 0.3526 -0.0227 -0.0129 0.0093  228 SER A C   
1858 O O   . SER A 238 ? 0.3727 0.3806 0.3501 -0.0234 -0.0127 0.0103  228 SER A O   
1859 C CB  . SER A 238 ? 0.3836 0.3844 0.3619 -0.0179 -0.0128 0.0085  228 SER A CB  
1860 O OG  . SER A 238 ? 0.3972 0.4002 0.3805 -0.0162 -0.0110 0.0101  228 SER A OG  
1861 N N   . ASN A 239 ? 0.3710 0.3723 0.3491 -0.0233 -0.0122 0.0095  229 ASN A N   
1862 C CA  . ASN A 239 ? 0.3744 0.3815 0.3546 -0.0249 -0.0114 0.0106  229 ASN A CA  
1863 C C   . ASN A 239 ? 0.3843 0.3883 0.3629 -0.0270 -0.0116 0.0098  229 ASN A C   
1864 O O   . ASN A 239 ? 0.3628 0.3679 0.3451 -0.0254 -0.0103 0.0099  229 ASN A O   
1865 C CB  . ASN A 239 ? 0.3689 0.3818 0.3552 -0.0219 -0.0095 0.0123  229 ASN A CB  
1866 C CG  . ASN A 239 ? 0.3739 0.3944 0.3624 -0.0228 -0.0088 0.0134  229 ASN A CG  
1867 O OD1 . ASN A 239 ? 0.3853 0.4071 0.3711 -0.0260 -0.0094 0.0128  229 ASN A OD1 
1868 N ND2 . ASN A 239 ? 0.3569 0.3825 0.3503 -0.0201 -0.0076 0.0150  229 ASN A ND2 
1869 N N   . PRO A 240 ? 0.4009 0.4009 0.3738 -0.0305 -0.0134 0.0089  230 PRO A N   
1870 C CA  . PRO A 240 ? 0.4217 0.4177 0.3916 -0.0332 -0.0142 0.0082  230 PRO A CA  
1871 C C   . PRO A 240 ? 0.4000 0.4013 0.3731 -0.0340 -0.0128 0.0087  230 PRO A C   
1872 O O   . PRO A 240 ? 0.4018 0.4000 0.3741 -0.0347 -0.0129 0.0080  230 PRO A O   
1873 C CB  . PRO A 240 ? 0.4357 0.4295 0.3995 -0.0376 -0.0162 0.0079  230 PRO A CB  
1874 C CG  . PRO A 240 ? 0.4353 0.4274 0.3977 -0.0363 -0.0171 0.0075  230 PRO A CG  
1875 C CD  . PRO A 240 ? 0.4239 0.4227 0.3924 -0.0325 -0.0150 0.0085  230 PRO A CD  
1876 N N   . LYS A 241 ? 0.3861 0.3958 0.3626 -0.0337 -0.0115 0.0096  231 LYS A N   
1877 C CA  . LYS A 241 ? 0.3797 0.3956 0.3595 -0.0341 -0.0103 0.0097  231 LYS A CA  
1878 C C   . LYS A 241 ? 0.3402 0.3560 0.3253 -0.0300 -0.0086 0.0095  231 LYS A C   
1879 O O   . LYS A 241 ? 0.3311 0.3509 0.3187 -0.0300 -0.0077 0.0090  231 LYS A O   
1880 C CB  . LYS A 241 ? 0.4107 0.4360 0.3923 -0.0349 -0.0097 0.0106  231 LYS A CB  
1881 C CG  . LYS A 241 ? 0.4338 0.4634 0.4202 -0.0309 -0.0086 0.0117  231 LYS A CG  
1882 C CD  . LYS A 241 ? 0.4519 0.4894 0.4379 -0.0326 -0.0088 0.0125  231 LYS A CD  
1883 C CE  . LYS A 241 ? 0.4792 0.5213 0.4698 -0.0287 -0.0078 0.0139  231 LYS A CE  
1884 N NZ  . LYS A 241 ? 0.5034 0.5515 0.4996 -0.0257 -0.0064 0.0142  231 LYS A NZ  
1885 N N   . HIS A 242 ? 0.3085 0.3201 0.2952 -0.0268 -0.0084 0.0096  232 HIS A N   
1886 C CA  . HIS A 242 ? 0.2891 0.2993 0.2801 -0.0235 -0.0071 0.0093  232 HIS A CA  
1887 C C   . HIS A 242 ? 0.2820 0.2852 0.2706 -0.0239 -0.0076 0.0081  232 HIS A C   
1888 O O   . HIS A 242 ? 0.2860 0.2836 0.2703 -0.0248 -0.0091 0.0077  232 HIS A O   
1889 C CB  . HIS A 242 ? 0.2856 0.2958 0.2796 -0.0201 -0.0065 0.0104  232 HIS A CB  
1890 C CG  . HIS A 242 ? 0.2876 0.3047 0.2856 -0.0185 -0.0056 0.0119  232 HIS A CG  
1891 N ND1 . HIS A 242 ? 0.2819 0.3011 0.2851 -0.0154 -0.0043 0.0124  232 HIS A ND1 
1892 C CD2 . HIS A 242 ? 0.2872 0.3096 0.2845 -0.0195 -0.0059 0.0128  232 HIS A CD2 
1893 C CE1 . HIS A 242 ? 0.2822 0.3075 0.2878 -0.0143 -0.0040 0.0138  232 HIS A CE1 
1894 N NE2 . HIS A 242 ? 0.2826 0.3104 0.2848 -0.0167 -0.0049 0.0141  232 HIS A NE2 
1895 N N   A VAL A 243 ? 0.2748 0.2784 0.2661 -0.0230 -0.0066 0.0073  233 VAL A N   
1896 N N   B VAL A 243 ? 0.2742 0.2777 0.2654 -0.0231 -0.0067 0.0073  233 VAL A N   
1897 C CA  A VAL A 243 ? 0.2757 0.2734 0.2657 -0.0228 -0.0069 0.0062  233 VAL A CA  
1898 C CA  B VAL A 243 ? 0.2747 0.2723 0.2646 -0.0229 -0.0069 0.0062  233 VAL A CA  
1899 C C   A VAL A 243 ? 0.2729 0.2696 0.2675 -0.0191 -0.0055 0.0061  233 VAL A C   
1900 C C   B VAL A 243 ? 0.2724 0.2691 0.2670 -0.0191 -0.0056 0.0061  233 VAL A C   
1901 O O   A VAL A 243 ? 0.2662 0.2670 0.2654 -0.0172 -0.0042 0.0066  233 VAL A O   
1902 O O   B VAL A 243 ? 0.2657 0.2666 0.2649 -0.0172 -0.0042 0.0066  233 VAL A O   
1903 C CB  A VAL A 243 ? 0.2802 0.2792 0.2694 -0.0252 -0.0068 0.0052  233 VAL A CB  
1904 C CB  B VAL A 243 ? 0.2782 0.2767 0.2672 -0.0252 -0.0069 0.0052  233 VAL A CB  
1905 C CG1 A VAL A 243 ? 0.2798 0.2750 0.2701 -0.0238 -0.0063 0.0041  233 VAL A CG1 
1906 C CG1 B VAL A 243 ? 0.2853 0.2851 0.2694 -0.0294 -0.0083 0.0056  233 VAL A CG1 
1907 C CG2 A VAL A 243 ? 0.2868 0.2836 0.2698 -0.0294 -0.0087 0.0053  233 VAL A CG2 
1908 C CG2 B VAL A 243 ? 0.2720 0.2765 0.2664 -0.0235 -0.0051 0.0048  233 VAL A CG2 
1909 N N   . VAL A 244 ? 0.2715 0.2627 0.2646 -0.0182 -0.0060 0.0055  234 VAL A N   
1910 C CA  . VAL A 244 ? 0.2668 0.2570 0.2638 -0.0152 -0.0048 0.0055  234 VAL A CA  
1911 C C   . VAL A 244 ? 0.2633 0.2542 0.2632 -0.0148 -0.0037 0.0044  234 VAL A C   
1912 O O   . VAL A 244 ? 0.2819 0.2710 0.2794 -0.0165 -0.0042 0.0033  234 VAL A O   
1913 C CB  . VAL A 244 ? 0.2592 0.2444 0.2536 -0.0144 -0.0057 0.0049  234 VAL A CB  
1914 C CG1 . VAL A 244 ? 0.2584 0.2434 0.2568 -0.0118 -0.0045 0.0049  234 VAL A CG1 
1915 C CG2 . VAL A 244 ? 0.2616 0.2465 0.2531 -0.0147 -0.0069 0.0055  234 VAL A CG2 
1916 N N   . TYR A 245 ? 0.2590 0.2523 0.2639 -0.0126 -0.0023 0.0048  235 TYR A N   
1917 C CA  . TYR A 245 ? 0.2561 0.2504 0.2640 -0.0120 -0.0012 0.0035  235 TYR A CA  
1918 C C   . TYR A 245 ? 0.2496 0.2395 0.2579 -0.0112 -0.0009 0.0024  235 TYR A C   
1919 O O   . TYR A 245 ? 0.2501 0.2368 0.2562 -0.0110 -0.0015 0.0027  235 TYR A O   
1920 C CB  . TYR A 245 ? 0.2660 0.2642 0.2788 -0.0099 -0.0002 0.0042  235 TYR A CB  
1921 C CG  . TYR A 245 ? 0.2782 0.2788 0.2941 -0.0093 0.0007  0.0025  235 TYR A CG  
1922 C CD1 . TYR A 245 ? 0.2958 0.2994 0.3100 -0.0115 0.0005  0.0011  235 TYR A CD1 
1923 C CD2 . TYR A 245 ? 0.2916 0.2916 0.3121 -0.0067 0.0016  0.0022  235 TYR A CD2 
1924 C CE1 . TYR A 245 ? 0.3103 0.3170 0.3275 -0.0108 0.0013  -0.0007 235 TYR A CE1 
1925 C CE2 . TYR A 245 ? 0.3032 0.3054 0.3266 -0.0058 0.0024  0.0002  235 TYR A CE2 
1926 C CZ  . TYR A 245 ? 0.3104 0.3164 0.3323 -0.0078 0.0023  -0.0013 235 TYR A CZ  
1927 O OH  . TYR A 245 ? 0.3300 0.3388 0.3548 -0.0068 0.0031  -0.0035 235 TYR A OH  
1928 N N   . VAL A 246 ? 0.2480 0.2385 0.2591 -0.0106 0.0000  0.0011  236 VAL A N   
1929 C CA  . VAL A 246 ? 0.2492 0.2364 0.2606 -0.0103 0.0004  -0.0002 236 VAL A CA  
1930 C C   . VAL A 246 ? 0.2455 0.2300 0.2578 -0.0088 0.0006  0.0005  236 VAL A C   
1931 O O   . VAL A 246 ? 0.2511 0.2328 0.2614 -0.0090 0.0002  -0.0001 236 VAL A O   
1932 C CB  . VAL A 246 ? 0.2584 0.2473 0.2733 -0.0097 0.0015  -0.0019 236 VAL A CB  
1933 C CG1 . VAL A 246 ? 0.2629 0.2529 0.2826 -0.0074 0.0025  -0.0014 236 VAL A CG1 
1934 C CG2 . VAL A 246 ? 0.2595 0.2454 0.2739 -0.0100 0.0018  -0.0035 236 VAL A CG2 
1935 N N   . TRP A 247 ? 0.2459 0.2314 0.2610 -0.0073 0.0011  0.0021  237 TRP A N   
1936 C CA  . TRP A 247 ? 0.2519 0.2356 0.2687 -0.0061 0.0015  0.0029  237 TRP A CA  
1937 C C   . TRP A 247 ? 0.2511 0.2332 0.2643 -0.0066 0.0006  0.0030  237 TRP A C   
1938 O O   . TRP A 247 ? 0.2630 0.2432 0.2757 -0.0066 0.0007  0.0020  237 TRP A O   
1939 C CB  . TRP A 247 ? 0.2611 0.2461 0.2809 -0.0048 0.0019  0.0050  237 TRP A CB  
1940 C CG  . TRP A 247 ? 0.2673 0.2543 0.2904 -0.0038 0.0024  0.0047  237 TRP A CG  
1941 C CD1 . TRP A 247 ? 0.2725 0.2628 0.2962 -0.0033 0.0022  0.0057  237 TRP A CD1 
1942 C CD2 . TRP A 247 ? 0.2771 0.2630 0.3031 -0.0031 0.0033  0.0030  237 TRP A CD2 
1943 N NE1 . TRP A 247 ? 0.2703 0.2620 0.2973 -0.0020 0.0028  0.0046  237 TRP A NE1 
1944 C CE2 . TRP A 247 ? 0.2786 0.2674 0.3070 -0.0018 0.0034  0.0029  237 TRP A CE2 
1945 C CE3 . TRP A 247 ? 0.2869 0.2700 0.3137 -0.0033 0.0039  0.0013  237 TRP A CE3 
1946 C CZ2 . TRP A 247 ? 0.2881 0.2769 0.3197 -0.0006 0.0040  0.0010  237 TRP A CZ2 
1947 C CZ3 . TRP A 247 ? 0.2916 0.2747 0.3216 -0.0024 0.0046  -0.0003 237 TRP A CZ3 
1948 C CH2 . TRP A 247 ? 0.2957 0.2814 0.3279 -0.0010 0.0046  -0.0006 237 TRP A CH2 
1949 N N   . ILE A 248 ? 0.2477 0.2308 0.2583 -0.0070 -0.0003 0.0040  238 ILE A N   
1950 C CA  . ILE A 248 ? 0.2450 0.2267 0.2519 -0.0071 -0.0014 0.0038  238 ILE A CA  
1951 C C   . ILE A 248 ? 0.2440 0.2230 0.2471 -0.0081 -0.0024 0.0019  238 ILE A C   
1952 O O   . ILE A 248 ? 0.2489 0.2260 0.2503 -0.0076 -0.0029 0.0009  238 ILE A O   
1953 C CB  . ILE A 248 ? 0.2504 0.2339 0.2557 -0.0072 -0.0022 0.0053  238 ILE A CB  
1954 C CG1 . ILE A 248 ? 0.2567 0.2428 0.2656 -0.0061 -0.0013 0.0074  238 ILE A CG1 
1955 C CG2 . ILE A 248 ? 0.2569 0.2389 0.2582 -0.0072 -0.0035 0.0045  238 ILE A CG2 
1956 C CD1 . ILE A 248 ? 0.2628 0.2517 0.2709 -0.0062 -0.0018 0.0090  238 ILE A CD1 
1957 N N   . ASP A 249 ? 0.2398 0.2188 0.2415 -0.0096 -0.0028 0.0015  239 ASP A N   
1958 C CA  . ASP A 249 ? 0.2371 0.2132 0.2346 -0.0109 -0.0041 0.0002  239 ASP A CA  
1959 C C   . ASP A 249 ? 0.2343 0.2087 0.2324 -0.0103 -0.0037 -0.0012 239 ASP A C   
1960 O O   . ASP A 249 ? 0.2443 0.2160 0.2395 -0.0098 -0.0047 -0.0021 239 ASP A O   
1961 C CB  . ASP A 249 ? 0.2438 0.2212 0.2402 -0.0130 -0.0043 0.0003  239 ASP A CB  
1962 C CG  . ASP A 249 ? 0.2491 0.2233 0.2406 -0.0149 -0.0059 -0.0005 239 ASP A CG  
1963 O OD1 . ASP A 249 ? 0.2607 0.2310 0.2491 -0.0144 -0.0072 -0.0011 239 ASP A OD1 
1964 O OD2 . ASP A 249 ? 0.2554 0.2312 0.2461 -0.0170 -0.0060 -0.0004 239 ASP A OD2 
1965 N N   . ALA A 250 ? 0.2255 0.2017 0.2276 -0.0101 -0.0022 -0.0016 240 ALA A N   
1966 C CA  . ALA A 250 ? 0.2289 0.2039 0.2315 -0.0099 -0.0017 -0.0032 240 ALA A CA  
1967 C C   . ALA A 250 ? 0.2270 0.2014 0.2307 -0.0084 -0.0013 -0.0034 240 ALA A C   
1968 O O   . ALA A 250 ? 0.2388 0.2117 0.2405 -0.0081 -0.0019 -0.0046 240 ALA A O   
1969 C CB  . ALA A 250 ? 0.2303 0.2074 0.2367 -0.0102 -0.0002 -0.0040 240 ALA A CB  
1970 N N   . LEU A 251 ? 0.2232 0.1991 0.2299 -0.0075 -0.0005 -0.0022 241 LEU A N   
1971 C CA  . LEU A 251 ? 0.2293 0.2055 0.2372 -0.0066 0.0000  -0.0022 241 LEU A CA  
1972 C C   . LEU A 251 ? 0.2210 0.1967 0.2254 -0.0059 -0.0013 -0.0027 241 LEU A C   
1973 O O   . LEU A 251 ? 0.2250 0.2010 0.2292 -0.0053 -0.0012 -0.0038 241 LEU A O   
1974 C CB  . LEU A 251 ? 0.2289 0.2066 0.2404 -0.0062 0.0010  -0.0004 241 LEU A CB  
1975 C CG  . LEU A 251 ? 0.2368 0.2145 0.2525 -0.0062 0.0023  -0.0003 241 LEU A CG  
1976 C CD1 . LEU A 251 ? 0.2442 0.2226 0.2626 -0.0057 0.0028  0.0019  241 LEU A CD1 
1977 C CD2 . LEU A 251 ? 0.2447 0.2215 0.2618 -0.0065 0.0031  -0.0020 241 LEU A CD2 
1978 N N   . VAL A 252 ? 0.2158 0.1910 0.2172 -0.0059 -0.0026 -0.0021 242 VAL A N   
1979 C CA  . VAL A 252 ? 0.2129 0.1875 0.2108 -0.0048 -0.0040 -0.0028 242 VAL A CA  
1980 C C   . VAL A 252 ? 0.2134 0.1851 0.2078 -0.0044 -0.0054 -0.0048 242 VAL A C   
1981 O O   . VAL A 252 ? 0.2188 0.1899 0.2104 -0.0030 -0.0067 -0.0058 242 VAL A O   
1982 C CB  . VAL A 252 ? 0.2160 0.1907 0.2117 -0.0047 -0.0052 -0.0019 242 VAL A CB  
1983 C CG1 . VAL A 252 ? 0.2132 0.1913 0.2122 -0.0047 -0.0040 0.0001  242 VAL A CG1 
1984 C CG2 . VAL A 252 ? 0.2168 0.1887 0.2093 -0.0060 -0.0064 -0.0019 242 VAL A CG2 
1985 N N   . ASN A 253 ? 0.2061 0.1762 0.2004 -0.0056 -0.0052 -0.0053 243 ASN A N   
1986 C CA  . ASN A 253 ? 0.2100 0.1776 0.2012 -0.0053 -0.0065 -0.0069 243 ASN A CA  
1987 C C   . ASN A 253 ? 0.2062 0.1753 0.1978 -0.0035 -0.0064 -0.0083 243 ASN A C   
1988 O O   . ASN A 253 ? 0.2131 0.1803 0.2011 -0.0022 -0.0081 -0.0096 243 ASN A O   
1989 C CB  . ASN A 253 ? 0.2067 0.1739 0.1987 -0.0069 -0.0058 -0.0073 243 ASN A CB  
1990 C CG  . ASN A 253 ? 0.1973 0.1667 0.1929 -0.0066 -0.0041 -0.0083 243 ASN A CG  
1991 O OD1 . ASN A 253 ? 0.2073 0.1764 0.2016 -0.0059 -0.0046 -0.0097 243 ASN A OD1 
1992 N ND2 . ASN A 253 ? 0.2034 0.1750 0.2034 -0.0072 -0.0023 -0.0078 243 ASN A ND2 
1993 N N   . TYR A 254 ? 0.2039 0.1764 0.1996 -0.0034 -0.0045 -0.0080 244 TYR A N   
1994 C CA  . TYR A 254 ? 0.2046 0.1796 0.2012 -0.0022 -0.0042 -0.0093 244 TYR A CA  
1995 C C   . TYR A 254 ? 0.2048 0.1811 0.1990 -0.0003 -0.0055 -0.0098 244 TYR A C   
1996 O O   . TYR A 254 ? 0.2156 0.1939 0.2090 0.0010  -0.0059 -0.0114 244 TYR A O   
1997 C CB  . TYR A 254 ? 0.2041 0.1820 0.2054 -0.0032 -0.0020 -0.0085 244 TYR A CB  
1998 C CG  . TYR A 254 ? 0.2082 0.1852 0.2124 -0.0047 -0.0006 -0.0085 244 TYR A CG  
1999 C CD1 . TYR A 254 ? 0.2098 0.1872 0.2176 -0.0056 0.0006  -0.0069 244 TYR A CD1 
2000 C CD2 . TYR A 254 ? 0.2087 0.1846 0.2120 -0.0051 -0.0008 -0.0100 244 TYR A CD2 
2001 C CE1 . TYR A 254 ? 0.2088 0.1855 0.2193 -0.0066 0.0018  -0.0073 244 TYR A CE1 
2002 C CE2 . TYR A 254 ? 0.2120 0.1877 0.2180 -0.0064 0.0004  -0.0103 244 TYR A CE2 
2003 C CZ  . TYR A 254 ? 0.2135 0.1896 0.2231 -0.0070 0.0017  -0.0091 244 TYR A CZ  
2004 O OH  . TYR A 254 ? 0.2208 0.1968 0.2332 -0.0079 0.0029  -0.0098 244 TYR A OH  
2005 N N   . ILE A 255 ? 0.2104 0.1863 0.2035 -0.0002 -0.0061 -0.0087 245 ILE A N   
2006 C CA  . ILE A 255 ? 0.2157 0.1929 0.2063 0.0017  -0.0075 -0.0095 245 ILE A CA  
2007 C C   . ILE A 255 ? 0.2211 0.1936 0.2067 0.0025  -0.0100 -0.0103 245 ILE A C   
2008 O O   . ILE A 255 ? 0.2257 0.1980 0.2083 0.0048  -0.0118 -0.0121 245 ILE A O   
2009 C CB  . ILE A 255 ? 0.2248 0.2062 0.2179 0.0013  -0.0065 -0.0079 245 ILE A CB  
2010 C CG1 . ILE A 255 ? 0.2278 0.2075 0.2216 -0.0001 -0.0061 -0.0058 245 ILE A CG1 
2011 C CG2 . ILE A 255 ? 0.2310 0.2165 0.2281 0.0005  -0.0045 -0.0073 245 ILE A CG2 
2012 C CD1 . ILE A 255 ? 0.2295 0.2133 0.2254 -0.0003 -0.0053 -0.0040 245 ILE A CD1 
2013 N N   . SER A 256 ? 0.2162 0.1850 0.2007 0.0008  -0.0104 -0.0092 246 SER A N   
2014 C CA  . SER A 256 ? 0.2282 0.1917 0.2075 0.0010  -0.0129 -0.0097 246 SER A CA  
2015 C C   . SER A 256 ? 0.2353 0.1953 0.2113 0.0023  -0.0146 -0.0115 246 SER A C   
2016 O O   . SER A 256 ? 0.2519 0.2083 0.2235 0.0040  -0.0171 -0.0127 246 SER A O   
2017 C CB  . SER A 256 ? 0.2322 0.1934 0.2111 -0.0016 -0.0128 -0.0081 246 SER A CB  
2018 O OG  . SER A 256 ? 0.2315 0.1916 0.2112 -0.0031 -0.0121 -0.0079 246 SER A OG  
2019 N N   . ALA A 257 ? 0.2404 0.2015 0.2184 0.0017  -0.0134 -0.0117 247 ALA A N   
2020 C CA  . ALA A 257 ? 0.2437 0.2023 0.2189 0.0030  -0.0150 -0.0132 247 ALA A CA  
2021 C C   . ALA A 257 ? 0.2532 0.2138 0.2272 0.0065  -0.0161 -0.0153 247 ALA A C   
2022 O O   . ALA A 257 ? 0.2590 0.2165 0.2294 0.0084  -0.0183 -0.0167 247 ALA A O   
2023 C CB  . ALA A 257 ? 0.2415 0.2022 0.2198 0.0016  -0.0132 -0.0132 247 ALA A CB  
2024 N N   . LEU A 258 ? 0.2445 0.2106 0.2216 0.0073  -0.0147 -0.0155 248 LEU A N   
2025 C CA  . LEU A 258 ? 0.2525 0.2221 0.2287 0.0104  -0.0156 -0.0176 248 LEU A CA  
2026 C C   . LEU A 258 ? 0.2703 0.2381 0.2432 0.0124  -0.0178 -0.0184 248 LEU A C   
2027 O O   . LEU A 258 ? 0.2914 0.2630 0.2638 0.0152  -0.0185 -0.0204 248 LEU A O   
2028 C CB  . LEU A 258 ? 0.2441 0.2213 0.2252 0.0099  -0.0131 -0.0173 248 LEU A CB  
2029 C CG  . LEU A 258 ? 0.2386 0.2179 0.2234 0.0079  -0.0109 -0.0166 248 LEU A CG  
2030 C CD1 . LEU A 258 ? 0.2371 0.2230 0.2261 0.0070  -0.0087 -0.0160 248 LEU A CD1 
2031 C CD2 . LEU A 258 ? 0.2450 0.2239 0.2283 0.0092  -0.0117 -0.0185 248 LEU A CD2 
2032 N N   . GLY A 259 ? 0.2708 0.2334 0.2414 0.0109  -0.0188 -0.0172 249 GLY A N   
2033 C CA  . GLY A 259 ? 0.2798 0.2398 0.2467 0.0126  -0.0210 -0.0182 249 GLY A CA  
2034 C C   . GLY A 259 ? 0.2817 0.2473 0.2513 0.0123  -0.0196 -0.0176 249 GLY A C   
2035 O O   . GLY A 259 ? 0.2947 0.2603 0.2619 0.0142  -0.0212 -0.0190 249 GLY A O   
2036 N N   . TYR A 260 ? 0.2839 0.2539 0.2582 0.0099  -0.0168 -0.0155 250 TYR A N   
2037 C CA  . TYR A 260 ? 0.2893 0.2643 0.2661 0.0092  -0.0155 -0.0142 250 TYR A CA  
2038 C C   . TYR A 260 ? 0.3028 0.2739 0.2765 0.0086  -0.0170 -0.0138 250 TYR A C   
2039 O O   . TYR A 260 ? 0.2985 0.2640 0.2703 0.0068  -0.0177 -0.0129 250 TYR A O   
2040 C CB  . TYR A 260 ? 0.2839 0.2622 0.2657 0.0066  -0.0126 -0.0117 250 TYR A CB  
2041 C CG  . TYR A 260 ? 0.2839 0.2668 0.2684 0.0055  -0.0113 -0.0098 250 TYR A CG  
2042 C CD1 . TYR A 260 ? 0.2906 0.2797 0.2760 0.0068  -0.0111 -0.0104 250 TYR A CD1 
2043 C CD2 . TYR A 260 ? 0.2818 0.2635 0.2680 0.0032  -0.0103 -0.0073 250 TYR A CD2 
2044 C CE1 . TYR A 260 ? 0.2947 0.2882 0.2823 0.0057  -0.0100 -0.0084 250 TYR A CE1 
2045 C CE2 . TYR A 260 ? 0.2839 0.2698 0.2724 0.0024  -0.0092 -0.0054 250 TYR A CE2 
2046 C CZ  . TYR A 260 ? 0.2926 0.2842 0.2818 0.0036  -0.0090 -0.0058 250 TYR A CZ  
2047 O OH  . TYR A 260 ? 0.3083 0.3042 0.2996 0.0026  -0.0081 -0.0037 250 TYR A OH  
2048 N N   . LEU A 261 ? 0.3099 0.2843 0.2830 0.0100  -0.0176 -0.0147 251 LEU A N   
2049 C CA  . LEU A 261 ? 0.3294 0.3009 0.2995 0.0095  -0.0191 -0.0147 251 LEU A CA  
2050 C C   . LEU A 261 ? 0.3543 0.3173 0.3187 0.0102  -0.0222 -0.0163 251 LEU A C   
2051 O O   . LEU A 261 ? 0.3798 0.3390 0.3416 0.0087  -0.0233 -0.0157 251 LEU A O   
2052 C CB  . LEU A 261 ? 0.3252 0.2975 0.2978 0.0062  -0.0174 -0.0116 251 LEU A CB  
2053 C CG  . LEU A 261 ? 0.3263 0.3060 0.3041 0.0054  -0.0147 -0.0096 251 LEU A CG  
2054 C CD1 . LEU A 261 ? 0.3229 0.3026 0.3027 0.0026  -0.0135 -0.0067 251 LEU A CD1 
2055 C CD2 . LEU A 261 ? 0.3301 0.3159 0.3082 0.0071  -0.0149 -0.0106 251 LEU A CD2 
2056 N N   . SER A 262 ? 0.3520 0.3120 0.3143 0.0125  -0.0236 -0.0182 252 SER A N   
2057 C CA  . SER A 262 ? 0.3678 0.3191 0.3243 0.0136  -0.0269 -0.0198 252 SER A CA  
2058 C C   . SER A 262 ? 0.3826 0.3345 0.3364 0.0178  -0.0292 -0.0232 252 SER A C   
2059 O O   . SER A 262 ? 0.3758 0.3356 0.3324 0.0196  -0.0280 -0.0243 252 SER A O   
2060 C CB  . SER A 262 ? 0.3688 0.3161 0.3244 0.0134  -0.0273 -0.0196 252 SER A CB  
2061 O OG  . SER A 262 ? 0.3575 0.3083 0.3140 0.0169  -0.0274 -0.0218 252 SER A OG  
2062 N N   . ASP A 263 ? 0.4154 0.3590 0.3636 0.0195  -0.0325 -0.0250 253 ASP A N   
2063 C CA  . ASP A 263 ? 0.4353 0.3786 0.3805 0.0243  -0.0351 -0.0288 253 ASP A CA  
2064 C C   . ASP A 263 ? 0.4146 0.3624 0.3614 0.0279  -0.0350 -0.0307 253 ASP A C   
2065 O O   . ASP A 263 ? 0.4278 0.3768 0.3727 0.0323  -0.0370 -0.0341 253 ASP A O   
2066 C CB  . ASP A 263 ? 0.4789 0.4107 0.4173 0.0252  -0.0392 -0.0302 253 ASP A CB  
2067 C CG  . ASP A 263 ? 0.5085 0.4319 0.4438 0.0242  -0.0407 -0.0290 253 ASP A CG  
2068 O OD1 . ASP A 263 ? 0.5725 0.4859 0.5019 0.0244  -0.0442 -0.0297 253 ASP A OD1 
2069 O OD2 . ASP A 263 ? 0.5321 0.4588 0.4706 0.0230  -0.0386 -0.0274 253 ASP A OD2 
2070 N N   . ASP A 264 ? 0.3879 0.3385 0.3382 0.0261  -0.0326 -0.0288 254 ASP A N   
2071 C CA  . ASP A 264 ? 0.3695 0.3254 0.3216 0.0289  -0.0322 -0.0304 254 ASP A CA  
2072 C C   . ASP A 264 ? 0.3461 0.3091 0.3040 0.0258  -0.0283 -0.0280 254 ASP A C   
2073 O O   . ASP A 264 ? 0.3335 0.2935 0.2923 0.0232  -0.0273 -0.0260 254 ASP A O   
2074 C CB  . ASP A 264 ? 0.3813 0.3292 0.3293 0.0305  -0.0348 -0.0312 254 ASP A CB  
2075 C CG  . ASP A 264 ? 0.3881 0.3415 0.3381 0.0329  -0.0341 -0.0326 254 ASP A CG  
2076 O OD1 . ASP A 264 ? 0.3704 0.3338 0.3243 0.0340  -0.0322 -0.0336 254 ASP A OD1 
2077 O OD2 . ASP A 264 ? 0.3897 0.3375 0.3372 0.0334  -0.0356 -0.0324 254 ASP A OD2 
2078 N N   . GLU A 265 ? 0.3248 0.2972 0.2865 0.0261  -0.0263 -0.0283 255 GLU A N   
2079 C CA  . GLU A 265 ? 0.3159 0.2951 0.2831 0.0233  -0.0228 -0.0261 255 GLU A CA  
2080 C C   . GLU A 265 ? 0.2992 0.2847 0.2684 0.0250  -0.0220 -0.0276 255 GLU A C   
2081 O O   . GLU A 265 ? 0.2895 0.2816 0.2630 0.0230  -0.0194 -0.0263 255 GLU A O   
2082 C CB  . GLU A 265 ? 0.3252 0.3109 0.2953 0.0218  -0.0210 -0.0248 255 GLU A CB  
2083 C CG  . GLU A 265 ? 0.3385 0.3195 0.3076 0.0194  -0.0211 -0.0228 255 GLU A CG  
2084 C CD  . GLU A 265 ? 0.3492 0.3371 0.3213 0.0180  -0.0194 -0.0214 255 GLU A CD  
2085 O OE1 . GLU A 265 ? 0.3811 0.3752 0.3531 0.0202  -0.0199 -0.0234 255 GLU A OE1 
2086 O OE2 . GLU A 265 ? 0.3455 0.3327 0.3198 0.0148  -0.0178 -0.0184 255 GLU A OE2 
2087 N N   . SER A 266 ? 0.2970 0.2802 0.2629 0.0286  -0.0244 -0.0304 256 SER A N   
2088 C CA  . SER A 266 ? 0.2953 0.2856 0.2628 0.0307  -0.0239 -0.0323 256 SER A CA  
2089 C C   . SER A 266 ? 0.2915 0.2834 0.2626 0.0275  -0.0214 -0.0302 256 SER A C   
2090 O O   . SER A 266 ? 0.2863 0.2865 0.2608 0.0269  -0.0194 -0.0304 256 SER A O   
2091 C CB  . SER A 266 ? 0.3100 0.2970 0.2731 0.0356  -0.0273 -0.0356 256 SER A CB  
2092 O OG  . SER A 266 ? 0.3170 0.2939 0.2770 0.0351  -0.0290 -0.0346 256 SER A OG  
2093 N N   . LEU A 267 ? 0.2757 0.2600 0.2460 0.0252  -0.0213 -0.0282 257 LEU A N   
2094 C CA  . LEU A 267 ? 0.2738 0.2595 0.2476 0.0220  -0.0189 -0.0265 257 LEU A CA  
2095 C C   . LEU A 267 ? 0.2580 0.2488 0.2365 0.0187  -0.0158 -0.0242 257 LEU A C   
2096 O O   . LEU A 267 ? 0.2660 0.2621 0.2480 0.0172  -0.0138 -0.0239 257 LEU A O   
2097 C CB  . LEU A 267 ? 0.2767 0.2540 0.2487 0.0201  -0.0194 -0.0248 257 LEU A CB  
2098 C CG  . LEU A 267 ? 0.2910 0.2623 0.2583 0.0226  -0.0224 -0.0263 257 LEU A CG  
2099 C CD1 . LEU A 267 ? 0.2978 0.2615 0.2635 0.0196  -0.0227 -0.0241 257 LEU A CD1 
2100 C CD2 . LEU A 267 ? 0.2932 0.2690 0.2611 0.0247  -0.0225 -0.0282 257 LEU A CD2 
2101 N N   . PHE A 268 ? 0.2572 0.2461 0.2357 0.0174  -0.0157 -0.0227 258 PHE A N   
2102 C CA  . PHE A 268 ? 0.2594 0.2525 0.2420 0.0145  -0.0131 -0.0203 258 PHE A CA  
2103 C C   . PHE A 268 ? 0.2630 0.2655 0.2478 0.0152  -0.0121 -0.0212 258 PHE A C   
2104 O O   . PHE A 268 ? 0.2540 0.2607 0.2425 0.0127  -0.0098 -0.0197 258 PHE A O   
2105 C CB  . PHE A 268 ? 0.2627 0.2525 0.2442 0.0136  -0.0136 -0.0188 258 PHE A CB  
2106 C CG  . PHE A 268 ? 0.2635 0.2575 0.2488 0.0111  -0.0114 -0.0163 258 PHE A CG  
2107 C CD1 . PHE A 268 ? 0.2690 0.2611 0.2573 0.0081  -0.0095 -0.0138 258 PHE A CD1 
2108 C CD2 . PHE A 268 ? 0.2759 0.2762 0.2619 0.0117  -0.0112 -0.0164 258 PHE A CD2 
2109 C CE1 . PHE A 268 ? 0.2644 0.2598 0.2561 0.0060  -0.0077 -0.0113 258 PHE A CE1 
2110 C CE2 . PHE A 268 ? 0.2736 0.2776 0.2629 0.0093  -0.0092 -0.0137 258 PHE A CE2 
2111 C CZ  . PHE A 268 ? 0.2719 0.2730 0.2640 0.0065  -0.0076 -0.0111 258 PHE A CZ  
2112 N N   . ASN A 269 ? 0.2673 0.2730 0.2498 0.0184  -0.0138 -0.0237 259 ASN A N   
2113 C CA  . ASN A 269 ? 0.2743 0.2901 0.2584 0.0193  -0.0131 -0.0250 259 ASN A CA  
2114 C C   . ASN A 269 ? 0.2822 0.3032 0.2682 0.0190  -0.0120 -0.0260 259 ASN A C   
2115 O O   . ASN A 269 ? 0.2916 0.3211 0.2801 0.0177  -0.0105 -0.0258 259 ASN A O   
2116 C CB  . ASN A 269 ? 0.2844 0.3023 0.2651 0.0235  -0.0156 -0.0282 259 ASN A CB  
2117 C CG  . ASN A 269 ? 0.2900 0.3052 0.2693 0.0234  -0.0164 -0.0274 259 ASN A CG  
2118 O OD1 . ASN A 269 ? 0.2979 0.3131 0.2796 0.0201  -0.0147 -0.0243 259 ASN A OD1 
2119 N ND2 . ASN A 269 ? 0.2922 0.3052 0.2677 0.0271  -0.0191 -0.0302 259 ASN A ND2 
2120 N N   . LYS A 270 ? 0.2796 0.2958 0.2642 0.0201  -0.0129 -0.0269 260 LYS A N   
2121 C CA  . LYS A 270 ? 0.2959 0.3166 0.2820 0.0198  -0.0120 -0.0280 260 LYS A CA  
2122 C C   . LYS A 270 ? 0.2801 0.2997 0.2697 0.0155  -0.0094 -0.0255 260 LYS A C   
2123 O O   . LYS A 270 ? 0.2838 0.3099 0.2761 0.0137  -0.0077 -0.0254 260 LYS A O   
2124 C CB  . LYS A 270 ? 0.3277 0.3439 0.3104 0.0230  -0.0142 -0.0302 260 LYS A CB  
2125 C CG  . LYS A 270 ? 0.3612 0.3830 0.3417 0.0276  -0.0162 -0.0339 260 LYS A CG  
2126 C CD  . LYS A 270 ? 0.3699 0.3867 0.3472 0.0306  -0.0185 -0.0356 260 LYS A CD  
2127 C CE  . LYS A 270 ? 0.3721 0.3921 0.3515 0.0290  -0.0170 -0.0356 260 LYS A CE  
2128 N NZ  . LYS A 270 ? 0.3816 0.3993 0.3578 0.0328  -0.0194 -0.0378 260 LYS A NZ  
2129 N N   . TYR A 271 ? 0.2567 0.2680 0.2461 0.0139  -0.0093 -0.0236 261 TYR A N   
2130 C CA  . TYR A 271 ? 0.2467 0.2560 0.2390 0.0106  -0.0073 -0.0219 261 TYR A CA  
2131 C C   . TYR A 271 ? 0.2431 0.2519 0.2386 0.0072  -0.0053 -0.0190 261 TYR A C   
2132 O O   . TYR A 271 ? 0.2363 0.2461 0.2349 0.0045  -0.0034 -0.0180 261 TYR A O   
2133 C CB  . TYR A 271 ? 0.2497 0.2513 0.2400 0.0109  -0.0084 -0.0221 261 TYR A CB  
2134 C CG  . TYR A 271 ? 0.2484 0.2505 0.2358 0.0140  -0.0102 -0.0247 261 TYR A CG  
2135 C CD1 . TYR A 271 ? 0.2544 0.2519 0.2373 0.0172  -0.0131 -0.0260 261 TYR A CD1 
2136 C CD2 . TYR A 271 ? 0.2479 0.2550 0.2368 0.0137  -0.0093 -0.0260 261 TYR A CD2 
2137 C CE1 . TYR A 271 ? 0.2640 0.2616 0.2441 0.0203  -0.0150 -0.0283 261 TYR A CE1 
2138 C CE2 . TYR A 271 ? 0.2517 0.2598 0.2381 0.0167  -0.0110 -0.0284 261 TYR A CE2 
2139 C CZ  . TYR A 271 ? 0.2609 0.2641 0.2429 0.0202  -0.0140 -0.0295 261 TYR A CZ  
2140 O OH  . TYR A 271 ? 0.2751 0.2789 0.2544 0.0235  -0.0160 -0.0317 261 TYR A OH  
2141 N N   . TRP A 272 ? 0.2339 0.2412 0.2288 0.0073  -0.0057 -0.0176 262 TRP A N   
2142 C CA  . TRP A 272 ? 0.2374 0.2441 0.2353 0.0044  -0.0040 -0.0146 262 TRP A CA  
2143 C C   . TRP A 272 ? 0.2375 0.2519 0.2377 0.0030  -0.0028 -0.0140 262 TRP A C   
2144 O O   . TRP A 272 ? 0.2377 0.2576 0.2364 0.0048  -0.0036 -0.0154 262 TRP A O   
2145 C CB  . TRP A 272 ? 0.2355 0.2383 0.2319 0.0048  -0.0049 -0.0133 262 TRP A CB  
2146 C CG  . TRP A 272 ? 0.2344 0.2361 0.2341 0.0020  -0.0032 -0.0103 262 TRP A CG  
2147 C CD1 . TRP A 272 ? 0.2364 0.2416 0.2377 0.0008  -0.0024 -0.0083 262 TRP A CD1 
2148 C CD2 . TRP A 272 ? 0.2269 0.2240 0.2285 0.0001  -0.0021 -0.0090 262 TRP A CD2 
2149 N NE1 . TRP A 272 ? 0.2379 0.2405 0.2421 -0.0014 -0.0010 -0.0057 262 TRP A NE1 
2150 C CE2 . TRP A 272 ? 0.2311 0.2288 0.2356 -0.0017 -0.0008 -0.0063 262 TRP A CE2 
2151 C CE3 . TRP A 272 ? 0.2242 0.2172 0.2254 0.0000  -0.0022 -0.0100 262 TRP A CE3 
2152 C CZ2 . TRP A 272 ? 0.2307 0.2248 0.2378 -0.0034 0.0002  -0.0049 262 TRP A CZ2 
2153 C CZ3 . TRP A 272 ? 0.2263 0.2164 0.2302 -0.0018 -0.0009 -0.0087 262 TRP A CZ3 
2154 C CH2 . TRP A 272 ? 0.2287 0.2193 0.2356 -0.0034 0.0002  -0.0063 262 TRP A CH2 
2155 N N   . PRO A 273 ? 0.2362 0.2513 0.2397 0.0000  -0.0009 -0.0120 263 PRO A N   
2156 C CA  . PRO A 273 ? 0.2322 0.2414 0.2379 -0.0021 0.0002  -0.0103 263 PRO A CA  
2157 C C   . PRO A 273 ? 0.2298 0.2372 0.2361 -0.0026 0.0007  -0.0118 263 PRO A C   
2158 O O   . PRO A 273 ? 0.2289 0.2408 0.2352 -0.0026 0.0009  -0.0135 263 PRO A O   
2159 C CB  . PRO A 273 ? 0.2359 0.2472 0.2446 -0.0050 0.0017  -0.0075 263 PRO A CB  
2160 C CG  . PRO A 273 ? 0.2356 0.2549 0.2440 -0.0053 0.0018  -0.0084 263 PRO A CG  
2161 C CD  . PRO A 273 ? 0.2394 0.2615 0.2447 -0.0019 0.0001  -0.0109 263 PRO A CD  
2162 N N   . ALA A 274 ? 0.2264 0.2278 0.2334 -0.0033 0.0010  -0.0112 264 ALA A N   
2163 C CA  . ALA A 274 ? 0.2246 0.2240 0.2323 -0.0040 0.0016  -0.0126 264 ALA A CA  
2164 C C   . ALA A 274 ? 0.2320 0.2346 0.2426 -0.0064 0.0032  -0.0125 264 ALA A C   
2165 O O   . ALA A 274 ? 0.2359 0.2390 0.2487 -0.0084 0.0041  -0.0104 264 ALA A O   
2166 C CB  . ALA A 274 ? 0.2281 0.2217 0.2367 -0.0046 0.0018  -0.0117 264 ALA A CB  
2167 N N   . ASP A 275 ? 0.2347 0.2394 0.2451 -0.0064 0.0033  -0.0147 265 ASP A N   
2168 C CA  . ASP A 275 ? 0.2433 0.2507 0.2562 -0.0090 0.0048  -0.0149 265 ASP A CA  
2169 C C   . ASP A 275 ? 0.2428 0.2449 0.2581 -0.0109 0.0059  -0.0144 265 ASP A C   
2170 O O   . ASP A 275 ? 0.2414 0.2432 0.2593 -0.0134 0.0071  -0.0133 265 ASP A O   
2171 C CB  . ASP A 275 ? 0.2506 0.2627 0.2623 -0.0082 0.0045  -0.0176 265 ASP A CB  
2172 C CG  . ASP A 275 ? 0.2608 0.2794 0.2705 -0.0064 0.0035  -0.0185 265 ASP A CG  
2173 O OD1 . ASP A 275 ? 0.2790 0.3032 0.2899 -0.0082 0.0043  -0.0181 265 ASP A OD1 
2174 O OD2 . ASP A 275 ? 0.2529 0.2706 0.2597 -0.0031 0.0018  -0.0194 265 ASP A OD2 
2175 N N   . ILE A 276 ? 0.2379 0.2361 0.2524 -0.0096 0.0054  -0.0152 266 ILE A N   
2176 C CA  . ILE A 276 ? 0.2426 0.2364 0.2595 -0.0110 0.0064  -0.0152 266 ILE A CA  
2177 C C   . ILE A 276 ? 0.2357 0.2254 0.2514 -0.0096 0.0055  -0.0147 266 ILE A C   
2178 O O   . ILE A 276 ? 0.2366 0.2262 0.2494 -0.0080 0.0043  -0.0158 266 ILE A O   
2179 C CB  . ILE A 276 ? 0.2476 0.2424 0.2651 -0.0119 0.0070  -0.0176 266 ILE A CB  
2180 C CG1 . ILE A 276 ? 0.2541 0.2532 0.2730 -0.0140 0.0080  -0.0181 266 ILE A CG1 
2181 C CG2 . ILE A 276 ? 0.2566 0.2472 0.2765 -0.0129 0.0078  -0.0178 266 ILE A CG2 
2182 C CD1 . ILE A 276 ? 0.2595 0.2602 0.2791 -0.0151 0.0086  -0.0206 266 ILE A CD1 
2183 N N   . HIS A 277 ? 0.2320 0.2184 0.2497 -0.0102 0.0061  -0.0131 267 HIS A N   
2184 C CA  . HIS A 277 ? 0.2320 0.2152 0.2494 -0.0096 0.0058  -0.0130 267 HIS A CA  
2185 C C   . HIS A 277 ? 0.2387 0.2205 0.2587 -0.0108 0.0069  -0.0144 267 HIS A C   
2186 O O   . HIS A 277 ? 0.2439 0.2246 0.2669 -0.0120 0.0079  -0.0140 267 HIS A O   
2187 C CB  . HIS A 277 ? 0.2269 0.2081 0.2451 -0.0093 0.0056  -0.0106 267 HIS A CB  
2188 C CG  . HIS A 277 ? 0.2268 0.2092 0.2425 -0.0081 0.0045  -0.0093 267 HIS A CG  
2189 N ND1 . HIS A 277 ? 0.2172 0.1997 0.2293 -0.0067 0.0031  -0.0101 267 HIS A ND1 
2190 C CD2 . HIS A 277 ? 0.2227 0.2060 0.2389 -0.0081 0.0045  -0.0072 267 HIS A CD2 
2191 C CE1 . HIS A 277 ? 0.2205 0.2039 0.2311 -0.0058 0.0022  -0.0089 267 HIS A CE1 
2192 N NE2 . HIS A 277 ? 0.2248 0.2092 0.2378 -0.0067 0.0031  -0.0071 267 HIS A NE2 
2193 N N   . LEU A 278 ? 0.2381 0.2199 0.2570 -0.0106 0.0066  -0.0162 268 LEU A N   
2194 C CA  . LEU A 278 ? 0.2516 0.2329 0.2728 -0.0116 0.0076  -0.0179 268 LEU A CA  
2195 C C   . LEU A 278 ? 0.2429 0.2224 0.2648 -0.0113 0.0076  -0.0176 268 LEU A C   
2196 O O   . LEU A 278 ? 0.2365 0.2155 0.2560 -0.0105 0.0065  -0.0166 268 LEU A O   
2197 C CB  . LEU A 278 ? 0.2680 0.2516 0.2874 -0.0117 0.0073  -0.0201 268 LEU A CB  
2198 C CG  . LEU A 278 ? 0.2874 0.2716 0.3087 -0.0129 0.0083  -0.0224 268 LEU A CG  
2199 C CD1 . LEU A 278 ? 0.3034 0.2908 0.3239 -0.0134 0.0085  -0.0243 268 LEU A CD1 
2200 C CD2 . LEU A 278 ? 0.2922 0.2760 0.3123 -0.0126 0.0077  -0.0228 268 LEU A CD2 
2201 N N   . MET A 279 ? 0.2380 0.2165 0.2632 -0.0119 0.0086  -0.0186 269 MET A N   
2202 C CA  . MET A 279 ? 0.2465 0.2243 0.2728 -0.0114 0.0087  -0.0188 269 MET A CA  
2203 C C   . MET A 279 ? 0.2561 0.2335 0.2860 -0.0119 0.0098  -0.0209 269 MET A C   
2204 O O   . MET A 279 ? 0.2657 0.2423 0.2972 -0.0127 0.0105  -0.0217 269 MET A O   
2205 C CB  . MET A 279 ? 0.2440 0.2201 0.2708 -0.0105 0.0083  -0.0163 269 MET A CB  
2206 C CG  . MET A 279 ? 0.2535 0.2275 0.2832 -0.0106 0.0090  -0.0152 269 MET A CG  
2207 S SD  . MET A 279 ? 0.2627 0.2358 0.2917 -0.0099 0.0083  -0.0116 269 MET A SD  
2208 C CE  . MET A 279 ? 0.2583 0.2338 0.2835 -0.0102 0.0076  -0.0114 269 MET A CE  
2209 N N   . ALA A 280 ? 0.2675 0.2454 0.2986 -0.0113 0.0100  -0.0218 270 ALA A N   
2210 C CA  . ALA A 280 ? 0.2786 0.2555 0.3135 -0.0111 0.0109  -0.0237 270 ALA A CA  
2211 C C   . ALA A 280 ? 0.2922 0.2659 0.3294 -0.0099 0.0108  -0.0219 270 ALA A C   
2212 O O   . ALA A 280 ? 0.2870 0.2601 0.3230 -0.0093 0.0102  -0.0192 270 ALA A O   
2213 C CB  . ALA A 280 ? 0.2824 0.2623 0.3179 -0.0109 0.0110  -0.0259 270 ALA A CB  
2214 N N   . LYS A 281 ? 0.3089 0.2802 0.3493 -0.0096 0.0114  -0.0235 271 LYS A N   
2215 C CA  . LYS A 281 ? 0.3389 0.3060 0.3814 -0.0087 0.0112  -0.0217 271 LYS A CA  
2216 C C   . LYS A 281 ? 0.3378 0.3050 0.3807 -0.0067 0.0106  -0.0197 271 LYS A C   
2217 O O   . LYS A 281 ? 0.3467 0.3110 0.3901 -0.0062 0.0101  -0.0170 271 LYS A O   
2218 C CB  . LYS A 281 ? 0.3582 0.3223 0.4040 -0.0085 0.0117  -0.0243 271 LYS A CB  
2219 C CG  . LYS A 281 ? 0.3701 0.3364 0.4178 -0.0071 0.0120  -0.0276 271 LYS A CG  
2220 C CD  . LYS A 281 ? 0.3929 0.3558 0.4435 -0.0070 0.0124  -0.0305 271 LYS A CD  
2221 C CE  . LYS A 281 ? 0.4087 0.3757 0.4608 -0.0063 0.0129  -0.0347 271 LYS A CE  
2222 N NZ  . LYS A 281 ? 0.4224 0.3855 0.4776 -0.0056 0.0131  -0.0378 271 LYS A NZ  
2223 N N   A GLU A 282 ? 0.3446 0.3156 0.3871 -0.0059 0.0105  -0.0208 272 GLU A N   
2224 N N   B GLU A 282 ? 0.3428 0.3138 0.3853 -0.0059 0.0105  -0.0208 272 GLU A N   
2225 C CA  A GLU A 282 ? 0.3491 0.3211 0.3923 -0.0040 0.0099  -0.0194 272 GLU A CA  
2226 C CA  B GLU A 282 ? 0.3461 0.3181 0.3893 -0.0040 0.0099  -0.0194 272 GLU A CA  
2227 C C   A GLU A 282 ? 0.3388 0.3111 0.3794 -0.0042 0.0092  -0.0158 272 GLU A C   
2228 C C   B GLU A 282 ? 0.3372 0.3094 0.3778 -0.0042 0.0092  -0.0158 272 GLU A C   
2229 O O   A GLU A 282 ? 0.3433 0.3157 0.3846 -0.0027 0.0087  -0.0142 272 GLU A O   
2230 O O   B GLU A 282 ? 0.3419 0.3143 0.3833 -0.0027 0.0087  -0.0142 272 GLU A O   
2231 C CB  A GLU A 282 ? 0.3619 0.3387 0.4055 -0.0034 0.0100  -0.0218 272 GLU A CB  
2232 C CB  B GLU A 282 ? 0.3560 0.3330 0.3995 -0.0035 0.0100  -0.0219 272 GLU A CB  
2233 C CG  A GLU A 282 ? 0.3724 0.3533 0.4123 -0.0050 0.0098  -0.0215 272 GLU A CG  
2234 C CG  B GLU A 282 ? 0.3640 0.3449 0.4037 -0.0050 0.0097  -0.0213 272 GLU A CG  
2235 C CD  A GLU A 282 ? 0.3878 0.3692 0.4259 -0.0069 0.0101  -0.0230 272 GLU A CD  
2236 C CD  B GLU A 282 ? 0.3771 0.3581 0.4146 -0.0070 0.0099  -0.0222 272 GLU A CD  
2237 O OE1 A GLU A 282 ? 0.4000 0.3832 0.4345 -0.0083 0.0095  -0.0221 272 GLU A OE1 
2238 O OE1 B GLU A 282 ? 0.3884 0.3684 0.4276 -0.0074 0.0106  -0.0245 272 GLU A OE1 
2239 O OE2 A GLU A 282 ? 0.3947 0.3743 0.4347 -0.0071 0.0107  -0.0249 272 GLU A OE2 
2240 O OE2 B GLU A 282 ? 0.3679 0.3497 0.4017 -0.0082 0.0092  -0.0207 272 GLU A OE2 
2241 N N   . ILE A 283 ? 0.3223 0.2948 0.3599 -0.0058 0.0090  -0.0149 273 ILE A N   
2242 C CA  . ILE A 283 ? 0.3077 0.2805 0.3428 -0.0059 0.0083  -0.0119 273 ILE A CA  
2243 C C   . ILE A 283 ? 0.2970 0.2674 0.3318 -0.0066 0.0083  -0.0100 273 ILE A C   
2244 O O   . ILE A 283 ? 0.2779 0.2490 0.3105 -0.0067 0.0077  -0.0078 273 ILE A O   
2245 C CB  . ILE A 283 ? 0.2968 0.2724 0.3281 -0.0068 0.0077  -0.0120 273 ILE A CB  
2246 C CG1 . ILE A 283 ? 0.2930 0.2689 0.3225 -0.0081 0.0078  -0.0136 273 ILE A CG1 
2247 C CG2 . ILE A 283 ? 0.3022 0.2807 0.3337 -0.0065 0.0076  -0.0133 273 ILE A CG2 
2248 C CD1 . ILE A 283 ? 0.2833 0.2609 0.3087 -0.0089 0.0069  -0.0136 273 ILE A CD1 
2249 N N   . VAL A 284 ? 0.3019 0.2696 0.3389 -0.0070 0.0088  -0.0107 274 VAL A N   
2250 C CA  . VAL A 284 ? 0.3140 0.2797 0.3509 -0.0081 0.0088  -0.0086 274 VAL A CA  
2251 C C   . VAL A 284 ? 0.3125 0.2771 0.3496 -0.0073 0.0082  -0.0053 274 VAL A C   
2252 O O   . VAL A 284 ? 0.2915 0.2570 0.3269 -0.0081 0.0079  -0.0032 274 VAL A O   
2253 C CB  . VAL A 284 ? 0.3401 0.3025 0.3794 -0.0091 0.0094  -0.0098 274 VAL A CB  
2254 C CG1 . VAL A 284 ? 0.3520 0.3126 0.3910 -0.0106 0.0092  -0.0072 274 VAL A CG1 
2255 C CG2 . VAL A 284 ? 0.3505 0.3146 0.3892 -0.0103 0.0100  -0.0129 274 VAL A CG2 
2256 N N   . ARG A 285 ? 0.3226 0.2859 0.3618 -0.0055 0.0080  -0.0049 275 ARG A N   
2257 C CA  . ARG A 285 ? 0.3518 0.3143 0.3914 -0.0045 0.0073  -0.0017 275 ARG A CA  
2258 C C   . ARG A 285 ? 0.3277 0.2938 0.3645 -0.0046 0.0068  0.0000  275 ARG A C   
2259 O O   . ARG A 285 ? 0.3259 0.2921 0.3619 -0.0050 0.0064  0.0027  275 ARG A O   
2260 C CB  . ARG A 285 ? 0.3941 0.3553 0.4364 -0.0022 0.0070  -0.0019 275 ARG A CB  
2261 C CG  . ARG A 285 ? 0.4295 0.3946 0.4717 -0.0010 0.0071  -0.0040 275 ARG A CG  
2262 C CD  . ARG A 285 ? 0.4767 0.4412 0.5219 0.0015  0.0068  -0.0049 275 ARG A CD  
2263 N NE  . ARG A 285 ? 0.5080 0.4727 0.5536 0.0031  0.0060  -0.0019 275 ARG A NE  
2264 C CZ  . ARG A 285 ? 0.5412 0.5069 0.5889 0.0057  0.0055  -0.0021 275 ARG A CZ  
2265 N NH1 . ARG A 285 ? 0.5531 0.5193 0.6009 0.0070  0.0048  0.0008  275 ARG A NH1 
2266 N NH2 . ARG A 285 ? 0.5546 0.5213 0.6044 0.0072  0.0058  -0.0055 275 ARG A NH2 
2267 N N   . PHE A 286 ? 0.3024 0.2714 0.3374 -0.0045 0.0068  -0.0017 276 PHE A N   
2268 C CA  . PHE A 286 ? 0.2934 0.2652 0.3254 -0.0046 0.0061  -0.0004 276 PHE A CA  
2269 C C   . PHE A 286 ? 0.2749 0.2473 0.3044 -0.0059 0.0060  0.0000  276 PHE A C   
2270 O O   . PHE A 286 ? 0.2831 0.2569 0.3109 -0.0059 0.0054  0.0020  276 PHE A O   
2271 C CB  . PHE A 286 ? 0.3024 0.2765 0.3329 -0.0045 0.0059  -0.0022 276 PHE A CB  
2272 C CG  . PHE A 286 ? 0.3148 0.2896 0.3479 -0.0033 0.0062  -0.0033 276 PHE A CG  
2273 C CD1 . PHE A 286 ? 0.3298 0.3044 0.3651 -0.0017 0.0060  -0.0015 276 PHE A CD1 
2274 C CD2 . PHE A 286 ? 0.3262 0.3024 0.3596 -0.0035 0.0066  -0.0061 276 PHE A CD2 
2275 C CE1 . PHE A 286 ? 0.3317 0.3075 0.3696 -0.0001 0.0061  -0.0028 276 PHE A CE1 
2276 C CE2 . PHE A 286 ? 0.3327 0.3105 0.3686 -0.0022 0.0068  -0.0074 276 PHE A CE2 
2277 C CZ  . PHE A 286 ? 0.3342 0.3118 0.3724 -0.0003 0.0065  -0.0059 276 PHE A CZ  
2278 N N   . HIS A 287 ? 0.2647 0.2366 0.2942 -0.0069 0.0065  -0.0018 277 HIS A N   
2279 C CA  . HIS A 287 ? 0.2659 0.2391 0.2933 -0.0079 0.0063  -0.0017 277 HIS A CA  
2280 C C   . HIS A 287 ? 0.2660 0.2388 0.2944 -0.0088 0.0066  0.0002  277 HIS A C   
2281 O O   . HIS A 287 ? 0.2645 0.2397 0.2911 -0.0094 0.0063  0.0007  277 HIS A O   
2282 C CB  . HIS A 287 ? 0.2599 0.2334 0.2867 -0.0086 0.0067  -0.0045 277 HIS A CB  
2283 C CG  . HIS A 287 ? 0.2519 0.2265 0.2762 -0.0081 0.0062  -0.0061 277 HIS A CG  
2284 N ND1 . HIS A 287 ? 0.2534 0.2277 0.2784 -0.0078 0.0063  -0.0071 277 HIS A ND1 
2285 C CD2 . HIS A 287 ? 0.2551 0.2310 0.2759 -0.0080 0.0053  -0.0066 277 HIS A CD2 
2286 C CE1 . HIS A 287 ? 0.2523 0.2276 0.2743 -0.0079 0.0055  -0.0080 277 HIS A CE1 
2287 N NE2 . HIS A 287 ? 0.2471 0.2229 0.2665 -0.0079 0.0048  -0.0077 277 HIS A NE2 
2288 N N   . SER A 288 ? 0.2725 0.2424 0.3038 -0.0090 0.0069  0.0011  278 SER A N   
2289 C CA  . SER A 288 ? 0.2862 0.2551 0.3183 -0.0104 0.0071  0.0032  278 SER A CA  
2290 C C   . SER A 288 ? 0.2841 0.2524 0.3167 -0.0099 0.0065  0.0067  278 SER A C   
2291 O O   . SER A 288 ? 0.2869 0.2553 0.3196 -0.0113 0.0064  0.0090  278 SER A O   
2292 C CB  . SER A 288 ? 0.3001 0.2652 0.3345 -0.0114 0.0077  0.0020  278 SER A CB  
2293 O OG  . SER A 288 ? 0.3318 0.2932 0.3687 -0.0100 0.0075  0.0021  278 SER A OG  
2294 N N   . ILE A 289 ? 0.2787 0.2471 0.3117 -0.0080 0.0060  0.0072  279 ILE A N   
2295 C CA  . ILE A 289 ? 0.2785 0.2472 0.3119 -0.0072 0.0054  0.0104  279 ILE A CA  
2296 C C   . ILE A 289 ? 0.2737 0.2464 0.3047 -0.0064 0.0049  0.0108  279 ILE A C   
2297 O O   . ILE A 289 ? 0.2831 0.2584 0.3125 -0.0070 0.0045  0.0127  279 ILE A O   
2298 C CB  . ILE A 289 ? 0.2870 0.2522 0.3231 -0.0055 0.0052  0.0109  279 ILE A CB  
2299 C CG1 . ILE A 289 ? 0.2962 0.2565 0.3345 -0.0064 0.0054  0.0106  279 ILE A CG1 
2300 C CG2 . ILE A 289 ? 0.2892 0.2553 0.3256 -0.0044 0.0044  0.0143  279 ILE A CG2 
2301 C CD1 . ILE A 289 ? 0.3026 0.2590 0.3436 -0.0043 0.0052  0.0098  279 ILE A CD1 
2302 N N   . ILE A 290 ? 0.2643 0.2377 0.2948 -0.0052 0.0048  0.0090  280 ILE A N   
2303 C CA  . ILE A 290 ? 0.2542 0.2308 0.2823 -0.0047 0.0042  0.0094  280 ILE A CA  
2304 C C   . ILE A 290 ? 0.2410 0.2197 0.2660 -0.0056 0.0039  0.0087  280 ILE A C   
2305 O O   . ILE A 290 ? 0.2369 0.2181 0.2601 -0.0055 0.0033  0.0101  280 ILE A O   
2306 C CB  . ILE A 290 ? 0.2606 0.2376 0.2884 -0.0039 0.0041  0.0075  280 ILE A CB  
2307 C CG1 . ILE A 290 ? 0.2670 0.2431 0.2981 -0.0025 0.0042  0.0080  280 ILE A CG1 
2308 C CG2 . ILE A 290 ? 0.2550 0.2348 0.2799 -0.0039 0.0033  0.0079  280 ILE A CG2 
2309 C CD1 . ILE A 290 ? 0.2754 0.2528 0.3066 -0.0019 0.0043  0.0058  280 ILE A CD1 
2310 N N   . TRP A 291 ? 0.2291 0.2071 0.2533 -0.0062 0.0042  0.0063  281 TRP A N   
2311 C CA  . TRP A 291 ? 0.2287 0.2087 0.2498 -0.0065 0.0037  0.0051  281 TRP A CA  
2312 C C   . TRP A 291 ? 0.2347 0.2173 0.2555 -0.0071 0.0037  0.0067  281 TRP A C   
2313 O O   . TRP A 291 ? 0.2375 0.2227 0.2559 -0.0067 0.0029  0.0070  281 TRP A O   
2314 C CB  . TRP A 291 ? 0.2203 0.1992 0.2410 -0.0068 0.0041  0.0023  281 TRP A CB  
2315 C CG  . TRP A 291 ? 0.2102 0.1908 0.2277 -0.0067 0.0034  0.0006  281 TRP A CG  
2316 C CD1 . TRP A 291 ? 0.2179 0.1990 0.2352 -0.0072 0.0038  -0.0011 281 TRP A CD1 
2317 C CD2 . TRP A 291 ? 0.2111 0.1928 0.2251 -0.0059 0.0022  0.0003  281 TRP A CD2 
2318 N NE1 . TRP A 291 ? 0.2155 0.1982 0.2296 -0.0064 0.0028  -0.0024 281 TRP A NE1 
2319 C CE2 . TRP A 291 ? 0.2039 0.1865 0.2157 -0.0055 0.0017  -0.0017 281 TRP A CE2 
2320 C CE3 . TRP A 291 ? 0.2062 0.1881 0.2186 -0.0053 0.0013  0.0013  281 TRP A CE3 
2321 C CZ2 . TRP A 291 ? 0.2030 0.1861 0.2111 -0.0044 0.0003  -0.0027 281 TRP A CZ2 
2322 C CZ3 . TRP A 291 ? 0.2051 0.1875 0.2137 -0.0046 0.0000  0.0003  281 TRP A CZ3 
2323 C CH2 . TRP A 291 ? 0.2037 0.1864 0.2102 -0.0040 -0.0005 -0.0016 281 TRP A CH2 
2324 N N   . PRO A 292 ? 0.2497 0.2316 0.2726 -0.0083 0.0044  0.0077  282 PRO A N   
2325 C CA  . PRO A 292 ? 0.2561 0.2413 0.2785 -0.0093 0.0043  0.0096  282 PRO A CA  
2326 C C   . PRO A 292 ? 0.2523 0.2393 0.2744 -0.0088 0.0037  0.0123  282 PRO A C   
2327 O O   . PRO A 292 ? 0.2466 0.2378 0.2670 -0.0090 0.0033  0.0129  282 PRO A O   
2328 C CB  . PRO A 292 ? 0.2663 0.2496 0.2910 -0.0111 0.0050  0.0106  282 PRO A CB  
2329 C CG  . PRO A 292 ? 0.2753 0.2540 0.3021 -0.0106 0.0055  0.0093  282 PRO A CG  
2330 C CD  . PRO A 292 ? 0.2560 0.2346 0.2815 -0.0090 0.0052  0.0070  282 PRO A CD  
2331 N N   . ILE A 293 ? 0.2475 0.2320 0.2712 -0.0080 0.0036  0.0138  283 ILE A N   
2332 C CA  . ILE A 293 ? 0.2517 0.2384 0.2753 -0.0075 0.0031  0.0164  283 ILE A CA  
2333 C C   . ILE A 293 ? 0.2464 0.2360 0.2670 -0.0066 0.0023  0.0152  283 ILE A C   
2334 O O   . ILE A 293 ? 0.2343 0.2277 0.2536 -0.0067 0.0019  0.0165  283 ILE A O   
2335 C CB  . ILE A 293 ? 0.2568 0.2405 0.2829 -0.0066 0.0031  0.0181  283 ILE A CB  
2336 C CG1 . ILE A 293 ? 0.2672 0.2479 0.2957 -0.0076 0.0034  0.0201  283 ILE A CG1 
2337 C CG2 . ILE A 293 ? 0.2590 0.2455 0.2846 -0.0058 0.0024  0.0204  283 ILE A CG2 
2338 C CD1 . ILE A 293 ? 0.2731 0.2499 0.3042 -0.0063 0.0032  0.0213  283 ILE A CD1 
2339 N N   . LEU A 294 ? 0.2448 0.2327 0.2642 -0.0059 0.0022  0.0127  284 LEU A N   
2340 C CA  . LEU A 294 ? 0.2395 0.2290 0.2557 -0.0053 0.0013  0.0112  284 LEU A CA  
2341 C C   . LEU A 294 ? 0.2405 0.2328 0.2543 -0.0053 0.0008  0.0102  284 LEU A C   
2342 O O   . LEU A 294 ? 0.2397 0.2347 0.2514 -0.0049 0.0000  0.0103  284 LEU A O   
2343 C CB  . LEU A 294 ? 0.2403 0.2269 0.2554 -0.0050 0.0011  0.0088  284 LEU A CB  
2344 C CG  . LEU A 294 ? 0.2478 0.2345 0.2589 -0.0047 0.0000  0.0073  284 LEU A CG  
2345 C CD1 . LEU A 294 ? 0.2498 0.2386 0.2601 -0.0046 -0.0007 0.0089  284 LEU A CD1 
2346 C CD2 . LEU A 294 ? 0.2552 0.2391 0.2655 -0.0049 -0.0002 0.0055  284 LEU A CD2 
2347 N N   . LEU A 295 ? 0.2427 0.2350 0.2571 -0.0058 0.0013  0.0090  285 LEU A N   
2348 C CA  . LEU A 295 ? 0.2437 0.2396 0.2561 -0.0057 0.0009  0.0077  285 LEU A CA  
2349 C C   . LEU A 295 ? 0.2502 0.2509 0.2631 -0.0064 0.0010  0.0100  285 LEU A C   
2350 O O   . LEU A 295 ? 0.2514 0.2562 0.2621 -0.0057 0.0002  0.0092  285 LEU A O   
2351 C CB  . LEU A 295 ? 0.2406 0.2359 0.2538 -0.0063 0.0016  0.0060  285 LEU A CB  
2352 C CG  . LEU A 295 ? 0.2366 0.2285 0.2485 -0.0055 0.0013  0.0033  285 LEU A CG  
2353 C CD1 . LEU A 295 ? 0.2423 0.2336 0.2557 -0.0064 0.0022  0.0022  285 LEU A CD1 
2354 C CD2 . LEU A 295 ? 0.2396 0.2324 0.2477 -0.0039 0.0000  0.0011  285 LEU A CD2 
2355 N N   . MET A 296 ? 0.2578 0.2580 0.2734 -0.0077 0.0017  0.0129  286 MET A N   
2356 C CA  . MET A 296 ? 0.2763 0.2809 0.2922 -0.0086 0.0017  0.0157  286 MET A CA  
2357 C C   . MET A 296 ? 0.2708 0.2777 0.2852 -0.0076 0.0008  0.0164  286 MET A C   
2358 O O   . MET A 296 ? 0.2666 0.2788 0.2795 -0.0076 0.0004  0.0166  286 MET A O   
2359 C CB  . MET A 296 ? 0.2970 0.2991 0.3157 -0.0101 0.0023  0.0190  286 MET A CB  
2360 C CG  . MET A 296 ? 0.3234 0.3245 0.3434 -0.0119 0.0030  0.0188  286 MET A CG  
2361 S SD  . MET A 296 ? 0.3679 0.3642 0.3909 -0.0133 0.0033  0.0226  286 MET A SD  
2362 C CE  . MET A 296 ? 0.3738 0.3695 0.3975 -0.0159 0.0040  0.0219  286 MET A CE  
2363 N N   . ALA A 297 ? 0.2780 0.2815 0.2926 -0.0067 0.0006  0.0164  287 ALA A N   
2364 C CA  . ALA A 297 ? 0.2802 0.2856 0.2932 -0.0059 -0.0001 0.0169  287 ALA A CA  
2365 C C   . ALA A 297 ? 0.2801 0.2875 0.2896 -0.0049 -0.0011 0.0140  287 ALA A C   
2366 O O   . ALA A 297 ? 0.2846 0.2954 0.2925 -0.0046 -0.0018 0.0142  287 ALA A O   
2367 C CB  . ALA A 297 ? 0.2831 0.2850 0.2971 -0.0053 -0.0001 0.0173  287 ALA A CB  
2368 N N   . LEU A 298 ? 0.2750 0.2803 0.2833 -0.0044 -0.0012 0.0111  288 LEU A N   
2369 C CA  . LEU A 298 ? 0.2843 0.2906 0.2892 -0.0031 -0.0024 0.0080  288 LEU A CA  
2370 C C   . LEU A 298 ? 0.2842 0.2959 0.2886 -0.0029 -0.0024 0.0070  288 LEU A C   
2371 O O   . LEU A 298 ? 0.2845 0.2973 0.2860 -0.0013 -0.0035 0.0042  288 LEU A O   
2372 C CB  . LEU A 298 ? 0.2949 0.2959 0.2983 -0.0024 -0.0028 0.0055  288 LEU A CB  
2373 C CG  . LEU A 298 ? 0.2987 0.2954 0.3018 -0.0028 -0.0030 0.0059  288 LEU A CG  
2374 C CD1 . LEU A 298 ? 0.2973 0.2893 0.2995 -0.0026 -0.0032 0.0038  288 LEU A CD1 
2375 C CD2 . LEU A 298 ? 0.3088 0.3059 0.3090 -0.0023 -0.0043 0.0056  288 LEU A CD2 
2376 N N   . ASP A 299 ? 0.2891 0.3040 0.2959 -0.0044 -0.0013 0.0093  289 ASP A N   
2377 C CA  . ASP A 299 ? 0.2971 0.3182 0.3038 -0.0048 -0.0012 0.0087  289 ASP A CA  
2378 C C   . ASP A 299 ? 0.2875 0.3080 0.2930 -0.0037 -0.0014 0.0053  289 ASP A C   
2379 O O   . ASP A 299 ? 0.2846 0.3098 0.2881 -0.0024 -0.0021 0.0029  289 ASP A O   
2380 C CB  . ASP A 299 ? 0.3168 0.3442 0.3216 -0.0040 -0.0020 0.0084  289 ASP A CB  
2381 C CG  . ASP A 299 ? 0.3363 0.3718 0.3414 -0.0050 -0.0017 0.0086  289 ASP A CG  
2382 O OD1 . ASP A 299 ? 0.3440 0.3805 0.3512 -0.0070 -0.0006 0.0103  289 ASP A OD1 
2383 O OD2 . ASP A 299 ? 0.3682 0.4096 0.3715 -0.0037 -0.0025 0.0068  289 ASP A OD2 
2384 N N   . LEU A 300 ? 0.2736 0.2885 0.2801 -0.0040 -0.0009 0.0049  290 LEU A N   
2385 C CA  . LEU A 300 ? 0.2766 0.2904 0.2822 -0.0031 -0.0010 0.0019  290 LEU A CA  
2386 C C   . LEU A 300 ? 0.2735 0.2878 0.2817 -0.0052 0.0002  0.0028  290 LEU A C   
2387 O O   . LEU A 300 ? 0.2692 0.2810 0.2799 -0.0070 0.0012  0.0055  290 LEU A O   
2388 C CB  . LEU A 300 ? 0.2798 0.2868 0.2840 -0.0020 -0.0017 0.0004  290 LEU A CB  
2389 C CG  . LEU A 300 ? 0.2887 0.2938 0.2896 -0.0002 -0.0033 -0.0009 290 LEU A CG  
2390 C CD1 . LEU A 300 ? 0.2865 0.2849 0.2862 0.0000  -0.0039 -0.0018 290 LEU A CD1 
2391 C CD2 . LEU A 300 ? 0.2987 0.3075 0.2967 0.0019  -0.0047 -0.0037 290 LEU A CD2 
2392 N N   . PRO A 301 ? 0.2789 0.2962 0.2865 -0.0047 0.0002  0.0004  291 PRO A N   
2393 C CA  . PRO A 301 ? 0.2856 0.3030 0.2953 -0.0069 0.0015  0.0008  291 PRO A CA  
2394 C C   . PRO A 301 ? 0.2797 0.2898 0.2909 -0.0074 0.0021  0.0011  291 PRO A C   
2395 O O   . PRO A 301 ? 0.2790 0.2848 0.2889 -0.0058 0.0014  -0.0002 291 PRO A O   
2396 C CB  . PRO A 301 ? 0.2975 0.3191 0.3056 -0.0055 0.0010  -0.0025 291 PRO A CB  
2397 C CG  . PRO A 301 ? 0.3037 0.3290 0.3090 -0.0029 -0.0003 -0.0042 291 PRO A CG  
2398 C CD  . PRO A 301 ? 0.2883 0.3089 0.2929 -0.0022 -0.0010 -0.0029 291 PRO A CD  
2399 N N   . LEU A 302 ? 0.2768 0.2858 0.2907 -0.0099 0.0033  0.0027  292 LEU A N   
2400 C CA  . LEU A 302 ? 0.2816 0.2843 0.2973 -0.0105 0.0039  0.0028  292 LEU A CA  
2401 C C   . LEU A 302 ? 0.2717 0.2743 0.2873 -0.0106 0.0043  0.0000  292 LEU A C   
2402 O O   . LEU A 302 ? 0.2664 0.2742 0.2814 -0.0111 0.0044  -0.0011 292 LEU A O   
2403 C CB  . LEU A 302 ? 0.2916 0.2922 0.3101 -0.0128 0.0048  0.0059  292 LEU A CB  
2404 C CG  . LEU A 302 ? 0.3058 0.3037 0.3250 -0.0123 0.0044  0.0086  292 LEU A CG  
2405 C CD1 . LEU A 302 ? 0.3067 0.3088 0.3239 -0.0111 0.0036  0.0092  292 LEU A CD1 
2406 C CD2 . LEU A 302 ? 0.3177 0.3138 0.3393 -0.0145 0.0050  0.0118  292 LEU A CD2 
2407 N N   . PRO A 303 ? 0.2745 0.2720 0.2908 -0.0101 0.0045  -0.0010 293 PRO A N   
2408 C CA  . PRO A 303 ? 0.2742 0.2717 0.2905 -0.0104 0.0049  -0.0035 293 PRO A CA  
2409 C C   . PRO A 303 ? 0.2868 0.2856 0.3053 -0.0132 0.0060  -0.0030 293 PRO A C   
2410 O O   . PRO A 303 ? 0.2948 0.2920 0.3152 -0.0150 0.0065  -0.0004 293 PRO A O   
2411 C CB  . PRO A 303 ? 0.2807 0.2727 0.2976 -0.0098 0.0049  -0.0043 293 PRO A CB  
2412 C CG  . PRO A 303 ? 0.2783 0.2673 0.2965 -0.0098 0.0049  -0.0018 293 PRO A CG  
2413 C CD  . PRO A 303 ? 0.2759 0.2682 0.2933 -0.0097 0.0045  0.0001  293 PRO A CD  
2414 N N   . LYS A 304 ? 0.2920 0.2937 0.3101 -0.0136 0.0063  -0.0053 294 LYS A N   
2415 C CA  . LYS A 304 ? 0.3052 0.3090 0.3250 -0.0166 0.0073  -0.0051 294 LYS A CA  
2416 C C   . LYS A 304 ? 0.3026 0.3007 0.3248 -0.0182 0.0082  -0.0052 294 LYS A C   
2417 O O   . LYS A 304 ? 0.2956 0.2929 0.3195 -0.0211 0.0089  -0.0037 294 LYS A O   
2418 C CB  . LYS A 304 ? 0.3170 0.3271 0.3353 -0.0163 0.0072  -0.0077 294 LYS A CB  
2419 C CG  . LYS A 304 ? 0.3392 0.3558 0.3554 -0.0149 0.0063  -0.0078 294 LYS A CG  
2420 C CD  . LYS A 304 ? 0.3571 0.3812 0.3722 -0.0146 0.0062  -0.0104 294 LYS A CD  
2421 C CE  . LYS A 304 ? 0.3690 0.4005 0.3824 -0.0136 0.0055  -0.0103 294 LYS A CE  
2422 N NZ  . LYS A 304 ? 0.3820 0.4217 0.3943 -0.0129 0.0053  -0.0131 294 LYS A NZ  
2423 N N   . LYS A 305 ? 0.2978 0.2922 0.3201 -0.0166 0.0081  -0.0068 295 LYS A N   
2424 C CA  . LYS A 305 ? 0.3064 0.2963 0.3310 -0.0178 0.0089  -0.0077 295 LYS A CA  
2425 C C   . LYS A 305 ? 0.2990 0.2848 0.3237 -0.0157 0.0086  -0.0085 295 LYS A C   
2426 O O   . LYS A 305 ? 0.2768 0.2638 0.2994 -0.0139 0.0079  -0.0098 295 LYS A O   
2427 C CB  . LYS A 305 ? 0.3237 0.3163 0.3483 -0.0191 0.0095  -0.0103 295 LYS A CB  
2428 C CG  . LYS A 305 ? 0.3527 0.3412 0.3797 -0.0206 0.0104  -0.0115 295 LYS A CG  
2429 C CD  . LYS A 305 ? 0.3786 0.3704 0.4055 -0.0219 0.0110  -0.0143 295 LYS A CD  
2430 C CE  . LYS A 305 ? 0.4126 0.4093 0.4393 -0.0246 0.0114  -0.0139 295 LYS A CE  
2431 N NZ  . LYS A 305 ? 0.4473 0.4406 0.4758 -0.0277 0.0119  -0.0117 295 LYS A NZ  
2432 N N   . VAL A 306 ? 0.2947 0.2758 0.3217 -0.0162 0.0091  -0.0077 296 VAL A N   
2433 C CA  . VAL A 306 ? 0.3111 0.2892 0.3389 -0.0149 0.0091  -0.0090 296 VAL A CA  
2434 C C   . VAL A 306 ? 0.3140 0.2909 0.3435 -0.0162 0.0100  -0.0114 296 VAL A C   
2435 O O   . VAL A 306 ? 0.3176 0.2922 0.3492 -0.0179 0.0105  -0.0110 296 VAL A O   
2436 C CB  . VAL A 306 ? 0.3255 0.3000 0.3549 -0.0141 0.0089  -0.0069 296 VAL A CB  
2437 C CG1 . VAL A 306 ? 0.3355 0.3076 0.3663 -0.0130 0.0091  -0.0085 296 VAL A CG1 
2438 C CG2 . VAL A 306 ? 0.3325 0.3087 0.3599 -0.0128 0.0080  -0.0048 296 VAL A CG2 
2439 N N   . PHE A 307 ? 0.3180 0.2964 0.3465 -0.0155 0.0100  -0.0140 297 PHE A N   
2440 C CA  . PHE A 307 ? 0.3237 0.3017 0.3538 -0.0166 0.0108  -0.0166 297 PHE A CA  
2441 C C   . PHE A 307 ? 0.3143 0.2901 0.3455 -0.0155 0.0108  -0.0178 297 PHE A C   
2442 O O   . PHE A 307 ? 0.2994 0.2765 0.3287 -0.0142 0.0102  -0.0182 297 PHE A O   
2443 C CB  . PHE A 307 ? 0.3476 0.3299 0.3759 -0.0170 0.0108  -0.0187 297 PHE A CB  
2444 C CG  . PHE A 307 ? 0.3782 0.3605 0.4080 -0.0183 0.0117  -0.0214 297 PHE A CG  
2445 C CD1 . PHE A 307 ? 0.4051 0.3860 0.4371 -0.0206 0.0125  -0.0218 297 PHE A CD1 
2446 C CD2 . PHE A 307 ? 0.4003 0.3840 0.4294 -0.0176 0.0116  -0.0237 297 PHE A CD2 
2447 C CE1 . PHE A 307 ? 0.4213 0.4022 0.4550 -0.0220 0.0133  -0.0246 297 PHE A CE1 
2448 C CE2 . PHE A 307 ? 0.4060 0.3903 0.4368 -0.0189 0.0125  -0.0264 297 PHE A CE2 
2449 C CZ  . PHE A 307 ? 0.4205 0.4034 0.4536 -0.0210 0.0134  -0.0270 297 PHE A CZ  
2450 N N   . ALA A 308 ? 0.3156 0.2882 0.3498 -0.0160 0.0115  -0.0185 298 ALA A N   
2451 C CA  . ALA A 308 ? 0.3271 0.2984 0.3627 -0.0148 0.0116  -0.0201 298 ALA A CA  
2452 C C   . ALA A 308 ? 0.3300 0.3016 0.3672 -0.0158 0.0124  -0.0235 298 ALA A C   
2453 O O   . ALA A 308 ? 0.3503 0.3199 0.3891 -0.0173 0.0129  -0.0242 298 ALA A O   
2454 C CB  . ALA A 308 ? 0.3400 0.3073 0.3779 -0.0138 0.0114  -0.0185 298 ALA A CB  
2455 N N   . HIS A 309 ? 0.3117 0.2860 0.3482 -0.0152 0.0124  -0.0255 299 HIS A N   
2456 C CA  . HIS A 309 ? 0.3055 0.2809 0.3436 -0.0160 0.0132  -0.0289 299 HIS A CA  
2457 C C   . HIS A 309 ? 0.3131 0.2873 0.3536 -0.0146 0.0133  -0.0303 299 HIS A C   
2458 O O   . HIS A 309 ? 0.3104 0.2833 0.3512 -0.0131 0.0128  -0.0285 299 HIS A O   
2459 C CB  . HIS A 309 ? 0.2988 0.2787 0.3345 -0.0165 0.0131  -0.0305 299 HIS A CB  
2460 C CG  . HIS A 309 ? 0.2907 0.2726 0.3239 -0.0153 0.0123  -0.0295 299 HIS A CG  
2461 N ND1 . HIS A 309 ? 0.2869 0.2697 0.3209 -0.0146 0.0123  -0.0305 299 HIS A ND1 
2462 C CD2 . HIS A 309 ? 0.2811 0.2642 0.3109 -0.0149 0.0112  -0.0278 299 HIS A CD2 
2463 C CE1 . HIS A 309 ? 0.2849 0.2692 0.3159 -0.0142 0.0113  -0.0292 299 HIS A CE1 
2464 N NE2 . HIS A 309 ? 0.2810 0.2650 0.3093 -0.0142 0.0106  -0.0275 299 HIS A NE2 
2465 N N   . GLY A 310 ? 0.3202 0.2954 0.3625 -0.0151 0.0140  -0.0337 300 GLY A N   
2466 C CA  . GLY A 310 ? 0.3265 0.3016 0.3712 -0.0137 0.0142  -0.0358 300 GLY A CA  
2467 C C   . GLY A 310 ? 0.3288 0.3091 0.3722 -0.0131 0.0141  -0.0368 300 GLY A C   
2468 O O   . GLY A 310 ? 0.3136 0.2962 0.3538 -0.0136 0.0135  -0.0351 300 GLY A O   
2469 N N   . TRP A 311 ? 0.3316 0.3134 0.3773 -0.0122 0.0144  -0.0396 301 TRP A N   
2470 C CA  . TRP A 311 ? 0.3403 0.3275 0.3851 -0.0119 0.0143  -0.0407 301 TRP A CA  
2471 C C   . TRP A 311 ? 0.3437 0.3353 0.3888 -0.0132 0.0150  -0.0443 301 TRP A C   
2472 O O   . TRP A 311 ? 0.3444 0.3349 0.3921 -0.0133 0.0157  -0.0473 301 TRP A O   
2473 C CB  . TRP A 311 ? 0.3551 0.3427 0.4024 -0.0097 0.0142  -0.0414 301 TRP A CB  
2474 C CG  . TRP A 311 ? 0.3711 0.3560 0.4181 -0.0083 0.0134  -0.0379 301 TRP A CG  
2475 C CD1 . TRP A 311 ? 0.3724 0.3566 0.4162 -0.0089 0.0128  -0.0343 301 TRP A CD1 
2476 C CD2 . TRP A 311 ? 0.3858 0.3685 0.4355 -0.0059 0.0132  -0.0379 301 TRP A CD2 
2477 N NE1 . TRP A 311 ? 0.3755 0.3575 0.4200 -0.0073 0.0122  -0.0320 301 TRP A NE1 
2478 C CE2 . TRP A 311 ? 0.3897 0.3708 0.4378 -0.0053 0.0124  -0.0340 301 TRP A CE2 
2479 C CE3 . TRP A 311 ? 0.4055 0.3874 0.4589 -0.0039 0.0134  -0.0410 301 TRP A CE3 
2480 C CZ2 . TRP A 311 ? 0.4012 0.3802 0.4513 -0.0030 0.0119  -0.0328 301 TRP A CZ2 
2481 C CZ3 . TRP A 311 ? 0.4136 0.3930 0.4689 -0.0012 0.0128  -0.0399 301 TRP A CZ3 
2482 C CH2 . TRP A 311 ? 0.4125 0.3906 0.4661 -0.0008 0.0121  -0.0357 301 TRP A CH2 
2483 N N   . ILE A 312 ? 0.3395 0.3359 0.3818 -0.0142 0.0146  -0.0440 302 ILE A N   
2484 C CA  . ILE A 312 ? 0.3452 0.3473 0.3877 -0.0152 0.0151  -0.0472 302 ILE A CA  
2485 C C   . ILE A 312 ? 0.3719 0.3772 0.4168 -0.0138 0.0153  -0.0491 302 ILE A C   
2486 O O   . ILE A 312 ? 0.3533 0.3595 0.3972 -0.0131 0.0147  -0.0470 302 ILE A O   
2487 C CB  . ILE A 312 ? 0.3335 0.3394 0.3718 -0.0170 0.0145  -0.0458 302 ILE A CB  
2488 C CG1 . ILE A 312 ? 0.3325 0.3358 0.3686 -0.0178 0.0142  -0.0442 302 ILE A CG1 
2489 C CG2 . ILE A 312 ? 0.3323 0.3448 0.3708 -0.0182 0.0149  -0.0490 302 ILE A CG2 
2490 C CD1 . ILE A 312 ? 0.3219 0.3280 0.3537 -0.0191 0.0132  -0.0428 302 ILE A CD1 
2491 N N   . LEU A 313 ? 0.3894 0.3965 0.4376 -0.0133 0.0161  -0.0532 303 LEU A N   
2492 C CA  . LEU A 313 ? 0.4222 0.4329 0.4731 -0.0116 0.0163  -0.0560 303 LEU A CA  
2493 C C   . LEU A 313 ? 0.4377 0.4569 0.4881 -0.0131 0.0168  -0.0590 303 LEU A C   
2494 O O   . LEU A 313 ? 0.4102 0.4314 0.4591 -0.0152 0.0171  -0.0596 303 LEU A O   
2495 C CB  . LEU A 313 ? 0.4367 0.4430 0.4918 -0.0096 0.0167  -0.0590 303 LEU A CB  
2496 C CG  . LEU A 313 ? 0.4502 0.4478 0.5061 -0.0084 0.0163  -0.0564 303 LEU A CG  
2497 C CD1 . LEU A 313 ? 0.4595 0.4525 0.5192 -0.0068 0.0165  -0.0598 303 LEU A CD1 
2498 C CD2 . LEU A 313 ? 0.4520 0.4485 0.5074 -0.0066 0.0155  -0.0531 303 LEU A CD2 
2499 N N   . MET A 314 ? 0.4668 0.4915 0.5186 -0.0120 0.0168  -0.0607 304 MET A N   
2500 C CA  . MET A 314 ? 0.5094 0.5428 0.5619 -0.0129 0.0173  -0.0645 304 MET A CA  
2501 C C   . MET A 314 ? 0.5572 0.5914 0.6146 -0.0099 0.0178  -0.0692 304 MET A C   
2502 O O   . MET A 314 ? 0.5579 0.5848 0.6175 -0.0075 0.0176  -0.0690 304 MET A O   
2503 C CB  . MET A 314 ? 0.5056 0.5462 0.5552 -0.0144 0.0168  -0.0627 304 MET A CB  
2504 C CG  . MET A 314 ? 0.5020 0.5420 0.5466 -0.0174 0.0160  -0.0587 304 MET A CG  
2505 S SD  . MET A 314 ? 0.4886 0.5308 0.5316 -0.0200 0.0165  -0.0603 304 MET A SD  
2506 C CE  . MET A 314 ? 0.4975 0.5506 0.5379 -0.0228 0.0162  -0.0609 304 MET A CE  
2507 N N   . LYS A 315 ? 0.6088 0.6516 0.6677 -0.0100 0.0183  -0.0733 305 LYS A N   
2508 C CA  . LYS A 315 ? 0.6455 0.6898 0.7089 -0.0068 0.0187  -0.0783 305 LYS A CA  
2509 C C   . LYS A 315 ? 0.6611 0.7102 0.7256 -0.0045 0.0182  -0.0781 305 LYS A C   
2510 O O   . LYS A 315 ? 0.7009 0.7593 0.7670 -0.0038 0.0185  -0.0818 305 LYS A O   
2511 C CB  . LYS A 315 ? 0.6673 0.7185 0.7322 -0.0078 0.0195  -0.0835 305 LYS A CB  
2512 C CG  . LYS A 315 ? 0.6778 0.7230 0.7428 -0.0091 0.0200  -0.0845 305 LYS A CG  
2513 C CD  . LYS A 315 ? 0.6855 0.7381 0.7488 -0.0124 0.0207  -0.0862 305 LYS A CD  
2514 C CE  . LYS A 315 ? 0.6997 0.7622 0.7656 -0.0117 0.0213  -0.0920 305 LYS A CE  
2515 N NZ  . LYS A 315 ? 0.7085 0.7812 0.7732 -0.0123 0.0211  -0.0916 305 LYS A NZ  
2516 N N   . ASP A 316 ? 0.6539 0.6971 0.7171 -0.0037 0.0174  -0.0737 306 ASP A N   
2517 C CA  . ASP A 316 ? 0.6609 0.7058 0.7254 -0.0010 0.0168  -0.0728 306 ASP A CA  
2518 C C   . ASP A 316 ? 0.6509 0.6870 0.7136 -0.0007 0.0161  -0.0673 306 ASP A C   
2519 O O   . ASP A 316 ? 0.6593 0.6973 0.7212 0.0000  0.0155  -0.0648 306 ASP A O   
2520 C CB  . ASP A 316 ? 0.6810 0.7376 0.7439 -0.0025 0.0168  -0.0730 306 ASP A CB  
2521 C CG  . ASP A 316 ? 0.6905 0.7482 0.7482 -0.0067 0.0165  -0.0681 306 ASP A CG  
2522 O OD1 . ASP A 316 ? 0.6877 0.7399 0.7429 -0.0089 0.0165  -0.0659 306 ASP A OD1 
2523 O OD2 . ASP A 316 ? 0.6929 0.7574 0.7489 -0.0078 0.0161  -0.0667 306 ASP A OD2 
2524 N N   . GLY A 317 ? 0.6143 0.6413 0.6764 -0.0013 0.0161  -0.0657 307 GLY A N   
2525 C CA  . GLY A 317 ? 0.5784 0.5975 0.6389 -0.0013 0.0155  -0.0608 307 GLY A CA  
2526 C C   . GLY A 317 ? 0.5497 0.5675 0.6057 -0.0047 0.0153  -0.0568 307 GLY A C   
2527 O O   . GLY A 317 ? 0.5157 0.5383 0.5696 -0.0073 0.0156  -0.0574 307 GLY A O   
2528 N N   . LYS A 318 ? 0.5261 0.5375 0.5808 -0.0043 0.0147  -0.0527 308 LYS A N   
2529 C CA  . LYS A 318 ? 0.5036 0.5127 0.5543 -0.0068 0.0143  -0.0486 308 LYS A CA  
2530 C C   . LYS A 318 ? 0.4691 0.4848 0.5163 -0.0092 0.0141  -0.0477 308 LYS A C   
2531 O O   . LYS A 318 ? 0.4655 0.4867 0.5128 -0.0088 0.0138  -0.0479 308 LYS A O   
2532 C CB  . LYS A 318 ? 0.5157 0.5193 0.5659 -0.0055 0.0136  -0.0447 308 LYS A CB  
2533 C CG  . LYS A 318 ? 0.5214 0.5218 0.5677 -0.0075 0.0131  -0.0408 308 LYS A CG  
2534 C CD  . LYS A 318 ? 0.5299 0.5281 0.5751 -0.0065 0.0123  -0.0371 308 LYS A CD  
2535 C CE  . LYS A 318 ? 0.5246 0.5212 0.5656 -0.0084 0.0117  -0.0337 308 LYS A CE  
2536 N NZ  . LYS A 318 ? 0.5245 0.5261 0.5621 -0.0103 0.0112  -0.0333 308 LYS A NZ  
2537 N N   . MET A 319 ? 0.4259 0.4413 0.4699 -0.0117 0.0140  -0.0466 309 MET A N   
2538 C CA  . MET A 319 ? 0.4193 0.4394 0.4593 -0.0142 0.0133  -0.0451 309 MET A CA  
2539 C C   . MET A 319 ? 0.4247 0.4427 0.4622 -0.0142 0.0123  -0.0410 309 MET A C   
2540 O O   . MET A 319 ? 0.4037 0.4154 0.4403 -0.0134 0.0119  -0.0384 309 MET A O   
2541 C CB  . MET A 319 ? 0.4055 0.4247 0.4425 -0.0164 0.0132  -0.0445 309 MET A CB  
2542 C CG  . MET A 319 ? 0.4004 0.4245 0.4331 -0.0191 0.0123  -0.0433 309 MET A CG  
2543 S SD  . MET A 319 ? 0.3801 0.4040 0.4096 -0.0212 0.0120  -0.0431 309 MET A SD  
2544 C CE  . MET A 319 ? 0.3883 0.4173 0.4220 -0.0211 0.0136  -0.0484 309 MET A CE  
2545 N N   . SER A 320 ? 0.4283 0.4521 0.4645 -0.0151 0.0119  -0.0407 310 SER A N   
2546 C CA  . SER A 320 ? 0.4486 0.4716 0.4827 -0.0153 0.0110  -0.0374 310 SER A CA  
2547 C C   . SER A 320 ? 0.4693 0.4978 0.4992 -0.0185 0.0102  -0.0363 310 SER A C   
2548 O O   . SER A 320 ? 0.4615 0.4974 0.4922 -0.0195 0.0106  -0.0388 310 SER A O   
2549 C CB  . SER A 320 ? 0.4543 0.4788 0.4923 -0.0124 0.0114  -0.0385 310 SER A CB  
2550 O OG  . SER A 320 ? 0.4483 0.4747 0.4845 -0.0129 0.0106  -0.0360 310 SER A OG  
2551 N N   . LYS A 321 ? 0.4856 0.5106 0.5110 -0.0201 0.0089  -0.0327 311 LYS A N   
2552 C CA  . LYS A 321 ? 0.5143 0.5432 0.5351 -0.0236 0.0078  -0.0311 311 LYS A CA  
2553 C C   . LYS A 321 ? 0.5348 0.5706 0.5563 -0.0242 0.0078  -0.0314 311 LYS A C   
2554 O O   . LYS A 321 ? 0.5351 0.5773 0.5543 -0.0272 0.0075  -0.0316 311 LYS A O   
2555 C CB  . LYS A 321 ? 0.5222 0.5446 0.5376 -0.0251 0.0062  -0.0274 311 LYS A CB  
2556 C CG  . LYS A 321 ? 0.5330 0.5506 0.5481 -0.0236 0.0056  -0.0249 311 LYS A CG  
2557 C CD  . LYS A 321 ? 0.5283 0.5395 0.5383 -0.0248 0.0040  -0.0219 311 LYS A CD  
2558 C CE  . LYS A 321 ? 0.5434 0.5482 0.5546 -0.0221 0.0041  -0.0208 311 LYS A CE  
2559 N NZ  . LYS A 321 ? 0.5471 0.5518 0.5601 -0.0207 0.0043  -0.0197 311 LYS A NZ  
2560 N N   . SER A 322 ? 0.5490 0.5837 0.5734 -0.0215 0.0082  -0.0312 312 SER A N   
2561 C CA  . SER A 322 ? 0.5761 0.6181 0.6019 -0.0215 0.0083  -0.0318 312 SER A CA  
2562 C C   . SER A 322 ? 0.5801 0.6302 0.6100 -0.0203 0.0095  -0.0361 312 SER A C   
2563 O O   . SER A 322 ? 0.5778 0.6367 0.6078 -0.0215 0.0095  -0.0371 312 SER A O   
2564 C CB  . SER A 322 ? 0.5767 0.6152 0.6045 -0.0186 0.0083  -0.0303 312 SER A CB  
2565 O OG  . SER A 322 ? 0.5803 0.6157 0.6129 -0.0147 0.0092  -0.0323 312 SER A OG  
2566 N N   . LYS A 323 ? 0.5884 0.6360 0.6219 -0.0178 0.0104  -0.0389 313 LYS A N   
2567 C CA  . LYS A 323 ? 0.5992 0.6539 0.6368 -0.0164 0.0115  -0.0435 313 LYS A CA  
2568 C C   . LYS A 323 ? 0.5996 0.6608 0.6350 -0.0199 0.0116  -0.0450 313 LYS A C   
2569 O O   . LYS A 323 ? 0.6036 0.6742 0.6409 -0.0200 0.0122  -0.0482 313 LYS A O   
2570 C CB  . LYS A 323 ? 0.6107 0.6596 0.6526 -0.0129 0.0123  -0.0459 313 LYS A CB  
2571 C CG  . LYS A 323 ? 0.6232 0.6783 0.6696 -0.0107 0.0133  -0.0511 313 LYS A CG  
2572 C CD  . LYS A 323 ? 0.6389 0.6870 0.6890 -0.0076 0.0138  -0.0533 313 LYS A CD  
2573 C CE  . LYS A 323 ? 0.6563 0.6996 0.7096 -0.0036 0.0136  -0.0528 313 LYS A CE  
2574 N NZ  . LYS A 323 ? 0.6656 0.7028 0.7226 -0.0009 0.0140  -0.0555 313 LYS A NZ  
2575 N N   . GLY A 324 ? 0.5824 0.6390 0.6138 -0.0225 0.0110  -0.0428 314 GLY A N   
2576 C CA  . GLY A 324 ? 0.5782 0.6402 0.6070 -0.0259 0.0109  -0.0436 314 GLY A CA  
2577 C C   . GLY A 324 ? 0.5665 0.6295 0.5981 -0.0250 0.0120  -0.0473 314 GLY A C   
2578 O O   . GLY A 324 ? 0.5885 0.6569 0.6183 -0.0277 0.0120  -0.0483 314 GLY A O   
2579 N N   . ASN A 325 ? 0.5534 0.6111 0.5891 -0.0214 0.0128  -0.0492 315 ASN A N   
2580 C CA  . ASN A 325 ? 0.5115 0.5686 0.5497 -0.0206 0.0138  -0.0526 315 ASN A CA  
2581 C C   . ASN A 325 ? 0.4921 0.5422 0.5271 -0.0220 0.0133  -0.0502 315 ASN A C   
2582 O O   . ASN A 325 ? 0.4966 0.5404 0.5336 -0.0202 0.0137  -0.0508 315 ASN A O   
2583 C CB  . ASN A 325 ? 0.5083 0.5621 0.5520 -0.0164 0.0146  -0.0556 315 ASN A CB  
2584 C CG  . ASN A 325 ? 0.5045 0.5482 0.5484 -0.0144 0.0142  -0.0526 315 ASN A CG  
2585 O OD1 . ASN A 325 ? 0.4648 0.5053 0.5054 -0.0154 0.0133  -0.0485 315 ASN A OD1 
2586 N ND2 . ASN A 325 ? 0.4934 0.5319 0.5412 -0.0116 0.0148  -0.0547 315 ASN A ND2 
2587 N N   . VAL A 326 ? 0.4501 0.5017 0.4801 -0.0254 0.0123  -0.0476 316 VAL A N   
2588 C CA  . VAL A 326 ? 0.4271 0.4717 0.4535 -0.0263 0.0113  -0.0445 316 VAL A CA  
2589 C C   . VAL A 326 ? 0.4056 0.4524 0.4298 -0.0284 0.0112  -0.0453 316 VAL A C   
2590 O O   . VAL A 326 ? 0.3974 0.4520 0.4210 -0.0306 0.0113  -0.0468 316 VAL A O   
2591 C CB  . VAL A 326 ? 0.4301 0.4713 0.4515 -0.0279 0.0097  -0.0399 316 VAL A CB  
2592 C CG1 . VAL A 326 ? 0.4340 0.4718 0.4573 -0.0256 0.0097  -0.0387 316 VAL A CG1 
2593 C CG2 . VAL A 326 ? 0.4284 0.4764 0.4461 -0.0315 0.0088  -0.0389 316 VAL A CG2 
2594 N N   . VAL A 327 ? 0.3772 0.4176 0.4002 -0.0278 0.0109  -0.0441 317 VAL A N   
2595 C CA  . VAL A 327 ? 0.3665 0.4077 0.3865 -0.0296 0.0103  -0.0438 317 VAL A CA  
2596 C C   . VAL A 327 ? 0.3655 0.4006 0.3803 -0.0303 0.0084  -0.0394 317 VAL A C   
2597 O O   . VAL A 327 ? 0.3388 0.3672 0.3537 -0.0284 0.0081  -0.0377 317 VAL A O   
2598 C CB  . VAL A 327 ? 0.3756 0.4154 0.3988 -0.0282 0.0115  -0.0466 317 VAL A CB  
2599 C CG1 . VAL A 327 ? 0.3722 0.4134 0.3921 -0.0299 0.0109  -0.0462 317 VAL A CG1 
2600 C CG2 . VAL A 327 ? 0.3806 0.4254 0.4090 -0.0272 0.0132  -0.0512 317 VAL A CG2 
2601 N N   . ASP A 328 ? 0.3625 0.3999 0.3726 -0.0330 0.0070  -0.0376 318 ASP A N   
2602 C CA  . ASP A 328 ? 0.3665 0.3981 0.3709 -0.0338 0.0048  -0.0336 318 ASP A CA  
2603 C C   . ASP A 328 ? 0.3456 0.3739 0.3484 -0.0330 0.0042  -0.0334 318 ASP A C   
2604 O O   . ASP A 328 ? 0.3380 0.3709 0.3403 -0.0343 0.0043  -0.0348 318 ASP A O   
2605 C CB  . ASP A 328 ? 0.3888 0.4243 0.3886 -0.0375 0.0033  -0.0316 318 ASP A CB  
2606 C CG  . ASP A 328 ? 0.4018 0.4305 0.3954 -0.0385 0.0007  -0.0274 318 ASP A CG  
2607 O OD1 . ASP A 328 ? 0.4005 0.4220 0.3929 -0.0362 0.0000  -0.0261 318 ASP A OD1 
2608 O OD2 . ASP A 328 ? 0.4275 0.4582 0.4170 -0.0417 -0.0005 -0.0253 318 ASP A OD2 
2609 N N   . PRO A 329 ? 0.3303 0.3516 0.3324 -0.0307 0.0036  -0.0318 319 PRO A N   
2610 C CA  . PRO A 329 ? 0.3323 0.3515 0.3329 -0.0297 0.0030  -0.0319 319 PRO A CA  
2611 C C   . PRO A 329 ? 0.3332 0.3527 0.3282 -0.0315 0.0008  -0.0299 319 PRO A C   
2612 O O   . PRO A 329 ? 0.3343 0.3552 0.3287 -0.0312 0.0007  -0.0308 319 PRO A O   
2613 C CB  . PRO A 329 ? 0.3276 0.3398 0.3279 -0.0272 0.0025  -0.0303 319 PRO A CB  
2614 C CG  . PRO A 329 ? 0.3334 0.3431 0.3328 -0.0275 0.0019  -0.0283 319 PRO A CG  
2615 C CD  . PRO A 329 ? 0.3344 0.3502 0.3368 -0.0290 0.0033  -0.0301 319 PRO A CD  
2616 N N   . ASN A 330 ? 0.3408 0.3587 0.3314 -0.0335 -0.0009 -0.0271 320 ASN A N   
2617 C CA  . ASN A 330 ? 0.3565 0.3741 0.3412 -0.0356 -0.0032 -0.0249 320 ASN A CA  
2618 C C   . ASN A 330 ? 0.3630 0.3886 0.3486 -0.0377 -0.0024 -0.0269 320 ASN A C   
2619 O O   . ASN A 330 ? 0.3658 0.3916 0.3483 -0.0381 -0.0037 -0.0262 320 ASN A O   
2620 C CB  . ASN A 330 ? 0.3622 0.3773 0.3422 -0.0382 -0.0052 -0.0217 320 ASN A CB  
2621 C CG  . ASN A 330 ? 0.3679 0.3740 0.3445 -0.0364 -0.0071 -0.0191 320 ASN A CG  
2622 O OD1 . ASN A 330 ? 0.3859 0.3871 0.3601 -0.0343 -0.0086 -0.0183 320 ASN A OD1 
2623 N ND2 . ASN A 330 ? 0.3599 0.3641 0.3363 -0.0372 -0.0072 -0.0178 320 ASN A ND2 
2624 N N   . ILE A 331 ? 0.3673 0.3996 0.3572 -0.0388 -0.0003 -0.0295 321 ILE A N   
2625 C CA  . ILE A 331 ? 0.3775 0.4185 0.3688 -0.0408 0.0006  -0.0318 321 ILE A CA  
2626 C C   . ILE A 331 ? 0.3650 0.4073 0.3591 -0.0389 0.0018  -0.0346 321 ILE A C   
2627 O O   . ILE A 331 ? 0.3518 0.3982 0.3441 -0.0403 0.0013  -0.0349 321 ILE A O   
2628 C CB  . ILE A 331 ? 0.4002 0.4484 0.3957 -0.0420 0.0026  -0.0344 321 ILE A CB  
2629 C CG1 . ILE A 331 ? 0.4226 0.4709 0.4143 -0.0447 0.0012  -0.0315 321 ILE A CG1 
2630 C CG2 . ILE A 331 ? 0.3997 0.4575 0.3972 -0.0437 0.0039  -0.0377 321 ILE A CG2 
2631 C CD1 . ILE A 331 ? 0.4353 0.4909 0.4307 -0.0456 0.0028  -0.0337 321 ILE A CD1 
2632 N N   . LEU A 332 ? 0.3392 0.3781 0.3375 -0.0360 0.0033  -0.0363 322 LEU A N   
2633 C CA  . LEU A 332 ? 0.3322 0.3719 0.3332 -0.0343 0.0044  -0.0388 322 LEU A CA  
2634 C C   . LEU A 332 ? 0.3340 0.3706 0.3305 -0.0336 0.0024  -0.0367 322 LEU A C   
2635 O O   . LEU A 332 ? 0.3350 0.3757 0.3318 -0.0339 0.0027  -0.0383 322 LEU A O   
2636 C CB  . LEU A 332 ? 0.3279 0.3638 0.3335 -0.0318 0.0060  -0.0404 322 LEU A CB  
2637 C CG  . LEU A 332 ? 0.3377 0.3766 0.3485 -0.0317 0.0081  -0.0433 322 LEU A CG  
2638 C CD1 . LEU A 332 ? 0.3376 0.3713 0.3521 -0.0292 0.0092  -0.0440 322 LEU A CD1 
2639 C CD2 . LEU A 332 ? 0.3423 0.3890 0.3560 -0.0330 0.0096  -0.0472 322 LEU A CD2 
2640 N N   . ILE A 333 ? 0.3281 0.3576 0.3207 -0.0325 0.0003  -0.0333 323 ILE A N   
2641 C CA  . ILE A 333 ? 0.3327 0.3587 0.3209 -0.0313 -0.0018 -0.0313 323 ILE A CA  
2642 C C   . ILE A 333 ? 0.3577 0.3870 0.3414 -0.0337 -0.0036 -0.0299 323 ILE A C   
2643 O O   . ILE A 333 ? 0.3467 0.3783 0.3294 -0.0331 -0.0041 -0.0305 323 ILE A O   
2644 C CB  . ILE A 333 ? 0.3303 0.3478 0.3151 -0.0294 -0.0038 -0.0283 323 ILE A CB  
2645 C CG1 . ILE A 333 ? 0.3296 0.3445 0.3187 -0.0270 -0.0021 -0.0296 323 ILE A CG1 
2646 C CG2 . ILE A 333 ? 0.3351 0.3492 0.3150 -0.0278 -0.0064 -0.0265 323 ILE A CG2 
2647 C CD1 . ILE A 333 ? 0.3300 0.3380 0.3170 -0.0258 -0.0034 -0.0271 323 ILE A CD1 
2648 N N   . ASP A 334 ? 0.3723 0.4021 0.3533 -0.0365 -0.0045 -0.0280 324 ASP A N   
2649 C CA  . ASP A 334 ? 0.4061 0.4392 0.3825 -0.0395 -0.0063 -0.0262 324 ASP A CA  
2650 C C   . ASP A 334 ? 0.4089 0.4512 0.3880 -0.0407 -0.0047 -0.0292 324 ASP A C   
2651 O O   . ASP A 334 ? 0.4225 0.4667 0.3982 -0.0415 -0.0062 -0.0282 324 ASP A O   
2652 C CB  . ASP A 334 ? 0.4213 0.4550 0.3952 -0.0430 -0.0071 -0.0241 324 ASP A CB  
2653 C CG  . ASP A 334 ? 0.4461 0.4705 0.4154 -0.0425 -0.0095 -0.0204 324 ASP A CG  
2654 O OD1 . ASP A 334 ? 0.4786 0.4959 0.4462 -0.0394 -0.0108 -0.0194 324 ASP A OD1 
2655 O OD2 . ASP A 334 ? 0.4600 0.4847 0.4274 -0.0454 -0.0100 -0.0187 324 ASP A OD2 
2656 N N   . ARG A 335 ? 0.4061 0.4540 0.3913 -0.0408 -0.0017 -0.0330 325 ARG A N   
2657 C CA  . ARG A 335 ? 0.4176 0.4746 0.4057 -0.0421 0.0000  -0.0364 325 ARG A CA  
2658 C C   . ARG A 335 ? 0.4050 0.4626 0.3955 -0.0397 0.0008  -0.0387 325 ARG A C   
2659 O O   . ARG A 335 ? 0.3866 0.4493 0.3760 -0.0407 0.0005  -0.0395 325 ARG A O   
2660 C CB  . ARG A 335 ? 0.4429 0.5058 0.4365 -0.0430 0.0026  -0.0399 325 ARG A CB  
2661 C CG  . ARG A 335 ? 0.4815 0.5544 0.4776 -0.0447 0.0041  -0.0436 325 ARG A CG  
2662 C CD  . ARG A 335 ? 0.5212 0.6007 0.5214 -0.0460 0.0061  -0.0466 325 ARG A CD  
2663 N NE  . ARG A 335 ? 0.5549 0.6438 0.5582 -0.0472 0.0077  -0.0509 325 ARG A NE  
2664 C CZ  . ARG A 335 ? 0.5806 0.6766 0.5883 -0.0477 0.0097  -0.0549 325 ARG A CZ  
2665 N NH1 . ARG A 335 ? 0.5889 0.6840 0.5986 -0.0472 0.0103  -0.0553 325 ARG A NH1 
2666 N NH2 . ARG A 335 ? 0.5909 0.6953 0.6010 -0.0487 0.0110  -0.0589 325 ARG A NH2 
2667 N N   . TYR A 336 ? 0.3866 0.4394 0.3804 -0.0370 0.0020  -0.0399 326 TYR A N   
2668 C CA  . TYR A 336 ? 0.3786 0.4328 0.3755 -0.0351 0.0033  -0.0427 326 TYR A CA  
2669 C C   . TYR A 336 ? 0.3705 0.4189 0.3648 -0.0324 0.0017  -0.0407 326 TYR A C   
2670 O O   . TYR A 336 ? 0.3683 0.4190 0.3643 -0.0313 0.0024  -0.0427 326 TYR A O   
2671 C CB  . TYR A 336 ? 0.3877 0.4422 0.3908 -0.0344 0.0060  -0.0461 326 TYR A CB  
2672 C CG  . TYR A 336 ? 0.4049 0.4660 0.4113 -0.0365 0.0078  -0.0491 326 TYR A CG  
2673 C CD1 . TYR A 336 ? 0.4220 0.4910 0.4299 -0.0380 0.0088  -0.0523 326 TYR A CD1 
2674 C CD2 . TYR A 336 ? 0.4200 0.4800 0.4280 -0.0367 0.0083  -0.0491 326 TYR A CD2 
2675 C CE1 . TYR A 336 ? 0.4318 0.5075 0.4428 -0.0396 0.0104  -0.0554 326 TYR A CE1 
2676 C CE2 . TYR A 336 ? 0.4316 0.4983 0.4427 -0.0382 0.0098  -0.0522 326 TYR A CE2 
2677 C CZ  . TYR A 336 ? 0.4377 0.5123 0.4504 -0.0396 0.0108  -0.0554 326 TYR A CZ  
2678 O OH  . TYR A 336 ? 0.4733 0.5551 0.4891 -0.0409 0.0123  -0.0589 326 TYR A OH  
2679 N N   . GLY A 337 ? 0.3496 0.3911 0.3398 -0.0314 -0.0005 -0.0371 327 GLY A N   
2680 C CA  . GLY A 337 ? 0.3522 0.3882 0.3396 -0.0285 -0.0023 -0.0353 327 GLY A CA  
2681 C C   . GLY A 337 ? 0.3403 0.3712 0.3305 -0.0263 -0.0013 -0.0356 327 GLY A C   
2682 O O   . GLY A 337 ? 0.3180 0.3499 0.3129 -0.0268 0.0009  -0.0376 327 GLY A O   
2683 N N   . LEU A 338 ? 0.3383 0.3640 0.3254 -0.0237 -0.0032 -0.0337 328 LEU A N   
2684 C CA  . LEU A 338 ? 0.3340 0.3547 0.3227 -0.0215 -0.0028 -0.0334 328 LEU A CA  
2685 C C   . LEU A 338 ? 0.3198 0.3436 0.3136 -0.0206 -0.0005 -0.0363 328 LEU A C   
2686 O O   . LEU A 338 ? 0.2982 0.3204 0.2956 -0.0206 0.0012  -0.0371 328 LEU A O   
2687 C CB  . LEU A 338 ? 0.3418 0.3566 0.3255 -0.0189 -0.0058 -0.0307 328 LEU A CB  
2688 C CG  . LEU A 338 ? 0.3411 0.3515 0.3261 -0.0164 -0.0056 -0.0305 328 LEU A CG  
2689 C CD1 . LEU A 338 ? 0.3441 0.3518 0.3315 -0.0178 -0.0043 -0.0299 328 LEU A CD1 
2690 C CD2 . LEU A 338 ? 0.3540 0.3589 0.3339 -0.0136 -0.0087 -0.0284 328 LEU A CD2 
2691 N N   . ASP A 339 ? 0.3176 0.3456 0.3113 -0.0199 -0.0005 -0.0378 329 ASP A N   
2692 C CA  . ASP A 339 ? 0.3134 0.3448 0.3114 -0.0196 0.0016  -0.0405 329 ASP A CA  
2693 C C   . ASP A 339 ? 0.2911 0.3251 0.2942 -0.0220 0.0043  -0.0431 329 ASP A C   
2694 O O   . ASP A 339 ? 0.2804 0.3131 0.2871 -0.0219 0.0060  -0.0442 329 ASP A O   
2695 C CB  . ASP A 339 ? 0.3233 0.3603 0.3204 -0.0189 0.0011  -0.0420 329 ASP A CB  
2696 C CG  . ASP A 339 ? 0.3400 0.3751 0.3338 -0.0156 -0.0010 -0.0405 329 ASP A CG  
2697 O OD1 . ASP A 339 ? 0.3476 0.3768 0.3395 -0.0138 -0.0022 -0.0385 329 ASP A OD1 
2698 O OD2 . ASP A 339 ? 0.3645 0.4044 0.3574 -0.0146 -0.0015 -0.0417 329 ASP A OD2 
2699 N N   . ALA A 340 ? 0.2887 0.3262 0.2918 -0.0241 0.0047  -0.0439 330 ALA A N   
2700 C CA  . ALA A 340 ? 0.2806 0.3209 0.2884 -0.0261 0.0071  -0.0467 330 ALA A CA  
2701 C C   . ALA A 340 ? 0.2712 0.3064 0.2812 -0.0257 0.0078  -0.0460 330 ALA A C   
2702 O O   . ALA A 340 ? 0.2677 0.3026 0.2819 -0.0260 0.0097  -0.0482 330 ALA A O   
2703 C CB  . ALA A 340 ? 0.2898 0.3351 0.2966 -0.0282 0.0070  -0.0474 330 ALA A CB  
2704 N N   . THR A 341 ? 0.2685 0.2996 0.2753 -0.0252 0.0062  -0.0429 331 THR A N   
2705 C CA  . THR A 341 ? 0.2656 0.2924 0.2739 -0.0249 0.0067  -0.0419 331 THR A CA  
2706 C C   . THR A 341 ? 0.2614 0.2838 0.2715 -0.0231 0.0072  -0.0415 331 THR A C   
2707 O O   . THR A 341 ? 0.2538 0.2748 0.2678 -0.0231 0.0087  -0.0426 331 THR A O   
2708 C CB  . THR A 341 ? 0.2768 0.3004 0.2806 -0.0251 0.0046  -0.0386 331 THR A CB  
2709 O OG1 . THR A 341 ? 0.2880 0.3163 0.2900 -0.0273 0.0041  -0.0388 331 THR A OG1 
2710 C CG2 . THR A 341 ? 0.2775 0.2976 0.2830 -0.0249 0.0051  -0.0376 331 THR A CG2 
2711 N N   . ARG A 342 ? 0.2614 0.2820 0.2688 -0.0214 0.0058  -0.0400 332 ARG A N   
2712 C CA  . ARG A 342 ? 0.2577 0.2754 0.2667 -0.0199 0.0063  -0.0397 332 ARG A CA  
2713 C C   . ARG A 342 ? 0.2576 0.2783 0.2710 -0.0209 0.0084  -0.0427 332 ARG A C   
2714 O O   . ARG A 342 ? 0.2584 0.2765 0.2747 -0.0208 0.0096  -0.0429 332 ARG A O   
2715 C CB  . ARG A 342 ? 0.2611 0.2775 0.2661 -0.0178 0.0042  -0.0380 332 ARG A CB  
2716 C CG  . ARG A 342 ? 0.2570 0.2683 0.2577 -0.0167 0.0020  -0.0350 332 ARG A CG  
2717 C CD  . ARG A 342 ? 0.2575 0.2678 0.2541 -0.0143 -0.0002 -0.0339 332 ARG A CD  
2718 N NE  . ARG A 342 ? 0.2542 0.2648 0.2525 -0.0126 0.0003  -0.0345 332 ARG A NE  
2719 C CZ  . ARG A 342 ? 0.2522 0.2589 0.2494 -0.0107 -0.0005 -0.0330 332 ARG A CZ  
2720 N NH1 . ARG A 342 ? 0.2626 0.2642 0.2568 -0.0102 -0.0022 -0.0307 332 ARG A NH1 
2721 N NH2 . ARG A 342 ? 0.2491 0.2576 0.2481 -0.0097 0.0002  -0.0338 332 ARG A NH2 
2722 N N   . TYR A 343 ? 0.2629 0.2888 0.2765 -0.0219 0.0089  -0.0448 333 TYR A N   
2723 C CA  . TYR A 343 ? 0.2700 0.2989 0.2875 -0.0232 0.0109  -0.0479 333 TYR A CA  
2724 C C   . TYR A 343 ? 0.2765 0.3039 0.2981 -0.0245 0.0126  -0.0497 333 TYR A C   
2725 O O   . TYR A 343 ? 0.2735 0.2988 0.2982 -0.0249 0.0138  -0.0506 333 TYR A O   
2726 C CB  . TYR A 343 ? 0.2710 0.3063 0.2878 -0.0243 0.0110  -0.0501 333 TYR A CB  
2727 C CG  . TYR A 343 ? 0.2730 0.3115 0.2937 -0.0260 0.0130  -0.0534 333 TYR A CG  
2728 C CD1 . TYR A 343 ? 0.2791 0.3210 0.3023 -0.0279 0.0144  -0.0565 333 TYR A CD1 
2729 C CD2 . TYR A 343 ? 0.2747 0.3129 0.2963 -0.0259 0.0134  -0.0535 333 TYR A CD2 
2730 C CE1 . TYR A 343 ? 0.2828 0.3268 0.3093 -0.0297 0.0160  -0.0596 333 TYR A CE1 
2731 C CE2 . TYR A 343 ? 0.2839 0.3246 0.3087 -0.0279 0.0151  -0.0563 333 TYR A CE2 
2732 C CZ  . TYR A 343 ? 0.2804 0.3236 0.3075 -0.0298 0.0164  -0.0594 333 TYR A CZ  
2733 O OH  . TYR A 343 ? 0.2910 0.3360 0.3210 -0.0321 0.0180  -0.0624 333 TYR A OH  
2734 N N   . TYR A 344 ? 0.2777 0.3062 0.2993 -0.0251 0.0126  -0.0501 334 TYR A N   
2735 C CA  . TYR A 344 ? 0.2911 0.3188 0.3166 -0.0258 0.0140  -0.0521 334 TYR A CA  
2736 C C   . TYR A 344 ? 0.2821 0.3036 0.3091 -0.0246 0.0142  -0.0503 334 TYR A C   
2737 O O   . TYR A 344 ? 0.2816 0.3009 0.3120 -0.0249 0.0154  -0.0519 334 TYR A O   
2738 C CB  . TYR A 344 ? 0.3019 0.3325 0.3267 -0.0265 0.0138  -0.0525 334 TYR A CB  
2739 C CG  . TYR A 344 ? 0.3174 0.3467 0.3461 -0.0264 0.0149  -0.0542 334 TYR A CG  
2740 C CD1 . TYR A 344 ? 0.3208 0.3527 0.3533 -0.0272 0.0165  -0.0583 334 TYR A CD1 
2741 C CD2 . TYR A 344 ? 0.3261 0.3513 0.3545 -0.0252 0.0144  -0.0519 334 TYR A CD2 
2742 C CE1 . TYR A 344 ? 0.3387 0.3690 0.3746 -0.0266 0.0173  -0.0600 334 TYR A CE1 
2743 C CE2 . TYR A 344 ? 0.3366 0.3607 0.3685 -0.0247 0.0153  -0.0535 334 TYR A CE2 
2744 C CZ  . TYR A 344 ? 0.3417 0.3683 0.3774 -0.0252 0.0167  -0.0576 334 TYR A CZ  
2745 O OH  . TYR A 344 ? 0.3620 0.3872 0.4010 -0.0242 0.0174  -0.0593 334 TYR A OH  
2746 N N   . LEU A 345 ? 0.2866 0.3050 0.3106 -0.0234 0.0127  -0.0470 335 LEU A N   
2747 C CA  . LEU A 345 ? 0.2870 0.3002 0.3121 -0.0222 0.0127  -0.0451 335 LEU A CA  
2748 C C   . LEU A 345 ? 0.2876 0.2983 0.3145 -0.0221 0.0134  -0.0451 335 LEU A C   
2749 O O   . LEU A 345 ? 0.3047 0.3119 0.3345 -0.0220 0.0142  -0.0452 335 LEU A O   
2750 C CB  . LEU A 345 ? 0.2927 0.3034 0.3139 -0.0211 0.0109  -0.0416 335 LEU A CB  
2751 C CG  . LEU A 345 ? 0.2924 0.3044 0.3117 -0.0216 0.0101  -0.0409 335 LEU A CG  
2752 C CD1 . LEU A 345 ? 0.2908 0.3001 0.3053 -0.0208 0.0081  -0.0375 335 LEU A CD1 
2753 C CD2 . LEU A 345 ? 0.3011 0.3124 0.3235 -0.0216 0.0111  -0.0415 335 LEU A CD2 
2754 N N   . MET A 346 ? 0.2855 0.2983 0.3108 -0.0222 0.0131  -0.0450 336 MET A N   
2755 C CA  . MET A 346 ? 0.2860 0.2974 0.3125 -0.0225 0.0136  -0.0449 336 MET A CA  
2756 C C   . MET A 346 ? 0.2985 0.3114 0.3283 -0.0245 0.0152  -0.0479 336 MET A C   
2757 O O   . MET A 346 ? 0.2971 0.3072 0.3289 -0.0252 0.0159  -0.0477 336 MET A O   
2758 C CB  . MET A 346 ? 0.2786 0.2922 0.3019 -0.0215 0.0125  -0.0435 336 MET A CB  
2759 C CG  . MET A 346 ? 0.2758 0.2867 0.2956 -0.0194 0.0107  -0.0405 336 MET A CG  
2760 S SD  . MET A 346 ? 0.2788 0.2841 0.2998 -0.0186 0.0107  -0.0380 336 MET A SD  
2761 C CE  . MET A 346 ? 0.2844 0.2870 0.3065 -0.0187 0.0109  -0.0377 336 MET A CE  
2762 N N   . ARG A 347 ? 0.2986 0.3158 0.3289 -0.0256 0.0158  -0.0506 337 ARG A N   
2763 C CA  . ARG A 347 ? 0.3143 0.3332 0.3476 -0.0276 0.0172  -0.0539 337 ARG A CA  
2764 C C   . ARG A 347 ? 0.3308 0.3466 0.3676 -0.0281 0.0182  -0.0560 337 ARG A C   
2765 O O   . ARG A 347 ? 0.3250 0.3382 0.3643 -0.0295 0.0191  -0.0575 337 ARG A O   
2766 C CB  . ARG A 347 ? 0.3146 0.3402 0.3468 -0.0286 0.0173  -0.0563 337 ARG A CB  
2767 C CG  . ARG A 347 ? 0.3210 0.3491 0.3560 -0.0310 0.0188  -0.0601 337 ARG A CG  
2768 C CD  . ARG A 347 ? 0.3303 0.3571 0.3662 -0.0324 0.0193  -0.0600 337 ARG A CD  
2769 N NE  . ARG A 347 ? 0.3355 0.3639 0.3740 -0.0350 0.0206  -0.0637 337 ARG A NE  
2770 C CZ  . ARG A 347 ? 0.3569 0.3805 0.3984 -0.0361 0.0215  -0.0655 337 ARG A CZ  
2771 N NH1 . ARG A 347 ? 0.3534 0.3707 0.3961 -0.0346 0.0212  -0.0640 337 ARG A NH1 
2772 N NH2 . ARG A 347 ? 0.3658 0.3910 0.4091 -0.0386 0.0225  -0.0691 337 ARG A NH2 
2773 N N   . GLU A 348 ? 0.3567 0.3728 0.3935 -0.0271 0.0179  -0.0562 338 GLU A N   
2774 C CA  . GLU A 348 ? 0.3841 0.3988 0.4243 -0.0272 0.0188  -0.0590 338 GLU A CA  
2775 C C   . GLU A 348 ? 0.3932 0.4013 0.4353 -0.0259 0.0187  -0.0574 338 GLU A C   
2776 O O   . GLU A 348 ? 0.4069 0.4124 0.4521 -0.0259 0.0194  -0.0598 338 GLU A O   
2777 C CB  . GLU A 348 ? 0.4064 0.4257 0.4461 -0.0268 0.0186  -0.0602 338 GLU A CB  
2778 C CG  . GLU A 348 ? 0.4298 0.4504 0.4730 -0.0270 0.0196  -0.0643 338 GLU A CG  
2779 C CD  . GLU A 348 ? 0.4574 0.4809 0.5023 -0.0288 0.0207  -0.0682 338 GLU A CD  
2780 O OE1 . GLU A 348 ? 0.4801 0.5036 0.5281 -0.0289 0.0214  -0.0719 338 GLU A OE1 
2781 O OE2 . GLU A 348 ? 0.4707 0.4967 0.5140 -0.0302 0.0207  -0.0679 338 GLU A OE2 
2782 N N   . LEU A 349 ? 0.3931 0.3983 0.4332 -0.0248 0.0178  -0.0536 339 LEU A N   
2783 C CA  . LEU A 349 ? 0.4052 0.4049 0.4466 -0.0233 0.0175  -0.0517 339 LEU A CA  
2784 C C   . LEU A 349 ? 0.4110 0.4066 0.4519 -0.0235 0.0173  -0.0489 339 LEU A C   
2785 O O   . LEU A 349 ? 0.4090 0.4046 0.4473 -0.0227 0.0164  -0.0458 339 LEU A O   
2786 C CB  . LEU A 349 ? 0.4189 0.4197 0.4584 -0.0217 0.0166  -0.0496 339 LEU A CB  
2787 C CG  . LEU A 349 ? 0.4309 0.4366 0.4705 -0.0218 0.0168  -0.0520 339 LEU A CG  
2788 C CD1 . LEU A 349 ? 0.4359 0.4437 0.4722 -0.0212 0.0157  -0.0494 339 LEU A CD1 
2789 C CD2 . LEU A 349 ? 0.4358 0.4404 0.4792 -0.0209 0.0175  -0.0545 339 LEU A CD2 
2790 N N   . PRO A 350 ? 0.4075 0.3997 0.4507 -0.0248 0.0179  -0.0499 340 PRO A N   
2791 C CA  . PRO A 350 ? 0.4050 0.3935 0.4476 -0.0254 0.0176  -0.0470 340 PRO A CA  
2792 C C   . PRO A 350 ? 0.3981 0.3825 0.4406 -0.0234 0.0169  -0.0438 340 PRO A C   
2793 O O   . PRO A 350 ? 0.3866 0.3691 0.4308 -0.0219 0.0168  -0.0445 340 PRO A O   
2794 C CB  . PRO A 350 ? 0.4175 0.4023 0.4627 -0.0274 0.0183  -0.0490 340 PRO A CB  
2795 C CG  . PRO A 350 ? 0.4254 0.4133 0.4720 -0.0281 0.0191  -0.0533 340 PRO A CG  
2796 C CD  . PRO A 350 ? 0.4176 0.4088 0.4637 -0.0259 0.0188  -0.0537 340 PRO A CD  
2797 N N   . PHE A 351 ? 0.3935 0.3773 0.4342 -0.0233 0.0163  -0.0406 341 PHE A N   
2798 C CA  . PHE A 351 ? 0.3914 0.3722 0.4316 -0.0215 0.0155  -0.0374 341 PHE A CA  
2799 C C   . PHE A 351 ? 0.4088 0.3835 0.4516 -0.0213 0.0156  -0.0366 341 PHE A C   
2800 O O   . PHE A 351 ? 0.3991 0.3716 0.4422 -0.0194 0.0150  -0.0348 341 PHE A O   
2801 C CB  . PHE A 351 ? 0.3871 0.3691 0.4246 -0.0216 0.0149  -0.0344 341 PHE A CB  
2802 C CG  . PHE A 351 ? 0.3717 0.3588 0.4061 -0.0211 0.0144  -0.0347 341 PHE A CG  
2803 C CD1 . PHE A 351 ? 0.3657 0.3547 0.3989 -0.0198 0.0140  -0.0354 341 PHE A CD1 
2804 C CD2 . PHE A 351 ? 0.3722 0.3624 0.4049 -0.0220 0.0143  -0.0343 341 PHE A CD2 
2805 C CE1 . PHE A 351 ? 0.3610 0.3537 0.3911 -0.0194 0.0132  -0.0354 341 PHE A CE1 
2806 C CE2 . PHE A 351 ? 0.3706 0.3651 0.4005 -0.0211 0.0136  -0.0346 341 PHE A CE2 
2807 C CZ  . PHE A 351 ? 0.3667 0.3620 0.3952 -0.0198 0.0129  -0.0351 341 PHE A CZ  
2808 N N   . GLY A 352 ? 0.4355 0.4074 0.4800 -0.0232 0.0161  -0.0380 342 GLY A N   
2809 C CA  . GLY A 352 ? 0.4548 0.4200 0.5016 -0.0231 0.0159  -0.0373 342 GLY A CA  
2810 C C   . GLY A 352 ? 0.4724 0.4352 0.5218 -0.0214 0.0159  -0.0403 342 GLY A C   
2811 O O   . GLY A 352 ? 0.4867 0.4434 0.5380 -0.0209 0.0155  -0.0400 342 GLY A O   
2812 N N   . SER A 353 ? 0.4721 0.4398 0.5217 -0.0204 0.0163  -0.0430 343 SER A N   
2813 C CA  . SER A 353 ? 0.4849 0.4521 0.5370 -0.0188 0.0165  -0.0464 343 SER A CA  
2814 C C   . SER A 353 ? 0.4621 0.4344 0.5134 -0.0168 0.0164  -0.0466 343 SER A C   
2815 O O   . SER A 353 ? 0.4296 0.4061 0.4782 -0.0172 0.0162  -0.0449 343 SER A O   
2816 C CB  . SER A 353 ? 0.4954 0.4643 0.5486 -0.0205 0.0173  -0.0506 343 SER A CB  
2817 O OG  . SER A 353 ? 0.5324 0.4968 0.5860 -0.0230 0.0174  -0.0506 343 SER A OG  
2818 N N   . ASP A 354 ? 0.4613 0.4333 0.5150 -0.0146 0.0163  -0.0487 344 ASP A N   
2819 C CA  . ASP A 354 ? 0.4674 0.4454 0.5208 -0.0133 0.0163  -0.0500 344 ASP A CA  
2820 C C   . ASP A 354 ? 0.4803 0.4628 0.5345 -0.0145 0.0171  -0.0544 344 ASP A C   
2821 O O   . ASP A 354 ? 0.4988 0.4786 0.5553 -0.0150 0.0175  -0.0573 344 ASP A O   
2822 C CB  . ASP A 354 ? 0.4719 0.4486 0.5276 -0.0104 0.0158  -0.0504 344 ASP A CB  
2823 C CG  . ASP A 354 ? 0.4798 0.4528 0.5347 -0.0091 0.0150  -0.0461 344 ASP A CG  
2824 O OD1 . ASP A 354 ? 0.4724 0.4447 0.5247 -0.0105 0.0148  -0.0427 344 ASP A OD1 
2825 O OD2 . ASP A 354 ? 0.4831 0.4542 0.5400 -0.0066 0.0145  -0.0462 344 ASP A OD2 
2826 N N   . GLY A 355 ? 0.4641 0.4533 0.5163 -0.0152 0.0173  -0.0548 345 GLY A N   
2827 C CA  . GLY A 355 ? 0.4630 0.4576 0.5156 -0.0165 0.0180  -0.0586 345 GLY A CA  
2828 C C   . GLY A 355 ? 0.4541 0.4556 0.5063 -0.0159 0.0180  -0.0600 345 GLY A C   
2829 O O   . GLY A 355 ? 0.4378 0.4410 0.4878 -0.0154 0.0174  -0.0571 345 GLY A O   
2830 N N   . VAL A 356 ? 0.4425 0.4483 0.4968 -0.0160 0.0187  -0.0644 346 VAL A N   
2831 C CA  . VAL A 356 ? 0.4451 0.4588 0.4990 -0.0159 0.0187  -0.0662 346 VAL A CA  
2832 C C   . VAL A 356 ? 0.4317 0.4512 0.4825 -0.0184 0.0188  -0.0658 346 VAL A C   
2833 O O   . VAL A 356 ? 0.4435 0.4638 0.4945 -0.0199 0.0194  -0.0679 346 VAL A O   
2834 C CB  . VAL A 356 ? 0.4592 0.4755 0.5170 -0.0145 0.0194  -0.0716 346 VAL A CB  
2835 C CG1 . VAL A 356 ? 0.4625 0.4881 0.5200 -0.0145 0.0195  -0.0733 346 VAL A CG1 
2836 C CG2 . VAL A 356 ? 0.4697 0.4795 0.5305 -0.0116 0.0190  -0.0720 346 VAL A CG2 
2837 N N   . PHE A 357 ? 0.4201 0.4435 0.4679 -0.0190 0.0182  -0.0632 347 PHE A N   
2838 C CA  . PHE A 357 ? 0.4080 0.4372 0.4526 -0.0213 0.0180  -0.0630 347 PHE A CA  
2839 C C   . PHE A 357 ? 0.4210 0.4580 0.4674 -0.0219 0.0187  -0.0674 347 PHE A C   
2840 O O   . PHE A 357 ? 0.4128 0.4529 0.4612 -0.0206 0.0189  -0.0691 347 PHE A O   
2841 C CB  . PHE A 357 ? 0.4042 0.4347 0.4447 -0.0219 0.0168  -0.0589 347 PHE A CB  
2842 C CG  . PHE A 357 ? 0.3948 0.4310 0.4317 -0.0242 0.0163  -0.0584 347 PHE A CG  
2843 C CD1 . PHE A 357 ? 0.3971 0.4313 0.4310 -0.0251 0.0156  -0.0563 347 PHE A CD1 
2844 C CD2 . PHE A 357 ? 0.3952 0.4392 0.4319 -0.0254 0.0163  -0.0600 347 PHE A CD2 
2845 C CE1 . PHE A 357 ? 0.3891 0.4281 0.4195 -0.0271 0.0149  -0.0557 347 PHE A CE1 
2846 C CE2 . PHE A 357 ? 0.3940 0.4429 0.4271 -0.0278 0.0157  -0.0593 347 PHE A CE2 
2847 C CZ  . PHE A 357 ? 0.3963 0.4424 0.4263 -0.0285 0.0149  -0.0570 347 PHE A CZ  
2848 N N   . THR A 358 ? 0.4246 0.4656 0.4704 -0.0237 0.0192  -0.0693 348 THR A N   
2849 C CA  . THR A 358 ? 0.4436 0.4937 0.4899 -0.0249 0.0197  -0.0728 348 THR A CA  
2850 C C   . THR A 358 ? 0.4395 0.4938 0.4818 -0.0275 0.0192  -0.0712 348 THR A C   
2851 O O   . THR A 358 ? 0.4279 0.4787 0.4688 -0.0280 0.0190  -0.0697 348 THR A O   
2852 C CB  . THR A 358 ? 0.4590 0.5106 0.5096 -0.0244 0.0209  -0.0785 348 THR A CB  
2853 O OG1 . THR A 358 ? 0.4533 0.5037 0.5034 -0.0260 0.0213  -0.0793 348 THR A OG1 
2854 C CG2 . THR A 358 ? 0.4714 0.5163 0.5257 -0.0216 0.0211  -0.0799 348 THR A CG2 
2855 N N   . PRO A 359 ? 0.4521 0.5144 0.4925 -0.0291 0.0188  -0.0713 349 PRO A N   
2856 C CA  . PRO A 359 ? 0.4542 0.5206 0.4907 -0.0315 0.0182  -0.0698 349 PRO A CA  
2857 C C   . PRO A 359 ? 0.4598 0.5288 0.4978 -0.0324 0.0191  -0.0732 349 PRO A C   
2858 O O   . PRO A 359 ? 0.4439 0.5131 0.4789 -0.0335 0.0185  -0.0713 349 PRO A O   
2859 C CB  . PRO A 359 ? 0.4576 0.5327 0.4925 -0.0333 0.0178  -0.0700 349 PRO A CB  
2860 C CG  . PRO A 359 ? 0.4617 0.5388 0.5004 -0.0317 0.0186  -0.0728 349 PRO A CG  
2861 C CD  . PRO A 359 ? 0.4583 0.5262 0.4997 -0.0289 0.0188  -0.0724 349 PRO A CD  
2862 N N   . GLU A 360 ? 0.4822 0.5530 0.5247 -0.0316 0.0205  -0.0781 350 GLU A N   
2863 C CA  . GLU A 360 ? 0.4980 0.5712 0.5422 -0.0326 0.0215  -0.0819 350 GLU A CA  
2864 C C   . GLU A 360 ? 0.4762 0.5419 0.5201 -0.0323 0.0215  -0.0803 350 GLU A C   
2865 O O   . GLU A 360 ? 0.4754 0.5434 0.5180 -0.0338 0.0216  -0.0806 350 GLU A O   
2866 C CB  . GLU A 360 ? 0.5229 0.5986 0.5719 -0.0317 0.0228  -0.0878 350 GLU A CB  
2867 C CG  . GLU A 360 ? 0.5487 0.6346 0.5984 -0.0323 0.0230  -0.0905 350 GLU A CG  
2868 C CD  . GLU A 360 ? 0.5746 0.6608 0.6241 -0.0309 0.0224  -0.0888 350 GLU A CD  
2869 O OE1 . GLU A 360 ? 0.5769 0.6550 0.6272 -0.0289 0.0221  -0.0866 350 GLU A OE1 
2870 O OE2 . GLU A 360 ? 0.5950 0.6902 0.6437 -0.0321 0.0223  -0.0895 350 GLU A OE2 
2871 N N   . ALA A 361 ? 0.4506 0.5080 0.4957 -0.0305 0.0213  -0.0786 351 ALA A N   
2872 C CA  . ALA A 361 ? 0.4338 0.4842 0.4784 -0.0303 0.0212  -0.0767 351 ALA A CA  
2873 C C   . ALA A 361 ? 0.4088 0.4589 0.4489 -0.0309 0.0200  -0.0721 351 ALA A C   
2874 O O   . ALA A 361 ? 0.4052 0.4547 0.4444 -0.0316 0.0200  -0.0717 351 ALA A O   
2875 C CB  . ALA A 361 ? 0.4415 0.4837 0.4882 -0.0283 0.0212  -0.0756 351 ALA A CB  
2876 N N   . PHE A 362 ? 0.3835 0.4342 0.4207 -0.0305 0.0188  -0.0688 352 PHE A N   
2877 C CA  . PHE A 362 ? 0.3653 0.4157 0.3978 -0.0309 0.0173  -0.0647 352 PHE A CA  
2878 C C   . PHE A 362 ? 0.3673 0.4240 0.3976 -0.0325 0.0171  -0.0656 352 PHE A C   
2879 O O   . PHE A 362 ? 0.3483 0.4040 0.3764 -0.0325 0.0164  -0.0640 352 PHE A O   
2880 C CB  . PHE A 362 ? 0.3542 0.4046 0.3838 -0.0307 0.0161  -0.0615 352 PHE A CB  
2881 C CG  . PHE A 362 ? 0.3397 0.3877 0.3642 -0.0307 0.0142  -0.0571 352 PHE A CG  
2882 C CD1 . PHE A 362 ? 0.3366 0.3775 0.3599 -0.0291 0.0133  -0.0539 352 PHE A CD1 
2883 C CD2 . PHE A 362 ? 0.3377 0.3902 0.3587 -0.0321 0.0131  -0.0562 352 PHE A CD2 
2884 C CE1 . PHE A 362 ? 0.3374 0.3758 0.3560 -0.0288 0.0115  -0.0502 352 PHE A CE1 
2885 C CE2 . PHE A 362 ? 0.3447 0.3941 0.3608 -0.0317 0.0111  -0.0523 352 PHE A CE2 
2886 C CZ  . PHE A 362 ? 0.3384 0.3807 0.3534 -0.0300 0.0103  -0.0494 352 PHE A CZ  
2887 N N   . VAL A 363 ? 0.3595 0.4235 0.3907 -0.0339 0.0176  -0.0683 353 VAL A N   
2888 C CA  . VAL A 363 ? 0.3804 0.4513 0.4096 -0.0357 0.0175  -0.0694 353 VAL A CA  
2889 C C   . VAL A 363 ? 0.3796 0.4513 0.4109 -0.0361 0.0185  -0.0722 353 VAL A C   
2890 O O   . VAL A 363 ? 0.3679 0.4420 0.3967 -0.0366 0.0179  -0.0711 353 VAL A O   
2891 C CB  . VAL A 363 ? 0.3849 0.4643 0.4149 -0.0373 0.0180  -0.0720 353 VAL A CB  
2892 C CG1 . VAL A 363 ? 0.4002 0.4874 0.4290 -0.0392 0.0180  -0.0737 353 VAL A CG1 
2893 C CG2 . VAL A 363 ? 0.4012 0.4812 0.4280 -0.0378 0.0166  -0.0685 353 VAL A CG2 
2894 N N   . GLU A 364 ? 0.4056 0.4755 0.4414 -0.0358 0.0201  -0.0759 354 GLU A N   
2895 C CA  . GLU A 364 ? 0.4347 0.5051 0.4725 -0.0367 0.0212  -0.0789 354 GLU A CA  
2896 C C   . GLU A 364 ? 0.4237 0.4889 0.4598 -0.0360 0.0205  -0.0757 354 GLU A C   
2897 O O   . GLU A 364 ? 0.4010 0.4693 0.4358 -0.0369 0.0204  -0.0760 354 GLU A O   
2898 C CB  . GLU A 364 ? 0.4808 0.5487 0.5235 -0.0365 0.0226  -0.0832 354 GLU A CB  
2899 C CG  . GLU A 364 ? 0.5167 0.5917 0.5617 -0.0373 0.0236  -0.0879 354 GLU A CG  
2900 C CD  . GLU A 364 ? 0.5544 0.6279 0.6036 -0.0377 0.0250  -0.0932 354 GLU A CD  
2901 O OE1 . GLU A 364 ? 0.5919 0.6724 0.6426 -0.0390 0.0258  -0.0976 354 GLU A OE1 
2902 O OE2 . GLU A 364 ? 0.5779 0.6433 0.6288 -0.0369 0.0251  -0.0930 354 GLU A OE2 
2903 N N   . ARG A 365 ? 0.4148 0.4727 0.4507 -0.0344 0.0200  -0.0728 355 ARG A N   
2904 C CA  . ARG A 365 ? 0.4165 0.4697 0.4512 -0.0336 0.0195  -0.0701 355 ARG A CA  
2905 C C   . ARG A 365 ? 0.4165 0.4728 0.4468 -0.0334 0.0180  -0.0674 355 ARG A C   
2906 O O   . ARG A 365 ? 0.4288 0.4866 0.4584 -0.0337 0.0180  -0.0675 355 ARG A O   
2907 C CB  . ARG A 365 ? 0.4163 0.4618 0.4513 -0.0319 0.0190  -0.0674 355 ARG A CB  
2908 C CG  . ARG A 365 ? 0.4124 0.4532 0.4463 -0.0311 0.0185  -0.0647 355 ARG A CG  
2909 C CD  . ARG A 365 ? 0.4084 0.4492 0.4445 -0.0326 0.0197  -0.0670 355 ARG A CD  
2910 N NE  . ARG A 365 ? 0.4035 0.4394 0.4433 -0.0330 0.0208  -0.0690 355 ARG A NE  
2911 C CZ  . ARG A 365 ? 0.4087 0.4435 0.4507 -0.0347 0.0217  -0.0713 355 ARG A CZ  
2912 N NH1 . ARG A 365 ? 0.4048 0.4440 0.4459 -0.0364 0.0220  -0.0722 355 ARG A NH1 
2913 N NH2 . ARG A 365 ? 0.4177 0.4467 0.4627 -0.0349 0.0224  -0.0728 355 ARG A NH2 
2914 N N   . THR A 366 ? 0.4112 0.4689 0.4384 -0.0329 0.0167  -0.0650 356 THR A N   
2915 C CA  . THR A 366 ? 0.4232 0.4825 0.4457 -0.0323 0.0148  -0.0621 356 THR A CA  
2916 C C   . THR A 366 ? 0.4266 0.4938 0.4480 -0.0337 0.0148  -0.0639 356 THR A C   
2917 O O   . THR A 366 ? 0.4334 0.5021 0.4521 -0.0330 0.0137  -0.0625 356 THR A O   
2918 C CB  . THR A 366 ? 0.4429 0.4994 0.4620 -0.0315 0.0131  -0.0584 356 THR A CB  
2919 O OG1 . THR A 366 ? 0.4336 0.4945 0.4533 -0.0331 0.0135  -0.0598 356 THR A OG1 
2920 C CG2 . THR A 366 ? 0.4464 0.4953 0.4665 -0.0300 0.0130  -0.0564 356 THR A CG2 
2921 N N   . ASN A 367 ? 0.3963 0.4691 0.4198 -0.0355 0.0160  -0.0671 357 ASN A N   
2922 C CA  . ASN A 367 ? 0.3997 0.4806 0.4225 -0.0370 0.0161  -0.0692 357 ASN A CA  
2923 C C   . ASN A 367 ? 0.3750 0.4578 0.4003 -0.0376 0.0174  -0.0721 357 ASN A C   
2924 O O   . ASN A 367 ? 0.3832 0.4704 0.4064 -0.0377 0.0168  -0.0719 357 ASN A O   
2925 C CB  . ASN A 367 ? 0.4081 0.4953 0.4324 -0.0389 0.0170  -0.0721 357 ASN A CB  
2926 C CG  . ASN A 367 ? 0.4274 0.5168 0.4476 -0.0393 0.0152  -0.0689 357 ASN A CG  
2927 O OD1 . ASN A 367 ? 0.4416 0.5286 0.4617 -0.0392 0.0150  -0.0677 357 ASN A OD1 
2928 N ND2 . ASN A 367 ? 0.4427 0.5367 0.4593 -0.0398 0.0139  -0.0674 357 ASN A ND2 
2929 N N   . PHE A 368 ? 0.3588 0.4384 0.3881 -0.0381 0.0191  -0.0749 358 PHE A N   
2930 C CA  . PHE A 368 ? 0.3510 0.4324 0.3827 -0.0395 0.0204  -0.0780 358 PHE A CA  
2931 C C   . PHE A 368 ? 0.3406 0.4193 0.3708 -0.0385 0.0198  -0.0755 358 PHE A C   
2932 O O   . PHE A 368 ? 0.3264 0.4100 0.3562 -0.0393 0.0200  -0.0767 358 PHE A O   
2933 C CB  . PHE A 368 ? 0.3585 0.4363 0.3948 -0.0404 0.0221  -0.0815 358 PHE A CB  
2934 C CG  . PHE A 368 ? 0.3571 0.4384 0.3955 -0.0412 0.0230  -0.0849 358 PHE A CG  
2935 C CD1 . PHE A 368 ? 0.3562 0.4450 0.3927 -0.0418 0.0225  -0.0851 358 PHE A CD1 
2936 C CD2 . PHE A 368 ? 0.3683 0.4455 0.4106 -0.0413 0.0241  -0.0880 358 PHE A CD2 
2937 C CE1 . PHE A 368 ? 0.3592 0.4522 0.3979 -0.0425 0.0233  -0.0884 358 PHE A CE1 
2938 C CE2 . PHE A 368 ? 0.3674 0.4483 0.4119 -0.0417 0.0248  -0.0916 358 PHE A CE2 
2939 C CZ  . PHE A 368 ? 0.3628 0.4521 0.4055 -0.0423 0.0245  -0.0919 358 PHE A CZ  
2940 N N   . ASP A 369 ? 0.3329 0.4044 0.3623 -0.0367 0.0190  -0.0723 359 ASP A N   
2941 C CA  . ASP A 369 ? 0.3297 0.3988 0.3578 -0.0356 0.0184  -0.0702 359 ASP A CA  
2942 C C   . ASP A 369 ? 0.3176 0.3891 0.3413 -0.0336 0.0164  -0.0671 359 ASP A C   
2943 O O   . ASP A 369 ? 0.3207 0.3955 0.3433 -0.0333 0.0160  -0.0671 359 ASP A O   
2944 C CB  . ASP A 369 ? 0.3412 0.4019 0.3704 -0.0345 0.0184  -0.0681 359 ASP A CB  
2945 C CG  . ASP A 369 ? 0.3607 0.4180 0.3941 -0.0362 0.0201  -0.0708 359 ASP A CG  
2946 O OD1 . ASP A 369 ? 0.3800 0.4412 0.4155 -0.0384 0.0214  -0.0745 359 ASP A OD1 
2947 O OD2 . ASP A 369 ? 0.3609 0.4114 0.3953 -0.0354 0.0202  -0.0692 359 ASP A OD2 
2948 N N   . LEU A 370 ? 0.2993 0.3688 0.3203 -0.0323 0.0149  -0.0645 360 LEU A N   
2949 C CA  . LEU A 370 ? 0.2985 0.3684 0.3147 -0.0301 0.0125  -0.0612 360 LEU A CA  
2950 C C   . LEU A 370 ? 0.3066 0.3841 0.3207 -0.0307 0.0118  -0.0621 360 LEU A C   
2951 O O   . LEU A 370 ? 0.3006 0.3823 0.3137 -0.0301 0.0113  -0.0625 360 LEU A O   
2952 C CB  . LEU A 370 ? 0.2964 0.3602 0.3100 -0.0286 0.0109  -0.0577 360 LEU A CB  
2953 C CG  . LEU A 370 ? 0.2944 0.3510 0.3097 -0.0278 0.0114  -0.0565 360 LEU A CG  
2954 C CD1 . LEU A 370 ? 0.2939 0.3454 0.3066 -0.0267 0.0099  -0.0533 360 LEU A CD1 
2955 C CD2 . LEU A 370 ? 0.2968 0.3517 0.3120 -0.0263 0.0111  -0.0557 360 LEU A CD2 
2956 N N   . ALA A 371 ? 0.3106 0.3905 0.3243 -0.0321 0.0117  -0.0625 361 ALA A N   
2957 C CA  . ALA A 371 ? 0.3251 0.4123 0.3364 -0.0328 0.0108  -0.0628 361 ALA A CA  
2958 C C   . ALA A 371 ? 0.3298 0.4244 0.3436 -0.0344 0.0124  -0.0667 361 ALA A C   
2959 O O   . ALA A 371 ? 0.3315 0.4312 0.3431 -0.0337 0.0115  -0.0665 361 ALA A O   
2960 C CB  . ALA A 371 ? 0.3257 0.4147 0.3363 -0.0345 0.0107  -0.0627 361 ALA A CB  
2961 N N   . ASN A 372 ? 0.3300 0.4250 0.3484 -0.0364 0.0148  -0.0703 362 ASN A N   
2962 C CA  . ASN A 372 ? 0.3401 0.4421 0.3610 -0.0385 0.0165  -0.0744 362 ASN A CA  
2963 C C   . ASN A 372 ? 0.3534 0.4556 0.3749 -0.0380 0.0168  -0.0748 362 ASN A C   
2964 O O   . ASN A 372 ? 0.3819 0.4904 0.4019 -0.0378 0.0162  -0.0751 362 ASN A O   
2965 C CB  . ASN A 372 ? 0.3328 0.4349 0.3581 -0.0408 0.0187  -0.0783 362 ASN A CB  
2966 C CG  . ASN A 372 ? 0.3395 0.4448 0.3644 -0.0416 0.0185  -0.0788 362 ASN A CG  
2967 O OD1 . ASN A 372 ? 0.3369 0.4440 0.3580 -0.0409 0.0167  -0.0758 362 ASN A OD1 
2968 N ND2 . ASN A 372 ? 0.3302 0.4360 0.3588 -0.0432 0.0203  -0.0826 362 ASN A ND2 
2969 N N   . ASP A 373 ? 0.3387 0.4343 0.3623 -0.0379 0.0176  -0.0746 363 ASP A N   
2970 C CA  . ASP A 373 ? 0.3418 0.4384 0.3665 -0.0383 0.0183  -0.0754 363 ASP A CA  
2971 C C   . ASP A 373 ? 0.3307 0.4285 0.3517 -0.0355 0.0163  -0.0723 363 ASP A C   
2972 O O   . ASP A 373 ? 0.3152 0.4201 0.3353 -0.0355 0.0160  -0.0733 363 ASP A O   
2973 C CB  . ASP A 373 ? 0.3642 0.4531 0.3918 -0.0391 0.0194  -0.0756 363 ASP A CB  
2974 C CG  . ASP A 373 ? 0.3924 0.4833 0.4224 -0.0417 0.0210  -0.0783 363 ASP A CG  
2975 O OD1 . ASP A 373 ? 0.4242 0.5226 0.4535 -0.0424 0.0210  -0.0795 363 ASP A OD1 
2976 O OD2 . ASP A 373 ? 0.4127 0.4977 0.4454 -0.0431 0.0221  -0.0791 363 ASP A OD2 
2977 N N   . LEU A 374 ? 0.3091 0.4003 0.3279 -0.0328 0.0148  -0.0688 364 LEU A N   
2978 C CA  . LEU A 374 ? 0.3119 0.4035 0.3272 -0.0297 0.0127  -0.0661 364 LEU A CA  
2979 C C   . LEU A 374 ? 0.3109 0.4069 0.3224 -0.0280 0.0106  -0.0649 364 LEU A C   
2980 O O   . LEU A 374 ? 0.3124 0.4137 0.3220 -0.0263 0.0095  -0.0648 364 LEU A O   
2981 C CB  . LEU A 374 ? 0.3148 0.3978 0.3289 -0.0274 0.0116  -0.0628 364 LEU A CB  
2982 C CG  . LEU A 374 ? 0.3182 0.4009 0.3288 -0.0238 0.0094  -0.0603 364 LEU A CG  
2983 C CD1 . LEU A 374 ? 0.3205 0.4096 0.3318 -0.0237 0.0099  -0.0620 364 LEU A CD1 
2984 C CD2 . LEU A 374 ? 0.3223 0.3964 0.3323 -0.0222 0.0087  -0.0576 364 LEU A CD2 
2985 N N   . GLY A 375 ? 0.3158 0.4100 0.3260 -0.0284 0.0100  -0.0638 365 GLY A N   
2986 C CA  . GLY A 375 ? 0.3177 0.4150 0.3237 -0.0271 0.0077  -0.0620 365 GLY A CA  
2987 C C   . GLY A 375 ? 0.3192 0.4265 0.3254 -0.0282 0.0081  -0.0645 365 GLY A C   
2988 O O   . GLY A 375 ? 0.3174 0.4282 0.3203 -0.0259 0.0061  -0.0632 365 GLY A O   
2989 N N   . ASN A 376 ? 0.3213 0.4331 0.3313 -0.0315 0.0106  -0.0682 366 ASN A N   
2990 C CA  . ASN A 376 ? 0.3283 0.4502 0.3388 -0.0329 0.0112  -0.0710 366 ASN A CA  
2991 C C   . ASN A 376 ? 0.3248 0.4508 0.3358 -0.0320 0.0114  -0.0721 366 ASN A C   
2992 O O   . ASN A 376 ? 0.3191 0.4531 0.3285 -0.0314 0.0106  -0.0727 366 ASN A O   
2993 C CB  . ASN A 376 ? 0.3309 0.4566 0.3455 -0.0368 0.0138  -0.0751 366 ASN A CB  
2994 C CG  . ASN A 376 ? 0.3343 0.4597 0.3482 -0.0379 0.0136  -0.0747 366 ASN A CG  
2995 O OD1 . ASN A 376 ? 0.3475 0.4734 0.3575 -0.0366 0.0115  -0.0717 366 ASN A OD1 
2996 N ND2 . ASN A 376 ? 0.3226 0.4474 0.3403 -0.0404 0.0157  -0.0777 366 ASN A ND2 
2997 N N   . LEU A 377 ? 0.3261 0.4475 0.3392 -0.0319 0.0124  -0.0722 367 LEU A N   
2998 C CA  . LEU A 377 ? 0.3320 0.4578 0.3452 -0.0312 0.0125  -0.0730 367 LEU A CA  
2999 C C   . LEU A 377 ? 0.3370 0.4652 0.3460 -0.0269 0.0096  -0.0705 367 LEU A C   
3000 O O   . LEU A 377 ? 0.3354 0.4720 0.3436 -0.0262 0.0092  -0.0718 367 LEU A O   
3001 C CB  . LEU A 377 ? 0.3304 0.4502 0.3459 -0.0317 0.0136  -0.0728 367 LEU A CB  
3002 C CG  . LEU A 377 ? 0.3399 0.4640 0.3551 -0.0306 0.0134  -0.0730 367 LEU A CG  
3003 C CD1 . LEU A 377 ? 0.3378 0.4722 0.3545 -0.0333 0.0147  -0.0765 367 LEU A CD1 
3004 C CD2 . LEU A 377 ? 0.3351 0.4526 0.3523 -0.0314 0.0144  -0.0722 367 LEU A CD2 
3005 N N   . VAL A 378 ? 0.3418 0.4624 0.3477 -0.0239 0.0075  -0.0669 368 VAL A N   
3006 C CA  . VAL A 378 ? 0.3557 0.4766 0.3572 -0.0194 0.0044  -0.0644 368 VAL A CA  
3007 C C   . VAL A 378 ? 0.3688 0.4960 0.3676 -0.0188 0.0029  -0.0643 368 VAL A C   
3008 O O   . VAL A 378 ? 0.3816 0.5152 0.3784 -0.0163 0.0014  -0.0645 368 VAL A O   
3009 C CB  . VAL A 378 ? 0.3560 0.4664 0.3547 -0.0167 0.0024  -0.0607 368 VAL A CB  
3010 C CG1 . VAL A 378 ? 0.3575 0.4675 0.3513 -0.0118 -0.0010 -0.0583 368 VAL A CG1 
3011 C CG2 . VAL A 378 ? 0.3582 0.4633 0.3595 -0.0169 0.0038  -0.0608 368 VAL A CG2 
3012 N N   . ASN A 379 ? 0.3700 0.4962 0.3687 -0.0212 0.0032  -0.0641 369 ASN A N   
3013 C CA  . ASN A 379 ? 0.3851 0.5172 0.3809 -0.0210 0.0017  -0.0636 369 ASN A CA  
3014 C C   . ASN A 379 ? 0.3731 0.5169 0.3710 -0.0227 0.0031  -0.0671 369 ASN A C   
3015 O O   . ASN A 379 ? 0.3697 0.5196 0.3648 -0.0206 0.0012  -0.0666 369 ASN A O   
3016 C CB  . ASN A 379 ? 0.4017 0.5314 0.3971 -0.0236 0.0019  -0.0626 369 ASN A CB  
3017 C CG  . ASN A 379 ? 0.4288 0.5614 0.4195 -0.0225 -0.0008 -0.0603 369 ASN A CG  
3018 O OD1 . ASN A 379 ? 0.4622 0.5895 0.4483 -0.0191 -0.0039 -0.0567 369 ASN A OD1 
3019 N ND2 . ASN A 379 ? 0.4348 0.5759 0.4265 -0.0252 0.0002  -0.0623 369 ASN A ND2 
3020 N N   . ARG A 380 ? 0.3631 0.5098 0.3657 -0.0264 0.0063  -0.0707 370 ARG A N   
3021 C CA  . ARG A 380 ? 0.3644 0.5220 0.3692 -0.0285 0.0079  -0.0744 370 ARG A CA  
3022 C C   . ARG A 380 ? 0.3696 0.5323 0.3730 -0.0254 0.0067  -0.0743 370 ARG A C   
3023 O O   . ARG A 380 ? 0.3594 0.5317 0.3618 -0.0248 0.0060  -0.0755 370 ARG A O   
3024 C CB  . ARG A 380 ? 0.3656 0.5234 0.3754 -0.0328 0.0113  -0.0781 370 ARG A CB  
3025 C CG  . ARG A 380 ? 0.3701 0.5264 0.3820 -0.0362 0.0128  -0.0797 370 ARG A CG  
3026 C CD  . ARG A 380 ? 0.3656 0.5185 0.3821 -0.0396 0.0157  -0.0827 370 ARG A CD  
3027 N NE  . ARG A 380 ? 0.3590 0.5204 0.3782 -0.0430 0.0177  -0.0871 370 ARG A NE  
3028 C CZ  . ARG A 380 ? 0.3674 0.5271 0.3903 -0.0462 0.0200  -0.0901 370 ARG A CZ  
3029 N NH1 . ARG A 380 ? 0.3675 0.5173 0.3919 -0.0463 0.0205  -0.0891 370 ARG A NH1 
3030 N NH2 . ARG A 380 ? 0.3622 0.5297 0.3871 -0.0495 0.0216  -0.0941 370 ARG A NH2 
3031 N N   . THR A 381 ? 0.3573 0.5141 0.3608 -0.0234 0.0064  -0.0731 371 THR A N   
3032 C CA  . THR A 381 ? 0.3685 0.5304 0.3712 -0.0205 0.0054  -0.0734 371 THR A CA  
3033 C C   . THR A 381 ? 0.3833 0.5473 0.3812 -0.0154 0.0019  -0.0710 371 THR A C   
3034 O O   . THR A 381 ? 0.3795 0.5533 0.3766 -0.0140 0.0012  -0.0724 371 THR A O   
3035 C CB  . THR A 381 ? 0.3580 0.5128 0.3618 -0.0196 0.0059  -0.0724 371 THR A CB  
3036 O OG1 . THR A 381 ? 0.3366 0.4901 0.3448 -0.0245 0.0090  -0.0747 371 THR A OG1 
3037 C CG2 . THR A 381 ? 0.3561 0.5169 0.3589 -0.0164 0.0048  -0.0728 371 THR A CG2 
3038 N N   . ILE A 382 ? 0.4026 0.5573 0.3972 -0.0126 -0.0004 -0.0674 372 ILE A N   
3039 C CA  . ILE A 382 ? 0.4263 0.5809 0.4158 -0.0077 -0.0042 -0.0648 372 ILE A CA  
3040 C C   . ILE A 382 ? 0.4417 0.6046 0.4298 -0.0084 -0.0049 -0.0653 372 ILE A C   
3041 O O   . ILE A 382 ? 0.4402 0.6090 0.4255 -0.0048 -0.0072 -0.0651 372 ILE A O   
3042 C CB  . ILE A 382 ? 0.4440 0.5860 0.4300 -0.0055 -0.0066 -0.0608 372 ILE A CB  
3043 C CG1 . ILE A 382 ? 0.4471 0.5823 0.4339 -0.0035 -0.0065 -0.0602 372 ILE A CG1 
3044 C CG2 . ILE A 382 ? 0.4514 0.5925 0.4317 -0.0009 -0.0108 -0.0579 372 ILE A CG2 
3045 C CD1 . ILE A 382 ? 0.4524 0.5750 0.4368 -0.0026 -0.0080 -0.0568 372 ILE A CD1 
3046 N N   . SER A 383 ? 0.4421 0.6058 0.4320 -0.0130 -0.0030 -0.0662 373 SER A N   
3047 C CA  . SER A 383 ? 0.4525 0.6249 0.4414 -0.0145 -0.0033 -0.0670 373 SER A CA  
3048 C C   . SER A 383 ? 0.4551 0.6402 0.4457 -0.0146 -0.0023 -0.0703 373 SER A C   
3049 O O   . SER A 383 ? 0.4540 0.6463 0.4420 -0.0124 -0.0043 -0.0699 373 SER A O   
3050 C CB  . SER A 383 ? 0.4553 0.6274 0.4468 -0.0197 -0.0008 -0.0683 373 SER A CB  
3051 O OG  . SER A 383 ? 0.4569 0.6192 0.4460 -0.0196 -0.0022 -0.0650 373 SER A OG  
3052 N N   . MET A 384 ? 0.4528 0.6406 0.4478 -0.0171 0.0005  -0.0736 374 MET A N   
3053 C CA  . MET A 384 ? 0.4540 0.6542 0.4509 -0.0179 0.0017  -0.0769 374 MET A CA  
3054 C C   . MET A 384 ? 0.4718 0.6759 0.4658 -0.0122 -0.0008 -0.0759 374 MET A C   
3055 O O   . MET A 384 ? 0.4610 0.6763 0.4545 -0.0112 -0.0014 -0.0775 374 MET A O   
3056 C CB  . MET A 384 ? 0.4498 0.6508 0.4517 -0.0225 0.0054  -0.0803 374 MET A CB  
3057 C CG  . MET A 384 ? 0.4468 0.6487 0.4518 -0.0281 0.0081  -0.0829 374 MET A CG  
3058 S SD  . MET A 384 ? 0.4331 0.6362 0.4435 -0.0337 0.0121  -0.0871 374 MET A SD  
3059 C CE  . MET A 384 ? 0.4450 0.6341 0.4558 -0.0323 0.0120  -0.0844 374 MET A CE  
3060 N N   . VAL A 385 ? 0.4720 0.6674 0.4644 -0.0085 -0.0025 -0.0736 375 VAL A N   
3061 C CA  . VAL A 385 ? 0.4896 0.6879 0.4790 -0.0024 -0.0054 -0.0727 375 VAL A CA  
3062 C C   . VAL A 385 ? 0.4969 0.6969 0.4816 0.0016  -0.0091 -0.0704 375 VAL A C   
3063 O O   . VAL A 385 ? 0.4867 0.6959 0.4699 0.0051  -0.0107 -0.0713 375 VAL A O   
3064 C CB  . VAL A 385 ? 0.4895 0.6773 0.4779 0.0007  -0.0066 -0.0706 375 VAL A CB  
3065 C CG1 . VAL A 385 ? 0.4965 0.6870 0.4815 0.0076  -0.0100 -0.0698 375 VAL A CG1 
3066 C CG2 . VAL A 385 ? 0.4857 0.6733 0.4786 -0.0030 -0.0033 -0.0728 375 VAL A CG2 
3067 N N   . ASN A 386 ? 0.5077 0.6989 0.4899 0.0011  -0.0104 -0.0674 376 ASN A N   
3068 C CA  . ASN A 386 ? 0.5341 0.7257 0.5114 0.0041  -0.0139 -0.0647 376 ASN A CA  
3069 C C   . ASN A 386 ? 0.5505 0.7553 0.5287 0.0019  -0.0130 -0.0668 376 ASN A C   
3070 O O   . ASN A 386 ? 0.5499 0.7604 0.5248 0.0058  -0.0159 -0.0660 376 ASN A O   
3071 C CB  . ASN A 386 ? 0.5401 0.7200 0.5148 0.0028  -0.0151 -0.0610 376 ASN A CB  
3072 C CG  . ASN A 386 ? 0.5484 0.7155 0.5198 0.0070  -0.0179 -0.0578 376 ASN A CG  
3073 O OD1 . ASN A 386 ? 0.5609 0.7278 0.5298 0.0126  -0.0206 -0.0573 376 ASN A OD1 
3074 N ND2 . ASN A 386 ? 0.5372 0.6939 0.5086 0.0043  -0.0172 -0.0558 376 ASN A ND2 
3075 N N   . LYS A 387 ? 0.5588 0.7682 0.5413 -0.0041 -0.0092 -0.0697 377 LYS A N   
3076 C CA  . LYS A 387 ? 0.5789 0.8010 0.5626 -0.0070 -0.0080 -0.0721 377 LYS A CA  
3077 C C   . LYS A 387 ? 0.5833 0.8183 0.5684 -0.0055 -0.0076 -0.0753 377 LYS A C   
3078 O O   . LYS A 387 ? 0.5721 0.8166 0.5552 -0.0036 -0.0092 -0.0754 377 LYS A O   
3079 C CB  . LYS A 387 ? 0.5865 0.8095 0.5746 -0.0139 -0.0041 -0.0748 377 LYS A CB  
3080 C CG  . LYS A 387 ? 0.5948 0.8306 0.5840 -0.0171 -0.0028 -0.0776 377 LYS A CG  
3081 C CD  . LYS A 387 ? 0.6070 0.8421 0.5993 -0.0231 0.0000  -0.0794 377 LYS A CD  
3082 C CE  . LYS A 387 ? 0.6144 0.8621 0.6070 -0.0258 0.0007  -0.0817 377 LYS A CE  
3083 N NZ  . LYS A 387 ? 0.6279 0.8763 0.6157 -0.0233 -0.0025 -0.0779 377 LYS A NZ  
3084 N N   . TYR A 388 ? 0.5828 0.8187 0.5712 -0.0065 -0.0054 -0.0777 378 TYR A N   
3085 C CA  . TYR A 388 ? 0.5919 0.8410 0.5823 -0.0062 -0.0044 -0.0811 378 TYR A CA  
3086 C C   . TYR A 388 ? 0.5916 0.8435 0.5792 0.0006  -0.0075 -0.0802 378 TYR A C   
3087 O O   . TYR A 388 ? 0.5711 0.8359 0.5587 0.0021  -0.0078 -0.0824 378 TYR A O   
3088 C CB  . TYR A 388 ? 0.5944 0.8442 0.5897 -0.0115 -0.0004 -0.0844 378 TYR A CB  
3089 C CG  . TYR A 388 ? 0.5924 0.8393 0.5910 -0.0182 0.0027  -0.0861 378 TYR A CG  
3090 C CD1 . TYR A 388 ? 0.5860 0.8246 0.5877 -0.0217 0.0052  -0.0868 378 TYR A CD1 
3091 C CD2 . TYR A 388 ? 0.5907 0.8434 0.5892 -0.0208 0.0031  -0.0870 378 TYR A CD2 
3092 C CE1 . TYR A 388 ? 0.5897 0.8255 0.5944 -0.0273 0.0079  -0.0886 378 TYR A CE1 
3093 C CE2 . TYR A 388 ? 0.5923 0.8428 0.5939 -0.0266 0.0059  -0.0890 378 TYR A CE2 
3094 C CZ  . TYR A 388 ? 0.5912 0.8330 0.5958 -0.0297 0.0083  -0.0899 378 TYR A CZ  
3095 O OH  . TYR A 388 ? 0.6002 0.8395 0.6079 -0.0349 0.0109  -0.0921 378 TYR A OH  
3096 N N   . PHE A 389 ? 0.5933 0.8338 0.5786 0.0048  -0.0097 -0.0773 379 PHE A N   
3097 C CA  . PHE A 389 ? 0.5942 0.8365 0.5769 0.0118  -0.0127 -0.0768 379 PHE A CA  
3098 C C   . PHE A 389 ? 0.6024 0.8350 0.5794 0.0181  -0.0174 -0.0726 379 PHE A C   
3099 O O   . PHE A 389 ? 0.5873 0.8180 0.5619 0.0242  -0.0201 -0.0719 379 PHE A O   
3100 C CB  . PHE A 389 ? 0.5897 0.8290 0.5750 0.0114  -0.0110 -0.0780 379 PHE A CB  
3101 C CG  . PHE A 389 ? 0.5843 0.8333 0.5745 0.0056  -0.0069 -0.0819 379 PHE A CG  
3102 C CD1 . PHE A 389 ? 0.5797 0.8230 0.5734 -0.0009 -0.0035 -0.0827 379 PHE A CD1 
3103 C CD2 . PHE A 389 ? 0.5871 0.8512 0.5782 0.0066  -0.0067 -0.0849 379 PHE A CD2 
3104 C CE1 . PHE A 389 ? 0.5753 0.8265 0.5732 -0.0065 0.0000  -0.0861 379 PHE A CE1 
3105 C CE2 . PHE A 389 ? 0.5800 0.8528 0.5752 0.0006  -0.0030 -0.0884 379 PHE A CE2 
3106 C CZ  . PHE A 389 ? 0.5796 0.8455 0.5781 -0.0059 0.0002  -0.0889 379 PHE A CZ  
3107 N N   . ASP A 390 ? 0.6174 0.8441 0.5922 0.0165  -0.0184 -0.0700 380 ASP A N   
3108 C CA  . ASP A 390 ? 0.6442 0.8605 0.6132 0.0214  -0.0229 -0.0656 380 ASP A CA  
3109 C C   . ASP A 390 ? 0.6472 0.8499 0.6146 0.0247  -0.0245 -0.0635 380 ASP A C   
3110 O O   . ASP A 390 ? 0.6468 0.8435 0.6095 0.0309  -0.0287 -0.0611 380 ASP A O   
3111 C CB  . ASP A 390 ? 0.6730 0.8971 0.6381 0.0273  -0.0267 -0.0651 380 ASP A CB  
3112 C CG  . ASP A 390 ? 0.6866 0.9215 0.6521 0.0241  -0.0259 -0.0659 380 ASP A CG  
3113 O OD1 . ASP A 390 ? 0.7112 0.9479 0.6723 0.0280  -0.0296 -0.0637 380 ASP A OD1 
3114 O OD2 . ASP A 390 ? 0.6804 0.9218 0.6504 0.0176  -0.0218 -0.0686 380 ASP A OD2 
3115 N N   . GLY A 391 ? 0.6358 0.8336 0.6070 0.0204  -0.0212 -0.0645 381 GLY A N   
3116 C CA  . GLY A 391 ? 0.6328 0.8179 0.6030 0.0225  -0.0221 -0.0626 381 GLY A CA  
3117 C C   . GLY A 391 ? 0.6256 0.8140 0.5975 0.0256  -0.0217 -0.0649 381 GLY A C   
3118 O O   . GLY A 391 ? 0.6032 0.7825 0.5755 0.0259  -0.0214 -0.0640 381 GLY A O   
3119 N N   . GLU A 392 ? 0.6230 0.8248 0.5959 0.0278  -0.0217 -0.0677 382 GLU A N   
3120 C CA  . GLU A 392 ? 0.6191 0.8262 0.5935 0.0309  -0.0216 -0.0700 382 GLU A CA  
3121 C C   . GLU A 392 ? 0.5872 0.8003 0.5672 0.0246  -0.0168 -0.0730 382 GLU A C   
3122 O O   . GLU A 392 ? 0.5632 0.7891 0.5458 0.0217  -0.0147 -0.0759 382 GLU A O   
3123 C CB  . GLU A 392 ? 0.6428 0.8618 0.6151 0.0368  -0.0242 -0.0717 382 GLU A CB  
3124 C CG  . GLU A 392 ? 0.6595 0.8836 0.6325 0.0413  -0.0248 -0.0739 382 GLU A CG  
3125 C CD  . GLU A 392 ? 0.6737 0.9053 0.6433 0.0494  -0.0289 -0.0746 382 GLU A CD  
3126 O OE1 . GLU A 392 ? 0.6912 0.9188 0.6586 0.0556  -0.0316 -0.0745 382 GLU A OE1 
3127 O OE2 . GLU A 392 ? 0.6873 0.9287 0.6563 0.0497  -0.0295 -0.0755 382 GLU A OE2 
3128 N N   . LEU A 393 ? 0.5709 0.7745 0.5525 0.0225  -0.0153 -0.0722 383 LEU A N   
3129 C CA  . LEU A 393 ? 0.5662 0.7731 0.5527 0.0166  -0.0111 -0.0744 383 LEU A CA  
3130 C C   . LEU A 393 ? 0.5714 0.7908 0.5594 0.0184  -0.0106 -0.0774 383 LEU A C   
3131 O O   . LEU A 393 ? 0.5651 0.7830 0.5513 0.0237  -0.0128 -0.0770 383 LEU A O   
3132 C CB  . LEU A 393 ? 0.5571 0.7505 0.5443 0.0151  -0.0102 -0.0724 383 LEU A CB  
3133 C CG  . LEU A 393 ? 0.5499 0.7443 0.5418 0.0093  -0.0063 -0.0741 383 LEU A CG  
3134 C CD1 . LEU A 393 ? 0.5448 0.7411 0.5399 0.0024  -0.0031 -0.0754 383 LEU A CD1 
3135 C CD2 . LEU A 393 ? 0.5424 0.7239 0.5342 0.0097  -0.0064 -0.0719 383 LEU A CD2 
3136 N N   . PRO A 394 ? 0.5808 0.8127 0.5720 0.0138  -0.0079 -0.0805 384 PRO A N   
3137 C CA  . PRO A 394 ? 0.5797 0.8242 0.5724 0.0148  -0.0073 -0.0833 384 PRO A CA  
3138 C C   . PRO A 394 ? 0.5728 0.8129 0.5673 0.0132  -0.0058 -0.0832 384 PRO A C   
3139 O O   . PRO A 394 ? 0.5308 0.7614 0.5274 0.0083  -0.0035 -0.0821 384 PRO A O   
3140 C CB  . PRO A 394 ? 0.5867 0.8433 0.5825 0.0086  -0.0042 -0.0863 384 PRO A CB  
3141 C CG  . PRO A 394 ? 0.5891 0.8426 0.5837 0.0076  -0.0047 -0.0852 384 PRO A CG  
3142 C CD  . PRO A 394 ? 0.5889 0.8254 0.5820 0.0082  -0.0056 -0.0817 384 PRO A CD  
3143 N N   . ALA A 395 ? 0.5514 0.7989 0.5453 0.0176  -0.0071 -0.0845 385 ALA A N   
3144 C CA  . ALA A 395 ? 0.5468 0.7923 0.5422 0.0168  -0.0060 -0.0845 385 ALA A CA  
3145 C C   . ALA A 395 ? 0.5316 0.7811 0.5312 0.0083  -0.0019 -0.0860 385 ALA A C   
3146 O O   . ALA A 395 ? 0.5077 0.7680 0.5089 0.0043  -0.0001 -0.0883 385 ALA A O   
3147 C CB  . ALA A 395 ? 0.5514 0.8075 0.5454 0.0229  -0.0082 -0.0863 385 ALA A CB  
3148 N N   . TYR A 396 ? 0.5119 0.7525 0.5129 0.0055  -0.0004 -0.0846 386 TYR A N   
3149 C CA  . TYR A 396 ? 0.5085 0.7522 0.5130 -0.0020 0.0030  -0.0857 386 TYR A CA  
3150 C C   . TYR A 396 ? 0.5183 0.7786 0.5235 -0.0021 0.0034  -0.0884 386 TYR A C   
3151 O O   . TYR A 396 ? 0.5157 0.7810 0.5191 0.0039  0.0011  -0.0888 386 TYR A O   
3152 C CB  . TYR A 396 ? 0.4909 0.7221 0.4963 -0.0038 0.0039  -0.0833 386 TYR A CB  
3153 C CG  . TYR A 396 ? 0.4768 0.7104 0.4854 -0.0115 0.0072  -0.0841 386 TYR A CG  
3154 C CD1 . TYR A 396 ? 0.4744 0.7017 0.4853 -0.0181 0.0097  -0.0840 386 TYR A CD1 
3155 C CD2 . TYR A 396 ? 0.4752 0.7175 0.4844 -0.0121 0.0076  -0.0850 386 TYR A CD2 
3156 C CE1 . TYR A 396 ? 0.4700 0.6985 0.4835 -0.0252 0.0124  -0.0846 386 TYR A CE1 
3157 C CE2 . TYR A 396 ? 0.4726 0.7169 0.4844 -0.0195 0.0104  -0.0854 386 TYR A CE2 
3158 C CZ  . TYR A 396 ? 0.4735 0.7102 0.4873 -0.0260 0.0127  -0.0851 386 TYR A CZ  
3159 O OH  . TYR A 396 ? 0.4724 0.7101 0.4884 -0.0333 0.0152  -0.0854 386 TYR A OH  
3160 N N   . GLN A 397 ? 0.5365 0.8053 0.5443 -0.0091 0.0062  -0.0905 387 GLN A N   
3161 C CA  . GLN A 397 ? 0.5602 0.8457 0.5690 -0.0108 0.0071  -0.0932 387 GLN A CA  
3162 C C   . GLN A 397 ? 0.5554 0.8405 0.5667 -0.0187 0.0101  -0.0931 387 GLN A C   
3163 O O   . GLN A 397 ? 0.5509 0.8422 0.5624 -0.0186 0.0101  -0.0934 387 GLN A O   
3164 C CB  . GLN A 397 ? 0.5730 0.8718 0.5820 -0.0121 0.0074  -0.0959 387 GLN A CB  
3165 C CG  . GLN A 397 ? 0.5890 0.8913 0.5952 -0.0040 0.0042  -0.0962 387 GLN A CG  
3166 C CD  . GLN A 397 ? 0.6074 0.9231 0.6140 -0.0056 0.0047  -0.0988 387 GLN A CD  
3167 O OE1 . GLN A 397 ? 0.6102 0.9403 0.6183 -0.0094 0.0063  -0.1015 387 GLN A OE1 
3168 N NE2 . GLN A 397 ? 0.6112 0.9227 0.6163 -0.0029 0.0033  -0.0981 387 GLN A NE2 
3169 N N   . GLY A 398 ? 0.5535 0.8317 0.5668 -0.0256 0.0124  -0.0929 388 GLY A N   
3170 C CA  . GLY A 398 ? 0.5613 0.8371 0.5768 -0.0336 0.0151  -0.0926 388 GLY A CA  
3171 C C   . GLY A 398 ? 0.5599 0.8268 0.5772 -0.0399 0.0172  -0.0927 388 GLY A C   
3172 O O   . GLY A 398 ? 0.5557 0.8178 0.5726 -0.0378 0.0166  -0.0927 388 GLY A O   
3173 N N   . PRO A 399 ? 0.5771 0.8414 0.5963 -0.0476 0.0195  -0.0927 389 PRO A N   
3174 C CA  . PRO A 399 ? 0.5919 0.8477 0.6129 -0.0538 0.0215  -0.0932 389 PRO A CA  
3175 C C   . PRO A 399 ? 0.6000 0.8677 0.6218 -0.0580 0.0227  -0.0967 389 PRO A C   
3176 O O   . PRO A 399 ? 0.5989 0.8722 0.6218 -0.0650 0.0245  -0.0982 389 PRO A O   
3177 C CB  . PRO A 399 ? 0.5923 0.8414 0.6146 -0.0598 0.0230  -0.0917 389 PRO A CB  
3178 C CG  . PRO A 399 ? 0.5855 0.8475 0.6071 -0.0598 0.0227  -0.0920 389 PRO A CG  
3179 C CD  . PRO A 399 ? 0.5782 0.8465 0.5978 -0.0508 0.0203  -0.0920 389 PRO A CD  
3180 N N   . LEU A 400 ? 0.6180 0.8893 0.6389 -0.0538 0.0216  -0.0978 390 LEU A N   
3181 C CA  . LEU A 400 ? 0.6350 0.9195 0.6563 -0.0565 0.0223  -0.1012 390 LEU A CA  
3182 C C   . LEU A 400 ? 0.6320 0.9110 0.6552 -0.0632 0.0244  -0.1029 390 LEU A C   
3183 O O   . LEU A 400 ? 0.6234 0.9117 0.6476 -0.0691 0.0260  -0.1056 390 LEU A O   
3184 C CB  . LEU A 400 ? 0.6478 0.9393 0.6671 -0.0491 0.0201  -0.1016 390 LEU A CB  
3185 C CG  . LEU A 400 ? 0.6680 0.9653 0.6851 -0.0414 0.0175  -0.1005 390 LEU A CG  
3186 C CD1 . LEU A 400 ? 0.6764 0.9824 0.6917 -0.0352 0.0154  -0.1015 390 LEU A CD1 
3187 C CD2 . LEU A 400 ? 0.6749 0.9845 0.6924 -0.0436 0.0182  -0.1016 390 LEU A CD2 
3188 N N   . HIS A 401 ? 0.6123 0.8767 0.6359 -0.0622 0.0244  -0.1014 391 HIS A N   
3189 C CA  . HIS A 401 ? 0.6085 0.8664 0.6340 -0.0679 0.0262  -0.1032 391 HIS A CA  
3190 C C   . HIS A 401 ? 0.6155 0.8666 0.6426 -0.0749 0.0280  -0.1030 391 HIS A C   
3191 O O   . HIS A 401 ? 0.5926 0.8393 0.6193 -0.0743 0.0276  -0.1005 391 HIS A O   
3192 C CB  . HIS A 401 ? 0.6018 0.8471 0.6272 -0.0643 0.0255  -0.1017 391 HIS A CB  
3193 C CG  . HIS A 401 ? 0.5907 0.8339 0.6177 -0.0684 0.0269  -0.1043 391 HIS A CG  
3194 N ND1 . HIS A 401 ? 0.5853 0.8187 0.6144 -0.0741 0.0286  -0.1052 391 HIS A ND1 
3195 C CD2 . HIS A 401 ? 0.5830 0.8327 0.6098 -0.0676 0.0267  -0.1064 391 HIS A CD2 
3196 C CE1 . HIS A 401 ? 0.5877 0.8219 0.6179 -0.0765 0.0295  -0.1080 391 HIS A CE1 
3197 N NE2 . HIS A 401 ? 0.5831 0.8274 0.6119 -0.0727 0.0285  -0.1087 391 HIS A NE2 
3198 N N   . GLU A 402 ? 0.6312 0.8814 0.6599 -0.0816 0.0298  -0.1057 392 GLU A N   
3199 C CA  . GLU A 402 ? 0.6618 0.9045 0.6917 -0.0888 0.0314  -0.1058 392 GLU A CA  
3200 C C   . GLU A 402 ? 0.6377 0.8633 0.6682 -0.0874 0.0311  -0.1026 392 GLU A C   
3201 O O   . GLU A 402 ? 0.6284 0.8490 0.6589 -0.0907 0.0314  -0.1009 392 GLU A O   
3202 C CB  . GLU A 402 ? 0.7018 0.9445 0.7333 -0.0952 0.0330  -0.1095 392 GLU A CB  
3203 C CG  . GLU A 402 ? 0.7407 0.9798 0.7729 -0.1038 0.0345  -0.1103 392 GLU A CG  
3204 C CD  . GLU A 402 ? 0.7715 0.9924 0.8050 -0.1060 0.0349  -0.1094 392 GLU A CD  
3205 O OE1 . GLU A 402 ? 0.7944 1.0091 0.8278 -0.1103 0.0353  -0.1077 392 GLU A OE1 
3206 O OE2 . GLU A 402 ? 0.7907 1.0037 0.8252 -0.1036 0.0349  -0.1103 392 GLU A OE2 
3207 N N   . LEU A 403 ? 0.6196 0.8367 0.6502 -0.0827 0.0303  -0.1018 393 LEU A N   
3208 C CA  . LEU A 403 ? 0.6097 0.8110 0.6408 -0.0808 0.0299  -0.0990 393 LEU A CA  
3209 C C   . LEU A 403 ? 0.5887 0.7878 0.6183 -0.0756 0.0284  -0.0952 393 LEU A C   
3210 O O   . LEU A 403 ? 0.5824 0.7697 0.6125 -0.0753 0.0283  -0.0927 393 LEU A O   
3211 C CB  . LEU A 403 ? 0.6076 0.8022 0.6393 -0.0777 0.0296  -0.0996 393 LEU A CB  
3212 C CG  . LEU A 403 ? 0.6124 0.8065 0.6459 -0.0825 0.0311  -0.1034 393 LEU A CG  
3213 C CD1 . LEU A 403 ? 0.6149 0.8072 0.6484 -0.0785 0.0305  -0.1041 393 LEU A CD1 
3214 C CD2 . LEU A 403 ? 0.6161 0.7981 0.6513 -0.0877 0.0323  -0.1038 393 LEU A CD2 
3215 N N   . ASP A 404 ? 0.5722 0.7829 0.6002 -0.0714 0.0272  -0.0949 394 ASP A N   
3216 C CA  . ASP A 404 ? 0.5696 0.7790 0.5960 -0.0655 0.0255  -0.0918 394 ASP A CA  
3217 C C   . ASP A 404 ? 0.5863 0.7915 0.6128 -0.0677 0.0258  -0.0895 394 ASP A C   
3218 O O   . ASP A 404 ? 0.5667 0.7626 0.5927 -0.0642 0.0249  -0.0867 394 ASP A O   
3219 C CB  . ASP A 404 ? 0.5524 0.7762 0.5768 -0.0609 0.0241  -0.0926 394 ASP A CB  
3220 C CG  . ASP A 404 ? 0.5315 0.7574 0.5550 -0.0563 0.0229  -0.0935 394 ASP A CG  
3221 O OD1 . ASP A 404 ? 0.5186 0.7347 0.5427 -0.0562 0.0231  -0.0932 394 ASP A OD1 
3222 O OD2 . ASP A 404 ? 0.5046 0.7424 0.5266 -0.0528 0.0217  -0.0945 394 ASP A OD2 
3223 N N   . GLU A 405 ? 0.6058 0.8180 0.6328 -0.0738 0.0271  -0.0907 395 GLU A N   
3224 C CA  . GLU A 405 ? 0.6264 0.8362 0.6534 -0.0767 0.0273  -0.0885 395 GLU A CA  
3225 C C   . GLU A 405 ? 0.6041 0.7965 0.6320 -0.0776 0.0276  -0.0860 395 GLU A C   
3226 O O   . GLU A 405 ? 0.5817 0.7682 0.6090 -0.0744 0.0267  -0.0830 395 GLU A O   
3227 C CB  . GLU A 405 ? 0.6613 0.8798 0.6887 -0.0847 0.0288  -0.0903 395 GLU A CB  
3228 C CG  . GLU A 405 ? 0.6851 0.9037 0.7120 -0.0883 0.0291  -0.0880 395 GLU A CG  
3229 C CD  . GLU A 405 ? 0.7122 0.9406 0.7391 -0.0965 0.0304  -0.0898 395 GLU A CD  
3230 O OE1 . GLU A 405 ? 0.7192 0.9638 0.7454 -0.0962 0.0304  -0.0919 395 GLU A OE1 
3231 O OE2 . GLU A 405 ? 0.7202 0.9401 0.7477 -0.1033 0.0314  -0.0891 395 GLU A OE2 
3232 N N   . GLU A 406 ? 0.5897 0.7742 0.6191 -0.0817 0.0287  -0.0875 396 GLU A N   
3233 C CA  . GLU A 406 ? 0.5952 0.7635 0.6257 -0.0826 0.0289  -0.0857 396 GLU A CA  
3234 C C   . GLU A 406 ? 0.5579 0.7180 0.5882 -0.0755 0.0277  -0.0838 396 GLU A C   
3235 O O   . GLU A 406 ? 0.5375 0.6863 0.5681 -0.0746 0.0274  -0.0812 396 GLU A O   
3236 C CB  . GLU A 406 ? 0.6225 0.7855 0.6547 -0.0880 0.0302  -0.0884 396 GLU A CB  
3237 C CG  . GLU A 406 ? 0.6513 0.7981 0.6848 -0.0899 0.0305  -0.0870 396 GLU A CG  
3238 C CD  . GLU A 406 ? 0.6773 0.8190 0.7124 -0.0942 0.0315  -0.0903 396 GLU A CD  
3239 O OE1 . GLU A 406 ? 0.6826 0.8306 0.7177 -0.1000 0.0324  -0.0928 396 GLU A OE1 
3240 O OE2 . GLU A 406 ? 0.6921 0.8240 0.7284 -0.0918 0.0314  -0.0907 396 GLU A OE2 
3241 N N   . MET A 407 ? 0.5235 0.6892 0.5530 -0.0708 0.0269  -0.0850 397 MET A N   
3242 C CA  . MET A 407 ? 0.5061 0.6646 0.5349 -0.0645 0.0255  -0.0832 397 MET A CA  
3243 C C   . MET A 407 ? 0.4938 0.6528 0.5208 -0.0594 0.0239  -0.0802 397 MET A C   
3244 O O   . MET A 407 ? 0.4810 0.6303 0.5078 -0.0560 0.0231  -0.0777 397 MET A O   
3245 C CB  . MET A 407 ? 0.4848 0.6488 0.5131 -0.0615 0.0250  -0.0853 397 MET A CB  
3246 C CG  . MET A 407 ? 0.4713 0.6267 0.4989 -0.0563 0.0238  -0.0834 397 MET A CG  
3247 S SD  . MET A 407 ? 0.4385 0.5983 0.4655 -0.0541 0.0233  -0.0856 397 MET A SD  
3248 C CE  . MET A 407 ? 0.4447 0.6167 0.4688 -0.0488 0.0213  -0.0851 397 MET A CE  
3249 N N   . GLU A 408 ? 0.4839 0.6549 0.5097 -0.0587 0.0235  -0.0806 398 GLU A N   
3250 C CA  . GLU A 408 ? 0.4851 0.6577 0.5093 -0.0544 0.0221  -0.0783 398 GLU A CA  
3251 C C   . GLU A 408 ? 0.4868 0.6512 0.5118 -0.0573 0.0227  -0.0757 398 GLU A C   
3252 O O   . GLU A 408 ? 0.4756 0.6348 0.4997 -0.0534 0.0215  -0.0732 398 GLU A O   
3253 C CB  . GLU A 408 ? 0.4835 0.6719 0.5066 -0.0535 0.0216  -0.0798 398 GLU A CB  
3254 C CG  . GLU A 408 ? 0.4782 0.6745 0.4999 -0.0488 0.0204  -0.0817 398 GLU A CG  
3255 C CD  . GLU A 408 ? 0.4758 0.6881 0.4963 -0.0469 0.0196  -0.0833 398 GLU A CD  
3256 O OE1 . GLU A 408 ? 0.4609 0.6814 0.4806 -0.0444 0.0189  -0.0852 398 GLU A OE1 
3257 O OE2 . GLU A 408 ? 0.4695 0.6868 0.4898 -0.0477 0.0196  -0.0826 398 GLU A OE2 
3258 N N   . ALA A 409 ? 0.4887 0.6519 0.5152 -0.0642 0.0243  -0.0764 399 ALA A N   
3259 C CA  . ALA A 409 ? 0.4930 0.6472 0.5202 -0.0678 0.0249  -0.0739 399 ALA A CA  
3260 C C   . ALA A 409 ? 0.4844 0.6232 0.5125 -0.0659 0.0247  -0.0722 399 ALA A C   
3261 O O   . ALA A 409 ? 0.4918 0.6232 0.5198 -0.0650 0.0242  -0.0693 399 ALA A O   
3262 C CB  . ALA A 409 ? 0.4952 0.6512 0.5235 -0.0758 0.0264  -0.0752 399 ALA A CB  
3263 N N   . MET A 410 ? 0.4632 0.5981 0.4922 -0.0656 0.0250  -0.0741 400 MET A N   
3264 C CA  . MET A 410 ? 0.4549 0.5772 0.4848 -0.0632 0.0247  -0.0730 400 MET A CA  
3265 C C   . MET A 410 ? 0.4366 0.5565 0.4649 -0.0564 0.0231  -0.0706 400 MET A C   
3266 O O   . MET A 410 ? 0.4194 0.5292 0.4481 -0.0549 0.0227  -0.0683 400 MET A O   
3267 C CB  . MET A 410 ? 0.4588 0.5798 0.4899 -0.0639 0.0254  -0.0759 400 MET A CB  
3268 C CG  . MET A 410 ? 0.4607 0.5688 0.4931 -0.0630 0.0254  -0.0753 400 MET A CG  
3269 S SD  . MET A 410 ? 0.4484 0.5569 0.4819 -0.0626 0.0259  -0.0787 400 MET A SD  
3270 C CE  . MET A 410 ? 0.4582 0.5519 0.4933 -0.0614 0.0259  -0.0774 400 MET A CE  
3271 N N   . ALA A 411 ? 0.4223 0.5513 0.4488 -0.0524 0.0219  -0.0712 401 ALA A N   
3272 C CA  . ALA A 411 ? 0.4284 0.5555 0.4529 -0.0460 0.0201  -0.0690 401 ALA A CA  
3273 C C   . ALA A 411 ? 0.4348 0.5588 0.4589 -0.0454 0.0196  -0.0662 401 ALA A C   
3274 O O   . ALA A 411 ? 0.4052 0.5201 0.4289 -0.0426 0.0189  -0.0639 401 ALA A O   
3275 C CB  . ALA A 411 ? 0.4215 0.5594 0.4440 -0.0420 0.0188  -0.0704 401 ALA A CB  
3276 N N   . LEU A 412 ? 0.4405 0.5722 0.4646 -0.0483 0.0202  -0.0665 402 LEU A N   
3277 C CA  . LEU A 412 ? 0.4566 0.5867 0.4804 -0.0484 0.0199  -0.0639 402 LEU A CA  
3278 C C   . LEU A 412 ? 0.4447 0.5627 0.4700 -0.0518 0.0208  -0.0618 402 LEU A C   
3279 O O   . LEU A 412 ? 0.4378 0.5496 0.4627 -0.0497 0.0201  -0.0591 402 LEU A O   
3280 C CB  . LEU A 412 ? 0.4783 0.6207 0.5016 -0.0512 0.0203  -0.0648 402 LEU A CB  
3281 C CG  . LEU A 412 ? 0.5059 0.6614 0.5276 -0.0471 0.0192  -0.0668 402 LEU A CG  
3282 C CD1 . LEU A 412 ? 0.5185 0.6868 0.5401 -0.0508 0.0199  -0.0678 402 LEU A CD1 
3283 C CD2 . LEU A 412 ? 0.5185 0.6726 0.5382 -0.0397 0.0171  -0.0656 402 LEU A CD2 
3284 N N   . GLU A 413 ? 0.4445 0.5589 0.4716 -0.0569 0.0222  -0.0630 403 GLU A N   
3285 C CA  . GLU A 413 ? 0.4590 0.5612 0.4876 -0.0599 0.0228  -0.0613 403 GLU A CA  
3286 C C   . GLU A 413 ? 0.4340 0.5259 0.4629 -0.0555 0.0221  -0.0602 403 GLU A C   
3287 O O   . GLU A 413 ? 0.4213 0.5040 0.4508 -0.0556 0.0220  -0.0578 403 GLU A O   
3288 C CB  . GLU A 413 ? 0.4844 0.5848 0.5146 -0.0659 0.0242  -0.0635 403 GLU A CB  
3289 C CG  . GLU A 413 ? 0.5125 0.6005 0.5442 -0.0694 0.0247  -0.0618 403 GLU A CG  
3290 C CD  . GLU A 413 ? 0.5447 0.6313 0.5757 -0.0716 0.0244  -0.0585 403 GLU A CD  
3291 O OE1 . GLU A 413 ? 0.5806 0.6564 0.6123 -0.0717 0.0242  -0.0561 403 GLU A OE1 
3292 O OE2 . GLU A 413 ? 0.5563 0.6531 0.5861 -0.0731 0.0244  -0.0582 403 GLU A OE2 
3293 N N   . THR A 414 ? 0.4095 0.5035 0.4379 -0.0521 0.0216  -0.0619 404 THR A N   
3294 C CA  . THR A 414 ? 0.3971 0.4830 0.4253 -0.0481 0.0208  -0.0610 404 THR A CA  
3295 C C   . THR A 414 ? 0.3878 0.4711 0.4145 -0.0439 0.0195  -0.0579 404 THR A C   
3296 O O   . THR A 414 ? 0.3717 0.4458 0.3989 -0.0428 0.0192  -0.0559 404 THR A O   
3297 C CB  . THR A 414 ? 0.3904 0.4807 0.4179 -0.0455 0.0204  -0.0632 404 THR A CB  
3298 O OG1 . THR A 414 ? 0.3811 0.4732 0.4103 -0.0495 0.0218  -0.0662 404 THR A OG1 
3299 C CG2 . THR A 414 ? 0.3818 0.4647 0.4088 -0.0416 0.0195  -0.0620 404 THR A CG2 
3300 N N   . VAL A 415 ? 0.3819 0.4737 0.4067 -0.0416 0.0185  -0.0578 405 VAL A N   
3301 C CA  . VAL A 415 ? 0.3923 0.4826 0.4153 -0.0375 0.0171  -0.0553 405 VAL A CA  
3302 C C   . VAL A 415 ? 0.4024 0.4877 0.4265 -0.0401 0.0177  -0.0528 405 VAL A C   
3303 O O   . VAL A 415 ? 0.3828 0.4611 0.4064 -0.0377 0.0169  -0.0505 405 VAL A O   
3304 C CB  . VAL A 415 ? 0.3927 0.4940 0.4136 -0.0344 0.0159  -0.0562 405 VAL A CB  
3305 C CG1 . VAL A 415 ? 0.3947 0.4946 0.4139 -0.0303 0.0145  -0.0541 405 VAL A CG1 
3306 C CG2 . VAL A 415 ? 0.3912 0.4962 0.4108 -0.0311 0.0150  -0.0582 405 VAL A CG2 
3307 N N   . LYS A 416 ? 0.4164 0.5051 0.4416 -0.0453 0.0189  -0.0532 406 LYS A N   
3308 C CA  . LYS A 416 ? 0.4304 0.5148 0.4564 -0.0485 0.0194  -0.0507 406 LYS A CA  
3309 C C   . LYS A 416 ? 0.4168 0.4883 0.4443 -0.0492 0.0197  -0.0491 406 LYS A C   
3310 O O   . LYS A 416 ? 0.4025 0.4682 0.4299 -0.0480 0.0192  -0.0464 406 LYS A O   
3311 C CB  . LYS A 416 ? 0.4617 0.5522 0.4883 -0.0546 0.0206  -0.0514 406 LYS A CB  
3312 C CG  . LYS A 416 ? 0.4941 0.5818 0.5208 -0.0580 0.0208  -0.0485 406 LYS A CG  
3313 C CD  . LYS A 416 ? 0.5242 0.6167 0.5513 -0.0649 0.0219  -0.0490 406 LYS A CD  
3314 C CE  . LYS A 416 ? 0.5468 0.6343 0.5740 -0.0688 0.0219  -0.0456 406 LYS A CE  
3315 N NZ  . LYS A 416 ? 0.5674 0.6579 0.5947 -0.0762 0.0229  -0.0459 406 LYS A NZ  
3316 N N   . SER A 417 ? 0.3987 0.4664 0.4277 -0.0512 0.0205  -0.0511 407 SER A N   
3317 C CA  . SER A 417 ? 0.3956 0.4519 0.4264 -0.0516 0.0208  -0.0505 407 SER A CA  
3318 C C   . SER A 417 ? 0.3700 0.4212 0.4001 -0.0463 0.0198  -0.0491 407 SER A C   
3319 O O   . SER A 417 ? 0.3678 0.4108 0.3986 -0.0457 0.0195  -0.0469 407 SER A O   
3320 C CB  . SER A 417 ? 0.4052 0.4603 0.4375 -0.0540 0.0217  -0.0537 407 SER A CB  
3321 O OG  . SER A 417 ? 0.4146 0.4592 0.4485 -0.0540 0.0219  -0.0535 407 SER A OG  
3322 N N   . TYR A 418 ? 0.3486 0.4045 0.3772 -0.0427 0.0190  -0.0504 408 TYR A N   
3323 C CA  . TYR A 418 ? 0.3466 0.3986 0.3740 -0.0379 0.0178  -0.0492 408 TYR A CA  
3324 C C   . TYR A 418 ? 0.3481 0.3978 0.3744 -0.0360 0.0169  -0.0461 408 TYR A C   
3325 O O   . TYR A 418 ? 0.3461 0.3885 0.3726 -0.0343 0.0165  -0.0442 408 TYR A O   
3326 C CB  . TYR A 418 ? 0.3305 0.3894 0.3558 -0.0348 0.0169  -0.0508 408 TYR A CB  
3327 C CG  . TYR A 418 ? 0.3169 0.3735 0.3399 -0.0299 0.0152  -0.0494 408 TYR A CG  
3328 C CD1 . TYR A 418 ? 0.3150 0.3675 0.3377 -0.0282 0.0148  -0.0498 408 TYR A CD1 
3329 C CD2 . TYR A 418 ? 0.3129 0.3720 0.3339 -0.0270 0.0139  -0.0478 408 TYR A CD2 
3330 C CE1 . TYR A 418 ? 0.3038 0.3540 0.3240 -0.0242 0.0130  -0.0483 408 TYR A CE1 
3331 C CE2 . TYR A 418 ? 0.3005 0.3569 0.3190 -0.0226 0.0121  -0.0467 408 TYR A CE2 
3332 C CZ  . TYR A 418 ? 0.3009 0.3527 0.3189 -0.0214 0.0117  -0.0468 408 TYR A CZ  
3333 O OH  . TYR A 418 ? 0.2885 0.3371 0.3037 -0.0175 0.0098  -0.0454 408 TYR A OH  
3334 N N   . THR A 419 ? 0.3541 0.4110 0.3793 -0.0363 0.0167  -0.0457 409 THR A N   
3335 C CA  . THR A 419 ? 0.3649 0.4212 0.3890 -0.0346 0.0159  -0.0431 409 THR A CA  
3336 C C   . THR A 419 ? 0.3774 0.4258 0.4032 -0.0372 0.0165  -0.0406 409 THR A C   
3337 O O   . THR A 419 ? 0.3518 0.3949 0.3772 -0.0349 0.0158  -0.0384 409 THR A O   
3338 C CB  . THR A 419 ? 0.3668 0.4336 0.3896 -0.0348 0.0156  -0.0436 409 THR A CB  
3339 O OG1 . THR A 419 ? 0.3657 0.4394 0.3870 -0.0319 0.0148  -0.0460 409 THR A OG1 
3340 C CG2 . THR A 419 ? 0.3717 0.4390 0.3932 -0.0325 0.0146  -0.0413 409 THR A CG2 
3341 N N   . GLU A 420 ? 0.3907 0.4379 0.4182 -0.0420 0.0177  -0.0410 410 GLU A N   
3342 C CA  . GLU A 420 ? 0.4147 0.4536 0.4438 -0.0446 0.0181  -0.0387 410 GLU A CA  
3343 C C   . GLU A 420 ? 0.3966 0.4261 0.4266 -0.0421 0.0178  -0.0383 410 GLU A C   
3344 O O   . GLU A 420 ? 0.3834 0.4071 0.4137 -0.0411 0.0174  -0.0356 410 GLU A O   
3345 C CB  . GLU A 420 ? 0.4531 0.4913 0.4836 -0.0502 0.0192  -0.0396 410 GLU A CB  
3346 C CG  . GLU A 420 ? 0.4890 0.5360 0.5185 -0.0537 0.0195  -0.0393 410 GLU A CG  
3347 C CD  . GLU A 420 ? 0.5301 0.5771 0.5606 -0.0597 0.0205  -0.0404 410 GLU A CD  
3348 O OE1 . GLU A 420 ? 0.5714 0.6269 0.6009 -0.0630 0.0208  -0.0406 410 GLU A OE1 
3349 O OE2 . GLU A 420 ? 0.5608 0.5994 0.5928 -0.0613 0.0209  -0.0412 410 GLU A OE2 
3350 N N   . SER A 421 ? 0.3709 0.3998 0.4015 -0.0411 0.0181  -0.0408 411 SER A N   
3351 C CA  . SER A 421 ? 0.3549 0.3766 0.3864 -0.0387 0.0179  -0.0408 411 SER A CA  
3352 C C   . SER A 421 ? 0.3426 0.3634 0.3724 -0.0344 0.0166  -0.0389 411 SER A C   
3353 O O   . SER A 421 ? 0.3352 0.3496 0.3656 -0.0332 0.0163  -0.0372 411 SER A O   
3354 C CB  . SER A 421 ? 0.3551 0.3782 0.3873 -0.0387 0.0184  -0.0441 411 SER A CB  
3355 O OG  . SER A 421 ? 0.3552 0.3777 0.3893 -0.0428 0.0194  -0.0460 411 SER A OG  
3356 N N   . MET A 422 ? 0.3303 0.3576 0.3578 -0.0321 0.0158  -0.0393 412 MET A N   
3357 C CA  . MET A 422 ? 0.3244 0.3506 0.3497 -0.0280 0.0144  -0.0377 412 MET A CA  
3358 C C   . MET A 422 ? 0.3346 0.3585 0.3598 -0.0279 0.0141  -0.0348 412 MET A C   
3359 O O   . MET A 422 ? 0.3314 0.3503 0.3561 -0.0258 0.0134  -0.0330 412 MET A O   
3360 C CB  . MET A 422 ? 0.3128 0.3462 0.3355 -0.0255 0.0134  -0.0389 412 MET A CB  
3361 C CG  . MET A 422 ? 0.3080 0.3440 0.3303 -0.0250 0.0133  -0.0414 412 MET A CG  
3362 S SD  . MET A 422 ? 0.2984 0.3277 0.3206 -0.0233 0.0129  -0.0414 412 MET A SD  
3363 C CE  . MET A 422 ? 0.2992 0.3277 0.3176 -0.0188 0.0107  -0.0395 412 MET A CE  
3364 N N   . GLU A 423 ? 0.3559 0.3839 0.3813 -0.0304 0.0146  -0.0342 413 GLU A N   
3365 C CA  . GLU A 423 ? 0.3734 0.4001 0.3987 -0.0307 0.0143  -0.0313 413 GLU A CA  
3366 C C   . GLU A 423 ? 0.3816 0.3994 0.4088 -0.0319 0.0146  -0.0293 413 GLU A C   
3367 O O   . GLU A 423 ? 0.3671 0.3822 0.3938 -0.0306 0.0140  -0.0268 413 GLU A O   
3368 C CB  . GLU A 423 ? 0.3890 0.4226 0.4142 -0.0338 0.0148  -0.0311 413 GLU A CB  
3369 C CG  . GLU A 423 ? 0.4056 0.4489 0.4287 -0.0318 0.0141  -0.0328 413 GLU A CG  
3370 C CD  . GLU A 423 ? 0.4146 0.4589 0.4355 -0.0273 0.0126  -0.0318 413 GLU A CD  
3371 O OE1 . GLU A 423 ? 0.4381 0.4791 0.4591 -0.0271 0.0124  -0.0293 413 GLU A OE1 
3372 O OE2 . GLU A 423 ? 0.4153 0.4636 0.4344 -0.0240 0.0116  -0.0336 413 GLU A OE2 
3373 N N   . SER A 424 ? 0.3802 0.3938 0.4094 -0.0341 0.0155  -0.0305 414 SER A N   
3374 C CA  . SER A 424 ? 0.3867 0.3918 0.4179 -0.0347 0.0157  -0.0291 414 SER A CA  
3375 C C   . SER A 424 ? 0.3736 0.3742 0.4052 -0.0317 0.0154  -0.0301 414 SER A C   
3376 O O   . SER A 424 ? 0.3652 0.3593 0.3986 -0.0319 0.0156  -0.0296 414 SER A O   
3377 C CB  . SER A 424 ? 0.4105 0.4128 0.4435 -0.0389 0.0166  -0.0300 414 SER A CB  
3378 O OG  . SER A 424 ? 0.4180 0.4228 0.4516 -0.0398 0.0173  -0.0335 414 SER A OG  
3379 N N   . LEU A 425 ? 0.3590 0.3632 0.3889 -0.0290 0.0149  -0.0313 415 LEU A N   
3380 C CA  . LEU A 425 ? 0.3593 0.3606 0.3890 -0.0265 0.0145  -0.0320 415 LEU A CA  
3381 C C   . LEU A 425 ? 0.3594 0.3583 0.3915 -0.0278 0.0154  -0.0345 415 LEU A C   
3382 O O   . LEU A 425 ? 0.3652 0.3604 0.3981 -0.0264 0.0153  -0.0347 415 LEU A O   
3383 C CB  . LEU A 425 ? 0.3625 0.3591 0.3921 -0.0246 0.0138  -0.0293 415 LEU A CB  
3384 C CG  . LEU A 425 ? 0.3634 0.3624 0.3907 -0.0231 0.0128  -0.0271 415 LEU A CG  
3385 C CD1 . LEU A 425 ? 0.3632 0.3576 0.3907 -0.0216 0.0123  -0.0245 415 LEU A CD1 
3386 C CD2 . LEU A 425 ? 0.3654 0.3690 0.3898 -0.0208 0.0118  -0.0282 415 LEU A CD2 
3387 N N   . GLN A 426 ? 0.3611 0.3625 0.3941 -0.0305 0.0162  -0.0365 416 GLN A N   
3388 C CA  . GLN A 426 ? 0.3669 0.3668 0.4019 -0.0319 0.0171  -0.0395 416 GLN A CA  
3389 C C   . GLN A 426 ? 0.3506 0.3564 0.3843 -0.0310 0.0170  -0.0419 416 GLN A C   
3390 O O   . GLN A 426 ? 0.3462 0.3565 0.3800 -0.0329 0.0176  -0.0439 416 GLN A O   
3391 C CB  . GLN A 426 ? 0.3858 0.3845 0.4224 -0.0357 0.0179  -0.0403 416 GLN A CB  
3392 C CG  . GLN A 426 ? 0.4103 0.4019 0.4482 -0.0365 0.0177  -0.0378 416 GLN A CG  
3393 C CD  . GLN A 426 ? 0.4364 0.4254 0.4757 -0.0405 0.0183  -0.0384 416 GLN A CD  
3394 O OE1 . GLN A 426 ? 0.4737 0.4629 0.5122 -0.0428 0.0182  -0.0362 416 GLN A OE1 
3395 N NE2 . GLN A 426 ? 0.4563 0.4428 0.4974 -0.0416 0.0189  -0.0415 416 GLN A NE2 
3396 N N   . PHE A 427 ? 0.3434 0.3491 0.3757 -0.0282 0.0162  -0.0414 417 PHE A N   
3397 C CA  . PHE A 427 ? 0.3362 0.3471 0.3666 -0.0271 0.0158  -0.0430 417 PHE A CA  
3398 C C   . PHE A 427 ? 0.3295 0.3422 0.3614 -0.0286 0.0167  -0.0463 417 PHE A C   
3399 O O   . PHE A 427 ? 0.3191 0.3375 0.3500 -0.0291 0.0167  -0.0480 417 PHE A O   
3400 C CB  . PHE A 427 ? 0.3359 0.3454 0.3640 -0.0242 0.0145  -0.0413 417 PHE A CB  
3401 C CG  . PHE A 427 ? 0.3449 0.3540 0.3708 -0.0224 0.0133  -0.0386 417 PHE A CG  
3402 C CD1 . PHE A 427 ? 0.3479 0.3597 0.3734 -0.0230 0.0134  -0.0379 417 PHE A CD1 
3403 C CD2 . PHE A 427 ? 0.3500 0.3565 0.3739 -0.0201 0.0121  -0.0367 417 PHE A CD2 
3404 C CE1 . PHE A 427 ? 0.3564 0.3684 0.3799 -0.0212 0.0123  -0.0357 417 PHE A CE1 
3405 C CE2 . PHE A 427 ? 0.3531 0.3591 0.3748 -0.0183 0.0110  -0.0345 417 PHE A CE2 
3406 C CZ  . PHE A 427 ? 0.3516 0.3605 0.3732 -0.0187 0.0111  -0.0341 417 PHE A CZ  
3407 N N   . SER A 428 ? 0.3243 0.3326 0.3588 -0.0293 0.0174  -0.0474 418 SER A N   
3408 C CA  . SER A 428 ? 0.3335 0.3437 0.3699 -0.0308 0.0183  -0.0510 418 SER A CA  
3409 C C   . SER A 428 ? 0.3386 0.3517 0.3758 -0.0338 0.0192  -0.0529 418 SER A C   
3410 O O   . SER A 428 ? 0.3294 0.3474 0.3666 -0.0348 0.0197  -0.0557 418 SER A O   
3411 C CB  . SER A 428 ? 0.3449 0.3497 0.3840 -0.0306 0.0188  -0.0520 418 SER A CB  
3412 O OG  . SER A 428 ? 0.3663 0.3655 0.4072 -0.0317 0.0191  -0.0512 418 SER A OG  
3413 N N   . VAL A 429 ? 0.3350 0.3455 0.3726 -0.0353 0.0194  -0.0514 419 VAL A N   
3414 C CA  . VAL A 429 ? 0.3441 0.3573 0.3822 -0.0387 0.0201  -0.0528 419 VAL A CA  
3415 C C   . VAL A 429 ? 0.3362 0.3577 0.3719 -0.0385 0.0198  -0.0528 419 VAL A C   
3416 O O   . VAL A 429 ? 0.3354 0.3621 0.3713 -0.0405 0.0204  -0.0553 419 VAL A O   
3417 C CB  . VAL A 429 ? 0.3613 0.3693 0.4002 -0.0407 0.0202  -0.0506 419 VAL A CB  
3418 C CG1 . VAL A 429 ? 0.3645 0.3755 0.4037 -0.0449 0.0209  -0.0519 419 VAL A CG1 
3419 C CG2 . VAL A 429 ? 0.3700 0.3696 0.4114 -0.0405 0.0203  -0.0508 419 VAL A CG2 
3420 N N   . ALA A 430 ? 0.3289 0.3518 0.3624 -0.0359 0.0187  -0.0501 420 ALA A N   
3421 C CA  . ALA A 430 ? 0.3242 0.3547 0.3552 -0.0348 0.0181  -0.0502 420 ALA A CA  
3422 C C   . ALA A 430 ? 0.3163 0.3512 0.3466 -0.0340 0.0180  -0.0528 420 ALA A C   
3423 O O   . ALA A 430 ? 0.3151 0.3569 0.3448 -0.0351 0.0183  -0.0546 420 ALA A O   
3424 C CB  . ALA A 430 ? 0.3277 0.3577 0.3562 -0.0314 0.0167  -0.0473 420 ALA A CB  
3425 N N   . LEU A 431 ? 0.3082 0.3398 0.3388 -0.0325 0.0178  -0.0529 421 LEU A N   
3426 C CA  . LEU A 431 ? 0.3031 0.3388 0.3329 -0.0319 0.0176  -0.0549 421 LEU A CA  
3427 C C   . LEU A 431 ? 0.3107 0.3493 0.3428 -0.0350 0.0190  -0.0585 421 LEU A C   
3428 O O   . LEU A 431 ? 0.3000 0.3453 0.3311 -0.0354 0.0190  -0.0603 421 LEU A O   
3429 C CB  . LEU A 431 ? 0.3011 0.3329 0.3303 -0.0299 0.0169  -0.0540 421 LEU A CB  
3430 C CG  . LEU A 431 ? 0.2902 0.3203 0.3163 -0.0268 0.0152  -0.0508 421 LEU A CG  
3431 C CD1 . LEU A 431 ? 0.2898 0.3155 0.3157 -0.0256 0.0147  -0.0497 421 LEU A CD1 
3432 C CD2 . LEU A 431 ? 0.2902 0.3259 0.3131 -0.0252 0.0139  -0.0508 421 LEU A CD2 
3433 N N   . SER A 432 ? 0.3203 0.3539 0.3551 -0.0370 0.0201  -0.0596 422 SER A N   
3434 C CA  . SER A 432 ? 0.3445 0.3802 0.3815 -0.0402 0.0214  -0.0632 422 SER A CA  
3435 C C   . SER A 432 ? 0.3425 0.3841 0.3789 -0.0426 0.0218  -0.0640 422 SER A C   
3436 O O   . SER A 432 ? 0.3338 0.3812 0.3706 -0.0444 0.0224  -0.0669 422 SER A O   
3437 C CB  . SER A 432 ? 0.3693 0.3974 0.4092 -0.0418 0.0221  -0.0642 422 SER A CB  
3438 O OG  . SER A 432 ? 0.4082 0.4314 0.4482 -0.0425 0.0219  -0.0615 422 SER A OG  
3439 N N   . THR A 433 ? 0.3389 0.3800 0.3743 -0.0427 0.0214  -0.0615 423 THR A N   
3440 C CA  . THR A 433 ? 0.3452 0.3931 0.3798 -0.0449 0.0217  -0.0619 423 THR A CA  
3441 C C   . THR A 433 ? 0.3302 0.3870 0.3626 -0.0429 0.0210  -0.0627 423 THR A C   
3442 O O   . THR A 433 ? 0.3313 0.3951 0.3638 -0.0450 0.0216  -0.0651 423 THR A O   
3443 C CB  . THR A 433 ? 0.3497 0.3955 0.3836 -0.0451 0.0213  -0.0588 423 THR A CB  
3444 O OG1 . THR A 433 ? 0.3563 0.3945 0.3923 -0.0479 0.0219  -0.0584 423 THR A OG1 
3445 C CG2 . THR A 433 ? 0.3556 0.4100 0.3882 -0.0467 0.0213  -0.0590 423 THR A CG2 
3446 N N   . VAL A 434 ? 0.3148 0.3712 0.3450 -0.0389 0.0196  -0.0608 424 VAL A N   
3447 C CA  . VAL A 434 ? 0.3097 0.3734 0.3375 -0.0365 0.0186  -0.0614 424 VAL A CA  
3448 C C   . VAL A 434 ? 0.3090 0.3761 0.3377 -0.0379 0.0193  -0.0645 424 VAL A C   
3449 O O   . VAL A 434 ? 0.3130 0.3881 0.3408 -0.0383 0.0192  -0.0662 424 VAL A O   
3450 C CB  . VAL A 434 ? 0.3064 0.3675 0.3315 -0.0321 0.0167  -0.0587 424 VAL A CB  
3451 C CG1 . VAL A 434 ? 0.3033 0.3707 0.3257 -0.0297 0.0154  -0.0593 424 VAL A CG1 
3452 C CG2 . VAL A 434 ? 0.2971 0.3567 0.3210 -0.0306 0.0160  -0.0561 424 VAL A CG2 
3453 N N   . TRP A 435 ? 0.3119 0.3735 0.3423 -0.0386 0.0199  -0.0653 425 TRP A N   
3454 C CA  . TRP A 435 ? 0.3194 0.3846 0.3508 -0.0398 0.0206  -0.0684 425 TRP A CA  
3455 C C   . TRP A 435 ? 0.3308 0.4002 0.3642 -0.0438 0.0221  -0.0718 425 TRP A C   
3456 O O   . TRP A 435 ? 0.3290 0.4050 0.3623 -0.0447 0.0224  -0.0743 425 TRP A O   
3457 C CB  . TRP A 435 ? 0.3143 0.3739 0.3469 -0.0391 0.0207  -0.0686 425 TRP A CB  
3458 C CG  . TRP A 435 ? 0.3033 0.3659 0.3333 -0.0366 0.0194  -0.0677 425 TRP A CG  
3459 C CD1 . TRP A 435 ? 0.3056 0.3738 0.3353 -0.0372 0.0196  -0.0699 425 TRP A CD1 
3460 C CD2 . TRP A 435 ? 0.2972 0.3576 0.3241 -0.0333 0.0176  -0.0642 425 TRP A CD2 
3461 N NE1 . TRP A 435 ? 0.3028 0.3722 0.3294 -0.0346 0.0179  -0.0677 425 TRP A NE1 
3462 C CE2 . TRP A 435 ? 0.3004 0.3646 0.3251 -0.0322 0.0167  -0.0642 425 TRP A CE2 
3463 C CE3 . TRP A 435 ? 0.2929 0.3484 0.3186 -0.0314 0.0167  -0.0610 425 TRP A CE3 
3464 C CZ2 . TRP A 435 ? 0.3010 0.3635 0.3222 -0.0294 0.0146  -0.0612 425 TRP A CZ2 
3465 C CZ3 . TRP A 435 ? 0.2978 0.3518 0.3201 -0.0283 0.0148  -0.0583 425 TRP A CZ3 
3466 C CH2 . TRP A 435 ? 0.3018 0.3590 0.3219 -0.0274 0.0137  -0.0583 425 TRP A CH2 
3467 N N   . LYS A 436 ? 0.3485 0.4143 0.3835 -0.0464 0.0229  -0.0717 426 LYS A N   
3468 C CA  . LYS A 436 ? 0.3729 0.4429 0.4093 -0.0506 0.0241  -0.0747 426 LYS A CA  
3469 C C   . LYS A 436 ? 0.3684 0.4490 0.4029 -0.0506 0.0238  -0.0752 426 LYS A C   
3470 O O   . LYS A 436 ? 0.3682 0.4550 0.4033 -0.0531 0.0247  -0.0783 426 LYS A O   
3471 C CB  . LYS A 436 ? 0.3988 0.4631 0.4364 -0.0535 0.0247  -0.0737 426 LYS A CB  
3472 C CG  . LYS A 436 ? 0.4294 0.4837 0.4693 -0.0544 0.0252  -0.0742 426 LYS A CG  
3473 C CD  . LYS A 436 ? 0.4624 0.5103 0.5030 -0.0569 0.0253  -0.0723 426 LYS A CD  
3474 C CE  . LYS A 436 ? 0.4889 0.5262 0.5316 -0.0568 0.0254  -0.0725 426 LYS A CE  
3475 N NZ  . LYS A 436 ? 0.5047 0.5351 0.5477 -0.0589 0.0252  -0.0700 426 LYS A NZ  
3476 N N   . PHE A 437 ? 0.3590 0.4417 0.3912 -0.0475 0.0226  -0.0724 427 PHE A N   
3477 C CA  . PHE A 437 ? 0.3589 0.4518 0.3890 -0.0466 0.0219  -0.0727 427 PHE A CA  
3478 C C   . PHE A 437 ? 0.3501 0.4480 0.3787 -0.0441 0.0211  -0.0738 427 PHE A C   
3479 O O   . PHE A 437 ? 0.3482 0.4550 0.3764 -0.0450 0.0213  -0.0759 427 PHE A O   
3480 C CB  . PHE A 437 ? 0.3598 0.4530 0.3879 -0.0437 0.0207  -0.0697 427 PHE A CB  
3481 C CG  . PHE A 437 ? 0.3637 0.4676 0.3900 -0.0426 0.0200  -0.0703 427 PHE A CG  
3482 C CD1 . PHE A 437 ? 0.3712 0.4826 0.3984 -0.0465 0.0212  -0.0725 427 PHE A CD1 
3483 C CD2 . PHE A 437 ? 0.3661 0.4727 0.3895 -0.0376 0.0181  -0.0687 427 PHE A CD2 
3484 C CE1 . PHE A 437 ? 0.3681 0.4904 0.3938 -0.0453 0.0206  -0.0732 427 PHE A CE1 
3485 C CE2 . PHE A 437 ? 0.3661 0.4829 0.3879 -0.0361 0.0173  -0.0695 427 PHE A CE2 
3486 C CZ  . PHE A 437 ? 0.3714 0.4965 0.3944 -0.0398 0.0186  -0.0718 427 PHE A CZ  
3487 N N   . ILE A 438 ? 0.3351 0.4276 0.3628 -0.0411 0.0202  -0.0722 428 ILE A N   
3488 C CA  . ILE A 438 ? 0.3279 0.4243 0.3541 -0.0393 0.0193  -0.0728 428 ILE A CA  
3489 C C   . ILE A 438 ? 0.3292 0.4297 0.3574 -0.0427 0.0208  -0.0766 428 ILE A C   
3490 O O   . ILE A 438 ? 0.3226 0.4313 0.3498 -0.0426 0.0206  -0.0781 428 ILE A O   
3491 C CB  . ILE A 438 ? 0.3181 0.4072 0.3430 -0.0365 0.0182  -0.0703 428 ILE A CB  
3492 C CG1 . ILE A 438 ? 0.3161 0.4024 0.3383 -0.0327 0.0163  -0.0668 428 ILE A CG1 
3493 C CG2 . ILE A 438 ? 0.3149 0.4076 0.3385 -0.0356 0.0175  -0.0711 428 ILE A CG2 
3494 C CD1 . ILE A 438 ? 0.3096 0.3874 0.3310 -0.0308 0.0154  -0.0642 428 ILE A CD1 
3495 N N   . SER A 439 ? 0.3382 0.4330 0.3693 -0.0454 0.0223  -0.0782 429 SER A N   
3496 C CA  . SER A 439 ? 0.3555 0.4533 0.3888 -0.0487 0.0237  -0.0822 429 SER A CA  
3497 C C   . SER A 439 ? 0.3651 0.4711 0.3988 -0.0517 0.0246  -0.0847 429 SER A C   
3498 O O   . SER A 439 ? 0.3565 0.4697 0.3905 -0.0531 0.0251  -0.0875 429 SER A O   
3499 C CB  . SER A 439 ? 0.3705 0.4598 0.4069 -0.0506 0.0248  -0.0835 429 SER A CB  
3500 O OG  . SER A 439 ? 0.3749 0.4582 0.4110 -0.0479 0.0241  -0.0816 429 SER A OG  
3501 N N   . ARG A 440 ? 0.3659 0.4715 0.3996 -0.0529 0.0247  -0.0835 430 ARG A N   
3502 C CA  . ARG A 440 ? 0.3824 0.4965 0.4163 -0.0561 0.0255  -0.0857 430 ARG A CA  
3503 C C   . ARG A 440 ? 0.3759 0.5008 0.4074 -0.0537 0.0245  -0.0856 430 ARG A C   
3504 O O   . ARG A 440 ? 0.3679 0.5016 0.3996 -0.0561 0.0252  -0.0884 430 ARG A O   
3505 C CB  . ARG A 440 ? 0.3970 0.5085 0.4311 -0.0581 0.0258  -0.0841 430 ARG A CB  
3506 C CG  . ARG A 440 ? 0.4057 0.5245 0.4406 -0.0630 0.0270  -0.0867 430 ARG A CG  
3507 C CD  . ARG A 440 ? 0.4140 0.5438 0.4468 -0.0616 0.0262  -0.0860 430 ARG A CD  
3508 N NE  . ARG A 440 ? 0.4162 0.5549 0.4496 -0.0664 0.0274  -0.0890 430 ARG A NE  
3509 C CZ  . ARG A 440 ? 0.4292 0.5749 0.4631 -0.0681 0.0281  -0.0924 430 ARG A CZ  
3510 N NH1 . ARG A 440 ? 0.4148 0.5601 0.4486 -0.0654 0.0277  -0.0933 430 ARG A NH1 
3511 N NH2 . ARG A 440 ? 0.4306 0.5842 0.4650 -0.0727 0.0291  -0.0949 430 ARG A NH2 
3512 N N   . THR A 441 ? 0.3628 0.4868 0.3918 -0.0489 0.0227  -0.0826 431 THR A N   
3513 C CA  . THR A 441 ? 0.3599 0.4929 0.3862 -0.0458 0.0212  -0.0823 431 THR A CA  
3514 C C   . THR A 441 ? 0.3625 0.5000 0.3887 -0.0461 0.0213  -0.0843 431 THR A C   
3515 O O   . THR A 441 ? 0.3469 0.4944 0.3723 -0.0462 0.0211  -0.0860 431 THR A O   
3516 C CB  . THR A 441 ? 0.3558 0.4853 0.3792 -0.0405 0.0190  -0.0785 431 THR A CB  
3517 O OG1 . THR A 441 ? 0.3446 0.4703 0.3684 -0.0406 0.0191  -0.0768 431 THR A OG1 
3518 C CG2 . THR A 441 ? 0.3504 0.4889 0.3709 -0.0371 0.0172  -0.0782 431 THR A CG2 
3519 N N   . ASN A 442 ? 0.3574 0.4883 0.3845 -0.0462 0.0216  -0.0843 432 ASN A N   
3520 C CA  . ASN A 442 ? 0.3677 0.5031 0.3952 -0.0474 0.0220  -0.0868 432 ASN A CA  
3521 C C   . ASN A 442 ? 0.3780 0.5197 0.4080 -0.0521 0.0239  -0.0912 432 ASN A C   
3522 O O   . ASN A 442 ? 0.3821 0.5329 0.4116 -0.0528 0.0240  -0.0932 432 ASN A O   
3523 C CB  . ASN A 442 ? 0.3603 0.4877 0.3889 -0.0472 0.0222  -0.0865 432 ASN A CB  
3524 C CG  . ASN A 442 ? 0.3512 0.4763 0.3766 -0.0431 0.0201  -0.0829 432 ASN A CG  
3525 O OD1 . ASN A 442 ? 0.3349 0.4663 0.3577 -0.0413 0.0187  -0.0822 432 ASN A OD1 
3526 N ND2 . ASN A 442 ? 0.3446 0.4603 0.3701 -0.0418 0.0198  -0.0807 432 ASN A ND2 
3527 N N   . LYS A 443 ? 0.4066 0.5433 0.4391 -0.0553 0.0254  -0.0924 433 LYS A N   
3528 C CA  . LYS A 443 ? 0.4296 0.5707 0.4643 -0.0603 0.0272  -0.0965 433 LYS A CA  
3529 C C   . LYS A 443 ? 0.4266 0.5792 0.4600 -0.0613 0.0271  -0.0974 433 LYS A C   
3530 O O   . LYS A 443 ? 0.4083 0.5683 0.4426 -0.0645 0.0281  -0.1009 433 LYS A O   
3531 C CB  . LYS A 443 ? 0.4586 0.5905 0.4955 -0.0635 0.0283  -0.0970 433 LYS A CB  
3532 C CG  . LYS A 443 ? 0.4888 0.6232 0.5279 -0.0690 0.0300  -0.1012 433 LYS A CG  
3533 C CD  . LYS A 443 ? 0.5170 0.6400 0.5582 -0.0717 0.0308  -0.1017 433 LYS A CD  
3534 C CE  . LYS A 443 ? 0.5405 0.6652 0.5830 -0.0776 0.0320  -0.1049 433 LYS A CE  
3535 N NZ  . LYS A 443 ? 0.5521 0.6844 0.5955 -0.0801 0.0330  -0.1096 433 LYS A NZ  
3536 N N   . TYR A 444 ? 0.4179 0.5722 0.4492 -0.0584 0.0258  -0.0943 434 TYR A N   
3537 C CA  . TYR A 444 ? 0.4240 0.5899 0.4539 -0.0582 0.0254  -0.0948 434 TYR A CA  
3538 C C   . TYR A 444 ? 0.4257 0.6014 0.4541 -0.0562 0.0246  -0.0960 434 TYR A C   
3539 O O   . TYR A 444 ? 0.4127 0.5991 0.4411 -0.0582 0.0251  -0.0983 434 TYR A O   
3540 C CB  . TYR A 444 ? 0.4160 0.5810 0.4440 -0.0545 0.0239  -0.0913 434 TYR A CB  
3541 C CG  . TYR A 444 ? 0.4110 0.5879 0.4374 -0.0535 0.0233  -0.0916 434 TYR A CG  
3542 C CD1 . TYR A 444 ? 0.4252 0.6074 0.4527 -0.0578 0.0246  -0.0932 434 TYR A CD1 
3543 C CD2 . TYR A 444 ? 0.4047 0.5870 0.4282 -0.0481 0.0211  -0.0900 434 TYR A CD2 
3544 C CE1 . TYR A 444 ? 0.4142 0.6083 0.4404 -0.0568 0.0239  -0.0935 434 TYR A CE1 
3545 C CE2 . TYR A 444 ? 0.4081 0.6015 0.4303 -0.0465 0.0203  -0.0904 434 TYR A CE2 
3546 C CZ  . TYR A 444 ? 0.4103 0.6101 0.4339 -0.0508 0.0218  -0.0923 434 TYR A CZ  
3547 O OH  . TYR A 444 ? 0.4057 0.6175 0.4279 -0.0491 0.0210  -0.0928 434 TYR A OH  
3548 N N   . ILE A 445 ? 0.4249 0.5969 0.4518 -0.0527 0.0233  -0.0942 435 ILE A N   
3549 C CA  . ILE A 445 ? 0.4335 0.6138 0.4589 -0.0512 0.0224  -0.0950 435 ILE A CA  
3550 C C   . ILE A 445 ? 0.4405 0.6263 0.4683 -0.0561 0.0244  -0.0996 435 ILE A C   
3551 O O   . ILE A 445 ? 0.4329 0.6299 0.4603 -0.0571 0.0246  -0.1017 435 ILE A O   
3552 C CB  . ILE A 445 ? 0.4240 0.5985 0.4475 -0.0476 0.0208  -0.0924 435 ILE A CB  
3553 C CG1 . ILE A 445 ? 0.4217 0.5907 0.4424 -0.0426 0.0186  -0.0880 435 ILE A CG1 
3554 C CG2 . ILE A 445 ? 0.4219 0.6054 0.4437 -0.0468 0.0200  -0.0932 435 ILE A CG2 
3555 C CD1 . ILE A 445 ? 0.4119 0.5737 0.4304 -0.0396 0.0169  -0.0850 435 ILE A CD1 
3556 N N   . ASP A 446 ? 0.4587 0.6367 0.4891 -0.0591 0.0259  -0.1012 436 ASP A N   
3557 C CA  . ASP A 446 ? 0.4808 0.6625 0.5137 -0.0635 0.0277  -0.1058 436 ASP A CA  
3558 C C   . ASP A 446 ? 0.4967 0.6847 0.5308 -0.0680 0.0291  -0.1089 436 ASP A C   
3559 O O   . ASP A 446 ? 0.4891 0.6861 0.5239 -0.0708 0.0300  -0.1124 436 ASP A O   
3560 C CB  . ASP A 446 ? 0.4916 0.6625 0.5270 -0.0652 0.0288  -0.1070 436 ASP A CB  
3561 C CG  . ASP A 446 ? 0.4940 0.6591 0.5282 -0.0614 0.0276  -0.1044 436 ASP A CG  
3562 O OD1 . ASP A 446 ? 0.4782 0.6467 0.5096 -0.0578 0.0259  -0.1015 436 ASP A OD1 
3563 O OD2 . ASP A 446 ? 0.5334 0.6903 0.5697 -0.0622 0.0283  -0.1052 436 ASP A OD2 
3564 N N   . GLU A 447 ? 0.5034 0.6871 0.5378 -0.0690 0.0293  -0.1074 437 GLU A N   
3565 C CA  . GLU A 447 ? 0.5251 0.7146 0.5603 -0.0736 0.0305  -0.1097 437 GLU A CA  
3566 C C   . GLU A 447 ? 0.5282 0.7321 0.5616 -0.0727 0.0299  -0.1101 437 GLU A C   
3567 O O   . GLU A 447 ? 0.5150 0.7276 0.5492 -0.0769 0.0311  -0.1135 437 GLU A O   
3568 C CB  . GLU A 447 ? 0.5300 0.7117 0.5655 -0.0746 0.0306  -0.1074 437 GLU A CB  
3569 C CG  . GLU A 447 ? 0.5363 0.7047 0.5740 -0.0771 0.0315  -0.1079 437 GLU A CG  
3570 C CD  . GLU A 447 ? 0.5482 0.7086 0.5857 -0.0774 0.0313  -0.1049 437 GLU A CD  
3571 O OE1 . GLU A 447 ? 0.5234 0.6852 0.5591 -0.0736 0.0301  -0.1014 437 GLU A OE1 
3572 O OE2 . GLU A 447 ? 0.5752 0.7279 0.6144 -0.0815 0.0323  -0.1059 437 GLU A OE2 
3573 N N   . THR A 448 ? 0.5264 0.7328 0.5573 -0.0672 0.0280  -0.1068 438 THR A N   
3574 C CA  . THR A 448 ? 0.5295 0.7493 0.5585 -0.0653 0.0270  -0.1068 438 THR A CA  
3575 C C   . THR A 448 ? 0.5310 0.7597 0.5589 -0.0637 0.0264  -0.1082 438 THR A C   
3576 O O   . THR A 448 ? 0.5307 0.7719 0.5576 -0.0634 0.0260  -0.1094 438 THR A O   
3577 C CB  . THR A 448 ? 0.5308 0.7497 0.5574 -0.0597 0.0250  -0.1028 438 THR A CB  
3578 O OG1 . THR A 448 ? 0.5131 0.7245 0.5380 -0.0548 0.0232  -0.0999 438 THR A OG1 
3579 C CG2 . THR A 448 ? 0.5360 0.7483 0.5635 -0.0615 0.0256  -0.1015 438 THR A CG2 
3580 N N   . THR A 449 ? 0.5331 0.7560 0.5612 -0.0627 0.0262  -0.1079 439 THR A N   
3581 C CA  . THR A 449 ? 0.5336 0.7641 0.5605 -0.0612 0.0254  -0.1087 439 THR A CA  
3582 C C   . THR A 449 ? 0.5261 0.7663 0.5497 -0.0565 0.0232  -0.1067 439 THR A C   
3583 O O   . THR A 449 ? 0.5098 0.7624 0.5332 -0.0577 0.0234  -0.1091 439 THR A O   
3584 C CB  . THR A 449 ? 0.5388 0.7770 0.5678 -0.0666 0.0274  -0.1137 439 THR A CB  
3585 O OG1 . THR A 449 ? 0.5385 0.7860 0.5680 -0.0695 0.0283  -0.1159 439 THR A OG1 
3586 C CG2 . THR A 449 ? 0.5429 0.7715 0.5749 -0.0706 0.0293  -0.1161 439 THR A CG2 
3587 N N   . PRO A 450 ? 0.5155 0.7500 0.5366 -0.0510 0.0209  -0.1025 440 PRO A N   
3588 C CA  . PRO A 450 ? 0.5186 0.7606 0.5364 -0.0457 0.0183  -0.1004 440 PRO A CA  
3589 C C   . PRO A 450 ? 0.5241 0.7767 0.5403 -0.0448 0.0174  -0.1014 440 PRO A C   
3590 O O   . PRO A 450 ? 0.5176 0.7810 0.5323 -0.0426 0.0162  -0.1017 440 PRO A O   
3591 C CB  . PRO A 450 ? 0.5245 0.7552 0.5398 -0.0407 0.0161  -0.0959 440 PRO A CB  
3592 C CG  . PRO A 450 ? 0.5156 0.7349 0.5334 -0.0433 0.0177  -0.0957 440 PRO A CG  
3593 C CD  . PRO A 450 ? 0.5153 0.7356 0.5363 -0.0493 0.0205  -0.0995 440 PRO A CD  
3594 N N   . TRP A 451 ? 0.5203 0.7699 0.5369 -0.0464 0.0178  -0.1017 441 TRP A N   
3595 C CA  . TRP A 451 ? 0.5286 0.7878 0.5439 -0.0465 0.0172  -0.1028 441 TRP A CA  
3596 C C   . TRP A 451 ? 0.5371 0.8106 0.5540 -0.0500 0.0187  -0.1070 441 TRP A C   
3597 O O   . TRP A 451 ? 0.5384 0.8225 0.5534 -0.0481 0.0174  -0.1071 441 TRP A O   
3598 C CB  . TRP A 451 ? 0.5200 0.7741 0.5362 -0.0487 0.0180  -0.1032 441 TRP A CB  
3599 C CG  . TRP A 451 ? 0.5117 0.7593 0.5317 -0.0537 0.0208  -0.1063 441 TRP A CG  
3600 C CD1 . TRP A 451 ? 0.5080 0.7614 0.5311 -0.0590 0.0233  -0.1111 441 TRP A CD1 
3601 C CD2 . TRP A 451 ? 0.5025 0.7365 0.5238 -0.0538 0.0213  -0.1048 441 TRP A CD2 
3602 N NE1 . TRP A 451 ? 0.5034 0.7470 0.5294 -0.0621 0.0252  -0.1127 441 TRP A NE1 
3603 C CE2 . TRP A 451 ? 0.4993 0.7312 0.5243 -0.0589 0.0240  -0.1088 441 TRP A CE2 
3604 C CE3 . TRP A 451 ? 0.4958 0.7191 0.5153 -0.0499 0.0197  -0.1005 441 TRP A CE3 
3605 C CZ2 . TRP A 451 ? 0.4980 0.7176 0.5251 -0.0600 0.0250  -0.1086 441 TRP A CZ2 
3606 C CZ3 . TRP A 451 ? 0.4921 0.7039 0.5137 -0.0512 0.0208  -0.1003 441 TRP A CZ3 
3607 C CH2 . TRP A 451 ? 0.4978 0.7078 0.5231 -0.0561 0.0235  -0.1042 441 TRP A CH2 
3608 N N   . VAL A 452 ? 0.5489 0.8223 0.5691 -0.0551 0.0214  -0.1104 442 VAL A N   
3609 C CA  . VAL A 452 ? 0.5770 0.8634 0.5988 -0.0592 0.0230  -0.1145 442 VAL A CA  
3610 C C   . VAL A 452 ? 0.5837 0.8789 0.6038 -0.0560 0.0216  -0.1135 442 VAL A C   
3611 O O   . VAL A 452 ? 0.5790 0.8878 0.5984 -0.0560 0.0213  -0.1153 442 VAL A O   
3612 C CB  . VAL A 452 ? 0.5933 0.8757 0.6187 -0.0658 0.0260  -0.1182 442 VAL A CB  
3613 C CG1 . VAL A 452 ? 0.5985 0.8942 0.6252 -0.0702 0.0275  -0.1222 442 VAL A CG1 
3614 C CG2 . VAL A 452 ? 0.5994 0.8750 0.6268 -0.0687 0.0273  -0.1200 442 VAL A CG2 
3615 N N   . LEU A 453 ? 0.5832 0.8711 0.6027 -0.0533 0.0208  -0.1109 443 LEU A N   
3616 C CA  . LEU A 453 ? 0.5996 0.8953 0.6175 -0.0498 0.0194  -0.1099 443 LEU A CA  
3617 C C   . LEU A 453 ? 0.6103 0.9118 0.6245 -0.0430 0.0162  -0.1075 443 LEU A C   
3618 O O   . LEU A 453 ? 0.6021 0.9151 0.6151 -0.0404 0.0151  -0.1081 443 LEU A O   
3619 C CB  . LEU A 453 ? 0.5966 0.8821 0.6145 -0.0482 0.0191  -0.1076 443 LEU A CB  
3620 C CG  . LEU A 453 ? 0.6046 0.8831 0.6256 -0.0544 0.0218  -0.1092 443 LEU A CG  
3621 C CD1 . LEU A 453 ? 0.6069 0.8757 0.6274 -0.0518 0.0211  -0.1061 443 LEU A CD1 
3622 C CD2 . LEU A 453 ? 0.6143 0.9043 0.6371 -0.0601 0.0238  -0.1131 443 LEU A CD2 
3623 N N   . ALA A 454 ? 0.6227 0.9164 0.6351 -0.0401 0.0146  -0.1048 444 ALA A N   
3624 C CA  . ALA A 454 ? 0.6482 0.9454 0.6568 -0.0340 0.0113  -0.1021 444 ALA A CA  
3625 C C   . ALA A 454 ? 0.6785 0.9899 0.6865 -0.0350 0.0111  -0.1043 444 ALA A C   
3626 O O   . ALA A 454 ? 0.6695 0.9853 0.6742 -0.0299 0.0082  -0.1021 444 ALA A O   
3627 C CB  . ALA A 454 ? 0.6539 0.9378 0.6604 -0.0316 0.0097  -0.0984 444 ALA A CB  
3628 N N   . LYS A 455 ? 0.7265 1.0447 0.7377 -0.0414 0.0141  -0.1084 445 LYS A N   
3629 C CA  . LYS A 455 ? 0.7717 1.1039 0.7828 -0.0431 0.0144  -0.1109 445 LYS A CA  
3630 C C   . LYS A 455 ? 0.8048 1.1521 0.8148 -0.0407 0.0133  -0.1121 445 LYS A C   
3631 O O   . LYS A 455 ? 0.8041 1.1613 0.8121 -0.0382 0.0117  -0.1119 445 LYS A O   
3632 C CB  . LYS A 455 ? 0.7756 1.1103 0.7904 -0.0510 0.0179  -0.1155 445 LYS A CB  
3633 C CG  . LYS A 455 ? 0.7858 1.1081 0.8020 -0.0536 0.0191  -0.1153 445 LYS A CG  
3634 C CD  . LYS A 455 ? 0.7961 1.1200 0.8101 -0.0520 0.0177  -0.1138 445 LYS A CD  
3635 C CE  . LYS A 455 ? 0.8019 1.1135 0.8171 -0.0538 0.0185  -0.1132 445 LYS A CE  
3636 N NZ  . LYS A 455 ? 0.8081 1.1197 0.8273 -0.0605 0.0219  -0.1181 445 LYS A NZ  
3637 N N   . ASP A 456 ? 0.8471 1.1965 0.8584 -0.0414 0.0142  -0.1133 446 ASP A N   
3638 C CA  . ASP A 456 ? 0.8830 1.2480 0.8938 -0.0396 0.0135  -0.1150 446 ASP A CA  
3639 C C   . ASP A 456 ? 0.8937 1.2561 0.9028 -0.0338 0.0114  -0.1126 446 ASP A C   
3640 O O   . ASP A 456 ? 0.8910 1.2420 0.9010 -0.0343 0.0121  -0.1113 446 ASP A O   
3641 C CB  . ASP A 456 ? 0.8981 1.2730 0.9122 -0.0472 0.0169  -0.1198 446 ASP A CB  
3642 C CG  . ASP A 456 ? 0.9008 1.2653 0.9176 -0.0524 0.0194  -0.1207 446 ASP A CG  
3643 O OD1 . ASP A 456 ? 0.9212 1.2703 0.9382 -0.0523 0.0195  -0.1186 446 ASP A OD1 
3644 O OD2 . ASP A 456 ? 0.8991 1.2712 0.9176 -0.0568 0.0212  -0.1234 446 ASP A OD2 
3645 N N   . ASP A 457 ? 0.9112 1.2847 0.9179 -0.0280 0.0089  -0.1121 447 ASP A N   
3646 C CA  . ASP A 457 ? 0.9265 1.2997 0.9313 -0.0215 0.0065  -0.1103 447 ASP A CA  
3647 C C   . ASP A 457 ? 0.9136 1.2920 0.9209 -0.0248 0.0086  -0.1127 447 ASP A C   
3648 O O   . ASP A 457 ? 0.9141 1.2903 0.9203 -0.0202 0.0071  -0.1113 447 ASP A O   
3649 C CB  . ASP A 457 ? 0.9433 1.3285 0.9450 -0.0144 0.0031  -0.1098 447 ASP A CB  
3650 C CG  . ASP A 457 ? 0.9625 1.3421 0.9610 -0.0103 0.0003  -0.1067 447 ASP A CG  
3651 O OD1 . ASP A 457 ? 0.9696 1.3381 0.9685 -0.0137 0.0013  -0.1054 447 ASP A OD1 
3652 O OD2 . ASP A 457 ? 0.9760 1.3626 0.9714 -0.0037 -0.0029 -0.1055 447 ASP A OD2 
3653 N N   . SER A 458 ? 0.8916 1.2771 0.9019 -0.0327 0.0119  -0.1163 448 SER A N   
3654 C CA  . SER A 458 ? 0.8740 1.2632 0.8866 -0.0374 0.0142  -0.1184 448 SER A CA  
3655 C C   . SER A 458 ? 0.8505 1.2229 0.8641 -0.0392 0.0151  -0.1164 448 SER A C   
3656 O O   . SER A 458 ? 0.8282 1.2021 0.8427 -0.0408 0.0160  -0.1169 448 SER A O   
3657 C CB  . SER A 458 ? 0.8725 1.2717 0.8878 -0.0461 0.0174  -0.1227 448 SER A CB  
3658 O OG  . SER A 458 ? 0.8626 1.2496 0.8799 -0.0523 0.0197  -0.1231 448 SER A OG  
3659 N N   . GLN A 459 ? 0.8371 1.1943 0.8505 -0.0388 0.0150  -0.1141 449 GLN A N   
3660 C CA  . GLN A 459 ? 0.8229 1.1637 0.8373 -0.0404 0.0159  -0.1121 449 GLN A CA  
3661 C C   . GLN A 459 ? 0.8050 1.1338 0.8167 -0.0330 0.0130  -0.1079 449 GLN A C   
3662 O O   . GLN A 459 ? 0.7909 1.1051 0.8033 -0.0340 0.0135  -0.1059 449 GLN A O   
3663 C CB  . GLN A 459 ? 0.8295 1.1616 0.8461 -0.0467 0.0182  -0.1132 449 GLN A CB  
3664 C CG  . GLN A 459 ? 0.8342 1.1749 0.8534 -0.0548 0.0212  -0.1175 449 GLN A CG  
3665 C CD  . GLN A 459 ? 0.8346 1.1700 0.8559 -0.0603 0.0233  -0.1182 449 GLN A CD  
3666 O OE1 . GLN A 459 ? 0.8240 1.1585 0.8447 -0.0579 0.0226  -0.1165 449 GLN A OE1 
3667 N NE2 . GLN A 459 ? 0.8370 1.1688 0.8607 -0.0676 0.0259  -0.1208 449 GLN A NE2 
3668 N N   . LYS A 460 ? 0.7866 1.1214 0.7954 -0.0258 0.0098  -0.1065 450 LYS A N   
3669 C CA  . LYS A 460 ? 0.7921 1.1156 0.7979 -0.0186 0.0067  -0.1026 450 LYS A CA  
3670 C C   . LYS A 460 ? 0.7825 1.0991 0.7887 -0.0173 0.0067  -0.1014 450 LYS A C   
3671 O O   . LYS A 460 ? 0.7699 1.0725 0.7749 -0.0145 0.0055  -0.0984 450 LYS A O   
3672 C CB  . LYS A 460 ? 0.7972 1.1289 0.7996 -0.0110 0.0031  -0.1017 450 LYS A CB  
3673 C CG  . LYS A 460 ? 0.8125 1.1322 0.8113 -0.0035 -0.0004 -0.0977 450 LYS A CG  
3674 C CD  . LYS A 460 ? 0.8232 1.1441 0.8184 0.0014  -0.0036 -0.0959 450 LYS A CD  
3675 C CE  . LYS A 460 ? 0.8330 1.1519 0.8241 0.0107  -0.0080 -0.0935 450 LYS A CE  
3676 N NZ  . LYS A 460 ? 0.8338 1.1352 0.8230 0.0136  -0.0096 -0.0900 450 LYS A NZ  
3677 N N   . ASP A 461 ? 0.7666 1.0939 0.7745 -0.0196 0.0081  -0.1038 451 ASP A N   
3678 C CA  . ASP A 461 ? 0.7610 1.0845 0.7695 -0.0193 0.0085  -0.1031 451 ASP A CA  
3679 C C   . ASP A 461 ? 0.7232 1.0326 0.7340 -0.0252 0.0109  -0.1021 451 ASP A C   
3680 O O   . ASP A 461 ? 0.7131 1.0106 0.7232 -0.0228 0.0101  -0.0995 451 ASP A O   
3681 C CB  . ASP A 461 ? 0.7783 1.1185 0.7881 -0.0217 0.0096  -0.1063 451 ASP A CB  
3682 C CG  . ASP A 461 ? 0.7961 1.1353 0.8060 -0.0205 0.0095  -0.1056 451 ASP A CG  
3683 O OD1 . ASP A 461 ? 0.8105 1.1449 0.8183 -0.0132 0.0068  -0.1035 451 ASP A OD1 
3684 O OD2 . ASP A 461 ? 0.8210 1.1646 0.8333 -0.0269 0.0121  -0.1072 451 ASP A OD2 
3685 N N   . MET A 462 ? 0.6865 0.9973 0.6998 -0.0327 0.0138  -0.1043 452 MET A N   
3686 C CA  . MET A 462 ? 0.6681 0.9658 0.6836 -0.0385 0.0161  -0.1038 452 MET A CA  
3687 C C   . MET A 462 ? 0.6453 0.9279 0.6599 -0.0359 0.0151  -0.1010 452 MET A C   
3688 O O   . MET A 462 ? 0.6301 0.8998 0.6456 -0.0372 0.0158  -0.0992 452 MET A O   
3689 C CB  . MET A 462 ? 0.6733 0.9763 0.6914 -0.0466 0.0190  -0.1072 452 MET A CB  
3690 C CG  . MET A 462 ? 0.6767 0.9666 0.6972 -0.0527 0.0213  -0.1072 452 MET A CG  
3691 S SD  . MET A 462 ? 0.6667 0.9489 0.6881 -0.0550 0.0222  -0.1055 452 MET A SD  
3692 C CE  . MET A 462 ? 0.6847 0.9845 0.7069 -0.0599 0.0236  -0.1087 452 MET A CE  
3693 N N   . LEU A 463 ? 0.6156 0.9002 0.6283 -0.0325 0.0134  -0.1006 453 LEU A N   
3694 C CA  . LEU A 463 ? 0.6046 0.8762 0.6159 -0.0300 0.0122  -0.0978 453 LEU A CA  
3695 C C   . LEU A 463 ? 0.5843 0.8463 0.5934 -0.0241 0.0098  -0.0942 453 LEU A C   
3696 O O   . LEU A 463 ? 0.5528 0.8013 0.5621 -0.0244 0.0100  -0.0921 453 LEU A O   
3697 C CB  . LEU A 463 ? 0.6096 0.8868 0.6188 -0.0274 0.0105  -0.0977 453 LEU A CB  
3698 C CG  . LEU A 463 ? 0.6169 0.8827 0.6243 -0.0252 0.0090  -0.0948 453 LEU A CG  
3699 C CD1 . LEU A 463 ? 0.6110 0.8671 0.6211 -0.0308 0.0116  -0.0954 453 LEU A CD1 
3700 C CD2 . LEU A 463 ? 0.6216 0.8953 0.6267 -0.0229 0.0073  -0.0947 453 LEU A CD2 
3701 N N   . GLY A 464 ? 0.5557 0.8253 0.5627 -0.0187 0.0076  -0.0940 454 GLY A N   
3702 C CA  . GLY A 464 ? 0.5413 0.8035 0.5461 -0.0129 0.0053  -0.0912 454 GLY A CA  
3703 C C   . GLY A 464 ? 0.5281 0.7823 0.5351 -0.0159 0.0071  -0.0906 454 GLY A C   
3704 O O   . GLY A 464 ? 0.5203 0.7624 0.5261 -0.0133 0.0059  -0.0879 454 GLY A O   
3705 N N   . ASN A 465 ? 0.5046 0.7656 0.5144 -0.0218 0.0098  -0.0932 455 ASN A N   
3706 C CA  . ASN A 465 ? 0.5008 0.7550 0.5128 -0.0258 0.0117  -0.0927 455 ASN A CA  
3707 C C   . ASN A 465 ? 0.4939 0.7331 0.5072 -0.0292 0.0131  -0.0912 455 ASN A C   
3708 O O   . ASN A 465 ? 0.4734 0.7024 0.4871 -0.0290 0.0132  -0.0891 455 ASN A O   
3709 C CB  . ASN A 465 ? 0.5029 0.7679 0.5173 -0.0321 0.0143  -0.0957 455 ASN A CB  
3710 C CG  . ASN A 465 ? 0.4980 0.7557 0.5145 -0.0372 0.0163  -0.0951 455 ASN A CG  
3711 O OD1 . ASN A 465 ? 0.5067 0.7633 0.5227 -0.0352 0.0156  -0.0937 455 ASN A OD1 
3712 N ND2 . ASN A 465 ? 0.4839 0.7364 0.5028 -0.0438 0.0187  -0.0962 455 ASN A ND2 
3713 N N   . VAL A 466 ? 0.4773 0.7164 0.4916 -0.0323 0.0142  -0.0925 456 VAL A N   
3714 C CA  . VAL A 466 ? 0.4763 0.7025 0.4919 -0.0352 0.0153  -0.0916 456 VAL A CA  
3715 C C   . VAL A 466 ? 0.4550 0.6702 0.4682 -0.0297 0.0129  -0.0880 456 VAL A C   
3716 O O   . VAL A 466 ? 0.4439 0.6474 0.4577 -0.0303 0.0134  -0.0861 456 VAL A O   
3717 C CB  . VAL A 466 ? 0.4893 0.7195 0.5063 -0.0393 0.0168  -0.0942 456 VAL A CB  
3718 C CG1 . VAL A 466 ? 0.4918 0.7098 0.5098 -0.0409 0.0175  -0.0933 456 VAL A CG1 
3719 C CG2 . VAL A 466 ? 0.4930 0.7309 0.5127 -0.0458 0.0194  -0.0977 456 VAL A CG2 
3720 N N   . MET A 467 ? 0.4359 0.6547 0.4459 -0.0243 0.0103  -0.0869 457 MET A N   
3721 C CA  . MET A 467 ? 0.4387 0.6476 0.4457 -0.0189 0.0076  -0.0834 457 MET A CA  
3722 C C   . MET A 467 ? 0.4325 0.6353 0.4389 -0.0160 0.0067  -0.0815 457 MET A C   
3723 O O   . MET A 467 ? 0.4073 0.5981 0.4129 -0.0148 0.0061  -0.0789 457 MET A O   
3724 C CB  . MET A 467 ? 0.4441 0.6588 0.4474 -0.0135 0.0046  -0.0826 457 MET A CB  
3725 C CG  . MET A 467 ? 0.4544 0.6750 0.4577 -0.0156 0.0049  -0.0839 457 MET A CG  
3726 S SD  . MET A 467 ? 0.4535 0.6635 0.4576 -0.0193 0.0061  -0.0828 457 MET A SD  
3727 C CE  . MET A 467 ? 0.4436 0.6570 0.4529 -0.0272 0.0104  -0.0868 457 MET A CE  
3728 N N   . ALA A 468 ? 0.4180 0.6297 0.4246 -0.0150 0.0067  -0.0828 458 ALA A N   
3729 C CA  . ALA A 468 ? 0.4195 0.6273 0.4256 -0.0125 0.0060  -0.0814 458 ALA A CA  
3730 C C   . ALA A 468 ? 0.4049 0.6031 0.4137 -0.0172 0.0083  -0.0806 458 ALA A C   
3731 O O   . ALA A 468 ? 0.4125 0.6012 0.4204 -0.0149 0.0074  -0.0782 458 ALA A O   
3732 C CB  . ALA A 468 ? 0.4220 0.6433 0.4283 -0.0114 0.0059  -0.0836 458 ALA A CB  
3733 N N   . HIS A 469 ? 0.3990 0.5994 0.4108 -0.0237 0.0111  -0.0826 459 HIS A N   
3734 C CA  . HIS A 469 ? 0.4094 0.6005 0.4238 -0.0284 0.0132  -0.0820 459 HIS A CA  
3735 C C   . HIS A 469 ? 0.4081 0.5859 0.4224 -0.0281 0.0131  -0.0800 459 HIS A C   
3736 O O   . HIS A 469 ? 0.3914 0.5595 0.4065 -0.0288 0.0135  -0.0782 459 HIS A O   
3737 C CB  . HIS A 469 ? 0.4206 0.6172 0.4380 -0.0354 0.0161  -0.0848 459 HIS A CB  
3738 C CG  . HIS A 469 ? 0.4368 0.6423 0.4548 -0.0373 0.0168  -0.0859 459 HIS A CG  
3739 N ND1 . HIS A 469 ? 0.4454 0.6652 0.4625 -0.0360 0.0162  -0.0879 459 HIS A ND1 
3740 C CD2 . HIS A 469 ? 0.4471 0.6496 0.4664 -0.0404 0.0179  -0.0851 459 HIS A CD2 
3741 C CE1 . HIS A 469 ? 0.4484 0.6742 0.4663 -0.0385 0.0170  -0.0884 459 HIS A CE1 
3742 N NE2 . HIS A 469 ? 0.4468 0.6621 0.4660 -0.0413 0.0181  -0.0867 459 HIS A NE2 
3743 N N   . LEU A 470 ? 0.3919 0.5699 0.4052 -0.0272 0.0124  -0.0803 460 LEU A N   
3744 C CA  . LEU A 470 ? 0.3919 0.5588 0.4049 -0.0268 0.0121  -0.0784 460 LEU A CA  
3745 C C   . LEU A 470 ? 0.3815 0.5404 0.3917 -0.0215 0.0096  -0.0750 460 LEU A C   
3746 O O   . LEU A 470 ? 0.3752 0.5237 0.3860 -0.0220 0.0100  -0.0731 460 LEU A O   
3747 C CB  . LEU A 470 ? 0.3964 0.5667 0.4084 -0.0268 0.0116  -0.0793 460 LEU A CB  
3748 C CG  . LEU A 470 ? 0.3971 0.5732 0.4121 -0.0323 0.0141  -0.0828 460 LEU A CG  
3749 C CD1 . LEU A 470 ? 0.3948 0.5767 0.4082 -0.0314 0.0132  -0.0835 460 LEU A CD1 
3750 C CD2 . LEU A 470 ? 0.3965 0.5634 0.4144 -0.0365 0.0162  -0.0832 460 LEU A CD2 
3751 N N   . VAL A 471 ? 0.3793 0.5431 0.3864 -0.0165 0.0071  -0.0743 461 VAL A N   
3752 C CA  . VAL A 471 ? 0.3878 0.5444 0.3918 -0.0111 0.0044  -0.0713 461 VAL A CA  
3753 C C   . VAL A 471 ? 0.3875 0.5399 0.3926 -0.0112 0.0050  -0.0705 461 VAL A C   
3754 O O   . VAL A 471 ? 0.3698 0.5119 0.3739 -0.0096 0.0042  -0.0680 461 VAL A O   
3755 C CB  . VAL A 471 ? 0.3946 0.5576 0.3949 -0.0053 0.0014  -0.0712 461 VAL A CB  
3756 C CG1 . VAL A 471 ? 0.3928 0.5483 0.3899 0.0002  -0.0014 -0.0685 461 VAL A CG1 
3757 C CG2 . VAL A 471 ? 0.3948 0.5597 0.3934 -0.0050 0.0003  -0.0710 461 VAL A CG2 
3758 N N   . GLU A 472 ? 0.3772 0.5379 0.3842 -0.0132 0.0065  -0.0724 462 GLU A N   
3759 C CA  . GLU A 472 ? 0.3834 0.5413 0.3915 -0.0136 0.0071  -0.0716 462 GLU A CA  
3760 C C   . GLU A 472 ? 0.3754 0.5231 0.3860 -0.0181 0.0092  -0.0705 462 GLU A C   
3761 O O   . GLU A 472 ? 0.3683 0.5081 0.3786 -0.0168 0.0087  -0.0684 462 GLU A O   
3762 C CB  . GLU A 472 ? 0.3869 0.5569 0.3961 -0.0151 0.0081  -0.0738 462 GLU A CB  
3763 C CG  . GLU A 472 ? 0.3912 0.5598 0.4013 -0.0157 0.0086  -0.0729 462 GLU A CG  
3764 C CD  . GLU A 472 ? 0.3984 0.5650 0.4057 -0.0092 0.0059  -0.0713 462 GLU A CD  
3765 O OE1 . GLU A 472 ? 0.4024 0.5653 0.4069 -0.0042 0.0034  -0.0703 462 GLU A OE1 
3766 O OE2 . GLU A 472 ? 0.4012 0.5702 0.4091 -0.0093 0.0062  -0.0711 462 GLU A OE2 
3767 N N   . ASN A 473 ? 0.3620 0.5098 0.3750 -0.0230 0.0113  -0.0721 463 ASN A N   
3768 C CA  . ASN A 473 ? 0.3581 0.4956 0.3734 -0.0266 0.0129  -0.0713 463 ASN A CA  
3769 C C   . ASN A 473 ? 0.3509 0.4780 0.3645 -0.0234 0.0114  -0.0686 463 ASN A C   
3770 O O   . ASN A 473 ? 0.3343 0.4526 0.3486 -0.0239 0.0118  -0.0668 463 ASN A O   
3771 C CB  . ASN A 473 ? 0.3598 0.4995 0.3776 -0.0315 0.0150  -0.0739 463 ASN A CB  
3772 C CG  . ASN A 473 ? 0.3570 0.5031 0.3771 -0.0365 0.0171  -0.0762 463 ASN A CG  
3773 O OD1 . ASN A 473 ? 0.3510 0.5039 0.3706 -0.0361 0.0168  -0.0763 463 ASN A OD1 
3774 N ND2 . ASN A 473 ? 0.3434 0.4876 0.3660 -0.0413 0.0190  -0.0782 463 ASN A ND2 
3775 N N   . ILE A 474 ? 0.3403 0.4684 0.3514 -0.0206 0.0097  -0.0683 464 ILE A N   
3776 C CA  . ILE A 474 ? 0.3487 0.4677 0.3576 -0.0179 0.0081  -0.0657 464 ILE A CA  
3777 C C   . ILE A 474 ? 0.3445 0.4581 0.3514 -0.0140 0.0063  -0.0632 464 ILE A C   
3778 O O   . ILE A 474 ? 0.3282 0.4324 0.3350 -0.0138 0.0061  -0.0611 464 ILE A O   
3779 C CB  . ILE A 474 ? 0.3534 0.4756 0.3595 -0.0156 0.0062  -0.0656 464 ILE A CB  
3780 C CG1 . ILE A 474 ? 0.3594 0.4849 0.3677 -0.0198 0.0081  -0.0678 464 ILE A CG1 
3781 C CG2 . ILE A 474 ? 0.3593 0.4724 0.3620 -0.0123 0.0038  -0.0624 464 ILE A CG2 
3782 C CD1 . ILE A 474 ? 0.3587 0.4909 0.3646 -0.0184 0.0067  -0.0684 464 ILE A CD1 
3783 N N   . ARG A 475 ? 0.3342 0.4544 0.3396 -0.0109 0.0050  -0.0637 465 ARG A N   
3784 C CA  . ARG A 475 ? 0.3345 0.4509 0.3378 -0.0069 0.0032  -0.0619 465 ARG A CA  
3785 C C   . ARG A 475 ? 0.3293 0.4402 0.3351 -0.0095 0.0049  -0.0610 465 ARG A C   
3786 O O   . ARG A 475 ? 0.3171 0.4197 0.3217 -0.0076 0.0039  -0.0587 465 ARG A O   
3787 C CB  . ARG A 475 ? 0.3431 0.4694 0.3450 -0.0034 0.0018  -0.0633 465 ARG A CB  
3788 C CG  . ARG A 475 ? 0.3517 0.4743 0.3507 0.0019  -0.0007 -0.0617 465 ARG A CG  
3789 C CD  . ARG A 475 ? 0.3572 0.4907 0.3551 0.0055  -0.0020 -0.0636 465 ARG A CD  
3790 N NE  . ARG A 475 ? 0.3613 0.5026 0.3624 0.0018  0.0004  -0.0653 465 ARG A NE  
3791 C CZ  . ARG A 475 ? 0.3676 0.5072 0.3698 0.0012  0.0011  -0.0646 465 ARG A CZ  
3792 N NH1 . ARG A 475 ? 0.3648 0.4951 0.3653 0.0041  -0.0003 -0.0624 465 ARG A NH1 
3793 N NH2 . ARG A 475 ? 0.3600 0.5074 0.3648 -0.0026 0.0032  -0.0660 465 ARG A NH2 
3794 N N   . TYR A 476 ? 0.3179 0.4334 0.3270 -0.0140 0.0074  -0.0626 466 TYR A N   
3795 C CA  . TYR A 476 ? 0.3237 0.4339 0.3352 -0.0172 0.0091  -0.0617 466 TYR A CA  
3796 C C   . TYR A 476 ? 0.3131 0.4120 0.3253 -0.0181 0.0095  -0.0599 466 TYR A C   
3797 O O   . TYR A 476 ? 0.2990 0.3909 0.3109 -0.0170 0.0091  -0.0578 466 TYR A O   
3798 C CB  . TYR A 476 ? 0.3324 0.4480 0.3470 -0.0226 0.0117  -0.0637 466 TYR A CB  
3799 C CG  . TYR A 476 ? 0.3436 0.4684 0.3583 -0.0229 0.0118  -0.0646 466 TYR A CG  
3800 C CD1 . TYR A 476 ? 0.3499 0.4848 0.3627 -0.0195 0.0104  -0.0660 466 TYR A CD1 
3801 C CD2 . TYR A 476 ? 0.3492 0.4729 0.3658 -0.0265 0.0133  -0.0640 466 TYR A CD2 
3802 C CE1 . TYR A 476 ? 0.3576 0.5021 0.3706 -0.0198 0.0106  -0.0670 466 TYR A CE1 
3803 C CE2 . TYR A 476 ? 0.3522 0.4852 0.3689 -0.0272 0.0135  -0.0647 466 TYR A CE2 
3804 C CZ  . TYR A 476 ? 0.3575 0.5013 0.3724 -0.0238 0.0122  -0.0663 466 TYR A CZ  
3805 O OH  . TYR A 476 ? 0.3601 0.5140 0.3749 -0.0245 0.0124  -0.0673 466 TYR A OH  
3806 N N   . ALA A 477 ? 0.3046 0.4026 0.3177 -0.0202 0.0103  -0.0610 467 ALA A N   
3807 C CA  . ALA A 477 ? 0.2965 0.3852 0.3102 -0.0210 0.0106  -0.0596 467 ALA A CA  
3808 C C   . ALA A 477 ? 0.3002 0.3826 0.3107 -0.0168 0.0082  -0.0569 467 ALA A C   
3809 O O   . ALA A 477 ? 0.2959 0.3704 0.3068 -0.0169 0.0083  -0.0550 467 ALA A O   
3810 C CB  . ALA A 477 ? 0.3020 0.3925 0.3168 -0.0233 0.0115  -0.0615 467 ALA A CB  
3811 N N   . ALA A 478 ? 0.2900 0.3756 0.2971 -0.0132 0.0060  -0.0566 468 ALA A N   
3812 C CA  . ALA A 478 ? 0.3042 0.3835 0.3077 -0.0094 0.0034  -0.0541 468 ALA A CA  
3813 C C   . ALA A 478 ? 0.2994 0.3745 0.3024 -0.0073 0.0027  -0.0525 468 ALA A C   
3814 O O   . ALA A 478 ? 0.3087 0.3755 0.3104 -0.0064 0.0019  -0.0503 468 ALA A O   
3815 C CB  . ALA A 478 ? 0.3070 0.3905 0.3068 -0.0058 0.0010  -0.0543 468 ALA A CB  
3816 N N   . VAL A 479 ? 0.2975 0.3787 0.3013 -0.0068 0.0031  -0.0536 469 VAL A N   
3817 C CA  . VAL A 479 ? 0.3003 0.3787 0.3037 -0.0050 0.0026  -0.0523 469 VAL A CA  
3818 C C   . VAL A 479 ? 0.2993 0.3709 0.3054 -0.0083 0.0045  -0.0510 469 VAL A C   
3819 O O   . VAL A 479 ? 0.2949 0.3597 0.2999 -0.0068 0.0036  -0.0489 469 VAL A O   
3820 C CB  . VAL A 479 ? 0.3075 0.3953 0.3115 -0.0044 0.0028  -0.0539 469 VAL A CB  
3821 C CG1 . VAL A 479 ? 0.3102 0.3955 0.3141 -0.0032 0.0026  -0.0526 469 VAL A CG1 
3822 C CG2 . VAL A 479 ? 0.3160 0.4103 0.3170 0.0000  0.0005  -0.0551 469 VAL A CG2 
3823 N N   . LEU A 480 ? 0.2908 0.3642 0.3004 -0.0128 0.0069  -0.0522 470 LEU A N   
3824 C CA  . LEU A 480 ? 0.2946 0.3616 0.3069 -0.0159 0.0087  -0.0512 470 LEU A CA  
3825 C C   . LEU A 480 ? 0.2884 0.3469 0.3003 -0.0155 0.0082  -0.0496 470 LEU A C   
3826 O O   . LEU A 480 ? 0.2787 0.3310 0.2919 -0.0164 0.0088  -0.0481 470 LEU A O   
3827 C CB  . LEU A 480 ? 0.3030 0.3732 0.3187 -0.0207 0.0111  -0.0532 470 LEU A CB  
3828 C CG  . LEU A 480 ? 0.3097 0.3883 0.3263 -0.0224 0.0119  -0.0546 470 LEU A CG  
3829 C CD1 . LEU A 480 ? 0.3155 0.3960 0.3351 -0.0274 0.0141  -0.0566 470 LEU A CD1 
3830 C CD2 . LEU A 480 ? 0.3122 0.3899 0.3289 -0.0222 0.0118  -0.0528 470 LEU A CD2 
3831 N N   . LEU A 481 ? 0.2816 0.3403 0.2916 -0.0143 0.0072  -0.0500 471 LEU A N   
3832 C CA  . LEU A 481 ? 0.2834 0.3351 0.2926 -0.0142 0.0066  -0.0485 471 LEU A CA  
3833 C C   . LEU A 481 ? 0.2838 0.3302 0.2892 -0.0106 0.0042  -0.0460 471 LEU A C   
3834 O O   . LEU A 481 ? 0.2725 0.3130 0.2772 -0.0108 0.0037  -0.0445 471 LEU A O   
3835 C CB  . LEU A 481 ? 0.2934 0.3479 0.3024 -0.0153 0.0068  -0.0499 471 LEU A CB  
3836 C CG  . LEU A 481 ? 0.3012 0.3590 0.3141 -0.0193 0.0093  -0.0525 471 LEU A CG  
3837 C CD1 . LEU A 481 ? 0.3038 0.3661 0.3162 -0.0201 0.0093  -0.0542 471 LEU A CD1 
3838 C CD2 . LEU A 481 ? 0.3055 0.3570 0.3213 -0.0215 0.0109  -0.0522 471 LEU A CD2 
3839 N N   . ARG A 482 ? 0.2819 0.3306 0.2850 -0.0074 0.0025  -0.0457 472 ARG A N   
3840 C CA  . ARG A 482 ? 0.2915 0.3349 0.2908 -0.0039 0.0000  -0.0436 472 ARG A CA  
3841 C C   . ARG A 482 ? 0.2838 0.3196 0.2836 -0.0044 0.0002  -0.0415 472 ARG A C   
3842 O O   . ARG A 482 ? 0.2966 0.3267 0.2935 -0.0028 -0.0015 -0.0397 472 ARG A O   
3843 C CB  . ARG A 482 ? 0.3016 0.3492 0.2987 -0.0001 -0.0017 -0.0442 472 ARG A CB  
3844 C CG  . ARG A 482 ? 0.3142 0.3674 0.3090 0.0019  -0.0032 -0.0456 472 ARG A CG  
3845 C CD  . ARG A 482 ? 0.3289 0.3862 0.3214 0.0063  -0.0052 -0.0463 472 ARG A CD  
3846 N NE  . ARG A 482 ? 0.3465 0.3963 0.3356 0.0096  -0.0077 -0.0444 472 ARG A NE  
3847 C CZ  . ARG A 482 ? 0.3573 0.4078 0.3452 0.0129  -0.0090 -0.0446 472 ARG A CZ  
3848 N NH1 . ARG A 482 ? 0.3487 0.4077 0.3384 0.0133  -0.0080 -0.0465 472 ARG A NH1 
3849 N NH2 . ARG A 482 ? 0.3777 0.4204 0.3624 0.0155  -0.0112 -0.0430 472 ARG A NH2 
3850 N N   . PRO A 483 ? 0.2760 0.3118 0.2794 -0.0066 0.0023  -0.0415 473 PRO A N   
3851 C CA  . PRO A 483 ? 0.2708 0.2996 0.2747 -0.0071 0.0025  -0.0395 473 PRO A CA  
3852 C C   . PRO A 483 ? 0.2761 0.3005 0.2809 -0.0091 0.0031  -0.0389 473 PRO A C   
3853 O O   . PRO A 483 ? 0.2794 0.2981 0.2832 -0.0088 0.0025  -0.0371 473 PRO A O   
3854 C CB  . PRO A 483 ? 0.2717 0.3020 0.2792 -0.0093 0.0046  -0.0397 473 PRO A CB  
3855 C CG  . PRO A 483 ? 0.2753 0.3134 0.2827 -0.0087 0.0046  -0.0414 473 PRO A CG  
3856 C CD  . PRO A 483 ? 0.2738 0.3154 0.2801 -0.0085 0.0041  -0.0431 473 PRO A CD  
3857 N N   . PHE A 484 ? 0.2641 0.2918 0.2705 -0.0113 0.0044  -0.0407 474 PHE A N   
3858 C CA  . PHE A 484 ? 0.2752 0.3004 0.2831 -0.0134 0.0053  -0.0409 474 PHE A CA  
3859 C C   . PHE A 484 ? 0.2808 0.3055 0.2853 -0.0127 0.0036  -0.0403 474 PHE A C   
3860 O O   . PHE A 484 ? 0.2853 0.3059 0.2889 -0.0132 0.0032  -0.0390 474 PHE A O   
3861 C CB  . PHE A 484 ? 0.2668 0.2959 0.2785 -0.0163 0.0076  -0.0434 474 PHE A CB  
3862 C CG  . PHE A 484 ? 0.2614 0.2895 0.2765 -0.0178 0.0093  -0.0436 474 PHE A CG  
3863 C CD1 . PHE A 484 ? 0.2656 0.2979 0.2814 -0.0182 0.0098  -0.0445 474 PHE A CD1 
3864 C CD2 . PHE A 484 ? 0.2595 0.2825 0.2769 -0.0190 0.0102  -0.0429 474 PHE A CD2 
3865 C CE1 . PHE A 484 ? 0.2626 0.2937 0.2812 -0.0201 0.0112  -0.0443 474 PHE A CE1 
3866 C CE2 . PHE A 484 ? 0.2580 0.2794 0.2782 -0.0204 0.0116  -0.0428 474 PHE A CE2 
3867 C CZ  . PHE A 484 ? 0.2617 0.2868 0.2824 -0.0212 0.0120  -0.0434 474 PHE A CZ  
3868 N N   . LEU A 485 ? 0.2844 0.3137 0.2870 -0.0118 0.0027  -0.0414 475 LEU A N   
3869 C CA  . LEU A 485 ? 0.2885 0.3184 0.2879 -0.0116 0.0011  -0.0410 475 LEU A CA  
3870 C C   . LEU A 485 ? 0.3020 0.3302 0.2966 -0.0081 -0.0018 -0.0394 475 LEU A C   
3871 O O   . LEU A 485 ? 0.3139 0.3456 0.3080 -0.0060 -0.0023 -0.0403 475 LEU A O   
3872 C CB  . LEU A 485 ? 0.2901 0.3270 0.2911 -0.0132 0.0023  -0.0435 475 LEU A CB  
3873 C CG  . LEU A 485 ? 0.2927 0.3321 0.2987 -0.0164 0.0052  -0.0459 475 LEU A CG  
3874 C CD1 . LEU A 485 ? 0.2975 0.3439 0.3044 -0.0180 0.0061  -0.0485 475 LEU A CD1 
3875 C CD2 . LEU A 485 ? 0.2958 0.3308 0.3033 -0.0181 0.0060  -0.0452 475 LEU A CD2 
3876 N N   . THR A 486 ? 0.3097 0.3326 0.3005 -0.0075 -0.0039 -0.0371 476 THR A N   
3877 C CA  . THR A 486 ? 0.3335 0.3529 0.3192 -0.0041 -0.0071 -0.0355 476 THR A CA  
3878 C C   . THR A 486 ? 0.3425 0.3640 0.3245 -0.0031 -0.0093 -0.0353 476 THR A C   
3879 O O   . THR A 486 ? 0.3593 0.3789 0.3373 0.0002  -0.0120 -0.0345 476 THR A O   
3880 C CB  . THR A 486 ? 0.3385 0.3498 0.3214 -0.0039 -0.0087 -0.0328 476 THR A CB  
3881 O OG1 . THR A 486 ? 0.3478 0.3576 0.3299 -0.0068 -0.0086 -0.0318 476 THR A OG1 
3882 C CG2 . THR A 486 ? 0.3387 0.3479 0.3249 -0.0043 -0.0070 -0.0327 476 THR A CG2 
3883 N N   . HIS A 487 ? 0.3534 0.3788 0.3366 -0.0059 -0.0081 -0.0361 477 HIS A N   
3884 C CA  . HIS A 487 ? 0.3648 0.3930 0.3446 -0.0053 -0.0100 -0.0359 477 HIS A CA  
3885 C C   . HIS A 487 ? 0.3524 0.3894 0.3346 -0.0050 -0.0088 -0.0386 477 HIS A C   
3886 O O   . HIS A 487 ? 0.3479 0.3871 0.3273 -0.0020 -0.0108 -0.0387 477 HIS A O   
3887 C CB  . HIS A 487 ? 0.3926 0.4199 0.3711 -0.0085 -0.0101 -0.0346 477 HIS A CB  
3888 C CG  . HIS A 487 ? 0.4174 0.4365 0.3920 -0.0087 -0.0122 -0.0315 477 HIS A CG  
3889 N ND1 . HIS A 487 ? 0.4481 0.4662 0.4214 -0.0119 -0.0124 -0.0301 477 HIS A ND1 
3890 C CD2 . HIS A 487 ? 0.4329 0.4449 0.4047 -0.0063 -0.0143 -0.0297 477 HIS A CD2 
3891 C CE1 . HIS A 487 ? 0.4511 0.4616 0.4208 -0.0117 -0.0144 -0.0273 477 HIS A CE1 
3892 N NE2 . HIS A 487 ? 0.4448 0.4512 0.4134 -0.0083 -0.0156 -0.0271 477 HIS A NE2 
3893 N N   . ALA A 488 ? 0.3411 0.3829 0.3282 -0.0081 -0.0055 -0.0409 478 ALA A N   
3894 C CA  . ALA A 488 ? 0.3383 0.3890 0.3278 -0.0087 -0.0041 -0.0437 478 ALA A CA  
3895 C C   . ALA A 488 ? 0.3425 0.3972 0.3317 -0.0057 -0.0048 -0.0449 478 ALA A C   
3896 O O   . ALA A 488 ? 0.3312 0.3919 0.3191 -0.0044 -0.0057 -0.0459 478 ALA A O   
3897 C CB  . ALA A 488 ? 0.3380 0.3919 0.3328 -0.0125 -0.0007 -0.0462 478 ALA A CB  
3898 N N   . PRO A 489 ? 0.3370 0.3893 0.3276 -0.0045 -0.0042 -0.0449 479 PRO A N   
3899 C CA  . PRO A 489 ? 0.3442 0.4020 0.3348 -0.0018 -0.0047 -0.0463 479 PRO A CA  
3900 C C   . PRO A 489 ? 0.3670 0.4247 0.3526 0.0026  -0.0083 -0.0453 479 PRO A C   
3901 O O   . PRO A 489 ? 0.3591 0.4241 0.3443 0.0041  -0.0087 -0.0470 479 PRO A O   
3902 C CB  . PRO A 489 ? 0.3389 0.3932 0.3313 -0.0014 -0.0039 -0.0458 479 PRO A CB  
3903 C CG  . PRO A 489 ? 0.3357 0.3855 0.3310 -0.0051 -0.0017 -0.0453 479 PRO A CG  
3904 C CD  . PRO A 489 ? 0.3359 0.3823 0.3287 -0.0058 -0.0029 -0.0439 479 PRO A CD  
3905 N N   . LYS A 490 ? 0.3874 0.4368 0.3691 0.0046  -0.0108 -0.0427 480 LYS A N   
3906 C CA  . LYS A 490 ? 0.4196 0.4667 0.3959 0.0090  -0.0146 -0.0415 480 LYS A CA  
3907 C C   . LYS A 490 ? 0.4191 0.4708 0.3936 0.0086  -0.0156 -0.0417 480 LYS A C   
3908 O O   . LYS A 490 ? 0.4136 0.4697 0.3860 0.0121  -0.0175 -0.0425 480 LYS A O   
3909 C CB  . LYS A 490 ? 0.4627 0.4989 0.4351 0.0098  -0.0170 -0.0385 480 LYS A CB  
3910 C CG  . LYS A 490 ? 0.4991 0.5309 0.4655 0.0144  -0.0214 -0.0370 480 LYS A CG  
3911 C CD  . LYS A 490 ? 0.5384 0.5592 0.5012 0.0151  -0.0235 -0.0344 480 LYS A CD  
3912 C CE  . LYS A 490 ? 0.5728 0.5878 0.5291 0.0196  -0.0282 -0.0330 480 LYS A CE  
3913 N NZ  . LYS A 490 ? 0.5921 0.6048 0.5447 0.0180  -0.0301 -0.0308 480 LYS A NZ  
3914 N N   . GLU A 491 ? 0.4023 0.4533 0.3777 0.0046  -0.0143 -0.0410 481 GLU A N   
3915 C CA  . GLU A 491 ? 0.4065 0.4625 0.3806 0.0034  -0.0148 -0.0412 481 GLU A CA  
3916 C C   . GLU A 491 ? 0.3888 0.4557 0.3660 0.0034  -0.0131 -0.0444 481 GLU A C   
3917 O O   . GLU A 491 ? 0.3802 0.4518 0.3550 0.0053  -0.0148 -0.0447 481 GLU A O   
3918 C CB  . GLU A 491 ? 0.4249 0.4796 0.4003 -0.0013 -0.0132 -0.0405 481 GLU A CB  
3919 C CG  . GLU A 491 ? 0.4477 0.5073 0.4212 -0.0027 -0.0139 -0.0403 481 GLU A CG  
3920 C CD  . GLU A 491 ? 0.4716 0.5267 0.4386 0.0002  -0.0183 -0.0373 481 GLU A CD  
3921 O OE1 . GLU A 491 ? 0.4965 0.5423 0.4600 0.0015  -0.0205 -0.0347 481 GLU A OE1 
3922 O OE2 . GLU A 491 ? 0.4923 0.5528 0.4574 0.0011  -0.0196 -0.0376 481 GLU A OE2 
3923 N N   . ILE A 492 ? 0.3732 0.4440 0.3555 0.0011  -0.0098 -0.0468 482 ILE A N   
3924 C CA  . ILE A 492 ? 0.3787 0.4599 0.3641 0.0004  -0.0079 -0.0499 482 ILE A CA  
3925 C C   . ILE A 492 ? 0.3890 0.4745 0.3722 0.0052  -0.0101 -0.0505 482 ILE A C   
3926 O O   . ILE A 492 ? 0.3760 0.4697 0.3588 0.0062  -0.0106 -0.0520 482 ILE A O   
3927 C CB  . ILE A 492 ? 0.3686 0.4518 0.3595 -0.0033 -0.0042 -0.0520 482 ILE A CB  
3928 C CG1 . ILE A 492 ? 0.3700 0.4519 0.3634 -0.0078 -0.0021 -0.0523 482 ILE A CG1 
3929 C CG2 . ILE A 492 ? 0.3676 0.4611 0.3611 -0.0038 -0.0027 -0.0550 482 ILE A CG2 
3930 C CD1 . ILE A 492 ? 0.3705 0.4506 0.3685 -0.0111 0.0009  -0.0536 482 ILE A CD1 
3931 N N   . PHE A 493 ? 0.3960 0.4764 0.3780 0.0083  -0.0114 -0.0496 483 PHE A N   
3932 C CA  . PHE A 493 ? 0.4178 0.5021 0.3975 0.0135  -0.0137 -0.0504 483 PHE A CA  
3933 C C   . PHE A 493 ? 0.4346 0.5181 0.4092 0.0174  -0.0175 -0.0491 483 PHE A C   
3934 O O   . PHE A 493 ? 0.4444 0.5356 0.4181 0.0205  -0.0187 -0.0507 483 PHE A O   
3935 C CB  . PHE A 493 ? 0.4214 0.4999 0.4003 0.0162  -0.0147 -0.0496 483 PHE A CB  
3936 C CG  . PHE A 493 ? 0.4228 0.5027 0.4065 0.0129  -0.0113 -0.0507 483 PHE A CG  
3937 C CD1 . PHE A 493 ? 0.4250 0.4963 0.4092 0.0118  -0.0108 -0.0489 483 PHE A CD1 
3938 C CD2 . PHE A 493 ? 0.4329 0.5229 0.4203 0.0109  -0.0088 -0.0534 483 PHE A CD2 
3939 C CE1 . PHE A 493 ? 0.4245 0.4966 0.4127 0.0089  -0.0080 -0.0496 483 PHE A CE1 
3940 C CE2 . PHE A 493 ? 0.4297 0.5202 0.4210 0.0077  -0.0060 -0.0540 483 PHE A CE2 
3941 C CZ  . PHE A 493 ? 0.4228 0.5043 0.4145 0.0068  -0.0057 -0.0520 483 PHE A CZ  
3942 N N   . GLU A 494 ? 0.4539 0.5282 0.4250 0.0170  -0.0194 -0.0462 484 GLU A N   
3943 C CA  . GLU A 494 ? 0.4877 0.5594 0.4533 0.0203  -0.0233 -0.0444 484 GLU A CA  
3944 C C   . GLU A 494 ? 0.4843 0.5651 0.4503 0.0190  -0.0228 -0.0455 484 GLU A C   
3945 O O   . GLU A 494 ? 0.4868 0.5710 0.4497 0.0230  -0.0256 -0.0456 484 GLU A O   
3946 C CB  . GLU A 494 ? 0.5195 0.5797 0.4815 0.0190  -0.0251 -0.0408 484 GLU A CB  
3947 C CG  . GLU A 494 ? 0.5569 0.6071 0.5158 0.0224  -0.0276 -0.0392 484 GLU A CG  
3948 C CD  . GLU A 494 ? 0.5882 0.6273 0.5438 0.0201  -0.0290 -0.0357 484 GLU A CD  
3949 O OE1 . GLU A 494 ? 0.6089 0.6400 0.5633 0.0213  -0.0299 -0.0347 484 GLU A OE1 
3950 O OE2 . GLU A 494 ? 0.6038 0.6426 0.5580 0.0169  -0.0291 -0.0341 484 GLU A OE2 
3951 N N   . GLN A 495 ? 0.4667 0.5516 0.4366 0.0135  -0.0195 -0.0464 485 GLN A N   
3952 C CA  . GLN A 495 ? 0.4649 0.5590 0.4355 0.0117  -0.0187 -0.0478 485 GLN A CA  
3953 C C   . GLN A 495 ? 0.4689 0.5748 0.4422 0.0131  -0.0175 -0.0512 485 GLN A C   
3954 O O   . GLN A 495 ? 0.4638 0.5770 0.4356 0.0145  -0.0187 -0.0519 485 GLN A O   
3955 C CB  . GLN A 495 ? 0.4592 0.5543 0.4332 0.0055  -0.0155 -0.0483 485 GLN A CB  
3956 C CG  . GLN A 495 ? 0.4629 0.5490 0.4339 0.0038  -0.0169 -0.0450 485 GLN A CG  
3957 C CD  . GLN A 495 ? 0.4624 0.5517 0.4360 -0.0016 -0.0142 -0.0457 485 GLN A CD  
3958 O OE1 . GLN A 495 ? 0.4709 0.5696 0.4471 -0.0035 -0.0124 -0.0482 485 GLN A OE1 
3959 N NE2 . GLN A 495 ? 0.4512 0.5332 0.4241 -0.0040 -0.0141 -0.0436 485 GLN A NE2 
3960 N N   . LEU A 496 ? 0.4660 0.5740 0.4430 0.0125  -0.0152 -0.0532 486 LEU A N   
3961 C CA  . LEU A 496 ? 0.4759 0.5950 0.4551 0.0139  -0.0143 -0.0563 486 LEU A CA  
3962 C C   . LEU A 496 ? 0.4935 0.6137 0.4692 0.0207  -0.0178 -0.0562 486 LEU A C   
3963 O O   . LEU A 496 ? 0.5020 0.6325 0.4788 0.0225  -0.0175 -0.0587 486 LEU A O   
3964 C CB  . LEU A 496 ? 0.4649 0.5858 0.4490 0.0104  -0.0107 -0.0582 486 LEU A CB  
3965 C CG  . LEU A 496 ? 0.4613 0.5825 0.4496 0.0039  -0.0070 -0.0591 486 LEU A CG  
3966 C CD1 . LEU A 496 ? 0.4570 0.5775 0.4493 0.0012  -0.0043 -0.0603 486 LEU A CD1 
3967 C CD2 . LEU A 496 ? 0.4565 0.5881 0.4464 0.0013  -0.0057 -0.0615 486 LEU A CD2 
3968 N N   . ASN A 497 ? 0.5167 0.6263 0.4881 0.0243  -0.0210 -0.0534 487 ASN A N   
3969 C CA  . ASN A 497 ? 0.5463 0.6546 0.5137 0.0312  -0.0248 -0.0533 487 ASN A CA  
3970 C C   . ASN A 497 ? 0.5489 0.6630 0.5192 0.0330  -0.0236 -0.0558 487 ASN A C   
3971 O O   . ASN A 497 ? 0.5416 0.6637 0.5111 0.0376  -0.0251 -0.0578 487 ASN A O   
3972 C CB  . ASN A 497 ? 0.5598 0.6745 0.5242 0.0348  -0.0276 -0.0535 487 ASN A CB  
3973 C CG  . ASN A 497 ? 0.5780 0.6875 0.5369 0.0423  -0.0325 -0.0525 487 ASN A CG  
3974 O OD1 . ASN A 497 ? 0.5884 0.6858 0.5442 0.0440  -0.0347 -0.0501 487 ASN A OD1 
3975 N ND2 . ASN A 497 ? 0.5870 0.7056 0.5447 0.0470  -0.0344 -0.0543 487 ASN A ND2 
3976 N N   . ILE A 498 ? 0.5553 0.6658 0.5288 0.0292  -0.0207 -0.0558 488 ILE A N   
3977 C CA  . ILE A 498 ? 0.5648 0.6784 0.5405 0.0304  -0.0197 -0.0574 488 ILE A CA  
3978 C C   . ILE A 498 ? 0.5753 0.6774 0.5475 0.0343  -0.0225 -0.0554 488 ILE A C   
3979 O O   . ILE A 498 ? 0.5556 0.6479 0.5279 0.0315  -0.0218 -0.0532 488 ILE A O   
3980 C CB  . ILE A 498 ? 0.5652 0.6809 0.5462 0.0239  -0.0152 -0.0583 488 ILE A CB  
3981 C CG1 . ILE A 498 ? 0.5581 0.6849 0.5422 0.0201  -0.0127 -0.0606 488 ILE A CG1 
3982 C CG2 . ILE A 498 ? 0.5600 0.6783 0.5429 0.0249  -0.0143 -0.0595 488 ILE A CG2 
3983 C CD1 . ILE A 498 ? 0.5580 0.6852 0.5469 0.0133  -0.0085 -0.0612 488 ILE A CD1 
3984 N N   . ASN A 499 ? 0.5838 0.6875 0.5529 0.0409  -0.0259 -0.0562 489 ASN A N   
3985 C CA  . ASN A 499 ? 0.6082 0.7011 0.5731 0.0456  -0.0293 -0.0546 489 ASN A CA  
3986 C C   . ASN A 499 ? 0.5993 0.6934 0.5656 0.0475  -0.0288 -0.0561 489 ASN A C   
3987 O O   . ASN A 499 ? 0.6051 0.6892 0.5691 0.0494  -0.0305 -0.0547 489 ASN A O   
3988 C CB  . ASN A 499 ? 0.6278 0.7201 0.5875 0.0522  -0.0340 -0.0546 489 ASN A CB  
3989 C CG  . ASN A 499 ? 0.6356 0.7243 0.5927 0.0506  -0.0352 -0.0524 489 ASN A CG  
3990 O OD1 . ASN A 499 ? 0.6542 0.7320 0.6093 0.0480  -0.0357 -0.0493 489 ASN A OD1 
3991 N ND2 . ASN A 499 ? 0.6435 0.7421 0.6006 0.0519  -0.0356 -0.0538 489 ASN A ND2 
3992 N N   . ASN A 500 ? 0.5768 0.6836 0.5468 0.0470  -0.0266 -0.0590 490 ASN A N   
3993 C CA  . ASN A 500 ? 0.5740 0.6841 0.5459 0.0481  -0.0257 -0.0606 490 ASN A CA  
3994 C C   . ASN A 500 ? 0.5591 0.6611 0.5333 0.0429  -0.0231 -0.0586 490 ASN A C   
3995 O O   . ASN A 500 ? 0.5327 0.6373 0.5107 0.0368  -0.0195 -0.0583 490 ASN A O   
3996 C CB  . ASN A 500 ? 0.5747 0.7007 0.5502 0.0468  -0.0233 -0.0637 490 ASN A CB  
3997 C CG  . ASN A 500 ? 0.5828 0.7145 0.5600 0.0481  -0.0226 -0.0655 490 ASN A CG  
3998 O OD1 . ASN A 500 ? 0.5873 0.7113 0.5631 0.0502  -0.0238 -0.0646 490 ASN A OD1 
3999 N ND2 . ASN A 500 ? 0.5769 0.7229 0.5572 0.0465  -0.0205 -0.0681 490 ASN A ND2 
4000 N N   . PRO A 501 ? 0.5594 0.6516 0.5312 0.0454  -0.0249 -0.0572 491 PRO A N   
4001 C CA  . PRO A 501 ? 0.5394 0.6241 0.5134 0.0408  -0.0226 -0.0552 491 PRO A CA  
4002 C C   . PRO A 501 ? 0.5171 0.6100 0.4962 0.0365  -0.0188 -0.0564 491 PRO A C   
4003 O O   . PRO A 501 ? 0.4800 0.5685 0.4617 0.0312  -0.0161 -0.0548 491 PRO A O   
4004 C CB  . PRO A 501 ? 0.5581 0.6340 0.5285 0.0454  -0.0256 -0.0544 491 PRO A CB  
4005 C CG  . PRO A 501 ? 0.5736 0.6479 0.5392 0.0516  -0.0299 -0.0550 491 PRO A CG  
4006 C CD  . PRO A 501 ? 0.5702 0.6580 0.5374 0.0527  -0.0293 -0.0577 491 PRO A CD  
4007 N N   . GLN A 502 ? 0.5102 0.6149 0.4903 0.0387  -0.0186 -0.0592 492 GLN A N   
4008 C CA  . GLN A 502 ? 0.5168 0.6306 0.5013 0.0344  -0.0153 -0.0604 492 GLN A CA  
4009 C C   . GLN A 502 ? 0.4887 0.6057 0.4767 0.0278  -0.0119 -0.0602 492 GLN A C   
4010 O O   . GLN A 502 ? 0.4607 0.5789 0.4521 0.0227  -0.0089 -0.0598 492 GLN A O   
4011 C CB  . GLN A 502 ? 0.5587 0.6859 0.5431 0.0383  -0.0161 -0.0636 492 GLN A CB  
4012 C CG  . GLN A 502 ? 0.5909 0.7289 0.5794 0.0338  -0.0129 -0.0649 492 GLN A CG  
4013 C CD  . GLN A 502 ? 0.6178 0.7498 0.6078 0.0309  -0.0114 -0.0630 492 GLN A CD  
4014 O OE1 . GLN A 502 ? 0.6667 0.7960 0.6550 0.0348  -0.0132 -0.0630 492 GLN A OE1 
4015 N NE2 . GLN A 502 ? 0.6311 0.7611 0.6243 0.0240  -0.0082 -0.0615 492 GLN A NE2 
4016 N N   . PHE A 503 ? 0.4628 0.5813 0.4499 0.0279  -0.0124 -0.0606 493 PHE A N   
4017 C CA  . PHE A 503 ? 0.4515 0.5730 0.4417 0.0219  -0.0095 -0.0607 493 PHE A CA  
4018 C C   . PHE A 503 ? 0.4320 0.5420 0.4231 0.0177  -0.0081 -0.0582 493 PHE A C   
4019 O O   . PHE A 503 ? 0.4030 0.5143 0.3965 0.0130  -0.0058 -0.0584 493 PHE A O   
4020 C CB  . PHE A 503 ? 0.4598 0.5881 0.4488 0.0235  -0.0105 -0.0622 493 PHE A CB  
4021 C CG  . PHE A 503 ? 0.4742 0.6161 0.4630 0.0269  -0.0114 -0.0652 493 PHE A CG  
4022 C CD1 . PHE A 503 ? 0.4840 0.6311 0.4704 0.0307  -0.0136 -0.0664 493 PHE A CD1 
4023 C CD2 . PHE A 503 ? 0.4757 0.6257 0.4665 0.0261  -0.0100 -0.0667 493 PHE A CD2 
4024 C CE1 . PHE A 503 ? 0.4887 0.6491 0.4750 0.0341  -0.0144 -0.0692 493 PHE A CE1 
4025 C CE2 . PHE A 503 ? 0.4832 0.6469 0.4739 0.0292  -0.0108 -0.0696 493 PHE A CE2 
4026 C CZ  . PHE A 503 ? 0.4893 0.6582 0.4777 0.0334  -0.0130 -0.0710 493 PHE A CZ  
4027 N N   . MET A 504 ? 0.4239 0.5234 0.4132 0.0194  -0.0094 -0.0560 494 MET A N   
4028 C CA  . MET A 504 ? 0.4268 0.5159 0.4170 0.0156  -0.0081 -0.0536 494 MET A CA  
4029 C C   . MET A 504 ? 0.4141 0.5003 0.4069 0.0130  -0.0062 -0.0527 494 MET A C   
4030 O O   . MET A 504 ? 0.3814 0.4594 0.3752 0.0102  -0.0051 -0.0508 494 MET A O   
4031 C CB  . MET A 504 ? 0.4457 0.5246 0.4318 0.0189  -0.0112 -0.0515 494 MET A CB  
4032 C CG  . MET A 504 ? 0.4643 0.5451 0.4471 0.0220  -0.0136 -0.0519 494 MET A CG  
4033 S SD  . MET A 504 ? 0.4993 0.5679 0.4761 0.0262  -0.0179 -0.0493 494 MET A SD  
4034 C CE  . MET A 504 ? 0.5038 0.5778 0.4774 0.0297  -0.0205 -0.0503 494 MET A CE  
4035 N N   . GLU A 505 ? 0.4014 0.4949 0.3953 0.0139  -0.0058 -0.0540 495 GLU A N   
4036 C CA  . GLU A 505 ? 0.4030 0.4947 0.3989 0.0118  -0.0043 -0.0531 495 GLU A CA  
4037 C C   . GLU A 505 ? 0.3769 0.4755 0.3769 0.0062  -0.0011 -0.0539 495 GLU A C   
4038 O O   . GLU A 505 ? 0.3658 0.4731 0.3668 0.0049  -0.0003 -0.0559 495 GLU A O   
4039 C CB  . GLU A 505 ? 0.4210 0.5160 0.4149 0.0166  -0.0063 -0.0538 495 GLU A CB  
4040 C CG  . GLU A 505 ? 0.4362 0.5242 0.4257 0.0224  -0.0099 -0.0532 495 GLU A CG  
4041 C CD  . GLU A 505 ? 0.4559 0.5310 0.4445 0.0214  -0.0102 -0.0504 495 GLU A CD  
4042 O OE1 . GLU A 505 ? 0.4705 0.5426 0.4619 0.0172  -0.0079 -0.0490 495 GLU A OE1 
4043 O OE2 . GLU A 505 ? 0.4843 0.5523 0.4691 0.0249  -0.0130 -0.0495 495 GLU A OE2 
4044 N N   . PHE A 506 ? 0.3625 0.4569 0.3645 0.0030  0.0004  -0.0523 496 PHE A N   
4045 C CA  . PHE A 506 ? 0.3608 0.4594 0.3664 -0.0026 0.0033  -0.0526 496 PHE A CA  
4046 C C   . PHE A 506 ? 0.3690 0.4805 0.3752 -0.0029 0.0037  -0.0547 496 PHE A C   
4047 O O   . PHE A 506 ? 0.3615 0.4788 0.3699 -0.0074 0.0057  -0.0558 496 PHE A O   
4048 C CB  . PHE A 506 ? 0.3538 0.4458 0.3611 -0.0052 0.0045  -0.0503 496 PHE A CB  
4049 C CG  . PHE A 506 ? 0.3442 0.4250 0.3523 -0.0070 0.0051  -0.0484 496 PHE A CG  
4050 C CD1 . PHE A 506 ? 0.3423 0.4150 0.3499 -0.0061 0.0046  -0.0461 496 PHE A CD1 
4051 C CD2 . PHE A 506 ? 0.3398 0.4186 0.3492 -0.0097 0.0062  -0.0491 496 PHE A CD2 
4052 C CE1 . PHE A 506 ? 0.3366 0.3999 0.3451 -0.0077 0.0052  -0.0444 496 PHE A CE1 
4053 C CE2 . PHE A 506 ? 0.3360 0.4055 0.3463 -0.0111 0.0068  -0.0476 496 PHE A CE2 
4054 C CZ  . PHE A 506 ? 0.3349 0.3967 0.3447 -0.0101 0.0063  -0.0453 496 PHE A CZ  
4055 N N   . SER A 507 ? 0.3945 0.5106 0.3987 0.0015  0.0019  -0.0553 497 SER A N   
4056 C CA  . SER A 507 ? 0.4121 0.5417 0.4166 0.0018  0.0021  -0.0576 497 SER A CA  
4057 C C   . SER A 507 ? 0.4163 0.5550 0.4207 0.0019  0.0021  -0.0601 497 SER A C   
4058 O O   . SER A 507 ? 0.4239 0.5740 0.4297 -0.0005 0.0033  -0.0619 497 SER A O   
4059 C CB  . SER A 507 ? 0.4272 0.5600 0.4293 0.0077  -0.0002 -0.0582 497 SER A CB  
4060 O OG  . SER A 507 ? 0.4529 0.5816 0.4519 0.0137  -0.0030 -0.0588 497 SER A OG  
4061 N N   . SER A 508 ? 0.4109 0.5449 0.4137 0.0046  0.0007  -0.0603 498 SER A N   
4062 C CA  . SER A 508 ? 0.4024 0.5443 0.4051 0.0047  0.0007  -0.0625 498 SER A CA  
4063 C C   . SER A 508 ? 0.4103 0.5536 0.4160 -0.0020 0.0035  -0.0629 498 SER A C   
4064 O O   . SER A 508 ? 0.3987 0.5495 0.4046 -0.0026 0.0038  -0.0649 498 SER A O   
4065 C CB  . SER A 508 ? 0.4034 0.5398 0.4030 0.0097  -0.0018 -0.0623 498 SER A CB  
4066 O OG  . SER A 508 ? 0.3894 0.5148 0.3893 0.0072  -0.0012 -0.0604 498 SER A OG  
4067 N N   . LEU A 509 ? 0.4130 0.5491 0.4209 -0.0069 0.0055  -0.0611 499 LEU A N   
4068 C CA  . LEU A 509 ? 0.4275 0.5641 0.4383 -0.0134 0.0082  -0.0616 499 LEU A CA  
4069 C C   . LEU A 509 ? 0.4454 0.5904 0.4581 -0.0182 0.0100  -0.0623 499 LEU A C   
4070 O O   . LEU A 509 ? 0.4376 0.5829 0.4525 -0.0240 0.0121  -0.0628 499 LEU A O   
4071 C CB  . LEU A 509 ? 0.4299 0.5532 0.4419 -0.0160 0.0092  -0.0594 499 LEU A CB  
4072 C CG  . LEU A 509 ? 0.4324 0.5466 0.4425 -0.0120 0.0074  -0.0582 499 LEU A CG  
4073 C CD1 . LEU A 509 ? 0.4332 0.5360 0.4449 -0.0150 0.0087  -0.0564 499 LEU A CD1 
4074 C CD2 . LEU A 509 ? 0.4301 0.5486 0.4389 -0.0103 0.0066  -0.0600 499 LEU A CD2 
4075 N N   . GLU A 510 ? 0.4703 0.6224 0.4821 -0.0160 0.0092  -0.0625 500 GLU A N   
4076 C CA  . GLU A 510 ? 0.5013 0.6621 0.5146 -0.0207 0.0108  -0.0629 500 GLU A CA  
4077 C C   . GLU A 510 ? 0.4937 0.6661 0.5079 -0.0243 0.0120  -0.0655 500 GLU A C   
4078 O O   . GLU A 510 ? 0.4764 0.6513 0.4924 -0.0308 0.0140  -0.0655 500 GLU A O   
4079 C CB  . GLU A 510 ? 0.5292 0.6968 0.5411 -0.0169 0.0094  -0.0629 500 GLU A CB  
4080 C CG  . GLU A 510 ? 0.5660 0.7234 0.5774 -0.0154 0.0088  -0.0601 500 GLU A CG  
4081 C CD  . GLU A 510 ? 0.5850 0.7496 0.5949 -0.0113 0.0074  -0.0606 500 GLU A CD  
4082 O OE1 . GLU A 510 ? 0.5978 0.7760 0.6073 -0.0099 0.0069  -0.0631 500 GLU A OE1 
4083 O OE2 . GLU A 510 ? 0.5984 0.7555 0.6078 -0.0095 0.0067  -0.0585 500 GLU A OE2 
4084 N N   . GLN A 511 ? 0.4909 0.6702 0.5036 -0.0200 0.0106  -0.0678 501 GLN A N   
4085 C CA  . GLN A 511 ? 0.5050 0.6963 0.5184 -0.0226 0.0115  -0.0705 501 GLN A CA  
4086 C C   . GLN A 511 ? 0.4831 0.6720 0.4959 -0.0202 0.0108  -0.0716 501 GLN A C   
4087 O O   . GLN A 511 ? 0.4768 0.6642 0.4873 -0.0138 0.0084  -0.0717 501 GLN A O   
4088 C CB  . GLN A 511 ? 0.5228 0.7296 0.5352 -0.0196 0.0105  -0.0726 501 GLN A CB  
4089 C CG  . GLN A 511 ? 0.5444 0.7652 0.5577 -0.0238 0.0118  -0.0753 501 GLN A CG  
4090 C CD  . GLN A 511 ? 0.5545 0.7917 0.5672 -0.0222 0.0112  -0.0773 501 GLN A CD  
4091 O OE1 . GLN A 511 ? 0.5521 0.7905 0.5635 -0.0173 0.0097  -0.0769 501 GLN A OE1 
4092 N NE2 . GLN A 511 ? 0.5603 0.8108 0.5739 -0.0263 0.0125  -0.0796 501 GLN A NE2 
4093 N N   . TYR A 512 ? 0.4681 0.6568 0.4827 -0.0257 0.0127  -0.0725 502 TYR A N   
4094 C CA  . TYR A 512 ? 0.4705 0.6572 0.4847 -0.0247 0.0124  -0.0736 502 TYR A CA  
4095 C C   . TYR A 512 ? 0.4666 0.6658 0.4791 -0.0203 0.0108  -0.0760 502 TYR A C   
4096 O O   . TYR A 512 ? 0.4434 0.6558 0.4563 -0.0216 0.0112  -0.0779 502 TYR A O   
4097 C CB  . TYR A 512 ? 0.4629 0.6484 0.4796 -0.0320 0.0149  -0.0746 502 TYR A CB  
4098 C CG  . TYR A 512 ? 0.4641 0.6458 0.4809 -0.0318 0.0149  -0.0755 502 TYR A CG  
4099 C CD1 . TYR A 512 ? 0.4586 0.6270 0.4763 -0.0330 0.0154  -0.0740 502 TYR A CD1 
4100 C CD2 . TYR A 512 ? 0.4551 0.6471 0.4712 -0.0305 0.0144  -0.0780 502 TYR A CD2 
4101 C CE1 . TYR A 512 ? 0.4558 0.6216 0.4736 -0.0330 0.0155  -0.0750 502 TYR A CE1 
4102 C CE2 . TYR A 512 ? 0.4561 0.6453 0.4722 -0.0305 0.0145  -0.0787 502 TYR A CE2 
4103 C CZ  . TYR A 512 ? 0.4520 0.6283 0.4690 -0.0319 0.0150  -0.0773 502 TYR A CZ  
4104 O OH  . TYR A 512 ? 0.4310 0.6057 0.4480 -0.0321 0.0151  -0.0783 502 TYR A OH  
4105 N N   . GLY A 513 ? 0.4635 0.6586 0.4740 -0.0149 0.0087  -0.0757 503 GLY A N   
4106 C CA  . GLY A 513 ? 0.4772 0.6826 0.4860 -0.0107 0.0070  -0.0777 503 GLY A CA  
4107 C C   . GLY A 513 ? 0.4816 0.6894 0.4874 -0.0027 0.0039  -0.0776 503 GLY A C   
4108 O O   . GLY A 513 ? 0.4705 0.6913 0.4756 0.0000  0.0030  -0.0798 503 GLY A O   
4109 N N   . VAL A 514 ? 0.4815 0.6770 0.4856 0.0010  0.0023  -0.0752 504 VAL A N   
4110 C CA  . VAL A 514 ? 0.4824 0.6779 0.4834 0.0087  -0.0009 -0.0750 504 VAL A CA  
4111 C C   . VAL A 514 ? 0.4868 0.6852 0.4849 0.0147  -0.0037 -0.0758 504 VAL A C   
4112 O O   . VAL A 514 ? 0.4886 0.6915 0.4843 0.0212  -0.0064 -0.0768 504 VAL A O   
4113 C CB  . VAL A 514 ? 0.4795 0.6604 0.4794 0.0106  -0.0019 -0.0721 504 VAL A CB  
4114 C CG1 . VAL A 514 ? 0.4756 0.6544 0.4781 0.0056  0.0004  -0.0711 504 VAL A CG1 
4115 C CG2 . VAL A 514 ? 0.4755 0.6436 0.4744 0.0102  -0.0023 -0.0699 504 VAL A CG2 
4116 N N   . LEU A 515 ? 0.4852 0.6811 0.4833 0.0127  -0.0033 -0.0755 505 LEU A N   
4117 C CA  . LEU A 515 ? 0.4992 0.6967 0.4942 0.0179  -0.0062 -0.0758 505 LEU A CA  
4118 C C   . LEU A 515 ? 0.5170 0.7313 0.5127 0.0185  -0.0060 -0.0790 505 LEU A C   
4119 O O   . LEU A 515 ? 0.5090 0.7285 0.5059 0.0148  -0.0046 -0.0801 505 LEU A O   
4120 C CB  . LEU A 515 ? 0.5007 0.6890 0.4954 0.0155  -0.0059 -0.0740 505 LEU A CB  
4121 C CG  . LEU A 515 ? 0.5056 0.6780 0.4998 0.0146  -0.0059 -0.0710 505 LEU A CG  
4122 C CD1 . LEU A 515 ? 0.5040 0.6700 0.4984 0.0110  -0.0050 -0.0698 505 LEU A CD1 
4123 C CD2 . LEU A 515 ? 0.5090 0.6736 0.4992 0.0214  -0.0096 -0.0692 505 LEU A CD2 
4124 N N   . ASN A 516 ? 0.5269 0.7499 0.5216 0.0232  -0.0076 -0.0806 506 ASN A N   
4125 C CA  . ASN A 516 ? 0.5371 0.7777 0.5324 0.0240  -0.0075 -0.0839 506 ASN A CA  
4126 C C   . ASN A 516 ? 0.5716 0.8167 0.5635 0.0318  -0.0112 -0.0848 506 ASN A C   
4127 O O   . ASN A 516 ? 0.5677 0.8278 0.5597 0.0338  -0.0116 -0.0876 506 ASN A O   
4128 C CB  . ASN A 516 ? 0.4914 0.7418 0.4883 0.0233  -0.0064 -0.0857 506 ASN A CB  
4129 C CG  . ASN A 516 ? 0.4906 0.7361 0.4853 0.0298  -0.0090 -0.0850 506 ASN A CG  
4130 O OD1 . ASN A 516 ? 0.4984 0.7383 0.4899 0.0369  -0.0125 -0.0844 506 ASN A OD1 
4131 N ND2 . ASN A 516 ? 0.5057 0.7533 0.5021 0.0275  -0.0076 -0.0852 506 ASN A ND2 
4132 N N   . GLU A 517 ? 0.6201 0.8522 0.6088 0.0363  -0.0140 -0.0823 507 GLU A N   
4133 C CA  . GLU A 517 ? 0.6672 0.9002 0.6523 0.0426  -0.0176 -0.0823 507 GLU A CA  
4134 C C   . GLU A 517 ? 0.6666 0.8906 0.6510 0.0392  -0.0172 -0.0799 507 GLU A C   
4135 O O   . GLU A 517 ? 0.6496 0.8635 0.6356 0.0338  -0.0150 -0.0780 507 GLU A O   
4136 C CB  . GLU A 517 ? 0.7171 0.9420 0.6983 0.0509  -0.0218 -0.0813 507 GLU A CB  
4137 C CG  . GLU A 517 ? 0.7582 0.9924 0.7397 0.0551  -0.0225 -0.0839 507 GLU A CG  
4138 C CD  . GLU A 517 ? 0.8006 1.0235 0.7788 0.0616  -0.0259 -0.0827 507 GLU A CD  
4139 O OE1 . GLU A 517 ? 0.8306 1.0559 0.8101 0.0621  -0.0252 -0.0839 507 GLU A OE1 
4140 O OE2 . GLU A 517 ? 0.8330 1.0446 0.8073 0.0659  -0.0292 -0.0806 507 GLU A OE2 
4141 N N   . SER A 518 ? 0.6578 0.8861 0.6399 0.0424  -0.0194 -0.0801 508 SER A N   
4142 C CA  . SER A 518 ? 0.6550 0.8757 0.6360 0.0398  -0.0195 -0.0778 508 SER A CA  
4143 C C   . SER A 518 ? 0.6551 0.8586 0.6323 0.0430  -0.0223 -0.0742 508 SER A C   
4144 O O   . SER A 518 ? 0.6397 0.8389 0.6140 0.0494  -0.0255 -0.0738 508 SER A O   
4145 C CB  . SER A 518 ? 0.6603 0.8913 0.6396 0.0426  -0.0213 -0.0789 508 SER A CB  
4146 O OG  . SER A 518 ? 0.6648 0.8940 0.6395 0.0513  -0.0260 -0.0783 508 SER A OG  
4147 N N   . ILE A 519 ? 0.6445 0.8385 0.6219 0.0383  -0.0211 -0.0718 509 ILE A N   
4148 C CA  . ILE A 519 ? 0.6413 0.8194 0.6151 0.0402  -0.0236 -0.0682 509 ILE A CA  
4149 C C   . ILE A 519 ? 0.6212 0.7959 0.5932 0.0379  -0.0241 -0.0662 509 ILE A C   
4150 O O   . ILE A 519 ? 0.5862 0.7674 0.5611 0.0325  -0.0212 -0.0673 509 ILE A O   
4151 C CB  . ILE A 519 ? 0.6513 0.8186 0.6270 0.0365  -0.0215 -0.0668 509 ILE A CB  
4152 C CG1 . ILE A 519 ? 0.6531 0.8238 0.6338 0.0284  -0.0167 -0.0679 509 ILE A CG1 
4153 C CG2 . ILE A 519 ? 0.6609 0.8287 0.6367 0.0404  -0.0223 -0.0679 509 ILE A CG2 
4154 C CD1 . ILE A 519 ? 0.6605 0.8205 0.6432 0.0246  -0.0147 -0.0664 509 ILE A CD1 
4155 N N   . MET A 520 ? 0.6157 0.7802 0.5827 0.0421  -0.0281 -0.0631 510 MET A N   
4156 C CA  . MET A 520 ? 0.6259 0.7859 0.5905 0.0400  -0.0291 -0.0606 510 MET A CA  
4157 C C   . MET A 520 ? 0.5992 0.7471 0.5646 0.0349  -0.0273 -0.0582 510 MET A C   
4158 O O   . MET A 520 ? 0.5783 0.7142 0.5408 0.0371  -0.0295 -0.0557 510 MET A O   
4159 C CB  . MET A 520 ? 0.6549 0.8095 0.6132 0.0468  -0.0345 -0.0582 510 MET A CB  
4160 C CG  . MET A 520 ? 0.6768 0.8436 0.6338 0.0522  -0.0367 -0.0604 510 MET A CG  
4161 S SD  . MET A 520 ? 0.7047 0.8859 0.6641 0.0479  -0.0344 -0.0619 510 MET A SD  
4162 C CE  . MET A 520 ? 0.6972 0.8673 0.6522 0.0457  -0.0366 -0.0572 510 MET A CE  
4163 N N   . VAL A 521 ? 0.5785 0.7300 0.5477 0.0282  -0.0235 -0.0590 511 VAL A N   
4164 C CA  . VAL A 521 ? 0.5660 0.7074 0.5361 0.0232  -0.0218 -0.0570 511 VAL A CA  
4165 C C   . VAL A 521 ? 0.5598 0.6937 0.5250 0.0239  -0.0249 -0.0534 511 VAL A C   
4166 O O   . VAL A 521 ? 0.5585 0.6959 0.5202 0.0274  -0.0279 -0.0527 511 VAL A O   
4167 C CB  . VAL A 521 ? 0.5626 0.7099 0.5382 0.0161  -0.0171 -0.0593 511 VAL A CB  
4168 C CG1 . VAL A 521 ? 0.5497 0.7038 0.5298 0.0148  -0.0142 -0.0624 511 VAL A CG1 
4169 C CG2 . VAL A 521 ? 0.5631 0.7197 0.5389 0.0139  -0.0166 -0.0603 511 VAL A CG2 
4170 N N   . THR A 522 ? 0.5443 0.6682 0.5093 0.0204  -0.0242 -0.0511 512 THR A N   
4171 C CA  . THR A 522 ? 0.5535 0.6705 0.5139 0.0201  -0.0269 -0.0475 512 THR A CA  
4172 C C   . THR A 522 ? 0.5589 0.6851 0.5195 0.0174  -0.0262 -0.0481 512 THR A C   
4173 O O   . THR A 522 ? 0.5220 0.6572 0.4874 0.0133  -0.0225 -0.0511 512 THR A O   
4174 C CB  . THR A 522 ? 0.5500 0.6560 0.5103 0.0161  -0.0259 -0.0452 512 THR A CB  
4175 O OG1 . THR A 522 ? 0.5482 0.6481 0.5033 0.0159  -0.0290 -0.0415 512 THR A OG1 
4176 C CG2 . THR A 522 ? 0.5357 0.6464 0.5018 0.0097  -0.0211 -0.0474 512 THR A CG2 
4177 N N   . GLY A 523 ? 0.5876 0.7113 0.5428 0.0196  -0.0300 -0.0452 513 GLY A N   
4178 C CA  . GLY A 523 ? 0.6103 0.7418 0.5649 0.0170  -0.0299 -0.0450 513 GLY A CA  
4179 C C   . GLY A 523 ? 0.6246 0.7517 0.5791 0.0112  -0.0287 -0.0430 513 GLY A C   
4180 O O   . GLY A 523 ? 0.6174 0.7521 0.5727 0.0078  -0.0275 -0.0435 513 GLY A O   
4181 N N   . GLN A 524 ? 0.6370 0.7524 0.5904 0.0103  -0.0290 -0.0407 514 GLN A N   
4182 C CA  . GLN A 524 ? 0.6541 0.7650 0.6072 0.0050  -0.0280 -0.0387 514 GLN A CA  
4183 C C   . GLN A 524 ? 0.6287 0.7355 0.5865 0.0020  -0.0245 -0.0403 514 GLN A C   
4184 O O   . GLN A 524 ? 0.6055 0.7017 0.5613 0.0021  -0.0256 -0.0379 514 GLN A O   
4185 C CB  . GLN A 524 ? 0.6973 0.7973 0.6432 0.0065  -0.0326 -0.0337 514 GLN A CB  
4186 C CG  . GLN A 524 ? 0.7332 0.8365 0.6740 0.0084  -0.0362 -0.0314 514 GLN A CG  
4187 C CD  . GLN A 524 ? 0.7634 0.8689 0.7021 0.0152  -0.0391 -0.0321 514 GLN A CD  
4188 O OE1 . GLN A 524 ? 0.7855 0.8853 0.7238 0.0196  -0.0402 -0.0326 514 GLN A OE1 
4189 N NE2 . GLN A 524 ? 0.7859 0.9003 0.7231 0.0164  -0.0404 -0.0322 514 GLN A NE2 
4190 N N   . PRO A 525 ? 0.6085 0.7237 0.5724 -0.0008 -0.0203 -0.0444 515 PRO A N   
4191 C CA  . PRO A 525 ? 0.5985 0.7096 0.5668 -0.0037 -0.0170 -0.0458 515 PRO A CA  
4192 C C   . PRO A 525 ? 0.5818 0.6881 0.5497 -0.0080 -0.0164 -0.0439 515 PRO A C   
4193 O O   . PRO A 525 ? 0.5782 0.6881 0.5442 -0.0103 -0.0171 -0.0429 515 PRO A O   
4194 C CB  . PRO A 525 ? 0.5971 0.7187 0.5713 -0.0062 -0.0131 -0.0504 515 PRO A CB  
4195 C CG  . PRO A 525 ? 0.6057 0.7372 0.5788 -0.0067 -0.0138 -0.0511 515 PRO A CG  
4196 C CD  . PRO A 525 ? 0.6098 0.7380 0.5766 -0.0019 -0.0184 -0.0477 515 PRO A CD  
4197 N N   . LYS A 526 ? 0.5507 0.6495 0.5203 -0.0091 -0.0151 -0.0435 516 LYS A N   
4198 C CA  . LYS A 526 ? 0.5363 0.6307 0.5059 -0.0130 -0.0144 -0.0420 516 LYS A CA  
4199 C C   . LYS A 526 ? 0.4885 0.5810 0.4635 -0.0152 -0.0108 -0.0444 516 LYS A C   
4200 O O   . LYS A 526 ? 0.4505 0.5427 0.4282 -0.0133 -0.0097 -0.0461 516 LYS A O   
4201 C CB  . LYS A 526 ? 0.5751 0.6592 0.5385 -0.0114 -0.0182 -0.0374 516 LYS A CB  
4202 C CG  . LYS A 526 ? 0.6056 0.6811 0.5676 -0.0073 -0.0198 -0.0362 516 LYS A CG  
4203 C CD  . LYS A 526 ? 0.6376 0.7023 0.5936 -0.0065 -0.0234 -0.0318 516 LYS A CD  
4204 C CE  . LYS A 526 ? 0.6525 0.7083 0.6080 -0.0035 -0.0242 -0.0312 516 LYS A CE  
4205 N NZ  . LYS A 526 ? 0.6802 0.7253 0.6307 -0.0040 -0.0270 -0.0272 516 LYS A NZ  
4206 N N   . PRO A 527 ? 0.4571 0.5487 0.4338 -0.0191 -0.0091 -0.0444 517 PRO A N   
4207 C CA  . PRO A 527 ? 0.4456 0.5358 0.4276 -0.0209 -0.0058 -0.0469 517 PRO A CA  
4208 C C   . PRO A 527 ? 0.4301 0.5111 0.4119 -0.0185 -0.0065 -0.0454 517 PRO A C   
4209 O O   . PRO A 527 ? 0.4066 0.4802 0.3841 -0.0171 -0.0091 -0.0419 517 PRO A O   
4210 C CB  . PRO A 527 ? 0.4555 0.5460 0.4382 -0.0249 -0.0048 -0.0467 517 PRO A CB  
4211 C CG  . PRO A 527 ? 0.4648 0.5615 0.4443 -0.0261 -0.0063 -0.0458 517 PRO A CG  
4212 C CD  . PRO A 527 ? 0.4658 0.5591 0.4400 -0.0221 -0.0100 -0.0427 517 PRO A CD  
4213 N N   . ILE A 528 ? 0.4212 0.5031 0.4075 -0.0183 -0.0041 -0.0479 518 ILE A N   
4214 C CA  . ILE A 528 ? 0.4213 0.4956 0.4080 -0.0163 -0.0041 -0.0469 518 ILE A CA  
4215 C C   . ILE A 528 ? 0.4232 0.4911 0.4105 -0.0183 -0.0035 -0.0455 518 ILE A C   
4216 O O   . ILE A 528 ? 0.4161 0.4763 0.4013 -0.0166 -0.0050 -0.0431 518 ILE A O   
4217 C CB  . ILE A 528 ? 0.4199 0.4977 0.4116 -0.0164 -0.0015 -0.0501 518 ILE A CB  
4218 C CG1 . ILE A 528 ? 0.4222 0.5076 0.4134 -0.0146 -0.0020 -0.0517 518 ILE A CG1 
4219 C CG2 . ILE A 528 ? 0.4247 0.4954 0.4169 -0.0146 -0.0016 -0.0489 518 ILE A CG2 
4220 C CD1 . ILE A 528 ? 0.4305 0.5140 0.4169 -0.0101 -0.0055 -0.0495 518 ILE A CD1 
4221 N N   . PHE A 529 ? 0.4187 0.4902 0.4088 -0.0219 -0.0015 -0.0472 519 PHE A N   
4222 C CA  . PHE A 529 ? 0.4333 0.5004 0.4245 -0.0239 -0.0006 -0.0464 519 PHE A CA  
4223 C C   . PHE A 529 ? 0.4779 0.5477 0.4664 -0.0264 -0.0016 -0.0452 519 PHE A C   
4224 O O   . PHE A 529 ? 0.4912 0.5680 0.4791 -0.0273 -0.0017 -0.0462 519 PHE A O   
4225 C CB  . PHE A 529 ? 0.4057 0.4747 0.4030 -0.0258 0.0027  -0.0499 519 PHE A CB  
4226 C CG  . PHE A 529 ? 0.3860 0.4523 0.3856 -0.0240 0.0036  -0.0507 519 PHE A CG  
4227 C CD1 . PHE A 529 ? 0.3746 0.4465 0.3767 -0.0241 0.0050  -0.0535 519 PHE A CD1 
4228 C CD2 . PHE A 529 ? 0.3767 0.4354 0.3758 -0.0224 0.0030  -0.0485 519 PHE A CD2 
4229 C CE1 . PHE A 529 ? 0.3716 0.4417 0.3757 -0.0229 0.0057  -0.0541 519 PHE A CE1 
4230 C CE2 . PHE A 529 ? 0.3688 0.4257 0.3699 -0.0209 0.0038  -0.0491 519 PHE A CE2 
4231 C CZ  . PHE A 529 ? 0.3655 0.4281 0.3691 -0.0213 0.0051  -0.0518 519 PHE A CZ  
4232 N N   . PRO A 530 ? 0.5472 0.6125 0.5342 -0.0277 -0.0023 -0.0429 520 PRO A N   
4233 C CA  . PRO A 530 ? 0.5641 0.6219 0.5521 -0.0269 -0.0019 -0.0418 520 PRO A CA  
4234 C C   . PRO A 530 ? 0.5813 0.6311 0.5647 -0.0239 -0.0048 -0.0383 520 PRO A C   
4235 O O   . PRO A 530 ? 0.6172 0.6671 0.5973 -0.0217 -0.0069 -0.0374 520 PRO A O   
4236 C CB  . PRO A 530 ? 0.5747 0.6328 0.5623 -0.0300 -0.0016 -0.0410 520 PRO A CB  
4237 C CG  . PRO A 530 ? 0.5764 0.6390 0.5600 -0.0316 -0.0034 -0.0396 520 PRO A CG  
4238 C CD  . PRO A 530 ? 0.5738 0.6425 0.5585 -0.0306 -0.0030 -0.0419 520 PRO A CD  
# 
