data_9EIZ
# 
_entry.id   9EIZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9EIZ         pdb_00009eiz 10.2210/pdb9eiz/pdb 
WWPDB D_1000290516 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-09 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EIZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ret6@cornell.edu 
_pdbx_contact_author.name_first         Robert 
_pdbx_contact_author.name_last          Thorne 
_pdbx_contact_author.name_mi            E. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7489-8074 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'McLeod, M.J.'    1 0000-0001-5540-916X 
'Barwell, S.A.E.' 2 0000-0002-5703-5525 
'Holyoak, T.'     3 0000-0002-7329-1115 
'Thorne, R.E.'    4 0000-0002-7489-8074 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                924 
_citation.page_last                 934.e2 
_citation.title                     'A structural perspective on the temperature dependent activity of enzymes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2025.02.013 
_citation.pdbx_database_id_PubMed   40120576 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McLeod, M.J.'    1 ? 
primary 'Barwell, S.A.E.' 2 ? 
primary 'Holyoak, T.'     3 ? 
primary 'Thorne, R.E.'    4 ? 
# 
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 'Phosphoenolpyruvate carboxykinase, cytosolic [GTP]' 69499.664 1  4.1.1.32 ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'                                 54.938    3  ?        ? ? ? 
3 non-polymer syn 'OXALATE ION'                                        88.019    1  ?        ? ? ? 
4 non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"                          523.180   1  ?        ? ? ? 
5 non-polymer syn 'TRIETHYLENE GLYCOL'                                 150.173   1  ?        ? ? ? 
6 water       nat water                                                18.015    87 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        PEPCK-C 
# 
_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       
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_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 'MANGANESE (II) ION'        MN  
3 'OXALATE ION'               OXL 
4 "GUANOSINE-5'-TRIPHOSPHATE" GTP 
5 'TRIETHYLENE GLYCOL'        PGE 
6 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   PRO n 
1 3   PRO n 
1 4   GLN n 
1 5   LEU n 
1 6   HIS n 
1 7   ASN n 
1 8   GLY n 
1 9   LEU n 
1 10  ASP n 
1 11  PHE n 
1 12  SER n 
1 13  ALA n 
1 14  LYS n 
1 15  VAL n 
1 16  ILE n 
1 17  GLN n 
1 18  GLY n 
1 19  SER n 
1 20  LEU n 
1 21  ASP n 
1 22  SER n 
1 23  LEU n 
1 24  PRO n 
1 25  GLN n 
1 26  GLU n 
1 27  VAL n 
1 28  ARG n 
1 29  LYS n 
1 30  PHE n 
1 31  VAL n 
1 32  GLU n 
1 33  GLY n 
1 34  ASN n 
1 35  ALA n 
1 36  GLN n 
1 37  LEU n 
1 38  CYS n 
1 39  GLN n 
1 40  PRO n 
1 41  GLU n 
1 42  TYR n 
1 43  ILE n 
1 44  HIS n 
1 45  ILE n 
1 46  CYS n 
1 47  ASP n 
1 48  GLY n 
1 49  SER n 
1 50  GLU n 
1 51  GLU n 
1 52  GLU n 
1 53  TYR n 
1 54  GLY n 
1 55  ARG n 
1 56  LEU n 
1 57  LEU n 
1 58  ALA n 
1 59  HIS n 
1 60  MET n 
1 61  GLN n 
1 62  GLU n 
1 63  GLU n 
1 64  GLY n 
1 65  VAL n 
1 66  ILE n 
1 67  ARG n 
1 68  LYS n 
1 69  LEU n 
1 70  LYS n 
1 71  LYS n 
1 72  TYR n 
1 73  ASP n 
1 74  ASN n 
1 75  CYS n 
1 76  TRP n 
1 77  LEU n 
1 78  ALA n 
1 79  LEU n 
1 80  THR n 
1 81  ASP n 
1 82  PRO n 
1 83  ARG n 
1 84  ASP n 
1 85  VAL n 
1 86  ALA n 
1 87  ARG n 
1 88  ILE n 
1 89  GLU n 
1 90  SER n 
1 91  LYS n 
1 92  THR n 
1 93  VAL n 
1 94  ILE n 
1 95  ILE n 
1 96  THR n 
1 97  GLN n 
1 98  GLU n 
1 99  GLN n 
1 100 ARG n 
1 101 ASP n 
1 102 THR n 
1 103 VAL n 
1 104 PRO n 
1 105 ILE n 
1 106 PRO n 
1 107 LYS n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 SER n 
1 112 GLN n 
1 113 LEU n 
1 114 GLY n 
1 115 ARG n 
1 116 TRP n 
1 117 MET n 
1 118 SER n 
1 119 GLU n 
1 120 GLU n 
1 121 ASP n 
1 122 PHE n 
1 123 GLU n 
1 124 LYS n 
1 125 ALA n 
1 126 PHE n 
1 127 ASN n 
1 128 ALA n 
1 129 ARG n 
1 130 PHE n 
1 131 PRO n 
1 132 GLY n 
1 133 CYS n 
1 134 MET n 
1 135 LYS n 
1 136 GLY n 
1 137 ARG n 
1 138 THR n 
1 139 MET n 
1 140 TYR n 
1 141 VAL n 
1 142 ILE n 
1 143 PRO n 
1 144 PHE n 
1 145 SER n 
1 146 MET n 
1 147 GLY n 
1 148 PRO n 
1 149 LEU n 
1 150 GLY n 
1 151 SER n 
1 152 PRO n 
1 153 LEU n 
1 154 ALA n 
1 155 LYS n 
1 156 ILE n 
1 157 GLY n 
1 158 ILE n 
1 159 GLU n 
1 160 LEU n 
1 161 THR n 
1 162 ASP n 
1 163 SER n 
1 164 PRO n 
1 165 TYR n 
1 166 VAL n 
1 167 VAL n 
1 168 ALA n 
1 169 SER n 
1 170 MET n 
1 171 ARG n 
1 172 ILE n 
1 173 MET n 
1 174 THR n 
1 175 ARG n 
1 176 MET n 
1 177 GLY n 
1 178 THR n 
1 179 SER n 
1 180 VAL n 
1 181 LEU n 
1 182 GLU n 
1 183 ALA n 
1 184 LEU n 
1 185 GLY n 
1 186 ASP n 
1 187 GLY n 
1 188 GLU n 
1 189 PHE n 
1 190 ILE n 
1 191 LYS n 
1 192 CYS n 
1 193 LEU n 
1 194 HIS n 
1 195 SER n 
1 196 VAL n 
1 197 GLY n 
1 198 CYS n 
1 199 PRO n 
1 200 LEU n 
1 201 PRO n 
1 202 LEU n 
1 203 LYS n 
1 204 LYS n 
1 205 PRO n 
1 206 LEU n 
1 207 VAL n 
1 208 ASN n 
1 209 ASN n 
1 210 TRP n 
1 211 ALA n 
1 212 CYS n 
1 213 ASN n 
1 214 PRO n 
1 215 GLU n 
1 216 LEU n 
1 217 THR n 
1 218 LEU n 
1 219 ILE n 
1 220 ALA n 
1 221 HIS n 
1 222 LEU n 
1 223 PRO n 
1 224 ASP n 
1 225 ARG n 
1 226 ARG n 
1 227 GLU n 
1 228 ILE n 
1 229 ILE n 
1 230 SER n 
1 231 PHE n 
1 232 GLY n 
1 233 SER n 
1 234 GLY n 
1 235 TYR n 
1 236 GLY n 
1 237 GLY n 
1 238 ASN n 
1 239 SER n 
1 240 LEU n 
1 241 LEU n 
1 242 GLY n 
1 243 LYS n 
1 244 LYS n 
1 245 CYS n 
1 246 PHE n 
1 247 ALA n 
1 248 LEU n 
1 249 ARG n 
1 250 ILE n 
1 251 ALA n 
1 252 SER n 
1 253 ARG n 
1 254 LEU n 
1 255 ALA n 
1 256 LYS n 
1 257 GLU n 
1 258 GLU n 
1 259 GLY n 
1 260 TRP n 
1 261 LEU n 
1 262 ALA n 
1 263 GLU n 
1 264 HIS n 
1 265 MET n 
1 266 LEU n 
1 267 ILE n 
1 268 LEU n 
1 269 GLY n 
1 270 ILE n 
1 271 THR n 
1 272 ASN n 
1 273 PRO n 
1 274 GLU n 
1 275 GLY n 
1 276 LYS n 
1 277 LYS n 
1 278 LYS n 
1 279 TYR n 
1 280 LEU n 
1 281 ALA n 
1 282 ALA n 
1 283 ALA n 
1 284 PHE n 
1 285 PRO n 
1 286 SER n 
1 287 ALA n 
1 288 CYS n 
1 289 GLY n 
1 290 LYS n 
1 291 THR n 
1 292 ASN n 
1 293 LEU n 
1 294 ALA n 
1 295 MET n 
1 296 MET n 
1 297 ASN n 
1 298 PRO n 
1 299 THR n 
1 300 LEU n 
1 301 PRO n 
1 302 GLY n 
1 303 TRP n 
1 304 LYS n 
1 305 VAL n 
1 306 GLU n 
1 307 CYS n 
1 308 VAL n 
1 309 GLY n 
1 310 ASP n 
1 311 ASP n 
1 312 ILE n 
1 313 ALA n 
1 314 TRP n 
1 315 MET n 
1 316 LYS n 
1 317 PHE n 
1 318 ASP n 
1 319 ALA n 
1 320 GLN n 
1 321 GLY n 
1 322 ASN n 
1 323 LEU n 
1 324 ARG n 
1 325 ALA n 
1 326 ILE n 
1 327 ASN n 
1 328 PRO n 
1 329 GLU n 
1 330 ASN n 
1 331 GLY n 
1 332 PHE n 
1 333 PHE n 
1 334 GLY n 
1 335 VAL n 
1 336 ALA n 
1 337 PRO n 
1 338 GLY n 
1 339 THR n 
1 340 SER n 
1 341 VAL n 
1 342 LYS n 
1 343 THR n 
1 344 ASN n 
1 345 PRO n 
1 346 ASN n 
1 347 ALA n 
1 348 ILE n 
1 349 LYS n 
1 350 THR n 
1 351 ILE n 
1 352 GLN n 
1 353 LYS n 
1 354 ASN n 
1 355 THR n 
1 356 ILE n 
1 357 PHE n 
1 358 THR n 
1 359 ASN n 
1 360 VAL n 
1 361 ALA n 
1 362 GLU n 
1 363 THR n 
1 364 SER n 
1 365 ASP n 
1 366 GLY n 
1 367 GLY n 
1 368 VAL n 
1 369 TYR n 
1 370 TRP n 
1 371 GLU n 
1 372 GLY n 
1 373 ILE n 
1 374 ASP n 
1 375 GLU n 
1 376 PRO n 
1 377 LEU n 
1 378 ALA n 
1 379 PRO n 
1 380 GLY n 
1 381 VAL n 
1 382 THR n 
1 383 ILE n 
1 384 THR n 
1 385 SER n 
1 386 TRP n 
1 387 LYS n 
1 388 ASN n 
1 389 LYS n 
1 390 GLU n 
1 391 TRP n 
1 392 ARG n 
1 393 PRO n 
1 394 GLN n 
1 395 ASP n 
1 396 GLU n 
1 397 GLU n 
1 398 PRO n 
1 399 CYS n 
1 400 ALA n 
1 401 HIS n 
1 402 PRO n 
1 403 ASN n 
1 404 SER n 
1 405 ARG n 
1 406 PHE n 
1 407 CYS n 
1 408 THR n 
1 409 PRO n 
1 410 ALA n 
1 411 SER n 
1 412 GLN n 
1 413 CYS n 
1 414 PRO n 
1 415 ILE n 
1 416 ILE n 
1 417 ASP n 
1 418 PRO n 
1 419 ALA n 
1 420 TRP n 
1 421 GLU n 
1 422 SER n 
1 423 PRO n 
1 424 GLU n 
1 425 GLY n 
1 426 VAL n 
1 427 PRO n 
1 428 ILE n 
1 429 GLU n 
1 430 GLY n 
1 431 ILE n 
1 432 ILE n 
1 433 PHE n 
1 434 GLY n 
1 435 GLY n 
1 436 ARG n 
1 437 ARG n 
1 438 PRO n 
1 439 ALA n 
1 440 GLY n 
1 441 VAL n 
1 442 PRO n 
1 443 LEU n 
1 444 VAL n 
1 445 TYR n 
1 446 GLU n 
1 447 ALA n 
1 448 LEU n 
1 449 SER n 
1 450 TRP n 
1 451 GLN n 
1 452 HIS n 
1 453 GLY n 
1 454 VAL n 
1 455 PHE n 
1 456 VAL n 
1 457 GLY n 
1 458 ALA n 
1 459 ALA n 
1 460 MET n 
1 461 ARG n 
1 462 SER n 
1 463 GLU n 
1 464 ALA n 
1 465 THR n 
1 466 ALA n 
1 467 ALA n 
1 468 ALA n 
1 469 GLU n 
1 470 HIS n 
1 471 LYS n 
1 472 GLY n 
1 473 LYS n 
1 474 VAL n 
1 475 ILE n 
1 476 MET n 
1 477 HIS n 
1 478 ASP n 
1 479 PRO n 
1 480 PHE n 
1 481 ALA n 
1 482 MET n 
1 483 ARG n 
1 484 PRO n 
1 485 PHE n 
1 486 PHE n 
1 487 GLY n 
1 488 TYR n 
1 489 ASN n 
1 490 PHE n 
1 491 GLY n 
1 492 LYS n 
1 493 TYR n 
1 494 LEU n 
1 495 ALA n 
1 496 HIS n 
1 497 TRP n 
1 498 LEU n 
1 499 SER n 
1 500 MET n 
1 501 ALA n 
1 502 HIS n 
1 503 ARG n 
1 504 PRO n 
1 505 ALA n 
1 506 ALA n 
1 507 LYS n 
1 508 LEU n 
1 509 PRO n 
1 510 LYS n 
1 511 ILE n 
1 512 PHE n 
1 513 HIS n 
1 514 VAL n 
1 515 ASN n 
1 516 TRP n 
1 517 PHE n 
1 518 ARG n 
1 519 LYS n 
1 520 ASP n 
1 521 LYS n 
1 522 ASN n 
1 523 GLY n 
1 524 LYS n 
1 525 PHE n 
1 526 LEU n 
1 527 TRP n 
1 528 PRO n 
1 529 GLY n 
1 530 PHE n 
1 531 GLY n 
1 532 GLU n 
1 533 ASN n 
1 534 SER n 
1 535 ARG n 
1 536 VAL n 
1 537 LEU n 
1 538 GLU n 
1 539 TRP n 
1 540 MET n 
1 541 PHE n 
1 542 GLY n 
1 543 ARG n 
1 544 ILE n 
1 545 GLU n 
1 546 GLY n 
1 547 GLU n 
1 548 ASP n 
1 549 SER n 
1 550 ALA n 
1 551 LYS n 
1 552 LEU n 
1 553 THR n 
1 554 PRO n 
1 555 ILE n 
1 556 GLY n 
1 557 TYR n 
1 558 VAL n 
1 559 PRO n 
1 560 LYS n 
1 561 GLU n 
1 562 ASP n 
1 563 ALA n 
1 564 LEU n 
1 565 ASN n 
1 566 LEU n 
1 567 LYS n 
1 568 GLY n 
1 569 LEU n 
1 570 GLY n 
1 571 ASP n 
1 572 VAL n 
1 573 ASN n 
1 574 VAL n 
1 575 GLU n 
1 576 GLU n 
1 577 LEU n 
1 578 PHE n 
1 579 GLY n 
1 580 ILE n 
1 581 SER n 
1 582 LYS n 
1 583 GLU n 
1 584 PHE n 
1 585 TRP n 
1 586 GLU n 
1 587 LYS n 
1 588 GLU n 
1 589 VAL n 
1 590 GLU n 
1 591 GLU n 
1 592 ILE n 
1 593 ASP n 
1 594 LYS n 
1 595 TYR n 
1 596 LEU n 
1 597 GLU n 
1 598 ASP n 
1 599 GLN n 
1 600 VAL n 
1 601 ASN n 
1 602 ALA n 
1 603 ASP n 
1 604 LEU n 
1 605 PRO n 
1 606 TYR n 
1 607 GLU n 
1 608 ILE n 
1 609 GLU n 
1 610 ARG n 
1 611 GLU n 
1 612 LEU n 
1 613 ARG n 
1 614 ALA n 
1 615 LEU n 
1 616 LYS n 
1 617 GLN n 
1 618 ARG n 
1 619 ILE n 
1 620 SER n 
1 621 GLN n 
1 622 MET 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                   622 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Pck1 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
GTP non-polymer         n "GUANOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O14 P3' 523.180 
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 
MN  non-polymer         . 'MANGANESE (II) ION'        ? 'Mn 2'              54.938  
OXL non-polymer         . 'OXALATE ION'               ? 'C2 O4 -2'          88.019  
PGE non-polymer         . 'TRIETHYLENE GLYCOL'        ? 'C6 H14 O4'         150.173 
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   HIS 6   6   6   HIS HIS A . n 
A 1 7   ASN 7   7   7   ASN ASN A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  ASN 34  34  34  ASN ASN A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  HIS 44  44  44  HIS HIS A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  CYS 46  46  46  CYS CYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  MET 60  60  60  MET MET A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  CYS 75  75  75  CYS CYS A . n 
A 1 76  TRP 76  76  76  TRP TRP A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 TRP 116 116 116 TRP TRP A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 MET 134 134 134 MET MET A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 MET 139 139 139 MET MET A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 MET 146 146 146 MET MET A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 MET 170 170 170 MET MET A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 CYS 192 192 192 CYS CYS A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 HIS 194 194 194 HIS HIS A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 TRP 210 210 210 TRP TRP A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 CYS 212 212 212 CYS CYS A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 ILE 228 228 228 ILE ILE A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 CYS 245 245 245 CYS CYS A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 TRP 260 260 260 TRP TRP A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 MET 265 265 265 MET MET A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 PRO 273 273 273 PRO PRO A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 CYS 288 288 288 CYS CYS A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 THR 291 291 291 THR THR A . n 
A 1 292 ASN 292 292 292 ASN ASN A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 MET 295 295 295 MET MET A . n 
A 1 296 MET 296 296 296 MET MET A . n 
A 1 297 ASN 297 297 297 ASN ASN A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 TRP 303 303 303 TRP TRP A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 CYS 307 307 307 CYS CYS A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 TRP 314 314 314 TRP TRP A . n 
A 1 315 MET 315 315 315 MET MET A . n 
A 1 316 LYS 316 316 316 LYS LYS A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 ARG 324 324 324 ARG ARG A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 ILE 326 326 326 ILE ILE A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 PRO 328 328 328 PRO PRO A . n 
A 1 329 GLU 329 329 329 GLU GLU A . n 
A 1 330 ASN 330 330 330 ASN ASN A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 PHE 333 333 333 PHE PHE A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 LYS 342 342 342 LYS LYS A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 ASN 346 346 346 ASN ASN A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 GLN 352 352 352 GLN GLN A . n 
A 1 353 LYS 353 353 353 LYS LYS A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 ILE 356 356 356 ILE ILE A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 ASN 359 359 359 ASN ASN A . n 
A 1 360 VAL 360 360 360 VAL VAL A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 THR 363 363 363 THR THR A . n 
A 1 364 SER 364 364 364 SER SER A . n 
A 1 365 ASP 365 365 365 ASP ASP A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 TRP 370 370 370 TRP TRP A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 PRO 379 379 379 PRO PRO A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 SER 385 385 385 SER SER A . n 
A 1 386 TRP 386 386 386 TRP TRP A . n 
A 1 387 LYS 387 387 387 LYS LYS A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 LYS 389 389 389 LYS LYS A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 ARG 392 392 392 ARG ARG A . n 
A 1 393 PRO 393 393 393 PRO PRO A . n 
A 1 394 GLN 394 394 394 GLN GLN A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 PRO 398 398 398 PRO PRO A . n 
A 1 399 CYS 399 399 399 CYS CYS A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 HIS 401 401 401 HIS HIS A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 ASN 403 403 403 ASN ASN A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 ARG 405 405 405 ARG ARG A . n 
A 1 406 PHE 406 406 406 PHE PHE A . n 
A 1 407 CYS 407 407 407 CYS CYS A . n 
A 1 408 THR 408 408 408 THR THR A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 SER 411 411 411 SER SER A . n 
A 1 412 GLN 412 412 412 GLN GLN A . n 
A 1 413 CYS 413 413 413 CYS CYS A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 ILE 416 416 416 ILE ILE A . n 
A 1 417 ASP 417 417 417 ASP ASP A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 TRP 420 420 420 TRP TRP A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 SER 422 422 422 SER SER A . n 
A 1 423 PRO 423 423 423 PRO PRO A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 PRO 427 427 427 PRO PRO A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 GLY 430 430 430 GLY GLY A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 PHE 433 433 433 PHE PHE A . n 
A 1 434 GLY 434 434 434 GLY GLY A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 ARG 436 436 436 ARG ARG A . n 
A 1 437 ARG 437 437 437 ARG ARG A . n 
A 1 438 PRO 438 438 438 PRO PRO A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 GLY 440 440 440 GLY GLY A . n 
A 1 441 VAL 441 441 441 VAL VAL A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 VAL 444 444 444 VAL VAL A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 SER 449 449 449 SER SER A . n 
A 1 450 TRP 450 450 450 TRP TRP A . n 
A 1 451 GLN 451 451 451 GLN GLN A . n 
A 1 452 HIS 452 452 452 HIS HIS A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 MET 460 460 460 MET MET A . n 
A 1 461 ARG 461 461 461 ARG ARG A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 ALA 464 464 464 ALA ALA A . n 
A 1 465 THR 465 465 465 THR THR A . n 
A 1 466 ALA 466 466 466 ALA ALA A . n 
A 1 467 ALA 467 467 467 ALA ALA A . n 
A 1 468 ALA 468 468 468 ALA ALA A . n 
A 1 469 GLU 469 469 469 GLU GLU A . n 
A 1 470 HIS 470 470 470 HIS HIS A . n 
A 1 471 LYS 471 471 471 LYS LYS A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 LYS 473 473 473 LYS LYS A . n 
A 1 474 VAL 474 474 474 VAL VAL A . n 
A 1 475 ILE 475 475 475 ILE ILE A . n 
A 1 476 MET 476 476 476 MET MET A . n 
A 1 477 HIS 477 477 477 HIS HIS A . n 
A 1 478 ASP 478 478 478 ASP ASP A . n 
A 1 479 PRO 479 479 479 PRO PRO A . n 
A 1 480 PHE 480 480 480 PHE PHE A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 MET 482 482 482 MET MET A . n 
A 1 483 ARG 483 483 483 ARG ARG A . n 
A 1 484 PRO 484 484 484 PRO PRO A . n 
A 1 485 PHE 485 485 485 PHE PHE A . n 
A 1 486 PHE 486 486 486 PHE PHE A . n 
A 1 487 GLY 487 487 487 GLY GLY A . n 
A 1 488 TYR 488 488 488 TYR TYR A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 PHE 490 490 490 PHE PHE A . n 
A 1 491 GLY 491 491 491 GLY GLY A . n 
A 1 492 LYS 492 492 492 LYS LYS A . n 
A 1 493 TYR 493 493 493 TYR TYR A . n 
A 1 494 LEU 494 494 494 LEU LEU A . n 
A 1 495 ALA 495 495 495 ALA ALA A . n 
A 1 496 HIS 496 496 496 HIS HIS A . n 
A 1 497 TRP 497 497 497 TRP TRP A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 SER 499 499 499 SER SER A . n 
A 1 500 MET 500 500 500 MET MET A . n 
A 1 501 ALA 501 501 501 ALA ALA A . n 
A 1 502 HIS 502 502 502 HIS HIS A . n 
A 1 503 ARG 503 503 503 ARG ARG A . n 
A 1 504 PRO 504 504 504 PRO PRO A . n 
A 1 505 ALA 505 505 505 ALA ALA A . n 
A 1 506 ALA 506 506 506 ALA ALA A . n 
A 1 507 LYS 507 507 507 LYS LYS A . n 
A 1 508 LEU 508 508 508 LEU LEU A . n 
A 1 509 PRO 509 509 509 PRO PRO A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 ILE 511 511 511 ILE ILE A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 HIS 513 513 513 HIS HIS A . n 
A 1 514 VAL 514 514 514 VAL VAL A . n 
A 1 515 ASN 515 515 515 ASN ASN A . n 
A 1 516 TRP 516 516 516 TRP TRP A . n 
A 1 517 PHE 517 517 517 PHE PHE A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 LYS 519 519 519 LYS LYS A . n 
A 1 520 ASP 520 520 520 ASP ASP A . n 
A 1 521 LYS 521 521 521 LYS LYS A . n 
A 1 522 ASN 522 522 522 ASN ASN A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 LYS 524 524 524 LYS LYS A . n 
A 1 525 PHE 525 525 525 PHE PHE A . n 
A 1 526 LEU 526 526 526 LEU LEU A . n 
A 1 527 TRP 527 527 527 TRP TRP A . n 
A 1 528 PRO 528 528 528 PRO PRO A . n 
A 1 529 GLY 529 529 529 GLY GLY A . n 
A 1 530 PHE 530 530 530 PHE PHE A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 GLU 532 532 532 GLU GLU A . n 
A 1 533 ASN 533 533 533 ASN ASN A . n 
A 1 534 SER 534 534 534 SER SER A . n 
A 1 535 ARG 535 535 535 ARG ARG A . n 
A 1 536 VAL 536 536 536 VAL VAL A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 TRP 539 539 539 TRP TRP A . n 
A 1 540 MET 540 540 540 MET MET A . n 
A 1 541 PHE 541 541 541 PHE PHE A . n 
A 1 542 GLY 542 542 542 GLY GLY A . n 
A 1 543 ARG 543 543 543 ARG ARG A . n 
A 1 544 ILE 544 544 544 ILE ILE A . n 
A 1 545 GLU 545 545 545 GLU GLU A . n 
A 1 546 GLY 546 546 546 GLY GLY A . n 
A 1 547 GLU 547 547 547 GLU GLU A . n 
A 1 548 ASP 548 548 548 ASP ASP A . n 
A 1 549 SER 549 549 549 SER SER A . n 
A 1 550 ALA 550 550 550 ALA ALA A . n 
A 1 551 LYS 551 551 551 LYS LYS A . n 
A 1 552 LEU 552 552 552 LEU LEU A . n 
A 1 553 THR 553 553 553 THR THR A . n 
A 1 554 PRO 554 554 554 PRO PRO A . n 
A 1 555 ILE 555 555 555 ILE ILE A . n 
A 1 556 GLY 556 556 556 GLY GLY A . n 
A 1 557 TYR 557 557 557 TYR TYR A . n 
A 1 558 VAL 558 558 558 VAL VAL A . n 
A 1 559 PRO 559 559 559 PRO PRO A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 GLU 561 561 561 GLU GLU A . n 
A 1 562 ASP 562 562 562 ASP ASP A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 LEU 564 564 564 LEU LEU A . n 
A 1 565 ASN 565 565 565 ASN ASN A . n 
A 1 566 LEU 566 566 566 LEU LEU A . n 
A 1 567 LYS 567 567 567 LYS LYS A . n 
A 1 568 GLY 568 568 568 GLY GLY A . n 
A 1 569 LEU 569 569 569 LEU LEU A . n 
A 1 570 GLY 570 570 570 GLY GLY A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 VAL 572 572 572 VAL VAL A . n 
A 1 573 ASN 573 573 573 ASN ASN A . n 
A 1 574 VAL 574 574 574 VAL VAL A . n 
A 1 575 GLU 575 575 575 GLU GLU A . n 
A 1 576 GLU 576 576 576 GLU GLU A . n 
A 1 577 LEU 577 577 577 LEU LEU A . n 
A 1 578 PHE 578 578 578 PHE PHE A . n 
A 1 579 GLY 579 579 579 GLY GLY A . n 
A 1 580 ILE 580 580 580 ILE ILE A . n 
A 1 581 SER 581 581 581 SER SER A . n 
A 1 582 LYS 582 582 582 LYS LYS A . n 
A 1 583 GLU 583 583 583 GLU GLU A . n 
A 1 584 PHE 584 584 584 PHE PHE A . n 
A 1 585 TRP 585 585 585 TRP TRP A . n 
A 1 586 GLU 586 586 586 GLU GLU A . n 
A 1 587 LYS 587 587 587 LYS LYS A . n 
A 1 588 GLU 588 588 588 GLU GLU A . n 
A 1 589 VAL 589 589 589 VAL VAL A . n 
A 1 590 GLU 590 590 590 GLU GLU A . n 
A 1 591 GLU 591 591 591 GLU GLU A . n 
A 1 592 ILE 592 592 592 ILE ILE A . n 
A 1 593 ASP 593 593 593 ASP ASP A . n 
A 1 594 LYS 594 594 594 LYS LYS A . n 
A 1 595 TYR 595 595 595 TYR TYR A . n 
A 1 596 LEU 596 596 596 LEU LEU A . n 
A 1 597 GLU 597 597 597 GLU GLU A . n 
A 1 598 ASP 598 598 598 ASP ASP A . n 
A 1 599 GLN 599 599 599 GLN GLN A . n 
A 1 600 VAL 600 600 600 VAL VAL A . n 
A 1 601 ASN 601 601 601 ASN ASN A . n 
A 1 602 ALA 602 602 602 ALA ALA A . n 
A 1 603 ASP 603 603 603 ASP ASP A . n 
A 1 604 LEU 604 604 604 LEU LEU A . n 
A 1 605 PRO 605 605 605 PRO PRO A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 GLU 607 607 607 GLU GLU A . n 
A 1 608 ILE 608 608 608 ILE ILE A . n 
A 1 609 GLU 609 609 609 GLU GLU A . n 
A 1 610 ARG 610 610 610 ARG ARG A . n 
A 1 611 GLU 611 611 611 GLU GLU A . n 
A 1 612 LEU 612 612 612 LEU LEU A . n 
A 1 613 ARG 613 613 613 ARG ARG A . n 
A 1 614 ALA 614 614 614 ALA ALA A . n 
A 1 615 LEU 615 615 615 LEU LEU A . n 
A 1 616 LYS 616 616 616 LYS LYS A . n 
A 1 617 GLN 617 617 617 GLN GLN A . n 
A 1 618 ARG 618 618 618 ARG ARG A . n 
A 1 619 ILE 619 619 619 ILE ILE A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 GLN 621 621 621 GLN GLN A . n 
A 1 622 MET 622 622 622 MET MET A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 GTP ? ? GTP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 OXL ? ? OXL ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 MN  1  701 700  MN  MN  A . 
C 2 MN  1  702 701  MN  MN  A . 
D 2 MN  1  703 702  MN  MN  A . 
E 3 OXL 1  704 800  OXL OXL A . 
F 4 GTP 1  705 900  GTP GTP A . 
G 5 PGE 1  706 1100 PGE 1PE A . 
H 6 HOH 1  801 42   HOH HOH A . 
H 6 HOH 2  802 44   HOH HOH A . 
H 6 HOH 3  803 56   HOH HOH A . 
H 6 HOH 4  804 1    HOH HOH A . 
H 6 HOH 5  805 49   HOH HOH A . 
H 6 HOH 6  806 12   HOH HOH A . 
H 6 HOH 7  807 82   HOH HOH A . 
H 6 HOH 8  808 58   HOH HOH A . 
H 6 HOH 9  809 52   HOH HOH A . 
H 6 HOH 10 810 70   HOH HOH A . 
H 6 HOH 11 811 54   HOH HOH A . 
H 6 HOH 12 812 77   HOH HOH A . 
H 6 HOH 13 813 59   HOH HOH A . 
H 6 HOH 14 814 83   HOH HOH A . 
H 6 HOH 15 815 75   HOH HOH A . 
H 6 HOH 16 816 67   HOH HOH A . 
H 6 HOH 17 817 81   HOH HOH A . 
H 6 HOH 18 818 62   HOH HOH A . 
H 6 HOH 19 819 76   HOH HOH A . 
H 6 HOH 20 820 51   HOH HOH A . 
H 6 HOH 21 821 17   HOH HOH A . 
H 6 HOH 22 822 11   HOH HOH A . 
H 6 HOH 23 823 10   HOH HOH A . 
H 6 HOH 24 824 68   HOH HOH A . 
H 6 HOH 25 825 34   HOH HOH A . 
H 6 HOH 26 826 41   HOH HOH A . 
H 6 HOH 27 827 43   HOH HOH A . 
H 6 HOH 28 828 45   HOH HOH A . 
H 6 HOH 29 829 13   HOH HOH A . 
H 6 HOH 30 830 66   HOH HOH A . 
H 6 HOH 31 831 39   HOH HOH A . 
H 6 HOH 32 832 4    HOH HOH A . 
H 6 HOH 33 833 55   HOH HOH A . 
H 6 HOH 34 834 84   HOH HOH A . 
H 6 HOH 35 835 60   HOH HOH A . 
H 6 HOH 36 836 29   HOH HOH A . 
H 6 HOH 37 837 50   HOH HOH A . 
H 6 HOH 38 838 9    HOH HOH A . 
H 6 HOH 39 839 69   HOH HOH A . 
H 6 HOH 40 840 30   HOH HOH A . 
H 6 HOH 41 841 80   HOH HOH A . 
H 6 HOH 42 842 57   HOH HOH A . 
H 6 HOH 43 843 79   HOH HOH A . 
H 6 HOH 44 844 48   HOH HOH A . 
H 6 HOH 45 845 63   HOH HOH A . 
H 6 HOH 46 846 28   HOH HOH A . 
H 6 HOH 47 847 85   HOH HOH A . 
H 6 HOH 48 848 8    HOH HOH A . 
H 6 HOH 49 849 21   HOH HOH A . 
H 6 HOH 50 850 18   HOH HOH A . 
H 6 HOH 51 851 23   HOH HOH A . 
H 6 HOH 52 852 40   HOH HOH A . 
H 6 HOH 53 853 6    HOH HOH A . 
H 6 HOH 54 854 16   HOH HOH A . 
H 6 HOH 55 855 7    HOH HOH A . 
H 6 HOH 56 856 19   HOH HOH A . 
H 6 HOH 57 857 2    HOH HOH A . 
H 6 HOH 58 858 38   HOH HOH A . 
H 6 HOH 59 859 53   HOH HOH A . 
H 6 HOH 60 860 33   HOH HOH A . 
H 6 HOH 61 861 24   HOH HOH A . 
H 6 HOH 62 862 37   HOH HOH A . 
H 6 HOH 63 863 65   HOH HOH A . 
H 6 HOH 64 864 27   HOH HOH A . 
H 6 HOH 65 865 5    HOH HOH A . 
H 6 HOH 66 866 64   HOH HOH A . 
H 6 HOH 67 867 20   HOH HOH A . 
H 6 HOH 68 868 46   HOH HOH A . 
H 6 HOH 69 869 3    HOH HOH A . 
H 6 HOH 70 870 72   HOH HOH A . 
H 6 HOH 71 871 22   HOH HOH A . 
H 6 HOH 72 872 78   HOH HOH A . 
H 6 HOH 73 873 15   HOH HOH A . 
H 6 HOH 74 874 26   HOH HOH A . 
H 6 HOH 75 875 35   HOH HOH A . 
H 6 HOH 76 876 36   HOH HOH A . 
H 6 HOH 77 877 71   HOH HOH A . 
H 6 HOH 78 878 73   HOH HOH A . 
H 6 HOH 79 879 14   HOH HOH A . 
H 6 HOH 80 880 25   HOH HOH A . 
H 6 HOH 81 881 74   HOH HOH A . 
H 6 HOH 82 882 47   HOH HOH A . 
H 6 HOH 83 883 31   HOH HOH A . 
H 6 HOH 84 884 86   HOH HOH A . 
H 6 HOH 85 885 61   HOH HOH A . 
H 6 HOH 86 886 32   HOH HOH A . 
H 6 HOH 87 887 87   HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.37 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EIZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.216 
_cell.length_a_esd                 ? 
_cell.length_b                     120.165 
_cell.length_b_esd                 ? 
_cell.length_c                     60.639 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EIZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EIZ 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES pH 7.5, 0.5 uL of 100 mM MnCl2, 10 mM GTP, and 18-28% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     253 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-01 
_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   1.1271 
_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                        'CHESS BEAMLINE 7B2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1271 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   7B2 
_diffrn_source.pdbx_synchrotron_site       CHESS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EIZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.04 
_reflns.d_resolution_low                               60.13 
_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                                     37701 
_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                           99.0500 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5500 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.3000 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.1930 
_reflns.pdbx_Rpim_I_all                                0.0750 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9920 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1770 
_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                                    2.05 
_reflns_shell.d_res_low                                     2.09 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.3000 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1863 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.5100 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.4620 
_reflns_shell.pdbx_Rpim_I_all                               0.5660 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.8370 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.1600 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.3450 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EIZ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.04 
_refine.ls_d_res_low                             56.47 
_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                     35852 
_refine.ls_number_reflns_R_free                  1667 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.65 
_refine.ls_percent_reflns_R_free                 4.65 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2095 
_refine.ls_R_factor_R_free                       0.2636 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2069 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.35 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.38 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4869 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             87 
_refine_hist.number_atoms_total               5007 
_refine_hist.d_res_high                       2.04 
_refine_hist.d_res_low                        56.47 
# 
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' ? 0.002  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.533  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.474 ? 1894 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 716  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 892  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.04 2.10  . . 110 1906 64.00 . . . . 0.3855 . . . . . . . . . . . 0.4136 
'X-RAY DIFFRACTION' 2.10 2.17  . . 141 2547 84.00 . . . . 0.3678 . . . . . . . . . . . 0.4246 
'X-RAY DIFFRACTION' 2.17 2.25  . . 132 2859 94.00 . . . . 0.3532 . . . . . . . . . . . 0.3833 
'X-RAY DIFFRACTION' 2.25 2.34  . . 145 2913 97.00 . . . . 0.3222 . . . . . . . . . . . 0.3466 
'X-RAY DIFFRACTION' 2.34 2.44  . . 163 2926 97.00 . . . . 0.2879 . . . . . . . . . . . 0.3489 
'X-RAY DIFFRACTION' 2.44 2.57  . . 119 2980 98.00 . . . . 0.2763 . . . . . . . . . . . 0.3256 
'X-RAY DIFFRACTION' 2.57 2.73  . . 126 2982 98.00 . . . . 0.2524 . . . . . . . . . . . 0.3073 
'X-RAY DIFFRACTION' 2.73 2.94  . . 128 3010 98.00 . . . . 0.2221 . . . . . . . . . . . 0.2966 
'X-RAY DIFFRACTION' 2.94 3.24  . . 152 3007 98.00 . . . . 0.2046 . . . . . . . . . . . 0.2644 
'X-RAY DIFFRACTION' 3.24 3.71  . . 154 2980 99.00 . . . . 0.1825 . . . . . . . . . . . 0.2407 
'X-RAY DIFFRACTION' 3.71 4.67  . . 144 3021 99.00 . . . . 0.1535 . . . . . . . . . . . 0.2303 
'X-RAY DIFFRACTION' 4.67 56.47 . . 153 3054 99.00 . . . . 0.1597 . . . . . . . . . . . 0.2010 
# 
_struct.entry_id                     9EIZ 
_struct.title                        'Rat cytosolic PEPCK in complex with GTP and oxalate (253K)' 
_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        9EIZ 
_struct_keywords.text            'Inhibitor complex, Metabolic enzyme, Multi-temperature, Ambient temperature, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PCKGC_RAT 
_struct_ref.pdbx_db_accession          P07379 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EIZ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 622 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P07379 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  622 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       622 
# 
_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 ASP A 10  ? ALA A 13  ? ASP A 10  ALA A 13  5 ? 4  
HELX_P HELX_P2  AA2 SER A 19  ? LEU A 23  ? SER A 19  LEU A 23  5 ? 5  
HELX_P HELX_P3  AA3 PRO A 24  ? GLN A 39  ? PRO A 24  GLN A 39  1 ? 16 
HELX_P HELX_P4  AA4 SER A 49  ? GLU A 63  ? SER A 49  GLU A 63  1 ? 15 
HELX_P HELX_P5  AA5 ILE A 88  ? SER A 90  ? ILE A 88  SER A 90  5 ? 3  
HELX_P HELX_P6  AA6 GLU A 98  ? VAL A 103 ? GLU A 98  VAL A 103 1 ? 6  
HELX_P HELX_P7  AA7 SER A 118 ? ALA A 128 ? SER A 118 ALA A 128 1 ? 11 
HELX_P HELX_P8  AA8 SER A 163 ? THR A 174 ? SER A 163 THR A 174 1 ? 12 
HELX_P HELX_P9  AA9 GLY A 177 ? GLY A 185 ? GLY A 177 GLY A 185 1 ? 9  
HELX_P HELX_P10 AB1 TYR A 235 ? LEU A 240 ? TYR A 235 LEU A 240 1 ? 6  
HELX_P HELX_P11 AB2 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P12 AB3 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P13 AB4 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P14 AB5 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P15 AB6 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P16 AB7 PRO A 479 ? PHE A 486 ? PRO A 479 PHE A 486 5 ? 8  
HELX_P HELX_P17 AB8 ASN A 489 ? SER A 499 ? ASN A 489 SER A 499 1 ? 11 
HELX_P HELX_P18 AB9 MET A 500 ? ARG A 503 ? MET A 500 ARG A 503 5 ? 4  
HELX_P HELX_P19 AC1 GLY A 529 ? GLU A 532 ? GLY A 529 GLU A 532 5 ? 4  
HELX_P HELX_P20 AC2 ASN A 533 ? GLY A 546 ? ASN A 533 GLY A 546 1 ? 14 
HELX_P HELX_P21 AC3 ASN A 573 ? PHE A 578 ? ASN A 573 PHE A 578 1 ? 6  
HELX_P HELX_P22 AC4 SER A 581 ? VAL A 600 ? SER A 581 VAL A 600 1 ? 20 
HELX_P HELX_P23 AC5 ASN A 601 ? LEU A 604 ? ASN A 601 LEU A 604 5 ? 4  
HELX_P HELX_P24 AC6 PRO A 605 ? GLN A 621 ? PRO A 605 GLN A 621 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A GLU 63  OE2 ? ? ? 1_555 D MN  . MN  ? ? A GLU 63  A MN  703 2_645 ? ? ? ? ? ? ? 2.571 ? ? 
metalc2  metalc ? ? A LYS 244 NZ  ? ? ? 1_555 C MN  . MN  ? ? A LYS 244 A MN  702 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc3  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 C MN  . MN  ? ? A HIS 264 A MN  702 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc4  metalc ? ? A THR 291 OG1 ? ? ? 1_555 B MN  . MN  ? ? A THR 291 A MN  701 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc5  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 C MN  . MN  ? ? A ASP 311 A MN  702 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc6  metalc ? ? A HIS 502 NE2 ? ? ? 1_555 D MN  . MN  ? ? A HIS 502 A MN  703 1_555 ? ? ? ? ? ? ? 2.725 ? ? 
metalc7  metalc ? ? A GLU 607 OE1 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 1_555 ? ? ? ? ? ? ? 2.571 ? ? 
metalc8  metalc ? ? A GLU 607 OE2 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 1_555 ? ? ? ? ? ? ? 2.621 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1G ? ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc10 metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1B ? ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.392 ? ? 
metalc11 metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 801 1_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc12 metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 826 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc13 metalc ? ? C MN  .   MN  ? ? ? 1_555 E OXL . O1  ? ? A MN  702 A OXL 704 1_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc14 metalc ? ? C MN  .   MN  ? ? ? 1_555 E OXL . O2  ? ? A MN  702 A OXL 704 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc15 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O3G ? ? A MN  702 A GTP 705 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 2_645 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 37.6  ? 
2  OE2 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 2_645 OE1 ? A GLU 607 ? A GLU 607 ? 1_555 38.5  ? 
3  NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 2_645 OE1 ? A GLU 607 ? A GLU 607 ? 1_555 4.9   ? 
4  OE2 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 2_645 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 40.0  ? 
5  NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 2_645 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 4.4   ? 
6  OE1 ? A GLU 607 ? A GLU 607 ? 1_555 MN ? D MN . ? A MN 703 ? 2_645 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 2.0   ? 
7  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 87.3  ? 
8  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 98.1  ? 
9  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 85.6  ? 
10 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O1  ? E OXL .   ? A OXL 704 ? 1_555 91.0  ? 
11 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O1  ? E OXL .   ? A OXL 704 ? 1_555 175.4 ? 
12 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O1  ? E OXL .   ? A OXL 704 ? 1_555 98.9  ? 
13 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2  ? E OXL .   ? A OXL 704 ? 1_555 91.1  ? 
14 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2  ? E OXL .   ? A OXL 704 ? 1_555 101.6 ? 
15 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2  ? E OXL .   ? A OXL 704 ? 1_555 168.6 ? 
16 O1  ? E OXL .   ? A OXL 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2  ? E OXL .   ? A OXL 704 ? 1_555 74.1  ? 
17 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 175.0 ? 
18 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 96.5  ? 
19 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 85.4  ? 
20 O1  ? E OXL .   ? A OXL 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 85.0  ? 
21 O2  ? E OXL .   ? A OXL 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 85.0  ? 
22 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G ? F GTP .   ? A GTP 705 ? 1_555 149.8 ? 
23 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1B ? F GTP .   ? A GTP 705 ? 1_555 85.8  ? 
24 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1B ? F GTP .   ? A GTP 705 ? 1_555 75.7  ? 
25 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 801 ? 1_555 83.8  ? 
26 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 801 ? 1_555 69.3  ? 
27 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 801 ? 1_555 78.2  ? 
28 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 826 ? 1_555 114.2 ? 
29 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 826 ? 1_555 87.5  ? 
30 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 826 ? 1_555 83.3  ? 
31 O   ? H HOH .   ? A HOH 801 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 826 ? 1_555 153.2 ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           200 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            200 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    201 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     201 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.72 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 7 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 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 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 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 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA1 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA1 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA1 4 LYS A 155 ? THR A 161 ? LYS A 155 THR A 161 
AA1 5 ILE A 190 ? SER A 195 ? ILE A 190 SER A 195 
AA1 6 GLU A 227 ? PHE A 231 ? GLU A 227 PHE A 231 
AA1 7 LEU A 218 ? LEU A 222 ? LEU A 218 LEU A 222 
AA1 8 THR A 92  ? ILE A 94  ? THR A 92  ILE A 94  
AA2 1 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA2 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA2 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA2 4 ARG A 175 ? MET A 176 ? ARG A 175 MET A 176 
AA3 1 ILE A 66  ? LEU A 69  ? ILE A 66  LEU A 69  
AA3 2 CYS A 75  ? ALA A 78  ? CYS A 75  ALA A 78  
AA3 3 ILE A 356 ? THR A 358 ? ILE A 356 THR A 358 
AA3 4 ARG A 405 ? PRO A 409 ? ARG A 405 PRO A 409 
AA3 5 GLY A 331 ? VAL A 335 ? GLY A 331 VAL A 335 
AA4 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA4 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA4 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA4 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA4 5 LYS A 277 ? ALA A 283 ? LYS A 277 ALA A 283 
AA4 6 LEU A 266 ? THR A 271 ? LEU A 266 THR A 271 
AA4 7 LYS A 304 ? GLY A 309 ? LYS A 304 GLY A 309 
AA5 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA5 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA5 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA5 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA5 5 LYS A 510 ? VAL A 514 ? LYS A 510 VAL A 514 
AA5 6 VAL A 444 ? GLU A 446 ? VAL A 444 GLU A 446 
AA6 1 VAL A 368 ? TYR A 369 ? VAL A 368 TYR A 369 
AA6 2 ALA A 361 ? THR A 363 ? ALA A 361 THR A 363 
AA6 3 ILE A 383 ? THR A 384 ? ILE A 383 THR A 384 
AA6 4 GLU A 390 ? TRP A 391 ? GLU A 390 TRP A 391 
AA7 1 ARG A 461 ? GLU A 463 ? ARG A 461 GLU A 463 
AA7 2 ILE A 475 ? HIS A 477 ? ILE A 475 HIS A 477 
AA8 1 ALA A 550 ? THR A 553 ? ALA A 550 THR A 553 
AA8 2 GLY A 556 ? PRO A 559 ? GLY A 556 PRO A 559 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 17  ? N GLN A 17  O ILE A 45  ? O ILE A 45  
AA1 2 3 N HIS A 44  ? N HIS A 44  O VAL A 141 ? O VAL A 141 
AA1 3 4 N PHE A 144 ? N PHE A 144 O GLY A 157 ? O GLY A 157 
AA1 4 5 N LEU A 160 ? N LEU A 160 O HIS A 194 ? O HIS A 194 
AA1 5 6 N LYS A 191 ? N LYS A 191 O ILE A 228 ? O ILE A 228 
AA1 6 7 O ILE A 229 ? O ILE A 229 N ALA A 220 ? N ALA A 220 
AA1 7 8 O ILE A 219 ? O ILE A 219 N VAL A 93  ? N VAL A 93  
AA2 1 2 N GLN A 17  ? N GLN A 17  O ILE A 45  ? O ILE A 45  
AA2 2 3 N HIS A 44  ? N HIS A 44  O VAL A 141 ? O VAL A 141 
AA2 3 4 N SER A 145 ? N SER A 145 O ARG A 175 ? O ARG A 175 
AA3 1 2 N ARG A 67  ? N ARG A 67  O LEU A 77  ? O LEU A 77  
AA3 2 3 N TRP A 76  ? N TRP A 76  O PHE A 357 ? O PHE A 357 
AA3 3 4 N THR A 358 ? N THR A 358 O ARG A 405 ? O ARG A 405 
AA3 4 5 O THR A 408 ? O THR A 408 N PHE A 332 ? N PHE A 332 
AA4 1 2 N LEU A 261 ? N LEU A 261 O MET A 315 ? O MET A 315 
AA4 2 3 N LYS A 316 ? N LYS A 316 O ARG A 324 ? O ARG A 324 
AA4 3 4 N LEU A 323 ? N LEU A 323 O ILE A 428 ? O ILE A 428 
AA4 4 5 O ILE A 432 ? O ILE A 432 N ALA A 283 ? N ALA A 283 
AA4 5 6 O LYS A 278 ? O LYS A 278 N ILE A 270 ? N ILE A 270 
AA4 6 7 N GLY A 269 ? N GLY A 269 O GLU A 306 ? O GLU A 306 
AA5 1 2 N LEU A 261 ? N LEU A 261 O MET A 315 ? O MET A 315 
AA5 2 3 N LYS A 316 ? N LYS A 316 O ARG A 324 ? O ARG A 324 
AA5 3 4 N LEU A 323 ? N LEU A 323 O ILE A 428 ? O ILE A 428 
AA5 4 5 N ILE A 431 ? N ILE A 431 O LYS A 510 ? O LYS A 510 
AA5 5 6 O HIS A 513 ? O HIS A 513 N TYR A 445 ? N TYR A 445 
AA6 1 2 O TYR A 369 ? O TYR A 369 N ALA A 361 ? N ALA A 361 
AA6 2 3 N GLU A 362 ? N GLU A 362 O THR A 384 ? O THR A 384 
AA6 3 4 N ILE A 383 ? N ILE A 383 O TRP A 391 ? O TRP A 391 
AA7 1 2 N SER A 462 ? N SER A 462 O MET A 476 ? O MET A 476 
AA8 1 2 N LYS A 551 ? N LYS A 551 O VAL A 558 ? O VAL A 558 
# 
_pdbx_entry_details.entry_id                   9EIZ 
_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 GLN A 110 ? ? 63.03   104.47  
2  1 ARG A 129 ? ? -132.94 -56.16  
3  1 LYS A 243 ? ? -97.58  -84.50  
4  1 PHE A 246 ? ? -90.12  -61.06  
5  1 PRO A 285 ? ? -59.48  176.66  
6  1 ASP A 311 ? ? -151.42 -36.91  
7  1 PHE A 333 ? ? -107.91 68.73   
8  1 ASN A 344 ? ? -156.16 70.52   
9  1 PRO A 418 ? ? -66.39  2.83    
10 1 ALA A 468 ? ? -115.93 -152.68 
11 1 LYS A 473 ? ? -104.30 72.56   
12 1 ASP A 478 ? ? -151.06 67.63   
13 1 PHE A 480 ? ? 56.46   16.51   
14 1 PHE A 530 ? ? 57.70   -122.91 
15 1 LEU A 569 ? ? -118.61 54.60   
16 1 ASN A 601 ? ? 59.82   -121.40 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 24.5883 -11.4120 -5.2990 0.3219 ? 0.0496  ? -0.0100 ? 0.2618 ? 0.0089  ? 0.2627 ? 2.0365 ? 1.4158  
? -0.6526 ? 4.6932 ? 0.4942 ? 2.0193 ? 0.0397  ? 0.1609  ? -0.1820 ? -0.1643 ? -0.1321 ? -0.1568 ? 0.1096  ? 0.1581  ? 0.0898 ? 
2 'X-RAY DIFFRACTION' ? refined 15.9638 -4.6750  11.2137 0.5999 ? -0.1002 ? 0.1106  ? 0.2741 ? -0.0458 ? 0.3764 ? 1.1015 ? -0.3857 
? -0.2279 ? 2.7359 ? 0.3476 ? 0.4882 ? -0.0180 ? -0.0141 ? -0.2315 ? 0.6484  ? -0.1219 ? 0.2404  ? 0.2070  ? -0.0417 ? 0.0682 ? 
3 'X-RAY DIFFRACTION' ? refined 18.9027 15.0264  17.9338 0.5529 ? -0.0328 ? 0.0275  ? 0.1861 ? 0.0250  ? 0.2800 ? 4.3098 ? 0.0323  
? -1.1316 ? 2.6159 ? 0.2544 ? 1.9018 ? -0.1431 ? -0.2068 ? -0.0353 ? 0.4188  ? -0.0036 ? -0.1000 ? -0.0615 ? 0.1029  ? 0.1050 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 10 through 215 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 216 through 412 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 413 through 622 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A PRO 2 ? A PRO 2 
# 
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  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GTP PG     P  N N 137 
GTP O1G    O  N N 138 
GTP O2G    O  N N 139 
GTP O3G    O  N N 140 
GTP O3B    O  N N 141 
GTP PB     P  N N 142 
GTP O1B    O  N N 143 
GTP O2B    O  N N 144 
GTP O3A    O  N N 145 
GTP PA     P  N N 146 
GTP O1A    O  N N 147 
GTP O2A    O  N N 148 
GTP "O5'"  O  N N 149 
GTP "C5'"  C  N N 150 
GTP "C4'"  C  N R 151 
GTP "O4'"  O  N N 152 
GTP "C3'"  C  N S 153 
GTP "O3'"  O  N N 154 
GTP "C2'"  C  N R 155 
GTP "O2'"  O  N N 156 
GTP "C1'"  C  N R 157 
GTP N9     N  Y N 158 
GTP C8     C  Y N 159 
GTP N7     N  Y N 160 
GTP C5     C  Y N 161 
GTP C6     C  N N 162 
GTP O6     O  N N 163 
GTP N1     N  N N 164 
GTP C2     C  N N 165 
GTP N2     N  N N 166 
GTP N3     N  N N 167 
GTP C4     C  Y N 168 
GTP HOG2   H  N N 169 
GTP HOG3   H  N N 170 
GTP HOB2   H  N N 171 
GTP HOA2   H  N N 172 
GTP "H5'"  H  N N 173 
GTP "H5''" H  N N 174 
GTP "H4'"  H  N N 175 
GTP "H3'"  H  N N 176 
GTP "HO3'" H  N N 177 
GTP "H2'"  H  N N 178 
GTP "HO2'" H  N N 179 
GTP "H1'"  H  N N 180 
GTP H8     H  N N 181 
GTP HN1    H  N N 182 
GTP HN21   H  N N 183 
GTP HN22   H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
MN  MN     MN N N 298 
OXL C1     C  N N 299 
OXL C2     C  N N 300 
OXL O1     O  N N 301 
OXL O2     O  N N 302 
OXL O3     O  N N 303 
OXL O4     O  N N 304 
PGE C1     C  N N 305 
PGE O1     O  N N 306 
PGE C2     C  N N 307 
PGE O2     O  N N 308 
PGE C3     C  N N 309 
PGE C4     C  N N 310 
PGE O4     O  N N 311 
PGE C6     C  N N 312 
PGE C5     C  N N 313 
PGE O3     O  N N 314 
PGE H1     H  N N 315 
PGE H12    H  N N 316 
PGE HO1    H  N N 317 
PGE H2     H  N N 318 
PGE H22    H  N N 319 
PGE H3     H  N N 320 
PGE H32    H  N N 321 
PGE H4     H  N N 322 
PGE H42    H  N N 323 
PGE HO4    H  N N 324 
PGE H6     H  N N 325 
PGE H62    H  N N 326 
PGE H5     H  N N 327 
PGE H52    H  N N 328 
PHE N      N  N N 329 
PHE CA     C  N S 330 
PHE C      C  N N 331 
PHE O      O  N N 332 
PHE CB     C  N N 333 
PHE CG     C  Y N 334 
PHE CD1    C  Y N 335 
PHE CD2    C  Y N 336 
PHE CE1    C  Y N 337 
PHE CE2    C  Y N 338 
PHE CZ     C  Y N 339 
PHE OXT    O  N N 340 
PHE H      H  N N 341 
PHE H2     H  N N 342 
PHE HA     H  N N 343 
PHE HB2    H  N N 344 
PHE HB3    H  N N 345 
PHE HD1    H  N N 346 
PHE HD2    H  N N 347 
PHE HE1    H  N N 348 
PHE HE2    H  N N 349 
PHE HZ     H  N N 350 
PHE HXT    H  N N 351 
PRO N      N  N N 352 
PRO CA     C  N S 353 
PRO C      C  N N 354 
PRO O      O  N N 355 
PRO CB     C  N N 356 
PRO CG     C  N N 357 
PRO CD     C  N N 358 
PRO OXT    O  N N 359 
PRO H      H  N N 360 
PRO HA     H  N N 361 
PRO HB2    H  N N 362 
PRO HB3    H  N N 363 
PRO HG2    H  N N 364 
PRO HG3    H  N N 365 
PRO HD2    H  N N 366 
PRO HD3    H  N N 367 
PRO HXT    H  N N 368 
SER N      N  N N 369 
SER CA     C  N S 370 
SER C      C  N N 371 
SER O      O  N N 372 
SER CB     C  N N 373 
SER OG     O  N N 374 
SER OXT    O  N N 375 
SER H      H  N N 376 
SER H2     H  N N 377 
SER HA     H  N N 378 
SER HB2    H  N N 379 
SER HB3    H  N N 380 
SER HG     H  N N 381 
SER HXT    H  N N 382 
THR N      N  N N 383 
THR CA     C  N S 384 
THR C      C  N N 385 
THR O      O  N N 386 
THR CB     C  N R 387 
THR OG1    O  N N 388 
THR CG2    C  N N 389 
THR OXT    O  N N 390 
THR H      H  N N 391 
THR H2     H  N N 392 
THR HA     H  N N 393 
THR HB     H  N N 394 
THR HG1    H  N N 395 
THR HG21   H  N N 396 
THR HG22   H  N N 397 
THR HG23   H  N N 398 
THR HXT    H  N N 399 
TRP N      N  N N 400 
TRP CA     C  N S 401 
TRP C      C  N N 402 
TRP O      O  N N 403 
TRP CB     C  N N 404 
TRP CG     C  Y N 405 
TRP CD1    C  Y N 406 
TRP CD2    C  Y N 407 
TRP NE1    N  Y N 408 
TRP CE2    C  Y N 409 
TRP CE3    C  Y N 410 
TRP CZ2    C  Y N 411 
TRP CZ3    C  Y N 412 
TRP CH2    C  Y N 413 
TRP OXT    O  N N 414 
TRP H      H  N N 415 
TRP H2     H  N N 416 
TRP HA     H  N N 417 
TRP HB2    H  N N 418 
TRP HB3    H  N N 419 
TRP HD1    H  N N 420 
TRP HE1    H  N N 421 
TRP HE3    H  N N 422 
TRP HZ2    H  N N 423 
TRP HZ3    H  N N 424 
TRP HH2    H  N N 425 
TRP HXT    H  N N 426 
TYR N      N  N N 427 
TYR CA     C  N S 428 
TYR C      C  N N 429 
TYR O      O  N N 430 
TYR CB     C  N N 431 
TYR CG     C  Y N 432 
TYR CD1    C  Y N 433 
TYR CD2    C  Y N 434 
TYR CE1    C  Y N 435 
TYR CE2    C  Y N 436 
TYR CZ     C  Y N 437 
TYR OH     O  N N 438 
TYR OXT    O  N N 439 
TYR H      H  N N 440 
TYR H2     H  N N 441 
TYR HA     H  N N 442 
TYR HB2    H  N N 443 
TYR HB3    H  N N 444 
TYR HD1    H  N N 445 
TYR HD2    H  N N 446 
TYR HE1    H  N N 447 
TYR HE2    H  N N 448 
TYR HH     H  N N 449 
TYR HXT    H  N N 450 
VAL N      N  N N 451 
VAL CA     C  N S 452 
VAL C      C  N N 453 
VAL O      O  N N 454 
VAL CB     C  N N 455 
VAL CG1    C  N N 456 
VAL CG2    C  N N 457 
VAL OXT    O  N N 458 
VAL H      H  N N 459 
VAL H2     H  N N 460 
VAL HA     H  N N 461 
VAL HB     H  N N 462 
VAL HG11   H  N N 463 
VAL HG12   H  N N 464 
VAL HG13   H  N N 465 
VAL HG21   H  N N 466 
VAL HG22   H  N N 467 
VAL HG23   H  N N 468 
VAL HXT    H  N N 469 
# 
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  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GTP PG    O1G    doub N N 129 
GTP PG    O2G    sing N N 130 
GTP PG    O3G    sing N N 131 
GTP PG    O3B    sing N N 132 
GTP O2G   HOG2   sing N N 133 
GTP O3G   HOG3   sing N N 134 
GTP O3B   PB     sing N N 135 
GTP PB    O1B    doub N N 136 
GTP PB    O2B    sing N N 137 
GTP PB    O3A    sing N N 138 
GTP O2B   HOB2   sing N N 139 
GTP O3A   PA     sing N N 140 
GTP PA    O1A    doub N N 141 
GTP PA    O2A    sing N N 142 
GTP PA    "O5'"  sing N N 143 
GTP O2A   HOA2   sing N N 144 
GTP "O5'" "C5'"  sing N N 145 
GTP "C5'" "C4'"  sing N N 146 
GTP "C5'" "H5'"  sing N N 147 
GTP "C5'" "H5''" sing N N 148 
GTP "C4'" "O4'"  sing N N 149 
GTP "C4'" "C3'"  sing N N 150 
GTP "C4'" "H4'"  sing N N 151 
GTP "O4'" "C1'"  sing N N 152 
GTP "C3'" "O3'"  sing N N 153 
GTP "C3'" "C2'"  sing N N 154 
GTP "C3'" "H3'"  sing N N 155 
GTP "O3'" "HO3'" sing N N 156 
GTP "C2'" "O2'"  sing N N 157 
GTP "C2'" "C1'"  sing N N 158 
GTP "C2'" "H2'"  sing N N 159 
GTP "O2'" "HO2'" sing N N 160 
GTP "C1'" N9     sing N N 161 
GTP "C1'" "H1'"  sing N N 162 
GTP N9    C8     sing Y N 163 
GTP N9    C4     sing Y N 164 
GTP C8    N7     doub Y N 165 
GTP C8    H8     sing N N 166 
GTP N7    C5     sing Y N 167 
GTP C5    C6     sing N N 168 
GTP C5    C4     doub Y N 169 
GTP C6    O6     doub N N 170 
GTP C6    N1     sing N N 171 
GTP N1    C2     sing N N 172 
GTP N1    HN1    sing N N 173 
GTP C2    N2     sing N N 174 
GTP C2    N3     doub N N 175 
GTP N2    HN21   sing N N 176 
GTP N2    HN22   sing N N 177 
GTP N3    C4     sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
OXL C1    C2     sing N N 287 
OXL C1    O1     doub N N 288 
OXL C1    O3     sing N N 289 
OXL C2    O2     doub N N 290 
OXL C2    O4     sing N N 291 
PGE C1    O1     sing N N 292 
PGE C1    C2     sing N N 293 
PGE C1    H1     sing N N 294 
PGE C1    H12    sing N N 295 
PGE O1    HO1    sing N N 296 
PGE C2    O2     sing N N 297 
PGE C2    H2     sing N N 298 
PGE C2    H22    sing N N 299 
PGE O2    C3     sing N N 300 
PGE C3    C4     sing N N 301 
PGE C3    H3     sing N N 302 
PGE C3    H32    sing N N 303 
PGE C4    O3     sing N N 304 
PGE C4    H4     sing N N 305 
PGE C4    H42    sing N N 306 
PGE O4    C6     sing N N 307 
PGE O4    HO4    sing N N 308 
PGE C6    C5     sing N N 309 
PGE C6    H6     sing N N 310 
PGE C6    H62    sing N N 311 
PGE C5    O3     sing N N 312 
PGE C5    H5     sing N N 313 
PGE C5    H52    sing N N 314 
PHE N     CA     sing N N 315 
PHE N     H      sing N N 316 
PHE N     H2     sing N N 317 
PHE CA    C      sing N N 318 
PHE CA    CB     sing N N 319 
PHE CA    HA     sing N N 320 
PHE C     O      doub N N 321 
PHE C     OXT    sing N N 322 
PHE CB    CG     sing N N 323 
PHE CB    HB2    sing N N 324 
PHE CB    HB3    sing N N 325 
PHE CG    CD1    doub Y N 326 
PHE CG    CD2    sing Y N 327 
PHE CD1   CE1    sing Y N 328 
PHE CD1   HD1    sing N N 329 
PHE CD2   CE2    doub Y N 330 
PHE CD2   HD2    sing N N 331 
PHE CE1   CZ     doub Y N 332 
PHE CE1   HE1    sing N N 333 
PHE CE2   CZ     sing Y N 334 
PHE CE2   HE2    sing N N 335 
PHE CZ    HZ     sing N N 336 
PHE OXT   HXT    sing N N 337 
PRO N     CA     sing N N 338 
PRO N     CD     sing N N 339 
PRO N     H      sing N N 340 
PRO CA    C      sing N N 341 
PRO CA    CB     sing N N 342 
PRO CA    HA     sing N N 343 
PRO C     O      doub N N 344 
PRO C     OXT    sing N N 345 
PRO CB    CG     sing N N 346 
PRO CB    HB2    sing N N 347 
PRO CB    HB3    sing N N 348 
PRO CG    CD     sing N N 349 
PRO CG    HG2    sing N N 350 
PRO CG    HG3    sing N N 351 
PRO CD    HD2    sing N N 352 
PRO CD    HD3    sing N N 353 
PRO OXT   HXT    sing N N 354 
SER N     CA     sing N N 355 
SER N     H      sing N N 356 
SER N     H2     sing N N 357 
SER CA    C      sing N N 358 
SER CA    CB     sing N N 359 
SER CA    HA     sing N N 360 
SER C     O      doub N N 361 
SER C     OXT    sing N N 362 
SER CB    OG     sing N N 363 
SER CB    HB2    sing N N 364 
SER CB    HB3    sing N N 365 
SER OG    HG     sing N N 366 
SER OXT   HXT    sing N N 367 
THR N     CA     sing N N 368 
THR N     H      sing N N 369 
THR N     H2     sing N N 370 
THR CA    C      sing N N 371 
THR CA    CB     sing N N 372 
THR CA    HA     sing N N 373 
THR C     O      doub N N 374 
THR C     OXT    sing N N 375 
THR CB    OG1    sing N N 376 
THR CB    CG2    sing N N 377 
THR CB    HB     sing N N 378 
THR OG1   HG1    sing N N 379 
THR CG2   HG21   sing N N 380 
THR CG2   HG22   sing N N 381 
THR CG2   HG23   sing N N 382 
THR OXT   HXT    sing N N 383 
TRP N     CA     sing N N 384 
TRP N     H      sing N N 385 
TRP N     H2     sing N N 386 
TRP CA    C      sing N N 387 
TRP CA    CB     sing N N 388 
TRP CA    HA     sing N N 389 
TRP C     O      doub N N 390 
TRP C     OXT    sing N N 391 
TRP CB    CG     sing N N 392 
TRP CB    HB2    sing N N 393 
TRP CB    HB3    sing N N 394 
TRP CG    CD1    doub Y N 395 
TRP CG    CD2    sing Y N 396 
TRP CD1   NE1    sing Y N 397 
TRP CD1   HD1    sing N N 398 
TRP CD2   CE2    doub Y N 399 
TRP CD2   CE3    sing Y N 400 
TRP NE1   CE2    sing Y N 401 
TRP NE1   HE1    sing N N 402 
TRP CE2   CZ2    sing Y N 403 
TRP CE3   CZ3    doub Y N 404 
TRP CE3   HE3    sing N N 405 
TRP CZ2   CH2    doub Y N 406 
TRP CZ2   HZ2    sing N N 407 
TRP CZ3   CH2    sing Y N 408 
TRP CZ3   HZ3    sing N N 409 
TRP CH2   HH2    sing N N 410 
TRP OXT   HXT    sing N N 411 
TYR N     CA     sing N N 412 
TYR N     H      sing N N 413 
TYR N     H2     sing N N 414 
TYR CA    C      sing N N 415 
TYR CA    CB     sing N N 416 
TYR CA    HA     sing N N 417 
TYR C     O      doub N N 418 
TYR C     OXT    sing N N 419 
TYR CB    CG     sing N N 420 
TYR CB    HB2    sing N N 421 
TYR CB    HB3    sing N N 422 
TYR CG    CD1    doub Y N 423 
TYR CG    CD2    sing Y N 424 
TYR CD1   CE1    sing Y N 425 
TYR CD1   HD1    sing N N 426 
TYR CD2   CE2    doub Y N 427 
TYR CD2   HD2    sing N N 428 
TYR CE1   CZ     doub Y N 429 
TYR CE1   HE1    sing N N 430 
TYR CE2   CZ     sing Y N 431 
TYR CE2   HE2    sing N N 432 
TYR CZ    OH     sing N N 433 
TYR OH    HH     sing N N 434 
TYR OXT   HXT    sing N N 435 
VAL N     CA     sing N N 436 
VAL N     H      sing N N 437 
VAL N     H2     sing N N 438 
VAL CA    C      sing N N 439 
VAL CA    CB     sing N N 440 
VAL CA    HA     sing N N 441 
VAL C     O      doub N N 442 
VAL C     OXT    sing N N 443 
VAL CB    CG1    sing N N 444 
VAL CB    CG2    sing N N 445 
VAL CB    HB     sing N N 446 
VAL CG1   HG11   sing N N 447 
VAL CG1   HG12   sing N N 448 
VAL CG1   HG13   sing N N 449 
VAL CG2   HG21   sing N N 450 
VAL CG2   HG22   sing N N 451 
VAL CG2   HG23   sing N N 452 
VAL OXT   HXT    sing N N 453 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' DBI-2210041     1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 5R01GM127528-02 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3DT2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EIZ 
_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]   0.022116 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008654 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008322 
_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]   0.017709 
_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  
MN 
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     . PRO A 1 3   ? 25.139 -15.768 -35.476 1.00 84.83  ? 3   PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? 25.459 -14.644 -34.588 1.00 86.01  ? 3   PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? 26.841 -14.771 -33.944 1.00 85.07  ? 3   PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? 27.430 -13.760 -33.558 1.00 86.03  ? 3   PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? 24.352 -14.706 -33.529 1.00 89.19  ? 3   PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? 23.870 -16.119 -33.560 1.00 88.80  ? 3   PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? 23.989 -16.549 -34.989 1.00 88.27  ? 3   PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? 27.344 -15.999 -33.825 1.00 81.38  ? 4   GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? 28.675 -16.247 -33.290 1.00 81.29  ? 4   GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? 29.365 -17.309 -34.136 1.00 80.30  ? 4   GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? 28.722 -18.062 -34.872 1.00 80.55  ? 4   GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? 28.635 -16.692 -31.819 1.00 87.72  ? 4   GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? 28.272 -15.596 -30.821 1.00 87.11  ? 4   GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? 26.775 -15.369 -30.708 1.00 92.46  ? 4   GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? 25.975 -16.219 -31.100 1.00 94.59  ? 4   GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? 26.389 -14.216 -30.168 1.00 88.65  ? 4   GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? 30.695 -17.360 -34.021 1.00 77.82  ? 5   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? 31.475 -18.333 -34.781 1.00 77.21  ? 5   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? 31.514 -19.692 -34.096 1.00 75.68  ? 5   LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? 31.644 -20.720 -34.771 1.00 73.16  ? 5   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? 32.898 -17.814 -34.997 1.00 71.35  ? 5   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? 33.020 -16.526 -35.809 1.00 65.76  ? 5   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? 34.475 -16.115 -35.948 1.00 57.30  ? 5   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? 32.375 -16.698 -37.174 1.00 62.77  ? 5   LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? 31.412 -19.716 -32.766 1.00 80.33  ? 6   HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? 31.353 -20.954 -32.005 1.00 82.38  ? 6   HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? 30.176 -20.990 -31.038 1.00 85.36  ? 6   HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? 30.015 -21.985 -30.323 1.00 88.06  ? 6   HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? 32.663 -21.169 -31.226 1.00 77.24  ? 6   HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? 33.899 -21.021 -32.063 1.00 78.71  ? 6   HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? 34.551 -22.097 -32.627 1.00 76.81  ? 6   HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? 34.603 -19.923 -32.428 1.00 76.52  ? 6   HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? 35.601 -21.669 -33.305 1.00 70.48  ? 6   HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? 35.656 -20.353 -33.200 1.00 72.53  ? 6   HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? 29.349 -19.940 -31.006 1.00 91.78  ? 7   ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? 28.262 -19.791 -30.034 1.00 92.07  ? 7   ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? 28.755 -19.948 -28.599 1.00 91.01  ? 7   ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? 28.050 -20.491 -27.745 1.00 97.74  ? 7   ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? 27.115 -20.768 -30.312 1.00 95.32  ? 7   ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? 26.221 -20.314 -31.454 1.00 99.04  ? 7   ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? 25.932 -19.125 -31.601 1.00 94.57  ? 7   ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? 25.781 -21.265 -32.272 1.00 103.36 ? 7   ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? 29.970 -19.472 -28.316 1.00 89.73  ? 8   GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? 30.485 -19.547 -26.960 1.00 91.06  ? 8   GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? 29.824 -18.579 -26.002 1.00 91.25  ? 8   GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? 29.957 -18.741 -24.785 1.00 87.52  ? 8   GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? 29.120 -17.577 -26.524 1.00 92.50  ? 9   LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? 28.396 -16.612 -25.709 1.00 87.38  ? 9   LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? 26.940 -17.006 -25.493 1.00 83.65  ? 9   LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? 26.149 -16.181 -25.024 1.00 84.35  ? 9   LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? 28.466 -15.222 -26.349 1.00 87.15  ? 9   LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? 29.826 -14.754 -26.871 1.00 89.08  ? 9   LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? 29.735 -13.312 -27.338 1.00 84.74  ? 9   LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? 30.912 -14.913 -25.816 1.00 83.83  ? 9   LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? 26.572 -18.239 -25.825 1.00 86.61  ? 10  ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? 25.198 -18.722 -25.717 1.00 84.51  ? 10  ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? 25.141 -19.702 -24.546 1.00 79.73  ? 10  ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? 25.408 -20.896 -24.700 1.00 79.54  ? 10  ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? 24.748 -19.367 -27.031 1.00 84.81  ? 10  ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? 23.253 -19.622 -27.078 1.00 81.74  ? 10  ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? 22.715 -20.206 -26.118 1.00 79.57  ? 10  ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? 22.613 -19.235 -28.078 1.00 87.31  ? 10  ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? 24.787 -19.184 -23.370 1.00 67.38  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 24.694 -19.975 -22.151 1.00 62.66  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 23.319 -20.607 -21.958 1.00 58.57  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 22.986 -21.009 -20.838 1.00 57.19  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 25.047 -19.113 -20.935 1.00 62.43  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 26.521 -19.070 -20.622 1.00 65.81  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 27.385 -18.293 -21.380 1.00 63.45  ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 27.038 -19.797 -19.559 1.00 61.62  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 28.741 -18.252 -21.090 1.00 58.04  ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 28.391 -19.759 -19.263 1.00 57.70  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 29.244 -18.987 -20.030 1.00 54.93  ? 11  PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? 22.520 -20.711 -23.025 1.00 58.53  ? 12  SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? 21.172 -21.260 -22.896 1.00 58.48  ? 12  SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? 21.191 -22.713 -22.436 1.00 61.63  ? 12  SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? 20.274 -23.151 -21.733 1.00 56.94  ? 12  SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? 20.425 -21.142 -24.225 1.00 61.37  ? 12  SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? 20.416 -19.805 -24.692 1.00 67.86  ? 12  SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? 22.220 -23.473 -22.822 1.00 60.51  ? 13  ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? 22.318 -24.879 -22.450 1.00 53.82  ? 13  ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? 22.561 -25.086 -20.961 1.00 54.96  ? 13  ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? 22.368 -26.204 -20.472 1.00 54.21  ? 13  ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? 23.430 -25.556 -23.251 1.00 52.89  ? 13  ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? 22.973 -24.050 -20.233 1.00 51.32  ? 14  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? 23.246 -24.158 -18.807 1.00 54.09  ? 14  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? 22.139 -23.566 -17.941 1.00 50.65  ? 14  LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? 22.350 -23.359 -16.741 1.00 47.07  ? 14  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? 24.583 -23.492 -18.476 1.00 54.20  ? 14  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? 25.800 -24.304 -18.896 1.00 57.11  ? 14  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? 27.099 -23.606 -18.513 1.00 58.01  ? 14  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? 28.290 -24.545 -18.651 1.00 66.39  ? 14  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? 28.395 -25.128 -20.021 1.00 69.13  ? 14  LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? 20.968 -23.298 -18.511 1.00 52.38  ? 15  VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? 19.855 -22.713 -17.769 1.00 50.25  ? 15  VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? 18.985 -23.840 -17.225 1.00 50.01  ? 15  VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? 18.364 -24.585 -17.993 1.00 49.37  ? 15  VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? 19.036 -21.761 -18.652 1.00 45.34  ? 15  VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? 17.834 -21.233 -17.886 1.00 44.64  ? 15  VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? 19.906 -20.615 -19.146 1.00 43.49  ? 15  VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? 18.931 -23.962 -15.896 1.00 41.82  ? 16  ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? 18.136 -25.009 -15.260 1.00 48.11  ? 16  ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? 16.740 -24.541 -14.872 1.00 47.54  ? 16  ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? 15.895 -25.382 -14.523 1.00 47.51  ? 16  ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? 18.859 -25.590 -14.026 1.00 47.00  ? 16  ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? 19.169 -24.497 -13.010 1.00 48.11  ? 16  ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? 20.138 -26.301 -14.447 1.00 47.97  ? 16  ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? 19.891 -25.000 -11.783 1.00 49.36  ? 16  ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? 16.468 -23.238 -14.922 1.00 45.28  ? 17  GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? 15.121 -22.723 -14.702 1.00 46.93  ? 17  GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? 15.002 -21.365 -15.374 1.00 46.32  ? 17  GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? 15.832 -20.482 -15.139 1.00 46.52  ? 17  GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? 14.788 -22.601 -13.210 1.00 47.00  ? 17  GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? 13.409 -21.997 -12.959 1.00 45.59  ? 17  GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? 13.060 -21.894 -11.486 1.00 49.74  ? 17  GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? 13.208 -22.854 -10.730 1.00 54.44  ? 17  GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? 12.595 -20.721 -11.070 1.00 44.09  ? 17  GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? 13.975 -21.204 -16.197 1.00 44.06  ? 18  GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? 13.755 -19.969 -16.915 1.00 46.12  ? 18  GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? 14.212 -20.046 -18.358 1.00 50.63  ? 18  GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? 14.447 -21.118 -18.919 1.00 57.19  ? 18  GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? 14.339 -18.869 -18.965 1.00 51.62  ? 19  SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? 14.755 -18.764 -20.357 1.00 54.91  ? 19  SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? 15.436 -17.424 -20.579 1.00 58.12  ? 19  SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? 14.899 -16.382 -20.191 1.00 61.91  ? 19  SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? 13.561 -18.907 -21.304 1.00 54.77  ? 19  SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? 13.936 -18.607 -22.638 1.00 63.90  ? 19  SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? 16.616 -17.458 -21.202 1.00 58.58  ? 20  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? 17.270 -16.218 -21.601 1.00 60.94  ? 20  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? 16.461 -15.485 -22.662 1.00 65.65  ? 20  LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? 16.550 -14.256 -22.770 1.00 64.90  ? 20  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? 18.683 -16.505 -22.109 1.00 57.74  ? 20  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? 19.659 -17.163 -21.131 1.00 57.61  ? 20  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? 20.965 -17.527 -21.831 1.00 56.58  ? 20  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? 19.925 -16.260 -19.939 1.00 48.95  ? 20  LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? 15.662 -16.218 -23.445 1.00 64.89  ? 21  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? 14.815 -15.598 -24.457 1.00 72.58  ? 21  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? 13.659 -14.817 -23.849 1.00 77.22  ? 21  ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? 13.053 -13.993 -24.542 1.00 84.04  ? 21  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? 14.267 -16.660 -25.411 1.00 77.31  ? 21  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? 15.357 -17.358 -26.197 1.00 77.78  ? 21  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? 16.545 -17.043 -25.977 1.00 71.86  ? 21  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? 15.024 -18.223 -27.036 1.00 77.42  ? 21  ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? 13.334 -15.062 -22.582 1.00 70.83  ? 22  SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? 12.262 -14.352 -21.899 1.00 68.52  ? 22  SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? 12.755 -13.128 -21.141 1.00 67.60  ? 22  SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? 11.936 -12.397 -20.575 1.00 70.49  ? 22  SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? 11.536 -15.296 -20.937 1.00 65.55  ? 22  SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? 10.910 -16.353 -21.644 1.00 71.64  ? 22  SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? 14.054 -12.890 -21.119 1.00 64.35  ? 23  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? 14.606 -11.739 -20.426 1.00 61.15  ? 23  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? 14.582 -10.505 -21.322 1.00 65.91  ? 23  LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? 14.638 -10.620 -22.551 1.00 68.50  ? 23  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? 16.042 -12.017 -19.993 1.00 58.64  ? 23  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? 16.265 -13.139 -18.982 1.00 59.28  ? 23  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? 17.746 -13.267 -18.668 1.00 57.26  ? 23  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? 15.464 -12.884 -17.715 1.00 55.75  ? 23  LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? 14.489 -9.315  -20.729 1.00 63.32  ? 24  PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? 14.685 -8.090  -21.510 1.00 60.73  ? 24  PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? 16.090 -8.035  -22.090 1.00 61.45  ? 24  PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? 17.006 -8.732  -21.643 1.00 57.01  ? 24  PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? 14.460 -6.971  -20.486 1.00 62.51  ? 24  PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? 13.623 -7.598  -19.421 1.00 63.91  ? 24  PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? 14.060 -9.031  -19.350 1.00 61.24  ? 24  PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? 16.248 -7.182  -23.105 1.00 60.84  ? 25  GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? 17.511 -7.097  -23.832 1.00 59.97  ? 25  GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? 18.678 -6.821  -22.890 1.00 56.68  ? 25  GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? 19.638 -7.595  -22.826 1.00 56.57  ? 25  GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? 17.420 -6.014  -24.908 1.00 67.69  ? 25  GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? 18.667 -5.893  -25.770 1.00 74.92  ? 25  GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? 18.624 -4.693  -26.699 1.00 81.04  ? 25  GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? 17.868 -3.746  -26.475 1.00 82.24  ? 25  GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? 19.437 -4.728  -27.750 1.00 79.40  ? 25  GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? 18.610 -5.717  -22.142 1.00 56.76  ? 26  GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? 19.714 -5.363  -21.259 1.00 54.81  ? 26  GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? 19.842 -6.315  -20.077 1.00 53.84  ? 26  GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? 20.908 -6.372  -19.456 1.00 52.97  ? 26  GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? 19.554 -3.925  -20.761 1.00 56.36  ? 26  GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? 19.508 -2.888  -21.878 1.00 61.81  ? 26  GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? 20.762 -2.890  -22.739 1.00 60.22  ? 26  GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? 21.870 -3.077  -22.191 1.00 54.74  ? 26  GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? 20.637 -2.709  -23.969 1.00 71.08  ? 26  GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? 18.789 -7.065  -19.752 1.00 54.35  ? 27  VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? 18.906 -8.065  -18.697 1.00 55.28  ? 27  VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? 19.654 -9.292  -19.205 1.00 51.34  ? 27  VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? 20.519 -9.835  -18.509 1.00 47.08  ? 27  VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? 17.514 -8.428  -18.146 1.00 56.01  ? 27  VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? 17.626 -9.487  -17.059 1.00 49.49  ? 27  VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? 16.825 -7.184  -17.604 1.00 54.37  ? 27  VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? 19.352 -9.738  -20.426 1.00 51.80  ? 28  ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? 20.067 -10.883 -20.982 1.00 54.87  ? 28  ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? 21.548 -10.576 -21.167 1.00 48.56  ? 28  ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? 22.403 -11.417 -20.866 1.00 50.94  ? 28  ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? 19.446 -11.309 -22.310 1.00 50.10  ? 28  ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? 19.995 -12.626 -22.818 1.00 55.81  ? 28  ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? 19.757 -12.796 -24.305 1.00 65.53  ? 28  ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? 20.383 -14.010 -24.817 1.00 61.32  ? 28  ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? 19.717 -15.086 -25.211 1.00 63.20  ? 28  ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? 18.395 -15.129 -25.183 1.00 67.15  ? 28  ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? 20.394 -16.142 -25.652 1.00 64.96  ? 28  ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? 21.873 -9.380  -21.665 1.00 48.89  ? 29  LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? 23.275 -9.003  -21.815 1.00 51.21  ? 29  LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? 23.985 -8.986  -20.469 1.00 44.10  ? 29  LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? 25.153 -9.380  -20.369 1.00 42.00  ? 29  LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? 23.388 -7.636  -22.492 1.00 50.93  ? 29  LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? 23.033 -7.625  -23.971 1.00 54.09  ? 29  LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? 23.087 -6.209  -24.528 1.00 58.74  ? 29  LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? 22.872 -6.184  -26.035 1.00 72.08  ? 29  LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? 24.003 -6.815  -26.782 1.00 72.87  ? 29  LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? 23.293 -8.536  -19.420 1.00 46.37  ? 30  PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? 23.902 -8.479  -18.095 1.00 43.69  ? 30  PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? 24.178 -9.875  -17.549 1.00 41.10  ? 30  PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? 25.229 -10.112 -16.944 1.00 40.96  ? 30  PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? 23.001 -7.687  -17.147 1.00 43.27  ? 30  PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? 23.523 -7.594  -15.745 1.00 37.57  ? 30  PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? 24.759 -7.027  -15.488 1.00 41.80  ? 30  PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? 22.770 -8.059  -14.680 1.00 40.40  ? 30  PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? 25.241 -6.941  -14.199 1.00 38.60  ? 30  PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? 23.242 -7.969  -13.385 1.00 39.62  ? 30  PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? 24.479 -7.411  -13.145 1.00 40.18  ? 30  PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? 23.253 -10.815 -17.764 1.00 44.61  ? 31  VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? 23.444 -12.178 -17.269 1.00 45.06  ? 31  VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? 24.517 -12.897 -18.078 1.00 42.60  ? 31  VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? 25.473 -13.447 -17.520 1.00 38.15  ? 31  VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? 22.115 -12.954 -17.294 1.00 46.03  ? 31  VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? 22.336 -14.390 -16.843 1.00 43.56  ? 31  VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? 21.076 -12.268 -16.419 1.00 44.15  ? 31  VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? 24.374 -12.902 -19.407 1.00 46.49  ? 32  GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? 25.312 -13.636 -20.254 1.00 47.88  ? 32  GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? 26.722 -13.070 -20.154 1.00 44.77  ? 32  GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? 27.703 -13.822 -20.202 1.00 44.42  ? 32  GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? 24.838 -13.622 -21.708 1.00 44.43  ? 32  GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? 23.748 -14.632 -22.023 1.00 57.50  ? 32  GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? 23.476 -14.749 -23.512 1.00 60.83  ? 32  GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? 23.839 -13.815 -24.259 1.00 61.09  ? 32  GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? 22.902 -15.775 -23.936 1.00 61.33  ? 32  GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? 26.846 -11.748 -20.021 1.00 45.33  ? 33  GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? 28.167 -11.146 -19.936 1.00 43.50  ? 33  GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? 28.937 -11.609 -18.715 1.00 44.66  ? 33  GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? 30.093 -12.028 -18.813 1.00 43.78  ? 33  GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? 28.298 -11.551 -17.545 1.00 42.39  ? 34  ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? 28.960 -11.976 -16.319 1.00 42.99  ? 34  ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? 29.039 -13.490 -16.202 1.00 41.43  ? 34  ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? 29.941 -14.004 -15.533 1.00 44.44  ? 34  ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? 28.245 -11.387 -15.109 1.00 40.40  ? 34  ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? 28.442 -9.904  -15.002 1.00 41.17  ? 34  ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? 29.481 -9.440  -14.534 1.00 45.23  ? 34  ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? 27.452 -9.142  -15.446 1.00 43.25  ? 34  ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? 28.113 -14.216 -16.834 1.00 44.24  ? 35  ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? 28.261 -15.664 -16.922 1.00 49.79  ? 35  ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? 29.535 -16.028 -17.668 1.00 49.95  ? 35  ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? 30.259 -16.946 -17.266 1.00 51.04  ? 35  ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? 27.040 -16.285 -17.602 1.00 44.75  ? 35  ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? 29.835 -15.302 -18.748 1.00 49.13  ? 36  GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? 31.072 -15.529 -19.489 1.00 49.20  ? 36  GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? 32.296 -15.204 -18.644 1.00 46.97  ? 36  GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? 33.342 -15.845 -18.792 1.00 49.89  ? 36  GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? 31.066 -14.691 -20.768 1.00 53.71  ? 36  GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? 32.303 -14.841 -21.637 1.00 69.20  ? 36  GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? 32.307 -13.870 -22.804 1.00 78.32  ? 36  GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? 31.411 -13.033 -22.931 1.00 80.44  ? 36  GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? 33.317 -13.976 -23.663 1.00 74.18  ? 36  GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? 32.183 -14.225 -17.748 1.00 46.95  ? 37  LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? 33.310 -13.829 -16.911 1.00 50.17  ? 37  LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? 33.457 -14.734 -15.691 1.00 51.27  ? 37  LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? 34.569 -15.157 -15.354 1.00 49.40  ? 37  LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? 33.143 -12.372 -16.474 1.00 51.82  ? 37  LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? 34.072 -11.876 -15.365 1.00 49.24  ? 37  LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? 35.505 -11.787 -15.862 1.00 50.37  ? 37  LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? 33.593 -10.536 -14.838 1.00 50.84  ? 37  LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? 32.346 -15.035 -15.014 1.00 47.87  ? 38  CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? 32.403 -15.805 -13.777 1.00 50.89  ? 38  CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? 32.414 -17.310 -14.014 1.00 50.87  ? 38  CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? 32.836 -18.058 -13.124 1.00 53.75  ? 38  CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? 31.223 -15.431 -12.877 1.00 45.73  ? 38  CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? 31.123 -13.671 -12.475 1.00 47.17  ? 38  CYS A SG    1 
ATOM   277  N  N     A GLN A 1 39  ? 31.963 -17.764 -15.185 0.50 50.00  ? 39  GLN A N     1 
ATOM   278  N  N     B GLN A 1 39  ? 31.958 -17.763 -15.183 0.50 50.80  ? 39  GLN A N     1 
ATOM   279  C  CA    A GLN A 1 39  ? 31.924 -19.174 -15.561 0.50 54.09  ? 39  GLN A CA    1 
ATOM   280  C  CA    B GLN A 1 39  ? 31.916 -19.169 -15.571 0.50 55.51  ? 39  GLN A CA    1 
ATOM   281  C  C     A GLN A 1 39  ? 31.151 -20.011 -14.545 0.50 53.70  ? 39  GLN A C     1 
ATOM   282  C  C     B GLN A 1 39  ? 31.150 -20.013 -14.556 0.50 55.32  ? 39  GLN A C     1 
ATOM   283  O  O     A GLN A 1 39  ? 31.750 -20.835 -13.841 0.50 57.17  ? 39  GLN A O     1 
ATOM   284  O  O     B GLN A 1 39  ? 31.752 -20.842 -13.862 0.50 54.69  ? 39  GLN A O     1 
ATOM   285  C  CB    A GLN A 1 39  ? 33.345 -19.723 -15.722 0.50 53.15  ? 39  GLN A CB    1 
ATOM   286  C  CB    B GLN A 1 39  ? 33.335 -19.716 -15.748 0.50 53.07  ? 39  GLN A CB    1 
ATOM   287  C  CG    A GLN A 1 39  ? 34.097 -19.163 -16.920 0.50 54.50  ? 39  GLN A CG    1 
ATOM   288  C  CG    B GLN A 1 39  ? 34.209 -18.891 -16.683 0.50 54.58  ? 39  GLN A CG    1 
ATOM   289  C  CD    A GLN A 1 39  ? 33.547 -19.666 -18.240 0.50 51.74  ? 39  GLN A CD    1 
ATOM   290  C  CD    B GLN A 1 39  ? 35.602 -19.468 -16.839 0.50 50.09  ? 39  GLN A CD    1 
ATOM   291  O  OE1   A GLN A 1 39  ? 32.846 -18.946 -18.951 0.50 51.08  ? 39  GLN A OE1   1 
ATOM   292  O  OE1   B GLN A 1 39  ? 35.765 -20.647 -17.148 0.50 53.48  ? 39  GLN A OE1   1 
ATOM   293  N  NE2   A GLN A 1 39  ? 33.866 -20.909 -18.576 0.50 52.63  ? 39  GLN A NE2   1 
ATOM   294  N  NE2   B GLN A 1 39  ? 36.614 -18.639 -16.618 0.50 47.70  ? 39  GLN A NE2   1 
ATOM   295  N  N     . PRO A 1 40  ? 29.836 -19.838 -14.434 1.00 54.65  ? 40  PRO A N     1 
ATOM   296  C  CA    . PRO A 1 40  ? 29.046 -20.723 -13.577 1.00 54.06  ? 40  PRO A CA    1 
ATOM   297  C  C     . PRO A 1 40  ? 28.649 -21.988 -14.320 1.00 54.05  ? 40  PRO A C     1 
ATOM   298  O  O     . PRO A 1 40  ? 28.477 -22.001 -15.540 1.00 51.19  ? 40  PRO A O     1 
ATOM   299  C  CB    . PRO A 1 40  ? 27.814 -19.870 -13.249 1.00 48.24  ? 40  PRO A CB    1 
ATOM   300  C  CG    . PRO A 1 40  ? 27.615 -19.072 -14.495 1.00 47.99  ? 40  PRO A CG    1 
ATOM   301  C  CD    . PRO A 1 40  ? 28.998 -18.784 -15.038 1.00 48.25  ? 40  PRO A CD    1 
ATOM   302  N  N     . GLU A 1 41  ? 28.509 -23.073 -13.557 1.00 51.42  ? 41  GLU A N     1 
ATOM   303  C  CA    . GLU A 1 41  ? 28.095 -24.332 -14.166 1.00 51.44  ? 41  GLU A CA    1 
ATOM   304  C  C     . GLU A 1 41  ? 26.623 -24.308 -14.551 1.00 50.72  ? 41  GLU A C     1 
ATOM   305  O  O     . GLU A 1 41  ? 26.232 -24.934 -15.542 1.00 51.39  ? 41  GLU A O     1 
ATOM   306  C  CB    . GLU A 1 41  ? 28.375 -25.498 -13.219 1.00 53.44  ? 41  GLU A CB    1 
ATOM   307  C  CG    . GLU A 1 41  ? 28.305 -26.862 -13.890 1.00 60.84  ? 41  GLU A CG    1 
ATOM   308  C  CD    . GLU A 1 41  ? 28.401 -28.001 -12.896 1.00 69.92  ? 41  GLU A CD    1 
ATOM   309  O  OE1   . GLU A 1 41  ? 28.267 -27.738 -11.681 1.00 70.22  ? 41  GLU A OE1   1 
ATOM   310  O  OE2   . GLU A 1 41  ? 28.609 -29.157 -13.328 1.00 77.45  ? 41  GLU A OE2   1 
ATOM   311  N  N     . TYR A 1 42  ? 25.796 -23.595 -13.790 1.00 50.37  ? 42  TYR A N     1 
ATOM   312  C  CA    . TYR A 1 42  ? 24.372 -23.496 -14.067 1.00 48.49  ? 42  TYR A CA    1 
ATOM   313  C  C     . TYR A 1 42  ? 23.925 -22.054 -13.881 1.00 46.57  ? 42  TYR A C     1 
ATOM   314  O  O     . TYR A 1 42  ? 24.541 -21.278 -13.147 1.00 45.29  ? 42  TYR A O     1 
ATOM   315  C  CB    . TYR A 1 42  ? 23.542 -24.417 -13.158 1.00 47.21  ? 42  TYR A CB    1 
ATOM   316  C  CG    . TYR A 1 42  ? 23.988 -25.858 -13.170 1.00 51.74  ? 42  TYR A CG    1 
ATOM   317  C  CD1   . TYR A 1 42  ? 23.758 -26.666 -14.276 1.00 55.03  ? 42  TYR A CD1   1 
ATOM   318  C  CD2   . TYR A 1 42  ? 24.636 -26.414 -12.076 1.00 51.82  ? 42  TYR A CD2   1 
ATOM   319  C  CE1   . TYR A 1 42  ? 24.163 -27.983 -14.294 1.00 58.21  ? 42  TYR A CE1   1 
ATOM   320  C  CE2   . TYR A 1 42  ? 25.044 -27.733 -12.084 1.00 57.49  ? 42  TYR A CE2   1 
ATOM   321  C  CZ    . TYR A 1 42  ? 24.803 -28.513 -13.192 1.00 56.65  ? 42  TYR A CZ    1 
ATOM   322  O  OH    . TYR A 1 42  ? 25.208 -29.828 -13.206 1.00 67.35  ? 42  TYR A OH    1 
ATOM   323  N  N     . ILE A 1 43  ? 22.839 -21.704 -14.562 1.00 45.71  ? 43  ILE A N     1 
ATOM   324  C  CA    . ILE A 1 43  ? 22.213 -20.396 -14.434 1.00 46.68  ? 43  ILE A CA    1 
ATOM   325  C  C     . ILE A 1 43  ? 20.756 -20.620 -14.062 1.00 45.59  ? 43  ILE A C     1 
ATOM   326  O  O     . ILE A 1 43  ? 20.029 -21.331 -14.770 1.00 41.60  ? 43  ILE A O     1 
ATOM   327  C  CB    . ILE A 1 43  ? 22.335 -19.566 -15.721 1.00 41.22  ? 43  ILE A CB    1 
ATOM   328  C  CG1   . ILE A 1 43  ? 23.807 -19.399 -16.102 1.00 43.94  ? 43  ILE A CG1   1 
ATOM   329  C  CG2   . ILE A 1 43  ? 21.678 -18.210 -15.532 1.00 34.53  ? 43  ILE A CG2   1 
ATOM   330  C  CD1   . ILE A 1 43  ? 24.026 -18.593 -17.362 1.00 43.84  ? 43  ILE A CD1   1 
ATOM   331  N  N     . HIS A 1 44  ? 20.333 -20.014 -12.956 1.00 38.38  ? 44  HIS A N     1 
ATOM   332  C  CA    . HIS A 1 44  ? 18.998 -20.204 -12.400 1.00 39.98  ? 44  HIS A CA    1 
ATOM   333  C  C     . HIS A 1 44  ? 18.297 -18.853 -12.366 1.00 39.43  ? 44  HIS A C     1 
ATOM   334  O  O     . HIS A 1 44  ? 18.661 -17.983 -11.569 1.00 39.62  ? 44  HIS A O     1 
ATOM   335  C  CB    . HIS A 1 44  ? 19.083 -20.818 -11.003 1.00 34.07  ? 44  HIS A CB    1 
ATOM   336  C  CG    . HIS A 1 44  ? 17.756 -21.001 -10.337 1.00 43.39  ? 44  HIS A CG    1 
ATOM   337  N  ND1   . HIS A 1 44  ? 17.098 -22.211 -10.308 1.00 46.55  ? 44  HIS A ND1   1 
ATOM   338  C  CD2   . HIS A 1 44  ? 16.965 -20.127 -9.669  1.00 44.44  ? 44  HIS A CD2   1 
ATOM   339  C  CE1   . HIS A 1 44  ? 15.958 -22.076 -9.654  1.00 37.73  ? 44  HIS A CE1   1 
ATOM   340  N  NE2   . HIS A 1 44  ? 15.852 -20.821 -9.259  1.00 43.63  ? 44  HIS A NE2   1 
ATOM   341  N  N     . ILE A 1 45  ? 17.296 -18.679 -13.223 1.00 37.34  ? 45  ILE A N     1 
ATOM   342  C  CA    . ILE A 1 45  ? 16.510 -17.450 -13.262 1.00 41.10  ? 45  ILE A CA    1 
ATOM   343  C  C     . ILE A 1 45  ? 15.361 -17.602 -12.272 1.00 42.67  ? 45  ILE A C     1 
ATOM   344  O  O     . ILE A 1 45  ? 14.454 -18.412 -12.482 1.00 42.81  ? 45  ILE A O     1 
ATOM   345  C  CB    . ILE A 1 45  ? 15.986 -17.153 -14.671 1.00 38.86  ? 45  ILE A CB    1 
ATOM   346  C  CG1   . ILE A 1 45  ? 17.125 -17.180 -15.689 1.00 39.69  ? 45  ILE A CG1   1 
ATOM   347  C  CG2   . ILE A 1 45  ? 15.280 -15.802 -14.692 1.00 38.89  ? 45  ILE A CG2   1 
ATOM   348  C  CD1   . ILE A 1 45  ? 16.658 -16.992 -17.118 1.00 45.39  ? 45  ILE A CD1   1 
ATOM   349  N  N     . CYS A 1 46  ? 15.391 -16.812 -11.202 1.00 39.94  ? 46  CYS A N     1 
ATOM   350  C  CA    . CYS A 1 46  ? 14.414 -16.968 -10.133 1.00 38.04  ? 46  CYS A CA    1 
ATOM   351  C  C     . CYS A 1 46  ? 13.035 -16.492 -10.570 1.00 39.17  ? 46  CYS A C     1 
ATOM   352  O  O     . CYS A 1 46  ? 12.898 -15.511 -11.308 1.00 43.23  ? 46  CYS A O     1 
ATOM   353  C  CB    . CYS A 1 46  ? 14.861 -16.203 -8.891  1.00 35.30  ? 46  CYS A CB    1 
ATOM   354  S  SG    . CYS A 1 46  ? 16.447 -16.750 -8.236  1.00 40.11  ? 46  CYS A SG    1 
ATOM   355  N  N     . ASP A 1 47  ? 12.005 -17.202 -10.111 1.00 40.89  ? 47  ASP A N     1 
ATOM   356  C  CA    . ASP A 1 47  ? 10.625 -16.806 -10.348 1.00 45.31  ? 47  ASP A CA    1 
ATOM   357  C  C     . ASP A 1 47  ? 9.896  -16.376 -9.082  1.00 40.10  ? 47  ASP A C     1 
ATOM   358  O  O     . ASP A 1 47  ? 8.741  -15.944 -9.173  1.00 41.69  ? 47  ASP A O     1 
ATOM   359  C  CB    . ASP A 1 47  ? 9.845  -17.947 -11.023 1.00 40.92  ? 47  ASP A CB    1 
ATOM   360  C  CG    . ASP A 1 47  ? 9.697  -19.174 -10.135 1.00 43.64  ? 47  ASP A CG    1 
ATOM   361  O  OD1   . ASP A 1 47  ? 10.292 -19.217 -9.039  1.00 45.45  ? 47  ASP A OD1   1 
ATOM   362  O  OD2   . ASP A 1 47  ? 8.979  -20.106 -10.544 1.00 49.16  ? 47  ASP A OD2   1 
ATOM   363  N  N     . GLY A 1 48  ? 10.530 -16.486 -7.915  1.00 41.79  ? 48  GLY A N     1 
ATOM   364  C  CA    . GLY A 1 48  ? 9.927  -16.060 -6.668  1.00 45.28  ? 48  GLY A CA    1 
ATOM   365  C  C     . GLY A 1 48  ? 8.848  -16.965 -6.115  1.00 45.96  ? 48  GLY A C     1 
ATOM   366  O  O     . GLY A 1 48  ? 8.271  -16.636 -5.071  1.00 42.29  ? 48  GLY A O     1 
ATOM   367  N  N     . SER A 1 49  ? 8.554  -18.088 -6.767  1.00 44.86  ? 49  SER A N     1 
ATOM   368  C  CA    . SER A 1 49  ? 7.486  -18.968 -6.314  1.00 47.81  ? 49  SER A CA    1 
ATOM   369  C  C     . SER A 1 49  ? 7.854  -19.642 -4.995  1.00 49.93  ? 49  SER A C     1 
ATOM   370  O  O     . SER A 1 49  ? 9.024  -19.737 -4.613  1.00 47.53  ? 49  SER A O     1 
ATOM   371  C  CB    . SER A 1 49  ? 7.186  -20.035 -7.365  1.00 46.05  ? 49  SER A CB    1 
ATOM   372  O  OG    . SER A 1 49  ? 8.287  -20.914 -7.502  1.00 46.08  ? 49  SER A OG    1 
ATOM   373  N  N     . GLU A 1 50  ? 6.825  -20.117 -4.290  1.00 49.02  ? 50  GLU A N     1 
ATOM   374  C  CA    . GLU A 1 50  ? 7.060  -20.863 -3.060  1.00 54.41  ? 50  GLU A CA    1 
ATOM   375  C  C     . GLU A 1 50  ? 7.630  -22.248 -3.335  1.00 54.45  ? 50  GLU A C     1 
ATOM   376  O  O     . GLU A 1 50  ? 8.322  -22.802 -2.473  1.00 50.22  ? 50  GLU A O     1 
ATOM   377  C  CB    . GLU A 1 50  ? 5.769  -20.963 -2.244  1.00 57.01  ? 50  GLU A CB    1 
ATOM   378  C  CG    . GLU A 1 50  ? 5.392  -19.656 -1.567  1.00 62.19  ? 50  GLU A CG    1 
ATOM   379  C  CD    . GLU A 1 50  ? 4.181  -19.774 -0.666  1.00 76.23  ? 50  GLU A CD    1 
ATOM   380  O  OE1   . GLU A 1 50  ? 3.462  -20.793 -0.756  1.00 76.34  ? 50  GLU A OE1   1 
ATOM   381  O  OE2   . GLU A 1 50  ? 3.949  -18.843 0.137   1.00 76.99  ? 50  GLU A OE2   1 
ATOM   382  N  N     . GLU A 1 51  ? 7.361  -22.815 -4.514  1.00 57.52  ? 51  GLU A N     1 
ATOM   383  C  CA    . GLU A 1 51  ? 8.000  -24.072 -4.892  1.00 55.48  ? 51  GLU A CA    1 
ATOM   384  C  C     . GLU A 1 51  ? 9.506  -23.891 -5.023  1.00 57.05  ? 51  GLU A C     1 
ATOM   385  O  O     . GLU A 1 51  ? 10.291 -24.694 -4.505  1.00 58.31  ? 51  GLU A O     1 
ATOM   386  C  CB    . GLU A 1 51  ? 7.406  -24.596 -6.202  1.00 54.98  ? 51  GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 51  ? 5.960  -25.077 -6.111  1.00 68.59  ? 51  GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 51  ? 4.950  -23.941 -6.063  1.00 73.08  ? 51  GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 51  ? 5.362  -22.766 -6.186  1.00 65.11  ? 51  GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 51  ? 3.743  -24.227 -5.902  1.00 78.06  ? 51  GLU A OE2   1 
ATOM   391  N  N     . GLU A 1 52  ? 9.926  -22.831 -5.717  1.00 52.36  ? 52  GLU A N     1 
ATOM   392  C  CA    . GLU A 1 52  ? 11.347 -22.525 -5.831  1.00 49.84  ? 52  GLU A CA    1 
ATOM   393  C  C     . GLU A 1 52  ? 11.966 -22.284 -4.462  1.00 50.94  ? 52  GLU A C     1 
ATOM   394  O  O     . GLU A 1 52  ? 13.030 -22.829 -4.147  1.00 47.53  ? 52  GLU A O     1 
ATOM   395  C  CB    . GLU A 1 52  ? 11.540 -21.307 -6.733  1.00 43.64  ? 52  GLU A CB    1 
ATOM   396  C  CG    . GLU A 1 52  ? 12.835 -20.556 -6.520  1.00 40.84  ? 52  GLU A CG    1 
ATOM   397  C  CD    . GLU A 1 52  ? 12.915 -19.303 -7.371  1.00 44.16  ? 52  GLU A CD    1 
ATOM   398  O  OE1   . GLU A 1 52  ? 13.100 -19.431 -8.600  1.00 39.68  ? 52  GLU A OE1   1 
ATOM   399  O  OE2   . GLU A 1 52  ? 12.770 -18.193 -6.813  1.00 42.48  ? 52  GLU A OE2   1 
ATOM   400  N  N     . TYR A 1 53  ? 11.304 -21.475 -3.633  1.00 49.80  ? 53  TYR A N     1 
ATOM   401  C  CA    . TYR A 1 53  ? 11.791 -21.225 -2.281  1.00 49.35  ? 53  TYR A CA    1 
ATOM   402  C  C     . TYR A 1 53  ? 11.874 -22.517 -1.478  1.00 47.08  ? 53  TYR A C     1 
ATOM   403  O  O     . TYR A 1 53  ? 12.853 -22.749 -0.759  1.00 43.78  ? 53  TYR A O     1 
ATOM   404  C  CB    . TYR A 1 53  ? 10.881 -20.209 -1.592  1.00 46.44  ? 53  TYR A CB    1 
ATOM   405  C  CG    . TYR A 1 53  ? 11.353 -19.762 -0.231  1.00 47.97  ? 53  TYR A CG    1 
ATOM   406  C  CD1   . TYR A 1 53  ? 12.583 -19.139 -0.073  1.00 46.29  ? 53  TYR A CD1   1 
ATOM   407  C  CD2   . TYR A 1 53  ? 10.557 -19.939 0.892   1.00 47.64  ? 53  TYR A CD2   1 
ATOM   408  C  CE1   . TYR A 1 53  ? 13.014 -18.720 1.169   1.00 45.98  ? 53  TYR A CE1   1 
ATOM   409  C  CE2   . TYR A 1 53  ? 10.979 -19.523 2.137   1.00 45.17  ? 53  TYR A CE2   1 
ATOM   410  C  CZ    . TYR A 1 53  ? 12.208 -18.914 2.270   1.00 46.53  ? 53  TYR A CZ    1 
ATOM   411  O  OH    . TYR A 1 53  ? 12.632 -18.496 3.510   1.00 49.25  ? 53  TYR A OH    1 
ATOM   412  N  N     . GLY A 1 54  ? 10.859 -23.375 -1.596  1.00 49.25  ? 54  GLY A N     1 
ATOM   413  C  CA    . GLY A 1 54  ? 10.900 -24.652 -0.900  1.00 52.07  ? 54  GLY A CA    1 
ATOM   414  C  C     . GLY A 1 54  ? 12.056 -25.523 -1.354  1.00 54.44  ? 54  GLY A C     1 
ATOM   415  O  O     . GLY A 1 54  ? 12.815 -26.045 -0.533  1.00 50.29  ? 54  GLY A O     1 
ATOM   416  N  N     . ARG A 1 55  ? 12.210 -25.687 -2.673  1.00 52.70  ? 55  ARG A N     1 
ATOM   417  C  CA    . ARG A 1 55  ? 13.302 -26.504 -3.192  1.00 52.53  ? 55  ARG A CA    1 
ATOM   418  C  C     . ARG A 1 55  ? 14.658 -25.902 -2.854  1.00 51.95  ? 55  ARG A C     1 
ATOM   419  O  O     . ARG A 1 55  ? 15.621 -26.638 -2.607  1.00 52.21  ? 55  ARG A O     1 
ATOM   420  C  CB    . ARG A 1 55  ? 13.158 -26.676 -4.705  1.00 56.34  ? 55  ARG A CB    1 
ATOM   421  C  CG    . ARG A 1 55  ? 11.860 -27.347 -5.129  1.00 65.27  ? 55  ARG A CG    1 
ATOM   422  C  CD    . ARG A 1 55  ? 11.912 -27.805 -6.577  1.00 77.44  ? 55  ARG A CD    1 
ATOM   423  N  NE    . ARG A 1 55  ? 12.885 -28.874 -6.768  1.00 84.49  ? 55  ARG A NE    1 
ATOM   424  C  CZ    . ARG A 1 55  ? 12.637 -30.160 -6.557  1.00 80.58  ? 55  ARG A CZ    1 
ATOM   425  N  NH1   . ARG A 1 55  ? 11.447 -30.577 -6.153  1.00 80.87  ? 55  ARG A NH1   1 
ATOM   426  N  NH2   . ARG A 1 55  ? 13.608 -31.049 -6.752  1.00 74.80  ? 55  ARG A NH2   1 
ATOM   427  N  N     . LEU A 1 56  ? 14.748 -24.571 -2.836  1.00 48.65  ? 56  LEU A N     1 
ATOM   428  C  CA    . LEU A 1 56  ? 15.995 -23.911 -2.470  1.00 46.06  ? 56  LEU A CA    1 
ATOM   429  C  C     . LEU A 1 56  ? 16.394 -24.247 -1.039  1.00 49.06  ? 56  LEU A C     1 
ATOM   430  O  O     . LEU A 1 56  ? 17.556 -24.574 -0.769  1.00 48.85  ? 56  LEU A O     1 
ATOM   431  C  CB    . LEU A 1 56  ? 15.847 -22.401 -2.646  1.00 46.41  ? 56  LEU A CB    1 
ATOM   432  C  CG    . LEU A 1 56  ? 17.104 -21.559 -2.482  1.00 47.79  ? 56  LEU A CG    1 
ATOM   433  C  CD1   . LEU A 1 56  ? 17.991 -21.725 -3.698  1.00 47.51  ? 56  LEU A CD1   1 
ATOM   434  C  CD2   . LEU A 1 56  ? 16.745 -20.091 -2.259  1.00 46.87  ? 56  LEU A CD2   1 
ATOM   435  N  N     . LEU A 1 57  ? 15.439 -24.168 -0.108  1.00 47.38  ? 57  LEU A N     1 
ATOM   436  C  CA    . LEU A 1 57  ? 15.720 -24.512 1.283   1.00 50.54  ? 57  LEU A CA    1 
ATOM   437  C  C     . LEU A 1 57  ? 16.152 -25.966 1.419   1.00 53.10  ? 57  LEU A C     1 
ATOM   438  O  O     . LEU A 1 57  ? 17.075 -26.276 2.182   1.00 56.04  ? 57  LEU A O     1 
ATOM   439  C  CB    . LEU A 1 57  ? 14.490 -24.243 2.149   1.00 49.31  ? 57  LEU A CB    1 
ATOM   440  C  CG    . LEU A 1 57  ? 14.111 -22.778 2.358   1.00 46.99  ? 57  LEU A CG    1 
ATOM   441  C  CD1   . LEU A 1 57  ? 12.742 -22.682 3.001   1.00 48.96  ? 57  LEU A CD1   1 
ATOM   442  C  CD2   . LEU A 1 57  ? 15.157 -22.076 3.210   1.00 40.20  ? 57  LEU A CD2   1 
ATOM   443  N  N     . ALA A 1 58  ? 15.493 -26.874 0.694   1.00 53.60  ? 58  ALA A N     1 
ATOM   444  C  CA    . ALA A 1 58  ? 15.864 -28.283 0.773   1.00 57.52  ? 58  ALA A CA    1 
ATOM   445  C  C     . ALA A 1 58  ? 17.290 -28.502 0.285   1.00 55.00  ? 58  ALA A C     1 
ATOM   446  O  O     . ALA A 1 58  ? 18.053 -29.257 0.897   1.00 54.94  ? 58  ALA A O     1 
ATOM   447  C  CB    . ALA A 1 58  ? 14.881 -29.138 -0.027  1.00 53.45  ? 58  ALA A CB    1 
ATOM   448  N  N     . HIS A 1 59  ? 17.672 -27.842 -0.811  1.00 51.64  ? 59  HIS A N     1 
ATOM   449  C  CA    . HIS A 1 59  ? 19.045 -27.940 -1.295  1.00 52.61  ? 59  HIS A CA    1 
ATOM   450  C  C     . HIS A 1 59  ? 20.033 -27.463 -0.238  1.00 57.94  ? 59  HIS A C     1 
ATOM   451  O  O     . HIS A 1 59  ? 21.039 -28.130 0.036   1.00 58.91  ? 59  HIS A O     1 
ATOM   452  C  CB    . HIS A 1 59  ? 19.209 -27.133 -2.581  1.00 52.59  ? 59  HIS A CB    1 
ATOM   453  C  CG    . HIS A 1 59  ? 20.578 -27.226 -3.180  1.00 58.81  ? 59  HIS A CG    1 
ATOM   454  N  ND1   . HIS A 1 59  ? 21.228 -26.141 -3.726  1.00 62.00  ? 59  HIS A ND1   1 
ATOM   455  C  CD2   . HIS A 1 59  ? 21.418 -28.279 -3.321  1.00 61.39  ? 59  HIS A CD2   1 
ATOM   456  C  CE1   . HIS A 1 59  ? 22.411 -26.520 -4.177  1.00 63.94  ? 59  HIS A CE1   1 
ATOM   457  N  NE2   . HIS A 1 59  ? 22.550 -27.813 -3.944  1.00 67.64  ? 59  HIS A NE2   1 
ATOM   458  N  N     . MET A 1 60  ? 19.761 -26.302 0.369   1.00 55.51  ? 60  MET A N     1 
ATOM   459  C  CA    . MET A 1 60  ? 20.636 -25.797 1.421   1.00 52.72  ? 60  MET A CA    1 
ATOM   460  C  C     . MET A 1 60  ? 20.676 -26.740 2.613   1.00 53.55  ? 60  MET A C     1 
ATOM   461  O  O     . MET A 1 60  ? 21.727 -26.896 3.245   1.00 55.63  ? 60  MET A O     1 
ATOM   462  C  CB    . MET A 1 60  ? 20.187 -24.406 1.861   1.00 49.57  ? 60  MET A CB    1 
ATOM   463  C  CG    . MET A 1 60  ? 20.565 -23.314 0.885   1.00 49.33  ? 60  MET A CG    1 
ATOM   464  S  SD    . MET A 1 60  ? 20.211 -21.675 1.532   1.00 40.92  ? 60  MET A SD    1 
ATOM   465  C  CE    . MET A 1 60  ? 18.462 -21.550 1.168   1.00 43.79  ? 60  MET A CE    1 
ATOM   466  N  N     . GLN A 1 61  ? 19.549 -27.379 2.931   1.00 51.18  ? 61  GLN A N     1 
ATOM   467  C  CA    . GLN A 1 61  ? 19.529 -28.338 4.028   1.00 55.40  ? 61  GLN A CA    1 
ATOM   468  C  C     . GLN A 1 61  ? 20.316 -29.599 3.684   1.00 61.90  ? 61  GLN A C     1 
ATOM   469  O  O     . GLN A 1 61  ? 20.923 -30.208 4.573   1.00 55.77  ? 61  GLN A O     1 
ATOM   470  C  CB    . GLN A 1 61  ? 18.085 -28.686 4.390   1.00 55.90  ? 61  GLN A CB    1 
ATOM   471  C  CG    . GLN A 1 61  ? 17.932 -29.507 5.661   1.00 52.43  ? 61  GLN A CG    1 
ATOM   472  C  CD    . GLN A 1 61  ? 16.481 -29.843 5.959   1.00 60.02  ? 61  GLN A CD    1 
ATOM   473  O  OE1   . GLN A 1 61  ? 15.648 -29.888 5.053   1.00 60.90  ? 61  GLN A OE1   1 
ATOM   474  N  NE2   . GLN A 1 61  ? 16.170 -30.072 7.234   1.00 52.48  ? 61  GLN A NE2   1 
ATOM   475  N  N     . GLU A 1 62  ? 20.323 -30.000 2.408   1.00 64.57  ? 62  GLU A N     1 
ATOM   476  C  CA    . GLU A 1 62  ? 21.103 -31.168 2.004   1.00 64.37  ? 62  GLU A CA    1 
ATOM   477  C  C     . GLU A 1 62  ? 22.593 -30.854 1.940   1.00 63.23  ? 62  GLU A C     1 
ATOM   478  O  O     . GLU A 1 62  ? 23.422 -31.745 2.157   1.00 63.65  ? 62  GLU A O     1 
ATOM   479  C  CB    . GLU A 1 62  ? 20.613 -31.694 0.653   1.00 63.59  ? 62  GLU A CB    1 
ATOM   480  C  CG    . GLU A 1 62  ? 19.178 -32.218 0.650   1.00 59.87  ? 62  GLU A CG    1 
ATOM   481  C  CD    . GLU A 1 62  ? 18.612 -32.363 -0.754  1.00 58.15  ? 62  GLU A CD    1 
ATOM   482  O  OE1   . GLU A 1 62  ? 19.342 -32.063 -1.721  1.00 59.46  ? 62  GLU A OE1   1 
ATOM   483  O  OE2   . GLU A 1 62  ? 17.439 -32.769 -0.893  1.00 56.21  ? 62  GLU A OE2   1 
ATOM   484  N  N     . GLU A 1 63  ? 22.954 -29.604 1.650   1.00 58.21  ? 63  GLU A N     1 
ATOM   485  C  CA    . GLU A 1 63  ? 24.352 -29.191 1.602   1.00 62.63  ? 63  GLU A CA    1 
ATOM   486  C  C     . GLU A 1 63  ? 24.917 -28.842 2.972   1.00 61.97  ? 63  GLU A C     1 
ATOM   487  O  O     . GLU A 1 63  ? 26.075 -28.419 3.056   1.00 61.10  ? 63  GLU A O     1 
ATOM   488  C  CB    . GLU A 1 63  ? 24.514 -27.987 0.670   1.00 62.24  ? 63  GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 63  ? 24.193 -28.272 -0.786  1.00 68.10  ? 63  GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 63  ? 25.262 -29.100 -1.468  1.00 73.73  ? 63  GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 63  ? 26.412 -29.109 -0.980  1.00 79.13  ? 63  GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 63  ? 24.952 -29.743 -2.493  1.00 76.61  ? 63  GLU A OE2   1 
ATOM   493  N  N     . GLY A 1 64  ? 24.133 -28.996 4.038   1.00 61.09  ? 64  GLY A N     1 
ATOM   494  C  CA    . GLY A 1 64  ? 24.570 -28.597 5.360   1.00 58.86  ? 64  GLY A CA    1 
ATOM   495  C  C     . GLY A 1 64  ? 24.684 -27.105 5.579   1.00 57.26  ? 64  GLY A C     1 
ATOM   496  O  O     . GLY A 1 64  ? 25.243 -26.688 6.598   1.00 59.20  ? 64  GLY A O     1 
ATOM   497  N  N     . VAL A 1 65  ? 24.168 -26.284 4.663   1.00 56.72  ? 65  VAL A N     1 
ATOM   498  C  CA    . VAL A 1 65  ? 24.327 -24.838 4.792   1.00 54.96  ? 65  VAL A CA    1 
ATOM   499  C  C     . VAL A 1 65  ? 23.455 -24.300 5.919   1.00 57.28  ? 65  VAL A C     1 
ATOM   500  O  O     . VAL A 1 65  ? 23.898 -23.475 6.728   1.00 59.03  ? 65  VAL A O     1 
ATOM   501  C  CB    . VAL A 1 65  ? 24.016 -24.140 3.456   1.00 52.63  ? 65  VAL A CB    1 
ATOM   502  C  CG1   . VAL A 1 65  ? 24.109 -22.634 3.618   1.00 52.43  ? 65  VAL A CG1   1 
ATOM   503  C  CG2   . VAL A 1 65  ? 24.968 -24.617 2.377   1.00 54.13  ? 65  VAL A CG2   1 
ATOM   504  N  N     . ILE A 1 66  ? 22.202 -24.751 5.990   1.00 57.62  ? 66  ILE A N     1 
ATOM   505  C  CA    . ILE A 1 66  ? 21.268 -24.290 7.007   1.00 52.59  ? 66  ILE A CA    1 
ATOM   506  C  C     . ILE A 1 66  ? 20.658 -25.491 7.716   1.00 55.45  ? 66  ILE A C     1 
ATOM   507  O  O     . ILE A 1 66  ? 20.643 -26.611 7.201   1.00 52.20  ? 66  ILE A O     1 
ATOM   508  C  CB    . ILE A 1 66  ? 20.150 -23.401 6.423   1.00 47.10  ? 66  ILE A CB    1 
ATOM   509  C  CG1   . ILE A 1 66  ? 19.277 -24.208 5.466   1.00 48.47  ? 66  ILE A CG1   1 
ATOM   510  C  CG2   . ILE A 1 66  ? 20.738 -22.193 5.713   1.00 54.87  ? 66  ILE A CG2   1 
ATOM   511  C  CD1   . ILE A 1 66  ? 18.109 -23.426 4.920   1.00 52.90  ? 66  ILE A CD1   1 
ATOM   512  N  N     . ARG A 1 67  ? 20.151 -25.238 8.918   1.00 54.46  ? 67  ARG A N     1 
ATOM   513  C  CA    . ARG A 1 67  ? 19.430 -26.224 9.704   1.00 50.28  ? 67  ARG A CA    1 
ATOM   514  C  C     . ARG A 1 67  ? 17.984 -25.781 9.872   1.00 50.49  ? 67  ARG A C     1 
ATOM   515  O  O     . ARG A 1 67  ? 17.684 -24.584 9.894   1.00 51.60  ? 67  ARG A O     1 
ATOM   516  C  CB    . ARG A 1 67  ? 20.068 -26.418 11.083  1.00 54.30  ? 67  ARG A CB    1 
ATOM   517  C  CG    . ARG A 1 67  ? 21.379 -27.178 11.065  1.00 59.29  ? 67  ARG A CG    1 
ATOM   518  C  CD    . ARG A 1 67  ? 21.910 -27.371 12.475  1.00 60.33  ? 67  ARG A CD    1 
ATOM   519  N  NE    . ARG A 1 67  ? 20.896 -27.910 13.373  1.00 60.18  ? 67  ARG A NE    1 
ATOM   520  C  CZ    . ARG A 1 67  ? 20.623 -29.202 13.509  1.00 73.93  ? 67  ARG A CZ    1 
ATOM   521  N  NH1   . ARG A 1 67  ? 21.257 -30.122 12.797  1.00 73.11  ? 67  ARG A NH1   1 
ATOM   522  N  NH2   . ARG A 1 67  ? 19.693 -29.582 14.381  1.00 69.82  ? 67  ARG A NH2   1 
ATOM   523  N  N     . LYS A 1 68  ? 17.088 -26.757 9.989   1.00 47.47  ? 68  LYS A N     1 
ATOM   524  C  CA    . LYS A 1 68  ? 15.675 -26.482 10.197  1.00 52.35  ? 68  LYS A CA    1 
ATOM   525  C  C     . LYS A 1 68  ? 15.376 -26.416 11.688  1.00 52.36  ? 68  LYS A C     1 
ATOM   526  O  O     . LYS A 1 68  ? 15.884 -27.222 12.471  1.00 53.88  ? 68  LYS A O     1 
ATOM   527  C  CB    . LYS A 1 68  ? 14.807 -27.555 9.539   1.00 51.66  ? 68  LYS A CB    1 
ATOM   528  C  CG    . LYS A 1 68  ? 13.336 -27.186 9.429   1.00 51.29  ? 68  LYS A CG    1 
ATOM   529  C  CD    . LYS A 1 68  ? 12.572 -28.213 8.607   1.00 55.44  ? 68  LYS A CD    1 
ATOM   530  C  CE    . LYS A 1 68  ? 11.184 -27.712 8.237   1.00 59.58  ? 68  LYS A CE    1 
ATOM   531  N  NZ    . LYS A 1 68  ? 10.329 -27.481 9.434   1.00 64.81  ? 68  LYS A NZ    1 
ATOM   532  N  N     . LEU A 1 69  ? 14.555 -25.445 12.074  1.00 51.10  ? 69  LEU A N     1 
ATOM   533  C  CA    . LEU A 1 69  ? 14.127 -25.274 13.461  1.00 58.72  ? 69  LEU A CA    1 
ATOM   534  C  C     . LEU A 1 69  ? 12.760 -25.936 13.601  1.00 60.53  ? 69  LEU A C     1 
ATOM   535  O  O     . LEU A 1 69  ? 11.732 -25.342 13.266  1.00 61.50  ? 69  LEU A O     1 
ATOM   536  C  CB    . LEU A 1 69  ? 14.095 -23.795 13.832  1.00 50.75  ? 69  LEU A CB    1 
ATOM   537  C  CG    . LEU A 1 69  ? 15.445 -23.088 13.669  1.00 49.78  ? 69  LEU A CG    1 
ATOM   538  C  CD1   . LEU A 1 69  ? 15.272 -21.586 13.536  1.00 42.67  ? 69  LEU A CD1   1 
ATOM   539  C  CD2   . LEU A 1 69  ? 16.365 -23.424 14.837  1.00 45.25  ? 69  LEU A CD2   1 
ATOM   540  N  N     . LYS A 1 70  ? 12.753 -27.175 14.097  1.00 70.13  ? 70  LYS A N     1 
ATOM   541  C  CA    . LYS A 1 70  ? 11.527 -27.966 14.106  1.00 72.04  ? 70  LYS A CA    1 
ATOM   542  C  C     . LYS A 1 70  ? 10.496 -27.449 15.103  1.00 72.91  ? 70  LYS A C     1 
ATOM   543  O  O     . LYS A 1 70  ? 9.316  -27.793 14.985  1.00 73.94  ? 70  LYS A O     1 
ATOM   544  C  CB    . LYS A 1 70  ? 11.848 -29.433 14.397  1.00 75.31  ? 70  LYS A CB    1 
ATOM   545  C  CG    . LYS A 1 70  ? 12.592 -29.673 15.700  1.00 82.44  ? 70  LYS A CG    1 
ATOM   546  C  CD    . LYS A 1 70  ? 12.762 -31.164 15.966  1.00 89.04  ? 70  LYS A CD    1 
ATOM   547  C  CE    . LYS A 1 70  ? 13.487 -31.422 17.281  1.00 85.65  ? 70  LYS A CE    1 
ATOM   548  N  NZ    . LYS A 1 70  ? 14.880 -30.892 17.261  1.00 83.44  ? 70  LYS A NZ    1 
ATOM   549  N  N     . LYS A 1 71  ? 10.907 -26.630 16.074  1.00 59.75  ? 71  LYS A N     1 
ATOM   550  C  CA    . LYS A 1 71  ? 9.948  -26.099 17.037  1.00 64.20  ? 71  LYS A CA    1 
ATOM   551  C  C     . LYS A 1 71  ? 9.003  -25.089 16.397  1.00 64.06  ? 71  LYS A C     1 
ATOM   552  O  O     . LYS A 1 71  ? 7.871  -24.920 16.864  1.00 65.27  ? 71  LYS A O     1 
ATOM   553  C  CB    . LYS A 1 71  ? 10.685 -25.460 18.215  1.00 64.23  ? 71  LYS A CB    1 
ATOM   554  C  CG    . LYS A 1 71  ? 9.776  -24.963 19.322  1.00 59.02  ? 71  LYS A CG    1 
ATOM   555  C  CD    . LYS A 1 71  ? 10.566 -24.522 20.536  1.00 61.69  ? 71  LYS A CD    1 
ATOM   556  C  CE    . LYS A 1 71  ? 9.633  -24.227 21.700  1.00 75.05  ? 71  LYS A CE    1 
ATOM   557  N  NZ    . LYS A 1 71  ? 10.371 -24.011 22.973  1.00 80.99  ? 71  LYS A NZ    1 
ATOM   558  N  N     . TYR A 1 72  ? 9.437  -24.422 15.335  1.00 61.28  ? 72  TYR A N     1 
ATOM   559  C  CA    . TYR A 1 72  ? 8.655  -23.376 14.695  1.00 63.02  ? 72  TYR A CA    1 
ATOM   560  C  C     . TYR A 1 72  ? 8.204  -23.818 13.309  1.00 62.32  ? 72  TYR A C     1 
ATOM   561  O  O     . TYR A 1 72  ? 8.593  -24.874 12.801  1.00 65.27  ? 72  TYR A O     1 
ATOM   562  C  CB    . TYR A 1 72  ? 9.462  -22.075 14.607  1.00 56.79  ? 72  TYR A CB    1 
ATOM   563  C  CG    . TYR A 1 72  ? 10.084 -21.666 15.922  1.00 59.18  ? 72  TYR A CG    1 
ATOM   564  C  CD1   . TYR A 1 72  ? 9.290  -21.326 17.012  1.00 55.19  ? 72  TYR A CD1   1 
ATOM   565  C  CD2   . TYR A 1 72  ? 11.464 -21.619 16.075  1.00 53.23  ? 72  TYR A CD2   1 
ATOM   566  C  CE1   . TYR A 1 72  ? 9.853  -20.953 18.217  1.00 58.20  ? 72  TYR A CE1   1 
ATOM   567  C  CE2   . TYR A 1 72  ? 12.036 -21.246 17.276  1.00 55.54  ? 72  TYR A CE2   1 
ATOM   568  C  CZ    . TYR A 1 72  ? 11.227 -20.913 18.342  1.00 60.54  ? 72  TYR A CZ    1 
ATOM   569  O  OH    . TYR A 1 72  ? 11.796 -20.537 19.539  1.00 61.00  ? 72  TYR A OH    1 
ATOM   570  N  N     . ASP A 1 73  ? 7.375  -22.979 12.694  1.00 61.07  ? 73  ASP A N     1 
ATOM   571  C  CA    . ASP A 1 73  ? 6.794  -23.260 11.386  1.00 62.00  ? 73  ASP A CA    1 
ATOM   572  C  C     . ASP A 1 73  ? 7.666  -22.623 10.310  1.00 58.64  ? 73  ASP A C     1 
ATOM   573  O  O     . ASP A 1 73  ? 7.668  -21.398 10.150  1.00 58.11  ? 73  ASP A O     1 
ATOM   574  C  CB    . ASP A 1 73  ? 5.361  -22.737 11.322  1.00 65.06  ? 73  ASP A CB    1 
ATOM   575  C  CG    . ASP A 1 73  ? 4.745  -22.875 9.943   1.00 67.67  ? 73  ASP A CG    1 
ATOM   576  O  OD1   . ASP A 1 73  ? 5.193  -23.745 9.166   1.00 76.21  ? 73  ASP A OD1   1 
ATOM   577  O  OD2   . ASP A 1 73  ? 3.810  -22.106 9.634   1.00 65.50  ? 73  ASP A OD2   1 
ATOM   578  N  N     . ASN A 1 74  ? 8.406  -23.457 9.574   1.00 60.82  ? 74  ASN A N     1 
ATOM   579  C  CA    . ASN A 1 74  ? 9.205  -23.016 8.429   1.00 48.95  ? 74  ASN A CA    1 
ATOM   580  C  C     . ASN A 1 74  ? 10.251 -21.978 8.844   1.00 47.07  ? 74  ASN A C     1 
ATOM   581  O  O     . ASN A 1 74  ? 10.372 -20.906 8.249   1.00 45.26  ? 74  ASN A O     1 
ATOM   582  C  CB    . ASN A 1 74  ? 8.306  -22.480 7.309   1.00 49.11  ? 74  ASN A CB    1 
ATOM   583  C  CG    . ASN A 1 74  ? 9.063  -22.234 6.007   1.00 54.52  ? 74  ASN A CG    1 
ATOM   584  O  OD1   . ASN A 1 74  ? 10.033 -22.929 5.690   1.00 53.27  ? 74  ASN A OD1   1 
ATOM   585  N  ND2   . ASN A 1 74  ? 8.625  -21.233 5.252   1.00 53.85  ? 74  ASN A ND2   1 
ATOM   586  N  N     . CYS A 1 75  ? 11.019 -22.308 9.877   1.00 47.14  ? 75  CYS A N     1 
ATOM   587  C  CA    . CYS A 1 75  ? 12.112 -21.461 10.327  1.00 46.51  ? 75  CYS A CA    1 
ATOM   588  C  C     . CYS A 1 75  ? 13.429 -22.212 10.199  1.00 46.55  ? 75  CYS A C     1 
ATOM   589  O  O     . CYS A 1 75  ? 13.480 -23.440 10.327  1.00 48.80  ? 75  CYS A O     1 
ATOM   590  C  CB    . CYS A 1 75  ? 11.908 -20.990 11.769  1.00 47.82  ? 75  CYS A CB    1 
ATOM   591  S  SG    . CYS A 1 75  ? 10.587 -19.769 11.954  1.00 48.01  ? 75  CYS A SG    1 
ATOM   592  N  N     . TRP A 1 76  ? 14.495 -21.458 9.939   1.00 42.37  ? 76  TRP A N     1 
ATOM   593  C  CA    . TRP A 1 76  ? 15.777 -22.035 9.576   1.00 44.94  ? 76  TRP A CA    1 
ATOM   594  C  C     . TRP A 1 76  ? 16.904 -21.253 10.233  1.00 44.29  ? 76  TRP A C     1 
ATOM   595  O  O     . TRP A 1 76  ? 16.807 -20.041 10.437  1.00 50.08  ? 76  TRP A O     1 
ATOM   596  C  CB    . TRP A 1 76  ? 15.958 -22.052 8.053   1.00 45.29  ? 76  TRP A CB    1 
ATOM   597  C  CG    . TRP A 1 76  ? 14.802 -22.675 7.327   1.00 41.06  ? 76  TRP A CG    1 
ATOM   598  C  CD1   . TRP A 1 76  ? 13.623 -22.074 6.994   1.00 43.31  ? 76  TRP A CD1   1 
ATOM   599  C  CD2   . TRP A 1 76  ? 14.715 -24.021 6.846   1.00 47.30  ? 76  TRP A CD2   1 
ATOM   600  N  NE1   . TRP A 1 76  ? 12.806 -22.962 6.339   1.00 41.40  ? 76  TRP A NE1   1 
ATOM   601  C  CE2   . TRP A 1 76  ? 13.454 -24.164 6.232   1.00 47.38  ? 76  TRP A CE2   1 
ATOM   602  C  CE3   . TRP A 1 76  ? 15.579 -25.119 6.873   1.00 52.82  ? 76  TRP A CE3   1 
ATOM   603  C  CZ2   . TRP A 1 76  ? 13.039 -25.360 5.651   1.00 52.00  ? 76  TRP A CZ2   1 
ATOM   604  C  CZ3   . TRP A 1 76  ? 15.167 -26.304 6.293   1.00 51.02  ? 76  TRP A CZ3   1 
ATOM   605  C  CH2   . TRP A 1 76  ? 13.908 -26.416 5.693   1.00 52.15  ? 76  TRP A CH2   1 
ATOM   606  N  N     . LEU A 1 77  ? 17.977 -21.965 10.556  1.00 45.35  ? 77  LEU A N     1 
ATOM   607  C  CA    . LEU A 1 77  ? 19.154 -21.395 11.192  1.00 46.50  ? 77  LEU A CA    1 
ATOM   608  C  C     . LEU A 1 77  ? 20.364 -21.561 10.281  1.00 49.98  ? 77  LEU A C     1 
ATOM   609  O  O     . LEU A 1 77  ? 20.555 -22.619 9.676   1.00 52.62  ? 77  LEU A O     1 
ATOM   610  C  CB    . LEU A 1 77  ? 19.420 -22.068 12.539  1.00 39.90  ? 77  LEU A CB    1 
ATOM   611  C  CG    . LEU A 1 77  ? 20.706 -21.673 13.259  1.00 45.88  ? 77  LEU A CG    1 
ATOM   612  C  CD1   . LEU A 1 77  ? 20.745 -20.172 13.483  1.00 50.82  ? 77  LEU A CD1   1 
ATOM   613  C  CD2   . LEU A 1 77  ? 20.818 -22.414 14.578  1.00 46.05  ? 77  LEU A CD2   1 
ATOM   614  N  N     . ALA A 1 78  ? 21.178 -20.511 10.186  1.00 45.80  ? 78  ALA A N     1 
ATOM   615  C  CA    . ALA A 1 78  ? 22.429 -20.550 9.441   1.00 47.06  ? 78  ALA A CA    1 
ATOM   616  C  C     . ALA A 1 78  ? 23.565 -20.094 10.344  1.00 47.42  ? 78  ALA A C     1 
ATOM   617  O  O     . ALA A 1 78  ? 23.445 -19.073 11.026  1.00 55.45  ? 78  ALA A O     1 
ATOM   618  C  CB    . ALA A 1 78  ? 22.360 -19.665 8.191   1.00 42.66  ? 78  ALA A CB    1 
ATOM   619  N  N     . LEU A 1 79  ? 24.660 -20.848 10.350  1.00 47.38  ? 79  LEU A N     1 
ATOM   620  C  CA    . LEU A 1 79  ? 25.877 -20.471 11.060  1.00 48.26  ? 79  LEU A CA    1 
ATOM   621  C  C     . LEU A 1 79  ? 26.949 -20.116 10.038  1.00 53.13  ? 79  LEU A C     1 
ATOM   622  O  O     . LEU A 1 79  ? 27.296 -20.941 9.186   1.00 56.26  ? 79  LEU A O     1 
ATOM   623  C  CB    . LEU A 1 79  ? 26.354 -21.600 11.972  1.00 48.92  ? 79  LEU A CB    1 
ATOM   624  C  CG    . LEU A 1 79  ? 25.328 -22.061 13.008  1.00 55.87  ? 79  LEU A CG    1 
ATOM   625  C  CD1   . LEU A 1 79  ? 25.924 -23.109 13.935  1.00 56.34  ? 79  LEU A CD1   1 
ATOM   626  C  CD2   . LEU A 1 79  ? 24.797 -20.872 13.798  1.00 53.04  ? 79  LEU A CD2   1 
ATOM   627  N  N     . THR A 1 80  ? 27.472 -18.899 10.125  1.00 46.77  ? 80  THR A N     1 
ATOM   628  C  CA    . THR A 1 80  ? 28.458 -18.405 9.177   1.00 50.70  ? 80  THR A CA    1 
ATOM   629  C  C     . THR A 1 80  ? 29.872 -18.582 9.721   1.00 57.37  ? 80  THR A C     1 
ATOM   630  O  O     . THR A 1 80  ? 30.086 -18.924 10.887  1.00 51.03  ? 80  THR A O     1 
ATOM   631  C  CB    . THR A 1 80  ? 28.207 -16.926 8.849   1.00 53.25  ? 80  THR A CB    1 
ATOM   632  O  OG1   . THR A 1 80  ? 28.620 -16.106 9.951   1.00 50.48  ? 80  THR A OG1   1 
ATOM   633  C  CG2   . THR A 1 80  ? 26.731 -16.683 8.568   1.00 49.72  ? 80  THR A CG2   1 
ATOM   634  N  N     . ASP A 1 81  ? 30.842 -18.350 8.842   1.00 55.77  ? 81  ASP A N     1 
ATOM   635  C  CA    . ASP A 1 81  ? 32.230 -18.260 9.266   1.00 53.79  ? 81  ASP A CA    1 
ATOM   636  C  C     . ASP A 1 81  ? 32.374 -17.099 10.245  1.00 51.61  ? 81  ASP A C     1 
ATOM   637  O  O     . ASP A 1 81  ? 31.781 -16.034 10.031  1.00 50.97  ? 81  ASP A O     1 
ATOM   638  C  CB    . ASP A 1 81  ? 33.142 -18.055 8.049   1.00 53.70  ? 81  ASP A CB    1 
ATOM   639  C  CG    . ASP A 1 81  ? 34.624 -18.188 8.380   1.00 58.04  ? 81  ASP A CG    1 
ATOM   640  O  OD1   . ASP A 1 81  ? 35.139 -17.406 9.208   1.00 58.41  ? 81  ASP A OD1   1 
ATOM   641  O  OD2   . ASP A 1 81  ? 35.282 -19.075 7.795   1.00 55.91  ? 81  ASP A OD2   1 
ATOM   642  N  N     . PRO A 1 82  ? 33.123 -17.269 11.338  1.00 50.69  ? 82  PRO A N     1 
ATOM   643  C  CA    . PRO A 1 82  ? 33.277 -16.165 12.301  1.00 54.62  ? 82  PRO A CA    1 
ATOM   644  C  C     . PRO A 1 82  ? 33.942 -14.925 11.718  1.00 54.76  ? 82  PRO A C     1 
ATOM   645  O  O     . PRO A 1 82  ? 33.870 -13.860 12.344  1.00 59.43  ? 82  PRO A O     1 
ATOM   646  C  CB    . PRO A 1 82  ? 34.127 -16.785 13.421  1.00 55.41  ? 82  PRO A CB    1 
ATOM   647  C  CG    . PRO A 1 82  ? 34.755 -18.000 12.816  1.00 56.44  ? 82  PRO A CG    1 
ATOM   648  C  CD    . PRO A 1 82  ? 33.777 -18.503 11.800  1.00 56.74  ? 82  PRO A CD    1 
ATOM   649  N  N     . ARG A 1 83  ? 34.569 -15.020 10.547  1.00 54.95  ? 83  ARG A N     1 
ATOM   650  C  CA    . ARG A 1 83  ? 35.181 -13.873 9.887   1.00 55.14  ? 83  ARG A CA    1 
ATOM   651  C  C     . ARG A 1 83  ? 34.208 -13.106 9.003   1.00 51.63  ? 83  ARG A C     1 
ATOM   652  O  O     . ARG A 1 83  ? 34.599 -12.098 8.407   1.00 59.64  ? 83  ARG A O     1 
ATOM   653  C  CB    . ARG A 1 83  ? 36.377 -14.326 9.044   1.00 55.01  ? 83  ARG A CB    1 
ATOM   654  C  CG    . ARG A 1 83  ? 37.460 -15.039 9.831   1.00 58.86  ? 83  ARG A CG    1 
ATOM   655  C  CD    . ARG A 1 83  ? 38.476 -15.687 8.906   1.00 66.37  ? 83  ARG A CD    1 
ATOM   656  N  NE    . ARG A 1 83  ? 37.883 -16.735 8.083   1.00 64.19  ? 83  ARG A NE    1 
ATOM   657  C  CZ    . ARG A 1 83  ? 38.550 -17.451 7.189   1.00 66.09  ? 83  ARG A CZ    1 
ATOM   658  N  NH1   . ARG A 1 83  ? 39.842 -17.258 6.974   1.00 75.97  ? 83  ARG A NH1   1 
ATOM   659  N  NH2   . ARG A 1 83  ? 37.907 -18.383 6.491   1.00 67.41  ? 83  ARG A NH2   1 
ATOM   660  N  N     . ASP A 1 84  ? 32.954 -13.552 8.904   1.00 57.38  ? 84  ASP A N     1 
ATOM   661  C  CA    . ASP A 1 84  ? 31.960 -12.967 7.999   1.00 54.93  ? 84  ASP A CA    1 
ATOM   662  C  C     . ASP A 1 84  ? 30.661 -12.794 8.790   1.00 54.12  ? 84  ASP A C     1 
ATOM   663  O  O     . ASP A 1 84  ? 29.710 -13.558 8.617   1.00 53.11  ? 84  ASP A O     1 
ATOM   664  C  CB    . ASP A 1 84  ? 31.777 -13.859 6.763   1.00 45.72  ? 84  ASP A CB    1 
ATOM   665  C  CG    . ASP A 1 84  ? 30.922 -13.218 5.693   1.00 48.74  ? 84  ASP A CG    1 
ATOM   666  O  OD1   . ASP A 1 84  ? 30.644 -12.002 5.788   1.00 53.11  ? 84  ASP A OD1   1 
ATOM   667  O  OD2   . ASP A 1 84  ? 30.523 -13.935 4.751   1.00 51.28  ? 84  ASP A OD2   1 
ATOM   668  N  N     . VAL A 1 85  ? 30.621 -11.781 9.657   1.00 52.40  ? 85  VAL A N     1 
ATOM   669  C  CA    . VAL A 1 85  ? 29.535 -11.668 10.626  1.00 55.10  ? 85  VAL A CA    1 
ATOM   670  C  C     . VAL A 1 85  ? 28.881 -10.291 10.605  1.00 57.67  ? 85  VAL A C     1 
ATOM   671  O  O     . VAL A 1 85  ? 27.804 -10.104 11.182  1.00 57.30  ? 85  VAL A O     1 
ATOM   672  C  CB    . VAL A 1 85  ? 30.035 -11.997 12.045  1.00 54.35  ? 85  VAL A CB    1 
ATOM   673  C  CG1   . VAL A 1 85  ? 30.433 -13.464 12.145  1.00 54.15  ? 85  VAL A CG1   1 
ATOM   674  C  CG2   . VAL A 1 85  ? 31.197 -11.095 12.422  1.00 53.01  ? 85  VAL A CG2   1 
ATOM   675  N  N     . ALA A 1 86  ? 29.510 -9.318  9.950   1.00 61.08  ? 86  ALA A N     1 
ATOM   676  C  CA    . ALA A 1 86  ? 28.989 -7.956  9.960   1.00 60.52  ? 86  ALA A CA    1 
ATOM   677  C  C     . ALA A 1 86  ? 29.479 -7.216  8.720   1.00 58.26  ? 86  ALA A C     1 
ATOM   678  O  O     . ALA A 1 86  ? 30.153 -7.784  7.856   1.00 54.06  ? 86  ALA A O     1 
ATOM   679  C  CB    . ALA A 1 86  ? 29.397 -7.221  11.241  1.00 59.88  ? 86  ALA A CB    1 
ATOM   680  N  N     . ARG A 1 87  ? 29.119 -5.937  8.638   1.00 59.07  ? 87  ARG A N     1 
ATOM   681  C  CA    . ARG A 1 87  ? 29.625 -5.077  7.579   1.00 57.82  ? 87  ARG A CA    1 
ATOM   682  C  C     . ARG A 1 87  ? 31.088 -4.733  7.825   1.00 57.60  ? 87  ARG A C     1 
ATOM   683  O  O     . ARG A 1 87  ? 31.544 -4.631  8.967   1.00 61.52  ? 87  ARG A O     1 
ATOM   684  C  CB    . ARG A 1 87  ? 28.807 -3.787  7.489   1.00 54.11  ? 87  ARG A CB    1 
ATOM   685  C  CG    . ARG A 1 87  ? 27.431 -3.951  6.870   1.00 53.61  ? 87  ARG A CG    1 
ATOM   686  C  CD    . ARG A 1 87  ? 26.713 -2.614  6.734   1.00 43.26  ? 87  ARG A CD    1 
ATOM   687  N  NE    . ARG A 1 87  ? 26.389 -2.015  8.024   1.00 48.86  ? 87  ARG A NE    1 
ATOM   688  C  CZ    . ARG A 1 87  ? 27.093 -1.054  8.609   1.00 54.60  ? 87  ARG A CZ    1 
ATOM   689  N  NH1   . ARG A 1 87  ? 28.181 -0.554  8.048   1.00 51.87  ? 87  ARG A NH1   1 
ATOM   690  N  NH2   . ARG A 1 87  ? 26.693 -0.583  9.787   1.00 48.89  ? 87  ARG A NH2   1 
ATOM   691  N  N     . ILE A 1 88  ? 31.824 -4.552  6.737   1.00 57.79  ? 88  ILE A N     1 
ATOM   692  C  CA    . ILE A 1 88  ? 33.226 -4.142  6.786   1.00 58.65  ? 88  ILE A CA    1 
ATOM   693  C  C     . ILE A 1 88  ? 33.300 -2.795  6.077   1.00 59.21  ? 88  ILE A C     1 
ATOM   694  O  O     . ILE A 1 88  ? 33.414 -2.723  4.849   1.00 57.16  ? 88  ILE A O     1 
ATOM   695  C  CB    . ILE A 1 88  ? 34.161 -5.169  6.143   1.00 56.58  ? 88  ILE A CB    1 
ATOM   696  C  CG1   . ILE A 1 88  ? 33.919 -6.557  6.738   1.00 57.70  ? 88  ILE A CG1   1 
ATOM   697  C  CG2   . ILE A 1 88  ? 35.608 -4.756  6.335   1.00 63.31  ? 88  ILE A CG2   1 
ATOM   698  C  CD1   . ILE A 1 88  ? 34.751 -7.652  6.100   1.00 59.04  ? 88  ILE A CD1   1 
ATOM   699  N  N     . GLU A 1 89  ? 33.227 -1.712  6.854   1.00 58.07  ? 89  GLU A N     1 
ATOM   700  C  CA    . GLU A 1 89  ? 33.266 -0.376  6.269   1.00 59.90  ? 89  GLU A CA    1 
ATOM   701  C  C     . GLU A 1 89  ? 34.604 -0.094  5.599   1.00 59.11  ? 89  GLU A C     1 
ATOM   702  O  O     . GLU A 1 89  ? 34.649 0.616   4.588   1.00 58.70  ? 89  GLU A O     1 
ATOM   703  C  CB    . GLU A 1 89  ? 32.977 0.677   7.339   1.00 61.24  ? 89  GLU A CB    1 
ATOM   704  C  CG    . GLU A 1 89  ? 31.612 0.533   7.992   1.00 66.98  ? 89  GLU A CG    1 
ATOM   705  C  CD    . GLU A 1 89  ? 31.369 1.555   9.092   1.00 71.00  ? 89  GLU A CD    1 
ATOM   706  O  OE1   . GLU A 1 89  ? 32.186 2.492   9.237   1.00 70.73  ? 89  GLU A OE1   1 
ATOM   707  O  OE2   . GLU A 1 89  ? 30.356 1.417   9.813   1.00 68.34  ? 89  GLU A OE2   1 
ATOM   708  N  N     . SER A 1 90  ? 35.697 -0.641  6.138   1.00 64.20  ? 90  SER A N     1 
ATOM   709  C  CA    . SER A 1 90  ? 37.016 -0.401  5.563   1.00 63.34  ? 90  SER A CA    1 
ATOM   710  C  C     . SER A 1 90  ? 37.183 -1.057  4.199   1.00 60.95  ? 90  SER A C     1 
ATOM   711  O  O     . SER A 1 90  ? 38.063 -0.650  3.434   1.00 62.24  ? 90  SER A O     1 
ATOM   712  C  CB    . SER A 1 90  ? 38.106 -0.897  6.515   1.00 62.82  ? 90  SER A CB    1 
ATOM   713  O  OG    . SER A 1 90  ? 37.996 -2.291  6.741   1.00 68.83  ? 90  SER A OG    1 
ATOM   714  N  N     . LYS A 1 91  ? 36.363 -2.057  3.877   1.00 61.00  ? 91  LYS A N     1 
ATOM   715  C  CA    . LYS A 1 91  ? 36.396 -2.710  2.575   1.00 54.70  ? 91  LYS A CA    1 
ATOM   716  C  C     . LYS A 1 91  ? 35.180 -2.356  1.725   1.00 48.98  ? 91  LYS A C     1 
ATOM   717  O  O     . LYS A 1 91  ? 34.887 -3.048  0.744   1.00 47.61  ? 91  LYS A O     1 
ATOM   718  C  CB    . LYS A 1 91  ? 36.513 -4.225  2.747   1.00 54.90  ? 91  LYS A CB    1 
ATOM   719  C  CG    . LYS A 1 91  ? 37.880 -4.676  3.242   1.00 58.49  ? 91  LYS A CG    1 
ATOM   720  C  CD    . LYS A 1 91  ? 37.927 -6.177  3.461   1.00 64.15  ? 91  LYS A CD    1 
ATOM   721  C  CE    . LYS A 1 91  ? 39.354 -6.662  3.674   1.00 68.17  ? 91  LYS A CE    1 
ATOM   722  N  NZ    . LYS A 1 91  ? 40.014 -5.968  4.814   1.00 74.88  ? 91  LYS A NZ    1 
ATOM   723  N  N     . THR A 1 92  ? 34.468 -1.293  2.084   1.00 47.59  ? 92  THR A N     1 
ATOM   724  C  CA    . THR A 1 92  ? 33.339 -0.786  1.314   1.00 48.97  ? 92  THR A CA    1 
ATOM   725  C  C     . THR A 1 92  ? 33.772 0.503   0.626   1.00 49.69  ? 92  THR A C     1 
ATOM   726  O  O     . THR A 1 92  ? 34.159 1.467   1.296   1.00 51.74  ? 92  THR A O     1 
ATOM   727  C  CB    . THR A 1 92  ? 32.128 -0.547  2.217   1.00 49.11  ? 92  THR A CB    1 
ATOM   728  O  OG1   . THR A 1 92  ? 31.825 -1.752  2.929   1.00 52.12  ? 92  THR A OG1   1 
ATOM   729  C  CG2   . THR A 1 92  ? 30.916 -0.134  1.398   1.00 49.42  ? 92  THR A CG2   1 
ATOM   730  N  N     . VAL A 1 93  ? 33.711 0.518   -0.707  1.00 49.24  ? 93  VAL A N     1 
ATOM   731  C  CA    . VAL A 1 93  ? 34.267 1.602   -1.505  1.00 46.58  ? 93  VAL A CA    1 
ATOM   732  C  C     . VAL A 1 93  ? 33.214 2.138   -2.467  1.00 43.55  ? 93  VAL A C     1 
ATOM   733  O  O     . VAL A 1 93  ? 32.237 1.466   -2.805  1.00 42.20  ? 93  VAL A O     1 
ATOM   734  C  CB    . VAL A 1 93  ? 35.519 1.156   -2.290  1.00 45.58  ? 93  VAL A CB    1 
ATOM   735  C  CG1   . VAL A 1 93  ? 36.609 0.698   -1.335  1.00 49.40  ? 93  VAL A CG1   1 
ATOM   736  C  CG2   . VAL A 1 93  ? 35.161 0.053   -3.271  1.00 41.19  ? 93  VAL A CG2   1 
ATOM   737  N  N     . ILE A 1 94  ? 33.434 3.378   -2.905  1.00 43.34  ? 94  ILE A N     1 
ATOM   738  C  CA    . ILE A 1 94  ? 32.608 4.042   -3.907  1.00 43.09  ? 94  ILE A CA    1 
ATOM   739  C  C     . ILE A 1 94  ? 33.531 4.571   -4.995  1.00 45.98  ? 94  ILE A C     1 
ATOM   740  O  O     . ILE A 1 94  ? 34.545 5.212   -4.696  1.00 45.70  ? 94  ILE A O     1 
ATOM   741  C  CB    . ILE A 1 94  ? 31.771 5.184   -3.298  1.00 45.50  ? 94  ILE A CB    1 
ATOM   742  C  CG1   . ILE A 1 94  ? 30.786 4.632   -2.267  1.00 41.85  ? 94  ILE A CG1   1 
ATOM   743  C  CG2   . ILE A 1 94  ? 31.036 5.962   -4.386  1.00 38.95  ? 94  ILE A CG2   1 
ATOM   744  C  CD1   . ILE A 1 94  ? 29.880 5.677   -1.677  1.00 48.59  ? 94  ILE A CD1   1 
ATOM   745  N  N     . ILE A 1 95  ? 33.181 4.309   -6.251  1.00 48.00  ? 95  ILE A N     1 
ATOM   746  C  CA    . ILE A 1 95  ? 34.043 4.607   -7.391  1.00 47.56  ? 95  ILE A CA    1 
ATOM   747  C  C     . ILE A 1 95  ? 33.436 5.767   -8.170  1.00 46.24  ? 95  ILE A C     1 
ATOM   748  O  O     . ILE A 1 95  ? 32.332 5.649   -8.717  1.00 45.38  ? 95  ILE A O     1 
ATOM   749  C  CB    . ILE A 1 95  ? 34.237 3.377   -8.292  1.00 47.86  ? 95  ILE A CB    1 
ATOM   750  C  CG1   . ILE A 1 95  ? 35.139 2.345   -7.613  1.00 48.64  ? 95  ILE A CG1   1 
ATOM   751  C  CG2   . ILE A 1 95  ? 34.822 3.779   -9.638  1.00 46.48  ? 95  ILE A CG2   1 
ATOM   752  C  CD1   . ILE A 1 95  ? 34.419 1.405   -6.682  1.00 47.99  ? 95  ILE A CD1   1 
ATOM   753  N  N     . THR A 1 96  ? 34.153 6.889   -8.214  1.00 48.26  ? 96  THR A N     1 
ATOM   754  C  CA    . THR A 1 96  ? 33.781 8.026   -9.045  1.00 53.11  ? 96  THR A CA    1 
ATOM   755  C  C     . THR A 1 96  ? 35.033 8.590   -9.700  1.00 54.37  ? 96  THR A C     1 
ATOM   756  O  O     . THR A 1 96  ? 36.153 8.391   -9.223  1.00 52.93  ? 96  THR A O     1 
ATOM   757  C  CB    . THR A 1 96  ? 33.069 9.134   -8.249  1.00 52.41  ? 96  THR A CB    1 
ATOM   758  O  OG1   . THR A 1 96  ? 33.886 9.542   -7.146  1.00 51.71  ? 96  THR A OG1   1 
ATOM   759  C  CG2   . THR A 1 96  ? 31.715 8.652   -7.737  1.00 47.85  ? 96  THR A CG2   1 
ATOM   760  N  N     . GLN A 1 97  ? 34.825 9.301   -10.811 1.00 60.49  ? 97  GLN A N     1 
ATOM   761  C  CA    . GLN A 1 97  ? 35.944 9.921   -11.515 1.00 61.53  ? 97  GLN A CA    1 
ATOM   762  C  C     . GLN A 1 97  ? 36.689 10.897  -10.611 1.00 58.55  ? 97  GLN A C     1 
ATOM   763  O  O     . GLN A 1 97  ? 37.925 10.894  -10.569 1.00 55.41  ? 97  GLN A O     1 
ATOM   764  C  CB    . GLN A 1 97  ? 35.443 10.626  -12.776 1.00 60.53  ? 97  GLN A CB    1 
ATOM   765  C  CG    . GLN A 1 97  ? 36.540 11.253  -13.621 1.00 73.66  ? 97  GLN A CG    1 
ATOM   766  C  CD    . GLN A 1 97  ? 37.435 10.223  -14.284 1.00 80.41  ? 97  GLN A CD    1 
ATOM   767  O  OE1   . GLN A 1 97  ? 36.983 9.141   -14.664 1.00 84.12  ? 97  GLN A OE1   1 
ATOM   768  N  NE2   . GLN A 1 97  ? 38.714 10.554  -14.424 1.00 78.86  ? 97  GLN A NE2   1 
ATOM   769  N  N     . GLU A 1 98  ? 35.956 11.728  -9.874  1.00 57.15  ? 98  GLU A N     1 
ATOM   770  C  CA    . GLU A 1 98  ? 36.532 12.685  -8.940  1.00 56.87  ? 98  GLU A CA    1 
ATOM   771  C  C     . GLU A 1 98  ? 36.276 12.226  -7.511  1.00 50.00  ? 98  GLU A C     1 
ATOM   772  O  O     . GLU A 1 98  ? 35.164 11.811  -7.175  1.00 51.26  ? 98  GLU A O     1 
ATOM   773  C  CB    . GLU A 1 98  ? 35.939 14.084  -9.141  1.00 58.64  ? 98  GLU A CB    1 
ATOM   774  C  CG    . GLU A 1 98  ? 35.937 14.572  -10.581 1.00 66.23  ? 98  GLU A CG    1 
ATOM   775  C  CD    . GLU A 1 98  ? 37.269 15.150  -11.009 1.00 73.26  ? 98  GLU A CD    1 
ATOM   776  O  OE1   . GLU A 1 98  ? 38.068 15.529  -10.125 1.00 73.06  ? 98  GLU A OE1   1 
ATOM   777  O  OE2   . GLU A 1 98  ? 37.516 15.226  -12.231 1.00 80.10  ? 98  GLU A OE2   1 
ATOM   778  N  N     . GLN A 1 99  ? 37.306 12.313  -6.668  1.00 47.09  ? 99  GLN A N     1 
ATOM   779  C  CA    . GLN A 1 99  ? 37.138 11.937  -5.270  1.00 51.30  ? 99  GLN A CA    1 
ATOM   780  C  C     . GLN A 1 99  ? 36.165 12.863  -4.551  1.00 54.39  ? 99  GLN A C     1 
ATOM   781  O  O     . GLN A 1 99  ? 35.410 12.414  -3.680  1.00 54.24  ? 99  GLN A O     1 
ATOM   782  C  CB    . GLN A 1 99  ? 38.490 11.939  -4.558  1.00 49.97  ? 99  GLN A CB    1 
ATOM   783  C  CG    . GLN A 1 99  ? 38.404 11.508  -3.103  1.00 49.65  ? 99  GLN A CG    1 
ATOM   784  C  CD    . GLN A 1 99  ? 39.742 11.551  -2.395  1.00 54.19  ? 99  GLN A CD    1 
ATOM   785  O  OE1   . GLN A 1 99  ? 40.732 12.042  -2.938  1.00 53.28  ? 99  GLN A OE1   1 
ATOM   786  N  NE2   . GLN A 1 99  ? 39.778 11.032  -1.174  1.00 55.53  ? 99  GLN A NE2   1 
ATOM   787  N  N     . ARG A 1 100 ? 36.159 14.149  -4.911  1.00 50.09  ? 100 ARG A N     1 
ATOM   788  C  CA    . ARG A 1 100 ? 35.314 15.130  -4.242  1.00 50.20  ? 100 ARG A CA    1 
ATOM   789  C  C     . ARG A 1 100 ? 33.830 14.866  -4.459  1.00 50.62  ? 100 ARG A C     1 
ATOM   790  O  O     . ARG A 1 100 ? 33.005 15.362  -3.682  1.00 52.11  ? 100 ARG A O     1 
ATOM   791  C  CB    . ARG A 1 100 ? 35.674 16.540  -4.721  1.00 56.84  ? 100 ARG A CB    1 
ATOM   792  C  CG    . ARG A 1 100 ? 35.144 17.654  -3.832  1.00 59.88  ? 100 ARG A CG    1 
ATOM   793  C  CD    . ARG A 1 100 ? 35.600 19.023  -4.309  1.00 71.33  ? 100 ARG A CD    1 
ATOM   794  N  NE    . ARG A 1 100 ? 35.155 20.075  -3.403  1.00 72.73  ? 100 ARG A NE    1 
ATOM   795  C  CZ    . ARG A 1 100 ? 35.459 21.359  -3.533  1.00 75.66  ? 100 ARG A CZ    1 
ATOM   796  N  NH1   . ARG A 1 100 ? 36.216 21.794  -4.528  1.00 77.86  ? 100 ARG A NH1   1 
ATOM   797  N  NH2   . ARG A 1 100 ? 34.992 22.229  -2.640  1.00 70.75  ? 100 ARG A NH2   1 
ATOM   798  N  N     . ASP A 1 101 ? 33.467 14.102  -5.490  1.00 47.14  ? 101 ASP A N     1 
ATOM   799  C  CA    . ASP A 1 101 ? 32.063 13.761  -5.683  1.00 47.39  ? 101 ASP A CA    1 
ATOM   800  C  C     . ASP A 1 101 ? 31.593 12.733  -4.663  1.00 47.23  ? 101 ASP A C     1 
ATOM   801  O  O     . ASP A 1 101 ? 30.403 12.686  -4.333  1.00 42.25  ? 101 ASP A O     1 
ATOM   802  C  CB    . ASP A 1 101 ? 31.837 13.243  -7.101  1.00 51.89  ? 101 ASP A CB    1 
ATOM   803  C  CG    . ASP A 1 101 ? 32.161 14.277  -8.154  1.00 58.64  ? 101 ASP A CG    1 
ATOM   804  O  OD1   . ASP A 1 101 ? 31.896 15.474  -7.910  1.00 69.40  ? 101 ASP A OD1   1 
ATOM   805  O  OD2   . ASP A 1 101 ? 32.685 13.898  -9.223  1.00 65.76  ? 101 ASP A OD2   1 
ATOM   806  N  N     . THR A 1 102 ? 32.506 11.910  -4.152  1.00 45.32  ? 102 THR A N     1 
ATOM   807  C  CA    . THR A 1 102 ? 32.164 10.871  -3.190  1.00 52.65  ? 102 THR A CA    1 
ATOM   808  C  C     . THR A 1 102 ? 32.351 11.335  -1.751  1.00 50.08  ? 102 THR A C     1 
ATOM   809  O  O     . THR A 1 102 ? 31.499 11.074  -0.897  1.00 46.20  ? 102 THR A O     1 
ATOM   810  C  CB    . THR A 1 102 ? 33.013 9.621   -3.446  1.00 46.84  ? 102 THR A CB    1 
ATOM   811  O  OG1   . THR A 1 102 ? 32.690 9.080   -4.732  1.00 47.56  ? 102 THR A OG1   1 
ATOM   812  C  CG2   . THR A 1 102 ? 32.765 8.569   -2.379  1.00 45.34  ? 102 THR A CG2   1 
ATOM   813  N  N     . VAL A 1 103 ? 33.446 12.031  -1.471  1.00 52.27  ? 103 VAL A N     1 
ATOM   814  C  CA    . VAL A 1 103 ? 33.791 12.399  -0.104  1.00 47.31  ? 103 VAL A CA    1 
ATOM   815  C  C     . VAL A 1 103 ? 34.388 13.801  -0.117  1.00 52.91  ? 103 VAL A C     1 
ATOM   816  O  O     . VAL A 1 103 ? 35.073 14.174  -1.082  1.00 54.00  ? 103 VAL A O     1 
ATOM   817  C  CB    . VAL A 1 103 ? 34.748 11.361  0.509   1.00 48.98  ? 103 VAL A CB    1 
ATOM   818  C  CG1   . VAL A 1 103 ? 36.140 11.944  0.739   1.00 48.46  ? 103 VAL A CG1   1 
ATOM   819  C  CG2   . VAL A 1 103 ? 34.166 10.790  1.786   1.00 44.77  ? 103 VAL A CG2   1 
ATOM   820  N  N     . PRO A 1 104 ? 34.124 14.625  0.895   1.00 54.12  ? 104 PRO A N     1 
ATOM   821  C  CA    . PRO A 1 104 ? 34.779 15.936  0.960   1.00 50.70  ? 104 PRO A CA    1 
ATOM   822  C  C     . PRO A 1 104 ? 36.267 15.779  1.221   1.00 49.32  ? 104 PRO A C     1 
ATOM   823  O  O     . PRO A 1 104 ? 36.691 14.898  1.970   1.00 52.58  ? 104 PRO A O     1 
ATOM   824  C  CB    . PRO A 1 104 ? 34.075 16.633  2.133   1.00 50.99  ? 104 PRO A CB    1 
ATOM   825  C  CG    . PRO A 1 104 ? 32.793 15.881  2.319   1.00 49.94  ? 104 PRO A CG    1 
ATOM   826  C  CD    . PRO A 1 104 ? 33.105 14.463  1.945   1.00 47.67  ? 104 PRO A CD    1 
ATOM   827  N  N     . ILE A 1 105 ? 37.061 16.638  0.592   1.00 52.89  ? 105 ILE A N     1 
ATOM   828  C  CA    . ILE A 1 105 ? 38.509 16.610  0.778   1.00 56.53  ? 105 ILE A CA    1 
ATOM   829  C  C     . ILE A 1 105 ? 38.817 17.144  2.171   1.00 56.02  ? 105 ILE A C     1 
ATOM   830  O  O     . ILE A 1 105 ? 38.649 18.345  2.421   1.00 56.18  ? 105 ILE A O     1 
ATOM   831  C  CB    . ILE A 1 105 ? 39.232 17.421  -0.309  1.00 53.92  ? 105 ILE A CB    1 
ATOM   832  C  CG1   . ILE A 1 105 ? 38.908 16.859  -1.693  1.00 54.84  ? 105 ILE A CG1   1 
ATOM   833  C  CG2   . ILE A 1 105 ? 40.732 17.414  -0.069  1.00 56.65  ? 105 ILE A CG2   1 
ATOM   834  C  CD1   . ILE A 1 105 ? 39.249 15.389  -1.849  1.00 56.50  ? 105 ILE A CD1   1 
ATOM   835  N  N     . PRO A 1 106 ? 39.262 16.303  3.102   1.00 57.47  ? 106 PRO A N     1 
ATOM   836  C  CA    . PRO A 1 106 ? 39.463 16.769  4.477   1.00 57.97  ? 106 PRO A CA    1 
ATOM   837  C  C     . PRO A 1 106 ? 40.640 17.726  4.590   1.00 59.89  ? 106 PRO A C     1 
ATOM   838  O  O     . PRO A 1 106 ? 41.491 17.827  3.704   1.00 63.83  ? 106 PRO A O     1 
ATOM   839  C  CB    . PRO A 1 106 ? 39.719 15.477  5.258   1.00 56.89  ? 106 PRO A CB    1 
ATOM   840  C  CG    . PRO A 1 106 ? 40.283 14.542  4.249   1.00 59.30  ? 106 PRO A CG    1 
ATOM   841  C  CD    . PRO A 1 106 ? 39.625 14.884  2.939   1.00 52.83  ? 106 PRO A CD    1 
ATOM   842  N  N     . LYS A 1 107 ? 40.671 18.442  5.715   1.00 62.01  ? 107 LYS A N     1 
ATOM   843  C  CA    . LYS A 1 107 ? 41.737 19.407  5.965   1.00 66.76  ? 107 LYS A CA    1 
ATOM   844  C  C     . LYS A 1 107 ? 42.969 18.724  6.548   1.00 70.73  ? 107 LYS A C     1 
ATOM   845  O  O     . LYS A 1 107 ? 44.036 18.705  5.925   1.00 72.64  ? 107 LYS A O     1 
ATOM   846  C  CB    . LYS A 1 107 ? 41.234 20.514  6.898   1.00 65.35  ? 107 LYS A CB    1 
ATOM   847  C  CG    . LYS A 1 107 ? 41.560 21.924  6.431   1.00 59.96  ? 107 LYS A CG    1 
ATOM   848  C  CD    . LYS A 1 107 ? 40.930 22.968  7.345   1.00 66.20  ? 107 LYS A CD    1 
ATOM   849  C  CE    . LYS A 1 107 ? 41.148 24.374  6.811   1.00 67.64  ? 107 LYS A CE    1 
ATOM   850  N  NZ    . LYS A 1 107 ? 40.569 25.416  7.707   1.00 78.49  ? 107 LYS A NZ    1 
ATOM   851  N  N     . SER A 1 108 ? 42.838 18.161  7.752   1.00 82.72  ? 108 SER A N     1 
ATOM   852  C  CA    . SER A 1 108 ? 43.947 17.417  8.340   1.00 84.54  ? 108 SER A CA    1 
ATOM   853  C  C     . SER A 1 108 ? 44.235 16.149  7.547   1.00 82.93  ? 108 SER A C     1 
ATOM   854  O  O     . SER A 1 108 ? 45.399 15.791  7.334   1.00 84.66  ? 108 SER A O     1 
ATOM   855  C  CB    . SER A 1 108 ? 43.642 17.083  9.801   1.00 85.41  ? 108 SER A CB    1 
ATOM   856  O  OG    . SER A 1 108 ? 42.583 16.145  9.905   1.00 82.70  ? 108 SER A OG    1 
ATOM   857  N  N     . GLY A 1 109 ? 43.189 15.458  7.101   1.00 71.56  ? 109 GLY A N     1 
ATOM   858  C  CA    . GLY A 1 109 ? 43.372 14.334  6.207   1.00 72.37  ? 109 GLY A CA    1 
ATOM   859  C  C     . GLY A 1 109 ? 42.679 13.064  6.646   1.00 64.62  ? 109 GLY A C     1 
ATOM   860  O  O     . GLY A 1 109 ? 42.308 12.921  7.814   1.00 72.27  ? 109 GLY A O     1 
ATOM   861  N  N     . GLN A 1 110 ? 42.517 12.134  5.704   1.00 68.45  ? 110 GLN A N     1 
ATOM   862  C  CA    . GLN A 1 110 ? 41.841 10.859  5.922   1.00 64.56  ? 110 GLN A CA    1 
ATOM   863  C  C     . GLN A 1 110 ? 40.379 11.081  6.286   1.00 61.62  ? 110 GLN A C     1 
ATOM   864  O  O     . GLN A 1 110 ? 40.054 11.465  7.414   1.00 61.14  ? 110 GLN A O     1 
ATOM   865  C  CB    . GLN A 1 110 ? 42.557 10.034  6.997   1.00 64.96  ? 110 GLN A CB    1 
ATOM   866  C  CG    . GLN A 1 110 ? 42.019 8.620   7.174   1.00 67.81  ? 110 GLN A CG    1 
ATOM   867  C  CD    . GLN A 1 110 ? 42.461 7.663   6.076   1.00 66.98  ? 110 GLN A CD    1 
ATOM   868  O  OE1   . GLN A 1 110 ? 43.130 8.055   5.117   1.00 66.87  ? 110 GLN A OE1   1 
ATOM   869  N  NE2   . GLN A 1 110 ? 42.092 6.397   6.219   1.00 65.49  ? 110 GLN A NE2   1 
ATOM   870  N  N     . SER A 1 111 ? 39.492 10.832  5.330   1.00 57.54  ? 111 SER A N     1 
ATOM   871  C  CA    . SER A 1 111 ? 38.072 11.091  5.508   1.00 51.05  ? 111 SER A CA    1 
ATOM   872  C  C     . SER A 1 111 ? 37.379 9.936   6.221   1.00 54.51  ? 111 SER A C     1 
ATOM   873  O  O     . SER A 1 111 ? 37.661 8.762   5.959   1.00 53.72  ? 111 SER A O     1 
ATOM   874  C  CB    . SER A 1 111 ? 37.414 11.329  4.151   1.00 50.18  ? 111 SER A CB    1 
ATOM   875  O  OG    . SER A 1 111 ? 36.008 11.408  4.270   1.00 46.24  ? 111 SER A OG    1 
ATOM   876  N  N     . GLN A 1 112 ? 36.456 10.280  7.119   1.00 45.75  ? 112 GLN A N     1 
ATOM   877  C  CA    . GLN A 1 112 ? 35.603 9.311   7.791   1.00 47.18  ? 112 GLN A CA    1 
ATOM   878  C  C     . GLN A 1 112 ? 34.205 9.251   7.195   1.00 45.24  ? 112 GLN A C     1 
ATOM   879  O  O     . GLN A 1 112 ? 33.367 8.491   7.689   1.00 50.53  ? 112 GLN A O     1 
ATOM   880  C  CB    . GLN A 1 112 ? 35.497 9.637   9.284   1.00 47.91  ? 112 GLN A CB    1 
ATOM   881  C  CG    . GLN A 1 112 ? 36.823 9.776   10.004  1.00 53.32  ? 112 GLN A CG    1 
ATOM   882  C  CD    . GLN A 1 112 ? 36.642 10.116  11.469  1.00 56.66  ? 112 GLN A CD    1 
ATOM   883  O  OE1   . GLN A 1 112 ? 35.522 10.119  11.979  1.00 59.61  ? 112 GLN A OE1   1 
ATOM   884  N  NE2   . GLN A 1 112 ? 37.743 10.406  12.155  1.00 59.49  ? 112 GLN A NE2   1 
ATOM   885  N  N     . LEU A 1 113 ? 33.932 10.032  6.156   1.00 45.05  ? 113 LEU A N     1 
ATOM   886  C  CA    . LEU A 1 113 ? 32.602 10.130  5.573   1.00 42.72  ? 113 LEU A CA    1 
ATOM   887  C  C     . LEU A 1 113 ? 32.423 9.221   4.370   1.00 46.43  ? 113 LEU A C     1 
ATOM   888  O  O     . LEU A 1 113 ? 31.428 9.354   3.649   1.00 48.13  ? 113 LEU A O     1 
ATOM   889  C  CB    . LEU A 1 113 ? 32.310 11.581  5.181   1.00 49.00  ? 113 LEU A CB    1 
ATOM   890  C  CG    . LEU A 1 113 ? 32.367 12.568  6.347   1.00 48.37  ? 113 LEU A CG    1 
ATOM   891  C  CD1   . LEU A 1 113 ? 32.292 14.003  5.856   1.00 47.70  ? 113 LEU A CD1   1 
ATOM   892  C  CD2   . LEU A 1 113 ? 31.242 12.270  7.321   1.00 44.26  ? 113 LEU A CD2   1 
ATOM   893  N  N     . GLY A 1 114 ? 33.350 8.306   4.146   1.00 54.21  ? 114 GLY A N     1 
ATOM   894  C  CA    . GLY A 1 114 ? 33.292 7.397   3.018   1.00 43.24  ? 114 GLY A CA    1 
ATOM   895  C  C     . GLY A 1 114 ? 34.684 6.976   2.605   1.00 48.57  ? 114 GLY A C     1 
ATOM   896  O  O     . GLY A 1 114 ? 35.692 7.482   3.097   1.00 46.81  ? 114 GLY A O     1 
ATOM   897  N  N     . ARG A 1 115 ? 34.729 6.022   1.680   1.00 45.05  ? 115 ARG A N     1 
ATOM   898  C  CA    . ARG A 1 115 ? 35.988 5.522   1.144   1.00 50.89  ? 115 ARG A CA    1 
ATOM   899  C  C     . ARG A 1 115 ? 35.901 5.517   -0.373  1.00 46.36  ? 115 ARG A C     1 
ATOM   900  O  O     . ARG A 1 115 ? 35.068 4.808   -0.948  1.00 46.70  ? 115 ARG A O     1 
ATOM   901  C  CB    . ARG A 1 115 ? 36.308 4.123   1.680   1.00 55.62  ? 115 ARG A CB    1 
ATOM   902  C  CG    . ARG A 1 115 ? 37.671 3.600   1.241   1.00 66.14  ? 115 ARG A CG    1 
ATOM   903  C  CD    . ARG A 1 115 ? 38.066 2.343   2.002   1.00 73.54  ? 115 ARG A CD    1 
ATOM   904  N  NE    . ARG A 1 115 ? 38.221 2.599   3.430   1.00 80.00  ? 115 ARG A NE    1 
ATOM   905  C  CZ    . ARG A 1 115 ? 39.358 2.967   4.005   1.00 84.69  ? 115 ARG A CZ    1 
ATOM   906  N  NH1   . ARG A 1 115 ? 40.468 3.130   3.303   1.00 78.94  ? 115 ARG A NH1   1 
ATOM   907  N  NH2   . ARG A 1 115 ? 39.381 3.179   5.319   1.00 83.46  ? 115 ARG A NH2   1 
ATOM   908  N  N     . TRP A 1 116 ? 36.752 6.306   -1.015  1.00 48.76  ? 116 TRP A N     1 
ATOM   909  C  CA    . TRP A 1 116 ? 36.741 6.466   -2.461  1.00 50.59  ? 116 TRP A CA    1 
ATOM   910  C  C     . TRP A 1 116 ? 37.859 5.646   -3.089  1.00 49.86  ? 116 TRP A C     1 
ATOM   911  O  O     . TRP A 1 116 ? 38.971 5.578   -2.557  1.00 55.83  ? 116 TRP A O     1 
ATOM   912  C  CB    . TRP A 1 116 ? 36.893 7.941   -2.843  1.00 54.94  ? 116 TRP A CB    1 
ATOM   913  C  CG    . TRP A 1 116 ? 37.004 8.186   -4.320  1.00 50.35  ? 116 TRP A CG    1 
ATOM   914  C  CD1   . TRP A 1 116 ? 35.981 8.245   -5.221  1.00 49.49  ? 116 TRP A CD1   1 
ATOM   915  C  CD2   . TRP A 1 116 ? 38.206 8.419   -5.063  1.00 50.15  ? 116 TRP A CD2   1 
ATOM   916  N  NE1   . TRP A 1 116 ? 36.471 8.493   -6.479  1.00 49.85  ? 116 TRP A NE1   1 
ATOM   917  C  CE2   . TRP A 1 116 ? 37.835 8.607   -6.410  1.00 50.74  ? 116 TRP A CE2   1 
ATOM   918  C  CE3   . TRP A 1 116 ? 39.560 8.487   -4.721  1.00 50.74  ? 116 TRP A CE3   1 
ATOM   919  C  CZ2   . TRP A 1 116 ? 38.769 8.854   -7.415  1.00 51.16  ? 116 TRP A CZ2   1 
ATOM   920  C  CZ3   . TRP A 1 116 ? 40.487 8.735   -5.720  1.00 50.31  ? 116 TRP A CZ3   1 
ATOM   921  C  CH2   . TRP A 1 116 ? 40.087 8.915   -7.051  1.00 49.61  ? 116 TRP A CH2   1 
ATOM   922  N  N     . MET A 1 117 ? 37.557 5.023   -4.223  1.00 48.58  ? 117 MET A N     1 
ATOM   923  C  CA    . MET A 1 117 ? 38.535 4.272   -4.998  1.00 49.88  ? 117 MET A CA    1 
ATOM   924  C  C     . MET A 1 117 ? 38.412 4.681   -6.456  1.00 47.71  ? 117 MET A C     1 
ATOM   925  O  O     . MET A 1 117 ? 37.304 4.725   -6.998  1.00 49.89  ? 117 MET A O     1 
ATOM   926  C  CB    . MET A 1 117 ? 38.327 2.761   -4.850  1.00 49.90  ? 117 MET A CB    1 
ATOM   927  C  CG    . MET A 1 117 ? 39.293 1.923   -5.668  1.00 56.70  ? 117 MET A CG    1 
ATOM   928  S  SD    . MET A 1 117 ? 39.033 0.149   -5.478  1.00 59.85  ? 117 MET A SD    1 
ATOM   929  C  CE    . MET A 1 117 ? 39.360 -0.054  -3.729  1.00 59.37  ? 117 MET A CE    1 
ATOM   930  N  N     . SER A 1 118 ? 39.541 4.984   -7.086  1.00 51.33  ? 118 SER A N     1 
ATOM   931  C  CA    . SER A 1 118 ? 39.515 5.390   -8.481  1.00 61.41  ? 118 SER A CA    1 
ATOM   932  C  C     . SER A 1 118 ? 39.063 4.234   -9.368  1.00 60.90  ? 118 SER A C     1 
ATOM   933  O  O     . SER A 1 118 ? 39.061 3.065   -8.968  1.00 57.67  ? 118 SER A O     1 
ATOM   934  C  CB    . SER A 1 118 ? 40.891 5.881   -8.929  1.00 57.58  ? 118 SER A CB    1 
ATOM   935  O  OG    . SER A 1 118 ? 41.804 4.803   -9.023  1.00 63.43  ? 118 SER A OG    1 
ATOM   936  N  N     . GLU A 1 119 ? 38.670 4.581   -10.594 1.00 58.58  ? 119 GLU A N     1 
ATOM   937  C  CA    . GLU A 1 119 ? 38.255 3.564   -11.553 1.00 61.78  ? 119 GLU A CA    1 
ATOM   938  C  C     . GLU A 1 119 ? 39.426 2.688   -11.980 1.00 64.93  ? 119 GLU A C     1 
ATOM   939  O  O     . GLU A 1 119 ? 39.237 1.498   -12.256 1.00 68.41  ? 119 GLU A O     1 
ATOM   940  C  CB    . GLU A 1 119 ? 37.612 4.228   -12.768 1.00 68.71  ? 119 GLU A CB    1 
ATOM   941  C  CG    . GLU A 1 119 ? 36.525 5.227   -12.414 1.00 73.39  ? 119 GLU A CG    1 
ATOM   942  C  CD    . GLU A 1 119 ? 36.242 6.213   -13.531 1.00 87.35  ? 119 GLU A CD    1 
ATOM   943  O  OE1   . GLU A 1 119 ? 36.952 6.173   -14.561 1.00 95.60  ? 119 GLU A OE1   1 
ATOM   944  O  OE2   . GLU A 1 119 ? 35.310 7.031   -13.377 1.00 87.45  ? 119 GLU A OE2   1 
ATOM   945  N  N     . GLU A 1 120 ? 40.635 3.253   -12.036 1.00 68.26  ? 120 GLU A N     1 
ATOM   946  C  CA    . GLU A 1 120 ? 41.806 2.463   -12.405 1.00 71.07  ? 120 GLU A CA    1 
ATOM   947  C  C     . GLU A 1 120 ? 42.117 1.411   -11.348 1.00 65.47  ? 120 GLU A C     1 
ATOM   948  O  O     . GLU A 1 120 ? 42.399 0.253   -11.679 1.00 63.62  ? 120 GLU A O     1 
ATOM   949  C  CB    . GLU A 1 120 ? 43.016 3.374   -12.621 1.00 67.48  ? 120 GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 120 ? 42.855 4.398   -13.735 1.00 77.28  ? 120 GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 120 ? 42.157 5.667   -13.279 1.00 79.34  ? 120 GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 120 ? 41.741 5.733   -12.104 1.00 70.56  ? 120 GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 120 ? 42.028 6.601   -14.097 1.00 83.82  ? 120 GLU A OE2   1 
ATOM   954  N  N     . ASP A 1 121 ? 42.070 1.795   -10.071 1.00 63.25  ? 121 ASP A N     1 
ATOM   955  C  CA    . ASP A 1 121 ? 42.364 0.842   -9.007  1.00 63.28  ? 121 ASP A CA    1 
ATOM   956  C  C     . ASP A 1 121 ? 41.294 -0.238  -8.919  1.00 57.91  ? 121 ASP A C     1 
ATOM   957  O  O     . ASP A 1 121 ? 41.604 -1.404  -8.650  1.00 58.22  ? 121 ASP A O     1 
ATOM   958  C  CB    . ASP A 1 121 ? 42.505 1.572   -7.672  1.00 62.55  ? 121 ASP A CB    1 
ATOM   959  C  CG    . ASP A 1 121 ? 43.590 2.630   -7.700  1.00 66.67  ? 121 ASP A CG    1 
ATOM   960  O  OD1   . ASP A 1 121 ? 44.518 2.509   -8.527  1.00 70.94  ? 121 ASP A OD1   1 
ATOM   961  O  OD2   . ASP A 1 121 ? 43.513 3.583   -6.897  1.00 69.52  ? 121 ASP A OD2   1 
ATOM   962  N  N     . PHE A 1 122 ? 40.029 0.126   -9.152  1.00 56.50  ? 122 PHE A N     1 
ATOM   963  C  CA    . PHE A 1 122 ? 38.955 -0.854  -9.035  1.00 55.91  ? 122 PHE A CA    1 
ATOM   964  C  C     . PHE A 1 122 ? 39.031 -1.904  -10.135 1.00 61.75  ? 122 PHE A C     1 
ATOM   965  O  O     . PHE A 1 122 ? 38.730 -3.080  -9.896  1.00 55.89  ? 122 PHE A O     1 
ATOM   966  C  CB    . PHE A 1 122 ? 37.593 -0.167  -9.059  1.00 54.91  ? 122 PHE A CB    1 
ATOM   967  C  CG    . PHE A 1 122 ? 36.448 -1.126  -9.183  1.00 51.94  ? 122 PHE A CG    1 
ATOM   968  C  CD1   . PHE A 1 122 ? 36.141 -1.991  -8.145  1.00 50.24  ? 122 PHE A CD1   1 
ATOM   969  C  CD2   . PHE A 1 122 ? 35.692 -1.179  -10.341 1.00 48.50  ? 122 PHE A CD2   1 
ATOM   970  C  CE1   . PHE A 1 122 ? 35.095 -2.884  -8.255  1.00 46.03  ? 122 PHE A CE1   1 
ATOM   971  C  CE2   . PHE A 1 122 ? 34.644 -2.069  -10.458 1.00 52.70  ? 122 PHE A CE2   1 
ATOM   972  C  CZ    . PHE A 1 122 ? 34.344 -2.923  -9.411  1.00 50.27  ? 122 PHE A CZ    1 
ATOM   973  N  N     . GLU A 1 123 ? 39.415 -1.500  -11.350 1.00 58.27  ? 123 GLU A N     1 
ATOM   974  C  CA    . GLU A 1 123 ? 39.540 -2.465  -12.438 1.00 60.57  ? 123 GLU A CA    1 
ATOM   975  C  C     . GLU A 1 123 ? 40.611 -3.502  -12.131 1.00 58.18  ? 123 GLU A C     1 
ATOM   976  O  O     . GLU A 1 123 ? 40.436 -4.691  -12.422 1.00 56.89  ? 123 GLU A O     1 
ATOM   977  C  CB    . GLU A 1 123 ? 39.844 -1.748  -13.753 1.00 65.06  ? 123 GLU A CB    1 
ATOM   978  C  CG    . GLU A 1 123 ? 38.659 -1.000  -14.333 1.00 70.53  ? 123 GLU A CG    1 
ATOM   979  C  CD    . GLU A 1 123 ? 38.919 -0.496  -15.739 1.00 88.84  ? 123 GLU A CD    1 
ATOM   980  O  OE1   . GLU A 1 123 ? 40.025 -0.742  -16.268 1.00 88.84  ? 123 GLU A OE1   1 
ATOM   981  O  OE2   . GLU A 1 123 ? 38.015 0.146   -16.316 1.00 96.90  ? 123 GLU A OE2   1 
ATOM   982  N  N     . LYS A 1 124 ? 41.726 -3.073  -11.535 1.00 59.71  ? 124 LYS A N     1 
ATOM   983  C  CA    . LYS A 1 124 ? 42.731 -4.028  -11.084 1.00 56.04  ? 124 LYS A CA    1 
ATOM   984  C  C     . LYS A 1 124 ? 42.172 -4.938  -9.996  1.00 57.25  ? 124 LYS A C     1 
ATOM   985  O  O     . LYS A 1 124 ? 42.422 -6.149  -10.002 1.00 57.43  ? 124 LYS A O     1 
ATOM   986  C  CB    . LYS A 1 124 ? 43.970 -3.285  -10.584 1.00 59.79  ? 124 LYS A CB    1 
ATOM   987  C  CG    . LYS A 1 124 ? 44.568 -2.313  -11.595 1.00 64.31  ? 124 LYS A CG    1 
ATOM   988  C  CD    . LYS A 1 124 ? 45.851 -1.683  -11.070 1.00 65.92  ? 124 LYS A CD    1 
ATOM   989  C  CE    . LYS A 1 124 ? 46.439 -0.701  -12.072 1.00 77.10  ? 124 LYS A CE    1 
ATOM   990  N  NZ    . LYS A 1 124 ? 45.523 0.442   -12.338 1.00 80.89  ? 124 LYS A NZ    1 
ATOM   991  N  N     . ALA A 1 125 ? 41.407 -4.375  -9.057  1.00 56.45  ? 125 ALA A N     1 
ATOM   992  C  CA    . ALA A 1 125 ? 40.833 -5.184  -7.989  1.00 55.38  ? 125 ALA A CA    1 
ATOM   993  C  C     . ALA A 1 125 ? 39.735 -6.098  -8.512  1.00 55.57  ? 125 ALA A C     1 
ATOM   994  O  O     . ALA A 1 125 ? 39.583 -7.227  -8.029  1.00 54.82  ? 125 ALA A O     1 
ATOM   995  C  CB    . ALA A 1 125 ? 40.294 -4.282  -6.879  1.00 49.17  ? 125 ALA A CB    1 
ATOM   996  N  N     . PHE A 1 126 ? 38.969 -5.630  -9.497  1.00 53.98  ? 126 PHE A N     1 
ATOM   997  C  CA    . PHE A 1 126 ? 37.901 -6.442  -10.067 1.00 51.39  ? 126 PHE A CA    1 
ATOM   998  C  C     . PHE A 1 126 ? 38.465 -7.639  -10.825 1.00 54.73  ? 126 PHE A C     1 
ATOM   999  O  O     . PHE A 1 126 ? 38.018 -8.776  -10.632 1.00 55.56  ? 126 PHE A O     1 
ATOM   1000 C  CB    . PHE A 1 126 ? 37.035 -5.580  -10.982 1.00 50.90  ? 126 PHE A CB    1 
ATOM   1001 C  CG    . PHE A 1 126 ? 35.904 -6.322  -11.624 1.00 53.44  ? 126 PHE A CG    1 
ATOM   1002 C  CD1   . PHE A 1 126 ? 34.723 -6.536  -10.938 1.00 48.46  ? 126 PHE A CD1   1 
ATOM   1003 C  CD2   . PHE A 1 126 ? 36.016 -6.795  -12.920 1.00 51.24  ? 126 PHE A CD2   1 
ATOM   1004 C  CE1   . PHE A 1 126 ? 33.676 -7.213  -11.529 1.00 48.33  ? 126 PHE A CE1   1 
ATOM   1005 C  CE2   . PHE A 1 126 ? 34.970 -7.475  -13.515 1.00 48.55  ? 126 PHE A CE2   1 
ATOM   1006 C  CZ    . PHE A 1 126 ? 33.799 -7.682  -12.819 1.00 43.74  ? 126 PHE A CZ    1 
ATOM   1007 N  N     . ASN A 1 127 ? 39.456 -7.404  -11.687 1.00 52.78  ? 127 ASN A N     1 
ATOM   1008 C  CA    . ASN A 1 127 ? 40.023 -8.481  -12.489 1.00 54.64  ? 127 ASN A CA    1 
ATOM   1009 C  C     . ASN A 1 127 ? 40.831 -9.474  -11.666 1.00 52.14  ? 127 ASN A C     1 
ATOM   1010 O  O     . ASN A 1 127 ? 41.210 -10.523 -12.196 1.00 52.82  ? 127 ASN A O     1 
ATOM   1011 C  CB    . ASN A 1 127 ? 40.903 -7.909  -13.601 1.00 55.40  ? 127 ASN A CB    1 
ATOM   1012 C  CG    . ASN A 1 127 ? 40.107 -7.144  -14.637 1.00 57.29  ? 127 ASN A CG    1 
ATOM   1013 O  OD1   . ASN A 1 127 ? 38.937 -7.442  -14.884 1.00 54.70  ? 127 ASN A OD1   1 
ATOM   1014 N  ND2   . ASN A 1 127 ? 40.739 -6.152  -15.252 1.00 59.15  ? 127 ASN A ND2   1 
ATOM   1015 N  N     . ALA A 1 128 ? 41.106 -9.180  -10.398 1.00 51.54  ? 128 ALA A N     1 
ATOM   1016 C  CA    . ALA A 1 128 ? 41.824 -10.101 -9.530  1.00 53.11  ? 128 ALA A CA    1 
ATOM   1017 C  C     . ALA A 1 128 ? 40.891 -10.957 -8.685  1.00 55.06  ? 128 ALA A C     1 
ATOM   1018 O  O     . ALA A 1 128 ? 41.362 -11.669 -7.793  1.00 55.25  ? 128 ALA A O     1 
ATOM   1019 C  CB    . ALA A 1 128 ? 42.790 -9.332  -8.625  1.00 48.32  ? 128 ALA A CB    1 
ATOM   1020 N  N     . ARG A 1 129 ? 39.583 -10.911 -8.946  1.00 53.17  ? 129 ARG A N     1 
ATOM   1021 C  CA    . ARG A 1 129 ? 38.616 -11.583 -8.087  1.00 47.09  ? 129 ARG A CA    1 
ATOM   1022 C  C     . ARG A 1 129 ? 37.601 -12.397 -8.882  1.00 49.76  ? 129 ARG A C     1 
ATOM   1023 O  O     . ARG A 1 129 ? 37.456 -13.605 -8.666  1.00 49.36  ? 129 ARG A O     1 
ATOM   1024 C  CB    . ARG A 1 129 ? 37.883 -10.558 -7.216  1.00 50.33  ? 129 ARG A CB    1 
ATOM   1025 C  CG    . ARG A 1 129 ? 38.728 -9.940  -6.113  1.00 47.23  ? 129 ARG A CG    1 
ATOM   1026 C  CD    . ARG A 1 129 ? 38.016 -8.755  -5.467  1.00 45.39  ? 129 ARG A CD    1 
ATOM   1027 N  NE    . ARG A 1 129 ? 38.638 -8.374  -4.205  1.00 50.66  ? 129 ARG A NE    1 
ATOM   1028 C  CZ    . ARG A 1 129 ? 39.738 -7.640  -4.102  1.00 52.48  ? 129 ARG A CZ    1 
ATOM   1029 N  NH1   . ARG A 1 129 ? 40.356 -7.169  -5.172  1.00 55.21  ? 129 ARG A NH1   1 
ATOM   1030 N  NH2   . ARG A 1 129 ? 40.233 -7.377  -2.896  1.00 51.74  ? 129 ARG A NH2   1 
ATOM   1031 N  N     . PHE A 1 130 ? 36.905 -11.747 -9.806  1.00 46.38  ? 130 PHE A N     1 
ATOM   1032 C  CA    . PHE A 1 130 ? 35.713 -12.316 -10.428 1.00 48.32  ? 130 PHE A CA    1 
ATOM   1033 C  C     . PHE A 1 130 ? 35.949 -13.318 -11.559 1.00 50.76  ? 130 PHE A C     1 
ATOM   1034 O  O     . PHE A 1 130 ? 35.105 -14.202 -11.750 1.00 50.64  ? 130 PHE A O     1 
ATOM   1035 C  CB    . PHE A 1 130 ? 34.816 -11.182 -10.927 1.00 45.29  ? 130 PHE A CB    1 
ATOM   1036 C  CG    . PHE A 1 130 ? 33.985 -10.561 -9.843  1.00 53.84  ? 130 PHE A CG    1 
ATOM   1037 C  CD1   . PHE A 1 130 ? 34.495 -9.539  -9.058  1.00 48.00  ? 130 PHE A CD1   1 
ATOM   1038 C  CD2   . PHE A 1 130 ? 32.702 -11.019 -9.590  1.00 46.93  ? 130 PHE A CD2   1 
ATOM   1039 C  CE1   . PHE A 1 130 ? 33.738 -8.981  -8.051  1.00 47.48  ? 130 PHE A CE1   1 
ATOM   1040 C  CE2   . PHE A 1 130 ? 31.938 -10.461 -8.586  1.00 43.88  ? 130 PHE A CE2   1 
ATOM   1041 C  CZ    . PHE A 1 130 ? 32.456 -9.442  -7.815  1.00 44.85  ? 130 PHE A CZ    1 
ATOM   1042 N  N     . PRO A 1 131 ? 37.038 -13.219 -12.361 1.00 53.60  ? 131 PRO A N     1 
ATOM   1043 C  CA    . PRO A 1 131 ? 37.256 -14.236 -13.404 1.00 54.23  ? 131 PRO A CA    1 
ATOM   1044 C  C     . PRO A 1 131 ? 37.269 -15.669 -12.885 1.00 51.63  ? 131 PRO A C     1 
ATOM   1045 O  O     . PRO A 1 131 ? 38.150 -16.061 -12.111 1.00 48.78  ? 131 PRO A O     1 
ATOM   1046 C  CB    . PRO A 1 131 ? 38.615 -13.840 -13.990 1.00 50.81  ? 131 PRO A CB    1 
ATOM   1047 C  CG    . PRO A 1 131 ? 38.629 -12.367 -13.856 1.00 55.74  ? 131 PRO A CG    1 
ATOM   1048 C  CD    . PRO A 1 131 ? 37.938 -12.065 -12.551 1.00 45.93  ? 131 PRO A CD    1 
ATOM   1049 N  N     . GLY A 1 132 ? 36.284 -16.458 -13.315 1.00 52.23  ? 132 GLY A N     1 
ATOM   1050 C  CA    . GLY A 1 132 ? 36.172 -17.839 -12.892 1.00 47.78  ? 132 GLY A CA    1 
ATOM   1051 C  C     . GLY A 1 132 ? 35.780 -18.037 -11.446 1.00 50.50  ? 132 GLY A C     1 
ATOM   1052 O  O     . GLY A 1 132 ? 36.020 -19.115 -10.895 1.00 53.34  ? 132 GLY A O     1 
ATOM   1053 N  N     . CYS A 1 133 ? 35.171 -17.031 -10.813 1.00 45.69  ? 133 CYS A N     1 
ATOM   1054 C  CA    . CYS A 1 133 ? 34.880 -17.109 -9.386  1.00 51.94  ? 133 CYS A CA    1 
ATOM   1055 C  C     . CYS A 1 133 ? 33.690 -18.008 -9.067  1.00 49.06  ? 133 CYS A C     1 
ATOM   1056 O  O     . CYS A 1 133 ? 33.601 -18.513 -7.944  1.00 52.36  ? 133 CYS A O     1 
ATOM   1057 C  CB    . CYS A 1 133 ? 34.633 -15.708 -8.819  1.00 44.98  ? 133 CYS A CB    1 
ATOM   1058 S  SG    . CYS A 1 133 ? 33.106 -14.924 -9.381  1.00 44.87  ? 133 CYS A SG    1 
ATOM   1059 N  N     . MET A 1 134 ? 32.780 -18.222 -10.019 1.00 43.68  ? 134 MET A N     1 
ATOM   1060 C  CA    . MET A 1 134 ? 31.624 -19.087 -9.825  1.00 48.81  ? 134 MET A CA    1 
ATOM   1061 C  C     . MET A 1 134 ? 31.819 -20.468 -10.443 1.00 55.08  ? 134 MET A C     1 
ATOM   1062 O  O     . MET A 1 134 ? 30.837 -21.132 -10.793 1.00 56.47  ? 134 MET A O     1 
ATOM   1063 C  CB    . MET A 1 134 ? 30.367 -18.435 -10.398 1.00 45.70  ? 134 MET A CB    1 
ATOM   1064 C  CG    . MET A 1 134 ? 29.991 -17.124 -9.748  1.00 44.36  ? 134 MET A CG    1 
ATOM   1065 S  SD    . MET A 1 134 ? 28.383 -16.531 -10.303 1.00 40.87  ? 134 MET A SD    1 
ATOM   1066 C  CE    . MET A 1 134 ? 28.328 -14.943 -9.475  1.00 41.77  ? 134 MET A CE    1 
ATOM   1067 N  N     . LYS A 1 135 ? 33.066 -20.911 -10.587 1.00 55.90  ? 135 LYS A N     1 
ATOM   1068 C  CA    . LYS A 1 135 ? 33.343 -22.193 -11.224 1.00 57.54  ? 135 LYS A CA    1 
ATOM   1069 C  C     . LYS A 1 135 ? 32.703 -23.326 -10.431 1.00 59.84  ? 135 LYS A C     1 
ATOM   1070 O  O     . LYS A 1 135 ? 32.979 -23.496 -9.239  1.00 62.26  ? 135 LYS A O     1 
ATOM   1071 C  CB    . LYS A 1 135 ? 34.852 -22.404 -11.338 1.00 56.69  ? 135 LYS A CB    1 
ATOM   1072 C  CG    . LYS A 1 135 ? 35.280 -23.258 -12.522 1.00 62.70  ? 135 LYS A CG    1 
ATOM   1073 C  CD    . LYS A 1 135 ? 34.929 -22.580 -13.840 1.00 63.48  ? 135 LYS A CD    1 
ATOM   1074 C  CE    . LYS A 1 135 ? 35.619 -23.245 -15.026 1.00 66.23  ? 135 LYS A CE    1 
ATOM   1075 N  NZ    . LYS A 1 135 ? 35.237 -24.677 -15.196 1.00 75.95  ? 135 LYS A NZ    1 
ATOM   1076 N  N     . GLY A 1 136 ? 31.837 -24.092 -11.092 1.00 58.27  ? 136 GLY A N     1 
ATOM   1077 C  CA    . GLY A 1 136 ? 31.163 -25.205 -10.463 1.00 54.99  ? 136 GLY A CA    1 
ATOM   1078 C  C     . GLY A 1 136 ? 29.936 -24.851 -9.653  1.00 56.26  ? 136 GLY A C     1 
ATOM   1079 O  O     . GLY A 1 136 ? 29.317 -25.756 -9.077  1.00 51.87  ? 136 GLY A O     1 
ATOM   1080 N  N     . ARG A 1 137 ? 29.564 -23.576 -9.584  1.00 53.59  ? 137 ARG A N     1 
ATOM   1081 C  CA    . ARG A 1 137 ? 28.406 -23.124 -8.827  1.00 47.52  ? 137 ARG A CA    1 
ATOM   1082 C  C     . ARG A 1 137 ? 27.291 -22.687 -9.769  1.00 47.21  ? 137 ARG A C     1 
ATOM   1083 O  O     . ARG A 1 137 ? 27.476 -22.554 -10.981 1.00 54.05  ? 137 ARG A O     1 
ATOM   1084 C  CB    . ARG A 1 137 ? 28.781 -21.973 -7.888  1.00 44.09  ? 137 ARG A CB    1 
ATOM   1085 C  CG    . ARG A 1 137 ? 29.911 -22.296 -6.928  1.00 49.56  ? 137 ARG A CG    1 
ATOM   1086 C  CD    . ARG A 1 137 ? 30.019 -21.242 -5.840  1.00 48.64  ? 137 ARG A CD    1 
ATOM   1087 N  NE    . ARG A 1 137 ? 31.081 -21.546 -4.888  1.00 53.40  ? 137 ARG A NE    1 
ATOM   1088 C  CZ    . ARG A 1 137 ? 30.945 -22.364 -3.853  1.00 50.47  ? 137 ARG A CZ    1 
ATOM   1089 N  NH1   . ARG A 1 137 ? 29.807 -22.996 -3.616  1.00 43.86  ? 137 ARG A NH1   1 
ATOM   1090 N  NH2   . ARG A 1 137 ? 31.978 -22.554 -3.037  1.00 49.01  ? 137 ARG A NH2   1 
ATOM   1091 N  N     . THR A 1 138 ? 26.118 -22.463 -9.187  1.00 39.90  ? 138 THR A N     1 
ATOM   1092 C  CA    . THR A 1 138 ? 24.955 -21.959 -9.907  1.00 46.02  ? 138 THR A CA    1 
ATOM   1093 C  C     . THR A 1 138 ? 24.886 -20.446 -9.752  1.00 41.59  ? 138 THR A C     1 
ATOM   1094 O  O     . THR A 1 138 ? 24.985 -19.932 -8.634  1.00 45.10  ? 138 THR A O     1 
ATOM   1095 C  CB    . THR A 1 138 ? 23.667 -22.595 -9.376  1.00 41.20  ? 138 THR A CB    1 
ATOM   1096 O  OG1   . THR A 1 138 ? 23.687 -24.005 -9.620  1.00 47.91  ? 138 THR A OG1   1 
ATOM   1097 C  CG2   . THR A 1 138 ? 22.450 -21.984 -10.048 1.00 43.90  ? 138 THR A CG2   1 
ATOM   1098 N  N     . MET A 1 139 ? 24.726 -19.734 -10.868 1.00 37.88  ? 139 MET A N     1 
ATOM   1099 C  CA    . MET A 1 139 ? 24.478 -18.294 -10.834 1.00 39.31  ? 139 MET A CA    1 
ATOM   1100 C  C     . MET A 1 139 ? 22.972 -18.068 -10.795 1.00 36.81  ? 139 MET A C     1 
ATOM   1101 O  O     . MET A 1 139 ? 22.263 -18.387 -11.756 1.00 38.35  ? 139 MET A O     1 
ATOM   1102 C  CB    . MET A 1 139 ? 25.101 -17.586 -12.036 1.00 44.64  ? 139 MET A CB    1 
ATOM   1103 C  CG    . MET A 1 139 ? 24.694 -16.113 -12.155 1.00 35.10  ? 139 MET A CG    1 
ATOM   1104 S  SD    . MET A 1 139 ? 25.268 -15.281 -13.658 1.00 39.83  ? 139 MET A SD    1 
ATOM   1105 C  CE    . MET A 1 139 ? 27.031 -15.182 -13.355 1.00 37.44  ? 139 MET A CE    1 
ATOM   1106 N  N     . TYR A 1 140 ? 22.487 -17.516 -9.687  1.00 39.38  ? 140 TYR A N     1 
ATOM   1107 C  CA    . TYR A 1 140 ? 21.075 -17.192 -9.534  1.00 36.53  ? 140 TYR A CA    1 
ATOM   1108 C  C     . TYR A 1 140 ? 20.812 -15.783 -10.051 1.00 39.63  ? 140 TYR A C     1 
ATOM   1109 O  O     . TYR A 1 140 ? 21.572 -14.855 -9.756  1.00 36.34  ? 140 TYR A O     1 
ATOM   1110 C  CB    . TYR A 1 140 ? 20.648 -17.310 -8.069  1.00 36.90  ? 140 TYR A CB    1 
ATOM   1111 C  CG    . TYR A 1 140 ? 20.764 -18.713 -7.518  1.00 35.96  ? 140 TYR A CG    1 
ATOM   1112 C  CD1   . TYR A 1 140 ? 19.747 -19.639 -7.712  1.00 36.19  ? 140 TYR A CD1   1 
ATOM   1113 C  CD2   . TYR A 1 140 ? 21.892 -19.116 -6.813  1.00 31.98  ? 140 TYR A CD2   1 
ATOM   1114 C  CE1   . TYR A 1 140 ? 19.847 -20.927 -7.219  1.00 39.17  ? 140 TYR A CE1   1 
ATOM   1115 C  CE2   . TYR A 1 140 ? 22.001 -20.403 -6.312  1.00 33.34  ? 140 TYR A CE2   1 
ATOM   1116 C  CZ    . TYR A 1 140 ? 20.973 -21.304 -6.519  1.00 35.51  ? 140 TYR A CZ    1 
ATOM   1117 O  OH    . TYR A 1 140 ? 21.069 -22.589 -6.031  1.00 41.62  ? 140 TYR A OH    1 
ATOM   1118 N  N     . VAL A 1 141 ? 19.743 -15.634 -10.826 1.00 37.28  ? 141 VAL A N     1 
ATOM   1119 C  CA    . VAL A 1 141 ? 19.314 -14.343 -11.350 1.00 33.97  ? 141 VAL A CA    1 
ATOM   1120 C  C     . VAL A 1 141 ? 18.127 -13.889 -10.514 1.00 38.43  ? 141 VAL A C     1 
ATOM   1121 O  O     . VAL A 1 141 ? 17.053 -14.498 -10.566 1.00 39.43  ? 141 VAL A O     1 
ATOM   1122 C  CB    . VAL A 1 141 ? 18.950 -14.426 -12.838 1.00 37.09  ? 141 VAL A CB    1 
ATOM   1123 C  CG1   . VAL A 1 141 ? 18.548 -13.049 -13.363 1.00 31.48  ? 141 VAL A CG1   1 
ATOM   1124 C  CG2   . VAL A 1 141 ? 20.112 -14.988 -13.634 1.00 35.75  ? 141 VAL A CG2   1 
ATOM   1125 N  N     . ILE A 1 142 ? 18.313 -12.814 -9.752  1.00 40.16  ? 142 ILE A N     1 
ATOM   1126 C  CA    . ILE A 1 142 ? 17.307 -12.331 -8.807  1.00 35.88  ? 142 ILE A CA    1 
ATOM   1127 C  C     . ILE A 1 142 ? 16.691 -11.029 -9.309  1.00 38.01  ? 142 ILE A C     1 
ATOM   1128 O  O     . ILE A 1 142 ? 17.314 -9.963  -9.193  1.00 37.24  ? 142 ILE A O     1 
ATOM   1129 C  CB    . ILE A 1 142 ? 17.914 -12.128 -7.409  1.00 33.46  ? 142 ILE A CB    1 
ATOM   1130 C  CG1   . ILE A 1 142 ? 18.478 -13.435 -6.862  1.00 33.30  ? 142 ILE A CG1   1 
ATOM   1131 C  CG2   . ILE A 1 142 ? 16.878 -11.569 -6.451  1.00 41.87  ? 142 ILE A CG2   1 
ATOM   1132 C  CD1   . ILE A 1 142 ? 19.133 -13.280 -5.514  1.00 29.20  ? 142 ILE A CD1   1 
ATOM   1133 N  N     . PRO A 1 143 ? 15.485 -11.060 -9.873  1.00 39.62  ? 143 PRO A N     1 
ATOM   1134 C  CA    . PRO A 1 143 ? 14.783 -9.807  -10.174 1.00 42.82  ? 143 PRO A CA    1 
ATOM   1135 C  C     . PRO A 1 143 ? 14.000 -9.314  -8.967  1.00 42.12  ? 143 PRO A C     1 
ATOM   1136 O  O     . PRO A 1 143 ? 13.129 -10.026 -8.459  1.00 42.14  ? 143 PRO A O     1 
ATOM   1137 C  CB    . PRO A 1 143 ? 13.861 -10.200 -11.333 1.00 42.48  ? 143 PRO A CB    1 
ATOM   1138 C  CG    . PRO A 1 143 ? 13.556 -11.644 -11.075 1.00 37.69  ? 143 PRO A CG    1 
ATOM   1139 C  CD    . PRO A 1 143 ? 14.758 -12.238 -10.376 1.00 39.14  ? 143 PRO A CD    1 
ATOM   1140 N  N     . PHE A 1 144 ? 14.299 -8.109  -8.485  1.00 39.58  ? 144 PHE A N     1 
ATOM   1141 C  CA    . PHE A 1 144 ? 13.664 -7.605  -7.278  1.00 43.91  ? 144 PHE A CA    1 
ATOM   1142 C  C     . PHE A 1 144 ? 13.341 -6.126  -7.429  1.00 46.56  ? 144 PHE A C     1 
ATOM   1143 O  O     . PHE A 1 144 ? 14.044 -5.381  -8.116  1.00 42.48  ? 144 PHE A O     1 
ATOM   1144 C  CB    . PHE A 1 144 ? 14.542 -7.826  -6.041  1.00 42.67  ? 144 PHE A CB    1 
ATOM   1145 C  CG    . PHE A 1 144 ? 15.821 -7.039  -6.054  1.00 41.86  ? 144 PHE A CG    1 
ATOM   1146 C  CD1   . PHE A 1 144 ? 16.916 -7.483  -6.775  1.00 42.33  ? 144 PHE A CD1   1 
ATOM   1147 C  CD2   . PHE A 1 144 ? 15.934 -5.861  -5.331  1.00 42.38  ? 144 PHE A CD2   1 
ATOM   1148 C  CE1   . PHE A 1 144 ? 18.097 -6.768  -6.782  1.00 36.27  ? 144 PHE A CE1   1 
ATOM   1149 C  CE2   . PHE A 1 144 ? 17.115 -5.141  -5.334  1.00 40.70  ? 144 PHE A CE2   1 
ATOM   1150 C  CZ    . PHE A 1 144 ? 18.196 -5.597  -6.059  1.00 35.42  ? 144 PHE A CZ    1 
ATOM   1151 N  N     . SER A 1 145 ? 12.263 -5.713  -6.771  1.00 49.58  ? 145 SER A N     1 
ATOM   1152 C  CA    . SER A 1 145 ? 11.801 -4.333  -6.782  1.00 53.71  ? 145 SER A CA    1 
ATOM   1153 C  C     . SER A 1 145 ? 11.872 -3.773  -5.369  1.00 53.00  ? 145 SER A C     1 
ATOM   1154 O  O     . SER A 1 145 ? 11.320 -4.364  -4.434  1.00 51.09  ? 145 SER A O     1 
ATOM   1155 C  CB    . SER A 1 145 ? 10.370 -4.239  -7.324  1.00 55.52  ? 145 SER A CB    1 
ATOM   1156 O  OG    . SER A 1 145 ? 9.843  -2.932  -7.178  1.00 55.75  ? 145 SER A OG    1 
ATOM   1157 N  N     . MET A 1 146 ? 12.560 -2.644  -5.215  1.00 51.86  ? 146 MET A N     1 
ATOM   1158 C  CA    . MET A 1 146 ? 12.608 -1.928  -3.945  1.00 51.78  ? 146 MET A CA    1 
ATOM   1159 C  C     . MET A 1 146 ? 11.396 -1.009  -3.885  1.00 49.80  ? 146 MET A C     1 
ATOM   1160 O  O     . MET A 1 146 ? 11.279 -0.075  -4.683  1.00 45.94  ? 146 MET A O     1 
ATOM   1161 C  CB    . MET A 1 146 ? 13.908 -1.142  -3.808  1.00 47.93  ? 146 MET A CB    1 
ATOM   1162 C  CG    . MET A 1 146 ? 15.156 -2.003  -3.848  1.00 40.85  ? 146 MET A CG    1 
ATOM   1163 S  SD    . MET A 1 146 ? 15.187 -3.256  -2.553  1.00 33.63  ? 146 MET A SD    1 
ATOM   1164 C  CE    . MET A 1 146 ? 14.983 -2.243  -1.089  1.00 39.16  ? 146 MET A CE    1 
ATOM   1165 N  N     . GLY A 1 147 ? 10.491 -1.279  -2.949  1.00 54.26  ? 147 GLY A N     1 
ATOM   1166 C  CA    . GLY A 1 147 ? 9.227  -0.588  -2.891  1.00 58.67  ? 147 GLY A CA    1 
ATOM   1167 C  C     . GLY A 1 147 ? 8.127  -1.415  -3.525  1.00 62.84  ? 147 GLY A C     1 
ATOM   1168 O  O     . GLY A 1 147 ? 8.380  -2.464  -4.123  1.00 61.39  ? 147 GLY A O     1 
ATOM   1169 N  N     . PRO A 1 148 ? 6.879  -0.960  -3.401  1.00 79.87  ? 148 PRO A N     1 
ATOM   1170 C  CA    . PRO A 1 148 ? 5.756  -1.730  -3.952  1.00 80.28  ? 148 PRO A CA    1 
ATOM   1171 C  C     . PRO A 1 148 ? 5.885  -1.921  -5.456  1.00 83.16  ? 148 PRO A C     1 
ATOM   1172 O  O     . PRO A 1 148 ? 6.240  -0.998  -6.192  1.00 85.32  ? 148 PRO A O     1 
ATOM   1173 C  CB    . PRO A 1 148 ? 4.534  -0.876  -3.596  1.00 77.57  ? 148 PRO A CB    1 
ATOM   1174 C  CG    . PRO A 1 148 ? 4.974  -0.061  -2.423  1.00 78.19  ? 148 PRO A CG    1 
ATOM   1175 C  CD    . PRO A 1 148 ? 6.426  0.227   -2.658  1.00 75.16  ? 148 PRO A CD    1 
ATOM   1176 N  N     . LEU A 1 149 ? 5.596  -3.139  -5.906  1.00 77.72  ? 149 LEU A N     1 
ATOM   1177 C  CA    . LEU A 1 149 ? 5.705  -3.463  -7.321  1.00 82.15  ? 149 LEU A CA    1 
ATOM   1178 C  C     . LEU A 1 149 ? 4.687  -2.669  -8.128  1.00 86.22  ? 149 LEU A C     1 
ATOM   1179 O  O     . LEU A 1 149 ? 3.547  -2.469  -7.699  1.00 91.09  ? 149 LEU A O     1 
ATOM   1180 C  CB    . LEU A 1 149 ? 5.502  -4.965  -7.536  1.00 85.20  ? 149 LEU A CB    1 
ATOM   1181 C  CG    . LEU A 1 149 ? 5.664  -5.529  -8.951  1.00 79.29  ? 149 LEU A CG    1 
ATOM   1182 C  CD1   . LEU A 1 149 ? 6.350  -6.880  -8.893  1.00 74.14  ? 149 LEU A CD1   1 
ATOM   1183 C  CD2   . LEU A 1 149 ? 4.320  -5.654  -9.655  1.00 80.60  ? 149 LEU A CD2   1 
ATOM   1184 N  N     . GLY A 1 150 ? 5.108  -2.214  -9.308  1.00 85.84  ? 150 GLY A N     1 
ATOM   1185 C  CA    . GLY A 1 150 ? 4.274  -1.387  -10.151 1.00 88.24  ? 150 GLY A CA    1 
ATOM   1186 C  C     . GLY A 1 150 ? 4.195  0.067   -9.744  1.00 93.46  ? 150 GLY A C     1 
ATOM   1187 O  O     . GLY A 1 150 ? 3.742  0.892   -10.548 1.00 93.18  ? 150 GLY A O     1 
ATOM   1188 N  N     . SER A 1 151 ? 4.611  0.409   -8.531  1.00 92.38  ? 151 SER A N     1 
ATOM   1189 C  CA    . SER A 1 151 ? 4.599  1.800   -8.100  1.00 95.20  ? 151 SER A CA    1 
ATOM   1190 C  C     . SER A 1 151 ? 5.609  2.599   -8.914  1.00 102.06 ? 151 SER A C     1 
ATOM   1191 O  O     . SER A 1 151 ? 6.772  2.190   -9.022  1.00 95.81  ? 151 SER A O     1 
ATOM   1192 C  CB    . SER A 1 151 ? 4.921  1.901   -6.612  1.00 88.61  ? 151 SER A CB    1 
ATOM   1193 O  OG    . SER A 1 151 ? 5.081  3.252   -6.218  1.00 94.26  ? 151 SER A OG    1 
ATOM   1194 N  N     . PRO A 1 152 ? 5.212  3.731   -9.503  1.00 110.84 ? 152 PRO A N     1 
ATOM   1195 C  CA    . PRO A 1 152 ? 6.171  4.528   -10.287 1.00 109.64 ? 152 PRO A CA    1 
ATOM   1196 C  C     . PRO A 1 152 ? 7.321  5.081   -9.463  1.00 109.50 ? 152 PRO A C     1 
ATOM   1197 O  O     . PRO A 1 152 ? 8.326  5.512   -10.041 1.00 110.59 ? 152 PRO A O     1 
ATOM   1198 C  CB    . PRO A 1 152 ? 5.303  5.657   -10.862 1.00 110.93 ? 152 PRO A CB    1 
ATOM   1199 C  CG    . PRO A 1 152 ? 3.898  5.138   -10.797 1.00 109.28 ? 152 PRO A CG    1 
ATOM   1200 C  CD    . PRO A 1 152 ? 3.848  4.278   -9.572  1.00 107.05 ? 152 PRO A CD    1 
ATOM   1201 N  N     . LEU A 1 153 ? 7.209  5.081   -8.136  1.00 107.18 ? 153 LEU A N     1 
ATOM   1202 C  CA    . LEU A 1 153 ? 8.256  5.573   -7.254  1.00 94.87  ? 153 LEU A CA    1 
ATOM   1203 C  C     . LEU A 1 153 ? 9.156  4.456   -6.741  1.00 94.33  ? 153 LEU A C     1 
ATOM   1204 O  O     . LEU A 1 153 ? 9.913  4.668   -5.788  1.00 88.81  ? 153 LEU A O     1 
ATOM   1205 C  CB    . LEU A 1 153 ? 7.627  6.330   -6.086  1.00 88.94  ? 153 LEU A CB    1 
ATOM   1206 C  CG    . LEU A 1 153 ? 6.547  7.313   -6.546  1.00 95.61  ? 153 LEU A CG    1 
ATOM   1207 C  CD1   . LEU A 1 153 ? 5.639  7.710   -5.399  1.00 96.61  ? 153 LEU A CD1   1 
ATOM   1208 C  CD2   . LEU A 1 153 ? 7.177  8.543   -7.184  1.00 96.72  ? 153 LEU A CD2   1 
ATOM   1209 N  N     . ALA A 1 154 ? 9.091  3.277   -7.352  1.00 84.00  ? 154 ALA A N     1 
ATOM   1210 C  CA    . ALA A 1 154 ? 9.911  2.138   -6.977  1.00 72.04  ? 154 ALA A CA    1 
ATOM   1211 C  C     . ALA A 1 154 ? 10.966 1.881   -8.044  1.00 67.55  ? 154 ALA A C     1 
ATOM   1212 O  O     . ALA A 1 154 ? 10.747 2.132   -9.233  1.00 67.47  ? 154 ALA A O     1 
ATOM   1213 C  CB    . ALA A 1 154 ? 9.054  0.885   -6.781  1.00 70.25  ? 154 ALA A CB    1 
ATOM   1214 N  N     . LYS A 1 155 ? 12.114 1.370   -7.610  1.00 53.87  ? 155 LYS A N     1 
ATOM   1215 C  CA    . LYS A 1 155 ? 13.232 1.083   -8.495  1.00 53.01  ? 155 LYS A CA    1 
ATOM   1216 C  C     . LYS A 1 155 ? 13.524 -0.412  -8.496  1.00 50.71  ? 155 LYS A C     1 
ATOM   1217 O  O     . LYS A 1 155 ? 13.466 -1.071  -7.451  1.00 46.68  ? 155 LYS A O     1 
ATOM   1218 C  CB    . LYS A 1 155 ? 14.470 1.874   -8.077  1.00 52.93  ? 155 LYS A CB    1 
ATOM   1219 C  CG    . LYS A 1 155 ? 14.140 3.274   -7.593  1.00 53.84  ? 155 LYS A CG    1 
ATOM   1220 C  CD    . LYS A 1 155 ? 15.319 4.210   -7.737  1.00 56.58  ? 155 LYS A CD    1 
ATOM   1221 C  CE    . LYS A 1 155 ? 15.362 4.822   -9.127  1.00 67.15  ? 155 LYS A CE    1 
ATOM   1222 N  NZ    . LYS A 1 155 ? 14.175 5.688   -9.384  1.00 62.15  ? 155 LYS A NZ    1 
ATOM   1223 N  N     . ILE A 1 156 ? 13.844 -0.940  -9.675  1.00 51.67  ? 156 ILE A N     1 
ATOM   1224 C  CA    . ILE A 1 156 ? 13.972 -2.375  -9.905  1.00 46.36  ? 156 ILE A CA    1 
ATOM   1225 C  C     . ILE A 1 156 ? 15.447 -2.738  -10.019 1.00 44.89  ? 156 ILE A C     1 
ATOM   1226 O  O     . ILE A 1 156 ? 16.229 -2.016  -10.648 1.00 46.83  ? 156 ILE A O     1 
ATOM   1227 C  CB    . ILE A 1 156 ? 13.191 -2.791  -11.167 1.00 42.64  ? 156 ILE A CB    1 
ATOM   1228 C  CG1   . ILE A 1 156 ? 11.687 -2.642  -10.922 1.00 44.95  ? 156 ILE A CG1   1 
ATOM   1229 C  CG2   . ILE A 1 156 ? 13.542 -4.208  -11.589 1.00 45.94  ? 156 ILE A CG2   1 
ATOM   1230 C  CD1   . ILE A 1 156 ? 10.826 -3.013  -12.108 1.00 50.18  ? 156 ILE A CD1   1 
ATOM   1231 N  N     . GLY A 1 157 ? 15.828 -3.859  -9.402  1.00 43.27  ? 157 GLY A N     1 
ATOM   1232 C  CA    . GLY A 1 157 ? 17.195 -4.324  -9.453  1.00 42.55  ? 157 GLY A CA    1 
ATOM   1233 C  C     . GLY A 1 157 ? 17.289 -5.758  -9.934  1.00 39.46  ? 157 GLY A C     1 
ATOM   1234 O  O     . GLY A 1 157 ? 16.336 -6.534  -9.857  1.00 37.65  ? 157 GLY A O     1 
ATOM   1235 N  N     . ILE A 1 158 ? 18.473 -6.099  -10.439 1.00 40.66  ? 158 ILE A N     1 
ATOM   1236 C  CA    . ILE A 1 158 ? 18.812 -7.455  -10.866 1.00 36.03  ? 158 ILE A CA    1 
ATOM   1237 C  C     . ILE A 1 158 ? 20.092 -7.840  -10.138 1.00 37.03  ? 158 ILE A C     1 
ATOM   1238 O  O     . ILE A 1 158 ? 21.145 -7.235  -10.375 1.00 34.74  ? 158 ILE A O     1 
ATOM   1239 C  CB    . ILE A 1 158 ? 19.006 -7.563  -12.386 1.00 35.11  ? 158 ILE A CB    1 
ATOM   1240 C  CG1   . ILE A 1 158 ? 17.715 -7.226  -13.131 1.00 35.06  ? 158 ILE A CG1   1 
ATOM   1241 C  CG2   . ILE A 1 158 ? 19.479 -8.960  -12.764 1.00 39.44  ? 158 ILE A CG2   1 
ATOM   1242 C  CD1   . ILE A 1 158 ? 16.624 -8.240  -12.924 1.00 43.52  ? 158 ILE A CD1   1 
ATOM   1243 N  N     . GLU A 1 159 ? 20.012 -8.837  -9.258  1.00 35.44  ? 159 GLU A N     1 
ATOM   1244 C  CA    . GLU A 1 159 ? 21.186 -9.334  -8.553  1.00 32.81  ? 159 GLU A CA    1 
ATOM   1245 C  C     . GLU A 1 159 ? 21.590 -10.696 -9.100  1.00 36.62  ? 159 GLU A C     1 
ATOM   1246 O  O     . GLU A 1 159 ? 20.736 -11.557 -9.337  1.00 32.77  ? 159 GLU A O     1 
ATOM   1247 C  CB    . GLU A 1 159 ? 20.948 -9.430  -7.045  1.00 31.28  ? 159 GLU A CB    1 
ATOM   1248 C  CG    . GLU A 1 159 ? 22.115 -10.094 -6.322  1.00 33.54  ? 159 GLU A CG    1 
ATOM   1249 C  CD    . GLU A 1 159 ? 22.195 -9.754  -4.849  1.00 38.04  ? 159 GLU A CD    1 
ATOM   1250 O  OE1   . GLU A 1 159 ? 21.306 -9.038  -4.349  1.00 37.78  ? 159 GLU A OE1   1 
ATOM   1251 O  OE2   . GLU A 1 159 ? 23.158 -10.208 -4.194  1.00 34.34  ? 159 GLU A OE2   1 
ATOM   1252 N  N     . LEU A 1 160 ? 22.893 -10.879 -9.305  1.00 33.20  ? 160 LEU A N     1 
ATOM   1253 C  CA    . LEU A 1 160 ? 23.480 -12.155 -9.684  1.00 33.71  ? 160 LEU A CA    1 
ATOM   1254 C  C     . LEU A 1 160 ? 24.331 -12.640 -8.519  1.00 36.61  ? 160 LEU A C     1 
ATOM   1255 O  O     . LEU A 1 160 ? 25.219 -11.919 -8.051  1.00 36.83  ? 160 LEU A O     1 
ATOM   1256 C  CB    . LEU A 1 160 ? 24.325 -12.020 -10.952 1.00 31.94  ? 160 LEU A CB    1 
ATOM   1257 C  CG    . LEU A 1 160 ? 23.665 -11.335 -12.147 1.00 36.21  ? 160 LEU A CG    1 
ATOM   1258 C  CD1   . LEU A 1 160 ? 24.593 -11.331 -13.357 1.00 35.03  ? 160 LEU A CD1   1 
ATOM   1259 C  CD2   . LEU A 1 160 ? 22.334 -11.996 -12.486 1.00 36.32  ? 160 LEU A CD2   1 
ATOM   1260 N  N     . THR A 1 161 ? 24.059 -13.852 -8.051  1.00 34.52  ? 161 THR A N     1 
ATOM   1261 C  CA    . THR A 1 161 ? 24.765 -14.391 -6.902  1.00 35.58  ? 161 THR A CA    1 
ATOM   1262 C  C     . THR A 1 161 ? 24.933 -15.891 -7.084  1.00 33.14  ? 161 THR A C     1 
ATOM   1263 O  O     . THR A 1 161 ? 24.149 -16.540 -7.782  1.00 35.03  ? 161 THR A O     1 
ATOM   1264 C  CB    . THR A 1 161 ? 24.020 -14.081 -5.593  1.00 34.02  ? 161 THR A CB    1 
ATOM   1265 O  OG1   . THR A 1 161 ? 24.737 -14.633 -4.481  1.00 33.30  ? 161 THR A OG1   1 
ATOM   1266 C  CG2   . THR A 1 161 ? 22.609 -14.655 -5.624  1.00 31.44  ? 161 THR A CG2   1 
ATOM   1267 N  N     . ASP A 1 162 ? 25.982 -16.433 -6.468  1.00 30.49  ? 162 ASP A N     1 
ATOM   1268 C  CA    . ASP A 1 162 ? 26.188 -17.872 -6.404  1.00 36.51  ? 162 ASP A CA    1 
ATOM   1269 C  C     . ASP A 1 162 ? 25.867 -18.428 -5.022  1.00 36.69  ? 162 ASP A C     1 
ATOM   1270 O  O     . ASP A 1 162 ? 26.371 -19.493 -4.653  1.00 37.84  ? 162 ASP A O     1 
ATOM   1271 C  CB    . ASP A 1 162 ? 27.622 -18.225 -6.808  1.00 37.16  ? 162 ASP A CB    1 
ATOM   1272 C  CG    . ASP A 1 162 ? 28.664 -17.494 -5.980  1.00 38.85  ? 162 ASP A CG    1 
ATOM   1273 O  OD1   . ASP A 1 162 ? 28.281 -16.645 -5.149  1.00 37.20  ? 162 ASP A OD1   1 
ATOM   1274 O  OD2   . ASP A 1 162 ? 29.869 -17.776 -6.161  1.00 42.37  ? 162 ASP A OD2   1 
ATOM   1275 N  N     . SER A 1 163 ? 25.039 -17.725 -4.260  1.00 35.94  ? 163 SER A N     1 
ATOM   1276 C  CA    . SER A 1 163 ? 24.721 -18.091 -2.882  1.00 35.36  ? 163 SER A CA    1 
ATOM   1277 C  C     . SER A 1 163 ? 23.228 -18.342 -2.747  1.00 35.04  ? 163 SER A C     1 
ATOM   1278 O  O     . SER A 1 163 ? 22.431 -17.394 -2.879  1.00 33.79  ? 163 SER A O     1 
ATOM   1279 C  CB    . SER A 1 163 ? 25.166 -16.984 -1.928  1.00 35.91  ? 163 SER A CB    1 
ATOM   1280 O  OG    . SER A 1 163 ? 24.680 -17.206 -0.616  1.00 37.85  ? 163 SER A OG    1 
ATOM   1281 N  N     . PRO A 1 164 ? 22.796 -19.581 -2.502  1.00 34.57  ? 164 PRO A N     1 
ATOM   1282 C  CA    . PRO A 1 164 ? 21.366 -19.819 -2.250  1.00 36.87  ? 164 PRO A CA    1 
ATOM   1283 C  C     . PRO A 1 164 ? 20.875 -19.186 -0.961  1.00 38.30  ? 164 PRO A C     1 
ATOM   1284 O  O     . PRO A 1 164 ? 19.670 -18.936 -0.831  1.00 36.16  ? 164 PRO A O     1 
ATOM   1285 C  CB    . PRO A 1 164 ? 21.265 -21.349 -2.204  1.00 40.27  ? 164 PRO A CB    1 
ATOM   1286 C  CG    . PRO A 1 164 ? 22.640 -21.810 -1.855  1.00 41.15  ? 164 PRO A CG    1 
ATOM   1287 C  CD    . PRO A 1 164 ? 23.582 -20.825 -2.484  1.00 34.58  ? 164 PRO A CD    1 
ATOM   1288 N  N     . TYR A 1 165 ? 21.769 -18.924 -0.004  1.00 34.92  ? 165 TYR A N     1 
ATOM   1289 C  CA    . TYR A 1 165 ? 21.397 -18.174 1.191   1.00 36.25  ? 165 TYR A CA    1 
ATOM   1290 C  C     . TYR A 1 165 ? 20.980 -16.749 0.845   1.00 39.72  ? 165 TYR A C     1 
ATOM   1291 O  O     . TYR A 1 165 ? 20.088 -16.188 1.491   1.00 37.57  ? 165 TYR A O     1 
ATOM   1292 C  CB    . TYR A 1 165 ? 22.566 -18.170 2.180   1.00 37.69  ? 165 TYR A CB    1 
ATOM   1293 C  CG    . TYR A 1 165 ? 22.395 -17.245 3.365   1.00 38.25  ? 165 TYR A CG    1 
ATOM   1294 C  CD1   . TYR A 1 165 ? 21.774 -17.683 4.528   1.00 36.57  ? 165 TYR A CD1   1 
ATOM   1295 C  CD2   . TYR A 1 165 ? 22.872 -15.940 3.328   1.00 35.72  ? 165 TYR A CD2   1 
ATOM   1296 C  CE1   . TYR A 1 165 ? 21.622 -16.842 5.617   1.00 38.84  ? 165 TYR A CE1   1 
ATOM   1297 C  CE2   . TYR A 1 165 ? 22.724 -15.092 4.410   1.00 40.55  ? 165 TYR A CE2   1 
ATOM   1298 C  CZ    . TYR A 1 165 ? 22.098 -15.546 5.551   1.00 40.71  ? 165 TYR A CZ    1 
ATOM   1299 O  OH    . TYR A 1 165 ? 21.950 -14.704 6.629   1.00 41.10  ? 165 TYR A OH    1 
ATOM   1300 N  N     . VAL A 1 166 ? 21.615 -16.150 -0.165  1.00 39.12  ? 166 VAL A N     1 
ATOM   1301 C  CA    . VAL A 1 166 ? 21.254 -14.798 -0.582  1.00 34.57  ? 166 VAL A CA    1 
ATOM   1302 C  C     . VAL A 1 166 ? 19.893 -14.798 -1.265  1.00 33.73  ? 166 VAL A C     1 
ATOM   1303 O  O     . VAL A 1 166 ? 19.072 -13.900 -1.046  1.00 36.82  ? 166 VAL A O     1 
ATOM   1304 C  CB    . VAL A 1 166 ? 22.351 -14.217 -1.494  1.00 36.23  ? 166 VAL A CB    1 
ATOM   1305 C  CG1   . VAL A 1 166 ? 21.890 -12.923 -2.144  1.00 32.73  ? 166 VAL A CG1   1 
ATOM   1306 C  CG2   . VAL A 1 166 ? 23.629 -13.996 -0.709  1.00 35.19  ? 166 VAL A CG2   1 
ATOM   1307 N  N     . VAL A 1 167 ? 19.627 -15.806 -2.099  1.00 36.54  ? 167 VAL A N     1 
ATOM   1308 C  CA    . VAL A 1 167 ? 18.356 -15.865 -2.818  1.00 35.42  ? 167 VAL A CA    1 
ATOM   1309 C  C     . VAL A 1 167 ? 17.189 -15.930 -1.844  1.00 35.51  ? 167 VAL A C     1 
ATOM   1310 O  O     . VAL A 1 167 ? 16.181 -15.233 -2.011  1.00 37.66  ? 167 VAL A O     1 
ATOM   1311 C  CB    . VAL A 1 167 ? 18.345 -17.062 -3.785  1.00 35.50  ? 167 VAL A CB    1 
ATOM   1312 C  CG1   . VAL A 1 167 ? 17.060 -17.071 -4.605  1.00 36.57  ? 167 VAL A CG1   1 
ATOM   1313 C  CG2   . VAL A 1 167 ? 19.564 -17.025 -4.686  1.00 32.82  ? 167 VAL A CG2   1 
ATOM   1314 N  N     . ALA A 1 168 ? 17.305 -16.769 -0.812  1.00 37.32  ? 168 ALA A N     1 
ATOM   1315 C  CA    . ALA A 1 168 ? 16.211 -16.925 0.137   1.00 36.53  ? 168 ALA A CA    1 
ATOM   1316 C  C     . ALA A 1 168 ? 15.992 -15.648 0.937   1.00 37.24  ? 168 ALA A C     1 
ATOM   1317 O  O     . ALA A 1 168 ? 14.846 -15.244 1.168   1.00 36.57  ? 168 ALA A O     1 
ATOM   1318 C  CB    . ALA A 1 168 ? 16.487 -18.107 1.066   1.00 38.64  ? 168 ALA A CB    1 
ATOM   1319 N  N     . SER A 1 169 ? 17.078 -14.995 1.356   1.00 33.36  ? 169 SER A N     1 
ATOM   1320 C  CA    . SER A 1 169 ? 16.952 -13.762 2.127   1.00 35.78  ? 169 SER A CA    1 
ATOM   1321 C  C     . SER A 1 169 ? 16.365 -12.635 1.285   1.00 35.89  ? 169 SER A C     1 
ATOM   1322 O  O     . SER A 1 169 ? 15.581 -11.823 1.789   1.00 38.43  ? 169 SER A O     1 
ATOM   1323 C  CB    . SER A 1 169 ? 18.314 -13.356 2.693   1.00 38.17  ? 169 SER A CB    1 
ATOM   1324 O  OG    . SER A 1 169 ? 18.832 -14.354 3.560   1.00 36.31  ? 169 SER A OG    1 
ATOM   1325 N  N     . MET A 1 170 ? 16.731 -12.569 -0.001  1.00 35.10  ? 170 MET A N     1 
ATOM   1326 C  CA    . MET A 1 170 ? 16.195 -11.524 -0.870  1.00 33.03  ? 170 MET A CA    1 
ATOM   1327 C  C     . MET A 1 170 ? 14.710 -11.725 -1.140  1.00 35.86  ? 170 MET A C     1 
ATOM   1328 O  O     . MET A 1 170 ? 13.987 -10.751 -1.376  1.00 36.45  ? 170 MET A O     1 
ATOM   1329 C  CB    . MET A 1 170 ? 16.970 -11.478 -2.189  1.00 31.20  ? 170 MET A CB    1 
ATOM   1330 C  CG    . MET A 1 170 ? 18.399 -10.959 -2.068  1.00 34.05  ? 170 MET A CG    1 
ATOM   1331 S  SD    . MET A 1 170 ? 18.509 -9.169  -1.853  1.00 34.59  ? 170 MET A SD    1 
ATOM   1332 C  CE    . MET A 1 170 ? 17.813 -8.588  -3.401  1.00 30.07  ? 170 MET A CE    1 
ATOM   1333 N  N     . ARG A 1 171 ? 14.237 -12.974 -1.117  1.00 38.62  ? 171 ARG A N     1 
ATOM   1334 C  CA    . ARG A 1 171 ? 12.804 -13.218 -1.246  1.00 38.26  ? 171 ARG A CA    1 
ATOM   1335 C  C     . ARG A 1 171 ? 12.039 -12.624 -0.075  1.00 38.59  ? 171 ARG A C     1 
ATOM   1336 O  O     . ARG A 1 171 ? 10.883 -12.214 -0.227  1.00 39.49  ? 171 ARG A O     1 
ATOM   1337 C  CB    . ARG A 1 171 ? 12.528 -14.718 -1.351  1.00 37.88  ? 171 ARG A CB    1 
ATOM   1338 C  CG    . ARG A 1 171 ? 11.085 -15.051 -1.692  1.00 43.30  ? 171 ARG A CG    1 
ATOM   1339 C  CD    . ARG A 1 171 ? 10.864 -16.551 -1.808  1.00 39.94  ? 171 ARG A CD    1 
ATOM   1340 N  NE    . ARG A 1 171 ? 9.597  -16.854 -2.464  1.00 42.85  ? 171 ARG A NE    1 
ATOM   1341 C  CZ    . ARG A 1 171 ? 8.430  -16.940 -1.841  1.00 48.51  ? 171 ARG A CZ    1 
ATOM   1342 N  NH1   . ARG A 1 171 ? 8.329  -16.771 -0.532  1.00 50.59  ? 171 ARG A NH1   1 
ATOM   1343 N  NH2   . ARG A 1 171 ? 7.334  -17.198 -2.549  1.00 47.83  ? 171 ARG A NH2   1 
ATOM   1344 N  N     . ILE A 1 172 ? 12.666 -12.565 1.096   1.00 38.21  ? 172 ILE A N     1 
ATOM   1345 C  CA    . ILE A 1 172 ? 12.014 -11.982 2.259   1.00 40.57  ? 172 ILE A CA    1 
ATOM   1346 C  C     . ILE A 1 172 ? 12.179 -10.471 2.261   1.00 37.83  ? 172 ILE A C     1 
ATOM   1347 O  O     . ILE A 1 172 ? 11.209 -9.724  2.427   1.00 37.75  ? 172 ILE A O     1 
ATOM   1348 C  CB    . ILE A 1 172 ? 12.571 -12.620 3.543   1.00 41.62  ? 172 ILE A CB    1 
ATOM   1349 C  CG1   . ILE A 1 172 ? 12.267 -14.120 3.544   1.00 38.84  ? 172 ILE A CG1   1 
ATOM   1350 C  CG2   . ILE A 1 172 ? 12.010 -11.925 4.773   1.00 36.82  ? 172 ILE A CG2   1 
ATOM   1351 C  CD1   . ILE A 1 172 ? 12.871 -14.880 4.702   1.00 40.97  ? 172 ILE A CD1   1 
ATOM   1352 N  N     . MET A 1 173 ? 13.406 -9.998  2.043   1.00 37.40  ? 173 MET A N     1 
ATOM   1353 C  CA    . MET A 1 173 ? 13.707 -8.583  2.199   1.00 38.12  ? 173 MET A CA    1 
ATOM   1354 C  C     . MET A 1 173 ? 13.227 -7.726  1.034   1.00 37.86  ? 173 MET A C     1 
ATOM   1355 O  O     . MET A 1 173 ? 13.077 -6.512  1.207   1.00 38.96  ? 173 MET A O     1 
ATOM   1356 C  CB    . MET A 1 173 ? 15.212 -8.395  2.400   1.00 38.12  ? 173 MET A CB    1 
ATOM   1357 C  CG    . MET A 1 173 ? 15.725 -9.037  3.680   1.00 31.50  ? 173 MET A CG    1 
ATOM   1358 S  SD    . MET A 1 173 ? 14.809 -8.445  5.118   1.00 38.10  ? 173 MET A SD    1 
ATOM   1359 C  CE    . MET A 1 173 ? 15.199 -6.697  5.086   1.00 36.80  ? 173 MET A CE    1 
ATOM   1360 N  N     . THR A 1 174 ? 12.986 -8.310  -0.138  1.00 37.81  ? 174 THR A N     1 
ATOM   1361 C  CA    . THR A 1 174 ? 12.542 -7.552  -1.301  1.00 39.20  ? 174 THR A CA    1 
ATOM   1362 C  C     . THR A 1 174 ? 11.307 -8.209  -1.911  1.00 40.19  ? 174 THR A C     1 
ATOM   1363 O  O     . THR A 1 174 ? 10.850 -9.266  -1.466  1.00 37.37  ? 174 THR A O     1 
ATOM   1364 C  CB    . THR A 1 174 ? 13.658 -7.430  -2.352  1.00 37.70  ? 174 THR A CB    1 
ATOM   1365 O  OG1   . THR A 1 174 ? 13.933 -8.717  -2.921  1.00 38.61  ? 174 THR A OG1   1 
ATOM   1366 C  CG2   . THR A 1 174 ? 14.934 -6.877  -1.724  1.00 30.68  ? 174 THR A CG2   1 
ATOM   1367 N  N     . ARG A 1 175 ? 10.752 -7.553  -2.929  1.00 37.62  ? 175 ARG A N     1 
ATOM   1368 C  CA    . ARG A 1 175 ? 9.716  -8.148  -3.772  1.00 42.39  ? 175 ARG A CA    1 
ATOM   1369 C  C     . ARG A 1 175 ? 10.423 -8.817  -4.944  1.00 46.92  ? 175 ARG A C     1 
ATOM   1370 O  O     . ARG A 1 175 ? 10.873 -8.147  -5.875  1.00 43.95  ? 175 ARG A O     1 
ATOM   1371 C  CB    . ARG A 1 175 ? 8.717  -7.101  -4.253  1.00 41.94  ? 175 ARG A CB    1 
ATOM   1372 C  CG    . ARG A 1 175 ? 7.633  -6.731  -3.253  1.00 46.52  ? 175 ARG A CG    1 
ATOM   1373 C  CD    . ARG A 1 175 ? 8.088  -5.629  -2.319  1.00 47.56  ? 175 ARG A CD    1 
ATOM   1374 N  NE    . ARG A 1 175 ? 6.990  -5.115  -1.511  1.00 55.04  ? 175 ARG A NE    1 
ATOM   1375 C  CZ    . ARG A 1 175 ? 7.108  -4.134  -0.627  1.00 50.44  ? 175 ARG A CZ    1 
ATOM   1376 N  NH1   . ARG A 1 175 ? 8.267  -3.530  -0.417  1.00 46.86  ? 175 ARG A NH1   1 
ATOM   1377 N  NH2   . ARG A 1 175 ? 6.040  -3.755  0.069   1.00 56.91  ? 175 ARG A NH2   1 
ATOM   1378 N  N     . MET A 1 176 ? 10.521 -10.144 -4.900  1.00 45.07  ? 176 MET A N     1 
ATOM   1379 C  CA    . MET A 1 176 ? 11.318 -10.908 -5.849  1.00 43.04  ? 176 MET A CA    1 
ATOM   1380 C  C     . MET A 1 176 ? 10.435 -11.886 -6.610  1.00 42.16  ? 176 MET A C     1 
ATOM   1381 O  O     . MET A 1 176 ? 9.558  -12.526 -6.025  1.00 43.33  ? 176 MET A O     1 
ATOM   1382 C  CB    . MET A 1 176 ? 12.440 -11.668 -5.127  1.00 39.28  ? 176 MET A CB    1 
ATOM   1383 C  CG    . MET A 1 176 ? 13.464 -12.302 -6.046  1.00 43.60  ? 176 MET A CG    1 
ATOM   1384 S  SD    . MET A 1 176 ? 13.079 -13.998 -6.511  1.00 47.54  ? 176 MET A SD    1 
ATOM   1385 C  CE    . MET A 1 176 ? 13.261 -14.827 -4.935  1.00 41.76  ? 176 MET A CE    1 
ATOM   1386 N  N     . GLY A 1 177 ? 10.670 -12.004 -7.906  1.00 44.38  ? 177 GLY A N     1 
ATOM   1387 C  CA    . GLY A 1 177 ? 9.977  -13.002 -8.698  1.00 48.33  ? 177 GLY A CA    1 
ATOM   1388 C  C     . GLY A 1 177 ? 9.821  -12.560 -10.137 1.00 49.54  ? 177 GLY A C     1 
ATOM   1389 O  O     . GLY A 1 177 ? 10.360 -11.544 -10.569 1.00 50.68  ? 177 GLY A O     1 
ATOM   1390 N  N     . THR A 1 178 ? 9.048  -13.360 -10.877 1.00 49.46  ? 178 THR A N     1 
ATOM   1391 C  CA    . THR A 1 178 ? 8.836  -13.095 -12.296 1.00 56.86  ? 178 THR A CA    1 
ATOM   1392 C  C     . THR A 1 178 ? 8.033  -11.820 -12.520 1.00 58.65  ? 178 THR A C     1 
ATOM   1393 O  O     . THR A 1 178 ? 8.231  -11.134 -13.530 1.00 60.04  ? 178 THR A O     1 
ATOM   1394 C  CB    . THR A 1 178 ? 8.136  -14.289 -12.950 1.00 49.81  ? 178 THR A CB    1 
ATOM   1395 O  OG1   . THR A 1 178 ? 8.909  -15.470 -12.724 1.00 51.25  ? 178 THR A OG1   1 
ATOM   1396 C  CG2   . THR A 1 178 ? 7.981  -14.081 -14.450 1.00 56.21  ? 178 THR A CG2   1 
ATOM   1397 N  N     . SER A 1 179 ? 7.134  -11.483 -11.591 1.00 59.00  ? 179 SER A N     1 
ATOM   1398 C  CA    . SER A 1 179 ? 6.331  -10.273 -11.728 1.00 60.33  ? 179 SER A CA    1 
ATOM   1399 C  C     . SER A 1 179 ? 7.183  -9.011  -11.781 1.00 61.34  ? 179 SER A C     1 
ATOM   1400 O  O     . SER A 1 179 ? 6.719  -7.986  -12.293 1.00 58.96  ? 179 SER A O     1 
ATOM   1401 C  CB    . SER A 1 179 ? 5.332  -10.176 -10.575 1.00 61.37  ? 179 SER A CB    1 
ATOM   1402 O  OG    . SER A 1 179 ? 6.005  -10.128 -9.329  1.00 64.66  ? 179 SER A OG    1 
ATOM   1403 N  N     . VAL A 1 180 ? 8.412  -9.058  -11.265 1.00 55.95  ? 180 VAL A N     1 
ATOM   1404 C  CA    . VAL A 1 180 ? 9.283  -7.891  -11.334 1.00 56.12  ? 180 VAL A CA    1 
ATOM   1405 C  C     . VAL A 1 180 ? 9.843  -7.720  -12.742 1.00 57.36  ? 180 VAL A C     1 
ATOM   1406 O  O     . VAL A 1 180 ? 9.992  -6.592  -13.228 1.00 62.29  ? 180 VAL A O     1 
ATOM   1407 C  CB    . VAL A 1 180 ? 10.400 -7.998  -10.279 1.00 50.27  ? 180 VAL A CB    1 
ATOM   1408 C  CG1   . VAL A 1 180 ? 11.254 -6.742  -10.276 1.00 49.30  ? 180 VAL A CG1   1 
ATOM   1409 C  CG2   . VAL A 1 180 ? 9.802  -8.232  -8.906  1.00 50.40  ? 180 VAL A CG2   1 
ATOM   1410 N  N     . LEU A 1 181 ? 10.148 -8.827  -13.426 1.00 57.25  ? 181 LEU A N     1 
ATOM   1411 C  CA    . LEU A 1 181 ? 10.627 -8.735  -14.803 1.00 57.02  ? 181 LEU A CA    1 
ATOM   1412 C  C     . LEU A 1 181 ? 9.553  -8.195  -15.737 1.00 61.31  ? 181 LEU A C     1 
ATOM   1413 O  O     . LEU A 1 181 ? 9.867  -7.479  -16.695 1.00 61.37  ? 181 LEU A O     1 
ATOM   1414 C  CB    . LEU A 1 181 ? 11.106 -10.103 -15.294 1.00 56.28  ? 181 LEU A CB    1 
ATOM   1415 C  CG    . LEU A 1 181 ? 12.443 -10.616 -14.755 1.00 53.86  ? 181 LEU A CG    1 
ATOM   1416 C  CD1   . LEU A 1 181 ? 12.721 -12.021 -15.269 1.00 50.03  ? 181 LEU A CD1   1 
ATOM   1417 C  CD2   . LEU A 1 181 ? 13.568 -9.668  -15.139 1.00 50.15  ? 181 LEU A CD2   1 
ATOM   1418 N  N     . GLU A 1 182 ? 8.287  -8.527  -15.480 1.00 64.11  ? 182 GLU A N     1 
ATOM   1419 C  CA    . GLU A 1 182 ? 7.212  -8.041  -16.337 1.00 64.26  ? 182 GLU A CA    1 
ATOM   1420 C  C     . GLU A 1 182 ? 6.974  -6.551  -16.128 1.00 63.41  ? 182 GLU A C     1 
ATOM   1421 O  O     . GLU A 1 182 ? 6.725  -5.816  -17.090 1.00 66.11  ? 182 GLU A O     1 
ATOM   1422 C  CB    . GLU A 1 182 ? 5.936  -8.840  -16.076 1.00 67.38  ? 182 GLU A CB    1 
ATOM   1423 C  CG    . GLU A 1 182 ? 6.096  -10.334 -16.310 1.00 73.44  ? 182 GLU A CG    1 
ATOM   1424 C  CD    . GLU A 1 182 ? 4.814  -11.107 -16.066 1.00 84.71  ? 182 GLU A CD    1 
ATOM   1425 O  OE1   . GLU A 1 182 ? 3.790  -10.474 -15.729 1.00 89.10  ? 182 GLU A OE1   1 
ATOM   1426 O  OE2   . GLU A 1 182 ? 4.831  -12.349 -16.210 1.00 85.20  ? 182 GLU A OE2   1 
ATOM   1427 N  N     . ALA A 1 183 ? 7.055  -6.086  -14.880 1.00 65.63  ? 183 ALA A N     1 
ATOM   1428 C  CA    . ALA A 1 183 ? 6.933  -4.657  -14.620 1.00 61.77  ? 183 ALA A CA    1 
ATOM   1429 C  C     . ALA A 1 183 ? 8.151  -3.892  -15.119 1.00 61.29  ? 183 ALA A C     1 
ATOM   1430 O  O     . ALA A 1 183 ? 8.037  -2.713  -15.471 1.00 61.48  ? 183 ALA A O     1 
ATOM   1431 C  CB    . ALA A 1 183 ? 6.722  -4.408  -13.127 1.00 61.07  ? 183 ALA A CB    1 
ATOM   1432 N  N     . LEU A 1 184 ? 9.317  -4.540  -15.159 1.00 62.53  ? 184 LEU A N     1 
ATOM   1433 C  CA    . LEU A 1 184 ? 10.528 -3.876  -15.630 1.00 59.90  ? 184 LEU A CA    1 
ATOM   1434 C  C     . LEU A 1 184 ? 10.435 -3.555  -17.117 1.00 64.01  ? 184 LEU A C     1 
ATOM   1435 O  O     . LEU A 1 184 ? 10.544 -2.392  -17.523 1.00 61.87  ? 184 LEU A O     1 
ATOM   1436 C  CB    . LEU A 1 184 ? 11.751 -4.750  -15.345 1.00 55.16  ? 184 LEU A CB    1 
ATOM   1437 C  CG    . LEU A 1 184 ? 13.085 -4.210  -15.865 1.00 58.82  ? 184 LEU A CG    1 
ATOM   1438 C  CD1   . LEU A 1 184 ? 13.449 -2.915  -15.158 1.00 54.34  ? 184 LEU A CD1   1 
ATOM   1439 C  CD2   . LEU A 1 184 ? 14.195 -5.242  -15.711 1.00 51.37  ? 184 LEU A CD2   1 
ATOM   1440 N  N     . GLY A 1 185 ? 10.232 -4.576  -17.944 1.00 62.95  ? 185 GLY A N     1 
ATOM   1441 C  CA    . GLY A 1 185 ? 10.184 -4.352  -19.380 1.00 62.71  ? 185 GLY A CA    1 
ATOM   1442 C  C     . GLY A 1 185 ? 11.540 -3.909  -19.890 1.00 70.99  ? 185 GLY A C     1 
ATOM   1443 O  O     . GLY A 1 185 ? 12.577 -4.488  -19.547 1.00 70.66  ? 185 GLY A O     1 
ATOM   1444 N  N     . ASP A 1 186 ? 11.539 -2.866  -20.717 1.00 79.11  ? 186 ASP A N     1 
ATOM   1445 C  CA    . ASP A 1 186 ? 12.765 -2.276  -21.237 1.00 76.66  ? 186 ASP A CA    1 
ATOM   1446 C  C     . ASP A 1 186 ? 13.291 -1.145  -20.362 1.00 73.21  ? 186 ASP A C     1 
ATOM   1447 O  O     . ASP A 1 186 ? 14.160 -0.388  -20.807 1.00 73.22  ? 186 ASP A O     1 
ATOM   1448 C  CB    . ASP A 1 186 ? 12.543 -1.766  -22.663 1.00 77.42  ? 186 ASP A CB    1 
ATOM   1449 C  CG    . ASP A 1 186 ? 12.284 -2.888  -23.649 1.00 83.87  ? 186 ASP A CG    1 
ATOM   1450 O  OD1   . ASP A 1 186 ? 12.792 -4.008  -23.423 1.00 84.14  ? 186 ASP A OD1   1 
ATOM   1451 O  OD2   . ASP A 1 186 ? 11.572 -2.652  -24.648 1.00 86.63  ? 186 ASP A OD2   1 
ATOM   1452 N  N     . GLY A 1 187 ? 12.789 -1.015  -19.137 1.00 66.17  ? 187 GLY A N     1 
ATOM   1453 C  CA    . GLY A 1 187 ? 13.237 0.043   -18.258 1.00 65.61  ? 187 GLY A CA    1 
ATOM   1454 C  C     . GLY A 1 187 ? 14.615 -0.226  -17.684 1.00 67.38  ? 187 GLY A C     1 
ATOM   1455 O  O     . GLY A 1 187 ? 15.159 -1.328  -17.755 1.00 64.77  ? 187 GLY A O     1 
ATOM   1456 N  N     . GLU A 1 188 ? 15.190 0.822   -17.101 1.00 62.28  ? 188 GLU A N     1 
ATOM   1457 C  CA    . GLU A 1 188 ? 16.507 0.703   -16.498 1.00 60.27  ? 188 GLU A CA    1 
ATOM   1458 C  C     . GLU A 1 188 ? 16.436 -0.115  -15.211 1.00 56.31  ? 188 GLU A C     1 
ATOM   1459 O  O     . GLU A 1 188 ? 15.368 -0.312  -14.624 1.00 56.29  ? 188 GLU A O     1 
ATOM   1460 C  CB    . GLU A 1 188 ? 17.090 2.086   -16.211 1.00 62.99  ? 188 GLU A CB    1 
ATOM   1461 C  CG    . GLU A 1 188 ? 17.147 2.996   -17.425 1.00 77.41  ? 188 GLU A CG    1 
ATOM   1462 C  CD    . GLU A 1 188 ? 17.621 4.393   -17.081 1.00 88.04  ? 188 GLU A CD    1 
ATOM   1463 O  OE1   . GLU A 1 188 ? 18.012 4.617   -15.915 1.00 85.74  ? 188 GLU A OE1   1 
ATOM   1464 O  OE2   . GLU A 1 188 ? 17.602 5.266   -17.977 1.00 94.14  ? 188 GLU A OE2   1 
ATOM   1465 N  N     . PHE A 1 189 ? 17.598 -0.598  -14.776 1.00 50.81  ? 189 PHE A N     1 
ATOM   1466 C  CA    . PHE A 1 189 ? 17.693 -1.351  -13.536 1.00 51.22  ? 189 PHE A CA    1 
ATOM   1467 C  C     . PHE A 1 189 ? 19.095 -1.196  -12.971 1.00 50.93  ? 189 PHE A C     1 
ATOM   1468 O  O     . PHE A 1 189 ? 20.048 -0.918  -13.703 1.00 49.44  ? 189 PHE A O     1 
ATOM   1469 C  CB    . PHE A 1 189 ? 17.357 -2.837  -13.742 1.00 53.15  ? 189 PHE A CB    1 
ATOM   1470 C  CG    . PHE A 1 189 ? 18.221 -3.525  -14.765 1.00 50.09  ? 189 PHE A CG    1 
ATOM   1471 C  CD1   . PHE A 1 189 ? 17.875 -3.511  -16.106 1.00 49.53  ? 189 PHE A CD1   1 
ATOM   1472 C  CD2   . PHE A 1 189 ? 19.372 -4.195  -14.384 1.00 47.33  ? 189 PHE A CD2   1 
ATOM   1473 C  CE1   . PHE A 1 189 ? 18.664 -4.142  -17.049 1.00 52.55  ? 189 PHE A CE1   1 
ATOM   1474 C  CE2   . PHE A 1 189 ? 20.166 -4.827  -15.322 1.00 44.46  ? 189 PHE A CE2   1 
ATOM   1475 C  CZ    . PHE A 1 189 ? 19.811 -4.801  -16.655 1.00 50.07  ? 189 PHE A CZ    1 
ATOM   1476 N  N     . ILE A 1 190 ? 19.212 -1.374  -11.661 1.00 42.24  ? 190 ILE A N     1 
ATOM   1477 C  CA    . ILE A 1 190 ? 20.515 -1.321  -11.011 1.00 46.72  ? 190 ILE A CA    1 
ATOM   1478 C  C     . ILE A 1 190 ? 21.171 -2.690  -11.123 1.00 47.02  ? 190 ILE A C     1 
ATOM   1479 O  O     . ILE A 1 190 ? 20.570 -3.715  -10.778 1.00 44.56  ? 190 ILE A O     1 
ATOM   1480 C  CB    . ILE A 1 190 ? 20.380 -0.867  -9.547  1.00 45.87  ? 190 ILE A CB    1 
ATOM   1481 C  CG1   . ILE A 1 190 ? 21.684 -1.106  -8.782  1.00 46.18  ? 190 ILE A CG1   1 
ATOM   1482 C  CG2   . ILE A 1 190 ? 19.216 -1.552  -8.872  1.00 52.96  ? 190 ILE A CG2   1 
ATOM   1483 C  CD1   . ILE A 1 190 ? 22.630 0.072   -8.822  1.00 52.34  ? 190 ILE A CD1   1 
ATOM   1484 N  N     . LYS A 1 191 ? 22.396 -2.713  -11.642 1.00 46.45  ? 191 LYS A N     1 
ATOM   1485 C  CA    . LYS A 1 191 ? 23.114 -3.960  -11.861 1.00 41.76  ? 191 LYS A CA    1 
ATOM   1486 C  C     . LYS A 1 191 ? 23.812 -4.372  -10.573 1.00 39.97  ? 191 LYS A C     1 
ATOM   1487 O  O     . LYS A 1 191 ? 24.667 -3.643  -10.060 1.00 43.17  ? 191 LYS A O     1 
ATOM   1488 C  CB    . LYS A 1 191 ? 24.119 -3.797  -12.997 1.00 41.85  ? 191 LYS A CB    1 
ATOM   1489 C  CG    . LYS A 1 191 ? 23.490 -3.351  -14.304 1.00 46.54  ? 191 LYS A CG    1 
ATOM   1490 C  CD    . LYS A 1 191 ? 24.545 -3.031  -15.349 1.00 48.65  ? 191 LYS A CD    1 
ATOM   1491 C  CE    . LYS A 1 191 ? 23.915 -2.443  -16.599 1.00 53.93  ? 191 LYS A CE    1 
ATOM   1492 N  NZ    . LYS A 1 191 ? 24.936 -2.088  -17.619 1.00 63.29  ? 191 LYS A NZ    1 
ATOM   1493 N  N     . CYS A 1 192 ? 23.444 -5.536  -10.048 1.00 34.41  ? 192 CYS A N     1 
ATOM   1494 C  CA    . CYS A 1 192 ? 24.002 -6.049  -8.805  1.00 36.76  ? 192 CYS A CA    1 
ATOM   1495 C  C     . CYS A 1 192 ? 24.677 -7.380  -9.092  1.00 37.59  ? 192 CYS A C     1 
ATOM   1496 O  O     . CYS A 1 192 ? 24.042 -8.299  -9.621  1.00 37.52  ? 192 CYS A O     1 
ATOM   1497 C  CB    . CYS A 1 192 ? 22.917 -6.205  -7.738  1.00 35.36  ? 192 CYS A CB    1 
ATOM   1498 S  SG    . CYS A 1 192 ? 22.029 -4.680  -7.362  1.00 35.26  ? 192 CYS A SG    1 
ATOM   1499 N  N     . LEU A 1 193 ? 25.960 -7.476  -8.752  1.00 34.07  ? 193 LEU A N     1 
ATOM   1500 C  CA    . LEU A 1 193 ? 26.754 -8.675  -8.982  1.00 36.55  ? 193 LEU A CA    1 
ATOM   1501 C  C     . LEU A 1 193 ? 27.406 -9.075  -7.671  1.00 39.71  ? 193 LEU A C     1 
ATOM   1502 O  O     . LEU A 1 193 ? 28.174 -8.298  -7.092  1.00 39.86  ? 193 LEU A O     1 
ATOM   1503 C  CB    . LEU A 1 193 ? 27.814 -8.444  -10.062 1.00 35.18  ? 193 LEU A CB    1 
ATOM   1504 C  CG    . LEU A 1 193 ? 28.874 -9.535  -10.233 1.00 39.68  ? 193 LEU A CG    1 
ATOM   1505 C  CD1   . LEU A 1 193 ? 28.242 -10.855 -10.644 1.00 34.15  ? 193 LEU A CD1   1 
ATOM   1506 C  CD2   . LEU A 1 193 ? 29.924 -9.099  -11.248 1.00 42.45  ? 193 LEU A CD2   1 
ATOM   1507 N  N     . HIS A 1 194 ? 27.102 -10.280 -7.205  1.00 38.37  ? 194 HIS A N     1 
ATOM   1508 C  CA    . HIS A 1 194 ? 27.645 -10.787 -5.958  1.00 37.62  ? 194 HIS A CA    1 
ATOM   1509 C  C     . HIS A 1 194 ? 28.205 -12.184 -6.171  1.00 40.99  ? 194 HIS A C     1 
ATOM   1510 O  O     . HIS A 1 194 ? 27.653 -12.972 -6.943  1.00 34.88  ? 194 HIS A O     1 
ATOM   1511 C  CB    . HIS A 1 194 ? 26.580 -10.814 -4.861  1.00 36.47  ? 194 HIS A CB    1 
ATOM   1512 C  CG    . HIS A 1 194 ? 27.012 -11.544 -3.632  1.00 33.71  ? 194 HIS A CG    1 
ATOM   1513 N  ND1   . HIS A 1 194 ? 26.581 -12.819 -3.335  1.00 36.11  ? 194 HIS A ND1   1 
ATOM   1514 C  CD2   . HIS A 1 194 ? 27.859 -11.191 -2.638  1.00 35.10  ? 194 HIS A CD2   1 
ATOM   1515 C  CE1   . HIS A 1 194 ? 27.134 -13.214 -2.203  1.00 41.02  ? 194 HIS A CE1   1 
ATOM   1516 N  NE2   . HIS A 1 194 ? 27.913 -12.244 -1.759  1.00 41.01  ? 194 HIS A NE2   1 
ATOM   1517 N  N     . SER A 1 195 ? 29.306 -12.481 -5.482  1.00 36.24  ? 195 SER A N     1 
ATOM   1518 C  CA    . SER A 1 195 ? 29.885 -13.813 -5.482  1.00 39.58  ? 195 SER A CA    1 
ATOM   1519 C  C     . SER A 1 195 ? 30.591 -14.046 -4.157  1.00 46.22  ? 195 SER A C     1 
ATOM   1520 O  O     . SER A 1 195 ? 31.264 -13.149 -3.640  1.00 40.22  ? 195 SER A O     1 
ATOM   1521 C  CB    . SER A 1 195 ? 30.870 -14.003 -6.640  1.00 42.35  ? 195 SER A CB    1 
ATOM   1522 O  OG    . SER A 1 195 ? 31.550 -15.239 -6.517  1.00 45.53  ? 195 SER A OG    1 
ATOM   1523 N  N     . VAL A 1 196 ? 30.436 -15.259 -3.616  1.00 45.18  ? 196 VAL A N     1 
ATOM   1524 C  CA    . VAL A 1 196 ? 31.130 -15.619 -2.385  1.00 44.87  ? 196 VAL A CA    1 
ATOM   1525 C  C     . VAL A 1 196 ? 32.625 -15.794 -2.617  1.00 51.58  ? 196 VAL A C     1 
ATOM   1526 O  O     . VAL A 1 196 ? 33.401 -15.796 -1.655  1.00 55.27  ? 196 VAL A O     1 
ATOM   1527 C  CB    . VAL A 1 196 ? 30.524 -16.896 -1.767  1.00 48.33  ? 196 VAL A CB    1 
ATOM   1528 C  CG1   . VAL A 1 196 ? 29.082 -16.652 -1.340  1.00 43.17  ? 196 VAL A CG1   1 
ATOM   1529 C  CG2   . VAL A 1 196 ? 30.610 -18.064 -2.743  1.00 44.00  ? 196 VAL A CG2   1 
ATOM   1530 N  N     . GLY A 1 197 ? 33.053 -15.948 -3.867  1.00 66.16  ? 197 GLY A N     1 
ATOM   1531 C  CA    . GLY A 1 197 ? 34.471 -15.995 -4.167  1.00 67.02  ? 197 GLY A CA    1 
ATOM   1532 C  C     . GLY A 1 197 ? 35.158 -17.291 -3.807  1.00 67.37  ? 197 GLY A C     1 
ATOM   1533 O  O     . GLY A 1 197 ? 36.346 -17.281 -3.465  1.00 68.32  ? 197 GLY A O     1 
ATOM   1534 N  N     . CYS A 1 198 ? 34.442 -18.413 -3.872  1.00 59.38  ? 198 CYS A N     1 
ATOM   1535 C  CA    . CYS A 1 198 ? 35.005 -19.735 -3.603  1.00 53.30  ? 198 CYS A CA    1 
ATOM   1536 C  C     . CYS A 1 198 ? 34.647 -20.655 -4.760  1.00 54.86  ? 198 CYS A C     1 
ATOM   1537 O  O     . CYS A 1 198 ? 33.770 -21.521 -4.632  1.00 52.50  ? 198 CYS A O     1 
ATOM   1538 C  CB    . CYS A 1 198 ? 34.499 -20.296 -2.274  1.00 56.02  ? 198 CYS A CB    1 
ATOM   1539 S  SG    . CYS A 1 198 ? 35.010 -19.351 -0.824  1.00 58.85  ? 198 CYS A SG    1 
ATOM   1540 N  N     . PRO A 1 199 ? 35.301 -20.495 -5.908  1.00 56.12  ? 199 PRO A N     1 
ATOM   1541 C  CA    . PRO A 1 199 ? 35.046 -21.402 -7.029  1.00 56.19  ? 199 PRO A CA    1 
ATOM   1542 C  C     . PRO A 1 199 ? 35.465 -22.824 -6.691  1.00 60.60  ? 199 PRO A C     1 
ATOM   1543 O  O     . PRO A 1 199 ? 36.395 -23.056 -5.916  1.00 62.44  ? 199 PRO A O     1 
ATOM   1544 C  CB    . PRO A 1 199 ? 35.903 -20.821 -8.158  1.00 58.50  ? 199 PRO A CB    1 
ATOM   1545 C  CG    . PRO A 1 199 ? 36.993 -20.083 -7.452  1.00 59.81  ? 199 PRO A CG    1 
ATOM   1546 C  CD    . PRO A 1 199 ? 36.345 -19.506 -6.226  1.00 54.09  ? 199 PRO A CD    1 
ATOM   1547 N  N     . LEU A 1 200 ? 34.753 -23.782 -7.282  1.00 59.94  ? 200 LEU A N     1 
ATOM   1548 C  CA    . LEU A 1 200 ? 35.007 -25.200 -7.050  1.00 62.75  ? 200 LEU A CA    1 
ATOM   1549 C  C     . LEU A 1 200 ? 35.973 -25.744 -8.098  1.00 67.58  ? 200 LEU A C     1 
ATOM   1550 O  O     . LEU A 1 200 ? 35.881 -25.379 -9.273  1.00 69.23  ? 200 LEU A O     1 
ATOM   1551 C  CB    . LEU A 1 200 ? 33.707 -25.994 -7.093  1.00 61.42  ? 200 LEU A CB    1 
ATOM   1552 C  CG    . LEU A 1 200 ? 32.602 -25.471 -6.172  1.00 60.22  ? 200 LEU A CG    1 
ATOM   1553 C  CD1   . LEU A 1 200 ? 31.296 -26.210 -6.416  1.00 60.16  ? 200 LEU A CD1   1 
ATOM   1554 C  CD2   . LEU A 1 200 ? 33.029 -25.582 -4.718  1.00 57.33  ? 200 LEU A CD2   1 
ATOM   1555 N  N     . PRO A 1 201 ? 36.908 -26.625 -7.711  1.00 69.99  ? 201 PRO A N     1 
ATOM   1556 C  CA    . PRO A 1 201 ? 37.120 -27.189 -6.366  1.00 74.62  ? 201 PRO A CA    1 
ATOM   1557 C  C     . PRO A 1 201 ? 37.714 -26.180 -5.386  1.00 74.79  ? 201 PRO A C     1 
ATOM   1558 O  O     . PRO A 1 201 ? 38.389 -25.236 -5.790  1.00 75.62  ? 201 PRO A O     1 
ATOM   1559 C  CB    . PRO A 1 201 ? 38.077 -28.359 -6.637  1.00 77.82  ? 201 PRO A CB    1 
ATOM   1560 C  CG    . PRO A 1 201 ? 38.864 -27.918 -7.834  1.00 77.85  ? 201 PRO A CG    1 
ATOM   1561 C  CD    . PRO A 1 201 ? 37.876 -27.161 -8.686  1.00 73.68  ? 201 PRO A CD    1 
ATOM   1562 N  N     . LEU A 1 202 ? 37.471 -26.365 -4.090  1.00 75.45  ? 202 LEU A N     1 
ATOM   1563 C  CA    . LEU A 1 202 ? 37.924 -25.403 -3.093  1.00 82.83  ? 202 LEU A CA    1 
ATOM   1564 C  C     . LEU A 1 202 ? 39.426 -25.523 -2.870  1.00 90.62  ? 202 LEU A C     1 
ATOM   1565 O  O     . LEU A 1 202 ? 39.960 -26.626 -2.720  1.00 87.61  ? 202 LEU A O     1 
ATOM   1566 C  CB    . LEU A 1 202 ? 37.179 -25.610 -1.774  1.00 79.81  ? 202 LEU A CB    1 
ATOM   1567 C  CG    . LEU A 1 202 ? 35.677 -25.312 -1.771  1.00 69.49  ? 202 LEU A CG    1 
ATOM   1568 C  CD1   . LEU A 1 202 ? 35.108 -25.457 -0.368  1.00 68.14  ? 202 LEU A CD1   1 
ATOM   1569 C  CD2   . LEU A 1 202 ? 35.401 -23.925 -2.323  1.00 70.40  ? 202 LEU A CD2   1 
ATOM   1570 N  N     . LYS A 1 203 ? 40.108 -24.379 -2.853  1.00 99.73  ? 203 LYS A N     1 
ATOM   1571 C  CA    . LYS A 1 203 ? 41.527 -24.328 -2.525  1.00 107.20 ? 203 LYS A CA    1 
ATOM   1572 C  C     . LYS A 1 203 ? 41.756 -24.277 -1.018  1.00 111.35 ? 203 LYS A C     1 
ATOM   1573 O  O     . LYS A 1 203 ? 42.638 -24.971 -0.502  1.00 112.49 ? 203 LYS A O     1 
ATOM   1574 C  CB    . LYS A 1 203 ? 42.186 -23.115 -3.195  1.00 110.30 ? 203 LYS A CB    1 
ATOM   1575 C  CG    . LYS A 1 203 ? 42.031 -23.061 -4.707  1.00 109.62 ? 203 LYS A CG    1 
ATOM   1576 C  CD    . LYS A 1 203 ? 42.686 -24.256 -5.379  1.00 114.22 ? 203 LYS A CD    1 
ATOM   1577 C  CE    . LYS A 1 203 ? 42.610 -24.150 -6.894  1.00 114.21 ? 203 LYS A CE    1 
ATOM   1578 N  NZ    . LYS A 1 203 ? 41.206 -24.038 -7.380  1.00 110.87 ? 203 LYS A NZ    1 
ATOM   1579 N  N     . LYS A 1 204 ? 40.972 -23.469 -0.305  1.00 120.19 ? 204 LYS A N     1 
ATOM   1580 C  CA    . LYS A 1 204 ? 40.974 -23.247 1.133   1.00 120.38 ? 204 LYS A CA    1 
ATOM   1581 C  C     . LYS A 1 204 ? 39.890 -24.080 1.806   1.00 116.39 ? 204 LYS A C     1 
ATOM   1582 O  O     . LYS A 1 204 ? 38.810 -24.274 1.236   1.00 112.09 ? 204 LYS A O     1 
ATOM   1583 C  CB    . LYS A 1 204 ? 40.746 -21.769 1.454   1.00 122.52 ? 204 LYS A CB    1 
ATOM   1584 C  CG    . LYS A 1 204 ? 41.684 -20.814 0.727   1.00 126.51 ? 204 LYS A CG    1 
ATOM   1585 C  CD    . LYS A 1 204 ? 41.279 -19.363 0.955   1.00 132.06 ? 204 LYS A CD    1 
ATOM   1586 C  CE    . LYS A 1 204 ? 42.157 -18.409 0.158   1.00 122.03 ? 204 LYS A CE    1 
ATOM   1587 N  NZ    . LYS A 1 204 ? 41.720 -16.993 0.313   1.00 112.59 ? 204 LYS A NZ    1 
ATOM   1588 N  N     . PRO A 1 205 ? 40.140 -24.588 3.012   1.00 110.50 ? 205 PRO A N     1 
ATOM   1589 C  CA    . PRO A 1 205 ? 39.114 -25.383 3.698   1.00 104.72 ? 205 PRO A CA    1 
ATOM   1590 C  C     . PRO A 1 205 ? 37.960 -24.512 4.169   1.00 97.47  ? 205 PRO A C     1 
ATOM   1591 O  O     . PRO A 1 205 ? 38.157 -23.412 4.691   1.00 92.71  ? 205 PRO A O     1 
ATOM   1592 C  CB    . PRO A 1 205 ? 39.873 -25.998 4.879   1.00 101.61 ? 205 PRO A CB    1 
ATOM   1593 C  CG    . PRO A 1 205 ? 40.985 -25.038 5.142   1.00 107.55 ? 205 PRO A CG    1 
ATOM   1594 C  CD    . PRO A 1 205 ? 41.383 -24.489 3.797   1.00 110.60 ? 205 PRO A CD    1 
ATOM   1595 N  N     . LEU A 1 206 ? 36.746 -25.019 3.978   1.00 90.96  ? 206 LEU A N     1 
ATOM   1596 C  CA    . LEU A 1 206 ? 35.547 -24.287 4.352   1.00 80.50  ? 206 LEU A CA    1 
ATOM   1597 C  C     . LEU A 1 206 ? 35.246 -24.472 5.836   1.00 80.55  ? 206 LEU A C     1 
ATOM   1598 O  O     . LEU A 1 206 ? 35.523 -25.522 6.422   1.00 83.56  ? 206 LEU A O     1 
ATOM   1599 C  CB    . LEU A 1 206 ? 34.358 -24.754 3.515   1.00 71.34  ? 206 LEU A CB    1 
ATOM   1600 C  CG    . LEU A 1 206 ? 33.399 -23.664 3.050   1.00 68.49  ? 206 LEU A CG    1 
ATOM   1601 C  CD1   . LEU A 1 206 ? 34.146 -22.623 2.234   1.00 65.31  ? 206 LEU A CD1   1 
ATOM   1602 C  CD2   . LEU A 1 206 ? 32.265 -24.266 2.242   1.00 66.31  ? 206 LEU A CD2   1 
ATOM   1603 N  N     . VAL A 1 207 ? 34.671 -23.436 6.442   1.00 71.59  ? 207 VAL A N     1 
ATOM   1604 C  CA    . VAL A 1 207 ? 34.354 -23.428 7.866   1.00 72.09  ? 207 VAL A CA    1 
ATOM   1605 C  C     . VAL A 1 207 ? 32.854 -23.238 8.031   1.00 71.64  ? 207 VAL A C     1 
ATOM   1606 O  O     . VAL A 1 207 ? 32.281 -22.284 7.489   1.00 69.84  ? 207 VAL A O     1 
ATOM   1607 C  CB    . VAL A 1 207 ? 35.129 -22.330 8.616   1.00 68.00  ? 207 VAL A CB    1 
ATOM   1608 C  CG1   . VAL A 1 207 ? 34.666 -22.251 10.061  1.00 66.40  ? 207 VAL A CG1   1 
ATOM   1609 C  CG2   . VAL A 1 207 ? 36.622 -22.600 8.547   1.00 74.09  ? 207 VAL A CG2   1 
ATOM   1610 N  N     . ASN A 1 208 ? 32.224 -24.145 8.782   1.00 67.39  ? 208 ASN A N     1 
ATOM   1611 C  CA    . ASN A 1 208 ? 30.783 -24.119 9.033   1.00 65.86  ? 208 ASN A CA    1 
ATOM   1612 C  C     . ASN A 1 208 ? 29.978 -24.116 7.738   1.00 61.92  ? 208 ASN A C     1 
ATOM   1613 O  O     . ASN A 1 208 ? 28.882 -23.550 7.680   1.00 63.43  ? 208 ASN A O     1 
ATOM   1614 C  CB    . ASN A 1 208 ? 30.387 -22.925 9.906   1.00 67.37  ? 208 ASN A CB    1 
ATOM   1615 C  CG    . ASN A 1 208 ? 30.857 -23.072 11.337  1.00 71.59  ? 208 ASN A CG    1 
ATOM   1616 O  OD1   . ASN A 1 208 ? 31.187 -24.171 11.784  1.00 77.52  ? 208 ASN A OD1   1 
ATOM   1617 N  ND2   . ASN A 1 208 ? 30.881 -21.964 12.070  1.00 67.31  ? 208 ASN A ND2   1 
ATOM   1618 N  N     . ASN A 1 209 ? 30.523 -24.745 6.693   1.00 63.47  ? 209 ASN A N     1 
ATOM   1619 C  CA    . ASN A 1 209 ? 29.893 -24.809 5.373   1.00 62.93  ? 209 ASN A CA    1 
ATOM   1620 C  C     . ASN A 1 209 ? 29.573 -23.427 4.819   1.00 57.22  ? 209 ASN A C     1 
ATOM   1621 O  O     . ASN A 1 209 ? 28.690 -23.284 3.969   1.00 60.01  ? 209 ASN A O     1 
ATOM   1622 C  CB    . ASN A 1 209 ? 28.625 -25.668 5.402   1.00 60.33  ? 209 ASN A CB    1 
ATOM   1623 C  CG    . ASN A 1 209 ? 28.926 -27.145 5.334   1.00 62.74  ? 209 ASN A CG    1 
ATOM   1624 O  OD1   . ASN A 1 209 ? 28.900 -27.745 4.260   1.00 66.35  ? 209 ASN A OD1   1 
ATOM   1625 N  ND2   . ASN A 1 209 ? 29.216 -27.743 6.482   1.00 65.32  ? 209 ASN A ND2   1 
ATOM   1626 N  N     . TRP A 1 210 ? 30.270 -22.397 5.291   1.00 55.72  ? 210 TRP A N     1 
ATOM   1627 C  CA    . TRP A 1 210 ? 29.996 -21.020 4.898   1.00 59.15  ? 210 TRP A CA    1 
ATOM   1628 C  C     . TRP A 1 210 ? 31.040 -20.594 3.873   1.00 53.74  ? 210 TRP A C     1 
ATOM   1629 O  O     . TRP A 1 210 ? 32.207 -20.380 4.216   1.00 55.92  ? 210 TRP A O     1 
ATOM   1630 C  CB    . TRP A 1 210 ? 29.995 -20.094 6.113   1.00 54.75  ? 210 TRP A CB    1 
ATOM   1631 C  CG    . TRP A 1 210 ? 29.491 -18.718 5.809   1.00 49.87  ? 210 TRP A CG    1 
ATOM   1632 C  CD1   . TRP A 1 210 ? 30.239 -17.583 5.666   1.00 48.63  ? 210 TRP A CD1   1 
ATOM   1633 C  CD2   . TRP A 1 210 ? 28.129 -18.328 5.600   1.00 47.95  ? 210 TRP A CD2   1 
ATOM   1634 N  NE1   . TRP A 1 210 ? 29.427 -16.513 5.384   1.00 43.96  ? 210 TRP A NE1   1 
ATOM   1635 C  CE2   . TRP A 1 210 ? 28.127 -16.943 5.337   1.00 46.68  ? 210 TRP A CE2   1 
ATOM   1636 C  CE3   . TRP A 1 210 ? 26.910 -19.015 5.610   1.00 45.10  ? 210 TRP A CE3   1 
ATOM   1637 C  CZ2   . TRP A 1 210 ? 26.954 -16.230 5.089   1.00 48.30  ? 210 TRP A CZ2   1 
ATOM   1638 C  CZ3   . TRP A 1 210 ? 25.747 -18.307 5.361   1.00 44.84  ? 210 TRP A CZ3   1 
ATOM   1639 C  CH2   . TRP A 1 210 ? 25.778 -16.928 5.102   1.00 48.26  ? 210 TRP A CH2   1 
ATOM   1640 N  N     . ALA A 1 211 ? 30.621 -20.486 2.617   1.00 51.02  ? 211 ALA A N     1 
ATOM   1641 C  CA    . ALA A 1 211 ? 31.512 -20.065 1.543   1.00 54.16  ? 211 ALA A CA    1 
ATOM   1642 C  C     . ALA A 1 211 ? 31.763 -18.566 1.648   1.00 52.10  ? 211 ALA A C     1 
ATOM   1643 O  O     . ALA A 1 211 ? 30.828 -17.764 1.548   1.00 49.67  ? 211 ALA A O     1 
ATOM   1644 C  CB    . ALA A 1 211 ? 30.916 -20.417 0.182   1.00 46.03  ? 211 ALA A CB    1 
ATOM   1645 N  N     . CYS A 1 212 ? 33.023 -18.191 1.852   1.00 52.09  ? 212 CYS A N     1 
ATOM   1646 C  CA    . CYS A 1 212 ? 33.396 -16.788 1.947   1.00 50.98  ? 212 CYS A CA    1 
ATOM   1647 C  C     . CYS A 1 212 ? 34.890 -16.663 1.695   1.00 53.98  ? 212 CYS A C     1 
ATOM   1648 O  O     . CYS A 1 212 ? 35.642 -17.635 1.808   1.00 52.85  ? 212 CYS A O     1 
ATOM   1649 C  CB    . CYS A 1 212 ? 33.031 -16.200 3.314   1.00 51.13  ? 212 CYS A CB    1 
ATOM   1650 S  SG    . CYS A 1 212 ? 33.999 -16.881 4.680   1.00 48.22  ? 212 CYS A SG    1 
ATOM   1651 N  N     . ASN A 1 213 ? 35.311 -15.446 1.355   1.00 55.08  ? 213 ASN A N     1 
ATOM   1652 C  CA    . ASN A 1 213 ? 36.717 -15.130 1.114   1.00 58.09  ? 213 ASN A CA    1 
ATOM   1653 C  C     . ASN A 1 213 ? 37.025 -13.828 1.839   1.00 59.70  ? 213 ASN A C     1 
ATOM   1654 O  O     . ASN A 1 213 ? 36.949 -12.742 1.248   1.00 60.41  ? 213 ASN A O     1 
ATOM   1655 C  CB    . ASN A 1 213 ? 37.014 -15.024 -0.381  1.00 58.69  ? 213 ASN A CB    1 
ATOM   1656 C  CG    . ASN A 1 213 ? 38.493 -15.121 -0.690  1.00 62.82  ? 213 ASN A CG    1 
ATOM   1657 O  OD1   . ASN A 1 213 ? 39.336 -14.693 0.099   1.00 69.84  ? 213 ASN A OD1   1 
ATOM   1658 N  ND2   . ASN A 1 213 ? 38.817 -15.693 -1.844  1.00 65.14  ? 213 ASN A ND2   1 
ATOM   1659 N  N     . PRO A 1 214 ? 37.370 -13.898 3.126   1.00 62.48  ? 214 PRO A N     1 
ATOM   1660 C  CA    . PRO A 1 214 ? 37.629 -12.661 3.881   1.00 63.86  ? 214 PRO A CA    1 
ATOM   1661 C  C     . PRO A 1 214 ? 38.800 -11.855 3.348   1.00 67.78  ? 214 PRO A C     1 
ATOM   1662 O  O     . PRO A 1 214 ? 38.774 -10.620 3.426   1.00 66.38  ? 214 PRO A O     1 
ATOM   1663 C  CB    . PRO A 1 214 ? 37.897 -13.171 5.305   1.00 63.76  ? 214 PRO A CB    1 
ATOM   1664 C  CG    . PRO A 1 214 ? 37.271 -14.532 5.353   1.00 59.67  ? 214 PRO A CG    1 
ATOM   1665 C  CD    . PRO A 1 214 ? 37.444 -15.095 3.979   1.00 61.02  ? 214 PRO A CD    1 
ATOM   1666 N  N     . GLU A 1 215 ? 39.824 -12.515 2.801   1.00 73.42  ? 215 GLU A N     1 
ATOM   1667 C  CA    . GLU A 1 215 ? 41.010 -11.799 2.338   1.00 77.58  ? 215 GLU A CA    1 
ATOM   1668 C  C     . GLU A 1 215 ? 40.686 -10.866 1.177   1.00 76.72  ? 215 GLU A C     1 
ATOM   1669 O  O     . GLU A 1 215 ? 41.142 -9.717  1.150   1.00 73.27  ? 215 GLU A O     1 
ATOM   1670 C  CB    . GLU A 1 215 ? 42.099 -12.794 1.936   1.00 81.24  ? 215 GLU A CB    1 
ATOM   1671 C  CG    . GLU A 1 215 ? 42.541 -13.738 3.047   1.00 94.18  ? 215 GLU A CG    1 
ATOM   1672 C  CD    . GLU A 1 215 ? 43.387 -13.054 4.110   1.00 102.23 ? 215 GLU A CD    1 
ATOM   1673 O  OE1   . GLU A 1 215 ? 42.872 -12.154 4.807   1.00 99.15  ? 215 GLU A OE1   1 
ATOM   1674 O  OE2   . GLU A 1 215 ? 44.574 -13.420 4.247   1.00 104.97 ? 215 GLU A OE2   1 
ATOM   1675 N  N     . LEU A 1 216 ? 39.900 -11.340 0.210   1.00 67.34  ? 216 LEU A N     1 
ATOM   1676 C  CA    . LEU A 1 216 ? 39.573 -10.571 -0.982  1.00 61.03  ? 216 LEU A CA    1 
ATOM   1677 C  C     . LEU A 1 216 ? 38.237 -9.850  -0.863  1.00 54.87  ? 216 LEU A C     1 
ATOM   1678 O  O     . LEU A 1 216 ? 37.676 -9.429  -1.881  1.00 53.83  ? 216 LEU A O     1 
ATOM   1679 C  CB    . LEU A 1 216 ? 39.570 -11.484 -2.209  1.00 56.65  ? 216 LEU A CB    1 
ATOM   1680 C  CG    . LEU A 1 216 ? 40.847 -12.295 -2.427  1.00 57.90  ? 216 LEU A CG    1 
ATOM   1681 C  CD1   . LEU A 1 216 ? 40.713 -13.191 -3.645  1.00 56.26  ? 216 LEU A CD1   1 
ATOM   1682 C  CD2   . LEU A 1 216 ? 42.046 -11.371 -2.564  1.00 57.70  ? 216 LEU A CD2   1 
ATOM   1683 N  N     . THR A 1 217 ? 37.718 -9.700  0.353   1.00 54.30  ? 217 THR A N     1 
ATOM   1684 C  CA    . THR A 1 217 ? 36.409 -9.087  0.539   1.00 55.00  ? 217 THR A CA    1 
ATOM   1685 C  C     . THR A 1 217 ? 36.423 -7.636  0.069   1.00 57.83  ? 217 THR A C     1 
ATOM   1686 O  O     . THR A 1 217 ? 37.320 -6.862  0.417   1.00 52.74  ? 217 THR A O     1 
ATOM   1687 C  CB    . THR A 1 217 ? 35.990 -9.173  2.007   1.00 53.88  ? 217 THR A CB    1 
ATOM   1688 O  OG1   . THR A 1 217 ? 35.668 -10.532 2.328   1.00 57.70  ? 217 THR A OG1   1 
ATOM   1689 C  CG2   . THR A 1 217 ? 34.778 -8.293  2.280   1.00 47.58  ? 217 THR A CG2   1 
ATOM   1690 N  N     . LEU A 1 218 ? 35.426 -7.275  -0.735  1.00 50.30  ? 218 LEU A N     1 
ATOM   1691 C  CA    . LEU A 1 218 ? 35.327 -5.929  -1.280  1.00 45.00  ? 218 LEU A CA    1 
ATOM   1692 C  C     . LEU A 1 218 ? 33.892 -5.692  -1.721  1.00 45.28  ? 218 LEU A C     1 
ATOM   1693 O  O     . LEU A 1 218 ? 33.312 -6.529  -2.420  1.00 45.24  ? 218 LEU A O     1 
ATOM   1694 C  CB    . LEU A 1 218 ? 36.293 -5.742  -2.456  1.00 51.37  ? 218 LEU A CB    1 
ATOM   1695 C  CG    . LEU A 1 218 ? 36.410 -4.337  -3.052  1.00 42.40  ? 218 LEU A CG    1 
ATOM   1696 C  CD1   . LEU A 1 218 ? 36.956 -3.362  -2.024  1.00 45.98  ? 218 LEU A CD1   1 
ATOM   1697 C  CD2   . LEU A 1 218 ? 37.293 -4.362  -4.289  1.00 43.95  ? 218 LEU A CD2   1 
ATOM   1698 N  N     . ILE A 1 219 ? 33.323 -4.566  -1.304  1.00 44.48  ? 219 ILE A N     1 
ATOM   1699 C  CA    . ILE A 1 219 ? 31.978 -4.165  -1.701  1.00 44.13  ? 219 ILE A CA    1 
ATOM   1700 C  C     . ILE A 1 219 ? 32.106 -2.813  -2.385  1.00 44.04  ? 219 ILE A C     1 
ATOM   1701 O  O     . ILE A 1 219 ? 32.457 -1.816  -1.741  1.00 43.55  ? 219 ILE A O     1 
ATOM   1702 C  CB    . ILE A 1 219 ? 31.009 -4.094  -0.512  1.00 38.72  ? 219 ILE A CB    1 
ATOM   1703 C  CG1   . ILE A 1 219 ? 30.967 -5.429  0.243   1.00 46.34  ? 219 ILE A CG1   1 
ATOM   1704 C  CG2   . ILE A 1 219 ? 29.617 -3.724  -0.995  1.00 40.24  ? 219 ILE A CG2   1 
ATOM   1705 C  CD1   . ILE A 1 219 ? 31.923 -5.509  1.421   1.00 44.45  ? 219 ILE A CD1   1 
ATOM   1706 N  N     . ALA A 1 220 ? 31.830 -2.775  -3.685  1.00 41.72  ? 220 ALA A N     1 
ATOM   1707 C  CA    . ALA A 1 220 ? 32.045 -1.584  -4.492  1.00 43.70  ? 220 ALA A CA    1 
ATOM   1708 C  C     . ALA A 1 220 ? 30.724 -1.027  -5.005  1.00 38.83  ? 220 ALA A C     1 
ATOM   1709 O  O     . ALA A 1 220 ? 29.766 -1.767  -5.247  1.00 38.04  ? 220 ALA A O     1 
ATOM   1710 C  CB    . ALA A 1 220 ? 32.973 -1.882  -5.674  1.00 42.48  ? 220 ALA A CB    1 
ATOM   1711 N  N     . HIS A 1 221 ? 30.689 0.293   -5.172  1.00 38.41  ? 221 HIS A N     1 
ATOM   1712 C  CA    . HIS A 1 221 ? 29.539 0.998   -5.718  1.00 38.58  ? 221 HIS A CA    1 
ATOM   1713 C  C     . HIS A 1 221 ? 30.011 1.887   -6.857  1.00 42.05  ? 221 HIS A C     1 
ATOM   1714 O  O     . HIS A 1 221 ? 31.010 2.601   -6.716  1.00 44.43  ? 221 HIS A O     1 
ATOM   1715 C  CB    . HIS A 1 221 ? 28.836 1.839   -4.648  1.00 36.95  ? 221 HIS A CB    1 
ATOM   1716 C  CG    . HIS A 1 221 ? 28.431 1.058   -3.438  1.00 41.63  ? 221 HIS A CG    1 
ATOM   1717 N  ND1   . HIS A 1 221 ? 29.326 0.689   -2.456  1.00 43.10  ? 221 HIS A ND1   1 
ATOM   1718 C  CD2   . HIS A 1 221 ? 27.230 0.562   -3.058  1.00 33.37  ? 221 HIS A CD2   1 
ATOM   1719 C  CE1   . HIS A 1 221 ? 28.691 0.008   -1.520  1.00 41.57  ? 221 HIS A CE1   1 
ATOM   1720 N  NE2   . HIS A 1 221 ? 27.418 -0.081  -1.860  1.00 42.95  ? 221 HIS A NE2   1 
ATOM   1721 N  N     . LEU A 1 222 ? 29.297 1.840   -7.980  1.00 43.18  ? 222 LEU A N     1 
ATOM   1722 C  CA    . LEU A 1 222 ? 29.613 2.644   -9.162  1.00 47.37  ? 222 LEU A CA    1 
ATOM   1723 C  C     . LEU A 1 222 ? 28.352 3.389   -9.579  1.00 48.00  ? 222 LEU A C     1 
ATOM   1724 O  O     . LEU A 1 222 ? 27.640 2.967   -10.501 1.00 49.89  ? 222 LEU A O     1 
ATOM   1725 C  CB    . LEU A 1 222 ? 30.153 1.776   -10.299 1.00 47.29  ? 222 LEU A CB    1 
ATOM   1726 C  CG    . LEU A 1 222 ? 31.485 1.052   -10.059 1.00 50.64  ? 222 LEU A CG    1 
ATOM   1727 C  CD1   . LEU A 1 222 ? 31.277 -0.286  -9.358  1.00 48.42  ? 222 LEU A CD1   1 
ATOM   1728 C  CD2   . LEU A 1 222 ? 32.244 0.863   -11.363 1.00 47.61  ? 222 LEU A CD2   1 
ATOM   1729 N  N     . PRO A 1 223 ? 28.046 4.509   -8.919  1.00 46.87  ? 223 PRO A N     1 
ATOM   1730 C  CA    . PRO A 1 223 ? 26.783 5.209   -9.209  1.00 51.19  ? 223 PRO A CA    1 
ATOM   1731 C  C     . PRO A 1 223 ? 26.674 5.712   -10.637 1.00 53.71  ? 223 PRO A C     1 
ATOM   1732 O  O     . PRO A 1 223 ? 25.572 5.696   -11.199 1.00 56.01  ? 223 PRO A O     1 
ATOM   1733 C  CB    . PRO A 1 223 ? 26.781 6.366   -8.199  1.00 48.91  ? 223 PRO A CB    1 
ATOM   1734 C  CG    . PRO A 1 223 ? 28.213 6.540   -7.801  1.00 47.93  ? 223 PRO A CG    1 
ATOM   1735 C  CD    . PRO A 1 223 ? 28.818 5.169   -7.852  1.00 49.02  ? 223 PRO A CD    1 
ATOM   1736 N  N     . ASP A 1 224 ? 27.778 6.159   -11.242 1.00 52.31  ? 224 ASP A N     1 
ATOM   1737 C  CA    . ASP A 1 224 ? 27.731 6.604   -12.632 1.00 63.61  ? 224 ASP A CA    1 
ATOM   1738 C  C     . ASP A 1 224 ? 27.320 5.476   -13.568 1.00 64.90  ? 224 ASP A C     1 
ATOM   1739 O  O     . ASP A 1 224 ? 26.668 5.722   -14.590 1.00 66.73  ? 224 ASP A O     1 
ATOM   1740 C  CB    . ASP A 1 224 ? 29.088 7.166   -13.059 1.00 65.94  ? 224 ASP A CB    1 
ATOM   1741 C  CG    . ASP A 1 224 ? 29.488 8.393   -12.270 1.00 67.00  ? 224 ASP A CG    1 
ATOM   1742 O  OD1   . ASP A 1 224 ? 28.588 9.131   -11.816 1.00 59.36  ? 224 ASP A OD1   1 
ATOM   1743 O  OD2   . ASP A 1 224 ? 30.706 8.622   -12.110 1.00 73.79  ? 224 ASP A OD2   1 
ATOM   1744 N  N     . ARG A 1 225 ? 27.693 4.241   -13.240 1.00 61.13  ? 225 ARG A N     1 
ATOM   1745 C  CA    . ARG A 1 225 ? 27.346 3.077   -14.040 1.00 62.68  ? 225 ARG A CA    1 
ATOM   1746 C  C     . ARG A 1 225 ? 26.162 2.305   -13.476 1.00 58.48  ? 225 ARG A C     1 
ATOM   1747 O  O     . ARG A 1 225 ? 25.746 1.312   -14.082 1.00 59.99  ? 225 ARG A O     1 
ATOM   1748 C  CB    . ARG A 1 225 ? 28.562 2.153   -14.170 1.00 61.41  ? 225 ARG A CB    1 
ATOM   1749 C  CG    . ARG A 1 225 ? 29.745 2.807   -14.873 1.00 72.92  ? 225 ARG A CG    1 
ATOM   1750 C  CD    . ARG A 1 225 ? 31.026 2.020   -14.669 1.00 76.01  ? 225 ARG A CD    1 
ATOM   1751 N  NE    . ARG A 1 225 ? 30.880 0.631   -15.086 1.00 79.58  ? 225 ARG A NE    1 
ATOM   1752 C  CZ    . ARG A 1 225 ? 31.075 0.196   -16.323 1.00 87.20  ? 225 ARG A CZ    1 
ATOM   1753 N  NH1   . ARG A 1 225 ? 31.428 1.019   -17.297 1.00 87.47  ? 225 ARG A NH1   1 
ATOM   1754 N  NH2   . ARG A 1 225 ? 30.910 -1.098  -16.589 1.00 87.32  ? 225 ARG A NH2   1 
ATOM   1755 N  N     . ARG A 1 226 ? 25.606 2.745   -12.344 1.00 53.58  ? 226 ARG A N     1 
ATOM   1756 C  CA    . ARG A 1 226 ? 24.470 2.081   -11.705 1.00 52.75  ? 226 ARG A CA    1 
ATOM   1757 C  C     . ARG A 1 226 ? 24.765 0.604   -11.454 1.00 49.75  ? 226 ARG A C     1 
ATOM   1758 O  O     . ARG A 1 226 ? 23.926 -0.268  -11.685 1.00 47.37  ? 226 ARG A O     1 
ATOM   1759 C  CB    . ARG A 1 226 ? 23.195 2.242   -12.535 1.00 59.55  ? 226 ARG A CB    1 
ATOM   1760 C  CG    . ARG A 1 226 ? 22.786 3.680   -12.813 1.00 68.77  ? 226 ARG A CG    1 
ATOM   1761 C  CD    . ARG A 1 226 ? 21.565 3.737   -13.732 1.00 77.05  ? 226 ARG A CD    1 
ATOM   1762 N  NE    . ARG A 1 226 ? 21.841 3.207   -15.064 1.00 77.06  ? 226 ARG A NE    1 
ATOM   1763 C  CZ    . ARG A 1 226 ? 21.538 1.979   -15.468 1.00 78.32  ? 226 ARG A CZ    1 
ATOM   1764 N  NH1   . ARG A 1 226 ? 20.931 1.116   -14.669 1.00 73.78  ? 226 ARG A NH1   1 
ATOM   1765 N  NH2   . ARG A 1 226 ? 21.854 1.607   -16.705 1.00 77.24  ? 226 ARG A NH2   1 
ATOM   1766 N  N     . GLU A 1 227 ? 25.976 0.320   -10.988 1.00 49.48  ? 227 GLU A N     1 
ATOM   1767 C  CA    . GLU A 1 227 ? 26.410 -1.043  -10.728 1.00 48.86  ? 227 GLU A CA    1 
ATOM   1768 C  C     . GLU A 1 227 ? 26.817 -1.189  -9.271  1.00 43.80  ? 227 GLU A C     1 
ATOM   1769 O  O     . GLU A 1 227 ? 27.444 -0.293  -8.698  1.00 45.96  ? 227 GLU A O     1 
ATOM   1770 C  CB    . GLU A 1 227 ? 27.584 -1.445  -11.630 1.00 52.42  ? 227 GLU A CB    1 
ATOM   1771 C  CG    . GLU A 1 227 ? 27.261 -1.469  -13.114 1.00 58.02  ? 227 GLU A CG    1 
ATOM   1772 C  CD    . GLU A 1 227 ? 28.407 -2.001  -13.951 1.00 55.84  ? 227 GLU A CD    1 
ATOM   1773 O  OE1   . GLU A 1 227 ? 29.352 -2.577  -13.372 1.00 53.69  ? 227 GLU A OE1   1 
ATOM   1774 O  OE2   . GLU A 1 227 ? 28.362 -1.842  -15.188 1.00 61.48  ? 227 GLU A OE2   1 
ATOM   1775 N  N     . ILE A 1 228 ? 26.453 -2.323  -8.680  1.00 42.28  ? 228 ILE A N     1 
ATOM   1776 C  CA    . ILE A 1 228 ? 26.899 -2.719  -7.351  1.00 42.61  ? 228 ILE A CA    1 
ATOM   1777 C  C     . ILE A 1 228 ? 27.646 -4.036  -7.509  1.00 43.03  ? 228 ILE A C     1 
ATOM   1778 O  O     . ILE A 1 228 ? 27.102 -5.001  -8.061  1.00 35.37  ? 228 ILE A O     1 
ATOM   1779 C  CB    . ILE A 1 228 ? 25.726 -2.860  -6.368  1.00 40.99  ? 228 ILE A CB    1 
ATOM   1780 C  CG1   . ILE A 1 228 ? 25.033 -1.511  -6.173  1.00 41.79  ? 228 ILE A CG1   1 
ATOM   1781 C  CG2   . ILE A 1 228 ? 26.206 -3.422  -5.038  1.00 41.08  ? 228 ILE A CG2   1 
ATOM   1782 C  CD1   . ILE A 1 228 ? 23.792 -1.576  -5.310  1.00 35.01  ? 228 ILE A CD1   1 
ATOM   1783 N  N     . ILE A 1 229 ? 28.895 -4.069  -7.047  1.00 39.29  ? 229 ILE A N     1 
ATOM   1784 C  CA    . ILE A 1 229 ? 29.777 -5.216  -7.234  1.00 39.99  ? 229 ILE A CA    1 
ATOM   1785 C  C     . ILE A 1 229 ? 30.357 -5.584  -5.873  1.00 41.28  ? 229 ILE A C     1 
ATOM   1786 O  O     . ILE A 1 229 ? 31.168 -4.833  -5.318  1.00 42.25  ? 229 ILE A O     1 
ATOM   1787 C  CB    . ILE A 1 229 ? 30.891 -4.924  -8.251  1.00 41.51  ? 229 ILE A CB    1 
ATOM   1788 C  CG1   . ILE A 1 229 ? 30.285 -4.516  -9.597  1.00 38.91  ? 229 ILE A CG1   1 
ATOM   1789 C  CG2   . ILE A 1 229 ? 31.779 -6.135  -8.445  1.00 39.45  ? 229 ILE A CG2   1 
ATOM   1790 C  CD1   . ILE A 1 229 ? 31.307 -4.121  -10.641 1.00 45.07  ? 229 ILE A CD1   1 
ATOM   1791 N  N     . SER A 1 230 ? 29.943 -6.733  -5.336  1.00 39.74  ? 230 SER A N     1 
ATOM   1792 C  CA    . SER A 1 230 ? 30.359 -7.193  -4.015  1.00 41.94  ? 230 SER A CA    1 
ATOM   1793 C  C     . SER A 1 230 ? 30.951 -8.593  -4.110  1.00 41.03  ? 230 SER A C     1 
ATOM   1794 O  O     . SER A 1 230 ? 30.433 -9.448  -4.835  1.00 38.93  ? 230 SER A O     1 
ATOM   1795 C  CB    . SER A 1 230 ? 29.184 -7.193  -3.031  1.00 38.58  ? 230 SER A CB    1 
ATOM   1796 O  OG    . SER A 1 230 ? 29.582 -7.707  -1.772  1.00 44.08  ? 230 SER A OG    1 
ATOM   1797 N  N     . PHE A 1 231 ? 32.024 -8.828  -3.355  1.00 46.29  ? 231 PHE A N     1 
ATOM   1798 C  CA    . PHE A 1 231 ? 32.806 -10.050 -3.495  1.00 44.39  ? 231 PHE A CA    1 
ATOM   1799 C  C     . PHE A 1 231 ? 33.323 -10.514 -2.139  1.00 46.91  ? 231 PHE A C     1 
ATOM   1800 O  O     . PHE A 1 231 ? 33.876 -9.717  -1.377  1.00 46.16  ? 231 PHE A O     1 
ATOM   1801 C  CB    . PHE A 1 231 ? 33.980 -9.821  -4.455  1.00 44.75  ? 231 PHE A CB    1 
ATOM   1802 C  CG    . PHE A 1 231 ? 34.824 -11.043 -4.706  1.00 44.25  ? 231 PHE A CG    1 
ATOM   1803 C  CD1   . PHE A 1 231 ? 34.508 -11.920 -5.729  1.00 48.37  ? 231 PHE A CD1   1 
ATOM   1804 C  CD2   . PHE A 1 231 ? 35.951 -11.294 -3.940  1.00 45.62  ? 231 PHE A CD2   1 
ATOM   1805 C  CE1   . PHE A 1 231 ? 35.289 -13.037 -5.973  1.00 50.05  ? 231 PHE A CE1   1 
ATOM   1806 C  CE2   . PHE A 1 231 ? 36.735 -12.407 -4.177  1.00 49.56  ? 231 PHE A CE2   1 
ATOM   1807 C  CZ    . PHE A 1 231 ? 36.405 -13.280 -5.196  1.00 48.31  ? 231 PHE A CZ    1 
ATOM   1808 N  N     . GLY A 1 232 ? 33.146 -11.802 -1.853  1.00 46.64  ? 232 GLY A N     1 
ATOM   1809 C  CA    . GLY A 1 232 ? 33.838 -12.449 -0.757  1.00 50.36  ? 232 GLY A CA    1 
ATOM   1810 C  C     . GLY A 1 232 ? 33.115 -12.494 0.570   1.00 52.92  ? 232 GLY A C     1 
ATOM   1811 O  O     . GLY A 1 232 ? 33.701 -12.961 1.554   1.00 55.43  ? 232 GLY A O     1 
ATOM   1812 N  N     . SER A 1 233 ? 31.868 -12.037 0.637   1.00 48.63  ? 233 SER A N     1 
ATOM   1813 C  CA    . SER A 1 233 ? 31.134 -12.020 1.893   1.00 46.38  ? 233 SER A CA    1 
ATOM   1814 C  C     . SER A 1 233 ? 29.723 -12.547 1.679   1.00 52.18  ? 233 SER A C     1 
ATOM   1815 O  O     . SER A 1 233 ? 29.104 -12.306 0.639   1.00 49.67  ? 233 SER A O     1 
ATOM   1816 C  CB    . SER A 1 233 ? 31.080 -10.612 2.493   1.00 49.52  ? 233 SER A CB    1 
ATOM   1817 O  OG    . SER A 1 233 ? 30.293 -10.595 3.670   1.00 46.71  ? 233 SER A OG    1 
ATOM   1818 N  N     . GLY A 1 234 ? 29.220 -13.271 2.681   1.00 53.44  ? 234 GLY A N     1 
ATOM   1819 C  CA    . GLY A 1 234 ? 27.870 -13.799 2.644   1.00 43.72  ? 234 GLY A CA    1 
ATOM   1820 C  C     . GLY A 1 234 ? 26.909 -13.067 3.559   1.00 49.08  ? 234 GLY A C     1 
ATOM   1821 O  O     . GLY A 1 234 ? 25.690 -13.204 3.413   1.00 49.90  ? 234 GLY A O     1 
ATOM   1822 N  N     . TYR A 1 235 ? 27.445 -12.284 4.497   1.00 54.72  ? 235 TYR A N     1 
ATOM   1823 C  CA    . TYR A 1 235 ? 26.616 -11.554 5.450   1.00 56.25  ? 235 TYR A CA    1 
ATOM   1824 C  C     . TYR A 1 235 ? 25.643 -10.625 4.732   1.00 57.83  ? 235 TYR A C     1 
ATOM   1825 O  O     . TYR A 1 235 ? 25.957 -10.041 3.689   1.00 57.92  ? 235 TYR A O     1 
ATOM   1826 C  CB    . TYR A 1 235 ? 27.491 -10.751 6.418   1.00 58.06  ? 235 TYR A CB    1 
ATOM   1827 C  CG    . TYR A 1 235 ? 26.727 -9.788  7.313   1.00 61.72  ? 235 TYR A CG    1 
ATOM   1828 C  CD1   . TYR A 1 235 ? 25.995 -10.249 8.405   1.00 58.94  ? 235 TYR A CD1   1 
ATOM   1829 C  CD2   . TYR A 1 235 ? 26.754 -8.414  7.074   1.00 61.25  ? 235 TYR A CD2   1 
ATOM   1830 C  CE1   . TYR A 1 235 ? 25.299 -9.371  9.226   1.00 59.45  ? 235 TYR A CE1   1 
ATOM   1831 C  CE2   . TYR A 1 235 ? 26.062 -7.525  7.889   1.00 58.67  ? 235 TYR A CE2   1 
ATOM   1832 C  CZ    . TYR A 1 235 ? 25.336 -8.008  8.963   1.00 61.27  ? 235 TYR A CZ    1 
ATOM   1833 O  OH    . TYR A 1 235 ? 24.647 -7.132  9.774   1.00 56.59  ? 235 TYR A OH    1 
ATOM   1834 N  N     . GLY A 1 236 ? 24.455 -10.477 5.324   1.00 52.36  ? 236 GLY A N     1 
ATOM   1835 C  CA    . GLY A 1 236 ? 23.368 -9.784  4.649   1.00 51.36  ? 236 GLY A CA    1 
ATOM   1836 C  C     . GLY A 1 236 ? 23.715 -8.368  4.233   1.00 48.14  ? 236 GLY A C     1 
ATOM   1837 O  O     . GLY A 1 236 ? 23.297 -7.906  3.170   1.00 49.28  ? 236 GLY A O     1 
ATOM   1838 N  N     . GLY A 1 237 ? 24.479 -7.656  5.065   1.00 49.30  ? 237 GLY A N     1 
ATOM   1839 C  CA    . GLY A 1 237 ? 24.849 -6.292  4.729   1.00 47.69  ? 237 GLY A CA    1 
ATOM   1840 C  C     . GLY A 1 237 ? 25.742 -6.194  3.508   1.00 52.70  ? 237 GLY A C     1 
ATOM   1841 O  O     . GLY A 1 237 ? 25.720 -5.183  2.800   1.00 49.67  ? 237 GLY A O     1 
ATOM   1842 N  N     . ASN A 1 238 ? 26.531 -7.236  3.239   1.00 50.23  ? 238 ASN A N     1 
ATOM   1843 C  CA    . ASN A 1 238 ? 27.439 -7.247  2.101   1.00 47.43  ? 238 ASN A CA    1 
ATOM   1844 C  C     . ASN A 1 238 ? 26.890 -7.995  0.896   1.00 47.76  ? 238 ASN A C     1 
ATOM   1845 O  O     . ASN A 1 238 ? 27.374 -7.776  -0.218  1.00 49.87  ? 238 ASN A O     1 
ATOM   1846 C  CB    . ASN A 1 238 ? 28.782 -7.879  2.490   1.00 44.65  ? 238 ASN A CB    1 
ATOM   1847 C  CG    . ASN A 1 238 ? 29.373 -7.275  3.746   1.00 47.57  ? 238 ASN A CG    1 
ATOM   1848 O  OD1   . ASN A 1 238 ? 29.219 -6.083  4.008   1.00 53.58  ? 238 ASN A OD1   1 
ATOM   1849 N  ND2   . ASN A 1 238 ? 30.055 -8.099  4.533   1.00 48.66  ? 238 ASN A ND2   1 
ATOM   1850 N  N     . SER A 1 239 ? 25.903 -8.869  1.087   1.00 46.87  ? 239 SER A N     1 
ATOM   1851 C  CA    . SER A 1 239 ? 25.425 -9.742  0.024   1.00 43.97  ? 239 SER A CA    1 
ATOM   1852 C  C     . SER A 1 239 ? 24.011 -9.434  -0.435  1.00 42.33  ? 239 SER A C     1 
ATOM   1853 O  O     . SER A 1 239 ? 23.681 -9.706  -1.590  1.00 41.61  ? 239 SER A O     1 
ATOM   1854 C  CB    . SER A 1 239 ? 25.488 -11.205 0.476   1.00 41.98  ? 239 SER A CB    1 
ATOM   1855 O  OG    . SER A 1 239 ? 24.581 -11.440 1.540   1.00 43.58  ? 239 SER A OG    1 
ATOM   1856 N  N     . LEU A 1 240 ? 23.167 -8.893  0.440   1.00 44.18  ? 240 LEU A N     1 
ATOM   1857 C  CA    . LEU A 1 240 ? 21.821 -8.461  0.066   1.00 44.07  ? 240 LEU A CA    1 
ATOM   1858 C  C     . LEU A 1 240 ? 21.946 -7.047  -0.476  1.00 39.30  ? 240 LEU A C     1 
ATOM   1859 O  O     . LEU A 1 240 ? 21.785 -6.062  0.246   1.00 44.19  ? 240 LEU A O     1 
ATOM   1860 C  CB    . LEU A 1 240 ? 20.874 -8.533  1.257   1.00 46.92  ? 240 LEU A CB    1 
ATOM   1861 C  CG    . LEU A 1 240 ? 20.819 -9.888  1.968   1.00 37.84  ? 240 LEU A CG    1 
ATOM   1862 C  CD1   . LEU A 1 240 ? 19.758 -9.876  3.052   1.00 37.64  ? 240 LEU A CD1   1 
ATOM   1863 C  CD2   . LEU A 1 240 ? 20.561 -10.996 0.967   1.00 39.56  ? 240 LEU A CD2   1 
ATOM   1864 N  N     . LEU A 1 241 ? 22.236 -6.953  -1.775  1.00 40.16  ? 241 LEU A N     1 
ATOM   1865 C  CA    . LEU A 1 241 ? 22.693 -5.700  -2.361  1.00 41.77  ? 241 LEU A CA    1 
ATOM   1866 C  C     . LEU A 1 241 ? 21.588 -4.660  -2.486  1.00 39.46  ? 241 LEU A C     1 
ATOM   1867 O  O     . LEU A 1 241 ? 21.891 -3.468  -2.607  1.00 42.66  ? 241 LEU A O     1 
ATOM   1868 C  CB    . LEU A 1 241 ? 23.327 -5.977  -3.724  1.00 35.95  ? 241 LEU A CB    1 
ATOM   1869 C  CG    . LEU A 1 241 ? 24.562 -6.872  -3.618  1.00 37.85  ? 241 LEU A CG    1 
ATOM   1870 C  CD1   . LEU A 1 241 ? 25.222 -7.099  -4.977  1.00 35.78  ? 241 LEU A CD1   1 
ATOM   1871 C  CD2   . LEU A 1 241 ? 25.553 -6.283  -2.629  1.00 37.13  ? 241 LEU A CD2   1 
ATOM   1872 N  N     . GLY A 1 242 ? 20.328 -5.066  -2.454  1.00 41.11  ? 242 GLY A N     1 
ATOM   1873 C  CA    . GLY A 1 242 ? 19.277 -4.074  -2.507  1.00 40.34  ? 242 GLY A CA    1 
ATOM   1874 C  C     . GLY A 1 242 ? 19.015 -3.321  -1.222  1.00 41.10  ? 242 GLY A C     1 
ATOM   1875 O  O     . GLY A 1 242 ? 18.138 -2.456  -1.195  1.00 44.98  ? 242 GLY A O     1 
ATOM   1876 N  N     . LYS A 1 243 ? 19.751 -3.606  -0.149  1.00 38.19  ? 243 LYS A N     1 
ATOM   1877 C  CA    . LYS A 1 243 ? 19.442 -3.022  1.152   1.00 38.51  ? 243 LYS A CA    1 
ATOM   1878 C  C     . LYS A 1 243 ? 20.314 -1.801  1.432   1.00 42.25  ? 243 LYS A C     1 
ATOM   1879 O  O     . LYS A 1 243 ? 19.896 -0.664  1.187   1.00 42.03  ? 243 LYS A O     1 
ATOM   1880 C  CB    . LYS A 1 243 ? 19.603 -4.078  2.252   1.00 38.36  ? 243 LYS A CB    1 
ATOM   1881 C  CG    . LYS A 1 243 ? 19.243 -3.613  3.661   1.00 43.00  ? 243 LYS A CG    1 
ATOM   1882 C  CD    . LYS A 1 243 ? 19.215 -4.790  4.643   1.00 31.53  ? 243 LYS A CD    1 
ATOM   1883 C  CE    . LYS A 1 243 ? 18.980 -4.327  6.070   1.00 36.91  ? 243 LYS A CE    1 
ATOM   1884 N  NZ    . LYS A 1 243 ? 17.784 -3.439  6.191   1.00 34.84  ? 243 LYS A NZ    1 
ATOM   1885 N  N     . LYS A 1 244 ? 21.525 -2.022  1.948   1.00 39.72  ? 244 LYS A N     1 
ATOM   1886 C  CA    . LYS A 1 244 ? 22.432 -0.910  2.205   1.00 36.00  ? 244 LYS A CA    1 
ATOM   1887 C  C     . LYS A 1 244 ? 23.074 -0.405  0.918   1.00 39.85  ? 244 LYS A C     1 
ATOM   1888 O  O     . LYS A 1 244 ? 23.170 0.808   0.703   1.00 39.38  ? 244 LYS A O     1 
ATOM   1889 C  CB    . LYS A 1 244 ? 23.508 -1.329  3.207   1.00 37.82  ? 244 LYS A CB    1 
ATOM   1890 C  CG    . LYS A 1 244 ? 22.962 -1.830  4.540   1.00 41.08  ? 244 LYS A CG    1 
ATOM   1891 C  CD    . LYS A 1 244 ? 22.177 -0.742  5.260   1.00 41.91  ? 244 LYS A CD    1 
ATOM   1892 C  CE    . LYS A 1 244 ? 21.698 -1.204  6.629   1.00 36.42  ? 244 LYS A CE    1 
ATOM   1893 N  NZ    . LYS A 1 244 ? 21.046 -0.096  7.396   1.00 35.04  ? 244 LYS A NZ    1 
ATOM   1894 N  N     . CYS A 1 245 ? 23.501 -1.321  0.049   1.00 39.40  ? 245 CYS A N     1 
ATOM   1895 C  CA    . CYS A 1 245 ? 24.227 -0.929  -1.154  1.00 38.24  ? 245 CYS A CA    1 
ATOM   1896 C  C     . CYS A 1 245 ? 23.345 -0.123  -2.099  1.00 39.53  ? 245 CYS A C     1 
ATOM   1897 O  O     . CYS A 1 245 ? 23.757 0.927   -2.603  1.00 40.62  ? 245 CYS A O     1 
ATOM   1898 C  CB    . CYS A 1 245 ? 24.779 -2.171  -1.854  1.00 37.86  ? 245 CYS A CB    1 
ATOM   1899 S  SG    . CYS A 1 245 ? 25.984 -3.093  -0.878  1.00 38.54  ? 245 CYS A SG    1 
ATOM   1900 N  N     . PHE A 1 246 ? 22.123 -0.593  -2.345  1.00 38.51  ? 246 PHE A N     1 
ATOM   1901 C  CA    . PHE A 1 246 ? 21.228 0.078   -3.283  1.00 40.67  ? 246 PHE A CA    1 
ATOM   1902 C  C     . PHE A 1 246 ? 20.358 1.129   -2.593  1.00 41.89  ? 246 PHE A C     1 
ATOM   1903 O  O     . PHE A 1 246 ? 20.425 2.315   -2.930  1.00 42.95  ? 246 PHE A O     1 
ATOM   1904 C  CB    . PHE A 1 246 ? 20.356 -0.960  -3.999  1.00 37.58  ? 246 PHE A CB    1 
ATOM   1905 C  CG    . PHE A 1 246 ? 19.373 -0.367  -4.969  1.00 42.35  ? 246 PHE A CG    1 
ATOM   1906 C  CD1   . PHE A 1 246 ? 19.620 0.853   -5.580  1.00 49.52  ? 246 PHE A CD1   1 
ATOM   1907 C  CD2   . PHE A 1 246 ? 18.198 -1.033  -5.269  1.00 49.52  ? 246 PHE A CD2   1 
ATOM   1908 C  CE1   . PHE A 1 246 ? 18.712 1.399   -6.463  1.00 56.91  ? 246 PHE A CE1   1 
ATOM   1909 C  CE2   . PHE A 1 246 ? 17.284 -0.493  -6.151  1.00 50.50  ? 246 PHE A CE2   1 
ATOM   1910 C  CZ    . PHE A 1 246 ? 17.541 0.725   -6.748  1.00 57.71  ? 246 PHE A CZ    1 
ATOM   1911 N  N     . ALA A 1 247 ? 19.530 0.707   -1.635  1.00 40.66  ? 247 ALA A N     1 
ATOM   1912 C  CA    . ALA A 1 247 ? 18.496 1.580   -1.090  1.00 42.56  ? 247 ALA A CA    1 
ATOM   1913 C  C     . ALA A 1 247 ? 19.057 2.746   -0.287  1.00 39.90  ? 247 ALA A C     1 
ATOM   1914 O  O     . ALA A 1 247 ? 18.326 3.713   -0.052  1.00 37.74  ? 247 ALA A O     1 
ATOM   1915 C  CB    . ALA A 1 247 ? 17.529 0.771   -0.221  1.00 41.90  ? 247 ALA A CB    1 
ATOM   1916 N  N     . LEU A 1 248 ? 20.321 2.688   0.131   1.00 39.38  ? 248 LEU A N     1 
ATOM   1917 C  CA    . LEU A 1 248 ? 20.959 3.805   0.821   1.00 36.09  ? 248 LEU A CA    1 
ATOM   1918 C  C     . LEU A 1 248 ? 22.069 4.438   -0.008  1.00 44.48  ? 248 LEU A C     1 
ATOM   1919 O  O     . LEU A 1 248 ? 21.964 5.614   -0.368  1.00 41.80  ? 248 LEU A O     1 
ATOM   1920 C  CB    . LEU A 1 248 ? 21.496 3.352   2.186   1.00 33.82  ? 248 LEU A CB    1 
ATOM   1921 C  CG    . LEU A 1 248 ? 20.443 3.095   3.271   1.00 40.52  ? 248 LEU A CG    1 
ATOM   1922 C  CD1   . LEU A 1 248 ? 21.093 2.778   4.612   1.00 36.93  ? 248 LEU A CD1   1 
ATOM   1923 C  CD2   . LEU A 1 248 ? 19.496 4.280   3.403   1.00 32.95  ? 248 LEU A CD2   1 
ATOM   1924 N  N     . ARG A 1 249 ? 23.132 3.699   -0.337  1.00 41.61  ? 249 ARG A N     1 
ATOM   1925 C  CA    . ARG A 1 249 ? 24.295 4.331   -0.955  1.00 41.76  ? 249 ARG A CA    1 
ATOM   1926 C  C     . ARG A 1 249 ? 24.002 4.770   -2.387  1.00 39.31  ? 249 ARG A C     1 
ATOM   1927 O  O     . ARG A 1 249 ? 24.223 5.931   -2.747  1.00 40.79  ? 249 ARG A O     1 
ATOM   1928 C  CB    . ARG A 1 249 ? 25.495 3.386   -0.909  1.00 40.87  ? 249 ARG A CB    1 
ATOM   1929 C  CG    . ARG A 1 249 ? 25.891 2.976   0.498   1.00 41.15  ? 249 ARG A CG    1 
ATOM   1930 C  CD    . ARG A 1 249 ? 27.325 2.468   0.562   1.00 39.14  ? 249 ARG A CD    1 
ATOM   1931 N  NE    . ARG A 1 249 ? 27.650 1.989   1.900   1.00 44.02  ? 249 ARG A NE    1 
ATOM   1932 C  CZ    . ARG A 1 249 ? 27.510 0.730   2.295   1.00 44.59  ? 249 ARG A CZ    1 
ATOM   1933 N  NH1   . ARG A 1 249 ? 27.097 -0.213  1.463   1.00 36.98  ? 249 ARG A NH1   1 
ATOM   1934 N  NH2   . ARG A 1 249 ? 27.795 0.411   3.556   1.00 41.92  ? 249 ARG A NH2   1 
ATOM   1935 N  N     . ILE A 1 250 ? 23.512 3.855   -3.223  1.00 42.23  ? 250 ILE A N     1 
ATOM   1936 C  CA    . ILE A 1 250 ? 23.186 4.224   -4.596  1.00 41.28  ? 250 ILE A CA    1 
ATOM   1937 C  C     . ILE A 1 250 ? 21.968 5.138   -4.629  1.00 41.43  ? 250 ILE A C     1 
ATOM   1938 O  O     . ILE A 1 250 ? 21.915 6.097   -5.408  1.00 43.99  ? 250 ILE A O     1 
ATOM   1939 C  CB    . ILE A 1 250 ? 22.973 2.962   -5.453  1.00 47.22  ? 250 ILE A CB    1 
ATOM   1940 C  CG1   . ILE A 1 250 ? 24.275 2.169   -5.563  1.00 44.55  ? 250 ILE A CG1   1 
ATOM   1941 C  CG2   . ILE A 1 250 ? 22.470 3.330   -6.841  1.00 42.27  ? 250 ILE A CG2   1 
ATOM   1942 C  CD1   . ILE A 1 250 ? 25.375 2.910   -6.285  1.00 38.78  ? 250 ILE A CD1   1 
ATOM   1943 N  N     . ALA A 1 251 ? 20.976 4.867   -3.777  1.00 46.40  ? 251 ALA A N     1 
ATOM   1944 C  CA    . ALA A 1 251 ? 19.740 5.642   -3.813  1.00 44.77  ? 251 ALA A CA    1 
ATOM   1945 C  C     . ALA A 1 251 ? 19.943 7.072   -3.329  1.00 38.87  ? 251 ALA A C     1 
ATOM   1946 O  O     . ALA A 1 251 ? 19.236 7.978   -3.782  1.00 37.04  ? 251 ALA A O     1 
ATOM   1947 C  CB    . ALA A 1 251 ? 18.659 4.955   -2.981  1.00 38.92  ? 251 ALA A CB    1 
ATOM   1948 N  N     . SER A 1 252 ? 20.886 7.298   -2.411  1.00 37.54  ? 252 SER A N     1 
ATOM   1949 C  CA    . SER A 1 252 ? 21.095 8.651   -1.906  1.00 41.20  ? 252 SER A CA    1 
ATOM   1950 C  C     . SER A 1 252 ? 21.592 9.574   -3.010  1.00 45.66  ? 252 SER A C     1 
ATOM   1951 O  O     . SER A 1 252 ? 21.194 10.743  -3.076  1.00 38.65  ? 252 SER A O     1 
ATOM   1952 C  CB    . SER A 1 252 ? 22.073 8.641   -0.731  1.00 37.27  ? 252 SER A CB    1 
ATOM   1953 O  OG    . SER A 1 252 ? 23.322 8.082   -1.104  1.00 42.90  ? 252 SER A OG    1 
ATOM   1954 N  N     . ARG A 1 253 ? 22.454 9.064   -3.895  1.00 43.18  ? 253 ARG A N     1 
ATOM   1955 C  CA    . ARG A 1 253 ? 22.920 9.879   -5.011  1.00 42.62  ? 253 ARG A CA    1 
ATOM   1956 C  C     . ARG A 1 253 ? 21.808 10.112  -6.025  1.00 44.06  ? 253 ARG A C     1 
ATOM   1957 O  O     . ARG A 1 253 ? 21.635 11.235  -6.516  1.00 45.36  ? 253 ARG A O     1 
ATOM   1958 C  CB    . ARG A 1 253 ? 24.132 9.230   -5.675  1.00 42.73  ? 253 ARG A CB    1 
ATOM   1959 C  CG    . ARG A 1 253 ? 24.571 9.944   -6.944  1.00 52.16  ? 253 ARG A CG    1 
ATOM   1960 C  CD    . ARG A 1 253 ? 26.051 9.781   -7.190  1.00 52.30  ? 253 ARG A CD    1 
ATOM   1961 N  NE    . ARG A 1 253 ? 26.431 10.275  -8.507  1.00 61.10  ? 253 ARG A NE    1 
ATOM   1962 C  CZ    . ARG A 1 253 ? 27.683 10.412  -8.919  1.00 58.55  ? 253 ARG A CZ    1 
ATOM   1963 N  NH1   . ARG A 1 253 ? 28.704 10.122  -8.130  1.00 59.73  ? 253 ARG A NH1   1 
ATOM   1964 N  NH2   . ARG A 1 253 ? 27.915 10.854  -10.151 1.00 75.53  ? 253 ARG A NH2   1 
ATOM   1965 N  N     . LEU A 1 254 ? 21.045 9.067   -6.352  1.00 42.79  ? 254 LEU A N     1 
ATOM   1966 C  CA    . LEU A 1 254 ? 19.887 9.245   -7.221  1.00 45.38  ? 254 LEU A CA    1 
ATOM   1967 C  C     . LEU A 1 254 ? 18.889 10.217  -6.610  1.00 49.99  ? 254 LEU A C     1 
ATOM   1968 O  O     . LEU A 1 254 ? 18.299 11.041  -7.320  1.00 48.05  ? 254 LEU A O     1 
ATOM   1969 C  CB    . LEU A 1 254 ? 19.216 7.900   -7.489  1.00 49.43  ? 254 LEU A CB    1 
ATOM   1970 C  CG    . LEU A 1 254 ? 20.031 6.873   -8.270  1.00 52.54  ? 254 LEU A CG    1 
ATOM   1971 C  CD1   . LEU A 1 254 ? 19.252 5.575   -8.393  1.00 54.90  ? 254 LEU A CD1   1 
ATOM   1972 C  CD2   . LEU A 1 254 ? 20.386 7.420   -9.639  1.00 51.89  ? 254 LEU A CD2   1 
ATOM   1973 N  N     . ALA A 1 255 ? 18.686 10.134  -5.292  1.00 43.67  ? 255 ALA A N     1 
ATOM   1974 C  CA    . ALA A 1 255 ? 17.771 11.050  -4.623  1.00 42.95  ? 255 ALA A CA    1 
ATOM   1975 C  C     . ALA A 1 255 ? 18.256 12.489  -4.734  1.00 45.53  ? 255 ALA A C     1 
ATOM   1976 O  O     . ALA A 1 255 ? 17.457 13.403  -4.970  1.00 46.24  ? 255 ALA A O     1 
ATOM   1977 C  CB    . ALA A 1 255 ? 17.605 10.649  -3.158  1.00 44.37  ? 255 ALA A CB    1 
ATOM   1978 N  N     . LYS A 1 256 ? 19.563 12.708  -4.569  1.00 45.01  ? 256 LYS A N     1 
ATOM   1979 C  CA    . LYS A 1 256 ? 20.116 14.052  -4.704  1.00 45.47  ? 256 LYS A CA    1 
ATOM   1980 C  C     . LYS A 1 256 ? 19.912 14.593  -6.113  1.00 49.50  ? 256 LYS A C     1 
ATOM   1981 O  O     . LYS A 1 256 ? 19.570 15.767  -6.292  1.00 48.25  ? 256 LYS A O     1 
ATOM   1982 C  CB    . LYS A 1 256 ? 21.600 14.041  -4.337  1.00 45.85  ? 256 LYS A CB    1 
ATOM   1983 C  CG    . LYS A 1 256 ? 22.363 15.291  -4.748  1.00 48.06  ? 256 LYS A CG    1 
ATOM   1984 C  CD    . LYS A 1 256 ? 23.561 14.930  -5.625  1.00 55.59  ? 256 LYS A CD    1 
ATOM   1985 C  CE    . LYS A 1 256 ? 24.312 16.170  -6.103  1.00 57.30  ? 256 LYS A CE    1 
ATOM   1986 N  NZ    . LYS A 1 256 ? 25.451 15.817  -6.997  1.00 59.15  ? 256 LYS A NZ    1 
ATOM   1987 N  N     . GLU A 1 257 ? 20.100 13.744  -7.127  1.00 53.59  ? 257 GLU A N     1 
ATOM   1988 C  CA    . GLU A 1 257 ? 19.921 14.180  -8.508  1.00 54.17  ? 257 GLU A CA    1 
ATOM   1989 C  C     . GLU A 1 257 ? 18.456 14.463  -8.822  1.00 53.74  ? 257 GLU A C     1 
ATOM   1990 O  O     . GLU A 1 257 ? 18.142 15.449  -9.499  1.00 57.53  ? 257 GLU A O     1 
ATOM   1991 C  CB    . GLU A 1 257 ? 20.472 13.124  -9.467  1.00 56.83  ? 257 GLU A CB    1 
ATOM   1992 C  CG    . GLU A 1 257 ? 21.962 12.863  -9.327  1.00 57.81  ? 257 GLU A CG    1 
ATOM   1993 C  CD    . GLU A 1 257 ? 22.427 11.678  -10.152 1.00 63.36  ? 257 GLU A CD    1 
ATOM   1994 O  OE1   . GLU A 1 257 ? 21.574 11.025  -10.791 1.00 61.17  ? 257 GLU A OE1   1 
ATOM   1995 O  OE2   . GLU A 1 257 ? 23.646 11.399  -10.158 1.00 66.78  ? 257 GLU A OE2   1 
ATOM   1996 N  N     . GLU A 1 258 ? 17.546 13.611  -8.346  1.00 50.17  ? 258 GLU A N     1 
ATOM   1997 C  CA    . GLU A 1 258 ? 16.134 13.724  -8.691  1.00 51.59  ? 258 GLU A CA    1 
ATOM   1998 C  C     . GLU A 1 258 ? 15.338 14.577  -7.710  1.00 52.02  ? 258 GLU A C     1 
ATOM   1999 O  O     . GLU A 1 258 ? 14.203 14.957  -8.022  1.00 51.28  ? 258 GLU A O     1 
ATOM   2000 C  CB    . GLU A 1 258 ? 15.501 12.330  -8.781  1.00 51.76  ? 258 GLU A CB    1 
ATOM   2001 C  CG    . GLU A 1 258 ? 16.216 11.366  -9.720  1.00 53.65  ? 258 GLU A CG    1 
ATOM   2002 C  CD    . GLU A 1 258 ? 15.757 9.927   -9.543  1.00 61.17  ? 258 GLU A CD    1 
ATOM   2003 O  OE1   . GLU A 1 258 ? 14.625 9.714   -9.055  1.00 61.63  ? 258 GLU A OE1   1 
ATOM   2004 O  OE2   . GLU A 1 258 ? 16.532 9.005   -9.882  1.00 65.64  ? 258 GLU A OE2   1 
ATOM   2005 N  N     . GLY A 1 259 ? 15.889 14.879  -6.536  1.00 52.02  ? 259 GLY A N     1 
ATOM   2006 C  CA    . GLY A 1 259 ? 15.225 15.773  -5.606  1.00 50.98  ? 259 GLY A CA    1 
ATOM   2007 C  C     . GLY A 1 259 ? 14.381 15.092  -4.547  1.00 50.32  ? 259 GLY A C     1 
ATOM   2008 O  O     . GLY A 1 259 ? 13.323 15.603  -4.172  1.00 50.45  ? 259 GLY A O     1 
ATOM   2009 N  N     . TRP A 1 260 ? 14.828 13.942  -4.056  1.00 49.48  ? 260 TRP A N     1 
ATOM   2010 C  CA    . TRP A 1 260 ? 14.143 13.257  -2.967  1.00 46.00  ? 260 TRP A CA    1 
ATOM   2011 C  C     . TRP A 1 260 ? 15.199 12.817  -1.955  1.00 37.85  ? 260 TRP A C     1 
ATOM   2012 O  O     . TRP A 1 260 ? 16.340 13.293  -1.954  1.00 44.20  ? 260 TRP A O     1 
ATOM   2013 C  CB    . TRP A 1 260 ? 13.272 12.109  -3.497  1.00 48.90  ? 260 TRP A CB    1 
ATOM   2014 C  CG    . TRP A 1 260 ? 13.946 11.152  -4.442  1.00 51.90  ? 260 TRP A CG    1 
ATOM   2015 C  CD1   . TRP A 1 260 ? 14.262 11.375  -5.751  1.00 55.17  ? 260 TRP A CD1   1 
ATOM   2016 C  CD2   . TRP A 1 260 ? 14.341 9.803   -4.160  1.00 46.00  ? 260 TRP A CD2   1 
ATOM   2017 N  NE1   . TRP A 1 260 ? 14.847 10.257  -6.295  1.00 48.38  ? 260 TRP A NE1   1 
ATOM   2018 C  CE2   . TRP A 1 260 ? 14.906 9.277   -5.340  1.00 50.08  ? 260 TRP A CE2   1 
ATOM   2019 C  CE3   . TRP A 1 260 ? 14.281 8.993   -3.023  1.00 41.81  ? 260 TRP A CE3   1 
ATOM   2020 C  CZ2   . TRP A 1 260 ? 15.409 7.981   -5.413  1.00 49.10  ? 260 TRP A CZ2   1 
ATOM   2021 C  CZ3   . TRP A 1 260 ? 14.781 7.707   -3.098  1.00 45.41  ? 260 TRP A CZ3   1 
ATOM   2022 C  CH2   . TRP A 1 260 ? 15.336 7.212   -4.286  1.00 44.67  ? 260 TRP A CH2   1 
ATOM   2023 N  N     . LEU A 1 261 ? 14.825 11.907  -1.061  1.00 37.71  ? 261 LEU A N     1 
ATOM   2024 C  CA    . LEU A 1 261 ? 15.684 11.550  0.059   1.00 37.45  ? 261 LEU A CA    1 
ATOM   2025 C  C     . LEU A 1 261 ? 15.689 10.044  0.268   1.00 40.71  ? 261 LEU A C     1 
ATOM   2026 O  O     . LEU A 1 261 ? 14.649 9.387   0.168   1.00 42.88  ? 261 LEU A O     1 
ATOM   2027 C  CB    . LEU A 1 261 ? 15.232 12.246  1.352   1.00 36.69  ? 261 LEU A CB    1 
ATOM   2028 C  CG    . LEU A 1 261 ? 15.266 13.774  1.402   1.00 37.99  ? 261 LEU A CG    1 
ATOM   2029 C  CD1   . LEU A 1 261 ? 14.735 14.265  2.742   1.00 40.72  ? 261 LEU A CD1   1 
ATOM   2030 C  CD2   . LEU A 1 261 ? 16.676 14.295  1.164   1.00 39.88  ? 261 LEU A CD2   1 
ATOM   2031 N  N     . ALA A 1 262 ? 16.871 9.508   0.567   1.00 36.88  ? 262 ALA A N     1 
ATOM   2032 C  CA    . ALA A 1 262 ? 17.047 8.107   0.930   1.00 34.85  ? 262 ALA A CA    1 
ATOM   2033 C  C     . ALA A 1 262 ? 17.823 8.091   2.235   1.00 33.91  ? 262 ALA A C     1 
ATOM   2034 O  O     . ALA A 1 262 ? 18.968 8.553   2.280   1.00 30.47  ? 262 ALA A O     1 
ATOM   2035 C  CB    . ALA A 1 262 ? 17.784 7.330   -0.163  1.00 36.15  ? 262 ALA A CB    1 
ATOM   2036 N  N     . GLU A 1 263 ? 17.205 7.581   3.298   1.00 31.38  ? 263 GLU A N     1 
ATOM   2037 C  CA    . GLU A 1 263 ? 17.713 7.798   4.641   1.00 35.17  ? 263 GLU A CA    1 
ATOM   2038 C  C     . GLU A 1 263 ? 17.642 6.526   5.470   1.00 36.48  ? 263 GLU A C     1 
ATOM   2039 O  O     . GLU A 1 263 ? 16.808 5.643   5.247   1.00 37.27  ? 263 GLU A O     1 
ATOM   2040 C  CB    . GLU A 1 263 ? 16.943 8.919   5.362   1.00 36.46  ? 263 GLU A CB    1 
ATOM   2041 C  CG    . GLU A 1 263 ? 16.979 10.264  4.642   1.00 32.54  ? 263 GLU A CG    1 
ATOM   2042 C  CD    . GLU A 1 263 ? 18.374 10.859  4.572   1.00 31.69  ? 263 GLU A CD    1 
ATOM   2043 O  OE1   . GLU A 1 263 ? 19.226 10.509  5.413   1.00 31.48  ? 263 GLU A OE1   1 
ATOM   2044 O  OE2   . GLU A 1 263 ? 18.622 11.686  3.673   1.00 38.74  ? 263 GLU A OE2   1 
ATOM   2045 N  N     . HIS A 1 264 ? 18.532 6.473   6.458   1.00 35.91  ? 264 HIS A N     1 
ATOM   2046 C  CA    . HIS A 1 264 ? 18.626 5.356   7.393   1.00 37.12  ? 264 HIS A CA    1 
ATOM   2047 C  C     . HIS A 1 264 ? 17.634 5.581   8.538   1.00 36.13  ? 264 HIS A C     1 
ATOM   2048 O  O     . HIS A 1 264 ? 17.996 5.828   9.690   1.00 32.72  ? 264 HIS A O     1 
ATOM   2049 C  CB    . HIS A 1 264 ? 20.061 5.226   7.891   1.00 36.58  ? 264 HIS A CB    1 
ATOM   2050 C  CG    . HIS A 1 264 ? 20.317 3.990   8.691   1.00 33.86  ? 264 HIS A CG    1 
ATOM   2051 N  ND1   . HIS A 1 264 ? 21.359 3.888   9.588   1.00 32.06  ? 264 HIS A ND1   1 
ATOM   2052 C  CD2   . HIS A 1 264 ? 19.668 2.803   8.730   1.00 30.04  ? 264 HIS A CD2   1 
ATOM   2053 C  CE1   . HIS A 1 264 ? 21.340 2.692   10.145  1.00 29.83  ? 264 HIS A CE1   1 
ATOM   2054 N  NE2   . HIS A 1 264 ? 20.324 2.014   9.643   1.00 35.71  ? 264 HIS A NE2   1 
ATOM   2055 N  N     . MET A 1 265 ? 16.346 5.487   8.192   1.00 35.58  ? 265 MET A N     1 
ATOM   2056 C  CA    . MET A 1 265 ? 15.269 5.914   9.076   1.00 36.04  ? 265 MET A CA    1 
ATOM   2057 C  C     . MET A 1 265 ? 14.149 4.888   9.142   1.00 39.04  ? 265 MET A C     1 
ATOM   2058 O  O     . MET A 1 265 ? 13.749 4.320   8.121   1.00 34.00  ? 265 MET A O     1 
ATOM   2059 C  CB    . MET A 1 265 ? 14.663 7.245   8.621   1.00 36.66  ? 265 MET A CB    1 
ATOM   2060 C  CG    . MET A 1 265 ? 15.562 8.441   8.766   1.00 39.40  ? 265 MET A CG    1 
ATOM   2061 S  SD    . MET A 1 265 ? 14.730 9.932   8.200   1.00 39.88  ? 265 MET A SD    1 
ATOM   2062 C  CE    . MET A 1 265 ? 15.991 11.159  8.528   1.00 37.51  ? 265 MET A CE    1 
ATOM   2063 N  N     . LEU A 1 266 ? 13.619 4.688   10.347  1.00 42.86  ? 266 LEU A N     1 
ATOM   2064 C  CA    . LEU A 1 266 ? 12.372 3.963   10.524  1.00 35.56  ? 266 LEU A CA    1 
ATOM   2065 C  C     . LEU A 1 266 ? 11.189 4.873   10.198  1.00 38.69  ? 266 LEU A C     1 
ATOM   2066 O  O     . LEU A 1 266 ? 11.306 6.101   10.168  1.00 36.46  ? 266 LEU A O     1 
ATOM   2067 C  CB    . LEU A 1 266 ? 12.253 3.442   11.958  1.00 39.44  ? 266 LEU A CB    1 
ATOM   2068 C  CG    . LEU A 1 266 ? 12.037 4.502   13.049  1.00 37.23  ? 266 LEU A CG    1 
ATOM   2069 C  CD1   . LEU A 1 266 ? 10.559 4.692   13.349  1.00 40.16  ? 266 LEU A CD1   1 
ATOM   2070 C  CD2   . LEU A 1 266 ? 12.794 4.156   14.320  1.00 33.97  ? 266 LEU A CD2   1 
ATOM   2071 N  N     . ILE A 1 267 ? 10.034 4.256   9.959   1.00 37.05  ? 267 ILE A N     1 
ATOM   2072 C  CA    . ILE A 1 267 ? 8.780  4.980   9.765   1.00 42.05  ? 267 ILE A CA    1 
ATOM   2073 C  C     . ILE A 1 267 ? 7.719  4.317   10.631  1.00 39.42  ? 267 ILE A C     1 
ATOM   2074 O  O     . ILE A 1 267 ? 7.423  3.129   10.453  1.00 48.49  ? 267 ILE A O     1 
ATOM   2075 C  CB    . ILE A 1 267 ? 8.334  4.998   8.293   1.00 40.37  ? 267 ILE A CB    1 
ATOM   2076 C  CG1   . ILE A 1 267 ? 9.456  5.509   7.389   1.00 41.79  ? 267 ILE A CG1   1 
ATOM   2077 C  CG2   . ILE A 1 267 ? 7.091  5.858   8.127   1.00 36.13  ? 267 ILE A CG2   1 
ATOM   2078 C  CD1   . ILE A 1 267 ? 9.195  5.277   5.911   1.00 38.33  ? 267 ILE A CD1   1 
ATOM   2079 N  N     . LEU A 1 268 ? 7.148  5.075   11.564  1.00 41.60  ? 268 LEU A N     1 
ATOM   2080 C  CA    . LEU A 1 268 ? 6.083  4.574   12.420  1.00 43.36  ? 268 LEU A CA    1 
ATOM   2081 C  C     . LEU A 1 268 ? 4.882  5.504   12.346  1.00 44.10  ? 268 LEU A C     1 
ATOM   2082 O  O     . LEU A 1 268 ? 5.021  6.713   12.144  1.00 44.23  ? 268 LEU A O     1 
ATOM   2083 C  CB    . LEU A 1 268 ? 6.549  4.421   13.888  1.00 45.31  ? 268 LEU A CB    1 
ATOM   2084 C  CG    . LEU A 1 268 ? 6.927  5.648   14.730  1.00 42.42  ? 268 LEU A CG    1 
ATOM   2085 C  CD1   . LEU A 1 268 ? 5.718  6.277   15.407  1.00 44.01  ? 268 LEU A CD1   1 
ATOM   2086 C  CD2   . LEU A 1 268 ? 7.972  5.274   15.772  1.00 47.09  ? 268 LEU A CD2   1 
ATOM   2087 N  N     . GLY A 1 269 ? 3.697  4.923   12.509  1.00 50.36  ? 269 GLY A N     1 
ATOM   2088 C  CA    . GLY A 1 269 ? 2.465  5.676   12.653  1.00 45.71  ? 269 GLY A CA    1 
ATOM   2089 C  C     . GLY A 1 269 ? 1.954  5.544   14.079  1.00 44.92  ? 269 GLY A C     1 
ATOM   2090 O  O     . GLY A 1 269 ? 1.886  4.442   14.620  1.00 49.24  ? 269 GLY A O     1 
ATOM   2091 N  N     . ILE A 1 270 ? 1.614  6.680   14.679  1.00 48.51  ? 270 ILE A N     1 
ATOM   2092 C  CA    . ILE A 1 270 ? 1.181  6.718   16.069  1.00 50.02  ? 270 ILE A CA    1 
ATOM   2093 C  C     . ILE A 1 270 ? -0.174 7.410   16.149  1.00 51.84  ? 270 ILE A C     1 
ATOM   2094 O  O     . ILE A 1 270 ? -0.411 8.418   15.475  1.00 51.32  ? 270 ILE A O     1 
ATOM   2095 C  CB    . ILE A 1 270 ? 2.229  7.411   16.968  1.00 45.16  ? 270 ILE A CB    1 
ATOM   2096 C  CG1   . ILE A 1 270 ? 1.786  7.386   18.430  1.00 47.97  ? 270 ILE A CG1   1 
ATOM   2097 C  CG2   . ILE A 1 270 ? 2.503  8.830   16.497  1.00 48.33  ? 270 ILE A CG2   1 
ATOM   2098 C  CD1   . ILE A 1 270 ? 2.864  7.814   19.392  1.00 50.29  ? 270 ILE A CD1   1 
ATOM   2099 N  N     . THR A 1 271 ? -1.070 6.851   16.957  1.00 53.64  ? 271 THR A N     1 
ATOM   2100 C  CA    . THR A 1 271 ? -2.429 7.349   17.114  1.00 54.09  ? 271 THR A CA    1 
ATOM   2101 C  C     . THR A 1 271 ? -2.698 7.635   18.585  1.00 57.29  ? 271 THR A C     1 
ATOM   2102 O  O     . THR A 1 271 ? -2.361 6.824   19.454  1.00 55.69  ? 271 THR A O     1 
ATOM   2103 C  CB    . THR A 1 271 ? -3.454 6.337   16.584  1.00 56.65  ? 271 THR A CB    1 
ATOM   2104 O  OG1   . THR A 1 271 ? -3.133 5.996   15.231  1.00 60.57  ? 271 THR A OG1   1 
ATOM   2105 C  CG2   . THR A 1 271 ? -4.860 6.912   16.635  1.00 56.14  ? 271 THR A CG2   1 
ATOM   2106 N  N     . ASN A 1 272 ? -3.310 8.781   18.856  1.00 60.38  ? 272 ASN A N     1 
ATOM   2107 C  CA    . ASN A 1 272 ? -3.596 9.222   20.215  1.00 60.07  ? 272 ASN A CA    1 
ATOM   2108 C  C     . ASN A 1 272 ? -4.982 8.758   20.638  1.00 61.00  ? 272 ASN A C     1 
ATOM   2109 O  O     . ASN A 1 272 ? -5.772 8.281   19.820  1.00 61.89  ? 272 ASN A O     1 
ATOM   2110 C  CB    . ASN A 1 272 ? -3.456 10.747  20.304  1.00 60.23  ? 272 ASN A CB    1 
ATOM   2111 C  CG    . ASN A 1 272 ? -4.481 11.499  19.467  1.00 57.67  ? 272 ASN A CG    1 
ATOM   2112 O  OD1   . ASN A 1 272 ? -5.328 10.909  18.801  1.00 67.25  ? 272 ASN A OD1   1 
ATOM   2113 N  ND2   . ASN A 1 272 ? -4.404 12.820  19.507  1.00 64.26  ? 272 ASN A ND2   1 
ATOM   2114 N  N     . PRO A 1 273 ? -5.314 8.870   21.929  1.00 65.24  ? 273 PRO A N     1 
ATOM   2115 C  CA    . PRO A 1 273 ? -6.668 8.495   22.373  1.00 63.78  ? 273 PRO A CA    1 
ATOM   2116 C  C     . PRO A 1 273 ? -7.780 9.356   21.786  1.00 65.28  ? 273 PRO A C     1 
ATOM   2117 O  O     . PRO A 1 273 ? -8.956 9.017   21.964  1.00 71.01  ? 273 PRO A O     1 
ATOM   2118 C  CB    . PRO A 1 273 ? -6.595 8.656   23.896  1.00 63.32  ? 273 PRO A CB    1 
ATOM   2119 C  CG    . PRO A 1 273 ? -5.153 8.507   24.223  1.00 61.31  ? 273 PRO A CG    1 
ATOM   2120 C  CD    . PRO A 1 273 ? -4.414 9.114   23.073  1.00 58.56  ? 273 PRO A CD    1 
ATOM   2121 N  N     . GLU A 1 274 ? -7.454 10.454  21.107  1.00 68.21  ? 274 GLU A N     1 
ATOM   2122 C  CA    . GLU A 1 274 ? -8.440 11.308  20.457  1.00 65.40  ? 274 GLU A CA    1 
ATOM   2123 C  C     . GLU A 1 274 ? -8.688 10.922  19.002  1.00 69.20  ? 274 GLU A C     1 
ATOM   2124 O  O     . GLU A 1 274 ? -9.257 11.724  18.251  1.00 66.75  ? 274 GLU A O     1 
ATOM   2125 C  CB    . GLU A 1 274 ? -7.999 12.771  20.524  1.00 62.05  ? 274 GLU A CB    1 
ATOM   2126 C  CG    . GLU A 1 274 ? -7.595 13.245  21.905  1.00 63.56  ? 274 GLU A CG    1 
ATOM   2127 C  CD    . GLU A 1 274 ? -8.779 13.455  22.821  1.00 69.95  ? 274 GLU A CD    1 
ATOM   2128 O  OE1   . GLU A 1 274 ? -9.928 13.445  22.329  1.00 67.18  ? 274 GLU A OE1   1 
ATOM   2129 O  OE2   . GLU A 1 274 ? -8.560 13.636  24.037  1.00 78.11  ? 274 GLU A OE2   1 
ATOM   2130 N  N     . GLY A 1 275 ? -8.259 9.732   18.584  1.00 64.00  ? 275 GLY A N     1 
ATOM   2131 C  CA    . GLY A 1 275 ? -8.497 9.275   17.229  1.00 68.13  ? 275 GLY A CA    1 
ATOM   2132 C  C     . GLY A 1 275 ? -7.705 9.978   16.149  1.00 70.75  ? 275 GLY A C     1 
ATOM   2133 O  O     . GLY A 1 275 ? -8.124 9.972   14.990  1.00 71.92  ? 275 GLY A O     1 
ATOM   2134 N  N     . LYS A 1 276 ? -6.567 10.577  16.488  1.00 71.44  ? 276 LYS A N     1 
ATOM   2135 C  CA    . LYS A 1 276 ? -5.749 11.321  15.538  1.00 68.96  ? 276 LYS A CA    1 
ATOM   2136 C  C     . LYS A 1 276 ? -4.422 10.599  15.345  1.00 68.31  ? 276 LYS A C     1 
ATOM   2137 O  O     . LYS A 1 276 ? -3.763 10.235  16.323  1.00 70.22  ? 276 LYS A O     1 
ATOM   2138 C  CB    . LYS A 1 276 ? -5.518 12.754  16.026  1.00 70.83  ? 276 LYS A CB    1 
ATOM   2139 C  CG    . LYS A 1 276 ? -5.010 13.710  14.960  1.00 79.70  ? 276 LYS A CG    1 
ATOM   2140 C  CD    . LYS A 1 276 ? -5.126 15.157  15.425  1.00 83.20  ? 276 LYS A CD    1 
ATOM   2141 C  CE    . LYS A 1 276 ? -4.663 16.134  14.350  1.00 81.66  ? 276 LYS A CE    1 
ATOM   2142 N  NZ    . LYS A 1 276 ? -5.507 16.048  13.124  1.00 82.62  ? 276 LYS A NZ    1 
ATOM   2143 N  N     . LYS A 1 277 ? -4.035 10.394  14.087  1.00 60.27  ? 277 LYS A N     1 
ATOM   2144 C  CA    . LYS A 1 277 ? -2.853 9.614   13.744  1.00 53.65  ? 277 LYS A CA    1 
ATOM   2145 C  C     . LYS A 1 277 ? -1.831 10.476  13.015  1.00 55.19  ? 277 LYS A C     1 
ATOM   2146 O  O     . LYS A 1 277 ? -2.185 11.287  12.153  1.00 51.04  ? 277 LYS A O     1 
ATOM   2147 C  CB    . LYS A 1 277 ? -3.231 8.407   12.875  1.00 56.26  ? 277 LYS A CB    1 
ATOM   2148 C  CG    . LYS A 1 277 ? -2.065 7.498   12.511  1.00 50.78  ? 277 LYS A CG    1 
ATOM   2149 C  CD    . LYS A 1 277 ? -2.542 6.287   11.721  1.00 50.99  ? 277 LYS A CD    1 
ATOM   2150 C  CE    . LYS A 1 277 ? -1.385 5.377   11.338  1.00 53.12  ? 277 LYS A CE    1 
ATOM   2151 N  NZ    . LYS A 1 277 ? -1.855 4.157   10.620  1.00 52.50  ? 277 LYS A NZ    1 
ATOM   2152 N  N     . LYS A 1 278 ? -0.558 10.295  13.363  1.00 48.04  ? 278 LYS A N     1 
ATOM   2153 C  CA    . LYS A 1 278 ? 0.535  10.955  12.669  1.00 45.92  ? 278 LYS A CA    1 
ATOM   2154 C  C     . LYS A 1 278 ? 1.638  9.942   12.393  1.00 49.78  ? 278 LYS A C     1 
ATOM   2155 O  O     . LYS A 1 278 ? 1.763  8.930   13.088  1.00 45.11  ? 278 LYS A O     1 
ATOM   2156 C  CB    . LYS A 1 278 ? 1.087  12.136  13.475  1.00 47.96  ? 278 LYS A CB    1 
ATOM   2157 C  CG    . LYS A 1 278 ? 0.067  13.238  13.721  1.00 49.55  ? 278 LYS A CG    1 
ATOM   2158 C  CD    . LYS A 1 278 ? 0.649  14.362  14.550  1.00 47.83  ? 278 LYS A CD    1 
ATOM   2159 C  CE    . LYS A 1 278 ? -0.374 15.469  14.759  1.00 52.78  ? 278 LYS A CE    1 
ATOM   2160 N  NZ    . LYS A 1 278 ? -0.845 16.035  13.461  1.00 60.15  ? 278 LYS A NZ    1 
ATOM   2161 N  N     . TYR A 1 279 ? 2.431  10.223  11.363  1.00 43.49  ? 279 TYR A N     1 
ATOM   2162 C  CA    . TYR A 1 279 ? 3.555  9.384   10.976  1.00 41.05  ? 279 TYR A CA    1 
ATOM   2163 C  C     . TYR A 1 279 ? 4.857  10.102  11.299  1.00 42.38  ? 279 TYR A C     1 
ATOM   2164 O  O     . TYR A 1 279 ? 5.015  11.285  10.976  1.00 50.46  ? 279 TYR A O     1 
ATOM   2165 C  CB    . TYR A 1 279 ? 3.499  9.038   9.487   1.00 44.59  ? 279 TYR A CB    1 
ATOM   2166 C  CG    . TYR A 1 279 ? 2.422  8.041   9.120   1.00 45.62  ? 279 TYR A CG    1 
ATOM   2167 C  CD1   . TYR A 1 279 ? 1.136  8.461   8.804   1.00 47.30  ? 279 TYR A CD1   1 
ATOM   2168 C  CD2   . TYR A 1 279 ? 2.694  6.678   9.086   1.00 44.37  ? 279 TYR A CD2   1 
ATOM   2169 C  CE1   . TYR A 1 279 ? 0.151  7.551   8.465   1.00 49.08  ? 279 TYR A CE1   1 
ATOM   2170 C  CE2   . TYR A 1 279 ? 1.717  5.762   8.746   1.00 43.95  ? 279 TYR A CE2   1 
ATOM   2171 C  CZ    . TYR A 1 279 ? 0.449  6.204   8.436   1.00 48.65  ? 279 TYR A CZ    1 
ATOM   2172 O  OH    . TYR A 1 279 ? -0.528 5.296   8.098   1.00 49.01  ? 279 TYR A OH    1 
ATOM   2173 N  N     . LEU A 1 280 ? 5.783  9.389   11.930  1.00 40.33  ? 280 LEU A N     1 
ATOM   2174 C  CA    . LEU A 1 280 ? 7.080  9.932   12.296  1.00 36.29  ? 280 LEU A CA    1 
ATOM   2175 C  C     . LEU A 1 280 ? 8.185  9.086   11.680  1.00 39.16  ? 280 LEU A C     1 
ATOM   2176 O  O     . LEU A 1 280 ? 8.001  7.898   11.401  1.00 38.58  ? 280 LEU A O     1 
ATOM   2177 C  CB    . LEU A 1 280 ? 7.253  9.979   13.822  1.00 39.31  ? 280 LEU A CB    1 
ATOM   2178 C  CG    . LEU A 1 280 ? 6.211  10.758  14.636  1.00 46.04  ? 280 LEU A CG    1 
ATOM   2179 C  CD1   . LEU A 1 280 ? 6.388  10.502  16.122  1.00 44.12  ? 280 LEU A CD1   1 
ATOM   2180 C  CD2   . LEU A 1 280 ? 6.291  12.245  14.347  1.00 38.87  ? 280 LEU A CD2   1 
ATOM   2181 N  N     . ALA A 1 281 ? 9.336  9.714   11.462  1.00 37.46  ? 281 ALA A N     1 
ATOM   2182 C  CA    . ALA A 1 281 ? 10.536 9.039   11.000  1.00 38.87  ? 281 ALA A CA    1 
ATOM   2183 C  C     . ALA A 1 281 ? 11.659 9.297   11.991  1.00 37.36  ? 281 ALA A C     1 
ATOM   2184 O  O     . ALA A 1 281 ? 11.740 10.373  12.589  1.00 38.33  ? 281 ALA A O     1 
ATOM   2185 C  CB    . ALA A 1 281 ? 10.956 9.514   9.601   1.00 30.88  ? 281 ALA A CB    1 
ATOM   2186 N  N     . ALA A 1 282 ? 12.526 8.304   12.168  1.00 36.66  ? 282 ALA A N     1 
ATOM   2187 C  CA    . ALA A 1 282 ? 13.606 8.417   13.137  1.00 38.09  ? 282 ALA A CA    1 
ATOM   2188 C  C     . ALA A 1 282 ? 14.878 7.822   12.557  1.00 37.90  ? 282 ALA A C     1 
ATOM   2189 O  O     . ALA A 1 282 ? 14.860 6.706   12.031  1.00 36.93  ? 282 ALA A O     1 
ATOM   2190 C  CB    . ALA A 1 282 ? 13.243 7.720   14.453  1.00 35.20  ? 282 ALA A CB    1 
ATOM   2191 N  N     . ALA A 1 283 ? 15.974 8.564   12.662  1.00 37.57  ? 283 ALA A N     1 
ATOM   2192 C  CA    . ALA A 1 283 ? 17.284 8.117   12.202  1.00 36.79  ? 283 ALA A CA    1 
ATOM   2193 C  C     . ALA A 1 283 ? 18.147 7.850   13.428  1.00 32.95  ? 283 ALA A C     1 
ATOM   2194 O  O     . ALA A 1 283 ? 18.614 8.783   14.086  1.00 32.91  ? 283 ALA A O     1 
ATOM   2195 C  CB    . ALA A 1 283 ? 17.930 9.151   11.286  1.00 32.86  ? 283 ALA A CB    1 
ATOM   2196 N  N     . PHE A 1 284 ? 18.339 6.581   13.739  1.00 31.28  ? 284 PHE A N     1 
ATOM   2197 C  CA    . PHE A 1 284 ? 19.283 6.163   14.756  1.00 34.42  ? 284 PHE A CA    1 
ATOM   2198 C  C     . PHE A 1 284 ? 20.391 5.342   14.110  1.00 35.76  ? 284 PHE A C     1 
ATOM   2199 O  O     . PHE A 1 284 ? 20.147 4.629   13.131  1.00 35.13  ? 284 PHE A O     1 
ATOM   2200 C  CB    . PHE A 1 284 ? 18.619 5.317   15.850  1.00 37.12  ? 284 PHE A CB    1 
ATOM   2201 C  CG    . PHE A 1 284 ? 17.437 5.969   16.504  1.00 36.81  ? 284 PHE A CG    1 
ATOM   2202 C  CD1   . PHE A 1 284 ? 17.392 7.343   16.699  1.00 38.91  ? 284 PHE A CD1   1 
ATOM   2203 C  CD2   . PHE A 1 284 ? 16.370 5.197   16.945  1.00 42.11  ? 284 PHE A CD2   1 
ATOM   2204 C  CE1   . PHE A 1 284 ? 16.299 7.933   17.308  1.00 34.39  ? 284 PHE A CE1   1 
ATOM   2205 C  CE2   . PHE A 1 284 ? 15.279 5.779   17.560  1.00 40.98  ? 284 PHE A CE2   1 
ATOM   2206 C  CZ    . PHE A 1 284 ? 15.240 7.151   17.740  1.00 36.16  ? 284 PHE A CZ    1 
ATOM   2207 N  N     . PRO A 1 285 ? 21.622 5.422   14.626  1.00 35.91  ? 285 PRO A N     1 
ATOM   2208 C  CA    . PRO A 1 285 ? 22.710 4.606   14.068  1.00 38.44  ? 285 PRO A CA    1 
ATOM   2209 C  C     . PRO A 1 285 ? 22.419 3.115   14.149  1.00 45.26  ? 285 PRO A C     1 
ATOM   2210 O  O     . PRO A 1 285 ? 21.389 2.703   14.693  1.00 46.21  ? 285 PRO A O     1 
ATOM   2211 C  CB    . PRO A 1 285 ? 23.916 4.995   14.933  1.00 36.08  ? 285 PRO A CB    1 
ATOM   2212 C  CG    . PRO A 1 285 ? 23.589 6.366   15.429  1.00 39.34  ? 285 PRO A CG    1 
ATOM   2213 C  CD    . PRO A 1 285 ? 22.106 6.351   15.659  1.00 38.28  ? 285 PRO A CD    1 
ATOM   2214 N  N     . SER A 1 286 ? 23.315 2.297   13.607  1.00 44.19  ? 286 SER A N     1 
ATOM   2215 C  CA    . SER A 1 286 ? 23.111 0.856   13.647  1.00 46.84  ? 286 SER A CA    1 
ATOM   2216 C  C     . SER A 1 286 ? 23.128 0.354   15.086  1.00 46.49  ? 286 SER A C     1 
ATOM   2217 O  O     . SER A 1 286 ? 23.934 0.799   15.909  1.00 44.14  ? 286 SER A O     1 
ATOM   2218 C  CB    . SER A 1 286 ? 24.184 0.148   12.819  1.00 49.56  ? 286 SER A CB    1 
ATOM   2219 O  OG    . SER A 1 286 ? 24.236 0.661   11.496  1.00 45.43  ? 286 SER A OG    1 
ATOM   2220 N  N     . ALA A 1 287 ? 22.213 -0.571  15.385  1.00 50.42  ? 287 ALA A N     1 
ATOM   2221 C  CA    . ALA A 1 287 ? 22.065 -1.158  16.720  1.00 52.10  ? 287 ALA A CA    1 
ATOM   2222 C  C     . ALA A 1 287 ? 21.871 -0.078  17.784  1.00 51.39  ? 287 ALA A C     1 
ATOM   2223 O  O     . ALA A 1 287 ? 22.484 -0.104  18.855  1.00 48.24  ? 287 ALA A O     1 
ATOM   2224 C  CB    . ALA A 1 287 ? 23.250 -2.063  17.062  1.00 52.46  ? 287 ALA A CB    1 
ATOM   2225 N  N     . CYS A 1 288 ? 20.998 0.883   17.478  1.00 51.98  ? 288 CYS A N     1 
ATOM   2226 C  CA    . CYS A 1 288 ? 20.690 1.969   18.395  1.00 49.55  ? 288 CYS A CA    1 
ATOM   2227 C  C     . CYS A 1 288 ? 19.206 2.088   18.711  1.00 49.46  ? 288 CYS A C     1 
ATOM   2228 O  O     . CYS A 1 288 ? 18.817 3.010   19.440  1.00 46.69  ? 288 CYS A O     1 
ATOM   2229 C  CB    . CYS A 1 288 ? 21.217 3.300   17.841  1.00 44.69  ? 288 CYS A CB    1 
ATOM   2230 S  SG    . CYS A 1 288 ? 22.975 3.582   18.201  1.00 49.69  ? 288 CYS A SG    1 
ATOM   2231 N  N     . GLY A 1 289 ? 18.367 1.196   18.181  1.00 50.60  ? 289 GLY A N     1 
ATOM   2232 C  CA    . GLY A 1 289 ? 17.012 1.067   18.679  1.00 44.46  ? 289 GLY A CA    1 
ATOM   2233 C  C     . GLY A 1 289 ? 15.901 1.331   17.686  1.00 44.27  ? 289 GLY A C     1 
ATOM   2234 O  O     . GLY A 1 289 ? 14.742 1.469   18.087  1.00 42.19  ? 289 GLY A O     1 
ATOM   2235 N  N     . LYS A 1 290 ? 16.221 1.398   16.392  1.00 41.04  ? 290 LYS A N     1 
ATOM   2236 C  CA    . LYS A 1 290 ? 15.190 1.708   15.405  1.00 40.09  ? 290 LYS A CA    1 
ATOM   2237 C  C     . LYS A 1 290 ? 14.099 0.641   15.387  1.00 44.94  ? 290 LYS A C     1 
ATOM   2238 O  O     . LYS A 1 290 ? 12.904 0.962   15.421  1.00 41.57  ? 290 LYS A O     1 
ATOM   2239 C  CB    . LYS A 1 290 ? 15.809 1.872   14.016  1.00 44.06  ? 290 LYS A CB    1 
ATOM   2240 C  CG    . LYS A 1 290 ? 16.638 3.146   13.847  1.00 39.63  ? 290 LYS A CG    1 
ATOM   2241 C  CD    . LYS A 1 290 ? 16.964 3.418   12.383  1.00 38.66  ? 290 LYS A CD    1 
ATOM   2242 C  CE    . LYS A 1 290 ? 17.762 2.273   11.757  1.00 35.82  ? 290 LYS A CE    1 
ATOM   2243 N  NZ    . LYS A 1 290 ? 19.067 2.057   12.447  1.00 36.80  ? 290 LYS A NZ    1 
ATOM   2244 N  N     . THR A 1 291 ? 14.488 -0.637  15.339  1.00 46.22  ? 291 THR A N     1 
ATOM   2245 C  CA    . THR A 1 291 ? 13.493 -1.703  15.262  1.00 45.73  ? 291 THR A CA    1 
ATOM   2246 C  C     . THR A 1 291 ? 12.624 -1.739  16.514  1.00 42.66  ? 291 THR A C     1 
ATOM   2247 O  O     . THR A 1 291 ? 11.399 -1.876  16.423  1.00 43.23  ? 291 THR A O     1 
ATOM   2248 C  CB    . THR A 1 291 ? 14.175 -3.054  15.035  1.00 42.99  ? 291 THR A CB    1 
ATOM   2249 O  OG1   . THR A 1 291 ? 14.828 -3.051  13.760  1.00 48.29  ? 291 THR A OG1   1 
ATOM   2250 C  CG2   . THR A 1 291 ? 13.153 -4.187  15.059  1.00 47.20  ? 291 THR A CG2   1 
ATOM   2251 N  N     . ASN A 1 292 ? 13.236 -1.597  17.691  1.00 44.20  ? 292 ASN A N     1 
ATOM   2252 C  CA    . ASN A 1 292 ? 12.458 -1.572  18.927  1.00 47.23  ? 292 ASN A CA    1 
ATOM   2253 C  C     . ASN A 1 292 ? 11.466 -0.413  18.943  1.00 43.52  ? 292 ASN A C     1 
ATOM   2254 O  O     . ASN A 1 292 ? 10.328 -0.569  19.397  1.00 44.37  ? 292 ASN A O     1 
ATOM   2255 C  CB    . ASN A 1 292 ? 13.394 -1.494  20.134  1.00 50.50  ? 292 ASN A CB    1 
ATOM   2256 C  CG    . ASN A 1 292 ? 14.146 -2.791  20.367  1.00 54.84  ? 292 ASN A CG    1 
ATOM   2257 O  OD1   . ASN A 1 292 ? 13.767 -3.595  21.218  1.00 61.61  ? 292 ASN A OD1   1 
ATOM   2258 N  ND2   . ASN A 1 292 ? 15.213 -3.004  19.603  1.00 52.73  ? 292 ASN A ND2   1 
ATOM   2259 N  N     . LEU A 1 293 ? 11.874 0.760   18.453  1.00 50.57  ? 293 LEU A N     1 
ATOM   2260 C  CA    . LEU A 1 293 ? 10.955 1.896   18.447  1.00 45.77  ? 293 LEU A CA    1 
ATOM   2261 C  C     . LEU A 1 293 ? 9.884  1.737   17.373  1.00 45.83  ? 293 LEU A C     1 
ATOM   2262 O  O     . LEU A 1 293 ? 8.715  2.067   17.602  1.00 42.57  ? 293 LEU A O     1 
ATOM   2263 C  CB    . LEU A 1 293 ? 11.725 3.205   18.251  1.00 39.27  ? 293 LEU A CB    1 
ATOM   2264 C  CG    . LEU A 1 293 ? 10.890 4.492   18.197  1.00 44.37  ? 293 LEU A CG    1 
ATOM   2265 C  CD1   . LEU A 1 293 ? 10.212 4.773   19.533  1.00 43.14  ? 293 LEU A CD1   1 
ATOM   2266 C  CD2   . LEU A 1 293 ? 11.730 5.684   17.768  1.00 43.47  ? 293 LEU A CD2   1 
ATOM   2267 N  N     . ALA A 1 294 ? 10.260 1.217   16.199  1.00 45.05  ? 294 ALA A N     1 
ATOM   2268 C  CA    . ALA A 1 294 ? 9.323  1.118   15.084  1.00 43.85  ? 294 ALA A CA    1 
ATOM   2269 C  C     . ALA A 1 294 ? 8.180  0.146   15.353  1.00 50.16  ? 294 ALA A C     1 
ATOM   2270 O  O     . ALA A 1 294 ? 7.127  0.258   14.716  1.00 51.35  ? 294 ALA A O     1 
ATOM   2271 C  CB    . ALA A 1 294 ? 10.061 0.704   13.811  1.00 41.80  ? 294 ALA A CB    1 
ATOM   2272 N  N     . MET A 1 295 ? 8.358  -0.803  16.267  1.00 46.55  ? 295 MET A N     1 
ATOM   2273 C  CA    . MET A 1 295 ? 7.314  -1.764  16.599  1.00 52.04  ? 295 MET A CA    1 
ATOM   2274 C  C     . MET A 1 295 ? 7.202  -1.928  18.108  1.00 53.54  ? 295 MET A C     1 
ATOM   2275 O  O     . MET A 1 295 ? 7.031  -3.038  18.622  1.00 57.23  ? 295 MET A O     1 
ATOM   2276 C  CB    . MET A 1 295 ? 7.559  -3.109  15.908  1.00 51.25  ? 295 MET A CB    1 
ATOM   2277 C  CG    . MET A 1 295 ? 8.923  -3.741  16.168  1.00 49.00  ? 295 MET A CG    1 
ATOM   2278 S  SD    . MET A 1 295 ? 9.179  -5.330  15.332  1.00 55.14  ? 295 MET A SD    1 
ATOM   2279 C  CE    . MET A 1 295 ? 9.139  -4.847  13.607  1.00 51.54  ? 295 MET A CE    1 
ATOM   2280 N  N     . MET A 1 296 ? 7.280  -0.820  18.842  1.00 54.33  ? 296 MET A N     1 
ATOM   2281 C  CA    . MET A 1 296 ? 7.207  -0.883  20.292  1.00 52.38  ? 296 MET A CA    1 
ATOM   2282 C  C     . MET A 1 296 ? 5.779  -1.150  20.756  1.00 51.39  ? 296 MET A C     1 
ATOM   2283 O  O     . MET A 1 296 ? 4.802  -0.903  20.041  1.00 49.65  ? 296 MET A O     1 
ATOM   2284 C  CB    . MET A 1 296 ? 7.710  0.414   20.929  1.00 54.01  ? 296 MET A CB    1 
ATOM   2285 C  CG    . MET A 1 296 ? 6.743  1.587   20.807  1.00 57.69  ? 296 MET A CG    1 
ATOM   2286 S  SD    . MET A 1 296 ? 7.051  2.917   21.992  1.00 60.33  ? 296 MET A SD    1 
ATOM   2287 C  CE    . MET A 1 296 ? 5.982  4.179   21.322  1.00 62.12  ? 296 MET A CE    1 
ATOM   2288 N  N     . ASN A 1 297 ? 5.674  -1.673  21.978  1.00 47.25  ? 297 ASN A N     1 
ATOM   2289 C  CA    . ASN A 1 297 ? 4.393  -1.833  22.644  1.00 58.97  ? 297 ASN A CA    1 
ATOM   2290 C  C     . ASN A 1 297 ? 4.183  -0.638  23.562  1.00 56.48  ? 297 ASN A C     1 
ATOM   2291 O  O     . ASN A 1 297 ? 4.860  -0.540  24.597  1.00 53.14  ? 297 ASN A O     1 
ATOM   2292 C  CB    . ASN A 1 297 ? 4.359  -3.138  23.440  1.00 59.14  ? 297 ASN A CB    1 
ATOM   2293 C  CG    . ASN A 1 297 ? 2.971  -3.478  23.950  1.00 67.29  ? 297 ASN A CG    1 
ATOM   2294 O  OD1   . ASN A 1 297 ? 1.967  -3.069  23.368  1.00 73.83  ? 297 ASN A OD1   1 
ATOM   2295 N  ND2   . ASN A 1 297 ? 2.908  -4.230  25.045  1.00 63.01  ? 297 ASN A ND2   1 
ATOM   2296 N  N     . PRO A 1 298 ? 3.292  0.294   23.229  1.00 56.78  ? 298 PRO A N     1 
ATOM   2297 C  CA    . PRO A 1 298 ? 3.121  1.487   24.070  1.00 57.72  ? 298 PRO A CA    1 
ATOM   2298 C  C     . PRO A 1 298 ? 2.581  1.144   25.451  1.00 57.04  ? 298 PRO A C     1 
ATOM   2299 O  O     . PRO A 1 298 ? 1.700  0.294   25.604  1.00 62.45  ? 298 PRO A O     1 
ATOM   2300 C  CB    . PRO A 1 298 ? 2.119  2.340   23.281  1.00 54.38  ? 298 PRO A CB    1 
ATOM   2301 C  CG    . PRO A 1 298 ? 2.174  1.818   21.884  1.00 59.43  ? 298 PRO A CG    1 
ATOM   2302 C  CD    . PRO A 1 298 ? 2.483  0.357   22.002  1.00 57.74  ? 298 PRO A CD    1 
ATOM   2303 N  N     . THR A 1 299 ? 3.118  1.826   26.464  1.00 57.02  ? 299 THR A N     1 
ATOM   2304 C  CA    . THR A 1 299 ? 2.654  1.658   27.835  1.00 59.91  ? 299 THR A CA    1 
ATOM   2305 C  C     . THR A 1 299 ? 1.538  2.625   28.209  1.00 62.65  ? 299 THR A C     1 
ATOM   2306 O  O     . THR A 1 299 ? 0.762  2.325   29.122  1.00 67.56  ? 299 THR A O     1 
ATOM   2307 C  CB    . THR A 1 299 ? 3.816  1.829   28.823  1.00 59.08  ? 299 THR A CB    1 
ATOM   2308 O  OG1   . THR A 1 299 ? 4.371  3.145   28.695  1.00 56.06  ? 299 THR A OG1   1 
ATOM   2309 C  CG2   . THR A 1 299 ? 4.902  0.798   28.554  1.00 55.32  ? 299 THR A CG2   1 
ATOM   2310 N  N     . LEU A 1 300 ? 1.438  3.767   27.534  1.00 61.53  ? 300 LEU A N     1 
ATOM   2311 C  CA    . LEU A 1 300 ? 0.354  4.706   27.810  1.00 58.06  ? 300 LEU A CA    1 
ATOM   2312 C  C     . LEU A 1 300 ? -0.955 4.164   27.245  1.00 63.71  ? 300 LEU A C     1 
ATOM   2313 O  O     . LEU A 1 300 ? -1.010 3.802   26.064  1.00 64.00  ? 300 LEU A O     1 
ATOM   2314 C  CB    . LEU A 1 300 ? 0.661  6.072   27.201  1.00 58.87  ? 300 LEU A CB    1 
ATOM   2315 C  CG    . LEU A 1 300 ? 1.924  6.788   27.683  1.00 55.91  ? 300 LEU A CG    1 
ATOM   2316 C  CD1   . LEU A 1 300 ? 2.113  8.104   26.940  1.00 56.97  ? 300 LEU A CD1   1 
ATOM   2317 C  CD2   . LEU A 1 300 ? 1.864  7.016   29.184  1.00 56.49  ? 300 LEU A CD2   1 
ATOM   2318 N  N     . PRO A 1 301 ? -2.021 4.090   28.043  1.00 64.34  ? 301 PRO A N     1 
ATOM   2319 C  CA    . PRO A 1 301 ? -3.296 3.584   27.518  1.00 61.98  ? 301 PRO A CA    1 
ATOM   2320 C  C     . PRO A 1 301 ? -3.888 4.536   26.491  1.00 63.02  ? 301 PRO A C     1 
ATOM   2321 O  O     . PRO A 1 301 ? -3.809 5.759   26.631  1.00 62.74  ? 301 PRO A O     1 
ATOM   2322 C  CB    . PRO A 1 301 ? -4.185 3.487   28.765  1.00 65.73  ? 301 PRO A CB    1 
ATOM   2323 C  CG    . PRO A 1 301 ? -3.238 3.526   29.929  1.00 67.79  ? 301 PRO A CG    1 
ATOM   2324 C  CD    . PRO A 1 301 ? -2.090 4.374   29.485  1.00 66.14  ? 301 PRO A CD    1 
ATOM   2325 N  N     . GLY A 1 302 ? -4.482 3.962   25.446  1.00 60.23  ? 302 GLY A N     1 
ATOM   2326 C  CA    . GLY A 1 302 ? -5.109 4.738   24.397  1.00 60.02  ? 302 GLY A CA    1 
ATOM   2327 C  C     . GLY A 1 302 ? -4.205 5.127   23.249  1.00 64.68  ? 302 GLY A C     1 
ATOM   2328 O  O     . GLY A 1 302 ? -4.673 5.786   22.311  1.00 66.85  ? 302 GLY A O     1 
ATOM   2329 N  N     . TRP A 1 303 ? -2.931 4.752   23.293  1.00 66.73  ? 303 TRP A N     1 
ATOM   2330 C  CA    . TRP A 1 303 ? -1.982 5.029   22.225  1.00 58.52  ? 303 TRP A CA    1 
ATOM   2331 C  C     . TRP A 1 303 ? -1.690 3.747   21.460  1.00 60.53  ? 303 TRP A C     1 
ATOM   2332 O  O     . TRP A 1 303 ? -1.607 2.666   22.053  1.00 54.74  ? 303 TRP A O     1 
ATOM   2333 C  CB    . TRP A 1 303 ? -0.683 5.611   22.785  1.00 57.37  ? 303 TRP A CB    1 
ATOM   2334 C  CG    . TRP A 1 303 ? -0.833 6.992   23.341  1.00 60.74  ? 303 TRP A CG    1 
ATOM   2335 C  CD1   . TRP A 1 303 ? -1.219 7.330   24.604  1.00 59.12  ? 303 TRP A CD1   1 
ATOM   2336 C  CD2   . TRP A 1 303 ? -0.595 8.224   22.649  1.00 54.65  ? 303 TRP A CD2   1 
ATOM   2337 N  NE1   . TRP A 1 303 ? -1.238 8.698   24.742  1.00 59.55  ? 303 TRP A NE1   1 
ATOM   2338 C  CE2   . TRP A 1 303 ? -0.858 9.269   23.556  1.00 53.58  ? 303 TRP A CE2   1 
ATOM   2339 C  CE3   . TRP A 1 303 ? -0.185 8.543   21.352  1.00 52.17  ? 303 TRP A CE3   1 
ATOM   2340 C  CZ2   . TRP A 1 303 ? -0.724 10.610  23.207  1.00 52.96  ? 303 TRP A CZ2   1 
ATOM   2341 C  CZ3   . TRP A 1 303 ? -0.052 9.877   21.007  1.00 56.13  ? 303 TRP A CZ3   1 
ATOM   2342 C  CH2   . TRP A 1 303 ? -0.320 10.893  21.930  1.00 50.19  ? 303 TRP A CH2   1 
ATOM   2343 N  N     . LYS A 1 304 ? -1.538 3.870   20.141  1.00 54.45  ? 304 LYS A N     1 
ATOM   2344 C  CA    . LYS A 1 304 ? -1.217 2.727   19.298  1.00 52.22  ? 304 LYS A CA    1 
ATOM   2345 C  C     . LYS A 1 304 ? -0.129 3.119   18.313  1.00 60.19  ? 304 LYS A C     1 
ATOM   2346 O  O     . LYS A 1 304 ? -0.196 4.191   17.705  1.00 56.93  ? 304 LYS A O     1 
ATOM   2347 C  CB    . LYS A 1 304 ? -2.451 2.215   18.545  1.00 58.03  ? 304 LYS A CB    1 
ATOM   2348 C  CG    . LYS A 1 304 ? -2.169 0.999   17.667  1.00 61.72  ? 304 LYS A CG    1 
ATOM   2349 C  CD    . LYS A 1 304 ? -3.445 0.401   17.096  1.00 64.85  ? 304 LYS A CD    1 
ATOM   2350 C  CE    . LYS A 1 304 ? -3.160 -0.898  16.355  1.00 68.44  ? 304 LYS A CE    1 
ATOM   2351 N  NZ    . LYS A 1 304 ? -4.412 -1.599  15.958  1.00 70.83  ? 304 LYS A NZ    1 
ATOM   2352 N  N     . VAL A 1 305 ? 0.865  2.250   18.157  1.00 59.04  ? 305 VAL A N     1 
ATOM   2353 C  CA    . VAL A 1 305 ? 1.968  2.462   17.231  1.00 55.22  ? 305 VAL A CA    1 
ATOM   2354 C  C     . VAL A 1 305 ? 1.922  1.368   16.176  1.00 57.16  ? 305 VAL A C     1 
ATOM   2355 O  O     . VAL A 1 305 ? 1.772  0.185   16.505  1.00 58.53  ? 305 VAL A O     1 
ATOM   2356 C  CB    . VAL A 1 305 ? 3.324  2.471   17.958  1.00 59.46  ? 305 VAL A CB    1 
ATOM   2357 C  CG1   . VAL A 1 305 ? 4.466  2.528   16.952  1.00 55.15  ? 305 VAL A CG1   1 
ATOM   2358 C  CG2   . VAL A 1 305 ? 3.394  3.652   18.911  1.00 54.22  ? 305 VAL A CG2   1 
ATOM   2359 N  N     . GLU A 1 306 ? 2.033  1.766   14.913  1.00 51.83  ? 306 GLU A N     1 
ATOM   2360 C  CA    . GLU A 1 306 ? 2.040  0.841   13.792  1.00 54.28  ? 306 GLU A CA    1 
ATOM   2361 C  C     . GLU A 1 306 ? 3.319  1.036   12.988  1.00 51.64  ? 306 GLU A C     1 
ATOM   2362 O  O     . GLU A 1 306 ? 3.833  2.152   12.873  1.00 49.89  ? 306 GLU A O     1 
ATOM   2363 C  CB    . GLU A 1 306 ? 0.801  1.040   12.909  1.00 54.34  ? 306 GLU A CB    1 
ATOM   2364 C  CG    . GLU A 1 306 ? -0.497 0.604   13.583  1.00 57.25  ? 306 GLU A CG    1 
ATOM   2365 C  CD    . GLU A 1 306 ? -1.736 1.128   12.880  1.00 58.25  ? 306 GLU A CD    1 
ATOM   2366 O  OE1   . GLU A 1 306 ? -1.887 2.362   12.777  1.00 55.73  ? 306 GLU A OE1   1 
ATOM   2367 O  OE2   . GLU A 1 306 ? -2.560 0.306   12.429  1.00 65.91  ? 306 GLU A OE2   1 
ATOM   2368 N  N     . CYS A 1 307 ? 3.835  -0.061  12.439  1.00 49.77  ? 307 CYS A N     1 
ATOM   2369 C  CA    . CYS A 1 307 ? 5.147  -0.076  11.803  1.00 50.94  ? 307 CYS A CA    1 
ATOM   2370 C  C     . CYS A 1 307 ? 5.006  -0.026  10.286  1.00 51.79  ? 307 CYS A C     1 
ATOM   2371 O  O     . CYS A 1 307 ? 4.385  -0.913  9.687   1.00 47.35  ? 307 CYS A O     1 
ATOM   2372 C  CB    . CYS A 1 307 ? 5.933  -1.320  12.211  1.00 50.98  ? 307 CYS A CB    1 
ATOM   2373 S  SG    . CYS A 1 307 ? 7.560  -1.424  11.451  1.00 46.16  ? 307 CYS A SG    1 
ATOM   2374 N  N     . VAL A 1 308 ? 5.594  1.001   9.675   1.00 46.95  ? 308 VAL A N     1 
ATOM   2375 C  CA    . VAL A 1 308 ? 5.730  1.057   8.222   1.00 41.87  ? 308 VAL A CA    1 
ATOM   2376 C  C     . VAL A 1 308 ? 7.071  0.490   7.778   1.00 43.05  ? 308 VAL A C     1 
ATOM   2377 O  O     . VAL A 1 308 ? 7.146  -0.249  6.795   1.00 40.23  ? 308 VAL A O     1 
ATOM   2378 C  CB    . VAL A 1 308 ? 5.551  2.505   7.725   1.00 48.26  ? 308 VAL A CB    1 
ATOM   2379 C  CG1   . VAL A 1 308 ? 5.640  2.560   6.207   1.00 46.99  ? 308 VAL A CG1   1 
ATOM   2380 C  CG2   . VAL A 1 308 ? 4.235  3.081   8.213   1.00 45.43  ? 308 VAL A CG2   1 
ATOM   2381 N  N     . GLY A 1 309 ? 8.139  0.831   8.492   1.00 41.90  ? 309 GLY A N     1 
ATOM   2382 C  CA    . GLY A 1 309 ? 9.467  0.319   8.208   1.00 35.73  ? 309 GLY A CA    1 
ATOM   2383 C  C     . GLY A 1 309 ? 10.352 0.544   9.411   1.00 41.03  ? 309 GLY A C     1 
ATOM   2384 O  O     . GLY A 1 309 ? 10.008 1.287   10.333  1.00 42.63  ? 309 GLY A O     1 
ATOM   2385 N  N     . ASP A 1 310 ? 11.513 -0.108  9.395   1.00 40.27  ? 310 ASP A N     1 
ATOM   2386 C  CA    . ASP A 1 310 ? 12.399 -0.079  10.547  1.00 36.26  ? 310 ASP A CA    1 
ATOM   2387 C  C     . ASP A 1 310 ? 13.846 0.268   10.224  1.00 38.53  ? 310 ASP A C     1 
ATOM   2388 O  O     . ASP A 1 310 ? 14.680 0.234   11.135  1.00 39.72  ? 310 ASP A O     1 
ATOM   2389 C  CB    . ASP A 1 310 ? 12.370 -1.434  11.273  1.00 38.97  ? 310 ASP A CB    1 
ATOM   2390 C  CG    . ASP A 1 310 ? 13.202 -2.492  10.566  1.00 41.50  ? 310 ASP A CG    1 
ATOM   2391 O  OD1   . ASP A 1 310 ? 13.192 -2.528  9.313   1.00 34.91  ? 310 ASP A OD1   1 
ATOM   2392 O  OD2   . ASP A 1 310 ? 13.880 -3.274  11.267  1.00 39.52  ? 310 ASP A OD2   1 
ATOM   2393 N  N     . ASP A 1 311 ? 14.179 0.597   8.973   1.00 40.39  ? 311 ASP A N     1 
ATOM   2394 C  CA    . ASP A 1 311 ? 15.591 0.774   8.650   1.00 36.11  ? 311 ASP A CA    1 
ATOM   2395 C  C     . ASP A 1 311 ? 15.860 1.755   7.515   1.00 32.24  ? 311 ASP A C     1 
ATOM   2396 O  O     . ASP A 1 311 ? 16.864 2.473   7.543   1.00 29.78  ? 311 ASP A O     1 
ATOM   2397 C  CB    . ASP A 1 311 ? 16.222 -0.574  8.297   1.00 31.33  ? 311 ASP A CB    1 
ATOM   2398 C  CG    . ASP A 1 311 ? 17.731 -0.493  8.215   1.00 34.95  ? 311 ASP A CG    1 
ATOM   2399 O  OD1   . ASP A 1 311 ? 18.362 -0.188  9.248   1.00 29.91  ? 311 ASP A OD1   1 
ATOM   2400 O  OD2   . ASP A 1 311 ? 18.284 -0.720  7.120   1.00 37.32  ? 311 ASP A OD2   1 
ATOM   2401 N  N     . ILE A 1 312 ? 15.005 1.774   6.499   1.00 29.08  ? 312 ILE A N     1 
ATOM   2402 C  CA    . ILE A 1 312 ? 15.253 2.543   5.287   1.00 28.82  ? 312 ILE A CA    1 
ATOM   2403 C  C     . ILE A 1 312 ? 13.975 3.279   4.911   1.00 35.84  ? 312 ILE A C     1 
ATOM   2404 O  O     . ILE A 1 312 ? 12.890 2.685   4.905   1.00 31.40  ? 312 ILE A O     1 
ATOM   2405 C  CB    . ILE A 1 312 ? 15.728 1.648   4.123   1.00 36.50  ? 312 ILE A CB    1 
ATOM   2406 C  CG1   . ILE A 1 312 ? 17.022 0.920   4.494   1.00 37.09  ? 312 ILE A CG1   1 
ATOM   2407 C  CG2   . ILE A 1 312 ? 15.946 2.473   2.858   1.00 37.21  ? 312 ILE A CG2   1 
ATOM   2408 C  CD1   . ILE A 1 312 ? 17.481 -0.069  3.444   1.00 44.27  ? 312 ILE A CD1   1 
ATOM   2409 N  N     . ALA A 1 313 ? 14.105 4.570   4.603   1.00 39.56  ? 313 ALA A N     1 
ATOM   2410 C  CA    . ALA A 1 313 ? 12.982 5.397   4.188   1.00 32.75  ? 313 ALA A CA    1 
ATOM   2411 C  C     . ALA A 1 313 ? 13.347 6.138   2.911   1.00 35.44  ? 313 ALA A C     1 
ATOM   2412 O  O     . ALA A 1 313 ? 14.456 6.666   2.791   1.00 33.12  ? 313 ALA A O     1 
ATOM   2413 C  CB    . ALA A 1 313 ? 12.589 6.396   5.283   1.00 32.95  ? 313 ALA A CB    1 
ATOM   2414 N  N     . TRP A 1 314 ? 12.417 6.165   1.962   1.00 37.24  ? 314 TRP A N     1 
ATOM   2415 C  CA    . TRP A 1 314 ? 12.539 6.961   0.749   1.00 42.34  ? 314 TRP A CA    1 
ATOM   2416 C  C     . TRP A 1 314 ? 11.476 8.049   0.808   1.00 42.29  ? 314 TRP A C     1 
ATOM   2417 O  O     . TRP A 1 314 ? 10.278 7.748   0.809   1.00 43.53  ? 314 TRP A O     1 
ATOM   2418 C  CB    . TRP A 1 314 ? 12.373 6.096   -0.504  1.00 37.14  ? 314 TRP A CB    1 
ATOM   2419 C  CG    . TRP A 1 314 ? 13.557 5.214   -0.821  1.00 37.27  ? 314 TRP A CG    1 
ATOM   2420 C  CD1   . TRP A 1 314 ? 14.715 5.098   -0.105  1.00 41.95  ? 314 TRP A CD1   1 
ATOM   2421 C  CD2   . TRP A 1 314 ? 13.697 4.335   -1.949  1.00 37.16  ? 314 TRP A CD2   1 
ATOM   2422 N  NE1   . TRP A 1 314 ? 15.564 4.198   -0.715  1.00 35.96  ? 314 TRP A NE1   1 
ATOM   2423 C  CE2   . TRP A 1 314 ? 14.961 3.719   -1.848  1.00 34.44  ? 314 TRP A CE2   1 
ATOM   2424 C  CE3   . TRP A 1 314 ? 12.873 4.010   -3.032  1.00 37.03  ? 314 TRP A CE3   1 
ATOM   2425 C  CZ2   . TRP A 1 314 ? 15.420 2.796   -2.785  1.00 39.71  ? 314 TRP A CZ2   1 
ATOM   2426 C  CZ3   . TRP A 1 314 ? 13.332 3.092   -3.964  1.00 41.72  ? 314 TRP A CZ3   1 
ATOM   2427 C  CH2   . TRP A 1 314 ? 14.593 2.497   -3.834  1.00 40.65  ? 314 TRP A CH2   1 
ATOM   2428 N  N     . MET A 1 315 ? 11.910 9.305   0.864   1.00 41.91  ? 315 MET A N     1 
ATOM   2429 C  CA    . MET A 1 315 ? 11.018 10.424  1.129   1.00 46.52  ? 315 MET A CA    1 
ATOM   2430 C  C     . MET A 1 315 ? 11.093 11.459  0.014   1.00 47.18  ? 315 MET A C     1 
ATOM   2431 O  O     . MET A 1 315 ? 12.153 11.688  -0.578  1.00 45.72  ? 315 MET A O     1 
ATOM   2432 C  CB    . MET A 1 315 ? 11.349 11.080  2.474   1.00 43.67  ? 315 MET A CB    1 
ATOM   2433 C  CG    . MET A 1 315 ? 11.385 10.095  3.631   1.00 40.34  ? 315 MET A CG    1 
ATOM   2434 S  SD    . MET A 1 315 ? 11.544 10.890  5.240   1.00 44.20  ? 315 MET A SD    1 
ATOM   2435 C  CE    . MET A 1 315 ? 13.084 11.776  5.027   1.00 39.89  ? 315 MET A CE    1 
ATOM   2436 N  N     . LYS A 1 316 ? 9.954  12.095  -0.254  1.00 49.02  ? 316 LYS A N     1 
ATOM   2437 C  CA    . LYS A 1 316 ? 9.843  13.083  -1.317  1.00 53.29  ? 316 LYS A CA    1 
ATOM   2438 C  C     . LYS A 1 316 ? 8.657  13.991  -1.026  1.00 53.65  ? 316 LYS A C     1 
ATOM   2439 O  O     . LYS A 1 316 ? 7.607  13.521  -0.584  1.00 52.96  ? 316 LYS A O     1 
ATOM   2440 C  CB    . LYS A 1 316 ? 9.674  12.406  -2.684  1.00 57.99  ? 316 LYS A CB    1 
ATOM   2441 C  CG    . LYS A 1 316 ? 9.021  13.279  -3.744  1.00 57.54  ? 316 LYS A CG    1 
ATOM   2442 C  CD    . LYS A 1 316 ? 8.807  12.513  -5.035  1.00 63.67  ? 316 LYS A CD    1 
ATOM   2443 C  CE    . LYS A 1 316 ? 10.134 12.167  -5.687  1.00 67.58  ? 316 LYS A CE    1 
ATOM   2444 N  NZ    . LYS A 1 316 ? 10.906 13.391  -6.046  1.00 68.71  ? 316 LYS A NZ    1 
ATOM   2445 N  N     . PHE A 1 317 ? 8.832  15.289  -1.271  1.00 55.62  ? 317 PHE A N     1 
ATOM   2446 C  CA    . PHE A 1 317 ? 7.718  16.221  -1.163  1.00 60.97  ? 317 PHE A CA    1 
ATOM   2447 C  C     . PHE A 1 317 ? 6.784  16.065  -2.357  1.00 63.55  ? 317 PHE A C     1 
ATOM   2448 O  O     . PHE A 1 317 ? 7.229  15.945  -3.503  1.00 63.56  ? 317 PHE A O     1 
ATOM   2449 C  CB    . PHE A 1 317 ? 8.224  17.661  -1.076  1.00 58.22  ? 317 PHE A CB    1 
ATOM   2450 C  CG    . PHE A 1 317 ? 8.790  18.025  0.267   1.00 59.25  ? 317 PHE A CG    1 
ATOM   2451 C  CD1   . PHE A 1 317 ? 7.953  18.363  1.319   1.00 62.14  ? 317 PHE A CD1   1 
ATOM   2452 C  CD2   . PHE A 1 317 ? 10.158 18.033  0.478   1.00 61.28  ? 317 PHE A CD2   1 
ATOM   2453 C  CE1   . PHE A 1 317 ? 8.470  18.700  2.558   1.00 57.76  ? 317 PHE A CE1   1 
ATOM   2454 C  CE2   . PHE A 1 317 ? 10.681 18.367  1.713   1.00 60.04  ? 317 PHE A CE2   1 
ATOM   2455 C  CZ    . PHE A 1 317 ? 9.835  18.702  2.755   1.00 55.90  ? 317 PHE A CZ    1 
ATOM   2456 N  N     . ASP A 1 318 ? 5.480  16.064  -2.083  1.00 62.67  ? 318 ASP A N     1 
ATOM   2457 C  CA    . ASP A 1 318 ? 4.476  15.912  -3.125  1.00 58.21  ? 318 ASP A CA    1 
ATOM   2458 C  C     . ASP A 1 318 ? 4.001  17.291  -3.589  1.00 69.23  ? 318 ASP A C     1 
ATOM   2459 O  O     . ASP A 1 318 ? 4.522  18.328  -3.170  1.00 61.30  ? 318 ASP A O     1 
ATOM   2460 C  CB    . ASP A 1 318 ? 3.323  15.033  -2.632  1.00 65.31  ? 318 ASP A CB    1 
ATOM   2461 C  CG    . ASP A 1 318 ? 2.576  15.632  -1.441  1.00 64.51  ? 318 ASP A CG    1 
ATOM   2462 O  OD1   . ASP A 1 318 ? 2.996  16.682  -0.911  1.00 69.70  ? 318 ASP A OD1   1 
ATOM   2463 O  OD2   . ASP A 1 318 ? 1.555  15.039  -1.034  1.00 60.23  ? 318 ASP A OD2   1 
ATOM   2464 N  N     . ALA A 1 319 ? 3.000  17.313  -4.473  1.00 70.27  ? 319 ALA A N     1 
ATOM   2465 C  CA    . ALA A 1 319 ? 2.496  18.585  -4.980  1.00 69.68  ? 319 ALA A CA    1 
ATOM   2466 C  C     . ALA A 1 319 ? 1.786  19.382  -3.896  1.00 70.95  ? 319 ALA A C     1 
ATOM   2467 O  O     . ALA A 1 319 ? 1.717  20.614  -3.979  1.00 70.72  ? 319 ALA A O     1 
ATOM   2468 C  CB    . ALA A 1 319 ? 1.560  18.348  -6.165  1.00 71.17  ? 319 ALA A CB    1 
ATOM   2469 N  N     . GLN A 1 320 ? 1.254  18.705  -2.877  1.00 69.51  ? 320 GLN A N     1 
ATOM   2470 C  CA    . GLN A 1 320 ? 0.574  19.384  -1.783  1.00 68.66  ? 320 GLN A CA    1 
ATOM   2471 C  C     . GLN A 1 320 ? 1.536  19.948  -0.748  1.00 66.18  ? 320 GLN A C     1 
ATOM   2472 O  O     . GLN A 1 320 ? 1.089  20.625  0.184   1.00 64.25  ? 320 GLN A O     1 
ATOM   2473 C  CB    . GLN A 1 320 ? -0.407 18.426  -1.104  1.00 67.43  ? 320 GLN A CB    1 
ATOM   2474 C  CG    . GLN A 1 320 ? -1.294 17.663  -2.074  1.00 70.48  ? 320 GLN A CG    1 
ATOM   2475 C  CD    . GLN A 1 320 ? -2.181 18.576  -2.900  1.00 74.69  ? 320 GLN A CD    1 
ATOM   2476 O  OE1   . GLN A 1 320 ? -2.575 19.652  -2.450  1.00 76.92  ? 320 GLN A OE1   1 
ATOM   2477 N  NE2   . GLN A 1 320 ? -2.500 18.148  -4.117  1.00 78.73  ? 320 GLN A NE2   1 
ATOM   2478 N  N     . GLY A 1 321 ? 2.837  19.690  -0.886  1.00 66.93  ? 321 GLY A N     1 
ATOM   2479 C  CA    . GLY A 1 321 ? 3.822  20.170  0.055   1.00 62.69  ? 321 GLY A CA    1 
ATOM   2480 C  C     . GLY A 1 321 ? 4.155  19.217  1.181   1.00 63.19  ? 321 GLY A C     1 
ATOM   2481 O  O     . GLY A 1 321 ? 5.063  19.510  1.969   1.00 62.37  ? 321 GLY A O     1 
ATOM   2482 N  N     . ASN A 1 322 ? 3.453  18.092  1.289   1.00 61.21  ? 322 ASN A N     1 
ATOM   2483 C  CA    . ASN A 1 322 ? 3.729  17.130  2.344   1.00 58.99  ? 322 ASN A CA    1 
ATOM   2484 C  C     . ASN A 1 322 ? 4.939  16.275  1.985   1.00 59.48  ? 322 ASN A C     1 
ATOM   2485 O  O     . ASN A 1 322 ? 5.194  15.982  0.815   1.00 60.19  ? 322 ASN A O     1 
ATOM   2486 C  CB    . ASN A 1 322 ? 2.518  16.229  2.587   1.00 57.97  ? 322 ASN A CB    1 
ATOM   2487 C  CG    . ASN A 1 322 ? 1.236  17.012  2.779   1.00 63.92  ? 322 ASN A CG    1 
ATOM   2488 O  OD1   . ASN A 1 322 ? 0.409  17.097  1.872   1.00 65.80  ? 322 ASN A OD1   1 
ATOM   2489 N  ND2   . ASN A 1 322 ? 1.064  17.590  3.964   1.00 63.16  ? 322 ASN A ND2   1 
ATOM   2490 N  N     . LEU A 1 323 ? 5.688  15.879  3.009   1.00 58.05  ? 323 LEU A N     1 
ATOM   2491 C  CA    . LEU A 1 323 ? 6.813  14.965  2.843   1.00 53.88  ? 323 LEU A CA    1 
ATOM   2492 C  C     . LEU A 1 323 ? 6.279  13.538  2.899   1.00 50.97  ? 323 LEU A C     1 
ATOM   2493 O  O     . LEU A 1 323 ? 5.822  13.080  3.951   1.00 50.42  ? 323 LEU A O     1 
ATOM   2494 C  CB    . LEU A 1 323 ? 7.870  15.209  3.917   1.00 54.83  ? 323 LEU A CB    1 
ATOM   2495 C  CG    . LEU A 1 323 ? 9.159  14.389  3.815   1.00 52.11  ? 323 LEU A CG    1 
ATOM   2496 C  CD1   . LEU A 1 323 ? 9.872  14.666  2.502   1.00 48.50  ? 323 LEU A CD1   1 
ATOM   2497 C  CD2   . LEU A 1 323 ? 10.072 14.679  4.997   1.00 47.26  ? 323 LEU A CD2   1 
ATOM   2498 N  N     . ARG A 1 324 ? 6.324  12.841  1.766   1.00 49.45  ? 324 ARG A N     1 
ATOM   2499 C  CA    . ARG A 1 324 ? 5.785  11.493  1.647   1.00 51.12  ? 324 ARG A CA    1 
ATOM   2500 C  C     . ARG A 1 324 ? 6.915  10.474  1.729   1.00 49.34  ? 324 ARG A C     1 
ATOM   2501 O  O     . ARG A 1 324 ? 7.938  10.622  1.056   1.00 50.64  ? 324 ARG A O     1 
ATOM   2502 C  CB    . ARG A 1 324 ? 5.022  11.329  0.331   1.00 55.67  ? 324 ARG A CB    1 
ATOM   2503 C  CG    . ARG A 1 324 ? 3.750  12.160  0.225   1.00 56.87  ? 324 ARG A CG    1 
ATOM   2504 C  CD    . ARG A 1 324 ? 2.572  11.454  0.875   1.00 59.06  ? 324 ARG A CD    1 
ATOM   2505 N  NE    . ARG A 1 324 ? 1.388  12.303  0.936   1.00 64.77  ? 324 ARG A NE    1 
ATOM   2506 C  CZ    . ARG A 1 324 ? 0.199  11.899  1.361   1.00 64.69  ? 324 ARG A CZ    1 
ATOM   2507 N  NH1   . ARG A 1 324 ? -0.008 10.651  1.752   1.00 63.66  ? 324 ARG A NH1   1 
ATOM   2508 N  NH2   . ARG A 1 324 ? -0.809 12.767  1.393   1.00 68.96  ? 324 ARG A NH2   1 
ATOM   2509 N  N     . ALA A 1 325 ? 6.719  9.436   2.542   1.00 49.33  ? 325 ALA A N     1 
ATOM   2510 C  CA    . ALA A 1 325 ? 7.729  8.413   2.768   1.00 46.10  ? 325 ALA A CA    1 
ATOM   2511 C  C     . ALA A 1 325 ? 7.163  7.033   2.470   1.00 45.11  ? 325 ALA A C     1 
ATOM   2512 O  O     . ALA A 1 325 ? 5.978  6.771   2.692   1.00 43.58  ? 325 ALA A O     1 
ATOM   2513 C  CB    . ALA A 1 325 ? 8.245  8.444   4.208   1.00 44.12  ? 325 ALA A CB    1 
ATOM   2514 N  N     . ILE A 1 326 ? 8.028  6.151   1.961   1.00 43.50  ? 326 ILE A N     1 
ATOM   2515 C  CA    . ILE A 1 326 ? 7.715  4.738   1.786   1.00 42.73  ? 326 ILE A CA    1 
ATOM   2516 C  C     . ILE A 1 326 ? 8.852  3.911   2.368   1.00 39.14  ? 326 ILE A C     1 
ATOM   2517 O  O     . ILE A 1 326 ? 9.997  4.366   2.459   1.00 38.82  ? 326 ILE A O     1 
ATOM   2518 C  CB    . ILE A 1 326 ? 7.492  4.351   0.305   1.00 42.54  ? 326 ILE A CB    1 
ATOM   2519 C  CG1   . ILE A 1 326 ? 8.787  4.530   -0.493  1.00 47.79  ? 326 ILE A CG1   1 
ATOM   2520 C  CG2   . ILE A 1 326 ? 6.349  5.151   -0.302  1.00 50.40  ? 326 ILE A CG2   1 
ATOM   2521 C  CD1   . ILE A 1 326 ? 8.683  4.119   -1.947  1.00 53.33  ? 326 ILE A CD1   1 
ATOM   2522 N  N     . ASN A 1 327 ? 8.525  2.683   2.766   1.00 38.87  ? 327 ASN A N     1 
ATOM   2523 C  CA    . ASN A 1 327 ? 9.530  1.704   3.148   1.00 39.62  ? 327 ASN A CA    1 
ATOM   2524 C  C     . ASN A 1 327 ? 9.830  0.837   1.936   1.00 38.60  ? 327 ASN A C     1 
ATOM   2525 O  O     . ASN A 1 327 ? 8.975  0.032   1.540   1.00 45.17  ? 327 ASN A O     1 
ATOM   2526 C  CB    . ASN A 1 327 ? 9.035  0.848   4.314   1.00 40.11  ? 327 ASN A CB    1 
ATOM   2527 C  CG    . ASN A 1 327 ? 9.917  -0.369  4.574   1.00 42.28  ? 327 ASN A CG    1 
ATOM   2528 O  OD1   . ASN A 1 327 ? 11.108 -0.376  4.256   1.00 38.42  ? 327 ASN A OD1   1 
ATOM   2529 N  ND2   . ASN A 1 327 ? 9.327  -1.407  5.159   1.00 36.45  ? 327 ASN A ND2   1 
ATOM   2530 N  N     . PRO A 1 328 ? 11.007 0.959   1.312   1.00 41.68  ? 328 PRO A N     1 
ATOM   2531 C  CA    . PRO A 1 328 ? 11.284 0.195   0.085   1.00 43.02  ? 328 PRO A CA    1 
ATOM   2532 C  C     . PRO A 1 328 ? 11.557 -1.283  0.319   1.00 43.20  ? 328 PRO A C     1 
ATOM   2533 O  O     . PRO A 1 328 ? 11.720 -2.023  -0.659  1.00 43.43  ? 328 PRO A O     1 
ATOM   2534 C  CB    . PRO A 1 328 ? 12.528 0.896   -0.478  1.00 40.07  ? 328 PRO A CB    1 
ATOM   2535 C  CG    . PRO A 1 328 ? 13.230 1.400   0.743   1.00 38.38  ? 328 PRO A CG    1 
ATOM   2536 C  CD    . PRO A 1 328 ? 12.133 1.834   1.683   1.00 36.58  ? 328 PRO A CD    1 
ATOM   2537 N  N     . GLU A 1 329 ? 11.618 -1.730  1.569   1.00 40.21  ? 329 GLU A N     1 
ATOM   2538 C  CA    . GLU A 1 329 ? 11.926 -3.111  1.901   1.00 39.13  ? 329 GLU A CA    1 
ATOM   2539 C  C     . GLU A 1 329 ? 10.652 -3.943  2.019   1.00 39.22  ? 329 GLU A C     1 
ATOM   2540 O  O     . GLU A 1 329 ? 9.534  -3.426  2.023   1.00 41.66  ? 329 GLU A O     1 
ATOM   2541 C  CB    . GLU A 1 329 ? 12.723 -3.184  3.204   1.00 36.10  ? 329 GLU A CB    1 
ATOM   2542 C  CG    . GLU A 1 329 ? 14.131 -2.618  3.114   1.00 35.53  ? 329 GLU A CG    1 
ATOM   2543 C  CD    . GLU A 1 329 ? 14.975 -3.000  4.313   1.00 35.78  ? 329 GLU A CD    1 
ATOM   2544 O  OE1   . GLU A 1 329 ? 14.573 -2.684  5.448   1.00 38.99  ? 329 GLU A OE1   1 
ATOM   2545 O  OE2   . GLU A 1 329 ? 16.025 -3.642  4.124   1.00 37.30  ? 329 GLU A OE2   1 
ATOM   2546 N  N     . ASN A 1 330 ? 10.840 -5.257  2.131   1.00 35.69  ? 330 ASN A N     1 
ATOM   2547 C  CA    . ASN A 1 330 ? 9.736  -6.196  2.259   1.00 41.82  ? 330 ASN A CA    1 
ATOM   2548 C  C     . ASN A 1 330 ? 9.815  -7.026  3.534   1.00 43.67  ? 330 ASN A C     1 
ATOM   2549 O  O     . ASN A 1 330 ? 8.919  -7.842  3.783   1.00 38.55  ? 330 ASN A O     1 
ATOM   2550 C  CB    . ASN A 1 330 ? 9.686  -7.126  1.036   1.00 42.02  ? 330 ASN A CB    1 
ATOM   2551 C  CG    . ASN A 1 330 ? 8.314  -7.746  0.824   1.00 43.12  ? 330 ASN A CG    1 
ATOM   2552 O  OD1   . ASN A 1 330 ? 7.294  -7.173  1.208   1.00 43.95  ? 330 ASN A OD1   1 
ATOM   2553 N  ND2   . ASN A 1 330 ? 8.285  -8.926  0.215   1.00 39.86  ? 330 ASN A ND2   1 
ATOM   2554 N  N     . GLY A 1 331 ? 10.847 -6.838  4.348   1.00 41.70  ? 331 GLY A N     1 
ATOM   2555 C  CA    . GLY A 1 331 ? 10.988 -7.591  5.573   1.00 40.79  ? 331 GLY A CA    1 
ATOM   2556 C  C     . GLY A 1 331 ? 11.869 -6.863  6.566   1.00 39.83  ? 331 GLY A C     1 
ATOM   2557 O  O     . GLY A 1 331 ? 12.277 -5.721  6.346   1.00 38.62  ? 331 GLY A O     1 
ATOM   2558 N  N     . PHE A 1 332 ? 12.164 -7.550  7.668   1.00 37.46  ? 332 PHE A N     1 
ATOM   2559 C  CA    . PHE A 1 332 ? 12.953 -6.998  8.763   1.00 39.38  ? 332 PHE A CA    1 
ATOM   2560 C  C     . PHE A 1 332 ? 14.214 -7.830  8.934   1.00 34.72  ? 332 PHE A C     1 
ATOM   2561 O  O     . PHE A 1 332 ? 14.136 -9.040  9.171   1.00 40.96  ? 332 PHE A O     1 
ATOM   2562 C  CB    . PHE A 1 332 ? 12.148 -6.978  10.066  1.00 43.80  ? 332 PHE A CB    1 
ATOM   2563 C  CG    . PHE A 1 332 ? 10.861 -6.217  9.969   1.00 41.34  ? 332 PHE A CG    1 
ATOM   2564 C  CD1   . PHE A 1 332 ? 10.821 -4.976  9.357   1.00 39.86  ? 332 PHE A CD1   1 
ATOM   2565 C  CD2   . PHE A 1 332 ? 9.684  -6.754  10.465  1.00 38.19  ? 332 PHE A CD2   1 
ATOM   2566 C  CE1   . PHE A 1 332 ? 9.636  -4.276  9.255   1.00 41.09  ? 332 PHE A CE1   1 
ATOM   2567 C  CE2   . PHE A 1 332 ? 8.495  -6.060  10.367  1.00 48.63  ? 332 PHE A CE2   1 
ATOM   2568 C  CZ    . PHE A 1 332 ? 8.470  -4.817  9.763   1.00 48.66  ? 332 PHE A CZ    1 
ATOM   2569 N  N     . PHE A 1 333 ? 15.366 -7.181  8.817   1.00 36.99  ? 333 PHE A N     1 
ATOM   2570 C  CA    . PHE A 1 333 ? 16.665 -7.803  9.047   1.00 39.00  ? 333 PHE A CA    1 
ATOM   2571 C  C     . PHE A 1 333 ? 17.217 -7.258  10.361  1.00 35.92  ? 333 PHE A C     1 
ATOM   2572 O  O     . PHE A 1 333 ? 18.184 -6.493  10.397  1.00 38.05  ? 333 PHE A O     1 
ATOM   2573 C  CB    . PHE A 1 333 ? 17.599 -7.519  7.849   1.00 41.22  ? 333 PHE A CB    1 
ATOM   2574 C  CG    . PHE A 1 333 ? 18.858 -8.346  7.829   1.00 36.72  ? 333 PHE A CG    1 
ATOM   2575 C  CD1   . PHE A 1 333 ? 18.811 -9.709  7.571   1.00 42.11  ? 333 PHE A CD1   1 
ATOM   2576 C  CD2   . PHE A 1 333 ? 20.094 -7.748  8.030   1.00 38.47  ? 333 PHE A CD2   1 
ATOM   2577 C  CE1   . PHE A 1 333 ? 19.978 -10.468 7.538   1.00 41.96  ? 333 PHE A CE1   1 
ATOM   2578 C  CE2   . PHE A 1 333 ? 21.263 -8.496  7.999   1.00 41.61  ? 333 PHE A CE2   1 
ATOM   2579 C  CZ    . PHE A 1 333 ? 21.206 -9.857  7.750   1.00 42.09  ? 333 PHE A CZ    1 
ATOM   2580 N  N     . GLY A 1 334 ? 16.561 -7.649  11.459  1.00 38.96  ? 334 GLY A N     1 
ATOM   2581 C  CA    . GLY A 1 334 ? 16.781 -7.036  12.749  1.00 40.41  ? 334 GLY A CA    1 
ATOM   2582 C  C     . GLY A 1 334 ? 17.769 -7.777  13.628  1.00 40.14  ? 334 GLY A C     1 
ATOM   2583 O  O     . GLY A 1 334 ? 17.978 -8.979  13.492  1.00 42.49  ? 334 GLY A O     1 
ATOM   2584 N  N     . VAL A 1 335 ? 18.379 -7.027  14.547  1.00 40.34  ? 335 VAL A N     1 
ATOM   2585 C  CA    . VAL A 1 335 ? 19.307 -7.616  15.505  1.00 44.75  ? 335 VAL A CA    1 
ATOM   2586 C  C     . VAL A 1 335 ? 18.547 -8.538  16.450  1.00 46.71  ? 335 VAL A C     1 
ATOM   2587 O  O     . VAL A 1 335 ? 17.467 -8.194  16.951  1.00 41.78  ? 335 VAL A O     1 
ATOM   2588 C  CB    . VAL A 1 335 ? 20.051 -6.516  16.281  1.00 45.06  ? 335 VAL A CB    1 
ATOM   2589 C  CG1   . VAL A 1 335 ? 21.045 -7.130  17.258  1.00 46.14  ? 335 VAL A CG1   1 
ATOM   2590 C  CG2   . VAL A 1 335 ? 20.759 -5.574  15.319  1.00 46.55  ? 335 VAL A CG2   1 
ATOM   2591 N  N     . ALA A 1 336 ? 19.114 -9.721  16.702  1.00 44.02  ? 336 ALA A N     1 
ATOM   2592 C  CA    . ALA A 1 336 ? 18.454 -10.728 17.527  1.00 46.94  ? 336 ALA A CA    1 
ATOM   2593 C  C     . ALA A 1 336 ? 18.667 -10.499 19.027  1.00 45.33  ? 336 ALA A C     1 
ATOM   2594 O  O     . ALA A 1 336 ? 17.677 -10.423 19.766  1.00 43.00  ? 336 ALA A O     1 
ATOM   2595 C  CB    . ALA A 1 336 ? 18.912 -12.134 17.121  1.00 49.71  ? 336 ALA A CB    1 
ATOM   2596 N  N     . PRO A 1 337 ? 19.906 -10.386 19.528  1.00 44.68  ? 337 PRO A N     1 
ATOM   2597 C  CA    . PRO A 1 337 ? 20.087 -10.261 20.982  1.00 44.62  ? 337 PRO A CA    1 
ATOM   2598 C  C     . PRO A 1 337 ? 19.383 -9.032  21.542  1.00 50.13  ? 337 PRO A C     1 
ATOM   2599 O  O     . PRO A 1 337 ? 19.363 -7.963  20.926  1.00 49.54  ? 337 PRO A O     1 
ATOM   2600 C  CB    . PRO A 1 337 ? 21.608 -10.157 21.146  1.00 46.16  ? 337 PRO A CB    1 
ATOM   2601 C  CG    . PRO A 1 337 ? 22.166 -10.774 19.922  1.00 46.97  ? 337 PRO A CG    1 
ATOM   2602 C  CD    . PRO A 1 337 ? 21.209 -10.398 18.835  1.00 44.00  ? 337 PRO A CD    1 
ATOM   2603 N  N     . GLY A 1 338 ? 18.805 -9.197  22.731  1.00 45.89  ? 338 GLY A N     1 
ATOM   2604 C  CA    . GLY A 1 338 ? 18.015 -8.167  23.357  1.00 46.39  ? 338 GLY A CA    1 
ATOM   2605 C  C     . GLY A 1 338 ? 16.536 -8.226  23.046  1.00 52.48  ? 338 GLY A C     1 
ATOM   2606 O  O     . GLY A 1 338 ? 15.738 -7.633  23.782  1.00 55.83  ? 338 GLY A O     1 
ATOM   2607 N  N     . THR A 1 339 ? 16.146 -8.919  21.979  1.00 46.13  ? 339 THR A N     1 
ATOM   2608 C  CA    . THR A 1 339 ? 14.735 -9.067  21.650  1.00 47.99  ? 339 THR A CA    1 
ATOM   2609 C  C     . THR A 1 339 ? 14.081 -10.041 22.626  1.00 56.94  ? 339 THR A C     1 
ATOM   2610 O  O     . THR A 1 339 ? 14.429 -11.226 22.657  1.00 53.58  ? 339 THR A O     1 
ATOM   2611 C  CB    . THR A 1 339 ? 14.578 -9.557  20.211  1.00 48.38  ? 339 THR A CB    1 
ATOM   2612 O  OG1   . THR A 1 339 ? 15.355 -8.731  19.336  1.00 50.60  ? 339 THR A OG1   1 
ATOM   2613 C  CG2   . THR A 1 339 ? 13.122 -9.501  19.778  1.00 50.29  ? 339 THR A CG2   1 
ATOM   2614 N  N     . SER A 1 340 ? 13.140 -9.541  23.425  1.00 55.19  ? 340 SER A N     1 
ATOM   2615 C  CA    . SER A 1 340 ? 12.398 -10.368 24.365  1.00 60.74  ? 340 SER A CA    1 
ATOM   2616 C  C     . SER A 1 340 ? 10.930 -9.970  24.314  1.00 63.13  ? 340 SER A C     1 
ATOM   2617 O  O     . SER A 1 340 ? 10.518 -9.118  23.521  1.00 62.76  ? 340 SER A O     1 
ATOM   2618 C  CB    . SER A 1 340 ? 12.955 -10.240 25.788  1.00 58.25  ? 340 SER A CB    1 
ATOM   2619 O  OG    . SER A 1 340 ? 12.724 -8.946  26.319  1.00 66.87  ? 340 SER A OG    1 
ATOM   2620 N  N     . VAL A 1 341 ? 10.133 -10.605 25.174  1.00 63.72  ? 341 VAL A N     1 
ATOM   2621 C  CA    . VAL A 1 341 ? 8.715  -10.286 25.253  1.00 70.91  ? 341 VAL A CA    1 
ATOM   2622 C  C     . VAL A 1 341 ? 8.482  -8.938  25.923  1.00 67.99  ? 341 VAL A C     1 
ATOM   2623 O  O     . VAL A 1 341 ? 7.448  -8.302  25.690  1.00 70.16  ? 341 VAL A O     1 
ATOM   2624 C  CB    . VAL A 1 341 ? 7.967  -11.411 25.994  1.00 73.14  ? 341 VAL A CB    1 
ATOM   2625 C  CG1   . VAL A 1 341 ? 6.457  -11.259 25.841  1.00 71.67  ? 341 VAL A CG1   1 
ATOM   2626 C  CG2   . VAL A 1 341 ? 8.427  -12.767 25.483  1.00 74.47  ? 341 VAL A CG2   1 
ATOM   2627 N  N     . LYS A 1 342 ? 9.420  -8.476  26.749  1.00 65.29  ? 342 LYS A N     1 
ATOM   2628 C  CA    . LYS A 1 342 ? 9.238  -7.206  27.438  1.00 66.75  ? 342 LYS A CA    1 
ATOM   2629 C  C     . LYS A 1 342 ? 9.826  -6.030  26.670  1.00 66.58  ? 342 LYS A C     1 
ATOM   2630 O  O     . LYS A 1 342 ? 9.331  -4.905  26.809  1.00 69.67  ? 342 LYS A O     1 
ATOM   2631 C  CB    . LYS A 1 342 ? 9.851  -7.271  28.841  1.00 73.83  ? 342 LYS A CB    1 
ATOM   2632 C  CG    . LYS A 1 342 ? 11.368 -7.355  28.869  1.00 80.23  ? 342 LYS A CG    1 
ATOM   2633 C  CD    . LYS A 1 342 ? 11.892 -7.335  30.298  1.00 87.12  ? 342 LYS A CD    1 
ATOM   2634 C  CE    . LYS A 1 342 ? 13.411 -7.232  30.329  1.00 95.55  ? 342 LYS A CE    1 
ATOM   2635 N  NZ    . LYS A 1 342 ? 13.901 -5.955  29.730  1.00 91.97  ? 342 LYS A NZ    1 
ATOM   2636 N  N     . THR A 1 343 ? 10.860 -6.256  25.858  1.00 62.08  ? 343 THR A N     1 
ATOM   2637 C  CA    . THR A 1 343 ? 11.470 -5.189  25.074  1.00 61.89  ? 343 THR A CA    1 
ATOM   2638 C  C     . THR A 1 343 ? 10.901 -5.077  23.669  1.00 56.83  ? 343 THR A C     1 
ATOM   2639 O  O     . THR A 1 343 ? 10.870 -3.976  23.114  1.00 61.30  ? 343 THR A O     1 
ATOM   2640 C  CB    . THR A 1 343 ? 12.988 -5.386  24.969  1.00 58.97  ? 343 THR A CB    1 
ATOM   2641 O  OG1   . THR A 1 343 ? 13.268 -6.573  24.216  1.00 60.10  ? 343 THR A OG1   1 
ATOM   2642 C  CG2   . THR A 1 343 ? 13.618 -5.495  26.349  1.00 61.34  ? 343 THR A CG2   1 
ATOM   2643 N  N     . ASN A 1 344 ? 10.467 -6.182  23.074  1.00 56.99  ? 344 ASN A N     1 
ATOM   2644 C  CA    . ASN A 1 344 ? 9.914  -6.122  21.728  1.00 55.63  ? 344 ASN A CA    1 
ATOM   2645 C  C     . ASN A 1 344 ? 8.984  -7.306  21.497  1.00 58.12  ? 344 ASN A C     1 
ATOM   2646 O  O     . ASN A 1 344 ? 9.317  -8.217  20.728  1.00 56.14  ? 344 ASN A O     1 
ATOM   2647 C  CB    . ASN A 1 344 ? 11.036 -6.102  20.687  1.00 56.30  ? 344 ASN A CB    1 
ATOM   2648 C  CG    . ASN A 1 344 ? 10.593 -5.519  19.359  1.00 48.96  ? 344 ASN A CG    1 
ATOM   2649 O  OD1   . ASN A 1 344 ? 9.401  -5.465  19.055  1.00 49.22  ? 344 ASN A OD1   1 
ATOM   2650 N  ND2   . ASN A 1 344 ? 11.555 -5.085  18.555  1.00 53.97  ? 344 ASN A ND2   1 
ATOM   2651 N  N     . PRO A 1 345 ? 7.813  -7.329  22.143  1.00 60.11  ? 345 PRO A N     1 
ATOM   2652 C  CA    . PRO A 1 345 ? 6.907  -8.473  21.959  1.00 57.57  ? 345 PRO A CA    1 
ATOM   2653 C  C     . PRO A 1 345 ? 6.349  -8.578  20.552  1.00 53.73  ? 345 PRO A C     1 
ATOM   2654 O  O     . PRO A 1 345 ? 5.994  -9.683  20.122  1.00 55.14  ? 345 PRO A O     1 
ATOM   2655 C  CB    . PRO A 1 345 ? 5.798  -8.208  22.986  1.00 56.90  ? 345 PRO A CB    1 
ATOM   2656 C  CG    . PRO A 1 345 ? 5.808  -6.724  23.163  1.00 61.88  ? 345 PRO A CG    1 
ATOM   2657 C  CD    . PRO A 1 345 ? 7.251  -6.320  23.057  1.00 58.77  ? 345 PRO A CD    1 
ATOM   2658 N  N     . ASN A 1 346 ? 6.252  -7.465  19.823  1.00 52.20  ? 346 ASN A N     1 
ATOM   2659 C  CA    . ASN A 1 346 ? 5.748  -7.534  18.457  1.00 53.44  ? 346 ASN A CA    1 
ATOM   2660 C  C     . ASN A 1 346 ? 6.739  -8.221  17.527  1.00 56.73  ? 346 ASN A C     1 
ATOM   2661 O  O     . ASN A 1 346 ? 6.329  -8.875  16.561  1.00 54.42  ? 346 ASN A O     1 
ATOM   2662 C  CB    . ASN A 1 346 ? 5.414  -6.133  17.951  1.00 50.04  ? 346 ASN A CB    1 
ATOM   2663 C  CG    . ASN A 1 346 ? 4.240  -5.519  18.684  1.00 59.30  ? 346 ASN A CG    1 
ATOM   2664 O  OD1   . ASN A 1 346 ? 4.354  -4.445  19.279  1.00 54.45  ? 346 ASN A OD1   1 
ATOM   2665 N  ND2   . ASN A 1 346 ? 3.102  -6.203  18.650  1.00 48.42  ? 346 ASN A ND2   1 
ATOM   2666 N  N     . ALA A 1 347 ? 8.040  -8.086  17.798  1.00 53.99  ? 347 ALA A N     1 
ATOM   2667 C  CA    . ALA A 1 347 ? 9.032  -8.819  17.022  1.00 53.80  ? 347 ALA A CA    1 
ATOM   2668 C  C     . ALA A 1 347 ? 8.997  -10.307 17.338  1.00 54.40  ? 347 ALA A C     1 
ATOM   2669 O  O     . ALA A 1 347 ? 9.237  -11.132 16.450  1.00 53.46  ? 347 ALA A O     1 
ATOM   2670 C  CB    . ALA A 1 347 ? 10.428 -8.252  17.278  1.00 45.81  ? 347 ALA A CB    1 
ATOM   2671 N  N     . ILE A 1 348 ? 8.699  -10.668 18.589  1.00 60.89  ? 348 ILE A N     1 
ATOM   2672 C  CA    . ILE A 1 348 ? 8.606  -12.077 18.960  1.00 50.63  ? 348 ILE A CA    1 
ATOM   2673 C  C     . ILE A 1 348 ? 7.481  -12.754 18.190  1.00 57.82  ? 348 ILE A C     1 
ATOM   2674 O  O     . ILE A 1 348 ? 7.632  -13.880 17.700  1.00 58.33  ? 348 ILE A O     1 
ATOM   2675 C  CB    . ILE A 1 348 ? 8.416  -12.218 20.482  1.00 54.82  ? 348 ILE A CB    1 
ATOM   2676 C  CG1   . ILE A 1 348 ? 9.620  -11.642 21.229  1.00 56.84  ? 348 ILE A CG1   1 
ATOM   2677 C  CG2   . ILE A 1 348 ? 8.195  -13.674 20.864  1.00 59.33  ? 348 ILE A CG2   1 
ATOM   2678 C  CD1   . ILE A 1 348 ? 10.926 -12.347 20.934  1.00 53.76  ? 348 ILE A CD1   1 
ATOM   2679 N  N     . LYS A 1 349 ? 6.337  -12.077 18.063  1.00 53.01  ? 349 LYS A N     1 
ATOM   2680 C  CA    . LYS A 1 349 ? 5.218  -12.630 17.312  1.00 53.43  ? 349 LYS A CA    1 
ATOM   2681 C  C     . LYS A 1 349 ? 5.510  -12.729 15.821  1.00 60.20  ? 349 LYS A C     1 
ATOM   2682 O  O     . LYS A 1 349 ? 4.914  -13.573 15.142  1.00 60.02  ? 349 LYS A O     1 
ATOM   2683 C  CB    . LYS A 1 349 ? 3.964  -11.783 17.538  1.00 53.61  ? 349 LYS A CB    1 
ATOM   2684 C  CG    . LYS A 1 349 ? 3.543  -11.684 18.991  1.00 67.85  ? 349 LYS A CG    1 
ATOM   2685 C  CD    . LYS A 1 349 ? 2.261  -10.887 19.134  1.00 74.07  ? 349 LYS A CD    1 
ATOM   2686 C  CE    . LYS A 1 349 ? 1.878  -10.723 20.590  1.00 75.20  ? 349 LYS A CE    1 
ATOM   2687 N  NZ    . LYS A 1 349 ? 0.598  -9.983  20.736  1.00 84.65  ? 349 LYS A NZ    1 
ATOM   2688 N  N     . THR A 1 350 ? 6.414  -11.890 15.302  1.00 58.49  ? 350 THR A N     1 
ATOM   2689 C  CA    . THR A 1 350 ? 6.686  -11.868 13.869  1.00 56.11  ? 350 THR A CA    1 
ATOM   2690 C  C     . THR A 1 350 ? 7.605  -13.008 13.444  1.00 50.77  ? 350 THR A C     1 
ATOM   2691 O  O     . THR A 1 350 ? 7.393  -13.618 12.390  1.00 50.69  ? 350 THR A O     1 
ATOM   2692 C  CB    . THR A 1 350 ? 7.307  -10.526 13.473  1.00 55.16  ? 350 THR A CB    1 
ATOM   2693 O  OG1   . THR A 1 350 ? 6.455  -9.457  13.892  1.00 55.35  ? 350 THR A OG1   1 
ATOM   2694 C  CG2   . THR A 1 350 ? 7.496  -10.445 11.964  1.00 52.71  ? 350 THR A CG2   1 
ATOM   2695 N  N     . ILE A 1 351 ? 8.622  -13.313 14.247  1.00 51.84  ? 351 ILE A N     1 
ATOM   2696 C  CA    . ILE A 1 351 ? 9.665  -14.252 13.849  1.00 51.99  ? 351 ILE A CA    1 
ATOM   2697 C  C     . ILE A 1 351 ? 9.260  -15.682 14.185  1.00 58.05  ? 351 ILE A C     1 
ATOM   2698 O  O     . ILE A 1 351 ? 10.092 -16.596 14.154  1.00 56.03  ? 351 ILE A O     1 
ATOM   2699 C  CB    . ILE A 1 351 ? 11.006 -13.892 14.512  1.00 45.45  ? 351 ILE A CB    1 
ATOM   2700 C  CG1   . ILE A 1 351 ? 10.870 -13.919 16.034  1.00 48.78  ? 351 ILE A CG1   1 
ATOM   2701 C  CG2   . ILE A 1 351 ? 11.479 -12.528 14.043  1.00 46.64  ? 351 ILE A CG2   1 
ATOM   2702 C  CD1   . ILE A 1 351 ? 12.141 -13.561 16.766  1.00 48.78  ? 351 ILE A CD1   1 
ATOM   2703 N  N     . GLN A 1 352 ? 7.977  -15.886 14.498  1.00 68.05  ? 352 GLN A N     1 
ATOM   2704 C  CA    . GLN A 1 352 ? 7.489  -17.217 14.842  1.00 65.61  ? 352 GLN A CA    1 
ATOM   2705 C  C     . GLN A 1 352 ? 7.474  -18.165 13.651  1.00 67.05  ? 352 GLN A C     1 
ATOM   2706 O  O     . GLN A 1 352 ? 7.480  -19.384 13.851  1.00 66.73  ? 352 GLN A O     1 
ATOM   2707 C  CB    . GLN A 1 352 ? 6.078  -17.136 15.429  1.00 71.58  ? 352 GLN A CB    1 
ATOM   2708 C  CG    . GLN A 1 352 ? 5.984  -16.430 16.768  1.00 77.90  ? 352 GLN A CG    1 
ATOM   2709 C  CD    . GLN A 1 352 ? 6.623  -17.216 17.896  1.00 82.52  ? 352 GLN A CD    1 
ATOM   2710 O  OE1   . GLN A 1 352 ? 6.816  -18.427 17.795  1.00 88.83  ? 352 GLN A OE1   1 
ATOM   2711 N  NE2   . GLN A 1 352 ? 6.953  -16.527 18.981  1.00 81.99  ? 352 GLN A NE2   1 
ATOM   2712 N  N     . LYS A 1 353 ? 7.443  -17.644 12.426  1.00 56.93  ? 353 LYS A N     1 
ATOM   2713 C  CA    . LYS A 1 353 ? 7.318  -18.502 11.260  1.00 54.30  ? 353 LYS A CA    1 
ATOM   2714 C  C     . LYS A 1 353 ? 7.912  -17.812 10.042  1.00 56.89  ? 353 LYS A C     1 
ATOM   2715 O  O     . LYS A 1 353 ? 8.016  -16.582 9.983   1.00 52.43  ? 353 LYS A O     1 
ATOM   2716 C  CB    . LYS A 1 353 ? 5.856  -18.884 11.001  1.00 56.91  ? 353 LYS A CB    1 
ATOM   2717 C  CG    . LYS A 1 353 ? 4.936  -17.708 10.739  1.00 55.40  ? 353 LYS A CG    1 
ATOM   2718 C  CD    . LYS A 1 353 ? 3.508  -18.181 10.523  1.00 60.58  ? 353 LYS A CD    1 
ATOM   2719 C  CE    . LYS A 1 353 ? 2.566  -17.014 10.295  1.00 64.50  ? 353 LYS A CE    1 
ATOM   2720 N  NZ    . LYS A 1 353 ? 1.157  -17.470 10.143  1.00 79.77  ? 353 LYS A NZ    1 
ATOM   2721 N  N     . ASN A 1 354 ? 8.313  -18.637 9.068   1.00 53.97  ? 354 ASN A N     1 
ATOM   2722 C  CA    . ASN A 1 354 ? 8.825  -18.166 7.780   1.00 46.48  ? 354 ASN A CA    1 
ATOM   2723 C  C     . ASN A 1 354 ? 10.029 -17.246 7.957   1.00 45.35  ? 354 ASN A C     1 
ATOM   2724 O  O     . ASN A 1 354 ? 10.223 -16.294 7.198   1.00 49.83  ? 354 ASN A O     1 
ATOM   2725 C  CB    . ASN A 1 354 ? 7.723  -17.476 6.975   1.00 45.38  ? 354 ASN A CB    1 
ATOM   2726 C  CG    . ASN A 1 354 ? 6.518  -18.368 6.761   1.00 46.46  ? 354 ASN A CG    1 
ATOM   2727 O  OD1   . ASN A 1 354 ? 6.655  -19.569 6.544   1.00 53.48  ? 354 ASN A OD1   1 
ATOM   2728 N  ND2   . ASN A 1 354 ? 5.329  -17.785 6.829   1.00 51.73  ? 354 ASN A ND2   1 
ATOM   2729 N  N     . THR A 1 355 ? 10.857 -17.543 8.953   1.00 43.73  ? 355 THR A N     1 
ATOM   2730 C  CA    . THR A 1 355 ? 11.920 -16.645 9.381   1.00 49.17  ? 355 THR A CA    1 
ATOM   2731 C  C     . THR A 1 355 ? 13.264 -17.352 9.313   1.00 46.08  ? 355 THR A C     1 
ATOM   2732 O  O     . THR A 1 355 ? 13.390 -18.507 9.730   1.00 42.57  ? 355 THR A O     1 
ATOM   2733 C  CB    . THR A 1 355 ? 11.655 -16.139 10.805  1.00 46.15  ? 355 THR A CB    1 
ATOM   2734 O  OG1   . THR A 1 355 ? 10.399 -15.450 10.835  1.00 46.98  ? 355 THR A OG1   1 
ATOM   2735 C  CG2   . THR A 1 355 ? 12.757 -15.199 11.268  1.00 39.90  ? 355 THR A CG2   1 
ATOM   2736 N  N     . ILE A 1 356 ? 14.265 -16.656 8.780   1.00 41.52  ? 356 ILE A N     1 
ATOM   2737 C  CA    . ILE A 1 356 ? 15.627 -17.171 8.692   1.00 45.70  ? 356 ILE A CA    1 
ATOM   2738 C  C     . ILE A 1 356 ? 16.465 -16.462 9.746   1.00 38.34  ? 356 ILE A C     1 
ATOM   2739 O  O     . ILE A 1 356 ? 16.563 -15.231 9.747   1.00 40.19  ? 356 ILE A O     1 
ATOM   2740 C  CB    . ILE A 1 356 ? 16.224 -16.979 7.288   1.00 43.11  ? 356 ILE A CB    1 
ATOM   2741 C  CG1   . ILE A 1 356 ? 15.376 -17.705 6.242   1.00 43.32  ? 356 ILE A CG1   1 
ATOM   2742 C  CG2   . ILE A 1 356 ? 17.661 -17.490 7.238   1.00 38.57  ? 356 ILE A CG2   1 
ATOM   2743 C  CD1   . ILE A 1 356 ? 15.987 -17.710 4.862   1.00 45.20  ? 356 ILE A CD1   1 
ATOM   2744 N  N     . PHE A 1 357 ? 17.061 -17.237 10.643  1.00 40.34  ? 357 PHE A N     1 
ATOM   2745 C  CA    . PHE A 1 357 ? 17.965 -16.721 11.658  1.00 41.30  ? 357 PHE A CA    1 
ATOM   2746 C  C     . PHE A 1 357 ? 19.404 -16.996 11.242  1.00 41.10  ? 357 PHE A C     1 
ATOM   2747 O  O     . PHE A 1 357 ? 19.687 -17.961 10.529  1.00 45.01  ? 357 PHE A O     1 
ATOM   2748 C  CB    . PHE A 1 357 ? 17.687 -17.361 13.023  1.00 41.70  ? 357 PHE A CB    1 
ATOM   2749 C  CG    . PHE A 1 357 ? 16.298 -17.115 13.544  1.00 43.32  ? 357 PHE A CG    1 
ATOM   2750 C  CD1   . PHE A 1 357 ? 15.245 -17.932 13.162  1.00 42.19  ? 357 PHE A CD1   1 
ATOM   2751 C  CD2   . PHE A 1 357 ? 16.046 -16.071 14.423  1.00 47.89  ? 357 PHE A CD2   1 
ATOM   2752 C  CE1   . PHE A 1 357 ? 13.966 -17.708 13.641  1.00 45.49  ? 357 PHE A CE1   1 
ATOM   2753 C  CE2   . PHE A 1 357 ? 14.768 -15.845 14.908  1.00 42.95  ? 357 PHE A CE2   1 
ATOM   2754 C  CZ    . PHE A 1 357 ? 13.727 -16.665 14.517  1.00 42.99  ? 357 PHE A CZ    1 
ATOM   2755 N  N     . THR A 1 358 ? 20.314 -16.138 11.695  1.00 42.60  ? 358 THR A N     1 
ATOM   2756 C  CA    . THR A 1 358 ? 21.727 -16.262 11.350  1.00 46.02  ? 358 THR A CA    1 
ATOM   2757 C  C     . THR A 1 358 ? 22.561 -16.048 12.602  1.00 43.00  ? 358 THR A C     1 
ATOM   2758 O  O     . THR A 1 358 ? 22.479 -14.987 13.226  1.00 46.94  ? 358 THR A O     1 
ATOM   2759 C  CB    . THR A 1 358 ? 22.129 -15.258 10.262  1.00 46.87  ? 358 THR A CB    1 
ATOM   2760 O  OG1   . THR A 1 358 ? 21.394 -15.526 9.062   1.00 43.76  ? 358 THR A OG1   1 
ATOM   2761 C  CG2   . THR A 1 358 ? 23.617 -15.361 9.968   1.00 41.38  ? 358 THR A CG2   1 
ATOM   2762 N  N     . ASN A 1 359 ? 23.347 -17.063 12.966  1.00 46.63  ? 359 ASN A N     1 
ATOM   2763 C  CA    . ASN A 1 359 ? 24.319 -16.991 14.060  1.00 50.91  ? 359 ASN A CA    1 
ATOM   2764 C  C     . ASN A 1 359 ? 23.660 -16.791 15.424  1.00 49.82  ? 359 ASN A C     1 
ATOM   2765 O  O     . ASN A 1 359 ? 24.250 -16.189 16.324  1.00 58.31  ? 359 ASN A O     1 
ATOM   2766 C  CB    . ASN A 1 359 ? 25.365 -15.899 13.803  1.00 50.31  ? 359 ASN A CB    1 
ATOM   2767 C  CG    . ASN A 1 359 ? 26.265 -16.224 12.628  1.00 47.44  ? 359 ASN A CG    1 
ATOM   2768 O  OD1   . ASN A 1 359 ? 26.423 -17.387 12.259  1.00 50.29  ? 359 ASN A OD1   1 
ATOM   2769 N  ND2   . ASN A 1 359 ? 26.859 -15.199 12.032  1.00 46.00  ? 359 ASN A ND2   1 
ATOM   2770 N  N     . VAL A 1 360 ? 22.439 -17.290 15.598  1.00 53.31  ? 360 VAL A N     1 
ATOM   2771 C  CA    . VAL A 1 360 ? 21.823 -17.378 16.915  1.00 48.96  ? 360 VAL A CA    1 
ATOM   2772 C  C     . VAL A 1 360 ? 21.967 -18.812 17.406  1.00 53.43  ? 360 VAL A C     1 
ATOM   2773 O  O     . VAL A 1 360 ? 22.203 -19.743 16.631  1.00 50.58  ? 360 VAL A O     1 
ATOM   2774 C  CB    . VAL A 1 360 ? 20.338 -16.946 16.917  1.00 50.67  ? 360 VAL A CB    1 
ATOM   2775 C  CG1   . VAL A 1 360 ? 20.174 -15.568 16.299  1.00 46.79  ? 360 VAL A CG1   1 
ATOM   2776 C  CG2   . VAL A 1 360 ? 19.475 -17.984 16.209  1.00 43.89  ? 360 VAL A CG2   1 
ATOM   2777 N  N     . ALA A 1 361 ? 21.820 -18.997 18.716  1.00 54.99  ? 361 ALA A N     1 
ATOM   2778 C  CA    . ALA A 1 361 ? 21.958 -20.320 19.307  1.00 56.27  ? 361 ALA A CA    1 
ATOM   2779 C  C     . ALA A 1 361 ? 20.701 -21.150 19.082  1.00 49.43  ? 361 ALA A C     1 
ATOM   2780 O  O     . ALA A 1 361 ? 19.593 -20.622 18.961  1.00 48.97  ? 361 ALA A O     1 
ATOM   2781 C  CB    . ALA A 1 361 ? 22.247 -20.218 20.805  1.00 57.35  ? 361 ALA A CB    1 
ATOM   2782 N  N     . GLU A 1 362 ? 20.887 -22.466 19.026  1.00 52.94  ? 362 GLU A N     1 
ATOM   2783 C  CA    . GLU A 1 362 ? 19.797 -23.415 18.858  1.00 51.84  ? 362 GLU A CA    1 
ATOM   2784 C  C     . GLU A 1 362 ? 19.607 -24.201 20.147  1.00 54.21  ? 362 GLU A C     1 
ATOM   2785 O  O     . GLU A 1 362 ? 20.584 -24.598 20.791  1.00 58.10  ? 362 GLU A O     1 
ATOM   2786 C  CB    . GLU A 1 362 ? 20.074 -24.375 17.693  1.00 54.62  ? 362 GLU A CB    1 
ATOM   2787 C  CG    . GLU A 1 362 ? 18.982 -25.421 17.460  1.00 54.82  ? 362 GLU A CG    1 
ATOM   2788 C  CD    . GLU A 1 362 ? 19.322 -26.394 16.336  1.00 60.63  ? 362 GLU A CD    1 
ATOM   2789 O  OE1   . GLU A 1 362 ? 20.412 -26.266 15.740  1.00 62.00  ? 362 GLU A OE1   1 
ATOM   2790 O  OE2   . GLU A 1 362 ? 18.498 -27.289 16.049  1.00 58.29  ? 362 GLU A OE2   1 
ATOM   2791 N  N     . THR A 1 363 ? 18.351 -24.412 20.527  1.00 55.08  ? 363 THR A N     1 
ATOM   2792 C  CA    . THR A 1 363 ? 18.043 -25.247 21.676  1.00 56.92  ? 363 THR A CA    1 
ATOM   2793 C  C     . THR A 1 363 ? 17.765 -26.679 21.226  1.00 59.88  ? 363 THR A C     1 
ATOM   2794 O  O     . THR A 1 363 ? 17.405 -26.937 20.075  1.00 56.63  ? 363 THR A O     1 
ATOM   2795 C  CB    . THR A 1 363 ? 16.847 -24.695 22.455  1.00 57.79  ? 363 THR A CB    1 
ATOM   2796 O  OG1   . THR A 1 363 ? 15.659 -24.795 21.661  1.00 57.17  ? 363 THR A OG1   1 
ATOM   2797 C  CG2   . THR A 1 363 ? 17.080 -23.241 22.827  1.00 58.27  ? 363 THR A CG2   1 
ATOM   2798 N  N     . SER A 1 364 ? 17.938 -27.617 22.161  1.00 60.00  ? 364 SER A N     1 
ATOM   2799 C  CA    . SER A 1 364 ? 17.826 -29.033 21.827  1.00 61.05  ? 364 SER A CA    1 
ATOM   2800 C  C     . SER A 1 364 ? 16.427 -29.417 21.365  1.00 61.26  ? 364 SER A C     1 
ATOM   2801 O  O     . SER A 1 364 ? 16.275 -30.419 20.658  1.00 61.46  ? 364 SER A O     1 
ATOM   2802 C  CB    . SER A 1 364 ? 18.232 -29.887 23.028  1.00 63.60  ? 364 SER A CB    1 
ATOM   2803 O  OG    . SER A 1 364 ? 17.473 -29.542 24.171  1.00 65.17  ? 364 SER A OG    1 
ATOM   2804 N  N     . ASP A 1 365 ? 15.406 -28.651 21.740  1.00 61.33  ? 365 ASP A N     1 
ATOM   2805 C  CA    . ASP A 1 365 ? 14.044 -28.904 21.292  1.00 61.58  ? 365 ASP A CA    1 
ATOM   2806 C  C     . ASP A 1 365 ? 13.718 -28.201 19.978  1.00 62.34  ? 365 ASP A C     1 
ATOM   2807 O  O     . ASP A 1 365 ? 12.547 -28.159 19.585  1.00 63.91  ? 365 ASP A O     1 
ATOM   2808 C  CB    . ASP A 1 365 ? 13.040 -28.495 22.377  1.00 63.14  ? 365 ASP A CB    1 
ATOM   2809 C  CG    . ASP A 1 365 ? 13.118 -27.018 22.734  1.00 69.34  ? 365 ASP A CG    1 
ATOM   2810 O  OD1   . ASP A 1 365 ? 14.058 -26.329 22.279  1.00 67.77  ? 365 ASP A OD1   1 
ATOM   2811 O  OD2   . ASP A 1 365 ? 12.226 -26.542 23.473  1.00 70.29  ? 365 ASP A OD2   1 
ATOM   2812 N  N     . GLY A 1 366 ? 14.719 -27.649 19.296  1.00 61.76  ? 366 GLY A N     1 
ATOM   2813 C  CA    . GLY A 1 366 ? 14.514 -27.053 17.992  1.00 57.96  ? 366 GLY A CA    1 
ATOM   2814 C  C     . GLY A 1 366 ? 14.141 -25.590 17.988  1.00 62.81  ? 366 GLY A C     1 
ATOM   2815 O  O     . GLY A 1 366 ? 13.587 -25.115 16.990  1.00 65.23  ? 366 GLY A O     1 
ATOM   2816 N  N     . GLY A 1 367 ? 14.422 -24.857 19.066  1.00 59.48  ? 367 GLY A N     1 
ATOM   2817 C  CA    . GLY A 1 367 ? 14.148 -23.442 19.145  1.00 53.43  ? 367 GLY A CA    1 
ATOM   2818 C  C     . GLY A 1 367 ? 15.415 -22.603 19.084  1.00 53.83  ? 367 GLY A C     1 
ATOM   2819 O  O     . GLY A 1 367 ? 16.525 -23.101 18.911  1.00 55.23  ? 367 GLY A O     1 
ATOM   2820 N  N     . VAL A 1 368 ? 15.217 -21.295 19.232  1.00 51.53  ? 368 VAL A N     1 
ATOM   2821 C  CA    . VAL A 1 368 ? 16.300 -20.322 19.158  1.00 55.98  ? 368 VAL A CA    1 
ATOM   2822 C  C     . VAL A 1 368 ? 16.573 -19.766 20.550  1.00 52.86  ? 368 VAL A C     1 
ATOM   2823 O  O     . VAL A 1 368 ? 15.737 -19.835 21.456  1.00 52.35  ? 368 VAL A O     1 
ATOM   2824 C  CB    . VAL A 1 368 ? 15.993 -19.176 18.171  1.00 48.43  ? 368 VAL A CB    1 
ATOM   2825 C  CG1   . VAL A 1 368 ? 15.876 -19.707 16.750  1.00 46.65  ? 368 VAL A CG1   1 
ATOM   2826 C  CG2   . VAL A 1 368 ? 14.725 -18.450 18.583  1.00 48.03  ? 368 VAL A CG2   1 
ATOM   2827 N  N     . TYR A 1 369 ? 17.766 -19.196 20.710  1.00 51.25  ? 369 TYR A N     1 
ATOM   2828 C  CA    . TYR A 1 369 ? 18.159 -18.611 21.984  1.00 55.95  ? 369 TYR A CA    1 
ATOM   2829 C  C     . TYR A 1 369 ? 19.256 -17.580 21.754  1.00 50.11  ? 369 TYR A C     1 
ATOM   2830 O  O     . TYR A 1 369 ? 20.117 -17.764 20.890  1.00 52.50  ? 369 TYR A O     1 
ATOM   2831 C  CB    . TYR A 1 369 ? 18.640 -19.686 22.962  1.00 53.57  ? 369 TYR A CB    1 
ATOM   2832 C  CG    . TYR A 1 369 ? 18.315 -19.386 24.406  1.00 55.62  ? 369 TYR A CG    1 
ATOM   2833 C  CD1   . TYR A 1 369 ? 17.045 -19.630 24.915  1.00 59.87  ? 369 TYR A CD1   1 
ATOM   2834 C  CD2   . TYR A 1 369 ? 19.277 -18.869 25.264  1.00 56.24  ? 369 TYR A CD2   1 
ATOM   2835 C  CE1   . TYR A 1 369 ? 16.739 -19.364 26.235  1.00 59.63  ? 369 TYR A CE1   1 
ATOM   2836 C  CE2   . TYR A 1 369 ? 18.979 -18.602 26.589  1.00 61.03  ? 369 TYR A CE2   1 
ATOM   2837 C  CZ    . TYR A 1 369 ? 17.709 -18.851 27.067  1.00 61.28  ? 369 TYR A CZ    1 
ATOM   2838 O  OH    . TYR A 1 369 ? 17.402 -18.588 28.383  1.00 71.72  ? 369 TYR A OH    1 
ATOM   2839 N  N     . TRP A 1 370 ? 19.219 -16.505 22.536  1.00 50.37  ? 370 TRP A N     1 
ATOM   2840 C  CA    . TRP A 1 370 ? 20.234 -15.462 22.460  1.00 63.10  ? 370 TRP A CA    1 
ATOM   2841 C  C     . TRP A 1 370 ? 20.230 -14.685 23.767  1.00 61.44  ? 370 TRP A C     1 
ATOM   2842 O  O     . TRP A 1 370 ? 19.320 -14.816 24.590  1.00 56.76  ? 370 TRP A O     1 
ATOM   2843 C  CB    . TRP A 1 370 ? 20.005 -14.525 21.267  1.00 47.17  ? 370 TRP A CB    1 
ATOM   2844 C  CG    . TRP A 1 370 ? 18.609 -13.990 21.170  1.00 46.83  ? 370 TRP A CG    1 
ATOM   2845 C  CD1   . TRP A 1 370 ? 18.031 -13.053 21.976  1.00 50.09  ? 370 TRP A CD1   1 
ATOM   2846 C  CD2   . TRP A 1 370 ? 17.619 -14.348 20.197  1.00 46.68  ? 370 TRP A CD2   1 
ATOM   2847 N  NE1   . TRP A 1 370 ? 16.739 -12.813 21.572  1.00 46.91  ? 370 TRP A NE1   1 
ATOM   2848 C  CE2   . TRP A 1 370 ? 16.462 -13.597 20.483  1.00 47.75  ? 370 TRP A CE2   1 
ATOM   2849 C  CE3   . TRP A 1 370 ? 17.596 -15.236 19.117  1.00 45.37  ? 370 TRP A CE3   1 
ATOM   2850 C  CZ2   . TRP A 1 370 ? 15.297 -13.703 19.723  1.00 45.62  ? 370 TRP A CZ2   1 
ATOM   2851 C  CZ3   . TRP A 1 370 ? 16.439 -15.339 18.366  1.00 44.87  ? 370 TRP A CZ3   1 
ATOM   2852 C  CH2   . TRP A 1 370 ? 15.308 -14.577 18.671  1.00 45.01  ? 370 TRP A CH2   1 
ATOM   2853 N  N     . GLU A 1 371 ? 21.264 -13.866 23.944  1.00 59.58  ? 371 GLU A N     1 
ATOM   2854 C  CA    . GLU A 1 371 ? 21.377 -13.050 25.145  1.00 59.73  ? 371 GLU A CA    1 
ATOM   2855 C  C     . GLU A 1 371 ? 20.234 -12.045 25.203  1.00 55.11  ? 371 GLU A C     1 
ATOM   2856 O  O     . GLU A 1 371 ? 19.924 -11.383 24.208  1.00 50.45  ? 371 GLU A O     1 
ATOM   2857 C  CB    . GLU A 1 371 ? 22.726 -12.331 25.172  1.00 53.19  ? 371 GLU A CB    1 
ATOM   2858 C  CG    . GLU A 1 371 ? 23.894 -13.197 25.646  1.00 59.61  ? 371 GLU A CG    1 
ATOM   2859 C  CD    . GLU A 1 371 ? 24.217 -14.347 24.704  1.00 62.67  ? 371 GLU A CD    1 
ATOM   2860 O  OE1   . GLU A 1 371 ? 23.940 -14.236 23.489  1.00 53.96  ? 371 GLU A OE1   1 
ATOM   2861 O  OE2   . GLU A 1 371 ? 24.750 -15.368 25.186  1.00 66.49  ? 371 GLU A OE2   1 
ATOM   2862 N  N     . GLY A 1 372 ? 19.595 -11.946 26.366  1.00 54.93  ? 372 GLY A N     1 
ATOM   2863 C  CA    . GLY A 1 372 ? 18.501 -11.016 26.551  1.00 52.64  ? 372 GLY A CA    1 
ATOM   2864 C  C     . GLY A 1 372 ? 17.148 -11.508 26.091  1.00 54.95  ? 372 GLY A C     1 
ATOM   2865 O  O     . GLY A 1 372 ? 16.210 -10.707 26.012  1.00 61.06  ? 372 GLY A O     1 
ATOM   2866 N  N     . ILE A 1 373 ? 17.013 -12.800 25.780  1.00 54.58  ? 373 ILE A N     1 
ATOM   2867 C  CA    . ILE A 1 373 ? 15.725 -13.335 25.358  1.00 58.14  ? 373 ILE A CA    1 
ATOM   2868 C  C     . ILE A 1 373 ? 14.749 -13.422 26.526  1.00 61.11  ? 373 ILE A C     1 
ATOM   2869 O  O     . ILE A 1 373 ? 13.530 -13.459 26.312  1.00 59.94  ? 373 ILE A O     1 
ATOM   2870 C  CB    . ILE A 1 373 ? 15.922 -14.708 24.685  1.00 56.48  ? 373 ILE A CB    1 
ATOM   2871 C  CG1   . ILE A 1 373 ? 14.682 -15.096 23.877  1.00 53.35  ? 373 ILE A CG1   1 
ATOM   2872 C  CG2   . ILE A 1 373 ? 16.253 -15.776 25.723  1.00 58.69  ? 373 ILE A CG2   1 
ATOM   2873 C  CD1   . ILE A 1 373 ? 14.819 -16.409 23.151  1.00 63.04  ? 373 ILE A CD1   1 
ATOM   2874 N  N     . ASP A 1 374 ? 15.259 -13.460 27.759  1.00 60.35  ? 374 ASP A N     1 
ATOM   2875 C  CA    . ASP A 1 374 ? 14.440 -13.354 28.968  1.00 64.17  ? 374 ASP A CA    1 
ATOM   2876 C  C     . ASP A 1 374 ? 13.382 -14.455 29.039  1.00 68.65  ? 374 ASP A C     1 
ATOM   2877 O  O     . ASP A 1 374 ? 12.263 -14.238 29.506  1.00 73.91  ? 374 ASP A O     1 
ATOM   2878 C  CB    . ASP A 1 374 ? 13.793 -11.972 29.069  1.00 65.34  ? 374 ASP A CB    1 
ATOM   2879 C  CG    . ASP A 1 374 ? 13.415 -11.607 30.489  1.00 79.66  ? 374 ASP A CG    1 
ATOM   2880 O  OD1   . ASP A 1 374 ? 13.607 -12.447 31.395  1.00 80.70  ? 374 ASP A OD1   1 
ATOM   2881 O  OD2   . ASP A 1 374 ? 12.930 -10.476 30.702  1.00 89.85  ? 374 ASP A OD2   1 
ATOM   2882 N  N     . GLU A 1 375 ? 13.735 -15.650 28.575  1.00 61.34  ? 375 GLU A N     1 
ATOM   2883 C  CA    . GLU A 1 375 ? 12.833 -16.795 28.635  1.00 66.52  ? 375 GLU A CA    1 
ATOM   2884 C  C     . GLU A 1 375 ? 13.585 -17.961 29.261  1.00 72.61  ? 375 GLU A C     1 
ATOM   2885 O  O     . GLU A 1 375 ? 14.616 -18.398 28.708  1.00 70.21  ? 375 GLU A O     1 
ATOM   2886 C  CB    . GLU A 1 375 ? 12.300 -17.173 27.251  1.00 70.53  ? 375 GLU A CB    1 
ATOM   2887 C  CG    . GLU A 1 375 ? 11.324 -16.173 26.649  1.00 74.27  ? 375 GLU A CG    1 
ATOM   2888 C  CD    . GLU A 1 375 ? 10.498 -16.780 25.529  1.00 77.71  ? 375 GLU A CD    1 
ATOM   2889 O  OE1   . GLU A 1 375 ? 9.990  -17.905 25.713  1.00 81.77  ? 375 GLU A OE1   1 
ATOM   2890 O  OE2   . GLU A 1 375 ? 10.362 -16.142 24.464  1.00 75.17  ? 375 GLU A OE2   1 
ATOM   2891 N  N     . PRO A 1 376 ? 13.132 -18.486 30.396  1.00 71.69  ? 376 PRO A N     1 
ATOM   2892 C  CA    . PRO A 1 376 ? 13.766 -19.682 30.955  1.00 71.41  ? 376 PRO A CA    1 
ATOM   2893 C  C     . PRO A 1 376 ? 13.450 -20.910 30.120  1.00 69.50  ? 376 PRO A C     1 
ATOM   2894 O  O     . PRO A 1 376 ? 12.382 -21.022 29.513  1.00 70.08  ? 376 PRO A O     1 
ATOM   2895 C  CB    . PRO A 1 376 ? 13.153 -19.789 32.356  1.00 71.29  ? 376 PRO A CB    1 
ATOM   2896 C  CG    . PRO A 1 376 ? 11.830 -19.108 32.231  1.00 72.34  ? 376 PRO A CG    1 
ATOM   2897 C  CD    . PRO A 1 376 ? 12.041 -17.983 31.250  1.00 72.03  ? 376 PRO A CD    1 
ATOM   2898 N  N     . LEU A 1 377 ? 14.400 -21.838 30.094  1.00 70.89  ? 377 LEU A N     1 
ATOM   2899 C  CA    . LEU A 1 377 ? 14.256 -23.074 29.342  1.00 69.12  ? 377 LEU A CA    1 
ATOM   2900 C  C     . LEU A 1 377 ? 13.782 -24.200 30.252  1.00 77.06  ? 377 LEU A C     1 
ATOM   2901 O  O     . LEU A 1 377 ? 14.009 -24.185 31.465  1.00 73.46  ? 377 LEU A O     1 
ATOM   2902 C  CB    . LEU A 1 377 ? 15.576 -23.464 28.670  1.00 67.94  ? 377 LEU A CB    1 
ATOM   2903 C  CG    . LEU A 1 377 ? 16.016 -22.557 27.515  1.00 65.10  ? 377 LEU A CG    1 
ATOM   2904 C  CD1   . LEU A 1 377 ? 17.361 -22.988 26.955  1.00 62.99  ? 377 LEU A CD1   1 
ATOM   2905 C  CD2   . LEU A 1 377 ? 14.961 -22.538 26.419  1.00 62.69  ? 377 LEU A CD2   1 
ATOM   2906 N  N     . ALA A 1 378 ? 13.109 -25.176 29.650  1.00 80.58  ? 378 ALA A N     1 
ATOM   2907 C  CA    . ALA A 1 378 ? 12.622 -26.320 30.395  1.00 79.03  ? 378 ALA A CA    1 
ATOM   2908 C  C     . ALA A 1 378 ? 13.792 -27.190 30.848  1.00 78.22  ? 378 ALA A C     1 
ATOM   2909 O  O     . ALA A 1 378 ? 14.881 -27.130 30.270  1.00 75.73  ? 378 ALA A O     1 
ATOM   2910 C  CB    . ALA A 1 378 ? 11.656 -27.137 29.539  1.00 78.64  ? 378 ALA A CB    1 
ATOM   2911 N  N     . PRO A 1 379 ? 13.597 -27.989 31.899  1.00 87.59  ? 379 PRO A N     1 
ATOM   2912 C  CA    . PRO A 1 379 ? 14.634 -28.951 32.292  1.00 80.04  ? 379 PRO A CA    1 
ATOM   2913 C  C     . PRO A 1 379 ? 14.956 -29.908 31.155  1.00 78.74  ? 379 PRO A C     1 
ATOM   2914 O  O     . PRO A 1 379 ? 14.070 -30.364 30.429  1.00 78.23  ? 379 PRO A O     1 
ATOM   2915 C  CB    . PRO A 1 379 ? 14.006 -29.682 33.484  1.00 83.62  ? 379 PRO A CB    1 
ATOM   2916 C  CG    . PRO A 1 379 ? 13.031 -28.707 34.046  1.00 84.12  ? 379 PRO A CG    1 
ATOM   2917 C  CD    . PRO A 1 379 ? 12.489 -27.943 32.870  1.00 82.74  ? 379 PRO A CD    1 
ATOM   2918 N  N     . GLY A 1 380 ? 16.245 -30.204 31.001  1.00 78.31  ? 380 GLY A N     1 
ATOM   2919 C  CA    . GLY A 1 380 ? 16.717 -31.063 29.942  1.00 77.11  ? 380 GLY A CA    1 
ATOM   2920 C  C     . GLY A 1 380 ? 17.075 -30.355 28.650  1.00 73.76  ? 380 GLY A C     1 
ATOM   2921 O  O     . GLY A 1 380 ? 17.799 -30.929 27.828  1.00 72.73  ? 380 GLY A O     1 
ATOM   2922 N  N     . VAL A 1 381 ? 16.595 -29.131 28.447  1.00 72.15  ? 381 VAL A N     1 
ATOM   2923 C  CA    . VAL A 1 381 ? 16.862 -28.396 27.214  1.00 69.08  ? 381 VAL A CA    1 
ATOM   2924 C  C     . VAL A 1 381 ? 18.292 -27.874 27.248  1.00 68.20  ? 381 VAL A C     1 
ATOM   2925 O  O     . VAL A 1 381 ? 18.669 -27.124 28.154  1.00 68.92  ? 381 VAL A O     1 
ATOM   2926 C  CB    . VAL A 1 381 ? 15.858 -27.250 27.025  1.00 67.84  ? 381 VAL A CB    1 
ATOM   2927 C  CG1   . VAL A 1 381 ? 16.208 -26.439 25.787  1.00 69.66  ? 381 VAL A CG1   1 
ATOM   2928 C  CG2   . VAL A 1 381 ? 14.443 -27.799 26.928  1.00 68.81  ? 381 VAL A CG2   1 
ATOM   2929 N  N     . THR A 1 382 ? 19.092 -28.276 26.267  1.00 66.79  ? 382 THR A N     1 
ATOM   2930 C  CA    . THR A 1 382 ? 20.462 -27.809 26.126  1.00 66.96  ? 382 THR A CA    1 
ATOM   2931 C  C     . THR A 1 382 ? 20.565 -26.800 24.987  1.00 62.94  ? 382 THR A C     1 
ATOM   2932 O  O     . THR A 1 382 ? 19.663 -26.661 24.158  1.00 61.62  ? 382 THR A O     1 
ATOM   2933 C  CB    . THR A 1 382 ? 21.417 -28.982 25.885  1.00 66.60  ? 382 THR A CB    1 
ATOM   2934 O  OG1   . THR A 1 382 ? 20.962 -29.752 24.766  1.00 65.64  ? 382 THR A OG1   1 
ATOM   2935 C  CG2   . THR A 1 382 ? 21.492 -29.865 27.114  1.00 69.65  ? 382 THR A CG2   1 
ATOM   2936 N  N     . ILE A 1 383 ? 21.691 -26.094 24.951  1.00 63.65  ? 383 ILE A N     1 
ATOM   2937 C  CA    . ILE A 1 383 ? 21.917 -25.007 24.005  1.00 62.59  ? 383 ILE A CA    1 
ATOM   2938 C  C     . ILE A 1 383 ? 23.183 -25.297 23.212  1.00 63.51  ? 383 ILE A C     1 
ATOM   2939 O  O     . ILE A 1 383 ? 24.214 -25.665 23.788  1.00 71.78  ? 383 ILE A O     1 
ATOM   2940 C  CB    . ILE A 1 383 ? 22.029 -23.648 24.721  1.00 62.73  ? 383 ILE A CB    1 
ATOM   2941 C  CG1   . ILE A 1 383 ? 20.745 -23.330 25.482  1.00 61.70  ? 383 ILE A CG1   1 
ATOM   2942 C  CG2   . ILE A 1 383 ? 22.338 -22.540 23.723  1.00 62.36  ? 383 ILE A CG2   1 
ATOM   2943 C  CD1   . ILE A 1 383 ? 20.803 -22.024 26.242  1.00 63.10  ? 383 ILE A CD1   1 
ATOM   2944 N  N     . THR A 1 384 ? 23.103 -25.133 21.894  1.00 61.78  ? 384 THR A N     1 
ATOM   2945 C  CA    . THR A 1 384 ? 24.261 -25.180 21.010  1.00 65.63  ? 384 THR A CA    1 
ATOM   2946 C  C     . THR A 1 384 ? 24.510 -23.772 20.489  1.00 58.36  ? 384 THR A C     1 
ATOM   2947 O  O     . THR A 1 384 ? 23.629 -23.177 19.860  1.00 59.23  ? 384 THR A O     1 
ATOM   2948 C  CB    . THR A 1 384 ? 24.043 -26.156 19.853  1.00 61.95  ? 384 THR A CB    1 
ATOM   2949 O  OG1   . THR A 1 384 ? 23.925 -27.489 20.364  1.00 68.21  ? 384 THR A OG1   1 
ATOM   2950 C  CG2   . THR A 1 384 ? 25.210 -26.097 18.879  1.00 63.82  ? 384 THR A CG2   1 
ATOM   2951 N  N     . SER A 1 385 ? 25.702 -23.242 20.758  1.00 64.20  ? 385 SER A N     1 
ATOM   2952 C  CA    . SER A 1 385 ? 26.011 -21.856 20.439  1.00 66.35  ? 385 SER A CA    1 
ATOM   2953 C  C     . SER A 1 385 ? 26.129 -21.659 18.928  1.00 67.15  ? 385 SER A C     1 
ATOM   2954 O  O     . SER A 1 385 ? 26.074 -22.605 18.137  1.00 60.09  ? 385 SER A O     1 
ATOM   2955 C  CB    . SER A 1 385 ? 27.305 -21.424 21.126  1.00 66.52  ? 385 SER A CB    1 
ATOM   2956 O  OG    . SER A 1 385 ? 28.416 -22.144 20.619  1.00 69.98  ? 385 SER A OG    1 
ATOM   2957 N  N     . TRP A 1 386 ? 26.299 -20.394 18.531  1.00 60.21  ? 386 TRP A N     1 
ATOM   2958 C  CA    . TRP A 1 386 ? 26.448 -20.077 17.116  1.00 61.63  ? 386 TRP A CA    1 
ATOM   2959 C  C     . TRP A 1 386 ? 27.759 -20.602 16.547  1.00 62.21  ? 386 TRP A C     1 
ATOM   2960 O  O     . TRP A 1 386 ? 27.880 -20.733 15.324  1.00 66.01  ? 386 TRP A O     1 
ATOM   2961 C  CB    . TRP A 1 386 ? 26.347 -18.566 16.898  1.00 58.88  ? 386 TRP A CB    1 
ATOM   2962 C  CG    . TRP A 1 386 ? 27.556 -17.816 17.351  1.00 63.62  ? 386 TRP A CG    1 
ATOM   2963 C  CD1   . TRP A 1 386 ? 27.871 -17.462 18.630  1.00 61.48  ? 386 TRP A CD1   1 
ATOM   2964 C  CD2   . TRP A 1 386 ? 28.616 -17.325 16.525  1.00 61.62  ? 386 TRP A CD2   1 
ATOM   2965 N  NE1   . TRP A 1 386 ? 29.065 -16.783 18.652  1.00 60.47  ? 386 TRP A NE1   1 
ATOM   2966 C  CE2   . TRP A 1 386 ? 29.542 -16.686 17.371  1.00 63.99  ? 386 TRP A CE2   1 
ATOM   2967 C  CE3   . TRP A 1 386 ? 28.873 -17.364 15.151  1.00 61.32  ? 386 TRP A CE3   1 
ATOM   2968 C  CZ2   . TRP A 1 386 ? 30.703 -16.090 16.890  1.00 64.67  ? 386 TRP A CZ2   1 
ATOM   2969 C  CZ3   . TRP A 1 386 ? 30.027 -16.774 14.676  1.00 60.73  ? 386 TRP A CZ3   1 
ATOM   2970 C  CH2   . TRP A 1 386 ? 30.927 -16.144 15.542  1.00 64.17  ? 386 TRP A CH2   1 
ATOM   2971 N  N     . LYS A 1 387 ? 28.737 -20.904 17.399  1.00 64.47  ? 387 LYS A N     1 
ATOM   2972 C  CA    . LYS A 1 387 ? 29.966 -21.562 16.975  1.00 67.69  ? 387 LYS A CA    1 
ATOM   2973 C  C     . LYS A 1 387 ? 29.797 -23.068 16.810  1.00 75.41  ? 387 LYS A C     1 
ATOM   2974 O  O     . LYS A 1 387 ? 30.796 -23.766 16.603  1.00 80.34  ? 387 LYS A O     1 
ATOM   2975 C  CB    . LYS A 1 387 ? 31.093 -21.277 17.972  1.00 73.38  ? 387 LYS A CB    1 
ATOM   2976 C  CG    . LYS A 1 387 ? 31.562 -19.829 17.999  1.00 74.20  ? 387 LYS A CG    1 
ATOM   2977 C  CD    . LYS A 1 387 ? 32.800 -19.674 18.872  1.00 81.24  ? 387 LYS A CD    1 
ATOM   2978 C  CE    . LYS A 1 387 ? 33.379 -18.270 18.782  1.00 82.99  ? 387 LYS A CE    1 
ATOM   2979 N  NZ    . LYS A 1 387 ? 32.447 -17.241 19.318  1.00 85.85  ? 387 LYS A NZ    1 
ATOM   2980 N  N     . ASN A 1 388 ? 28.563 -23.571 16.904  1.00 74.72  ? 388 ASN A N     1 
ATOM   2981 C  CA    . ASN A 1 388 ? 28.262 -24.997 16.768  1.00 72.46  ? 388 ASN A CA    1 
ATOM   2982 C  C     . ASN A 1 388 ? 28.992 -25.813 17.835  1.00 80.85  ? 388 ASN A C     1 
ATOM   2983 O  O     . ASN A 1 388 ? 29.634 -26.826 17.551  1.00 77.86  ? 388 ASN A O     1 
ATOM   2984 C  CB    . ASN A 1 388 ? 28.595 -25.499 15.360  1.00 70.71  ? 388 ASN A CB    1 
ATOM   2985 C  CG    . ASN A 1 388 ? 27.891 -26.795 15.023  1.00 72.48  ? 388 ASN A CG    1 
ATOM   2986 O  OD1   . ASN A 1 388 ? 26.906 -27.164 15.663  1.00 73.54  ? 388 ASN A OD1   1 
ATOM   2987 N  ND2   . ASN A 1 388 ? 28.392 -27.495 14.013  1.00 79.54  ? 388 ASN A ND2   1 
ATOM   2988 N  N     . LYS A 1 389 ? 28.887 -25.354 19.081  1.00 83.94  ? 389 LYS A N     1 
ATOM   2989 C  CA    . LYS A 1 389 ? 29.530 -26.002 20.213  1.00 86.61  ? 389 LYS A CA    1 
ATOM   2990 C  C     . LYS A 1 389 ? 28.567 -26.032 21.390  1.00 88.34  ? 389 LYS A C     1 
ATOM   2991 O  O     . LYS A 1 389 ? 27.671 -25.189 21.499  1.00 83.44  ? 389 LYS A O     1 
ATOM   2992 C  CB    . LYS A 1 389 ? 30.823 -25.282 20.625  1.00 88.25  ? 389 LYS A CB    1 
ATOM   2993 C  CG    . LYS A 1 389 ? 31.897 -25.237 19.549  1.00 92.30  ? 389 LYS A CG    1 
ATOM   2994 C  CD    . LYS A 1 389 ? 33.080 -24.388 19.994  1.00 101.05 ? 389 LYS A CD    1 
ATOM   2995 C  CE    . LYS A 1 389 ? 34.122 -24.262 18.894  1.00 104.53 ? 389 LYS A CE    1 
ATOM   2996 N  NZ    . LYS A 1 389 ? 35.244 -23.364 19.287  1.00 103.63 ? 389 LYS A NZ    1 
ATOM   2997 N  N     . GLU A 1 390 ? 28.761 -27.015 22.268  1.00 98.82  ? 390 GLU A N     1 
ATOM   2998 C  CA    . GLU A 1 390 ? 27.982 -27.092 23.498  1.00 97.57  ? 390 GLU A CA    1 
ATOM   2999 C  C     . GLU A 1 390 ? 28.253 -25.869 24.364  1.00 97.74  ? 390 GLU A C     1 
ATOM   3000 O  O     . GLU A 1 390 ? 29.388 -25.641 24.793  1.00 100.86 ? 390 GLU A O     1 
ATOM   3001 C  CB    . GLU A 1 390 ? 28.326 -28.372 24.257  1.00 105.04 ? 390 GLU A CB    1 
ATOM   3002 C  CG    . GLU A 1 390 ? 27.710 -29.633 23.673  1.00 114.17 ? 390 GLU A CG    1 
ATOM   3003 C  CD    . GLU A 1 390 ? 26.241 -29.780 24.024  1.00 115.16 ? 390 GLU A CD    1 
ATOM   3004 O  OE1   . GLU A 1 390 ? 25.739 -28.980 24.842  1.00 111.89 ? 390 GLU A OE1   1 
ATOM   3005 O  OE2   . GLU A 1 390 ? 25.588 -30.699 23.484  1.00 115.45 ? 390 GLU A OE2   1 
ATOM   3006 N  N     . TRP A 1 391 ? 27.210 -25.084 24.620  1.00 86.63  ? 391 TRP A N     1 
ATOM   3007 C  CA    . TRP A 1 391 ? 27.327 -23.827 25.347  1.00 88.18  ? 391 TRP A CA    1 
ATOM   3008 C  C     . TRP A 1 391 ? 26.506 -23.890 26.627  1.00 86.07  ? 391 TRP A C     1 
ATOM   3009 O  O     . TRP A 1 391 ? 25.341 -24.299 26.602  1.00 79.40  ? 391 TRP A O     1 
ATOM   3010 C  CB    . TRP A 1 391 ? 26.863 -22.651 24.484  1.00 80.27  ? 391 TRP A CB    1 
ATOM   3011 C  CG    . TRP A 1 391 ? 26.932 -21.330 25.184  1.00 81.15  ? 391 TRP A CG    1 
ATOM   3012 C  CD1   . TRP A 1 391 ? 27.988 -20.468 25.203  1.00 84.30  ? 391 TRP A CD1   1 
ATOM   3013 C  CD2   . TRP A 1 391 ? 25.900 -20.718 25.969  1.00 81.97  ? 391 TRP A CD2   1 
ATOM   3014 N  NE1   . TRP A 1 391 ? 27.679 -19.357 25.949  1.00 87.95  ? 391 TRP A NE1   1 
ATOM   3015 C  CE2   . TRP A 1 391 ? 26.403 -19.486 26.431  1.00 85.95  ? 391 TRP A CE2   1 
ATOM   3016 C  CE3   . TRP A 1 391 ? 24.601 -21.093 26.326  1.00 79.49  ? 391 TRP A CE3   1 
ATOM   3017 C  CZ2   . TRP A 1 391 ? 25.653 -18.627 27.232  1.00 85.76  ? 391 TRP A CZ2   1 
ATOM   3018 C  CZ3   . TRP A 1 391 ? 23.858 -20.238 27.120  1.00 82.26  ? 391 TRP A CZ3   1 
ATOM   3019 C  CH2   . TRP A 1 391 ? 24.386 -19.020 27.564  1.00 82.87  ? 391 TRP A CH2   1 
ATOM   3020 N  N     . ARG A 1 392 ? 27.113 -23.471 27.736  1.00 88.98  ? 392 ARG A N     1 
ATOM   3021 C  CA    . ARG A 1 392 ? 26.461 -23.427 29.033  1.00 92.66  ? 392 ARG A CA    1 
ATOM   3022 C  C     . ARG A 1 392 ? 26.341 -21.986 29.514  1.00 99.19  ? 392 ARG A C     1 
ATOM   3023 O  O     . ARG A 1 392 ? 27.148 -21.132 29.134  1.00 99.69  ? 392 ARG A O     1 
ATOM   3024 C  CB    . ARG A 1 392 ? 27.235 -24.255 30.067  1.00 96.11  ? 392 ARG A CB    1 
ATOM   3025 C  CG    . ARG A 1 392 ? 27.299 -25.735 29.730  1.00 90.58  ? 392 ARG A CG    1 
ATOM   3026 C  CD    . ARG A 1 392 ? 28.045 -26.520 30.789  1.00 86.67  ? 392 ARG A CD    1 
ATOM   3027 N  NE    . ARG A 1 392 ? 28.073 -27.944 30.477  1.00 92.37  ? 392 ARG A NE    1 
ATOM   3028 C  CZ    . ARG A 1 392 ? 28.610 -28.871 31.257  1.00 93.84  ? 392 ARG A CZ    1 
ATOM   3029 N  NH1   . ARG A 1 392 ? 29.178 -28.558 32.411  1.00 95.75  ? 392 ARG A NH1   1 
ATOM   3030 N  NH2   . ARG A 1 392 ? 28.576 -30.144 30.871  1.00 90.50  ? 392 ARG A NH2   1 
ATOM   3031 N  N     . PRO A 1 393 ? 25.338 -21.682 30.345  1.00 102.87 ? 393 PRO A N     1 
ATOM   3032 C  CA    . PRO A 1 393 ? 25.142 -20.286 30.772  1.00 107.77 ? 393 PRO A CA    1 
ATOM   3033 C  C     . PRO A 1 393 ? 26.315 -19.702 31.540  1.00 117.55 ? 393 PRO A C     1 
ATOM   3034 O  O     . PRO A 1 393 ? 26.521 -18.482 31.500  1.00 118.96 ? 393 PRO A O     1 
ATOM   3035 C  CB    . PRO A 1 393 ? 23.881 -20.365 31.646  1.00 106.80 ? 393 PRO A CB    1 
ATOM   3036 C  CG    . PRO A 1 393 ? 23.167 -21.585 31.169  1.00 101.54 ? 393 PRO A CG    1 
ATOM   3037 C  CD    . PRO A 1 393 ? 24.247 -22.558 30.804  1.00 99.86  ? 393 PRO A CD    1 
ATOM   3038 N  N     . GLN A 1 394 ? 27.093 -20.529 32.238  1.00 130.70 ? 394 GLN A N     1 
ATOM   3039 C  CA    . GLN A 1 394 ? 28.212 -20.053 33.039  1.00 134.44 ? 394 GLN A CA    1 
ATOM   3040 C  C     . GLN A 1 394 ? 29.512 -19.959 32.245  1.00 132.37 ? 394 GLN A C     1 
ATOM   3041 O  O     . GLN A 1 394 ? 30.596 -20.003 32.840  1.00 134.75 ? 394 GLN A O     1 
ATOM   3042 C  CB    . GLN A 1 394 ? 28.402 -20.953 34.263  1.00 146.90 ? 394 GLN A CB    1 
ATOM   3043 C  CG    . GLN A 1 394 ? 27.230 -20.925 35.236  1.00 153.48 ? 394 GLN A CG    1 
ATOM   3044 C  CD    . GLN A 1 394 ? 27.460 -21.794 36.459  1.00 172.30 ? 394 GLN A CD    1 
ATOM   3045 O  OE1   . GLN A 1 394 ? 28.442 -22.533 36.535  1.00 175.95 ? 394 GLN A OE1   1 
ATOM   3046 N  NE2   . GLN A 1 394 ? 26.554 -21.706 37.426  1.00 176.30 ? 394 GLN A NE2   1 
ATOM   3047 N  N     . ASP A 1 395 ? 29.431 -19.829 30.926  1.00 127.87 ? 395 ASP A N     1 
ATOM   3048 C  CA    . ASP A 1 395 ? 30.603 -19.660 30.081  1.00 127.09 ? 395 ASP A CA    1 
ATOM   3049 C  C     . ASP A 1 395 ? 30.801 -18.186 29.740  1.00 127.37 ? 395 ASP A C     1 
ATOM   3050 O  O     . ASP A 1 395 ? 29.928 -17.343 29.963  1.00 123.17 ? 395 ASP A O     1 
ATOM   3051 C  CB    . ASP A 1 395 ? 30.472 -20.498 28.804  1.00 117.90 ? 395 ASP A CB    1 
ATOM   3052 C  CG    . ASP A 1 395 ? 30.355 -21.982 29.092  1.00 112.06 ? 395 ASP A CG    1 
ATOM   3053 O  OD1   . ASP A 1 395 ? 30.339 -22.354 30.284  1.00 112.73 ? 395 ASP A OD1   1 
ATOM   3054 O  OD2   . ASP A 1 395 ? 30.281 -22.777 28.130  1.00 104.68 ? 395 ASP A OD2   1 
ATOM   3055 N  N     . GLU A 1 396 ? 31.978 -17.880 29.192  1.00 138.73 ? 396 GLU A N     1 
ATOM   3056 C  CA    . GLU A 1 396 ? 32.296 -16.497 28.853  1.00 138.85 ? 396 GLU A CA    1 
ATOM   3057 C  C     . GLU A 1 396 ? 31.745 -16.112 27.485  1.00 135.93 ? 396 GLU A C     1 
ATOM   3058 O  O     . GLU A 1 396 ? 31.171 -15.029 27.328  1.00 135.39 ? 396 GLU A O     1 
ATOM   3059 C  CB    . GLU A 1 396 ? 33.809 -16.278 28.894  1.00 141.83 ? 396 GLU A CB    1 
ATOM   3060 C  CG    . GLU A 1 396 ? 34.230 -14.835 28.652  1.00 147.04 ? 396 GLU A CG    1 
ATOM   3061 C  CD    . GLU A 1 396 ? 35.729 -14.682 28.466  1.00 140.58 ? 396 GLU A CD    1 
ATOM   3062 O  OE1   . GLU A 1 396 ? 36.396 -15.691 28.154  1.00 139.21 ? 396 GLU A OE1   1 
ATOM   3063 O  OE2   . GLU A 1 396 ? 36.238 -13.551 28.631  1.00 139.01 ? 396 GLU A OE2   1 
ATOM   3064 N  N     . GLU A 1 397 ? 31.909 -16.980 26.491  1.00 123.37 ? 397 GLU A N     1 
ATOM   3065 C  CA    . GLU A 1 397 ? 31.450 -16.665 25.147  1.00 111.38 ? 397 GLU A CA    1 
ATOM   3066 C  C     . GLU A 1 397 ? 29.924 -16.634 25.101  1.00 101.59 ? 397 GLU A C     1 
ATOM   3067 O  O     . GLU A 1 397 ? 29.266 -17.503 25.682  1.00 103.51 ? 397 GLU A O     1 
ATOM   3068 C  CB    . GLU A 1 397 ? 31.978 -17.691 24.143  1.00 111.73 ? 397 GLU A CB    1 
ATOM   3069 C  CG    . GLU A 1 397 ? 33.493 -17.704 23.984  1.00 121.43 ? 397 GLU A CG    1 
ATOM   3070 C  CD    . GLU A 1 397 ? 34.017 -16.499 23.222  1.00 122.74 ? 397 GLU A CD    1 
ATOM   3071 O  OE1   . GLU A 1 397 ? 33.206 -15.789 22.589  1.00 119.39 ? 397 GLU A OE1   1 
ATOM   3072 O  OE2   . GLU A 1 397 ? 35.243 -16.262 23.256  1.00 128.32 ? 397 GLU A OE2   1 
ATOM   3073 N  N     . PRO A 1 398 ? 29.333 -15.652 24.426  1.00 90.07  ? 398 PRO A N     1 
ATOM   3074 C  CA    . PRO A 1 398 ? 27.875 -15.638 24.282  1.00 79.34  ? 398 PRO A CA    1 
ATOM   3075 C  C     . PRO A 1 398 ? 27.407 -16.723 23.325  1.00 78.73  ? 398 PRO A C     1 
ATOM   3076 O  O     . PRO A 1 398 ? 28.113 -17.111 22.391  1.00 74.30  ? 398 PRO A O     1 
ATOM   3077 C  CB    . PRO A 1 398 ? 27.587 -14.242 23.723  1.00 75.22  ? 398 PRO A CB    1 
ATOM   3078 C  CG    . PRO A 1 398 ? 28.833 -13.885 22.981  1.00 78.01  ? 398 PRO A CG    1 
ATOM   3079 C  CD    . PRO A 1 398 ? 29.966 -14.496 23.767  1.00 91.80  ? 398 PRO A CD    1 
ATOM   3080 N  N     . CYS A 1 399 ? 26.192 -17.216 23.572  1.00 74.38  ? 399 CYS A N     1 
ATOM   3081 C  CA    . CYS A 1 399 ? 25.646 -18.270 22.724  1.00 72.37  ? 399 CYS A CA    1 
ATOM   3082 C  C     . CYS A 1 399 ? 25.310 -17.751 21.332  1.00 62.14  ? 399 CYS A C     1 
ATOM   3083 O  O     . CYS A 1 399 ? 25.311 -18.524 20.368  1.00 63.72  ? 399 CYS A O     1 
ATOM   3084 C  CB    . CYS A 1 399 ? 24.410 -18.892 23.379  1.00 65.78  ? 399 CYS A CB    1 
ATOM   3085 S  SG    . CYS A 1 399 ? 22.970 -17.801 23.489  1.00 57.97  ? 399 CYS A SG    1 
ATOM   3086 N  N     . ALA A 1 400 ? 25.027 -16.458 21.204  1.00 61.40  ? 400 ALA A N     1 
ATOM   3087 C  CA    . ALA A 1 400 ? 24.729 -15.847 19.919  1.00 61.69  ? 400 ALA A CA    1 
ATOM   3088 C  C     . ALA A 1 400 ? 25.724 -14.733 19.634  1.00 58.26  ? 400 ALA A C     1 
ATOM   3089 O  O     . ALA A 1 400 ? 26.273 -14.115 20.552  1.00 61.07  ? 400 ALA A O     1 
ATOM   3090 C  CB    . ALA A 1 400 ? 23.301 -15.290 19.878  1.00 55.55  ? 400 ALA A CB    1 
ATOM   3091 N  N     . HIS A 1 401 ? 25.956 -14.484 18.352  1.00 59.01  ? 401 HIS A N     1 
ATOM   3092 C  CA    . HIS A 1 401 ? 26.838 -13.397 17.969  1.00 51.31  ? 401 HIS A CA    1 
ATOM   3093 C  C     . HIS A 1 401 ? 26.156 -12.059 18.249  1.00 53.19  ? 401 HIS A C     1 
ATOM   3094 O  O     . HIS A 1 401 ? 24.936 -11.942 18.095  1.00 51.32  ? 401 HIS A O     1 
ATOM   3095 C  CB    . HIS A 1 401 ? 27.210 -13.501 16.494  1.00 54.26  ? 401 HIS A CB    1 
ATOM   3096 C  CG    . HIS A 1 401 ? 28.343 -12.609 16.097  1.00 55.98  ? 401 HIS A CG    1 
ATOM   3097 N  ND1   . HIS A 1 401 ? 28.158 -11.303 15.699  1.00 51.15  ? 401 HIS A ND1   1 
ATOM   3098 C  CD2   . HIS A 1 401 ? 29.677 -12.831 16.052  1.00 52.82  ? 401 HIS A CD2   1 
ATOM   3099 C  CE1   . HIS A 1 401 ? 29.329 -10.762 15.416  1.00 54.33  ? 401 HIS A CE1   1 
ATOM   3100 N  NE2   . HIS A 1 401 ? 30.268 -11.668 15.623  1.00 50.44  ? 401 HIS A NE2   1 
ATOM   3101 N  N     . PRO A 1 402 ? 26.907 -11.043 18.684  1.00 52.18  ? 402 PRO A N     1 
ATOM   3102 C  CA    . PRO A 1 402 ? 26.281 -9.739  18.959  1.00 51.29  ? 402 PRO A CA    1 
ATOM   3103 C  C     . PRO A 1 402 ? 25.563 -9.136  17.763  1.00 51.86  ? 402 PRO A C     1 
ATOM   3104 O  O     . PRO A 1 402 ? 24.623 -8.354  17.950  1.00 52.23  ? 402 PRO A O     1 
ATOM   3105 C  CB    . PRO A 1 402 ? 27.467 -8.871  19.401  1.00 47.96  ? 402 PRO A CB    1 
ATOM   3106 C  CG    . PRO A 1 402 ? 28.450 -9.838  19.951  1.00 52.47  ? 402 PRO A CG    1 
ATOM   3107 C  CD    . PRO A 1 402 ? 28.313 -11.085 19.122  1.00 48.43  ? 402 PRO A CD    1 
ATOM   3108 N  N     . ASN A 1 403 ? 25.972 -9.469  16.538  1.00 49.13  ? 403 ASN A N     1 
ATOM   3109 C  CA    . ASN A 1 403 ? 25.315 -8.960  15.340  1.00 50.92  ? 403 ASN A CA    1 
ATOM   3110 C  C     . ASN A 1 403 ? 24.454 -10.022 14.661  1.00 52.65  ? 403 ASN A C     1 
ATOM   3111 O  O     . ASN A 1 403 ? 24.158 -9.906  13.467  1.00 47.84  ? 403 ASN A O     1 
ATOM   3112 C  CB    . ASN A 1 403 ? 26.348 -8.401  14.360  1.00 54.40  ? 403 ASN A CB    1 
ATOM   3113 C  CG    . ASN A 1 403 ? 25.733 -7.459  13.336  1.00 58.45  ? 403 ASN A CG    1 
ATOM   3114 O  OD1   . ASN A 1 403 ? 24.873 -6.641  13.663  1.00 55.94  ? 403 ASN A OD1   1 
ATOM   3115 N  ND2   . ASN A 1 403 ? 26.162 -7.584  12.085  1.00 59.37  ? 403 ASN A ND2   1 
ATOM   3116 N  N     . SER A 1 404 ? 24.051 -11.056 15.397  1.00 48.81  ? 404 SER A N     1 
ATOM   3117 C  CA    . SER A 1 404 ? 23.165 -12.066 14.835  1.00 46.08  ? 404 SER A CA    1 
ATOM   3118 C  C     . SER A 1 404 ? 21.825 -11.439 14.468  1.00 43.55  ? 404 SER A C     1 
ATOM   3119 O  O     . SER A 1 404 ? 21.351 -10.505 15.120  1.00 48.22  ? 404 SER A O     1 
ATOM   3120 C  CB    . SER A 1 404 ? 22.963 -13.217 15.825  1.00 49.89  ? 404 SER A CB    1 
ATOM   3121 O  OG    . SER A 1 404 ? 22.370 -12.766 17.030  1.00 48.82  ? 404 SER A OG    1 
ATOM   3122 N  N     . ARG A 1 405 ? 21.215 -11.956 13.405  1.00 43.23  ? 405 ARG A N     1 
ATOM   3123 C  CA    . ARG A 1 405 ? 20.044 -11.329 12.814  1.00 45.88  ? 405 ARG A CA    1 
ATOM   3124 C  C     . ARG A 1 405 ? 18.944 -12.355 12.587  1.00 43.54  ? 405 ARG A C     1 
ATOM   3125 O  O     . ARG A 1 405 ? 19.194 -13.556 12.462  1.00 44.33  ? 405 ARG A O     1 
ATOM   3126 C  CB    . ARG A 1 405 ? 20.389 -10.650 11.477  1.00 39.20  ? 405 ARG A CB    1 
ATOM   3127 C  CG    . ARG A 1 405 ? 21.433 -9.551  11.581  1.00 40.48  ? 405 ARG A CG    1 
ATOM   3128 C  CD    . ARG A 1 405 ? 20.792 -8.183  11.728  1.00 42.08  ? 405 ARG A CD    1 
ATOM   3129 N  NE    . ARG A 1 405 ? 21.786 -7.142  11.955  1.00 43.36  ? 405 ARG A NE    1 
ATOM   3130 C  CZ    . ARG A 1 405 ? 21.520 -5.845  11.976  1.00 41.05  ? 405 ARG A CZ    1 
ATOM   3131 N  NH1   . ARG A 1 405 ? 20.298 -5.386  11.761  1.00 39.81  ? 405 ARG A NH1   1 
ATOM   3132 N  NH2   . ARG A 1 405 ? 22.504 -4.985  12.218  1.00 43.73  ? 405 ARG A NH2   1 
ATOM   3133 N  N     . PHE A 1 406 ? 17.712 -11.860 12.540  1.00 40.78  ? 406 PHE A N     1 
ATOM   3134 C  CA    . PHE A 1 406 ? 16.591 -12.613 12.009  1.00 38.24  ? 406 PHE A CA    1 
ATOM   3135 C  C     . PHE A 1 406 ? 16.105 -11.941 10.733  1.00 40.62  ? 406 PHE A C     1 
ATOM   3136 O  O     . PHE A 1 406 ? 16.241 -10.728 10.554  1.00 42.09  ? 406 PHE A O     1 
ATOM   3137 C  CB    . PHE A 1 406 ? 15.444 -12.733 13.024  1.00 41.30  ? 406 PHE A CB    1 
ATOM   3138 C  CG    . PHE A 1 406 ? 15.025 -11.428 13.643  1.00 40.96  ? 406 PHE A CG    1 
ATOM   3139 C  CD1   . PHE A 1 406 ? 14.183 -10.558 12.966  1.00 38.69  ? 406 PHE A CD1   1 
ATOM   3140 C  CD2   . PHE A 1 406 ? 15.453 -11.082 14.916  1.00 39.45  ? 406 PHE A CD2   1 
ATOM   3141 C  CE1   . PHE A 1 406 ? 13.791 -9.365  13.535  1.00 37.45  ? 406 PHE A CE1   1 
ATOM   3142 C  CE2   . PHE A 1 406 ? 15.059 -9.889  15.494  1.00 43.62  ? 406 PHE A CE2   1 
ATOM   3143 C  CZ    . PHE A 1 406 ? 14.227 -9.029  14.803  1.00 43.12  ? 406 PHE A CZ    1 
ATOM   3144 N  N     . CYS A 1 407 ? 15.556 -12.743 9.837   1.00 38.07  ? 407 CYS A N     1 
ATOM   3145 C  CA    . CYS A 1 407 ? 15.087 -12.276 8.537   1.00 41.66  ? 407 CYS A CA    1 
ATOM   3146 C  C     . CYS A 1 407 ? 13.630 -12.709 8.420   1.00 38.71  ? 407 CYS A C     1 
ATOM   3147 O  O     . CYS A 1 407 ? 13.344 -13.881 8.157   1.00 41.53  ? 407 CYS A O     1 
ATOM   3148 C  CB    . CYS A 1 407 ? 15.949 -12.847 7.412   1.00 43.22  ? 407 CYS A CB    1 
ATOM   3149 S  SG    . CYS A 1 407 ? 15.719 -12.056 5.808   1.00 42.31  ? 407 CYS A SG    1 
ATOM   3150 N  N     . THR A 1 408 ? 12.712 -11.772 8.623   1.00 37.48  ? 408 THR A N     1 
ATOM   3151 C  CA    . THR A 1 408 ? 11.306 -12.118 8.728   1.00 38.78  ? 408 THR A CA    1 
ATOM   3152 C  C     . THR A 1 408 ? 10.476 -11.269 7.778   1.00 40.28  ? 408 THR A C     1 
ATOM   3153 O  O     . THR A 1 408 ? 10.831 -10.122 7.492   1.00 44.61  ? 408 THR A O     1 
ATOM   3154 C  CB    . THR A 1 408 ? 10.810 -11.933 10.171  1.00 44.39  ? 408 THR A CB    1 
ATOM   3155 O  OG1   . THR A 1 408 ? 9.462  -12.407 10.285  1.00 49.33  ? 408 THR A OG1   1 
ATOM   3156 C  CG2   . THR A 1 408 ? 10.879 -10.462 10.589  1.00 37.46  ? 408 THR A CG2   1 
ATOM   3157 N  N     . PRO A 1 409 ? 9.383  -11.818 7.248   1.00 42.56  ? 409 PRO A N     1 
ATOM   3158 C  CA    . PRO A 1 409 ? 8.525  -11.030 6.355   1.00 38.59  ? 409 PRO A CA    1 
ATOM   3159 C  C     . PRO A 1 409 ? 7.796  -9.929  7.111   1.00 46.53  ? 409 PRO A C     1 
ATOM   3160 O  O     . PRO A 1 409 ? 7.245  -10.149 8.193   1.00 42.65  ? 409 PRO A O     1 
ATOM   3161 C  CB    . PRO A 1 409 ? 7.544  -12.067 5.795   1.00 48.09  ? 409 PRO A CB    1 
ATOM   3162 C  CG    . PRO A 1 409 ? 8.223  -13.393 5.996   1.00 47.87  ? 409 PRO A CG    1 
ATOM   3163 C  CD    . PRO A 1 409 ? 8.999  -13.240 7.268   1.00 45.75  ? 409 PRO A CD    1 
ATOM   3164 N  N     . ALA A 1 410 ? 7.787  -8.733  6.515   1.00 41.81  ? 410 ALA A N     1 
ATOM   3165 C  CA    . ALA A 1 410 ? 7.139  -7.586  7.140   1.00 48.80  ? 410 ALA A CA    1 
ATOM   3166 C  C     . ALA A 1 410 ? 5.630  -7.757  7.240   1.00 54.68  ? 410 ALA A C     1 
ATOM   3167 O  O     . ALA A 1 410 ? 5.008  -7.165  8.131   1.00 48.41  ? 410 ALA A O     1 
ATOM   3168 C  CB    . ALA A 1 410 ? 7.468  -6.307  6.366   1.00 45.17  ? 410 ALA A CB    1 
ATOM   3169 N  N     . SER A 1 411 ? 5.028  -8.560  6.359   1.00 49.89  ? 411 SER A N     1 
ATOM   3170 C  CA    . SER A 1 411 ? 3.582  -8.751  6.400   1.00 53.59  ? 411 SER A CA    1 
ATOM   3171 C  C     . SER A 1 411 ? 3.128  -9.491  7.651   1.00 52.40  ? 411 SER A C     1 
ATOM   3172 O  O     . SER A 1 411 ? 1.974  -9.330  8.064   1.00 56.07  ? 411 SER A O     1 
ATOM   3173 C  CB    . SER A 1 411 ? 3.113  -9.506  5.157   1.00 49.69  ? 411 SER A CB    1 
ATOM   3174 O  OG    . SER A 1 411 ? 3.611  -10.832 5.157   1.00 53.49  ? 411 SER A OG    1 
ATOM   3175 N  N     . GLN A 1 412 ? 4.005  -10.288 8.266   1.00 51.67  ? 412 GLN A N     1 
ATOM   3176 C  CA    . GLN A 1 412 ? 3.641  -11.067 9.443   1.00 53.38  ? 412 GLN A CA    1 
ATOM   3177 C  C     . GLN A 1 412 ? 3.628  -10.249 10.727  1.00 59.00  ? 412 GLN A C     1 
ATOM   3178 O  O     . GLN A 1 412 ? 3.203  -10.770 11.764  1.00 61.34  ? 412 GLN A O     1 
ATOM   3179 C  CB    . GLN A 1 412 ? 4.598  -12.251 9.609   1.00 52.13  ? 412 GLN A CB    1 
ATOM   3180 C  CG    . GLN A 1 412 ? 4.604  -13.211 8.434   1.00 51.36  ? 412 GLN A CG    1 
ATOM   3181 C  CD    . GLN A 1 412 ? 5.500  -14.416 8.659   1.00 56.00  ? 412 GLN A CD    1 
ATOM   3182 O  OE1   . GLN A 1 412 ? 5.392  -15.421 7.954   1.00 53.20  ? 412 GLN A OE1   1 
ATOM   3183 N  NE2   . GLN A 1 412 ? 6.390  -14.323 9.644   1.00 50.70  ? 412 GLN A NE2   1 
ATOM   3184 N  N     . CYS A 1 413 ? 4.075  -9.000  10.688  1.00 59.99  ? 413 CYS A N     1 
ATOM   3185 C  CA    . CYS A 1 413 ? 4.116  -8.185  11.897  1.00 58.27  ? 413 CYS A CA    1 
ATOM   3186 C  C     . CYS A 1 413 ? 2.698  -7.853  12.346  1.00 60.91  ? 413 CYS A C     1 
ATOM   3187 O  O     . CYS A 1 413 ? 1.894  -7.373  11.538  1.00 62.01  ? 413 CYS A O     1 
ATOM   3188 C  CB    . CYS A 1 413 ? 4.907  -6.903  11.651  1.00 54.82  ? 413 CYS A CB    1 
ATOM   3189 S  SG    . CYS A 1 413 ? 5.196  -5.910  13.129  1.00 58.00  ? 413 CYS A SG    1 
ATOM   3190 N  N     . PRO A 1 414 ? 2.352  -8.087  13.616  1.00 61.09  ? 414 PRO A N     1 
ATOM   3191 C  CA    . PRO A 1 414 ? 0.966  -7.852  14.048  1.00 61.29  ? 414 PRO A CA    1 
ATOM   3192 C  C     . PRO A 1 414 ? 0.534  -6.398  13.955  1.00 57.50  ? 414 PRO A C     1 
ATOM   3193 O  O     . PRO A 1 414 ? -0.661 -6.131  13.772  1.00 58.29  ? 414 PRO A O     1 
ATOM   3194 C  CB    . PRO A 1 414 ? 0.964  -8.347  15.503  1.00 63.86  ? 414 PRO A CB    1 
ATOM   3195 C  CG    . PRO A 1 414 ? 2.169  -9.232  15.619  1.00 61.79  ? 414 PRO A CG    1 
ATOM   3196 C  CD    . PRO A 1 414 ? 3.184  -8.634  14.700  1.00 59.29  ? 414 PRO A CD    1 
ATOM   3197 N  N     . ILE A 1 415 ? 1.463  -5.450  14.070  1.00 54.30  ? 415 ILE A N     1 
ATOM   3198 C  CA    . ILE A 1 415 ? 1.116  -4.033  14.063  1.00 59.23  ? 415 ILE A CA    1 
ATOM   3199 C  C     . ILE A 1 415 ? 1.623  -3.362  12.791  1.00 55.81  ? 415 ILE A C     1 
ATOM   3200 O  O     . ILE A 1 415 ? 1.865  -2.151  12.775  1.00 50.93  ? 415 ILE A O     1 
ATOM   3201 C  CB    . ILE A 1 415 ? 1.671  -3.319  15.309  1.00 57.95  ? 415 ILE A CB    1 
ATOM   3202 C  CG1   . ILE A 1 415 ? 3.183  -3.536  15.414  1.00 58.95  ? 415 ILE A CG1   1 
ATOM   3203 C  CG2   . ILE A 1 415 ? 0.956  -3.801  16.570  1.00 51.82  ? 415 ILE A CG2   1 
ATOM   3204 C  CD1   . ILE A 1 415 ? 3.832  -2.765  16.541  1.00 62.13  ? 415 ILE A CD1   1 
ATOM   3205 N  N     . ILE A 1 416 ? 1.785  -4.142  11.718  1.00 58.68  ? 416 ILE A N     1 
ATOM   3206 C  CA    . ILE A 1 416 ? 2.205  -3.575  10.441  1.00 54.40  ? 416 ILE A CA    1 
ATOM   3207 C  C     . ILE A 1 416 ? 1.166  -2.559  9.987   1.00 53.93  ? 416 ILE A C     1 
ATOM   3208 O  O     . ILE A 1 416 ? -0.044 -2.808  10.050  1.00 58.84  ? 416 ILE A O     1 
ATOM   3209 C  CB    . ILE A 1 416 ? 2.422  -4.693  9.405   1.00 53.31  ? 416 ILE A CB    1 
ATOM   3210 C  CG1   . ILE A 1 416 ? 3.055  -4.144  8.126   1.00 52.40  ? 416 ILE A CG1   1 
ATOM   3211 C  CG2   . ILE A 1 416 ? 1.119  -5.411  9.077   1.00 56.46  ? 416 ILE A CG2   1 
ATOM   3212 C  CD1   . ILE A 1 416 ? 4.524  -3.790  8.266   1.00 50.08  ? 416 ILE A CD1   1 
ATOM   3213 N  N     . ASP A 1 417 ? 1.634  -1.392  9.556   1.00 57.00  ? 417 ASP A N     1 
ATOM   3214 C  CA    . ASP A 1 417 ? 0.717  -0.306  9.240   1.00 55.37  ? 417 ASP A CA    1 
ATOM   3215 C  C     . ASP A 1 417 ? -0.116 -0.659  8.010   1.00 54.35  ? 417 ASP A C     1 
ATOM   3216 O  O     . ASP A 1 417 ? 0.421  -1.172  7.024   1.00 55.66  ? 417 ASP A O     1 
ATOM   3217 C  CB    . ASP A 1 417 ? 1.486  0.991   8.991   1.00 55.51  ? 417 ASP A CB    1 
ATOM   3218 C  CG    . ASP A 1 417 ? 0.580  2.211   8.959   1.00 57.32  ? 417 ASP A CG    1 
ATOM   3219 O  OD1   . ASP A 1 417 ? 0.169  2.678   10.044  1.00 54.30  ? 417 ASP A OD1   1 
ATOM   3220 O  OD2   . ASP A 1 417 ? 0.273  2.696   7.848   1.00 56.48  ? 417 ASP A OD2   1 
ATOM   3221 N  N     . PRO A 1 418 ? -1.425 -0.388  8.030   1.00 57.82  ? 418 PRO A N     1 
ATOM   3222 C  CA    . PRO A 1 418 ? -2.266 -0.715  6.867   1.00 62.07  ? 418 PRO A CA    1 
ATOM   3223 C  C     . PRO A 1 418 ? -1.945 0.096   5.620   1.00 60.55  ? 418 PRO A C     1 
ATOM   3224 O  O     . PRO A 1 418 ? -2.633 -0.064  4.605   1.00 68.44  ? 418 PRO A O     1 
ATOM   3225 C  CB    . PRO A 1 418 ? -3.688 -0.419  7.371   1.00 56.21  ? 418 PRO A CB    1 
ATOM   3226 C  CG    . PRO A 1 418 ? -3.506 0.563   8.469   1.00 60.69  ? 418 PRO A CG    1 
ATOM   3227 C  CD    . PRO A 1 418 ? -2.206 0.204   9.130   1.00 62.52  ? 418 PRO A CD    1 
ATOM   3228 N  N     . ALA A 1 419 ? -0.930 0.961   5.660   1.00 62.80  ? 419 ALA A N     1 
ATOM   3229 C  CA    . ALA A 1 419 ? -0.500 1.723   4.495   1.00 64.27  ? 419 ALA A CA    1 
ATOM   3230 C  C     . ALA A 1 419 ? 0.984  1.525   4.213   1.00 62.82  ? 419 ALA A C     1 
ATOM   3231 O  O     . ALA A 1 419 ? 1.610  2.389   3.590   1.00 64.31  ? 419 ALA A O     1 
ATOM   3232 C  CB    . ALA A 1 419 ? -0.807 3.213   4.672   1.00 60.91  ? 419 ALA A CB    1 
ATOM   3233 N  N     . TRP A 1 420 ? 1.564  0.404   4.654   1.00 58.73  ? 420 TRP A N     1 
ATOM   3234 C  CA    . TRP A 1 420 ? 2.994  0.197   4.454   1.00 59.98  ? 420 TRP A CA    1 
ATOM   3235 C  C     . TRP A 1 420 ? 3.333  -0.149  3.011   1.00 57.48  ? 420 TRP A C     1 
ATOM   3236 O  O     . TRP A 1 420 ? 4.496  -0.020  2.617   1.00 54.66  ? 420 TRP A O     1 
ATOM   3237 C  CB    . TRP A 1 420 ? 3.518  -0.889  5.400   1.00 56.71  ? 420 TRP A CB    1 
ATOM   3238 C  CG    . TRP A 1 420 ? 3.202  -2.304  5.002   1.00 56.62  ? 420 TRP A CG    1 
ATOM   3239 C  CD1   . TRP A 1 420 ? 2.003  -2.941  5.120   1.00 55.15  ? 420 TRP A CD1   1 
ATOM   3240 C  CD2   . TRP A 1 420 ? 4.115  -3.265  4.451   1.00 55.51  ? 420 TRP A CD2   1 
ATOM   3241 N  NE1   . TRP A 1 420 ? 2.106  -4.234  4.664   1.00 57.97  ? 420 TRP A NE1   1 
ATOM   3242 C  CE2   . TRP A 1 420 ? 3.392  -4.459  4.251   1.00 56.22  ? 420 TRP A CE2   1 
ATOM   3243 C  CE3   . TRP A 1 420 ? 5.470  -3.229  4.102   1.00 53.49  ? 420 TRP A CE3   1 
ATOM   3244 C  CZ2   . TRP A 1 420 ? 3.977  -5.606  3.713   1.00 58.36  ? 420 TRP A CZ2   1 
ATOM   3245 C  CZ3   . TRP A 1 420 ? 6.050  -4.370  3.569   1.00 53.96  ? 420 TRP A CZ3   1 
ATOM   3246 C  CH2   . TRP A 1 420 ? 5.303  -5.542  3.382   1.00 57.18  ? 420 TRP A CH2   1 
ATOM   3247 N  N     . GLU A 1 421 ? 2.352  -0.573  2.215   1.00 60.39  ? 421 GLU A N     1 
ATOM   3248 C  CA    . GLU A 1 421 ? 2.557  -0.826  0.795   1.00 60.88  ? 421 GLU A CA    1 
ATOM   3249 C  C     . GLU A 1 421 ? 1.843  0.190   -0.086  1.00 63.65  ? 421 GLU A C     1 
ATOM   3250 O  O     . GLU A 1 421 ? 1.711  -0.034  -1.294  1.00 64.93  ? 421 GLU A O     1 
ATOM   3251 C  CB    . GLU A 1 421 ? 2.104  -2.241  0.435   1.00 59.67  ? 421 GLU A CB    1 
ATOM   3252 C  CG    . GLU A 1 421 ? 2.848  -3.327  1.179   1.00 62.53  ? 421 GLU A CG    1 
ATOM   3253 C  CD    . GLU A 1 421 ? 2.545  -4.715  0.647   1.00 62.62  ? 421 GLU A CD    1 
ATOM   3254 O  OE1   . GLU A 1 421 ? 2.948  -5.013  -0.497  1.00 64.51  ? 421 GLU A OE1   1 
ATOM   3255 O  OE2   . GLU A 1 421 ? 1.899  -5.501  1.369   1.00 63.87  ? 421 GLU A OE2   1 
ATOM   3256 N  N     . SER A 1 422 ? 1.380  1.292   0.486   1.00 65.42  ? 422 SER A N     1 
ATOM   3257 C  CA    . SER A 1 422 ? 0.715  2.330   -0.292  1.00 67.04  ? 422 SER A CA    1 
ATOM   3258 C  C     . SER A 1 422 ? 1.726  3.018   -1.197  1.00 65.71  ? 422 SER A C     1 
ATOM   3259 O  O     . SER A 1 422 ? 2.726  3.551   -0.698  1.00 64.41  ? 422 SER A O     1 
ATOM   3260 C  CB    . SER A 1 422 ? 0.053  3.347   0.633   1.00 69.59  ? 422 SER A CB    1 
ATOM   3261 O  OG    . SER A 1 422 ? -0.972 2.744   1.406   1.00 75.42  ? 422 SER A OG    1 
ATOM   3262 N  N     . PRO A 1 423 ? 1.517  3.036   -2.517  1.00 72.01  ? 423 PRO A N     1 
ATOM   3263 C  CA    . PRO A 1 423 ? 2.524  3.631   -3.409  1.00 70.15  ? 423 PRO A CA    1 
ATOM   3264 C  C     . PRO A 1 423 ? 2.665  5.136   -3.261  1.00 74.29  ? 423 PRO A C     1 
ATOM   3265 O  O     . PRO A 1 423 ? 3.723  5.674   -3.611  1.00 76.88  ? 423 PRO A O     1 
ATOM   3266 C  CB    . PRO A 1 423 ? 2.024  3.250   -4.809  1.00 68.52  ? 423 PRO A CB    1 
ATOM   3267 C  CG    . PRO A 1 423 ? 0.556  3.035   -4.640  1.00 70.18  ? 423 PRO A CG    1 
ATOM   3268 C  CD    . PRO A 1 423 ? 0.369  2.484   -3.256  1.00 70.74  ? 423 PRO A CD    1 
ATOM   3269 N  N     . GLU A 1 424 ? 1.649  5.834   -2.751  1.00 79.02  ? 424 GLU A N     1 
ATOM   3270 C  CA    . GLU A 1 424 ? 1.745  7.278   -2.582  1.00 77.27  ? 424 GLU A CA    1 
ATOM   3271 C  C     . GLU A 1 424 ? 2.483  7.677   -1.311  1.00 76.30  ? 424 GLU A C     1 
ATOM   3272 O  O     . GLU A 1 424 ? 2.807  8.857   -1.146  1.00 77.06  ? 424 GLU A O     1 
ATOM   3273 C  CB    . GLU A 1 424 ? 0.349  7.909   -2.588  1.00 79.73  ? 424 GLU A CB    1 
ATOM   3274 C  CG    . GLU A 1 424 ? -0.370 7.873   -1.247  1.00 82.15  ? 424 GLU A CG    1 
ATOM   3275 C  CD    . GLU A 1 424 ? -0.842 6.484   -0.858  1.00 85.02  ? 424 GLU A CD    1 
ATOM   3276 O  OE1   . GLU A 1 424 ? -0.867 5.587   -1.729  1.00 83.06  ? 424 GLU A OE1   1 
ATOM   3277 O  OE2   . GLU A 1 424 ? -1.192 6.293   0.326   1.00 87.71  ? 424 GLU A OE2   1 
ATOM   3278 N  N     . GLY A 1 425 ? 2.756  6.735   -0.416  1.00 67.53  ? 425 GLY A N     1 
ATOM   3279 C  CA    . GLY A 1 425 ? 3.508  7.018   0.785   1.00 60.67  ? 425 GLY A CA    1 
ATOM   3280 C  C     . GLY A 1 425 ? 2.650  7.571   1.907   1.00 58.71  ? 425 GLY A C     1 
ATOM   3281 O  O     . GLY A 1 425 ? 1.454  7.832   1.760   1.00 63.95  ? 425 GLY A O     1 
ATOM   3282 N  N     . VAL A 1 426 ? 3.290  7.746   3.059   1.00 52.33  ? 426 VAL A N     1 
ATOM   3283 C  CA    . VAL A 1 426 ? 2.633  8.290   4.244   1.00 52.16  ? 426 VAL A CA    1 
ATOM   3284 C  C     . VAL A 1 426 ? 3.214  9.668   4.544   1.00 52.25  ? 426 VAL A C     1 
ATOM   3285 O  O     . VAL A 1 426 ? 4.418  9.889   4.351   1.00 50.83  ? 426 VAL A O     1 
ATOM   3286 C  CB    . VAL A 1 426 ? 2.776  7.345   5.447   1.00 47.16  ? 426 VAL A CB    1 
ATOM   3287 C  CG1   . VAL A 1 426 ? 2.080  6.023   5.161   1.00 48.92  ? 426 VAL A CG1   1 
ATOM   3288 C  CG2   . VAL A 1 426 ? 4.244  7.116   5.781   1.00 46.28  ? 426 VAL A CG2   1 
ATOM   3289 N  N     . PRO A 1 427 ? 2.403  10.624  5.001   1.00 51.10  ? 427 PRO A N     1 
ATOM   3290 C  CA    . PRO A 1 427 ? 2.909  11.977  5.280   1.00 50.07  ? 427 PRO A CA    1 
ATOM   3291 C  C     . PRO A 1 427 ? 3.684  12.010  6.590   1.00 46.13  ? 427 PRO A C     1 
ATOM   3292 O  O     . PRO A 1 427 ? 3.160  11.640  7.643   1.00 47.73  ? 427 PRO A O     1 
ATOM   3293 C  CB    . PRO A 1 427 ? 1.631  12.819  5.362   1.00 53.94  ? 427 PRO A CB    1 
ATOM   3294 C  CG    . PRO A 1 427 ? 0.597  11.844  5.825   1.00 58.57  ? 427 PRO A CG    1 
ATOM   3295 C  CD    . PRO A 1 427 ? 0.946  10.525  5.199   1.00 52.89  ? 427 PRO A CD    1 
ATOM   3296 N  N     . ILE A 1 428 ? 4.933  12.463  6.523   1.00 45.74  ? 428 ILE A N     1 
ATOM   3297 C  CA    . ILE A 1 428 ? 5.796  12.556  7.694   1.00 41.78  ? 428 ILE A CA    1 
ATOM   3298 C  C     . ILE A 1 428 ? 5.605  13.921  8.340   1.00 46.94  ? 428 ILE A C     1 
ATOM   3299 O  O     . ILE A 1 428 ? 5.738  14.955  7.675   1.00 47.05  ? 428 ILE A O     1 
ATOM   3300 C  CB    . ILE A 1 428 ? 7.268  12.336  7.312   1.00 42.77  ? 428 ILE A CB    1 
ATOM   3301 C  CG1   . ILE A 1 428 ? 7.460  10.961  6.666   1.00 42.00  ? 428 ILE A CG1   1 
ATOM   3302 C  CG2   . ILE A 1 428 ? 8.166  12.503  8.530   1.00 39.23  ? 428 ILE A CG2   1 
ATOM   3303 C  CD1   . ILE A 1 428 ? 7.128  9.792   7.573   1.00 38.81  ? 428 ILE A CD1   1 
ATOM   3304 N  N     . GLU A 1 429 ? 5.299  13.931  9.638   1.00 41.23  ? 429 GLU A N     1 
ATOM   3305 C  CA    . GLU A 1 429 ? 5.124  15.174  10.375  1.00 40.24  ? 429 GLU A CA    1 
ATOM   3306 C  C     . GLU A 1 429 ? 6.236  15.437  11.378  1.00 40.17  ? 429 GLU A C     1 
ATOM   3307 O  O     . GLU A 1 429 ? 6.221  16.484  12.035  1.00 47.78  ? 429 GLU A O     1 
ATOM   3308 C  CB    . GLU A 1 429 ? 3.772  15.185  11.095  1.00 42.20  ? 429 GLU A CB    1 
ATOM   3309 C  CG    . GLU A 1 429 ? 2.585  15.063  10.165  1.00 47.68  ? 429 GLU A CG    1 
ATOM   3310 C  CD    . GLU A 1 429 ? 1.268  15.238  10.883  1.00 51.06  ? 429 GLU A CD    1 
ATOM   3311 O  OE1   . GLU A 1 429 ? 1.193  16.087  11.793  1.00 54.07  ? 429 GLU A OE1   1 
ATOM   3312 O  OE2   . GLU A 1 429 ? 0.305  14.524  10.539  1.00 58.03  ? 429 GLU A OE2   1 
ATOM   3313 N  N     . GLY A 1 430 ? 7.198  14.530  11.512  1.00 39.28  ? 430 GLY A N     1 
ATOM   3314 C  CA    . GLY A 1 430 ? 8.285  14.727  12.451  1.00 40.12  ? 430 GLY A CA    1 
ATOM   3315 C  C     . GLY A 1 430 ? 9.446  13.824  12.126  1.00 32.56  ? 430 GLY A C     1 
ATOM   3316 O  O     . GLY A 1 430 ? 9.270  12.731  11.580  1.00 39.10  ? 430 GLY A O     1 
ATOM   3317 N  N     . ILE A 1 431 ? 10.648 14.284  12.464  1.00 31.94  ? 431 ILE A N     1 
ATOM   3318 C  CA    . ILE A 1 431 ? 11.881 13.550  12.212  1.00 33.02  ? 431 ILE A CA    1 
ATOM   3319 C  C     . ILE A 1 431 ? 12.677 13.512  13.507  1.00 32.91  ? 431 ILE A C     1 
ATOM   3320 O  O     . ILE A 1 431 ? 12.841 14.543  14.166  1.00 34.76  ? 431 ILE A O     1 
ATOM   3321 C  CB    . ILE A 1 431 ? 12.713 14.188  11.083  1.00 35.83  ? 431 ILE A CB    1 
ATOM   3322 C  CG1   . ILE A 1 431 ? 11.931 14.188  9.770   1.00 37.35  ? 431 ILE A CG1   1 
ATOM   3323 C  CG2   . ILE A 1 431 ? 14.034 13.457  10.911  1.00 36.44  ? 431 ILE A CG2   1 
ATOM   3324 C  CD1   . ILE A 1 431 ? 12.677 14.842  8.622   1.00 33.68  ? 431 ILE A CD1   1 
ATOM   3325 N  N     . ILE A 1 432 ? 13.172 12.332  13.870  1.00 35.12  ? 432 ILE A N     1 
ATOM   3326 C  CA    . ILE A 1 432 ? 13.851 12.121  15.142  1.00 33.70  ? 432 ILE A CA    1 
ATOM   3327 C  C     . ILE A 1 432 ? 15.283 11.683  14.876  1.00 34.16  ? 432 ILE A C     1 
ATOM   3328 O  O     . ILE A 1 432 ? 15.521 10.753  14.098  1.00 34.69  ? 432 ILE A O     1 
ATOM   3329 C  CB    . ILE A 1 432 ? 13.123 11.076  16.006  1.00 33.29  ? 432 ILE A CB    1 
ATOM   3330 C  CG1   . ILE A 1 432 ? 11.631 11.406  16.102  1.00 32.55  ? 432 ILE A CG1   1 
ATOM   3331 C  CG2   . ILE A 1 432 ? 13.754 11.008  17.390  1.00 33.05  ? 432 ILE A CG2   1 
ATOM   3332 C  CD1   . ILE A 1 432 ? 10.813 10.321  16.774  1.00 34.80  ? 432 ILE A CD1   1 
ATOM   3333 N  N     . PHE A 1 433 ? 16.229 12.352  15.524  1.00 33.22  ? 433 PHE A N     1 
ATOM   3334 C  CA    . PHE A 1 433 ? 17.625 11.946  15.558  1.00 30.99  ? 433 PHE A CA    1 
ATOM   3335 C  C     . PHE A 1 433 ? 17.975 11.490  16.968  1.00 36.72  ? 433 PHE A C     1 
ATOM   3336 O  O     . PHE A 1 433 ? 17.225 11.714  17.923  1.00 36.25  ? 433 PHE A O     1 
ATOM   3337 C  CB    . PHE A 1 433 ? 18.543 13.095  15.123  1.00 32.40  ? 433 PHE A CB    1 
ATOM   3338 C  CG    . PHE A 1 433 ? 18.311 13.567  13.709  1.00 31.47  ? 433 PHE A CG    1 
ATOM   3339 C  CD1   . PHE A 1 433 ? 18.512 12.711  12.635  1.00 32.31  ? 433 PHE A CD1   1 
ATOM   3340 C  CD2   . PHE A 1 433 ? 17.917 14.872  13.455  1.00 32.30  ? 433 PHE A CD2   1 
ATOM   3341 C  CE1   . PHE A 1 433 ? 18.305 13.143  11.333  1.00 35.29  ? 433 PHE A CE1   1 
ATOM   3342 C  CE2   . PHE A 1 433 ? 17.712 15.311  12.157  1.00 39.71  ? 433 PHE A CE2   1 
ATOM   3343 C  CZ    . PHE A 1 433 ? 17.907 14.443  11.092  1.00 32.43  ? 433 PHE A CZ    1 
ATOM   3344 N  N     . GLY A 1 434 ? 19.121 10.851  17.099  1.00 35.45  ? 434 GLY A N     1 
ATOM   3345 C  CA    . GLY A 1 434 ? 19.594 10.437  18.405  1.00 35.90  ? 434 GLY A CA    1 
ATOM   3346 C  C     . GLY A 1 434 ? 20.501 9.230   18.316  1.00 36.35  ? 434 GLY A C     1 
ATOM   3347 O  O     . GLY A 1 434 ? 20.522 8.495   17.333  1.00 37.21  ? 434 GLY A O     1 
ATOM   3348 N  N     . GLY A 1 435 ? 21.273 9.029   19.373  1.00 40.69  ? 435 GLY A N     1 
ATOM   3349 C  CA    . GLY A 1 435 ? 22.159 7.894   19.457  1.00 37.63  ? 435 GLY A CA    1 
ATOM   3350 C  C     . GLY A 1 435 ? 22.460 7.533   20.893  1.00 39.22  ? 435 GLY A C     1 
ATOM   3351 O  O     . GLY A 1 435 ? 21.714 7.874   21.813  1.00 42.65  ? 435 GLY A O     1 
ATOM   3352 N  N     . ARG A 1 436 ? 23.572 6.830   21.078  1.00 40.04  ? 436 ARG A N     1 
ATOM   3353 C  CA    . ARG A 1 436 ? 23.997 6.385   22.404  1.00 44.60  ? 436 ARG A CA    1 
ATOM   3354 C  C     . ARG A 1 436 ? 24.959 7.419   22.977  1.00 45.32  ? 436 ARG A C     1 
ATOM   3355 O  O     . ARG A 1 436 ? 26.136 7.465   22.608  1.00 48.69  ? 436 ARG A O     1 
ATOM   3356 C  CB    . ARG A 1 436 ? 24.635 5.000   22.336  1.00 48.17  ? 436 ARG A CB    1 
ATOM   3357 C  CG    . ARG A 1 436 ? 23.652 3.873   22.031  1.00 47.94  ? 436 ARG A CG    1 
ATOM   3358 C  CD    . ARG A 1 436 ? 24.370 2.545   21.826  1.00 46.00  ? 436 ARG A CD    1 
ATOM   3359 N  NE    . ARG A 1 436 ? 23.445 1.496   21.414  1.00 51.74  ? 436 ARG A NE    1 
ATOM   3360 C  CZ    . ARG A 1 436 ? 22.892 0.617   22.240  1.00 50.53  ? 436 ARG A CZ    1 
ATOM   3361 N  NH1   . ARG A 1 436 ? 23.183 0.600   23.530  1.00 44.05  ? 436 ARG A NH1   1 
ATOM   3362 N  NH2   . ARG A 1 436 ? 22.022 -0.266  21.759  1.00 51.36  ? 436 ARG A NH2   1 
ATOM   3363 N  N     . ARG A 1 437 ? 24.455 8.254   23.877  1.00 42.88  ? 437 ARG A N     1 
ATOM   3364 C  CA    . ARG A 1 437 ? 25.280 9.215   24.608  1.00 49.02  ? 437 ARG A CA    1 
ATOM   3365 C  C     . ARG A 1 437 ? 25.153 8.924   26.093  1.00 51.53  ? 437 ARG A C     1 
ATOM   3366 O  O     . ARG A 1 437 ? 24.103 9.223   26.693  1.00 48.81  ? 437 ARG A O     1 
ATOM   3367 C  CB    . ARG A 1 437 ? 24.863 10.654  24.307  1.00 40.36  ? 437 ARG A CB    1 
ATOM   3368 C  CG    . ARG A 1 437 ? 25.107 11.085  22.877  1.00 43.00  ? 437 ARG A CG    1 
ATOM   3369 C  CD    . ARG A 1 437 ? 26.566 10.927  22.495  1.00 44.95  ? 437 ARG A CD    1 
ATOM   3370 N  NE    . ARG A 1 437 ? 27.462 11.777  23.271  1.00 41.67  ? 437 ARG A NE    1 
ATOM   3371 C  CZ    . ARG A 1 437 ? 27.811 13.010  22.926  1.00 43.36  ? 437 ARG A CZ    1 
ATOM   3372 N  NH1   . ARG A 1 437 ? 27.300 13.600  21.857  1.00 37.86  ? 437 ARG A NH1   1 
ATOM   3373 N  NH2   . ARG A 1 437 ? 28.697 13.667  23.671  1.00 39.74  ? 437 ARG A NH2   1 
ATOM   3374 N  N     . PRO A 1 438 ? 26.173 8.343   26.728  1.00 51.53  ? 438 PRO A N     1 
ATOM   3375 C  CA    . PRO A 1 438 ? 26.055 8.011   28.155  1.00 56.70  ? 438 PRO A CA    1 
ATOM   3376 C  C     . PRO A 1 438 ? 26.063 9.223   29.075  1.00 53.75  ? 438 PRO A C     1 
ATOM   3377 O  O     . PRO A 1 438 ? 25.788 9.061   30.271  1.00 56.58  ? 438 PRO A O     1 
ATOM   3378 C  CB    . PRO A 1 438 ? 27.275 7.115   28.407  1.00 55.93  ? 438 PRO A CB    1 
ATOM   3379 C  CG    . PRO A 1 438 ? 28.265 7.534   27.362  1.00 50.33  ? 438 PRO A CG    1 
ATOM   3380 C  CD    . PRO A 1 438 ? 27.454 7.897   26.151  1.00 47.06  ? 438 PRO A CD    1 
ATOM   3381 N  N     . ALA A 1 439 ? 26.355 10.420  28.572  1.00 49.32  ? 439 ALA A N     1 
ATOM   3382 C  CA    . ALA A 1 439 ? 26.448 11.588  29.436  1.00 52.32  ? 439 ALA A CA    1 
ATOM   3383 C  C     . ALA A 1 439 ? 26.146 12.853  28.647  1.00 49.13  ? 439 ALA A C     1 
ATOM   3384 O  O     . ALA A 1 439 ? 26.396 12.927  27.440  1.00 51.14  ? 439 ALA A O     1 
ATOM   3385 C  CB    . ALA A 1 439 ? 27.834 11.697  30.082  1.00 49.17  ? 439 ALA A CB    1 
ATOM   3386 N  N     . GLY A 1 440 ? 25.608 13.841  29.342  1.00 46.48  ? 440 GLY A N     1 
ATOM   3387 C  CA    . GLY A 1 440 ? 25.412 15.180  28.792  1.00 47.51  ? 440 GLY A CA    1 
ATOM   3388 C  C     . GLY A 1 440 ? 24.146 15.470  28.013  1.00 48.21  ? 440 GLY A C     1 
ATOM   3389 O  O     . GLY A 1 440 ? 23.487 16.480  28.255  1.00 49.37  ? 440 GLY A O     1 
ATOM   3390 N  N     . VAL A 1 441 ? 23.802 14.604  27.071  1.00 48.03  ? 441 VAL A N     1 
ATOM   3391 C  CA    . VAL A 1 441 ? 22.670 14.868  26.178  1.00 45.56  ? 441 VAL A CA    1 
ATOM   3392 C  C     . VAL A 1 441 ? 21.376 14.536  26.906  1.00 47.40  ? 441 VAL A C     1 
ATOM   3393 O  O     . VAL A 1 441 ? 21.228 13.410  27.411  1.00 47.19  ? 441 VAL A O     1 
ATOM   3394 C  CB    . VAL A 1 441 ? 22.802 14.060  24.892  1.00 39.44  ? 441 VAL A CB    1 
ATOM   3395 C  CG1   . VAL A 1 441 ? 21.632 14.353  23.960  1.00 39.01  ? 441 VAL A CG1   1 
ATOM   3396 C  CG2   . VAL A 1 441 ? 24.123 14.367  24.213  1.00 39.08  ? 441 VAL A CG2   1 
ATOM   3397 N  N     . PRO A 1 442 ? 20.417 15.465  26.979  1.00 48.91  ? 442 PRO A N     1 
ATOM   3398 C  CA    . PRO A 1 442 ? 19.166 15.187  27.697  1.00 46.72  ? 442 PRO A CA    1 
ATOM   3399 C  C     . PRO A 1 442 ? 18.266 14.209  26.962  1.00 40.81  ? 442 PRO A C     1 
ATOM   3400 O  O     . PRO A 1 442 ? 18.560 13.805  25.833  1.00 40.29  ? 442 PRO A O     1 
ATOM   3401 C  CB    . PRO A 1 442 ? 18.517 16.571  27.813  1.00 50.45  ? 442 PRO A CB    1 
ATOM   3402 C  CG    . PRO A 1 442 ? 19.045 17.323  26.643  1.00 43.21  ? 442 PRO A CG    1 
ATOM   3403 C  CD    . PRO A 1 442 ? 20.456 16.835  26.440  1.00 42.36  ? 442 PRO A CD    1 
ATOM   3404 N  N     . LEU A 1 443 ? 17.156 13.835  27.607  1.00 47.17  ? 443 LEU A N     1 
ATOM   3405 C  CA    . LEU A 1 443 ? 16.282 12.794  27.074  1.00 39.64  ? 443 LEU A CA    1 
ATOM   3406 C  C     . LEU A 1 443 ? 15.709 13.178  25.717  1.00 39.53  ? 443 LEU A C     1 
ATOM   3407 O  O     . LEU A 1 443 ? 15.673 12.355  24.795  1.00 42.89  ? 443 LEU A O     1 
ATOM   3408 C  CB    . LEU A 1 443 ? 15.151 12.508  28.060  1.00 40.41  ? 443 LEU A CB    1 
ATOM   3409 C  CG    . LEU A 1 443 ? 14.012 11.624  27.547  1.00 43.81  ? 443 LEU A CG    1 
ATOM   3410 C  CD1   . LEU A 1 443 ? 14.519 10.229  27.218  1.00 43.34  ? 443 LEU A CD1   1 
ATOM   3411 C  CD2   . LEU A 1 443 ? 12.888 11.561  28.571  1.00 51.90  ? 443 LEU A CD2   1 
ATOM   3412 N  N     . VAL A 1 444 ? 15.249 14.415  25.574  1.00 35.74  ? 444 VAL A N     1 
ATOM   3413 C  CA    . VAL A 1 444 ? 14.609 14.848  24.337  1.00 38.17  ? 444 VAL A CA    1 
ATOM   3414 C  C     . VAL A 1 444 ? 14.688 16.366  24.268  1.00 39.63  ? 444 VAL A C     1 
ATOM   3415 O  O     . VAL A 1 444 ? 14.600 17.054  25.289  1.00 38.30  ? 444 VAL A O     1 
ATOM   3416 C  CB    . VAL A 1 444 ? 13.148 14.339  24.255  1.00 37.13  ? 444 VAL A CB    1 
ATOM   3417 C  CG1   . VAL A 1 444 ? 12.301 14.940  25.377  1.00 41.26  ? 444 VAL A CG1   1 
ATOM   3418 C  CG2   . VAL A 1 444 ? 12.537 14.638  22.894  1.00 30.75  ? 444 VAL A CG2   1 
ATOM   3419 N  N     . TYR A 1 445 ? 14.876 16.883  23.057  1.00 35.58  ? 445 TYR A N     1 
ATOM   3420 C  CA    . TYR A 1 445 ? 14.737 18.310  22.821  1.00 36.02  ? 445 TYR A CA    1 
ATOM   3421 C  C     . TYR A 1 445 ? 14.320 18.527  21.376  1.00 35.33  ? 445 TYR A C     1 
ATOM   3422 O  O     . TYR A 1 445 ? 14.419 17.627  20.538  1.00 34.04  ? 445 TYR A O     1 
ATOM   3423 C  CB    . TYR A 1 445 ? 16.019 19.088  23.165  1.00 38.56  ? 445 TYR A CB    1 
ATOM   3424 C  CG    . TYR A 1 445 ? 17.247 18.756  22.348  1.00 36.08  ? 445 TYR A CG    1 
ATOM   3425 C  CD1   . TYR A 1 445 ? 17.546 19.465  21.191  1.00 43.38  ? 445 TYR A CD1   1 
ATOM   3426 C  CD2   . TYR A 1 445 ? 18.131 17.766  22.755  1.00 36.01  ? 445 TYR A CD2   1 
ATOM   3427 C  CE1   . TYR A 1 445 ? 18.679 19.179  20.445  1.00 40.90  ? 445 TYR A CE1   1 
ATOM   3428 C  CE2   . TYR A 1 445 ? 19.265 17.468  22.015  1.00 32.27  ? 445 TYR A CE2   1 
ATOM   3429 C  CZ    . TYR A 1 445 ? 19.536 18.179  20.865  1.00 40.70  ? 445 TYR A CZ    1 
ATOM   3430 O  OH    . TYR A 1 445 ? 20.661 17.894  20.127  1.00 38.39  ? 445 TYR A OH    1 
ATOM   3431 N  N     . GLU A 1 446 ? 13.823 19.730  21.100  1.00 38.89  ? 446 GLU A N     1 
ATOM   3432 C  CA    . GLU A 1 446 ? 13.270 20.079  19.799  1.00 38.63  ? 446 GLU A CA    1 
ATOM   3433 C  C     . GLU A 1 446 ? 14.095 21.188  19.158  1.00 37.27  ? 446 GLU A C     1 
ATOM   3434 O  O     . GLU A 1 446 ? 14.494 22.146  19.828  1.00 36.96  ? 446 GLU A O     1 
ATOM   3435 C  CB    . GLU A 1 446 ? 11.804 20.518  19.932  1.00 36.44  ? 446 GLU A CB    1 
ATOM   3436 C  CG    . GLU A 1 446 ? 11.194 21.084  18.660  1.00 40.87  ? 446 GLU A CG    1 
ATOM   3437 C  CD    . GLU A 1 446 ? 9.769  21.553  18.862  1.00 40.63  ? 446 GLU A CD    1 
ATOM   3438 O  OE1   . GLU A 1 446 ? 9.059  20.947  19.688  1.00 41.81  ? 446 GLU A OE1   1 
ATOM   3439 O  OE2   . GLU A 1 446 ? 9.356  22.524  18.197  1.00 39.74  ? 446 GLU A OE2   1 
ATOM   3440 N  N     . ALA A 1 447 ? 14.338 21.050  17.855  1.00 38.15  ? 447 ALA A N     1 
ATOM   3441 C  CA    . ALA A 1 447 ? 15.130 22.019  17.110  1.00 36.78  ? 447 ALA A CA    1 
ATOM   3442 C  C     . ALA A 1 447 ? 14.390 23.345  16.972  1.00 38.51  ? 447 ALA A C     1 
ATOM   3443 O  O     . ALA A 1 447 ? 13.157 23.396  16.928  1.00 41.68  ? 447 ALA A O     1 
ATOM   3444 C  CB    . ALA A 1 447 ? 15.472 21.471  15.725  1.00 33.26  ? 447 ALA A CB    1 
ATOM   3445 N  N     . LEU A 1 448 ? 15.167 24.429  16.889  1.00 38.80  ? 448 LEU A N     1 
ATOM   3446 C  CA    . LEU A 1 448 ? 14.600 25.774  16.828  1.00 39.38  ? 448 LEU A CA    1 
ATOM   3447 C  C     . LEU A 1 448 ? 14.072 26.122  15.445  1.00 40.56  ? 448 LEU A C     1 
ATOM   3448 O  O     . LEU A 1 448 ? 13.184 26.974  15.324  1.00 38.17  ? 448 LEU A O     1 
ATOM   3449 C  CB    . LEU A 1 448 ? 15.647 26.807  17.242  1.00 33.52  ? 448 LEU A CB    1 
ATOM   3450 C  CG    . LEU A 1 448 ? 16.306 26.576  18.602  1.00 42.85  ? 448 LEU A CG    1 
ATOM   3451 C  CD1   . LEU A 1 448 ? 17.282 27.701  18.926  1.00 47.23  ? 448 LEU A CD1   1 
ATOM   3452 C  CD2   . LEU A 1 448 ? 15.245 26.452  19.678  1.00 43.85  ? 448 LEU A CD2   1 
ATOM   3453 N  N     . SER A 1 449 ? 14.602 25.488  14.403  1.00 39.69  ? 449 SER A N     1 
ATOM   3454 C  CA    . SER A 1 449 ? 14.213 25.781  13.031  1.00 38.22  ? 449 SER A CA    1 
ATOM   3455 C  C     . SER A 1 449 ? 14.642 24.609  12.163  1.00 37.98  ? 449 SER A C     1 
ATOM   3456 O  O     . SER A 1 449 ? 15.218 23.631  12.647  1.00 33.36  ? 449 SER A O     1 
ATOM   3457 C  CB    . SER A 1 449 ? 14.841 27.088  12.544  1.00 42.32  ? 449 SER A CB    1 
ATOM   3458 O  OG    . SER A 1 449 ? 16.252 26.965  12.487  1.00 41.04  ? 449 SER A OG    1 
ATOM   3459 N  N     . TRP A 1 450 ? 14.367 24.718  10.862  1.00 41.26  ? 450 TRP A N     1 
ATOM   3460 C  CA    . TRP A 1 450 ? 14.806 23.679  9.938   1.00 41.66  ? 450 TRP A CA    1 
ATOM   3461 C  C     . TRP A 1 450 ? 16.324 23.665  9.812   1.00 40.39  ? 450 TRP A C     1 
ATOM   3462 O  O     . TRP A 1 450 ? 16.942 22.594  9.800   1.00 38.27  ? 450 TRP A O     1 
ATOM   3463 C  CB    . TRP A 1 450 ? 14.152 23.876  8.572   1.00 38.98  ? 450 TRP A CB    1 
ATOM   3464 C  CG    . TRP A 1 450 ? 14.542 22.837  7.568   1.00 43.02  ? 450 TRP A CG    1 
ATOM   3465 C  CD1   . TRP A 1 450 ? 15.390 22.996  6.509   1.00 43.31  ? 450 TRP A CD1   1 
ATOM   3466 C  CD2   . TRP A 1 450 ? 14.110 21.471  7.533   1.00 45.73  ? 450 TRP A CD2   1 
ATOM   3467 N  NE1   . TRP A 1 450 ? 15.507 21.816  5.814   1.00 44.32  ? 450 TRP A NE1   1 
ATOM   3468 C  CE2   . TRP A 1 450 ? 14.731 20.865  6.423   1.00 42.42  ? 450 TRP A CE2   1 
ATOM   3469 C  CE3   . TRP A 1 450 ? 13.257 20.702  8.333   1.00 39.25  ? 450 TRP A CE3   1 
ATOM   3470 C  CZ2   . TRP A 1 450 ? 14.523 19.530  6.090   1.00 41.15  ? 450 TRP A CZ2   1 
ATOM   3471 C  CZ3   . TRP A 1 450 ? 13.051 19.379  8.000   1.00 38.06  ? 450 TRP A CZ3   1 
ATOM   3472 C  CH2   . TRP A 1 450 ? 13.682 18.805  6.890   1.00 42.61  ? 450 TRP A CH2   1 
ATOM   3473 N  N     . GLN A 1 451 ? 16.942 24.846  9.736   1.00 39.96  ? 451 GLN A N     1 
ATOM   3474 C  CA    . GLN A 1 451 ? 18.396 24.915  9.631   1.00 38.91  ? 451 GLN A CA    1 
ATOM   3475 C  C     . GLN A 1 451 ? 19.067 24.358  10.879  1.00 34.98  ? 451 GLN A C     1 
ATOM   3476 O  O     . GLN A 1 451 ? 20.044 23.606  10.781  1.00 39.58  ? 451 GLN A O     1 
ATOM   3477 C  CB    . GLN A 1 451 ? 18.841 26.356  9.372   1.00 40.44  ? 451 GLN A CB    1 
ATOM   3478 C  CG    . GLN A 1 451 ? 18.401 26.922  8.027   1.00 47.50  ? 451 GLN A CG    1 
ATOM   3479 C  CD    . GLN A 1 451 ? 16.924 27.279  7.987   1.00 52.88  ? 451 GLN A CD    1 
ATOM   3480 O  OE1   . GLN A 1 451 ? 16.311 27.555  9.021   1.00 48.74  ? 451 GLN A OE1   1 
ATOM   3481 N  NE2   . GLN A 1 451 ? 16.343 27.268  6.791   1.00 53.87  ? 451 GLN A NE2   1 
ATOM   3482 N  N     . HIS A 1 452 ? 18.553 24.703  12.062  1.00 36.67  ? 452 HIS A N     1 
ATOM   3483 C  CA    . HIS A 1 452 ? 19.093 24.130  13.292  1.00 36.07  ? 452 HIS A CA    1 
ATOM   3484 C  C     . HIS A 1 452 ? 18.859 22.625  13.348  1.00 35.79  ? 452 HIS A C     1 
ATOM   3485 O  O     . HIS A 1 452 ? 19.714 21.875  13.831  1.00 31.96  ? 452 HIS A O     1 
ATOM   3486 C  CB    . HIS A 1 452 ? 18.475 24.821  14.507  1.00 39.57  ? 452 HIS A CB    1 
ATOM   3487 C  CG    . HIS A 1 452 ? 18.989 24.314  15.818  1.00 36.54  ? 452 HIS A CG    1 
ATOM   3488 N  ND1   . HIS A 1 452 ? 18.156 23.908  16.837  1.00 33.91  ? 452 HIS A ND1   1 
ATOM   3489 C  CD2   . HIS A 1 452 ? 20.252 24.149  16.277  1.00 33.36  ? 452 HIS A CD2   1 
ATOM   3490 C  CE1   . HIS A 1 452 ? 18.882 23.512  17.867  1.00 38.46  ? 452 HIS A CE1   1 
ATOM   3491 N  NE2   . HIS A 1 452 ? 20.158 23.649  17.553  1.00 35.65  ? 452 HIS A NE2   1 
ATOM   3492 N  N     . GLY A 1 453 ? 17.712 22.164  12.849  1.00 35.30  ? 453 GLY A N     1 
ATOM   3493 C  CA    . GLY A 1 453 ? 17.449 20.736  12.828  1.00 32.43  ? 453 GLY A CA    1 
ATOM   3494 C  C     . GLY A 1 453 ? 18.427 19.973  11.957  1.00 35.52  ? 453 GLY A C     1 
ATOM   3495 O  O     . GLY A 1 453 ? 18.941 18.928  12.361  1.00 32.95  ? 453 GLY A O     1 
ATOM   3496 N  N     . VAL A 1 454 ? 18.693 20.483  10.750  1.00 35.34  ? 454 VAL A N     1 
ATOM   3497 C  CA    . VAL A 1 454 ? 19.709 19.881  9.890   1.00 34.49  ? 454 VAL A CA    1 
ATOM   3498 C  C     . VAL A 1 454 ? 21.058 19.867  10.598  1.00 35.00  ? 454 VAL A C     1 
ATOM   3499 O  O     . VAL A 1 454 ? 21.828 18.906  10.481  1.00 35.30  ? 454 VAL A O     1 
ATOM   3500 C  CB    . VAL A 1 454 ? 19.781 20.625  8.541   1.00 38.51  ? 454 VAL A CB    1 
ATOM   3501 C  CG1   . VAL A 1 454 ? 20.905 20.064  7.677   1.00 34.01  ? 454 VAL A CG1   1 
ATOM   3502 C  CG2   . VAL A 1 454 ? 18.454 20.536  7.805   1.00 36.97  ? 454 VAL A CG2   1 
ATOM   3503 N  N     . PHE A 1 455 ? 21.363 20.928  11.350  1.00 34.41  ? 455 PHE A N     1 
ATOM   3504 C  CA    . PHE A 1 455 ? 22.608 20.951  12.109  1.00 34.80  ? 455 PHE A CA    1 
ATOM   3505 C  C     . PHE A 1 455 ? 22.608 19.886  13.199  1.00 33.45  ? 455 PHE A C     1 
ATOM   3506 O  O     . PHE A 1 455 ? 23.657 19.316  13.522  1.00 38.77  ? 455 PHE A O     1 
ATOM   3507 C  CB    . PHE A 1 455 ? 22.837 22.336  12.718  1.00 33.35  ? 455 PHE A CB    1 
ATOM   3508 C  CG    . PHE A 1 455 ? 23.875 22.346  13.808  1.00 36.59  ? 455 PHE A CG    1 
ATOM   3509 C  CD1   . PHE A 1 455 ? 25.220 22.476  13.501  1.00 37.14  ? 455 PHE A CD1   1 
ATOM   3510 C  CD2   . PHE A 1 455 ? 23.507 22.203  15.141  1.00 38.14  ? 455 PHE A CD2   1 
ATOM   3511 C  CE1   . PHE A 1 455 ? 26.177 22.469  14.497  1.00 37.75  ? 455 PHE A CE1   1 
ATOM   3512 C  CE2   . PHE A 1 455 ? 24.460 22.192  16.142  1.00 37.54  ? 455 PHE A CE2   1 
ATOM   3513 C  CZ    . PHE A 1 455 ? 25.797 22.328  15.819  1.00 39.83  ? 455 PHE A CZ    1 
ATOM   3514 N  N     . VAL A 1 456 ? 21.444 19.625  13.800  1.00 33.91  ? 456 VAL A N     1 
ATOM   3515 C  CA    . VAL A 1 456 ? 21.361 18.618  14.856  1.00 33.44  ? 456 VAL A CA    1 
ATOM   3516 C  C     . VAL A 1 456 ? 21.682 17.238  14.297  1.00 36.03  ? 456 VAL A C     1 
ATOM   3517 O  O     . VAL A 1 456 ? 22.396 16.446  14.925  1.00 36.80  ? 456 VAL A O     1 
ATOM   3518 C  CB    . VAL A 1 456 ? 19.973 18.653  15.525  1.00 36.23  ? 456 VAL A CB    1 
ATOM   3519 C  CG1   . VAL A 1 456 ? 19.760 17.421  16.401  1.00 35.45  ? 456 VAL A CG1   1 
ATOM   3520 C  CG2   . VAL A 1 456 ? 19.808 19.927  16.347  1.00 31.21  ? 456 VAL A CG2   1 
ATOM   3521 N  N     . GLY A 1 457 ? 21.171 16.933  13.103  1.00 34.25  ? 457 GLY A N     1 
ATOM   3522 C  CA    . GLY A 1 457 ? 21.511 15.668  12.470  1.00 34.73  ? 457 GLY A CA    1 
ATOM   3523 C  C     . GLY A 1 457 ? 22.988 15.566  12.143  1.00 36.11  ? 457 GLY A C     1 
ATOM   3524 O  O     . GLY A 1 457 ? 23.603 14.509  12.323  1.00 33.12  ? 457 GLY A O     1 
ATOM   3525 N  N     . ALA A 1 458 ? 23.579 16.668  11.670  1.00 31.47  ? 458 ALA A N     1 
ATOM   3526 C  CA    . ALA A 1 458 ? 24.986 16.677  11.299  1.00 32.57  ? 458 ALA A CA    1 
ATOM   3527 C  C     . ALA A 1 458 ? 25.907 16.506  12.497  1.00 33.46  ? 458 ALA A C     1 
ATOM   3528 O  O     . ALA A 1 458 ? 27.032 16.022  12.332  1.00 34.93  ? 458 ALA A O     1 
ATOM   3529 C  CB    . ALA A 1 458 ? 25.322 17.976  10.566  1.00 34.09  ? 458 ALA A CB    1 
ATOM   3530 N  N     . ALA A 1 459 ? 25.459 16.885  13.691  1.00 35.21  ? 459 ALA A N     1 
ATOM   3531 C  CA    . ALA A 1 459 ? 26.286 16.827  14.888  1.00 33.86  ? 459 ALA A CA    1 
ATOM   3532 C  C     . ALA A 1 459 ? 26.079 15.548  15.696  1.00 31.90  ? 459 ALA A C     1 
ATOM   3533 O  O     . ALA A 1 459 ? 26.570 15.459  16.827  1.00 37.25  ? 459 ALA A O     1 
ATOM   3534 C  CB    . ALA A 1 459 ? 26.017 18.051  15.763  1.00 33.01  ? 459 ALA A CB    1 
ATOM   3535 N  N     . MET A 1 460 ? 25.365 14.564  15.151  1.00 28.44  ? 460 MET A N     1 
ATOM   3536 C  CA    . MET A 1 460 ? 25.067 13.344  15.894  1.00 34.22  ? 460 MET A CA    1 
ATOM   3537 C  C     . MET A 1 460 ? 26.332 12.577  16.253  1.00 34.09  ? 460 MET A C     1 
ATOM   3538 O  O     . MET A 1 460 ? 27.230 12.396  15.426  1.00 36.17  ? 460 MET A O     1 
ATOM   3539 C  CB    . MET A 1 460 ? 24.144 12.435  15.086  1.00 28.77  ? 460 MET A CB    1 
ATOM   3540 C  CG    . MET A 1 460 ? 22.705 12.882  15.070  1.00 32.31  ? 460 MET A CG    1 
ATOM   3541 S  SD    . MET A 1 460 ? 21.770 11.890  13.905  1.00 32.95  ? 460 MET A SD    1 
ATOM   3542 C  CE    . MET A 1 460 ? 21.927 10.267  14.653  1.00 27.28  ? 460 MET A CE    1 
ATOM   3543 N  N     . ARG A 1 461 ? 26.387 12.116  17.498  1.00 33.66  ? 461 ARG A N     1 
ATOM   3544 C  CA    . ARG A 1 461 ? 27.464 11.267  17.980  1.00 38.15  ? 461 ARG A CA    1 
ATOM   3545 C  C     . ARG A 1 461 ? 26.857 10.140  18.804  1.00 43.22  ? 461 ARG A C     1 
ATOM   3546 O  O     . ARG A 1 461 ? 25.801 10.306  19.418  1.00 44.13  ? 461 ARG A O     1 
ATOM   3547 C  CB    . ARG A 1 461 ? 28.481 12.063  18.809  1.00 37.03  ? 461 ARG A CB    1 
ATOM   3548 C  CG    . ARG A 1 461 ? 29.201 13.152  18.021  1.00 40.32  ? 461 ARG A CG    1 
ATOM   3549 C  CD    . ARG A 1 461 ? 30.039 14.036  18.934  1.00 38.31  ? 461 ARG A CD    1 
ATOM   3550 N  NE    . ARG A 1 461 ? 31.238 13.355  19.402  1.00 40.31  ? 461 ARG A NE    1 
ATOM   3551 C  CZ    . ARG A 1 461 ? 31.984 13.766  20.417  1.00 40.16  ? 461 ARG A CZ    1 
ATOM   3552 N  NH1   . ARG A 1 461 ? 31.664 14.840  21.118  1.00 41.13  ? 461 ARG A NH1   1 
ATOM   3553 N  NH2   . ARG A 1 461 ? 33.076 13.080  20.739  1.00 47.70  ? 461 ARG A NH2   1 
ATOM   3554 N  N     . SER A 1 462 ? 27.525 8.987   18.804  1.00 44.87  ? 462 SER A N     1 
ATOM   3555 C  CA    . SER A 1 462 ? 26.970 7.798   19.440  1.00 45.84  ? 462 SER A CA    1 
ATOM   3556 C  C     . SER A 1 462 ? 28.078 6.792   19.715  1.00 49.47  ? 462 SER A C     1 
ATOM   3557 O  O     . SER A 1 462 ? 29.143 6.826   19.094  1.00 48.70  ? 462 SER A O     1 
ATOM   3558 C  CB    . SER A 1 462 ? 25.882 7.157   18.571  1.00 41.62  ? 462 SER A CB    1 
ATOM   3559 O  OG    . SER A 1 462 ? 25.402 5.964   19.162  1.00 46.81  ? 462 SER A OG    1 
ATOM   3560 N  N     . GLU A 1 463 ? 27.804 5.890   20.657  1.00 50.94  ? 463 GLU A N     1 
ATOM   3561 C  CA    . GLU A 1 463 ? 28.720 4.795   20.940  1.00 57.07  ? 463 GLU A CA    1 
ATOM   3562 C  C     . GLU A 1 463 ? 28.719 3.783   19.801  1.00 52.39  ? 463 GLU A C     1 
ATOM   3563 O  O     . GLU A 1 463 ? 27.718 3.597   19.104  1.00 46.60  ? 463 GLU A O     1 
ATOM   3564 C  CB    . GLU A 1 463 ? 28.343 4.092   22.242  1.00 59.23  ? 463 GLU A CB    1 
ATOM   3565 C  CG    . GLU A 1 463 ? 28.681 4.859   23.504  1.00 62.49  ? 463 GLU A CG    1 
ATOM   3566 C  CD    . GLU A 1 463 ? 28.509 4.014   24.757  1.00 74.70  ? 463 GLU A CD    1 
ATOM   3567 O  OE1   . GLU A 1 463 ? 27.897 2.925   24.667  1.00 70.00  ? 463 GLU A OE1   1 
ATOM   3568 O  OE2   . GLU A 1 463 ? 28.990 4.436   25.831  1.00 73.40  ? 463 GLU A OE2   1 
ATOM   3569 N  N     . ALA A 1 464 ? 29.858 3.119   19.626  1.00 63.57  ? 464 ALA A N     1 
ATOM   3570 C  CA    . ALA A 1 464 ? 30.014 2.111   18.587  1.00 68.65  ? 464 ALA A CA    1 
ATOM   3571 C  C     . ALA A 1 464 ? 29.273 0.829   18.955  1.00 70.06  ? 464 ALA A C     1 
ATOM   3572 O  O     . ALA A 1 464 ? 29.173 0.453   20.127  1.00 69.50  ? 464 ALA A O     1 
ATOM   3573 C  CB    . ALA A 1 464 ? 31.495 1.805   18.353  1.00 72.34  ? 464 ALA A CB    1 
ATOM   3574 N  N     . THR A 1 465 ? 28.756 0.156   17.934  1.00 71.60  ? 465 THR A N     1 
ATOM   3575 C  CA    . THR A 1 465 ? 27.977 -1.063  18.100  1.00 74.25  ? 465 THR A CA    1 
ATOM   3576 C  C     . THR A 1 465 ? 28.631 -2.206  17.319  1.00 79.00  ? 465 THR A C     1 
ATOM   3577 O  O     . THR A 1 465 ? 29.717 -2.060  16.751  1.00 74.84  ? 465 THR A O     1 
ATOM   3578 C  CB    . THR A 1 465 ? 26.530 -0.834  17.661  1.00 68.99  ? 465 THR A CB    1 
ATOM   3579 O  OG1   . THR A 1 465 ? 26.500 -0.461  16.278  1.00 67.09  ? 465 THR A OG1   1 
ATOM   3580 C  CG2   . THR A 1 465 ? 25.885 0.267   18.494  1.00 64.78  ? 465 THR A CG2   1 
ATOM   3581 N  N     . ALA A 1 466 ? 27.948 -3.350  17.288  1.00 76.38  ? 466 ALA A N     1 
ATOM   3582 C  CA    . ALA A 1 466 ? 28.477 -4.571  16.692  1.00 80.30  ? 466 ALA A CA    1 
ATOM   3583 C  C     . ALA A 1 466 ? 28.048 -4.767  15.241  1.00 77.14  ? 466 ALA A C     1 
ATOM   3584 O  O     . ALA A 1 466 ? 28.335 -5.820  14.660  1.00 72.87  ? 466 ALA A O     1 
ATOM   3585 C  CB    . ALA A 1 466 ? 28.055 -5.784  17.525  1.00 68.84  ? 466 ALA A CB    1 
ATOM   3586 N  N     . ALA A 1 467 ? 27.376 -3.783  14.640  1.00 86.96  ? 467 ALA A N     1 
ATOM   3587 C  CA    . ALA A 1 467 ? 26.932 -3.912  13.257  1.00 74.03  ? 467 ALA A CA    1 
ATOM   3588 C  C     . ALA A 1 467 ? 28.063 -3.723  12.256  1.00 69.83  ? 467 ALA A C     1 
ATOM   3589 O  O     . ALA A 1 467 ? 27.972 -4.236  11.135  1.00 62.75  ? 467 ALA A O     1 
ATOM   3590 C  CB    . ALA A 1 467 ? 25.812 -2.914  12.966  1.00 63.32  ? 467 ALA A CB    1 
ATOM   3591 N  N     . ALA A 1 468 ? 29.116 -2.999  12.633  1.00 72.96  ? 468 ALA A N     1 
ATOM   3592 C  CA    . ALA A 1 468 ? 30.287 -2.838  11.781  1.00 71.33  ? 468 ALA A CA    1 
ATOM   3593 C  C     . ALA A 1 468 ? 31.506 -3.469  12.443  1.00 76.98  ? 468 ALA A C     1 
ATOM   3594 O  O     . ALA A 1 468 ? 31.371 -4.403  13.241  1.00 77.26  ? 468 ALA A O     1 
ATOM   3595 C  CB    . ALA A 1 468 ? 30.534 -1.357  11.486  1.00 74.72  ? 468 ALA A CB    1 
ATOM   3596 N  N     . GLU A 1 469 ? 32.699 -2.965  12.129  1.00 78.71  ? 469 GLU A N     1 
ATOM   3597 C  CA    . GLU A 1 469 ? 33.936 -3.476  12.703  1.00 82.34  ? 469 GLU A CA    1 
ATOM   3598 C  C     . GLU A 1 469 ? 34.482 -2.598  13.822  1.00 86.18  ? 469 GLU A C     1 
ATOM   3599 O  O     . GLU A 1 469 ? 35.552 -2.899  14.360  1.00 84.14  ? 469 GLU A O     1 
ATOM   3600 C  CB    . GLU A 1 469 ? 35.003 -3.639  11.611  1.00 83.79  ? 469 GLU A CB    1 
ATOM   3601 C  CG    . GLU A 1 469 ? 35.555 -2.335  11.045  1.00 79.62  ? 469 GLU A CG    1 
ATOM   3602 C  CD    . GLU A 1 469 ? 34.730 -1.789  9.892   1.00 77.69  ? 469 GLU A CD    1 
ATOM   3603 O  OE1   . GLU A 1 469 ? 33.485 -1.785  9.989   1.00 73.37  ? 469 GLU A OE1   1 
ATOM   3604 O  OE2   . GLU A 1 469 ? 35.333 -1.368  8.881   1.00 76.85  ? 469 GLU A OE2   1 
ATOM   3605 N  N     . HIS A 1 470 ? 33.777 -1.530  14.188  1.00 93.84  ? 470 HIS A N     1 
ATOM   3606 C  CA    . HIS A 1 470 ? 34.245 -0.622  15.227  1.00 95.06  ? 470 HIS A CA    1 
ATOM   3607 C  C     . HIS A 1 470 ? 33.981 -1.233  16.599  1.00 96.45  ? 470 HIS A C     1 
ATOM   3608 O  O     . HIS A 1 470 ? 32.827 -1.481  16.964  1.00 93.76  ? 470 HIS A O     1 
ATOM   3609 C  CB    . HIS A 1 470 ? 33.557 0.735   15.094  1.00 94.10  ? 470 HIS A CB    1 
ATOM   3610 C  CG    . HIS A 1 470 ? 33.638 1.321   13.718  1.00 91.21  ? 470 HIS A CG    1 
ATOM   3611 N  ND1   . HIS A 1 470 ? 34.811 1.810   13.185  1.00 94.84  ? 470 HIS A ND1   1 
ATOM   3612 C  CD2   . HIS A 1 470 ? 32.691 1.495   12.767  1.00 90.71  ? 470 HIS A CD2   1 
ATOM   3613 C  CE1   . HIS A 1 470 ? 34.583 2.261   11.964  1.00 91.13  ? 470 HIS A CE1   1 
ATOM   3614 N  NE2   . HIS A 1 470 ? 33.304 2.082   11.686  1.00 91.42  ? 470 HIS A NE2   1 
ATOM   3615 N  N     . LYS A 1 471 ? 35.048 -1.475  17.355  1.00 94.96  ? 471 LYS A N     1 
ATOM   3616 C  CA    . LYS A 1 471 ? 34.961 -2.076  18.676  1.00 96.36  ? 471 LYS A CA    1 
ATOM   3617 C  C     . LYS A 1 471 ? 35.222 -1.030  19.753  1.00 98.75  ? 471 LYS A C     1 
ATOM   3618 O  O     . LYS A 1 471 ? 35.743 0.057   19.487  1.00 93.03  ? 471 LYS A O     1 
ATOM   3619 C  CB    . LYS A 1 471 ? 35.956 -3.232  18.821  1.00 93.49  ? 471 LYS A CB    1 
ATOM   3620 C  CG    . LYS A 1 471 ? 35.809 -4.320  17.772  1.00 91.93  ? 471 LYS A CG    1 
ATOM   3621 C  CD    . LYS A 1 471 ? 34.422 -4.939  17.805  1.00 94.36  ? 471 LYS A CD    1 
ATOM   3622 C  CE    . LYS A 1 471 ? 34.307 -6.094  16.820  1.00 90.56  ? 471 LYS A CE    1 
ATOM   3623 N  NZ    . LYS A 1 471 ? 35.247 -7.204  17.147  1.00 95.13  ? 471 LYS A NZ    1 
ATOM   3624 N  N     . GLY A 1 472 ? 34.848 -1.377  20.981  1.00 104.84 ? 472 GLY A N     1 
ATOM   3625 C  CA    . GLY A 1 472 ? 35.053 -0.510  22.121  1.00 105.61 ? 472 GLY A CA    1 
ATOM   3626 C  C     . GLY A 1 472 ? 33.880 0.419   22.379  1.00 105.97 ? 472 GLY A C     1 
ATOM   3627 O  O     . GLY A 1 472 ? 32.930 0.524   21.598  1.00 101.23 ? 472 GLY A O     1 
ATOM   3628 N  N     . LYS A 1 473 ? 33.957 1.102   23.518  1.00 122.39 ? 473 LYS A N     1 
ATOM   3629 C  CA    . LYS A 1 473 ? 32.960 2.088   23.923  1.00 117.58 ? 473 LYS A CA    1 
ATOM   3630 C  C     . LYS A 1 473 ? 33.529 3.488   23.711  1.00 119.51 ? 473 LYS A C     1 
ATOM   3631 O  O     . LYS A 1 473 ? 33.875 4.201   24.657  1.00 121.47 ? 473 LYS A O     1 
ATOM   3632 C  CB    . LYS A 1 473 ? 32.541 1.858   25.387  1.00 118.65 ? 473 LYS A CB    1 
ATOM   3633 C  CG    . LYS A 1 473 ? 31.771 0.563   25.617  1.00 119.04 ? 473 LYS A CG    1 
ATOM   3634 C  CD    . LYS A 1 473 ? 30.503 0.520   24.772  1.00 114.18 ? 473 LYS A CD    1 
ATOM   3635 C  CE    . LYS A 1 473 ? 29.726 -0.768  24.989  1.00 113.79 ? 473 LYS A CE    1 
ATOM   3636 N  NZ    . LYS A 1 473 ? 28.478 -0.800  24.177  1.00 111.18 ? 473 LYS A NZ    1 
ATOM   3637 N  N     . VAL A 1 474 ? 33.625 3.877   22.441  1.00 97.04  ? 474 VAL A N     1 
ATOM   3638 C  CA    . VAL A 1 474 ? 34.181 5.162   22.030  1.00 83.69  ? 474 VAL A CA    1 
ATOM   3639 C  C     . VAL A 1 474 ? 33.089 5.945   21.314  1.00 70.58  ? 474 VAL A C     1 
ATOM   3640 O  O     . VAL A 1 474 ? 32.373 5.391   20.473  1.00 71.38  ? 474 VAL A O     1 
ATOM   3641 C  CB    . VAL A 1 474 ? 35.416 4.976   21.128  1.00 79.27  ? 474 VAL A CB    1 
ATOM   3642 C  CG1   . VAL A 1 474 ? 35.787 6.275   20.438  1.00 73.76  ? 474 VAL A CG1   1 
ATOM   3643 C  CG2   . VAL A 1 474 ? 36.587 4.450   21.945  1.00 81.96  ? 474 VAL A CG2   1 
ATOM   3644 N  N     . ILE A 1 475 ? 32.952 7.223   21.654  1.00 63.67  ? 475 ILE A N     1 
ATOM   3645 C  CA    . ILE A 1 475 ? 31.927 8.066   21.048  1.00 58.98  ? 475 ILE A CA    1 
ATOM   3646 C  C     . ILE A 1 475 ? 32.424 8.547   19.690  1.00 56.40  ? 475 ILE A C     1 
ATOM   3647 O  O     . ILE A 1 475 ? 33.421 9.271   19.599  1.00 61.05  ? 475 ILE A O     1 
ATOM   3648 C  CB    . ILE A 1 475 ? 31.569 9.248   21.959  1.00 57.46  ? 475 ILE A CB    1 
ATOM   3649 C  CG1   . ILE A 1 475 ? 31.169 8.749   23.349  1.00 55.01  ? 475 ILE A CG1   1 
ATOM   3650 C  CG2   . ILE A 1 475 ? 30.437 10.059  21.346  1.00 49.67  ? 475 ILE A CG2   1 
ATOM   3651 C  CD1   . ILE A 1 475 ? 30.887 9.865   24.335  1.00 58.63  ? 475 ILE A CD1   1 
ATOM   3652 N  N     . MET A 1 476 ? 31.727 8.147   18.634  1.00 53.96  ? 476 MET A N     1 
ATOM   3653 C  CA    . MET A 1 476 ? 32.084 8.485   17.267  1.00 48.95  ? 476 MET A CA    1 
ATOM   3654 C  C     . MET A 1 476 ? 31.019 9.380   16.652  1.00 43.37  ? 476 MET A C     1 
ATOM   3655 O  O     . MET A 1 476 ? 29.874 9.424   17.107  1.00 43.48  ? 476 MET A O     1 
ATOM   3656 C  CB    . MET A 1 476 ? 32.238 7.228   16.406  1.00 52.07  ? 476 MET A CB    1 
ATOM   3657 C  CG    . MET A 1 476 ? 33.253 6.225   16.905  1.00 60.20  ? 476 MET A CG    1 
ATOM   3658 S  SD    . MET A 1 476 ? 33.138 4.693   15.961  1.00 80.60  ? 476 MET A SD    1 
ATOM   3659 C  CE    . MET A 1 476 ? 33.464 5.296   14.305  1.00 71.26  ? 476 MET A CE    1 
ATOM   3660 N  N     . HIS A 1 477 ? 31.412 10.085  15.594  1.00 40.31  ? 477 HIS A N     1 
ATOM   3661 C  CA    . HIS A 1 477 ? 30.470 10.874  14.817  1.00 37.00  ? 477 HIS A CA    1 
ATOM   3662 C  C     . HIS A 1 477 ? 29.698 9.976   13.862  1.00 40.39  ? 477 HIS A C     1 
ATOM   3663 O  O     . HIS A 1 477 ? 30.261 9.055   13.262  1.00 44.13  ? 477 HIS A O     1 
ATOM   3664 C  CB    . HIS A 1 477 ? 31.206 11.963  14.035  1.00 37.97  ? 477 HIS A CB    1 
ATOM   3665 C  CG    . HIS A 1 477 ? 31.720 13.077  14.892  1.00 39.16  ? 477 HIS A CG    1 
ATOM   3666 N  ND1   . HIS A 1 477 ? 31.015 14.244  15.095  1.00 33.37  ? 477 HIS A ND1   1 
ATOM   3667 C  CD2   . HIS A 1 477 ? 32.865 13.200  15.605  1.00 38.81  ? 477 HIS A CD2   1 
ATOM   3668 C  CE1   . HIS A 1 477 ? 31.705 15.039  15.894  1.00 40.48  ? 477 HIS A CE1   1 
ATOM   3669 N  NE2   . HIS A 1 477 ? 32.832 14.431  16.216  1.00 41.31  ? 477 HIS A NE2   1 
ATOM   3670 N  N     . ASP A 1 478 ? 28.397 10.240  13.726  1.00 35.68  ? 478 ASP A N     1 
ATOM   3671 C  CA    . ASP A 1 478 ? 27.536 9.470   12.825  1.00 34.42  ? 478 ASP A CA    1 
ATOM   3672 C  C     . ASP A 1 478 ? 26.407 10.365  12.341  1.00 35.60  ? 478 ASP A C     1 
ATOM   3673 O  O     . ASP A 1 478 ? 25.232 10.144  12.659  1.00 35.53  ? 478 ASP A O     1 
ATOM   3674 C  CB    . ASP A 1 478 ? 26.993 8.223   13.522  1.00 38.80  ? 478 ASP A CB    1 
ATOM   3675 C  CG    . ASP A 1 478 ? 26.671 7.103   12.547  1.00 39.40  ? 478 ASP A CG    1 
ATOM   3676 O  OD1   . ASP A 1 478 ? 26.310 7.402   11.388  1.00 41.79  ? 478 ASP A OD1   1 
ATOM   3677 O  OD2   . ASP A 1 478 ? 26.787 5.923   12.942  1.00 38.46  ? 478 ASP A OD2   1 
ATOM   3678 N  N     . PRO A 1 479 ? 26.728 11.380  11.537  1.00 33.46  ? 479 PRO A N     1 
ATOM   3679 C  CA    . PRO A 1 479 ? 25.719 12.379  11.165  1.00 32.07  ? 479 PRO A CA    1 
ATOM   3680 C  C     . PRO A 1 479 ? 24.563 11.750  10.402  1.00 33.99  ? 479 PRO A C     1 
ATOM   3681 O  O     . PRO A 1 479 ? 24.763 10.965  9.473   1.00 37.65  ? 479 PRO A O     1 
ATOM   3682 C  CB    . PRO A 1 479 ? 26.502 13.371  10.296  1.00 35.41  ? 479 PRO A CB    1 
ATOM   3683 C  CG    . PRO A 1 479 ? 27.660 12.601  9.774   1.00 39.97  ? 479 PRO A CG    1 
ATOM   3684 C  CD    . PRO A 1 479 ? 28.009 11.591  10.838  1.00 35.72  ? 479 PRO A CD    1 
ATOM   3685 N  N     . PHE A 1 480 ? 23.343 12.096  10.818  1.00 33.06  ? 480 PHE A N     1 
ATOM   3686 C  CA    . PHE A 1 480 ? 22.104 11.557  10.258  1.00 34.27  ? 480 PHE A CA    1 
ATOM   3687 C  C     . PHE A 1 480 ? 22.045 10.034  10.329  1.00 33.09  ? 480 PHE A C     1 
ATOM   3688 O  O     . PHE A 1 480 ? 21.227 9.413   9.641   1.00 34.94  ? 480 PHE A O     1 
ATOM   3689 C  CB    . PHE A 1 480 ? 21.896 12.021  8.811   1.00 36.20  ? 480 PHE A CB    1 
ATOM   3690 C  CG    . PHE A 1 480 ? 21.555 13.482  8.681   1.00 38.83  ? 480 PHE A CG    1 
ATOM   3691 C  CD1   . PHE A 1 480 ? 22.540 14.452  8.796   1.00 34.65  ? 480 PHE A CD1   1 
ATOM   3692 C  CD2   . PHE A 1 480 ? 20.252 13.884  8.429   1.00 35.69  ? 480 PHE A CD2   1 
ATOM   3693 C  CE1   . PHE A 1 480 ? 22.231 15.795  8.671   1.00 35.26  ? 480 PHE A CE1   1 
ATOM   3694 C  CE2   . PHE A 1 480 ? 19.936 15.227  8.299   1.00 38.24  ? 480 PHE A CE2   1 
ATOM   3695 C  CZ    . PHE A 1 480 ? 20.928 16.184  8.420   1.00 34.61  ? 480 PHE A CZ    1 
ATOM   3696 N  N     . ALA A 1 481 ? 22.900 9.425   11.154  1.00 31.73  ? 481 ALA A N     1 
ATOM   3697 C  CA    . ALA A 1 481 ? 23.052 7.968   11.221  1.00 40.26  ? 481 ALA A CA    1 
ATOM   3698 C  C     . ALA A 1 481 ? 23.408 7.372   9.861   1.00 35.59  ? 481 ALA A C     1 
ATOM   3699 O  O     . ALA A 1 481 ? 23.038 6.236   9.552   1.00 37.24  ? 481 ALA A O     1 
ATOM   3700 C  CB    . ALA A 1 481 ? 21.795 7.297   11.783  1.00 31.84  ? 481 ALA A CB    1 
ATOM   3701 N  N     . MET A 1 482 ? 24.138 8.132   9.044   1.00 34.27  ? 482 MET A N     1 
ATOM   3702 C  CA    . MET A 1 482 ? 24.433 7.738   7.673   1.00 35.48  ? 482 MET A CA    1 
ATOM   3703 C  C     . MET A 1 482 ? 25.922 7.656   7.373   1.00 34.31  ? 482 MET A C     1 
ATOM   3704 O  O     . MET A 1 482 ? 26.291 7.540   6.198   1.00 40.77  ? 482 MET A O     1 
ATOM   3705 C  CB    . MET A 1 482 ? 23.773 8.710   6.694   1.00 36.99  ? 482 MET A CB    1 
ATOM   3706 C  CG    . MET A 1 482 ? 22.285 8.531   6.580   1.00 35.46  ? 482 MET A CG    1 
ATOM   3707 S  SD    . MET A 1 482 ? 21.896 7.336   5.303   1.00 39.10  ? 482 MET A SD    1 
ATOM   3708 C  CE    . MET A 1 482 ? 22.307 8.290   3.842   1.00 34.82  ? 482 MET A CE    1 
ATOM   3709 N  N     . ARG A 1 483 ? 26.785 7.711   8.388   1.00 32.12  ? 483 ARG A N     1 
ATOM   3710 C  CA    . ARG A 1 483 ? 28.223 7.675   8.124   1.00 38.12  ? 483 ARG A CA    1 
ATOM   3711 C  C     . ARG A 1 483 ? 28.653 6.483   7.276   1.00 42.38  ? 483 ARG A C     1 
ATOM   3712 O  O     . ARG A 1 483 ? 29.443 6.681   6.335   1.00 46.16  ? 483 ARG A O     1 
ATOM   3713 C  CB    . ARG A 1 483 ? 29.002 7.714   9.441   1.00 37.32  ? 483 ARG A CB    1 
ATOM   3714 C  CG    . ARG A 1 483 ? 30.489 7.931   9.232   1.00 37.26  ? 483 ARG A CG    1 
ATOM   3715 C  CD    . ARG A 1 483 ? 31.298 7.655   10.482  1.00 39.21  ? 483 ARG A CD    1 
ATOM   3716 N  NE    . ARG A 1 483 ? 31.432 6.225   10.728  1.00 50.08  ? 483 ARG A NE    1 
ATOM   3717 C  CZ    . ARG A 1 483 ? 30.693 5.538   11.587  1.00 53.42  ? 483 ARG A CZ    1 
ATOM   3718 N  NH1   . ARG A 1 483 ? 29.770 6.128   12.329  1.00 47.57  ? 483 ARG A NH1   1 
ATOM   3719 N  NH2   . ARG A 1 483 ? 30.883 4.226   11.703  1.00 63.59  ? 483 ARG A NH2   1 
ATOM   3720 N  N     . PRO A 1 484 ? 28.202 5.250   7.525   1.00 44.96  ? 484 PRO A N     1 
ATOM   3721 C  CA    . PRO A 1 484 ? 28.630 4.131   6.676   1.00 41.04  ? 484 PRO A CA    1 
ATOM   3722 C  C     . PRO A 1 484 ? 27.920 4.059   5.336   1.00 40.77  ? 484 PRO A C     1 
ATOM   3723 O  O     . PRO A 1 484 ? 28.226 3.160   4.543   1.00 42.27  ? 484 PRO A O     1 
ATOM   3724 C  CB    . PRO A 1 484 ? 28.289 2.893   7.531   1.00 45.72  ? 484 PRO A CB    1 
ATOM   3725 C  CG    . PRO A 1 484 ? 27.952 3.414   8.896   1.00 42.57  ? 484 PRO A CG    1 
ATOM   3726 C  CD    . PRO A 1 484 ? 27.398 4.769   8.663   1.00 38.81  ? 484 PRO A CD    1 
ATOM   3727 N  N     . PHE A 1 485 ? 26.987 4.972   5.055   1.00 40.34  ? 485 PHE A N     1 
ATOM   3728 C  CA    . PHE A 1 485 ? 26.078 4.799   3.930   1.00 43.31  ? 485 PHE A CA    1 
ATOM   3729 C  C     . PHE A 1 485 ? 25.993 6.016   3.012   1.00 40.86  ? 485 PHE A C     1 
ATOM   3730 O  O     . PHE A 1 485 ? 25.126 6.045   2.131   1.00 40.54  ? 485 PHE A O     1 
ATOM   3731 C  CB    . PHE A 1 485 ? 24.675 4.440   4.439   1.00 37.57  ? 485 PHE A CB    1 
ATOM   3732 C  CG    . PHE A 1 485 ? 24.665 3.390   5.524   1.00 39.15  ? 485 PHE A CG    1 
ATOM   3733 C  CD1   . PHE A 1 485 ? 24.968 2.066   5.236   1.00 37.45  ? 485 PHE A CD1   1 
ATOM   3734 C  CD2   . PHE A 1 485 ? 24.340 3.727   6.832   1.00 37.42  ? 485 PHE A CD2   1 
ATOM   3735 C  CE1   . PHE A 1 485 ? 24.955 1.098   6.234   1.00 41.47  ? 485 PHE A CE1   1 
ATOM   3736 C  CE2   . PHE A 1 485 ? 24.322 2.764   7.832   1.00 41.76  ? 485 PHE A CE2   1 
ATOM   3737 C  CZ    . PHE A 1 485 ? 24.627 1.448   7.535   1.00 37.08  ? 485 PHE A CZ    1 
ATOM   3738 N  N     . PHE A 1 486 ? 26.855 7.015   3.178   1.00 36.55  ? 486 PHE A N     1 
ATOM   3739 C  CA    . PHE A 1 486 ? 26.804 8.177   2.296   1.00 44.16  ? 486 PHE A CA    1 
ATOM   3740 C  C     . PHE A 1 486 ? 27.177 7.756   0.881   1.00 41.17  ? 486 PHE A C     1 
ATOM   3741 O  O     . PHE A 1 486 ? 28.233 7.153   0.661   1.00 44.57  ? 486 PHE A O     1 
ATOM   3742 C  CB    . PHE A 1 486 ? 27.727 9.290   2.794   1.00 37.30  ? 486 PHE A CB    1 
ATOM   3743 C  CG    . PHE A 1 486 ? 27.211 10.002  4.013   1.00 36.71  ? 486 PHE A CG    1 
ATOM   3744 C  CD1   . PHE A 1 486 ? 25.974 10.625  3.993   1.00 35.26  ? 486 PHE A CD1   1 
ATOM   3745 C  CD2   . PHE A 1 486 ? 27.961 10.050  5.177   1.00 38.90  ? 486 PHE A CD2   1 
ATOM   3746 C  CE1   . PHE A 1 486 ? 25.491 11.277  5.112   1.00 36.56  ? 486 PHE A CE1   1 
ATOM   3747 C  CE2   . PHE A 1 486 ? 27.485 10.705  6.300   1.00 39.10  ? 486 PHE A CE2   1 
ATOM   3748 C  CZ    . PHE A 1 486 ? 26.247 11.316  6.268   1.00 36.92  ? 486 PHE A CZ    1 
ATOM   3749 N  N     . GLY A 1 487 ? 26.294 8.044   -0.073  1.00 43.06  ? 487 GLY A N     1 
ATOM   3750 C  CA    . GLY A 1 487 ? 26.557 7.733   -1.462  1.00 44.30  ? 487 GLY A CA    1 
ATOM   3751 C  C     . GLY A 1 487 ? 27.330 8.784   -2.220  1.00 43.03  ? 487 GLY A C     1 
ATOM   3752 O  O     . GLY A 1 487 ? 27.799 8.511   -3.330  1.00 42.22  ? 487 GLY A O     1 
ATOM   3753 N  N     . TYR A 1 488 ? 27.486 9.974   -1.644  1.00 39.87  ? 488 TYR A N     1 
ATOM   3754 C  CA    . TYR A 1 488 ? 28.156 11.087  -2.310  1.00 41.78  ? 488 TYR A CA    1 
ATOM   3755 C  C     . TYR A 1 488 ? 28.653 12.065  -1.248  1.00 41.74  ? 488 TYR A C     1 
ATOM   3756 O  O     . TYR A 1 488 ? 28.561 11.802  -0.043  1.00 43.07  ? 488 TYR A O     1 
ATOM   3757 C  CB    . TYR A 1 488 ? 27.221 11.768  -3.315  1.00 43.43  ? 488 TYR A CB    1 
ATOM   3758 C  CG    . TYR A 1 488 ? 26.007 12.406  -2.681  1.00 41.53  ? 488 TYR A CG    1 
ATOM   3759 C  CD1   . TYR A 1 488 ? 24.905 11.638  -2.316  1.00 40.79  ? 488 TYR A CD1   1 
ATOM   3760 C  CD2   . TYR A 1 488 ? 25.960 13.777  -2.451  1.00 40.68  ? 488 TYR A CD2   1 
ATOM   3761 C  CE1   . TYR A 1 488 ? 23.792 12.216  -1.732  1.00 46.44  ? 488 TYR A CE1   1 
ATOM   3762 C  CE2   . TYR A 1 488 ? 24.850 14.367  -1.871  1.00 45.27  ? 488 TYR A CE2   1 
ATOM   3763 C  CZ    . TYR A 1 488 ? 23.769 13.581  -1.510  1.00 44.92  ? 488 TYR A CZ    1 
ATOM   3764 O  OH    . TYR A 1 488 ? 22.659 14.157  -0.932  1.00 45.95  ? 488 TYR A OH    1 
ATOM   3765 N  N     . ASN A 1 489 ? 29.171 13.204  -1.709  1.00 42.39  ? 489 ASN A N     1 
ATOM   3766 C  CA    . ASN A 1 489 ? 29.781 14.201  -0.835  1.00 47.13  ? 489 ASN A CA    1 
ATOM   3767 C  C     . ASN A 1 489 ? 28.825 14.623  0.276   1.00 43.94  ? 489 ASN A C     1 
ATOM   3768 O  O     . ASN A 1 489 ? 27.692 15.040  0.016   1.00 41.37  ? 489 ASN A O     1 
ATOM   3769 C  CB    . ASN A 1 489 ? 30.202 15.420  -1.661  1.00 44.66  ? 489 ASN A CB    1 
ATOM   3770 C  CG    . ASN A 1 489 ? 31.036 16.411  -0.867  1.00 47.45  ? 489 ASN A CG    1 
ATOM   3771 O  OD1   . ASN A 1 489 ? 30.519 17.142  -0.022  1.00 45.94  ? 489 ASN A OD1   1 
ATOM   3772 N  ND2   . ASN A 1 489 ? 32.332 16.447  -1.146  1.00 42.90  ? 489 ASN A ND2   1 
ATOM   3773 N  N     . PHE A 1 490 ? 29.294 14.521  1.523   1.00 42.28  ? 490 PHE A N     1 
ATOM   3774 C  CA    . PHE A 1 490 ? 28.444 14.832  2.667   1.00 40.76  ? 490 PHE A CA    1 
ATOM   3775 C  C     . PHE A 1 490 ? 28.114 16.319  2.745   1.00 42.18  ? 490 PHE A C     1 
ATOM   3776 O  O     . PHE A 1 490 ? 27.021 16.685  3.197   1.00 39.13  ? 490 PHE A O     1 
ATOM   3777 C  CB    . PHE A 1 490 ? 29.112 14.359  3.959   1.00 41.79  ? 490 PHE A CB    1 
ATOM   3778 C  CG    . PHE A 1 490 ? 28.366 14.747  5.206   1.00 40.96  ? 490 PHE A CG    1 
ATOM   3779 C  CD1   . PHE A 1 490 ? 27.016 14.472  5.339   1.00 35.74  ? 490 PHE A CD1   1 
ATOM   3780 C  CD2   . PHE A 1 490 ? 29.019 15.380  6.248   1.00 40.50  ? 490 PHE A CD2   1 
ATOM   3781 C  CE1   . PHE A 1 490 ? 26.333 14.831  6.481   1.00 35.47  ? 490 PHE A CE1   1 
ATOM   3782 C  CE2   . PHE A 1 490 ? 28.342 15.732  7.396   1.00 39.14  ? 490 PHE A CE2   1 
ATOM   3783 C  CZ    . PHE A 1 490 ? 26.997 15.462  7.511   1.00 33.59  ? 490 PHE A CZ    1 
ATOM   3784 N  N     . GLY A 1 491 ? 29.038 17.187  2.327   1.00 43.65  ? 491 GLY A N     1 
ATOM   3785 C  CA    . GLY A 1 491 ? 28.713 18.602  2.236   1.00 39.47  ? 491 GLY A CA    1 
ATOM   3786 C  C     . GLY A 1 491 ? 27.543 18.862  1.306   1.00 38.82  ? 491 GLY A C     1 
ATOM   3787 O  O     . GLY A 1 491 ? 26.599 19.574  1.658   1.00 39.85  ? 491 GLY A O     1 
ATOM   3788 N  N     . LYS A 1 492 ? 27.590 18.283  0.103   1.00 38.02  ? 492 LYS A N     1 
ATOM   3789 C  CA    . LYS A 1 492 ? 26.457 18.384  -0.813  1.00 40.83  ? 492 LYS A CA    1 
ATOM   3790 C  C     . LYS A 1 492 ? 25.209 17.740  -0.226  1.00 39.87  ? 492 LYS A C     1 
ATOM   3791 O  O     . LYS A 1 492 ? 24.090 18.186  -0.504  1.00 40.96  ? 492 LYS A O     1 
ATOM   3792 C  CB    . LYS A 1 492 ? 26.801 17.732  -2.152  1.00 45.59  ? 492 LYS A CB    1 
ATOM   3793 C  CG    . LYS A 1 492 ? 28.070 18.256  -2.787  1.00 46.10  ? 492 LYS A CG    1 
ATOM   3794 C  CD    . LYS A 1 492 ? 27.966 19.743  -3.060  1.00 50.94  ? 492 LYS A CD    1 
ATOM   3795 C  CE    . LYS A 1 492 ? 29.240 20.271  -3.692  1.00 56.95  ? 492 LYS A CE    1 
ATOM   3796 N  NZ    . LYS A 1 492 ? 29.163 21.734  -3.926  1.00 67.84  ? 492 LYS A NZ    1 
ATOM   3797 N  N     . TYR A 1 493 ? 25.382 16.686  0.575   1.00 42.24  ? 493 TYR A N     1 
ATOM   3798 C  CA    . TYR A 1 493 ? 24.249 16.077  1.263   1.00 37.30  ? 493 TYR A CA    1 
ATOM   3799 C  C     . TYR A 1 493 ? 23.599 17.067  2.227   1.00 37.52  ? 493 TYR A C     1 
ATOM   3800 O  O     . TYR A 1 493 ? 22.370 17.210  2.245   1.00 35.41  ? 493 TYR A O     1 
ATOM   3801 C  CB    . TYR A 1 493 ? 24.720 14.810  1.982   1.00 36.92  ? 493 TYR A CB    1 
ATOM   3802 C  CG    . TYR A 1 493 ? 23.711 14.136  2.888   1.00 36.01  ? 493 TYR A CG    1 
ATOM   3803 C  CD1   . TYR A 1 493 ? 22.824 13.187  2.394   1.00 37.43  ? 493 TYR A CD1   1 
ATOM   3804 C  CD2   . TYR A 1 493 ? 23.674 14.422  4.248   1.00 37.77  ? 493 TYR A CD2   1 
ATOM   3805 C  CE1   . TYR A 1 493 ? 21.912 12.553  3.230   1.00 35.95  ? 493 TYR A CE1   1 
ATOM   3806 C  CE2   . TYR A 1 493 ? 22.769 13.795  5.088   1.00 38.93  ? 493 TYR A CE2   1 
ATOM   3807 C  CZ    . TYR A 1 493 ? 21.891 12.864  4.574   1.00 40.77  ? 493 TYR A CZ    1 
ATOM   3808 O  OH    . TYR A 1 493 ? 20.991 12.246  5.416   1.00 40.90  ? 493 TYR A OH    1 
ATOM   3809 N  N     . LEU A 1 494 ? 24.406 17.780  3.015   1.00 34.69  ? 494 LEU A N     1 
ATOM   3810 C  CA    . LEU A 1 494 ? 23.860 18.811  3.897   1.00 38.42  ? 494 LEU A CA    1 
ATOM   3811 C  C     . LEU A 1 494 ? 23.138 19.895  3.103   1.00 39.39  ? 494 LEU A C     1 
ATOM   3812 O  O     . LEU A 1 494 ? 22.027 20.305  3.460   1.00 38.53  ? 494 LEU A O     1 
ATOM   3813 C  CB    . LEU A 1 494 ? 24.975 19.421  4.748   1.00 41.43  ? 494 LEU A CB    1 
ATOM   3814 C  CG    . LEU A 1 494 ? 25.599 18.498  5.795   1.00 38.07  ? 494 LEU A CG    1 
ATOM   3815 C  CD1   . LEU A 1 494 ? 26.803 19.165  6.450   1.00 37.86  ? 494 LEU A CD1   1 
ATOM   3816 C  CD2   . LEU A 1 494 ? 24.571 18.096  6.835   1.00 32.48  ? 494 LEU A CD2   1 
ATOM   3817 N  N     . ALA A 1 495 ? 23.753 20.375  2.018   1.00 42.72  ? 495 ALA A N     1 
ATOM   3818 C  CA    . ALA A 1 495 ? 23.115 21.419  1.220   1.00 40.79  ? 495 ALA A CA    1 
ATOM   3819 C  C     . ALA A 1 495 ? 21.809 20.932  0.607   1.00 43.22  ? 495 ALA A C     1 
ATOM   3820 O  O     . ALA A 1 495 ? 20.870 21.718  0.437   1.00 46.85  ? 495 ALA A O     1 
ATOM   3821 C  CB    . ALA A 1 495 ? 24.066 21.910  0.130   1.00 38.23  ? 495 ALA A CB    1 
ATOM   3822 N  N     . HIS A 1 496 ? 21.731 19.644  0.272   1.00 40.72  ? 496 HIS A N     1 
ATOM   3823 C  CA    . HIS A 1 496 ? 20.493 19.087  -0.261  1.00 38.85  ? 496 HIS A CA    1 
ATOM   3824 C  C     . HIS A 1 496 ? 19.390 19.101  0.792   1.00 43.62  ? 496 HIS A C     1 
ATOM   3825 O  O     . HIS A 1 496 ? 18.230 19.402  0.483   1.00 43.13  ? 496 HIS A O     1 
ATOM   3826 C  CB    . HIS A 1 496 ? 20.761 17.670  -0.773  1.00 44.02  ? 496 HIS A CB    1 
ATOM   3827 C  CG    . HIS A 1 496 ? 19.586 17.023  -1.436  1.00 44.80  ? 496 HIS A CG    1 
ATOM   3828 N  ND1   . HIS A 1 496 ? 18.885 17.621  -2.461  1.00 45.80  ? 496 HIS A ND1   1 
ATOM   3829 C  CD2   . HIS A 1 496 ? 19.004 15.818  -1.234  1.00 36.30  ? 496 HIS A CD2   1 
ATOM   3830 C  CE1   . HIS A 1 496 ? 17.912 16.817  -2.853  1.00 44.87  ? 496 HIS A CE1   1 
ATOM   3831 N  NE2   . HIS A 1 496 ? 17.965 15.715  -2.126  1.00 39.38  ? 496 HIS A NE2   1 
ATOM   3832 N  N     . TRP A 1 497 ? 19.735 18.784  2.043   1.00 39.61  ? 497 TRP A N     1 
ATOM   3833 C  CA    . TRP A 1 497 ? 18.760 18.855  3.127   1.00 38.41  ? 497 TRP A CA    1 
ATOM   3834 C  C     . TRP A 1 497 ? 18.298 20.288  3.362   1.00 45.02  ? 497 TRP A C     1 
ATOM   3835 O  O     . TRP A 1 497 ? 17.098 20.541  3.518   1.00 42.73  ? 497 TRP A O     1 
ATOM   3836 C  CB    . TRP A 1 497 ? 19.356 18.268  4.407   1.00 33.79  ? 497 TRP A CB    1 
ATOM   3837 C  CG    . TRP A 1 497 ? 19.032 16.817  4.610   1.00 39.84  ? 497 TRP A CG    1 
ATOM   3838 C  CD1   . TRP A 1 497 ? 19.659 15.745  4.039   1.00 38.14  ? 497 TRP A CD1   1 
ATOM   3839 C  CD2   . TRP A 1 497 ? 18.002 16.279  5.445   1.00 39.48  ? 497 TRP A CD2   1 
ATOM   3840 N  NE1   . TRP A 1 497 ? 19.080 14.576  4.466   1.00 39.85  ? 497 TRP A NE1   1 
ATOM   3841 C  CE2   . TRP A 1 497 ? 18.060 14.876  5.329   1.00 41.00  ? 497 TRP A CE2   1 
ATOM   3842 C  CE3   . TRP A 1 497 ? 17.035 16.849  6.279   1.00 39.18  ? 497 TRP A CE3   1 
ATOM   3843 C  CZ2   . TRP A 1 497 ? 17.190 14.035  6.021   1.00 41.17  ? 497 TRP A CZ2   1 
ATOM   3844 C  CZ3   . TRP A 1 497 ? 16.172 16.013  6.961   1.00 38.43  ? 497 TRP A CZ3   1 
ATOM   3845 C  CH2   . TRP A 1 497 ? 16.255 14.622  6.828   1.00 39.80  ? 497 TRP A CH2   1 
ATOM   3846 N  N     . LEU A 1 498 ? 19.238 21.238  3.385   1.00 42.65  ? 498 LEU A N     1 
ATOM   3847 C  CA    . LEU A 1 498 ? 18.880 22.637  3.594   1.00 44.93  ? 498 LEU A CA    1 
ATOM   3848 C  C     . LEU A 1 498 ? 17.982 23.161  2.482   1.00 46.33  ? 498 LEU A C     1 
ATOM   3849 O  O     . LEU A 1 498 ? 17.110 23.999  2.737   1.00 51.97  ? 498 LEU A O     1 
ATOM   3850 C  CB    . LEU A 1 498 ? 20.142 23.492  3.701   1.00 44.09  ? 498 LEU A CB    1 
ATOM   3851 C  CG    . LEU A 1 498 ? 21.038 23.211  4.909   1.00 44.77  ? 498 LEU A CG    1 
ATOM   3852 C  CD1   . LEU A 1 498 ? 22.332 23.999  4.814   1.00 46.32  ? 498 LEU A CD1   1 
ATOM   3853 C  CD2   . LEU A 1 498 ? 20.305 23.541  6.200   1.00 42.96  ? 498 LEU A CD2   1 
ATOM   3854 N  N     . SER A 1 499 ? 18.166 22.674  1.254   1.00 43.51  ? 499 SER A N     1 
ATOM   3855 C  CA    . SER A 1 499 ? 17.392 23.169  0.121   1.00 52.90  ? 499 SER A CA    1 
ATOM   3856 C  C     . SER A 1 499 ? 15.912 22.827  0.216   1.00 51.57  ? 499 SER A C     1 
ATOM   3857 O  O     . SER A 1 499 ? 15.115 23.400  -0.536  1.00 57.07  ? 499 SER A O     1 
ATOM   3858 C  CB    . SER A 1 499 ? 17.962 22.617  -1.188  1.00 50.45  ? 499 SER A CB    1 
ATOM   3859 O  OG    . SER A 1 499 ? 17.856 21.204  -1.236  1.00 52.90  ? 499 SER A OG    1 
ATOM   3860 N  N     . MET A 1 500 ? 15.523 21.918  1.113   1.00 50.68  ? 500 MET A N     1 
ATOM   3861 C  CA    . MET A 1 500 ? 14.113 21.567  1.234   1.00 52.79  ? 500 MET A CA    1 
ATOM   3862 C  C     . MET A 1 500 ? 13.287 22.730  1.773   1.00 56.64  ? 500 MET A C     1 
ATOM   3863 O  O     . MET A 1 500 ? 12.092 22.830  1.470   1.00 60.84  ? 500 MET A O     1 
ATOM   3864 C  CB    . MET A 1 500 ? 13.958 20.333  2.123   1.00 49.62  ? 500 MET A CB    1 
ATOM   3865 C  CG    . MET A 1 500 ? 14.664 19.095  1.586   1.00 52.83  ? 500 MET A CG    1 
ATOM   3866 S  SD    . MET A 1 500 ? 14.119 18.662  -0.080  1.00 67.27  ? 500 MET A SD    1 
ATOM   3867 C  CE    . MET A 1 500 ? 15.277 17.363  -0.505  1.00 48.04  ? 500 MET A CE    1 
ATOM   3868 N  N     . ALA A 1 501 ? 13.901 23.623  2.553   1.00 53.84  ? 501 ALA A N     1 
ATOM   3869 C  CA    . ALA A 1 501 ? 13.181 24.779  3.073   1.00 60.29  ? 501 ALA A CA    1 
ATOM   3870 C  C     . ALA A 1 501 ? 12.819 25.779  1.983   1.00 65.76  ? 501 ALA A C     1 
ATOM   3871 O  O     . ALA A 1 501 ? 11.951 26.629  2.204   1.00 68.06  ? 501 ALA A O     1 
ATOM   3872 C  CB    . ALA A 1 501 ? 14.008 25.473  4.155   1.00 59.86  ? 501 ALA A CB    1 
ATOM   3873 N  N     . HIS A 1 502 ? 13.456 25.697  0.818   1.00 67.67  ? 502 HIS A N     1 
ATOM   3874 C  CA    . HIS A 1 502 ? 13.189 26.609  -0.286  1.00 72.30  ? 502 HIS A CA    1 
ATOM   3875 C  C     . HIS A 1 502 ? 12.094 26.110  -1.222  1.00 78.42  ? 502 HIS A C     1 
ATOM   3876 O  O     . HIS A 1 502 ? 11.840 26.749  -2.248  1.00 85.57  ? 502 HIS A O     1 
ATOM   3877 C  CB    . HIS A 1 502 ? 14.473 26.856  -1.090  1.00 72.15  ? 502 HIS A CB    1 
ATOM   3878 C  CG    . HIS A 1 502 ? 15.625 27.337  -0.262  1.00 72.63  ? 502 HIS A CG    1 
ATOM   3879 N  ND1   . HIS A 1 502 ? 16.939 27.148  -0.636  1.00 76.49  ? 502 HIS A ND1   1 
ATOM   3880 C  CD2   . HIS A 1 502 ? 15.662 28.002  0.917   1.00 70.91  ? 502 HIS A CD2   1 
ATOM   3881 C  CE1   . HIS A 1 502 ? 17.735 27.673  0.278   1.00 77.11  ? 502 HIS A CE1   1 
ATOM   3882 N  NE2   . HIS A 1 502 ? 16.986 28.199  1.231   1.00 76.83  ? 502 HIS A NE2   1 
ATOM   3883 N  N     . ARG A 1 503 ? 11.444 24.990  -0.901  1.00 77.14  ? 503 ARG A N     1 
ATOM   3884 C  CA    . ARG A 1 503 ? 10.410 24.451  -1.769  1.00 82.56  ? 503 ARG A CA    1 
ATOM   3885 C  C     . ARG A 1 503 ? 9.080  25.170  -1.548  1.00 91.91  ? 503 ARG A C     1 
ATOM   3886 O  O     . ARG A 1 503 ? 8.778  25.606  -0.433  1.00 86.15  ? 503 ARG A O     1 
ATOM   3887 C  CB    . ARG A 1 503 ? 10.232 22.956  -1.526  1.00 82.98  ? 503 ARG A CB    1 
ATOM   3888 C  CG    . ARG A 1 503 ? 11.393 22.115  -2.013  1.00 79.06  ? 503 ARG A CG    1 
ATOM   3889 C  CD    . ARG A 1 503 ? 10.905 20.797  -2.586  1.00 81.73  ? 503 ARG A CD    1 
ATOM   3890 N  NE    . ARG A 1 503 ? 11.984 20.053  -3.223  1.00 85.37  ? 503 ARG A NE    1 
ATOM   3891 C  CZ    . ARG A 1 503 ? 11.814 18.949  -3.937  1.00 77.71  ? 503 ARG A CZ    1 
ATOM   3892 N  NH1   . ARG A 1 503 ? 10.612 18.431  -4.134  1.00 75.72  ? 503 ARG A NH1   1 
ATOM   3893 N  NH2   . ARG A 1 503 ? 12.876 18.351  -4.469  1.00 76.14  ? 503 ARG A NH2   1 
ATOM   3894 N  N     . PRO A 1 504 ? 8.271  25.305  -2.600  1.00 100.31 ? 504 PRO A N     1 
ATOM   3895 C  CA    . PRO A 1 504 ? 6.996  26.025  -2.466  1.00 101.92 ? 504 PRO A CA    1 
ATOM   3896 C  C     . PRO A 1 504 ? 5.998  25.240  -1.626  1.00 101.32 ? 504 PRO A C     1 
ATOM   3897 O  O     . PRO A 1 504 ? 5.760  24.054  -1.865  1.00 102.22 ? 504 PRO A O     1 
ATOM   3898 C  CB    . PRO A 1 504 ? 6.515  26.173  -3.916  1.00 102.57 ? 504 PRO A CB    1 
ATOM   3899 C  CG    . PRO A 1 504 ? 7.726  25.919  -4.765  1.00 104.50 ? 504 PRO A CG    1 
ATOM   3900 C  CD    . PRO A 1 504 ? 8.548  24.935  -3.997  1.00 101.65 ? 504 PRO A CD    1 
ATOM   3901 N  N     . ALA A 1 505 ? 5.415  25.921  -0.636  1.00 91.29  ? 505 ALA A N     1 
ATOM   3902 C  CA    . ALA A 1 505 ? 4.371  25.355  0.218   1.00 82.67  ? 505 ALA A CA    1 
ATOM   3903 C  C     . ALA A 1 505 ? 4.827  24.069  0.901   1.00 77.20  ? 505 ALA A C     1 
ATOM   3904 O  O     . ALA A 1 505 ? 4.014  23.194  1.208   1.00 72.68  ? 505 ALA A O     1 
ATOM   3905 C  CB    . ALA A 1 505 ? 3.080  25.113  -0.569  1.00 78.38  ? 505 ALA A CB    1 
ATOM   3906 N  N     . ALA A 1 506 ? 6.128  23.948  1.148   1.00 74.49  ? 506 ALA A N     1 
ATOM   3907 C  CA    . ALA A 1 506 ? 6.671  22.744  1.763   1.00 71.74  ? 506 ALA A CA    1 
ATOM   3908 C  C     . ALA A 1 506 ? 6.308  22.702  3.242   1.00 64.74  ? 506 ALA A C     1 
ATOM   3909 O  O     . ALA A 1 506 ? 6.663  23.609  4.002   1.00 60.38  ? 506 ALA A O     1 
ATOM   3910 C  CB    . ALA A 1 506 ? 8.186  22.693  1.579   1.00 70.65  ? 506 ALA A CB    1 
ATOM   3911 N  N     . LYS A 1 507 ? 5.595  21.650  3.644   1.00 62.33  ? 507 LYS A N     1 
ATOM   3912 C  CA    . LYS A 1 507 ? 5.256  21.410  5.046   1.00 56.43  ? 507 LYS A CA    1 
ATOM   3913 C  C     . LYS A 1 507 ? 6.459  20.753  5.708   1.00 51.94  ? 507 LYS A C     1 
ATOM   3914 O  O     . LYS A 1 507 ? 6.578  19.529  5.755   1.00 56.13  ? 507 LYS A O     1 
ATOM   3915 C  CB    . LYS A 1 507 ? 4.017  20.530  5.162   1.00 55.44  ? 507 LYS A CB    1 
ATOM   3916 C  CG    . LYS A 1 507 ? 2.789  21.057  4.440   1.00 62.13  ? 507 LYS A CG    1 
ATOM   3917 C  CD    . LYS A 1 507 ? 2.211  22.267  5.146   1.00 67.97  ? 507 LYS A CD    1 
ATOM   3918 C  CE    . LYS A 1 507 ? 0.872  22.665  4.549   1.00 67.50  ? 507 LYS A CE    1 
ATOM   3919 N  NZ    . LYS A 1 507 ? 0.226  23.758  5.329   1.00 71.27  ? 507 LYS A NZ    1 
ATOM   3920 N  N     . LEU A 1 508 ? 7.362  21.571  6.229   1.00 49.27  ? 508 LEU A N     1 
ATOM   3921 C  CA    . LEU A 1 508 ? 8.583  21.036  6.822   1.00 51.40  ? 508 LEU A CA    1 
ATOM   3922 C  C     . LEU A 1 508 ? 8.271  20.350  8.149   1.00 50.07  ? 508 LEU A C     1 
ATOM   3923 O  O     . LEU A 1 508 ? 7.631  20.951  9.020   1.00 50.35  ? 508 LEU A O     1 
ATOM   3924 C  CB    . LEU A 1 508 ? 9.609  22.144  7.028   1.00 48.42  ? 508 LEU A CB    1 
ATOM   3925 C  CG    . LEU A 1 508 ? 10.129 22.823  5.760   1.00 50.03  ? 508 LEU A CG    1 
ATOM   3926 C  CD1   . LEU A 1 508 ? 11.103 23.921  6.135   1.00 48.46  ? 508 LEU A CD1   1 
ATOM   3927 C  CD2   . LEU A 1 508 ? 10.784 21.808  4.830   1.00 44.58  ? 508 LEU A CD2   1 
ATOM   3928 N  N     . PRO A 1 509 ? 8.696  19.106  8.342   1.00 47.00  ? 509 PRO A N     1 
ATOM   3929 C  CA    . PRO A 1 509 ? 8.415  18.419  9.606   1.00 43.96  ? 509 PRO A CA    1 
ATOM   3930 C  C     . PRO A 1 509 ? 9.208  19.017  10.758  1.00 43.60  ? 509 PRO A C     1 
ATOM   3931 O  O     . PRO A 1 509 ? 10.224 19.690  10.574  1.00 39.59  ? 509 PRO A O     1 
ATOM   3932 C  CB    . PRO A 1 509 ? 8.847  16.974  9.333   1.00 39.30  ? 509 PRO A CB    1 
ATOM   3933 C  CG    . PRO A 1 509 ? 8.942  16.866  7.829   1.00 43.31  ? 509 PRO A CG    1 
ATOM   3934 C  CD    . PRO A 1 509 ? 9.350  18.223  7.363   1.00 44.80  ? 509 PRO A CD    1 
ATOM   3935 N  N     . LYS A 1 510 ? 8.722  18.758  11.967  1.00 39.73  ? 510 LYS A N     1 
ATOM   3936 C  CA    . LYS A 1 510 ? 9.457  19.114  13.170  1.00 34.97  ? 510 LYS A CA    1 
ATOM   3937 C  C     . LYS A 1 510 ? 10.612 18.138  13.366  1.00 36.13  ? 510 LYS A C     1 
ATOM   3938 O  O     . LYS A 1 510 ? 10.545 16.977  12.951  1.00 36.23  ? 510 LYS A O     1 
ATOM   3939 C  CB    . LYS A 1 510 ? 8.523  19.102  14.383  1.00 36.58  ? 510 LYS A CB    1 
ATOM   3940 C  CG    . LYS A 1 510 ? 8.933  20.032  15.508  1.00 44.41  ? 510 LYS A CG    1 
ATOM   3941 C  CD    . LYS A 1 510 ? 7.781  20.242  16.483  1.00 44.65  ? 510 LYS A CD    1 
ATOM   3942 C  CE    . LYS A 1 510 ? 6.801  21.292  15.988  1.00 44.19  ? 510 LYS A CE    1 
ATOM   3943 N  NZ    . LYS A 1 510 ? 7.317  22.673  16.193  1.00 44.82  ? 510 LYS A NZ    1 
ATOM   3944 N  N     . ILE A 1 511 ? 11.690 18.620  13.982  1.00 35.20  ? 511 ILE A N     1 
ATOM   3945 C  CA    . ILE A 1 511 ? 12.901 17.827  14.172  1.00 31.36  ? 511 ILE A CA    1 
ATOM   3946 C  C     . ILE A 1 511 ? 13.211 17.739  15.660  1.00 34.93  ? 511 ILE A C     1 
ATOM   3947 O  O     . ILE A 1 511 ? 13.309 18.766  16.342  1.00 38.01  ? 511 ILE A O     1 
ATOM   3948 C  CB    . ILE A 1 511 ? 14.092 18.414  13.395  1.00 34.79  ? 511 ILE A CB    1 
ATOM   3949 C  CG1   . ILE A 1 511 ? 13.891 18.208  11.890  1.00 33.90  ? 511 ILE A CG1   1 
ATOM   3950 C  CG2   . ILE A 1 511 ? 15.398 17.788  13.861  1.00 28.81  ? 511 ILE A CG2   1 
ATOM   3951 C  CD1   . ILE A 1 511 ? 14.975 18.833  11.029  1.00 40.60  ? 511 ILE A CD1   1 
ATOM   3952 N  N     . PHE A 1 512 ? 13.367 16.513  16.153  1.00 31.07  ? 512 PHE A N     1 
ATOM   3953 C  CA    . PHE A 1 512 ? 13.657 16.235  17.550  1.00 33.41  ? 512 PHE A CA    1 
ATOM   3954 C  C     . PHE A 1 512 ? 14.964 15.462  17.668  1.00 32.34  ? 512 PHE A C     1 
ATOM   3955 O  O     . PHE A 1 512 ? 15.446 14.861  16.704  1.00 37.88  ? 512 PHE A O     1 
ATOM   3956 C  CB    . PHE A 1 512 ? 12.536 15.418  18.210  1.00 30.10  ? 512 PHE A CB    1 
ATOM   3957 C  CG    . PHE A 1 512 ? 11.174 16.038  18.098  1.00 32.70  ? 512 PHE A CG    1 
ATOM   3958 C  CD1   . PHE A 1 512 ? 10.724 16.928  19.059  1.00 30.61  ? 512 PHE A CD1   1 
ATOM   3959 C  CD2   . PHE A 1 512 ? 10.332 15.709  17.048  1.00 32.75  ? 512 PHE A CD2   1 
ATOM   3960 C  CE1   . PHE A 1 512 ? 9.467  17.496  18.966  1.00 32.80  ? 512 PHE A CE1   1 
ATOM   3961 C  CE2   . PHE A 1 512 ? 9.071  16.271  16.953  1.00 36.68  ? 512 PHE A CE2   1 
ATOM   3962 C  CZ    . PHE A 1 512 ? 8.639  17.167  17.914  1.00 32.17  ? 512 PHE A CZ    1 
ATOM   3963 N  N     . HIS A 1 513 ? 15.529 15.476  18.873  1.00 29.35  ? 513 HIS A N     1 
ATOM   3964 C  CA    . HIS A 1 513 ? 16.703 14.675  19.192  1.00 33.70  ? 513 HIS A CA    1 
ATOM   3965 C  C     . HIS A 1 513 ? 16.471 13.986  20.529  1.00 36.02  ? 513 HIS A C     1 
ATOM   3966 O  O     . HIS A 1 513 ? 16.103 14.643  21.508  1.00 29.82  ? 513 HIS A O     1 
ATOM   3967 C  CB    . HIS A 1 513 ? 17.967 15.540  19.241  1.00 32.19  ? 513 HIS A CB    1 
ATOM   3968 C  CG    . HIS A 1 513 ? 19.236 14.756  19.375  1.00 34.79  ? 513 HIS A CG    1 
ATOM   3969 N  ND1   . HIS A 1 513 ? 19.785 14.429  20.596  1.00 36.99  ? 513 HIS A ND1   1 
ATOM   3970 C  CD2   . HIS A 1 513 ? 20.067 14.238  18.439  1.00 36.68  ? 513 HIS A CD2   1 
ATOM   3971 C  CE1   . HIS A 1 513 ? 20.897 13.741  20.407  1.00 34.31  ? 513 HIS A CE1   1 
ATOM   3972 N  NE2   . HIS A 1 513 ? 21.092 13.614  19.108  1.00 37.45  ? 513 HIS A NE2   1 
ATOM   3973 N  N     . VAL A 1 514 ? 16.678 12.667  20.569  1.00 34.99  ? 514 VAL A N     1 
ATOM   3974 C  CA    . VAL A 1 514 ? 16.424 11.879  21.768  1.00 35.98  ? 514 VAL A CA    1 
ATOM   3975 C  C     . VAL A 1 514 ? 17.701 11.174  22.194  1.00 36.89  ? 514 VAL A C     1 
ATOM   3976 O  O     . VAL A 1 514 ? 18.656 11.028  21.426  1.00 38.80  ? 514 VAL A O     1 
ATOM   3977 C  CB    . VAL A 1 514 ? 15.293 10.847  21.577  1.00 33.83  ? 514 VAL A CB    1 
ATOM   3978 C  CG1   . VAL A 1 514 ? 13.985 11.545  21.292  1.00 31.11  ? 514 VAL A CG1   1 
ATOM   3979 C  CG2   . VAL A 1 514 ? 15.645 9.866   20.465  1.00 35.00  ? 514 VAL A CG2   1 
ATOM   3980 N  N     . ASN A 1 515 ? 17.699 10.728  23.448  1.00 32.30  ? 515 ASN A N     1 
ATOM   3981 C  CA    . ASN A 1 515 ? 18.807 9.957   24.002  1.00 39.66  ? 515 ASN A CA    1 
ATOM   3982 C  C     . ASN A 1 515 ? 18.208 8.984   25.013  1.00 39.99  ? 515 ASN A C     1 
ATOM   3983 O  O     . ASN A 1 515 ? 17.843 9.386   26.122  1.00 41.53  ? 515 ASN A O     1 
ATOM   3984 C  CB    . ASN A 1 515 ? 19.847 10.868  24.641  1.00 40.06  ? 515 ASN A CB    1 
ATOM   3985 C  CG    . ASN A 1 515 ? 21.004 10.098  25.250  1.00 42.13  ? 515 ASN A CG    1 
ATOM   3986 O  OD1   . ASN A 1 515 ? 21.259 8.949   24.891  1.00 44.30  ? 515 ASN A OD1   1 
ATOM   3987 N  ND2   . ASN A 1 515 ? 21.713 10.730  26.180  1.00 42.66  ? 515 ASN A ND2   1 
ATOM   3988 N  N     . TRP A 1 516 ? 18.095 7.715   24.624  1.00 42.09  ? 516 TRP A N     1 
ATOM   3989 C  CA    . TRP A 1 516 ? 17.607 6.710   25.557  1.00 42.72  ? 516 TRP A CA    1 
ATOM   3990 C  C     . TRP A 1 516 ? 18.680 6.222   26.516  1.00 42.54  ? 516 TRP A C     1 
ATOM   3991 O  O     . TRP A 1 516 ? 18.356 5.483   27.451  1.00 49.57  ? 516 TRP A O     1 
ATOM   3992 C  CB    . TRP A 1 516 ? 17.043 5.487   24.820  1.00 40.83  ? 516 TRP A CB    1 
ATOM   3993 C  CG    . TRP A 1 516 ? 16.075 5.748   23.692  1.00 41.97  ? 516 TRP A CG    1 
ATOM   3994 C  CD1   . TRP A 1 516 ? 16.012 5.066   22.513  1.00 42.23  ? 516 TRP A CD1   1 
ATOM   3995 C  CD2   . TRP A 1 516 ? 15.031 6.735   23.639  1.00 41.46  ? 516 TRP A CD2   1 
ATOM   3996 N  NE1   . TRP A 1 516 ? 15.001 5.563   21.729  1.00 42.33  ? 516 TRP A NE1   1 
ATOM   3997 C  CE2   . TRP A 1 516 ? 14.385 6.589   22.395  1.00 39.76  ? 516 TRP A CE2   1 
ATOM   3998 C  CE3   . TRP A 1 516 ? 14.581 7.727   24.518  1.00 42.03  ? 516 TRP A CE3   1 
ATOM   3999 C  CZ2   . TRP A 1 516 ? 13.316 7.397   22.008  1.00 39.15  ? 516 TRP A CZ2   1 
ATOM   4000 C  CZ3   . TRP A 1 516 ? 13.520 8.526   24.129  1.00 43.06  ? 516 TRP A CZ3   1 
ATOM   4001 C  CH2   . TRP A 1 516 ? 12.899 8.355   22.887  1.00 34.25  ? 516 TRP A CH2   1 
ATOM   4002 N  N     . PHE A 1 517 ? 19.937 6.619   26.321  1.00 41.63  ? 517 PHE A N     1 
ATOM   4003 C  CA    . PHE A 1 517 ? 21.064 5.904   26.906  1.00 48.14  ? 517 PHE A CA    1 
ATOM   4004 C  C     . PHE A 1 517 ? 21.873 6.752   27.880  1.00 44.81  ? 517 PHE A C     1 
ATOM   4005 O  O     . PHE A 1 517 ? 23.038 6.440   28.143  1.00 48.65  ? 517 PHE A O     1 
ATOM   4006 C  CB    . PHE A 1 517 ? 21.962 5.362   25.792  1.00 48.91  ? 517 PHE A CB    1 
ATOM   4007 C  CG    . PHE A 1 517 ? 21.224 4.539   24.772  1.00 50.46  ? 517 PHE A CG    1 
ATOM   4008 C  CD1   . PHE A 1 517 ? 21.010 3.181   24.979  1.00 53.03  ? 517 PHE A CD1   1 
ATOM   4009 C  CD2   . PHE A 1 517 ? 20.731 5.123   23.616  1.00 44.76  ? 517 PHE A CD2   1 
ATOM   4010 C  CE1   . PHE A 1 517 ? 20.326 2.418   24.045  1.00 45.11  ? 517 PHE A CE1   1 
ATOM   4011 C  CE2   . PHE A 1 517 ? 20.047 4.367   22.677  1.00 49.32  ? 517 PHE A CE2   1 
ATOM   4012 C  CZ    . PHE A 1 517 ? 19.842 3.011   22.894  1.00 47.61  ? 517 PHE A CZ    1 
ATOM   4013 N  N     . ARG A 1 518 ? 21.284 7.804   28.437  1.00 50.42  ? 518 ARG A N     1 
ATOM   4014 C  CA    . ARG A 1 518 ? 22.002 8.621   29.407  1.00 55.28  ? 518 ARG A CA    1 
ATOM   4015 C  C     . ARG A 1 518 ? 22.115 7.864   30.724  1.00 64.32  ? 518 ARG A C     1 
ATOM   4016 O  O     . ARG A 1 518 ? 21.101 7.476   31.316  1.00 64.19  ? 518 ARG A O     1 
ATOM   4017 C  CB    . ARG A 1 518 ? 21.303 9.963   29.610  1.00 53.37  ? 518 ARG A CB    1 
ATOM   4018 C  CG    . ARG A 1 518 ? 22.121 10.953  30.431  1.00 56.00  ? 518 ARG A CG    1 
ATOM   4019 C  CD    . ARG A 1 518 ? 21.479 12.330  30.458  1.00 52.03  ? 518 ARG A CD    1 
ATOM   4020 N  NE    . ARG A 1 518 ? 22.343 13.317  31.096  1.00 52.92  ? 518 ARG A NE    1 
ATOM   4021 C  CZ    . ARG A 1 518 ? 22.125 14.625  31.083  1.00 57.09  ? 518 ARG A CZ    1 
ATOM   4022 N  NH1   . ARG A 1 518 ? 21.066 15.144  30.483  1.00 55.19  ? 518 ARG A NH1   1 
ATOM   4023 N  NH2   . ARG A 1 518 ? 22.991 15.434  31.687  1.00 58.78  ? 518 ARG A NH2   1 
ATOM   4024 N  N     . LYS A 1 519 ? 23.344 7.646   31.176  1.00 69.80  ? 519 LYS A N     1 
ATOM   4025 C  CA    . LYS A 1 519 ? 23.608 6.900   32.395  1.00 74.22  ? 519 LYS A CA    1 
ATOM   4026 C  C     . LYS A 1 519 ? 23.985 7.844   33.531  1.00 84.41  ? 519 LYS A C     1 
ATOM   4027 O  O     . LYS A 1 519 ? 24.436 8.971   33.315  1.00 80.82  ? 519 LYS A O     1 
ATOM   4028 C  CB    . LYS A 1 519 ? 24.722 5.872   32.171  1.00 75.90  ? 519 LYS A CB    1 
ATOM   4029 C  CG    . LYS A 1 519 ? 24.380 4.797   31.147  1.00 70.66  ? 519 LYS A CG    1 
ATOM   4030 C  CD    . LYS A 1 519 ? 25.525 3.810   30.973  1.00 71.82  ? 519 LYS A CD    1 
ATOM   4031 C  CE    . LYS A 1 519 ? 25.161 2.701   29.997  1.00 68.97  ? 519 LYS A CE    1 
ATOM   4032 N  NZ    . LYS A 1 519 ? 26.279 1.734   29.813  1.00 69.99  ? 519 LYS A NZ    1 
ATOM   4033 N  N     . ASP A 1 520 ? 23.788 7.363   34.753  1.00 101.03 ? 520 ASP A N     1 
ATOM   4034 C  CA    . ASP A 1 520 ? 24.101 8.130   35.949  1.00 105.00 ? 520 ASP A CA    1 
ATOM   4035 C  C     . ASP A 1 520 ? 25.575 7.927   36.304  1.00 111.11 ? 520 ASP A C     1 
ATOM   4036 O  O     . ASP A 1 520 ? 26.367 7.454   35.484  1.00 111.31 ? 520 ASP A O     1 
ATOM   4037 C  CB    . ASP A 1 520 ? 23.160 7.723   37.087  1.00 108.40 ? 520 ASP A CB    1 
ATOM   4038 C  CG    . ASP A 1 520 ? 23.230 6.238   37.405  1.00 109.93 ? 520 ASP A CG    1 
ATOM   4039 O  OD1   . ASP A 1 520 ? 23.893 5.491   36.656  1.00 108.17 ? 520 ASP A OD1   1 
ATOM   4040 O  OD2   . ASP A 1 520 ? 22.619 5.817   38.410  1.00 111.98 ? 520 ASP A OD2   1 
ATOM   4041 N  N     . LYS A 1 521 ? 25.959 8.279   37.530  1.00 109.44 ? 521 LYS A N     1 
ATOM   4042 C  CA    . LYS A 1 521 ? 27.326 8.080   37.990  1.00 110.76 ? 521 LYS A CA    1 
ATOM   4043 C  C     . LYS A 1 521 ? 27.637 6.623   38.308  1.00 108.40 ? 521 LYS A C     1 
ATOM   4044 O  O     . LYS A 1 521 ? 28.814 6.274   38.440  1.00 109.45 ? 521 LYS A O     1 
ATOM   4045 C  CB    . LYS A 1 521 ? 27.590 8.945   39.225  1.00 112.64 ? 521 LYS A CB    1 
ATOM   4046 C  CG    . LYS A 1 521 ? 27.283 10.420  39.024  1.00 115.53 ? 521 LYS A CG    1 
ATOM   4047 C  CD    . LYS A 1 521 ? 27.492 11.208  40.308  1.00 119.25 ? 521 LYS A CD    1 
ATOM   4048 C  CE    . LYS A 1 521 ? 27.154 12.677  40.111  1.00 119.84 ? 521 LYS A CE    1 
ATOM   4049 N  NZ    . LYS A 1 521 ? 27.332 13.457  41.367  1.00 127.49 ? 521 LYS A NZ    1 
ATOM   4050 N  N     . ASN A 1 522 ? 26.620 5.770   38.429  1.00 105.90 ? 522 ASN A N     1 
ATOM   4051 C  CA    . ASN A 1 522 ? 26.819 4.365   38.757  1.00 107.43 ? 522 ASN A CA    1 
ATOM   4052 C  C     . ASN A 1 522 ? 26.803 3.455   37.537  1.00 100.99 ? 522 ASN A C     1 
ATOM   4053 O  O     . ASN A 1 522 ? 27.062 2.256   37.677  1.00 97.90  ? 522 ASN A O     1 
ATOM   4054 C  CB    . ASN A 1 522 ? 25.752 3.897   39.755  1.00 109.25 ? 522 ASN A CB    1 
ATOM   4055 C  CG    . ASN A 1 522 ? 25.816 4.649   41.073  1.00 110.10 ? 522 ASN A CG    1 
ATOM   4056 O  OD1   . ASN A 1 522 ? 26.880 5.117   41.483  1.00 108.84 ? 522 ASN A OD1   1 
ATOM   4057 N  ND2   . ASN A 1 522 ? 24.675 4.767   41.744  1.00 105.96 ? 522 ASN A ND2   1 
ATOM   4058 N  N     . GLY A 1 523 ? 26.503 3.984   36.357  1.00 98.67  ? 523 GLY A N     1 
ATOM   4059 C  CA    . GLY A 1 523 ? 26.558 3.211   35.136  1.00 93.57  ? 523 GLY A CA    1 
ATOM   4060 C  C     . GLY A 1 523 ? 25.256 2.594   34.680  1.00 90.25  ? 523 GLY A C     1 
ATOM   4061 O  O     . GLY A 1 523 ? 25.275 1.777   33.752  1.00 87.29  ? 523 GLY A O     1 
ATOM   4062 N  N     . LYS A 1 524 ? 24.130 2.952   35.291  1.00 89.10  ? 524 LYS A N     1 
ATOM   4063 C  CA    . LYS A 1 524 ? 22.833 2.429   34.892  1.00 85.69  ? 524 LYS A CA    1 
ATOM   4064 C  C     . LYS A 1 524 ? 22.013 3.516   34.209  1.00 80.26  ? 524 LYS A C     1 
ATOM   4065 O  O     . LYS A 1 524 ? 22.205 4.711   34.452  1.00 79.74  ? 524 LYS A O     1 
ATOM   4066 C  CB    . LYS A 1 524 ? 22.064 1.866   36.091  1.00 91.63  ? 524 LYS A CB    1 
ATOM   4067 C  CG    . LYS A 1 524 ? 21.656 2.895   37.130  1.00 90.90  ? 524 LYS A CG    1 
ATOM   4068 C  CD    . LYS A 1 524 ? 20.820 2.246   38.222  1.00 97.44  ? 524 LYS A CD    1 
ATOM   4069 C  CE    . LYS A 1 524 ? 20.324 3.267   39.231  1.00 95.61  ? 524 LYS A CE    1 
ATOM   4070 N  NZ    . LYS A 1 524 ? 19.433 2.637   40.245  1.00 93.71  ? 524 LYS A NZ    1 
ATOM   4071 N  N     . PHE A 1 525 ? 21.090 3.084   33.353  1.00 74.51  ? 525 PHE A N     1 
ATOM   4072 C  CA    . PHE A 1 525 ? 20.316 4.015   32.544  1.00 67.72  ? 525 PHE A CA    1 
ATOM   4073 C  C     . PHE A 1 525 ? 19.349 4.818   33.404  1.00 66.22  ? 525 PHE A C     1 
ATOM   4074 O  O     . PHE A 1 525 ? 18.716 4.289   34.322  1.00 75.03  ? 525 PHE A O     1 
ATOM   4075 C  CB    . PHE A 1 525 ? 19.547 3.258   31.461  1.00 64.07  ? 525 PHE A CB    1 
ATOM   4076 C  CG    . PHE A 1 525 ? 20.429 2.492   30.513  1.00 67.59  ? 525 PHE A CG    1 
ATOM   4077 C  CD1   . PHE A 1 525 ? 20.908 3.087   29.357  1.00 58.86  ? 525 PHE A CD1   1 
ATOM   4078 C  CD2   . PHE A 1 525 ? 20.776 1.176   30.777  1.00 63.34  ? 525 PHE A CD2   1 
ATOM   4079 C  CE1   . PHE A 1 525 ? 21.718 2.385   28.483  1.00 57.46  ? 525 PHE A CE1   1 
ATOM   4080 C  CE2   . PHE A 1 525 ? 21.586 0.471   29.907  1.00 59.58  ? 525 PHE A CE2   1 
ATOM   4081 C  CZ    . PHE A 1 525 ? 22.057 1.076   28.757  1.00 57.80  ? 525 PHE A CZ    1 
ATOM   4082 N  N     . LEU A 1 526 ? 19.238 6.112   33.099  1.00 67.52  ? 526 LEU A N     1 
ATOM   4083 C  CA    . LEU A 1 526 ? 18.282 6.977   33.777  1.00 65.86  ? 526 LEU A CA    1 
ATOM   4084 C  C     . LEU A 1 526 ? 16.866 6.821   33.241  1.00 61.92  ? 526 LEU A C     1 
ATOM   4085 O  O     . LEU A 1 526 ? 15.909 7.123   33.961  1.00 62.30  ? 526 LEU A O     1 
ATOM   4086 C  CB    . LEU A 1 526 ? 18.715 8.441   33.650  1.00 61.51  ? 526 LEU A CB    1 
ATOM   4087 C  CG    . LEU A 1 526 ? 20.008 8.845   34.360  1.00 72.61  ? 526 LEU A CG    1 
ATOM   4088 C  CD1   . LEU A 1 526 ? 20.417 10.258  33.965  1.00 75.20  ? 526 LEU A CD1   1 
ATOM   4089 C  CD2   . LEU A 1 526 ? 19.840 8.737   35.867  1.00 79.34  ? 526 LEU A CD2   1 
ATOM   4090 N  N     . TRP A 1 527 ? 16.711 6.358   32.003  1.00 61.57  ? 527 TRP A N     1 
ATOM   4091 C  CA    . TRP A 1 527 ? 15.419 6.203   31.364  1.00 55.22  ? 527 TRP A CA    1 
ATOM   4092 C  C     . TRP A 1 527 ? 15.162 4.728   31.077  1.00 60.64  ? 527 TRP A C     1 
ATOM   4093 O  O     . TRP A 1 527 ? 16.056 4.039   30.564  1.00 60.78  ? 527 TRP A O     1 
ATOM   4094 C  CB    . TRP A 1 527 ? 15.369 7.019   30.060  1.00 45.05  ? 527 TRP A CB    1 
ATOM   4095 C  CG    . TRP A 1 527 ? 14.042 7.021   29.371  1.00 44.37  ? 527 TRP A CG    1 
ATOM   4096 C  CD1   . TRP A 1 527 ? 13.743 6.446   28.170  1.00 48.59  ? 527 TRP A CD1   1 
ATOM   4097 C  CD2   . TRP A 1 527 ? 12.833 7.633   29.834  1.00 48.07  ? 527 TRP A CD2   1 
ATOM   4098 N  NE1   . TRP A 1 527 ? 12.423 6.660   27.857  1.00 45.96  ? 527 TRP A NE1   1 
ATOM   4099 C  CE2   . TRP A 1 527 ? 11.841 7.386   28.863  1.00 44.47  ? 527 TRP A CE2   1 
ATOM   4100 C  CE3   . TRP A 1 527 ? 12.490 8.363   30.978  1.00 49.75  ? 527 TRP A CE3   1 
ATOM   4101 C  CZ2   . TRP A 1 527 ? 10.530 7.842   29.000  1.00 47.74  ? 527 TRP A CZ2   1 
ATOM   4102 C  CZ3   . TRP A 1 527 ? 11.190 8.819   31.109  1.00 51.04  ? 527 TRP A CZ3   1 
ATOM   4103 C  CH2   . TRP A 1 527 ? 10.226 8.556   30.127  1.00 43.58  ? 527 TRP A CH2   1 
ATOM   4104 N  N     . PRO A 1 528 ? 13.978 4.199   31.404  1.00 60.38  ? 528 PRO A N     1 
ATOM   4105 C  CA    . PRO A 1 528 ? 13.737 2.769   31.146  1.00 57.58  ? 528 PRO A CA    1 
ATOM   4106 C  C     . PRO A 1 528 ? 13.689 2.423   29.667  1.00 57.27  ? 528 PRO A C     1 
ATOM   4107 O  O     . PRO A 1 528 ? 14.174 1.355   29.271  1.00 56.74  ? 528 PRO A O     1 
ATOM   4108 C  CB    . PRO A 1 528 ? 12.394 2.509   31.845  1.00 58.51  ? 528 PRO A CB    1 
ATOM   4109 C  CG    . PRO A 1 528 ? 11.740 3.848   31.931  1.00 57.10  ? 528 PRO A CG    1 
ATOM   4110 C  CD    . PRO A 1 528 ? 12.856 4.830   32.122  1.00 58.96  ? 528 PRO A CD    1 
ATOM   4111 N  N     . GLY A 1 529 ? 13.115 3.292   28.839  1.00 53.64  ? 529 GLY A N     1 
ATOM   4112 C  CA    . GLY A 1 529 ? 13.091 3.058   27.410  1.00 49.90  ? 529 GLY A CA    1 
ATOM   4113 C  C     . GLY A 1 529 ? 12.071 2.013   26.986  1.00 50.85  ? 529 GLY A C     1 
ATOM   4114 O  O     . GLY A 1 529 ? 11.149 1.646   27.726  1.00 50.89  ? 529 GLY A O     1 
ATOM   4115 N  N     . PHE A 1 530 ? 12.254 1.534   25.753  1.00 48.22  ? 530 PHE A N     1 
ATOM   4116 C  CA    . PHE A 1 530 ? 11.398 0.522   25.123  1.00 52.25  ? 530 PHE A CA    1 
ATOM   4117 C  C     . PHE A 1 530 ? 9.968  1.049   25.106  1.00 51.22  ? 530 PHE A C     1 
ATOM   4118 O  O     . PHE A 1 530 ? 9.741  2.134   24.543  1.00 51.26  ? 530 PHE A O     1 
ATOM   4119 C  CB    . PHE A 1 530 ? 11.611 -0.821  25.826  1.00 47.67  ? 530 PHE A CB    1 
ATOM   4120 C  CG    . PHE A 1 530 ? 13.013 -1.341  25.715  1.00 50.81  ? 530 PHE A CG    1 
ATOM   4121 C  CD1   . PHE A 1 530 ? 13.473 -1.876  24.522  1.00 50.30  ? 530 PHE A CD1   1 
ATOM   4122 C  CD2   . PHE A 1 530 ? 13.873 -1.290  26.798  1.00 51.47  ? 530 PHE A CD2   1 
ATOM   4123 C  CE1   . PHE A 1 530 ? 14.767 -2.356  24.412  1.00 48.99  ? 530 PHE A CE1   1 
ATOM   4124 C  CE2   . PHE A 1 530 ? 15.168 -1.766  26.694  1.00 53.91  ? 530 PHE A CE2   1 
ATOM   4125 C  CZ    . PHE A 1 530 ? 15.615 -2.301  25.498  1.00 49.44  ? 530 PHE A CZ    1 
ATOM   4126 N  N     . GLY A 1 531 ? 8.992  0.347   25.684  1.00 50.63  ? 531 GLY A N     1 
ATOM   4127 C  CA    . GLY A 1 531 ? 7.615  0.805   25.639  1.00 51.65  ? 531 GLY A CA    1 
ATOM   4128 C  C     . GLY A 1 531 ? 7.380  2.129   26.335  1.00 54.67  ? 531 GLY A C     1 
ATOM   4129 O  O     . GLY A 1 531 ? 6.398  2.816   26.027  1.00 51.88  ? 531 GLY A O     1 
ATOM   4130 N  N     . GLU A 1 532 ? 8.257  2.507   27.269  1.00 53.05  ? 532 GLU A N     1 
ATOM   4131 C  CA    . GLU A 1 532 ? 8.098  3.781   27.957  1.00 49.73  ? 532 GLU A CA    1 
ATOM   4132 C  C     . GLU A 1 532 ? 8.442  4.969   27.071  1.00 51.41  ? 532 GLU A C     1 
ATOM   4133 O  O     . GLU A 1 532 ? 8.090  6.102   27.418  1.00 52.67  ? 532 GLU A O     1 
ATOM   4134 C  CB    . GLU A 1 532 ? 8.954  3.809   29.224  1.00 51.48  ? 532 GLU A CB    1 
ATOM   4135 C  CG    . GLU A 1 532 ? 8.684  2.661   30.200  1.00 56.77  ? 532 GLU A CG    1 
ATOM   4136 C  CD    . GLU A 1 532 ? 7.294  2.702   30.824  1.00 55.50  ? 532 GLU A CD    1 
ATOM   4137 O  OE1   . GLU A 1 532 ? 6.562  3.694   30.628  1.00 60.84  ? 532 GLU A OE1   1 
ATOM   4138 O  OE2   . GLU A 1 532 ? 6.934  1.735   31.523  1.00 63.49  ? 532 GLU A OE2   1 
ATOM   4139 N  N     . ASN A 1 533 ? 9.105  4.744   25.936  1.00 46.63  ? 533 ASN A N     1 
ATOM   4140 C  CA    . ASN A 1 533 ? 9.371  5.824   24.997  1.00 49.75  ? 533 ASN A CA    1 
ATOM   4141 C  C     . ASN A 1 533 ? 8.099  6.393   24.388  1.00 49.60  ? 533 ASN A C     1 
ATOM   4142 O  O     . ASN A 1 533 ? 8.164  7.424   23.711  1.00 47.12  ? 533 ASN A O     1 
ATOM   4143 C  CB    . ASN A 1 533 ? 10.312 5.337   23.895  1.00 47.04  ? 533 ASN A CB    1 
ATOM   4144 C  CG    . ASN A 1 533 ? 11.693 5.004   24.422  1.00 46.39  ? 533 ASN A CG    1 
ATOM   4145 O  OD1   . ASN A 1 533 ? 12.123 5.546   25.442  1.00 43.99  ? 533 ASN A OD1   1 
ATOM   4146 N  ND2   . ASN A 1 533 ? 12.394 4.110   23.733  1.00 42.49  ? 533 ASN A ND2   1 
ATOM   4147 N  N     . SER A 1 534 ? 6.952  5.747   24.606  1.00 49.94  ? 534 SER A N     1 
ATOM   4148 C  CA    . SER A 1 534 ? 5.684  6.340   24.198  1.00 52.07  ? 534 SER A CA    1 
ATOM   4149 C  C     . SER A 1 534 ? 5.407  7.632   24.952  1.00 45.97  ? 534 SER A C     1 
ATOM   4150 O  O     . SER A 1 534 ? 4.684  8.498   24.450  1.00 46.79  ? 534 SER A O     1 
ATOM   4151 C  CB    . SER A 1 534 ? 4.546  5.345   24.416  1.00 48.90  ? 534 SER A CB    1 
ATOM   4152 O  OG    . SER A 1 534 ? 4.466  4.967   25.776  1.00 56.64  ? 534 SER A OG    1 
ATOM   4153 N  N     . ARG A 1 535 ? 5.964  7.780   26.158  1.00 50.43  ? 535 ARG A N     1 
ATOM   4154 C  CA    . ARG A 1 535 ? 5.822  9.037   26.887  1.00 50.05  ? 535 ARG A CA    1 
ATOM   4155 C  C     . ARG A 1 535 ? 6.547  10.169  26.170  1.00 50.08  ? 535 ARG A C     1 
ATOM   4156 O  O     . ARG A 1 535 ? 6.065  11.308  26.146  1.00 44.11  ? 535 ARG A O     1 
ATOM   4157 C  CB    . ARG A 1 535 ? 6.349  8.884   28.314  1.00 46.11  ? 535 ARG A CB    1 
ATOM   4158 C  CG    . ARG A 1 535 ? 5.748  7.725   29.081  1.00 49.27  ? 535 ARG A CG    1 
ATOM   4159 C  CD    . ARG A 1 535 ? 6.511  7.471   30.372  1.00 60.52  ? 535 ARG A CD    1 
ATOM   4160 N  NE    . ARG A 1 535 ? 6.075  6.251   31.043  1.00 57.53  ? 535 ARG A NE    1 
ATOM   4161 C  CZ    . ARG A 1 535 ? 5.134  6.201   31.976  1.00 64.29  ? 535 ARG A CZ    1 
ATOM   4162 N  NH1   . ARG A 1 535 ? 4.495  7.289   32.372  1.00 64.07  ? 535 ARG A NH1   1 
ATOM   4163 N  NH2   . ARG A 1 535 ? 4.828  5.030   32.527  1.00 61.22  ? 535 ARG A NH2   1 
ATOM   4164 N  N     . VAL A 1 536 ? 7.706  9.872   25.576  1.00 45.61  ? 536 VAL A N     1 
ATOM   4165 C  CA    . VAL A 1 536 ? 8.421  10.879  24.802  1.00 41.64  ? 536 VAL A CA    1 
ATOM   4166 C  C     . VAL A 1 536 ? 7.672  11.183  23.513  1.00 41.97  ? 536 VAL A C     1 
ATOM   4167 O  O     . VAL A 1 536 ? 7.561  12.343  23.103  1.00 45.58  ? 536 VAL A O     1 
ATOM   4168 C  CB    . VAL A 1 536 ? 9.865  10.417  24.528  1.00 44.40  ? 536 VAL A CB    1 
ATOM   4169 C  CG1   . VAL A 1 536 ? 10.572 11.389  23.595  1.00 40.74  ? 536 VAL A CG1   1 
ATOM   4170 C  CG2   . VAL A 1 536 ? 10.633 10.273  25.831  1.00 39.87  ? 536 VAL A CG2   1 
ATOM   4171 N  N     . LEU A 1 537 ? 7.142  10.150  22.854  1.00 47.35  ? 537 LEU A N     1 
ATOM   4172 C  CA    . LEU A 1 537 ? 6.402  10.378  21.618  1.00 45.36  ? 537 LEU A CA    1 
ATOM   4173 C  C     . LEU A 1 537 ? 5.137  11.189  21.864  1.00 41.37  ? 537 LEU A C     1 
ATOM   4174 O  O     . LEU A 1 537 ? 4.725  11.967  20.997  1.00 44.18  ? 537 LEU A O     1 
ATOM   4175 C  CB    . LEU A 1 537 ? 6.054  9.050   20.948  1.00 44.06  ? 537 LEU A CB    1 
ATOM   4176 C  CG    . LEU A 1 537 ? 7.181  8.152   20.426  1.00 46.85  ? 537 LEU A CG    1 
ATOM   4177 C  CD1   . LEU A 1 537 ? 6.599  7.137   19.458  1.00 50.90  ? 537 LEU A CD1   1 
ATOM   4178 C  CD2   . LEU A 1 537 ? 8.288  8.939   19.765  1.00 33.87  ? 537 LEU A CD2   1 
ATOM   4179 N  N     . GLU A 1 538 ? 4.515  11.031  23.036  1.00 42.21  ? 538 GLU A N     1 
ATOM   4180 C  CA    . GLU A 1 538 ? 3.333  11.827  23.358  1.00 44.49  ? 538 GLU A CA    1 
ATOM   4181 C  C     . GLU A 1 538 ? 3.653  13.315  23.358  1.00 40.48  ? 538 GLU A C     1 
ATOM   4182 O  O     . GLU A 1 538 ? 2.846  14.131  22.898  1.00 42.01  ? 538 GLU A O     1 
ATOM   4183 C  CB    . GLU A 1 538 ? 2.764  11.407  24.713  1.00 48.60  ? 538 GLU A CB    1 
ATOM   4184 C  CG    . GLU A 1 538 ? 1.624  12.294  25.209  1.00 47.20  ? 538 GLU A CG    1 
ATOM   4185 C  CD    . GLU A 1 538 ? 1.089  11.857  26.560  1.00 51.19  ? 538 GLU A CD    1 
ATOM   4186 O  OE1   . GLU A 1 538 ? 1.896  11.419  27.406  1.00 48.36  ? 538 GLU A OE1   1 
ATOM   4187 O  OE2   . GLU A 1 538 ? -0.138 11.944  26.772  1.00 54.47  ? 538 GLU A OE2   1 
ATOM   4188 N  N     . TRP A 1 539 ? 4.830  13.690  23.865  1.00 41.55  ? 539 TRP A N     1 
ATOM   4189 C  CA    . TRP A 1 539 ? 5.203  15.099  23.885  1.00 39.41  ? 539 TRP A CA    1 
ATOM   4190 C  C     . TRP A 1 539 ? 5.474  15.620  22.477  1.00 42.21  ? 539 TRP A C     1 
ATOM   4191 O  O     . TRP A 1 539 ? 5.092  16.749  22.148  1.00 39.80  ? 539 TRP A O     1 
ATOM   4192 C  CB    . TRP A 1 539 ? 6.419  15.311  24.784  1.00 42.83  ? 539 TRP A CB    1 
ATOM   4193 C  CG    . TRP A 1 539 ? 6.855  16.745  24.854  1.00 44.23  ? 539 TRP A CG    1 
ATOM   4194 C  CD1   . TRP A 1 539 ? 6.261  17.749  25.564  1.00 41.34  ? 539 TRP A CD1   1 
ATOM   4195 C  CD2   . TRP A 1 539 ? 7.979  17.335  24.188  1.00 43.99  ? 539 TRP A CD2   1 
ATOM   4196 N  NE1   . TRP A 1 539 ? 6.945  18.925  25.382  1.00 44.34  ? 539 TRP A NE1   1 
ATOM   4197 C  CE2   . TRP A 1 539 ? 8.004  18.700  24.542  1.00 43.06  ? 539 TRP A CE2   1 
ATOM   4198 C  CE3   . TRP A 1 539 ? 8.966  16.841  23.326  1.00 36.43  ? 539 TRP A CE3   1 
ATOM   4199 C  CZ2   . TRP A 1 539 ? 8.979  19.579  24.065  1.00 41.82  ? 539 TRP A CZ2   1 
ATOM   4200 C  CZ3   . TRP A 1 539 ? 9.931  17.713  22.854  1.00 39.84  ? 539 TRP A CZ3   1 
ATOM   4201 C  CH2   . TRP A 1 539 ? 9.930  19.069  23.224  1.00 41.35  ? 539 TRP A CH2   1 
ATOM   4202 N  N     . MET A 1 540 ? 6.126  14.814  21.632  1.00 39.00  ? 540 MET A N     1 
ATOM   4203 C  CA    . MET A 1 540 ? 6.338  15.219  20.245  1.00 37.36  ? 540 MET A CA    1 
ATOM   4204 C  C     . MET A 1 540 ? 5.012  15.407  19.523  1.00 41.07  ? 540 MET A C     1 
ATOM   4205 O  O     . MET A 1 540 ? 4.853  16.346  18.733  1.00 41.43  ? 540 MET A O     1 
ATOM   4206 C  CB    . MET A 1 540 ? 7.185  14.184  19.507  1.00 34.15  ? 540 MET A CB    1 
ATOM   4207 C  CG    . MET A 1 540 ? 8.598  14.009  20.015  1.00 34.66  ? 540 MET A CG    1 
ATOM   4208 S  SD    . MET A 1 540 ? 9.331  12.556  19.239  1.00 43.77  ? 540 MET A SD    1 
ATOM   4209 C  CE    . MET A 1 540 ? 10.974 12.589  19.932  1.00 37.30  ? 540 MET A CE    1 
ATOM   4210 N  N     . PHE A 1 541 ? 4.054  14.511  19.776  1.00 39.62  ? 541 PHE A N     1 
ATOM   4211 C  CA    . PHE A 1 541 ? 2.736  14.619  19.159  1.00 41.32  ? 541 PHE A CA    1 
ATOM   4212 C  C     . PHE A 1 541 ? 2.079  15.946  19.513  1.00 42.09  ? 541 PHE A C     1 
ATOM   4213 O  O     . PHE A 1 541 ? 1.566  16.651  18.637  1.00 44.55  ? 541 PHE A O     1 
ATOM   4214 C  CB    . PHE A 1 541 ? 1.864  13.442  19.603  1.00 42.78  ? 541 PHE A CB    1 
ATOM   4215 C  CG    . PHE A 1 541 ? 0.682  13.179  18.711  1.00 43.37  ? 541 PHE A CG    1 
ATOM   4216 C  CD1   . PHE A 1 541 ? -0.467 13.950  18.807  1.00 40.09  ? 541 PHE A CD1   1 
ATOM   4217 C  CD2   . PHE A 1 541 ? 0.710  12.139  17.793  1.00 47.37  ? 541 PHE A CD2   1 
ATOM   4218 C  CE1   . PHE A 1 541 ? -1.559 13.701  17.994  1.00 47.55  ? 541 PHE A CE1   1 
ATOM   4219 C  CE2   . PHE A 1 541 ? -0.378 11.883  16.976  1.00 48.10  ? 541 PHE A CE2   1 
ATOM   4220 C  CZ    . PHE A 1 541 ? -1.514 12.666  17.076  1.00 54.73  ? 541 PHE A CZ    1 
ATOM   4221 N  N     . GLY A 1 542 ? 2.096  16.309  20.799  1.00 35.25  ? 542 GLY A N     1 
ATOM   4222 C  CA    . GLY A 1 542 ? 1.498  17.567  21.211  1.00 44.60  ? 542 GLY A CA    1 
ATOM   4223 C  C     . GLY A 1 542 ? 2.214  18.774  20.636  1.00 45.11  ? 542 GLY A C     1 
ATOM   4224 O  O     . GLY A 1 542 ? 1.577  19.759  20.252  1.00 45.15  ? 542 GLY A O     1 
ATOM   4225 N  N     . ARG A 1 543 ? 3.547  18.712  20.560  1.00 40.01  ? 543 ARG A N     1 
ATOM   4226 C  CA    . ARG A 1 543 ? 4.308  19.814  19.983  1.00 41.79  ? 543 ARG A CA    1 
ATOM   4227 C  C     . ARG A 1 543 ? 3.986  19.995  18.506  1.00 43.11  ? 543 ARG A C     1 
ATOM   4228 O  O     . ARG A 1 543 ? 3.962  21.124  18.003  1.00 47.61  ? 543 ARG A O     1 
ATOM   4229 C  CB    . ARG A 1 543 ? 5.807  19.583  20.183  1.00 36.83  ? 543 ARG A CB    1 
ATOM   4230 C  CG    . ARG A 1 543 ? 6.282  19.840  21.606  1.00 46.66  ? 543 ARG A CG    1 
ATOM   4231 C  CD    . ARG A 1 543 ? 6.069  21.300  21.989  1.00 42.20  ? 543 ARG A CD    1 
ATOM   4232 N  NE    . ARG A 1 543 ? 6.727  22.195  21.047  1.00 37.33  ? 543 ARG A NE    1 
ATOM   4233 C  CZ    . ARG A 1 543 ? 6.547  23.507  21.002  1.00 46.41  ? 543 ARG A CZ    1 
ATOM   4234 N  NH1   . ARG A 1 543 ? 5.732  24.123  21.844  1.00 47.30  ? 543 ARG A NH1   1 
ATOM   4235 N  NH2   . ARG A 1 543 ? 7.204  24.221  20.090  1.00 45.54  ? 543 ARG A NH2   1 
ATOM   4236 N  N     . ILE A 1 544 ? 3.741  18.896  17.792  1.00 45.36  ? 544 ILE A N     1 
ATOM   4237 C  CA    . ILE A 1 544 ? 3.350  18.999  16.390  1.00 44.19  ? 544 ILE A CA    1 
ATOM   4238 C  C     . ILE A 1 544 ? 1.987  19.669  16.269  1.00 41.97  ? 544 ILE A C     1 
ATOM   4239 O  O     . ILE A 1 544 ? 1.757  20.484  15.367  1.00 48.52  ? 544 ILE A O     1 
ATOM   4240 C  CB    . ILE A 1 544 ? 3.373  17.608  15.727  1.00 44.05  ? 544 ILE A CB    1 
ATOM   4241 C  CG1   . ILE A 1 544 ? 4.814  17.107  15.593  1.00 38.72  ? 544 ILE A CG1   1 
ATOM   4242 C  CG2   . ILE A 1 544 ? 2.684  17.637  14.370  1.00 36.89  ? 544 ILE A CG2   1 
ATOM   4243 C  CD1   . ILE A 1 544 ? 4.930  15.680  15.075  1.00 35.71  ? 544 ILE A CD1   1 
ATOM   4244 N  N     . GLU A 1 545 ? 1.070  19.357  17.185  1.00 39.47  ? 545 GLU A N     1 
ATOM   4245 C  CA    . GLU A 1 545 ? -0.232 20.012  17.199  1.00 47.13  ? 545 GLU A CA    1 
ATOM   4246 C  C     . GLU A 1 545 ? -0.161 21.465  17.650  1.00 47.36  ? 545 GLU A C     1 
ATOM   4247 O  O     . GLU A 1 545 ? -1.166 22.174  17.546  1.00 46.03  ? 545 GLU A O     1 
ATOM   4248 C  CB    . GLU A 1 545 ? -1.202 19.248  18.102  1.00 43.75  ? 545 GLU A CB    1 
ATOM   4249 C  CG    . GLU A 1 545 ? -1.682 17.931  17.526  1.00 47.67  ? 545 GLU A CG    1 
ATOM   4250 C  CD    . GLU A 1 545 ? -2.750 17.288  18.383  1.00 53.82  ? 545 GLU A CD    1 
ATOM   4251 O  OE1   . GLU A 1 545 ? -2.738 17.503  19.613  1.00 60.40  ? 545 GLU A OE1   1 
ATOM   4252 O  OE2   . GLU A 1 545 ? -3.612 16.578  17.828  1.00 55.32  ? 545 GLU A OE2   1 
ATOM   4253 N  N     . GLY A 1 546 ? 0.984  21.918  18.151  1.00 43.07  ? 546 GLY A N     1 
ATOM   4254 C  CA    . GLY A 1 546 ? 1.129  23.294  18.570  1.00 44.62  ? 546 GLY A CA    1 
ATOM   4255 C  C     . GLY A 1 546 ? 0.845  23.555  20.029  1.00 50.51  ? 546 GLY A C     1 
ATOM   4256 O  O     . GLY A 1 546 ? 0.433  24.666  20.378  1.00 57.53  ? 546 GLY A O     1 
ATOM   4257 N  N     . GLU A 1 547 ? 1.049  22.570  20.897  1.00 50.64  ? 547 GLU A N     1 
ATOM   4258 C  CA    . GLU A 1 547 ? 0.812  22.763  22.318  1.00 51.36  ? 547 GLU A CA    1 
ATOM   4259 C  C     . GLU A 1 547 ? 1.937  23.574  22.951  1.00 52.34  ? 547 GLU A C     1 
ATOM   4260 O  O     . GLU A 1 547 ? 3.103  23.479  22.557  1.00 44.99  ? 547 GLU A O     1 
ATOM   4261 C  CB    . GLU A 1 547 ? 0.673  21.417  23.029  1.00 48.54  ? 547 GLU A CB    1 
ATOM   4262 C  CG    . GLU A 1 547 ? -0.527 20.611  22.576  1.00 53.93  ? 547 GLU A CG    1 
ATOM   4263 C  CD    . GLU A 1 547 ? -0.850 19.476  23.522  1.00 68.87  ? 547 GLU A CD    1 
ATOM   4264 O  OE1   . GLU A 1 547 ? -0.430 19.551  24.698  1.00 70.34  ? 547 GLU A OE1   1 
ATOM   4265 O  OE2   . GLU A 1 547 ? -1.520 18.509  23.092  1.00 69.87  ? 547 GLU A OE2   1 
ATOM   4266 N  N     . ASP A 1 548 ? 1.570  24.382  23.946  1.00 61.71  ? 548 ASP A N     1 
ATOM   4267 C  CA    . ASP A 1 548 ? 2.519  25.252  24.644  1.00 61.14  ? 548 ASP A CA    1 
ATOM   4268 C  C     . ASP A 1 548 ? 3.152  24.481  25.803  1.00 60.84  ? 548 ASP A C     1 
ATOM   4269 O  O     . ASP A 1 548 ? 2.949  24.771  26.984  1.00 60.65  ? 548 ASP A O     1 
ATOM   4270 C  CB    . ASP A 1 548 ? 1.820  26.519  25.122  1.00 65.59  ? 548 ASP A CB    1 
ATOM   4271 C  CG    . ASP A 1 548 ? 2.793  27.592  25.567  1.00 70.78  ? 548 ASP A CG    1 
ATOM   4272 O  OD1   . ASP A 1 548 ? 3.990  27.481  25.231  1.00 72.81  ? 548 ASP A OD1   1 
ATOM   4273 O  OD2   . ASP A 1 548 ? 2.362  28.544  26.252  1.00 76.42  ? 548 ASP A OD2   1 
ATOM   4274 N  N     . SER A 1 549 ? 3.942  23.472  25.435  1.00 52.14  ? 549 SER A N     1 
ATOM   4275 C  CA    . SER A 1 549 ? 4.547  22.567  26.404  1.00 51.60  ? 549 SER A CA    1 
ATOM   4276 C  C     . SER A 1 549 ? 6.068  22.597  26.373  1.00 47.72  ? 549 SER A C     1 
ATOM   4277 O  O     . SER A 1 549 ? 6.705  21.729  26.983  1.00 48.46  ? 549 SER A O     1 
ATOM   4278 C  CB    . SER A 1 549 ? 4.057  21.137  26.166  1.00 46.46  ? 549 SER A CB    1 
ATOM   4279 O  OG    . SER A 1 549 ? 4.474  20.677  24.892  1.00 47.57  ? 549 SER A OG    1 
ATOM   4280 N  N     . ALA A 1 550 ? 6.666  23.568  25.691  1.00 47.60  ? 550 ALA A N     1 
ATOM   4281 C  CA    . ALA A 1 550 ? 8.103  23.613  25.487  1.00 48.30  ? 550 ALA A CA    1 
ATOM   4282 C  C     . ALA A 1 550 ? 8.731  24.744  26.289  1.00 49.41  ? 550 ALA A C     1 
ATOM   4283 O  O     . ALA A 1 550 ? 8.120  25.793  26.504  1.00 42.06  ? 550 ALA A O     1 
ATOM   4284 C  CB    . ALA A 1 550 ? 8.442  23.788  24.004  1.00 46.25  ? 550 ALA A CB    1 
ATOM   4285 N  N     . LYS A 1 551 ? 9.966  24.514  26.720  1.00 49.81  ? 551 LYS A N     1 
ATOM   4286 C  CA    . LYS A 1 551 ? 10.791 25.516  27.377  1.00 47.04  ? 551 LYS A CA    1 
ATOM   4287 C  C     . LYS A 1 551 ? 12.066 25.700  26.566  1.00 48.55  ? 551 LYS A C     1 
ATOM   4288 O  O     . LYS A 1 551 ? 12.695 24.716  26.160  1.00 47.08  ? 551 LYS A O     1 
ATOM   4289 C  CB    . LYS A 1 551 ? 11.115 25.095  28.811  1.00 45.79  ? 551 LYS A CB    1 
ATOM   4290 C  CG    . LYS A 1 551 ? 12.085 26.000  29.529  1.00 51.79  ? 551 LYS A CG    1 
ATOM   4291 C  CD    . LYS A 1 551 ? 12.318 25.517  30.953  1.00 64.60  ? 551 LYS A CD    1 
ATOM   4292 C  CE    . LYS A 1 551 ? 12.903 24.113  30.967  1.00 64.88  ? 551 LYS A CE    1 
ATOM   4293 N  NZ    . LYS A 1 551 ? 13.176 23.636  32.349  1.00 79.79  ? 551 LYS A NZ    1 
ATOM   4294 N  N     . LEU A 1 552 ? 12.439 26.956  26.324  1.00 44.99  ? 552 LEU A N     1 
ATOM   4295 C  CA    . LEU A 1 552 ? 13.597 27.263  25.494  1.00 46.92  ? 552 LEU A CA    1 
ATOM   4296 C  C     . LEU A 1 552 ? 14.887 27.102  26.289  1.00 48.65  ? 552 LEU A C     1 
ATOM   4297 O  O     . LEU A 1 552 ? 15.010 27.619  27.403  1.00 47.05  ? 552 LEU A O     1 
ATOM   4298 C  CB    . LEU A 1 552 ? 13.490 28.687  24.945  1.00 45.19  ? 552 LEU A CB    1 
ATOM   4299 C  CG    . LEU A 1 552 ? 14.631 29.159  24.045  1.00 48.70  ? 552 LEU A CG    1 
ATOM   4300 C  CD1   . LEU A 1 552 ? 14.858 28.160  22.913  1.00 48.73  ? 552 LEU A CD1   1 
ATOM   4301 C  CD2   . LEU A 1 552 ? 14.349 30.542  23.488  1.00 43.85  ? 552 LEU A CD2   1 
ATOM   4302 N  N     . THR A 1 553 ? 15.850 26.390  25.715  1.00 46.72  ? 553 THR A N     1 
ATOM   4303 C  CA    . THR A 1 553 ? 17.165 26.186  26.296  1.00 43.93  ? 553 THR A CA    1 
ATOM   4304 C  C     . THR A 1 553 ? 18.222 26.563  25.272  1.00 42.43  ? 553 THR A C     1 
ATOM   4305 O  O     . THR A 1 553 ? 17.905 26.801  24.102  1.00 39.58  ? 553 THR A O     1 
ATOM   4306 C  CB    . THR A 1 553 ? 17.351 24.725  26.748  1.00 41.78  ? 553 THR A CB    1 
ATOM   4307 O  OG1   . THR A 1 553 ? 17.296 23.849  25.616  1.00 42.23  ? 553 THR A OG1   1 
ATOM   4308 C  CG2   . THR A 1 553 ? 16.274 24.338  27.743  1.00 41.68  ? 553 THR A CG2   1 
ATOM   4309 N  N     . PRO A 1 554 ? 19.491 26.658  25.682  1.00 41.46  ? 554 PRO A N     1 
ATOM   4310 C  CA    . PRO A 1 554 ? 20.553 26.947  24.703  1.00 40.89  ? 554 PRO A CA    1 
ATOM   4311 C  C     . PRO A 1 554 ? 20.706 25.894  23.613  1.00 47.23  ? 554 PRO A C     1 
ATOM   4312 O  O     . PRO A 1 554 ? 21.304 26.192  22.570  1.00 45.12  ? 554 PRO A O     1 
ATOM   4313 C  CB    . PRO A 1 554 ? 21.814 27.033  25.571  1.00 43.46  ? 554 PRO A CB    1 
ATOM   4314 C  CG    . PRO A 1 554 ? 21.315 27.455  26.902  1.00 45.01  ? 554 PRO A CG    1 
ATOM   4315 C  CD    . PRO A 1 554 ? 19.981 26.791  27.068  1.00 43.86  ? 554 PRO A CD    1 
ATOM   4316 N  N     . ILE A 1 555 ? 20.196 24.675  23.810  1.00 40.10  ? 555 ILE A N     1 
ATOM   4317 C  CA    . ILE A 1 555 ? 20.308 23.635  22.790  1.00 40.66  ? 555 ILE A CA    1 
ATOM   4318 C  C     . ILE A 1 555 ? 19.011 23.417  22.024  1.00 41.47  ? 555 ILE A C     1 
ATOM   4319 O  O     . ILE A 1 555 ? 19.003 22.644  21.053  1.00 42.36  ? 555 ILE A O     1 
ATOM   4320 C  CB    . ILE A 1 555 ? 20.772 22.293  23.396  1.00 37.91  ? 555 ILE A CB    1 
ATOM   4321 C  CG1   . ILE A 1 555 ? 19.719 21.757  24.372  1.00 41.88  ? 555 ILE A CG1   1 
ATOM   4322 C  CG2   . ILE A 1 555 ? 22.118 22.453  24.086  1.00 40.37  ? 555 ILE A CG2   1 
ATOM   4323 C  CD1   . ILE A 1 555 ? 20.036 20.381  24.910  1.00 41.04  ? 555 ILE A CD1   1 
ATOM   4324 N  N     . GLY A 1 556 ? 17.923 24.065  22.419  1.00 43.39  ? 556 GLY A N     1 
ATOM   4325 C  CA    . GLY A 1 556 ? 16.642 23.898  21.773  1.00 43.12  ? 556 GLY A CA    1 
ATOM   4326 C  C     . GLY A 1 556 ? 15.534 23.811  22.799  1.00 42.79  ? 556 GLY A C     1 
ATOM   4327 O  O     . GLY A 1 556 ? 15.748 23.992  23.996  1.00 43.06  ? 556 GLY A O     1 
ATOM   4328 N  N     . TYR A 1 557 ? 14.327 23.529  22.319  1.00 42.69  ? 557 TYR A N     1 
ATOM   4329 C  CA    . TYR A 1 557 ? 13.170 23.428  23.197  1.00 40.60  ? 557 TYR A CA    1 
ATOM   4330 C  C     . TYR A 1 557 ? 13.171 22.086  23.919  1.00 43.99  ? 557 TYR A C     1 
ATOM   4331 O  O     . TYR A 1 557 ? 13.342 21.035  23.295  1.00 43.21  ? 557 TYR A O     1 
ATOM   4332 C  CB    . TYR A 1 557 ? 11.875 23.590  22.402  1.00 38.85  ? 557 TYR A CB    1 
ATOM   4333 C  CG    . TYR A 1 557 ? 11.708 24.933  21.735  1.00 44.74  ? 557 TYR A CG    1 
ATOM   4334 C  CD1   . TYR A 1 557 ? 11.437 26.072  22.479  1.00 45.71  ? 557 TYR A CD1   1 
ATOM   4335 C  CD2   . TYR A 1 557 ? 11.802 25.059  20.354  1.00 48.01  ? 557 TYR A CD2   1 
ATOM   4336 C  CE1   . TYR A 1 557 ? 11.277 27.302  21.870  1.00 46.50  ? 557 TYR A CE1   1 
ATOM   4337 C  CE2   . TYR A 1 557 ? 11.641 26.284  19.736  1.00 46.57  ? 557 TYR A CE2   1 
ATOM   4338 C  CZ    . TYR A 1 557 ? 11.379 27.403  20.501  1.00 50.55  ? 557 TYR A CZ    1 
ATOM   4339 O  OH    . TYR A 1 557 ? 11.221 28.625  19.887  1.00 52.19  ? 557 TYR A OH    1 
ATOM   4340 N  N     . VAL A 1 558 ? 12.980 22.127  25.230  1.00 43.87  ? 558 VAL A N     1 
ATOM   4341 C  CA    . VAL A 1 558 ? 12.804 20.927  26.043  1.00 45.32  ? 558 VAL A CA    1 
ATOM   4342 C  C     . VAL A 1 558 ? 11.408 20.989  26.644  1.00 45.42  ? 558 VAL A C     1 
ATOM   4343 O  O     . VAL A 1 558 ? 10.793 22.069  26.702  1.00 45.90  ? 558 VAL A O     1 
ATOM   4344 C  CB    . VAL A 1 558 ? 13.892 20.808  27.136  1.00 40.69  ? 558 VAL A CB    1 
ATOM   4345 C  CG1   . VAL A 1 558 ? 15.278 20.868  26.520  1.00 38.87  ? 558 VAL A CG1   1 
ATOM   4346 C  CG2   . VAL A 1 558 ? 13.711 21.899  28.179  1.00 46.13  ? 558 VAL A CG2   1 
ATOM   4347 N  N     . PRO A 1 559 ? 10.862 19.856  27.089  1.00 46.53  ? 559 PRO A N     1 
ATOM   4348 C  CA    . PRO A 1 559 ? 9.532  19.887  27.707  1.00 44.43  ? 559 PRO A CA    1 
ATOM   4349 C  C     . PRO A 1 559 ? 9.541  20.702  28.990  1.00 47.46  ? 559 PRO A C     1 
ATOM   4350 O  O     . PRO A 1 559 ? 10.524 20.718  29.735  1.00 52.21  ? 559 PRO A O     1 
ATOM   4351 C  CB    . PRO A 1 559 ? 9.230  18.410  27.988  1.00 44.26  ? 559 PRO A CB    1 
ATOM   4352 C  CG    . PRO A 1 559 ? 10.130 17.651  27.080  1.00 41.29  ? 559 PRO A CG    1 
ATOM   4353 C  CD    . PRO A 1 559 ? 11.369 18.478  26.957  1.00 42.05  ? 559 PRO A CD    1 
ATOM   4354 N  N     . LYS A 1 560 ? 8.426  21.384  29.239  1.00 48.20  ? 560 LYS A N     1 
ATOM   4355 C  CA    . LYS A 1 560 ? 8.251  22.129  30.476  1.00 58.36  ? 560 LYS A CA    1 
ATOM   4356 C  C     . LYS A 1 560 ? 8.233  21.182  31.675  1.00 66.18  ? 560 LYS A C     1 
ATOM   4357 O  O     . LYS A 1 560 ? 8.244  19.955  31.541  1.00 63.52  ? 560 LYS A O     1 
ATOM   4358 C  CB    . LYS A 1 560 ? 6.952  22.934  30.442  1.00 58.90  ? 560 LYS A CB    1 
ATOM   4359 C  CG    . LYS A 1 560 ? 6.927  24.082  29.451  1.00 52.47  ? 560 LYS A CG    1 
ATOM   4360 C  CD    . LYS A 1 560 ? 5.577  24.777  29.492  1.00 50.96  ? 560 LYS A CD    1 
ATOM   4361 C  CE    . LYS A 1 560 ? 5.548  25.989  28.586  1.00 58.66  ? 560 LYS A CE    1 
ATOM   4362 N  NZ    . LYS A 1 560 ? 4.237  26.693  28.646  1.00 54.70  ? 560 LYS A NZ    1 
ATOM   4363 N  N     . GLU A 1 561 ? 8.196  21.773  32.867  1.00 80.73  ? 561 GLU A N     1 
ATOM   4364 C  CA    . GLU A 1 561 ? 8.042  20.983  34.079  1.00 85.21  ? 561 GLU A CA    1 
ATOM   4365 C  C     . GLU A 1 561 ? 6.664  20.336  34.096  1.00 84.52  ? 561 GLU A C     1 
ATOM   4366 O  O     . GLU A 1 561 ? 5.658  20.985  33.791  1.00 87.42  ? 561 GLU A O     1 
ATOM   4367 C  CB    . GLU A 1 561 ? 8.238  21.855  35.318  1.00 95.08  ? 561 GLU A CB    1 
ATOM   4368 C  CG    . GLU A 1 561 ? 9.636  22.437  35.459  1.00 105.38 ? 561 GLU A CG    1 
ATOM   4369 C  CD    . GLU A 1 561 ? 9.840  23.152  36.783  1.00 120.89 ? 561 GLU A CD    1 
ATOM   4370 O  OE1   . GLU A 1 561 ? 8.957  23.046  37.661  1.00 118.73 ? 561 GLU A OE1   1 
ATOM   4371 O  OE2   . GLU A 1 561 ? 10.884 23.820  36.945  1.00 125.19 ? 561 GLU A OE2   1 
ATOM   4372 N  N     . ASP A 1 562 ? 6.624  19.048  34.435  1.00 67.11  ? 562 ASP A N     1 
ATOM   4373 C  CA    . ASP A 1 562 ? 5.396  18.255  34.454  1.00 72.69  ? 562 ASP A CA    1 
ATOM   4374 C  C     . ASP A 1 562 ? 4.719  18.202  33.088  1.00 68.52  ? 562 ASP A C     1 
ATOM   4375 O  O     . ASP A 1 562 ? 3.524  17.908  32.995  1.00 68.09  ? 562 ASP A O     1 
ATOM   4376 C  CB    . ASP A 1 562 ? 4.412  18.769  35.513  1.00 81.44  ? 562 ASP A CB    1 
ATOM   4377 C  CG    . ASP A 1 562 ? 4.930  18.587  36.927  1.00 85.53  ? 562 ASP A CG    1 
ATOM   4378 O  OD1   . ASP A 1 562 ? 5.663  17.603  37.169  1.00 83.64  ? 562 ASP A OD1   1 
ATOM   4379 O  OD2   . ASP A 1 562 ? 4.606  19.428  37.794  1.00 87.71  ? 562 ASP A OD2   1 
ATOM   4380 N  N     . ALA A 1 563 ? 5.465  18.481  32.018  1.00 70.11  ? 563 ALA A N     1 
ATOM   4381 C  CA    . ALA A 1 563 ? 4.909  18.355  30.678  1.00 61.59  ? 563 ALA A CA    1 
ATOM   4382 C  C     . ALA A 1 563 ? 4.919  16.910  30.198  1.00 54.12  ? 563 ALA A C     1 
ATOM   4383 O  O     . ALA A 1 563 ? 4.012  16.499  29.468  1.00 47.61  ? 563 ALA A O     1 
ATOM   4384 C  CB    . ALA A 1 563 ? 5.675  19.249  29.702  1.00 54.51  ? 563 ALA A CB    1 
ATOM   4385 N  N     . LEU A 1 564 ? 5.920  16.130  30.598  1.00 52.59  ? 564 LEU A N     1 
ATOM   4386 C  CA    . LEU A 1 564 ? 5.933  14.705  30.303  1.00 52.22  ? 564 LEU A CA    1 
ATOM   4387 C  C     . LEU A 1 564 ? 5.007  13.951  31.247  1.00 52.38  ? 564 LEU A C     1 
ATOM   4388 O  O     . LEU A 1 564 ? 4.861  14.299  32.423  1.00 58.46  ? 564 LEU A O     1 
ATOM   4389 C  CB    . LEU A 1 564 ? 7.346  14.132  30.424  1.00 53.23  ? 564 LEU A CB    1 
ATOM   4390 C  CG    . LEU A 1 564 ? 8.365  14.469  29.336  1.00 54.06  ? 564 LEU A CG    1 
ATOM   4391 C  CD1   . LEU A 1 564 ? 9.683  13.768  29.623  1.00 54.86  ? 564 LEU A CD1   1 
ATOM   4392 C  CD2   . LEU A 1 564 ? 7.831  14.076  27.973  1.00 51.85  ? 564 LEU A CD2   1 
ATOM   4393 N  N     . ASN A 1 565 ? 4.380  12.904  30.718  1.00 57.32  ? 565 ASN A N     1 
ATOM   4394 C  CA    . ASN A 1 565 ? 3.591  11.981  31.527  1.00 56.84  ? 565 ASN A CA    1 
ATOM   4395 C  C     . ASN A 1 565 ? 4.543  11.002  32.204  1.00 56.38  ? 565 ASN A C     1 
ATOM   4396 O  O     . ASN A 1 565 ? 5.134  10.141  31.545  1.00 52.91  ? 565 ASN A O     1 
ATOM   4397 C  CB    . ASN A 1 565 ? 2.570  11.247  30.660  1.00 56.77  ? 565 ASN A CB    1 
ATOM   4398 C  CG    . ASN A 1 565 ? 1.564  10.452  31.475  1.00 64.12  ? 565 ASN A CG    1 
ATOM   4399 O  OD1   . ASN A 1 565 ? 1.769  10.187  32.660  1.00 65.45  ? 565 ASN A OD1   1 
ATOM   4400 N  ND2   . ASN A 1 565 ? 0.468  10.060  30.836  1.00 66.24  ? 565 ASN A ND2   1 
ATOM   4401 N  N     . LEU A 1 566 ? 4.697  11.133  33.522  1.00 60.99  ? 566 LEU A N     1 
ATOM   4402 C  CA    . LEU A 1 566 ? 5.537  10.231  34.302  1.00 67.42  ? 566 LEU A CA    1 
ATOM   4403 C  C     . LEU A 1 566 ? 4.725  9.408   35.297  1.00 77.63  ? 566 LEU A C     1 
ATOM   4404 O  O     . LEU A 1 566 ? 5.270  8.950   36.308  1.00 84.43  ? 566 LEU A O     1 
ATOM   4405 C  CB    . LEU A 1 566 ? 6.631  11.013  35.029  1.00 66.13  ? 566 LEU A CB    1 
ATOM   4406 C  CG    . LEU A 1 566 ? 7.562  11.825  34.132  1.00 60.59  ? 566 LEU A CG    1 
ATOM   4407 C  CD1   . LEU A 1 566 ? 8.597  12.557  34.968  1.00 63.14  ? 566 LEU A CD1   1 
ATOM   4408 C  CD2   . LEU A 1 566 ? 8.231  10.925  33.111  1.00 56.72  ? 566 LEU A CD2   1 
ATOM   4409 N  N     . LYS A 1 567 ? 3.433  9.217   35.038  1.00 75.19  ? 567 LYS A N     1 
ATOM   4410 C  CA    . LYS A 1 567 ? 2.614  8.377   35.901  1.00 77.59  ? 567 LYS A CA    1 
ATOM   4411 C  C     . LYS A 1 567 ? 3.109  6.938   35.845  1.00 79.79  ? 567 LYS A C     1 
ATOM   4412 O  O     . LYS A 1 567 ? 3.370  6.402   34.764  1.00 75.22  ? 567 LYS A O     1 
ATOM   4413 C  CB    . LYS A 1 567 ? 1.147  8.452   35.482  1.00 79.21  ? 567 LYS A CB    1 
ATOM   4414 C  CG    . LYS A 1 567 ? 0.526  9.830   35.638  1.00 87.81  ? 567 LYS A CG    1 
ATOM   4415 C  CD    . LYS A 1 567 ? -0.952 9.819   35.276  1.00 93.67  ? 567 LYS A CD    1 
ATOM   4416 C  CE    . LYS A 1 567 ? -1.575 11.193  35.467  1.00 98.66  ? 567 LYS A CE    1 
ATOM   4417 N  NZ    . LYS A 1 567 ? -3.035 11.196  35.172  1.00 96.74  ? 567 LYS A NZ    1 
ATOM   4418 N  N     . GLY A 1 568 ? 3.238  6.314   37.016  1.00 85.06  ? 568 GLY A N     1 
ATOM   4419 C  CA    . GLY A 1 568 ? 3.802  4.989   37.125  1.00 84.24  ? 568 GLY A CA    1 
ATOM   4420 C  C     . GLY A 1 568 ? 5.311  4.944   37.190  1.00 94.46  ? 568 GLY A C     1 
ATOM   4421 O  O     . GLY A 1 568 ? 5.869  3.937   37.641  1.00 95.00  ? 568 GLY A O     1 
ATOM   4422 N  N     . LEU A 1 569 ? 5.992  6.002   36.754  1.00 110.32 ? 569 LEU A N     1 
ATOM   4423 C  CA    . LEU A 1 569 ? 7.445  6.064   36.820  1.00 113.61 ? 569 LEU A CA    1 
ATOM   4424 C  C     . LEU A 1 569 ? 7.879  7.227   37.701  1.00 116.90 ? 569 LEU A C     1 
ATOM   4425 O  O     . LEU A 1 569 ? 8.652  8.088   37.266  1.00 117.78 ? 569 LEU A O     1 
ATOM   4426 C  CB    . LEU A 1 569 ? 8.046  6.202   35.419  1.00 106.21 ? 569 LEU A CB    1 
ATOM   4427 C  CG    . LEU A 1 569 ? 7.771  5.071   34.426  1.00 105.08 ? 569 LEU A CG    1 
ATOM   4428 C  CD1   . LEU A 1 569 ? 8.495  5.332   33.120  1.00 101.74 ? 569 LEU A CD1   1 
ATOM   4429 C  CD2   . LEU A 1 569 ? 8.179  3.728   35.011  1.00 107.77 ? 569 LEU A CD2   1 
ATOM   4430 N  N     . GLY A 1 570 ? 7.381  7.267   38.937  1.00 102.30 ? 570 GLY A N     1 
ATOM   4431 C  CA    . GLY A 1 570 ? 7.762  8.321   39.858  1.00 102.84 ? 570 GLY A CA    1 
ATOM   4432 C  C     . GLY A 1 570 ? 9.200  8.256   40.327  1.00 107.92 ? 570 GLY A C     1 
ATOM   4433 O  O     . GLY A 1 570 ? 9.675  9.213   40.950  1.00 103.05 ? 570 GLY A O     1 
ATOM   4434 N  N     . ASP A 1 571 ? 9.901  7.163   40.037  1.00 114.96 ? 571 ASP A N     1 
ATOM   4435 C  CA    . ASP A 1 571 ? 11.274 6.958   40.471  1.00 115.23 ? 571 ASP A CA    1 
ATOM   4436 C  C     . ASP A 1 571 ? 12.302 7.508   39.488  1.00 112.84 ? 571 ASP A C     1 
ATOM   4437 O  O     . ASP A 1 571 ? 13.502 7.281   39.675  1.00 112.79 ? 571 ASP A O     1 
ATOM   4438 C  CB    . ASP A 1 571 ? 11.526 5.467   40.701  1.00 117.24 ? 571 ASP A CB    1 
ATOM   4439 C  CG    . ASP A 1 571 ? 11.133 4.621   39.505  1.00 117.71 ? 571 ASP A CG    1 
ATOM   4440 O  OD1   . ASP A 1 571 ? 10.171 4.995   38.800  1.00 112.32 ? 571 ASP A OD1   1 
ATOM   4441 O  OD2   . ASP A 1 571 ? 11.786 3.583   39.268  1.00 127.53 ? 571 ASP A OD2   1 
ATOM   4442 N  N     . VAL A 1 572 ? 11.866 8.220   38.454  1.00 105.16 ? 572 VAL A N     1 
ATOM   4443 C  CA    . VAL A 1 572 ? 12.782 8.737   37.442  1.00 92.22  ? 572 VAL A CA    1 
ATOM   4444 C  C     . VAL A 1 572 ? 13.374 10.053  37.926  1.00 89.42  ? 572 VAL A C     1 
ATOM   4445 O  O     . VAL A 1 572 ? 12.643 10.982  38.290  1.00 88.31  ? 572 VAL A O     1 
ATOM   4446 C  CB    . VAL A 1 572 ? 12.061 8.917   36.098  1.00 88.96  ? 572 VAL A CB    1 
ATOM   4447 C  CG1   . VAL A 1 572 ? 13.007 9.508   35.066  1.00 80.37  ? 572 VAL A CG1   1 
ATOM   4448 C  CG2   . VAL A 1 572 ? 11.502 7.588   35.617  1.00 96.99  ? 572 VAL A CG2   1 
ATOM   4449 N  N     . ASN A 1 573 ? 14.702 10.137  37.928  1.00 85.45  ? 573 ASN A N     1 
ATOM   4450 C  CA    . ASN A 1 573 ? 15.394 11.366  38.301  1.00 83.16  ? 573 ASN A CA    1 
ATOM   4451 C  C     . ASN A 1 573 ? 15.343 12.329  37.122  1.00 82.02  ? 573 ASN A C     1 
ATOM   4452 O  O     . ASN A 1 573 ? 16.048 12.139  36.125  1.00 83.91  ? 573 ASN A O     1 
ATOM   4453 C  CB    . ASN A 1 573 ? 16.833 11.067  38.710  1.00 86.73  ? 573 ASN A CB    1 
ATOM   4454 C  CG    . ASN A 1 573 ? 17.609 12.319  39.070  1.00 89.20  ? 573 ASN A CG    1 
ATOM   4455 O  OD1   . ASN A 1 573 ? 17.026 13.372  39.335  1.00 88.84  ? 573 ASN A OD1   1 
ATOM   4456 N  ND2   . ASN A 1 573 ? 18.932 12.210  39.084  1.00 92.11  ? 573 ASN A ND2   1 
ATOM   4457 N  N     . VAL A 1 574 ? 14.513 13.368  37.235  1.00 85.16  ? 574 VAL A N     1 
ATOM   4458 C  CA    . VAL A 1 574 ? 14.319 14.288  36.118  1.00 82.82  ? 574 VAL A CA    1 
ATOM   4459 C  C     . VAL A 1 574 ? 15.395 15.364  36.052  1.00 78.42  ? 574 VAL A C     1 
ATOM   4460 O  O     . VAL A 1 574 ? 15.592 15.964  34.988  1.00 70.67  ? 574 VAL A O     1 
ATOM   4461 C  CB    . VAL A 1 574 ? 12.931 14.945  36.192  1.00 75.72  ? 574 VAL A CB    1 
ATOM   4462 C  CG1   . VAL A 1 574 ? 11.844 13.898  36.020  1.00 76.94  ? 574 VAL A CG1   1 
ATOM   4463 C  CG2   . VAL A 1 574 ? 12.763 15.681  37.513  1.00 78.42  ? 574 VAL A CG2   1 
ATOM   4464 N  N     . GLU A 1 575 ? 16.096 15.626  37.156  1.00 83.83  ? 575 GLU A N     1 
ATOM   4465 C  CA    . GLU A 1 575 ? 17.119 16.667  37.155  1.00 87.23  ? 575 GLU A CA    1 
ATOM   4466 C  C     . GLU A 1 575 ? 18.312 16.258  36.301  1.00 77.04  ? 575 GLU A C     1 
ATOM   4467 O  O     . GLU A 1 575 ? 18.707 16.976  35.376  1.00 73.61  ? 575 GLU A O     1 
ATOM   4468 C  CB    . GLU A 1 575 ? 17.557 16.974  38.588  1.00 94.11  ? 575 GLU A CB    1 
ATOM   4469 C  CG    . GLU A 1 575 ? 16.417 17.330  39.526  1.00 101.09 ? 575 GLU A CG    1 
ATOM   4470 C  CD    . GLU A 1 575 ? 16.903 17.735  40.902  1.00 112.30 ? 575 GLU A CD    1 
ATOM   4471 O  OE1   . GLU A 1 575 ? 18.090 18.104  41.028  1.00 115.35 ? 575 GLU A OE1   1 
ATOM   4472 O  OE2   . GLU A 1 575 ? 16.101 17.679  41.859  1.00 116.23 ? 575 GLU A OE2   1 
ATOM   4473 N  N     . GLU A 1 576 ? 18.903 15.100  36.601  1.00 82.73  ? 576 GLU A N     1 
ATOM   4474 C  CA    . GLU A 1 576 ? 20.046 14.622  35.834  1.00 83.03  ? 576 GLU A CA    1 
ATOM   4475 C  C     . GLU A 1 576 ? 19.655 14.191  34.427  1.00 79.17  ? 576 GLU A C     1 
ATOM   4476 O  O     . GLU A 1 576 ? 20.502 14.210  33.529  1.00 76.58  ? 576 GLU A O     1 
ATOM   4477 C  CB    . GLU A 1 576 ? 20.722 13.465  36.575  1.00 86.62  ? 576 GLU A CB    1 
ATOM   4478 C  CG    . GLU A 1 576 ? 22.070 13.047  36.007  1.00 93.50  ? 576 GLU A CG    1 
ATOM   4479 C  CD    . GLU A 1 576 ? 22.748 11.976  36.843  1.00 102.27 ? 576 GLU A CD    1 
ATOM   4480 O  OE1   . GLU A 1 576 ? 22.141 11.518  37.836  1.00 101.07 ? 576 GLU A OE1   1 
ATOM   4481 O  OE2   . GLU A 1 576 ? 23.889 11.593  36.506  1.00 103.38 ? 576 GLU A OE2   1 
ATOM   4482 N  N     . LEU A 1 577 ? 18.391 13.817  34.211  1.00 74.93  ? 577 LEU A N     1 
ATOM   4483 C  CA    . LEU A 1 577 ? 17.951 13.378  32.892  1.00 65.80  ? 577 LEU A CA    1 
ATOM   4484 C  C     . LEU A 1 577 ? 17.812 14.539  31.916  1.00 64.40  ? 577 LEU A C     1 
ATOM   4485 O  O     . LEU A 1 577 ? 17.980 14.348  30.705  1.00 57.31  ? 577 LEU A O     1 
ATOM   4486 C  CB    . LEU A 1 577 ? 16.626 12.620  33.010  1.00 64.14  ? 577 LEU A CB    1 
ATOM   4487 C  CG    . LEU A 1 577 ? 16.112 11.900  31.763  1.00 59.56  ? 577 LEU A CG    1 
ATOM   4488 C  CD1   . LEU A 1 577 ? 17.161 10.939  31.225  1.00 58.45  ? 577 LEU A CD1   1 
ATOM   4489 C  CD2   . LEU A 1 577 ? 14.819 11.164  32.071  1.00 58.55  ? 577 LEU A CD2   1 
ATOM   4490 N  N     . PHE A 1 578 ? 17.508 15.740  32.409  1.00 62.12  ? 578 PHE A N     1 
ATOM   4491 C  CA    . PHE A 1 578 ? 17.414 16.923  31.561  1.00 60.61  ? 578 PHE A CA    1 
ATOM   4492 C  C     . PHE A 1 578 ? 18.442 17.987  31.921  1.00 62.30  ? 578 PHE A C     1 
ATOM   4493 O  O     . PHE A 1 578 ? 18.323 19.130  31.461  1.00 60.92  ? 578 PHE A O     1 
ATOM   4494 C  CB    . PHE A 1 578 ? 16.006 17.520  31.624  1.00 60.19  ? 578 PHE A CB    1 
ATOM   4495 C  CG    . PHE A 1 578 ? 14.993 16.765  30.818  1.00 58.41  ? 578 PHE A CG    1 
ATOM   4496 C  CD1   . PHE A 1 578 ? 14.855 17.005  29.458  1.00 53.02  ? 578 PHE A CD1   1 
ATOM   4497 C  CD2   . PHE A 1 578 ? 14.181 15.816  31.418  1.00 53.76  ? 578 PHE A CD2   1 
ATOM   4498 C  CE1   . PHE A 1 578 ? 13.925 16.310  28.711  1.00 51.68  ? 578 PHE A CE1   1 
ATOM   4499 C  CE2   . PHE A 1 578 ? 13.246 15.121  30.681  1.00 53.70  ? 578 PHE A CE2   1 
ATOM   4500 C  CZ    . PHE A 1 578 ? 13.117 15.367  29.324  1.00 55.14  ? 578 PHE A CZ    1 
ATOM   4501 N  N     . GLY A 1 579 ? 19.445 17.644  32.724  1.00 69.41  ? 579 GLY A N     1 
ATOM   4502 C  CA    . GLY A 1 579 ? 20.465 18.615  33.087  1.00 65.29  ? 579 GLY A CA    1 
ATOM   4503 C  C     . GLY A 1 579 ? 21.296 19.015  31.882  1.00 65.56  ? 579 GLY A C     1 
ATOM   4504 O  O     . GLY A 1 579 ? 21.822 18.161  31.157  1.00 62.84  ? 579 GLY A O     1 
ATOM   4505 N  N     . ILE A 1 580 ? 21.416 20.318  31.660  1.00 59.95  ? 580 ILE A N     1 
ATOM   4506 C  CA    . ILE A 1 580 ? 22.211 20.867  30.571  1.00 57.79  ? 580 ILE A CA    1 
ATOM   4507 C  C     . ILE A 1 580 ? 23.383 21.601  31.208  1.00 55.26  ? 580 ILE A C     1 
ATOM   4508 O  O     . ILE A 1 580 ? 23.238 22.725  31.699  1.00 63.53  ? 580 ILE A O     1 
ATOM   4509 C  CB    . ILE A 1 580 ? 21.386 21.787  29.665  1.00 54.27  ? 580 ILE A CB    1 
ATOM   4510 C  CG1   . ILE A 1 580 ? 20.222 21.004  29.051  1.00 54.56  ? 580 ILE A CG1   1 
ATOM   4511 C  CG2   . ILE A 1 580 ? 22.264 22.394  28.580  1.00 54.96  ? 580 ILE A CG2   1 
ATOM   4512 C  CD1   . ILE A 1 580 ? 19.290 21.842  28.212  1.00 51.66  ? 580 ILE A CD1   1 
ATOM   4513 N  N     . SER A 1 581 ? 24.547 20.959  31.216  1.00 55.07  ? 581 SER A N     1 
ATOM   4514 C  CA    . SER A 1 581 ? 25.746 21.536  31.805  1.00 53.59  ? 581 SER A CA    1 
ATOM   4515 C  C     . SER A 1 581 ? 26.464 22.400  30.777  1.00 59.73  ? 581 SER A C     1 
ATOM   4516 O  O     . SER A 1 581 ? 26.711 21.960  29.649  1.00 62.70  ? 581 SER A O     1 
ATOM   4517 C  CB    . SER A 1 581 ? 26.678 20.437  32.313  1.00 57.12  ? 581 SER A CB    1 
ATOM   4518 O  OG    . SER A 1 581 ? 27.931 20.974  32.699  1.00 64.29  ? 581 SER A OG    1 
ATOM   4519 N  N     . LYS A 1 582 ? 26.793 23.632  31.172  1.00 65.70  ? 582 LYS A N     1 
ATOM   4520 C  CA    . LYS A 1 582 ? 27.555 24.511  30.291  1.00 60.77  ? 582 LYS A CA    1 
ATOM   4521 C  C     . LYS A 1 582 ? 28.938 23.938  30.011  1.00 61.02  ? 582 LYS A C     1 
ATOM   4522 O  O     . LYS A 1 582 ? 29.455 24.057  28.894  1.00 57.82  ? 582 LYS A O     1 
ATOM   4523 C  CB    . LYS A 1 582 ? 27.669 25.906  30.912  1.00 63.47  ? 582 LYS A CB    1 
ATOM   4524 C  CG    . LYS A 1 582 ? 28.479 26.897  30.086  1.00 63.14  ? 582 LYS A CG    1 
ATOM   4525 C  CD    . LYS A 1 582 ? 28.677 28.211  30.823  1.00 65.55  ? 582 LYS A CD    1 
ATOM   4526 C  CE    . LYS A 1 582 ? 29.447 29.214  29.972  1.00 67.91  ? 582 LYS A CE    1 
ATOM   4527 N  NZ    . LYS A 1 582 ? 29.584 30.540  30.647  1.00 66.88  ? 582 LYS A NZ    1 
ATOM   4528 N  N     . GLU A 1 583 ? 29.549 23.304  31.014  1.00 68.94  ? 583 GLU A N     1 
ATOM   4529 C  CA    . GLU A 1 583 ? 30.892 22.761  30.840  1.00 66.85  ? 583 GLU A CA    1 
ATOM   4530 C  C     . GLU A 1 583 ? 30.900 21.611  29.842  1.00 67.19  ? 583 GLU A C     1 
ATOM   4531 O  O     . GLU A 1 583 ? 31.852 21.461  29.067  1.00 67.20  ? 583 GLU A O     1 
ATOM   4532 C  CB    . GLU A 1 583 ? 31.451 22.311  32.189  1.00 73.78  ? 583 GLU A CB    1 
ATOM   4533 C  CG    . GLU A 1 583 ? 32.880 21.804  32.128  1.00 86.36  ? 583 GLU A CG    1 
ATOM   4534 C  CD    . GLU A 1 583 ? 33.501 21.650  33.500  1.00 97.18  ? 583 GLU A CD    1 
ATOM   4535 O  OE1   . GLU A 1 583 ? 32.911 22.154  34.480  1.00 98.33  ? 583 GLU A OE1   1 
ATOM   4536 O  OE2   . GLU A 1 583 ? 34.580 21.026  33.599  1.00 102.28 ? 583 GLU A OE2   1 
ATOM   4537 N  N     . PHE A 1 584 ? 29.848 20.789  29.841  1.00 62.17  ? 584 PHE A N     1 
ATOM   4538 C  CA    . PHE A 1 584 ? 29.785 19.688  28.887  1.00 58.80  ? 584 PHE A CA    1 
ATOM   4539 C  C     . PHE A 1 584 ? 29.593 20.199  27.465  1.00 53.72  ? 584 PHE A C     1 
ATOM   4540 O  O     . PHE A 1 584 ? 30.228 19.701  26.528  1.00 51.70  ? 584 PHE A O     1 
ATOM   4541 C  CB    . PHE A 1 584 ? 28.660 18.722  29.261  1.00 52.08  ? 584 PHE A CB    1 
ATOM   4542 C  CG    . PHE A 1 584 ? 28.418 17.653  28.232  1.00 47.78  ? 584 PHE A CG    1 
ATOM   4543 C  CD1   . PHE A 1 584 ? 29.175 16.495  28.227  1.00 48.91  ? 584 PHE A CD1   1 
ATOM   4544 C  CD2   . PHE A 1 584 ? 27.436 17.809  27.266  1.00 50.21  ? 584 PHE A CD2   1 
ATOM   4545 C  CE1   . PHE A 1 584 ? 28.959 15.513  27.280  1.00 49.30  ? 584 PHE A CE1   1 
ATOM   4546 C  CE2   . PHE A 1 584 ? 27.218 16.832  26.312  1.00 48.30  ? 584 PHE A CE2   1 
ATOM   4547 C  CZ    . PHE A 1 584 ? 27.980 15.682  26.320  1.00 46.16  ? 584 PHE A CZ    1 
ATOM   4548 N  N     . TRP A 1 585 ? 28.719 21.188  27.282  1.00 52.40  ? 585 TRP A N     1 
ATOM   4549 C  CA    . TRP A 1 585 ? 28.407 21.662  25.941  1.00 52.40  ? 585 TRP A CA    1 
ATOM   4550 C  C     . TRP A 1 585 ? 29.481 22.579  25.372  1.00 54.35  ? 585 TRP A C     1 
ATOM   4551 O  O     . TRP A 1 585 ? 29.530 22.769  24.153  1.00 52.33  ? 585 TRP A O     1 
ATOM   4552 C  CB    . TRP A 1 585 ? 27.046 22.359  25.943  1.00 45.86  ? 585 TRP A CB    1 
ATOM   4553 C  CG    . TRP A 1 585 ? 25.927 21.379  26.022  1.00 47.06  ? 585 TRP A CG    1 
ATOM   4554 C  CD1   . TRP A 1 585 ? 25.245 20.998  27.140  1.00 50.18  ? 585 TRP A CD1   1 
ATOM   4555 C  CD2   . TRP A 1 585 ? 25.382 20.619  24.940  1.00 49.38  ? 585 TRP A CD2   1 
ATOM   4556 N  NE1   . TRP A 1 585 ? 24.296 20.058  26.819  1.00 43.89  ? 585 TRP A NE1   1 
ATOM   4557 C  CE2   . TRP A 1 585 ? 24.360 19.807  25.474  1.00 44.96  ? 585 TRP A CE2   1 
ATOM   4558 C  CE3   . TRP A 1 585 ? 25.653 20.550  23.570  1.00 39.74  ? 585 TRP A CE3   1 
ATOM   4559 C  CZ2   . TRP A 1 585 ? 23.609 18.939  24.686  1.00 46.45  ? 585 TRP A CZ2   1 
ATOM   4560 C  CZ3   . TRP A 1 585 ? 24.905 19.688  22.790  1.00 49.52  ? 585 TRP A CZ3   1 
ATOM   4561 C  CH2   . TRP A 1 585 ? 23.896 18.891  23.351  1.00 44.15  ? 585 TRP A CH2   1 
ATOM   4562 N  N     . GLU A 1 586 ? 30.346 23.144  26.216  1.00 50.37  ? 586 GLU A N     1 
ATOM   4563 C  CA    . GLU A 1 586 ? 31.501 23.861  25.691  1.00 53.15  ? 586 GLU A CA    1 
ATOM   4564 C  C     . GLU A 1 586 ? 32.477 22.901  25.025  1.00 54.28  ? 586 GLU A C     1 
ATOM   4565 O  O     . GLU A 1 586 ? 33.049 23.218  23.975  1.00 53.19  ? 586 GLU A O     1 
ATOM   4566 C  CB    . GLU A 1 586 ? 32.188 24.647  26.808  1.00 57.90  ? 586 GLU A CB    1 
ATOM   4567 C  CG    . GLU A 1 586 ? 31.457 25.917  27.200  1.00 56.24  ? 586 GLU A CG    1 
ATOM   4568 C  CD    . GLU A 1 586 ? 32.207 26.716  28.242  1.00 66.68  ? 586 GLU A CD    1 
ATOM   4569 O  OE1   . GLU A 1 586 ? 33.022 26.116  28.976  1.00 62.84  ? 586 GLU A OE1   1 
ATOM   4570 O  OE2   . GLU A 1 586 ? 31.987 27.945  28.324  1.00 70.86  ? 586 GLU A OE2   1 
ATOM   4571 N  N     . LYS A 1 587 ? 32.674 21.720  25.619  1.00 55.68  ? 587 LYS A N     1 
ATOM   4572 C  CA    . LYS A 1 587 ? 33.487 20.693  24.977  1.00 47.77  ? 587 LYS A CA    1 
ATOM   4573 C  C     . LYS A 1 587 ? 32.794 20.144  23.738  1.00 46.71  ? 587 LYS A C     1 
ATOM   4574 O  O     . LYS A 1 587 ? 33.450 19.851  22.731  1.00 51.28  ? 587 LYS A O     1 
ATOM   4575 C  CB    . LYS A 1 587 ? 33.783 19.560  25.961  1.00 56.14  ? 587 LYS A CB    1 
ATOM   4576 C  CG    . LYS A 1 587 ? 34.245 20.008  27.343  1.00 67.77  ? 587 LYS A CG    1 
ATOM   4577 C  CD    . LYS A 1 587 ? 34.437 18.811  28.275  1.00 75.44  ? 587 LYS A CD    1 
ATOM   4578 C  CE    . LYS A 1 587 ? 34.679 19.240  29.721  1.00 83.48  ? 587 LYS A CE    1 
ATOM   4579 N  NZ    . LYS A 1 587 ? 35.913 20.061  29.885  1.00 83.99  ? 587 LYS A NZ    1 
ATOM   4580 N  N     . GLU A 1 588 ? 31.468 20.000  23.793  1.00 48.53  ? 588 GLU A N     1 
ATOM   4581 C  CA    . GLU A 1 588 ? 30.738 19.368  22.698  1.00 46.73  ? 588 GLU A CA    1 
ATOM   4582 C  C     . GLU A 1 588 ? 30.830 20.196  21.422  1.00 46.93  ? 588 GLU A C     1 
ATOM   4583 O  O     . GLU A 1 588 ? 31.104 19.660  20.342  1.00 44.28  ? 588 GLU A O     1 
ATOM   4584 C  CB    . GLU A 1 588 ? 29.279 19.152  23.102  1.00 46.00  ? 588 GLU A CB    1 
ATOM   4585 C  CG    . GLU A 1 588 ? 28.507 18.206  22.190  1.00 39.06  ? 588 GLU A CG    1 
ATOM   4586 C  CD    . GLU A 1 588 ? 28.989 16.766  22.290  1.00 48.08  ? 588 GLU A CD    1 
ATOM   4587 O  OE1   . GLU A 1 588 ? 29.609 16.412  23.320  1.00 43.68  ? 588 GLU A OE1   1 
ATOM   4588 O  OE2   . GLU A 1 588 ? 28.753 15.991  21.333  1.00 40.95  ? 588 GLU A OE2   1 
ATOM   4589 N  N     . VAL A 1 589 ? 30.606 21.509  21.527  1.00 47.69  ? 589 VAL A N     1 
ATOM   4590 C  CA    . VAL A 1 589 ? 30.736 22.373  20.358  1.00 49.69  ? 589 VAL A CA    1 
ATOM   4591 C  C     . VAL A 1 589 ? 32.181 22.418  19.877  1.00 48.27  ? 589 VAL A C     1 
ATOM   4592 O  O     . VAL A 1 589 ? 32.437 22.595  18.681  1.00 51.92  ? 589 VAL A O     1 
ATOM   4593 C  CB    . VAL A 1 589 ? 30.200 23.784  20.666  1.00 50.21  ? 589 VAL A CB    1 
ATOM   4594 C  CG1   . VAL A 1 589 ? 28.717 23.729  20.981  1.00 43.39  ? 589 VAL A CG1   1 
ATOM   4595 C  CG2   . VAL A 1 589 ? 30.970 24.411  21.814  1.00 51.95  ? 589 VAL A CG2   1 
ATOM   4596 N  N     . GLU A 1 590 ? 33.143 22.256  20.788  1.00 52.85  ? 590 GLU A N     1 
ATOM   4597 C  CA    . GLU A 1 590 ? 34.546 22.202  20.390  1.00 54.12  ? 590 GLU A CA    1 
ATOM   4598 C  C     . GLU A 1 590 ? 34.809 21.004  19.483  1.00 56.60  ? 590 GLU A C     1 
ATOM   4599 O  O     . GLU A 1 590 ? 35.443 21.136  18.429  1.00 56.21  ? 590 GLU A O     1 
ATOM   4600 C  CB    . GLU A 1 590 ? 35.434 22.150  21.636  1.00 59.59  ? 590 GLU A CB    1 
ATOM   4601 C  CG    . GLU A 1 590 ? 36.928 22.114  21.354  1.00 68.35  ? 590 GLU A CG    1 
ATOM   4602 C  CD    . GLU A 1 590 ? 37.514 23.491  21.106  1.00 85.38  ? 590 GLU A CD    1 
ATOM   4603 O  OE1   . GLU A 1 590 ? 36.828 24.494  21.404  1.00 88.37  ? 590 GLU A OE1   1 
ATOM   4604 O  OE2   . GLU A 1 590 ? 38.661 23.569  20.614  1.00 88.94  ? 590 GLU A OE2   1 
ATOM   4605 N  N     . GLU A 1 591 ? 34.317 19.822  19.873  1.00 52.64  ? 591 GLU A N     1 
ATOM   4606 C  CA    . GLU A 1 591 ? 34.527 18.631  19.055  1.00 50.92  ? 591 GLU A CA    1 
ATOM   4607 C  C     . GLU A 1 591 ? 33.745 18.707  17.750  1.00 47.16  ? 591 GLU A C     1 
ATOM   4608 O  O     . GLU A 1 591 ? 34.242 18.285  16.700  1.00 47.55  ? 591 GLU A O     1 
ATOM   4609 C  CB    . GLU A 1 591 ? 34.143 17.373  19.838  1.00 48.06  ? 591 GLU A CB    1 
ATOM   4610 C  CG    . GLU A 1 591 ? 35.119 17.015  20.947  1.00 49.47  ? 591 GLU A CG    1 
ATOM   4611 C  CD    . GLU A 1 591 ? 36.513 16.707  20.424  1.00 59.71  ? 591 GLU A CD    1 
ATOM   4612 O  OE1   . GLU A 1 591 ? 36.626 16.009  19.391  1.00 58.72  ? 591 GLU A OE1   1 
ATOM   4613 O  OE2   . GLU A 1 591 ? 37.498 17.170  21.044  1.00 56.18  ? 591 GLU A OE2   1 
ATOM   4614 N  N     . ILE A 1 592 ? 32.521 19.234  17.795  1.00 42.75  ? 592 ILE A N     1 
ATOM   4615 C  CA    . ILE A 1 592 ? 31.727 19.353  16.575  1.00 47.21  ? 592 ILE A CA    1 
ATOM   4616 C  C     . ILE A 1 592 ? 32.374 20.342  15.611  1.00 47.66  ? 592 ILE A C     1 
ATOM   4617 O  O     . ILE A 1 592 ? 32.396 20.120  14.394  1.00 44.06  ? 592 ILE A O     1 
ATOM   4618 C  CB    . ILE A 1 592 ? 30.279 19.749  16.921  1.00 47.82  ? 592 ILE A CB    1 
ATOM   4619 C  CG1   . ILE A 1 592 ? 29.607 18.641  17.736  1.00 49.14  ? 592 ILE A CG1   1 
ATOM   4620 C  CG2   . ILE A 1 592 ? 29.478 20.041  15.659  1.00 39.60  ? 592 ILE A CG2   1 
ATOM   4621 C  CD1   . ILE A 1 592 ? 28.336 19.080  18.436  1.00 41.89  ? 592 ILE A CD1   1 
ATOM   4622 N  N     . ASP A 1 593 ? 32.924 21.440  16.138  1.00 49.87  ? 593 ASP A N     1 
ATOM   4623 C  CA    . ASP A 1 593 ? 33.598 22.420  15.290  1.00 46.17  ? 593 ASP A CA    1 
ATOM   4624 C  C     . ASP A 1 593 ? 34.825 21.811  14.620  1.00 50.28  ? 593 ASP A C     1 
ATOM   4625 O  O     . ASP A 1 593 ? 34.988 21.908  13.399  1.00 52.52  ? 593 ASP A O     1 
ATOM   4626 C  CB    . ASP A 1 593 ? 33.982 23.647  16.120  1.00 48.71  ? 593 ASP A CB    1 
ATOM   4627 C  CG    . ASP A 1 593 ? 34.561 24.776  15.278  1.00 56.26  ? 593 ASP A CG    1 
ATOM   4628 O  OD1   . ASP A 1 593 ? 34.399 24.763  14.040  1.00 58.84  ? 593 ASP A OD1   1 
ATOM   4629 O  OD2   . ASP A 1 593 ? 35.184 25.683  15.865  1.00 56.53  ? 593 ASP A OD2   1 
ATOM   4630 N  N     . LYS A 1 594 ? 35.696 21.169  15.405  1.00 51.92  ? 594 LYS A N     1 
ATOM   4631 C  CA    . LYS A 1 594 ? 36.881 20.537  14.832  1.00 52.42  ? 594 LYS A CA    1 
ATOM   4632 C  C     . LYS A 1 594 ? 36.509 19.449  13.835  1.00 50.37  ? 594 LYS A C     1 
ATOM   4633 O  O     . LYS A 1 594 ? 37.221 19.243  12.846  1.00 47.08  ? 594 LYS A O     1 
ATOM   4634 C  CB    . LYS A 1 594 ? 37.763 19.959  15.941  1.00 49.54  ? 594 LYS A CB    1 
ATOM   4635 C  CG    . LYS A 1 594 ? 38.369 21.006  16.869  1.00 54.59  ? 594 LYS A CG    1 
ATOM   4636 C  CD    . LYS A 1 594 ? 39.337 20.378  17.866  1.00 56.71  ? 594 LYS A CD    1 
ATOM   4637 C  CE    . LYS A 1 594 ? 38.659 19.282  18.684  1.00 59.40  ? 594 LYS A CE    1 
ATOM   4638 N  NZ    . LYS A 1 594 ? 39.589 18.646  19.661  1.00 55.59  ? 594 LYS A NZ    1 
ATOM   4639 N  N     . TYR A 1 595 ? 35.395 18.753  14.071  1.00 47.11  ? 595 TYR A N     1 
ATOM   4640 C  CA    . TYR A 1 595 ? 34.986 17.681  13.172  1.00 47.29  ? 595 TYR A CA    1 
ATOM   4641 C  C     . TYR A 1 595 ? 34.504 18.237  11.836  1.00 48.75  ? 595 TYR A C     1 
ATOM   4642 O  O     . TYR A 1 595 ? 34.995 17.838  10.774  1.00 48.44  ? 595 TYR A O     1 
ATOM   4643 C  CB    . TYR A 1 595 ? 33.904 16.829  13.838  1.00 43.51  ? 595 TYR A CB    1 
ATOM   4644 C  CG    . TYR A 1 595 ? 33.329 15.756  12.944  1.00 41.51  ? 595 TYR A CG    1 
ATOM   4645 C  CD1   . TYR A 1 595 ? 34.019 14.574  12.712  1.00 41.74  ? 595 TYR A CD1   1 
ATOM   4646 C  CD2   . TYR A 1 595 ? 32.093 15.923  12.336  1.00 40.19  ? 595 TYR A CD2   1 
ATOM   4647 C  CE1   . TYR A 1 595 ? 33.496 13.592  11.894  1.00 40.70  ? 595 TYR A CE1   1 
ATOM   4648 C  CE2   . TYR A 1 595 ? 31.563 14.949  11.519  1.00 37.53  ? 595 TYR A CE2   1 
ATOM   4649 C  CZ    . TYR A 1 595 ? 32.267 13.788  11.299  1.00 38.38  ? 595 TYR A CZ    1 
ATOM   4650 O  OH    . TYR A 1 595 ? 31.736 12.817  10.485  1.00 50.99  ? 595 TYR A OH    1 
ATOM   4651 N  N     . LEU A 1 596 ? 33.544 19.164  11.870  1.00 48.79  ? 596 LEU A N     1 
ATOM   4652 C  CA    . LEU A 1 596 ? 33.002 19.716  10.631  1.00 49.78  ? 596 LEU A CA    1 
ATOM   4653 C  C     . LEU A 1 596 ? 34.074 20.445  9.828   1.00 54.70  ? 596 LEU A C     1 
ATOM   4654 O  O     . LEU A 1 596 ? 34.128 20.322  8.599   1.00 50.51  ? 596 LEU A O     1 
ATOM   4655 C  CB    . LEU A 1 596 ? 31.835 20.653  10.943  1.00 52.56  ? 596 LEU A CB    1 
ATOM   4656 C  CG    . LEU A 1 596 ? 30.562 19.995  11.482  1.00 41.56  ? 596 LEU A CG    1 
ATOM   4657 C  CD1   . LEU A 1 596 ? 29.559 21.048  11.925  1.00 43.56  ? 596 LEU A CD1   1 
ATOM   4658 C  CD2   . LEU A 1 596 ? 29.951 19.083  10.435  1.00 40.59  ? 596 LEU A CD2   1 
ATOM   4659 N  N     . GLU A 1 597 ? 34.940 21.203  10.507  1.00 60.81  ? 597 GLU A N     1 
ATOM   4660 C  CA    . GLU A 1 597 ? 35.991 21.937  9.808   1.00 62.20  ? 597 GLU A CA    1 
ATOM   4661 C  C     . GLU A 1 597 ? 36.966 20.991  9.119   1.00 62.56  ? 597 GLU A C     1 
ATOM   4662 O  O     . GLU A 1 597 ? 37.455 21.287  8.022   1.00 60.52  ? 597 GLU A O     1 
ATOM   4663 C  CB    . GLU A 1 597 ? 36.733 22.850  10.785  1.00 64.15  ? 597 GLU A CB    1 
ATOM   4664 C  CG    . GLU A 1 597 ? 37.912 23.588  10.173  1.00 72.40  ? 597 GLU A CG    1 
ATOM   4665 C  CD    . GLU A 1 597 ? 38.594 24.520  11.157  1.00 85.28  ? 597 GLU A CD    1 
ATOM   4666 O  OE1   . GLU A 1 597 ? 38.189 24.542  12.340  1.00 88.37  ? 597 GLU A OE1   1 
ATOM   4667 O  OE2   . GLU A 1 597 ? 39.533 25.235  10.748  1.00 90.72  ? 597 GLU A OE2   1 
ATOM   4668 N  N     . ASP A 1 598 ? 37.255 19.847  9.741   1.00 56.12  ? 598 ASP A N     1 
ATOM   4669 C  CA    . ASP A 1 598 ? 38.200 18.902  9.157   1.00 55.15  ? 598 ASP A CA    1 
ATOM   4670 C  C     . ASP A 1 598 ? 37.538 18.028  8.099   1.00 53.10  ? 598 ASP A C     1 
ATOM   4671 O  O     . ASP A 1 598 ? 38.037 17.919  6.974   1.00 57.68  ? 598 ASP A O     1 
ATOM   4672 C  CB    . ASP A 1 598 ? 38.825 18.035  10.254  1.00 58.52  ? 598 ASP A CB    1 
ATOM   4673 C  CG    . ASP A 1 598 ? 39.608 16.857  9.693   1.00 64.04  ? 598 ASP A CG    1 
ATOM   4674 O  OD1   . ASP A 1 598 ? 40.471 17.069  8.815   1.00 64.98  ? 598 ASP A OD1   1 
ATOM   4675 O  OD2   . ASP A 1 598 ? 39.366 15.714  10.134  1.00 64.84  ? 598 ASP A OD2   1 
ATOM   4676 N  N     . GLN A 1 599 ? 36.408 17.408  8.435   1.00 50.37  ? 599 GLN A N     1 
ATOM   4677 C  CA    . GLN A 1 599 ? 35.840 16.392  7.557   1.00 48.00  ? 599 GLN A CA    1 
ATOM   4678 C  C     . GLN A 1 599 ? 35.056 16.998  6.401   1.00 52.62  ? 599 GLN A C     1 
ATOM   4679 O  O     . GLN A 1 599 ? 35.075 16.457  5.290   1.00 57.25  ? 599 GLN A O     1 
ATOM   4680 C  CB    . GLN A 1 599 ? 34.960 15.440  8.367   1.00 50.96  ? 599 GLN A CB    1 
ATOM   4681 C  CG    . GLN A 1 599 ? 35.742 14.549  9.313   1.00 45.76  ? 599 GLN A CG    1 
ATOM   4682 C  CD    . GLN A 1 599 ? 36.646 13.579  8.577   1.00 47.97  ? 599 GLN A CD    1 
ATOM   4683 O  OE1   . GLN A 1 599 ? 36.247 12.976  7.582   1.00 46.14  ? 599 GLN A OE1   1 
ATOM   4684 N  NE2   . GLN A 1 599 ? 37.873 13.430  9.059   1.00 48.43  ? 599 GLN A NE2   1 
ATOM   4685 N  N     . VAL A 1 600 ? 34.363 18.110  6.631   1.00 52.10  ? 600 VAL A N     1 
ATOM   4686 C  CA    . VAL A 1 600 ? 33.570 18.713  5.563   1.00 48.20  ? 600 VAL A CA    1 
ATOM   4687 C  C     . VAL A 1 600 ? 34.340 19.824  4.857   1.00 49.53  ? 600 VAL A C     1 
ATOM   4688 O  O     . VAL A 1 600 ? 34.282 19.939  3.631   1.00 50.25  ? 600 VAL A O     1 
ATOM   4689 C  CB    . VAL A 1 600 ? 32.224 19.212  6.120   1.00 49.40  ? 600 VAL A CB    1 
ATOM   4690 C  CG1   . VAL A 1 600 ? 31.244 19.456  4.983   1.00 45.67  ? 600 VAL A CG1   1 
ATOM   4691 C  CG2   . VAL A 1 600 ? 31.655 18.200  7.104   1.00 46.24  ? 600 VAL A CG2   1 
ATOM   4692 N  N     . ASN A 1 601 ? 35.059 20.653  5.615   1.00 49.02  ? 601 ASN A N     1 
ATOM   4693 C  CA    . ASN A 1 601 ? 36.046 21.600  5.082   1.00 54.12  ? 601 ASN A CA    1 
ATOM   4694 C  C     . ASN A 1 601 ? 35.363 22.568  4.120   1.00 49.12  ? 601 ASN A C     1 
ATOM   4695 O  O     . ASN A 1 601 ? 34.421 23.263  4.538   1.00 47.65  ? 601 ASN A O     1 
ATOM   4696 C  CB    . ASN A 1 601 ? 37.209 20.797  4.496   1.00 53.01  ? 601 ASN A CB    1 
ATOM   4697 C  CG    . ASN A 1 601 ? 38.389 21.670  4.132   1.00 56.66  ? 601 ASN A CG    1 
ATOM   4698 O  OD1   . ASN A 1 601 ? 38.598 22.726  4.730   1.00 61.00  ? 601 ASN A OD1   1 
ATOM   4699 N  ND2   . ASN A 1 601 ? 39.166 21.240  3.143   1.00 54.61  ? 601 ASN A ND2   1 
ATOM   4700 N  N     . ALA A 1 602 ? 35.778 22.651  2.853   1.00 47.79  ? 602 ALA A N     1 
ATOM   4701 C  CA    . ALA A 1 602 ? 35.296 23.675  1.935   1.00 47.89  ? 602 ALA A CA    1 
ATOM   4702 C  C     . ALA A 1 602 ? 33.882 23.428  1.426   1.00 51.26  ? 602 ALA A C     1 
ATOM   4703 O  O     . ALA A 1 602 ? 33.314 24.315  0.780   1.00 51.26  ? 602 ALA A O     1 
ATOM   4704 C  CB    . ALA A 1 602 ? 36.247 23.793  0.743   1.00 46.64  ? 602 ALA A CB    1 
ATOM   4705 N  N     . ASP A 1 603 ? 33.303 22.259  1.684   1.00 45.57  ? 603 ASP A N     1 
ATOM   4706 C  CA    . ASP A 1 603 ? 31.952 21.951  1.238   1.00 49.12  ? 603 ASP A CA    1 
ATOM   4707 C  C     . ASP A 1 603 ? 30.916 22.130  2.341   1.00 43.43  ? 603 ASP A C     1 
ATOM   4708 O  O     . ASP A 1 603 ? 29.766 21.715  2.169   1.00 43.96  ? 603 ASP A O     1 
ATOM   4709 C  CB    . ASP A 1 603 ? 31.894 20.527  0.678   1.00 46.49  ? 603 ASP A CB    1 
ATOM   4710 C  CG    . ASP A 1 603 ? 32.575 20.404  -0.676  1.00 56.61  ? 603 ASP A CG    1 
ATOM   4711 O  OD1   . ASP A 1 603 ? 32.218 21.172  -1.597  1.00 58.60  ? 603 ASP A OD1   1 
ATOM   4712 O  OD2   . ASP A 1 603 ? 33.477 19.550  -0.817  1.00 56.76  ? 603 ASP A OD2   1 
ATOM   4713 N  N     . LEU A 1 604 ? 31.293 22.742  3.458   1.00 42.65  ? 604 LEU A N     1 
ATOM   4714 C  CA    . LEU A 1 604 ? 30.353 22.978  4.546   1.00 45.81  ? 604 LEU A CA    1 
ATOM   4715 C  C     . LEU A 1 604 ? 29.442 24.147  4.194   1.00 40.75  ? 604 LEU A C     1 
ATOM   4716 O  O     . LEU A 1 604 ? 29.939 25.253  3.966   1.00 48.72  ? 604 LEU A O     1 
ATOM   4717 C  CB    . LEU A 1 604 ? 31.101 23.273  5.838   1.00 46.64  ? 604 LEU A CB    1 
ATOM   4718 C  CG    . LEU A 1 604 ? 30.245 23.453  7.093   1.00 47.84  ? 604 LEU A CG    1 
ATOM   4719 C  CD1   . LEU A 1 604 ? 29.533 22.158  7.433   1.00 39.71  ? 604 LEU A CD1   1 
ATOM   4720 C  CD2   . LEU A 1 604 ? 31.091 23.933  8.263   1.00 48.82  ? 604 LEU A CD2   1 
ATOM   4721 N  N     . PRO A 1 605 ? 28.125 23.953  4.123   1.00 41.32  ? 605 PRO A N     1 
ATOM   4722 C  CA    . PRO A 1 605 ? 27.235 25.087  3.855   1.00 46.99  ? 605 PRO A CA    1 
ATOM   4723 C  C     . PRO A 1 605 ? 27.335 26.129  4.958   1.00 45.44  ? 605 PRO A C     1 
ATOM   4724 O  O     . PRO A 1 605 ? 27.513 25.803  6.133   1.00 45.88  ? 605 PRO A O     1 
ATOM   4725 C  CB    . PRO A 1 605 ? 25.842 24.447  3.814   1.00 44.73  ? 605 PRO A CB    1 
ATOM   4726 C  CG    . PRO A 1 605 ? 26.091 23.010  3.523   1.00 42.60  ? 605 PRO A CG    1 
ATOM   4727 C  CD    . PRO A 1 605 ? 27.391 22.680  4.190   1.00 43.71  ? 605 PRO A CD    1 
ATOM   4728 N  N     . TYR A 1 606 ? 27.228 27.401  4.560   1.00 47.33  ? 606 TYR A N     1 
ATOM   4729 C  CA    . TYR A 1 606 ? 27.349 28.491  5.526   1.00 49.02  ? 606 TYR A CA    1 
ATOM   4730 C  C     . TYR A 1 606 ? 26.284 28.409  6.612   1.00 46.50  ? 606 TYR A C     1 
ATOM   4731 O  O     . TYR A 1 606 ? 26.551 28.761  7.766   1.00 45.93  ? 606 TYR A O     1 
ATOM   4732 C  CB    . TYR A 1 606 ? 27.268 29.843  4.819   1.00 49.05  ? 606 TYR A CB    1 
ATOM   4733 C  CG    . TYR A 1 606 ? 27.143 31.011  5.773   1.00 59.19  ? 606 TYR A CG    1 
ATOM   4734 C  CD1   . TYR A 1 606 ? 28.242 31.473  6.484   1.00 62.36  ? 606 TYR A CD1   1 
ATOM   4735 C  CD2   . TYR A 1 606 ? 25.923 31.648  5.966   1.00 55.67  ? 606 TYR A CD2   1 
ATOM   4736 C  CE1   . TYR A 1 606 ? 28.131 32.538  7.362   1.00 70.01  ? 606 TYR A CE1   1 
ATOM   4737 C  CE2   . TYR A 1 606 ? 25.802 32.715  6.839   1.00 60.42  ? 606 TYR A CE2   1 
ATOM   4738 C  CZ    . TYR A 1 606 ? 26.909 33.157  7.536   1.00 68.78  ? 606 TYR A CZ    1 
ATOM   4739 O  OH    . TYR A 1 606 ? 26.795 34.223  8.408   1.00 65.37  ? 606 TYR A OH    1 
ATOM   4740 N  N     . GLU A 1 607 ? 25.078 27.955  6.265   1.00 42.87  ? 607 GLU A N     1 
ATOM   4741 C  CA    . GLU A 1 607 ? 24.004 27.896  7.250   1.00 47.60  ? 607 GLU A CA    1 
ATOM   4742 C  C     . GLU A 1 607 ? 24.339 26.924  8.375   1.00 46.73  ? 607 GLU A C     1 
ATOM   4743 O  O     . GLU A 1 607 ? 24.019 27.180  9.542   1.00 46.89  ? 607 GLU A O     1 
ATOM   4744 C  CB    . GLU A 1 607 ? 22.694 27.510  6.565   1.00 50.30  ? 607 GLU A CB    1 
ATOM   4745 C  CG    . GLU A 1 607 ? 22.417 28.312  5.305   1.00 57.15  ? 607 GLU A CG    1 
ATOM   4746 C  CD    . GLU A 1 607 ? 21.082 27.974  4.673   1.00 61.68  ? 607 GLU A CD    1 
ATOM   4747 O  OE1   . GLU A 1 607 ? 20.065 27.962  5.398   1.00 58.62  ? 607 GLU A OE1   1 
ATOM   4748 O  OE2   . GLU A 1 607 ? 21.050 27.714  3.450   1.00 70.91  ? 607 GLU A OE2   1 
ATOM   4749 N  N     . ILE A 1 608 ? 24.998 25.811  8.048   1.00 44.21  ? 608 ILE A N     1 
ATOM   4750 C  CA    . ILE A 1 608 ? 25.452 24.883  9.079   1.00 44.99  ? 608 ILE A CA    1 
ATOM   4751 C  C     . ILE A 1 608 ? 26.542 25.524  9.927   1.00 46.74  ? 608 ILE A C     1 
ATOM   4752 O  O     . ILE A 1 608 ? 26.602 25.322  11.147  1.00 46.07  ? 608 ILE A O     1 
ATOM   4753 C  CB    . ILE A 1 608 ? 25.930 23.568  8.436   1.00 39.52  ? 608 ILE A CB    1 
ATOM   4754 C  CG1   . ILE A 1 608 ? 24.790 22.922  7.648   1.00 41.90  ? 608 ILE A CG1   1 
ATOM   4755 C  CG2   . ILE A 1 608 ? 26.447 22.608  9.492   1.00 40.50  ? 608 ILE A CG2   1 
ATOM   4756 C  CD1   . ILE A 1 608 ? 23.598 22.552  8.503   1.00 39.78  ? 608 ILE A CD1   1 
ATOM   4757 N  N     . GLU A 1 609 ? 27.420 26.309  9.295   1.00 43.04  ? 609 GLU A N     1 
ATOM   4758 C  CA    . GLU A 1 609 ? 28.433 27.050  10.038  1.00 49.91  ? 609 GLU A CA    1 
ATOM   4759 C  C     . GLU A 1 609 ? 27.795 28.103  10.937  1.00 48.15  ? 609 GLU A C     1 
ATOM   4760 O  O     . GLU A 1 609 ? 28.264 28.341  12.057  1.00 44.23  ? 609 GLU A O     1 
ATOM   4761 C  CB    . GLU A 1 609 ? 29.418 27.698  9.065   1.00 51.21  ? 609 GLU A CB    1 
ATOM   4762 C  CG    . GLU A 1 609 ? 30.339 28.746  9.683   1.00 61.86  ? 609 GLU A CG    1 
ATOM   4763 C  CD    . GLU A 1 609 ? 31.619 28.155  10.244  1.00 69.44  ? 609 GLU A CD    1 
ATOM   4764 O  OE1   . GLU A 1 609 ? 31.651 26.935  10.515  1.00 70.09  ? 609 GLU A OE1   1 
ATOM   4765 O  OE2   . GLU A 1 609 ? 32.600 28.912  10.408  1.00 73.84  ? 609 GLU A OE2   1 
ATOM   4766 N  N     . ARG A 1 610 ? 26.723 28.744  10.462  1.00 46.18  ? 610 ARG A N     1 
ATOM   4767 C  CA    . ARG A 1 610 ? 26.054 29.765  11.262  1.00 47.39  ? 610 ARG A CA    1 
ATOM   4768 C  C     . ARG A 1 610 ? 25.381 29.155  12.484  1.00 45.97  ? 610 ARG A C     1 
ATOM   4769 O  O     . ARG A 1 610 ? 25.378 29.759  13.564  1.00 43.38  ? 610 ARG A O     1 
ATOM   4770 C  CB    . ARG A 1 610 ? 25.036 30.516  10.404  1.00 51.94  ? 610 ARG A CB    1 
ATOM   4771 C  CG    . ARG A 1 610 ? 24.304 31.635  11.130  1.00 51.01  ? 610 ARG A CG    1 
ATOM   4772 C  CD    . ARG A 1 610 ? 23.435 32.429  10.170  1.00 50.38  ? 610 ARG A CD    1 
ATOM   4773 N  NE    . ARG A 1 610 ? 22.387 31.605  9.582   1.00 50.12  ? 610 ARG A NE    1 
ATOM   4774 C  CZ    . ARG A 1 610 ? 21.645 31.968  8.546   1.00 53.24  ? 610 ARG A CZ    1 
ATOM   4775 N  NH1   . ARG A 1 610 ? 21.818 33.134  7.947   1.00 65.56  ? 610 ARG A NH1   1 
ATOM   4776 N  NH2   . ARG A 1 610 ? 20.707 31.138  8.097   1.00 50.98  ? 610 ARG A NH2   1 
ATOM   4777 N  N     . GLU A 1 611 ? 24.808 27.957  12.331  1.00 43.42  ? 611 GLU A N     1 
ATOM   4778 C  CA    . GLU A 1 611 ? 24.190 27.279  13.467  1.00 43.56  ? 611 GLU A CA    1 
ATOM   4779 C  C     . GLU A 1 611 ? 25.231 26.880  14.503  1.00 42.22  ? 611 GLU A C     1 
ATOM   4780 O  O     . GLU A 1 611 ? 24.992 27.004  15.710  1.00 41.67  ? 611 GLU A O     1 
ATOM   4781 C  CB    . GLU A 1 611 ? 23.411 26.055  12.987  1.00 40.39  ? 611 GLU A CB    1 
ATOM   4782 C  CG    . GLU A 1 611 ? 22.221 26.391  12.101  1.00 43.84  ? 611 GLU A CG    1 
ATOM   4783 C  CD    . GLU A 1 611 ? 21.193 27.255  12.807  1.00 42.57  ? 611 GLU A CD    1 
ATOM   4784 O  OE1   . GLU A 1 611 ? 21.090 27.166  14.048  1.00 40.03  ? 611 GLU A OE1   1 
ATOM   4785 O  OE2   . GLU A 1 611 ? 20.484 28.019  12.123  1.00 45.78  ? 611 GLU A OE2   1 
ATOM   4786 N  N     . LEU A 1 612 ? 26.390 26.394  14.051  1.00 41.42  ? 612 LEU A N     1 
ATOM   4787 C  CA    . LEU A 1 612 ? 27.487 26.117  14.970  1.00 41.49  ? 612 LEU A CA    1 
ATOM   4788 C  C     . LEU A 1 612 ? 27.902 27.374  15.729  1.00 47.24  ? 612 LEU A C     1 
ATOM   4789 O  O     . LEU A 1 612 ? 28.136 27.326  16.943  1.00 45.46  ? 612 LEU A O     1 
ATOM   4790 C  CB    . LEU A 1 612 ? 28.672 25.534  14.203  1.00 41.70  ? 612 LEU A CB    1 
ATOM   4791 C  CG    . LEU A 1 612 ? 29.972 25.349  14.986  1.00 46.03  ? 612 LEU A CG    1 
ATOM   4792 C  CD1   . LEU A 1 612 ? 29.801 24.320  16.093  1.00 44.91  ? 612 LEU A CD1   1 
ATOM   4793 C  CD2   . LEU A 1 612 ? 31.096 24.952  14.047  1.00 54.37  ? 612 LEU A CD2   1 
ATOM   4794 N  N     . ARG A 1 613 ? 27.990 28.511  15.031  1.00 45.25  ? 613 ARG A N     1 
ATOM   4795 C  CA    . ARG A 1 613 ? 28.363 29.759  15.692  1.00 43.31  ? 613 ARG A CA    1 
ATOM   4796 C  C     . ARG A 1 613 ? 27.277 30.226  16.650  1.00 42.18  ? 613 ARG A C     1 
ATOM   4797 O  O     . ARG A 1 613 ? 27.578 30.747  17.731  1.00 44.11  ? 613 ARG A O     1 
ATOM   4798 C  CB    . ARG A 1 613 ? 28.649 30.848  14.659  1.00 45.03  ? 613 ARG A CB    1 
ATOM   4799 C  CG    . ARG A 1 613 ? 29.855 30.595  13.780  1.00 52.11  ? 613 ARG A CG    1 
ATOM   4800 C  CD    . ARG A 1 613 ? 30.115 31.788  12.880  1.00 54.97  ? 613 ARG A CD    1 
ATOM   4801 N  NE    . ARG A 1 613 ? 31.198 31.540  11.937  1.00 66.02  ? 613 ARG A NE    1 
ATOM   4802 C  CZ    . ARG A 1 613 ? 31.747 32.467  11.164  1.00 72.93  ? 613 ARG A CZ    1 
ATOM   4803 N  NH1   . ARG A 1 613 ? 31.349 33.729  11.208  1.00 68.01  ? 613 ARG A NH1   1 
ATOM   4804 N  NH2   . ARG A 1 613 ? 32.722 32.121  10.327  1.00 78.62  ? 613 ARG A NH2   1 
ATOM   4805 N  N     . ALA A 1 614 ? 26.009 30.064  16.266  1.00 41.55  ? 614 ALA A N     1 
ATOM   4806 C  CA    . ALA A 1 614 ? 24.919 30.513  17.123  1.00 41.05  ? 614 ALA A CA    1 
ATOM   4807 C  C     . ALA A 1 614 ? 24.806 29.648  18.375  1.00 45.26  ? 614 ALA A C     1 
ATOM   4808 O  O     . ALA A 1 614 ? 24.575 30.169  19.473  1.00 48.31  ? 614 ALA A O     1 
ATOM   4809 C  CB    . ALA A 1 614 ? 23.605 30.516  16.343  1.00 40.25  ? 614 ALA A CB    1 
ATOM   4810 N  N     . LEU A 1 615 ? 24.971 28.329  18.233  1.00 42.68  ? 615 LEU A N     1 
ATOM   4811 C  CA    . LEU A 1 615 ? 24.948 27.448  19.397  1.00 43.52  ? 615 LEU A CA    1 
ATOM   4812 C  C     . LEU A 1 615 ? 26.088 27.765  20.356  1.00 48.36  ? 615 LEU A C     1 
ATOM   4813 O  O     . LEU A 1 615 ? 25.888 27.818  21.575  1.00 43.04  ? 615 LEU A O     1 
ATOM   4814 C  CB    . LEU A 1 615 ? 25.016 25.984  18.955  1.00 47.17  ? 615 LEU A CB    1 
ATOM   4815 C  CG    . LEU A 1 615 ? 25.140 24.928  20.063  1.00 43.10  ? 615 LEU A CG    1 
ATOM   4816 C  CD1   . LEU A 1 615 ? 23.949 24.981  21.007  1.00 44.42  ? 615 LEU A CD1   1 
ATOM   4817 C  CD2   . LEU A 1 615 ? 25.286 23.541  19.470  1.00 34.68  ? 615 LEU A CD2   1 
ATOM   4818 N  N     . LYS A 1 616 ? 27.295 27.982  19.823  1.00 47.01  ? 616 LYS A N     1 
ATOM   4819 C  CA    . LYS A 1 616 ? 28.433 28.300  20.679  1.00 49.22  ? 616 LYS A CA    1 
ATOM   4820 C  C     . LYS A 1 616 ? 28.232 29.625  21.404  1.00 50.34  ? 616 LYS A C     1 
ATOM   4821 O  O     . LYS A 1 616 ? 28.733 29.806  22.521  1.00 49.59  ? 616 LYS A O     1 
ATOM   4822 C  CB    . LYS A 1 616 ? 29.719 28.325  19.849  1.00 49.53  ? 616 LYS A CB    1 
ATOM   4823 C  CG    . LYS A 1 616 ? 30.989 28.505  20.668  1.00 60.47  ? 616 LYS A CG    1 
ATOM   4824 C  CD    . LYS A 1 616 ? 32.220 28.057  19.894  1.00 69.15  ? 616 LYS A CD    1 
ATOM   4825 C  CE    . LYS A 1 616 ? 33.454 28.029  20.787  1.00 76.47  ? 616 LYS A CE    1 
ATOM   4826 N  NZ    . LYS A 1 616 ? 34.628 27.403  20.110  1.00 81.34  ? 616 LYS A NZ    1 
ATOM   4827 N  N     . GLN A 1 617 ? 27.493 30.554  20.795  1.00 48.85  ? 617 GLN A N     1 
ATOM   4828 C  CA    . GLN A 1 617 ? 27.225 31.826  21.454  1.00 52.36  ? 617 GLN A CA    1 
ATOM   4829 C  C     . GLN A 1 617 ? 26.211 31.661  22.579  1.00 52.00  ? 617 GLN A C     1 
ATOM   4830 O  O     . GLN A 1 617 ? 26.395 32.209  23.673  1.00 50.80  ? 617 GLN A O     1 
ATOM   4831 C  CB    . GLN A 1 617 ? 26.737 32.852  20.430  1.00 49.30  ? 617 GLN A CB    1 
ATOM   4832 C  CG    . GLN A 1 617 ? 26.526 34.246  20.994  1.00 51.59  ? 617 GLN A CG    1 
ATOM   4833 C  CD    . GLN A 1 617 ? 27.827 34.920  21.375  1.00 54.38  ? 617 GLN A CD    1 
ATOM   4834 O  OE1   . GLN A 1 617 ? 28.901 34.513  20.931  1.00 62.69  ? 617 GLN A OE1   1 
ATOM   4835 N  NE2   . GLN A 1 617 ? 27.740 35.957  22.203  1.00 59.25  ? 617 GLN A NE2   1 
ATOM   4836 N  N     . ARG A 1 618 ? 25.135 30.906  22.333  1.00 46.09  ? 618 ARG A N     1 
ATOM   4837 C  CA    . ARG A 1 618 ? 24.127 30.700  23.368  1.00 52.07  ? 618 ARG A CA    1 
ATOM   4838 C  C     . ARG A 1 618 ? 24.693 29.945  24.563  1.00 53.84  ? 618 ARG A C     1 
ATOM   4839 O  O     . ARG A 1 618 ? 24.252 30.162  25.698  1.00 57.03  ? 618 ARG A O     1 
ATOM   4840 C  CB    . ARG A 1 618 ? 22.923 29.956  22.794  1.00 43.75  ? 618 ARG A CB    1 
ATOM   4841 C  CG    . ARG A 1 618 ? 22.149 30.744  21.755  1.00 46.17  ? 618 ARG A CG    1 
ATOM   4842 C  CD    . ARG A 1 618 ? 20.865 30.033  21.373  1.00 41.43  ? 618 ARG A CD    1 
ATOM   4843 N  NE    . ARG A 1 618 ? 21.109 28.667  20.926  1.00 41.14  ? 618 ARG A NE    1 
ATOM   4844 C  CZ    . ARG A 1 618 ? 21.345 28.321  19.668  1.00 44.59  ? 618 ARG A CZ    1 
ATOM   4845 N  NH1   . ARG A 1 618 ? 21.386 29.220  18.699  1.00 46.17  ? 618 ARG A NH1   1 
ATOM   4846 N  NH2   . ARG A 1 618 ? 21.546 27.040  19.374  1.00 45.84  ? 618 ARG A NH2   1 
ATOM   4847 N  N     . ILE A 1 619 ? 25.664 29.063  24.334  1.00 50.92  ? 619 ILE A N     1 
ATOM   4848 C  CA    . ILE A 1 619 ? 26.272 28.328  25.437  1.00 55.59  ? 619 ILE A CA    1 
ATOM   4849 C  C     . ILE A 1 619 ? 27.208 29.226  26.234  1.00 57.47  ? 619 ILE A C     1 
ATOM   4850 O  O     . ILE A 1 619 ? 27.294 29.115  27.463  1.00 60.92  ? 619 ILE A O     1 
ATOM   4851 C  CB    . ILE A 1 619 ? 26.992 27.078  24.900  1.00 49.89  ? 619 ILE A CB    1 
ATOM   4852 C  CG1   . ILE A 1 619 ? 25.964 26.091  24.342  1.00 47.65  ? 619 ILE A CG1   1 
ATOM   4853 C  CG2   . ILE A 1 619 ? 27.845 26.429  25.987  1.00 49.14  ? 619 ILE A CG2   1 
ATOM   4854 C  CD1   . ILE A 1 619 ? 26.570 24.950  23.572  1.00 49.17  ? 619 ILE A CD1   1 
ATOM   4855 N  N     . SER A 1 620 ? 27.908 30.141  25.558  1.00 54.17  ? 620 SER A N     1 
ATOM   4856 C  CA    . SER A 1 620 ? 28.798 31.058  26.261  1.00 59.23  ? 620 SER A CA    1 
ATOM   4857 C  C     . SER A 1 620 ? 28.042 32.016  27.174  1.00 59.75  ? 620 SER A C     1 
ATOM   4858 O  O     . SER A 1 620 ? 28.652 32.603  28.076  1.00 60.41  ? 620 SER A O     1 
ATOM   4859 C  CB    . SER A 1 620 ? 29.642 31.849  25.259  1.00 59.98  ? 620 SER A CB    1 
ATOM   4860 O  OG    . SER A 1 620 ? 28.833 32.705  24.470  1.00 61.86  ? 620 SER A OG    1 
ATOM   4861 N  N     . GLN A 1 621 ? 26.738 32.183  26.971  1.00 56.78  ? 621 GLN A N     1 
ATOM   4862 C  CA    . GLN A 1 621 ? 25.932 33.072  27.797  1.00 63.26  ? 621 GLN A CA    1 
ATOM   4863 C  C     . GLN A 1 621 ? 25.313 32.372  29.000  1.00 67.65  ? 621 GLN A C     1 
ATOM   4864 O  O     . GLN A 1 621 ? 24.569 33.009  29.753  1.00 69.30  ? 621 GLN A O     1 
ATOM   4865 C  CB    . GLN A 1 621 ? 24.828 33.718  26.955  1.00 64.55  ? 621 GLN A CB    1 
ATOM   4866 C  CG    . GLN A 1 621 ? 25.347 34.602  25.830  1.00 62.21  ? 621 GLN A CG    1 
ATOM   4867 C  CD    . GLN A 1 621 ? 26.201 35.749  26.334  1.00 68.08  ? 621 GLN A CD    1 
ATOM   4868 O  OE1   . GLN A 1 621 ? 25.720 36.633  27.047  1.00 69.40  ? 621 GLN A OE1   1 
ATOM   4869 N  NE2   . GLN A 1 621 ? 27.478 35.740  25.967  1.00 69.07  ? 621 GLN A NE2   1 
ATOM   4870 N  N     . MET A 1 622 ? 25.594 31.088  29.198  1.00 66.53  ? 622 MET A N     1 
ATOM   4871 C  CA    . MET A 1 622 ? 25.069 30.364  30.350  1.00 68.17  ? 622 MET A CA    1 
ATOM   4872 C  C     . MET A 1 622 ? 25.790 30.787  31.622  1.00 69.09  ? 622 MET A C     1 
ATOM   4873 O  O     . MET A 1 622 ? 26.947 31.211  31.579  1.00 70.31  ? 622 MET A O     1 
ATOM   4874 C  CB    . MET A 1 622 ? 25.202 28.853  30.150  1.00 67.29  ? 622 MET A CB    1 
ATOM   4875 C  CG    . MET A 1 622 ? 24.392 28.301  28.994  1.00 59.04  ? 622 MET A CG    1 
ATOM   4876 S  SD    . MET A 1 622 ? 24.525 26.509  28.883  1.00 60.08  ? 622 MET A SD    1 
ATOM   4877 C  CE    . MET A 1 622 ? 23.826 26.023  30.459  1.00 60.38  ? 622 MET A CE    1 
ATOM   4878 O  OXT   . MET A 1 622 ? 25.234 30.715  32.717  1.00 74.21  ? 622 MET A OXT   1 
HETATM 4879 MN MN    . MN  B 2 .   ? 16.854 -2.769  12.645  1.00 48.56  ? 701 MN  A MN    1 
HETATM 4880 MN MN    . MN  C 2 .   ? 20.383 -0.305  9.553   1.00 30.49  ? 702 MN  A MN    1 
HETATM 4881 MN MN    . MN  D 2 .   ? 18.588 28.611  3.396   1.00 100.45 ? 703 MN  A MN    1 
HETATM 4882 C  C1    . OXL E 3 .   ? 21.832 -2.963  9.531   1.00 40.38  ? 704 OXL A C1    1 
HETATM 4883 C  C2    . OXL E 3 .   ? 22.850 -1.858  9.893   1.00 39.54  ? 704 OXL A C2    1 
HETATM 4884 O  O1    . OXL E 3 .   ? 20.638 -2.707  9.442   1.00 34.86  ? 704 OXL A O1    1 
HETATM 4885 O  O2    . OXL E 3 .   ? 22.316 -0.695  10.150  1.00 30.88  ? 704 OXL A O2    1 
HETATM 4886 O  O3    . OXL E 3 .   ? 22.364 -4.140  9.335   1.00 40.42  ? 704 OXL A O3    1 
HETATM 4887 O  O4    . OXL E 3 .   ? 24.048 -2.103  9.922   1.00 45.47  ? 704 OXL A O4    1 
HETATM 4888 P  PG    . GTP F 4 .   ? 20.039 -1.717  12.783  1.00 43.95  ? 705 GTP A PG    1 
HETATM 4889 O  O1G   . GTP F 4 .   ? 18.945 -2.752  12.674  1.00 45.58  ? 705 GTP A O1G   1 
HETATM 4890 O  O2G   . GTP F 4 .   ? 21.387 -2.367  12.612  1.00 39.33  ? 705 GTP A O2G   1 
HETATM 4891 O  O3G   . GTP F 4 .   ? 19.854 -0.660  11.718  1.00 36.70  ? 705 GTP A O3G   1 
HETATM 4892 O  O3B   . GTP F 4 .   ? 19.985 -1.035  14.254  1.00 54.77  ? 705 GTP A O3B   1 
HETATM 4893 P  PB    . GTP F 4 .   ? 18.639 -0.718  15.099  1.00 46.23  ? 705 GTP A PB    1 
HETATM 4894 O  O1B   . GTP F 4 .   ? 17.407 -1.246  14.404  1.00 39.87  ? 705 GTP A O1B   1 
HETATM 4895 O  O2B   . GTP F 4 .   ? 18.519 0.769   15.342  1.00 49.90  ? 705 GTP A O2B   1 
HETATM 4896 O  O3A   . GTP F 4 .   ? 18.868 -1.478  16.506  1.00 52.76  ? 705 GTP A O3A   1 
HETATM 4897 P  PA    . GTP F 4 .   ? 17.718 -2.379  17.192  1.00 52.72  ? 705 GTP A PA    1 
HETATM 4898 O  O1A   . GTP F 4 .   ? 17.638 -3.691  16.437  1.00 53.54  ? 705 GTP A O1A   1 
HETATM 4899 O  O2A   . GTP F 4 .   ? 16.372 -1.695  17.198  1.00 43.99  ? 705 GTP A O2A   1 
HETATM 4900 O  "O5'" . GTP F 4 .   ? 18.264 -2.661  18.682  1.00 51.32  ? 705 GTP A "O5'" 1 
HETATM 4901 C  "C5'" . GTP F 4 .   ? 19.611 -2.415  19.019  1.00 47.98  ? 705 GTP A "C5'" 1 
HETATM 4902 C  "C4'" . GTP F 4 .   ? 19.866 -2.804  20.472  1.00 49.30  ? 705 GTP A "C4'" 1 
HETATM 4903 O  "O4'" . GTP F 4 .   ? 19.663 -1.660  21.278  1.00 55.93  ? 705 GTP A "O4'" 1 
HETATM 4904 C  "C3'" . GTP F 4 .   ? 18.902 -3.867  20.973  1.00 56.35  ? 705 GTP A "C3'" 1 
HETATM 4905 O  "O3'" . GTP F 4 .   ? 19.527 -5.131  21.038  1.00 57.45  ? 705 GTP A "O3'" 1 
HETATM 4906 C  "C2'" . GTP F 4 .   ? 18.490 -3.408  22.359  1.00 57.77  ? 705 GTP A "C2'" 1 
HETATM 4907 O  "O2'" . GTP F 4 .   ? 19.082 -4.206  23.360  1.00 63.12  ? 705 GTP A "O2'" 1 
HETATM 4908 C  "C1'" . GTP F 4 .   ? 18.979 -1.969  22.476  1.00 56.00  ? 705 GTP A "C1'" 1 
HETATM 4909 N  N9    . GTP F 4 .   ? 17.813 -1.079  22.648  1.00 45.71  ? 705 GTP A N9    1 
HETATM 4910 C  C8    . GTP F 4 .   ? 16.769 -0.916  21.773  1.00 49.35  ? 705 GTP A C8    1 
HETATM 4911 N  N7    . GTP F 4 .   ? 15.900 -0.019  22.293  1.00 44.79  ? 705 GTP A N7    1 
HETATM 4912 C  C5    . GTP F 4 .   ? 16.373 0.395   23.491  1.00 45.86  ? 705 GTP A C5    1 
HETATM 4913 C  C6    . GTP F 4 .   ? 15.885 1.292   24.434  1.00 42.55  ? 705 GTP A C6    1 
HETATM 4914 O  O6    . GTP F 4 .   ? 14.820 1.880   24.241  1.00 42.80  ? 705 GTP A O6    1 
HETATM 4915 N  N1    . GTP F 4 .   ? 16.606 1.515   25.589  1.00 41.39  ? 705 GTP A N1    1 
HETATM 4916 C  C2    . GTP F 4 .   ? 17.797 0.849   25.802  1.00 41.76  ? 705 GTP A C2    1 
HETATM 4917 N  N2    . GTP F 4 .   ? 18.500 1.059   26.911  1.00 44.21  ? 705 GTP A N2    1 
HETATM 4918 N  N3    . GTP F 4 .   ? 18.270 -0.039  24.860  1.00 49.84  ? 705 GTP A N3    1 
HETATM 4919 C  C4    . GTP F 4 .   ? 17.572 -0.265  23.724  1.00 44.62  ? 705 GTP A C4    1 
HETATM 4920 C  C1    . PGE G 5 .   ? 6.033  10.321  -2.918  1.00 67.31  ? 706 PGE A C1    1 
HETATM 4921 O  O1    . PGE G 5 .   ? 4.663  10.334  -3.286  1.00 66.70  ? 706 PGE A O1    1 
HETATM 4922 C  C2    . PGE G 5 .   ? 6.391  9.066   -2.177  1.00 68.92  ? 706 PGE A C2    1 
HETATM 4923 O  O2    . PGE G 5 .   ? 7.806  8.912   -2.127  1.00 68.83  ? 706 PGE A O2    1 
HETATM 4924 C  C3    . PGE G 5 .   ? 8.435  9.081   -3.390  1.00 68.74  ? 706 PGE A C3    1 
HETATM 4925 C  C4    . PGE G 5 .   ? 9.820  8.526   -3.355  1.00 63.86  ? 706 PGE A C4    1 
HETATM 4926 O  O4    . PGE G 5 .   ? 10.362 9.397   -7.367  1.00 74.93  ? 706 PGE A O4    1 
HETATM 4927 C  C6    . PGE G 5 .   ? 11.259 8.511   -6.713  1.00 70.36  ? 706 PGE A C6    1 
HETATM 4928 C  C5    . PGE G 5 .   ? 11.231 8.752   -5.239  1.00 64.82  ? 706 PGE A C5    1 
HETATM 4929 O  O3    . PGE G 5 .   ? 10.165 8.030   -4.640  1.00 70.24  ? 706 PGE A O3    1 
HETATM 4930 O  O     . HOH H 6 .   ? 17.643 -4.170  14.239  1.00 39.87  ? 801 HOH A O     1 
HETATM 4931 O  O     . HOH H 6 .   ? 23.449 -4.686  7.405   1.00 46.95  ? 802 HOH A O     1 
HETATM 4932 O  O     . HOH H 6 .   ? 35.730 14.004  3.839   1.00 47.28  ? 803 HOH A O     1 
HETATM 4933 O  O     . HOH H 6 .   ? 6.971  -4.408  20.500  1.00 45.27  ? 804 HOH A O     1 
HETATM 4934 O  O     . HOH H 6 .   ? 3.212  3.589   1.617   1.00 56.71  ? 805 HOH A O     1 
HETATM 4935 O  O     . HOH H 6 .   ? 31.505 3.241   21.320  1.00 77.57  ? 806 HOH A O     1 
HETATM 4936 O  O     . HOH H 6 .   ? 35.819 19.224  -0.540  1.00 52.19  ? 807 HOH A O     1 
HETATM 4937 O  O     . HOH H 6 .   ? -1.656 11.049  9.823   1.00 55.74  ? 808 HOH A O     1 
HETATM 4938 O  O     . HOH H 6 .   ? 29.777 6.769   3.917   1.00 38.36  ? 809 HOH A O     1 
HETATM 4939 O  O     . HOH H 6 .   ? 5.897  26.030  24.752  1.00 49.39  ? 810 HOH A O     1 
HETATM 4940 O  O     . HOH H 6 .   ? 19.353 10.806  1.400   1.00 32.85  ? 811 HOH A O     1 
HETATM 4941 O  O     . HOH H 6 .   ? 37.613 -6.055  -16.423 1.00 55.39  ? 812 HOH A O     1 
HETATM 4942 O  O     . HOH H 6 .   ? 32.121 -18.640 -5.635  1.00 44.16  ? 813 HOH A O     1 
HETATM 4943 O  O     . HOH H 6 .   ? 6.194  1.829   2.766   1.00 44.40  ? 814 HOH A O     1 
HETATM 4944 O  O     . HOH H 6 .   ? 22.068 26.719  16.288  1.00 41.01  ? 815 HOH A O     1 
HETATM 4945 O  O     . HOH H 6 .   ? 18.297 8.882   28.514  1.00 42.93  ? 816 HOH A O     1 
HETATM 4946 O  O     . HOH H 6 .   ? 30.610 5.726   -10.533 1.00 52.16  ? 817 HOH A O     1 
HETATM 4947 O  O     . HOH H 6 .   ? 23.214 12.386  18.591  1.00 38.74  ? 818 HOH A O     1 
HETATM 4948 O  O     . HOH H 6 .   ? 33.222 2.408   3.554   1.00 52.32  ? 819 HOH A O     1 
HETATM 4949 O  O     . HOH H 6 .   ? 30.228 1.619   4.854   1.00 41.44  ? 820 HOH A O     1 
HETATM 4950 O  O     . HOH H 6 .   ? 29.911 -3.049  4.009   1.00 43.68  ? 821 HOH A O     1 
HETATM 4951 O  O     . HOH H 6 .   ? 10.669 -25.188 10.942  1.00 54.80  ? 822 HOH A O     1 
HETATM 4952 O  O     . HOH H 6 .   ? 11.938 2.533   7.284   1.00 39.17  ? 823 HOH A O     1 
HETATM 4953 O  O     . HOH H 6 .   ? 19.111 6.340   30.110  1.00 50.73  ? 824 HOH A O     1 
HETATM 4954 O  O     . HOH H 6 .   ? 11.344 -18.217 -4.651  1.00 40.88  ? 825 HOH A O     1 
HETATM 4955 O  O     . HOH H 6 .   ? 16.950 -0.988  11.418  1.00 42.94  ? 826 HOH A O     1 
HETATM 4956 O  O     . HOH H 6 .   ? 25.172 -4.619  10.172  1.00 49.23  ? 827 HOH A O     1 
HETATM 4957 O  O     . HOH H 6 .   ? 23.235 -4.227  1.382   1.00 40.59  ? 828 HOH A O     1 
HETATM 4958 O  O     . HOH H 6 .   ? 26.657 15.940  19.392  1.00 30.99  ? 829 HOH A O     1 
HETATM 4959 O  O     . HOH H 6 .   ? 28.143 11.263  25.763  1.00 45.30  ? 830 HOH A O     1 
HETATM 4960 O  O     . HOH H 6 .   ? 18.850 -14.179 8.971   1.00 39.69  ? 831 HOH A O     1 
HETATM 4961 O  O     . HOH H 6 .   ? 14.239 2.339   20.523  1.00 42.02  ? 832 HOH A O     1 
HETATM 4962 O  O     . HOH H 6 .   ? 19.156 9.219   7.710   1.00 33.27  ? 833 HOH A O     1 
HETATM 4963 O  O     . HOH H 6 .   ? 11.043 -2.775  6.656   1.00 41.96  ? 834 HOH A O     1 
HETATM 4964 O  O     . HOH H 6 .   ? 13.207 -0.587  6.367   1.00 33.73  ? 835 HOH A O     1 
HETATM 4965 O  O     . HOH H 6 .   ? 14.194 -6.443  18.600  1.00 48.93  ? 836 HOH A O     1 
HETATM 4966 O  O     . HOH H 6 .   ? 34.729 -20.490 5.597   1.00 53.87  ? 837 HOH A O     1 
HETATM 4967 O  O     . HOH H 6 .   ? 28.771 34.425  11.105  1.00 55.34  ? 838 HOH A O     1 
HETATM 4968 O  O     . HOH H 6 .   ? 28.612 14.403  13.770  1.00 37.41  ? 839 HOH A O     1 
HETATM 4969 O  O     . HOH H 6 .   ? -2.930 12.310  2.979   1.00 60.53  ? 840 HOH A O     1 
HETATM 4970 O  O     . HOH H 6 .   ? 29.179 4.934   1.853   1.00 40.48  ? 841 HOH A O     1 
HETATM 4971 O  O     . HOH H 6 .   ? 1.109  12.196  9.438   1.00 46.63  ? 842 HOH A O     1 
HETATM 4972 O  O     . HOH H 6 .   ? 4.480  12.389  28.066  1.00 49.06  ? 843 HOH A O     1 
HETATM 4973 O  O     . HOH H 6 .   ? 10.927 -4.486  -1.457  1.00 42.12  ? 844 HOH A O     1 
HETATM 4974 O  O     . HOH H 6 .   ? 18.351 14.431  23.008  1.00 34.78  ? 845 HOH A O     1 
HETATM 4975 O  O     . HOH H 6 .   ? -1.100 4.220   14.933  1.00 52.26  ? 846 HOH A O     1 
HETATM 4976 O  O     . HOH H 6 .   ? 23.723 -12.654 6.952   1.00 47.92  ? 847 HOH A O     1 
HETATM 4977 O  O     . HOH H 6 .   ? 21.385 10.628  21.815  1.00 38.33  ? 848 HOH A O     1 
HETATM 4978 O  O     . HOH H 6 .   ? 27.174 -2.503  3.081   1.00 41.49  ? 849 HOH A O     1 
HETATM 4979 O  O     . HOH H 6 .   ? 8.474  -22.741 -9.709  1.00 50.07  ? 850 HOH A O     1 
HETATM 4980 O  O     . HOH H 6 .   ? 40.086 -6.991  -0.072  1.00 55.59  ? 851 HOH A O     1 
HETATM 4981 O  O     . HOH H 6 .   ? 17.924 -3.760  9.011   1.00 37.46  ? 852 HOH A O     1 
HETATM 4982 O  O     . HOH H 6 .   ? 11.846 16.278  -1.831  1.00 52.92  ? 853 HOH A O     1 
HETATM 4983 O  O     . HOH H 6 .   ? 20.726 31.997  18.693  1.00 45.55  ? 854 HOH A O     1 
HETATM 4984 O  O     . HOH H 6 .   ? 6.394  -9.169  3.619   1.00 45.10  ? 855 HOH A O     1 
HETATM 4985 O  O     . HOH H 6 .   ? 24.065 35.034  8.174   1.00 50.14  ? 856 HOH A O     1 
HETATM 4986 O  O     . HOH H 6 .   ? 30.821 11.613  1.834   1.00 41.79  ? 857 HOH A O     1 
HETATM 4987 O  O     . HOH H 6 .   ? 19.163 -13.580 6.311   1.00 42.48  ? 858 HOH A O     1 
HETATM 4988 O  O     . HOH H 6 .   ? 20.235 12.565  -0.964  1.00 37.84  ? 859 HOH A O     1 
HETATM 4989 O  O     . HOH H 6 .   ? 22.887 37.029  27.581  1.00 70.67  ? 860 HOH A O     1 
HETATM 4990 O  O     . HOH H 6 .   ? -5.091 4.706   13.493  1.00 56.43  ? 861 HOH A O     1 
HETATM 4991 O  O     . HOH H 6 .   ? 26.152 -12.090 12.568  1.00 54.32  ? 862 HOH A O     1 
HETATM 4992 O  O     . HOH H 6 .   ? 18.323 5.908   19.436  1.00 40.81  ? 863 HOH A O     1 
HETATM 4993 O  O     . HOH H 6 .   ? 28.207 3.790   28.600  1.00 58.34  ? 864 HOH A O     1 
HETATM 4994 O  O     . HOH H 6 .   ? -0.851 -10.016 23.335  1.00 61.01  ? 865 HOH A O     1 
HETATM 4995 O  O     . HOH H 6 .   ? 18.730 7.586   21.706  1.00 37.24  ? 866 HOH A O     1 
HETATM 4996 O  O     . HOH H 6 .   ? 38.423 15.419  -6.396  1.00 49.63  ? 867 HOH A O     1 
HETATM 4997 O  O     . HOH H 6 .   ? 15.751 -4.972  1.423   1.00 35.29  ? 868 HOH A O     1 
HETATM 4998 O  O     . HOH H 6 .   ? 12.223 21.567  14.478  1.00 37.16  ? 869 HOH A O     1 
HETATM 4999 O  O     . HOH H 6 .   ? 37.060 20.530  1.028   1.00 52.86  ? 870 HOH A O     1 
HETATM 5000 O  O     . HOH H 6 .   ? 21.615 24.709  0.458   1.00 51.23  ? 871 HOH A O     1 
HETATM 5001 O  O     . HOH H 6 .   ? 12.417 26.953  9.998   1.00 47.18  ? 872 HOH A O     1 
HETATM 5002 O  O     . HOH H 6 .   ? 24.313 -4.071  -28.179 1.00 58.50  ? 873 HOH A O     1 
HETATM 5003 O  O     . HOH H 6 .   ? 38.644 6.785   3.761   1.00 56.76  ? 874 HOH A O     1 
HETATM 5004 O  O     . HOH H 6 .   ? 6.169  -27.035 18.446  1.00 57.38  ? 875 HOH A O     1 
HETATM 5005 O  O     . HOH H 6 .   ? 7.369  -26.575 8.651   1.00 57.10  ? 876 HOH A O     1 
HETATM 5006 O  O     . HOH H 6 .   ? 36.958 14.490  16.600  1.00 60.78  ? 877 HOH A O     1 
HETATM 5007 O  O     . HOH H 6 .   ? 18.737 -35.542 0.127   1.00 50.66  ? 878 HOH A O     1 
HETATM 5008 O  O     . HOH H 6 .   ? 17.415 -25.595 31.623  1.00 67.85  ? 879 HOH A O     1 
HETATM 5009 O  O     . HOH H 6 .   ? 4.514  -12.963 2.820   1.00 53.30  ? 880 HOH A O     1 
HETATM 5010 O  O     . HOH H 6 .   ? 33.236 28.023  14.127  1.00 63.46  ? 881 HOH A O     1 
HETATM 5011 O  O     . HOH H 6 .   ? 17.785 -6.504  -0.189  1.00 40.49  ? 882 HOH A O     1 
HETATM 5012 O  O     . HOH H 6 .   ? 0.350  22.565  27.872  1.00 54.73  ? 883 HOH A O     1 
HETATM 5013 O  O     . HOH H 6 .   ? 6.649  -18.343 2.425   1.00 48.98  ? 884 HOH A O     1 
HETATM 5014 O  O     . HOH H 6 .   ? 24.784 -30.181 17.564  1.00 56.82  ? 885 HOH A O     1 
HETATM 5015 O  O     . HOH H 6 .   ? 37.851 1.641   10.018  1.00 56.66  ? 886 HOH A O     1 
HETATM 5016 O  O     . HOH H 6 .   ? 27.702 -5.321  -17.407 1.00 45.06  ? 887 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 
55   N N   . ASP A 10  ? 1.4507 1.0498 0.7902 -0.0706 0.1759  -0.1621 10  ASP A N   
56   C CA  . ASP A 10  ? 1.4289 1.0275 0.7548 -0.0736 0.1409  -0.1645 10  ASP A CA  
57   C C   . ASP A 10  ? 1.3433 0.9585 0.7277 -0.0584 0.1473  -0.1741 10  ASP A C   
58   O O   . ASP A 10  ? 1.3378 0.9450 0.7392 -0.0592 0.1680  -0.1900 10  ASP A O   
59   C CB  . ASP A 10  ? 1.4587 1.0301 0.7335 -0.0935 0.1381  -0.1755 10  ASP A CB  
60   C CG  . ASP A 10  ? 1.4249 0.9984 0.6824 -0.0996 0.0963  -0.1754 10  ASP A CG  
61   O OD1 . ASP A 10  ? 1.3784 0.9688 0.6762 -0.0899 0.0861  -0.1804 10  ASP A OD1 
62   O OD2 . ASP A 10  ? 1.5176 1.0759 0.7238 -0.1145 0.0734  -0.1700 10  ASP A OD2 
63   N N   . PHE A 11  ? 1.1588 0.8074 0.5938 -0.0427 0.1247  -0.1579 11  PHE A N   
64   C CA  . PHE A 11  ? 1.0673 0.7409 0.5724 -0.0269 0.1236  -0.1583 11  PHE A CA  
65   C C   . PHE A 11  ? 1.0158 0.6904 0.5193 -0.0316 0.0948  -0.1632 11  PHE A C   
66   O O   . PHE A 11  ? 0.9727 0.6696 0.5305 -0.0199 0.0861  -0.1589 11  PHE A O   
67   C CB  . PHE A 11  ? 1.0327 0.7431 0.5962 -0.0097 0.1147  -0.1377 11  PHE A CB  
68   C CG  . PHE A 11  ? 1.0602 0.7794 0.6611 0.0004  0.1469  -0.1368 11  PHE A CG  
69   C CD1 . PHE A 11  ? 1.0430 0.7519 0.6159 -0.0063 0.1669  -0.1359 11  PHE A CD1 
70   C CD2 . PHE A 11  ? 0.9794 0.7170 0.6449 0.0161  0.1562  -0.1364 11  PHE A CD2 
71   C CE1 . PHE A 11  ? 0.9561 0.6774 0.5718 0.0024  0.1968  -0.1364 11  PHE A CE1 
72   C CE2 . PHE A 11  ? 0.9118 0.6613 0.6192 0.0261  0.1821  -0.1350 11  PHE A CE2 
73   C CZ  . PHE A 11  ? 0.8858 0.6294 0.5718 0.0192  0.2029  -0.1359 11  PHE A CZ  
74   N N   . SER A 12  ? 1.0439 0.6942 0.4857 -0.0501 0.0799  -0.1725 12  SER A N   
75   C CA  . SER A 12  ? 1.0413 0.6956 0.4850 -0.0566 0.0506  -0.1780 12  SER A CA  
76   C C   . SER A 12  ? 1.0728 0.7210 0.5477 -0.0543 0.0691  -0.1949 12  SER A C   
77   O O   . SER A 12  ? 0.9972 0.6609 0.5055 -0.0523 0.0503  -0.1951 12  SER A O   
78   C CB  . SER A 12  ? 1.1124 0.7393 0.4802 -0.0789 0.0305  -0.1857 12  SER A CB  
79   O OG  . SER A 12  ? 1.2057 0.8325 0.5403 -0.0809 0.0127  -0.1682 12  SER A OG  
80   N N   . ALA A 13  ? 1.0694 0.6936 0.5360 -0.0549 0.1073  -0.2096 13  ALA A N   
81   C CA  . ALA A 13  ? 0.9788 0.5917 0.4744 -0.0518 0.1273  -0.2253 13  ALA A CA  
82   C C   . ALA A 13  ? 0.9588 0.5995 0.5300 -0.0302 0.1280  -0.2124 13  ALA A C   
83   O O   . ALA A 13  ? 0.9434 0.5758 0.5407 -0.0274 0.1359  -0.2215 13  ALA A O   
84   C CB  . ALA A 13  ? 0.9738 0.5697 0.4663 -0.0536 0.1639  -0.2352 13  ALA A CB  
85   N N   . LYS A 14  ? 0.8922 0.5624 0.4954 -0.0165 0.1196  -0.1914 14  LYS A N   
86   C CA  . LYS A 14  ? 0.8976 0.5923 0.5654 0.0020  0.1181  -0.1777 14  LYS A CA  
87   C C   . LYS A 14  ? 0.8390 0.5595 0.5261 0.0032  0.0846  -0.1637 14  LYS A C   
88   O O   . LYS A 14  ? 0.7718 0.5129 0.5037 0.0164  0.0807  -0.1496 14  LYS A O   
89   C CB  . LYS A 14  ? 0.8845 0.5943 0.5806 0.0159  0.1348  -0.1656 14  LYS A CB  
90   C CG  . LYS A 14  ? 0.9240 0.6149 0.6309 0.0208  0.1724  -0.1787 14  LYS A CG  
91   C CD  . LYS A 14  ? 0.9158 0.6278 0.6604 0.0342  0.1865  -0.1666 14  LYS A CD  
92   C CE  . LYS A 14  ? 1.0150 0.7147 0.7930 0.0437  0.2225  -0.1783 14  LYS A CE  
93   N NZ  . LYS A 14  ? 1.0780 0.7411 0.8076 0.0289  0.2506  -0.2027 14  LYS A NZ  
94   N N   . VAL A 15  ? 0.8720 0.5911 0.5273 -0.0107 0.0606  -0.1679 15  VAL A N   
95   C CA  . VAL A 15  ? 0.8288 0.5732 0.5074 -0.0100 0.0308  -0.1569 15  VAL A CA  
96   C C   . VAL A 15  ? 0.8199 0.5604 0.5200 -0.0146 0.0276  -0.1675 15  VAL A C   
97   O O   . VAL A 15  ? 0.8270 0.5491 0.4998 -0.0292 0.0251  -0.1845 15  VAL A O   
98   C CB  . VAL A 15  ? 0.7776 0.5256 0.4194 -0.0210 0.0037  -0.1541 15  VAL A CB  
99   C CG1 . VAL A 15  ? 0.7484 0.5235 0.4241 -0.0194 -0.0249 -0.1452 15  VAL A CG1 
100  C CG2 . VAL A 15  ? 0.7623 0.5099 0.3802 -0.0172 0.0086  -0.1422 15  VAL A CG2 
101  N N   . ILE A 16  ? 0.6960 0.4513 0.4417 -0.0043 0.0280  -0.1577 16  ILE A N   
102  C CA  . ILE A 16  ? 0.7708 0.5198 0.5372 -0.0094 0.0278  -0.1662 16  ILE A CA  
103  C C   . ILE A 16  ? 0.7509 0.5215 0.5339 -0.0171 0.0024  -0.1644 16  ILE A C   
104  O O   . ILE A 16  ? 0.7475 0.5132 0.5446 -0.0258 0.0012  -0.1745 16  ILE A O   
105  C CB  . ILE A 16  ? 0.7464 0.4914 0.5478 0.0041  0.0446  -0.1573 16  ILE A CB  
106  C CG1 . ILE A 16  ? 0.7434 0.5141 0.5704 0.0154  0.0361  -0.1366 16  ILE A CG1 
107  C CG2 . ILE A 16  ? 0.7683 0.4909 0.5636 0.0118  0.0706  -0.1625 16  ILE A CG2 
108  C CD1 . ILE A 16  ? 0.7512 0.5170 0.6073 0.0272  0.0476  -0.1258 16  ILE A CD1 
109  N N   . GLN A 17  ? 0.7139 0.5076 0.4990 -0.0143 -0.0164 -0.1526 17  GLN A N   
110  C CA  . GLN A 17  ? 0.7206 0.5362 0.5263 -0.0208 -0.0408 -0.1522 17  GLN A CA  
111  C C   . GLN A 17  ? 0.7133 0.5431 0.5036 -0.0189 -0.0615 -0.1419 17  GLN A C   
112  O O   . GLN A 17  ? 0.7143 0.5494 0.5037 -0.0080 -0.0562 -0.1276 17  GLN A O   
113  C CB  . GLN A 17  ? 0.7014 0.5324 0.5520 -0.0149 -0.0374 -0.1437 17  GLN A CB  
114  C CG  . GLN A 17  ? 0.6654 0.5212 0.5455 -0.0209 -0.0587 -0.1446 17  GLN A CG  
115  C CD  . GLN A 17  ? 0.7011 0.5677 0.6210 -0.0180 -0.0504 -0.1388 17  GLN A CD  
116  O OE1 . GLN A 17  ? 0.7636 0.6149 0.6899 -0.0202 -0.0331 -0.1423 17  GLN A OE1 
117  N NE2 . GLN A 17  ? 0.6140 0.5033 0.5579 -0.0136 -0.0617 -0.1299 17  GLN A NE2 
118  N N   . GLY A 18  ? 0.6866 0.5215 0.4658 -0.0299 -0.0862 -0.1487 18  GLY A N   
119  C CA  . GLY A 18  ? 0.7155 0.5595 0.4772 -0.0287 -0.1099 -0.1379 18  GLY A CA  
120  C C   . GLY A 18  ? 0.8024 0.6207 0.5005 -0.0379 -0.1128 -0.1430 18  GLY A C   
121  O O   . GLY A 18  ? 0.9030 0.6981 0.5719 -0.0482 -0.0997 -0.1588 18  GLY A O   
122  N N   . SER A 19  ? 0.8230 0.6419 0.4964 -0.0352 -0.1288 -0.1294 19  SER A N   
123  C CA  . SER A 19  ? 0.8971 0.6878 0.5016 -0.0457 -0.1325 -0.1318 19  SER A CA  
124  C C   . SER A 19  ? 0.9451 0.7334 0.5297 -0.0372 -0.1337 -0.1126 19  SER A C   
125  O O   . SER A 19  ? 0.9770 0.7854 0.5899 -0.0288 -0.1546 -0.0977 19  SER A O   
126  C CB  . SER A 19  ? 0.9043 0.6920 0.4846 -0.0614 -0.1679 -0.1392 19  SER A CB  
127  O OG  . SER A 19  ? 1.0551 0.8123 0.5604 -0.0727 -0.1748 -0.1381 19  SER A OG  
128  N N   . LEU A 20  ? 0.9752 0.7374 0.5133 -0.0400 -0.1090 -0.1139 20  LEU A N   
129  C CA  . LEU A 20  ? 1.0174 0.7714 0.5268 -0.0361 -0.1088 -0.0972 20  LEU A CA  
130  C C   . LEU A 20  ? 1.0966 0.8379 0.5599 -0.0458 -0.1450 -0.0890 20  LEU A C   
131  O O   . LEU A 20  ? 1.0899 0.8311 0.5450 -0.0400 -0.1569 -0.0706 20  LEU A O   
132  C CB  . LEU A 20  ? 0.9984 0.7264 0.4692 -0.0397 -0.0715 -0.1034 20  LEU A CB  
133  C CG  . LEU A 20  ? 0.9776 0.7166 0.4946 -0.0284 -0.0369 -0.1089 20  LEU A CG  
134  C CD1 . LEU A 20  ? 0.9853 0.6981 0.4665 -0.0335 -0.0008 -0.1182 20  LEU A CD1 
135  C CD2 . LEU A 20  ? 0.8406 0.6085 0.4108 -0.0122 -0.0377 -0.0918 20  LEU A CD2 
136  N N   . ASP A 21  ? 1.1012 0.8304 0.5338 -0.0611 -0.1644 -0.1019 21  ASP A N   
137  C CA  . ASP A 21  ? 1.2170 0.9344 0.6061 -0.0713 -0.2050 -0.0934 21  ASP A CA  
138  C C   . ASP A 21  ? 1.2444 0.9963 0.6934 -0.0596 -0.2421 -0.0795 21  ASP A C   
139  O O   . ASP A 21  ? 1.3341 1.0870 0.7722 -0.0606 -0.2713 -0.0643 21  ASP A O   
140  C CB  . ASP A 21  ? 1.2891 0.9968 0.6516 -0.0897 -0.2105 -0.1100 21  ASP A CB  
141  C CG  . ASP A 21  ? 1.3240 0.9986 0.6326 -0.1012 -0.1721 -0.1228 21  ASP A CG  
142  O OD1 . ASP A 21  ? 1.2571 0.9190 0.5542 -0.0947 -0.1404 -0.1194 21  ASP A OD1 
143  O OD2 . ASP A 21  ? 1.3327 0.9948 0.6140 -0.1168 -0.1729 -0.1369 21  ASP A OD2 
144  N N   . SER A 22  ? 1.1261 0.9122 0.6531 -0.0474 -0.2336 -0.0828 22  SER A N   
145  C CA  . SER A 22  ? 1.0637 0.8836 0.6560 -0.0361 -0.2615 -0.0724 22  SER A CA  
146  C C   . SER A 22  ? 1.0389 0.8690 0.6605 -0.0187 -0.2516 -0.0537 22  SER A C   
147  O O   . SER A 22  ? 1.0492 0.9042 0.7247 -0.0083 -0.2713 -0.0445 22  SER A O   
148  C CB  . SER A 22  ? 0.9947 0.8430 0.6528 -0.0357 -0.2560 -0.0881 22  SER A CB  
149  O OG  . SER A 22  ? 1.0817 0.9224 0.7180 -0.0531 -0.2697 -0.1057 22  SER A OG  
150  N N   . LEU A 23  ? 1.0141 0.8261 0.6047 -0.0161 -0.2209 -0.0492 23  LEU A N   
151  C CA  . LEU A 23  ? 0.9633 0.7826 0.5775 -0.0022 -0.2101 -0.0327 23  LEU A CA  
152  C C   . LEU A 23  ? 1.0446 0.8436 0.6160 -0.0021 -0.2323 -0.0137 23  LEU A C   
153  O O   . LEU A 23  ? 1.1096 0.8794 0.6137 -0.0148 -0.2444 -0.0134 23  LEU A O   
154  C CB  . LEU A 23  ? 0.9371 0.7484 0.5424 -0.0002 -0.1685 -0.0363 23  LEU A CB  
155  C CG  . LEU A 23  ? 0.9259 0.7533 0.5731 0.0023  -0.1447 -0.0508 23  LEU A CG  
156  C CD1 . LEU A 23  ? 0.9056 0.7250 0.5449 0.0057  -0.1088 -0.0510 23  LEU A CD1 
157  C CD2 . LEU A 23  ? 0.8481 0.7062 0.5640 0.0121  -0.1524 -0.0481 23  LEU A CD2 
158  N N   . PRO A 24  ? 0.9967 0.8067 0.6024 0.0110  -0.2377 0.0024  24  PRO A N   
159  C CA  . PRO A 24  ? 0.9870 0.7715 0.5489 0.0119  -0.2525 0.0224  24  PRO A CA  
160  C C   . PRO A 24  ? 1.0282 0.7811 0.5256 0.0032  -0.2220 0.0233  24  PRO A C   
161  O O   . PRO A 24  ? 0.9685 0.7257 0.4719 0.0014  -0.1871 0.0109  24  PRO A O   
162  C CB  . PRO A 24  ? 0.9827 0.7872 0.6053 0.0283  -0.2533 0.0352  24  PRO A CB  
163  C CG  . PRO A 24  ? 0.9633 0.8047 0.6602 0.0342  -0.2543 0.0223  24  PRO A CG  
164  C CD  . PRO A 24  ? 0.9332 0.7761 0.6176 0.0242  -0.2324 0.0026  24  PRO A CD  
165  N N   . GLN A 25  ? 1.0500 0.7714 0.4900 -0.0023 -0.2340 0.0386  25  GLN A N   
166  C CA  . GLN A 25  ? 1.0696 0.7601 0.4489 -0.0137 -0.2026 0.0385  25  GLN A CA  
167  C C   . GLN A 25  ? 1.0177 0.7156 0.4204 -0.0067 -0.1663 0.0379  25  GLN A C   
168  O O   . GLN A 25  ? 1.0189 0.7159 0.4145 -0.0123 -0.1325 0.0236  25  GLN A O   
169  C CB  . GLN A 25  ? 1.1877 0.8540 0.5302 -0.0188 -0.2149 0.0564  25  GLN A CB  
170  C CG  . GLN A 25  ? 1.3113 0.9440 0.5913 -0.0329 -0.1823 0.0553  25  GLN A CG  
171  C CD  . GLN A 25  ? 1.4096 1.0156 0.6542 -0.0371 -0.1936 0.0745  25  GLN A CD  
172  O OE1 . GLN A 25  ? 1.4126 1.0261 0.6861 -0.0258 -0.2203 0.0909  25  GLN A OE1 
173  N NE2 . GLN A 25  ? 1.4203 0.9933 0.6033 -0.0533 -0.1719 0.0717  25  GLN A NE2 
174  N N   . GLU A 26  ? 1.0009 0.7113 0.4442 0.0058  -0.1702 0.0523  26  GLU A N   
175  C CA  . GLU A 26  ? 0.9623 0.6844 0.4360 0.0107  -0.1358 0.0519  26  GLU A CA  
176  C C   . GLU A 26  ? 0.9175 0.6753 0.4530 0.0170  -0.1190 0.0361  26  GLU A C   
177  O O   . GLU A 26  ? 0.8972 0.6641 0.4514 0.0181  -0.0894 0.0321  26  GLU A O   
178  C CB  . GLU A 26  ? 0.9736 0.6962 0.4716 0.0205  -0.1447 0.0702  26  GLU A CB  
179  C CG  . GLU A 26  ? 1.0769 0.7591 0.5124 0.0150  -0.1604 0.0890  26  GLU A CG  
180  C CD  . GLU A 26  ? 1.0888 0.7397 0.4597 -0.0004 -0.1304 0.0874  26  GLU A CD  
181  O OE1 . GLU A 26  ? 1.0100 0.6716 0.3981 -0.0021 -0.0952 0.0786  26  GLU A OE1 
182  O OE2 . GLU A 26  ? 1.2491 0.8764 0.5751 -0.0113 -0.1376 0.0915  26  GLU A OE2 
183  N N   . VAL A 27  ? 0.9067 0.6839 0.4742 0.0204  -0.1380 0.0276  27  VAL A N   
184  C CA  . VAL A 27  ? 0.8931 0.6973 0.5100 0.0243  -0.1215 0.0131  27  VAL A CA  
185  C C   . VAL A 27  ? 0.8567 0.6500 0.4440 0.0153  -0.0995 -0.0023 27  VAL A C   
186  O O   . VAL A 27  ? 0.7908 0.5952 0.4030 0.0180  -0.0732 -0.0096 27  VAL A O   
187  C CB  . VAL A 27  ? 0.8792 0.7063 0.5424 0.0295  -0.1457 0.0084  27  VAL A CB  
188  C CG1 . VAL A 27  ? 0.7749 0.6237 0.4816 0.0317  -0.1276 -0.0056 27  VAL A CG1 
189  C CG2 . VAL A 27  ? 0.8429 0.6805 0.5423 0.0396  -0.1628 0.0222  27  VAL A CG2 
190  N N   . ARG A 28  ? 0.8885 0.6580 0.4217 0.0040  -0.1100 -0.0074 28  ARG A N   
191  C CA  . ARG A 28  ? 0.9428 0.6970 0.4448 -0.0057 -0.0857 -0.0240 28  ARG A CA  
192  C C   . ARG A 28  ? 0.8738 0.6149 0.3562 -0.0081 -0.0509 -0.0229 28  ARG A C   
193  O O   . ARG A 28  ? 0.8963 0.6427 0.3963 -0.0073 -0.0222 -0.0352 28  ARG A O   
194  C CB  . ARG A 28  ? 0.9128 0.6390 0.3516 -0.0205 -0.1041 -0.0300 28  ARG A CB  
195  C CG  . ARG A 28  ? 0.9998 0.7098 0.4110 -0.0312 -0.0788 -0.0509 28  ARG A CG  
196  C CD  . ARG A 28  ? 1.1636 0.8346 0.4916 -0.0501 -0.0890 -0.0558 28  ARG A CD  
197  N NE  . ARG A 28  ? 1.1267 0.7775 0.4256 -0.0615 -0.0587 -0.0777 28  ARG A NE  
198  C CZ  . ARG A 28  ? 1.1575 0.8012 0.4426 -0.0716 -0.0676 -0.0941 28  ARG A CZ  
199  N NH1 . ARG A 28  ? 1.1983 0.8561 0.4970 -0.0727 -0.1072 -0.0915 28  ARG A NH1 
200  N NH2 . ARG A 28  ? 1.1900 0.8178 0.4605 -0.0800 -0.0345 -0.1131 28  ARG A NH2 
201  N N   . LYS A 29  ? 0.8949 0.6185 0.3442 -0.0109 -0.0527 -0.0082 29  LYS A N   
202  C CA  . LYS A 29  ? 0.9322 0.6455 0.3682 -0.0145 -0.0182 -0.0075 29  LYS A CA  
203  C C   . LYS A 29  ? 0.8074 0.5545 0.3136 -0.0024 -0.0004 -0.0078 29  LYS A C   
204  O O   . LYS A 29  ? 0.7759 0.5262 0.2939 -0.0036 0.0310  -0.0160 29  LYS A O   
205  C CB  . LYS A 29  ? 0.9526 0.6399 0.3426 -0.0202 -0.0252 0.0101  29  LYS A CB  
206  C CG  . LYS A 29  ? 1.0354 0.6798 0.3399 -0.0361 -0.0369 0.0114  29  LYS A CG  
207  C CD  . LYS A 29  ? 1.1137 0.7345 0.3836 -0.0399 -0.0460 0.0319  29  LYS A CD  
208  C CE  . LYS A 29  ? 1.3116 0.9023 0.5249 -0.0556 -0.0532 0.0328  29  LYS A CE  
209  N NZ  . LYS A 29  ? 1.3392 0.9106 0.5190 -0.0706 -0.0129 0.0171  29  LYS A NZ  
210  N N   . PHE A 30  ? 0.8121 0.5838 0.3659 0.0087  -0.0202 0.0007  30  PHE A N   
211  C CA  . PHE A 30  ? 0.7487 0.5492 0.3620 0.0180  -0.0069 0.0012  30  PHE A CA  
212  C C   . PHE A 30  ? 0.7003 0.5160 0.3454 0.0215  0.0060  -0.0133 30  PHE A C   
213  O O   . PHE A 30  ? 0.6838 0.5128 0.3595 0.0251  0.0272  -0.0159 30  PHE A O   
214  C CB  . PHE A 30  ? 0.7256 0.5433 0.3752 0.0265  -0.0296 0.0118  30  PHE A CB  
215  C CG  . PHE A 30  ? 0.6272 0.4705 0.3298 0.0334  -0.0187 0.0125  30  PHE A CG  
216  C CD1 . PHE A 30  ? 0.6773 0.5238 0.3871 0.0318  0.0015  0.0164  30  PHE A CD1 
217  C CD2 . PHE A 30  ? 0.6430 0.5058 0.3863 0.0396  -0.0292 0.0090  30  PHE A CD2 
218  C CE1 . PHE A 30  ? 0.6142 0.4833 0.3692 0.0363  0.0077  0.0173  30  PHE A CE1 
219  C CE2 . PHE A 30  ? 0.6135 0.4951 0.3967 0.0436  -0.0208 0.0103  30  PHE A CE2 
220  C CZ  . PHE A 30  ? 0.6178 0.5028 0.4060 0.0420  -0.0041 0.0148  30  PHE A CZ  
221  N N   . VAL A 31  ? 0.7476 0.5605 0.3870 0.0203  -0.0073 -0.0225 31  VAL A N   
222  C CA  . VAL A 31  ? 0.7411 0.5630 0.4079 0.0233  0.0048  -0.0359 31  VAL A CA  
223  C C   . VAL A 31  ? 0.7236 0.5285 0.3666 0.0178  0.0335  -0.0475 31  VAL A C   
224  O O   . VAL A 31  ? 0.6521 0.4679 0.3294 0.0237  0.0546  -0.0520 31  VAL A O   
225  C CB  . VAL A 31  ? 0.7530 0.5752 0.4207 0.0215  -0.0162 -0.0435 31  VAL A CB  
226  C CG1 . VAL A 31  ? 0.7129 0.5381 0.4040 0.0236  -0.0017 -0.0571 31  VAL A CG1 
227  C CG2 . VAL A 31  ? 0.7117 0.5531 0.4127 0.0274  -0.0399 -0.0341 31  VAL A CG2 
228  N N   . GLU A 32  ? 0.8020 0.5785 0.3860 0.0059  0.0346  -0.0527 32  GLU A N   
229  C CA  . GLU A 32  ? 0.8355 0.5912 0.3926 -0.0017 0.0656  -0.0670 32  GLU A CA  
230  C C   . GLU A 32  ? 0.7891 0.5500 0.3621 0.0002  0.0943  -0.0635 32  GLU A C   
231  O O   . GLU A 32  ? 0.7781 0.5392 0.3702 0.0016  0.1238  -0.0752 32  GLU A O   
232  C CB  . GLU A 32  ? 0.8295 0.5488 0.3097 -0.0182 0.0601  -0.0726 32  GLU A CB  
233  C CG  . GLU A 32  ? 1.0036 0.7141 0.4671 -0.0238 0.0420  -0.0845 32  GLU A CG  
234  C CD  . GLU A 32  ? 1.0864 0.7571 0.4678 -0.0431 0.0398  -0.0925 32  GLU A CD  
235  O OE1 . GLU A 32  ? 1.1128 0.7624 0.4460 -0.0514 0.0427  -0.0835 32  GLU A OE1 
236  O OE2 . GLU A 32  ? 1.1037 0.7613 0.4651 -0.0514 0.0353  -0.1079 32  GLU A OE2 
237  N N   . GLY A 33  ? 0.7960 0.5613 0.3652 0.0000  0.0867  -0.0479 33  GLY A N   
238  C CA  . GLY A 33  ? 0.7652 0.5366 0.3510 -0.0005 0.1135  -0.0451 33  GLY A CA  
239  C C   . GLY A 33  ? 0.7441 0.5492 0.4035 0.0123  0.1238  -0.0467 33  GLY A C   
240  O O   . GLY A 33  ? 0.7236 0.5335 0.4062 0.0128  0.1529  -0.0553 33  GLY A O   
241  N N   . ASN A 34  ? 0.6951 0.5231 0.3926 0.0223  0.0999  -0.0384 34  ASN A N   
242  C CA  . ASN A 34  ? 0.6721 0.5287 0.4328 0.0332  0.1045  -0.0375 34  ASN A CA  
243  C C   . ASN A 34  ? 0.6456 0.5017 0.4267 0.0392  0.1132  -0.0502 34  ASN A C   
244  O O   . ASN A 34  ? 0.6621 0.5353 0.4912 0.0475  0.1248  -0.0515 34  ASN A O   
245  C CB  . ASN A 34  ? 0.6247 0.4997 0.4106 0.0390  0.0785  -0.0252 34  ASN A CB  
246  C CG  . ASN A 34  ? 0.6355 0.5136 0.4152 0.0350  0.0747  -0.0130 34  ASN A CG  
247  O OD1 . ASN A 34  ? 0.6723 0.5656 0.4805 0.0353  0.0865  -0.0094 34  ASN A OD1 
248  N ND2 . ASN A 34  ? 0.6785 0.5417 0.4230 0.0311  0.0576  -0.0065 34  ASN A ND2 
249  N N   . ALA A 35  ? 0.6994 0.5354 0.4463 0.0348  0.1064  -0.0593 35  ALA A N   
250  C CA  . ALA A 35  ? 0.7679 0.5962 0.5275 0.0383  0.1199  -0.0735 35  ALA A CA  
251  C C   . ALA A 35  ? 0.7723 0.5914 0.5342 0.0364  0.1552  -0.0849 35  ALA A C   
252  O O   . ALA A 35  ? 0.7691 0.5957 0.5746 0.0458  0.1711  -0.0913 35  ALA A O   
253  C CB  . ALA A 35  ? 0.7259 0.5319 0.4426 0.0302  0.1071  -0.0829 35  ALA A CB  
254  N N   . GLN A 36  ? 0.7830 0.5843 0.4994 0.0242  0.1688  -0.0871 36  GLN A N   
255  C CA  . GLN A 36  ? 0.7865 0.5782 0.5048 0.0200  0.2073  -0.0992 36  GLN A CA  
256  C C   . GLN A 36  ? 0.7245 0.5488 0.5114 0.0305  0.2195  -0.0928 36  GLN A C   
257  O O   . GLN A 36  ? 0.7479 0.5763 0.5713 0.0347  0.2488  -0.1039 36  GLN A O   
258  C CB  . GLN A 36  ? 0.8770 0.6392 0.5243 0.0021  0.2180  -0.1008 36  GLN A CB  
259  C CG  . GLN A 36  ? 1.0801 0.8277 0.7213 -0.0061 0.2627  -0.1152 36  GLN A CG  
260  C CD  . GLN A 36  ? 1.2318 0.9470 0.7971 -0.0257 0.2724  -0.1135 36  GLN A CD  
261  O OE1 . GLN A 36  ? 1.2765 0.9820 0.7979 -0.0311 0.2425  -0.0993 36  GLN A OE1 
262  N NE2 . GLN A 36  ? 1.1889 0.8873 0.7424 -0.0366 0.3127  -0.1267 36  GLN A NE2 
263  N N   . LEU A 37  ? 0.7094 0.5571 0.5174 0.0343  0.1971  -0.0757 37  LEU A N   
264  C CA  . LEU A 37  ? 0.7187 0.5984 0.5894 0.0418  0.2039  -0.0689 37  LEU A CA  
265  C C   . LEU A 37  ? 0.7043 0.6072 0.6364 0.0577  0.1914  -0.0658 37  LEU A C   
266  O O   . LEU A 37  ? 0.6555 0.5772 0.6442 0.0660  0.2065  -0.0686 37  LEU A O   
267  C CB  . LEU A 37  ? 0.7386 0.6293 0.6009 0.0368  0.1863  -0.0530 37  LEU A CB  
268  C CG  . LEU A 37  ? 0.6733 0.5992 0.5984 0.0429  0.1831  -0.0439 37  LEU A CG  
269  C CD1 . LEU A 37  ? 0.6739 0.6096 0.6304 0.0395  0.2166  -0.0522 37  LEU A CD1 
270  C CD2 . LEU A 37  ? 0.6971 0.6280 0.6068 0.0377  0.1617  -0.0293 37  LEU A CD2 
271  N N   . CYS A 38  ? 0.6650 0.5659 0.5877 0.0618  0.1635  -0.0595 38  CYS A N   
272  C CA  . CYS A 38  ? 0.6815 0.5991 0.6530 0.0748  0.1491  -0.0538 38  CYS A CA  
273  C C   . CYS A 38  ? 0.6824 0.5851 0.6654 0.0821  0.1614  -0.0660 38  CYS A C   
274  O O   . CYS A 38  ? 0.6992 0.6134 0.7299 0.0944  0.1564  -0.0617 38  CYS A O   
275  C CB  . CYS A 38  ? 0.6202 0.5403 0.5771 0.0741  0.1177  -0.0423 38  CYS A CB  
276  S SG  . CYS A 38  ? 0.6373 0.5715 0.5835 0.0665  0.1033  -0.0284 38  CYS A SG  
277  N N   A GLN A 39  ? 0.6956 0.5702 0.6337 0.0741  0.1764  -0.0807 39  GLN A N   
278  N N   B GLN A 39  ? 0.7059 0.5805 0.6439 0.0741  0.1762  -0.0806 39  GLN A N   
279  C CA  A GLN A 39  ? 0.7530 0.6074 0.6946 0.0783  0.1917  -0.0954 39  GLN A CA  
280  C CA  B GLN A 39  ? 0.7714 0.6255 0.7122 0.0781  0.1917  -0.0954 39  GLN A CA  
281  C C   A GLN A 39  ? 0.7430 0.5967 0.7007 0.0865  0.1693  -0.0896 39  GLN A C   
282  C C   B GLN A 39  ? 0.7637 0.6172 0.7211 0.0864  0.1695  -0.0898 39  GLN A C   
283  O O   A GLN A 39  ? 0.7685 0.6286 0.7752 0.0997  0.1723  -0.0872 39  GLN A O   
284  O O   B GLN A 39  ? 0.7372 0.5970 0.7436 0.0997  0.1727  -0.0875 39  GLN A O   
285  C CB  A GLN A 39  ? 0.7214 0.5831 0.7148 0.0875  0.2219  -0.1034 39  GLN A CB  
286  C CB  B GLN A 39  ? 0.7210 0.5822 0.7131 0.0872  0.2222  -0.1036 39  GLN A CB  
287  C CG  A GLN A 39  ? 0.7480 0.6019 0.7209 0.0766  0.2539  -0.1150 39  GLN A CG  
288  C CG  B GLN A 39  ? 0.7429 0.6057 0.7250 0.0777  0.2492  -0.1102 39  GLN A CG  
289  C CD  A GLN A 39  ? 0.7479 0.5621 0.6560 0.0629  0.2729  -0.1339 39  GLN A CD  
290  C CD  B GLN A 39  ? 0.6624 0.5353 0.7055 0.0870  0.2819  -0.1203 39  GLN A CD  
291  O OE1 A GLN A 39  ? 0.7669 0.5643 0.6096 0.0476  0.2654  -0.1336 39  GLN A OE1 
292  O OE1 B GLN A 39  ? 0.7061 0.5620 0.7638 0.0932  0.3009  -0.1341 39  GLN A OE1 
293  N NE2 A GLN A 39  ? 0.7592 0.5562 0.6841 0.0679  0.2969  -0.1503 39  GLN A NE2 
294  N NE2 B GLN A 39  ? 0.6093 0.5102 0.6927 0.0879  0.2893  -0.1141 39  GLN A NE2 
295  N N   . PRO A 40  ? 0.7703 0.6157 0.6905 0.0790  0.1470  -0.0870 40  PRO A N   
296  C CA  . PRO A 40  ? 0.7609 0.6008 0.6921 0.0838  0.1310  -0.0845 40  PRO A CA  
297  C C   . PRO A 40  ? 0.7772 0.5877 0.6888 0.0804  0.1454  -0.1024 40  PRO A C   
298  O O   . PRO A 40  ? 0.7608 0.5528 0.6314 0.0695  0.1587  -0.1166 40  PRO A O   
299  C CB  . PRO A 40  ? 0.6948 0.5405 0.5977 0.0753  0.1046  -0.0763 40  PRO A CB  
300  C CG  . PRO A 40  ? 0.7095 0.5469 0.5671 0.0637  0.1093  -0.0824 40  PRO A CG  
301  C CD  . PRO A 40  ? 0.7075 0.5487 0.5773 0.0659  0.1344  -0.0850 40  PRO A CD  
302  N N   . GLU A 41  ? 0.7377 0.5404 0.6757 0.0887  0.1426  -0.1016 41  GLU A N   
303  C CA  . GLU A 41  ? 0.7537 0.5258 0.6751 0.0851  0.1565  -0.1191 41  GLU A CA  
304  C C   . GLU A 41  ? 0.7642 0.5243 0.6386 0.0695  0.1405  -0.1262 41  GLU A C   
305  O O   . GLU A 41  ? 0.7921 0.5275 0.6330 0.0591  0.1520  -0.1443 41  GLU A O   
306  C CB  . GLU A 41  ? 0.7679 0.5315 0.7310 0.0985  0.1579  -0.1146 41  GLU A CB  
307  C CG  . GLU A 41  ? 0.8754 0.6049 0.8313 0.0974  0.1801  -0.1339 41  GLU A CG  
308  C CD  . GLU A 41  ? 0.9829 0.6988 0.9751 0.1100  0.1780  -0.1271 41  GLU A CD  
309  O OE1 . GLU A 41  ? 0.9754 0.7059 0.9867 0.1160  0.1555  -0.1076 41  GLU A OE1 
310  O OE2 . GLU A 41  ? 1.0856 0.7730 1.0842 0.1132  0.1993  -0.1412 41  GLU A OE2 
311  N N   . TYR A 42  ? 0.7545 0.5317 0.6276 0.0668  0.1145  -0.1134 42  TYR A N   
312  C CA  . TYR A 42  ? 0.7433 0.5154 0.5837 0.0533  0.0969  -0.1191 42  TYR A CA  
313  C C   . TYR A 42  ? 0.7140 0.5093 0.5462 0.0500  0.0762  -0.1065 42  TYR A C   
314  O O   . TYR A 42  ? 0.6834 0.4981 0.5392 0.0581  0.0727  -0.0918 42  TYR A O   
315  C CB  . TYR A 42  ? 0.7245 0.4887 0.5805 0.0530  0.0885  -0.1194 42  TYR A CB  
316  C CG  . TYR A 42  ? 0.7863 0.5245 0.6550 0.0580  0.1082  -0.1293 42  TYR A CG  
317  C CD1 . TYR A 42  ? 0.8460 0.5582 0.6866 0.0484  0.1228  -0.1500 42  TYR A CD1 
318  C CD2 . TYR A 42  ? 0.7751 0.5119 0.6819 0.0718  0.1114  -0.1176 42  TYR A CD2 
319  C CE1 . TYR A 42  ? 0.8910 0.5762 0.7445 0.0532  0.1431  -0.1601 42  TYR A CE1 
320  C CE2 . TYR A 42  ? 0.8509 0.5612 0.7721 0.0781  0.1289  -0.1252 42  TYR A CE2 
321  C CZ  . TYR A 42  ? 0.8573 0.5417 0.7535 0.0692  0.1462  -0.1471 42  TYR A CZ  
322  O OH  . TYR A 42  ? 0.9973 0.6522 0.9093 0.0757  0.1659  -0.1557 42  TYR A OH  
323  N N   . ILE A 43  ? 0.7151 0.5073 0.5146 0.0378  0.0615  -0.1124 43  ILE A N   
324  C CA  . ILE A 43  ? 0.7231 0.5340 0.5166 0.0351  0.0401  -0.1013 43  ILE A CA  
325  C C   . ILE A 43  ? 0.7063 0.5212 0.5046 0.0281  0.0204  -0.1046 43  ILE A C   
326  O O   . ILE A 43  ? 0.6673 0.4681 0.4452 0.0180  0.0172  -0.1186 43  ILE A O   
327  C CB  . ILE A 43  ? 0.6702 0.4745 0.4216 0.0276  0.0387  -0.1029 43  ILE A CB  
328  C CG1 . ILE A 43  ? 0.7066 0.5064 0.4563 0.0325  0.0635  -0.1021 43  ILE A CG1 
329  C CG2 . ILE A 43  ? 0.5802 0.4016 0.3300 0.0268  0.0155  -0.0896 43  ILE A CG2 
330  C CD1 . ILE A 43  ? 0.7254 0.5129 0.4274 0.0231  0.0666  -0.1034 43  ILE A CD1 
331  N N   . HIS A 44  ? 0.5996 0.4332 0.4256 0.0322  0.0087  -0.0930 44  HIS A N   
332  C CA  . HIS A 44  ? 0.6126 0.4527 0.4537 0.0261  -0.0055 -0.0963 44  HIS A CA  
333  C C   . HIS A 44  ? 0.5977 0.4570 0.4433 0.0252  -0.0246 -0.0878 44  HIS A C   
334  O O   . HIS A 44  ? 0.5905 0.4622 0.4525 0.0317  -0.0247 -0.0752 44  HIS A O   
335  C CB  . HIS A 44  ? 0.5282 0.3676 0.3987 0.0303  0.0021  -0.0918 44  HIS A CB  
336  C CG  . HIS A 44  ? 0.6387 0.4835 0.5264 0.0224  -0.0072 -0.0959 44  HIS A CG  
337  N ND1 . HIS A 44  ? 0.6829 0.5132 0.5727 0.0144  -0.0028 -0.1085 44  HIS A ND1 
338  C CD2 . HIS A 44  ? 0.6400 0.5022 0.5463 0.0205  -0.0179 -0.0905 44  HIS A CD2 
339  C CE1 . HIS A 44  ? 0.5610 0.4014 0.4710 0.0072  -0.0102 -0.1108 44  HIS A CE1 
340  N NE2 . HIS A 44  ? 0.6255 0.4855 0.5470 0.0112  -0.0189 -0.1003 44  HIS A NE2 
341  N N   . ILE A 45  ? 0.5754 0.4361 0.4074 0.0170  -0.0418 -0.0946 45  ILE A N   
342  C CA  . ILE A 45  ? 0.6141 0.4919 0.4555 0.0175  -0.0624 -0.0866 45  ILE A CA  
343  C C   . ILE A 45  ? 0.6156 0.5081 0.4977 0.0150  -0.0688 -0.0899 45  ILE A C   
344  O O   . ILE A 45  ? 0.6153 0.5070 0.5044 0.0062  -0.0749 -0.1026 45  ILE A O   
345  C CB  . ILE A 45  ? 0.5987 0.4705 0.4072 0.0103  -0.0818 -0.0902 45  ILE A CB  
346  C CG1 . ILE A 45  ? 0.6320 0.4828 0.3934 0.0091  -0.0695 -0.0902 45  ILE A CG1 
347  C CG2 . ILE A 45  ? 0.5892 0.4771 0.4113 0.0139  -0.1041 -0.0787 45  ILE A CG2 
348  C CD1 . ILE A 45  ? 0.7240 0.5610 0.4398 -0.0012 -0.0879 -0.0941 45  ILE A CD1 
349  N N   . CYS A 46  ? 0.5681 0.4730 0.4764 0.0209  -0.0658 -0.0800 46  CYS A N   
350  C CA  . CYS A 46  ? 0.5282 0.4435 0.4736 0.0172  -0.0649 -0.0842 46  CYS A CA  
351  C C   . CYS A 46  ? 0.5292 0.4613 0.4980 0.0131  -0.0855 -0.0894 46  CYS A C   
352  O O   . CYS A 46  ? 0.5804 0.5192 0.5430 0.0172  -0.1025 -0.0825 46  CYS A O   
353  C CB  . CYS A 46  ? 0.4867 0.4069 0.4476 0.0226  -0.0546 -0.0732 46  CYS A CB  
354  S SG  . CYS A 46  ? 0.5588 0.4635 0.5015 0.0276  -0.0356 -0.0653 46  CYS A SG  
355  N N   . ASP A 47  ? 0.5392 0.4775 0.5371 0.0047  -0.0845 -0.1014 47  ASP A N   
356  C CA  . ASP A 47  ? 0.5759 0.5352 0.6106 0.0008  -0.1031 -0.1078 47  ASP A CA  
357  C C   . ASP A 47  ? 0.4894 0.4627 0.5717 0.0002  -0.0927 -0.1093 47  ASP A C   
358  O O   . ASP A 47  ? 0.4886 0.4826 0.6128 -0.0015 -0.1059 -0.1147 47  ASP A O   
359  C CB  . ASP A 47  ? 0.5200 0.4786 0.5560 -0.0115 -0.1121 -0.1240 47  ASP A CB  
360  C CG  . ASP A 47  ? 0.5546 0.5024 0.6012 -0.0208 -0.0897 -0.1351 47  ASP A CG  
361  O OD1 . ASP A 47  ? 0.5811 0.5188 0.6269 -0.0174 -0.0685 -0.1289 47  ASP A OD1 
362  O OD2 . ASP A 47  ? 0.6225 0.5698 0.6757 -0.0326 -0.0943 -0.1499 47  ASP A OD2 
363  N N   . GLY A 48  ? 0.5164 0.4778 0.5934 0.0006  -0.0694 -0.1050 48  GLY A N   
364  C CA  . GLY A 48  ? 0.5465 0.5149 0.6588 -0.0025 -0.0554 -0.1071 48  GLY A CA  
365  C C   . GLY A 48  ? 0.5439 0.5150 0.6873 -0.0158 -0.0449 -0.1229 48  GLY A C   
366  O O   . GLY A 48  ? 0.4863 0.4614 0.6591 -0.0207 -0.0295 -0.1268 48  GLY A O   
367  N N   . SER A 49  ? 0.5335 0.5005 0.6703 -0.0234 -0.0502 -0.1332 49  SER A N   
368  C CA  . SER A 49  ? 0.5595 0.5292 0.7277 -0.0381 -0.0400 -0.1495 49  SER A CA  
369  C C   . SER A 49  ? 0.6001 0.5440 0.7528 -0.0456 -0.0108 -0.1490 49  SER A C   
370  O O   . SER A 49  ? 0.5902 0.5124 0.7032 -0.0396 -0.0027 -0.1365 49  SER A O   
371  C CB  . SER A 49  ? 0.5413 0.5087 0.6999 -0.0460 -0.0526 -0.1610 49  SER A CB  
372  O OG  . SER A 49  ? 0.5680 0.5059 0.6770 -0.0449 -0.0430 -0.1569 49  SER A OG  
373  N N   . GLU A 50  ? 0.5772 0.5228 0.7625 -0.0599 0.0045  -0.1624 50  GLU A N   
374  C CA  . GLU A 50  ? 0.6624 0.5777 0.8272 -0.0703 0.0320  -0.1622 50  GLU A CA  
375  C C   . GLU A 50  ? 0.6846 0.5716 0.8125 -0.0743 0.0354  -0.1627 50  GLU A C   
376  O O   . GLU A 50  ? 0.6527 0.5081 0.7474 -0.0765 0.0517  -0.1543 50  GLU A O   
377  C CB  . GLU A 50  ? 0.6782 0.6006 0.8872 -0.0867 0.0513  -0.1777 50  GLU A CB  
378  C CG  . GLU A 50  ? 0.7283 0.6670 0.9677 -0.0836 0.0588  -0.1763 50  GLU A CG  
379  C CD  . GLU A 50  ? 0.8903 0.8327 1.1733 -0.1010 0.0846  -0.1932 50  GLU A CD  
380  O OE1 . GLU A 50  ? 0.8866 0.8273 1.1868 -0.1153 0.0918  -0.2073 50  GLU A OE1 
381  O OE2 . GLU A 50  ? 0.8931 0.8387 1.1934 -0.1016 0.0999  -0.1935 50  GLU A OE2 
382  N N   . GLU A 51  ? 0.7195 0.6148 0.8512 -0.0756 0.0199  -0.1721 51  GLU A N   
383  C CA  . GLU A 51  ? 0.7154 0.5817 0.8110 -0.0777 0.0239  -0.1732 51  GLU A CA  
384  C C   . GLU A 51  ? 0.7544 0.6048 0.8083 -0.0614 0.0213  -0.1556 51  GLU A C   
385  O O   . GLU A 51  ? 0.7900 0.6094 0.8159 -0.0602 0.0344  -0.1487 51  GLU A O   
386  C CB  . GLU A 51  ? 0.7020 0.5803 0.8068 -0.0839 0.0070  -0.1884 51  GLU A CB  
387  C CG  . GLU A 51  ? 0.8551 0.7472 1.0036 -0.1027 0.0100  -0.2082 51  GLU A CG  
388  C CD  . GLU A 51  ? 0.8806 0.8131 1.0831 -0.1023 -0.0017 -0.2121 51  GLU A CD  
389  O OE1 . GLU A 51  ? 0.7748 0.7223 0.9767 -0.0872 -0.0138 -0.1990 51  GLU A OE1 
390  O OE2 . GLU A 51  ? 0.9225 0.8716 1.1716 -0.1172 0.0019  -0.2285 51  GLU A OE2 
391  N N   . GLU A 52  ? 0.6888 0.5599 0.7406 -0.0488 0.0041  -0.1479 52  GLU A N   
392  C CA  . GLU A 52  ? 0.6714 0.5319 0.6905 -0.0342 0.0029  -0.1321 52  GLU A CA  
393  C C   . GLU A 52  ? 0.6929 0.5395 0.7032 -0.0316 0.0169  -0.1186 52  GLU A C   
394  O O   . GLU A 52  ? 0.6656 0.4898 0.6505 -0.0256 0.0234  -0.1087 52  GLU A O   
395  C CB  . GLU A 52  ? 0.5846 0.4690 0.6046 -0.0241 -0.0161 -0.1266 52  GLU A CB  
396  C CG  . GLU A 52  ? 0.5572 0.4385 0.5562 -0.0108 -0.0148 -0.1096 52  GLU A CG  
397  C CD  . GLU A 52  ? 0.5923 0.4939 0.5917 -0.0029 -0.0318 -0.1041 52  GLU A CD  
398  O OE1 . GLU A 52  ? 0.5417 0.4430 0.5229 -0.0013 -0.0426 -0.1073 52  GLU A OE1 
399  O OE2 . GLU A 52  ? 0.5614 0.4760 0.5766 0.0006  -0.0334 -0.0968 52  GLU A OE2 
400  N N   . TYR A 53  ? 0.6674 0.5258 0.6989 -0.0365 0.0213  -0.1184 53  TYR A N   
401  C CA  . TYR A 53  ? 0.6720 0.5139 0.6892 -0.0379 0.0346  -0.1071 53  TYR A CA  
402  C C   . TYR A 53  ? 0.6613 0.4687 0.6588 -0.0476 0.0503  -0.1070 53  TYR A C   
403  O O   . TYR A 53  ? 0.6366 0.4212 0.6056 -0.0437 0.0539  -0.0927 53  TYR A O   
404  C CB  . TYR A 53  ? 0.6206 0.4784 0.6653 -0.0447 0.0408  -0.1116 53  TYR A CB  
405  C CG  . TYR A 53  ? 0.6526 0.4928 0.6771 -0.0486 0.0540  -0.1013 53  TYR A CG  
406  C CD1 . TYR A 53  ? 0.6405 0.4779 0.6402 -0.0380 0.0465  -0.0853 53  TYR A CD1 
407  C CD2 . TYR A 53  ? 0.6518 0.4773 0.6808 -0.0650 0.0746  -0.1085 53  TYR A CD2 
408  C CE1 . TYR A 53  ? 0.6496 0.4702 0.6274 -0.0437 0.0559  -0.0763 53  TYR A CE1 
409  C CE2 . TYR A 53  ? 0.6364 0.4414 0.6385 -0.0713 0.0865  -0.0996 53  TYR A CE2 
410  C CZ  . TYR A 53  ? 0.6632 0.4659 0.6388 -0.0607 0.0754  -0.0833 53  TYR A CZ  
411  O OH  . TYR A 53  ? 0.7148 0.4963 0.6604 -0.0691 0.0845  -0.0749 53  TYR A OH  
412  N N   . GLY A 54  ? 0.6854 0.4875 0.6981 -0.0605 0.0583  -0.1222 54  GLY A N   
413  C CA  . GLY A 54  ? 0.7407 0.5052 0.7324 -0.0706 0.0740  -0.1220 54  GLY A CA  
414  C C   . GLY A 54  ? 0.7873 0.5296 0.7517 -0.0591 0.0692  -0.1129 54  GLY A C   
415  O O   . GLY A 54  ? 0.7538 0.4652 0.6917 -0.0572 0.0753  -0.0992 54  GLY A O   
416  N N   . ARG A 55  ? 0.7584 0.5148 0.7291 -0.0517 0.0579  -0.1203 55  ARG A N   
417  C CA  . ARG A 55  ? 0.7702 0.5059 0.7198 -0.0406 0.0570  -0.1145 55  ARG A CA  
418  C C   . ARG A 55  ? 0.7673 0.5036 0.7031 -0.0244 0.0510  -0.0949 55  ARG A C   
419  O O   . ARG A 55  ? 0.7836 0.4952 0.7049 -0.0162 0.0544  -0.0846 55  ARG A O   
420  C CB  . ARG A 55  ? 0.8121 0.5619 0.7665 -0.0386 0.0480  -0.1285 55  ARG A CB  
421  C CG  . ARG A 55  ? 0.9201 0.6705 0.8895 -0.0558 0.0507  -0.1491 55  ARG A CG  
422  C CD  . ARG A 55  ? 1.0763 0.8284 1.0376 -0.0558 0.0428  -0.1623 55  ARG A CD  
423  N NE  . ARG A 55  ? 1.1848 0.9026 1.1230 -0.0493 0.0544  -0.1604 55  ARG A NE  
424  C CZ  . ARG A 55  ? 1.1476 0.8332 1.0807 -0.0587 0.0687  -0.1687 55  ARG A CZ  
425  N NH1 . ARG A 55  ? 1.1473 0.8303 1.0951 -0.0769 0.0743  -0.1805 55  ARG A NH1 
426  N NH2 . ARG A 55  ? 1.0906 0.7448 1.0065 -0.0497 0.0792  -0.1657 55  ARG A NH2 
427  N N   . LEU A 56  ? 0.7135 0.4778 0.6570 -0.0198 0.0418  -0.0894 56  LEU A N   
428  C CA  . LEU A 56  ? 0.6831 0.4506 0.6162 -0.0070 0.0359  -0.0719 56  LEU A CA  
429  C C   . LEU A 56  ? 0.7355 0.4765 0.6520 -0.0103 0.0416  -0.0578 56  LEU A C   
430  O O   . LEU A 56  ? 0.7407 0.4687 0.6467 0.0002  0.0378  -0.0438 56  LEU A O   
431  C CB  . LEU A 56  ? 0.6734 0.4724 0.6175 -0.0046 0.0269  -0.0703 56  LEU A CB  
432  C CG  . LEU A 56  ? 0.6905 0.4983 0.6272 0.0072  0.0199  -0.0548 56  LEU A CG  
433  C CD1 . LEU A 56  ? 0.6852 0.4995 0.6205 0.0194  0.0156  -0.0552 56  LEU A CD1 
434  C CD2 . LEU A 56  ? 0.6682 0.4986 0.6139 0.0052  0.0151  -0.0532 56  LEU A CD2 
435  N N   . LEU A 57  ? 0.7181 0.4501 0.6321 -0.0257 0.0506  -0.0615 57  LEU A N   
436  C CA  . LEU A 57  ? 0.7773 0.4775 0.6656 -0.0327 0.0565  -0.0483 57  LEU A CA  
437  C C   . LEU A 57  ? 0.8270 0.4905 0.6999 -0.0306 0.0603  -0.0426 57  LEU A C   
438  O O   . LEU A 57  ? 0.8790 0.5191 0.7311 -0.0254 0.0548  -0.0244 57  LEU A O   
439  C CB  . LEU A 57  ? 0.7641 0.4580 0.6515 -0.0526 0.0710  -0.0573 57  LEU A CB  
440  C CG  . LEU A 57  ? 0.7208 0.4428 0.6217 -0.0554 0.0703  -0.0605 57  LEU A CG  
441  C CD1 . LEU A 57  ? 0.7438 0.4613 0.6552 -0.0749 0.0893  -0.0748 57  LEU A CD1 
442  C CD2 . LEU A 57  ? 0.6458 0.3609 0.5209 -0.0517 0.0629  -0.0427 57  LEU A CD2 
443  N N   . ALA A 58  ? 0.8322 0.4886 0.7156 -0.0349 0.0684  -0.0575 58  ALA A N   
444  C CA  . ALA A 58  ? 0.8991 0.5170 0.7693 -0.0328 0.0742  -0.0534 58  ALA A CA  
445  C C   . ALA A 58  ? 0.8663 0.4842 0.7391 -0.0113 0.0635  -0.0411 58  ALA A C   
446  O O   . ALA A 58  ? 0.8805 0.4667 0.7401 -0.0047 0.0618  -0.0256 58  ALA A O   
447  C CB  . ALA A 58  ? 0.8451 0.4579 0.7278 -0.0428 0.0853  -0.0746 58  ALA A CB  
448  N N   . HIS A 59  ? 0.8064 0.4584 0.6974 -0.0004 0.0564  -0.0475 59  HIS A N   
449  C CA  . HIS A 59  ? 0.8149 0.4705 0.7135 0.0191  0.0497  -0.0378 59  HIS A CA  
450  C C   . HIS A 59  ? 0.8851 0.5390 0.7774 0.0267  0.0380  -0.0151 59  HIS A C   
451  O O   . HIS A 59  ? 0.9027 0.5381 0.7976 0.0390  0.0337  -0.0015 59  HIS A O   
452  C CB  . HIS A 59  ? 0.7980 0.4895 0.7109 0.0256  0.0460  -0.0486 59  HIS A CB  
453  C CG  . HIS A 59  ? 0.8714 0.5679 0.7954 0.0436  0.0442  -0.0424 59  HIS A CG  
454  N ND1 . HIS A 59  ? 0.8985 0.6261 0.8312 0.0514  0.0378  -0.0400 59  HIS A ND1 
455  C CD2 . HIS A 59  ? 0.9091 0.5827 0.8406 0.0553  0.0502  -0.0387 59  HIS A CD2 
456  C CE1 . HIS A 59  ? 0.9193 0.6449 0.8654 0.0660  0.0411  -0.0363 59  HIS A CE1 
457  N NE2 . HIS A 59  ? 0.9760 0.6699 0.9240 0.0695  0.0484  -0.0355 59  HIS A NE2 
458  N N   . MET A 60  ? 0.8503 0.5229 0.7359 0.0190  0.0320  -0.0110 60  MET A N   
459  C CA  . MET A 60  ? 0.8195 0.4895 0.6942 0.0223  0.0195  0.0093  60  MET A CA  
460  C C   . MET A 60  ? 0.8532 0.4793 0.7021 0.0163  0.0189  0.0233  60  MET A C   
461  O O   . MET A 60  ? 0.8850 0.4998 0.7288 0.0251  0.0049  0.0429  60  MET A O   
462  C CB  . MET A 60  ? 0.7740 0.4668 0.6425 0.0120  0.0169  0.0078  60  MET A CB  
463  C CG  . MET A 60  ? 0.7506 0.4833 0.6406 0.0211  0.0117  0.0024  60  MET A CG  
464  S SD  . MET A 60  ? 0.6394 0.3929 0.5226 0.0107  0.0084  0.0034  60  MET A SD  
465  C CE  . MET A 60  ? 0.6714 0.4300 0.5624 -0.0027 0.0222  -0.0174 60  MET A CE  
466  N N   . GLN A 61  ? 0.8373 0.4373 0.6699 0.0005  0.0332  0.0143  61  GLN A N   
467  C CA  . GLN A 61  ? 0.9174 0.4685 0.7191 -0.0073 0.0348  0.0279  61  GLN A CA  
468  C C   . GLN A 61  ? 1.0050 0.5308 0.8161 0.0088  0.0318  0.0363  61  GLN A C   
469  O O   . GLN A 61  ? 0.9457 0.4365 0.7369 0.0119  0.0221  0.0569  61  GLN A O   
470  C CB  . GLN A 61  ? 0.9363 0.4664 0.7212 -0.0300 0.0549  0.0137  61  GLN A CB  
471  C CG  . GLN A 61  ? 0.9248 0.3999 0.6674 -0.0435 0.0596  0.0278  61  GLN A CG  
472  C CD  . GLN A 61  ? 1.0312 0.4873 0.7619 -0.0679 0.0839  0.0109  61  GLN A CD  
473  O OE1 . GLN A 61  ? 1.0246 0.5038 0.7853 -0.0713 0.0956  -0.0112 61  GLN A OE1 
474  N NE2 . GLN A 61  ? 0.9647 0.3782 0.6511 -0.0864 0.0916  0.0210  61  GLN A NE2 
475  N N   . GLU A 62  ? 1.0243 0.5648 0.8643 0.0188  0.0396  0.0207  62  GLU A N   
476  C CA  . GLU A 62  ? 1.0251 0.5417 0.8789 0.0350  0.0403  0.0260  62  GLU A CA  
477  C C   . GLU A 62  ? 0.9967 0.5315 0.8741 0.0571  0.0233  0.0423  62  GLU A C   
478  O O   . GLU A 62  ? 1.0075 0.5165 0.8945 0.0714  0.0178  0.0563  62  GLU A O   
479  C CB  . GLU A 62  ? 1.0067 0.5301 0.8793 0.0357  0.0567  0.0016  62  GLU A CB  
480  C CG  . GLU A 62  ? 0.9713 0.4754 0.8282 0.0141  0.0730  -0.0157 62  GLU A CG  
481  C CD  . GLU A 62  ? 0.9373 0.4604 0.8115 0.0113  0.0836  -0.0418 62  GLU A CD  
482  O OE1 . GLU A 62  ? 0.9400 0.4869 0.8323 0.0255  0.0802  -0.0462 62  GLU A OE1 
483  O OE2 . GLU A 62  ? 0.9179 0.4314 0.7864 -0.0067 0.0952  -0.0583 62  GLU A OE2 
484  N N   . GLU A 63  ? 0.9142 0.4927 0.8047 0.0601  0.0150  0.0407  63  GLU A N   
485  C CA  . GLU A 63  ? 0.9539 0.5547 0.8709 0.0785  -0.0003 0.0546  63  GLU A CA  
486  C C   . GLU A 63  ? 0.9546 0.5461 0.8541 0.0766  -0.0222 0.0793  63  GLU A C   
487  O O   . GLU A 63  ? 0.9283 0.5414 0.8520 0.0899  -0.0383 0.0917  63  GLU A O   
488  C CB  . GLU A 63  ? 0.9266 0.5756 0.8627 0.0808  0.0015  0.0420  63  GLU A CB  
489  C CG  . GLU A 63  ? 0.9926 0.6514 0.9436 0.0838  0.0193  0.0195  63  GLU A CG  
490  C CD  . GLU A 63  ? 1.0554 0.7084 1.0377 0.1031  0.0252  0.0195  63  GLU A CD  
491  O OE1 . GLU A 63  ? 1.1148 0.7720 1.1196 0.1172  0.0129  0.0368  63  GLU A OE1 
492  O OE2 . GLU A 63  ? 1.0935 0.7376 1.0796 0.1035  0.0424  0.0014  63  GLU A OE2 
493  N N   . GLY A 64  ? 0.9681 0.5276 0.8253 0.0587  -0.0227 0.0858  64  GLY A N   
494  C CA  . GLY A 64  ? 0.9536 0.5001 0.7825 0.0522  -0.0434 0.1079  64  GLY A CA  
495  C C   . GLY A 64  ? 0.9223 0.5057 0.7476 0.0444  -0.0514 0.1064  64  GLY A C   
496  O O   . GLY A 64  ? 0.9560 0.5330 0.7605 0.0397  -0.0712 0.1244  64  GLY A O   
497  N N   . VAL A 65  ? 0.8976 0.5170 0.7403 0.0421  -0.0378 0.0860  65  VAL A N   
498  C CA  . VAL A 65  ? 0.8641 0.5173 0.7069 0.0364  -0.0443 0.0845  65  VAL A CA  
499  C C   . VAL A 65  ? 0.9148 0.5486 0.7129 0.0129  -0.0410 0.0850  65  VAL A C   
500  O O   . VAL A 65  ? 0.9415 0.5796 0.7217 0.0056  -0.0543 0.0952  65  VAL A O   
501  C CB  . VAL A 65  ? 0.8119 0.5039 0.6838 0.0412  -0.0315 0.0642  65  VAL A CB  
502  C CG1 . VAL A 65  ? 0.8000 0.5219 0.6702 0.0346  -0.0366 0.0630  65  VAL A CG1 
503  C CG2 . VAL A 65  ? 0.8126 0.5207 0.7235 0.0620  -0.0317 0.0628  65  VAL A CG2 
504  N N   . ILE A 66  ? 0.9324 0.5442 0.7126 -0.0007 -0.0217 0.0726  66  ILE A N   
505  C CA  . ILE A 66  ? 0.8883 0.4803 0.6295 -0.0244 -0.0119 0.0694  66  ILE A CA  
506  C C   . ILE A 66  ? 0.9528 0.4936 0.6603 -0.0365 -0.0021 0.0736  66  ILE A C   
507  O O   . ILE A 66  ? 0.9125 0.4382 0.6329 -0.0274 0.0020  0.0728  66  ILE A O   
508  C CB  . ILE A 66  ? 0.8037 0.4241 0.5619 -0.0328 0.0066  0.0463  66  ILE A CB  
509  C CG1 . ILE A 66  ? 0.8130 0.4346 0.5942 -0.0305 0.0222  0.0294  66  ILE A CG1 
510  C CG2 . ILE A 66  ? 0.8775 0.5430 0.6644 -0.0217 -0.0025 0.0434  66  ILE A CG2 
511  C CD1 . ILE A 66  ? 0.8533 0.5019 0.6549 -0.0388 0.0367  0.0081  66  ILE A CD1 
512  N N   . ARG A 67  ? 0.9658 0.4767 0.6268 -0.0587 0.0038  0.0774  67  ARG A N   
513  C CA  . ARG A 67  ? 0.9439 0.4020 0.5645 -0.0759 0.0177  0.0801  67  ARG A CA  
514  C C   . ARG A 67  ? 0.9484 0.4068 0.5632 -0.0983 0.0473  0.0575  67  ARG A C   
515  O O   . ARG A 67  ? 0.9499 0.4369 0.5736 -0.1043 0.0526  0.0468  67  ARG A O   
516  C CB  . ARG A 67  ? 1.0295 0.4423 0.5915 -0.0865 0.0008  0.1051  67  ARG A CB  
517  C CG  . ARG A 67  ? 1.0940 0.4959 0.6627 -0.0653 -0.0286 0.1298  67  ARG A CG  
518  C CD  . ARG A 67  ? 1.1293 0.5090 0.6540 -0.0751 -0.0472 0.1488  67  ARG A CD  
519  N NE  . ARG A 67  ? 1.1547 0.4975 0.6344 -0.0984 -0.0264 0.1422  67  ARG A NE  
520  C CZ  . ARG A 67  ? 1.3419 0.6534 0.8139 -0.0975 -0.0196 0.1464  67  ARG A CZ  
521  N NH1 . ARG A 67  ? 1.3198 0.6309 0.8273 -0.0746 -0.0305 0.1563  67  ARG A NH1 
522  N NH2 . ARG A 67  ? 1.3149 0.5943 0.7436 -0.1204 0.0002  0.1393  67  ARG A NH2 
523  N N   . LYS A 68  ? 0.9246 0.3506 0.5283 -0.1105 0.0677  0.0497  68  LYS A N   
524  C CA  . LYS A 68  ? 0.9868 0.4113 0.5910 -0.1329 0.0980  0.0275  68  LYS A CA  
525  C C   . LYS A 68  ? 1.0160 0.4083 0.5651 -0.1552 0.1076  0.0328  68  LYS A C   
526  O O   . LYS A 68  ? 1.0597 0.4183 0.5692 -0.1563 0.0966  0.0502  68  LYS A O   
527  C CB  . LYS A 68  ? 0.9727 0.3892 0.6009 -0.1354 0.1160  0.0126  68  LYS A CB  
528  C CG  . LYS A 68  ? 0.9501 0.3921 0.6067 -0.1515 0.1431  -0.0145 68  LYS A CG  
529  C CD  . LYS A 68  ? 0.9892 0.4380 0.6794 -0.1506 0.1543  -0.0297 68  LYS A CD  
530  C CE  . LYS A 68  ? 1.0134 0.5017 0.7486 -0.1614 0.1742  -0.0563 68  LYS A CE  
531  N NZ  . LYS A 68  ? 1.0893 0.5696 0.8036 -0.1816 0.1970  -0.0619 68  LYS A NZ  
532  N N   . LEU A 69  ? 0.9940 0.4026 0.5448 -0.1708 0.1271  0.0158  69  LEU A N   
533  C CA  . LEU A 69  ? 1.1149 0.4996 0.6165 -0.1919 0.1409  0.0137  69  LEU A CA  
534  C C   . LEU A 69  ? 1.1360 0.5160 0.6476 -0.2056 0.1727  -0.0061 69  LEU A C   
535  O O   . LEU A 69  ? 1.1247 0.5357 0.6762 -0.2111 0.1951  -0.0285 69  LEU A O   
536  C CB  . LEU A 69  ? 1.0086 0.4125 0.5069 -0.1995 0.1452  0.0058  69  LEU A CB  
537  C CG  . LEU A 69  ? 0.9960 0.4084 0.4869 -0.1870 0.1137  0.0248  69  LEU A CG  
538  C CD1 . LEU A 69  ? 0.8896 0.3315 0.3999 -0.1906 0.1211  0.0124  69  LEU A CD1 
539  C CD2 . LEU A 69  ? 0.9703 0.3486 0.4004 -0.1921 0.0915  0.0459  69  LEU A CD2 
540  N N   . LYS A 70  ? 1.2810 0.6238 0.7599 -0.2102 0.1738  0.0026  70  LYS A N   
541  C CA  . LYS A 70  ? 1.3025 0.6405 0.7940 -0.2218 0.2025  -0.0148 70  LYS A CA  
542  C C   . LYS A 70  ? 1.3226 0.6552 0.7927 -0.2438 0.2329  -0.0328 70  LYS A C   
543  O O   . LYS A 70  ? 1.3232 0.6662 0.8200 -0.2530 0.2605  -0.0523 70  LYS A O   
544  C CB  . LYS A 70  ? 1.3689 0.6644 0.8283 -0.2210 0.1957  0.0003  70  LYS A CB  
545  C CG  . LYS A 70  ? 1.4988 0.7474 0.8861 -0.2284 0.1812  0.0208  70  LYS A CG  
546  C CD  . LYS A 70  ? 1.6051 0.8117 0.9664 -0.2277 0.1771  0.0344  70  LYS A CD  
547  C CE  . LYS A 70  ? 1.6012 0.7611 0.8921 -0.2354 0.1594  0.0555  70  LYS A CE  
548  N NZ  . LYS A 70  ? 1.5711 0.7402 0.8591 -0.2188 0.1213  0.0780  70  LYS A NZ  
549  N N   . LYS A 71  ? 1.1763 0.4931 0.6007 -0.2527 0.2288  -0.0284 71  LYS A N   
550  C CA  . LYS A 71  ? 1.2433 0.5508 0.6452 -0.2735 0.2601  -0.0483 71  LYS A CA  
551  C C   . LYS A 71  ? 1.2022 0.5611 0.6705 -0.2716 0.2823  -0.0722 71  LYS A C   
552  O O   . LYS A 71  ? 1.2143 0.5754 0.6901 -0.2855 0.3156  -0.0938 71  LYS A O   
553  C CB  . LYS A 71  ? 1.2770 0.5520 0.6113 -0.2843 0.2479  -0.0391 71  LYS A CB  
554  C CG  . LYS A 71  ? 1.2295 0.4837 0.5295 -0.3076 0.2808  -0.0611 71  LYS A CG  
555  C CD  . LYS A 71  ? 1.3021 0.5148 0.5269 -0.3211 0.2648  -0.0517 71  LYS A CD  
556  C CE  . LYS A 71  ? 1.4967 0.6762 0.6786 -0.3471 0.2998  -0.0756 71  LYS A CE  
557  N NZ  . LYS A 71  ? 1.6163 0.7446 0.7163 -0.3647 0.2828  -0.0666 71  LYS A NZ  
558  N N   . TYR A 72  ? 1.1366 0.5363 0.6556 -0.2541 0.2644  -0.0689 72  TYR A N   
559  C CA  . TYR A 72  ? 1.1201 0.5695 0.7049 -0.2499 0.2792  -0.0887 72  TYR A CA  
560  C C   . TYR A 72  ? 1.0743 0.5623 0.7311 -0.2363 0.2744  -0.0954 72  TYR A C   
561  O O   . TYR A 72  ? 1.1167 0.5926 0.7706 -0.2295 0.2599  -0.0850 72  TYR A O   
562  C CB  . TYR A 72  ? 1.0363 0.5009 0.6207 -0.2424 0.2623  -0.0823 72  TYR A CB  
563  C CG  . TYR A 72  ? 1.1050 0.5296 0.6140 -0.2560 0.2597  -0.0746 72  TYR A CG  
564  C CD1 . TYR A 72  ? 1.0709 0.4759 0.5502 -0.2750 0.2899  -0.0921 72  TYR A CD1 
565  C CD2 . TYR A 72  ? 1.0492 0.4552 0.5179 -0.2502 0.2262  -0.0511 72  TYR A CD2 
566  C CE1 . TYR A 72  ? 1.1467 0.5111 0.5534 -0.2896 0.2854  -0.0879 72  TYR A CE1 
567  C CE2 . TYR A 72  ? 1.1125 0.4835 0.5142 -0.2639 0.2192  -0.0449 72  TYR A CE2 
568  C CZ  . TYR A 72  ? 1.1944 0.5429 0.5631 -0.2845 0.2483  -0.0639 72  TYR A CZ  
569  O OH  . TYR A 72  ? 1.2361 0.5457 0.5360 -0.3005 0.2395  -0.0601 72  TYR A OH  
570  N N   . ASP A 73  ? 1.0213 0.5553 0.7437 -0.2323 0.2855  -0.1137 73  ASP A N   
571  C CA  . ASP A 73  ? 0.9959 0.5702 0.7897 -0.2213 0.2797  -0.1242 73  ASP A CA  
572  C C   . ASP A 73  ? 0.9369 0.5350 0.7562 -0.2023 0.2495  -0.1161 73  ASP A C   
573  O O   . ASP A 73  ? 0.9136 0.5365 0.7578 -0.1971 0.2476  -0.1211 73  ASP A O   
574  C CB  . ASP A 73  ? 1.0024 0.6128 0.8566 -0.2272 0.3060  -0.1488 73  ASP A CB  
575  C CG  . ASP A 73  ? 0.9951 0.6503 0.9256 -0.2163 0.2949  -0.1605 73  ASP A CG  
576  O OD1 . ASP A 73  ? 1.1053 0.7561 1.0342 -0.2091 0.2752  -0.1531 73  ASP A OD1 
577  O OD2 . ASP A 73  ? 0.9344 0.6277 0.9265 -0.2149 0.3053  -0.1780 73  ASP A OD2 
578  N N   . ASN A 74  ? 0.9702 0.5582 0.7825 -0.1917 0.2276  -0.1048 74  ASN A N   
579  C CA  . ASN A 74  ? 0.8054 0.4133 0.6412 -0.1731 0.2009  -0.1001 74  ASN A CA  
580  C C   . ASN A 74  ? 0.7951 0.3937 0.5996 -0.1689 0.1887  -0.0867 74  ASN A C   
581  O O   . ASN A 74  ? 0.7505 0.3822 0.5869 -0.1576 0.1790  -0.0909 74  ASN A O   
582  C CB  . ASN A 74  ? 0.7667 0.4241 0.6751 -0.1659 0.1998  -0.1200 74  ASN A CB  
583  C CG  . ASN A 74  ? 0.8208 0.5011 0.7495 -0.1447 0.1713  -0.1159 74  ASN A CG  
584  O OD1 . ASN A 74  ? 0.8189 0.4850 0.7203 -0.1335 0.1545  -0.1012 74  ASN A OD1 
585  N ND2 . ASN A 74  ? 0.7812 0.5058 0.7591 -0.1347 0.1633  -0.1256 74  ASN A ND2 
586  N N   . CYS A 75  ? 0.8307 0.3883 0.5721 -0.1762 0.1860  -0.0689 75  CYS A N   
587  C CA  . CYS A 75  ? 0.8384 0.3841 0.5445 -0.1739 0.1707  -0.0536 75  CYS A CA  
588  C C   . CYS A 75  ? 0.8539 0.3840 0.5306 -0.1589 0.1419  -0.0294 75  CYS A C   
589  O O   . CYS A 75  ? 0.8999 0.3980 0.5561 -0.1616 0.1425  -0.0221 75  CYS A O   
590  C CB  . CYS A 75  ? 0.8777 0.4019 0.5373 -0.1924 0.1868  -0.0533 75  CYS A CB  
591  S SG  . CYS A 75  ? 0.8541 0.4128 0.5573 -0.2006 0.2169  -0.0797 75  CYS A SG  
592  N N   . TRP A 76  ? 0.7926 0.3456 0.4715 -0.1429 0.1178  -0.0173 76  TRP A N   
593  C CA  . TRP A 76  ? 0.8280 0.3800 0.4996 -0.1239 0.0896  0.0030  76  TRP A CA  
594  C C   . TRP A 76  ? 0.8305 0.3802 0.4719 -0.1227 0.0699  0.0199  76  TRP A C   
595  O O   . TRP A 76  ? 0.8971 0.4644 0.5414 -0.1282 0.0740  0.0132  76  TRP A O   
596  C CB  . TRP A 76  ? 0.7991 0.3956 0.5263 -0.1001 0.0783  -0.0034 76  TRP A CB  
597  C CG  . TRP A 76  ? 0.7320 0.3362 0.4918 -0.1028 0.0949  -0.0223 76  TRP A CG  
598  C CD1 . TRP A 76  ? 0.7409 0.3696 0.5352 -0.1101 0.1111  -0.0431 76  TRP A CD1 
599  C CD2 . TRP A 76  ? 0.8152 0.4028 0.5792 -0.0987 0.0958  -0.0227 76  TRP A CD2 
600  N NE1 . TRP A 76  ? 0.7074 0.3382 0.5273 -0.1120 0.1201  -0.0564 76  TRP A NE1 
601  C CE2 . TRP A 76  ? 0.7989 0.4032 0.5983 -0.1059 0.1121  -0.0449 76  TRP A CE2 
602  C CE3 . TRP A 76  ? 0.9009 0.4607 0.6452 -0.0895 0.0842  -0.0068 76  TRP A CE3 
603  C CZ2 . TRP A 76  ? 0.8572 0.4503 0.6681 -0.1063 0.1176  -0.0526 76  TRP A CZ2 
604  C CZ3 . TRP A 76  ? 0.8787 0.4250 0.6349 -0.0885 0.0919  -0.0143 76  TRP A CZ3 
605  C CH2 . TRP A 76  ? 0.8773 0.4398 0.6642 -0.0980 0.1087  -0.0375 76  TRP A CH2 
606  N N   . LEU A 77  ? 0.8600 0.3878 0.4753 -0.1153 0.0477  0.0419  77  LEU A N   
607  C CA  . LEU A 77  ? 0.8844 0.4096 0.4727 -0.1141 0.0236  0.0602  77  LEU A CA  
608  C C   . LEU A 77  ? 0.9050 0.4619 0.5320 -0.0867 -0.0026 0.0719  77  LEU A C   
609  O O   . LEU A 77  ? 0.9331 0.4864 0.5798 -0.0723 -0.0065 0.0759  77  LEU A O   
610  C CB  . LEU A 77  ? 0.8424 0.3103 0.3632 -0.1316 0.0169  0.0786  77  LEU A CB  
611  C CG  . LEU A 77  ? 0.9308 0.3920 0.4207 -0.1312 -0.0147 0.1007  77  LEU A CG  
612  C CD1 . LEU A 77  ? 0.9858 0.4713 0.4740 -0.1409 -0.0118 0.0909  77  LEU A CD1 
613  C CD2 . LEU A 77  ? 0.9641 0.3849 0.4007 -0.1453 -0.0221 0.1116  77  LEU A CD2 
614  N N   . ALA A 78  ? 0.8382 0.4250 0.4771 -0.0807 -0.0179 0.0759  78  ALA A N   
615  C CA  . ALA A 78  ? 0.8318 0.4490 0.5072 -0.0574 -0.0411 0.0868  78  ALA A CA  
616  C C   . ALA A 78  ? 0.8466 0.4584 0.4969 -0.0617 -0.0671 0.1056  78  ALA A C   
617  O O   . ALA A 78  ? 0.9577 0.5678 0.5811 -0.0787 -0.0651 0.1024  78  ALA A O   
618  C CB  . ALA A 78  ? 0.7434 0.4094 0.4681 -0.0445 -0.0344 0.0716  78  ALA A CB  
619  N N   . LEU A 79  ? 0.8434 0.4524 0.5046 -0.0468 -0.0916 0.1246  79  LEU A N   
620  C CA  . LEU A 79  ? 0.8572 0.4692 0.5073 -0.0476 -0.1222 0.1436  79  LEU A CA  
621  C C   . LEU A 79  ? 0.8812 0.5433 0.5944 -0.0247 -0.1345 0.1441  79  LEU A C   
622  O O   . LEU A 79  ? 0.9034 0.5763 0.6578 -0.0036 -0.1345 0.1454  79  LEU A O   
623  C CB  . LEU A 79  ? 0.8913 0.4598 0.5076 -0.0487 -0.1444 0.1675  79  LEU A CB  
624  C CG  . LEU A 79  ? 1.0160 0.5359 0.5709 -0.0724 -0.1282 0.1647  79  LEU A CG  
625  C CD1 . LEU A 79  ? 1.0358 0.5321 0.5728 -0.0711 -0.1484 0.1822  79  LEU A CD1 
626  C CD2 . LEU A 79  ? 0.9955 0.5110 0.5088 -0.0989 -0.1167 0.1531  79  LEU A CD2 
627  N N   . THR A 80  ? 0.7890 0.4790 0.5089 -0.0302 -0.1425 0.1420  80  THR A N   
628  C CA  . THR A 80  ? 0.8038 0.5413 0.5813 -0.0123 -0.1502 0.1405  80  THR A CA  
629  C C   . THR A 80  ? 0.8809 0.6264 0.6727 -0.0062 -0.1847 0.1616  80  THR A C   
630  O O   . THR A 80  ? 0.8248 0.5388 0.5754 -0.0177 -0.2063 0.1782  80  THR A O   
631  C CB  . THR A 80  ? 0.8255 0.5901 0.6076 -0.0215 -0.1371 0.1250  80  THR A CB  
632  O OG1 . THR A 80  ? 0.8043 0.5614 0.5521 -0.0406 -0.1531 0.1322  80  THR A OG1 
633  C CG2 . THR A 80  ? 0.7904 0.5435 0.5552 -0.0303 -0.1071 0.1063  80  THR A CG2 
634  N N   . ASP A 81  ? 0.8265 0.6142 0.6783 0.0116  -0.1901 0.1606  81  ASP A N   
635  C CA  . ASP A 81  ? 0.7859 0.5931 0.6649 0.0167  -0.2223 0.1774  81  ASP A CA  
636  C C   . ASP A 81  ? 0.7716 0.5779 0.6114 -0.0076 -0.2363 0.1795  81  ASP A C   
637  O O   . ASP A 81  ? 0.7655 0.5802 0.5907 -0.0201 -0.2160 0.1632  81  ASP A O   
638  C CB  . ASP A 81  ? 0.7438 0.5994 0.6971 0.0372  -0.2171 0.1707  81  ASP A CB  
639  C CG  . ASP A 81  ? 0.7755 0.6554 0.7743 0.0467  -0.2498 0.1877  81  ASP A CG  
640  O OD1 . ASP A 81  ? 0.7825 0.6705 0.7662 0.0312  -0.2716 0.1946  81  ASP A OD1 
641  O OD2 . ASP A 81  ? 0.7265 0.6185 0.7794 0.0694  -0.2522 0.1926  81  ASP A OD2 
642  N N   . PRO A 82  ? 0.7679 0.5658 0.5924 -0.0157 -0.2651 0.1946  82  PRO A N   
643  C CA  . PRO A 82  ? 0.8311 0.6273 0.6168 -0.0413 -0.2749 0.1923  82  PRO A CA  
644  C C   . PRO A 82  ? 0.8061 0.6455 0.6291 -0.0424 -0.2780 0.1858  82  PRO A C   
645  O O   . PRO A 82  ? 0.8782 0.7138 0.6661 -0.0653 -0.2794 0.1800  82  PRO A O   
646  C CB  . PRO A 82  ? 0.8470 0.6332 0.6251 -0.0448 -0.3033 0.2072  82  PRO A CB  
647  C CG  . PRO A 82  ? 0.8367 0.6363 0.6715 -0.0163 -0.3108 0.2171  82  PRO A CG  
648  C CD  . PRO A 82  ? 0.8423 0.6310 0.6825 -0.0033 -0.2830 0.2090  82  PRO A CD  
649  N N   . ARG A 83  ? 0.7721 0.6509 0.6649 -0.0198 -0.2750 0.1841  83  ARG A N   
650  C CA  . ARG A 83  ? 0.7463 0.6684 0.6804 -0.0207 -0.2677 0.1726  83  ARG A CA  
651  C C   . ARG A 83  ? 0.7033 0.6285 0.6297 -0.0229 -0.2290 0.1510  83  ARG A C   
652  O O   . ARG A 83  ? 0.7857 0.7409 0.7394 -0.0247 -0.2193 0.1410  83  ARG A O   
653  C CB  . ARG A 83  ? 0.7032 0.6671 0.7198 0.0034  -0.2760 0.1772  83  ARG A CB  
654  C CG  . ARG A 83  ? 0.7426 0.7114 0.7823 0.0086  -0.3100 0.1947  83  ARG A CG  
655  C CD  . ARG A 83  ? 0.7968 0.8026 0.9223 0.0354  -0.3090 0.1959  83  ARG A CD  
656  N NE  . ARG A 83  ? 0.7703 0.7606 0.9080 0.0559  -0.2886 0.1936  83  ARG A NE  
657  C CZ  . ARG A 83  ? 0.7643 0.7773 0.9695 0.0797  -0.2794 0.1914  83  ARG A CZ  
658  N NH1 . ARG A 83  ? 0.8539 0.9080 1.1246 0.0871  -0.2877 0.1913  83  ARG A NH1 
659  N NH2 . ARG A 83  ? 0.7871 0.7798 0.9943 0.0953  -0.2593 0.1876  83  ARG A NH2 
660  N N   . ASP A 84  ? 0.7980 0.6926 0.6894 -0.0231 -0.2076 0.1439  84  ASP A N   
661  C CA  . ASP A 84  ? 0.7665 0.6643 0.6564 -0.0222 -0.1741 0.1249  84  ASP A CA  
662  C C   . ASP A 84  ? 0.7896 0.6484 0.6183 -0.0409 -0.1614 0.1187  84  ASP A C   
663  O O   . ASP A 84  ? 0.7884 0.6259 0.6036 -0.0365 -0.1469 0.1147  84  ASP A O   
664  C CB  . ASP A 84  ? 0.6340 0.5415 0.5617 0.0009  -0.1583 0.1200  84  ASP A CB  
665  C CG  . ASP A 84  ? 0.6682 0.5840 0.5997 0.0031  -0.1294 0.1022  84  ASP A CG  
666  O OD1 . ASP A 84  ? 0.7270 0.6470 0.6438 -0.0098 -0.1217 0.0944  84  ASP A OD1 
667  O OD2 . ASP A 84  ? 0.6946 0.6108 0.6431 0.0174  -0.1153 0.0961  84  ASP A OD2 
668  N N   . VAL A 85  ? 0.7830 0.6320 0.5760 -0.0631 -0.1649 0.1163  85  VAL A N   
669  C CA  . VAL A 85  ? 0.8512 0.6591 0.5833 -0.0839 -0.1537 0.1112  85  VAL A CA  
670  C C   . VAL A 85  ? 0.8881 0.6963 0.6067 -0.0983 -0.1311 0.0941  85  VAL A C   
671  O O   . VAL A 85  ? 0.9069 0.6845 0.5858 -0.1133 -0.1125 0.0846  85  VAL A O   
672  C CB  . VAL A 85  ? 0.8676 0.6464 0.5512 -0.1019 -0.1811 0.1269  85  VAL A CB  
673  C CG1 . VAL A 85  ? 0.8660 0.6343 0.5574 -0.0873 -0.2012 0.1449  85  VAL A CG1 
674  C CG2 . VAL A 85  ? 0.8408 0.6414 0.5320 -0.1120 -0.2045 0.1320  85  VAL A CG2 
675  N N   . ALA A 86  ? 0.9092 0.7495 0.6620 -0.0942 -0.1306 0.0894  86  ALA A N   
676  C CA  . ALA A 86  ? 0.9068 0.7447 0.6481 -0.1074 -0.1109 0.0746  86  ALA A CA  
677  C C   . ALA A 86  ? 0.8495 0.7239 0.6401 -0.0934 -0.1042 0.0698  86  ALA A C   
678  O O   . ALA A 86  ? 0.7741 0.6745 0.6055 -0.0747 -0.1118 0.0760  86  ALA A O   
679  C CB  . ALA A 86  ? 0.9198 0.7388 0.6167 -0.1345 -0.1226 0.0759  86  ALA A CB  
680  N N   . ARG A 87  ? 0.8623 0.7348 0.6473 -0.1033 -0.0878 0.0582  87  ARG A N   
681  C CA  . ARG A 87  ? 0.8247 0.7251 0.6473 -0.0945 -0.0813 0.0546  87  ARG A CA  
682  C C   . ARG A 87  ? 0.8094 0.7317 0.6475 -0.1013 -0.1021 0.0623  87  ARG A C   
683  O O   . ARG A 87  ? 0.8719 0.7831 0.6823 -0.1197 -0.1192 0.0667  87  ARG A O   
684  C CB  . ARG A 87  ? 0.7856 0.6731 0.5971 -0.1033 -0.0585 0.0412  87  ARG A CB  
685  C CG  . ARG A 87  ? 0.7810 0.6586 0.5975 -0.0918 -0.0380 0.0328  87  ARG A CG  
686  C CD  . ARG A 87  ? 0.6541 0.5208 0.4689 -0.0978 -0.0176 0.0211  87  ARG A CD  
687  N NE  . ARG A 87  ? 0.7467 0.5853 0.5244 -0.1211 -0.0101 0.0135  87  ARG A NE  
688  C CZ  . ARG A 87  ? 0.8263 0.6598 0.5884 -0.1387 -0.0128 0.0116  87  ARG A CZ  
689  N NH1 . ARG A 87  ? 0.7767 0.6335 0.5606 -0.1359 -0.0229 0.0170  87  ARG A NH1 
690  N NH2 . ARG A 87  ? 0.7773 0.5803 0.4999 -0.1614 -0.0033 0.0026  87  ARG A NH2 
691  N N   . ILE A 88  ? 0.7869 0.7399 0.6690 -0.0879 -0.1005 0.0634  88  ILE A N   
692  C CA  . ILE A 88  ? 0.7796 0.7596 0.6891 -0.0935 -0.1163 0.0684  88  ILE A CA  
693  C C   . ILE A 88  ? 0.7806 0.7680 0.7011 -0.0982 -0.0974 0.0590  88  ILE A C   
694  O O   . ILE A 88  ? 0.7395 0.7428 0.6897 -0.0835 -0.0839 0.0571  88  ILE A O   
695  C CB  . ILE A 88  ? 0.7278 0.7372 0.6848 -0.0746 -0.1286 0.0776  88  ILE A CB  
696  C CG1 . ILE A 88  ? 0.7508 0.7462 0.6954 -0.0671 -0.1445 0.0874  88  ILE A CG1 
697  C CG2 . ILE A 88  ? 0.7915 0.8312 0.7829 -0.0821 -0.1464 0.0821  88  ILE A CG2 
698  C CD1 . ILE A 88  ? 0.7429 0.7632 0.7371 -0.0461 -0.1540 0.0957  88  ILE A CD1 
699  N N   . GLU A 89  ? 0.7807 0.7525 0.6732 -0.1200 -0.0953 0.0529  89  GLU A N   
700  C CA  . GLU A 89  ? 0.8012 0.7740 0.7007 -0.1258 -0.0767 0.0444  89  GLU A CA  
701  C C   . GLU A 89  ? 0.7652 0.7723 0.7084 -0.1242 -0.0818 0.0475  89  GLU A C   
702  O O   . GLU A 89  ? 0.7530 0.7651 0.7123 -0.1192 -0.0632 0.0434  89  GLU A O   
703  C CB  . GLU A 89  ? 0.8402 0.7864 0.7003 -0.1513 -0.0730 0.0361  89  GLU A CB  
704  C CG  . GLU A 89  ? 0.9383 0.8488 0.7578 -0.1551 -0.0612 0.0299  89  GLU A CG  
705  C CD  . GLU A 89  ? 1.0127 0.8936 0.7913 -0.1822 -0.0542 0.0195  89  GLU A CD  
706  O OE1 . GLU A 89  ? 1.0061 0.8932 0.7879 -0.1975 -0.0571 0.0165  89  GLU A OE1 
707  O OE2 . GLU A 89  ? 1.0012 0.8512 0.7443 -0.1895 -0.0437 0.0132  89  GLU A OE2 
708  N N   . SER A 90  ? 0.8152 0.8452 0.7790 -0.1285 -0.1067 0.0550  90  SER A N   
709  C CA  . SER A 90  ? 0.7754 0.8418 0.7894 -0.1281 -0.1109 0.0566  90  SER A CA  
710  C C   . SER A 90  ? 0.7255 0.8114 0.7790 -0.1040 -0.0970 0.0583  90  SER A C   
711  O O   . SER A 90  ? 0.7209 0.8311 0.8127 -0.1036 -0.0880 0.0560  90  SER A O   
712  C CB  . SER A 90  ? 0.7552 0.8436 0.7882 -0.1373 -0.1446 0.0650  90  SER A CB  
713  O OG  . SER A 90  ? 0.8292 0.9187 0.8671 -0.1213 -0.1613 0.0754  90  SER A OG  
714  N N   . LYS A 91  ? 0.7335 0.8073 0.7768 -0.0861 -0.0934 0.0611  91  LYS A N   
715  C CA  . LYS A 91  ? 0.6403 0.7261 0.7119 -0.0650 -0.0785 0.0608  91  LYS A CA  
716  C C   . LYS A 91  ? 0.5856 0.6468 0.6285 -0.0579 -0.0553 0.0548  91  LYS A C   
717  O O   . LYS A 91  ? 0.5652 0.6273 0.6166 -0.0413 -0.0450 0.0544  91  LYS A O   
718  C CB  . LYS A 91  ? 0.6348 0.7278 0.7233 -0.0492 -0.0935 0.0685  91  LYS A CB  
719  C CG  . LYS A 91  ? 0.6547 0.7789 0.7888 -0.0500 -0.1164 0.0759  91  LYS A CG  
720  C CD  . LYS A 91  ? 0.7210 0.8463 0.8702 -0.0332 -0.1318 0.0850  91  LYS A CD  
721  C CE  . LYS A 91  ? 0.7396 0.9008 0.9497 -0.0286 -0.1525 0.0926  91  LYS A CE  
722  N NZ  . LYS A 91  ? 0.8221 0.9931 1.0298 -0.0495 -0.1792 0.0974  91  LYS A NZ  
723  N N   . THR A 92  ? 0.5866 0.6250 0.5966 -0.0704 -0.0478 0.0500  92  THR A N   
724  C CA  . THR A 92  ? 0.6188 0.6348 0.6070 -0.0641 -0.0287 0.0454  92  THR A CA  
725  C C   . THR A 92  ? 0.6264 0.6423 0.6193 -0.0718 -0.0134 0.0424  92  THR A C   
726  O O   . THR A 92  ? 0.6553 0.6679 0.6427 -0.0894 -0.0145 0.0398  92  THR A O   
727  C CB  . THR A 92  ? 0.6418 0.6295 0.5946 -0.0709 -0.0289 0.0418  92  THR A CB  
728  O OG1 . THR A 92  ? 0.6832 0.6686 0.6286 -0.0669 -0.0424 0.0451  92  THR A OG1 
729  C CG2 . THR A 92  ? 0.6563 0.6247 0.5966 -0.0614 -0.0125 0.0379  92  THR A CG2 
730  N N   . VAL A 93  ? 0.6186 0.6347 0.6177 -0.0602 0.0011  0.0427  93  VAL A N   
731  C CA  . VAL A 93  ? 0.5840 0.5988 0.5871 -0.0671 0.0169  0.0415  93  VAL A CA  
732  C C   . VAL A 93  ? 0.5636 0.5509 0.5402 -0.0591 0.0303  0.0421  93  VAL A C   
733  O O   . VAL A 93  ? 0.5536 0.5314 0.5183 -0.0455 0.0277  0.0429  93  VAL A O   
734  C CB  . VAL A 93  ? 0.5506 0.5927 0.5883 -0.0642 0.0230  0.0420  93  VAL A CB  
735  C CG1 . VAL A 93  ? 0.5774 0.6498 0.6499 -0.0714 0.0062  0.0427  93  VAL A CG1 
736  C CG2 . VAL A 93  ? 0.4948 0.5372 0.5332 -0.0456 0.0280  0.0429  93  VAL A CG2 
737  N N   . ILE A 94  ? 0.5683 0.5419 0.5365 -0.0682 0.0434  0.0421  94  ILE A N   
738  C CA  . ILE A 94  ? 0.5827 0.5281 0.5263 -0.0615 0.0545  0.0453  94  ILE A CA  
739  C C   . ILE A 94  ? 0.6191 0.5640 0.5639 -0.0668 0.0707  0.0475  94  ILE A C   
740  O O   . ILE A 94  ? 0.6074 0.5620 0.5670 -0.0821 0.0773  0.0451  94  ILE A O   
741  C CB  . ILE A 94  ? 0.6281 0.5461 0.5544 -0.0679 0.0564  0.0442  94  ILE A CB  
742  C CG1 . ILE A 94  ? 0.5836 0.4993 0.5071 -0.0639 0.0450  0.0403  94  ILE A CG1 
743  C CG2 . ILE A 94  ? 0.5621 0.4505 0.4675 -0.0603 0.0654  0.0501  94  ILE A CG2 
744  C CD1 . ILE A 94  ? 0.6824 0.5706 0.5932 -0.0690 0.0506  0.0368  94  ILE A CD1 
745  N N   . ILE A 95  ? 0.6548 0.5870 0.5820 -0.0562 0.0776  0.0515  95  ILE A N   
746  C CA  . ILE A 95  ? 0.6520 0.5807 0.5742 -0.0616 0.0958  0.0530  95  ILE A CA  
747  C C   . ILE A 95  ? 0.6609 0.5500 0.5459 -0.0633 0.1041  0.0604  95  ILE A C   
748  O O   . ILE A 95  ? 0.6657 0.5335 0.5252 -0.0511 0.0964  0.0658  95  ILE A O   
749  C CB  . ILE A 95  ? 0.6514 0.5915 0.5755 -0.0509 0.0995  0.0514  95  ILE A CB  
750  C CG1 . ILE A 95  ? 0.6337 0.6126 0.6019 -0.0502 0.0946  0.0452  95  ILE A CG1 
751  C CG2 . ILE A 95  ? 0.6463 0.5699 0.5499 -0.0570 0.1216  0.0530  95  ILE A CG2 
752  C CD1 . ILE A 95  ? 0.6193 0.6084 0.5959 -0.0396 0.0737  0.0446  95  ILE A CD1 
753  N N   . THR A 96  ? 0.6905 0.5691 0.5741 -0.0788 0.1184  0.0610  96  THR A N   
754  C CA  . THR A 96  ? 0.7779 0.6150 0.6251 -0.0819 0.1286  0.0697  96  THR A CA  
755  C C   . THR A 96  ? 0.7953 0.6294 0.6412 -0.0987 0.1524  0.0689  96  THR A C   
756  O O   . THR A 96  ? 0.7543 0.6205 0.6362 -0.1100 0.1595  0.0604  96  THR A O   
757  C CB  . THR A 96  ? 0.7783 0.5925 0.6207 -0.0846 0.1233  0.0718  96  THR A CB  
758  O OG1 . THR A 96  ? 0.7541 0.5871 0.6236 -0.1011 0.1270  0.0632  96  THR A OG1 
759  C CG2 . THR A 96  ? 0.7206 0.5335 0.5639 -0.0682 0.1040  0.0722  96  THR A CG2 
760  N N   . GLN A 97  ? 0.9000 0.6941 0.7042 -0.1007 0.1641  0.0783  97  GLN A N   
761  C CA  . GLN A 97  ? 0.9194 0.7030 0.7155 -0.1188 0.1907  0.0778  97  GLN A CA  
762  C C   . GLN A 97  ? 0.8701 0.6613 0.6934 -0.1372 0.1991  0.0722  97  GLN A C   
763  O O   . GLN A 97  ? 0.8124 0.6281 0.6648 -0.1528 0.2157  0.0638  97  GLN A O   
764  C CB  . GLN A 97  ? 0.9444 0.6743 0.6812 -0.1187 0.1989  0.0915  97  GLN A CB  
765  C CG  . GLN A 97  ? 1.1231 0.8341 0.8417 -0.1391 0.2300  0.0917  97  GLN A CG  
766  C CD  . GLN A 97  ? 1.1965 0.9328 0.9261 -0.1431 0.2477  0.0822  97  GLN A CD  
767  O OE1 . GLN A 97  ? 1.2429 0.9883 0.9647 -0.1290 0.2376  0.0810  97  GLN A OE1 
768  N NE2 . GLN A 97  ? 1.1658 0.9136 0.9169 -0.1629 0.2758  0.0740  97  GLN A NE2 
769  N N   . GLU A 98  ? 0.8610 0.6322 0.6782 -0.1364 0.1886  0.0754  98  GLU A N   
770  C CA  . GLU A 98  ? 0.8498 0.6235 0.6876 -0.1550 0.1952  0.0688  98  GLU A CA  
771  C C   . GLU A 98  ? 0.7417 0.5466 0.6113 -0.1522 0.1750  0.0599  98  GLU A C   
772  O O   . GLU A 98  ? 0.7618 0.5619 0.6238 -0.1355 0.1579  0.0624  98  GLU A O   
773  C CB  . GLU A 98  ? 0.9013 0.6215 0.7052 -0.1590 0.2026  0.0778  98  GLU A CB  
774  C CG  . GLU A 98  ? 1.0267 0.7041 0.7857 -0.1597 0.2183  0.0909  98  GLU A CG  
775  C CD  . GLU A 98  ? 1.1151 0.7914 0.8772 -0.1834 0.2455  0.0863  98  GLU A CD  
776  O OE1 . GLU A 98  ? 1.0924 0.7929 0.8906 -0.2002 0.2510  0.0744  98  GLU A OE1 
777  O OE2 . GLU A 98  ? 1.2176 0.8752 0.9505 -0.1825 0.2559  0.0917  98  GLU A OE2 
778  N N   . GLN A 99  ? 0.6831 0.5188 0.5872 -0.1700 0.1767  0.0493  99  GLN A N   
779  C CA  . GLN A 99  ? 0.7209 0.5812 0.6470 -0.1712 0.1568  0.0415  99  GLN A CA  
780  C C   . GLN A 99  ? 0.7791 0.6042 0.6831 -0.1729 0.1538  0.0413  99  GLN A C   
781  O O   . GLN A 99  ? 0.7752 0.6055 0.6802 -0.1650 0.1380  0.0381  99  GLN A O   
782  C CB  . GLN A 99  ? 0.6782 0.5765 0.6439 -0.1922 0.1564  0.0314  99  GLN A CB  
783  C CG  . GLN A 99  ? 0.6610 0.5826 0.6428 -0.1961 0.1330  0.0246  99  GLN A CG  
784  C CD  . GLN A 99  ? 0.6928 0.6521 0.7141 -0.2178 0.1275  0.0159  99  GLN A CD  
785  O OE1 . GLN A 99  ? 0.6717 0.6400 0.7127 -0.2319 0.1441  0.0131  99  GLN A OE1 
786  N NE2 . GLN A 99  ? 0.6986 0.6797 0.7315 -0.2217 0.1035  0.0116  99  GLN A NE2 
787  N N   . ARG A 100 ? 0.7440 0.5307 0.6283 -0.1832 0.1709  0.0441  100 ARG A N   
788  C CA  . ARG A 100 ? 0.7630 0.5133 0.6310 -0.1857 0.1723  0.0424  100 ARG A CA  
789  C C   . ARG A 100 ? 0.7811 0.5095 0.6328 -0.1606 0.1624  0.0501  100 ARG A C   
790  O O   . ARG A 100 ? 0.8079 0.5158 0.6563 -0.1593 0.1608  0.0458  100 ARG A O   
791  C CB  . ARG A 100 ? 0.8662 0.5763 0.7172 -0.2010 0.1943  0.0453  100 ARG A CB  
792  C CG  . ARG A 100 ? 0.9190 0.5947 0.7614 -0.2106 0.2000  0.0390  100 ARG A CG  
793  C CD  . ARG A 100 ? 1.0786 0.7226 0.9091 -0.2209 0.2172  0.0402  100 ARG A CD  
794  N NE  . ARG A 100 ? 1.1055 0.7246 0.9330 -0.2261 0.2201  0.0307  100 ARG A NE  
795  C CZ  . ARG A 100 ? 1.1543 0.7467 0.9738 -0.2344 0.2330  0.0283  100 ARG A CZ  
796  N NH1 . ARG A 100 ? 1.1868 0.7725 0.9992 -0.2394 0.2440  0.0349  100 ARG A NH1 
797  N NH2 . ARG A 100 ? 1.1002 0.6707 0.9174 -0.2383 0.2367  0.0182  100 ARG A NH2 
798  N N   . ASP A 101 ? 0.7386 0.4710 0.5816 -0.1419 0.1564  0.0602  101 ASP A N   
799  C CA  . ASP A 101 ? 0.7497 0.4675 0.5834 -0.1187 0.1436  0.0666  101 ASP A CA  
800  C C   . ASP A 101 ? 0.7309 0.4795 0.5840 -0.1121 0.1278  0.0576  101 ASP A C   
801  O O   . ASP A 101 ? 0.6719 0.4082 0.5253 -0.0990 0.1205  0.0575  101 ASP A O   
802  C CB  . ASP A 101 ? 0.8155 0.5267 0.6295 -0.1036 0.1404  0.0793  101 ASP A CB  
803  C CG  . ASP A 101 ? 0.9238 0.5955 0.7087 -0.1101 0.1557  0.0905  101 ASP A CG  
804  O OD1 . ASP A 101 ? 1.0742 0.7109 0.8519 -0.1155 0.1637  0.0930  101 ASP A OD1 
805  O OD2 . ASP A 101 ? 1.0198 0.6920 0.7869 -0.1107 0.1615  0.0966  101 ASP A OD2 
806  N N   . THR A 102 ? 0.6877 0.4752 0.5588 -0.1211 0.1227  0.0503  102 THR A N   
807  C CA  . THR A 102 ? 0.7672 0.5811 0.6520 -0.1164 0.1071  0.0434  102 THR A CA  
808  C C   . THR A 102 ? 0.7332 0.5472 0.6222 -0.1349 0.1066  0.0321  102 THR A C   
809  O O   . THR A 102 ? 0.6867 0.4958 0.5727 -0.1314 0.1003  0.0268  102 THR A O   
810  C CB  . THR A 102 ? 0.6746 0.5284 0.5768 -0.1137 0.0989  0.0435  102 THR A CB  
811  O OG1 . THR A 102 ? 0.6882 0.5384 0.5807 -0.0970 0.0998  0.0519  102 THR A OG1 
812  C CG2 . THR A 102 ? 0.6438 0.5213 0.5577 -0.1108 0.0821  0.0379  102 THR A CG2 
813  N N   . VAL A 103 ? 0.7581 0.5758 0.6520 -0.1564 0.1142  0.0275  103 VAL A N   
814  C CA  . VAL A 103 ? 0.6943 0.5144 0.5888 -0.1779 0.1110  0.0159  103 VAL A CA  
815  C C   . VAL A 103 ? 0.7749 0.5717 0.6637 -0.1986 0.1281  0.0119  103 VAL A C   
816  O O   . VAL A 103 ? 0.7871 0.5838 0.6810 -0.2010 0.1389  0.0175  103 VAL A O   
817  C CB  . VAL A 103 ? 0.6940 0.5583 0.6085 -0.1855 0.0930  0.0130  103 VAL A CB  
818  C CG1 . VAL A 103 ? 0.6764 0.5573 0.6073 -0.2100 0.0953  0.0078  103 VAL A CG1 
819  C CG2 . VAL A 103 ? 0.6440 0.5095 0.5477 -0.1881 0.0786  0.0069  103 VAL A CG2 
820  N N   . PRO A 104 ? 0.8026 0.5754 0.6784 -0.2150 0.1338  0.0015  104 PRO A N   
821  C CA  . PRO A 104 ? 0.7684 0.5189 0.6393 -0.2379 0.1503  -0.0042 104 PRO A CA  
822  C C   . PRO A 104 ? 0.7318 0.5193 0.6228 -0.2601 0.1431  -0.0090 104 PRO A C   
823  O O   . PRO A 104 ? 0.7576 0.5799 0.6603 -0.2651 0.1229  -0.0127 104 PRO A O   
824  C CB  . PRO A 104 ? 0.7892 0.5073 0.6408 -0.2502 0.1566  -0.0169 104 PRO A CB  
825  C CG  . PRO A 104 ? 0.7787 0.4929 0.6258 -0.2275 0.1498  -0.0148 104 PRO A CG  
826  C CD  . PRO A 104 ? 0.7303 0.4883 0.5924 -0.2134 0.1298  -0.0064 104 PRO A CD  
827  N N   . ILE A 105 ? 0.7778 0.5571 0.6747 -0.2735 0.1592  -0.0085 105 ILE A N   
828  C CA  . ILE A 105 ? 0.8026 0.6184 0.7268 -0.2963 0.1549  -0.0144 105 ILE A CA  
829  C C   . ILE A 105 ? 0.7991 0.6129 0.7165 -0.3230 0.1467  -0.0291 105 ILE A C   
830  O O   . ILE A 105 ? 0.8179 0.5995 0.7171 -0.3281 0.1590  -0.0359 105 ILE A O   
831  C CB  . ILE A 105 ? 0.7707 0.5760 0.7021 -0.3035 0.1775  -0.0108 105 ILE A CB  
832  C CG1 . ILE A 105 ? 0.7841 0.5868 0.7127 -0.2789 0.1852  0.0036  105 ILE A CG1 
833  C CG2 . ILE A 105 ? 0.7788 0.6265 0.7471 -0.3259 0.1729  -0.0190 105 ILE A CG2 
834  C CD1 . ILE A 105 ? 0.7795 0.6319 0.7355 -0.2642 0.1675  0.0066  105 ILE A CD1 
835  N N   . PRO A 106 ? 0.8015 0.6513 0.7310 -0.3323 0.1218  -0.0336 106 PRO A N   
836  C CA  . PRO A 106 ? 0.8151 0.6594 0.7280 -0.3553 0.1104  -0.0469 106 PRO A CA  
837  C C   . PRO A 106 ? 0.8306 0.6851 0.7599 -0.3761 0.1140  -0.0550 106 PRO A C   
838  O O   . PRO A 106 ? 0.8627 0.7382 0.8243 -0.3776 0.1222  -0.0512 106 PRO A O   
839  C CB  . PRO A 106 ? 0.7855 0.6679 0.7080 -0.3580 0.0789  -0.0453 106 PRO A CB  
840  C CG  . PRO A 106 ? 0.7881 0.7125 0.7525 -0.3372 0.0729  -0.0335 106 PRO A CG  
841  C CD  . PRO A 106 ? 0.7172 0.6149 0.6751 -0.3158 0.0998  -0.0258 106 PRO A CD  
842  N N   . LYS A 107 ? 0.8710 0.7090 0.7760 -0.3928 0.1095  -0.0673 107 LYS A N   
843  C CA  . LYS A 107 ? 0.9251 0.7696 0.8419 -0.4147 0.1121  -0.0766 107 LYS A CA  
844  C C   . LYS A 107 ? 0.9463 0.8437 0.8976 -0.4327 0.0822  -0.0785 107 LYS A C   
845  O O   . LYS A 107 ? 0.9439 0.8753 0.9406 -0.4384 0.0822  -0.0767 107 LYS A O   
846  C CB  . LYS A 107 ? 0.9355 0.7377 0.8100 -0.4253 0.1220  -0.0894 107 LYS A CB  
847  C CG  . LYS A 107 ? 0.8760 0.6524 0.7497 -0.4322 0.1467  -0.0949 107 LYS A CG  
848  C CD  . LYS A 107 ? 0.9835 0.7163 0.8154 -0.4405 0.1591  -0.1080 107 LYS A CD  
849  C CE  . LYS A 107 ? 1.0123 0.7152 0.8424 -0.4450 0.1849  -0.1123 107 LYS A CE  
850  N NZ  . LYS A 107 ? 1.1762 0.8375 0.9688 -0.4537 0.1992  -0.1263 107 LYS A NZ  
851  N N   . SER A 108 ? 1.1026 1.0069 1.0336 -0.4411 0.0561  -0.0819 108 SER A N   
852  C CA  . SER A 108 ? 1.0975 1.0524 1.0621 -0.4545 0.0215  -0.0811 108 SER A CA  
853  C C   . SER A 108 ? 1.0468 1.0457 1.0583 -0.4389 0.0097  -0.0685 108 SER A C   
854  O O   . SER A 108 ? 1.0340 1.0816 1.1010 -0.4446 -0.0052 -0.0668 108 SER A O   
855  C CB  . SER A 108 ? 1.1262 1.0710 1.0481 -0.4650 -0.0042 -0.0850 108 SER A CB  
856  O OG  . SER A 108 ? 1.1049 1.0369 1.0004 -0.4479 -0.0086 -0.0775 108 SER A OG  
857  N N   . GLY A 109 ? 0.9138 0.8974 0.9075 -0.4186 0.0170  -0.0602 109 GLY A N   
858  C CA  . GLY A 109 ? 0.8979 0.9185 0.9331 -0.4009 0.0121  -0.0485 109 GLY A CA  
859  C C   . GLY A 109 ? 0.8032 0.8292 0.8228 -0.3786 -0.0104 -0.0390 109 GLY A C   
860  O O   . GLY A 109 ? 0.9179 0.9284 0.8997 -0.3908 -0.0294 -0.0424 109 GLY A O   
861  N N   . GLN A 110 ? 0.8366 0.8819 0.8823 -0.3478 -0.0068 -0.0277 110 GLN A N   
862  C CA  . GLN A 110 ? 0.7892 0.8391 0.8245 -0.3237 -0.0242 -0.0180 110 GLN A CA  
863  C C   . GLN A 110 ? 0.7886 0.7878 0.7648 -0.3176 -0.0121 -0.0201 110 GLN A C   
864  O O   . GLN A 110 ? 0.8041 0.7784 0.7406 -0.3376 -0.0198 -0.0278 110 GLN A O   
865  C CB  . GLN A 110 ? 0.7783 0.8614 0.8286 -0.3335 -0.0645 -0.0149 110 GLN A CB  
866  C CG  . GLN A 110 ? 0.8138 0.9038 0.8590 -0.3085 -0.0833 -0.0033 110 GLN A CG  
867  C CD  . GLN A 110 ? 0.7725 0.8995 0.8730 -0.2810 -0.0808 0.0059  110 GLN A CD  
868  O OE1 . GLN A 110 ? 0.7512 0.8974 0.8921 -0.2799 -0.0622 0.0033  110 GLN A OE1 
869  N NE2 . GLN A 110 ? 0.7513 0.8852 0.8518 -0.2600 -0.0974 0.0157  110 GLN A NE2 
870  N N   . SER A 111 ? 0.7439 0.7274 0.7149 -0.2909 0.0070  -0.0141 111 SER A N   
871  C CA  . SER A 111 ? 0.6914 0.6300 0.6182 -0.2825 0.0214  -0.0164 111 SER A CA  
872  C C   . SER A 111 ? 0.7413 0.6804 0.6493 -0.2713 0.0027  -0.0123 111 SER A C   
873  O O   . SER A 111 ? 0.7131 0.6827 0.6452 -0.2547 -0.0137 -0.0030 111 SER A O   
874  C CB  . SER A 111 ? 0.6843 0.6068 0.6154 -0.2593 0.0462  -0.0107 111 SER A CB  
875  O OG  . SER A 111 ? 0.6569 0.5432 0.5566 -0.2469 0.0563  -0.0116 111 SER A OG  
876  N N   . GLN A 112 ? 0.6573 0.5592 0.5218 -0.2810 0.0079  -0.0201 112 GLN A N   
877  C CA  . GLN A 112 ? 0.6870 0.5793 0.5263 -0.2723 -0.0027 -0.0179 112 GLN A CA  
878  C C   . GLN A 112 ? 0.6738 0.5407 0.5043 -0.2493 0.0188  -0.0174 112 GLN A C   
879  O O   . GLN A 112 ? 0.7508 0.6072 0.5621 -0.2419 0.0149  -0.0171 112 GLN A O   
880  C CB  . GLN A 112 ? 0.7201 0.5866 0.5138 -0.3014 -0.0103 -0.0283 112 GLN A CB  
881  C CG  . GLN A 112 ? 0.7799 0.6686 0.5775 -0.3281 -0.0358 -0.0295 112 GLN A CG  
882  C CD  . GLN A 112 ? 0.8516 0.7081 0.5931 -0.3592 -0.0431 -0.0404 112 GLN A CD  
883  O OE1 . GLN A 112 ? 0.9152 0.7337 0.6160 -0.3598 -0.0277 -0.0470 112 GLN A OE1 
884  N NE2 . GLN A 112 ? 0.8832 0.7544 0.6226 -0.3863 -0.0661 -0.0430 112 GLN A NE2 
885  N N   . LEU A 113 ? 0.6705 0.5264 0.5146 -0.2386 0.0403  -0.0171 113 LEU A N   
886  C CA  . LEU A 113 ? 0.6509 0.4822 0.4903 -0.2177 0.0582  -0.0163 113 LEU A CA  
887  C C   . LEU A 113 ? 0.6822 0.5358 0.5462 -0.1893 0.0538  -0.0042 113 LEU A C   
888  O O   . LEU A 113 ? 0.7089 0.5460 0.5740 -0.1711 0.0658  -0.0017 113 LEU A O   
889  C CB  . LEU A 113 ? 0.7424 0.5414 0.5779 -0.2228 0.0824  -0.0218 113 LEU A CB  
890  C CG  . LEU A 113 ? 0.7532 0.5230 0.5616 -0.2517 0.0918  -0.0366 113 LEU A CG  
891  C CD1 . LEU A 113 ? 0.7546 0.4935 0.5641 -0.2568 0.1156  -0.0408 113 LEU A CD1 
892  C CD2 . LEU A 113 ? 0.7180 0.4634 0.5003 -0.2532 0.0969  -0.0456 113 LEU A CD2 
893  N N   . GLY A 114 ? 0.7619 0.6515 0.6463 -0.1857 0.0365  0.0029  114 GLY A N   
894  C CA  . GLY A 114 ? 0.6092 0.5189 0.5149 -0.1613 0.0339  0.0125  114 GLY A CA  
895  C C   . GLY A 114 ? 0.6541 0.6006 0.5908 -0.1635 0.0242  0.0172  114 GLY A C   
896  O O   . GLY A 114 ? 0.6246 0.5831 0.5707 -0.1834 0.0192  0.0137  114 GLY A O   
897  N N   . ARG A 115 ? 0.5972 0.5622 0.5525 -0.1433 0.0223  0.0242  115 ARG A N   
898  C CA  . ARG A 115 ? 0.6473 0.6476 0.6389 -0.1419 0.0176  0.0277  115 ARG A CA  
899  C C   . ARG A 115 ? 0.5887 0.5864 0.5865 -0.1267 0.0355  0.0314  115 ARG A C   
900  O O   . ARG A 115 ? 0.5988 0.5888 0.5868 -0.1080 0.0364  0.0349  115 ARG A O   
901  C CB  . ARG A 115 ? 0.6925 0.7191 0.7018 -0.1340 -0.0045 0.0318  115 ARG A CB  
902  C CG  . ARG A 115 ? 0.7967 0.8626 0.8536 -0.1323 -0.0098 0.0343  115 ARG A CG  
903  C CD  . ARG A 115 ? 0.8762 0.9655 0.9526 -0.1266 -0.0358 0.0395  115 ARG A CD  
904  N NE  . ARG A 115 ? 0.9646 1.0504 1.0246 -0.1459 -0.0572 0.0389  115 ARG A NE  
905  C CZ  . ARG A 115 ? 1.0079 1.1172 1.0928 -0.1636 -0.0720 0.0379  115 ARG A CZ  
906  N NH1 . ARG A 115 ? 0.9078 1.0491 1.0424 -0.1642 -0.0659 0.0367  115 ARG A NH1 
907  N NH2 . ARG A 115 ? 1.0040 1.1041 1.0630 -0.1827 -0.0929 0.0374  115 ARG A NH2 
908  N N   . TRP A 116 ? 0.6132 0.6151 0.6243 -0.1366 0.0500  0.0302  116 TRP A N   
909  C CA  . TRP A 116 ? 0.6407 0.6331 0.6483 -0.1270 0.0695  0.0337  116 TRP A CA  
910  C C   . TRP A 116 ? 0.6074 0.6344 0.6528 -0.1231 0.0726  0.0336  116 TRP A C   
911  O O   . TRP A 116 ? 0.6605 0.7184 0.7425 -0.1349 0.0660  0.0301  116 TRP A O   
912  C CB  . TRP A 116 ? 0.7098 0.6761 0.7018 -0.1416 0.0884  0.0327  116 TRP A CB  
913  C CG  . TRP A 116 ? 0.6599 0.6117 0.6416 -0.1357 0.1088  0.0375  116 TRP A CG  
914  C CD1 . TRP A 116 ? 0.6702 0.5912 0.6190 -0.1210 0.1143  0.0444  116 TRP A CD1 
915  C CD2 . TRP A 116 ? 0.6459 0.6116 0.6480 -0.1463 0.1265  0.0356  116 TRP A CD2 
916  N NE1 . TRP A 116 ? 0.6812 0.5920 0.6208 -0.1226 0.1334  0.0479  116 TRP A NE1 
917  C CE2 . TRP A 116 ? 0.6728 0.6101 0.6449 -0.1384 0.1437  0.0418  116 TRP A CE2 
918  C CE3 . TRP A 116 ? 0.6279 0.6276 0.6722 -0.1628 0.1293  0.0289  116 TRP A CE3 
919  C CZ2 . TRP A 116 ? 0.6761 0.6141 0.6536 -0.1475 0.1672  0.0409  116 TRP A CZ2 
920  C CZ3 . TRP A 116 ? 0.6159 0.6209 0.6748 -0.1707 0.1531  0.0271  116 TRP A CZ3 
921  C CH2 . TRP A 116 ? 0.6298 0.6024 0.6527 -0.1637 0.1736  0.0328  116 TRP A CH2 
922  N N   . MET A 117 ? 0.5953 0.6170 0.6334 -0.1072 0.0826  0.0367  117 MET A N   
923  C CA  . MET A 117 ? 0.5920 0.6402 0.6632 -0.1028 0.0927  0.0347  117 MET A CA  
924  C C   . MET A 117 ? 0.5819 0.6047 0.6262 -0.1010 0.1179  0.0363  117 MET A C   
925  O O   . MET A 117 ? 0.6337 0.6254 0.6367 -0.0908 0.1180  0.0412  117 MET A O   
926  C CB  . MET A 117 ? 0.5806 0.6473 0.6679 -0.0848 0.0784  0.0356  117 MET A CB  
927  C CG  . MET A 117 ? 0.6459 0.7378 0.7706 -0.0785 0.0915  0.0320  117 MET A CG  
928  S SD  . MET A 117 ? 0.6739 0.7822 0.8178 -0.0568 0.0758  0.0330  117 MET A SD  
929  C CE  . MET A 117 ? 0.6506 0.7831 0.8223 -0.0625 0.0431  0.0364  117 MET A CE  
930  N N   . SER A 118 ? 0.6161 0.6511 0.6832 -0.1120 0.1386  0.0321  118 SER A N   
931  C CA  . SER A 118 ? 0.7640 0.7704 0.7989 -0.1138 0.1648  0.0338  118 SER A CA  
932  C C   . SER A 118 ? 0.7642 0.7657 0.7840 -0.0963 0.1678  0.0342  118 SER A C   
933  O O   . SER A 118 ? 0.7059 0.7325 0.7529 -0.0838 0.1545  0.0315  118 SER A O   
934  C CB  . SER A 118 ? 0.6998 0.7219 0.7660 -0.1316 0.1902  0.0272  118 SER A CB  
935  O OG  . SER A 118 ? 0.7429 0.8051 0.8619 -0.1264 0.1946  0.0198  118 SER A OG  
936  N N   . GLU A 119 ? 0.7629 0.7278 0.7350 -0.0967 0.1850  0.0379  119 GLU A N   
937  C CA  . GLU A 119 ? 0.8144 0.7693 0.7638 -0.0838 0.1898  0.0371  119 GLU A CA  
938  C C   . GLU A 119 ? 0.8306 0.8147 0.8218 -0.0850 0.2100  0.0264  119 GLU A C   
939  O O   . GLU A 119 ? 0.8701 0.8622 0.8669 -0.0718 0.2078  0.0223  119 GLU A O   
940  C CB  . GLU A 119 ? 0.9407 0.8463 0.8236 -0.0870 0.2014  0.0446  119 GLU A CB  
941  C CG  . GLU A 119 ? 1.0213 0.8968 0.8704 -0.0854 0.1837  0.0557  119 GLU A CG  
942  C CD  . GLU A 119 ? 1.2339 1.0603 1.0247 -0.0932 0.1970  0.0653  119 GLU A CD  
943  O OE1 . GLU A 119 ? 1.3488 1.1629 1.1206 -0.1031 0.2223  0.0628  119 GLU A OE1 
944  O OE2 . GLU A 119 ? 1.2535 1.0516 1.0175 -0.0897 0.1829  0.0755  119 GLU A OE2 
945  N N   . GLU A 120 ? 0.8562 0.8566 0.8808 -0.1009 0.2311  0.0207  120 GLU A N   
946  C CA  . GLU A 120 ? 0.8642 0.8960 0.9403 -0.1020 0.2527  0.0091  120 GLU A CA  
947  C C   . GLU A 120 ? 0.7565 0.8342 0.8968 -0.0887 0.2297  0.0059  120 GLU A C   
948  O O   . GLU A 120 ? 0.7192 0.8122 0.8859 -0.0770 0.2365  -0.0007 120 GLU A O   
949  C CB  . GLU A 120 ? 0.8057 0.8477 0.9104 -0.1235 0.2800  0.0031  120 GLU A CB  
950  C CG  . GLU A 120 ? 0.9680 0.9607 1.0078 -0.1388 0.3069  0.0067  120 GLU A CG  
951  C CD  . GLU A 120 ? 1.0171 0.9805 1.0171 -0.1460 0.2914  0.0183  120 GLU A CD  
952  O OE1 . GLU A 120 ? 0.8936 0.8741 0.9132 -0.1397 0.2613  0.0219  120 GLU A OE1 
953  O OE2 . GLU A 120 ? 1.1058 1.0259 1.0532 -0.1585 0.3104  0.0238  120 GLU A OE2 
954  N N   . ASP A 121 ? 0.7147 0.8111 0.8776 -0.0909 0.2026  0.0106  121 ASP A N   
955  C CA  . ASP A 121 ? 0.6840 0.8194 0.9011 -0.0799 0.1772  0.0101  121 ASP A CA  
956  C C   . ASP A 121 ? 0.6289 0.7514 0.8199 -0.0599 0.1595  0.0142  121 ASP A C   
957  O O   . ASP A 121 ? 0.6116 0.7579 0.8425 -0.0469 0.1514  0.0118  121 ASP A O   
958  C CB  . ASP A 121 ? 0.6637 0.8149 0.8980 -0.0906 0.1520  0.0143  121 ASP A CB  
959  C CG  . ASP A 121 ? 0.7010 0.8670 0.9652 -0.1124 0.1682  0.0090  121 ASP A CG  
960  O OD1 . ASP A 121 ? 0.7393 0.9196 1.0366 -0.1169 0.1961  0.0010  121 ASP A OD1 
961  O OD2 . ASP A 121 ? 0.7414 0.9036 0.9963 -0.1262 0.1552  0.0116  121 ASP A OD2 
962  N N   . PHE A 122 ? 0.6450 0.7295 0.7724 -0.0572 0.1534  0.0202  122 PHE A N   
963  C CA  . PHE A 122 ? 0.6490 0.7220 0.7533 -0.0404 0.1365  0.0231  122 PHE A CA  
964  C C   . PHE A 122 ? 0.7258 0.7934 0.8269 -0.0304 0.1546  0.0166  122 PHE A C   
965  O O   . PHE A 122 ? 0.6449 0.7200 0.7586 -0.0163 0.1435  0.0153  122 PHE A O   
966  C CB  . PHE A 122 ? 0.6681 0.7050 0.7135 -0.0403 0.1261  0.0301  122 PHE A CB  
967  C CG  . PHE A 122 ? 0.6434 0.6665 0.6636 -0.0250 0.1132  0.0314  122 PHE A CG  
968  C CD1 . PHE A 122 ? 0.6093 0.6485 0.6510 -0.0158 0.0918  0.0323  122 PHE A CD1 
969  C CD2 . PHE A 122 ? 0.6254 0.6182 0.5992 -0.0213 0.1220  0.0319  122 PHE A CD2 
970  C CE1 . PHE A 122 ? 0.5673 0.5936 0.5879 -0.0035 0.0819  0.0325  122 PHE A CE1 
971  C CE2 . PHE A 122 ? 0.6887 0.6710 0.6428 -0.0090 0.1093  0.0318  122 PHE A CE2 
972  C CZ  . PHE A 122 ? 0.6436 0.6434 0.6231 -0.0001 0.0906  0.0315  122 PHE A CZ  
973  N N   . GLU A 123 ? 0.6946 0.7450 0.7745 -0.0390 0.1841  0.0118  123 GLU A N   
974  C CA  . GLU A 123 ? 0.7295 0.7706 0.8011 -0.0327 0.2053  0.0033  123 GLU A CA  
975  C C   . GLU A 123 ? 0.6622 0.7419 0.8066 -0.0249 0.2121  -0.0053 123 GLU A C   
976  O O   . GLU A 123 ? 0.6443 0.7228 0.7945 -0.0121 0.2146  -0.0107 123 GLU A O   
977  C CB  . GLU A 123 ? 0.8097 0.8218 0.8404 -0.0472 0.2379  -0.0003 123 GLU A CB  
978  C CG  . GLU A 123 ? 0.9204 0.8869 0.8724 -0.0508 0.2303  0.0092  123 GLU A CG  
979  C CD  . GLU A 123 ? 1.1814 1.1119 1.0824 -0.0649 0.2616  0.0067  123 GLU A CD  
980  O OE1 . GLU A 123 ? 1.1689 1.1102 1.0963 -0.0728 0.2935  -0.0045 123 GLU A OE1 
981  O OE2 . GLU A 123 ? 1.3189 1.2092 1.1535 -0.0683 0.2546  0.0162  123 GLU A OE2 
982  N N   . LYS A 124 ? 0.6505 0.7643 0.8539 -0.0323 0.2143  -0.0068 124 LYS A N   
983  C CA  . LYS A 124 ? 0.5639 0.7187 0.8467 -0.0229 0.2137  -0.0126 124 LYS A CA  
984  C C   . LYS A 124 ? 0.5708 0.7365 0.8679 -0.0064 0.1778  -0.0048 124 LYS A C   
985  O O   . LYS A 124 ? 0.5571 0.7349 0.8900 0.0083  0.1781  -0.0087 124 LYS A O   
986  C CB  . LYS A 124 ? 0.5786 0.7701 0.9233 -0.0357 0.2174  -0.0145 124 LYS A CB  
987  C CG  . LYS A 124 ? 0.6442 0.8237 0.9757 -0.0549 0.2551  -0.0222 124 LYS A CG  
988  C CD  . LYS A 124 ? 0.6267 0.8477 1.0301 -0.0682 0.2590  -0.0260 124 LYS A CD  
989  C CE  . LYS A 124 ? 0.7783 0.9843 1.1667 -0.0894 0.2997  -0.0341 124 LYS A CE  
990  N NZ  . LYS A 124 ? 0.8706 1.0298 1.1729 -0.1015 0.2984  -0.0252 124 LYS A NZ  
991  N N   . ALA A 125 ? 0.5729 0.7310 0.8408 -0.0095 0.1487  0.0057  125 ALA A N   
992  C CA  . ALA A 125 ? 0.5558 0.7190 0.8292 0.0030  0.1164  0.0132  125 ALA A CA  
993  C C   . ALA A 125 ? 0.5821 0.7165 0.8128 0.0157  0.1173  0.0121  125 ALA A C   
994  O O   . ALA A 125 ? 0.5643 0.7044 0.8142 0.0292  0.1032  0.0139  125 ALA A O   
995  C CB  . ALA A 125 ? 0.4868 0.6456 0.7358 -0.0067 0.0904  0.0224  125 ALA A CB  
996  N N   . PHE A 126 ? 0.5922 0.6941 0.7646 0.0108  0.1325  0.0095  126 PHE A N   
997  C CA  . PHE A 126 ? 0.5824 0.6572 0.7129 0.0203  0.1321  0.0074  126 PHE A CA  
998  C C   . PHE A 126 ? 0.6151 0.6935 0.7709 0.0295  0.1528  -0.0032 126 PHE A C   
999  O O   . PHE A 126 ? 0.6258 0.7002 0.7853 0.0420  0.1438  -0.0043 126 PHE A O   
1000 C CB  . PHE A 126 ? 0.6098 0.6501 0.6742 0.0117  0.1404  0.0083  126 PHE A CB  
1001 C CG  . PHE A 126 ? 0.6656 0.6790 0.6859 0.0191  0.1374  0.0058  126 PHE A CG  
1002 C CD1 . PHE A 126 ? 0.6112 0.6168 0.6134 0.0252  0.1121  0.0115  126 PHE A CD1 
1003 C CD2 . PHE A 126 ? 0.6521 0.6469 0.6478 0.0180  0.1609  -0.0034 126 PHE A CD2 
1004 C CE1 . PHE A 126 ? 0.6289 0.6125 0.5950 0.0306  0.1082  0.0083  126 PHE A CE1 
1005 C CE2 . PHE A 126 ? 0.6405 0.6103 0.5938 0.0226  0.1559  -0.0065 126 PHE A CE2 
1006 C CZ  . PHE A 126 ? 0.5849 0.5509 0.5260 0.0291  0.1285  -0.0005 126 PHE A CZ  
1007 N N   . ASN A 127 ? 0.5825 0.6666 0.7565 0.0227  0.1834  -0.0120 127 ASN A N   
1008 C CA  . ASN A 127 ? 0.5978 0.6822 0.7959 0.0300  0.2093  -0.0248 127 ASN A CA  
1009 C C   . ASN A 127 ? 0.5286 0.6471 0.8053 0.0445  0.2003  -0.0251 127 ASN A C   
1010 O O   . ASN A 127 ? 0.5290 0.6467 0.8313 0.0540  0.2194  -0.0355 127 ASN A O   
1011 C CB  . ASN A 127 ? 0.6091 0.6892 0.8067 0.0166  0.2484  -0.0355 127 ASN A CB  
1012 C CG  . ASN A 127 ? 0.6757 0.7132 0.7877 0.0033  0.2597  -0.0351 127 ASN A CG  
1013 O OD1 . ASN A 127 ? 0.6706 0.6802 0.7275 0.0071  0.2457  -0.0322 127 ASN A OD1 
1014 N ND2 . ASN A 127 ? 0.7049 0.7364 0.8061 -0.0129 0.2843  -0.0376 127 ASN A ND2 
1015 N N   . ALA A 128 ? 0.4995 0.6453 0.8135 0.0460  0.1713  -0.0139 128 ALA A N   
1016 C CA  . ALA A 128 ? 0.4854 0.6614 0.8709 0.0602  0.1554  -0.0105 128 ALA A CA  
1017 C C   . ALA A 128 ? 0.5210 0.6838 0.8872 0.0722  0.1250  -0.0010 128 ALA A C   
1018 O O   . ALA A 128 ? 0.5001 0.6829 0.9163 0.0834  0.1046  0.0061  128 ALA A O   
1019 C CB  . ALA A 128 ? 0.3943 0.6082 0.8334 0.0529  0.1395  -0.0037 128 ALA A CB  
1020 N N   . ARG A 129 ? 0.5316 0.6608 0.8277 0.0696  0.1211  -0.0003 129 ARG A N   
1021 C CA  . ARG A 129 ? 0.4664 0.5820 0.7408 0.0774  0.0938  0.0082  129 ARG A CA  
1022 C C   . ARG A 129 ? 0.5259 0.6091 0.7557 0.0826  0.1045  0.0005  129 ARG A C   
1023 O O   . ARG A 129 ? 0.5180 0.5948 0.7626 0.0948  0.1000  -0.0001 129 ARG A O   
1024 C CB  . ARG A 129 ? 0.5212 0.6322 0.7588 0.0664  0.0702  0.0185  129 ARG A CB  
1025 C CG  . ARG A 129 ? 0.4595 0.5992 0.7359 0.0605  0.0510  0.0274  129 ARG A CG  
1026 C CD  . ARG A 129 ? 0.4539 0.5835 0.6873 0.0463  0.0364  0.0335  129 ARG A CD  
1027 N NE  . ARG A 129 ? 0.5043 0.6554 0.7653 0.0397  0.0122  0.0424  129 ARG A NE  
1028 C CZ  . ARG A 129 ? 0.5056 0.6835 0.8048 0.0307  0.0142  0.0418  129 ARG A CZ  
1029 N NH1 . ARG A 129 ? 0.5322 0.7182 0.8473 0.0267  0.0420  0.0328  129 ARG A NH1 
1030 N NH2 . ARG A 129 ? 0.4833 0.6790 0.8035 0.0236  -0.0122 0.0500  129 ARG A NH2 
1031 N N   . PHE A 130 ? 0.5087 0.5699 0.6837 0.0727  0.1174  -0.0050 130 PHE A N   
1032 C CA  . PHE A 130 ? 0.5606 0.5909 0.6845 0.0741  0.1190  -0.0104 130 PHE A CA  
1033 C C   . PHE A 130 ? 0.5969 0.6122 0.7196 0.0787  0.1458  -0.0250 130 PHE A C   
1034 O O   . PHE A 130 ? 0.6106 0.6051 0.7084 0.0831  0.1423  -0.0294 130 PHE A O   
1035 C CB  . PHE A 130 ? 0.5477 0.5596 0.6134 0.0619  0.1167  -0.0085 130 PHE A CB  
1036 C CG  . PHE A 130 ? 0.6598 0.6733 0.7125 0.0594  0.0894  0.0028  130 PHE A CG  
1037 C CD1 . PHE A 130 ? 0.5739 0.6050 0.6447 0.0530  0.0807  0.0109  130 PHE A CD1 
1038 C CD2 . PHE A 130 ? 0.5874 0.5842 0.6115 0.0621  0.0742  0.0037  130 PHE A CD2 
1039 C CE1 . PHE A 130 ? 0.5728 0.6018 0.6294 0.0493  0.0592  0.0191  130 PHE A CE1 
1040 C CE2 . PHE A 130 ? 0.5518 0.5489 0.5664 0.0589  0.0536  0.0120  130 PHE A CE2 
1041 C CZ  . PHE A 130 ? 0.5544 0.5661 0.5834 0.0525  0.0469  0.0194  130 PHE A CZ  
1042 N N   . PRO A 131 ? 0.6224 0.6451 0.7689 0.0761  0.1752  -0.0345 131 PRO A N   
1043 C CA  . PRO A 131 ? 0.6372 0.6419 0.7813 0.0796  0.2040  -0.0506 131 PRO A CA  
1044 C C   . PRO A 131 ? 0.5917 0.5970 0.7731 0.0958  0.1980  -0.0524 131 PRO A C   
1045 O O   . PRO A 131 ? 0.5246 0.5558 0.7729 0.1074  0.1924  -0.0473 131 PRO A O   
1046 C CB  . PRO A 131 ? 0.5755 0.5966 0.7584 0.0750  0.2357  -0.0590 131 PRO A CB  
1047 C CG  . PRO A 131 ? 0.6422 0.6711 0.8044 0.0617  0.2280  -0.0498 131 PRO A CG  
1048 C CD  . PRO A 131 ? 0.5142 0.5541 0.6767 0.0659  0.1880  -0.0334 131 PRO A CD  
1049 N N   . GLY A 132 ? 0.6235 0.5991 0.7620 0.0964  0.1978  -0.0593 132 GLY A N   
1050 C CA  . GLY A 132 ? 0.5604 0.5290 0.7259 0.1103  0.1937  -0.0615 132 GLY A CA  
1051 C C   . GLY A 132 ? 0.5846 0.5646 0.7697 0.1186  0.1585  -0.0444 132 GLY A C   
1052 O O   . GLY A 132 ? 0.6085 0.5875 0.8306 0.1320  0.1538  -0.0422 132 GLY A O   
1053 N N   . CYS A 133 ? 0.5300 0.5172 0.6888 0.1104  0.1347  -0.0323 133 CYS A N   
1054 C CA  . CYS A 133 ? 0.6012 0.5976 0.7746 0.1152  0.1038  -0.0166 133 CYS A CA  
1055 C C   . CYS A 133 ? 0.5833 0.5543 0.7266 0.1172  0.0919  -0.0166 133 CYS A C   
1056 O O   . CYS A 133 ? 0.6193 0.5909 0.7794 0.1234  0.0722  -0.0055 133 CYS A O   
1057 C CB  . CYS A 133 ? 0.5149 0.5245 0.6697 0.1041  0.0867  -0.0062 133 CYS A CB  
1058 S SG  . CYS A 133 ? 0.5450 0.5320 0.6279 0.0910  0.0827  -0.0094 133 CYS A SG  
1059 N N   . MET A 134 ? 0.5381 0.4856 0.6360 0.1107  0.1027  -0.0287 134 MET A N   
1060 C CA  . MET A 134 ? 0.6196 0.5439 0.6912 0.1105  0.0937  -0.0314 134 MET A CA  
1061 C C   . MET A 134 ? 0.7024 0.6065 0.7840 0.1179  0.1129  -0.0443 134 MET A C   
1062 O O   . MET A 134 ? 0.7385 0.6190 0.7882 0.1134  0.1137  -0.0531 134 MET A O   
1063 C CB  . MET A 134 ? 0.6021 0.5146 0.6196 0.0975  0.0883  -0.0362 134 MET A CB  
1064 C CG  . MET A 134 ? 0.5837 0.5110 0.5908 0.0908  0.0701  -0.0245 134 MET A CG  
1065 S SD  . MET A 134 ? 0.5615 0.4748 0.5167 0.0792  0.0598  -0.0289 134 MET A SD  
1066 C CE  . MET A 134 ? 0.5661 0.4977 0.5233 0.0744  0.0446  -0.0150 134 MET A CE  
1067 N N   . LYS A 135 ? 0.6940 0.6071 0.8227 0.1286  0.1291  -0.0466 135 LYS A N   
1068 C CA  . LYS A 135 ? 0.7171 0.6092 0.8597 0.1363  0.1518  -0.0606 135 LYS A CA  
1069 C C   . LYS A 135 ? 0.7522 0.6244 0.8971 0.1431  0.1379  -0.0556 135 LYS A C   
1070 O O   . LYS A 135 ? 0.7695 0.6511 0.9451 0.1520  0.1175  -0.0389 135 LYS A O   
1071 C CB  . LYS A 135 ? 0.6791 0.5892 0.8856 0.1488  0.1704  -0.0622 135 LYS A CB  
1072 C CG  . LYS A 135 ? 0.7601 0.6496 0.9725 0.1512  0.2075  -0.0838 135 LYS A CG  
1073 C CD  . LYS A 135 ? 0.7937 0.6705 0.9479 0.1331  0.2281  -0.0995 135 LYS A CD  
1074 C CE  . LYS A 135 ? 0.8320 0.6905 0.9940 0.1330  0.2704  -0.1220 135 LYS A CE  
1075 N NZ  . LYS A 135 ? 0.9663 0.7930 1.1265 0.1389  0.2807  -0.1339 135 LYS A NZ  
1076 N N   . GLY A 136 ? 0.7543 0.5967 0.8630 0.1370  0.1482  -0.0700 136 GLY A N   
1077 C CA  . GLY A 136 ? 0.7215 0.5402 0.8278 0.1407  0.1391  -0.0678 136 GLY A CA  
1078 C C   . GLY A 136 ? 0.7490 0.5660 0.8224 0.1309  0.1132  -0.0580 136 GLY A C   
1079 O O   . GLY A 136 ? 0.7022 0.4977 0.7709 0.1317  0.1067  -0.0560 136 GLY A O   
1080 N N   . ARG A 137 ? 0.7158 0.5527 0.7678 0.1213  0.1005  -0.0526 137 ARG A N   
1081 C CA  . ARG A 137 ? 0.6475 0.4848 0.6733 0.1117  0.0790  -0.0450 137 ARG A CA  
1082 C C   . ARG A 137 ? 0.6598 0.4915 0.6423 0.0976  0.0801  -0.0579 137 ARG A C   
1083 O O   . ARG A 137 ? 0.7535 0.5812 0.7189 0.0937  0.0947  -0.0703 137 ARG A O   
1084 C CB  . ARG A 137 ? 0.5913 0.4544 0.6295 0.1118  0.0617  -0.0280 137 ARG A CB  
1085 C CG  . ARG A 137 ? 0.6435 0.5153 0.7242 0.1244  0.0546  -0.0134 137 ARG A CG  
1086 C CD  . ARG A 137 ? 0.6249 0.5160 0.7070 0.1199  0.0338  0.0025  137 ARG A CD  
1087 N NE  . ARG A 137 ? 0.6698 0.5692 0.7901 0.1304  0.0217  0.0177  137 ARG A NE  
1088 C CZ  . ARG A 137 ? 0.6380 0.5195 0.7602 0.1341  0.0078  0.0292  137 ARG A CZ  
1089 N NH1 . ARG A 137 ? 0.5740 0.4281 0.6641 0.1277  0.0076  0.0260  137 ARG A NH1 
1090 N NH2 . ARG A 137 ? 0.6049 0.4953 0.7621 0.1437  -0.0072 0.0448  137 ARG A NH2 
1091 N N   . THR A 138 ? 0.5737 0.4039 0.5383 0.0891  0.0640  -0.0547 138 THR A N   
1092 C CA  . THR A 138 ? 0.6626 0.4921 0.5940 0.0765  0.0583  -0.0640 138 THR A CA  
1093 C C   . THR A 138 ? 0.6007 0.4525 0.5270 0.0734  0.0464  -0.0544 138 THR A C   
1094 O O   . THR A 138 ? 0.6362 0.4998 0.5777 0.0753  0.0362  -0.0416 138 THR A O   
1095 C CB  . THR A 138 ? 0.6082 0.4252 0.5318 0.0689  0.0495  -0.0679 138 THR A CB  
1096 O OG1 . THR A 138 ? 0.7012 0.4932 0.6259 0.0703  0.0620  -0.0781 138 THR A OG1 
1097 C CG2 . THR A 138 ? 0.6489 0.4710 0.5480 0.0568  0.0394  -0.0762 138 THR A CG2 
1098 N N   . MET A 139 ? 0.5612 0.4153 0.4628 0.0675  0.0480  -0.0604 139 MET A N   
1099 C CA  . MET A 139 ? 0.5767 0.4468 0.4698 0.0638  0.0363  -0.0519 139 MET A CA  
1100 C C   . MET A 139 ? 0.5499 0.4192 0.4296 0.0558  0.0201  -0.0549 139 MET A C   
1101 O O   . MET A 139 ? 0.5806 0.4394 0.4372 0.0491  0.0175  -0.0658 139 MET A O   
1102 C CB  . MET A 139 ? 0.6518 0.5212 0.5233 0.0614  0.0456  -0.0545 139 MET A CB  
1103 C CG  . MET A 139 ? 0.5324 0.4119 0.3894 0.0569  0.0327  -0.0458 139 MET A CG  
1104 S SD  . MET A 139 ? 0.6080 0.4779 0.4272 0.0509  0.0431  -0.0479 139 MET A SD  
1105 C CE  . MET A 139 ? 0.5634 0.4452 0.4138 0.0575  0.0652  -0.0441 139 MET A CE  
1106 N N   . TYR A 140 ? 0.5735 0.4539 0.4690 0.0555  0.0093  -0.0462 140 TYR A N   
1107 C CA  . TYR A 140 ? 0.5368 0.4206 0.4307 0.0487  -0.0041 -0.0492 140 TYR A CA  
1108 C C   . TYR A 140 ? 0.5758 0.4698 0.4600 0.0474  -0.0142 -0.0438 140 TYR A C   
1109 O O   . TYR A 140 ? 0.5305 0.4322 0.4182 0.0507  -0.0119 -0.0339 140 TYR A O   
1110 C CB  . TYR A 140 ? 0.5337 0.4202 0.4482 0.0474  -0.0064 -0.0442 140 TYR A CB  
1111 C CG  . TYR A 140 ? 0.5249 0.3959 0.4454 0.0479  0.0015  -0.0477 140 TYR A CG  
1112 C CD1 . TYR A 140 ? 0.5322 0.3923 0.4506 0.0411  0.0016  -0.0595 140 TYR A CD1 
1113 C CD2 . TYR A 140 ? 0.4729 0.3395 0.4027 0.0548  0.0076  -0.0388 140 TYR A CD2 
1114 C CE1 . TYR A 140 ? 0.5751 0.4165 0.4969 0.0409  0.0101  -0.0622 140 TYR A CE1 
1115 C CE2 . TYR A 140 ? 0.4945 0.3430 0.4292 0.0563  0.0134  -0.0398 140 TYR A CE2 
1116 C CZ  . TYR A 140 ? 0.5288 0.3628 0.4577 0.0493  0.0158  -0.0515 140 TYR A CZ  
1117 O OH  . TYR A 140 ? 0.6128 0.4242 0.5444 0.0502  0.0228  -0.0522 140 TYR A OH  
1118 N N   . VAL A 141 ? 0.5504 0.4432 0.4230 0.0422  -0.0264 -0.0500 141 VAL A N   
1119 C CA  . VAL A 141 ? 0.5092 0.4083 0.3733 0.0417  -0.0398 -0.0437 141 VAL A CA  
1120 C C   . VAL A 141 ? 0.5520 0.4634 0.4447 0.0407  -0.0509 -0.0428 141 VAL A C   
1121 O O   . VAL A 141 ? 0.5604 0.4736 0.4640 0.0360  -0.0586 -0.0521 141 VAL A O   
1122 C CB  . VAL A 141 ? 0.5635 0.4516 0.3942 0.0367  -0.0493 -0.0495 141 VAL A CB  
1123 C CG1 . VAL A 141 ? 0.4950 0.3859 0.3153 0.0373  -0.0656 -0.0396 141 VAL A CG1 
1124 C CG2 . VAL A 141 ? 0.5612 0.4338 0.3632 0.0358  -0.0322 -0.0537 141 VAL A CG2 
1125 N N   . ILE A 142 ? 0.5666 0.4859 0.4732 0.0438  -0.0500 -0.0332 142 ILE A N   
1126 C CA  . ILE A 142 ? 0.4992 0.4282 0.4357 0.0425  -0.0543 -0.0336 142 ILE A CA  
1127 C C   . ILE A 142 ? 0.5225 0.4572 0.4644 0.0455  -0.0683 -0.0278 142 ILE A C   
1128 O O   . ILE A 142 ? 0.5151 0.4485 0.4514 0.0487  -0.0656 -0.0180 142 ILE A O   
1129 C CB  . ILE A 142 ? 0.4647 0.3944 0.4123 0.0421  -0.0413 -0.0284 142 ILE A CB  
1130 C CG1 . ILE A 142 ? 0.4667 0.3882 0.4104 0.0403  -0.0310 -0.0316 142 ILE A CG1 
1131 C CG2 . ILE A 142 ? 0.5602 0.4959 0.5347 0.0387  -0.0412 -0.0308 142 ILE A CG2 
1132 C CD1 . ILE A 142 ? 0.4140 0.3333 0.3622 0.0388  -0.0226 -0.0246 142 ILE A CD1 
1133 N N   . PRO A 143 ? 0.5368 0.4773 0.4915 0.0445  -0.0845 -0.0332 143 PRO A N   
1134 C CA  . PRO A 143 ? 0.5703 0.5167 0.5401 0.0492  -0.0998 -0.0263 143 PRO A CA  
1135 C C   . PRO A 143 ? 0.5429 0.5004 0.5573 0.0498  -0.0935 -0.0292 143 PRO A C   
1136 O O   . PRO A 143 ? 0.5308 0.4970 0.5731 0.0451  -0.0911 -0.0404 143 PRO A O   
1137 C CB  . PRO A 143 ? 0.5665 0.5151 0.5324 0.0473  -0.1227 -0.0311 143 PRO A CB  
1138 C CG  . PRO A 143 ? 0.5029 0.4540 0.4753 0.0398  -0.1157 -0.0455 143 PRO A CG  
1139 C CD  . PRO A 143 ? 0.5301 0.4713 0.4856 0.0389  -0.0917 -0.0453 143 PRO A CD  
1140 N N   . PHE A 144 ? 0.5092 0.4646 0.5300 0.0539  -0.0881 -0.0207 144 PHE A N   
1141 C CA  . PHE A 144 ? 0.5493 0.5109 0.6080 0.0528  -0.0769 -0.0252 144 PHE A CA  
1142 C C   . PHE A 144 ? 0.5773 0.5382 0.6534 0.0604  -0.0837 -0.0170 144 PHE A C   
1143 O O   . PHE A 144 ? 0.5380 0.4887 0.5872 0.0648  -0.0901 -0.0051 144 PHE A O   
1144 C CB  . PHE A 144 ? 0.5403 0.4943 0.5866 0.0463  -0.0547 -0.0259 144 PHE A CB  
1145 C CG  . PHE A 144 ? 0.5423 0.4872 0.5610 0.0480  -0.0499 -0.0146 144 PHE A CG  
1146 C CD1 . PHE A 144 ? 0.5608 0.5010 0.5466 0.0490  -0.0517 -0.0092 144 PHE A CD1 
1147 C CD2 . PHE A 144 ? 0.5473 0.4879 0.5751 0.0475  -0.0414 -0.0110 144 PHE A CD2 
1148 C CE1 . PHE A 144 ? 0.4925 0.4268 0.4587 0.0492  -0.0458 -0.0001 144 PHE A CE1 
1149 C CE2 . PHE A 144 ? 0.5365 0.4693 0.5407 0.0470  -0.0368 -0.0017 144 PHE A CE2 
1150 C CZ  . PHE A 144 ? 0.4797 0.4110 0.4550 0.0478  -0.0393 0.0039  144 PHE A CZ  
1151 N N   . SER A 145 ? 0.5971 0.5670 0.7199 0.0614  -0.0802 -0.0239 145 SER A N   
1152 C CA  . SER A 145 ? 0.6406 0.6092 0.7908 0.0697  -0.0844 -0.0179 145 SER A CA  
1153 C C   . SER A 145 ? 0.6281 0.5908 0.7947 0.0644  -0.0578 -0.0240 145 SER A C   
1154 O O   . SER A 145 ? 0.5948 0.5630 0.7835 0.0565  -0.0420 -0.0371 145 SER A O   
1155 C CB  . SER A 145 ? 0.6414 0.6265 0.8416 0.0769  -0.1043 -0.0218 145 SER A CB  
1156 O OG  . SER A 145 ? 0.6325 0.6162 0.8696 0.0864  -0.1059 -0.0170 145 SER A OG  
1157 N N   . MET A 146 ? 0.6234 0.5720 0.7751 0.0667  -0.0516 -0.0150 146 MET A N   
1158 C CA  . MET A 146 ? 0.6215 0.5606 0.7854 0.0606  -0.0272 -0.0210 146 MET A CA  
1159 C C   . MET A 146 ? 0.5765 0.5195 0.7962 0.0693  -0.0274 -0.0251 146 MET A C   
1160 O O   . MET A 146 ? 0.5262 0.4645 0.7546 0.0811  -0.0426 -0.0140 146 MET A O   
1161 C CB  . MET A 146 ? 0.5915 0.5137 0.7161 0.0575  -0.0203 -0.0111 146 MET A CB  
1162 C CG  . MET A 146 ? 0.5173 0.4385 0.5963 0.0502  -0.0199 -0.0071 146 MET A CG  
1163 S SD  . MET A 146 ? 0.4271 0.3504 0.5003 0.0365  -0.0037 -0.0194 146 MET A SD  
1164 C CE  . MET A 146 ? 0.4985 0.4072 0.5823 0.0261  0.0205  -0.0273 146 MET A CE  
1165 N N   . GLY A 147 ? 0.6177 0.5675 0.8763 0.0634  -0.0096 -0.0409 147 GLY A N   
1166 C CA  . GLY A 147 ? 0.6489 0.6072 0.9729 0.0722  -0.0082 -0.0478 147 GLY A CA  
1167 C C   . GLY A 147 ? 0.6792 0.6631 1.0455 0.0772  -0.0267 -0.0535 147 GLY A C   
1168 O O   . GLY A 147 ? 0.6674 0.6591 1.0059 0.0740  -0.0420 -0.0512 147 GLY A O   
1169 N N   . PRO A 148 ? 0.8664 0.8642 1.3041 0.0845  -0.0250 -0.0623 148 PRO A N   
1170 C CA  . PRO A 148 ? 0.8457 0.8718 1.3328 0.0878  -0.0434 -0.0696 148 PRO A CA  
1171 C C   . PRO A 148 ? 0.8865 0.9200 1.3532 0.0980  -0.0855 -0.0534 148 PRO A C   
1172 O O   . PRO A 148 ? 0.9228 0.9446 1.3744 0.1100  -0.1043 -0.0364 148 PRO A O   
1173 C CB  . PRO A 148 ? 0.7786 0.8169 1.3518 0.0971  -0.0350 -0.0790 148 PRO A CB  
1174 C CG  . PRO A 148 ? 0.7985 0.8120 1.3604 0.0906  0.0023  -0.0851 148 PRO A CG  
1175 C CD  . PRO A 148 ? 0.7954 0.7840 1.2764 0.0885  -0.0030 -0.0685 148 PRO A CD  
1176 N N   . LEU A 149 ? 0.8140 0.8632 1.2759 0.0915  -0.0990 -0.0591 149 LEU A N   
1177 C CA  . LEU A 149 ? 0.8777 0.9311 1.3123 0.0971  -0.1374 -0.0465 149 LEU A CA  
1178 C C   . LEU A 149 ? 0.9054 0.9737 1.3967 0.1129  -0.1695 -0.0389 149 LEU A C   
1179 O O   . LEU A 149 ? 0.9336 1.0234 1.5038 0.1170  -0.1658 -0.0502 149 LEU A O   
1180 C CB  . LEU A 149 ? 0.9161 0.9822 1.3389 0.0849  -0.1420 -0.0578 149 LEU A CB  
1181 C CG  . LEU A 149 ? 0.8539 0.9207 1.2380 0.0855  -0.1776 -0.0489 149 LEU A CG  
1182 C CD1 . LEU A 149 ? 0.8086 0.8675 1.1410 0.0714  -0.1657 -0.0565 149 LEU A CD1 
1183 C CD2 . LEU A 149 ? 0.8415 0.9356 1.2853 0.0899  -0.2094 -0.0531 149 LEU A CD2 
1184 N N   . GLY A 150 ? 0.9182 0.9737 1.3696 0.1214  -0.2010 -0.0192 150 GLY A N   
1185 C CA  . GLY A 150 ? 0.9318 0.9949 1.4261 0.1373  -0.2367 -0.0069 150 GLY A CA  
1186 C C   . GLY A 150 ? 0.9945 1.0431 1.5133 0.1481  -0.2235 0.0015  150 GLY A C   
1187 O O   . GLY A 150 ? 0.9919 1.0348 1.5137 0.1564  -0.2464 0.0161  150 GLY A O   
1188 N N   . SER A 151 ? 0.9795 1.0193 1.5111 0.1466  -0.1858 -0.0080 151 SER A N   
1189 C CA  . SER A 151 ? 1.0155 1.0376 1.5640 0.1542  -0.1695 -0.0020 151 SER A CA  
1190 C C   . SER A 151 ? 1.1344 1.1250 1.6183 0.1606  -0.1851 0.0215  151 SER A C   
1191 O O   . SER A 151 ? 1.0831 1.0577 1.4994 0.1523  -0.1797 0.0259  151 SER A O   
1192 C CB  . SER A 151 ? 0.9296 0.9442 1.4931 0.1467  -0.1235 -0.0191 151 SER A CB  
1193 O OG  . SER A 151 ? 1.0070 0.9995 1.5749 0.1518  -0.1067 -0.0135 151 SER A OG  
1194 N N   . PRO A 152 ? 1.2464 1.2263 1.7389 0.1707  -0.1998 0.0362  152 PRO A N   
1195 C CA  . PRO A 152 ? 1.2639 1.2102 1.6919 0.1749  -0.2117 0.0586  152 PRO A CA  
1196 C C   . PRO A 152 ? 1.2807 1.1999 1.6798 0.1717  -0.1801 0.0583  152 PRO A C   
1197 O O   . PRO A 152 ? 1.3244 1.2150 1.6626 0.1712  -0.1861 0.0748  152 PRO A O   
1198 C CB  . PRO A 152 ? 1.2713 1.2136 1.7302 0.1871  -0.2289 0.0709  152 PRO A CB  
1199 C CG  . PRO A 152 ? 1.2151 1.1932 1.7440 0.1884  -0.2397 0.0580  152 PRO A CG  
1200 C CD  . PRO A 152 ? 1.1698 1.1672 1.7306 0.1784  -0.2083 0.0336  152 PRO A CD  
1201 N N   . LEU A 153 ? 1.2365 1.1616 1.6744 0.1671  -0.1453 0.0395  153 LEU A N   
1202 C CA  . LEU A 153 ? 1.1000 1.0008 1.5039 0.1578  -0.1114 0.0358  153 LEU A CA  
1203 C C   . LEU A 153 ? 1.1087 1.0158 1.4597 0.1383  -0.0933 0.0251  153 LEU A C   
1204 O O   . LEU A 153 ? 1.0511 0.9452 1.3782 0.1263  -0.0632 0.0175  153 LEU A O   
1205 C CB  . LEU A 153 ? 1.0057 0.9042 1.4695 0.1594  -0.0802 0.0206  153 LEU A CB  
1206 C CG  . LEU A 153 ? 1.0736 0.9764 1.5827 0.1721  -0.0938 0.0276  153 LEU A CG  
1207 C CD1 . LEU A 153 ? 1.0622 0.9748 1.6339 0.1687  -0.0623 0.0072  153 LEU A CD1 
1208 C CD2 . LEU A 153 ? 1.1113 0.9800 1.5835 0.1800  -0.1026 0.0486  153 LEU A CD2 
1209 N N   . ALA A 154 ? 0.9778 0.9033 1.3106 0.1346  -0.1121 0.0245  154 ALA A N   
1210 C CA  . ALA A 154 ? 0.8401 0.7709 1.1263 0.1185  -0.0983 0.0160  154 ALA A CA  
1211 C C   . ALA A 154 ? 0.8101 0.7286 1.0277 0.1161  -0.1150 0.0310  154 ALA A C   
1212 O O   . ALA A 154 ? 0.8147 0.7277 1.0213 0.1250  -0.1439 0.0452  154 ALA A O   
1213 C CB  . ALA A 154 ? 0.7976 0.7560 1.1157 0.1141  -0.1012 0.0008  154 ALA A CB  
1214 N N   . LYS A 155 ? 0.6541 0.5673 0.8254 0.1034  -0.0966 0.0276  155 LYS A N   
1215 C CA  . LYS A 155 ? 0.6674 0.5695 0.7771 0.0993  -0.1047 0.0386  155 LYS A CA  
1216 C C   . LYS A 155 ? 0.6402 0.5569 0.7297 0.0905  -0.1030 0.0292  155 LYS A C   
1217 O O   . LYS A 155 ? 0.5805 0.5077 0.6852 0.0830  -0.0853 0.0159  155 LYS A O   
1218 C CB  . LYS A 155 ? 0.6838 0.5666 0.7608 0.0929  -0.0848 0.0441  155 LYS A CB  
1219 C CG  . LYS A 155 ? 0.6909 0.5587 0.7962 0.0984  -0.0761 0.0473  155 LYS A CG  
1220 C CD  . LYS A 155 ? 0.7468 0.5904 0.8124 0.0936  -0.0662 0.0580  155 LYS A CD  
1221 C CE  . LYS A 155 ? 0.8957 0.7201 0.9357 0.1021  -0.0883 0.0770  155 LYS A CE  
1222 N NZ  . LYS A 155 ? 0.8208 0.6374 0.9032 0.1174  -0.1039 0.0839  155 LYS A NZ  
1223 N N   . ILE A 156 ? 0.6661 0.5792 0.7180 0.0904  -0.1205 0.0361  156 ILE A N   
1224 C CA  . ILE A 156 ? 0.6008 0.5250 0.6357 0.0837  -0.1222 0.0271  156 ILE A CA  
1225 C C   . ILE A 156 ? 0.6019 0.5159 0.5877 0.0762  -0.1075 0.0297  156 ILE A C   
1226 O O   . ILE A 156 ? 0.6432 0.5404 0.5959 0.0764  -0.1078 0.0411  156 ILE A O   
1227 C CB  . ILE A 156 ? 0.5546 0.4816 0.5839 0.0873  -0.1519 0.0301  156 ILE A CB  
1228 C CG1 . ILE A 156 ? 0.5571 0.5022 0.6487 0.0943  -0.1663 0.0245  156 ILE A CG1 
1229 C CG2 . ILE A 156 ? 0.6051 0.5360 0.6043 0.0788  -0.1516 0.0214  156 ILE A CG2 
1230 C CD1 . ILE A 156 ? 0.6210 0.5719 0.7135 0.0971  -0.2005 0.0273  156 ILE A CD1 
1231 N N   . GLY A 157 ? 0.5789 0.5024 0.5629 0.0693  -0.0942 0.0191  157 GLY A N   
1232 C CA  . GLY A 157 ? 0.5834 0.5013 0.5321 0.0636  -0.0808 0.0204  157 GLY A CA  
1233 C C   . GLY A 157 ? 0.5480 0.4700 0.4813 0.0604  -0.0829 0.0125  157 GLY A C   
1234 O O   . GLY A 157 ? 0.5155 0.4467 0.4685 0.0599  -0.0903 0.0036  157 GLY A O   
1235 N N   . ILE A 158 ? 0.5768 0.4912 0.4769 0.0574  -0.0743 0.0149  158 ILE A N   
1236 C CA  . ILE A 158 ? 0.5235 0.4380 0.4073 0.0543  -0.0707 0.0068  158 ILE A CA  
1237 C C   . ILE A 158 ? 0.5354 0.4527 0.4190 0.0522  -0.0513 0.0062  158 ILE A C   
1238 O O   . ILE A 158 ? 0.5130 0.4256 0.3815 0.0513  -0.0426 0.0128  158 ILE A O   
1239 C CB  . ILE A 158 ? 0.5303 0.4303 0.3733 0.0525  -0.0787 0.0089  158 ILE A CB  
1240 C CG1 . ILE A 158 ? 0.5308 0.4280 0.3733 0.0543  -0.1040 0.0111  158 ILE A CG1 
1241 C CG2 . ILE A 158 ? 0.5916 0.4887 0.4184 0.0485  -0.0695 -0.0015 158 ILE A CG2 
1242 C CD1 . ILE A 158 ? 0.6254 0.5352 0.4930 0.0529  -0.1139 -0.0009 158 ILE A CD1 
1243 N N   . GLU A 159 ? 0.5070 0.4313 0.4082 0.0509  -0.0454 -0.0010 159 GLU A N   
1244 C CA  . GLU A 159 ? 0.4720 0.3990 0.3758 0.0499  -0.0317 -0.0003 159 GLU A CA  
1245 C C   . GLU A 159 ? 0.5248 0.4477 0.4188 0.0506  -0.0265 -0.0072 159 GLU A C   
1246 O O   . GLU A 159 ? 0.4769 0.3968 0.3714 0.0496  -0.0317 -0.0154 159 GLU A O   
1247 C CB  . GLU A 159 ? 0.4437 0.3756 0.3693 0.0472  -0.0283 -0.0010 159 GLU A CB  
1248 C CG  . GLU A 159 ? 0.4711 0.4047 0.3988 0.0465  -0.0198 0.0014  159 GLU A CG  
1249 C CD  . GLU A 159 ? 0.5244 0.4590 0.4620 0.0412  -0.0178 0.0046  159 GLU A CD  
1250 O OE1 . GLU A 159 ? 0.5196 0.4525 0.4634 0.0374  -0.0188 0.0029  159 GLU A OE1 
1251 O OE2 . GLU A 159 ? 0.4765 0.4124 0.4158 0.0403  -0.0153 0.0087  159 GLU A OE2 
1252 N N   . LEU A 160 ? 0.4833 0.4061 0.3718 0.0520  -0.0151 -0.0049 160 LEU A N   
1253 C CA  . LEU A 160 ? 0.4923 0.4105 0.3782 0.0540  -0.0058 -0.0117 160 LEU A CA  
1254 C C   . LEU A 160 ? 0.5184 0.4440 0.4286 0.0568  0.0001  -0.0079 160 LEU A C   
1255 O O   . LEU A 160 ? 0.5147 0.4495 0.4349 0.0569  0.0029  -0.0004 160 LEU A O   
1256 C CB  . LEU A 160 ? 0.4796 0.3906 0.3434 0.0534  0.0048  -0.0133 160 LEU A CB  
1257 C CG  . LEU A 160 ? 0.5488 0.4480 0.3791 0.0490  -0.0032 -0.0133 160 LEU A CG  
1258 C CD1 . LEU A 160 ? 0.5477 0.4342 0.3490 0.0457  0.0118  -0.0160 160 LEU A CD1 
1259 C CD2 . LEU A 160 ? 0.5548 0.4480 0.3771 0.0470  -0.0173 -0.0210 160 LEU A CD2 
1260 N N   . THR A 161 ? 0.4908 0.4111 0.4096 0.0584  0.0005  -0.0126 161 THR A N   
1261 C CA  . THR A 161 ? 0.4968 0.4199 0.4352 0.0612  0.0018  -0.0068 161 THR A CA  
1262 C C   . THR A 161 ? 0.4681 0.3798 0.4113 0.0659  0.0081  -0.0129 161 THR A C   
1263 O O   . THR A 161 ? 0.4999 0.4007 0.4305 0.0640  0.0098  -0.0230 161 THR A O   
1264 C CB  . THR A 161 ? 0.4759 0.3985 0.4180 0.0557  -0.0066 -0.0025 161 THR A CB  
1265 O OG1 . THR A 161 ? 0.4637 0.3846 0.4169 0.0569  -0.0081 0.0049  161 THR A OG1 
1266 C CG2 . THR A 161 ? 0.4484 0.3613 0.3849 0.0516  -0.0092 -0.0112 161 THR A CG2 
1267 N N   . ASP A 162 ? 0.4271 0.3411 0.3903 0.0719  0.0107  -0.0067 162 ASP A N   
1268 C CA  . ASP A 162 ? 0.5048 0.4050 0.4775 0.0780  0.0159  -0.0100 162 ASP A CA  
1269 C C   . ASP A 162 ? 0.5090 0.3994 0.4857 0.0765  0.0065  -0.0020 162 ASP A C   
1270 O O   . ASP A 162 ? 0.5229 0.4022 0.5127 0.0833  0.0077  0.0014  162 ASP A O   
1271 C CB  . ASP A 162 ? 0.5027 0.4096 0.4997 0.0877  0.0262  -0.0087 162 ASP A CB  
1272 C CG  . ASP A 162 ? 0.5098 0.4361 0.5303 0.0900  0.0186  0.0043  162 ASP A CG  
1273 O OD1 . ASP A 162 ? 0.4902 0.4220 0.5013 0.0828  0.0064  0.0117  162 ASP A OD1 
1274 O OD2 . ASP A 162 ? 0.5412 0.4772 0.5916 0.0984  0.0253  0.0061  162 ASP A OD2 
1275 N N   . SER A 163 ? 0.5033 0.3946 0.4678 0.0674  -0.0017 0.0011  163 SER A N   
1276 C CA  . SER A 163 ? 0.5017 0.3802 0.4617 0.0623  -0.0087 0.0087  163 SER A CA  
1277 C C   . SER A 163 ? 0.5066 0.3724 0.4522 0.0529  -0.0062 -0.0004 163 SER A C   
1278 O O   . SER A 163 ? 0.4893 0.3643 0.4302 0.0464  -0.0070 -0.0052 163 SER A O   
1279 C CB  . SER A 163 ? 0.5054 0.3946 0.4643 0.0571  -0.0176 0.0193  163 SER A CB  
1280 O OG  . SER A 163 ? 0.5406 0.4130 0.4845 0.0481  -0.0229 0.0250  163 SER A OG  
1281 N N   . PRO A 164 ? 0.5089 0.3537 0.4508 0.0517  -0.0025 -0.0035 164 PRO A N   
1282 C CA  . PRO A 164 ? 0.5447 0.3788 0.4774 0.0404  0.0013  -0.0129 164 PRO A CA  
1283 C C   . PRO A 164 ? 0.5675 0.3972 0.4906 0.0293  -0.0005 -0.0075 164 PRO A C   
1284 O O   . PRO A 164 ? 0.5406 0.3701 0.4634 0.0196  0.0044  -0.0169 164 PRO A O   
1285 C CB  . PRO A 164 ? 0.5970 0.4059 0.5273 0.0415  0.0072  -0.0157 164 PRO A CB  
1286 C CG  . PRO A 164 ? 0.6081 0.4106 0.5450 0.0528  0.0033  -0.0022 164 PRO A CG  
1287 C CD  . PRO A 164 ? 0.5117 0.3410 0.4613 0.0608  -0.0002 0.0007  164 PRO A CD  
1288 N N   . TYR A 165 ? 0.5283 0.3541 0.4443 0.0296  -0.0070 0.0064  165 TYR A N   
1289 C CA  . TYR A 165 ? 0.5524 0.3722 0.4528 0.0169  -0.0076 0.0105  165 TYR A CA  
1290 C C   . TYR A 165 ? 0.5866 0.4281 0.4946 0.0141  -0.0061 0.0043  165 TYR A C   
1291 O O   . TYR A 165 ? 0.5629 0.3997 0.4649 0.0026  0.0004  -0.0009 165 TYR A O   
1292 C CB  . TYR A 165 ? 0.5772 0.3889 0.4660 0.0172  -0.0191 0.0273  165 TYR A CB  
1293 C CG  . TYR A 165 ? 0.5938 0.3988 0.4605 0.0025  -0.0205 0.0314  165 TYR A CG  
1294 C CD1 . TYR A 165 ? 0.5926 0.3671 0.4299 -0.0124 -0.0157 0.0331  165 TYR A CD1 
1295 C CD2 . TYR A 165 ? 0.5533 0.3787 0.4250 0.0016  -0.0248 0.0327  165 TYR A CD2 
1296 C CE1 . TYR A 165 ? 0.6333 0.3975 0.4448 -0.0282 -0.0143 0.0350  165 TYR A CE1 
1297 C CE2 . TYR A 165 ? 0.6251 0.4413 0.4742 -0.0134 -0.0243 0.0346  165 TYR A CE2 
1298 C CZ  . TYR A 165 ? 0.6478 0.4332 0.4658 -0.0285 -0.0188 0.0352  165 TYR A CZ  
1299 O OH  . TYR A 165 ? 0.6663 0.4386 0.4567 -0.0458 -0.0156 0.0352  165 TYR A OH  
1300 N N   . VAL A 166 ? 0.5673 0.4302 0.4888 0.0241  -0.0103 0.0047  166 VAL A N   
1301 C CA  . VAL A 166 ? 0.5021 0.3819 0.4298 0.0227  -0.0097 0.0005  166 VAL A CA  
1302 C C   . VAL A 166 ? 0.4870 0.3702 0.4243 0.0209  -0.0055 -0.0123 166 VAL A C   
1303 O O   . VAL A 166 ? 0.5223 0.4105 0.4662 0.0155  -0.0029 -0.0170 166 VAL A O   
1304 C CB  . VAL A 166 ? 0.5147 0.4118 0.4500 0.0324  -0.0141 0.0053  166 VAL A CB  
1305 C CG1 . VAL A 166 ? 0.4649 0.3747 0.4041 0.0320  -0.0138 0.0015  166 VAL A CG1 
1306 C CG2 . VAL A 166 ? 0.5012 0.4006 0.4351 0.0322  -0.0200 0.0173  166 VAL A CG2 
1307 N N   . VAL A 167 ? 0.5224 0.4029 0.4631 0.0252  -0.0052 -0.0188 167 VAL A N   
1308 C CA  . VAL A 167 ? 0.5027 0.3887 0.4544 0.0227  -0.0051 -0.0313 167 VAL A CA  
1309 C C   . VAL A 167 ? 0.5037 0.3825 0.4629 0.0111  0.0024  -0.0380 167 VAL A C   
1310 O O   . VAL A 167 ? 0.5211 0.4113 0.4985 0.0081  0.0023  -0.0454 167 VAL A O   
1311 C CB  . VAL A 167 ? 0.5065 0.3867 0.4557 0.0263  -0.0053 -0.0382 167 VAL A CB  
1312 C CG1 . VAL A 167 ? 0.5136 0.4019 0.4741 0.0223  -0.0097 -0.0511 167 VAL A CG1 
1313 C CG2 . VAL A 167 ? 0.4738 0.3582 0.4151 0.0364  -0.0075 -0.0332 167 VAL A CG2 
1314 N N   . ALA A 168 ? 0.5377 0.3959 0.4842 0.0042  0.0097  -0.0353 168 ALA A N   
1315 C CA  . ALA A 168 ? 0.5307 0.3773 0.4801 -0.0096 0.0214  -0.0429 168 ALA A CA  
1316 C C   . ALA A 168 ? 0.5378 0.3885 0.4888 -0.0158 0.0265  -0.0419 168 ALA A C   
1317 O O   . ALA A 168 ? 0.5212 0.3764 0.4917 -0.0234 0.0359  -0.0530 168 ALA A O   
1318 C CB  . ALA A 168 ? 0.5750 0.3920 0.5013 -0.0166 0.0280  -0.0379 168 ALA A CB  
1319 N N   . SER A 169 ? 0.4947 0.3442 0.4286 -0.0133 0.0214  -0.0300 169 SER A N   
1320 C CA  . SER A 169 ? 0.5261 0.3758 0.4574 -0.0207 0.0273  -0.0300 169 SER A CA  
1321 C C   . SER A 169 ? 0.5104 0.3826 0.4706 -0.0139 0.0253  -0.0363 169 SER A C   
1322 O O   . SER A 169 ? 0.5382 0.4105 0.5114 -0.0207 0.0358  -0.0437 169 SER A O   
1323 C CB  . SER A 169 ? 0.5663 0.4107 0.4733 -0.0205 0.0195  -0.0161 169 SER A CB  
1324 O OG  . SER A 169 ? 0.5593 0.3807 0.4396 -0.0266 0.0179  -0.0079 169 SER A OG  
1325 N N   . MET A 170 ? 0.4918 0.3806 0.4613 -0.0009 0.0126  -0.0335 170 MET A N   
1326 C CA  . MET A 170 ? 0.4522 0.3584 0.4444 0.0060  0.0070  -0.0367 170 MET A CA  
1327 C C   . MET A 170 ? 0.4751 0.3891 0.4982 0.0038  0.0093  -0.0497 170 MET A C   
1328 O O   . MET A 170 ? 0.4703 0.3953 0.5194 0.0066  0.0079  -0.0534 170 MET A O   
1329 C CB  . MET A 170 ? 0.4278 0.3441 0.4135 0.0179  -0.0064 -0.0301 170 MET A CB  
1330 C CG  . MET A 170 ? 0.4704 0.3858 0.4374 0.0208  -0.0081 -0.0185 170 MET A CG  
1331 S SD  . MET A 170 ? 0.4745 0.3939 0.4461 0.0200  -0.0067 -0.0143 170 MET A SD  
1332 C CE  . MET A 170 ? 0.4086 0.3391 0.3947 0.0304  -0.0178 -0.0156 170 MET A CE  
1333 N N   . ARG A 171 ? 0.5115 0.4199 0.5358 -0.0011 0.0123  -0.0567 171 ARG A N   
1334 C CA  . ARG A 171 ? 0.4926 0.4100 0.5512 -0.0060 0.0158  -0.0706 171 ARG A CA  
1335 C C   . ARG A 171 ? 0.4925 0.4050 0.5687 -0.0165 0.0345  -0.0781 171 ARG A C   
1336 O O   . ARG A 171 ? 0.4851 0.4124 0.6031 -0.0171 0.0370  -0.0888 171 ARG A O   
1337 C CB  . ARG A 171 ? 0.4926 0.4010 0.5457 -0.0120 0.0183  -0.0773 171 ARG A CB  
1338 C CG  . ARG A 171 ? 0.5435 0.4656 0.6361 -0.0176 0.0188  -0.0928 171 ARG A CG  
1339 C CD  . ARG A 171 ? 0.5076 0.4178 0.5920 -0.0252 0.0225  -0.1001 171 ARG A CD  
1340 N NE  . ARG A 171 ? 0.5253 0.4539 0.6489 -0.0295 0.0166  -0.1149 171 ARG A NE  
1341 C CZ  . ARG A 171 ? 0.5831 0.5172 0.7427 -0.0411 0.0305  -0.1282 171 ARG A CZ  
1342 N NH1 . ARG A 171 ? 0.6162 0.5345 0.7716 -0.0510 0.0539  -0.1294 171 ARG A NH1 
1343 N NH2 . ARG A 171 ? 0.5536 0.5093 0.7544 -0.0443 0.0210  -0.1414 171 ARG A NH2 
1344 N N   . ILE A 172 ? 0.5048 0.3963 0.5506 -0.0253 0.0476  -0.0731 172 ILE A N   
1345 C CA  . ILE A 172 ? 0.5356 0.4166 0.5892 -0.0380 0.0690  -0.0815 172 ILE A CA  
1346 C C   . ILE A 172 ? 0.4948 0.3835 0.5593 -0.0324 0.0685  -0.0788 172 ILE A C   
1347 O O   . ILE A 172 ? 0.4788 0.3751 0.5804 -0.0338 0.0796  -0.0893 172 ILE A O   
1348 C CB  . ILE A 172 ? 0.5748 0.4240 0.5825 -0.0531 0.0823  -0.0773 172 ILE A CB  
1349 C CG1 . ILE A 172 ? 0.5460 0.3836 0.5461 -0.0589 0.0849  -0.0805 172 ILE A CG1 
1350 C CG2 . ILE A 172 ? 0.5203 0.3532 0.5253 -0.0690 0.1068  -0.0863 172 ILE A CG2 
1351 C CD1 . ILE A 172 ? 0.6013 0.4035 0.5518 -0.0721 0.0933  -0.0727 172 ILE A CD1 
1352 N N   . MET A 173 ? 0.4992 0.3862 0.5358 -0.0256 0.0565  -0.0651 173 MET A N   
1353 C CA  . MET A 173 ? 0.5072 0.3951 0.5461 -0.0233 0.0585  -0.0620 173 MET A CA  
1354 C C   . MET A 173 ? 0.4845 0.3935 0.5605 -0.0083 0.0461  -0.0617 173 MET A C   
1355 O O   . MET A 173 ? 0.4940 0.4022 0.5840 -0.0066 0.0518  -0.0625 173 MET A O   
1356 C CB  . MET A 173 ? 0.5236 0.4030 0.5219 -0.0234 0.0501  -0.0480 173 MET A CB  
1357 C CG  . MET A 173 ? 0.4606 0.3162 0.4200 -0.0389 0.0588  -0.0458 173 MET A CG  
1358 S SD  . MET A 173 ? 0.5531 0.3860 0.5086 -0.0590 0.0871  -0.0597 173 MET A SD  
1359 C CE  . MET A 173 ? 0.5333 0.3699 0.4952 -0.0562 0.0886  -0.0585 173 MET A CE  
1360 N N   . THR A 174 ? 0.4741 0.3988 0.5635 0.0018  0.0288  -0.0603 174 THR A N   
1361 C CA  . THR A 174 ? 0.4769 0.4182 0.5944 0.0153  0.0125  -0.0577 174 THR A CA  
1362 C C   . THR A 174 ? 0.4714 0.4290 0.6266 0.0175  0.0044  -0.0676 174 THR A C   
1363 O O   . THR A 174 ? 0.4351 0.3908 0.5940 0.0082  0.0135  -0.0771 174 THR A O   
1364 C CB  . THR A 174 ? 0.4675 0.4101 0.5549 0.0247  -0.0053 -0.0439 174 THR A CB  
1365 O OG1 . THR A 174 ? 0.4841 0.4284 0.5543 0.0248  -0.0134 -0.0440 174 THR A OG1 
1366 C CG2 . THR A 174 ? 0.3937 0.3236 0.4484 0.0209  0.0022  -0.0351 174 THR A CG2 
1367 N N   . ARG A 175 ? 0.4245 0.3969 0.6080 0.0291  -0.0139 -0.0649 175 ARG A N   
1368 C CA  . ARG A 175 ? 0.4680 0.4586 0.6842 0.0320  -0.0304 -0.0719 175 ARG A CA  
1369 C C   . ARG A 175 ? 0.5388 0.5279 0.7162 0.0359  -0.0505 -0.0638 175 ARG A C   
1370 O O   . ARG A 175 ? 0.5070 0.4951 0.6677 0.0451  -0.0674 -0.0523 175 ARG A O   
1371 C CB  . ARG A 175 ? 0.4397 0.4461 0.7078 0.0424  -0.0432 -0.0721 175 ARG A CB  
1372 C CG  . ARG A 175 ? 0.4765 0.4901 0.8008 0.0380  -0.0223 -0.0862 175 ARG A CG  
1373 C CD  . ARG A 175 ? 0.4977 0.4944 0.8149 0.0372  -0.0007 -0.0839 175 ARG A CD  
1374 N NE  . ARG A 175 ? 0.5711 0.5737 0.9466 0.0344  0.0202  -0.0984 175 ARG A NE  
1375 C CZ  . ARG A 175 ? 0.5166 0.5039 0.8960 0.0319  0.0433  -0.1013 175 ARG A CZ  
1376 N NH1 . ARG A 175 ? 0.4948 0.4617 0.8240 0.0312  0.0461  -0.0901 175 ARG A NH1 
1377 N NH2 . ARG A 175 ? 0.5777 0.5702 1.0143 0.0287  0.0655  -0.1172 175 ARG A NH2 
1378 N N   . MET A 176 ? 0.5219 0.5076 0.6830 0.0280  -0.0467 -0.0703 176 MET A N   
1379 C CA  . MET A 176 ? 0.5118 0.4910 0.6325 0.0296  -0.0585 -0.0652 176 MET A CA  
1380 C C   . MET A 176 ? 0.4925 0.4816 0.6277 0.0256  -0.0717 -0.0759 176 MET A C   
1381 O O   . MET A 176 ? 0.4954 0.4904 0.6606 0.0171  -0.0625 -0.0885 176 MET A O   
1382 C CB  . MET A 176 ? 0.4822 0.4440 0.5664 0.0243  -0.0416 -0.0625 176 MET A CB  
1383 C CG  . MET A 176 ? 0.5524 0.5062 0.5981 0.0278  -0.0489 -0.0569 176 MET A CG  
1384 S SD  . MET A 176 ? 0.6057 0.5548 0.6457 0.0209  -0.0500 -0.0691 176 MET A SD  
1385 C CE  . MET A 176 ? 0.5379 0.4720 0.5770 0.0120  -0.0268 -0.0719 176 MET A CE  
1386 N N   . GLY A 177 ? 0.5286 0.5175 0.6403 0.0296  -0.0921 -0.0716 177 GLY A N   
1387 C CA  . GLY A 177 ? 0.5753 0.5699 0.6909 0.0234  -0.1057 -0.0823 177 GLY A CA  
1388 C C   . GLY A 177 ? 0.5946 0.5926 0.6951 0.0282  -0.1349 -0.0763 177 GLY A C   
1389 O O   . GLY A 177 ? 0.6173 0.6097 0.6986 0.0366  -0.1428 -0.0629 177 GLY A O   
1390 N N   . THR A 178 ? 0.5893 0.5941 0.6959 0.0208  -0.1514 -0.0869 178 THR A N   
1391 C CA  . THR A 178 ? 0.6906 0.6950 0.7748 0.0219  -0.1824 -0.0821 178 THR A CA  
1392 C C   . THR A 178 ? 0.6952 0.7160 0.8173 0.0315  -0.2059 -0.0729 178 THR A C   
1393 O O   . THR A 178 ? 0.7255 0.7378 0.8177 0.0365  -0.2287 -0.0604 178 THR A O   
1394 C CB  . THR A 178 ? 0.6005 0.6084 0.6838 0.0092  -0.1952 -0.0974 178 THR A CB  
1395 O OG1 . THR A 178 ? 0.6364 0.6252 0.6859 0.0017  -0.1714 -0.1056 178 THR A OG1 
1396 C CG2 . THR A 178 ? 0.6952 0.6974 0.7430 0.0073  -0.2287 -0.0926 178 THR A CG2 
1397 N N   . SER A 179 ? 0.6709 0.7126 0.8582 0.0339  -0.1993 -0.0787 179 SER A N   
1398 C CA  . SER A 179 ? 0.6666 0.7247 0.9009 0.0449  -0.2196 -0.0707 179 SER A CA  
1399 C C   . SER A 179 ? 0.6942 0.7355 0.9009 0.0568  -0.2175 -0.0521 179 SER A C   
1400 O O   . SER A 179 ? 0.6561 0.7017 0.8825 0.0671  -0.2411 -0.0408 179 SER A O   
1401 C CB  . SER A 179 ? 0.6467 0.7275 0.9576 0.0444  -0.2032 -0.0830 179 SER A CB  
1402 O OG  . SER A 179 ? 0.6955 0.7637 0.9977 0.0426  -0.1659 -0.0848 179 SER A OG  
1403 N N   . VAL A 180 ? 0.6466 0.6685 0.8106 0.0555  -0.1908 -0.0483 180 VAL A N   
1404 C CA  . VAL A 180 ? 0.6634 0.6689 0.7998 0.0643  -0.1874 -0.0318 180 VAL A CA  
1405 C C   . VAL A 180 ? 0.7044 0.6921 0.7829 0.0651  -0.2095 -0.0196 180 VAL A C   
1406 O O   . VAL A 180 ? 0.7741 0.7514 0.8413 0.0734  -0.2224 -0.0044 180 VAL A O   
1407 C CB  . VAL A 180 ? 0.6004 0.5941 0.7154 0.0611  -0.1535 -0.0325 180 VAL A CB  
1408 C CG1 . VAL A 180 ? 0.6004 0.5793 0.6935 0.0684  -0.1488 -0.0173 180 VAL A CG1 
1409 C CG2 . VAL A 180 ? 0.5824 0.5880 0.7447 0.0570  -0.1317 -0.0450 180 VAL A CG2 
1410 N N   . LEU A 181 ? 0.7189 0.6991 0.7571 0.0556  -0.2126 -0.0265 181 LEU A N   
1411 C CA  . LEU A 181 ? 0.7433 0.7028 0.7205 0.0531  -0.2313 -0.0173 181 LEU A CA  
1412 C C   . LEU A 181 ? 0.7917 0.7566 0.7813 0.0563  -0.2715 -0.0100 181 LEU A C   
1413 O O   . LEU A 181 ? 0.8140 0.7583 0.7596 0.0586  -0.2894 0.0052  181 LEU A O   
1414 C CB  . LEU A 181 ? 0.7515 0.7004 0.6862 0.0408  -0.2231 -0.0296 181 LEU A CB  
1415 C CG  . LEU A 181 ? 0.7343 0.6706 0.6415 0.0387  -0.1884 -0.0325 181 LEU A CG  
1416 C CD1 . LEU A 181 ? 0.7001 0.6259 0.5751 0.0278  -0.1815 -0.0463 181 LEU A CD1 
1417 C CD2 . LEU A 181 ? 0.7074 0.6245 0.5737 0.0430  -0.1809 -0.0176 181 LEU A CD2 
1418 N N   . GLU A 182 ? 0.7984 0.7898 0.8478 0.0561  -0.2868 -0.0200 182 GLU A N   
1419 C CA  . GLU A 182 ? 0.7901 0.7909 0.8608 0.0599  -0.3295 -0.0127 182 GLU A CA  
1420 C C   . GLU A 182 ? 0.7679 0.7694 0.8719 0.0763  -0.3389 0.0044  182 GLU A C   
1421 O O   . GLU A 182 ? 0.8124 0.8021 0.8976 0.0817  -0.3724 0.0208  182 GLU A O   
1422 C CB  . GLU A 182 ? 0.7974 0.8305 0.9322 0.0544  -0.3415 -0.0301 182 GLU A CB  
1423 C CG  . GLU A 182 ? 0.8860 0.9156 0.9889 0.0373  -0.3328 -0.0478 182 GLU A CG  
1424 C CD  . GLU A 182 ? 0.9967 1.0577 1.1642 0.0296  -0.3441 -0.0657 182 GLU A CD  
1425 O OE1 . GLU A 182 ? 1.0185 1.1068 1.2600 0.0382  -0.3590 -0.0647 182 GLU A OE1 
1426 O OE2 . GLU A 182 ? 1.0106 1.0687 1.1580 0.0148  -0.3367 -0.0816 182 GLU A OE2 
1427 N N   . ALA A 183 ? 0.7775 0.7887 0.9275 0.0834  -0.3095 0.0012  183 ALA A N   
1428 C CA  . ALA A 183 ? 0.7202 0.7273 0.8995 0.0983  -0.3126 0.0160  183 ALA A CA  
1429 C C   . ALA A 183 ? 0.7493 0.7215 0.8579 0.1003  -0.3071 0.0338  183 ALA A C   
1430 O O   . ALA A 183 ? 0.7551 0.7143 0.8667 0.1113  -0.3230 0.0511  183 ALA A O   
1431 C CB  . ALA A 183 ? 0.6856 0.7085 0.9264 0.1021  -0.2789 0.0049  183 ALA A CB  
1432 N N   . LEU A 184 ? 0.7905 0.7465 0.8386 0.0898  -0.2840 0.0298  184 LEU A N   
1433 C CA  . LEU A 184 ? 0.7892 0.7138 0.7731 0.0894  -0.2748 0.0445  184 LEU A CA  
1434 C C   . LEU A 184 ? 0.8667 0.7680 0.7975 0.0881  -0.3091 0.0597  184 LEU A C   
1435 O O   . LEU A 184 ? 0.8514 0.7323 0.7672 0.0958  -0.3209 0.0784  184 LEU A O   
1436 C CB  . LEU A 184 ? 0.7459 0.6628 0.6871 0.0786  -0.2427 0.0348  184 LEU A CB  
1437 C CG  . LEU A 184 ? 0.8234 0.7107 0.7008 0.0757  -0.2294 0.0467  184 LEU A CG  
1438 C CD1 . LEU A 184 ? 0.7620 0.6435 0.6591 0.0839  -0.2157 0.0573  184 LEU A CD1 
1439 C CD2 . LEU A 184 ? 0.7413 0.6252 0.5855 0.0657  -0.2014 0.0355  184 LEU A CD2 
1440 N N   . GLY A 185 ? 0.8648 0.7650 0.7622 0.0771  -0.3251 0.0521  185 GLY A N   
1441 C CA  . GLY A 185 ? 0.8901 0.7651 0.7274 0.0710  -0.3517 0.0647  185 GLY A CA  
1442 C C   . GLY A 185 ? 1.0328 0.8706 0.7939 0.0656  -0.3323 0.0753  185 GLY A C   
1443 O O   . GLY A 185 ? 1.0396 0.8713 0.7737 0.0592  -0.3020 0.0659  185 GLY A O   
1444 N N   . ASP A 186 ? 1.1519 0.9682 0.8856 0.0665  -0.3420 0.0931  186 ASP A N   
1445 C CA  . ASP A 186 ? 1.1551 0.9358 0.8220 0.0605  -0.3223 0.1040  186 ASP A CA  
1446 C C   . ASP A 186 ? 1.1048 0.8807 0.7963 0.0718  -0.3044 0.1143  186 ASP A C   
1447 O O   . ASP A 186 ? 1.1300 0.8769 0.7753 0.0678  -0.2906 0.1259  186 ASP A O   
1448 C CB  . ASP A 186 ? 1.1900 0.9449 0.8066 0.0531  -0.3413 0.1174  186 ASP A CB  
1449 C CG  . ASP A 186 ? 1.2872 1.0379 0.8618 0.0378  -0.3536 0.1067  186 ASP A CG  
1450 O OD1 . ASP A 186 ? 1.2947 1.0493 0.8531 0.0293  -0.3361 0.0898  186 ASP A OD1 
1451 O OD2 . ASP A 186 ? 1.3308 1.0728 0.8880 0.0340  -0.3806 0.1151  186 ASP A OD2 
1452 N N   . GLY A 187 ? 0.9828 0.7852 0.7459 0.0845  -0.3026 0.1092  187 GLY A N   
1453 C CA  . GLY A 187 ? 0.9695 0.7660 0.7576 0.0942  -0.2847 0.1172  187 GLY A CA  
1454 C C   . GLY A 187 ? 1.0005 0.7942 0.7655 0.0854  -0.2432 0.1084  187 GLY A C   
1455 O O   . GLY A 187 ? 0.9727 0.7732 0.7150 0.0753  -0.2283 0.0948  187 GLY A O   
1456 N N   . GLU A 188 ? 0.9361 0.7198 0.7105 0.0893  -0.2242 0.1160  188 GLU A N   
1457 C CA  . GLU A 188 ? 0.9153 0.6992 0.6755 0.0810  -0.1871 0.1086  188 GLU A CA  
1458 C C   . GLU A 188 ? 0.8365 0.6547 0.6482 0.0813  -0.1689 0.0899  188 GLU A C   
1459 O O   . GLU A 188 ? 0.8118 0.6514 0.6756 0.0883  -0.1795 0.0832  188 GLU A O   
1460 C CB  . GLU A 188 ? 0.9577 0.7209 0.7149 0.0833  -0.1735 0.1211  188 GLU A CB  
1461 C CG  . GLU A 188 ? 1.1713 0.8945 0.8753 0.0828  -0.1906 0.1420  188 GLU A CG  
1462 C CD  . GLU A 188 ? 1.3126 1.0135 1.0189 0.0853  -0.1768 0.1541  188 GLU A CD  
1463 O OE1 . GLU A 188 ? 1.2650 0.9826 1.0102 0.0852  -0.1525 0.1446  188 GLU A OE1 
1464 O OE2 . GLU A 188 ? 1.4149 1.0801 1.0820 0.0858  -0.1901 0.1729  188 GLU A OE2 
1465 N N   . PHE A 189 ? 0.7702 0.5927 0.5675 0.0729  -0.1410 0.0816  189 PHE A N   
1466 C CA  . PHE A 189 ? 0.7534 0.6025 0.5902 0.0718  -0.1237 0.0666  189 PHE A CA  
1467 C C   . PHE A 189 ? 0.7540 0.6017 0.5793 0.0650  -0.0958 0.0652  189 PHE A C   
1468 O O   . PHE A 189 ? 0.7545 0.5849 0.5393 0.0593  -0.0875 0.0715  189 PHE A O   
1469 C CB  . PHE A 189 ? 0.7732 0.6368 0.6093 0.0684  -0.1287 0.0536  189 PHE A CB  
1470 C CG  . PHE A 189 ? 0.7570 0.6065 0.5398 0.0602  -0.1231 0.0523  189 PHE A CG  
1471 C CD1 . PHE A 189 ? 0.7708 0.6006 0.5107 0.0575  -0.1430 0.0585  189 PHE A CD1 
1472 C CD2 . PHE A 189 ? 0.7226 0.5773 0.4984 0.0547  -0.0980 0.0444  189 PHE A CD2 
1473 C CE1 . PHE A 189 ? 0.8322 0.6452 0.5194 0.0479  -0.1338 0.0551  189 PHE A CE1 
1474 C CE2 . PHE A 189 ? 0.7053 0.5466 0.4375 0.0474  -0.0889 0.0412  189 PHE A CE2 
1475 C CZ  . PHE A 189 ? 0.7991 0.6183 0.4850 0.0432  -0.1047 0.0455  189 PHE A CZ  
1476 N N   . ILE A 190 ? 0.6262 0.4916 0.4871 0.0643  -0.0817 0.0566  190 ILE A N   
1477 C CA  . ILE A 190 ? 0.6836 0.5520 0.5396 0.0573  -0.0593 0.0546  190 ILE A CA  
1478 C C   . ILE A 190 ? 0.6871 0.5664 0.5328 0.0533  -0.0516 0.0458  190 ILE A C   
1479 O O   . ILE A 190 ? 0.6463 0.5381 0.5087 0.0549  -0.0561 0.0368  190 ILE A O   
1480 C CB  . ILE A 190 ? 0.6577 0.5357 0.5493 0.0563  -0.0495 0.0502  190 ILE A CB  
1481 C CG1 . ILE A 190 ? 0.6598 0.5459 0.5489 0.0479  -0.0316 0.0468  190 ILE A CG1 
1482 C CG2 . ILE A 190 ? 0.7319 0.6241 0.6564 0.0598  -0.0559 0.0405  190 ILE A CG2 
1483 C CD1 . ILE A 190 ? 0.7460 0.6204 0.6225 0.0423  -0.0210 0.0543  190 ILE A CD1 
1484 N N   . LYS A 191 ? 0.6906 0.5637 0.5107 0.0479  -0.0384 0.0479  191 LYS A N   
1485 C CA  . LYS A 191 ? 0.6309 0.5119 0.4438 0.0453  -0.0286 0.0396  191 LYS A CA  
1486 C C   . LYS A 191 ? 0.5918 0.4916 0.4352 0.0439  -0.0171 0.0347  191 LYS A C   
1487 O O   . LYS A 191 ? 0.6290 0.5318 0.4796 0.0398  -0.0072 0.0386  191 LYS A O   
1488 C CB  . LYS A 191 ? 0.6493 0.5151 0.4255 0.0396  -0.0167 0.0426  191 LYS A CB  
1489 C CG  . LYS A 191 ? 0.7309 0.5718 0.4656 0.0387  -0.0297 0.0495  191 LYS A CG  
1490 C CD  . LYS A 191 ? 0.7785 0.5989 0.4712 0.0300  -0.0133 0.0529  191 LYS A CD  
1491 C CE  . LYS A 191 ? 0.8724 0.6615 0.5153 0.0274  -0.0287 0.0629  191 LYS A CE  
1492 N NZ  . LYS A 191 ? 1.0155 0.7790 0.6102 0.0162  -0.0095 0.0661  191 LYS A NZ  
1493 N N   . CYS A 192 ? 0.5124 0.4230 0.3720 0.0462  -0.0196 0.0267  192 CYS A N   
1494 C CA  . CYS A 192 ? 0.5293 0.4538 0.4134 0.0449  -0.0128 0.0237  192 CYS A CA  
1495 C C   . CYS A 192 ? 0.5384 0.4674 0.4224 0.0466  -0.0059 0.0178  192 CYS A C   
1496 O O   . CYS A 192 ? 0.5416 0.4659 0.4180 0.0490  -0.0101 0.0115  192 CYS A O   
1497 C CB  . CYS A 192 ? 0.5038 0.4321 0.4076 0.0453  -0.0201 0.0202  192 CYS A CB  
1498 S SG  . CYS A 192 ? 0.5019 0.4238 0.4140 0.0447  -0.0250 0.0246  192 CYS A SG  
1499 N N   . LEU A 193 ? 0.4870 0.4251 0.3825 0.0453  0.0046  0.0194  193 LEU A N   
1500 C CA  . LEU A 193 ? 0.5140 0.4570 0.4178 0.0486  0.0132  0.0143  193 LEU A CA  
1501 C C   . LEU A 193 ? 0.5398 0.4966 0.4725 0.0493  0.0117  0.0171  193 LEU A C   
1502 O O   . LEU A 193 ? 0.5344 0.5009 0.4791 0.0451  0.0128  0.0226  193 LEU A O   
1503 C CB  . LEU A 193 ? 0.5008 0.4415 0.3944 0.0467  0.0287  0.0135  193 LEU A CB  
1504 C CG  . LEU A 193 ? 0.5487 0.4971 0.4617 0.0506  0.0423  0.0076  193 LEU A CG  
1505 C CD1 . LEU A 193 ? 0.4852 0.4229 0.3895 0.0552  0.0416  -0.0012 193 LEU A CD1 
1506 C CD2 . LEU A 193 ? 0.5871 0.5334 0.4925 0.0464  0.0619  0.0056  193 LEU A CD2 
1507 N N   . HIS A 194 ? 0.5203 0.4758 0.4618 0.0534  0.0080  0.0137  194 HIS A N   
1508 C CA  . HIS A 194 ? 0.5010 0.4643 0.4641 0.0541  0.0031  0.0182  194 HIS A CA  
1509 C C   . HIS A 194 ? 0.5390 0.5018 0.5168 0.0621  0.0080  0.0150  194 HIS A C   
1510 O O   . HIS A 194 ? 0.4691 0.4206 0.4356 0.0652  0.0128  0.0071  194 HIS A O   
1511 C CB  . HIS A 194 ? 0.4910 0.4467 0.4481 0.0497  -0.0069 0.0192  194 HIS A CB  
1512 C CG  . HIS A 194 ? 0.4521 0.4079 0.4207 0.0493  -0.0134 0.0244  194 HIS A CG  
1513 N ND1 . HIS A 194 ? 0.4864 0.4310 0.4547 0.0526  -0.0151 0.0224  194 HIS A ND1 
1514 C CD2 . HIS A 194 ? 0.4640 0.4276 0.4421 0.0450  -0.0201 0.0325  194 HIS A CD2 
1515 C CE1 . HIS A 194 ? 0.5469 0.4900 0.5218 0.0511  -0.0232 0.0305  194 HIS A CE1 
1516 N NE2 . HIS A 194 ? 0.5406 0.4961 0.5214 0.0463  -0.0277 0.0367  194 HIS A NE2 
1517 N N   . SER A 195 ? 0.4660 0.4405 0.4705 0.0650  0.0058  0.0210  195 SER A N   
1518 C CA  . SER A 195 ? 0.5015 0.4748 0.5275 0.0745  0.0087  0.0200  195 SER A CA  
1519 C C   . SER A 195 ? 0.5750 0.5568 0.6243 0.0757  -0.0056 0.0312  195 SER A C   
1520 O O   . SER A 195 ? 0.4903 0.4874 0.5504 0.0704  -0.0120 0.0376  195 SER A O   
1521 C CB  . SER A 195 ? 0.5285 0.5093 0.5714 0.0801  0.0265  0.0135  195 SER A CB  
1522 O OG  . SER A 195 ? 0.5586 0.5397 0.6318 0.0907  0.0299  0.0130  195 SER A OG  
1523 N N   . VAL A 196 ? 0.5643 0.5335 0.6188 0.0817  -0.0116 0.0340  196 VAL A N   
1524 C CA  . VAL A 196 ? 0.5530 0.5257 0.6261 0.0836  -0.0285 0.0469  196 VAL A CA  
1525 C C   . VAL A 196 ? 0.6149 0.6098 0.7351 0.0932  -0.0276 0.0505  196 VAL A C   
1526 O O   . VAL A 196 ? 0.6510 0.6564 0.7927 0.0937  -0.0454 0.0625  196 VAL A O   
1527 C CB  . VAL A 196 ? 0.6087 0.5564 0.6711 0.0871  -0.0348 0.0502  196 VAL A CB  
1528 C CG1 . VAL A 196 ? 0.5632 0.4920 0.5852 0.0753  -0.0356 0.0466  196 VAL A CG1 
1529 C CG2 . VAL A 196 ? 0.5519 0.4907 0.6293 0.0993  -0.0202 0.0417  196 VAL A CG2 
1530 N N   . GLY A 197 ? 0.7914 0.7934 0.9289 0.0999  -0.0073 0.0400  197 GLY A N   
1531 C CA  . GLY A 197 ? 0.7774 0.8034 0.9657 0.1078  -0.0014 0.0407  197 GLY A CA  
1532 C C   . GLY A 197 ? 0.7683 0.7935 0.9981 0.1230  -0.0072 0.0464  197 GLY A C   
1533 O O   . GLY A 197 ? 0.7557 0.8047 1.0354 0.1292  -0.0149 0.0532  197 GLY A O   
1534 N N   . CYS A 198 ? 0.6816 0.6798 0.8949 0.1292  -0.0042 0.0438  198 CYS A N   
1535 C CA  . CYS A 198 ? 0.5948 0.5851 0.8453 0.1450  -0.0077 0.0490  198 CYS A CA  
1536 C C   . CYS A 198 ? 0.6229 0.5931 0.8685 0.1516  0.0190  0.0328  198 CYS A C   
1537 O O   . CYS A 198 ? 0.6117 0.5527 0.8305 0.1522  0.0185  0.0312  198 CYS A O   
1538 C CB  . CYS A 198 ? 0.6429 0.6122 0.8734 0.1441  -0.0337 0.0647  198 CYS A CB  
1539 S SG  . CYS A 198 ? 0.6726 0.6598 0.9038 0.1344  -0.0670 0.0839  198 CYS A SG  
1540 N N   . PRO A 199 ? 0.6270 0.6098 0.8955 0.1546  0.0442  0.0193  199 PRO A N   
1541 C CA  . PRO A 199 ? 0.6376 0.5983 0.8989 0.1592  0.0714  0.0021  199 PRO A CA  
1542 C C   . PRO A 199 ? 0.6855 0.6315 0.9856 0.1761  0.0712  0.0056  199 PRO A C   
1543 O O   . PRO A 199 ? 0.6863 0.6481 1.0378 0.1880  0.0560  0.0193  199 PRO A O   
1544 C CB  . PRO A 199 ? 0.6540 0.6330 0.9359 0.1575  0.0984  -0.0110 199 PRO A CB  
1545 C CG  . PRO A 199 ? 0.6425 0.6570 0.9728 0.1601  0.0844  0.0015  199 PRO A CG  
1546 C CD  . PRO A 199 ? 0.5794 0.5951 0.8808 0.1522  0.0512  0.0181  199 PRO A CD  
1547 N N   . LEU A 200 ? 0.6961 0.6102 0.9712 0.1769  0.0869  -0.0067 200 LEU A N   
1548 C CA  . LEU A 200 ? 0.7289 0.6207 1.0345 0.1923  0.0900  -0.0051 200 LEU A CA  
1549 C C   . LEU A 200 ? 0.7742 0.6682 1.1255 0.2035  0.1226  -0.0213 200 LEU A C   
1550 O O   . LEU A 200 ? 0.8030 0.6959 1.1316 0.1941  0.1493  -0.0403 200 LEU A O   
1551 C CB  . LEU A 200 ? 0.7417 0.5950 0.9969 0.1854  0.0914  -0.0114 200 LEU A CB  
1552 C CG  . LEU A 200 ? 0.7439 0.5924 0.9517 0.1718  0.0659  0.0002  200 LEU A CG  
1553 C CD1 . LEU A 200 ? 0.7697 0.5838 0.9324 0.1627  0.0723  -0.0104 200 LEU A CD1 
1554 C CD2 . LEU A 200 ? 0.6991 0.5510 0.9284 0.1789  0.0370  0.0243  200 LEU A CD2 
1555 N N   . PRO A 201 ? 0.7845 0.6807 1.1942 0.2209  0.1203  -0.0143 201 PRO A N   
1556 C CA  . PRO A 201 ? 0.8374 0.7309 1.2671 0.2307  0.0866  0.0091  201 PRO A CA  
1557 C C   . PRO A 201 ? 0.8195 0.7482 1.2741 0.2308  0.0565  0.0291  201 PRO A C   
1558 O O   . PRO A 201 ? 0.8102 0.7725 1.2904 0.2276  0.0644  0.0242  201 PRO A O   
1559 C CB  . PRO A 201 ? 0.8642 0.7544 1.3381 0.2431  0.0977  0.0048  201 PRO A CB  
1560 C CG  . PRO A 201 ? 0.8482 0.7614 1.3483 0.2400  0.1294  -0.0145 201 PRO A CG  
1561 C CD  . PRO A 201 ? 0.8178 0.7201 1.2615 0.2247  0.1488  -0.0304 201 PRO A CD  
1562 N N   . LEU A 202 ? 0.8348 0.7541 1.2780 0.2320  0.0221  0.0513  202 LEU A N   
1563 C CA  . LEU A 202 ? 0.9148 0.8629 1.3693 0.2278  -0.0095 0.0699  202 LEU A CA  
1564 C C   . LEU A 202 ? 0.9814 0.9624 1.4993 0.2372  -0.0187 0.0758  202 LEU A C   
1565 O O   . LEU A 202 ? 0.9382 0.9085 1.4822 0.2493  -0.0206 0.0791  202 LEU A O   
1566 C CB  . LEU A 202 ? 0.8997 0.8216 1.3113 0.2224  -0.0421 0.0908  202 LEU A CB  
1567 C CG  . LEU A 202 ? 0.8035 0.6993 1.1375 0.2037  -0.0369 0.0840  202 LEU A CG  
1568 C CD1 . LEU A 202 ? 0.8080 0.6796 1.1012 0.1957  -0.0674 0.1044  202 LEU A CD1 
1569 C CD2 . LEU A 202 ? 0.8144 0.7365 1.1238 0.1875  -0.0269 0.0719  202 LEU A CD2 
1570 N N   . LYS A 203 ? 1.0746 1.0952 1.6193 0.2313  -0.0242 0.0768  203 LYS A N   
1571 C CA  . LYS A 203 ? 1.1370 1.1926 1.7436 0.2374  -0.0368 0.0832  203 LYS A CA  
1572 C C   . LYS A 203 ? 1.1909 1.2490 1.7908 0.2352  -0.0821 0.1081  203 LYS A C   
1573 O O   . LYS A 203 ? 1.1908 1.2548 1.8286 0.2454  -0.0983 0.1180  203 LYS A O   
1574 C CB  . LYS A 203 ? 1.1521 1.2482 1.7905 0.2296  -0.0206 0.0717  203 LYS A CB  
1575 C CG  . LYS A 203 ? 1.1453 1.2372 1.7825 0.2283  0.0259  0.0466  203 LYS A CG  
1576 C CD  . LYS A 203 ? 1.1945 1.2772 1.8681 0.2404  0.0490  0.0353  203 LYS A CD  
1577 C CE  . LYS A 203 ? 1.1994 1.2758 1.8642 0.2348  0.0960  0.0093  203 LYS A CE  
1578 N NZ  . LYS A 203 ? 1.1918 1.2350 1.7859 0.2267  0.1091  0.0006  203 LYS A NZ  
1579 N N   . LYS A 204 ? 1.3219 1.3733 1.8713 0.2211  -0.1023 0.1180  204 LYS A N   
1580 C CA  . LYS A 204 ? 1.3349 1.3819 1.8570 0.2124  -0.1431 0.1397  204 LYS A CA  
1581 C C   . LYS A 204 ? 1.3213 1.3188 1.7823 0.2109  -0.1533 0.1501  204 LYS A C   
1582 O O   . LYS A 204 ? 1.2874 1.2582 1.7134 0.2093  -0.1323 0.1404  204 LYS A O   
1583 C CB  . LYS A 204 ? 1.3632 1.4304 1.8618 0.1939  -0.1547 0.1416  204 LYS A CB  
1584 C CG  . LYS A 204 ? 1.3797 1.4938 1.9333 0.1922  -0.1406 0.1299  204 LYS A CG  
1585 C CD  . LYS A 204 ? 1.4548 1.5833 1.9796 0.1735  -0.1485 0.1308  204 LYS A CD  
1586 C CE  . LYS A 204 ? 1.2953 1.4679 1.8733 0.1706  -0.1301 0.1181  204 LYS A CE  
1587 N NZ  . LYS A 204 ? 1.1903 1.3688 1.7189 0.1469  -0.1302 0.1139  204 LYS A NZ  
1588 N N   . PRO A 205 ? 1.2566 1.2393 1.7026 0.2103  -0.1843 0.1693  205 PRO A N   
1589 C CA  . PRO A 205 ? 1.2206 1.1531 1.6051 0.2068  -0.1918 0.1795  205 PRO A CA  
1590 C C   . PRO A 205 ? 1.1573 1.0726 1.4735 0.1856  -0.1971 0.1812  205 PRO A C   
1591 O O   . PRO A 205 ? 1.0939 1.0300 1.3986 0.1712  -0.2137 0.1854  205 PRO A O   
1592 C CB  . PRO A 205 ? 1.1816 1.1077 1.5713 0.2104  -0.2244 0.2002  205 PRO A CB  
1593 C CG  . PRO A 205 ? 1.2277 1.2004 1.6582 0.2058  -0.2429 0.2029  205 PRO A CG  
1594 C CD  . PRO A 205 ? 1.2363 1.2457 1.7205 0.2121  -0.2132 0.1824  205 PRO A CD  
1595 N N   . LEU A 206 ? 1.1029 0.9787 1.3746 0.1827  -0.1818 0.1768  206 LEU A N   
1596 C CA  . LEU A 206 ? 0.9983 0.8538 1.2064 0.1626  -0.1831 0.1764  206 LEU A CA  
1597 C C   . LEU A 206 ? 1.0285 0.8532 1.1789 0.1476  -0.2083 0.1943  206 LEU A C   
1598 O O   . LEU A 206 ? 1.0748 0.8772 1.2227 0.1546  -0.2184 0.2062  206 LEU A O   
1599 C CB  . LEU A 206 ? 0.9000 0.7289 1.0818 0.1617  -0.1519 0.1594  206 LEU A CB  
1600 C CG  . LEU A 206 ? 0.8733 0.7134 1.0156 0.1430  -0.1320 0.1405  206 LEU A CG  
1601 C CD1 . LEU A 206 ? 0.8043 0.6911 0.9861 0.1453  -0.1234 0.1298  206 LEU A CD1 
1602 C CD2 . LEU A 206 ? 0.8617 0.6780 0.9799 0.1413  -0.1034 0.1227  206 LEU A CD2 
1603 N N   . VAL A 207 ? 0.9323 0.7537 1.0340 0.1260  -0.2165 0.1954  207 VAL A N   
1604 C CA  . VAL A 207 ? 0.9689 0.7611 1.0089 0.1068  -0.2362 0.2089  207 VAL A CA  
1605 C C   . VAL A 207 ? 0.9980 0.7523 0.9717 0.0886  -0.2205 0.2020  207 VAL A C   
1606 O O   . VAL A 207 ? 0.9724 0.7433 0.9378 0.0793  -0.2026 0.1855  207 VAL A O   
1607 C CB  . VAL A 207 ? 0.9083 0.7287 0.9467 0.0934  -0.2597 0.2146  207 VAL A CB  
1608 C CG1 . VAL A 207 ? 0.9239 0.7092 0.8899 0.0700  -0.2753 0.2248  207 VAL A CG1 
1609 C CG2 . VAL A 207 ? 0.9513 0.8071 1.0568 0.1101  -0.2766 0.2216  207 VAL A CG2 
1610 N N   . ASN A 208 ? 0.9743 0.6838 0.9024 0.0815  -0.2201 0.2095  208 ASN A N   
1611 C CA  . ASN A 208 ? 0.9891 0.6586 0.8547 0.0625  -0.2024 0.2021  208 ASN A CA  
1612 C C   . ASN A 208 ? 0.9284 0.6101 0.8142 0.0682  -0.1686 0.1781  208 ASN A C   
1613 O O   . ASN A 208 ? 0.9596 0.6374 0.8128 0.0515  -0.1482 0.1622  208 ASN A O   
1614 C CB  . ASN A 208 ? 1.0260 0.6939 0.8400 0.0360  -0.2072 0.2003  208 ASN A CB  
1615 C CG  . ASN A 208 ? 1.0962 0.7487 0.8752 0.0228  -0.2294 0.2150  208 ASN A CG  
1616 O OD1 . ASN A 208 ? 1.1777 0.8103 0.9573 0.0307  -0.2393 0.2276  208 ASN A OD1 
1617 N ND2 . ASN A 208 ? 1.0508 0.7097 0.7971 0.0020  -0.2372 0.2129  208 ASN A ND2 
1618 N N   . ASN A 209 ? 0.9236 0.6227 0.8651 0.0909  -0.1608 0.1731  209 ASN A N   
1619 C CA  . ASN A 209 ? 0.9054 0.6187 0.8668 0.0962  -0.1293 0.1490  209 ASN A CA  
1620 C C   . ASN A 209 ? 0.8209 0.5707 0.7824 0.0864  -0.1172 0.1322  209 ASN A C   
1621 O O   . ASN A 209 ? 0.8562 0.6106 0.8135 0.0829  -0.0938 0.1129  209 ASN A O   
1622 C CB  . ASN A 209 ? 0.8985 0.5709 0.8231 0.0874  -0.1104 0.1410  209 ASN A CB  
1623 C CG  . ASN A 209 ? 0.9343 0.5749 0.8745 0.1028  -0.1113 0.1499  209 ASN A CG  
1624 O OD1 . ASN A 209 ? 0.9681 0.6132 0.9397 0.1154  -0.0926 0.1362  209 ASN A OD1 
1625 N ND2 . ASN A 209 ? 0.9871 0.5920 0.9029 0.1013  -0.1332 0.1733  209 ASN A ND2 
1626 N N   . TRP A 210 ? 0.7924 0.5667 0.7580 0.0812  -0.1342 0.1396  210 TRP A N   
1627 C CA  . TRP A 210 ? 0.8273 0.6309 0.7894 0.0708  -0.1241 0.1260  210 TRP A CA  
1628 C C   . TRP A 210 ? 0.7264 0.5717 0.7437 0.0856  -0.1212 0.1208  210 TRP A C   
1629 O O   . TRP A 210 ? 0.7376 0.6024 0.7845 0.0912  -0.1407 0.1329  210 TRP A O   
1630 C CB  . TRP A 210 ? 0.7857 0.5845 0.7101 0.0514  -0.1407 0.1350  210 TRP A CB  
1631 C CG  . TRP A 210 ? 0.7203 0.5399 0.6347 0.0390  -0.1272 0.1202  210 TRP A CG  
1632 C CD1 . TRP A 210 ? 0.6873 0.5392 0.6212 0.0369  -0.1335 0.1194  210 TRP A CD1 
1633 C CD2 . TRP A 210 ? 0.7087 0.5177 0.5956 0.0274  -0.1051 0.1044  210 TRP A CD2 
1634 N NE1 . TRP A 210 ? 0.6317 0.4902 0.5484 0.0255  -0.1166 0.1050  210 TRP A NE1 
1635 C CE2 . TRP A 210 ? 0.6830 0.5171 0.5736 0.0203  -0.0999 0.0958  210 TRP A CE2 
1636 C CE3 . TRP A 210 ? 0.6896 0.4710 0.5529 0.0221  -0.0893 0.0964  210 TRP A CE3 
1637 C CZ2 . TRP A 210 ? 0.7096 0.5419 0.5837 0.0104  -0.0810 0.0807  210 TRP A CZ2 
1638 C CZ3 . TRP A 210 ? 0.6901 0.4736 0.5402 0.0112  -0.0706 0.0803  210 TRP A CZ3 
1639 C CH2 . TRP A 210 ? 0.7227 0.5316 0.5795 0.0066  -0.0673 0.0732  210 TRP A CH2 
1640 N N   . ALA A 211 ? 0.6834 0.5411 0.7139 0.0906  -0.0971 0.1028  211 ALA A N   
1641 C CA  . ALA A 211 ? 0.6966 0.5890 0.7722 0.1018  -0.0883 0.0953  211 ALA A CA  
1642 C C   . ALA A 211 ? 0.6629 0.5818 0.7350 0.0904  -0.0921 0.0938  211 ALA A C   
1643 O O   . ALA A 211 ? 0.6437 0.5596 0.6839 0.0778  -0.0828 0.0847  211 ALA A O   
1644 C CB  . ALA A 211 ? 0.5934 0.4837 0.6720 0.1072  -0.0619 0.0767  211 ALA A CB  
1645 N N   . CYS A 212 ? 0.6420 0.5868 0.7506 0.0948  -0.1057 0.1024  212 CYS A N   
1646 C CA  . CYS A 212 ? 0.6193 0.5891 0.7285 0.0834  -0.1090 0.1008  212 CYS A CA  
1647 C C   . CYS A 212 ? 0.6264 0.6302 0.7945 0.0931  -0.1163 0.1054  212 CYS A C   
1648 O O   . CYS A 212 ? 0.5985 0.6048 0.8049 0.1077  -0.1261 0.1139  212 CYS A O   
1649 C CB  . CYS A 212 ? 0.6402 0.5956 0.7071 0.0652  -0.1282 0.1102  212 CYS A CB  
1650 S SG  . CYS A 212 ? 0.6027 0.5511 0.6783 0.0665  -0.1649 0.1334  212 CYS A SG  
1651 N N   . ASN A 213 ? 0.6284 0.6579 0.8066 0.0849  -0.1106 0.0995  213 ASN A N   
1652 C CA  . ASN A 213 ? 0.6349 0.7007 0.8716 0.0903  -0.1148 0.1015  213 ASN A CA  
1653 C C   . ASN A 213 ? 0.6543 0.7349 0.8793 0.0720  -0.1293 0.1052  213 ASN A C   
1654 O O   . ASN A 213 ? 0.6619 0.7534 0.8799 0.0628  -0.1128 0.0950  213 ASN A O   
1655 C CB  . ASN A 213 ? 0.6276 0.7091 0.8933 0.0985  -0.0837 0.0861  213 ASN A CB  
1656 C CG  . ASN A 213 ? 0.6441 0.7606 0.9822 0.1082  -0.0833 0.0870  213 ASN A CG  
1657 O OD1 . ASN A 213 ? 0.7159 0.8551 1.0824 0.1034  -0.1060 0.0968  213 ASN A OD1 
1658 N ND2 . ASN A 213 ? 0.6614 0.7825 1.0312 0.1209  -0.0569 0.0756  213 ASN A ND2 
1659 N N   . PRO A 214 ? 0.6927 0.7703 0.9112 0.0650  -0.1606 0.1199  214 PRO A N   
1660 C CA  . PRO A 214 ? 0.7125 0.8002 0.9137 0.0444  -0.1748 0.1221  214 PRO A CA  
1661 C C   . PRO A 214 ? 0.7303 0.8592 0.9857 0.0430  -0.1707 0.1171  214 PRO A C   
1662 O O   . PRO A 214 ? 0.7164 0.8517 0.9541 0.0259  -0.1661 0.1110  214 PRO A O   
1663 C CB  . PRO A 214 ? 0.7207 0.7951 0.9067 0.0390  -0.2119 0.1402  214 PRO A CB  
1664 C CG  . PRO A 214 ? 0.6840 0.7280 0.8551 0.0529  -0.2114 0.1462  214 PRO A CG  
1665 C CD  . PRO A 214 ? 0.6808 0.7394 0.8983 0.0733  -0.1848 0.1356  214 PRO A CD  
1666 N N   . GLU A 215 ? 0.7701 0.9261 1.0934 0.0599  -0.1700 0.1184  215 GLU A N   
1667 C CA  . GLU A 215 ? 0.7894 0.9868 1.1715 0.0574  -0.1649 0.1130  215 GLU A CA  
1668 C C   . GLU A 215 ? 0.7823 0.9817 1.1510 0.0510  -0.1282 0.0961  215 GLU A C   
1669 O O   . GLU A 215 ? 0.7304 0.9477 1.1059 0.0360  -0.1248 0.0915  215 GLU A O   
1670 C CB  . GLU A 215 ? 0.7997 1.0242 1.2627 0.0786  -0.1670 0.1161  215 GLU A CB  
1671 C CG  . GLU A 215 ? 0.9570 1.1803 1.4412 0.0874  -0.2070 0.1357  215 GLU A CG  
1672 C CD  . GLU A 215 ? 1.0445 1.2927 1.5470 0.0724  -0.2440 0.1467  215 GLU A CD  
1673 O OE1 . GLU A 215 ? 1.0308 1.2637 1.4728 0.0499  -0.2539 0.1473  215 GLU A OE1 
1674 O OE2 . GLU A 215 ? 1.0485 1.3252 1.6145 0.0808  -0.2570 0.1503  215 GLU A OE2 
1675 N N   . LEU A 216 ? 0.8445 0.6765 1.0378 0.0064  0.0090  -0.0226 216 LEU A N   
1676 C CA  . LEU A 216 ? 0.7612 0.6073 0.9502 0.0056  0.0277  -0.0255 216 LEU A CA  
1677 C C   . LEU A 216 ? 0.6965 0.5413 0.8469 -0.0001 0.0286  -0.0255 216 LEU A C   
1678 O O   . LEU A 216 ? 0.6848 0.5380 0.8227 -0.0004 0.0433  -0.0286 216 LEU A O   
1679 C CB  . LEU A 216 ? 0.7035 0.5529 0.8960 0.0097  0.0454  -0.0318 216 LEU A CB  
1680 C CG  . LEU A 216 ? 0.7057 0.5563 0.9379 0.0158  0.0474  -0.0328 216 LEU A CG  
1681 C CD1 . LEU A 216 ? 0.6854 0.5371 0.9151 0.0195  0.0660  -0.0402 216 LEU A CD1 
1682 C CD2 . LEU A 216 ? 0.6863 0.5488 0.9572 0.0180  0.0493  -0.0293 216 LEU A CD2 
1683 N N   . THR A 217 ? 0.6997 0.5330 0.8304 -0.0042 0.0134  -0.0222 217 THR A N   
1684 C CA  . THR A 217 ? 0.7209 0.5520 0.8170 -0.0097 0.0147  -0.0226 217 THR A CA  
1685 C C   . THR A 217 ? 0.7513 0.5954 0.8506 -0.0110 0.0208  -0.0211 217 THR A C   
1686 O O   . THR A 217 ? 0.6780 0.5264 0.7994 -0.0104 0.0144  -0.0172 217 THR A O   
1687 C CB  . THR A 217 ? 0.7192 0.5332 0.7949 -0.0134 -0.0016 -0.0189 217 THR A CB  
1688 O OG1 . THR A 217 ? 0.7756 0.5756 0.8410 -0.0129 -0.0036 -0.0203 217 THR A OG1 
1689 C CG2 . THR A 217 ? 0.6498 0.4627 0.6955 -0.0192 0.0001  -0.0189 217 THR A CG2 
1690 N N   . LEU A 218 ? 0.6608 0.5110 0.7393 -0.0126 0.0326  -0.0243 218 LEU A N   
1691 C CA  . LEU A 218 ? 0.5901 0.4512 0.6683 -0.0132 0.0398  -0.0224 218 LEU A CA  
1692 C C   . LEU A 218 ? 0.6038 0.4658 0.6506 -0.0158 0.0461  -0.0259 218 LEU A C   
1693 O O   . LEU A 218 ? 0.6073 0.4689 0.6427 -0.0143 0.0532  -0.0315 218 LEU A O   
1694 C CB  . LEU A 218 ? 0.6588 0.5311 0.7619 -0.0080 0.0538  -0.0224 218 LEU A CB  
1695 C CG  . LEU A 218 ? 0.5406 0.4227 0.6476 -0.0079 0.0628  -0.0190 218 LEU A CG  
1696 C CD1 . LEU A 218 ? 0.5806 0.4626 0.7038 -0.0111 0.0505  -0.0138 218 LEU A CD1 
1697 C CD2 . LEU A 218 ? 0.5509 0.4406 0.6784 -0.0022 0.0802  -0.0193 218 LEU A CD2 
1698 N N   . ILE A 219 ? 0.5974 0.4606 0.6321 -0.0195 0.0428  -0.0232 219 ILE A N   
1699 C CA  . ILE A 219 ? 0.6007 0.4661 0.6100 -0.0216 0.0478  -0.0262 219 ILE A CA  
1700 C C   . ILE A 219 ? 0.5951 0.4707 0.6077 -0.0201 0.0551  -0.0229 219 ILE A C   
1701 O O   . ILE A 219 ? 0.5861 0.4620 0.6066 -0.0224 0.0497  -0.0181 219 ILE A O   
1702 C CB  . ILE A 219 ? 0.5420 0.3973 0.5319 -0.0275 0.0383  -0.0262 219 ILE A CB  
1703 C CG1 . ILE A 219 ? 0.6442 0.4864 0.6302 -0.0288 0.0319  -0.0279 219 ILE A CG1 
1704 C CG2 . ILE A 219 ? 0.5668 0.4261 0.5361 -0.0293 0.0440  -0.0302 219 ILE A CG2 
1705 C CD1 . ILE A 219 ? 0.6203 0.4521 0.6164 -0.0292 0.0191  -0.0227 219 ILE A CD1 
1706 N N   . ALA A 220 ? 0.5658 0.4480 0.5713 -0.0159 0.0671  -0.0255 220 ALA A N   
1707 C CA  . ALA A 220 ? 0.5877 0.4774 0.5952 -0.0131 0.0763  -0.0215 220 ALA A CA  
1708 C C   . ALA A 220 ? 0.5340 0.4258 0.5155 -0.0131 0.0786  -0.0237 220 ALA A C   
1709 O O   . ALA A 220 ? 0.5302 0.4203 0.4948 -0.0132 0.0771  -0.0302 220 ALA A O   
1710 C CB  . ALA A 220 ? 0.5670 0.4605 0.5867 -0.0068 0.0901  -0.0214 220 ALA A CB  
1711 N N   . HIS A 221 ? 0.5276 0.4232 0.5086 -0.0129 0.0816  -0.0184 221 HIS A N   
1712 C CA  . HIS A 221 ? 0.5362 0.4341 0.4956 -0.0117 0.0835  -0.0192 221 HIS A CA  
1713 C C   . HIS A 221 ? 0.5791 0.4804 0.5381 -0.0059 0.0960  -0.0140 221 HIS A C   
1714 O O   . HIS A 221 ? 0.6024 0.5049 0.5810 -0.0060 0.1005  -0.0074 221 HIS A O   
1715 C CB  . HIS A 221 ? 0.5171 0.4137 0.4732 -0.0175 0.0746  -0.0174 221 HIS A CB  
1716 C CG  . HIS A 221 ? 0.5791 0.4692 0.5335 -0.0233 0.0642  -0.0213 221 HIS A CG  
1717 N ND1 . HIS A 221 ? 0.5947 0.4792 0.5636 -0.0262 0.0577  -0.0192 221 HIS A ND1 
1718 C CD2 . HIS A 221 ? 0.4804 0.3673 0.4201 -0.0265 0.0597  -0.0269 221 HIS A CD2 
1719 C CE1 . HIS A 221 ? 0.5813 0.4577 0.5405 -0.0305 0.0501  -0.0225 221 HIS A CE1 
1720 N NE2 . HIS A 221 ? 0.6037 0.4816 0.5466 -0.0312 0.0524  -0.0272 221 HIS A NE2 
1721 N N   . LEU A 222 ? 0.6008 0.5024 0.5373 -0.0005 0.1014  -0.0169 222 LEU A N   
1722 C CA  . LEU A 222 ? 0.6569 0.5581 0.5850 0.0062  0.1141  -0.0116 222 LEU A CA  
1723 C C   . LEU A 222 ? 0.6727 0.5742 0.5767 0.0084  0.1104  -0.0119 222 LEU A C   
1724 O O   . LEU A 222 ? 0.7050 0.6047 0.5858 0.0137  0.1106  -0.0173 222 LEU A O   
1725 C CB  . LEU A 222 ? 0.6593 0.5573 0.5801 0.0129  0.1253  -0.0148 222 LEU A CB  
1726 C CG  . LEU A 222 ? 0.6928 0.5908 0.6405 0.0121  0.1311  -0.0143 222 LEU A CG  
1727 C CD1 . LEU A 222 ? 0.6631 0.5606 0.6159 0.0083  0.1205  -0.0223 222 LEU A CD1 
1728 C CD2 . LEU A 222 ? 0.6575 0.5514 0.6002 0.0198  0.1491  -0.0132 222 LEU A CD2 
1729 N N   . PRO A 223 ? 0.6561 0.5593 0.5656 0.0049  0.1061  -0.0068 223 PRO A N   
1730 C CA  . PRO A 223 ? 0.7170 0.6209 0.6071 0.0068  0.1012  -0.0075 223 PRO A CA  
1731 C C   . PRO A 223 ? 0.7575 0.6577 0.6257 0.0162  0.1101  -0.0040 223 PRO A C   
1732 O O   . PRO A 223 ? 0.7937 0.6936 0.6406 0.0202  0.1041  -0.0084 223 PRO A O   
1733 C CB  . PRO A 223 ? 0.6829 0.5880 0.5874 0.0013  0.0976  -0.0017 223 PRO A CB  
1734 C CG  . PRO A 223 ? 0.6626 0.5672 0.5915 -0.0011 0.1037  0.0040  223 PRO A CG  
1735 C CD  . PRO A 223 ? 0.6746 0.5788 0.6092 -0.0010 0.1044  -0.0011 223 PRO A CD  
1736 N N   . ASP A 224 ? 0.7395 0.6358 0.6124 0.0201  0.1242  0.0039  224 ASP A N   
1737 C CA  . ASP A 224 ? 0.8935 0.7827 0.7408 0.0298  0.1346  0.0081  224 ASP A CA  
1738 C C   . ASP A 224 ? 0.9194 0.8049 0.7416 0.0358  0.1336  -0.0008 224 ASP A C   
1739 O O   . ASP A 224 ? 0.9547 0.8341 0.7467 0.0439  0.1336  -0.0011 224 ASP A O   
1740 C CB  . ASP A 224 ? 0.9203 0.8048 0.7804 0.0322  0.1531  0.0180  224 ASP A CB  
1741 C CG  . ASP A 224 ? 0.9247 0.8118 0.8094 0.0270  0.1543  0.0265  224 ASP A CG  
1742 O OD1 . ASP A 224 ? 0.8288 0.7179 0.7089 0.0249  0.1444  0.0273  224 ASP A OD1 
1743 O OD2 . ASP A 224 ? 1.0020 0.8891 0.9126 0.0249  0.1653  0.0318  224 ASP A OD2 
1744 N N   . ARG A 225 ? 0.8671 0.7550 0.7006 0.0325  0.1319  -0.0082 225 ARG A N   
1745 C CA  . ARG A 225 ? 0.8948 0.7791 0.7078 0.0373  0.1306  -0.0182 225 ARG A CA  
1746 C C   . ARG A 225 ? 0.8402 0.7300 0.6520 0.0328  0.1134  -0.0293 225 ARG A C   
1747 O O   . ARG A 225 ? 0.8652 0.7524 0.6619 0.0362  0.1100  -0.0391 225 ARG A O   
1748 C CB  . ARG A 225 ? 0.8748 0.7568 0.7017 0.0374  0.1419  -0.0196 225 ARG A CB  
1749 C CG  . ARG A 225 ? 1.0219 0.8975 0.8513 0.0424  0.1619  -0.0097 225 ARG A CG  
1750 C CD  . ARG A 225 ? 1.0518 0.9282 0.9081 0.0405  0.1722  -0.0103 225 ARG A CD  
1751 N NE  . ARG A 225 ? 1.1016 0.9753 0.9469 0.0429  0.1705  -0.0214 225 ARG A NE  
1752 C CZ  . ARG A 225 ? 1.2096 1.0734 1.0301 0.0513  0.1826  -0.0247 225 ARG A CZ  
1753 N NH1 . ARG A 225 ? 1.2225 1.0771 1.0239 0.0585  0.1984  -0.0170 225 ARG A NH1 
1754 N NH2 . ARG A 225 ? 1.2144 1.0760 1.0275 0.0526  0.1795  -0.0359 225 ARG A NH2 
1755 N N   . ARG A 226 ? 0.7707 0.6669 0.5982 0.0254  0.1034  -0.0283 226 ARG A N   
1756 C CA  . ARG A 226 ? 0.7579 0.6586 0.5878 0.0203  0.0895  -0.0380 226 ARG A CA  
1757 C C   . ARG A 226 ? 0.7173 0.6172 0.5556 0.0172  0.0885  -0.0463 226 ARG A C   
1758 O O   . ARG A 226 ? 0.6897 0.5900 0.5203 0.0174  0.0812  -0.0569 226 ARG A O   
1759 C CB  . ARG A 226 ? 0.8517 0.7525 0.6586 0.0261  0.0811  -0.0442 226 ARG A CB  
1760 C CG  . ARG A 226 ? 0.9716 0.8721 0.7691 0.0300  0.0806  -0.0361 226 ARG A CG  
1761 C CD  . ARG A 226 ? 1.0845 0.9842 0.8588 0.0373  0.0704  -0.0429 226 ARG A CD  
1762 N NE  . ARG A 226 ? 1.0965 0.9877 0.8437 0.0467  0.0744  -0.0463 226 ARG A NE  
1763 C CZ  . ARG A 226 ? 1.1152 1.0055 0.8551 0.0479  0.0691  -0.0586 226 ARG A CZ  
1764 N NH1 . ARG A 226 ? 1.0489 0.9464 0.8082 0.0401  0.0600  -0.0683 226 ARG A NH1 
1765 N NH2 . ARG A 226 ? 1.1141 0.9945 0.8259 0.0571  0.0738  -0.0613 226 ARG A NH2 
1766 N N   . GLU A 227 ? 0.7083 0.6071 0.5647 0.0145  0.0957  -0.0418 227 GLU A N   
1767 C CA  . GLU A 227 ? 0.6976 0.5945 0.5642 0.0122  0.0956  -0.0482 227 GLU A CA  
1768 C C   . GLU A 227 ? 0.6252 0.5232 0.5158 0.0038  0.0907  -0.0449 227 GLU A C   
1769 O O   . GLU A 227 ? 0.6479 0.5471 0.5514 0.0015  0.0925  -0.0362 227 GLU A O   
1770 C CB  . GLU A 227 ? 0.7444 0.6370 0.6104 0.0183  0.1090  -0.0468 227 GLU A CB  
1771 C CG  . GLU A 227 ? 0.8267 0.7144 0.6634 0.0275  0.1146  -0.0509 227 GLU A CG  
1772 C CD  . GLU A 227 ? 0.8015 0.6830 0.6370 0.0333  0.1297  -0.0507 227 GLU A CD  
1773 O OE1 . GLU A 227 ? 0.7655 0.6481 0.6264 0.0299  0.1338  -0.0495 227 GLU A OE1 
1774 O OE2 . GLU A 227 ? 0.8842 0.7587 0.6929 0.0417  0.1376  -0.0517 227 GLU A OE2 
1775 N N   . ILE A 228 ? 0.6049 0.5009 0.5004 -0.0005 0.0843  -0.0520 228 ILE A N   
1776 C CA  . ILE A 228 ? 0.6040 0.4972 0.5177 -0.0073 0.0796  -0.0495 228 ILE A CA  
1777 C C   . ILE A 228 ? 0.6078 0.4969 0.5304 -0.0058 0.0826  -0.0535 228 ILE A C   
1778 O O   . ILE A 228 ? 0.5142 0.4016 0.4281 -0.0042 0.0824  -0.0625 228 ILE A O   
1779 C CB  . ILE A 228 ? 0.5850 0.4766 0.4958 -0.0140 0.0703  -0.0532 228 ILE A CB  
1780 C CG1 . ILE A 228 ? 0.5958 0.4913 0.5006 -0.0152 0.0679  -0.0491 228 ILE A CG1 
1781 C CG2 . ILE A 228 ? 0.5841 0.4688 0.5078 -0.0199 0.0656  -0.0506 228 ILE A CG2 
1782 C CD1 . ILE A 228 ? 0.5113 0.4053 0.4137 -0.0214 0.0612  -0.0534 228 ILE A CD1 
1783 N N   . ILE A 229 ? 0.5544 0.4422 0.4962 -0.0061 0.0849  -0.0475 229 ILE A N   
1784 C CA  . ILE A 229 ? 0.5603 0.4446 0.5147 -0.0038 0.0888  -0.0502 229 ILE A CA  
1785 C C   . ILE A 229 ? 0.5720 0.4515 0.5449 -0.0087 0.0803  -0.0462 229 ILE A C   
1786 O O   . ILE A 229 ? 0.5787 0.4596 0.5668 -0.0097 0.0785  -0.0388 229 ILE A O   
1787 C CB  . ILE A 229 ? 0.5760 0.4628 0.5382 0.0028  0.1019  -0.0470 229 ILE A CB  
1788 C CG1 . ILE A 229 ? 0.5512 0.4392 0.4882 0.0086  0.1098  -0.0503 229 ILE A CG1 
1789 C CG2 . ILE A 229 ? 0.5461 0.4293 0.5235 0.0055  0.1066  -0.0506 229 ILE A CG2 
1790 C CD1 . ILE A 229 ? 0.6283 0.5161 0.5679 0.0155  0.1255  -0.0462 229 ILE A CD1 
1791 N N   . SER A 230 ? 0.5554 0.4279 0.5267 -0.0116 0.0747  -0.0513 230 SER A N   
1792 C CA  . SER A 230 ? 0.5822 0.4465 0.5650 -0.0156 0.0655  -0.0475 230 SER A CA  
1793 C C   . SER A 230 ? 0.5687 0.4271 0.5630 -0.0133 0.0667  -0.0512 230 SER A C   
1794 O O   . SER A 230 ? 0.5451 0.4025 0.5315 -0.0117 0.0715  -0.0592 230 SER A O   
1795 C CB  . SER A 230 ? 0.5468 0.4044 0.5145 -0.0221 0.0578  -0.0485 230 SER A CB  
1796 O OG  . SER A 230 ? 0.6186 0.4646 0.5917 -0.0252 0.0494  -0.0445 230 SER A OG  
1797 N N   . PHE A 231 ? 0.6306 0.4844 0.6440 -0.0129 0.0612  -0.0458 231 PHE A N   
1798 C CA  . PHE A 231 ? 0.6027 0.4517 0.6324 -0.0094 0.0627  -0.0482 231 PHE A CA  
1799 C C   . PHE A 231 ? 0.6350 0.4727 0.6747 -0.0114 0.0499  -0.0428 231 PHE A C   
1800 O O   . PHE A 231 ? 0.6229 0.4605 0.6707 -0.0125 0.0416  -0.0361 231 PHE A O   
1801 C CB  . PHE A 231 ? 0.5973 0.4550 0.6478 -0.0033 0.0730  -0.0474 231 PHE A CB  
1802 C CG  . PHE A 231 ? 0.5859 0.4395 0.6560 0.0010  0.0763  -0.0505 231 PHE A CG  
1803 C CD1 . PHE A 231 ? 0.6409 0.4937 0.7031 0.0042  0.0865  -0.0592 231 PHE A CD1 
1804 C CD2 . PHE A 231 ? 0.5952 0.4457 0.6926 0.0023  0.0687  -0.0453 231 PHE A CD2 
1805 C CE1 . PHE A 231 ? 0.6574 0.5059 0.7385 0.0083  0.0905  -0.0625 231 PHE A CE1 
1806 C CE2 . PHE A 231 ? 0.6394 0.4864 0.7573 0.0067  0.0719  -0.0481 231 PHE A CE2 
1807 C CZ  . PHE A 231 ? 0.6266 0.4726 0.7365 0.0096  0.0836  -0.0566 231 PHE A CZ  
1808 N N   . GLY A 232 ? 0.6356 0.4625 0.6740 -0.0116 0.0477  -0.0460 232 GLY A N   
1809 C CA  . GLY A 232 ? 0.6833 0.4975 0.7326 -0.0112 0.0364  -0.0409 232 GLY A CA  
1810 C C   . GLY A 232 ? 0.7277 0.5266 0.7562 -0.0165 0.0258  -0.0369 232 GLY A C   
1811 O O   . GLY A 232 ? 0.7625 0.5481 0.7956 -0.0155 0.0148  -0.0316 232 GLY A O   
1812 N N   . SER A 233 ? 0.6811 0.4801 0.6865 -0.0216 0.0289  -0.0391 233 SER A N   
1813 C CA  . SER A 233 ? 0.6649 0.4481 0.6492 -0.0268 0.0218  -0.0354 233 SER A CA  
1814 C C   . SER A 233 ? 0.7450 0.5248 0.7127 -0.0312 0.0299  -0.0419 233 SER A C   
1815 O O   . SER A 233 ? 0.7089 0.5021 0.6761 -0.0314 0.0383  -0.0487 233 SER A O   
1816 C CB  . SER A 233 ? 0.7066 0.4925 0.6823 -0.0293 0.0160  -0.0304 233 SER A CB  
1817 O OG  . SER A 233 ? 0.6846 0.4537 0.6365 -0.0343 0.0114  -0.0275 233 SER A OG  
1818 N N   . GLY A 234 ? 0.7720 0.5324 0.7261 -0.0346 0.0272  -0.0396 234 GLY A N   
1819 C CA  . GLY A 234 ? 0.6547 0.4099 0.5966 -0.0397 0.0352  -0.0455 234 GLY A CA  
1820 C C   . GLY A 234 ? 0.7321 0.4794 0.6534 -0.0457 0.0352  -0.0427 234 GLY A C   
1821 O O   . GLY A 234 ? 0.7444 0.4920 0.6594 -0.0503 0.0430  -0.0485 234 GLY A O   
1822 N N   . TYR A 235 ? 0.8091 0.5489 0.7211 -0.0455 0.0265  -0.0346 235 TYR A N   
1823 C CA  . TYR A 235 ? 0.8391 0.5688 0.7294 -0.0507 0.0269  -0.0318 235 TYR A CA  
1824 C C   . TYR A 235 ? 0.8528 0.6006 0.7441 -0.0536 0.0344  -0.0378 235 TYR A C   
1825 O O   . TYR A 235 ? 0.8427 0.6106 0.7476 -0.0505 0.0350  -0.0408 235 TYR A O   
1826 C CB  . TYR A 235 ? 0.8677 0.5887 0.7494 -0.0490 0.0146  -0.0235 235 TYR A CB  
1827 C CG  . TYR A 235 ? 0.9247 0.6367 0.7836 -0.0538 0.0151  -0.0214 235 TYR A CG  
1828 C CD1 . TYR A 235 ? 0.9061 0.5934 0.7401 -0.0577 0.0185  -0.0187 235 TYR A CD1 
1829 C CD2 . TYR A 235 ? 0.9128 0.6397 0.7748 -0.0542 0.0135  -0.0218 235 TYR A CD2 
1830 C CE1 . TYR A 235 ? 0.9229 0.6007 0.7352 -0.0619 0.0208  -0.0172 235 TYR A CE1 
1831 C CE2 . TYR A 235 ? 0.8896 0.6079 0.7316 -0.0584 0.0146  -0.0205 235 TYR A CE2 
1832 C CZ  . TYR A 235 ? 0.9391 0.6329 0.7560 -0.0622 0.0184  -0.0184 235 TYR A CZ  
1833 O OH  . TYR A 235 ? 0.8899 0.5739 0.6862 -0.0661 0.0212  -0.0176 235 TYR A OH  
1834 N N   . GLY A 236 ? 0.7913 0.5303 0.6680 -0.0593 0.0406  -0.0392 236 GLY A N   
1835 C CA  . GLY A 236 ? 0.7721 0.5271 0.6522 -0.0620 0.0477  -0.0460 236 GLY A CA  
1836 C C   . GLY A 236 ? 0.7248 0.4962 0.6082 -0.0597 0.0437  -0.0444 236 GLY A C   
1837 O O   . GLY A 236 ? 0.7300 0.5198 0.6226 -0.0584 0.0471  -0.0499 236 GLY A O   
1838 N N   . GLY A 237 ? 0.7448 0.5084 0.6201 -0.0590 0.0361  -0.0369 237 GLY A N   
1839 C CA  . GLY A 237 ? 0.7180 0.4958 0.5982 -0.0573 0.0327  -0.0351 237 GLY A CA  
1840 C C   . GLY A 237 ? 0.7689 0.5648 0.6687 -0.0516 0.0318  -0.0361 237 GLY A C   
1841 O O   . GLY A 237 ? 0.7235 0.5345 0.6291 -0.0500 0.0337  -0.0366 237 GLY A O   
1842 N N   . ASN A 238 ? 0.7351 0.5286 0.6449 -0.0483 0.0300  -0.0360 238 ASN A N   
1843 C CA  . ASN A 238 ? 0.6884 0.4967 0.6169 -0.0426 0.0313  -0.0371 238 ASN A CA  
1844 C C   . ASN A 238 ? 0.6882 0.5056 0.6209 -0.0408 0.0397  -0.0452 238 ASN A C   
1845 O O   . ASN A 238 ? 0.7072 0.5377 0.6499 -0.0361 0.0435  -0.0470 238 ASN A O   
1846 C CB  . ASN A 238 ? 0.6515 0.4525 0.5924 -0.0391 0.0240  -0.0325 238 ASN A CB  
1847 C CG  . ASN A 238 ? 0.6941 0.4835 0.6299 -0.0403 0.0126  -0.0255 238 ASN A CG  
1848 O OD1 . ASN A 238 ? 0.7707 0.5638 0.7015 -0.0422 0.0108  -0.0235 238 ASN A OD1 
1849 N ND2 . ASN A 238 ? 0.7128 0.4870 0.6492 -0.0388 0.0040  -0.0219 238 ASN A ND2 
1850 N N   . SER A 239 ? 0.6820 0.4917 0.6072 -0.0443 0.0429  -0.0503 239 SER A N   
1851 C CA  . SER A 239 ? 0.6414 0.4574 0.5719 -0.0427 0.0488  -0.0593 239 SER A CA  
1852 C C   . SER A 239 ? 0.6201 0.4435 0.5447 -0.0456 0.0529  -0.0667 239 SER A C   
1853 O O   . SER A 239 ? 0.6064 0.4399 0.5345 -0.0427 0.0558  -0.0747 239 SER A O   
1854 C CB  . SER A 239 ? 0.6203 0.4216 0.5532 -0.0440 0.0491  -0.0609 239 SER A CB  
1855 O OG  . SER A 239 ? 0.6492 0.4360 0.5707 -0.0501 0.0499  -0.0599 239 SER A OG  
1856 N N   . LEU A 240 ? 0.6484 0.4663 0.5642 -0.0509 0.0529  -0.0649 240 LEU A N   
1857 C CA  . LEU A 240 ? 0.6447 0.4708 0.5590 -0.0535 0.0561  -0.0718 240 LEU A CA  
1858 C C   . LEU A 240 ? 0.5804 0.4201 0.4928 -0.0503 0.0543  -0.0690 240 LEU A C   
1859 O O   . LEU A 240 ? 0.6449 0.4826 0.5516 -0.0528 0.0532  -0.0638 240 LEU A O   
1860 C CB  . LEU A 240 ? 0.6873 0.5003 0.5952 -0.0606 0.0591  -0.0711 240 LEU A CB  
1861 C CG  . LEU A 240 ? 0.5785 0.3736 0.4858 -0.0640 0.0622  -0.0714 240 LEU A CG  
1862 C CD1 . LEU A 240 ? 0.5830 0.3644 0.4827 -0.0709 0.0684  -0.0709 240 LEU A CD1 
1863 C CD2 . LEU A 240 ? 0.5942 0.3950 0.5139 -0.0624 0.0643  -0.0811 240 LEU A CD2 
1864 N N   . LEU A 241 ? 0.5859 0.4382 0.5018 -0.0444 0.0547  -0.0726 241 LEU A N   
1865 C CA  . LEU A 241 ? 0.6035 0.4661 0.5173 -0.0400 0.0542  -0.0679 241 LEU A CA  
1866 C C   . LEU A 241 ? 0.5734 0.4433 0.4827 -0.0411 0.0537  -0.0697 241 LEU A C   
1867 O O   . LEU A 241 ? 0.6128 0.4881 0.5198 -0.0390 0.0533  -0.0639 241 LEU A O   
1868 C CB  . LEU A 241 ? 0.5267 0.3971 0.4420 -0.0328 0.0567  -0.0709 241 LEU A CB  
1869 C CG  . LEU A 241 ? 0.5501 0.4142 0.4737 -0.0309 0.0579  -0.0684 241 LEU A CG  
1870 C CD1 . LEU A 241 ? 0.5215 0.3920 0.4460 -0.0236 0.0629  -0.0714 241 LEU A CD1 
1871 C CD2 . LEU A 241 ? 0.5408 0.4001 0.4700 -0.0324 0.0550  -0.0581 241 LEU A CD2 
1872 N N   . GLY A 242 ? 0.5937 0.4640 0.5042 -0.0444 0.0539  -0.0777 242 GLY A N   
1873 C CA  . GLY A 242 ? 0.5819 0.4592 0.4917 -0.0453 0.0530  -0.0795 242 GLY A CA  
1874 C C   . GLY A 242 ? 0.5945 0.4647 0.5024 -0.0509 0.0543  -0.0736 242 GLY A C   
1875 O O   . GLY A 242 ? 0.6414 0.5170 0.5505 -0.0518 0.0544  -0.0750 242 GLY A O   
1876 N N   . LYS A 243 ? 0.5634 0.4205 0.4673 -0.0543 0.0549  -0.0674 243 LYS A N   
1877 C CA  . LYS A 243 ? 0.5730 0.4195 0.4707 -0.0597 0.0564  -0.0630 243 LYS A CA  
1878 C C   . LYS A 243 ? 0.6215 0.4688 0.5150 -0.0578 0.0531  -0.0546 243 LYS A C   
1879 O O   . LYS A 243 ? 0.6158 0.4711 0.5101 -0.0568 0.0534  -0.0540 243 LYS A O   
1880 C CB  . LYS A 243 ? 0.5793 0.4072 0.4712 -0.0643 0.0582  -0.0615 243 LYS A CB  
1881 C CG  . LYS A 243 ? 0.6472 0.4594 0.5270 -0.0698 0.0609  -0.0574 243 LYS A CG  
1882 C CD  . LYS A 243 ? 0.5119 0.3033 0.3828 -0.0738 0.0642  -0.0563 243 LYS A CD  
1883 C CE  . LYS A 243 ? 0.5926 0.3644 0.4453 -0.0783 0.0672  -0.0515 243 LYS A CE  
1884 N NZ  . LYS A 243 ? 0.5640 0.3408 0.4191 -0.0815 0.0742  -0.0554 243 LYS A NZ  
1885 N N   . LYS A 244 ? 0.5930 0.4319 0.4841 -0.0572 0.0494  -0.0485 244 LYS A N   
1886 C CA  . LYS A 244 ? 0.5456 0.3854 0.4369 -0.0556 0.0453  -0.0415 244 LYS A CA  
1887 C C   . LYS A 244 ? 0.5859 0.4411 0.4872 -0.0495 0.0458  -0.0401 244 LYS A C   
1888 O O   . LYS A 244 ? 0.5772 0.4387 0.4803 -0.0480 0.0460  -0.0367 244 LYS A O   
1889 C CB  . LYS A 244 ? 0.5745 0.4000 0.4624 -0.0567 0.0394  -0.0362 244 LYS A CB  
1890 C CG  . LYS A 244 ? 0.6276 0.4333 0.4998 -0.0621 0.0394  -0.0362 244 LYS A CG  
1891 C CD  . LYS A 244 ? 0.6430 0.4441 0.5051 -0.0658 0.0417  -0.0360 244 LYS A CD  
1892 C CE  . LYS A 244 ? 0.5877 0.3657 0.4303 -0.0708 0.0436  -0.0354 244 LYS A CE  
1893 N NZ  . LYS A 244 ? 0.5761 0.3476 0.4075 -0.0742 0.0466  -0.0354 244 LYS A NZ  
1894 N N   . CYS A 245 ? 0.5769 0.4366 0.4835 -0.0457 0.0472  -0.0426 245 CYS A N   
1895 C CA  . CYS A 245 ? 0.5562 0.4272 0.4696 -0.0394 0.0497  -0.0408 245 CYS A CA  
1896 C C   . CYS A 245 ? 0.5707 0.4521 0.4793 -0.0364 0.0527  -0.0432 245 CYS A C   
1897 O O   . CYS A 245 ? 0.5819 0.4692 0.4922 -0.0330 0.0546  -0.0383 245 CYS A O   
1898 C CB  . CYS A 245 ? 0.5497 0.4212 0.4678 -0.0360 0.0517  -0.0442 245 CYS A CB  
1899 S SG  . CYS A 245 ? 0.5594 0.4190 0.4861 -0.0376 0.0472  -0.0404 245 CYS A SG  
1900 N N   . PHE A 246 ? 0.5586 0.4419 0.4625 -0.0375 0.0527  -0.0509 246 PHE A N   
1901 C CA  . PHE A 246 ? 0.5842 0.4770 0.4840 -0.0338 0.0530  -0.0541 246 PHE A CA  
1902 C C   . PHE A 246 ? 0.5997 0.4927 0.4994 -0.0373 0.0520  -0.0528 246 PHE A C   
1903 O O   . PHE A 246 ? 0.6118 0.5096 0.5104 -0.0343 0.0524  -0.0480 246 PHE A O   
1904 C CB  . PHE A 246 ? 0.5445 0.4403 0.4429 -0.0324 0.0518  -0.0645 246 PHE A CB  
1905 C CG  . PHE A 246 ? 0.6034 0.5082 0.4975 -0.0278 0.0493  -0.0691 246 PHE A CG  
1906 C CD1 . PHE A 246 ? 0.6947 0.6042 0.5828 -0.0224 0.0499  -0.0628 246 PHE A CD1 
1907 C CD2 . PHE A 246 ? 0.6921 0.6000 0.5892 -0.0286 0.0457  -0.0797 246 PHE A CD2 
1908 C CE1 . PHE A 246 ? 0.7880 0.7041 0.6703 -0.0173 0.0460  -0.0664 246 PHE A CE1 
1909 C CE2 . PHE A 246 ? 0.7029 0.6188 0.5971 -0.0237 0.0407  -0.0845 246 PHE A CE2 
1910 C CZ  . PHE A 246 ? 0.7960 0.7155 0.6813 -0.0176 0.0404  -0.0775 246 PHE A CZ  
1911 N N   . ALA A 247 ? 0.5857 0.4724 0.4868 -0.0436 0.0519  -0.0569 247 ALA A N   
1912 C CA  . ALA A 247 ? 0.6091 0.4964 0.5114 -0.0467 0.0525  -0.0578 247 ALA A CA  
1913 C C   . ALA A 247 ? 0.5780 0.4603 0.4778 -0.0485 0.0528  -0.0498 247 ALA A C   
1914 O O   . ALA A 247 ? 0.5495 0.4337 0.4506 -0.0494 0.0538  -0.0497 247 ALA A O   
1915 C CB  . ALA A 247 ? 0.6024 0.4821 0.5074 -0.0533 0.0551  -0.0641 247 ALA A CB  
1916 N N   . LEU A 248 ? 0.5739 0.4500 0.4723 -0.0488 0.0515  -0.0437 248 LEU A N   
1917 C CA  . LEU A 248 ? 0.5339 0.4055 0.4319 -0.0501 0.0502  -0.0370 248 LEU A CA  
1918 C C   . LEU A 248 ? 0.6355 0.5145 0.5400 -0.0448 0.0501  -0.0310 248 LEU A C   
1919 O O   . LEU A 248 ? 0.5991 0.4833 0.5058 -0.0425 0.0516  -0.0277 248 LEU A O   
1920 C CB  . LEU A 248 ? 0.5122 0.3684 0.4045 -0.0553 0.0473  -0.0351 248 LEU A CB  
1921 C CG  . LEU A 248 ? 0.6043 0.4485 0.4868 -0.0612 0.0500  -0.0390 248 LEU A CG  
1922 C CD1 . LEU A 248 ? 0.5689 0.3945 0.4400 -0.0650 0.0462  -0.0358 248 LEU A CD1 
1923 C CD2 . LEU A 248 ? 0.5071 0.3547 0.3903 -0.0623 0.0533  -0.0402 248 LEU A CD2 
1924 N N   . ARG A 249 ? 0.5978 0.4766 0.5068 -0.0426 0.0495  -0.0292 249 ARG A N   
1925 C CA  . ARG A 249 ? 0.5948 0.4787 0.5132 -0.0384 0.0514  -0.0230 249 ARG A CA  
1926 C C   . ARG A 249 ? 0.5614 0.4552 0.4772 -0.0318 0.0570  -0.0225 249 ARG A C   
1927 O O   . ARG A 249 ? 0.5781 0.4750 0.4968 -0.0294 0.0599  -0.0172 249 ARG A O   
1928 C CB  . ARG A 249 ? 0.5817 0.4627 0.5085 -0.0375 0.0501  -0.0218 249 ARG A CB  
1929 C CG  . ARG A 249 ? 0.5892 0.4581 0.5162 -0.0427 0.0426  -0.0213 249 ARG A CG  
1930 C CD  . ARG A 249 ? 0.5594 0.4267 0.5011 -0.0409 0.0396  -0.0183 249 ARG A CD  
1931 N NE  . ARG A 249 ? 0.6267 0.4806 0.5653 -0.0448 0.0302  -0.0180 249 ARG A NE  
1932 C CZ  . ARG A 249 ? 0.6392 0.4844 0.5708 -0.0459 0.0277  -0.0206 249 ARG A CZ  
1933 N NH1 . ARG A 249 ? 0.5416 0.3916 0.4718 -0.0437 0.0336  -0.0247 249 ARG A NH1 
1934 N NH2 . ARG A 249 ? 0.6126 0.4429 0.5373 -0.0488 0.0188  -0.0193 249 ARG A NH2 
1935 N N   . ILE A 250 ? 0.5994 0.4966 0.5085 -0.0286 0.0583  -0.0281 250 ILE A N   
1936 C CA  . ILE A 250 ? 0.5877 0.4916 0.4891 -0.0215 0.0620  -0.0283 250 ILE A CA  
1937 C C   . ILE A 250 ? 0.5903 0.4974 0.4864 -0.0212 0.0596  -0.0294 250 ILE A C   
1938 O O   . ILE A 250 ? 0.6232 0.5334 0.5149 -0.0158 0.0622  -0.0249 250 ILE A O   
1939 C CB  . ILE A 250 ? 0.6648 0.5701 0.5591 -0.0179 0.0623  -0.0355 250 ILE A CB  
1940 C CG1 . ILE A 250 ? 0.6296 0.5321 0.5310 -0.0169 0.0663  -0.0337 250 ILE A CG1 
1941 C CG2 . ILE A 250 ? 0.6051 0.5150 0.4861 -0.0100 0.0640  -0.0368 250 ILE A CG2 
1942 C CD1 . ILE A 250 ? 0.5548 0.4587 0.4599 -0.0118 0.0742  -0.0259 250 ILE A CD1 
1943 N N   . ALA A 251 ? 0.6535 0.5589 0.5507 -0.0267 0.0555  -0.0350 251 ALA A N   
1944 C CA  . ALA A 251 ? 0.6320 0.5411 0.5280 -0.0263 0.0534  -0.0374 251 ALA A CA  
1945 C C   . ALA A 251 ? 0.5566 0.4642 0.4563 -0.0273 0.0550  -0.0301 251 ALA A C   
1946 O O   . ALA A 251 ? 0.5323 0.4441 0.4310 -0.0237 0.0545  -0.0292 251 ALA A O   
1947 C CB  . ALA A 251 ? 0.5575 0.4643 0.4570 -0.0325 0.0511  -0.0454 251 ALA A CB  
1948 N N   . SER A 252 ? 0.5400 0.4413 0.4450 -0.0317 0.0560  -0.0254 252 SER A N   
1949 C CA  . SER A 252 ? 0.5856 0.4846 0.4953 -0.0331 0.0570  -0.0196 252 SER A CA  
1950 C C   . SER A 252 ? 0.6402 0.5438 0.5509 -0.0263 0.0611  -0.0126 252 SER A C   
1951 O O   . SER A 252 ? 0.5506 0.4550 0.4628 -0.0248 0.0622  -0.0092 252 SER A O   
1952 C CB  . SER A 252 ? 0.5369 0.4272 0.4519 -0.0388 0.0551  -0.0171 252 SER A CB  
1953 O OG  . SER A 252 ? 0.6062 0.4971 0.5267 -0.0368 0.0557  -0.0140 252 SER A OG  
1954 N N   . ARG A 253 ? 0.6086 0.5141 0.5179 -0.0218 0.0646  -0.0101 253 ARG A N   
1955 C CA  . ARG A 253 ? 0.6016 0.5091 0.5088 -0.0147 0.0709  -0.0028 253 ARG A CA  
1956 C C   . ARG A 253 ? 0.6235 0.5343 0.5164 -0.0080 0.0696  -0.0047 253 ARG A C   
1957 O O   . ARG A 253 ? 0.6410 0.5514 0.5312 -0.0035 0.0723  0.0013  253 ARG A O   
1958 C CB  . ARG A 253 ? 0.6024 0.5094 0.5117 -0.0116 0.0770  -0.0001 253 ARG A CB  
1959 C CG  . ARG A 253 ? 0.7241 0.6306 0.6271 -0.0036 0.0863  0.0074  253 ARG A CG  
1960 C CD  . ARG A 253 ? 0.7223 0.6270 0.6378 -0.0029 0.0953  0.0125  253 ARG A CD  
1961 N NE  . ARG A 253 ? 0.8380 0.7400 0.7435 0.0053  0.1070  0.0193  253 ARG A NE  
1962 C CZ  . ARG A 253 ? 0.8026 0.7022 0.7199 0.0071  0.1188  0.0255  253 ARG A CZ  
1963 N NH1 . ARG A 253 ? 0.8084 0.7098 0.7512 0.0014  0.1187  0.0253  253 ARG A NH1 
1964 N NH2 . ARG A 253 ? 1.0239 0.9184 0.9274 0.0151  0.1311  0.0319  253 ARG A NH2 
1965 N N   . LEU A 254 ? 0.6092 0.5228 0.4938 -0.0068 0.0648  -0.0131 254 LEU A N   
1966 C CA  . LEU A 254 ? 0.6446 0.5617 0.5178 -0.0005 0.0602  -0.0166 254 LEU A CA  
1967 C C   . LEU A 254 ? 0.7000 0.6189 0.5805 -0.0027 0.0563  -0.0169 254 LEU A C   
1968 O O   . LEU A 254 ? 0.6771 0.5972 0.5514 0.0038  0.0544  -0.0142 254 LEU A O   
1969 C CB  . LEU A 254 ? 0.6965 0.6166 0.5649 -0.0005 0.0543  -0.0275 254 LEU A CB  
1970 C CG  . LEU A 254 ? 0.7396 0.6577 0.5988 0.0031  0.0577  -0.0290 254 LEU A CG  
1971 C CD1 . LEU A 254 ? 0.7692 0.6899 0.6268 0.0020  0.0511  -0.0410 254 LEU A CD1 
1972 C CD2 . LEU A 254 ? 0.7382 0.6536 0.5797 0.0133  0.0620  -0.0232 254 LEU A CD2 
1973 N N   . ALA A 255 ? 0.6165 0.5340 0.5089 -0.0114 0.0554  -0.0200 255 ALA A N   
1974 C CA  . ALA A 255 ? 0.6046 0.5226 0.5048 -0.0140 0.0537  -0.0208 255 ALA A CA  
1975 C C   . ALA A 255 ? 0.6375 0.5528 0.5398 -0.0113 0.0577  -0.0112 255 ALA A C   
1976 O O   . ALA A 255 ? 0.6453 0.5623 0.5491 -0.0078 0.0561  -0.0099 255 ALA A O   
1977 C CB  . ALA A 255 ? 0.6214 0.5349 0.5296 -0.0237 0.0540  -0.0255 255 ALA A CB  
1978 N N   . LYS A 256 ? 0.6314 0.5424 0.5363 -0.0129 0.0629  -0.0044 256 LYS A N   
1979 C CA  . LYS A 256 ? 0.6366 0.5445 0.5464 -0.0108 0.0679  0.0048  256 LYS A CA  
1980 C C   . LYS A 256 ? 0.6913 0.6000 0.5897 -0.0006 0.0702  0.0106  256 LYS A C   
1981 O O   . LYS A 256 ? 0.6754 0.5823 0.5754 0.0027  0.0715  0.0159  256 LYS A O   
1982 C CB  . LYS A 256 ? 0.6398 0.5438 0.5585 -0.0144 0.0727  0.0098  256 LYS A CB  
1983 C CG  . LYS A 256 ? 0.6664 0.5673 0.5923 -0.0114 0.0800  0.0197  256 LYS A CG  
1984 C CD  . LYS A 256 ? 0.7620 0.6622 0.6878 -0.0074 0.0878  0.0254  256 LYS A CD  
1985 C CE  . LYS A 256 ? 0.7822 0.6783 0.7166 -0.0043 0.0975  0.0359  256 LYS A CE  
1986 N NZ  . LYS A 256 ? 0.8059 0.7004 0.7412 -0.0003 0.1079  0.0414  256 LYS A NZ  
1987 N N   . GLU A 257 ? 0.7471 0.6571 0.6320 0.0050  0.0706  0.0096  257 GLU A N   
1988 C CA  . GLU A 257 ? 0.7610 0.6687 0.6287 0.0157  0.0724  0.0150  257 GLU A CA  
1989 C C   . GLU A 257 ? 0.7563 0.6673 0.6181 0.0205  0.0628  0.0105  257 GLU A C   
1990 O O   . GLU A 257 ? 0.8081 0.7156 0.6620 0.0279  0.0629  0.0171  257 GLU A O   
1991 C CB  . GLU A 257 ? 0.8004 0.7066 0.6525 0.0206  0.0752  0.0136  257 GLU A CB  
1992 C CG  . GLU A 257 ? 0.8110 0.7142 0.6713 0.0174  0.0857  0.0185  257 GLU A CG  
1993 C CD  . GLU A 257 ? 0.8861 0.7881 0.7331 0.0214  0.0887  0.0151  257 GLU A CD  
1994 O OE1 . GLU A 257 ? 0.8635 0.7668 0.6938 0.0261  0.0814  0.0080  257 GLU A OE1 
1995 O OE2 . GLU A 257 ? 0.9275 0.8273 0.7826 0.0198  0.0979  0.0187  257 GLU A OE2 
1996 N N   . GLU A 258 ? 0.7073 0.6245 0.5744 0.0165  0.0543  -0.0007 258 GLU A N   
1997 C CA  . GLU A 258 ? 0.7240 0.6460 0.5901 0.0211  0.0442  -0.0069 258 GLU A CA  
1998 C C   . GLU A 258 ? 0.7225 0.6469 0.6073 0.0163  0.0426  -0.0082 258 GLU A C   
1999 O O   . GLU A 258 ? 0.7107 0.6389 0.5987 0.0210  0.0350  -0.0116 258 GLU A O   
2000 C CB  . GLU A 258 ? 0.7245 0.6522 0.5900 0.0195  0.0366  -0.0194 258 GLU A CB  
2001 C CG  . GLU A 258 ? 0.7554 0.6804 0.6026 0.0240  0.0379  -0.0202 258 GLU A CG  
2002 C CD  . GLU A 258 ? 0.8476 0.7774 0.6991 0.0199  0.0321  -0.0328 258 GLU A CD  
2003 O OE1 . GLU A 258 ? 0.8468 0.7826 0.7125 0.0164  0.0251  -0.0415 258 GLU A OE1 
2004 O OE2 . GLU A 258 ? 0.9080 0.8352 0.7506 0.0200  0.0357  -0.0342 258 GLU A OE2 
2005 N N   . GLY A 259 ? 0.7192 0.6408 0.6164 0.0074  0.0492  -0.0063 259 GLY A N   
2006 C CA  . GLY A 259 ? 0.7012 0.6226 0.6135 0.0032  0.0495  -0.0073 259 GLY A CA  
2007 C C   . GLY A 259 ? 0.6878 0.6122 0.6121 -0.0048 0.0476  -0.0181 259 GLY A C   
2008 O O   . GLY A 259 ? 0.6846 0.6114 0.6209 -0.0053 0.0457  -0.0221 259 GLY A O   
2009 N N   . TRP A 260 ? 0.6783 0.6015 0.6004 -0.0109 0.0489  -0.0226 260 TRP A N   
2010 C CA  . TRP A 260 ? 0.6313 0.5540 0.5625 -0.0191 0.0495  -0.0316 260 TRP A CA  
2011 C C   . TRP A 260 ? 0.5323 0.4464 0.4595 -0.0269 0.0543  -0.0298 260 TRP A C   
2012 O O   . TRP A 260 ? 0.6153 0.5253 0.5388 -0.0266 0.0567  -0.0222 260 TRP A O   
2013 C CB  . TRP A 260 ? 0.6650 0.5948 0.5981 -0.0176 0.0439  -0.0411 260 TRP A CB  
2014 C CG  . TRP A 260 ? 0.7067 0.6381 0.6269 -0.0135 0.0409  -0.0410 260 TRP A CG  
2015 C CD1 . TRP A 260 ? 0.7517 0.6851 0.6593 -0.0041 0.0374  -0.0365 260 TRP A CD1 
2016 C CD2 . TRP A 260 ? 0.6337 0.5632 0.5511 -0.0183 0.0420  -0.0458 260 TRP A CD2 
2017 N NE1 . TRP A 260 ? 0.6693 0.6024 0.5666 -0.0029 0.0368  -0.0389 260 TRP A NE1 
2018 C CE2 . TRP A 260 ? 0.6888 0.6202 0.5935 -0.0116 0.0392  -0.0446 260 TRP A CE2 
2019 C CE3 . TRP A 260 ? 0.5804 0.5049 0.5033 -0.0272 0.0457  -0.0506 260 TRP A CE3 
2020 C CZ2 . TRP A 260 ? 0.6785 0.6084 0.5787 -0.0137 0.0397  -0.0487 260 TRP A CZ2 
2021 C CZ3 . TRP A 260 ? 0.6284 0.5509 0.5463 -0.0292 0.0456  -0.0538 260 TRP A CZ3 
2022 C CH2 . TRP A 260 ? 0.6210 0.5470 0.5292 -0.0225 0.0425  -0.0531 260 TRP A CH2 
2023 N N   . LEU A 261 ? 0.5311 0.4417 0.4601 -0.0339 0.0557  -0.0369 261 LEU A N   
2024 C CA  . LEU A 261 ? 0.5332 0.4331 0.4568 -0.0410 0.0587  -0.0355 261 LEU A CA  
2025 C C   . LEU A 261 ? 0.5765 0.4743 0.4961 -0.0444 0.0583  -0.0409 261 LEU A C   
2026 O O   . LEU A 261 ? 0.6010 0.5025 0.5260 -0.0453 0.0583  -0.0484 261 LEU A O   
2027 C CB  . LEU A 261 ? 0.5258 0.4165 0.4519 -0.0470 0.0631  -0.0372 261 LEU A CB  
2028 C CG  . LEU A 261 ? 0.5409 0.4308 0.4719 -0.0450 0.0643  -0.0324 261 LEU A CG  
2029 C CD1 . LEU A 261 ? 0.5790 0.4580 0.5103 -0.0513 0.0694  -0.0362 261 LEU A CD1 
2030 C CD2 . LEU A 261 ? 0.5664 0.4541 0.4945 -0.0433 0.0629  -0.0240 261 LEU A CD2 
2031 N N   . ALA A 262 ? 0.5323 0.4239 0.4449 -0.0464 0.0577  -0.0374 262 ALA A N   
2032 C CA  . ALA A 262 ? 0.5099 0.3964 0.4179 -0.0500 0.0575  -0.0412 262 ALA A CA  
2033 C C   . ALA A 262 ? 0.5052 0.3773 0.4059 -0.0558 0.0579  -0.0383 262 ALA A C   
2034 O O   . ALA A 262 ? 0.4624 0.3325 0.3626 -0.0547 0.0553  -0.0324 262 ALA A O   
2035 C CB  . ALA A 262 ? 0.5247 0.4177 0.4311 -0.0450 0.0548  -0.0400 262 ALA A CB  
2036 N N   . GLU A 263 ? 0.4788 0.3399 0.3738 -0.0616 0.0612  -0.0427 263 GLU A N   
2037 C CA  . GLU A 263 ? 0.5363 0.3805 0.4196 -0.0666 0.0612  -0.0404 263 GLU A CA  
2038 C C   . GLU A 263 ? 0.5613 0.3916 0.4333 -0.0710 0.0629  -0.0430 263 GLU A C   
2039 O O   . GLU A 263 ? 0.5693 0.4018 0.4448 -0.0722 0.0673  -0.0480 263 GLU A O   
2040 C CB  . GLU A 263 ? 0.5548 0.3934 0.4370 -0.0692 0.0659  -0.0420 263 GLU A CB  
2041 C CG  . GLU A 263 ? 0.4977 0.3477 0.3910 -0.0648 0.0646  -0.0388 263 GLU A CG  
2042 C CD  . GLU A 263 ? 0.4873 0.3362 0.3807 -0.0630 0.0588  -0.0322 263 GLU A CD  
2043 O OE1 . GLU A 263 ? 0.4916 0.3285 0.3760 -0.0661 0.0549  -0.0309 263 GLU A OE1 
2044 O OE2 . GLU A 263 ? 0.5697 0.4292 0.4732 -0.0583 0.0582  -0.0282 263 GLU A OE2 
2045 N N   . HIS A 264 ? 0.5638 0.3784 0.4222 -0.0734 0.0589  -0.0395 264 HIS A N   
2046 C CA  . HIS A 264 ? 0.5903 0.3870 0.4331 -0.0770 0.0596  -0.0401 264 HIS A CA  
2047 C C   . HIS A 264 ? 0.5881 0.3680 0.4166 -0.0821 0.0683  -0.0433 264 HIS A C   
2048 O O   . HIS A 264 ? 0.5581 0.3182 0.3668 -0.0846 0.0667  -0.0415 264 HIS A O   
2049 C CB  . HIS A 264 ? 0.5895 0.3764 0.4241 -0.0760 0.0493  -0.0349 264 HIS A CB  
2050 C CG  . HIS A 264 ? 0.5665 0.3351 0.3849 -0.0781 0.0478  -0.0343 264 HIS A CG  
2051 N ND1 . HIS A 264 ? 0.5539 0.3061 0.3583 -0.0780 0.0381  -0.0304 264 HIS A ND1 
2052 C CD2 . HIS A 264 ? 0.5211 0.2844 0.3357 -0.0799 0.0543  -0.0368 264 HIS A CD2 
2053 C CE1 . HIS A 264 ? 0.5356 0.2720 0.3258 -0.0793 0.0387  -0.0299 264 HIS A CE1 
2054 N NE2 . HIS A 264 ? 0.6059 0.3486 0.4024 -0.0808 0.0494  -0.0336 264 HIS A NE2 
2055 N N   . MET A 265 ? 0.5751 0.3625 0.4143 -0.0834 0.0778  -0.0486 265 MET A N   
2056 C CA  . MET A 265 ? 0.5870 0.3626 0.4197 -0.0878 0.0888  -0.0523 265 MET A CA  
2057 C C   . MET A 265 ? 0.6240 0.3969 0.4624 -0.0912 0.0998  -0.0578 265 MET A C   
2058 O O   . MET A 265 ? 0.5480 0.3379 0.4060 -0.0893 0.0990  -0.0612 265 MET A O   
2059 C CB  . MET A 265 ? 0.5852 0.3745 0.4332 -0.0859 0.0907  -0.0543 265 MET A CB  
2060 C CG  . MET A 265 ? 0.6217 0.4103 0.4650 -0.0838 0.0831  -0.0498 265 MET A CG  
2061 S SD  . MET A 265 ? 0.6164 0.4198 0.4790 -0.0814 0.0867  -0.0518 265 MET A SD  
2062 C CE  . MET A 265 ? 0.5906 0.3887 0.4460 -0.0800 0.0779  -0.0462 265 MET A CE  
2063 N N   . LEU A 266 ? 0.6856 0.4360 0.5068 -0.0961 0.1107  -0.0589 266 LEU A N   
2064 C CA  . LEU A 266 ? 0.5912 0.3380 0.4219 -0.1003 0.1251  -0.0646 266 LEU A CA  
2065 C C   . LEU A 266 ? 0.6186 0.3792 0.4724 -0.1006 0.1327  -0.0706 266 LEU A C   
2066 O O   . LEU A 266 ? 0.5883 0.3540 0.4430 -0.0984 0.1293  -0.0696 266 LEU A O   
2067 C CB  . LEU A 266 ? 0.6609 0.3755 0.4622 -0.1052 0.1363  -0.0628 266 LEU A CB  
2068 C CG  . LEU A 266 ? 0.6457 0.3420 0.4267 -0.1072 0.1435  -0.0625 266 LEU A CG  
2069 C CD1 . LEU A 266 ? 0.6790 0.3731 0.4737 -0.1113 0.1629  -0.0691 266 LEU A CD1 
2070 C CD2 . LEU A 266 ? 0.6293 0.2927 0.3687 -0.1085 0.1426  -0.0571 266 LEU A CD2 
2071 N N   . ILE A 267 ? 0.5887 0.3551 0.4638 -0.1032 0.1429  -0.0773 267 ILE A N   
2072 C CA  . ILE A 267 ? 0.6397 0.4175 0.5405 -0.1039 0.1513  -0.0840 267 ILE A CA  
2073 C C   . ILE A 267 ? 0.6107 0.3722 0.5148 -0.1104 0.1711  -0.0889 267 ILE A C   
2074 O O   . ILE A 267 ? 0.7226 0.4836 0.6361 -0.1129 0.1750  -0.0917 267 ILE A O   
2075 C CB  . ILE A 267 ? 0.5975 0.4050 0.5314 -0.0991 0.1415  -0.0890 267 ILE A CB  
2076 C CG1 . ILE A 267 ? 0.6132 0.4339 0.5408 -0.0924 0.1242  -0.0832 267 ILE A CG1 
2077 C CG2 . ILE A 267 ? 0.5308 0.3498 0.4922 -0.0988 0.1478  -0.0956 267 ILE A CG2 
2078 C CD1 . ILE A 267 ? 0.5534 0.3986 0.5044 -0.0870 0.1136  -0.0873 267 ILE A CD1 
2079 N N   . LEU A 268 ? 0.6453 0.3927 0.5425 -0.1133 0.1847  -0.0901 268 LEU A N   
2080 C CA  . LEU A 268 ? 0.6719 0.4024 0.5731 -0.1196 0.2069  -0.0947 268 LEU A CA  
2081 C C   . LEU A 268 ? 0.6674 0.4091 0.5991 -0.1201 0.2171  -0.1019 268 LEU A C   
2082 O O   . LEU A 268 ? 0.6654 0.4161 0.5992 -0.1163 0.2100  -0.1012 268 LEU A O   
2083 C CB  . LEU A 268 ? 0.7241 0.4175 0.5797 -0.1232 0.2181  -0.0889 268 LEU A CB  
2084 C CG  . LEU A 268 ? 0.7023 0.3798 0.5297 -0.1223 0.2189  -0.0860 268 LEU A CG  
2085 C CD1 . LEU A 268 ? 0.7224 0.3906 0.5592 -0.1258 0.2408  -0.0920 268 LEU A CD1 
2086 C CD2 . LEU A 268 ? 0.7887 0.4345 0.5659 -0.1228 0.2162  -0.0785 268 LEU A CD2 
2087 N N   . GLY A 269 ? 0.7381 0.4791 0.6962 -0.1247 0.2341  -0.1090 269 GLY A N   
2088 C CA  . GLY A 269 ? 0.6669 0.4143 0.6557 -0.1261 0.2480  -0.1165 269 GLY A CA  
2089 C C   . GLY A 269 ? 0.6741 0.3893 0.6433 -0.1326 0.2751  -0.1167 269 GLY A C   
2090 O O   . GLY A 269 ? 0.7391 0.4355 0.6963 -0.1374 0.2876  -0.1155 269 GLY A O   
2091 N N   . ILE A 270 ? 0.7238 0.4311 0.6883 -0.1324 0.2848  -0.1180 270 ILE A N   
2092 C CA  . ILE A 270 ? 0.7623 0.4361 0.7021 -0.1377 0.3114  -0.1181 270 ILE A CA  
2093 C C   . ILE A 270 ? 0.7689 0.4511 0.7496 -0.1394 0.3295  -0.1272 270 ILE A C   
2094 O O   . ILE A 270 ? 0.7454 0.4511 0.7534 -0.1348 0.3185  -0.1306 270 ILE A O   
2095 C CB  . ILE A 270 ? 0.7282 0.3759 0.6120 -0.1361 0.3072  -0.1108 270 ILE A CB  
2096 C CG1 . ILE A 270 ? 0.7875 0.3963 0.6389 -0.1411 0.3351  -0.1110 270 ILE A CG1 
2097 C CG2 . ILE A 270 ? 0.7594 0.4249 0.6519 -0.1307 0.2922  -0.1114 270 ILE A CG2 
2098 C CD1 . ILE A 270 ? 0.8474 0.4256 0.6377 -0.1395 0.3296  -0.1042 270 ILE A CD1 
2099 N N   . THR A 271 ? 0.7963 0.4588 0.7829 -0.1456 0.3579  -0.1311 271 THR A N   
2100 C CA  . THR A 271 ? 0.7855 0.4541 0.8155 -0.1480 0.3791  -0.1405 271 THR A CA  
2101 C C   . THR A 271 ? 0.8510 0.4804 0.8452 -0.1523 0.4090  -0.1395 271 THR A C   
2102 O O   . THR A 271 ? 0.8551 0.4536 0.8073 -0.1551 0.4212  -0.1342 271 THR A O   
2103 C CB  . THR A 271 ? 0.7947 0.4795 0.8783 -0.1520 0.3883  -0.1482 271 THR A CB  
2104 O OG1 . THR A 271 ? 0.8247 0.5425 0.9343 -0.1476 0.3594  -0.1493 271 THR A OG1 
2105 C CG2 . THR A 271 ? 0.7665 0.4637 0.9029 -0.1526 0.4065  -0.1587 271 THR A CG2 
2106 N N   . ASN A 272 ? 0.8846 0.5155 0.8940 -0.1512 0.4195  -0.1448 272 ASN A N   
2107 C CA  . ASN A 272 ? 0.9044 0.4988 0.8789 -0.1526 0.4450  -0.1455 272 ASN A CA  
2108 C C   . ASN A 272 ? 0.9064 0.4947 0.9166 -0.1527 0.4674  -0.1543 272 ASN A C   
2109 O O   . ASN A 272 ? 0.8882 0.5074 0.9558 -0.1517 0.4668  -0.1612 272 ASN A O   
2110 C CB  . ASN A 272 ? 0.9072 0.5046 0.8769 -0.1498 0.4415  -0.1470 272 ASN A CB  
2111 C CG  . ASN A 272 ? 0.8401 0.4724 0.8786 -0.1472 0.4401  -0.1561 272 ASN A CG  
2112 O OD1 . ASN A 272 ? 0.9359 0.5910 1.0283 -0.1487 0.4429  -0.1619 272 ASN A OD1 
2113 N ND2 . ASN A 272 ? 0.9228 0.5587 0.9602 -0.1430 0.4350  -0.1577 272 ASN A ND2 
2114 N N   . PRO A 273 ? 0.9828 0.5348 0.9613 -0.1545 0.4846  -0.1515 273 PRO A N   
2115 C CA  . PRO A 273 ? 0.9540 0.5016 0.9678 -0.1551 0.5060  -0.1579 273 PRO A CA  
2116 C C   . PRO A 273 ? 0.9406 0.5188 1.0207 -0.1539 0.5088  -0.1673 273 PRO A C   
2117 O O   . PRO A 273 ? 0.9994 0.5797 1.1190 -0.1541 0.5245  -0.1738 273 PRO A O   
2118 C CB  . PRO A 273 ? 0.9830 0.4823 0.9405 -0.1575 0.5224  -0.1517 273 PRO A CB  
2119 C CG  . PRO A 273 ? 0.9875 0.4640 0.8782 -0.1576 0.5084  -0.1418 273 PRO A CG  
2120 C CD  . PRO A 273 ? 0.9364 0.4464 0.8420 -0.1562 0.4855  -0.1419 273 PRO A CD  
2121 N N   . GLU A 274 ? 0.9656 0.5662 1.0598 -0.1524 0.4943  -0.1681 274 GLU A N   
2122 C CA  . GLU A 274 ? 0.8986 0.5294 1.0570 -0.1503 0.4939  -0.1767 274 GLU A CA  
2123 C C   . GLU A 274 ? 0.9128 0.5867 1.1298 -0.1467 0.4782  -0.1843 274 GLU A C   
2124 O O   . GLU A 274 ? 0.8554 0.5574 1.1233 -0.1438 0.4708  -0.1908 274 GLU A O   
2125 C CB  . GLU A 274 ? 0.8608 0.4918 1.0049 -0.1502 0.4880  -0.1738 274 GLU A CB  
2126 C CG  . GLU A 274 ? 0.9144 0.5034 0.9970 -0.1537 0.5007  -0.1665 274 GLU A CG  
2127 C CD  . GLU A 274 ? 0.9963 0.5673 1.0940 -0.1558 0.5242  -0.1703 274 GLU A CD  
2128 O OE1 . GLU A 274 ? 0.9326 0.5267 1.0932 -0.1543 0.5293  -0.1789 274 GLU A OE1 
2129 O OE2 . GLU A 274 ? 1.1297 0.6620 1.1762 -0.1587 0.5373  -0.1651 274 GLU A OE2 
2130 N N   . GLY A 275 ? 0.8474 0.5261 1.0584 -0.1469 0.4722  -0.1835 275 GLY A N   
2131 C CA  . GLY A 275 ? 0.8675 0.5884 1.1327 -0.1455 0.4530  -0.1874 275 GLY A CA  
2132 C C   . GLY A 275 ? 0.8911 0.6364 1.1606 -0.1450 0.4241  -0.1832 275 GLY A C   
2133 O O   . GLY A 275 ? 0.8778 0.6557 1.1990 -0.1427 0.4055  -0.1890 275 GLY A O   
2134 N N   . LYS A 276 ? 0.9245 0.6525 1.1373 -0.1439 0.4150  -0.1741 276 LYS A N   
2135 C CA  . LYS A 276 ? 0.8883 0.6383 1.0936 -0.1357 0.3815  -0.1694 276 LYS A CA  
2136 C C   . LYS A 276 ? 0.8985 0.6416 1.0554 -0.1352 0.3626  -0.1597 276 LYS A C   
2137 O O   . LYS A 276 ? 0.9506 0.6621 1.0553 -0.1390 0.3736  -0.1534 276 LYS A O   
2138 C CB  . LYS A 276 ? 0.9221 0.6623 1.1069 -0.1322 0.3836  -0.1676 276 LYS A CB  
2139 C CG  . LYS A 276 ? 1.0225 0.7890 1.2166 -0.1235 0.3531  -0.1647 276 LYS A CG  
2140 C CD  . LYS A 276 ? 1.0707 0.8298 1.2606 -0.1205 0.3595  -0.1657 276 LYS A CD  
2141 C CE  . LYS A 276 ? 1.0392 0.8231 1.2402 -0.1117 0.3307  -0.1620 276 LYS A CE  
2142 N NZ  . LYS A 276 ? 1.0199 0.8383 1.2808 -0.1066 0.3168  -0.1676 276 LYS A NZ  
2143 N N   . LYS A 277 ? 0.7817 0.5531 0.9553 -0.1300 0.3341  -0.1585 277 LYS A N   
2144 C CA  . LYS A 277 ? 0.7107 0.4797 0.8480 -0.1292 0.3160  -0.1504 277 LYS A CA  
2145 C C   . LYS A 277 ? 0.7320 0.5143 0.8506 -0.1215 0.2887  -0.1437 277 LYS A C   
2146 O O   . LYS A 277 ? 0.6608 0.4674 0.8111 -0.1155 0.2754  -0.1466 277 LYS A O   
2147 C CB  . LYS A 277 ? 0.7261 0.5142 0.8972 -0.1303 0.3081  -0.1551 277 LYS A CB  
2148 C CG  . LYS A 277 ? 0.6691 0.4543 0.8061 -0.1296 0.2912  -0.1476 277 LYS A CG  
2149 C CD  . LYS A 277 ? 0.6545 0.4564 0.8266 -0.1312 0.2860  -0.1539 277 LYS A CD  
2150 C CE  . LYS A 277 ? 0.6932 0.4922 0.8328 -0.1302 0.2700  -0.1470 277 LYS A CE  
2151 N NZ  . LYS A 277 ? 0.6697 0.4826 0.8424 -0.1321 0.2660  -0.1540 277 LYS A NZ  
2152 N N   . LYS A 278 ? 0.6638 0.4295 0.7318 -0.1216 0.2805  -0.1346 278 LYS A N   
2153 C CA  . LYS A 278 ? 0.6392 0.4163 0.6893 -0.1150 0.2557  -0.1277 278 LYS A CA  
2154 C C   . LYS A 278 ? 0.6986 0.4725 0.7204 -0.1151 0.2421  -0.1211 278 LYS A C   
2155 O O   . LYS A 278 ? 0.6529 0.4070 0.6542 -0.1204 0.2533  -0.1198 278 LYS A O   
2156 C CB  . LYS A 278 ? 0.6817 0.4407 0.6998 -0.1142 0.2588  -0.1236 278 LYS A CB  
2157 C CG  . LYS A 278 ? 0.6917 0.4537 0.7375 -0.1134 0.2718  -0.1301 278 LYS A CG  
2158 C CD  . LYS A 278 ? 0.6877 0.4297 0.6998 -0.1129 0.2749  -0.1269 278 LYS A CD  
2159 C CE  . LYS A 278 ? 0.7395 0.4848 0.7812 -0.1117 0.2881  -0.1336 278 LYS A CE  
2160 N NZ  . LYS A 278 ? 0.8060 0.5849 0.8945 -0.1048 0.2721  -0.1355 278 LYS A NZ  
2161 N N   . TYR A 279 ? 0.6129 0.4056 0.6340 -0.1089 0.2188  -0.1166 279 TYR A N   
2162 C CA  . TYR A 279 ? 0.5900 0.3823 0.5875 -0.1079 0.2045  -0.1103 279 TYR A CA  
2163 C C   . TYR A 279 ? 0.6229 0.4042 0.5833 -0.1055 0.1944  -0.1018 279 TYR A C   
2164 O O   . TYR A 279 ? 0.7205 0.5107 0.6862 -0.1012 0.1870  -0.1003 279 TYR A O   
2165 C CB  . TYR A 279 ? 0.6158 0.4371 0.6412 -0.1024 0.1864  -0.1123 279 TYR A CB  
2166 C CG  . TYR A 279 ? 0.6140 0.4455 0.6739 -0.1051 0.1925  -0.1211 279 TYR A CG  
2167 C CD1 . TYR A 279 ? 0.6161 0.4626 0.7185 -0.1042 0.1974  -0.1298 279 TYR A CD1 
2168 C CD2 . TYR A 279 ? 0.6023 0.4285 0.6551 -0.1084 0.1929  -0.1212 279 TYR A CD2 
2169 C CE1 . TYR A 279 ? 0.6233 0.4798 0.7617 -0.1069 0.2020  -0.1390 279 TYR A CE1 
2170 C CE2 . TYR A 279 ? 0.5825 0.4178 0.6695 -0.1113 0.1983  -0.1301 279 TYR A CE2 
2171 C CZ  . TYR A 279 ? 0.6224 0.4732 0.7529 -0.1106 0.2025  -0.1393 279 TYR A CZ  
2172 O OH  . TYR A 279 ? 0.6109 0.4715 0.7797 -0.1137 0.2070  -0.1492 279 TYR A OH  
2173 N N   . LEU A 280 ? 0.6152 0.3768 0.5403 -0.1082 0.1935  -0.0964 280 LEU A N   
2174 C CA  . LEU A 280 ? 0.5790 0.3292 0.4706 -0.1063 0.1827  -0.0891 280 LEU A CA  
2175 C C   . LEU A 280 ? 0.6168 0.3730 0.4981 -0.1040 0.1668  -0.0835 280 LEU A C   
2176 O O   . LEU A 280 ? 0.6066 0.3652 0.4942 -0.1056 0.1682  -0.0849 280 LEU A O   
2177 C CB  . LEU A 280 ? 0.6413 0.3572 0.4951 -0.1110 0.1956  -0.0880 280 LEU A CB  
2178 C CG  . LEU A 280 ? 0.7294 0.4330 0.5869 -0.1138 0.2150  -0.0937 280 LEU A CG  
2179 C CD1 . LEU A 280 ? 0.7323 0.3981 0.5461 -0.1183 0.2288  -0.0925 280 LEU A CD1 
2180 C CD2 . LEU A 280 ? 0.6313 0.3460 0.4996 -0.1099 0.2082  -0.0943 280 LEU A CD2 
2181 N N   . ALA A 281 ? 0.5990 0.3575 0.4668 -0.1003 0.1522  -0.0777 281 ALA A N   
2182 C CA  . ALA A 281 ? 0.6195 0.3814 0.4762 -0.0980 0.1379  -0.0719 281 ALA A CA  
2183 C C   . ALA A 281 ? 0.6191 0.3585 0.4417 -0.0991 0.1328  -0.0668 281 ALA A C   
2184 O O   . ALA A 281 ? 0.6377 0.3679 0.4507 -0.0994 0.1341  -0.0670 281 ALA A O   
2185 C CB  . ALA A 281 ? 0.5024 0.2909 0.3801 -0.0917 0.1238  -0.0697 281 ALA A CB  
2186 N N   . ALA A 282 ? 0.6191 0.3494 0.4245 -0.0994 0.1260  -0.0628 282 ALA A N   
2187 C CA  . ALA A 282 ? 0.6554 0.3632 0.4286 -0.0999 0.1187  -0.0584 282 ALA A CA  
2188 C C   . ALA A 282 ? 0.6502 0.3659 0.4237 -0.0965 0.1028  -0.0531 282 ALA A C   
2189 O O   . ALA A 282 ? 0.6332 0.3556 0.4144 -0.0962 0.1025  -0.0526 282 ALA A O   
2190 C CB  . ALA A 282 ? 0.6396 0.3159 0.3818 -0.1043 0.1306  -0.0591 282 ALA A CB  
2191 N N   . ALA A 283 ? 0.6485 0.3632 0.4159 -0.0942 0.0900  -0.0496 283 ALA A N   
2192 C CA  . ALA A 283 ? 0.6356 0.3568 0.4056 -0.0910 0.0751  -0.0447 283 ALA A CA  
2193 C C   . ALA A 283 ? 0.6064 0.3004 0.3453 -0.0921 0.0672  -0.0422 283 ALA A C   
2194 O O   . ALA A 283 ? 0.6133 0.2966 0.3405 -0.0922 0.0610  -0.0425 283 ALA A O   
2195 C CB  . ALA A 283 ? 0.5714 0.3135 0.3635 -0.0872 0.0665  -0.0426 283 ALA A CB  
2196 N N   . PHE A 284 ? 0.5939 0.2757 0.3190 -0.0926 0.0666  -0.0402 284 PHE A N   
2197 C CA  . PHE A 284 ? 0.6515 0.3084 0.3480 -0.0920 0.0557  -0.0369 284 PHE A CA  
2198 C C   . PHE A 284 ? 0.6604 0.3281 0.3703 -0.0884 0.0426  -0.0327 284 PHE A C   
2199 O O   . PHE A 284 ? 0.6394 0.3251 0.3701 -0.0875 0.0470  -0.0327 284 PHE A O   
2200 C CB  . PHE A 284 ? 0.7067 0.3336 0.3701 -0.0951 0.0665  -0.0370 284 PHE A CB  
2201 C CG  . PHE A 284 ? 0.7113 0.3256 0.3618 -0.0988 0.0832  -0.0414 284 PHE A CG  
2202 C CD1 . PHE A 284 ? 0.7368 0.3532 0.3885 -0.0990 0.0819  -0.0445 284 PHE A CD1 
2203 C CD2 . PHE A 284 ? 0.7873 0.3868 0.4261 -0.1023 0.1015  -0.0428 284 PHE A CD2 
2204 C CE1 . PHE A 284 ? 0.6871 0.2914 0.3282 -0.1022 0.0984  -0.0491 284 PHE A CE1 
2205 C CE2 . PHE A 284 ? 0.7801 0.3675 0.4094 -0.1058 0.1188  -0.0472 284 PHE A CE2 
2206 C CZ  . PHE A 284 ? 0.7180 0.3079 0.3481 -0.1056 0.1173  -0.0505 284 PHE A CZ  
2207 N N   . PRO A 285 ? 0.6691 0.3262 0.3690 -0.0861 0.0261  -0.0298 285 PRO A N   
2208 C CA  . PRO A 285 ? 0.6931 0.3595 0.4080 -0.0824 0.0141  -0.0261 285 PRO A CA  
2209 C C   . PRO A 285 ? 0.7862 0.4426 0.4910 -0.0826 0.0195  -0.0242 285 PRO A C   
2210 O O   . PRO A 285 ? 0.8098 0.4507 0.4952 -0.0858 0.0327  -0.0255 285 PRO A O   
2211 C CB  . PRO A 285 ? 0.6729 0.3234 0.3746 -0.0803 -0.0047 -0.0244 285 PRO A CB  
2212 C CG  . PRO A 285 ? 0.7185 0.3640 0.4122 -0.0825 -0.0033 -0.0281 285 PRO A CG  
2213 C CD  . PRO A 285 ? 0.7124 0.3507 0.3913 -0.0863 0.0165  -0.0309 285 PRO A CD  
2214 N N   . SER A 286 ? 0.7648 0.4296 0.4844 -0.0791 0.0104  -0.0212 286 SER A N   
2215 C CA  . SER A 286 ? 0.8041 0.4593 0.5163 -0.0790 0.0149  -0.0194 286 SER A CA  
2216 C C   . SER A 286 ? 0.8253 0.4440 0.4973 -0.0797 0.0121  -0.0164 286 SER A C   
2217 O O   . SER A 286 ? 0.8066 0.4094 0.4611 -0.0776 -0.0025 -0.0146 286 SER A O   
2218 C CB  . SER A 286 ? 0.8255 0.4957 0.5620 -0.0746 0.0049  -0.0170 286 SER A CB  
2219 O OG  . SER A 286 ? 0.7520 0.4530 0.5211 -0.0733 0.0080  -0.0193 286 SER A OG  
2220 N N   . ALA A 287 ? 0.8848 0.4890 0.5418 -0.0824 0.0262  -0.0161 287 ALA A N   
2221 C CA  . ALA A 287 ? 0.9328 0.4990 0.5477 -0.0830 0.0278  -0.0124 287 ALA A CA  
2222 C C   . ALA A 287 ? 0.9410 0.4867 0.5251 -0.0844 0.0271  -0.0137 287 ALA A C   
2223 O O   . ALA A 287 ? 0.9220 0.4390 0.4720 -0.0819 0.0153  -0.0104 287 ALA A O   
2224 C CB  . ALA A 287 ? 0.9452 0.4972 0.5507 -0.0779 0.0107  -0.0066 287 ALA A CB  
2225 N N   . CYS A 288 ? 0.9398 0.4995 0.5357 -0.0879 0.0393  -0.0189 288 CYS A N   
2226 C CA  . CYS A 288 ? 0.9235 0.4656 0.4934 -0.0896 0.0414  -0.0214 288 CYS A CA  
2227 C C   . CYS A 288 ? 0.9287 0.4619 0.4888 -0.0947 0.0660  -0.0249 288 CYS A C   
2228 O O   . CYS A 288 ? 0.9052 0.4240 0.4450 -0.0964 0.0711  -0.0278 288 CYS A O   
2229 C CB  . CYS A 288 ? 0.8457 0.4119 0.4406 -0.0885 0.0306  -0.0246 288 CYS A CB  
2230 S SG  . CYS A 288 ? 0.9119 0.4727 0.5032 -0.0832 0.0011  -0.0219 288 CYS A SG  
2231 N N   . GLY A 289 ? 0.9349 0.4763 0.5113 -0.0973 0.0816  -0.0254 289 GLY A N   
2232 C CA  . GLY A 289 ? 0.8659 0.3925 0.4309 -0.1022 0.1056  -0.0281 289 GLY A CA  
2233 C C   . GLY A 289 ? 0.8401 0.3965 0.4455 -0.1055 0.1202  -0.0344 289 GLY A C   
2234 O O   . GLY A 289 ? 0.8180 0.3651 0.4201 -0.1097 0.1402  -0.0379 289 GLY A O   
2235 N N   . LYS A 290 ? 0.7749 0.3659 0.4184 -0.1033 0.1106  -0.0360 290 LYS A N   
2236 C CA  . LYS A 290 ? 0.7411 0.3602 0.4217 -0.1053 0.1212  -0.0423 290 LYS A CA  
2237 C C   . LYS A 290 ? 0.8014 0.4156 0.4906 -0.1095 0.1394  -0.0450 290 LYS A C   
2238 O O   . LYS A 290 ? 0.7534 0.3707 0.4554 -0.1131 0.1557  -0.0504 290 LYS A O   
2239 C CB  . LYS A 290 ? 0.7689 0.4221 0.4828 -0.1013 0.1071  -0.0428 290 LYS A CB  
2240 C CG  . LYS A 290 ? 0.7087 0.3722 0.4249 -0.0980 0.0934  -0.0415 290 LYS A CG  
2241 C CD  . LYS A 290 ? 0.6738 0.3710 0.4243 -0.0944 0.0852  -0.0425 290 LYS A CD  
2242 C CE  . LYS A 290 ? 0.6329 0.3368 0.3913 -0.0916 0.0768  -0.0397 290 LYS A CE  
2243 N NZ  . LYS A 290 ? 0.6575 0.3447 0.3962 -0.0894 0.0633  -0.0340 290 LYS A NZ  
2244 N N   . THR A 291 ? 0.8217 0.4280 0.5066 -0.1090 0.1371  -0.0416 291 THR A N   
2245 C CA  . THR A 291 ? 0.8128 0.4151 0.5098 -0.1132 0.1541  -0.0445 291 THR A CA  
2246 C C   . THR A 291 ? 0.7934 0.3635 0.4639 -0.1179 0.1750  -0.0440 291 THR A C   
2247 O O   . THR A 291 ? 0.7926 0.3665 0.4834 -0.1225 0.1937  -0.0497 291 THR A O   
2248 C CB  . THR A 291 ? 0.7804 0.3775 0.4757 -0.1114 0.1473  -0.0403 291 THR A CB  
2249 O OG1 . THR A 291 ? 0.8277 0.4559 0.5513 -0.1073 0.1316  -0.0422 291 THR A OG1 
2250 C CG2 . THR A 291 ? 0.8324 0.4217 0.5394 -0.1163 0.1659  -0.0433 291 THR A CG2 
2251 N N   . ASN A 292 ? 0.8388 0.3763 0.4642 -0.1166 0.1723  -0.0377 292 ASN A N   
2252 C CA  . ASN A 292 ? 0.8993 0.4023 0.4929 -0.1205 0.1933  -0.0368 292 ASN A CA  
2253 C C   . ASN A 292 ? 0.8440 0.3571 0.4526 -0.1234 0.2065  -0.0439 292 ASN A C   
2254 O O   . ASN A 292 ? 0.8583 0.3587 0.4688 -0.1283 0.2306  -0.0471 292 ASN A O   
2255 C CB  . ASN A 292 ? 0.9713 0.4374 0.5099 -0.1172 0.1840  -0.0292 292 ASN A CB  
2256 C CG  . ASN A 292 ? 1.0390 0.4864 0.5584 -0.1146 0.1761  -0.0215 292 ASN A CG  
2257 O OD1 . ASN A 292 ? 1.1457 0.5594 0.6359 -0.1164 0.1913  -0.0171 292 ASN A OD1 
2258 N ND2 . ASN A 292 ? 0.9995 0.4678 0.5360 -0.1101 0.1534  -0.0197 292 ASN A ND2 
2259 N N   . LEU A 293 ? 0.9216 0.4569 0.5428 -0.1205 0.1920  -0.0465 293 LEU A N   
2260 C CA  . LEU A 293 ? 0.8523 0.3974 0.4892 -0.1227 0.2037  -0.0531 293 LEU A CA  
2261 C C   . LEU A 293 ? 0.8253 0.4020 0.5140 -0.1251 0.2129  -0.0603 293 LEU A C   
2262 O O   . LEU A 293 ? 0.7798 0.3552 0.4826 -0.1289 0.2324  -0.0659 293 LEU A O   
2263 C CB  . LEU A 293 ? 0.7663 0.3242 0.4016 -0.1187 0.1855  -0.0534 293 LEU A CB  
2264 C CG  . LEU A 293 ? 0.8215 0.3904 0.4738 -0.1201 0.1950  -0.0598 293 LEU A CG  
2265 C CD1 . LEU A 293 ? 0.8288 0.3626 0.4476 -0.1235 0.2157  -0.0613 293 LEU A CD1 
2266 C CD2 . LEU A 293 ? 0.8026 0.3885 0.4607 -0.1159 0.1754  -0.0596 293 LEU A CD2 
2267 N N   . ALA A 294 ? 0.7965 0.4008 0.5142 -0.1227 0.1989  -0.0608 294 ALA A N   
2268 C CA  . ALA A 294 ? 0.7550 0.3903 0.5209 -0.1238 0.2031  -0.0684 294 ALA A CA  
2269 C C   . ALA A 294 ? 0.8334 0.4589 0.6134 -0.1295 0.2249  -0.0725 294 ALA A C   
2270 O O   . ALA A 294 ? 0.8283 0.4747 0.6483 -0.1314 0.2326  -0.0806 294 ALA A O   
2271 C CB  . ALA A 294 ? 0.7129 0.3754 0.4999 -0.1194 0.1833  -0.0680 294 ALA A CB  
2272 N N   . MET A 295 ? 0.8084 0.4022 0.5580 -0.1321 0.2349  -0.0672 295 MET A N   
2273 C CA  . MET A 295 ? 0.8782 0.4590 0.6400 -0.1380 0.2580  -0.0702 295 MET A CA  
2274 C C   . MET A 295 ? 0.9274 0.4637 0.6431 -0.1409 0.2772  -0.0644 295 MET A C   
2275 O O   . MET A 295 ? 0.9864 0.4989 0.6891 -0.1439 0.2906  -0.0608 295 MET A O   
2276 C CB  . MET A 295 ? 0.8598 0.4489 0.6387 -0.1381 0.2519  -0.0700 295 MET A CB  
2277 C CG  . MET A 295 ? 0.8486 0.4213 0.5917 -0.1341 0.2364  -0.0604 295 MET A CG  
2278 S SD  . MET A 295 ? 0.9158 0.4978 0.6814 -0.1341 0.2306  -0.0610 295 MET A SD  
2279 C CE  . MET A 295 ? 0.8376 0.4692 0.6516 -0.1305 0.2121  -0.0702 295 MET A CE  
2280 N N   . MET A 296 ? 0.9508 0.4737 0.6397 -0.1398 0.2795  -0.0633 296 MET A N   
2281 C CA  . MET A 296 ? 0.9579 0.4357 0.5965 -0.1417 0.2970  -0.0581 296 MET A CA  
2282 C C   . MET A 296 ? 0.9443 0.4093 0.5988 -0.1483 0.3303  -0.0630 296 MET A C   
2283 O O   . MET A 296 ? 0.8958 0.3891 0.6017 -0.1511 0.3383  -0.0719 296 MET A O   
2284 C CB  . MET A 296 ? 0.9936 0.4600 0.5986 -0.1385 0.2891  -0.0570 296 MET A CB  
2285 C CG  . MET A 296 ? 1.0260 0.5078 0.6580 -0.1405 0.3012  -0.0655 296 MET A CG  
2286 S SD  . MET A 296 ? 1.0857 0.5384 0.6681 -0.1385 0.3031  -0.0647 296 MET A SD  
2287 C CE  . MET A 296 ? 1.0798 0.5659 0.7144 -0.1399 0.3112  -0.0753 296 MET A CE  
2288 N N   . ASN A 297 ? 0.9197 0.3447 0.5311 -0.1485 0.3474  -0.0579 297 ASN A N   
2289 C CA  . ASN A 297 ? 1.0674 0.4831 0.6902 -0.1491 0.3753  -0.0644 297 ASN A CA  
2290 C C   . ASN A 297 ? 1.0527 0.4477 0.6456 -0.1479 0.3840  -0.0667 297 ASN A C   
2291 O O   . ASN A 297 ? 1.0419 0.4004 0.5767 -0.1445 0.3803  -0.0605 297 ASN A O   
2292 C CB  . ASN A 297 ? 1.0881 0.4743 0.6847 -0.1471 0.3865  -0.0596 297 ASN A CB  
2293 C CG  . ASN A 297 ? 1.1861 0.5655 0.8051 -0.1482 0.4160  -0.0670 297 ASN A CG  
2294 O OD1 . ASN A 297 ? 1.2424 0.6497 0.9132 -0.1510 0.4260  -0.0766 297 ASN A OD1 
2295 N ND2 . ASN A 297 ? 1.1573 0.4985 0.7382 -0.1456 0.4296  -0.0627 297 ASN A ND2 
2296 N N   . PRO A 298 ? 1.0370 0.4530 0.6674 -0.1500 0.3938  -0.0756 298 PRO A N   
2297 C CA  . PRO A 298 ? 1.0644 0.4605 0.6682 -0.1489 0.4010  -0.0781 298 PRO A CA  
2298 C C   . PRO A 298 ? 1.0815 0.4348 0.6511 -0.1472 0.4220  -0.0781 298 PRO A C   
2299 O O   . PRO A 298 ? 1.1439 0.4940 0.7351 -0.1479 0.4411  -0.0815 298 PRO A O   
2300 C CB  . PRO A 298 ? 0.9905 0.4221 0.6537 -0.1516 0.4088  -0.0882 298 PRO A CB  
2301 C CG  . PRO A 298 ? 1.0245 0.4963 0.7374 -0.1537 0.3954  -0.0891 298 PRO A CG  
2302 C CD  . PRO A 298 ? 1.0112 0.4711 0.7114 -0.1531 0.3948  -0.0838 298 PRO A CD  
2303 N N   . THR A 299 ? 1.1102 0.4298 0.6265 -0.1450 0.4178  -0.0740 299 THR A N   
2304 C CA  . THR A 299 ? 1.1739 0.4491 0.6533 -0.1435 0.4364  -0.0730 299 THR A CA  
2305 C C   . THR A 299 ? 1.2024 0.4750 0.7032 -0.1459 0.4565  -0.0808 299 THR A C   
2306 O O   . THR A 299 ? 1.2781 0.5209 0.7680 -0.1460 0.4791  -0.0823 299 THR A O   
2307 C CB  . THR A 299 ? 1.1997 0.4368 0.6082 -0.1393 0.4200  -0.0639 299 THR A CB  
2308 O OG1 . THR A 299 ? 1.1610 0.4079 0.5611 -0.1392 0.4038  -0.0643 299 THR A OG1 
2309 C CG2 . THR A 299 ? 1.1598 0.3955 0.5464 -0.1364 0.4006  -0.0558 299 THR A CG2 
2310 N N   . LEU A 300 ? 1.1682 0.4703 0.6994 -0.1479 0.4495  -0.0854 300 LEU A N   
2311 C CA  . LEU A 300 ? 1.1154 0.4181 0.6726 -0.1503 0.4680  -0.0927 300 LEU A CA  
2312 C C   . LEU A 300 ? 1.1587 0.4836 0.7785 -0.1525 0.4883  -0.1020 300 LEU A C   
2313 O O   . LEU A 300 ? 1.1342 0.4984 0.7989 -0.1529 0.4800  -0.1055 300 LEU A O   
2314 C CB  . LEU A 300 ? 1.1111 0.4413 0.6845 -0.1511 0.4536  -0.0947 300 LEU A CB  
2315 C CG  . LEU A 300 ? 1.0971 0.4116 0.6159 -0.1482 0.4321  -0.0875 300 LEU A CG  
2316 C CD1 . LEU A 300 ? 1.0908 0.4385 0.6352 -0.1480 0.4197  -0.0914 300 LEU A CD1 
2317 C CD2 . LEU A 300 ? 1.1377 0.4047 0.6040 -0.1470 0.4426  -0.0841 300 LEU A CD2 
2318 N N   . PRO A 301 ? 1.1725 0.4740 0.7981 -0.1536 0.5143  -0.1062 301 PRO A N   
2319 C CA  . PRO A 301 ? 1.1143 0.4377 0.8031 -0.1550 0.5330  -0.1160 301 PRO A CA  
2320 C C   . PRO A 301 ? 1.0913 0.4607 0.8423 -0.1563 0.5279  -0.1239 301 PRO A C   
2321 O O   . PRO A 301 ? 1.0892 0.4597 0.8349 -0.1572 0.5237  -0.1238 301 PRO A O   
2322 C CB  . PRO A 301 ? 1.1801 0.4644 0.8530 -0.1556 0.5608  -0.1168 301 PRO A CB  
2323 C CG  . PRO A 301 ? 1.2487 0.4848 0.8420 -0.1539 0.5564  -0.1069 301 PRO A CG  
2324 C CD  . PRO A 301 ? 1.2292 0.4815 0.8023 -0.1532 0.5278  -0.1020 301 PRO A CD  
2325 N N   . GLY A 302 ? 1.0235 0.4308 0.8343 -0.1561 0.5279  -0.1309 302 GLY A N   
2326 C CA  . GLY A 302 ? 0.9848 0.4368 0.8588 -0.1564 0.5222  -0.1391 302 GLY A CA  
2327 C C   . GLY A 302 ? 1.0305 0.5146 0.9124 -0.1556 0.4967  -0.1381 302 GLY A C   
2328 O O   . GLY A 302 ? 1.0283 0.5496 0.9621 -0.1551 0.4904  -0.1448 302 GLY A O   
2329 N N   . TRP A 303 ? 1.0761 0.5499 0.9097 -0.1551 0.4800  -0.1282 303 TRP A N   
2330 C CA  . TRP A 303 ? 0.9601 0.4647 0.7987 -0.1549 0.4543  -0.1242 303 TRP A CA  
2331 C C   . TRP A 303 ? 0.9739 0.4968 0.8290 -0.1556 0.4440  -0.1212 303 TRP A C   
2332 O O   . TRP A 303 ? 0.9166 0.4160 0.7473 -0.1554 0.4521  -0.1176 303 TRP A O   
2333 C CB  . TRP A 303 ? 0.9753 0.4549 0.7497 -0.1541 0.4402  -0.1150 303 TRP A CB  
2334 C CG  . TRP A 303 ? 1.0257 0.4940 0.7881 -0.1541 0.4442  -0.1167 303 TRP A CG  
2335 C CD1 . TRP A 303 ? 1.0277 0.4589 0.7599 -0.1550 0.4601  -0.1157 303 TRP A CD1 
2336 C CD2 . TRP A 303 ? 0.9333 0.4288 0.7145 -0.1531 0.4320  -0.1189 303 TRP A CD2 
2337 N NE1 . TRP A 303 ? 1.0316 0.4672 0.7638 -0.1550 0.4578  -0.1167 303 TRP A NE1 
2338 C CE2 . TRP A 303 ? 0.9327 0.4080 0.6950 -0.1531 0.4405  -0.1191 303 TRP A CE2 
2339 C CE3 . TRP A 303 ? 0.8775 0.4135 0.6913 -0.1501 0.4097  -0.1204 303 TRP A CE3 
2340 C CZ2 . TRP A 303 ? 0.9145 0.4091 0.6887 -0.1503 0.4313  -0.1221 303 TRP A CZ2 
2341 C CZ3 . TRP A 303 ? 0.9180 0.4712 0.7436 -0.1458 0.3968  -0.1233 303 TRP A CZ3 
2342 C CH2 . TRP A 303 ? 0.8574 0.3882 0.6614 -0.1460 0.4123  -0.1264 303 TRP A CH2 
2343 N N   . LYS A 304 ? 0.8699 0.4321 0.7668 -0.1565 0.4248  -0.1227 304 LYS A N   
2344 C CA  . LYS A 304 ? 0.8299 0.4093 0.7451 -0.1576 0.4109  -0.1206 304 LYS A CA  
2345 C C   . LYS A 304 ? 0.9262 0.5231 0.8378 -0.1569 0.3807  -0.1164 304 LYS A C   
2346 O O   . LYS A 304 ? 0.8693 0.4912 0.8027 -0.1527 0.3672  -0.1203 304 LYS A O   
2347 C CB  . LYS A 304 ? 0.8704 0.4802 0.8542 -0.1582 0.4175  -0.1310 304 LYS A CB  
2348 C CG  . LYS A 304 ? 0.9050 0.5314 0.9087 -0.1593 0.4033  -0.1304 304 LYS A CG  
2349 C CD  . LYS A 304 ? 0.9145 0.5662 0.9831 -0.1599 0.4116  -0.1414 304 LYS A CD  
2350 C CE  . LYS A 304 ? 0.9513 0.6144 1.0347 -0.1611 0.3994  -0.1412 304 LYS A CE  
2351 N NZ  . LYS A 304 ? 0.9550 0.6381 1.0982 -0.1617 0.4092  -0.1521 304 LYS A NZ  
2352 N N   . VAL A 305 ? 0.9226 0.5134 0.8071 -0.1555 0.3655  -0.1091 305 VAL A N   
2353 C CA  . VAL A 305 ? 0.8681 0.4819 0.7480 -0.1493 0.3327  -0.1055 305 VAL A CA  
2354 C C   . VAL A 305 ? 0.8738 0.5105 0.7877 -0.1495 0.3218  -0.1082 305 VAL A C   
2355 O O   . VAL A 305 ? 0.8979 0.5182 0.8077 -0.1537 0.3339  -0.1068 305 VAL A O   
2356 C CB  . VAL A 305 ? 0.9516 0.5384 0.7692 -0.1465 0.3216  -0.0948 305 VAL A CB  
2357 C CG1 . VAL A 305 ? 0.8885 0.4996 0.7072 -0.1406 0.2899  -0.0913 305 VAL A CG1 
2358 C CG2 . VAL A 305 ? 0.9031 0.4691 0.6879 -0.1457 0.3291  -0.0938 305 VAL A CG2 
2359 N N   . GLU A 306 ? 0.7834 0.4562 0.7296 -0.1447 0.2996  -0.1123 306 GLU A N   
2360 C CA  . GLU A 306 ? 0.7964 0.4926 0.7733 -0.1437 0.2860  -0.1161 306 GLU A CA  
2361 C C   . GLU A 306 ? 0.7639 0.4748 0.7233 -0.1369 0.2575  -0.1105 306 GLU A C   
2362 O O   . GLU A 306 ? 0.7437 0.4613 0.6906 -0.1323 0.2460  -0.1075 306 GLU A O   
2363 C CB  . GLU A 306 ? 0.7669 0.4933 0.8044 -0.1441 0.2869  -0.1282 306 GLU A CB  
2364 C CG  . GLU A 306 ? 0.7986 0.5130 0.8637 -0.1515 0.3160  -0.1350 306 GLU A CG  
2365 C CD  . GLU A 306 ? 0.7816 0.5247 0.9069 -0.1511 0.3168  -0.1472 306 GLU A CD  
2366 O OE1 . GLU A 306 ? 0.7445 0.4981 0.8750 -0.1472 0.3119  -0.1482 306 GLU A OE1 
2367 O OE2 . GLU A 306 ? 0.8600 0.6150 1.0291 -0.1546 0.3216  -0.1560 306 GLU A OE2 
2368 N N   . CYS A 307 ? 0.7387 0.4538 0.6986 -0.1363 0.2476  -0.1092 307 CYS A N   
2369 C CA  . CYS A 307 ? 0.7572 0.4811 0.6973 -0.1304 0.2240  -0.1031 307 CYS A CA  
2370 C C   . CYS A 307 ? 0.7443 0.5033 0.7203 -0.1257 0.2061  -0.1097 307 CYS A C   
2371 O O   . CYS A 307 ? 0.6744 0.4444 0.6804 -0.1275 0.2072  -0.1171 307 CYS A O   
2372 C CB  . CYS A 307 ? 0.7736 0.4767 0.6868 -0.1320 0.2242  -0.0967 307 CYS A CB  
2373 S SG  . CYS A 307 ? 0.7157 0.4291 0.6091 -0.1248 0.1972  -0.0896 307 CYS A SG  
2374 N N   . VAL A 308 ? 0.6793 0.4540 0.6508 -0.1194 0.1896  -0.1070 308 VAL A N   
2375 C CA  . VAL A 308 ? 0.5978 0.4014 0.5915 -0.1134 0.1706  -0.1109 308 VAL A CA  
2376 C C   . VAL A 308 ? 0.6206 0.4235 0.5915 -0.1096 0.1562  -0.1044 308 VAL A C   
2377 O O   . VAL A 308 ? 0.5753 0.3923 0.5609 -0.1072 0.1467  -0.1086 308 VAL A O   
2378 C CB  . VAL A 308 ? 0.6697 0.4903 0.6734 -0.1081 0.1624  -0.1114 308 VAL A CB  
2379 C CG1 . VAL A 308 ? 0.6383 0.4858 0.6611 -0.1011 0.1434  -0.1150 308 VAL A CG1 
2380 C CG2 . VAL A 308 ? 0.6256 0.4464 0.6539 -0.1116 0.1773  -0.1180 308 VAL A CG2 
2381 N N   . GLY A 309 ? 0.6231 0.4094 0.5594 -0.1089 0.1541  -0.0949 309 GLY A N   
2382 C CA  . GLY A 309 ? 0.5525 0.3364 0.4688 -0.1056 0.1415  -0.0883 309 GLY A CA  
2383 C C   . GLY A 309 ? 0.6403 0.3987 0.5200 -0.1069 0.1436  -0.0793 309 GLY A C   
2384 O O   . GLY A 309 ? 0.6692 0.4139 0.5366 -0.1095 0.1528  -0.0782 309 GLY A O   
2385 N N   . ASP A 310 ? 0.6388 0.3903 0.5010 -0.1048 0.1343  -0.0735 310 ASP A N   
2386 C CA  . ASP A 310 ? 0.6083 0.3338 0.4355 -0.1056 0.1336  -0.0654 310 ASP A CA  
2387 C C   . ASP A 310 ? 0.6389 0.3696 0.4554 -0.1002 0.1162  -0.0590 310 ASP A C   
2388 O O   . ASP A 310 ? 0.6701 0.3799 0.4592 -0.1001 0.1122  -0.0528 310 ASP A O   
2389 C CB  . ASP A 310 ? 0.6554 0.3573 0.4680 -0.1092 0.1422  -0.0634 310 ASP A CB  
2390 C CG  . ASP A 310 ? 0.6836 0.3921 0.5012 -0.1062 0.1315  -0.0617 310 ASP A CG  
2391 O OD1 . ASP A 310 ? 0.5831 0.3174 0.4260 -0.1030 0.1239  -0.0663 310 ASP A OD1 
2392 O OD2 . ASP A 310 ? 0.6735 0.3600 0.4683 -0.1064 0.1305  -0.0557 310 ASP A OD2 
2393 N N   . ASP A 311 ? 0.6472 0.4036 0.4838 -0.0955 0.1059  -0.0605 311 ASP A N   
2394 C CA  . ASP A 311 ? 0.5940 0.3544 0.4238 -0.0908 0.0917  -0.0545 311 ASP A CA  
2395 C C   . ASP A 311 ? 0.5312 0.3159 0.3779 -0.0858 0.0838  -0.0548 311 ASP A C   
2396 O O   . ASP A 311 ? 0.5017 0.2873 0.3426 -0.0830 0.0754  -0.0496 311 ASP A O   
2397 C CB  . ASP A 311 ? 0.5337 0.2923 0.3643 -0.0894 0.0875  -0.0534 311 ASP A CB  
2398 C CG  . ASP A 311 ? 0.5821 0.3404 0.4056 -0.0851 0.0744  -0.0469 311 ASP A CG  
2399 O OD1 . ASP A 311 ? 0.5311 0.2711 0.3341 -0.0857 0.0704  -0.0417 311 ASP A OD1 
2400 O OD2 . ASP A 311 ? 0.6013 0.3767 0.4398 -0.0808 0.0681  -0.0474 311 ASP A OD2 
2401 N N   . ILE A 312 ? 0.4777 0.2814 0.3456 -0.0843 0.0859  -0.0608 312 ILE A N   
2402 C CA  . ILE A 312 ? 0.4630 0.2880 0.3440 -0.0785 0.0785  -0.0606 312 ILE A CA  
2403 C C   . ILE A 312 ? 0.5428 0.3794 0.4395 -0.0783 0.0829  -0.0663 312 ILE A C   
2404 O O   . ILE A 312 ? 0.4822 0.3201 0.3906 -0.0812 0.0893  -0.0733 312 ILE A O   
2405 C CB  . ILE A 312 ? 0.5534 0.3904 0.4428 -0.0742 0.0726  -0.0622 312 ILE A CB  
2406 C CG1 . ILE A 312 ? 0.5686 0.3945 0.4461 -0.0738 0.0682  -0.0566 312 ILE A CG1 
2407 C CG2 . ILE A 312 ? 0.5532 0.4091 0.4515 -0.0675 0.0665  -0.0614 312 ILE A CG2 
2408 C CD1 . ILE A 312 ? 0.6539 0.4891 0.5392 -0.0700 0.0644  -0.0587 312 ILE A CD1 
2409 N N   . ALA A 313 ? 0.5863 0.4312 0.4856 -0.0750 0.0795  -0.0634 313 ALA A N   
2410 C CA  . ALA A 313 ? 0.4909 0.3473 0.4060 -0.0735 0.0818  -0.0679 313 ALA A CA  
2411 C C   . ALA A 313 ? 0.5172 0.3905 0.4388 -0.0659 0.0732  -0.0652 313 ALA A C   
2412 O O   . ALA A 313 ? 0.4912 0.3635 0.4039 -0.0633 0.0688  -0.0580 313 ALA A O   
2413 C CB  . ALA A 313 ? 0.4990 0.3442 0.4089 -0.0772 0.0890  -0.0668 313 ALA A CB  
2414 N N   . TRP A 314 ? 0.5301 0.4177 0.4673 -0.0621 0.0706  -0.0709 314 TRP A N   
2415 C CA  . TRP A 314 ? 0.5888 0.4901 0.5296 -0.0541 0.0630  -0.0684 314 TRP A CA  
2416 C C   . TRP A 314 ? 0.5821 0.4886 0.5362 -0.0529 0.0645  -0.0707 314 TRP A C   
2417 O O   . TRP A 314 ? 0.5907 0.5021 0.5613 -0.0544 0.0662  -0.0790 314 TRP A O   
2418 C CB  . TRP A 314 ? 0.5180 0.4301 0.4628 -0.0490 0.0561  -0.0735 314 TRP A CB  
2419 C CG  . TRP A 314 ? 0.5250 0.4337 0.4572 -0.0480 0.0542  -0.0703 314 TRP A CG  
2420 C CD1 . TRP A 314 ? 0.5917 0.4897 0.5126 -0.0510 0.0569  -0.0635 314 TRP A CD1 
2421 C CD2 . TRP A 314 ? 0.5218 0.4373 0.4527 -0.0432 0.0487  -0.0744 314 TRP A CD2 
2422 N NE1 . TRP A 314 ? 0.5175 0.4162 0.4327 -0.0484 0.0542  -0.0628 314 TRP A NE1 
2423 C CE2 . TRP A 314 ? 0.4933 0.4021 0.4133 -0.0437 0.0500  -0.0695 314 TRP A CE2 
2424 C CE3 . TRP A 314 ? 0.5144 0.4404 0.4523 -0.0381 0.0421  -0.0824 314 TRP A CE3 
2425 C CZ2 . TRP A 314 ? 0.5603 0.4723 0.4761 -0.0396 0.0468  -0.0723 314 TRP A CZ2 
2426 C CZ3 . TRP A 314 ? 0.5754 0.5035 0.5061 -0.0340 0.0379  -0.0855 314 TRP A CZ3 
2427 C CH2 . TRP A 314 ? 0.5679 0.4890 0.4877 -0.0349 0.0412  -0.0804 314 TRP A CH2 
2428 N N   . MET A 315 ? 0.5790 0.4845 0.5288 -0.0504 0.0641  -0.0638 315 MET A N   
2429 C CA  . MET A 315 ? 0.6328 0.5404 0.5946 -0.0499 0.0669  -0.0650 315 MET A CA  
2430 C C   . MET A 315 ? 0.6369 0.5545 0.6011 -0.0410 0.0598  -0.0601 315 MET A C   
2431 O O   . MET A 315 ? 0.6224 0.5400 0.5746 -0.0369 0.0564  -0.0526 315 MET A O   
2432 C CB  . MET A 315 ? 0.6042 0.4972 0.5580 -0.0559 0.0749  -0.0618 315 MET A CB  
2433 C CG  . MET A 315 ? 0.5698 0.4484 0.5144 -0.0640 0.0821  -0.0650 315 MET A CG  
2434 S SD  . MET A 315 ? 0.6298 0.4883 0.5613 -0.0703 0.0911  -0.0632 315 MET A SD  
2435 C CE  . MET A 315 ? 0.5797 0.4368 0.4993 -0.0669 0.0828  -0.0535 315 MET A CE  
2436 N N   . LYS A 316 ? 0.6522 0.5772 0.6330 -0.0378 0.0583  -0.0641 316 LYS A N   
2437 C CA  . LYS A 316 ? 0.7030 0.6359 0.6859 -0.0285 0.0510  -0.0595 316 LYS A CA  
2438 C C   . LYS A 316 ? 0.6997 0.6360 0.7029 -0.0276 0.0526  -0.0633 316 LYS A C   
2439 O O   . LYS A 316 ? 0.6840 0.6232 0.7050 -0.0314 0.0555  -0.0725 316 LYS A O   
2440 C CB  . LYS A 316 ? 0.7602 0.7029 0.7404 -0.0209 0.0403  -0.0622 316 LYS A CB  
2441 C CG  . LYS A 316 ? 0.7500 0.7006 0.7357 -0.0106 0.0311  -0.0609 316 LYS A CG  
2442 C CD  . LYS A 316 ? 0.8272 0.7851 0.8067 -0.0031 0.0195  -0.0652 316 LYS A CD  
2443 C CE  . LYS A 316 ? 0.8872 0.8398 0.8406 0.0000  0.0199  -0.0577 316 LYS A CE  
2444 N NZ  . LYS A 316 ? 0.9076 0.8549 0.8483 0.0055  0.0225  -0.0451 316 LYS A NZ  
2445 N N   . PHE A 317 ? 0.7251 0.6607 0.7277 -0.0226 0.0516  -0.0561 317 PHE A N   
2446 C CA  . PHE A 317 ? 0.7845 0.7241 0.8078 -0.0200 0.0518  -0.0591 317 PHE A CA  
2447 C C   . PHE A 317 ? 0.8088 0.7613 0.8446 -0.0110 0.0394  -0.0636 317 PHE A C   
2448 O O   . PHE A 317 ? 0.8128 0.7684 0.8340 -0.0032 0.0299  -0.0591 317 PHE A O   
2449 C CB  . PHE A 317 ? 0.7531 0.6867 0.7722 -0.0170 0.0544  -0.0497 317 PHE A CB  
2450 C CG  . PHE A 317 ? 0.7723 0.6931 0.7858 -0.0259 0.0656  -0.0484 317 PHE A CG  
2451 C CD1 . PHE A 317 ? 0.8059 0.7220 0.8333 -0.0313 0.0743  -0.0549 317 PHE A CD1 
2452 C CD2 . PHE A 317 ? 0.8071 0.7196 0.8017 -0.0285 0.0672  -0.0412 317 PHE A CD2 
2453 C CE1 . PHE A 317 ? 0.7585 0.6601 0.7762 -0.0388 0.0838  -0.0543 317 PHE A CE1 
2454 C CE2 . PHE A 317 ? 0.7977 0.6974 0.7862 -0.0361 0.0749  -0.0409 317 PHE A CE2 
2455 C CZ  . PHE A 317 ? 0.7444 0.6377 0.7420 -0.0411 0.0829  -0.0475 317 PHE A CZ  
2456 N N   . ASP A 318 ? 0.7864 0.7455 0.8492 -0.0119 0.0394  -0.0729 318 ASP A N   
2457 C CA  . ASP A 318 ? 0.7201 0.6919 0.7997 -0.0035 0.0255  -0.0791 318 ASP A CA  
2458 C C   . ASP A 318 ? 0.8556 0.8298 0.9449 0.0056  0.0197  -0.0743 318 ASP A C   
2459 O O   . ASP A 318 ? 0.7604 0.7265 0.8424 0.0051  0.0270  -0.0658 318 ASP A O   
2460 C CB  . ASP A 318 ? 0.7981 0.7767 0.9068 -0.0094 0.0281  -0.0930 318 ASP A CB  
2461 C CG  . ASP A 318 ? 0.7811 0.7564 0.9136 -0.0158 0.0419  -0.0969 318 ASP A CG  
2462 O OD1 . ASP A 318 ? 0.8523 0.8192 0.9768 -0.0164 0.0494  -0.0895 318 ASP A OD1 
2463 O OD2 . ASP A 318 ? 0.7158 0.6964 0.8763 -0.0204 0.0462  -0.1079 318 ASP A OD2 
2464 N N   . ALA A 319 ? 0.8593 0.8444 0.9662 0.0142  0.0054  -0.0800 319 ALA A N   
2465 C CA  . ALA A 319 ? 0.8481 0.8350 0.9645 0.0241  -0.0021 -0.0752 319 ALA A CA  
2466 C C   . ALA A 319 ? 0.8548 0.8410 1.0000 0.0189  0.0096  -0.0784 319 ALA A C   
2467 O O   . ALA A 319 ? 0.8519 0.8348 1.0004 0.0246  0.0094  -0.0715 319 ALA A O   
2468 C CB  . ALA A 319 ? 0.8592 0.8572 0.9878 0.0351  -0.0227 -0.0816 319 ALA A CB  
2469 N N   . GLN A 320 ? 0.8294 0.8170 0.9947 0.0085  0.0210  -0.0885 320 GLN A N   
2470 C CA  . GLN A 320 ? 0.8110 0.7958 1.0018 0.0031  0.0350  -0.0925 320 GLN A CA  
2471 C C   . GLN A 320 ? 0.7922 0.7614 0.9611 -0.0044 0.0511  -0.0849 320 GLN A C   
2472 O O   . GLN A 320 ? 0.7644 0.7281 0.9488 -0.0085 0.0636  -0.0875 320 GLN A O   
2473 C CB  . GLN A 320 ? 0.7838 0.7742 1.0042 -0.0050 0.0429  -0.1064 320 GLN A CB  
2474 C CG  . GLN A 320 ? 0.8093 0.8154 1.0531 0.0008  0.0262  -0.1159 320 GLN A CG  
2475 C CD  . GLN A 320 ? 0.8508 0.8674 1.1198 0.0128  0.0107  -0.1170 320 GLN A CD  
2476 O OE1 . GLN A 320 ? 0.8742 0.8886 1.1597 0.0142  0.0173  -0.1150 320 GLN A OE1 
2477 N NE2 . GLN A 320 ? 0.8977 0.9246 1.1691 0.0220  -0.0109 -0.1204 320 GLN A NE2 
2478 N N   . GLY A 321 ? 0.8156 0.7770 0.9502 -0.0059 0.0509  -0.0764 321 GLY A N   
2479 C CA  . GLY A 321 ? 0.7736 0.7203 0.8881 -0.0127 0.0633  -0.0700 321 GLY A CA  
2480 C C   . GLY A 321 ? 0.7864 0.7240 0.8905 -0.0243 0.0755  -0.0748 321 GLY A C   
2481 O O   . GLY A 321 ? 0.7870 0.7113 0.8713 -0.0298 0.0835  -0.0700 321 GLY A O   
2482 N N   . ASN A 322 ? 0.7551 0.6983 0.8722 -0.0281 0.0767  -0.0842 322 ASN A N   
2483 C CA  . ASN A 322 ? 0.7344 0.6669 0.8401 -0.0386 0.0888  -0.0881 322 ASN A CA  
2484 C C   . ASN A 322 ? 0.7511 0.6807 0.8282 -0.0395 0.0829  -0.0825 322 ASN A C   
2485 O O   . ASN A 322 ? 0.7582 0.6976 0.8312 -0.0327 0.0699  -0.0800 322 ASN A O   
2486 C CB  . ASN A 322 ? 0.7104 0.6491 0.8432 -0.0426 0.0941  -0.1000 322 ASN A CB  
2487 C CG  . ASN A 322 ? 0.7720 0.7165 0.9400 -0.0406 0.0989  -0.1065 322 ASN A CG  
2488 O OD1 . ASN A 322 ? 0.7818 0.7419 0.9765 -0.0335 0.0873  -0.1109 322 ASN A OD1 
2489 N ND2 . ASN A 322 ? 0.7667 0.6980 0.9350 -0.0465 0.1157  -0.1076 322 ASN A ND2 
2490 N N   . LEU A 323 ? 0.7449 0.6596 0.8012 -0.0475 0.0924  -0.0808 323 LEU A N   
2491 C CA  . LEU A 323 ? 0.7013 0.6121 0.7337 -0.0493 0.0882  -0.0765 323 LEU A CA  
2492 C C   . LEU A 323 ? 0.6613 0.5746 0.7007 -0.0535 0.0902  -0.0845 323 LEU A C   
2493 O O   . LEU A 323 ? 0.6570 0.5601 0.6988 -0.0610 0.1026  -0.0896 323 LEU A O   
2494 C CB  . LEU A 323 ? 0.7274 0.6205 0.7355 -0.0552 0.0950  -0.0712 323 LEU A CB  
2495 C CG  . LEU A 323 ? 0.7021 0.5905 0.6874 -0.0566 0.0902  -0.0660 323 LEU A CG  
2496 C CD1 . LEU A 323 ? 0.6536 0.5532 0.6361 -0.0486 0.0788  -0.0590 323 LEU A CD1 
2497 C CD2 . LEU A 323 ? 0.6537 0.5238 0.6182 -0.0624 0.0954  -0.0623 323 LEU A CD2 
2498 N N   . ARG A 324 ? 0.6372 0.5625 0.6791 -0.0484 0.0788  -0.0856 324 ARG A N   
2499 C CA  . ARG A 324 ? 0.6536 0.5830 0.7057 -0.0516 0.0789  -0.0940 324 ARG A CA  
2500 C C   . ARG A 324 ? 0.6418 0.5634 0.6694 -0.0546 0.0783  -0.0902 324 ARG A C   
2501 O O   . ARG A 324 ? 0.6635 0.5867 0.6738 -0.0498 0.0702  -0.0830 324 ARG A O   
2502 C CB  . ARG A 324 ? 0.6987 0.6459 0.7706 -0.0437 0.0651  -0.0998 324 ARG A CB  
2503 C CG  . ARG A 324 ? 0.7007 0.6570 0.8032 -0.0403 0.0641  -0.1054 324 ARG A CG  
2504 C CD  . ARG A 324 ? 0.7180 0.6759 0.8500 -0.0472 0.0737  -0.1170 324 ARG A CD  
2505 N NE  . ARG A 324 ? 0.7768 0.7425 0.9415 -0.0447 0.0751  -0.1225 324 ARG A NE  
2506 C CZ  . ARG A 324 ? 0.7630 0.7328 0.9622 -0.0492 0.0832  -0.1333 324 ARG A CZ  
2507 N NH1 . ARG A 324 ? 0.7490 0.7154 0.9543 -0.0566 0.0909  -0.1399 324 ARG A NH1 
2508 N NH2 . ARG A 324 ? 0.8042 0.7814 1.0347 -0.0461 0.0842  -0.1378 324 ARG A NH2 
2509 N N   . ALA A 325 ? 0.6448 0.5573 0.6723 -0.0624 0.0875  -0.0949 325 ALA A N   
2510 C CA  . ALA A 325 ? 0.6142 0.5173 0.6201 -0.0657 0.0878  -0.0915 325 ALA A CA  
2511 C C   . ALA A 325 ? 0.5959 0.5032 0.6147 -0.0681 0.0878  -0.1000 325 ALA A C   
2512 O O   . ALA A 325 ? 0.5675 0.4780 0.6104 -0.0712 0.0939  -0.1086 325 ALA A O   
2513 C CB  . ALA A 325 ? 0.6026 0.4848 0.5889 -0.0729 0.0994  -0.0874 325 ALA A CB  
2514 N N   . ILE A 326 ? 0.5802 0.4874 0.5851 -0.0666 0.0814  -0.0978 326 ILE A N   
2515 C CA  . ILE A 326 ? 0.5676 0.4753 0.5808 -0.0697 0.0820  -0.1051 326 ILE A CA  
2516 C C   . ILE A 326 ? 0.5351 0.4278 0.5244 -0.0734 0.0855  -0.0992 326 ILE A C   
2517 O O   . ILE A 326 ? 0.5397 0.4272 0.5083 -0.0712 0.0822  -0.0903 326 ILE A O   
2518 C CB  . ILE A 326 ? 0.5560 0.4806 0.5798 -0.0625 0.0680  -0.1109 326 ILE A CB  
2519 C CG1 . ILE A 326 ? 0.6299 0.5560 0.6300 -0.0559 0.0589  -0.1027 326 ILE A CG1 
2520 C CG2 . ILE A 326 ? 0.6428 0.5817 0.6906 -0.0577 0.0617  -0.1170 326 ILE A CG2 
2521 C CD1 . ILE A 326 ? 0.6950 0.6336 0.6976 -0.0482 0.0459  -0.1080 326 ILE A CD1 
2522 N N   . ASN A 327 ? 0.5323 0.4177 0.5268 -0.0789 0.0920  -0.1043 327 ASN A N   
2523 C CA  . ASN A 327 ? 0.5527 0.4249 0.5276 -0.0814 0.0933  -0.0997 327 ASN A CA  
2524 C C   . ASN A 327 ? 0.5344 0.4181 0.5142 -0.0768 0.0830  -0.1038 327 ASN A C   
2525 O O   . ASN A 327 ? 0.6090 0.4987 0.6086 -0.0783 0.0832  -0.1135 327 ASN A O   
2526 C CB  . ASN A 327 ? 0.5648 0.4192 0.5398 -0.0897 0.1076  -0.1020 327 ASN A CB  
2527 C CG  . ASN A 327 ? 0.6021 0.4435 0.5609 -0.0916 0.1077  -0.0985 327 ASN A CG  
2528 O OD1 . ASN A 327 ? 0.5586 0.4000 0.5012 -0.0875 0.0990  -0.0921 327 ASN A OD1 
2529 N ND2 . ASN A 327 ? 0.5300 0.3596 0.4953 -0.0977 0.1186  -0.1026 327 ASN A ND2 
2530 N N   . PRO A 328 ? 0.5778 0.4643 0.5415 -0.0713 0.0745  -0.0976 328 PRO A N   
2531 C CA  . PRO A 328 ? 0.5906 0.4870 0.5567 -0.0662 0.0657  -0.1020 328 PRO A CA  
2532 C C   . PRO A 328 ? 0.5963 0.4836 0.5616 -0.0701 0.0690  -0.1051 328 PRO A C   
2533 O O   . PRO A 328 ? 0.5959 0.4901 0.5640 -0.0663 0.0625  -0.1103 328 PRO A O   
2534 C CB  . PRO A 328 ? 0.5583 0.4575 0.5069 -0.0597 0.0594  -0.0929 328 PRO A CB  
2535 C CG  . PRO A 328 ? 0.5457 0.4312 0.4813 -0.0639 0.0653  -0.0838 328 PRO A CG  
2536 C CD  . PRO A 328 ? 0.5217 0.4022 0.4660 -0.0695 0.0732  -0.0867 328 PRO A CD  
2537 N N   . GLU A 329 ? 0.5659 0.4363 0.5255 -0.0770 0.0789  -0.1019 329 GLU A N   
2538 C CA  . GLU A 329 ? 0.5570 0.4156 0.5140 -0.0806 0.0828  -0.1031 329 GLU A CA  
2539 C C   . GLU A 329 ? 0.5509 0.4090 0.5302 -0.0860 0.0898  -0.1136 329 GLU A C   
2540 O O   . GLU A 329 ? 0.5732 0.4389 0.5706 -0.0877 0.0927  -0.1195 329 GLU A O   
2541 C CB  . GLU A 329 ? 0.5329 0.3703 0.4686 -0.0845 0.0890  -0.0932 329 GLU A CB  
2542 C CG  . GLU A 329 ? 0.5317 0.3685 0.4497 -0.0796 0.0812  -0.0837 329 GLU A CG  
2543 C CD  . GLU A 329 ? 0.5486 0.3637 0.4470 -0.0827 0.0839  -0.0755 329 GLU A CD  
2544 O OE1 . GLU A 329 ? 0.5977 0.3977 0.4862 -0.0873 0.0913  -0.0730 329 GLU A OE1 
2545 O OE2 . GLU A 329 ? 0.5710 0.3828 0.4634 -0.0800 0.0786  -0.0719 329 GLU A OE2 
2546 N N   . ASN A 330 ? 0.5089 0.3578 0.4894 -0.0889 0.0930  -0.1160 330 ASN A N   
2547 C CA  . ASN A 330 ? 0.5795 0.4262 0.5833 -0.0946 0.1008  -0.1260 330 ASN A CA  
2548 C C   . ASN A 330 ? 0.6142 0.4362 0.6088 -0.1017 0.1149  -0.1210 330 ASN A C   
2549 O O   . ASN A 330 ? 0.5447 0.3614 0.5586 -0.1074 0.1245  -0.1281 330 ASN A O   
2550 C CB  . ASN A 330 ? 0.5734 0.4319 0.5915 -0.0913 0.0916  -0.1361 330 ASN A CB  
2551 C CG  . ASN A 330 ? 0.5742 0.4387 0.6256 -0.0958 0.0952  -0.1499 330 ASN A CG  
2552 O OD1 . ASN A 330 ? 0.5778 0.4458 0.6464 -0.0992 0.1011  -0.1533 330 ASN A OD1 
2553 N ND2 . ASN A 330 ? 0.5287 0.3944 0.5915 -0.0960 0.0919  -0.1584 330 ASN A ND2 
2554 N N   . GLY A 331 ? 0.6042 0.4100 0.5700 -0.1012 0.1161  -0.1090 331 GLY A N   
2555 C CA  . GLY A 331 ? 0.6065 0.3857 0.5575 -0.1067 0.1281  -0.1031 331 GLY A CA  
2556 C C   . GLY A 331 ? 0.6104 0.3734 0.5294 -0.1056 0.1277  -0.0908 331 GLY A C   
2557 O O   . GLY A 331 ? 0.5940 0.3674 0.5062 -0.1017 0.1197  -0.0876 331 GLY A O   
2558 N N   . PHE A 332 ? 0.5961 0.3322 0.4950 -0.1090 0.1360  -0.0841 332 PHE A N   
2559 C CA  . PHE A 332 ? 0.6383 0.3541 0.5039 -0.1083 0.1351  -0.0731 332 PHE A CA  
2560 C C   . PHE A 332 ? 0.5893 0.2922 0.4377 -0.1050 0.1266  -0.0658 332 PHE A C   
2561 O O   . PHE A 332 ? 0.6731 0.3616 0.5215 -0.1072 0.1328  -0.0657 332 PHE A O   
2562 C CB  . PHE A 332 ? 0.7076 0.3980 0.5587 -0.1144 0.1527  -0.0709 332 PHE A CB  
2563 C CG  . PHE A 332 ? 0.6656 0.3677 0.5376 -0.1179 0.1629  -0.0785 332 PHE A CG  
2564 C CD1 . PHE A 332 ? 0.6362 0.3604 0.5178 -0.1145 0.1540  -0.0809 332 PHE A CD1 
2565 C CD2 . PHE A 332 ? 0.6252 0.3160 0.5097 -0.1245 0.1818  -0.0832 332 PHE A CD2 
2566 C CE1 . PHE A 332 ? 0.6410 0.3762 0.5441 -0.1170 0.1624  -0.0880 332 PHE A CE1 
2567 C CE2 . PHE A 332 ? 0.7456 0.4482 0.6541 -0.1275 0.1912  -0.0908 332 PHE A CE2 
2568 C CZ  . PHE A 332 ? 0.7353 0.4604 0.6530 -0.1235 0.1807  -0.0932 332 PHE A CZ  
2569 N N   . PHE A 333 ? 0.6205 0.3282 0.4567 -0.0996 0.1129  -0.0599 333 PHE A N   
2570 C CA  . PHE A 333 ? 0.6547 0.3507 0.4763 -0.0958 0.1031  -0.0526 333 PHE A CA  
2571 C C   . PHE A 333 ? 0.6346 0.3064 0.4238 -0.0957 0.1007  -0.0435 333 PHE A C   
2572 O O   . PHE A 333 ? 0.6628 0.3387 0.4443 -0.0916 0.0882  -0.0390 333 PHE A O   
2573 C CB  . PHE A 333 ? 0.6697 0.3903 0.5063 -0.0895 0.0893  -0.0538 333 PHE A CB  
2574 C CG  . PHE A 333 ? 0.6167 0.3299 0.4487 -0.0852 0.0803  -0.0485 333 PHE A CG  
2575 C CD1 . PHE A 333 ? 0.6841 0.3916 0.5244 -0.0856 0.0837  -0.0511 333 PHE A CD1 
2576 C CD2 . PHE A 333 ? 0.6419 0.3547 0.4651 -0.0807 0.0681  -0.0417 333 PHE A CD2 
2577 C CE1 . PHE A 333 ? 0.6849 0.3859 0.5234 -0.0812 0.0754  -0.0464 333 PHE A CE1 
2578 C CE2 . PHE A 333 ? 0.6835 0.3906 0.5069 -0.0764 0.0593  -0.0373 333 PHE A CE2 
2579 C CZ  . PHE A 333 ? 0.6891 0.3903 0.5198 -0.0765 0.0630  -0.0395 333 PHE A CZ  
2580 N N   . GLY A 334 ? 0.6885 0.3335 0.4584 -0.1003 0.1135  -0.0410 334 GLY A N   
2581 C CA  . GLY A 334 ? 0.7269 0.3463 0.4622 -0.1008 0.1139  -0.0342 334 GLY A CA  
2582 C C   . GLY A 334 ? 0.7428 0.3336 0.4489 -0.0978 0.1062  -0.0250 334 GLY A C   
2583 O O   . GLY A 334 ? 0.7736 0.3571 0.4837 -0.0971 0.1069  -0.0234 334 GLY A O   
2584 N N   . VAL A 335 ? 0.7608 0.3346 0.4372 -0.0957 0.0977  -0.0193 335 VAL A N   
2585 C CA  . VAL A 335 ? 0.8374 0.3810 0.4819 -0.0920 0.0880  -0.0104 335 VAL A CA  
2586 C C   . VAL A 335 ? 0.8823 0.3916 0.5008 -0.0956 0.1051  -0.0067 335 VAL A C   
2587 O O   . VAL A 335 ? 0.8268 0.3254 0.4351 -0.1007 0.1228  -0.0090 335 VAL A O   
2588 C CB  . VAL A 335 ? 0.8535 0.3863 0.4720 -0.0890 0.0739  -0.0068 335 VAL A CB  
2589 C CG1 . VAL A 335 ? 0.8889 0.3900 0.4742 -0.0841 0.0605  0.0019  335 VAL A CG1 
2590 C CG2 . VAL A 335 ? 0.8515 0.4181 0.4991 -0.0860 0.0597  -0.0103 335 VAL A CG2 
2591 N N   . ALA A 336 ? 0.8578 0.3486 0.4663 -0.0928 0.1008  -0.0007 336 ALA A N   
2592 C CA  . ALA A 336 ? 0.9140 0.3707 0.4990 -0.0958 0.1179  0.0039  336 ALA A CA  
2593 C C   . ALA A 336 ? 0.9260 0.3401 0.4562 -0.0939 0.1173  0.0127  336 ALA A C   
2594 O O   . ALA A 336 ? 0.9113 0.3028 0.4197 -0.0987 0.1377  0.0131  336 ALA A O   
2595 C CB  . ALA A 336 ? 0.9454 0.3994 0.5439 -0.0934 0.1148  0.0067  336 ALA A CB  
2596 N N   . PRO A 337 ? 0.9303 0.3309 0.4365 -0.0869 0.0948  0.0192  337 PRO A N   
2597 C CA  . PRO A 337 ? 0.9634 0.3194 0.4125 -0.0844 0.0929  0.0272  337 PRO A CA  
2598 C C   . PRO A 337 ? 1.0418 0.3920 0.4709 -0.0881 0.1029  0.0234  337 PRO A C   
2599 O O   . PRO A 337 ? 1.0155 0.3968 0.4701 -0.0894 0.0977  0.0162  337 PRO A O   
2600 C CB  . PRO A 337 ? 0.9867 0.3405 0.4268 -0.0759 0.0620  0.0319  337 PRO A CB  
2601 C CG  . PRO A 337 ? 0.9699 0.3568 0.4581 -0.0741 0.0536  0.0292  337 PRO A CG  
2602 C CD  . PRO A 337 ? 0.9065 0.3295 0.4357 -0.0807 0.0699  0.0195  337 PRO A CD  
2603 N N   . GLY A 338 ? 1.0179 0.3259 0.3997 -0.0895 0.1181  0.0285  338 GLY A N   
2604 C CA  . GLY A 338 ? 1.0353 0.3322 0.3949 -0.0934 0.1323  0.0248  338 GLY A CA  
2605 C C   . GLY A 338 ? 1.1014 0.4076 0.4849 -0.1018 0.1635  0.0189  338 GLY A C   
2606 O O   . GLY A 338 ? 1.1587 0.4453 0.5174 -0.1052 0.1815  0.0174  338 GLY A O   
2607 N N   . THR A 339 ? 0.9953 0.3304 0.4271 -0.1050 0.1703  0.0147  339 THR A N   
2608 C CA  . THR A 339 ? 1.0062 0.3509 0.4662 -0.1129 0.1984  0.0082  339 THR A CA  
2609 C C   . THR A 339 ? 1.1449 0.4458 0.5727 -0.1158 0.2227  0.0150  339 THR A C   
2610 O O   . THR A 339 ? 1.1082 0.3953 0.5321 -0.1138 0.2213  0.0211  339 THR A O   
2611 C CB  . THR A 339 ? 0.9772 0.3643 0.4968 -0.1148 0.1954  0.0010  339 THR A CB  
2612 O OG1 . THR A 339 ? 0.9855 0.4085 0.5287 -0.1109 0.1721  -0.0033 339 THR A OG1 
2613 C CG2 . THR A 339 ? 0.9842 0.3871 0.5393 -0.1226 0.2202  -0.0081 339 THR A CG2 
2614 N N   . SER A 340 ? 1.1340 0.4195 0.5435 -0.1185 0.2441  0.0125  340 SER A N   
2615 C CA  . SER A 340 ? 1.2190 0.4792 0.6095 -0.1175 0.2663  0.0142  340 SER A CA  
2616 C C   . SER A 340 ? 1.2345 0.5092 0.6551 -0.1235 0.2938  0.0041  340 SER A C   
2617 O O   . SER A 340 ? 1.2077 0.5128 0.6642 -0.1281 0.2941  -0.0038 340 SER A O   
2618 C CB  . SER A 340 ? 1.2245 0.4409 0.5479 -0.1106 0.2607  0.0216  340 SER A CB  
2619 O OG  . SER A 340 ? 1.3430 0.5529 0.6448 -0.1110 0.2629  0.0173  340 SER A OG  
2620 N N   . VAL A 341 ? 1.2541 0.5060 0.6611 -0.1230 0.3170  0.0042  341 VAL A N   
2621 C CA  . VAL A 341 ? 1.3325 0.5941 0.7676 -0.1278 0.3443  -0.0054 341 VAL A CA  
2622 C C   . VAL A 341 ? 1.3080 0.5582 0.7170 -0.1273 0.3482  -0.0091 341 VAL A C   
2623 O O   . VAL A 341 ? 1.3187 0.5869 0.7601 -0.1315 0.3646  -0.0185 341 VAL A O   
2624 C CB  . VAL A 341 ? 1.3709 0.6086 0.7996 -0.1271 0.3686  -0.0040 341 VAL A CB  
2625 C CG1 . VAL A 341 ? 1.3322 0.5863 0.8049 -0.1324 0.3966  -0.0150 341 VAL A CG1 
2626 C CG2 . VAL A 341 ? 1.3810 0.6231 0.8253 -0.1265 0.3615  0.0016  341 VAL A CG2 
2627 N N   . LYS A 342 ? 1.3024 0.5233 0.6550 -0.1218 0.3325  -0.0026 342 LYS A N   
2628 C CA  . LYS A 342 ? 1.3344 0.5417 0.6601 -0.1211 0.3352  -0.0066 342 LYS A CA  
2629 C C   . LYS A 342 ? 1.3190 0.5528 0.6581 -0.1228 0.3148  -0.0088 342 LYS A C   
2630 O O   . LYS A 342 ? 1.3554 0.5939 0.6977 -0.1249 0.3218  -0.0153 342 LYS A O   
2631 C CB  . LYS A 342 ? 1.4636 0.6219 0.7199 -0.1140 0.3294  0.0002  342 LYS A CB  
2632 C CG  . LYS A 342 ? 1.5590 0.7077 0.7817 -0.1084 0.2965  0.0091  342 LYS A CG  
2633 C CD  . LYS A 342 ? 1.6849 0.7852 0.8401 -0.1009 0.2897  0.0143  342 LYS A CD  
2634 C CE  . LYS A 342 ? 1.8040 0.8971 0.9292 -0.0948 0.2537  0.0214  342 LYS A CE  
2635 N NZ  . LYS A 342 ? 1.7464 0.8637 0.8844 -0.0968 0.2355  0.0174  342 LYS A NZ  
2636 N N   . THR A 343 ? 1.2533 0.5038 0.6018 -0.1220 0.2904  -0.0037 343 THR A N   
2637 C CA  . THR A 343 ? 1.2379 0.5128 0.6008 -0.1236 0.2710  -0.0051 343 THR A CA  
2638 C C   . THR A 343 ? 1.1369 0.4565 0.5658 -0.1298 0.2746  -0.0123 343 THR A C   
2639 O O   . THR A 343 ? 1.1752 0.5250 0.6291 -0.1295 0.2654  -0.0193 343 THR A O   
2640 C CB  . THR A 343 ? 1.2112 0.4793 0.5502 -0.1181 0.2395  0.0034  343 THR A CB  
2641 O OG1 . THR A 343 ? 1.2108 0.4936 0.5791 -0.1178 0.2338  0.0062  343 THR A OG1 
2642 C CG2 . THR A 343 ? 1.2784 0.5011 0.5511 -0.1113 0.2317  0.0101  343 THR A CG2 
2643 N N   . ASN A 344 ? 1.1225 0.4561 0.5867 -0.1319 0.2828  -0.0136 344 ASN A N   
2644 C CA  . ASN A 344 ? 1.0693 0.4471 0.5974 -0.1362 0.2830  -0.0225 344 ASN A CA  
2645 C C   . ASN A 344 ? 1.0882 0.4715 0.6486 -0.1394 0.3024  -0.0258 344 ASN A C   
2646 O O   . ASN A 344 ? 1.0508 0.4472 0.6350 -0.1396 0.2937  -0.0252 344 ASN A O   
2647 C CB  . ASN A 344 ? 1.0598 0.4704 0.6091 -0.1307 0.2514  -0.0227 344 ASN A CB  
2648 C CG  . ASN A 344 ? 0.9316 0.3907 0.5380 -0.1320 0.2457  -0.0331 344 ASN A CG  
2649 O OD1 . ASN A 344 ? 0.9197 0.3914 0.5592 -0.1373 0.2642  -0.0407 344 ASN A OD1 
2650 N ND2 . ASN A 344 ? 0.9819 0.4679 0.6007 -0.1269 0.2200  -0.0335 344 ASN A ND2 
2651 N N   . PRO A 345 ? 1.1147 0.4900 0.6793 -0.1410 0.3280  -0.0306 345 PRO A N   
2652 C CA  . PRO A 345 ? 1.0688 0.4510 0.6675 -0.1433 0.3459  -0.0345 345 PRO A CA  
2653 C C   . PRO A 345 ? 0.9836 0.4091 0.6487 -0.1478 0.3429  -0.0442 345 PRO A C   
2654 O O   . PRO A 345 ? 0.9887 0.4232 0.6833 -0.1492 0.3481  -0.0465 345 PRO A O   
2655 C CB  . PRO A 345 ? 1.0700 0.4333 0.6586 -0.1436 0.3734  -0.0385 345 PRO A CB  
2656 C CG  . PRO A 345 ? 1.1365 0.5021 0.7128 -0.1437 0.3698  -0.0416 345 PRO A CG  
2657 C CD  . PRO A 345 ? 1.1110 0.4701 0.6521 -0.1407 0.3421  -0.0334 345 PRO A CD  
2658 N N   . ASN A 346 ? 0.9474 0.3992 0.6367 -0.1496 0.3338  -0.0505 346 ASN A N   
2659 C CA  . ASN A 346 ? 0.9294 0.4214 0.6796 -0.1528 0.3279  -0.0607 346 ASN A CA  
2660 C C   . ASN A 346 ? 0.9653 0.4676 0.7227 -0.1516 0.3060  -0.0586 346 ASN A C   
2661 O O   . ASN A 346 ? 0.9131 0.4399 0.7149 -0.1534 0.3039  -0.0662 346 ASN A O   
2662 C CB  . ASN A 346 ? 0.8718 0.3866 0.6430 -0.1540 0.3231  -0.0678 346 ASN A CB  
2663 C CG  . ASN A 346 ? 0.9884 0.4987 0.7660 -0.1554 0.3465  -0.0727 346 ASN A CG  
2664 O OD1 . ASN A 346 ? 0.9398 0.4383 0.6907 -0.1545 0.3484  -0.0709 346 ASN A OD1 
2665 N ND2 . ASN A 346 ? 0.8355 0.3544 0.6498 -0.1574 0.3647  -0.0795 346 ASN A ND2 
2666 N N   . ALA A 347 ? 0.9485 0.4377 0.6653 -0.1461 0.2871  -0.0494 347 ALA A N   
2667 C CA  . ALA A 347 ? 0.9392 0.4421 0.6628 -0.1417 0.2655  -0.0473 347 ALA A CA  
2668 C C   . ALA A 347 ? 0.9567 0.4353 0.6749 -0.1441 0.2766  -0.0428 347 ALA A C   
2669 O O   . ALA A 347 ? 0.9299 0.4260 0.6755 -0.1433 0.2673  -0.0461 347 ALA A O   
2670 C CB  . ALA A 347 ? 0.8525 0.3497 0.5386 -0.1345 0.2421  -0.0391 347 ALA A CB  
2671 N N   . ILE A 348 ? 1.0617 0.5059 0.7458 -0.1444 0.2946  -0.0358 348 ILE A N   
2672 C CA  . ILE A 348 ? 0.9385 0.3662 0.6191 -0.1436 0.3042  -0.0316 348 ILE A CA  
2673 C C   . ILE A 348 ? 1.0017 0.4556 0.7397 -0.1481 0.3170  -0.0425 348 ILE A C   
2674 O O   . ILE A 348 ? 1.0004 0.4586 0.7573 -0.1483 0.3141  -0.0431 348 ILE A O   
2675 C CB  . ILE A 348 ? 1.0207 0.4093 0.6528 -0.1410 0.3208  -0.0235 348 ILE A CB  
2676 C CG1 . ILE A 348 ? 1.0748 0.4362 0.6487 -0.1356 0.3040  -0.0131 348 ILE A CG1 
2677 C CG2 . ILE A 348 ? 1.0838 0.4553 0.7153 -0.1403 0.3332  -0.0196 348 ILE A CG2 
2678 C CD1 . ILE A 348 ? 1.0430 0.3971 0.6026 -0.1314 0.2815  -0.0050 348 ILE A CD1 
2679 N N   . LYS A 349 ? 0.9247 0.3967 0.6928 -0.1516 0.3303  -0.0519 349 LYS A N   
2680 C CA  . LYS A 349 ? 0.9017 0.4005 0.7280 -0.1556 0.3404  -0.0636 349 LYS A CA  
2681 C C   . LYS A 349 ? 0.9630 0.4951 0.8291 -0.1564 0.3198  -0.0720 349 LYS A C   
2682 O O   . LYS A 349 ? 0.9409 0.4906 0.8491 -0.1586 0.3225  -0.0802 349 LYS A O   
2683 C CB  . LYS A 349 ? 0.8922 0.4025 0.7421 -0.1581 0.3576  -0.0718 349 LYS A CB  
2684 C CG  . LYS A 349 ? 1.0961 0.5729 0.9089 -0.1569 0.3806  -0.0661 349 LYS A CG  
2685 C CD  . LYS A 349 ? 1.1608 0.6503 1.0033 -0.1591 0.3984  -0.0758 349 LYS A CD  
2686 C CE  . LYS A 349 ? 1.2006 0.6538 1.0028 -0.1572 0.4216  -0.0712 349 LYS A CE  
2687 N NZ  . LYS A 349 ? 1.3059 0.7704 1.1402 -0.1589 0.4404  -0.0815 349 LYS A NZ  
2688 N N   . THR A 350 ? 0.9431 0.4832 0.7961 -0.1544 0.2993  -0.0708 350 THR A N   
2689 C CA  . THR A 350 ? 0.8911 0.4622 0.7787 -0.1541 0.2800  -0.0801 350 THR A CA  
2690 C C   . THR A 350 ? 0.8261 0.3939 0.7089 -0.1510 0.2674  -0.0767 350 THR A C   
2691 O O   . THR A 350 ? 0.8050 0.3957 0.7252 -0.1514 0.2605  -0.0864 350 THR A O   
2692 C CB  . THR A 350 ? 0.8755 0.4680 0.7522 -0.1479 0.2598  -0.0795 350 THR A CB  
2693 O OG1 . THR A 350 ? 0.8757 0.4701 0.7571 -0.1506 0.2718  -0.0827 350 THR A OG1 
2694 C CG2 . THR A 350 ? 0.8197 0.4515 0.7313 -0.1439 0.2388  -0.0888 350 THR A CG2 
2695 N N   . ILE A 351 ? 0.8644 0.4034 0.7018 -0.1474 0.2638  -0.0637 351 ILE A N   
2696 C CA  . ILE A 351 ? 0.8691 0.4060 0.7002 -0.1429 0.2489  -0.0595 351 ILE A CA  
2697 C C   . ILE A 351 ? 0.9505 0.4663 0.7890 -0.1468 0.2651  -0.0582 351 ILE A C   
2698 O O   . ILE A 351 ? 0.9331 0.4358 0.7599 -0.1438 0.2576  -0.0525 351 ILE A O   
2699 C CB  . ILE A 351 ? 0.8084 0.3270 0.5913 -0.1359 0.2339  -0.0465 351 ILE A CB  
2700 C CG1 . ILE A 351 ? 0.8803 0.3551 0.6182 -0.1378 0.2505  -0.0355 351 ILE A CG1 
2701 C CG2 . ILE A 351 ? 0.8151 0.3598 0.5971 -0.1313 0.2161  -0.0486 351 ILE A CG2 
2702 C CD1 . ILE A 351 ? 0.9033 0.3576 0.5926 -0.1308 0.2342  -0.0235 351 ILE A CD1 
2703 N N   . GLN A 352 ? 1.0680 0.5881 0.9294 -0.1507 0.2850  -0.0632 352 GLN A N   
2704 C CA  . GLN A 352 ? 1.0372 0.5459 0.9097 -0.1520 0.2998  -0.0621 352 GLN A CA  
2705 C C   . GLN A 352 ? 1.0341 0.5647 0.9486 -0.1529 0.2909  -0.0720 352 GLN A C   
2706 O O   . GLN A 352 ? 1.0332 0.5512 0.9512 -0.1528 0.2976  -0.0691 352 GLN A O   
2707 C CB  . GLN A 352 ? 1.1065 0.6160 0.9973 -0.1558 0.3241  -0.0666 352 GLN A CB  
2708 C CG  . GLN A 352 ? 1.2105 0.6924 1.0568 -0.1544 0.3377  -0.0573 352 GLN A CG  
2709 C CD  . GLN A 352 ? 1.2986 0.7406 1.0961 -0.1507 0.3437  -0.0432 352 GLN A CD  
2710 O OE1 . GLN A 352 ? 1.3786 0.8134 1.1831 -0.1502 0.3446  -0.0408 352 GLN A OE1 
2711 N NE2 . GLN A 352 ? 1.3176 0.7328 1.0648 -0.1477 0.3470  -0.0342 352 GLN A NE2 
2712 N N   . LYS A 353 ? 0.8853 0.4472 0.8307 -0.1534 0.2760  -0.0839 353 LYS A N   
2713 C CA  . LYS A 353 ? 0.8315 0.4149 0.8169 -0.1539 0.2675  -0.0955 353 LYS A CA  
2714 C C   . LYS A 353 ? 0.8531 0.4604 0.8481 -0.1514 0.2456  -0.1041 353 LYS A C   
2715 O O   . LYS A 353 ? 0.7963 0.4152 0.7807 -0.1492 0.2382  -0.1035 353 LYS A O   
2716 C CB  . LYS A 353 ? 0.8425 0.4445 0.8755 -0.1584 0.2807  -0.1073 353 LYS A CB  
2717 C CG  . LYS A 353 ? 0.8083 0.4329 0.8639 -0.1604 0.2821  -0.1161 353 LYS A CG  
2718 C CD  . LYS A 353 ? 0.8515 0.4932 0.9569 -0.1642 0.2947  -0.1277 353 LYS A CD  
2719 C CE  . LYS A 353 ? 0.8855 0.5493 1.0160 -0.1655 0.2959  -0.1364 353 LYS A CE  
2720 N NZ  . LYS A 353 ? 1.0565 0.7363 1.2379 -0.1686 0.3083  -0.1478 353 LYS A NZ  
2721 N N   . ASN A 354 ? 0.8061 0.4244 0.8201 -0.1497 0.2342  -0.1115 354 ASN A N   
2722 C CA  . ASN A 354 ? 0.6968 0.3477 0.7215 -0.1431 0.2111  -0.1195 354 ASN A CA  
2723 C C   . ASN A 354 ? 0.6947 0.3466 0.6817 -0.1355 0.1967  -0.1079 354 ASN A C   
2724 O O   . ASN A 354 ? 0.7419 0.4192 0.7322 -0.1309 0.1825  -0.1119 354 ASN A O   
2725 C CB  . ASN A 354 ? 0.6608 0.3415 0.7219 -0.1452 0.2084  -0.1343 354 ASN A CB  
2726 C CG  . ASN A 354 ? 0.6590 0.3432 0.7630 -0.1519 0.2202  -0.1466 354 ASN A CG  
2727 O OD1 . ASN A 354 ? 0.7459 0.4257 0.8603 -0.1518 0.2207  -0.1485 354 ASN A OD1 
2728 N ND2 . ASN A 354 ? 0.7123 0.4111 0.8421 -0.1549 0.2273  -0.1530 354 ASN A ND2 
2729 N N   . THR A 355 ? 0.6956 0.3188 0.6472 -0.1339 0.1998  -0.0935 355 THR A N   
2730 C CA  . THR A 355 ? 0.7778 0.3970 0.6935 -0.1277 0.1880  -0.0821 355 THR A CA  
2731 C C   . THR A 355 ? 0.7473 0.3570 0.6465 -0.1215 0.1758  -0.0745 355 THR A C   
2732 O O   . THR A 355 ? 0.7116 0.2987 0.6072 -0.1229 0.1831  -0.0707 355 THR A O   
2733 C CB  . THR A 355 ? 0.7594 0.3504 0.6436 -0.1308 0.2016  -0.0715 355 THR A CB  
2734 O OG1 . THR A 355 ? 0.7602 0.3614 0.6635 -0.1364 0.2138  -0.0792 355 THR A OG1 
2735 C CG2 . THR A 355 ? 0.6938 0.2803 0.5420 -0.1245 0.1876  -0.0609 355 THR A CG2 
2736 N N   . ILE A 356 ? 0.6864 0.3132 0.5777 -0.1146 0.1579  -0.0724 356 ILE A N   
2737 C CA  . ILE A 356 ? 0.7457 0.3663 0.6244 -0.1079 0.1451  -0.0654 356 ILE A CA  
2738 C C   . ILE A 356 ? 0.6707 0.2733 0.5129 -0.1044 0.1389  -0.0519 356 ILE A C   
2739 O O   . ILE A 356 ? 0.6923 0.3074 0.5271 -0.1030 0.1327  -0.0511 356 ILE A O   
2740 C CB  . ILE A 356 ? 0.6959 0.3476 0.5946 -0.1023 0.1304  -0.0733 356 ILE A CB  
2741 C CG1 . ILE A 356 ? 0.6821 0.3497 0.6141 -0.1052 0.1348  -0.0880 356 ILE A CG1 
2742 C CG2 . ILE A 356 ? 0.6439 0.2890 0.5327 -0.0953 0.1188  -0.0661 356 ILE A CG2 
2743 C CD1 . ILE A 356 ? 0.6926 0.3853 0.6394 -0.0991 0.1218  -0.0959 356 ILE A CD1 
2744 N N   . PHE A 357 ? 0.7136 0.2861 0.5331 -0.1028 0.1396  -0.0415 357 PHE A N   
2745 C CA  . PHE A 357 ? 0.7445 0.2968 0.5280 -0.0985 0.1304  -0.0290 357 PHE A CA  
2746 C C   . PHE A 357 ? 0.7391 0.2977 0.5248 -0.0904 0.1117  -0.0252 357 PHE A C   
2747 O O   . PHE A 357 ? 0.7796 0.3446 0.5861 -0.0887 0.1103  -0.0291 357 PHE A O   
2748 C CB  . PHE A 357 ? 0.7741 0.2845 0.5258 -0.1009 0.1426  -0.0190 357 PHE A CB  
2749 C CG  . PHE A 357 ? 0.7989 0.2993 0.5478 -0.1089 0.1639  -0.0219 357 PHE A CG  
2750 C CD1 . PHE A 357 ? 0.7746 0.2773 0.5512 -0.1153 0.1809  -0.0298 357 PHE A CD1 
2751 C CD2 . PHE A 357 ? 0.8701 0.3586 0.5908 -0.1101 0.1675  -0.0174 357 PHE A CD2 
2752 C CE1 . PHE A 357 ? 0.8185 0.3126 0.5975 -0.1228 0.2016  -0.0330 357 PHE A CE1 
2753 C CE2 . PHE A 357 ? 0.8110 0.2899 0.5310 -0.1173 0.1890  -0.0203 357 PHE A CE2 
2754 C CZ  . PHE A 357 ? 0.8002 0.2823 0.5508 -0.1237 0.2064  -0.0280 357 PHE A CZ  
2755 N N   . THR A 358 ? 0.7652 0.3219 0.5314 -0.0856 0.0977  -0.0181 358 THR A N   
2756 C CA  . THR A 358 ? 0.8044 0.3682 0.5761 -0.0779 0.0797  -0.0145 358 THR A CA  
2757 C C   . THR A 358 ? 0.7869 0.3227 0.5242 -0.0737 0.0684  -0.0024 358 THR A C   
2758 O O   . THR A 358 ? 0.8451 0.3766 0.5619 -0.0745 0.0655  0.0002  358 THR A O   
2759 C CB  . THR A 358 ? 0.7957 0.3954 0.5897 -0.0754 0.0706  -0.0211 358 THR A CB  
2760 O OG1 . THR A 358 ? 0.7389 0.3623 0.5616 -0.0781 0.0789  -0.0325 358 THR A OG1 
2761 C CG2 . THR A 358 ? 0.7215 0.3273 0.5235 -0.0676 0.0539  -0.0171 358 THR A CG2 
2762 N N   . ASN A 359 ? 0.8416 0.3577 0.5725 -0.0689 0.0613  0.0044  359 ASN A N   
2763 C CA  . ASN A 359 ? 0.9147 0.4044 0.6154 -0.0629 0.0458  0.0156  359 ASN A CA  
2764 C C   . ASN A 359 ? 0.9275 0.3815 0.5838 -0.0659 0.0539  0.0228  359 ASN A C   
2765 O O   . ASN A 359 ? 1.0508 0.4875 0.6773 -0.0621 0.0407  0.0296  359 ASN A O   
2766 C CB  . ASN A 359 ? 0.8973 0.4077 0.6066 -0.0580 0.0267  0.0152  359 ASN A CB  
2767 C CG  . ASN A 359 ? 0.8387 0.3767 0.5870 -0.0533 0.0182  0.0106  359 ASN A CG  
2768 O OD1 . ASN A 359 ? 0.8714 0.4057 0.6337 -0.0516 0.0212  0.0101  359 ASN A OD1 
2769 N ND2 . ASN A 359 ? 0.8059 0.3703 0.5717 -0.0513 0.0089  0.0071  359 ASN A ND2 
2770 N N   . VAL A 360 ? 0.9775 0.4192 0.6290 -0.0727 0.0757  0.0210  360 VAL A N   
2771 C CA  . VAL A 360 ? 0.9501 0.3519 0.5581 -0.0751 0.0872  0.0290  360 VAL A CA  
2772 C C   . VAL A 360 ? 1.0220 0.3913 0.6169 -0.0729 0.0918  0.0372  360 VAL A C   
2773 O O   . VAL A 360 ? 0.9718 0.3528 0.5972 -0.0718 0.0915  0.0341  360 VAL A O   
2774 C CB  . VAL A 360 ? 0.9696 0.3754 0.5804 -0.0843 0.1110  0.0225  360 VAL A CB  
2775 C CG1 . VAL A 360 ? 0.9031 0.3432 0.5314 -0.0861 0.1063  0.0140  360 VAL A CG1 
2776 C CG2 . VAL A 360 ? 0.8704 0.2841 0.5132 -0.0899 0.1290  0.0159  360 VAL A CG2 
2777 N N   . ALA A 361 ? 1.0721 0.3980 0.6194 -0.0719 0.0966  0.0479  361 ALA A N   
2778 C CA  . ALA A 361 ? 1.1067 0.3961 0.6353 -0.0690 0.1013  0.0576  361 ALA A CA  
2779 C C   . ALA A 361 ? 1.0165 0.3003 0.5613 -0.0775 0.1301  0.0538  361 ALA A C   
2780 O O   . ALA A 361 ? 1.0045 0.2986 0.5576 -0.0855 0.1486  0.0468  361 ALA A O   
2781 C CB  . ALA A 361 ? 1.1570 0.3982 0.6238 -0.0641 0.0963  0.0710  361 ALA A CB  
2782 N N   . GLU A 362 ? 1.0640 0.3315 0.6160 -0.0756 0.1336  0.0583  362 GLU A N   
2783 C CA  . GLU A 362 ? 1.0454 0.3077 0.6164 -0.0828 0.1594  0.0549  362 GLU A CA  
2784 C C   . GLU A 362 ? 1.0997 0.3263 0.6336 -0.0792 0.1687  0.0669  362 GLU A C   
2785 O O   . GLU A 362 ? 1.1670 0.3689 0.6718 -0.0704 0.1525  0.0782  362 GLU A O   
2786 C CB  . GLU A 362 ? 1.0582 0.3411 0.6759 -0.0828 0.1567  0.0475  362 GLU A CB  
2787 C CG  . GLU A 362 ? 1.0506 0.3363 0.6960 -0.0893 0.1802  0.0421  362 GLU A CG  
2788 C CD  . GLU A 362 ? 1.1047 0.4064 0.7927 -0.0889 0.1765  0.0344  362 GLU A CD  
2789 O OE1 . GLU A 362 ? 1.1134 0.4303 0.8118 -0.0824 0.1556  0.0331  362 GLU A OE1 
2790 O OE2 . GLU A 362 ? 1.0638 0.3716 0.7793 -0.0938 0.1927  0.0285  362 GLU A OE2 
2791 N N   . THR A 363 ? 1.1110 0.3351 0.6468 -0.0856 0.1944  0.0642  363 THR A N   
2792 C CA  . THR A 363 ? 1.1560 0.3466 0.6600 -0.0830 0.2074  0.0744  363 THR A CA  
2793 C C   . THR A 363 ? 1.1817 0.3740 0.7193 -0.0847 0.2183  0.0732  363 THR A C   
2794 O O   . THR A 363 ? 1.1142 0.3361 0.7016 -0.0904 0.2225  0.0616  363 THR A O   
2795 C CB  . THR A 363 ? 1.1759 0.3588 0.6609 -0.0882 0.2308  0.0725  363 THR A CB  
2796 O OG1 . THR A 363 ? 1.1425 0.3537 0.6761 -0.0977 0.2513  0.0598  363 THR A OG1 
2797 C CG2 . THR A 363 ? 1.1920 0.3750 0.6471 -0.0869 0.2204  0.0721  363 THR A CG2 
2798 N N   . SER A 364 ? 1.2038 0.3632 0.7127 -0.0796 0.2224  0.0849  364 SER A N   
2799 C CA  . SER A 364 ? 1.2087 0.3653 0.7457 -0.0802 0.2306  0.0855  364 SER A CA  
2800 C C   . SER A 364 ? 1.1917 0.3668 0.7691 -0.0903 0.2576  0.0744  364 SER A C   
2801 O O   . SER A 364 ? 1.1776 0.3635 0.7941 -0.0928 0.2622  0.0694  364 SER A O   
2802 C CB  . SER A 364 ? 1.2692 0.3843 0.7632 -0.0725 0.2306  0.1011  364 SER A CB  
2803 O OG  . SER A 364 ? 1.3099 0.4020 0.7641 -0.0735 0.2483  0.1055  364 SER A OG  
2804 N N   . ASP A 365 ? 1.1935 0.3727 0.7642 -0.0959 0.2750  0.0696  365 ASP A N   
2805 C CA  . ASP A 365 ? 1.1759 0.3752 0.7888 -0.1052 0.2994  0.0579  365 ASP A CA  
2806 C C   . ASP A 365 ? 1.1552 0.3978 0.8157 -0.1114 0.2940  0.0419  365 ASP A C   
2807 O O   . ASP A 365 ? 1.1565 0.4194 0.8524 -0.1188 0.3115  0.0306  365 ASP A O   
2808 C CB  . ASP A 365 ? 1.2109 0.3921 0.7961 -0.1076 0.3228  0.0602  365 ASP A CB  
2809 C CG  . ASP A 365 ? 1.2986 0.4819 0.8543 -0.1068 0.3163  0.0595  365 ASP A CG  
2810 O OD1 . ASP A 365 ? 1.2769 0.4712 0.8270 -0.1035 0.2922  0.0596  365 ASP A OD1 
2811 O OD2 . ASP A 365 ? 1.3193 0.4928 0.8585 -0.1093 0.3360  0.0583  365 ASP A OD2 
2812 N N   . GLY A 366 ? 1.1425 0.3990 0.8050 -0.1080 0.2700  0.0403  366 GLY A N   
2813 C CA  . GLY A 366 ? 1.0668 0.3626 0.7726 -0.1128 0.2635  0.0252  366 GLY A CA  
2814 C C   . GLY A 366 ? 1.1258 0.4364 0.8241 -0.1158 0.2630  0.0201  366 GLY A C   
2815 O O   . GLY A 366 ? 1.1325 0.4762 0.8699 -0.1212 0.2636  0.0063  366 GLY A O   
2816 N N   . GLY A 367 ? 1.1079 0.3950 0.7572 -0.1121 0.2612  0.0304  367 GLY A N   
2817 C CA  . GLY A 367 ? 1.0311 0.3292 0.6697 -0.1143 0.2600  0.0265  367 GLY A CA  
2818 C C   . GLY A 367 ? 1.0456 0.3413 0.6583 -0.1084 0.2343  0.0315  367 GLY A C   
2819 O O   . GLY A 367 ? 1.0683 0.3557 0.6745 -0.1023 0.2165  0.0374  367 GLY A O   
2820 N N   . VAL A 368 ? 1.0184 0.3215 0.6182 -0.1101 0.2327  0.0288  368 VAL A N   
2821 C CA  . VAL A 368 ? 1.0819 0.3852 0.6601 -0.1055 0.2092  0.0321  368 VAL A CA  
2822 C C   . VAL A 368 ? 1.0724 0.3431 0.5929 -0.1007 0.2068  0.0429  368 VAL A C   
2823 O O   . VAL A 368 ? 1.0786 0.3320 0.5783 -0.1024 0.2263  0.0451  368 VAL A O   
2824 C CB  . VAL A 368 ? 0.9644 0.3029 0.5730 -0.1105 0.2057  0.0199  368 VAL A CB  
2825 C CG1 . VAL A 368 ? 0.9106 0.2872 0.5748 -0.1123 0.2022  0.0078  368 VAL A CG1 
2826 C CG2 . VAL A 368 ? 0.9577 0.3008 0.5666 -0.1166 0.2261  0.0148  368 VAL A CG2 
2827 N N   . TYR A 369 ? 1.0635 0.3257 0.5582 -0.0943 0.1822  0.0489  369 TYR A N   
2828 C CA  . TYR A 369 ? 1.1518 0.3835 0.5905 -0.0888 0.1749  0.0579  369 TYR A CA  
2829 C C   . TYR A 369 ? 1.0779 0.3182 0.5080 -0.0843 0.1473  0.0584  369 TYR A C   
2830 O O   . TYR A 369 ? 1.0879 0.3564 0.5504 -0.0801 0.1278  0.0552  369 TYR A O   
2831 C CB  . TYR A 369 ? 1.1452 0.3414 0.5486 -0.0814 0.1719  0.0698  369 TYR A CB  
2832 C CG  . TYR A 369 ? 1.2008 0.3633 0.5492 -0.0785 0.1802  0.0758  369 TYR A CG  
2833 C CD1 . TYR A 369 ? 1.2582 0.4126 0.6038 -0.0835 0.2102  0.0731  369 TYR A CD1 
2834 C CD2 . TYR A 369 ? 1.2327 0.3709 0.5332 -0.0702 0.1579  0.0831  369 TYR A CD2 
2835 C CE1 . TYR A 369 ? 1.2833 0.4048 0.5776 -0.0804 0.2193  0.0774  369 TYR A CE1 
2836 C CE2 . TYR A 369 ? 1.3218 0.4273 0.5698 -0.0671 0.1652  0.0870  369 TYR A CE2 
2837 C CZ  . TYR A 369 ? 1.3292 0.4257 0.5733 -0.0722 0.1968  0.0841  369 TYR A CZ  
2838 O OH  . TYR A 369 ? 1.4907 0.5525 0.6819 -0.0688 0.2056  0.0870  369 TYR A OH  
2839 N N   . TRP A 370 ? 1.0977 0.3246 0.4915 -0.0836 0.1445  0.0599  370 TRP A N   
2840 C CA  . TRP A 370 ? 1.2543 0.4987 0.6446 -0.0778 0.1166  0.0581  370 TRP A CA  
2841 C C   . TRP A 370 ? 1.2652 0.4730 0.5962 -0.0756 0.1151  0.0638  370 TRP A C   
2842 O O   . TRP A 370 ? 1.2236 0.4067 0.5262 -0.0784 0.1375  0.0655  370 TRP A O   
2843 C CB  . TRP A 370 ? 1.0183 0.3151 0.4589 -0.0820 0.1145  0.0452  370 TRP A CB  
2844 C CG  . TRP A 370 ? 1.0077 0.3131 0.4587 -0.0909 0.1405  0.0378  370 TRP A CG  
2845 C CD1 . TRP A 370 ? 1.0649 0.3537 0.4846 -0.0935 0.1505  0.0376  370 TRP A CD1 
2846 C CD2 . TRP A 370 ? 0.9809 0.3138 0.4788 -0.0981 0.1588  0.0287  370 TRP A CD2 
2847 N NE1 . TRP A 370 ? 1.0103 0.3153 0.4569 -0.1018 0.1748  0.0293  370 TRP A NE1 
2848 C CE2 . TRP A 370 ? 0.9956 0.3279 0.4907 -0.1047 0.1794  0.0236  370 TRP A CE2 
2849 C CE3 . TRP A 370 ? 0.9415 0.2987 0.4837 -0.0992 0.1594  0.0236  370 TRP A CE3 
2850 C CZ2 . TRP A 370 ? 0.9465 0.3028 0.4841 -0.1122 0.1988  0.0137  370 TRP A CZ2 
2851 C CZ3 . TRP A 370 ? 0.9146 0.2946 0.4958 -0.1068 0.1781  0.0134  370 TRP A CZ3 
2852 C CH2 . TRP A 370 ? 0.9168 0.2968 0.4967 -0.1131 0.1968  0.0086  370 TRP A CH2 
2853 N N   . GLU A 371 ? 1.2435 0.4572 0.5632 -0.0693 0.0876  0.0638  371 GLU A N   
2854 C CA  . GLU A 371 ? 1.2752 0.4556 0.5386 -0.0663 0.0818  0.0676  371 GLU A CA  
2855 C C   . GLU A 371 ? 1.2140 0.4026 0.4773 -0.0743 0.1040  0.0599  371 GLU A C   
2856 O O   . GLU A 371 ? 1.1245 0.3570 0.4355 -0.0790 0.1064  0.0498  371 GLU A O   
2857 C CB  . GLU A 371 ? 1.1890 0.3805 0.4513 -0.0586 0.0462  0.0669  371 GLU A CB  
2858 C CG  . GLU A 371 ? 1.2859 0.4521 0.5270 -0.0487 0.0218  0.0767  371 GLU A CG  
2859 C CD  . GLU A 371 ? 1.3026 0.4896 0.5890 -0.0478 0.0210  0.0778  371 GLU A CD  
2860 O OE1 . GLU A 371 ? 1.1591 0.3904 0.5008 -0.0530 0.0287  0.0690  371 GLU A OE1 
2861 O OE2 . GLU A 371 ? 1.3680 0.5254 0.6329 -0.0413 0.0125  0.0875  371 GLU A OE2 
2862 N N   . GLY A 372 ? 1.2398 0.3923 0.4550 -0.0746 0.1201  0.0626  372 GLY A N   
2863 C CA  . GLY A 372 ? 1.2092 0.3674 0.4236 -0.0811 0.1421  0.0548  372 GLY A CA  
2864 C C   . GLY A 372 ? 1.2207 0.3956 0.4715 -0.0890 0.1746  0.0491  372 GLY A C   
2865 O O   . GLY A 372 ? 1.2900 0.4772 0.5530 -0.0950 0.1924  0.0413  372 GLY A O   
2866 N N   . ILE A 373 ? 1.2088 0.3853 0.4798 -0.0891 0.1824  0.0521  373 ILE A N   
2867 C CA  . ILE A 373 ? 1.2361 0.4285 0.5445 -0.0963 0.2120  0.0459  373 ILE A CA  
2868 C C   . ILE A 373 ? 1.2933 0.4580 0.5705 -0.0965 0.2375  0.0453  373 ILE A C   
2869 O O   . ILE A 373 ? 1.2641 0.4423 0.5710 -0.1028 0.2635  0.0380  373 ILE A O   
2870 C CB  . ILE A 373 ? 1.2018 0.4029 0.5413 -0.0962 0.2116  0.0489  373 ILE A CB  
2871 C CG1 . ILE A 373 ? 1.1351 0.3640 0.5279 -0.1046 0.2363  0.0397  373 ILE A CG1 
2872 C CG2 . ILE A 373 ? 1.2558 0.4192 0.5552 -0.0893 0.2120  0.0589  373 ILE A CG2 
2873 C CD1 . ILE A 373 ? 1.2432 0.4822 0.6697 -0.1050 0.2362  0.0408  373 ILE A CD1 
2874 N N   . ASP A 374 ? 1.3161 0.4416 0.5354 -0.0892 0.2300  0.0521  374 ASP A N   
2875 C CA  . ASP A 374 ? 1.3873 0.4813 0.5695 -0.0882 0.2521  0.0508  374 ASP A CA  
2876 C C   . ASP A 374 ? 1.4385 0.5288 0.6411 -0.0916 0.2821  0.0502  374 ASP A C   
2877 O O   . ASP A 374 ? 1.5074 0.5903 0.7104 -0.0950 0.3088  0.0445  374 ASP A O   
2878 C CB  . ASP A 374 ? 1.3989 0.5017 0.5821 -0.0925 0.2613  0.0417  374 ASP A CB  
2879 C CG  . ASP A 374 ? 1.6116 0.6736 0.7416 -0.0887 0.2733  0.0414  374 ASP A CG  
2880 O OD1 . ASP A 374 ? 1.6494 0.6759 0.7410 -0.0829 0.2756  0.0483  374 ASP A OD1 
2881 O OD2 . ASP A 374 ? 1.7412 0.8053 0.8676 -0.0913 0.2804  0.0341  374 ASP A OD2 
2882 N N   . GLU A 375 ? 1.3380 0.4330 0.5597 -0.0906 0.2778  0.0558  375 GLU A N   
2883 C CA  . GLU A 375 ? 1.3984 0.4888 0.6402 -0.0935 0.3041  0.0559  375 GLU A CA  
2884 C C   . GLU A 375 ? 1.4973 0.5560 0.7055 -0.0861 0.2952  0.0677  375 GLU A C   
2885 O O   . GLU A 375 ? 1.4612 0.5285 0.6780 -0.0828 0.2712  0.0731  375 GLU A O   
2886 C CB  . GLU A 375 ? 1.4114 0.5450 0.7234 -0.1013 0.3111  0.0488  375 GLU A CB  
2887 C CG  . GLU A 375 ? 1.4355 0.6004 0.7860 -0.1088 0.3243  0.0365  375 GLU A CG  
2888 C CD  . GLU A 375 ? 1.4451 0.6453 0.8623 -0.1160 0.3375  0.0285  375 GLU A CD  
2889 O OE1 . GLU A 375 ? 1.4960 0.6867 0.9241 -0.1167 0.3542  0.0301  375 GLU A OE1 
2890 O OE2 . GLU A 375 ? 1.3868 0.6236 0.8456 -0.1206 0.3305  0.0203  375 GLU A OE2 
2891 N N   . PRO A 376 ? 1.5107 0.5319 0.6813 -0.0828 0.3135  0.0719  376 PRO A N   
2892 C CA  . PRO A 376 ? 1.5267 0.5180 0.6685 -0.0759 0.3069  0.0834  376 PRO A CA  
2893 C C   . PRO A 376 ? 1.4793 0.4900 0.6712 -0.0801 0.3174  0.0842  376 PRO A C   
2894 O O   . PRO A 376 ? 1.4629 0.4979 0.7019 -0.0882 0.3401  0.0758  376 PRO A O   
2895 C CB  . PRO A 376 ? 1.5569 0.5038 0.6479 -0.0724 0.3285  0.0859  376 PRO A CB  
2896 C CG  . PRO A 376 ? 1.5562 0.5182 0.6740 -0.0803 0.3568  0.0745  376 PRO A CG  
2897 C CD  . PRO A 376 ? 1.5279 0.5300 0.6790 -0.0848 0.3408  0.0665  376 PRO A CD  
2898 N N   . LEU A 377 ? 1.5036 0.5033 0.6864 -0.0743 0.2996  0.0939  377 LEU A N   
2899 C CA  . LEU A 377 ? 1.4616 0.4760 0.6887 -0.0773 0.3064  0.0954  377 LEU A CA  
2900 C C   . LEU A 377 ? 1.5818 0.5608 0.7852 -0.0748 0.3280  0.1027  377 LEU A C   
2901 O O   . LEU A 377 ? 1.5693 0.5079 0.7140 -0.0678 0.3280  0.1100  377 LEU A O   
2902 C CB  . LEU A 377 ? 1.4394 0.4645 0.6775 -0.0724 0.2748  0.1011  377 LEU A CB  
2903 C CG  . LEU A 377 ? 1.3783 0.4428 0.6524 -0.0758 0.2557  0.0933  377 LEU A CG  
2904 C CD1 . LEU A 377 ? 1.3468 0.4170 0.6293 -0.0697 0.2254  0.0991  377 LEU A CD1 
2905 C CD2 . LEU A 377 ? 1.3143 0.4170 0.6505 -0.0863 0.2750  0.0812  377 LEU A CD2 
2906 N N   . ALA A 378 ? 1.6060 0.5997 0.8559 -0.0804 0.3463  0.1001  378 ALA A N   
2907 C CA  . ALA A 378 ? 1.6017 0.5644 0.8366 -0.0788 0.3684  0.1069  378 ALA A CA  
2908 C C   . ALA A 378 ? 1.6126 0.5469 0.8127 -0.0694 0.3476  0.1209  378 ALA A C   
2909 O O   . ALA A 378 ? 1.5740 0.5220 0.7815 -0.0658 0.3181  0.1236  378 ALA A O   
2910 C CB  . ALA A 378 ? 1.5667 0.5554 0.8657 -0.0875 0.3906  0.0995  378 ALA A CB  
2911 N N   . PRO A 379 ? 1.7575 0.6511 0.9193 -0.0648 0.3625  0.1299  379 PRO A N   
2912 C CA  . PRO A 379 ? 1.6800 0.5472 0.8139 -0.0558 0.3442  0.1435  379 PRO A CA  
2913 C C   . PRO A 379 ? 1.6358 0.5300 0.8259 -0.0587 0.3365  0.1436  379 PRO A C   
2914 O O   . PRO A 379 ? 1.6040 0.5218 0.8465 -0.0673 0.3573  0.1358  379 PRO A O   
2915 C CB  . PRO A 379 ? 1.7535 0.5762 0.8475 -0.0529 0.3705  0.1508  379 PRO A CB  
2916 C CG  . PRO A 379 ? 1.7680 0.5842 0.8440 -0.0566 0.3926  0.1426  379 PRO A CG  
2917 C CD  . PRO A 379 ? 1.7138 0.5800 0.8499 -0.0664 0.3952  0.1284  379 PRO A CD  
2918 N N   . GLY A 380 ? 1.6348 0.5254 0.8153 -0.0510 0.3057  0.1515  380 GLY A N   
2919 C CA  . GLY A 380 ? 1.5951 0.5089 0.8257 -0.0523 0.2950  0.1515  380 GLY A CA  
2920 C C   . GLY A 380 ? 1.5224 0.4808 0.7995 -0.0566 0.2775  0.1411  380 GLY A C   
2921 O O   . GLY A 380 ? 1.4934 0.4673 0.8030 -0.0549 0.2609  0.1417  380 GLY A O   
2922 N N   . VAL A 381 ? 1.4941 0.4722 0.7751 -0.0617 0.2811  0.1313  381 VAL A N   
2923 C CA  . VAL A 381 ? 1.4269 0.4468 0.7510 -0.0661 0.2663  0.1210  381 VAL A CA  
2924 C C   . VAL A 381 ? 1.4251 0.4413 0.7249 -0.0572 0.2308  0.1267  381 VAL A C   
2925 O O   . VAL A 381 ? 1.4580 0.4529 0.7077 -0.0516 0.2201  0.1312  381 VAL A O   
2926 C CB  . VAL A 381 ? 1.4002 0.4412 0.7363 -0.0743 0.2821  0.1092  381 VAL A CB  
2927 C CG1 . VAL A 381 ? 1.3964 0.4780 0.7723 -0.0780 0.2652  0.0994  381 VAL A CG1 
2928 C CG2 . VAL A 381 ? 1.3998 0.4472 0.7675 -0.0828 0.3162  0.1025  381 VAL A CG2 
2929 N N   . THR A 382 ? 1.3883 0.4249 0.7246 -0.0556 0.2122  0.1257  382 THR A N   
2930 C CA  . THR A 382 ? 1.3938 0.4320 0.7185 -0.0473 0.1782  0.1295  382 THR A CA  
2931 C C   . THR A 382 ? 1.3174 0.3947 0.6792 -0.0525 0.1689  0.1178  382 THR A C   
2932 O O   . THR A 382 ? 1.2780 0.3829 0.6802 -0.0620 0.1867  0.1068  382 THR A O   
2933 C CB  . THR A 382 ? 1.3873 0.4177 0.7255 -0.0401 0.1624  0.1372  382 THR A CB  
2934 O OG1 . THR A 382 ? 1.3478 0.4032 0.7432 -0.0470 0.1756  0.1295  382 THR A OG1 
2935 C CG2 . THR A 382 ? 1.4547 0.4431 0.7487 -0.0332 0.1668  0.1503  382 THR A CG2 
2936 N N   . ILE A 383 ? 1.3302 0.4095 0.6785 -0.0458 0.1398  0.1200  383 ILE A N   
2937 C CA  . ILE A 383 ? 1.2970 0.4088 0.6724 -0.0494 0.1287  0.1102  383 ILE A CA  
2938 C C   . ILE A 383 ? 1.2956 0.4198 0.6978 -0.0430 0.1024  0.1110  383 ILE A C   
2939 O O   . ILE A 383 ? 1.4149 0.5183 0.7940 -0.0328 0.0809  0.1206  383 ILE A O   
2940 C CB  . ILE A 383 ? 1.3149 0.4189 0.6499 -0.0478 0.1192  0.1104  383 ILE A CB  
2941 C CG1 . ILE A 383 ? 1.3139 0.4058 0.6246 -0.0539 0.1471  0.1083  383 ILE A CG1 
2942 C CG2 . ILE A 383 ? 1.2894 0.4262 0.6537 -0.0512 0.1066  0.1011  383 ILE A CG2 
2943 C CD1 . ILE A 383 ? 1.3489 0.4305 0.6181 -0.0523 0.1396  0.1076  383 ILE A CD1 
2944 N N   . THR A 384 ? 1.2460 0.4039 0.6976 -0.0486 0.1040  0.1001  384 THR A N   
2945 C CA  . THR A 384 ? 1.2798 0.4535 0.7604 -0.0433 0.0806  0.0979  384 THR A CA  
2946 C C   . THR A 384 ? 1.1730 0.3786 0.6656 -0.0450 0.0682  0.0891  384 THR A C   
2947 O O   . THR A 384 ? 1.1670 0.4008 0.6827 -0.0536 0.0834  0.0782  384 THR A O   
2948 C CB  . THR A 384 ? 1.2097 0.4030 0.7412 -0.0473 0.0916  0.0901  384 THR A CB  
2949 O OG1 . THR A 384 ? 1.2982 0.4693 0.8241 -0.0445 0.1003  0.0979  384 THR A OG1 
2950 C CG2 . THR A 384 ? 1.2093 0.4358 0.7797 -0.0410 0.0683  0.0841  384 THR A CG2 
2951 N N   . SER A 385 ? 1.2500 0.4573 0.7321 -0.0361 0.0397  0.0929  385 SER A N   
2952 C CA  . SER A 385 ? 1.2632 0.5023 0.7554 -0.0366 0.0265  0.0852  385 SER A CA  
2953 C C   . SER A 385 ? 1.2354 0.5272 0.7886 -0.0397 0.0265  0.0718  385 SER A C   
2954 O O   . SER A 385 ? 1.1310 0.4345 0.7177 -0.0406 0.0340  0.0679  385 SER A O   
2955 C CB  . SER A 385 ? 1.2773 0.5034 0.7465 -0.0261 -0.0049 0.0922  385 SER A CB  
2956 O OG  . SER A 385 ? 1.3072 0.5439 0.8079 -0.0184 -0.0229 0.0934  385 SER A OG  
2957 N N   . TRP A 386 ? 1.1333 0.4555 0.6990 -0.0411 0.0181  0.0645  386 TRP A N   
2958 C CA  . TRP A 386 ? 1.1179 0.4879 0.7357 -0.0432 0.0176  0.0525  386 TRP A CA  
2959 C C   . TRP A 386 ? 1.1108 0.4942 0.7587 -0.0350 -0.0014 0.0530  386 TRP A C   
2960 O O   . TRP A 386 ? 1.1335 0.5505 0.8242 -0.0361 0.0018  0.0438  386 TRP A O   
2961 C CB  . TRP A 386 ? 1.0736 0.4691 0.6945 -0.0461 0.0134  0.0462  386 TRP A CB  
2962 C CG  . TRP A 386 ? 1.1370 0.5317 0.7485 -0.0388 -0.0126 0.0502  386 TRP A CG  
2963 C CD1 . TRP A 386 ? 1.1358 0.4976 0.7025 -0.0349 -0.0250 0.0587  386 TRP A CD1 
2964 C CD2 . TRP A 386 ? 1.0882 0.5160 0.7371 -0.0344 -0.0294 0.0454  386 TRP A CD2 
2965 N NE1 . TRP A 386 ? 1.1158 0.4893 0.6923 -0.0285 -0.0503 0.0587  386 TRP A NE1 
2966 C CE2 . TRP A 386 ? 1.1295 0.5438 0.7579 -0.0283 -0.0524 0.0508  386 TRP A CE2 
2967 C CE3 . TRP A 386 ? 1.0557 0.5218 0.7526 -0.0349 -0.0267 0.0367  386 TRP A CE3 
2968 C CZ2 . TRP A 386 ? 1.1195 0.5588 0.7789 -0.0234 -0.0718 0.0478  386 TRP A CZ2 
2969 C CZ3 . TRP A 386 ? 1.0314 0.5206 0.7552 -0.0297 -0.0442 0.0346  386 TRP A CZ3 
2970 C CH2 . TRP A 386 ? 1.0847 0.5612 0.7922 -0.0243 -0.0662 0.0401  386 TRP A CH2 
2971 N N   . LYS A 387 ? 1.1553 0.5124 0.7818 -0.0264 -0.0210 0.0630  387 LYS A N   
2972 C CA  . LYS A 387 ? 1.1837 0.5487 0.8396 -0.0180 -0.0382 0.0644  387 LYS A CA  
2973 C C   . LYS A 387 ? 1.2841 0.6328 0.9486 -0.0169 -0.0277 0.0674  387 LYS A C   
2974 O O   . LYS A 387 ? 1.3396 0.6882 1.0249 -0.0091 -0.0413 0.0699  387 LYS A O   
2975 C CB  . LYS A 387 ? 1.2709 0.6141 0.9031 -0.0085 -0.0660 0.0735  387 LYS A CB  
2976 C CG  . LYS A 387 ? 1.2735 0.6372 0.9084 -0.0082 -0.0809 0.0693  387 LYS A CG  
2977 C CD  . LYS A 387 ? 1.3739 0.7187 0.9943 0.0019  -0.1116 0.0766  387 LYS A CD  
2978 C CE  . LYS A 387 ? 1.3839 0.7525 1.0167 0.0022  -0.1273 0.0710  387 LYS A CE  
2979 N NZ  . LYS A 387 ? 1.4348 0.7959 1.0312 -0.0047 -0.1177 0.0694  387 LYS A NZ  
2980 N N   . ASN A 388 ? 1.2843 0.6191 0.9358 -0.0245 -0.0036 0.0668  388 ASN A N   
2981 C CA  . ASN A 388 ? 1.2585 0.5762 0.9183 -0.0247 0.0092  0.0690  388 ASN A CA  
2982 C C   . ASN A 388 ? 1.3892 0.6643 1.0186 -0.0155 -0.0044 0.0836  388 ASN A C   
2983 O O   . ASN A 388 ? 1.3457 0.6166 0.9960 -0.0097 -0.0102 0.0859  388 ASN A O   
2984 C CB  . ASN A 388 ? 1.2065 0.5596 0.9205 -0.0245 0.0112  0.0579  388 ASN A CB  
2985 C CG  . ASN A 388 ? 1.2282 0.5704 0.9553 -0.0285 0.0306  0.0557  388 ASN A CG  
2986 O OD1 . ASN A 388 ? 1.2589 0.5744 0.9609 -0.0341 0.0476  0.0599  388 ASN A OD1 
2987 N ND2 . ASN A 388 ? 1.2974 0.6595 1.0651 -0.0257 0.0292  0.0486  388 ASN A ND2 
2988 N N   . LYS A 389 ? 1.4565 0.6983 1.0345 -0.0137 -0.0099 0.0936  389 LYS A N   
2989 C CA  . LYS A 389 ? 1.5181 0.7149 1.0576 -0.0042 -0.0247 0.1084  389 LYS A CA  
2990 C C   . LYS A 389 ? 1.5745 0.7267 1.0552 -0.0078 -0.0087 0.1179  389 LYS A C   
2991 O O   . LYS A 389 ? 1.5152 0.6735 0.9818 -0.0159 0.0060  0.1131  389 LYS A O   
2992 C CB  . LYS A 389 ? 1.5403 0.7394 1.0732 0.0057  -0.0580 0.1117  389 LYS A CB  
2993 C CG  . LYS A 389 ? 1.5586 0.7988 1.1497 0.0101  -0.0740 0.1035  389 LYS A CG  
2994 C CD  . LYS A 389 ? 1.6694 0.9133 1.2569 0.0186  -0.1056 0.1055  389 LYS A CD  
2995 C CE  . LYS A 389 ? 1.6788 0.9651 1.3278 0.0223  -0.1183 0.0969  389 LYS A CE  
2996 N NZ  . LYS A 389 ? 1.6643 0.9571 1.3163 0.0294  -0.1481 0.0975  389 LYS A NZ  
2997 N N   . GLU A 390 ? 1.7269 0.8466 1.1813 -0.0012 -0.0106 0.1293  390 GLU A N   
2998 C CA  . GLU A 390 ? 1.7374 0.8283 1.1417 -0.0027 0.0034  0.1367  390 GLU A CA  
2999 C C   . GLU A 390 ? 1.7570 0.8380 1.1186 0.0004  -0.0128 0.1385  390 GLU A C   
3000 O O   . GLU A 390 ? 1.8033 0.8765 1.1524 0.0105  -0.0429 0.1430  390 GLU A O   
3001 C CB  . GLU A 390 ? 1.8478 0.9091 1.2343 0.0054  0.0006  0.1484  390 GLU A CB  
3002 C CG  . GLU A 390 ? 1.9517 1.0157 1.3706 0.0004  0.0241  0.1473  390 GLU A CG  
3003 C CD  . GLU A 390 ? 1.9717 1.0280 1.3759 -0.0098 0.0576  0.1458  390 GLU A CD  
3004 O OE1 . GLU A 390 ? 1.9477 0.9921 1.3116 -0.0118 0.0631  0.1471  390 GLU A OE1 
3005 O OE2 . GLU A 390 ? 1.9630 1.0256 1.3980 -0.0156 0.0785  0.1426  390 GLU A OE2 
3006 N N   . TRP A 391 ? 1.6227 0.7047 0.9642 -0.0081 0.0066  0.1340  391 TRP A N   
3007 C CA  . TRP A 391 ? 1.6574 0.7321 0.9608 -0.0068 -0.0054 0.1334  391 TRP A CA  
3008 C C   . TRP A 391 ? 1.6596 0.7019 0.9089 -0.0077 0.0118  0.1385  391 TRP A C   
3009 O O   . TRP A 391 ? 1.5745 0.6154 0.8270 -0.0156 0.0429  0.1367  391 TRP A O   
3010 C CB  . TRP A 391 ? 1.5386 0.6442 0.8671 -0.0159 0.0016  0.1222  391 TRP A CB  
3011 C CG  . TRP A 391 ? 1.5641 0.6629 0.8562 -0.0152 -0.0094 0.1208  391 TRP A CG  
3012 C CD1 . TRP A 391 ? 1.6025 0.7072 0.8931 -0.0092 -0.0400 0.1199  391 TRP A CD1 
3013 C CD2 . TRP A 391 ? 1.5918 0.6767 0.8460 -0.0208 0.0105  0.1192  391 TRP A CD2 
3014 N NE1 . TRP A 391 ? 1.6648 0.7595 0.9174 -0.0108 -0.0410 0.1179  391 TRP A NE1 
3015 C CE2 . TRP A 391 ? 1.6516 0.7337 0.8806 -0.0177 -0.0098 0.1173  391 TRP A CE2 
3016 C CE3 . TRP A 391 ? 1.5678 0.6427 0.8098 -0.0278 0.0437  0.1186  391 TRP A CE3 
3017 C CZ2 . TRP A 391 ? 1.6668 0.7352 0.8566 -0.0214 0.0025  0.1146  391 TRP A CZ2 
3018 C CZ3 . TRP A 391 ? 1.6194 0.6815 0.8245 -0.0312 0.0563  0.1159  391 TRP A CZ3 
3019 C CH2 . TRP A 391 ? 1.6373 0.6957 0.8156 -0.0280 0.0360  0.1139  391 TRP A CH2 
3020 N N   . ARG A 392 ? 1.7209 0.7378 0.9222 0.0006  -0.0086 0.1436  392 ARG A N   
3021 C CA  . ARG A 392 ? 1.7980 0.7805 0.9420 0.0013  0.0048  0.1476  392 ARG A CA  
3022 C C   . ARG A 392 ? 1.8912 0.8724 1.0051 -0.0003 -0.0015 0.1415  392 ARG A C   
3023 O O   . ARG A 392 ? 1.8873 0.8859 1.0146 0.0021  -0.0269 0.1374  392 ARG A O   
3024 C CB  . ARG A 392 ? 1.8662 0.8133 0.9723 0.0133  -0.0130 0.1584  392 ARG A CB  
3025 C CG  . ARG A 392 ? 1.7889 0.7326 0.9203 0.0152  -0.0049 0.1654  392 ARG A CG  
3026 C CD  . ARG A 392 ? 1.7644 0.6720 0.8566 0.0273  -0.0226 0.1766  392 ARG A CD  
3027 N NE  . ARG A 392 ? 1.8298 0.7331 0.9467 0.0290  -0.0135 0.1837  392 ARG A NE  
3028 C CZ  . ARG A 392 ? 1.8673 0.7403 0.9580 0.0388  -0.0241 0.1945  392 ARG A CZ  
3029 N NH1 . ARG A 392 ? 1.9190 0.7624 0.9567 0.0481  -0.0450 0.1990  392 ARG A NH1 
3030 N NH2 . ARG A 392 ? 1.8162 0.6879 0.9347 0.0393  -0.0139 0.2003  392 ARG A NH2 
3031 N N   . PRO A 393 ? 1.9576 0.9182 1.0327 -0.0043 0.0217  0.1402  393 PRO A N   
3032 C CA  . PRO A 393 ? 2.0290 0.9884 1.0774 -0.0065 0.0182  0.1332  393 PRO A CA  
3033 C C   . PRO A 393 ? 2.1704 1.1123 1.1834 0.0039  -0.0185 0.1347  393 PRO A C   
3034 O O   . PRO A 393 ? 2.1860 1.1385 1.1955 0.0026  -0.0311 0.1279  393 PRO A O   
3035 C CB  . PRO A 393 ? 2.0372 0.9713 1.0493 -0.0109 0.0515  0.1327  393 PRO A CB  
3036 C CG  . PRO A 393 ? 1.9587 0.8981 1.0010 -0.0157 0.0781  0.1360  393 PRO A CG  
3037 C CD  . PRO A 393 ? 1.9306 0.8716 0.9919 -0.0082 0.0552  0.1436  393 PRO A CD  
3038 N N   . GLN A 394 ? 2.3541 1.2698 1.3423 0.0143  -0.0368 0.1430  394 GLN A N   
3039 C CA  . GLN A 394 ? 2.4185 1.3160 1.3737 0.0248  -0.0733 0.1436  394 GLN A CA  
3040 C C   . GLN A 394 ? 2.3687 1.2932 1.3675 0.0301  -0.1081 0.1430  394 GLN A C   
3041 O O   . GLN A 394 ? 2.4092 1.3194 1.3912 0.0405  -0.1407 0.1453  394 GLN A O   
3042 C CB  . GLN A 394 ? 2.6079 1.4614 1.5124 0.0340  -0.0767 0.1522  394 GLN A CB  
3043 C CG  . GLN A 394 ? 2.7187 1.5396 1.5732 0.0305  -0.0453 0.1523  394 GLN A CG  
3044 C CD  . GLN A 394 ? 2.9900 1.7648 1.7916 0.0403  -0.0495 0.1612  394 GLN A CD  
3045 O OE1 . GLN A 394 ? 3.0373 1.8056 1.8424 0.0493  -0.0742 0.1682  394 GLN A OE1 
3046 N NE2 . GLN A 394 ? 3.0680 1.8097 1.8209 0.0389  -0.0249 0.1611  394 GLN A NE2 
3047 N N   . ASP A 395 ? 2.2800 1.2428 1.3358 0.0234  -0.1019 0.1393  395 ASP A N   
3048 C CA  . ASP A 395 ? 2.2451 1.2359 1.3477 0.0278  -0.1317 0.1375  395 ASP A CA  
3049 C C   . ASP A 395 ? 2.2380 1.2500 1.3516 0.0242  -0.1444 0.1286  395 ASP A C   
3050 O O   . ASP A 395 ? 2.1928 1.2025 1.2846 0.0170  -0.1264 0.1235  395 ASP A O   
3051 C CB  . ASP A 395 ? 2.1006 1.1183 1.2608 0.0235  -0.1177 0.1385  395 ASP A CB  
3052 C CG  . ASP A 395 ? 2.0353 1.0330 1.1893 0.0273  -0.1068 0.1475  395 ASP A CG  
3053 O OD1 . ASP A 395 ? 2.0724 1.0348 1.1762 0.0331  -0.1090 0.1535  395 ASP A OD1 
3054 O OD2 . ASP A 395 ? 1.9207 0.9368 1.1197 0.0246  -0.0960 0.1480  395 ASP A OD2 
3055 N N   . GLU A 396 ? 2.3624 1.3957 1.5131 0.0297  -0.1755 0.1264  396 GLU A N   
3056 C CA  . GLU A 396 ? 2.3522 1.4061 1.5175 0.0272  -0.1904 0.1184  396 GLU A CA  
3057 C C   . GLU A 396 ? 2.2865 1.3767 1.5016 0.0171  -0.1704 0.1133  396 GLU A C   
3058 O O   . GLU A 396 ? 2.2730 1.3813 1.4900 0.0095  -0.1592 0.1050  396 GLU A O   
3059 C CB  . GLU A 396 ? 2.3795 1.4418 1.5675 0.0374  -0.2327 0.1171  396 GLU A CB  
3060 C CG  . GLU A 396 ? 2.4339 1.5157 1.6372 0.0358  -0.2510 0.1088  396 GLU A CG  
3061 C CD  . GLU A 396 ? 2.3334 1.4316 1.5763 0.0450  -0.2906 0.1065  396 GLU A CD  
3062 O OE1 . GLU A 396 ? 2.3042 1.4078 1.5773 0.0512  -0.2999 0.1108  396 GLU A OE1 
3063 O OE2 . GLU A 396 ? 2.3077 1.4172 1.5569 0.0456  -0.3110 0.0987  396 GLU A OE2 
3064 N N   . GLU A 397 ? 2.1012 1.2180 1.3684 0.0162  -0.1631 0.1129  397 GLU A N   
3065 C CA  . GLU A 397 ? 1.9119 1.0806 1.2393 0.0067  -0.1431 0.1024  397 GLU A CA  
3066 C C   . GLU A 397 ? 1.7958 0.9592 1.1051 -0.0041 -0.1060 0.1009  397 GLU A C   
3067 O O   . GLU A 397 ? 1.8445 0.9713 1.1173 -0.0045 -0.0891 0.1094  397 GLU A O   
3068 C CB  . GLU A 397 ? 1.8900 1.0833 1.2720 0.0090  -0.1436 0.1022  397 GLU A CB  
3069 C CG  . GLU A 397 ? 1.9974 1.2043 1.4119 0.0189  -0.1777 0.1019  397 GLU A CG  
3070 C CD  . GLU A 397 ? 1.9834 1.2359 1.4441 0.0162  -0.1876 0.0906  397 GLU A CD  
3071 O OE1 . GLU A 397 ? 1.9275 1.2063 1.4026 0.0066  -0.1665 0.0829  397 GLU A OE1 
3072 O OE2 . GLU A 397 ? 2.0433 1.3048 1.5273 0.0237  -0.2166 0.0895  397 GLU A OE2 
3073 N N   . PRO A 398 ? 1.6295 0.8279 0.9649 -0.0127 -0.0924 0.0905  398 PRO A N   
3074 C CA  . PRO A 398 ? 1.4965 0.6942 0.8240 -0.0229 -0.0575 0.0879  398 PRO A CA  
3075 C C   . PRO A 398 ? 1.4695 0.6849 0.8368 -0.0270 -0.0378 0.0868  398 PRO A C   
3076 O O   . PRO A 398 ? 1.3875 0.6328 0.8026 -0.0244 -0.0478 0.0835  398 PRO A O   
3077 C CB  . PRO A 398 ? 1.4239 0.6585 0.7758 -0.0292 -0.0546 0.0767  398 PRO A CB  
3078 C CG  . PRO A 398 ? 1.4322 0.7017 0.8299 -0.0243 -0.0804 0.0721  398 PRO A CG  
3079 C CD  . PRO A 398 ? 1.6245 0.8640 0.9994 -0.0134 -0.1080 0.0808  398 PRO A CD  
3080 N N   . CYS A 399 ? 1.4275 0.6233 0.7754 -0.0336 -0.0085 0.0889  399 CYS A N   
3081 C CA  . CYS A 399 ? 1.3851 0.5949 0.7696 -0.0382 0.0112  0.0869  399 CYS A CA  
3082 C C   . CYS A 399 ? 1.2181 0.4818 0.6610 -0.0449 0.0190  0.0735  399 CYS A C   
3083 O O   . CYS A 399 ? 1.2171 0.5027 0.7014 -0.0461 0.0246  0.0695  399 CYS A O   
3084 C CB  . CYS A 399 ? 1.3245 0.4988 0.6760 -0.0439 0.0412  0.0922  399 CYS A CB  
3085 S SG  . CYS A 399 ? 1.2260 0.4078 0.5689 -0.0550 0.0685  0.0842  399 CYS A SG  
3086 N N   . ALA A 400 ? 1.2011 0.4852 0.6467 -0.0488 0.0191  0.0664  400 ALA A N   
3087 C CA  . ALA A 400 ? 1.1716 0.5047 0.6677 -0.0541 0.0248  0.0545  400 ALA A CA  
3088 C C   . ALA A 400 ? 1.1149 0.4730 0.6257 -0.0500 0.0013  0.0508  400 ALA A C   
3089 O O   . ALA A 400 ? 1.1682 0.5062 0.6459 -0.0457 -0.0149 0.0551  400 ALA A O   
3090 C CB  . ALA A 400 ? 1.0930 0.4311 0.5865 -0.0636 0.0506  0.0484  400 ALA A CB  
3091 N N   . HIS A 401 ? 1.0936 0.4945 0.6540 -0.0512 -0.0004 0.0424  401 HIS A N   
3092 C CA  . HIS A 401 ? 0.9809 0.4079 0.5607 -0.0482 -0.0192 0.0385  401 HIS A CA  
3093 C C   . HIS A 401 ? 1.0081 0.4399 0.5730 -0.0533 -0.0127 0.0342  401 HIS A C   
3094 O O   . HIS A 401 ? 0.9839 0.4187 0.5472 -0.0603 0.0091  0.0303  401 HIS A O   
3095 C CB  . HIS A 401 ? 0.9864 0.4552 0.6200 -0.0480 -0.0193 0.0312  401 HIS A CB  
3096 C CG  . HIS A 401 ? 0.9925 0.4849 0.6497 -0.0436 -0.0390 0.0289  401 HIS A CG  
3097 N ND1 . HIS A 401 ? 0.9197 0.4358 0.5881 -0.0468 -0.0379 0.0231  401 HIS A ND1 
3098 C CD2 . HIS A 401 ? 0.9458 0.4413 0.6198 -0.0362 -0.0597 0.0317  401 HIS A CD2 
3099 C CE1 . HIS A 401 ? 0.9470 0.4793 0.6380 -0.0420 -0.0561 0.0224  401 HIS A CE1 
3100 N NE2 . HIS A 401 ? 0.8998 0.4207 0.5959 -0.0356 -0.0696 0.0273  401 HIS A NE2 
3101 N N   . PRO A 402 ? 0.9983 0.4304 0.5538 -0.0499 -0.0315 0.0344  402 PRO A N   
3102 C CA  . PRO A 402 ? 0.9904 0.4264 0.5322 -0.0546 -0.0255 0.0300  402 PRO A CA  
3103 C C   . PRO A 402 ? 0.9718 0.4467 0.5519 -0.0605 -0.0104 0.0212  402 PRO A C   
3104 O O   . PRO A 402 ? 0.9801 0.4553 0.5491 -0.0658 0.0029  0.0176  402 PRO A O   
3105 C CB  . PRO A 402 ? 0.9498 0.3851 0.4872 -0.0491 -0.0520 0.0307  402 PRO A CB  
3106 C CG  . PRO A 402 ? 1.0189 0.4309 0.5439 -0.0414 -0.0704 0.0381  402 PRO A CG  
3107 C CD  . PRO A 402 ? 0.9548 0.3778 0.5074 -0.0416 -0.0593 0.0390  402 PRO A CD  
3108 N N   . ASN A 403 ? 0.9123 0.4187 0.5358 -0.0593 -0.0120 0.0176  403 ASN A N   
3109 C CA  . ASN A 403 ? 0.9119 0.4536 0.5692 -0.0637 0.0008  0.0096  403 ASN A CA  
3110 C C   . ASN A 403 ? 0.9267 0.4742 0.5994 -0.0671 0.0187  0.0065  403 ASN A C   
3111 O O   . ASN A 403 ? 0.8447 0.4227 0.5502 -0.0687 0.0251  -0.0003 403 ASN A O   
3112 C CB  . ASN A 403 ? 0.9331 0.5067 0.6271 -0.0599 -0.0124 0.0066  403 ASN A CB  
3113 C CG  . ASN A 403 ? 0.9657 0.5710 0.6842 -0.0636 -0.0023 -0.0006 403 ASN A CG  
3114 O OD1 . ASN A 403 ? 0.9392 0.5422 0.6440 -0.0679 0.0063  -0.0029 403 ASN A OD1 
3115 N ND2 . ASN A 403 ? 0.9561 0.5897 0.7099 -0.0614 -0.0028 -0.0041 403 ASN A ND2 
3116 N N   . SER A 404 ? 0.8959 0.4136 0.5451 -0.0680 0.0265  0.0112  404 SER A N   
3117 C CA  . SER A 404 ? 0.8550 0.3761 0.5198 -0.0720 0.0442  0.0077  404 SER A CA  
3118 C C   . SER A 404 ? 0.8150 0.3508 0.4889 -0.0791 0.0622  0.0000  404 SER A C   
3119 O O   . SER A 404 ? 0.8837 0.4112 0.5372 -0.0818 0.0663  0.0003  404 SER A O   
3120 C CB  . SER A 404 ? 0.9261 0.4083 0.5612 -0.0719 0.0507  0.0153  404 SER A CB  
3121 O OG  . SER A 404 ? 0.9362 0.3885 0.5303 -0.0746 0.0583  0.0196  404 SER A OG  
3122 N N   . ARG A 405 ? 0.7932 0.3506 0.4988 -0.0819 0.0723  -0.0074 405 ARG A N   
3123 C CA  . ARG A 405 ? 0.8140 0.3920 0.5372 -0.0874 0.0855  -0.0161 405 ARG A CA  
3124 C C   . ARG A 405 ? 0.7814 0.3553 0.5176 -0.0927 0.1033  -0.0211 405 ARG A C   
3125 O O   . ARG A 405 ? 0.7925 0.3574 0.5343 -0.0916 0.1041  -0.0197 405 ARG A O   
3126 C CB  . ARG A 405 ? 0.7062 0.3223 0.4611 -0.0849 0.0770  -0.0229 405 ARG A CB  
3127 C CG  . ARG A 405 ? 0.7218 0.3453 0.4708 -0.0803 0.0610  -0.0191 405 ARG A CG  
3128 C CD  . ARG A 405 ? 0.7409 0.3727 0.4854 -0.0833 0.0650  -0.0218 405 ARG A CD  
3129 N NE  . ARG A 405 ? 0.7579 0.3934 0.4960 -0.0795 0.0501  -0.0181 405 ARG A NE  
3130 C CZ  . ARG A 405 ? 0.7257 0.3709 0.4631 -0.0808 0.0501  -0.0201 405 ARG A CZ  
3131 N NH1 . ARG A 405 ? 0.7054 0.3589 0.4485 -0.0853 0.0636  -0.0255 405 ARG A NH1 
3132 N NH2 . ARG A 405 ? 0.7604 0.4072 0.4938 -0.0775 0.0360  -0.0169 405 ARG A NH2 
3133 N N   . PHE A 406 ? 0.7417 0.3223 0.4855 -0.0985 0.1176  -0.0272 406 PHE A N   
3134 C CA  . PHE A 406 ? 0.6988 0.2862 0.4679 -0.1038 0.1329  -0.0354 406 PHE A CA  
3135 C C   . PHE A 406 ? 0.7053 0.3302 0.5080 -0.1042 0.1302  -0.0464 406 PHE A C   
3136 O O   . PHE A 406 ? 0.7193 0.3591 0.5206 -0.1024 0.1234  -0.0469 406 PHE A O   
3137 C CB  . PHE A 406 ? 0.7509 0.3131 0.5052 -0.1105 0.1537  -0.0342 406 PHE A CB  
3138 C CG  . PHE A 406 ? 0.7531 0.3127 0.4906 -0.1123 0.1577  -0.0334 406 PHE A CG  
3139 C CD1 . PHE A 406 ? 0.7066 0.2933 0.4703 -0.1149 0.1616  -0.0427 406 PHE A CD1 
3140 C CD2 . PHE A 406 ? 0.7586 0.2871 0.4533 -0.1108 0.1571  -0.0237 406 PHE A CD2 
3141 C CE1 . PHE A 406 ? 0.6964 0.2802 0.4462 -0.1163 0.1659  -0.0422 406 PHE A CE1 
3142 C CE2 . PHE A 406 ? 0.8181 0.3428 0.4966 -0.1124 0.1614  -0.0238 406 PHE A CE2 
3143 C CZ  . PHE A 406 ? 0.7927 0.3455 0.5000 -0.1153 0.1665  -0.0330 406 PHE A CZ  
3144 N N   . CYS A 407 ? 0.6587 0.2975 0.4905 -0.1060 0.1348  -0.0553 407 CYS A N   
3145 C CA  . CYS A 407 ? 0.6827 0.3551 0.5450 -0.1053 0.1306  -0.0664 407 CYS A CA  
3146 C C   . CYS A 407 ? 0.6370 0.3114 0.5225 -0.1121 0.1458  -0.0760 407 CYS A C   
3147 O O   . CYS A 407 ? 0.6690 0.3390 0.5699 -0.1144 0.1512  -0.0806 407 CYS A O   
3148 C CB  . CYS A 407 ? 0.6922 0.3810 0.5689 -0.0998 0.1183  -0.0697 407 CYS A CB  
3149 S SG  . CYS A 407 ? 0.6596 0.3865 0.5616 -0.0961 0.1092  -0.0806 407 CYS A SG  
3150 N N   . THR A 408 ? 0.6176 0.2984 0.5081 -0.1154 0.1528  -0.0793 408 THR A N   
3151 C CA  . THR A 408 ? 0.6268 0.3064 0.5403 -0.1224 0.1691  -0.0876 408 THR A CA  
3152 C C   . THR A 408 ? 0.6259 0.3361 0.5686 -0.1222 0.1649  -0.0987 408 THR A C   
3153 O O   . THR A 408 ? 0.6784 0.4027 0.6137 -0.1179 0.1548  -0.0967 408 THR A O   
3154 C CB  . THR A 408 ? 0.7151 0.3653 0.6061 -0.1276 0.1868  -0.0804 408 THR A CB  
3155 O OG1 . THR A 408 ? 0.7697 0.4173 0.6874 -0.1349 0.2052  -0.0884 408 THR A OG1 
3156 C CG2 . THR A 408 ? 0.6321 0.2856 0.5056 -0.1259 0.1838  -0.0765 408 THR A CG2 
3157 N N   . PRO A 409 ? 0.6398 0.3604 0.6170 -0.1263 0.1716  -0.1106 409 PRO A N   
3158 C CA  . PRO A 409 ? 0.5706 0.3193 0.5765 -0.1255 0.1660  -0.1216 409 PRO A CA  
3159 C C   . PRO A 409 ? 0.6729 0.4185 0.6767 -0.1284 0.1763  -0.1196 409 PRO A C   
3160 O O   . PRO A 409 ? 0.6326 0.3563 0.6314 -0.1346 0.1949  -0.1165 409 PRO A O   
3161 C CB  . PRO A 409 ? 0.6759 0.4315 0.7199 -0.1299 0.1712  -0.1350 409 PRO A CB  
3162 C CG  . PRO A 409 ? 0.6825 0.4198 0.7165 -0.1308 0.1737  -0.1311 409 PRO A CG  
3163 C CD  . PRO A 409 ? 0.6783 0.3876 0.6722 -0.1309 0.1810  -0.1153 409 PRO A CD  
3164 N N   . ALA A 410 ? 0.6049 0.3715 0.6120 -0.1238 0.1650  -0.1214 410 ALA A N   
3165 C CA  . ALA A 410 ? 0.6940 0.4598 0.7005 -0.1257 0.1734  -0.1201 410 ALA A CA  
3166 C C   . ALA A 410 ? 0.7547 0.5245 0.7982 -0.1320 0.1877  -0.1308 410 ALA A C   
3167 O O   . ALA A 410 ? 0.6796 0.4385 0.7212 -0.1359 0.2028  -0.1288 410 ALA A O   
3168 C CB  . ALA A 410 ? 0.6410 0.4292 0.6459 -0.1188 0.1573  -0.1199 410 ALA A CB  
3169 N N   . SER A 411 ? 0.6775 0.4622 0.7558 -0.1330 0.1838  -0.1426 411 SER A N   
3170 C CA  . SER A 411 ? 0.7084 0.4989 0.8288 -0.1390 0.1963  -0.1541 411 SER A CA  
3171 C C   . SER A 411 ? 0.7037 0.4654 0.8219 -0.1477 0.2222  -0.1505 411 SER A C   
3172 O O   . SER A 411 ? 0.7411 0.5019 0.8876 -0.1533 0.2385  -0.1566 411 SER A O   
3173 C CB  . SER A 411 ? 0.6394 0.4513 0.7972 -0.1379 0.1838  -0.1686 411 SER A CB  
3174 O OG  . SER A 411 ? 0.6938 0.4926 0.8458 -0.1400 0.1859  -0.1679 411 SER A OG  
3175 N N   . GLN A 412 ? 0.7136 0.4505 0.7991 -0.1485 0.2270  -0.1405 412 GLN A N   
3176 C CA  . GLN A 412 ? 0.7483 0.4538 0.8262 -0.1560 0.2519  -0.1356 412 GLN A CA  
3177 C C   . GLN A 412 ? 0.8383 0.5202 0.8833 -0.1577 0.2676  -0.1253 412 GLN A C   
3178 O O   . GLN A 412 ? 0.8788 0.5378 0.9143 -0.1612 0.2889  -0.1200 412 GLN A O   
3179 C CB  . GLN A 412 ? 0.7470 0.4330 0.8007 -0.1553 0.2498  -0.1282 412 GLN A CB  
3180 C CG  . GLN A 412 ? 0.7208 0.4253 0.8054 -0.1542 0.2372  -0.1389 412 GLN A CG  
3181 C CD  . GLN A 412 ? 0.7937 0.4772 0.8570 -0.1537 0.2373  -0.1317 412 GLN A CD  
3182 O OE1 . GLN A 412 ? 0.7476 0.4381 0.8357 -0.1547 0.2334  -0.1401 412 GLN A OE1 
3183 N NE2 . GLN A 412 ? 0.7507 0.4077 0.7679 -0.1519 0.2409  -0.1165 412 GLN A NE2 
3184 N N   . CYS A 413 ? 0.7239 0.4586 1.0969 -0.1868 0.3632  -0.2456 413 CYS A N   
3185 C CA  . CYS A 413 ? 0.7210 0.4331 1.0598 -0.1738 0.3581  -0.2108 413 CYS A CA  
3186 C C   . CYS A 413 ? 0.7469 0.4701 1.0972 -0.1817 0.3634  -0.2154 413 CYS A C   
3187 O O   . CYS A 413 ? 0.7460 0.5044 1.1058 -0.1947 0.3531  -0.2423 413 CYS A O   
3188 C CB  . CYS A 413 ? 0.6912 0.4083 0.9835 -0.1665 0.3327  -0.2009 413 CYS A CB  
3189 S SG  . CYS A 413 ? 0.7564 0.4441 1.0032 -0.1493 0.3261  -0.1586 413 CYS A SG  
3190 N N   . PRO A 414 ? 0.7582 0.4546 1.1082 -0.1741 0.3790  -0.1898 414 PRO A N   
3191 C CA  . PRO A 414 ? 0.7518 0.4589 1.1179 -0.1822 0.3875  -0.1955 414 PRO A CA  
3192 C C   . PRO A 414 ? 0.7061 0.4337 1.0449 -0.1838 0.3678  -0.1967 414 PRO A C   
3193 O O   . PRO A 414 ? 0.7002 0.4528 1.0618 -0.1952 0.3692  -0.2147 414 PRO A O   
3194 C CB  . PRO A 414 ? 0.7985 0.4683 1.1595 -0.1704 0.4075  -0.1621 414 PRO A CB  
3195 C CG  . PRO A 414 ? 0.7809 0.4256 1.1414 -0.1600 0.4133  -0.1474 414 PRO A CG  
3196 C CD  . PRO A 414 ? 0.7526 0.4103 1.0898 -0.1580 0.3902  -0.1555 414 PRO A CD  
3197 N N   . ILE A 415 ? 0.6835 0.4020 0.9775 -0.1728 0.3496  -0.1785 415 ILE A N   
3198 C CA  . ILE A 415 ? 0.7499 0.4830 1.0177 -0.1731 0.3325  -0.1769 415 ILE A CA  
3199 C C   . ILE A 415 ? 0.7023 0.4613 0.9570 -0.1777 0.3082  -0.1963 415 ILE A C   
3200 O O   . ILE A 415 ? 0.6506 0.4119 0.8728 -0.1730 0.2910  -0.1885 415 ILE A O   
3201 C CB  . ILE A 415 ? 0.7591 0.4605 0.9823 -0.1566 0.3313  -0.1402 415 ILE A CB  
3202 C CG1 . ILE A 415 ? 0.7886 0.4672 0.9840 -0.1431 0.3237  -0.1216 415 ILE A CG1 
3203 C CG2 . ILE A 415 ? 0.6849 0.3671 0.9170 -0.1532 0.3545  -0.1227 415 ILE A CG2 
3204 C CD1 . ILE A 415 ? 0.8529 0.5063 1.0015 -0.1270 0.3177  -0.0885 415 ILE A CD1 
3205 N N   . ILE A 416 ? 0.7240 0.5025 1.0032 -0.1867 0.3075  -0.2222 416 ILE A N   
3206 C CA  . ILE A 416 ? 0.6643 0.4722 0.9304 -0.1920 0.2854  -0.2429 416 ILE A CA  
3207 C C   . ILE A 416 ? 0.6453 0.4903 0.9137 -0.2015 0.2699  -0.2599 416 ILE A C   
3208 O O   . ILE A 416 ? 0.6889 0.5549 0.9919 -0.2118 0.2778  -0.2746 416 ILE A O   
3209 C CB  . ILE A 416 ? 0.6352 0.4605 0.9297 -0.2012 0.2909  -0.2702 416 ILE A CB  
3210 C CG1 . ILE A 416 ? 0.6215 0.4749 0.8946 -0.2043 0.2692  -0.2881 416 ILE A CG1 
3211 C CG2 . ILE A 416 ? 0.6504 0.5033 0.9917 -0.2166 0.3022  -0.2983 416 ILE A CG2 
3212 C CD1 . ILE A 416 ? 0.6135 0.4394 0.8499 -0.1903 0.2624  -0.2656 416 ILE A CD1 
3213 N N   . ASP A 417 ? 0.6927 0.5468 0.9264 -0.1976 0.2479  -0.2574 417 ASP A N   
3214 C CA  . ASP A 417 ? 0.6603 0.5496 0.8938 -0.2029 0.2312  -0.2680 417 ASP A CA  
3215 C C   . ASP A 417 ? 0.6179 0.5629 0.8845 -0.2203 0.2220  -0.3068 417 ASP A C   
3216 O O   . ASP A 417 ? 0.6299 0.5914 0.8935 -0.2238 0.2162  -0.3239 417 ASP A O   
3217 C CB  . ASP A 417 ? 0.6770 0.5737 0.8586 -0.1843 0.2054  -0.2466 417 ASP A CB  
3218 C CG  . ASP A 417 ? 0.6898 0.6233 0.8645 -0.1757 0.1869  -0.2387 417 ASP A CG  
3219 O OD1 . ASP A 417 ? 0.6589 0.5739 0.8302 -0.1665 0.1944  -0.2179 417 ASP A OD1 
3220 O OD2 . ASP A 417 ? 0.6637 0.6455 0.8367 -0.1776 0.1654  -0.2531 417 ASP A OD2 
3221 N N   . PRO A 418 ? 0.6398 0.6213 0.9358 -0.2270 0.2187  -0.3173 418 PRO A N   
3222 C CA  . PRO A 418 ? 0.6629 0.7040 0.9917 -0.2437 0.2072  -0.3553 418 PRO A CA  
3223 C C   . PRO A 418 ? 0.6389 0.7268 0.9351 -0.2389 0.1752  -0.3633 418 PRO A C   
3224 O O   . PRO A 418 ? 0.7128 0.8573 1.0304 -0.2522 0.1615  -0.3945 418 PRO A O   
3225 C CB  . PRO A 418 ? 0.5671 0.6354 0.9332 -0.2475 0.2100  -0.3567 418 PRO A CB  
3226 C CG  . PRO A 418 ? 0.6451 0.6824 0.9783 -0.2252 0.2106  -0.3157 418 PRO A CG  
3227 C CD  . PRO A 418 ? 0.7003 0.6740 1.0011 -0.2176 0.2254  -0.2942 418 PRO A CD  
3228 N N   . ALA A 419 ? 0.6910 0.7596 0.9356 -0.2199 0.1626  -0.3348 419 ALA A N   
3229 C CA  . ALA A 419 ? 0.7082 0.8161 0.9176 -0.2136 0.1351  -0.3365 419 ALA A CA  
3230 C C   . ALA A 419 ? 0.7125 0.7877 0.8868 -0.2096 0.1383  -0.3308 419 ALA A C   
3231 O O   . ALA A 419 ? 0.7396 0.8300 0.8740 -0.1984 0.1190  -0.3177 419 ALA A O   
3232 C CB  . ALA A 419 ? 0.6685 0.7939 0.8521 -0.1931 0.1139  -0.3058 419 ALA A CB  
3233 N N   . TRP A 420 ? 0.6699 0.7007 0.8610 -0.2180 0.1632  -0.3393 420 TRP A N   
3234 C CA  . TRP A 420 ? 0.7054 0.7049 0.8687 -0.2127 0.1676  -0.3328 420 TRP A CA  
3235 C C   . TRP A 420 ? 0.6625 0.7026 0.8191 -0.2204 0.1581  -0.3591 420 TRP A C   
3236 O O   . TRP A 420 ? 0.6405 0.6685 0.7678 -0.2138 0.1559  -0.3521 420 TRP A O   
3237 C CB  . TRP A 420 ? 0.6747 0.6220 0.8578 -0.2088 0.1945  -0.3185 420 TRP A CB  
3238 C CG  . TRP A 420 ? 0.6564 0.6147 0.8803 -0.2190 0.2111  -0.3405 420 TRP A CG  
3239 C CD1 . TRP A 420 ? 0.6182 0.5940 0.8832 -0.2297 0.2212  -0.3571 420 TRP A CD1 
3240 C CD2 . TRP A 420 ? 0.6428 0.5935 0.8729 -0.2194 0.2214  -0.3490 420 TRP A CD2 
3241 N NE1 . TRP A 420 ? 0.6431 0.6215 0.9379 -0.2369 0.2371  -0.3761 420 TRP A NE1 
3242 C CE2 . TRP A 420 ? 0.6327 0.5958 0.9075 -0.2308 0.2378  -0.3716 420 TRP A CE2 
3243 C CE3 . TRP A 420 ? 0.6306 0.5660 0.8356 -0.2115 0.2194  -0.3408 420 TRP A CE3 
3244 C CZ2 . TRP A 420 ? 0.6543 0.6139 0.9492 -0.2347 0.2524  -0.3867 420 TRP A CZ2 
3245 C CZ3 . TRP A 420 ? 0.6301 0.5638 0.8564 -0.2154 0.2337  -0.3553 420 TRP A CZ3 
3246 C CH2 . TRP A 420 ? 0.6522 0.5973 0.9229 -0.2269 0.2502  -0.3781 420 TRP A CH2 
3247 N N   . GLU A 421 ? 0.6740 0.7640 0.8564 -0.2330 0.1526  -0.3874 421 GLU A N   
3248 C CA  . GLU A 421 ? 0.6686 0.8040 0.8406 -0.2393 0.1420  -0.4112 421 GLU A CA  
3249 C C   . GLU A 421 ? 0.6893 0.8884 0.8407 -0.2410 0.1120  -0.4201 421 GLU A C   
3250 O O   . GLU A 421 ? 0.6915 0.9385 0.8371 -0.2471 0.1017  -0.4410 421 GLU A O   
3251 C CB  . GLU A 421 ? 0.6351 0.7811 0.8511 -0.2517 0.1597  -0.4384 421 GLU A CB  
3252 C CG  . GLU A 421 ? 0.6827 0.7727 0.9203 -0.2488 0.1884  -0.4289 421 GLU A CG  
3253 C CD  . GLU A 421 ? 0.6661 0.7689 0.9445 -0.2611 0.2059  -0.4583 421 GLU A CD  
3254 O OE1 . GLU A 421 ? 0.6831 0.8147 0.9534 -0.2668 0.2017  -0.4798 421 GLU A OE1 
3255 O OE2 . GLU A 421 ? 0.6747 0.7590 0.9930 -0.2652 0.2249  -0.4603 421 GLU A OE2 
3256 N N   . SER A 422 ? 0.7142 0.9168 0.8545 -0.2332 0.0980  -0.4005 422 SER A N   
3257 C CA  . SER A 422 ? 0.7206 0.9848 0.8420 -0.2260 0.0681  -0.3939 422 SER A CA  
3258 C C   . SER A 422 ? 0.7170 0.9944 0.7853 -0.2162 0.0534  -0.3809 422 SER A C   
3259 O O   . SER A 422 ? 0.7248 0.9579 0.7646 -0.2015 0.0581  -0.3496 422 SER A O   
3260 C CB  . SER A 422 ? 0.7542 1.0104 0.8796 -0.2086 0.0608  -0.3585 422 SER A CB  
3261 O OG  . SER A 422 ? 0.8132 1.0641 0.9885 -0.2183 0.0750  -0.3711 422 SER A OG  
3262 N N   . PRO A 423 ? 0.7815 1.1201 0.8344 -0.2243 0.0358  -0.4037 423 PRO A N   
3263 C CA  . PRO A 423 ? 0.7714 1.1222 0.7720 -0.2161 0.0252  -0.3910 423 PRO A CA  
3264 C C   . PRO A 423 ? 0.8350 1.1857 0.8020 -0.1923 0.0073  -0.3426 423 PRO A C   
3265 O O   . PRO A 423 ? 0.8855 1.2229 0.8126 -0.1831 0.0060  -0.3225 423 PRO A O   
3266 C CB  . PRO A 423 ? 0.7294 1.1464 0.7278 -0.2253 0.0125  -0.4171 423 PRO A CB  
3267 C CG  . PRO A 423 ? 0.7239 1.1774 0.7653 -0.2325 0.0041  -0.4332 423 PRO A CG  
3268 C CD  . PRO A 423 ? 0.7357 1.1335 0.8188 -0.2376 0.0269  -0.4351 423 PRO A CD  
3269 N N   . GLU A 424 ? 0.8845 1.2485 0.8695 -0.1821 -0.0048 -0.3237 424 GLU A N   
3270 C CA  . GLU A 424 ? 0.8724 1.2328 0.8310 -0.1591 -0.0200 -0.2786 424 GLU A CA  
3271 C C   . GLU A 424 ? 0.8853 1.1736 0.8402 -0.1467 -0.0041 -0.2485 424 GLU A C   
3272 O O   . GLU A 424 ? 0.9070 1.1827 0.8382 -0.1288 -0.0130 -0.2126 424 GLU A O   
3273 C CB  . GLU A 424 ? 0.8802 1.2865 0.8626 -0.1516 -0.0393 -0.2709 424 GLU A CB  
3274 C CG  . GLU A 424 ? 0.9084 1.2812 0.9317 -0.1481 -0.0268 -0.2644 424 GLU A CG  
3275 C CD  . GLU A 424 ? 0.9327 1.2989 0.9988 -0.1698 -0.0080 -0.3030 424 GLU A CD  
3276 O OE1 . GLU A 424 ? 0.8951 1.2943 0.9664 -0.1883 -0.0086 -0.3394 424 GLU A OE1 
3277 O OE2 . GLU A 424 ? 0.9700 1.2976 1.0650 -0.1687 0.0088  -0.2973 424 GLU A OE2 
3278 N N   . GLY A 425 ? 0.7821 1.0238 0.7600 -0.1556 0.0190  -0.2620 425 GLY A N   
3279 C CA  . GLY A 425 ? 0.7188 0.8961 0.6904 -0.1449 0.0332  -0.2356 425 GLY A CA  
3280 C C   . GLY A 425 ? 0.6924 0.8534 0.6850 -0.1347 0.0342  -0.2172 425 GLY A C   
3281 O O   . GLY A 425 ? 0.7384 0.9382 0.7531 -0.1341 0.0236  -0.2217 425 GLY A O   
3282 N N   . VAL A 426 ? 0.6326 0.7371 0.6186 -0.1266 0.0476  -0.1969 426 VAL A N   
3283 C CA  . VAL A 426 ? 0.6331 0.7154 0.6334 -0.1165 0.0520  -0.1790 426 VAL A CA  
3284 C C   . VAL A 426 ? 0.6510 0.7130 0.6211 -0.0979 0.0424  -0.1453 426 VAL A C   
3285 O O   . VAL A 426 ? 0.6497 0.6904 0.5911 -0.0949 0.0419  -0.1344 426 VAL A O   
3286 C CB  . VAL A 426 ? 0.5797 0.6145 0.5977 -0.1229 0.0765  -0.1841 426 VAL A CB  
3287 C CG1 . VAL A 426 ? 0.5832 0.6370 0.6386 -0.1420 0.0879  -0.2175 426 VAL A CG1 
3288 C CG2 . VAL A 426 ? 0.5920 0.5818 0.5845 -0.1204 0.0855  -0.1735 426 VAL A CG2 
3289 N N   . PRO A 427 ? 0.6317 0.6996 0.6104 -0.0855 0.0358  -0.1292 427 PRO A N   
3290 C CA  . PRO A 427 ? 0.6335 0.6805 0.5882 -0.0684 0.0281  -0.0991 427 PRO A CA  
3291 C C   . PRO A 427 ? 0.6069 0.5956 0.5501 -0.0650 0.0433  -0.0881 427 PRO A C   
3292 O O   . PRO A 427 ? 0.6282 0.5970 0.5881 -0.0663 0.0570  -0.0922 427 PRO A O   
3293 C CB  . PRO A 427 ? 0.6660 0.7406 0.6430 -0.0573 0.0188  -0.0907 427 PRO A CB  
3294 C CG  . PRO A 427 ? 0.7084 0.7951 0.7219 -0.0682 0.0303  -0.1135 427 PRO A CG  
3295 C CD  . PRO A 427 ? 0.6320 0.7299 0.6477 -0.0869 0.0354  -0.1396 427 PRO A CD  
3296 N N   . ILE A 428 ? 0.6199 0.5839 0.5342 -0.0608 0.0408  -0.0738 428 ILE A N   
3297 C CA  . ILE A 428 ? 0.5910 0.5048 0.4915 -0.0574 0.0516  -0.0632 428 ILE A CA  
3298 C C   . ILE A 428 ? 0.6638 0.5615 0.5583 -0.0431 0.0471  -0.0433 428 ILE A C   
3299 O O   . ILE A 428 ? 0.6640 0.5740 0.5497 -0.0349 0.0345  -0.0290 428 ILE A O   
3300 C CB  . ILE A 428 ? 0.6164 0.5143 0.4943 -0.0609 0.0515  -0.0600 428 ILE A CB  
3301 C CG1 . ILE A 428 ? 0.5989 0.5110 0.4860 -0.0747 0.0584  -0.0824 428 ILE A CG1 
3302 C CG2 . ILE A 428 ? 0.5914 0.4431 0.4562 -0.0566 0.0593  -0.0483 428 ILE A CG2 
3303 C CD1 . ILE A 428 ? 0.5586 0.4499 0.4660 -0.0820 0.0757  -0.0954 428 ILE A CD1 
3304 N N   . GLU A 429 ? 0.5993 0.4687 0.4986 -0.0402 0.0587  -0.0422 429 GLU A N   
3305 C CA  . GLU A 429 ? 0.5946 0.4450 0.4892 -0.0276 0.0576  -0.0279 429 GLU A CA  
3306 C C   . GLU A 429 ? 0.6160 0.4233 0.4868 -0.0260 0.0630  -0.0201 429 GLU A C   
3307 O O   . GLU A 429 ? 0.7206 0.5090 0.5858 -0.0171 0.0628  -0.0113 429 GLU A O   
3308 C CB  . GLU A 429 ? 0.6092 0.4663 0.5280 -0.0242 0.0666  -0.0340 429 GLU A CB  
3309 C CG  . GLU A 429 ? 0.6531 0.5579 0.6007 -0.0246 0.0591  -0.0416 429 GLU A CG  
3310 C CD  . GLU A 429 ? 0.6837 0.5966 0.6597 -0.0196 0.0683  -0.0460 429 GLU A CD  
3311 O OE1 . GLU A 429 ? 0.7319 0.6192 0.7035 -0.0095 0.0746  -0.0373 429 GLU A OE1 
3312 O OE2 . GLU A 429 ? 0.7515 0.6976 0.7561 -0.0265 0.0702  -0.0601 429 GLU A OE2 
3313 N N   . GLY A 430 ? 0.6137 0.4063 0.4724 -0.0341 0.0675  -0.0240 430 GLY A N   
3314 C CA  . GLY A 430 ? 0.6432 0.4007 0.4806 -0.0324 0.0701  -0.0166 430 GLY A CA  
3315 C C   . GLY A 430 ? 0.5519 0.3041 0.3813 -0.0397 0.0706  -0.0185 430 GLY A C   
3316 O O   . GLY A 430 ? 0.6258 0.3924 0.4674 -0.0473 0.0756  -0.0293 430 GLY A O   
3317 N N   . ILE A 431 ? 0.5564 0.2884 0.3686 -0.0377 0.0659  -0.0096 431 ILE A N   
3318 C CA  . ILE A 431 ? 0.5735 0.3003 0.3807 -0.0427 0.0659  -0.0097 431 ILE A CA  
3319 C C   . ILE A 431 ? 0.5863 0.2845 0.3794 -0.0400 0.0681  -0.0034 431 ILE A C   
3320 O O   . ILE A 431 ? 0.6182 0.3031 0.3993 -0.0353 0.0630  0.0025  431 ILE A O   
3321 C CB  . ILE A 431 ? 0.6063 0.3460 0.4093 -0.0435 0.0559  -0.0043 431 ILE A CB  
3322 C CG1 . ILE A 431 ? 0.6114 0.3842 0.4234 -0.0457 0.0524  -0.0095 431 ILE A CG1 
3323 C CG2 . ILE A 431 ? 0.6164 0.3505 0.4175 -0.0480 0.0576  -0.0051 431 ILE A CG2 
3324 C CD1 . ILE A 431 ? 0.5626 0.3502 0.3668 -0.0461 0.0442  -0.0015 431 ILE A CD1 
3325 N N   . ILE A 432 ? 0.6164 0.3060 0.4118 -0.0428 0.0754  -0.0048 432 ILE A N   
3326 C CA  . ILE A 432 ? 0.6107 0.2776 0.3922 -0.0393 0.0769  0.0029  432 ILE A CA  
3327 C C   . ILE A 432 ? 0.6166 0.2818 0.3996 -0.0402 0.0723  0.0072  432 ILE A C   
3328 O O   . ILE A 432 ? 0.6152 0.2890 0.4141 -0.0440 0.0778  0.0019  432 ILE A O   
3329 C CB  . ILE A 432 ? 0.6081 0.2644 0.3924 -0.0393 0.0915  0.0025  432 ILE A CB  
3330 C CG1 . ILE A 432 ? 0.5943 0.2577 0.3847 -0.0395 0.0982  -0.0039 432 ILE A CG1 
3331 C CG2 . ILE A 432 ? 0.6189 0.2547 0.3822 -0.0340 0.0914  0.0136  432 ILE A CG2 
3332 C CD1 . ILE A 432 ? 0.6224 0.2783 0.4215 -0.0418 0.1157  -0.0052 432 ILE A CD1 
3333 N N   . PHE A 433 ? 0.6124 0.2681 0.3817 -0.0370 0.0628  0.0147  433 PHE A N   
3334 C CA  . PHE A 433 ? 0.5834 0.2379 0.3561 -0.0364 0.0578  0.0202  433 PHE A CA  
3335 C C   . PHE A 433 ? 0.6654 0.3049 0.4249 -0.0309 0.0578  0.0291  433 PHE A C   
3336 O O   . PHE A 433 ? 0.6683 0.2980 0.4111 -0.0284 0.0608  0.0304  433 PHE A O   
3337 C CB  . PHE A 433 ? 0.5999 0.2603 0.3708 -0.0381 0.0454  0.0219  433 PHE A CB  
3338 C CG  . PHE A 433 ? 0.5797 0.2560 0.3600 -0.0425 0.0455  0.0177  433 PHE A CG  
3339 C CD1 . PHE A 433 ? 0.5808 0.2716 0.3754 -0.0460 0.0517  0.0126  433 PHE A CD1 
3340 C CD2 . PHE A 433 ? 0.5918 0.2690 0.3664 -0.0426 0.0399  0.0192  433 PHE A CD2 
3341 C CE1 . PHE A 433 ? 0.6112 0.3205 0.4092 -0.0500 0.0512  0.0095  433 PHE A CE1 
3342 C CE2 . PHE A 433 ? 0.6781 0.3717 0.4589 -0.0452 0.0394  0.0195  433 PHE A CE2 
3343 C CZ  . PHE A 433 ? 0.5770 0.2884 0.3670 -0.0490 0.0445  0.0148  433 PHE A CZ  
3344 N N   . GLY A 434 ? 0.6467 0.2866 0.4137 -0.0283 0.0546  0.0358  434 GLY A N   
3345 C CA  . GLY A 434 ? 0.6601 0.2903 0.4137 -0.0216 0.0516  0.0476  434 GLY A CA  
3346 C C   . GLY A 434 ? 0.6590 0.2898 0.4322 -0.0170 0.0549  0.0563  434 GLY A C   
3347 O O   . GLY A 434 ? 0.6606 0.2950 0.4581 -0.0196 0.0645  0.0507  434 GLY A O   
3348 N N   . GLY A 435 ? 0.7182 0.3467 0.4810 -0.0097 0.0465  0.0696  435 GLY A N   
3349 C CA  . GLY A 435 ? 0.6727 0.3013 0.4558 -0.0023 0.0488  0.0817  435 GLY A CA  
3350 C C   . GLY A 435 ? 0.7012 0.3246 0.4643 0.0078  0.0430  0.1006  435 GLY A C   
3351 O O   . GLY A 435 ? 0.7574 0.3733 0.4897 0.0083  0.0435  0.1034  435 GLY A O   
3352 N N   . ARG A 436 ? 0.7038 0.3331 0.4845 0.0166  0.0376  0.1142  436 ARG A N   
3353 C CA  . ARG A 436 ? 0.7675 0.3963 0.5307 0.0285  0.0300  0.1364  436 ARG A CA  
3354 C C   . ARG A 436 ? 0.7752 0.4251 0.5218 0.0286  0.0046  0.1352  436 ARG A C   
3355 O O   . ARG A 436 ? 0.8038 0.4710 0.5753 0.0306  -0.0071 0.1357  436 ARG A O   
3356 C CB  . ARG A 436 ? 0.8035 0.4277 0.5990 0.0400  0.0383  0.1544  436 ARG A CB  
3357 C CG  . ARG A 436 ? 0.8034 0.4033 0.6147 0.0398  0.0649  0.1569  436 ARG A CG  
3358 C CD  . ARG A 436 ? 0.7679 0.3608 0.6192 0.0509  0.0749  0.1720  436 ARG A CD  
3359 N NE  . ARG A 436 ? 0.8385 0.4139 0.7136 0.0470  0.0998  0.1669  436 ARG A NE  
3360 C CZ  . ARG A 436 ? 0.8248 0.3947 0.7004 0.0515  0.1090  0.1811  436 ARG A CZ  
3361 N NH1 . ARG A 436 ? 0.7509 0.3228 0.6000 0.0625  0.0987  0.2069  436 ARG A NH1 
3362 N NH2 . ARG A 436 ? 0.8287 0.3920 0.7308 0.0445  0.1291  0.1691  436 ARG A NH2 
3363 N N   . ARG A 437 ? 0.7574 0.4072 0.4645 0.0257  -0.0030 0.1314  437 ARG A N   
3364 C CA  . ARG A 437 ? 0.8350 0.5046 0.5229 0.0247  -0.0269 0.1278  437 ARG A CA  
3365 C C   . ARG A 437 ? 0.8793 0.5506 0.5281 0.0338  -0.0328 0.1444  437 ARG A C   
3366 O O   . ARG A 437 ? 0.8603 0.5192 0.4750 0.0311  -0.0239 0.1405  437 ARG A O   
3367 C CB  . ARG A 437 ? 0.7295 0.3987 0.4053 0.0114  -0.0310 0.1035  437 ARG A CB  
3368 C CG  . ARG A 437 ? 0.7509 0.4223 0.4608 0.0026  -0.0277 0.0899  437 ARG A CG  
3369 C CD  . ARG A 437 ? 0.7581 0.4502 0.4995 0.0045  -0.0404 0.0939  437 ARG A CD  
3370 N NE  . ARG A 437 ? 0.7136 0.4249 0.4448 0.0021  -0.0630 0.0896  437 ARG A NE  
3371 C CZ  . ARG A 437 ? 0.7307 0.4489 0.4679 -0.0096 -0.0716 0.0724  437 ARG A CZ  
3372 N NH1 . ARG A 437 ? 0.6610 0.3679 0.4097 -0.0185 -0.0600 0.0609  437 ARG A NH1 
3373 N NH2 . ARG A 437 ? 0.6798 0.4177 0.4125 -0.0125 -0.0924 0.0671  437 ARG A NH2 
3374 N N   . PRO A 438 ? 0.8727 0.5610 0.5244 0.0454  -0.0471 0.1641  438 PRO A N   
3375 C CA  . PRO A 438 ? 0.9506 0.6433 0.5605 0.0554  -0.0530 0.1836  438 PRO A CA  
3376 C C   . PRO A 438 ? 0.9226 0.6308 0.4889 0.0483  -0.0707 0.1676  438 PRO A C   
3377 O O   . PRO A 438 ? 0.9715 0.6836 0.4945 0.0547  -0.0735 0.1801  438 PRO A O   
3378 C CB  . PRO A 438 ? 0.9270 0.6383 0.5598 0.0705  -0.0662 0.2090  438 PRO A CB  
3379 C CG  . PRO A 438 ? 0.8357 0.5630 0.5137 0.0645  -0.0766 0.1934  438 PRO A CG  
3380 C CD  . PRO A 438 ? 0.7959 0.5014 0.4907 0.0511  -0.0570 0.1712  438 PRO A CD  
3381 N N   . ALA A 439 ? 0.8605 0.5770 0.4364 0.0351  -0.0812 0.1404  439 ALA A N   
3382 C CA  . ALA A 439 ? 0.9057 0.6364 0.4457 0.0273  -0.0978 0.1216  439 ALA A CA  
3383 C C   . ALA A 439 ? 0.8638 0.5852 0.4175 0.0114  -0.0948 0.0911  439 ALA A C   
3384 O O   . ALA A 439 ? 0.8772 0.5941 0.4718 0.0066  -0.0899 0.0861  439 ALA A O   
3385 C CB  . ALA A 439 ? 0.8536 0.6207 0.3940 0.0312  -0.1275 0.1262  439 ALA A CB  
3386 N N   . GLY A 440 ? 0.8429 0.5614 0.3619 0.0038  -0.0966 0.0717  440 GLY A N   
3387 C CA  . GLY A 440 ? 0.8548 0.5651 0.3855 -0.0105 -0.0960 0.0431  440 GLY A CA  
3388 C C   . GLY A 440 ? 0.8705 0.5524 0.4089 -0.0145 -0.0725 0.0351  440 GLY A C   
3389 O O   . GLY A 440 ? 0.8940 0.5650 0.4170 -0.0217 -0.0677 0.0150  440 GLY A O   
3390 N N   . VAL A 441 ? 0.8631 0.5343 0.4273 -0.0099 -0.0579 0.0494  441 VAL A N   
3391 C CA  . VAL A 441 ? 0.8344 0.4849 0.4116 -0.0140 -0.0384 0.0417  441 VAL A CA  
3392 C C   . VAL A 441 ? 0.8727 0.5090 0.4192 -0.0096 -0.0215 0.0447  441 VAL A C   
3393 O O   . VAL A 441 ? 0.8743 0.5100 0.4088 -0.0011 -0.0149 0.0640  441 VAL A O   
3394 C CB  . VAL A 441 ? 0.7448 0.3935 0.3603 -0.0122 -0.0299 0.0522  441 VAL A CB  
3395 C CG1 . VAL A 441 ? 0.7403 0.3737 0.3679 -0.0165 -0.0127 0.0439  441 VAL A CG1 
3396 C CG2 . VAL A 441 ? 0.7248 0.3896 0.3706 -0.0164 -0.0445 0.0498  441 VAL A CG2 
3397 N N   . PRO A 442 ? 0.8993 0.5236 0.4354 -0.0147 -0.0123 0.0275  442 PRO A N   
3398 C CA  . PRO A 442 ? 0.8844 0.4972 0.3935 -0.0110 0.0057  0.0291  442 PRO A CA  
3399 C C   . PRO A 442 ? 0.8059 0.4086 0.3363 -0.0077 0.0253  0.0413  442 PRO A C   
3400 O O   . PRO A 442 ? 0.7873 0.3915 0.3519 -0.0088 0.0250  0.0459  442 PRO A O   
3401 C CB  . PRO A 442 ? 0.9367 0.5409 0.4393 -0.0173 0.0093  0.0046  442 PRO A CB  
3402 C CG  . PRO A 442 ? 0.8327 0.4371 0.3718 -0.0237 0.0007  -0.0039 442 PRO A CG  
3403 C CD  . PRO A 442 ? 0.8127 0.4330 0.3638 -0.0237 -0.0168 0.0066  442 PRO A CD  
3404 N N   . LEU A 443 ? 0.8959 0.4896 0.4066 -0.0048 0.0434  0.0447  443 LEU A N   
3405 C CA  . LEU A 443 ? 0.7965 0.3820 0.3277 -0.0028 0.0631  0.0558  443 LEU A CA  
3406 C C   . LEU A 443 ? 0.7831 0.3671 0.3516 -0.0081 0.0679  0.0439  443 LEU A C   
3407 O O   . LEU A 443 ? 0.8157 0.4004 0.4133 -0.0087 0.0733  0.0505  443 LEU A O   
3408 C CB  . LEU A 443 ? 0.8178 0.3953 0.3224 -0.0003 0.0830  0.0592  443 LEU A CB  
3409 C CG  . LEU A 443 ? 0.8553 0.4245 0.3849 -0.0010 0.1061  0.0652  443 LEU A CG  
3410 C CD1 . LEU A 443 ? 0.8439 0.4103 0.3924 0.0022  0.1092  0.0859  443 LEU A CD1 
3411 C CD2 . LEU A 443 ? 0.9684 0.5314 0.4721 0.0003  0.1268  0.0660  443 LEU A CD2 
3412 N N   . VAL A 444 ? 0.7357 0.3183 0.3041 -0.0117 0.0665  0.0264  444 VAL A N   
3413 C CA  . VAL A 444 ? 0.7553 0.3388 0.3563 -0.0149 0.0706  0.0179  444 VAL A CA  
3414 C C   . VAL A 444 ? 0.7748 0.3560 0.3750 -0.0174 0.0620  0.0022  444 VAL A C   
3415 O O   . VAL A 444 ? 0.7681 0.3439 0.3430 -0.0170 0.0620  -0.0074 444 VAL A O   
3416 C CB  . VAL A 444 ? 0.7396 0.3206 0.3507 -0.0141 0.0915  0.0177  444 VAL A CB  
3417 C CG1 . VAL A 444 ? 0.8023 0.3768 0.3884 -0.0120 0.1024  0.0094  444 VAL A CG1 
3418 C CG2 . VAL A 444 ? 0.6446 0.2331 0.2907 -0.0167 0.0928  0.0110  444 VAL A CG2 
3419 N N   . TYR A 445 ? 0.7129 0.2980 0.3409 -0.0202 0.0558  -0.0005 445 TYR A N   
3420 C CA  . TYR A 445 ? 0.7178 0.2974 0.3533 -0.0218 0.0519  -0.0127 445 TYR A CA  
3421 C C   . TYR A 445 ? 0.6964 0.2823 0.3638 -0.0220 0.0530  -0.0096 445 TYR A C   
3422 O O   . TYR A 445 ? 0.6717 0.2682 0.3532 -0.0229 0.0534  -0.0011 445 TYR A O   
3423 C CB  . TYR A 445 ? 0.7534 0.3311 0.3807 -0.0263 0.0359  -0.0187 445 TYR A CB  
3424 C CG  . TYR A 445 ? 0.7132 0.3009 0.3569 -0.0299 0.0234  -0.0099 445 TYR A CG  
3425 C CD1 . TYR A 445 ? 0.7965 0.3855 0.4661 -0.0334 0.0193  -0.0097 445 TYR A CD1 
3426 C CD2 . TYR A 445 ? 0.7125 0.3089 0.3468 -0.0290 0.0164  -0.0006 445 TYR A CD2 
3427 C CE1 . TYR A 445 ? 0.7565 0.3560 0.4414 -0.0371 0.0102  -0.0024 445 TYR A CE1 
3428 C CE2 . TYR A 445 ? 0.6553 0.2622 0.3085 -0.0317 0.0065  0.0063  445 TYR A CE2 
3429 C CZ  . TYR A 445 ? 0.7532 0.3619 0.4312 -0.0363 0.0040  0.0042  445 TYR A CZ  
3430 O OH  . TYR A 445 ? 0.7138 0.3341 0.4108 -0.0394 -0.0034 0.0104  445 TYR A OH  
3431 N N   . GLU A 446 ? 0.7396 0.3196 0.4184 -0.0208 0.0541  -0.0168 446 GLU A N   
3432 C CA  . GLU A 446 ? 0.7245 0.3124 0.4309 -0.0189 0.0550  -0.0120 446 GLU A CA  
3433 C C   . GLU A 446 ? 0.7049 0.2879 0.4234 -0.0217 0.0449  -0.0106 446 GLU A C   
3434 O O   . GLU A 446 ? 0.7078 0.2760 0.4203 -0.0234 0.0423  -0.0196 446 GLU A O   
3435 C CB  . GLU A 446 ? 0.6938 0.2807 0.4100 -0.0126 0.0669  -0.0172 446 GLU A CB  
3436 C CG  . GLU A 446 ? 0.7370 0.3344 0.4816 -0.0086 0.0655  -0.0110 446 GLU A CG  
3437 C CD  . GLU A 446 ? 0.7287 0.3275 0.4875 -0.0007 0.0765  -0.0159 446 GLU A CD  
3438 O OE1 . GLU A 446 ? 0.7463 0.3456 0.4966 0.0002  0.0879  -0.0224 446 GLU A OE1 
3439 O OE2 . GLU A 446 ? 0.7100 0.3097 0.4901 0.0052  0.0748  -0.0120 446 GLU A OE2 
3440 N N   . ALA A 447 ? 0.7061 0.3018 0.4418 -0.0228 0.0407  -0.0003 447 ALA A N   
3441 C CA  . ALA A 447 ? 0.6856 0.2779 0.4342 -0.0259 0.0335  0.0049  447 ALA A CA  
3442 C C   . ALA A 447 ? 0.7066 0.2868 0.4697 -0.0204 0.0375  0.0044  447 ALA A C   
3443 O O   . ALA A 447 ? 0.7432 0.3271 0.5132 -0.0130 0.0447  0.0042  447 ALA A O   
3444 C CB  . ALA A 447 ? 0.6307 0.2424 0.3906 -0.0279 0.0303  0.0168  447 ALA A CB  
3445 N N   . LEU A 448 ? 0.7122 0.2781 0.4840 -0.0242 0.0336  0.0046  448 LEU A N   
3446 C CA  . LEU A 448 ? 0.7193 0.2681 0.5088 -0.0190 0.0389  0.0044  448 LEU A CA  
3447 C C   . LEU A 448 ? 0.7238 0.2837 0.5337 -0.0122 0.0395  0.0238  448 LEU A C   
3448 O O   . LEU A 448 ? 0.6907 0.2423 0.5175 -0.0031 0.0452  0.0274  448 LEU A O   
3449 C CB  . LEU A 448 ? 0.6501 0.1778 0.4455 -0.0270 0.0359  -0.0034 448 LEU A CB  
3450 C CG  . LEU A 448 ? 0.7777 0.2987 0.5516 -0.0346 0.0320  -0.0234 448 LEU A CG  
3451 C CD1 . LEU A 448 ? 0.8355 0.3381 0.6211 -0.0440 0.0287  -0.0340 448 LEU A CD1 
3452 C CD2 . LEU A 448 ? 0.7976 0.3127 0.5558 -0.0284 0.0405  -0.0376 448 LEU A CD2 
3453 N N   . SER A 449 ? 0.7065 0.2864 0.5151 -0.0158 0.0340  0.0365  449 SER A N   
3454 C CA  . SER A 449 ? 0.6782 0.2737 0.5004 -0.0101 0.0331  0.0560  449 SER A CA  
3455 C C   . SER A 449 ? 0.6695 0.2925 0.4813 -0.0152 0.0286  0.0612  449 SER A C   
3456 O O   . SER A 449 ? 0.6141 0.2405 0.4130 -0.0219 0.0273  0.0508  449 SER A O   
3457 C CB  . SER A 449 ? 0.7305 0.3085 0.5691 -0.0111 0.0339  0.0687  449 SER A CB  
3458 O OG  . SER A 449 ? 0.7167 0.2918 0.5509 -0.0231 0.0306  0.0675  449 SER A OG  
3459 N N   . TRP A 450 ? 0.7022 0.3455 0.5198 -0.0115 0.0268  0.0776  450 TRP A N   
3460 C CA  . TRP A 450 ? 0.7015 0.3719 0.5093 -0.0172 0.0240  0.0802  450 TRP A CA  
3461 C C   . TRP A 450 ? 0.6888 0.3525 0.4935 -0.0273 0.0235  0.0815  450 TRP A C   
3462 O O   . TRP A 450 ? 0.6609 0.3357 0.4576 -0.0337 0.0231  0.0733  450 TRP A O   
3463 C CB  . TRP A 450 ? 0.6576 0.3548 0.4687 -0.0109 0.0213  0.0968  450 TRP A CB  
3464 C CG  . TRP A 450 ? 0.7026 0.4298 0.5020 -0.0173 0.0196  0.0960  450 TRP A CG  
3465 C CD1 . TRP A 450 ? 0.7042 0.4435 0.4980 -0.0218 0.0197  0.1086  450 TRP A CD1 
3466 C CD2 . TRP A 450 ? 0.7320 0.4802 0.5254 -0.0208 0.0197  0.0801  450 TRP A CD2 
3467 N NE1 . TRP A 450 ? 0.7110 0.4786 0.4942 -0.0274 0.0197  0.0996  450 TRP A NE1 
3468 C CE2 . TRP A 450 ? 0.6850 0.4574 0.4695 -0.0272 0.0195  0.0816  450 TRP A CE2 
3469 C CE3 . TRP A 450 ? 0.6490 0.3971 0.4453 -0.0197 0.0218  0.0644  450 TRP A CE3 
3470 C CZ2 . TRP A 450 ? 0.6628 0.4576 0.4431 -0.0326 0.0211  0.0658  450 TRP A CZ2 
3471 C CZ3 . TRP A 450 ? 0.6276 0.3972 0.4212 -0.0254 0.0234  0.0513  450 TRP A CZ3 
3472 C CH2 . TRP A 450 ? 0.6802 0.4721 0.4667 -0.0318 0.0229  0.0509  450 TRP A CH2 
3473 N N   . GLN A 451 ? 0.6859 0.3314 0.5010 -0.0288 0.0247  0.0915  451 GLN A N   
3474 C CA  . GLN A 451 ? 0.6733 0.3142 0.4910 -0.0394 0.0249  0.0924  451 GLN A CA  
3475 C C   . GLN A 451 ? 0.6286 0.2588 0.4419 -0.0457 0.0219  0.0733  451 GLN A C   
3476 O O   . GLN A 451 ? 0.6838 0.3250 0.4950 -0.0525 0.0203  0.0696  451 GLN A O   
3477 C CB  . GLN A 451 ? 0.6938 0.3146 0.5283 -0.0408 0.0284  0.1063  451 GLN A CB  
3478 C CG  . GLN A 451 ? 0.7780 0.4112 0.6156 -0.0343 0.0315  0.1314  451 GLN A CG  
3479 C CD  . GLN A 451 ? 0.8448 0.4793 0.6850 -0.0203 0.0304  0.1377  451 GLN A CD  
3480 O OE1 . GLN A 451 ? 0.7965 0.4121 0.6431 -0.0159 0.0308  0.1250  451 GLN A OE1 
3481 N NE2 . GLN A 451 ? 0.8506 0.5104 0.6860 -0.0130 0.0289  0.1569  451 GLN A NE2 
3482 N N   . HIS A 452 ? 0.6569 0.2678 0.4686 -0.0428 0.0212  0.0613  452 HIS A N   
3483 C CA  . HIS A 452 ? 0.6546 0.2593 0.4566 -0.0474 0.0172  0.0446  452 HIS A CA  
3484 C C   . HIS A 452 ? 0.6495 0.2724 0.4381 -0.0456 0.0168  0.0405  452 HIS A C   
3485 O O   . HIS A 452 ? 0.6011 0.2282 0.3849 -0.0500 0.0131  0.0348  452 HIS A O   
3486 C CB  . HIS A 452 ? 0.7074 0.2899 0.5061 -0.0443 0.0183  0.0319  452 HIS A CB  
3487 C CG  . HIS A 452 ? 0.6754 0.2538 0.4590 -0.0485 0.0134  0.0159  452 HIS A CG  
3488 N ND1 . HIS A 452 ? 0.6493 0.2232 0.4158 -0.0434 0.0159  0.0053  452 HIS A ND1 
3489 C CD2 . HIS A 452 ? 0.6345 0.2156 0.4175 -0.0568 0.0057  0.0100  452 HIS A CD2 
3490 C CE1 . HIS A 452 ? 0.7118 0.2855 0.4639 -0.0479 0.0097  -0.0049 452 HIS A CE1 
3491 N NE2 . HIS A 452 ? 0.6708 0.2500 0.4337 -0.0558 0.0022  -0.0026 452 HIS A NE2 
3492 N N   . GLY A 453 ? 0.6403 0.2748 0.4260 -0.0391 0.0207  0.0435  453 GLY A N   
3493 C CA  . GLY A 453 ? 0.6015 0.2514 0.3793 -0.0388 0.0226  0.0385  453 GLY A CA  
3494 C C   . GLY A 453 ? 0.6339 0.3008 0.4151 -0.0443 0.0221  0.0418  453 GLY A C   
3495 O O   . GLY A 453 ? 0.6012 0.2711 0.3798 -0.0464 0.0225  0.0361  453 GLY A O   
3496 N N   . VAL A 454 ? 0.6256 0.3039 0.4133 -0.0461 0.0226  0.0522  454 VAL A N   
3497 C CA  . VAL A 454 ? 0.6081 0.3030 0.3994 -0.0520 0.0243  0.0544  454 VAL A CA  
3498 C C   . VAL A 454 ? 0.6156 0.3009 0.4134 -0.0573 0.0212  0.0512  454 VAL A C   
3499 O O   . VAL A 454 ? 0.6144 0.3103 0.4165 -0.0599 0.0227  0.0472  454 VAL A O   
3500 C CB  . VAL A 454 ? 0.6539 0.3618 0.4476 -0.0529 0.0264  0.0685  454 VAL A CB  
3501 C CG1 . VAL A 454 ? 0.5901 0.3154 0.3869 -0.0597 0.0307  0.0696  454 VAL A CG1 
3502 C CG2 . VAL A 454 ? 0.6310 0.3557 0.4181 -0.0469 0.0267  0.0718  454 VAL A CG2 
3503 N N   . PHE A 455 ? 0.6131 0.2798 0.4147 -0.0588 0.0168  0.0515  455 PHE A N   
3504 C CA  . PHE A 455 ? 0.6170 0.2789 0.4261 -0.0645 0.0113  0.0462  455 PHE A CA  
3505 C C   . PHE A 455 ? 0.6034 0.2647 0.4027 -0.0612 0.0074  0.0370  455 PHE A C   
3506 O O   . PHE A 455 ? 0.6659 0.3348 0.4723 -0.0635 0.0032  0.0351  455 PHE A O   
3507 C CB  . PHE A 455 ? 0.6031 0.2453 0.4189 -0.0683 0.0075  0.0445  455 PHE A CB  
3508 C CG  . PHE A 455 ? 0.6437 0.2828 0.4638 -0.0738 -0.0013 0.0341  455 PHE A CG  
3509 C CD1 . PHE A 455 ? 0.6407 0.2902 0.4804 -0.0820 -0.0038 0.0357  455 PHE A CD1 
3510 C CD2 . PHE A 455 ? 0.6717 0.3013 0.4762 -0.0708 -0.0072 0.0226  455 PHE A CD2 
3511 C CE1 . PHE A 455 ? 0.6453 0.2976 0.4913 -0.0870 -0.0143 0.0257  455 PHE A CE1 
3512 C CE2 . PHE A 455 ? 0.6630 0.2950 0.4684 -0.0755 -0.0176 0.0133  455 PHE A CE2 
3513 C CZ  . PHE A 455 ? 0.6804 0.3249 0.5079 -0.0835 -0.0224 0.0145  455 PHE A CZ  
3514 N N   . VAL A 456 ? 0.6167 0.2700 0.4015 -0.0551 0.0093  0.0328  456 VAL A N   
3515 C CA  . VAL A 456 ? 0.6153 0.2664 0.3887 -0.0514 0.0078  0.0275  456 VAL A CA  
3516 C C   . VAL A 456 ? 0.6410 0.3066 0.4214 -0.0504 0.0125  0.0298  456 VAL A C   
3517 O O   . VAL A 456 ? 0.6495 0.3172 0.4313 -0.0488 0.0095  0.0300  456 VAL A O   
3518 C CB  . VAL A 456 ? 0.6594 0.2995 0.4178 -0.0459 0.0124  0.0232  456 VAL A CB  
3519 C CG1 . VAL A 456 ? 0.6536 0.2930 0.4004 -0.0418 0.0150  0.0217  456 VAL A CG1 
3520 C CG2 . VAL A 456 ? 0.6036 0.2269 0.3555 -0.0465 0.0086  0.0173  456 VAL A CG2 
3521 N N   . GLY A 457 ? 0.6128 0.2898 0.3987 -0.0509 0.0200  0.0312  457 GLY A N   
3522 C CA  . GLY A 457 ? 0.6113 0.3018 0.4067 -0.0513 0.0264  0.0295  457 GLY A CA  
3523 C C   . GLY A 457 ? 0.6206 0.3202 0.4311 -0.0547 0.0241  0.0320  457 GLY A C   
3524 O O   . GLY A 457 ? 0.5780 0.2819 0.3985 -0.0526 0.0265  0.0308  457 GLY A O   
3525 N N   . ALA A 458 ? 0.5591 0.2615 0.3750 -0.0596 0.0207  0.0363  458 ALA A N   
3526 C CA  . ALA A 458 ? 0.5632 0.2769 0.3975 -0.0641 0.0201  0.0386  458 ALA A CA  
3527 C C   . ALA A 458 ? 0.5730 0.2834 0.4148 -0.0627 0.0102  0.0375  458 ALA A C   
3528 O O   . ALA A 458 ? 0.5808 0.3042 0.4422 -0.0636 0.0101  0.0382  458 ALA A O   
3529 C CB  . ALA A 458 ? 0.5802 0.2955 0.4197 -0.0706 0.0205  0.0450  458 ALA A CB  
3530 N N   . ALA A 459 ? 0.6050 0.3010 0.4318 -0.0602 0.0018  0.0354  459 ALA A N   
3531 C CA  . ALA A 459 ? 0.5871 0.2837 0.4158 -0.0591 -0.0102 0.0342  459 ALA A CA  
3532 C C   . ALA A 459 ? 0.5654 0.2609 0.3856 -0.0500 -0.0105 0.0367  459 ALA A C   
3533 O O   . ALA A 459 ? 0.6347 0.3314 0.4492 -0.0470 -0.0217 0.0377  459 ALA A O   
3534 C CB  . ALA A 459 ? 0.5853 0.2684 0.4006 -0.0626 -0.0189 0.0285  459 ALA A CB  
3535 N N   . MET A 460 ? 0.5224 0.2164 0.3419 -0.0459 0.0017  0.0378  460 MET A N   
3536 C CA  . MET A 460 ? 0.5992 0.2877 0.4132 -0.0376 0.0048  0.0420  460 MET A CA  
3537 C C   . MET A 460 ? 0.5875 0.2872 0.4206 -0.0324 -0.0008 0.0488  460 MET A C   
3538 O O   . MET A 460 ? 0.6008 0.3142 0.4594 -0.0344 0.0017  0.0481  460 MET A O   
3539 C CB  . MET A 460 ? 0.5299 0.2156 0.3475 -0.0367 0.0205  0.0391  460 MET A CB  
3540 C CG  . MET A 460 ? 0.5842 0.2603 0.3832 -0.0384 0.0253  0.0345  460 MET A CG  
3541 S SD  . MET A 460 ? 0.5869 0.2684 0.3965 -0.0403 0.0415  0.0271  460 MET A SD  
3542 C CE  . MET A 460 ? 0.5150 0.1869 0.3348 -0.0335 0.0500  0.0317  460 MET A CE  
3543 N N   . ARG A 461 ? 0.5876 0.2828 0.4084 -0.0248 -0.0079 0.0563  461 ARG A N   
3544 C CA  . ARG A 461 ? 0.6349 0.3412 0.4734 -0.0164 -0.0141 0.0667  461 ARG A CA  
3545 C C   . ARG A 461 ? 0.7076 0.4008 0.5337 -0.0060 -0.0078 0.0782  461 ARG A C   
3546 O O   . ARG A 461 ? 0.7334 0.4123 0.5310 -0.0061 -0.0047 0.0779  461 ARG A O   
3547 C CB  . ARG A 461 ? 0.6162 0.3376 0.4531 -0.0177 -0.0349 0.0675  461 ARG A CB  
3548 C CG  . ARG A 461 ? 0.6476 0.3812 0.5032 -0.0290 -0.0394 0.0575  461 ARG A CG  
3549 C CD  . ARG A 461 ? 0.6182 0.3655 0.4718 -0.0330 -0.0600 0.0540  461 ARG A CD  
3550 N NE  . ARG A 461 ? 0.6286 0.3986 0.5046 -0.0253 -0.0718 0.0630  461 ARG A NE  
3551 C CZ  . ARG A 461 ? 0.6216 0.4094 0.4948 -0.0255 -0.0927 0.0623  461 ARG A CZ  
3552 N NH1 . ARG A 461 ? 0.6440 0.4274 0.4915 -0.0338 -0.1029 0.0505  461 ARG A NH1 
3553 N NH2 . ARG A 461 ? 0.7004 0.5128 0.5989 -0.0169 -0.1037 0.0724  461 ARG A NH2 
3554 N N   . SER A 462 ? 0.7189 0.4163 0.5694 0.0034  -0.0040 0.0891  462 SER A N   
3555 C CA  . SER A 462 ? 0.7381 0.4199 0.5836 0.0136  0.0062  0.1026  462 SER A CA  
3556 C C   . SER A 462 ? 0.7714 0.4622 0.6459 0.0265  0.0034  0.1188  462 SER A C   
3557 O O   . SER A 462 ? 0.7455 0.4538 0.6512 0.0265  -0.0008 0.1156  462 SER A O   
3558 C CB  . SER A 462 ? 0.6877 0.3531 0.5408 0.0092  0.0287  0.0939  462 SER A CB  
3559 O OG  . SER A 462 ? 0.7585 0.4069 0.6132 0.0180  0.0410  0.1072  462 SER A OG  
3560 N N   . GLU A 463 ? 0.7971 0.4760 0.6626 0.0381  0.0069  0.1378  463 GLU A N   
3561 C CA  . GLU A 463 ? 0.8631 0.5467 0.7587 0.0533  0.0068  0.1574  463 GLU A CA  
3562 C C   . GLU A 463 ? 0.7934 0.4659 0.7311 0.0539  0.0296  0.1508  463 GLU A C   
3563 O O   . GLU A 463 ? 0.7263 0.3821 0.6623 0.0448  0.0477  0.1365  463 GLU A O   
3564 C CB  . GLU A 463 ? 0.9021 0.5735 0.7749 0.0661  0.0067  0.1828  463 GLU A CB  
3565 C CG  . GLU A 463 ? 0.9501 0.6393 0.7848 0.0695  -0.0183 0.1925  463 GLU A CG  
3566 C CD  . GLU A 463 ? 1.1142 0.7959 0.9282 0.0850  -0.0183 0.2228  463 GLU A CD  
3567 O OE1 . GLU A 463 ? 1.0591 0.7153 0.8854 0.0910  0.0042  0.2353  463 GLU A OE1 
3568 O OE2 . GLU A 463 ? 1.1005 0.8023 0.8859 0.0908  -0.0403 0.2341  463 GLU A OE2 
3569 N N   . ALA A 464 ? 0.9178 0.6020 0.8955 0.0648  0.0285  0.1601  464 ALA A N   
3570 C CA  . ALA A 464 ? 0.9705 0.6454 0.9925 0.0666  0.0510  0.1522  464 ALA A CA  
3571 C C   . ALA A 464 ? 0.9959 0.6405 1.0257 0.0751  0.0712  0.1656  464 ALA A C   
3572 O O   . ALA A 464 ? 0.9967 0.6331 1.0109 0.0871  0.0657  0.1915  464 ALA A O   
3573 C CB  . ALA A 464 ? 0.9949 0.6921 1.0615 0.0772  0.0447  0.1584  464 ALA A CB  
3574 N N   . THR A 465 ? 1.0126 0.6413 1.0668 0.0682  0.0956  0.1475  465 THR A N   
3575 C CA  . THR A 465 ? 1.0516 0.6492 1.1204 0.0723  0.1190  0.1545  465 THR A CA  
3576 C C   . THR A 465 ? 1.0932 0.6915 1.2169 0.0776  0.1361  0.1459  465 THR A C   
3577 O O   . THR A 465 ? 1.0265 0.6377 1.1795 0.0824  0.1337  0.1423  465 THR A O   
3578 C CB  . THR A 465 ? 0.9960 0.5847 1.0406 0.0545  0.1298  0.1320  465 THR A CB  
3579 O OG1 . THR A 465 ? 0.9653 0.5625 1.0215 0.0411  0.1371  0.1021  465 THR A OG1 
3580 C CG2 . THR A 465 ? 0.9598 0.5493 0.9522 0.0504  0.1141  0.1396  465 THR A CG2 
3581 N N   . ALA A 466 ? 1.0585 0.6458 1.1977 0.0757  0.1541  0.1408  466 ALA A N   
3582 C CA  . ALA A 466 ? 1.0915 0.6775 1.2820 0.0811  0.1724  0.1335  466 ALA A CA  
3583 C C   . ALA A 466 ? 1.0447 0.6326 1.2537 0.0647  0.1917  0.0957  466 ALA A C   
3584 O O   . ALA A 466 ? 0.9771 0.5638 1.2277 0.0663  0.2102  0.0845  466 ALA A O   
3585 C CB  . ALA A 466 ? 0.9474 0.5200 1.1484 0.0889  0.1825  0.1515  466 ALA A CB  
3586 N N   . ALA A 467 ? 1.1776 0.7701 1.3564 0.0491  0.1879  0.0756  467 ALA A N   
3587 C CA  . ALA A 467 ? 1.0078 0.6066 1.1984 0.0331  0.2039  0.0396  467 ALA A CA  
3588 C C   . ALA A 467 ? 0.9418 0.5526 1.1588 0.0339  0.2086  0.0247  467 ALA A C   
3589 O O   . ALA A 467 ? 0.8429 0.4601 1.0813 0.0244  0.2263  -0.0040 467 ALA A O   
3590 C CB  . ALA A 467 ? 0.8851 0.4870 1.0338 0.0171  0.1973  0.0251  467 ALA A CB  
3591 N N   . ALA A 468 ? 0.9796 0.5956 1.1968 0.0445  0.1937  0.0426  468 ALA A N   
3592 C CA  . ALA A 468 ? 0.9427 0.5792 1.1882 0.0462  0.1966  0.0306  468 ALA A CA  
3593 C C   . ALA A 468 ? 1.0003 0.6366 1.2881 0.0678  0.1945  0.0555  468 ALA A C   
3594 O O   . ALA A 468 ? 1.0039 0.6275 1.3042 0.0789  0.1974  0.0742  468 ALA A O   
3595 C CB  . ALA A 468 ? 0.9877 0.6546 1.1968 0.0362  0.1752  0.0265  468 ALA A CB  
3596 N N   . GLU A 469 ? 1.0069 0.6724 1.3112 0.0718  0.1850  0.0555  469 GLU A N   
3597 C CA  . GLU A 469 ? 1.0356 0.7088 1.3841 0.0929  0.1804  0.0785  469 GLU A CA  
3598 C C   . GLU A 469 ? 1.0849 0.7789 1.4106 0.1010  0.1475  0.1070  469 GLU A C   
3599 O O   . GLU A 469 ? 1.0429 0.7508 1.4032 0.1188  0.1384  0.1279  469 GLU A O   
3600 C CB  . GLU A 469 ? 1.0317 0.7268 1.4251 0.0931  0.1944  0.0583  469 GLU A CB  
3601 C CG  . GLU A 469 ? 0.9735 0.7048 1.3467 0.0806  0.1797  0.0471  469 GLU A CG  
3602 C CD  . GLU A 469 ? 0.9599 0.6936 1.2985 0.0579  0.1905  0.0158  469 GLU A CD  
3603 O OE1 . GLU A 469 ? 0.9238 0.6372 1.2268 0.0487  0.1919  0.0106  469 GLU A OE1 
3604 O OE2 . GLU A 469 ? 0.9381 0.6960 1.2857 0.0495  0.1979  -0.0027 469 GLU A OE2 
3605 N N   . HIS A 470 ? 1.1991 0.8969 1.4696 0.0886  0.1295  0.1072  470 HIS A N   
3606 C CA  . HIS A 470 ? 1.2160 0.9342 1.4618 0.0934  0.0986  0.1286  470 HIS A CA  
3607 C C   . HIS A 470 ? 1.2424 0.9436 1.4785 0.1099  0.0903  0.1606  470 HIS A C   
3608 O O   . HIS A 470 ? 1.2273 0.9013 1.4337 0.1061  0.0980  0.1636  470 HIS A O   
3609 C CB  . HIS A 470 ? 1.2190 0.9444 1.4120 0.0742  0.0854  0.1151  470 HIS A CB  
3610 C CG  . HIS A 470 ? 1.1767 0.9158 1.3729 0.0578  0.0957  0.0869  470 HIS A CG  
3611 N ND1 . HIS A 470 ? 1.2041 0.9727 1.4265 0.0563  0.0911  0.0812  470 HIS A ND1 
3612 C CD2 . HIS A 470 ? 1.1805 0.9101 1.3561 0.0423  0.1103  0.0639  470 HIS A CD2 
3613 C CE1 . HIS A 470 ? 1.1575 0.9324 1.3727 0.0408  0.1039  0.0575  470 HIS A CE1 
3614 N NE2 . HIS A 470 ? 1.1783 0.9310 1.3641 0.0325  0.1144  0.0468  470 HIS A NE2 
3615 N N   . LYS A 471 ? 1.2090 0.9284 1.4707 0.1284  0.0748  0.1856  471 LYS A N   
3616 C CA  . LYS A 471 ? 1.2331 0.9418 1.4863 0.1468  0.0653  0.2208  471 LYS A CA  
3617 C C   . LYS A 471 ? 1.2685 1.0039 1.4796 0.1470  0.0309  0.2352  471 LYS A C   
3618 O O   . LYS A 471 ? 1.1889 0.9534 1.3925 0.1358  0.0141  0.2199  471 LYS A O   
3619 C CB  . LYS A 471 ? 1.1756 0.8864 1.4903 0.1709  0.0723  0.2424  471 LYS A CB  
3620 C CG  . LYS A 471 ? 1.1485 0.8354 1.5089 0.1701  0.1072  0.2237  471 LYS A CG  
3621 C CD  . LYS A 471 ? 1.2002 0.8557 1.5292 0.1579  0.1258  0.2139  471 LYS A CD  
3622 C CE  . LYS A 471 ? 1.1425 0.7852 1.5134 0.1532  0.1570  0.1906  471 LYS A CE  
3623 N NZ  . LYS A 471 ? 1.1821 0.8306 1.6019 0.1727  0.1618  0.2094  471 LYS A NZ  
3624 N N   . GLY A 472 ? 1.3582 1.0834 1.5419 0.1593  0.0219  0.2645  472 GLY A N   
3625 C CA  . GLY A 472 ? 1.3739 1.1243 1.5145 0.1608  -0.0100 0.2784  472 GLY A CA  
3626 C C   . GLY A 472 ? 1.4037 1.1415 1.4813 0.1422  -0.0129 0.2637  472 GLY A C   
3627 O O   . GLY A 472 ? 1.3548 1.0688 1.4226 0.1271  0.0072  0.2416  472 GLY A O   
3628 N N   . LYS A 473 ? 1.6194 1.3762 1.6546 0.1440  -0.0390 0.2758  473 LYS A N   
3629 C CA  . LYS A 473 ? 1.5808 1.3301 1.5565 0.1281  -0.0445 0.2622  473 LYS A CA  
3630 C C   . LYS A 473 ? 1.5980 1.3777 1.5653 0.1132  -0.0663 0.2385  473 LYS A C   
3631 O O   . LYS A 473 ? 1.6245 1.4284 1.5627 0.1132  -0.0920 0.2425  473 LYS A O   
3632 C CB  . LYS A 473 ? 1.6108 1.3569 1.5406 0.1395  -0.0547 0.2902  473 LYS A CB  
3633 C CG  . LYS A 473 ? 1.6266 1.3364 1.5600 0.1512  -0.0290 0.3139  473 LYS A CG  
3634 C CD  . LYS A 473 ? 1.5781 1.2530 1.5071 0.1348  -0.0005 0.2906  473 LYS A CD  
3635 C CE  . LYS A 473 ? 1.5811 1.2236 1.5189 0.1412  0.0252  0.3065  473 LYS A CE  
3636 N NZ  . LYS A 473 ? 1.5569 1.1741 1.4934 0.1229  0.0497  0.2795  473 LYS A NZ  
3637 N N   . VAL A 474 ? 1.3049 1.0836 1.2984 0.0997  -0.0548 0.2131  474 VAL A N   
3638 C CA  . VAL A 474 ? 1.1273 0.9307 1.1220 0.0844  -0.0698 0.1907  474 VAL A CA  
3639 C C   . VAL A 474 ? 0.9775 0.7592 0.9450 0.0653  -0.0562 0.1667  474 VAL A C   
3640 O O   . VAL A 474 ? 0.9927 0.7506 0.9686 0.0624  -0.0322 0.1598  474 VAL A O   
3641 C CB  . VAL A 474 ? 1.0439 0.8705 1.0975 0.0864  -0.0683 0.1853  474 VAL A CB  
3642 C CG1 . VAL A 474 ? 0.9673 0.8112 1.0242 0.0672  -0.0749 0.1605  474 VAL A CG1 
3643 C CG2 . VAL A 474 ? 1.0586 0.9154 1.1402 0.1052  -0.0881 0.2087  474 VAL A CG2 
3644 N N   . ILE A 475 ? 0.8972 0.6879 0.8340 0.0526  -0.0716 0.1534  475 ILE A N   
3645 C CA  . ILE A 475 ? 0.8524 0.6242 0.7645 0.0363  -0.0608 0.1332  475 ILE A CA  
3646 C C   . ILE A 475 ? 0.8059 0.5864 0.7505 0.0250  -0.0530 0.1162  475 ILE A C   
3647 O O   . ILE A 475 ? 0.8505 0.6555 0.8137 0.0195  -0.0668 0.1102  475 ILE A O   
3648 C CB  . ILE A 475 ? 0.8464 0.6213 0.7157 0.0279  -0.0779 0.1254  475 ILE A CB  
3649 C CG1 . ILE A 475 ? 0.8286 0.5993 0.6623 0.0396  -0.0855 0.1433  475 ILE A CG1 
3650 C CG2 . ILE A 475 ? 0.7621 0.5155 0.6098 0.0140  -0.0651 0.1074  475 ILE A CG2 
3651 C CD1 . ILE A 475 ? 0.8870 0.6636 0.6772 0.0319  -0.1022 0.1333  475 ILE A CD1 
3652 N N   . MET A 476 ? 0.7788 0.5413 0.7301 0.0209  -0.0304 0.1080  476 MET A N   
3653 C CA  . MET A 476 ? 0.7043 0.4746 0.6812 0.0109  -0.0195 0.0932  476 MET A CA  
3654 C C   . MET A 476 ? 0.6476 0.4038 0.5964 -0.0029 -0.0121 0.0789  476 MET A C   
3655 O O   . MET A 476 ? 0.6661 0.4033 0.5829 -0.0033 -0.0095 0.0792  476 MET A O   
3656 C CB  . MET A 476 ? 0.7338 0.4998 0.7446 0.0177  0.0014  0.0934  476 MET A CB  
3657 C CG  . MET A 476 ? 0.8212 0.5987 0.8673 0.0339  -0.0023 0.1093  476 MET A CG  
3658 S SD  . MET A 476 ? 1.0721 0.8346 1.1555 0.0416  0.0272  0.1064  476 MET A SD  
3659 C CE  . MET A 476 ? 0.9434 0.7205 1.0435 0.0258  0.0408  0.0816  476 MET A CE  
3660 N N   . HIS A 477 ? 0.6005 0.3675 0.5634 -0.0136 -0.0078 0.0679  477 HIS A N   
3661 C CA  . HIS A 477 ? 0.5693 0.3257 0.5109 -0.0249 0.0005  0.0573  477 HIS A CA  
3662 C C   . HIS A 477 ? 0.6145 0.3617 0.5586 -0.0244 0.0211  0.0514  477 HIS A C   
3663 O O   . HIS A 477 ? 0.6498 0.4044 0.6224 -0.0203 0.0325  0.0497  477 HIS A O   
3664 C CB  . HIS A 477 ? 0.5718 0.3435 0.5272 -0.0362 -0.0014 0.0510  477 HIS A CB  
3665 C CG  . HIS A 477 ? 0.5865 0.3642 0.5372 -0.0412 -0.0205 0.0515  477 HIS A CG  
3666 N ND1 . HIS A 477 ? 0.5260 0.2909 0.4510 -0.0494 -0.0252 0.0465  477 HIS A ND1 
3667 C CD2 . HIS A 477 ? 0.5691 0.3657 0.5399 -0.0395 -0.0361 0.0546  477 HIS A CD2 
3668 C CE1 . HIS A 477 ? 0.6119 0.3853 0.5408 -0.0537 -0.0417 0.0443  477 HIS A CE1 
3669 N NE2 . HIS A 477 ? 0.6064 0.4010 0.5621 -0.0483 -0.0497 0.0489  477 HIS A NE2 
3670 N N   . ASP A 478 ? 0.5689 0.3013 0.4854 -0.0286 0.0261  0.0464  478 ASP A N   
3671 C CA  . ASP A 478 ? 0.5546 0.2814 0.4720 -0.0302 0.0438  0.0376  478 ASP A CA  
3672 C C   . ASP A 478 ? 0.5794 0.3023 0.4709 -0.0384 0.0445  0.0311  478 ASP A C   
3673 O O   . ASP A 478 ? 0.5883 0.2986 0.4630 -0.0376 0.0479  0.0294  478 ASP A O   
3674 C CB  . ASP A 478 ? 0.6147 0.3255 0.5339 -0.0215 0.0509  0.0422  478 ASP A CB  
3675 C CG  . ASP A 478 ? 0.6164 0.3257 0.5550 -0.0227 0.0709  0.0307  478 ASP A CG  
3676 O OD1 . ASP A 478 ? 0.6443 0.3635 0.5799 -0.0317 0.0782  0.0171  478 ASP A OD1 
3677 O OD2 . ASP A 478 ? 0.6017 0.3005 0.5591 -0.0145 0.0795  0.0353  478 ASP A OD2 
3678 N N   . PRO A 479 ? 0.5488 0.2833 0.4392 -0.0461 0.0424  0.0287  479 PRO A N   
3679 C CA  . PRO A 479 ? 0.5400 0.2709 0.4076 -0.0516 0.0409  0.0269  479 PRO A CA  
3680 C C   . PRO A 479 ? 0.5662 0.2986 0.4267 -0.0530 0.0524  0.0181  479 PRO A C   
3681 O O   . PRO A 479 ? 0.6044 0.3485 0.4777 -0.0550 0.0637  0.0098  479 PRO A O   
3682 C CB  . PRO A 479 ? 0.5754 0.3200 0.4501 -0.0588 0.0400  0.0289  479 PRO A CB  
3683 C CG  . PRO A 479 ? 0.6193 0.3788 0.5204 -0.0585 0.0476  0.0264  479 PRO A CG  
3684 C CD  . PRO A 479 ? 0.5638 0.3161 0.4771 -0.0495 0.0441  0.0286  479 PRO A CD  
3685 N N   . PHE A 480 ? 0.5641 0.2862 0.4058 -0.0523 0.0497  0.0181  480 PHE A N   
3686 C CA  . PHE A 480 ? 0.5799 0.3055 0.4166 -0.0540 0.0582  0.0090  480 PHE A CA  
3687 C C   . PHE A 480 ? 0.5609 0.2830 0.4133 -0.0522 0.0699  0.0011  480 PHE A C   
3688 O O   . PHE A 480 ? 0.5809 0.3102 0.4365 -0.0561 0.0791  -0.0110 480 PHE A O   
3689 C CB  . PHE A 480 ? 0.5987 0.3450 0.4317 -0.0600 0.0612  0.0042  480 PHE A CB  
3690 C CG  . PHE A 480 ? 0.6368 0.3835 0.4551 -0.0607 0.0523  0.0137  480 PHE A CG  
3691 C CD1 . PHE A 480 ? 0.5842 0.3278 0.4047 -0.0620 0.0463  0.0235  480 PHE A CD1 
3692 C CD2 . PHE A 480 ? 0.5995 0.3502 0.4063 -0.0601 0.0507  0.0128  480 PHE A CD2 
3693 C CE1 . PHE A 480 ? 0.5961 0.3362 0.4074 -0.0626 0.0404  0.0325  480 PHE A CE1 
3694 C CE2 . PHE A 480 ? 0.6354 0.3846 0.4330 -0.0589 0.0437  0.0233  480 PHE A CE2 
3695 C CZ  . PHE A 480 ? 0.5911 0.3329 0.3909 -0.0602 0.0394  0.0334  480 PHE A CZ  
3696 N N   . ALA A 481 ? 0.5431 0.2549 0.4077 -0.0463 0.0695  0.0079  481 ALA A N   
3697 C CA  . ALA A 481 ? 0.6461 0.3516 0.5320 -0.0429 0.0822  0.0035  481 ALA A CA  
3698 C C   . ALA A 481 ? 0.5754 0.2970 0.4797 -0.0484 0.0945  -0.0117 481 ALA A C   
3699 O O   . ALA A 481 ? 0.5923 0.3102 0.5126 -0.0496 0.1086  -0.0235 481 ALA A O   
3700 C CB  . ALA A 481 ? 0.5458 0.2365 0.4273 -0.0422 0.0897  0.0012  481 ALA A CB  
3701 N N   . MET A 482 ? 0.5534 0.2926 0.4560 -0.0523 0.0909  -0.0125 482 MET A N   
3702 C CA  . MET A 482 ? 0.5589 0.3173 0.4718 -0.0585 0.1030  -0.0277 482 MET A CA  
3703 C C   . MET A 482 ? 0.5338 0.3019 0.4681 -0.0566 0.1065  -0.0254 482 MET A C   
3704 O O   . MET A 482 ? 0.6076 0.3944 0.5470 -0.0622 0.1169  -0.0372 482 MET A O   
3705 C CB  . MET A 482 ? 0.5800 0.3565 0.4689 -0.0662 0.0992  -0.0313 482 MET A CB  
3706 C CG  . MET A 482 ? 0.5647 0.3418 0.4408 -0.0694 0.0997  -0.0402 482 MET A CG  
3707 S SD  . MET A 482 ? 0.6007 0.3970 0.4879 -0.0776 0.1163  -0.0678 482 MET A SD  
3708 C CE  . MET A 482 ? 0.5423 0.3711 0.4096 -0.0838 0.1144  -0.0685 482 MET A CE  
3709 N N   . ARG A 483 ? 0.5048 0.2637 0.4519 -0.0488 0.0982  -0.0112 483 ARG A N   
3710 C CA  . ARG A 483 ? 0.5679 0.3398 0.5406 -0.0467 0.1006  -0.0088 483 ARG A CA  
3711 C C   . ARG A 483 ? 0.6102 0.3896 0.6106 -0.0462 0.1205  -0.0244 483 ARG A C   
3712 O O   . ARG A 483 ? 0.6480 0.4471 0.6589 -0.0506 0.1285  -0.0309 483 ARG A O   
3713 C CB  . ARG A 483 ? 0.5562 0.3201 0.5416 -0.0372 0.0872  0.0078  483 ARG A CB  
3714 C CG  . ARG A 483 ? 0.5400 0.3223 0.5536 -0.0359 0.0859  0.0115  483 ARG A CG  
3715 C CD  . ARG A 483 ? 0.5591 0.3389 0.5918 -0.0248 0.0730  0.0261  483 ARG A CD  
3716 N NE  . ARG A 483 ? 0.6911 0.4620 0.7496 -0.0135 0.0838  0.0269  483 ARG A NE  
3717 C CZ  . ARG A 483 ? 0.7435 0.4934 0.7929 -0.0061 0.0830  0.0343  483 ARG A CZ  
3718 N NH1 . ARG A 483 ? 0.6854 0.4228 0.6993 -0.0084 0.0717  0.0403  483 ARG A NH1 
3719 N NH2 . ARG A 483 ? 0.8658 0.6059 0.9443 0.0041  0.0958  0.0360  483 ARG A NH2 
3720 N N   . PRO A 484 ? 0.6429 0.4073 0.6580 -0.0416 0.1312  -0.0316 484 PRO A N   
3721 C CA  . PRO A 484 ? 0.5815 0.3514 0.6266 -0.0417 0.1524  -0.0500 484 PRO A CA  
3722 C C   . PRO A 484 ? 0.5782 0.3630 0.6080 -0.0542 0.1648  -0.0742 484 PRO A C   
3723 O O   . PRO A 484 ? 0.5876 0.3788 0.6397 -0.0563 0.1838  -0.0944 484 PRO A O   
3724 C CB  . PRO A 484 ? 0.6422 0.3861 0.7090 -0.0326 0.1594  -0.0472 484 PRO A CB  
3725 C CG  . PRO A 484 ? 0.6136 0.3426 0.6612 -0.0261 0.1405  -0.0236 484 PRO A CG  
3726 C CD  . PRO A 484 ? 0.5749 0.3150 0.5846 -0.0354 0.1267  -0.0226 484 PRO A CD  
3727 N N   . PHE A 485 ? 0.5823 0.3747 0.5757 -0.0621 0.1546  -0.0735 485 PHE A N   
3728 C CA  . PHE A 485 ? 0.6203 0.4283 0.5969 -0.0728 0.1631  -0.0956 485 PHE A CA  
3729 C C   . PHE A 485 ? 0.5915 0.4249 0.5362 -0.0803 0.1560  -0.0925 485 PHE A C   
3730 O O   . PHE A 485 ? 0.5884 0.4390 0.5128 -0.0885 0.1583  -0.1070 485 PHE A O   
3731 C CB  . PHE A 485 ? 0.5555 0.3489 0.5229 -0.0746 0.1598  -0.0998 485 PHE A CB  
3732 C CG  . PHE A 485 ? 0.5762 0.3403 0.5710 -0.0663 0.1658  -0.0953 485 PHE A CG  
3733 C CD1 . PHE A 485 ? 0.5459 0.3023 0.5748 -0.0657 0.1857  -0.1127 485 PHE A CD1 
3734 C CD2 . PHE A 485 ? 0.5639 0.3077 0.5502 -0.0590 0.1529  -0.0732 485 PHE A CD2 
3735 C CE1 . PHE A 485 ? 0.5975 0.3249 0.6532 -0.0570 0.1925  -0.1045 485 PHE A CE1 
3736 C CE2 . PHE A 485 ? 0.6202 0.3381 0.6283 -0.0507 0.1591  -0.0653 485 PHE A CE2 
3737 C CZ  . PHE A 485 ? 0.5521 0.2609 0.5958 -0.0492 0.1789  -0.0791 485 PHE A CZ  
3738 N N   . PHE A 486 ? 0.5366 0.3741 0.4779 -0.0780 0.1475  -0.0736 486 PHE A N   
3739 C CA  . PHE A 486 ? 0.6353 0.4940 0.5488 -0.0846 0.1432  -0.0672 486 PHE A CA  
3740 C C   . PHE A 486 ? 0.5889 0.4747 0.5008 -0.0919 0.1608  -0.0863 486 PHE A C   
3741 O O   . PHE A 486 ? 0.6217 0.5117 0.5602 -0.0905 0.1748  -0.0943 486 PHE A O   
3742 C CB  . PHE A 486 ? 0.5485 0.4035 0.4652 -0.0821 0.1332  -0.0444 486 PHE A CB  
3743 C CG  . PHE A 486 ? 0.5513 0.3847 0.4587 -0.0774 0.1148  -0.0276 486 PHE A CG  
3744 C CD1 . PHE A 486 ? 0.5430 0.3738 0.4228 -0.0791 0.1059  -0.0238 486 PHE A CD1 
3745 C CD2 . PHE A 486 ? 0.5777 0.3959 0.5044 -0.0710 0.1065  -0.0164 486 PHE A CD2 
3746 C CE1 . PHE A 486 ? 0.5687 0.3796 0.4408 -0.0748 0.0915  -0.0109 486 PHE A CE1 
3747 C CE2 . PHE A 486 ? 0.5902 0.3903 0.5050 -0.0675 0.0906  -0.0040 486 PHE A CE2 
3748 C CZ  . PHE A 486 ? 0.5733 0.3684 0.4610 -0.0696 0.0843  -0.0020 486 PHE A CZ  
3749 N N   . GLY A 487 ? 0.6162 0.5227 0.4974 -0.0990 0.1604  -0.0943 487 GLY A N   
3750 C CA  . GLY A 487 ? 0.6251 0.5619 0.4962 -0.1068 0.1760  -0.1130 487 GLY A CA  
3751 C C   . GLY A 487 ? 0.6080 0.5647 0.4624 -0.1098 0.1786  -0.0970 487 GLY A C   
3752 O O   . GLY A 487 ? 0.5914 0.5737 0.4391 -0.1157 0.1948  -0.1112 487 GLY A O   
3753 N N   . TYR A 488 ? 0.5738 0.5188 0.4224 -0.1064 0.1649  -0.0686 488 TYR A N   
3754 C CA  . TYR A 488 ? 0.5975 0.5575 0.4324 -0.1099 0.1677  -0.0496 488 TYR A CA  
3755 C C   . TYR A 488 ? 0.5999 0.5362 0.4499 -0.1057 0.1551  -0.0244 488 TYR A C   
3756 O O   . TYR A 488 ? 0.6186 0.5306 0.4873 -0.0998 0.1447  -0.0234 488 TYR A O   
3757 C CB  . TYR A 488 ? 0.6249 0.6082 0.4172 -0.1140 0.1634  -0.0432 488 TYR A CB  
3758 C CG  . TYR A 488 ? 0.6104 0.5794 0.3880 -0.1093 0.1430  -0.0295 488 TYR A CG  
3759 C CD1 . TYR A 488 ? 0.6028 0.5674 0.3798 -0.1078 0.1361  -0.0466 488 TYR A CD1 
3760 C CD2 . TYR A 488 ? 0.6062 0.5655 0.3741 -0.1067 0.1326  -0.0002 488 TYR A CD2 
3761 C CE1 . TYR A 488 ? 0.6815 0.6350 0.4482 -0.1033 0.1192  -0.0348 488 TYR A CE1 
3762 C CE2 . TYR A 488 ? 0.6721 0.6182 0.4298 -0.1015 0.1158  0.0111  488 TYR A CE2 
3763 C CZ  . TYR A 488 ? 0.6684 0.6129 0.4253 -0.0995 0.1091  -0.0062 488 TYR A CZ  
3764 O OH  . TYR A 488 ? 0.6876 0.6210 0.4374 -0.0940 0.0941  0.0042  488 TYR A OH  
3765 N N   . ASN A 489 ? 0.6084 0.5525 0.4496 -0.1093 0.1568  -0.0043 489 ASN A N   
3766 C CA  . ASN A 489 ? 0.6691 0.5937 0.5281 -0.1082 0.1473  0.0165  489 ASN A CA  
3767 C C   . ASN A 489 ? 0.6394 0.5380 0.4920 -0.1025 0.1273  0.0243  489 ASN A C   
3768 O O   . ASN A 489 ? 0.6157 0.5150 0.4412 -0.1013 0.1200  0.0297  489 ASN A O   
3769 C CB  . ASN A 489 ? 0.6381 0.5743 0.4845 -0.1142 0.1539  0.0377  489 ASN A CB  
3770 C CG  . ASN A 489 ? 0.6708 0.5891 0.5432 -0.1160 0.1481  0.0550  489 ASN A CG  
3771 O OD1 . ASN A 489 ? 0.6597 0.5553 0.5303 -0.1133 0.1326  0.0657  489 ASN A OD1 
3772 N ND2 . ASN A 489 ? 0.6004 0.5304 0.4991 -0.1214 0.1616  0.0559  489 ASN A ND2 
3773 N N   . PHE A 490 ? 0.6167 0.4949 0.4948 -0.0987 0.1184  0.0248  490 PHE A N   
3774 C CA  . PHE A 490 ? 0.6077 0.4616 0.4793 -0.0934 0.1014  0.0296  490 PHE A CA  
3775 C C   . PHE A 490 ? 0.6334 0.4771 0.4921 -0.0953 0.0930  0.0489  490 PHE A C   
3776 O O   . PHE A 490 ? 0.6046 0.4349 0.4474 -0.0912 0.0826  0.0524  490 PHE A O   
3777 C CB  . PHE A 490 ? 0.6168 0.4556 0.5155 -0.0889 0.0941  0.0262  490 PHE A CB  
3778 C CG  . PHE A 490 ? 0.6170 0.4320 0.5072 -0.0841 0.0778  0.0311  490 PHE A CG  
3779 C CD1 . PHE A 490 ? 0.5606 0.3679 0.4296 -0.0805 0.0743  0.0268  490 PHE A CD1 
3780 C CD2 . PHE A 490 ? 0.6106 0.4134 0.5148 -0.0839 0.0667  0.0382  490 PHE A CD2 
3781 C CE1 . PHE A 490 ? 0.5667 0.3532 0.4278 -0.0762 0.0619  0.0306  490 PHE A CE1 
3782 C CE2 . PHE A 490 ? 0.6038 0.3863 0.4972 -0.0800 0.0532  0.0403  490 PHE A CE2 
3783 C CZ  . PHE A 490 ? 0.5438 0.3173 0.4151 -0.0758 0.0519  0.0371  490 PHE A CZ  
3784 N N   . GLY A 491 ? 0.6469 0.4957 0.5159 -0.1013 0.0988  0.0614  491 GLY A N   
3785 C CA  . GLY A 491 ? 0.6010 0.4386 0.4601 -0.1033 0.0944  0.0808  491 GLY A CA  
3786 C C   . GLY A 491 ? 0.6002 0.4478 0.4271 -0.1006 0.0955  0.0887  491 GLY A C   
3787 O O   . GLY A 491 ? 0.6219 0.4547 0.4376 -0.0960 0.0856  0.0980  491 GLY A O   
3788 N N   . LYS A 492 ? 0.5857 0.4609 0.3978 -0.1029 0.1074  0.0842  492 LYS A N   
3789 C CA  . LYS A 492 ? 0.6265 0.5189 0.4062 -0.1000 0.1061  0.0892  492 LYS A CA  
3790 C C   . LYS A 492 ? 0.6187 0.5056 0.3906 -0.0937 0.0941  0.0751  492 LYS A C   
3791 O O   . LYS A 492 ? 0.6372 0.5291 0.3899 -0.0891 0.0862  0.0836  492 LYS A O   
3792 C CB  . LYS A 492 ? 0.6805 0.6073 0.4445 -0.1050 0.1212  0.0812  492 LYS A CB  
3793 C CG  . LYS A 492 ? 0.6811 0.6166 0.4538 -0.1120 0.1370  0.0939  492 LYS A CG  
3794 C CD  . LYS A 492 ? 0.7483 0.6749 0.5124 -0.1119 0.1357  0.1258  492 LYS A CD  
3795 C CE  . LYS A 492 ? 0.8178 0.7526 0.5935 -0.1202 0.1539  0.1396  492 LYS A CE  
3796 N NZ  . LYS A 492 ? 0.9614 0.8830 0.7333 -0.1205 0.1549  0.1727  492 LYS A NZ  
3797 N N   . TYR A 493 ? 0.6462 0.5238 0.4348 -0.0930 0.0932  0.0551  493 TYR A N   
3798 C CA  . TYR A 493 ? 0.5878 0.4565 0.3731 -0.0879 0.0839  0.0429  493 TYR A CA  
3799 C C   . TYR A 493 ? 0.5988 0.4427 0.3840 -0.0824 0.0709  0.0566  493 TYR A C   
3800 O O   . TYR A 493 ? 0.5757 0.4212 0.3484 -0.0779 0.0638  0.0574  493 TYR A O   
3801 C CB  . TYR A 493 ? 0.5789 0.4390 0.3851 -0.0877 0.0879  0.0236  493 TYR A CB  
3802 C CG  . TYR A 493 ? 0.5716 0.4174 0.3793 -0.0830 0.0809  0.0129  493 TYR A CG  
3803 C CD1 . TYR A 493 ? 0.5869 0.4472 0.3880 -0.0844 0.0848  -0.0045 493 TYR A CD1 
3804 C CD2 . TYR A 493 ? 0.5999 0.4188 0.4163 -0.0783 0.0716  0.0190  493 TYR A CD2 
3805 C CE1 . TYR A 493 ? 0.5710 0.4176 0.3772 -0.0812 0.0809  -0.0136 493 TYR A CE1 
3806 C CE2 . TYR A 493 ? 0.6188 0.4248 0.4355 -0.0742 0.0678  0.0109  493 TYR A CE2 
3807 C CZ  . TYR A 493 ? 0.6390 0.4580 0.4521 -0.0758 0.0732  -0.0044 493 TYR A CZ  
3808 O OH  . TYR A 493 ? 0.6440 0.4496 0.4606 -0.0728 0.0716  -0.0115 493 TYR A OH  
3809 N N   . LEU A 494 ? 0.5648 0.3874 0.3657 -0.0832 0.0682  0.0659  494 LEU A N   
3810 C CA  . LEU A 494 ? 0.6200 0.4183 0.4214 -0.0790 0.0580  0.0764  494 LEU A CA  
3811 C C   . LEU A 494 ? 0.6354 0.4388 0.4225 -0.0763 0.0570  0.0951  494 LEU A C   
3812 O O   . LEU A 494 ? 0.6293 0.4242 0.4103 -0.0697 0.0494  0.0986  494 LEU A O   
3813 C CB  . LEU A 494 ? 0.6579 0.4368 0.4796 -0.0828 0.0559  0.0802  494 LEU A CB  
3814 C CG  . LEU A 494 ? 0.6126 0.3848 0.4490 -0.0825 0.0525  0.0656  494 LEU A CG  
3815 C CD1 . LEU A 494 ? 0.6062 0.3683 0.4640 -0.0876 0.0492  0.0691  494 LEU A CD1 
3816 C CD2 . LEU A 494 ? 0.5497 0.3070 0.3773 -0.0759 0.0443  0.0576  494 LEU A CD2 
3817 N N   . ALA A 495 ? 0.6740 0.4923 0.4568 -0.0806 0.0654  0.1088  495 ALA A N   
3818 C CA  . ALA A 495 ? 0.6523 0.4763 0.4213 -0.0765 0.0648  0.1316  495 ALA A CA  
3819 C C   . ALA A 495 ? 0.6821 0.5304 0.4296 -0.0703 0.0591  0.1279  495 ALA A C   
3820 O O   . ALA A 495 ? 0.7305 0.5784 0.4713 -0.0625 0.0526  0.1437  495 ALA A O   
3821 C CB  . ALA A 495 ? 0.6162 0.4542 0.3821 -0.0827 0.0772  0.1484  495 ALA A CB  
3822 N N   . HIS A 496 ? 0.6456 0.5160 0.3858 -0.0736 0.0617  0.1063  496 HIS A N   
3823 C CA  . HIS A 496 ? 0.6188 0.5150 0.3425 -0.0699 0.0557  0.0976  496 HIS A CA  
3824 C C   . HIS A 496 ? 0.6818 0.5605 0.4149 -0.0630 0.0451  0.0919  496 HIS A C   
3825 O O   . HIS A 496 ? 0.6734 0.5666 0.3985 -0.0565 0.0371  0.0980  496 HIS A O   
3826 C CB  . HIS A 496 ? 0.6779 0.5975 0.3973 -0.0771 0.0632  0.0714  496 HIS A CB  
3827 C CG  . HIS A 496 ? 0.6822 0.6335 0.3865 -0.0765 0.0579  0.0578  496 HIS A CG  
3828 N ND1 . HIS A 496 ? 0.6924 0.6737 0.3742 -0.0729 0.0517  0.0725  496 HIS A ND1 
3829 C CD2 . HIS A 496 ? 0.5698 0.5292 0.2802 -0.0796 0.0579  0.0305  496 HIS A CD2 
3830 C CE1 . HIS A 496 ? 0.6735 0.6833 0.3481 -0.0744 0.0462  0.0527  496 HIS A CE1 
3831 N NE2 . HIS A 496 ? 0.6025 0.5981 0.2956 -0.0793 0.0509  0.0262  496 HIS A NE2 
3832 N N   . TRP A 497 ? 0.6350 0.4850 0.3851 -0.0639 0.0452  0.0810  497 TRP A N   
3833 C CA  . TRP A 497 ? 0.6236 0.4550 0.3810 -0.0577 0.0378  0.0763  497 TRP A CA  
3834 C C   . TRP A 497 ? 0.7117 0.5272 0.4715 -0.0502 0.0323  0.0972  497 TRP A C   
3835 O O   . TRP A 497 ? 0.6815 0.5003 0.4416 -0.0428 0.0262  0.0993  497 TRP A O   
3836 C CB  . TRP A 497 ? 0.5692 0.3747 0.3400 -0.0601 0.0396  0.0631  497 TRP A CB  
3837 C CG  . TRP A 497 ? 0.6423 0.4557 0.4159 -0.0624 0.0431  0.0419  497 TRP A CG  
3838 C CD1 . TRP A 497 ? 0.6151 0.4432 0.3910 -0.0684 0.0511  0.0286  497 TRP A CD1 
3839 C CD2 . TRP A 497 ? 0.6392 0.4443 0.4166 -0.0591 0.0409  0.0314  497 TRP A CD2 
3840 N NE1 . TRP A 497 ? 0.6347 0.4620 0.4174 -0.0690 0.0541  0.0108  497 TRP A NE1 
3841 C CE2 . TRP A 497 ? 0.6536 0.4675 0.4369 -0.0638 0.0480  0.0131  497 TRP A CE2 
3842 C CE3 . TRP A 497 ? 0.6398 0.4306 0.4184 -0.0528 0.0356  0.0353  497 TRP A CE3 
3843 C CZ2 . TRP A 497 ? 0.6554 0.4631 0.4459 -0.0631 0.0502  0.0006  497 TRP A CZ2 
3844 C CZ3 . TRP A 497 ? 0.6297 0.4171 0.4134 -0.0520 0.0378  0.0224  497 TRP A CZ3 
3845 C CH2 . TRP A 497 ? 0.6423 0.4377 0.4320 -0.0574 0.0451  0.0061  497 TRP A CH2 
3846 N N   . LEU A 498 ? 0.6854 0.4838 0.4511 -0.0523 0.0355  0.1124  498 LEU A N   
3847 C CA  . LEU A 498 ? 0.7185 0.4974 0.4912 -0.0457 0.0329  0.1320  498 LEU A CA  
3848 C C   . LEU A 498 ? 0.7319 0.5344 0.4938 -0.0377 0.0298  0.1514  498 LEU A C   
3849 O O   . LEU A 498 ? 0.8043 0.5964 0.5738 -0.0279 0.0252  0.1631  498 LEU A O   
3850 C CB  . LEU A 498 ? 0.7109 0.4689 0.4954 -0.0519 0.0389  0.1432  498 LEU A CB  
3851 C CG  . LEU A 498 ? 0.7225 0.4579 0.5206 -0.0587 0.0388  0.1263  498 LEU A CG  
3852 C CD1 . LEU A 498 ? 0.7412 0.4644 0.5542 -0.0670 0.0448  0.1361  498 LEU A CD1 
3853 C CD2 . LEU A 498 ? 0.7060 0.4162 0.5101 -0.0533 0.0327  0.1174  498 LEU A CD2 
3854 N N   . SER A 499 ? 0.6907 0.5271 0.4352 -0.0409 0.0320  0.1547  499 SER A N   
3855 C CA  . SER A 499 ? 0.8050 0.6699 0.5351 -0.0331 0.0275  0.1754  499 SER A CA  
3856 C C   . SER A 499 ? 0.7818 0.6657 0.5118 -0.0246 0.0165  0.1674  499 SER A C   
3857 O O   . SER A 499 ? 0.8462 0.7526 0.5696 -0.0150 0.0096  0.1870  499 SER A O   
3858 C CB  . SER A 499 ? 0.7697 0.6706 0.4767 -0.0400 0.0330  0.1765  499 SER A CB  
3859 O OG  . SER A 499 ? 0.7959 0.7176 0.4965 -0.0470 0.0329  0.1460  499 SER A OG  
3860 N N   . MET A 500 ? 0.7699 0.6470 0.5088 -0.0275 0.0149  0.1408  500 MET A N   
3861 C CA  . MET A 500 ? 0.7887 0.6849 0.5323 -0.0208 0.0061  0.1317  500 MET A CA  
3862 C C   . MET A 500 ? 0.8380 0.7161 0.5978 -0.0075 0.0014  0.1493  500 MET A C   
3863 O O   . MET A 500 ? 0.8815 0.7842 0.6459 0.0015  -0.0071 0.1533  500 MET A O   
3864 C CB  . MET A 500 ? 0.7484 0.6372 0.4999 -0.0278 0.0090  0.1012  500 MET A CB  
3865 C CG  . MET A 500 ? 0.7866 0.6930 0.5277 -0.0397 0.0150  0.0817  500 MET A CG  
3866 S SD  . MET A 500 ? 0.9570 0.9209 0.6780 -0.0419 0.0095  0.0793  500 MET A SD  
3867 C CE  . MET A 500 ? 0.7137 0.6846 0.4269 -0.0564 0.0219  0.0548  500 MET A CE  
3868 N N   . ALA A 501 ? 0.8124 0.6494 0.5839 -0.0062 0.0070  0.1586  501 ALA A N   
3869 C CA  . ALA A 501 ? 0.8950 0.7107 0.6849 0.0063  0.0053  0.1734  501 ALA A CA  
3870 C C   . ALA A 501 ? 0.9590 0.7915 0.7480 0.0176  0.0012  0.2062  501 ALA A C   
3871 O O   . ALA A 501 ? 0.9848 0.8093 0.7918 0.0312  -0.0016 0.2199  501 ALA A O   
3872 C CB  . ALA A 501 ? 0.9012 0.6692 0.7039 0.0027  0.0130  0.1714  501 ALA A CB  
3873 N N   . HIS A 502 ? 0.9822 0.8380 0.7510 0.0132  0.0019  0.2201  502 HIS A N   
3874 C CA  . HIS A 502 ? 1.0367 0.9109 0.7996 0.0240  -0.0014 0.2553  502 HIS A CA  
3875 C C   . HIS A 502 ? 1.1005 1.0293 0.8497 0.0313  -0.0148 0.2577  502 HIS A C   
3876 O O   . HIS A 502 ? 1.1865 1.1396 0.9253 0.0411  -0.0199 0.2884  502 HIS A O   
3877 C CB  . HIS A 502 ? 1.0408 0.9138 0.7867 0.0153  0.0081  0.2718  502 HIS A CB  
3878 C CG  . HIS A 502 ? 1.0574 0.8828 0.8195 0.0062  0.0204  0.2685  502 HIS A CG  
3879 N ND1 . HIS A 502 ? 1.1103 0.9332 0.8627 -0.0069 0.0305  0.2684  502 HIS A ND1 
3880 C CD2 . HIS A 502 ? 1.0414 0.8229 0.8299 0.0078  0.0240  0.2633  502 HIS A CD2 
3881 C CE1 . HIS A 502 ? 1.1248 0.9060 0.8989 -0.0132 0.0383  0.2637  502 HIS A CE1 
3882 N NE2 . HIS A 502 ? 1.1231 0.8784 0.9175 -0.0049 0.0343  0.2597  502 HIS A NE2 
3883 N N   . ARG A 503 ? 1.0771 1.0271 0.8267 0.0266  -0.0208 0.2269  503 ARG A N   
3884 C CA  . ARG A 503 ? 1.1306 1.1362 0.8703 0.0309  -0.0344 0.2240  503 ARG A CA  
3885 C C   . ARG A 503 ? 1.2379 1.2517 1.0025 0.0490  -0.0446 0.2388  503 ARG A C   
3886 O O   . ARG A 503 ? 1.1683 1.1451 0.9598 0.0544  -0.0397 0.2348  503 ARG A O   
3887 C CB  . ARG A 503 ? 1.1309 1.1549 0.8671 0.0172  -0.0348 0.1837  503 ARG A CB  
3888 C CG  . ARG A 503 ? 1.0875 1.1164 0.8000 0.0012  -0.0262 0.1685  503 ARG A CG  
3889 C CD  . ARG A 503 ? 1.1098 1.1836 0.8119 -0.0084 -0.0314 0.1386  503 ARG A CD  
3890 N NE  . ARG A 503 ? 1.1605 1.2432 0.8400 -0.0222 -0.0220 0.1250  503 ARG A NE  
3891 C CZ  . ARG A 503 ? 1.0548 1.1766 0.7211 -0.0325 -0.0235 0.0986  503 ARG A CZ  
3892 N NH1 . ARG A 503 ? 1.0151 1.1735 0.6885 -0.0321 -0.0353 0.0822  503 ARG A NH1 
3893 N NH2 . ARG A 503 ? 1.0397 1.1652 0.6881 -0.0441 -0.0122 0.0866  503 ARG A NH2 
3894 N N   . PRO A 504 ? 1.3301 1.3947 1.0866 0.0590  -0.0590 0.2555  504 PRO A N   
3895 C CA  . PRO A 504 ? 1.3368 1.4142 1.1213 0.0785  -0.0697 0.2726  504 PRO A CA  
3896 C C   . PRO A 504 ? 1.3180 1.4043 1.1275 0.0761  -0.0730 0.2395  504 PRO A C   
3897 O O   . PRO A 504 ? 1.3213 1.4413 1.1212 0.0635  -0.0777 0.2104  504 PRO A O   
3898 C CB  . PRO A 504 ? 1.3316 1.4703 1.0952 0.0875  -0.0861 0.2969  504 PRO A CB  
3899 C CG  . PRO A 504 ? 1.3679 1.5117 1.0911 0.0747  -0.0794 0.3017  504 PRO A CG  
3900 C CD  . PRO A 504 ? 1.3428 1.4561 1.0634 0.0543  -0.0658 0.2631  504 PRO A CD  
3901 N N   . ALA A 505 ? 1.1902 1.2449 1.0336 0.0878  -0.0686 0.2434  505 ALA A N   
3902 C CA  . ALA A 505 ? 1.0694 1.1310 0.9409 0.0880  -0.0693 0.2168  505 ALA A CA  
3903 C C   . ALA A 505 ? 1.0078 1.0557 0.8696 0.0671  -0.0598 0.1780  505 ALA A C   
3904 O O   . ALA A 505 ? 0.9384 1.0090 0.8143 0.0619  -0.0620 0.1527  505 ALA A O   
3905 C CB  . ALA A 505 ? 0.9890 1.1164 0.8729 0.0971  -0.0879 0.2192  505 ALA A CB  
3906 N N   . ALA A 506 ? 0.9929 1.0038 0.8336 0.0555  -0.0486 0.1743  506 ALA A N   
3907 C CA  . ALA A 506 ? 0.9659 0.9624 0.7976 0.0375  -0.0395 0.1418  506 ALA A CA  
3908 C C   . ALA A 506 ? 0.8821 0.8416 0.7361 0.0382  -0.0293 0.1261  506 ALA A C   
3909 O O   . ALA A 506 ? 0.8385 0.7558 0.6999 0.0444  -0.0219 0.1366  506 ALA A O   
3910 C CB  . ALA A 506 ? 0.9689 0.9401 0.7755 0.0269  -0.0314 0.1449  506 ALA A CB  
3911 N N   . LYS A 507 ? 0.8425 0.8185 0.7074 0.0312  -0.0279 0.1001  507 LYS A N   
3912 C CA  . LYS A 507 ? 0.7729 0.7173 0.6541 0.0298  -0.0162 0.0835  507 LYS A CA  
3913 C C   . LYS A 507 ? 0.7343 0.6429 0.5962 0.0162  -0.0053 0.0701  507 LYS A C   
3914 O O   . LYS A 507 ? 0.7860 0.7032 0.6433 0.0039  -0.0013 0.0497  507 LYS A O   
3915 C CB  . LYS A 507 ? 0.7420 0.7197 0.6448 0.0270  -0.0173 0.0634  507 LYS A CB  
3916 C CG  . LYS A 507 ? 0.8041 0.8270 0.7296 0.0402  -0.0307 0.0750  507 LYS A CG  
3917 C CD  . LYS A 507 ? 0.8775 0.8781 0.8270 0.0578  -0.0270 0.0909  507 LYS A CD  
3918 C CE  . LYS A 507 ? 0.8454 0.8941 0.8254 0.0722  -0.0398 0.1007  507 LYS A CE  
3919 N NZ  . LYS A 507 ? 0.8906 0.9164 0.9007 0.0899  -0.0331 0.1127  507 LYS A NZ  
3920 N N   . LEU A 508 ? 0.7165 0.5852 0.5704 0.0186  -0.0003 0.0815  508 LEU A N   
3921 C CA  . LEU A 508 ? 0.7591 0.5978 0.5962 0.0070  0.0076  0.0713  508 LEU A CA  
3922 C C   . LEU A 508 ? 0.7472 0.5653 0.5898 0.0031  0.0174  0.0520  508 LEU A C   
3923 O O   . LEU A 508 ? 0.7523 0.5537 0.6072 0.0108  0.0219  0.0520  508 LEU A O   
3924 C CB  . LEU A 508 ? 0.7347 0.5399 0.5652 0.0096  0.0093  0.0872  508 LEU A CB  
3925 C CG  . LEU A 508 ? 0.7528 0.5727 0.5754 0.0121  0.0031  0.1096  508 LEU A CG  
3926 C CD1 . LEU A 508 ? 0.7455 0.5274 0.5685 0.0130  0.0077  0.1230  508 LEU A CD1 
3927 C CD2 . LEU A 508 ? 0.6811 0.5273 0.4853 0.0009  0.0014  0.1027  508 LEU A CD2 
3928 N N   . PRO A 509 ? 0.7109 0.5293 0.5455 -0.0083 0.0224  0.0362  509 PRO A N   
3929 C CA  . PRO A 509 ? 0.6779 0.4765 0.5158 -0.0115 0.0329  0.0218  509 PRO A CA  
3930 C C   . PRO A 509 ? 0.6906 0.4489 0.5171 -0.0099 0.0375  0.0251  509 PRO A C   
3931 O O   . PRO A 509 ? 0.6477 0.3920 0.4647 -0.0101 0.0334  0.0346  509 PRO A O   
3932 C CB  . PRO A 509 ? 0.6172 0.4254 0.4506 -0.0234 0.0369  0.0080  509 PRO A CB  
3933 C CG  . PRO A 509 ? 0.6570 0.5000 0.4885 -0.0262 0.0280  0.0100  509 PRO A CG  
3934 C CD  . PRO A 509 ? 0.6797 0.5189 0.5037 -0.0180 0.0200  0.0307  509 PRO A CD  
3935 N N   . LYS A 510 ? 0.6467 0.3883 0.4746 -0.0091 0.0467  0.0160  510 LYS A N   
3936 C CA  . LYS A 510 ? 0.6027 0.3102 0.4157 -0.0093 0.0509  0.0149  510 LYS A CA  
3937 C C   . LYS A 510 ? 0.6250 0.3245 0.4230 -0.0181 0.0514  0.0118  510 LYS A C   
3938 O O   . LYS A 510 ? 0.6203 0.3345 0.4219 -0.0237 0.0542  0.0063  510 LYS A O   
3939 C CB  . LYS A 510 ? 0.6261 0.3220 0.4417 -0.0054 0.0619  0.0064  510 LYS A CB  
3940 C CG  . LYS A 510 ? 0.7397 0.4052 0.5426 -0.0021 0.0647  0.0049  510 LYS A CG  
3941 C CD  . LYS A 510 ? 0.7427 0.4024 0.5513 0.0036  0.0769  -0.0034 510 LYS A CD  
3942 C CE  . LYS A 510 ? 0.7253 0.3944 0.5595 0.0141  0.0765  0.0004  510 LYS A CE  
3943 N NZ  . LYS A 510 ? 0.7414 0.3868 0.5747 0.0191  0.0737  0.0037  510 LYS A NZ  
3944 N N   . ILE A 511 ? 0.6253 0.3024 0.4097 -0.0192 0.0486  0.0145  511 ILE A N   
3945 C CA  . ILE A 511 ? 0.5823 0.2533 0.3559 -0.0256 0.0471  0.0139  511 ILE A CA  
3946 C C   . ILE A 511 ? 0.6401 0.2890 0.3979 -0.0251 0.0504  0.0099  511 ILE A C   
3947 O O   . ILE A 511 ? 0.6866 0.3201 0.4375 -0.0226 0.0483  0.0085  511 ILE A O   
3948 C CB  . ILE A 511 ? 0.6253 0.2976 0.3989 -0.0286 0.0386  0.0216  511 ILE A CB  
3949 C CG1 . ILE A 511 ? 0.6022 0.3008 0.3851 -0.0300 0.0366  0.0257  511 ILE A CG1 
3950 C CG2 . ILE A 511 ? 0.5549 0.2191 0.3206 -0.0335 0.0367  0.0206  511 ILE A CG2 
3951 C CD1 . ILE A 511 ? 0.6860 0.3878 0.4687 -0.0329 0.0310  0.0354  511 ILE A CD1 
3952 N N   . PHE A 512 ? 0.5935 0.2413 0.3456 -0.0275 0.0558  0.0080  512 PHE A N   
3953 C CA  . PHE A 512 ? 0.6350 0.2662 0.3683 -0.0263 0.0588  0.0073  512 PHE A CA  
3954 C C   . PHE A 512 ? 0.6235 0.2533 0.3518 -0.0289 0.0537  0.0125  512 PHE A C   
3955 O O   . PHE A 512 ? 0.6854 0.3264 0.4274 -0.0319 0.0525  0.0144  512 PHE A O   
3956 C CB  . PHE A 512 ? 0.5940 0.2237 0.3260 -0.0248 0.0729  0.0046  512 PHE A CB  
3957 C CG  . PHE A 512 ? 0.6214 0.2567 0.3643 -0.0216 0.0794  -0.0010 512 PHE A CG  
3958 C CD1 . PHE A 512 ? 0.6030 0.2257 0.3343 -0.0172 0.0831  -0.0054 512 PHE A CD1 
3959 C CD2 . PHE A 512 ? 0.6076 0.2630 0.3737 -0.0228 0.0819  -0.0033 512 PHE A CD2 
3960 C CE1 . PHE A 512 ? 0.6238 0.2525 0.3700 -0.0128 0.0903  -0.0104 512 PHE A CE1 
3961 C CE2 . PHE A 512 ? 0.6496 0.3142 0.4300 -0.0187 0.0867  -0.0075 512 PHE A CE2 
3962 C CZ  . PHE A 512 ? 0.6000 0.2504 0.3720 -0.0130 0.0915  -0.0102 512 PHE A CZ  
3963 N N   . HIS A 513 ? 0.5962 0.2142 0.3049 -0.0273 0.0508  0.0141  513 HIS A N   
3964 C CA  . HIS A 513 ? 0.6525 0.2708 0.3573 -0.0273 0.0455  0.0212  513 HIS A CA  
3965 C C   . HIS A 513 ? 0.6918 0.3009 0.3757 -0.0231 0.0516  0.0261  513 HIS A C   
3966 O O   . HIS A 513 ? 0.6230 0.2245 0.2854 -0.0215 0.0518  0.0219  513 HIS A O   
3967 C CB  . HIS A 513 ? 0.6337 0.2533 0.3363 -0.0296 0.0305  0.0207  513 HIS A CB  
3968 C CG  . HIS A 513 ? 0.6632 0.2889 0.3698 -0.0290 0.0236  0.0283  513 HIS A CG  
3969 N ND1 . HIS A 513 ? 0.6979 0.3212 0.3862 -0.0253 0.0177  0.0333  513 HIS A ND1 
3970 C CD2 . HIS A 513 ? 0.6766 0.3128 0.4043 -0.0307 0.0218  0.0319  513 HIS A CD2 
3971 C CE1 . HIS A 513 ? 0.6567 0.2889 0.3580 -0.0238 0.0116  0.0412  513 HIS A CE1 
3972 N NE2 . HIS A 513 ? 0.6858 0.3251 0.4121 -0.0273 0.0150  0.0395  513 HIS A NE2 
3973 N N   . VAL A 514 ? 0.6767 0.2858 0.3670 -0.0212 0.0581  0.0352  514 VAL A N   
3974 C CA  . VAL A 514 ? 0.6987 0.2984 0.3702 -0.0164 0.0664  0.0448  514 VAL A CA  
3975 C C   . VAL A 514 ? 0.7106 0.3118 0.3793 -0.0119 0.0578  0.0582  514 VAL A C   
3976 O O   . VAL A 514 ? 0.7254 0.3349 0.4141 -0.0128 0.0496  0.0589  514 VAL A O   
3977 C CB  . VAL A 514 ? 0.6683 0.2635 0.3537 -0.0172 0.0862  0.0465  514 VAL A CB  
3978 C CG1 . VAL A 514 ? 0.6315 0.2293 0.3212 -0.0204 0.0938  0.0341  514 VAL A CG1 
3979 C CG2 . VAL A 514 ? 0.6710 0.2712 0.3878 -0.0199 0.0900  0.0471  514 VAL A CG2 
3980 N N   . ASN A 515 ? 0.6629 0.2578 0.3064 -0.0061 0.0603  0.0699  515 ASN A N   
3981 C CA  . ASN A 515 ? 0.7563 0.3541 0.3963 0.0010  0.0523  0.0870  515 ASN A CA  
3982 C C   . ASN A 515 ? 0.7703 0.3566 0.3925 0.0074  0.0672  0.1040  515 ASN A C   
3983 O O   . ASN A 515 ? 0.8023 0.3869 0.3886 0.0095  0.0674  0.1060  515 ASN A O   
3984 C CB  . ASN A 515 ? 0.7642 0.3739 0.3839 0.0019  0.0303  0.0846  515 ASN A CB  
3985 C CG  . ASN A 515 ? 0.7883 0.4066 0.4058 0.0106  0.0193  0.1035  515 ASN A CG  
3986 O OD1 . ASN A 515 ? 0.8092 0.4240 0.4500 0.0161  0.0271  0.1176  515 ASN A OD1 
3987 N ND2 . ASN A 515 ? 0.7995 0.4305 0.3908 0.0123  0.0009  0.1032  515 ASN A ND2 
3988 N N   . TRP A 516 ? 0.7912 0.3690 0.4388 0.0100  0.0814  0.1155  516 TRP A N   
3989 C CA  . TRP A 516 ? 0.8079 0.3722 0.4429 0.0163  0.0977  0.1356  516 TRP A CA  
3990 C C   . TRP A 516 ? 0.8105 0.3784 0.4276 0.0281  0.0864  0.1600  516 TRP A C   
3991 O O   . TRP A 516 ? 0.9033 0.4698 0.5103 0.0343  0.0963  0.1778  516 TRP A O   
3992 C CB  . TRP A 516 ? 0.7715 0.3298 0.4502 0.0138  0.1178  0.1360  516 TRP A CB  
3993 C CG  . TRP A 516 ? 0.7779 0.3365 0.4803 0.0026  0.1277  0.1132  516 TRP A CG  
3994 C CD1 . TRP A 516 ? 0.7656 0.3288 0.5103 -0.0026 0.1346  0.1023  516 TRP A CD1 
3995 C CD2 . TRP A 516 ? 0.7768 0.3348 0.4635 -0.0042 0.1311  0.0979  516 TRP A CD2 
3996 N NE1 . TRP A 516 ? 0.7629 0.3293 0.5161 -0.0124 0.1407  0.0828  516 TRP A NE1 
3997 C CE2 . TRP A 516 ? 0.7423 0.3055 0.4630 -0.0129 0.1386  0.0808  516 TRP A CE2 
3998 C CE3 . TRP A 516 ? 0.7951 0.3550 0.4469 -0.0034 0.1276  0.0945  516 TRP A CE3 
3999 C CZ2 . TRP A 516 ? 0.7310 0.3028 0.4535 -0.0191 0.1411  0.0638  516 TRP A CZ2 
4000 C CZ3 . TRP A 516 ? 0.8049 0.3698 0.4612 -0.0097 0.1324  0.0764  516 TRP A CZ3 
4001 C CH2 . TRP A 516 ? 0.6792 0.2507 0.3715 -0.0167 0.1383  0.0629  516 TRP A CH2 
4002 N N   . PHE A 517 ? 0.7918 0.3758 0.4143 0.0309  0.0639  0.1588  517 PHE A N   
4003 C CA  . PHE A 517 ? 0.8719 0.4628 0.4946 0.0434  0.0531  0.1832  517 PHE A CA  
4004 C C   . PHE A 517 ? 0.8348 0.4469 0.4210 0.0470  0.0277  0.1849  517 PHE A C   
4005 O O   . PHE A 517 ? 0.8760 0.5035 0.4692 0.0560  0.0111  0.1995  517 PHE A O   
4006 C CB  . PHE A 517 ? 0.8641 0.4589 0.5353 0.0449  0.0503  0.1822  517 PHE A CB  
4007 C CG  . PHE A 517 ? 0.8775 0.4544 0.5853 0.0397  0.0743  0.1754  517 PHE A CG  
4008 C CD1 . PHE A 517 ? 0.9030 0.4742 0.6376 0.0454  0.0902  0.1905  517 PHE A CD1 
4009 C CD2 . PHE A 517 ? 0.7990 0.3782 0.5234 0.0272  0.0779  0.1490  517 PHE A CD2 
4010 C CE1 . PHE A 517 ? 0.7911 0.3568 0.5661 0.0379  0.1093  0.1766  517 PHE A CE1 
4011 C CE2 . PHE A 517 ? 0.8489 0.4182 0.6066 0.0212  0.0978  0.1394  517 PHE A CE2 
4012 C CZ  . PHE A 517 ? 0.8190 0.3855 0.6044 0.0258  0.1125  0.1503  517 PHE A CZ  
4013 N N   . ARG A 518 ? 0.9170 0.5321 0.4668 0.0401  0.0243  0.1691  518 ARG A N   
4014 C CA  . ARG A 518 ? 0.9835 0.6196 0.4973 0.0415  0.0008  0.1662  518 ARG A CA  
4015 C C   . ARG A 518 ? 1.1088 0.7491 0.5861 0.0542  0.0002  0.1950  518 ARG A C   
4016 O O   . ARG A 518 ? 1.1205 0.7456 0.5728 0.0559  0.0202  0.2046  518 ARG A O   
4017 C CB  . ARG A 518 ? 0.9682 0.6036 0.4560 0.0303  0.0002  0.1384  518 ARG A CB  
4018 C CG  . ARG A 518 ? 1.0040 0.6619 0.4618 0.0281  -0.0250 0.1268  518 ARG A CG  
4019 C CD  . ARG A 518 ? 0.9604 0.6135 0.4030 0.0163  -0.0236 0.0957  518 ARG A CD  
4020 N NE  . ARG A 518 ? 0.9713 0.6454 0.3940 0.0115  -0.0477 0.0794  518 ARG A NE  
4021 C CZ  . ARG A 518 ? 1.0266 0.6985 0.4440 0.0006  -0.0508 0.0500  518 ARG A CZ  
4022 N NH1 . ARG A 518 ? 1.0056 0.6564 0.4350 -0.0049 -0.0324 0.0359  518 ARG A NH1 
4023 N NH2 . ARG A 518 ? 1.0462 0.7383 0.4488 -0.0049 -0.0730 0.0341  518 ARG A NH2 
4024 N N   . LYS A 519 ? 1.1712 0.8340 0.6467 0.0634  -0.0223 0.2101  519 LYS A N   
4025 C CA  . LYS A 519 ? 1.2355 0.9072 0.6771 0.0778  -0.0266 0.2420  519 LYS A CA  
4026 C C   . LYS A 519 ? 1.3729 1.0723 0.7620 0.0761  -0.0498 0.2323  519 LYS A C   
4027 O O   . LYS A 519 ? 1.3215 1.0366 0.7126 0.0653  -0.0678 0.2031  519 LYS A O   
4028 C CB  . LYS A 519 ? 1.2415 0.9225 0.7196 0.0922  -0.0361 0.2697  519 LYS A CB  
4029 C CG  . LYS A 519 ? 1.1662 0.8208 0.6978 0.0941  -0.0112 0.2787  519 LYS A CG  
4030 C CD  . LYS A 519 ? 1.1633 0.8290 0.7365 0.1085  -0.0200 0.3035  519 LYS A CD  
4031 C CE  . LYS A 519 ? 1.1157 0.7581 0.7469 0.1072  0.0056  0.3056  519 LYS A CE  
4032 N NZ  . LYS A 519 ? 1.1114 0.7619 0.7862 0.1212  -0.0013 0.3266  519 LYS A NZ  
4033 N N   . ASP A 520 ? 1.5903 1.3035 0.9449 0.0838  -0.0478 0.2537  520 ASP A N   
4034 C CA  . ASP A 520 ? 1.6469 1.3921 0.9504 0.0819  -0.0682 0.2448  520 ASP A CA  
4035 C C   . ASP A 520 ? 1.7108 1.4920 1.0186 0.0920  -0.1011 0.2609  520 ASP A C   
4036 O O   . ASP A 520 ? 1.7006 1.4782 1.0504 0.0996  -0.1091 0.2722  520 ASP A O   
4037 C CB  . ASP A 520 ? 1.6985 1.4493 0.9707 0.0820  -0.0495 0.2579  520 ASP A CB  
4038 C CG  . ASP A 520 ? 1.7105 1.4610 1.0053 0.0928  -0.0399 0.2991  520 ASP A CG  
4039 O OD1 . ASP A 520 ? 1.6756 1.4184 1.0158 0.1006  -0.0435 0.3154  520 ASP A OD1 
4040 O OD2 . ASP A 520 ? 1.7440 1.4994 1.0114 0.0926  -0.0283 0.3142  520 ASP A OD2 
4041 N N   . LYS A 521 ? 1.6907 1.5099 0.9576 0.0920  -0.1204 0.2612  521 LYS A N   
4042 C CA  . LYS A 521 ? 1.6924 1.5527 0.9634 0.1006  -0.1536 0.2770  521 LYS A CA  
4043 C C   . LYS A 521 ? 1.6549 1.5156 0.9481 0.1145  -0.1504 0.3223  521 LYS A C   
4044 O O   . LYS A 521 ? 1.6545 1.5394 0.9647 0.1243  -0.1765 0.3384  521 LYS A O   
4045 C CB  . LYS A 521 ? 1.7196 1.6214 0.9388 0.0923  -0.1757 0.2593  521 LYS A CB  
4046 C CG  . LYS A 521 ? 1.7646 1.6619 0.9631 0.0765  -0.1789 0.2098  521 LYS A CG  
4047 C CD  . LYS A 521 ? 1.8133 1.7539 0.9640 0.0672  -0.1969 0.1899  521 LYS A CD  
4048 C CE  . LYS A 521 ? 1.8284 1.7593 0.9657 0.0500  -0.1973 0.1377  521 LYS A CE  
4049 N NZ  . LYS A 521 ? 1.9250 1.8999 1.0193 0.0400  -0.2120 0.1138  521 LYS A NZ  
4050 N N   . ASN A 522 ? 1.6325 1.4632 0.9280 0.1153  -0.1197 0.3405  522 ASN A N   
4051 C CA  . ASN A 522 ? 1.6490 1.4690 0.9637 0.1276  -0.1142 0.3795  522 ASN A CA  
4052 C C   . ASN A 522 ? 1.5567 1.3443 0.9363 0.1343  -0.0952 0.3899  522 ASN A C   
4053 O O   . ASN A 522 ? 1.5130 1.2893 0.9174 0.1460  -0.0898 0.4188  522 ASN A O   
4054 C CB  . ASN A 522 ? 1.6885 1.4967 0.9659 0.1241  -0.0926 0.3934  522 ASN A CB  
4055 C CG  . ASN A 522 ? 1.7107 1.5510 0.9215 0.1178  -0.1106 0.3854  522 ASN A CG  
4056 O OD1 . ASN A 522 ? 1.6898 1.5621 0.8837 0.1201  -0.1439 0.3809  522 ASN A OD1 
4057 N ND2 . ASN A 522 ? 1.6731 1.5057 0.8471 0.1093  -0.0884 0.3815  522 ASN A ND2 
4058 N N   . GLY A 523 ? 1.5240 1.2947 0.9304 0.1274  -0.0841 0.3651  523 GLY A N   
4059 C CA  . GLY A 523 ? 1.4482 1.1912 0.9157 0.1314  -0.0675 0.3695  523 GLY A CA  
4060 C C   . GLY A 523 ? 1.4120 1.1183 0.8989 0.1240  -0.0311 0.3667  523 GLY A C   
4061 O O   . GLY A 523 ? 1.3644 1.0490 0.9034 0.1264  -0.0161 0.3700  523 GLY A O   
4062 N N   . LYS A 524 ? 1.4117 1.1126 0.8609 0.1148  -0.0162 0.3582  524 LYS A N   
4063 C CA  . LYS A 524 ? 1.3721 1.0427 0.8409 0.1072  0.0173  0.3531  524 LYS A CA  
4064 C C   . LYS A 524 ? 1.3101 0.9693 0.7702 0.0943  0.0272  0.3180  524 LYS A C   
4065 O O   . LYS A 524 ? 1.3114 0.9844 0.7338 0.0902  0.0112  0.2988  524 LYS A O   
4066 C CB  . LYS A 524 ? 1.4577 1.1277 0.8961 0.1076  0.0311  0.3723  524 LYS A CB  
4067 C CG  . LYS A 524 ? 1.4626 1.1528 0.8382 0.1017  0.0244  0.3614  524 LYS A CG  
4068 C CD  . LYS A 524 ? 1.5554 1.2420 0.9048 0.1015  0.0424  0.3812  524 LYS A CD  
4069 C CE  . LYS A 524 ? 1.5460 1.2529 0.8339 0.0945  0.0397  0.3668  524 LYS A CE  
4070 N NZ  . LYS A 524 ? 1.5319 1.2340 0.7949 0.0935  0.0605  0.3858  524 LYS A NZ  
4071 N N   . PHE A 525 ? 1.2339 0.8672 0.7299 0.0873  0.0528  0.3077  525 PHE A N   
4072 C CA  . PHE A 525 ? 1.1526 0.7723 0.6481 0.0752  0.0620  0.2754  525 PHE A CA  
4073 C C   . PHE A 525 ? 1.1489 0.7713 0.5960 0.0689  0.0693  0.2632  525 PHE A C   
4074 O O   . PHE A 525 ? 1.2650 0.8896 0.6963 0.0706  0.0828  0.2782  525 PHE A O   
4075 C CB  . PHE A 525 ? 1.0964 0.6938 0.6440 0.0690  0.0864  0.2676  525 PHE A CB  
4076 C CG  . PHE A 525 ? 1.1255 0.7192 0.7234 0.0736  0.0824  0.2735  525 PHE A CG  
4077 C CD1 . PHE A 525 ? 1.0093 0.6006 0.6266 0.0691  0.0741  0.2536  525 PHE A CD1 
4078 C CD2 . PHE A 525 ? 1.0632 0.6544 0.6888 0.0823  0.0881  0.2982  525 PHE A CD2 
4079 C CE1 . PHE A 525 ? 0.9766 0.5659 0.6406 0.0733  0.0725  0.2572  525 PHE A CE1 
4080 C CE2 . PHE A 525 ? 1.0013 0.5882 0.6743 0.0870  0.0862  0.3008  525 PHE A CE2 
4081 C CZ  . PHE A 525 ? 0.9720 0.5593 0.6647 0.0825  0.0789  0.2798  525 PHE A CZ  
4082 N N   . LEU A 526 ? 1.1735 0.7943 0.5977 0.0613  0.0611  0.2351  526 LEU A N   
4083 C CA  . LEU A 526 ? 1.1661 0.7868 0.5495 0.0545  0.0699  0.2176  526 LEU A CA  
4084 C C   . LEU A 526 ? 1.1157 0.7152 0.5220 0.0467  0.0989  0.2060  526 LEU A C   
4085 O O   . LEU A 526 ? 1.1291 0.7284 0.5095 0.0435  0.1135  0.1999  526 LEU A O   
4086 C CB  . LEU A 526 ? 1.1197 0.7444 0.4732 0.0483  0.0498  0.1895  526 LEU A CB  
4087 C CG  . LEU A 526 ? 1.2615 0.9129 0.5845 0.0534  0.0187  0.1932  526 LEU A CG  
4088 C CD1 . LEU A 526 ? 1.2951 0.9510 0.6113 0.0430  -0.0002 0.1590  526 LEU A CD1 
4089 C CD2 . LEU A 526 ? 1.3531 1.0284 0.6332 0.0574  0.0184  0.2041  526 LEU A CD2 
4090 N N   . TRP A 527 ? 1.0998 0.6846 0.5550 0.0432  0.1074  0.2017  527 TRP A N   
4091 C CA  . TRP A 527 ? 1.0154 0.5849 0.4978 0.0350  0.1319  0.1887  527 TRP A CA  
4092 C C   . TRP A 527 ? 1.0708 0.6347 0.5985 0.0371  0.1483  0.2055  527 TRP A C   
4093 O O   . TRP A 527 ? 1.0622 0.6275 0.6196 0.0416  0.1396  0.2159  527 TRP A O   
4094 C CB  . TRP A 527 ? 0.8832 0.4437 0.3849 0.0266  0.1270  0.1638  527 TRP A CB  
4095 C CG  . TRP A 527 ? 0.8694 0.4194 0.3971 0.0179  0.1487  0.1484  527 TRP A CG  
4096 C CD1 . TRP A 527 ? 0.9078 0.4537 0.4847 0.0126  0.1569  0.1415  527 TRP A CD1 
4097 C CD2 . TRP A 527 ? 0.9244 0.4702 0.4319 0.0133  0.1648  0.1365  527 TRP A CD2 
4098 N NE1 . TRP A 527 ? 0.8723 0.4131 0.4606 0.0049  0.1753  0.1271  527 TRP A NE1 
4099 C CE2 . TRP A 527 ? 0.8675 0.4070 0.4152 0.0057  0.1815  0.1249  527 TRP A CE2 
4100 C CE3 . TRP A 527 ? 0.9601 0.5094 0.4208 0.0148  0.1671  0.1329  527 TRP A CE3 
4101 C CZ2 . TRP A 527 ? 0.9112 0.4470 0.4557 0.0002  0.2006  0.1125  527 TRP A CZ2 
4102 C CZ3 . TRP A 527 ? 0.9790 0.5234 0.4369 0.0096  0.1876  0.1189  527 TRP A CZ3 
4103 C CH2 . TRP A 527 ? 0.8727 0.4101 0.3731 0.0028  0.2043  0.1101  527 TRP A CH2 
4104 N N   . PRO A 528 ? 1.0671 0.6243 0.6029 0.0337  0.1726  0.2077  528 PRO A N   
4105 C CA  . PRO A 528 ? 1.0192 0.5693 0.5992 0.0346  0.1885  0.2217  528 PRO A CA  
4106 C C   . PRO A 528 ? 1.0002 0.5437 0.6322 0.0280  0.1918  0.2049  528 PRO A C   
4107 O O   . PRO A 528 ? 0.9824 0.5229 0.6504 0.0309  0.1936  0.2148  528 PRO A O   
4108 C CB  . PRO A 528 ? 1.0351 0.5801 0.6078 0.0307  0.2137  0.2236  528 PRO A CB  
4109 C CG  . PRO A 528 ? 1.0270 0.5738 0.5687 0.0251  0.2142  0.2015  528 PRO A CG  
4110 C CD  . PRO A 528 ? 1.0597 0.6160 0.5647 0.0296  0.1872  0.1984  528 PRO A CD  
4111 N N   . GLY A 529 ? 0.9531 0.4951 0.5897 0.0191  0.1927  0.1792  529 GLY A N   
4112 C CA  . GLY A 529 ? 0.8911 0.4322 0.5726 0.0120  0.1935  0.1617  529 GLY A CA  
4113 C C   . GLY A 529 ? 0.8908 0.4270 0.6143 0.0053  0.2170  0.1566  529 GLY A C   
4114 O O   . GLY A 529 ? 0.8943 0.4260 0.6134 0.0044  0.2352  0.1633  529 GLY A O   
4115 N N   . PHE A 530 ? 0.8430 0.3813 0.6081 0.0001  0.2167  0.1429  530 PHE A N   
4116 C CA  . PHE A 530 ? 0.8797 0.4159 0.6898 -0.0080 0.2368  0.1325  530 PHE A CA  
4117 C C   . PHE A 530 ? 0.8665 0.4044 0.6751 -0.0174 0.2510  0.1174  530 PHE A C   
4118 O O   . PHE A 530 ? 0.8685 0.4127 0.6665 -0.0224 0.2422  0.1010  530 PHE A O   
4119 C CB  . PHE A 530 ? 0.8196 0.3467 0.6448 -0.0013 0.2487  0.1546  530 PHE A CB  
4120 C CG  . PHE A 530 ? 0.8570 0.3832 0.6904 0.0079  0.2351  0.1682  530 PHE A CG  
4121 C CD1 . PHE A 530 ? 0.8367 0.3651 0.7094 0.0044  0.2342  0.1536  530 PHE A CD1 
4122 C CD2 . PHE A 530 ? 0.8762 0.4015 0.6781 0.0202  0.2235  0.1949  530 PHE A CD2 
4123 C CE1 . PHE A 530 ? 0.8170 0.3442 0.7003 0.0135  0.2236  0.1656  530 PHE A CE1 
4124 C CE2 . PHE A 530 ? 0.9032 0.4290 0.7162 0.0293  0.2109  0.2081  530 PHE A CE2 
4125 C CZ  . PHE A 530 ? 0.8326 0.3582 0.6878 0.0263  0.2117  0.1935  530 PHE A CZ  
4126 N N   . GLY A 531 ? 0.8568 0.3894 0.6775 -0.0199 0.2730  0.1228  531 GLY A N   
4127 C CA  . GLY A 531 ? 0.8670 0.4030 0.6927 -0.0292 0.2882  0.1079  531 GLY A CA  
4128 C C   . GLY A 531 ? 0.9203 0.4567 0.7001 -0.0263 0.2829  0.1088  531 GLY A C   
4129 O O   . GLY A 531 ? 0.8818 0.4232 0.6664 -0.0340 0.2906  0.0926  531 GLY A O   
4130 N N   . GLU A 532 ? 0.9156 0.4482 0.6521 -0.0157 0.2703  0.1266  532 GLU A N   
4131 C CA  . GLU A 532 ? 0.8887 0.4219 0.5788 -0.0132 0.2653  0.1245  532 GLU A CA  
4132 C C   . GLU A 532 ? 0.9114 0.4479 0.5940 -0.0163 0.2475  0.1067  532 GLU A C   
4133 O O   . GLU A 532 ? 0.9378 0.4735 0.5899 -0.0165 0.2467  0.0991  532 GLU A O   
4134 C CB  . GLU A 532 ? 0.9262 0.4582 0.5714 -0.0021 0.2556  0.1468  532 GLU A CB  
4135 C CG  . GLU A 532 ? 0.9935 0.5222 0.6413 0.0021  0.2721  0.1692  532 GLU A CG  
4136 C CD  . GLU A 532 ? 0.9790 0.5063 0.6236 -0.0028 0.2973  0.1660  532 GLU A CD  
4137 O OE1 . GLU A 532 ? 1.0483 0.5784 0.6850 -0.0081 0.3017  0.1469  532 GLU A OE1 
4138 O OE2 . GLU A 532 ? 1.0791 0.6026 0.7308 -0.0011 0.3136  0.1833  532 GLU A OE2 
4139 N N   . ASN A 533 ? 0.8404 0.3808 0.5506 -0.0187 0.2345  0.0995  533 ASN A N   
4140 C CA  . ASN A 533 ? 0.8796 0.4236 0.5869 -0.0224 0.2185  0.0834  533 ASN A CA  
4141 C C   . ASN A 533 ? 0.8673 0.4218 0.5956 -0.0307 0.2268  0.0630  533 ASN A C   
4142 O O   . ASN A 533 ? 0.8303 0.3995 0.5605 -0.0309 0.2096  0.0478  533 ASN A O   
4143 C CB  . ASN A 533 ? 0.8336 0.3840 0.5696 -0.0233 0.2046  0.0793  533 ASN A CB  
4144 C CG  . ASN A 533 ? 0.8314 0.3798 0.5514 -0.0134 0.1906  0.0970  533 ASN A CG  
4145 O OD1 . ASN A 533 ? 0.8157 0.3603 0.4956 -0.0065 0.1829  0.1086  533 ASN A OD1 
4146 N ND2 . ASN A 533 ? 0.7701 0.3224 0.5220 -0.0128 0.1874  0.0984  533 ASN A ND2 
4147 N N   . SER A 534 ? 0.8655 0.4176 0.6144 -0.0366 0.2514  0.0624  534 SER A N   
4148 C CA  . SER A 534 ? 0.8789 0.4492 0.6503 -0.0424 0.2575  0.0430  534 SER A CA  
4149 C C   . SER A 534 ? 0.8112 0.3858 0.5496 -0.0357 0.2529  0.0393  534 SER A C   
4150 O O   . SER A 534 ? 0.8105 0.4023 0.5649 -0.0367 0.2484  0.0225  534 SER A O   
4151 C CB  . SER A 534 ? 0.8296 0.3970 0.6316 -0.0508 0.2867  0.0438  534 SER A CB  
4152 O OG  . SER A 534 ? 0.9419 0.4941 0.7160 -0.0455 0.3035  0.0631  534 SER A OG  
4153 N N   . ARG A 535 ? 0.8875 0.4479 0.5807 -0.0286 0.2540  0.0542  535 ARG A N   
4154 C CA  . ARG A 535 ? 0.8928 0.4563 0.5525 -0.0230 0.2490  0.0468  535 ARG A CA  
4155 C C   . ARG A 535 ? 0.8912 0.4630 0.5488 -0.0203 0.2215  0.0342  535 ARG A C   
4156 O O   . ARG A 535 ? 0.8133 0.3925 0.4702 -0.0184 0.2180  0.0196  535 ARG A O   
4157 C CB  . ARG A 535 ? 0.8646 0.4145 0.4729 -0.0169 0.2544  0.0642  535 ARG A CB  
4158 C CG  . ARG A 535 ? 0.9089 0.4479 0.5153 -0.0187 0.2830  0.0826  535 ARG A CG  
4159 C CD  . ARG A 535 ? 1.0671 0.6033 0.6291 -0.0099 0.2774  0.1013  535 ARG A CD  
4160 N NE  . ARG A 535 ? 1.0249 0.5610 0.5999 -0.0088 0.2949  0.1186  535 ARG A NE  
4161 C CZ  . ARG A 535 ? 1.1135 0.6520 0.6773 -0.0091 0.3159  0.1209  535 ARG A CZ  
4162 N NH1 . ARG A 535 ? 1.1167 0.6596 0.6582 -0.0099 0.3229  0.1051  535 ARG A NH1 
4163 N NH2 . ARG A 535 ? 1.0707 0.6075 0.6477 -0.0084 0.3310  0.1392  535 ARG A NH2 
4164 N N   . VAL A 536 ? 0.8347 0.4045 0.4940 -0.0200 0.2035  0.0402  536 VAL A N   
4165 C CA  . VAL A 536 ? 0.7810 0.3586 0.4424 -0.0188 0.1795  0.0299  536 VAL A CA  
4166 C C   . VAL A 536 ? 0.7663 0.3602 0.4680 -0.0231 0.1775  0.0157  536 VAL A C   
4167 O O   . VAL A 536 ? 0.8085 0.4101 0.5133 -0.0209 0.1664  0.0053  536 VAL A O   
4168 C CB  . VAL A 536 ? 0.8195 0.3930 0.4747 -0.0175 0.1631  0.0406  536 VAL A CB  
4169 C CG1 . VAL A 536 ? 0.7673 0.3499 0.4306 -0.0180 0.1412  0.0305  536 VAL A CG1 
4170 C CG2 . VAL A 536 ? 0.7793 0.3425 0.3930 -0.0117 0.1607  0.0551  536 VAL A CG2 
4171 N N   . LEU A 537 ? 0.8216 0.4219 0.5557 -0.0292 0.1881  0.0152  537 LEU A N   
4172 C CA  . LEU A 537 ? 0.7769 0.3986 0.5480 -0.0336 0.1845  0.0011  537 LEU A CA  
4173 C C   . LEU A 537 ? 0.7195 0.3520 0.5002 -0.0314 0.1928  -0.0085 537 LEU A C   
4174 O O   . LEU A 537 ? 0.7425 0.3932 0.5430 -0.0300 0.1824  -0.0179 537 LEU A O   
4175 C CB  . LEU A 537 ? 0.7473 0.3751 0.5519 -0.0424 0.1954  -0.0013 537 LEU A CB  
4176 C CG  . LEU A 537 ? 0.7841 0.4042 0.5920 -0.0450 0.1893  0.0044  537 LEU A CG  
4177 C CD1 . LEU A 537 ? 0.8173 0.4500 0.6665 -0.0553 0.1985  -0.0075 537 LEU A CD1 
4178 C CD2 . LEU A 537 ? 0.6222 0.2472 0.4173 -0.0412 0.1659  0.0037  537 LEU A CD2 
4179 N N   . GLU A 538 ? 0.7379 0.3606 0.5053 -0.0300 0.2123  -0.0050 538 GLU A N   
4180 C CA  . GLU A 538 ? 0.7600 0.3928 0.5378 -0.0269 0.2226  -0.0150 538 GLU A CA  
4181 C C   . GLU A 538 ? 0.7146 0.3463 0.4770 -0.0188 0.2070  -0.0212 538 GLU A C   
4182 O O   . GLU A 538 ? 0.7208 0.3675 0.5077 -0.0151 0.2056  -0.0308 538 GLU A O   
4183 C CB  . GLU A 538 ? 0.8221 0.4428 0.5816 -0.0268 0.2480  -0.0093 538 GLU A CB  
4184 C CG  . GLU A 538 ? 0.7990 0.4285 0.5659 -0.0224 0.2612  -0.0206 538 GLU A CG  
4185 C CD  . GLU A 538 ? 0.8605 0.4790 0.6056 -0.0230 0.2887  -0.0147 538 GLU A CD  
4186 O OE1 . GLU A 538 ? 0.8447 0.4445 0.5482 -0.0222 0.2908  -0.0011 538 GLU A OE1 
4187 O OE2 . GLU A 538 ? 0.8896 0.5203 0.6597 -0.0238 0.3085  -0.0226 538 GLU A OE2 
4188 N N   . TRP A 539 ? 0.7462 0.3609 0.4715 -0.0159 0.1953  -0.0157 539 TRP A N   
4189 C CA  . TRP A 539 ? 0.7244 0.3351 0.4379 -0.0100 0.1818  -0.0231 539 TRP A CA  
4190 C C   . TRP A 539 ? 0.7469 0.3702 0.4868 -0.0097 0.1629  -0.0250 539 TRP A C   
4191 O O   . TRP A 539 ? 0.7105 0.3382 0.4636 -0.0043 0.1580  -0.0316 539 TRP A O   
4192 C CB  . TRP A 539 ? 0.7883 0.3811 0.4579 -0.0090 0.1733  -0.0188 539 TRP A CB  
4193 C CG  . TRP A 539 ? 0.8113 0.3978 0.4713 -0.0052 0.1608  -0.0291 539 TRP A CG  
4194 C CD1 . TRP A 539 ? 0.7792 0.3598 0.4318 -0.0009 0.1698  -0.0421 539 TRP A CD1 
4195 C CD2 . TRP A 539 ? 0.8090 0.3932 0.4693 -0.0061 0.1393  -0.0283 539 TRP A CD2 
4196 N NE1 . TRP A 539 ? 0.8208 0.3933 0.4704 0.0007  0.1551  -0.0499 539 TRP A NE1 
4197 C CE2 . TRP A 539 ? 0.8023 0.3773 0.4567 -0.0028 0.1363  -0.0408 539 TRP A CE2 
4198 C CE3 . TRP A 539 ? 0.7094 0.2980 0.3767 -0.0097 0.1241  -0.0191 539 TRP A CE3 
4199 C CZ2 . TRP A 539 ? 0.7878 0.3570 0.4442 -0.0040 0.1187  -0.0430 539 TRP A CZ2 
4200 C CZ3 . TRP A 539 ? 0.7536 0.3390 0.4211 -0.0103 0.1069  -0.0209 539 TRP A CZ3 
4201 C CH2 . TRP A 539 ? 0.7776 0.3530 0.4403 -0.0079 0.1043  -0.0322 539 TRP A CH2 
4202 N N   . MET A 540 ? 0.7014 0.3308 0.4496 -0.0148 0.1534  -0.0185 540 MET A N   
4203 C CA  . MET A 540 ? 0.6680 0.3129 0.4385 -0.0151 0.1373  -0.0195 540 MET A CA  
4204 C C   . MET A 540 ? 0.6952 0.3639 0.5014 -0.0136 0.1416  -0.0260 540 MET A C   
4205 O O   . MET A 540 ? 0.6911 0.3713 0.5117 -0.0087 0.1303  -0.0266 540 MET A O   
4206 C CB  . MET A 540 ? 0.6251 0.2739 0.3987 -0.0216 0.1304  -0.0142 540 MET A CB  
4207 C CG  . MET A 540 ? 0.6468 0.2778 0.3923 -0.0219 0.1226  -0.0064 540 MET A CG  
4208 S SD  . MET A 540 ? 0.7564 0.3922 0.5145 -0.0285 0.1216  -0.0016 540 MET A SD  
4209 C CE  . MET A 540 ? 0.6901 0.3086 0.4187 -0.0259 0.1105  0.0089  540 MET A CE  
4210 N N   . PHE A 541 ? 0.6682 0.3459 0.4912 -0.0178 0.1579  -0.0297 541 PHE A N   
4211 C CA  . PHE A 541 ? 0.6678 0.3732 0.5289 -0.0170 0.1620  -0.0373 541 PHE A CA  
4212 C C   . PHE A 541 ? 0.6755 0.3814 0.5424 -0.0062 0.1634  -0.0403 541 PHE A C   
4213 O O   . PHE A 541 ? 0.6911 0.4180 0.5837 -0.0005 0.1533  -0.0411 541 PHE A O   
4214 C CB  . PHE A 541 ? 0.6785 0.3898 0.5571 -0.0246 0.1828  -0.0416 541 PHE A CB  
4215 C CG  . PHE A 541 ? 0.6590 0.4057 0.5831 -0.0282 0.1838  -0.0513 541 PHE A CG  
4216 C CD1 . PHE A 541 ? 0.6031 0.3679 0.5522 -0.0211 0.1885  -0.0566 541 PHE A CD1 
4217 C CD2 . PHE A 541 ? 0.6972 0.4611 0.6415 -0.0388 0.1803  -0.0567 541 PHE A CD2 
4218 C CE1 . PHE A 541 ? 0.6701 0.4729 0.6637 -0.0241 0.1874  -0.0656 541 PHE A CE1 
4219 C CE2 . PHE A 541 ? 0.6801 0.4812 0.6665 -0.0436 0.1795  -0.0683 541 PHE A CE2 
4220 C CZ  . PHE A 541 ? 0.7486 0.5709 0.7599 -0.0360 0.1819  -0.0720 541 PHE A CZ  
4221 N N   . GLY A 542 ? 0.6044 0.2877 0.4474 -0.0027 0.1762  -0.0417 542 GLY A N   
4222 C CA  . GLY A 542 ? 0.7216 0.4019 0.5712 0.0075  0.1805  -0.0476 542 GLY A CA  
4223 C C   . GLY A 542 ? 0.7317 0.4045 0.5776 0.0141  0.1619  -0.0444 542 GLY A C   
4224 O O   . GLY A 542 ? 0.7209 0.4023 0.5923 0.0234  0.1597  -0.0459 542 GLY A O   
4225 N N   . ARG A 543 ? 0.6819 0.3386 0.4995 0.0097  0.1491  -0.0389 543 ARG A N   
4226 C CA  . ARG A 543 ? 0.7077 0.3563 0.5238 0.0140  0.1328  -0.0349 543 ARG A CA  
4227 C C   . ARG A 543 ? 0.7057 0.3798 0.5526 0.0169  0.1200  -0.0272 543 ARG A C   
4228 O O   . ARG A 543 ? 0.7585 0.4316 0.6189 0.0250  0.1124  -0.0226 543 ARG A O   
4229 C CB  . ARG A 543 ? 0.6615 0.2925 0.4453 0.0072  0.1224  -0.0309 543 ARG A CB  
4230 C CG  . ARG A 543 ? 0.8052 0.4122 0.5555 0.0064  0.1294  -0.0383 543 ARG A CG  
4231 C CD  . ARG A 543 ? 0.7521 0.3449 0.5065 0.0132  0.1316  -0.0478 543 ARG A CD  
4232 N NE  . ARG A 543 ? 0.6870 0.2765 0.4551 0.0148  0.1162  -0.0420 543 ARG A NE  
4233 C CZ  . ARG A 543 ? 0.8008 0.3783 0.5843 0.0214  0.1167  -0.0464 543 ARG A CZ  
4234 N NH1 . ARG A 543 ? 0.8139 0.3818 0.6017 0.0275  0.1316  -0.0593 543 ARG A NH1 
4235 N NH2 . ARG A 543 ? 0.7868 0.3607 0.5830 0.0219  0.1039  -0.0374 543 ARG A NH2 
4236 N N   . ILE A 544 ? 0.7225 0.4200 0.5809 0.0105  0.1179  -0.0257 544 ILE A N   
4237 C CA  . ILE A 544 ? 0.6887 0.4169 0.5734 0.0127  0.1053  -0.0203 544 ILE A CA  
4238 C C   . ILE A 544 ? 0.6427 0.3905 0.5614 0.0232  0.1094  -0.0219 544 ILE A C   
4239 O O   . ILE A 544 ? 0.7143 0.4779 0.6512 0.0319  0.0975  -0.0130 544 ILE A O   
4240 C CB  . ILE A 544 ? 0.6782 0.4276 0.5677 0.0016  0.1037  -0.0235 544 ILE A CB  
4241 C CG1 . ILE A 544 ? 0.6254 0.3582 0.4874 -0.0060 0.0970  -0.0195 544 ILE A CG1 
4242 C CG2 . ILE A 544 ? 0.5649 0.3541 0.4826 0.0033  0.0920  -0.0222 544 ILE A CG2 
4243 C CD1 . ILE A 544 ? 0.5808 0.3280 0.4480 -0.0170 0.0989  -0.0249 544 ILE A CD1 
4244 N N   . GLU A 545 ? 0.6077 0.3555 0.5366 0.0236  0.1271  -0.0315 545 GLU A N   
4245 C CA  . GLU A 545 ? 0.6864 0.4528 0.6515 0.0346  0.1334  -0.0342 545 GLU A CA  
4246 C C   . GLU A 545 ? 0.6972 0.4402 0.6622 0.0475  0.1353  -0.0319 545 GLU A C   
4247 O O   . GLU A 545 ? 0.6641 0.4216 0.6634 0.0596  0.1390  -0.0318 545 GLU A O   
4248 C CB  . GLU A 545 ? 0.6377 0.4100 0.6148 0.0302  0.1551  -0.0459 545 GLU A CB  
4249 C CG  . GLU A 545 ? 0.6709 0.4732 0.6670 0.0187  0.1556  -0.0504 545 GLU A CG  
4250 C CD  . GLU A 545 ? 0.7399 0.5494 0.7555 0.0147  0.1793  -0.0606 545 GLU A CD  
4251 O OE1 . GLU A 545 ? 0.8389 0.6215 0.8347 0.0168  0.1972  -0.0634 545 GLU A OE1 
4252 O OE2 . GLU A 545 ? 0.7357 0.5794 0.7869 0.0088  0.1807  -0.0668 545 GLU A OE2 
4253 N N   . GLY A 546 ? 0.6656 0.3741 0.5970 0.0453  0.1332  -0.0311 546 GLY A N   
4254 C CA  . GLY A 546 ? 0.6929 0.3765 0.6260 0.0554  0.1358  -0.0319 546 GLY A CA  
4255 C C   . GLY A 546 ? 0.7796 0.4399 0.6997 0.0564  0.1562  -0.0479 546 GLY A C   
4256 O O   . GLY A 546 ? 0.8672 0.5148 0.8040 0.0671  0.1640  -0.0532 546 GLY A O   
4257 N N   . GLU A 547 ? 0.7930 0.4473 0.6839 0.0461  0.1663  -0.0554 547 GLU A N   
4258 C CA  . GLU A 547 ? 0.8153 0.4499 0.6863 0.0464  0.1863  -0.0701 547 GLU A CA  
4259 C C   . GLU A 547 ? 0.8495 0.4517 0.6876 0.0446  0.1817  -0.0768 547 GLU A C   
4260 O O   . GLU A 547 ? 0.7655 0.3596 0.5843 0.0382  0.1651  -0.0695 547 GLU A O   
4261 C CB  . GLU A 547 ? 0.7853 0.4249 0.6341 0.0365  0.1990  -0.0720 547 GLU A CB  
4262 C CG  . GLU A 547 ? 0.8311 0.5018 0.7163 0.0360  0.2077  -0.0701 547 GLU A CG  
4263 C CD  . GLU A 547 ? 1.0264 0.6962 0.8940 0.0275  0.2279  -0.0731 547 GLU A CD  
4264 O OE1 . GLU A 547 ? 1.0658 0.7127 0.8941 0.0258  0.2389  -0.0782 547 GLU A OE1 
4265 O OE2 . GLU A 547 ? 1.0230 0.7158 0.9159 0.0220  0.2330  -0.0704 547 GLU A OE2 
4266 N N   . ASP A 548 ? 0.9752 0.5605 0.8090 0.0497  0.1976  -0.0928 548 ASP A N   
4267 C CA  . ASP A 548 ? 0.9871 0.5429 0.7931 0.0472  0.1952  -0.1050 548 ASP A CA  
4268 C C   . ASP A 548 ? 1.0034 0.5515 0.7569 0.0366  0.1999  -0.1124 548 ASP A C   
4269 O O   . ASP A 548 ? 1.0125 0.5494 0.7426 0.0365  0.2157  -0.1298 548 ASP A O   
4270 C CB  . ASP A 548 ? 1.0408 0.5822 0.8692 0.0576  0.2107  -0.1215 548 ASP A CB  
4271 C CG  . ASP A 548 ? 1.1222 0.6331 0.9340 0.0546  0.2061  -0.1354 548 ASP A CG  
4272 O OD1 . ASP A 548 ? 1.1565 0.6610 0.9491 0.0459  0.1875  -0.1282 548 ASP A OD1 
4273 O OD2 . ASP A 548 ? 1.1932 0.6941 1.0164 0.0595  0.2190  -0.1531 548 ASP A OD2 
4274 N N   . SER A 549 ? 0.8969 0.4526 0.6317 0.0284  0.1859  -0.0982 549 SER A N   
4275 C CA  . SER A 549 ? 0.9065 0.4589 0.5950 0.0202  0.1883  -0.0984 549 SER A CA  
4276 C C   . SER A 549 ? 0.8696 0.4122 0.5313 0.0130  0.1675  -0.0950 549 SER A C   
4277 O O   . SER A 549 ? 0.8903 0.4341 0.5171 0.0073  0.1647  -0.0897 549 SER A O   
4278 C CB  . SER A 549 ? 0.8340 0.4045 0.5269 0.0172  0.1945  -0.0840 549 SER A CB  
4279 O OG  . SER A 549 ? 0.8371 0.4189 0.5515 0.0149  0.1774  -0.0696 549 SER A OG  
4280 N N   . ALA A 550 ? 0.8651 0.3990 0.5445 0.0136  0.1536  -0.0967 550 ALA A N   
4281 C CA  . ALA A 550 ? 0.8811 0.4094 0.5446 0.0062  0.1337  -0.0927 550 ALA A CA  
4282 C C   . ALA A 550 ? 0.9070 0.4162 0.5542 0.0030  0.1316  -0.1130 550 ALA A C   
4283 O O   . ALA A 550 ? 0.8127 0.3093 0.4762 0.0078  0.1424  -0.1279 550 ALA A O   
4284 C CB  . ALA A 550 ? 0.8422 0.3765 0.5386 0.0069  0.1196  -0.0777 550 ALA A CB  
4285 N N   . LYS A 551 ? 0.9219 0.4304 0.5401 -0.0054 0.1174  -0.1145 551 LYS A N   
4286 C CA  . LYS A 551 ? 0.8961 0.3907 0.5005 -0.0117 0.1106  -0.1349 551 LYS A CA  
4287 C C   . LYS A 551 ? 0.9106 0.4056 0.5287 -0.0185 0.0900  -0.1262 551 LYS A C   
4288 O O   . LYS A 551 ? 0.8894 0.3986 0.5010 -0.0208 0.0787  -0.1086 551 LYS A O   
4289 C CB  . LYS A 551 ? 0.8957 0.3948 0.4495 -0.0161 0.1120  -0.1474 551 LYS A CB  
4290 C CG  . LYS A 551 ? 0.9801 0.4713 0.5163 -0.0250 0.1016  -0.1710 551 LYS A CG  
4291 C CD  . LYS A 551 ? 1.1572 0.6588 0.6383 -0.0283 0.1021  -0.1818 551 LYS A CD  
4292 C CE  . LYS A 551 ? 1.1620 0.6828 0.6203 -0.0280 0.0904  -0.1558 551 LYS A CE  
4293 N NZ  . LYS A 551 ? 1.3653 0.8984 0.7677 -0.0297 0.0894  -0.1615 551 LYS A NZ  
4294 N N   . LEU A 552 ? 0.8636 0.3421 0.5037 -0.0216 0.0871  -0.1385 552 LEU A N   
4295 C CA  . LEU A 552 ? 0.8820 0.3597 0.5411 -0.0287 0.0707  -0.1301 552 LEU A CA  
4296 C C   . LEU A 552 ? 0.9110 0.3955 0.5420 -0.0399 0.0554  -0.1413 552 LEU A C   
4297 O O   . LEU A 552 ? 0.9002 0.3786 0.5091 -0.0447 0.0572  -0.1660 552 LEU A O   
4298 C CB  . LEU A 552 ? 0.8548 0.3103 0.5517 -0.0281 0.0755  -0.1371 552 LEU A CB  
4299 C CG  . LEU A 552 ? 0.8919 0.3450 0.6136 -0.0359 0.0622  -0.1274 552 LEU A CG  
4300 C CD1 . LEU A 552 ? 0.8841 0.3564 0.6110 -0.0335 0.0540  -0.0990 552 LEU A CD1 
4301 C CD2 . LEU A 552 ? 0.8180 0.2609 0.5870 -0.0322 0.0685  -0.1271 552 LEU A CD2 
4302 N N   . THR A 553 ? 0.8810 0.3805 0.5136 -0.0439 0.0404  -0.1243 553 THR A N   
4303 C CA  . THR A 553 ? 0.8480 0.3593 0.4620 -0.0534 0.0231  -0.1309 553 THR A CA  
4304 C C   . THR A 553 ? 0.8177 0.3300 0.4645 -0.0605 0.0114  -0.1224 553 THR A C   
4305 O O   . THR A 553 ? 0.7736 0.2792 0.4509 -0.0570 0.0170  -0.1078 553 THR A O   
4306 C CB  . THR A 553 ? 0.8242 0.3566 0.4068 -0.0497 0.0174  -0.1160 553 THR A CB  
4307 O OG1 . THR A 553 ? 0.8205 0.3610 0.4229 -0.0450 0.0175  -0.0907 553 THR A OG1 
4308 C CG2 . THR A 553 ? 0.8342 0.3652 0.3843 -0.0431 0.0320  -0.1217 553 THR A CG2 
4309 N N   . PRO A 554 ? 0.8034 0.3263 0.4455 -0.0708 -0.0047 -0.1313 554 PRO A N   
4310 C CA  . PRO A 554 ? 0.7838 0.3103 0.4594 -0.0783 -0.0143 -0.1223 554 PRO A CA  
4311 C C   . PRO A 554 ? 0.8557 0.3968 0.5421 -0.0726 -0.0159 -0.0939 554 PRO A C   
4312 O O   . PRO A 554 ? 0.8189 0.3603 0.5353 -0.0769 -0.0179 -0.0837 554 PRO A O   
4313 C CB  . PRO A 554 ? 0.8147 0.3571 0.4793 -0.0897 -0.0322 -0.1389 554 PRO A CB  
4314 C CG  . PRO A 554 ? 0.8470 0.3834 0.4799 -0.0908 -0.0292 -0.1649 554 PRO A CG  
4315 C CD  . PRO A 554 ? 0.8417 0.3729 0.4517 -0.0774 -0.0139 -0.1544 554 PRO A CD  
4316 N N   . ILE A 555 ? 0.7690 0.3216 0.4328 -0.0638 -0.0134 -0.0816 555 ILE A N   
4317 C CA  . ILE A 555 ? 0.7680 0.3335 0.4434 -0.0591 -0.0133 -0.0585 555 ILE A CA  
4318 C C   . ILE A 555 ? 0.7780 0.3368 0.4609 -0.0506 0.0015  -0.0479 555 ILE A C   
4319 O O   . ILE A 555 ? 0.7818 0.3513 0.4764 -0.0478 0.0029  -0.0318 555 ILE A O   
4320 C CB  . ILE A 555 ? 0.7346 0.3185 0.3875 -0.0557 -0.0209 -0.0499 555 ILE A CB  
4321 C CG1 . ILE A 555 ? 0.7970 0.3769 0.4174 -0.0483 -0.0114 -0.0520 555 ILE A CG1 
4322 C CG2 . ILE A 555 ? 0.7626 0.3602 0.4111 -0.0631 -0.0387 -0.0584 555 ILE A CG2 
4323 C CD1 . ILE A 555 ? 0.7883 0.3829 0.3882 -0.0430 -0.0156 -0.0382 555 ILE A CD1 
4324 N N   . GLY A 556 ? 0.8086 0.3526 0.4873 -0.0465 0.0125  -0.0577 556 GLY A N   
4325 C CA  . GLY A 556 ? 0.8026 0.3445 0.4914 -0.0379 0.0253  -0.0489 556 GLY A CA  
4326 C C   . GLY A 556 ? 0.8072 0.3429 0.4757 -0.0323 0.0370  -0.0595 556 GLY A C   
4327 O O   . GLY A 556 ? 0.8204 0.3516 0.4642 -0.0350 0.0360  -0.0745 556 GLY A O   
4328 N N   . TYR A 557 ? 0.8015 0.3397 0.4807 -0.0246 0.0486  -0.0524 557 TYR A N   
4329 C CA  . TYR A 557 ? 0.7809 0.3151 0.4464 -0.0189 0.0628  -0.0614 557 TYR A CA  
4330 C C   . TYR A 557 ? 0.8298 0.3745 0.4671 -0.0189 0.0651  -0.0562 557 TYR A C   
4331 O O   . TYR A 557 ? 0.8139 0.3709 0.4568 -0.0190 0.0624  -0.0414 557 TYR A O   
4332 C CB  . TYR A 557 ? 0.7488 0.2860 0.4415 -0.0108 0.0738  -0.0552 557 TYR A CB  
4333 C CG  . TYR A 557 ? 0.8175 0.3430 0.5394 -0.0076 0.0738  -0.0564 557 TYR A CG  
4334 C CD1 . TYR A 557 ? 0.8356 0.3413 0.5597 -0.0060 0.0815  -0.0738 557 TYR A CD1 
4335 C CD2 . TYR A 557 ? 0.8475 0.3816 0.5950 -0.0058 0.0676  -0.0398 557 TYR A CD2 
4336 C CE1 . TYR A 557 ? 0.8400 0.3315 0.5953 -0.0020 0.0834  -0.0729 557 TYR A CE1 
4337 C CE2 . TYR A 557 ? 0.8241 0.3467 0.5987 -0.0016 0.0685  -0.0363 557 TYR A CE2 
4338 C CZ  . TYR A 557 ? 0.8802 0.3799 0.6607 0.0007  0.0767  -0.0520 557 TYR A CZ  
4339 O OH  . TYR A 557 ? 0.8955 0.3803 0.7071 0.0059  0.0794  -0.0466 557 TYR A OH  
4340 N N   . VAL A 558 ? 0.8401 0.3796 0.4472 -0.0189 0.0712  -0.0683 558 VAL A N   
4341 C CA  . VAL A 558 ? 0.8655 0.4128 0.4438 -0.0173 0.0772  -0.0611 558 VAL A CA  
4342 C C   . VAL A 558 ? 0.8699 0.4131 0.4427 -0.0121 0.0983  -0.0686 558 VAL A C   
4343 O O   . VAL A 558 ? 0.8751 0.4087 0.4601 -0.0099 0.1058  -0.0835 558 VAL A O   
4344 C CB  . VAL A 558 ? 0.8182 0.3683 0.3597 -0.0214 0.0654  -0.0656 558 VAL A CB  
4345 C CG1 . VAL A 558 ? 0.7888 0.3451 0.3430 -0.0267 0.0449  -0.0602 558 VAL A CG1 
4346 C CG2 . VAL A 558 ? 0.8973 0.4380 0.4174 -0.0234 0.0694  -0.0899 558 VAL A CG2 
4347 N N   . PRO A 559 ? 0.8867 0.4362 0.4451 -0.0099 0.1100  -0.0583 559 PRO A N   
4348 C CA  . PRO A 559 ? 0.8621 0.4096 0.4166 -0.0058 0.1324  -0.0655 559 PRO A CA  
4349 C C   . PRO A 559 ? 0.9145 0.4537 0.4350 -0.0062 0.1380  -0.0851 559 PRO A C   
4350 O O   . PRO A 559 ? 0.9859 0.5255 0.4721 -0.0099 0.1263  -0.0884 559 PRO A O   
4351 C CB  . PRO A 559 ? 0.8612 0.4160 0.4045 -0.0054 0.1428  -0.0480 559 PRO A CB  
4352 C CG  . PRO A 559 ? 0.8168 0.3774 0.3747 -0.0079 0.1272  -0.0322 559 PRO A CG  
4353 C CD  . PRO A 559 ? 0.8294 0.3873 0.3810 -0.0107 0.1060  -0.0387 559 PRO A CD  
4354 N N   . LYS A 560 ? 0.9220 0.4559 0.4535 -0.0021 0.1561  -0.0996 560 LYS A N   
4355 C CA  . LYS A 560 ? 1.0638 0.5900 0.5637 -0.0024 0.1664  -0.1218 560 LYS A CA  
4356 C C   . LYS A 560 ? 1.1768 0.7103 0.6275 -0.0033 0.1760  -0.1154 560 LYS A C   
4357 O O   . LYS A 560 ? 1.1419 0.6833 0.5884 -0.0029 0.1773  -0.0925 560 LYS A O   
4358 C CB  . LYS A 560 ? 1.0632 0.5835 0.5912 0.0038  0.1874  -0.1370 560 LYS A CB  
4359 C CG  . LYS A 560 ? 0.9699 0.4805 0.5433 0.0067  0.1800  -0.1440 560 LYS A CG  
4360 C CD  . LYS A 560 ? 0.9420 0.4489 0.5454 0.0153  0.2020  -0.1565 560 LYS A CD  
4361 C CE  . LYS A 560 ? 1.0283 0.5235 0.6769 0.0202  0.1957  -0.1611 560 LYS A CE  
4362 N NZ  . LYS A 560 ? 0.9640 0.4634 0.6508 0.0302  0.2141  -0.1697 560 LYS A NZ  
4363 N N   . GLU A 561 ? 1.3748 0.9051 0.7875 -0.0046 0.1841  -0.1361 561 GLU A N   
4364 C CA  . GLU A 561 ? 1.4449 0.9843 0.8082 -0.0044 0.1960  -0.1295 561 GLU A CA  
4365 C C   . GLU A 561 ? 1.4297 0.9721 0.8095 0.0002  0.2239  -0.1194 561 GLU A C   
4366 O O   . GLU A 561 ? 1.4551 0.9952 0.8714 0.0035  0.2386  -0.1324 561 GLU A O   
4367 C CB  . GLU A 561 ? 1.5751 1.1253 0.9120 -0.0074 0.1940  -0.1533 561 GLU A CB  
4368 C CG  . GLU A 561 ? 1.7103 1.2631 1.0306 -0.0137 0.1663  -0.1651 561 GLU A CG  
4369 C CD  . GLU A 561 ? 1.9111 1.4806 1.2016 -0.0172 0.1645  -0.1898 561 GLU A CD  
4370 O OE1 . GLU A 561 ? 1.8856 1.4653 1.1605 -0.0140 0.1846  -0.1940 561 GLU A OE1 
4371 O OE2 . GLU A 561 ? 1.9662 1.5403 1.2502 -0.0236 0.1435  -0.2062 561 GLU A OE2 
4372 N N   . ASP A 562 ? 1.2141 0.7632 0.5726 0.0006  0.2310  -0.0948 562 ASP A N   
4373 C CA  . ASP A 562 ? 1.2773 0.8304 0.6542 0.0028  0.2577  -0.0824 562 ASP A CA  
4374 C C   . ASP A 562 ? 1.2044 0.7562 0.6428 0.0041  0.2604  -0.0797 562 ASP A C   
4375 O O   . ASP A 562 ? 1.1885 0.7451 0.6534 0.0057  0.2835  -0.0788 562 ASP A O   
4376 C CB  . ASP A 562 ? 1.3866 0.9498 0.7580 0.0042  0.2785  -0.0981 562 ASP A CB  
4377 C CG  . ASP A 562 ? 1.4520 1.0283 0.7696 0.0028  0.2751  -0.0960 562 ASP A CG  
4378 O OD1 . ASP A 562 ? 1.4356 1.0161 0.7262 0.0025  0.2652  -0.0720 562 ASP A OD1 
4379 O OD2 . ASP A 562 ? 1.4812 1.0660 0.7854 0.0028  0.2819  -0.1182 562 ASP A OD2 
4380 N N   . ALA A 563 ? 1.2160 0.7664 0.6816 0.0032  0.2355  -0.0778 563 ALA A N   
4381 C CA  . ALA A 563 ? 1.0871 0.6431 0.6101 0.0042  0.2335  -0.0725 563 ALA A CA  
4382 C C   . ALA A 563 ? 0.9862 0.5486 0.5215 0.0012  0.2349  -0.0490 563 ALA A C   
4383 O O   . ALA A 563 ? 0.8870 0.4583 0.4639 0.0008  0.2449  -0.0459 563 ALA A O   
4384 C CB  . ALA A 563 ? 0.9910 0.5435 0.5366 0.0042  0.2087  -0.0788 563 ALA A CB  
4385 N N   . LEU A 564 ? 0.9788 0.5379 0.4816 -0.0009 0.2252  -0.0333 564 LEU A N   
4386 C CA  . LEU A 564 ? 0.9699 0.5308 0.4835 -0.0032 0.2305  -0.0111 564 LEU A CA  
4387 C C   . LEU A 564 ? 0.9772 0.5372 0.4758 -0.0034 0.2601  -0.0025 564 LEU A C   
4388 O O   . LEU A 564 ? 1.0689 0.6263 0.5260 -0.0013 0.2715  -0.0073 564 LEU A O   
4389 C CB  . LEU A 564 ? 0.9924 0.5498 0.4804 -0.0033 0.2107  0.0049  564 LEU A CB  
4390 C CG  . LEU A 564 ? 0.9949 0.5545 0.5044 -0.0046 0.1837  0.0029  564 LEU A CG  
4391 C CD1 . LEU A 564 ? 1.0133 0.5719 0.4992 -0.0036 0.1681  0.0202  564 LEU A CD1 
4392 C CD2 . LEU A 564 ? 0.9477 0.5133 0.5089 -0.0072 0.1853  0.0039  564 LEU A CD2 
4393 N N   . ASN A 565 ? 1.0273 0.5901 0.5604 -0.0068 0.2737  0.0092  565 ASN A N   
4394 C CA  . ASN A 565 ? 1.0251 0.5851 0.5493 -0.0085 0.3034  0.0222  565 ASN A CA  
4395 C C   . ASN A 565 ? 1.0355 0.5852 0.5214 -0.0070 0.3007  0.0481  565 ASN A C   
4396 O O   . ASN A 565 ? 0.9863 0.5320 0.4922 -0.0086 0.2913  0.0624  565 ASN A O   
4397 C CB  . ASN A 565 ? 1.0024 0.5700 0.5845 -0.0144 0.3187  0.0228  565 ASN A CB  
4398 C CG  . ASN A 565 ? 1.0962 0.6620 0.6779 -0.0177 0.3536  0.0327  565 ASN A CG  
4399 O OD1 . ASN A 565 ? 1.1274 0.6890 0.6706 -0.0144 0.3591  0.0447  565 ASN A OD1 
4400 N ND2 . ASN A 565 ? 1.1015 0.6783 0.7370 -0.0238 0.3694  0.0264  565 ASN A ND2 
4401 N N   . LEU A 566 ? 1.1074 0.6603 0.5496 -0.0029 0.3030  0.0526  566 LEU A N   
4402 C CA  . LEU A 566 ? 1.1968 0.7517 0.6133 0.0011  0.2940  0.0775  566 LEU A CA  
4403 C C   . LEU A 566 ? 1.3251 0.8856 0.7390 0.0015  0.3175  0.0925  566 LEU A C   
4404 O O   . LEU A 566 ? 1.4202 0.9875 0.8003 0.0061  0.3127  0.1108  566 LEU A O   
4405 C CB  . LEU A 566 ? 1.1951 0.7564 0.5610 0.0055  0.2705  0.0728  566 LEU A CB  
4406 C CG  . LEU A 566 ? 1.1268 0.6823 0.4931 0.0047  0.2457  0.0590  566 LEU A CG  
4407 C CD1 . LEU A 566 ? 1.1717 0.7365 0.4909 0.0074  0.2233  0.0522  566 LEU A CD1 
4408 C CD2 . LEU A 566 ? 1.0697 0.6184 0.4668 0.0043  0.2351  0.0763  566 LEU A CD2 
4409 N N   . LYS A 567 ? 1.2825 0.8424 0.7321 -0.0035 0.3428  0.0856  567 LYS A N   
4410 C CA  . LYS A 567 ? 1.3105 0.8744 0.7631 -0.0044 0.3670  0.1003  567 LYS A CA  
4411 C C   . LYS A 567 ? 1.3352 0.8931 0.8033 -0.0033 0.3655  0.1285  567 LYS A C   
4412 O O   . LYS A 567 ? 1.2669 0.8172 0.7739 -0.0061 0.3591  0.1300  567 LYS A O   
4413 C CB  . LYS A 567 ? 1.3154 0.8818 0.8126 -0.0109 0.3930  0.0854  567 LYS A CB  
4414 C CG  . LYS A 567 ? 1.4244 0.9989 0.9132 -0.0103 0.3981  0.0580  567 LYS A CG  
4415 C CD  . LYS A 567 ? 1.4793 1.0613 1.0182 -0.0157 0.4240  0.0457  567 LYS A CD  
4416 C CE  . LYS A 567 ? 1.5401 1.1318 1.0766 -0.0130 0.4290  0.0187  567 LYS A CE  
4417 N NZ  . LYS A 567 ? 1.4940 1.0981 1.0835 -0.0170 0.4535  0.0072  567 LYS A NZ  
4418 N N   . GLY A 568 ? 1.4100 0.9728 0.8489 0.0007  0.3718  0.1506  568 GLY A N   
4419 C CA  . GLY A 568 ? 1.3978 0.9554 0.8476 0.0036  0.3696  0.1796  568 GLY A CA  
4420 C C   . GLY A 568 ? 1.5349 1.0956 0.9584 0.0110  0.3399  0.1930  568 GLY A C   
4421 O O   . GLY A 568 ? 1.5428 1.1035 0.9634 0.0157  0.3372  0.2206  568 GLY A O   
4422 N N   . LEU A 569 ? 1.7406 1.3041 1.1470 0.0121  0.3177  0.1748  569 LEU A N   
4423 C CA  . LEU A 569 ? 1.7883 1.3577 1.1708 0.0186  0.2884  0.1851  569 LEU A CA  
4424 C C   . LEU A 569 ? 1.8438 1.4284 1.1695 0.0210  0.2742  0.1729  569 LEU A C   
4425 O O   . LEU A 569 ? 1.8582 1.4442 1.1727 0.0213  0.2520  0.1571  569 LEU A O   
4426 C CB  . LEU A 569 ? 1.6862 1.2460 1.1031 0.0168  0.2721  0.1741  569 LEU A CB  
4427 C CG  . LEU A 569 ? 1.6562 1.2045 1.1317 0.0135  0.2825  0.1812  569 LEU A CG  
4428 C CD1 . LEU A 569 ? 1.6069 1.1506 1.1082 0.0117  0.2637  0.1691  569 LEU A CD1 
4429 C CD2 . LEU A 569 ? 1.6883 1.2364 1.1702 0.0191  0.2859  0.2123  569 LEU A CD2 
4430 N N   . GLY A 570 ? 1.6664 1.2634 0.9570 0.0217  0.2872  0.1784  570 GLY A N   
4431 C CA  . GLY A 570 ? 1.6851 1.3007 0.9218 0.0230  0.2748  0.1640  570 GLY A CA  
4432 C C   . GLY A 570 ? 1.7547 1.3872 0.9585 0.0287  0.2450  0.1784  570 GLY A C   
4433 O O   . GLY A 570 ? 1.7009 1.3510 0.8634 0.0285  0.2299  0.1616  570 GLY A O   
4434 N N   . ASP A 571 ? 1.8381 1.4672 1.0628 0.0334  0.2363  0.2071  571 ASP A N   
4435 C CA  . ASP A 571 ? 1.8437 1.4908 1.0436 0.0397  0.2082  0.2251  571 ASP A CA  
4436 C C   . ASP A 571 ? 1.8096 1.4531 1.0249 0.0406  0.1817  0.2111  571 ASP A C   
4437 O O   . ASP A 571 ? 1.8075 1.4658 1.0123 0.0462  0.1573  0.2261  571 ASP A O   
4438 C CB  . ASP A 571 ? 1.8640 1.5085 1.0819 0.0452  0.2129  0.2647  571 ASP A CB  
4439 C CG  . ASP A 571 ? 1.8578 1.4756 1.1391 0.0440  0.2268  0.2690  571 ASP A CG  
4440 O OD1 . ASP A 571 ? 1.7860 1.3888 1.0928 0.0374  0.2437  0.2463  571 ASP A OD1 
4441 O OD2 . ASP A 571 ? 1.9753 1.5883 1.2820 0.0492  0.2205  0.2938  571 ASP A OD2 
4442 N N   . VAL A 572 ? 1.7099 1.3353 0.9504 0.0350  0.1859  0.1838  572 VAL A N   
4443 C CA  . VAL A 572 ? 1.5426 1.1621 0.7992 0.0345  0.1629  0.1710  572 VAL A CA  
4444 C C   . VAL A 572 ? 1.5159 1.1507 0.7309 0.0322  0.1422  0.1461  572 VAL A C   
4445 O O   . VAL A 572 ? 1.5083 1.1430 0.7039 0.0270  0.1522  0.1208  572 VAL A O   
4446 C CB  . VAL A 572 ? 1.4946 1.0897 0.7957 0.0283  0.1759  0.1540  572 VAL A CB  
4447 C CG1 . VAL A 572 ? 1.3834 0.9730 0.6975 0.0267  0.1526  0.1412  572 VAL A CG1 
4448 C CG2 . VAL A 572 ? 1.5851 1.1685 0.9314 0.0289  0.1954  0.1742  572 VAL A CG2 
4449 N N   . ASN A 573 ? 1.4642 1.1130 0.6693 0.0357  0.1134  0.1516  573 ASN A N   
4450 C CA  . ASN A 573 ? 1.4411 1.1057 0.6130 0.0319  0.0906  0.1253  573 ASN A CA  
4451 C C   . ASN A 573 ? 1.4264 1.0685 0.6216 0.0244  0.0867  0.0962  573 ASN A C   
4452 O O   . ASN A 573 ? 1.4442 1.0768 0.6672 0.0249  0.0736  0.1016  573 ASN A O   
4453 C CB  . ASN A 573 ? 1.4823 1.1732 0.6397 0.0378  0.0604  0.1420  573 ASN A CB  
4454 C CG  . ASN A 573 ? 1.5168 1.2270 0.6453 0.0320  0.0350  0.1118  573 ASN A CG  
4455 O OD1 . ASN A 573 ? 1.5187 1.2264 0.6304 0.0241  0.0419  0.0797  573 ASN A OD1 
4456 N ND2 . ASN A 573 ? 1.5471 1.2780 0.6745 0.0356  0.0055  0.1207  573 ASN A ND2 
4457 N N   . VAL A 574 ? 1.4717 1.1063 0.6576 0.0175  0.0987  0.0660  574 VAL A N   
4458 C CA  . VAL A 574 ? 1.4411 1.0537 0.6520 0.0104  0.0983  0.0403  574 VAL A CA  
4459 C C   . VAL A 574 ? 1.3867 1.0067 0.5861 0.0048  0.0704  0.0165  574 VAL A C   
4460 O O   . VAL A 574 ? 1.2764 0.8890 0.5197 -0.0004 0.0624  0.0021  574 VAL A O   
4461 C CB  . VAL A 574 ? 1.3533 0.9543 0.5693 0.0065  0.1244  0.0185  574 VAL A CB  
4462 C CG1 . VAL A 574 ? 1.3645 0.9565 0.6024 0.0099  0.1520  0.0396  574 VAL A CG1 
4463 C CG2 . VAL A 574 ? 1.3938 1.0140 0.5717 0.0048  0.1255  -0.0009 574 VAL A CG2 
4464 N N   . GLU A 575 ? 1.4577 1.1051 0.6224 0.0049  0.0535  0.0114  575 GLU A N   
4465 C CA  . GLU A 575 ? 1.4994 1.1571 0.6579 -0.0025 0.0268  -0.0146 575 GLU A CA  
4466 C C   . GLU A 575 ? 1.3589 1.0208 0.5473 -0.0013 0.0029  0.0007  575 GLU A C   
4467 O O   . GLU A 575 ? 1.3031 0.9601 0.5336 -0.0084 -0.0070 -0.0164 575 GLU A O   
4468 C CB  . GLU A 575 ? 1.5881 1.2821 0.7057 -0.0032 0.0145  -0.0245 575 GLU A CB  
4469 C CG  . GLU A 575 ? 1.6824 1.3813 0.7773 -0.0039 0.0387  -0.0391 575 GLU A CG  
4470 C CD  . GLU A 575 ? 1.8251 1.5638 0.8780 -0.0057 0.0255  -0.0533 575 GLU A CD  
4471 O OE1 . GLU A 575 ? 1.8584 1.6185 0.9058 -0.0095 -0.0035 -0.0633 575 GLU A OE1 
4472 O OE2 . GLU A 575 ? 1.8796 1.6310 0.9057 -0.0037 0.0440  -0.0553 575 GLU A OE2 
4473 N N   . GLU A 576 ? 1.4306 1.1056 0.6071 0.0086  -0.0054 0.0344  576 GLU A N   
4474 C CA  . GLU A 576 ? 1.4181 1.1028 0.6336 0.0114  -0.0264 0.0503  576 GLU A CA  
4475 C C   . GLU A 576 ? 1.3574 1.0197 0.6309 0.0114  -0.0124 0.0585  576 GLU A C   
4476 O O   . GLU A 576 ? 1.3095 0.9766 0.6237 0.0095  -0.0271 0.0590  576 GLU A O   
4477 C CB  . GLU A 576 ? 1.4660 1.1699 0.6554 0.0243  -0.0371 0.0862  576 GLU A CB  
4478 C CG  . GLU A 576 ? 1.5352 1.2563 0.7610 0.0285  -0.0623 0.1005  576 GLU A CG  
4479 C CD  . GLU A 576 ? 1.6461 1.3906 0.8493 0.0430  -0.0740 0.1367  576 GLU A CD  
4480 O OE1 . GLU A 576 ? 1.6351 1.3917 0.8133 0.0476  -0.0601 0.1505  576 GLU A OE1 
4481 O OE2 . GLU A 576 ? 1.6462 1.4068 0.8750 0.0488  -0.0957 0.1505  576 GLU A OE2 
4482 N N   . LEU A 577 ? 1.3093 0.9500 0.5878 0.0127  0.0160  0.0636  577 LEU A N   
4483 C CA  . LEU A 577 ? 1.1818 0.8052 0.5131 0.0118  0.0289  0.0693  577 LEU A CA  
4484 C C   . LEU A 577 ? 1.1551 0.7719 0.5200 0.0022  0.0258  0.0410  577 LEU A C   
4485 O O   . LEU A 577 ? 1.0522 0.6640 0.4614 0.0006  0.0249  0.0439  577 LEU A O   
4486 C CB  . LEU A 577 ? 1.1674 0.7737 0.4959 0.0150  0.0594  0.0820  577 LEU A CB  
4487 C CG  . LEU A 577 ? 1.0971 0.6889 0.4770 0.0144  0.0740  0.0902  577 LEU A CG  
4488 C CD1 . LEU A 577 ? 1.0729 0.6691 0.4788 0.0198  0.0620  0.1118  577 LEU A CD1 
4489 C CD2 . LEU A 577 ? 1.0903 0.6684 0.4658 0.0161  0.1041  0.1013  577 LEU A CD2 
4490 N N   . PHE A 578 ? 1.1331 0.7493 0.4779 -0.0040 0.0251  0.0141  578 PHE A N   
4491 C CA  . PHE A 578 ? 1.1061 0.7141 0.4829 -0.0122 0.0225  -0.0107 578 PHE A CA  
4492 C C   . PHE A 578 ? 1.1265 0.7461 0.4947 -0.0195 0.0000  -0.0322 578 PHE A C   
4493 O O   . PHE A 578 ? 1.1051 0.7154 0.4940 -0.0268 -0.0002 -0.0551 578 PHE A O   
4494 C CB  . PHE A 578 ? 1.1064 0.6984 0.4822 -0.0134 0.0457  -0.0265 578 PHE A CB  
4495 C CG  . PHE A 578 ? 1.0776 0.6592 0.4825 -0.0097 0.0657  -0.0123 578 PHE A CG  
4496 C CD1 . PHE A 578 ? 0.9956 0.5719 0.4472 -0.0121 0.0651  -0.0146 578 PHE A CD1 
4497 C CD2 . PHE A 578 ? 1.0259 0.6048 0.4118 -0.0046 0.0853  0.0030  578 PHE A CD2 
4498 C CE1 . PHE A 578 ? 0.9713 0.5426 0.4498 -0.0099 0.0816  -0.0045 578 PHE A CE1 
4499 C CE2 . PHE A 578 ? 1.0174 0.5886 0.4344 -0.0032 0.1036  0.0131  578 PHE A CE2 
4500 C CZ  . PHE A 578 ? 1.0210 0.5899 0.4843 -0.0061 0.1006  0.0079  578 PHE A CZ  
4501 N N   . GLY A 579 ? 1.2185 0.8592 0.5594 -0.0178 -0.0190 -0.0252 579 GLY A N   
4502 C CA  . GLY A 579 ? 1.1629 0.8191 0.4986 -0.0265 -0.0419 -0.0478 579 GLY A CA  
4503 C C   . GLY A 579 ? 1.1490 0.8051 0.5367 -0.0327 -0.0543 -0.0510 579 GLY A C   
4504 O O   . GLY A 579 ? 1.1039 0.7655 0.5182 -0.0278 -0.0590 -0.0284 579 GLY A O   
4505 N N   . ILE A 580 ? 1.0751 0.7241 0.4788 -0.0436 -0.0577 -0.0791 580 ILE A N   
4506 C CA  . ILE A 580 ? 1.0319 0.6802 0.4836 -0.0511 -0.0676 -0.0836 580 ILE A CA  
4507 C C   . ILE A 580 ? 0.9946 0.6636 0.4413 -0.0614 -0.0910 -0.1045 580 ILE A C   
4508 O O   . ILE A 580 ? 1.1045 0.7668 0.5428 -0.0709 -0.0906 -0.1344 580 ILE A O   
4509 C CB  . ILE A 580 ? 0.9862 0.6075 0.4684 -0.0553 -0.0507 -0.0957 580 ILE A CB  
4510 C CG1 . ILE A 580 ? 0.9925 0.5998 0.4807 -0.0455 -0.0299 -0.0762 580 ILE A CG1 
4511 C CG2 . ILE A 580 ? 0.9796 0.6007 0.5081 -0.0635 -0.0600 -0.0983 580 ILE A CG2 
4512 C CD1 . ILE A 580 ? 0.9538 0.5390 0.4698 -0.0469 -0.0140 -0.0851 580 ILE A CD1 
4513 N N   . SER A 581 ? 0.9808 0.6762 0.4356 -0.0597 -0.1112 -0.0901 581 SER A N   
4514 C CA  . SER A 581 ? 0.9530 0.6755 0.4075 -0.0696 -0.1363 -0.1086 581 SER A CA  
4515 C C   . SER A 581 ? 1.0144 0.7323 0.5228 -0.0820 -0.1409 -0.1209 581 SER A C   
4516 O O   . SER A 581 ? 1.0409 0.7546 0.5866 -0.0788 -0.1364 -0.1014 581 SER A O   
4517 C CB  . SER A 581 ? 0.9904 0.7474 0.4323 -0.0605 -0.1568 -0.0855 581 SER A CB  
4518 O OG  . SER A 581 ? 1.0673 0.8557 0.5198 -0.0705 -0.1833 -0.1025 581 SER A OG  
4519 N N   . LYS A 582 ? 1.0884 0.8068 0.6011 -0.0968 -0.1481 -0.1540 582 LYS A N   
4520 C CA  . LYS A 582 ? 1.0098 0.7242 0.5749 -0.1103 -0.1520 -0.1658 582 LYS A CA  
4521 C C   . LYS A 582 ? 0.9924 0.7410 0.5851 -0.1112 -0.1732 -0.1521 582 LYS A C   
4522 O O   . LYS A 582 ? 0.9374 0.6824 0.5770 -0.1153 -0.1701 -0.1434 582 LYS A O   
4523 C CB  . LYS A 582 ? 1.0461 0.7545 0.6111 -0.1270 -0.1553 -0.2063 582 LYS A CB  
4524 C CG  . LYS A 582 ? 1.0250 0.7275 0.6467 -0.1429 -0.1577 -0.2197 582 LYS A CG  
4525 C CD  . LYS A 582 ? 1.0563 0.7545 0.6797 -0.1608 -0.1619 -0.2627 582 LYS A CD  
4526 C CE  . LYS A 582 ? 1.0693 0.7574 0.7536 -0.1775 -0.1608 -0.2743 582 LYS A CE  
4527 N NZ  . LYS A 582 ? 1.0569 0.7353 0.7490 -0.1963 -0.1617 -0.3187 582 LYS A NZ  
4528 N N   . GLU A 583 ? 1.0903 0.8743 0.6547 -0.1066 -0.1945 -0.1488 583 GLU A N   
4529 C CA  . GLU A 583 ? 1.0419 0.8628 0.6354 -0.1060 -0.2163 -0.1361 583 GLU A CA  
4530 C C   . GLU A 583 ? 1.0401 0.8562 0.6568 -0.0917 -0.2063 -0.0999 583 GLU A C   
4531 O O   . GLU A 583 ? 1.0199 0.8510 0.6825 -0.0942 -0.2125 -0.0917 583 GLU A O   
4532 C CB  . GLU A 583 ? 1.1289 0.9908 0.6836 -0.1016 -0.2421 -0.1379 583 GLU A CB  
4533 C CG  . GLU A 583 ? 1.2626 1.1687 0.8501 -0.1001 -0.2677 -0.1262 583 GLU A CG  
4534 C CD  . GLU A 583 ? 1.3965 1.3484 0.9476 -0.0989 -0.2973 -0.1340 583 GLU A CD  
4535 O OE1 . GLU A 583 ? 1.4283 1.3777 0.9302 -0.1037 -0.2981 -0.1559 583 GLU A OE1 
4536 O OE2 . GLU A 583 ? 1.4405 1.4332 1.0125 -0.0926 -0.3198 -0.1183 583 GLU A OE2 
4537 N N   . PHE A 584 ? 0.9927 0.7886 0.5808 -0.0775 -0.1893 -0.0796 584 PHE A N   
4538 C CA  . PHE A 584 ? 0.9447 0.7339 0.5555 -0.0652 -0.1778 -0.0490 584 PHE A CA  
4539 C C   . PHE A 584 ? 0.8744 0.6398 0.5269 -0.0724 -0.1606 -0.0514 584 PHE A C   
4540 O O   . PHE A 584 ? 0.8337 0.6071 0.5235 -0.0702 -0.1594 -0.0368 584 PHE A O   
4541 C CB  . PHE A 584 ? 0.8779 0.6506 0.4505 -0.0504 -0.1624 -0.0294 584 PHE A CB  
4542 C CG  . PHE A 584 ? 0.8192 0.5796 0.4165 -0.0400 -0.1468 -0.0033 584 PHE A CG  
4543 C CD1 . PHE A 584 ? 0.8223 0.6028 0.4331 -0.0283 -0.1552 0.0208  584 PHE A CD1 
4544 C CD2 . PHE A 584 ? 0.8561 0.5865 0.4650 -0.0417 -0.1239 -0.0040 584 PHE A CD2 
4545 C CE1 . PHE A 584 ? 0.8231 0.5912 0.4588 -0.0197 -0.1391 0.0408  584 PHE A CE1 
4546 C CE2 . PHE A 584 ? 0.8273 0.5492 0.4585 -0.0338 -0.1101 0.0158  584 PHE A CE2 
4547 C CZ  . PHE A 584 ? 0.7899 0.5293 0.4346 -0.0235 -0.1168 0.0367  584 PHE A CZ  
4548 N N   . TRP A 585 ? 0.8691 0.6063 0.5158 -0.0803 -0.1465 -0.0687 585 TRP A N   
4549 C CA  . TRP A 585 ? 0.8652 0.5796 0.5462 -0.0851 -0.1295 -0.0668 585 TRP A CA  
4550 C C   . TRP A 585 ? 0.8727 0.5959 0.5965 -0.0998 -0.1373 -0.0791 585 TRP A C   
4551 O O   . TRP A 585 ? 0.8399 0.5523 0.5960 -0.1026 -0.1253 -0.0709 585 TRP A O   
4552 C CB  . TRP A 585 ? 0.7992 0.4811 0.4620 -0.0857 -0.1113 -0.0773 585 TRP A CB  
4553 C CG  . TRP A 585 ? 0.8270 0.4981 0.4629 -0.0719 -0.0975 -0.0606 585 TRP A CG  
4554 C CD1 . TRP A 585 ? 0.8812 0.5514 0.4741 -0.0652 -0.0959 -0.0620 585 TRP A CD1 
4555 C CD2 . TRP A 585 ? 0.8545 0.5161 0.5056 -0.0643 -0.0825 -0.0406 585 TRP A CD2 
4556 N NE1 . TRP A 585 ? 0.8081 0.4670 0.3924 -0.0542 -0.0798 -0.0434 585 TRP A NE1 
4557 C CE2 . TRP A 585 ? 0.8114 0.4655 0.4315 -0.0539 -0.0722 -0.0315 585 TRP A CE2 
4558 C CE3 . TRP A 585 ? 0.7209 0.3810 0.4080 -0.0660 -0.0762 -0.0306 585 TRP A CE3 
4559 C CZ2 . TRP A 585 ? 0.8306 0.4758 0.4585 -0.0463 -0.0568 -0.0150 585 TRP A CZ2 
4560 C CZ3 . TRP A 585 ? 0.8462 0.4991 0.5363 -0.0578 -0.0617 -0.0149 585 TRP A CZ3 
4561 C CH2 . TRP A 585 ? 0.7898 0.4354 0.4524 -0.0486 -0.0527 -0.0083 585 TRP A CH2 
4562 N N   . GLU A 586 ? 0.8147 0.5591 0.5399 -0.1099 -0.1566 -0.0987 586 GLU A N   
4563 C CA  . GLU A 586 ? 0.8298 0.5877 0.6018 -0.1245 -0.1645 -0.1087 586 GLU A CA  
4564 C C   . GLU A 586 ? 0.8249 0.6093 0.6280 -0.1185 -0.1704 -0.0869 586 GLU A C   
4565 O O   . GLU A 586 ? 0.7971 0.5813 0.6426 -0.1260 -0.1634 -0.0833 586 GLU A O   
4566 C CB  . GLU A 586 ? 0.8846 0.6630 0.6524 -0.1379 -0.1850 -0.1380 586 GLU A CB  
4567 C CG  . GLU A 586 ? 0.8773 0.6264 0.6331 -0.1492 -0.1757 -0.1663 586 GLU A CG  
4568 C CD  . GLU A 586 ? 1.0023 0.7734 0.7580 -0.1651 -0.1958 -0.2001 586 GLU A CD  
4569 O OE1 . GLU A 586 ? 0.9435 0.7555 0.6888 -0.1631 -0.2195 -0.1998 586 GLU A OE1 
4570 O OE2 . GLU A 586 ? 1.0589 0.8072 0.8264 -0.1795 -0.1880 -0.2273 586 GLU A OE2 
4571 N N   . LYS A 587 ? 0.8418 0.6486 0.6251 -0.1045 -0.1817 -0.0713 587 LYS A N   
4572 C CA  . LYS A 587 ? 0.7242 0.5528 0.5382 -0.0957 -0.1840 -0.0492 587 LYS A CA  
4573 C C   . LYS A 587 ? 0.7162 0.5196 0.5391 -0.0883 -0.1595 -0.0311 587 LYS A C   
4574 O O   . LYS A 587 ? 0.7584 0.5707 0.6194 -0.0889 -0.1535 -0.0216 587 LYS A O   
4575 C CB  . LYS A 587 ? 0.8291 0.6842 0.6200 -0.0804 -0.2007 -0.0344 587 LYS A CB  
4576 C CG  . LYS A 587 ? 0.9751 0.8575 0.7424 -0.0855 -0.2263 -0.0516 587 LYS A CG  
4577 C CD  . LYS A 587 ? 1.0729 0.9808 0.8128 -0.0673 -0.2414 -0.0303 587 LYS A CD  
4578 C CE  . LYS A 587 ? 1.1780 1.1131 0.8807 -0.0713 -0.2661 -0.0471 587 LYS A CE  
4579 N NZ  . LYS A 587 ? 1.1607 1.1319 0.8985 -0.0871 -0.2892 -0.0701 587 LYS A NZ  
4580 N N   . GLU A 588 ? 0.7604 0.5348 0.5488 -0.0819 -0.1447 -0.0277 588 GLU A N   
4581 C CA  . GLU A 588 ? 0.7422 0.4974 0.5359 -0.0745 -0.1235 -0.0119 588 GLU A CA  
4582 C C   . GLU A 588 ? 0.7381 0.4819 0.5633 -0.0853 -0.1109 -0.0158 588 GLU A C   
4583 O O   . GLU A 588 ? 0.6951 0.4431 0.5443 -0.0828 -0.1008 -0.0036 588 GLU A O   
4584 C CB  . GLU A 588 ? 0.7549 0.4849 0.5082 -0.0671 -0.1115 -0.0100 588 GLU A CB  
4585 C CG  . GLU A 588 ? 0.6706 0.3872 0.4263 -0.0579 -0.0928 0.0063  588 GLU A CG  
4586 C CD  . GLU A 588 ? 0.7777 0.5096 0.5395 -0.0458 -0.0951 0.0244  588 GLU A CD  
4587 O OE1 . GLU A 588 ? 0.7193 0.4694 0.4710 -0.0407 -0.1112 0.0282  588 GLU A OE1 
4588 O OE2 . GLU A 588 ? 0.6839 0.4105 0.4616 -0.0410 -0.0809 0.0347  588 GLU A OE2 
4589 N N   . VAL A 589 ? 0.7525 0.4815 0.5779 -0.0972 -0.1100 -0.0324 589 VAL A N   
4590 C CA  . VAL A 589 ? 0.7716 0.4890 0.6273 -0.1072 -0.0977 -0.0329 589 VAL A CA  
4591 C C   . VAL A 589 ? 0.7310 0.4741 0.6289 -0.1155 -0.1043 -0.0317 589 VAL A C   
4592 O O   . VAL A 589 ? 0.7690 0.5102 0.6933 -0.1197 -0.0913 -0.0232 589 VAL A O   
4593 C CB  . VAL A 589 ? 0.7880 0.4811 0.6388 -0.1173 -0.0944 -0.0504 589 VAL A CB  
4594 C CG1 . VAL A 589 ? 0.7217 0.3904 0.5365 -0.1080 -0.0844 -0.0502 589 VAL A CG1 
4595 C CG2 . VAL A 589 ? 0.8047 0.5115 0.6576 -0.1279 -0.1127 -0.0725 589 VAL A CG2 
4596 N N   . GLU A 590 ? 0.7774 0.5478 0.6827 -0.1179 -0.1243 -0.0399 590 GLU A N   
4597 C CA  . GLU A 590 ? 0.7687 0.5688 0.7188 -0.1247 -0.1314 -0.0388 590 GLU A CA  
4598 C C   . GLU A 590 ? 0.7912 0.6028 0.7565 -0.1133 -0.1215 -0.0182 590 GLU A C   
4599 O O   . GLU A 590 ? 0.7721 0.5910 0.7727 -0.1193 -0.1109 -0.0133 590 GLU A O   
4600 C CB  . GLU A 590 ? 0.8265 0.6586 0.7790 -0.1271 -0.1577 -0.0508 590 GLU A CB  
4601 C CG  . GLU A 590 ? 0.9082 0.7770 0.9120 -0.1343 -0.1677 -0.0516 590 GLU A CG  
4602 C CD  . GLU A 590 ? 1.1125 0.9802 1.1513 -0.1564 -0.1667 -0.0706 590 GLU A CD  
4603 O OE1 . GLU A 590 ? 1.1656 1.0056 1.1865 -0.1656 -0.1626 -0.0859 590 GLU A OE1 
4604 O OE2 . GLU A 590 ? 1.1328 1.0265 1.2200 -0.1645 -0.1685 -0.0703 590 GLU A OE2 
4605 N N   . GLU A 591 ? 0.7494 0.5617 0.6890 -0.0970 -0.1229 -0.0065 591 GLU A N   
4606 C CA  . GLU A 591 ? 0.7195 0.5401 0.6752 -0.0860 -0.1119 0.0102  591 GLU A CA  
4607 C C   . GLU A 591 ? 0.6802 0.4780 0.6337 -0.0875 -0.0882 0.0155  591 GLU A C   
4608 O O   . GLU A 591 ? 0.6730 0.4807 0.6532 -0.0872 -0.0764 0.0224  591 GLU A O   
4609 C CB  . GLU A 591 ? 0.6908 0.5136 0.6216 -0.0688 -0.1175 0.0218  591 GLU A CB  
4610 C CG  . GLU A 591 ? 0.6956 0.5498 0.6341 -0.0636 -0.1413 0.0234  591 GLU A CG  
4611 C CD  . GLU A 591 ? 0.7971 0.6837 0.7880 -0.0640 -0.1457 0.0274  591 GLU A CD  
4612 O OE1 . GLU A 591 ? 0.7776 0.6622 0.7912 -0.0587 -0.1284 0.0369  591 GLU A OE1 
4613 O OE2 . GLU A 591 ? 0.7360 0.6519 0.7468 -0.0701 -0.1660 0.0193  591 GLU A OE2 
4614 N N   . ILE A 592 ? 0.6442 0.4141 0.5662 -0.0885 -0.0810 0.0121  592 ILE A N   
4615 C CA  . ILE A 592 ? 0.7076 0.4601 0.6260 -0.0892 -0.0611 0.0179  592 ILE A CA  
4616 C C   . ILE A 592 ? 0.7025 0.4579 0.6503 -0.1022 -0.0537 0.0169  592 ILE A C   
4617 O O   . ILE A 592 ? 0.6524 0.4105 0.6112 -0.1025 -0.0385 0.0252  592 ILE A O   
4618 C CB  . ILE A 592 ? 0.7363 0.4617 0.6189 -0.0864 -0.0568 0.0148  592 ILE A CB  
4619 C CG1 . ILE A 592 ? 0.7631 0.4857 0.6182 -0.0736 -0.0595 0.0186  592 ILE A CG1 
4620 C CG2 . ILE A 592 ? 0.6373 0.3491 0.5183 -0.0875 -0.0393 0.0210  592 ILE A CG2 
4621 C CD1 . ILE A 592 ? 0.6899 0.3904 0.5113 -0.0715 -0.0579 0.0127  592 ILE A CD1 
4622 N N   . ASP A 593 ? 0.7259 0.4816 0.6873 -0.1139 -0.0632 0.0062  593 ASP A N   
4623 C CA  . ASP A 593 ? 0.6679 0.4249 0.6615 -0.1276 -0.0546 0.0063  593 ASP A CA  
4624 C C   . ASP A 593 ? 0.6981 0.4845 0.7278 -0.1292 -0.0513 0.0124  593 ASP A C   
4625 O O   . ASP A 593 ? 0.7213 0.5090 0.7651 -0.1327 -0.0342 0.0216  593 ASP A O   
4626 C CB  . ASP A 593 ? 0.6980 0.4494 0.7033 -0.1410 -0.0658 -0.0098 593 ASP A CB  
4627 C CG  . ASP A 593 ? 0.7837 0.5299 0.8239 -0.1564 -0.0541 -0.0088 593 ASP A CG  
4628 O OD1 . ASP A 593 ? 0.8163 0.5577 0.8616 -0.1556 -0.0361 0.0067  593 ASP A OD1 
4629 O OD2 . ASP A 593 ? 0.7793 0.5268 0.8418 -0.1701 -0.0626 -0.0237 593 ASP A OD2 
4630 N N   . LYS A 594 ? 0.7052 0.5174 0.7500 -0.1258 -0.0672 0.0079  594 LYS A N   
4631 C CA  . LYS A 594 ? 0.6884 0.5309 0.7726 -0.1255 -0.0639 0.0131  594 LYS A CA  
4632 C C   . LYS A 594 ? 0.6650 0.5067 0.7422 -0.1143 -0.0463 0.0249  594 LYS A C   
4633 O O   . LYS A 594 ? 0.6084 0.4659 0.7146 -0.1173 -0.0326 0.0293  594 LYS A O   
4634 C CB  . LYS A 594 ? 0.6368 0.5086 0.7371 -0.1203 -0.0864 0.0084  594 LYS A CB  
4635 C CG  . LYS A 594 ? 0.6924 0.5747 0.8069 -0.1339 -0.1053 -0.0075 594 LYS A CG  
4636 C CD  . LYS A 594 ? 0.7006 0.6206 0.8336 -0.1279 -0.1293 -0.0103 594 LYS A CD  
4637 C CE  . LYS A 594 ? 0.7491 0.6652 0.8426 -0.1085 -0.1387 -0.0013 594 LYS A CE  
4638 N NZ  . LYS A 594 ? 0.6827 0.6372 0.7924 -0.1001 -0.1631 0.0005  594 LYS A NZ  
4639 N N   . TYR A 595 ? 0.6419 0.4660 0.6821 -0.1024 -0.0450 0.0285  595 TYR A N   
4640 C CA  . TYR A 595 ? 0.6464 0.4697 0.6808 -0.0930 -0.0285 0.0358  595 TYR A CA  
4641 C C   . TYR A 595 ? 0.6705 0.4836 0.6983 -0.1002 -0.0090 0.0392  595 TYR A C   
4642 O O   . TYR A 595 ? 0.6558 0.4831 0.7016 -0.1013 0.0060  0.0423  595 TYR A O   
4643 C CB  . TYR A 595 ? 0.6154 0.4226 0.6154 -0.0802 -0.0320 0.0377  595 TYR A CB  
4644 C CG  . TYR A 595 ? 0.5934 0.3968 0.5871 -0.0725 -0.0146 0.0415  595 TYR A CG  
4645 C CD1 . TYR A 595 ? 0.5826 0.4021 0.6014 -0.0642 -0.0091 0.0438  595 TYR A CD1 
4646 C CD2 . TYR A 595 ? 0.5923 0.3772 0.5575 -0.0734 -0.0037 0.0412  595 TYR A CD2 
4647 C CE1 . TYR A 595 ? 0.5721 0.3871 0.5873 -0.0587 0.0081  0.0432  595 TYR A CE1 
4648 C CE2 . TYR A 595 ? 0.5604 0.3449 0.5208 -0.0682 0.0112  0.0410  595 TYR A CE2 
4649 C CZ  . TYR A 595 ? 0.5583 0.3567 0.5432 -0.0617 0.0177  0.0407  595 TYR A CZ  
4650 O OH  . TYR A 595 ? 0.7194 0.5165 0.7015 -0.0580 0.0337  0.0365  595 TYR A OH  
4651 N N   . LEU A 596 ? 0.6874 0.4773 0.6893 -0.1044 -0.0087 0.0393  596 LEU A N   
4652 C CA  . LEU A 596 ? 0.7057 0.4872 0.6984 -0.1092 0.0079  0.0463  596 LEU A CA  
4653 C C   . LEU A 596 ? 0.7531 0.5478 0.7776 -0.1213 0.0174  0.0505  596 LEU A C   
4654 O O   . LEU A 596 ? 0.6969 0.4999 0.7224 -0.1230 0.0344  0.0578  596 LEU A O   
4655 C CB  . LEU A 596 ? 0.7590 0.5137 0.7245 -0.1099 0.0049  0.0470  596 LEU A CB  
4656 C CG  . LEU A 596 ? 0.6351 0.3764 0.5676 -0.0987 0.0011  0.0445  596 LEU A CG  
4657 C CD1 . LEU A 596 ? 0.6750 0.3917 0.5883 -0.0997 -0.0022 0.0435  596 LEU A CD1 
4658 C CD2 . LEU A 596 ? 0.6246 0.3727 0.5452 -0.0927 0.0142  0.0489  596 LEU A CD2 
4659 N N   . GLU A 597 ? 0.8204 0.6191 0.8712 -0.1306 0.0073  0.0452  597 GLU A N   
4660 C CA  . GLU A 597 ? 0.8220 0.6331 0.9084 -0.1439 0.0176  0.0489  597 GLU A CA  
4661 C C   . GLU A 597 ? 0.8077 0.6488 0.9205 -0.1418 0.0277  0.0505  597 GLU A C   
4662 O O   . GLU A 597 ? 0.7734 0.6242 0.9019 -0.1493 0.0460  0.0579  597 GLU A O   
4663 C CB  . GLU A 597 ? 0.8373 0.6492 0.9508 -0.1554 0.0030  0.0386  597 GLU A CB  
4664 C CG  . GLU A 597 ? 0.9221 0.7486 1.0803 -0.1709 0.0136  0.0409  597 GLU A CG  
4665 C CD  . GLU A 597 ? 1.0749 0.9027 1.2626 -0.1845 -0.0013 0.0269  597 GLU A CD  
4666 O OE1 . GLU A 597 ? 1.1225 0.9425 1.2926 -0.1809 -0.0209 0.0146  597 GLU A OE1 
4667 O OE2 . GLU A 597 ? 1.1268 0.9647 1.3555 -0.1995 0.0073  0.0271  597 GLU A OE2 
4668 N N   . ASP A 598 ? 0.7192 0.5752 0.8380 -0.1311 0.0176  0.0445  598 ASP A N   
4669 C CA  . ASP A 598 ? 0.6874 0.5714 0.8368 -0.1274 0.0278  0.0446  598 ASP A CA  
4670 C C   . ASP A 598 ? 0.6698 0.5513 0.7963 -0.1196 0.0465  0.0478  598 ASP A C   
4671 O O   . ASP A 598 ? 0.7181 0.6148 0.8587 -0.1238 0.0661  0.0501  598 ASP A O   
4672 C CB  . ASP A 598 ? 0.7174 0.6187 0.8874 -0.1175 0.0096  0.0391  598 ASP A CB  
4673 C CG  . ASP A 598 ? 0.7688 0.6950 0.9694 -0.1091 0.0212  0.0395  598 ASP A CG  
4674 O OD1 . ASP A 598 ? 0.7637 0.7090 0.9963 -0.1170 0.0369  0.0399  598 ASP A OD1 
4675 O OD2 . ASP A 598 ? 0.7810 0.7069 0.9758 -0.0943 0.0165  0.0396  598 ASP A OD2 
4676 N N   . GLN A 599 ? 0.6528 0.5168 0.7441 -0.1092 0.0416  0.0464  599 GLN A N   
4677 C CA  . GLN A 599 ? 0.6279 0.4932 0.7028 -0.1019 0.0573  0.0448  599 GLN A CA  
4678 C C   . GLN A 599 ? 0.6985 0.5564 0.7446 -0.1082 0.0716  0.0500  599 GLN A C   
4679 O O   . GLN A 599 ? 0.7539 0.6248 0.7968 -0.1081 0.0894  0.0480  599 GLN A O   
4680 C CB  . GLN A 599 ? 0.6772 0.5281 0.7308 -0.0894 0.0477  0.0412  599 GLN A CB  
4681 C CG  . GLN A 599 ? 0.5986 0.4602 0.6799 -0.0798 0.0371  0.0396  599 GLN A CG  
4682 C CD  . GLN A 599 ? 0.6077 0.4910 0.7237 -0.0756 0.0526  0.0361  599 GLN A CD  
4683 O OE1 . GLN A 599 ? 0.5875 0.4707 0.6949 -0.0747 0.0712  0.0308  599 GLN A OE1 
4684 N NE2 . GLN A 599 ? 0.5928 0.4971 0.7501 -0.0731 0.0453  0.0374  599 GLN A NE2 
4685 N N   . VAL A 600 ? 0.7051 0.5440 0.7304 -0.1129 0.0645  0.0566  600 VAL A N   
4686 C CA  . VAL A 600 ? 0.6667 0.4998 0.6648 -0.1165 0.0763  0.0653  600 VAL A CA  
4687 C C   . VAL A 600 ? 0.6758 0.5151 0.6912 -0.1285 0.0872  0.0765  600 VAL A C   
4688 O O   . VAL A 600 ? 0.6852 0.5350 0.6893 -0.1316 0.1040  0.0845  600 VAL A O   
4689 C CB  . VAL A 600 ? 0.7008 0.5088 0.6673 -0.1123 0.0649  0.0680  600 VAL A CB  
4690 C CG1 . VAL A 600 ? 0.6634 0.4717 0.6002 -0.1115 0.0753  0.0765  600 VAL A CG1 
4691 C CG2 . VAL A 600 ? 0.6665 0.4672 0.6231 -0.1021 0.0535  0.0575  600 VAL A CG2 
4692 N N   . ASN A 601 ? 0.6622 0.4958 0.7046 -0.1360 0.0784  0.0770  601 ASN A N   
4693 C CA  . ASN A 601 ? 0.7145 0.5558 0.7861 -0.1492 0.0898  0.0855  601 ASN A CA  
4694 C C   . ASN A 601 ? 0.6634 0.4914 0.7115 -0.1532 0.1026  0.1032  601 ASN A C   
4695 O O   . ASN A 601 ? 0.6597 0.4626 0.6881 -0.1508 0.0937  0.1078  601 ASN A O   
4696 C CB  . ASN A 601 ? 0.6801 0.5525 0.7816 -0.1509 0.1029  0.0809  601 ASN A CB  
4697 C CG  . ASN A 601 ? 0.7092 0.5934 0.8502 -0.1654 0.1143  0.0873  601 ASN A CG  
4698 O OD1 . ASN A 601 ? 0.7632 0.6337 0.9210 -0.1746 0.1061  0.0893  601 ASN A OD1 
4699 N ND2 . ASN A 601 ? 0.6693 0.5789 0.8269 -0.1684 0.1348  0.0891  601 ASN A ND2 
4700 N N   . ALA A 602 ? 0.6409 0.4854 0.6896 -0.1582 0.1236  0.1145  602 ALA A N   
4701 C CA  . ALA A 602 ? 0.6518 0.4860 0.6817 -0.1622 0.1363  0.1363  602 ALA A CA  
4702 C C   . ALA A 602 ? 0.7123 0.5413 0.6942 -0.1511 0.1341  0.1427  602 ALA A C   
4703 O O   . ALA A 602 ? 0.7216 0.5407 0.6855 -0.1514 0.1407  0.1632  602 ALA A O   
4704 C CB  . ALA A 602 ? 0.6238 0.4810 0.6674 -0.1712 0.1608  0.1475  602 ALA A CB  
4705 N N   . ASP A 603 ? 0.6439 0.4802 0.6074 -0.1414 0.1255  0.1267  603 ASP A N   
4706 C CA  . ASP A 603 ? 0.7028 0.5382 0.6252 -0.1321 0.1223  0.1293  603 ASP A CA  
4707 C C   . ASP A 603 ? 0.6426 0.4527 0.5550 -0.1246 0.1032  0.1243  603 ASP A C   
4708 O O   . ASP A 603 ? 0.6584 0.4693 0.5424 -0.1164 0.0983  0.1222  603 ASP A O   
4709 C CB  . ASP A 603 ? 0.6654 0.5259 0.5749 -0.1277 0.1285  0.1133  603 ASP A CB  
4710 C CG  . ASP A 603 ? 0.7857 0.6735 0.6917 -0.1337 0.1503  0.1190  603 ASP A CG  
4711 O OD1 . ASP A 603 ? 0.8170 0.7092 0.7002 -0.1357 0.1586  0.1388  603 ASP A OD1 
4712 O OD2 . ASP A 603 ? 0.7748 0.6805 0.7013 -0.1359 0.1599  0.1048  603 ASP A OD2 
4713 N N   . LEU A 604 ? 0.6316 0.4216 0.5674 -0.1281 0.0930  0.1208  604 LEU A N   
4714 C CA  . LEU A 604 ? 0.6830 0.4490 0.6087 -0.1217 0.0769  0.1148  604 LEU A CA  
4715 C C   . LEU A 604 ? 0.6296 0.3772 0.5414 -0.1196 0.0786  0.1326  604 LEU A C   
4716 O O   . LEU A 604 ? 0.7284 0.4650 0.6577 -0.1271 0.0858  0.1461  604 LEU A O   
4717 C CB  . LEU A 604 ? 0.6883 0.4423 0.6414 -0.1270 0.0656  0.1031  604 LEU A CB  
4718 C CG  . LEU A 604 ? 0.7150 0.4462 0.6566 -0.1211 0.0499  0.0935  604 LEU A CG  
4719 C CD1 . LEU A 604 ? 0.6169 0.3550 0.5369 -0.1105 0.0437  0.0830  604 LEU A CD1 
4720 C CD2 . LEU A 604 ? 0.7214 0.4447 0.6890 -0.1287 0.0391  0.0819  604 LEU A CD2 
4721 N N   . PRO A 605 ? 0.6471 0.3911 0.5317 -0.1093 0.0732  0.1341  605 PRO A N   
4722 C CA  . PRO A 605 ? 0.7275 0.4543 0.6036 -0.1049 0.0738  0.1524  605 PRO A CA  
4723 C C   . PRO A 605 ? 0.7115 0.4061 0.6090 -0.1081 0.0679  0.1493  605 PRO A C   
4724 O O   . PRO A 605 ? 0.7174 0.4035 0.6225 -0.1093 0.0576  0.1296  605 PRO A O   
4725 C CB  . PRO A 605 ? 0.7058 0.4394 0.5544 -0.0932 0.0662  0.1479  605 PRO A CB  
4726 C CG  . PRO A 605 ? 0.6733 0.4328 0.5127 -0.0936 0.0676  0.1324  605 PRO A CG  
4727 C CD  . PRO A 605 ? 0.6798 0.4373 0.5439 -0.1014 0.0679  0.1201  605 PRO A CD  
4728 N N   . TYR A 606 ? 0.7381 0.4150 0.6453 -0.1096 0.0753  0.1692  606 TYR A N   
4729 C CA  . TYR A 606 ? 0.7623 0.4064 0.6938 -0.1142 0.0725  0.1645  606 TYR A CA  
4730 C C   . TYR A 606 ? 0.7395 0.3672 0.6599 -0.1051 0.0602  0.1489  606 TYR A C   
4731 O O   . TYR A 606 ? 0.7337 0.3428 0.6686 -0.1102 0.0537  0.1311  606 TYR A O   
4732 C CB  . TYR A 606 ? 0.7630 0.3920 0.7087 -0.1149 0.0830  0.1897  606 TYR A CB  
4733 C CG  . TYR A 606 ? 0.8929 0.4936 0.8625 -0.1167 0.0767  0.1797  606 TYR A CG  
4734 C CD1 . TYR A 606 ? 0.9266 0.5171 0.9257 -0.1312 0.0763  0.1639  606 TYR A CD1 
4735 C CD2 . TYR A 606 ? 0.8554 0.4408 0.8189 -0.1043 0.0720  0.1841  606 TYR A CD2 
4736 C CE1 . TYR A 606 ? 1.0258 0.5905 1.0438 -0.1339 0.0718  0.1512  606 TYR A CE1 
4737 C CE2 . TYR A 606 ? 0.9178 0.4760 0.9019 -0.1060 0.0689  0.1723  606 TYR A CE2 
4738 C CZ  . TYR A 606 ? 1.0187 0.5662 1.0284 -0.1211 0.0690  0.1552  606 TYR A CZ  
4739 O OH  . TYR A 606 ? 0.9779 0.4992 1.0065 -0.1237 0.0670  0.1406  606 TYR A OH  
4740 N N   . GLU A 607 ? 0.6991 0.3356 0.5942 -0.0923 0.0571  0.1542  607 GLU A N   
4741 C CA  . GLU A 607 ? 0.7667 0.3889 0.6530 -0.0834 0.0481  0.1407  607 GLU A CA  
4742 C C   . GLU A 607 ? 0.7559 0.3826 0.6372 -0.0865 0.0384  0.1146  607 GLU A C   
4743 O O   . GLU A 607 ? 0.7636 0.3718 0.6463 -0.0855 0.0323  0.0994  607 GLU A O   
4744 C CB  . GLU A 607 ? 0.8032 0.4405 0.6675 -0.0701 0.0469  0.1514  607 GLU A CB  
4745 C CG  . GLU A 607 ? 0.8885 0.5299 0.7530 -0.0654 0.0549  0.1813  607 GLU A CG  
4746 C CD  . GLU A 607 ? 0.9460 0.6072 0.7903 -0.0518 0.0506  0.1908  607 GLU A CD  
4747 O OE1 . GLU A 607 ? 0.9104 0.5625 0.7543 -0.0433 0.0444  0.1811  607 GLU A OE1 
4748 O OE2 . GLU A 607 ? 1.0588 0.7475 0.8879 -0.0501 0.0535  0.2071  607 GLU A OE2 
4749 N N   . ILE A 608 ? 0.7175 0.3692 0.5932 -0.0898 0.0378  0.1098  608 ILE A N   
4750 C CA  . ILE A 608 ? 0.7262 0.3829 0.6005 -0.0917 0.0291  0.0896  608 ILE A CA  
4751 C C   . ILE A 608 ? 0.7445 0.3898 0.6416 -0.1023 0.0247  0.0798  608 ILE A C   
4752 O O   . ILE A 608 ? 0.7391 0.3780 0.6335 -0.1025 0.0147  0.0632  608 ILE A O   
4753 C CB  . ILE A 608 ? 0.6494 0.3341 0.5183 -0.0917 0.0317  0.0881  608 ILE A CB  
4754 C CG1 . ILE A 608 ? 0.6824 0.3802 0.5293 -0.0831 0.0351  0.0929  608 ILE A CG1 
4755 C CG2 . ILE A 608 ? 0.6596 0.3488 0.5306 -0.0918 0.0231  0.0715  608 ILE A CG2 
4756 C CD1 . ILE A 608 ? 0.6636 0.3517 0.4961 -0.0747 0.0285  0.0832  608 ILE A CD1 
4757 N N   . GLU A 609 ? 0.6904 0.3349 0.6101 -0.1118 0.0323  0.0898  609 GLU A N   
4758 C CA  . GLU A 609 ? 0.7717 0.4062 0.7186 -0.1240 0.0286  0.0791  609 GLU A CA  
4759 C C   . GLU A 609 ? 0.7588 0.3626 0.7080 -0.1240 0.0252  0.0701  609 GLU A C   
4760 O O   . GLU A 609 ? 0.7082 0.3058 0.6667 -0.1310 0.0159  0.0503  609 GLU A O   
4761 C CB  . GLU A 609 ? 0.7775 0.4168 0.7513 -0.1349 0.0409  0.0935  609 GLU A CB  
4762 C CG  . GLU A 609 ? 0.9055 0.5307 0.9143 -0.1497 0.0401  0.0839  609 GLU A CG  
4763 C CD  . GLU A 609 ? 0.9869 0.6359 1.0158 -0.1589 0.0309  0.0677  609 GLU A CD  
4764 O OE1 . GLU A 609 ? 0.9935 0.6634 1.0063 -0.1513 0.0222  0.0610  609 GLU A OE1 
4765 O OE2 . GLU A 609 ? 1.0315 0.6787 1.0954 -0.1735 0.0326  0.0623  609 GLU A OE2 
4766 N N   . ARG A 610 ? 0.7422 0.3285 0.6838 -0.1160 0.0328  0.0837  610 ARG A N   
4767 C CA  . ARG A 610 ? 0.7661 0.3213 0.7132 -0.1145 0.0325  0.0748  610 ARG A CA  
4768 C C   . ARG A 610 ? 0.7561 0.3103 0.6802 -0.1080 0.0215  0.0536  610 ARG A C   
4769 O O   . ARG A 610 ? 0.7276 0.2637 0.6570 -0.1123 0.0174  0.0342  610 ARG A O   
4770 C CB  . ARG A 610 ? 0.8251 0.3728 0.7757 -0.1031 0.0416  0.0968  610 ARG A CB  
4771 C CG  . ARG A 610 ? 0.8158 0.3408 0.7817 -0.0981 0.0411  0.0882  610 ARG A CG  
4772 C CD  . ARG A 610 ? 0.8070 0.3282 0.7789 -0.0869 0.0473  0.1133  610 ARG A CD  
4773 N NE  . ARG A 610 ? 0.8071 0.3438 0.7532 -0.0733 0.0472  0.1262  610 ARG A NE  
4774 C CZ  . ARG A 610 ? 0.8456 0.3882 0.7891 -0.0628 0.0507  0.1512  610 ARG A CZ  
4775 N NH1 . ARG A 610 ? 0.9994 0.5316 0.9599 -0.0634 0.0558  0.1676  610 ARG A NH1 
4776 N NH2 . ARG A 610 ? 0.8196 0.3783 0.7389 -0.0517 0.0492  0.1592  610 ARG A NH2 
4777 N N   . GLU A 611 ? 0.7258 0.2994 0.6245 -0.0982 0.0179  0.0561  611 GLU A N   
4778 C CA  . GLU A 611 ? 0.7350 0.3087 0.6112 -0.0921 0.0098  0.0390  611 GLU A CA  
4779 C C   . GLU A 611 ? 0.7148 0.2973 0.5919 -0.1005 -0.0016 0.0209  611 GLU A C   
4780 O O   . GLU A 611 ? 0.7147 0.2880 0.5804 -0.1005 -0.0081 0.0032  611 GLU A O   
4781 C CB  . GLU A 611 ? 0.6959 0.2884 0.5503 -0.0815 0.0104  0.0467  611 GLU A CB  
4782 C CG  . GLU A 611 ? 0.7417 0.3312 0.5927 -0.0719 0.0182  0.0621  611 GLU A CG  
4783 C CD  . GLU A 611 ? 0.7336 0.2989 0.5850 -0.0655 0.0203  0.0558  611 GLU A CD  
4784 O OE1 . GLU A 611 ? 0.7075 0.2634 0.5501 -0.0664 0.0161  0.0369  611 GLU A OE1 
4785 O OE2 . GLU A 611 ? 0.7739 0.3310 0.6344 -0.0589 0.0268  0.0704  611 GLU A OE2 
4786 N N   . LEU A 612 ? 0.6934 0.2964 0.5840 -0.1072 -0.0040 0.0252  612 LEU A N   
4787 C CA  . LEU A 612 ? 0.6876 0.3031 0.5855 -0.1151 -0.0164 0.0100  612 LEU A CA  
4788 C C   . LEU A 612 ? 0.7604 0.3590 0.6755 -0.1266 -0.0201 -0.0063 612 LEU A C   
4789 O O   . LEU A 612 ? 0.7398 0.3412 0.6461 -0.1296 -0.0323 -0.0256 612 LEU A O   
4790 C CB  . LEU A 612 ? 0.6752 0.3159 0.5933 -0.1202 -0.0158 0.0187  612 LEU A CB  
4791 C CG  . LEU A 612 ? 0.7179 0.3771 0.6538 -0.1288 -0.0292 0.0057  612 LEU A CG  
4792 C CD1 . LEU A 612 ? 0.7083 0.3784 0.6197 -0.1201 -0.0425 -0.0029 612 LEU A CD1 
4793 C CD2 . LEU A 612 ? 0.8066 0.4893 0.7699 -0.1339 -0.0243 0.0157  612 LEU A CD2 
4794 N N   . ARG A 613 ? 0.7328 0.3139 0.6726 -0.1335 -0.0092 0.0009  613 ARG A N   
4795 C CA  . ARG A 613 ? 0.7075 0.2687 0.6693 -0.1460 -0.0100 -0.0166 613 ARG A CA  
4796 C C   . ARG A 613 ? 0.7076 0.2450 0.6499 -0.1401 -0.0105 -0.0325 613 ARG A C   
4797 O O   . ARG A 613 ? 0.7333 0.2642 0.6786 -0.1489 -0.0179 -0.0578 613 ARG A O   
4798 C CB  . ARG A 613 ? 0.7239 0.2679 0.7192 -0.1537 0.0051  -0.0013 613 ARG A CB  
4799 C CG  . ARG A 613 ? 0.7979 0.3644 0.8176 -0.1629 0.0084  0.0114  613 ARG A CG  
4800 C CD  . ARG A 613 ? 0.8300 0.3760 0.8826 -0.1716 0.0253  0.0269  613 ARG A CD  
4801 N NE  . ARG A 613 ? 0.9553 0.5236 1.0297 -0.1799 0.0321  0.0415  613 ARG A NE  
4802 C CZ  . ARG A 613 ? 1.0351 0.6002 1.1357 -0.1876 0.0438  0.0553  613 ARG A CZ  
4803 N NH1 . ARG A 613 ? 0.9780 0.5201 1.0859 -0.1869 0.0483  0.0566  613 ARG A NH1 
4804 N NH2 . ARG A 613 ? 1.0938 0.6813 1.2119 -0.1950 0.0518  0.0676  613 ARG A NH2 
4805 N N   . ALA A 614 ? 0.7096 0.2361 0.6330 -0.1257 -0.0021 -0.0196 614 ALA A N   
4806 C CA  . ALA A 614 ? 0.7157 0.2204 0.6238 -0.1191 0.0003  -0.0341 614 ALA A CA  
4807 C C   . ALA A 614 ? 0.7750 0.2940 0.6507 -0.1164 -0.0120 -0.0529 614 ALA A C   
4808 O O   . ALA A 614 ? 0.8207 0.3270 0.6878 -0.1195 -0.0142 -0.0764 614 ALA A O   
4809 C CB  . ALA A 614 ? 0.7107 0.2067 0.6121 -0.1036 0.0116  -0.0140 614 ALA A CB  
4810 N N   . LEU A 615 ? 0.7399 0.2849 0.5970 -0.1105 -0.0188 -0.0428 615 LEU A N   
4811 C CA  . LEU A 615 ? 0.7558 0.3150 0.5826 -0.1072 -0.0299 -0.0556 615 LEU A CA  
4812 C C   . LEU A 615 ? 0.8119 0.3814 0.6441 -0.1199 -0.0442 -0.0765 615 LEU A C   
4813 O O   . LEU A 615 ? 0.7525 0.3215 0.5614 -0.1204 -0.0511 -0.0961 615 LEU A O   
4814 C CB  . LEU A 615 ? 0.7985 0.3813 0.6125 -0.0988 -0.0326 -0.0385 615 LEU A CB  
4815 C CG  . LEU A 615 ? 0.7509 0.3500 0.5366 -0.0942 -0.0437 -0.0449 615 LEU A CG  
4816 C CD1 . LEU A 615 ? 0.7825 0.3673 0.5379 -0.0872 -0.0391 -0.0551 615 LEU A CD1 
4817 C CD2 . LEU A 615 ? 0.6389 0.2570 0.4218 -0.0865 -0.0434 -0.0270 615 LEU A CD2 
4818 N N   . LYS A 616 ? 0.7805 0.3622 0.6436 -0.1308 -0.0488 -0.0735 616 LYS A N   
4819 C CA  . LYS A 616 ? 0.7997 0.3965 0.6739 -0.1441 -0.0640 -0.0944 616 LYS A CA  
4820 C C   . LYS A 616 ? 0.8196 0.3927 0.7005 -0.1546 -0.0618 -0.1209 616 LYS A C   
4821 O O   . LYS A 616 ? 0.8089 0.3937 0.6815 -0.1630 -0.0758 -0.1458 616 LYS A O   
4822 C CB  . LYS A 616 ? 0.7847 0.3995 0.6978 -0.1542 -0.0663 -0.0853 616 LYS A CB  
4823 C CG  . LYS A 616 ? 0.9094 0.5486 0.8395 -0.1680 -0.0845 -0.1058 616 LYS A CG  
4824 C CD  . LYS A 616 ? 0.9987 0.6656 0.9630 -0.1731 -0.0877 -0.0927 616 LYS A CD  
4825 C CE  . LYS A 616 ? 1.0751 0.7748 1.0556 -0.1841 -0.1094 -0.1119 616 LYS A CE  
4826 N NZ  . LYS A 616 ? 1.1148 0.8465 1.1291 -0.1861 -0.1129 -0.0983 616 LYS A NZ  
4827 N N   . GLN A 617 ? 0.8064 0.3471 0.7026 -0.1538 -0.0445 -0.1165 617 GLN A N   
4828 C CA  . GLN A 617 ? 0.8564 0.3698 0.7631 -0.1626 -0.0391 -0.1425 617 GLN A CA  
4829 C C   . GLN A 617 ? 0.8676 0.3742 0.7341 -0.1539 -0.0396 -0.1602 617 GLN A C   
4830 O O   . GLN A 617 ? 0.8557 0.3599 0.7148 -0.1633 -0.0457 -0.1916 617 GLN A O   
4831 C CB  . GLN A 617 ? 0.8166 0.2995 0.7571 -0.1609 -0.0193 -0.1278 617 GLN A CB  
4832 C CG  . GLN A 617 ? 0.8419 0.3088 0.8096 -0.1639 -0.0144 -0.1490 617 GLN A CG  
4833 C CD  . GLN A 617 ? 0.8655 0.3393 0.8612 -0.1838 -0.0245 -0.1695 617 GLN A CD  
4834 O OE1 . GLN A 617 ? 0.9601 0.4513 0.9705 -0.1951 -0.0309 -0.1627 617 GLN A OE1 
4835 N NE2 . GLN A 617 ? 0.9293 0.3904 0.9313 -0.1888 -0.0252 -0.1947 617 GLN A NE2 
4836 N N   . ARG A 618 ? 0.8020 0.3071 0.6423 -0.1368 -0.0326 -0.1418 618 ARG A N   
4837 C CA  . ARG A 618 ? 0.8919 0.3915 0.6948 -0.1283 -0.0302 -0.1564 618 ARG A CA  
4838 C C   . ARG A 618 ? 0.9164 0.4443 0.6850 -0.1313 -0.0480 -0.1714 618 ARG A C   
4839 O O   . ARG A 618 ? 0.9673 0.4916 0.7079 -0.1317 -0.0484 -0.1948 618 ARG A O   
4840 C CB  . ARG A 618 ? 0.7927 0.2895 0.5800 -0.1106 -0.0192 -0.1323 618 ARG A CB  
4841 C CG  . ARG A 618 ? 0.8224 0.2937 0.6382 -0.1047 -0.0026 -0.1180 618 ARG A CG  
4842 C CD  . ARG A 618 ? 0.7673 0.2404 0.5665 -0.0880 0.0063  -0.1000 618 ARG A CD  
4843 N NE  . ARG A 618 ? 0.7597 0.2599 0.5436 -0.0835 -0.0012 -0.0809 618 ARG A NE  
4844 C CZ  . ARG A 618 ? 0.7947 0.3045 0.5951 -0.0816 -0.0003 -0.0574 618 ARG A CZ  
4845 N NH1 . ARG A 618 ? 0.8094 0.3056 0.6393 -0.0832 0.0070  -0.0461 618 ARG A NH1 
4846 N NH2 . ARG A 618 ? 0.8074 0.3405 0.5939 -0.0778 -0.0057 -0.0447 618 ARG A NH2 
4847 N N   . ILE A 619 ? 0.8692 0.4264 0.6393 -0.1327 -0.0624 -0.1577 619 ILE A N   
4848 C CA  . ILE A 619 ? 0.9284 0.5156 0.6683 -0.1338 -0.0812 -0.1675 619 ILE A CA  
4849 C C   . ILE A 619 ? 0.9457 0.5413 0.6964 -0.1513 -0.0946 -0.1994 619 ILE A C   
4850 O O   . ILE A 619 ? 0.9954 0.6066 0.7127 -0.1534 -0.1065 -0.2196 619 ILE A O   
4851 C CB  . ILE A 619 ? 0.8454 0.4609 0.5893 -0.1278 -0.0912 -0.1413 619 ILE A CB  
4852 C CG1 . ILE A 619 ? 0.8250 0.4337 0.5520 -0.1113 -0.0783 -0.1159 619 ILE A CG1 
4853 C CG2 . ILE A 619 ? 0.8320 0.4816 0.5537 -0.1291 -0.1133 -0.1489 619 ILE A CG2 
4854 C CD1 . ILE A 619 ? 0.8332 0.4629 0.5721 -0.1055 -0.0826 -0.0910 619 ILE A CD1 
4855 N N   . SER A 620 ? 0.8915 0.4780 0.6886 -0.1649 -0.0923 -0.2050 620 SER A N   
4856 C CA  . SER A 620 ? 0.9474 0.5412 0.7620 -0.1842 -0.1039 -0.2385 620 SER A CA  
4857 C C   . SER A 620 ? 0.9678 0.5367 0.7658 -0.1891 -0.0956 -0.2719 620 SER A C   
4858 O O   . SER A 620 ? 0.9712 0.5532 0.7707 -0.2034 -0.1076 -0.3054 620 SER A O   
4859 C CB  . SER A 620 ? 0.9403 0.5256 0.8132 -0.1983 -0.0988 -0.2352 620 SER A CB  
4860 O OG  . SER A 620 ? 0.9708 0.5141 0.8655 -0.1963 -0.0751 -0.2279 620 SER A OG  
4861 N N   . GLN A 621 ? 0.9447 0.4824 0.7302 -0.1767 -0.0753 -0.2647 621 GLN A N   
4862 C CA  . GLN A 621 ? 1.0316 0.5577 0.8145 -0.1730 -0.0645 -0.2905 621 GLN A CA  
4863 C C   . GLN A 621 ? 1.1024 0.6427 0.8251 -0.1652 -0.0688 -0.3019 621 GLN A C   
4864 O O   . GLN A 621 ? 1.1280 0.6613 0.8437 -0.1603 -0.0591 -0.3227 621 GLN A O   
4865 C CB  . GLN A 621 ? 1.0492 0.5428 0.8607 -0.1603 -0.0406 -0.2739 621 GLN A CB  
4866 C CG  . GLN A 621 ? 1.0054 0.4836 0.8747 -0.1660 -0.0349 -0.2605 621 GLN A CG  
4867 C CD  . GLN A 621 ? 1.0713 0.5475 0.9680 -0.1813 -0.0428 -0.2869 621 GLN A CD  
4868 O OE1 . GLN A 621 ? 1.0934 0.5551 0.9884 -0.1803 -0.0372 -0.3081 621 GLN A OE1 
4869 N NE2 . GLN A 621 ? 1.0713 0.5616 0.9916 -0.1964 -0.0546 -0.2851 621 GLN A NE2 
4870 N N   . MET A 622 ? 1.0950 0.6564 0.7763 -0.1615 -0.0833 -0.2858 622 MET A N   
4871 C CA  . MET A 622 ? 1.1296 0.7078 0.7526 -0.1528 -0.0875 -0.2913 622 MET A CA  
4872 C C   . MET A 622 ? 1.1371 0.7445 0.7434 -0.1643 -0.1048 -0.3262 622 MET A C   
4873 O O   . MET A 622 ? 1.1370 0.7619 0.7727 -0.1786 -0.1211 -0.3395 622 MET A O   
4874 C CB  . MET A 622 ? 1.1171 0.7213 0.7183 -0.1389 -0.0968 -0.2549 622 MET A CB  
4875 C CG  . MET A 622 ? 1.0135 0.5992 0.6304 -0.1250 -0.0796 -0.2213 622 MET A CG  
4876 S SD  . MET A 622 ? 1.0256 0.6391 0.6181 -0.1100 -0.0881 -0.1841 622 MET A SD  
4877 C CE  . MET A 622 ? 1.0478 0.6712 0.5751 -0.1030 -0.0878 -0.1948 622 MET A CE  
4878 O OXT . MET A 622 ? 1.2110 0.8304 0.7783 -0.1583 -0.1027 -0.3409 622 MET A OXT 
# 
