data_9EJ0
# 
_entry.id   9EJ0 
# 
_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   9EJ0         pdb_00009ej0 10.2210/pdb9ej0/pdb 
WWPDB D_1000290517 ?            ?                   
# 
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                        9EJ0 
_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    155 ?        ? ? ? 
# 
_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   801 120  HOH HOH A . 
H 6 HOH 2   802 90   HOH HOH A . 
H 6 HOH 3   803 23   HOH HOH A . 
H 6 HOH 4   804 57   HOH HOH A . 
H 6 HOH 5   805 91   HOH HOH A . 
H 6 HOH 6   806 24   HOH HOH A . 
H 6 HOH 7   807 148  HOH HOH A . 
H 6 HOH 8   808 33   HOH HOH A . 
H 6 HOH 9   809 132  HOH HOH A . 
H 6 HOH 10  810 76   HOH HOH A . 
H 6 HOH 11  811 22   HOH HOH A . 
H 6 HOH 12  812 69   HOH HOH A . 
H 6 HOH 13  813 92   HOH HOH A . 
H 6 HOH 14  814 115  HOH HOH A . 
H 6 HOH 15  815 117  HOH HOH A . 
H 6 HOH 16  816 155  HOH HOH A . 
H 6 HOH 17  817 37   HOH HOH A . 
H 6 HOH 18  818 129  HOH HOH A . 
H 6 HOH 19  819 128  HOH HOH A . 
H 6 HOH 20  820 63   HOH HOH A . 
H 6 HOH 21  821 145  HOH HOH A . 
H 6 HOH 22  822 47   HOH HOH A . 
H 6 HOH 23  823 25   HOH HOH A . 
H 6 HOH 24  824 72   HOH HOH A . 
H 6 HOH 25  825 32   HOH HOH A . 
H 6 HOH 26  826 82   HOH HOH A . 
H 6 HOH 27  827 144  HOH HOH A . 
H 6 HOH 28  828 51   HOH HOH A . 
H 6 HOH 29  829 151  HOH HOH A . 
H 6 HOH 30  830 121  HOH HOH A . 
H 6 HOH 31  831 56   HOH HOH A . 
H 6 HOH 32  832 6    HOH HOH A . 
H 6 HOH 33  833 38   HOH HOH A . 
H 6 HOH 34  834 68   HOH HOH A . 
H 6 HOH 35  835 9    HOH HOH A . 
H 6 HOH 36  836 31   HOH HOH A . 
H 6 HOH 37  837 93   HOH HOH A . 
H 6 HOH 38  838 140  HOH HOH A . 
H 6 HOH 39  839 40   HOH HOH A . 
H 6 HOH 40  840 41   HOH HOH A . 
H 6 HOH 41  841 103  HOH HOH A . 
H 6 HOH 42  842 43   HOH HOH A . 
H 6 HOH 43  843 39   HOH HOH A . 
H 6 HOH 44  844 26   HOH HOH A . 
H 6 HOH 45  845 48   HOH HOH A . 
H 6 HOH 46  846 118  HOH HOH A . 
H 6 HOH 47  847 105  HOH HOH A . 
H 6 HOH 48  848 54   HOH HOH A . 
H 6 HOH 49  849 150  HOH HOH A . 
H 6 HOH 50  850 14   HOH HOH A . 
H 6 HOH 51  851 20   HOH HOH A . 
H 6 HOH 52  852 97   HOH HOH A . 
H 6 HOH 53  853 100  HOH HOH A . 
H 6 HOH 54  854 29   HOH HOH A . 
H 6 HOH 55  855 34   HOH HOH A . 
H 6 HOH 56  856 80   HOH HOH A . 
H 6 HOH 57  857 60   HOH HOH A . 
H 6 HOH 58  858 73   HOH HOH A . 
H 6 HOH 59  859 106  HOH HOH A . 
H 6 HOH 60  860 62   HOH HOH A . 
H 6 HOH 61  861 84   HOH HOH A . 
H 6 HOH 62  862 64   HOH HOH A . 
H 6 HOH 63  863 134  HOH HOH A . 
H 6 HOH 64  864 7    HOH HOH A . 
H 6 HOH 65  865 96   HOH HOH A . 
H 6 HOH 66  866 65   HOH HOH A . 
H 6 HOH 67  867 87   HOH HOH A . 
H 6 HOH 68  868 36   HOH HOH A . 
H 6 HOH 69  869 49   HOH HOH A . 
H 6 HOH 70  870 71   HOH HOH A . 
H 6 HOH 71  871 19   HOH HOH A . 
H 6 HOH 72  872 94   HOH HOH A . 
H 6 HOH 73  873 78   HOH HOH A . 
H 6 HOH 74  874 8    HOH HOH A . 
H 6 HOH 75  875 70   HOH HOH A . 
H 6 HOH 76  876 17   HOH HOH A . 
H 6 HOH 77  877 79   HOH HOH A . 
H 6 HOH 78  878 58   HOH HOH A . 
H 6 HOH 79  879 89   HOH HOH A . 
H 6 HOH 80  880 11   HOH HOH A . 
H 6 HOH 81  881 21   HOH HOH A . 
H 6 HOH 82  882 123  HOH HOH A . 
H 6 HOH 83  883 83   HOH HOH A . 
H 6 HOH 84  884 35   HOH HOH A . 
H 6 HOH 85  885 30   HOH HOH A . 
H 6 HOH 86  886 46   HOH HOH A . 
H 6 HOH 87  887 116  HOH HOH A . 
H 6 HOH 88  888 81   HOH HOH A . 
H 6 HOH 89  889 143  HOH HOH A . 
H 6 HOH 90  890 95   HOH HOH A . 
H 6 HOH 91  891 53   HOH HOH A . 
H 6 HOH 92  892 61   HOH HOH A . 
H 6 HOH 93  893 88   HOH HOH A . 
H 6 HOH 94  894 15   HOH HOH A . 
H 6 HOH 95  895 77   HOH HOH A . 
H 6 HOH 96  896 110  HOH HOH A . 
H 6 HOH 97  897 42   HOH HOH A . 
H 6 HOH 98  898 12   HOH HOH A . 
H 6 HOH 99  899 107  HOH HOH A . 
H 6 HOH 100 900 55   HOH HOH A . 
H 6 HOH 101 901 85   HOH HOH A . 
H 6 HOH 102 902 102  HOH HOH A . 
H 6 HOH 103 903 44   HOH HOH A . 
H 6 HOH 104 904 147  HOH HOH A . 
H 6 HOH 105 905 112  HOH HOH A . 
H 6 HOH 106 906 99   HOH HOH A . 
H 6 HOH 107 907 104  HOH HOH A . 
H 6 HOH 108 908 16   HOH HOH A . 
H 6 HOH 109 909 114  HOH HOH A . 
H 6 HOH 110 910 75   HOH HOH A . 
H 6 HOH 111 911 138  HOH HOH A . 
H 6 HOH 112 912 131  HOH HOH A . 
H 6 HOH 113 913 125  HOH HOH A . 
H 6 HOH 114 914 18   HOH HOH A . 
H 6 HOH 115 915 149  HOH HOH A . 
H 6 HOH 116 916 5    HOH HOH A . 
H 6 HOH 117 917 45   HOH HOH A . 
H 6 HOH 118 918 27   HOH HOH A . 
H 6 HOH 119 919 3    HOH HOH A . 
H 6 HOH 120 920 67   HOH HOH A . 
H 6 HOH 121 921 141  HOH HOH A . 
H 6 HOH 122 922 13   HOH HOH A . 
H 6 HOH 123 923 146  HOH HOH A . 
H 6 HOH 124 924 4    HOH HOH A . 
H 6 HOH 125 925 1    HOH HOH A . 
H 6 HOH 126 926 101  HOH HOH A . 
H 6 HOH 127 927 127  HOH HOH A . 
H 6 HOH 128 928 74   HOH HOH A . 
H 6 HOH 129 929 50   HOH HOH A . 
H 6 HOH 130 930 59   HOH HOH A . 
H 6 HOH 131 931 10   HOH HOH A . 
H 6 HOH 132 932 86   HOH HOH A . 
H 6 HOH 133 933 2    HOH HOH A . 
H 6 HOH 134 934 139  HOH HOH A . 
H 6 HOH 135 935 52   HOH HOH A . 
H 6 HOH 136 936 66   HOH HOH A . 
H 6 HOH 137 937 122  HOH HOH A . 
H 6 HOH 138 938 124  HOH HOH A . 
H 6 HOH 139 939 130  HOH HOH A . 
H 6 HOH 140 940 153  HOH HOH A . 
H 6 HOH 141 941 98   HOH HOH A . 
H 6 HOH 142 942 113  HOH HOH A . 
H 6 HOH 143 943 108  HOH HOH A . 
H 6 HOH 144 944 154  HOH HOH A . 
H 6 HOH 145 945 152  HOH HOH A . 
H 6 HOH 146 946 109  HOH HOH A . 
H 6 HOH 147 947 142  HOH HOH A . 
H 6 HOH 148 948 126  HOH HOH A . 
H 6 HOH 149 949 28   HOH HOH A . 
H 6 HOH 150 950 111  HOH HOH A . 
H 6 HOH 151 951 133  HOH HOH A . 
H 6 HOH 152 952 136  HOH HOH A . 
H 6 HOH 153 953 119  HOH HOH A . 
H 6 HOH 154 954 135  HOH HOH A . 
H 6 HOH 155 955 137  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                   111.84 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EJ0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.281 
_cell.length_a_esd                 ? 
_cell.length_b                     120.174 
_cell.length_b_esd                 ? 
_cell.length_c                     60.817 
_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                         9EJ0 
_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                   9EJ0 
_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          44.34 
_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                     273 
_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                                       9EJ0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               120.43 
_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                                     43997 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.78 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.5 
_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                                0.116 
_reflns.pdbx_Rpim_I_all                                0.044 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.107 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.95 
_reflns_shell.d_res_low                                     1.98 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.6000 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2210 
_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                               6.8400 
_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                               1.6150 
_reflns_shell.pdbx_Rpim_I_all                               0.6120 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.6440 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.4920 
_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                                 9EJ0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             56.45 
_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                     43903 
_refine.ls_number_reflns_R_free                  2246 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.58 
_refine.ls_percent_reflns_R_free                 5.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1738 
_refine.ls_R_factor_R_free                       0.2053 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1720 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_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                 24.62 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4869 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             155 
_refine_hist.number_atoms_total               5075 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        56.45 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.896  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.013 ? 1902 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 718  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 897  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.95 1.99  . . 132 2473 95.00  . . . . 0.3111 . . . . . . . . . . . 0.3592 
'X-RAY DIFFRACTION' 1.99 2.04  . . 144 2634 100.00 . . . . 0.2765 . . . . . . . . . . . 0.3204 
'X-RAY DIFFRACTION' 2.04 2.09  . . 142 2589 100.00 . . . . 0.2421 . . . . . . . . . . . 0.2464 
'X-RAY DIFFRACTION' 2.09 2.14  . . 139 2602 100.00 . . . . 0.2243 . . . . . . . . . . . 0.2624 
'X-RAY DIFFRACTION' 2.14 2.21  . . 140 2609 100.00 . . . . 0.2110 . . . . . . . . . . . 0.2311 
'X-RAY DIFFRACTION' 2.21 2.28  . . 142 2602 100.00 . . . . 0.2048 . . . . . . . . . . . 0.2468 
'X-RAY DIFFRACTION' 2.28 2.36  . . 129 2602 100.00 . . . . 0.1858 . . . . . . . . . . . 0.2292 
'X-RAY DIFFRACTION' 2.36 2.45  . . 153 2612 100.00 . . . . 0.1854 . . . . . . . . . . . 0.2287 
'X-RAY DIFFRACTION' 2.45 2.57  . . 143 2569 100.00 . . . . 0.1778 . . . . . . . . . . . 0.2632 
'X-RAY DIFFRACTION' 2.57 2.70  . . 129 2622 100.00 . . . . 0.1840 . . . . . . . . . . . 0.2403 
'X-RAY DIFFRACTION' 2.70 2.87  . . 121 2654 100.00 . . . . 0.1743 . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 2.87 3.09  . . 158 2566 100.00 . . . . 0.1704 . . . . . . . . . . . 0.2323 
'X-RAY DIFFRACTION' 3.09 3.40  . . 119 2662 100.00 . . . . 0.1606 . . . . . . . . . . . 0.1701 
'X-RAY DIFFRACTION' 3.40 3.89  . . 141 2592 100.00 . . . . 0.1512 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 3.90 4.91  . . 163 2616 100.00 . . . . 0.1411 . . . . . . . . . . . 0.1655 
'X-RAY DIFFRACTION' 4.91 56.45 . . 151 2653 100.00 . . . . 0.1630 . . . . . . . . . . . 0.1821 
# 
_struct.entry_id                     9EJ0 
_struct.title                        'Rat cytosolic PEPCK in complex with GTP and oxalate (273K)' 
_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        9EJ0 
_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              9EJ0 
_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 PHE A 11  ? ALA A 13  ? PHE A 11  ALA A 13  5 ? 3  
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  ? THR A 102 ? GLU A 98  THR A 102 5 ? 5  
HELX_P HELX_P7  AA7 SER A 118 ? PHE A 130 ? SER A 118 PHE A 130 1 ? 13 
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 PRO A 223 ? ARG A 225 ? PRO A 223 ARG A 225 5 ? 3  
HELX_P HELX_P11 AB2 TYR A 235 ? LEU A 240 ? TYR A 235 LEU A 240 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P13 AB4 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P14 AB5 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P15 AB6 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P16 AB7 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P17 AB8 PRO A 479 ? PHE A 486 ? PRO A 479 PHE A 486 5 ? 8  
HELX_P HELX_P18 AB9 ASN A 489 ? MET A 500 ? ASN A 489 MET A 500 1 ? 12 
HELX_P HELX_P19 AC1 ALA A 501 ? ARG A 503 ? ALA A 501 ARG A 503 5 ? 3  
HELX_P HELX_P20 AC2 GLY A 529 ? GLU A 532 ? GLY A 529 GLU A 532 5 ? 4  
HELX_P HELX_P21 AC3 ASN A 533 ? GLY A 546 ? ASN A 533 GLY A 546 1 ? 14 
HELX_P HELX_P22 AC4 ASN A 573 ? GLY A 579 ? ASN A 573 GLY A 579 1 ? 7  
HELX_P HELX_P23 AC5 SER A 581 ? VAL A 600 ? SER A 581 VAL A 600 1 ? 20 
HELX_P HELX_P24 AC6 ASN A 601 ? LEU A 604 ? ASN A 601 LEU A 604 5 ? 4  
HELX_P HELX_P25 AC7 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 LYS 244 NZ  ? ? ? 1_555 C MN  . MN  ? ? A LYS 244 A MN  702 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc2  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 C MN  . MN  ? ? A HIS 264 A MN  702 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc3  metalc ? ? A THR 291 OG1 ? ? ? 1_555 B MN  . MN  ? ? A THR 291 A MN  701 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
metalc4  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 C MN  . MN  ? ? A ASP 311 A MN  702 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc5  metalc ? ? A HIS 502 NE2 ? ? ? 1_555 D MN  . MN  ? ? A HIS 502 A MN  703 1_555 ? ? ? ? ? ? ? 2.489 ? ? 
metalc6  metalc ? ? A GLU 607 OE1 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 1_555 ? ? ? ? ? ? ? 2.687 ? ? 
metalc7  metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1B ? ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc8  metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1G ? ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 803 1_555 ? ? ? ? ? ? ? 1.925 ? ? 
metalc10 metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 811 1_555 ? ? ? ? ? ? ? 2.169 ? ? 
metalc11 metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 812 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc12 metalc ? ? C MN  .   MN  ? ? ? 1_555 E OXL . O1  ? ? A MN  702 A OXL 704 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
metalc13 metalc ? ? C MN  .   MN  ? ? ? 1_555 E OXL . O2  ? ? A MN  702 A OXL 704 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc14 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O3G ? ? A MN  702 A GTP 705 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
# 
_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  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 85.6  ? 
2  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 96.8  ? 
3  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 90.9  ? 
4  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 87.1  ? 
5  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O1  ? E OXL .   ? A OXL 704 ? 1_555 171.9 ? 
6  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 93.5  ? 
7  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 89.4  ? 
8  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 96.7  ? 
9  OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2  ? E OXL .   ? A OXL 704 ? 1_555 170.6 ? 
10 O1  ? E OXL .   ? A OXL 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2  ? E OXL .   ? A OXL 704 ? 1_555 79.6  ? 
11 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 174.7 ? 
12 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 95.5  ? 
13 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 88.4  ? 
14 O1  ? E OXL .   ? A OXL 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 91.4  ? 
15 O2  ? E OXL .   ? A OXL 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G ? F GTP .   ? A GTP 705 ? 1_555 85.3  ? 
16 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 82.4  ? 
17 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G ? F GTP .   ? A GTP 705 ? 1_555 162.4 ? 
18 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G ? F GTP .   ? A GTP 705 ? 1_555 94.5  ? 
19 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 803 ? 1_555 92.8  ? 
20 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 803 ? 1_555 76.0  ? 
21 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 803 ? 1_555 69.8  ? 
22 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 811 ? 1_555 103.8 ? 
23 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 811 ? 1_555 87.9  ? 
24 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 811 ? 1_555 93.4  ? 
25 O   ? H HOH .   ? A HOH 803 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 811 ? 1_555 155.2 ? 
26 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 812 ? 1_555 86.2  ? 
27 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 812 ? 1_555 167.0 ? 
28 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 812 ? 1_555 98.2  ? 
29 O   ? H HOH .   ? A HOH 803 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 812 ? 1_555 111.2 ? 
30 O   ? H HOH .   ? A HOH 811 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 812 ? 1_555 88.6  ? 
31 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 OE1 ? A GLU 607 ? A GLU 607 ? 1_555 148.5 ? 
# 
_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       5.46 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
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      
AA1 8 9 ? 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 95  ? THR A 92  ILE A 95  
AA1 9 TRP A 116 ? MET A 117 ? TRP A 116 MET A 117 
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  ? LYS A 68  ? ILE A 66  LYS A 68  
AA3 2 TRP A 76  ? ALA A 78  ? TRP A 76  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 TYR A 42  ? N TYR A 42  O MET A 139 ? O MET A 139 
AA1 3 4 N MET A 146 ? N MET A 146 O LYS A 155 ? O LYS A 155 
AA1 4 5 N LEU A 160 ? N LEU A 160 O HIS A 194 ? O HIS A 194 
AA1 5 6 N LEU A 193 ? N LEU A 193 O SER A 230 ? O SER A 230 
AA1 6 7 O ILE A 229 ? O ILE A 229 N ALA A 220 ? N ALA A 220 
AA1 7 8 O HIS A 221 ? O HIS A 221 N ILE A 95  ? N ILE A 95  
AA1 8 9 N ILE A 94  ? N ILE A 94  O MET A 117 ? O MET A 117 
AA2 1 2 N GLN A 17  ? N GLN A 17  O ILE A 45  ? O ILE A 45  
AA2 2 3 N TYR A 42  ? N TYR A 42  O MET A 139 ? O MET A 139 
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 PHE A 406 ? O PHE A 406 N GLY A 334 ? N GLY A 334 
AA4 1 2 N GLU A 263 ? N GLU A 263 O ALA A 313 ? O ALA A 313 
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 GLU A 263 ? N GLU A 263 O ALA A 313 ? O ALA A 313 
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 PHE A 433 ? N PHE A 433 O PHE A 512 ? O PHE A 512 
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                   9EJ0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 A ASP 224 ? ? NH2 A ARG 253 ? ? 2.15 
2 1 OD2 A ASP 598 ? ? O   A HOH 801 ? ? 2.19 
# 
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 HIS A 6   ? ? -137.60 -142.40 
2  1 SER A 108 ? ? -138.19 -48.69  
3  1 LYS A 243 ? ? -88.64  -90.64  
4  1 ASP A 311 ? ? -147.10 -34.27  
5  1 PHE A 333 ? ? -115.25 76.53   
6  1 PRO A 393 ? ? -67.95  14.50   
7  1 ASP A 395 ? ? -101.04 -161.63 
8  1 ALA A 468 ? ? -129.13 -160.24 
9  1 PHE A 480 ? ? 59.02   17.35   
10 1 PHE A 530 ? ? 56.67   -126.62 
11 1 ASN A 601 ? ? 57.50   -123.61 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 24.5709 -11.4415 -5.4464 0.2543 ? 0.0288  ? 0.0491 ? 0.2703 ? 0.0006  ? 0.2700 ? 2.0182 ? 0.7750  
? -0.4966 ? 4.3376 ? 0.6940 ? 2.2973 ? 0.0225  ? 0.0953  ? -0.0858 ? -0.2806 ? -0.0408 ? -0.1419 ? 0.0156  ? 0.2503 ? 0.0379 ? 
2 'X-RAY DIFFRACTION' ? refined 14.7156 -4.2749  10.6287 0.3823 ? -0.0815 ? 0.1200 ? 0.2811 ? -0.0416 ? 0.3639 ? 0.7995 ? -0.2978 
? -0.2040 ? 2.7893 ? 0.2614 ? 1.1554 ? 0.0211  ? -0.0910 ? -0.1168 ? 0.5189  ? -0.0891 ? 0.2577  ? 0.0796  ? 0.0076 ? 0.0506 ? 
3 'X-RAY DIFFRACTION' ? refined 19.8641 16.0077  18.6029 0.4614 ? -0.0278 ? 0.0333 ? 0.1793 ? 0.0414  ? 0.2898 ? 3.6249 ? 0.4250  
? -0.8693 ? 2.7969 ? 0.3196 ? 2.0683 ? -0.0797 ? -0.2725 ? -0.0787 ? 0.4673  ? -0.0395 ? -0.1520 ? -0.0430 ? 0.1459 ? 0.0919 ? 
# 
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 427 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 428 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                    9EJ0 
_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]   0.022084 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008851 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008321 
_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]   0.017714 
_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   ? 25.244  -14.182 -34.708 1.00 78.05  ? 3   PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? 25.702  -15.326 -33.912 1.00 77.67  ? 3   PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? 27.187  -15.254 -33.555 1.00 74.27  ? 3   PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? 27.774  -14.173 -33.555 1.00 73.65  ? 3   PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? 25.423  -16.526 -34.831 1.00 77.58  ? 3   PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? 25.371  -15.948 -36.212 1.00 74.75  ? 3   PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? 24.745  -14.601 -36.030 1.00 76.81  ? 3   PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? 27.773  -16.408 -33.254 1.00 72.45  ? 4   GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? 29.182  -16.553 -32.917 1.00 68.39  ? 4   GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? 29.892  -17.317 -34.032 1.00 61.16  ? 4   GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? 29.283  -17.716 -35.029 1.00 60.03  ? 4   GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? 29.346  -17.282 -31.577 1.00 68.82  ? 4   GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? 28.215  -17.058 -30.576 1.00 74.46  ? 4   GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? 28.272  -15.691 -29.921 1.00 76.48  ? 4   GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? 29.331  -15.257 -29.460 1.00 78.38  ? 4   GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? 27.134  -15.002 -29.879 1.00 78.42  ? 4   GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? 31.196  -17.531 -33.849 1.00 58.02  ? 5   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? 31.961  -18.399 -34.740 1.00 57.23  ? 5   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? 32.105  -19.815 -34.202 1.00 56.28  ? 5   LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? 32.471  -20.721 -34.963 1.00 51.99  ? 5   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? 33.356  -17.811 -34.997 1.00 52.53  ? 5   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? 33.352  -16.513 -35.811 1.00 53.95  ? 5   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? 34.756  -15.942 -35.956 1.00 46.44  ? 5   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? 32.722  -16.752 -37.179 1.00 53.01  ? 5   LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? 31.827  -20.015 -32.916 1.00 57.74  ? 6   HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? 31.890  -21.322 -32.276 1.00 61.87  ? 6   HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? 30.683  -21.482 -31.362 1.00 64.37  ? 6   HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? 29.582  -21.042 -31.709 1.00 66.88  ? 6   HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? 33.203  -21.467 -31.509 1.00 57.97  ? 6   HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? 34.411  -21.338 -32.380 1.00 59.69  ? 6   HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? 35.011  -20.125 -32.644 1.00 56.49  ? 6   HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? 35.108  -22.265 -33.081 1.00 49.94  ? 6   HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? 36.036  -20.312 -33.456 1.00 50.88  ? 6   HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? 36.117  -21.601 -33.737 1.00 55.35  ? 6   HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? 30.860  -22.113 -30.206 1.00 69.12  ? 7   ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? 29.840  -21.981 -29.173 1.00 77.80  ? 7   ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? 29.941  -20.574 -28.607 1.00 75.83  ? 7   ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? 29.069  -19.724 -28.836 1.00 71.82  ? 7   ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? 30.021  -23.020 -28.068 1.00 80.06  ? 7   ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? 29.455  -24.366 -28.442 1.00 84.98  ? 7   ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? 28.458  -24.454 -29.162 1.00 84.00  ? 7   ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? 30.082  -25.429 -27.949 1.00 92.56  ? 7   ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? 31.029  -20.328 -27.887 1.00 72.52  ? 8   GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? 31.328  -19.012 -27.379 1.00 73.28  ? 8   GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? 30.399  -18.557 -26.277 1.00 71.98  ? 8   GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? 30.561  -18.943 -25.114 1.00 69.78  ? 8   GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? 29.405  -17.751 -26.641 1.00 73.54  ? 9   LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? 28.732  -16.885 -25.687 1.00 70.17  ? 9   LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? 27.280  -17.253 -25.425 1.00 65.70  ? 9   LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? 26.628  -16.578 -24.622 1.00 63.64  ? 9   LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? 28.812  -15.431 -26.166 1.00 71.41  ? 9   LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? 30.133  -14.688 -25.942 1.00 75.07  ? 9   LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? 31.280  -15.262 -26.775 1.00 68.99  ? 9   LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? 29.943  -13.202 -26.224 1.00 73.77  ? 9   LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? 26.742  -18.280 -26.075 1.00 63.85  ? 10  ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? 25.363  -18.688 -25.822 1.00 62.72  ? 10  ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? 25.338  -19.658 -24.642 1.00 55.50  ? 10  ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? 25.703  -20.832 -24.781 1.00 54.54  ? 10  ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? 24.736  -19.315 -27.065 1.00 60.23  ? 10  ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? 23.236  -19.512 -26.918 1.00 58.53  ? 10  ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? 22.719  -19.341 -25.791 1.00 61.84  ? 10  ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? 22.568  -19.827 -27.924 1.00 65.49  ? 10  ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? 24.880  -19.173 -23.495 1.00 52.63  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 24.782  -19.969 -22.279 1.00 52.55  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 23.436  -20.676 -22.128 1.00 49.18  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 23.122  -21.146 -21.028 1.00 45.09  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 25.051  -19.088 -21.058 1.00 46.19  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 26.495  -19.065 -20.641 1.00 48.43  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 27.437  -18.384 -21.389 1.00 50.65  ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 26.911  -19.729 -19.496 1.00 51.66  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 28.775  -18.372 -21.003 1.00 52.14  ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 28.248  -19.720 -19.102 1.00 50.31  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 29.178  -19.039 -19.856 1.00 46.98  ? 11  PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? 22.660  -20.781 -23.213 1.00 48.30  ? 12  SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? 21.342  -21.412 -23.165 1.00 49.17  ? 12  SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? 21.414  -22.838 -22.625 1.00 51.20  ? 12  SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? 20.588  -23.241 -21.800 1.00 47.67  ? 12  SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? 20.711  -21.416 -24.563 1.00 53.85  ? 12  SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? 20.235  -20.126 -24.906 1.00 59.03  ? 12  SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? 22.385  -23.626 -23.101 1.00 49.28  ? 13  ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? 22.481  -25.020 -22.674 1.00 46.44  ? 13  ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? 22.695  -25.162 -21.172 1.00 45.86  ? 13  ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? 22.470  -26.248 -20.633 1.00 46.39  ? 13  ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? 23.609  -25.732 -23.421 1.00 48.79  ? 13  ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? 23.116  -24.103 -20.479 1.00 42.60  ? 14  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? 23.379  -24.190 -19.048 1.00 42.55  ? 14  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? 22.216  -23.719 -18.178 1.00 39.59  ? 14  LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? 22.345  -23.723 -16.949 1.00 37.06  ? 14  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? 24.640  -23.393 -18.690 1.00 41.44  ? 14  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? 25.940  -24.068 -19.126 1.00 50.32  ? 14  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? 27.139  -23.307 -18.578 1.00 53.82  ? 14  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? 28.229  -24.252 -18.085 1.00 55.36  ? 14  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? 28.733  -25.152 -19.138 1.00 55.02  ? 14  LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? 21.085  -23.339 -18.764 1.00 39.89  ? 15  VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? 19.994  -22.731 -17.999 1.00 39.67  ? 15  VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? 19.112  -23.839 -17.437 1.00 39.49  ? 15  VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? 18.478  -24.583 -18.194 1.00 43.41  ? 15  VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? 19.177  -21.757 -18.865 1.00 43.01  ? 15  VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? 17.942  -21.274 -18.097 1.00 41.25  ? 15  VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? 20.030  -20.553 -19.276 1.00 41.63  ? 15  VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? 19.063  -23.955 -16.106 1.00 34.73  ? 16  ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? 18.283  -25.017 -15.477 1.00 36.92  ? 16  ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? 16.918  -24.545 -14.996 1.00 42.89  ? 16  ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? 16.122  -25.375 -14.537 1.00 38.33  ? 16  ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? 19.060  -25.670 -14.313 1.00 38.72  ? 16  ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? 19.438  -24.624 -13.270 1.00 36.82  ? 16  ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? 20.303  -26.347 -14.844 1.00 38.46  ? 16  ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? 19.963  -25.217 -11.975 1.00 38.33  ? 16  ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? 16.622  -23.247 -15.077 1.00 39.60  ? 17  GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? 15.257  -22.771 -14.890 1.00 40.62  ? 17  GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? 15.091  -21.451 -15.629 1.00 40.79  ? 17  GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? 15.893  -20.533 -15.449 1.00 36.92  ? 17  GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? 14.893  -22.588 -13.409 1.00 38.15  ? 17  GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? 13.528  -21.915 -13.244 1.00 41.50  ? 17  GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? 13.012  -21.916 -11.824 1.00 44.68  ? 17  GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? 12.946  -22.959 -11.175 1.00 46.36  ? 17  GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? 12.629  -20.744 -11.334 1.00 39.64  ? 17  GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? 14.057  -21.365 -16.453 1.00 41.66  ? 18  GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? 13.805  -20.176 -17.233 1.00 40.64  ? 18  GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? 14.348  -20.281 -18.642 1.00 47.39  ? 18  GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? 14.660  -21.358 -19.159 1.00 46.63  ? 18  GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? 14.469  -19.116 -19.267 1.00 48.59  ? 19  SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? 14.867  -19.001 -20.661 1.00 49.45  ? 19  SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? 15.568  -17.666 -20.841 1.00 52.42  ? 19  SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? 15.008  -16.627 -20.480 1.00 54.16  ? 19  SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? 13.643  -19.091 -21.577 1.00 51.96  ? 19  SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? 13.990  -18.846 -22.925 1.00 56.62  ? 19  SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? 16.796  -17.693 -21.370 1.00 52.02  ? 20  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? 17.458  -16.434 -21.698 1.00 54.44  ? 20  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? 16.663  -15.664 -22.744 1.00 57.22  ? 20  LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? 16.672  -14.428 -22.747 1.00 55.87  ? 20  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? 18.889  -16.683 -22.192 1.00 50.35  ? 20  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? 19.950  -17.225 -21.226 1.00 49.82  ? 20  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? 21.255  -17.528 -21.965 1.00 52.78  ? 20  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? 20.214  -16.279 -20.072 1.00 49.70  ? 20  LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? 15.933  -16.383 -23.606 1.00 57.95  ? 21  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? 15.171  -15.747 -24.677 1.00 68.05  ? 21  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? 14.017  -14.913 -24.145 1.00 71.13  ? 21  ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? 13.615  -13.940 -24.788 1.00 81.23  ? 21  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? 14.633  -16.803 -25.642 1.00 74.35  ? 21  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? 15.729  -17.520 -26.390 1.00 78.50  ? 21  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? 16.722  -16.858 -26.757 1.00 76.95  ? 21  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? 15.601  -18.745 -26.616 1.00 82.55  ? 21  ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? 13.460  -15.279 -22.994 1.00 63.12  ? 22  SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? 12.339  -14.529 -22.447 1.00 62.26  ? 22  SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? 12.773  -13.285 -21.679 1.00 59.09  ? 22  SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? 11.909  -12.545 -21.200 1.00 63.62  ? 22  SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? 11.497  -15.429 -21.542 1.00 60.48  ? 22  SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? 12.112  -15.576 -20.273 1.00 61.60  ? 22  SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? 14.110  -13.024 -21.549 1.00 58.45  ? 23  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? 14.603  -11.863 -20.819 1.00 55.95  ? 23  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? 14.636  -10.629 -21.717 1.00 56.19  ? 23  LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? 14.859  -10.742 -22.927 1.00 53.19  ? 23  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? 16.011  -12.117 -20.293 1.00 51.32  ? 23  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? 16.289  -13.198 -19.258 1.00 51.70  ? 23  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? 17.794  -13.306 -19.084 1.00 50.96  ? 23  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? 15.605  -12.881 -17.926 1.00 49.33  ? 23  LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? 14.425  -9.445  -21.140 1.00 52.57  ? 24  PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? 14.709  -8.203  -21.873 1.00 53.31  ? 24  PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? 16.151  -8.188  -22.367 1.00 53.85  ? 24  PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? 17.059  -8.705  -21.709 1.00 52.14  ? 24  PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? 14.464  -7.104  -20.831 1.00 53.39  ? 24  PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? 13.620  -7.739  -19.770 1.00 54.72  ? 24  PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? 13.944  -9.198  -19.768 1.00 52.96  ? 24  PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? 16.352  -7.578  -23.537 1.00 53.61  ? 25  GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? 17.659  -7.586  -24.195 1.00 55.59  ? 25  GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? 18.787  -7.159  -23.256 1.00 53.85  ? 25  GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? 19.805  -7.850  -23.139 1.00 50.79  ? 25  GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? 17.617  -6.679  -25.425 1.00 64.46  ? 25  GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? 18.972  -6.448  -26.068 1.00 71.05  ? 25  GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? 18.926  -5.382  -27.148 1.00 78.03  ? 25  GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? 18.592  -4.225  -26.879 1.00 78.64  ? 25  GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? 19.254  -5.767  -28.378 1.00 81.74  ? 25  GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? 18.630  -6.016  -22.584 1.00 53.02  ? 26  GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? 19.698  -5.542  -21.709 1.00 50.19  ? 26  GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? 19.886  -6.451  -20.502 1.00 49.01  ? 26  GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? 21.002  -6.569  -19.982 1.00 48.11  ? 26  GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? 19.413  -4.110  -21.258 1.00 53.80  ? 26  GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? 19.467  -3.090  -22.392 1.00 58.88  ? 26  GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? 20.792  -3.116  -23.146 1.00 62.18  ? 26  GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? 21.854  -3.241  -22.493 1.00 59.41  ? 26  GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? 20.766  -3.016  -24.395 1.00 65.04  ? 26  GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? 18.815  -7.089  -20.031 1.00 48.37  ? 27  VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? 18.972  -8.071  -18.965 1.00 46.32  ? 27  VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? 19.769  -9.268  -19.468 1.00 44.14  ? 27  VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? 20.680  -9.752  -18.788 1.00 41.53  ? 27  VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? 17.598  -8.488  -18.406 1.00 48.61  ? 27  VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? 17.752  -9.610  -17.382 1.00 39.96  ? 27  VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? 16.905  -7.288  -17.771 1.00 45.60  ? 27  VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? 19.466  -9.746  -20.678 1.00 40.75  ? 28  ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? 20.179  -10.915 -21.183 1.00 47.82  ? 28  ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? 21.665  -10.627 -21.355 1.00 44.26  ? 28  ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? 22.507  -11.446 -20.975 1.00 45.66  ? 28  ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? 19.585  -11.405 -22.503 1.00 44.04  ? 28  ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? 20.212  -12.741 -22.902 1.00 47.99  ? 28  ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? 19.800  -13.259 -24.266 1.00 52.82  ? 28  ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? 20.604  -14.431 -24.605 1.00 54.30  ? 28  ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? 20.203  -15.423 -25.389 1.00 56.58  ? 28  ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? 19.007  -15.418 -25.952 1.00 58.39  ? 28  ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? 21.021  -16.452 -25.605 1.00 58.43  ? 28  ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? 22.006  -9.466  -21.917 1.00 41.86  ? 29  LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? 23.412  -9.100  -22.060 1.00 43.63  ? 29  LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? 24.119  -9.090  -20.708 1.00 43.33  ? 29  LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? 25.276  -9.513  -20.605 1.00 40.74  ? 29  LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? 23.537  -7.729  -22.738 1.00 46.49  ? 29  LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? 23.038  -7.681  -24.180 1.00 56.26  ? 29  LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? 23.183  -6.271  -24.765 1.00 58.79  ? 29  LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? 22.759  -6.204  -26.226 1.00 72.44  ? 29  LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? 23.788  -6.750  -27.167 1.00 80.45  ? 29  LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? 23.430  -8.612  -19.663 1.00 39.85  ? 30  PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? 23.999  -8.563  -18.316 1.00 36.85  ? 30  PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? 24.267  -9.964  -17.769 1.00 39.39  ? 30  PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? 25.332  -10.226 -17.196 1.00 37.53  ? 30  PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? 23.047  -7.795  -17.388 1.00 34.67  ? 30  PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? 23.520  -7.679  -15.957 1.00 33.40  ? 30  PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? 24.778  -7.202  -15.661 1.00 36.09  ? 30  PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? 22.669  -8.010  -14.905 1.00 33.07  ? 30  PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? 25.204  -7.086  -14.343 1.00 34.56  ? 30  PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? 23.081  -7.887  -13.578 1.00 33.10  ? 30  PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? 24.350  -7.429  -13.298 1.00 33.77  ? 30  PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? 23.292  -10.871 -17.901 1.00 38.95  ? 31  VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? 23.489  -12.237 -17.413 1.00 37.36  ? 31  VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? 24.604  -12.920 -18.196 1.00 39.72  ? 31  VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? 25.519  -13.515 -17.615 1.00 40.37  ? 31  VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? 22.172  -13.040 -17.483 1.00 40.97  ? 31  VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? 22.404  -14.517 -17.123 1.00 36.68  ? 31  VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? 21.149  -12.447 -16.542 1.00 34.07  ? 31  VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? 24.571  -12.809 -19.525 1.00 38.54  ? 32  GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? 25.491  -13.599 -20.340 1.00 42.65  ? 32  GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? 26.913  -13.060 -20.275 1.00 43.74  ? 32  GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? 27.875  -13.841 -20.304 1.00 43.52  ? 32  GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? 25.006  -13.660 -21.789 1.00 48.52  ? 32  GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? 24.072  -14.840 -22.030 1.00 51.05  ? 32  GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? 23.759  -15.081 -23.492 1.00 52.81  ? 32  GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? 23.672  -14.103 -24.268 1.00 48.05  ? 32  GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? 23.591  -16.264 -23.856 1.00 56.34  ? 32  GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? 27.068  -11.731 -20.227 1.00 43.83  ? 33  GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? 28.399  -11.156 -20.112 1.00 42.13  ? 33  GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? 29.097  -11.568 -18.830 1.00 41.58  ? 33  GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? 30.291  -11.881 -18.830 1.00 43.95  ? 33  GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? 28.359  -11.584 -17.721 1.00 39.83  ? 34  ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? 28.952  -12.012 -16.462 1.00 39.38  ? 34  ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? 29.063  -13.527 -16.353 1.00 41.06  ? 34  ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? 29.962  -14.024 -15.664 1.00 44.09  ? 34  ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? 28.153  -11.438 -15.300 1.00 40.34  ? 34  ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? 28.466  -10.002 -15.095 1.00 41.49  ? 34  ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? 29.598  -9.657  -14.744 1.00 45.11  ? 34  ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? 27.502  -9.137  -15.375 1.00 41.95  ? 34  ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? 28.181  -14.276 -17.019 1.00 39.80  ? 35  ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? 28.357  -15.724 -17.084 1.00 39.19  ? 35  ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? 29.662  -16.063 -17.786 1.00 44.90  ? 35  ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? 30.450  -16.879 -17.301 1.00 42.06  ? 35  ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? 27.171  -16.372 -17.797 1.00 38.72  ? 35  ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? 29.927  -15.408 -18.920 1.00 44.39  ? 36  GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? 31.188  -15.633 -19.622 1.00 46.46  ? 36  GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? 32.379  -15.266 -18.737 1.00 43.12  ? 36  GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? 33.401  -15.961 -18.741 1.00 44.52  ? 36  GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? 31.193  -14.835 -20.928 1.00 48.89  ? 36  GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? 32.254  -15.224 -21.928 1.00 64.14  ? 36  GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? 32.289  -14.249 -23.091 1.00 76.07  ? 36  GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? 31.639  -13.192 -23.046 1.00 74.36  ? 36  GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? 33.043  -14.592 -24.138 1.00 72.60  ? 36  GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? 32.239  -14.218 -17.921 1.00 44.15  ? 37  LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? 33.327  -13.783 -17.047 1.00 41.94  ? 37  LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? 33.500  -14.693 -15.830 1.00 44.31  ? 37  LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? 34.622  -15.102 -15.511 1.00 44.24  ? 37  LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? 33.083  -12.346 -16.589 1.00 43.24  ? 37  LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? 34.034  -11.831 -15.505 1.00 43.87  ? 37  LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? 35.351  -11.397 -16.107 1.00 49.84  ? 37  LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? 33.390  -10.699 -14.715 1.00 49.31  ? 37  LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? 32.404  -15.004 -15.128 1.00 41.21  ? 38  CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? 32.474  -15.729 -13.864 1.00 43.32  ? 38  CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? 32.452  -17.247 -14.029 1.00 43.13  ? 38  CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? 32.788  -17.962 -13.078 1.00 45.44  ? 38  CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? 31.314  -15.316 -12.952 1.00 36.95  ? 38  CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? 31.231  -13.558 -12.569 1.00 41.44  ? 38  CYS A SG    1 
ATOM   277  N  N     A GLN A 1 39  ? 32.053  -17.748 -15.195 0.50 42.20  ? 39  GLN A N     1 
ATOM   278  N  N     B GLN A 1 39  ? 32.038  -17.740 -15.194 0.50 42.13  ? 39  GLN A N     1 
ATOM   279  C  CA    A GLN A 1 39  ? 32.039  -19.173 -15.519 0.50 44.00  ? 39  GLN A CA    1 
ATOM   280  C  CA    B GLN A 1 39  ? 31.997  -19.153 -15.568 0.50 43.98  ? 39  GLN A CA    1 
ATOM   281  C  C     A GLN A 1 39  ? 31.200  -20.019 -14.561 0.50 43.31  ? 39  GLN A C     1 
ATOM   282  C  C     B GLN A 1 39  ? 31.193  -20.022 -14.599 0.50 43.37  ? 39  GLN A C     1 
ATOM   283  O  O     A GLN A 1 39  ? 31.716  -20.994 -13.997 0.50 43.39  ? 39  GLN A O     1 
ATOM   284  O  O     B GLN A 1 39  ? 31.724  -21.009 -14.070 0.50 43.42  ? 39  GLN A O     1 
ATOM   285  C  CB    A GLN A 1 39  ? 33.470  -19.717 -15.546 0.50 45.90  ? 39  GLN A CB    1 
ATOM   286  C  CB    B GLN A 1 39  ? 33.423  -19.688 -15.702 0.50 45.97  ? 39  GLN A CB    1 
ATOM   287  C  CG    A GLN A 1 39  ? 34.282  -19.274 -16.748 0.50 46.63  ? 39  GLN A CG    1 
ATOM   288  C  CG    B GLN A 1 39  ? 34.312  -18.824 -16.595 0.50 46.40  ? 39  GLN A CG    1 
ATOM   289  C  CD    A GLN A 1 39  ? 33.724  -19.816 -18.038 0.50 47.77  ? 39  GLN A CD    1 
ATOM   290  C  CD    B GLN A 1 39  ? 35.657  -19.460 -16.876 0.50 47.15  ? 39  GLN A CD    1 
ATOM   291  O  OE1   A GLN A 1 39  ? 33.443  -19.064 -18.969 0.50 48.34  ? 39  GLN A OE1   1 
ATOM   292  O  OE1   B GLN A 1 39  ? 35.735  -20.497 -17.522 0.50 51.27  ? 39  GLN A OE1   1 
ATOM   293  N  NE2   A GLN A 1 39  ? 33.567  -21.135 -18.108 0.50 52.39  ? 39  GLN A NE2   1 
ATOM   294  N  NE2   B GLN A 1 39  ? 36.724  -18.837 -16.390 0.50 48.53  ? 39  GLN A NE2   1 
ATOM   295  N  N     . PRO A 1 40  ? 29.917  -19.717 -14.358 1.00 40.60  ? 40  PRO A N     1 
ATOM   296  C  CA    . PRO A 1 40  ? 29.097  -20.607 -13.534 1.00 40.04  ? 40  PRO A CA    1 
ATOM   297  C  C     . PRO A 1 40  ? 28.838  -21.909 -14.278 1.00 43.35  ? 40  PRO A C     1 
ATOM   298  O  O     . PRO A 1 40  ? 28.909  -21.974 -15.508 1.00 40.82  ? 40  PRO A O     1 
ATOM   299  C  CB    . PRO A 1 40  ? 27.802  -19.808 -13.326 1.00 39.96  ? 40  PRO A CB    1 
ATOM   300  C  CG    . PRO A 1 40  ? 27.701  -18.978 -14.583 1.00 38.65  ? 40  PRO A CG    1 
ATOM   301  C  CD    . PRO A 1 40  ? 29.124  -18.578 -14.871 1.00 41.32  ? 40  PRO A CD    1 
ATOM   302  N  N     . GLU A 1 41  ? 28.567  -22.967 -13.516 1.00 40.64  ? 41  GLU A N     1 
ATOM   303  C  CA    . GLU A 1 41  ? 28.222  -24.234 -14.153 1.00 40.40  ? 41  GLU A CA    1 
ATOM   304  C  C     . GLU A 1 41  ? 26.776  -24.253 -14.641 1.00 41.15  ? 41  GLU A C     1 
ATOM   305  O  O     . GLU A 1 41  ? 26.475  -24.909 -15.643 1.00 44.68  ? 41  GLU A O     1 
ATOM   306  C  CB    . GLU A 1 41  ? 28.455  -25.395 -13.179 1.00 43.81  ? 41  GLU A CB    1 
ATOM   307  C  CG    . GLU A 1 41  ? 28.450  -26.781 -13.858 1.00 45.94  ? 41  GLU A CG    1 
ATOM   308  C  CD    . GLU A 1 41  ? 29.491  -26.887 -14.947 1.00 56.87  ? 41  GLU A CD    1 
ATOM   309  O  OE1   . GLU A 1 41  ? 30.536  -26.212 -14.830 1.00 58.13  ? 41  GLU A OE1   1 
ATOM   310  O  OE2   . GLU A 1 41  ? 29.270  -27.638 -15.925 1.00 64.83  ? 41  GLU A OE2   1 
ATOM   311  N  N     . TYR A 1 42  ? 25.879  -23.563 -13.937 1.00 38.08  ? 42  TYR A N     1 
ATOM   312  C  CA    . TYR A 1 42  ? 24.447  -23.549 -14.205 1.00 37.72  ? 42  TYR A CA    1 
ATOM   313  C  C     . TYR A 1 42  ? 23.951  -22.123 -14.075 1.00 37.61  ? 42  TYR A C     1 
ATOM   314  O  O     . TYR A 1 42  ? 24.523  -21.333 -13.327 1.00 38.35  ? 42  TYR A O     1 
ATOM   315  C  CB    . TYR A 1 42  ? 23.646  -24.401 -13.203 1.00 37.60  ? 42  TYR A CB    1 
ATOM   316  C  CG    . TYR A 1 42  ? 24.204  -25.779 -12.998 1.00 41.46  ? 42  TYR A CG    1 
ATOM   317  C  CD1   . TYR A 1 42  ? 23.932  -26.787 -13.896 1.00 42.23  ? 42  TYR A CD1   1 
ATOM   318  C  CD2   . TYR A 1 42  ? 25.000  -26.069 -11.897 1.00 45.57  ? 42  TYR A CD2   1 
ATOM   319  C  CE1   . TYR A 1 42  ? 24.441  -28.059 -13.715 1.00 46.49  ? 42  TYR A CE1   1 
ATOM   320  C  CE2   . TYR A 1 42  ? 25.514  -27.331 -11.705 1.00 46.14  ? 42  TYR A CE2   1 
ATOM   321  C  CZ    . TYR A 1 42  ? 25.228  -28.324 -12.614 1.00 44.70  ? 42  TYR A CZ    1 
ATOM   322  O  OH    . TYR A 1 42  ? 25.739  -29.595 -12.440 1.00 55.53  ? 42  TYR A OH    1 
ATOM   323  N  N     . ILE A 1 43  ? 22.857  -21.810 -14.770 1.00 38.34  ? 43  ILE A N     1 
ATOM   324  C  CA    . ILE A 1 43  ? 22.169  -20.533 -14.612 1.00 32.51  ? 43  ILE A CA    1 
ATOM   325  C  C     . ILE A 1 43  ? 20.717  -20.800 -14.229 1.00 35.12  ? 43  ILE A C     1 
ATOM   326  O  O     . ILE A 1 43  ? 20.002  -21.524 -14.932 1.00 34.19  ? 43  ILE A O     1 
ATOM   327  C  CB    . ILE A 1 43  ? 22.249  -19.672 -15.884 1.00 35.79  ? 43  ILE A CB    1 
ATOM   328  C  CG1   . ILE A 1 43  ? 23.706  -19.367 -16.204 1.00 35.71  ? 43  ILE A CG1   1 
ATOM   329  C  CG2   . ILE A 1 43  ? 21.472  -18.377 -15.687 1.00 33.84  ? 43  ILE A CG2   1 
ATOM   330  C  CD1   . ILE A 1 43  ? 23.909  -18.700 -17.539 1.00 42.84  ? 43  ILE A CD1   1 
ATOM   331  N  N     . HIS A 1 44  ? 20.284  -20.193 -13.130 1.00 29.48  ? 44  HIS A N     1 
ATOM   332  C  CA    . HIS A 1 44  ? 18.937  -20.357 -12.590 1.00 30.67  ? 44  HIS A CA    1 
ATOM   333  C  C     . HIS A 1 44  ? 18.288  -18.982 -12.576 1.00 31.05  ? 44  HIS A C     1 
ATOM   334  O  O     . HIS A 1 44  ? 18.707  -18.117 -11.802 1.00 29.95  ? 44  HIS A O     1 
ATOM   335  C  CB    . HIS A 1 44  ? 19.004  -20.946 -11.181 1.00 31.83  ? 44  HIS A CB    1 
ATOM   336  C  CG    . HIS A 1 44  ? 17.673  -21.100 -10.512 1.00 34.57  ? 44  HIS A CG    1 
ATOM   337  N  ND1   . HIS A 1 44  ? 17.150  -22.329 -10.172 1.00 34.95  ? 44  HIS A ND1   1 
ATOM   338  C  CD2   . HIS A 1 44  ? 16.766  -20.181 -10.106 1.00 32.11  ? 44  HIS A CD2   1 
ATOM   339  C  CE1   . HIS A 1 44  ? 15.974  -22.163 -9.596  1.00 35.07  ? 44  HIS A CE1   1 
ATOM   340  N  NE2   . HIS A 1 44  ? 15.722  -20.867 -9.539  1.00 34.47  ? 44  HIS A NE2   1 
ATOM   341  N  N     . ILE A 1 45  ? 17.275  -18.780 -13.416 1.00 32.15  ? 45  ILE A N     1 
ATOM   342  C  CA    . ILE A 1 45  ? 16.545  -17.515 -13.460 1.00 32.91  ? 45  ILE A CA    1 
ATOM   343  C  C     . ILE A 1 45  ? 15.379  -17.617 -12.487 1.00 34.32  ? 45  ILE A C     1 
ATOM   344  O  O     . ILE A 1 45  ? 14.432  -18.375 -12.718 1.00 34.53  ? 45  ILE A O     1 
ATOM   345  C  CB    . ILE A 1 45  ? 16.046  -17.188 -14.870 1.00 32.99  ? 45  ILE A CB    1 
ATOM   346  C  CG1   . ILE A 1 45  ? 17.215  -17.114 -15.857 1.00 36.68  ? 45  ILE A CG1   1 
ATOM   347  C  CG2   . ILE A 1 45  ? 15.287  -15.854 -14.843 1.00 33.77  ? 45  ILE A CG2   1 
ATOM   348  C  CD1   . ILE A 1 45  ? 16.777  -17.018 -17.286 1.00 40.66  ? 45  ILE A CD1   1 
ATOM   349  N  N     . CYS A 1 46  ? 15.432  -16.835 -11.414 1.00 32.52  ? 46  CYS A N     1 
ATOM   350  C  CA    . CYS A 1 46  ? 14.448  -16.970 -10.347 1.00 32.42  ? 46  CYS A CA    1 
ATOM   351  C  C     . CYS A 1 46  ? 13.068  -16.513 -10.793 1.00 34.62  ? 46  CYS A C     1 
ATOM   352  O  O     . CYS A 1 46  ? 12.923  -15.498 -11.479 1.00 34.36  ? 46  CYS A O     1 
ATOM   353  C  CB    . CYS A 1 46  ? 14.885  -16.169 -9.126  1.00 28.25  ? 46  CYS A CB    1 
ATOM   354  S  SG    . CYS A 1 46  ? 16.395  -16.805 -8.402  1.00 32.43  ? 46  CYS A SG    1 
ATOM   355  N  N     . ASP A 1 47  ? 12.044  -17.258 -10.378 1.00 36.51  ? 47  ASP A N     1 
ATOM   356  C  CA    . ASP A 1 47  ? 10.663  -16.850 -10.604 1.00 35.61  ? 47  ASP A CA    1 
ATOM   357  C  C     . ASP A 1 47  ? 9.942   -16.413 -9.336  1.00 34.59  ? 47  ASP A C     1 
ATOM   358  O  O     . ASP A 1 47  ? 8.799   -15.962 -9.429  1.00 37.25  ? 47  ASP A O     1 
ATOM   359  C  CB    . ASP A 1 47  ? 9.864   -17.969 -11.301 1.00 34.13  ? 47  ASP A CB    1 
ATOM   360  C  CG    . ASP A 1 47  ? 9.738   -19.257 -10.471 1.00 38.28  ? 47  ASP A CG    1 
ATOM   361  O  OD1   . ASP A 1 47  ? 9.967   -19.276 -9.247  1.00 40.49  ? 47  ASP A OD1   1 
ATOM   362  O  OD2   . ASP A 1 47  ? 9.394   -20.288 -11.076 1.00 41.79  ? 47  ASP A OD2   1 
ATOM   363  N  N     . GLY A 1 48  ? 10.565  -16.531 -8.161  1.00 33.23  ? 48  GLY A N     1 
ATOM   364  C  CA    . GLY A 1 48  ? 9.932   -16.081 -6.928  1.00 36.62  ? 48  GLY A CA    1 
ATOM   365  C  C     . GLY A 1 48  ? 8.849   -16.986 -6.372  1.00 41.32  ? 48  GLY A C     1 
ATOM   366  O  O     . GLY A 1 48  ? 8.186   -16.608 -5.390  1.00 38.23  ? 48  GLY A O     1 
ATOM   367  N  N     . SER A 1 49  ? 8.662   -18.174 -6.941  1.00 38.00  ? 49  SER A N     1 
ATOM   368  C  CA    . SER A 1 49  ? 7.524   -19.009 -6.583  1.00 42.38  ? 49  SER A CA    1 
ATOM   369  C  C     . SER A 1 49  ? 7.778   -19.782 -5.292  1.00 42.93  ? 49  SER A C     1 
ATOM   370  O  O     . SER A 1 49  ? 8.920   -19.998 -4.870  1.00 36.49  ? 49  SER A O     1 
ATOM   371  C  CB    . SER A 1 49  ? 7.220   -20.005 -7.700  1.00 41.21  ? 49  SER A CB    1 
ATOM   372  O  OG    . SER A 1 49  ? 8.249   -20.973 -7.753  1.00 44.24  ? 49  SER A OG    1 
ATOM   373  N  N     . GLU A 1 50  ? 6.678   -20.231 -4.681  1.00 46.59  ? 50  GLU A N     1 
ATOM   374  C  CA    . GLU A 1 50  ? 6.774   -21.064 -3.487  1.00 45.99  ? 50  GLU A CA    1 
ATOM   375  C  C     . GLU A 1 50  ? 7.508   -22.370 -3.773  1.00 44.76  ? 50  GLU A C     1 
ATOM   376  O  O     . GLU A 1 50  ? 8.302   -22.835 -2.947  1.00 43.89  ? 50  GLU A O     1 
ATOM   377  C  CB    . GLU A 1 50  ? 5.375   -21.354 -2.930  1.00 49.41  ? 50  GLU A CB    1 
ATOM   378  C  CG    . GLU A 1 50  ? 4.727   -20.160 -2.238  1.00 57.84  ? 50  GLU A CG    1 
ATOM   379  C  CD    . GLU A 1 50  ? 5.467   -19.737 -0.974  1.00 60.93  ? 50  GLU A CD    1 
ATOM   380  O  OE1   . GLU A 1 50  ? 6.271   -20.546 -0.457  1.00 62.31  ? 50  GLU A OE1   1 
ATOM   381  O  OE2   . GLU A 1 50  ? 5.241   -18.601 -0.494  1.00 64.56  ? 50  GLU A OE2   1 
ATOM   382  N  N     . GLU A 1 51  ? 7.241   -22.989 -4.926  1.00 44.88  ? 51  GLU A N     1 
ATOM   383  C  CA    . GLU A 1 51  ? 7.941   -24.224 -5.278  1.00 47.56  ? 51  GLU A CA    1 
ATOM   384  C  C     . GLU A 1 51  ? 9.443   -23.997 -5.319  1.00 48.67  ? 51  GLU A C     1 
ATOM   385  O  O     . GLU A 1 51  ? 10.219  -24.807 -4.804  1.00 43.77  ? 51  GLU A O     1 
ATOM   386  C  CB    . GLU A 1 51  ? 7.456   -24.757 -6.628  1.00 45.02  ? 51  GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 51  ? 6.014   -25.254 -6.657  1.00 56.15  ? 51  GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 51  ? 4.981   -24.135 -6.524  1.00 61.60  ? 51  GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 51  ? 5.318   -22.954 -6.795  1.00 52.85  ? 51  GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 51  ? 3.827   -24.447 -6.143  1.00 67.43  ? 51  GLU A OE2   1 
ATOM   391  N  N     . GLU A 1 52  ? 9.869   -22.881 -5.915  1.00 43.53  ? 52  GLU A N     1 
ATOM   392  C  CA    . GLU A 1 52  ? 11.291  -22.600 -6.037  1.00 41.00  ? 52  GLU A CA    1 
ATOM   393  C  C     . GLU A 1 52  ? 11.932  -22.395 -4.671  1.00 43.91  ? 52  GLU A C     1 
ATOM   394  O  O     . GLU A 1 52  ? 13.033  -22.892 -4.412  1.00 43.11  ? 52  GLU A O     1 
ATOM   395  C  CB    . GLU A 1 52  ? 11.484  -21.366 -6.910  1.00 41.16  ? 52  GLU A CB    1 
ATOM   396  C  CG    . GLU A 1 52  ? 12.836  -20.722 -6.767  1.00 35.76  ? 52  GLU A CG    1 
ATOM   397  C  CD    . GLU A 1 52  ? 12.957  -19.471 -7.607  1.00 39.75  ? 52  GLU A CD    1 
ATOM   398  O  OE1   . GLU A 1 52  ? 13.275  -19.575 -8.814  1.00 38.79  ? 52  GLU A OE1   1 
ATOM   399  O  OE2   . GLU A 1 52  ? 12.731  -18.387 -7.045  1.00 35.18  ? 52  GLU A OE2   1 
ATOM   400  N  N     . TYR A 1 53  ? 11.259  -21.649 -3.793  1.00 42.34  ? 53  TYR A N     1 
ATOM   401  C  CA    . TYR A 1 53  ? 11.750  -21.453 -2.432  1.00 41.68  ? 53  TYR A CA    1 
ATOM   402  C  C     . TYR A 1 53  ? 11.947  -22.791 -1.730  1.00 41.86  ? 53  TYR A C     1 
ATOM   403  O  O     . TYR A 1 53  ? 12.991  -23.033 -1.115  1.00 40.71  ? 53  TYR A O     1 
ATOM   404  C  CB    . TYR A 1 53  ? 10.759  -20.568 -1.670  1.00 42.17  ? 53  TYR A CB    1 
ATOM   405  C  CG    . TYR A 1 53  ? 11.227  -19.991 -0.354  1.00 41.75  ? 53  TYR A CG    1 
ATOM   406  C  CD1   . TYR A 1 53  ? 12.401  -19.263 -0.261  1.00 41.73  ? 53  TYR A CD1   1 
ATOM   407  C  CD2   . TYR A 1 53  ? 10.451  -20.132 0.794   1.00 48.06  ? 53  TYR A CD2   1 
ATOM   408  C  CE1   . TYR A 1 53  ? 12.808  -18.704 0.949   1.00 44.45  ? 53  TYR A CE1   1 
ATOM   409  C  CE2   . TYR A 1 53  ? 10.845  -19.590 1.997   1.00 47.56  ? 53  TYR A CE2   1 
ATOM   410  C  CZ    . TYR A 1 53  ? 12.024  -18.880 2.074   1.00 47.87  ? 53  TYR A CZ    1 
ATOM   411  O  OH    . TYR A 1 53  ? 12.405  -18.345 3.282   1.00 49.57  ? 53  TYR A OH    1 
ATOM   412  N  N     . GLY A 1 54  ? 10.962  -23.684 -1.842  1.00 42.93  ? 54  GLY A N     1 
ATOM   413  C  CA    . GLY A 1 54  ? 11.082  -24.990 -1.215  1.00 45.10  ? 54  GLY A CA    1 
ATOM   414  C  C     . GLY A 1 54  ? 12.286  -25.761 -1.716  1.00 50.52  ? 54  GLY A C     1 
ATOM   415  O  O     . GLY A 1 54  ? 13.008  -26.379 -0.928  1.00 49.12  ? 54  GLY A O     1 
ATOM   416  N  N     . ARG A 1 55  ? 12.530  -25.712 -3.033  1.00 51.30  ? 55  ARG A N     1 
ATOM   417  C  CA    . ARG A 1 55  ? 13.688  -26.380 -3.612  1.00 51.98  ? 55  ARG A CA    1 
ATOM   418  C  C     . ARG A 1 55  ? 14.995  -25.760 -3.124  1.00 54.89  ? 55  ARG A C     1 
ATOM   419  O  O     . ARG A 1 55  ? 15.947  -26.487 -2.814  1.00 57.00  ? 55  ARG A O     1 
ATOM   420  C  CB    . ARG A 1 55  ? 13.605  -26.348 -5.142  1.00 53.52  ? 55  ARG A CB    1 
ATOM   421  C  CG    . ARG A 1 55  ? 12.522  -27.245 -5.723  1.00 62.23  ? 55  ARG A CG    1 
ATOM   422  C  CD    . ARG A 1 55  ? 12.698  -28.679 -5.212  1.00 73.62  ? 55  ARG A CD    1 
ATOM   423  N  NE    . ARG A 1 55  ? 11.747  -29.635 -5.770  1.00 84.15  ? 55  ARG A NE    1 
ATOM   424  C  CZ    . ARG A 1 55  ? 11.643  -30.898 -5.372  1.00 89.76  ? 55  ARG A CZ    1 
ATOM   425  N  NH1   . ARG A 1 55  ? 12.408  -31.383 -4.407  1.00 92.22  ? 55  ARG A NH1   1 
ATOM   426  N  NH2   . ARG A 1 55  ? 10.748  -31.694 -5.955  1.00 86.63  ? 55  ARG A NH2   1 
ATOM   427  N  N     . LEU A 1 56  ? 15.065  -24.423 -3.047  1.00 42.71  ? 56  LEU A N     1 
ATOM   428  C  CA    . LEU A 1 56  ? 16.276  -23.775 -2.541  1.00 43.02  ? 56  LEU A CA    1 
ATOM   429  C  C     . LEU A 1 56  ? 16.551  -24.176 -1.099  1.00 43.80  ? 56  LEU A C     1 
ATOM   430  O  O     . LEU A 1 56  ? 17.695  -24.467 -0.733  1.00 46.66  ? 56  LEU A O     1 
ATOM   431  C  CB    . LEU A 1 56  ? 16.164  -22.252 -2.621  1.00 45.37  ? 56  LEU A CB    1 
ATOM   432  C  CG    . LEU A 1 56  ? 16.068  -21.385 -3.879  1.00 51.94  ? 56  LEU A CG    1 
ATOM   433  C  CD1   . LEU A 1 56  ? 15.297  -20.132 -3.503  1.00 43.09  ? 56  LEU A CD1   1 
ATOM   434  C  CD2   . LEU A 1 56  ? 17.430  -20.978 -4.414  1.00 47.13  ? 56  LEU A CD2   1 
ATOM   435  N  N     . LEU A 1 57  ? 15.515  -24.136 -0.255  1.00 41.26  ? 57  LEU A N     1 
ATOM   436  C  CA    . LEU A 1 57  ? 15.642  -24.535 1.145   1.00 45.74  ? 57  LEU A CA    1 
ATOM   437  C  C     . LEU A 1 57  ? 16.063  -25.995 1.262   1.00 47.42  ? 57  LEU A C     1 
ATOM   438  O  O     . LEU A 1 57  ? 16.998  -26.332 2.001   1.00 46.02  ? 57  LEU A O     1 
ATOM   439  C  CB    . LEU A 1 57  ? 14.309  -24.309 1.873   1.00 41.10  ? 57  LEU A CB    1 
ATOM   440  C  CG    . LEU A 1 57  ? 13.922  -22.842 2.084   1.00 44.21  ? 57  LEU A CG    1 
ATOM   441  C  CD1   . LEU A 1 57  ? 12.491  -22.751 2.572   1.00 47.40  ? 57  LEU A CD1   1 
ATOM   442  C  CD2   . LEU A 1 57  ? 14.862  -22.185 3.076   1.00 42.65  ? 57  LEU A CD2   1 
ATOM   443  N  N     . ALA A 1 58  ? 15.366  -26.880 0.553   1.00 47.50  ? 58  ALA A N     1 
ATOM   444  C  CA    . ALA A 1 58  ? 15.750  -28.290 0.550   1.00 48.45  ? 58  ALA A CA    1 
ATOM   445  C  C     . ALA A 1 58  ? 17.201  -28.459 0.112   1.00 48.09  ? 58  ALA A C     1 
ATOM   446  O  O     . ALA A 1 58  ? 17.976  -29.164 0.766   1.00 49.22  ? 58  ALA A O     1 
ATOM   447  C  CB    . ALA A 1 58  ? 14.808  -29.090 -0.350  1.00 50.87  ? 58  ALA A CB    1 
ATOM   448  N  N     . HIS A 1 59  ? 17.594  -27.784 -0.975  1.00 46.65  ? 59  HIS A N     1 
ATOM   449  C  CA    . HIS A 1 59  ? 18.982  -27.812 -1.434  1.00 48.15  ? 59  HIS A CA    1 
ATOM   450  C  C     . HIS A 1 59  ? 19.951  -27.423 -0.323  1.00 53.31  ? 59  HIS A C     1 
ATOM   451  O  O     . HIS A 1 59  ? 20.893  -28.167 -0.009  1.00 51.01  ? 59  HIS A O     1 
ATOM   452  C  CB    . HIS A 1 59  ? 19.160  -26.874 -2.630  1.00 49.18  ? 59  HIS A CB    1 
ATOM   453  C  CG    . HIS A 1 59  ? 20.586  -26.714 -3.067  1.00 52.36  ? 59  HIS A CG    1 
ATOM   454  N  ND1   . HIS A 1 59  ? 21.199  -25.482 -3.188  1.00 56.82  ? 59  HIS A ND1   1 
ATOM   455  C  CD2   . HIS A 1 59  ? 21.521  -27.634 -3.406  1.00 51.94  ? 59  HIS A CD2   1 
ATOM   456  C  CE1   . HIS A 1 59  ? 22.448  -25.652 -3.588  1.00 55.04  ? 59  HIS A CE1   1 
ATOM   457  N  NE2   . HIS A 1 59  ? 22.667  -26.949 -3.725  1.00 55.84  ? 59  HIS A NE2   1 
ATOM   458  N  N     . MET A 1 60  ? 19.727  -26.243 0.280   1.00 47.35  ? 60  MET A N     1 
ATOM   459  C  CA    . MET A 1 60  ? 20.637  -25.721 1.295   1.00 47.50  ? 60  MET A CA    1 
ATOM   460  C  C     . MET A 1 60  ? 20.709  -26.631 2.502   1.00 46.52  ? 60  MET A C     1 
ATOM   461  O  O     . MET A 1 60  ? 21.755  -26.710 3.151   1.00 50.27  ? 60  MET A O     1 
ATOM   462  C  CB    . MET A 1 60  ? 20.204  -24.319 1.737   1.00 42.10  ? 60  MET A CB    1 
ATOM   463  C  CG    . MET A 1 60  ? 20.586  -23.231 0.770   1.00 45.11  ? 60  MET A CG    1 
ATOM   464  S  SD    . MET A 1 60  ? 20.271  -21.618 1.480   1.00 44.83  ? 60  MET A SD    1 
ATOM   465  C  CE    . MET A 1 60  ? 18.506  -21.476 1.241   1.00 38.42  ? 60  MET A CE    1 
ATOM   466  N  N     . GLN A 1 61  ? 19.605  -27.306 2.827   1.00 46.65  ? 61  GLN A N     1 
ATOM   467  C  CA    . GLN A 1 61  ? 19.602  -28.235 3.950   1.00 49.77  ? 61  GLN A CA    1 
ATOM   468  C  C     . GLN A 1 61  ? 20.419  -29.475 3.632   1.00 55.02  ? 61  GLN A C     1 
ATOM   469  O  O     . GLN A 1 61  ? 21.032  -30.064 4.533   1.00 49.02  ? 61  GLN A O     1 
ATOM   470  C  CB    . GLN A 1 61  ? 18.168  -28.623 4.306   1.00 50.49  ? 61  GLN A CB    1 
ATOM   471  C  CG    . GLN A 1 61  ? 18.005  -29.348 5.639   1.00 49.34  ? 61  GLN A CG    1 
ATOM   472  C  CD    . GLN A 1 61  ? 16.546  -29.642 5.944   1.00 57.39  ? 61  GLN A CD    1 
ATOM   473  O  OE1   . GLN A 1 61  ? 15.705  -29.635 5.044   1.00 60.24  ? 61  GLN A OE1   1 
ATOM   474  N  NE2   . GLN A 1 61  ? 16.235  -29.893 7.217   1.00 60.89  ? 61  GLN A NE2   1 
ATOM   475  N  N     . GLU A 1 62  ? 20.438  -29.879 2.360   1.00 53.72  ? 62  GLU A N     1 
ATOM   476  C  CA    . GLU A 1 62  ? 21.204  -31.045 1.942   1.00 60.36  ? 62  GLU A CA    1 
ATOM   477  C  C     . GLU A 1 62  ? 22.695  -30.748 1.863   1.00 59.46  ? 62  GLU A C     1 
ATOM   478  O  O     . GLU A 1 62  ? 23.502  -31.678 1.965   1.00 61.12  ? 62  GLU A O     1 
ATOM   479  C  CB    . GLU A 1 62  ? 20.684  -31.563 0.591   1.00 58.44  ? 62  GLU A CB    1 
ATOM   480  C  CG    . GLU A 1 62  ? 19.221  -32.045 0.626   1.00 55.31  ? 62  GLU A CG    1 
ATOM   481  C  CD    . GLU A 1 62  ? 18.616  -32.267 -0.763  1.00 51.09  ? 62  GLU A CD    1 
ATOM   482  O  OE1   . GLU A 1 62  ? 19.342  -32.132 -1.773  1.00 49.14  ? 62  GLU A OE1   1 
ATOM   483  O  OE2   . GLU A 1 62  ? 17.405  -32.577 -0.841  1.00 52.40  ? 62  GLU A OE2   1 
ATOM   484  N  N     . GLU A 1 63  ? 23.073  -29.478 1.706   1.00 55.44  ? 63  GLU A N     1 
ATOM   485  C  CA    . GLU A 1 63  ? 24.473  -29.073 1.664   1.00 58.67  ? 63  GLU A CA    1 
ATOM   486  C  C     . GLU A 1 63  ? 25.004  -28.627 3.022   1.00 61.74  ? 63  GLU A C     1 
ATOM   487  O  O     . GLU A 1 63  ? 26.111  -28.081 3.090   1.00 64.15  ? 63  GLU A O     1 
ATOM   488  C  CB    . GLU A 1 63  ? 24.666  -27.934 0.660   1.00 56.07  ? 63  GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 63  ? 24.100  -28.204 -0.723  1.00 60.88  ? 63  GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 63  ? 25.033  -29.021 -1.600  1.00 65.65  ? 63  GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 63  ? 26.047  -29.533 -1.082  1.00 66.03  ? 63  GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 63  ? 24.752  -29.142 -2.813  1.00 68.08  ? 63  GLU A OE2   1 
ATOM   493  N  N     . GLY A 1 64  ? 24.232  -28.811 4.092   1.00 57.23  ? 64  GLY A N     1 
ATOM   494  C  CA    . GLY A 1 64  ? 24.643  -28.350 5.404   1.00 55.17  ? 64  GLY A CA    1 
ATOM   495  C  C     . GLY A 1 64  ? 24.708  -26.849 5.586   1.00 55.65  ? 64  GLY A C     1 
ATOM   496  O  O     . GLY A 1 64  ? 25.373  -26.379 6.512   1.00 60.80  ? 64  GLY A O     1 
ATOM   497  N  N     . VAL A 1 65  ? 24.030  -26.071 4.747   1.00 52.45  ? 65  VAL A N     1 
ATOM   498  C  CA    . VAL A 1 65  ? 24.105  -24.620 4.878   1.00 52.66  ? 65  VAL A CA    1 
ATOM   499  C  C     . VAL A 1 65  ? 23.095  -24.093 5.894   1.00 51.79  ? 65  VAL A C     1 
ATOM   500  O  O     . VAL A 1 65  ? 23.385  -23.141 6.628   1.00 48.86  ? 65  VAL A O     1 
ATOM   501  C  CB    . VAL A 1 65  ? 23.927  -23.947 3.501   1.00 52.90  ? 65  VAL A CB    1 
ATOM   502  C  CG1   . VAL A 1 65  ? 24.156  -22.474 3.624   1.00 47.64  ? 65  VAL A CG1   1 
ATOM   503  C  CG2   . VAL A 1 65  ? 24.898  -24.538 2.494   1.00 56.98  ? 65  VAL A CG2   1 
ATOM   504  N  N     . ILE A 1 66  ? 21.891  -24.668 5.955   1.00 49.30  ? 66  ILE A N     1 
ATOM   505  C  CA    . ILE A 1 66  ? 20.908  -24.280 6.956   1.00 42.18  ? 66  ILE A CA    1 
ATOM   506  C  C     . ILE A 1 66  ? 20.365  -25.523 7.636   1.00 47.63  ? 66  ILE A C     1 
ATOM   507  O  O     . ILE A 1 66  ? 20.511  -26.645 7.151   1.00 41.18  ? 66  ILE A O     1 
ATOM   508  C  CB    . ILE A 1 66  ? 19.736  -23.447 6.388   1.00 45.96  ? 66  ILE A CB    1 
ATOM   509  C  CG1   . ILE A 1 66  ? 19.008  -24.187 5.264   1.00 44.56  ? 66  ILE A CG1   1 
ATOM   510  C  CG2   . ILE A 1 66  ? 20.195  -22.065 5.957   1.00 47.02  ? 66  ILE A CG2   1 
ATOM   511  C  CD1   . ILE A 1 66  ? 18.096  -23.251 4.455   1.00 48.15  ? 66  ILE A CD1   1 
ATOM   512  N  N     . ARG A 1 67  ? 19.721  -25.285 8.774   1.00 44.95  ? 67  ARG A N     1 
ATOM   513  C  CA    . ARG A 1 67  ? 19.038  -26.286 9.573   1.00 42.49  ? 67  ARG A CA    1 
ATOM   514  C  C     . ARG A 1 67  ? 17.582  -25.878 9.741   1.00 44.28  ? 67  ARG A C     1 
ATOM   515  O  O     . ARG A 1 67  ? 17.279  -24.689 9.880   1.00 40.03  ? 67  ARG A O     1 
ATOM   516  C  CB    . ARG A 1 67  ? 19.681  -26.408 10.961  1.00 52.42  ? 67  ARG A CB    1 
ATOM   517  C  CG    . ARG A 1 67  ? 20.914  -27.285 11.014  1.00 57.22  ? 67  ARG A CG    1 
ATOM   518  C  CD    . ARG A 1 67  ? 21.484  -27.351 12.428  1.00 61.63  ? 67  ARG A CD    1 
ATOM   519  N  NE    . ARG A 1 67  ? 20.538  -27.890 13.402  1.00 65.28  ? 67  ARG A NE    1 
ATOM   520  C  CZ    . ARG A 1 67  ? 20.288  -29.182 13.577  1.00 69.00  ? 67  ARG A CZ    1 
ATOM   521  N  NH1   . ARG A 1 67  ? 20.855  -30.106 12.817  1.00 69.04  ? 67  ARG A NH1   1 
ATOM   522  N  NH2   . ARG A 1 67  ? 19.448  -29.558 14.540  1.00 70.09  ? 67  ARG A NH2   1 
ATOM   523  N  N     . LYS A 1 68  ? 16.678  -26.854 9.735   1.00 42.80  ? 68  LYS A N     1 
ATOM   524  C  CA    . LYS A 1 68  ? 15.288  -26.570 10.066  1.00 47.98  ? 68  LYS A CA    1 
ATOM   525  C  C     . LYS A 1 68  ? 15.140  -26.404 11.569  1.00 47.68  ? 68  LYS A C     1 
ATOM   526  O  O     . LYS A 1 68  ? 15.705  -27.174 12.345  1.00 48.55  ? 68  LYS A O     1 
ATOM   527  C  CB    . LYS A 1 68  ? 14.359  -27.683 9.580   1.00 50.81  ? 68  LYS A CB    1 
ATOM   528  C  CG    . LYS A 1 68  ? 12.896  -27.257 9.549   1.00 50.84  ? 68  LYS A CG    1 
ATOM   529  C  CD    . LYS A 1 68  ? 12.065  -28.195 8.686   1.00 57.12  ? 68  LYS A CD    1 
ATOM   530  C  CE    . LYS A 1 68  ? 10.769  -27.523 8.234   1.00 58.62  ? 68  LYS A CE    1 
ATOM   531  N  NZ    . LYS A 1 68  ? 9.836   -27.249 9.370   1.00 62.00  ? 68  LYS A NZ    1 
ATOM   532  N  N     . LEU A 1 69  ? 14.392  -25.382 11.978  1.00 43.65  ? 69  LEU A N     1 
ATOM   533  C  CA    . LEU A 1 69  ? 14.036  -25.199 13.386  1.00 46.25  ? 69  LEU A CA    1 
ATOM   534  C  C     . LEU A 1 69  ? 12.663  -25.832 13.598  1.00 49.54  ? 69  LEU A C     1 
ATOM   535  O  O     . LEU A 1 69  ? 11.628  -25.212 13.342  1.00 48.61  ? 69  LEU A O     1 
ATOM   536  C  CB    . LEU A 1 69  ? 14.069  -23.718 13.757  1.00 43.79  ? 69  LEU A CB    1 
ATOM   537  C  CG    . LEU A 1 69  ? 15.480  -23.121 13.659  1.00 41.34  ? 69  LEU A CG    1 
ATOM   538  C  CD1   . LEU A 1 69  ? 15.466  -21.603 13.494  1.00 37.92  ? 69  LEU A CD1   1 
ATOM   539  C  CD2   . LEU A 1 69  ? 16.301  -23.535 14.880  1.00 45.20  ? 69  LEU A CD2   1 
ATOM   540  N  N     . LYS A 1 70  ? 12.658  -27.081 14.073  1.00 49.50  ? 70  LYS A N     1 
ATOM   541  C  CA    . LYS A 1 70  ? 11.444  -27.890 14.059  1.00 53.87  ? 70  LYS A CA    1 
ATOM   542  C  C     . LYS A 1 70  ? 10.375  -27.377 15.017  1.00 51.58  ? 70  LYS A C     1 
ATOM   543  O  O     . LYS A 1 70  ? 9.210   -27.766 14.889  1.00 52.91  ? 70  LYS A O     1 
ATOM   544  C  CB    . LYS A 1 70  ? 11.787  -29.350 14.371  1.00 57.51  ? 70  LYS A CB    1 
ATOM   545  C  CG    . LYS A 1 70  ? 12.898  -29.560 15.404  1.00 59.15  ? 70  LYS A CG    1 
ATOM   546  C  CD    . LYS A 1 70  ? 13.180  -31.055 15.606  1.00 71.43  ? 70  LYS A CD    1 
ATOM   547  C  CE    . LYS A 1 70  ? 14.080  -31.330 16.818  1.00 72.17  ? 70  LYS A CE    1 
ATOM   548  N  NZ    . LYS A 1 70  ? 15.432  -30.708 16.665  1.00 68.29  ? 70  LYS A NZ    1 
ATOM   549  N  N     . LYS A 1 71  ? 10.735  -26.496 15.954  1.00 53.22  ? 71  LYS A N     1 
ATOM   550  C  CA    . LYS A 1 71  ? 9.762   -25.983 16.916  1.00 51.98  ? 71  LYS A CA    1 
ATOM   551  C  C     . LYS A 1 71  ? 8.776   -25.012 16.268  1.00 54.57  ? 71  LYS A C     1 
ATOM   552  O  O     . LYS A 1 71  ? 7.636   -24.892 16.732  1.00 52.48  ? 71  LYS A O     1 
ATOM   553  C  CB    . LYS A 1 71  ? 10.504  -25.299 18.064  1.00 52.92  ? 71  LYS A CB    1 
ATOM   554  C  CG    . LYS A 1 71  ? 9.684   -24.986 19.298  1.00 55.89  ? 71  LYS A CG    1 
ATOM   555  C  CD    . LYS A 1 71  ? 10.634  -24.613 20.423  1.00 57.26  ? 71  LYS A CD    1 
ATOM   556  C  CE    . LYS A 1 71  ? 9.903   -24.184 21.658  1.00 60.31  ? 71  LYS A CE    1 
ATOM   557  N  NZ    . LYS A 1 71  ? 10.549  -24.734 22.889  1.00 68.38  ? 71  LYS A NZ    1 
ATOM   558  N  N     . TYR A 1 72  ? 9.191   -24.315 15.210  1.00 49.13  ? 72  TYR A N     1 
ATOM   559  C  CA    . TYR A 1 72  ? 8.406   -23.264 14.570  1.00 53.09  ? 72  TYR A CA    1 
ATOM   560  C  C     . TYR A 1 72  ? 7.980   -23.713 13.177  1.00 51.67  ? 72  TYR A C     1 
ATOM   561  O  O     . TYR A 1 72  ? 8.352   -24.785 12.697  1.00 53.81  ? 72  TYR A O     1 
ATOM   562  C  CB    . TYR A 1 72  ? 9.193   -21.939 14.511  1.00 45.89  ? 72  TYR A CB    1 
ATOM   563  C  CG    . TYR A 1 72  ? 9.847   -21.607 15.834  1.00 48.67  ? 72  TYR A CG    1 
ATOM   564  C  CD1   . TYR A 1 72  ? 9.085   -21.416 16.974  1.00 48.14  ? 72  TYR A CD1   1 
ATOM   565  C  CD2   . TYR A 1 72  ? 11.231  -21.531 15.947  1.00 49.18  ? 72  TYR A CD2   1 
ATOM   566  C  CE1   . TYR A 1 72  ? 9.672   -21.152 18.193  1.00 49.79  ? 72  TYR A CE1   1 
ATOM   567  C  CE2   . TYR A 1 72  ? 11.826  -21.263 17.159  1.00 46.07  ? 72  TYR A CE2   1 
ATOM   568  C  CZ    . TYR A 1 72  ? 11.045  -21.078 18.274  1.00 48.73  ? 72  TYR A CZ    1 
ATOM   569  O  OH    . TYR A 1 72  ? 11.644  -20.806 19.479  1.00 50.63  ? 72  TYR A OH    1 
ATOM   570  N  N     . ASP A 1 73  ? 7.205   -22.860 12.521  1.00 48.70  ? 73  ASP A N     1 
ATOM   571  C  CA    . ASP A 1 73  ? 6.585   -23.164 11.239  1.00 52.28  ? 73  ASP A CA    1 
ATOM   572  C  C     . ASP A 1 73  ? 7.446   -22.566 10.134  1.00 47.79  ? 73  ASP A C     1 
ATOM   573  O  O     . ASP A 1 73  ? 7.498   -21.340 9.972   1.00 48.36  ? 73  ASP A O     1 
ATOM   574  C  CB    . ASP A 1 73  ? 5.152   -22.624 11.225  1.00 60.52  ? 73  ASP A CB    1 
ATOM   575  C  CG    . ASP A 1 73  ? 4.539   -22.558 9.828   1.00 64.91  ? 73  ASP A CG    1 
ATOM   576  O  OD1   . ASP A 1 73  ? 5.011   -23.252 8.906   1.00 65.94  ? 73  ASP A OD1   1 
ATOM   577  O  OD2   . ASP A 1 73  ? 3.561   -21.794 9.657   1.00 70.18  ? 73  ASP A OD2   1 
ATOM   578  N  N     . ASN A 1 74  ? 8.143   -23.428 9.387   1.00 46.52  ? 74  ASN A N     1 
ATOM   579  C  CA    . ASN A 1 74  ? 8.965   -23.000 8.245   1.00 48.12  ? 74  ASN A CA    1 
ATOM   580  C  C     . ASN A 1 74  ? 10.017  -21.951 8.634   1.00 42.92  ? 74  ASN A C     1 
ATOM   581  O  O     . ASN A 1 74  ? 10.207  -20.933 7.954   1.00 43.60  ? 74  ASN A O     1 
ATOM   582  C  CB    . ASN A 1 74  ? 8.071   -22.486 7.113   1.00 45.47  ? 74  ASN A CB    1 
ATOM   583  C  CG    . ASN A 1 74  ? 8.827   -22.276 5.814   1.00 49.58  ? 74  ASN A CG    1 
ATOM   584  O  OD1   . ASN A 1 74  ? 9.851   -22.917 5.557   1.00 49.93  ? 74  ASN A OD1   1 
ATOM   585  N  ND2   . ASN A 1 74  ? 8.337   -21.353 4.993   1.00 51.76  ? 74  ASN A ND2   1 
ATOM   586  N  N     . CYS A 1 75  ? 10.737  -22.206 9.725   1.00 39.95  ? 75  CYS A N     1 
ATOM   587  C  CA    . CYS A 1 75  ? 11.859  -21.353 10.108  1.00 40.67  ? 75  CYS A CA    1 
ATOM   588  C  C     . CYS A 1 75  ? 13.165  -22.135 10.015  1.00 42.04  ? 75  CYS A C     1 
ATOM   589  O  O     . CYS A 1 75  ? 13.185  -23.354 10.200  1.00 40.97  ? 75  CYS A O     1 
ATOM   590  C  CB    . CYS A 1 75  ? 11.688  -20.790 11.527  1.00 42.80  ? 75  CYS A CB    1 
ATOM   591  S  SG    . CYS A 1 75  ? 10.243  -19.708 11.777  1.00 43.77  ? 75  CYS A SG    1 
ATOM   592  N  N     . TRP A 1 76  ? 14.257  -21.420 9.724   1.00 36.41  ? 76  TRP A N     1 
ATOM   593  C  CA    . TRP A 1 76  ? 15.538  -22.026 9.381   1.00 40.77  ? 76  TRP A CA    1 
ATOM   594  C  C     . TRP A 1 76  ? 16.676  -21.263 10.044  1.00 39.64  ? 76  TRP A C     1 
ATOM   595  O  O     . TRP A 1 76  ? 16.575  -20.057 10.271  1.00 39.08  ? 76  TRP A O     1 
ATOM   596  C  CB    . TRP A 1 76  ? 15.742  -22.034 7.853   1.00 39.59  ? 76  TRP A CB    1 
ATOM   597  C  CG    . TRP A 1 76  ? 14.624  -22.721 7.154   1.00 41.96  ? 76  TRP A CG    1 
ATOM   598  C  CD1   . TRP A 1 76  ? 13.416  -22.186 6.805   1.00 41.12  ? 76  TRP A CD1   1 
ATOM   599  C  CD2   . TRP A 1 76  ? 14.584  -24.097 6.764   1.00 44.10  ? 76  TRP A CD2   1 
ATOM   600  N  NE1   . TRP A 1 76  ? 12.629  -23.147 6.209   1.00 42.92  ? 76  TRP A NE1   1 
ATOM   601  C  CE2   . TRP A 1 76  ? 13.328  -24.326 6.166   1.00 44.79  ? 76  TRP A CE2   1 
ATOM   602  C  CE3   . TRP A 1 76  ? 15.494  -25.153 6.850   1.00 44.03  ? 76  TRP A CE3   1 
ATOM   603  C  CZ2   . TRP A 1 76  ? 12.962  -25.575 5.657   1.00 48.43  ? 76  TRP A CZ2   1 
ATOM   604  C  CZ3   . TRP A 1 76  ? 15.130  -26.386 6.337   1.00 47.79  ? 76  TRP A CZ3   1 
ATOM   605  C  CH2   . TRP A 1 76  ? 13.872  -26.587 5.755   1.00 45.26  ? 76  TRP A CH2   1 
ATOM   606  N  N     . LEU A 1 77  ? 17.763  -21.972 10.347  1.00 38.83  ? 77  LEU A N     1 
ATOM   607  C  CA    . LEU A 1 77  ? 18.949  -21.378 10.957  1.00 38.22  ? 77  LEU A CA    1 
ATOM   608  C  C     . LEU A 1 77  ? 20.173  -21.561 10.060  1.00 41.13  ? 77  LEU A C     1 
ATOM   609  O  O     . LEU A 1 77  ? 20.454  -22.669 9.592   1.00 41.21  ? 77  LEU A O     1 
ATOM   610  C  CB    . LEU A 1 77  ? 19.218  -21.994 12.337  1.00 35.95  ? 77  LEU A CB    1 
ATOM   611  C  CG    . LEU A 1 77  ? 20.476  -21.514 13.079  1.00 39.69  ? 77  LEU A CG    1 
ATOM   612  C  CD1   . LEU A 1 77  ? 20.354  -20.056 13.489  1.00 39.74  ? 77  LEU A CD1   1 
ATOM   613  C  CD2   . LEU A 1 77  ? 20.768  -22.377 14.313  1.00 41.99  ? 77  LEU A CD2   1 
ATOM   614  N  N     . ALA A 1 78  ? 20.904  -20.475 9.843   1.00 39.24  ? 78  ALA A N     1 
ATOM   615  C  CA    . ALA A 1 78  ? 22.179  -20.481 9.141   1.00 40.25  ? 78  ALA A CA    1 
ATOM   616  C  C     . ALA A 1 78  ? 23.259  -19.964 10.079  1.00 41.83  ? 78  ALA A C     1 
ATOM   617  O  O     . ALA A 1 78  ? 23.058  -18.948 10.756  1.00 42.03  ? 78  ALA A O     1 
ATOM   618  C  CB    . ALA A 1 78  ? 22.116  -19.609 7.884   1.00 38.33  ? 78  ALA A CB    1 
ATOM   619  N  N     . LEU A 1 79  ? 24.401  -20.649 10.103  1.00 43.05  ? 79  LEU A N     1 
ATOM   620  C  CA    . LEU A 1 79  ? 25.566  -20.267 10.895  1.00 43.11  ? 79  LEU A CA    1 
ATOM   621  C  C     . LEU A 1 79  ? 26.715  -19.914 9.956   1.00 47.38  ? 79  LEU A C     1 
ATOM   622  O  O     . LEU A 1 79  ? 27.017  -20.681 9.039   1.00 49.21  ? 79  LEU A O     1 
ATOM   623  C  CB    . LEU A 1 79  ? 25.987  -21.410 11.821  1.00 47.17  ? 79  LEU A CB    1 
ATOM   624  C  CG    . LEU A 1 79  ? 24.952  -21.879 12.846  1.00 46.91  ? 79  LEU A CG    1 
ATOM   625  C  CD1   . LEU A 1 79  ? 25.532  -22.990 13.715  1.00 49.97  ? 79  LEU A CD1   1 
ATOM   626  C  CD2   . LEU A 1 79  ? 24.464  -20.706 13.700  1.00 45.20  ? 79  LEU A CD2   1 
ATOM   627  N  N     . THR A 1 80  ? 27.367  -18.777 10.192  1.00 44.78  ? 80  THR A N     1 
ATOM   628  C  CA    . THR A 1 80  ? 28.382  -18.280 9.273   1.00 43.66  ? 80  THR A CA    1 
ATOM   629  C  C     . THR A 1 80  ? 29.795  -18.500 9.808   1.00 46.09  ? 80  THR A C     1 
ATOM   630  O  O     . THR A 1 80  ? 30.020  -18.807 10.983  1.00 46.58  ? 80  THR A O     1 
ATOM   631  C  CB    . THR A 1 80  ? 28.171  -16.785 8.978   1.00 45.99  ? 80  THR A CB    1 
ATOM   632  O  OG1   . THR A 1 80  ? 28.572  -15.994 10.112  1.00 42.57  ? 80  THR A OG1   1 
ATOM   633  C  CG2   . THR A 1 80  ? 26.708  -16.507 8.649   1.00 43.84  ? 80  THR A CG2   1 
ATOM   634  N  N     . ASP A 1 81  ? 30.754  -18.354 8.900   1.00 48.41  ? 81  ASP A N     1 
ATOM   635  C  CA    . ASP A 1 81  ? 32.142  -18.149 9.279   1.00 48.47  ? 81  ASP A CA    1 
ATOM   636  C  C     . ASP A 1 81  ? 32.222  -16.948 10.218  1.00 45.38  ? 81  ASP A C     1 
ATOM   637  O  O     . ASP A 1 81  ? 31.601  -15.912 9.940   1.00 45.03  ? 81  ASP A O     1 
ATOM   638  C  CB    . ASP A 1 81  ? 32.979  -17.912 8.016   1.00 51.45  ? 81  ASP A CB    1 
ATOM   639  C  CG    . ASP A 1 81  ? 34.479  -17.981 8.265   1.00 53.03  ? 81  ASP A CG    1 
ATOM   640  O  OD1   . ASP A 1 81  ? 35.010  -17.163 9.049   1.00 52.23  ? 81  ASP A OD1   1 
ATOM   641  O  OD2   . ASP A 1 81  ? 35.128  -18.853 7.653   1.00 55.39  ? 81  ASP A OD2   1 
ATOM   642  N  N     . PRO A 1 82  ? 32.936  -17.048 11.342  1.00 44.31  ? 82  PRO A N     1 
ATOM   643  C  CA    . PRO A 1 82  ? 32.984  -15.910 12.281  1.00 48.55  ? 82  PRO A CA    1 
ATOM   644  C  C     . PRO A 1 82  ? 33.657  -14.655 11.720  1.00 49.27  ? 82  PRO A C     1 
ATOM   645  O  O     . PRO A 1 82  ? 33.562  -13.589 12.345  1.00 51.29  ? 82  PRO A O     1 
ATOM   646  C  CB    . PRO A 1 82  ? 33.754  -16.471 13.487  1.00 50.49  ? 82  PRO A CB    1 
ATOM   647  C  CG    . PRO A 1 82  ? 34.421  -17.721 12.994  1.00 51.27  ? 82  PRO A CG    1 
ATOM   648  C  CD    . PRO A 1 82  ? 33.587  -18.252 11.876  1.00 49.26  ? 82  PRO A CD    1 
ATOM   649  N  N     . ARG A 1 83  ? 34.324  -14.735 10.572  1.00 48.64  ? 83  ARG A N     1 
ATOM   650  C  CA    . ARG A 1 83  ? 34.875  -13.546 9.934   1.00 48.56  ? 83  ARG A CA    1 
ATOM   651  C  C     . ARG A 1 83  ? 33.862  -12.822 9.057   1.00 48.28  ? 83  ARG A C     1 
ATOM   652  O  O     . ARG A 1 83  ? 34.148  -11.722 8.571   1.00 48.63  ? 83  ARG A O     1 
ATOM   653  C  CB    . ARG A 1 83  ? 36.103  -13.936 9.112   1.00 46.73  ? 83  ARG A CB    1 
ATOM   654  C  CG    . ARG A 1 83  ? 37.237  -14.444 9.979   1.00 51.61  ? 83  ARG A CG    1 
ATOM   655  C  CD    . ARG A 1 83  ? 38.283  -15.171 9.160   1.00 56.37  ? 83  ARG A CD    1 
ATOM   656  N  NE    . ARG A 1 83  ? 37.692  -16.226 8.346   1.00 58.76  ? 83  ARG A NE    1 
ATOM   657  C  CZ    . ARG A 1 83  ? 38.386  -17.009 7.531   1.00 62.81  ? 83  ARG A CZ    1 
ATOM   658  N  NH1   . ARG A 1 83  ? 39.699  -16.892 7.415   1.00 63.60  ? 83  ARG A NH1   1 
ATOM   659  N  NH2   . ARG A 1 83  ? 37.748  -17.929 6.813   1.00 58.59  ? 83  ARG A NH2   1 
ATOM   660  N  N     . ASP A 1 84  ? 32.680  -13.392 8.871   1.00 47.22  ? 84  ASP A N     1 
ATOM   661  C  CA    . ASP A 1 84  ? 31.691  -12.885 7.932   1.00 45.97  ? 84  ASP A CA    1 
ATOM   662  C  C     . ASP A 1 84  ? 30.386  -12.648 8.704   1.00 46.47  ? 84  ASP A C     1 
ATOM   663  O  O     . ASP A 1 84  ? 29.401  -13.369 8.516   1.00 44.55  ? 84  ASP A O     1 
ATOM   664  C  CB    . ASP A 1 84  ? 31.512  -13.875 6.772   1.00 42.80  ? 84  ASP A CB    1 
ATOM   665  C  CG    . ASP A 1 84  ? 30.751  -13.286 5.609   1.00 44.37  ? 84  ASP A CG    1 
ATOM   666  O  OD1   . ASP A 1 84  ? 30.706  -12.040 5.511   1.00 45.56  ? 84  ASP A OD1   1 
ATOM   667  O  OD2   . ASP A 1 84  ? 30.204  -14.068 4.795   1.00 40.54  ? 84  ASP A OD2   1 
ATOM   668  N  N     . VAL A 1 85  ? 30.379  -11.626 9.569   1.00 42.99  ? 85  VAL A N     1 
ATOM   669  C  CA    . VAL A 1 85  ? 29.299  -11.461 10.541  1.00 40.17  ? 85  VAL A CA    1 
ATOM   670  C  C     . VAL A 1 85  ? 28.657  -10.073 10.506  1.00 46.42  ? 85  VAL A C     1 
ATOM   671  O  O     . VAL A 1 85  ? 27.645  -9.843  11.182  1.00 43.86  ? 85  VAL A O     1 
ATOM   672  C  CB    . VAL A 1 85  ? 29.798  -11.765 11.968  1.00 47.62  ? 85  VAL A CB    1 
ATOM   673  C  CG1   . VAL A 1 85  ? 30.327  -13.188 12.067  1.00 45.16  ? 85  VAL A CG1   1 
ATOM   674  C  CG2   . VAL A 1 85  ? 30.863  -10.756 12.398  1.00 44.60  ? 85  VAL A CG2   1 
ATOM   675  N  N     . ALA A 1 86  ? 29.219  -9.136  9.739   1.00 42.12  ? 86  ALA A N     1 
ATOM   676  C  CA    . ALA A 1 86  ? 28.717  -7.761  9.774   1.00 46.03  ? 86  ALA A CA    1 
ATOM   677  C  C     . ALA A 1 86  ? 29.226  -6.994  8.554   1.00 46.24  ? 86  ALA A C     1 
ATOM   678  O  O     . ALA A 1 86  ? 29.985  -7.516  7.732   1.00 45.20  ? 86  ALA A O     1 
ATOM   679  C  CB    . ALA A 1 86  ? 29.125  -7.051  11.068  1.00 47.27  ? 86  ALA A CB    1 
ATOM   680  N  N     . ARG A 1 87  ? 28.777  -5.743  8.441   1.00 46.54  ? 87  ARG A N     1 
ATOM   681  C  CA    . ARG A 1 87  ? 29.318  -4.840  7.437   1.00 44.42  ? 87  ARG A CA    1 
ATOM   682  C  C     . ARG A 1 87  ? 30.789  -4.569  7.725   1.00 45.11  ? 87  ARG A C     1 
ATOM   683  O  O     . ARG A 1 87  ? 31.237  -4.616  8.874   1.00 46.65  ? 87  ARG A O     1 
ATOM   684  C  CB    . ARG A 1 87  ? 28.537  -3.519  7.416   1.00 42.24  ? 87  ARG A CB    1 
ATOM   685  C  CG    . ARG A 1 87  ? 27.153  -3.612  6.751   1.00 43.92  ? 87  ARG A CG    1 
ATOM   686  C  CD    . ARG A 1 87  ? 26.439  -2.262  6.674   1.00 40.79  ? 87  ARG A CD    1 
ATOM   687  N  NE    . ARG A 1 87  ? 26.090  -1.733  7.989   1.00 44.49  ? 87  ARG A NE    1 
ATOM   688  C  CZ    . ARG A 1 87  ? 26.818  -0.852  8.661   1.00 43.12  ? 87  ARG A CZ    1 
ATOM   689  N  NH1   . ARG A 1 87  ? 27.962  -0.392  8.181   1.00 40.75  ? 87  ARG A NH1   1 
ATOM   690  N  NH2   . ARG A 1 87  ? 26.385  -0.418  9.842   1.00 42.61  ? 87  ARG A NH2   1 
ATOM   691  N  N     . ILE A 1 88  ? 31.544  -4.292  6.662   1.00 43.78  ? 88  ILE A N     1 
ATOM   692  C  CA    . ILE A 1 88  ? 32.949  -3.899  6.752   1.00 45.42  ? 88  ILE A CA    1 
ATOM   693  C  C     . ILE A 1 88  ? 33.060  -2.547  6.063   1.00 48.42  ? 88  ILE A C     1 
ATOM   694  O  O     . ILE A 1 88  ? 33.212  -2.485  4.834   1.00 44.37  ? 88  ILE A O     1 
ATOM   695  C  CB    . ILE A 1 88  ? 33.886  -4.918  6.098   1.00 48.74  ? 88  ILE A CB    1 
ATOM   696  C  CG1   . ILE A 1 88  ? 33.517  -6.334  6.524   1.00 50.19  ? 88  ILE A CG1   1 
ATOM   697  C  CG2   . ILE A 1 88  ? 35.336  -4.606  6.452   1.00 49.35  ? 88  ILE A CG2   1 
ATOM   698  C  CD1   . ILE A 1 88  ? 34.165  -7.404  5.666   1.00 53.58  ? 88  ILE A CD1   1 
ATOM   699  N  N     . GLU A 1 89  ? 33.009  -1.462  6.843   1.00 45.39  ? 89  GLU A N     1 
ATOM   700  C  CA    . GLU A 1 89  ? 32.986  -0.132  6.244   1.00 46.66  ? 89  GLU A CA    1 
ATOM   701  C  C     . GLU A 1 89  ? 34.287  0.176   5.514   1.00 48.72  ? 89  GLU A C     1 
ATOM   702  O  O     . GLU A 1 89  ? 34.274  0.877   4.494   1.00 49.17  ? 89  GLU A O     1 
ATOM   703  C  CB    . GLU A 1 89  ? 32.685  0.918   7.322   1.00 47.39  ? 89  GLU A CB    1 
ATOM   704  C  CG    . GLU A 1 89  ? 31.330  0.634   8.007   1.00 50.11  ? 89  GLU A CG    1 
ATOM   705  C  CD    . GLU A 1 89  ? 30.917  1.650   9.070   1.00 51.25  ? 89  GLU A CD    1 
ATOM   706  O  OE1   . GLU A 1 89  ? 31.663  2.621   9.335   1.00 48.83  ? 89  GLU A OE1   1 
ATOM   707  O  OE2   . GLU A 1 89  ? 29.818  1.454   9.641   1.00 50.91  ? 89  GLU A OE2   1 
ATOM   708  N  N     . SER A 1 90  ? 35.412  -0.354  6.002   1.00 48.85  ? 90  SER A N     1 
ATOM   709  C  CA    . SER A 1 90  ? 36.718  -0.095  5.397   1.00 50.38  ? 90  SER A CA    1 
ATOM   710  C  C     . SER A 1 90  ? 36.913  -0.796  4.061   1.00 49.91  ? 90  SER A C     1 
ATOM   711  O  O     . SER A 1 90  ? 37.864  -0.456  3.347   1.00 53.27  ? 90  SER A O     1 
ATOM   712  C  CB    . SER A 1 90  ? 37.837  -0.521  6.348   1.00 50.68  ? 90  SER A CB    1 
ATOM   713  O  OG    . SER A 1 90  ? 37.622  -1.844  6.806   1.00 55.87  ? 90  SER A OG    1 
ATOM   714  N  N     . LYS A 1 91  ? 36.058  -1.763  3.715   1.00 47.53  ? 91  LYS A N     1 
ATOM   715  C  CA    . LYS A 1 91  ? 36.094  -2.436  2.421   1.00 44.89  ? 91  LYS A CA    1 
ATOM   716  C  C     . LYS A 1 91  ? 34.879  -2.098  1.557   1.00 42.23  ? 91  LYS A C     1 
ATOM   717  O  O     . LYS A 1 91  ? 34.610  -2.783  0.566   1.00 43.48  ? 91  LYS A O     1 
ATOM   718  C  CB    . LYS A 1 91  ? 36.206  -3.945  2.620   1.00 48.63  ? 91  LYS A CB    1 
ATOM   719  C  CG    . LYS A 1 91  ? 37.542  -4.386  3.220   1.00 52.25  ? 91  LYS A CG    1 
ATOM   720  C  CD    . LYS A 1 91  ? 37.598  -5.900  3.364   1.00 52.73  ? 91  LYS A CD    1 
ATOM   721  C  CE    . LYS A 1 91  ? 38.998  -6.386  3.679   1.00 55.92  ? 91  LYS A CE    1 
ATOM   722  N  NZ    . LYS A 1 91  ? 39.643  -5.497  4.686   1.00 64.19  ? 91  LYS A NZ    1 
ATOM   723  N  N     . THR A 1 92  ? 34.142  -1.052  1.910   1.00 40.31  ? 92  THR A N     1 
ATOM   724  C  CA    . THR A 1 92  ? 32.986  -0.596  1.150   1.00 39.64  ? 92  THR A CA    1 
ATOM   725  C  C     . THR A 1 92  ? 33.379  0.705   0.462   1.00 43.56  ? 92  THR A C     1 
ATOM   726  O  O     . THR A 1 92  ? 33.746  1.676   1.136   1.00 43.12  ? 92  THR A O     1 
ATOM   727  C  CB    . THR A 1 92  ? 31.783  -0.402  2.076   1.00 41.67  ? 92  THR A CB    1 
ATOM   728  O  OG1   . THR A 1 92  ? 31.541  -1.618  2.792   1.00 39.33  ? 92  THR A OG1   1 
ATOM   729  C  CG2   . THR A 1 92  ? 30.515  -0.021  1.296   1.00 38.20  ? 92  THR A CG2   1 
ATOM   730  N  N     . VAL A 1 93  ? 33.321  0.723   -0.876  1.00 39.31  ? 93  VAL A N     1 
ATOM   731  C  CA    . VAL A 1 93  ? 33.895  1.813   -1.659  1.00 40.61  ? 93  VAL A CA    1 
ATOM   732  C  C     . VAL A 1 93  ? 32.904  2.317   -2.701  1.00 37.82  ? 93  VAL A C     1 
ATOM   733  O  O     . VAL A 1 93  ? 32.017  1.593   -3.163  1.00 35.77  ? 93  VAL A O     1 
ATOM   734  C  CB    . VAL A 1 93  ? 35.206  1.390   -2.359  1.00 44.04  ? 93  VAL A CB    1 
ATOM   735  C  CG1   . VAL A 1 93  ? 36.253  0.992   -1.336  1.00 45.22  ? 93  VAL A CG1   1 
ATOM   736  C  CG2   . VAL A 1 93  ? 34.929  0.253   -3.338  1.00 39.54  ? 93  VAL A CG2   1 
ATOM   737  N  N     . ILE A 1 94  ? 33.102  3.575   -3.094  1.00 40.92  ? 94  ILE A N     1 
ATOM   738  C  CA    . ILE A 1 94  ? 32.328  4.237   -4.139  1.00 39.29  ? 94  ILE A CA    1 
ATOM   739  C  C     . ILE A 1 94  ? 33.310  4.764   -5.181  1.00 41.32  ? 94  ILE A C     1 
ATOM   740  O  O     . ILE A 1 94  ? 34.289  5.429   -4.828  1.00 42.65  ? 94  ILE A O     1 
ATOM   741  C  CB    . ILE A 1 94  ? 31.458  5.372   -3.562  1.00 37.98  ? 94  ILE A CB    1 
ATOM   742  C  CG1   . ILE A 1 94  ? 30.429  4.793   -2.574  1.00 39.30  ? 94  ILE A CG1   1 
ATOM   743  C  CG2   . ILE A 1 94  ? 30.759  6.157   -4.675  1.00 36.58  ? 94  ILE A CG2   1 
ATOM   744  C  CD1   . ILE A 1 94  ? 29.438  5.825   -2.083  1.00 44.32  ? 94  ILE A CD1   1 
ATOM   745  N  N     . ILE A 1 95  ? 33.051  4.453   -6.452  1.00 39.14  ? 95  ILE A N     1 
ATOM   746  C  CA    . ILE A 1 95  ? 33.929  4.803   -7.569  1.00 42.10  ? 95  ILE A CA    1 
ATOM   747  C  C     . ILE A 1 95  ? 33.276  5.927   -8.356  1.00 45.87  ? 95  ILE A C     1 
ATOM   748  O  O     . ILE A 1 95  ? 32.171  5.760   -8.895  1.00 45.33  ? 95  ILE A O     1 
ATOM   749  C  CB    . ILE A 1 95  ? 34.212  3.600   -8.483  1.00 46.15  ? 95  ILE A CB    1 
ATOM   750  C  CG1   . ILE A 1 95  ? 35.201  2.645   -7.827  1.00 47.27  ? 95  ILE A CG1   1 
ATOM   751  C  CG2   . ILE A 1 95  ? 34.770  4.061   -9.839  1.00 49.87  ? 95  ILE A CG2   1 
ATOM   752  C  CD1   . ILE A 1 95  ? 34.575  1.601   -7.013  1.00 42.63  ? 95  ILE A CD1   1 
ATOM   753  N  N     . THR A 1 96  ? 33.956  7.071   -8.404  1.00 42.59  ? 96  THR A N     1 
ATOM   754  C  CA    . THR A 1 96  ? 33.593  8.201   -9.244  1.00 44.46  ? 96  THR A CA    1 
ATOM   755  C  C     . THR A 1 96  ? 34.851  8.699   -9.949  1.00 49.33  ? 96  THR A C     1 
ATOM   756  O  O     . THR A 1 96  ? 35.979  8.442   -9.515  1.00 50.73  ? 96  THR A O     1 
ATOM   757  C  CB    . THR A 1 96  ? 32.949  9.352   -8.439  1.00 45.53  ? 96  THR A CB    1 
ATOM   758  O  OG1   . THR A 1 96  ? 33.777  9.671   -7.316  1.00 48.18  ? 96  THR A OG1   1 
ATOM   759  C  CG2   . THR A 1 96  ? 31.533  8.970   -7.928  1.00 45.51  ? 96  THR A CG2   1 
ATOM   760  N  N     . GLN A 1 97  ? 34.649  9.417   -11.052 1.00 54.39  ? 97  GLN A N     1 
ATOM   761  C  CA    . GLN A 1 97  ? 35.787  10.006  -11.752 1.00 55.11  ? 97  GLN A CA    1 
ATOM   762  C  C     . GLN A 1 97  ? 36.551  10.959  -10.835 1.00 57.55  ? 97  GLN A C     1 
ATOM   763  O  O     . GLN A 1 97  ? 37.782  10.898  -10.745 1.00 59.61  ? 97  GLN A O     1 
ATOM   764  C  CB    . GLN A 1 97  ? 35.305  10.717  -13.019 1.00 62.58  ? 97  GLN A CB    1 
ATOM   765  C  CG    . GLN A 1 97  ? 36.400  11.407  -13.822 1.00 71.77  ? 97  GLN A CG    1 
ATOM   766  C  CD    . GLN A 1 97  ? 37.433  10.442  -14.379 1.00 80.69  ? 97  GLN A CD    1 
ATOM   767  O  OE1   . GLN A 1 97  ? 37.192  9.237   -14.486 1.00 81.12  ? 97  GLN A OE1   1 
ATOM   768  N  NE2   . GLN A 1 97  ? 38.599  10.973  -14.740 1.00 82.05  ? 97  GLN A NE2   1 
ATOM   769  N  N     . GLU A 1 98  ? 35.830  11.819  -10.115 1.00 54.12  ? 98  GLU A N     1 
ATOM   770  C  CA    . GLU A 1 98  ? 36.419  12.794  -9.205  1.00 50.67  ? 98  GLU A CA    1 
ATOM   771  C  C     . GLU A 1 98  ? 36.123  12.415  -7.760  1.00 49.75  ? 98  GLU A C     1 
ATOM   772  O  O     . GLU A 1 98  ? 34.986  12.067  -7.427  1.00 47.26  ? 98  GLU A O     1 
ATOM   773  C  CB    . GLU A 1 98  ? 35.887  14.195  -9.508  1.00 60.26  ? 98  GLU A CB    1 
ATOM   774  C  CG    . GLU A 1 98  ? 36.257  14.689  -10.902 1.00 64.57  ? 98  GLU A CG    1 
ATOM   775  C  CD    . GLU A 1 98  ? 37.728  15.005  -11.017 1.00 72.27  ? 98  GLU A CD    1 
ATOM   776  O  OE1   . GLU A 1 98  ? 38.259  15.651  -10.085 1.00 74.21  ? 98  GLU A OE1   1 
ATOM   777  O  OE2   . GLU A 1 98  ? 38.354  14.607  -12.029 1.00 80.96  ? 98  GLU A OE2   1 
ATOM   778  N  N     . GLN A 1 99  ? 37.144  12.492  -6.902  1.00 48.56  ? 99  GLN A N     1 
ATOM   779  C  CA    . GLN A 1 99  ? 36.955  12.122  -5.504  1.00 50.64  ? 99  GLN A CA    1 
ATOM   780  C  C     . GLN A 1 99  ? 35.926  13.021  -4.817  1.00 46.53  ? 99  GLN A C     1 
ATOM   781  O  O     . GLN A 1 99  ? 35.134  12.554  -3.985  1.00 45.70  ? 99  GLN A O     1 
ATOM   782  C  CB    . GLN A 1 99  ? 38.287  12.174  -4.753  1.00 51.52  ? 99  GLN A CB    1 
ATOM   783  C  CG    . GLN A 1 99  ? 38.117  11.743  -3.288  1.00 52.11  ? 99  GLN A CG    1 
ATOM   784  C  CD    . GLN A 1 99  ? 39.404  11.796  -2.496  1.00 56.58  ? 99  GLN A CD    1 
ATOM   785  O  OE1   . GLN A 1 99  ? 40.458  12.161  -3.016  1.00 58.27  ? 99  GLN A OE1   1 
ATOM   786  N  NE2   . GLN A 1 99  ? 39.324  11.420  -1.225  1.00 61.81  ? 99  GLN A NE2   1 
ATOM   787  N  N     . ARG A 1 100 ? 35.914  14.311  -5.170  1.00 48.62  ? 100 ARG A N     1 
ATOM   788  C  CA    . ARG A 1 100 ? 35.037  15.285  -4.534  1.00 48.79  ? 100 ARG A CA    1 
ATOM   789  C  C     . ARG A 1 100 ? 33.562  14.964  -4.745  1.00 46.80  ? 100 ARG A C     1 
ATOM   790  O  O     . ARG A 1 100 ? 32.726  15.385  -3.942  1.00 48.76  ? 100 ARG A O     1 
ATOM   791  C  CB    . ARG A 1 100 ? 35.358  16.697  -5.057  1.00 51.78  ? 100 ARG A CB    1 
ATOM   792  C  CG    . ARG A 1 100 ? 34.888  17.827  -4.136  1.00 56.27  ? 100 ARG A CG    1 
ATOM   793  C  CD    . ARG A 1 100 ? 35.152  19.213  -4.730  1.00 61.92  ? 100 ARG A CD    1 
ATOM   794  N  NE    . ARG A 1 100 ? 34.749  20.273  -3.811  1.00 69.03  ? 100 ARG A NE    1 
ATOM   795  C  CZ    . ARG A 1 100 ? 35.096  21.547  -3.928  1.00 68.85  ? 100 ARG A CZ    1 
ATOM   796  N  NH1   . ARG A 1 100 ? 35.864  21.970  -4.922  1.00 77.33  ? 100 ARG A NH1   1 
ATOM   797  N  NH2   . ARG A 1 100 ? 34.665  22.423  -3.022  1.00 69.79  ? 100 ARG A NH2   1 
ATOM   798  N  N     . ASP A 1 101 ? 33.217  14.214  -5.794  1.00 47.18  ? 101 ASP A N     1 
ATOM   799  C  CA    . ASP A 1 101 ? 31.829  13.813  -5.957  1.00 45.77  ? 101 ASP A CA    1 
ATOM   800  C  C     . ASP A 1 101 ? 31.393  12.813  -4.891  1.00 43.92  ? 101 ASP A C     1 
ATOM   801  O  O     . ASP A 1 101 ? 30.200  12.739  -4.591  1.00 45.63  ? 101 ASP A O     1 
ATOM   802  C  CB    . ASP A 1 101 ? 31.598  13.214  -7.346  1.00 51.65  ? 101 ASP A CB    1 
ATOM   803  C  CG    . ASP A 1 101 ? 31.833  14.214  -8.459  1.00 57.46  ? 101 ASP A CG    1 
ATOM   804  O  OD1   . ASP A 1 101 ? 31.844  15.429  -8.178  1.00 60.38  ? 101 ASP A OD1   1 
ATOM   805  O  OD2   . ASP A 1 101 ? 32.000  13.783  -9.616  1.00 63.68  ? 101 ASP A OD2   1 
ATOM   806  N  N     . THR A 1 102 ? 32.326  12.056  -4.312  1.00 45.17  ? 102 THR A N     1 
ATOM   807  C  CA    . THR A 1 102 ? 32.010  11.007  -3.346  1.00 41.42  ? 102 THR A CA    1 
ATOM   808  C  C     . THR A 1 102 ? 32.132  11.483  -1.902  1.00 42.55  ? 102 THR A C     1 
ATOM   809  O  O     . THR A 1 102 ? 31.270  11.169  -1.076  1.00 46.00  ? 102 THR A O     1 
ATOM   810  C  CB    . THR A 1 102 ? 32.914  9.781   -3.561  1.00 43.91  ? 102 THR A CB    1 
ATOM   811  O  OG1   . THR A 1 102 ? 32.594  9.163   -4.813  1.00 44.74  ? 102 THR A OG1   1 
ATOM   812  C  CG2   . THR A 1 102 ? 32.748  8.743   -2.417  1.00 40.00  ? 102 THR A CG2   1 
ATOM   813  N  N     . VAL A 1 103 ? 33.217  12.178  -1.574  1.00 41.25  ? 103 VAL A N     1 
ATOM   814  C  CA    . VAL A 1 103 ? 33.439  12.721  -0.231  1.00 42.82  ? 103 VAL A CA    1 
ATOM   815  C  C     . VAL A 1 103 ? 33.980  14.128  -0.350  1.00 45.29  ? 103 VAL A C     1 
ATOM   816  O  O     . VAL A 1 103 ? 34.633  14.486  -1.341  1.00 49.95  ? 103 VAL A O     1 
ATOM   817  C  CB    . VAL A 1 103 ? 34.435  11.867  0.580   1.00 43.67  ? 103 VAL A CB    1 
ATOM   818  C  CG1   . VAL A 1 103 ? 33.848  10.524  0.892   1.00 42.83  ? 103 VAL A CG1   1 
ATOM   819  C  CG2   . VAL A 1 103 ? 35.766  11.732  -0.199  1.00 47.07  ? 103 VAL A CG2   1 
ATOM   820  N  N     . PRO A 1 104 ? 33.747  14.958  0.672   1.00 45.79  ? 104 PRO A N     1 
ATOM   821  C  CA    . PRO A 1 104 ? 34.462  16.231  0.741   1.00 48.59  ? 104 PRO A CA    1 
ATOM   822  C  C     . PRO A 1 104 ? 35.946  15.969  0.926   1.00 49.97  ? 104 PRO A C     1 
ATOM   823  O  O     . PRO A 1 104 ? 36.343  14.996  1.569   1.00 49.06  ? 104 PRO A O     1 
ATOM   824  C  CB    . PRO A 1 104 ? 33.861  16.928  1.974   1.00 49.23  ? 104 PRO A CB    1 
ATOM   825  C  CG    . PRO A 1 104 ? 32.602  16.198  2.273   1.00 46.83  ? 104 PRO A CG    1 
ATOM   826  C  CD    . PRO A 1 104 ? 32.841  14.770  1.821   1.00 44.71  ? 104 PRO A CD    1 
ATOM   827  N  N     . ILE A 1 105 ? 36.763  16.835  0.334   1.00 52.41  ? 105 ILE A N     1 
ATOM   828  C  CA    . ILE A 1 105 ? 38.213  16.756  0.489   1.00 54.36  ? 105 ILE A CA    1 
ATOM   829  C  C     . ILE A 1 105 ? 38.557  17.287  1.875   1.00 55.93  ? 105 ILE A C     1 
ATOM   830  O  O     . ILE A 1 105 ? 38.345  18.478  2.144   1.00 57.66  ? 105 ILE A O     1 
ATOM   831  C  CB    . ILE A 1 105 ? 38.948  17.548  -0.609  1.00 56.80  ? 105 ILE A CB    1 
ATOM   832  C  CG1   . ILE A 1 105 ? 38.542  17.039  -1.996  1.00 55.51  ? 105 ILE A CG1   1 
ATOM   833  C  CG2   . ILE A 1 105 ? 40.458  17.481  -0.404  1.00 59.17  ? 105 ILE A CG2   1 
ATOM   834  C  CD1   . ILE A 1 105 ? 38.666  15.545  -2.165  1.00 58.34  ? 105 ILE A CD1   1 
ATOM   835  N  N     . PRO A 1 106 ? 39.065  16.456  2.781   1.00 55.62  ? 106 PRO A N     1 
ATOM   836  C  CA    . PRO A 1 106 ? 39.240  16.905  4.162   1.00 57.12  ? 106 PRO A CA    1 
ATOM   837  C  C     . PRO A 1 106 ? 40.353  17.927  4.268   1.00 60.70  ? 106 PRO A C     1 
ATOM   838  O  O     . PRO A 1 106 ? 41.196  18.079  3.380   1.00 62.10  ? 106 PRO A O     1 
ATOM   839  C  CB    . PRO A 1 106 ? 39.579  15.619  4.931   1.00 56.09  ? 106 PRO A CB    1 
ATOM   840  C  CG    . PRO A 1 106 ? 39.161  14.522  4.060   1.00 53.37  ? 106 PRO A CG    1 
ATOM   841  C  CD    . PRO A 1 106 ? 39.326  15.014  2.647   1.00 53.82  ? 106 PRO A CD    1 
ATOM   842  N  N     . LYS A 1 107 ? 40.330  18.656  5.376   1.00 62.41  ? 107 LYS A N     1 
ATOM   843  C  CA    . LYS A 1 107 ? 41.322  19.703  5.566   1.00 66.08  ? 107 LYS A CA    1 
ATOM   844  C  C     . LYS A 1 107 ? 42.682  19.128  5.932   1.00 67.93  ? 107 LYS A C     1 
ATOM   845  O  O     . LYS A 1 107 ? 43.716  19.645  5.493   1.00 70.66  ? 107 LYS A O     1 
ATOM   846  C  CB    . LYS A 1 107 ? 40.854  20.680  6.643   1.00 67.61  ? 107 LYS A CB    1 
ATOM   847  C  CG    . LYS A 1 107 ? 41.561  22.011  6.606   1.00 71.32  ? 107 LYS A CG    1 
ATOM   848  C  CD    . LYS A 1 107 ? 40.986  22.981  7.616   1.00 72.82  ? 107 LYS A CD    1 
ATOM   849  C  CE    . LYS A 1 107 ? 41.663  24.340  7.477   1.00 76.64  ? 107 LYS A CE    1 
ATOM   850  N  NZ    . LYS A 1 107 ? 41.242  25.299  8.536   1.00 82.26  ? 107 LYS A NZ    1 
ATOM   851  N  N     . SER A 1 108 ? 42.708  18.065  6.732   1.00 66.78  ? 108 SER A N     1 
ATOM   852  C  CA    . SER A 1 108 ? 43.971  17.603  7.291   1.00 69.13  ? 108 SER A CA    1 
ATOM   853  C  C     . SER A 1 108 ? 44.101  16.089  7.267   1.00 67.15  ? 108 SER A C     1 
ATOM   854  O  O     . SER A 1 108 ? 45.136  15.554  6.850   1.00 68.40  ? 108 SER A O     1 
ATOM   855  C  CB    . SER A 1 108 ? 44.128  18.107  8.723   1.00 71.47  ? 108 SER A CB    1 
ATOM   856  O  OG    . SER A 1 108 ? 44.485  19.474  8.722   1.00 74.43  ? 108 SER A OG    1 
ATOM   857  N  N     . GLY A 1 109 ? 43.076  15.392  7.732   1.00 64.35  ? 109 GLY A N     1 
ATOM   858  C  CA    . GLY A 1 109 ? 43.137  13.967  7.891   1.00 62.71  ? 109 GLY A CA    1 
ATOM   859  C  C     . GLY A 1 109 ? 42.509  13.211  6.738   1.00 59.49  ? 109 GLY A C     1 
ATOM   860  O  O     . GLY A 1 109 ? 42.263  13.746  5.650   1.00 58.90  ? 109 GLY A O     1 
ATOM   861  N  N     . GLN A 1 110 ? 42.263  11.937  6.981   1.00 57.63  ? 110 GLN A N     1 
ATOM   862  C  CA    . GLN A 1 110 ? 41.583  11.082  6.040   1.00 54.57  ? 110 GLN A CA    1 
ATOM   863  C  C     . GLN A 1 110 ? 40.081  11.257  6.241   1.00 52.05  ? 110 GLN A C     1 
ATOM   864  O  O     . GLN A 1 110 ? 39.634  11.616  7.330   1.00 53.84  ? 110 GLN A O     1 
ATOM   865  C  CB    . GLN A 1 110 ? 42.049  9.648   6.290   1.00 54.15  ? 110 GLN A CB    1 
ATOM   866  C  CG    . GLN A 1 110 ? 41.318  8.523   5.641   1.00 55.40  ? 110 GLN A CG    1 
ATOM   867  C  CD    . GLN A 1 110 ? 42.019  7.218   5.953   1.00 57.05  ? 110 GLN A CD    1 
ATOM   868  O  OE1   . GLN A 1 110 ? 43.114  6.949   5.440   1.00 60.23  ? 110 GLN A OE1   1 
ATOM   869  N  NE2   . GLN A 1 110 ? 41.433  6.432   6.840   1.00 50.41  ? 110 GLN A NE2   1 
ATOM   870  N  N     . SER A 1 111 ? 39.304  11.031  5.182   1.00 49.71  ? 111 SER A N     1 
ATOM   871  C  CA    . SER A 1 111 ? 37.854  11.189  5.272   1.00 47.55  ? 111 SER A CA    1 
ATOM   872  C  C     . SER A 1 111 ? 37.184  9.992   5.936   1.00 50.42  ? 111 SER A C     1 
ATOM   873  O  O     . SER A 1 111 ? 37.456  8.837   5.593   1.00 48.55  ? 111 SER A O     1 
ATOM   874  C  CB    . SER A 1 111 ? 37.244  11.387  3.886   1.00 46.12  ? 111 SER A CB    1 
ATOM   875  O  OG    . SER A 1 111 ? 35.825  11.389  3.952   1.00 44.13  ? 111 SER A OG    1 
ATOM   876  N  N     . GLN A 1 112 ? 36.266  10.284  6.863   1.00 47.33  ? 112 GLN A N     1 
ATOM   877  C  CA    . GLN A 1 112 ? 35.407  9.291   7.487   1.00 43.46  ? 112 GLN A CA    1 
ATOM   878  C  C     . GLN A 1 112 ? 33.996  9.301   6.933   1.00 47.61  ? 112 GLN A C     1 
ATOM   879  O  O     . GLN A 1 112 ? 33.103  8.716   7.548   1.00 50.31  ? 112 GLN A O     1 
ATOM   880  C  CB    . GLN A 1 112 ? 35.281  9.512   8.988   1.00 46.22  ? 112 GLN A CB    1 
ATOM   881  C  CG    . GLN A 1 112 ? 36.457  9.995   9.758   1.00 49.10  ? 112 GLN A CG    1 
ATOM   882  C  CD    . GLN A 1 112 ? 36.056  10.172  11.204  1.00 49.03  ? 112 GLN A CD    1 
ATOM   883  O  OE1   . GLN A 1 112 ? 34.925  9.832   11.578  1.00 52.63  ? 112 GLN A OE1   1 
ATOM   884  N  NE2   . GLN A 1 112 ? 36.959  10.689  12.023  1.00 51.96  ? 112 GLN A NE2   1 
ATOM   885  N  N     . LEU A 1 113 ? 33.755  9.992   5.828   1.00 48.39  ? 113 LEU A N     1 
ATOM   886  C  CA    . LEU A 1 113 ? 32.406  10.154  5.303   1.00 41.58  ? 113 LEU A CA    1 
ATOM   887  C  C     . LEU A 1 113 ? 32.186  9.295   4.082   1.00 45.03  ? 113 LEU A C     1 
ATOM   888  O  O     . LEU A 1 113 ? 31.144  9.403   3.426   1.00 46.83  ? 113 LEU A O     1 
ATOM   889  C  CB    . LEU A 1 113 ? 32.145  11.630  4.995   1.00 48.73  ? 113 LEU A CB    1 
ATOM   890  C  CG    . LEU A 1 113 ? 32.120  12.458  6.273   1.00 44.77  ? 113 LEU A CG    1 
ATOM   891  C  CD1   . LEU A 1 113 ? 32.191  13.936  5.972   1.00 44.43  ? 113 LEU A CD1   1 
ATOM   892  C  CD2   . LEU A 1 113 ? 30.855  12.134  7.018   1.00 44.94  ? 113 LEU A CD2   1 
ATOM   893  N  N     . GLY A 1 114 ? 33.142  8.432   3.786   1.00 49.61  ? 114 GLY A N     1 
ATOM   894  C  CA    . GLY A 1 114 ? 33.035  7.475   2.705   1.00 47.30  ? 114 GLY A CA    1 
ATOM   895  C  C     . GLY A 1 114 ? 34.426  6.997   2.360   1.00 46.29  ? 114 GLY A C     1 
ATOM   896  O  O     . GLY A 1 114 ? 35.426  7.475   2.901   1.00 45.78  ? 114 GLY A O     1 
ATOM   897  N  N     . ARG A 1 115 ? 34.474  6.034   1.450   1.00 47.43  ? 115 ARG A N     1 
ATOM   898  C  CA    . ARG A 1 115 ? 35.743  5.550   0.913   1.00 48.74  ? 115 ARG A CA    1 
ATOM   899  C  C     . ARG A 1 115 ? 35.671  5.616   -0.606  1.00 43.91  ? 115 ARG A C     1 
ATOM   900  O  O     . ARG A 1 115 ? 34.912  4.865   -1.228  1.00 45.07  ? 115 ARG A O     1 
ATOM   901  C  CB    . ARG A 1 115 ? 36.038  4.131   1.401   1.00 49.79  ? 115 ARG A CB    1 
ATOM   902  C  CG    . ARG A 1 115 ? 36.917  4.073   2.639   1.00 55.82  ? 115 ARG A CG    1 
ATOM   903  C  CD    . ARG A 1 115 ? 37.792  2.808   2.636   1.00 64.79  ? 115 ARG A CD    1 
ATOM   904  N  NE    . ARG A 1 115 ? 38.664  2.734   1.463   1.00 69.03  ? 115 ARG A NE    1 
ATOM   905  C  CZ    . ARG A 1 115 ? 39.557  1.775   1.239   1.00 69.43  ? 115 ARG A CZ    1 
ATOM   906  N  NH1   . ARG A 1 115 ? 39.741  0.784   2.097   1.00 64.79  ? 115 ARG A NH1   1 
ATOM   907  N  NH2   . ARG A 1 115 ? 40.287  1.812   0.127   1.00 67.91  ? 115 ARG A NH2   1 
ATOM   908  N  N     . TRP A 1 116 ? 36.427  6.535   -1.193  1.00 46.56  ? 116 TRP A N     1 
ATOM   909  C  CA    . TRP A 1 116 ? 36.483  6.710   -2.636  1.00 48.37  ? 116 TRP A CA    1 
ATOM   910  C  C     . TRP A 1 116 ? 37.604  5.855   -3.202  1.00 49.89  ? 116 TRP A C     1 
ATOM   911  O  O     . TRP A 1 116 ? 38.681  5.765   -2.609  1.00 53.18  ? 116 TRP A O     1 
ATOM   912  C  CB    . TRP A 1 116 ? 36.726  8.186   -3.000  1.00 45.55  ? 116 TRP A CB    1 
ATOM   913  C  CG    . TRP A 1 116 ? 36.931  8.421   -4.476  1.00 46.76  ? 116 TRP A CG    1 
ATOM   914  C  CD1   . TRP A 1 116 ? 35.961  8.506   -5.435  1.00 47.28  ? 116 TRP A CD1   1 
ATOM   915  C  CD2   . TRP A 1 116 ? 38.183  8.609   -5.155  1.00 48.53  ? 116 TRP A CD2   1 
ATOM   916  N  NE1   . TRP A 1 116 ? 36.530  8.730   -6.669  1.00 46.99  ? 116 TRP A NE1   1 
ATOM   917  C  CE2   . TRP A 1 116 ? 37.892  8.800   -6.524  1.00 45.14  ? 116 TRP A CE2   1 
ATOM   918  C  CE3   . TRP A 1 116 ? 39.517  8.631   -4.740  1.00 48.71  ? 116 TRP A CE3   1 
ATOM   919  C  CZ2   . TRP A 1 116 ? 38.886  9.001   -7.478  1.00 47.04  ? 116 TRP A CZ2   1 
ATOM   920  C  CZ3   . TRP A 1 116 ? 40.516  8.844   -5.700  1.00 50.66  ? 116 TRP A CZ3   1 
ATOM   921  C  CH2   . TRP A 1 116 ? 40.188  9.030   -7.047  1.00 50.24  ? 116 TRP A CH2   1 
ATOM   922  N  N     . MET A 1 117 ? 37.348  5.230   -4.354  1.00 48.71  ? 117 MET A N     1 
ATOM   923  C  CA    . MET A 1 117 ? 38.368  4.495   -5.095  1.00 49.84  ? 117 MET A CA    1 
ATOM   924  C  C     . MET A 1 117 ? 38.326  4.907   -6.561  1.00 46.69  ? 117 MET A C     1 
ATOM   925  O  O     . MET A 1 117 ? 37.246  5.067   -7.136  1.00 48.69  ? 117 MET A O     1 
ATOM   926  C  CB    . MET A 1 117 ? 38.156  2.977   -4.964  1.00 47.69  ? 117 MET A CB    1 
ATOM   927  C  CG    . MET A 1 117 ? 39.243  2.142   -5.623  1.00 54.02  ? 117 MET A CG    1 
ATOM   928  S  SD    . MET A 1 117 ? 38.887  0.374   -5.509  1.00 55.98  ? 117 MET A SD    1 
ATOM   929  C  CE    . MET A 1 117 ? 38.826  0.136   -3.737  1.00 56.06  ? 117 MET A CE    1 
ATOM   930  N  N     . SER A 1 118 ? 39.492  5.083   -7.170  1.00 51.56  ? 118 SER A N     1 
ATOM   931  C  CA    . SER A 1 118 ? 39.494  5.502   -8.562  1.00 53.90  ? 118 SER A CA    1 
ATOM   932  C  C     . SER A 1 118 ? 39.007  4.363   -9.457  1.00 55.24  ? 118 SER A C     1 
ATOM   933  O  O     . SER A 1 118 ? 39.087  3.177   -9.112  1.00 52.00  ? 118 SER A O     1 
ATOM   934  C  CB    . SER A 1 118 ? 40.885  5.962   -8.997  1.00 52.25  ? 118 SER A CB    1 
ATOM   935  O  OG    . SER A 1 118 ? 41.697  4.848   -9.322  1.00 55.63  ? 118 SER A OG    1 
ATOM   936  N  N     . GLU A 1 119 ? 38.468  4.743   -10.617 1.00 56.50  ? 119 GLU A N     1 
ATOM   937  C  CA    . GLU A 1 119 ? 38.000  3.744   -11.569 1.00 59.59  ? 119 GLU A CA    1 
ATOM   938  C  C     . GLU A 1 119 ? 39.141  2.841   -12.034 1.00 59.74  ? 119 GLU A C     1 
ATOM   939  O  O     . GLU A 1 119 ? 38.937  1.638   -12.238 1.00 56.79  ? 119 GLU A O     1 
ATOM   940  C  CB    . GLU A 1 119 ? 37.327  4.440   -12.756 1.00 64.80  ? 119 GLU A CB    1 
ATOM   941  C  CG    . GLU A 1 119 ? 36.879  3.497   -13.868 1.00 72.45  ? 119 GLU A CG    1 
ATOM   942  C  CD    . GLU A 1 119 ? 35.627  2.724   -13.516 1.00 77.12  ? 119 GLU A CD    1 
ATOM   943  O  OE1   . GLU A 1 119 ? 34.521  3.260   -13.734 1.00 81.29  ? 119 GLU A OE1   1 
ATOM   944  O  OE2   . GLU A 1 119 ? 35.745  1.580   -13.015 1.00 75.68  ? 119 GLU A OE2   1 
ATOM   945  N  N     . GLU A 1 120 ? 40.349  3.394   -12.178 1.00 59.64  ? 120 GLU A N     1 
ATOM   946  C  CA    . GLU A 1 120 ? 41.488  2.589   -12.616 1.00 64.13  ? 120 GLU A CA    1 
ATOM   947  C  C     . GLU A 1 120 ? 41.912  1.591   -11.545 1.00 60.12  ? 120 GLU A C     1 
ATOM   948  O  O     . GLU A 1 120 ? 42.279  0.451   -11.861 1.00 60.84  ? 120 GLU A O     1 
ATOM   949  C  CB    . GLU A 1 120 ? 42.659  3.493   -12.994 1.00 61.93  ? 120 GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 120 ? 42.417  4.321   -14.243 1.00 72.68  ? 120 GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 120 ? 41.826  5.689   -13.948 1.00 74.66  ? 120 GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 120 ? 41.027  5.817   -12.995 1.00 67.52  ? 120 GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 120 ? 42.171  6.643   -14.671 1.00 81.84  ? 120 GLU A OE2   1 
ATOM   954  N  N     . ASP A 1 121 ? 41.867  1.996   -10.275 1.00 56.99  ? 121 ASP A N     1 
ATOM   955  C  CA    . ASP A 1 121 ? 42.209  1.067   -9.205  1.00 57.04  ? 121 ASP A CA    1 
ATOM   956  C  C     . ASP A 1 121 ? 41.147  -0.014  -9.046  1.00 55.18  ? 121 ASP A C     1 
ATOM   957  O  O     . ASP A 1 121 ? 41.475  -1.172  -8.758  1.00 52.60  ? 121 ASP A O     1 
ATOM   958  C  CB    . ASP A 1 121 ? 42.413  1.822   -7.898  1.00 54.91  ? 121 ASP A CB    1 
ATOM   959  C  CG    . ASP A 1 121 ? 43.596  2.770   -7.960  1.00 61.99  ? 121 ASP A CG    1 
ATOM   960  O  OD1   . ASP A 1 121 ? 44.529  2.515   -8.757  1.00 64.27  ? 121 ASP A OD1   1 
ATOM   961  O  OD2   . ASP A 1 121 ? 43.592  3.774   -7.218  1.00 63.79  ? 121 ASP A OD2   1 
ATOM   962  N  N     . PHE A 1 122 ? 39.870  0.334   -9.235  1.00 51.92  ? 122 PHE A N     1 
ATOM   963  C  CA    . PHE A 1 122 ? 38.828  -0.683  -9.130  1.00 50.86  ? 122 PHE A CA    1 
ATOM   964  C  C     . PHE A 1 122 ? 38.959  -1.727  -10.235 1.00 51.54  ? 122 PHE A C     1 
ATOM   965  O  O     . PHE A 1 122 ? 38.692  -2.914  -10.010 1.00 54.11  ? 122 PHE A O     1 
ATOM   966  C  CB    . PHE A 1 122 ? 37.431  -0.060  -9.160  1.00 47.69  ? 122 PHE A CB    1 
ATOM   967  C  CG    . PHE A 1 122 ? 36.338  -1.090  -9.167  1.00 48.17  ? 122 PHE A CG    1 
ATOM   968  C  CD1   . PHE A 1 122 ? 36.142  -1.899  -8.057  1.00 45.57  ? 122 PHE A CD1   1 
ATOM   969  C  CD2   . PHE A 1 122 ? 35.552  -1.298  -10.292 1.00 44.88  ? 122 PHE A CD2   1 
ATOM   970  C  CE1   . PHE A 1 122 ? 35.175  -2.883  -8.049  1.00 43.48  ? 122 PHE A CE1   1 
ATOM   971  C  CE2   . PHE A 1 122 ? 34.569  -2.284  -10.292 1.00 41.66  ? 122 PHE A CE2   1 
ATOM   972  C  CZ    . PHE A 1 122 ? 34.382  -3.076  -9.168  1.00 43.05  ? 122 PHE A CZ    1 
ATOM   973  N  N     . GLU A 1 123 ? 39.361  -1.301  -11.439 1.00 50.70  ? 123 GLU A N     1 
ATOM   974  C  CA    . GLU A 1 123 ? 39.570  -2.244  -12.535 1.00 52.48  ? 123 GLU A CA    1 
ATOM   975  C  C     . GLU A 1 123 ? 40.557  -3.333  -12.144 1.00 51.90  ? 123 GLU A C     1 
ATOM   976  O  O     . GLU A 1 123 ? 40.326  -4.518  -12.410 1.00 51.31  ? 123 GLU A O     1 
ATOM   977  C  CB    . GLU A 1 123 ? 40.074  -1.509  -13.778 1.00 59.86  ? 123 GLU A CB    1 
ATOM   978  C  CG    . GLU A 1 123 ? 38.992  -0.940  -14.667 1.00 66.10  ? 123 GLU A CG    1 
ATOM   979  C  CD    . GLU A 1 123 ? 39.450  -0.804  -16.111 1.00 77.02  ? 123 GLU A CD    1 
ATOM   980  O  OE1   . GLU A 1 123 ? 40.649  -0.509  -16.349 1.00 79.08  ? 123 GLU A OE1   1 
ATOM   981  O  OE2   . GLU A 1 123 ? 38.611  -1.007  -17.013 1.00 81.46  ? 123 GLU A OE2   1 
ATOM   982  N  N     . LYS A 1 124 ? 41.663  -2.951  -11.503 1.00 51.77  ? 124 LYS A N     1 
ATOM   983  C  CA    . LYS A 1 124 ? 42.654  -3.939  -11.094 1.00 54.28  ? 124 LYS A CA    1 
ATOM   984  C  C     . LYS A 1 124 ? 42.104  -4.854  -10.006 1.00 50.67  ? 124 LYS A C     1 
ATOM   985  O  O     . LYS A 1 124 ? 42.381  -6.058  -10.004 1.00 54.22  ? 124 LYS A O     1 
ATOM   986  C  CB    . LYS A 1 124 ? 43.934  -3.234  -10.633 1.00 53.10  ? 124 LYS A CB    1 
ATOM   987  C  CG    . LYS A 1 124 ? 44.513  -2.269  -11.670 1.00 64.05  ? 124 LYS A CG    1 
ATOM   988  C  CD    . LYS A 1 124 ? 45.745  -1.530  -11.150 1.00 67.05  ? 124 LYS A CD    1 
ATOM   989  C  CE    . LYS A 1 124 ? 46.382  -0.682  -12.247 1.00 78.42  ? 124 LYS A CE    1 
ATOM   990  N  NZ    . LYS A 1 124 ? 45.441  0.326   -12.820 1.00 77.94  ? 124 LYS A NZ    1 
ATOM   991  N  N     . ALA A 1 125 ? 41.300  -4.311  -9.087  1.00 51.77  ? 125 ALA A N     1 
ATOM   992  C  CA    . ALA A 1 125 ? 40.728  -5.142  -8.035  1.00 47.84  ? 125 ALA A CA    1 
ATOM   993  C  C     . ALA A 1 125 ? 39.682  -6.101  -8.594  1.00 49.89  ? 125 ALA A C     1 
ATOM   994  O  O     . ALA A 1 125 ? 39.635  -7.274  -8.209  1.00 49.54  ? 125 ALA A O     1 
ATOM   995  C  CB    . ALA A 1 125 ? 40.117  -4.254  -6.951  1.00 49.10  ? 125 ALA A CB    1 
ATOM   996  N  N     . PHE A 1 126 ? 38.814  -5.605  -9.477  1.00 48.41  ? 126 PHE A N     1 
ATOM   997  C  CA    . PHE A 1 126 ? 37.801  -6.447  -10.101 1.00 46.25  ? 126 PHE A CA    1 
ATOM   998  C  C     . PHE A 1 126 ? 38.443  -7.626  -10.824 1.00 50.32  ? 126 PHE A C     1 
ATOM   999  O  O     . PHE A 1 126 ? 38.094  -8.789  -10.579 1.00 47.83  ? 126 PHE A O     1 
ATOM   1000 C  CB    . PHE A 1 126 ? 36.978  -5.594  -11.066 1.00 44.83  ? 126 PHE A CB    1 
ATOM   1001 C  CG    . PHE A 1 126 ? 35.897  -6.342  -11.782 1.00 46.19  ? 126 PHE A CG    1 
ATOM   1002 C  CD1   . PHE A 1 126 ? 34.650  -6.478  -11.215 1.00 40.72  ? 126 PHE A CD1   1 
ATOM   1003 C  CD2   . PHE A 1 126 ? 36.118  -6.880  -13.040 1.00 49.42  ? 126 PHE A CD2   1 
ATOM   1004 C  CE1   . PHE A 1 126 ? 33.640  -7.152  -11.873 1.00 44.52  ? 126 PHE A CE1   1 
ATOM   1005 C  CE2   . PHE A 1 126 ? 35.106  -7.565  -13.705 1.00 45.26  ? 126 PHE A CE2   1 
ATOM   1006 C  CZ    . PHE A 1 126 ? 33.866  -7.694  -13.119 1.00 43.77  ? 126 PHE A CZ    1 
ATOM   1007 N  N     . ASN A 1 127 ? 39.416  -7.337  -11.699 1.00 47.00  ? 127 ASN A N     1 
ATOM   1008 C  CA    . ASN A 1 127 ? 40.056  -8.369  -12.505 1.00 51.92  ? 127 ASN A CA    1 
ATOM   1009 C  C     . ASN A 1 127 ? 40.847  -9.359  -11.667 1.00 52.27  ? 127 ASN A C     1 
ATOM   1010 O  O     . ASN A 1 127 ? 41.149  -10.455 -12.148 1.00 50.44  ? 127 ASN A O     1 
ATOM   1011 C  CB    . ASN A 1 127 ? 40.988  -7.733  -13.537 1.00 52.31  ? 127 ASN A CB    1 
ATOM   1012 C  CG    . ASN A 1 127 ? 40.238  -7.036  -14.645 1.00 55.32  ? 127 ASN A CG    1 
ATOM   1013 O  OD1   . ASN A 1 127 ? 39.114  -7.410  -14.977 1.00 55.07  ? 127 ASN A OD1   1 
ATOM   1014 N  ND2   . ASN A 1 127 ? 40.863  -6.018  -15.236 1.00 59.87  ? 127 ASN A ND2   1 
ATOM   1015 N  N     . ALA A 1 128 ? 41.209  -8.997  -10.439 1.00 51.31  ? 128 ALA A N     1 
ATOM   1016 C  CA    . ALA A 1 128 ? 41.882  -9.943  -9.561  1.00 50.90  ? 128 ALA A CA    1 
ATOM   1017 C  C     . ALA A 1 128 ? 40.915  -10.839 -8.801  1.00 51.62  ? 128 ALA A C     1 
ATOM   1018 O  O     . ALA A 1 128 ? 41.364  -11.789 -8.155  1.00 53.97  ? 128 ALA A O     1 
ATOM   1019 C  CB    . ALA A 1 128 ? 42.778  -9.203  -8.561  1.00 51.36  ? 128 ALA A CB    1 
ATOM   1020 N  N     . ARG A 1 129 ? 39.611  -10.571 -8.861  1.00 49.51  ? 129 ARG A N     1 
ATOM   1021 C  CA    . ARG A 1 129 ? 38.631  -11.310 -8.075  1.00 47.26  ? 129 ARG A CA    1 
ATOM   1022 C  C     . ARG A 1 129 ? 37.654  -12.107 -8.926  1.00 48.99  ? 129 ARG A C     1 
ATOM   1023 O  O     . ARG A 1 129 ? 37.468  -13.310 -8.694  1.00 48.58  ? 129 ARG A O     1 
ATOM   1024 C  CB    . ARG A 1 129 ? 37.854  -10.341 -7.166  1.00 47.92  ? 129 ARG A CB    1 
ATOM   1025 C  CG    . ARG A 1 129 ? 38.675  -9.772  -6.015  1.00 48.51  ? 129 ARG A CG    1 
ATOM   1026 C  CD    . ARG A 1 129 ? 38.075  -8.476  -5.471  1.00 46.03  ? 129 ARG A CD    1 
ATOM   1027 N  NE    . ARG A 1 129 ? 38.694  -8.086  -4.208  1.00 45.81  ? 129 ARG A NE    1 
ATOM   1028 C  CZ    . ARG A 1 129 ? 39.853  -7.449  -4.103  1.00 51.58  ? 129 ARG A CZ    1 
ATOM   1029 N  NH1   . ARG A 1 129 ? 40.542  -7.082  -5.173  1.00 53.43  ? 129 ARG A NH1   1 
ATOM   1030 N  NH2   . ARG A 1 129 ? 40.338  -7.175  -2.895  1.00 49.52  ? 129 ARG A NH2   1 
ATOM   1031 N  N     . PHE A 1 130 ? 37.029  -11.484 -9.912  1.00 45.91  ? 130 PHE A N     1 
ATOM   1032 C  CA    . PHE A 1 130 ? 35.834  -12.086 -10.486 1.00 45.59  ? 130 PHE A CA    1 
ATOM   1033 C  C     . PHE A 1 130 ? 36.059  -13.136 -11.568 1.00 45.65  ? 130 PHE A C     1 
ATOM   1034 O  O     . PHE A 1 130 ? 35.240  -14.055 -11.664 1.00 45.16  ? 130 PHE A O     1 
ATOM   1035 C  CB    . PHE A 1 130 ? 34.908  -10.987 -11.007 1.00 42.42  ? 130 PHE A CB    1 
ATOM   1036 C  CG    . PHE A 1 130 ? 34.053  -10.397 -9.922  1.00 43.76  ? 130 PHE A CG    1 
ATOM   1037 C  CD1   . PHE A 1 130 ? 32.859  -11.006 -9.560  1.00 40.73  ? 130 PHE A CD1   1 
ATOM   1038 C  CD2   . PHE A 1 130 ? 34.476  -9.283  -9.216  1.00 45.18  ? 130 PHE A CD2   1 
ATOM   1039 C  CE1   . PHE A 1 130 ? 32.078  -10.496 -8.528  1.00 39.19  ? 130 PHE A CE1   1 
ATOM   1040 C  CE2   . PHE A 1 130 ? 33.697  -8.769  -8.178  1.00 43.21  ? 130 PHE A CE2   1 
ATOM   1041 C  CZ    . PHE A 1 130 ? 32.497  -9.376  -7.843  1.00 38.22  ? 130 PHE A CZ    1 
ATOM   1042 N  N     . PRO A 1 131 ? 37.119  -13.043 -12.424 1.00 48.62  ? 131 PRO A N     1 
ATOM   1043 C  CA    . PRO A 1 131 ? 37.319  -14.086 -13.445 1.00 47.08  ? 131 PRO A CA    1 
ATOM   1044 C  C     . PRO A 1 131 ? 37.303  -15.509 -12.893 1.00 47.92  ? 131 PRO A C     1 
ATOM   1045 O  O     . PRO A 1 131 ? 38.140  -15.880 -12.062 1.00 49.33  ? 131 PRO A O     1 
ATOM   1046 C  CB    . PRO A 1 131 ? 38.691  -13.732 -14.036 1.00 45.99  ? 131 PRO A CB    1 
ATOM   1047 C  CG    . PRO A 1 131 ? 38.768  -12.260 -13.910 1.00 49.55  ? 131 PRO A CG    1 
ATOM   1048 C  CD    . PRO A 1 131 ? 38.067  -11.924 -12.616 1.00 45.18  ? 131 PRO A CD    1 
ATOM   1049 N  N     . GLY A 1 132 ? 36.344  -16.310 -13.357 1.00 49.24  ? 132 GLY A N     1 
ATOM   1050 C  CA    . GLY A 1 132 ? 36.227  -17.704 -12.965 1.00 46.25  ? 132 GLY A CA    1 
ATOM   1051 C  C     . GLY A 1 132 ? 35.733  -17.944 -11.557 1.00 46.54  ? 132 GLY A C     1 
ATOM   1052 O  O     . GLY A 1 132 ? 35.824  -19.073 -11.072 1.00 45.15  ? 132 GLY A O     1 
ATOM   1053 N  N     . CYS A 1 133 ? 35.187  -16.925 -10.886 1.00 42.77  ? 133 CYS A N     1 
ATOM   1054 C  CA    . CYS A 1 133 ? 34.914  -17.050 -9.457  1.00 42.33  ? 133 CYS A CA    1 
ATOM   1055 C  C     . CYS A 1 133 ? 33.725  -17.957 -9.144  1.00 45.12  ? 133 CYS A C     1 
ATOM   1056 O  O     . CYS A 1 133 ? 33.593  -18.396 -7.996  1.00 46.17  ? 133 CYS A O     1 
ATOM   1057 C  CB    . CYS A 1 133 ? 34.683  -15.666 -8.848  1.00 41.83  ? 133 CYS A CB    1 
ATOM   1058 S  SG    . CYS A 1 133 ? 33.185  -14.850 -9.425  1.00 42.29  ? 133 CYS A SG    1 
ATOM   1059 N  N     . MET A 1 134 ? 32.860  -18.247 -10.122 1.00 40.74  ? 134 MET A N     1 
ATOM   1060 C  CA    . MET A 1 134 ? 31.698  -19.104 -9.912  1.00 39.00  ? 134 MET A CA    1 
ATOM   1061 C  C     . MET A 1 134 ? 31.880  -20.506 -10.501 1.00 41.46  ? 134 MET A C     1 
ATOM   1062 O  O     . MET A 1 134 ? 30.886  -21.196 -10.744 1.00 40.01  ? 134 MET A O     1 
ATOM   1063 C  CB    . MET A 1 134 ? 30.443  -18.469 -10.510 1.00 38.90  ? 134 MET A CB    1 
ATOM   1064 C  CG    . MET A 1 134 ? 30.019  -17.093 -9.911  1.00 32.79  ? 134 MET A CG    1 
ATOM   1065 S  SD    . MET A 1 134 ? 28.403  -16.593 -10.571 1.00 34.85  ? 134 MET A SD    1 
ATOM   1066 C  CE    . MET A 1 134 ? 28.176  -15.032 -9.682  1.00 33.53  ? 134 MET A CE    1 
ATOM   1067 N  N     . LYS A 1 135 ? 33.114  -20.932 -10.750 1.00 42.85  ? 135 LYS A N     1 
ATOM   1068 C  CA    . LYS A 1 135 ? 33.324  -22.247 -11.350 1.00 43.31  ? 135 LYS A CA    1 
ATOM   1069 C  C     . LYS A 1 135 ? 32.681  -23.315 -10.473 1.00 44.48  ? 135 LYS A C     1 
ATOM   1070 O  O     . LYS A 1 135 ? 32.799  -23.278 -9.244  1.00 46.74  ? 135 LYS A O     1 
ATOM   1071 C  CB    . LYS A 1 135 ? 34.817  -22.521 -11.541 1.00 49.82  ? 135 LYS A CB    1 
ATOM   1072 C  CG    . LYS A 1 135 ? 35.371  -21.906 -12.837 1.00 55.27  ? 135 LYS A CG    1 
ATOM   1073 C  CD    . LYS A 1 135 ? 36.899  -21.973 -12.956 1.00 57.84  ? 135 LYS A CD    1 
ATOM   1074 C  CE    . LYS A 1 135 ? 37.389  -20.948 -13.991 1.00 61.59  ? 135 LYS A CE    1 
ATOM   1075 N  NZ    . LYS A 1 135 ? 38.873  -20.854 -14.149 1.00 63.52  ? 135 LYS A NZ    1 
ATOM   1076 N  N     . GLY A 1 136 ? 31.938  -24.223 -11.107 1.00 46.71  ? 136 GLY A N     1 
ATOM   1077 C  CA    . GLY A 1 136 ? 31.245  -25.296 -10.416 1.00 43.36  ? 136 GLY A CA    1 
ATOM   1078 C  C     . GLY A 1 136 ? 30.019  -24.894 -9.622  1.00 43.17  ? 136 GLY A C     1 
ATOM   1079 O  O     . GLY A 1 136 ? 29.452  -25.749 -8.940  1.00 42.57  ? 136 GLY A O     1 
ATOM   1080 N  N     . ARG A 1 137 ? 29.597  -23.627 -9.665  1.00 39.77  ? 137 ARG A N     1 
ATOM   1081 C  CA    . ARG A 1 137 ? 28.433  -23.154 -8.920  1.00 40.00  ? 137 ARG A CA    1 
ATOM   1082 C  C     . ARG A 1 137 ? 27.301  -22.743 -9.856  1.00 38.07  ? 137 ARG A C     1 
ATOM   1083 O  O     . ARG A 1 137 ? 27.462  -22.640 -11.077 1.00 41.03  ? 137 ARG A O     1 
ATOM   1084 C  CB    . ARG A 1 137 ? 28.800  -21.976 -8.009  1.00 39.72  ? 137 ARG A CB    1 
ATOM   1085 C  CG    . ARG A 1 137 ? 29.900  -22.299 -7.010  1.00 46.79  ? 137 ARG A CG    1 
ATOM   1086 C  CD    . ARG A 1 137 ? 29.923  -21.328 -5.834  1.00 44.64  ? 137 ARG A CD    1 
ATOM   1087 N  NE    . ARG A 1 137 ? 31.004  -21.648 -4.905  1.00 45.46  ? 137 ARG A NE    1 
ATOM   1088 C  CZ    . ARG A 1 137 ? 30.842  -22.319 -3.771  1.00 47.60  ? 137 ARG A CZ    1 
ATOM   1089 N  NH1   . ARG A 1 137 ? 29.645  -22.712 -3.367  1.00 49.42  ? 137 ARG A NH1   1 
ATOM   1090 N  NH2   . ARG A 1 137 ? 31.906  -22.593 -3.019  1.00 45.25  ? 137 ARG A NH2   1 
ATOM   1091 N  N     . THR A 1 138 ? 26.134  -22.506 -9.259  1.00 35.01  ? 138 THR A N     1 
ATOM   1092 C  CA    . THR A 1 138 ? 24.979  -21.982 -9.981  1.00 36.03  ? 138 THR A CA    1 
ATOM   1093 C  C     . THR A 1 138 ? 24.974  -20.460 -9.874  1.00 35.99  ? 138 THR A C     1 
ATOM   1094 O  O     . THR A 1 138 ? 25.184  -19.913 -8.786  1.00 33.79  ? 138 THR A O     1 
ATOM   1095 C  CB    . THR A 1 138 ? 23.676  -22.549 -9.411  1.00 35.82  ? 138 THR A CB    1 
ATOM   1096 O  OG1   . THR A 1 138 ? 23.632  -23.968 -9.603  1.00 40.02  ? 138 THR A OG1   1 
ATOM   1097 C  CG2   . THR A 1 138 ? 22.474  -21.933 -10.111 1.00 36.03  ? 138 THR A CG2   1 
ATOM   1098 N  N     . MET A 1 139 ? 24.756  -19.773 -10.996 1.00 34.05  ? 139 MET A N     1 
ATOM   1099 C  CA    . MET A 1 139 ? 24.495  -18.333 -10.959 1.00 34.27  ? 139 MET A CA    1 
ATOM   1100 C  C     . MET A 1 139 ? 22.988  -18.123 -10.945 1.00 33.31  ? 139 MET A C     1 
ATOM   1101 O  O     . MET A 1 139 ? 22.308  -18.420 -11.937 1.00 34.63  ? 139 MET A O     1 
ATOM   1102 C  CB    . MET A 1 139 ? 25.117  -17.611 -12.155 1.00 35.12  ? 139 MET A CB    1 
ATOM   1103 C  CG    . MET A 1 139 ? 24.588  -16.163 -12.315 1.00 34.80  ? 139 MET A CG    1 
ATOM   1104 S  SD    . MET A 1 139 ? 25.140  -15.383 -13.856 1.00 37.75  ? 139 MET A SD    1 
ATOM   1105 C  CE    . MET A 1 139 ? 26.800  -14.943 -13.370 1.00 35.26  ? 139 MET A CE    1 
ATOM   1106 N  N     . TYR A 1 140 ? 22.468  -17.608 -9.829  1.00 31.01  ? 140 TYR A N     1 
ATOM   1107 C  CA    . TYR A 1 140 ? 21.057  -17.271 -9.696  1.00 27.15  ? 140 TYR A CA    1 
ATOM   1108 C  C     . TYR A 1 140 ? 20.825  -15.850 -10.189 1.00 32.06  ? 140 TYR A C     1 
ATOM   1109 O  O     . TYR A 1 140 ? 21.614  -14.947 -9.899  1.00 28.32  ? 140 TYR A O     1 
ATOM   1110 C  CB    . TYR A 1 140 ? 20.595  -17.378 -8.237  1.00 26.24  ? 140 TYR A CB    1 
ATOM   1111 C  CG    . TYR A 1 140 ? 20.720  -18.766 -7.664  1.00 32.63  ? 140 TYR A CG    1 
ATOM   1112 C  CD1   . TYR A 1 140 ? 19.696  -19.688 -7.816  1.00 32.91  ? 140 TYR A CD1   1 
ATOM   1113 C  CD2   . TYR A 1 140 ? 21.866  -19.159 -6.982  1.00 31.47  ? 140 TYR A CD2   1 
ATOM   1114 C  CE1   . TYR A 1 140 ? 19.803  -20.961 -7.299  1.00 35.75  ? 140 TYR A CE1   1 
ATOM   1115 C  CE2   . TYR A 1 140 ? 21.986  -20.444 -6.469  1.00 34.44  ? 140 TYR A CE2   1 
ATOM   1116 C  CZ    . TYR A 1 140 ? 20.951  -21.336 -6.632  1.00 36.44  ? 140 TYR A CZ    1 
ATOM   1117 O  OH    . TYR A 1 140 ? 21.058  -22.614 -6.125  1.00 43.46  ? 140 TYR A OH    1 
ATOM   1118 N  N     . VAL A 1 141 ? 19.740  -15.662 -10.935 1.00 28.82  ? 141 VAL A N     1 
ATOM   1119 C  CA    . VAL A 1 141 ? 19.372  -14.368 -11.498 1.00 27.63  ? 141 VAL A CA    1 
ATOM   1120 C  C     . VAL A 1 141 ? 18.125  -13.911 -10.754 1.00 31.47  ? 141 VAL A C     1 
ATOM   1121 O  O     . VAL A 1 141 ? 17.042  -14.464 -10.965 1.00 30.85  ? 141 VAL A O     1 
ATOM   1122 C  CB    . VAL A 1 141 ? 19.119  -14.460 -13.011 1.00 29.36  ? 141 VAL A CB    1 
ATOM   1123 C  CG1   . VAL A 1 141 ? 18.679  -13.108 -13.582 1.00 31.19  ? 141 VAL A CG1   1 
ATOM   1124 C  CG2   . VAL A 1 141 ? 20.360  -14.992 -13.722 1.00 27.92  ? 141 VAL A CG2   1 
ATOM   1125 N  N     . ILE A 1 142 ? 18.264  -12.879 -9.922  1.00 30.32  ? 142 ILE A N     1 
ATOM   1126 C  CA    . ILE A 1 142 ? 17.209  -12.410 -9.027  1.00 27.93  ? 142 ILE A CA    1 
ATOM   1127 C  C     . ILE A 1 142 ? 16.624  -11.117 -9.595  1.00 29.92  ? 142 ILE A C     1 
ATOM   1128 O  O     . ILE A 1 142 ? 17.270  -10.069 -9.492  1.00 31.50  ? 142 ILE A O     1 
ATOM   1129 C  CB    . ILE A 1 142 ? 17.749  -12.157 -7.615  1.00 27.39  ? 142 ILE A CB    1 
ATOM   1130 C  CG1   . ILE A 1 142 ? 18.498  -13.374 -7.053  1.00 28.53  ? 142 ILE A CG1   1 
ATOM   1131 C  CG2   . ILE A 1 142 ? 16.618  -11.764 -6.699  1.00 30.85  ? 142 ILE A CG2   1 
ATOM   1132 C  CD1   . ILE A 1 142 ? 19.262  -12.994 -5.749  1.00 28.11  ? 142 ILE A CD1   1 
ATOM   1133 N  N     . PRO A 1 143 ? 15.415  -11.130 -10.157 1.00 29.65  ? 143 PRO A N     1 
ATOM   1134 C  CA    . PRO A 1 143 ? 14.759  -9.871  -10.506 1.00 30.70  ? 143 PRO A CA    1 
ATOM   1135 C  C     . PRO A 1 143 ? 14.006  -9.337  -9.297  1.00 34.84  ? 143 PRO A C     1 
ATOM   1136 O  O     . PRO A 1 143 ? 13.166  -10.057 -8.749  1.00 34.44  ? 143 PRO A O     1 
ATOM   1137 C  CB    . PRO A 1 143 ? 13.803  -10.266 -11.644 1.00 33.99  ? 143 PRO A CB    1 
ATOM   1138 C  CG    . PRO A 1 143 ? 13.790  -11.814 -11.668 1.00 34.72  ? 143 PRO A CG    1 
ATOM   1139 C  CD    . PRO A 1 143 ? 14.572  -12.294 -10.478 1.00 33.55  ? 143 PRO A CD    1 
ATOM   1140 N  N     . PHE A 1 144 ? 14.292  -8.119  -8.838  1.00 31.64  ? 144 PHE A N     1 
ATOM   1141 C  CA    . PHE A 1 144 ? 13.631  -7.652  -7.625  1.00 33.64  ? 144 PHE A CA    1 
ATOM   1142 C  C     . PHE A 1 144 ? 13.229  -6.197  -7.771  1.00 34.45  ? 144 PHE A C     1 
ATOM   1143 O  O     . PHE A 1 144 ? 13.829  -5.442  -8.537  1.00 32.74  ? 144 PHE A O     1 
ATOM   1144 C  CB    . PHE A 1 144 ? 14.512  -7.827  -6.372  1.00 31.49  ? 144 PHE A CB    1 
ATOM   1145 C  CG    . PHE A 1 144 ? 15.768  -7.012  -6.386  1.00 31.54  ? 144 PHE A CG    1 
ATOM   1146 C  CD1   . PHE A 1 144 ? 16.917  -7.500  -6.991  1.00 33.04  ? 144 PHE A CD1   1 
ATOM   1147 C  CD2   . PHE A 1 144 ? 15.810  -5.758  -5.775  1.00 34.84  ? 144 PHE A CD2   1 
ATOM   1148 C  CE1   . PHE A 1 144 ? 18.072  -6.772  -6.997  1.00 29.82  ? 144 PHE A CE1   1 
ATOM   1149 C  CE2   . PHE A 1 144 ? 16.963  -5.008  -5.776  1.00 34.66  ? 144 PHE A CE2   1 
ATOM   1150 C  CZ    . PHE A 1 144 ? 18.101  -5.500  -6.387  1.00 34.67  ? 144 PHE A CZ    1 
ATOM   1151 N  N     . SER A 1 145 ? 12.197  -5.821  -7.019  1.00 33.47  ? 145 SER A N     1 
ATOM   1152 C  CA    . SER A 1 145 ? 11.686  -4.467  -6.990  1.00 35.87  ? 145 SER A CA    1 
ATOM   1153 C  C     . SER A 1 145 ? 11.911  -3.882  -5.601  1.00 37.13  ? 145 SER A C     1 
ATOM   1154 O  O     . SER A 1 145 ? 11.647  -4.546  -4.594  1.00 34.97  ? 145 SER A O     1 
ATOM   1155 C  CB    . SER A 1 145 ? 10.190  -4.453  -7.346  1.00 40.29  ? 145 SER A CB    1 
ATOM   1156 O  OG    . SER A 1 145 ? 9.662   -3.138  -7.297  1.00 51.21  ? 145 SER A OG    1 
ATOM   1157 N  N     . MET A 1 146 ? 12.420  -2.649  -5.545  1.00 39.95  ? 146 MET A N     1 
ATOM   1158 C  CA    . MET A 1 146 ? 12.457  -1.883  -4.301  1.00 38.05  ? 146 MET A CA    1 
ATOM   1159 C  C     . MET A 1 146 ? 11.255  -0.961  -4.330  1.00 43.40  ? 146 MET A C     1 
ATOM   1160 O  O     . MET A 1 146 ? 11.171  -0.072  -5.185  1.00 42.67  ? 146 MET A O     1 
ATOM   1161 C  CB    . MET A 1 146 ? 13.751  -1.091  -4.139  1.00 41.20  ? 146 MET A CB    1 
ATOM   1162 C  CG    . MET A 1 146 ? 15.004  -1.954  -4.121  1.00 38.20  ? 146 MET A CG    1 
ATOM   1163 S  SD    . MET A 1 146 ? 14.904  -3.329  -2.968  1.00 36.40  ? 146 MET A SD    1 
ATOM   1164 C  CE    . MET A 1 146 ? 15.090  -2.543  -1.375  1.00 37.17  ? 146 MET A CE    1 
ATOM   1165 N  N     . GLY A 1 147 ? 10.317  -1.188  -3.417  1.00 45.04  ? 147 GLY A N     1 
ATOM   1166 C  CA    . GLY A 1 147 ? 9.062   -0.482  -3.433  1.00 45.89  ? 147 GLY A CA    1 
ATOM   1167 C  C     . GLY A 1 147 ? 7.982   -1.326  -4.077  1.00 52.38  ? 147 GLY A C     1 
ATOM   1168 O  O     . GLY A 1 147 ? 8.268   -2.287  -4.796  1.00 50.10  ? 147 GLY A O     1 
ATOM   1169 N  N     . PRO A 1 148 ? 6.717   -0.982  -3.825  1.00 57.69  ? 148 PRO A N     1 
ATOM   1170 C  CA    . PRO A 1 148 ? 5.607   -1.794  -4.340  1.00 62.29  ? 148 PRO A CA    1 
ATOM   1171 C  C     . PRO A 1 148 ? 5.694   -1.996  -5.849  1.00 68.66  ? 148 PRO A C     1 
ATOM   1172 O  O     . PRO A 1 148 ? 5.967   -1.067  -6.610  1.00 71.96  ? 148 PRO A O     1 
ATOM   1173 C  CB    . PRO A 1 148 ? 4.366   -0.984  -3.946  1.00 61.89  ? 148 PRO A CB    1 
ATOM   1174 C  CG    . PRO A 1 148 ? 4.792   -0.233  -2.732  1.00 59.09  ? 148 PRO A CG    1 
ATOM   1175 C  CD    . PRO A 1 148 ? 6.246   0.113   -2.957  1.00 56.15  ? 148 PRO A CD    1 
ATOM   1176 N  N     . LEU A 1 149 ? 5.463   -3.237  -6.269  1.00 79.22  ? 149 LEU A N     1 
ATOM   1177 C  CA    . LEU A 1 149 ? 5.607   -3.604  -7.669  1.00 79.22  ? 149 LEU A CA    1 
ATOM   1178 C  C     . LEU A 1 149 ? 4.654   -2.801  -8.543  1.00 87.77  ? 149 LEU A C     1 
ATOM   1179 O  O     . LEU A 1 149 ? 3.528   -2.487  -8.145  1.00 90.33  ? 149 LEU A O     1 
ATOM   1180 C  CB    . LEU A 1 149 ? 5.348   -5.100  -7.836  1.00 82.80  ? 149 LEU A CB    1 
ATOM   1181 C  CG    . LEU A 1 149 ? 5.309   -5.656  -9.255  1.00 80.22  ? 149 LEU A CG    1 
ATOM   1182 C  CD1   . LEU A 1 149 ? 6.650   -5.454  -9.934  1.00 78.37  ? 149 LEU A CD1   1 
ATOM   1183 C  CD2   . LEU A 1 149 ? 4.929   -7.118  -9.216  1.00 76.50  ? 149 LEU A CD2   1 
ATOM   1184 N  N     . GLY A 1 150 ? 5.119   -2.456  -9.744  1.00 84.98  ? 150 GLY A N     1 
ATOM   1185 C  CA    . GLY A 1 150 ? 4.332   -1.666  -10.664 1.00 83.27  ? 150 GLY A CA    1 
ATOM   1186 C  C     . GLY A 1 150 ? 4.156   -0.219  -10.279 1.00 87.27  ? 150 GLY A C     1 
ATOM   1187 O  O     . GLY A 1 150 ? 3.723   0.578   -11.123 1.00 89.85  ? 150 GLY A O     1 
ATOM   1188 N  N     . SER A 1 151 ? 4.463   0.155   -9.038  1.00 86.16  ? 151 SER A N     1 
ATOM   1189 C  CA    . SER A 1 151 ? 4.380   1.551   -8.649  1.00 85.40  ? 151 SER A CA    1 
ATOM   1190 C  C     . SER A 1 151 ? 5.362   2.372   -9.482  1.00 86.42  ? 151 SER A C     1 
ATOM   1191 O  O     . SER A 1 151 ? 6.422   1.872   -9.875  1.00 82.92  ? 151 SER A O     1 
ATOM   1192 C  CB    . SER A 1 151 ? 4.683   1.714   -7.160  1.00 79.15  ? 151 SER A CB    1 
ATOM   1193 O  OG    . SER A 1 151 ? 4.659   3.079   -6.780  1.00 79.44  ? 151 SER A OG    1 
ATOM   1194 N  N     . PRO A 1 152 ? 5.020   3.625   -9.796  1.00 91.31  ? 152 PRO A N     1 
ATOM   1195 C  CA    . PRO A 1 152 ? 5.958   4.463   -10.561 1.00 90.68  ? 152 PRO A CA    1 
ATOM   1196 C  C     . PRO A 1 152 ? 7.217   4.819   -9.790  1.00 90.39  ? 152 PRO A C     1 
ATOM   1197 O  O     . PRO A 1 152 ? 8.255   5.083   -10.410 1.00 92.53  ? 152 PRO A O     1 
ATOM   1198 C  CB    . PRO A 1 152 ? 5.125   5.712   -10.890 1.00 92.03  ? 152 PRO A CB    1 
ATOM   1199 C  CG    . PRO A 1 152 ? 3.699   5.261   -10.779 1.00 94.46  ? 152 PRO A CG    1 
ATOM   1200 C  CD    . PRO A 1 152 ? 3.694   4.251   -9.671  1.00 92.95  ? 152 PRO A CD    1 
ATOM   1201 N  N     . LEU A 1 153 ? 7.163   4.834   -8.461  1.00 78.57  ? 153 LEU A N     1 
ATOM   1202 C  CA    . LEU A 1 153 ? 8.305   5.217   -7.642  1.00 74.40  ? 153 LEU A CA    1 
ATOM   1203 C  C     . LEU A 1 153 ? 9.192   4.033   -7.281  1.00 67.09  ? 153 LEU A C     1 
ATOM   1204 O  O     . LEU A 1 153 ? 10.230  4.219   -6.635  1.00 56.51  ? 153 LEU A O     1 
ATOM   1205 C  CB    . LEU A 1 153 ? 7.814   5.910   -6.374  1.00 68.26  ? 153 LEU A CB    1 
ATOM   1206 C  CG    . LEU A 1 153 ? 6.600   6.788   -6.676  1.00 76.72  ? 153 LEU A CG    1 
ATOM   1207 C  CD1   . LEU A 1 153 ? 5.983   7.318   -5.397  1.00 70.55  ? 153 LEU A CD1   1 
ATOM   1208 C  CD2   . LEU A 1 153 ? 6.963   7.935   -7.621  1.00 82.65  ? 153 LEU A CD2   1 
ATOM   1209 N  N     . ALA A 1 154 ? 8.808   2.827   -7.679  1.00 66.26  ? 154 ALA A N     1 
ATOM   1210 C  CA    . ALA A 1 154 ? 9.647   1.669   -7.434  1.00 57.66  ? 154 ALA A CA    1 
ATOM   1211 C  C     . ALA A 1 154 ? 10.888  1.723   -8.317  1.00 53.19  ? 154 ALA A C     1 
ATOM   1212 O  O     . ALA A 1 154 ? 10.888  2.327   -9.394  1.00 53.54  ? 154 ALA A O     1 
ATOM   1213 C  CB    . ALA A 1 154 ? 8.866   0.384   -7.695  1.00 59.78  ? 154 ALA A CB    1 
ATOM   1214 N  N     . LYS A 1 155 ? 11.960  1.096   -7.839  1.00 48.11  ? 155 LYS A N     1 
ATOM   1215 C  CA    . LYS A 1 155 ? 13.189  0.920   -8.598  1.00 40.81  ? 155 LYS A CA    1 
ATOM   1216 C  C     . LYS A 1 155 ? 13.478  -0.572  -8.688  1.00 42.13  ? 155 LYS A C     1 
ATOM   1217 O  O     . LYS A 1 155 ? 13.372  -1.292  -7.685  1.00 41.10  ? 155 LYS A O     1 
ATOM   1218 C  CB    . LYS A 1 155 ? 14.359  1.659   -7.946  1.00 37.06  ? 155 LYS A CB    1 
ATOM   1219 C  CG    . LYS A 1 155 ? 14.181  3.202   -7.857  1.00 43.96  ? 155 LYS A CG    1 
ATOM   1220 C  CD    . LYS A 1 155 ? 14.454  3.892   -9.182  1.00 43.69  ? 155 LYS A CD    1 
ATOM   1221 C  CE    . LYS A 1 155 ? 14.259  5.424   -9.088  1.00 52.10  ? 155 LYS A CE    1 
ATOM   1222 N  NZ    . LYS A 1 155 ? 12.823  5.843   -9.170  1.00 59.90  ? 155 LYS A NZ    1 
ATOM   1223 N  N     . ILE A 1 156 ? 13.835  -1.035  -9.881  1.00 37.71  ? 156 ILE A N     1 
ATOM   1224 C  CA    . ILE A 1 156 ? 14.027  -2.456  -10.159 1.00 37.86  ? 156 ILE A CA    1 
ATOM   1225 C  C     . ILE A 1 156 ? 15.518  -2.741  -10.306 1.00 38.26  ? 156 ILE A C     1 
ATOM   1226 O  O     . ILE A 1 156 ? 16.259  -1.931  -10.870 1.00 36.95  ? 156 ILE A O     1 
ATOM   1227 C  CB    . ILE A 1 156 ? 13.238  -2.861  -11.422 1.00 38.48  ? 156 ILE A CB    1 
ATOM   1228 C  CG1   . ILE A 1 156 ? 11.744  -2.917  -11.101 1.00 41.16  ? 156 ILE A CG1   1 
ATOM   1229 C  CG2   . ILE A 1 156 ? 13.716  -4.192  -11.984 1.00 37.11  ? 156 ILE A CG2   1 
ATOM   1230 C  CD1   . ILE A 1 156 ? 10.838  -2.997  -12.320 1.00 45.74  ? 156 ILE A CD1   1 
ATOM   1231 N  N     . GLY A 1 157 ? 15.966  -3.881  -9.764  1.00 34.54  ? 157 GLY A N     1 
ATOM   1232 C  CA    . GLY A 1 157 ? 17.323  -4.334  -9.963  1.00 35.10  ? 157 GLY A CA    1 
ATOM   1233 C  C     . GLY A 1 157 ? 17.339  -5.788  -10.411 1.00 33.68  ? 157 GLY A C     1 
ATOM   1234 O  O     . GLY A 1 157 ? 16.321  -6.481  -10.370 1.00 31.02  ? 157 GLY A O     1 
ATOM   1235 N  N     . ILE A 1 158 ? 18.504  -6.221  -10.882 1.00 34.64  ? 158 ILE A N     1 
ATOM   1236 C  CA    . ILE A 1 158 ? 18.796  -7.626  -11.166 1.00 31.02  ? 158 ILE A CA    1 
ATOM   1237 C  C     . ILE A 1 158 ? 20.032  -7.965  -10.354 1.00 31.19  ? 158 ILE A C     1 
ATOM   1238 O  O     . ILE A 1 158 ? 21.075  -7.335  -10.550 1.00 34.59  ? 158 ILE A O     1 
ATOM   1239 C  CB    . ILE A 1 158 ? 19.070  -7.878  -12.660 1.00 32.94  ? 158 ILE A CB    1 
ATOM   1240 C  CG1   . ILE A 1 158 ? 17.951  -7.334  -13.551 1.00 36.83  ? 158 ILE A CG1   1 
ATOM   1241 C  CG2   . ILE A 1 158 ? 19.335  -9.381  -12.919 1.00 32.67  ? 158 ILE A CG2   1 
ATOM   1242 C  CD1   . ILE A 1 158 ? 16.737  -8.181  -13.604 1.00 36.86  ? 158 ILE A CD1   1 
ATOM   1243 N  N     . GLU A 1 159 ? 19.932  -8.926  -9.431  1.00 28.55  ? 159 GLU A N     1 
ATOM   1244 C  CA    . GLU A 1 159 ? 21.129  -9.397  -8.741  1.00 25.64  ? 159 GLU A CA    1 
ATOM   1245 C  C     . GLU A 1 159 ? 21.538  -10.777 -9.248  1.00 30.68  ? 159 GLU A C     1 
ATOM   1246 O  O     . GLU A 1 159 ? 20.732  -11.716 -9.252  1.00 31.56  ? 159 GLU A O     1 
ATOM   1247 C  CB    . GLU A 1 159 ? 20.973  -9.441  -7.219  1.00 27.72  ? 159 GLU A CB    1 
ATOM   1248 C  CG    . GLU A 1 159 ? 22.234  -10.014 -6.550  1.00 26.97  ? 159 GLU A CG    1 
ATOM   1249 C  CD    . GLU A 1 159 ? 22.295  -9.782  -5.035  1.00 31.93  ? 159 GLU A CD    1 
ATOM   1250 O  OE1   . GLU A 1 159 ? 21.507  -8.965  -4.535  1.00 33.31  ? 159 GLU A OE1   1 
ATOM   1251 O  OE2   . GLU A 1 159 ? 23.161  -10.381 -4.355  1.00 28.92  ? 159 GLU A OE2   1 
ATOM   1252 N  N     . LEU A 1 160 ? 22.796  -10.887 -9.672  1.00 28.61  ? 160 LEU A N     1 
ATOM   1253 C  CA    . LEU A 1 160 ? 23.435  -12.159 -9.957  1.00 30.65  ? 160 LEU A CA    1 
ATOM   1254 C  C     . LEU A 1 160 ? 24.205  -12.570 -8.711  1.00 31.09  ? 160 LEU A C     1 
ATOM   1255 O  O     . LEU A 1 160 ? 24.930  -11.755 -8.141  1.00 31.52  ? 160 LEU A O     1 
ATOM   1256 C  CB    . LEU A 1 160 ? 24.393  -12.042 -11.150 1.00 29.71  ? 160 LEU A CB    1 
ATOM   1257 C  CG    . LEU A 1 160 ? 23.888  -11.275 -12.364 1.00 31.18  ? 160 LEU A CG    1 
ATOM   1258 C  CD1   . LEU A 1 160 ? 24.938  -11.266 -13.492 1.00 32.56  ? 160 LEU A CD1   1 
ATOM   1259 C  CD2   . LEU A 1 160 ? 22.555  -11.834 -12.841 1.00 30.98  ? 160 LEU A CD2   1 
ATOM   1260 N  N     . THR A 1 161 ? 24.047  -13.823 -8.287  1.00 29.41  ? 161 THR A N     1 
ATOM   1261 C  CA    . THR A 1 161 ? 24.749  -14.298 -7.107  1.00 29.34  ? 161 THR A CA    1 
ATOM   1262 C  C     . THR A 1 161 ? 24.944  -15.796 -7.248  1.00 30.75  ? 161 THR A C     1 
ATOM   1263 O  O     . THR A 1 161 ? 24.213  -16.473 -7.981  1.00 29.82  ? 161 THR A O     1 
ATOM   1264 C  CB    . THR A 1 161 ? 23.989  -13.973 -5.797  1.00 29.00  ? 161 THR A CB    1 
ATOM   1265 O  OG1   . THR A 1 161 ? 24.670  -14.581 -4.683  1.00 30.33  ? 161 THR A OG1   1 
ATOM   1266 C  CG2   . THR A 1 161 ? 22.566  -14.526 -5.831  1.00 27.24  ? 161 THR A CG2   1 
ATOM   1267 N  N     . ASP A 1 162 ? 25.949  -16.318 -6.550  1.00 31.19  ? 162 ASP A N     1 
ATOM   1268 C  CA    . ASP A 1 162 ? 26.155  -17.759 -6.532  1.00 29.94  ? 162 ASP A CA    1 
ATOM   1269 C  C     . ASP A 1 162 ? 25.762  -18.384 -5.200  1.00 33.21  ? 162 ASP A C     1 
ATOM   1270 O  O     . ASP A 1 162 ? 26.094  -19.547 -4.945  1.00 34.03  ? 162 ASP A O     1 
ATOM   1271 C  CB    . ASP A 1 162 ? 27.600  -18.120 -6.887  1.00 32.50  ? 162 ASP A CB    1 
ATOM   1272 C  CG    . ASP A 1 162 ? 28.626  -17.377 -6.046  1.00 32.21  ? 162 ASP A CG    1 
ATOM   1273 O  OD1   . ASP A 1 162 ? 28.244  -16.679 -5.089  1.00 30.67  ? 162 ASP A OD1   1 
ATOM   1274 O  OD2   . ASP A 1 162 ? 29.829  -17.491 -6.366  1.00 38.82  ? 162 ASP A OD2   1 
ATOM   1275 N  N     . SER A 1 163 ? 25.014  -17.661 -4.372  1.00 35.45  ? 163 SER A N     1 
ATOM   1276 C  CA    . SER A 1 163 ? 24.659  -18.127 -3.039  1.00 32.68  ? 163 SER A CA    1 
ATOM   1277 C  C     . SER A 1 163 ? 23.160  -18.350 -2.925  1.00 29.06  ? 163 SER A C     1 
ATOM   1278 O  O     . SER A 1 163 ? 22.396  -17.384 -3.038  1.00 30.86  ? 163 SER A O     1 
ATOM   1279 C  CB    . SER A 1 163 ? 25.116  -17.107 -2.001  1.00 34.18  ? 163 SER A CB    1 
ATOM   1280 O  OG    . SER A 1 163 ? 24.443  -17.323 -0.773  1.00 34.82  ? 163 SER A OG    1 
ATOM   1281 N  N     . PRO A 1 164 ? 22.693  -19.578 -2.669  1.00 31.88  ? 164 PRO A N     1 
ATOM   1282 C  CA    . PRO A 1 164 ? 21.255  -19.780 -2.403  1.00 31.50  ? 164 PRO A CA    1 
ATOM   1283 C  C     . PRO A 1 164 ? 20.760  -19.062 -1.155  1.00 33.02  ? 164 PRO A C     1 
ATOM   1284 O  O     . PRO A 1 164 ? 19.572  -18.710 -1.088  1.00 30.31  ? 164 PRO A O     1 
ATOM   1285 C  CB    . PRO A 1 164 ? 21.131  -21.309 -2.263  1.00 31.42  ? 164 PRO A CB    1 
ATOM   1286 C  CG    . PRO A 1 164 ? 22.502  -21.776 -1.934  1.00 37.26  ? 164 PRO A CG    1 
ATOM   1287 C  CD    . PRO A 1 164 ? 23.447  -20.847 -2.643  1.00 31.96  ? 164 PRO A CD    1 
ATOM   1288 N  N     . TYR A 1 165 ? 21.633  -18.824 -0.170  1.00 31.81  ? 165 TYR A N     1 
ATOM   1289 C  CA    . TYR A 1 165 ? 21.244  -18.058 1.016   1.00 30.69  ? 165 TYR A CA    1 
ATOM   1290 C  C     . TYR A 1 165 ? 20.843  -16.627 0.652   1.00 32.53  ? 165 TYR A C     1 
ATOM   1291 O  O     . TYR A 1 165 ? 19.896  -16.065 1.225   1.00 30.09  ? 165 TYR A O     1 
ATOM   1292 C  CB    . TYR A 1 165 ? 22.404  -18.060 2.021   1.00 33.16  ? 165 TYR A CB    1 
ATOM   1293 C  CG    . TYR A 1 165 ? 22.222  -17.113 3.202   1.00 36.29  ? 165 TYR A CG    1 
ATOM   1294 C  CD1   . TYR A 1 165 ? 21.595  -17.543 4.373   1.00 31.78  ? 165 TYR A CD1   1 
ATOM   1295 C  CD2   . TYR A 1 165 ? 22.695  -15.802 3.154   1.00 32.86  ? 165 TYR A CD2   1 
ATOM   1296 C  CE1   . TYR A 1 165 ? 21.435  -16.697 5.452   1.00 34.62  ? 165 TYR A CE1   1 
ATOM   1297 C  CE2   . TYR A 1 165 ? 22.529  -14.939 4.233   1.00 34.92  ? 165 TYR A CE2   1 
ATOM   1298 C  CZ    . TYR A 1 165 ? 21.901  -15.396 5.378   1.00 35.70  ? 165 TYR A CZ    1 
ATOM   1299 O  OH    . TYR A 1 165 ? 21.734  -14.567 6.458   1.00 34.29  ? 165 TYR A OH    1 
ATOM   1300 N  N     . VAL A 1 166 ? 21.568  -16.009 -0.285  1.00 29.28  ? 166 VAL A N     1 
ATOM   1301 C  CA    . VAL A 1 166 ? 21.194  -14.675 -0.755  1.00 26.55  ? 166 VAL A CA    1 
ATOM   1302 C  C     . VAL A 1 166 ? 19.846  -14.726 -1.454  1.00 28.48  ? 166 VAL A C     1 
ATOM   1303 O  O     . VAL A 1 166 ? 18.977  -13.887 -1.215  1.00 27.90  ? 166 VAL A O     1 
ATOM   1304 C  CB    . VAL A 1 166 ? 22.304  -14.121 -1.675  1.00 30.45  ? 166 VAL A CB    1 
ATOM   1305 C  CG1   . VAL A 1 166 ? 21.862  -12.848 -2.395  1.00 29.69  ? 166 VAL A CG1   1 
ATOM   1306 C  CG2   . VAL A 1 166 ? 23.572  -13.883 -0.867  1.00 30.79  ? 166 VAL A CG2   1 
ATOM   1307 N  N     . VAL A 1 167 ? 19.623  -15.745 -2.290  1.00 26.82  ? 167 VAL A N     1 
ATOM   1308 C  CA    . VAL A 1 167 ? 18.343  -15.853 -2.996  1.00 28.46  ? 167 VAL A CA    1 
ATOM   1309 C  C     . VAL A 1 167 ? 17.181  -15.921 -2.000  1.00 29.83  ? 167 VAL A C     1 
ATOM   1310 O  O     . VAL A 1 167 ? 16.181  -15.200 -2.128  1.00 31.41  ? 167 VAL A O     1 
ATOM   1311 C  CB    . VAL A 1 167 ? 18.345  -17.082 -3.933  1.00 27.47  ? 167 VAL A CB    1 
ATOM   1312 C  CG1   . VAL A 1 167 ? 16.983  -17.196 -4.655  1.00 28.35  ? 167 VAL A CG1   1 
ATOM   1313 C  CG2   . VAL A 1 167 ? 19.499  -16.995 -4.939  1.00 29.59  ? 167 VAL A CG2   1 
ATOM   1314 N  N     . ALA A 1 168 ? 17.287  -16.796 -0.999  1.00 29.53  ? 168 ALA A N     1 
ATOM   1315 C  CA    . ALA A 1 168 ? 16.184  -16.973 -0.050  1.00 30.20  ? 168 ALA A CA    1 
ATOM   1316 C  C     . ALA A 1 168 ? 15.911  -15.690 0.734   1.00 30.11  ? 168 ALA A C     1 
ATOM   1317 O  O     . ALA A 1 168 ? 14.749  -15.331 0.978   1.00 30.08  ? 168 ALA A O     1 
ATOM   1318 C  CB    . ALA A 1 168 ? 16.504  -18.115 0.910   1.00 29.55  ? 168 ALA A CB    1 
ATOM   1319 N  N     . SER A 1 169 ? 16.972  -15.001 1.159   1.00 27.64  ? 169 SER A N     1 
ATOM   1320 C  CA    . SER A 1 169 ? 16.800  -13.779 1.938   1.00 29.43  ? 169 SER A CA    1 
ATOM   1321 C  C     . SER A 1 169 ? 16.240  -12.647 1.080   1.00 32.20  ? 169 SER A C     1 
ATOM   1322 O  O     . SER A 1 169 ? 15.466  -11.814 1.570   1.00 30.42  ? 169 SER A O     1 
ATOM   1323 C  CB    . SER A 1 169 ? 18.138  -13.365 2.558   1.00 31.94  ? 169 SER A CB    1 
ATOM   1324 O  OG    . SER A 1 169 ? 18.711  -14.429 3.299   1.00 32.64  ? 169 SER A OG    1 
ATOM   1325 N  N     . MET A 1 170 ? 16.640  -12.580 -0.197  1.00 25.06  ? 170 MET A N     1 
ATOM   1326 C  CA    . MET A 1 170 ? 16.095  -11.561 -1.099  1.00 26.32  ? 170 MET A CA    1 
ATOM   1327 C  C     . MET A 1 170 ? 14.606  -11.773 -1.352  1.00 27.52  ? 170 MET A C     1 
ATOM   1328 O  O     . MET A 1 170 ? 13.870  -10.815 -1.609  1.00 28.71  ? 170 MET A O     1 
ATOM   1329 C  CB    . MET A 1 170 ? 16.868  -11.576 -2.429  1.00 26.02  ? 170 MET A CB    1 
ATOM   1330 C  CG    . MET A 1 170 ? 18.291  -10.981 -2.345  1.00 27.61  ? 170 MET A CG    1 
ATOM   1331 S  SD    . MET A 1 170 ? 18.303  -9.170  -2.085  1.00 34.02  ? 170 MET A SD    1 
ATOM   1332 C  CE    . MET A 1 170 ? 17.851  -8.566  -3.719  1.00 29.03  ? 170 MET A CE    1 
ATOM   1333 N  N     . ARG A 1 171 ? 14.148  -13.016 -1.297  1.00 29.80  ? 171 ARG A N     1 
ATOM   1334 C  CA    . ARG A 1 171 ? 12.725  -13.286 -1.443  1.00 30.24  ? 171 ARG A CA    1 
ATOM   1335 C  C     . ARG A 1 171 ? 11.942  -12.703 -0.280  1.00 29.98  ? 171 ARG A C     1 
ATOM   1336 O  O     . ARG A 1 171 ? 10.782  -12.301 -0.445  1.00 33.01  ? 171 ARG A O     1 
ATOM   1337 C  CB    . ARG A 1 171 ? 12.495  -14.803 -1.553  1.00 31.82  ? 171 ARG A CB    1 
ATOM   1338 C  CG    . ARG A 1 171 ? 11.023  -15.166 -1.760  1.00 36.97  ? 171 ARG A CG    1 
ATOM   1339 C  CD    . ARG A 1 171 ? 10.796  -16.686 -1.917  1.00 37.26  ? 171 ARG A CD    1 
ATOM   1340 N  NE    . ARG A 1 171 ? 9.487   -16.938 -2.510  1.00 38.55  ? 171 ARG A NE    1 
ATOM   1341 C  CZ    . ARG A 1 171 ? 8.348   -17.001 -1.832  1.00 43.80  ? 171 ARG A CZ    1 
ATOM   1342 N  NH1   . ARG A 1 171 ? 8.322   -16.927 -0.511  1.00 46.05  ? 171 ARG A NH1   1 
ATOM   1343 N  NH2   . ARG A 1 171 ? 7.204   -17.133 -2.496  1.00 43.03  ? 171 ARG A NH2   1 
ATOM   1344 N  N     . ILE A 1 172 ? 12.559  -12.632 0.895   1.00 30.17  ? 172 ILE A N     1 
ATOM   1345 C  CA    . ILE A 1 172 ? 11.882  -12.054 2.048   1.00 32.15  ? 172 ILE A CA    1 
ATOM   1346 C  C     . ILE A 1 172 ? 12.025  -10.536 2.054   1.00 32.34  ? 172 ILE A C     1 
ATOM   1347 O  O     . ILE A 1 172 ? 11.063  -9.812  2.316   1.00 33.12  ? 172 ILE A O     1 
ATOM   1348 C  CB    . ILE A 1 172 ? 12.424  -12.679 3.351   1.00 34.10  ? 172 ILE A CB    1 
ATOM   1349 C  CG1   . ILE A 1 172 ? 12.070  -14.166 3.432   1.00 33.02  ? 172 ILE A CG1   1 
ATOM   1350 C  CG2   . ILE A 1 172 ? 11.868  -11.956 4.579   1.00 33.81  ? 172 ILE A CG2   1 
ATOM   1351 C  CD1   . ILE A 1 172 ? 12.877  -14.904 4.466   1.00 35.17  ? 172 ILE A CD1   1 
ATOM   1352 N  N     . MET A 1 173 ? 13.213  -10.031 1.754   1.00 31.98  ? 173 MET A N     1 
ATOM   1353 C  CA    . MET A 1 173 ? 13.503  -8.617  1.946   1.00 30.24  ? 173 MET A CA    1 
ATOM   1354 C  C     . MET A 1 173 ? 13.106  -7.739  0.762   1.00 33.26  ? 173 MET A C     1 
ATOM   1355 O  O     . MET A 1 173 ? 13.085  -6.508  0.903   1.00 34.45  ? 173 MET A O     1 
ATOM   1356 C  CB    . MET A 1 173 ? 14.996  -8.449  2.239   1.00 30.68  ? 173 MET A CB    1 
ATOM   1357 C  CG    . MET A 1 173 ? 15.427  -9.090  3.546   1.00 30.00  ? 173 MET A CG    1 
ATOM   1358 S  SD    . MET A 1 173 ? 14.504  -8.392  4.919   1.00 30.74  ? 173 MET A SD    1 
ATOM   1359 C  CE    . MET A 1 173 ? 14.880  -6.650  4.686   1.00 30.41  ? 173 MET A CE    1 
ATOM   1360 N  N     . THR A 1 174 ? 12.806  -8.320  -0.398  1.00 30.65  ? 174 THR A N     1 
ATOM   1361 C  CA    . THR A 1 174 ? 12.366  -7.554  -1.556  1.00 30.56  ? 174 THR A CA    1 
ATOM   1362 C  C     . THR A 1 174 ? 11.144  -8.228  -2.167  1.00 31.31  ? 174 THR A C     1 
ATOM   1363 O  O     . THR A 1 174 ? 10.753  -9.332  -1.778  1.00 36.19  ? 174 THR A O     1 
ATOM   1364 C  CB    . THR A 1 174 ? 13.485  -7.435  -2.608  1.00 31.77  ? 174 THR A CB    1 
ATOM   1365 O  OG1   . THR A 1 174 ? 13.742  -8.729  -3.178  1.00 29.95  ? 174 THR A OG1   1 
ATOM   1366 C  CG2   . THR A 1 174 ? 14.774  -6.916  -1.977  1.00 31.65  ? 174 THR A CG2   1 
ATOM   1367 N  N     . ARG A 1 175 ? 10.525  -7.552  -3.127  1.00 32.10  ? 175 ARG A N     1 
ATOM   1368 C  CA    . ARG A 1 175 ? 9.542   -8.190  -3.998  1.00 34.60  ? 175 ARG A CA    1 
ATOM   1369 C  C     . ARG A 1 175 ? 10.285  -8.782  -5.191  1.00 34.37  ? 175 ARG A C     1 
ATOM   1370 O  O     . ARG A 1 175 ? 10.929  -8.046  -5.944  1.00 34.58  ? 175 ARG A O     1 
ATOM   1371 C  CB    . ARG A 1 175 ? 8.496   -7.179  -4.450  1.00 37.49  ? 175 ARG A CB    1 
ATOM   1372 C  CG    . ARG A 1 175 ? 7.590   -6.735  -3.321  1.00 42.50  ? 175 ARG A CG    1 
ATOM   1373 C  CD    . ARG A 1 175 ? 7.479   -5.255  -3.274  1.00 45.00  ? 175 ARG A CD    1 
ATOM   1374 N  NE    . ARG A 1 175 ? 6.524   -4.814  -2.267  1.00 45.75  ? 175 ARG A NE    1 
ATOM   1375 C  CZ    . ARG A 1 175 ? 6.850   -4.072  -1.218  1.00 48.04  ? 175 ARG A CZ    1 
ATOM   1376 N  NH1   . ARG A 1 175 ? 8.099   -3.692  -1.005  1.00 39.89  ? 175 ARG A NH1   1 
ATOM   1377 N  NH2   . ARG A 1 175 ? 5.899   -3.706  -0.359  1.00 49.37  ? 175 ARG A NH2   1 
ATOM   1378 N  N     . MET A 1 176 ? 10.194  -10.104 -5.367  1.00 34.31  ? 176 MET A N     1 
ATOM   1379 C  CA    . MET A 1 176 ? 11.131  -10.831 -6.213  1.00 34.94  ? 176 MET A CA    1 
ATOM   1380 C  C     . MET A 1 176 ? 10.406  -11.803 -7.135  1.00 38.19  ? 176 MET A C     1 
ATOM   1381 O  O     . MET A 1 176 ? 9.464   -12.478 -6.709  1.00 37.34  ? 176 MET A O     1 
ATOM   1382 C  CB    . MET A 1 176 ? 12.119  -11.607 -5.319  1.00 34.65  ? 176 MET A CB    1 
ATOM   1383 C  CG    . MET A 1 176 ? 13.301  -12.208 -6.028  1.00 37.71  ? 176 MET A CG    1 
ATOM   1384 S  SD    . MET A 1 176 ? 13.089  -13.876 -6.666  1.00 44.47  ? 176 MET A SD    1 
ATOM   1385 C  CE    . MET A 1 176 ? 13.495  -14.883 -5.239  1.00 39.56  ? 176 MET A CE    1 
ATOM   1386 N  N     . GLY A 1 177 ? 10.856  -11.886 -8.397  1.00 35.92  ? 177 GLY A N     1 
ATOM   1387 C  CA    . GLY A 1 177 ? 10.504  -12.989 -9.279  1.00 37.34  ? 177 GLY A CA    1 
ATOM   1388 C  C     . GLY A 1 177 ? 9.958   -12.525 -10.623 1.00 40.82  ? 177 GLY A C     1 
ATOM   1389 O  O     . GLY A 1 177 ? 10.275  -11.430 -11.103 1.00 39.18  ? 177 GLY A O     1 
ATOM   1390 N  N     . THR A 1 178 ? 9.107   -13.372 -11.212 1.00 39.85  ? 178 THR A N     1 
ATOM   1391 C  CA    . THR A 1 178 ? 8.760   -13.244 -12.626 1.00 42.45  ? 178 THR A CA    1 
ATOM   1392 C  C     . THR A 1 178 ? 7.975   -11.969 -12.900 1.00 47.40  ? 178 THR A C     1 
ATOM   1393 O  O     . THR A 1 178 ? 8.185   -11.310 -13.925 1.00 44.94  ? 178 THR A O     1 
ATOM   1394 C  CB    . THR A 1 178 ? 7.961   -14.475 -13.082 1.00 41.14  ? 178 THR A CB    1 
ATOM   1395 O  OG1   . THR A 1 178 ? 8.804   -15.631 -13.049 1.00 43.12  ? 178 THR A OG1   1 
ATOM   1396 C  CG2   . THR A 1 178 ? 7.431   -14.295 -14.490 1.00 45.45  ? 178 THR A CG2   1 
ATOM   1397 N  N     . SER A 1 179 ? 7.073   -11.598 -11.991 1.00 46.17  ? 179 SER A N     1 
ATOM   1398 C  CA    . SER A 1 179 ? 6.251   -10.419 -12.221 1.00 48.97  ? 179 SER A CA    1 
ATOM   1399 C  C     . SER A 1 179 ? 7.093   -9.145  -12.270 1.00 51.22  ? 179 SER A C     1 
ATOM   1400 O  O     . SER A 1 179 ? 6.696   -8.168  -12.915 1.00 49.79  ? 179 SER A O     1 
ATOM   1401 C  CB    . SER A 1 179 ? 5.182   -10.323 -11.140 1.00 46.29  ? 179 SER A CB    1 
ATOM   1402 O  OG    . SER A 1 179 ? 5.789   -10.048 -9.890  1.00 59.05  ? 179 SER A OG    1 
ATOM   1403 N  N     . VAL A 1 180 ? 8.257   -9.140  -11.614 1.00 46.32  ? 180 VAL A N     1 
ATOM   1404 C  CA    . VAL A 1 180 ? 9.142   -7.980  -11.684 1.00 46.03  ? 180 VAL A CA    1 
ATOM   1405 C  C     . VAL A 1 180 ? 9.712   -7.825  -13.091 1.00 47.80  ? 180 VAL A C     1 
ATOM   1406 O  O     . VAL A 1 180 ? 9.769   -6.717  -13.635 1.00 48.87  ? 180 VAL A O     1 
ATOM   1407 C  CB    . VAL A 1 180 ? 10.254  -8.098  -10.623 1.00 40.79  ? 180 VAL A CB    1 
ATOM   1408 C  CG1   . VAL A 1 180 ? 11.268  -6.984  -10.784 1.00 42.83  ? 180 VAL A CG1   1 
ATOM   1409 C  CG2   . VAL A 1 180 ? 9.650   -8.062  -9.225  1.00 42.72  ? 180 VAL A CG2   1 
ATOM   1410 N  N     . LEU A 1 181 ? 10.145  -8.930  -13.706 1.00 46.44  ? 181 LEU A N     1 
ATOM   1411 C  CA    . LEU A 1 181 ? 10.628  -8.870  -15.084 1.00 48.07  ? 181 LEU A CA    1 
ATOM   1412 C  C     . LEU A 1 181 ? 9.559   -8.316  -16.014 1.00 51.58  ? 181 LEU A C     1 
ATOM   1413 O  O     . LEU A 1 181 ? 9.857   -7.543  -16.934 1.00 53.03  ? 181 LEU A O     1 
ATOM   1414 C  CB    . LEU A 1 181 ? 11.064  -10.260 -15.555 1.00 47.56  ? 181 LEU A CB    1 
ATOM   1415 C  CG    . LEU A 1 181 ? 12.424  -10.818 -15.134 1.00 48.61  ? 181 LEU A CG    1 
ATOM   1416 C  CD1   . LEU A 1 181 ? 12.611  -12.219 -15.699 1.00 43.34  ? 181 LEU A CD1   1 
ATOM   1417 C  CD2   . LEU A 1 181 ? 13.538  -9.905  -15.601 1.00 48.21  ? 181 LEU A CD2   1 
ATOM   1418 N  N     . GLU A 1 182 ? 8.300   -8.689  -15.779 1.00 52.14  ? 182 GLU A N     1 
ATOM   1419 C  CA    . GLU A 1 182 ? 7.217   -8.202  -16.626 1.00 55.35  ? 182 GLU A CA    1 
ATOM   1420 C  C     . GLU A 1 182 ? 7.011   -6.705  -16.450 1.00 54.15  ? 182 GLU A C     1 
ATOM   1421 O  O     . GLU A 1 182 ? 6.667   -6.003  -17.410 1.00 59.55  ? 182 GLU A O     1 
ATOM   1422 C  CB    . GLU A 1 182 ? 5.932   -8.969  -16.320 1.00 57.08  ? 182 GLU A CB    1 
ATOM   1423 C  CG    . GLU A 1 182 ? 6.039   -10.455 -16.627 1.00 65.19  ? 182 GLU A CG    1 
ATOM   1424 C  CD    . GLU A 1 182 ? 4.816   -11.243 -16.196 1.00 75.52  ? 182 GLU A CD    1 
ATOM   1425 O  OE1   . GLU A 1 182 ? 3.913   -10.654 -15.561 1.00 78.10  ? 182 GLU A OE1   1 
ATOM   1426 O  OE2   . GLU A 1 182 ? 4.762   -12.455 -16.493 1.00 77.39  ? 182 GLU A OE2   1 
ATOM   1427 N  N     . ALA A 1 183 ? 7.210   -6.198  -15.232 1.00 54.06  ? 183 ALA A N     1 
ATOM   1428 C  CA    . ALA A 1 183 ? 7.093   -4.761  -15.010 1.00 51.43  ? 183 ALA A CA    1 
ATOM   1429 C  C     . ALA A 1 183 ? 8.280   -4.012  -15.599 1.00 52.46  ? 183 ALA A C     1 
ATOM   1430 O  O     . ALA A 1 183 ? 8.129   -2.887  -16.085 1.00 54.07  ? 183 ALA A O     1 
ATOM   1431 C  CB    . ALA A 1 183 ? 6.963   -4.463  -13.514 1.00 54.73  ? 183 ALA A CB    1 
ATOM   1432 N  N     . LEU A 1 184 ? 9.472   -4.612  -15.559 1.00 53.38  ? 184 LEU A N     1 
ATOM   1433 C  CA    . LEU A 1 184 ? 10.661  -3.911  -16.035 1.00 52.32  ? 184 LEU A CA    1 
ATOM   1434 C  C     . LEU A 1 184 ? 10.591  -3.634  -17.534 1.00 51.87  ? 184 LEU A C     1 
ATOM   1435 O  O     . LEU A 1 184 ? 10.923  -2.531  -17.981 1.00 51.98  ? 184 LEU A O     1 
ATOM   1436 C  CB    . LEU A 1 184 ? 11.918  -4.712  -15.690 1.00 50.03  ? 184 LEU A CB    1 
ATOM   1437 C  CG    . LEU A 1 184 ? 13.221  -4.160  -16.277 1.00 50.80  ? 184 LEU A CG    1 
ATOM   1438 C  CD1   . LEU A 1 184 ? 13.628  -2.838  -15.609 1.00 47.47  ? 184 LEU A CD1   1 
ATOM   1439 C  CD2   . LEU A 1 184 ? 14.332  -5.188  -16.180 1.00 46.20  ? 184 LEU A CD2   1 
ATOM   1440 N  N     . GLY A 1 185 ? 10.160  -4.613  -18.325 1.00 56.13  ? 185 GLY A N     1 
ATOM   1441 C  CA    . GLY A 1 185 ? 10.190  -4.440  -19.768 1.00 56.00  ? 185 GLY A CA    1 
ATOM   1442 C  C     . GLY A 1 185 ? 11.586  -4.100  -20.241 1.00 59.14  ? 185 GLY A C     1 
ATOM   1443 O  O     . GLY A 1 185 ? 12.576  -4.688  -19.794 1.00 54.84  ? 185 GLY A O     1 
ATOM   1444 N  N     . ASP A 1 186 ? 11.678  -3.112  -21.133 1.00 66.16  ? 186 ASP A N     1 
ATOM   1445 C  CA    . ASP A 1 186 ? 12.960  -2.612  -21.621 1.00 67.00  ? 186 ASP A CA    1 
ATOM   1446 C  C     . ASP A 1 186 ? 13.402  -1.330  -20.914 1.00 64.11  ? 186 ASP A C     1 
ATOM   1447 O  O     . ASP A 1 186 ? 14.147  -0.534  -21.492 1.00 64.89  ? 186 ASP A O     1 
ATOM   1448 C  CB    . ASP A 1 186 ? 12.909  -2.388  -23.134 1.00 71.65  ? 186 ASP A CB    1 
ATOM   1449 C  CG    . ASP A 1 186 ? 13.133  -3.669  -23.925 1.00 77.40  ? 186 ASP A CG    1 
ATOM   1450 O  OD1   . ASP A 1 186 ? 13.675  -4.643  -23.354 1.00 71.93  ? 186 ASP A OD1   1 
ATOM   1451 O  OD2   . ASP A 1 186 ? 12.777  -3.698  -25.122 1.00 86.93  ? 186 ASP A OD2   1 
ATOM   1452 N  N     . GLY A 1 187 ? 12.962  -1.115  -19.672 1.00 60.84  ? 187 GLY A N     1 
ATOM   1453 C  CA    . GLY A 1 187 ? 13.379  0.041   -18.905 1.00 53.65  ? 187 GLY A CA    1 
ATOM   1454 C  C     . GLY A 1 187 ? 14.677  -0.202  -18.152 1.00 54.54  ? 187 GLY A C     1 
ATOM   1455 O  O     . GLY A 1 187 ? 15.281  -1.271  -18.218 1.00 50.34  ? 187 GLY A O     1 
ATOM   1456 N  N     . GLU A 1 188 ? 15.097  0.821   -17.412 1.00 49.35  ? 188 GLU A N     1 
ATOM   1457 C  CA    . GLU A 1 188 ? 16.375  0.789   -16.713 1.00 52.03  ? 188 GLU A CA    1 
ATOM   1458 C  C     . GLU A 1 188 ? 16.294  -0.063  -15.451 1.00 49.53  ? 188 GLU A C     1 
ATOM   1459 O  O     . GLU A 1 188 ? 15.256  -0.126  -14.786 1.00 47.94  ? 188 GLU A O     1 
ATOM   1460 C  CB    . GLU A 1 188 ? 16.820  2.197   -16.325 1.00 55.15  ? 188 GLU A CB    1 
ATOM   1461 C  CG    . GLU A 1 188 ? 17.144  3.114   -17.484 1.00 69.09  ? 188 GLU A CG    1 
ATOM   1462 C  CD    . GLU A 1 188 ? 17.559  4.494   -17.011 1.00 80.30  ? 188 GLU A CD    1 
ATOM   1463 O  OE1   . GLU A 1 188 ? 17.870  4.638   -15.805 1.00 79.41  ? 188 GLU A OE1   1 
ATOM   1464 O  OE2   . GLU A 1 188 ? 17.567  5.431   -17.839 1.00 87.65  ? 188 GLU A OE2   1 
ATOM   1465 N  N     . PHE A 1 189 ? 17.420  -0.693  -15.106 1.00 43.54  ? 189 PHE A N     1 
ATOM   1466 C  CA    . PHE A 1 189 ? 17.525  -1.462  -13.873 1.00 40.52  ? 189 PHE A CA    1 
ATOM   1467 C  C     . PHE A 1 189 ? 18.904  -1.262  -13.255 1.00 41.25  ? 189 PHE A C     1 
ATOM   1468 O  O     . PHE A 1 189 ? 19.881  -0.973  -13.949 1.00 41.65  ? 189 PHE A O     1 
ATOM   1469 C  CB    . PHE A 1 189 ? 17.259  -2.966  -14.116 1.00 40.87  ? 189 PHE A CB    1 
ATOM   1470 C  CG    . PHE A 1 189 ? 18.160  -3.600  -15.150 1.00 40.45  ? 189 PHE A CG    1 
ATOM   1471 C  CD1   . PHE A 1 189 ? 17.846  -3.534  -16.504 1.00 44.35  ? 189 PHE A CD1   1 
ATOM   1472 C  CD2   . PHE A 1 189 ? 19.299  -4.289  -14.765 1.00 40.61  ? 189 PHE A CD2   1 
ATOM   1473 C  CE1   . PHE A 1 189 ? 18.665  -4.123  -17.454 1.00 44.83  ? 189 PHE A CE1   1 
ATOM   1474 C  CE2   . PHE A 1 189 ? 20.119  -4.885  -15.709 1.00 40.90  ? 189 PHE A CE2   1 
ATOM   1475 C  CZ    . PHE A 1 189 ? 19.806  -4.800  -17.051 1.00 43.91  ? 189 PHE A CZ    1 
ATOM   1476 N  N     . ILE A 1 190 ? 18.980  -1.432  -11.937 1.00 39.08  ? 190 ILE A N     1 
ATOM   1477 C  CA    . ILE A 1 190 ? 20.262  -1.404  -11.237 1.00 37.88  ? 190 ILE A CA    1 
ATOM   1478 C  C     . ILE A 1 190 ? 20.933  -2.767  -11.380 1.00 39.03  ? 190 ILE A C     1 
ATOM   1479 O  O     . ILE A 1 190 ? 20.315  -3.801  -11.114 1.00 33.36  ? 190 ILE A O     1 
ATOM   1480 C  CB    . ILE A 1 190 ? 20.067  -1.037  -9.756  1.00 40.62  ? 190 ILE A CB    1 
ATOM   1481 C  CG1   . ILE A 1 190 ? 19.355  0.317   -9.632  1.00 42.94  ? 190 ILE A CG1   1 
ATOM   1482 C  CG2   . ILE A 1 190 ? 21.402  -1.037  -9.026  1.00 38.07  ? 190 ILE A CG2   1 
ATOM   1483 C  CD1   . ILE A 1 190 ? 20.059  1.455   -10.352 1.00 45.51  ? 190 ILE A CD1   1 
ATOM   1484 N  N     . LYS A 1 191 ? 22.198  -2.771  -11.799 1.00 37.24  ? 191 LYS A N     1 
ATOM   1485 C  CA    . LYS A 1 191 ? 22.941  -4.001  -12.042 1.00 36.58  ? 191 LYS A CA    1 
ATOM   1486 C  C     . LYS A 1 191 ? 23.707  -4.385  -10.784 1.00 35.49  ? 191 LYS A C     1 
ATOM   1487 O  O     . LYS A 1 191 ? 24.569  -3.627  -10.327 1.00 34.41  ? 191 LYS A O     1 
ATOM   1488 C  CB    . LYS A 1 191 ? 23.906  -3.832  -13.217 1.00 35.80  ? 191 LYS A CB    1 
ATOM   1489 C  CG    . LYS A 1 191 ? 23.233  -3.523  -14.533 1.00 37.74  ? 191 LYS A CG    1 
ATOM   1490 C  CD    . LYS A 1 191 ? 24.279  -3.191  -15.602 1.00 42.19  ? 191 LYS A CD    1 
ATOM   1491 C  CE    . LYS A 1 191 ? 23.745  -2.168  -16.585 1.00 52.76  ? 191 LYS A CE    1 
ATOM   1492 N  NZ    . LYS A 1 191 ? 24.816  -1.648  -17.488 1.00 58.52  ? 191 LYS A NZ    1 
ATOM   1493 N  N     . CYS A 1 192 ? 23.406  -5.569  -10.236 1.00 31.49  ? 192 CYS A N     1 
ATOM   1494 C  CA    . CYS A 1 192 ? 23.996  -6.041  -8.994  1.00 30.91  ? 192 CYS A CA    1 
ATOM   1495 C  C     . CYS A 1 192 ? 24.701  -7.361  -9.258  1.00 32.64  ? 192 CYS A C     1 
ATOM   1496 O  O     . CYS A 1 192 ? 24.104  -8.280  -9.818  1.00 35.10  ? 192 CYS A O     1 
ATOM   1497 C  CB    . CYS A 1 192 ? 22.921  -6.221  -7.903  1.00 31.43  ? 192 CYS A CB    1 
ATOM   1498 S  SG    . CYS A 1 192 ? 21.970  -4.712  -7.574  1.00 33.26  ? 192 CYS A SG    1 
ATOM   1499 N  N     . LEU A 1 193 ? 25.967  -7.445  -8.873  1.00 32.16  ? 193 LEU A N     1 
ATOM   1500 C  CA    . LEU A 1 193 ? 26.777  -8.627  -9.115  1.00 31.37  ? 193 LEU A CA    1 
ATOM   1501 C  C     . LEU A 1 193 ? 27.379  -9.049  -7.790  1.00 34.82  ? 193 LEU A C     1 
ATOM   1502 O  O     . LEU A 1 193 ? 28.104  -8.270  -7.160  1.00 31.38  ? 193 LEU A O     1 
ATOM   1503 C  CB    . LEU A 1 193 ? 27.878  -8.355  -10.147 1.00 32.28  ? 193 LEU A CB    1 
ATOM   1504 C  CG    . LEU A 1 193 ? 28.921  -9.446  -10.407 1.00 35.15  ? 193 LEU A CG    1 
ATOM   1505 C  CD1   . LEU A 1 193 ? 28.259  -10.729 -10.925 1.00 31.71  ? 193 LEU A CD1   1 
ATOM   1506 C  CD2   . LEU A 1 193 ? 29.968  -8.945  -11.401 1.00 37.77  ? 193 LEU A CD2   1 
ATOM   1507 N  N     . HIS A 1 194 ? 27.093  -10.280 -7.377  1.00 31.00  ? 194 HIS A N     1 
ATOM   1508 C  CA    . HIS A 1 194 ? 27.612  -10.808 -6.134  1.00 31.67  ? 194 HIS A CA    1 
ATOM   1509 C  C     . HIS A 1 194 ? 28.253  -12.170 -6.359  1.00 33.37  ? 194 HIS A C     1 
ATOM   1510 O  O     . HIS A 1 194 ? 27.735  -12.988 -7.125  1.00 32.14  ? 194 HIS A O     1 
ATOM   1511 C  CB    . HIS A 1 194 ? 26.493  -10.919 -5.097  1.00 30.38  ? 194 HIS A CB    1 
ATOM   1512 C  CG    . HIS A 1 194 ? 26.933  -11.542 -3.814  1.00 32.56  ? 194 HIS A CG    1 
ATOM   1513 N  ND1   . HIS A 1 194 ? 26.563  -12.817 -3.443  1.00 32.65  ? 194 HIS A ND1   1 
ATOM   1514 C  CD2   . HIS A 1 194 ? 27.719  -11.068 -2.815  1.00 31.41  ? 194 HIS A CD2   1 
ATOM   1515 C  CE1   . HIS A 1 194 ? 27.105  -13.101 -2.272  1.00 35.87  ? 194 HIS A CE1   1 
ATOM   1516 N  NE2   . HIS A 1 194 ? 27.806  -12.056 -1.867  1.00 35.68  ? 194 HIS A NE2   1 
ATOM   1517 N  N     . SER A 1 195 ? 29.384  -12.405 -5.688  1.00 32.28  ? 195 SER A N     1 
ATOM   1518 C  CA    . SER A 1 195 ? 29.950  -13.739 -5.552  1.00 35.22  ? 195 SER A CA    1 
ATOM   1519 C  C     . SER A 1 195 ? 30.507  -13.922 -4.150  1.00 36.94  ? 195 SER A C     1 
ATOM   1520 O  O     . SER A 1 195 ? 31.108  -12.998 -3.593  1.00 36.66  ? 195 SER A O     1 
ATOM   1521 C  CB    . SER A 1 195 ? 31.073  -13.987 -6.569  1.00 33.89  ? 195 SER A CB    1 
ATOM   1522 O  OG    . SER A 1 195 ? 31.671  -15.258 -6.360  1.00 37.60  ? 195 SER A OG    1 
ATOM   1523 N  N     . VAL A 1 196 ? 30.322  -15.126 -3.590  1.00 34.70  ? 196 VAL A N     1 
ATOM   1524 C  CA    . VAL A 1 196 ? 31.003  -15.480 -2.348  1.00 37.30  ? 196 VAL A CA    1 
ATOM   1525 C  C     . VAL A 1 196 ? 32.501  -15.633 -2.558  1.00 41.49  ? 196 VAL A C     1 
ATOM   1526 O  O     . VAL A 1 196 ? 33.263  -15.667 -1.580  1.00 42.66  ? 196 VAL A O     1 
ATOM   1527 C  CB    . VAL A 1 196 ? 30.431  -16.782 -1.744  1.00 39.73  ? 196 VAL A CB    1 
ATOM   1528 C  CG1   . VAL A 1 196 ? 28.988  -16.594 -1.304  1.00 37.31  ? 196 VAL A CG1   1 
ATOM   1529 C  CG2   . VAL A 1 196 ? 30.547  -17.930 -2.734  1.00 39.18  ? 196 VAL A CG2   1 
ATOM   1530 N  N     . GLY A 1 197 ? 32.943  -15.770 -3.807  1.00 40.48  ? 197 GLY A N     1 
ATOM   1531 C  CA    . GLY A 1 197 ? 34.358  -15.788 -4.097  1.00 41.72  ? 197 GLY A CA    1 
ATOM   1532 C  C     . GLY A 1 197 ? 35.042  -17.088 -3.768  1.00 48.48  ? 197 GLY A C     1 
ATOM   1533 O  O     . GLY A 1 197 ? 36.221  -17.083 -3.399  1.00 48.89  ? 197 GLY A O     1 
ATOM   1534 N  N     A CYS A 1 198 ? 34.329  -18.209 -3.865  0.50 46.35  ? 198 CYS A N     1 
ATOM   1535 N  N     B CYS A 1 198 ? 34.345  -18.211 -3.929  0.50 46.07  ? 198 CYS A N     1 
ATOM   1536 C  CA    A CYS A 1 198 ? 34.861  -19.529 -3.526  0.50 47.10  ? 198 CYS A CA    1 
ATOM   1537 C  CA    B CYS A 1 198 ? 34.835  -19.525 -3.517  0.50 47.09  ? 198 CYS A CA    1 
ATOM   1538 C  C     A CYS A 1 198 ? 34.623  -20.482 -4.689  0.50 47.70  ? 198 CYS A C     1 
ATOM   1539 C  C     B CYS A 1 198 ? 34.652  -20.514 -4.666  0.50 47.87  ? 198 CYS A C     1 
ATOM   1540 O  O     A CYS A 1 198 ? 33.757  -21.363 -4.622  0.50 48.12  ? 198 CYS A O     1 
ATOM   1541 O  O     B CYS A 1 198 ? 33.852  -21.453 -4.567  0.50 48.47  ? 198 CYS A O     1 
ATOM   1542 C  CB    A CYS A 1 198 ? 34.220  -20.066 -2.246  0.50 45.78  ? 198 CYS A CB    1 
ATOM   1543 C  CB    B CYS A 1 198 ? 34.091  -19.988 -2.261  0.50 46.07  ? 198 CYS A CB    1 
ATOM   1544 S  SG    A CYS A 1 198 ? 34.781  -19.255 -0.751  0.50 42.57  ? 198 CYS A SG    1 
ATOM   1545 S  SG    B CYS A 1 198 ? 35.010  -21.056 -1.129  0.50 53.78  ? 198 CYS A SG    1 
ATOM   1546 N  N     . PRO A 1 199 ? 35.377  -20.329 -5.777  1.00 48.60  ? 199 PRO A N     1 
ATOM   1547 C  CA    . PRO A 1 199 ? 35.231  -21.256 -6.907  1.00 48.84  ? 199 PRO A CA    1 
ATOM   1548 C  C     . PRO A 1 199 ? 35.596  -22.678 -6.509  1.00 53.95  ? 199 PRO A C     1 
ATOM   1549 O  O     . PRO A 1 199 ? 36.507  -22.903 -5.709  1.00 55.69  ? 199 PRO A O     1 
ATOM   1550 C  CB    . PRO A 1 199 ? 36.209  -20.704 -7.957  1.00 51.78  ? 199 PRO A CB    1 
ATOM   1551 C  CG    . PRO A 1 199 ? 37.173  -19.859 -7.193  1.00 48.81  ? 199 PRO A CG    1 
ATOM   1552 C  CD    . PRO A 1 199 ? 36.375  -19.280 -6.051  1.00 48.56  ? 199 PRO A CD    1 
ATOM   1553 N  N     . LEU A 1 200 ? 34.861  -23.640 -7.071  1.00 53.54  ? 200 LEU A N     1 
ATOM   1554 C  CA    . LEU A 1 200 ? 35.079  -25.069 -6.854  1.00 58.13  ? 200 LEU A CA    1 
ATOM   1555 C  C     . LEU A 1 200 ? 36.050  -25.618 -7.899  1.00 60.90  ? 200 LEU A C     1 
ATOM   1556 O  O     . LEU A 1 200 ? 35.976  -25.241 -9.070  1.00 59.61  ? 200 LEU A O     1 
ATOM   1557 C  CB    . LEU A 1 200 ? 33.752  -25.826 -6.922  1.00 54.66  ? 200 LEU A CB    1 
ATOM   1558 C  CG    . LEU A 1 200 ? 32.706  -25.324 -5.924  1.00 56.70  ? 200 LEU A CG    1 
ATOM   1559 C  CD1   . LEU A 1 200 ? 31.306  -25.861 -6.212  1.00 49.66  ? 200 LEU A CD1   1 
ATOM   1560 C  CD2   . LEU A 1 200 ? 33.127  -25.691 -4.518  1.00 59.45  ? 200 LEU A CD2   1 
ATOM   1561 N  N     . PRO A 1 201 ? 36.984  -26.516 -7.541  1.00 67.84  ? 201 PRO A N     1 
ATOM   1562 C  CA    . PRO A 1 201 ? 37.172  -27.177 -6.241  1.00 68.52  ? 201 PRO A CA    1 
ATOM   1563 C  C     . PRO A 1 201 ? 37.766  -26.262 -5.176  1.00 69.07  ? 201 PRO A C     1 
ATOM   1564 O  O     . PRO A 1 201 ? 38.534  -25.349 -5.470  1.00 72.15  ? 201 PRO A O     1 
ATOM   1565 C  CB    . PRO A 1 201 ? 38.118  -28.337 -6.590  1.00 73.39  ? 201 PRO A CB    1 
ATOM   1566 C  CG    . PRO A 1 201 ? 38.958  -27.786 -7.706  1.00 75.09  ? 201 PRO A CG    1 
ATOM   1567 C  CD    . PRO A 1 201 ? 38.015  -26.924 -8.514  1.00 68.92  ? 201 PRO A CD    1 
ATOM   1568 N  N     . LEU A 1 202 ? 37.425  -26.512 -3.916  1.00 72.29  ? 202 LEU A N     1 
ATOM   1569 C  CA    . LEU A 1 202 ? 37.845  -25.640 -2.828  1.00 81.59  ? 202 LEU A CA    1 
ATOM   1570 C  C     . LEU A 1 202 ? 39.333  -25.806 -2.551  1.00 90.04  ? 202 LEU A C     1 
ATOM   1571 O  O     . LEU A 1 202 ? 39.795  -26.909 -2.241  1.00 90.07  ? 202 LEU A O     1 
ATOM   1572 C  CB    . LEU A 1 202 ? 37.036  -25.944 -1.571  1.00 78.59  ? 202 LEU A CB    1 
ATOM   1573 C  CG    . LEU A 1 202 ? 35.547  -25.645 -1.691  1.00 68.78  ? 202 LEU A CG    1 
ATOM   1574 C  CD1   . LEU A 1 202 ? 34.855  -25.793 -0.353  1.00 67.49  ? 202 LEU A CD1   1 
ATOM   1575 C  CD2   . LEU A 1 202 ? 35.368  -24.249 -2.233  1.00 63.41  ? 202 LEU A CD2   1 
ATOM   1576 N  N     . LYS A 1 203 ? 40.081  -24.707 -2.660  1.00 99.36  ? 203 LYS A N     1 
ATOM   1577 C  CA    . LYS A 1 203 ? 41.461  -24.707 -2.191  1.00 105.57 ? 203 LYS A CA    1 
ATOM   1578 C  C     . LYS A 1 203 ? 41.528  -24.652 -0.669  1.00 110.38 ? 203 LYS A C     1 
ATOM   1579 O  O     . LYS A 1 203 ? 42.462  -25.197 -0.071  1.00 114.06 ? 203 LYS A O     1 
ATOM   1580 C  CB    . LYS A 1 203 ? 42.224  -23.527 -2.797  1.00 110.38 ? 203 LYS A CB    1 
ATOM   1581 C  CG    . LYS A 1 203 ? 42.274  -23.519 -4.318  1.00 111.89 ? 203 LYS A CG    1 
ATOM   1582 C  CD    . LYS A 1 203 ? 43.072  -24.699 -4.856  1.00 112.95 ? 203 LYS A CD    1 
ATOM   1583 C  CE    . LYS A 1 203 ? 43.211  -24.625 -6.369  1.00 115.39 ? 203 LYS A CE    1 
ATOM   1584 N  NZ    . LYS A 1 203 ? 41.885  -24.570 -7.045  1.00 109.90 ? 203 LYS A NZ    1 
ATOM   1585 N  N     . LYS A 1 204 ? 40.551  -24.009 -0.031  1.00 115.88 ? 204 LYS A N     1 
ATOM   1586 C  CA    . LYS A 1 204 ? 40.517  -23.813 1.409   1.00 113.17 ? 204 LYS A CA    1 
ATOM   1587 C  C     . LYS A 1 204 ? 39.261  -24.452 1.989   1.00 112.66 ? 204 LYS A C     1 
ATOM   1588 O  O     . LYS A 1 204 ? 38.162  -24.237 1.455   1.00 108.58 ? 204 LYS A O     1 
ATOM   1589 C  CB    . LYS A 1 204 ? 40.541  -22.311 1.757   1.00 116.72 ? 204 LYS A CB    1 
ATOM   1590 C  CG    . LYS A 1 204 ? 41.511  -21.479 0.926   1.00 121.90 ? 204 LYS A CG    1 
ATOM   1591 C  CD    . LYS A 1 204 ? 41.273  -19.988 1.136   1.00 128.28 ? 204 LYS A CD    1 
ATOM   1592 C  CE    . LYS A 1 204 ? 42.141  -19.144 0.214   1.00 126.90 ? 204 LYS A CE    1 
ATOM   1593 N  NZ    . LYS A 1 204 ? 41.879  -17.687 0.381   1.00 116.09 ? 204 LYS A NZ    1 
ATOM   1594 N  N     . PRO A 1 205 ? 39.370  -25.234 3.063   1.00 105.09 ? 205 PRO A N     1 
ATOM   1595 C  CA    . PRO A 1 205 ? 38.168  -25.805 3.682   1.00 94.62  ? 205 PRO A CA    1 
ATOM   1596 C  C     . PRO A 1 205 ? 37.296  -24.728 4.313   1.00 85.45  ? 205 PRO A C     1 
ATOM   1597 O  O     . PRO A 1 205 ? 37.779  -23.685 4.763   1.00 83.35  ? 205 PRO A O     1 
ATOM   1598 C  CB    . PRO A 1 205 ? 38.732  -26.763 4.741   1.00 97.29  ? 205 PRO A CB    1 
ATOM   1599 C  CG    . PRO A 1 205 ? 40.112  -26.259 5.018   1.00 100.52 ? 205 PRO A CG    1 
ATOM   1600 C  CD    . PRO A 1 205 ? 40.607  -25.688 3.720   1.00 104.04 ? 205 PRO A CD    1 
ATOM   1601 N  N     . LEU A 1 206 ? 35.989  -24.993 4.335   1.00 77.80  ? 206 LEU A N     1 
ATOM   1602 C  CA    . LEU A 1 206 ? 35.004  -24.013 4.775   1.00 67.31  ? 206 LEU A CA    1 
ATOM   1603 C  C     . LEU A 1 206 ? 34.689  -24.163 6.259   1.00 67.47  ? 206 LEU A C     1 
ATOM   1604 O  O     . LEU A 1 206 ? 34.655  -25.275 6.798   1.00 69.79  ? 206 LEU A O     1 
ATOM   1605 C  CB    . LEU A 1 206 ? 33.716  -24.143 3.963   1.00 61.60  ? 206 LEU A CB    1 
ATOM   1606 C  CG    . LEU A 1 206 ? 33.791  -23.807 2.471   1.00 60.76  ? 206 LEU A CG    1 
ATOM   1607 C  CD1   . LEU A 1 206 ? 32.396  -23.726 1.880   1.00 56.87  ? 206 LEU A CD1   1 
ATOM   1608 C  CD2   . LEU A 1 206 ? 34.551  -22.512 2.231   1.00 55.79  ? 206 LEU A CD2   1 
ATOM   1609 N  N     . VAL A 1 207 ? 34.456  -23.029 6.913   1.00 62.89  ? 207 VAL A N     1 
ATOM   1610 C  CA    . VAL A 1 207 ? 34.081  -22.990 8.323   1.00 61.32  ? 207 VAL A CA    1 
ATOM   1611 C  C     . VAL A 1 207 ? 32.562  -22.938 8.412   1.00 61.20  ? 207 VAL A C     1 
ATOM   1612 O  O     . VAL A 1 207 ? 31.930  -22.044 7.834   1.00 59.18  ? 207 VAL A O     1 
ATOM   1613 C  CB    . VAL A 1 207 ? 34.715  -21.786 9.036   1.00 62.10  ? 207 VAL A CB    1 
ATOM   1614 C  CG1   . VAL A 1 207 ? 34.340  -21.783 10.514  1.00 60.19  ? 207 VAL A CG1   1 
ATOM   1615 C  CG2   . VAL A 1 207 ? 36.233  -21.804 8.865   1.00 66.01  ? 207 VAL A CG2   1 
ATOM   1616 N  N     . ASN A 1 208 ? 31.976  -23.899 9.132   1.00 55.73  ? 208 ASN A N     1 
ATOM   1617 C  CA    . ASN A 1 208 ? 30.523  -24.006 9.272   1.00 58.40  ? 208 ASN A CA    1 
ATOM   1618 C  C     . ASN A 1 208 ? 29.826  -24.087 7.919   1.00 55.73  ? 208 ASN A C     1 
ATOM   1619 O  O     . ASN A 1 208 ? 28.706  -23.588 7.761   1.00 56.26  ? 208 ASN A O     1 
ATOM   1620 C  CB    . ASN A 1 208 ? 29.944  -22.840 10.080  1.00 57.39  ? 208 ASN A CB    1 
ATOM   1621 C  CG    . ASN A 1 208 ? 29.934  -23.104 11.570  1.00 58.89  ? 208 ASN A CG    1 
ATOM   1622 O  OD1   . ASN A 1 208 ? 30.020  -24.248 12.014  1.00 67.18  ? 208 ASN A OD1   1 
ATOM   1623 N  ND2   . ASN A 1 208 ? 29.810  -22.038 12.354  1.00 59.32  ? 208 ASN A ND2   1 
ATOM   1624 N  N     . ASN A 1 209 ? 30.487  -24.699 6.934   1.00 54.38  ? 209 ASN A N     1 
ATOM   1625 C  CA    . ASN A 1 209 ? 29.973  -24.812 5.569   1.00 57.40  ? 209 ASN A CA    1 
ATOM   1626 C  C     . ASN A 1 209 ? 29.681  -23.452 4.934   1.00 51.09  ? 209 ASN A C     1 
ATOM   1627 O  O     . ASN A 1 209 ? 28.888  -23.368 3.994   1.00 49.84  ? 209 ASN A O     1 
ATOM   1628 C  CB    . ASN A 1 209 ? 28.708  -25.677 5.517   1.00 54.96  ? 209 ASN A CB    1 
ATOM   1629 C  CG    . ASN A 1 209 ? 28.988  -27.137 5.777   1.00 61.39  ? 209 ASN A CG    1 
ATOM   1630 O  OD1   . ASN A 1 209 ? 29.821  -27.751 5.111   1.00 65.22  ? 209 ASN A OD1   1 
ATOM   1631 N  ND2   . ASN A 1 209 ? 28.299  -27.702 6.760   1.00 63.29  ? 209 ASN A ND2   1 
ATOM   1632 N  N     . TRP A 1 210 ? 30.300  -22.379 5.417   1.00 49.41  ? 210 TRP A N     1 
ATOM   1633 C  CA    . TRP A 1 210 ? 29.949  -21.026 4.991   1.00 48.40  ? 210 TRP A CA    1 
ATOM   1634 C  C     . TRP A 1 210 ? 30.982  -20.521 3.987   1.00 46.15  ? 210 TRP A C     1 
ATOM   1635 O  O     . TRP A 1 210 ? 32.119  -20.214 4.356   1.00 43.67  ? 210 TRP A O     1 
ATOM   1636 C  CB    . TRP A 1 210 ? 29.854  -20.090 6.190   1.00 47.82  ? 210 TRP A CB    1 
ATOM   1637 C  CG    . TRP A 1 210 ? 29.348  -18.734 5.821   1.00 43.56  ? 210 TRP A CG    1 
ATOM   1638 C  CD1   . TRP A 1 210 ? 30.092  -17.605 5.617   1.00 45.25  ? 210 TRP A CD1   1 
ATOM   1639 C  CD2   . TRP A 1 210 ? 27.982  -18.360 5.600   1.00 44.14  ? 210 TRP A CD2   1 
ATOM   1640 N  NE1   . TRP A 1 210 ? 29.273  -16.551 5.294   1.00 39.28  ? 210 TRP A NE1   1 
ATOM   1641 C  CE2   . TRP A 1 210 ? 27.972  -16.989 5.277   1.00 43.92  ? 210 TRP A CE2   1 
ATOM   1642 C  CE3   . TRP A 1 210 ? 26.766  -19.051 5.649   1.00 47.07  ? 210 TRP A CE3   1 
ATOM   1643 C  CZ2   . TRP A 1 210 ? 26.792  -16.297 4.999   1.00 42.82  ? 210 TRP A CZ2   1 
ATOM   1644 C  CZ3   . TRP A 1 210 ? 25.599  -18.363 5.380   1.00 42.52  ? 210 TRP A CZ3   1 
ATOM   1645 C  CH2   . TRP A 1 210 ? 25.619  -16.997 5.056   1.00 40.63  ? 210 TRP A CH2   1 
ATOM   1646 N  N     . ALA A 1 211 ? 30.583  -20.428 2.722   1.00 42.84  ? 211 ALA A N     1 
ATOM   1647 C  CA    . ALA A 1 211 ? 31.498  -20.000 1.671   1.00 45.54  ? 211 ALA A CA    1 
ATOM   1648 C  C     . ALA A 1 211 ? 31.657  -18.483 1.724   1.00 44.68  ? 211 ALA A C     1 
ATOM   1649 O  O     . ALA A 1 211 ? 30.668  -17.745 1.658   1.00 41.81  ? 211 ALA A O     1 
ATOM   1650 C  CB    . ALA A 1 211 ? 30.988  -20.447 0.303   1.00 44.02  ? 211 ALA A CB    1 
ATOM   1651 N  N     . CYS A 1 212 ? 32.898  -18.026 1.862   1.00 46.01  ? 212 CYS A N     1 
ATOM   1652 C  CA    . CYS A 1 212 ? 33.227  -16.607 1.893   1.00 45.38  ? 212 CYS A CA    1 
ATOM   1653 C  C     . CYS A 1 212 ? 34.721  -16.479 1.631   1.00 46.96  ? 212 CYS A C     1 
ATOM   1654 O  O     . CYS A 1 212 ? 35.461  -17.462 1.683   1.00 43.01  ? 212 CYS A O     1 
ATOM   1655 C  CB    . CYS A 1 212 ? 32.852  -15.971 3.238   1.00 44.68  ? 212 CYS A CB    1 
ATOM   1656 S  SG    . CYS A 1 212 ? 33.841  -16.610 4.628   1.00 48.08  ? 212 CYS A SG    1 
ATOM   1657 N  N     . ASN A 1 213 ? 35.161  -15.251 1.367   1.00 45.74  ? 213 ASN A N     1 
ATOM   1658 C  CA    . ASN A 1 213 ? 36.567  -14.960 1.073   1.00 50.37  ? 213 ASN A CA    1 
ATOM   1659 C  C     . ASN A 1 213 ? 36.914  -13.660 1.777   1.00 51.26  ? 213 ASN A C     1 
ATOM   1660 O  O     . ASN A 1 213 ? 36.845  -12.575 1.185   1.00 51.18  ? 213 ASN A O     1 
ATOM   1661 C  CB    . ASN A 1 213 ? 36.800  -14.862 -0.437  1.00 50.05  ? 213 ASN A CB    1 
ATOM   1662 C  CG    . ASN A 1 213 ? 38.263  -14.971 -0.823  1.00 54.40  ? 213 ASN A CG    1 
ATOM   1663 O  OD1   . ASN A 1 213 ? 39.151  -14.460 -0.135  1.00 57.12  ? 213 ASN A OD1   1 
ATOM   1664 N  ND2   . ASN A 1 213 ? 38.521  -15.644 -1.939  1.00 51.73  ? 213 ASN A ND2   1 
ATOM   1665 N  N     . PRO A 1 214 ? 37.259  -13.726 3.067   1.00 51.29  ? 214 PRO A N     1 
ATOM   1666 C  CA    . PRO A 1 214 ? 37.440  -12.479 3.836   1.00 53.53  ? 214 PRO A CA    1 
ATOM   1667 C  C     . PRO A 1 214 ? 38.581  -11.613 3.330   1.00 55.56  ? 214 PRO A C     1 
ATOM   1668 O  O     . PRO A 1 214 ? 38.462  -10.380 3.321   1.00 54.59  ? 214 PRO A O     1 
ATOM   1669 C  CB    . PRO A 1 214 ? 37.695  -12.988 5.264   1.00 56.38  ? 214 PRO A CB    1 
ATOM   1670 C  CG    . PRO A 1 214 ? 37.152  -14.395 5.285   1.00 53.83  ? 214 PRO A CG    1 
ATOM   1671 C  CD    . PRO A 1 214 ? 37.409  -14.926 3.910   1.00 52.78  ? 214 PRO A CD    1 
ATOM   1672 N  N     . GLU A 1 215 ? 39.681  -12.227 2.891   1.00 54.70  ? 215 GLU A N     1 
ATOM   1673 C  CA    . GLU A 1 215 ? 40.839  -11.459 2.446   1.00 61.01  ? 215 GLU A CA    1 
ATOM   1674 C  C     . GLU A 1 215 ? 40.500  -10.578 1.251   1.00 56.86  ? 215 GLU A C     1 
ATOM   1675 O  O     . GLU A 1 215 ? 40.997  -9.451  1.137   1.00 53.28  ? 215 GLU A O     1 
ATOM   1676 C  CB    . GLU A 1 215 ? 41.982  -12.408 2.088   1.00 70.66  ? 215 GLU A CB    1 
ATOM   1677 C  CG    . GLU A 1 215 ? 42.269  -13.462 3.136   1.00 78.67  ? 215 GLU A CG    1 
ATOM   1678 C  CD    . GLU A 1 215 ? 43.260  -14.497 2.647   1.00 96.82  ? 215 GLU A CD    1 
ATOM   1679 O  OE1   . GLU A 1 215 ? 43.393  -14.651 1.413   1.00 100.51 ? 215 GLU A OE1   1 
ATOM   1680 O  OE2   . GLU A 1 215 ? 43.909  -15.152 3.493   1.00 106.02 ? 215 GLU A OE2   1 
ATOM   1681 N  N     . LEU A 1 216 ? 39.663  -11.076 0.343   1.00 53.08  ? 216 LEU A N     1 
ATOM   1682 C  CA    . LEU A 1 216 ? 39.370  -10.384 -0.903  1.00 51.93  ? 216 LEU A CA    1 
ATOM   1683 C  C     . LEU A 1 216 ? 38.059  -9.617  -0.860  1.00 49.19  ? 216 LEU A C     1 
ATOM   1684 O  O     . LEU A 1 216 ? 37.621  -9.128  -1.904  1.00 49.35  ? 216 LEU A O     1 
ATOM   1685 C  CB    . LEU A 1 216 ? 39.352  -11.380 -2.068  1.00 50.15  ? 216 LEU A CB    1 
ATOM   1686 C  CG    . LEU A 1 216 ? 40.652  -12.127 -2.379  1.00 53.84  ? 216 LEU A CG    1 
ATOM   1687 C  CD1   . LEU A 1 216 ? 40.479  -13.074 -3.566  1.00 53.02  ? 216 LEU A CD1   1 
ATOM   1688 C  CD2   . LEU A 1 216 ? 41.802  -11.154 -2.628  1.00 54.81  ? 216 LEU A CD2   1 
ATOM   1689 N  N     . THR A 1 217 ? 37.442  -9.483  0.321   1.00 47.45  ? 217 THR A N     1 
ATOM   1690 C  CA    . THR A 1 217 ? 36.123  -8.862  0.437   1.00 45.37  ? 217 THR A CA    1 
ATOM   1691 C  C     . THR A 1 217 ? 36.153  -7.398  -0.003  1.00 48.29  ? 217 THR A C     1 
ATOM   1692 O  O     . THR A 1 217 ? 36.997  -6.609  0.434   1.00 45.15  ? 217 THR A O     1 
ATOM   1693 C  CB    . THR A 1 217 ? 35.604  -8.965  1.878   1.00 47.56  ? 217 THR A CB    1 
ATOM   1694 O  OG1   . THR A 1 217 ? 35.357  -10.335 2.200   1.00 45.53  ? 217 THR A OG1   1 
ATOM   1695 C  CG2   . THR A 1 217 ? 34.294  -8.177  2.062   1.00 44.97  ? 217 THR A CG2   1 
ATOM   1696 N  N     . LEU A 1 218 ? 35.204  -7.039  -0.859  1.00 42.96  ? 218 LEU A N     1 
ATOM   1697 C  CA    . LEU A 1 218 ? 35.151  -5.703  -1.437  1.00 41.92  ? 218 LEU A CA    1 
ATOM   1698 C  C     . LEU A 1 218 ? 33.723  -5.472  -1.896  1.00 40.97  ? 218 LEU A C     1 
ATOM   1699 O  O     . LEU A 1 218 ? 33.179  -6.283  -2.653  1.00 38.92  ? 218 LEU A O     1 
ATOM   1700 C  CB    . LEU A 1 218 ? 36.135  -5.569  -2.603  1.00 42.36  ? 218 LEU A CB    1 
ATOM   1701 C  CG    . LEU A 1 218 ? 36.277  -4.162  -3.210  1.00 43.33  ? 218 LEU A CG    1 
ATOM   1702 C  CD1   . LEU A 1 218 ? 36.924  -3.199  -2.218  1.00 40.65  ? 218 LEU A CD1   1 
ATOM   1703 C  CD2   . LEU A 1 218 ? 37.086  -4.221  -4.495  1.00 49.16  ? 218 LEU A CD2   1 
ATOM   1704 N  N     . ILE A 1 219 ? 33.109  -4.396  -1.418  1.00 37.28  ? 219 ILE A N     1 
ATOM   1705 C  CA    . ILE A 1 219 ? 31.742  -4.048  -1.775  1.00 36.67  ? 219 ILE A CA    1 
ATOM   1706 C  C     . ILE A 1 219 ? 31.828  -2.697  -2.477  1.00 41.22  ? 219 ILE A C     1 
ATOM   1707 O  O     . ILE A 1 219 ? 32.121  -1.677  -1.838  1.00 41.23  ? 219 ILE A O     1 
ATOM   1708 C  CB    . ILE A 1 219 ? 30.815  -3.998  -0.549  1.00 36.78  ? 219 ILE A CB    1 
ATOM   1709 C  CG1   . ILE A 1 219 ? 30.862  -5.323  0.229   1.00 42.69  ? 219 ILE A CG1   1 
ATOM   1710 C  CG2   . ILE A 1 219 ? 29.380  -3.717  -0.970  1.00 33.59  ? 219 ILE A CG2   1 
ATOM   1711 C  CD1   . ILE A 1 219 ? 31.918  -5.391  1.342   1.00 39.94  ? 219 ILE A CD1   1 
ATOM   1712 N  N     . ALA A 1 220 ? 31.604  -2.685  -3.791  1.00 37.83  ? 220 ALA A N     1 
ATOM   1713 C  CA    . ALA A 1 220 ? 31.863  -1.497  -4.592  1.00 36.03  ? 220 ALA A CA    1 
ATOM   1714 C  C     . ALA A 1 220 ? 30.577  -0.955  -5.201  1.00 35.67  ? 220 ALA A C     1 
ATOM   1715 O  O     . ALA A 1 220 ? 29.656  -1.709  -5.532  1.00 34.57  ? 220 ALA A O     1 
ATOM   1716 C  CB    . ALA A 1 220 ? 32.874  -1.795  -5.703  1.00 39.17  ? 220 ALA A CB    1 
ATOM   1717 N  N     . HIS A 1 221 ? 30.536  0.368   -5.370  1.00 34.93  ? 221 HIS A N     1 
ATOM   1718 C  CA    . HIS A 1 221 ? 29.379  1.056   -5.923  1.00 34.59  ? 221 HIS A CA    1 
ATOM   1719 C  C     . HIS A 1 221 ? 29.863  1.973   -7.031  1.00 37.54  ? 221 HIS A C     1 
ATOM   1720 O  O     . HIS A 1 221 ? 30.860  2.682   -6.858  1.00 39.24  ? 221 HIS A O     1 
ATOM   1721 C  CB    . HIS A 1 221 ? 28.641  1.878   -4.853  1.00 36.73  ? 221 HIS A CB    1 
ATOM   1722 C  CG    . HIS A 1 221 ? 28.293  1.097   -3.625  1.00 34.45  ? 221 HIS A CG    1 
ATOM   1723 N  ND1   . HIS A 1 221 ? 29.242  0.671   -2.719  1.00 35.61  ? 221 HIS A ND1   1 
ATOM   1724 C  CD2   . HIS A 1 221 ? 27.096  0.689   -3.138  1.00 33.31  ? 221 HIS A CD2   1 
ATOM   1725 C  CE1   . HIS A 1 221 ? 28.644  0.023   -1.733  1.00 35.44  ? 221 HIS A CE1   1 
ATOM   1726 N  NE2   . HIS A 1 221 ? 27.343  0.017   -1.966  1.00 33.63  ? 221 HIS A NE2   1 
ATOM   1727 N  N     . LEU A 1 222 ? 29.163  1.956   -8.162  1.00 38.24  ? 222 LEU A N     1 
ATOM   1728 C  CA    . LEU A 1 222 ? 29.541  2.730   -9.347  1.00 40.29  ? 222 LEU A CA    1 
ATOM   1729 C  C     . LEU A 1 222 ? 28.298  3.482   -9.802  1.00 45.48  ? 222 LEU A C     1 
ATOM   1730 O  O     . LEU A 1 222 ? 27.612  3.067   -10.749 1.00 43.96  ? 222 LEU A O     1 
ATOM   1731 C  CB    . LEU A 1 222 ? 30.106  1.831   -10.449 1.00 42.74  ? 222 LEU A CB    1 
ATOM   1732 C  CG    . LEU A 1 222 ? 31.425  1.126   -10.106 1.00 45.46  ? 222 LEU A CG    1 
ATOM   1733 C  CD1   . LEU A 1 222 ? 31.185  -0.252  -9.460  1.00 42.67  ? 222 LEU A CD1   1 
ATOM   1734 C  CD2   . LEU A 1 222 ? 32.322  1.004   -11.325 1.00 48.78  ? 222 LEU A CD2   1 
ATOM   1735 N  N     . PRO A 1 223 ? 27.974  4.596   -9.138  1.00 42.91  ? 223 PRO A N     1 
ATOM   1736 C  CA    . PRO A 1 223 ? 26.693  5.266   -9.415  1.00 47.19  ? 223 PRO A CA    1 
ATOM   1737 C  C     . PRO A 1 223 ? 26.538  5.698   -10.858 1.00 52.00  ? 223 PRO A C     1 
ATOM   1738 O  O     . PRO A 1 223 ? 25.420  5.644   -11.385 1.00 51.01  ? 223 PRO A O     1 
ATOM   1739 C  CB    . PRO A 1 223 ? 26.697  6.465   -8.451  1.00 47.03  ? 223 PRO A CB    1 
ATOM   1740 C  CG    . PRO A 1 223 ? 28.134  6.621   -7.983  1.00 48.02  ? 223 PRO A CG    1 
ATOM   1741 C  CD    . PRO A 1 223 ? 28.725  5.228   -8.042  1.00 42.65  ? 223 PRO A CD    1 
ATOM   1742 N  N     . ASP A 1 224 ? 27.632  6.085   -11.525 1.00 50.73  ? 224 ASP A N     1 
ATOM   1743 C  CA    . ASP A 1 224 ? 27.541  6.541   -12.909 1.00 56.77  ? 224 ASP A CA    1 
ATOM   1744 C  C     . ASP A 1 224 ? 27.125  5.419   -13.844 1.00 56.34  ? 224 ASP A C     1 
ATOM   1745 O  O     . ASP A 1 224 ? 26.489  5.675   -14.873 1.00 57.81  ? 224 ASP A O     1 
ATOM   1746 C  CB    . ASP A 1 224 ? 28.878  7.129   -13.372 1.00 62.97  ? 224 ASP A CB    1 
ATOM   1747 C  CG    . ASP A 1 224 ? 29.259  8.382   -12.616 1.00 64.10  ? 224 ASP A CG    1 
ATOM   1748 O  OD1   . ASP A 1 224 ? 28.341  9.102   -12.171 1.00 58.39  ? 224 ASP A OD1   1 
ATOM   1749 O  OD2   . ASP A 1 224 ? 30.473  8.647   -12.468 1.00 70.41  ? 224 ASP A OD2   1 
ATOM   1750 N  N     . ARG A 1 225 ? 27.481  4.180   -13.511 1.00 52.09  ? 225 ARG A N     1 
ATOM   1751 C  CA    . ARG A 1 225 ? 27.126  3.017   -14.306 1.00 52.62  ? 225 ARG A CA    1 
ATOM   1752 C  C     . ARG A 1 225 ? 25.924  2.272   -13.746 1.00 50.37  ? 225 ARG A C     1 
ATOM   1753 O  O     . ARG A 1 225 ? 25.492  1.285   -14.352 1.00 51.80  ? 225 ARG A O     1 
ATOM   1754 C  CB    . ARG A 1 225 ? 28.331  2.072   -14.416 1.00 55.65  ? 225 ARG A CB    1 
ATOM   1755 C  CG    . ARG A 1 225 ? 29.422  2.605   -15.349 1.00 66.68  ? 225 ARG A CG    1 
ATOM   1756 C  CD    . ARG A 1 225 ? 30.800  2.050   -15.020 1.00 70.80  ? 225 ARG A CD    1 
ATOM   1757 N  NE    . ARG A 1 225 ? 30.829  0.594   -15.059 1.00 72.62  ? 225 ARG A NE    1 
ATOM   1758 C  CZ    . ARG A 1 225 ? 31.221  -0.123  -16.105 1.00 81.62  ? 225 ARG A CZ    1 
ATOM   1759 N  NH1   . ARG A 1 225 ? 31.614  0.456   -17.232 1.00 85.81  ? 225 ARG A NH1   1 
ATOM   1760 N  NH2   . ARG A 1 225 ? 31.225  -1.455  -16.016 1.00 70.69  ? 225 ARG A NH2   1 
ATOM   1761 N  N     . ARG A 1 226 ? 25.378  2.739   -12.618 1.00 44.74  ? 226 ARG A N     1 
ATOM   1762 C  CA    . ARG A 1 226 ? 24.268  2.097   -11.910 1.00 49.42  ? 226 ARG A CA    1 
ATOM   1763 C  C     . ARG A 1 226 ? 24.597  0.638   -11.599 1.00 44.20  ? 226 ARG A C     1 
ATOM   1764 O  O     . ARG A 1 226 ? 23.789  -0.265  -11.810 1.00 42.80  ? 226 ARG A O     1 
ATOM   1765 C  CB    . ARG A 1 226 ? 22.954  2.216   -12.691 1.00 45.23  ? 226 ARG A CB    1 
ATOM   1766 C  CG    . ARG A 1 226 ? 22.190  3.508   -12.431 1.00 53.80  ? 226 ARG A CG    1 
ATOM   1767 C  CD    . ARG A 1 226 ? 22.512  4.556   -13.479 1.00 57.73  ? 226 ARG A CD    1 
ATOM   1768 N  NE    . ARG A 1 226 ? 21.669  5.741   -13.365 1.00 57.88  ? 226 ARG A NE    1 
ATOM   1769 C  CZ    . ARG A 1 226 ? 22.007  6.841   -12.704 1.00 59.99  ? 226 ARG A CZ    1 
ATOM   1770 N  NH1   . ARG A 1 226 ? 23.147  6.923   -12.037 1.00 55.96  ? 226 ARG A NH1   1 
ATOM   1771 N  NH2   . ARG A 1 226 ? 21.183  7.889   -12.718 1.00 63.67  ? 226 ARG A NH2   1 
ATOM   1772 N  N     . GLU A 1 227 ? 25.808  0.415   -11.102 1.00 42.30  ? 227 GLU A N     1 
ATOM   1773 C  CA    . GLU A 1 227 ? 26.309  -0.923  -10.827 1.00 41.42  ? 227 GLU A CA    1 
ATOM   1774 C  C     . GLU A 1 227 ? 26.712  -1.031  -9.370  1.00 37.33  ? 227 GLU A C     1 
ATOM   1775 O  O     . GLU A 1 227 ? 27.249  -0.082  -8.788  1.00 40.39  ? 227 GLU A O     1 
ATOM   1776 C  CB    . GLU A 1 227 ? 27.515  -1.269  -11.709 1.00 43.86  ? 227 GLU A CB    1 
ATOM   1777 C  CG    . GLU A 1 227 ? 27.151  -1.918  -13.009 1.00 47.58  ? 227 GLU A CG    1 
ATOM   1778 C  CD    . GLU A 1 227 ? 28.323  -2.029  -13.946 1.00 53.57  ? 227 GLU A CD    1 
ATOM   1779 O  OE1   . GLU A 1 227 ? 29.441  -2.336  -13.482 1.00 55.78  ? 227 GLU A OE1   1 
ATOM   1780 O  OE2   . GLU A 1 227 ? 28.122  -1.795  -15.151 1.00 61.54  ? 227 GLU A OE2   1 
ATOM   1781 N  N     . ILE A 1 228 ? 26.427  -2.191  -8.795  1.00 35.86  ? 228 ILE A N     1 
ATOM   1782 C  CA    . ILE A 1 228 ? 26.883  -2.586  -7.472  1.00 34.19  ? 228 ILE A CA    1 
ATOM   1783 C  C     . ILE A 1 228 ? 27.590  -3.917  -7.654  1.00 33.90  ? 228 ILE A C     1 
ATOM   1784 O  O     . ILE A 1 228 ? 27.012  -4.842  -8.230  1.00 32.12  ? 228 ILE A O     1 
ATOM   1785 C  CB    . ILE A 1 228 ? 25.707  -2.740  -6.485  1.00 33.99  ? 228 ILE A CB    1 
ATOM   1786 C  CG1   . ILE A 1 228 ? 24.898  -1.453  -6.384  1.00 36.92  ? 228 ILE A CG1   1 
ATOM   1787 C  CG2   . ILE A 1 228 ? 26.190  -3.186  -5.114  1.00 33.71  ? 228 ILE A CG2   1 
ATOM   1788 C  CD1   . ILE A 1 228 ? 23.663  -1.595  -5.495  1.00 33.17  ? 228 ILE A CD1   1 
ATOM   1789 N  N     . ILE A 1 229 ? 28.829  -4.015  -7.174  1.00 30.60  ? 229 ILE A N     1 
ATOM   1790 C  CA    . ILE A 1 229 ? 29.666  -5.197  -7.365  1.00 33.46  ? 229 ILE A CA    1 
ATOM   1791 C  C     . ILE A 1 229 ? 30.226  -5.612  -6.009  1.00 35.42  ? 229 ILE A C     1 
ATOM   1792 O  O     . ILE A 1 229 ? 30.965  -4.848  -5.382  1.00 36.37  ? 229 ILE A O     1 
ATOM   1793 C  CB    . ILE A 1 229 ? 30.799  -4.921  -8.366  1.00 34.59  ? 229 ILE A CB    1 
ATOM   1794 C  CG1   . ILE A 1 229 ? 30.220  -4.637  -9.749  1.00 33.13  ? 229 ILE A CG1   1 
ATOM   1795 C  CG2   . ILE A 1 229 ? 31.738  -6.085  -8.464  1.00 35.34  ? 229 ILE A CG2   1 
ATOM   1796 C  CD1   . ILE A 1 229 ? 31.270  -4.183  -10.740 1.00 40.36  ? 229 ILE A CD1   1 
ATOM   1797 N  N     . SER A 1 230 ? 29.890  -6.817  -5.557  1.00 32.86  ? 230 SER A N     1 
ATOM   1798 C  CA    . SER A 1 230 ? 30.226  -7.223  -4.197  1.00 33.41  ? 230 SER A CA    1 
ATOM   1799 C  C     . SER A 1 230 ? 30.855  -8.606  -4.229  1.00 35.90  ? 230 SER A C     1 
ATOM   1800 O  O     . SER A 1 230 ? 30.332  -9.500  -4.894  1.00 36.38  ? 230 SER A O     1 
ATOM   1801 C  CB    . SER A 1 230 ? 28.971  -7.207  -3.308  1.00 35.34  ? 230 SER A CB    1 
ATOM   1802 O  OG    . SER A 1 230 ? 29.288  -7.548  -1.976  1.00 38.50  ? 230 SER A OG    1 
ATOM   1803 N  N     . PHE A 1 231 ? 31.966  -8.782  -3.512  1.00 34.44  ? 231 PHE A N     1 
ATOM   1804 C  CA    . PHE A 1 231 ? 32.779  -9.991  -3.614  1.00 36.26  ? 231 PHE A CA    1 
ATOM   1805 C  C     . PHE A 1 231 ? 33.193  -10.458 -2.228  1.00 42.56  ? 231 PHE A C     1 
ATOM   1806 O  O     . PHE A 1 231 ? 33.677  -9.658  -1.422  1.00 40.33  ? 231 PHE A O     1 
ATOM   1807 C  CB    . PHE A 1 231 ? 34.041  -9.746  -4.458  1.00 40.56  ? 231 PHE A CB    1 
ATOM   1808 C  CG    . PHE A 1 231 ? 34.850  -10.995 -4.732  1.00 42.43  ? 231 PHE A CG    1 
ATOM   1809 C  CD1   . PHE A 1 231 ? 34.560  -11.793 -5.824  1.00 40.74  ? 231 PHE A CD1   1 
ATOM   1810 C  CD2   . PHE A 1 231 ? 35.898  -11.361 -3.903  1.00 42.50  ? 231 PHE A CD2   1 
ATOM   1811 C  CE1   . PHE A 1 231 ? 35.299  -12.937 -6.088  1.00 42.32  ? 231 PHE A CE1   1 
ATOM   1812 C  CE2   . PHE A 1 231 ? 36.639  -12.496 -4.156  1.00 44.97  ? 231 PHE A CE2   1 
ATOM   1813 C  CZ    . PHE A 1 231 ? 36.346  -13.287 -5.251  1.00 46.17  ? 231 PHE A CZ    1 
ATOM   1814 N  N     . GLY A 1 232 ? 32.998  -11.752 -1.952  1.00 38.76  ? 232 GLY A N     1 
ATOM   1815 C  CA    . GLY A 1 232 ? 33.659  -12.400 -0.844  1.00 42.13  ? 232 GLY A CA    1 
ATOM   1816 C  C     . GLY A 1 232 ? 32.872  -12.510 0.449   1.00 44.87  ? 232 GLY A C     1 
ATOM   1817 O  O     . GLY A 1 232 ? 33.278  -13.287 1.320   1.00 45.49  ? 232 GLY A O     1 
ATOM   1818 N  N     . SER A 1 233 ? 31.775  -11.774 0.615   1.00 42.27  ? 233 SER A N     1 
ATOM   1819 C  CA    . SER A 1 233 ? 31.001  -11.809 1.857   1.00 41.27  ? 233 SER A CA    1 
ATOM   1820 C  C     . SER A 1 233 ? 29.581  -12.291 1.603   1.00 43.33  ? 233 SER A C     1 
ATOM   1821 O  O     . SER A 1 233 ? 28.972  -11.945 0.585   1.00 41.10  ? 233 SER A O     1 
ATOM   1822 C  CB    . SER A 1 233 ? 30.953  -10.430 2.522   1.00 42.62  ? 233 SER A CB    1 
ATOM   1823 O  OG    . SER A 1 233 ? 29.985  -10.381 3.570   1.00 42.01  ? 233 SER A OG    1 
ATOM   1824 N  N     . GLY A 1 234 ? 29.049  -13.072 2.548   1.00 44.43  ? 234 GLY A N     1 
ATOM   1825 C  CA    . GLY A 1 234 ? 27.671  -13.523 2.500   1.00 39.13  ? 234 GLY A CA    1 
ATOM   1826 C  C     . GLY A 1 234 ? 26.740  -12.786 3.451   1.00 40.99  ? 234 GLY A C     1 
ATOM   1827 O  O     . GLY A 1 234 ? 25.516  -12.891 3.314   1.00 41.85  ? 234 GLY A O     1 
ATOM   1828 N  N     . TYR A 1 235 ? 27.296  -12.047 4.417   1.00 40.61  ? 235 TYR A N     1 
ATOM   1829 C  CA    . TYR A 1 235 ? 26.468  -11.357 5.404   1.00 41.17  ? 235 TYR A CA    1 
ATOM   1830 C  C     . TYR A 1 235 ? 25.532  -10.369 4.725   1.00 40.90  ? 235 TYR A C     1 
ATOM   1831 O  O     . TYR A 1 235 ? 25.931  -9.643  3.807   1.00 40.99  ? 235 TYR A O     1 
ATOM   1832 C  CB    . TYR A 1 235 ? 27.324  -10.608 6.432   1.00 43.42  ? 235 TYR A CB    1 
ATOM   1833 C  CG    . TYR A 1 235 ? 26.508  -9.638  7.299   1.00 47.59  ? 235 TYR A CG    1 
ATOM   1834 C  CD1   . TYR A 1 235 ? 25.763  -10.097 8.384   1.00 43.90  ? 235 TYR A CD1   1 
ATOM   1835 C  CD2   . TYR A 1 235 ? 26.482  -8.264  7.021   1.00 46.18  ? 235 TYR A CD2   1 
ATOM   1836 C  CE1   . TYR A 1 235 ? 25.005  -9.211  9.177   1.00 45.05  ? 235 TYR A CE1   1 
ATOM   1837 C  CE2   . TYR A 1 235 ? 25.727  -7.372  7.805   1.00 43.78  ? 235 TYR A CE2   1 
ATOM   1838 C  CZ    . TYR A 1 235 ? 24.992  -7.855  8.879   1.00 44.77  ? 235 TYR A CZ    1 
ATOM   1839 O  OH    . TYR A 1 235 ? 24.250  -6.974  9.657   1.00 43.04  ? 235 TYR A OH    1 
ATOM   1840 N  N     . GLY A 1 236 ? 24.304  -10.293 5.249   1.00 35.76  ? 236 GLY A N     1 
ATOM   1841 C  CA    . GLY A 1 236 ? 23.211  -9.662  4.522   1.00 39.97  ? 236 GLY A CA    1 
ATOM   1842 C  C     . GLY A 1 236 ? 23.503  -8.243  4.065   1.00 39.01  ? 236 GLY A C     1 
ATOM   1843 O  O     . GLY A 1 236 ? 23.155  -7.866  2.946   1.00 41.22  ? 236 GLY A O     1 
ATOM   1844 N  N     . GLY A 1 237 ? 24.127  -7.435  4.924   1.00 38.53  ? 237 GLY A N     1 
ATOM   1845 C  CA    . GLY A 1 237 ? 24.439  -6.065  4.541   1.00 37.57  ? 237 GLY A CA    1 
ATOM   1846 C  C     . GLY A 1 237 ? 25.367  -5.953  3.339   1.00 39.03  ? 237 GLY A C     1 
ATOM   1847 O  O     . GLY A 1 237 ? 25.326  -4.943  2.628   1.00 39.51  ? 237 GLY A O     1 
ATOM   1848 N  N     . ASN A 1 238 ? 26.204  -6.969  3.099   1.00 37.49  ? 238 ASN A N     1 
ATOM   1849 C  CA    . ASN A 1 238 ? 27.140  -6.985  1.980   1.00 39.37  ? 238 ASN A CA    1 
ATOM   1850 C  C     . ASN A 1 238 ? 26.630  -7.749  0.765   1.00 40.34  ? 238 ASN A C     1 
ATOM   1851 O  O     . ASN A 1 238 ? 27.167  -7.562  -0.333  1.00 37.42  ? 238 ASN A O     1 
ATOM   1852 C  CB    . ASN A 1 238 ? 28.471  -7.634  2.387   1.00 39.56  ? 238 ASN A CB    1 
ATOM   1853 C  CG    . ASN A 1 238 ? 29.107  -6.981  3.593   1.00 41.65  ? 238 ASN A CG    1 
ATOM   1854 O  OD1   . ASN A 1 238 ? 29.005  -5.765  3.800   1.00 39.52  ? 238 ASN A OD1   1 
ATOM   1855 N  ND2   . ASN A 1 238 ? 29.778  -7.792  4.400   1.00 42.39  ? 238 ASN A ND2   1 
ATOM   1856 N  N     . SER A 1 239 ? 25.642  -8.629  0.937   1.00 35.16  ? 239 SER A N     1 
ATOM   1857 C  CA    . SER A 1 239 ? 25.234  -9.534  -0.125  1.00 35.01  ? 239 SER A CA    1 
ATOM   1858 C  C     . SER A 1 239 ? 23.810  -9.307  -0.606  1.00 37.69  ? 239 SER A C     1 
ATOM   1859 O  O     . SER A 1 239 ? 23.485  -9.713  -1.734  1.00 34.65  ? 239 SER A O     1 
ATOM   1860 C  CB    . SER A 1 239 ? 25.374  -10.994 0.339   1.00 35.85  ? 239 SER A CB    1 
ATOM   1861 O  OG    . SER A 1 239 ? 24.412  -11.291 1.346   1.00 37.86  ? 239 SER A OG    1 
ATOM   1862 N  N     . LEU A 1 240 ? 22.949  -8.706  0.220   1.00 35.39  ? 240 LEU A N     1 
ATOM   1863 C  CA    . LEU A 1 240 ? 21.589  -8.355  -0.173  1.00 37.34  ? 240 LEU A CA    1 
ATOM   1864 C  C     . LEU A 1 240 ? 21.693  -6.957  -0.745  1.00 33.73  ? 240 LEU A C     1 
ATOM   1865 O  O     . LEU A 1 240 ? 21.552  -5.953  -0.042  1.00 37.82  ? 240 LEU A O     1 
ATOM   1866 C  CB    . LEU A 1 240 ? 20.626  -8.428  1.008   1.00 40.72  ? 240 LEU A CB    1 
ATOM   1867 C  CG    . LEU A 1 240 ? 20.674  -9.700  1.866   1.00 37.88  ? 240 LEU A CG    1 
ATOM   1868 C  CD1   . LEU A 1 240 ? 19.570  -9.667  2.914   1.00 36.54  ? 240 LEU A CD1   1 
ATOM   1869 C  CD2   . LEU A 1 240 ? 20.596  -10.989 1.059   1.00 34.37  ? 240 LEU A CD2   1 
ATOM   1870 N  N     . LEU A 1 241 ? 21.985  -6.893  -2.038  1.00 35.08  ? 241 LEU A N     1 
ATOM   1871 C  CA    . LEU A 1 241 ? 22.406  -5.646  -2.646  1.00 33.41  ? 241 LEU A CA    1 
ATOM   1872 C  C     . LEU A 1 241 ? 21.265  -4.657  -2.832  1.00 34.47  ? 241 LEU A C     1 
ATOM   1873 O  O     . LEU A 1 241 ? 21.539  -3.478  -3.061  1.00 35.44  ? 241 LEU A O     1 
ATOM   1874 C  CB    . LEU A 1 241 ? 23.096  -5.941  -3.988  1.00 31.95  ? 241 LEU A CB    1 
ATOM   1875 C  CG    . LEU A 1 241 ? 24.346  -6.829  -3.841  1.00 33.03  ? 241 LEU A CG    1 
ATOM   1876 C  CD1   . LEU A 1 241 ? 25.114  -6.973  -5.169  1.00 29.90  ? 241 LEU A CD1   1 
ATOM   1877 C  CD2   . LEU A 1 241 ? 25.245  -6.265  -2.743  1.00 33.61  ? 241 LEU A CD2   1 
ATOM   1878 N  N     . GLY A 1 242 ? 20.005  -5.090  -2.724  1.00 36.02  ? 242 GLY A N     1 
ATOM   1879 C  CA    . GLY A 1 242 ? 18.908  -4.138  -2.799  1.00 34.19  ? 242 GLY A CA    1 
ATOM   1880 C  C     . GLY A 1 242 ? 18.805  -3.206  -1.599  1.00 35.53  ? 242 GLY A C     1 
ATOM   1881 O  O     . GLY A 1 242 ? 18.205  -2.131  -1.710  1.00 39.83  ? 242 GLY A O     1 
ATOM   1882 N  N     . LYS A 1 243 ? 19.426  -3.568  -0.482  1.00 34.57  ? 243 LYS A N     1 
ATOM   1883 C  CA    . LYS A 1 243 ? 19.176  -2.944  0.808   1.00 35.72  ? 243 LYS A CA    1 
ATOM   1884 C  C     . LYS A 1 243 ? 20.060  -1.729  1.069   1.00 34.60  ? 243 LYS A C     1 
ATOM   1885 O  O     . LYS A 1 243 ? 19.681  -0.593  0.746   1.00 39.52  ? 243 LYS A O     1 
ATOM   1886 C  CB    . LYS A 1 243 ? 19.358  -4.000  1.912   1.00 31.71  ? 243 LYS A CB    1 
ATOM   1887 C  CG    . LYS A 1 243 ? 19.026  -3.483  3.329   1.00 33.20  ? 243 LYS A CG    1 
ATOM   1888 C  CD    . LYS A 1 243 ? 18.830  -4.647  4.340   1.00 29.29  ? 243 LYS A CD    1 
ATOM   1889 C  CE    . LYS A 1 243 ? 18.624  -4.137  5.778   1.00 28.81  ? 243 LYS A CE    1 
ATOM   1890 N  NZ    . LYS A 1 243 ? 17.293  -3.457  5.996   1.00 31.63  ? 243 LYS A NZ    1 
ATOM   1891 N  N     . LYS A 1 244 ? 21.227  -1.943  1.684   1.00 33.45  ? 244 LYS A N     1 
ATOM   1892 C  CA    . LYS A 1 244 ? 22.139  -0.834  1.957   1.00 29.31  ? 244 LYS A CA    1 
ATOM   1893 C  C     . LYS A 1 244 ? 22.774  -0.306  0.673   1.00 32.09  ? 244 LYS A C     1 
ATOM   1894 O  O     . LYS A 1 244 ? 22.847  0.906   0.452   1.00 30.47  ? 244 LYS A O     1 
ATOM   1895 C  CB    . LYS A 1 244 ? 23.220  -1.285  2.936   1.00 28.80  ? 244 LYS A CB    1 
ATOM   1896 C  CG    . LYS A 1 244 ? 22.665  -1.850  4.241   1.00 33.78  ? 244 LYS A CG    1 
ATOM   1897 C  CD    . LYS A 1 244 ? 21.944  -0.741  5.017   1.00 32.87  ? 244 LYS A CD    1 
ATOM   1898 C  CE    . LYS A 1 244 ? 21.404  -1.209  6.373   1.00 31.63  ? 244 LYS A CE    1 
ATOM   1899 N  NZ    . LYS A 1 244 ? 20.759  -0.046  7.125   1.00 29.79  ? 244 LYS A NZ    1 
ATOM   1900 N  N     . CYS A 1 245 ? 23.275  -1.207  -0.168  1.00 31.40  ? 245 CYS A N     1 
ATOM   1901 C  CA    . CYS A 1 245 ? 24.042  -0.793  -1.341  1.00 32.34  ? 245 CYS A CA    1 
ATOM   1902 C  C     . CYS A 1 245 ? 23.172  -0.018  -2.323  1.00 31.05  ? 245 CYS A C     1 
ATOM   1903 O  O     . CYS A 1 245 ? 23.536  1.073   -2.771  1.00 35.36  ? 245 CYS A O     1 
ATOM   1904 C  CB    . CYS A 1 245 ? 24.653  -2.034  -2.004  1.00 32.77  ? 245 CYS A CB    1 
ATOM   1905 S  SG    . CYS A 1 245 ? 25.858  -2.904  -0.969  1.00 34.44  ? 245 CYS A SG    1 
ATOM   1906 N  N     . PHE A 1 246 ? 21.999  -0.561  -2.639  1.00 34.37  ? 246 PHE A N     1 
ATOM   1907 C  CA    . PHE A 1 246 ? 21.067  0.052   -3.577  1.00 34.08  ? 246 PHE A CA    1 
ATOM   1908 C  C     . PHE A 1 246 ? 20.212  1.123   -2.884  1.00 34.98  ? 246 PHE A C     1 
ATOM   1909 O  O     . PHE A 1 246 ? 20.275  2.308   -3.235  1.00 37.66  ? 246 PHE A O     1 
ATOM   1910 C  CB    . PHE A 1 246 ? 20.243  -1.099  -4.180  1.00 33.12  ? 246 PHE A CB    1 
ATOM   1911 C  CG    . PHE A 1 246 ? 19.138  -0.724  -5.143  1.00 40.44  ? 246 PHE A CG    1 
ATOM   1912 C  CD1   . PHE A 1 246 ? 18.625  0.554   -5.261  1.00 39.34  ? 246 PHE A CD1   1 
ATOM   1913 C  CD2   . PHE A 1 246 ? 18.568  -1.734  -5.913  1.00 42.86  ? 246 PHE A CD2   1 
ATOM   1914 C  CE1   . PHE A 1 246 ? 17.578  0.825   -6.134  1.00 44.94  ? 246 PHE A CE1   1 
ATOM   1915 C  CE2   . PHE A 1 246 ? 17.537  -1.470  -6.795  1.00 44.06  ? 246 PHE A CE2   1 
ATOM   1916 C  CZ    . PHE A 1 246 ? 17.045  -0.187  -6.906  1.00 45.22  ? 246 PHE A CZ    1 
ATOM   1917 N  N     . ALA A 1 247 ? 19.407  0.726   -1.893  1.00 36.04  ? 247 ALA A N     1 
ATOM   1918 C  CA    . ALA A 1 247 ? 18.345  1.603   -1.401  1.00 35.16  ? 247 ALA A CA    1 
ATOM   1919 C  C     . ALA A 1 247 ? 18.845  2.755   -0.529  1.00 33.31  ? 247 ALA A C     1 
ATOM   1920 O  O     . ALA A 1 247 ? 18.080  3.700   -0.299  1.00 35.56  ? 247 ALA A O     1 
ATOM   1921 C  CB    . ALA A 1 247 ? 17.294  0.785   -0.633  1.00 34.16  ? 247 ALA A CB    1 
ATOM   1922 N  N     . LEU A 1 248 ? 20.092  2.719   -0.050  1.00 32.76  ? 248 LEU A N     1 
ATOM   1923 C  CA    . LEU A 1 248 ? 20.706  3.888   0.583   1.00 32.37  ? 248 LEU A CA    1 
ATOM   1924 C  C     . LEU A 1 248 ? 21.821  4.491   -0.266  1.00 35.52  ? 248 LEU A C     1 
ATOM   1925 O  O     . LEU A 1 248 ? 21.768  5.680   -0.589  1.00 35.76  ? 248 LEU A O     1 
ATOM   1926 C  CB    . LEU A 1 248 ? 21.240  3.542   1.982   1.00 31.69  ? 248 LEU A CB    1 
ATOM   1927 C  CG    . LEU A 1 248 ? 20.130  3.305   3.019   1.00 32.91  ? 248 LEU A CG    1 
ATOM   1928 C  CD1   . LEU A 1 248 ? 20.710  2.891   4.365   1.00 35.45  ? 248 LEU A CD1   1 
ATOM   1929 C  CD2   . LEU A 1 248 ? 19.281  4.541   3.182   1.00 34.22  ? 248 LEU A CD2   1 
ATOM   1930 N  N     . ARG A 1 249 ? 22.841  3.715   -0.647  1.00 31.95  ? 249 ARG A N     1 
ATOM   1931 C  CA    . ARG A 1 249 ? 24.026  4.341   -1.236  1.00 34.23  ? 249 ARG A CA    1 
ATOM   1932 C  C     . ARG A 1 249 ? 23.769  4.807   -2.665  1.00 36.54  ? 249 ARG A C     1 
ATOM   1933 O  O     . ARG A 1 249 ? 23.965  5.981   -2.988  1.00 36.37  ? 249 ARG A O     1 
ATOM   1934 C  CB    . ARG A 1 249 ? 25.227  3.395   -1.176  1.00 34.06  ? 249 ARG A CB    1 
ATOM   1935 C  CG    . ARG A 1 249 ? 25.667  3.096   0.254   1.00 36.85  ? 249 ARG A CG    1 
ATOM   1936 C  CD    . ARG A 1 249 ? 27.129  2.666   0.363   1.00 34.08  ? 249 ARG A CD    1 
ATOM   1937 N  NE    . ARG A 1 249 ? 27.395  2.077   1.670   1.00 39.27  ? 249 ARG A NE    1 
ATOM   1938 C  CZ    . ARG A 1 249 ? 27.198  0.798   1.977   1.00 39.25  ? 249 ARG A CZ    1 
ATOM   1939 N  NH1   . ARG A 1 249 ? 26.835  -0.093  1.062   1.00 33.75  ? 249 ARG A NH1   1 
ATOM   1940 N  NH2   . ARG A 1 249 ? 27.366  0.400   3.234   1.00 38.75  ? 249 ARG A NH2   1 
ATOM   1941 N  N     . ILE A 1 250 ? 23.332  3.906   -3.541  1.00 37.64  ? 250 ILE A N     1 
ATOM   1942 C  CA    . ILE A 1 250 ? 23.026  4.332   -4.903  1.00 38.81  ? 250 ILE A CA    1 
ATOM   1943 C  C     . ILE A 1 250 ? 21.829  5.280   -4.909  1.00 38.14  ? 250 ILE A C     1 
ATOM   1944 O  O     . ILE A 1 250 ? 21.824  6.298   -5.612  1.00 35.40  ? 250 ILE A O     1 
ATOM   1945 C  CB    . ILE A 1 250 ? 22.786  3.102   -5.799  1.00 36.32  ? 250 ILE A CB    1 
ATOM   1946 C  CG1   . ILE A 1 250 ? 24.082  2.289   -5.948  1.00 37.69  ? 250 ILE A CG1   1 
ATOM   1947 C  CG2   . ILE A 1 250 ? 22.246  3.524   -7.156  1.00 41.01  ? 250 ILE A CG2   1 
ATOM   1948 C  CD1   . ILE A 1 250 ? 25.176  2.981   -6.753  1.00 39.69  ? 250 ILE A CD1   1 
ATOM   1949 N  N     . ALA A 1 251 ? 20.783  4.945   -4.146  1.00 37.83  ? 251 ALA A N     1 
ATOM   1950 C  CA    . ALA A 1 251 ? 19.563  5.748   -4.164  1.00 38.21  ? 251 ALA A CA    1 
ATOM   1951 C  C     . ALA A 1 251 ? 19.790  7.144   -3.608  1.00 36.12  ? 251 ALA A C     1 
ATOM   1952 O  O     . ALA A 1 251 ? 19.147  8.097   -4.057  1.00 36.67  ? 251 ALA A O     1 
ATOM   1953 C  CB    . ALA A 1 251 ? 18.447  5.045   -3.385  1.00 33.84  ? 251 ALA A CB    1 
ATOM   1954 N  N     . SER A 1 252 ? 20.696  7.307   -2.647  1.00 34.57  ? 252 SER A N     1 
ATOM   1955 C  CA    . SER A 1 252 ? 20.873  8.661   -2.127  1.00 34.62  ? 252 SER A CA    1 
ATOM   1956 C  C     . SER A 1 252 ? 21.430  9.592   -3.199  1.00 38.07  ? 252 SER A C     1 
ATOM   1957 O  O     . SER A 1 252 ? 21.097  10.785  -3.215  1.00 35.38  ? 252 SER A O     1 
ATOM   1958 C  CB    . SER A 1 252 ? 21.762  8.660   -0.886  1.00 34.26  ? 252 SER A CB    1 
ATOM   1959 O  OG    . SER A 1 252 ? 23.092  8.304   -1.186  1.00 35.66  ? 252 SER A OG    1 
ATOM   1960 N  N     . ARG A 1 253 ? 22.241  9.067   -4.124  1.00 37.06  ? 253 ARG A N     1 
ATOM   1961 C  CA    . ARG A 1 253 ? 22.723  9.909   -5.216  1.00 38.70  ? 253 ARG A CA    1 
ATOM   1962 C  C     . ARG A 1 253 ? 21.619  10.172  -6.229  1.00 40.05  ? 253 ARG A C     1 
ATOM   1963 O  O     . ARG A 1 253 ? 21.433  11.311  -6.673  1.00 45.33  ? 253 ARG A O     1 
ATOM   1964 C  CB    . ARG A 1 253 ? 23.931  9.274   -5.903  1.00 42.18  ? 253 ARG A CB    1 
ATOM   1965 C  CG    . ARG A 1 253 ? 24.396  10.114  -7.097  1.00 47.02  ? 253 ARG A CG    1 
ATOM   1966 C  CD    . ARG A 1 253 ? 25.850  9.978   -7.315  1.00 51.14  ? 253 ARG A CD    1 
ATOM   1967 N  NE    . ARG A 1 253 ? 26.169  10.103  -8.729  1.00 55.28  ? 253 ARG A NE    1 
ATOM   1968 C  CZ    . ARG A 1 253 ? 27.402  10.182  -9.197  1.00 53.55  ? 253 ARG A CZ    1 
ATOM   1969 N  NH1   . ARG A 1 253 ? 28.445  10.214  -8.383  1.00 56.17  ? 253 ARG A NH1   1 
ATOM   1970 N  NH2   . ARG A 1 253 ? 27.595  10.236  -10.510 1.00 62.26  ? 253 ARG A NH2   1 
ATOM   1971 N  N     . LEU A 1 254 ? 20.871  9.129   -6.603  1.00 42.27  ? 254 LEU A N     1 
ATOM   1972 C  CA    . LEU A 1 254 ? 19.712  9.325   -7.469  1.00 42.74  ? 254 LEU A CA    1 
ATOM   1973 C  C     . LEU A 1 254 ? 18.756  10.351  -6.881  1.00 44.78  ? 254 LEU A C     1 
ATOM   1974 O  O     . LEU A 1 254 ? 18.196  11.176  -7.608  1.00 47.54  ? 254 LEU A O     1 
ATOM   1975 C  CB    . LEU A 1 254 ? 18.988  7.999   -7.691  1.00 44.72  ? 254 LEU A CB    1 
ATOM   1976 C  CG    . LEU A 1 254 ? 19.796  6.884   -8.350  1.00 48.36  ? 254 LEU A CG    1 
ATOM   1977 C  CD1   . LEU A 1 254 ? 18.898  5.694   -8.648  1.00 48.27  ? 254 LEU A CD1   1 
ATOM   1978 C  CD2   . LEU A 1 254 ? 20.437  7.413   -9.613  1.00 49.10  ? 254 LEU A CD2   1 
ATOM   1979 N  N     . ALA A 1 255 ? 18.563  10.313  -5.557  1.00 42.45  ? 255 ALA A N     1 
ATOM   1980 C  CA    . ALA A 1 255 ? 17.657  11.246  -4.893  1.00 40.29  ? 255 ALA A CA    1 
ATOM   1981 C  C     . ALA A 1 255 ? 18.167  12.677  -4.986  1.00 45.36  ? 255 ALA A C     1 
ATOM   1982 O  O     . ALA A 1 255 ? 17.384  13.615  -5.196  1.00 43.22  ? 255 ALA A O     1 
ATOM   1983 C  CB    . ALA A 1 255 ? 17.472  10.830  -3.432  1.00 40.08  ? 255 ALA A CB    1 
ATOM   1984 N  N     . LYS A 1 256 ? 19.478  12.864  -4.820  1.00 42.64  ? 256 LYS A N     1 
ATOM   1985 C  CA    . LYS A 1 256 ? 20.070  14.179  -5.018  1.00 42.49  ? 256 LYS A CA    1 
ATOM   1986 C  C     . LYS A 1 256 ? 19.786  14.689  -6.425  1.00 43.21  ? 256 LYS A C     1 
ATOM   1987 O  O     . LYS A 1 256 ? 19.371  15.835  -6.604  1.00 45.87  ? 256 LYS A O     1 
ATOM   1988 C  CB    . LYS A 1 256 ? 21.576  14.114  -4.760  1.00 41.14  ? 256 LYS A CB    1 
ATOM   1989 C  CG    . LYS A 1 256 ? 22.320  15.376  -5.159  1.00 47.07  ? 256 LYS A CG    1 
ATOM   1990 C  CD    . LYS A 1 256 ? 21.908  16.550  -4.280  1.00 42.70  ? 256 LYS A CD    1 
ATOM   1991 C  CE    . LYS A 1 256 ? 22.459  17.867  -4.816  1.00 52.88  ? 256 LYS A CE    1 
ATOM   1992 N  NZ    . LYS A 1 256 ? 23.781  17.673  -5.476  1.00 58.74  ? 256 LYS A NZ    1 
ATOM   1993 N  N     . GLU A 1 257 ? 19.973  13.828  -7.432  1.00 45.05  ? 257 GLU A N     1 
ATOM   1994 C  CA    . GLU A 1 257 ? 19.783  14.227  -8.825  1.00 49.16  ? 257 GLU A CA    1 
ATOM   1995 C  C     . GLU A 1 257 ? 18.321  14.487  -9.156  1.00 49.29  ? 257 GLU A C     1 
ATOM   1996 O  O     . GLU A 1 257 ? 18.028  15.295  -10.042 1.00 50.81  ? 257 GLU A O     1 
ATOM   1997 C  CB    . GLU A 1 257 ? 20.306  13.143  -9.777  1.00 52.66  ? 257 GLU A CB    1 
ATOM   1998 C  CG    . GLU A 1 257 ? 21.771  12.762  -9.651  1.00 54.63  ? 257 GLU A CG    1 
ATOM   1999 C  CD    . GLU A 1 257 ? 22.070  11.445  -10.356 1.00 61.96  ? 257 GLU A CD    1 
ATOM   2000 O  OE1   . GLU A 1 257 ? 21.256  11.037  -11.218 1.00 65.47  ? 257 GLU A OE1   1 
ATOM   2001 O  OE2   . GLU A 1 257 ? 23.097  10.803  -10.037 1.00 64.15  ? 257 GLU A OE2   1 
ATOM   2002 N  N     . GLU A 1 258 ? 17.394  13.784  -8.507  1.00 47.45  ? 258 GLU A N     1 
ATOM   2003 C  CA    . GLU A 1 258 ? 15.990  13.831  -8.896  1.00 46.62  ? 258 GLU A CA    1 
ATOM   2004 C  C     . GLU A 1 258 ? 15.104  14.570  -7.905  1.00 47.14  ? 258 GLU A C     1 
ATOM   2005 O  O     . GLU A 1 258 ? 13.907  14.721  -8.169  1.00 50.37  ? 258 GLU A O     1 
ATOM   2006 C  CB    . GLU A 1 258 ? 15.448  12.412  -9.096  1.00 49.83  ? 258 GLU A CB    1 
ATOM   2007 C  CG    . GLU A 1 258 ? 16.145  11.609  -10.169 1.00 50.09  ? 258 GLU A CG    1 
ATOM   2008 C  CD    . GLU A 1 258 ? 15.795  10.141  -10.080 1.00 53.91  ? 258 GLU A CD    1 
ATOM   2009 O  OE1   . GLU A 1 258 ? 14.801  9.813   -9.403  1.00 57.22  ? 258 GLU A OE1   1 
ATOM   2010 O  OE2   . GLU A 1 258 ? 16.510  9.308   -10.675 1.00 60.04  ? 258 GLU A OE2   1 
ATOM   2011 N  N     . GLY A 1 259 ? 15.643  15.020  -6.774  1.00 47.81  ? 259 GLY A N     1 
ATOM   2012 C  CA    . GLY A 1 259 ? 14.877  15.848  -5.860  1.00 47.62  ? 259 GLY A CA    1 
ATOM   2013 C  C     . GLY A 1 259 ? 14.087  15.117  -4.795  1.00 48.75  ? 259 GLY A C     1 
ATOM   2014 O  O     . GLY A 1 259 ? 13.010  15.584  -4.409  1.00 52.55  ? 259 GLY A O     1 
ATOM   2015 N  N     . TRP A 1 260 ? 14.579  13.989  -4.299  1.00 43.47  ? 260 TRP A N     1 
ATOM   2016 C  CA    . TRP A 1 260 ? 13.932  13.298  -3.188  1.00 42.22  ? 260 TRP A CA    1 
ATOM   2017 C  C     . TRP A 1 260 ? 15.007  12.930  -2.169  1.00 38.85  ? 260 TRP A C     1 
ATOM   2018 O  O     . TRP A 1 260 ? 16.104  13.494  -2.142  1.00 41.63  ? 260 TRP A O     1 
ATOM   2019 C  CB    . TRP A 1 260 ? 13.107  12.093  -3.676  1.00 43.06  ? 260 TRP A CB    1 
ATOM   2020 C  CG    . TRP A 1 260 ? 13.765  11.131  -4.659  1.00 46.87  ? 260 TRP A CG    1 
ATOM   2021 C  CD1   . TRP A 1 260 ? 14.001  11.348  -5.989  1.00 47.02  ? 260 TRP A CD1   1 
ATOM   2022 C  CD2   . TRP A 1 260 ? 14.179  9.779   -4.398  1.00 41.51  ? 260 TRP A CD2   1 
ATOM   2023 N  NE1   . TRP A 1 260 ? 14.562  10.227  -6.560  1.00 43.74  ? 260 TRP A NE1   1 
ATOM   2024 C  CE2   . TRP A 1 260 ? 14.694  9.256   -5.605  1.00 42.91  ? 260 TRP A CE2   1 
ATOM   2025 C  CE3   . TRP A 1 260 ? 14.191  8.974   -3.257  1.00 39.64  ? 260 TRP A CE3   1 
ATOM   2026 C  CZ2   . TRP A 1 260 ? 15.196  7.953   -5.707  1.00 43.26  ? 260 TRP A CZ2   1 
ATOM   2027 C  CZ3   . TRP A 1 260 ? 14.702  7.677   -3.356  1.00 38.85  ? 260 TRP A CZ3   1 
ATOM   2028 C  CH2   . TRP A 1 260 ? 15.193  7.182   -4.575  1.00 39.40  ? 260 TRP A CH2   1 
ATOM   2029 N  N     . LEU A 1 261 ? 14.701  11.970  -1.306  1.00 37.99  ? 261 LEU A N     1 
ATOM   2030 C  CA    . LEU A 1 261 ? 15.560  11.625  -0.184  1.00 35.22  ? 261 LEU A CA    1 
ATOM   2031 C  C     . LEU A 1 261 ? 15.527  10.125  0.024   1.00 36.55  ? 261 LEU A C     1 
ATOM   2032 O  O     . LEU A 1 261 ? 14.466  9.506   -0.087  1.00 39.29  ? 261 LEU A O     1 
ATOM   2033 C  CB    . LEU A 1 261 ? 15.099  12.313  1.117   1.00 32.98  ? 261 LEU A CB    1 
ATOM   2034 C  CG    . LEU A 1 261 ? 15.141  13.839  1.179   1.00 34.83  ? 261 LEU A CG    1 
ATOM   2035 C  CD1   . LEU A 1 261 ? 14.430  14.324  2.434   1.00 37.52  ? 261 LEU A CD1   1 
ATOM   2036 C  CD2   . LEU A 1 261 ? 16.567  14.367  1.161   1.00 36.11  ? 261 LEU A CD2   1 
ATOM   2037 N  N     . ALA A 1 262 ? 16.685  9.551   0.348   1.00 33.86  ? 262 ALA A N     1 
ATOM   2038 C  CA    . ALA A 1 262 ? 16.807  8.141   0.701   1.00 31.14  ? 262 ALA A CA    1 
ATOM   2039 C  C     . ALA A 1 262 ? 17.594  8.064   1.997   1.00 31.69  ? 262 ALA A C     1 
ATOM   2040 O  O     . ALA A 1 262 ? 18.767  8.447   2.030   1.00 27.99  ? 262 ALA A O     1 
ATOM   2041 C  CB    . ALA A 1 262 ? 17.507  7.342   -0.407  1.00 33.50  ? 262 ALA A CB    1 
ATOM   2042 N  N     . GLU A 1 263 ? 16.960  7.569   3.061   1.00 32.36  ? 263 GLU A N     1 
ATOM   2043 C  CA    . GLU A 1 263 ? 17.472  7.806   4.402   1.00 32.68  ? 263 GLU A CA    1 
ATOM   2044 C  C     . GLU A 1 263 ? 17.399  6.547   5.244   1.00 31.92  ? 263 GLU A C     1 
ATOM   2045 O  O     . GLU A 1 263 ? 16.592  5.649   4.997   1.00 29.80  ? 263 GLU A O     1 
ATOM   2046 C  CB    . GLU A 1 263 ? 16.692  8.907   5.130   1.00 32.45  ? 263 GLU A CB    1 
ATOM   2047 C  CG    . GLU A 1 263 ? 16.687  10.224  4.421   1.00 30.31  ? 263 GLU A CG    1 
ATOM   2048 C  CD    . GLU A 1 263 ? 18.051  10.870  4.350   1.00 33.82  ? 263 GLU A CD    1 
ATOM   2049 O  OE1   . GLU A 1 263 ? 18.954  10.511  5.141   1.00 31.67  ? 263 GLU A OE1   1 
ATOM   2050 O  OE2   . GLU A 1 263 ? 18.214  11.748  3.489   1.00 34.23  ? 263 GLU A OE2   1 
ATOM   2051 N  N     . HIS A 1 264 ? 18.242  6.525   6.273   1.00 29.51  ? 264 HIS A N     1 
ATOM   2052 C  CA    . HIS A 1 264 ? 18.347  5.382   7.181   1.00 31.35  ? 264 HIS A CA    1 
ATOM   2053 C  C     . HIS A 1 264 ? 17.343  5.578   8.325   1.00 29.87  ? 264 HIS A C     1 
ATOM   2054 O  O     . HIS A 1 264 ? 17.704  5.804   9.477   1.00 29.05  ? 264 HIS A O     1 
ATOM   2055 C  CB    . HIS A 1 264 ? 19.790  5.266   7.679   1.00 30.40  ? 264 HIS A CB    1 
ATOM   2056 C  CG    . HIS A 1 264 ? 20.076  4.029   8.477   1.00 27.97  ? 264 HIS A CG    1 
ATOM   2057 N  ND1   . HIS A 1 264 ? 21.086  3.972   9.418   1.00 27.66  ? 264 HIS A ND1   1 
ATOM   2058 C  CD2   . HIS A 1 264 ? 19.504  2.800   8.462   1.00 27.68  ? 264 HIS A CD2   1 
ATOM   2059 C  CE1   . HIS A 1 264 ? 21.120  2.761   9.951   1.00 31.10  ? 264 HIS A CE1   1 
ATOM   2060 N  NE2   . HIS A 1 264 ? 20.163  2.038   9.399   1.00 26.79  ? 264 HIS A NE2   1 
ATOM   2061 N  N     . MET A 1 265 ? 16.050  5.502   7.978   1.00 28.85  ? 265 MET A N     1 
ATOM   2062 C  CA    . MET A 1 265 ? 14.980  5.864   8.909   1.00 30.52  ? 265 MET A CA    1 
ATOM   2063 C  C     . MET A 1 265 ? 13.881  4.813   8.965   1.00 33.03  ? 265 MET A C     1 
ATOM   2064 O  O     . MET A 1 265 ? 13.506  4.232   7.941   1.00 35.59  ? 265 MET A O     1 
ATOM   2065 C  CB    . MET A 1 265 ? 14.320  7.188   8.513   1.00 29.67  ? 265 MET A CB    1 
ATOM   2066 C  CG    . MET A 1 265 ? 15.162  8.419   8.749   1.00 32.94  ? 265 MET A CG    1 
ATOM   2067 S  SD    . MET A 1 265 ? 14.415  9.872   7.974   1.00 33.97  ? 265 MET A SD    1 
ATOM   2068 C  CE    . MET A 1 265 ? 15.631  11.119  8.375   1.00 36.59  ? 265 MET A CE    1 
ATOM   2069 N  N     . LEU A 1 266 ? 13.327  4.617   10.162  1.00 34.96  ? 266 LEU A N     1 
ATOM   2070 C  CA    . LEU A 1 266 ? 12.035  3.957   10.302  1.00 30.54  ? 266 LEU A CA    1 
ATOM   2071 C  C     . LEU A 1 266 ? 10.895  4.901   9.925   1.00 32.00  ? 266 LEU A C     1 
ATOM   2072 O  O     . LEU A 1 266 ? 11.041  6.132   9.918   1.00 31.73  ? 266 LEU A O     1 
ATOM   2073 C  CB    . LEU A 1 266 ? 11.834  3.474   11.736  1.00 30.45  ? 266 LEU A CB    1 
ATOM   2074 C  CG    . LEU A 1 266 ? 11.717  4.557   12.823  1.00 34.87  ? 266 LEU A CG    1 
ATOM   2075 C  CD1   . LEU A 1 266 ? 10.262  4.916   13.091  1.00 33.87  ? 266 LEU A CD1   1 
ATOM   2076 C  CD2   . LEU A 1 266 ? 12.368  4.084   14.098  1.00 32.58  ? 266 LEU A CD2   1 
ATOM   2077 N  N     . ILE A 1 267 ? 9.733   4.308   9.648   1.00 31.63  ? 267 ILE A N     1 
ATOM   2078 C  CA    . ILE A 1 267 ? 8.480   5.042   9.456   1.00 31.72  ? 267 ILE A CA    1 
ATOM   2079 C  C     . ILE A 1 267 ? 7.421   4.365   10.315  1.00 33.57  ? 267 ILE A C     1 
ATOM   2080 O  O     . ILE A 1 267 ? 7.178   3.154   10.170  1.00 37.47  ? 267 ILE A O     1 
ATOM   2081 C  CB    . ILE A 1 267 ? 8.025   5.065   7.987   1.00 33.99  ? 267 ILE A CB    1 
ATOM   2082 C  CG1   . ILE A 1 267 ? 9.115   5.615   7.064   1.00 34.60  ? 267 ILE A CG1   1 
ATOM   2083 C  CG2   . ILE A 1 267 ? 6.760   5.872   7.824   1.00 35.63  ? 267 ILE A CG2   1 
ATOM   2084 C  CD1   . ILE A 1 267 ? 8.954   5.112   5.631   1.00 33.60  ? 267 ILE A CD1   1 
ATOM   2085 N  N     . LEU A 1 268 ? 6.798   5.129   11.211  1.00 32.45  ? 268 LEU A N     1 
ATOM   2086 C  CA    . LEU A 1 268 ? 5.716   4.602   12.031  1.00 35.05  ? 268 LEU A CA    1 
ATOM   2087 C  C     . LEU A 1 268 ? 4.521   5.541   11.969  1.00 37.14  ? 268 LEU A C     1 
ATOM   2088 O  O     . LEU A 1 268 ? 4.644   6.740   11.691  1.00 39.50  ? 268 LEU A O     1 
ATOM   2089 C  CB    . LEU A 1 268 ? 6.160   4.368   13.492  1.00 34.84  ? 268 LEU A CB    1 
ATOM   2090 C  CG    . LEU A 1 268 ? 6.637   5.505   14.406  1.00 38.88  ? 268 LEU A CG    1 
ATOM   2091 C  CD1   . LEU A 1 268 ? 5.463   6.266   14.980  1.00 37.94  ? 268 LEU A CD1   1 
ATOM   2092 C  CD2   . LEU A 1 268 ? 7.499   4.949   15.538  1.00 39.50  ? 268 LEU A CD2   1 
ATOM   2093 N  N     . GLY A 1 269 ? 3.349   4.979   12.227  1.00 37.70  ? 269 GLY A N     1 
ATOM   2094 C  CA    . GLY A 1 269 ? 2.139   5.760   12.412  1.00 37.74  ? 269 GLY A CA    1 
ATOM   2095 C  C     . GLY A 1 269 ? 1.709   5.603   13.859  1.00 40.85  ? 269 GLY A C     1 
ATOM   2096 O  O     . GLY A 1 269 ? 1.713   4.491   14.395  1.00 40.99  ? 269 GLY A O     1 
ATOM   2097 N  N     . ILE A 1 270 ? 1.355   6.712   14.487  1.00 37.82  ? 270 ILE A N     1 
ATOM   2098 C  CA    . ILE A 1 270 ? 0.918   6.694   15.873  1.00 40.47  ? 270 ILE A CA    1 
ATOM   2099 C  C     . ILE A 1 270 ? -0.455  7.351   15.962  1.00 43.26  ? 270 ILE A C     1 
ATOM   2100 O  O     . ILE A 1 270 ? -0.662  8.450   15.434  1.00 43.71  ? 270 ILE A O     1 
ATOM   2101 C  CB    . ILE A 1 270 ? 1.958   7.374   16.783  1.00 42.95  ? 270 ILE A CB    1 
ATOM   2102 C  CG1   . ILE A 1 270 ? 1.480   7.384   18.237  1.00 45.22  ? 270 ILE A CG1   1 
ATOM   2103 C  CG2   . ILE A 1 270 ? 2.308   8.770   16.268  1.00 42.89  ? 270 ILE A CG2   1 
ATOM   2104 C  CD1   . ILE A 1 270 ? 2.538   7.855   19.206  1.00 42.83  ? 270 ILE A CD1   1 
ATOM   2105 N  N     . THR A 1 271 ? -1.395  6.666   16.605  1.00 41.99  ? 271 THR A N     1 
ATOM   2106 C  CA    . THR A 1 271 ? -2.756  7.156   16.799  1.00 44.09  ? 271 THR A CA    1 
ATOM   2107 C  C     . THR A 1 271 ? -2.990  7.450   18.272  1.00 49.15  ? 271 THR A C     1 
ATOM   2108 O  O     . THR A 1 271 ? -2.588  6.666   19.139  1.00 45.46  ? 271 THR A O     1 
ATOM   2109 C  CB    . THR A 1 271 ? -3.782  6.122   16.312  1.00 45.65  ? 271 THR A CB    1 
ATOM   2110 O  OG1   . THR A 1 271 ? -3.482  5.762   14.954  1.00 49.78  ? 271 THR A OG1   1 
ATOM   2111 C  CG2   . THR A 1 271 ? -5.208  6.661   16.412  1.00 48.33  ? 271 THR A CG2   1 
ATOM   2112 N  N     . ASN A 1 272 ? -3.672  8.556   18.556  1.00 46.56  ? 272 ASN A N     1 
ATOM   2113 C  CA    . ASN A 1 272 ? -3.878  9.001   19.920  1.00 48.04  ? 272 ASN A CA    1 
ATOM   2114 C  C     . ASN A 1 272 ? -5.290  8.642   20.392  1.00 52.42  ? 272 ASN A C     1 
ATOM   2115 O  O     . ASN A 1 272 ? -6.106  8.109   19.629  1.00 50.76  ? 272 ASN A O     1 
ATOM   2116 C  CB    . ASN A 1 272 ? -3.562  10.515  20.022  1.00 47.93  ? 272 ASN A CB    1 
ATOM   2117 C  CG    . ASN A 1 272 ? -4.723  11.437  19.609  1.00 49.22  ? 272 ASN A CG    1 
ATOM   2118 O  OD1   . ASN A 1 272 ? -5.702  11.025  18.998  1.00 49.94  ? 272 ASN A OD1   1 
ATOM   2119 N  ND2   . ASN A 1 272 ? -4.579  12.725  19.936  1.00 49.60  ? 272 ASN A ND2   1 
ATOM   2120 N  N     . PRO A 1 273 ? -5.607  8.857   21.674  1.00 52.18  ? 273 PRO A N     1 
ATOM   2121 C  CA    . PRO A 1 273 ? -6.947  8.470   22.146  1.00 54.62  ? 273 PRO A CA    1 
ATOM   2122 C  C     . PRO A 1 273 ? -8.077  9.291   21.537  1.00 55.77  ? 273 PRO A C     1 
ATOM   2123 O  O     . PRO A 1 273 ? -9.235  8.878   21.631  1.00 59.27  ? 273 PRO A O     1 
ATOM   2124 C  CB    . PRO A 1 273 ? -6.864  8.673   23.665  1.00 56.25  ? 273 PRO A CB    1 
ATOM   2125 C  CG    . PRO A 1 273 ? -5.419  8.672   23.988  1.00 54.55  ? 273 PRO A CG    1 
ATOM   2126 C  CD    . PRO A 1 273 ? -4.730  9.255   22.792  1.00 52.24  ? 273 PRO A CD    1 
ATOM   2127 N  N     . GLU A 1 274 ? -7.791  10.437  20.922  1.00 54.81  ? 274 GLU A N     1 
ATOM   2128 C  CA    . GLU A 1 274 ? -8.820  11.260  20.296  1.00 55.93  ? 274 GLU A CA    1 
ATOM   2129 C  C     . GLU A 1 274 ? -9.091  10.870  18.842  1.00 55.61  ? 274 GLU A C     1 
ATOM   2130 O  O     . GLU A 1 274 ? -9.788  11.606  18.138  1.00 55.61  ? 274 GLU A O     1 
ATOM   2131 C  CB    . GLU A 1 274 ? -8.430  12.739  20.362  1.00 55.63  ? 274 GLU A CB    1 
ATOM   2132 C  CG    . GLU A 1 274 ? -8.142  13.271  21.764  1.00 56.71  ? 274 GLU A CG    1 
ATOM   2133 C  CD    . GLU A 1 274 ? -9.377  13.399  22.642  1.00 61.68  ? 274 GLU A CD    1 
ATOM   2134 O  OE1   . GLU A 1 274 ? -10.519 13.238  22.147  1.00 60.99  ? 274 GLU A OE1   1 
ATOM   2135 O  OE2   . GLU A 1 274 ? -9.204  13.679  23.847  1.00 66.72  ? 274 GLU A OE2   1 
ATOM   2136 N  N     . GLY A 1 275 ? -8.543  9.751   18.375  1.00 53.51  ? 275 GLY A N     1 
ATOM   2137 C  CA    . GLY A 1 275 ? -8.793  9.292   17.020  1.00 53.77  ? 275 GLY A CA    1 
ATOM   2138 C  C     . GLY A 1 275 ? -7.965  9.948   15.929  1.00 56.40  ? 275 GLY A C     1 
ATOM   2139 O  O     . GLY A 1 275 ? -8.313  9.823   14.748  1.00 56.82  ? 275 GLY A O     1 
ATOM   2140 N  N     . LYS A 1 276 ? -6.873  10.628  16.275  1.00 50.11  ? 276 LYS A N     1 
ATOM   2141 C  CA    . LYS A 1 276 ? -6.005  11.275  15.302  1.00 49.29  ? 276 LYS A CA    1 
ATOM   2142 C  C     . LYS A 1 276 ? -4.725  10.474  15.131  1.00 47.95  ? 276 LYS A C     1 
ATOM   2143 O  O     . LYS A 1 276 ? -4.159  9.977   16.108  1.00 49.37  ? 276 LYS A O     1 
ATOM   2144 C  CB    . LYS A 1 276 ? -5.641  12.701  15.725  1.00 53.74  ? 276 LYS A CB    1 
ATOM   2145 C  CG    . LYS A 1 276 ? -6.639  13.768  15.335  1.00 57.18  ? 276 LYS A CG    1 
ATOM   2146 C  CD    . LYS A 1 276 ? -7.741  13.834  16.343  1.00 52.86  ? 276 LYS A CD    1 
ATOM   2147 C  CE    . LYS A 1 276 ? -8.595  15.058  16.179  1.00 52.95  ? 276 LYS A CE    1 
ATOM   2148 N  NZ    . LYS A 1 276 ? -9.739  14.955  17.128  1.00 55.46  ? 276 LYS A NZ    1 
ATOM   2149 N  N     . LYS A 1 277 ? -4.257  10.380  13.892  1.00 45.08  ? 277 LYS A N     1 
ATOM   2150 C  CA    . LYS A 1 277 ? -3.079  9.604   13.558  1.00 42.02  ? 277 LYS A CA    1 
ATOM   2151 C  C     . LYS A 1 277 ? -2.091  10.466  12.781  1.00 43.61  ? 277 LYS A C     1 
ATOM   2152 O  O     . LYS A 1 277 ? -2.483  11.204  11.874  1.00 44.94  ? 277 LYS A O     1 
ATOM   2153 C  CB    . LYS A 1 277 ? -3.469  8.377   12.737  1.00 45.41  ? 277 LYS A CB    1 
ATOM   2154 C  CG    . LYS A 1 277 ? -2.309  7.511   12.326  1.00 42.02  ? 277 LYS A CG    1 
ATOM   2155 C  CD    . LYS A 1 277 ? -2.804  6.258   11.576  1.00 42.02  ? 277 LYS A CD    1 
ATOM   2156 C  CE    . LYS A 1 277 ? -1.646  5.334   11.230  1.00 43.20  ? 277 LYS A CE    1 
ATOM   2157 N  NZ    . LYS A 1 277 ? -2.099  4.084   10.524  1.00 41.75  ? 277 LYS A NZ    1 
ATOM   2158 N  N     . LYS A 1 278 ? -0.811  10.362  13.142  1.00 39.44  ? 278 LYS A N     1 
ATOM   2159 C  CA    . LYS A 1 278 ? 0.280   11.027  12.445  1.00 38.92  ? 278 LYS A CA    1 
ATOM   2160 C  C     . LYS A 1 278 ? 1.397   10.027  12.189  1.00 42.62  ? 278 LYS A C     1 
ATOM   2161 O  O     . LYS A 1 278 ? 1.580   9.064   12.940  1.00 40.72  ? 278 LYS A O     1 
ATOM   2162 C  CB    . LYS A 1 278 ? 0.832   12.202  13.253  1.00 39.81  ? 278 LYS A CB    1 
ATOM   2163 C  CG    . LYS A 1 278 ? -0.195  13.256  13.606  1.00 42.03  ? 278 LYS A CG    1 
ATOM   2164 C  CD    . LYS A 1 278 ? 0.424   14.376  14.426  1.00 42.60  ? 278 LYS A CD    1 
ATOM   2165 C  CE    . LYS A 1 278 ? -0.610  15.462  14.729  1.00 45.76  ? 278 LYS A CE    1 
ATOM   2166 N  NZ    . LYS A 1 278 ? -1.132  16.024  13.454  1.00 44.23  ? 278 LYS A NZ    1 
ATOM   2167 N  N     . TYR A 1 279 ? 2.151   10.268  11.123  1.00 39.74  ? 279 TYR A N     1 
ATOM   2168 C  CA    . TYR A 1 279 ? 3.313   9.460   10.806  1.00 34.25  ? 279 TYR A CA    1 
ATOM   2169 C  C     . TYR A 1 279 ? 4.592   10.204  11.156  1.00 37.45  ? 279 TYR A C     1 
ATOM   2170 O  O     . TYR A 1 279 ? 4.695   11.429  10.971  1.00 38.28  ? 279 TYR A O     1 
ATOM   2171 C  CB    . TYR A 1 279 ? 3.317   9.062   9.328   1.00 37.81  ? 279 TYR A CB    1 
ATOM   2172 C  CG    . TYR A 1 279 ? 2.222   8.063   8.975   1.00 39.76  ? 279 TYR A CG    1 
ATOM   2173 C  CD1   . TYR A 1 279 ? 0.922   8.484   8.732   1.00 39.04  ? 279 TYR A CD1   1 
ATOM   2174 C  CD2   . TYR A 1 279 ? 2.499   6.704   8.864   1.00 38.88  ? 279 TYR A CD2   1 
ATOM   2175 C  CE1   . TYR A 1 279 ? -0.090  7.573   8.400   1.00 39.52  ? 279 TYR A CE1   1 
ATOM   2176 C  CE2   . TYR A 1 279 ? 1.497   5.789   8.531   1.00 43.83  ? 279 TYR A CE2   1 
ATOM   2177 C  CZ    . TYR A 1 279 ? 0.206   6.232   8.297   1.00 43.08  ? 279 TYR A CZ    1 
ATOM   2178 O  OH    . TYR A 1 279 ? -0.802  5.331   7.975   1.00 44.71  ? 279 TYR A OH    1 
ATOM   2179 N  N     . LEU A 1 280 ? 5.568   9.451   11.649  1.00 36.67  ? 280 LEU A N     1 
ATOM   2180 C  CA    . LEU A 1 280 ? 6.865   9.972   12.050  1.00 34.11  ? 280 LEU A CA    1 
ATOM   2181 C  C     . LEU A 1 280 ? 7.963   9.116   11.436  1.00 32.59  ? 280 LEU A C     1 
ATOM   2182 O  O     . LEU A 1 280 ? 7.793   7.912   11.237  1.00 34.49  ? 280 LEU A O     1 
ATOM   2183 C  CB    . LEU A 1 280 ? 7.016   9.963   13.580  1.00 38.05  ? 280 LEU A CB    1 
ATOM   2184 C  CG    . LEU A 1 280 ? 5.959   10.707  14.403  1.00 42.58  ? 280 LEU A CG    1 
ATOM   2185 C  CD1   . LEU A 1 280 ? 6.161   10.495  15.905  1.00 45.50  ? 280 LEU A CD1   1 
ATOM   2186 C  CD2   . LEU A 1 280 ? 5.992   12.177  14.080  1.00 39.40  ? 280 LEU A CD2   1 
ATOM   2187 N  N     . ALA A 1 281 ? 9.104   9.736   11.172  1.00 33.87  ? 281 ALA A N     1 
ATOM   2188 C  CA    . ALA A 1 281 ? 10.296  9.030   10.734  1.00 33.82  ? 281 ALA A CA    1 
ATOM   2189 C  C     . ALA A 1 281 ? 11.411  9.247   11.752  1.00 32.00  ? 281 ALA A C     1 
ATOM   2190 O  O     . ALA A 1 281 ? 11.477  10.284  12.397  1.00 34.39  ? 281 ALA A O     1 
ATOM   2191 C  CB    . ALA A 1 281 ? 10.735  9.508   9.345   1.00 31.22  ? 281 ALA A CB    1 
ATOM   2192 N  N     . ALA A 1 282 ? 12.297  8.267   11.903  1.00 31.12  ? 282 ALA A N     1 
ATOM   2193 C  CA    . ALA A 1 282 ? 13.381  8.403   12.873  1.00 31.66  ? 282 ALA A CA    1 
ATOM   2194 C  C     . ALA A 1 282 ? 14.653  7.781   12.325  1.00 32.72  ? 282 ALA A C     1 
ATOM   2195 O  O     . ALA A 1 282 ? 14.628  6.623   11.906  1.00 31.11  ? 282 ALA A O     1 
ATOM   2196 C  CB    . ALA A 1 282 ? 13.032  7.739   14.204  1.00 29.68  ? 282 ALA A CB    1 
ATOM   2197 N  N     . ALA A 1 283 ? 15.762  8.533   12.394  1.00 31.36  ? 283 ALA A N     1 
ATOM   2198 C  CA    . ALA A 1 283 ? 17.097  8.090   12.000  1.00 32.53  ? 283 ALA A CA    1 
ATOM   2199 C  C     . ALA A 1 283 ? 17.935  7.881   13.256  1.00 29.87  ? 283 ALA A C     1 
ATOM   2200 O  O     . ALA A 1 283 ? 18.333  8.848   13.907  1.00 29.18  ? 283 ALA A O     1 
ATOM   2201 C  CB    . ALA A 1 283 ? 17.770  9.115   11.076  1.00 30.47  ? 283 ALA A CB    1 
ATOM   2202 N  N     . PHE A 1 284 ? 18.185  6.620   13.605  1.00 33.56  ? 284 PHE A N     1 
ATOM   2203 C  CA    . PHE A 1 284 ? 19.159  6.238   14.613  1.00 31.25  ? 284 PHE A CA    1 
ATOM   2204 C  C     . PHE A 1 284 ? 20.229  5.394   13.935  1.00 33.42  ? 284 PHE A C     1 
ATOM   2205 O  O     . PHE A 1 284 ? 19.930  4.703   12.955  1.00 29.07  ? 284 PHE A O     1 
ATOM   2206 C  CB    . PHE A 1 284 ? 18.553  5.408   15.754  1.00 32.94  ? 284 PHE A CB    1 
ATOM   2207 C  CG    . PHE A 1 284 ? 17.293  5.973   16.336  1.00 33.37  ? 284 PHE A CG    1 
ATOM   2208 C  CD1   . PHE A 1 284 ? 17.140  7.352   16.515  1.00 32.41  ? 284 PHE A CD1   1 
ATOM   2209 C  CD2   . PHE A 1 284 ? 16.269  5.122   16.725  1.00 34.78  ? 284 PHE A CD2   1 
ATOM   2210 C  CE1   . PHE A 1 284 ? 15.977  7.870   17.068  1.00 34.11  ? 284 PHE A CE1   1 
ATOM   2211 C  CE2   . PHE A 1 284 ? 15.101  5.625   17.283  1.00 36.93  ? 284 PHE A CE2   1 
ATOM   2212 C  CZ    . PHE A 1 284 ? 14.953  7.016   17.448  1.00 35.30  ? 284 PHE A CZ    1 
ATOM   2213 N  N     . PRO A 1 285 ? 21.472  5.416   14.420  1.00 33.43  ? 285 PRO A N     1 
ATOM   2214 C  CA    . PRO A 1 285 ? 22.524  4.623   13.773  1.00 31.19  ? 285 PRO A CA    1 
ATOM   2215 C  C     . PRO A 1 285 ? 22.213  3.134   13.880  1.00 36.14  ? 285 PRO A C     1 
ATOM   2216 O  O     . PRO A 1 285 ? 21.260  2.715   14.540  1.00 33.08  ? 285 PRO A O     1 
ATOM   2217 C  CB    . PRO A 1 285 ? 23.787  5.003   14.548  1.00 35.57  ? 285 PRO A CB    1 
ATOM   2218 C  CG    . PRO A 1 285 ? 23.485  6.403   15.110  1.00 33.89  ? 285 PRO A CG    1 
ATOM   2219 C  CD    . PRO A 1 285 ? 22.016  6.287   15.480  1.00 37.03  ? 285 PRO A CD    1 
ATOM   2220 N  N     . SER A 1 286 ? 23.015  2.326   13.192  1.00 32.85  ? 286 SER A N     1 
ATOM   2221 C  CA    . SER A 1 286 ? 22.775  0.888   13.234  1.00 36.07  ? 286 SER A CA    1 
ATOM   2222 C  C     . SER A 1 286 ? 22.840  0.376   14.669  1.00 35.80  ? 286 SER A C     1 
ATOM   2223 O  O     . SER A 1 286 ? 23.687  0.802   15.464  1.00 37.80  ? 286 SER A O     1 
ATOM   2224 C  CB    . SER A 1 286 ? 23.787  0.147   12.364  1.00 35.21  ? 286 SER A CB    1 
ATOM   2225 O  OG    . SER A 1 286 ? 24.020  0.830   11.148  1.00 38.84  ? 286 SER A OG    1 
ATOM   2226 N  N     . ALA A 1 287 ? 21.898  -0.511  14.997  1.00 40.02  ? 287 ALA A N     1 
ATOM   2227 C  CA    . ALA A 1 287 ? 21.768  -1.126  16.324  1.00 40.21  ? 287 ALA A CA    1 
ATOM   2228 C  C     . ALA A 1 287 ? 21.509  -0.087  17.418  1.00 40.60  ? 287 ALA A C     1 
ATOM   2229 O  O     . ALA A 1 287 ? 21.964  -0.230  18.557  1.00 41.52  ? 287 ALA A O     1 
ATOM   2230 C  CB    . ALA A 1 287 ? 22.990  -1.988  16.660  1.00 40.48  ? 287 ALA A CB    1 
ATOM   2231 N  N     . CYS A 1 288 ? 20.727  0.953   17.096  1.00 39.29  ? 288 CYS A N     1 
ATOM   2232 C  CA    . CYS A 1 288 ? 20.421  1.987   18.082  1.00 37.12  ? 288 CYS A CA    1 
ATOM   2233 C  C     . CYS A 1 288 ? 18.924  2.180   18.336  1.00 41.52  ? 288 CYS A C     1 
ATOM   2234 O  O     . CYS A 1 288 ? 18.539  3.174   18.981  1.00 38.02  ? 288 CYS A O     1 
ATOM   2235 C  CB    . CYS A 1 288 ? 21.072  3.312   17.669  1.00 37.24  ? 288 CYS A CB    1 
ATOM   2236 S  SG    . CYS A 1 288 ? 22.859  3.341   18.028  1.00 39.37  ? 288 CYS A SG    1 
ATOM   2237 N  N     . GLY A 1 289 ? 18.069  1.271   17.851  1.00 33.74  ? 289 GLY A N     1 
ATOM   2238 C  CA    . GLY A 1 289 ? 16.710  1.206   18.361  1.00 34.79  ? 289 GLY A CA    1 
ATOM   2239 C  C     . GLY A 1 289 ? 15.597  1.384   17.348  1.00 35.80  ? 289 GLY A C     1 
ATOM   2240 O  O     . GLY A 1 289 ? 14.432  1.470   17.737  1.00 34.23  ? 289 GLY A O     1 
ATOM   2241 N  N     . LYS A 1 290 ? 15.910  1.430   16.053  1.00 32.60  ? 290 LYS A N     1 
ATOM   2242 C  CA    . LYS A 1 290 ? 14.866  1.767   15.085  1.00 34.56  ? 290 LYS A CA    1 
ATOM   2243 C  C     . LYS A 1 290 ? 13.781  0.691   15.062  1.00 35.38  ? 290 LYS A C     1 
ATOM   2244 O  O     . LYS A 1 290 ? 12.580  0.990   15.132  1.00 33.67  ? 290 LYS A O     1 
ATOM   2245 C  CB    . LYS A 1 290 ? 15.474  1.978   13.690  1.00 29.30  ? 290 LYS A CB    1 
ATOM   2246 C  CG    . LYS A 1 290 ? 16.272  3.308   13.503  1.00 30.56  ? 290 LYS A CG    1 
ATOM   2247 C  CD    . LYS A 1 290 ? 16.752  3.480   12.043  1.00 31.80  ? 290 LYS A CD    1 
ATOM   2248 C  CE    . LYS A 1 290 ? 17.584  2.243   11.555  1.00 30.22  ? 290 LYS A CE    1 
ATOM   2249 N  NZ    . LYS A 1 290 ? 18.804  2.029   12.429  1.00 29.89  ? 290 LYS A NZ    1 
ATOM   2250 N  N     . THR A 1 291 ? 14.192  -0.577  15.015  1.00 35.01  ? 291 THR A N     1 
ATOM   2251 C  CA    . THR A 1 291 ? 13.221  -1.664  14.948  1.00 34.76  ? 291 THR A CA    1 
ATOM   2252 C  C     . THR A 1 291 ? 12.372  -1.738  16.213  1.00 35.26  ? 291 THR A C     1 
ATOM   2253 O  O     . THR A 1 291 ? 11.169  -2.008  16.145  1.00 35.26  ? 291 THR A O     1 
ATOM   2254 C  CB    . THR A 1 291 ? 13.947  -2.977  14.685  1.00 33.09  ? 291 THR A CB    1 
ATOM   2255 O  OG1   . THR A 1 291 ? 14.562  -2.899  13.386  1.00 34.37  ? 291 THR A OG1   1 
ATOM   2256 C  CG2   . THR A 1 291 ? 12.956  -4.180  14.719  1.00 33.62  ? 291 THR A CG2   1 
ATOM   2257 N  N     . ASN A 1 292 ? 12.965  -1.481  17.375  1.00 35.46  ? 292 ASN A N     1 
ATOM   2258 C  CA    . ASN A 1 292 ? 12.178  -1.532  18.598  1.00 35.76  ? 292 ASN A CA    1 
ATOM   2259 C  C     . ASN A 1 292 ? 11.201  -0.368  18.718  1.00 38.06  ? 292 ASN A C     1 
ATOM   2260 O  O     . ASN A 1 292 ? 10.137  -0.519  19.332  1.00 39.44  ? 292 ASN A O     1 
ATOM   2261 C  CB    . ASN A 1 292 ? 13.106  -1.573  19.798  1.00 41.37  ? 292 ASN A CB    1 
ATOM   2262 C  CG    . ASN A 1 292 ? 13.622  -2.962  20.040  1.00 43.41  ? 292 ASN A CG    1 
ATOM   2263 O  OD1   . ASN A 1 292 ? 13.107  -3.671  20.887  1.00 47.47  ? 292 ASN A OD1   1 
ATOM   2264 N  ND2   . ASN A 1 292 ? 14.608  -3.381  19.248  1.00 41.60  ? 292 ASN A ND2   1 
ATOM   2265 N  N     . LEU A 1 293 ? 11.542  0.797   18.158  1.00 37.02  ? 293 LEU A N     1 
ATOM   2266 C  CA    . LEU A 1 293 ? 10.607  1.920   18.167  1.00 36.51  ? 293 LEU A CA    1 
ATOM   2267 C  C     . LEU A 1 293 ? 9.501   1.712   17.135  1.00 36.74  ? 293 LEU A C     1 
ATOM   2268 O  O     . LEU A 1 293 ? 8.323   1.905   17.434  1.00 34.73  ? 293 LEU A O     1 
ATOM   2269 C  CB    . LEU A 1 293 ? 11.361  3.231   17.896  1.00 34.43  ? 293 LEU A CB    1 
ATOM   2270 C  CG    . LEU A 1 293 ? 10.562  4.528   18.063  1.00 34.89  ? 293 LEU A CG    1 
ATOM   2271 C  CD1   . LEU A 1 293 ? 10.094  4.660   19.502  1.00 36.71  ? 293 LEU A CD1   1 
ATOM   2272 C  CD2   . LEU A 1 293 ? 11.412  5.725   17.679  1.00 34.84  ? 293 LEU A CD2   1 
ATOM   2273 N  N     . ALA A 1 294 ? 9.863   1.281   15.922  1.00 38.02  ? 294 ALA A N     1 
ATOM   2274 C  CA    . ALA A 1 294 ? 8.875   1.119   14.856  1.00 37.24  ? 294 ALA A CA    1 
ATOM   2275 C  C     . ALA A 1 294 ? 7.813   0.067   15.189  1.00 41.01  ? 294 ALA A C     1 
ATOM   2276 O  O     . ALA A 1 294 ? 6.705   0.114   14.637  1.00 40.54  ? 294 ALA A O     1 
ATOM   2277 C  CB    . ALA A 1 294 ? 9.585   0.733   13.552  1.00 36.56  ? 294 ALA A CB    1 
ATOM   2278 N  N     . MET A 1 295 ? 8.141   -0.916  16.034  1.00 38.99  ? 295 MET A N     1 
ATOM   2279 C  CA    . MET A 1 295 ? 7.208   -1.984  16.384  1.00 43.72  ? 295 MET A CA    1 
ATOM   2280 C  C     . MET A 1 295 ? 6.700   -1.877  17.806  1.00 42.15  ? 295 MET A C     1 
ATOM   2281 O  O     . MET A 1 295 ? 6.125   -2.846  18.312  1.00 43.41  ? 295 MET A O     1 
ATOM   2282 C  CB    . MET A 1 295 ? 7.850   -3.361  16.228  1.00 40.07  ? 295 MET A CB    1 
ATOM   2283 C  CG    . MET A 1 295 ? 8.290   -3.678  14.875  1.00 41.74  ? 295 MET A CG    1 
ATOM   2284 S  SD    . MET A 1 295 ? 8.828   -5.393  14.783  1.00 45.81  ? 295 MET A SD    1 
ATOM   2285 C  CE    . MET A 1 295 ? 9.397   -5.329  13.104  1.00 42.10  ? 295 MET A CE    1 
ATOM   2286 N  N     . MET A 1 296 ? 6.913   -0.738  18.458  1.00 40.23  ? 296 MET A N     1 
ATOM   2287 C  CA    . MET A 1 296 ? 6.720   -0.637  19.898  1.00 40.22  ? 296 MET A CA    1 
ATOM   2288 C  C     . MET A 1 296 ? 5.296   -0.999  20.302  1.00 46.36  ? 296 MET A C     1 
ATOM   2289 O  O     . MET A 1 296 ? 4.335   -0.754  19.567  1.00 48.49  ? 296 MET A O     1 
ATOM   2290 C  CB    . MET A 1 296 ? 7.056   0.789   20.361  1.00 42.39  ? 296 MET A CB    1 
ATOM   2291 C  CG    . MET A 1 296 ? 6.126   1.349   21.404  1.00 48.17  ? 296 MET A CG    1 
ATOM   2292 S  SD    . MET A 1 296 ? 6.610   2.982   21.982  1.00 51.60  ? 296 MET A SD    1 
ATOM   2293 C  CE    . MET A 1 296 ? 6.608   3.859   20.453  1.00 42.81  ? 296 MET A CE    1 
ATOM   2294 N  N     . ASN A 1 297 ? 5.176   -1.618  21.487  1.00 43.03  ? 297 ASN A N     1 
ATOM   2295 C  CA    . ASN A 1 297 ? 3.911   -1.758  22.192  1.00 45.21  ? 297 ASN A CA    1 
ATOM   2296 C  C     . ASN A 1 297 ? 3.807   -0.649  23.233  1.00 48.81  ? 297 ASN A C     1 
ATOM   2297 O  O     . ASN A 1 297 ? 4.503   -0.710  24.257  1.00 47.82  ? 297 ASN A O     1 
ATOM   2298 C  CB    . ASN A 1 297 ? 3.829   -3.133  22.864  1.00 49.87  ? 297 ASN A CB    1 
ATOM   2299 C  CG    . ASN A 1 297 ? 2.443   -3.462  23.366  1.00 56.17  ? 297 ASN A CG    1 
ATOM   2300 O  OD1   . ASN A 1 297 ? 1.483   -3.508  22.597  1.00 64.45  ? 297 ASN A OD1   1 
ATOM   2301 N  ND2   . ASN A 1 297 ? 2.335   -3.741  24.658  1.00 56.95  ? 297 ASN A ND2   1 
ATOM   2302 N  N     . PRO A 1 298 ? 2.988   0.382   23.023  1.00 49.39  ? 298 PRO A N     1 
ATOM   2303 C  CA    . PRO A 1 298 ? 2.965   1.505   23.970  1.00 48.08  ? 298 PRO A CA    1 
ATOM   2304 C  C     . PRO A 1 298 ? 2.419   1.102   25.330  1.00 48.42  ? 298 PRO A C     1 
ATOM   2305 O  O     . PRO A 1 298 ? 1.468   0.330   25.431  1.00 49.64  ? 298 PRO A O     1 
ATOM   2306 C  CB    . PRO A 1 298 ? 2.041   2.528   23.292  1.00 51.91  ? 298 PRO A CB    1 
ATOM   2307 C  CG    . PRO A 1 298 ? 1.941   2.090   21.859  1.00 53.13  ? 298 PRO A CG    1 
ATOM   2308 C  CD    . PRO A 1 298 ? 2.095   0.599   21.876  1.00 49.03  ? 298 PRO A CD    1 
ATOM   2309 N  N     . THR A 1 299 ? 3.001   1.676   26.388  1.00 48.72  ? 299 THR A N     1 
ATOM   2310 C  CA    . THR A 1 299 ? 2.469   1.447   27.727  1.00 50.64  ? 299 THR A CA    1 
ATOM   2311 C  C     . THR A 1 299 ? 1.300   2.373   28.065  1.00 52.14  ? 299 THR A C     1 
ATOM   2312 O  O     . THR A 1 299 ? 0.498   2.026   28.930  1.00 56.39  ? 299 THR A O     1 
ATOM   2313 C  CB    . THR A 1 299 ? 3.583   1.600   28.770  1.00 53.12  ? 299 THR A CB    1 
ATOM   2314 O  OG1   . THR A 1 299 ? 4.145   2.921   28.687  1.00 52.00  ? 299 THR A OG1   1 
ATOM   2315 C  CG2   . THR A 1 299 ? 4.690   0.563   28.517  1.00 52.38  ? 299 THR A CG2   1 
ATOM   2316 N  N     . LEU A 1 300 ? 1.171   3.519   27.382  1.00 51.17  ? 300 LEU A N     1 
ATOM   2317 C  CA    . LEU A 1 300 ? 0.077   4.457   27.648  1.00 54.71  ? 300 LEU A CA    1 
ATOM   2318 C  C     . LEU A 1 300 ? -1.232  3.931   27.069  1.00 53.26  ? 300 LEU A C     1 
ATOM   2319 O  O     . LEU A 1 300 ? -1.287  3.610   25.878  1.00 51.69  ? 300 LEU A O     1 
ATOM   2320 C  CB    . LEU A 1 300 ? 0.387   5.826   27.024  1.00 54.07  ? 300 LEU A CB    1 
ATOM   2321 C  CG    . LEU A 1 300 ? 1.522   6.686   27.580  1.00 57.53  ? 300 LEU A CG    1 
ATOM   2322 C  CD1   . LEU A 1 300 ? 1.577   8.030   26.858  1.00 54.84  ? 300 LEU A CD1   1 
ATOM   2323 C  CD2   . LEU A 1 300 ? 1.346   6.892   29.070  1.00 56.02  ? 300 LEU A CD2   1 
ATOM   2324 N  N     . PRO A 1 301 ? -2.314  3.876   27.845  1.00 55.66  ? 301 PRO A N     1 
ATOM   2325 C  CA    . PRO A 1 301 ? -3.575  3.363   27.292  1.00 56.48  ? 301 PRO A CA    1 
ATOM   2326 C  C     . PRO A 1 301 ? -4.187  4.348   26.305  1.00 56.56  ? 301 PRO A C     1 
ATOM   2327 O  O     . PRO A 1 301 ? -4.091  5.567   26.467  1.00 55.87  ? 301 PRO A O     1 
ATOM   2328 C  CB    . PRO A 1 301 ? -4.469  3.182   28.529  1.00 59.49  ? 301 PRO A CB    1 
ATOM   2329 C  CG    . PRO A 1 301 ? -3.748  3.896   29.682  1.00 63.47  ? 301 PRO A CG    1 
ATOM   2330 C  CD    . PRO A 1 301 ? -2.514  4.559   29.132  1.00 57.78  ? 301 PRO A CD    1 
ATOM   2331 N  N     . GLY A 1 302 ? -4.823  3.804   25.267  1.00 55.35  ? 302 GLY A N     1 
ATOM   2332 C  CA    . GLY A 1 302 ? -5.432  4.612   24.229  1.00 54.82  ? 302 GLY A CA    1 
ATOM   2333 C  C     . GLY A 1 302 ? -4.509  4.996   23.087  1.00 56.97  ? 302 GLY A C     1 
ATOM   2334 O  O     . GLY A 1 302 ? -4.946  5.695   22.162  1.00 57.31  ? 302 GLY A O     1 
ATOM   2335 N  N     . TRP A 1 303 ? -3.249  4.578   23.122  1.00 51.29  ? 303 TRP A N     1 
ATOM   2336 C  CA    . TRP A 1 303 ? -2.275  4.905   22.091  1.00 48.11  ? 303 TRP A CA    1 
ATOM   2337 C  C     . TRP A 1 303 ? -1.981  3.658   21.274  1.00 48.94  ? 303 TRP A C     1 
ATOM   2338 O  O     . TRP A 1 303 ? -1.997  2.545   21.806  1.00 47.59  ? 303 TRP A O     1 
ATOM   2339 C  CB    . TRP A 1 303 ? -0.995  5.451   22.713  1.00 47.31  ? 303 TRP A CB    1 
ATOM   2340 C  CG    . TRP A 1 303 ? -1.163  6.858   23.227  1.00 50.01  ? 303 TRP A CG    1 
ATOM   2341 C  CD1   . TRP A 1 303 ? -1.645  7.240   24.447  1.00 51.19  ? 303 TRP A CD1   1 
ATOM   2342 C  CD2   . TRP A 1 303 ? -0.870  8.060   22.516  1.00 49.09  ? 303 TRP A CD2   1 
ATOM   2343 N  NE1   . TRP A 1 303 ? -1.661  8.613   24.541  1.00 52.05  ? 303 TRP A NE1   1 
ATOM   2344 C  CE2   . TRP A 1 303 ? -1.182  9.138   23.368  1.00 49.28  ? 303 TRP A CE2   1 
ATOM   2345 C  CE3   . TRP A 1 303 ? -0.361  8.329   21.242  1.00 49.35  ? 303 TRP A CE3   1 
ATOM   2346 C  CZ2   . TRP A 1 303 ? -1.013  10.464  22.983  1.00 50.49  ? 303 TRP A CZ2   1 
ATOM   2347 C  CZ3   . TRP A 1 303 ? -0.186  9.653   20.864  1.00 47.86  ? 303 TRP A CZ3   1 
ATOM   2348 C  CH2   . TRP A 1 303 ? -0.511  10.700  21.732  1.00 47.81  ? 303 TRP A CH2   1 
ATOM   2349 N  N     . LYS A 1 304 ? -1.747  3.838   19.977  1.00 45.25  ? 304 LYS A N     1 
ATOM   2350 C  CA    . LYS A 1 304 ? -1.427  2.712   19.113  1.00 44.84  ? 304 LYS A CA    1 
ATOM   2351 C  C     . LYS A 1 304 ? -0.325  3.106   18.141  1.00 48.45  ? 304 LYS A C     1 
ATOM   2352 O  O     . LYS A 1 304 ? -0.350  4.206   17.576  1.00 46.65  ? 304 LYS A O     1 
ATOM   2353 C  CB    . LYS A 1 304 ? -2.668  2.224   18.349  1.00 48.67  ? 304 LYS A CB    1 
ATOM   2354 C  CG    . LYS A 1 304 ? -2.378  1.080   17.395  1.00 51.41  ? 304 LYS A CG    1 
ATOM   2355 C  CD    . LYS A 1 304 ? -3.635  0.576   16.703  1.00 59.96  ? 304 LYS A CD    1 
ATOM   2356 C  CE    . LYS A 1 304 ? -3.305  -0.595  15.789  1.00 60.97  ? 304 LYS A CE    1 
ATOM   2357 N  NZ    . LYS A 1 304 ? -4.522  -1.346  15.382  1.00 68.18  ? 304 LYS A NZ    1 
ATOM   2358 N  N     . VAL A 1 305 ? 0.645   2.205   17.964  1.00 41.13  ? 305 VAL A N     1 
ATOM   2359 C  CA    . VAL A 1 305 ? 1.736   2.373   17.015  1.00 43.11  ? 305 VAL A CA    1 
ATOM   2360 C  C     . VAL A 1 305 ? 1.587   1.318   15.925  1.00 43.84  ? 305 VAL A C     1 
ATOM   2361 O  O     . VAL A 1 305 ? 1.335   0.141   16.216  1.00 45.00  ? 305 VAL A O     1 
ATOM   2362 C  CB    . VAL A 1 305 ? 3.114   2.272   17.694  1.00 42.55  ? 305 VAL A CB    1 
ATOM   2363 C  CG1   . VAL A 1 305 ? 4.230   2.252   16.624  1.00 42.18  ? 305 VAL A CG1   1 
ATOM   2364 C  CG2   . VAL A 1 305 ? 3.325   3.453   18.634  1.00 48.04  ? 305 VAL A CG2   1 
ATOM   2365 N  N     . GLU A 1 306 ? 1.705   1.742   14.675  1.00 38.38  ? 306 GLU A N     1 
ATOM   2366 C  CA    . GLU A 1 306 ? 1.762   0.810   13.557  1.00 43.29  ? 306 GLU A CA    1 
ATOM   2367 C  C     . GLU A 1 306 ? 3.046   1.040   12.777  1.00 42.03  ? 306 GLU A C     1 
ATOM   2368 O  O     . GLU A 1 306 ? 3.587   2.149   12.755  1.00 39.89  ? 306 GLU A O     1 
ATOM   2369 C  CB    . GLU A 1 306 ? 0.529   0.950   12.661  1.00 43.09  ? 306 GLU A CB    1 
ATOM   2370 C  CG    . GLU A 1 306 ? -0.761  0.765   13.460  1.00 48.74  ? 306 GLU A CG    1 
ATOM   2371 C  CD    . GLU A 1 306 ? -1.994  1.214   12.712  1.00 49.61  ? 306 GLU A CD    1 
ATOM   2372 O  OE1   . GLU A 1 306 ? -2.342  2.410   12.801  1.00 48.54  ? 306 GLU A OE1   1 
ATOM   2373 O  OE2   . GLU A 1 306 ? -2.619  0.368   12.041  1.00 52.99  ? 306 GLU A OE2   1 
ATOM   2374 N  N     . CYS A 1 307 ? 3.539   -0.029  12.146  1.00 42.57  ? 307 CYS A N     1 
ATOM   2375 C  CA    . CYS A 1 307 ? 4.861   -0.051  11.533  1.00 37.45  ? 307 CYS A CA    1 
ATOM   2376 C  C     . CYS A 1 307 ? 4.730   0.051   10.015  1.00 40.06  ? 307 CYS A C     1 
ATOM   2377 O  O     . CYS A 1 307 ? 4.074   -0.785  9.388   1.00 41.24  ? 307 CYS A O     1 
ATOM   2378 C  CB    . CYS A 1 307 ? 5.599   -1.340  11.913  1.00 38.59  ? 307 CYS A CB    1 
ATOM   2379 S  SG    . CYS A 1 307 ? 7.264   -1.491  11.211  1.00 40.82  ? 307 CYS A SG    1 
ATOM   2380 N  N     . VAL A 1 308 ? 5.351   1.068   9.427   1.00 39.98  ? 308 VAL A N     1 
ATOM   2381 C  CA    . VAL A 1 308 ? 5.442   1.141   7.970   1.00 38.30  ? 308 VAL A CA    1 
ATOM   2382 C  C     . VAL A 1 308 ? 6.745   0.524   7.479   1.00 36.84  ? 308 VAL A C     1 
ATOM   2383 O  O     . VAL A 1 308 ? 6.754   -0.206  6.487   1.00 39.95  ? 308 VAL A O     1 
ATOM   2384 C  CB    . VAL A 1 308 ? 5.297   2.600   7.491   1.00 36.02  ? 308 VAL A CB    1 
ATOM   2385 C  CG1   . VAL A 1 308 ? 5.497   2.687   5.964   1.00 35.89  ? 308 VAL A CG1   1 
ATOM   2386 C  CG2   . VAL A 1 308 ? 3.949   3.171   7.878   1.00 38.56  ? 308 VAL A CG2   1 
ATOM   2387 N  N     . GLY A 1 309 ? 7.838   0.801   8.188   1.00 35.27  ? 309 GLY A N     1 
ATOM   2388 C  CA    . GLY A 1 309 ? 9.158   0.287   7.860   1.00 31.66  ? 309 GLY A CA    1 
ATOM   2389 C  C     . GLY A 1 309 ? 10.081  0.522   9.037   1.00 35.42  ? 309 GLY A C     1 
ATOM   2390 O  O     . GLY A 1 309 ? 9.803   1.345   9.914   1.00 33.99  ? 309 GLY A O     1 
ATOM   2391 N  N     . ASP A 1 310 ? 11.181  -0.219  9.065   1.00 35.64  ? 310 ASP A N     1 
ATOM   2392 C  CA    . ASP A 1 310 ? 12.063  -0.143  10.224  1.00 33.42  ? 310 ASP A CA    1 
ATOM   2393 C  C     . ASP A 1 310 ? 13.490  0.279   9.906   1.00 34.18  ? 310 ASP A C     1 
ATOM   2394 O  O     . ASP A 1 310 ? 14.295  0.407   10.840  1.00 34.08  ? 310 ASP A O     1 
ATOM   2395 C  CB    . ASP A 1 310 ? 12.080  -1.488  10.971  1.00 34.92  ? 310 ASP A CB    1 
ATOM   2396 C  CG    . ASP A 1 310 ? 12.931  -2.551  10.275  1.00 39.52  ? 310 ASP A CG    1 
ATOM   2397 O  OD1   . ASP A 1 310 ? 13.076  -2.502  9.031   1.00 34.25  ? 310 ASP A OD1   1 
ATOM   2398 O  OD2   . ASP A 1 310 ? 13.449  -3.435  10.994  1.00 34.43  ? 310 ASP A OD2   1 
ATOM   2399 N  N     . ASP A 1 311 ? 13.835  0.520   8.637   1.00 30.26  ? 311 ASP A N     1 
ATOM   2400 C  CA    . ASP A 1 311 ? 15.254  0.728   8.346   1.00 31.73  ? 311 ASP A CA    1 
ATOM   2401 C  C     . ASP A 1 311 ? 15.539  1.709   7.209   1.00 29.24  ? 311 ASP A C     1 
ATOM   2402 O  O     . ASP A 1 311 ? 16.547  2.412   7.260   1.00 30.36  ? 311 ASP A O     1 
ATOM   2403 C  CB    . ASP A 1 311 ? 15.924  -0.629  8.048   1.00 30.09  ? 311 ASP A CB    1 
ATOM   2404 C  CG    . ASP A 1 311 ? 17.457  -0.542  7.992   1.00 30.67  ? 311 ASP A CG    1 
ATOM   2405 O  OD1   . ASP A 1 311 ? 18.115  -0.218  9.012   1.00 26.70  ? 311 ASP A OD1   1 
ATOM   2406 O  OD2   . ASP A 1 311 ? 18.012  -0.820  6.919   1.00 33.35  ? 311 ASP A OD2   1 
ATOM   2407 N  N     . ILE A 1 312 ? 14.700  1.768   6.174   1.00 30.02  ? 312 ILE A N     1 
ATOM   2408 C  CA    . ILE A 1 312 ? 14.982  2.605   5.008   1.00 30.08  ? 312 ILE A CA    1 
ATOM   2409 C  C     . ILE A 1 312 ? 13.710  3.335   4.600   1.00 30.36  ? 312 ILE A C     1 
ATOM   2410 O  O     . ILE A 1 312 ? 12.646  2.718   4.477   1.00 29.33  ? 312 ILE A O     1 
ATOM   2411 C  CB    . ILE A 1 312 ? 15.527  1.789   3.812   1.00 32.95  ? 312 ILE A CB    1 
ATOM   2412 C  CG1   . ILE A 1 312 ? 16.826  1.061   4.187   1.00 35.48  ? 312 ILE A CG1   1 
ATOM   2413 C  CG2   . ILE A 1 312 ? 15.808  2.695   2.610   1.00 32.10  ? 312 ILE A CG2   1 
ATOM   2414 C  CD1   . ILE A 1 312 ? 17.343  0.146   3.079   1.00 38.02  ? 312 ILE A CD1   1 
ATOM   2415 N  N     . ALA A 1 313 ? 13.827  4.644   4.367   1.00 34.20  ? 313 ALA A N     1 
ATOM   2416 C  CA    . ALA A 1 313 ? 12.723  5.476   3.920   1.00 32.65  ? 313 ALA A CA    1 
ATOM   2417 C  C     . ALA A 1 313 ? 13.114  6.217   2.648   1.00 34.40  ? 313 ALA A C     1 
ATOM   2418 O  O     . ALA A 1 313 ? 14.201  6.797   2.563   1.00 37.08  ? 313 ALA A O     1 
ATOM   2419 C  CB    . ALA A 1 313 ? 12.327  6.493   5.006   1.00 31.17  ? 313 ALA A CB    1 
ATOM   2420 N  N     . TRP A 1 314 ? 12.213  6.226   1.677   1.00 33.78  ? 314 TRP A N     1 
ATOM   2421 C  CA    . TRP A 1 314 ? 12.334  7.060   0.487   1.00 37.14  ? 314 TRP A CA    1 
ATOM   2422 C  C     . TRP A 1 314 ? 11.242  8.121   0.546   1.00 38.53  ? 314 TRP A C     1 
ATOM   2423 O  O     . TRP A 1 314 ? 10.064  7.783   0.697   1.00 38.14  ? 314 TRP A O     1 
ATOM   2424 C  CB    . TRP A 1 314 ? 12.205  6.218   -0.789  1.00 37.39  ? 314 TRP A CB    1 
ATOM   2425 C  CG    . TRP A 1 314 ? 13.371  5.278   -1.094  1.00 35.23  ? 314 TRP A CG    1 
ATOM   2426 C  CD1   . TRP A 1 314 ? 14.523  5.116   -0.379  1.00 36.36  ? 314 TRP A CD1   1 
ATOM   2427 C  CD2   . TRP A 1 314 ? 13.477  4.392   -2.224  1.00 36.88  ? 314 TRP A CD2   1 
ATOM   2428 N  NE1   . TRP A 1 314 ? 15.343  4.174   -0.996  1.00 35.53  ? 314 TRP A NE1   1 
ATOM   2429 C  CE2   . TRP A 1 314 ? 14.714  3.722   -2.124  1.00 33.31  ? 314 TRP A CE2   1 
ATOM   2430 C  CE3   . TRP A 1 314 ? 12.635  4.093   -3.301  1.00 37.75  ? 314 TRP A CE3   1 
ATOM   2431 C  CZ2   . TRP A 1 314 ? 15.133  2.783   -3.066  1.00 37.26  ? 314 TRP A CZ2   1 
ATOM   2432 C  CZ3   . TRP A 1 314 ? 13.058  3.148   -4.235  1.00 39.04  ? 314 TRP A CZ3   1 
ATOM   2433 C  CH2   . TRP A 1 314 ? 14.293  2.521   -4.115  1.00 36.27  ? 314 TRP A CH2   1 
ATOM   2434 N  N     . MET A 1 315 ? 11.624  9.396   0.422   1.00 36.28  ? 315 MET A N     1 
ATOM   2435 C  CA    . MET A 1 315 ? 10.726  10.499  0.740   1.00 41.30  ? 315 MET A CA    1 
ATOM   2436 C  C     . MET A 1 315 ? 10.768  11.572  -0.340  1.00 40.99  ? 315 MET A C     1 
ATOM   2437 O  O     . MET A 1 315 ? 11.820  11.861  -0.918  1.00 39.67  ? 315 MET A O     1 
ATOM   2438 C  CB    . MET A 1 315 ? 11.079  11.142  2.096   1.00 39.88  ? 315 MET A CB    1 
ATOM   2439 C  CG    . MET A 1 315 ? 11.268  10.132  3.221   1.00 42.37  ? 315 MET A CG    1 
ATOM   2440 S  SD    . MET A 1 315 ? 11.168  10.880  4.864   1.00 42.94  ? 315 MET A SD    1 
ATOM   2441 C  CE    . MET A 1 315 ? 12.700  11.761  4.980   1.00 39.32  ? 315 MET A CE    1 
ATOM   2442 N  N     . LYS A 1 316 ? 9.622   12.204  -0.567  1.00 41.58  ? 316 LYS A N     1 
ATOM   2443 C  CA    . LYS A 1 316 ? 9.547   13.264  -1.562  1.00 48.23  ? 316 LYS A CA    1 
ATOM   2444 C  C     . LYS A 1 316 ? 8.369   14.173  -1.236  1.00 48.36  ? 316 LYS A C     1 
ATOM   2445 O  O     . LYS A 1 316 ? 7.324   13.697  -0.787  1.00 46.74  ? 316 LYS A O     1 
ATOM   2446 C  CB    . LYS A 1 316 ? 9.423   12.644  -2.961  1.00 50.85  ? 316 LYS A CB    1 
ATOM   2447 C  CG    . LYS A 1 316 ? 8.639   13.425  -3.977  1.00 55.76  ? 316 LYS A CG    1 
ATOM   2448 C  CD    . LYS A 1 316 ? 8.584   12.666  -5.297  1.00 57.54  ? 316 LYS A CD    1 
ATOM   2449 C  CE    . LYS A 1 316 ? 9.988   12.389  -5.839  1.00 63.26  ? 316 LYS A CE    1 
ATOM   2450 N  NZ    . LYS A 1 316 ? 10.693  13.632  -6.289  1.00 64.39  ? 316 LYS A NZ    1 
ATOM   2451 N  N     . PHE A 1 317 ? 8.549   15.478  -1.436  1.00 47.08  ? 317 PHE A N     1 
ATOM   2452 C  CA    . PHE A 1 317 ? 7.420   16.393  -1.343  1.00 52.64  ? 317 PHE A CA    1 
ATOM   2453 C  C     . PHE A 1 317 ? 6.462   16.159  -2.506  1.00 56.31  ? 317 PHE A C     1 
ATOM   2454 O  O     . PHE A 1 317 ? 6.883   15.934  -3.645  1.00 55.40  ? 317 PHE A O     1 
ATOM   2455 C  CB    . PHE A 1 317 ? 7.899   17.847  -1.321  1.00 54.08  ? 317 PHE A CB    1 
ATOM   2456 C  CG    . PHE A 1 317 ? 8.553   18.241  -0.027  1.00 52.42  ? 317 PHE A CG    1 
ATOM   2457 C  CD1   . PHE A 1 317 ? 7.785   18.583  1.074   1.00 51.87  ? 317 PHE A CD1   1 
ATOM   2458 C  CD2   . PHE A 1 317 ? 9.933   18.239  0.101   1.00 56.25  ? 317 PHE A CD2   1 
ATOM   2459 C  CE1   . PHE A 1 317 ? 8.381   18.933  2.274   1.00 51.68  ? 317 PHE A CE1   1 
ATOM   2460 C  CE2   . PHE A 1 317 ? 10.535  18.584  1.300   1.00 50.10  ? 317 PHE A CE2   1 
ATOM   2461 C  CZ    . PHE A 1 317 ? 9.758   18.933  2.385   1.00 52.26  ? 317 PHE A CZ    1 
ATOM   2462 N  N     . ASP A 1 318 ? 5.167   16.186  -2.213  1.00 55.49  ? 318 ASP A N     1 
ATOM   2463 C  CA    . ASP A 1 318 ? 4.160   15.983  -3.239  1.00 55.85  ? 318 ASP A CA    1 
ATOM   2464 C  C     . ASP A 1 318 ? 3.652   17.337  -3.728  1.00 58.60  ? 318 ASP A C     1 
ATOM   2465 O  O     . ASP A 1 318 ? 4.128   18.397  -3.313  1.00 52.97  ? 318 ASP A O     1 
ATOM   2466 C  CB    . ASP A 1 318 ? 3.025   15.088  -2.723  1.00 59.13  ? 318 ASP A CB    1 
ATOM   2467 C  CG    . ASP A 1 318 ? 2.196   15.733  -1.609  1.00 54.02  ? 318 ASP A CG    1 
ATOM   2468 O  OD1   . ASP A 1 318 ? 2.426   16.901  -1.234  1.00 56.86  ? 318 ASP A OD1   1 
ATOM   2469 O  OD2   . ASP A 1 318 ? 1.294   15.044  -1.094  1.00 58.13  ? 318 ASP A OD2   1 
ATOM   2470 N  N     . ALA A 1 319 ? 2.652   17.293  -4.613  1.00 62.26  ? 319 ALA A N     1 
ATOM   2471 C  CA    . ALA A 1 319 ? 2.130   18.520  -5.203  1.00 61.79  ? 319 ALA A CA    1 
ATOM   2472 C  C     . ALA A 1 319 ? 1.534   19.450  -4.154  1.00 62.51  ? 319 ALA A C     1 
ATOM   2473 O  O     . ALA A 1 319 ? 1.516   20.670  -4.350  1.00 63.54  ? 319 ALA A O     1 
ATOM   2474 C  CB    . ALA A 1 319 ? 1.087   18.184  -6.271  1.00 63.56  ? 319 ALA A CB    1 
ATOM   2475 N  N     . GLN A 1 320 ? 1.053   18.909  -3.036  1.00 58.95  ? 320 GLN A N     1 
ATOM   2476 C  CA    . GLN A 1 320 ? 0.407   19.724  -2.015  1.00 58.59  ? 320 GLN A CA    1 
ATOM   2477 C  C     . GLN A 1 320 ? 1.373   20.210  -0.942  1.00 56.06  ? 320 GLN A C     1 
ATOM   2478 O  O     . GLN A 1 320 ? 0.950   20.905  -0.016  1.00 57.80  ? 320 GLN A O     1 
ATOM   2479 C  CB    . GLN A 1 320 ? -0.739  18.942  -1.354  1.00 59.10  ? 320 GLN A CB    1 
ATOM   2480 C  CG    . GLN A 1 320 ? -1.627  18.176  -2.332  1.00 61.67  ? 320 GLN A CG    1 
ATOM   2481 C  CD    . GLN A 1 320 ? -2.585  19.068  -3.105  1.00 64.30  ? 320 GLN A CD    1 
ATOM   2482 O  OE1   . GLN A 1 320 ? -3.016  20.112  -2.616  1.00 67.10  ? 320 GLN A OE1   1 
ATOM   2483 N  NE2   . GLN A 1 320 ? -2.933  18.649  -4.318  1.00 67.35  ? 320 GLN A NE2   1 
ATOM   2484 N  N     . GLY A 1 321 ? 2.651   19.857  -1.033  1.00 59.27  ? 321 GLY A N     1 
ATOM   2485 C  CA    . GLY A 1 321 ? 3.627   20.284  -0.055  1.00 55.81  ? 321 GLY A CA    1 
ATOM   2486 C  C     . GLY A 1 321 ? 3.876   19.316  1.082   1.00 54.08  ? 321 GLY A C     1 
ATOM   2487 O  O     . GLY A 1 321 ? 4.650   19.650  1.989   1.00 52.11  ? 321 GLY A O     1 
ATOM   2488 N  N     . ASN A 1 322 ? 3.248   18.137  1.069   1.00 52.01  ? 322 ASN A N     1 
ATOM   2489 C  CA    . ASN A 1 322 ? 3.455   17.148  2.120   1.00 50.14  ? 322 ASN A CA    1 
ATOM   2490 C  C     . ASN A 1 322 ? 4.686   16.309  1.816   1.00 50.72  ? 322 ASN A C     1 
ATOM   2491 O  O     . ASN A 1 322 ? 4.897   15.887  0.677   1.00 49.33  ? 322 ASN A O     1 
ATOM   2492 C  CB    . ASN A 1 322 ? 2.237   16.231  2.261   1.00 53.02  ? 322 ASN A CB    1 
ATOM   2493 C  CG    . ASN A 1 322 ? 0.970   16.991  2.614   1.00 55.50  ? 322 ASN A CG    1 
ATOM   2494 O  OD1   . ASN A 1 322 ? 0.813   17.470  3.735   1.00 60.27  ? 322 ASN A OD1   1 
ATOM   2495 N  ND2   . ASN A 1 322 ? 0.062   17.109  1.653   1.00 58.97  ? 322 ASN A ND2   1 
ATOM   2496 N  N     . LEU A 1 323 ? 5.505   16.077  2.840   1.00 44.94  ? 323 LEU A N     1 
ATOM   2497 C  CA    . LEU A 1 323 ? 6.635   15.162  2.728   1.00 46.11  ? 323 LEU A CA    1 
ATOM   2498 C  C     . LEU A 1 323 ? 6.096   13.745  2.847   1.00 42.10  ? 323 LEU A C     1 
ATOM   2499 O  O     . LEU A 1 323 ? 5.578   13.360  3.901   1.00 44.87  ? 323 LEU A O     1 
ATOM   2500 C  CB    . LEU A 1 323 ? 7.670   15.458  3.809   1.00 43.44  ? 323 LEU A CB    1 
ATOM   2501 C  CG    . LEU A 1 323 ? 8.911   14.569  3.806   1.00 40.87  ? 323 LEU A CG    1 
ATOM   2502 C  CD1   . LEU A 1 323 ? 9.632   14.645  2.460   1.00 43.81  ? 323 LEU A CD1   1 
ATOM   2503 C  CD2   . LEU A 1 323 ? 9.836   14.967  4.947   1.00 40.67  ? 323 LEU A CD2   1 
ATOM   2504 N  N     . ARG A 1 324 ? 6.181   12.974  1.767   1.00 40.40  ? 324 ARG A N     1 
ATOM   2505 C  CA    . ARG A 1 324 ? 5.602   11.641  1.724   1.00 43.52  ? 324 ARG A CA    1 
ATOM   2506 C  C     . ARG A 1 324 ? 6.698   10.586  1.686   1.00 43.33  ? 324 ARG A C     1 
ATOM   2507 O  O     . ARG A 1 324 ? 7.701   10.745  0.984   1.00 41.21  ? 324 ARG A O     1 
ATOM   2508 C  CB    . ARG A 1 324 ? 4.669   11.486  0.520   1.00 47.06  ? 324 ARG A CB    1 
ATOM   2509 C  CG    . ARG A 1 324 ? 3.549   12.519  0.522   1.00 52.21  ? 324 ARG A CG    1 
ATOM   2510 C  CD    . ARG A 1 324 ? 2.393   12.109  -0.369  1.00 57.50  ? 324 ARG A CD    1 
ATOM   2511 N  NE    . ARG A 1 324 ? 1.571   11.076  0.247   1.00 54.75  ? 324 ARG A NE    1 
ATOM   2512 C  CZ    . ARG A 1 324 ? 0.516   11.318  1.013   1.00 52.23  ? 324 ARG A CZ    1 
ATOM   2513 N  NH1   . ARG A 1 324 ? 0.121   12.550  1.280   1.00 50.60  ? 324 ARG A NH1   1 
ATOM   2514 N  NH2   . ARG A 1 324 ? -0.152  10.296  1.534   1.00 51.06  ? 324 ARG A NH2   1 
ATOM   2515 N  N     . ALA A 1 325 ? 6.498   9.504   2.440   1.00 38.13  ? 325 ALA A N     1 
ATOM   2516 C  CA    . ALA A 1 325 ? 7.505   8.463   2.608   1.00 38.62  ? 325 ALA A CA    1 
ATOM   2517 C  C     . ALA A 1 325 ? 6.936   7.106   2.237   1.00 37.86  ? 325 ALA A C     1 
ATOM   2518 O  O     . ALA A 1 325 ? 5.769   6.821   2.520   1.00 39.59  ? 325 ALA A O     1 
ATOM   2519 C  CB    . ALA A 1 325 ? 8.010   8.404   4.054   1.00 37.40  ? 325 ALA A CB    1 
ATOM   2520 N  N     . ILE A 1 326 ? 7.772   6.266   1.618   1.00 35.08  ? 326 ILE A N     1 
ATOM   2521 C  CA    . ILE A 1 326 ? 7.478   4.846   1.465   1.00 37.86  ? 326 ILE A CA    1 
ATOM   2522 C  C     . ILE A 1 326 ? 8.629   4.045   2.053   1.00 34.67  ? 326 ILE A C     1 
ATOM   2523 O  O     . ILE A 1 326 ? 9.768   4.509   2.154   1.00 36.79  ? 326 ILE A O     1 
ATOM   2524 C  CB    . ILE A 1 326 ? 7.236   4.413   0.001   1.00 39.67  ? 326 ILE A CB    1 
ATOM   2525 C  CG1   . ILE A 1 326 ? 8.472   4.686   -0.861  1.00 40.58  ? 326 ILE A CG1   1 
ATOM   2526 C  CG2   . ILE A 1 326 ? 5.982   5.061   -0.577  1.00 44.13  ? 326 ILE A CG2   1 
ATOM   2527 C  CD1   . ILE A 1 326 ? 9.109   3.411   -1.396  1.00 41.11  ? 326 ILE A CD1   1 
ATOM   2528 N  N     . ASN A 1 327 ? 8.310   2.821   2.444   1.00 38.45  ? 327 ASN A N     1 
ATOM   2529 C  CA    . ASN A 1 327 ? 9.308   1.837   2.822   1.00 33.99  ? 327 ASN A CA    1 
ATOM   2530 C  C     . ASN A 1 327 ? 9.593   0.976   1.602   1.00 34.90  ? 327 ASN A C     1 
ATOM   2531 O  O     . ASN A 1 327 ? 8.688   0.268   1.140   1.00 36.74  ? 327 ASN A O     1 
ATOM   2532 C  CB    . ASN A 1 327 ? 8.788   0.982   3.973   1.00 35.57  ? 327 ASN A CB    1 
ATOM   2533 C  CG    . ASN A 1 327 ? 9.645   -0.250  4.234   1.00 34.09  ? 327 ASN A CG    1 
ATOM   2534 O  OD1   . ASN A 1 327 ? 10.824  -0.301  3.877   1.00 32.91  ? 327 ASN A OD1   1 
ATOM   2535 N  ND2   . ASN A 1 327 ? 9.046   -1.250  4.877   1.00 37.76  ? 327 ASN A ND2   1 
ATOM   2536 N  N     . PRO A 1 328 ? 10.802  1.013   1.029   1.00 35.86  ? 328 PRO A N     1 
ATOM   2537 C  CA    . PRO A 1 328 ? 11.060  0.232   -0.190  1.00 34.29  ? 328 PRO A CA    1 
ATOM   2538 C  C     . PRO A 1 328 ? 11.291  -1.256  0.041   1.00 34.26  ? 328 PRO A C     1 
ATOM   2539 O  O     . PRO A 1 328 ? 11.332  -1.997  -0.946  1.00 35.09  ? 328 PRO A O     1 
ATOM   2540 C  CB    . PRO A 1 328 ? 12.326  0.893   -0.757  1.00 35.31  ? 328 PRO A CB    1 
ATOM   2541 C  CG    . PRO A 1 328 ? 13.055  1.358   0.456   1.00 32.80  ? 328 PRO A CG    1 
ATOM   2542 C  CD    . PRO A 1 328 ? 11.976  1.827   1.412   1.00 32.30  ? 328 PRO A CD    1 
ATOM   2543 N  N     . GLU A 1 329 ? 11.435  -1.712  1.290   1.00 35.00  ? 329 GLU A N     1 
ATOM   2544 C  CA    . GLU A 1 329 ? 11.703  -3.104  1.640   1.00 33.27  ? 329 GLU A CA    1 
ATOM   2545 C  C     . GLU A 1 329 ? 10.408  -3.909  1.767   1.00 34.08  ? 329 GLU A C     1 
ATOM   2546 O  O     . GLU A 1 329 ? 9.310   -3.355  1.853   1.00 38.16  ? 329 GLU A O     1 
ATOM   2547 C  CB    . GLU A 1 329 ? 12.493  -3.192  2.952   1.00 33.57  ? 329 GLU A CB    1 
ATOM   2548 C  CG    . GLU A 1 329 ? 13.798  -2.378  2.980   1.00 33.32  ? 329 GLU A CG    1 
ATOM   2549 C  CD    . GLU A 1 329 ? 14.778  -2.864  4.060   1.00 36.94  ? 329 GLU A CD    1 
ATOM   2550 O  OE1   . GLU A 1 329 ? 14.561  -2.559  5.247   1.00 36.78  ? 329 GLU A OE1   1 
ATOM   2551 O  OE2   . GLU A 1 329 ? 15.760  -3.566  3.736   1.00 34.53  ? 329 GLU A OE2   1 
ATOM   2552 N  N     . ASN A 1 330 ? 10.561  -5.248  1.794   1.00 33.46  ? 330 ASN A N     1 
ATOM   2553 C  CA    . ASN A 1 330 ? 9.460   -6.200  1.903   1.00 36.54  ? 330 ASN A CA    1 
ATOM   2554 C  C     . ASN A 1 330 ? 9.535   -7.047  3.175   1.00 34.78  ? 330 ASN A C     1 
ATOM   2555 O  O     . ASN A 1 330 ? 8.695   -7.931  3.366   1.00 33.37  ? 330 ASN A O     1 
ATOM   2556 C  CB    . ASN A 1 330 ? 9.448   -7.130  0.666   1.00 33.81  ? 330 ASN A CB    1 
ATOM   2557 C  CG    . ASN A 1 330 ? 8.100   -7.823  0.435   1.00 38.14  ? 330 ASN A CG    1 
ATOM   2558 O  OD1   . ASN A 1 330 ? 7.044   -7.274  0.722   1.00 39.43  ? 330 ASN A OD1   1 
ATOM   2559 N  ND2   . ASN A 1 330 ? 8.145   -9.043  -0.117  1.00 39.03  ? 330 ASN A ND2   1 
ATOM   2560 N  N     . GLY A 1 331 ? 10.548  -6.846  4.015   1.00 33.37  ? 331 GLY A N     1 
ATOM   2561 C  CA    . GLY A 1 331 ? 10.706  -7.594  5.246   1.00 32.85  ? 331 GLY A CA    1 
ATOM   2562 C  C     . GLY A 1 331 ? 11.542  -6.782  6.219   1.00 34.31  ? 331 GLY A C     1 
ATOM   2563 O  O     . GLY A 1 331 ? 11.954  -5.658  5.917   1.00 34.62  ? 331 GLY A O     1 
ATOM   2564 N  N     . PHE A 1 332 ? 11.803  -7.367  7.390   1.00 32.72  ? 332 PHE A N     1 
ATOM   2565 C  CA    . PHE A 1 332 ? 12.694  -6.800  8.400   1.00 31.65  ? 332 PHE A CA    1 
ATOM   2566 C  C     . PHE A 1 332 ? 13.908  -7.703  8.588   1.00 33.04  ? 332 PHE A C     1 
ATOM   2567 O  O     . PHE A 1 332 ? 13.767  -8.923  8.711   1.00 33.24  ? 332 PHE A O     1 
ATOM   2568 C  CB    . PHE A 1 332 ? 11.980  -6.645  9.749   1.00 35.36  ? 332 PHE A CB    1 
ATOM   2569 C  CG    . PHE A 1 332 ? 10.613  -6.052  9.645   1.00 36.97  ? 332 PHE A CG    1 
ATOM   2570 C  CD1   . PHE A 1 332 ? 10.440  -4.761  9.161   1.00 35.99  ? 332 PHE A CD1   1 
ATOM   2571 C  CD2   . PHE A 1 332 ? 9.498   -6.785  10.032  1.00 35.05  ? 332 PHE A CD2   1 
ATOM   2572 C  CE1   . PHE A 1 332 ? 9.180   -4.203  9.060   1.00 42.09  ? 332 PHE A CE1   1 
ATOM   2573 C  CE2   . PHE A 1 332 ? 8.238   -6.249  9.939   1.00 39.11  ? 332 PHE A CE2   1 
ATOM   2574 C  CZ    . PHE A 1 332 ? 8.069   -4.943  9.455   1.00 39.18  ? 332 PHE A CZ    1 
ATOM   2575 N  N     . PHE A 1 333 ? 15.089  -7.098  8.616   1.00 33.57  ? 333 PHE A N     1 
ATOM   2576 C  CA    . PHE A 1 333 ? 16.368  -7.767  8.843   1.00 33.19  ? 333 PHE A CA    1 
ATOM   2577 C  C     . PHE A 1 333 ? 16.909  -7.221  10.163  1.00 31.54  ? 333 PHE A C     1 
ATOM   2578 O  O     . PHE A 1 333 ? 17.797  -6.372  10.194  1.00 30.48  ? 333 PHE A O     1 
ATOM   2579 C  CB    . PHE A 1 333 ? 17.320  -7.490  7.640   1.00 33.20  ? 333 PHE A CB    1 
ATOM   2580 C  CG    . PHE A 1 333 ? 18.620  -8.253  7.678   1.00 31.99  ? 333 PHE A CG    1 
ATOM   2581 C  CD1   . PHE A 1 333 ? 18.634  -9.633  7.486   1.00 36.53  ? 333 PHE A CD1   1 
ATOM   2582 C  CD2   . PHE A 1 333 ? 19.828  -7.583  7.865   1.00 36.41  ? 333 PHE A CD2   1 
ATOM   2583 C  CE1   . PHE A 1 333 ? 19.833  -10.343 7.492   1.00 37.32  ? 333 PHE A CE1   1 
ATOM   2584 C  CE2   . PHE A 1 333 ? 21.038  -8.286  7.880   1.00 35.23  ? 333 PHE A CE2   1 
ATOM   2585 C  CZ    . PHE A 1 333 ? 21.036  -9.666  7.686   1.00 35.21  ? 333 PHE A CZ    1 
ATOM   2586 N  N     . GLY A 1 334 ? 16.339  -7.705  11.263  1.00 33.10  ? 334 GLY A N     1 
ATOM   2587 C  CA    . GLY A 1 334 ? 16.551  -7.130  12.580  1.00 29.91  ? 334 GLY A CA    1 
ATOM   2588 C  C     . GLY A 1 334 ? 17.511  -7.899  13.474  1.00 32.51  ? 334 GLY A C     1 
ATOM   2589 O  O     . GLY A 1 334 ? 17.664  -9.113  13.356  1.00 35.41  ? 334 GLY A O     1 
ATOM   2590 N  N     . VAL A 1 335 ? 18.148  -7.153  14.377  1.00 32.63  ? 335 VAL A N     1 
ATOM   2591 C  CA    . VAL A 1 335 ? 19.067  -7.677  15.382  1.00 32.62  ? 335 VAL A CA    1 
ATOM   2592 C  C     . VAL A 1 335 ? 18.287  -8.570  16.338  1.00 33.71  ? 335 VAL A C     1 
ATOM   2593 O  O     . VAL A 1 335 ? 17.282  -8.141  16.919  1.00 37.67  ? 335 VAL A O     1 
ATOM   2594 C  CB    . VAL A 1 335 ? 19.727  -6.511  16.149  1.00 33.35  ? 335 VAL A CB    1 
ATOM   2595 C  CG1   . VAL A 1 335 ? 20.564  -7.026  17.310  1.00 37.23  ? 335 VAL A CG1   1 
ATOM   2596 C  CG2   . VAL A 1 335 ? 20.577  -5.621  15.218  1.00 36.79  ? 335 VAL A CG2   1 
ATOM   2597 N  N     . ALA A 1 336 ? 18.747  -9.817  16.516  1.00 35.46  ? 336 ALA A N     1 
ATOM   2598 C  CA    . ALA A 1 336 ? 18.043  -10.724 17.423  1.00 33.73  ? 336 ALA A CA    1 
ATOM   2599 C  C     . ALA A 1 336 ? 18.321  -10.437 18.903  1.00 38.81  ? 336 ALA A C     1 
ATOM   2600 O  O     . ALA A 1 336 ? 17.358  -10.264 19.666  1.00 40.95  ? 336 ALA A O     1 
ATOM   2601 C  CB    . ALA A 1 336 ? 18.367  -12.192 17.091  1.00 37.32  ? 336 ALA A CB    1 
ATOM   2602 N  N     . PRO A 1 337 ? 19.579  -10.391 19.365  1.00 39.33  ? 337 PRO A N     1 
ATOM   2603 C  CA    . PRO A 1 337 ? 19.815  -10.259 20.814  1.00 41.41  ? 337 PRO A CA    1 
ATOM   2604 C  C     . PRO A 1 337 ? 19.103  -9.047  21.409  1.00 41.00  ? 337 PRO A C     1 
ATOM   2605 O  O     . PRO A 1 337 ? 19.041  -7.974  20.804  1.00 45.01  ? 337 PRO A O     1 
ATOM   2606 C  CB    . PRO A 1 337 ? 21.341  -10.128 20.917  1.00 40.04  ? 337 PRO A CB    1 
ATOM   2607 C  CG    . PRO A 1 337 ? 21.849  -10.865 19.719  1.00 43.34  ? 337 PRO A CG    1 
ATOM   2608 C  CD    . PRO A 1 337 ? 20.858  -10.507 18.626  1.00 35.14  ? 337 PRO A CD    1 
ATOM   2609 N  N     . GLY A 1 338 ? 18.533  -9.240  22.600  1.00 39.04  ? 338 GLY A N     1 
ATOM   2610 C  CA    . GLY A 1 338 ? 17.737  -8.226  23.257  1.00 40.82  ? 338 GLY A CA    1 
ATOM   2611 C  C     . GLY A 1 338 ? 16.254  -8.260  22.940  1.00 43.01  ? 338 GLY A C     1 
ATOM   2612 O  O     . GLY A 1 338 ? 15.470  -7.606  23.644  1.00 44.23  ? 338 GLY A O     1 
ATOM   2613 N  N     . THR A 1 339 ? 15.842  -8.995  21.911  1.00 39.79  ? 339 THR A N     1 
ATOM   2614 C  CA    . THR A 1 339 ? 14.431  -9.144  21.566  1.00 41.61  ? 339 THR A CA    1 
ATOM   2615 C  C     . THR A 1 339 ? 13.754  -10.114 22.529  1.00 43.43  ? 339 THR A C     1 
ATOM   2616 O  O     . THR A 1 339 ? 14.156  -11.282 22.624  1.00 44.43  ? 339 THR A O     1 
ATOM   2617 C  CB    . THR A 1 339 ? 14.296  -9.659  20.134  1.00 40.28  ? 339 THR A CB    1 
ATOM   2618 O  OG1   . THR A 1 339 ? 15.008  -8.790  19.258  1.00 39.58  ? 339 THR A OG1   1 
ATOM   2619 C  CG2   . THR A 1 339 ? 12.845  -9.726  19.701  1.00 41.90  ? 339 THR A CG2   1 
ATOM   2620 N  N     . SER A 1 340 ? 12.698  -9.655  23.203  1.00 41.55  ? 340 SER A N     1 
ATOM   2621 C  CA    . SER A 1 340 ? 11.965  -10.509 24.127  1.00 46.44  ? 340 SER A CA    1 
ATOM   2622 C  C     . SER A 1 340 ? 10.514  -10.056 24.188  1.00 50.26  ? 340 SER A C     1 
ATOM   2623 O  O     . SER A 1 340 ? 10.132  -9.021  23.631  1.00 47.81  ? 340 SER A O     1 
ATOM   2624 C  CB    . SER A 1 340 ? 12.593  -10.490 25.522  1.00 48.89  ? 340 SER A CB    1 
ATOM   2625 O  OG    . SER A 1 340 ? 12.557  -9.185  26.067  1.00 56.45  ? 340 SER A OG    1 
ATOM   2626 N  N     . VAL A 1 341 ? 9.708   -10.837 24.908  1.00 48.94  ? 341 VAL A N     1 
ATOM   2627 C  CA    . VAL A 1 341 ? 8.305   -10.487 25.092  1.00 52.65  ? 341 VAL A CA    1 
ATOM   2628 C  C     . VAL A 1 341 ? 8.175   -9.119  25.746  1.00 51.41  ? 341 VAL A C     1 
ATOM   2629 O  O     . VAL A 1 341 ? 7.215   -8.383  25.482  1.00 55.81  ? 341 VAL A O     1 
ATOM   2630 C  CB    . VAL A 1 341 ? 7.595   -11.597 25.903  1.00 57.97  ? 341 VAL A CB    1 
ATOM   2631 C  CG1   . VAL A 1 341 ? 6.240   -11.133 26.403  1.00 63.53  ? 341 VAL A CG1   1 
ATOM   2632 C  CG2   . VAL A 1 341 ? 7.432   -12.825 25.044  1.00 61.52  ? 341 VAL A CG2   1 
ATOM   2633 N  N     . LYS A 1 342 ? 9.143   -8.732  26.575  1.00 49.83  ? 342 LYS A N     1 
ATOM   2634 C  CA    . LYS A 1 342 ? 9.026   -7.461  27.276  1.00 47.61  ? 342 LYS A CA    1 
ATOM   2635 C  C     . LYS A 1 342 ? 9.562   -6.281  26.470  1.00 53.33  ? 342 LYS A C     1 
ATOM   2636 O  O     . LYS A 1 342 ? 9.052   -5.163  26.622  1.00 52.54  ? 342 LYS A O     1 
ATOM   2637 C  CB    . LYS A 1 342 ? 9.732   -7.534  28.632  1.00 61.32  ? 342 LYS A CB    1 
ATOM   2638 C  CG    . LYS A 1 342 ? 11.252  -7.605  28.590  1.00 67.81  ? 342 LYS A CG    1 
ATOM   2639 C  CD    . LYS A 1 342 ? 11.813  -7.529  30.017  1.00 77.65  ? 342 LYS A CD    1 
ATOM   2640 C  CE    . LYS A 1 342 ? 13.228  -6.953  30.054  1.00 83.88  ? 342 LYS A CE    1 
ATOM   2641 N  NZ    . LYS A 1 342 ? 13.247  -5.482  29.792  1.00 77.81  ? 342 LYS A NZ    1 
ATOM   2642 N  N     . THR A 1 343 ? 10.562  -6.494  25.609  1.00 48.36  ? 343 THR A N     1 
ATOM   2643 C  CA    . THR A 1 343 ? 11.129  -5.383  24.852  1.00 47.57  ? 343 THR A CA    1 
ATOM   2644 C  C     . THR A 1 343 ? 10.444  -5.177  23.511  1.00 48.41  ? 343 THR A C     1 
ATOM   2645 O  O     . THR A 1 343 ? 10.244  -4.033  23.088  1.00 48.11  ? 343 THR A O     1 
ATOM   2646 C  CB    . THR A 1 343 ? 12.625  -5.590  24.605  1.00 47.06  ? 343 THR A CB    1 
ATOM   2647 O  OG1   . THR A 1 343 ? 12.822  -6.782  23.833  1.00 45.92  ? 343 THR A OG1   1 
ATOM   2648 C  CG2   . THR A 1 343 ? 13.392  -5.673  25.918  1.00 53.08  ? 343 THR A CG2   1 
ATOM   2649 N  N     . ASN A 1 344 ? 10.124  -6.250  22.791  1.00 41.91  ? 344 ASN A N     1 
ATOM   2650 C  CA    . ASN A 1 344 ? 9.558   -6.126  21.449  1.00 44.32  ? 344 ASN A CA    1 
ATOM   2651 C  C     . ASN A 1 344 ? 8.631   -7.309  21.199  1.00 46.52  ? 344 ASN A C     1 
ATOM   2652 O  O     . ASN A 1 344 ? 8.901   -8.171  20.352  1.00 44.45  ? 344 ASN A O     1 
ATOM   2653 C  CB    . ASN A 1 344 ? 10.679  -6.031  20.406  1.00 37.05  ? 344 ASN A CB    1 
ATOM   2654 C  CG    . ASN A 1 344 ? 10.197  -5.533  19.057  1.00 40.80  ? 344 ASN A CG    1 
ATOM   2655 O  OD1   . ASN A 1 344 ? 8.999   -5.454  18.796  1.00 42.99  ? 344 ASN A OD1   1 
ATOM   2656 N  ND2   . ASN A 1 344 ? 11.134  -5.211  18.183  1.00 39.42  ? 344 ASN A ND2   1 
ATOM   2657 N  N     . PRO A 1 345 ? 7.502   -7.368  21.921  1.00 44.94  ? 345 PRO A N     1 
ATOM   2658 C  CA    . PRO A 1 345 ? 6.558   -8.480  21.729  1.00 44.83  ? 345 PRO A CA    1 
ATOM   2659 C  C     . PRO A 1 345 ? 6.028   -8.603  20.312  1.00 46.66  ? 345 PRO A C     1 
ATOM   2660 O  O     . PRO A 1 345 ? 5.720   -9.721  19.873  1.00 47.98  ? 345 PRO A O     1 
ATOM   2661 C  CB    . PRO A 1 345 ? 5.428   -8.158  22.725  1.00 49.74  ? 345 PRO A CB    1 
ATOM   2662 C  CG    . PRO A 1 345 ? 5.553   -6.659  22.956  1.00 47.99  ? 345 PRO A CG    1 
ATOM   2663 C  CD    . PRO A 1 345 ? 7.018   -6.404  22.929  1.00 46.76  ? 345 PRO A CD    1 
ATOM   2664 N  N     . ASN A 1 346 ? 5.913   -7.495  19.579  1.00 44.72  ? 346 ASN A N     1 
ATOM   2665 C  CA    . ASN A 1 346 ? 5.414   -7.572  18.213  1.00 43.31  ? 346 ASN A CA    1 
ATOM   2666 C  C     . ASN A 1 346 ? 6.428   -8.233  17.289  1.00 44.30  ? 346 ASN A C     1 
ATOM   2667 O  O     . ASN A 1 346 ? 6.036   -8.889  16.319  1.00 47.31  ? 346 ASN A O     1 
ATOM   2668 C  CB    . ASN A 1 346 ? 5.037   -6.179  17.706  1.00 45.25  ? 346 ASN A CB    1 
ATOM   2669 C  CG    . ASN A 1 346 ? 3.797   -5.641  18.386  1.00 50.09  ? 346 ASN A CG    1 
ATOM   2670 O  OD1   . ASN A 1 346 ? 3.734   -4.471  18.785  1.00 48.65  ? 346 ASN A OD1   1 
ATOM   2671 N  ND2   . ASN A 1 346 ? 2.809   -6.504  18.540  1.00 44.73  ? 346 ASN A ND2   1 
ATOM   2672 N  N     . ALA A 1 347 ? 7.722   -8.100  17.593  1.00 41.69  ? 347 ALA A N     1 
ATOM   2673 C  CA    . ALA A 1 347 ? 8.730   -8.860  16.862  1.00 41.33  ? 347 ALA A CA    1 
ATOM   2674 C  C     . ALA A 1 347 ? 8.609   -10.348 17.157  1.00 44.63  ? 347 ALA A C     1 
ATOM   2675 O  O     . ALA A 1 347 ? 8.735   -11.172 16.247  1.00 43.18  ? 347 ALA A O     1 
ATOM   2676 C  CB    . ALA A 1 347 ? 10.130  -8.370  17.212  1.00 41.18  ? 347 ALA A CB    1 
ATOM   2677 N  N     . ILE A 1 348 ? 8.355   -10.702 18.423  1.00 45.98  ? 348 ILE A N     1 
ATOM   2678 C  CA    . ILE A 1 348 ? 8.250   -12.109 18.815  1.00 41.32  ? 348 ILE A CA    1 
ATOM   2679 C  C     . ILE A 1 348 ? 7.131   -12.794 18.039  1.00 48.26  ? 348 ILE A C     1 
ATOM   2680 O  O     . ILE A 1 348 ? 7.290   -13.915 17.542  1.00 49.41  ? 348 ILE A O     1 
ATOM   2681 C  CB    . ILE A 1 348 ? 8.032   -12.234 20.334  1.00 46.63  ? 348 ILE A CB    1 
ATOM   2682 C  CG1   . ILE A 1 348 ? 9.239   -11.686 21.094  1.00 50.60  ? 348 ILE A CG1   1 
ATOM   2683 C  CG2   . ILE A 1 348 ? 7.828   -13.686 20.720  1.00 55.08  ? 348 ILE A CG2   1 
ATOM   2684 C  CD1   . ILE A 1 348 ? 10.528  -12.420 20.796  1.00 51.70  ? 348 ILE A CD1   1 
ATOM   2685 N  N     . LYS A 1 349 ? 5.972   -12.135 17.941  1.00 46.56  ? 349 LYS A N     1 
ATOM   2686 C  CA    . LYS A 1 349 ? 4.870   -12.689 17.159  1.00 50.89  ? 349 LYS A CA    1 
ATOM   2687 C  C     . LYS A 1 349 ? 5.225   -12.813 15.681  1.00 48.17  ? 349 LYS A C     1 
ATOM   2688 O  O     . LYS A 1 349 ? 4.713   -13.705 14.996  1.00 51.79  ? 349 LYS A O     1 
ATOM   2689 C  CB    . LYS A 1 349 ? 3.623   -11.819 17.314  1.00 52.57  ? 349 LYS A CB    1 
ATOM   2690 C  CG    . LYS A 1 349 ? 3.074   -11.722 18.725  1.00 62.51  ? 349 LYS A CG    1 
ATOM   2691 C  CD    . LYS A 1 349 ? 1.771   -10.939 18.708  1.00 68.66  ? 349 LYS A CD    1 
ATOM   2692 C  CE    . LYS A 1 349 ? 1.217   -10.699 20.094  1.00 75.30  ? 349 LYS A CE    1 
ATOM   2693 N  NZ    . LYS A 1 349 ? -0.091  -9.991  20.005  1.00 77.29  ? 349 LYS A NZ    1 
ATOM   2694 N  N     . THR A 1 350 ? 6.089   -11.933 15.171  1.00 47.85  ? 350 THR A N     1 
ATOM   2695 C  CA    . THR A 1 350 ? 6.362   -11.896 13.737  1.00 45.85  ? 350 THR A CA    1 
ATOM   2696 C  C     . THR A 1 350 ? 7.272   -13.045 13.295  1.00 43.65  ? 350 THR A C     1 
ATOM   2697 O  O     . THR A 1 350 ? 7.086   -13.594 12.200  1.00 41.96  ? 350 THR A O     1 
ATOM   2698 C  CB    . THR A 1 350 ? 6.989   -10.546 13.354  1.00 46.44  ? 350 THR A CB    1 
ATOM   2699 O  OG1   . THR A 1 350 ? 6.115   -9.465  13.727  1.00 46.31  ? 350 THR A OG1   1 
ATOM   2700 C  CG2   . THR A 1 350 ? 7.273   -10.472 11.846  1.00 40.99  ? 350 THR A CG2   1 
ATOM   2701 N  N     . ILE A 1 351 ? 8.248   -13.424 14.128  1.00 40.59  ? 351 ILE A N     1 
ATOM   2702 C  CA    . ILE A 1 351 ? 9.367   -14.255 13.681  1.00 40.82  ? 351 ILE A CA    1 
ATOM   2703 C  C     . ILE A 1 351 ? 9.144   -15.743 13.925  1.00 42.60  ? 351 ILE A C     1 
ATOM   2704 O  O     . ILE A 1 351 ? 10.072  -16.547 13.758  1.00 44.13  ? 351 ILE A O     1 
ATOM   2705 C  CB    . ILE A 1 351 ? 10.681  -13.820 14.352  1.00 36.27  ? 351 ILE A CB    1 
ATOM   2706 C  CG1   . ILE A 1 351 ? 10.584  -13.940 15.872  1.00 40.37  ? 351 ILE A CG1   1 
ATOM   2707 C  CG2   . ILE A 1 351 ? 11.059  -12.397 13.915  1.00 34.79  ? 351 ILE A CG2   1 
ATOM   2708 C  CD1   . ILE A 1 351 ? 11.824  -13.419 16.604  1.00 43.11  ? 351 ILE A CD1   1 
ATOM   2709 N  N     . GLN A 1 352 ? 7.936   -16.130 14.319  1.00 42.25  ? 352 GLN A N     1 
ATOM   2710 C  CA    . GLN A 1 352 ? 7.671   -17.538 14.614  1.00 45.74  ? 352 GLN A CA    1 
ATOM   2711 C  C     . GLN A 1 352 ? 7.260   -18.348 13.395  1.00 42.55  ? 352 GLN A C     1 
ATOM   2712 O  O     . GLN A 1 352 ? 6.937   -19.533 13.534  1.00 47.58  ? 352 GLN A O     1 
ATOM   2713 C  CB    . GLN A 1 352 ? 6.602   -17.646 15.689  1.00 48.38  ? 352 GLN A CB    1 
ATOM   2714 C  CG    . GLN A 1 352 ? 7.014   -16.907 16.919  1.00 53.57  ? 352 GLN A CG    1 
ATOM   2715 C  CD    . GLN A 1 352 ? 5.992   -16.949 18.007  1.00 62.44  ? 352 GLN A CD    1 
ATOM   2716 O  OE1   . GLN A 1 352 ? 4.840   -17.349 17.796  1.00 73.63  ? 352 GLN A OE1   1 
ATOM   2717 N  NE2   . GLN A 1 352 ? 6.405   -16.543 19.200  1.00 59.64  ? 352 GLN A NE2   1 
ATOM   2718 N  N     . LYS A 1 353 ? 7.273   -17.758 12.206  1.00 41.32  ? 353 LYS A N     1 
ATOM   2719 C  CA    . LYS A 1 353 ? 7.018   -18.549 11.015  1.00 45.60  ? 353 LYS A CA    1 
ATOM   2720 C  C     . LYS A 1 353 ? 7.657   -17.867 9.818   1.00 43.44  ? 353 LYS A C     1 
ATOM   2721 O  O     . LYS A 1 353 ? 7.848   -16.644 9.808   1.00 45.16  ? 353 LYS A O     1 
ATOM   2722 C  CB    . LYS A 1 353 ? 5.517   -18.786 10.788  1.00 52.27  ? 353 LYS A CB    1 
ATOM   2723 C  CG    . LYS A 1 353 ? 4.703   -17.566 10.419  1.00 53.43  ? 353 LYS A CG    1 
ATOM   2724 C  CD    . LYS A 1 353 ? 3.218   -17.944 10.366  1.00 59.15  ? 353 LYS A CD    1 
ATOM   2725 C  CE    . LYS A 1 353 ? 2.360   -16.745 9.980   1.00 65.46  ? 353 LYS A CE    1 
ATOM   2726 N  NZ    . LYS A 1 353 ? 0.919   -17.105 9.936   1.00 78.03  ? 353 LYS A NZ    1 
ATOM   2727 N  N     . ASN A 1 354 ? 8.030   -18.692 8.835   1.00 42.73  ? 354 ASN A N     1 
ATOM   2728 C  CA    . ASN A 1 354 ? 8.584   -18.228 7.562   1.00 41.66  ? 354 ASN A CA    1 
ATOM   2729 C  C     . ASN A 1 354 ? 9.784   -17.302 7.754   1.00 37.80  ? 354 ASN A C     1 
ATOM   2730 O  O     . ASN A 1 354 ? 9.964   -16.329 7.018   1.00 40.41  ? 354 ASN A O     1 
ATOM   2731 C  CB    . ASN A 1 354 ? 7.504   -17.543 6.727   1.00 42.70  ? 354 ASN A CB    1 
ATOM   2732 C  CG    . ASN A 1 354 ? 6.302   -18.432 6.494   1.00 48.13  ? 354 ASN A CG    1 
ATOM   2733 O  OD1   . ASN A 1 354 ? 6.439   -19.623 6.198   1.00 47.59  ? 354 ASN A OD1   1 
ATOM   2734 N  ND2   . ASN A 1 354 ? 5.115   -17.864 6.642   1.00 48.85  ? 354 ASN A ND2   1 
ATOM   2735 N  N     . THR A 1 355 ? 10.636  -17.614 8.729   1.00 39.07  ? 355 THR A N     1 
ATOM   2736 C  CA    . THR A 1 355 ? 11.713  -16.710 9.120   1.00 35.98  ? 355 THR A CA    1 
ATOM   2737 C  C     . THR A 1 355 ? 13.059  -17.418 9.096   1.00 38.36  ? 355 THR A C     1 
ATOM   2738 O  O     . THR A 1 355 ? 13.171  -18.566 9.538   1.00 38.88  ? 355 THR A O     1 
ATOM   2739 C  CB    . THR A 1 355 ? 11.445  -16.123 10.521  1.00 38.79  ? 355 THR A CB    1 
ATOM   2740 O  OG1   . THR A 1 355 ? 10.261  -15.322 10.472  1.00 37.35  ? 355 THR A OG1   1 
ATOM   2741 C  CG2   . THR A 1 355 ? 12.601  -15.252 10.988  1.00 32.44  ? 355 THR A CG2   1 
ATOM   2742 N  N     . ILE A 1 356 ? 14.072  -16.730 8.560   1.00 36.28  ? 356 ILE A N     1 
ATOM   2743 C  CA    . ILE A 1 356 ? 15.446  -17.218 8.504   1.00 34.04  ? 356 ILE A CA    1 
ATOM   2744 C  C     . ILE A 1 356 ? 16.265  -16.511 9.576   1.00 33.90  ? 356 ILE A C     1 
ATOM   2745 O  O     . ILE A 1 356 ? 16.357  -15.279 9.581   1.00 36.10  ? 356 ILE A O     1 
ATOM   2746 C  CB    . ILE A 1 356 ? 16.074  -16.984 7.122   1.00 35.81  ? 356 ILE A CB    1 
ATOM   2747 C  CG1   . ILE A 1 356 ? 15.306  -17.746 6.036   1.00 39.99  ? 356 ILE A CG1   1 
ATOM   2748 C  CG2   . ILE A 1 356 ? 17.557  -17.392 7.138   1.00 32.60  ? 356 ILE A CG2   1 
ATOM   2749 C  CD1   . ILE A 1 356 ? 15.970  -17.686 4.662   1.00 41.40  ? 356 ILE A CD1   1 
ATOM   2750 N  N     . PHE A 1 357 ? 16.875  -17.283 10.473  1.00 32.59  ? 357 PHE A N     1 
ATOM   2751 C  CA    . PHE A 1 357 ? 17.751  -16.738 11.506  1.00 35.49  ? 357 PHE A CA    1 
ATOM   2752 C  C     . PHE A 1 357 ? 19.196  -17.003 11.114  1.00 35.65  ? 357 PHE A C     1 
ATOM   2753 O  O     . PHE A 1 357 ? 19.513  -18.077 10.591  1.00 38.40  ? 357 PHE A O     1 
ATOM   2754 C  CB    . PHE A 1 357 ? 17.488  -17.370 12.884  1.00 33.85  ? 357 PHE A CB    1 
ATOM   2755 C  CG    . PHE A 1 357 ? 16.083  -17.195 13.394  1.00 33.94  ? 357 PHE A CG    1 
ATOM   2756 C  CD1   . PHE A 1 357 ? 15.082  -18.077 13.029  1.00 34.35  ? 357 PHE A CD1   1 
ATOM   2757 C  CD2   . PHE A 1 357 ? 15.772  -16.158 14.264  1.00 39.41  ? 357 PHE A CD2   1 
ATOM   2758 C  CE1   . PHE A 1 357 ? 13.788  -17.924 13.510  1.00 38.52  ? 357 PHE A CE1   1 
ATOM   2759 C  CE2   . PHE A 1 357 ? 14.472  -15.999 14.757  1.00 38.01  ? 357 PHE A CE2   1 
ATOM   2760 C  CZ    . PHE A 1 357 ? 13.485  -16.869 14.377  1.00 36.64  ? 357 PHE A CZ    1 
ATOM   2761 N  N     . THR A 1 358 ? 20.076  -16.044 11.404  1.00 33.66  ? 358 THR A N     1 
ATOM   2762 C  CA    . THR A 1 358 ? 21.504  -16.182 11.135  1.00 37.02  ? 358 THR A CA    1 
ATOM   2763 C  C     . THR A 1 358 ? 22.271  -15.927 12.425  1.00 38.26  ? 358 THR A C     1 
ATOM   2764 O  O     . THR A 1 358 ? 22.147  -14.850 13.014  1.00 36.26  ? 358 THR A O     1 
ATOM   2765 C  CB    . THR A 1 358 ? 21.973  -15.206 10.039  1.00 37.39  ? 358 THR A CB    1 
ATOM   2766 O  OG1   . THR A 1 358 ? 21.141  -15.349 8.879   1.00 37.40  ? 358 THR A OG1   1 
ATOM   2767 C  CG2   . THR A 1 358 ? 23.400  -15.512 9.645   1.00 36.87  ? 358 THR A CG2   1 
ATOM   2768 N  N     . ASN A 1 359 ? 23.041  -16.927 12.864  1.00 39.21  ? 359 ASN A N     1 
ATOM   2769 C  CA    . ASN A 1 359 ? 24.005  -16.803 13.962  1.00 41.42  ? 359 ASN A CA    1 
ATOM   2770 C  C     . ASN A 1 359 ? 23.352  -16.640 15.341  1.00 41.60  ? 359 ASN A C     1 
ATOM   2771 O  O     . ASN A 1 359 ? 23.951  -16.054 16.249  1.00 41.06  ? 359 ASN A O     1 
ATOM   2772 C  CB    . ASN A 1 359 ? 24.995  -15.659 13.705  1.00 38.12  ? 359 ASN A CB    1 
ATOM   2773 C  CG    . ASN A 1 359 ? 25.983  -15.978 12.582  1.00 41.13  ? 359 ASN A CG    1 
ATOM   2774 O  OD1   . ASN A 1 359 ? 26.172  -17.137 12.211  1.00 41.16  ? 359 ASN A OD1   1 
ATOM   2775 N  ND2   . ASN A 1 359 ? 26.614  -14.947 12.044  1.00 42.60  ? 359 ASN A ND2   1 
ATOM   2776 N  N     . VAL A 1 360 ? 22.150  -17.165 15.546  1.00 40.79  ? 360 VAL A N     1 
ATOM   2777 C  CA    . VAL A 1 360 ? 21.596  -17.306 16.888  1.00 38.15  ? 360 VAL A CA    1 
ATOM   2778 C  C     . VAL A 1 360 ? 21.808  -18.742 17.361  1.00 43.33  ? 360 VAL A C     1 
ATOM   2779 O  O     . VAL A 1 360 ? 22.227  -19.615 16.604  1.00 38.88  ? 360 VAL A O     1 
ATOM   2780 C  CB    . VAL A 1 360 ? 20.102  -16.902 16.952  1.00 36.62  ? 360 VAL A CB    1 
ATOM   2781 C  CG1   . VAL A 1 360 ? 19.903  -15.479 16.418  1.00 36.66  ? 360 VAL A CG1   1 
ATOM   2782 C  CG2   . VAL A 1 360 ? 19.220  -17.924 16.213  1.00 36.16  ? 360 VAL A CG2   1 
ATOM   2783 N  N     . ALA A 1 361 ? 21.520  -18.996 18.641  1.00 40.63  ? 361 ALA A N     1 
ATOM   2784 C  CA    . ALA A 1 361 ? 21.665  -20.343 19.176  1.00 43.16  ? 361 ALA A CA    1 
ATOM   2785 C  C     . ALA A 1 361 ? 20.425  -21.181 18.877  1.00 42.81  ? 361 ALA A C     1 
ATOM   2786 O  O     . ALA A 1 361 ? 19.327  -20.661 18.680  1.00 42.24  ? 361 ALA A O     1 
ATOM   2787 C  CB    . ALA A 1 361 ? 21.906  -20.309 20.689  1.00 43.86  ? 361 ALA A CB    1 
ATOM   2788 N  N     . GLU A 1 362 ? 20.613  -22.499 18.851  1.00 42.10  ? 362 GLU A N     1 
ATOM   2789 C  CA    . GLU A 1 362 ? 19.520  -23.449 18.682  1.00 45.62  ? 362 GLU A CA    1 
ATOM   2790 C  C     . GLU A 1 362 ? 19.332  -24.241 19.964  1.00 47.88  ? 362 GLU A C     1 
ATOM   2791 O  O     . GLU A 1 362 ? 20.308  -24.728 20.542  1.00 47.13  ? 362 GLU A O     1 
ATOM   2792 C  CB    . GLU A 1 362 ? 19.802  -24.427 17.530  1.00 45.23  ? 362 GLU A CB    1 
ATOM   2793 C  CG    . GLU A 1 362 ? 18.664  -25.396 17.215  1.00 48.33  ? 362 GLU A CG    1 
ATOM   2794 C  CD    . GLU A 1 362 ? 19.022  -26.358 16.073  1.00 52.94  ? 362 GLU A CD    1 
ATOM   2795 O  OE1   . GLU A 1 362 ? 20.090  -26.178 15.452  1.00 55.48  ? 362 GLU A OE1   1 
ATOM   2796 O  OE2   . GLU A 1 362 ? 18.241  -27.286 15.789  1.00 52.85  ? 362 GLU A OE2   1 
ATOM   2797 N  N     . THR A 1 363 ? 18.080  -24.381 20.398  1.00 45.83  ? 363 THR A N     1 
ATOM   2798 C  CA    . THR A 1 363 ? 17.779  -25.265 21.510  1.00 47.59  ? 363 THR A CA    1 
ATOM   2799 C  C     . THR A 1 363 ? 17.530  -26.684 20.989  1.00 48.22  ? 363 THR A C     1 
ATOM   2800 O  O     . THR A 1 363 ? 17.202  -26.898 19.818  1.00 47.02  ? 363 THR A O     1 
ATOM   2801 C  CB    . THR A 1 363 ? 16.572  -24.766 22.309  1.00 48.63  ? 363 THR A CB    1 
ATOM   2802 O  OG1   . THR A 1 363 ? 15.414  -24.716 21.468  1.00 48.80  ? 363 THR A OG1   1 
ATOM   2803 C  CG2   . THR A 1 363 ? 16.843  -23.368 22.879  1.00 47.90  ? 363 THR A CG2   1 
ATOM   2804 N  N     . SER A 1 364 ? 17.693  -27.661 21.881  1.00 51.11  ? 364 SER A N     1 
ATOM   2805 C  CA    . SER A 1 364 ? 17.605  -29.056 21.462  1.00 52.40  ? 364 SER A CA    1 
ATOM   2806 C  C     . SER A 1 364 ? 16.193  -29.462 21.072  1.00 53.80  ? 364 SER A C     1 
ATOM   2807 O  O     . SER A 1 364 ? 16.024  -30.492 20.410  1.00 58.28  ? 364 SER A O     1 
ATOM   2808 C  CB    . SER A 1 364 ? 18.125  -29.975 22.564  1.00 53.40  ? 364 SER A CB    1 
ATOM   2809 O  OG    . SER A 1 364 ? 17.438  -29.747 23.777  1.00 56.32  ? 364 SER A OG    1 
ATOM   2810 N  N     . ASP A 1 365 ? 15.173  -28.696 21.465  1.00 52.07  ? 365 ASP A N     1 
ATOM   2811 C  CA    . ASP A 1 365 ? 13.822  -28.975 21.001  1.00 52.96  ? 365 ASP A CA    1 
ATOM   2812 C  C     . ASP A 1 365 ? 13.480  -28.172 19.755  1.00 49.16  ? 365 ASP A C     1 
ATOM   2813 O  O     . ASP A 1 365 ? 12.300  -27.999 19.435  1.00 52.64  ? 365 ASP A O     1 
ATOM   2814 C  CB    . ASP A 1 365 ? 12.796  -28.740 22.118  1.00 52.96  ? 365 ASP A CB    1 
ATOM   2815 C  CG    . ASP A 1 365 ? 12.719  -27.273 22.566  1.00 56.43  ? 365 ASP A CG    1 
ATOM   2816 O  OD1   . ASP A 1 365 ? 13.577  -26.451 22.164  1.00 56.22  ? 365 ASP A OD1   1 
ATOM   2817 O  OD2   . ASP A 1 365 ? 11.781  -26.944 23.321  1.00 58.08  ? 365 ASP A OD2   1 
ATOM   2818 N  N     . GLY A 1 366 ? 14.494  -27.671 19.056  1.00 49.84  ? 366 GLY A N     1 
ATOM   2819 C  CA    . GLY A 1 366 ? 14.305  -27.042 17.765  1.00 49.97  ? 366 GLY A CA    1 
ATOM   2820 C  C     . GLY A 1 366 ? 13.900  -25.590 17.778  1.00 49.48  ? 366 GLY A C     1 
ATOM   2821 O  O     . GLY A 1 366 ? 13.327  -25.126 16.789  1.00 49.09  ? 366 GLY A O     1 
ATOM   2822 N  N     . GLY A 1 367 ? 14.178  -24.854 18.858  1.00 48.19  ? 367 GLY A N     1 
ATOM   2823 C  CA    . GLY A 1 367 ? 13.913  -23.437 18.927  1.00 47.47  ? 367 GLY A CA    1 
ATOM   2824 C  C     . GLY A 1 367 ? 15.175  -22.598 18.830  1.00 45.21  ? 367 GLY A C     1 
ATOM   2825 O  O     . GLY A 1 367 ? 16.260  -23.088 18.512  1.00 42.43  ? 367 GLY A O     1 
ATOM   2826 N  N     . VAL A 1 368 ? 15.012  -21.301 19.113  1.00 45.37  ? 368 VAL A N     1 
ATOM   2827 C  CA    . VAL A 1 368 ? 16.084  -20.315 19.012  1.00 42.95  ? 368 VAL A CA    1 
ATOM   2828 C  C     . VAL A 1 368 ? 16.396  -19.774 20.399  1.00 45.79  ? 368 VAL A C     1 
ATOM   2829 O  O     . VAL A 1 368 ? 15.534  -19.747 21.280  1.00 45.66  ? 368 VAL A O     1 
ATOM   2830 C  CB    . VAL A 1 368 ? 15.733  -19.133 18.066  1.00 43.01  ? 368 VAL A CB    1 
ATOM   2831 C  CG1   . VAL A 1 368 ? 15.617  -19.600 16.622  1.00 40.57  ? 368 VAL A CG1   1 
ATOM   2832 C  CG2   . VAL A 1 368 ? 14.444  -18.458 18.518  1.00 43.01  ? 368 VAL A CG2   1 
ATOM   2833 N  N     . TYR A 1 369 ? 17.627  -19.303 20.588  1.00 43.24  ? 369 TYR A N     1 
ATOM   2834 C  CA    . TYR A 1 369 ? 17.978  -18.641 21.836  1.00 44.26  ? 369 TYR A CA    1 
ATOM   2835 C  C     . TYR A 1 369 ? 18.954  -17.508 21.568  1.00 41.83  ? 369 TYR A C     1 
ATOM   2836 O  O     . TYR A 1 369 ? 19.751  -17.569 20.634  1.00 42.29  ? 369 TYR A O     1 
ATOM   2837 C  CB    . TYR A 1 369 ? 18.592  -19.617 22.838  1.00 45.17  ? 369 TYR A CB    1 
ATOM   2838 C  CG    . TYR A 1 369 ? 18.165  -19.347 24.250  1.00 46.64  ? 369 TYR A CG    1 
ATOM   2839 C  CD1   . TYR A 1 369 ? 16.841  -19.535 24.630  1.00 49.67  ? 369 TYR A CD1   1 
ATOM   2840 C  CD2   . TYR A 1 369 ? 19.073  -18.927 25.211  1.00 47.73  ? 369 TYR A CD2   1 
ATOM   2841 C  CE1   . TYR A 1 369 ? 16.425  -19.316 25.926  1.00 50.00  ? 369 TYR A CE1   1 
ATOM   2842 C  CE2   . TYR A 1 369 ? 18.661  -18.707 26.526  1.00 50.96  ? 369 TYR A CE2   1 
ATOM   2843 C  CZ    . TYR A 1 369 ? 17.333  -18.900 26.870  1.00 52.40  ? 369 TYR A CZ    1 
ATOM   2844 O  OH    . TYR A 1 369 ? 16.892  -18.680 28.159  1.00 57.76  ? 369 TYR A OH    1 
ATOM   2845 N  N     . TRP A 1 370 ? 18.889  -16.471 22.399  1.00 42.26  ? 370 TRP A N     1 
ATOM   2846 C  CA    . TRP A 1 370 ? 19.876  -15.403 22.316  1.00 44.63  ? 370 TRP A CA    1 
ATOM   2847 C  C     . TRP A 1 370 ? 19.864  -14.641 23.629  1.00 47.42  ? 370 TRP A C     1 
ATOM   2848 O  O     . TRP A 1 370 ? 18.920  -14.745 24.422  1.00 46.76  ? 370 TRP A O     1 
ATOM   2849 C  CB    . TRP A 1 370 ? 19.622  -14.456 21.124  1.00 39.56  ? 370 TRP A CB    1 
ATOM   2850 C  CG    . TRP A 1 370 ? 18.225  -13.934 21.049  1.00 39.59  ? 370 TRP A CG    1 
ATOM   2851 C  CD1   . TRP A 1 370 ? 17.649  -13.018 21.880  1.00 39.95  ? 370 TRP A CD1   1 
ATOM   2852 C  CD2   . TRP A 1 370 ? 17.216  -14.301 20.096  1.00 38.28  ? 370 TRP A CD2   1 
ATOM   2853 N  NE1   . TRP A 1 370 ? 16.347  -12.791 21.505  1.00 39.30  ? 370 TRP A NE1   1 
ATOM   2854 C  CE2   . TRP A 1 370 ? 16.056  -13.567 20.414  1.00 38.42  ? 370 TRP A CE2   1 
ATOM   2855 C  CE3   . TRP A 1 370 ? 17.186  -15.176 19.002  1.00 40.24  ? 370 TRP A CE3   1 
ATOM   2856 C  CZ2   . TRP A 1 370 ? 14.880  -13.673 19.678  1.00 37.86  ? 370 TRP A CZ2   1 
ATOM   2857 C  CZ3   . TRP A 1 370 ? 16.017  -15.289 18.276  1.00 37.36  ? 370 TRP A CZ3   1 
ATOM   2858 C  CH2   . TRP A 1 370 ? 14.880  -14.532 18.614  1.00 40.49  ? 370 TRP A CH2   1 
ATOM   2859 N  N     . GLU A 1 371 ? 20.937  -13.887 23.849  1.00 46.68  ? 371 GLU A N     1 
ATOM   2860 C  CA    . GLU A 1 371 ? 21.041  -13.029 25.026  1.00 49.60  ? 371 GLU A CA    1 
ATOM   2861 C  C     . GLU A 1 371 ? 19.854  -12.073 25.100  1.00 48.37  ? 371 GLU A C     1 
ATOM   2862 O  O     . GLU A 1 371 ? 19.452  -11.479 24.095  1.00 44.22  ? 371 GLU A O     1 
ATOM   2863 C  CB    . GLU A 1 371 ? 22.359  -12.246 24.988  1.00 49.32  ? 371 GLU A CB    1 
ATOM   2864 C  CG    . GLU A 1 371 ? 23.598  -13.046 25.439  1.00 53.21  ? 371 GLU A CG    1 
ATOM   2865 C  CD    . GLU A 1 371 ? 23.854  -14.312 24.614  1.00 54.23  ? 371 GLU A CD    1 
ATOM   2866 O  OE1   . GLU A 1 371 ? 23.588  -14.311 23.388  1.00 50.46  ? 371 GLU A OE1   1 
ATOM   2867 O  OE2   . GLU A 1 371 ? 24.329  -15.312 25.198  1.00 52.01  ? 371 GLU A OE2   1 
ATOM   2868 N  N     . GLY A 1 372 ? 19.277  -11.947 26.294  1.00 51.11  ? 372 GLY A N     1 
ATOM   2869 C  CA    . GLY A 1 372 ? 18.158  -11.061 26.510  1.00 45.92  ? 372 GLY A CA    1 
ATOM   2870 C  C     . GLY A 1 372 ? 16.818  -11.591 26.055  1.00 50.22  ? 372 GLY A C     1 
ATOM   2871 O  O     . GLY A 1 372 ? 15.819  -10.862 26.160  1.00 45.77  ? 372 GLY A O     1 
ATOM   2872 N  N     . ILE A 1 373 ? 16.755  -12.838 25.564  1.00 44.73  ? 373 ILE A N     1 
ATOM   2873 C  CA    . ILE A 1 373 ? 15.469  -13.425 25.185  1.00 44.66  ? 373 ILE A CA    1 
ATOM   2874 C  C     . ILE A 1 373 ? 14.536  -13.487 26.382  1.00 46.65  ? 373 ILE A C     1 
ATOM   2875 O  O     . ILE A 1 373 ? 13.309  -13.475 26.224  1.00 49.90  ? 373 ILE A O     1 
ATOM   2876 C  CB    . ILE A 1 373 ? 15.668  -14.820 24.554  1.00 47.28  ? 373 ILE A CB    1 
ATOM   2877 C  CG1   . ILE A 1 373 ? 14.396  -15.275 23.837  1.00 48.38  ? 373 ILE A CG1   1 
ATOM   2878 C  CG2   . ILE A 1 373 ? 16.021  -15.845 25.617  1.00 49.15  ? 373 ILE A CG2   1 
ATOM   2879 C  CD1   . ILE A 1 373 ? 14.632  -16.444 22.909  1.00 49.40  ? 373 ILE A CD1   1 
ATOM   2880 N  N     . ASP A 1 374 ? 15.092  -13.587 27.590  1.00 50.06  ? 374 ASP A N     1 
ATOM   2881 C  CA    . ASP A 1 374 ? 14.336  -13.406 28.832  1.00 53.97  ? 374 ASP A CA    1 
ATOM   2882 C  C     . ASP A 1 374 ? 13.307  -14.515 29.061  1.00 59.44  ? 374 ASP A C     1 
ATOM   2883 O  O     . ASP A 1 374 ? 12.323  -14.325 29.778  1.00 64.56  ? 374 ASP A O     1 
ATOM   2884 C  CB    . ASP A 1 374 ? 13.665  -12.029 28.842  1.00 58.12  ? 374 ASP A CB    1 
ATOM   2885 C  CG    . ASP A 1 374 ? 13.409  -11.512 30.228  1.00 69.79  ? 374 ASP A CG    1 
ATOM   2886 O  OD1   . ASP A 1 374 ? 13.740  -12.212 31.207  1.00 77.13  ? 374 ASP A OD1   1 
ATOM   2887 O  OD2   . ASP A 1 374 ? 12.872  -10.395 30.338  1.00 79.81  ? 374 ASP A OD2   1 
ATOM   2888 N  N     . GLU A 1 375 ? 13.526  -15.690 28.481  1.00 53.63  ? 375 GLU A N     1 
ATOM   2889 C  CA    . GLU A 1 375 ? 12.585  -16.800 28.588  1.00 58.24  ? 375 GLU A CA    1 
ATOM   2890 C  C     . GLU A 1 375 ? 13.321  -18.004 29.155  1.00 57.49  ? 375 GLU A C     1 
ATOM   2891 O  O     . GLU A 1 375 ? 14.347  -18.424 28.581  1.00 55.61  ? 375 GLU A O     1 
ATOM   2892 C  CB    . GLU A 1 375 ? 11.979  -17.165 27.234  1.00 61.66  ? 375 GLU A CB    1 
ATOM   2893 C  CG    . GLU A 1 375 ? 10.844  -16.295 26.764  1.00 64.04  ? 375 GLU A CG    1 
ATOM   2894 C  CD    . GLU A 1 375 ? 10.119  -16.943 25.602  1.00 67.06  ? 375 GLU A CD    1 
ATOM   2895 O  OE1   . GLU A 1 375 ? 9.656   -18.095 25.766  1.00 63.21  ? 375 GLU A OE1   1 
ATOM   2896 O  OE2   . GLU A 1 375 ? 10.032  -16.318 24.525  1.00 64.13  ? 375 GLU A OE2   1 
ATOM   2897 N  N     . PRO A 1 376 ? 12.852  -18.585 30.251  1.00 56.62  ? 376 PRO A N     1 
ATOM   2898 C  CA    . PRO A 1 376 ? 13.473  -19.815 30.750  1.00 58.82  ? 376 PRO A CA    1 
ATOM   2899 C  C     . PRO A 1 376 ? 13.150  -21.009 29.870  1.00 62.01  ? 376 PRO A C     1 
ATOM   2900 O  O     . PRO A 1 376 ? 12.081  -21.096 29.261  1.00 62.43  ? 376 PRO A O     1 
ATOM   2901 C  CB    . PRO A 1 376 ? 12.864  -19.984 32.148  1.00 61.08  ? 376 PRO A CB    1 
ATOM   2902 C  CG    . PRO A 1 376 ? 11.595  -19.189 32.114  1.00 64.33  ? 376 PRO A CG    1 
ATOM   2903 C  CD    . PRO A 1 376 ? 11.864  -18.031 31.194  1.00 58.27  ? 376 PRO A CD    1 
ATOM   2904 N  N     . LEU A 1 377 ? 14.086  -21.949 29.833  1.00 65.84  ? 377 LEU A N     1 
ATOM   2905 C  CA    . LEU A 1 377 ? 13.886  -23.214 29.143  1.00 61.44  ? 377 LEU A CA    1 
ATOM   2906 C  C     . LEU A 1 377 ? 13.431  -24.289 30.120  1.00 64.87  ? 377 LEU A C     1 
ATOM   2907 O  O     . LEU A 1 377 ? 13.685  -24.212 31.326  1.00 62.82  ? 377 LEU A O     1 
ATOM   2908 C  CB    . LEU A 1 377 ? 15.169  -23.648 28.436  1.00 57.22  ? 377 LEU A CB    1 
ATOM   2909 C  CG    . LEU A 1 377 ? 15.540  -22.662 27.321  1.00 56.96  ? 377 LEU A CG    1 
ATOM   2910 C  CD1   . LEU A 1 377 ? 16.807  -23.075 26.600  1.00 53.09  ? 377 LEU A CD1   1 
ATOM   2911 C  CD2   . LEU A 1 377 ? 14.383  -22.537 26.347  1.00 56.47  ? 377 LEU A CD2   1 
ATOM   2912 N  N     . ALA A 1 378 ? 12.735  -25.287 29.582  1.00 65.56  ? 378 ALA A N     1 
ATOM   2913 C  CA    . ALA A 1 378 ? 12.258  -26.393 30.379  1.00 64.66  ? 378 ALA A CA    1 
ATOM   2914 C  C     . ALA A 1 378 ? 13.420  -27.311 30.741  1.00 67.33  ? 378 ALA A C     1 
ATOM   2915 O  O     . ALA A 1 378 ? 14.451  -27.319 30.063  1.00 63.23  ? 378 ALA A O     1 
ATOM   2916 C  CB    . ALA A 1 378 ? 11.187  -27.170 29.615  1.00 69.84  ? 378 ALA A CB    1 
ATOM   2917 N  N     . PRO A 1 379 ? 13.277  -28.093 31.809  1.00 72.01  ? 379 PRO A N     1 
ATOM   2918 C  CA    . PRO A 1 379 ? 14.322  -29.062 32.161  1.00 68.90  ? 379 PRO A CA    1 
ATOM   2919 C  C     . PRO A 1 379 ? 14.681  -29.981 31.002  1.00 67.60  ? 379 PRO A C     1 
ATOM   2920 O  O     . PRO A 1 379 ? 13.831  -30.394 30.209  1.00 66.87  ? 379 PRO A O     1 
ATOM   2921 C  CB    . PRO A 1 379 ? 13.698  -29.837 33.326  1.00 72.18  ? 379 PRO A CB    1 
ATOM   2922 C  CG    . PRO A 1 379 ? 12.801  -28.851 33.971  1.00 72.73  ? 379 PRO A CG    1 
ATOM   2923 C  CD    . PRO A 1 379 ? 12.248  -27.991 32.861  1.00 69.88  ? 379 PRO A CD    1 
ATOM   2924 N  N     . GLY A 1 380 ? 15.966  -30.293 30.901  1.00 67.42  ? 380 GLY A N     1 
ATOM   2925 C  CA    . GLY A 1 380 ? 16.453  -31.167 29.869  1.00 66.41  ? 380 GLY A CA    1 
ATOM   2926 C  C     . GLY A 1 380 ? 16.772  -30.494 28.551  1.00 63.32  ? 380 GLY A C     1 
ATOM   2927 O  O     . GLY A 1 380 ? 17.460  -31.096 27.721  1.00 62.47  ? 380 GLY A O     1 
ATOM   2928 N  N     . VAL A 1 381 ? 16.298  -29.269 28.331  1.00 61.77  ? 381 VAL A N     1 
ATOM   2929 C  CA    . VAL A 1 381 ? 16.574  -28.566 27.084  1.00 58.92  ? 381 VAL A CA    1 
ATOM   2930 C  C     . VAL A 1 381 ? 18.002  -28.042 27.122  1.00 59.41  ? 381 VAL A C     1 
ATOM   2931 O  O     . VAL A 1 381 ? 18.415  -27.401 28.097  1.00 62.76  ? 381 VAL A O     1 
ATOM   2932 C  CB    . VAL A 1 381 ? 15.565  -27.427 26.862  1.00 60.15  ? 381 VAL A CB    1 
ATOM   2933 C  CG1   . VAL A 1 381 ? 15.959  -26.582 25.657  1.00 54.88  ? 381 VAL A CG1   1 
ATOM   2934 C  CG2   . VAL A 1 381 ? 14.169  -27.993 26.677  1.00 61.21  ? 381 VAL A CG2   1 
ATOM   2935 N  N     . THR A 1 382 ? 18.754  -28.303 26.055  1.00 57.57  ? 382 THR A N     1 
ATOM   2936 C  CA    . THR A 1 382 ? 20.146  -27.898 25.931  1.00 57.96  ? 382 THR A CA    1 
ATOM   2937 C  C     . THR A 1 382 ? 20.296  -26.896 24.789  1.00 54.07  ? 382 THR A C     1 
ATOM   2938 O  O     . THR A 1 382 ? 19.404  -26.739 23.953  1.00 54.96  ? 382 THR A O     1 
ATOM   2939 C  CB    . THR A 1 382 ? 21.053  -29.120 25.705  1.00 57.13  ? 382 THR A CB    1 
ATOM   2940 O  OG1   . THR A 1 382 ? 20.603  -29.840 24.554  1.00 57.62  ? 382 THR A OG1   1 
ATOM   2941 C  CG2   . THR A 1 382 ? 20.999  -30.051 26.911  1.00 61.75  ? 382 THR A CG2   1 
ATOM   2942 N  N     . ILE A 1 383 ? 21.438  -26.213 24.756  1.00 53.17  ? 383 ILE A N     1 
ATOM   2943 C  CA    . ILE A 1 383 ? 21.662  -25.109 23.827  1.00 54.96  ? 383 ILE A CA    1 
ATOM   2944 C  C     . ILE A 1 383 ? 22.933  -25.360 23.029  1.00 58.01  ? 383 ILE A C     1 
ATOM   2945 O  O     . ILE A 1 383 ? 23.963  -25.746 23.594  1.00 62.27  ? 383 ILE A O     1 
ATOM   2946 C  CB    . ILE A 1 383 ? 21.750  -23.756 24.569  1.00 56.02  ? 383 ILE A CB    1 
ATOM   2947 C  CG1   . ILE A 1 383 ? 20.450  -23.474 25.320  1.00 53.85  ? 383 ILE A CG1   1 
ATOM   2948 C  CG2   . ILE A 1 383 ? 22.071  -22.623 23.594  1.00 54.41  ? 383 ILE A CG2   1 
ATOM   2949 C  CD1   . ILE A 1 383 ? 20.444  -22.154 26.074  1.00 57.76  ? 383 ILE A CD1   1 
ATOM   2950 N  N     . THR A 1 384 ? 22.861  -25.133 21.714  1.00 51.34  ? 384 THR A N     1 
ATOM   2951 C  CA    . THR A 1 384 ? 24.025  -25.135 20.836  1.00 52.64  ? 384 THR A CA    1 
ATOM   2952 C  C     . THR A 1 384 ? 24.270  -23.702 20.368  1.00 55.13  ? 384 THR A C     1 
ATOM   2953 O  O     . THR A 1 384 ? 23.367  -23.064 19.812  1.00 50.94  ? 384 THR A O     1 
ATOM   2954 C  CB    . THR A 1 384 ? 23.828  -26.056 19.629  1.00 55.05  ? 384 THR A CB    1 
ATOM   2955 O  OG1   . THR A 1 384 ? 23.492  -27.383 20.062  1.00 55.45  ? 384 THR A OG1   1 
ATOM   2956 C  CG2   . THR A 1 384 ? 25.104  -26.111 18.797  1.00 55.77  ? 384 THR A CG2   1 
ATOM   2957 N  N     . SER A 1 385 ? 25.486  -23.204 20.594  1.00 54.43  ? 385 SER A N     1 
ATOM   2958 C  CA    . SER A 1 385 ? 25.834  -21.824 20.293  1.00 56.82  ? 385 SER A CA    1 
ATOM   2959 C  C     . SER A 1 385 ? 25.868  -21.586 18.783  1.00 52.37  ? 385 SER A C     1 
ATOM   2960 O  O     . SER A 1 385 ? 25.794  -22.508 17.973  1.00 52.10  ? 385 SER A O     1 
ATOM   2961 C  CB    . SER A 1 385 ? 27.193  -21.476 20.901  1.00 58.39  ? 385 SER A CB    1 
ATOM   2962 O  OG    . SER A 1 385 ? 28.223  -22.226 20.276  1.00 63.22  ? 385 SER A OG    1 
ATOM   2963 N  N     . TRP A 1 386 ? 25.999  -20.317 18.403  1.00 51.19  ? 386 TRP A N     1 
ATOM   2964 C  CA    . TRP A 1 386 ? 26.144  -19.998 16.988  1.00 49.79  ? 386 TRP A CA    1 
ATOM   2965 C  C     . TRP A 1 386 ? 27.456  -20.515 16.409  1.00 53.98  ? 386 TRP A C     1 
ATOM   2966 O  O     . TRP A 1 386 ? 27.602  -20.549 15.182  1.00 54.55  ? 386 TRP A O     1 
ATOM   2967 C  CB    . TRP A 1 386 ? 26.039  -18.489 16.777  1.00 48.37  ? 386 TRP A CB    1 
ATOM   2968 C  CG    . TRP A 1 386 ? 27.240  -17.774 17.264  1.00 50.17  ? 386 TRP A CG    1 
ATOM   2969 C  CD1   . TRP A 1 386 ? 27.599  -17.562 18.567  1.00 50.91  ? 386 TRP A CD1   1 
ATOM   2970 C  CD2   . TRP A 1 386 ? 28.266  -17.184 16.463  1.00 52.45  ? 386 TRP A CD2   1 
ATOM   2971 N  NE1   . TRP A 1 386 ? 28.785  -16.874 18.625  1.00 51.00  ? 386 TRP A NE1   1 
ATOM   2972 C  CE2   . TRP A 1 386 ? 29.214  -16.623 17.347  1.00 54.47  ? 386 TRP A CE2   1 
ATOM   2973 C  CE3   . TRP A 1 386 ? 28.478  -17.071 15.082  1.00 51.27  ? 386 TRP A CE3   1 
ATOM   2974 C  CZ2   . TRP A 1 386 ? 30.356  -15.961 16.895  1.00 52.91  ? 386 TRP A CZ2   1 
ATOM   2975 C  CZ3   . TRP A 1 386 ? 29.612  -16.408 14.636  1.00 50.46  ? 386 TRP A CZ3   1 
ATOM   2976 C  CH2   . TRP A 1 386 ? 30.535  -15.861 15.541  1.00 51.77  ? 386 TRP A CH2   1 
ATOM   2977 N  N     . LYS A 1 387 ? 28.408  -20.914 17.254  1.00 55.77  ? 387 LYS A N     1 
ATOM   2978 C  CA    . LYS A 1 387 ? 29.650  -21.527 16.803  1.00 57.83  ? 387 LYS A CA    1 
ATOM   2979 C  C     . LYS A 1 387 ? 29.511  -23.023 16.595  1.00 62.70  ? 387 LYS A C     1 
ATOM   2980 O  O     . LYS A 1 387 ? 30.522  -23.699 16.380  1.00 66.63  ? 387 LYS A O     1 
ATOM   2981 C  CB    . LYS A 1 387 ? 30.781  -21.257 17.800  1.00 63.30  ? 387 LYS A CB    1 
ATOM   2982 C  CG    . LYS A 1 387 ? 31.299  -19.825 17.826  1.00 62.46  ? 387 LYS A CG    1 
ATOM   2983 C  CD    . LYS A 1 387 ? 32.477  -19.705 18.787  1.00 71.73  ? 387 LYS A CD    1 
ATOM   2984 C  CE    . LYS A 1 387 ? 33.032  -18.295 18.838  1.00 75.38  ? 387 LYS A CE    1 
ATOM   2985 N  NZ    . LYS A 1 387 ? 32.049  -17.340 19.417  1.00 82.24  ? 387 LYS A NZ    1 
ATOM   2986 N  N     . ASN A 1 388 ? 28.286  -23.549 16.661  1.00 61.01  ? 388 ASN A N     1 
ATOM   2987 C  CA    . ASN A 1 388 ? 28.015  -24.977 16.508  1.00 64.95  ? 388 ASN A CA    1 
ATOM   2988 C  C     . ASN A 1 388 ? 28.724  -25.771 17.603  1.00 70.05  ? 388 ASN A C     1 
ATOM   2989 O  O     . ASN A 1 388 ? 29.392  -26.773 17.345  1.00 71.32  ? 388 ASN A O     1 
ATOM   2990 C  CB    . ASN A 1 388 ? 28.412  -25.474 15.115  1.00 63.13  ? 388 ASN A CB    1 
ATOM   2991 C  CG    . ASN A 1 388 ? 27.543  -26.611 14.636  1.00 65.65  ? 388 ASN A CG    1 
ATOM   2992 O  OD1   . ASN A 1 388 ? 26.349  -26.664 14.930  1.00 63.75  ? 388 ASN A OD1   1 
ATOM   2993 N  ND2   . ASN A 1 388 ? 28.138  -27.535 13.894  1.00 73.88  ? 388 ASN A ND2   1 
ATOM   2994 N  N     . LYS A 1 389 ? 28.582  -25.297 18.840  1.00 71.33  ? 389 LYS A N     1 
ATOM   2995 C  CA    . LYS A 1 389 ? 29.223  -25.905 19.995  1.00 74.69  ? 389 LYS A CA    1 
ATOM   2996 C  C     . LYS A 1 389 ? 28.216  -26.008 21.130  1.00 73.03  ? 389 LYS A C     1 
ATOM   2997 O  O     . LYS A 1 389 ? 27.292  -25.196 21.237  1.00 69.52  ? 389 LYS A O     1 
ATOM   2998 C  CB    . LYS A 1 389 ? 30.448  -25.097 20.465  1.00 77.69  ? 389 LYS A CB    1 
ATOM   2999 C  CG    . LYS A 1 389 ? 31.619  -25.089 19.487  1.00 82.63  ? 389 LYS A CG    1 
ATOM   3000 C  CD    . LYS A 1 389 ? 32.768  -24.225 19.996  1.00 87.35  ? 389 LYS A CD    1 
ATOM   3001 C  CE    . LYS A 1 389 ? 33.917  -24.185 18.995  1.00 94.27  ? 389 LYS A CE    1 
ATOM   3002 N  NZ    . LYS A 1 389 ? 34.986  -23.225 19.398  1.00 99.48  ? 389 LYS A NZ    1 
ATOM   3003 N  N     . GLU A 1 390 ? 28.399  -27.026 21.967  1.00 75.64  ? 390 GLU A N     1 
ATOM   3004 C  CA    . GLU A 1 390 ? 27.639  -27.121 23.205  1.00 77.81  ? 390 GLU A CA    1 
ATOM   3005 C  C     . GLU A 1 390 ? 27.931  -25.911 24.079  1.00 74.31  ? 390 GLU A C     1 
ATOM   3006 O  O     . GLU A 1 390 ? 29.093  -25.544 24.281  1.00 77.03  ? 390 GLU A O     1 
ATOM   3007 C  CB    . GLU A 1 390 ? 27.990  -28.413 23.940  1.00 83.25  ? 390 GLU A CB    1 
ATOM   3008 C  CG    . GLU A 1 390 ? 27.079  -29.576 23.611  1.00 90.35  ? 390 GLU A CG    1 
ATOM   3009 C  CD    . GLU A 1 390 ? 25.806  -29.567 24.440  1.00 93.52  ? 390 GLU A CD    1 
ATOM   3010 O  OE1   . GLU A 1 390 ? 25.520  -28.534 25.082  1.00 86.20  ? 390 GLU A OE1   1 
ATOM   3011 O  OE2   . GLU A 1 390 ? 25.096  -30.597 24.460  1.00 94.73  ? 390 GLU A OE2   1 
ATOM   3012 N  N     . TRP A 1 391 ? 26.876  -25.283 24.593  1.00 73.62  ? 391 TRP A N     1 
ATOM   3013 C  CA    . TRP A 1 391 ? 27.000  -24.004 25.279  1.00 78.67  ? 391 TRP A CA    1 
ATOM   3014 C  C     . TRP A 1 391 ? 26.241  -24.029 26.596  1.00 81.86  ? 391 TRP A C     1 
ATOM   3015 O  O     . TRP A 1 391 ? 25.044  -24.332 26.623  1.00 74.81  ? 391 TRP A O     1 
ATOM   3016 C  CB    . TRP A 1 391 ? 26.477  -22.864 24.403  1.00 73.86  ? 391 TRP A CB    1 
ATOM   3017 C  CG    . TRP A 1 391 ? 26.592  -21.521 25.039  1.00 73.12  ? 391 TRP A CG    1 
ATOM   3018 C  CD1   . TRP A 1 391 ? 27.646  -20.660 24.950  1.00 75.64  ? 391 TRP A CD1   1 
ATOM   3019 C  CD2   . TRP A 1 391 ? 25.614  -20.876 25.864  1.00 74.71  ? 391 TRP A CD2   1 
ATOM   3020 N  NE1   . TRP A 1 391 ? 27.385  -19.518 25.667  1.00 75.34  ? 391 TRP A NE1   1 
ATOM   3021 C  CE2   . TRP A 1 391 ? 26.144  -19.625 26.237  1.00 74.65  ? 391 TRP A CE2   1 
ATOM   3022 C  CE3   . TRP A 1 391 ? 24.342  -21.234 26.320  1.00 74.47  ? 391 TRP A CE3   1 
ATOM   3023 C  CZ2   . TRP A 1 391 ? 25.445  -18.729 27.048  1.00 75.59  ? 391 TRP A CZ2   1 
ATOM   3024 C  CZ3   . TRP A 1 391 ? 23.650  -20.345 27.126  1.00 77.66  ? 391 TRP A CZ3   1 
ATOM   3025 C  CH2   . TRP A 1 391 ? 24.202  -19.106 27.478  1.00 79.27  ? 391 TRP A CH2   1 
ATOM   3026 N  N     . ARG A 1 392 ? 26.933  -23.686 27.678  1.00 85.19  ? 392 ARG A N     1 
ATOM   3027 C  CA    . ARG A 1 392 ? 26.306  -23.581 28.982  1.00 91.94  ? 392 ARG A CA    1 
ATOM   3028 C  C     . ARG A 1 392 ? 26.205  -22.120 29.407  1.00 95.96  ? 392 ARG A C     1 
ATOM   3029 O  O     . ARG A 1 392 ? 27.081  -21.311 29.085  1.00 95.63  ? 392 ARG A O     1 
ATOM   3030 C  CB    . ARG A 1 392 ? 27.089  -24.362 30.043  1.00 96.44  ? 392 ARG A CB    1 
ATOM   3031 C  CG    . ARG A 1 392 ? 27.220  -25.843 29.748  1.00 98.15  ? 392 ARG A CG    1 
ATOM   3032 C  CD    . ARG A 1 392 ? 27.846  -26.563 30.922  1.00 101.72 ? 392 ARG A CD    1 
ATOM   3033 N  NE    . ARG A 1 392 ? 27.961  -27.996 30.689  1.00 109.28 ? 392 ARG A NE    1 
ATOM   3034 C  CZ    . ARG A 1 392 ? 28.439  -28.858 31.576  1.00 112.66 ? 392 ARG A CZ    1 
ATOM   3035 N  NH1   . ARG A 1 392 ? 28.850  -28.462 32.770  1.00 112.73 ? 392 ARG A NH1   1 
ATOM   3036 N  NH2   . ARG A 1 392 ? 28.505  -30.148 31.258  1.00 113.31 ? 392 ARG A NH2   1 
ATOM   3037 N  N     . PRO A 1 393 ? 25.149  -21.751 30.142  1.00 99.98  ? 393 PRO A N     1 
ATOM   3038 C  CA    . PRO A 1 393 ? 24.963  -20.342 30.523  1.00 102.13 ? 393 PRO A CA    1 
ATOM   3039 C  C     . PRO A 1 393 ? 25.996  -19.811 31.507  1.00 110.60 ? 393 PRO A C     1 
ATOM   3040 O  O     . PRO A 1 393 ? 25.792  -18.741 32.089  1.00 115.85 ? 393 PRO A O     1 
ATOM   3041 C  CB    . PRO A 1 393 ? 23.558  -20.331 31.144  1.00 101.43 ? 393 PRO A CB    1 
ATOM   3042 C  CG    . PRO A 1 393 ? 22.876  -21.540 30.579  1.00 100.42 ? 393 PRO A CG    1 
ATOM   3043 C  CD    . PRO A 1 393 ? 23.962  -22.568 30.450  1.00 97.68  ? 393 PRO A CD    1 
ATOM   3044 N  N     . GLN A 1 394 ? 27.103  -20.522 31.702  1.00 117.76 ? 394 GLN A N     1 
ATOM   3045 C  CA    . GLN A 1 394 ? 28.152  -20.085 32.614  1.00 127.56 ? 394 GLN A CA    1 
ATOM   3046 C  C     . GLN A 1 394 ? 29.521  -20.160 31.948  1.00 128.38 ? 394 GLN A C     1 
ATOM   3047 O  O     . GLN A 1 394 ? 30.523  -20.522 32.572  1.00 133.84 ? 394 GLN A O     1 
ATOM   3048 C  CB    . GLN A 1 394 ? 28.118  -20.892 33.911  1.00 135.48 ? 394 GLN A CB    1 
ATOM   3049 C  CG    . GLN A 1 394 ? 26.918  -20.559 34.797  1.00 139.32 ? 394 GLN A CG    1 
ATOM   3050 C  CD    . GLN A 1 394 ? 26.981  -21.215 36.164  1.00 148.98 ? 394 GLN A CD    1 
ATOM   3051 O  OE1   . GLN A 1 394 ? 27.505  -22.319 36.315  1.00 155.66 ? 394 GLN A OE1   1 
ATOM   3052 N  NE2   . GLN A 1 394 ? 26.447  -20.531 37.170  1.00 150.60 ? 394 GLN A NE2   1 
ATOM   3053 N  N     . ASP A 1 395 ? 29.581  -19.815 30.667  1.00 128.47 ? 395 ASP A N     1 
ATOM   3054 C  CA    . ASP A 1 395 ? 30.834  -19.607 29.961  1.00 132.75 ? 395 ASP A CA    1 
ATOM   3055 C  C     . ASP A 1 395 ? 31.095  -18.101 29.861  1.00 139.74 ? 395 ASP A C     1 
ATOM   3056 O  O     . ASP A 1 395 ? 30.511  -17.304 30.604  1.00 140.14 ? 395 ASP A O     1 
ATOM   3057 C  CB    . ASP A 1 395 ? 30.775  -20.283 28.585  1.00 122.04 ? 395 ASP A CB    1 
ATOM   3058 C  CG    . ASP A 1 395 ? 30.445  -21.758 28.673  1.00 116.15 ? 395 ASP A CG    1 
ATOM   3059 O  OD1   . ASP A 1 395 ? 30.419  -22.297 29.799  1.00 119.96 ? 395 ASP A OD1   1 
ATOM   3060 O  OD2   . ASP A 1 395 ? 30.208  -22.379 27.614  1.00 106.52 ? 395 ASP A OD2   1 
ATOM   3061 N  N     . GLU A 1 396 ? 31.973  -17.701 28.944  1.00 154.19 ? 396 GLU A N     1 
ATOM   3062 C  CA    . GLU A 1 396 ? 32.159  -16.291 28.630  1.00 156.43 ? 396 GLU A CA    1 
ATOM   3063 C  C     . GLU A 1 396 ? 31.655  -15.916 27.247  1.00 153.98 ? 396 GLU A C     1 
ATOM   3064 O  O     . GLU A 1 396 ? 31.212  -14.782 27.051  1.00 153.49 ? 396 GLU A O     1 
ATOM   3065 C  CB    . GLU A 1 396 ? 33.640  -15.902 28.746  1.00 160.72 ? 396 GLU A CB    1 
ATOM   3066 C  CG    . GLU A 1 396 ? 33.884  -14.396 28.801  1.00 160.88 ? 396 GLU A CG    1 
ATOM   3067 C  CD    . GLU A 1 396 ? 35.359  -14.034 28.756  1.00 156.30 ? 396 GLU A CD    1 
ATOM   3068 O  OE1   . GLU A 1 396 ? 36.177  -14.903 28.388  1.00 157.13 ? 396 GLU A OE1   1 
ATOM   3069 O  OE2   . GLU A 1 396 ? 35.700  -12.879 29.091  1.00 156.08 ? 396 GLU A OE2   1 
ATOM   3070 N  N     . GLU A 1 397 ? 31.707  -16.838 26.292  1.00 125.00 ? 397 GLU A N     1 
ATOM   3071 C  CA    . GLU A 1 397 ? 31.154  -16.579 24.969  1.00 104.70 ? 397 GLU A CA    1 
ATOM   3072 C  C     . GLU A 1 397 ? 29.636  -16.476 25.060  1.00 89.84  ? 397 GLU A C     1 
ATOM   3073 O  O     . GLU A 1 397 ? 29.001  -17.327 25.692  1.00 89.55  ? 397 GLU A O     1 
ATOM   3074 C  CB    . GLU A 1 397 ? 31.538  -17.693 23.992  1.00 104.09 ? 397 GLU A CB    1 
ATOM   3075 C  CG    . GLU A 1 397 ? 33.021  -17.781 23.654  1.00 112.67 ? 397 GLU A CG    1 
ATOM   3076 C  CD    . GLU A 1 397 ? 33.458  -16.764 22.608  1.00 114.46 ? 397 GLU A CD    1 
ATOM   3077 O  OE1   . GLU A 1 397 ? 32.609  -15.974 22.141  1.00 109.66 ? 397 GLU A OE1   1 
ATOM   3078 O  OE2   . GLU A 1 397 ? 34.656  -16.760 22.248  1.00 119.60 ? 397 GLU A OE2   1 
ATOM   3079 N  N     . PRO A 1 398 ? 29.020  -15.461 24.458  1.00 80.89  ? 398 PRO A N     1 
ATOM   3080 C  CA    . PRO A 1 398 ? 27.562  -15.474 24.315  1.00 68.87  ? 398 PRO A CA    1 
ATOM   3081 C  C     . PRO A 1 398 ? 27.140  -16.603 23.390  1.00 63.91  ? 398 PRO A C     1 
ATOM   3082 O  O     . PRO A 1 398 ? 27.932  -17.119 22.599  1.00 61.74  ? 398 PRO A O     1 
ATOM   3083 C  CB    . PRO A 1 398 ? 27.253  -14.108 23.704  1.00 63.22  ? 398 PRO A CB    1 
ATOM   3084 C  CG    . PRO A 1 398 ? 28.503  -13.771 22.948  1.00 68.14  ? 398 PRO A CG    1 
ATOM   3085 C  CD    . PRO A 1 398 ? 29.628  -14.298 23.791  1.00 77.31  ? 398 PRO A CD    1 
ATOM   3086 N  N     . CYS A 1 399 ? 25.870  -16.994 23.495  1.00 57.85  ? 399 CYS A N     1 
ATOM   3087 C  CA    . CYS A 1 399 ? 25.388  -18.088 22.661  1.00 57.85  ? 399 CYS A CA    1 
ATOM   3088 C  C     . CYS A 1 399 ? 24.981  -17.618 21.270  1.00 51.90  ? 399 CYS A C     1 
ATOM   3089 O  O     . CYS A 1 399 ? 24.993  -18.423 20.334  1.00 50.32  ? 399 CYS A O     1 
ATOM   3090 C  CB    . CYS A 1 399 ? 24.221  -18.823 23.346  1.00 56.18  ? 399 CYS A CB    1 
ATOM   3091 S  SG    . CYS A 1 399 ? 22.663  -17.894 23.538  1.00 55.26  ? 399 CYS A SG    1 
ATOM   3092 N  N     . ALA A 1 400 ? 24.643  -16.339 21.109  1.00 49.51  ? 400 ALA A N     1 
ATOM   3093 C  CA    . ALA A 1 400 ? 24.304  -15.775 19.811  1.00 48.22  ? 400 ALA A CA    1 
ATOM   3094 C  C     . ALA A 1 400 ? 25.249  -14.628 19.488  1.00 49.60  ? 400 ALA A C     1 
ATOM   3095 O  O     . ALA A 1 400 ? 25.632  -13.853 20.374  1.00 45.62  ? 400 ALA A O     1 
ATOM   3096 C  CB    . ALA A 1 400 ? 22.855  -15.271 19.772  1.00 44.71  ? 400 ALA A CB    1 
ATOM   3097 N  N     . HIS A 1 401 ? 25.619  -14.512 18.221  1.00 45.64  ? 401 HIS A N     1 
ATOM   3098 C  CA    . HIS A 1 401 ? 26.503  -13.425 17.843  1.00 42.78  ? 401 HIS A CA    1 
ATOM   3099 C  C     . HIS A 1 401 ? 25.828  -12.088 18.138  1.00 42.47  ? 401 HIS A C     1 
ATOM   3100 O  O     . HIS A 1 401 ? 24.605  -11.966 17.989  1.00 42.54  ? 401 HIS A O     1 
ATOM   3101 C  CB    . HIS A 1 401 ? 26.877  -13.523 16.368  1.00 43.60  ? 401 HIS A CB    1 
ATOM   3102 C  CG    . HIS A 1 401 ? 27.958  -12.571 15.972  1.00 44.27  ? 401 HIS A CG    1 
ATOM   3103 N  ND1   . HIS A 1 401 ? 27.705  -11.262 15.631  1.00 41.31  ? 401 HIS A ND1   1 
ATOM   3104 C  CD2   . HIS A 1 401 ? 29.301  -12.727 15.903  1.00 45.38  ? 401 HIS A CD2   1 
ATOM   3105 C  CE1   . HIS A 1 401 ? 28.844  -10.656 15.347  1.00 42.55  ? 401 HIS A CE1   1 
ATOM   3106 N  NE2   . HIS A 1 401 ? 29.828  -11.522 15.507  1.00 40.17  ? 401 HIS A NE2   1 
ATOM   3107 N  N     . PRO A 1 402 ? 26.577  -11.079 18.597  1.00 41.47  ? 402 PRO A N     1 
ATOM   3108 C  CA    . PRO A 1 402 ? 25.949  -9.786  18.915  1.00 41.66  ? 402 PRO A CA    1 
ATOM   3109 C  C     . PRO A 1 402 ? 25.220  -9.136  17.748  1.00 40.32  ? 402 PRO A C     1 
ATOM   3110 O  O     . PRO A 1 402 ? 24.310  -8.328  17.981  1.00 40.34  ? 402 PRO A O     1 
ATOM   3111 C  CB    . PRO A 1 402 ? 27.135  -8.932  19.381  1.00 41.45  ? 402 PRO A CB    1 
ATOM   3112 C  CG    . PRO A 1 402 ? 28.087  -9.941  19.960  1.00 41.85  ? 402 PRO A CG    1 
ATOM   3113 C  CD    . PRO A 1 402 ? 27.969  -11.148 19.076  1.00 41.76  ? 402 PRO A CD    1 
ATOM   3114 N  N     . ASN A 1 403 ? 25.582  -9.448  16.507  1.00 40.28  ? 403 ASN A N     1 
ATOM   3115 C  CA    . ASN A 1 403 ? 24.908  -8.882  15.342  1.00 37.14  ? 403 ASN A CA    1 
ATOM   3116 C  C     . ASN A 1 403 ? 24.134  -9.963  14.593  1.00 41.06  ? 403 ASN A C     1 
ATOM   3117 O  O     . ASN A 1 403 ? 23.947  -9.869  13.377  1.00 34.05  ? 403 ASN A O     1 
ATOM   3118 C  CB    . ASN A 1 403 ? 25.912  -8.181  14.417  1.00 40.34  ? 403 ASN A CB    1 
ATOM   3119 C  CG    . ASN A 1 403 ? 25.237  -7.400  13.267  1.00 41.90  ? 403 ASN A CG    1 
ATOM   3120 O  OD1   . ASN A 1 403 ? 24.301  -6.621  13.484  1.00 42.77  ? 403 ASN A OD1   1 
ATOM   3121 N  ND2   . ASN A 1 403 ? 25.712  -7.621  12.042  1.00 41.83  ? 403 ASN A ND2   1 
ATOM   3122 N  N     . SER A 1 404 ? 23.700  -11.014 15.306  1.00 33.20  ? 404 SER A N     1 
ATOM   3123 C  CA    . SER A 1 404 ? 22.861  -12.020 14.679  1.00 35.26  ? 404 SER A CA    1 
ATOM   3124 C  C     . SER A 1 404 ? 21.512  -11.405 14.330  1.00 34.85  ? 404 SER A C     1 
ATOM   3125 O  O     . SER A 1 404 ? 21.091  -10.391 14.902  1.00 34.30  ? 404 SER A O     1 
ATOM   3126 C  CB    . SER A 1 404 ? 22.686  -13.241 15.598  1.00 37.10  ? 404 SER A CB    1 
ATOM   3127 O  OG    . SER A 1 404 ? 22.223  -12.840 16.880  1.00 34.49  ? 404 SER A OG    1 
ATOM   3128 N  N     . ARG A 1 405 ? 20.832  -12.009 13.365  1.00 34.92  ? 405 ARG A N     1 
ATOM   3129 C  CA    . ARG A 1 405 ? 19.697  -11.334 12.755  1.00 34.61  ? 405 ARG A CA    1 
ATOM   3130 C  C     . ARG A 1 405 ? 18.576  -12.324 12.505  1.00 34.42  ? 405 ARG A C     1 
ATOM   3131 O  O     . ARG A 1 405 ? 18.808  -13.513 12.290  1.00 33.03  ? 405 ARG A O     1 
ATOM   3132 C  CB    . ARG A 1 405 ? 20.084  -10.658 11.412  1.00 33.12  ? 405 ARG A CB    1 
ATOM   3133 C  CG    . ARG A 1 405 ? 21.164  -9.564  11.500  1.00 34.80  ? 405 ARG A CG    1 
ATOM   3134 C  CD    . ARG A 1 405 ? 20.561  -8.161  11.518  1.00 35.23  ? 405 ARG A CD    1 
ATOM   3135 N  NE    . ARG A 1 405 ? 21.557  -7.118  11.751  1.00 33.88  ? 405 ARG A NE    1 
ATOM   3136 C  CZ    . ARG A 1 405 ? 21.272  -5.825  11.846  1.00 36.14  ? 405 ARG A CZ    1 
ATOM   3137 N  NH1   . ARG A 1 405 ? 20.055  -5.365  11.615  1.00 34.33  ? 405 ARG A NH1   1 
ATOM   3138 N  NH2   . ARG A 1 405 ? 22.231  -4.973  12.189  1.00 34.10  ? 405 ARG A NH2   1 
ATOM   3139 N  N     . PHE A 1 406 ? 17.354  -11.824 12.516  1.00 33.67  ? 406 PHE A N     1 
ATOM   3140 C  CA    . PHE A 1 406 ? 16.270  -12.561 11.897  1.00 33.67  ? 406 PHE A CA    1 
ATOM   3141 C  C     . PHE A 1 406 ? 15.925  -11.867 10.594  1.00 34.48  ? 406 PHE A C     1 
ATOM   3142 O  O     . PHE A 1 406 ? 16.168  -10.667 10.418  1.00 35.53  ? 406 PHE A O     1 
ATOM   3143 C  CB    . PHE A 1 406 ? 15.034  -12.657 12.806  1.00 31.27  ? 406 PHE A CB    1 
ATOM   3144 C  CG    . PHE A 1 406 ? 14.570  -11.325 13.351  1.00 31.52  ? 406 PHE A CG    1 
ATOM   3145 C  CD1   . PHE A 1 406 ? 13.814  -10.456 12.571  1.00 34.94  ? 406 PHE A CD1   1 
ATOM   3146 C  CD2   . PHE A 1 406 ? 14.873  -10.952 14.646  1.00 34.60  ? 406 PHE A CD2   1 
ATOM   3147 C  CE1   . PHE A 1 406 ? 13.388  -9.204  13.072  1.00 35.48  ? 406 PHE A CE1   1 
ATOM   3148 C  CE2   . PHE A 1 406 ? 14.442  -9.723  15.163  1.00 37.53  ? 406 PHE A CE2   1 
ATOM   3149 C  CZ    . PHE A 1 406 ? 13.699  -8.848  14.377  1.00 34.51  ? 406 PHE A CZ    1 
ATOM   3150 N  N     . CYS A 1 407 ? 15.371  -12.640 9.675   1.00 32.00  ? 407 CYS A N     1 
ATOM   3151 C  CA    . CYS A 1 407 ? 14.975  -12.131 8.369   1.00 31.28  ? 407 CYS A CA    1 
ATOM   3152 C  C     . CYS A 1 407 ? 13.538  -12.586 8.169   1.00 33.80  ? 407 CYS A C     1 
ATOM   3153 O  O     . CYS A 1 407 ? 13.284  -13.784 8.021   1.00 34.95  ? 407 CYS A O     1 
ATOM   3154 C  CB    . CYS A 1 407 ? 15.903  -12.672 7.276   1.00 37.59  ? 407 CYS A CB    1 
ATOM   3155 S  SG    . CYS A 1 407 ? 15.600  -12.021 5.643   1.00 34.62  ? 407 CYS A SG    1 
ATOM   3156 N  N     . THR A 1 408 ? 12.596  -11.650 8.199   1.00 34.99  ? 408 THR A N     1 
ATOM   3157 C  CA    . THR A 1 408 ? 11.204  -12.025 8.356   1.00 31.26  ? 408 THR A CA    1 
ATOM   3158 C  C     . THR A 1 408 ? 10.304  -11.168 7.474   1.00 35.05  ? 408 THR A C     1 
ATOM   3159 O  O     . THR A 1 408 ? 10.575  -9.980  7.275   1.00 35.34  ? 408 THR A O     1 
ATOM   3160 C  CB    . THR A 1 408 ? 10.794  -11.909 9.841   1.00 35.10  ? 408 THR A CB    1 
ATOM   3161 O  OG1   . THR A 1 408 ? 9.577   -12.616 10.059  1.00 37.30  ? 408 THR A OG1   1 
ATOM   3162 C  CG2   . THR A 1 408 ? 10.645  -10.435 10.312  1.00 33.40  ? 408 THR A CG2   1 
ATOM   3163 N  N     . PRO A 1 409 ? 9.228   -11.740 6.931   1.00 35.69  ? 409 PRO A N     1 
ATOM   3164 C  CA    . PRO A 1 409 ? 8.327   -10.948 6.076   1.00 36.63  ? 409 PRO A CA    1 
ATOM   3165 C  C     . PRO A 1 409 ? 7.590   -9.847  6.845   1.00 39.23  ? 409 PRO A C     1 
ATOM   3166 O  O     . PRO A 1 409 ? 7.051   -10.065 7.935   1.00 37.77  ? 409 PRO A O     1 
ATOM   3167 C  CB    . PRO A 1 409 ? 7.345   -11.993 5.530   1.00 38.84  ? 409 PRO A CB    1 
ATOM   3168 C  CG    . PRO A 1 409 ? 8.071   -13.314 5.664   1.00 41.50  ? 409 PRO A CG    1 
ATOM   3169 C  CD    . PRO A 1 409 ? 8.902   -13.173 6.915   1.00 38.62  ? 409 PRO A CD    1 
ATOM   3170 N  N     . ALA A 1 410 ? 7.527   -8.663  6.236   1.00 35.86  ? 410 ALA A N     1 
ATOM   3171 C  CA    . ALA A 1 410 ? 6.861   -7.539  6.895   1.00 39.78  ? 410 ALA A CA    1 
ATOM   3172 C  C     . ALA A 1 410 ? 5.360   -7.747  6.992   1.00 41.79  ? 410 ALA A C     1 
ATOM   3173 O  O     . ALA A 1 410 ? 4.740   -7.298  7.964   1.00 42.70  ? 410 ALA A O     1 
ATOM   3174 C  CB    . ALA A 1 410 ? 7.145   -6.224  6.164   1.00 37.28  ? 410 ALA A CB    1 
ATOM   3175 N  N     . SER A 1 411 ? 4.757   -8.424  6.013   1.00 43.29  ? 411 SER A N     1 
ATOM   3176 C  CA    . SER A 1 411 ? 3.309   -8.603  6.030   1.00 43.73  ? 411 SER A CA    1 
ATOM   3177 C  C     . SER A 1 411 ? 2.841   -9.428  7.227   1.00 48.39  ? 411 SER A C     1 
ATOM   3178 O  O     . SER A 1 411 ? 1.654   -9.378  7.574   1.00 48.09  ? 411 SER A O     1 
ATOM   3179 C  CB    . SER A 1 411 ? 2.844   -9.251  4.721   1.00 47.93  ? 411 SER A CB    1 
ATOM   3180 O  OG    . SER A 1 411 ? 3.415   -10.541 4.552   1.00 45.94  ? 411 SER A OG    1 
ATOM   3181 N  N     . GLN A 1 412 ? 3.750   -10.152 7.887   1.00 45.56  ? 412 GLN A N     1 
ATOM   3182 C  CA    . GLN A 1 412 ? 3.406   -10.960 9.052   1.00 47.36  ? 412 GLN A CA    1 
ATOM   3183 C  C     . GLN A 1 412 ? 3.358   -10.171 10.353  1.00 46.28  ? 412 GLN A C     1 
ATOM   3184 O  O     . GLN A 1 412 ? 2.880   -10.708 11.355  1.00 49.48  ? 412 GLN A O     1 
ATOM   3185 C  CB    . GLN A 1 412 ? 4.408   -12.106 9.205   1.00 44.15  ? 412 GLN A CB    1 
ATOM   3186 C  CG    . GLN A 1 412 ? 4.197   -13.194 8.193   1.00 47.84  ? 412 GLN A CG    1 
ATOM   3187 C  CD    . GLN A 1 412 ? 5.204   -14.314 8.322   1.00 43.61  ? 412 GLN A CD    1 
ATOM   3188 O  OE1   . GLN A 1 412 ? 5.144   -15.296 7.584   1.00 48.07  ? 412 GLN A OE1   1 
ATOM   3189 N  NE2   . GLN A 1 412 ? 6.140   -14.173 9.254   1.00 43.18  ? 412 GLN A NE2   1 
ATOM   3190 N  N     . CYS A 1 413 ? 3.851   -8.941  10.372  1.00 48.18  ? 413 CYS A N     1 
ATOM   3191 C  CA    . CYS A 1 413 ? 3.872   -8.160  11.605  1.00 44.46  ? 413 CYS A CA    1 
ATOM   3192 C  C     . CYS A 1 413 ? 2.446   -7.844  12.034  1.00 46.20  ? 413 CYS A C     1 
ATOM   3193 O  O     . CYS A 1 413 ? 1.655   -7.370  11.211  1.00 44.93  ? 413 CYS A O     1 
ATOM   3194 C  CB    . CYS A 1 413 ? 4.666   -6.863  11.395  1.00 40.11  ? 413 CYS A CB    1 
ATOM   3195 S  SG    . CYS A 1 413 ? 4.918   -5.913  12.902  1.00 43.89  ? 413 CYS A SG    1 
ATOM   3196 N  N     . PRO A 1 414 ? 2.079   -8.093  13.298  1.00 47.37  ? 414 PRO A N     1 
ATOM   3197 C  CA    . PRO A 1 414 ? 0.687   -7.863  13.726  1.00 45.66  ? 414 PRO A CA    1 
ATOM   3198 C  C     . PRO A 1 414 ? 0.236   -6.416  13.635  1.00 47.41  ? 414 PRO A C     1 
ATOM   3199 O  O     . PRO A 1 414 ? -0.976  -6.164  13.572  1.00 46.96  ? 414 PRO A O     1 
ATOM   3200 C  CB    . PRO A 1 414 ? 0.677   -8.340  15.188  1.00 46.52  ? 414 PRO A CB    1 
ATOM   3201 C  CG    . PRO A 1 414 ? 1.926   -9.119  15.371  1.00 50.71  ? 414 PRO A CG    1 
ATOM   3202 C  CD    . PRO A 1 414 ? 2.921   -8.606  14.391  1.00 46.21  ? 414 PRO A CD    1 
ATOM   3203 N  N     . ILE A 1 415 ? 1.161   -5.461  13.653  1.00 42.71  ? 415 ILE A N     1 
ATOM   3204 C  CA    . ILE A 1 415 ? 0.848   -4.041  13.637  1.00 43.06  ? 415 ILE A CA    1 
ATOM   3205 C  C     . ILE A 1 415 ? 1.343   -3.376  12.351  1.00 43.88  ? 415 ILE A C     1 
ATOM   3206 O  O     . ILE A 1 415 ? 1.594   -2.186  12.338  1.00 41.98  ? 415 ILE A O     1 
ATOM   3207 C  CB    . ILE A 1 415 ? 1.434   -3.338  14.876  1.00 45.43  ? 415 ILE A CB    1 
ATOM   3208 C  CG1   . ILE A 1 415 ? 2.944   -3.596  14.939  1.00 46.88  ? 415 ILE A CG1   1 
ATOM   3209 C  CG2   . ILE A 1 415 ? 0.702   -3.772  16.166  1.00 45.36  ? 415 ILE A CG2   1 
ATOM   3210 C  CD1   . ILE A 1 415 ? 3.636   -2.912  16.080  1.00 51.06  ? 415 ILE A CD1   1 
ATOM   3211 N  N     . ILE A 1 416 ? 1.512   -4.145  11.271  1.00 41.74  ? 416 ILE A N     1 
ATOM   3212 C  CA    . ILE A 1 416 ? 1.918   -3.544  10.005  1.00 42.65  ? 416 ILE A CA    1 
ATOM   3213 C  C     . ILE A 1 416 ? 0.876   -2.501  9.607   1.00 47.13  ? 416 ILE A C     1 
ATOM   3214 O  O     . ILE A 1 416 ? -0.334  -2.728  9.731   1.00 46.34  ? 416 ILE A O     1 
ATOM   3215 C  CB    . ILE A 1 416 ? 2.117   -4.635  8.938   1.00 41.72  ? 416 ILE A CB    1 
ATOM   3216 C  CG1   . ILE A 1 416 ? 2.976   -4.111  7.788   1.00 45.57  ? 416 ILE A CG1   1 
ATOM   3217 C  CG2   . ILE A 1 416 ? 0.783   -5.198  8.442   1.00 45.81  ? 416 ILE A CG2   1 
ATOM   3218 C  CD1   . ILE A 1 416 ? 4.429   -3.848  8.197   1.00 41.61  ? 416 ILE A CD1   1 
ATOM   3219 N  N     . ASP A 1 417 ? 1.344   -1.326  9.185   1.00 45.28  ? 417 ASP A N     1 
ATOM   3220 C  CA    . ASP A 1 417 ? 0.433   -0.218  8.920   1.00 47.14  ? 417 ASP A CA    1 
ATOM   3221 C  C     . ASP A 1 417 ? -0.396  -0.493  7.667   1.00 47.15  ? 417 ASP A C     1 
ATOM   3222 O  O     . ASP A 1 417 ? 0.125   -1.015  6.678   1.00 47.98  ? 417 ASP A O     1 
ATOM   3223 C  CB    . ASP A 1 417 ? 1.206   1.091   8.750   1.00 44.64  ? 417 ASP A CB    1 
ATOM   3224 C  CG    . ASP A 1 417 ? 0.296   2.314   8.779   1.00 48.10  ? 417 ASP A CG    1 
ATOM   3225 O  OD1   . ASP A 1 417 ? -0.244  2.688   7.716   1.00 48.90  ? 417 ASP A OD1   1 
ATOM   3226 O  OD2   . ASP A 1 417 ? 0.101   2.888   9.870   1.00 47.73  ? 417 ASP A OD2   1 
ATOM   3227 N  N     . PRO A 1 418 ? -1.686  -0.156  7.677   1.00 48.05  ? 418 PRO A N     1 
ATOM   3228 C  CA    . PRO A 1 418 ? -2.525  -0.443  6.500   1.00 50.73  ? 418 PRO A CA    1 
ATOM   3229 C  C     . PRO A 1 418 ? -2.057  0.243   5.226   1.00 51.61  ? 418 PRO A C     1 
ATOM   3230 O  O     . PRO A 1 418 ? -2.380  -0.236  4.133   1.00 56.32  ? 418 PRO A O     1 
ATOM   3231 C  CB    . PRO A 1 418 ? -3.924  0.037   6.925   1.00 50.07  ? 418 PRO A CB    1 
ATOM   3232 C  CG    . PRO A 1 418 ? -3.765  0.698   8.239   1.00 51.35  ? 418 PRO A CG    1 
ATOM   3233 C  CD    . PRO A 1 418 ? -2.476  0.264   8.845   1.00 49.73  ? 418 PRO A CD    1 
ATOM   3234 N  N     . ALA A 1 419 ? -1.294  1.328   5.322   1.00 47.40  ? 419 ALA A N     1 
ATOM   3235 C  CA    . ALA A 1 419 ? -0.777  2.012   4.146   1.00 51.25  ? 419 ALA A CA    1 
ATOM   3236 C  C     . ALA A 1 419 ? 0.648   1.605   3.784   1.00 50.47  ? 419 ALA A C     1 
ATOM   3237 O  O     . ALA A 1 419 ? 1.273   2.297   2.975   1.00 54.52  ? 419 ALA A O     1 
ATOM   3238 C  CB    . ALA A 1 419 ? -0.824  3.529   4.350   1.00 46.22  ? 419 ALA A CB    1 
ATOM   3239 N  N     . TRP A 1 420 ? 1.175   0.506   4.344   1.00 47.29  ? 420 TRP A N     1 
ATOM   3240 C  CA    . TRP A 1 420 ? 2.598   0.216   4.165   1.00 47.87  ? 420 TRP A CA    1 
ATOM   3241 C  C     . TRP A 1 420 ? 2.959   -0.149  2.726   1.00 49.10  ? 420 TRP A C     1 
ATOM   3242 O  O     . TRP A 1 420 ? 4.129   -0.024  2.351   1.00 42.62  ? 420 TRP A O     1 
ATOM   3243 C  CB    . TRP A 1 420 ? 3.056   -0.893  5.128   1.00 44.39  ? 420 TRP A CB    1 
ATOM   3244 C  CG    . TRP A 1 420 ? 2.830   -2.314  4.656   1.00 46.96  ? 420 TRP A CG    1 
ATOM   3245 C  CD1   . TRP A 1 420 ? 1.678   -3.039  4.761   1.00 46.76  ? 420 TRP A CD1   1 
ATOM   3246 C  CD2   . TRP A 1 420 ? 3.802   -3.186  4.044   1.00 45.38  ? 420 TRP A CD2   1 
ATOM   3247 N  NE1   . TRP A 1 420 ? 1.864   -4.300  4.235   1.00 47.24  ? 420 TRP A NE1   1 
ATOM   3248 C  CE2   . TRP A 1 420 ? 3.159   -4.414  3.791   1.00 46.27  ? 420 TRP A CE2   1 
ATOM   3249 C  CE3   . TRP A 1 420 ? 5.150   -3.037  3.677   1.00 46.49  ? 420 TRP A CE3   1 
ATOM   3250 C  CZ2   . TRP A 1 420 ? 3.815   -5.493  3.179   1.00 45.12  ? 420 TRP A CZ2   1 
ATOM   3251 C  CZ3   . TRP A 1 420 ? 5.805   -4.109  3.072   1.00 43.06  ? 420 TRP A CZ3   1 
ATOM   3252 C  CH2   . TRP A 1 420 ? 5.135   -5.321  2.829   1.00 43.96  ? 420 TRP A CH2   1 
ATOM   3253 N  N     . GLU A 1 421 ? 1.995   -0.578  1.906   1.00 45.93  ? 421 GLU A N     1 
ATOM   3254 C  CA    . GLU A 1 421 ? 2.247   -0.805  0.486   1.00 49.80  ? 421 GLU A CA    1 
ATOM   3255 C  C     . GLU A 1 421 ? 1.565   0.239   -0.393  1.00 55.68  ? 421 GLU A C     1 
ATOM   3256 O  O     . GLU A 1 421 ? 1.431   0.036   -1.604  1.00 58.03  ? 421 GLU A O     1 
ATOM   3257 C  CB    . GLU A 1 421 ? 1.817   -2.220  0.084   1.00 51.86  ? 421 GLU A CB    1 
ATOM   3258 C  CG    . GLU A 1 421 ? 2.651   -3.284  0.751   1.00 49.61  ? 421 GLU A CG    1 
ATOM   3259 C  CD    . GLU A 1 421 ? 2.411   -4.684  0.198   1.00 50.02  ? 421 GLU A CD    1 
ATOM   3260 O  OE1   . GLU A 1 421 ? 1.374   -5.284  0.526   1.00 47.33  ? 421 GLU A OE1   1 
ATOM   3261 O  OE2   . GLU A 1 421 ? 3.275   -5.178  -0.561  1.00 45.93  ? 421 GLU A OE2   1 
ATOM   3262 N  N     . SER A 1 422 ? 1.154   1.359   0.187   1.00 56.13  ? 422 SER A N     1 
ATOM   3263 C  CA    . SER A 1 422 ? 0.477   2.399   -0.576  1.00 59.10  ? 422 SER A CA    1 
ATOM   3264 C  C     . SER A 1 422 ? 1.482   3.115   -1.461  1.00 60.92  ? 422 SER A C     1 
ATOM   3265 O  O     . SER A 1 422 ? 2.414   3.748   -0.942  1.00 58.79  ? 422 SER A O     1 
ATOM   3266 C  CB    . SER A 1 422 ? -0.212  3.389   0.357   1.00 58.94  ? 422 SER A CB    1 
ATOM   3267 O  OG    . SER A 1 422 ? -1.258  2.759   1.074   1.00 65.09  ? 422 SER A OG    1 
ATOM   3268 N  N     . PRO A 1 423 ? 1.343   3.049   -2.787  1.00 62.34  ? 423 PRO A N     1 
ATOM   3269 C  CA    . PRO A 1 423 ? 2.340   3.684   -3.661  1.00 64.78  ? 423 PRO A CA    1 
ATOM   3270 C  C     . PRO A 1 423 ? 2.393   5.190   -3.512  1.00 66.03  ? 423 PRO A C     1 
ATOM   3271 O  O     . PRO A 1 423 ? 3.365   5.802   -3.969  1.00 67.38  ? 423 PRO A O     1 
ATOM   3272 C  CB    . PRO A 1 423 ? 1.888   3.273   -5.069  1.00 68.63  ? 423 PRO A CB    1 
ATOM   3273 C  CG    . PRO A 1 423 ? 0.412   3.021   -4.923  1.00 65.95  ? 423 PRO A CG    1 
ATOM   3274 C  CD    . PRO A 1 423 ? 0.240   2.436   -3.549  1.00 65.07  ? 423 PRO A CD    1 
ATOM   3275 N  N     . GLU A 1 424 ? 1.390   5.807   -2.886  1.00 61.58  ? 424 GLU A N     1 
ATOM   3276 C  CA    . GLU A 1 424 ? 1.394   7.250   -2.691  1.00 63.61  ? 424 GLU A CA    1 
ATOM   3277 C  C     . GLU A 1 424 ? 2.192   7.688   -1.468  1.00 59.48  ? 424 GLU A C     1 
ATOM   3278 O  O     . GLU A 1 424 ? 2.408   8.893   -1.295  1.00 59.74  ? 424 GLU A O     1 
ATOM   3279 C  CB    . GLU A 1 424 ? -0.043  7.774   -2.590  1.00 63.52  ? 424 GLU A CB    1 
ATOM   3280 C  CG    . GLU A 1 424 ? -0.781  7.418   -1.298  1.00 64.15  ? 424 GLU A CG    1 
ATOM   3281 C  CD    . GLU A 1 424 ? -1.433  6.041   -1.326  1.00 74.79  ? 424 GLU A CD    1 
ATOM   3282 O  OE1   . GLU A 1 424 ? -1.011  5.179   -2.129  1.00 72.89  ? 424 GLU A OE1   1 
ATOM   3283 O  OE2   . GLU A 1 424 ? -2.376  5.818   -0.534  1.00 85.43  ? 424 GLU A OE2   1 
ATOM   3284 N  N     . GLY A 1 425 ? 2.642   6.755   -0.631  1.00 55.58  ? 425 GLY A N     1 
ATOM   3285 C  CA    . GLY A 1 425 ? 3.393   7.094   0.560   1.00 50.66  ? 425 GLY A CA    1 
ATOM   3286 C  C     . GLY A 1 425 ? 2.503   7.560   1.699   1.00 48.32  ? 425 GLY A C     1 
ATOM   3287 O  O     . GLY A 1 425 ? 1.290   7.712   1.564   1.00 51.26  ? 425 GLY A O     1 
ATOM   3288 N  N     . VAL A 1 426 ? 3.129   7.784   2.853   1.00 43.64  ? 426 VAL A N     1 
ATOM   3289 C  CA    . VAL A 1 426 ? 2.432   8.331   4.021   1.00 40.85  ? 426 VAL A CA    1 
ATOM   3290 C  C     . VAL A 1 426 ? 2.995   9.714   4.336   1.00 42.93  ? 426 VAL A C     1 
ATOM   3291 O  O     . VAL A 1 426 ? 4.193   9.951   4.120   1.00 38.11  ? 426 VAL A O     1 
ATOM   3292 C  CB    . VAL A 1 426 ? 2.556   7.402   5.239   1.00 42.89  ? 426 VAL A CB    1 
ATOM   3293 C  CG1   . VAL A 1 426 ? 1.880   6.078   4.953   1.00 44.02  ? 426 VAL A CG1   1 
ATOM   3294 C  CG2   . VAL A 1 426 ? 4.020   7.195   5.609   1.00 39.79  ? 426 VAL A CG2   1 
ATOM   3295 N  N     . PRO A 1 427 ? 2.185   10.648  4.844   1.00 41.78  ? 427 PRO A N     1 
ATOM   3296 C  CA    . PRO A 1 427 ? 2.682   12.008  5.098   1.00 42.56  ? 427 PRO A CA    1 
ATOM   3297 C  C     . PRO A 1 427 ? 3.414   12.098  6.433   1.00 42.60  ? 427 PRO A C     1 
ATOM   3298 O  O     . PRO A 1 427 ? 2.853   11.776  7.488   1.00 40.39  ? 427 PRO A O     1 
ATOM   3299 C  CB    . PRO A 1 427 ? 1.405   12.858  5.102   1.00 49.77  ? 427 PRO A CB    1 
ATOM   3300 C  CG    . PRO A 1 427 ? 0.328   11.922  5.544   1.00 45.02  ? 427 PRO A CG    1 
ATOM   3301 C  CD    . PRO A 1 427 ? 0.727   10.542  5.025   1.00 43.17  ? 427 PRO A CD    1 
ATOM   3302 N  N     . ILE A 1 428 ? 4.660   12.584  6.380   1.00 36.21  ? 428 ILE A N     1 
ATOM   3303 C  CA    . ILE A 1 428 ? 5.535   12.663  7.549   1.00 33.79  ? 428 ILE A CA    1 
ATOM   3304 C  C     . ILE A 1 428 ? 5.355   14.025  8.204   1.00 37.95  ? 428 ILE A C     1 
ATOM   3305 O  O     . ILE A 1 428 ? 5.505   15.061  7.547   1.00 35.19  ? 428 ILE A O     1 
ATOM   3306 C  CB    . ILE A 1 428 ? 7.006   12.445  7.151   1.00 34.68  ? 428 ILE A CB    1 
ATOM   3307 C  CG1   . ILE A 1 428 ? 7.218   11.060  6.518   1.00 33.92  ? 428 ILE A CG1   1 
ATOM   3308 C  CG2   . ILE A 1 428 ? 7.931   12.691  8.348   1.00 34.51  ? 428 ILE A CG2   1 
ATOM   3309 C  CD1   . ILE A 1 428 ? 6.782   9.881   7.403   1.00 34.79  ? 428 ILE A CD1   1 
ATOM   3310 N  N     . GLU A 1 429 ? 5.046   14.026  9.502   1.00 33.44  ? 429 GLU A N     1 
ATOM   3311 C  CA    . GLU A 1 429 ? 4.855   15.261  10.247  1.00 34.05  ? 429 GLU A CA    1 
ATOM   3312 C  C     . GLU A 1 429 ? 5.954   15.530  11.265  1.00 37.54  ? 429 GLU A C     1 
ATOM   3313 O  O     . GLU A 1 429 ? 5.991   16.625  11.846  1.00 34.77  ? 429 GLU A O     1 
ATOM   3314 C  CB    . GLU A 1 429 ? 3.489   15.247  10.951  1.00 35.69  ? 429 GLU A CB    1 
ATOM   3315 C  CG    . GLU A 1 429 ? 2.319   15.202  9.983   1.00 37.52  ? 429 GLU A CG    1 
ATOM   3316 C  CD    . GLU A 1 429 ? 0.981   15.357  10.671  1.00 45.53  ? 429 GLU A CD    1 
ATOM   3317 O  OE1   . GLU A 1 429 ? 0.811   16.295  11.483  1.00 46.82  ? 429 GLU A OE1   1 
ATOM   3318 O  OE2   . GLU A 1 429 ? 0.089   14.542  10.389  1.00 43.33  ? 429 GLU A OE2   1 
ATOM   3319 N  N     . GLY A 1 430 ? 6.846   14.576  11.496  1.00 35.95  ? 430 GLY A N     1 
ATOM   3320 C  CA    . GLY A 1 430 ? 7.961   14.800  12.395  1.00 33.63  ? 430 GLY A CA    1 
ATOM   3321 C  C     . GLY A 1 430 ? 9.096   13.866  12.054  1.00 34.87  ? 430 GLY A C     1 
ATOM   3322 O  O     . GLY A 1 430 ? 8.879   12.756  11.556  1.00 32.08  ? 430 GLY A O     1 
ATOM   3323 N  N     . ILE A 1 431 ? 10.319  14.330  12.314  1.00 31.00  ? 431 ILE A N     1 
ATOM   3324 C  CA    . ILE A 1 431 ? 11.544  13.587  12.050  1.00 33.01  ? 431 ILE A CA    1 
ATOM   3325 C  C     . ILE A 1 431 ? 12.340  13.546  13.344  1.00 31.47  ? 431 ILE A C     1 
ATOM   3326 O  O     . ILE A 1 431 ? 12.525  14.583  13.986  1.00 30.58  ? 431 ILE A O     1 
ATOM   3327 C  CB    . ILE A 1 431 ? 12.375  14.247  10.927  1.00 30.85  ? 431 ILE A CB    1 
ATOM   3328 C  CG1   . ILE A 1 431 ? 11.648  14.136  9.586   1.00 35.28  ? 431 ILE A CG1   1 
ATOM   3329 C  CG2   . ILE A 1 431 ? 13.732  13.594  10.810  1.00 35.92  ? 431 ILE A CG2   1 
ATOM   3330 C  CD1   . ILE A 1 431 ? 12.425  14.798  8.409   1.00 36.95  ? 431 ILE A CD1   1 
ATOM   3331 N  N     . ILE A 1 432 ? 12.818  12.359  13.724  1.00 31.04  ? 432 ILE A N     1 
ATOM   3332 C  CA    . ILE A 1 432 ? 13.509  12.154  14.992  1.00 34.08  ? 432 ILE A CA    1 
ATOM   3333 C  C     . ILE A 1 432 ? 14.944  11.712  14.730  1.00 33.15  ? 432 ILE A C     1 
ATOM   3334 O  O     . ILE A 1 432 ? 15.175  10.756  13.985  1.00 33.91  ? 432 ILE A O     1 
ATOM   3335 C  CB    . ILE A 1 432 ? 12.796  11.104  15.867  1.00 32.93  ? 432 ILE A CB    1 
ATOM   3336 C  CG1   . ILE A 1 432 ? 11.304  11.428  16.011  1.00 32.85  ? 432 ILE A CG1   1 
ATOM   3337 C  CG2   . ILE A 1 432 ? 13.451  11.062  17.235  1.00 34.56  ? 432 ILE A CG2   1 
ATOM   3338 C  CD1   . ILE A 1 432 ? 10.492  10.269  16.685  1.00 34.26  ? 432 ILE A CD1   1 
ATOM   3339 N  N     . PHE A 1 433 ? 15.899  12.373  15.377  1.00 32.30  ? 433 PHE A N     1 
ATOM   3340 C  CA    . PHE A 1 433 ? 17.284  11.923  15.391  1.00 31.32  ? 433 PHE A CA    1 
ATOM   3341 C  C     . PHE A 1 433 ? 17.652  11.429  16.782  1.00 34.83  ? 433 PHE A C     1 
ATOM   3342 O  O     . PHE A 1 433 ? 17.057  11.841  17.780  1.00 32.29  ? 433 PHE A O     1 
ATOM   3343 C  CB    . PHE A 1 433 ? 18.248  13.049  15.002  1.00 30.38  ? 433 PHE A CB    1 
ATOM   3344 C  CG    . PHE A 1 433 ? 18.050  13.574  13.609  1.00 32.40  ? 433 PHE A CG    1 
ATOM   3345 C  CD1   . PHE A 1 433 ? 18.181  12.720  12.510  1.00 31.86  ? 433 PHE A CD1   1 
ATOM   3346 C  CD2   . PHE A 1 433 ? 17.783  14.918  13.392  1.00 32.55  ? 433 PHE A CD2   1 
ATOM   3347 C  CE1   . PHE A 1 433 ? 18.014  13.195  11.213  1.00 33.38  ? 433 PHE A CE1   1 
ATOM   3348 C  CE2   . PHE A 1 433 ? 17.621  15.404  12.094  1.00 33.50  ? 433 PHE A CE2   1 
ATOM   3349 C  CZ    . PHE A 1 433 ? 17.741  14.527  10.998  1.00 31.90  ? 433 PHE A CZ    1 
ATOM   3350 N  N     . GLY A 1 434 ? 18.671  10.579  16.846  1.00 32.10  ? 434 GLY A N     1 
ATOM   3351 C  CA    . GLY A 1 434 ? 19.221  10.200  18.135  1.00 32.98  ? 434 GLY A CA    1 
ATOM   3352 C  C     . GLY A 1 434 ? 20.208  9.059   18.023  1.00 37.27  ? 434 GLY A C     1 
ATOM   3353 O  O     . GLY A 1 434 ? 20.281  8.353   17.018  1.00 37.99  ? 434 GLY A O     1 
ATOM   3354 N  N     . GLY A 1 435 ? 20.974  8.892   19.094  1.00 38.42  ? 435 GLY A N     1 
ATOM   3355 C  CA    . GLY A 1 435 ? 21.980  7.864   19.165  1.00 37.35  ? 435 GLY A CA    1 
ATOM   3356 C  C     . GLY A 1 435 ? 22.285  7.508   20.602  1.00 39.80  ? 435 GLY A C     1 
ATOM   3357 O  O     . GLY A 1 435 ? 21.636  7.986   21.537  1.00 37.84  ? 435 GLY A O     1 
ATOM   3358 N  N     . ARG A 1 436 ? 23.297  6.664   20.764  1.00 37.38  ? 436 ARG A N     1 
ATOM   3359 C  CA    . ARG A 1 436 ? 23.729  6.198   22.079  1.00 40.89  ? 436 ARG A CA    1 
ATOM   3360 C  C     . ARG A 1 436 ? 24.663  7.225   22.695  1.00 43.91  ? 436 ARG A C     1 
ATOM   3361 O  O     . ARG A 1 436 ? 25.842  7.300   22.343  1.00 41.38  ? 436 ARG A O     1 
ATOM   3362 C  CB    . ARG A 1 436 ? 24.418  4.845   21.970  1.00 43.21  ? 436 ARG A CB    1 
ATOM   3363 C  CG    . ARG A 1 436 ? 23.453  3.710   21.791  1.00 44.65  ? 436 ARG A CG    1 
ATOM   3364 C  CD    . ARG A 1 436 ? 24.160  2.460   21.309  1.00 44.52  ? 436 ARG A CD    1 
ATOM   3365 N  NE    . ARG A 1 436 ? 23.171  1.431   21.034  1.00 46.37  ? 436 ARG A NE    1 
ATOM   3366 C  CZ    . ARG A 1 436 ? 22.694  0.605   21.951  1.00 47.58  ? 436 ARG A CZ    1 
ATOM   3367 N  NH1   . ARG A 1 436 ? 23.183  0.586   23.185  1.00 49.02  ? 436 ARG A NH1   1 
ATOM   3368 N  NH2   . ARG A 1 436 ? 21.706  -0.226  21.623  1.00 48.35  ? 436 ARG A NH2   1 
ATOM   3369 N  N     . ARG A 1 437 ? 24.146  8.008   23.633  1.00 38.92  ? 437 ARG A N     1 
ATOM   3370 C  CA    . ARG A 1 437 ? 24.956  8.994   24.342  1.00 43.38  ? 437 ARG A CA    1 
ATOM   3371 C  C     . ARG A 1 437 ? 24.804  8.702   25.820  1.00 41.24  ? 437 ARG A C     1 
ATOM   3372 O  O     . ARG A 1 437 ? 23.735  8.996   26.393  1.00 41.74  ? 437 ARG A O     1 
ATOM   3373 C  CB    . ARG A 1 437 ? 24.537  10.429  24.039  1.00 34.98  ? 437 ARG A CB    1 
ATOM   3374 C  CG    . ARG A 1 437 ? 24.802  10.917  22.616  1.00 39.00  ? 437 ARG A CG    1 
ATOM   3375 C  CD    . ARG A 1 437 ? 26.250  10.773  22.184  1.00 43.46  ? 437 ARG A CD    1 
ATOM   3376 N  NE    . ARG A 1 437 ? 27.216  11.511  22.988  1.00 39.82  ? 437 ARG A NE    1 
ATOM   3377 C  CZ    . ARG A 1 437 ? 27.609  12.755  22.746  1.00 39.03  ? 437 ARG A CZ    1 
ATOM   3378 N  NH1   . ARG A 1 437 ? 27.041  13.493  21.804  1.00 36.67  ? 437 ARG A NH1   1 
ATOM   3379 N  NH2   . ARG A 1 437 ? 28.605  13.268  23.461  1.00 42.05  ? 437 ARG A NH2   1 
ATOM   3380 N  N     . PRO A 1 438 ? 25.821  8.128   26.468  1.00 44.97  ? 438 PRO A N     1 
ATOM   3381 C  CA    . PRO A 1 438 ? 25.696  7.805   27.898  1.00 47.70  ? 438 PRO A CA    1 
ATOM   3382 C  C     . PRO A 1 438 ? 25.746  9.024   28.809  1.00 46.26  ? 438 PRO A C     1 
ATOM   3383 O  O     . PRO A 1 438 ? 25.388  8.908   29.990  1.00 47.76  ? 438 PRO A O     1 
ATOM   3384 C  CB    . PRO A 1 438 ? 26.891  6.875   28.150  1.00 50.29  ? 438 PRO A CB    1 
ATOM   3385 C  CG    . PRO A 1 438 ? 27.908  7.306   27.109  1.00 49.94  ? 438 PRO A CG    1 
ATOM   3386 C  CD    . PRO A 1 438 ? 27.116  7.714   25.900  1.00 45.59  ? 438 PRO A CD    1 
ATOM   3387 N  N     . ALA A 1 439 ? 26.157  10.182  28.303  1.00 45.34  ? 439 ALA A N     1 
ATOM   3388 C  CA    . ALA A 1 439 ? 26.351  11.356  29.140  1.00 47.52  ? 439 ALA A CA    1 
ATOM   3389 C  C     . ALA A 1 439 ? 25.884  12.605  28.413  1.00 41.88  ? 439 ALA A C     1 
ATOM   3390 O  O     . ALA A 1 439 ? 25.974  12.696  27.185  1.00 39.39  ? 439 ALA A O     1 
ATOM   3391 C  CB    . ALA A 1 439 ? 27.824  11.534  29.532  1.00 46.85  ? 439 ALA A CB    1 
ATOM   3392 N  N     . GLY A 1 440 ? 25.374  13.561  29.192  1.00 41.54  ? 440 GLY A N     1 
ATOM   3393 C  CA    . GLY A 1 440 ? 25.228  14.940  28.753  1.00 43.43  ? 440 GLY A CA    1 
ATOM   3394 C  C     . GLY A 1 440 ? 24.020  15.304  27.909  1.00 46.63  ? 440 GLY A C     1 
ATOM   3395 O  O     . GLY A 1 440 ? 23.533  16.441  27.985  1.00 45.55  ? 440 GLY A O     1 
ATOM   3396 N  N     . VAL A 1 441 ? 23.534  14.377  27.093  1.00 42.70  ? 441 VAL A N     1 
ATOM   3397 C  CA    . VAL A 1 441 ? 22.496  14.663  26.105  1.00 39.82  ? 441 VAL A CA    1 
ATOM   3398 C  C     . VAL A 1 441 ? 21.145  14.298  26.711  1.00 40.02  ? 441 VAL A C     1 
ATOM   3399 O  O     . VAL A 1 441 ? 20.957  13.141  27.123  1.00 37.91  ? 441 VAL A O     1 
ATOM   3400 C  CB    . VAL A 1 441 ? 22.745  13.903  24.794  1.00 41.61  ? 441 VAL A CB    1 
ATOM   3401 C  CG1   . VAL A 1 441 ? 21.596  14.142  23.803  1.00 38.75  ? 441 VAL A CG1   1 
ATOM   3402 C  CG2   . VAL A 1 441 ? 24.080  14.342  24.200  1.00 39.93  ? 441 VAL A CG2   1 
ATOM   3403 N  N     . PRO A 1 442 ? 20.191  15.221  26.771  1.00 39.97  ? 442 PRO A N     1 
ATOM   3404 C  CA    . PRO A 1 442 ? 18.941  14.965  27.489  1.00 40.96  ? 442 PRO A CA    1 
ATOM   3405 C  C     . PRO A 1 442 ? 18.001  14.057  26.705  1.00 39.11  ? 442 PRO A C     1 
ATOM   3406 O  O     . PRO A 1 442 ? 18.206  13.764  25.528  1.00 37.65  ? 442 PRO A O     1 
ATOM   3407 C  CB    . PRO A 1 442 ? 18.343  16.369  27.667  1.00 44.00  ? 442 PRO A CB    1 
ATOM   3408 C  CG    . PRO A 1 442 ? 18.902  17.166  26.558  1.00 43.15  ? 442 PRO A CG    1 
ATOM   3409 C  CD    . PRO A 1 442 ? 20.266  16.605  26.256  1.00 43.13  ? 442 PRO A CD    1 
ATOM   3410 N  N     . LEU A 1 443 ? 16.934  13.642  27.400  1.00 37.98  ? 443 LEU A N     1 
ATOM   3411 C  CA    . LEU A 1 443 ? 16.023  12.620  26.891  1.00 37.89  ? 443 LEU A CA    1 
ATOM   3412 C  C     . LEU A 1 443 ? 15.389  13.026  25.564  1.00 38.46  ? 443 LEU A C     1 
ATOM   3413 O  O     . LEU A 1 443 ? 15.259  12.194  24.655  1.00 35.28  ? 443 LEU A O     1 
ATOM   3414 C  CB    . LEU A 1 443 ? 14.948  12.326  27.937  1.00 40.51  ? 443 LEU A CB    1 
ATOM   3415 C  CG    . LEU A 1 443 ? 13.785  11.420  27.532  1.00 40.46  ? 443 LEU A CG    1 
ATOM   3416 C  CD1   . LEU A 1 443 ? 14.269  10.001  27.184  1.00 40.15  ? 443 LEU A CD1   1 
ATOM   3417 C  CD2   . LEU A 1 443 ? 12.769  11.379  28.662  1.00 46.55  ? 443 LEU A CD2   1 
ATOM   3418 N  N     . VAL A 1 444 ? 15.009  14.294  25.419  1.00 31.46  ? 444 VAL A N     1 
ATOM   3419 C  CA    . VAL A 1 444 ? 14.386  14.759  24.179  1.00 30.62  ? 444 VAL A CA    1 
ATOM   3420 C  C     . VAL A 1 444 ? 14.486  16.279  24.131  1.00 34.70  ? 444 VAL A C     1 
ATOM   3421 O  O     . VAL A 1 444 ? 14.342  16.955  25.148  1.00 35.60  ? 444 VAL A O     1 
ATOM   3422 C  CB    . VAL A 1 444 ? 12.914  14.273  24.078  1.00 35.99  ? 444 VAL A CB    1 
ATOM   3423 C  CG1   . VAL A 1 444 ? 12.099  14.741  25.273  1.00 37.00  ? 444 VAL A CG1   1 
ATOM   3424 C  CG2   . VAL A 1 444 ? 12.259  14.706  22.738  1.00 31.28  ? 444 VAL A CG2   1 
ATOM   3425 N  N     . TYR A 1 445 ? 14.758  16.813  22.942  1.00 29.99  ? 445 TYR A N     1 
ATOM   3426 C  CA    . TYR A 1 445 ? 14.596  18.241  22.705  1.00 32.39  ? 445 TYR A CA    1 
ATOM   3427 C  C     . TYR A 1 445 ? 14.100  18.432  21.280  1.00 32.29  ? 445 TYR A C     1 
ATOM   3428 O  O     . TYR A 1 445 ? 14.075  17.493  20.485  1.00 32.31  ? 445 TYR A O     1 
ATOM   3429 C  CB    . TYR A 1 445 ? 15.879  19.032  22.988  1.00 31.69  ? 445 TYR A CB    1 
ATOM   3430 C  CG    . TYR A 1 445 ? 17.102  18.705  22.166  1.00 33.16  ? 445 TYR A CG    1 
ATOM   3431 C  CD1   . TYR A 1 445 ? 18.016  17.753  22.597  1.00 36.05  ? 445 TYR A CD1   1 
ATOM   3432 C  CD2   . TYR A 1 445 ? 17.382  19.395  20.988  1.00 35.96  ? 445 TYR A CD2   1 
ATOM   3433 C  CE1   . TYR A 1 445 ? 19.152  17.470  21.870  1.00 36.33  ? 445 TYR A CE1   1 
ATOM   3434 C  CE2   . TYR A 1 445 ? 18.519  19.115  20.250  1.00 35.68  ? 445 TYR A CE2   1 
ATOM   3435 C  CZ    . TYR A 1 445 ? 19.403  18.155  20.697  1.00 37.35  ? 445 TYR A CZ    1 
ATOM   3436 O  OH    . TYR A 1 445 ? 20.545  17.870  19.958  1.00 41.16  ? 445 TYR A OH    1 
ATOM   3437 N  N     . GLU A 1 446 ? 13.639  19.642  20.985  1.00 33.04  ? 446 GLU A N     1 
ATOM   3438 C  CA    . GLU A 1 446 ? 13.070  19.982  19.687  1.00 34.33  ? 446 GLU A CA    1 
ATOM   3439 C  C     . GLU A 1 446 ? 13.887  21.096  19.037  1.00 33.38  ? 446 GLU A C     1 
ATOM   3440 O  O     . GLU A 1 446 ? 14.322  22.035  19.712  1.00 34.84  ? 446 GLU A O     1 
ATOM   3441 C  CB    . GLU A 1 446 ? 11.604  20.407  19.844  1.00 35.10  ? 446 GLU A CB    1 
ATOM   3442 C  CG    . GLU A 1 446 ? 10.879  20.875  18.589  1.00 34.78  ? 446 GLU A CG    1 
ATOM   3443 C  CD    . GLU A 1 446 ? 9.565   21.573  18.937  1.00 38.87  ? 446 GLU A CD    1 
ATOM   3444 O  OE1   . GLU A 1 446 ? 8.862   21.067  19.826  1.00 42.54  ? 446 GLU A OE1   1 
ATOM   3445 O  OE2   . GLU A 1 446 ? 9.244   22.635  18.356  1.00 40.34  ? 446 GLU A OE2   1 
ATOM   3446 N  N     . ALA A 1 447 ? 14.092  20.984  17.725  1.00 33.42  ? 447 ALA A N     1 
ATOM   3447 C  CA    . ALA A 1 447 ? 14.894  21.951  16.989  1.00 32.78  ? 447 ALA A CA    1 
ATOM   3448 C  C     . ALA A 1 447 ? 14.162  23.289  16.874  1.00 34.84  ? 447 ALA A C     1 
ATOM   3449 O  O     . ALA A 1 447 ? 12.930  23.357  16.914  1.00 36.25  ? 447 ALA A O     1 
ATOM   3450 C  CB    . ALA A 1 447 ? 15.234  21.414  15.594  1.00 33.07  ? 447 ALA A CB    1 
ATOM   3451 N  N     . LEU A 1 448 ? 14.944  24.368  16.732  1.00 35.64  ? 448 LEU A N     1 
ATOM   3452 C  CA    . LEU A 1 448 ? 14.395  25.726  16.724  1.00 34.50  ? 448 LEU A CA    1 
ATOM   3453 C  C     . LEU A 1 448 ? 13.872  26.149  15.360  1.00 40.21  ? 448 LEU A C     1 
ATOM   3454 O  O     . LEU A 1 448 ? 13.110  27.121  15.271  1.00 36.63  ? 448 LEU A O     1 
ATOM   3455 C  CB    . LEU A 1 448 ? 15.464  26.725  17.164  1.00 34.54  ? 448 LEU A CB    1 
ATOM   3456 C  CG    . LEU A 1 448 ? 16.173  26.435  18.488  1.00 38.25  ? 448 LEU A CG    1 
ATOM   3457 C  CD1   . LEU A 1 448 ? 17.384  27.349  18.641  1.00 43.21  ? 448 LEU A CD1   1 
ATOM   3458 C  CD2   . LEU A 1 448 ? 15.189  26.656  19.628  1.00 41.08  ? 448 LEU A CD2   1 
ATOM   3459 N  N     . SER A 1 449 ? 14.289  25.463  14.303  1.00 37.41  ? 449 SER A N     1 
ATOM   3460 C  CA    . SER A 1 449 ? 13.993  25.857  12.934  1.00 37.24  ? 449 SER A CA    1 
ATOM   3461 C  C     . SER A 1 449 ? 14.404  24.681  12.063  1.00 35.39  ? 449 SER A C     1 
ATOM   3462 O  O     . SER A 1 449 ? 14.998  23.720  12.546  1.00 33.25  ? 449 SER A O     1 
ATOM   3463 C  CB    . SER A 1 449 ? 14.752  27.128  12.530  1.00 40.12  ? 449 SER A CB    1 
ATOM   3464 O  OG    . SER A 1 449 ? 16.157  26.882  12.495  1.00 35.78  ? 449 SER A OG    1 
ATOM   3465 N  N     . TRP A 1 450 ? 14.098  24.772  10.770  1.00 39.79  ? 450 TRP A N     1 
ATOM   3466 C  CA    . TRP A 1 450 ? 14.568  23.753  9.832   1.00 36.25  ? 450 TRP A CA    1 
ATOM   3467 C  C     . TRP A 1 450 ? 16.093  23.692  9.797   1.00 33.65  ? 450 TRP A C     1 
ATOM   3468 O  O     . TRP A 1 450 ? 16.682  22.603  9.844   1.00 32.71  ? 450 TRP A O     1 
ATOM   3469 C  CB    . TRP A 1 450 ? 14.011  24.031  8.442   1.00 37.36  ? 450 TRP A CB    1 
ATOM   3470 C  CG    . TRP A 1 450 ? 14.350  22.956  7.478   1.00 38.70  ? 450 TRP A CG    1 
ATOM   3471 C  CD1   . TRP A 1 450 ? 15.215  23.037  6.422   1.00 39.05  ? 450 TRP A CD1   1 
ATOM   3472 C  CD2   . TRP A 1 450 ? 13.845  21.622  7.488   1.00 36.42  ? 450 TRP A CD2   1 
ATOM   3473 N  NE1   . TRP A 1 450 ? 15.270  21.823  5.766   1.00 37.85  ? 450 TRP A NE1   1 
ATOM   3474 C  CE2   . TRP A 1 450 ? 14.431  20.943  6.402   1.00 38.98  ? 450 TRP A CE2   1 
ATOM   3475 C  CE3   . TRP A 1 450 ? 12.937  20.934  8.303   1.00 38.68  ? 450 TRP A CE3   1 
ATOM   3476 C  CZ2   . TRP A 1 450 ? 14.147  19.612  6.121   1.00 39.40  ? 450 TRP A CZ2   1 
ATOM   3477 C  CZ3   . TRP A 1 450 ? 12.657  19.610  8.021   1.00 36.91  ? 450 TRP A CZ3   1 
ATOM   3478 C  CH2   . TRP A 1 450 ? 13.259  18.964  6.941   1.00 38.30  ? 450 TRP A CH2   1 
ATOM   3479 N  N     . GLN A 1 451 ? 16.744  24.862  9.725   1.00 36.04  ? 451 GLN A N     1 
ATOM   3480 C  CA    . GLN A 1 451 ? 18.205  24.956  9.635   1.00 34.16  ? 451 GLN A CA    1 
ATOM   3481 C  C     . GLN A 1 451 ? 18.881  24.383  10.880  1.00 33.97  ? 451 GLN A C     1 
ATOM   3482 O  O     . GLN A 1 451 ? 19.862  23.633  10.783  1.00 35.28  ? 451 GLN A O     1 
ATOM   3483 C  CB    . GLN A 1 451 ? 18.623  26.425  9.424   1.00 40.70  ? 451 GLN A CB    1 
ATOM   3484 C  CG    . GLN A 1 451 ? 18.201  27.061  8.081   1.00 41.68  ? 451 GLN A CG    1 
ATOM   3485 C  CD    . GLN A 1 451 ? 16.699  27.353  7.993   1.00 48.54  ? 451 GLN A CD    1 
ATOM   3486 O  OE1   . GLN A 1 451 ? 16.030  27.536  9.008   1.00 43.62  ? 451 GLN A OE1   1 
ATOM   3487 N  NE2   . GLN A 1 451 ? 16.165  27.372  6.773   1.00 48.94  ? 451 GLN A NE2   1 
ATOM   3488 N  N     . HIS A 1 452 ? 18.366  24.717  12.060  1.00 32.77  ? 452 HIS A N     1 
ATOM   3489 C  CA    . HIS A 1 452 ? 18.897  24.129  13.282  1.00 30.50  ? 452 HIS A CA    1 
ATOM   3490 C  C     . HIS A 1 452 ? 18.693  22.620  13.289  1.00 31.34  ? 452 HIS A C     1 
ATOM   3491 O  O     . HIS A 1 452 ? 19.579  21.866  13.701  1.00 31.94  ? 452 HIS A O     1 
ATOM   3492 C  CB    . HIS A 1 452 ? 18.245  24.774  14.503  1.00 35.24  ? 452 HIS A CB    1 
ATOM   3493 C  CG    . HIS A 1 452 ? 18.769  24.248  15.804  1.00 33.96  ? 452 HIS A CG    1 
ATOM   3494 N  ND1   . HIS A 1 452 ? 17.943  23.788  16.807  1.00 35.04  ? 452 HIS A ND1   1 
ATOM   3495 C  CD2   . HIS A 1 452 ? 20.036  24.100  16.259  1.00 31.08  ? 452 HIS A CD2   1 
ATOM   3496 C  CE1   . HIS A 1 452 ? 18.680  23.358  17.820  1.00 36.09  ? 452 HIS A CE1   1 
ATOM   3497 N  NE2   . HIS A 1 452 ? 19.953  23.551  17.520  1.00 35.48  ? 452 HIS A NE2   1 
ATOM   3498 N  N     . GLY A 1 453 ? 17.550  22.161  12.783  1.00 31.22  ? 453 GLY A N     1 
ATOM   3499 C  CA    . GLY A 1 453 ? 17.285  20.737  12.751  1.00 29.82  ? 453 GLY A CA    1 
ATOM   3500 C  C     . GLY A 1 453 ? 18.243  19.980  11.851  1.00 30.72  ? 453 GLY A C     1 
ATOM   3501 O  O     . GLY A 1 453 ? 18.673  18.876  12.189  1.00 30.33  ? 453 GLY A O     1 
ATOM   3502 N  N     . VAL A 1 454 ? 18.579  20.553  10.690  1.00 29.31  ? 454 VAL A N     1 
ATOM   3503 C  CA    . VAL A 1 454 ? 19.574  19.930  9.820   1.00 29.87  ? 454 VAL A CA    1 
ATOM   3504 C  C     . VAL A 1 454 ? 20.920  19.873  10.522  1.00 30.39  ? 454 VAL A C     1 
ATOM   3505 O  O     . VAL A 1 454 ? 21.630  18.864  10.447  1.00 31.94  ? 454 VAL A O     1 
ATOM   3506 C  CB    . VAL A 1 454 ? 19.670  20.676  8.477   1.00 33.50  ? 454 VAL A CB    1 
ATOM   3507 C  CG1   . VAL A 1 454 ? 20.836  20.123  7.650   1.00 31.78  ? 454 VAL A CG1   1 
ATOM   3508 C  CG2   . VAL A 1 454 ? 18.349  20.570  7.721   1.00 32.09  ? 454 VAL A CG2   1 
ATOM   3509 N  N     . PHE A 1 455 ? 21.270  20.936  11.253  1.00 33.13  ? 455 PHE A N     1 
ATOM   3510 C  CA    . PHE A 1 455 ? 22.514  20.948  12.017  1.00 31.91  ? 455 PHE A CA    1 
ATOM   3511 C  C     . PHE A 1 455 ? 22.504  19.889  13.116  1.00 31.99  ? 455 PHE A C     1 
ATOM   3512 O  O     . PHE A 1 455 ? 23.540  19.275  13.409  1.00 32.35  ? 455 PHE A O     1 
ATOM   3513 C  CB    . PHE A 1 455 ? 22.757  22.347  12.607  1.00 32.62  ? 455 PHE A CB    1 
ATOM   3514 C  CG    . PHE A 1 455 ? 23.797  22.354  13.688  1.00 33.93  ? 455 PHE A CG    1 
ATOM   3515 C  CD1   . PHE A 1 455 ? 25.145  22.381  13.367  1.00 35.52  ? 455 PHE A CD1   1 
ATOM   3516 C  CD2   . PHE A 1 455 ? 23.430  22.272  15.020  1.00 35.75  ? 455 PHE A CD2   1 
ATOM   3517 C  CE1   . PHE A 1 455 ? 26.111  22.349  14.359  1.00 32.88  ? 455 PHE A CE1   1 
ATOM   3518 C  CE2   . PHE A 1 455 ? 24.382  22.247  16.014  1.00 35.72  ? 455 PHE A CE2   1 
ATOM   3519 C  CZ    . PHE A 1 455 ? 25.722  22.271  15.689  1.00 36.56  ? 455 PHE A CZ    1 
ATOM   3520 N  N     . VAL A 1 456 ? 21.345  19.660  13.739  1.00 30.67  ? 456 VAL A N     1 
ATOM   3521 C  CA    . VAL A 1 456 ? 21.233  18.618  14.759  1.00 30.40  ? 456 VAL A CA    1 
ATOM   3522 C  C     . VAL A 1 456 ? 21.510  17.238  14.162  1.00 32.37  ? 456 VAL A C     1 
ATOM   3523 O  O     . VAL A 1 456 ? 22.212  16.414  14.763  1.00 29.66  ? 456 VAL A O     1 
ATOM   3524 C  CB    . VAL A 1 456 ? 19.845  18.661  15.421  1.00 31.77  ? 456 VAL A CB    1 
ATOM   3525 C  CG1   . VAL A 1 456 ? 19.597  17.374  16.238  1.00 32.01  ? 456 VAL A CG1   1 
ATOM   3526 C  CG2   . VAL A 1 456 ? 19.702  19.902  16.283  1.00 32.14  ? 456 VAL A CG2   1 
ATOM   3527 N  N     . GLY A 1 457 ? 20.954  16.955  12.981  1.00 28.61  ? 457 GLY A N     1 
ATOM   3528 C  CA    . GLY A 1 457 ? 21.298  15.705  12.306  1.00 29.03  ? 457 GLY A CA    1 
ATOM   3529 C  C     . GLY A 1 457 ? 22.779  15.607  11.984  1.00 30.51  ? 457 GLY A C     1 
ATOM   3530 O  O     . GLY A 1 457 ? 23.398  14.565  12.189  1.00 30.99  ? 457 GLY A O     1 
ATOM   3531 N  N     . ALA A 1 458 ? 23.370  16.708  11.498  1.00 29.57  ? 458 ALA A N     1 
ATOM   3532 C  CA    . ALA A 1 458 ? 24.785  16.731  11.136  1.00 29.48  ? 458 ALA A CA    1 
ATOM   3533 C  C     . ALA A 1 458 ? 25.679  16.510  12.345  1.00 32.79  ? 458 ALA A C     1 
ATOM   3534 O  O     . ALA A 1 458 ? 26.794  15.981  12.206  1.00 32.03  ? 458 ALA A O     1 
ATOM   3535 C  CB    . ALA A 1 458 ? 25.128  18.073  10.464  1.00 31.66  ? 458 ALA A CB    1 
ATOM   3536 N  N     . ALA A 1 459 ? 25.201  16.882  13.532  1.00 29.67  ? 459 ALA A N     1 
ATOM   3537 C  CA    . ALA A 1 459 ? 25.981  16.835  14.764  1.00 32.10  ? 459 ALA A CA    1 
ATOM   3538 C  C     . ALA A 1 459 ? 25.850  15.516  15.517  1.00 30.21  ? 459 ALA A C     1 
ATOM   3539 O  O     . ALA A 1 459 ? 26.528  15.342  16.535  1.00 31.30  ? 459 ALA A O     1 
ATOM   3540 C  CB    . ALA A 1 459 ? 25.569  17.992  15.691  1.00 32.93  ? 459 ALA A CB    1 
ATOM   3541 N  N     . MET A 1 460 ? 25.034  14.577  15.030  1.00 30.24  ? 460 MET A N     1 
ATOM   3542 C  CA    . MET A 1 460 ? 24.810  13.308  15.734  1.00 32.03  ? 460 MET A CA    1 
ATOM   3543 C  C     . MET A 1 460 ? 26.107  12.574  16.055  1.00 31.97  ? 460 MET A C     1 
ATOM   3544 O  O     . MET A 1 460 ? 27.038  12.514  15.242  1.00 35.25  ? 460 MET A O     1 
ATOM   3545 C  CB    . MET A 1 460 ? 23.911  12.395  14.910  1.00 31.52  ? 460 MET A CB    1 
ATOM   3546 C  CG    . MET A 1 460 ? 22.474  12.836  14.908  1.00 34.11  ? 460 MET A CG    1 
ATOM   3547 S  SD    . MET A 1 460 ? 21.488  11.849  13.781  1.00 35.61  ? 460 MET A SD    1 
ATOM   3548 C  CE    . MET A 1 460 ? 21.772  10.206  14.429  1.00 31.48  ? 460 MET A CE    1 
ATOM   3549 N  N     . ARG A 1 461 ? 26.160  12.034  17.270  1.00 28.68  ? 461 ARG A N     1 
ATOM   3550 C  CA    . ARG A 1 461 ? 27.252  11.194  17.736  1.00 35.05  ? 461 ARG A CA    1 
ATOM   3551 C  C     . ARG A 1 461 ? 26.670  10.031  18.526  1.00 34.99  ? 461 ARG A C     1 
ATOM   3552 O  O     . ARG A 1 461 ? 25.575  10.126  19.080  1.00 34.56  ? 461 ARG A O     1 
ATOM   3553 C  CB    . ARG A 1 461 ? 28.232  11.989  18.594  1.00 33.89  ? 461 ARG A CB    1 
ATOM   3554 C  CG    . ARG A 1 461 ? 28.903  13.116  17.820  1.00 32.87  ? 461 ARG A CG    1 
ATOM   3555 C  CD    . ARG A 1 461 ? 29.731  13.939  18.760  1.00 41.08  ? 461 ARG A CD    1 
ATOM   3556 N  NE    . ARG A 1 461 ? 31.001  13.298  19.040  1.00 40.37  ? 461 ARG A NE    1 
ATOM   3557 C  CZ    . ARG A 1 461 ? 31.761  13.574  20.088  1.00 45.32  ? 461 ARG A CZ    1 
ATOM   3558 N  NH1   . ARG A 1 461 ? 31.372  14.431  21.012  1.00 40.47  ? 461 ARG A NH1   1 
ATOM   3559 N  NH2   . ARG A 1 461 ? 32.935  12.959  20.220  1.00 45.18  ? 461 ARG A NH2   1 
ATOM   3560 N  N     . SER A 1 462 ? 27.416  8.932   18.593  1.00 36.59  ? 462 SER A N     1 
ATOM   3561 C  CA    . SER A 1 462 ? 26.836  7.699   19.127  1.00 41.09  ? 462 SER A CA    1 
ATOM   3562 C  C     . SER A 1 462 ? 27.926  6.679   19.431  1.00 45.43  ? 462 SER A C     1 
ATOM   3563 O  O     . SER A 1 462 ? 28.908  6.571   18.689  1.00 44.39  ? 462 SER A O     1 
ATOM   3564 C  CB    . SER A 1 462 ? 25.831  7.105   18.128  1.00 38.81  ? 462 SER A CB    1 
ATOM   3565 O  OG    . SER A 1 462 ? 25.154  5.985   18.660  1.00 39.49  ? 462 SER A OG    1 
ATOM   3566 N  N     . GLU A 1 463 ? 27.737  5.933   20.524  1.00 46.63  ? 463 GLU A N     1 
ATOM   3567 C  CA    . GLU A 1 463 ? 28.591  4.791   20.819  1.00 55.55  ? 463 GLU A CA    1 
ATOM   3568 C  C     . GLU A 1 463 ? 28.568  3.814   19.655  1.00 52.24  ? 463 GLU A C     1 
ATOM   3569 O  O     . GLU A 1 463 ? 27.510  3.535   19.086  1.00 49.95  ? 463 GLU A O     1 
ATOM   3570 C  CB    . GLU A 1 463 ? 28.114  4.068   22.079  1.00 57.91  ? 463 GLU A CB    1 
ATOM   3571 C  CG    . GLU A 1 463 ? 28.552  4.668   23.393  1.00 64.89  ? 463 GLU A CG    1 
ATOM   3572 C  CD    . GLU A 1 463 ? 28.273  3.732   24.555  1.00 71.84  ? 463 GLU A CD    1 
ATOM   3573 O  OE1   . GLU A 1 463 ? 27.511  2.754   24.365  1.00 72.31  ? 463 GLU A OE1   1 
ATOM   3574 O  OE2   . GLU A 1 463 ? 28.821  3.963   25.652  1.00 78.18  ? 463 GLU A OE2   1 
ATOM   3575 N  N     . ALA A 1 464 ? 29.739  3.296   19.300  1.00 57.01  ? 464 ALA A N     1 
ATOM   3576 C  CA    . ALA A 1 464 ? 29.809  2.288   18.249  1.00 59.07  ? 464 ALA A CA    1 
ATOM   3577 C  C     . ALA A 1 464 ? 29.097  1.008   18.687  1.00 60.90  ? 464 ALA A C     1 
ATOM   3578 O  O     . ALA A 1 464 ? 29.004  0.694   19.880  1.00 61.07  ? 464 ALA A O     1 
ATOM   3579 C  CB    . ALA A 1 464 ? 31.266  1.995   17.883  1.00 63.66  ? 464 ALA A CB    1 
ATOM   3580 N  N     . THR A 1 465 ? 28.581  0.268   17.702  1.00 58.75  ? 465 THR A N     1 
ATOM   3581 C  CA    . THR A 1 465 ? 27.825  -0.962  17.923  1.00 53.72  ? 465 THR A CA    1 
ATOM   3582 C  C     . THR A 1 465 ? 28.446  -2.095  17.110  1.00 59.34  ? 465 THR A C     1 
ATOM   3583 O  O     . THR A 1 465 ? 29.457  -1.922  16.419  1.00 57.43  ? 465 THR A O     1 
ATOM   3584 C  CB    . THR A 1 465 ? 26.346  -0.795  17.538  1.00 55.56  ? 465 THR A CB    1 
ATOM   3585 O  OG1   . THR A 1 465 ? 26.243  -0.691  16.108  1.00 52.50  ? 465 THR A OG1   1 
ATOM   3586 C  CG2   . THR A 1 465 ? 25.731  0.482   18.182  1.00 54.03  ? 465 THR A CG2   1 
ATOM   3587 N  N     . ALA A 1 466 ? 27.817  -3.267  17.192  1.00 55.79  ? 466 ALA A N     1 
ATOM   3588 C  CA    . ALA A 1 466 ? 28.283  -4.461  16.499  1.00 54.41  ? 466 ALA A CA    1 
ATOM   3589 C  C     . ALA A 1 466 ? 27.818  -4.540  15.047  1.00 53.00  ? 466 ALA A C     1 
ATOM   3590 O  O     . ALA A 1 466 ? 28.093  -5.542  14.381  1.00 57.23  ? 466 ALA A O     1 
ATOM   3591 C  CB    . ALA A 1 466 ? 27.823  -5.720  17.260  1.00 52.27  ? 466 ALA A CB    1 
ATOM   3592 N  N     . ALA A 1 467 ? 27.123  -3.524  14.529  1.00 56.34  ? 467 ALA A N     1 
ATOM   3593 C  CA    . ALA A 1 467 ? 26.635  -3.621  13.159  1.00 51.81  ? 467 ALA A CA    1 
ATOM   3594 C  C     . ALA A 1 467 ? 27.764  -3.600  12.138  1.00 52.83  ? 467 ALA A C     1 
ATOM   3595 O  O     . ALA A 1 467 ? 27.589  -4.134  11.038  1.00 54.19  ? 467 ALA A O     1 
ATOM   3596 C  CB    . ALA A 1 467 ? 25.652  -2.500  12.864  1.00 49.62  ? 467 ALA A CB    1 
ATOM   3597 N  N     . ALA A 1 468 ? 28.912  -3.030  12.494  1.00 55.55  ? 468 ALA A N     1 
ATOM   3598 C  CA    . ALA A 1 468 ? 30.057  -2.913  11.600  1.00 57.65  ? 468 ALA A CA    1 
ATOM   3599 C  C     . ALA A 1 468 ? 31.289  -3.450  12.330  1.00 59.11  ? 468 ALA A C     1 
ATOM   3600 O  O     . ALA A 1 468 ? 31.198  -4.198  13.311  1.00 62.73  ? 468 ALA A O     1 
ATOM   3601 C  CB    . ALA A 1 468 ? 30.221  -1.459  11.135  1.00 55.85  ? 468 ALA A CB    1 
ATOM   3602 N  N     . GLU A 1 469 ? 32.473  -3.066  11.858  1.00 63.54  ? 469 GLU A N     1 
ATOM   3603 C  CA    . GLU A 1 469 ? 33.724  -3.585  12.401  1.00 68.94  ? 469 GLU A CA    1 
ATOM   3604 C  C     . GLU A 1 469 ? 34.268  -2.755  13.565  1.00 72.55  ? 469 GLU A C     1 
ATOM   3605 O  O     . GLU A 1 469 ? 35.348  -3.064  14.078  1.00 75.95  ? 469 GLU A O     1 
ATOM   3606 C  CB    . GLU A 1 469 ? 34.779  -3.691  11.284  1.00 66.25  ? 469 GLU A CB    1 
ATOM   3607 C  CG    . GLU A 1 469 ? 35.443  -2.370  10.874  1.00 66.67  ? 469 GLU A CG    1 
ATOM   3608 C  CD    . GLU A 1 469 ? 34.726  -1.656  9.737   1.00 63.13  ? 469 GLU A CD    1 
ATOM   3609 O  OE1   . GLU A 1 469 ? 33.474  -1.631  9.731   1.00 58.63  ? 469 GLU A OE1   1 
ATOM   3610 O  OE2   . GLU A 1 469 ? 35.419  -1.114  8.844   1.00 59.81  ? 469 GLU A OE2   1 
ATOM   3611 N  N     . HIS A 1 470 ? 33.541  -1.739  14.021  1.00 77.88  ? 470 HIS A N     1 
ATOM   3612 C  CA    . HIS A 1 470 ? 34.066  -0.827  15.032  1.00 82.18  ? 470 HIS A CA    1 
ATOM   3613 C  C     . HIS A 1 470 ? 33.915  -1.411  16.437  1.00 87.60  ? 470 HIS A C     1 
ATOM   3614 O  O     . HIS A 1 470 ? 32.823  -1.830  16.836  1.00 82.73  ? 470 HIS A O     1 
ATOM   3615 C  CB    . HIS A 1 470 ? 33.361  0.525   14.932  1.00 80.25  ? 470 HIS A CB    1 
ATOM   3616 C  CG    . HIS A 1 470 ? 33.456  1.153   13.574  1.00 75.71  ? 470 HIS A CG    1 
ATOM   3617 N  ND1   . HIS A 1 470 ? 34.642  1.620   13.049  1.00 79.84  ? 470 HIS A ND1   1 
ATOM   3618 C  CD2   . HIS A 1 470 ? 32.513  1.381   12.629  1.00 74.08  ? 470 HIS A CD2   1 
ATOM   3619 C  CE1   . HIS A 1 470 ? 34.426  2.111   11.841  1.00 74.81  ? 470 HIS A CE1   1 
ATOM   3620 N  NE2   . HIS A 1 470 ? 33.142  1.979   11.563  1.00 71.65  ? 470 HIS A NE2   1 
ATOM   3621 N  N     . LYS A 1 471 ? 35.018  -1.429  17.185  1.00 92.91  ? 471 LYS A N     1 
ATOM   3622 C  CA    . LYS A 1 471 ? 35.077  -1.916  18.557  1.00 95.66  ? 471 LYS A CA    1 
ATOM   3623 C  C     . LYS A 1 471 ? 35.312  -0.749  19.518  1.00 101.06 ? 471 LYS A C     1 
ATOM   3624 O  O     . LYS A 1 471 ? 35.523  0.398   19.110  1.00 97.61  ? 471 LYS A O     1 
ATOM   3625 C  CB    . LYS A 1 471 ? 36.185  -2.962  18.706  1.00 94.12  ? 471 LYS A CB    1 
ATOM   3626 C  CG    . LYS A 1 471 ? 36.175  -4.056  17.652  1.00 95.52  ? 471 LYS A CG    1 
ATOM   3627 C  CD    . LYS A 1 471 ? 34.961  -4.956  17.796  1.00 94.72  ? 471 LYS A CD    1 
ATOM   3628 C  CE    . LYS A 1 471 ? 35.043  -6.147  16.853  1.00 93.22  ? 471 LYS A CE    1 
ATOM   3629 N  NZ    . LYS A 1 471 ? 36.199  -7.036  17.173  1.00 101.07 ? 471 LYS A NZ    1 
ATOM   3630 N  N     . GLY A 1 472 ? 35.273  -1.056  20.816  1.00 104.01 ? 472 GLY A N     1 
ATOM   3631 C  CA    . GLY A 1 472 ? 35.686  -0.127  21.848  1.00 107.51 ? 472 GLY A CA    1 
ATOM   3632 C  C     . GLY A 1 472 ? 34.578  0.674   22.505  1.00 103.87 ? 472 GLY A C     1 
ATOM   3633 O  O     . GLY A 1 472 ? 34.827  1.283   23.554  1.00 104.87 ? 472 GLY A O     1 
ATOM   3634 N  N     . LYS A 1 473 ? 33.376  0.702   21.923  1.00 103.77 ? 473 LYS A N     1 
ATOM   3635 C  CA    . LYS A 1 473 ? 32.236  1.481   22.418  1.00 98.46  ? 473 LYS A CA    1 
ATOM   3636 C  C     . LYS A 1 473 ? 32.518  2.986   22.436  1.00 97.79  ? 473 LYS A C     1 
ATOM   3637 O  O     . LYS A 1 473 ? 31.776  3.755   23.059  1.00 97.72  ? 473 LYS A O     1 
ATOM   3638 C  CB    . LYS A 1 473 ? 31.791  1.006   23.810  1.00 100.92 ? 473 LYS A CB    1 
ATOM   3639 C  CG    . LYS A 1 473 ? 30.304  0.657   23.921  1.00 101.04 ? 473 LYS A CG    1 
ATOM   3640 C  CD    . LYS A 1 473 ? 29.949  0.146   25.317  1.00 102.43 ? 473 LYS A CD    1 
ATOM   3641 C  CE    . LYS A 1 473 ? 28.462  -0.178  25.447  1.00 104.66 ? 473 LYS A CE    1 
ATOM   3642 N  NZ    . LYS A 1 473 ? 28.035  -1.312  24.578  1.00 107.23 ? 473 LYS A NZ    1 
ATOM   3643 N  N     . VAL A 1 474 ? 33.577  3.419   21.742  1.00 84.56  ? 474 VAL A N     1 
ATOM   3644 C  CA    . VAL A 1 474 ? 33.938  4.830   21.689  1.00 72.83  ? 474 VAL A CA    1 
ATOM   3645 C  C     . VAL A 1 474 ? 32.818  5.637   21.021  1.00 62.53  ? 474 VAL A C     1 
ATOM   3646 O  O     . VAL A 1 474 ? 31.935  5.089   20.352  1.00 62.29  ? 474 VAL A O     1 
ATOM   3647 C  CB    . VAL A 1 474 ? 35.279  4.973   20.950  1.00 72.99  ? 474 VAL A CB    1 
ATOM   3648 C  CG1   . VAL A 1 474 ? 35.126  5.650   19.586  1.00 62.97  ? 474 VAL A CG1   1 
ATOM   3649 C  CG2   . VAL A 1 474 ? 36.281  5.692   21.815  1.00 71.42  ? 474 VAL A CG2   1 
ATOM   3650 N  N     . ILE A 1 475 ? 32.844  6.955   21.226  1.00 59.86  ? 475 ILE A N     1 
ATOM   3651 C  CA    . ILE A 1 475 ? 31.799  7.841   20.714  1.00 54.60  ? 475 ILE A CA    1 
ATOM   3652 C  C     . ILE A 1 475 ? 32.242  8.423   19.375  1.00 50.87  ? 475 ILE A C     1 
ATOM   3653 O  O     . ILE A 1 475 ? 33.192  9.213   19.306  1.00 51.82  ? 475 ILE A O     1 
ATOM   3654 C  CB    . ILE A 1 475 ? 31.446  8.945   21.723  1.00 51.28  ? 475 ILE A CB    1 
ATOM   3655 C  CG1   . ILE A 1 475 ? 30.722  8.325   22.920  1.00 52.37  ? 475 ILE A CG1   1 
ATOM   3656 C  CG2   . ILE A 1 475 ? 30.563  10.002  21.074  1.00 45.25  ? 475 ILE A CG2   1 
ATOM   3657 C  CD1   . ILE A 1 475 ? 30.287  9.312   23.960  1.00 59.45  ? 475 ILE A CD1   1 
ATOM   3658 N  N     . MET A 1 476 ? 31.522  8.054   18.322  1.00 49.35  ? 476 MET A N     1 
ATOM   3659 C  CA    . MET A 1 476 ? 31.844  8.363   16.938  1.00 45.14  ? 476 MET A CA    1 
ATOM   3660 C  C     . MET A 1 476 ? 30.813  9.312   16.354  1.00 40.19  ? 476 MET A C     1 
ATOM   3661 O  O     . MET A 1 476 ? 29.660  9.357   16.790  1.00 39.29  ? 476 MET A O     1 
ATOM   3662 C  CB    . MET A 1 476 ? 31.864  7.086   16.083  1.00 45.15  ? 476 MET A CB    1 
ATOM   3663 C  CG    . MET A 1 476 ? 32.928  6.094   16.432  1.00 53.88  ? 476 MET A CG    1 
ATOM   3664 S  SD    . MET A 1 476 ? 32.800  4.636   15.367  1.00 66.92  ? 476 MET A SD    1 
ATOM   3665 C  CE    . MET A 1 476 ? 33.335  5.328   13.800  1.00 61.96  ? 476 MET A CE    1 
ATOM   3666 N  N     . HIS A 1 477 ? 31.229  10.045  15.324  1.00 37.74  ? 477 HIS A N     1 
ATOM   3667 C  CA    . HIS A 1 477 ? 30.293  10.871  14.579  1.00 36.40  ? 477 HIS A CA    1 
ATOM   3668 C  C     . HIS A 1 477 ? 29.498  10.002  13.617  1.00 36.62  ? 477 HIS A C     1 
ATOM   3669 O  O     . HIS A 1 477 ? 30.060  9.132   12.948  1.00 40.50  ? 477 HIS A O     1 
ATOM   3670 C  CB    . HIS A 1 477 ? 31.037  11.956  13.812  1.00 39.16  ? 477 HIS A CB    1 
ATOM   3671 C  CG    . HIS A 1 477 ? 31.596  13.027  14.691  1.00 39.39  ? 477 HIS A CG    1 
ATOM   3672 N  ND1   . HIS A 1 477 ? 30.925  14.203  14.938  1.00 36.60  ? 477 HIS A ND1   1 
ATOM   3673 C  CD2   . HIS A 1 477 ? 32.747  13.089  15.402  1.00 39.62  ? 477 HIS A CD2   1 
ATOM   3674 C  CE1   . HIS A 1 477 ? 31.648  14.954  15.750  1.00 40.74  ? 477 HIS A CE1   1 
ATOM   3675 N  NE2   . HIS A 1 477 ? 32.755  14.299  16.051  1.00 41.04  ? 477 HIS A NE2   1 
ATOM   3676 N  N     . ASP A 1 478 ? 28.185  10.232  13.547  1.00 32.85  ? 478 ASP A N     1 
ATOM   3677 C  CA    . ASP A 1 478 ? 27.325  9.506   12.609  1.00 34.25  ? 478 ASP A CA    1 
ATOM   3678 C  C     . ASP A 1 478 ? 26.199  10.416  12.157  1.00 33.80  ? 478 ASP A C     1 
ATOM   3679 O  O     . ASP A 1 478 ? 25.035  10.247  12.548  1.00 32.33  ? 478 ASP A O     1 
ATOM   3680 C  CB    . ASP A 1 478 ? 26.790  8.217   13.241  1.00 36.00  ? 478 ASP A CB    1 
ATOM   3681 C  CG    . ASP A 1 478 ? 26.346  7.195   12.203  1.00 35.16  ? 478 ASP A CG    1 
ATOM   3682 O  OD1   . ASP A 1 478 ? 26.037  7.574   11.047  1.00 36.56  ? 478 ASP A OD1   1 
ATOM   3683 O  OD2   . ASP A 1 478 ? 26.285  6.018   12.556  1.00 32.24  ? 478 ASP A OD2   1 
ATOM   3684 N  N     . PRO A 1 479 ? 26.514  11.401  11.317  1.00 31.58  ? 479 PRO A N     1 
ATOM   3685 C  CA    . PRO A 1 479 ? 25.500  12.385  10.919  1.00 31.02  ? 479 PRO A CA    1 
ATOM   3686 C  C     . PRO A 1 479 ? 24.348  11.713  10.199  1.00 31.21  ? 479 PRO A C     1 
ATOM   3687 O  O     . PRO A 1 479 ? 24.559  10.924  9.279   1.00 30.69  ? 479 PRO A O     1 
ATOM   3688 C  CB    . PRO A 1 479 ? 26.262  13.355  9.989   1.00 31.08  ? 479 PRO A CB    1 
ATOM   3689 C  CG    . PRO A 1 479 ? 27.584  12.777  9.755   1.00 33.82  ? 479 PRO A CG    1 
ATOM   3690 C  CD    . PRO A 1 479 ? 27.845  11.681  10.749  1.00 36.19  ? 479 PRO A CD    1 
ATOM   3691 N  N     . PHE A 1 480 ? 23.124  12.042  10.634  1.00 33.01  ? 480 PHE A N     1 
ATOM   3692 C  CA    . PHE A 1 480 ? 21.873  11.537  10.067  1.00 30.68  ? 480 PHE A CA    1 
ATOM   3693 C  C     . PHE A 1 480 ? 21.768  10.015  10.128  1.00 32.48  ? 480 PHE A C     1 
ATOM   3694 O  O     . PHE A 1 480 ? 20.942  9.409   9.414   1.00 34.71  ? 480 PHE A O     1 
ATOM   3695 C  CB    . PHE A 1 480 ? 21.689  12.017  8.629   1.00 31.03  ? 480 PHE A CB    1 
ATOM   3696 C  CG    . PHE A 1 480 ? 21.395  13.483  8.516   1.00 34.45  ? 480 PHE A CG    1 
ATOM   3697 C  CD1   . PHE A 1 480 ? 22.409  14.419  8.665   1.00 32.18  ? 480 PHE A CD1   1 
ATOM   3698 C  CD2   . PHE A 1 480 ? 20.107  13.924  8.253   1.00 33.52  ? 480 PHE A CD2   1 
ATOM   3699 C  CE1   . PHE A 1 480 ? 22.146  15.763  8.556   1.00 31.46  ? 480 PHE A CE1   1 
ATOM   3700 C  CE2   . PHE A 1 480 ? 19.845  15.280  8.140   1.00 35.12  ? 480 PHE A CE2   1 
ATOM   3701 C  CZ    . PHE A 1 480 ? 20.866  16.192  8.288   1.00 32.62  ? 480 PHE A CZ    1 
ATOM   3702 N  N     . ALA A 1 481 ? 22.591  9.383   10.966  1.00 28.38  ? 481 ALA A N     1 
ATOM   3703 C  CA    . ALA A 1 481 ? 22.726  7.926   11.021  1.00 32.47  ? 481 ALA A CA    1 
ATOM   3704 C  C     . ALA A 1 481 ? 23.204  7.335   9.693   1.00 34.37  ? 481 ALA A C     1 
ATOM   3705 O  O     . ALA A 1 481 ? 23.018  6.131   9.438   1.00 32.46  ? 481 ALA A O     1 
ATOM   3706 C  CB    . ALA A 1 481 ? 21.420  7.257   11.452  1.00 34.36  ? 481 ALA A CB    1 
ATOM   3707 N  N     . MET A 1 482 ? 23.840  8.151   8.855   1.00 33.93  ? 482 MET A N     1 
ATOM   3708 C  CA    . MET A 1 482 ? 24.158  7.788   7.475   1.00 33.95  ? 482 MET A CA    1 
ATOM   3709 C  C     . MET A 1 482 ? 25.651  7.693   7.198   1.00 36.29  ? 482 MET A C     1 
ATOM   3710 O  O     . MET A 1 482 ? 26.036  7.525   6.034   1.00 37.66  ? 482 MET A O     1 
ATOM   3711 C  CB    . MET A 1 482 ? 23.531  8.810   6.516   1.00 35.45  ? 482 MET A CB    1 
ATOM   3712 C  CG    . MET A 1 482 ? 22.012  8.663   6.327   1.00 32.25  ? 482 MET A CG    1 
ATOM   3713 S  SD    . MET A 1 482 ? 21.677  7.343   5.160   1.00 34.99  ? 482 MET A SD    1 
ATOM   3714 C  CE    . MET A 1 482 ? 22.244  8.138   3.648   1.00 35.99  ? 482 MET A CE    1 
ATOM   3715 N  N     . ARG A 1 483 ? 26.508  7.783   8.219   1.00 34.98  ? 483 ARG A N     1 
ATOM   3716 C  CA    . ARG A 1 483 ? 27.948  7.740   7.960   1.00 37.43  ? 483 ARG A CA    1 
ATOM   3717 C  C     . ARG A 1 483 ? 28.368  6.567   7.077   1.00 40.01  ? 483 ARG A C     1 
ATOM   3718 O  O     . ARG A 1 483 ? 29.118  6.798   6.118   1.00 40.60  ? 483 ARG A O     1 
ATOM   3719 C  CB    . ARG A 1 483 ? 28.749  7.724   9.268   1.00 40.66  ? 483 ARG A CB    1 
ATOM   3720 C  CG    . ARG A 1 483 ? 30.243  8.012   9.025   1.00 40.54  ? 483 ARG A CG    1 
ATOM   3721 C  CD    . ARG A 1 483 ? 31.156  7.471   10.114  1.00 44.37  ? 483 ARG A CD    1 
ATOM   3722 N  NE    . ARG A 1 483 ? 30.961  6.040   10.315  1.00 44.85  ? 483 ARG A NE    1 
ATOM   3723 C  CZ    . ARG A 1 483 ? 30.392  5.503   11.387  1.00 47.91  ? 483 ARG A CZ    1 
ATOM   3724 N  NH1   . ARG A 1 483 ? 29.997  6.251   12.404  1.00 47.63  ? 483 ARG A NH1   1 
ATOM   3725 N  NH2   . ARG A 1 483 ? 30.213  4.184   11.437  1.00 47.24  ? 483 ARG A NH2   1 
ATOM   3726 N  N     . PRO A 1 484 ? 27.934  5.319   7.311   1.00 37.58  ? 484 PRO A N     1 
ATOM   3727 C  CA    . PRO A 1 484 ? 28.379  4.214   6.450   1.00 39.32  ? 484 PRO A CA    1 
ATOM   3728 C  C     . PRO A 1 484 ? 27.675  4.144   5.104   1.00 36.84  ? 484 PRO A C     1 
ATOM   3729 O  O     . PRO A 1 484 ? 27.974  3.236   4.316   1.00 39.01  ? 484 PRO A O     1 
ATOM   3730 C  CB    . PRO A 1 484 ? 28.047  2.959   7.289   1.00 39.77  ? 484 PRO A CB    1 
ATOM   3731 C  CG    . PRO A 1 484 ? 27.451  3.466   8.619   1.00 39.00  ? 484 PRO A CG    1 
ATOM   3732 C  CD    . PRO A 1 484 ? 26.992  4.841   8.348   1.00 37.98  ? 484 PRO A CD    1 
ATOM   3733 N  N     . PHE A 1 485 ? 26.760  5.064   4.821   1.00 36.04  ? 485 PHE A N     1 
ATOM   3734 C  CA    . PHE A 1 485 ? 25.800  4.902   3.743   1.00 39.34  ? 485 PHE A CA    1 
ATOM   3735 C  C     . PHE A 1 485 ? 25.720  6.079   2.763   1.00 37.58  ? 485 PHE A C     1 
ATOM   3736 O  O     . PHE A 1 485 ? 24.877  6.041   1.857   1.00 38.36  ? 485 PHE A O     1 
ATOM   3737 C  CB    . PHE A 1 485 ? 24.402  4.641   4.333   1.00 33.22  ? 485 PHE A CB    1 
ATOM   3738 C  CG    . PHE A 1 485 ? 24.356  3.473   5.289   1.00 33.95  ? 485 PHE A CG    1 
ATOM   3739 C  CD1   . PHE A 1 485 ? 24.749  2.214   4.869   1.00 34.82  ? 485 PHE A CD1   1 
ATOM   3740 C  CD2   . PHE A 1 485 ? 23.917  3.635   6.601   1.00 37.88  ? 485 PHE A CD2   1 
ATOM   3741 C  CE1   . PHE A 1 485 ? 24.729  1.103   5.723   1.00 39.00  ? 485 PHE A CE1   1 
ATOM   3742 C  CE2   . PHE A 1 485 ? 23.868  2.521   7.472   1.00 33.68  ? 485 PHE A CE2   1 
ATOM   3743 C  CZ    . PHE A 1 485 ? 24.283  1.256   7.027   1.00 37.87  ? 485 PHE A CZ    1 
ATOM   3744 N  N     . PHE A 1 486 ? 26.553  7.106   2.897   1.00 33.52  ? 486 PHE A N     1 
ATOM   3745 C  CA    . PHE A 1 486 ? 26.457  8.233   1.964   1.00 38.36  ? 486 PHE A CA    1 
ATOM   3746 C  C     . PHE A 1 486 ? 26.844  7.784   0.563   1.00 34.03  ? 486 PHE A C     1 
ATOM   3747 O  O     . PHE A 1 486 ? 27.897  7.179   0.372   1.00 37.60  ? 486 PHE A O     1 
ATOM   3748 C  CB    . PHE A 1 486 ? 27.347  9.408   2.393   1.00 38.01  ? 486 PHE A CB    1 
ATOM   3749 C  CG    . PHE A 1 486 ? 26.861  10.109  3.612   1.00 30.76  ? 486 PHE A CG    1 
ATOM   3750 C  CD1   . PHE A 1 486 ? 25.615  10.717  3.623   1.00 34.10  ? 486 PHE A CD1   1 
ATOM   3751 C  CD2   . PHE A 1 486 ? 27.627  10.139  4.765   1.00 33.71  ? 486 PHE A CD2   1 
ATOM   3752 C  CE1   . PHE A 1 486 ? 25.148  11.348  4.752   1.00 34.64  ? 486 PHE A CE1   1 
ATOM   3753 C  CE2   . PHE A 1 486 ? 27.161  10.776  5.904   1.00 34.34  ? 486 PHE A CE2   1 
ATOM   3754 C  CZ    . PHE A 1 486 ? 25.926  11.374  5.901   1.00 33.94  ? 486 PHE A CZ    1 
ATOM   3755 N  N     . GLY A 1 487 ? 25.972  8.045   -0.412  1.00 35.28  ? 487 GLY A N     1 
ATOM   3756 C  CA    . GLY A 1 487 ? 26.307  7.787   -1.802  1.00 36.46  ? 487 GLY A CA    1 
ATOM   3757 C  C     . GLY A 1 487 ? 27.102  8.879   -2.487  1.00 42.61  ? 487 GLY A C     1 
ATOM   3758 O  O     . GLY A 1 487 ? 27.541  8.681   -3.625  1.00 40.43  ? 487 GLY A O     1 
ATOM   3759 N  N     . TYR A 1 488 ? 27.285  10.025  -1.829  1.00 38.99  ? 488 TYR A N     1 
ATOM   3760 C  CA    . TYR A 1 488 ? 27.921  11.179  -2.456  1.00 40.64  ? 488 TYR A CA    1 
ATOM   3761 C  C     . TYR A 1 488 ? 28.360  12.163  -1.373  1.00 38.79  ? 488 TYR A C     1 
ATOM   3762 O  O     . TYR A 1 488 ? 28.117  11.960  -0.181  1.00 36.25  ? 488 TYR A O     1 
ATOM   3763 C  CB    . TYR A 1 488 ? 26.975  11.834  -3.474  1.00 40.56  ? 488 TYR A CB    1 
ATOM   3764 C  CG    . TYR A 1 488 ? 25.731  12.459  -2.859  1.00 39.25  ? 488 TYR A CG    1 
ATOM   3765 C  CD1   . TYR A 1 488 ? 24.669  11.666  -2.412  1.00 36.63  ? 488 TYR A CD1   1 
ATOM   3766 C  CD2   . TYR A 1 488 ? 25.623  13.839  -2.720  1.00 39.20  ? 488 TYR A CD2   1 
ATOM   3767 C  CE1   . TYR A 1 488 ? 23.536  12.242  -1.849  1.00 37.83  ? 488 TYR A CE1   1 
ATOM   3768 C  CE2   . TYR A 1 488 ? 24.494  14.427  -2.161  1.00 36.33  ? 488 TYR A CE2   1 
ATOM   3769 C  CZ    . TYR A 1 488 ? 23.454  13.628  -1.726  1.00 38.33  ? 488 TYR A CZ    1 
ATOM   3770 O  OH    . TYR A 1 488 ? 22.345  14.219  -1.175  1.00 37.61  ? 488 TYR A OH    1 
ATOM   3771 N  N     . ASN A 1 489 ? 29.002  13.247  -1.819  1.00 37.72  ? 489 ASN A N     1 
ATOM   3772 C  CA    . ASN A 1 489 ? 29.599  14.282  -0.976  1.00 40.06  ? 489 ASN A CA    1 
ATOM   3773 C  C     . ASN A 1 489 ? 28.638  14.736  0.121   1.00 38.18  ? 489 ASN A C     1 
ATOM   3774 O  O     . ASN A 1 489 ? 27.548  15.243  -0.165  1.00 36.65  ? 489 ASN A O     1 
ATOM   3775 C  CB    . ASN A 1 489 ? 30.005  15.460  -1.885  1.00 38.43  ? 489 ASN A CB    1 
ATOM   3776 C  CG    . ASN A 1 489 ? 30.831  16.534  -1.172  1.00 41.59  ? 489 ASN A CG    1 
ATOM   3777 O  OD1   . ASN A 1 489 ? 30.433  17.063  -0.141  1.00 40.85  ? 489 ASN A OD1   1 
ATOM   3778 N  ND2   . ASN A 1 489 ? 31.975  16.884  -1.756  1.00 40.39  ? 489 ASN A ND2   1 
ATOM   3779 N  N     . PHE A 1 490 ? 29.048  14.531  1.381   1.00 36.82  ? 490 PHE A N     1 
ATOM   3780 C  CA    . PHE A 1 490 ? 28.197  14.840  2.528   1.00 34.85  ? 490 PHE A CA    1 
ATOM   3781 C  C     . PHE A 1 490 ? 27.883  16.331  2.624   1.00 35.95  ? 490 PHE A C     1 
ATOM   3782 O  O     . PHE A 1 490 ? 26.806  16.705  3.098   1.00 33.01  ? 490 PHE A O     1 
ATOM   3783 C  CB    . PHE A 1 490 ? 28.873  14.346  3.809   1.00 36.80  ? 490 PHE A CB    1 
ATOM   3784 C  CG    . PHE A 1 490 ? 28.214  14.810  5.086   1.00 35.32  ? 490 PHE A CG    1 
ATOM   3785 C  CD1   . PHE A 1 490 ? 26.871  14.560  5.329   1.00 32.52  ? 490 PHE A CD1   1 
ATOM   3786 C  CD2   . PHE A 1 490 ? 28.957  15.487  6.050   1.00 36.94  ? 490 PHE A CD2   1 
ATOM   3787 C  CE1   . PHE A 1 490 ? 26.267  14.970  6.514   1.00 34.62  ? 490 PHE A CE1   1 
ATOM   3788 C  CE2   . PHE A 1 490 ? 28.370  15.901  7.237   1.00 36.80  ? 490 PHE A CE2   1 
ATOM   3789 C  CZ    . PHE A 1 490 ? 27.014  15.641  7.471   1.00 34.21  ? 490 PHE A CZ    1 
ATOM   3790 N  N     . GLY A 1 491 ? 28.806  17.195  2.191   1.00 37.90  ? 491 GLY A N     1 
ATOM   3791 C  CA    . GLY A 1 491 ? 28.500  18.620  2.155   1.00 37.39  ? 491 GLY A CA    1 
ATOM   3792 C  C     . GLY A 1 491 ? 27.363  18.932  1.201   1.00 38.09  ? 491 GLY A C     1 
ATOM   3793 O  O     . GLY A 1 491 ? 26.479  19.737  1.509   1.00 37.49  ? 491 GLY A O     1 
ATOM   3794 N  N     . LYS A 1 492 ? 27.364  18.286  0.032   1.00 37.30  ? 492 LYS A N     1 
ATOM   3795 C  CA    . LYS A 1 492 ? 26.254  18.435  -0.904  1.00 37.24  ? 492 LYS A CA    1 
ATOM   3796 C  C     . LYS A 1 492 ? 24.970  17.841  -0.341  1.00 36.21  ? 492 LYS A C     1 
ATOM   3797 O  O     . LYS A 1 492 ? 23.875  18.327  -0.635  1.00 35.51  ? 492 LYS A O     1 
ATOM   3798 C  CB    . LYS A 1 492 ? 26.597  17.777  -2.239  1.00 36.26  ? 492 LYS A CB    1 
ATOM   3799 C  CG    . LYS A 1 492 ? 27.826  18.383  -2.960  1.00 39.58  ? 492 LYS A CG    1 
ATOM   3800 C  CD    . LYS A 1 492 ? 27.852  19.902  -2.816  1.00 40.81  ? 492 LYS A CD    1 
ATOM   3801 C  CE    . LYS A 1 492 ? 29.070  20.536  -3.509  1.00 52.12  ? 492 LYS A CE    1 
ATOM   3802 N  NZ    . LYS A 1 492 ? 29.433  21.829  -2.838  1.00 56.01  ? 492 LYS A NZ    1 
ATOM   3803 N  N     . TYR A 1 493 ? 25.086  16.794  0.466   1.00 32.26  ? 493 TYR A N     1 
ATOM   3804 C  CA    . TYR A 1 493 ? 23.904  16.197  1.077   1.00 36.49  ? 493 TYR A CA    1 
ATOM   3805 C  C     . TYR A 1 493 ? 23.250  17.171  2.054   1.00 33.50  ? 493 TYR A C     1 
ATOM   3806 O  O     . TYR A 1 493 ? 22.022  17.299  2.079   1.00 35.16  ? 493 TYR A O     1 
ATOM   3807 C  CB    . TYR A 1 493 ? 24.314  14.872  1.736   1.00 33.81  ? 493 TYR A CB    1 
ATOM   3808 C  CG    . TYR A 1 493 ? 23.338  14.206  2.698   1.00 34.22  ? 493 TYR A CG    1 
ATOM   3809 C  CD1   . TYR A 1 493 ? 23.205  14.648  4.010   1.00 32.13  ? 493 TYR A CD1   1 
ATOM   3810 C  CD2   . TYR A 1 493 ? 22.622  13.062  2.318   1.00 33.18  ? 493 TYR A CD2   1 
ATOM   3811 C  CE1   . TYR A 1 493 ? 22.345  14.015  4.898   1.00 30.48  ? 493 TYR A CE1   1 
ATOM   3812 C  CE2   . TYR A 1 493 ? 21.749  12.416  3.216   1.00 32.12  ? 493 TYR A CE2   1 
ATOM   3813 C  CZ    . TYR A 1 493 ? 21.620  12.904  4.503   1.00 34.98  ? 493 TYR A CZ    1 
ATOM   3814 O  OH    . TYR A 1 493 ? 20.757  12.263  5.404   1.00 30.72  ? 493 TYR A OH    1 
ATOM   3815 N  N     . LEU A 1 494 ? 24.056  17.880  2.849   1.00 36.03  ? 494 LEU A N     1 
ATOM   3816 C  CA    . LEU A 1 494 ? 23.536  18.931  3.727   1.00 33.67  ? 494 LEU A CA    1 
ATOM   3817 C  C     . LEU A 1 494 ? 22.821  20.028  2.943   1.00 35.19  ? 494 LEU A C     1 
ATOM   3818 O  O     . LEU A 1 494 ? 21.747  20.490  3.347   1.00 33.70  ? 494 LEU A O     1 
ATOM   3819 C  CB    . LEU A 1 494 ? 24.677  19.533  4.546   1.00 32.85  ? 494 LEU A CB    1 
ATOM   3820 C  CG    . LEU A 1 494 ? 25.328  18.568  5.534   1.00 35.01  ? 494 LEU A CG    1 
ATOM   3821 C  CD1   . LEU A 1 494 ? 26.563  19.216  6.171   1.00 35.74  ? 494 LEU A CD1   1 
ATOM   3822 C  CD2   . LEU A 1 494 ? 24.314  18.191  6.582   1.00 29.64  ? 494 LEU A CD2   1 
ATOM   3823 N  N     . ALA A 1 495 ? 23.408  20.472  1.827   1.00 35.20  ? 495 ALA A N     1 
ATOM   3824 C  CA    . ALA A 1 495 ? 22.781  21.534  1.039   1.00 37.17  ? 495 ALA A CA    1 
ATOM   3825 C  C     . ALA A 1 495 ? 21.475  21.054  0.419   1.00 39.38  ? 495 ALA A C     1 
ATOM   3826 O  O     . ALA A 1 495 ? 20.516  21.827  0.314   1.00 39.95  ? 495 ALA A O     1 
ATOM   3827 C  CB    . ALA A 1 495 ? 23.747  22.041  -0.038  1.00 38.79  ? 495 ALA A CB    1 
ATOM   3828 N  N     . HIS A 1 496 ? 21.408  19.771  0.052   1.00 36.79  ? 496 HIS A N     1 
ATOM   3829 C  CA    . HIS A 1 496 ? 20.166  19.181  -0.435  1.00 37.90  ? 496 HIS A CA    1 
ATOM   3830 C  C     . HIS A 1 496 ? 19.076  19.245  0.637   1.00 37.55  ? 496 HIS A C     1 
ATOM   3831 O  O     . HIS A 1 496 ? 17.953  19.702  0.378   1.00 37.15  ? 496 HIS A O     1 
ATOM   3832 C  CB    . HIS A 1 496 ? 20.458  17.744  -0.875  1.00 35.89  ? 496 HIS A CB    1 
ATOM   3833 C  CG    . HIS A 1 496 ? 19.324  17.055  -1.567  1.00 41.61  ? 496 HIS A CG    1 
ATOM   3834 N  ND1   . HIS A 1 496 ? 18.707  17.563  -2.693  1.00 39.17  ? 496 HIS A ND1   1 
ATOM   3835 C  CD2   . HIS A 1 496 ? 18.723  15.867  -1.311  1.00 35.60  ? 496 HIS A CD2   1 
ATOM   3836 C  CE1   . HIS A 1 496 ? 17.764  16.724  -3.088  1.00 40.33  ? 496 HIS A CE1   1 
ATOM   3837 N  NE2   . HIS A 1 496 ? 17.754  15.687  -2.267  1.00 37.53  ? 496 HIS A NE2   1 
ATOM   3838 N  N     . TRP A 1 497 ? 19.402  18.822  1.860   1.00 33.20  ? 497 TRP A N     1 
ATOM   3839 C  CA    . TRP A 1 497 ? 18.456  18.930  2.969   1.00 35.27  ? 497 TRP A CA    1 
ATOM   3840 C  C     . TRP A 1 497 ? 18.029  20.371  3.206   1.00 38.15  ? 497 TRP A C     1 
ATOM   3841 O  O     . TRP A 1 497 ? 16.839  20.651  3.385   1.00 36.45  ? 497 TRP A O     1 
ATOM   3842 C  CB    . TRP A 1 497 ? 19.062  18.355  4.248   1.00 31.75  ? 497 TRP A CB    1 
ATOM   3843 C  CG    . TRP A 1 497 ? 18.758  16.892  4.441   1.00 33.93  ? 497 TRP A CG    1 
ATOM   3844 C  CD1   . TRP A 1 497 ? 19.418  15.835  3.886   1.00 33.42  ? 497 TRP A CD1   1 
ATOM   3845 C  CD2   . TRP A 1 497 ? 17.700  16.335  5.238   1.00 31.88  ? 497 TRP A CD2   1 
ATOM   3846 N  NE1   . TRP A 1 497 ? 18.836  14.644  4.297   1.00 32.39  ? 497 TRP A NE1   1 
ATOM   3847 C  CE2   . TRP A 1 497 ? 17.784  14.929  5.127   1.00 34.21  ? 497 TRP A CE2   1 
ATOM   3848 C  CE3   . TRP A 1 497 ? 16.703  16.890  6.051   1.00 33.76  ? 497 TRP A CE3   1 
ATOM   3849 C  CZ2   . TRP A 1 497 ? 16.899  14.067  5.799   1.00 37.20  ? 497 TRP A CZ2   1 
ATOM   3850 C  CZ3   . TRP A 1 497 ? 15.825  16.038  6.711   1.00 37.15  ? 497 TRP A CZ3   1 
ATOM   3851 C  CH2   . TRP A 1 497 ? 15.929  14.641  6.577   1.00 36.47  ? 497 TRP A CH2   1 
ATOM   3852 N  N     . LEU A 1 498 ? 18.994  21.299  3.236   1.00 36.08  ? 498 LEU A N     1 
ATOM   3853 C  CA    . LEU A 1 498 ? 18.651  22.689  3.522   1.00 39.08  ? 498 LEU A CA    1 
ATOM   3854 C  C     . LEU A 1 498 ? 17.770  23.277  2.433   1.00 42.52  ? 498 LEU A C     1 
ATOM   3855 O  O     . LEU A 1 498 ? 16.903  24.106  2.725   1.00 43.09  ? 498 LEU A O     1 
ATOM   3856 C  CB    . LEU A 1 498 ? 19.913  23.533  3.693   1.00 40.23  ? 498 LEU A CB    1 
ATOM   3857 C  CG    . LEU A 1 498 ? 20.747  23.263  4.946   1.00 36.72  ? 498 LEU A CG    1 
ATOM   3858 C  CD1   . LEU A 1 498 ? 22.155  23.788  4.752   1.00 37.29  ? 498 LEU A CD1   1 
ATOM   3859 C  CD2   . LEU A 1 498 ? 20.116  23.882  6.191   1.00 35.72  ? 498 LEU A CD2   1 
ATOM   3860 N  N     . SER A 1 499 ? 17.956  22.839  1.184   1.00 41.16  ? 499 SER A N     1 
ATOM   3861 C  CA    . SER A 1 499 ? 17.187  23.387  0.072   1.00 45.12  ? 499 SER A CA    1 
ATOM   3862 C  C     . SER A 1 499 ? 15.702  23.087  0.190   1.00 46.92  ? 499 SER A C     1 
ATOM   3863 O  O     . SER A 1 499 ? 14.891  23.772  -0.444  1.00 51.26  ? 499 SER A O     1 
ATOM   3864 C  CB    . SER A 1 499 ? 17.708  22.836  -1.259  1.00 42.78  ? 499 SER A CB    1 
ATOM   3865 O  OG    . SER A 1 499 ? 17.402  21.450  -1.386  1.00 45.14  ? 499 SER A OG    1 
ATOM   3866 N  N     A MET A 1 500 ? 15.328  22.079  0.984   0.50 45.46  ? 500 MET A N     1 
ATOM   3867 N  N     B MET A 1 500 ? 15.320  22.084  0.980   0.50 45.98  ? 500 MET A N     1 
ATOM   3868 C  CA    A MET A 1 500 ? 13.921  21.713  1.108   0.50 46.20  ? 500 MET A CA    1 
ATOM   3869 C  CA    B MET A 1 500 ? 13.907  21.739  1.084   0.50 46.20  ? 500 MET A CA    1 
ATOM   3870 C  C     A MET A 1 500 ? 13.086  22.858  1.671   0.50 48.52  ? 500 MET A C     1 
ATOM   3871 C  C     B MET A 1 500 ? 13.083  22.882  1.654   0.50 48.52  ? 500 MET A C     1 
ATOM   3872 O  O     A MET A 1 500 ? 11.892  22.960  1.368   0.50 51.54  ? 500 MET A O     1 
ATOM   3873 O  O     B MET A 1 500 ? 11.893  23.003  1.343   0.50 51.60  ? 500 MET A O     1 
ATOM   3874 C  CB    A MET A 1 500 ? 13.780  20.461  1.978   0.50 45.71  ? 500 MET A CB    1 
ATOM   3875 C  CB    B MET A 1 500 ? 13.743  20.489  1.936   0.50 45.28  ? 500 MET A CB    1 
ATOM   3876 C  CG    A MET A 1 500 ? 14.412  19.199  1.386   0.50 44.93  ? 500 MET A CG    1 
ATOM   3877 C  CG    B MET A 1 500 ? 14.028  19.223  1.179   0.50 45.09  ? 500 MET A CG    1 
ATOM   3878 S  SD    A MET A 1 500 ? 13.790  18.767  -0.257  0.50 45.94  ? 500 MET A SD    1 
ATOM   3879 S  SD    B MET A 1 500 ? 13.794  17.826  2.257   0.50 52.11  ? 500 MET A SD    1 
ATOM   3880 C  CE    A MET A 1 500 ? 14.946  17.489  -0.737  0.50 46.29  ? 500 MET A CE    1 
ATOM   3881 C  CE    B MET A 1 500 ? 15.173  18.009  3.336   0.50 37.15  ? 500 MET A CE    1 
ATOM   3882 N  N     . ALA A 1 501 ? 13.693  23.735  2.475   1.00 46.91  ? 501 ALA A N     1 
ATOM   3883 C  CA    . ALA A 1 501 ? 12.982  24.888  3.014   1.00 52.65  ? 501 ALA A CA    1 
ATOM   3884 C  C     . ALA A 1 501 ? 12.723  25.964  1.968   1.00 58.86  ? 501 ALA A C     1 
ATOM   3885 O  O     . ALA A 1 501 ? 12.044  26.947  2.278   1.00 61.66  ? 501 ALA A O     1 
ATOM   3886 C  CB    . ALA A 1 501 ? 13.762  25.490  4.182   1.00 51.33  ? 501 ALA A CB    1 
ATOM   3887 N  N     . HIS A 1 502 ? 13.258  25.814  0.755   1.00 64.29  ? 502 HIS A N     1 
ATOM   3888 C  CA    . HIS A 1 502 ? 12.977  26.723  -0.348  1.00 67.37  ? 502 HIS A CA    1 
ATOM   3889 C  C     . HIS A 1 502 ? 11.818  26.259  -1.223  1.00 70.84  ? 502 HIS A C     1 
ATOM   3890 O  O     . HIS A 1 502 ? 11.424  26.994  -2.133  1.00 83.29  ? 502 HIS A O     1 
ATOM   3891 C  CB    . HIS A 1 502 ? 14.217  26.901  -1.241  1.00 71.38  ? 502 HIS A CB    1 
ATOM   3892 C  CG    . HIS A 1 502 ? 15.458  27.291  -0.498  1.00 76.31  ? 502 HIS A CG    1 
ATOM   3893 N  ND1   . HIS A 1 502 ? 16.723  27.078  -1.005  1.00 79.03  ? 502 HIS A ND1   1 
ATOM   3894 C  CD2   . HIS A 1 502 ? 15.631  27.881  0.709   1.00 73.93  ? 502 HIS A CD2   1 
ATOM   3895 C  CE1   . HIS A 1 502 ? 17.621  27.515  -0.141  1.00 76.49  ? 502 HIS A CE1   1 
ATOM   3896 N  NE2   . HIS A 1 502 ? 16.985  28.008  0.907   1.00 80.60  ? 502 HIS A NE2   1 
ATOM   3897 N  N     . ARG A 1 503 ? 11.276  25.070  -0.984  1.00 68.45  ? 503 ARG A N     1 
ATOM   3898 C  CA    . ARG A 1 503 ? 10.227  24.549  -1.846  1.00 73.74  ? 503 ARG A CA    1 
ATOM   3899 C  C     . ARG A 1 503 ? 8.908   25.269  -1.577  1.00 81.88  ? 503 ARG A C     1 
ATOM   3900 O  O     . ARG A 1 503 ? 8.586   25.566  -0.419  1.00 74.89  ? 503 ARG A O     1 
ATOM   3901 C  CB    . ARG A 1 503 ? 10.045  23.048  -1.636  1.00 73.88  ? 503 ARG A CB    1 
ATOM   3902 C  CG    . ARG A 1 503 ? 11.205  22.214  -2.126  1.00 71.75  ? 503 ARG A CG    1 
ATOM   3903 C  CD    . ARG A 1 503 ? 10.713  20.902  -2.699  1.00 76.40  ? 503 ARG A CD    1 
ATOM   3904 N  NE    . ARG A 1 503 ? 11.797  20.150  -3.318  1.00 84.75  ? 503 ARG A NE    1 
ATOM   3905 C  CZ    . ARG A 1 503 ? 11.642  18.996  -3.953  1.00 84.77  ? 503 ARG A CZ    1 
ATOM   3906 N  NH1   . ARG A 1 503 ? 10.451  18.433  -4.081  1.00 84.68  ? 503 ARG A NH1   1 
ATOM   3907 N  NH2   . ARG A 1 503 ? 12.709  18.393  -4.469  1.00 82.66  ? 503 ARG A NH2   1 
ATOM   3908 N  N     . PRO A 1 504 ? 8.119   25.549  -2.619  1.00 89.69  ? 504 PRO A N     1 
ATOM   3909 C  CA    . PRO A 1 504 ? 6.855   26.266  -2.416  1.00 90.04  ? 504 PRO A CA    1 
ATOM   3910 C  C     . PRO A 1 504 ? 5.825   25.386  -1.725  1.00 91.44  ? 504 PRO A C     1 
ATOM   3911 O  O     . PRO A 1 504 ? 5.647   24.214  -2.069  1.00 90.49  ? 504 PRO A O     1 
ATOM   3912 C  CB    . PRO A 1 504 ? 6.411   26.627  -3.842  1.00 91.73  ? 504 PRO A CB    1 
ATOM   3913 C  CG    . PRO A 1 504 ? 7.577   26.296  -4.740  1.00 93.01  ? 504 PRO A CG    1 
ATOM   3914 C  CD    . PRO A 1 504 ? 8.342   25.220  -4.036  1.00 89.95  ? 504 PRO A CD    1 
ATOM   3915 N  N     . ALA A 1 505 ? 5.147   25.969  -0.735  1.00 79.18  ? 505 ALA A N     1 
ATOM   3916 C  CA    . ALA A 1 505 ? 4.103   25.298  0.038   1.00 73.68  ? 505 ALA A CA    1 
ATOM   3917 C  C     . ALA A 1 505 ? 4.622   24.071  0.781   1.00 65.30  ? 505 ALA A C     1 
ATOM   3918 O  O     . ALA A 1 505 ? 3.829   23.225  1.205   1.00 62.87  ? 505 ALA A O     1 
ATOM   3919 C  CB    . ALA A 1 505 ? 2.912   24.908  -0.847  1.00 73.51  ? 505 ALA A CB    1 
ATOM   3920 N  N     . ALA A 1 506 ? 5.941   23.959  0.954   1.00 65.02  ? 506 ALA A N     1 
ATOM   3921 C  CA    . ALA A 1 506 ? 6.516   22.825  1.669   1.00 61.92  ? 506 ALA A CA    1 
ATOM   3922 C  C     . ALA A 1 506 ? 6.098   22.854  3.131   1.00 54.66  ? 506 ALA A C     1 
ATOM   3923 O  O     . ALA A 1 506 ? 6.369   23.824  3.846   1.00 52.40  ? 506 ALA A O     1 
ATOM   3924 C  CB    . ALA A 1 506 ? 8.040   22.835  1.552   1.00 59.73  ? 506 ALA A CB    1 
ATOM   3925 N  N     . LYS A 1 507 ? 5.420   21.795  3.570   1.00 52.82  ? 507 LYS A N     1 
ATOM   3926 C  CA    . LYS A 1 507 ? 5.060   21.622  4.977   1.00 48.73  ? 507 LYS A CA    1 
ATOM   3927 C  C     . LYS A 1 507 ? 6.211   20.890  5.650   1.00 45.14  ? 507 LYS A C     1 
ATOM   3928 O  O     . LYS A 1 507 ? 6.242   19.664  5.705   1.00 41.44  ? 507 LYS A O     1 
ATOM   3929 C  CB    . LYS A 1 507 ? 3.751   20.854  5.115   1.00 50.55  ? 507 LYS A CB    1 
ATOM   3930 C  CG    . LYS A 1 507 ? 2.564   21.531  4.455   1.00 55.17  ? 507 LYS A CG    1 
ATOM   3931 C  CD    . LYS A 1 507 ? 1.389   20.570  4.304   1.00 59.54  ? 507 LYS A CD    1 
ATOM   3932 C  CE    . LYS A 1 507 ? 0.271   21.207  3.491   1.00 59.52  ? 507 LYS A CE    1 
ATOM   3933 N  NZ    . LYS A 1 507 ? -0.861  20.259  3.278   1.00 67.49  ? 507 LYS A NZ    1 
ATOM   3934 N  N     . LEU A 1 508 ? 7.173   21.646  6.160   1.00 43.72  ? 508 LEU A N     1 
ATOM   3935 C  CA    . LEU A 1 508 ? 8.353   21.029  6.763   1.00 41.19  ? 508 LEU A CA    1 
ATOM   3936 C  C     . LEU A 1 508 ? 7.989   20.367  8.091   1.00 41.38  ? 508 LEU A C     1 
ATOM   3937 O  O     . LEU A 1 508 ? 7.320   20.982  8.919   1.00 41.85  ? 508 LEU A O     1 
ATOM   3938 C  CB    . LEU A 1 508 ? 9.438   22.074  6.974   1.00 39.30  ? 508 LEU A CB    1 
ATOM   3939 C  CG    . LEU A 1 508 ? 9.873   22.816  5.709   1.00 42.61  ? 508 LEU A CG    1 
ATOM   3940 C  CD1   . LEU A 1 508 ? 10.752  24.002  6.061   1.00 39.55  ? 508 LEU A CD1   1 
ATOM   3941 C  CD2   . LEU A 1 508 ? 10.589  21.857  4.778   1.00 41.84  ? 508 LEU A CD2   1 
ATOM   3942 N  N     . PRO A 1 509 ? 8.406   19.130  8.332   1.00 39.72  ? 509 PRO A N     1 
ATOM   3943 C  CA    . PRO A 1 509 ? 8.126   18.501  9.629   1.00 38.66  ? 509 PRO A CA    1 
ATOM   3944 C  C     . PRO A 1 509 ? 8.964   19.099  10.755  1.00 38.74  ? 509 PRO A C     1 
ATOM   3945 O  O     . PRO A 1 509 ? 10.035  19.674  10.542  1.00 35.99  ? 509 PRO A O     1 
ATOM   3946 C  CB    . PRO A 1 509 ? 8.481   17.028  9.390   1.00 35.96  ? 509 PRO A CB    1 
ATOM   3947 C  CG    . PRO A 1 509 ? 9.485   17.061  8.271   1.00 38.65  ? 509 PRO A CG    1 
ATOM   3948 C  CD    . PRO A 1 509 ? 9.057   18.208  7.387   1.00 37.07  ? 509 PRO A CD    1 
ATOM   3949 N  N     . LYS A 1 510 ? 8.438   18.965  11.975  1.00 36.54  ? 510 LYS A N     1 
ATOM   3950 C  CA    . LYS A 1 510 ? 9.216   19.240  13.177  1.00 34.36  ? 510 LYS A CA    1 
ATOM   3951 C  C     . LYS A 1 510 ? 10.376  18.254  13.296  1.00 36.36  ? 510 LYS A C     1 
ATOM   3952 O  O     . LYS A 1 510 ? 10.278  17.087  12.894  1.00 34.98  ? 510 LYS A O     1 
ATOM   3953 C  CB    . LYS A 1 510 ? 8.326   19.142  14.420  1.00 33.59  ? 510 LYS A CB    1 
ATOM   3954 C  CG    . LYS A 1 510 ? 7.897   20.480  15.010  1.00 43.52  ? 510 LYS A CG    1 
ATOM   3955 C  CD    . LYS A 1 510 ? 6.854   20.251  16.100  1.00 41.30  ? 510 LYS A CD    1 
ATOM   3956 C  CE    . LYS A 1 510 ? 6.732   21.433  17.041  1.00 51.31  ? 510 LYS A CE    1 
ATOM   3957 N  NZ    . LYS A 1 510 ? 6.621   22.734  16.352  1.00 44.62  ? 510 LYS A NZ    1 
ATOM   3958 N  N     . ILE A 1 511 ? 11.487  18.720  13.864  1.00 34.55  ? 511 ILE A N     1 
ATOM   3959 C  CA    . ILE A 1 511 ? 12.662  17.879  14.072  1.00 31.31  ? 511 ILE A CA    1 
ATOM   3960 C  C     . ILE A 1 511 ? 12.947  17.791  15.566  1.00 33.29  ? 511 ILE A C     1 
ATOM   3961 O  O     . ILE A 1 511 ? 12.989  18.817  16.261  1.00 34.06  ? 511 ILE A O     1 
ATOM   3962 C  CB    . ILE A 1 511 ? 13.885  18.401  13.295  1.00 33.94  ? 511 ILE A CB    1 
ATOM   3963 C  CG1   . ILE A 1 511 ? 13.691  18.126  11.803  1.00 35.79  ? 511 ILE A CG1   1 
ATOM   3964 C  CG2   . ILE A 1 511 ? 15.175  17.738  13.793  1.00 28.26  ? 511 ILE A CG2   1 
ATOM   3965 C  CD1   . ILE A 1 511 ? 14.729  18.795  10.880  1.00 33.73  ? 511 ILE A CD1   1 
ATOM   3966 N  N     . PHE A 1 512 ? 13.094  16.561  16.053  1.00 29.71  ? 512 PHE A N     1 
ATOM   3967 C  CA    . PHE A 1 512 ? 13.389  16.226  17.439  1.00 32.81  ? 512 PHE A CA    1 
ATOM   3968 C  C     . PHE A 1 512 ? 14.690  15.438  17.513  1.00 34.76  ? 512 PHE A C     1 
ATOM   3969 O  O     . PHE A 1 512 ? 15.083  14.772  16.550  1.00 33.46  ? 512 PHE A O     1 
ATOM   3970 C  CB    . PHE A 1 512 ? 12.270  15.362  18.065  1.00 32.19  ? 512 PHE A CB    1 
ATOM   3971 C  CG    . PHE A 1 512 ? 10.909  15.993  18.014  1.00 31.73  ? 512 PHE A CG    1 
ATOM   3972 C  CD1   . PHE A 1 512 ? 10.511  16.897  18.987  1.00 32.60  ? 512 PHE A CD1   1 
ATOM   3973 C  CD2   . PHE A 1 512 ? 10.030  15.693  16.985  1.00 33.04  ? 512 PHE A CD2   1 
ATOM   3974 C  CE1   . PHE A 1 512 ? 9.256   17.508  18.931  1.00 34.32  ? 512 PHE A CE1   1 
ATOM   3975 C  CE2   . PHE A 1 512 ? 8.772   16.291  16.920  1.00 32.71  ? 512 PHE A CE2   1 
ATOM   3976 C  CZ    . PHE A 1 512 ? 8.381   17.205  17.903  1.00 34.48  ? 512 PHE A CZ    1 
ATOM   3977 N  N     . HIS A 1 513 ? 15.336  15.490  18.683  1.00 31.08  ? 513 HIS A N     1 
ATOM   3978 C  CA    . HIS A 1 513 ? 16.466  14.625  19.006  1.00 31.59  ? 513 HIS A CA    1 
ATOM   3979 C  C     . HIS A 1 513 ? 16.206  13.957  20.348  1.00 33.19  ? 513 HIS A C     1 
ATOM   3980 O  O     . HIS A 1 513 ? 15.806  14.630  21.308  1.00 30.58  ? 513 HIS A O     1 
ATOM   3981 C  CB    . HIS A 1 513 ? 17.781  15.428  19.034  1.00 31.78  ? 513 HIS A CB    1 
ATOM   3982 C  CG    . HIS A 1 513 ? 19.015  14.595  19.246  1.00 32.02  ? 513 HIS A CG    1 
ATOM   3983 N  ND1   . HIS A 1 513 ? 19.394  14.122  20.488  1.00 31.87  ? 513 HIS A ND1   1 
ATOM   3984 C  CD2   . HIS A 1 513 ? 19.973  14.181  18.379  1.00 30.54  ? 513 HIS A CD2   1 
ATOM   3985 C  CE1   . HIS A 1 513 ? 20.521  13.442  20.373  1.00 32.31  ? 513 HIS A CE1   1 
ATOM   3986 N  NE2   . HIS A 1 513 ? 20.892  13.460  19.103  1.00 36.50  ? 513 HIS A NE2   1 
ATOM   3987 N  N     . VAL A 1 514 ? 16.411  12.629  20.411  1.00 33.98  ? 514 VAL A N     1 
ATOM   3988 C  CA    . VAL A 1 514 ? 16.158  11.850  21.617  1.00 32.83  ? 514 VAL A CA    1 
ATOM   3989 C  C     . VAL A 1 514 ? 17.438  11.152  22.049  1.00 36.45  ? 514 VAL A C     1 
ATOM   3990 O  O     . VAL A 1 514 ? 18.397  11.003  21.284  1.00 37.97  ? 514 VAL A O     1 
ATOM   3991 C  CB    . VAL A 1 514 ? 15.027  10.810  21.448  1.00 32.19  ? 514 VAL A CB    1 
ATOM   3992 C  CG1   . VAL A 1 514 ? 13.768  11.487  20.952  1.00 32.87  ? 514 VAL A CG1   1 
ATOM   3993 C  CG2   . VAL A 1 514 ? 15.445  9.680   20.491  1.00 31.84  ? 514 VAL A CG2   1 
ATOM   3994 N  N     . ASN A 1 515 ? 17.435  10.709  23.301  1.00 31.71  ? 515 ASN A N     1 
ATOM   3995 C  CA    . ASN A 1 515 ? 18.523  9.898   23.839  1.00 35.36  ? 515 ASN A CA    1 
ATOM   3996 C  C     . ASN A 1 515 ? 17.890  8.909   24.813  1.00 38.13  ? 515 ASN A C     1 
ATOM   3997 O  O     . ASN A 1 515 ? 17.539  9.283   25.934  1.00 35.89  ? 515 ASN A O     1 
ATOM   3998 C  CB    . ASN A 1 515 ? 19.577  10.776  24.509  1.00 37.36  ? 515 ASN A CB    1 
ATOM   3999 C  CG    . ASN A 1 515 ? 20.737  9.975   25.093  1.00 40.64  ? 515 ASN A CG    1 
ATOM   4000 O  OD1   . ASN A 1 515 ? 20.976  8.827   24.710  1.00 38.17  ? 515 ASN A OD1   1 
ATOM   4001 N  ND2   . ASN A 1 515 ? 21.473  10.589  26.018  1.00 37.71  ? 515 ASN A ND2   1 
ATOM   4002 N  N     . TRP A 1 516 ? 17.711  7.653   24.382  1.00 37.50  ? 516 TRP A N     1 
ATOM   4003 C  CA    . TRP A 1 516 ? 17.222  6.659   25.328  1.00 42.03  ? 516 TRP A CA    1 
ATOM   4004 C  C     . TRP A 1 516 ? 18.308  6.126   26.241  1.00 42.28  ? 516 TRP A C     1 
ATOM   4005 O  O     . TRP A 1 516 ? 17.993  5.316   27.115  1.00 43.38  ? 516 TRP A O     1 
ATOM   4006 C  CB    . TRP A 1 516 ? 16.598  5.426   24.646  1.00 40.58  ? 516 TRP A CB    1 
ATOM   4007 C  CG    . TRP A 1 516 ? 15.693  5.642   23.481  1.00 40.03  ? 516 TRP A CG    1 
ATOM   4008 C  CD1   . TRP A 1 516 ? 15.673  4.912   22.327  1.00 41.35  ? 516 TRP A CD1   1 
ATOM   4009 C  CD2   . TRP A 1 516 ? 14.652  6.620   23.354  1.00 41.37  ? 516 TRP A CD2   1 
ATOM   4010 N  NE1   . TRP A 1 516 ? 14.698  5.386   21.482  1.00 43.35  ? 516 TRP A NE1   1 
ATOM   4011 C  CE2   . TRP A 1 516 ? 14.053  6.430   22.091  1.00 38.62  ? 516 TRP A CE2   1 
ATOM   4012 C  CE3   . TRP A 1 516 ? 14.171  7.645   24.181  1.00 37.14  ? 516 TRP A CE3   1 
ATOM   4013 C  CZ2   . TRP A 1 516 ? 12.996  7.214   21.643  1.00 39.09  ? 516 TRP A CZ2   1 
ATOM   4014 C  CZ3   . TRP A 1 516 ? 13.124  8.416   23.731  1.00 37.41  ? 516 TRP A CZ3   1 
ATOM   4015 C  CH2   . TRP A 1 516 ? 12.550  8.202   22.474  1.00 35.40  ? 516 TRP A CH2   1 
ATOM   4016 N  N     . PHE A 1 517 ? 19.566  6.513   26.041  1.00 42.19  ? 517 PHE A N     1 
ATOM   4017 C  CA    . PHE A 1 517 ? 20.682  5.728   26.557  1.00 45.43  ? 517 PHE A CA    1 
ATOM   4018 C  C     . PHE A 1 517 ? 21.506  6.460   27.607  1.00 44.41  ? 517 PHE A C     1 
ATOM   4019 O  O     . PHE A 1 517 ? 22.618  6.016   27.915  1.00 46.00  ? 517 PHE A O     1 
ATOM   4020 C  CB    . PHE A 1 517 ? 21.583  5.269   25.393  1.00 44.59  ? 517 PHE A CB    1 
ATOM   4021 C  CG    . PHE A 1 517 ? 20.860  4.416   24.369  1.00 43.30  ? 517 PHE A CG    1 
ATOM   4022 C  CD1   . PHE A 1 517 ? 20.705  3.041   24.563  1.00 47.45  ? 517 PHE A CD1   1 
ATOM   4023 C  CD2   . PHE A 1 517 ? 20.316  4.995   23.228  1.00 41.58  ? 517 PHE A CD2   1 
ATOM   4024 C  CE1   . PHE A 1 517 ? 20.027  2.264   23.627  1.00 45.07  ? 517 PHE A CE1   1 
ATOM   4025 C  CE2   . PHE A 1 517 ? 19.638  4.230   22.294  1.00 43.01  ? 517 PHE A CE2   1 
ATOM   4026 C  CZ    . PHE A 1 517 ? 19.493  2.866   22.490  1.00 41.66  ? 517 PHE A CZ    1 
ATOM   4027 N  N     . ARG A 1 518 ? 20.996  7.554   28.172  1.00 44.03  ? 518 ARG A N     1 
ATOM   4028 C  CA    . ARG A 1 518 ? 21.747  8.274   29.191  1.00 49.28  ? 518 ARG A CA    1 
ATOM   4029 C  C     . ARG A 1 518 ? 21.915  7.399   30.424  1.00 58.56  ? 518 ARG A C     1 
ATOM   4030 O  O     . ARG A 1 518 ? 21.041  6.592   30.762  1.00 56.54  ? 518 ARG A O     1 
ATOM   4031 C  CB    . ARG A 1 518 ? 21.051  9.597   29.549  1.00 56.38  ? 518 ARG A CB    1 
ATOM   4032 C  CG    . ARG A 1 518 ? 22.002  10.694  30.065  1.00 50.43  ? 518 ARG A CG    1 
ATOM   4033 C  CD    . ARG A 1 518 ? 21.269  11.984  30.441  1.00 55.00  ? 518 ARG A CD    1 
ATOM   4034 N  NE    . ARG A 1 518 ? 22.162  12.970  31.044  1.00 51.20  ? 518 ARG A NE    1 
ATOM   4035 C  CZ    . ARG A 1 518 ? 21.984  14.286  30.990  1.00 56.98  ? 518 ARG A CZ    1 
ATOM   4036 N  NH1   . ARG A 1 518 ? 20.961  14.826  30.339  1.00 51.86  ? 518 ARG A NH1   1 
ATOM   4037 N  NH2   . ARG A 1 518 ? 22.860  15.083  31.597  1.00 56.94  ? 518 ARG A NH2   1 
ATOM   4038 N  N     . LYS A 1 519 ? 23.066  7.532   31.077  1.00 62.78  ? 519 LYS A N     1 
ATOM   4039 C  CA    . LYS A 1 519 ? 23.390  6.730   32.245  1.00 67.20  ? 519 LYS A CA    1 
ATOM   4040 C  C     . LYS A 1 519 ? 23.729  7.629   33.424  1.00 76.39  ? 519 LYS A C     1 
ATOM   4041 O  O     . LYS A 1 519 ? 24.197  8.761   33.255  1.00 73.66  ? 519 LYS A O     1 
ATOM   4042 C  CB    . LYS A 1 519 ? 24.556  5.771   31.958  1.00 69.00  ? 519 LYS A CB    1 
ATOM   4043 C  CG    . LYS A 1 519 ? 24.181  4.625   31.023  1.00 65.89  ? 519 LYS A CG    1 
ATOM   4044 C  CD    . LYS A 1 519 ? 25.372  3.761   30.653  1.00 64.84  ? 519 LYS A CD    1 
ATOM   4045 C  CE    . LYS A 1 519 ? 24.927  2.599   29.780  1.00 68.94  ? 519 LYS A CE    1 
ATOM   4046 N  NZ    . LYS A 1 519 ? 26.003  1.599   29.563  1.00 75.15  ? 519 LYS A NZ    1 
ATOM   4047 N  N     . ASP A 1 520 ? 23.471  7.111   34.623  1.00 86.84  ? 520 ASP A N     1 
ATOM   4048 C  CA    . ASP A 1 520 ? 23.758  7.814   35.861  1.00 95.11  ? 520 ASP A CA    1 
ATOM   4049 C  C     . ASP A 1 520 ? 25.204  7.562   36.282  1.00 102.99 ? 520 ASP A C     1 
ATOM   4050 O  O     . ASP A 1 520 ? 25.985  6.922   35.574  1.00 103.20 ? 520 ASP A O     1 
ATOM   4051 C  CB    . ASP A 1 520 ? 22.778  7.387   36.956  1.00 98.54  ? 520 ASP A CB    1 
ATOM   4052 C  CG    . ASP A 1 520 ? 22.799  5.880   37.228  1.00 99.14  ? 520 ASP A CG    1 
ATOM   4053 O  OD1   . ASP A 1 520 ? 23.639  5.157   36.650  1.00 98.55  ? 520 ASP A OD1   1 
ATOM   4054 O  OD2   . ASP A 1 520 ? 21.960  5.416   38.029  1.00 99.34  ? 520 ASP A OD2   1 
ATOM   4055 N  N     . LYS A 1 521 ? 25.565  8.064   37.464  1.00 106.51 ? 521 LYS A N     1 
ATOM   4056 C  CA    . LYS A 1 521 ? 26.884  7.791   38.018  1.00 110.53 ? 521 LYS A CA    1 
ATOM   4057 C  C     . LYS A 1 521 ? 27.090  6.317   38.344  1.00 109.96 ? 521 LYS A C     1 
ATOM   4058 O  O     . LYS A 1 521 ? 28.235  5.901   38.551  1.00 112.01 ? 521 LYS A O     1 
ATOM   4059 C  CB    . LYS A 1 521 ? 27.108  8.634   39.273  1.00 115.94 ? 521 LYS A CB    1 
ATOM   4060 C  CG    . LYS A 1 521 ? 26.786  10.109  39.102  1.00 117.84 ? 521 LYS A CG    1 
ATOM   4061 C  CD    . LYS A 1 521 ? 26.888  10.835  40.432  1.00 123.78 ? 521 LYS A CD    1 
ATOM   4062 C  CE    . LYS A 1 521 ? 26.489  12.293  40.304  1.00 126.50 ? 521 LYS A CE    1 
ATOM   4063 N  NZ    . LYS A 1 521 ? 26.556  12.989  41.618  1.00 130.97 ? 521 LYS A NZ    1 
ATOM   4064 N  N     . ASN A 1 522 ? 26.020  5.521   38.398  1.00 107.53 ? 522 ASN A N     1 
ATOM   4065 C  CA    . ASN A 1 522 ? 26.151  4.091   38.647  1.00 106.14 ? 522 ASN A CA    1 
ATOM   4066 C  C     . ASN A 1 522 ? 26.440  3.296   37.382  1.00 102.27 ? 522 ASN A C     1 
ATOM   4067 O  O     . ASN A 1 522 ? 27.003  2.200   37.471  1.00 101.75 ? 522 ASN A O     1 
ATOM   4068 C  CB    . ASN A 1 522 ? 24.878  3.540   39.297  1.00 104.80 ? 522 ASN A CB    1 
ATOM   4069 C  CG    . ASN A 1 522 ? 24.557  4.209   40.618  1.00 110.17 ? 522 ASN A CG    1 
ATOM   4070 O  OD1   . ASN A 1 522 ? 23.394  4.298   41.015  1.00 109.74 ? 522 ASN A OD1   1 
ATOM   4071 N  ND2   . ASN A 1 522 ? 25.588  4.688   41.307  1.00 114.68 ? 522 ASN A ND2   1 
ATOM   4072 N  N     . GLY A 1 523 ? 26.064  3.811   36.217  1.00 99.50  ? 523 GLY A N     1 
ATOM   4073 C  CA    . GLY A 1 523 ? 26.214  3.082   34.978  1.00 93.17  ? 523 GLY A CA    1 
ATOM   4074 C  C     . GLY A 1 523 ? 24.980  2.347   34.507  1.00 86.59  ? 523 GLY A C     1 
ATOM   4075 O  O     . GLY A 1 523 ? 25.084  1.520   33.592  1.00 82.59  ? 523 GLY A O     1 
ATOM   4076 N  N     . LYS A 1 524 ? 23.822  2.606   35.105  1.00 85.59  ? 524 LYS A N     1 
ATOM   4077 C  CA    . LYS A 1 524 ? 22.567  2.042   34.636  1.00 83.71  ? 524 LYS A CA    1 
ATOM   4078 C  C     . LYS A 1 524 ? 21.727  3.131   33.983  1.00 75.09  ? 524 LYS A C     1 
ATOM   4079 O  O     . LYS A 1 524 ? 21.850  4.316   34.310  1.00 76.41  ? 524 LYS A O     1 
ATOM   4080 C  CB    . LYS A 1 524 ? 21.786  1.379   35.777  1.00 84.73  ? 524 LYS A CB    1 
ATOM   4081 C  CG    . LYS A 1 524 ? 21.759  2.151   37.093  1.00 91.73  ? 524 LYS A CG    1 
ATOM   4082 C  CD    . LYS A 1 524 ? 21.254  1.249   38.222  1.00 89.59  ? 524 LYS A CD    1 
ATOM   4083 C  CE    . LYS A 1 524 ? 21.389  1.905   39.588  1.00 87.95  ? 524 LYS A CE    1 
ATOM   4084 N  NZ    . LYS A 1 524 ? 21.037  0.952   40.691  1.00 84.16  ? 524 LYS A NZ    1 
ATOM   4085 N  N     . PHE A 1 525 ? 20.873  2.714   33.052  1.00 67.64  ? 525 PHE A N     1 
ATOM   4086 C  CA    . PHE A 1 525 ? 20.084  3.663   32.277  1.00 66.70  ? 525 PHE A CA    1 
ATOM   4087 C  C     . PHE A 1 525 ? 19.117  4.422   33.177  1.00 64.61  ? 525 PHE A C     1 
ATOM   4088 O  O     . PHE A 1 525 ? 18.528  3.854   34.103  1.00 70.48  ? 525 PHE A O     1 
ATOM   4089 C  CB    . PHE A 1 525 ? 19.309  2.940   31.174  1.00 62.70  ? 525 PHE A CB    1 
ATOM   4090 C  CG    . PHE A 1 525 ? 20.178  2.185   30.205  1.00 62.93  ? 525 PHE A CG    1 
ATOM   4091 C  CD1   . PHE A 1 525 ? 20.662  2.798   29.067  1.00 57.77  ? 525 PHE A CD1   1 
ATOM   4092 C  CD2   . PHE A 1 525 ? 20.496  0.855   30.426  1.00 67.54  ? 525 PHE A CD2   1 
ATOM   4093 C  CE1   . PHE A 1 525 ? 21.453  2.107   28.173  1.00 57.77  ? 525 PHE A CE1   1 
ATOM   4094 C  CE2   . PHE A 1 525 ? 21.288  0.159   29.530  1.00 67.11  ? 525 PHE A CE2   1 
ATOM   4095 C  CZ    . PHE A 1 525 ? 21.763  0.793   28.398  1.00 62.23  ? 525 PHE A CZ    1 
ATOM   4096 N  N     . LEU A 1 526 ? 18.962  5.715   32.903  1.00 59.99  ? 526 LEU A N     1 
ATOM   4097 C  CA    . LEU A 1 526 ? 18.008  6.545   33.631  1.00 64.64  ? 526 LEU A CA    1 
ATOM   4098 C  C     . LEU A 1 526 ? 16.589  6.379   33.104  1.00 63.49  ? 526 LEU A C     1 
ATOM   4099 O  O     . LEU A 1 526 ? 15.625  6.594   33.847  1.00 63.75  ? 526 LEU A O     1 
ATOM   4100 C  CB    . LEU A 1 526 ? 18.413  8.018   33.542  1.00 59.30  ? 526 LEU A CB    1 
ATOM   4101 C  CG    . LEU A 1 526 ? 19.707  8.454   34.226  1.00 69.57  ? 526 LEU A CG    1 
ATOM   4102 C  CD1   . LEU A 1 526 ? 20.232  9.743   33.593  1.00 69.45  ? 526 LEU A CD1   1 
ATOM   4103 C  CD2   . LEU A 1 526 ? 19.473  8.648   35.711  1.00 75.63  ? 526 LEU A CD2   1 
ATOM   4104 N  N     . TRP A 1 527 ? 16.442  5.996   31.843  1.00 55.76  ? 527 TRP A N     1 
ATOM   4105 C  CA    . TRP A 1 527 ? 15.148  5.871   31.198  1.00 53.49  ? 527 TRP A CA    1 
ATOM   4106 C  C     . TRP A 1 527 ? 14.873  4.409   30.867  1.00 51.70  ? 527 TRP A C     1 
ATOM   4107 O  O     . TRP A 1 527 ? 15.769  3.725   30.357  1.00 53.61  ? 527 TRP A O     1 
ATOM   4108 C  CB    . TRP A 1 527 ? 15.129  6.728   29.926  1.00 49.54  ? 527 TRP A CB    1 
ATOM   4109 C  CG    . TRP A 1 527 ? 13.824  6.790   29.214  1.00 48.58  ? 527 TRP A CG    1 
ATOM   4110 C  CD1   . TRP A 1 527 ? 13.546  6.280   27.983  1.00 48.59  ? 527 TRP A CD1   1 
ATOM   4111 C  CD2   . TRP A 1 527 ? 12.616  7.408   29.676  1.00 47.40  ? 527 TRP A CD2   1 
ATOM   4112 N  NE1   . TRP A 1 527 ? 12.238  6.535   27.649  1.00 48.87  ? 527 TRP A NE1   1 
ATOM   4113 C  CE2   . TRP A 1 527 ? 11.645  7.225   28.672  1.00 46.62  ? 527 TRP A CE2   1 
ATOM   4114 C  CE3   . TRP A 1 527 ? 12.259  8.092   30.844  1.00 52.12  ? 527 TRP A CE3   1 
ATOM   4115 C  CZ2   . TRP A 1 527 ? 10.339  7.700   28.797  1.00 48.68  ? 527 TRP A CZ2   1 
ATOM   4116 C  CZ3   . TRP A 1 527 ? 10.965  8.565   30.964  1.00 50.24  ? 527 TRP A CZ3   1 
ATOM   4117 C  CH2   . TRP A 1 527 ? 10.020  8.368   29.948  1.00 50.35  ? 527 TRP A CH2   1 
ATOM   4118 N  N     . PRO A 1 528 ? 13.680  3.881   31.165  1.00 53.74  ? 528 PRO A N     1 
ATOM   4119 C  CA    . PRO A 1 528 ? 13.428  2.452   30.885  1.00 52.59  ? 528 PRO A CA    1 
ATOM   4120 C  C     . PRO A 1 528 ? 13.308  2.124   29.402  1.00 53.27  ? 528 PRO A C     1 
ATOM   4121 O  O     . PRO A 1 528 ? 13.578  0.980   29.010  1.00 49.48  ? 528 PRO A O     1 
ATOM   4122 C  CB    . PRO A 1 528 ? 12.115  2.178   31.632  1.00 52.00  ? 528 PRO A CB    1 
ATOM   4123 C  CG    . PRO A 1 528 ? 11.489  3.526   31.823  1.00 52.20  ? 528 PRO A CG    1 
ATOM   4124 C  CD    . PRO A 1 528 ? 12.626  4.467   32.013  1.00 52.39  ? 528 PRO A CD    1 
ATOM   4125 N  N     . GLY A 1 529 ? 12.905  3.083   28.569  1.00 48.43  ? 529 GLY A N     1 
ATOM   4126 C  CA    . GLY A 1 529 ? 12.846  2.851   27.142  1.00 47.86  ? 529 GLY A CA    1 
ATOM   4127 C  C     . GLY A 1 529 ? 11.776  1.851   26.726  1.00 46.82  ? 529 GLY A C     1 
ATOM   4128 O  O     . GLY A 1 529 ? 10.847  1.528   27.476  1.00 46.86  ? 529 GLY A O     1 
ATOM   4129 N  N     . PHE A 1 530 ? 11.933  1.365   25.495  1.00 43.80  ? 530 PHE A N     1 
ATOM   4130 C  CA    . PHE A 1 530 ? 11.048  0.375   24.866  1.00 45.02  ? 530 PHE A CA    1 
ATOM   4131 C  C     . PHE A 1 530 ? 9.626   0.932   24.881  1.00 44.81  ? 530 PHE A C     1 
ATOM   4132 O  O     . PHE A 1 530 ? 9.415   2.059   24.397  1.00 44.86  ? 530 PHE A O     1 
ATOM   4133 C  CB    . PHE A 1 530 ? 11.241  -0.987  25.553  1.00 48.05  ? 530 PHE A CB    1 
ATOM   4134 C  CG    . PHE A 1 530 ? 12.653  -1.484  25.485  1.00 46.97  ? 530 PHE A CG    1 
ATOM   4135 C  CD1   . PHE A 1 530 ? 13.189  -1.903  24.278  1.00 47.88  ? 530 PHE A CD1   1 
ATOM   4136 C  CD2   . PHE A 1 530 ? 13.457  -1.497  26.612  1.00 49.39  ? 530 PHE A CD2   1 
ATOM   4137 C  CE1   . PHE A 1 530 ? 14.500  -2.341  24.202  1.00 50.57  ? 530 PHE A CE1   1 
ATOM   4138 C  CE2   . PHE A 1 530 ? 14.769  -1.937  26.546  1.00 47.58  ? 530 PHE A CE2   1 
ATOM   4139 C  CZ    . PHE A 1 530 ? 15.290  -2.360  25.344  1.00 49.51  ? 530 PHE A CZ    1 
ATOM   4140 N  N     . GLY A 1 531 ? 8.640   0.192   25.408  1.00 43.72  ? 531 GLY A N     1 
ATOM   4141 C  CA    . GLY A 1 531 ? 7.269   0.668   25.407  1.00 47.55  ? 531 GLY A CA    1 
ATOM   4142 C  C     . GLY A 1 531 ? 7.079   1.988   26.125  1.00 46.66  ? 531 GLY A C     1 
ATOM   4143 O  O     . GLY A 1 531 ? 6.131   2.722   25.832  1.00 45.13  ? 531 GLY A O     1 
ATOM   4144 N  N     . GLU A 1 532 ? 7.972   2.316   27.065  1.00 45.37  ? 532 GLU A N     1 
ATOM   4145 C  CA    . GLU A 1 532 ? 7.842   3.594   27.763  1.00 45.23  ? 532 GLU A CA    1 
ATOM   4146 C  C     . GLU A 1 532 ? 8.187   4.786   26.884  1.00 41.80  ? 532 GLU A C     1 
ATOM   4147 O  O     . GLU A 1 532 ? 7.809   5.913   27.220  1.00 45.37  ? 532 GLU A O     1 
ATOM   4148 C  CB    . GLU A 1 532 ? 8.711   3.629   29.019  1.00 48.73  ? 532 GLU A CB    1 
ATOM   4149 C  CG    . GLU A 1 532 ? 8.412   2.524   30.045  1.00 48.77  ? 532 GLU A CG    1 
ATOM   4150 C  CD    . GLU A 1 532 ? 6.960   2.476   30.549  1.00 49.48  ? 532 GLU A CD    1 
ATOM   4151 O  OE1   . GLU A 1 532 ? 6.158   3.405   30.336  1.00 50.56  ? 532 GLU A OE1   1 
ATOM   4152 O  OE2   . GLU A 1 532 ? 6.610   1.469   31.177  1.00 55.31  ? 532 GLU A OE2   1 
ATOM   4153 N  N     . ASN A 1 533 ? 8.897   4.578   25.774  1.00 40.86  ? 533 ASN A N     1 
ATOM   4154 C  CA    . ASN A 1 533 ? 9.160   5.680   24.855  1.00 40.28  ? 533 ASN A CA    1 
ATOM   4155 C  C     . ASN A 1 533 ? 7.883   6.281   24.294  1.00 40.08  ? 533 ASN A C     1 
ATOM   4156 O  O     . ASN A 1 533 ? 7.919   7.399   23.757  1.00 38.62  ? 533 ASN A O     1 
ATOM   4157 C  CB    . ASN A 1 533 ? 10.066  5.213   23.713  1.00 37.75  ? 533 ASN A CB    1 
ATOM   4158 C  CG    . ASN A 1 533 ? 11.431  4.782   24.205  1.00 43.36  ? 533 ASN A CG    1 
ATOM   4159 O  OD1   . ASN A 1 533 ? 11.880  5.227   25.263  1.00 43.65  ? 533 ASN A OD1   1 
ATOM   4160 N  ND2   . ASN A 1 533 ? 12.109  3.919   23.437  1.00 40.33  ? 533 ASN A ND2   1 
ATOM   4161 N  N     . SER A 1 534 ? 6.755   5.582   24.431  1.00 42.78  ? 534 SER A N     1 
ATOM   4162 C  CA    . SER A 1 534 ? 5.476   6.173   24.070  1.00 47.91  ? 534 SER A CA    1 
ATOM   4163 C  C     . SER A 1 534 ? 5.240   7.495   24.794  1.00 41.50  ? 534 SER A C     1 
ATOM   4164 O  O     . SER A 1 534 ? 4.553   8.368   24.263  1.00 40.58  ? 534 SER A O     1 
ATOM   4165 C  CB    . SER A 1 534 ? 4.349   5.199   24.379  1.00 44.33  ? 534 SER A CB    1 
ATOM   4166 O  OG    . SER A 1 534 ? 4.301   4.900   25.761  1.00 46.46  ? 534 SER A OG    1 
ATOM   4167 N  N     . ARG A 1 535 ? 5.798   7.656   25.998  1.00 41.29  ? 535 ARG A N     1 
ATOM   4168 C  CA    . ARG A 1 535 ? 5.608   8.889   26.761  1.00 42.73  ? 535 ARG A CA    1 
ATOM   4169 C  C     . ARG A 1 535 ? 6.303   10.074  26.085  1.00 43.27  ? 535 ARG A C     1 
ATOM   4170 O  O     . ARG A 1 535 ? 5.839   11.226  26.177  1.00 39.56  ? 535 ARG A O     1 
ATOM   4171 C  CB    . ARG A 1 535 ? 6.129   8.680   28.186  1.00 41.50  ? 535 ARG A CB    1 
ATOM   4172 C  CG    . ARG A 1 535 ? 5.418   7.552   28.967  1.00 42.81  ? 535 ARG A CG    1 
ATOM   4173 C  CD    . ARG A 1 535 ? 6.100   7.251   30.305  1.00 51.11  ? 535 ARG A CD    1 
ATOM   4174 N  NE    . ARG A 1 535 ? 5.618   6.024   30.946  1.00 47.53  ? 535 ARG A NE    1 
ATOM   4175 C  CZ    . ARG A 1 535 ? 4.668   5.992   31.870  1.00 54.70  ? 535 ARG A CZ    1 
ATOM   4176 N  NH1   . ARG A 1 535 ? 4.043   7.093   32.252  1.00 57.24  ? 535 ARG A NH1   1 
ATOM   4177 N  NH2   . ARG A 1 535 ? 4.353   4.832   32.443  1.00 53.27  ? 535 ARG A NH2   1 
ATOM   4178 N  N     . VAL A 1 536 ? 7.415   9.808   25.408  1.00 37.74  ? 536 VAL A N     1 
ATOM   4179 C  CA    . VAL A 1 536 ? 8.105   10.840  24.655  1.00 36.45  ? 536 VAL A CA    1 
ATOM   4180 C  C     . VAL A 1 536 ? 7.356   11.138  23.363  1.00 38.75  ? 536 VAL A C     1 
ATOM   4181 O  O     . VAL A 1 536 ? 7.152   12.300  22.997  1.00 37.15  ? 536 VAL A O     1 
ATOM   4182 C  CB    . VAL A 1 536 ? 9.558   10.402  24.400  1.00 40.34  ? 536 VAL A CB    1 
ATOM   4183 C  CG1   . VAL A 1 536 ? 10.269  11.384  23.488  1.00 38.53  ? 536 VAL A CG1   1 
ATOM   4184 C  CG2   . VAL A 1 536 ? 10.305  10.253  25.715  1.00 38.94  ? 536 VAL A CG2   1 
ATOM   4185 N  N     . LEU A 1 537 ? 6.912   10.094  22.660  1.00 41.63  ? 537 LEU A N     1 
ATOM   4186 C  CA    . LEU A 1 537 ? 6.125   10.308  21.447  1.00 40.57  ? 537 LEU A CA    1 
ATOM   4187 C  C     . LEU A 1 537 ? 4.855   11.112  21.725  1.00 38.96  ? 537 LEU A C     1 
ATOM   4188 O  O     . LEU A 1 537 ? 4.413   11.890  20.877  1.00 36.60  ? 537 LEU A O     1 
ATOM   4189 C  CB    . LEU A 1 537 ? 5.757   8.972   20.818  1.00 38.30  ? 537 LEU A CB    1 
ATOM   4190 C  CG    . LEU A 1 537 ? 6.669   8.464   19.702  1.00 44.52  ? 537 LEU A CG    1 
ATOM   4191 C  CD1   . LEU A 1 537 ? 8.130   8.522   20.108  1.00 43.82  ? 537 LEU A CD1   1 
ATOM   4192 C  CD2   . LEU A 1 537 ? 6.245   7.058   19.366  1.00 47.20  ? 537 LEU A CD2   1 
ATOM   4193 N  N     . GLU A 1 538 ? 4.219   10.895  22.879  1.00 35.85  ? 538 GLU A N     1 
ATOM   4194 C  CA    . GLU A 1 538 ? 3.042   11.696  23.221  1.00 37.51  ? 538 GLU A CA    1 
ATOM   4195 C  C     . GLU A 1 538 ? 3.379   13.186  23.237  1.00 40.29  ? 538 GLU A C     1 
ATOM   4196 O  O     . GLU A 1 538 ? 2.637   14.013  22.689  1.00 37.38  ? 538 GLU A O     1 
ATOM   4197 C  CB    . GLU A 1 538 ? 2.469   11.251  24.575  1.00 42.39  ? 538 GLU A CB    1 
ATOM   4198 C  CG    . GLU A 1 538 ? 1.220   12.032  24.972  1.00 46.54  ? 538 GLU A CG    1 
ATOM   4199 C  CD    . GLU A 1 538 ? 0.647   11.656  26.340  1.00 54.96  ? 538 GLU A CD    1 
ATOM   4200 O  OE1   . GLU A 1 538 ? 1.417   11.411  27.296  1.00 52.41  ? 538 GLU A OE1   1 
ATOM   4201 O  OE2   . GLU A 1 538 ? -0.593  11.632  26.455  1.00 56.48  ? 538 GLU A OE2   1 
ATOM   4202 N  N     . TRP A 1 539 ? 4.515   13.542  23.833  1.00 39.17  ? 539 TRP A N     1 
ATOM   4203 C  CA    . TRP A 1 539 ? 4.912   14.940  23.866  1.00 38.27  ? 539 TRP A CA    1 
ATOM   4204 C  C     . TRP A 1 539 ? 5.148   15.477  22.458  1.00 40.91  ? 539 TRP A C     1 
ATOM   4205 O  O     . TRP A 1 539 ? 4.730   16.601  22.138  1.00 36.94  ? 539 TRP A O     1 
ATOM   4206 C  CB    . TRP A 1 539 ? 6.159   15.106  24.733  1.00 40.31  ? 539 TRP A CB    1 
ATOM   4207 C  CG    . TRP A 1 539 ? 6.569   16.545  24.895  1.00 35.05  ? 539 TRP A CG    1 
ATOM   4208 C  CD1   . TRP A 1 539 ? 5.984   17.489  25.706  1.00 39.48  ? 539 TRP A CD1   1 
ATOM   4209 C  CD2   . TRP A 1 539 ? 7.666   17.198  24.243  1.00 36.90  ? 539 TRP A CD2   1 
ATOM   4210 N  NE1   . TRP A 1 539 ? 6.646   18.698  25.576  1.00 37.26  ? 539 TRP A NE1   1 
ATOM   4211 C  CE2   . TRP A 1 539 ? 7.682   18.543  24.690  1.00 35.83  ? 539 TRP A CE2   1 
ATOM   4212 C  CE3   . TRP A 1 539 ? 8.636   16.778  23.317  1.00 36.71  ? 539 TRP A CE3   1 
ATOM   4213 C  CZ2   . TRP A 1 539 ? 8.636   19.468  24.245  1.00 39.72  ? 539 TRP A CZ2   1 
ATOM   4214 C  CZ3   . TRP A 1 539 ? 9.577   17.701  22.872  1.00 38.17  ? 539 TRP A CZ3   1 
ATOM   4215 C  CH2   . TRP A 1 539 ? 9.571   19.028  23.336  1.00 38.57  ? 539 TRP A CH2   1 
ATOM   4216 N  N     . MET A 1 540 ? 5.816   14.686  21.602  1.00 35.74  ? 540 MET A N     1 
ATOM   4217 C  CA    . MET A 1 540 ? 6.060   15.108  20.220  1.00 36.87  ? 540 MET A CA    1 
ATOM   4218 C  C     . MET A 1 540 ? 4.754   15.300  19.460  1.00 35.09  ? 540 MET A C     1 
ATOM   4219 O  O     . MET A 1 540 ? 4.606   16.252  18.690  1.00 36.15  ? 540 MET A O     1 
ATOM   4220 C  CB    . MET A 1 540 ? 6.923   14.068  19.495  1.00 33.52  ? 540 MET A CB    1 
ATOM   4221 C  CG    . MET A 1 540 ? 8.352   13.930  19.983  1.00 32.52  ? 540 MET A CG    1 
ATOM   4222 S  SD    . MET A 1 540 ? 9.071   12.442  19.208  1.00 40.15  ? 540 MET A SD    1 
ATOM   4223 C  CE    . MET A 1 540 ? 10.673  12.425  19.986  1.00 37.15  ? 540 MET A CE    1 
ATOM   4224 N  N     . PHE A 1 541 ? 3.808   14.383  19.642  1.00 34.75  ? 541 PHE A N     1 
ATOM   4225 C  CA    . PHE A 1 541 ? 2.498   14.507  19.009  1.00 39.55  ? 541 PHE A CA    1 
ATOM   4226 C  C     . PHE A 1 541 ? 1.844   15.834  19.378  1.00 38.73  ? 541 PHE A C     1 
ATOM   4227 O  O     . PHE A 1 541 ? 1.363   16.570  18.506  1.00 38.29  ? 541 PHE A O     1 
ATOM   4228 C  CB    . PHE A 1 541 ? 1.627   13.331  19.446  1.00 39.08  ? 541 PHE A CB    1 
ATOM   4229 C  CG    . PHE A 1 541 ? 0.427   13.075  18.577  1.00 44.09  ? 541 PHE A CG    1 
ATOM   4230 C  CD1   . PHE A 1 541 ? -0.685  13.905  18.633  1.00 42.31  ? 541 PHE A CD1   1 
ATOM   4231 C  CD2   . PHE A 1 541 ? 0.383   11.935  17.755  1.00 41.36  ? 541 PHE A CD2   1 
ATOM   4232 C  CE1   . PHE A 1 541 ? -1.814  13.638  17.855  1.00 44.38  ? 541 PHE A CE1   1 
ATOM   4233 C  CE2   . PHE A 1 541 ? -0.730  11.662  16.972  1.00 42.56  ? 541 PHE A CE2   1 
ATOM   4234 C  CZ    . PHE A 1 541 ? -1.838  12.520  17.022  1.00 46.51  ? 541 PHE A CZ    1 
ATOM   4235 N  N     . GLY A 1 542 ? 1.826   16.158  20.674  1.00 36.91  ? 542 GLY A N     1 
ATOM   4236 C  CA    . GLY A 1 542 ? 1.242   17.419  21.108  1.00 39.42  ? 542 GLY A CA    1 
ATOM   4237 C  C     . GLY A 1 542 ? 1.960   18.633  20.547  1.00 40.31  ? 542 GLY A C     1 
ATOM   4238 O  O     . GLY A 1 542 ? 1.323   19.618  20.165  1.00 41.79  ? 542 GLY A O     1 
ATOM   4239 N  N     . ARG A 1 543 ? 3.297   18.581  20.488  1.00 36.97  ? 543 ARG A N     1 
ATOM   4240 C  CA    . ARG A 1 543 ? 4.061   19.691  19.922  1.00 38.10  ? 543 ARG A CA    1 
ATOM   4241 C  C     . ARG A 1 543 ? 3.744   19.894  18.446  1.00 39.75  ? 543 ARG A C     1 
ATOM   4242 O  O     . ARG A 1 543 ? 3.752   21.022  17.957  1.00 41.19  ? 543 ARG A O     1 
ATOM   4243 C  CB    . ARG A 1 543 ? 5.565   19.453  20.107  1.00 36.35  ? 543 ARG A CB    1 
ATOM   4244 C  CG    . ARG A 1 543 ? 6.084   19.696  21.515  1.00 37.55  ? 543 ARG A CG    1 
ATOM   4245 C  CD    . ARG A 1 543 ? 5.857   21.145  21.923  1.00 38.46  ? 543 ARG A CD    1 
ATOM   4246 N  NE    . ARG A 1 543 ? 6.659   22.056  21.120  1.00 34.31  ? 543 ARG A NE    1 
ATOM   4247 C  CZ    . ARG A 1 543 ? 6.431   23.358  21.023  1.00 42.64  ? 543 ARG A CZ    1 
ATOM   4248 N  NH1   . ARG A 1 543 ? 5.398   23.922  21.630  1.00 42.88  ? 543 ARG A NH1   1 
ATOM   4249 N  NH2   . ARG A 1 543 ? 7.266   24.112  20.314  1.00 43.79  ? 543 ARG A NH2   1 
ATOM   4250 N  N     . ILE A 1 544 ? 3.484   18.814  17.716  1.00 37.57  ? 544 ILE A N     1 
ATOM   4251 C  CA    . ILE A 1 544 ? 3.108   18.936  16.313  1.00 39.91  ? 544 ILE A CA    1 
ATOM   4252 C  C     . ILE A 1 544 ? 1.738   19.587  16.180  1.00 39.01  ? 544 ILE A C     1 
ATOM   4253 O  O     . ILE A 1 544 ? 1.484   20.332  15.224  1.00 37.61  ? 544 ILE A O     1 
ATOM   4254 C  CB    . ILE A 1 544 ? 3.146   17.543  15.642  1.00 38.22  ? 544 ILE A CB    1 
ATOM   4255 C  CG1   . ILE A 1 544 ? 4.592   17.059  15.479  1.00 36.19  ? 544 ILE A CG1   1 
ATOM   4256 C  CG2   . ILE A 1 544 ? 2.447   17.581  14.302  1.00 36.93  ? 544 ILE A CG2   1 
ATOM   4257 C  CD1   . ILE A 1 544 ? 4.701   15.554  15.130  1.00 34.78  ? 544 ILE A CD1   1 
ATOM   4258 N  N     . GLU A 1 545 ? 0.832   19.315  17.117  1.00 39.01  ? 545 GLU A N     1 
ATOM   4259 C  CA    . GLU A 1 545 ? -0.477  19.957  17.121  1.00 42.11  ? 545 GLU A CA    1 
ATOM   4260 C  C     . GLU A 1 545 ? -0.425  21.398  17.616  1.00 43.60  ? 545 GLU A C     1 
ATOM   4261 O  O     . GLU A 1 545 ? -1.434  22.104  17.525  1.00 47.02  ? 545 GLU A O     1 
ATOM   4262 C  CB    . GLU A 1 545 ? -1.459  19.156  17.984  1.00 44.97  ? 545 GLU A CB    1 
ATOM   4263 C  CG    . GLU A 1 545 ? -1.951  17.834  17.371  1.00 40.97  ? 545 GLU A CG    1 
ATOM   4264 C  CD    . GLU A 1 545 ? -3.076  17.205  18.201  1.00 51.10  ? 545 GLU A CD    1 
ATOM   4265 O  OE1   . GLU A 1 545 ? -3.039  17.310  19.449  1.00 53.18  ? 545 GLU A OE1   1 
ATOM   4266 O  OE2   . GLU A 1 545 ? -4.015  16.629  17.612  1.00 53.17  ? 545 GLU A OE2   1 
ATOM   4267 N  N     . GLY A 1 546 ? 0.709   21.845  18.142  1.00 42.74  ? 546 GLY A N     1 
ATOM   4268 C  CA    . GLY A 1 546 ? 0.851   23.204  18.609  1.00 44.08  ? 546 GLY A CA    1 
ATOM   4269 C  C     . GLY A 1 546 ? 0.639   23.425  20.089  1.00 46.05  ? 546 GLY A C     1 
ATOM   4270 O  O     . GLY A 1 546 ? 0.363   24.554  20.485  1.00 44.52  ? 546 GLY A O     1 
ATOM   4271 N  N     . GLU A 1 547 ? 0.767   22.394  20.918  1.00 44.24  ? 547 GLU A N     1 
ATOM   4272 C  CA    . GLU A 1 547 ? 0.578   22.571  22.349  1.00 46.98  ? 547 GLU A CA    1 
ATOM   4273 C  C     . GLU A 1 547 ? 1.702   23.412  22.952  1.00 47.02  ? 547 GLU A C     1 
ATOM   4274 O  O     . GLU A 1 547 ? 2.872   23.277  22.582  1.00 43.69  ? 547 GLU A O     1 
ATOM   4275 C  CB    . GLU A 1 547 ? 0.495   21.208  23.032  1.00 47.22  ? 547 GLU A CB    1 
ATOM   4276 C  CG    . GLU A 1 547 ? -0.780  20.447  22.689  1.00 54.34  ? 547 GLU A CG    1 
ATOM   4277 C  CD    . GLU A 1 547 ? -0.990  19.224  23.571  1.00 65.22  ? 547 GLU A CD    1 
ATOM   4278 O  OE1   . GLU A 1 547 ? -0.577  19.272  24.747  1.00 68.32  ? 547 GLU A OE1   1 
ATOM   4279 O  OE2   . GLU A 1 547 ? -1.559  18.212  23.094  1.00 69.21  ? 547 GLU A OE2   1 
ATOM   4280 N  N     . ASP A 1 548 ? 1.337   24.301  23.885  1.00 48.84  ? 548 ASP A N     1 
ATOM   4281 C  CA    . ASP A 1 548 ? 2.315   25.147  24.573  1.00 51.70  ? 548 ASP A CA    1 
ATOM   4282 C  C     . ASP A 1 548 ? 2.972   24.384  25.726  1.00 50.27  ? 548 ASP A C     1 
ATOM   4283 O  O     . ASP A 1 548 ? 2.834   24.716  26.904  1.00 54.64  ? 548 ASP A O     1 
ATOM   4284 C  CB    . ASP A 1 548 ? 1.659   26.425  25.078  1.00 52.35  ? 548 ASP A CB    1 
ATOM   4285 C  CG    . ASP A 1 548 ? 2.670   27.401  25.652  1.00 61.87  ? 548 ASP A CG    1 
ATOM   4286 O  OD1   . ASP A 1 548 ? 3.708   27.632  24.996  1.00 66.69  ? 548 ASP A OD1   1 
ATOM   4287 O  OD2   . ASP A 1 548 ? 2.426   27.944  26.750  1.00 68.05  ? 548 ASP A OD2   1 
ATOM   4288 N  N     . SER A 1 549 ? 3.726   23.352  25.360  1.00 46.44  ? 549 SER A N     1 
ATOM   4289 C  CA    . SER A 1 549 ? 4.261   22.412  26.330  1.00 46.15  ? 549 SER A CA    1 
ATOM   4290 C  C     . SER A 1 549 ? 5.784   22.401  26.369  1.00 44.06  ? 549 SER A C     1 
ATOM   4291 O  O     . SER A 1 549 ? 6.368   21.475  26.950  1.00 43.34  ? 549 SER A O     1 
ATOM   4292 C  CB    . SER A 1 549 ? 3.738   21.017  26.009  1.00 43.08  ? 549 SER A CB    1 
ATOM   4293 O  OG    . SER A 1 549 ? 4.060   20.738  24.659  1.00 39.92  ? 549 SER A OG    1 
ATOM   4294 N  N     . ALA A 1 550 ? 6.443   23.388  25.763  1.00 38.38  ? 550 ALA A N     1 
ATOM   4295 C  CA    . ALA A 1 550 ? 7.893   23.411  25.676  1.00 39.30  ? 550 ALA A CA    1 
ATOM   4296 C  C     . ALA A 1 550 ? 8.466   24.618  26.403  1.00 43.96  ? 550 ALA A C     1 
ATOM   4297 O  O     . ALA A 1 550 ? 7.814   25.652  26.557  1.00 42.06  ? 550 ALA A O     1 
ATOM   4298 C  CB    . ALA A 1 550 ? 8.373   23.421  24.218  1.00 44.10  ? 550 ALA A CB    1 
ATOM   4299 N  N     . LYS A 1 551 ? 9.716   24.458  26.819  1.00 43.45  ? 551 LYS A N     1 
ATOM   4300 C  CA    . LYS A 1 551 ? 10.533  25.487  27.443  1.00 44.32  ? 551 LYS A CA    1 
ATOM   4301 C  C     . LYS A 1 551 ? 11.791  25.695  26.602  1.00 43.64  ? 551 LYS A C     1 
ATOM   4302 O  O     . LYS A 1 551 ? 12.378  24.732  26.101  1.00 36.90  ? 551 LYS A O     1 
ATOM   4303 C  CB    . LYS A 1 551 ? 10.893  25.053  28.856  1.00 46.29  ? 551 LYS A CB    1 
ATOM   4304 C  CG    . LYS A 1 551 ? 11.837  25.951  29.588  1.00 54.04  ? 551 LYS A CG    1 
ATOM   4305 C  CD    . LYS A 1 551 ? 12.094  25.397  30.985  1.00 58.10  ? 551 LYS A CD    1 
ATOM   4306 C  CE    . LYS A 1 551 ? 12.822  24.071  30.926  1.00 57.87  ? 551 LYS A CE    1 
ATOM   4307 N  NZ    . LYS A 1 551 ? 13.100  23.546  32.293  1.00 66.56  ? 551 LYS A NZ    1 
ATOM   4308 N  N     . LEU A 1 552 ? 12.208  26.949  26.437  1.00 39.78  ? 552 LEU A N     1 
ATOM   4309 C  CA    . LEU A 1 552 ? 13.357  27.252  25.591  1.00 43.08  ? 552 LEU A CA    1 
ATOM   4310 C  C     . LEU A 1 552 ? 14.667  27.080  26.357  1.00 41.52  ? 552 LEU A C     1 
ATOM   4311 O  O     . LEU A 1 552 ? 14.815  27.596  27.463  1.00 43.16  ? 552 LEU A O     1 
ATOM   4312 C  CB    . LEU A 1 552 ? 13.248  28.685  25.062  1.00 39.96  ? 552 LEU A CB    1 
ATOM   4313 C  CG    . LEU A 1 552 ? 14.447  29.134  24.228  1.00 39.87  ? 552 LEU A CG    1 
ATOM   4314 C  CD1   . LEU A 1 552 ? 14.605  28.240  23.002  1.00 47.01  ? 552 LEU A CD1   1 
ATOM   4315 C  CD2   . LEU A 1 552 ? 14.324  30.636  23.855  1.00 45.38  ? 552 LEU A CD2   1 
ATOM   4316 N  N     . THR A 1 553 ? 15.630  26.395  25.757  1.00 38.53  ? 553 THR A N     1 
ATOM   4317 C  CA    . THR A 1 553 ? 16.952  26.193  26.336  1.00 40.55  ? 553 THR A CA    1 
ATOM   4318 C  C     . THR A 1 553 ? 18.009  26.506  25.289  1.00 41.04  ? 553 THR A C     1 
ATOM   4319 O  O     . THR A 1 553 ? 17.698  26.653  24.104  1.00 38.14  ? 553 THR A O     1 
ATOM   4320 C  CB    . THR A 1 553 ? 17.136  24.745  26.839  1.00 41.40  ? 553 THR A CB    1 
ATOM   4321 O  OG1   . THR A 1 553 ? 17.470  23.895  25.739  1.00 39.85  ? 553 THR A OG1   1 
ATOM   4322 C  CG2   . THR A 1 553 ? 15.880  24.208  27.531  1.00 40.72  ? 553 THR A CG2   1 
ATOM   4323 N  N     . PRO A 1 554 ? 19.282  26.598  25.690  1.00 37.65  ? 554 PRO A N     1 
ATOM   4324 C  CA    . PRO A 1 554 ? 20.350  26.822  24.705  1.00 37.74  ? 554 PRO A CA    1 
ATOM   4325 C  C     . PRO A 1 554 ? 20.453  25.782  23.592  1.00 41.19  ? 554 PRO A C     1 
ATOM   4326 O  O     . PRO A 1 554 ? 20.954  26.115  22.509  1.00 38.79  ? 554 PRO A O     1 
ATOM   4327 C  CB    . PRO A 1 554 ? 21.609  26.829  25.579  1.00 43.43  ? 554 PRO A CB    1 
ATOM   4328 C  CG    . PRO A 1 554 ? 21.143  27.392  26.877  1.00 44.49  ? 554 PRO A CG    1 
ATOM   4329 C  CD    . PRO A 1 554 ? 19.757  26.831  27.072  1.00 40.99  ? 554 PRO A CD    1 
ATOM   4330 N  N     . ILE A 1 555 ? 20.021  24.532  23.805  1.00 33.57  ? 555 ILE A N     1 
ATOM   4331 C  CA    . ILE A 1 555 ? 20.142  23.521  22.759  1.00 34.48  ? 555 ILE A CA    1 
ATOM   4332 C  C     . ILE A 1 555 ? 18.853  23.329  21.964  1.00 39.21  ? 555 ILE A C     1 
ATOM   4333 O  O     . ILE A 1 555 ? 18.869  22.609  20.950  1.00 37.44  ? 555 ILE A O     1 
ATOM   4334 C  CB    . ILE A 1 555 ? 20.592  22.166  23.347  1.00 39.73  ? 555 ILE A CB    1 
ATOM   4335 C  CG1   . ILE A 1 555 ? 19.514  21.624  24.299  1.00 39.15  ? 555 ILE A CG1   1 
ATOM   4336 C  CG2   . ILE A 1 555 ? 21.939  22.335  24.056  1.00 39.68  ? 555 ILE A CG2   1 
ATOM   4337 C  CD1   . ILE A 1 555 ? 19.650  20.139  24.667  1.00 39.54  ? 555 ILE A CD1   1 
ATOM   4338 N  N     . GLY A 1 556 ? 17.750  23.933  22.386  1.00 37.57  ? 556 GLY A N     1 
ATOM   4339 C  CA    . GLY A 1 556 ? 16.467  23.739  21.740  1.00 40.65  ? 556 GLY A CA    1 
ATOM   4340 C  C     . GLY A 1 556 ? 15.354  23.784  22.771  1.00 37.12  ? 556 GLY A C     1 
ATOM   4341 O  O     . GLY A 1 556 ? 15.556  24.174  23.909  1.00 39.84  ? 556 GLY A O     1 
ATOM   4342 N  N     . TYR A 1 557 ? 14.161  23.385  22.348  1.00 36.59  ? 557 TYR A N     1 
ATOM   4343 C  CA    . TYR A 1 557 ? 13.031  23.306  23.267  1.00 40.08  ? 557 TYR A CA    1 
ATOM   4344 C  C     . TYR A 1 557 ? 13.038  21.960  23.975  1.00 38.74  ? 557 TYR A C     1 
ATOM   4345 O  O     . TYR A 1 557 ? 13.332  20.932  23.360  1.00 34.96  ? 557 TYR A O     1 
ATOM   4346 C  CB    . TYR A 1 557 ? 11.703  23.465  22.533  1.00 37.25  ? 557 TYR A CB    1 
ATOM   4347 C  CG    . TYR A 1 557 ? 11.539  24.787  21.868  1.00 43.85  ? 557 TYR A CG    1 
ATOM   4348 C  CD1   . TYR A 1 557 ? 11.460  25.943  22.615  1.00 43.57  ? 557 TYR A CD1   1 
ATOM   4349 C  CD2   . TYR A 1 557 ? 11.455  24.885  20.485  1.00 43.63  ? 557 TYR A CD2   1 
ATOM   4350 C  CE1   . TYR A 1 557 ? 11.309  27.185  22.003  1.00 49.27  ? 557 TYR A CE1   1 
ATOM   4351 C  CE2   . TYR A 1 557 ? 11.302  26.121  19.865  1.00 39.45  ? 557 TYR A CE2   1 
ATOM   4352 C  CZ    . TYR A 1 557 ? 11.226  27.257  20.631  1.00 47.98  ? 557 TYR A CZ    1 
ATOM   4353 O  OH    . TYR A 1 557 ? 11.067  28.475  20.010  1.00 51.66  ? 557 TYR A OH    1 
ATOM   4354 N  N     . VAL A 1 558 ? 12.706  21.973  25.262  1.00 39.32  ? 558 VAL A N     1 
ATOM   4355 C  CA    . VAL A 1 558 ? 12.505  20.743  26.026  1.00 38.22  ? 558 VAL A CA    1 
ATOM   4356 C  C     . VAL A 1 558 ? 11.135  20.831  26.686  1.00 40.84  ? 558 VAL A C     1 
ATOM   4357 O  O     . VAL A 1 558 ? 10.553  21.926  26.785  1.00 39.29  ? 558 VAL A O     1 
ATOM   4358 C  CB    . VAL A 1 558 ? 13.628  20.534  27.073  1.00 40.01  ? 558 VAL A CB    1 
ATOM   4359 C  CG1   . VAL A 1 558 ? 15.001  20.610  26.414  1.00 39.62  ? 558 VAL A CG1   1 
ATOM   4360 C  CG2   . VAL A 1 558 ? 13.516  21.560  28.174  1.00 44.36  ? 558 VAL A CG2   1 
ATOM   4361 N  N     . PRO A 1 559 ? 10.580  19.700  27.126  1.00 40.67  ? 559 PRO A N     1 
ATOM   4362 C  CA    . PRO A 1 559 ? 9.253   19.732  27.757  1.00 39.13  ? 559 PRO A CA    1 
ATOM   4363 C  C     . PRO A 1 559 ? 9.268   20.558  29.027  1.00 39.88  ? 559 PRO A C     1 
ATOM   4364 O  O     . PRO A 1 559 ? 10.232  20.534  29.791  1.00 44.52  ? 559 PRO A O     1 
ATOM   4365 C  CB    . PRO A 1 559 ? 8.957   18.253  28.064  1.00 38.52  ? 559 PRO A CB    1 
ATOM   4366 C  CG    . PRO A 1 559 ? 9.883   17.477  27.197  1.00 37.24  ? 559 PRO A CG    1 
ATOM   4367 C  CD    . PRO A 1 559 ? 11.091  18.321  26.976  1.00 39.90  ? 559 PRO A CD    1 
ATOM   4368 N  N     . LYS A 1 560 ? 8.186   21.293  29.246  1.00 43.62  ? 560 LYS A N     1 
ATOM   4369 C  CA    . LYS A 1 560 ? 7.995   21.972  30.519  1.00 47.21  ? 560 LYS A CA    1 
ATOM   4370 C  C     . LYS A 1 560 ? 7.857   20.959  31.649  1.00 52.23  ? 560 LYS A C     1 
ATOM   4371 O  O     . LYS A 1 560 ? 7.585   19.781  31.425  1.00 53.59  ? 560 LYS A O     1 
ATOM   4372 C  CB    . LYS A 1 560 ? 6.740   22.835  30.490  1.00 52.29  ? 560 LYS A CB    1 
ATOM   4373 C  CG    . LYS A 1 560 ? 6.749   23.985  29.517  1.00 46.90  ? 560 LYS A CG    1 
ATOM   4374 C  CD    . LYS A 1 560 ? 5.357   24.600  29.514  1.00 47.48  ? 560 LYS A CD    1 
ATOM   4375 C  CE    . LYS A 1 560 ? 5.358   25.991  28.918  1.00 51.70  ? 560 LYS A CE    1 
ATOM   4376 N  NZ    . LYS A 1 560 ? 3.976   26.553  28.853  1.00 49.64  ? 560 LYS A NZ    1 
ATOM   4377 N  N     . GLU A 1 561 ? 8.017   21.440  32.883  1.00 58.01  ? 561 GLU A N     1 
ATOM   4378 C  CA    . GLU A 1 561 ? 7.735   20.599  34.042  1.00 65.02  ? 561 GLU A CA    1 
ATOM   4379 C  C     . GLU A 1 561 ? 6.305   20.072  33.973  1.00 63.28  ? 561 GLU A C     1 
ATOM   4380 O  O     . GLU A 1 561 ? 5.364   20.811  33.666  1.00 68.68  ? 561 GLU A O     1 
ATOM   4381 C  CB    . GLU A 1 561 ? 7.933   21.386  35.346  1.00 71.89  ? 561 GLU A CB    1 
ATOM   4382 C  CG    . GLU A 1 561 ? 9.329   21.964  35.552  1.00 77.86  ? 561 GLU A CG    1 
ATOM   4383 C  CD    . GLU A 1 561 ? 9.465   22.710  36.875  1.00 90.07  ? 561 GLU A CD    1 
ATOM   4384 O  OE1   . GLU A 1 561 ? 8.606   22.519  37.767  1.00 86.62  ? 561 GLU A OE1   1 
ATOM   4385 O  OE2   . GLU A 1 561 ? 10.432  23.492  37.021  1.00 94.28  ? 561 GLU A OE2   1 
ATOM   4386 N  N     . ASP A 1 562 ? 6.148   18.787  34.266  1.00 64.21  ? 562 ASP A N     1 
ATOM   4387 C  CA    . ASP A 1 562 ? 4.864   18.092  34.247  1.00 69.04  ? 562 ASP A CA    1 
ATOM   4388 C  C     . ASP A 1 562 ? 4.236   18.028  32.857  1.00 61.76  ? 562 ASP A C     1 
ATOM   4389 O  O     . ASP A 1 562 ? 3.058   17.677  32.731  1.00 61.35  ? 562 ASP A O     1 
ATOM   4390 C  CB    . ASP A 1 562 ? 3.871   18.716  35.241  1.00 79.95  ? 562 ASP A CB    1 
ATOM   4391 C  CG    . ASP A 1 562 ? 4.222   18.411  36.690  1.00 84.84  ? 562 ASP A CG    1 
ATOM   4392 O  OD1   . ASP A 1 562 ? 4.860   17.362  36.942  1.00 86.56  ? 562 ASP A OD1   1 
ATOM   4393 O  OD2   . ASP A 1 562 ? 3.853   19.217  37.575  1.00 85.18  ? 562 ASP A OD2   1 
ATOM   4394 N  N     . ALA A 1 563 ? 4.984   18.354  31.803  1.00 60.70  ? 563 ALA A N     1 
ATOM   4395 C  CA    . ALA A 1 563 ? 4.465   18.182  30.454  1.00 56.31  ? 563 ALA A CA    1 
ATOM   4396 C  C     . ALA A 1 563 ? 4.559   16.739  29.981  1.00 55.53  ? 563 ALA A C     1 
ATOM   4397 O  O     . ALA A 1 563 ? 3.806   16.348  29.086  1.00 57.62  ? 563 ALA A O     1 
ATOM   4398 C  CB    . ALA A 1 563 ? 5.209   19.088  29.471  1.00 50.75  ? 563 ALA A CB    1 
ATOM   4399 N  N     . LEU A 1 564 ? 5.474   15.956  30.545  1.00 55.53  ? 564 LEU A N     1 
ATOM   4400 C  CA    . LEU A 1 564 ? 5.608   14.540  30.218  1.00 54.72  ? 564 LEU A CA    1 
ATOM   4401 C  C     . LEU A 1 564 ? 4.761   13.708  31.161  1.00 52.81  ? 564 LEU A C     1 
ATOM   4402 O  O     . LEU A 1 564 ? 4.765   13.935  32.372  1.00 57.95  ? 564 LEU A O     1 
ATOM   4403 C  CB    . LEU A 1 564 ? 7.061   14.085  30.335  1.00 55.06  ? 564 LEU A CB    1 
ATOM   4404 C  CG    . LEU A 1 564 ? 8.015   14.334  29.180  1.00 56.14  ? 564 LEU A CG    1 
ATOM   4405 C  CD1   . LEU A 1 564 ? 9.369   13.735  29.504  1.00 59.90  ? 564 LEU A CD1   1 
ATOM   4406 C  CD2   . LEU A 1 564 ? 7.456   13.713  27.919  1.00 51.96  ? 564 LEU A CD2   1 
ATOM   4407 N  N     . ASN A 1 565 ? 4.047   12.732  30.609  1.00 57.30  ? 565 ASN A N     1 
ATOM   4408 C  CA    . ASN A 1 565 ? 3.351   11.766  31.457  1.00 58.47  ? 565 ASN A CA    1 
ATOM   4409 C  C     . ASN A 1 565 ? 4.388   10.828  32.061  1.00 59.66  ? 565 ASN A C     1 
ATOM   4410 O  O     . ASN A 1 565 ? 4.901   9.926   31.395  1.00 55.01  ? 565 ASN A O     1 
ATOM   4411 C  CB    . ASN A 1 565 ? 2.295   10.993  30.676  1.00 57.37  ? 565 ASN A CB    1 
ATOM   4412 C  CG    . ASN A 1 565 ? 1.387   10.178  31.586  1.00 63.41  ? 565 ASN A CG    1 
ATOM   4413 O  OD1   . ASN A 1 565 ? 1.682   9.995   32.767  1.00 64.13  ? 565 ASN A OD1   1 
ATOM   4414 N  ND2   . ASN A 1 565 ? 0.283   9.682   31.041  1.00 63.35  ? 565 ASN A ND2   1 
ATOM   4415 N  N     . LEU A 1 566 ? 4.701   11.041  33.334  1.00 62.30  ? 566 LEU A N     1 
ATOM   4416 C  CA    . LEU A 1 566 ? 5.627   10.190  34.067  1.00 65.38  ? 566 LEU A CA    1 
ATOM   4417 C  C     . LEU A 1 566 ? 4.920   9.281   35.058  1.00 68.94  ? 566 LEU A C     1 
ATOM   4418 O  O     . LEU A 1 566 ? 5.585   8.640   35.880  1.00 75.95  ? 566 LEU A O     1 
ATOM   4419 C  CB    . LEU A 1 566 ? 6.661   11.046  34.797  1.00 64.42  ? 566 LEU A CB    1 
ATOM   4420 C  CG    . LEU A 1 566 ? 7.583   11.855  33.897  1.00 61.28  ? 566 LEU A CG    1 
ATOM   4421 C  CD1   . LEU A 1 566 ? 8.343   12.881  34.716  1.00 65.15  ? 566 LEU A CD1   1 
ATOM   4422 C  CD2   . LEU A 1 566 ? 8.532   10.915  33.183  1.00 58.74  ? 566 LEU A CD2   1 
ATOM   4423 N  N     . LYS A 1 567 ? 3.592   9.217   35.010  1.00 67.82  ? 567 LYS A N     1 
ATOM   4424 C  CA    . LYS A 1 567 ? 2.845   8.446   35.992  1.00 71.54  ? 567 LYS A CA    1 
ATOM   4425 C  C     . LYS A 1 567 ? 3.112   6.960   35.808  1.00 72.23  ? 567 LYS A C     1 
ATOM   4426 O  O     . LYS A 1 567 ? 3.259   6.473   34.682  1.00 65.54  ? 567 LYS A O     1 
ATOM   4427 C  CB    . LYS A 1 567 ? 1.350   8.749   35.874  1.00 75.79  ? 567 LYS A CB    1 
ATOM   4428 C  CG    . LYS A 1 567 ? 1.038   10.246  35.963  1.00 85.15  ? 567 LYS A CG    1 
ATOM   4429 C  CD    . LYS A 1 567 ? -0.429  10.551  35.694  1.00 92.31  ? 567 LYS A CD    1 
ATOM   4430 C  CE    . LYS A 1 567 ? -0.676  12.051  35.620  1.00 94.99  ? 567 LYS A CE    1 
ATOM   4431 N  NZ    . LYS A 1 567 ? -2.127  12.363  35.504  1.00 102.11 ? 567 LYS A NZ    1 
ATOM   4432 N  N     . GLY A 1 568 ? 3.193   6.240   36.927  1.00 75.13  ? 568 GLY A N     1 
ATOM   4433 C  CA    . GLY A 1 568 ? 3.570   4.847   36.916  1.00 73.81  ? 568 GLY A CA    1 
ATOM   4434 C  C     . GLY A 1 568 ? 5.060   4.590   36.998  1.00 79.70  ? 568 GLY A C     1 
ATOM   4435 O  O     . GLY A 1 568 ? 5.464   3.510   37.440  1.00 83.22  ? 568 GLY A O     1 
ATOM   4436 N  N     . LEU A 1 569 ? 5.893   5.536   36.566  1.00 82.61  ? 569 LEU A N     1 
ATOM   4437 C  CA    . LEU A 1 569 ? 7.331   5.434   36.796  1.00 87.05  ? 569 LEU A CA    1 
ATOM   4438 C  C     . LEU A 1 569 ? 7.681   5.976   38.181  1.00 99.22  ? 569 LEU A C     1 
ATOM   4439 O  O     . LEU A 1 569 ? 8.185   5.241   39.036  1.00 101.34 ? 569 LEU A O     1 
ATOM   4440 C  CB    . LEU A 1 569 ? 8.102   6.174   35.692  1.00 84.64  ? 569 LEU A CB    1 
ATOM   4441 C  CG    . LEU A 1 569 ? 7.769   5.855   34.225  1.00 69.65  ? 569 LEU A CG    1 
ATOM   4442 C  CD1   . LEU A 1 569 ? 8.660   6.655   33.271  1.00 65.09  ? 569 LEU A CD1   1 
ATOM   4443 C  CD2   . LEU A 1 569 ? 7.866   4.368   33.922  1.00 67.50  ? 569 LEU A CD2   1 
ATOM   4444 N  N     . GLY A 1 570 ? 7.396   7.257   38.421  1.00 114.39 ? 570 GLY A N     1 
ATOM   4445 C  CA    . GLY A 1 570 ? 7.542   7.854   39.737  1.00 106.94 ? 570 GLY A CA    1 
ATOM   4446 C  C     . GLY A 1 570 ? 8.974   8.083   40.175  1.00 113.47 ? 570 GLY A C     1 
ATOM   4447 O  O     . GLY A 1 570 ? 9.354   9.200   40.545  1.00 110.15 ? 570 GLY A O     1 
ATOM   4448 N  N     . ASP A 1 571 ? 9.777   7.022   40.131  1.00 115.83 ? 571 ASP A N     1 
ATOM   4449 C  CA    . ASP A 1 571 ? 11.159  7.027   40.594  1.00 111.54 ? 571 ASP A CA    1 
ATOM   4450 C  C     . ASP A 1 571 ? 12.125  7.674   39.614  1.00 107.98 ? 571 ASP A C     1 
ATOM   4451 O  O     . ASP A 1 571 ? 13.324  7.733   39.906  1.00 107.26 ? 571 ASP A O     1 
ATOM   4452 C  CB    . ASP A 1 571 ? 11.606  5.594   40.860  1.00 112.61 ? 571 ASP A CB    1 
ATOM   4453 C  CG    . ASP A 1 571 ? 11.273  4.659   39.708  1.00 118.39 ? 571 ASP A CG    1 
ATOM   4454 O  OD1   . ASP A 1 571 ? 10.826  5.151   38.650  1.00 110.90 ? 571 ASP A OD1   1 
ATOM   4455 O  OD2   . ASP A 1 571 ? 11.450  3.431   39.861  1.00 121.27 ? 571 ASP A OD2   1 
ATOM   4456 N  N     . VAL A 1 572 ? 11.643  8.142   38.465  1.00 106.59 ? 572 VAL A N     1 
ATOM   4457 C  CA    . VAL A 1 572 ? 12.528  8.652   37.426  1.00 101.54 ? 572 VAL A CA    1 
ATOM   4458 C  C     . VAL A 1 572 ? 13.180  9.948   37.891  1.00 93.68  ? 572 VAL A C     1 
ATOM   4459 O  O     . VAL A 1 572 ? 12.505  10.867  38.372  1.00 92.93  ? 572 VAL A O     1 
ATOM   4460 C  CB    . VAL A 1 572 ? 11.751  8.849   36.117  1.00 97.04  ? 572 VAL A CB    1 
ATOM   4461 C  CG1   . VAL A 1 572 ? 12.445  9.863   35.229  1.00 85.78  ? 572 VAL A CG1   1 
ATOM   4462 C  CG2   . VAL A 1 572 ? 11.599  7.513   35.393  1.00 89.48  ? 572 VAL A CG2   1 
ATOM   4463 N  N     . ASN A 1 573 ? 14.503  10.021  37.758  1.00 90.01  ? 573 ASN A N     1 
ATOM   4464 C  CA    . ASN A 1 573 ? 15.252  11.226  38.104  1.00 88.40  ? 573 ASN A CA    1 
ATOM   4465 C  C     . ASN A 1 573 ? 15.123  12.211  36.950  1.00 84.54  ? 573 ASN A C     1 
ATOM   4466 O  O     . ASN A 1 573 ? 15.803  12.087  35.929  1.00 82.23  ? 573 ASN A O     1 
ATOM   4467 C  CB    . ASN A 1 573 ? 16.710  10.889  38.397  1.00 89.28  ? 573 ASN A CB    1 
ATOM   4468 C  CG    . ASN A 1 573 ? 17.537  12.117  38.765  1.00 91.31  ? 573 ASN A CG    1 
ATOM   4469 O  OD1   . ASN A 1 573 ? 17.014  13.227  38.897  1.00 90.94  ? 573 ASN A OD1   1 
ATOM   4470 N  ND2   . ASN A 1 573 ? 18.838  11.915  38.942  1.00 94.28  ? 573 ASN A ND2   1 
ATOM   4471 N  N     . VAL A 1 574 ? 14.252  13.208  37.122  1.00 85.56  ? 574 VAL A N     1 
ATOM   4472 C  CA    . VAL A 1 574 ? 13.969  14.152  36.046  1.00 81.86  ? 574 VAL A CA    1 
ATOM   4473 C  C     . VAL A 1 574 ? 15.058  15.213  35.933  1.00 80.02  ? 574 VAL A C     1 
ATOM   4474 O  O     . VAL A 1 574 ? 15.270  15.776  34.852  1.00 73.75  ? 574 VAL A O     1 
ATOM   4475 C  CB    . VAL A 1 574 ? 12.585  14.790  36.256  1.00 79.08  ? 574 VAL A CB    1 
ATOM   4476 C  CG1   . VAL A 1 574 ? 11.511  13.715  36.290  1.00 80.18  ? 574 VAL A CG1   1 
ATOM   4477 C  CG2   . VAL A 1 574 ? 12.562  15.614  37.539  1.00 78.26  ? 574 VAL A CG2   1 
ATOM   4478 N  N     . GLU A 1 575 ? 15.758  15.511  37.028  1.00 83.88  ? 575 GLU A N     1 
ATOM   4479 C  CA    . GLU A 1 575 ? 16.809  16.520  36.975  1.00 83.67  ? 575 GLU A CA    1 
ATOM   4480 C  C     . GLU A 1 575 ? 17.967  16.052  36.104  1.00 74.86  ? 575 GLU A C     1 
ATOM   4481 O  O     . GLU A 1 575 ? 18.433  16.787  35.227  1.00 67.52  ? 575 GLU A O     1 
ATOM   4482 C  CB    . GLU A 1 575 ? 17.293  16.849  38.387  1.00 89.44  ? 575 GLU A CB    1 
ATOM   4483 C  CG    . GLU A 1 575 ? 16.222  17.437  39.285  1.00 94.56  ? 575 GLU A CG    1 
ATOM   4484 C  CD    . GLU A 1 575 ? 16.668  17.544  40.728  1.00 103.92 ? 575 GLU A CD    1 
ATOM   4485 O  OE1   . GLU A 1 575 ? 17.693  16.923  41.085  1.00 106.41 ? 575 GLU A OE1   1 
ATOM   4486 O  OE2   . GLU A 1 575 ? 15.994  18.250  41.507  1.00 106.93 ? 575 GLU A OE2   1 
ATOM   4487 N  N     . GLU A 1 576 ? 18.436  14.822  36.329  1.00 74.59  ? 576 GLU A N     1 
ATOM   4488 C  CA    . GLU A 1 576 ? 19.565  14.301  35.568  1.00 74.44  ? 576 GLU A CA    1 
ATOM   4489 C  C     . GLU A 1 576 ? 19.176  13.965  34.133  1.00 70.03  ? 576 GLU A C     1 
ATOM   4490 O  O     . GLU A 1 576 ? 20.021  14.030  33.232  1.00 68.88  ? 576 GLU A O     1 
ATOM   4491 C  CB    . GLU A 1 576 ? 20.135  13.069  36.269  1.00 81.90  ? 576 GLU A CB    1 
ATOM   4492 C  CG    . GLU A 1 576 ? 21.502  12.630  35.778  1.00 86.65  ? 576 GLU A CG    1 
ATOM   4493 C  CD    . GLU A 1 576 ? 22.092  11.517  36.632  1.00 95.22  ? 576 GLU A CD    1 
ATOM   4494 O  OE1   . GLU A 1 576 ? 21.495  11.188  37.681  1.00 96.61  ? 576 GLU A OE1   1 
ATOM   4495 O  OE2   . GLU A 1 576 ? 23.153  10.972  36.257  1.00 99.57  ? 576 GLU A OE2   1 
ATOM   4496 N  N     . LEU A 1 577 ? 17.909  13.613  33.895  1.00 69.34  ? 577 LEU A N     1 
ATOM   4497 C  CA    . LEU A 1 577 ? 17.499  13.231  32.547  1.00 64.19  ? 577 LEU A CA    1 
ATOM   4498 C  C     . LEU A 1 577 ? 17.426  14.425  31.607  1.00 58.39  ? 577 LEU A C     1 
ATOM   4499 O  O     . LEU A 1 577 ? 17.537  14.251  30.389  1.00 52.96  ? 577 LEU A O     1 
ATOM   4500 C  CB    . LEU A 1 577 ? 16.151  12.517  32.579  1.00 62.41  ? 577 LEU A CB    1 
ATOM   4501 C  CG    . LEU A 1 577 ? 16.223  11.014  32.343  1.00 62.18  ? 577 LEU A CG    1 
ATOM   4502 C  CD1   . LEU A 1 577 ? 14.833  10.411  32.415  1.00 62.93  ? 577 LEU A CD1   1 
ATOM   4503 C  CD2   . LEU A 1 577 ? 16.893  10.721  31.000  1.00 54.57  ? 577 LEU A CD2   1 
ATOM   4504 N  N     . PHE A 1 578 ? 17.217  15.631  32.142  1.00 57.09  ? 578 PHE A N     1 
ATOM   4505 C  CA    . PHE A 1 578 ? 17.166  16.839  31.325  1.00 58.24  ? 578 PHE A CA    1 
ATOM   4506 C  C     . PHE A 1 578 ? 18.240  17.849  31.698  1.00 58.28  ? 578 PHE A C     1 
ATOM   4507 O  O     . PHE A 1 578 ? 18.199  18.986  31.216  1.00 59.19  ? 578 PHE A O     1 
ATOM   4508 C  CB    . PHE A 1 578 ? 15.781  17.483  31.410  1.00 57.24  ? 578 PHE A CB    1 
ATOM   4509 C  CG    . PHE A 1 578 ? 14.739  16.770  30.594  1.00 54.49  ? 578 PHE A CG    1 
ATOM   4510 C  CD1   . PHE A 1 578 ? 14.617  17.026  29.234  1.00 50.69  ? 578 PHE A CD1   1 
ATOM   4511 C  CD2   . PHE A 1 578 ? 13.892  15.835  31.183  1.00 54.09  ? 578 PHE A CD2   1 
ATOM   4512 C  CE1   . PHE A 1 578 ? 13.668  16.374  28.469  1.00 45.47  ? 578 PHE A CE1   1 
ATOM   4513 C  CE2   . PHE A 1 578 ? 12.934  15.174  30.430  1.00 51.71  ? 578 PHE A CE2   1 
ATOM   4514 C  CZ    . PHE A 1 578 ? 12.818  15.443  29.071  1.00 48.16  ? 578 PHE A CZ    1 
ATOM   4515 N  N     . GLY A 1 579 ? 19.208  17.461  32.520  1.00 60.32  ? 579 GLY A N     1 
ATOM   4516 C  CA    . GLY A 1 579 ? 20.297  18.347  32.868  1.00 58.93  ? 579 GLY A CA    1 
ATOM   4517 C  C     . GLY A 1 579 ? 21.084  18.817  31.661  1.00 60.05  ? 579 GLY A C     1 
ATOM   4518 O  O     . GLY A 1 579 ? 21.508  18.008  30.829  1.00 57.97  ? 579 GLY A O     1 
ATOM   4519 N  N     . ILE A 1 580 ? 21.268  20.130  31.554  1.00 56.57  ? 580 ILE A N     1 
ATOM   4520 C  CA    . ILE A 1 580 ? 22.082  20.750  30.515  1.00 55.55  ? 580 ILE A CA    1 
ATOM   4521 C  C     . ILE A 1 580 ? 23.280  21.377  31.213  1.00 53.12  ? 580 ILE A C     1 
ATOM   4522 O  O     . ILE A 1 580 ? 23.160  22.418  31.861  1.00 54.25  ? 580 ILE A O     1 
ATOM   4523 C  CB    . ILE A 1 580 ? 21.297  21.794  29.716  1.00 57.05  ? 580 ILE A CB    1 
ATOM   4524 C  CG1   . ILE A 1 580 ? 20.127  21.135  28.985  1.00 56.56  ? 580 ILE A CG1   1 
ATOM   4525 C  CG2   . ILE A 1 580 ? 22.211  22.494  28.724  1.00 55.92  ? 580 ILE A CG2   1 
ATOM   4526 C  CD1   . ILE A 1 580 ? 19.356  22.099  28.105  1.00 56.70  ? 580 ILE A CD1   1 
ATOM   4527 N  N     . SER A 1 581 ? 24.437  20.741  31.106  1.00 54.68  ? 581 SER A N     1 
ATOM   4528 C  CA    . SER A 1 581 ? 25.646  21.262  31.719  1.00 55.58  ? 581 SER A CA    1 
ATOM   4529 C  C     . SER A 1 581 ? 26.412  22.114  30.715  1.00 53.42  ? 581 SER A C     1 
ATOM   4530 O  O     . SER A 1 581 ? 26.584  21.722  29.558  1.00 50.29  ? 581 SER A O     1 
ATOM   4531 C  CB    . SER A 1 581 ? 26.524  20.116  32.219  1.00 54.67  ? 581 SER A CB    1 
ATOM   4532 O  OG    . SER A 1 581 ? 27.848  20.557  32.452  1.00 58.75  ? 581 SER A OG    1 
ATOM   4533 N  N     . LYS A 1 582 ? 26.878  23.278  31.167  1.00 53.06  ? 582 LYS A N     1 
ATOM   4534 C  CA    . LYS A 1 582 ? 27.639  24.164  30.289  1.00 51.09  ? 582 LYS A CA    1 
ATOM   4535 C  C     . LYS A 1 582 ? 29.007  23.578  29.966  1.00 53.92  ? 582 LYS A C     1 
ATOM   4536 O  O     . LYS A 1 582 ? 29.482  23.684  28.828  1.00 53.95  ? 582 LYS A O     1 
ATOM   4537 C  CB    . LYS A 1 582 ? 27.788  25.544  30.936  1.00 54.74  ? 582 LYS A CB    1 
ATOM   4538 C  CG    . LYS A 1 582 ? 28.638  26.512  30.123  1.00 53.92  ? 582 LYS A CG    1 
ATOM   4539 C  CD    . LYS A 1 582 ? 28.745  27.877  30.805  1.00 58.68  ? 582 LYS A CD    1 
ATOM   4540 C  CE    . LYS A 1 582 ? 29.602  28.834  29.987  1.00 55.14  ? 582 LYS A CE    1 
ATOM   4541 N  NZ    . LYS A 1 582 ? 29.420  30.250  30.429  1.00 63.12  ? 582 LYS A NZ    1 
ATOM   4542 N  N     . GLU A 1 583 ? 29.652  22.961  30.958  1.00 54.02  ? 583 GLU A N     1 
ATOM   4543 C  CA    . GLU A 1 583 ? 30.931  22.295  30.733  1.00 56.57  ? 583 GLU A CA    1 
ATOM   4544 C  C     . GLU A 1 583 ? 30.811  21.214  29.662  1.00 52.74  ? 583 GLU A C     1 
ATOM   4545 O  O     . GLU A 1 583 ? 31.665  21.104  28.772  1.00 52.78  ? 583 GLU A O     1 
ATOM   4546 C  CB    . GLU A 1 583 ? 31.435  21.691  32.046  1.00 63.40  ? 583 GLU A CB    1 
ATOM   4547 C  CG    . GLU A 1 583 ? 31.366  22.636  33.234  1.00 70.54  ? 583 GLU A CG    1 
ATOM   4548 C  CD    . GLU A 1 583 ? 31.558  21.918  34.559  1.00 86.96  ? 583 GLU A CD    1 
ATOM   4549 O  OE1   . GLU A 1 583 ? 31.188  20.726  34.655  1.00 87.86  ? 583 GLU A OE1   1 
ATOM   4550 O  OE2   . GLU A 1 583 ? 32.082  22.544  35.506  1.00 93.43  ? 583 GLU A OE2   1 
ATOM   4551 N  N     . PHE A 1 584 ? 29.761  20.395  29.735  1.00 52.98  ? 584 PHE A N     1 
ATOM   4552 C  CA    . PHE A 1 584 ? 29.603  19.338  28.741  1.00 50.14  ? 584 PHE A CA    1 
ATOM   4553 C  C     . PHE A 1 584 ? 29.413  19.926  27.349  1.00 47.42  ? 584 PHE A C     1 
ATOM   4554 O  O     . PHE A 1 584 ? 30.075  19.515  26.389  1.00 45.29  ? 584 PHE A O     1 
ATOM   4555 C  CB    . PHE A 1 584 ? 28.425  18.427  29.092  1.00 48.41  ? 584 PHE A CB    1 
ATOM   4556 C  CG    . PHE A 1 584 ? 28.123  17.411  28.020  1.00 47.31  ? 584 PHE A CG    1 
ATOM   4557 C  CD1   . PHE A 1 584 ? 28.848  16.235  27.947  1.00 47.25  ? 584 PHE A CD1   1 
ATOM   4558 C  CD2   . PHE A 1 584 ? 27.134  17.639  27.080  1.00 44.53  ? 584 PHE A CD2   1 
ATOM   4559 C  CE1   . PHE A 1 584 ? 28.595  15.311  26.959  1.00 45.63  ? 584 PHE A CE1   1 
ATOM   4560 C  CE2   . PHE A 1 584 ? 26.881  16.714  26.081  1.00 44.60  ? 584 PHE A CE2   1 
ATOM   4561 C  CZ    . PHE A 1 584 ? 27.616  15.545  26.027  1.00 42.67  ? 584 PHE A CZ    1 
ATOM   4562 N  N     . TRP A 1 585 ? 28.513  20.899  27.224  1.00 46.94  ? 585 TRP A N     1 
ATOM   4563 C  CA    . TRP A 1 585 ? 28.168  21.432  25.910  1.00 48.16  ? 585 TRP A CA    1 
ATOM   4564 C  C     . TRP A 1 585 ? 29.243  22.344  25.322  1.00 45.53  ? 585 TRP A C     1 
ATOM   4565 O  O     . TRP A 1 585 ? 29.287  22.513  24.098  1.00 43.43  ? 585 TRP A O     1 
ATOM   4566 C  CB    . TRP A 1 585 ? 26.822  22.141  25.995  1.00 46.00  ? 585 TRP A CB    1 
ATOM   4567 C  CG    . TRP A 1 585 ? 25.740  21.133  26.008  1.00 47.10  ? 585 TRP A CG    1 
ATOM   4568 C  CD1   . TRP A 1 585 ? 25.088  20.625  27.107  1.00 47.96  ? 585 TRP A CD1   1 
ATOM   4569 C  CD2   . TRP A 1 585 ? 25.226  20.430  24.876  1.00 46.01  ? 585 TRP A CD2   1 
ATOM   4570 N  NE1   . TRP A 1 585 ? 24.178  19.678  26.714  1.00 46.68  ? 585 TRP A NE1   1 
ATOM   4571 C  CE2   . TRP A 1 585 ? 24.245  19.534  25.351  1.00 43.57  ? 585 TRP A CE2   1 
ATOM   4572 C  CE3   . TRP A 1 585 ? 25.491  20.480  23.503  1.00 42.92  ? 585 TRP A CE3   1 
ATOM   4573 C  CZ2   . TRP A 1 585 ? 23.519  18.701  24.502  1.00 43.02  ? 585 TRP A CZ2   1 
ATOM   4574 C  CZ3   . TRP A 1 585 ? 24.769  19.653  22.662  1.00 46.92  ? 585 TRP A CZ3   1 
ATOM   4575 C  CH2   . TRP A 1 585 ? 23.796  18.773  23.164  1.00 45.65  ? 585 TRP A CH2   1 
ATOM   4576 N  N     . GLU A 1 586 ? 30.115  22.922  26.147  1.00 44.83  ? 586 GLU A N     1 
ATOM   4577 C  CA    . GLU A 1 586 ? 31.258  23.640  25.593  1.00 46.32  ? 586 GLU A CA    1 
ATOM   4578 C  C     . GLU A 1 586 ? 32.220  22.683  24.896  1.00 49.22  ? 586 GLU A C     1 
ATOM   4579 O  O     . GLU A 1 586 ? 32.741  22.994  23.818  1.00 46.51  ? 586 GLU A O     1 
ATOM   4580 C  CB    . GLU A 1 586 ? 31.972  24.419  26.698  1.00 53.44  ? 586 GLU A CB    1 
ATOM   4581 C  CG    . GLU A 1 586 ? 31.236  25.682  27.114  1.00 54.82  ? 586 GLU A CG    1 
ATOM   4582 C  CD    . GLU A 1 586 ? 31.984  26.475  28.157  1.00 62.86  ? 586 GLU A CD    1 
ATOM   4583 O  OE1   . GLU A 1 586 ? 32.671  25.859  28.999  1.00 60.63  ? 586 GLU A OE1   1 
ATOM   4584 O  OE2   . GLU A 1 586 ? 31.892  27.722  28.126  1.00 69.26  ? 586 GLU A OE2   1 
ATOM   4585 N  N     . LYS A 1 587 ? 32.464  21.508  25.492  1.00 45.20  ? 587 LYS A N     1 
ATOM   4586 C  CA    . LYS A 1 587 ? 33.313  20.513  24.848  1.00 45.33  ? 587 LYS A CA    1 
ATOM   4587 C  C     . LYS A 1 587 ? 32.628  19.916  23.627  1.00 41.90  ? 587 LYS A C     1 
ATOM   4588 O  O     . LYS A 1 587 ? 33.284  19.601  22.628  1.00 43.23  ? 587 LYS A O     1 
ATOM   4589 C  CB    . LYS A 1 587 ? 33.675  19.413  25.845  1.00 47.69  ? 587 LYS A CB    1 
ATOM   4590 C  CG    . LYS A 1 587 ? 34.257  19.924  27.153  1.00 56.98  ? 587 LYS A CG    1 
ATOM   4591 C  CD    . LYS A 1 587 ? 34.539  18.769  28.118  1.00 67.13  ? 587 LYS A CD    1 
ATOM   4592 C  CE    . LYS A 1 587 ? 34.884  19.257  29.525  1.00 73.49  ? 587 LYS A CE    1 
ATOM   4593 N  NZ    . LYS A 1 587 ? 36.092  20.131  29.556  1.00 78.33  ? 587 LYS A NZ    1 
ATOM   4594 N  N     . GLU A 1 588 ? 31.309  19.747  23.691  1.00 41.99  ? 588 GLU A N     1 
ATOM   4595 C  CA    . GLU A 1 588 ? 30.584  19.148  22.576  1.00 41.73  ? 588 GLU A CA    1 
ATOM   4596 C  C     . GLU A 1 588 ? 30.676  20.016  21.326  1.00 38.81  ? 588 GLU A C     1 
ATOM   4597 O  O     . GLU A 1 588 ? 30.897  19.511  20.219  1.00 36.99  ? 588 GLU A O     1 
ATOM   4598 C  CB    . GLU A 1 588 ? 29.129  18.924  22.974  1.00 41.37  ? 588 GLU A CB    1 
ATOM   4599 C  CG    . GLU A 1 588 ? 28.336  18.050  22.020  1.00 39.00  ? 588 GLU A CG    1 
ATOM   4600 C  CD    . GLU A 1 588 ? 28.791  16.591  22.002  1.00 40.48  ? 588 GLU A CD    1 
ATOM   4601 O  OE1   . GLU A 1 588 ? 29.475  16.137  22.948  1.00 38.46  ? 588 GLU A OE1   1 
ATOM   4602 O  OE2   . GLU A 1 588 ? 28.449  15.896  21.024  1.00 35.59  ? 588 GLU A OE2   1 
ATOM   4603 N  N     . VAL A 1 589 ? 30.490  21.326  21.475  1.00 39.16  ? 589 VAL A N     1 
ATOM   4604 C  CA    . VAL A 1 589 ? 30.551  22.207  20.304  1.00 40.20  ? 589 VAL A CA    1 
ATOM   4605 C  C     . VAL A 1 589 ? 31.961  22.245  19.724  1.00 41.39  ? 589 VAL A C     1 
ATOM   4606 O  O     . VAL A 1 589 ? 32.136  22.308  18.500  1.00 42.94  ? 589 VAL A O     1 
ATOM   4607 C  CB    . VAL A 1 589 ? 30.047  23.623  20.647  1.00 45.62  ? 589 VAL A CB    1 
ATOM   4608 C  CG1   . VAL A 1 589 ? 28.583  23.574  21.019  1.00 47.05  ? 589 VAL A CG1   1 
ATOM   4609 C  CG2   . VAL A 1 589 ? 30.843  24.214  21.766  1.00 46.30  ? 589 VAL A CG2   1 
ATOM   4610 N  N     . GLU A 1 590 ? 32.987  22.224  20.583  1.00 40.29  ? 590 GLU A N     1 
ATOM   4611 C  CA    . GLU A 1 590 ? 34.364  22.150  20.105  1.00 38.97  ? 590 GLU A CA    1 
ATOM   4612 C  C     . GLU A 1 590 ? 34.582  20.921  19.226  1.00 43.93  ? 590 GLU A C     1 
ATOM   4613 O  O     . GLU A 1 590 ? 35.194  21.009  18.154  1.00 43.92  ? 590 GLU A O     1 
ATOM   4614 C  CB    . GLU A 1 590 ? 35.333  22.129  21.292  1.00 44.26  ? 590 GLU A CB    1 
ATOM   4615 C  CG    . GLU A 1 590 ? 35.507  23.458  22.006  1.00 56.06  ? 590 GLU A CG    1 
ATOM   4616 C  CD    . GLU A 1 590 ? 36.628  23.412  23.033  1.00 63.65  ? 590 GLU A CD    1 
ATOM   4617 O  OE1   . GLU A 1 590 ? 37.391  22.421  23.028  1.00 67.06  ? 590 GLU A OE1   1 
ATOM   4618 O  OE2   . GLU A 1 590 ? 36.745  24.358  23.843  1.00 67.22  ? 590 GLU A OE2   1 
ATOM   4619 N  N     . GLU A 1 591 ? 34.088  19.757  19.666  1.00 39.50  ? 591 GLU A N     1 
ATOM   4620 C  CA    . GLU A 1 591 ? 34.296  18.542  18.887  1.00 41.68  ? 591 GLU A CA    1 
ATOM   4621 C  C     . GLU A 1 591 ? 33.501  18.575  17.593  1.00 41.17  ? 591 GLU A C     1 
ATOM   4622 O  O     . GLU A 1 591 ? 33.964  18.051  16.572  1.00 42.73  ? 591 GLU A O     1 
ATOM   4623 C  CB    . GLU A 1 591 ? 33.936  17.296  19.716  1.00 38.63  ? 591 GLU A CB    1 
ATOM   4624 C  CG    . GLU A 1 591 ? 34.929  17.002  20.830  1.00 42.18  ? 591 GLU A CG    1 
ATOM   4625 C  CD    . GLU A 1 591 ? 36.365  16.821  20.323  1.00 51.20  ? 591 GLU A CD    1 
ATOM   4626 O  OE1   . GLU A 1 591 ? 36.566  16.083  19.332  1.00 47.77  ? 591 GLU A OE1   1 
ATOM   4627 O  OE2   . GLU A 1 591 ? 37.294  17.424  20.912  1.00 50.47  ? 591 GLU A OE2   1 
ATOM   4628 N  N     . ILE A 1 592 ? 32.311  19.175  17.612  1.00 36.14  ? 592 ILE A N     1 
ATOM   4629 C  CA    . ILE A 1 592 ? 31.540  19.304  16.379  1.00 39.53  ? 592 ILE A CA    1 
ATOM   4630 C  C     . ILE A 1 592 ? 32.255  20.247  15.414  1.00 41.00  ? 592 ILE A C     1 
ATOM   4631 O  O     . ILE A 1 592 ? 32.377  19.966  14.214  1.00 41.15  ? 592 ILE A O     1 
ATOM   4632 C  CB    . ILE A 1 592 ? 30.114  19.789  16.703  1.00 37.17  ? 592 ILE A CB    1 
ATOM   4633 C  CG1   . ILE A 1 592 ? 29.393  18.794  17.613  1.00 40.35  ? 592 ILE A CG1   1 
ATOM   4634 C  CG2   . ILE A 1 592 ? 29.310  20.013  15.438  1.00 37.77  ? 592 ILE A CG2   1 
ATOM   4635 C  CD1   . ILE A 1 592 ? 28.125  19.359  18.223  1.00 39.00  ? 592 ILE A CD1   1 
ATOM   4636 N  N     . ASP A 1 593 ? 32.751  21.369  15.934  1.00 40.14  ? 593 ASP A N     1 
ATOM   4637 C  CA    . ASP A 1 593 ? 33.504  22.338  15.137  1.00 38.30  ? 593 ASP A CA    1 
ATOM   4638 C  C     . ASP A 1 593 ? 34.685  21.670  14.438  1.00 46.29  ? 593 ASP A C     1 
ATOM   4639 O  O     . ASP A 1 593 ? 34.806  21.717  13.207  1.00 44.60  ? 593 ASP A O     1 
ATOM   4640 C  CB    . ASP A 1 593 ? 33.975  23.467  16.060  1.00 44.13  ? 593 ASP A CB    1 
ATOM   4641 C  CG    . ASP A 1 593 ? 34.349  24.741  15.314  1.00 49.19  ? 593 ASP A CG    1 
ATOM   4642 O  OD1   . ASP A 1 593 ? 34.808  24.665  14.159  1.00 50.67  ? 593 ASP A OD1   1 
ATOM   4643 O  OD2   . ASP A 1 593 ? 34.190  25.824  15.904  1.00 52.37  ? 593 ASP A OD2   1 
ATOM   4644 N  N     . LYS A 1 594 ? 35.559  21.017  15.219  1.00 42.44  ? 594 LYS A N     1 
ATOM   4645 C  CA    . LYS A 1 594 ? 36.729  20.352  14.654  1.00 41.86  ? 594 LYS A CA    1 
ATOM   4646 C  C     . LYS A 1 594 ? 36.339  19.337  13.590  1.00 43.68  ? 594 LYS A C     1 
ATOM   4647 O  O     . LYS A 1 594 ? 37.002  19.219  12.550  1.00 40.80  ? 594 LYS A O     1 
ATOM   4648 C  CB    . LYS A 1 594 ? 37.521  19.665  15.765  1.00 43.93  ? 594 LYS A CB    1 
ATOM   4649 C  CG    . LYS A 1 594 ? 38.189  20.625  16.701  1.00 48.45  ? 594 LYS A CG    1 
ATOM   4650 C  CD    . LYS A 1 594 ? 39.254  19.916  17.513  1.00 52.39  ? 594 LYS A CD    1 
ATOM   4651 C  CE    . LYS A 1 594 ? 38.644  18.866  18.415  1.00 44.91  ? 594 LYS A CE    1 
ATOM   4652 N  NZ    . LYS A 1 594 ? 39.522  18.657  19.612  1.00 51.82  ? 594 LYS A NZ    1 
ATOM   4653 N  N     . TYR A 1 595 ? 35.262  18.595  13.834  1.00 42.16  ? 595 TYR A N     1 
ATOM   4654 C  CA    . TYR A 1 595 ? 34.870  17.540  12.912  1.00 42.27  ? 595 TYR A CA    1 
ATOM   4655 C  C     . TYR A 1 595 ? 34.357  18.125  11.600  1.00 41.76  ? 595 TYR A C     1 
ATOM   4656 O  O     . TYR A 1 595 ? 34.817  17.745  10.517  1.00 45.19  ? 595 TYR A O     1 
ATOM   4657 C  CB    . TYR A 1 595 ? 33.827  16.647  13.582  1.00 38.20  ? 595 TYR A CB    1 
ATOM   4658 C  CG    . TYR A 1 595 ? 33.190  15.640  12.671  1.00 40.37  ? 595 TYR A CG    1 
ATOM   4659 C  CD1   . TYR A 1 595 ? 33.789  14.412  12.430  1.00 39.16  ? 595 TYR A CD1   1 
ATOM   4660 C  CD2   . TYR A 1 595 ? 31.973  15.908  12.066  1.00 40.93  ? 595 TYR A CD2   1 
ATOM   4661 C  CE1   . TYR A 1 595 ? 33.197  13.484  11.590  1.00 40.91  ? 595 TYR A CE1   1 
ATOM   4662 C  CE2   . TYR A 1 595 ? 31.375  14.996  11.240  1.00 39.18  ? 595 TYR A CE2   1 
ATOM   4663 C  CZ    . TYR A 1 595 ? 31.987  13.795  10.997  1.00 39.90  ? 595 TYR A CZ    1 
ATOM   4664 O  OH    . TYR A 1 595 ? 31.367  12.887  10.165  1.00 47.40  ? 595 TYR A OH    1 
ATOM   4665 N  N     . LEU A 1 596 ? 33.424  19.071  11.677  1.00 36.89  ? 596 LEU A N     1 
ATOM   4666 C  CA    . LEU A 1 596 ? 32.893  19.683  10.463  1.00 42.37  ? 596 LEU A CA    1 
ATOM   4667 C  C     . LEU A 1 596 ? 33.982  20.414  9.685   1.00 43.71  ? 596 LEU A C     1 
ATOM   4668 O  O     . LEU A 1 596 ? 34.024  20.350  8.450   1.00 44.30  ? 596 LEU A O     1 
ATOM   4669 C  CB    . LEU A 1 596 ? 31.761  20.649  10.814  1.00 43.24  ? 596 LEU A CB    1 
ATOM   4670 C  CG    . LEU A 1 596 ? 30.481  20.083  11.437  1.00 38.77  ? 596 LEU A CG    1 
ATOM   4671 C  CD1   . LEU A 1 596 ? 29.586  21.231  11.879  1.00 46.30  ? 596 LEU A CD1   1 
ATOM   4672 C  CD2   . LEU A 1 596 ? 29.750  19.180  10.466  1.00 40.23  ? 596 LEU A CD2   1 
ATOM   4673 N  N     . GLU A 1 597 ? 34.870  21.124  10.390  1.00 42.09  ? 597 GLU A N     1 
ATOM   4674 C  CA    . GLU A 1 597 ? 35.913  21.885  9.705   1.00 47.20  ? 597 GLU A CA    1 
ATOM   4675 C  C     . GLU A 1 597 ? 36.875  20.960  8.972   1.00 47.68  ? 597 GLU A C     1 
ATOM   4676 O  O     . GLU A 1 597 ? 37.250  21.228  7.823   1.00 49.31  ? 597 GLU A O     1 
ATOM   4677 C  CB    . GLU A 1 597 ? 36.656  22.777  10.706  1.00 44.74  ? 597 GLU A CB    1 
ATOM   4678 C  CG    . GLU A 1 597 ? 38.108  23.044  10.365  1.00 52.09  ? 597 GLU A CG    1 
ATOM   4679 C  CD    . GLU A 1 597 ? 38.647  24.284  11.062  1.00 63.63  ? 597 GLU A CD    1 
ATOM   4680 O  OE1   . GLU A 1 597 ? 37.980  24.788  11.998  1.00 65.57  ? 597 GLU A OE1   1 
ATOM   4681 O  OE2   . GLU A 1 597 ? 39.728  24.766  10.661  1.00 70.00  ? 597 GLU A OE2   1 
ATOM   4682 N  N     . ASP A 1 598 ? 37.278  19.858  9.610   1.00 44.66  ? 598 ASP A N     1 
ATOM   4683 C  CA    . ASP A 1 598 ? 38.186  18.936  8.939   1.00 48.61  ? 598 ASP A CA    1 
ATOM   4684 C  C     . ASP A 1 598 ? 37.464  18.155  7.855   1.00 45.20  ? 598 ASP A C     1 
ATOM   4685 O  O     . ASP A 1 598 ? 37.919  18.105  6.709   1.00 48.30  ? 598 ASP A O     1 
ATOM   4686 C  CB    . ASP A 1 598 ? 38.838  17.974  9.934   1.00 49.26  ? 598 ASP A CB    1 
ATOM   4687 C  CG    . ASP A 1 598 ? 39.838  17.045  9.257   1.00 57.16  ? 598 ASP A CG    1 
ATOM   4688 O  OD1   . ASP A 1 598 ? 40.576  17.540  8.373   1.00 58.04  ? 598 ASP A OD1   1 
ATOM   4689 O  OD2   . ASP A 1 598 ? 39.893  15.836  9.593   1.00 52.23  ? 598 ASP A OD2   1 
ATOM   4690 N  N     . GLN A 1 599 ? 36.315  17.577  8.187   1.00 43.59  ? 599 GLN A N     1 
ATOM   4691 C  CA    . GLN A 1 599 ? 35.719  16.552  7.346   1.00 41.62  ? 599 GLN A CA    1 
ATOM   4692 C  C     . GLN A 1 599 ? 34.838  17.106  6.234   1.00 44.25  ? 599 GLN A C     1 
ATOM   4693 O  O     . GLN A 1 599 ? 34.697  16.451  5.195   1.00 42.11  ? 599 GLN A O     1 
ATOM   4694 C  CB    . GLN A 1 599 ? 34.914  15.584  8.214   1.00 41.78  ? 599 GLN A CB    1 
ATOM   4695 C  CG    . GLN A 1 599 ? 35.784  14.717  9.114   1.00 45.18  ? 599 GLN A CG    1 
ATOM   4696 C  CD    . GLN A 1 599 ? 36.568  13.688  8.326   1.00 48.78  ? 599 GLN A CD    1 
ATOM   4697 O  OE1   . GLN A 1 599 ? 35.991  12.891  7.592   1.00 46.71  ? 599 GLN A OE1   1 
ATOM   4698 N  NE2   . GLN A 1 599 ? 37.895  13.715  8.456   1.00 50.82  ? 599 GLN A NE2   1 
ATOM   4699 N  N     . VAL A 1 600 ? 34.225  18.279  6.408   1.00 41.15  ? 600 VAL A N     1 
ATOM   4700 C  CA    . VAL A 1 600 ? 33.421  18.862  5.346   1.00 41.82  ? 600 VAL A CA    1 
ATOM   4701 C  C     . VAL A 1 600 ? 34.113  20.047  4.672   1.00 42.80  ? 600 VAL A C     1 
ATOM   4702 O  O     . VAL A 1 600 ? 33.932  20.244  3.466   1.00 43.48  ? 600 VAL A O     1 
ATOM   4703 C  CB    . VAL A 1 600 ? 32.015  19.256  5.847   1.00 42.59  ? 600 VAL A CB    1 
ATOM   4704 C  CG1   . VAL A 1 600 ? 31.019  19.268  4.686   1.00 40.11  ? 600 VAL A CG1   1 
ATOM   4705 C  CG2   . VAL A 1 600 ? 31.544  18.293  6.926   1.00 42.36  ? 600 VAL A CG2   1 
ATOM   4706 N  N     . ASN A 1 601 ? 34.890  20.842  5.412   1.00 42.34  ? 601 ASN A N     1 
ATOM   4707 C  CA    . ASN A 1 601 ? 35.893  21.760  4.855   1.00 45.47  ? 601 ASN A CA    1 
ATOM   4708 C  C     . ASN A 1 601 ? 35.200  22.716  3.889   1.00 44.25  ? 601 ASN A C     1 
ATOM   4709 O  O     . ASN A 1 601 ? 34.218  23.356  4.298   1.00 42.09  ? 601 ASN A O     1 
ATOM   4710 C  CB    . ASN A 1 601 ? 37.037  20.930  4.263   1.00 45.94  ? 601 ASN A CB    1 
ATOM   4711 C  CG    . ASN A 1 601 ? 38.246  21.763  3.928   1.00 53.69  ? 601 ASN A CG    1 
ATOM   4712 O  OD1   . ASN A 1 601 ? 38.310  22.947  4.275   1.00 55.94  ? 601 ASN A OD1   1 
ATOM   4713 N  ND2   . ASN A 1 601 ? 39.223  21.156  3.252   1.00 52.12  ? 601 ASN A ND2   1 
ATOM   4714 N  N     . ALA A 1 602 ? 35.616  22.808  2.622   1.00 41.54  ? 602 ALA A N     1 
ATOM   4715 C  CA    . ALA A 1 602 ? 35.077  23.810  1.704   1.00 44.67  ? 602 ALA A CA    1 
ATOM   4716 C  C     . ALA A 1 602 ? 33.645  23.527  1.257   1.00 45.93  ? 602 ALA A C     1 
ATOM   4717 O  O     . ALA A 1 602 ? 33.015  24.418  0.678   1.00 44.01  ? 602 ALA A O     1 
ATOM   4718 C  CB    . ALA A 1 602 ? 35.980  23.926  0.479   1.00 48.28  ? 602 ALA A CB    1 
ATOM   4719 N  N     . ASP A 1 603 ? 33.110  22.329  1.504   1.00 38.10  ? 603 ASP A N     1 
ATOM   4720 C  CA    . ASP A 1 603 ? 31.753  21.999  1.089   1.00 42.42  ? 603 ASP A CA    1 
ATOM   4721 C  C     . ASP A 1 603 ? 30.733  22.162  2.212   1.00 38.70  ? 603 ASP A C     1 
ATOM   4722 O  O     . ASP A 1 603 ? 29.581  21.756  2.046   1.00 35.61  ? 603 ASP A O     1 
ATOM   4723 C  CB    . ASP A 1 603 ? 31.704  20.574  0.525   1.00 42.10  ? 603 ASP A CB    1 
ATOM   4724 C  CG    . ASP A 1 603 ? 32.409  20.464  -0.821  1.00 50.92  ? 603 ASP A CG    1 
ATOM   4725 O  OD1   . ASP A 1 603 ? 32.114  21.278  -1.724  1.00 49.37  ? 603 ASP A OD1   1 
ATOM   4726 O  OD2   . ASP A 1 603 ? 33.277  19.584  -0.967  1.00 49.95  ? 603 ASP A OD2   1 
ATOM   4727 N  N     . LEU A 1 604 ? 31.123  22.758  3.334   1.00 39.49  ? 604 LEU A N     1 
ATOM   4728 C  CA    . LEU A 1 604 ? 30.191  22.979  4.438   1.00 38.62  ? 604 LEU A CA    1 
ATOM   4729 C  C     . LEU A 1 604 ? 29.282  24.154  4.106   1.00 38.88  ? 604 LEU A C     1 
ATOM   4730 O  O     . LEU A 1 604 ? 29.785  25.247  3.836   1.00 39.63  ? 604 LEU A O     1 
ATOM   4731 C  CB    . LEU A 1 604 ? 30.951  23.261  5.727   1.00 40.30  ? 604 LEU A CB    1 
ATOM   4732 C  CG    . LEU A 1 604 ? 30.136  23.443  7.010   1.00 36.65  ? 604 LEU A CG    1 
ATOM   4733 C  CD1   . LEU A 1 604 ? 29.402  22.185  7.410   1.00 40.01  ? 604 LEU A CD1   1 
ATOM   4734 C  CD2   . LEU A 1 604 ? 31.058  23.908  8.134   1.00 44.04  ? 604 LEU A CD2   1 
ATOM   4735 N  N     . PRO A 1 605 ? 27.963  23.979  4.090   1.00 38.62  ? 605 PRO A N     1 
ATOM   4736 C  CA    . PRO A 1 605 ? 27.084  25.107  3.766   1.00 38.49  ? 605 PRO A CA    1 
ATOM   4737 C  C     . PRO A 1 605 ? 27.133  26.171  4.848   1.00 38.49  ? 605 PRO A C     1 
ATOM   4738 O  O     . PRO A 1 605 ? 27.262  25.871  6.037   1.00 38.48  ? 605 PRO A O     1 
ATOM   4739 C  CB    . PRO A 1 605 ? 25.694  24.464  3.680   1.00 37.83  ? 605 PRO A CB    1 
ATOM   4740 C  CG    . PRO A 1 605 ? 25.966  22.998  3.405   1.00 36.95  ? 605 PRO A CG    1 
ATOM   4741 C  CD    . PRO A 1 605 ? 27.235  22.698  4.145   1.00 36.73  ? 605 PRO A CD    1 
ATOM   4742 N  N     . TYR A 1 606 ? 27.014  27.430  4.422   1.00 39.12  ? 606 TYR A N     1 
ATOM   4743 C  CA    . TYR A 1 606 ? 27.083  28.535  5.378   1.00 38.03  ? 606 TYR A CA    1 
ATOM   4744 C  C     . TYR A 1 606 ? 26.028  28.418  6.483   1.00 40.79  ? 606 TYR A C     1 
ATOM   4745 O  O     . TYR A 1 606 ? 26.323  28.677  7.653   1.00 38.94  ? 606 TYR A O     1 
ATOM   4746 C  CB    . TYR A 1 606 ? 26.931  29.867  4.668   1.00 45.54  ? 606 TYR A CB    1 
ATOM   4747 C  CG    . TYR A 1 606 ? 26.811  30.986  5.662   1.00 49.35  ? 606 TYR A CG    1 
ATOM   4748 C  CD1   . TYR A 1 606 ? 27.893  31.343  6.457   1.00 49.33  ? 606 TYR A CD1   1 
ATOM   4749 C  CD2   . TYR A 1 606 ? 25.608  31.655  5.842   1.00 48.35  ? 606 TYR A CD2   1 
ATOM   4750 C  CE1   . TYR A 1 606 ? 27.784  32.370  7.386   1.00 55.32  ? 606 TYR A CE1   1 
ATOM   4751 C  CE2   . TYR A 1 606 ? 25.494  32.686  6.761   1.00 52.04  ? 606 TYR A CE2   1 
ATOM   4752 C  CZ    . TYR A 1 606 ? 26.583  33.032  7.533   1.00 47.45  ? 606 TYR A CZ    1 
ATOM   4753 O  OH    . TYR A 1 606 ? 26.473  34.049  8.452   1.00 65.61  ? 606 TYR A OH    1 
ATOM   4754 N  N     . GLU A 1 607 ? 24.793  28.044  6.135   1.00 36.56  ? 607 GLU A N     1 
ATOM   4755 C  CA    . GLU A 1 607 ? 23.742  27.925  7.144   1.00 43.19  ? 607 GLU A CA    1 
ATOM   4756 C  C     . GLU A 1 607 ? 24.092  26.920  8.238   1.00 40.67  ? 607 GLU A C     1 
ATOM   4757 O  O     . GLU A 1 607 ? 23.664  27.085  9.385   1.00 41.12  ? 607 GLU A O     1 
ATOM   4758 C  CB    . GLU A 1 607 ? 22.419  27.552  6.475   1.00 38.62  ? 607 GLU A CB    1 
ATOM   4759 C  CG    . GLU A 1 607 ? 21.905  28.671  5.565   1.00 51.60  ? 607 GLU A CG    1 
ATOM   4760 C  CD    . GLU A 1 607 ? 20.492  28.429  5.094   1.00 55.37  ? 607 GLU A CD    1 
ATOM   4761 O  OE1   . GLU A 1 607 ? 20.191  27.304  4.656   1.00 53.06  ? 607 GLU A OE1   1 
ATOM   4762 O  OE2   . GLU A 1 607 ? 19.672  29.357  5.179   1.00 64.84  ? 607 GLU A OE2   1 
ATOM   4763 N  N     . ILE A 1 608 ? 24.870  25.885  7.919   1.00 37.42  ? 608 ILE A N     1 
ATOM   4764 C  CA    . ILE A 1 608 ? 25.301  24.951  8.960   1.00 39.41  ? 608 ILE A CA    1 
ATOM   4765 C  C     . ILE A 1 608 ? 26.353  25.604  9.851   1.00 39.10  ? 608 ILE A C     1 
ATOM   4766 O  O     . ILE A 1 608 ? 26.302  25.497  11.084  1.00 36.81  ? 608 ILE A O     1 
ATOM   4767 C  CB    . ILE A 1 608 ? 25.829  23.646  8.336   1.00 35.54  ? 608 ILE A CB    1 
ATOM   4768 C  CG1   . ILE A 1 608 ? 24.739  22.966  7.498   1.00 36.19  ? 608 ILE A CG1   1 
ATOM   4769 C  CG2   . ILE A 1 608 ? 26.383  22.745  9.419   1.00 38.10  ? 608 ILE A CG2   1 
ATOM   4770 C  CD1   . ILE A 1 608 ? 23.478  22.549  8.307   1.00 36.13  ? 608 ILE A CD1   1 
ATOM   4771 N  N     . GLU A 1 609 ? 27.324  26.287  9.242   1.00 35.80  ? 609 GLU A N     1 
ATOM   4772 C  CA    . GLU A 1 609 ? 28.306  27.031  10.027  1.00 43.38  ? 609 GLU A CA    1 
ATOM   4773 C  C     . GLU A 1 609 ? 27.637  28.093  10.895  1.00 40.51  ? 609 GLU A C     1 
ATOM   4774 O  O     . GLU A 1 609 ? 28.057  28.323  12.035  1.00 41.08  ? 609 GLU A O     1 
ATOM   4775 C  CB    . GLU A 1 609 ? 29.345  27.683  9.113   1.00 43.31  ? 609 GLU A CB    1 
ATOM   4776 C  CG    . GLU A 1 609 ? 30.307  28.593  9.874   1.00 50.56  ? 609 GLU A CG    1 
ATOM   4777 C  CD    . GLU A 1 609 ? 31.371  29.198  8.991   1.00 59.47  ? 609 GLU A CD    1 
ATOM   4778 O  OE1   . GLU A 1 609 ? 31.244  29.104  7.750   1.00 62.63  ? 609 GLU A OE1   1 
ATOM   4779 O  OE2   . GLU A 1 609 ? 32.336  29.765  9.543   1.00 68.18  ? 609 GLU A OE2   1 
ATOM   4780 N  N     . ARG A 1 610 ? 26.593  28.748  10.378  1.00 39.93  ? 610 ARG A N     1 
ATOM   4781 C  CA    . ARG A 1 610 ? 25.879  29.741  11.176  1.00 38.51  ? 610 ARG A CA    1 
ATOM   4782 C  C     . ARG A 1 610 ? 25.196  29.116  12.389  1.00 36.38  ? 610 ARG A C     1 
ATOM   4783 O  O     . ARG A 1 610 ? 25.153  29.728  13.460  1.00 38.71  ? 610 ARG A O     1 
ATOM   4784 C  CB    . ARG A 1 610 ? 24.846  30.470  10.326  1.00 43.86  ? 610 ARG A CB    1 
ATOM   4785 C  CG    . ARG A 1 610 ? 24.149  31.606  11.071  1.00 42.64  ? 610 ARG A CG    1 
ATOM   4786 C  CD    . ARG A 1 610 ? 23.267  32.406  10.132  1.00 47.63  ? 610 ARG A CD    1 
ATOM   4787 N  NE    . ARG A 1 610 ? 22.276  31.544  9.495   1.00 46.11  ? 610 ARG A NE    1 
ATOM   4788 C  CZ    . ARG A 1 610 ? 21.452  31.946  8.538   1.00 49.79  ? 610 ARG A CZ    1 
ATOM   4789 N  NH1   . ARG A 1 610 ? 21.474  33.190  8.088   1.00 54.90  ? 610 ARG A NH1   1 
ATOM   4790 N  NH2   . ARG A 1 610 ? 20.588  31.080  8.019   1.00 53.42  ? 610 ARG A NH2   1 
ATOM   4791 N  N     . GLU A 1 611 ? 24.636  27.908  12.238  1.00 36.68  ? 611 GLU A N     1 
ATOM   4792 C  CA    . GLU A 1 611 ? 23.997  27.241  13.373  1.00 36.72  ? 611 GLU A CA    1 
ATOM   4793 C  C     . GLU A 1 611 ? 25.030  26.810  14.406  1.00 40.28  ? 611 GLU A C     1 
ATOM   4794 O  O     . GLU A 1 611 ? 24.776  26.871  15.618  1.00 39.76  ? 611 GLU A O     1 
ATOM   4795 C  CB    . GLU A 1 611 ? 23.174  26.037  12.896  1.00 36.12  ? 611 GLU A CB    1 
ATOM   4796 C  CG    . GLU A 1 611 ? 21.913  26.413  12.093  1.00 37.30  ? 611 GLU A CG    1 
ATOM   4797 C  CD    . GLU A 1 611 ? 21.008  27.363  12.855  1.00 36.77  ? 611 GLU A CD    1 
ATOM   4798 O  OE1   . GLU A 1 611 ? 20.784  27.127  14.060  1.00 35.97  ? 611 GLU A OE1   1 
ATOM   4799 O  OE2   . GLU A 1 611 ? 20.542  28.357  12.265  1.00 42.23  ? 611 GLU A OE2   1 
ATOM   4800 N  N     . LEU A 1 612 ? 26.199  26.362  13.950  1.00 40.04  ? 612 LEU A N     1 
ATOM   4801 C  CA    . LEU A 1 612 ? 27.287  26.070  14.877  1.00 39.07  ? 612 LEU A CA    1 
ATOM   4802 C  C     . LEU A 1 612 ? 27.690  27.317  15.660  1.00 41.86  ? 612 LEU A C     1 
ATOM   4803 O  O     . LEU A 1 612 ? 27.855  27.270  16.888  1.00 41.74  ? 612 LEU A O     1 
ATOM   4804 C  CB    . LEU A 1 612 ? 28.474  25.492  14.110  1.00 40.08  ? 612 LEU A CB    1 
ATOM   4805 C  CG    . LEU A 1 612 ? 29.753  25.286  14.919  1.00 46.85  ? 612 LEU A CG    1 
ATOM   4806 C  CD1   . LEU A 1 612 ? 29.582  24.150  15.912  1.00 38.16  ? 612 LEU A CD1   1 
ATOM   4807 C  CD2   . LEU A 1 612 ? 30.947  25.047  13.998  1.00 50.47  ? 612 LEU A CD2   1 
ATOM   4808 N  N     . ARG A 1 613 ? 27.847  28.454  14.966  1.00 40.39  ? 613 ARG A N     1 
ATOM   4809 C  CA    . ARG A 1 613 ? 28.209  29.687  15.656  1.00 38.32  ? 613 ARG A CA    1 
ATOM   4810 C  C     . ARG A 1 613 ? 27.138  30.094  16.654  1.00 38.04  ? 613 ARG A C     1 
ATOM   4811 O  O     . ARG A 1 613 ? 27.451  30.591  17.743  1.00 40.03  ? 613 ARG A O     1 
ATOM   4812 C  CB    . ARG A 1 613 ? 28.430  30.825  14.653  1.00 40.93  ? 613 ARG A CB    1 
ATOM   4813 C  CG    . ARG A 1 613 ? 29.649  30.665  13.785  1.00 41.08  ? 613 ARG A CG    1 
ATOM   4814 C  CD    . ARG A 1 613 ? 29.698  31.732  12.714  1.00 51.58  ? 613 ARG A CD    1 
ATOM   4815 N  NE    . ARG A 1 613 ? 30.977  31.674  12.026  1.00 58.05  ? 613 ARG A NE    1 
ATOM   4816 C  CZ    . ARG A 1 613 ? 31.892  32.631  12.049  1.00 57.95  ? 613 ARG A CZ    1 
ATOM   4817 N  NH1   . ARG A 1 613 ? 31.662  33.800  12.632  1.00 60.88  ? 613 ARG A NH1   1 
ATOM   4818 N  NH2   . ARG A 1 613 ? 33.064  32.415  11.458  1.00 65.34  ? 613 ARG A NH2   1 
ATOM   4819 N  N     . ALA A 1 614 ? 25.869  29.950  16.275  1.00 36.20  ? 614 ALA A N     1 
ATOM   4820 C  CA    . ALA A 1 614 ? 24.788  30.375  17.158  1.00 37.65  ? 614 ALA A CA    1 
ATOM   4821 C  C     . ALA A 1 614 ? 24.720  29.484  18.397  1.00 39.78  ? 614 ALA A C     1 
ATOM   4822 O  O     . ALA A 1 614 ? 24.581  29.984  19.517  1.00 38.56  ? 614 ALA A O     1 
ATOM   4823 C  CB    . ALA A 1 614 ? 23.456  30.362  16.402  1.00 36.91  ? 614 ALA A CB    1 
ATOM   4824 N  N     . LEU A 1 615 ? 24.857  28.165  18.219  1.00 36.31  ? 615 LEU A N     1 
ATOM   4825 C  CA    . LEU A 1 615 ? 24.885  27.273  19.375  1.00 37.17  ? 615 LEU A CA    1 
ATOM   4826 C  C     . LEU A 1 615 ? 26.022  27.641  20.317  1.00 35.71  ? 615 LEU A C     1 
ATOM   4827 O  O     . LEU A 1 615 ? 25.817  27.790  21.523  1.00 38.59  ? 615 LEU A O     1 
ATOM   4828 C  CB    . LEU A 1 615 ? 25.014  25.815  18.926  1.00 39.45  ? 615 LEU A CB    1 
ATOM   4829 C  CG    . LEU A 1 615 ? 25.048  24.819  20.094  1.00 38.17  ? 615 LEU A CG    1 
ATOM   4830 C  CD1   . LEU A 1 615 ? 23.820  25.009  20.962  1.00 40.14  ? 615 LEU A CD1   1 
ATOM   4831 C  CD2   . LEU A 1 615 ? 25.146  23.363  19.619  1.00 37.20  ? 615 LEU A CD2   1 
ATOM   4832 N  N     . LYS A 1 616 ? 27.227  27.834  19.769  1.00 39.97  ? 616 LYS A N     1 
ATOM   4833 C  CA    . LYS A 1 616 ? 28.380  28.225  20.576  1.00 39.93  ? 616 LYS A CA    1 
ATOM   4834 C  C     . LYS A 1 616 ? 28.109  29.494  21.377  1.00 45.11  ? 616 LYS A C     1 
ATOM   4835 O  O     . LYS A 1 616 ? 28.536  29.614  22.533  1.00 45.47  ? 616 LYS A O     1 
ATOM   4836 C  CB    . LYS A 1 616 ? 29.593  28.414  19.665  1.00 44.44  ? 616 LYS A CB    1 
ATOM   4837 C  CG    . LYS A 1 616 ? 30.897  28.698  20.386  1.00 50.26  ? 616 LYS A CG    1 
ATOM   4838 C  CD    . LYS A 1 616 ? 32.068  28.078  19.619  1.00 59.44  ? 616 LYS A CD    1 
ATOM   4839 C  CE    . LYS A 1 616 ? 33.279  27.844  20.522  1.00 65.99  ? 616 LYS A CE    1 
ATOM   4840 N  NZ    . LYS A 1 616 ? 34.027  26.594  20.146  1.00 64.14  ? 616 LYS A NZ    1 
ATOM   4841 N  N     . GLN A 1 617 ? 27.409  30.461  20.775  1.00 42.99  ? 617 GLN A N     1 
ATOM   4842 C  CA    . GLN A 1 617 ? 27.125  31.707  21.480  1.00 43.38  ? 617 GLN A CA    1 
ATOM   4843 C  C     . GLN A 1 617 ? 26.113  31.493  22.600  1.00 43.23  ? 617 GLN A C     1 
ATOM   4844 O  O     . GLN A 1 617 ? 26.293  32.008  23.706  1.00 45.95  ? 617 GLN A O     1 
ATOM   4845 C  CB    . GLN A 1 617 ? 26.631  32.770  20.493  1.00 41.50  ? 617 GLN A CB    1 
ATOM   4846 C  CG    . GLN A 1 617 ? 26.402  34.137  21.105  1.00 47.16  ? 617 GLN A CG    1 
ATOM   4847 C  CD    . GLN A 1 617 ? 27.692  34.818  21.542  1.00 49.62  ? 617 GLN A CD    1 
ATOM   4848 O  OE1   . GLN A 1 617 ? 28.787  34.390  21.182  1.00 57.41  ? 617 GLN A OE1   1 
ATOM   4849 N  NE2   . GLN A 1 617 ? 27.566  35.868  22.325  1.00 51.05  ? 617 GLN A NE2   1 
ATOM   4850 N  N     . ARG A 1 618 ? 25.046  30.741  22.332  1.00 40.61  ? 618 ARG A N     1 
ATOM   4851 C  CA    . ARG A 1 618 ? 24.034  30.485  23.356  1.00 45.11  ? 618 ARG A CA    1 
ATOM   4852 C  C     . ARG A 1 618 ? 24.622  29.733  24.546  1.00 46.04  ? 618 ARG A C     1 
ATOM   4853 O  O     . ARG A 1 618 ? 24.286  30.021  25.699  1.00 47.44  ? 618 ARG A O     1 
ATOM   4854 C  CB    . ARG A 1 618 ? 22.871  29.695  22.756  1.00 40.98  ? 618 ARG A CB    1 
ATOM   4855 C  CG    . ARG A 1 618 ? 22.060  30.480  21.746  1.00 41.47  ? 618 ARG A CG    1 
ATOM   4856 C  CD    . ARG A 1 618 ? 20.752  29.774  21.408  1.00 38.36  ? 618 ARG A CD    1 
ATOM   4857 N  NE    . ARG A 1 618 ? 20.961  28.409  20.950  1.00 38.23  ? 618 ARG A NE    1 
ATOM   4858 C  CZ    . ARG A 1 618 ? 21.105  28.068  19.676  1.00 42.31  ? 618 ARG A CZ    1 
ATOM   4859 N  NH1   . ARG A 1 618 ? 21.086  28.976  18.711  1.00 45.69  ? 618 ARG A NH1   1 
ATOM   4860 N  NH2   . ARG A 1 618 ? 21.280  26.789  19.361  1.00 38.28  ? 618 ARG A NH2   1 
ATOM   4861 N  N     . ILE A 1 619 ? 25.505  28.767  24.288  1.00 45.51  ? 619 ILE A N     1 
ATOM   4862 C  CA    . ILE A 1 619 ? 26.145  28.047  25.385  1.00 46.75  ? 619 ILE A CA    1 
ATOM   4863 C  C     . ILE A 1 619 ? 27.060  28.971  26.176  1.00 48.19  ? 619 ILE A C     1 
ATOM   4864 O  O     . ILE A 1 619 ? 27.076  28.938  27.413  1.00 48.94  ? 619 ILE A O     1 
ATOM   4865 C  CB    . ILE A 1 619 ? 26.901  26.821  24.850  1.00 47.27  ? 619 ILE A CB    1 
ATOM   4866 C  CG1   . ILE A 1 619 ? 25.893  25.804  24.320  1.00 44.28  ? 619 ILE A CG1   1 
ATOM   4867 C  CG2   . ILE A 1 619 ? 27.790  26.217  25.952  1.00 51.05  ? 619 ILE A CG2   1 
ATOM   4868 C  CD1   . ILE A 1 619 ? 26.513  24.688  23.554  1.00 51.50  ? 619 ILE A CD1   1 
ATOM   4869 N  N     . SER A 1 620 ? 27.824  29.820  25.480  1.00 49.31  ? 620 SER A N     1 
ATOM   4870 C  CA    . SER A 1 620 ? 28.723  30.757  26.147  1.00 50.35  ? 620 SER A CA    1 
ATOM   4871 C  C     . SER A 1 620 ? 27.986  31.740  27.050  1.00 50.19  ? 620 SER A C     1 
ATOM   4872 O  O     . SER A 1 620 ? 28.588  32.289  27.985  1.00 51.71  ? 620 SER A O     1 
ATOM   4873 C  CB    . SER A 1 620 ? 29.530  31.538  25.108  1.00 52.69  ? 620 SER A CB    1 
ATOM   4874 O  OG    . SER A 1 620 ? 28.792  32.666  24.662  1.00 54.27  ? 620 SER A OG    1 
ATOM   4875 N  N     . GLN A 1 621 ? 26.705  31.982  26.800  1.00 49.44  ? 621 GLN A N     1 
ATOM   4876 C  CA    . GLN A 1 621 ? 25.939  32.904  27.630  1.00 53.97  ? 621 GLN A CA    1 
ATOM   4877 C  C     . GLN A 1 621 ? 25.315  32.229  28.846  1.00 56.20  ? 621 GLN A C     1 
ATOM   4878 O  O     . GLN A 1 621 ? 24.701  32.917  29.669  1.00 54.60  ? 621 GLN A O     1 
ATOM   4879 C  CB    . GLN A 1 621 ? 24.855  33.586  26.786  1.00 53.93  ? 621 GLN A CB    1 
ATOM   4880 C  CG    . GLN A 1 621 ? 25.420  34.587  25.761  1.00 53.95  ? 621 GLN A CG    1 
ATOM   4881 C  CD    . GLN A 1 621 ? 26.233  35.694  26.397  1.00 59.21  ? 621 GLN A CD    1 
ATOM   4882 O  OE1   . GLN A 1 621 ? 25.776  36.373  27.321  1.00 64.02  ? 621 GLN A OE1   1 
ATOM   4883 N  NE2   . GLN A 1 621 ? 27.455  35.892  25.899  1.00 62.50  ? 621 GLN A NE2   1 
ATOM   4884 N  N     . MET A 1 622 ? 25.471  30.912  28.986  1.00 53.20  ? 622 MET A N     1 
ATOM   4885 C  CA    . MET A 1 622 ? 24.985  30.180  30.159  1.00 54.49  ? 622 MET A CA    1 
ATOM   4886 C  C     . MET A 1 622 ? 25.735  30.555  31.415  1.00 58.22  ? 622 MET A C     1 
ATOM   4887 O  O     . MET A 1 622 ? 26.926  30.864  31.360  1.00 59.42  ? 622 MET A O     1 
ATOM   4888 C  CB    . MET A 1 622 ? 25.115  28.669  29.955  1.00 55.23  ? 622 MET A CB    1 
ATOM   4889 C  CG    . MET A 1 622 ? 24.251  28.096  28.870  1.00 51.42  ? 622 MET A CG    1 
ATOM   4890 S  SD    . MET A 1 622 ? 24.401  26.294  28.845  1.00 54.20  ? 622 MET A SD    1 
ATOM   4891 C  CE    . MET A 1 622 ? 23.715  25.882  30.457  1.00 49.33  ? 622 MET A CE    1 
ATOM   4892 O  OXT   . MET A 1 622 ? 25.166  30.527  32.505  1.00 66.03  ? 622 MET A OXT   1 
HETATM 4893 MN MN    . MN  B 2 .   ? 16.629  -2.605  12.449  1.00 36.34  ? 701 MN  A MN    1 
HETATM 4894 MN MN    . MN  C 2 .   ? 20.095  -0.251  9.351   1.00 28.91  ? 702 MN  A MN    1 
HETATM 4895 MN MN    . MN  D 2 .   ? 18.563  28.364  2.799   1.00 88.21  ? 703 MN  A MN    1 
HETATM 4896 C  C1    . OXL E 3 .   ? 21.397  -2.777  9.207   1.00 34.42  ? 704 OXL A C1    1 
HETATM 4897 C  C2    . OXL E 3 .   ? 22.483  -1.791  9.678   1.00 37.61  ? 704 OXL A C2    1 
HETATM 4898 O  O1    . OXL E 3 .   ? 20.239  -2.401  9.082   1.00 28.13  ? 704 OXL A O1    1 
HETATM 4899 O  O2    . OXL E 3 .   ? 22.041  -0.558  9.879   1.00 29.05  ? 704 OXL A O2    1 
HETATM 4900 O  O3    . OXL E 3 .   ? 21.839  -3.990  8.932   1.00 33.65  ? 704 OXL A O3    1 
HETATM 4901 O  O4    . OXL E 3 .   ? 23.634  -2.169  9.843   1.00 36.92  ? 704 OXL A O4    1 
HETATM 4902 P  PG    . GTP F 4 .   ? 19.761  -1.702  12.470  1.00 37.98  ? 705 GTP A PG    1 
HETATM 4903 O  O1G   . GTP F 4 .   ? 18.782  -2.758  12.032  1.00 36.15  ? 705 GTP A O1G   1 
HETATM 4904 O  O2G   . GTP F 4 .   ? 21.134  -2.322  12.507  1.00 30.98  ? 705 GTP A O2G   1 
HETATM 4905 O  O3G   . GTP F 4 .   ? 19.655  -0.499  11.531  1.00 30.06  ? 705 GTP A O3G   1 
HETATM 4906 O  O3B   . GTP F 4 .   ? 19.548  -1.280  14.018  1.00 35.89  ? 705 GTP A O3B   1 
HETATM 4907 P  PB    . GTP F 4 .   ? 18.217  -0.766  14.752  1.00 38.14  ? 705 GTP A PB    1 
HETATM 4908 O  O1B   . GTP F 4 .   ? 16.886  -1.180  14.193  1.00 34.04  ? 705 GTP A O1B   1 
HETATM 4909 O  O2B   . GTP F 4 .   ? 18.221  0.774   14.840  1.00 34.64  ? 705 GTP A O2B   1 
HETATM 4910 O  O3A   . GTP F 4 .   ? 18.453  -1.343  16.219  1.00 34.48  ? 705 GTP A O3A   1 
HETATM 4911 P  PA    . GTP F 4 .   ? 17.329  -2.207  17.025  1.00 38.40  ? 705 GTP A PA    1 
HETATM 4912 O  O1A   . GTP F 4 .   ? 17.432  -3.591  16.427  1.00 37.52  ? 705 GTP A O1A   1 
HETATM 4913 O  O2A   . GTP F 4 .   ? 15.920  -1.675  17.039  1.00 38.09  ? 705 GTP A O2A   1 
HETATM 4914 O  "O5'" . GTP F 4 .   ? 18.013  -2.204  18.481  1.00 34.26  ? 705 GTP A "O5'" 1 
HETATM 4915 C  "C5'" . GTP F 4 .   ? 19.383  -2.501  18.643  1.00 33.71  ? 705 GTP A "C5'" 1 
HETATM 4916 C  "C4'" . GTP F 4 .   ? 19.561  -2.932  20.101  1.00 37.53  ? 705 GTP A "C4'" 1 
HETATM 4917 O  "O4'" . GTP F 4 .   ? 19.242  -1.841  20.961  1.00 43.44  ? 705 GTP A "O4'" 1 
HETATM 4918 C  "C3'" . GTP F 4 .   ? 18.598  -4.056  20.444  1.00 44.32  ? 705 GTP A "C3'" 1 
HETATM 4919 O  "O3'" . GTP F 4 .   ? 19.270  -5.130  21.066  1.00 43.82  ? 705 GTP A "O3'" 1 
HETATM 4920 C  "C2'" . GTP F 4 .   ? 17.620  -3.440  21.430  1.00 46.69  ? 705 GTP A "C2'" 1 
HETATM 4921 O  "O2'" . GTP F 4 .   ? 17.275  -4.388  22.421  1.00 49.08  ? 705 GTP A "O2'" 1 
HETATM 4922 C  "C1'" . GTP F 4 .   ? 18.329  -2.198  21.977  1.00 44.34  ? 705 GTP A "C1'" 1 
HETATM 4923 N  N9    . GTP F 4 .   ? 17.313  -1.148  22.262  1.00 42.82  ? 705 GTP A N9    1 
HETATM 4924 C  C8    . GTP F 4 .   ? 16.300  -0.794  21.404  1.00 41.32  ? 705 GTP A C8    1 
HETATM 4925 N  N7    . GTP F 4 .   ? 15.541  0.168   21.981  1.00 38.35  ? 705 GTP A N7    1 
HETATM 4926 C  C5    . GTP F 4 .   ? 16.048  0.431   23.210  1.00 40.49  ? 705 GTP A C5    1 
HETATM 4927 C  C6    . GTP F 4 .   ? 15.642  1.317   24.205  1.00 41.39  ? 705 GTP A C6    1 
HETATM 4928 O  O6    . GTP F 4 .   ? 14.653  2.035   24.041  1.00 40.18  ? 705 GTP A O6    1 
HETATM 4929 N  N1    . GTP F 4 .   ? 16.352  1.390   25.381  1.00 41.05  ? 705 GTP A N1    1 
HETATM 4930 C  C2    . GTP F 4 .   ? 17.450  0.573   25.562  1.00 40.75  ? 705 GTP A C2    1 
HETATM 4931 N  N2    . GTP F 4 .   ? 18.136  0.647   26.700  1.00 47.47  ? 705 GTP A N2    1 
HETATM 4932 N  N3    . GTP F 4 .   ? 17.851  -0.302  24.573  1.00 40.47  ? 705 GTP A N3    1 
HETATM 4933 C  C4    . GTP F 4 .   ? 17.163  -0.386  23.403  1.00 40.25  ? 705 GTP A C4    1 
HETATM 4934 C  C1    . PGE G 5 .   ? 5.310   10.621  -3.383  1.00 55.81  ? 706 PGE A C1    1 
HETATM 4935 O  O1    . PGE G 5 .   ? 4.073   10.802  -4.049  1.00 63.28  ? 706 PGE A O1    1 
HETATM 4936 C  C2    . PGE G 5 .   ? 5.310   9.350   -2.596  1.00 57.64  ? 706 PGE A C2    1 
HETATM 4937 O  O2    . PGE G 5 .   ? 6.614   9.067   -2.098  1.00 58.04  ? 706 PGE A O2    1 
HETATM 4938 C  C3    . PGE G 5 .   ? 7.662   9.544   -2.929  1.00 57.66  ? 706 PGE A C3    1 
HETATM 4939 C  C4    . PGE G 5 .   ? 8.943   8.868   -2.581  1.00 51.81  ? 706 PGE A C4    1 
HETATM 4940 O  O4    . PGE G 5 .   ? 10.021  9.311   -6.387  1.00 65.82  ? 706 PGE A O4    1 
HETATM 4941 C  C6    . PGE G 5 .   ? 10.757  8.343   -5.655  1.00 57.99  ? 706 PGE A C6    1 
HETATM 4942 C  C5    . PGE G 5 .   ? 10.653  8.621   -4.191  1.00 48.84  ? 706 PGE A C5    1 
HETATM 4943 O  O3    . PGE G 5 .   ? 9.400   8.163   -3.717  1.00 57.99  ? 706 PGE A O3    1 
HETATM 4944 O  O     . HOH H 6 .   ? 39.014  14.783  11.299  1.00 49.00  ? 801 HOH A O     1 
HETATM 4945 O  O     . HOH H 6 .   ? 29.510  -19.904 13.293  1.00 53.55  ? 802 HOH A O     1 
HETATM 4946 O  O     . HOH H 6 .   ? 17.495  -3.670  13.799  1.00 34.18  ? 803 HOH A O     1 
HETATM 4947 O  O     . HOH H 6 .   ? 35.605  19.256  -1.292  1.00 49.96  ? 804 HOH A O     1 
HETATM 4948 O  O     . HOH H 6 .   ? 33.320  12.302  -10.963 1.00 55.74  ? 805 HOH A O     1 
HETATM 4949 O  O     . HOH H 6 .   ? 24.948  -4.655  9.761   1.00 42.15  ? 806 HOH A O     1 
HETATM 4950 O  O     . HOH H 6 .   ? 38.743  -3.583  8.098   1.00 60.90  ? 807 HOH A O     1 
HETATM 4951 O  O     . HOH H 6 .   ? 29.726  6.848   3.751   1.00 40.40  ? 808 HOH A O     1 
HETATM 4952 O  O     . HOH H 6 .   ? 24.058  -11.722 -24.712 1.00 53.81  ? 809 HOH A O     1 
HETATM 4953 O  O     . HOH H 6 .   ? 10.542  23.732  16.489  1.00 40.68  ? 810 HOH A O     1 
HETATM 4954 O  O     . HOH H 6 .   ? 16.375  -0.870  11.173  1.00 35.78  ? 811 HOH A O     1 
HETATM 4955 O  O     . HOH H 6 .   ? 15.856  -3.932  10.700  1.00 36.57  ? 812 HOH A O     1 
HETATM 4956 O  O     . HOH H 6 .   ? 4.733   -7.184  -0.440  1.00 46.02  ? 813 HOH A O     1 
HETATM 4957 O  O     . HOH H 6 .   ? 21.422  -32.052 -3.184  1.00 51.49  ? 814 HOH A O     1 
HETATM 4958 O  O     . HOH H 6 .   ? 11.458  -15.413 -13.524 1.00 41.30  ? 815 HOH A O     1 
HETATM 4959 O  O     . HOH H 6 .   ? 24.491  2.072   24.759  1.00 54.68  ? 816 HOH A O     1 
HETATM 4960 O  O     . HOH H 6 .   ? 35.594  14.095  3.816   1.00 39.03  ? 817 HOH A O     1 
HETATM 4961 O  O     . HOH H 6 .   ? -2.287  -2.152  11.906  1.00 49.53  ? 818 HOH A O     1 
HETATM 4962 O  O     . HOH H 6 .   ? -2.409  10.009  27.215  1.00 54.53  ? 819 HOH A O     1 
HETATM 4963 O  O     . HOH H 6 .   ? 31.005  16.562  24.952  1.00 44.07  ? 820 HOH A O     1 
HETATM 4964 O  O     . HOH H 6 .   ? 24.438  -23.061 -24.927 1.00 48.78  ? 821 HOH A O     1 
HETATM 4965 O  O     . HOH H 6 .   ? 18.157  8.717   28.366  1.00 42.24  ? 822 HOH A O     1 
HETATM 4966 O  O     . HOH H 6 .   ? 23.866  -4.939  7.664   1.00 44.87  ? 823 HOH A O     1 
HETATM 4967 O  O     . HOH H 6 .   ? 22.456  16.354  20.812  1.00 34.47  ? 824 HOH A O     1 
HETATM 4968 O  O     . HOH H 6 .   ? 30.109  1.838   4.725   1.00 37.82  ? 825 HOH A O     1 
HETATM 4969 O  O     . HOH H 6 .   ? 24.336  4.440   10.892  1.00 34.81  ? 826 HOH A O     1 
HETATM 4970 O  O     . HOH H 6 .   ? 10.015  -29.217 19.591  1.00 58.50  ? 827 HOH A O     1 
HETATM 4971 O  O     . HOH H 6 .   ? 21.956  26.827  16.360  1.00 38.63  ? 828 HOH A O     1 
HETATM 4972 O  O     . HOH H 6 .   ? 6.535   -4.643  20.155  1.00 39.99  ? 829 HOH A O     1 
HETATM 4973 O  O     . HOH H 6 .   ? 5.686   25.956  24.670  1.00 46.43  ? 830 HOH A O     1 
HETATM 4974 O  O     . HOH H 6 .   ? 30.571  5.675   -10.960 1.00 49.07  ? 831 HOH A O     1 
HETATM 4975 O  O     . HOH H 6 .   ? 21.098  10.552  21.482  1.00 35.48  ? 832 HOH A O     1 
HETATM 4976 O  O     . HOH H 6 .   ? 0.933   12.273  9.366   1.00 37.72  ? 833 HOH A O     1 
HETATM 4977 O  O     . HOH H 6 .   ? 22.889  15.923  17.256  1.00 32.99  ? 834 HOH A O     1 
HETATM 4978 O  O     . HOH H 6 .   ? 26.470  15.869  19.289  1.00 34.93  ? 835 HOH A O     1 
HETATM 4979 O  O     . HOH H 6 .   ? 34.477  -20.339 5.524   1.00 49.42  ? 836 HOH A O     1 
HETATM 4980 O  O     . HOH H 6 .   ? 21.285  -29.189 7.009   1.00 49.30  ? 837 HOH A O     1 
HETATM 4981 O  O     . HOH H 6 .   ? 3.329   14.957  26.889  1.00 49.30  ? 838 HOH A O     1 
HETATM 4982 O  O     . HOH H 6 .   ? 32.093  -18.669 -5.662  1.00 40.34  ? 839 HOH A O     1 
HETATM 4983 O  O     . HOH H 6 .   ? 12.578  -0.549  5.845   1.00 26.93  ? 840 HOH A O     1 
HETATM 4984 O  O     . HOH H 6 .   ? 1.771   18.672  10.820  1.00 42.86  ? 841 HOH A O     1 
HETATM 4985 O  O     . HOH H 6 .   ? 18.128  14.398  22.800  1.00 32.19  ? 842 HOH A O     1 
HETATM 4986 O  O     . HOH H 6 .   ? -1.854  11.050  9.298   1.00 45.51  ? 843 HOH A O     1 
HETATM 4987 O  O     . HOH H 6 .   ? 23.149  -4.108  1.049   1.00 33.71  ? 844 HOH A O     1 
HETATM 4988 O  O     . HOH H 6 .   ? 18.688  5.991   29.631  1.00 49.11  ? 845 HOH A O     1 
HETATM 4989 O  O     . HOH H 6 .   ? 25.661  -21.842 -6.263  1.00 43.43  ? 846 HOH A O     1 
HETATM 4990 O  O     . HOH H 6 .   ? 41.819  5.194   -5.790  1.00 53.17  ? 847 HOH A O     1 
HETATM 4991 O  O     . HOH H 6 .   ? 3.977   12.241  27.822  1.00 45.98  ? 848 HOH A O     1 
HETATM 4992 O  O     . HOH H 6 .   ? 28.901  9.587   -5.812  1.00 45.27  ? 849 HOH A O     1 
HETATM 4993 O  O     . HOH H 6 .   ? -1.372  4.093   14.836  1.00 40.21  ? 850 HOH A O     1 
HETATM 4994 O  O     . HOH H 6 .   ? 18.772  -14.072 8.774   1.00 33.70  ? 851 HOH A O     1 
HETATM 4995 O  O     . HOH H 6 .   ? 10.848  -13.412 25.130  1.00 49.16  ? 852 HOH A O     1 
HETATM 4996 O  O     . HOH H 6 .   ? 4.704   18.960  11.454  1.00 43.88  ? 853 HOH A O     1 
HETATM 4997 O  O     . HOH H 6 .   ? 10.775  -4.409  -2.014  1.00 35.91  ? 854 HOH A O     1 
HETATM 4998 O  O     . HOH H 6 .   ? 20.223  12.549  -1.106  1.00 33.59  ? 855 HOH A O     1 
HETATM 4999 O  O     . HOH H 6 .   ? 24.776  13.766  20.350  1.00 35.58  ? 856 HOH A O     1 
HETATM 5000 O  O     . HOH H 6 .   ? 23.578  -12.277 6.943   1.00 35.85  ? 857 HOH A O     1 
HETATM 5001 O  O     . HOH H 6 .   ? 6.469   -1.395  0.933   1.00 44.42  ? 858 HOH A O     1 
HETATM 5002 O  O     . HOH H 6 .   ? 25.988  4.108   16.894  1.00 46.55  ? 859 HOH A O     1 
HETATM 5003 O  O     . HOH H 6 .   ? 3.103   18.369  23.755  1.00 37.71  ? 860 HOH A O     1 
HETATM 5004 O  O     . HOH H 6 .   ? 24.557  18.064  29.901  1.00 49.93  ? 861 HOH A O     1 
HETATM 5005 O  O     . HOH H 6 .   ? 14.752  -4.114  7.630   1.00 30.31  ? 862 HOH A O     1 
HETATM 5006 O  O     . HOH H 6 .   ? 9.245   -22.940 -10.488 1.00 50.86  ? 863 HOH A O     1 
HETATM 5007 O  O     . HOH H 6 .   ? 11.383  2.544   6.881   1.00 32.18  ? 864 HOH A O     1 
HETATM 5008 O  O     . HOH H 6 .   ? 12.376  -18.419 -14.502 1.00 41.27  ? 865 HOH A O     1 
HETATM 5009 O  O     . HOH H 6 .   ? 21.278  28.946  9.710   1.00 41.19  ? 866 HOH A O     1 
HETATM 5010 O  O     . HOH H 6 .   ? 5.073   16.933  5.616   1.00 43.15  ? 867 HOH A O     1 
HETATM 5011 O  O     . HOH H 6 .   ? 18.989  9.110   7.478   1.00 26.80  ? 868 HOH A O     1 
HETATM 5012 O  O     . HOH H 6 .   ? 28.464  14.366  13.764  1.00 32.34  ? 869 HOH A O     1 
HETATM 5013 O  O     . HOH H 6 .   ? 11.251  2.037   21.652  1.00 41.08  ? 870 HOH A O     1 
HETATM 5014 O  O     . HOH H 6 .   ? 18.859  -13.637 5.911   1.00 37.32  ? 871 HOH A O     1 
HETATM 5015 O  O     . HOH H 6 .   ? 16.148  -4.487  -22.194 1.00 58.60  ? 872 HOH A O     1 
HETATM 5016 O  O     . HOH H 6 .   ? 27.826  5.268   14.690  1.00 44.27  ? 873 HOH A O     1 
HETATM 5017 O  O     . HOH H 6 .   ? 10.478  -24.988 10.773  1.00 44.12  ? 874 HOH A O     1 
HETATM 5018 O  O     . HOH H 6 .   ? 7.393   -2.305  22.942  1.00 40.00  ? 875 HOH A O     1 
HETATM 5019 O  O     . HOH H 6 .   ? 11.133  -18.137 -4.826  1.00 35.71  ? 876 HOH A O     1 
HETATM 5020 O  O     . HOH H 6 .   ? 16.508  2.956   27.637  1.00 44.57  ? 877 HOH A O     1 
HETATM 5021 O  O     . HOH H 6 .   ? 5.576   2.319   2.338   1.00 39.62  ? 878 HOH A O     1 
HETATM 5022 O  O     . HOH H 6 .   ? 21.309  22.402  19.624  1.00 36.06  ? 879 HOH A O     1 
HETATM 5023 O  O     . HOH H 6 .   ? 29.331  -3.008  3.674   1.00 39.89  ? 880 HOH A O     1 
HETATM 5024 O  O     . HOH H 6 .   ? 17.843  -4.001  8.789   1.00 29.98  ? 881 HOH A O     1 
HETATM 5025 O  O     . HOH H 6 .   ? 24.127  -12.019 21.953  1.00 45.31  ? 882 HOH A O     1 
HETATM 5026 O  O     . HOH H 6 .   ? 27.950  -17.985 2.066   1.00 43.52  ? 883 HOH A O     1 
HETATM 5027 O  O     . HOH H 6 .   ? 19.187  11.097  0.982   1.00 33.86  ? 884 HOH A O     1 
HETATM 5028 O  O     . HOH H 6 .   ? 3.288   3.769   1.684   1.00 48.41  ? 885 HOH A O     1 
HETATM 5029 O  O     . HOH H 6 .   ? 27.760  11.053  25.846  1.00 40.54  ? 886 HOH A O     1 
HETATM 5030 O  O     . HOH H 6 .   ? 32.206  4.916   7.865   1.00 50.12  ? 887 HOH A O     1 
HETATM 5031 O  O     . HOH H 6 .   ? 29.804  3.665   14.137  1.00 51.70  ? 888 HOH A O     1 
HETATM 5032 O  O     . HOH H 6 .   ? 28.102  22.332  -0.236  1.00 51.15  ? 889 HOH A O     1 
HETATM 5033 O  O     . HOH H 6 .   ? 17.395  26.315  4.340   1.00 49.74  ? 890 HOH A O     1 
HETATM 5034 O  O     . HOH H 6 .   ? 12.578  26.919  9.862   1.00 43.86  ? 891 HOH A O     1 
HETATM 5035 O  O     . HOH H 6 .   ? 39.218  15.233  19.347  1.00 46.31  ? 892 HOH A O     1 
HETATM 5036 O  O     . HOH H 6 .   ? 23.632  -23.367 -5.366  1.00 44.50  ? 893 HOH A O     1 
HETATM 5037 O  O     . HOH H 6 .   ? 30.368  8.755   -0.013  1.00 48.49  ? 894 HOH A O     1 
HETATM 5038 O  O     . HOH H 6 .   ? 8.354   -12.860 0.818   1.00 41.93  ? 895 HOH A O     1 
HETATM 5039 O  O     . HOH H 6 .   ? 37.767  -15.858 -7.582  1.00 55.33  ? 896 HOH A O     1 
HETATM 5040 O  O     . HOH H 6 .   ? 23.353  12.231  18.600  1.00 34.75  ? 897 HOH A O     1 
HETATM 5041 O  O     . HOH H 6 .   ? 21.480  -24.912 -8.085  1.00 46.42  ? 898 HOH A O     1 
HETATM 5042 O  O     . HOH H 6 .   ? 26.050  2.180   14.856  1.00 39.24  ? 899 HOH A O     1 
HETATM 5043 O  O     . HOH H 6 .   ? 29.032  5.051   1.800   1.00 36.25  ? 900 HOH A O     1 
HETATM 5044 O  O     . HOH H 6 .   ? 30.783  -9.347  -0.431  1.00 42.35  ? 901 HOH A O     1 
HETATM 5045 O  O     . HOH H 6 .   ? 30.786  -24.506 -1.301  1.00 54.10  ? 902 HOH A O     1 
HETATM 5046 O  O     . HOH H 6 .   ? 18.491  7.462   21.691  1.00 34.16  ? 903 HOH A O     1 
HETATM 5047 O  O     . HOH H 6 .   ? 4.092   -19.441 -5.441  1.00 56.30  ? 904 HOH A O     1 
HETATM 5048 O  O     . HOH H 6 .   ? 39.470  11.935  11.684  1.00 45.48  ? 905 HOH A O     1 
HETATM 5049 O  O     . HOH H 6 .   ? 8.417   -10.782 2.577   1.00 34.80  ? 906 HOH A O     1 
HETATM 5050 O  O     . HOH H 6 .   ? 23.602  -7.195  20.477  1.00 42.76  ? 907 HOH A O     1 
HETATM 5051 O  O     . HOH H 6 .   ? 13.883  -6.410  18.188  1.00 36.67  ? 908 HOH A O     1 
HETATM 5052 O  O     . HOH H 6 .   ? 32.394  -4.486  15.897  1.00 65.15  ? 909 HOH A O     1 
HETATM 5053 O  O     . HOH H 6 .   ? 8.383   -13.949 -4.375  1.00 40.54  ? 910 HOH A O     1 
HETATM 5054 O  O     . HOH H 6 .   ? 15.597  -5.917  16.321  1.00 40.78  ? 911 HOH A O     1 
HETATM 5055 O  O     . HOH H 6 .   ? 19.776  19.682  -4.288  1.00 46.77  ? 912 HOH A O     1 
HETATM 5056 O  O     . HOH H 6 .   ? 15.365  -4.065  -19.579 1.00 52.89  ? 913 HOH A O     1 
HETATM 5057 O  O     . HOH H 6 .   ? 26.052  -11.888 12.409  1.00 45.02  ? 914 HOH A O     1 
HETATM 5058 O  O     . HOH H 6 .   ? 14.113  0.818   -12.328 1.00 48.26  ? 915 HOH A O     1 
HETATM 5059 O  O     . HOH H 6 .   ? 6.081   -9.107  3.209   1.00 37.71  ? 916 HOH A O     1 
HETATM 5060 O  O     . HOH H 6 .   ? 18.078  5.992   19.303  1.00 37.78  ? 917 HOH A O     1 
HETATM 5061 O  O     . HOH H 6 .   ? 15.680  -5.045  1.264   1.00 29.92  ? 918 HOH A O     1 
HETATM 5062 O  O     . HOH H 6 .   ? 13.905  2.210   20.479  1.00 33.87  ? 919 HOH A O     1 
HETATM 5063 O  O     . HOH H 6 .   ? 29.064  -0.636  5.350   1.00 42.27  ? 920 HOH A O     1 
HETATM 5064 O  O     . HOH H 6 .   ? 31.721  -9.513  6.525   1.00 47.56  ? 921 HOH A O     1 
HETATM 5065 O  O     . HOH H 6 .   ? 26.916  -2.519  2.861   1.00 35.71  ? 922 HOH A O     1 
HETATM 5066 O  O     . HOH H 6 .   ? 12.112  -23.517 -16.668 1.00 53.23  ? 923 HOH A O     1 
HETATM 5067 O  O     . HOH H 6 .   ? 11.864  16.144  -1.780  1.00 53.04  ? 924 HOH A O     1 
HETATM 5068 O  O     . HOH H 6 .   ? 30.365  11.804  1.692   1.00 36.06  ? 925 HOH A O     1 
HETATM 5069 O  O     . HOH H 6 .   ? 30.117  -7.654  14.593  1.00 50.70  ? 926 HOH A O     1 
HETATM 5070 O  O     . HOH H 6 .   ? 25.604  -23.206 8.558   1.00 55.91  ? 927 HOH A O     1 
HETATM 5071 O  O     . HOH H 6 .   ? 34.024  9.373   14.335  1.00 43.12  ? 928 HOH A O     1 
HETATM 5072 O  O     . HOH H 6 .   ? 36.845  20.618  0.762   1.00 47.58  ? 929 HOH A O     1 
HETATM 5073 O  O     . HOH H 6 .   ? 10.925  -2.862  6.506   1.00 37.49  ? 930 HOH A O     1 
HETATM 5074 O  O     . HOH H 6 .   ? 21.105  31.948  18.959  1.00 42.84  ? 931 HOH A O     1 
HETATM 5075 O  O     . HOH H 6 .   ? 9.161   -11.736 -3.076  1.00 37.47  ? 932 HOH A O     1 
HETATM 5076 O  O     . HOH H 6 .   ? 11.466  21.694  14.244  1.00 37.63  ? 933 HOH A O     1 
HETATM 5077 O  O     . HOH H 6 .   ? -1.557  24.259  24.711  1.00 58.35  ? 934 HOH A O     1 
HETATM 5078 O  O     . HOH H 6 .   ? 32.495  3.113   3.541   1.00 44.90  ? 935 HOH A O     1 
HETATM 5079 O  O     . HOH H 6 .   ? 21.035  24.788  0.121   1.00 50.23  ? 936 HOH A O     1 
HETATM 5080 O  O     . HOH H 6 .   ? 32.301  -9.354  9.038   1.00 47.83  ? 937 HOH A O     1 
HETATM 5081 O  O     . HOH H 6 .   ? 32.743  -6.878  10.211  1.00 52.15  ? 938 HOH A O     1 
HETATM 5082 O  O     . HOH H 6 .   ? 26.409  6.109   -4.774  1.00 45.45  ? 939 HOH A O     1 
HETATM 5083 O  O     . HOH H 6 .   ? 38.267  15.660  -6.544  1.00 54.10  ? 940 HOH A O     1 
HETATM 5084 O  O     . HOH H 6 .   ? 22.501  20.070  19.156  1.00 36.68  ? 941 HOH A O     1 
HETATM 5085 O  O     . HOH H 6 .   ? 22.736  36.605  27.508  1.00 62.63  ? 942 HOH A O     1 
HETATM 5086 O  O     . HOH H 6 .   ? 17.831  -20.346 -22.526 1.00 52.24  ? 943 HOH A O     1 
HETATM 5087 O  O     . HOH H 6 .   ? 24.342  -11.760 10.978  1.00 48.61  ? 944 HOH A O     1 
HETATM 5088 O  O     . HOH H 6 .   ? 39.944  13.247  -7.956  1.00 58.61  ? 945 HOH A O     1 
HETATM 5089 O  O     . HOH H 6 .   ? -5.752  19.852  -5.003  1.00 69.13  ? 946 HOH A O     1 
HETATM 5090 O  O     . HOH H 6 .   ? 7.043   -23.008 -9.838  1.00 54.05  ? 947 HOH A O     1 
HETATM 5091 O  O     . HOH H 6 .   ? 31.829  4.294   1.269   1.00 43.79  ? 948 HOH A O     1 
HETATM 5092 O  O     . HOH H 6 .   ? 17.633  -6.337  -0.442  1.00 37.63  ? 949 HOH A O     1 
HETATM 5093 O  O     . HOH H 6 .   ? 39.358  -16.352 -5.125  1.00 61.52  ? 950 HOH A O     1 
HETATM 5094 O  O     . HOH H 6 .   ? 26.451  -23.129 -4.643  1.00 53.44  ? 951 HOH A O     1 
HETATM 5095 O  O     . HOH H 6 .   ? 24.335  -25.194 9.800   1.00 58.85  ? 952 HOH A O     1 
HETATM 5096 O  O     . HOH H 6 .   ? 24.164  17.540  19.092  1.00 39.05  ? 953 HOH A O     1 
HETATM 5097 O  O     . HOH H 6 .   ? 24.573  -9.881  22.509  1.00 50.11  ? 954 HOH A O     1 
HETATM 5098 O  O     . HOH H 6 .   ? -3.917  19.732  14.272  1.00 47.00  ? 955 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  ? 1.1393 0.7700 0.5168 -0.0373 0.1974  -0.1291 10  ASP A N   
56   C CA  . ASP A 10  ? 1.1319 0.7549 0.4963 -0.0358 0.1624  -0.1321 10  ASP A CA  
57   C C   . ASP A 10  ? 1.0101 0.6592 0.4395 -0.0234 0.1654  -0.1406 10  ASP A C   
58   O O   . ASP A 10  ? 0.9946 0.6396 0.4379 -0.0212 0.1827  -0.1565 10  ASP A O   
59   C CB  . ASP A 10  ? 1.1294 0.7205 0.4386 -0.0465 0.1493  -0.1425 10  ASP A CB  
60   C CG  . ASP A 10  ? 1.1146 0.6997 0.4097 -0.0477 0.1072  -0.1439 10  ASP A CG  
61   O OD1 . ASP A 10  ? 1.1334 0.7430 0.4734 -0.0390 0.0905  -0.1377 10  ASP A OD1 
62   O OD2 . ASP A 10  ? 1.2258 0.7874 0.4751 -0.0573 0.0889  -0.1498 10  ASP A OD2 
63   N N   . PHE A 11  ? 0.9442 0.6273 0.4283 -0.0149 0.1436  -0.1257 11  PHE A N   
64   C CA  . PHE A 11  ? 0.9100 0.6229 0.4638 -0.0034 0.1404  -0.1274 11  PHE A CA  
65   C C   . PHE A 11  ? 0.8679 0.5765 0.4241 -0.0051 0.1107  -0.1330 11  PHE A C   
66   O O   . PHE A 11  ? 0.7901 0.5222 0.4010 0.0028  0.1030  -0.1306 11  PHE A O   
67   C CB  . PHE A 11  ? 0.7984 0.5487 0.4078 0.0050  0.1357  -0.1096 11  PHE A CB  
68   C CG  . PHE A 11  ? 0.8083 0.5777 0.4542 0.0115  0.1673  -0.1095 11  PHE A CG  
69   C CD1 . PHE A 11  ? 0.8490 0.6085 0.4669 0.0050  0.1917  -0.1094 11  PHE A CD1 
70   C CD2 . PHE A 11  ? 0.8191 0.6157 0.5281 0.0236  0.1720  -0.1094 11  PHE A CD2 
71   C CE1 . PHE A 11  ? 0.8464 0.6283 0.5064 0.0105  0.2207  -0.1109 11  PHE A CE1 
72   C CE2 . PHE A 11  ? 0.7818 0.5995 0.5301 0.0306  0.1973  -0.1094 11  PHE A CE2 
73   C CZ  . PHE A 11  ? 0.7481 0.5610 0.4758 0.0240  0.2217  -0.1110 11  PHE A CZ  
74   N N   . SER A 12  ? 0.8865 0.5648 0.3837 -0.0162 0.0943  -0.1410 12  SER A N   
75   C CA  . SER A 12  ? 0.8974 0.5731 0.3980 -0.0202 0.0644  -0.1480 12  SER A CA  
76   C C   . SER A 12  ? 0.9099 0.5878 0.4476 -0.0163 0.0772  -0.1624 12  SER A C   
77   O O   . SER A 12  ? 0.8455 0.5405 0.4253 -0.0141 0.0597  -0.1613 12  SER A O   
78   C CB  . SER A 12  ? 0.9942 0.6329 0.4188 -0.0340 0.0475  -0.1574 12  SER A CB  
79   O OG  . SER A 12  ? 1.0697 0.7070 0.4663 -0.0364 0.0232  -0.1411 12  SER A OG  
80   N N   . ALA A 13  ? 0.8974 0.5554 0.4195 -0.0157 0.1091  -0.1765 13  ALA A N   
81   C CA  . ALA A 13  ? 0.8527 0.5058 0.4061 -0.0111 0.1221  -0.1904 13  ALA A CA  
82   C C   . ALA A 13  ? 0.8096 0.4962 0.4366 0.0028  0.1237  -0.1780 13  ALA A C   
83   O O   . ALA A 13  ? 0.8080 0.4908 0.4637 0.0062  0.1260  -0.1853 13  ALA A O   
84   C CB  . ALA A 13  ? 0.8993 0.5262 0.4284 -0.0103 0.1595  -0.2072 13  ALA A CB  
85   N N   . LYS A 14  ? 0.7494 0.4653 0.4040 0.0099  0.1225  -0.1595 14  LYS A N   
86   C CA  . LYS A 14  ? 0.7179 0.4634 0.4355 0.0221  0.1233  -0.1476 14  LYS A CA  
87   C C   . LYS A 14  ? 0.6655 0.4310 0.4077 0.0201  0.0944  -0.1359 14  LYS A C   
88   O O   . LYS A 14  ? 0.6109 0.3983 0.3988 0.0282  0.0939  -0.1253 14  LYS A O   
89   C CB  . LYS A 14  ? 0.6894 0.4566 0.4284 0.0307  0.1414  -0.1364 14  LYS A CB  
90   C CG  . LYS A 14  ? 0.8040 0.5615 0.5463 0.0373  0.1748  -0.1479 14  LYS A CG  
91   C CD  . LYS A 14  ? 0.8267 0.6136 0.6047 0.0458  0.1895  -0.1367 14  LYS A CD  
92   C CE  . LYS A 14  ? 0.8278 0.6231 0.6525 0.0605  0.2116  -0.1420 14  LYS A CE  
93   N NZ  . LYS A 14  ? 0.8408 0.6074 0.6422 0.0602  0.2384  -0.1623 14  LYS A NZ  
94   N N   . VAL A 15  ? 0.6811 0.4393 0.3954 0.0095  0.0704  -0.1380 15  VAL A N   
95   C CA  . VAL A 15  ? 0.6617 0.4419 0.4037 0.0081  0.0447  -0.1275 15  VAL A CA  
96   C C   . VAL A 15  ? 0.6510 0.4294 0.4199 0.0048  0.0373  -0.1361 15  VAL A C   
97   O O   . VAL A 15  ? 0.7153 0.4732 0.4609 -0.0047 0.0298  -0.1512 15  VAL A O   
98   C CB  . VAL A 15  ? 0.7173 0.4929 0.4239 0.0001  0.0201  -0.1248 15  VAL A CB  
99   C CG1 . VAL A 15  ? 0.6751 0.4740 0.4184 -0.0006 -0.0058 -0.1173 15  VAL A CG1 
100  C CG2 . VAL A 15  ? 0.7084 0.4838 0.3897 0.0028  0.0285  -0.1132 15  VAL A CG2 
101  N N   . ILE A 16  ? 0.5689 0.3665 0.3840 0.0109  0.0398  -0.1268 16  ILE A N   
102  C CA  . ILE A 16  ? 0.5897 0.3828 0.4302 0.0067  0.0369  -0.1336 16  ILE A CA  
103  C C   . ILE A 16  ? 0.6512 0.4629 0.5154 -0.0007 0.0145  -0.1306 16  ILE A C   
104  O O   . ILE A 16  ? 0.5875 0.3958 0.4731 -0.0074 0.0119  -0.1375 16  ILE A O   
105  C CB  . ILE A 16  ? 0.6015 0.3964 0.4733 0.0171  0.0555  -0.1263 16  ILE A CB  
106  C CG1 . ILE A 16  ? 0.5598 0.3825 0.4566 0.0247  0.0543  -0.1080 16  ILE A CG1 
107  C CG2 . ILE A 16  ? 0.6095 0.3856 0.4662 0.0251  0.0775  -0.1328 16  ILE A CG2 
108  C CD1 . ILE A 16  ? 0.5683 0.3934 0.4947 0.0332  0.0653  -0.0991 16  ILE A CD1 
109  N N   . GLN A 17  ? 0.6036 0.4338 0.4674 0.0003  -0.0002 -0.1210 17  GLN A N   
110  C CA  . GLN A 17  ? 0.6033 0.4505 0.4895 -0.0063 -0.0232 -0.1213 17  GLN A CA  
111  C C   . GLN A 17  ? 0.6103 0.4640 0.4754 -0.0047 -0.0411 -0.1143 17  GLN A C   
112  O O   . GLN A 17  ? 0.5617 0.4211 0.4202 0.0030  -0.0333 -0.1017 17  GLN A O   
113  C CB  . GLN A 17  ? 0.5493 0.4178 0.4824 -0.0039 -0.0187 -0.1123 17  GLN A CB  
114  C CG  . GLN A 17  ? 0.5752 0.4648 0.5369 -0.0093 -0.0399 -0.1130 17  GLN A CG  
115  C CD  . GLN A 17  ? 0.5949 0.5015 0.6011 -0.0104 -0.0319 -0.1085 17  GLN A CD  
116  O OE1 . GLN A 17  ? 0.6150 0.5127 0.6338 -0.0151 -0.0185 -0.1128 17  GLN A OE1 
117  N NE2 . GLN A 17  ? 0.5169 0.4446 0.5446 -0.0066 -0.0389 -0.1000 17  GLN A NE2 
118  N N   . GLY A 18  ? 0.6256 0.4772 0.4803 -0.0122 -0.0660 -0.1222 18  GLY A N   
119  C CA  . GLY A 18  ? 0.6204 0.4729 0.4510 -0.0103 -0.0870 -0.1147 18  GLY A CA  
120  C C   . GLY A 18  ? 0.7377 0.5598 0.5032 -0.0142 -0.0887 -0.1200 18  GLY A C   
121  O O   . GLY A 18  ? 0.7434 0.5444 0.4841 -0.0204 -0.0780 -0.1338 18  GLY A O   
122  N N   . SER A 19  ? 0.7649 0.5815 0.4997 -0.0110 -0.1008 -0.1088 19  SER A N   
123  C CA  . SER A 19  ? 0.8099 0.5943 0.4748 -0.0162 -0.1051 -0.1116 19  SER A CA  
124  C C   . SER A 19  ? 0.8575 0.6365 0.4978 -0.0098 -0.1001 -0.0939 19  SER A C   
125  O O   . SER A 19  ? 0.8667 0.6610 0.5299 -0.0040 -0.1179 -0.0812 19  SER A O   
126  C CB  . SER A 19  ? 0.8513 0.6276 0.4953 -0.0243 -0.1423 -0.1197 19  SER A CB  
127  O OG  . SER A 19  ? 0.9474 0.6887 0.5150 -0.0298 -0.1489 -0.1202 19  SER A OG  
128  N N   . LEU A 20  ? 0.8741 0.6312 0.4713 -0.0112 -0.0739 -0.0937 20  LEU A N   
129  C CA  . LEU A 20  ? 0.9183 0.6650 0.4851 -0.0084 -0.0681 -0.0780 20  LEU A CA  
130  C C   . LEU A 20  ? 0.9770 0.7019 0.4953 -0.0119 -0.1008 -0.0713 20  LEU A C   
131  O O   . LEU A 20  ? 0.9629 0.6855 0.4743 -0.0073 -0.1090 -0.0547 20  LEU A O   
132  C CB  . LEU A 20  ? 0.8858 0.6122 0.4151 -0.0115 -0.0322 -0.0819 20  LEU A CB  
133  C CG  . LEU A 20  ? 0.8571 0.6038 0.4319 -0.0056 0.0010  -0.0848 20  LEU A CG  
134  C CD1 . LEU A 20  ? 0.9147 0.6397 0.4510 -0.0094 0.0346  -0.0919 20  LEU A CD1 
135  C CD2 . LEU A 20  ? 0.8298 0.6055 0.4530 0.0024  0.0041  -0.0695 20  LEU A CD2 
136  N N   . ASP A 21  ? 1.0027 0.7106 0.4884 -0.0200 -0.1220 -0.0841 21  ASP A N   
137  C CA  . ASP A 21  ? 1.1558 0.8402 0.5895 -0.0236 -0.1576 -0.0781 21  ASP A CA  
138  C C   . ASP A 21  ? 1.1696 0.8802 0.6527 -0.0145 -0.1924 -0.0664 21  ASP A C   
139  O O   . ASP A 21  ? 1.3144 1.0081 0.7638 -0.0119 -0.2187 -0.0530 21  ASP A O   
140  C CB  . ASP A 21  ? 1.2568 0.9197 0.6483 -0.0357 -0.1740 -0.0969 21  ASP A CB  
141  C CG  . ASP A 21  ? 1.3411 0.9698 0.6717 -0.0452 -0.1404 -0.1092 21  ASP A CG  
142  O OD1 . ASP A 21  ? 1.3423 0.9501 0.6312 -0.0452 -0.1173 -0.0993 21  ASP A OD1 
143  O OD2 . ASP A 21  ? 1.3962 1.0182 0.7221 -0.0532 -0.1354 -0.1296 21  ASP A OD2 
144  N N   . SER A 22  ? 1.0292 0.7785 0.5907 -0.0096 -0.1926 -0.0714 22  SER A N   
145  C CA  . SER A 22  ? 0.9912 0.7676 0.6067 -0.0009 -0.2219 -0.0631 22  SER A CA  
146  C C   . SER A 22  ? 0.9394 0.7258 0.5801 0.0101  -0.2095 -0.0448 22  SER A C   
147  O O   . SER A 22  ? 0.9750 0.7816 0.6609 0.0188  -0.2303 -0.0375 22  SER A O   
148  C CB  . SER A 22  ? 0.9329 0.7446 0.6206 -0.0024 -0.2248 -0.0774 22  SER A CB  
149  O OG  . SER A 22  ? 0.9249 0.7571 0.6586 0.0017  -0.1916 -0.0760 22  SER A OG  
150  N N   . LEU A 23  ? 0.9444 0.7174 0.5592 0.0096  -0.1750 -0.0384 23  LEU A N   
151  C CA  . LEU A 23  ? 0.9028 0.6836 0.5394 0.0176  -0.1617 -0.0228 23  LEU A CA  
152  C C   . LEU A 23  ? 0.9339 0.6832 0.5178 0.0199  -0.1775 -0.0060 23  LEU A C   
153  O O   . LEU A 23  ? 0.9309 0.6454 0.4445 0.0128  -0.1837 -0.0057 23  LEU A O   
154  C CB  . LEU A 23  ? 0.8435 0.6262 0.4801 0.0151  -0.1204 -0.0241 23  LEU A CB  
155  C CG  . LEU A 23  ? 0.8232 0.6325 0.5086 0.0148  -0.0992 -0.0361 23  LEU A CG  
156  C CD1 . LEU A 23  ? 0.8197 0.6243 0.4923 0.0131  -0.0634 -0.0353 23  LEU A CD1 
157  C CD2 . LEU A 23  ? 0.7592 0.6016 0.5136 0.0216  -0.1046 -0.0333 23  LEU A CD2 
158  N N   . PRO A 24  ? 0.8756 0.6327 0.4890 0.0291  -0.1830 0.0081  24  PRO A N   
159  C CA  . PRO A 24  ? 0.9139 0.6359 0.4756 0.0311  -0.1900 0.0265  24  PRO A CA  
160  C C   . PRO A 24  ? 0.9490 0.6436 0.4535 0.0210  -0.1554 0.0286  24  PRO A C   
161  O O   . PRO A 24  ? 0.9137 0.6259 0.4416 0.0173  -0.1223 0.0204  24  PRO A O   
162  C CB  . PRO A 24  ? 0.8902 0.6307 0.5076 0.0419  -0.1896 0.0371  24  PRO A CB  
163  C CG  . PRO A 24  ? 0.8667 0.6508 0.5617 0.0466  -0.1951 0.0245  24  PRO A CG  
164  C CD  . PRO A 24  ? 0.8416 0.6364 0.5343 0.0372  -0.1803 0.0074  24  PRO A CD  
165  N N   . GLN A 25  ? 0.9857 0.6360 0.4150 0.0166  -0.1634 0.0401  25  GLN A N   
166  C CA  . GLN A 25  ? 1.0415 0.6612 0.4093 0.0048  -0.1297 0.0408  25  GLN A CA  
167  C C   . GLN A 25  ? 1.0010 0.6390 0.4061 0.0040  -0.0914 0.0430  25  GLN A C   
168  O O   . GLN A 25  ? 0.9590 0.6052 0.3655 -0.0031 -0.0582 0.0319  25  GLN A O   
169  C CB  . GLN A 25  ? 1.1997 0.7661 0.4835 0.0009  -0.1447 0.0575  25  GLN A CB  
170  C CG  . GLN A 25  ? 1.3157 0.8475 0.5365 -0.0126 -0.1059 0.0604  25  GLN A CG  
171  C CD  . GLN A 25  ? 1.4324 0.9265 0.6060 -0.0162 -0.1140 0.0766  25  GLN A CD  
172  O OE1 . GLN A 25  ? 1.4381 0.9251 0.6247 -0.0083 -0.1278 0.0936  25  GLN A OE1 
173  N NE2 . GLN A 25  ? 1.5068 0.9742 0.6247 -0.0280 -0.1050 0.0711  25  GLN A NE2 
174  N N   . GLU A 26  ? 0.9777 0.6220 0.4148 0.0112  -0.0960 0.0565  26  GLU A N   
175  C CA  . GLU A 26  ? 0.9257 0.5860 0.3955 0.0086  -0.0622 0.0581  26  GLU A CA  
176  C C   . GLU A 26  ? 0.8717 0.5794 0.4111 0.0115  -0.0483 0.0433  26  GLU A C   
177  O O   . GLU A 26  ? 0.8494 0.5716 0.4070 0.0066  -0.0174 0.0390  26  GLU A O   
178  C CB  . GLU A 26  ? 0.9683 0.6210 0.4547 0.0151  -0.0714 0.0744  26  GLU A CB  
179  C CG  . GLU A 26  ? 1.0749 0.6741 0.4882 0.0114  -0.0794 0.0922  26  GLU A CG  
180  C CD  . GLU A 26  ? 1.1455 0.7167 0.5004 -0.0045 -0.0443 0.0922  26  GLU A CD  
181  O OE1 . GLU A 26  ? 1.0922 0.6864 0.4788 -0.0110 -0.0101 0.0846  26  GLU A OE1 
182  O OE2 . GLU A 26  ? 1.2228 0.7487 0.4997 -0.0110 -0.0510 0.0993  26  GLU A OE2 
183  N N   . VAL A 27  ? 0.8420 0.5739 0.4217 0.0190  -0.0710 0.0357  27  VAL A N   
184  C CA  . VAL A 27  ? 0.7846 0.5546 0.4206 0.0205  -0.0576 0.0223  27  VAL A CA  
185  C C   . VAL A 27  ? 0.7665 0.5324 0.3781 0.0132  -0.0372 0.0096  27  VAL A C   
186  O O   . VAL A 27  ? 0.7175 0.5031 0.3572 0.0121  -0.0116 0.0033  27  VAL A O   
187  C CB  . VAL A 27  ? 0.7905 0.5838 0.4726 0.0280  -0.0842 0.0166  27  VAL A CB  
188  C CG1 . VAL A 27  ? 0.6543 0.4794 0.3844 0.0278  -0.0694 0.0035  27  VAL A CG1 
189  C CG2 . VAL A 27  ? 0.7388 0.5391 0.4545 0.0363  -0.0987 0.0273  27  VAL A CG2 
190  N N   . ARG A 28  ? 0.7505 0.4892 0.3084 0.0085  -0.0483 0.0054  28  ARG A N   
191  C CA  . ARG A 28  ? 0.8503 0.5822 0.3847 0.0017  -0.0271 -0.0089 28  ARG A CA  
192  C C   . ARG A 28  ? 0.8141 0.5374 0.3300 -0.0043 0.0098  -0.0074 28  ARG A C   
193  O O   . ARG A 28  ? 0.8181 0.5580 0.3586 -0.0048 0.0351  -0.0182 28  ARG A O   
194  C CB  . ARG A 28  ? 0.8339 0.5334 0.3061 -0.0043 -0.0456 -0.0148 28  ARG A CB  
195  C CG  . ARG A 28  ? 0.8914 0.5851 0.3470 -0.0107 -0.0228 -0.0330 28  ARG A CG  
196  C CD  . ARG A 28  ? 0.9886 0.6452 0.3730 -0.0196 -0.0360 -0.0415 28  ARG A CD  
197  N NE  . ARG A 28  ? 1.0151 0.6636 0.3845 -0.0256 -0.0061 -0.0595 28  ARG A NE  
198  C CZ  . ARG A 28  ? 1.0632 0.6911 0.3954 -0.0326 -0.0135 -0.0753 28  ARG A CZ  
199  N NH1 . ARG A 28  ? 1.0995 0.7146 0.4045 -0.0357 -0.0521 -0.0755 28  ARG A NH1 
200  N NH2 . ARG A 28  ? 1.0916 0.7119 0.4164 -0.0365 0.0181  -0.0921 28  ARG A NH2 
201  N N   . LYS A 29  ? 0.8059 0.5033 0.2813 -0.0090 0.0135  0.0059  29  LYS A N   
202  C CA  . LYS A 29  ? 0.8346 0.5257 0.2975 -0.0167 0.0504  0.0070  29  LYS A CA  
203  C C   . LYS A 29  ? 0.7925 0.5258 0.3281 -0.0121 0.0679  0.0050  29  LYS A C   
204  O O   . LYS A 29  ? 0.7511 0.4960 0.3008 -0.0157 0.0983  -0.0030 29  LYS A O   
205  C CB  . LYS A 29  ? 0.8998 0.5550 0.3117 -0.0230 0.0496  0.0239  29  LYS A CB  
206  C CG  . LYS A 29  ? 1.0683 0.6745 0.3948 -0.0294 0.0346  0.0277  29  LYS A CG  
207  C CD  . LYS A 29  ? 1.1306 0.6972 0.4058 -0.0351 0.0341  0.0473  29  LYS A CD  
208  C CE  . LYS A 29  ? 1.3442 0.8656 0.5427 -0.0417 0.0184  0.0515  29  LYS A CE  
209  N NZ  . LYS A 29  ? 1.4599 0.9684 0.6285 -0.0550 0.0524  0.0394  29  LYS A NZ  
210  N N   . PHE A 30  ? 0.7252 0.4812 0.3076 -0.0041 0.0485  0.0116  30  PHE A N   
211  C CA  . PHE A 30  ? 0.6536 0.4469 0.2994 -0.0005 0.0608  0.0102  30  PHE A CA  
212  C C   . PHE A 30  ? 0.6652 0.4844 0.3469 0.0039  0.0692  -0.0036 30  PHE A C   
213  O O   . PHE A 30  ? 0.6242 0.4646 0.3373 0.0037  0.0909  -0.0078 30  PHE A O   
214  C CB  . PHE A 30  ? 0.6104 0.4164 0.2903 0.0063  0.0380  0.0187  30  PHE A CB  
215  C CG  . PHE A 30  ? 0.5636 0.4039 0.3014 0.0087  0.0476  0.0173  30  PHE A CG  
216  C CD1 . PHE A 30  ? 0.5914 0.4402 0.3396 0.0025  0.0712  0.0186  30  PHE A CD1 
217  C CD2 . PHE A 30  ? 0.5378 0.4007 0.3179 0.0159  0.0325  0.0146  30  PHE A CD2 
218  C CE1 . PHE A 30  ? 0.5454 0.4248 0.3431 0.0038  0.0763  0.0172  30  PHE A CE1 
219  C CE2 . PHE A 30  ? 0.5144 0.4042 0.3391 0.0169  0.0402  0.0138  30  PHE A CE2 
220  C CZ  . PHE A 30  ? 0.5176 0.4155 0.3498 0.0111  0.0603  0.0152  30  PHE A CZ  
221  N N   . VAL A 31  ? 0.6606 0.4783 0.3411 0.0081  0.0509  -0.0105 31  VAL A N   
222  C CA  . VAL A 31  ? 0.6242 0.4601 0.3352 0.0121  0.0588  -0.0229 31  VAL A CA  
223  C C   . VAL A 31  ? 0.6657 0.4902 0.3533 0.0081  0.0861  -0.0326 31  VAL A C   
224  O O   . VAL A 31  ? 0.6554 0.5000 0.3784 0.0117  0.1052  -0.0382 31  VAL A O   
225  C CB  . VAL A 31  ? 0.6705 0.5035 0.3826 0.0147  0.0346  -0.0293 31  VAL A CB  
226  C CG1 . VAL A 31  ? 0.6050 0.4481 0.3405 0.0176  0.0451  -0.0423 31  VAL A CG1 
227  C CG2 . VAL A 31  ? 0.5653 0.4158 0.3136 0.0194  0.0131  -0.0221 31  VAL A CG2 
228  N N   . GLU A 32  ? 0.6820 0.4730 0.3093 0.0006  0.0887  -0.0346 32  GLU A N   
229  C CA  . GLU A 32  ? 0.7473 0.5239 0.3492 -0.0038 0.1163  -0.0472 32  GLU A CA  
230  C C   . GLU A 32  ? 0.7539 0.5398 0.3683 -0.0073 0.1483  -0.0454 32  GLU A C   
231  O O   . GLU A 32  ? 0.7416 0.5369 0.3751 -0.0057 0.1744  -0.0568 32  GLU A O   
232  C CB  . GLU A 32  ? 0.8612 0.5952 0.3871 -0.0127 0.1100  -0.0510 32  GLU A CB  
233  C CG  . GLU A 32  ? 0.8983 0.6250 0.4164 -0.0110 0.0920  -0.0634 32  GLU A CG  
234  C CD  . GLU A 32  ? 0.9610 0.6446 0.4007 -0.0214 0.0883  -0.0708 32  GLU A CD  
235  O OE1 . GLU A 32  ? 0.9277 0.5843 0.3136 -0.0283 0.0822  -0.0603 32  GLU A OE1 
236  O OE2 . GLU A 32  ? 1.0126 0.6863 0.4417 -0.0230 0.0912  -0.0872 32  GLU A OE2 
237  N N   . GLY A 33  ? 0.7589 0.5416 0.3647 -0.0124 0.1476  -0.0320 33  GLY A N   
238  C CA  . GLY A 33  ? 0.7278 0.5220 0.3510 -0.0180 0.1776  -0.0309 33  GLY A CA  
239  C C   . GLY A 33  ? 0.6807 0.5198 0.3795 -0.0096 0.1847  -0.0345 33  GLY A C   
240  O O   . GLY A 33  ? 0.6970 0.5517 0.4212 -0.0105 0.2123  -0.0425 33  GLY A O   
241  N N   . ASN A 34  ? 0.6393 0.4992 0.3748 -0.0013 0.1598  -0.0291 34  ASN A N   
242  C CA  . ASN A 34  ? 0.5994 0.4977 0.3992 0.0066  0.1626  -0.0312 34  ASN A CA  
243  C C   . ASN A 34  ? 0.6118 0.5172 0.4312 0.0159  0.1668  -0.0430 34  ASN A C   
244  O O   . ASN A 34  ? 0.6257 0.5577 0.4920 0.0223  0.1777  -0.0467 34  ASN A O   
245  C CB  . ASN A 34  ? 0.5979 0.5112 0.4235 0.0103  0.1377  -0.0215 34  ASN A CB  
246  C CG  . ASN A 34  ? 0.6122 0.5267 0.4375 0.0025  0.1401  -0.0118 34  ASN A CG  
247  O OD1 . ASN A 34  ? 0.6424 0.5764 0.4952 -0.0014 0.1571  -0.0127 34  ASN A OD1 
248  N ND2 . ASN A 34  ? 0.6354 0.5282 0.4305 -0.0002 0.1235  -0.0030 34  ASN A ND2 
249  N N   . ALA A 35  ? 0.6152 0.4964 0.4007 0.0167  0.1572  -0.0489 35  ALA A N   
250  C CA  . ALA A 35  ? 0.6034 0.4841 0.4016 0.0239  0.1655  -0.0616 35  ALA A CA  
251  C C   . ALA A 35  ? 0.6764 0.5553 0.4743 0.0226  0.1990  -0.0721 35  ALA A C   
252  O O   . ALA A 35  ? 0.6194 0.5175 0.4612 0.0320  0.2119  -0.0787 35  ALA A O   
253  C CB  . ALA A 35  ? 0.6207 0.4729 0.3776 0.0217  0.1499  -0.0679 35  ALA A CB  
254  N N   . GLN A 36  ? 0.6941 0.5492 0.4435 0.0111  0.2143  -0.0734 36  GLN A N   
255  C CA  . GLN A 36  ? 0.7212 0.5741 0.4702 0.0077  0.2511  -0.0845 36  GLN A CA  
256  C C   . GLN A 36  ? 0.6432 0.5371 0.4583 0.0119  0.2650  -0.0817 36  GLN A C   
257  O O   . GLN A 36  ? 0.6431 0.5530 0.4954 0.0179  0.2889  -0.0928 36  GLN A O   
258  C CB  . GLN A 36  ? 0.7877 0.6041 0.4660 -0.0079 0.2645  -0.0838 36  GLN A CB  
259  C CG  . GLN A 36  ? 0.9861 0.7940 0.6569 -0.0140 0.2952  -0.0954 36  GLN A CG  
260  C CD  . GLN A 36  ? 1.1683 0.9441 0.7779 -0.0305 0.3006  -0.0889 36  GLN A CD  
261  O OE1 . GLN A 36  ? 1.1625 0.9240 0.7390 -0.0363 0.2843  -0.0750 36  GLN A OE1 
262  N NE2 . GLN A 36  ? 1.1345 0.8960 0.7279 -0.0378 0.3232  -0.0984 36  GLN A NE2 
263  N N   . LEU A 37  ? 0.6435 0.5559 0.4780 0.0095  0.2486  -0.0679 37  LEU A N   
264  C CA  . LEU A 37  ? 0.5822 0.5339 0.4776 0.0112  0.2577  -0.0654 37  LEU A CA  
265  C C   . LEU A 37  ? 0.5813 0.5648 0.5375 0.0271  0.2443  -0.0662 37  LEU A C   
266  O O   . LEU A 37  ? 0.5540 0.5655 0.5614 0.0335  0.2596  -0.0725 37  LEU A O   
267  C CB  . LEU A 37  ? 0.5989 0.5546 0.4893 0.0019  0.2445  -0.0515 37  LEU A CB  
268  C CG  . LEU A 37  ? 0.5721 0.5695 0.5252 0.0022  0.2463  -0.0486 37  LEU A CG  
269  C CD1 . LEU A 37  ? 0.6396 0.6469 0.6071 -0.0081 0.2802  -0.0556 37  LEU A CD1 
270  C CD2 . LEU A 37  ? 0.6414 0.6406 0.5914 -0.0029 0.2232  -0.0354 37  LEU A CD2 
271  N N   . CYS A 38  ? 0.5447 0.5240 0.4970 0.0333  0.2156  -0.0596 38  CYS A N   
272  C CA  . CYS A 38  ? 0.5468 0.5509 0.5483 0.0464  0.2004  -0.0569 38  CYS A CA  
273  C C   . CYS A 38  ? 0.5449 0.5395 0.5544 0.0586  0.2051  -0.0666 38  CYS A C   
274  O O   . CYS A 38  ? 0.5535 0.5668 0.6061 0.0709  0.1975  -0.0647 38  CYS A O   
275  C CB  . CYS A 38  ? 0.4690 0.4718 0.4631 0.0457  0.1709  -0.0456 38  CYS A CB  
276  S SG  . CYS A 38  ? 0.5251 0.5361 0.5134 0.0333  0.1631  -0.0344 38  CYS A SG  
277  N N   A GLN A 39  ? 0.5581 0.5211 0.5241 0.0550  0.2164  -0.0765 39  GLN A N   
278  N N   B GLN A 39  ? 0.5575 0.5203 0.5231 0.0549  0.2161  -0.0764 39  GLN A N   
279  C CA  A GLN A 39  ? 0.5855 0.5330 0.5532 0.0645  0.2247  -0.0883 39  GLN A CA  
280  C CA  B GLN A 39  ? 0.5867 0.5328 0.5515 0.0639  0.2246  -0.0884 39  GLN A CA  
281  C C   A GLN A 39  ? 0.5726 0.5183 0.5549 0.0737  0.2009  -0.0835 39  GLN A C   
282  C C   B GLN A 39  ? 0.5740 0.5189 0.5550 0.0735  0.2013  -0.0838 39  GLN A C   
283  O O   A GLN A 39  ? 0.5579 0.5121 0.5785 0.0872  0.2040  -0.0858 39  GLN A O   
284  O O   B GLN A 39  ? 0.5593 0.5123 0.5783 0.0869  0.2051  -0.0866 39  GLN A O   
285  C CB  A GLN A 39  ? 0.5870 0.5545 0.6024 0.0743  0.2504  -0.0973 39  GLN A CB  
286  C CB  B GLN A 39  ? 0.5915 0.5552 0.5998 0.0728  0.2520  -0.0983 39  GLN A CB  
287  C CG  A GLN A 39  ? 0.6049 0.5655 0.6012 0.0646  0.2832  -0.1081 39  GLN A CG  
288  C CG  B GLN A 39  ? 0.5991 0.5665 0.5973 0.0616  0.2799  -0.1037 39  GLN A CG  
289  C CD  A GLN A 39  ? 0.6538 0.5725 0.5890 0.0570  0.2918  -0.1192 39  GLN A CD  
290  C CD  B GLN A 39  ? 0.5882 0.5734 0.6299 0.0680  0.2996  -0.1131 39  GLN A CD  
291  O OE1 A GLN A 39  ? 0.6863 0.5829 0.5674 0.0419  0.2970  -0.1190 39  GLN A OE1 
292  O OE1 B GLN A 39  ? 0.6499 0.6162 0.6817 0.0723  0.3089  -0.1239 39  GLN A OE1 
293  N NE2 A GLN A 39  ? 0.7144 0.6199 0.6561 0.0666  0.2914  -0.1283 39  GLN A NE2 
294  N NE2 B GLN A 39  ? 0.5770 0.5991 0.6679 0.0679  0.3038  -0.1090 39  GLN A NE2 
295  N N   . PRO A 40  ? 0.5517 0.4850 0.5060 0.0672  0.1781  -0.0769 40  PRO A N   
296  C CA  . PRO A 40  ? 0.5426 0.4704 0.5084 0.0736  0.1604  -0.0743 40  PRO A CA  
297  C C   . PRO A 40  ? 0.6000 0.4991 0.5479 0.0763  0.1699  -0.0884 40  PRO A C   
298  O O   . PRO A 40  ? 0.5866 0.4653 0.4991 0.0699  0.1843  -0.1000 40  PRO A O   
299  C CB  . PRO A 40  ? 0.5512 0.4746 0.4927 0.0638  0.1379  -0.0664 40  PRO A CB  
300  C CG  . PRO A 40  ? 0.5538 0.4626 0.4521 0.0530  0.1442  -0.0700 40  PRO A CG  
301  C CD  . PRO A 40  ? 0.5781 0.5006 0.4911 0.0542  0.1676  -0.0716 40  PRO A CD  
302  N N   . GLU A 41  ? 0.5602 0.4544 0.5297 0.0851  0.1627  -0.0877 41  GLU A N   
303  C CA  . GLU A 41  ? 0.5730 0.4364 0.5256 0.0865  0.1708  -0.1017 41  GLU A CA  
304  C C   . GLU A 41  ? 0.6035 0.4448 0.5154 0.0732  0.1552  -0.1061 41  GLU A C   
305  O O   . GLU A 41  ? 0.6679 0.4816 0.5483 0.0679  0.1628  -0.1210 41  GLU A O   
306  C CB  . GLU A 41  ? 0.6048 0.4658 0.5938 0.1005  0.1694  -0.0986 41  GLU A CB  
307  C CG  . GLU A 41  ? 0.6463 0.4740 0.6255 0.1047  0.1844  -0.1147 41  GLU A CG  
308  C CD  . GLU A 41  ? 0.7874 0.6107 0.7627 0.1079  0.2120  -0.1291 41  GLU A CD  
309  O OE1 . GLU A 41  ? 0.7852 0.6363 0.7871 0.1134  0.2215  -0.1245 41  GLU A OE1 
310  O OE2 . GLU A 41  ? 0.9087 0.7004 0.8543 0.1037  0.2256  -0.1463 41  GLU A OE2 
311  N N   . TYR A 42  ? 0.5597 0.4132 0.4740 0.0677  0.1335  -0.0948 42  TYR A N   
312  C CA  . TYR A 42  ? 0.5679 0.4080 0.4572 0.0564  0.1154  -0.0979 42  TYR A CA  
313  C C   . TYR A 42  ? 0.5630 0.4204 0.4456 0.0498  0.1000  -0.0872 42  TYR A C   
314  O O   . TYR A 42  ? 0.5574 0.4374 0.4623 0.0540  0.1005  -0.0756 42  TYR A O   
315  C CB  . TYR A 42  ? 0.5606 0.3965 0.4717 0.0574  0.1050  -0.0956 42  TYR A CB  
316  C CG  . TYR A 42  ? 0.6103 0.4291 0.5361 0.0667  0.1191  -0.1017 42  TYR A CG  
317  C CD1 . TYR A 42  ? 0.6372 0.4262 0.5410 0.0628  0.1269  -0.1182 42  TYR A CD1 
318  C CD2 . TYR A 42  ? 0.6470 0.4771 0.6074 0.0797  0.1231  -0.0907 42  TYR A CD2 
319  C CE1 . TYR A 42  ? 0.6930 0.4622 0.6111 0.0723  0.1410  -0.1241 42  TYR A CE1 
320  C CE2 . TYR A 42  ? 0.6555 0.4671 0.6306 0.0903  0.1344  -0.0947 42  TYR A CE2 
321  C CZ  . TYR A 42  ? 0.6543 0.4348 0.6093 0.0870  0.1444  -0.1114 42  TYR A CZ  
322  O OH  . TYR A 42  ? 0.7938 0.5519 0.7641 0.0985  0.1569  -0.1159 42  TYR A OH  
323  N N   . ILE A 43  ? 0.5856 0.4318 0.4393 0.0397  0.0848  -0.0913 43  ILE A N   
324  C CA  . ILE A 43  ? 0.5083 0.3678 0.3592 0.0349  0.0671  -0.0813 43  ILE A CA  
325  C C   . ILE A 43  ? 0.5377 0.3977 0.3992 0.0296  0.0468  -0.0832 43  ILE A C   
326  O O   . ILE A 43  ? 0.5376 0.3803 0.3812 0.0233  0.0399  -0.0950 43  ILE A O   
327  C CB  . ILE A 43  ? 0.5687 0.4155 0.3756 0.0287  0.0655  -0.0822 43  ILE A CB  
328  C CG1 . ILE A 43  ? 0.5692 0.4174 0.3702 0.0320  0.0897  -0.0810 43  ILE A CG1 
329  C CG2 . ILE A 43  ? 0.5404 0.3979 0.3473 0.0257  0.0454  -0.0709 43  ILE A CG2 
330  C CD1 . ILE A 43  ? 0.6836 0.5113 0.4331 0.0242  0.0944  -0.0831 43  ILE A CD1 
331  N N   . HIS A 44  ? 0.4497 0.3297 0.3408 0.0310  0.0384  -0.0730 44  HIS A N   
332  C CA  . HIS A 44  ? 0.4565 0.3418 0.3671 0.0258  0.0231  -0.0747 44  HIS A CA  
333  C C   . HIS A 44  ? 0.4557 0.3548 0.3694 0.0241  0.0076  -0.0671 44  HIS A C   
334  O O   . HIS A 44  ? 0.4319 0.3455 0.3604 0.0279  0.0114  -0.0565 44  HIS A O   
335  C CB  . HIS A 44  ? 0.4578 0.3508 0.4009 0.0289  0.0309  -0.0700 44  HIS A CB  
336  C CG  . HIS A 44  ? 0.4829 0.3818 0.4488 0.0220  0.0207  -0.0721 44  HIS A CG  
337  N ND1 . HIS A 44  ? 0.4883 0.3751 0.4644 0.0174  0.0245  -0.0794 44  HIS A ND1 
338  C CD2 . HIS A 44  ? 0.4406 0.3556 0.4238 0.0187  0.0093  -0.0686 44  HIS A CD2 
339  C CE1 . HIS A 44  ? 0.4788 0.3758 0.4780 0.0101  0.0167  -0.0808 44  HIS A CE1 
340  N NE2 . HIS A 44  ? 0.4629 0.3781 0.4685 0.0116  0.0075  -0.0746 44  HIS A NE2 
341  N N   . ILE A 45  ? 0.4757 0.3694 0.3765 0.0187  -0.0110 -0.0726 45  ILE A N   
342  C CA  . ILE A 45  ? 0.4795 0.3842 0.3866 0.0190  -0.0284 -0.0655 45  ILE A CA  
343  C C   . ILE A 45  ? 0.4770 0.3992 0.4278 0.0167  -0.0364 -0.0676 45  ILE A C   
344  O O   . ILE A 45  ? 0.4765 0.3977 0.4378 0.0107  -0.0464 -0.0782 45  ILE A O   
345  C CB  . ILE A 45  ? 0.4976 0.3873 0.3685 0.0155  -0.0477 -0.0689 45  ILE A CB  
346  C CG1 . ILE A 45  ? 0.5678 0.4361 0.3899 0.0156  -0.0351 -0.0680 45  ILE A CG1 
347  C CG2 . ILE A 45  ? 0.5003 0.4002 0.3825 0.0186  -0.0673 -0.0597 45  ILE A CG2 
348  C CD1 . ILE A 45  ? 0.6414 0.4873 0.4160 0.0101  -0.0526 -0.0726 45  ILE A CD1 
349  N N   . CYS A 46  ? 0.4405 0.3782 0.4169 0.0202  -0.0309 -0.0587 46  CYS A N   
350  C CA  . CYS A 46  ? 0.4206 0.3733 0.4379 0.0172  -0.0314 -0.0614 46  CYS A CA  
351  C C   . CYS A 46  ? 0.4384 0.4010 0.4759 0.0151  -0.0530 -0.0666 46  CYS A C   
352  O O   . CYS A 46  ? 0.4388 0.4012 0.4655 0.0195  -0.0679 -0.0615 46  CYS A O   
353  C CB  . CYS A 46  ? 0.3588 0.3224 0.3920 0.0206  -0.0195 -0.0518 46  CYS A CB  
354  S SG  . CYS A 46  ? 0.4184 0.3755 0.4382 0.0232  0.0014  -0.0460 46  CYS A SG  
355  N N   . ASP A 47  ? 0.4488 0.4201 0.5185 0.0083  -0.0548 -0.0766 47  ASP A N   
356  C CA  . ASP A 47  ? 0.4205 0.4083 0.5242 0.0064  -0.0745 -0.0829 47  ASP A CA  
357  C C   . ASP A 47  ? 0.3850 0.3925 0.5368 0.0055  -0.0648 -0.0833 47  ASP A C   
358  O O   . ASP A 47  ? 0.4002 0.4254 0.5898 0.0056  -0.0792 -0.0887 47  ASP A O   
359  C CB  . ASP A 47  ? 0.4006 0.3863 0.5098 -0.0031 -0.0869 -0.0976 47  ASP A CB  
360  C CG  . ASP A 47  ? 0.4487 0.4309 0.5749 -0.0128 -0.0671 -0.1058 47  ASP A CG  
361  O OD1 . ASP A 47  ? 0.4706 0.4557 0.6120 -0.0130 -0.0464 -0.1008 47  ASP A OD1 
362  O OD2 . ASP A 47  ? 0.4980 0.4711 0.6185 -0.0214 -0.0728 -0.1176 47  ASP A OD2 
363  N N   . GLY A 48  ? 0.3688 0.3734 0.5204 0.0046  -0.0411 -0.0781 48  GLY A N   
364  C CA  . GLY A 48  ? 0.3944 0.4132 0.5837 0.0022  -0.0287 -0.0791 48  GLY A CA  
365  C C   . GLY A 48  ? 0.4389 0.4659 0.6651 -0.0091 -0.0210 -0.0913 48  GLY A C   
366  O O   . GLY A 48  ? 0.3844 0.4236 0.6445 -0.0125 -0.0086 -0.0944 48  GLY A O   
367  N N   . SER A 49  ? 0.4016 0.4205 0.6216 -0.0164 -0.0252 -0.0995 49  SER A N   
368  C CA  . SER A 49  ? 0.4413 0.4688 0.7001 -0.0293 -0.0198 -0.1129 49  SER A CA  
369  C C   . SER A 49  ? 0.4545 0.4676 0.7090 -0.0379 0.0091  -0.1110 49  SER A C   
370  O O   . SER A 49  ? 0.3921 0.3856 0.6086 -0.0337 0.0205  -0.1000 49  SER A O   
371  C CB  . SER A 49  ? 0.4311 0.4520 0.6826 -0.0358 -0.0355 -0.1236 49  SER A CB  
372  O OG  . SER A 49  ? 0.4930 0.4861 0.7017 -0.0369 -0.0237 -0.1200 49  SER A OG  
373  N N   . GLU A 50  ? 0.4844 0.5068 0.7791 -0.0506 0.0204  -0.1219 50  GLU A N   
374  C CA  . GLU A 50  ? 0.4856 0.4892 0.7727 -0.0614 0.0482  -0.1203 50  GLU A CA  
375  C C   . GLU A 50  ? 0.4926 0.4662 0.7420 -0.0644 0.0515  -0.1179 50  GLU A C   
376  O O   . GLU A 50  ? 0.4999 0.4494 0.7183 -0.0641 0.0682  -0.1074 50  GLU A O   
377  C CB  . GLU A 50  ? 0.5065 0.5252 0.8459 -0.0770 0.0611  -0.1346 50  GLU A CB  
378  C CG  . GLU A 50  ? 0.5927 0.6353 0.9696 -0.0748 0.0689  -0.1368 50  GLU A CG  
379  C CD  . GLU A 50  ? 0.6485 0.6736 0.9931 -0.0732 0.0919  -0.1247 50  GLU A CD  
380  O OE1 . GLU A 50  ? 0.6904 0.6858 0.9913 -0.0768 0.1041  -0.1155 50  GLU A OE1 
381  O OE2 . GLU A 50  ? 0.6836 0.7232 1.0462 -0.0682 0.0968  -0.1245 50  GLU A OE2 
382  N N   . GLU A 51  ? 0.4936 0.4667 0.7450 -0.0671 0.0351  -0.1279 51  GLU A N   
383  C CA  . GLU A 51  ? 0.5495 0.4917 0.7660 -0.0691 0.0391  -0.1275 51  GLU A CA  
384  C C   . GLU A 51  ? 0.5838 0.5102 0.7552 -0.0537 0.0399  -0.1122 51  GLU A C   
385  O O   . GLU A 51  ? 0.5391 0.4391 0.6850 -0.0524 0.0540  -0.1049 51  GLU A O   
386  C CB  . GLU A 51  ? 0.5150 0.4593 0.7361 -0.0743 0.0192  -0.1422 51  GLU A CB  
387  C CG  . GLU A 51  ? 0.6353 0.5942 0.9041 -0.0921 0.0175  -0.1598 51  GLU A CG  
388  C CD  . GLU A 51  ? 0.6743 0.6725 0.9938 -0.0918 0.0072  -0.1645 51  GLU A CD  
389  O OE1 . GLU A 51  ? 0.5607 0.5733 0.8741 -0.0770 -0.0064 -0.1557 51  GLU A OE1 
390  O OE2 . GLU A 51  ? 0.7267 0.7405 1.0947 -0.1065 0.0139  -0.1774 51  GLU A OE2 
391  N N   . GLU A 52  ? 0.5161 0.4583 0.6794 -0.0418 0.0249  -0.1071 52  GLU A N   
392  C CA  . GLU A 52  ? 0.5001 0.4314 0.6264 -0.0285 0.0261  -0.0944 52  GLU A CA  
393  C C   . GLU A 52  ? 0.5415 0.4669 0.6601 -0.0254 0.0428  -0.0813 52  GLU A C   
394  O O   . GLU A 52  ? 0.5458 0.4535 0.6385 -0.0189 0.0499  -0.0724 52  GLU A O   
395  C CB  . GLU A 52  ? 0.4983 0.4464 0.6191 -0.0193 0.0084  -0.0918 52  GLU A CB  
396  C CG  . GLU A 52  ? 0.4402 0.3849 0.5337 -0.0076 0.0127  -0.0784 52  GLU A CG  
397  C CD  . GLU A 52  ? 0.4888 0.4459 0.5754 -0.0006 -0.0026 -0.0753 52  GLU A CD  
398  O OE1 . GLU A 52  ? 0.4873 0.4365 0.5502 0.0019  -0.0128 -0.0783 52  GLU A OE1 
399  O OE2 . GLU A 52  ? 0.4211 0.3925 0.5232 0.0019  -0.0031 -0.0700 52  GLU A OE2 
400  N N   . TYR A 53  ? 0.5090 0.4492 0.6504 -0.0299 0.0487  -0.0804 53  TYR A N   
401  C CA  . TYR A 53  ? 0.5073 0.4394 0.6369 -0.0298 0.0643  -0.0695 53  TYR A CA  
402  C C   . TYR A 53  ? 0.5246 0.4278 0.6379 -0.0362 0.0790  -0.0662 53  TYR A C   
403  O O   . TYR A 53  ? 0.5249 0.4116 0.6104 -0.0299 0.0839  -0.0537 53  TYR A O   
404  C CB  . TYR A 53  ? 0.4980 0.4476 0.6567 -0.0366 0.0715  -0.0737 53  TYR A CB  
405  C CG  . TYR A 53  ? 0.4998 0.4437 0.6428 -0.0368 0.0852  -0.0639 53  TYR A CG  
406  C CD1 . TYR A 53  ? 0.5076 0.4522 0.6259 -0.0262 0.0793  -0.0528 53  TYR A CD1 
407  C CD2 . TYR A 53  ? 0.5785 0.5163 0.7314 -0.0494 0.1048  -0.0672 53  TYR A CD2 
408  C CE1 . TYR A 53  ? 0.5491 0.4884 0.6513 -0.0280 0.0896  -0.0454 53  TYR A CE1 
409  C CE2 . TYR A 53  ? 0.5817 0.5112 0.7140 -0.0513 0.1172  -0.0595 53  TYR A CE2 
410  C CZ  . TYR A 53  ? 0.5941 0.5244 0.7004 -0.0406 0.1080  -0.0487 53  TYR A CZ  
411  O OH  . TYR A 53  ? 0.6262 0.5475 0.7098 -0.0441 0.1184  -0.0423 53  TYR A OH  
412  N N   . GLY A 54  ? 0.5347 0.4305 0.6658 -0.0487 0.0849  -0.0772 54  GLY A N   
413  C CA  . GLY A 54  ? 0.5789 0.4418 0.6931 -0.0559 0.0998  -0.0738 54  GLY A CA  
414  C C   . GLY A 54  ? 0.6647 0.5056 0.7491 -0.0441 0.0948  -0.0668 54  GLY A C   
415  O O   . GLY A 54  ? 0.6639 0.4786 0.7238 -0.0406 0.1035  -0.0546 54  GLY A O   
416  N N   . ARG A 55  ? 0.6712 0.5213 0.7567 -0.0373 0.0805  -0.0742 55  ARG A N   
417  C CA  . ARG A 55  ? 0.6942 0.5255 0.7553 -0.0256 0.0782  -0.0702 55  ARG A CA  
418  C C   . ARG A 55  ? 0.7353 0.5710 0.7792 -0.0107 0.0769  -0.0545 55  ARG A C   
419  O O   . ARG A 55  ? 0.7746 0.5892 0.8021 -0.0020 0.0816  -0.0457 55  ARG A O   
420  C CB  . ARG A 55  ? 0.7107 0.5504 0.7724 -0.0238 0.0651  -0.0832 55  ARG A CB  
421  C CG  . ARG A 55  ? 0.8199 0.6499 0.8944 -0.0384 0.0643  -0.0999 55  ARG A CG  
422  C CD  . ARG A 55  ? 0.9802 0.7728 1.0443 -0.0426 0.0800  -0.0989 55  ARG A CD  
423  N NE  . ARG A 55  ? 1.1145 0.8936 1.1894 -0.0582 0.0811  -0.1160 55  ARG A NE  
424  C CZ  . ARG A 55  ? 1.1990 0.9431 1.2684 -0.0658 0.0955  -0.1177 55  ARG A CZ  
425  N NH1 . ARG A 55  ? 1.2450 0.9625 1.2965 -0.0581 0.1087  -0.1017 55  ARG A NH1 
426  N NH2 . ARG A 55  ? 1.1588 0.8927 1.2401 -0.0820 0.0955  -0.1355 55  ARG A NH2 
427  N N   . LEU A 56  ? 0.5700 0.4326 0.6200 -0.0075 0.0700  -0.0512 56  LEU A N   
428  C CA  . LEU A 56  ? 0.5763 0.4452 0.6130 0.0040  0.0684  -0.0378 56  LEU A CA  
429  C C   . LEU A 56  ? 0.5961 0.4474 0.6205 0.0025  0.0772  -0.0256 56  LEU A C   
430  O O   . LEU A 56  ? 0.6401 0.4824 0.6504 0.0132  0.0757  -0.0145 56  LEU A O   
431  C CB  . LEU A 56  ? 0.5939 0.4908 0.6393 0.0047  0.0612  -0.0373 56  LEU A CB  
432  C CG  . LEU A 56  ? 0.6691 0.5846 0.7198 0.0080  0.0496  -0.0440 56  LEU A CG  
433  C CD1 . LEU A 56  ? 0.5451 0.4800 0.6123 0.0036  0.0465  -0.0447 56  LEU A CD1 
434  C CD2 . LEU A 56  ? 0.6116 0.5316 0.6474 0.0194  0.0464  -0.0378 56  LEU A CD2 
435  N N   . LEU A 57  ? 0.5636 0.4107 0.5934 -0.0107 0.0862  -0.0274 57  LEU A N   
436  C CA  . LEU A 57  ? 0.6346 0.4590 0.6445 -0.0152 0.0961  -0.0159 57  LEU A CA  
437  C C   . LEU A 57  ? 0.6730 0.4623 0.6664 -0.0119 0.1003  -0.0098 57  LEU A C   
438  O O   . LEU A 57  ? 0.6686 0.4403 0.6398 -0.0036 0.0982  0.0049  57  LEU A O   
439  C CB  . LEU A 57  ? 0.5724 0.3965 0.5926 -0.0325 0.1097  -0.0225 57  LEU A CB  
440  C CG  . LEU A 57  ? 0.5972 0.4504 0.6321 -0.0349 0.1085  -0.0265 57  LEU A CG  
441  C CD1 . LEU A 57  ? 0.6297 0.4854 0.6860 -0.0515 0.1240  -0.0373 57  LEU A CD1 
442  C CD2 . LEU A 57  ? 0.5872 0.4378 0.5955 -0.0301 0.1069  -0.0134 57  LEU A CD2 
443  N N   . ALA A 58  ? 0.6743 0.4515 0.6789 -0.0185 0.1052  -0.0211 58  ALA A N   
444  C CA  . ALA A 58  ? 0.7035 0.4437 0.6938 -0.0150 0.1102  -0.0168 58  ALA A CA  
445  C C   . ALA A 58  ? 0.7017 0.4412 0.6842 0.0056  0.1001  -0.0089 58  ALA A C   
446  O O   . ALA A 58  ? 0.7304 0.4438 0.6958 0.0147  0.1005  0.0048  58  ALA A O   
447  C CB  . ALA A 58  ? 0.7317 0.4631 0.7380 -0.0260 0.1154  -0.0338 58  ALA A CB  
448  N N   . HIS A 59  ? 0.6698 0.4376 0.6652 0.0133  0.0911  -0.0170 59  HIS A N   
449  C CA  . HIS A 59  ? 0.6877 0.4604 0.6815 0.0317  0.0846  -0.0117 59  HIS A CA  
450  C C   . HIS A 59  ? 0.7550 0.5310 0.7395 0.0412  0.0788  0.0060  59  HIS A C   
451  O O   . HIS A 59  ? 0.7335 0.4918 0.7128 0.0544  0.0767  0.0162  59  HIS A O   
452  C CB  . HIS A 59  ? 0.6867 0.4906 0.6912 0.0347  0.0780  -0.0221 59  HIS A CB  
453  C CG  . HIS A 59  ? 0.7231 0.5370 0.7294 0.0514  0.0747  -0.0178 59  HIS A CG  
454  N ND1 . HIS A 59  ? 0.7677 0.6119 0.7791 0.0556  0.0684  -0.0147 59  HIS A ND1 
455  C CD2 . HIS A 59  ? 0.7226 0.5206 0.7301 0.0646  0.0784  -0.0170 59  HIS A CD2 
456  C CE1 . HIS A 59  ? 0.7418 0.5906 0.7589 0.0695  0.0690  -0.0126 59  HIS A CE1 
457  N NE2 . HIS A 59  ? 0.7611 0.5831 0.7775 0.0761  0.0750  -0.0141 59  HIS A NE2 
458  N N   . MET A 60  ? 0.6725 0.4709 0.6559 0.0349  0.0750  0.0093  60  MET A N   
459  C CA  . MET A 60  ? 0.6756 0.4804 0.6487 0.0416  0.0671  0.0241  60  MET A CA  
460  C C   . MET A 60  ? 0.6829 0.4523 0.6325 0.0411  0.0687  0.0382  60  MET A C   
461  O O   . MET A 60  ? 0.7345 0.5006 0.6751 0.0525  0.0582  0.0520  60  MET A O   
462  C CB  . MET A 60  ? 0.5989 0.4285 0.5722 0.0318  0.0656  0.0224  60  MET A CB  
463  C CG  . MET A 60  ? 0.6200 0.4831 0.6107 0.0362  0.0597  0.0150  60  MET A CG  
464  S SD  . MET A 60  ? 0.6096 0.4951 0.5986 0.0269  0.0578  0.0154  60  MET A SD  
465  C CE  . MET A 60  ? 0.5254 0.4092 0.5250 0.0120  0.0679  0.0024  60  MET A CE  
466  N N   . GLN A 61  ? 0.6970 0.4394 0.6361 0.0275  0.0811  0.0354  61  GLN A N   
467  C CA  . GLN A 61  ? 0.7600 0.4610 0.6702 0.0252  0.0850  0.0498  61  GLN A CA  
468  C C   . GLN A 61  ? 0.8354 0.5097 0.7454 0.0414  0.0811  0.0567  61  GLN A C   
469  O O   . GLN A 61  ? 0.7764 0.4224 0.6638 0.0492  0.0749  0.0742  61  GLN A O   
470  C CB  . GLN A 61  ? 0.7790 0.4580 0.6813 0.0041  0.1032  0.0430  61  GLN A CB  
471  C CG  . GLN A 61  ? 0.7925 0.4261 0.6561 -0.0036 0.1108  0.0586  61  GLN A CG  
472  C CD  . GLN A 61  ? 0.9012 0.5171 0.7622 -0.0272 0.1331  0.0493  61  GLN A CD  
473  O OE1 . GLN A 61  ? 0.9209 0.5542 0.8135 -0.0354 0.1404  0.0313  61  GLN A OE1 
474  N NE2 . GLN A 61  ? 0.9697 0.5511 0.7929 -0.0393 0.1439  0.0611  61  GLN A NE2 
475  N N   . GLU A 62  ? 0.8091 0.4899 0.7423 0.0468  0.0844  0.0431  62  GLU A N   
476  C CA  . GLU A 62  ? 0.9003 0.5557 0.8375 0.0629  0.0836  0.0464  62  GLU A CA  
477  C C   . GLU A 62  ? 0.8773 0.5537 0.8282 0.0850  0.0692  0.0548  62  GLU A C   
478  O O   . GLU A 62  ? 0.9053 0.5585 0.8584 0.1016  0.0656  0.0638  62  GLU A O   
479  C CB  . GLU A 62  ? 0.8710 0.5242 0.8251 0.0591  0.0937  0.0263  62  GLU A CB  
480  C CG  . GLU A 62  ? 0.8408 0.4724 0.7881 0.0369  0.1072  0.0165  62  GLU A CG  
481  C CD  . GLU A 62  ? 0.7792 0.4183 0.7436 0.0299  0.1125  -0.0060 62  GLU A CD  
482  O OE1 . GLU A 62  ? 0.7456 0.4006 0.7209 0.0423  0.1079  -0.0136 62  GLU A OE1 
483  O OE2 . GLU A 62  ? 0.7985 0.4274 0.7649 0.0109  0.1213  -0.0167 62  GLU A OE2 
484  N N   . GLU A 63  ? 0.8081 0.5274 0.7710 0.0856  0.0613  0.0520  63  GLU A N   
485  C CA  . GLU A 63  ? 0.8343 0.5794 0.8154 0.1036  0.0484  0.0585  63  GLU A CA  
486  C C   . GLU A 63  ? 0.8776 0.6252 0.8430 0.1057  0.0329  0.0766  63  GLU A C   
487  O O   . GLU A 63  ? 0.8928 0.6688 0.8759 0.1175  0.0198  0.0811  63  GLU A O   
488  C CB  . GLU A 63  ? 0.7800 0.5683 0.7822 0.1018  0.0495  0.0447  63  GLU A CB  
489  C CG  . GLU A 63  ? 0.8386 0.6255 0.8490 0.0974  0.0623  0.0262  63  GLU A CG  
490  C CD  . GLU A 63  ? 0.8951 0.6758 0.9236 0.1143  0.0673  0.0208  63  GLU A CD  
491  O OE1 . GLU A 63  ? 0.8983 0.6732 0.9375 0.1309  0.0609  0.0322  63  GLU A OE1 
492  O OE2 . GLU A 63  ? 0.9245 0.7058 0.9564 0.1110  0.0772  0.0046  63  GLU A OE2 
493  N N   . GLY A 64  ? 0.8413 0.5603 0.7728 0.0928  0.0346  0.0858  64  GLY A N   
494  C CA  . GLY A 64  ? 0.8241 0.5411 0.7310 0.0917  0.0200  0.1020  64  GLY A CA  
495  C C   . GLY A 64  ? 0.8158 0.5725 0.7262 0.0827  0.0147  0.0968  64  GLY A C   
496  O O   . GLY A 64  ? 0.8836 0.6465 0.7801 0.0848  -0.0013 0.1083  64  GLY A O   
497  N N   . VAL A 65  ? 0.7614 0.5430 0.6883 0.0726  0.0263  0.0801  65  VAL A N   
498  C CA  . VAL A 65  ? 0.7513 0.5672 0.6824 0.0650  0.0221  0.0752  65  VAL A CA  
499  C C   . VAL A 65  ? 0.7550 0.5575 0.6554 0.0459  0.0293  0.0760  65  VAL A C   
500  O O   . VAL A 65  ? 0.7177 0.5332 0.6058 0.0405  0.0217  0.0791  65  VAL A O   
501  C CB  . VAL A 65  ? 0.7340 0.5807 0.6952 0.0646  0.0294  0.0587  65  VAL A CB  
502  C CG1 . VAL A 65  ? 0.6552 0.5336 0.6214 0.0586  0.0245  0.0553  65  VAL A CG1 
503  C CG2 . VAL A 65  ? 0.7740 0.6295 0.7616 0.0817  0.0271  0.0562  65  VAL A CG2 
504  N N   . ILE A 66  ? 0.7357 0.5126 0.6246 0.0341  0.0455  0.0715  66  ILE A N   
505  C CA  . ILE A 66  ? 0.6599 0.4214 0.5213 0.0155  0.0568  0.0713  66  ILE A CA  
506  C C   . ILE A 66  ? 0.7544 0.4688 0.5865 0.0091  0.0668  0.0800  66  ILE A C   
507  O O   . ILE A 66  ? 0.6771 0.3720 0.5157 0.0177  0.0673  0.0829  66  ILE A O   
508  C CB  . ILE A 66  ? 0.6934 0.4763 0.5766 0.0026  0.0714  0.0535  66  ILE A CB  
509  C CG1 . ILE A 66  ? 0.6678 0.4488 0.5765 0.0025  0.0804  0.0423  66  ILE A CG1 
510  C CG2 . ILE A 66  ? 0.6873 0.5093 0.5898 0.0060  0.0629  0.0471  66  ILE A CG2 
511  C CD1 . ILE A 66  ? 0.6936 0.5043 0.6316 -0.0048 0.0864  0.0255  66  ILE A CD1 
512  N N   . ARG A 67  ? 0.7389 0.4324 0.5365 -0.0073 0.0769  0.0835  67  ARG A N   
513  C CA  . ARG A 67  ? 0.7357 0.3808 0.4981 -0.0190 0.0916  0.0913  67  ARG A CA  
514  C C   . ARG A 67  ? 0.7565 0.4024 0.5235 -0.0411 0.1175  0.0763  67  ARG A C   
515  O O   . ARG A 67  ? 0.6907 0.3638 0.4665 -0.0482 0.1212  0.0666  67  ARG A O   
516  C CB  . ARG A 67  ? 0.8904 0.5034 0.5978 -0.0198 0.0808  0.1112  67  ARG A CB  
517  C CG  . ARG A 67  ? 0.9599 0.5557 0.6583 0.0011  0.0574  0.1297  67  ARG A CG  
518  C CD  . ARG A 67  ? 1.0463 0.6092 0.6863 -0.0007 0.0430  0.1501  67  ARG A CD  
519  N NE  . ARG A 67  ? 1.1275 0.6382 0.7148 -0.0207 0.0637  0.1565  67  ARG A NE  
520  C CZ  . ARG A 67  ? 1.1984 0.6599 0.7635 -0.0206 0.0714  0.1681  67  ARG A CZ  
521  N NH1 . ARG A 67  ? 1.1910 0.6481 0.7840 -0.0009 0.0608  0.1732  67  ARG A NH1 
522  N NH2 . ARG A 67  ? 1.2458 0.6589 0.7584 -0.0416 0.0922  0.1740  67  ARG A NH2 
523  N N   . LYS A 68  ? 0.7486 0.3648 0.5129 -0.0523 0.1364  0.0736  68  LYS A N   
524  C CA  . LYS A 68  ? 0.8130 0.4274 0.5827 -0.0748 0.1633  0.0599  68  LYS A CA  
525  C C   . LYS A 68  ? 0.8390 0.4194 0.5530 -0.0897 0.1753  0.0700  68  LYS A C   
526  O O   . LYS A 68  ? 0.8809 0.4181 0.5459 -0.0879 0.1697  0.0891  68  LYS A O   
527  C CB  . LYS A 68  ? 0.8494 0.4438 0.6371 -0.0845 0.1808  0.0523  68  LYS A CB  
528  C CG  . LYS A 68  ? 0.8343 0.4450 0.6522 -0.1053 0.2058  0.0325  68  LYS A CG  
529  C CD  . LYS A 68  ? 0.9032 0.5106 0.7564 -0.1123 0.2160  0.0201  68  LYS A CD  
530  C CE  . LYS A 68  ? 0.8922 0.5374 0.7976 -0.1259 0.2300  -0.0030 68  LYS A CE  
531  N NZ  . LYS A 68  ? 0.9437 0.5751 0.8368 -0.1480 0.2593  -0.0073 68  LYS A NZ  
532  N N   . LEU A 69  ? 0.7803 0.3782 0.5000 -0.1040 0.1915  0.0571  69  LEU A N   
533  C CA  . LEU A 69  ? 0.8427 0.4061 0.5084 -0.1227 0.2101  0.0621  69  LEU A CA  
534  C C   . LEU A 69  ? 0.8867 0.4331 0.5626 -0.1424 0.2421  0.0504  69  LEU A C   
535  O O   . LEU A 69  ? 0.8504 0.4272 0.5695 -0.1519 0.2598  0.0296  69  LEU A O   
536  C CB  . LEU A 69  ? 0.8015 0.3938 0.4685 -0.1259 0.2101  0.0527  69  LEU A CB  
537  C CG  . LEU A 69  ? 0.7674 0.3788 0.4247 -0.1072 0.1763  0.0631  69  LEU A CG  
538  C CD1 . LEU A 69  ? 0.7020 0.3542 0.3847 -0.1070 0.1745  0.0488  69  LEU A CD1 
539  C CD2 . LEU A 69  ? 0.8552 0.4227 0.4396 -0.1089 0.1647  0.0843  69  LEU A CD2 
540  N N   . LYS A 70  ? 0.9098 0.4168 0.5540 -0.1443 0.2439  0.0611  70  LYS A N   
541  C CA  . LYS A 70  ? 0.9608 0.4603 0.6257 -0.1580 0.2675  0.0480  70  LYS A CA  
542  C C   . LYS A 70  ? 0.9332 0.4351 0.5917 -0.1759 0.2932  0.0326  70  LYS A C   
543  O O   . LYS A 70  ? 0.9372 0.4455 0.6275 -0.1876 0.3149  0.0165  70  LYS A O   
544  C CB  . LYS A 70  ? 1.0347 0.4876 0.6631 -0.1553 0.2631  0.0647  70  LYS A CB  
545  C CG  . LYS A 70  ? 1.0904 0.5062 0.6508 -0.1473 0.2442  0.0889  70  LYS A CG  
546  C CD  . LYS A 70  ? 1.2702 0.6411 0.8028 -0.1428 0.2393  0.1050  70  LYS A CD  
547  C CE  . LYS A 70  ? 1.3153 0.6474 0.7794 -0.1374 0.2218  0.1282  70  LYS A CE  
548  N NZ  . LYS A 70  ? 1.2641 0.6104 0.7203 -0.1175 0.1890  0.1424  70  LYS A NZ  
549  N N   . LYS A 71  ? 0.9681 0.4656 0.5885 -0.1781 0.2911  0.0355  71  LYS A N   
550  C CA  . LYS A 71  ? 0.9564 0.4509 0.5676 -0.1945 0.3166  0.0195  71  LYS A CA  
551  C C   . LYS A 71  ? 0.9502 0.4929 0.6303 -0.1976 0.3312  -0.0056 71  LYS A C   
552  O O   . LYS A 71  ? 0.9179 0.4624 0.6139 -0.2104 0.3567  -0.0234 71  LYS A O   
553  C CB  . LYS A 71  ? 0.9958 0.4700 0.5451 -0.1958 0.3076  0.0289  71  LYS A CB  
554  C CG  . LYS A 71  ? 1.0502 0.5037 0.5697 -0.2136 0.3330  0.0162  71  LYS A CG  
555  C CD  . LYS A 71  ? 1.1015 0.5255 0.5487 -0.2145 0.3176  0.0303  71  LYS A CD  
556  C CE  . LYS A 71  ? 1.1591 0.5598 0.5725 -0.2328 0.3424  0.0169  71  LYS A CE  
557  N NZ  . LYS A 71  ? 1.3068 0.6551 0.6361 -0.2385 0.3328  0.0351  71  LYS A NZ  
558  N N   . TYR A 72  ? 0.8544 0.4352 0.5769 -0.1853 0.3151  -0.0074 72  TYR A N   
559  C CA  . TYR A 72  ? 0.8675 0.4951 0.6548 -0.1849 0.3230  -0.0288 72  TYR A CA  
560  C C   . TYR A 72  ? 0.8182 0.4753 0.6697 -0.1796 0.3177  -0.0360 72  TYR A C   
561  O O   . TYR A 72  ? 0.8534 0.4935 0.6977 -0.1765 0.3088  -0.0252 72  TYR A O   
562  C CB  . TYR A 72  ? 0.7707 0.4188 0.5541 -0.1762 0.3087  -0.0267 72  TYR A CB  
563  C CG  . TYR A 72  ? 0.8403 0.4560 0.5528 -0.1811 0.3072  -0.0170 72  TYR A CG  
564  C CD1 . TYR A 72  ? 0.8479 0.4439 0.5373 -0.1951 0.3296  -0.0283 72  TYR A CD1 
565  C CD2 . TYR A 72  ? 0.8658 0.4688 0.5338 -0.1720 0.2822  0.0031  72  TYR A CD2 
566  C CE1 . TYR A 72  ? 0.9022 0.4657 0.5238 -0.2012 0.3269  -0.0202 72  TYR A CE1 
567  C CE2 . TYR A 72  ? 0.8576 0.4318 0.4610 -0.1770 0.2770  0.0115  72  TYR A CE2 
568  C CZ  . TYR A 72  ? 0.9062 0.4601 0.4853 -0.1921 0.2990  -0.0002 72  TYR A CZ  
569  O OH  . TYR A 72  ? 0.9625 0.4860 0.4752 -0.1984 0.2925  0.0074  72  TYR A OH  
570  N N   . ASP A 73  ? 0.7451 0.4456 0.6599 -0.1779 0.3215  -0.0548 73  ASP A N   
571  C CA  . ASP A 73  ? 0.7576 0.4904 0.7385 -0.1747 0.3158  -0.0659 73  ASP A CA  
572  C C   . ASP A 73  ? 0.6852 0.4428 0.6877 -0.1610 0.2914  -0.0601 73  ASP A C   
573  O O   . ASP A 73  ? 0.6760 0.4614 0.7002 -0.1550 0.2870  -0.0660 73  ASP A O   
574  C CB  . ASP A 73  ? 0.8324 0.5963 0.8708 -0.1803 0.3323  -0.0897 73  ASP A CB  
575  C CG  . ASP A 73  ? 0.8487 0.6558 0.9617 -0.1744 0.3194  -0.1025 73  ASP A CG  
576  O OD1 . ASP A 73  ? 0.8600 0.6669 0.9786 -0.1705 0.3028  -0.0957 73  ASP A OD1 
577  O OD2 . ASP A 73  ? 0.8871 0.7266 1.0529 -0.1733 0.3247  -0.1201 73  ASP A OD2 
578  N N   . ASN A 74  ? 0.6757 0.4215 0.6702 -0.1540 0.2744  -0.0491 74  ASN A N   
579  C CA  . ASN A 74  ? 0.6806 0.4555 0.6921 -0.1318 0.2412  -0.0461 74  ASN A CA  
580  C C   . ASN A 74  ? 0.6230 0.4035 0.6040 -0.1196 0.2270  -0.0361 74  ASN A C   
581  O O   . ASN A 74  ? 0.6112 0.4257 0.6198 -0.1077 0.2116  -0.0414 74  ASN A O   
582  C CB  . ASN A 74  ? 0.6093 0.4288 0.6897 -0.1289 0.2344  -0.0647 74  ASN A CB  
583  C CG  . ASN A 74  ? 0.6499 0.4918 0.7423 -0.1089 0.2026  -0.0618 74  ASN A CG  
584  O OD1 . ASN A 74  ? 0.6708 0.4947 0.7315 -0.0991 0.1887  -0.0491 74  ASN A OD1 
585  N ND2 . ASN A 74  ? 0.6496 0.5296 0.7876 -0.1023 0.1914  -0.0734 74  ASN A ND2 
586  N N   . CYS A 75  ? 0.6171 0.3622 0.5388 -0.1229 0.2307  -0.0209 75  CYS A N   
587  C CA  . CYS A 75  ? 0.6355 0.3841 0.5257 -0.1123 0.2139  -0.0108 75  CYS A CA  
588  C C   . CYS A 75  ? 0.6708 0.4002 0.5265 -0.0987 0.1912  0.0083  75  CYS A C   
589  O O   . CYS A 75  ? 0.6750 0.3720 0.5097 -0.1017 0.1952  0.0171  75  CYS A O   
590  C CB  . CYS A 75  ? 0.6839 0.4103 0.5322 -0.1271 0.2334  -0.0102 75  CYS A CB  
591  S SG  . CYS A 75  ? 0.6743 0.4234 0.5653 -0.1415 0.2635  -0.0341 75  CYS A SG  
592  N N   . TRP A 76  ? 0.5936 0.3430 0.4467 -0.0837 0.1681  0.0142  76  TRP A N   
593  C CA  . TRP A 76  ? 0.6556 0.3993 0.4940 -0.0672 0.1444  0.0291  76  TRP A CA  
594  C C   . TRP A 76  ? 0.6501 0.3973 0.4587 -0.0613 0.1280  0.0391  76  TRP A C   
595  O O   . TRP A 76  ? 0.6352 0.4013 0.4483 -0.0657 0.1302  0.0312  76  TRP A O   
596  C CB  . TRP A 76  ? 0.6149 0.3901 0.4992 -0.0527 0.1308  0.0221  76  TRP A CB  
597  C CG  . TRP A 76  ? 0.6350 0.4095 0.5496 -0.0595 0.1434  0.0104  76  TRP A CG  
598  C CD1 . TRP A 76  ? 0.6054 0.4006 0.5562 -0.0691 0.1556  -0.0062 76  TRP A CD1 
599  C CD2 . TRP A 76  ? 0.6705 0.4215 0.5835 -0.0582 0.1446  0.0136  76  TRP A CD2 
600  N NE1 . TRP A 76  ? 0.6229 0.4118 0.5960 -0.0749 0.1629  -0.0140 76  TRP A NE1 
601  C CE2 . TRP A 76  ? 0.6644 0.4245 0.6128 -0.0690 0.1572  -0.0025 76  TRP A CE2 
602  C CE3 . TRP A 76  ? 0.6874 0.4104 0.5753 -0.0482 0.1356  0.0279  76  TRP A CE3 
603  C CZ2 . TRP A 76  ? 0.7144 0.4552 0.6704 -0.0723 0.1619  -0.0055 76  TRP A CZ2 
604  C CZ3 . TRP A 76  ? 0.7397 0.4412 0.6350 -0.0499 0.1416  0.0255  76  TRP A CZ3 
605  C CH2 . TRP A 76  ? 0.6942 0.4039 0.6215 -0.0630 0.1551  0.0085  76  TRP A CH2 
606  N N   . LEU A 77  ? 0.6554 0.3841 0.4359 -0.0511 0.1106  0.0560  77  LEU A N   
607  C CA  . LEU A 77  ? 0.6543 0.3880 0.4098 -0.0449 0.0903  0.0662  77  LEU A CA  
608  C C   . LEU A 77  ? 0.6743 0.4317 0.4567 -0.0239 0.0664  0.0720  77  LEU A C   
609  O O   . LEU A 77  ? 0.6770 0.4220 0.4668 -0.0132 0.0616  0.0788  77  LEU A O   
610  C CB  . LEU A 77  ? 0.6610 0.3501 0.3548 -0.0521 0.0883  0.0825  77  LEU A CB  
611  C CG  . LEU A 77  ? 0.7179 0.4089 0.3812 -0.0465 0.0627  0.0944  77  LEU A CG  
612  C CD1 . LEU A 77  ? 0.7134 0.4244 0.3721 -0.0579 0.0668  0.0825  77  LEU A CD1 
613  C CD2 . LEU A 77  ? 0.7850 0.4261 0.3843 -0.0507 0.0559  0.1139  77  LEU A CD2 
614  N N   . ALA A 78  ? 0.6346 0.4244 0.4320 -0.0189 0.0534  0.0685  78  ALA A N   
615  C CA  . ALA A 78  ? 0.6307 0.4454 0.4531 -0.0013 0.0325  0.0733  78  ALA A CA  
616  C C   . ALA A 78  ? 0.6575 0.4758 0.4561 -0.0005 0.0126  0.0828  78  ALA A C   
617  O O   . ALA A 78  ? 0.6652 0.4866 0.4451 -0.0134 0.0156  0.0776  78  ALA A O   
618  C CB  . ALA A 78  ? 0.5792 0.4316 0.4454 0.0027  0.0353  0.0594  78  ALA A CB  
619  N N   . LEU A 79  ? 0.6718 0.4904 0.4736 0.0147  -0.0081 0.0956  79  LEU A N   
620  C CA  . LEU A 79  ? 0.6745 0.5016 0.4619 0.0179  -0.0328 0.1051  79  LEU A CA  
621  C C   . LEU A 79  ? 0.6975 0.5674 0.5353 0.0328  -0.0466 0.1016  79  LEU A C   
622  O O   . LEU A 79  ? 0.7078 0.5842 0.5777 0.0479  -0.0458 0.1023  79  LEU A O   
623  C CB  . LEU A 79  ? 0.7505 0.5410 0.5009 0.0244  -0.0484 0.1247  79  LEU A CB  
624  C CG  . LEU A 79  ? 0.7831 0.5239 0.4754 0.0084  -0.0338 0.1306  79  LEU A CG  
625  C CD1 . LEU A 79  ? 0.8479 0.5499 0.5008 0.0168  -0.0532 0.1530  79  LEU A CD1 
626  C CD2 . LEU A 79  ? 0.7733 0.5125 0.4316 -0.0127 -0.0255 0.1222  79  LEU A CD2 
627  N N   . THR A 80  ? 0.6532 0.5506 0.4977 0.0276  -0.0575 0.0970  80  THR A N   
628  C CA  . THR A 80  ? 0.6084 0.5479 0.5026 0.0376  -0.0655 0.0912  80  THR A CA  
629  C C   . THR A 80  ? 0.6306 0.5855 0.5352 0.0482  -0.0946 0.1019  80  THR A C   
630  O O   . THR A 80  ? 0.6562 0.5901 0.5236 0.0459  -0.1126 0.1139  80  THR A O   
631  C CB  . THR A 80  ? 0.6268 0.5898 0.5310 0.0242  -0.0560 0.0769  80  THR A CB  
632  O OG1 . THR A 80  ? 0.5922 0.5559 0.4695 0.0121  -0.0699 0.0781  80  THR A OG1 
633  C CG2 . THR A 80  ? 0.6086 0.5554 0.5016 0.0138  -0.0308 0.0672  80  THR A CG2 
634  N N   . ASP A 81  ? 0.6303 0.6221 0.5868 0.0599  -0.0991 0.0973  81  ASP A N   
635  C CA  . ASP A 81  ? 0.6130 0.6342 0.5945 0.0668  -0.1253 0.1019  81  ASP A CA  
636  C C   . ASP A 81  ? 0.5808 0.6081 0.5353 0.0476  -0.1357 0.0981  81  ASP A C   
637  O O   . ASP A 81  ? 0.5769 0.6085 0.5257 0.0326  -0.1177 0.0856  81  ASP A O   
638  C CB  . ASP A 81  ? 0.6159 0.6785 0.6603 0.0769  -0.1188 0.0923  81  ASP A CB  
639  C CG  . ASP A 81  ? 0.6109 0.7077 0.6963 0.0882  -0.1447 0.0967  81  ASP A CG  
640  O OD1 . ASP A 81  ? 0.5969 0.7104 0.6771 0.0774  -0.1633 0.0963  81  ASP A OD1 
641  O OD2 . ASP A 81  ? 0.6235 0.7315 0.7497 0.1078  -0.1461 0.0994  81  ASP A OD2 
642  N N   . PRO A 82  ? 0.5745 0.5997 0.5096 0.0472  -0.1649 0.1084  82  PRO A N   
643  C CA  . PRO A 82  ? 0.6383 0.6652 0.5411 0.0267  -0.1746 0.1030  82  PRO A CA  
644  C C   . PRO A 82  ? 0.6184 0.6893 0.5645 0.0185  -0.1729 0.0880  82  PRO A C   
645  O O   . PRO A 82  ? 0.6525 0.7229 0.5734 -0.0006 -0.1749 0.0800  82  PRO A O   
646  C CB  . PRO A 82  ? 0.6753 0.6917 0.5515 0.0312  -0.2113 0.1188  82  PRO A CB  
647  C CG  . PRO A 82  ? 0.6692 0.6932 0.5855 0.0575  -0.2233 0.1309  82  PRO A CG  
648  C CD  . PRO A 82  ? 0.6419 0.6548 0.5748 0.0649  -0.1903 0.1260  82  PRO A CD  
649  N N   . ARG A 83  ? 0.5782 0.6839 0.5858 0.0311  -0.1671 0.0833  83  ARG A N   
650  C CA  . ARG A 83  ? 0.5520 0.6947 0.5985 0.0215  -0.1597 0.0689  83  ARG A CA  
651  C C   . ARG A 83  ? 0.5536 0.6866 0.5943 0.0122  -0.1266 0.0574  83  ARG A C   
652  O O   . ARG A 83  ? 0.5436 0.6981 0.6060 0.0016  -0.1176 0.0461  83  ARG A O   
653  C CB  . ARG A 83  ? 0.4922 0.6762 0.6071 0.0378  -0.1662 0.0684  83  ARG A CB  
654  C CG  . ARG A 83  ? 0.5422 0.7444 0.6743 0.0471  -0.2031 0.0782  83  ARG A CG  
655  C CD  . ARG A 83  ? 0.5676 0.8045 0.7699 0.0687  -0.2064 0.0792  83  ARG A CD  
656  N NE  . ARG A 83  ? 0.6050 0.8191 0.8085 0.0853  -0.1857 0.0832  83  ARG A NE  
657  C CZ  . ARG A 83  ? 0.6315 0.8657 0.8892 0.1054  -0.1813 0.0831  83  ARG A CZ  
658  N NH1 . ARG A 83  ? 0.6053 0.8854 0.9259 0.1129  -0.1957 0.0795  83  ARG A NH1 
659  N NH2 . ARG A 83  ? 0.5890 0.7970 0.8400 0.1177  -0.1611 0.0850  83  ARG A NH2 
660  N N   . ASP A 84  ? 0.5605 0.6607 0.5728 0.0152  -0.1096 0.0602  84  ASP A N   
661  C CA  . ASP A 84  ? 0.5473 0.6395 0.5599 0.0103  -0.0816 0.0508  84  ASP A CA  
662  C C   . ASP A 84  ? 0.5823 0.6388 0.5445 -0.0024 -0.0716 0.0496  84  ASP A C   
663  O O   . ASP A 84  ? 0.5711 0.6036 0.5181 0.0019  -0.0588 0.0523  84  ASP A O   
664  C CB  . ASP A 84  ? 0.4992 0.5907 0.5362 0.0268  -0.0691 0.0527  84  ASP A CB  
665  C CG  . ASP A 84  ? 0.5169 0.6075 0.5615 0.0230  -0.0451 0.0428  84  ASP A CG  
666  O OD1 . ASP A 84  ? 0.5290 0.6280 0.5739 0.0104  -0.0391 0.0349  84  ASP A OD1 
667  O OD2 . ASP A 84  ? 0.4707 0.5501 0.5194 0.0324  -0.0335 0.0431  84  ASP A OD2 
668  N N   . VAL A 85  ? 0.5474 0.6007 0.4854 -0.0190 -0.0758 0.0441  85  VAL A N   
669  C CA  . VAL A 85  ? 0.5401 0.5586 0.4276 -0.0317 -0.0673 0.0427  85  VAL A CA  
670  C C   . VAL A 85  ? 0.6224 0.6376 0.5035 -0.0472 -0.0498 0.0286  85  VAL A C   
671  O O   . VAL A 85  ? 0.6111 0.5986 0.4569 -0.0576 -0.0368 0.0243  85  VAL A O   
672  C CB  . VAL A 85  ? 0.6528 0.6569 0.4996 -0.0379 -0.0904 0.0510  85  VAL A CB  
673  C CG1 . VAL A 85  ? 0.6217 0.6223 0.4719 -0.0208 -0.1083 0.0670  85  VAL A CG1 
674  C CG2 . VAL A 85  ? 0.6039 0.6322 0.4586 -0.0485 -0.1087 0.0449  85  VAL A CG2 
675  N N   . ALA A 86  ? 0.5483 0.5890 0.4632 -0.0491 -0.0475 0.0209  86  ALA A N   
676  C CA  . ALA A 86  ? 0.6021 0.6364 0.5103 -0.0635 -0.0329 0.0083  86  ALA A CA  
677  C C   . ALA A 86  ? 0.5829 0.6415 0.5324 -0.0612 -0.0265 0.0032  86  ALA A C   
678  O O   . ALA A 86  ? 0.5515 0.6327 0.5333 -0.0500 -0.0320 0.0081  86  ALA A O   
679  C CB  . ALA A 86  ? 0.6312 0.6579 0.5071 -0.0808 -0.0443 0.0031  86  ALA A CB  
680  N N   . ARG A 87  ? 0.5906 0.6408 0.5371 -0.0722 -0.0128 -0.0070 87  ARG A N   
681  C CA  . ARG A 87  ? 0.5480 0.6148 0.5251 -0.0740 -0.0066 -0.0116 87  ARG A CA  
682  C C   . ARG A 87  ? 0.5419 0.6357 0.5365 -0.0813 -0.0232 -0.0128 87  ARG A C   
683  O O   . ARG A 87  ? 0.5674 0.6618 0.5433 -0.0899 -0.0396 -0.0135 87  ARG A O   
684  C CB  . ARG A 87  ? 0.5303 0.5772 0.4973 -0.0846 0.0100  -0.0215 87  ARG A CB  
685  C CG  . ARG A 87  ? 0.5580 0.5862 0.5246 -0.0752 0.0266  -0.0212 87  ARG A CG  
686  C CD  . ARG A 87  ? 0.5257 0.5350 0.4891 -0.0829 0.0416  -0.0304 87  ARG A CD  
687  N NE  . ARG A 87  ? 0.5879 0.5788 0.5237 -0.0964 0.0452  -0.0396 87  ARG A NE  
688  C CZ  . ARG A 87  ? 0.5745 0.5643 0.4996 -0.1120 0.0413  -0.0474 87  ARG A CZ  
689  N NH1 . ARG A 87  ? 0.5317 0.5406 0.4760 -0.1167 0.0336  -0.0469 87  ARG A NH1 
690  N NH2 . ARG A 87  ? 0.5853 0.5539 0.4798 -0.1245 0.0467  -0.0571 87  ARG A NH2 
691  N N   . ILE A 88  ? 0.5056 0.6216 0.5362 -0.0786 -0.0191 -0.0133 88  ILE A N   
692  C CA  . ILE A 88  ? 0.5070 0.6532 0.5656 -0.0870 -0.0309 -0.0168 88  ILE A CA  
693  C C   . ILE A 88  ? 0.5420 0.6858 0.6118 -0.0994 -0.0142 -0.0251 88  ILE A C   
694  O O   . ILE A 88  ? 0.4813 0.6314 0.5731 -0.0936 -0.0005 -0.0233 88  ILE A O   
695  C CB  . ILE A 88  ? 0.5261 0.7028 0.6231 -0.0726 -0.0384 -0.0101 88  ILE A CB  
696  C CG1 . ILE A 88  ? 0.5515 0.7206 0.6347 -0.0567 -0.0498 0.0001  88  ILE A CG1 
697  C CG2 . ILE A 88  ? 0.5107 0.7229 0.6413 -0.0814 -0.0546 -0.0145 88  ILE A CG2 
698  C CD1 . ILE A 88  ? 0.5750 0.7658 0.6949 -0.0390 -0.0508 0.0061  88  ILE A CD1 
699  N N   . GLU A 89  ? 0.5139 0.6452 0.5654 -0.1173 -0.0145 -0.0344 89  GLU A N   
700  C CA  . GLU A 89  ? 0.5317 0.6521 0.5889 -0.1293 0.0029  -0.0418 89  GLU A CA  
701  C C   . GLU A 89  ? 0.5342 0.6851 0.6320 -0.1355 0.0040  -0.0438 89  GLU A C   
702  O O   . GLU A 89  ? 0.5395 0.6821 0.6467 -0.1384 0.0226  -0.0445 89  GLU A O   
703  C CB  . GLU A 89  ? 0.5578 0.6561 0.5865 -0.1477 0.0028  -0.0530 89  GLU A CB  
704  C CG  . GLU A 89  ? 0.6156 0.6825 0.6059 -0.1422 0.0073  -0.0526 89  GLU A CG  
705  C CD  . GLU A 89  ? 0.6496 0.6896 0.6082 -0.1599 0.0118  -0.0655 89  GLU A CD  
706  O OE1 . GLU A 89  ? 0.6164 0.6597 0.5793 -0.1777 0.0098  -0.0753 89  GLU A OE1 
707  O OE2 . GLU A 89  ? 0.6633 0.6780 0.5929 -0.1566 0.0192  -0.0669 89  GLU A OE2 
708  N N   . SER A 90  ? 0.5158 0.7015 0.6388 -0.1373 -0.0154 -0.0444 90  SER A N   
709  C CA  . SER A 90  ? 0.5079 0.7283 0.6778 -0.1444 -0.0138 -0.0483 90  SER A CA  
710  C C   . SER A 90  ? 0.4889 0.7217 0.6857 -0.1286 0.0006  -0.0413 90  SER A C   
711  O O   . SER A 90  ? 0.5115 0.7672 0.7452 -0.1356 0.0107  -0.0455 90  SER A O   
712  C CB  . SER A 90  ? 0.4911 0.7485 0.6860 -0.1489 -0.0420 -0.0512 90  SER A CB  
713  O OG  . SER A 90  ? 0.5584 0.8197 0.7447 -0.1302 -0.0597 -0.0411 90  SER A OG  
714  N N   . LYS A 91  ? 0.4697 0.6874 0.6488 -0.1092 0.0029  -0.0321 91  LYS A N   
715  C CA  . LYS A 91  ? 0.4293 0.6516 0.6248 -0.0949 0.0179  -0.0267 91  LYS A CA  
716  C C   . LYS A 91  ? 0.4190 0.6036 0.5818 -0.0906 0.0366  -0.0229 91  LYS A C   
717  O O   . LYS A 91  ? 0.4363 0.6164 0.5994 -0.0774 0.0463  -0.0178 91  LYS A O   
718  C CB  . LYS A 91  ? 0.4680 0.7053 0.6745 -0.0754 0.0039  -0.0197 91  LYS A CB  
719  C CG  . LYS A 91  ? 0.4858 0.7647 0.7348 -0.0753 -0.0155 -0.0218 91  LYS A CG  
720  C CD  . LYS A 91  ? 0.4858 0.7734 0.7444 -0.0536 -0.0287 -0.0133 91  LYS A CD  
721  C CE  . LYS A 91  ? 0.4935 0.8256 0.8056 -0.0493 -0.0463 -0.0147 91  LYS A CE  
722  N NZ  . LYS A 91  ? 0.5897 0.9396 0.9095 -0.0680 -0.0650 -0.0213 91  LYS A NZ  
723  N N   . THR A 92  ? 0.4132 0.5700 0.5486 -0.1011 0.0409  -0.0260 92  THR A N   
724  C CA  . THR A 92  ? 0.4253 0.5470 0.5340 -0.0968 0.0554  -0.0224 92  THR A CA  
725  C C   . THR A 92  ? 0.4779 0.5881 0.5890 -0.1114 0.0716  -0.0257 92  THR A C   
726  O O   . THR A 92  ? 0.4725 0.5810 0.5850 -0.1280 0.0707  -0.0331 92  THR A O   
727  C CB  . THR A 92  ? 0.4692 0.5656 0.5484 -0.0959 0.0498  -0.0236 92  THR A CB  
728  O OG1 . THR A 92  ? 0.4379 0.5435 0.5129 -0.0853 0.0359  -0.0203 92  THR A OG1 
729  C CG2 . THR A 92  ? 0.4428 0.5066 0.5021 -0.0883 0.0617  -0.0198 92  THR A CG2 
730  N N   . VAL A 93  ? 0.4286 0.5282 0.5369 -0.1064 0.0867  -0.0203 93  VAL A N   
731  C CA  . VAL A 93  ? 0.4479 0.5368 0.5583 -0.1207 0.1042  -0.0217 93  VAL A CA  
732  C C   . VAL A 93  ? 0.4371 0.4849 0.5148 -0.1149 0.1157  -0.0136 93  VAL A C   
733  O O   . VAL A 93  ? 0.4201 0.4570 0.4818 -0.0987 0.1117  -0.0073 93  VAL A O   
734  C CB  . VAL A 93  ? 0.4704 0.5901 0.6127 -0.1246 0.1142  -0.0236 93  VAL A CB  
735  C CG1 . VAL A 93  ? 0.4580 0.6209 0.6392 -0.1301 0.0998  -0.0314 93  VAL A CG1 
736  C CG2 . VAL A 93  ? 0.4154 0.5351 0.5519 -0.1067 0.1187  -0.0171 93  VAL A CG2 
737  N N   . ILE A 94  ? 0.4875 0.5116 0.5558 -0.1291 0.1292  -0.0138 94  ILE A N   
738  C CA  . ILE A 94  ? 0.4918 0.4732 0.5279 -0.1255 0.1393  -0.0047 94  ILE A CA  
739  C C   . ILE A 94  ? 0.5198 0.4948 0.5552 -0.1392 0.1600  -0.0027 94  ILE A C   
740  O O   . ILE A 94  ? 0.5260 0.5129 0.5816 -0.1581 0.1686  -0.0101 94  ILE A O   
741  C CB  . ILE A 94  ? 0.4918 0.4395 0.5116 -0.1288 0.1370  -0.0054 94  ILE A CB  
742  C CG1 . ILE A 94  ? 0.5068 0.4599 0.5267 -0.1157 0.1206  -0.0084 94  ILE A CG1 
743  C CG2 . ILE A 94  ? 0.4999 0.4014 0.4885 -0.1246 0.1456  0.0056  94  ILE A CG2 
744  C CD1 . ILE A 94  ? 0.5861 0.5053 0.5925 -0.1158 0.1208  -0.0102 94  ILE A CD1 
745  N N   . ILE A 95  ? 0.5069 0.4626 0.5176 -0.1312 0.1685  0.0065  95  ILE A N   
746  C CA  . ILE A 95  ? 0.5505 0.4962 0.5529 -0.1437 0.1915  0.0091  95  ILE A CA  
747  C C   . ILE A 95  ? 0.6317 0.5213 0.5900 -0.1470 0.1994  0.0203  95  ILE A C   
748  O O   . ILE A 95  ? 0.6450 0.5064 0.5711 -0.1313 0.1892  0.0302  95  ILE A O   
749  C CB  . ILE A 95  ? 0.5974 0.5582 0.5979 -0.1338 0.1977  0.0106  95  ILE A CB  
750  C CG1 . ILE A 95  ? 0.5767 0.5922 0.6273 -0.1336 0.1953  -0.0005 95  ILE A CG1 
751  C CG2 . ILE A 95  ? 0.6625 0.5963 0.6358 -0.1456 0.2240  0.0157  95  ILE A CG2 
752  C CD1 . ILE A 95  ? 0.5070 0.5433 0.5693 -0.1158 0.1721  -0.0018 95  ILE A CD1 
753  N N   . THR A 96  ? 0.5956 0.4686 0.5540 -0.1675 0.2161  0.0189  96  THR A N   
754  C CA  . THR A 96  ? 0.6527 0.4685 0.5682 -0.1737 0.2276  0.0307  96  THR A CA  
755  C C   . THR A 96  ? 0.7153 0.5276 0.6313 -0.1957 0.2551  0.0288  96  THR A C   
756  O O   . THR A 96  ? 0.7036 0.5610 0.6630 -0.2059 0.2607  0.0155  96  THR A O   
757  C CB  . THR A 96  ? 0.6766 0.4641 0.5891 -0.1763 0.2198  0.0305  96  THR A CB  
758  O OG1 . THR A 96  ? 0.6865 0.5053 0.6387 -0.1933 0.2223  0.0153  96  THR A OG1 
759  C CG2 . THR A 96  ? 0.6793 0.4626 0.5872 -0.1526 0.1948  0.0333  96  THR A CG2 
760  N N   . GLN A 97  ? 0.8111 0.5745 0.6810 -0.1961 0.2634  0.0407  97  GLN A N   
761  C CA  . GLN A 97  ? 0.8218 0.5814 0.6905 -0.2113 0.2832  0.0372  97  GLN A CA  
762  C C   . GLN A 97  ? 0.8360 0.6099 0.7407 -0.2287 0.2872  0.0254  97  GLN A C   
763  O O   . GLN A 97  ? 0.8385 0.6476 0.7787 -0.2418 0.2986  0.0136  97  GLN A O   
764  C CB  . GLN A 97  ? 0.9575 0.6557 0.7646 -0.2089 0.2889  0.0533  97  GLN A CB  
765  C CG  . GLN A 97  ? 1.0811 0.7668 0.8792 -0.2257 0.3117  0.0508  97  GLN A CG  
766  C CD  . GLN A 97  ? 1.1750 0.8981 0.9925 -0.2297 0.3272  0.0413  97  GLN A CD  
767  O OE1 . GLN A 97  ? 1.1709 0.9178 0.9933 -0.2174 0.3211  0.0401  97  GLN A OE1 
768  N NE2 . GLN A 97  ? 1.1867 0.9141 1.0169 -0.2470 0.3485  0.0338  97  GLN A NE2 
769  N N   . GLU A 98  ? 0.8035 0.5514 0.7016 -0.2287 0.2770  0.0274  98  GLU A N   
770  C CA  . GLU A 98  ? 0.7482 0.5031 0.6737 -0.2451 0.2792  0.0156  98  GLU A CA  
771  C C   . GLU A 98  ? 0.7139 0.5022 0.6741 -0.2434 0.2620  0.0043  98  GLU A C   
772  O O   . GLU A 98  ? 0.6909 0.4665 0.6382 -0.2290 0.2489  0.0099  98  GLU A O   
773  C CB  . GLU A 98  ? 0.9024 0.5964 0.7909 -0.2477 0.2832  0.0247  98  GLU A CB  
774  C CG  . GLU A 98  ? 0.9817 0.6394 0.8323 -0.2523 0.3004  0.0356  98  GLU A CG  
775  C CD  . GLU A 98  ? 1.0621 0.7444 0.9396 -0.2734 0.3196  0.0235  98  GLU A CD  
776  O OE1 . GLU A 98  ? 1.0709 0.7686 0.9802 -0.2873 0.3198  0.0108  98  GLU A OE1 
777  O OE2 . GLU A 98  ? 1.1744 0.8602 1.0414 -0.2764 0.3344  0.0257  98  GLU A OE2 
778  N N   . GLN A 99  ? 0.6706 0.5005 0.6739 -0.2584 0.2614  -0.0117 99  GLN A N   
779  C CA  . GLN A 99  ? 0.6765 0.5386 0.7090 -0.2586 0.2436  -0.0233 99  GLN A CA  
780  C C   . GLN A 99  ? 0.6454 0.4665 0.6559 -0.2569 0.2365  -0.0232 99  GLN A C   
781  O O   . GLN A 99  ? 0.6317 0.4595 0.6451 -0.2485 0.2225  -0.0262 99  GLN A O   
782  C CB  . GLN A 99  ? 0.6562 0.5662 0.7353 -0.2761 0.2417  -0.0399 99  GLN A CB  
783  C CG  . GLN A 99  ? 0.6446 0.5872 0.7481 -0.2771 0.2203  -0.0517 99  GLN A CG  
784  C CD  . GLN A 99  ? 0.6706 0.6603 0.8190 -0.2938 0.2133  -0.0673 99  GLN A CD  
785  O OE1 . GLN A 99  ? 0.6819 0.6829 0.8491 -0.3050 0.2258  -0.0703 99  GLN A OE1 
786  N NE2 . GLN A 99  ? 0.7222 0.7391 0.8871 -0.2959 0.1924  -0.0775 99  GLN A NE2 
787  N N   . ARG A 100 ? 0.6939 0.4709 0.6825 -0.2643 0.2472  -0.0201 100 ARG A N   
788  C CA  . ARG A 100 ? 0.7152 0.4518 0.6869 -0.2625 0.2429  -0.0215 100 ARG A CA  
789  C C   . ARG A 100 ? 0.7089 0.4142 0.6550 -0.2403 0.2344  -0.0089 100 ARG A C   
790  O O   . ARG A 100 ? 0.7411 0.4271 0.6846 -0.2350 0.2274  -0.0137 100 ARG A O   
791  C CB  . ARG A 100 ? 0.7737 0.4673 0.7264 -0.2732 0.2577  -0.0185 100 ARG A CB  
792  C CG  . ARG A 100 ? 0.8420 0.5055 0.7905 -0.2777 0.2555  -0.0272 100 ARG A CG  
793  C CD  . ARG A 100 ? 0.9360 0.5530 0.8638 -0.2871 0.2708  -0.0224 100 ARG A CD  
794  N NE  . ARG A 100 ? 1.0355 0.6256 0.9619 -0.2913 0.2698  -0.0324 100 ARG A NE  
795  C CZ  . ARG A 100 ? 1.0478 0.6039 0.9643 -0.3036 0.2822  -0.0343 100 ARG A CZ  
796  N NH1 . ARG A 100 ? 1.1629 0.7061 1.0693 -0.3140 0.2970  -0.0267 100 ARG A NH1 
797  N NH2 . ARG A 100 ? 1.0676 0.6007 0.9835 -0.3061 0.2810  -0.0447 100 ARG A NH2 
798  N N   . ASP A 101 ? 0.7215 0.4216 0.6494 -0.2269 0.2349  0.0060  101 ASP A N   
799  C CA  . ASP A 101 ? 0.7188 0.3934 0.6268 -0.2055 0.2242  0.0174  101 ASP A CA  
800  C C   . ASP A 101 ? 0.6716 0.3915 0.6057 -0.1930 0.2051  0.0066  101 ASP A C   
801  O O   . ASP A 101 ? 0.6996 0.4061 0.6279 -0.1738 0.1921  0.0091  101 ASP A O   
802  C CB  . ASP A 101 ? 0.8075 0.4688 0.6862 -0.1927 0.2252  0.0350  101 ASP A CB  
803  C CG  . ASP A 101 ? 0.9075 0.5238 0.7520 -0.1968 0.2365  0.0470  101 ASP A CG  
804  O OD1 . ASP A 101 ? 0.9550 0.5425 0.7965 -0.2037 0.2408  0.0447  101 ASP A OD1 
805  O OD2 . ASP A 101 ? 0.9973 0.6064 0.8159 -0.1930 0.2410  0.0582  101 ASP A OD2 
806  N N   . THR A 102 ? 0.6599 0.4326 0.6237 -0.2030 0.2027  -0.0052 102 THR A N   
807  C CA  . THR A 102 ? 0.5919 0.4063 0.5756 -0.1913 0.1840  -0.0135 102 THR A CA  
808  C C   . THR A 102 ? 0.5983 0.4216 0.5968 -0.2041 0.1790  -0.0301 102 THR A C   
809  O O   . THR A 102 ? 0.6415 0.4674 0.6387 -0.1922 0.1668  -0.0346 102 THR A O   
810  C CB  . THR A 102 ? 0.5991 0.4644 0.6049 -0.1912 0.1811  -0.0150 102 THR A CB  
811  O OG1 . THR A 102 ? 0.6189 0.4751 0.6060 -0.1764 0.1839  -0.0013 102 THR A OG1 
812  C CG2 . THR A 102 ? 0.5291 0.4356 0.5550 -0.1822 0.1614  -0.0237 102 THR A CG2 
813  N N   . VAL A 103 ? 0.5751 0.4047 0.5875 -0.2295 0.1885  -0.0404 103 VAL A N   
814  C CA  . VAL A 103 ? 0.5900 0.4249 0.6120 -0.2457 0.1837  -0.0578 103 VAL A CA  
815  C C   . VAL A 103 ? 0.6330 0.4378 0.6501 -0.2641 0.1978  -0.0626 103 VAL A C   
816  O O   . VAL A 103 ? 0.6944 0.4930 0.7106 -0.2686 0.2096  -0.0551 103 VAL A O   
817  C CB  . VAL A 103 ? 0.5714 0.4648 0.6231 -0.2551 0.1696  -0.0691 103 VAL A CB  
818  C CG1 . VAL A 103 ? 0.5515 0.4723 0.6037 -0.2323 0.1517  -0.0645 103 VAL A CG1 
819  C CG2 . VAL A 103 ? 0.5960 0.5180 0.6743 -0.2692 0.1798  -0.0681 103 VAL A CG2 
820  N N   . PRO A 104 ? 0.6471 0.4344 0.6582 -0.2720 0.1956  -0.0757 104 PRO A N   
821  C CA  . PRO A 104 ? 0.6887 0.4585 0.6992 -0.2887 0.2050  -0.0829 104 PRO A CA  
822  C C   . PRO A 104 ? 0.6799 0.4981 0.7205 -0.3072 0.2012  -0.0918 104 PRO A C   
823  O O   . PRO A 104 ? 0.6462 0.5103 0.7076 -0.3095 0.1862  -0.0985 104 PRO A O   
824  C CB  . PRO A 104 ? 0.7079 0.4560 0.7067 -0.2922 0.2014  -0.0975 104 PRO A CB  
825  C CG  . PRO A 104 ? 0.6832 0.4242 0.6719 -0.2733 0.1947  -0.0942 104 PRO A CG  
826  C CD  . PRO A 104 ? 0.6379 0.4198 0.6410 -0.2667 0.1860  -0.0855 104 PRO A CD  
827  N N   . ILE A 105 ? 0.7131 0.5206 0.7577 -0.3199 0.2145  -0.0914 105 ILE A N   
828  C CA  . ILE A 105 ? 0.7119 0.5633 0.7904 -0.3384 0.2127  -0.1011 105 ILE A CA  
829  C C   . ILE A 105 ? 0.7258 0.5872 0.8119 -0.3548 0.2010  -0.1201 105 ILE A C   
830  O O   . ILE A 105 ? 0.7668 0.5892 0.8347 -0.3630 0.2095  -0.1259 105 ILE A O   
831  C CB  . ILE A 105 ? 0.7487 0.5822 0.8273 -0.3478 0.2333  -0.0951 105 ILE A CB  
832  C CG1 . ILE A 105 ? 0.7433 0.5610 0.8047 -0.3315 0.2444  -0.0759 105 ILE A CG1 
833  C CG2 . ILE A 105 ? 0.7489 0.6303 0.8692 -0.3671 0.2320  -0.1067 105 ILE A CG2 
834  C CD1 . ILE A 105 ? 0.7571 0.6209 0.8387 -0.3202 0.2349  -0.0722 105 ILE A CD1 
835  N N   . PRO A 106 ? 0.6978 0.6079 0.8077 -0.3598 0.1808  -0.1300 106 PRO A N   
836  C CA  . PRO A 106 ? 0.7163 0.6306 0.8234 -0.3743 0.1667  -0.1476 106 PRO A CA  
837  C C   . PRO A 106 ? 0.7547 0.6722 0.8794 -0.3970 0.1723  -0.1582 106 PRO A C   
838  O O   . PRO A 106 ? 0.7606 0.6905 0.9085 -0.4030 0.1841  -0.1535 106 PRO A O   
839  C CB  . PRO A 106 ? 0.6785 0.6463 0.8065 -0.3724 0.1412  -0.1520 106 PRO A CB  
840  C CG  . PRO A 106 ? 0.6380 0.6186 0.7714 -0.3529 0.1439  -0.1368 106 PRO A CG  
841  C CD  . PRO A 106 ? 0.6507 0.6094 0.7850 -0.3499 0.1680  -0.1249 106 PRO A CD  
842  N N   . LYS A 107 ? 0.7854 0.6893 0.8967 -0.4103 0.1651  -0.1734 107 LYS A N   
843  C CA  . LYS A 107 ? 0.8272 0.7305 0.9532 -0.4334 0.1701  -0.1851 107 LYS A CA  
844  C C   . LYS A 107 ? 0.8145 0.7799 0.9867 -0.4471 0.1511  -0.1930 107 LYS A C   
845  O O   . LYS A 107 ? 0.8350 0.8137 1.0361 -0.4622 0.1596  -0.1963 107 LYS A O   
846  C CB  . LYS A 107 ? 0.8687 0.7360 0.9643 -0.4434 0.1689  -0.1997 107 LYS A CB  
847  C CG  . LYS A 107 ? 0.9207 0.7677 1.0213 -0.4649 0.1820  -0.2093 107 LYS A CG  
848  C CD  . LYS A 107 ? 0.9643 0.7707 1.0318 -0.4728 0.1838  -0.2234 107 LYS A CD  
849  C CE  . LYS A 107 ? 1.0192 0.8014 1.0914 -0.4941 0.1992  -0.2322 107 LYS A CE  
850  N NZ  . LYS A 107 ? 1.1123 0.8582 1.1551 -0.5044 0.2007  -0.2486 107 LYS A NZ  
851  N N   . SER A 108 ? 0.7843 0.7880 0.9652 -0.4419 0.1249  -0.1961 108 SER A N   
852  C CA  . SER A 108 ? 0.7802 0.8412 1.0051 -0.4546 0.1012  -0.2049 108 SER A CA  
853  C C   . SER A 108 ? 0.7308 0.8403 0.9802 -0.4388 0.0816  -0.1968 108 SER A C   
854  O O   . SER A 108 ? 0.7143 0.8712 1.0133 -0.4399 0.0759  -0.1946 108 SER A O   
855  C CB  . SER A 108 ? 0.8162 0.8739 1.0253 -0.4712 0.0805  -0.2225 108 SER A CB  
856  O OG  . SER A 108 ? 0.8647 0.8936 1.0698 -0.4906 0.0959  -0.2324 108 SER A OG  
857  N N   . GLY A 109 ? 0.7099 0.8083 0.9268 -0.4240 0.0717  -0.1928 109 GLY A N   
858  C CA  . GLY A 109 ? 0.6689 0.8100 0.9038 -0.4098 0.0504  -0.1863 109 GLY A CA  
859  C C   . GLY A 109 ? 0.6291 0.7667 0.8645 -0.3888 0.0674  -0.1699 109 GLY A C   
860  O O   . GLY A 109 ? 0.6332 0.7421 0.8627 -0.3856 0.0951  -0.1621 109 GLY A O   
861  N N   . GLN A 110 ? 0.5944 0.7605 0.8348 -0.3743 0.0494  -0.1643 110 GLN A N   
862  C CA  . GLN A 110 ? 0.5570 0.7212 0.7950 -0.3540 0.0619  -0.1498 110 GLN A CA  
863  C C   . GLN A 110 ? 0.5602 0.6735 0.7442 -0.3461 0.0704  -0.1467 110 GLN A C   
864  O O   . GLN A 110 ? 0.6000 0.6932 0.7524 -0.3533 0.0596  -0.1563 110 GLN A O   
865  C CB  . GLN A 110 ? 0.5226 0.7417 0.7933 -0.3425 0.0375  -0.1462 110 GLN A CB  
866  C CG  . GLN A 110 ? 0.5381 0.7618 0.8049 -0.3212 0.0426  -0.1334 110 GLN A CG  
867  C CD  . GLN A 110 ? 0.5275 0.8075 0.8328 -0.3092 0.0166  -0.1307 110 GLN A CD  
868  O OE1 . GLN A 110 ? 0.5370 0.8569 0.8947 -0.3086 0.0174  -0.1308 110 GLN A OE1 
869  N NE2 . GLN A 110 ? 0.4544 0.7312 0.7298 -0.2942 -0.0073 -0.1257 110 GLN A NE2 
870  N N   . SER A 111 ? 0.5417 0.6324 0.7147 -0.3309 0.0904  -0.1337 111 SER A N   
871  C CA  . SER A 111 ? 0.5449 0.5880 0.6738 -0.3211 0.0991  -0.1298 111 SER A CA  
872  C C   . SER A 111 ? 0.5822 0.6386 0.6948 -0.3003 0.0788  -0.1243 111 SER A C   
873  O O   . SER A 111 ? 0.5404 0.6314 0.6730 -0.2839 0.0687  -0.1145 111 SER A O   
874  C CB  . SER A 111 ? 0.5402 0.5518 0.6604 -0.3079 0.1237  -0.1151 111 SER A CB  
875  O OG  . SER A 111 ? 0.5406 0.5123 0.6239 -0.2890 0.1267  -0.1083 111 SER A OG  
876  N N   . GLN A 112 ? 0.5664 0.5910 0.6409 -0.3001 0.0755  -0.1305 112 GLN A N   
877  C CA  . GLN A 112 ? 0.5255 0.5500 0.5756 -0.2807 0.0623  -0.1249 112 GLN A CA  
878  C C   . GLN A 112 ? 0.5985 0.5848 0.6258 -0.2601 0.0790  -0.1153 112 GLN A C   
879  O O   . GLN A 112 ? 0.6434 0.6206 0.6474 -0.2477 0.0733  -0.1139 112 GLN A O   
880  C CB  . GLN A 112 ? 0.5739 0.5887 0.5936 -0.2951 0.0483  -0.1395 112 GLN A CB  
881  C CG  . GLN A 112 ? 0.5995 0.6358 0.6301 -0.3224 0.0328  -0.1548 112 GLN A CG  
882  C CD  . GLN A 112 ? 0.6206 0.6359 0.6065 -0.3341 0.0211  -0.1682 112 GLN A CD  
883  O OE1 . GLN A 112 ? 0.6868 0.6750 0.6378 -0.3202 0.0268  -0.1649 112 GLN A OE1 
884  N NE2 . GLN A 112 ? 0.6538 0.6808 0.6396 -0.3568 0.0056  -0.1823 112 GLN A NE2 
885  N N   . LEU A 113 ? 0.6146 0.5767 0.6474 -0.2572 0.0991  -0.1091 113 LEU A N   
886  C CA  . LEU A 113 ? 0.5472 0.4715 0.5611 -0.2383 0.1123  -0.1007 113 LEU A CA  
887  C C   . LEU A 113 ? 0.5831 0.5196 0.6082 -0.2167 0.1135  -0.0833 113 LEU A C   
888  O O   . LEU A 113 ? 0.6190 0.5275 0.6327 -0.2004 0.1222  -0.0744 113 LEU A O   
889  C CB  . LEU A 113 ? 0.6560 0.5347 0.6608 -0.2492 0.1319  -0.1056 113 LEU A CB  
890  C CG  . LEU A 113 ? 0.6181 0.4771 0.6059 -0.2688 0.1326  -0.1249 113 LEU A CG  
891  C CD1 . LEU A 113 ? 0.6291 0.4461 0.6131 -0.2839 0.1517  -0.1313 113 LEU A CD1 
892  C CD2 . LEU A 113 ? 0.6338 0.4750 0.5988 -0.2545 0.1320  -0.1280 113 LEU A CD2 
893  N N   . GLY A 114 ? 0.6198 0.5976 0.6677 -0.2162 0.1042  -0.0791 114 GLY A N   
894  C CA  . GLY A 114 ? 0.5827 0.5745 0.6399 -0.1970 0.1050  -0.0649 114 GLY A CA  
895  C C   . GLY A 114 ? 0.5450 0.5788 0.6348 -0.2047 0.1016  -0.0652 114 GLY A C   
896  O O   . GLY A 114 ? 0.5264 0.5785 0.6343 -0.2250 0.0981  -0.0759 114 GLY A O   
897  N N   . ARG A 115 ? 0.5510 0.6006 0.6505 -0.1886 0.1028  -0.0547 115 ARG A N   
898  C CA  . ARG A 115 ? 0.5431 0.6310 0.6778 -0.1931 0.1048  -0.0548 115 ARG A CA  
899  C C   . ARG A 115 ? 0.4895 0.5603 0.6184 -0.1872 0.1253  -0.0451 115 ARG A C   
900  O O   . ARG A 115 ? 0.5129 0.5739 0.6258 -0.1677 0.1250  -0.0354 115 ARG A O   
901  C CB  . ARG A 115 ? 0.5371 0.6641 0.6905 -0.1792 0.0853  -0.0532 115 ARG A CB  
902  C CG  . ARG A 115 ? 0.5953 0.7552 0.7705 -0.1919 0.0653  -0.0635 115 ARG A CG  
903  C CD  . ARG A 115 ? 0.6809 0.8875 0.8935 -0.1809 0.0514  -0.0610 115 ARG A CD  
904  N NE  . ARG A 115 ? 0.7160 0.9430 0.9638 -0.1822 0.0691  -0.0604 115 ARG A NE  
905  C CZ  . ARG A 115 ? 0.6933 0.9617 0.9831 -0.1736 0.0637  -0.0600 115 ARG A CZ  
906  N NH1 . ARG A 115 ? 0.6219 0.9157 0.9243 -0.1618 0.0380  -0.0585 115 ARG A NH1 
907  N NH2 . ARG A 115 ? 0.6596 0.9419 0.9786 -0.1767 0.0856  -0.0612 115 ARG A NH2 
908  N N   . TRP A 116 ? 0.5224 0.5863 0.6605 -0.2055 0.1433  -0.0479 116 TRP A N   
909  C CA  . TRP A 116 ? 0.5562 0.5991 0.6825 -0.2042 0.1652  -0.0389 116 TRP A CA  
910  C C   . TRP A 116 ? 0.5494 0.6344 0.7116 -0.2043 0.1721  -0.0408 116 TRP A C   
911  O O   . TRP A 116 ? 0.5633 0.6895 0.7678 -0.2164 0.1672  -0.0514 116 TRP A O   
912  C CB  . TRP A 116 ? 0.5363 0.5439 0.6503 -0.2257 0.1848  -0.0404 116 TRP A CB  
913  C CG  . TRP A 116 ? 0.5656 0.5486 0.6626 -0.2281 0.2090  -0.0306 116 TRP A CG  
914  C CD1 . TRP A 116 ? 0.6013 0.5402 0.6551 -0.2142 0.2144  -0.0163 116 TRP A CD1 
915  C CD2 . TRP A 116 ? 0.5754 0.5748 0.6936 -0.2412 0.2263  -0.0341 116 TRP A CD2 
916  N NE1 . TRP A 116 ? 0.6069 0.5302 0.6482 -0.2221 0.2371  -0.0104 116 TRP A NE1 
917  C CE2 . TRP A 116 ? 0.5582 0.5186 0.6382 -0.2355 0.2432  -0.0216 116 TRP A CE2 
918  C CE3 . TRP A 116 ? 0.5478 0.5909 0.7122 -0.2540 0.2257  -0.0465 116 TRP A CE3 
919  C CZ2 . TRP A 116 ? 0.5802 0.5426 0.6643 -0.2432 0.2618  -0.0220 116 TRP A CZ2 
920  C CZ3 . TRP A 116 ? 0.5678 0.6149 0.7421 -0.2609 0.2449  -0.0468 116 TRP A CZ3 
921  C CH2 . TRP A 116 ? 0.5900 0.5959 0.7229 -0.2560 0.2639  -0.0351 116 TRP A CH2 
922  N N   . MET A 117 ? 0.5432 0.6178 0.6897 -0.1909 0.1831  -0.0315 117 MET A N   
923  C CA  . MET A 117 ? 0.5367 0.6434 0.7135 -0.1912 0.1968  -0.0339 117 MET A CA  
924  C C   . MET A 117 ? 0.5198 0.5898 0.6644 -0.1958 0.2244  -0.0261 117 MET A C   
925  O O   . MET A 117 ? 0.5759 0.6021 0.6721 -0.1854 0.2238  -0.0149 117 MET A O   
926  C CB  . MET A 117 ? 0.4964 0.6305 0.6852 -0.1678 0.1813  -0.0320 117 MET A CB  
927  C CG  . MET A 117 ? 0.5518 0.7219 0.7788 -0.1660 0.1953  -0.0367 117 MET A CG  
928  S SD  . MET A 117 ? 0.5664 0.7586 0.8022 -0.1373 0.1781  -0.0337 117 MET A SD  
929  C CE  . MET A 117 ? 0.5505 0.7705 0.8089 -0.1338 0.1432  -0.0372 117 MET A CE  
930  N N   . SER A 118 ? 0.5688 0.6540 0.7362 -0.2075 0.2433  -0.0313 118 SER A N   
931  C CA  . SER A 118 ? 0.6254 0.6703 0.7523 -0.2091 0.2648  -0.0234 118 SER A CA  
932  C C   . SER A 118 ? 0.6520 0.6908 0.7561 -0.1916 0.2695  -0.0170 118 SER A C   
933  O O   . SER A 118 ? 0.5888 0.6644 0.7224 -0.1792 0.2613  -0.0215 118 SER A O   
934  C CB  . SER A 118 ? 0.5901 0.6510 0.7443 -0.2236 0.2820  -0.0314 118 SER A CB  
935  O OG  . SER A 118 ? 0.6072 0.7088 0.7979 -0.2156 0.2876  -0.0379 118 SER A OG  
936  N N   . GLU A 119 ? 0.7034 0.6921 0.7514 -0.1904 0.2814  -0.0063 119 GLU A N   
937  C CA  . GLU A 119 ? 0.7566 0.7332 0.7744 -0.1758 0.2858  -0.0009 119 GLU A CA  
938  C C   . GLU A 119 ? 0.7346 0.7479 0.7873 -0.1738 0.2993  -0.0113 119 GLU A C   
939  O O   . GLU A 119 ? 0.6910 0.7192 0.7475 -0.1591 0.2970  -0.0130 119 GLU A O   
940  C CB  . GLU A 119 ? 0.8664 0.7806 0.8151 -0.1771 0.2938  0.0123  119 GLU A CB  
941  C CG  . GLU A 119 ? 0.9827 0.8787 0.8915 -0.1646 0.2978  0.0172  119 GLU A CG  
942  C CD  . GLU A 119 ? 1.0485 0.9404 0.9413 -0.1477 0.2786  0.0232  119 GLU A CD  
943  O OE1 . GLU A 119 ? 1.1298 0.9801 0.9787 -0.1411 0.2633  0.0353  119 GLU A OE1 
944  O OE2 . GLU A 119 ? 1.0044 0.9372 0.9340 -0.1350 0.2684  0.0147  119 GLU A OE2 
945  N N   . GLU A 120 ? 0.7189 0.7473 0.8000 -0.1882 0.3138  -0.0191 120 GLU A N   
946  C CA  . GLU A 120 ? 0.7514 0.8146 0.8706 -0.1864 0.3281  -0.0297 120 GLU A CA  
947  C C   . GLU A 120 ? 0.6593 0.7816 0.8435 -0.1757 0.3121  -0.0387 120 GLU A C   
948  O O   . GLU A 120 ? 0.6535 0.7989 0.8591 -0.1631 0.3163  -0.0439 120 GLU A O   
949  C CB  . GLU A 120 ? 0.7178 0.7820 0.8534 -0.2054 0.3480  -0.0361 120 GLU A CB  
950  C CG  . GLU A 120 ? 0.8950 0.9005 0.9661 -0.2151 0.3673  -0.0279 120 GLU A CG  
951  C CD  . GLU A 120 ? 0.9437 0.9106 0.9825 -0.2259 0.3610  -0.0190 120 GLU A CD  
952  O OE1 . GLU A 120 ? 0.8517 0.8207 0.8931 -0.2205 0.3395  -0.0149 120 GLU A OE1 
953  O OE2 . GLU A 120 ? 1.0553 0.9881 1.0663 -0.2400 0.3785  -0.0165 120 GLU A OE2 
954  N N   . ASP A 121 ? 0.6018 0.7469 0.8165 -0.1802 0.2928  -0.0407 121 ASP A N   
955  C CA  . ASP A 121 ? 0.5655 0.7640 0.8376 -0.1697 0.2733  -0.0477 121 ASP A CA  
956  C C   . ASP A 121 ? 0.5490 0.7438 0.8039 -0.1499 0.2608  -0.0424 121 ASP A C   
957  O O   . ASP A 121 ? 0.4920 0.7221 0.7846 -0.1352 0.2531  -0.0472 121 ASP A O   
958  C CB  . ASP A 121 ? 0.5216 0.7412 0.8234 -0.1818 0.2545  -0.0518 121 ASP A CB  
959  C CG  . ASP A 121 ? 0.5985 0.8294 0.9274 -0.2010 0.2655  -0.0593 121 ASP A CG  
960  O OD1 . ASP A 121 ? 0.6167 0.8598 0.9653 -0.2019 0.2842  -0.0641 121 ASP A OD1 
961  O OD2 . ASP A 121 ? 0.6226 0.8485 0.9525 -0.2158 0.2566  -0.0612 121 ASP A OD2 
962  N N   . PHE A 122 ? 0.5408 0.6920 0.7401 -0.1486 0.2583  -0.0325 122 PHE A N   
963  C CA  . PHE A 122 ? 0.5385 0.6801 0.7140 -0.1259 0.2388  -0.0265 122 PHE A CA  
964  C C   . PHE A 122 ? 0.5514 0.6896 0.7173 -0.1152 0.2560  -0.0281 122 PHE A C   
965  O O   . PHE A 122 ? 0.5756 0.7281 0.7522 -0.0965 0.2426  -0.0291 122 PHE A O   
966  C CB  . PHE A 122 ? 0.5337 0.6272 0.6512 -0.1227 0.2258  -0.0151 122 PHE A CB  
967  C CG  . PHE A 122 ? 0.5511 0.6341 0.6451 -0.1010 0.2074  -0.0100 122 PHE A CG  
968  C CD1 . PHE A 122 ? 0.4997 0.6106 0.6213 -0.0883 0.1841  -0.0123 122 PHE A CD1 
969  C CD2 . PHE A 122 ? 0.5387 0.5838 0.5827 -0.0945 0.2135  -0.0031 122 PHE A CD2 
970  C CE1 . PHE A 122 ? 0.4825 0.5839 0.5854 -0.0704 0.1696  -0.0084 122 PHE A CE1 
971  C CE2 . PHE A 122 ? 0.5057 0.5440 0.5330 -0.0763 0.1963  -0.0002 122 PHE A CE2 
972  C CZ  . PHE A 122 ? 0.5036 0.5702 0.5620 -0.0647 0.1758  -0.0032 122 PHE A CZ  
973  N N   . GLU A 123 ? 0.5577 0.6714 0.6973 -0.1258 0.2826  -0.0282 123 GLU A N   
974  C CA  . GLU A 123 ? 0.5878 0.6937 0.7125 -0.1164 0.2974  -0.0314 123 GLU A CA  
975  C C   . GLU A 123 ? 0.5422 0.6984 0.7316 -0.1056 0.2967  -0.0426 123 GLU A C   
976  O O   . GLU A 123 ? 0.5337 0.6931 0.7228 -0.0895 0.2962  -0.0451 123 GLU A O   
977  C CB  . GLU A 123 ? 0.7038 0.7773 0.7934 -0.1303 0.3208  -0.0308 123 GLU A CB  
978  C CG  . GLU A 123 ? 0.8290 0.8425 0.8399 -0.1333 0.3225  -0.0186 123 GLU A CG  
979  C CD  . GLU A 123 ? 0.9910 0.9727 0.9625 -0.1409 0.3457  -0.0197 123 GLU A CD  
980  O OE1 . GLU A 123 ? 1.0015 0.9997 1.0033 -0.1518 0.3640  -0.0280 123 GLU A OE1 
981  O OE2 . GLU A 123 ? 1.0820 1.0217 0.9915 -0.1365 0.3452  -0.0127 123 GLU A OE2 
982  N N   . LYS A 124 ? 0.5089 0.7036 0.7544 -0.1137 0.2953  -0.0493 124 LYS A N   
983  C CA  . LYS A 124 ? 0.5029 0.7461 0.8135 -0.1022 0.2914  -0.0586 124 LYS A CA  
984  C C   . LYS A 124 ? 0.4408 0.7081 0.7765 -0.0846 0.2652  -0.0569 124 LYS A C   
985  O O   . LYS A 124 ? 0.4700 0.7566 0.8334 -0.0670 0.2622  -0.0609 124 LYS A O   
986  C CB  . LYS A 124 ? 0.4583 0.7368 0.8223 -0.1159 0.2928  -0.0656 124 LYS A CB  
987  C CG  . LYS A 124 ? 0.6132 0.8666 0.9540 -0.1348 0.3202  -0.0678 124 LYS A CG  
988  C CD  . LYS A 124 ? 0.6211 0.9098 1.0167 -0.1497 0.3212  -0.0756 124 LYS A CD  
989  C CE  . LYS A 124 ? 0.7804 1.0438 1.1554 -0.1678 0.3516  -0.0789 124 LYS A CE  
990  N NZ  . LYS A 124 ? 0.8184 1.0235 1.1195 -0.1794 0.3591  -0.0686 124 LYS A NZ  
991  N N   . ALA A 125 ? 0.4599 0.7228 0.7845 -0.0889 0.2466  -0.0510 125 ALA A N   
992  C CA  . ALA A 125 ? 0.4035 0.6780 0.7362 -0.0706 0.2140  -0.0466 125 ALA A CA  
993  C C   . ALA A 125 ? 0.4553 0.6972 0.7429 -0.0533 0.2116  -0.0410 125 ALA A C   
994  O O   . ALA A 125 ? 0.4399 0.6957 0.7467 -0.0350 0.1982  -0.0413 125 ALA A O   
995  C CB  . ALA A 125 ? 0.4283 0.6940 0.7433 -0.0787 0.1893  -0.0405 125 ALA A CB  
996  N N   . PHE A 126 ? 0.4718 0.6687 0.6988 -0.0589 0.2223  -0.0356 126 PHE A N   
997  C CA  . PHE A 126 ? 0.4697 0.6351 0.6526 -0.0451 0.2194  -0.0316 126 PHE A CA  
998  C C   . PHE A 126 ? 0.5103 0.6876 0.7139 -0.0347 0.2378  -0.0405 126 PHE A C   
999  O O   . PHE A 126 ? 0.4760 0.6561 0.6855 -0.0174 0.2254  -0.0408 126 PHE A O   
1000 C CB  . PHE A 126 ? 0.4890 0.6068 0.6075 -0.0552 0.2291  -0.0251 126 PHE A CB  
1001 C CG  . PHE A 126 ? 0.5333 0.6179 0.6039 -0.0436 0.2240  -0.0216 126 PHE A CG  
1002 C CD1 . PHE A 126 ? 0.4760 0.5460 0.5254 -0.0346 0.1975  -0.0145 126 PHE A CD1 
1003 C CD2 . PHE A 126 ? 0.5881 0.6552 0.6342 -0.0434 0.2468  -0.0268 126 PHE A CD2 
1004 C CE1 . PHE A 126 ? 0.5466 0.5888 0.5563 -0.0255 0.1913  -0.0126 126 PHE A CE1 
1005 C CE2 . PHE A 126 ? 0.5614 0.5972 0.5613 -0.0344 0.2397  -0.0249 126 PHE A CE2 
1006 C CZ  . PHE A 126 ? 0.5513 0.5763 0.5353 -0.0256 0.2109  -0.0178 126 PHE A CZ  
1007 N N   . ASN A 127 ? 0.4619 0.6453 0.6784 -0.0458 0.2696  -0.0486 127 ASN A N   
1008 C CA  . ASN A 127 ? 0.5187 0.7064 0.7477 -0.0365 0.2868  -0.0577 127 ASN A CA  
1009 C C   . ASN A 127 ? 0.4849 0.7176 0.7835 -0.0204 0.2748  -0.0633 127 ASN A C   
1010 O O   . ASN A 127 ? 0.4585 0.6914 0.7667 -0.0073 0.2823  -0.0696 127 ASN A O   
1011 C CB  . ASN A 127 ? 0.5293 0.7081 0.7500 -0.0517 0.3118  -0.0627 127 ASN A CB  
1012 C CG  . ASN A 127 ? 0.6109 0.7367 0.7543 -0.0639 0.3243  -0.0568 127 ASN A CG  
1013 O OD1 . ASN A 127 ? 0.6347 0.7289 0.7290 -0.0574 0.3181  -0.0520 127 ASN A OD1 
1014 N ND2 . ASN A 127 ? 0.6764 0.7905 0.8080 -0.0816 0.3410  -0.0568 127 ASN A ND2 
1015 N N   . ALA A 128 ? 0.4452 0.7137 0.7906 -0.0214 0.2553  -0.0611 128 ALA A N   
1016 C CA  . ALA A 128 ? 0.4061 0.7145 0.8134 -0.0044 0.2376  -0.0638 128 ALA A CA  
1017 C C   . ALA A 128 ? 0.4225 0.7213 0.8175 0.0135  0.2116  -0.0562 128 ALA A C   
1018 O O   . ALA A 128 ? 0.4292 0.7529 0.8685 0.0305  0.1971  -0.0568 128 ALA A O   
1019 C CB  . ALA A 128 ? 0.3809 0.7307 0.8400 -0.0136 0.2224  -0.0644 128 ALA A CB  
1020 N N   . ARG A 129 ? 0.4307 0.6892 0.7613 0.0105  0.2013  -0.0476 129 ARG A N   
1021 C CA  . ARG A 129 ? 0.4137 0.6578 0.7241 0.0243  0.1736  -0.0392 129 ARG A CA  
1022 C C   . ARG A 129 ? 0.4642 0.6697 0.7275 0.0324  0.1807  -0.0393 129 ARG A C   
1023 O O   . ARG A 129 ? 0.4569 0.6600 0.7288 0.0487  0.1724  -0.0392 129 ARG A O   
1024 C CB  . ARG A 129 ? 0.4343 0.6687 0.7177 0.0140  0.1515  -0.0302 129 ARG A CB  
1025 C CG  . ARG A 129 ? 0.4153 0.6860 0.7419 0.0079  0.1355  -0.0298 129 ARG A CG  
1026 C CD  . ARG A 129 ? 0.3986 0.6554 0.6950 -0.0085 0.1257  -0.0252 129 ARG A CD  
1027 N NE  . ARG A 129 ? 0.3746 0.6615 0.7042 -0.0138 0.1050  -0.0251 129 ARG A NE  
1028 C CZ  . ARG A 129 ? 0.4222 0.7421 0.7954 -0.0256 0.1104  -0.0320 129 ARG A CZ  
1029 N NH1 . ARG A 129 ? 0.4379 0.7645 0.8276 -0.0342 0.1391  -0.0394 129 ARG A NH1 
1030 N NH2 . ARG A 129 ? 0.3787 0.7247 0.7783 -0.0301 0.0867  -0.0321 129 ARG A NH2 
1031 N N   . PHE A 130 ? 0.4526 0.6263 0.6655 0.0212  0.1946  -0.0393 130 PHE A N   
1032 C CA  . PHE A 130 ? 0.4778 0.6140 0.6403 0.0268  0.1910  -0.0375 130 PHE A CA  
1033 C C   . PHE A 130 ? 0.4855 0.6084 0.6406 0.0344  0.2121  -0.0475 130 PHE A C   
1034 O O   . PHE A 130 ? 0.4937 0.5957 0.6266 0.0439  0.2032  -0.0475 130 PHE A O   
1035 C CB  . PHE A 130 ? 0.4662 0.5711 0.5746 0.0134  0.1899  -0.0316 130 PHE A CB  
1036 C CG  . PHE A 130 ? 0.4857 0.5893 0.5876 0.0118  0.1639  -0.0222 130 PHE A CG  
1037 C CD1 . PHE A 130 ? 0.4598 0.5467 0.5411 0.0202  0.1453  -0.0183 130 PHE A CD1 
1038 C CD2 . PHE A 130 ? 0.4924 0.6123 0.6119 0.0013  0.1597  -0.0190 130 PHE A CD2 
1039 C CE1 . PHE A 130 ? 0.4418 0.5278 0.5195 0.0185  0.1251  -0.0113 130 PHE A CE1 
1040 C CE2 . PHE A 130 ? 0.4707 0.5876 0.5833 -0.0004 0.1382  -0.0123 130 PHE A CE2 
1041 C CZ  . PHE A 130 ? 0.4202 0.5201 0.5118 0.0085  0.1220  -0.0086 130 PHE A CZ  
1042 N N   . PRO A 131 ? 0.5147 0.6466 0.6859 0.0293  0.2422  -0.0573 131 PRO A N   
1043 C CA  . PRO A 131 ? 0.5038 0.6197 0.6652 0.0364  0.2648  -0.0689 131 PRO A CA  
1044 C C   . PRO A 131 ? 0.5015 0.6252 0.6941 0.0568  0.2536  -0.0716 131 PRO A C   
1045 O O   . PRO A 131 ? 0.4873 0.6460 0.7410 0.0676  0.2474  -0.0717 131 PRO A O   
1046 C CB  . PRO A 131 ? 0.4735 0.6091 0.6649 0.0283  0.2909  -0.0775 131 PRO A CB  
1047 C CG  . PRO A 131 ? 0.5205 0.6600 0.7022 0.0104  0.2921  -0.0709 131 PRO A CG  
1048 C CD  . PRO A 131 ? 0.4585 0.6090 0.6493 0.0139  0.2603  -0.0595 131 PRO A CD  
1049 N N   . GLY A 132 ? 0.5438 0.6331 0.6941 0.0618  0.2496  -0.0735 132 GLY A N   
1050 C CA  . GLY A 132 ? 0.4997 0.5866 0.6708 0.0797  0.2418  -0.0764 132 GLY A CA  
1051 C C   . GLY A 132 ? 0.4935 0.5914 0.6834 0.0885  0.2090  -0.0637 132 GLY A C   
1052 O O   . GLY A 132 ? 0.4677 0.5659 0.6820 0.1042  0.2020  -0.0640 132 GLY A O   
1053 N N   . CYS A 133 ? 0.4488 0.5515 0.6247 0.0787  0.1897  -0.0527 133 CYS A N   
1054 C CA  . CYS A 133 ? 0.4323 0.5481 0.6280 0.0852  0.1619  -0.0415 133 CYS A CA  
1055 C C   . CYS A 133 ? 0.4862 0.5739 0.6544 0.0915  0.1468  -0.0378 133 CYS A C   
1056 O O   . CYS A 133 ? 0.4921 0.5857 0.6765 0.0993  0.1277  -0.0295 133 CYS A O   
1057 C CB  . CYS A 133 ? 0.4251 0.5517 0.6125 0.0715  0.1492  -0.0332 133 CYS A CB  
1058 S SG  . CYS A 133 ? 0.4639 0.5555 0.5874 0.0580  0.1449  -0.0298 133 CYS A SG  
1059 N N   . MET A 134 ? 0.4552 0.5116 0.5809 0.0873  0.1546  -0.0439 134 MET A N   
1060 C CA  . MET A 134 ? 0.4497 0.4801 0.5518 0.0908  0.1420  -0.0425 134 MET A CA  
1061 C C   . MET A 134 ? 0.4859 0.4982 0.5911 0.1016  0.1548  -0.0527 134 MET A C   
1062 O O   . MET A 134 ? 0.4860 0.4708 0.5635 0.1006  0.1502  -0.0558 134 MET A O   
1063 C CB  . MET A 134 ? 0.4718 0.4800 0.5262 0.0778  0.1363  -0.0425 134 MET A CB  
1064 C CG  . MET A 134 ? 0.3928 0.4121 0.4410 0.0678  0.1228  -0.0327 134 MET A CG  
1065 S SD  . MET A 134 ? 0.4441 0.4360 0.4441 0.0575  0.1122  -0.0327 134 MET A SD  
1066 C CE  . MET A 134 ? 0.4203 0.4276 0.4261 0.0494  0.1000  -0.0217 134 MET A CE  
1067 N N   . LYS A 135 ? 0.4869 0.5138 0.6274 0.1113  0.1716  -0.0591 135 LYS A N   
1068 C CA  . LYS A 135 ? 0.4980 0.5051 0.6427 0.1223  0.1868  -0.0705 135 LYS A CA  
1069 C C   . LYS A 135 ? 0.5172 0.5075 0.6652 0.1322  0.1693  -0.0639 135 LYS A C   
1070 O O   . LYS A 135 ? 0.5329 0.5384 0.7046 0.1383  0.1504  -0.0509 135 LYS A O   
1071 C CB  . LYS A 135 ? 0.5555 0.5866 0.7508 0.1340  0.2066  -0.0776 135 LYS A CB  
1072 C CG  . LYS A 135 ? 0.6290 0.6608 0.8102 0.1232  0.2359  -0.0907 135 LYS A CG  
1073 C CD  . LYS A 135 ? 0.6338 0.6969 0.8669 0.1293  0.2496  -0.0958 135 LYS A CD  
1074 C CE  . LYS A 135 ? 0.6864 0.7541 0.8995 0.1116  0.2710  -0.1024 135 LYS A CE  
1075 N NZ  . LYS A 135 ? 0.6840 0.7834 0.9460 0.1133  0.2840  -0.1074 135 LYS A NZ  
1076 N N   . GLY A 136 ? 0.5667 0.5225 0.6854 0.1315  0.1753  -0.0731 136 GLY A N   
1077 C CA  . GLY A 136 ? 0.5325 0.4656 0.6492 0.1381  0.1626  -0.0686 136 GLY A CA  
1078 C C   . GLY A 136 ? 0.5394 0.4674 0.6334 0.1275  0.1403  -0.0575 136 GLY A C   
1079 O O   . GLY A 136 ? 0.5386 0.4476 0.6314 0.1313  0.1311  -0.0526 136 GLY A O   
1080 N N   . ARG A 137 ? 0.4971 0.4397 0.5742 0.1145  0.1329  -0.0535 137 ARG A N   
1081 C CA  . ARG A 137 ? 0.5066 0.4466 0.5668 0.1047  0.1143  -0.0446 137 ARG A CA  
1082 C C   . ARG A 137 ? 0.4997 0.4244 0.5224 0.0907  0.1130  -0.0524 137 ARG A C   
1083 O O   . ARG A 137 ? 0.5467 0.4629 0.5495 0.0869  0.1249  -0.0629 137 ARG A O   
1084 C CB  . ARG A 137 ? 0.4882 0.4572 0.5636 0.1021  0.1035  -0.0326 137 ARG A CB  
1085 C CG  . ARG A 137 ? 0.5595 0.5464 0.6717 0.1150  0.0989  -0.0239 137 ARG A CG  
1086 C CD  . ARG A 137 ? 0.5234 0.5308 0.6420 0.1099  0.0828  -0.0118 137 ARG A CD  
1087 N NE  . ARG A 137 ? 0.5168 0.5415 0.6688 0.1220  0.0745  -0.0035 137 ARG A NE  
1088 C CZ  . ARG A 137 ? 0.5473 0.5612 0.6999 0.1282  0.0602  0.0072  137 ARG A CZ  
1089 N NH1 . ARG A 137 ? 0.5891 0.5761 0.7126 0.1219  0.0556  0.0103  137 ARG A NH1 
1090 N NH2 . ARG A 137 ? 0.5021 0.5322 0.6851 0.1405  0.0498  0.0151  137 ARG A NH2 
1091 N N   . THR A 138 ? 0.4655 0.3863 0.4784 0.0828  0.0981  -0.0471 138 THR A N   
1092 C CA  . THR A 138 ? 0.4906 0.4026 0.4757 0.0705  0.0912  -0.0525 138 THR A CA  
1093 C C   . THR A 138 ? 0.4844 0.4161 0.4669 0.0647  0.0847  -0.0450 138 THR A C   
1094 O O   . THR A 138 ? 0.4448 0.3935 0.4457 0.0660  0.0789  -0.0350 138 THR A O   
1095 C CB  . THR A 138 ? 0.4927 0.3921 0.4762 0.0649  0.0802  -0.0526 138 THR A CB  
1096 O OG1 . THR A 138 ? 0.5540 0.4299 0.5365 0.0685  0.0872  -0.0605 138 THR A OG1 
1097 C CG2 . THR A 138 ? 0.5031 0.3993 0.4665 0.0534  0.0695  -0.0580 138 THR A CG2 
1098 N N   . MET A 139 ? 0.4704 0.3965 0.4268 0.0580  0.0856  -0.0498 139 MET A N   
1099 C CA  . MET A 139 ? 0.4716 0.4091 0.4215 0.0518  0.0776  -0.0425 139 MET A CA  
1100 C C   . MET A 139 ? 0.4649 0.3952 0.4054 0.0454  0.0606  -0.0430 139 MET A C   
1101 O O   . MET A 139 ? 0.4951 0.4089 0.4118 0.0411  0.0556  -0.0509 139 MET A O   
1102 C CB  . MET A 139 ? 0.4925 0.4247 0.4171 0.0480  0.0876  -0.0450 139 MET A CB  
1103 C CG  . MET A 139 ? 0.4929 0.4268 0.4025 0.0410  0.0770  -0.0375 139 MET A CG  
1104 S SD  . MET A 139 ? 0.5504 0.4668 0.4170 0.0343  0.0885  -0.0392 139 MET A SD  
1105 C CE  . MET A 139 ? 0.5016 0.4409 0.3973 0.0362  0.1095  -0.0359 139 MET A CE  
1106 N N   . TYR A 140 ? 0.4251 0.3681 0.3851 0.0443  0.0519  -0.0357 140 TYR A N   
1107 C CA  . TYR A 140 ? 0.3761 0.3179 0.3375 0.0388  0.0376  -0.0365 140 TYR A CA  
1108 C C   . TYR A 140 ? 0.4413 0.3860 0.3910 0.0360  0.0301  -0.0318 140 TYR A C   
1109 O O   . TYR A 140 ? 0.3901 0.3437 0.3422 0.0367  0.0357  -0.0248 140 TYR A O   
1110 C CB  . TYR A 140 ? 0.3531 0.3043 0.3398 0.0382  0.0357  -0.0320 140 TYR A CB  
1111 C CG  . TYR A 140 ? 0.4340 0.3768 0.4290 0.0407  0.0418  -0.0342 140 TYR A CG  
1112 C CD1 . TYR A 140 ? 0.4413 0.3717 0.4374 0.0362  0.0386  -0.0421 140 TYR A CD1 
1113 C CD2 . TYR A 140 ? 0.4155 0.3618 0.4184 0.0474  0.0498  -0.0283 140 TYR A CD2 
1114 C CE1 . TYR A 140 ? 0.4800 0.3974 0.4811 0.0378  0.0454  -0.0433 140 TYR A CE1 
1115 C CE2 . TYR A 140 ? 0.4555 0.3893 0.4639 0.0512  0.0542  -0.0285 140 TYR A CE2 
1116 C CZ  . TYR A 140 ? 0.4872 0.4044 0.4928 0.0461  0.0531  -0.0357 140 TYR A CZ  
1117 O OH  . TYR A 140 ? 0.5809 0.4807 0.5898 0.0492  0.0586  -0.0352 140 TYR A OH  
1118 N N   . VAL A 141 ? 0.4069 0.3433 0.3449 0.0327  0.0162  -0.0356 141 VAL A N   
1119 C CA  . VAL A 141 ? 0.3970 0.3309 0.3217 0.0315  0.0055  -0.0301 141 VAL A CA  
1120 C C   . VAL A 141 ? 0.4327 0.3775 0.3857 0.0312  -0.0073 -0.0293 141 VAL A C   
1121 O O   . VAL A 141 ? 0.4220 0.3663 0.3840 0.0292  -0.0191 -0.0363 141 VAL A O   
1122 C CB  . VAL A 141 ? 0.4383 0.3522 0.3251 0.0291  -0.0033 -0.0344 141 VAL A CB  
1123 C CG1 . VAL A 141 ? 0.4693 0.3761 0.3395 0.0291  -0.0174 -0.0262 141 VAL A CG1 
1124 C CG2 . VAL A 141 ? 0.4330 0.3349 0.2927 0.0286  0.0147  -0.0379 141 VAL A CG2 
1125 N N   . ILE A 142 ? 0.4096 0.3643 0.3781 0.0322  -0.0043 -0.0220 142 ILE A N   
1126 C CA  . ILE A 142 ? 0.3654 0.3310 0.3646 0.0320  -0.0105 -0.0224 142 ILE A CA  
1127 C C   . ILE A 142 ? 0.3930 0.3543 0.3893 0.0347  -0.0239 -0.0176 142 ILE A C   
1128 O O   . ILE A 142 ? 0.4172 0.3750 0.4047 0.0355  -0.0187 -0.0100 142 ILE A O   
1129 C CB  . ILE A 142 ? 0.3496 0.3256 0.3656 0.0308  0.0029  -0.0189 142 ILE A CB  
1130 C CG1 . ILE A 142 ? 0.3638 0.3410 0.3792 0.0301  0.0141  -0.0204 142 ILE A CG1 
1131 C CG2 . ILE A 142 ? 0.3807 0.3652 0.4260 0.0293  0.0007  -0.0216 142 ILE A CG2 
1132 C CD1 . ILE A 142 ? 0.3530 0.3385 0.3765 0.0290  0.0238  -0.0150 142 ILE A CD1 
1133 N N   . PRO A 143 ? 0.3866 0.3477 0.3922 0.0363  -0.0420 -0.0216 143 PRO A N   
1134 C CA  . PRO A 143 ? 0.3993 0.3570 0.4101 0.0413  -0.0567 -0.0159 143 PRO A CA  
1135 C C   . PRO A 143 ? 0.4318 0.4051 0.4869 0.0429  -0.0526 -0.0182 143 PRO A C   
1136 O O   . PRO A 143 ? 0.4117 0.3989 0.4980 0.0404  -0.0524 -0.0272 143 PRO A O   
1137 C CB  . PRO A 143 ? 0.4449 0.3975 0.4489 0.0426  -0.0806 -0.0202 143 PRO A CB  
1138 C CG  . PRO A 143 ? 0.4530 0.4095 0.4568 0.0363  -0.0755 -0.0312 143 PRO A CG  
1139 C CD  . PRO A 143 ? 0.4318 0.3960 0.4471 0.0334  -0.0510 -0.0318 143 PRO A CD  
1140 N N   . PHE A 144 ? 0.3914 0.3613 0.4496 0.0455  -0.0469 -0.0115 144 PHE A N   
1141 C CA  . PHE A 144 ? 0.3994 0.3819 0.4970 0.0459  -0.0388 -0.0159 144 PHE A CA  
1142 C C   . PHE A 144 ? 0.4090 0.3836 0.5164 0.0532  -0.0464 -0.0103 144 PHE A C   
1143 O O   . PHE A 144 ? 0.4035 0.3600 0.4804 0.0558  -0.0518 -0.0005 144 PHE A O   
1144 C CB  . PHE A 144 ? 0.3716 0.3582 0.4668 0.0390  -0.0164 -0.0168 144 PHE A CB  
1145 C CG  . PHE A 144 ? 0.3847 0.3608 0.4530 0.0376  -0.0085 -0.0085 144 PHE A CG  
1146 C CD1 . PHE A 144 ? 0.4157 0.3864 0.4533 0.0352  -0.0054 -0.0043 144 PHE A CD1 
1147 C CD2 . PHE A 144 ? 0.4252 0.3968 0.5016 0.0377  -0.0025 -0.0063 144 PHE A CD2 
1148 C CE1 . PHE A 144 ? 0.3832 0.3476 0.4022 0.0323  0.0033  0.0019  144 PHE A CE1 
1149 C CE2 . PHE A 144 ? 0.4336 0.3958 0.4876 0.0341  0.0052  0.0001  144 PHE A CE2 
1150 C CZ  . PHE A 144 ? 0.4435 0.4036 0.4703 0.0310  0.0080  0.0043  144 PHE A CZ  
1151 N N   . SER A 145 ? 0.3782 0.3644 0.5289 0.0562  -0.0449 -0.0170 145 SER A N   
1152 C CA  . SER A 145 ? 0.4048 0.3839 0.5744 0.0647  -0.0501 -0.0136 145 SER A CA  
1153 C C   . SER A 145 ? 0.4151 0.3959 0.5997 0.0601  -0.0264 -0.0183 145 SER A C   
1154 O O   . SER A 145 ? 0.3769 0.3716 0.5803 0.0532  -0.0115 -0.0280 145 SER A O   
1155 C CB  . SER A 145 ? 0.4412 0.4337 0.6561 0.0737  -0.0692 -0.0193 145 SER A CB  
1156 O OG  . SER A 145 ? 0.5740 0.5591 0.8127 0.0845  -0.0745 -0.0160 145 SER A OG  
1157 N N   . MET A 146 ? 0.4611 0.4242 0.6326 0.0624  -0.0222 -0.0117 146 MET A N   
1158 C CA  . MET A 146 ? 0.4325 0.3935 0.6197 0.0586  -0.0021 -0.0178 146 MET A CA  
1159 C C   . MET A 146 ? 0.4869 0.4463 0.7160 0.0706  -0.0086 -0.0211 146 MET A C   
1160 O O   . MET A 146 ? 0.4852 0.4274 0.7086 0.0806  -0.0237 -0.0115 146 MET A O   
1161 C CB  . MET A 146 ? 0.4904 0.4331 0.6418 0.0521  0.0081  -0.0108 146 MET A CB  
1162 C CG  . MET A 146 ? 0.4623 0.4097 0.5795 0.0418  0.0138  -0.0078 146 MET A CG  
1163 S SD  . MET A 146 ? 0.4291 0.3973 0.5566 0.0333  0.0260  -0.0180 146 MET A SD  
1164 C CE  . MET A 146 ? 0.4389 0.4026 0.5710 0.0243  0.0469  -0.0259 146 MET A CE  
1165 N N   . GLY A 147 ? 0.4879 0.4638 0.7596 0.0699  0.0032  -0.0344 147 GLY A N   
1166 C CA  . GLY A 147 ? 0.4797 0.4605 0.8033 0.0825  -0.0023 -0.0402 147 GLY A CA  
1167 C C   . GLY A 147 ? 0.5421 0.5462 0.9018 0.0887  -0.0215 -0.0443 147 GLY A C   
1168 O O   . GLY A 147 ? 0.5198 0.5289 0.8551 0.0849  -0.0351 -0.0398 147 GLY A O   
1169 N N   . PRO A 148 ? 0.5838 0.6031 1.0051 0.0978  -0.0222 -0.0544 148 PRO A N   
1170 C CA  . PRO A 148 ? 0.6182 0.6648 1.0837 0.1020  -0.0402 -0.0611 148 PRO A CA  
1171 C C   . PRO A 148 ? 0.7090 0.7501 1.1497 0.1098  -0.0768 -0.0480 148 PRO A C   
1172 O O   . PRO A 148 ? 0.7654 0.7843 1.1845 0.1209  -0.0943 -0.0345 148 PRO A O   
1173 C CB  . PRO A 148 ? 0.5845 0.6444 1.1227 0.1145  -0.0371 -0.0717 148 PRO A CB  
1174 C CG  . PRO A 148 ? 0.5567 0.6008 1.0875 0.1089  -0.0034 -0.0776 148 PRO A CG  
1175 C CD  . PRO A 148 ? 0.5541 0.5679 1.0114 0.1033  -0.0035 -0.0627 148 PRO A CD  
1176 N N   . LEU A 149 ? 0.8374 0.8954 1.2773 0.1026  -0.0871 -0.0523 149 LEU A N   
1177 C CA  . LEU A 149 ? 0.8507 0.9015 1.2577 0.1063  -0.1196 -0.0421 149 LEU A CA  
1178 C C   . LEU A 149 ? 0.9472 0.9998 1.3878 0.1243  -0.1530 -0.0370 149 LEU A C   
1179 O O   . LEU A 149 ? 0.9488 1.0240 1.4593 0.1328  -0.1550 -0.0471 149 LEU A O   
1180 C CB  . LEU A 149 ? 0.8887 0.9586 1.2986 0.0945  -0.1226 -0.0517 149 LEU A CB  
1181 C CG  . LEU A 149 ? 0.8675 0.9326 1.2478 0.0959  -0.1560 -0.0460 149 LEU A CG  
1182 C CD1 . LEU A 149 ? 0.8811 0.9131 1.1834 0.0941  -0.1570 -0.0308 149 LEU A CD1 
1183 C CD2 . LEU A 149 ? 0.8095 0.8942 1.2030 0.0829  -0.1542 -0.0593 149 LEU A CD2 
1184 N N   . GLY A 150 ? 0.9372 0.9645 1.3273 0.1305  -0.1792 -0.0210 150 GLY A N   
1185 C CA  . GLY A 150 ? 0.9110 0.9326 1.3203 0.1484  -0.2153 -0.0122 150 GLY A CA  
1186 C C   . GLY A 150 ? 0.9591 0.9654 1.3914 0.1627  -0.2098 -0.0058 150 GLY A C   
1187 O O   . GLY A 150 ? 1.0002 0.9908 1.4227 0.1736  -0.2342 0.0059  150 GLY A O   
1188 N N   . SER A 151 ? 0.9386 0.9459 1.3893 0.1584  -0.1738 -0.0137 151 SER A N   
1189 C CA  . SER A 151 ? 0.9318 0.9197 1.3933 0.1679  -0.1633 -0.0090 151 SER A CA  
1190 C C   . SER A 151 ? 0.9809 0.9236 1.3790 0.1741  -0.1766 0.0124  151 SER A C   
1191 O O   . SER A 151 ? 0.9631 0.8912 1.2963 0.1610  -0.1722 0.0196  151 SER A O   
1192 C CB  . SER A 151 ? 0.8443 0.8370 1.3261 0.1592  -0.1215 -0.0226 151 SER A CB  
1193 O OG  . SER A 151 ? 0.8537 0.8243 1.3402 0.1665  -0.1099 -0.0193 151 SER A OG  
1194 N N   . PRO A 152 ? 1.0498 0.9708 1.4487 0.1861  -0.1848 0.0224  152 PRO A N   
1195 C CA  . PRO A 152 ? 1.0792 0.9520 1.4140 0.1898  -0.1936 0.0435  152 PRO A CA  
1196 C C   . PRO A 152 ? 1.0943 0.9448 1.3955 0.1775  -0.1598 0.0435  152 PRO A C   
1197 O O   . PRO A 152 ? 1.1545 0.9725 1.3888 0.1701  -0.1594 0.0579  152 PRO A O   
1198 C CB  . PRO A 152 ? 1.0942 0.9537 1.4487 0.2053  -0.2058 0.0511  152 PRO A CB  
1199 C CG  . PRO A 152 ? 1.0885 0.9915 1.5089 0.2105  -0.2175 0.0372  152 PRO A CG  
1200 C CD  . PRO A 152 ? 1.0459 0.9841 1.5015 0.1972  -0.1911 0.0164  152 PRO A CD  
1201 N N   . LEU A 153 ? 0.9259 0.7946 1.2648 0.1709  -0.1282 0.0266  153 LEU A N   
1202 C CA  . LEU A 153 ? 0.8901 0.7417 1.1949 0.1556  -0.0950 0.0242  153 LEU A CA  
1203 C C   . LEU A 153 ? 0.8023 0.6726 1.0740 0.1351  -0.0786 0.0179  153 LEU A C   
1204 O O   . LEU A 153 ? 0.6817 0.5418 0.9235 0.1211  -0.0543 0.0161  153 LEU A O   
1205 C CB  . LEU A 153 ? 0.7939 0.6500 1.1497 0.1585  -0.0697 0.0090  153 LEU A CB  
1206 C CG  . LEU A 153 ? 0.8863 0.7398 1.2888 0.1790  -0.0860 0.0107  153 LEU A CG  
1207 C CD1 . LEU A 153 ? 0.7890 0.6552 1.2363 0.1770  -0.0568 -0.0079 153 LEU A CD1 
1208 C CD2 . LEU A 153 ? 0.9897 0.7979 1.3527 0.1892  -0.1029 0.0318  153 LEU A CD2 
1209 N N   . ALA A 154 ? 0.7810 0.6777 1.0589 0.1331  -0.0923 0.0142  154 ALA A N   
1210 C CA  . ALA A 154 ? 0.6780 0.5887 0.9240 0.1159  -0.0788 0.0096  154 ALA A CA  
1211 C C   . ALA A 154 ? 0.6526 0.5375 0.8309 0.1089  -0.0825 0.0243  154 ALA A C   
1212 O O   . ALA A 154 ? 0.6743 0.5335 0.8265 0.1171  -0.1024 0.0386  154 ALA A O   
1213 C CB  . ALA A 154 ? 0.6864 0.6277 0.9571 0.1156  -0.0924 0.0014  154 ALA A CB  
1214 N N   . LYS A 155 ? 0.5956 0.4865 0.7458 0.0935  -0.0624 0.0208  155 LYS A N   
1215 C CA  . LYS A 155 ? 0.5278 0.4018 0.6209 0.0848  -0.0611 0.0311  155 LYS A CA  
1216 C C   . LYS A 155 ? 0.5405 0.4366 0.6236 0.0767  -0.0598 0.0248  155 LYS A C   
1217 O O   . LYS A 155 ? 0.5115 0.4308 0.6193 0.0710  -0.0464 0.0132  155 LYS A O   
1218 C CB  . LYS A 155 ? 0.4917 0.3518 0.5645 0.0741  -0.0375 0.0325  155 LYS A CB  
1219 C CG  . LYS A 155 ? 0.5867 0.4184 0.6651 0.0804  -0.0359 0.0385  155 LYS A CG  
1220 C CD  . LYS A 155 ? 0.6088 0.4051 0.6461 0.0851  -0.0507 0.0561  155 LYS A CD  
1221 C CE  . LYS A 155 ? 0.7247 0.4876 0.7673 0.0922  -0.0490 0.0630  155 LYS A CE  
1222 N NZ  . LYS A 155 ? 0.8092 0.5716 0.8951 0.1120  -0.0687 0.0631  155 LYS A NZ  
1223 N N   . ILE A 156 ? 0.5013 0.3864 0.5452 0.0759  -0.0728 0.0324  156 ILE A N   
1224 C CA  . ILE A 156 ? 0.5016 0.4026 0.5344 0.0699  -0.0737 0.0262  156 ILE A CA  
1225 C C   . ILE A 156 ? 0.5228 0.4162 0.5147 0.0590  -0.0559 0.0295  156 ILE A C   
1226 O O   . ILE A 156 ? 0.5254 0.3950 0.4837 0.0567  -0.0522 0.0395  156 ILE A O   
1227 C CB  . ILE A 156 ? 0.5155 0.4105 0.5360 0.0765  -0.1020 0.0293  156 ILE A CB  
1228 C CG1 . ILE A 156 ? 0.5241 0.4394 0.6002 0.0859  -0.1184 0.0216  156 ILE A CG1 
1229 C CG2 . ILE A 156 ? 0.5061 0.4058 0.4981 0.0686  -0.1010 0.0246  156 ILE A CG2 
1230 C CD1 . ILE A 156 ? 0.5861 0.4950 0.6567 0.0945  -0.1527 0.0259  156 ILE A CD1 
1231 N N   . GLY A 157 ? 0.4672 0.3803 0.4648 0.0521  -0.0437 0.0209  157 GLY A N   
1232 C CA  . GLY A 157 ? 0.4854 0.3960 0.4524 0.0438  -0.0288 0.0224  157 GLY A CA  
1233 C C   . GLY A 157 ? 0.4671 0.3867 0.4258 0.0423  -0.0315 0.0160  157 GLY A C   
1234 O O   . GLY A 157 ? 0.4231 0.3531 0.4023 0.0455  -0.0431 0.0094  157 GLY A O   
1235 N N   . ILE A 158 ? 0.4906 0.4050 0.4204 0.0368  -0.0196 0.0172  158 ILE A N   
1236 C CA  . ILE A 158 ? 0.4449 0.3663 0.3674 0.0349  -0.0160 0.0099  158 ILE A CA  
1237 C C   . ILE A 158 ? 0.4396 0.3746 0.3709 0.0305  0.0043  0.0082  158 ILE A C   
1238 O O   . ILE A 158 ? 0.4893 0.4189 0.4059 0.0264  0.0159  0.0129  158 ILE A O   
1239 C CB  . ILE A 158 ? 0.4914 0.3912 0.3690 0.0334  -0.0204 0.0118  158 ILE A CB  
1240 C CG1 . ILE A 158 ? 0.5516 0.4342 0.4135 0.0379  -0.0449 0.0165  158 ILE A CG1 
1241 C CG2 . ILE A 158 ? 0.4880 0.3931 0.3601 0.0316  -0.0148 0.0020  158 ILE A CG2 
1242 C CD1 . ILE A 158 ? 0.5417 0.4349 0.4238 0.0411  -0.0633 0.0081  158 ILE A CD1 
1243 N N   . GLU A 159 ? 0.3924 0.3442 0.3481 0.0308  0.0081  0.0018  159 GLU A N   
1244 C CA  . GLU A 159 ? 0.3491 0.3131 0.3119 0.0284  0.0231  0.0009  159 GLU A CA  
1245 C C   . GLU A 159 ? 0.4157 0.3793 0.3705 0.0301  0.0275  -0.0045 159 GLU A C   
1246 O O   . GLU A 159 ? 0.4253 0.3879 0.3857 0.0319  0.0209  -0.0100 159 GLU A O   
1247 C CB  . GLU A 159 ? 0.3614 0.3401 0.3516 0.0272  0.0258  -0.0004 159 GLU A CB  
1248 C CG  . GLU A 159 ? 0.3459 0.3368 0.3421 0.0260  0.0363  -0.0001 159 GLU A CG  
1249 C CD  . GLU A 159 ? 0.3996 0.4009 0.4125 0.0228  0.0381  0.0005  159 GLU A CD  
1250 O OE1 . GLU A 159 ? 0.4163 0.4145 0.4350 0.0203  0.0356  0.0001  159 GLU A OE1 
1251 O OE2 . GLU A 159 ? 0.3563 0.3674 0.3753 0.0229  0.0417  0.0013  159 GLU A OE2 
1252 N N   . LEU A 160 ? 0.3930 0.3571 0.3372 0.0290  0.0403  -0.0039 160 LEU A N   
1253 C CA  . LEU A 160 ? 0.4185 0.3841 0.3619 0.0318  0.0489  -0.0097 160 LEU A CA  
1254 C C   . LEU A 160 ? 0.4081 0.3928 0.3802 0.0341  0.0549  -0.0086 160 LEU A C   
1255 O O   . LEU A 160 ? 0.4061 0.4026 0.3889 0.0313  0.0590  -0.0043 160 LEU A O   
1256 C CB  . LEU A 160 ? 0.4181 0.3738 0.3369 0.0296  0.0619  -0.0110 160 LEU A CB  
1257 C CG  . LEU A 160 ? 0.4569 0.3897 0.3380 0.0255  0.0564  -0.0084 160 LEU A CG  
1258 C CD1 . LEU A 160 ? 0.4882 0.4083 0.3405 0.0213  0.0744  -0.0106 160 LEU A CD1 
1259 C CD2 . LEU A 160 ? 0.4629 0.3830 0.3311 0.0274  0.0387  -0.0124 160 LEU A CD2 
1260 N N   . THR A 161 ? 0.3831 0.3687 0.3657 0.0387  0.0541  -0.0122 161 THR A N   
1261 C CA  . THR A 161 ? 0.3700 0.3695 0.3753 0.0421  0.0565  -0.0093 161 THR A CA  
1262 C C   . THR A 161 ? 0.3888 0.3817 0.3978 0.0490  0.0603  -0.0137 161 THR A C   
1263 O O   . THR A 161 ? 0.3867 0.3640 0.3823 0.0490  0.0593  -0.0198 161 THR A O   
1264 C CB  . THR A 161 ? 0.3611 0.3645 0.3761 0.0389  0.0482  -0.0055 161 THR A CB  
1265 O OG1 . THR A 161 ? 0.3705 0.3823 0.3995 0.0422  0.0482  -0.0018 161 THR A OG1 
1266 C CG2 . THR A 161 ? 0.3442 0.3353 0.3557 0.0378  0.0420  -0.0095 161 THR A CG2 
1267 N N   . ASP A 162 ? 0.3844 0.3883 0.4124 0.0550  0.0637  -0.0108 162 ASP A N   
1268 C CA  . ASP A 162 ? 0.3694 0.3642 0.4038 0.0634  0.0669  -0.0135 162 ASP A CA  
1269 C C   . ASP A 162 ? 0.4096 0.4005 0.4516 0.0653  0.0586  -0.0073 162 ASP A C   
1270 O O   . ASP A 162 ? 0.4205 0.4027 0.4698 0.0734  0.0601  -0.0065 162 ASP A O   
1271 C CB  . ASP A 162 ? 0.3922 0.3982 0.4444 0.0717  0.0775  -0.0153 162 ASP A CB  
1272 C CG  . ASP A 162 ? 0.3721 0.4038 0.4477 0.0722  0.0743  -0.0086 162 ASP A CG  
1273 O OD1 . ASP A 162 ? 0.3514 0.3887 0.4253 0.0663  0.0637  -0.0022 162 ASP A OD1 
1274 O OD2 . ASP A 162 ? 0.4437 0.4904 0.5409 0.0779  0.0832  -0.0110 162 ASP A OD2 
1275 N N   . SER A 163 ? 0.4388 0.4318 0.4764 0.0577  0.0512  -0.0031 163 SER A N   
1276 C CA  . SER A 163 ? 0.4056 0.3922 0.4438 0.0569  0.0456  0.0032  163 SER A CA  
1277 C C   . SER A 163 ? 0.3682 0.3394 0.3967 0.0494  0.0453  -0.0006 163 SER A C   
1278 O O   . SER A 163 ? 0.3899 0.3661 0.4164 0.0422  0.0437  -0.0033 163 SER A O   
1279 C CB  . SER A 163 ? 0.4186 0.4203 0.4599 0.0526  0.0399  0.0098  163 SER A CB  
1280 O OG  . SER A 163 ? 0.4337 0.4242 0.4652 0.0477  0.0362  0.0143  163 SER A OG  
1281 N N   . PRO A 164 ? 0.4110 0.3637 0.4366 0.0506  0.0472  -0.0011 164 PRO A N   
1282 C CA  . PRO A 164 ? 0.4113 0.3522 0.4335 0.0411  0.0484  -0.0054 164 PRO A CA  
1283 C C   . PRO A 164 ? 0.4302 0.3743 0.4502 0.0331  0.0481  -0.0008 164 PRO A C   
1284 O O   . PRO A 164 ? 0.3945 0.3382 0.4189 0.0247  0.0503  -0.0065 164 PRO A O   
1285 C CB  . PRO A 164 ? 0.4192 0.3368 0.4379 0.0438  0.0526  -0.0055 164 PRO A CB  
1286 C CG  . PRO A 164 ? 0.4929 0.4099 0.5130 0.0556  0.0512  0.0030  164 PRO A CG  
1287 C CD  . PRO A 164 ? 0.4152 0.3558 0.4435 0.0606  0.0495  0.0016  164 PRO A CD  
1288 N N   . TYR A 165 ? 0.4156 0.3632 0.4299 0.0353  0.0452  0.0084  165 TYR A N   
1289 C CA  . TYR A 165 ? 0.4040 0.3522 0.4100 0.0263  0.0459  0.0114  165 TYR A CA  
1290 C C   . TYR A 165 ? 0.4192 0.3836 0.4333 0.0214  0.0461  0.0055  165 TYR A C   
1291 O O   . TYR A 165 ? 0.3889 0.3512 0.4032 0.0128  0.0511  0.0018  165 TYR A O   
1292 C CB  . TYR A 165 ? 0.4384 0.3877 0.4339 0.0297  0.0389  0.0220  165 TYR A CB  
1293 C CG  . TYR A 165 ? 0.4825 0.4325 0.4639 0.0195  0.0387  0.0239  165 TYR A CG  
1294 C CD1 . TYR A 165 ? 0.4401 0.3682 0.3994 0.0112  0.0437  0.0274  165 TYR A CD1 
1295 C CD2 . TYR A 165 ? 0.4309 0.3999 0.4178 0.0169  0.0354  0.0216  165 TYR A CD2 
1296 C CE1 . TYR A 165 ? 0.4829 0.4082 0.4244 0.0007  0.0457  0.0275  165 TYR A CE1 
1297 C CE2 . TYR A 165 ? 0.4627 0.4295 0.4347 0.0067  0.0363  0.0214  165 TYR A CE2 
1298 C CZ  . TYR A 165 ? 0.4877 0.4326 0.4361 -0.0013 0.0416  0.0239  165 TYR A CZ  
1299 O OH  . TYR A 165 ? 0.4783 0.4176 0.4069 -0.0126 0.0447  0.0222  165 TYR A OH  
1300 N N   . VAL A 166 ? 0.3709 0.3498 0.3920 0.0266  0.0422  0.0045  166 VAL A N   
1301 C CA  . VAL A 166 ? 0.3311 0.3201 0.3575 0.0229  0.0419  0.0003  166 VAL A CA  
1302 C C   . VAL A 166 ? 0.3546 0.3389 0.3887 0.0208  0.0426  -0.0072 166 VAL A C   
1303 O O   . VAL A 166 ? 0.3439 0.3306 0.3857 0.0161  0.0437  -0.0108 166 VAL A O   
1304 C CB  . VAL A 166 ? 0.3760 0.3768 0.4043 0.0278  0.0397  0.0017  166 VAL A CB  
1305 C CG1 . VAL A 166 ? 0.3649 0.3691 0.3941 0.0249  0.0392  -0.0014 166 VAL A CG1 
1306 C CG2 . VAL A 166 ? 0.3766 0.3878 0.4054 0.0282  0.0375  0.0076  166 VAL A CG2 
1307 N N   . VAL A 167 ? 0.3357 0.3132 0.3702 0.0243  0.0415  -0.0106 167 VAL A N   
1308 C CA  . VAL A 167 ? 0.3542 0.3293 0.3979 0.0214  0.0386  -0.0188 167 VAL A CA  
1309 C C   . VAL A 167 ? 0.3680 0.3409 0.4245 0.0135  0.0441  -0.0224 167 VAL A C   
1310 O O   . VAL A 167 ? 0.3802 0.3602 0.4532 0.0106  0.0422  -0.0279 167 VAL A O   
1311 C CB  . VAL A 167 ? 0.3466 0.3118 0.3855 0.0243  0.0371  -0.0234 167 VAL A CB  
1312 C CG1 . VAL A 167 ? 0.3543 0.3189 0.4041 0.0197  0.0307  -0.0330 167 VAL A CG1 
1313 C CG2 . VAL A 167 ? 0.3774 0.3436 0.4031 0.0312  0.0360  -0.0217 167 VAL A CG2 
1314 N N   . ALA A 168 ? 0.3705 0.3319 0.4198 0.0101  0.0518  -0.0193 168 ALA A N   
1315 C CA  . ALA A 168 ? 0.3781 0.3336 0.4360 0.0003  0.0614  -0.0234 168 ALA A CA  
1316 C C   . ALA A 168 ? 0.3727 0.3363 0.4351 -0.0039 0.0661  -0.0240 168 ALA A C   
1317 O O   . ALA A 168 ? 0.3642 0.3319 0.4468 -0.0100 0.0726  -0.0321 168 ALA A O   
1318 C CB  . ALA A 168 ? 0.3825 0.3179 0.4224 -0.0029 0.0692  -0.0172 168 ALA A CB  
1319 N N   . SER A 169 ? 0.3460 0.3120 0.3923 -0.0013 0.0637  -0.0169 169 SER A N   
1320 C CA  . SER A 169 ? 0.3673 0.3371 0.4140 -0.0064 0.0690  -0.0187 169 SER A CA  
1321 C C   . SER A 169 ? 0.3908 0.3733 0.4594 -0.0028 0.0644  -0.0244 169 SER A C   
1322 O O   . SER A 169 ? 0.3632 0.3475 0.4452 -0.0069 0.0716  -0.0304 169 SER A O   
1323 C CB  . SER A 169 ? 0.4065 0.3761 0.4309 -0.0057 0.0652  -0.0105 169 SER A CB  
1324 O OG  . SER A 169 ? 0.4264 0.3834 0.4303 -0.0066 0.0651  -0.0032 169 SER A OG  
1325 N N   . MET A 170 ? 0.2977 0.2862 0.3681 0.0051  0.0529  -0.0224 170 MET A N   
1326 C CA  . MET A 170 ? 0.3062 0.3018 0.3921 0.0093  0.0456  -0.0255 170 MET A CA  
1327 C C   . MET A 170 ? 0.3105 0.3104 0.4247 0.0083  0.0444  -0.0344 170 MET A C   
1328 O O   . MET A 170 ? 0.3168 0.3225 0.4515 0.0111  0.0407  -0.0380 170 MET A O   
1329 C CB  . MET A 170 ? 0.3065 0.3025 0.3796 0.0162  0.0347  -0.0210 170 MET A CB  
1330 C CG  . MET A 170 ? 0.3324 0.3292 0.3876 0.0171  0.0362  -0.0138 170 MET A CG  
1331 S SD  . MET A 170 ? 0.4124 0.4094 0.4709 0.0152  0.0377  -0.0128 170 MET A SD  
1332 C CE  . MET A 170 ? 0.3507 0.3431 0.4093 0.0221  0.0258  -0.0114 170 MET A CE  
1333 N N   . ARG A 171 ? 0.3387 0.3360 0.4574 0.0046  0.0471  -0.0382 171 ARG A N   
1334 C CA  . ARG A 171 ? 0.3311 0.3355 0.4824 0.0012  0.0471  -0.0483 171 ARG A CA  
1335 C C   . ARG A 171 ? 0.3199 0.3275 0.4918 -0.0051 0.0626  -0.0543 171 ARG A C   
1336 O O   . ARG A 171 ? 0.3418 0.3614 0.5510 -0.0048 0.0618  -0.0632 171 ARG A O   
1337 C CB  . ARG A 171 ? 0.3541 0.3516 0.5033 -0.0040 0.0494  -0.0516 171 ARG A CB  
1338 C CG  . ARG A 171 ? 0.4031 0.4108 0.5907 -0.0097 0.0489  -0.0638 171 ARG A CG  
1339 C CD  . ARG A 171 ? 0.4110 0.4089 0.5959 -0.0169 0.0518  -0.0682 171 ARG A CD  
1340 N NE  . ARG A 171 ? 0.4095 0.4215 0.6335 -0.0215 0.0444  -0.0808 171 ARG A NE  
1341 C CZ  . ARG A 171 ? 0.4605 0.4822 0.7216 -0.0309 0.0568  -0.0907 171 ARG A CZ  
1342 N NH1 . ARG A 171 ? 0.4928 0.5066 0.7504 -0.0381 0.0799  -0.0894 171 ARG A NH1 
1343 N NH2 . ARG A 171 ? 0.4307 0.4706 0.7337 -0.0338 0.0459  -0.1028 171 ARG A NH2 
1344 N N   . ILE A 172 ? 0.3336 0.3303 0.4822 -0.0107 0.0766  -0.0502 172 ILE A N   
1345 C CA  . ILE A 172 ? 0.3552 0.3505 0.5159 -0.0183 0.0946  -0.0571 172 ILE A CA  
1346 C C   . ILE A 172 ? 0.3541 0.3538 0.5207 -0.0131 0.0928  -0.0575 172 ILE A C   
1347 O O   . ILE A 172 ? 0.3516 0.3575 0.5494 -0.0135 0.1011  -0.0667 172 ILE A O   
1348 C CB  . ILE A 172 ? 0.3978 0.3745 0.5234 -0.0285 0.1098  -0.0528 172 ILE A CB  
1349 C CG1 . ILE A 172 ? 0.3881 0.3555 0.5110 -0.0347 0.1150  -0.0530 172 ILE A CG1 
1350 C CG2 . ILE A 172 ? 0.3956 0.3662 0.5230 -0.0379 0.1305  -0.0603 172 ILE A CG2 
1351 C CD1 . ILE A 172 ? 0.4374 0.3818 0.5170 -0.0410 0.1225  -0.0436 172 ILE A CD1 
1352 N N   . MET A 173 ? 0.3596 0.3556 0.4998 -0.0082 0.0831  -0.0484 173 MET A N   
1353 C CA  . MET A 173 ? 0.3387 0.3329 0.4776 -0.0062 0.0844  -0.0483 173 MET A CA  
1354 C C   . MET A 173 ? 0.3668 0.3681 0.5288 0.0047  0.0704  -0.0480 173 MET A C   
1355 O O   . MET A 173 ? 0.3812 0.3786 0.5491 0.0071  0.0729  -0.0493 173 MET A O   
1356 C CB  . MET A 173 ? 0.3588 0.3461 0.4606 -0.0083 0.0813  -0.0393 173 MET A CB  
1357 C CG  . MET A 173 ? 0.3626 0.3398 0.4376 -0.0185 0.0921  -0.0383 173 MET A CG  
1358 S SD  . MET A 173 ? 0.3740 0.3410 0.4529 -0.0294 0.1146  -0.0500 173 MET A SD  
1359 C CE  . MET A 173 ? 0.3680 0.3354 0.4521 -0.0258 0.1117  -0.0521 173 MET A CE  
1360 N N   . THR A 174 ? 0.3282 0.3365 0.4998 0.0111  0.0551  -0.0462 174 THR A N   
1361 C CA  . THR A 174 ? 0.3204 0.3320 0.5085 0.0215  0.0385  -0.0445 174 THR A CA  
1362 C C   . THR A 174 ? 0.3147 0.3389 0.5361 0.0243  0.0286  -0.0514 174 THR A C   
1363 O O   . THR A 174 ? 0.3723 0.4014 0.6015 0.0171  0.0358  -0.0573 174 THR A O   
1364 C CB  . THR A 174 ? 0.3494 0.3535 0.5043 0.0260  0.0254  -0.0336 174 THR A CB  
1365 O OG1 . THR A 174 ? 0.3302 0.3362 0.4718 0.0247  0.0195  -0.0326 174 THR A OG1 
1366 C CG2 . THR A 174 ? 0.3599 0.3559 0.4867 0.0212  0.0352  -0.0280 174 THR A CG2 
1367 N N   . ARG A 175 ? 0.3168 0.3448 0.5580 0.0341  0.0108  -0.0506 175 ARG A N   
1368 C CA  . ARG A 175 ? 0.3356 0.3760 0.6029 0.0373  -0.0067 -0.0557 175 ARG A CA  
1369 C C   . ARG A 175 ? 0.3489 0.3801 0.5770 0.0387  -0.0233 -0.0480 175 ARG A C   
1370 O O   . ARG A 175 ? 0.3649 0.3836 0.5655 0.0449  -0.0336 -0.0382 175 ARG A O   
1371 C CB  . ARG A 175 ? 0.3559 0.4046 0.6640 0.0484  -0.0213 -0.0580 175 ARG A CB  
1372 C CG  . ARG A 175 ? 0.3994 0.4598 0.7554 0.0470  -0.0025 -0.0694 175 ARG A CG  
1373 C CD  . ARG A 175 ? 0.4293 0.4821 0.7985 0.0577  -0.0039 -0.0662 175 ARG A CD  
1374 N NE  . ARG A 175 ? 0.4181 0.4822 0.8379 0.0574  0.0155  -0.0794 175 ARG A NE  
1375 C CZ  . ARG A 175 ? 0.4535 0.5056 0.8662 0.0537  0.0394  -0.0825 175 ARG A CZ  
1376 N NH1 . ARG A 175 ? 0.3745 0.4058 0.7352 0.0496  0.0449  -0.0733 175 ARG A NH1 
1377 N NH2 . ARG A 175 ? 0.4512 0.5129 0.9115 0.0533  0.0589  -0.0966 175 ARG A NH2 
1378 N N   . MET A 176 ? 0.3482 0.3830 0.5723 0.0322  -0.0237 -0.0530 176 MET A N   
1379 C CA  . MET A 176 ? 0.3745 0.3971 0.5561 0.0312  -0.0302 -0.0476 176 MET A CA  
1380 C C   . MET A 176 ? 0.4117 0.4386 0.6008 0.0291  -0.0465 -0.0550 176 MET A C   
1381 O O   . MET A 176 ? 0.3853 0.4247 0.6088 0.0231  -0.0433 -0.0655 176 MET A O   
1382 C CB  . MET A 176 ? 0.3804 0.3963 0.5399 0.0242  -0.0097 -0.0457 176 MET A CB  
1383 C CG  . MET A 176 ? 0.4365 0.4403 0.5560 0.0249  -0.0113 -0.0400 176 MET A CG  
1384 S SD  . MET A 176 ? 0.5260 0.5250 0.6386 0.0203  -0.0153 -0.0477 176 MET A SD  
1385 C CE  . MET A 176 ? 0.4645 0.4598 0.5786 0.0135  0.0068  -0.0480 176 MET A CE  
1386 N N   . GLY A 177 ? 0.3983 0.4133 0.5530 0.0323  -0.0626 -0.0506 177 GLY A N   
1387 C CA  . GLY A 177 ? 0.4199 0.4326 0.5662 0.0278  -0.0753 -0.0582 177 GLY A CA  
1388 C C   . GLY A 177 ? 0.4684 0.4776 0.6052 0.0330  -0.1048 -0.0571 177 GLY A C   
1389 O O   . GLY A 177 ? 0.4574 0.4568 0.5746 0.0408  -0.1138 -0.0466 177 GLY A O   
1390 N N   . THR A 178 ? 0.4496 0.4651 0.5993 0.0278  -0.1208 -0.0680 178 THR A N   
1391 C CA  . THR A 178 ? 0.4936 0.5001 0.6190 0.0302  -0.1511 -0.0677 178 THR A CA  
1392 C C   . THR A 178 ? 0.5454 0.5603 0.6952 0.0411  -0.1744 -0.0613 178 THR A C   
1393 O O   . THR A 178 ? 0.5331 0.5298 0.6446 0.0472  -0.1944 -0.0517 178 THR A O   
1394 C CB  . THR A 178 ? 0.4703 0.4838 0.6091 0.0203  -0.1636 -0.0832 178 THR A CB  
1395 O OG1 . THR A 178 ? 0.5116 0.5090 0.6179 0.0119  -0.1438 -0.0878 178 THR A OG1 
1396 C CG2 . THR A 178 ? 0.5347 0.5409 0.6512 0.0219  -0.1998 -0.0841 178 THR A CG2 
1397 N N   . SER A 179 ? 0.5007 0.5405 0.7131 0.0440  -0.1709 -0.0662 179 SER A N   
1398 C CA  . SER A 179 ? 0.5223 0.5714 0.7671 0.0564  -0.1932 -0.0613 179 SER A CA  
1399 C C   . SER A 179 ? 0.5695 0.5966 0.7802 0.0662  -0.1884 -0.0445 179 SER A C   
1400 O O   . SER A 179 ? 0.5537 0.5737 0.7645 0.0776  -0.2126 -0.0357 179 SER A O   
1401 C CB  . SER A 179 ? 0.4520 0.5324 0.7744 0.0568  -0.1834 -0.0722 179 SER A CB  
1402 O OG  . SER A 179 ? 0.6135 0.6916 0.9388 0.0548  -0.1488 -0.0702 179 SER A OG  
1403 N N   . VAL A 180 ? 0.5211 0.5361 0.7026 0.0618  -0.1588 -0.0397 180 VAL A N   
1404 C CA  . VAL A 180 ? 0.5359 0.5293 0.6838 0.0682  -0.1525 -0.0251 180 VAL A CA  
1405 C C   . VAL A 180 ? 0.5884 0.5538 0.6738 0.0694  -0.1705 -0.0149 180 VAL A C   
1406 O O   . VAL A 180 ? 0.6146 0.5615 0.6809 0.0778  -0.1834 -0.0024 180 VAL A O   
1407 C CB  . VAL A 180 ? 0.4744 0.4655 0.6101 0.0615  -0.1184 -0.0243 180 VAL A CB  
1408 C CG1 . VAL A 180 ? 0.5198 0.4887 0.6188 0.0650  -0.1115 -0.0107 180 VAL A CG1 
1409 C CG2 . VAL A 180 ? 0.4739 0.4863 0.6631 0.0599  -0.1008 -0.0331 180 VAL A CG2 
1410 N N   . LEU A 181 ? 0.5855 0.5437 0.6353 0.0606  -0.1699 -0.0201 181 LEU A N   
1411 C CA  . LEU A 181 ? 0.6371 0.5663 0.6230 0.0597  -0.1851 -0.0126 181 LEU A CA  
1412 C C   . LEU A 181 ? 0.6826 0.6068 0.6703 0.0678  -0.2239 -0.0083 181 LEU A C   
1413 O O   . LEU A 181 ? 0.7269 0.6220 0.6661 0.0720  -0.2379 0.0051  181 LEU A O   
1414 C CB  . LEU A 181 ? 0.6426 0.5666 0.5979 0.0489  -0.1783 -0.0231 181 LEU A CB  
1415 C CG  . LEU A 181 ? 0.6662 0.5835 0.5973 0.0424  -0.1448 -0.0239 181 LEU A CG  
1416 C CD1 . LEU A 181 ? 0.6097 0.5203 0.5167 0.0337  -0.1422 -0.0360 181 LEU A CD1 
1417 C CD2 . LEU A 181 ? 0.6851 0.5778 0.5687 0.0439  -0.1346 -0.0105 181 LEU A CD2 
1418 N N   . GLU A 182 ? 0.6616 0.6135 0.7059 0.0698  -0.2420 -0.0191 182 GLU A N   
1419 C CA  . GLU A 182 ? 0.6984 0.6507 0.7538 0.0786  -0.2831 -0.0157 182 GLU A CA  
1420 C C   . GLU A 182 ? 0.6801 0.6251 0.7522 0.0939  -0.2911 -0.0010 182 GLU A C   
1421 O O   . GLU A 182 ? 0.7636 0.6885 0.8105 0.1029  -0.3230 0.0108  182 GLU A O   
1422 C CB  . GLU A 182 ? 0.6853 0.6747 0.8087 0.0762  -0.2980 -0.0329 182 GLU A CB  
1423 C CG  . GLU A 182 ? 0.7936 0.7852 0.8980 0.0606  -0.2940 -0.0477 182 GLU A CG  
1424 C CD  . GLU A 182 ? 0.8882 0.9170 1.0642 0.0551  -0.3029 -0.0660 182 GLU A CD  
1425 O OE1 . GLU A 182 ? 0.8886 0.9449 1.1339 0.0635  -0.3083 -0.0680 182 GLU A OE1 
1426 O OE2 . GLU A 182 ? 0.9155 0.9451 1.0798 0.0418  -0.3027 -0.0792 182 GLU A OE2 
1427 N N   . ALA A 183 ? 0.6617 0.6193 0.7733 0.0968  -0.2630 -0.0015 183 ALA A N   
1428 C CA  . ALA A 183 ? 0.6271 0.5737 0.7533 0.1106  -0.2662 0.0112  183 ALA A CA  
1429 C C   . ALA A 183 ? 0.6788 0.5833 0.7312 0.1099  -0.2586 0.0286  183 ALA A C   
1430 O O   . ALA A 183 ? 0.7118 0.5924 0.7502 0.1212  -0.2757 0.0433  183 ALA A O   
1431 C CB  . ALA A 183 ? 0.6412 0.6111 0.8273 0.1116  -0.2362 0.0032  183 ALA A CB  
1432 N N   . LEU A 184 ? 0.7091 0.6031 0.7158 0.0968  -0.2321 0.0272  184 LEU A N   
1433 C CA  . LEU A 184 ? 0.7291 0.5866 0.6722 0.0939  -0.2192 0.0417  184 LEU A CA  
1434 C C   . LEU A 184 ? 0.7561 0.5781 0.6366 0.0961  -0.2483 0.0542  184 LEU A C   
1435 O O   . LEU A 184 ? 0.7803 0.5691 0.6257 0.1011  -0.2521 0.0707  184 LEU A O   
1436 C CB  . LEU A 184 ? 0.7085 0.5677 0.6248 0.0799  -0.1857 0.0354  184 LEU A CB  
1437 C CG  . LEU A 184 ? 0.7511 0.5759 0.6031 0.0739  -0.1696 0.0476  184 LEU A CG  
1438 C CD1 . LEU A 184 ? 0.7083 0.5234 0.5721 0.0777  -0.1550 0.0574  184 LEU A CD1 
1439 C CD2 . LEU A 184 ? 0.6987 0.5287 0.5281 0.0616  -0.1427 0.0391  184 LEU A CD2 
1440 N N   . GLY A 185 ? 0.8152 0.6402 0.6772 0.0915  -0.2688 0.0467  185 GLY A N   
1441 C CA  . GLY A 185 ? 0.8502 0.6371 0.6404 0.0909  -0.2950 0.0578  185 GLY A CA  
1442 C C   . GLY A 185 ? 0.9273 0.6760 0.6438 0.0816  -0.2688 0.0682  185 GLY A C   
1443 O O   . GLY A 185 ? 0.8722 0.6287 0.5829 0.0710  -0.2341 0.0600  185 GLY A O   
1444 N N   . ASP A 186 ? 1.0486 0.7549 0.7104 0.0858  -0.2849 0.0869  186 ASP A N   
1445 C CA  . ASP A 186 ? 1.0959 0.7620 0.6878 0.0762  -0.2588 0.0983  186 ASP A CA  
1446 C C   . ASP A 186 ? 1.0559 0.7127 0.6672 0.0814  -0.2401 0.1104  186 ASP A C   
1447 O O   . ASP A 186 ? 1.0993 0.7138 0.6524 0.0767  -0.2297 0.1253  186 ASP A O   
1448 C CB  . ASP A 186 ? 1.2008 0.8169 0.7048 0.0735  -0.2838 0.1115  186 ASP A CB  
1449 C CG  . ASP A 186 ? 1.2906 0.9027 0.7474 0.0602  -0.2834 0.0981  186 ASP A CG  
1450 O OD1 . ASP A 186 ? 1.2034 0.8438 0.6858 0.0517  -0.2546 0.0809  186 ASP A OD1 
1451 O OD2 . ASP A 186 ? 1.4348 1.0236 0.8446 0.0562  -0.3027 0.1010  186 ASP A OD2 
1452 N N   . GLY A 187 ? 0.9764 0.6691 0.6660 0.0895  -0.2338 0.1035  187 GLY A N   
1453 C CA  . GLY A 187 ? 0.8810 0.5660 0.5916 0.0929  -0.2143 0.1115  187 GLY A CA  
1454 C C   . GLY A 187 ? 0.8877 0.5849 0.5998 0.0789  -0.1713 0.1037  187 GLY A C   
1455 O O   . GLY A 187 ? 0.8341 0.5456 0.5331 0.0683  -0.1558 0.0928  187 GLY A O   
1456 N N   . GLU A 188 ? 0.8177 0.5089 0.5486 0.0795  -0.1530 0.1089  188 GLU A N   
1457 C CA  . GLU A 188 ? 0.8480 0.5486 0.5802 0.0661  -0.1153 0.1031  188 GLU A CA  
1458 C C   . GLU A 188 ? 0.7803 0.5290 0.5727 0.0649  -0.1024 0.0853  188 GLU A C   
1459 O O   . GLU A 188 ? 0.7353 0.5068 0.5792 0.0747  -0.1154 0.0790  188 GLU A O   
1460 C CB  . GLU A 188 ? 0.8957 0.5721 0.6274 0.0655  -0.1015 0.1134  188 GLU A CB  
1461 C CG  . GLU A 188 ? 1.1124 0.7345 0.7781 0.0634  -0.1067 0.1327  188 GLU A CG  
1462 C CD  . GLU A 188 ? 1.2611 0.8586 0.9313 0.0617  -0.0913 0.1415  188 GLU A CD  
1463 O OE1 . GLU A 188 ? 1.2251 0.8495 0.9427 0.0581  -0.0716 0.1305  188 GLU A OE1 
1464 O OE2 . GLU A 188 ? 1.3862 0.9346 1.0096 0.0633  -0.0992 0.1594  188 GLU A OE2 
1465 N N   . PHE A 189 ? 0.7017 0.4646 0.4879 0.0527  -0.0757 0.0776  189 PHE A N   
1466 C CA  . PHE A 189 ? 0.6341 0.4368 0.4689 0.0503  -0.0619 0.0632  189 PHE A CA  
1467 C C   . PHE A 189 ? 0.6421 0.4503 0.4749 0.0388  -0.0323 0.0613  189 PHE A C   
1468 O O   . PHE A 189 ? 0.6671 0.4549 0.4604 0.0304  -0.0195 0.0674  189 PHE A O   
1469 C CB  . PHE A 189 ? 0.6310 0.4538 0.4682 0.0495  -0.0680 0.0524  189 PHE A CB  
1470 C CG  . PHE A 189 ? 0.6479 0.4552 0.4338 0.0411  -0.0592 0.0529  189 PHE A CG  
1471 C CD1 . PHE A 189 ? 0.7242 0.5012 0.4599 0.0419  -0.0765 0.0601  189 PHE A CD1 
1472 C CD2 . PHE A 189 ? 0.6441 0.4667 0.4322 0.0328  -0.0340 0.0455  189 PHE A CD2 
1473 C CE1 . PHE A 189 ? 0.7527 0.5128 0.4379 0.0330  -0.0650 0.0587  189 PHE A CE1 
1474 C CE2 . PHE A 189 ? 0.6663 0.4754 0.4121 0.0257  -0.0227 0.0439  189 PHE A CE2 
1475 C CZ  . PHE A 189 ? 0.7329 0.5098 0.4257 0.0250  -0.0363 0.0498  189 PHE A CZ  
1476 N N   . ILE A 190 ? 0.5909 0.4271 0.4669 0.0374  -0.0214 0.0521  190 ILE A N   
1477 C CA  . ILE A 190 ? 0.5701 0.4183 0.4507 0.0266  0.0025  0.0484  190 ILE A CA  
1478 C C   . ILE A 190 ? 0.5800 0.4471 0.4560 0.0226  0.0107  0.0411  190 ILE A C   
1479 O O   . ILE A 190 ? 0.4963 0.3808 0.3903 0.0274  0.0027  0.0339  190 ILE A O   
1480 C CB  . ILE A 190 ? 0.5849 0.4516 0.5069 0.0262  0.0087  0.0418  190 ILE A CB  
1481 C CG1 . ILE A 190 ? 0.6190 0.4644 0.5482 0.0315  0.0023  0.0475  190 ILE A CG1 
1482 C CG2 . ILE A 190 ? 0.5465 0.4272 0.4729 0.0145  0.0288  0.0377  190 ILE A CG2 
1483 C CD1 . ILE A 190 ? 0.6737 0.4863 0.5690 0.0260  0.0088  0.0587  190 ILE A CD1 
1484 N N   . LYS A 191 ? 0.5658 0.4288 0.4204 0.0137  0.0280  0.0424  191 LYS A N   
1485 C CA  . LYS A 191 ? 0.5535 0.4316 0.4046 0.0111  0.0380  0.0354  191 LYS A CA  
1486 C C   . LYS A 191 ? 0.5172 0.4260 0.4052 0.0079  0.0499  0.0285  191 LYS A C   
1487 O O   . LYS A 191 ? 0.4995 0.4125 0.3955 0.0002  0.0620  0.0298  191 LYS A O   
1488 C CB  . LYS A 191 ? 0.5639 0.4216 0.3748 0.0033  0.0526  0.0392  191 LYS A CB  
1489 C CG  . LYS A 191 ? 0.6162 0.4383 0.3794 0.0053  0.0398  0.0471  191 LYS A CG  
1490 C CD  . LYS A 191 ? 0.6958 0.4931 0.4142 -0.0055 0.0595  0.0514  191 LYS A CD  
1491 C CE  . LYS A 191 ? 0.8605 0.6141 0.5299 -0.0060 0.0482  0.0652  191 LYS A CE  
1492 N NZ  . LYS A 191 ? 0.9579 0.6833 0.5823 -0.0193 0.0719  0.0706  191 LYS A NZ  
1493 N N   . CYS A 192 ? 0.4532 0.3816 0.3617 0.0129  0.0454  0.0214  192 CYS A N   
1494 C CA  . CYS A 192 ? 0.4268 0.3813 0.3664 0.0115  0.0520  0.0164  192 CYS A CA  
1495 C C   . CYS A 192 ? 0.4442 0.4102 0.3857 0.0137  0.0591  0.0112  192 CYS A C   
1496 O O   . CYS A 192 ? 0.4807 0.4405 0.4125 0.0187  0.0531  0.0080  192 CYS A O   
1497 C CB  . CYS A 192 ? 0.4229 0.3858 0.3855 0.0157  0.0414  0.0135  192 CYS A CB  
1498 S SG  . CYS A 192 ? 0.4494 0.3980 0.4162 0.0156  0.0346  0.0173  192 CYS A SG  
1499 N N   . LEU A 193 ? 0.4275 0.4104 0.3841 0.0099  0.0714  0.0096  193 LEU A N   
1500 C CA  . LEU A 193 ? 0.4110 0.4056 0.3755 0.0135  0.0800  0.0046  193 LEU A CA  
1501 C C   . LEU A 193 ? 0.4350 0.4550 0.4330 0.0152  0.0785  0.0032  193 LEU A C   
1502 O O   . LEU A 193 ? 0.3821 0.4151 0.3950 0.0088  0.0815  0.0045  193 LEU A O   
1503 C CB  . LEU A 193 ? 0.4280 0.4187 0.3800 0.0080  0.0979  0.0035  193 LEU A CB  
1504 C CG  . LEU A 193 ? 0.4542 0.4596 0.4219 0.0118  0.1114  -0.0033 193 LEU A CG  
1505 C CD1 . LEU A 193 ? 0.4192 0.4126 0.3732 0.0201  0.1072  -0.0082 193 LEU A CD1 
1506 C CD2 . LEU A 193 ? 0.4926 0.4936 0.4491 0.0036  0.1332  -0.0052 193 LEU A CD2 
1507 N N   . HIS A 194 ? 0.3819 0.4065 0.3894 0.0229  0.0730  0.0007  194 HIS A N   
1508 C CA  . HIS A 194 ? 0.3756 0.4191 0.4085 0.0258  0.0689  0.0013  194 HIS A CA  
1509 C C   . HIS A 194 ? 0.3911 0.4408 0.4362 0.0349  0.0735  -0.0018 194 HIS A C   
1510 O O   . HIS A 194 ? 0.3850 0.4197 0.4164 0.0395  0.0756  -0.0054 194 HIS A O   
1511 C CB  . HIS A 194 ? 0.3616 0.3995 0.3932 0.0260  0.0571  0.0031  194 HIS A CB  
1512 C CG  . HIS A 194 ? 0.3798 0.4301 0.4274 0.0285  0.0514  0.0052  194 HIS A CG  
1513 N ND1 . HIS A 194 ? 0.3826 0.4269 0.4311 0.0354  0.0476  0.0056  194 HIS A ND1 
1514 C CD2 . HIS A 194 ? 0.3560 0.4215 0.4159 0.0243  0.0476  0.0075  194 HIS A CD2 
1515 C CE1 . HIS A 194 ? 0.4171 0.4705 0.4752 0.0363  0.0412  0.0096  194 HIS A CE1 
1516 N NE2 . HIS A 194 ? 0.4076 0.4753 0.4728 0.0296  0.0399  0.0105  194 HIS A NE2 
1517 N N   . SER A 195 ? 0.3610 0.4323 0.4333 0.0375  0.0740  -0.0010 195 SER A N   
1518 C CA  . SER A 195 ? 0.3901 0.4676 0.4807 0.0489  0.0745  -0.0023 195 SER A CA  
1519 C C   . SER A 195 ? 0.3983 0.4934 0.5117 0.0518  0.0617  0.0031  195 SER A C   
1520 O O   . SER A 195 ? 0.3851 0.4976 0.5104 0.0446  0.0579  0.0047  195 SER A O   
1521 C CB  . SER A 195 ? 0.3648 0.4521 0.4707 0.0522  0.0913  -0.0085 195 SER A CB  
1522 O OG  . SER A 195 ? 0.4016 0.4956 0.5314 0.0653  0.0917  -0.0100 195 SER A OG  
1523 N N   . VAL A 196 ? 0.3714 0.4592 0.4879 0.0617  0.0543  0.0061  196 VAL A N   
1524 C CA  . VAL A 196 ? 0.3934 0.4949 0.5288 0.0668  0.0403  0.0128  196 VAL A CA  
1525 C C   . VAL A 196 ? 0.4241 0.5535 0.5988 0.0740  0.0430  0.0107  196 VAL A C   
1526 O O   . VAL A 196 ? 0.4257 0.5734 0.6217 0.0771  0.0285  0.0159  196 VAL A O   
1527 C CB  . VAL A 196 ? 0.4344 0.5153 0.5598 0.0759  0.0326  0.0181  196 VAL A CB  
1528 C CG1 . VAL A 196 ? 0.4220 0.4801 0.5154 0.0669  0.0301  0.0196  196 VAL A CG1 
1529 C CG2 . VAL A 196 ? 0.4286 0.4987 0.5612 0.0873  0.0438  0.0130  196 VAL A CG2 
1530 N N   . GLY A 197 ? 0.4066 0.5392 0.5921 0.0769  0.0611  0.0028  197 GLY A N   
1531 C CA  . GLY A 197 ? 0.3984 0.5603 0.6266 0.0820  0.0684  -0.0016 197 GLY A CA  
1532 C C   . GLY A 197 ? 0.4709 0.6399 0.7311 0.1003  0.0627  0.0003  197 GLY A C   
1533 O O   . GLY A 197 ? 0.4510 0.6510 0.7555 0.1061  0.0574  0.0003  197 GLY A O   
1534 N N   A CYS A 198 ? 0.4597 0.6004 0.7011 0.1098  0.0625  0.0019  198 CYS A N   
1535 N N   B CYS A 198 ? 0.4559 0.5968 0.6977 0.1098  0.0636  0.0013  198 CYS A N   
1536 C CA  A CYS A 198 ? 0.4610 0.6000 0.7285 0.1287  0.0567  0.0051  198 CYS A CA  
1537 C CA  B CYS A 198 ? 0.4614 0.5999 0.7280 0.1285  0.0565  0.0052  198 CYS A CA  
1538 C C   A CYS A 198 ? 0.4784 0.5947 0.7393 0.1363  0.0773  -0.0045 198 CYS A C   
1539 C C   B CYS A 198 ? 0.4800 0.5967 0.7422 0.1369  0.0769  -0.0043 198 CYS A C   
1540 O O   A CYS A 198 ? 0.5027 0.5874 0.7381 0.1402  0.0750  -0.0024 198 CYS A O   
1541 O O   B CYS A 198 ? 0.5055 0.5912 0.7448 0.1420  0.0743  -0.0020 198 CYS A O   
1542 C CB  A CYS A 198 ? 0.4576 0.5775 0.7044 0.1321  0.0341  0.0182  198 CYS A CB  
1543 C CB  B CYS A 198 ? 0.4635 0.5815 0.7056 0.1303  0.0346  0.0180  198 CYS A CB  
1544 S SG  A CYS A 198 ? 0.4052 0.5501 0.6622 0.1268  0.0073  0.0291  198 CYS A SG  
1545 S SG  B CYS A 198 ? 0.5481 0.6725 0.8228 0.1505  0.0122  0.0302  198 CYS A SG  
1546 N N   . PRO A 199 ? 0.4783 0.6083 0.7601 0.1369  0.0992  -0.0163 199 PRO A N   
1547 C CA  . PRO A 199 ? 0.4922 0.5985 0.7651 0.1434  0.1206  -0.0276 199 PRO A CA  
1548 C C   . PRO A 199 ? 0.5512 0.6480 0.8506 0.1642  0.1161  -0.0254 199 PRO A C   
1549 O O   . PRO A 199 ? 0.5508 0.6712 0.8941 0.1770  0.1032  -0.0185 199 PRO A O   
1550 C CB  . PRO A 199 ? 0.5147 0.6424 0.8102 0.1395  0.1459  -0.0401 199 PRO A CB  
1551 C CG  . PRO A 199 ? 0.4492 0.6184 0.7870 0.1376  0.1354  -0.0348 199 PRO A CG  
1552 C CD  . PRO A 199 ? 0.4562 0.6212 0.7678 0.1294  0.1081  -0.0212 199 PRO A CD  
1553 N N   . LEU A 200 ? 0.5674 0.6276 0.8395 0.1674  0.1254  -0.0310 200 LEU A N   
1554 C CA  . LEU A 200 ? 0.6258 0.6666 0.9164 0.1865  0.1249  -0.0303 200 LEU A CA  
1555 C C   . LEU A 200 ? 0.6480 0.6942 0.9719 0.1978  0.1518  -0.0461 200 LEU A C   
1556 O O   . LEU A 200 ? 0.6396 0.6814 0.9439 0.1869  0.1749  -0.0602 200 LEU A O   
1557 C CB  . LEU A 200 ? 0.6120 0.6084 0.8563 0.1816  0.1230  -0.0301 200 LEU A CB  
1558 C CG  . LEU A 200 ? 0.6509 0.6403 0.8632 0.1693  0.1011  -0.0167 200 LEU A CG  
1559 C CD1 . LEU A 200 ? 0.5889 0.5399 0.7579 0.1595  0.1033  -0.0205 200 LEU A CD1 
1560 C CD2 . LEU A 200 ? 0.6773 0.6717 0.9098 0.1812  0.0790  0.0001  200 LEU A CD2 
1561 N N   . PRO A 201 ? 0.7201 0.7736 1.0838 0.2157  0.1462  -0.0443 201 PRO A N   
1562 C CA  . PRO A 201 ? 0.7224 0.7740 1.1070 0.2318  0.1194  -0.0276 201 PRO A CA  
1563 C C   . PRO A 201 ? 0.7057 0.7974 1.1212 0.2326  0.0965  -0.0142 201 PRO A C   
1564 O O   . PRO A 201 ? 0.7234 0.8531 1.1647 0.2256  0.1026  -0.0205 201 PRO A O   
1565 C CB  . PRO A 201 ? 0.7756 0.8237 1.1890 0.2482  0.1259  -0.0349 201 PRO A CB  
1566 C CG  . PRO A 201 ? 0.7820 0.8572 1.2138 0.2409  0.1503  -0.0516 201 PRO A CG  
1567 C CD  . PRO A 201 ? 0.7229 0.7863 1.1092 0.2197  0.1666  -0.0594 201 PRO A CD  
1568 N N   . LEU A 202 ? 0.7522 0.8334 1.1611 0.2391  0.0691  0.0043  202 LEU A N   
1569 C CA  . LEU A 202 ? 0.8549 0.9683 1.2767 0.2348  0.0425  0.0169  202 LEU A CA  
1570 C C   . LEU A 202 ? 0.9292 1.0803 1.4115 0.2503  0.0321  0.0169  202 LEU A C   
1571 O O   . LEU A 202 ? 0.9298 1.0679 1.4247 0.2681  0.0225  0.0215  202 LEU A O   
1572 C CB  . LEU A 202 ? 0.8406 0.9245 1.2208 0.2329  0.0160  0.0356  202 LEU A CB  
1573 C CG  . LEU A 202 ? 0.7485 0.8000 1.0646 0.2122  0.0230  0.0346  202 LEU A CG  
1574 C CD1 . LEU A 202 ? 0.7528 0.7803 1.0313 0.2080  -0.0007 0.0523  202 LEU A CD1 
1575 C CD2 . LEU A 202 ? 0.6753 0.7521 0.9818 0.1920  0.0331  0.0250  202 LEU A CD2 
1576 N N   . LYS A 203 ? 1.0223 1.2185 1.5345 0.2406  0.0332  0.0110  203 LYS A N   
1577 C CA  . LYS A 203 ? 1.0710 1.3065 1.6338 0.2503  0.0175  0.0122  203 LYS A CA  
1578 C C   . LYS A 203 ? 1.1306 1.3713 1.6922 0.2555  -0.0229 0.0319  203 LYS A C   
1579 O O   . LYS A 203 ? 1.1624 1.4176 1.7538 0.2707  -0.0426 0.0381  203 LYS A O   
1580 C CB  . LYS A 203 ? 1.1070 1.3867 1.7001 0.2352  0.0330  -0.0010 203 LYS A CB  
1581 C CG  . LYS A 203 ? 1.1299 1.4031 1.7183 0.2280  0.0728  -0.0199 203 LYS A CG  
1582 C CD  . LYS A 203 ? 1.1357 1.4045 1.7513 0.2456  0.0846  -0.0276 203 LYS A CD  
1583 C CE  . LYS A 203 ? 1.1713 1.4338 1.7793 0.2361  0.1238  -0.0467 203 LYS A CE  
1584 N NZ  . LYS A 203 ? 1.1354 1.3569 1.6832 0.2242  0.1399  -0.0505 203 LYS A NZ  
1585 N N   . LYS A 204 ? 1.2169 1.4442 1.7417 0.2429  -0.0357 0.0424  204 LYS A N   
1586 C CA  . LYS A 204 ? 1.1873 1.4150 1.6976 0.2425  -0.0737 0.0608  204 LYS A CA  
1587 C C   . LYS A 204 ? 1.2231 1.3941 1.6634 0.2398  -0.0803 0.0738  204 LYS A C   
1588 O O   . LYS A 204 ? 1.1956 1.3401 1.5896 0.2244  -0.0592 0.0674  204 LYS A O   
1589 C CB  . LYS A 204 ? 1.2262 1.4833 1.7255 0.2181  -0.0806 0.0574  204 LYS A CB  
1590 C CG  . LYS A 204 ? 1.2559 1.5629 1.8128 0.2121  -0.0629 0.0408  204 LYS A CG  
1591 C CD  . LYS A 204 ? 1.3395 1.6623 1.8721 0.1848  -0.0637 0.0366  204 LYS A CD  
1592 C CE  . LYS A 204 ? 1.2910 1.6565 1.8741 0.1757  -0.0408 0.0199  204 LYS A CE  
1593 N NZ  . LYS A 204 ? 1.1596 1.5346 1.7168 0.1488  -0.0398 0.0160  204 LYS A NZ  
1594 N N   . PRO A 205 ? 1.1373 1.2876 1.5678 0.2538  -0.1090 0.0921  205 PRO A N   
1595 C CA  . PRO A 205 ? 1.0466 1.1409 1.4078 0.2482  -0.1130 0.1048  205 PRO A CA  
1596 C C   . PRO A 205 ? 0.9511 1.0394 1.2561 0.2212  -0.1175 0.1066  205 PRO A C   
1597 O O   . PRO A 205 ? 0.9099 1.0322 1.2247 0.2106  -0.1316 0.1054  205 PRO A O   
1598 C CB  . PRO A 205 ? 1.0838 1.1615 1.4514 0.2698  -0.1457 0.1254  205 PRO A CB  
1599 C CG  . PRO A 205 ? 1.0905 1.2217 1.5072 0.2751  -0.1641 0.1221  205 PRO A CG  
1600 C CD  . PRO A 205 ? 1.1042 1.2767 1.5721 0.2715  -0.1348 0.0994  205 PRO A CD  
1601 N N   . LEU A 206 ? 0.8877 0.9322 1.1362 0.2097  -0.1040 0.1082  206 LEU A N   
1602 C CA  . LEU A 206 ? 0.7743 0.8105 0.9726 0.1844  -0.1011 0.1068  206 LEU A CA  
1603 C C   . LEU A 206 ? 0.8019 0.8096 0.9519 0.1795  -0.1257 0.1248  206 LEU A C   
1604 O O   . LEU A 206 ? 0.8483 0.8211 0.9821 0.1924  -0.1365 0.1392  206 LEU A O   
1605 C CB  . LEU A 206 ? 0.7212 0.7296 0.8897 0.1730  -0.0724 0.0967  206 LEU A CB  
1606 C CG  . LEU A 206 ? 0.6935 0.7235 0.8918 0.1718  -0.0468 0.0781  206 LEU A CG  
1607 C CD1 . LEU A 206 ? 0.6654 0.6691 0.8263 0.1568  -0.0261 0.0697  206 LEU A CD1 
1608 C CD2 . LEU A 206 ? 0.6055 0.6819 0.8325 0.1639  -0.0480 0.0700  206 LEU A CD2 
1609 N N   . VAL A 207 ? 0.7490 0.7679 0.8725 0.1600  -0.1331 0.1236  207 VAL A N   
1610 C CA  . VAL A 207 ? 0.7571 0.7473 0.8254 0.1505  -0.1529 0.1380  207 VAL A CA  
1611 C C   . VAL A 207 ? 0.7863 0.7382 0.8010 0.1324  -0.1303 0.1350  207 VAL A C   
1612 O O   . VAL A 207 ? 0.7563 0.7214 0.7709 0.1174  -0.1104 0.1205  207 VAL A O   
1613 C CB  . VAL A 207 ? 0.7558 0.7786 0.8250 0.1384  -0.1733 0.1365  207 VAL A CB  
1614 C CG1 . VAL A 207 ? 0.7649 0.7532 0.7690 0.1275  -0.1935 0.1508  207 VAL A CG1 
1615 C CG2 . VAL A 207 ? 0.7689 0.8368 0.9023 0.1554  -0.1948 0.1369  207 VAL A CG2 
1616 N N   . ASN A 208 ? 0.7476 0.6513 0.7185 0.1338  -0.1332 0.1489  208 ASN A N   
1617 C CA  . ASN A 208 ? 0.8095 0.6754 0.7339 0.1167  -0.1105 0.1461  208 ASN A CA  
1618 C C   . ASN A 208 ? 0.7648 0.6373 0.7153 0.1155  -0.0818 0.1297  208 ASN A C   
1619 O O   . ASN A 208 ? 0.7805 0.6457 0.7113 0.0982  -0.0626 0.1200  208 ASN A O   
1620 C CB  . ASN A 208 ? 0.8096 0.6762 0.6947 0.0933  -0.1092 0.1421  208 ASN A CB  
1621 C CG  . ASN A 208 ? 0.8599 0.6906 0.6870 0.0871  -0.1277 0.1592  208 ASN A CG  
1622 O OD1 . ASN A 208 ? 0.9840 0.7784 0.7900 0.0978  -0.1369 0.1753  208 ASN A OD1 
1623 N ND2 . ASN A 208 ? 0.8737 0.7101 0.6702 0.0692  -0.1326 0.1556  208 ASN A ND2 
1624 N N   . ASN A 209 ? 0.7282 0.6147 0.7234 0.1337  -0.0791 0.1259  209 ASN A N   
1625 C CA  . ASN A 209 ? 0.7568 0.6493 0.7748 0.1333  -0.0543 0.1098  209 ASN A CA  
1626 C C   . ASN A 209 ? 0.6624 0.5882 0.6907 0.1188  -0.0431 0.0944  209 ASN A C   
1627 O O   . ASN A 209 ? 0.6466 0.5701 0.6769 0.1123  -0.0238 0.0821  209 ASN A O   
1628 C CB  . ASN A 209 ? 0.7510 0.5993 0.7379 0.1260  -0.0374 0.1096  209 ASN A CB  
1629 C CG  . ASN A 209 ? 0.8462 0.6576 0.8289 0.1421  -0.0427 0.1222  209 ASN A CG  
1630 O OD1 . ASN A 209 ? 0.8797 0.6994 0.8990 0.1612  -0.0443 0.1208  209 ASN A OD1 
1631 N ND2 . ASN A 209 ? 0.8997 0.6677 0.8371 0.1343  -0.0439 0.1347  209 ASN A ND2 
1632 N N   . TRP A 210 ? 0.6295 0.5844 0.6634 0.1133  -0.0560 0.0949  210 TRP A N   
1633 C CA  . TRP A 210 ? 0.6078 0.5868 0.6444 0.0980  -0.0459 0.0823  210 TRP A CA  
1634 C C   . TRP A 210 ? 0.5506 0.5690 0.6338 0.1053  -0.0435 0.0733  210 TRP A C   
1635 O O   . TRP A 210 ? 0.5024 0.5472 0.6097 0.1107  -0.0593 0.0768  210 TRP A O   
1636 C CB  . TRP A 210 ? 0.6097 0.5900 0.6174 0.0834  -0.0578 0.0865  210 TRP A CB  
1637 C CG  . TRP A 210 ? 0.5502 0.5475 0.5574 0.0677  -0.0458 0.0740  210 TRP A CG  
1638 C CD1 . TRP A 210 ? 0.5532 0.5836 0.5823 0.0632  -0.0500 0.0677  210 TRP A CD1 
1639 C CD2 . TRP A 210 ? 0.5697 0.5508 0.5564 0.0550  -0.0276 0.0662  210 TRP A CD2 
1640 N NE1 . TRP A 210 ? 0.4804 0.5120 0.4999 0.0491  -0.0357 0.0577  210 TRP A NE1 
1641 C CE2 . TRP A 210 ? 0.5566 0.5599 0.5523 0.0449  -0.0228 0.0566  210 TRP A CE2 
1642 C CE3 . TRP A 210 ? 0.6244 0.5747 0.5893 0.0509  -0.0151 0.0660  210 TRP A CE3 
1643 C CZ2 . TRP A 210 ? 0.5487 0.5445 0.5337 0.0335  -0.0076 0.0477  210 TRP A CZ2 
1644 C CZ3 . TRP A 210 ? 0.5701 0.5174 0.5280 0.0384  0.0002  0.0559  210 TRP A CZ3 
1645 C CH2 . TRP A 210 ? 0.5350 0.5050 0.5036 0.0310  0.0029  0.0473  210 TRP A CH2 
1646 N N   . ALA A 211 ? 0.5037 0.5256 0.5984 0.1042  -0.0238 0.0614  211 ALA A N   
1647 C CA  . ALA A 211 ? 0.5145 0.5681 0.6477 0.1094  -0.0162 0.0521  211 ALA A CA  
1648 C C   . ALA A 211 ? 0.4948 0.5734 0.6296 0.0947  -0.0166 0.0469  211 ALA A C   
1649 O O   . ALA A 211 ? 0.4703 0.5388 0.5795 0.0811  -0.0090 0.0428  211 ALA A O   
1650 C CB  . ALA A 211 ? 0.4984 0.5407 0.6335 0.1118  0.0047  0.0415  211 ALA A CB  
1651 N N   . CYS A 212 ? 0.4898 0.6008 0.6574 0.0977  -0.0255 0.0468  212 CYS A N   
1652 C CA  . CYS A 212 ? 0.4717 0.6069 0.6455 0.0834  -0.0254 0.0412  212 CYS A CA  
1653 C C   . CYS A 212 ? 0.4621 0.6355 0.6867 0.0903  -0.0294 0.0381  212 CYS A C   
1654 O O   . CYS A 212 ? 0.3998 0.5809 0.6534 0.1070  -0.0368 0.0421  212 CYS A O   
1655 C CB  . CYS A 212 ? 0.4756 0.6031 0.6188 0.0709  -0.0413 0.0470  212 CYS A CB  
1656 S SG  . CYS A 212 ? 0.5136 0.6489 0.6644 0.0800  -0.0726 0.0598  212 CYS A SG  
1657 N N   . ASN A 213 ? 0.4344 0.6313 0.6723 0.0773  -0.0240 0.0308  213 ASN A N   
1658 C CA  . ASN A 213 ? 0.4620 0.6991 0.7528 0.0797  -0.0243 0.0254  213 ASN A CA  
1659 C C   . ASN A 213 ? 0.4669 0.7228 0.7580 0.0620  -0.0351 0.0233  213 ASN A C   
1660 O O   . ASN A 213 ? 0.4652 0.7257 0.7537 0.0475  -0.0194 0.0154  213 ASN A O   
1661 C CB  . ASN A 213 ? 0.4495 0.6929 0.7592 0.0804  0.0043  0.0147  213 ASN A CB  
1662 C CG  . ASN A 213 ? 0.4706 0.7539 0.8424 0.0875  0.0086  0.0084  213 ASN A CG  
1663 O OD1 . ASN A 213 ? 0.4837 0.7989 0.8879 0.0830  -0.0069 0.0084  213 ASN A OD1 
1664 N ND2 . ASN A 213 ? 0.4310 0.7130 0.8213 0.0978  0.0306  0.0016  213 ASN A ND2 
1665 N N   . PRO A 214 ? 0.4655 0.7284 0.7550 0.0618  -0.0627 0.0305  214 PRO A N   
1666 C CA  . PRO A 214 ? 0.4933 0.7675 0.7733 0.0423  -0.0737 0.0272  214 PRO A CA  
1667 C C   . PRO A 214 ? 0.4890 0.8036 0.8186 0.0334  -0.0674 0.0167  214 PRO A C   
1668 O O   . PRO A 214 ? 0.4803 0.7956 0.7984 0.0141  -0.0599 0.0098  214 PRO A O   
1669 C CB  . PRO A 214 ? 0.5339 0.8064 0.8018 0.0466  -0.1068 0.0376  214 PRO A CB  
1670 C CG  . PRO A 214 ? 0.5166 0.7611 0.7674 0.0654  -0.1085 0.0483  214 PRO A CG  
1671 C CD  . PRO A 214 ? 0.4878 0.7421 0.7757 0.0781  -0.0855 0.0424  214 PRO A CD  
1672 N N   . GLU A 215 ? 0.4481 0.7952 0.8349 0.0467  -0.0680 0.0147  215 GLU A N   
1673 C CA  . GLU A 215 ? 0.4959 0.8851 0.9371 0.0373  -0.0605 0.0037  215 GLU A CA  
1674 C C   . GLU A 215 ? 0.4505 0.8295 0.8805 0.0234  -0.0260 -0.0056 215 GLU A C   
1675 O O   . GLU A 215 ? 0.3940 0.7908 0.8397 0.0051  -0.0189 -0.0138 215 GLU A O   
1676 C CB  . GLU A 215 ? 0.5840 1.0083 1.0924 0.0566  -0.0628 0.0022  215 GLU A CB  
1677 C CG  . GLU A 215 ? 0.6810 1.1090 1.1992 0.0753  -0.0974 0.0141  215 GLU A CG  
1678 C CD  . GLU A 215 ? 0.8786 1.3355 1.4644 0.0985  -0.0960 0.0126  215 GLU A CD  
1679 O OE1 . GLU A 215 ? 0.9167 1.3770 1.5250 0.1022  -0.0630 0.0032  215 GLU A OE1 
1680 O OE2 . GLU A 215 ? 0.9794 1.4541 1.5948 0.1133  -0.1279 0.0208  215 GLU A OE2 
1681 N N   . LEU A 216 ? 0.4975 0.6554 0.8641 0.0184  0.0544  -0.0162 216 LEU A N   
1682 C CA  . LEU A 216 ? 0.4855 0.6421 0.8454 0.0138  0.0754  -0.0183 216 LEU A CA  
1683 C C   . LEU A 216 ? 0.4692 0.6090 0.7908 0.0044  0.0755  -0.0188 216 LEU A C   
1684 O O   . LEU A 216 ? 0.4778 0.6114 0.7859 0.0018  0.0912  -0.0203 216 LEU A O   
1685 C CB  . LEU A 216 ? 0.4672 0.6160 0.8222 0.0238  0.0924  -0.0197 216 LEU A CB  
1686 C CG  . LEU A 216 ? 0.4954 0.6603 0.8899 0.0344  0.0981  -0.0198 216 LEU A CG  
1687 C CD1 . LEU A 216 ? 0.4938 0.6455 0.8753 0.0440  0.1162  -0.0220 216 LEU A CD1 
1688 C CD2 . LEU A 216 ? 0.4855 0.6752 0.9221 0.0298  0.1057  -0.0200 216 LEU A CD2 
1689 N N   . THR A 217 ? 0.4560 0.5874 0.7593 -0.0001 0.0585  -0.0177 217 THR A N   
1690 C CA  . THR A 217 ? 0.4469 0.5620 0.7149 -0.0078 0.0587  -0.0184 217 THR A CA  
1691 C C   . THR A 217 ? 0.4805 0.6018 0.7524 -0.0172 0.0665  -0.0194 217 THR A C   
1692 O O   . THR A 217 ? 0.4278 0.5636 0.7239 -0.0224 0.0613  -0.0191 217 THR A O   
1693 C CB  . THR A 217 ? 0.4838 0.5890 0.7341 -0.0107 0.0405  -0.0168 217 THR A CB  
1694 O OG1 . THR A 217 ? 0.4656 0.5593 0.7051 -0.0023 0.0357  -0.0154 217 THR A OG1 
1695 C CG2 . THR A 217 ? 0.4664 0.5569 0.6852 -0.0192 0.0417  -0.0179 217 THR A CG2 
1696 N N   . LEU A 218 ? 0.4253 0.5342 0.6727 -0.0194 0.0781  -0.0208 218 LEU A N   
1697 C CA  . LEU A 218 ? 0.4119 0.5224 0.6584 -0.0269 0.0876  -0.0212 218 LEU A CA  
1698 C C   . LEU A 218 ? 0.4180 0.5098 0.6288 -0.0285 0.0917  -0.0226 218 LEU A C   
1699 O O   . LEU A 218 ? 0.4005 0.4823 0.5960 -0.0221 0.0980  -0.0240 218 LEU A O   
1700 C CB  . LEU A 218 ? 0.4067 0.5274 0.6755 -0.0241 0.1047  -0.0211 218 LEU A CB  
1701 C CG  . LEU A 218 ? 0.4181 0.5397 0.6887 -0.0321 0.1163  -0.0206 218 LEU A CG  
1702 C CD1 . LEU A 218 ? 0.3719 0.5068 0.6658 -0.0414 0.1059  -0.0202 218 LEU A CD1 
1703 C CD2 . LEU A 218 ? 0.4856 0.6115 0.7707 -0.0279 0.1370  -0.0203 218 LEU A CD2 
1704 N N   . ILE A 219 ? 0.3771 0.4641 0.5755 -0.0365 0.0873  -0.0226 219 ILE A N   
1705 C CA  . ILE A 219 ? 0.3845 0.4557 0.5531 -0.0380 0.0899  -0.0241 219 ILE A CA  
1706 C C   . ILE A 219 ? 0.4429 0.5132 0.6101 -0.0432 0.0995  -0.0236 219 ILE A C   
1707 O O   . ILE A 219 ? 0.4390 0.5136 0.6141 -0.0507 0.0955  -0.0228 219 ILE A O   
1708 C CB  . ILE A 219 ? 0.3936 0.4569 0.5468 -0.0420 0.0773  -0.0246 219 ILE A CB  
1709 C CG1 . ILE A 219 ? 0.4686 0.5307 0.6228 -0.0372 0.0683  -0.0240 219 ILE A CG1 
1710 C CG2 . ILE A 219 ? 0.3664 0.4156 0.4942 -0.0427 0.0804  -0.0266 219 ILE A CG2 
1711 C CD1 . ILE A 219 ? 0.4243 0.4964 0.5970 -0.0384 0.0567  -0.0220 219 ILE A CD1 
1712 N N   . ALA A 220 ? 0.4064 0.4689 0.5618 -0.0390 0.1122  -0.0240 220 ALA A N   
1713 C CA  . ALA A 220 ? 0.3853 0.4448 0.5387 -0.0427 0.1239  -0.0225 220 ALA A CA  
1714 C C   . ALA A 220 ? 0.3971 0.4389 0.5193 -0.0420 0.1254  -0.0234 220 ALA A C   
1715 O O   . ALA A 220 ? 0.3923 0.4248 0.4962 -0.0364 0.1223  -0.0258 220 ALA A O   
1716 C CB  . ALA A 220 ? 0.4199 0.4832 0.5853 -0.0379 0.1397  -0.0214 220 ALA A CB  
1717 N N   . HIS A 221 ? 0.3910 0.4279 0.5084 -0.0475 0.1300  -0.0217 221 HIS A N   
1718 C CA  . HIS A 221 ? 0.4016 0.4216 0.4911 -0.0465 0.1306  -0.0221 221 HIS A CA  
1719 C C   . HIS A 221 ? 0.4444 0.4554 0.5268 -0.0468 0.1456  -0.0190 221 HIS A C   
1720 O O   . HIS A 221 ? 0.4570 0.4754 0.5585 -0.0530 0.1523  -0.0166 221 HIS A O   
1721 C CB  . HIS A 221 ? 0.4303 0.4487 0.5164 -0.0528 0.1202  -0.0228 221 HIS A CB  
1722 C CG  . HIS A 221 ? 0.3969 0.4224 0.4895 -0.0538 0.1075  -0.0250 221 HIS A CG  
1723 N ND1 . HIS A 221 ? 0.4001 0.4388 0.5141 -0.0567 0.1024  -0.0245 221 HIS A ND1 
1724 C CD2 . HIS A 221 ? 0.3887 0.4085 0.4686 -0.0522 0.0994  -0.0276 221 HIS A CD2 
1725 C CE1 . HIS A 221 ? 0.3994 0.4377 0.5094 -0.0565 0.0918  -0.0261 221 HIS A CE1 
1726 N NE2 . HIS A 221 ? 0.3867 0.4140 0.4772 -0.0543 0.0910  -0.0280 221 HIS A NE2 
1727 N N   . LEU A 222 ? 0.4682 0.4621 0.5229 -0.0401 0.1504  -0.0193 222 LEU A N   
1728 C CA  . LEU A 222 ? 0.5038 0.4834 0.5436 -0.0386 0.1658  -0.0159 222 LEU A CA  
1729 C C   . LEU A 222 ? 0.5864 0.5464 0.5952 -0.0358 0.1611  -0.0158 222 LEU A C   
1730 O O   . LEU A 222 ? 0.5809 0.5260 0.5634 -0.0275 0.1605  -0.0174 222 LEU A O   
1731 C CB  . LEU A 222 ? 0.5386 0.5133 0.5719 -0.0310 0.1779  -0.0160 222 LEU A CB  
1732 C CG  . LEU A 222 ? 0.5552 0.5496 0.6223 -0.0325 0.1846  -0.0158 222 LEU A CG  
1733 C CD1 . LEU A 222 ? 0.5130 0.5184 0.5900 -0.0285 0.1720  -0.0199 222 LEU A CD1 
1734 C CD2 . LEU A 222 ? 0.6012 0.5878 0.6644 -0.0281 0.2056  -0.0137 222 LEU A CD2 
1735 N N   . PRO A 223 ? 0.5534 0.5124 0.5645 -0.0421 0.1566  -0.0145 223 PRO A N   
1736 C CA  . PRO A 223 ? 0.6218 0.5642 0.6072 -0.0386 0.1497  -0.0150 223 PRO A CA  
1737 C C   . PRO A 223 ? 0.7008 0.6199 0.6552 -0.0316 0.1590  -0.0121 223 PRO A C   
1738 O O   . PRO A 223 ? 0.7007 0.6065 0.6312 -0.0242 0.1505  -0.0141 223 PRO A O   
1739 C CB  . PRO A 223 ? 0.6152 0.5602 0.6115 -0.0473 0.1472  -0.0135 223 PRO A CB  
1740 C CG  . PRO A 223 ? 0.6139 0.5728 0.6378 -0.0558 0.1555  -0.0115 223 PRO A CG  
1741 C CD  . PRO A 223 ? 0.5365 0.5094 0.5745 -0.0524 0.1560  -0.0133 223 PRO A CD  
1742 N N   . ASP A 224 ? 0.6867 0.5999 0.6407 -0.0334 0.1762  -0.0076 224 ASP A N   
1743 C CA  . ASP A 224 ? 0.7837 0.6702 0.7031 -0.0266 0.1871  -0.0040 224 ASP A CA  
1744 C C   . ASP A 224 ? 0.7891 0.6661 0.6855 -0.0159 0.1846  -0.0073 224 ASP A C   
1745 O O   . ASP A 224 ? 0.8281 0.6805 0.6881 -0.0078 0.1842  -0.0064 224 ASP A O   
1746 C CB  . ASP A 224 ? 0.8612 0.7437 0.7879 -0.0318 0.2091  0.0016  224 ASP A CB  
1747 C CG  . ASP A 224 ? 0.8680 0.7546 0.8131 -0.0426 0.2119  0.0048  224 ASP A CG  
1748 O OD1 . ASP A 224 ? 0.8009 0.6811 0.7367 -0.0432 0.2004  0.0043  224 ASP A OD1 
1749 O OD2 . ASP A 224 ? 0.9362 0.8325 0.9066 -0.0506 0.2258  0.0072  224 ASP A OD2 
1750 N N   . ARG A 225 ? 0.7230 0.6174 0.6387 -0.0154 0.1823  -0.0113 225 ARG A N   
1751 C CA  . ARG A 225 ? 0.7391 0.6250 0.6354 -0.0060 0.1794  -0.0156 225 ARG A CA  
1752 C C   . ARG A 225 ? 0.7072 0.6007 0.6061 -0.0037 0.1586  -0.0219 225 ARG A C   
1753 O O   . ARG A 225 ? 0.7327 0.6190 0.6164 0.0035  0.1535  -0.0266 225 ARG A O   
1754 C CB  . ARG A 225 ? 0.7674 0.6646 0.6824 -0.0060 0.1924  -0.0159 225 ARG A CB  
1755 C CG  . ARG A 225 ? 0.9144 0.7986 0.8204 -0.0057 0.2162  -0.0105 225 ARG A CG  
1756 C CD  . ARG A 225 ? 0.9477 0.8525 0.8901 -0.0095 0.2296  -0.0099 225 ARG A CD  
1757 N NE  . ARG A 225 ? 0.9667 0.8786 0.9140 -0.0033 0.2253  -0.0151 225 ARG A NE  
1758 C CZ  . ARG A 225 ? 1.0914 0.9894 1.0204 0.0048  0.2384  -0.0164 225 ARG A CZ  
1759 N NH1 . ARG A 225 ? 1.1611 1.0362 1.0633 0.0079  0.2575  -0.0125 225 ARG A NH1 
1760 N NH2 . ARG A 225 ? 0.9482 0.8533 0.8842 0.0100  0.2331  -0.0216 225 ARG A NH2 
1761 N N   . ARG A 226 ? 0.6253 0.5320 0.5426 -0.0098 0.1476  -0.0224 226 ARG A N   
1762 C CA  . ARG A 226 ? 0.6789 0.5948 0.6042 -0.0093 0.1303  -0.0281 226 ARG A CA  
1763 C C   . ARG A 226 ? 0.6032 0.5319 0.5441 -0.0086 0.1284  -0.0319 226 ARG A C   
1764 O O   . ARG A 226 ? 0.5888 0.5147 0.5227 -0.0040 0.1187  -0.0373 226 ARG A O   
1765 C CB  . ARG A 226 ? 0.6406 0.5393 0.5386 -0.0014 0.1191  -0.0313 226 ARG A CB  
1766 C CG  . ARG A 226 ? 0.7528 0.6456 0.6458 -0.0026 0.1134  -0.0292 226 ARG A CG  
1767 C CD  . ARG A 226 ? 0.8197 0.6895 0.6842 0.0013  0.1231  -0.0237 226 ARG A CD  
1768 N NE  . ARG A 226 ? 0.8275 0.6880 0.6835 0.0024  0.1163  -0.0219 226 ARG A NE  
1769 C CZ  . ARG A 226 ? 0.8499 0.7127 0.7167 -0.0045 0.1222  -0.0175 226 ARG A CZ  
1770 N NH1 . ARG A 226 ? 0.7872 0.6632 0.6760 -0.0137 0.1333  -0.0149 226 ARG A NH1 
1771 N NH2 . ARG A 226 ? 0.9040 0.7552 0.7599 -0.0018 0.1160  -0.0162 226 ARG A NH2 
1772 N N   . GLU A 227 ? 0.5672 0.5096 0.5306 -0.0132 0.1375  -0.0293 227 GLU A N   
1773 C CA  . GLU A 227 ? 0.5470 0.5006 0.5260 -0.0118 0.1374  -0.0320 227 GLU A CA  
1774 C C   . GLU A 227 ? 0.4783 0.4522 0.4880 -0.0193 0.1323  -0.0310 227 GLU A C   
1775 O O   . GLU A 227 ? 0.5102 0.4913 0.5331 -0.0259 0.1352  -0.0274 227 GLU A O   
1776 C CB  . GLU A 227 ? 0.5796 0.5295 0.5573 -0.0080 0.1538  -0.0300 227 GLU A CB  
1777 C CG  . GLU A 227 ? 0.6436 0.5736 0.5908 0.0014  0.1566  -0.0334 227 GLU A CG  
1778 C CD  . GLU A 227 ? 0.7237 0.6463 0.6654 0.0052  0.1763  -0.0309 227 GLU A CD  
1779 O OE1 . GLU A 227 ? 0.7364 0.6756 0.7073 0.0024  0.1850  -0.0289 227 GLU A OE1 
1780 O OE2 . GLU A 227 ? 0.8437 0.7430 0.7516 0.0114  0.1831  -0.0308 227 GLU A OE2 
1781 N N   . ILE A 228 ? 0.4543 0.4353 0.4731 -0.0181 0.1241  -0.0344 228 ILE A N   
1782 C CA  . ILE A 228 ? 0.4194 0.4166 0.4631 -0.0231 0.1187  -0.0335 228 ILE A CA  
1783 C C   . ILE A 228 ? 0.4112 0.4128 0.4642 -0.0181 0.1219  -0.0347 228 ILE A C   
1784 O O   . ILE A 228 ? 0.3960 0.3885 0.4360 -0.0125 0.1198  -0.0386 228 ILE A O   
1785 C CB  . ILE A 228 ? 0.4168 0.4149 0.4599 -0.0262 0.1059  -0.0360 228 ILE A CB  
1786 C CG1 . ILE A 228 ? 0.4590 0.4514 0.4923 -0.0297 0.1033  -0.0355 228 ILE A CG1 
1787 C CG2 . ILE A 228 ? 0.4026 0.4130 0.4654 -0.0306 0.1005  -0.0347 228 ILE A CG2 
1788 C CD1 . ILE A 228 ? 0.4114 0.4041 0.4449 -0.0321 0.0931  -0.0385 228 ILE A CD1 
1789 N N   . ILE A 229 ? 0.3569 0.3720 0.4335 -0.0199 0.1261  -0.0318 229 ILE A N   
1790 C CA  . ILE A 229 ? 0.3873 0.4075 0.4764 -0.0142 0.1305  -0.0324 229 ILE A CA  
1791 C C   . ILE A 229 ? 0.3989 0.4342 0.5128 -0.0173 0.1215  -0.0308 229 ILE A C   
1792 O O   . ILE A 229 ? 0.4008 0.4479 0.5332 -0.0228 0.1208  -0.0279 229 ILE A O   
1793 C CB  . ILE A 229 ? 0.3994 0.4205 0.4945 -0.0112 0.1471  -0.0305 229 ILE A CB  
1794 C CG1 . ILE A 229 ? 0.3983 0.3992 0.4615 -0.0067 0.1556  -0.0320 229 ILE A CG1 
1795 C CG2 . ILE A 229 ? 0.4006 0.4289 0.5132 -0.0050 0.1522  -0.0311 229 ILE A CG2 
1796 C CD1 . ILE A 229 ? 0.4904 0.4883 0.5548 -0.0046 0.1748  -0.0293 229 ILE A CD1 
1797 N N   . SER A 230 ? 0.3672 0.4006 0.4806 -0.0137 0.1142  -0.0327 230 SER A N   
1798 C CA  . SER A 230 ? 0.3656 0.4084 0.4953 -0.0160 0.1036  -0.0308 230 SER A CA  
1799 C C   . SER A 230 ? 0.3930 0.4375 0.5334 -0.0084 0.1041  -0.0311 230 SER A C   
1800 O O   . SER A 230 ? 0.4075 0.4407 0.5342 -0.0030 0.1069  -0.0343 230 SER A O   
1801 C CB  . SER A 230 ? 0.3974 0.4325 0.5126 -0.0205 0.0929  -0.0318 230 SER A CB  
1802 O OG  . SER A 230 ? 0.4325 0.4727 0.5578 -0.0225 0.0832  -0.0295 230 SER A OG  
1803 N N   . PHE A 231 ? 0.3618 0.4200 0.5269 -0.0076 0.1004  -0.0283 231 PHE A N   
1804 C CA  . PHE A 231 ? 0.3787 0.4404 0.5587 0.0010  0.1021  -0.0281 231 PHE A CA  
1805 C C   . PHE A 231 ? 0.4517 0.5198 0.6454 0.0011  0.0878  -0.0253 231 PHE A C   
1806 O O   . PHE A 231 ? 0.4155 0.4945 0.6225 -0.0044 0.0804  -0.0230 231 PHE A O   
1807 C CB  . PHE A 231 ? 0.4215 0.4953 0.6242 0.0046  0.1153  -0.0275 231 PHE A CB  
1808 C CG  . PHE A 231 ? 0.4391 0.5157 0.6575 0.0149  0.1195  -0.0280 231 PHE A CG  
1809 C CD1 . PHE A 231 ? 0.4278 0.4904 0.6298 0.0221  0.1303  -0.0314 231 PHE A CD1 
1810 C CD2 . PHE A 231 ? 0.4245 0.5166 0.6735 0.0179  0.1120  -0.0255 231 PHE A CD2 
1811 C CE1 . PHE A 231 ? 0.4431 0.5064 0.6586 0.0321  0.1352  -0.0322 231 PHE A CE1 
1812 C CE2 . PHE A 231 ? 0.4498 0.5443 0.7146 0.0284  0.1159  -0.0259 231 PHE A CE2 
1813 C CZ  . PHE A 231 ? 0.4754 0.5553 0.7236 0.0355  0.1285  -0.0292 231 PHE A CZ  
1814 N N   . GLY A 232 ? 0.4084 0.4675 0.5967 0.0074  0.0835  -0.0254 232 GLY A N   
1815 C CA  . GLY A 232 ? 0.4449 0.5085 0.6472 0.0110  0.0716  -0.0222 232 GLY A CA  
1816 C C   . GLY A 232 ? 0.4894 0.5418 0.6736 0.0065  0.0583  -0.0201 232 GLY A C   
1817 O O   . GLY A 232 ? 0.4968 0.5465 0.6851 0.0112  0.0484  -0.0172 232 GLY A O   
1818 N N   . SER A 233 ? 0.4659 0.5104 0.6298 -0.0017 0.0583  -0.0214 233 SER A N   
1819 C CA  . SER A 233 ? 0.4632 0.4958 0.6090 -0.0063 0.0484  -0.0195 233 SER A CA  
1820 C C   . SER A 233 ? 0.5025 0.5183 0.6257 -0.0083 0.0533  -0.0222 233 SER A C   
1821 O O   . SER A 233 ? 0.4761 0.4914 0.5943 -0.0099 0.0616  -0.0260 233 SER A O   
1822 C CB  . SER A 233 ? 0.4790 0.5172 0.6233 -0.0150 0.0433  -0.0189 233 SER A CB  
1823 O OG  . SER A 233 ? 0.4837 0.5072 0.6054 -0.0198 0.0375  -0.0179 233 SER A OG  
1824 N N   . GLY A 234 ? 0.5258 0.5270 0.6354 -0.0082 0.0478  -0.0202 234 GLY A N   
1825 C CA  . GLY A 234 ? 0.4698 0.4555 0.5615 -0.0115 0.0521  -0.0227 234 GLY A CA  
1826 C C   . GLY A 234 ? 0.5007 0.4793 0.5775 -0.0198 0.0499  -0.0220 234 GLY A C   
1827 O O   . GLY A 234 ? 0.5179 0.4875 0.5848 -0.0239 0.0550  -0.0249 234 GLY A O   
1828 N N   . TYR A 235 ? 0.4949 0.4772 0.5710 -0.0223 0.0425  -0.0186 235 TYR A N   
1829 C CA  . TYR A 235 ? 0.5107 0.4836 0.5699 -0.0296 0.0412  -0.0181 235 TYR A CA  
1830 C C   . TYR A 235 ? 0.5059 0.4835 0.5645 -0.0353 0.0485  -0.0225 235 TYR A C   
1831 O O   . TYR A 235 ? 0.4988 0.4897 0.5691 -0.0350 0.0508  -0.0245 235 TYR A O   
1832 C CB  . TYR A 235 ? 0.5386 0.5146 0.5966 -0.0312 0.0308  -0.0149 235 TYR A CB  
1833 C CG  . TYR A 235 ? 0.6006 0.5674 0.6404 -0.0390 0.0311  -0.0155 235 TYR A CG  
1834 C CD1 . TYR A 235 ? 0.5685 0.5145 0.5851 -0.0407 0.0315  -0.0133 235 TYR A CD1 
1835 C CD2 . TYR A 235 ? 0.5776 0.5545 0.6225 -0.0442 0.0325  -0.0181 235 TYR A CD2 
1836 C CE1 . TYR A 235 ? 0.5922 0.5283 0.5914 -0.0473 0.0339  -0.0142 235 TYR A CE1 
1837 C CE2 . TYR A 235 ? 0.5560 0.5232 0.5841 -0.0506 0.0336  -0.0191 235 TYR A CE2 
1838 C CZ  . TYR A 235 ? 0.5828 0.5300 0.5884 -0.0520 0.0346  -0.0173 235 TYR A CZ  
1839 O OH  . TYR A 235 ? 0.5702 0.5066 0.5585 -0.0578 0.0376  -0.0186 235 TYR A OH  
1840 N N   . GLY A 236 ? 0.4494 0.4151 0.4943 -0.0402 0.0525  -0.0237 236 GLY A N   
1841 C CA  . GLY A 236 ? 0.5013 0.4699 0.5475 -0.0439 0.0593  -0.0284 236 GLY A CA  
1842 C C   . GLY A 236 ? 0.4833 0.4638 0.5350 -0.0462 0.0590  -0.0297 236 GLY A C   
1843 O O   . GLY A 236 ? 0.5073 0.4941 0.5646 -0.0454 0.0629  -0.0331 236 GLY A O   
1844 N N   . GLY A 237 ? 0.4779 0.4597 0.5263 -0.0490 0.0540  -0.0272 237 GLY A N   
1845 C CA  . GLY A 237 ? 0.4608 0.4521 0.5146 -0.0519 0.0542  -0.0283 237 GLY A CA  
1846 C C   . GLY A 237 ? 0.4695 0.4743 0.5391 -0.0483 0.0558  -0.0285 237 GLY A C   
1847 O O   . GLY A 237 ? 0.4728 0.4829 0.5455 -0.0501 0.0596  -0.0299 237 GLY A O   
1848 N N   . ASN A 238 ? 0.4456 0.4544 0.5245 -0.0428 0.0540  -0.0269 238 ASN A N   
1849 C CA  . ASN A 238 ? 0.4604 0.4808 0.5548 -0.0386 0.0578  -0.0271 238 ASN A CA  
1850 C C   . ASN A 238 ? 0.4745 0.4916 0.5666 -0.0336 0.0648  -0.0300 238 ASN A C   
1851 O O   . ASN A 238 ? 0.4332 0.4565 0.5323 -0.0305 0.0708  -0.0308 238 ASN A O   
1852 C CB  . ASN A 238 ? 0.4552 0.4831 0.5646 -0.0344 0.0520  -0.0240 238 ASN A CB  
1853 C CG  . ASN A 238 ? 0.4798 0.5107 0.5920 -0.0386 0.0419  -0.0217 238 ASN A CG  
1854 O OD1 . ASN A 238 ? 0.4530 0.4857 0.5630 -0.0450 0.0415  -0.0226 238 ASN A OD1 
1855 N ND2 . ASN A 238 ? 0.4883 0.5181 0.6041 -0.0348 0.0328  -0.0190 238 ASN A ND2 
1856 N N   . SER A 239 ? 0.4159 0.4221 0.4980 -0.0329 0.0646  -0.0317 239 SER A N   
1857 C CA  . SER A 239 ? 0.4161 0.4177 0.4964 -0.0281 0.0690  -0.0352 239 SER A CA  
1858 C C   . SER A 239 ? 0.4554 0.4503 0.5262 -0.0307 0.0709  -0.0398 239 SER A C   
1859 O O   . SER A 239 ? 0.4189 0.4108 0.4869 -0.0270 0.0735  -0.0438 239 SER A O   
1860 C CB  . SER A 239 ? 0.4292 0.4231 0.5097 -0.0242 0.0667  -0.0342 239 SER A CB  
1861 O OG  . SER A 239 ? 0.4615 0.4447 0.5325 -0.0287 0.0644  -0.0338 239 SER A OG  
1862 N N   . LEU A 240 ? 0.4289 0.4209 0.4948 -0.0365 0.0692  -0.0398 240 LEU A N   
1863 C CA  . LEU A 240 ? 0.4562 0.4446 0.5181 -0.0388 0.0704  -0.0443 240 LEU A CA  
1864 C C   . LEU A 240 ? 0.4090 0.4032 0.4694 -0.0395 0.0715  -0.0444 240 LEU A C   
1865 O O   . LEU A 240 ? 0.4609 0.4563 0.5198 -0.0438 0.0711  -0.0427 240 LEU A O   
1866 C CB  . LEU A 240 ? 0.5021 0.4839 0.5612 -0.0442 0.0704  -0.0443 240 LEU A CB  
1867 C CG  . LEU A 240 ? 0.4698 0.4426 0.5270 -0.0444 0.0704  -0.0422 240 LEU A CG  
1868 C CD1 . LEU A 240 ? 0.4571 0.4213 0.5099 -0.0501 0.0735  -0.0425 240 LEU A CD1 
1869 C CD2 . LEU A 240 ? 0.4256 0.3942 0.4861 -0.0403 0.0709  -0.0452 240 LEU A CD2 
1870 N N   . LEU A 241 ? 0.4262 0.4216 0.4849 -0.0348 0.0735  -0.0461 241 LEU A N   
1871 C CA  . LEU A 241 ? 0.4049 0.4037 0.4608 -0.0346 0.0762  -0.0447 241 LEU A CA  
1872 C C   . LEU A 241 ? 0.4214 0.4169 0.4712 -0.0365 0.0747  -0.0470 241 LEU A C   
1873 O O   . LEU A 241 ? 0.4345 0.4310 0.4812 -0.0375 0.0768  -0.0450 241 LEU A O   
1874 C CB  . LEU A 241 ? 0.3881 0.3856 0.4404 -0.0285 0.0807  -0.0453 241 LEU A CB  
1875 C CG  . LEU A 241 ? 0.3969 0.3992 0.4588 -0.0257 0.0833  -0.0429 241 LEU A CG  
1876 C CD1 . LEU A 241 ? 0.3590 0.3596 0.4174 -0.0195 0.0909  -0.0434 241 LEU A CD1 
1877 C CD2 . LEU A 241 ? 0.3971 0.4088 0.4710 -0.0301 0.0819  -0.0381 241 LEU A CD2 
1878 N N   . GLY A 242 ? 0.4423 0.4341 0.4924 -0.0370 0.0714  -0.0513 242 GLY A N   
1879 C CA  . GLY A 242 ? 0.4201 0.4105 0.4686 -0.0381 0.0696  -0.0536 242 GLY A CA  
1880 C C   . GLY A 242 ? 0.4358 0.4278 0.4864 -0.0436 0.0712  -0.0509 242 GLY A C   
1881 O O   . GLY A 242 ? 0.4914 0.4821 0.5399 -0.0438 0.0710  -0.0517 242 GLY A O   
1882 N N   . LYS A 243 ? 0.4226 0.4156 0.4754 -0.0473 0.0723  -0.0478 243 LYS A N   
1883 C CA  . LYS A 243 ? 0.4384 0.4291 0.4898 -0.0526 0.0734  -0.0463 243 LYS A CA  
1884 C C   . LYS A 243 ? 0.4249 0.4171 0.4728 -0.0551 0.0736  -0.0431 243 LYS A C   
1885 O O   . LYS A 243 ? 0.4885 0.4792 0.5337 -0.0553 0.0749  -0.0438 243 LYS A O   
1886 C CB  . LYS A 243 ? 0.3889 0.3759 0.4398 -0.0549 0.0733  -0.0446 243 LYS A CB  
1887 C CG  . LYS A 243 ? 0.4124 0.3927 0.4565 -0.0601 0.0751  -0.0434 243 LYS A CG  
1888 C CD  . LYS A 243 ? 0.3671 0.3389 0.4069 -0.0617 0.0764  -0.0420 243 LYS A CD  
1889 C CE  . LYS A 243 ? 0.3687 0.3300 0.3958 -0.0663 0.0789  -0.0404 243 LYS A CE  
1890 N NZ  . LYS A 243 ? 0.4052 0.3631 0.4336 -0.0686 0.0859  -0.0439 243 LYS A NZ  
1891 N N   . LYS A 244 ? 0.4092 0.4037 0.4581 -0.0570 0.0718  -0.0397 244 LYS A N   
1892 C CA  . LYS A 244 ? 0.3560 0.3527 0.4049 -0.0604 0.0711  -0.0373 244 LYS A CA  
1893 C C   . LYS A 244 ? 0.3882 0.3898 0.4413 -0.0579 0.0743  -0.0364 244 LYS A C   
1894 O O   . LYS A 244 ? 0.3691 0.3688 0.4197 -0.0600 0.0765  -0.0358 244 LYS A O   
1895 C CB  . LYS A 244 ? 0.3479 0.3467 0.3995 -0.0626 0.0662  -0.0345 244 LYS A CB  
1896 C CG  . LYS A 244 ? 0.4172 0.4069 0.4593 -0.0646 0.0638  -0.0346 244 LYS A CG  
1897 C CD  . LYS A 244 ? 0.4122 0.3932 0.4436 -0.0692 0.0655  -0.0361 244 LYS A CD  
1898 C CE  . LYS A 244 ? 0.4052 0.3736 0.4230 -0.0714 0.0654  -0.0359 244 LYS A CE  
1899 N NZ  . LYS A 244 ? 0.3890 0.3476 0.3952 -0.0756 0.0686  -0.0379 244 LYS A NZ  
1900 N N   . CYS A 245 ? 0.3765 0.3823 0.4343 -0.0532 0.0756  -0.0361 245 CYS A N   
1901 C CA  . CYS A 245 ? 0.3867 0.3953 0.4468 -0.0507 0.0808  -0.0347 245 CYS A CA  
1902 C C   . CYS A 245 ? 0.3768 0.3777 0.4253 -0.0481 0.0838  -0.0362 245 CYS A C   
1903 O O   . CYS A 245 ? 0.4332 0.4316 0.4788 -0.0494 0.0880  -0.0342 245 CYS A O   
1904 C CB  . CYS A 245 ? 0.3890 0.4015 0.4544 -0.0453 0.0827  -0.0347 245 CYS A CB  
1905 S SG  . CYS A 245 ? 0.4020 0.4236 0.4829 -0.0464 0.0784  -0.0321 245 CYS A SG  
1906 N N   . PHE A 246 ? 0.4223 0.4187 0.4649 -0.0445 0.0809  -0.0397 246 PHE A N   
1907 C CA  . PHE A 246 ? 0.4247 0.4136 0.4568 -0.0406 0.0807  -0.0418 246 PHE A CA  
1908 C C   . PHE A 246 ? 0.4373 0.4232 0.4684 -0.0438 0.0789  -0.0424 246 PHE A C   
1909 O O   . PHE A 246 ? 0.4752 0.4558 0.4997 -0.0439 0.0813  -0.0406 246 PHE A O   
1910 C CB  . PHE A 246 ? 0.4138 0.4006 0.4440 -0.0356 0.0766  -0.0463 246 PHE A CB  
1911 C CG  . PHE A 246 ? 0.5122 0.4916 0.5329 -0.0305 0.0725  -0.0499 246 PHE A CG  
1912 C CD1 . PHE A 246 ? 0.5017 0.4764 0.5167 -0.0301 0.0719  -0.0490 246 PHE A CD1 
1913 C CD2 . PHE A 246 ? 0.5448 0.5211 0.5625 -0.0257 0.0678  -0.0546 246 PHE A CD2 
1914 C CE1 . PHE A 246 ? 0.5774 0.5453 0.5847 -0.0241 0.0658  -0.0524 246 PHE A CE1 
1915 C CE2 . PHE A 246 ? 0.5649 0.5345 0.5747 -0.0206 0.0611  -0.0586 246 PHE A CE2 
1916 C CZ  . PHE A 246 ? 0.5825 0.5482 0.5873 -0.0193 0.0597  -0.0573 246 PHE A CZ  
1917 N N   . ALA A 247 ? 0.4484 0.4359 0.4852 -0.0464 0.0761  -0.0449 247 ALA A N   
1918 C CA  . ALA A 247 ? 0.4386 0.4224 0.4749 -0.0475 0.0756  -0.0467 247 ALA A CA  
1919 C C   . ALA A 247 ? 0.4171 0.3980 0.4506 -0.0529 0.0783  -0.0441 247 ALA A C   
1920 O O   . ALA A 247 ? 0.4481 0.4239 0.4793 -0.0530 0.0791  -0.0454 247 ALA A O   
1921 C CB  . ALA A 247 ? 0.4227 0.4082 0.4669 -0.0488 0.0743  -0.0504 247 ALA A CB  
1922 N N   . LEU A 248 ? 0.4087 0.3926 0.4436 -0.0572 0.0792  -0.0410 248 LEU A N   
1923 C CA  . LEU A 248 ? 0.4056 0.3861 0.4380 -0.0627 0.0805  -0.0391 248 LEU A CA  
1924 C C   . LEU A 248 ? 0.4449 0.4265 0.4783 -0.0632 0.0837  -0.0359 248 LEU A C   
1925 O O   . LEU A 248 ? 0.4521 0.4267 0.4800 -0.0641 0.0867  -0.0349 248 LEU A O   
1926 C CB  . LEU A 248 ? 0.3961 0.3778 0.4300 -0.0683 0.0776  -0.0388 248 LEU A CB  
1927 C CG  . LEU A 248 ? 0.4154 0.3910 0.4440 -0.0692 0.0776  -0.0414 248 LEU A CG  
1928 C CD1 . LEU A 248 ? 0.4501 0.4229 0.4742 -0.0738 0.0743  -0.0405 248 LEU A CD1 
1929 C CD2 . LEU A 248 ? 0.4366 0.4040 0.4596 -0.0697 0.0808  -0.0434 248 LEU A CD2 
1930 N N   . ARG A 249 ? 0.3945 0.3840 0.4354 -0.0626 0.0843  -0.0341 249 ARG A N   
1931 C CA  . ARG A 249 ? 0.4212 0.4125 0.4670 -0.0648 0.0894  -0.0309 249 ARG A CA  
1932 C C   . ARG A 249 ? 0.4565 0.4399 0.4918 -0.0595 0.0957  -0.0296 249 ARG A C   
1933 O O   . ARG A 249 ? 0.4586 0.4345 0.4890 -0.0617 0.1004  -0.0276 249 ARG A O   
1934 C CB  . ARG A 249 ? 0.4102 0.4133 0.4704 -0.0652 0.0892  -0.0296 249 ARG A CB  
1935 C CG  . ARG A 249 ? 0.4410 0.4496 0.5094 -0.0702 0.0814  -0.0301 249 ARG A CG  
1936 C CD  . ARG A 249 ? 0.3956 0.4164 0.4829 -0.0719 0.0803  -0.0283 249 ARG A CD  
1937 N NE  . ARG A 249 ? 0.4589 0.4830 0.5500 -0.0740 0.0703  -0.0289 249 ARG A NE  
1938 C CZ  . ARG A 249 ? 0.4587 0.4841 0.5486 -0.0695 0.0663  -0.0290 249 ARG A CZ  
1939 N NH1 . ARG A 249 ? 0.3894 0.4152 0.4778 -0.0631 0.0711  -0.0291 249 ARG A NH1 
1940 N NH2 . ARG A 249 ? 0.4535 0.4774 0.5415 -0.0715 0.0571  -0.0290 249 ARG A NH2 
1941 N N   . ILE A 250 ? 0.4727 0.4553 0.5023 -0.0525 0.0956  -0.0309 250 ILE A N   
1942 C CA  . ILE A 250 ? 0.4962 0.4677 0.5106 -0.0465 0.1000  -0.0299 250 ILE A CA  
1943 C C   . ILE A 250 ? 0.4949 0.4561 0.4982 -0.0446 0.0964  -0.0310 250 ILE A C   
1944 O O   . ILE A 250 ? 0.4682 0.4176 0.4592 -0.0428 0.1005  -0.0284 250 ILE A O   
1945 C CB  . ILE A 250 ? 0.4667 0.4378 0.4753 -0.0392 0.0988  -0.0321 250 ILE A CB  
1946 C CG1 . ILE A 250 ? 0.4778 0.4573 0.4970 -0.0398 0.1046  -0.0304 250 ILE A CG1 
1947 C CG2 . ILE A 250 ? 0.5383 0.4944 0.5255 -0.0319 0.1003  -0.0319 250 ILE A CG2 
1948 C CD1 . ILE A 250 ? 0.5052 0.4807 0.5223 -0.0404 0.1164  -0.0261 250 ILE A CD1 
1949 N N   . ALA A 251 ? 0.4884 0.4529 0.4960 -0.0444 0.0893  -0.0349 251 ALA A N   
1950 C CA  . ALA A 251 ? 0.4980 0.4546 0.4992 -0.0414 0.0859  -0.0367 251 ALA A CA  
1951 C C   . ALA A 251 ? 0.4744 0.4243 0.4735 -0.0462 0.0895  -0.0344 251 ALA A C   
1952 O O   . ALA A 251 ? 0.4883 0.4272 0.4778 -0.0423 0.0894  -0.0339 251 ALA A O   
1953 C CB  . ALA A 251 ? 0.4373 0.4002 0.4481 -0.0411 0.0800  -0.0415 251 ALA A CB  
1954 N N   . SER A 252 ? 0.4503 0.4053 0.4577 -0.0543 0.0919  -0.0332 252 SER A N   
1955 C CA  . SER A 252 ? 0.4548 0.4014 0.4592 -0.0594 0.0948  -0.0320 252 SER A CA  
1956 C C   . SER A 252 ? 0.5052 0.4410 0.5002 -0.0583 0.1013  -0.0277 252 SER A C   
1957 O O   . SER A 252 ? 0.4781 0.4014 0.4649 -0.0585 0.1034  -0.0267 252 SER A O   
1958 C CB  . SER A 252 ? 0.4449 0.3979 0.4591 -0.0685 0.0939  -0.0323 252 SER A CB  
1959 O OG  . SER A 252 ? 0.4569 0.4177 0.4801 -0.0718 0.0965  -0.0297 252 SER A OG  
1960 N N   . ARG A 253 ? 0.4917 0.4300 0.4862 -0.0566 0.1058  -0.0250 253 ARG A N   
1961 C CA  . ARG A 253 ? 0.5211 0.4461 0.5034 -0.0551 0.1144  -0.0204 253 ARG A CA  
1962 C C   . ARG A 253 ? 0.5498 0.4601 0.5116 -0.0448 0.1117  -0.0201 253 ARG A C   
1963 O O   . ARG A 253 ? 0.6269 0.5207 0.5749 -0.0431 0.1153  -0.0171 253 ARG A O   
1964 C CB  . ARG A 253 ? 0.5615 0.4923 0.5491 -0.0560 0.1222  -0.0177 253 ARG A CB  
1965 C CG  . ARG A 253 ? 0.6337 0.5474 0.6054 -0.0542 0.1337  -0.0125 253 ARG A CG  
1966 C CD  . ARG A 253 ? 0.6789 0.5996 0.6646 -0.0600 0.1450  -0.0097 253 ARG A CD  
1967 N NE  . ARG A 253 ? 0.7428 0.6481 0.7095 -0.0546 0.1571  -0.0053 253 ARG A NE  
1968 C CZ  . ARG A 253 ? 0.7176 0.6239 0.6932 -0.0587 0.1714  -0.0018 253 ARG A CZ  
1969 N NH1 . ARG A 253 ? 0.7349 0.6585 0.7410 -0.0686 0.1740  -0.0024 253 ARG A NH1 
1970 N NH2 . ARG A 253 ? 0.8411 0.7300 0.7943 -0.0527 0.1836  0.0021  253 ARG A NH2 
1971 N N   . LEU A 254 ? 0.5771 0.4922 0.5366 -0.0378 0.1046  -0.0234 254 LEU A N   
1972 C CA  . LEU A 254 ? 0.5928 0.4957 0.5355 -0.0276 0.0983  -0.0245 254 LEU A CA  
1973 C C   . LEU A 254 ? 0.6203 0.5173 0.5638 -0.0268 0.0941  -0.0257 254 LEU A C   
1974 O O   . LEU A 254 ? 0.6661 0.5470 0.5934 -0.0199 0.0924  -0.0237 254 LEU A O   
1975 C CB  . LEU A 254 ? 0.6135 0.5255 0.5602 -0.0222 0.0893  -0.0296 254 LEU A CB  
1976 C CG  . LEU A 254 ? 0.6592 0.5750 0.6033 -0.0212 0.0929  -0.0294 254 LEU A CG  
1977 C CD1 . LEU A 254 ? 0.6560 0.5768 0.6015 -0.0154 0.0827  -0.0352 254 LEU A CD1 
1978 C CD2 . LEU A 254 ? 0.6823 0.5803 0.6031 -0.0170 0.1013  -0.0244 254 LEU A CD2 
1979 N N   . ALA A 255 ? 0.5813 0.4895 0.5420 -0.0332 0.0925  -0.0288 255 ALA A N   
1980 C CA  . ALA A 255 ? 0.5552 0.4579 0.5178 -0.0325 0.0901  -0.0306 255 ALA A CA  
1981 C C   . ALA A 255 ? 0.6285 0.5149 0.5801 -0.0352 0.0970  -0.0262 255 ALA A C   
1982 O O   . ALA A 255 ? 0.6086 0.4819 0.5518 -0.0296 0.0953  -0.0257 255 ALA A O   
1983 C CB  . ALA A 255 ? 0.5427 0.4581 0.5220 -0.0392 0.0892  -0.0347 255 ALA A CB  
1984 N N   . LYS A 256 ? 0.5932 0.4802 0.5468 -0.0439 0.1047  -0.0230 256 LYS A N   
1985 C CA  . LYS A 256 ? 0.5999 0.4705 0.5441 -0.0477 0.1125  -0.0187 256 LYS A CA  
1986 C C   . LYS A 256 ? 0.6227 0.4742 0.5447 -0.0384 0.1147  -0.0140 256 LYS A C   
1987 O O   . LYS A 256 ? 0.6666 0.5000 0.5764 -0.0354 0.1161  -0.0118 256 LYS A O   
1988 C CB  . LYS A 256 ? 0.5770 0.4543 0.5317 -0.0585 0.1201  -0.0165 256 LYS A CB  
1989 C CG  . LYS A 256 ? 0.6605 0.5207 0.6073 -0.0634 0.1301  -0.0116 256 LYS A CG  
1990 C CD  . LYS A 256 ? 0.6091 0.4584 0.5548 -0.0674 0.1289  -0.0135 256 LYS A CD  
1991 C CE  . LYS A 256 ? 0.7490 0.5766 0.6836 -0.0709 0.1391  -0.0084 256 LYS A CE  
1992 N NZ  . LYS A 256 ? 0.8204 0.6508 0.7607 -0.0770 0.1494  -0.0041 256 LYS A NZ  
1993 N N   . GLU A 257 ? 0.6482 0.5012 0.5622 -0.0330 0.1147  -0.0127 257 GLU A N   
1994 C CA  . GLU A 257 ? 0.7163 0.5480 0.6035 -0.0236 0.1166  -0.0081 257 GLU A CA  
1995 C C   . GLU A 257 ? 0.7245 0.5473 0.6011 -0.0118 0.1046  -0.0102 257 GLU A C   
1996 O O   . GLU A 257 ? 0.7592 0.5591 0.6121 -0.0041 0.1049  -0.0059 257 GLU A O   
1997 C CB  . GLU A 257 ? 0.7624 0.5969 0.6416 -0.0203 0.1191  -0.0072 257 GLU A CB  
1998 C CG  . GLU A 257 ? 0.7800 0.6241 0.6715 -0.0299 0.1315  -0.0050 257 GLU A CG  
1999 C CD  . GLU A 257 ? 0.8715 0.7227 0.7600 -0.0255 0.1318  -0.0064 257 GLU A CD  
2000 O OE1 . GLU A 257 ? 0.9258 0.7673 0.7946 -0.0149 0.1243  -0.0078 257 GLU A OE1 
2001 O OE2 . GLU A 257 ? 0.8882 0.7544 0.7946 -0.0322 0.1385  -0.0066 257 GLU A OE2 
2002 N N   . GLU A 258 ? 0.6897 0.5295 0.5837 -0.0098 0.0939  -0.0167 258 GLU A N   
2003 C CA  . GLU A 258 ? 0.6818 0.5176 0.5719 0.0019  0.0813  -0.0199 258 GLU A CA  
2004 C C   . GLU A 258 ? 0.6826 0.5210 0.5874 0.0019  0.0782  -0.0230 258 GLU A C   
2005 O O   . GLU A 258 ? 0.7239 0.5600 0.6301 0.0119  0.0679  -0.0258 258 GLU A O   
2006 C CB  . GLU A 258 ? 0.7137 0.5657 0.6138 0.0056  0.0714  -0.0257 258 GLU A CB  
2007 C CG  . GLU A 258 ? 0.7242 0.5715 0.6073 0.0078  0.0732  -0.0238 258 GLU A CG  
2008 C CD  . GLU A 258 ? 0.7617 0.6271 0.6593 0.0081  0.0655  -0.0301 258 GLU A CD  
2009 O OE1 . GLU A 258 ? 0.7923 0.6712 0.7105 0.0087  0.0571  -0.0358 258 GLU A OE1 
2010 O OE2 . GLU A 258 ? 0.8422 0.7076 0.7313 0.0077  0.0690  -0.0295 258 GLU A OE2 
2011 N N   . GLY A 259 ? 0.6859 0.5286 0.6021 -0.0085 0.0863  -0.0231 259 GLY A N   
2012 C CA  . GLY A 259 ? 0.6811 0.5216 0.6066 -0.0083 0.0857  -0.0259 259 GLY A CA  
2013 C C   . GLY A 259 ? 0.6811 0.5411 0.6301 -0.0100 0.0818  -0.0329 259 GLY A C   
2014 O O   . GLY A 259 ? 0.7268 0.5856 0.6841 -0.0045 0.0787  -0.0362 259 GLY A O   
2015 N N   . TRP A 260 ? 0.6049 0.4817 0.5650 -0.0172 0.0827  -0.0351 260 TRP A N   
2016 C CA  . TRP A 260 ? 0.5774 0.4696 0.5571 -0.0202 0.0815  -0.0409 260 TRP A CA  
2017 C C   . TRP A 260 ? 0.5314 0.4303 0.5145 -0.0323 0.0877  -0.0406 260 TRP A C   
2018 O O   . TRP A 260 ? 0.5718 0.4634 0.5464 -0.0385 0.0927  -0.0369 260 TRP A O   
2019 C CB  . TRP A 260 ? 0.5797 0.4853 0.5709 -0.0142 0.0731  -0.0448 260 TRP A CB  
2020 C CG  . TRP A 260 ? 0.6294 0.5385 0.6128 -0.0133 0.0699  -0.0430 260 TRP A CG  
2021 C CD1 . TRP A 260 ? 0.6415 0.5387 0.6062 -0.0065 0.0667  -0.0395 260 TRP A CD1 
2022 C CD2 . TRP A 260 ? 0.5539 0.4771 0.5462 -0.0183 0.0698  -0.0449 260 TRP A CD2 
2023 N NE1 . TRP A 260 ? 0.5991 0.5024 0.5606 -0.0073 0.0655  -0.0395 260 TRP A NE1 
2024 C CE2 . TRP A 260 ? 0.5771 0.4968 0.5565 -0.0144 0.0671  -0.0428 260 TRP A CE2 
2025 C CE3 . TRP A 260 ? 0.5209 0.4568 0.5283 -0.0253 0.0723  -0.0479 260 TRP A CE3 
2026 C CZ2 . TRP A 260 ? 0.5767 0.5064 0.5605 -0.0171 0.0667  -0.0441 260 TRP A CZ2 
2027 C CZ3 . TRP A 260 ? 0.5065 0.4519 0.5177 -0.0280 0.0713  -0.0485 260 TRP A CZ3 
2028 C CH2 . TRP A 260 ? 0.5178 0.4607 0.5184 -0.0238 0.0685  -0.0468 260 TRP A CH2 
2029 N N   . LEU A 261 ? 0.5117 0.4237 0.5079 -0.0356 0.0870  -0.0446 261 LEU A N   
2030 C CA  . LEU A 261 ? 0.4745 0.3911 0.4727 -0.0458 0.0909  -0.0448 261 LEU A CA  
2031 C C   . LEU A 261 ? 0.4832 0.4143 0.4912 -0.0470 0.0882  -0.0467 261 LEU A C   
2032 O O   . LEU A 261 ? 0.5125 0.4499 0.5303 -0.0420 0.0855  -0.0501 261 LEU A O   
2033 C CB  . LEU A 261 ? 0.4483 0.3581 0.4467 -0.0494 0.0952  -0.0480 261 LEU A CB  
2034 C CG  . LEU A 261 ? 0.4807 0.3738 0.4690 -0.0494 0.0988  -0.0469 261 LEU A CG  
2035 C CD1 . LEU A 261 ? 0.5169 0.4032 0.5056 -0.0510 0.1035  -0.0514 261 LEU A CD1 
2036 C CD2 . LEU A 261 ? 0.5020 0.3887 0.4814 -0.0576 0.1007  -0.0433 261 LEU A CD2 
2037 N N   . ALA A 262 ? 0.4477 0.3838 0.4549 -0.0536 0.0888  -0.0447 262 ALA A N   
2038 C CA  . ALA A 262 ? 0.4070 0.3544 0.4218 -0.0553 0.0867  -0.0459 262 ALA A CA  
2039 C C   . ALA A 262 ? 0.4149 0.3617 0.4276 -0.0636 0.0881  -0.0456 262 ALA A C   
2040 O O   . ALA A 262 ? 0.3693 0.3152 0.3792 -0.0684 0.0879  -0.0430 262 ALA A O   
2041 C CB  . ALA A 262 ? 0.4346 0.3884 0.4499 -0.0528 0.0844  -0.0435 262 ALA A CB  
2042 N N   . GLU A 263 ? 0.4230 0.3696 0.4370 -0.0653 0.0894  -0.0484 263 GLU A N   
2043 C CA  . GLU A 263 ? 0.4321 0.3719 0.4378 -0.0722 0.0903  -0.0487 263 GLU A CA  
2044 C C   . GLU A 263 ? 0.4215 0.3641 0.4272 -0.0739 0.0898  -0.0493 263 GLU A C   
2045 O O   . GLU A 263 ? 0.3902 0.3382 0.4038 -0.0704 0.0912  -0.0506 263 GLU A O   
2046 C CB  . GLU A 263 ? 0.4359 0.3630 0.4342 -0.0727 0.0953  -0.0516 263 GLU A CB  
2047 C CG  . GLU A 263 ? 0.4117 0.3322 0.4078 -0.0707 0.0963  -0.0510 263 GLU A CG  
2048 C CD  . GLU A 263 ? 0.4591 0.3761 0.4498 -0.0767 0.0939  -0.0483 263 GLU A CD  
2049 O OE1 . GLU A 263 ? 0.4324 0.3506 0.4205 -0.0831 0.0906  -0.0481 263 GLU A OE1 
2050 O OE2 . GLU A 263 ? 0.4661 0.3787 0.4560 -0.0750 0.0951  -0.0464 263 GLU A OE2 
2051 N N   . HIS A 264 ? 0.3961 0.3332 0.3920 -0.0796 0.0873  -0.0485 264 HIS A N   
2052 C CA  . HIS A 264 ? 0.4215 0.3573 0.4124 -0.0813 0.0860  -0.0480 264 HIS A CA  
2053 C C   . HIS A 264 ? 0.4114 0.3334 0.3902 -0.0824 0.0931  -0.0508 264 HIS A C   
2054 O O   . HIS A 264 ? 0.4110 0.3201 0.3726 -0.0865 0.0922  -0.0512 264 HIS A O   
2055 C CB  . HIS A 264 ? 0.4111 0.3472 0.3970 -0.0857 0.0778  -0.0457 264 HIS A CB  
2056 C CG  . HIS A 264 ? 0.3829 0.3171 0.3627 -0.0860 0.0743  -0.0442 264 HIS A CG  
2057 N ND1 . HIS A 264 ? 0.3844 0.3128 0.3537 -0.0897 0.0660  -0.0431 264 HIS A ND1 
2058 C CD2 . HIS A 264 ? 0.3778 0.3137 0.3601 -0.0830 0.0771  -0.0434 264 HIS A CD2 
2059 C CE1 . HIS A 264 ? 0.4308 0.3564 0.3944 -0.0881 0.0640  -0.0411 264 HIS A CE1 
2060 N NE2 . HIS A 264 ? 0.3723 0.3019 0.3436 -0.0844 0.0716  -0.0412 264 HIS A NE2 
2061 N N   . MET A 265 ? 0.3947 0.3187 0.3830 -0.0785 0.1004  -0.0532 265 MET A N   
2062 C CA  . MET A 265 ? 0.4221 0.3340 0.4034 -0.0788 0.1102  -0.0564 265 MET A CA  
2063 C C   . MET A 265 ? 0.4487 0.3646 0.4416 -0.0767 0.1174  -0.0578 265 MET A C   
2064 O O   . MET A 265 ? 0.4702 0.3999 0.4821 -0.0732 0.1149  -0.0581 265 MET A O   
2065 C CB  . MET A 265 ? 0.4107 0.3201 0.3966 -0.0759 0.1140  -0.0591 265 MET A CB  
2066 C CG  . MET A 265 ? 0.4600 0.3595 0.4321 -0.0792 0.1105  -0.0589 265 MET A CG  
2067 S SD  . MET A 265 ? 0.4713 0.3684 0.4509 -0.0741 0.1141  -0.0610 265 MET A SD  
2068 C CE  . MET A 265 ? 0.5149 0.3984 0.4768 -0.0804 0.1098  -0.0605 265 MET A CE  
2069 N N   . LEU A 266 ? 0.4818 0.3840 0.4627 -0.0790 0.1270  -0.0589 266 LEU A N   
2070 C CA  . LEU A 266 ? 0.4203 0.3244 0.4155 -0.0777 0.1380  -0.0613 266 LEU A CA  
2071 C C   . LEU A 266 ? 0.4318 0.3400 0.4440 -0.0737 0.1447  -0.0658 266 LEU A C   
2072 O O   . LEU A 266 ? 0.4326 0.3354 0.4378 -0.0724 0.1437  -0.0668 266 LEU A O   
2073 C CB  . LEU A 266 ? 0.4325 0.3175 0.4067 -0.0815 0.1486  -0.0606 266 LEU A CB  
2074 C CG  . LEU A 266 ? 0.5032 0.3680 0.4539 -0.0830 0.1564  -0.0626 266 LEU A CG  
2075 C CD1 . LEU A 266 ? 0.4870 0.3492 0.4509 -0.0809 0.1732  -0.0670 266 LEU A CD1 
2076 C CD2 . LEU A 266 ? 0.4925 0.3358 0.4095 -0.0870 0.1571  -0.0598 266 LEU A CD2 
2077 N N   . ILE A 267 ? 0.4161 0.3335 0.4523 -0.0716 0.1515  -0.0686 267 ILE A N   
2078 C CA  . ILE A 267 ? 0.4087 0.3307 0.4657 -0.0673 0.1591  -0.0734 267 ILE A CA  
2079 C C   . ILE A 267 ? 0.4302 0.3480 0.4971 -0.0696 0.1755  -0.0758 267 ILE A C   
2080 O O   . ILE A 267 ? 0.4732 0.3978 0.5527 -0.0718 0.1765  -0.0755 267 ILE A O   
2081 C CB  . ILE A 267 ? 0.4217 0.3632 0.5066 -0.0614 0.1488  -0.0755 267 ILE A CB  
2082 C CG1 . ILE A 267 ? 0.4326 0.3764 0.5059 -0.0593 0.1345  -0.0722 267 ILE A CG1 
2083 C CG2 . ILE A 267 ? 0.4334 0.3796 0.5409 -0.0558 0.1547  -0.0804 267 ILE A CG2 
2084 C CD1 . ILE A 267 ? 0.4084 0.3680 0.5003 -0.0546 0.1230  -0.0730 267 ILE A CD1 
2085 N N   . LEU A 268 ? 0.4223 0.3274 0.4831 -0.0693 0.1896  -0.0783 268 LEU A N   
2086 C CA  . LEU A 268 ? 0.4533 0.3534 0.5250 -0.0713 0.2087  -0.0809 268 LEU A CA  
2087 C C   . LEU A 268 ? 0.4697 0.3750 0.5663 -0.0661 0.2188  -0.0864 268 LEU A C   
2088 O O   . LEU A 268 ? 0.5016 0.4053 0.5941 -0.0614 0.2137  -0.0876 268 LEU A O   
2089 C CB  . LEU A 268 ? 0.4725 0.3457 0.5057 -0.0767 0.2206  -0.0780 268 LEU A CB  
2090 C CG  . LEU A 268 ? 0.5431 0.3932 0.5408 -0.0769 0.2244  -0.0781 268 LEU A CG  
2091 C CD1 . LEU A 268 ? 0.5309 0.3734 0.5374 -0.0741 0.2439  -0.0831 268 LEU A CD1 
2092 C CD2 . LEU A 268 ? 0.5733 0.3990 0.5286 -0.0822 0.2259  -0.0739 268 LEU A CD2 
2093 N N   . GLY A 269 ? 0.4655 0.3770 0.5900 -0.0667 0.2336  -0.0899 269 GLY A N   
2094 C CA  . GLY A 269 ? 0.4563 0.3713 0.6064 -0.0619 0.2474  -0.0955 269 GLY A CA  
2095 C C   . GLY A 269 ? 0.5085 0.4018 0.6419 -0.0662 0.2729  -0.0958 269 GLY A C   
2096 O O   . GLY A 269 ? 0.5147 0.4012 0.6415 -0.0725 0.2819  -0.0935 269 GLY A O   
2097 N N   . ILE A 270 ? 0.4778 0.3576 0.6015 -0.0626 0.2852  -0.0986 270 ILE A N   
2098 C CA  . ILE A 270 ? 0.5262 0.3817 0.6298 -0.0658 0.3113  -0.0994 270 ILE A CA  
2099 C C   . ILE A 270 ? 0.5464 0.4098 0.6874 -0.0600 0.3294  -0.1059 270 ILE A C   
2100 O O   . ILE A 270 ? 0.5451 0.4162 0.6995 -0.0525 0.3222  -0.1090 270 ILE A O   
2101 C CB  . ILE A 270 ? 0.5873 0.4114 0.6330 -0.0676 0.3105  -0.0966 270 ILE A CB  
2102 C CG1 . ILE A 270 ? 0.6350 0.4293 0.6537 -0.0700 0.3383  -0.0977 270 ILE A CG1 
2103 C CG2 . ILE A 270 ? 0.5874 0.4129 0.6292 -0.0616 0.2976  -0.0986 270 ILE A CG2 
2104 C CD1 . ILE A 270 ? 0.6365 0.3971 0.5939 -0.0726 0.3357  -0.0953 270 ILE A CD1 
2105 N N   . THR A 271 ? 0.5262 0.3861 0.6829 -0.0632 0.3456  -0.1059 271 THR A N   
2106 C CA  . THR A 271 ? 0.5392 0.4049 0.7312 -0.0586 0.3575  -0.1099 271 THR A CA  
2107 C C   . THR A 271 ? 0.6267 0.4581 0.7827 -0.0607 0.3775  -0.1079 271 THR A C   
2108 O O   . THR A 271 ? 0.5993 0.4078 0.7202 -0.0671 0.3849  -0.1035 271 THR A O   
2109 C CB  . THR A 271 ? 0.5339 0.4231 0.7775 -0.0606 0.3581  -0.1120 271 THR A CB  
2110 O OG1 . THR A 271 ? 0.5668 0.4854 0.8393 -0.0592 0.3380  -0.1138 271 THR A OG1 
2111 C CG2 . THR A 271 ? 0.5507 0.4493 0.8364 -0.0556 0.3689  -0.1167 271 THR A CG2 
2112 N N   . ASN A 272 ? 0.5925 0.4195 0.7571 -0.0547 0.3863  -0.1110 272 ASN A N   
2113 C CA  . ASN A 272 ? 0.6345 0.4277 0.7631 -0.0558 0.4050  -0.1096 272 ASN A CA  
2114 C C   . ASN A 272 ? 0.6775 0.4731 0.8411 -0.0562 0.4238  -0.1112 272 ASN A C   
2115 O O   . ASN A 272 ? 0.6290 0.4536 0.8462 -0.0556 0.4207  -0.1140 272 ASN A O   
2116 C CB  . ASN A 272 ? 0.6440 0.4257 0.7513 -0.0495 0.4029  -0.1118 272 ASN A CB  
2117 C CG  . ASN A 272 ? 0.6392 0.4384 0.7925 -0.0409 0.4076  -0.1166 272 ASN A CG  
2118 O OD1 . ASN A 272 ? 0.6214 0.4476 0.8283 -0.0389 0.4078  -0.1191 272 ASN A OD1 
2119 N ND2 . ASN A 272 ? 0.6568 0.4397 0.7880 -0.0356 0.4101  -0.1183 272 ASN A ND2 
2120 N N   . PRO A 273 ? 0.6950 0.4591 0.8286 -0.0578 0.4437  -0.1097 273 PRO A N   
2121 C CA  . PRO A 273 ? 0.7144 0.4793 0.8816 -0.0586 0.4636  -0.1114 273 PRO A CA  
2122 C C   . PRO A 273 ? 0.7016 0.4926 0.9247 -0.0513 0.4654  -0.1170 273 PRO A C   
2123 O O   . PRO A 273 ? 0.7289 0.5299 0.9933 -0.0520 0.4780  -0.1194 273 PRO A O   
2124 C CB  . PRO A 273 ? 0.7673 0.4884 0.8814 -0.0610 0.4838  -0.1083 273 PRO A CB  
2125 C CG  . PRO A 273 ? 0.7738 0.4720 0.8267 -0.0637 0.4721  -0.1042 273 PRO A CG  
2126 C CD  . PRO A 273 ? 0.7316 0.4558 0.7977 -0.0599 0.4490  -0.1063 273 PRO A CD  
2127 N N   . GLU A 274 ? 0.6850 0.4863 0.9111 -0.0439 0.4532  -0.1193 274 GLU A N   
2128 C CA  . GLU A 274 ? 0.6737 0.4996 0.9518 -0.0353 0.4526  -0.1245 274 GLU A CA  
2129 C C   . GLU A 274 ? 0.6377 0.5047 0.9706 -0.0322 0.4322  -0.1277 274 GLU A C   
2130 O O   . GLU A 274 ? 0.6165 0.5056 0.9910 -0.0235 0.4258  -0.1320 274 GLU A O   
2131 C CB  . GLU A 274 ? 0.6821 0.4961 0.9356 -0.0276 0.4497  -0.1256 274 GLU A CB  
2132 C CG  . GLU A 274 ? 0.7284 0.5006 0.9258 -0.0299 0.4677  -0.1232 274 GLU A CG  
2133 C CD  . GLU A 274 ? 0.7891 0.5509 1.0036 -0.0291 0.4928  -0.1247 274 GLU A CD  
2134 O OE1 . GLU A 274 ? 0.7515 0.5403 1.0254 -0.0260 0.4963  -0.1281 274 GLU A OE1 
2135 O OE2 . GLU A 274 ? 0.8806 0.6062 1.0484 -0.0316 0.5089  -0.1226 274 GLU A OE2 
2136 N N   . GLY A 275 ? 0.6081 0.4844 0.9405 -0.0384 0.4210  -0.1258 275 GLY A N   
2137 C CA  . GLY A 275 ? 0.5828 0.4958 0.9645 -0.0360 0.4012  -0.1291 275 GLY A CA  
2138 C C   . GLY A 275 ? 0.6127 0.5397 0.9906 -0.0293 0.3785  -0.1298 275 GLY A C   
2139 O O   . GLY A 275 ? 0.5932 0.5507 1.0150 -0.0245 0.3613  -0.1334 275 GLY A O   
2140 N N   . LYS A 276 ? 0.5579 0.4622 0.8839 -0.0286 0.3772  -0.1269 276 LYS A N   
2141 C CA  . LYS A 276 ? 0.5475 0.4602 0.8651 -0.0225 0.3576  -0.1276 276 LYS A CA  
2142 C C   . LYS A 276 ? 0.5437 0.4509 0.8272 -0.0298 0.3479  -0.1239 276 LYS A C   
2143 O O   . LYS A 276 ? 0.5838 0.4666 0.8254 -0.0380 0.3579  -0.1198 276 LYS A O   
2144 C CB  . LYS A 276 ? 0.6223 0.5128 0.9068 -0.0163 0.3614  -0.1279 276 LYS A CB  
2145 C CG  . LYS A 276 ? 0.6494 0.5520 0.9710 -0.0047 0.3614  -0.1321 276 LYS A CG  
2146 C CD  . LYS A 276 ? 0.5934 0.4876 0.9276 -0.0060 0.3832  -0.1328 276 LYS A CD  
2147 C CE  . LYS A 276 ? 0.5839 0.4834 0.9444 0.0056  0.3856  -0.1365 276 LYS A CE  
2148 N NZ  . LYS A 276 ? 0.6116 0.5056 0.9901 0.0035  0.4082  -0.1375 276 LYS A NZ  
2149 N N   . LYS A 277 ? 0.4948 0.4234 0.7948 -0.0261 0.3282  -0.1253 277 LYS A N   
2150 C CA  . LYS A 277 ? 0.4654 0.3927 0.7385 -0.0327 0.3159  -0.1215 277 LYS A CA  
2151 C C   . LYS A 277 ? 0.4953 0.4191 0.7426 -0.0282 0.2915  -0.1182 277 LYS A C   
2152 O O   . LYS A 277 ? 0.4990 0.4369 0.7715 -0.0189 0.2789  -0.1206 277 LYS A O   
2153 C CB  . LYS A 277 ? 0.4860 0.4405 0.7989 -0.0358 0.3056  -0.1223 277 LYS A CB  
2154 C CG  . LYS A 277 ? 0.4532 0.4058 0.7374 -0.0426 0.2876  -0.1164 277 LYS A CG  
2155 C CD  . LYS A 277 ? 0.4316 0.4088 0.7561 -0.0460 0.2797  -0.1183 277 LYS A CD  
2156 C CE  . LYS A 277 ? 0.4576 0.4310 0.7526 -0.0524 0.2641  -0.1126 277 LYS A CE  
2157 N NZ  . LYS A 277 ? 0.4205 0.4145 0.7514 -0.0561 0.2567  -0.1149 277 LYS A NZ  
2158 N N   . LYS A 278 ? 0.4655 0.3699 0.6631 -0.0347 0.2850  -0.1128 278 LYS A N   
2159 C CA  . LYS A 278 ? 0.4688 0.3692 0.6407 -0.0328 0.2631  -0.1090 278 LYS A CA  
2160 C C   . LYS A 278 ? 0.5226 0.4242 0.6726 -0.0407 0.2491  -0.1035 278 LYS A C   
2161 O O   . LYS A 278 ? 0.5057 0.3995 0.6422 -0.0481 0.2586  -0.1017 278 LYS A O   
2162 C CB  . LYS A 278 ? 0.5029 0.3751 0.6344 -0.0325 0.2698  -0.1088 278 LYS A CB  
2163 C CG  . LYS A 278 ? 0.5274 0.3940 0.6754 -0.0242 0.2854  -0.1144 278 LYS A CG  
2164 C CD  . LYS A 278 ? 0.5598 0.3952 0.6635 -0.0247 0.2914  -0.1147 278 LYS A CD  
2165 C CE  . LYS A 278 ? 0.5964 0.4251 0.7170 -0.0153 0.3073  -0.1205 278 LYS A CE  
2166 N NZ  . LYS A 278 ? 0.5568 0.4077 0.7161 -0.0048 0.2925  -0.1214 278 LYS A NZ  
2167 N N   . TYR A 279 ? 0.4847 0.3946 0.6305 -0.0384 0.2274  -0.1005 279 TYR A N   
2168 C CA  . TYR A 279 ? 0.4218 0.3326 0.5469 -0.0447 0.2136  -0.0954 279 TYR A CA  
2169 C C   . TYR A 279 ? 0.4829 0.3740 0.5660 -0.0478 0.2074  -0.0917 279 TYR A C   
2170 O O   . TYR A 279 ? 0.4983 0.3818 0.5742 -0.0434 0.2047  -0.0925 279 TYR A O   
2171 C CB  . TYR A 279 ? 0.4512 0.3846 0.6009 -0.0407 0.1944  -0.0947 279 TYR A CB  
2172 C CG  . TYR A 279 ? 0.4555 0.4090 0.6461 -0.0399 0.1971  -0.0986 279 TYR A CG  
2173 C CD1 . TYR A 279 ? 0.4296 0.3954 0.6582 -0.0328 0.2020  -0.1042 279 TYR A CD1 
2174 C CD2 . TYR A 279 ? 0.4414 0.4016 0.6343 -0.0461 0.1940  -0.0969 279 TYR A CD2 
2175 C CE1 . TYR A 279 ? 0.4151 0.4008 0.6857 -0.0329 0.2035  -0.1087 279 TYR A CE1 
2176 C CE2 . TYR A 279 ? 0.4852 0.4630 0.7169 -0.0464 0.1961  -0.1011 279 TYR A CE2 
2177 C CZ  . TYR A 279 ? 0.4580 0.4492 0.7295 -0.0402 0.2005  -0.1072 279 TYR A CZ  
2178 O OH  . TYR A 279 ? 0.4582 0.4682 0.7725 -0.0413 0.2019  -0.1122 279 TYR A OH  
2179 N N   . LEU A 280 ? 0.4845 0.3673 0.5413 -0.0553 0.2046  -0.0878 280 LEU A N   
2180 C CA  . LEU A 280 ? 0.4702 0.3361 0.4897 -0.0596 0.1972  -0.0847 280 LEU A CA  
2181 C C   . LEU A 280 ? 0.4494 0.3252 0.4638 -0.0634 0.1815  -0.0799 280 LEU A C   
2182 O O   . LEU A 280 ? 0.4655 0.3523 0.4927 -0.0650 0.1809  -0.0787 280 LEU A O   
2183 C CB  . LEU A 280 ? 0.5396 0.3799 0.5263 -0.0648 0.2108  -0.0854 280 LEU A CB  
2184 C CG  . LEU A 280 ? 0.6018 0.4278 0.5883 -0.0616 0.2305  -0.0904 280 LEU A CG  
2185 C CD1 . LEU A 280 ? 0.6610 0.4586 0.6092 -0.0669 0.2439  -0.0906 280 LEU A CD1 
2186 C CD2 . LEU A 280 ? 0.5641 0.3844 0.5485 -0.0568 0.2269  -0.0929 280 LEU A CD2 
2187 N N   . ALA A 281 ? 0.4733 0.3441 0.4696 -0.0652 0.1697  -0.0773 281 ALA A N   
2188 C CA  . ALA A 281 ? 0.4728 0.3505 0.4619 -0.0690 0.1562  -0.0728 281 ALA A CA  
2189 C C   . ALA A 281 ? 0.4668 0.3262 0.4229 -0.0754 0.1535  -0.0713 281 ALA A C   
2190 O O   . ALA A 281 ? 0.5085 0.3511 0.4471 -0.0765 0.1573  -0.0737 281 ALA A O   
2191 C CB  . ALA A 281 ? 0.4314 0.3221 0.4328 -0.0654 0.1437  -0.0710 281 ALA A CB  
2192 N N   . ALA A 282 ? 0.4577 0.3195 0.4052 -0.0794 0.1459  -0.0678 282 ALA A N   
2193 C CA  . ALA A 282 ? 0.4799 0.3252 0.3977 -0.0849 0.1404  -0.0666 282 ALA A CA  
2194 C C   . ALA A 282 ? 0.4884 0.3457 0.4091 -0.0872 0.1256  -0.0624 282 ALA A C   
2195 O O   . ALA A 282 ? 0.4599 0.3293 0.3928 -0.0859 0.1238  -0.0599 282 ALA A O   
2196 C CB  . ALA A 282 ? 0.4685 0.2953 0.3639 -0.0872 0.1501  -0.0669 282 ALA A CB  
2197 N N   . ALA A 283 ? 0.4763 0.3291 0.3864 -0.0908 0.1157  -0.0621 283 ALA A N   
2198 C CA  . ALA A 283 ? 0.4862 0.3496 0.4002 -0.0934 0.1020  -0.0586 283 ALA A CA  
2199 C C   . ALA A 283 ? 0.4663 0.3140 0.3546 -0.0981 0.0950  -0.0585 283 ALA A C   
2200 O O   . ALA A 283 ? 0.4681 0.3011 0.3395 -0.1020 0.0918  -0.0614 283 ALA A O   
2201 C CB  . ALA A 283 ? 0.4538 0.3250 0.3791 -0.0945 0.0961  -0.0585 283 ALA A CB  
2202 N N   . PHE A 284 ? 0.5140 0.3630 0.3981 -0.0975 0.0918  -0.0555 284 PHE A N   
2203 C CA  . PHE A 284 ? 0.4960 0.3330 0.3583 -0.1006 0.0808  -0.0543 284 PHE A CA  
2204 C C   . PHE A 284 ? 0.5109 0.3672 0.3917 -0.0998 0.0687  -0.0503 284 PHE A C   
2205 O O   . PHE A 284 ? 0.4430 0.3161 0.3455 -0.0962 0.0725  -0.0481 284 PHE A O   
2206 C CB  . PHE A 284 ? 0.5328 0.3496 0.3692 -0.0995 0.0880  -0.0534 284 PHE A CB  
2207 C CG  . PHE A 284 ? 0.5487 0.3482 0.3711 -0.0990 0.1048  -0.0569 284 PHE A CG  
2208 C CD1 . PHE A 284 ? 0.5421 0.3321 0.3571 -0.1009 0.1074  -0.0616 284 PHE A CD1 
2209 C CD2 . PHE A 284 ? 0.5707 0.3625 0.3884 -0.0969 0.1191  -0.0558 284 PHE A CD2 
2210 C CE1 . PHE A 284 ? 0.5731 0.3467 0.3763 -0.0996 0.1240  -0.0652 284 PHE A CE1 
2211 C CE2 . PHE A 284 ? 0.6063 0.3828 0.4141 -0.0963 0.1366  -0.0592 284 PHE A CE2 
2212 C CZ  . PHE A 284 ? 0.5909 0.3587 0.3916 -0.0971 0.1391  -0.0641 284 PHE A CZ  
2213 N N   . PRO A 285 ? 0.5141 0.3683 0.3878 -0.1027 0.0539  -0.0497 285 PRO A N   
2214 C CA  . PRO A 285 ? 0.4723 0.3460 0.3670 -0.1012 0.0432  -0.0462 285 PRO A CA  
2215 C C   . PRO A 285 ? 0.5358 0.4094 0.4281 -0.0964 0.0456  -0.0422 285 PRO A C   
2216 O O   . PRO A 285 ? 0.5085 0.3662 0.3821 -0.0952 0.0551  -0.0420 285 PRO A O   
2217 C CB  . PRO A 285 ? 0.5327 0.4007 0.4182 -0.1053 0.0265  -0.0474 285 PRO A CB  
2218 C CG  . PRO A 285 ? 0.5229 0.3739 0.3911 -0.1103 0.0288  -0.0526 285 PRO A CG  
2219 C CD  . PRO A 285 ? 0.5740 0.4094 0.4237 -0.1074 0.0454  -0.0532 285 PRO A CD  
2220 N N   . SER A 286 ? 0.4813 0.3726 0.3941 -0.0938 0.0385  -0.0391 286 SER A N   
2221 C CA  . SER A 286 ? 0.5228 0.4133 0.4342 -0.0892 0.0404  -0.0354 286 SER A CA  
2222 C C   . SER A 286 ? 0.5383 0.4046 0.4173 -0.0890 0.0356  -0.0337 286 SER A C   
2223 O O   . SER A 286 ? 0.5714 0.4288 0.4360 -0.0910 0.0225  -0.0344 286 SER A O   
2224 C CB  . SER A 286 ? 0.4968 0.4077 0.4333 -0.0859 0.0324  -0.0326 286 SER A CB  
2225 O OG  . SER A 286 ? 0.5282 0.4580 0.4896 -0.0867 0.0350  -0.0341 286 SER A OG  
2226 N N   . ALA A 287 ? 0.5999 0.4539 0.4665 -0.0867 0.0464  -0.0316 287 ALA A N   
2227 C CA  . ALA A 287 ? 0.6233 0.4498 0.4547 -0.0858 0.0458  -0.0290 287 ALA A CA  
2228 C C   . ALA A 287 ? 0.6466 0.4497 0.4465 -0.0896 0.0472  -0.0324 287 ALA A C   
2229 O O   . ALA A 287 ? 0.6766 0.4570 0.4441 -0.0892 0.0384  -0.0310 287 ALA A O   
2230 C CB  . ALA A 287 ? 0.6284 0.4542 0.4556 -0.0821 0.0285  -0.0248 287 ALA A CB  
2231 N N   . CYS A 288 ? 0.6266 0.4328 0.4335 -0.0925 0.0585  -0.0368 288 CYS A N   
2232 C CA  . CYS A 288 ? 0.6167 0.3997 0.3939 -0.0958 0.0617  -0.0408 288 CYS A CA  
2233 C C   . CYS A 288 ? 0.6795 0.4497 0.4482 -0.0960 0.0840  -0.0428 288 CYS A C   
2234 O O   . CYS A 288 ? 0.6477 0.4007 0.3962 -0.0982 0.0898  -0.0469 288 CYS A O   
2235 C CB  . CYS A 288 ? 0.6101 0.4045 0.4004 -0.0994 0.0525  -0.0452 288 CYS A CB  
2236 S SG  . CYS A 288 ? 0.6366 0.4344 0.4248 -0.1010 0.0256  -0.0446 288 CYS A SG  
2237 N N   . GLY A 289 ? 0.5729 0.3510 0.3580 -0.0938 0.0968  -0.0405 289 GLY A N   
2238 C CA  . GLY A 289 ? 0.5950 0.3573 0.3696 -0.0941 0.1180  -0.0418 289 GLY A CA  
2239 C C   . GLY A 289 ? 0.5890 0.3718 0.3994 -0.0935 0.1315  -0.0447 289 GLY A C   
2240 O O   . GLY A 289 ? 0.5735 0.3460 0.3812 -0.0939 0.1498  -0.0467 289 GLY A O   
2241 N N   . LYS A 290 ? 0.5280 0.3388 0.3720 -0.0921 0.1232  -0.0450 290 LYS A N   
2242 C CA  . LYS A 290 ? 0.5365 0.3650 0.4118 -0.0908 0.1331  -0.0484 290 LYS A CA  
2243 C C   . LYS A 290 ? 0.5428 0.3716 0.4301 -0.0902 0.1470  -0.0478 290 LYS A C   
2244 O O   . LYS A 290 ? 0.5179 0.3456 0.4157 -0.0903 0.1622  -0.0512 290 LYS A O   
2245 C CB  . LYS A 290 ? 0.4518 0.3065 0.3552 -0.0890 0.1209  -0.0484 290 LYS A CB  
2246 C CG  . LYS A 290 ? 0.4681 0.3250 0.3682 -0.0903 0.1114  -0.0502 290 LYS A CG  
2247 C CD  . LYS A 290 ? 0.4666 0.3475 0.3941 -0.0882 0.1031  -0.0497 290 LYS A CD  
2248 C CE  . LYS A 290 ? 0.4397 0.3322 0.3763 -0.0868 0.0942  -0.0457 290 LYS A CE  
2249 N NZ  . LYS A 290 ? 0.4450 0.3281 0.3626 -0.0890 0.0832  -0.0431 290 LYS A NZ  
2250 N N   . THR A 291 ? 0.5381 0.3674 0.4248 -0.0899 0.1426  -0.0436 291 THR A N   
2251 C CA  . THR A 291 ? 0.5306 0.3597 0.4304 -0.0904 0.1554  -0.0431 291 THR A CA  
2252 C C   . THR A 291 ? 0.5532 0.3564 0.4301 -0.0928 0.1741  -0.0430 291 THR A C   
2253 O O   . THR A 291 ? 0.5463 0.3518 0.4418 -0.0941 0.1903  -0.0455 291 THR A O   
2254 C CB  . THR A 291 ? 0.5084 0.3401 0.4088 -0.0893 0.1464  -0.0385 291 THR A CB  
2255 O OG1 . THR A 291 ? 0.5081 0.3647 0.4332 -0.0867 0.1328  -0.0395 291 THR A OG1 
2256 C CG2 . THR A 291 ? 0.5127 0.3403 0.4244 -0.0908 0.1603  -0.0379 291 THR A CG2 
2257 N N   . ASN A 292 ? 0.5776 0.3552 0.4144 -0.0935 0.1724  -0.0406 292 ASN A N   
2258 C CA  . ASN A 292 ? 0.6002 0.3490 0.4096 -0.0955 0.1917  -0.0402 292 ASN A CA  
2259 C C   . ASN A 292 ? 0.6266 0.3753 0.4440 -0.0959 0.2062  -0.0462 292 ASN A C   
2260 O O   . ASN A 292 ? 0.6498 0.3846 0.4641 -0.0974 0.2280  -0.0473 292 ASN A O   
2261 C CB  . ASN A 292 ? 0.6979 0.4163 0.4575 -0.0953 0.1840  -0.0363 292 ASN A CB  
2262 C CG  . ASN A 292 ? 0.7314 0.4398 0.4780 -0.0943 0.1788  -0.0296 292 ASN A CG  
2263 O OD1 . ASN A 292 ? 0.7993 0.4821 0.5224 -0.0953 0.1936  -0.0262 292 ASN A OD1 
2264 N ND2 . ASN A 292 ? 0.6964 0.4247 0.4597 -0.0921 0.1592  -0.0275 292 ASN A ND2 
2265 N N   . LEU A 293 ? 0.6053 0.3681 0.4332 -0.0945 0.1956  -0.0500 293 LEU A N   
2266 C CA  . LEU A 293 ? 0.5949 0.3588 0.4336 -0.0938 0.2085  -0.0557 293 LEU A CA  
2267 C C   . LEU A 293 ? 0.5730 0.3631 0.4597 -0.0923 0.2166  -0.0588 293 LEU A C   
2268 O O   . LEU A 293 ? 0.5447 0.3315 0.4433 -0.0922 0.2358  -0.0622 293 LEU A O   
2269 C CB  . LEU A 293 ? 0.5690 0.3370 0.4021 -0.0928 0.1942  -0.0583 293 LEU A CB  
2270 C CG  . LEU A 293 ? 0.5756 0.3386 0.4116 -0.0914 0.2061  -0.0641 293 LEU A CG  
2271 C CD1 . LEU A 293 ? 0.6224 0.3514 0.4210 -0.0927 0.2238  -0.0651 293 LEU A CD1 
2272 C CD2 . LEU A 293 ? 0.5748 0.3420 0.4069 -0.0911 0.1905  -0.0661 293 LEU A CD2 
2273 N N   . ALA A 294 ? 0.5713 0.3871 0.4861 -0.0910 0.2022  -0.0580 294 ALA A N   
2274 C CA  . ALA A 294 ? 0.5384 0.3790 0.4975 -0.0891 0.2057  -0.0616 294 ALA A CA  
2275 C C   . ALA A 294 ? 0.5822 0.4198 0.5561 -0.0917 0.2232  -0.0620 294 ALA A C   
2276 O O   . ALA A 294 ? 0.5586 0.4125 0.5692 -0.0907 0.2311  -0.0667 294 ALA A O   
2277 C CB  . ALA A 294 ? 0.5158 0.3792 0.4942 -0.0872 0.1865  -0.0604 294 ALA A CB  
2278 N N   . MET A 295 ? 0.5719 0.3895 0.5199 -0.0950 0.2286  -0.0572 295 MET A N   
2279 C CA  . MET A 295 ? 0.6298 0.4416 0.5899 -0.0985 0.2465  -0.0568 295 MET A CA  
2280 C C   . MET A 295 ? 0.6301 0.4112 0.5602 -0.1010 0.2691  -0.0557 295 MET A C   
2281 O O   . MET A 295 ? 0.6503 0.4190 0.5800 -0.1047 0.2854  -0.0536 295 MET A O   
2282 C CB  . MET A 295 ? 0.5864 0.3956 0.5402 -0.1002 0.2384  -0.0516 295 MET A CB  
2283 C CG  . MET A 295 ? 0.5896 0.4254 0.5708 -0.0980 0.2195  -0.0527 295 MET A CG  
2284 S SD  . MET A 295 ? 0.6450 0.4745 0.6209 -0.0999 0.2147  -0.0473 295 MET A SD  
2285 C CE  . MET A 295 ? 0.5777 0.4390 0.5830 -0.0958 0.1921  -0.0502 295 MET A CE  
2286 N N   . MET A 296 ? 0.6197 0.3860 0.5228 -0.0992 0.2710  -0.0570 296 MET A N   
2287 C CA  . MET A 296 ? 0.6456 0.3759 0.5065 -0.1009 0.2896  -0.0552 296 MET A CA  
2288 C C   . MET A 296 ? 0.7184 0.4438 0.5995 -0.1035 0.3189  -0.0575 296 MET A C   
2289 O O   . MET A 296 ? 0.7208 0.4717 0.6500 -0.1028 0.3252  -0.0630 296 MET A O   
2290 C CB  . MET A 296 ? 0.6858 0.4040 0.5208 -0.0983 0.2864  -0.0583 296 MET A CB  
2291 C CG  . MET A 296 ? 0.7728 0.4666 0.5907 -0.0985 0.3129  -0.0614 296 MET A CG  
2292 S SD  . MET A 296 ? 0.8342 0.5096 0.6167 -0.0956 0.3079  -0.0655 296 MET A SD  
2293 C CE  . MET A 296 ? 0.6922 0.4089 0.5257 -0.0921 0.2903  -0.0701 296 MET A CE  
2294 N N   . ASN A 297 ? 0.7000 0.3913 0.5437 -0.1063 0.3367  -0.0532 297 ASN A N   
2295 C CA  . ASN A 297 ? 0.7277 0.4074 0.5828 -0.1053 0.3568  -0.0557 297 ASN A CA  
2296 C C   . ASN A 297 ? 0.7943 0.4469 0.6135 -0.1024 0.3656  -0.0576 297 ASN A C   
2297 O O   . ASN A 297 ? 0.8120 0.4297 0.5751 -0.1025 0.3652  -0.0533 297 ASN A O   
2298 C CB  . ASN A 297 ? 0.8003 0.4575 0.6371 -0.1078 0.3651  -0.0500 297 ASN A CB  
2299 C CG  . ASN A 297 ? 0.8745 0.5256 0.7342 -0.1078 0.3865  -0.0531 297 ASN A CG  
2300 O OD1 . ASN A 297 ? 0.9513 0.6313 0.8661 -0.1081 0.3901  -0.0585 297 ASN A OD1 
2301 N ND2 . ASN A 297 ? 0.9114 0.5237 0.7285 -0.1075 0.4005  -0.0497 297 ASN A ND2 
2302 N N   . PRO A 298 ? 0.7877 0.4534 0.6354 -0.0996 0.3725  -0.0640 298 PRO A N   
2303 C CA  . PRO A 298 ? 0.7917 0.4309 0.6041 -0.0968 0.3796  -0.0659 298 PRO A CA  
2304 C C   . PRO A 298 ? 0.8189 0.4207 0.6000 -0.0972 0.3985  -0.0634 298 PRO A C   
2305 O O   . PRO A 298 ? 0.8247 0.4290 0.6325 -0.0984 0.4129  -0.0634 298 PRO A O   
2306 C CB  . PRO A 298 ? 0.8154 0.4810 0.6757 -0.0933 0.3838  -0.0729 298 PRO A CB  
2307 C CG  . PRO A 298 ? 0.7996 0.5065 0.7126 -0.0939 0.3723  -0.0747 298 PRO A CG  
2308 C CD  . PRO A 298 ? 0.7487 0.4533 0.6609 -0.0982 0.3719  -0.0697 298 PRO A CD  
2309 N N   . THR A 299 ? 0.8537 0.4196 0.5778 -0.0960 0.3985  -0.0617 299 THR A N   
2310 C CA  . THR A 299 ? 0.9022 0.4291 0.5927 -0.0957 0.4172  -0.0596 299 THR A CA  
2311 C C   . THR A 299 ? 0.9151 0.4400 0.6262 -0.0933 0.4359  -0.0648 299 THR A C   
2312 O O   . THR A 299 ? 0.9791 0.4808 0.6826 -0.0934 0.4562  -0.0639 299 THR A O   
2313 C CB  . THR A 299 ? 0.9715 0.4577 0.5892 -0.0951 0.4079  -0.0556 299 THR A CB  
2314 O OG1 . THR A 299 ? 0.9622 0.4489 0.5645 -0.0934 0.3962  -0.0596 299 THR A OG1 
2315 C CG2 . THR A 299 ? 0.9691 0.4549 0.5660 -0.0971 0.3905  -0.0496 299 THR A CG2 
2316 N N   . LEU A 300 ? 0.8860 0.4342 0.6239 -0.0908 0.4301  -0.0701 300 LEU A N   
2317 C CA  . LEU A 300 ? 0.9239 0.4715 0.6832 -0.0878 0.4468  -0.0747 300 LEU A CA  
2318 C C   . LEU A 300 ? 0.8750 0.4503 0.6982 -0.0881 0.4601  -0.0773 300 LEU A C   
2319 O O   . LEU A 300 ? 0.8275 0.4402 0.6964 -0.0885 0.4488  -0.0790 300 LEU A O   
2320 C CB  . LEU A 300 ? 0.9072 0.4715 0.6759 -0.0845 0.4349  -0.0794 300 LEU A CB  
2321 C CG  . LEU A 300 ? 0.9788 0.5169 0.6903 -0.0839 0.4224  -0.0793 300 LEU A CG  
2322 C CD1 . LEU A 300 ? 0.9315 0.4890 0.6632 -0.0803 0.4140  -0.0849 300 LEU A CD1 
2323 C CD2 . LEU A 300 ? 0.9919 0.4840 0.6527 -0.0836 0.4370  -0.0775 300 LEU A CD2 
2324 N N   . PRO A 301 ? 0.9088 0.4675 0.7384 -0.0878 0.4835  -0.0781 301 PRO A N   
2325 C CA  . PRO A 301 ? 0.8892 0.4748 0.7822 -0.0885 0.4952  -0.0813 301 PRO A CA  
2326 C C   . PRO A 301 ? 0.8601 0.4822 0.8067 -0.0845 0.4902  -0.0873 301 PRO A C   
2327 O O   . PRO A 301 ? 0.8576 0.4738 0.7913 -0.0806 0.4895  -0.0894 301 PRO A O   
2328 C CB  . PRO A 301 ? 0.9435 0.4958 0.8212 -0.0891 0.5227  -0.0806 301 PRO A CB  
2329 C CG  . PRO A 301 ? 1.0318 0.5407 0.8392 -0.0875 0.5249  -0.0778 301 PRO A CG  
2330 C CD  . PRO A 301 ? 0.9636 0.4821 0.7495 -0.0861 0.4994  -0.0777 301 PRO A CD  
2331 N N   . GLY A 302 ? 0.8125 0.4715 0.8190 -0.0851 0.4857  -0.0902 302 GLY A N   
2332 C CA  . GLY A 302 ? 0.7757 0.4710 0.8363 -0.0807 0.4786  -0.0959 302 GLY A CA  
2333 C C   . GLY A 302 ? 0.7926 0.5133 0.8587 -0.0785 0.4532  -0.0966 302 GLY A C   
2334 O O   . GLY A 302 ? 0.7729 0.5230 0.8816 -0.0739 0.4453  -0.1011 302 GLY A O   
2335 N N   . TRP A 303 ? 0.7383 0.4478 0.7628 -0.0814 0.4402  -0.0922 303 TRP A N   
2336 C CA  . TRP A 303 ? 0.6907 0.4212 0.7163 -0.0800 0.4174  -0.0926 303 TRP A CA  
2337 C C   . TRP A 303 ? 0.6869 0.4385 0.7339 -0.0839 0.4057  -0.0908 303 TRP A C   
2338 O O   . TRP A 303 ? 0.6791 0.4163 0.7129 -0.0884 0.4129  -0.0872 303 TRP A O   
2339 C CB  . TRP A 303 ? 0.7109 0.4132 0.6735 -0.0804 0.4102  -0.0895 303 TRP A CB  
2340 C CG  . TRP A 303 ? 0.7559 0.4428 0.7014 -0.0759 0.4165  -0.0925 303 TRP A CG  
2341 C CD1 . TRP A 303 ? 0.7905 0.4457 0.7087 -0.0755 0.4346  -0.0921 303 TRP A CD1 
2342 C CD2 . TRP A 303 ? 0.7364 0.4376 0.6911 -0.0710 0.4050  -0.0964 303 TRP A CD2 
2343 N NE1 . TRP A 303 ? 0.8061 0.4557 0.7161 -0.0708 0.4347  -0.0955 303 TRP A NE1 
2344 C CE2 . TRP A 303 ? 0.7545 0.4317 0.6864 -0.0679 0.4165  -0.0982 303 TRP A CE2 
2345 C CE3 . TRP A 303 ? 0.7221 0.4523 0.7005 -0.0687 0.3866  -0.0986 303 TRP A CE3 
2346 C CZ2 . TRP A 303 ? 0.7680 0.4493 0.7011 -0.0626 0.4097  -0.1022 303 TRP A CZ2 
2347 C CZ3 . TRP A 303 ? 0.7023 0.4355 0.6807 -0.0631 0.3803  -0.1025 303 TRP A CZ3 
2348 C CH2 . TRP A 303 ? 0.7172 0.4261 0.6734 -0.0601 0.3915  -0.1043 303 TRP A CH2 
2349 N N   . LYS A 304 ? 0.6184 0.4028 0.6982 -0.0817 0.3883  -0.0934 304 LYS A N   
2350 C CA  . LYS A 304 ? 0.5994 0.4045 0.6997 -0.0853 0.3757  -0.0920 304 LYS A CA  
2351 C C   . LYS A 304 ? 0.6417 0.4630 0.7361 -0.0839 0.3551  -0.0917 304 LYS A C   
2352 O O   . LYS A 304 ? 0.6102 0.4444 0.7178 -0.0784 0.3489  -0.0955 304 LYS A O   
2353 C CB  . LYS A 304 ? 0.6170 0.4514 0.7810 -0.0847 0.3769  -0.0968 304 LYS A CB  
2354 C CG  . LYS A 304 ? 0.6372 0.4928 0.8235 -0.0883 0.3627  -0.0962 304 LYS A CG  
2355 C CD  . LYS A 304 ? 0.7163 0.5982 0.9637 -0.0881 0.3629  -0.1019 304 LYS A CD  
2356 C CE  . LYS A 304 ? 0.7172 0.6167 0.9825 -0.0921 0.3481  -0.1016 304 LYS A CE  
2357 N NZ  . LYS A 304 ? 0.7854 0.7027 1.1025 -0.0937 0.3506  -0.1069 304 LYS A NZ  
2358 N N   . VAL A 305 ? 0.5567 0.3757 0.6305 -0.0885 0.3453  -0.0869 305 VAL A N   
2359 C CA  . VAL A 305 ? 0.5784 0.4123 0.6473 -0.0879 0.3233  -0.0856 305 VAL A CA  
2360 C C   . VAL A 305 ? 0.5660 0.4265 0.6732 -0.0896 0.3107  -0.0857 305 VAL A C   
2361 O O   . VAL A 305 ? 0.5807 0.4367 0.6925 -0.0953 0.3205  -0.0837 305 VAL A O   
2362 C CB  . VAL A 305 ? 0.5996 0.4071 0.6099 -0.0902 0.3136  -0.0792 305 VAL A CB  
2363 C CG1 . VAL A 305 ? 0.5890 0.4139 0.5999 -0.0885 0.2837  -0.0768 305 VAL A CG1 
2364 C CG2 . VAL A 305 ? 0.6904 0.4723 0.6626 -0.0880 0.3214  -0.0804 305 VAL A CG2 
2365 N N   . GLU A 306 ? 0.4798 0.3656 0.6130 -0.0848 0.2897  -0.0883 306 GLU A N   
2366 C CA  . GLU A 306 ? 0.5251 0.4333 0.6865 -0.0858 0.2736  -0.0887 306 GLU A CA  
2367 C C   . GLU A 306 ? 0.5148 0.4271 0.6549 -0.0830 0.2481  -0.0852 306 GLU A C   
2368 O O   . GLU A 306 ? 0.4958 0.4032 0.6167 -0.0791 0.2409  -0.0846 306 GLU A O   
2369 C CB  . GLU A 306 ? 0.4943 0.4303 0.7127 -0.0823 0.2727  -0.0960 306 GLU A CB  
2370 C CG  . GLU A 306 ? 0.5577 0.4915 0.8028 -0.0853 0.3001  -0.1000 306 GLU A CG  
2371 C CD  . GLU A 306 ? 0.5412 0.5014 0.8422 -0.0799 0.2979  -0.1078 306 GLU A CD  
2372 O OE1 . GLU A 306 ? 0.5258 0.4869 0.8316 -0.0733 0.3015  -0.1106 306 GLU A OE1 
2373 O OE2 . GLU A 306 ? 0.5652 0.5437 0.9044 -0.0817 0.2910  -0.1113 306 GLU A OE2 
2374 N N   . CYS A 307 ? 0.5178 0.4379 0.6616 -0.0853 0.2358  -0.0829 307 CYS A N   
2375 C CA  . CYS A 307 ? 0.4601 0.3814 0.5815 -0.0837 0.2149  -0.0788 307 CYS A CA  
2376 C C   . CYS A 307 ? 0.4751 0.4210 0.6261 -0.0789 0.1969  -0.0823 307 CYS A C   
2377 O O   . CYS A 307 ? 0.4753 0.4350 0.6567 -0.0798 0.1949  -0.0857 307 CYS A O   
2378 C CB  . CYS A 307 ? 0.4853 0.3950 0.5859 -0.0886 0.2140  -0.0735 307 CYS A CB  
2379 S SG  . CYS A 307 ? 0.5205 0.4327 0.5976 -0.0864 0.1902  -0.0684 307 CYS A SG  
2380 N N   . VAL A 308 ? 0.4763 0.4257 0.6171 -0.0739 0.1839  -0.0815 308 VAL A N   
2381 C CA  . VAL A 308 ? 0.4430 0.4105 0.6016 -0.0688 0.1658  -0.0835 308 VAL A CA  
2382 C C   . VAL A 308 ? 0.4320 0.3980 0.5698 -0.0698 0.1525  -0.0788 308 VAL A C   
2383 O O   . VAL A 308 ? 0.4629 0.4402 0.6148 -0.0685 0.1421  -0.0803 308 VAL A O   
2384 C CB  . VAL A 308 ? 0.4122 0.3833 0.5732 -0.0621 0.1602  -0.0852 308 VAL A CB  
2385 C CG1 . VAL A 308 ? 0.4023 0.3875 0.5740 -0.0562 0.1411  -0.0862 308 VAL A CG1 
2386 C CG2 . VAL A 308 ? 0.4345 0.4093 0.6214 -0.0596 0.1728  -0.0905 308 VAL A CG2 
2387 N N   . GLY A 309 ? 0.4279 0.3794 0.5330 -0.0721 0.1529  -0.0736 309 GLY A N   
2388 C CA  . GLY A 309 ? 0.3887 0.3388 0.4754 -0.0729 0.1415  -0.0689 309 GLY A CA  
2389 C C   . GLY A 309 ? 0.4531 0.3853 0.5073 -0.0764 0.1450  -0.0643 309 GLY A C   
2390 O O   . GLY A 309 ? 0.4428 0.3634 0.4852 -0.0774 0.1538  -0.0650 309 GLY A O   
2391 N N   . ASP A 310 ? 0.4618 0.3910 0.5014 -0.0778 0.1374  -0.0600 310 ASP A N   
2392 C CA  . ASP A 310 ? 0.4496 0.3615 0.4588 -0.0809 0.1383  -0.0558 310 ASP A CA  
2393 C C   . ASP A 310 ? 0.4625 0.3769 0.4593 -0.0801 0.1245  -0.0527 310 ASP A C   
2394 O O   . ASP A 310 ? 0.4736 0.3746 0.4466 -0.0825 0.1221  -0.0499 310 ASP A O   
2395 C CB  . ASP A 310 ? 0.4757 0.3760 0.4749 -0.0837 0.1437  -0.0528 310 ASP A CB  
2396 C CG  . ASP A 310 ? 0.5299 0.4383 0.5334 -0.0823 0.1326  -0.0499 310 ASP A CG  
2397 O OD1 . ASP A 310 ? 0.4514 0.3767 0.4732 -0.0793 0.1242  -0.0518 310 ASP A OD1 
2398 O OD2 . ASP A 310 ? 0.4754 0.3709 0.4617 -0.0837 0.1328  -0.0458 310 ASP A OD2 
2399 N N   . ASP A 311 ? 0.4026 0.3326 0.4145 -0.0769 0.1156  -0.0533 311 ASP A N   
2400 C CA  . ASP A 311 ? 0.4231 0.3561 0.4264 -0.0769 0.1046  -0.0500 311 ASP A CA  
2401 C C   . ASP A 311 ? 0.3849 0.3285 0.3977 -0.0742 0.0992  -0.0510 311 ASP A C   
2402 O O   . ASP A 311 ? 0.4022 0.3446 0.4067 -0.0757 0.0939  -0.0491 311 ASP A O   
2403 C CB  . ASP A 311 ? 0.3998 0.3374 0.4059 -0.0759 0.0992  -0.0472 311 ASP A CB  
2404 C CG  . ASP A 311 ? 0.4087 0.3489 0.4078 -0.0760 0.0890  -0.0436 311 ASP A CG  
2405 O OD1 . ASP A 311 ? 0.3674 0.2975 0.3497 -0.0788 0.0860  -0.0417 311 ASP A OD1 
2406 O OD2 . ASP A 311 ? 0.4346 0.3870 0.4455 -0.0732 0.0839  -0.0430 311 ASP A OD2 
2407 N N   . ILE A 312 ? 0.3860 0.3390 0.4155 -0.0702 0.0998  -0.0538 312 ILE A N   
2408 C CA  . ILE A 312 ? 0.3829 0.3427 0.4173 -0.0667 0.0946  -0.0538 312 ILE A CA  
2409 C C   . ILE A 312 ? 0.3826 0.3436 0.4275 -0.0630 0.0978  -0.0577 312 ILE A C   
2410 O O   . ILE A 312 ? 0.3632 0.3288 0.4225 -0.0612 0.1003  -0.0611 312 ILE A O   
2411 C CB  . ILE A 312 ? 0.4138 0.3832 0.4550 -0.0634 0.0882  -0.0527 312 ILE A CB  
2412 C CG1 . ILE A 312 ? 0.4481 0.4176 0.4824 -0.0660 0.0849  -0.0489 312 ILE A CG1 
2413 C CG2 . ILE A 312 ? 0.4019 0.3744 0.4434 -0.0595 0.0845  -0.0522 312 ILE A CG2 
2414 C CD1 . ILE A 312 ? 0.4753 0.4530 0.5163 -0.0623 0.0807  -0.0482 312 ILE A CD1 
2415 N N   . ALA A 313 ? 0.4341 0.3913 0.4740 -0.0616 0.0973  -0.0575 313 ALA A N   
2416 C CA  . ALA A 313 ? 0.4112 0.3686 0.4605 -0.0566 0.0989  -0.0606 313 ALA A CA  
2417 C C   . ALA A 313 ? 0.4339 0.3924 0.4806 -0.0518 0.0923  -0.0589 313 ALA A C   
2418 O O   . ALA A 313 ? 0.4736 0.4273 0.5080 -0.0544 0.0911  -0.0554 313 ALA A O   
2419 C CB  . ALA A 313 ? 0.3987 0.3448 0.4407 -0.0587 0.1068  -0.0621 313 ALA A CB  
2420 N N   . TRP A 314 ? 0.4206 0.3842 0.4788 -0.0450 0.0881  -0.0614 314 TRP A N   
2421 C CA  . TRP A 314 ? 0.4662 0.4264 0.5185 -0.0389 0.0824  -0.0598 314 TRP A CA  
2422 C C   . TRP A 314 ? 0.4831 0.4390 0.5420 -0.0336 0.0837  -0.0624 314 TRP A C   
2423 O O   . TRP A 314 ? 0.4698 0.4325 0.5470 -0.0306 0.0838  -0.0670 314 TRP A O   
2424 C CB  . TRP A 314 ? 0.4659 0.4326 0.5221 -0.0336 0.0741  -0.0607 314 TRP A CB  
2425 C CG  . TRP A 314 ? 0.4403 0.4097 0.4886 -0.0369 0.0731  -0.0579 314 TRP A CG  
2426 C CD1 . TRP A 314 ? 0.4573 0.4258 0.4985 -0.0436 0.0775  -0.0544 314 TRP A CD1 
2427 C CD2 . TRP A 314 ? 0.4604 0.4331 0.5078 -0.0327 0.0667  -0.0588 314 TRP A CD2 
2428 N NE1 . TRP A 314 ? 0.4462 0.4188 0.4848 -0.0435 0.0751  -0.0528 314 TRP A NE1 
2429 C CE2 . TRP A 314 ? 0.4169 0.3910 0.4577 -0.0369 0.0693  -0.0555 314 TRP A CE2 
2430 C CE3 . TRP A 314 ? 0.4697 0.4435 0.5209 -0.0254 0.0583  -0.0625 314 TRP A CE3 
2431 C CZ2 . TRP A 314 ? 0.4676 0.4433 0.5048 -0.0340 0.0658  -0.0557 314 TRP A CZ2 
2432 C CZ3 . TRP A 314 ? 0.4881 0.4622 0.5330 -0.0230 0.0536  -0.0631 314 TRP A CZ3 
2433 C CH2 . TRP A 314 ? 0.4554 0.4299 0.4929 -0.0272 0.0584  -0.0596 314 TRP A CH2 
2434 N N   . MET A 315 ? 0.4627 0.4072 0.5087 -0.0324 0.0850  -0.0596 315 MET A N   
2435 C CA  . MET A 315 ? 0.5272 0.4647 0.5774 -0.0281 0.0882  -0.0618 315 MET A CA  
2436 C C   . MET A 315 ? 0.5300 0.4574 0.5700 -0.0208 0.0831  -0.0589 315 MET A C   
2437 O O   . MET A 315 ? 0.5213 0.4415 0.5446 -0.0227 0.0821  -0.0541 315 MET A O   
2438 C CB  . MET A 315 ? 0.5154 0.4432 0.5567 -0.0352 0.0978  -0.0618 315 MET A CB  
2439 C CG  . MET A 315 ? 0.5447 0.4773 0.5878 -0.0428 0.1031  -0.0632 315 MET A CG  
2440 S SD  . MET A 315 ? 0.5604 0.4786 0.5926 -0.0483 0.1144  -0.0654 315 MET A SD  
2441 C CE  . MET A 315 ? 0.5263 0.4321 0.5357 -0.0547 0.1117  -0.0614 315 MET A CE  
2442 N N   . LYS A 316 ? 0.5346 0.4603 0.5849 -0.0123 0.0808  -0.0617 316 LYS A N   
2443 C CA  . LYS A 316 ? 0.6269 0.5399 0.6656 -0.0038 0.0754  -0.0586 316 LYS A CA  
2444 C C   . LYS A 316 ? 0.6257 0.5348 0.6769 0.0037  0.0767  -0.0620 316 LYS A C   
2445 O O   . LYS A 316 ? 0.5930 0.5146 0.6684 0.0059  0.0773  -0.0675 316 LYS A O   
2446 C CB  . LYS A 316 ? 0.6596 0.5765 0.6960 0.0033  0.0634  -0.0579 316 LYS A CB  
2447 C CG  . LYS A 316 ? 0.7258 0.6336 0.7591 0.0162  0.0538  -0.0575 316 LYS A CG  
2448 C CD  . LYS A 316 ? 0.7499 0.6597 0.7767 0.0225  0.0411  -0.0575 316 LYS A CD  
2449 C CE  . LYS A 316 ? 0.8337 0.7352 0.8349 0.0170  0.0449  -0.0517 316 LYS A CE  
2450 N NZ  . LYS A 316 ? 0.8638 0.7434 0.8392 0.0187  0.0496  -0.0448 316 LYS A NZ  
2451 N N   . PHE A 317 ? 0.6204 0.5118 0.6567 0.0073  0.0784  -0.0587 317 PHE A N   
2452 C CA  . PHE A 317 ? 0.6888 0.5748 0.7364 0.0171  0.0781  -0.0614 317 PHE A CA  
2453 C C   . PHE A 317 ? 0.7289 0.6216 0.7888 0.0299  0.0637  -0.0629 317 PHE A C   
2454 O O   . PHE A 317 ? 0.7240 0.6124 0.7685 0.0334  0.0542  -0.0592 317 PHE A O   
2455 C CB  . PHE A 317 ? 0.7220 0.5845 0.7482 0.0180  0.0831  -0.0571 317 PHE A CB  
2456 C CG  . PHE A 317 ? 0.7062 0.5612 0.7245 0.0067  0.0959  -0.0579 317 PHE A CG  
2457 C CD1 . PHE A 317 ? 0.6953 0.5496 0.7257 0.0071  0.1045  -0.0632 317 PHE A CD1 
2458 C CD2 . PHE A 317 ? 0.7633 0.6115 0.7624 -0.0042 0.0992  -0.0539 317 PHE A CD2 
2459 C CE1 . PHE A 317 ? 0.7002 0.5445 0.7188 -0.0029 0.1152  -0.0645 317 PHE A CE1 
2460 C CE2 . PHE A 317 ? 0.6905 0.5314 0.6819 -0.0145 0.1083  -0.0555 317 PHE A CE2 
2461 C CZ  . PHE A 317 ? 0.7164 0.5540 0.7152 -0.0138 0.1158  -0.0608 317 PHE A CZ  
2462 N N   . ASP A 318 ? 0.7057 0.6088 0.7939 0.0371  0.0621  -0.0687 318 ASP A N   
2463 C CA  . ASP A 318 ? 0.7021 0.6131 0.8068 0.0497  0.0463  -0.0714 318 ASP A CA  
2464 C C   . ASP A 318 ? 0.7445 0.6389 0.8430 0.0627  0.0411  -0.0693 318 ASP A C   
2465 O O   . ASP A 318 ? 0.6854 0.5613 0.7658 0.0611  0.0507  -0.0655 318 ASP A O   
2466 C CB  . ASP A 318 ? 0.7221 0.6573 0.8673 0.0497  0.0461  -0.0796 318 ASP A CB  
2467 C CG  . ASP A 318 ? 0.6490 0.5864 0.8170 0.0512  0.0590  -0.0838 318 ASP A CG  
2468 O OD1 . ASP A 318 ? 0.6960 0.6157 0.8485 0.0530  0.0667  -0.0810 318 ASP A OD1 
2469 O OD2 . ASP A 318 ? 0.6834 0.6396 0.8857 0.0502  0.0624  -0.0903 318 ASP A OD2 
2470 N N   . ALA A 319 ? 0.7836 0.6839 0.8981 0.0759  0.0249  -0.0720 319 ALA A N   
2471 C CA  . ALA A 319 ? 0.7854 0.6689 0.8932 0.0905  0.0170  -0.0696 319 ALA A CA  
2472 C C   . ALA A 319 ? 0.7895 0.6705 0.9150 0.0927  0.0298  -0.0722 319 ALA A C   
2473 O O   . ALA A 319 ? 0.8148 0.6745 0.9248 0.1009  0.0301  -0.0683 319 ALA A O   
2474 C CB  . ALA A 319 ? 0.7988 0.6917 0.9244 0.1047  -0.0052 -0.0733 319 ALA A CB  
2475 N N   . GLN A 320 ? 0.7281 0.6279 0.8838 0.0857  0.0416  -0.0787 320 GLN A N   
2476 C CA  . GLN A 320 ? 0.7186 0.6157 0.8919 0.0884  0.0554  -0.0822 320 GLN A CA  
2477 C C   . GLN A 320 ? 0.7006 0.5812 0.8481 0.0760  0.0745  -0.0795 320 GLN A C   
2478 O O   . GLN A 320 ? 0.7219 0.5964 0.8779 0.0771  0.0878  -0.0826 320 GLN A O   
2479 C CB  . GLN A 320 ? 0.7002 0.6244 0.9208 0.0884  0.0599  -0.0910 320 GLN A CB  
2480 C CG  . GLN A 320 ? 0.7157 0.6609 0.9666 0.0971  0.0399  -0.0953 320 GLN A CG  
2481 C CD  . GLN A 320 ? 0.7449 0.6868 1.0113 0.1159  0.0247  -0.0963 320 GLN A CD  
2482 O OE1 . GLN A 320 ? 0.7814 0.7138 1.0544 0.1230  0.0334  -0.0968 320 GLN A OE1 
2483 N NE2 . GLN A 320 ? 0.7797 0.7282 1.0510 0.1247  0.0013  -0.0970 320 GLN A NE2 
2484 N N   . GLY A 321 ? 0.7538 0.6271 0.8712 0.0645  0.0761  -0.0745 321 GLY A N   
2485 C CA  . GLY A 321 ? 0.7227 0.5811 0.8166 0.0523  0.0912  -0.0725 321 GLY A CA  
2486 C C   . GLY A 321 ? 0.6941 0.5654 0.7953 0.0392  0.1027  -0.0763 321 GLY A C   
2487 O O   . GLY A 321 ? 0.6800 0.5384 0.7615 0.0293  0.1140  -0.0755 321 GLY A O   
2488 N N   . ASN A 322 ? 0.6514 0.5458 0.7791 0.0388  0.0996  -0.0804 322 ASN A N   
2489 C CA  . ASN A 322 ? 0.6225 0.5270 0.7554 0.0268  0.1106  -0.0833 322 ASN A CA  
2490 C C   . ASN A 322 ? 0.6363 0.5426 0.7482 0.0168  0.1056  -0.0788 322 ASN A C   
2491 O O   . ASN A 322 ? 0.6175 0.5294 0.7274 0.0202  0.0924  -0.0762 322 ASN A O   
2492 C CB  . ASN A 322 ? 0.6382 0.5657 0.8105 0.0299  0.1112  -0.0896 322 ASN A CB  
2493 C CG  . ASN A 322 ? 0.6601 0.5889 0.8596 0.0401  0.1177  -0.0948 322 ASN A CG  
2494 O OD1 . ASN A 322 ? 0.7245 0.6438 0.9216 0.0372  0.1346  -0.0971 322 ASN A OD1 
2495 N ND2 . ASN A 322 ? 0.6918 0.6318 0.9171 0.0526  0.1040  -0.0969 322 ASN A ND2 
2496 N N   . LEU A 323 ? 0.5706 0.4708 0.6661 0.0050  0.1160  -0.0781 323 LEU A N   
2497 C CA  . LEU A 323 ? 0.5889 0.4932 0.6696 -0.0045 0.1124  -0.0746 323 LEU A CA  
2498 C C   . LEU A 323 ? 0.5243 0.4483 0.6270 -0.0067 0.1119  -0.0779 323 LEU A C   
2499 O O   . LEU A 323 ? 0.5548 0.4819 0.6682 -0.0105 0.1231  -0.0817 323 LEU A O   
2500 C CB  . LEU A 323 ? 0.5678 0.4582 0.6245 -0.0154 0.1215  -0.0731 323 LEU A CB  
2501 C CG  . LEU A 323 ? 0.5384 0.4330 0.5816 -0.0251 0.1179  -0.0695 323 LEU A CG  
2502 C CD1 . LEU A 323 ? 0.5780 0.4732 0.6131 -0.0225 0.1072  -0.0645 323 LEU A CD1 
2503 C CD2 . LEU A 323 ? 0.5477 0.4281 0.5694 -0.0349 0.1248  -0.0691 323 LEU A CD2 
2504 N N   . ARG A 324 ? 0.4972 0.4323 0.6055 -0.0041 0.0997  -0.0768 324 ARG A N   
2505 C CA  . ARG A 324 ? 0.5231 0.4762 0.6542 -0.0056 0.0976  -0.0805 324 ARG A CA  
2506 C C   . ARG A 324 ? 0.5248 0.4804 0.6411 -0.0142 0.0956  -0.0773 324 ARG A C   
2507 O O   . ARG A 324 ? 0.5068 0.4563 0.6028 -0.0148 0.0892  -0.0726 324 ARG A O   
2508 C CB  . ARG A 324 ? 0.5570 0.5213 0.7095 0.0049  0.0836  -0.0834 324 ARG A CB  
2509 C CG  . ARG A 324 ? 0.6166 0.5798 0.7875 0.0150  0.0841  -0.0867 324 ARG A CG  
2510 C CD  . ARG A 324 ? 0.6678 0.6468 0.8700 0.0244  0.0705  -0.0918 324 ARG A CD  
2511 N NE  . ARG A 324 ? 0.6159 0.6130 0.8515 0.0197  0.0769  -0.0980 324 ARG A NE  
2512 C CZ  . ARG A 324 ? 0.5715 0.5758 0.8371 0.0217  0.0877  -0.1031 324 ARG A CZ  
2513 N NH1 . ARG A 324 ? 0.5534 0.5490 0.8203 0.0290  0.0928  -0.1032 324 ARG A NH1 
2514 N NH2 . ARG A 324 ? 0.5416 0.5614 0.8369 0.0162  0.0949  -0.1082 324 ARG A NH2 
2515 N N   . ALA A 325 ? 0.4526 0.4165 0.5799 -0.0207 0.1022  -0.0797 325 ALA A N   
2516 C CA  . ALA A 325 ? 0.4627 0.4279 0.5769 -0.0287 0.1017  -0.0768 325 ALA A CA  
2517 C C   . ALA A 325 ? 0.4412 0.4208 0.5763 -0.0290 0.0976  -0.0801 325 ALA A C   
2518 O O   . ALA A 325 ? 0.4518 0.4398 0.6128 -0.0275 0.1018  -0.0852 325 ALA A O   
2519 C CB  . ALA A 325 ? 0.4551 0.4108 0.5550 -0.0373 0.1141  -0.0755 325 ALA A CB  
2520 N N   . ILE A 326 ? 0.4086 0.3907 0.5337 -0.0312 0.0903  -0.0776 326 ILE A N   
2521 C CA  . ILE A 326 ? 0.4355 0.4278 0.5752 -0.0338 0.0880  -0.0804 326 ILE A CA  
2522 C C   . ILE A 326 ? 0.4026 0.3902 0.5244 -0.0415 0.0922  -0.0762 326 ILE A C   
2523 O O   . ILE A 326 ? 0.4394 0.4191 0.5392 -0.0434 0.0920  -0.0713 326 ILE A O   
2524 C CB  . ILE A 326 ? 0.4536 0.4531 0.6006 -0.0274 0.0732  -0.0827 326 ILE A CB  
2525 C CG1 . ILE A 326 ? 0.4768 0.4683 0.5967 -0.0255 0.0665  -0.0774 326 ILE A CG1 
2526 C CG2 . ILE A 326 ? 0.5011 0.5064 0.6693 -0.0189 0.0663  -0.0876 326 ILE A CG2 
2527 C CD1 . ILE A 326 ? 0.4843 0.4788 0.5990 -0.0278 0.0618  -0.0771 326 ILE A CD1 
2528 N N   . ASN A 327 ? 0.4451 0.4375 0.5783 -0.0457 0.0956  -0.0782 327 ASN A N   
2529 C CA  . ASN A 327 ? 0.3945 0.3833 0.5137 -0.0513 0.0970  -0.0745 327 ASN A CA  
2530 C C   . ASN A 327 ? 0.4029 0.3981 0.5249 -0.0485 0.0861  -0.0755 327 ASN A C   
2531 O O   . ASN A 327 ? 0.4170 0.4197 0.5591 -0.0472 0.0826  -0.0806 327 ASN A O   
2532 C CB  . ASN A 327 ? 0.4128 0.3991 0.5394 -0.0573 0.1084  -0.0757 327 ASN A CB  
2533 C CG  . ASN A 327 ? 0.3991 0.3817 0.5144 -0.0617 0.1081  -0.0724 327 ASN A CG  
2534 O OD1 . ASN A 327 ? 0.3902 0.3709 0.4892 -0.0611 0.1015  -0.0685 327 ASN A OD1 
2535 N ND2 . ASN A 327 ? 0.4429 0.4238 0.5681 -0.0660 0.1161  -0.0739 327 ASN A ND2 
2536 N N   . PRO A 328 ? 0.4223 0.4144 0.5260 -0.0474 0.0807  -0.0713 328 PRO A N   
2537 C CA  . PRO A 328 ? 0.4012 0.3968 0.5047 -0.0438 0.0715  -0.0726 328 PRO A CA  
2538 C C   . PRO A 328 ? 0.3994 0.3961 0.5064 -0.0476 0.0728  -0.0732 328 PRO A C   
2539 O O   . PRO A 328 ? 0.4087 0.4074 0.5172 -0.0446 0.0656  -0.0757 328 PRO A O   
2540 C CB  . PRO A 328 ? 0.4228 0.4134 0.5056 -0.0417 0.0691  -0.0674 328 PRO A CB  
2541 C CG  . PRO A 328 ? 0.3955 0.3815 0.4691 -0.0474 0.0768  -0.0631 328 PRO A CG  
2542 C CD  . PRO A 328 ? 0.3863 0.3712 0.4697 -0.0493 0.0830  -0.0658 328 PRO A CD  
2543 N N   . GLU A 329 ? 0.4103 0.4034 0.5162 -0.0536 0.0815  -0.0710 329 GLU A N   
2544 C CA  . GLU A 329 ? 0.3889 0.3798 0.4955 -0.0572 0.0837  -0.0705 329 GLU A CA  
2545 C C   . GLU A 329 ? 0.3907 0.3848 0.5193 -0.0596 0.0866  -0.0761 329 GLU A C   
2546 O O   . GLU A 329 ? 0.4354 0.4342 0.5805 -0.0592 0.0888  -0.0801 329 GLU A O   
2547 C CB  . GLU A 329 ? 0.4006 0.3828 0.4920 -0.0619 0.0909  -0.0648 329 GLU A CB  
2548 C CG  . GLU A 329 ? 0.4040 0.3842 0.4779 -0.0609 0.0878  -0.0598 329 GLU A CG  
2549 C CD  . GLU A 329 ? 0.4571 0.4295 0.5169 -0.0645 0.0901  -0.0548 329 GLU A CD  
2550 O OE1 . GLU A 329 ? 0.4606 0.4245 0.5124 -0.0682 0.0961  -0.0535 329 GLU A OE1 
2551 O OE2 . GLU A 329 ? 0.4274 0.4011 0.4834 -0.0631 0.0856  -0.0522 329 GLU A OE2 
2552 N N   . ASN A 330 ? 0.3832 0.3744 0.5138 -0.0621 0.0871  -0.0765 330 ASN A N   
2553 C CA  . ASN A 330 ? 0.4144 0.4073 0.5667 -0.0658 0.0905  -0.0818 330 ASN A CA  
2554 C C   . ASN A 330 ? 0.3973 0.3794 0.5447 -0.0722 0.1026  -0.0782 330 ASN A C   
2555 O O   . ASN A 330 ? 0.3739 0.3551 0.5387 -0.0765 0.1079  -0.0818 330 ASN A O   
2556 C CB  . ASN A 330 ? 0.3767 0.3727 0.5354 -0.0631 0.0798  -0.0867 330 ASN A CB  
2557 C CG  . ASN A 330 ? 0.4199 0.4214 0.6078 -0.0663 0.0790  -0.0948 330 ASN A CG  
2558 O OD1 . ASN A 330 ? 0.4270 0.4356 0.6355 -0.0677 0.0825  -0.0983 330 ASN A OD1 
2559 N ND2 . ASN A 330 ? 0.4311 0.4295 0.6226 -0.0674 0.0744  -0.0982 330 ASN A ND2 
2560 N N   . GLY A 331 ? 0.3905 0.3632 0.5142 -0.0729 0.1064  -0.0711 331 GLY A N   
2561 C CA  . GLY A 331 ? 0.3924 0.3510 0.5049 -0.0777 0.1166  -0.0667 331 GLY A CA  
2562 C C   . GLY A 331 ? 0.4220 0.3719 0.5098 -0.0777 0.1191  -0.0606 331 GLY A C   
2563 O O   . GLY A 331 ? 0.4256 0.3814 0.5084 -0.0748 0.1137  -0.0602 331 GLY A O   
2564 N N   . PHE A 332 ? 0.4128 0.3466 0.4838 -0.0810 0.1267  -0.0558 332 PHE A N   
2565 C CA  . PHE A 332 ? 0.4122 0.3344 0.4561 -0.0810 0.1268  -0.0501 332 PHE A CA  
2566 C C   . PHE A 332 ? 0.4378 0.3522 0.4654 -0.0791 0.1199  -0.0446 332 PHE A C   
2567 O O   . PHE A 332 ? 0.4428 0.3491 0.4712 -0.0801 0.1231  -0.0434 332 PHE A O   
2568 C CB  . PHE A 332 ? 0.4687 0.3741 0.5005 -0.0854 0.1414  -0.0489 332 PHE A CB  
2569 C CG  . PHE A 332 ? 0.4796 0.3920 0.5330 -0.0873 0.1514  -0.0546 332 PHE A CG  
2570 C CD1 . PHE A 332 ? 0.4606 0.3847 0.5220 -0.0846 0.1473  -0.0579 332 PHE A CD1 
2571 C CD2 . PHE A 332 ? 0.4524 0.3595 0.5197 -0.0917 0.1653  -0.0568 332 PHE A CD2 
2572 C CE1 . PHE A 332 ? 0.5281 0.4593 0.6117 -0.0851 0.1556  -0.0633 332 PHE A CE1 
2573 C CE2 . PHE A 332 ? 0.4926 0.4084 0.5849 -0.0931 0.1745  -0.0625 332 PHE A CE2 
2574 C CZ  . PHE A 332 ? 0.4866 0.4149 0.5873 -0.0892 0.1692  -0.0659 332 PHE A CZ  
2575 N N   . PHE A 333 ? 0.4479 0.3646 0.4628 -0.0764 0.1104  -0.0415 333 PHE A N   
2576 C CA  . PHE A 333 ? 0.4492 0.3607 0.4510 -0.0736 0.1021  -0.0363 333 PHE A CA  
2577 C C   . PHE A 333 ? 0.4418 0.3385 0.4179 -0.0750 0.1012  -0.0321 333 PHE A C   
2578 O O   . PHE A 333 ? 0.4284 0.3303 0.3993 -0.0740 0.0927  -0.0312 333 PHE A O   
2579 C CB  . PHE A 333 ? 0.4396 0.3686 0.4531 -0.0692 0.0913  -0.0371 333 PHE A CB  
2580 C CG  . PHE A 333 ? 0.4265 0.3543 0.4345 -0.0653 0.0831  -0.0327 333 PHE A CG  
2581 C CD1 . PHE A 333 ? 0.4850 0.4073 0.4956 -0.0630 0.0838  -0.0317 333 PHE A CD1 
2582 C CD2 . PHE A 333 ? 0.4826 0.4152 0.4855 -0.0637 0.0745  -0.0300 333 PHE A CD2 
2583 C CE1 . PHE A 333 ? 0.4964 0.4178 0.5039 -0.0582 0.0763  -0.0277 333 PHE A CE1 
2584 C CE2 . PHE A 333 ? 0.4674 0.4011 0.4701 -0.0593 0.0664  -0.0262 333 PHE A CE2 
2585 C CZ  . PHE A 333 ? 0.4683 0.3965 0.4731 -0.0560 0.0674  -0.0250 333 PHE A CZ  
2586 N N   . GLY A 334 ? 0.4740 0.3505 0.4333 -0.0778 0.1106  -0.0298 334 GLY A N   
2587 C CA  . GLY A 334 ? 0.4494 0.3071 0.3798 -0.0795 0.1121  -0.0270 334 GLY A CA  
2588 C C   . GLY A 334 ? 0.4971 0.3366 0.4016 -0.0770 0.1047  -0.0206 334 GLY A C   
2589 O O   . GLY A 334 ? 0.5350 0.3696 0.4408 -0.0748 0.1042  -0.0176 334 GLY A O   
2590 N N   . VAL A 335 ? 0.5104 0.3386 0.3906 -0.0771 0.0979  -0.0189 335 VAL A N   
2591 C CA  . VAL A 335 ? 0.5266 0.3349 0.3777 -0.0742 0.0882  -0.0131 335 VAL A CA  
2592 C C   . VAL A 335 ? 0.5585 0.3379 0.3846 -0.0754 0.1017  -0.0093 335 VAL A C   
2593 O O   . VAL A 335 ? 0.6170 0.3829 0.4313 -0.0796 0.1169  -0.0111 335 VAL A O   
2594 C CB  . VAL A 335 ? 0.5451 0.3466 0.3755 -0.0752 0.0783  -0.0139 335 VAL A CB  
2595 C CG1 . VAL A 335 ? 0.6137 0.3909 0.4098 -0.0719 0.0670  -0.0084 335 VAL A CG1 
2596 C CG2 . VAL A 335 ? 0.5709 0.4000 0.4271 -0.0748 0.0659  -0.0172 335 VAL A CG2 
2597 N N   . ALA A 336 ? 0.5871 0.3553 0.4048 -0.0716 0.0974  -0.0039 336 ALA A N   
2598 C CA  . ALA A 336 ? 0.5841 0.3215 0.3759 -0.0728 0.1114  0.0007  336 ALA A CA  
2599 C C   . ALA A 336 ? 0.6754 0.3797 0.4194 -0.0720 0.1095  0.0050  336 ALA A C   
2600 O O   . ALA A 336 ? 0.7168 0.3993 0.4398 -0.0762 0.1272  0.0050  336 ALA A O   
2601 C CB  . ALA A 336 ? 0.6290 0.3623 0.4267 -0.0688 0.1087  0.0052  336 ALA A CB  
2602 N N   . PRO A 337 ? 0.6905 0.3887 0.4153 -0.0666 0.0890  0.0084  337 PRO A N   
2603 C CA  . PRO A 337 ? 0.7460 0.4077 0.4198 -0.0651 0.0857  0.0126  337 PRO A CA  
2604 C C   . PRO A 337 ? 0.7500 0.4016 0.4062 -0.0706 0.0969  0.0080  337 PRO A C   
2605 O O   . PRO A 337 ? 0.7845 0.4606 0.4652 -0.0737 0.0952  0.0015  337 PRO A O   
2606 C CB  . PRO A 337 ? 0.7274 0.3961 0.3977 -0.0589 0.0577  0.0142  337 PRO A CB  
2607 C CG  . PRO A 337 ? 0.7458 0.4434 0.4574 -0.0553 0.0510  0.0145  337 PRO A CG  
2608 C CD  . PRO A 337 ? 0.6214 0.3440 0.3696 -0.0612 0.0676  0.0085  337 PRO A CD  
2609 N N   . GLY A 338 ? 0.7528 0.3658 0.3648 -0.0716 0.1099  0.0115  338 GLY A N   
2610 C CA  . GLY A 338 ? 0.7873 0.3852 0.3786 -0.0763 0.1248  0.0074  338 GLY A CA  
2611 C C   . GLY A 338 ? 0.8065 0.4086 0.4190 -0.0820 0.1536  0.0045  338 GLY A C   
2612 O O   . GLY A 338 ? 0.8353 0.4186 0.4267 -0.0853 0.1705  0.0021  338 GLY A O   
2613 N N   . THR A 339 ? 0.7438 0.3698 0.3981 -0.0833 0.1594  0.0040  339 THR A N   
2614 C CA  . THR A 339 ? 0.7563 0.3884 0.4363 -0.0889 0.1848  0.0008  339 THR A CA  
2615 C C   . THR A 339 ? 0.8022 0.3968 0.4512 -0.0907 0.2056  0.0068  339 THR A C   
2616 O O   . THR A 339 ? 0.8227 0.4041 0.4612 -0.0880 0.2015  0.0133  339 THR A O   
2617 C CB  . THR A 339 ? 0.7098 0.3780 0.4425 -0.0894 0.1810  -0.0022 339 THR A CB  
2618 O OG1 . THR A 339 ? 0.6826 0.3819 0.4393 -0.0872 0.1624  -0.0067 339 THR A OG1 
2619 C CG2 . THR A 339 ? 0.7162 0.3947 0.4812 -0.0952 0.2038  -0.0069 339 THR A CG2 
2620 N N   . SER A 340 ? 0.7885 0.3655 0.4247 -0.0951 0.2296  0.0048  340 SER A N   
2621 C CA  . SER A 340 ? 0.8726 0.4123 0.4797 -0.0977 0.2537  0.0105  340 SER A CA  
2622 C C   . SER A 340 ? 0.9130 0.4555 0.5414 -0.1042 0.2833  0.0050  340 SER A C   
2623 O O   . SER A 340 ? 0.8624 0.4324 0.5218 -0.1055 0.2833  -0.0027 340 SER A O   
2624 C CB  . SER A 340 ? 0.9421 0.4355 0.4799 -0.0935 0.2500  0.0170  340 SER A CB  
2625 O OG  . SER A 340 ? 1.0473 0.5338 0.5638 -0.0936 0.2505  0.0122  340 SER A OG  
2626 N N   . VAL A 341 ? 0.9121 0.4243 0.5231 -0.1080 0.3095  0.0095  341 VAL A N   
2627 C CA  . VAL A 341 ? 0.9479 0.4665 0.5860 -0.1109 0.3336  0.0021  341 VAL A CA  
2628 C C   . VAL A 341 ? 0.9426 0.4523 0.5583 -0.1090 0.3370  -0.0026 341 VAL A C   
2629 O O   . VAL A 341 ? 0.9796 0.5096 0.6314 -0.1103 0.3484  -0.0107 341 VAL A O   
2630 C CB  . VAL A 341 ? 1.0285 0.5198 0.6544 -0.1106 0.3516  0.0047  341 VAL A CB  
2631 C CG1 . VAL A 341 ? 1.0933 0.5835 0.7371 -0.1116 0.3748  -0.0027 341 VAL A CG1 
2632 C CG2 . VAL A 341 ? 1.0551 0.5638 0.7187 -0.1136 0.3508  0.0062  341 VAL A CG2 
2633 N N   . LYS A 342 ? 0.9523 0.4318 0.5093 -0.1054 0.3254  0.0021  342 LYS A N   
2634 C CA  . LYS A 342 ? 0.9368 0.4035 0.4687 -0.1035 0.3283  -0.0029 342 LYS A CA  
2635 C C   . LYS A 342 ? 0.9937 0.4895 0.5431 -0.1043 0.3129  -0.0079 342 LYS A C   
2636 O O   . LYS A 342 ? 0.9805 0.4804 0.5354 -0.1043 0.3208  -0.0147 342 LYS A O   
2637 C CB  . LYS A 342 ? 1.1508 0.5689 0.6099 -0.0988 0.3219  0.0026  342 LYS A CB  
2638 C CG  . LYS A 342 ? 1.2490 0.6579 0.6698 -0.0961 0.2939  0.0090  342 LYS A CG  
2639 C CD  . LYS A 342 ? 1.4135 0.7737 0.7632 -0.0905 0.2862  0.0124  342 LYS A CD  
2640 C CE  . LYS A 342 ? 1.5030 0.8614 0.8225 -0.0868 0.2531  0.0130  342 LYS A CE  
2641 N NZ  . LYS A 342 ? 1.4139 0.7931 0.7494 -0.0883 0.2468  0.0033  342 LYS A NZ  
2642 N N   . THR A 343 ? 0.9146 0.4377 0.4850 -0.1016 0.2838  -0.0071 343 THR A N   
2643 C CA  . THR A 343 ? 0.8859 0.4408 0.4807 -0.0998 0.2626  -0.0135 343 THR A CA  
2644 C C   . THR A 343 ? 0.8596 0.4592 0.5207 -0.1020 0.2655  -0.0195 343 THR A C   
2645 O O   . THR A 343 ? 0.8427 0.4613 0.5239 -0.1019 0.2633  -0.0261 343 THR A O   
2646 C CB  . THR A 343 ? 0.8807 0.4425 0.4648 -0.0955 0.2297  -0.0101 343 THR A CB  
2647 O OG1 . THR A 343 ? 0.8510 0.4301 0.4636 -0.0950 0.2236  -0.0061 343 THR A OG1 
2648 C CG2 . THR A 343 ? 0.9935 0.5120 0.5115 -0.0923 0.2213  -0.0051 343 THR A CG2 
2649 N N   . ASN A 344 ? 0.7606 0.3766 0.4554 -0.1037 0.2685  -0.0176 344 ASN A N   
2650 C CA  . ASN A 344 ? 0.7568 0.4145 0.5125 -0.1052 0.2671  -0.0235 344 ASN A CA  
2651 C C   . ASN A 344 ? 0.7750 0.4349 0.5576 -0.1094 0.2847  -0.0224 344 ASN A C   
2652 O O   . ASN A 344 ? 0.7346 0.4120 0.5423 -0.1093 0.2738  -0.0213 344 ASN A O   
2653 C CB  . ASN A 344 ? 0.6493 0.3352 0.4233 -0.1016 0.2378  -0.0239 344 ASN A CB  
2654 C CG  . ASN A 344 ? 0.6658 0.3911 0.4932 -0.1017 0.2338  -0.0308 344 ASN A CG  
2655 O OD1 . ASN A 344 ? 0.6803 0.4156 0.5376 -0.1044 0.2507  -0.0352 344 ASN A OD1 
2656 N ND2 . ASN A 344 ? 0.6367 0.3842 0.4767 -0.0986 0.2111  -0.0316 344 ASN A ND2 
2657 N N   . PRO A 345 ? 0.7622 0.4038 0.5415 -0.1134 0.3134  -0.0231 345 PRO A N   
2658 C CA  . PRO A 345 ? 0.7501 0.3943 0.5591 -0.1178 0.3301  -0.0231 345 PRO A CA  
2659 C C   . PRO A 345 ? 0.7380 0.4242 0.6108 -0.1200 0.3244  -0.0295 345 PRO A C   
2660 O O   . PRO A 345 ? 0.7446 0.4374 0.6412 -0.1222 0.3253  -0.0292 345 PRO A O   
2661 C CB  . PRO A 345 ? 0.8198 0.4467 0.6235 -0.1164 0.3515  -0.0269 345 PRO A CB  
2662 C CG  . PRO A 345 ? 0.8018 0.4295 0.5922 -0.1139 0.3497  -0.0308 345 PRO A CG  
2663 C CD  . PRO A 345 ? 0.8022 0.4212 0.5534 -0.1133 0.3308  -0.0251 345 PRO A CD  
2664 N N   . ASN A 346 ? 0.6948 0.4093 0.5949 -0.1177 0.3151  -0.0361 346 ASN A N   
2665 C CA  . ASN A 346 ? 0.6452 0.3981 0.6025 -0.1182 0.3064  -0.0427 346 ASN A CA  
2666 C C   . ASN A 346 ? 0.6516 0.4184 0.6130 -0.1156 0.2811  -0.0405 346 ASN A C   
2667 O O   . ASN A 346 ? 0.6700 0.4578 0.6699 -0.1173 0.2768  -0.0441 346 ASN A O   
2668 C CB  . ASN A 346 ? 0.6542 0.4301 0.6350 -0.1149 0.3022  -0.0498 346 ASN A CB  
2669 C CG  . ASN A 346 ? 0.7140 0.4834 0.7057 -0.1155 0.3254  -0.0541 346 ASN A CG  
2670 O OD1 . ASN A 346 ? 0.7016 0.4663 0.6805 -0.1126 0.3291  -0.0563 346 ASN A OD1 
2671 N ND2 . ASN A 346 ? 0.6386 0.4073 0.6537 -0.1170 0.3370  -0.0561 346 ASN A ND2 
2672 N N   . ALA A 347 ? 0.6355 0.3902 0.5583 -0.1113 0.2646  -0.0352 347 ALA A N   
2673 C CA  . ALA A 347 ? 0.6275 0.3913 0.5516 -0.1085 0.2438  -0.0322 347 ALA A CA  
2674 C C   . ALA A 347 ? 0.6773 0.4231 0.5954 -0.1116 0.2524  -0.0274 347 ALA A C   
2675 O O   . ALA A 347 ? 0.6460 0.4064 0.5883 -0.1116 0.2434  -0.0285 347 ALA A O   
2676 C CB  . ALA A 347 ? 0.6408 0.3958 0.5281 -0.1034 0.2251  -0.0278 347 ALA A CB  
2677 N N   . ILE A 348 ? 0.7173 0.4288 0.6010 -0.1142 0.2704  -0.0220 348 ILE A N   
2678 C CA  . ILE A 348 ? 0.6696 0.3583 0.5422 -0.1172 0.2804  -0.0163 348 ILE A CA  
2679 C C   . ILE A 348 ? 0.7347 0.4415 0.6574 -0.1235 0.2921  -0.0219 348 ILE A C   
2680 O O   . ILE A 348 ? 0.7453 0.4527 0.6795 -0.1246 0.2874  -0.0205 348 ILE A O   
2681 C CB  . ILE A 348 ? 0.7671 0.4130 0.5918 -0.1189 0.3010  -0.0097 348 ILE A CB  
2682 C CG1 . ILE A 348 ? 0.8415 0.4673 0.6139 -0.1123 0.2851  -0.0043 348 ILE A CG1 
2683 C CG2 . ILE A 348 ? 0.8862 0.5064 0.7001 -0.1224 0.3138  -0.0033 348 ILE A CG2 
2684 C CD1 . ILE A 348 ? 0.8604 0.4852 0.6189 -0.1067 0.2609  0.0011  348 ILE A CD1 
2685 N N   . LYS A 349 ? 0.6979 0.4190 0.6521 -0.1275 0.3074  -0.0287 349 LYS A N   
2686 C CA  . LYS A 349 ? 0.7274 0.4721 0.7340 -0.1302 0.3110  -0.0366 349 LYS A CA  
2687 C C   . LYS A 349 ? 0.6713 0.4461 0.7127 -0.1306 0.2913  -0.0411 349 LYS A C   
2688 O O   . LYS A 349 ? 0.7027 0.4887 0.7763 -0.1336 0.2901  -0.0452 349 LYS A O   
2689 C CB  . LYS A 349 ? 0.7347 0.4936 0.7692 -0.1293 0.3228  -0.0445 349 LYS A CB  
2690 C CG  . LYS A 349 ? 0.8799 0.6095 0.8856 -0.1285 0.3437  -0.0420 349 LYS A CG  
2691 C CD  . LYS A 349 ? 0.9400 0.6864 0.9824 -0.1277 0.3548  -0.0507 349 LYS A CD  
2692 C CE  . LYS A 349 ? 1.0435 0.7600 1.0576 -0.1266 0.3765  -0.0491 349 LYS A CE  
2693 N NZ  . LYS A 349 ? 1.0493 0.7829 1.1046 -0.1258 0.3874  -0.0576 349 LYS A NZ  
2694 N N   . THR A 350 ? 0.6652 0.4552 0.6978 -0.1235 0.2702  -0.0418 350 THR A N   
2695 C CA  . THR A 350 ? 0.6196 0.4399 0.6826 -0.1202 0.2488  -0.0475 350 THR A CA  
2696 C C   . THR A 350 ? 0.5971 0.4117 0.6496 -0.1183 0.2356  -0.0436 350 THR A C   
2697 O O   . THR A 350 ? 0.5600 0.3919 0.6424 -0.1187 0.2264  -0.0489 350 THR A O   
2698 C CB  . THR A 350 ? 0.6242 0.4601 0.6803 -0.1136 0.2331  -0.0490 350 THR A CB  
2699 O OG1 . THR A 350 ? 0.6173 0.4579 0.6842 -0.1147 0.2454  -0.0530 350 THR A OG1 
2700 C CG2 . THR A 350 ? 0.5367 0.4008 0.6200 -0.1097 0.2124  -0.0543 350 THR A CG2 
2701 N N   . ILE A 351 ? 0.5809 0.3702 0.5909 -0.1155 0.2339  -0.0348 351 ILE A N   
2702 C CA  . ILE A 351 ? 0.5889 0.3754 0.5867 -0.1108 0.2174  -0.0309 351 ILE A CA  
2703 C C   . ILE A 351 ? 0.6192 0.3851 0.6145 -0.1147 0.2270  -0.0275 351 ILE A C   
2704 O O   . ILE A 351 ? 0.6463 0.4037 0.6268 -0.1103 0.2159  -0.0231 351 ILE A O   
2705 C CB  . ILE A 351 ? 0.5494 0.3227 0.5058 -0.1043 0.2058  -0.0236 351 ILE A CB  
2706 C CG1 . ILE A 351 ? 0.6264 0.3646 0.5430 -0.1062 0.2209  -0.0164 351 ILE A CG1 
2707 C CG2 . ILE A 351 ? 0.5216 0.3169 0.4832 -0.1006 0.1937  -0.0274 351 ILE A CG2 
2708 C CD1 . ILE A 351 ? 0.6796 0.4039 0.5546 -0.0998 0.2075  -0.0103 351 ILE A CD1 
2709 N N   . GLN A 352 ? 0.6124 0.3697 0.6234 -0.1228 0.2481  -0.0296 352 GLN A N   
2710 C CA  . GLN A 352 ? 0.6650 0.3996 0.6732 -0.1276 0.2596  -0.0261 352 GLN A CA  
2711 C C   . GLN A 352 ? 0.6049 0.3577 0.6539 -0.1308 0.2532  -0.0336 352 GLN A C   
2712 O O   . GLN A 352 ? 0.6735 0.4087 0.7257 -0.1359 0.2631  -0.0321 352 GLN A O   
2713 C CB  . GLN A 352 ? 0.7071 0.4199 0.7111 -0.1357 0.2880  -0.0241 352 GLN A CB  
2714 C CG  . GLN A 352 ? 0.7960 0.4857 0.7538 -0.1322 0.2944  -0.0168 352 GLN A CG  
2715 C CD  . GLN A 352 ? 0.9168 0.5898 0.8659 -0.1338 0.3166  -0.0168 352 GLN A CD  
2716 O OE1 . GLN A 352 ? 1.0424 0.7277 1.0275 -0.1371 0.3270  -0.0236 352 GLN A OE1 
2717 N NE2 . GLN A 352 ? 0.9074 0.5513 0.8075 -0.1307 0.3231  -0.0098 352 GLN A NE2 
2718 N N   . LYS A 353 ? 0.5692 0.3541 0.6468 -0.1278 0.2367  -0.0418 353 LYS A N   
2719 C CA  . LYS A 353 ? 0.6079 0.4070 0.7175 -0.1296 0.2276  -0.0492 353 LYS A CA  
2720 C C   . LYS A 353 ? 0.5688 0.3946 0.6871 -0.1219 0.2047  -0.0542 353 LYS A C   
2721 O O   . LYS A 353 ? 0.5874 0.4269 0.7016 -0.1178 0.1992  -0.0545 353 LYS A O   
2722 C CB  . LYS A 353 ? 0.6747 0.4835 0.8279 -0.1396 0.2411  -0.0578 353 LYS A CB  
2723 C CG  . LYS A 353 ? 0.6703 0.5063 0.8536 -0.1401 0.2402  -0.0655 353 LYS A CG  
2724 C CD  . LYS A 353 ? 0.7260 0.5727 0.9489 -0.1453 0.2504  -0.0731 353 LYS A CD  
2725 C CE  . LYS A 353 ? 0.7860 0.6605 1.0405 -0.1435 0.2476  -0.0809 353 LYS A CE  
2726 N NZ  . LYS A 353 ? 0.9284 0.8144 1.2221 -0.1465 0.2553  -0.0885 353 LYS A NZ  
2727 N N   . ASN A 354 ? 0.5555 0.3854 0.6828 -0.1197 0.1923  -0.0576 354 ASN A N   
2728 C CA  . ASN A 354 ? 0.5317 0.3840 0.6673 -0.1127 0.1722  -0.0629 354 ASN A CA  
2729 C C   . ASN A 354 ? 0.4909 0.3466 0.5987 -0.1042 0.1626  -0.0566 354 ASN A C   
2730 O O   . ASN A 354 ? 0.5149 0.3907 0.6299 -0.0999 0.1517  -0.0604 354 ASN A O   
2731 C CB  . ASN A 354 ? 0.5243 0.4014 0.6965 -0.1155 0.1686  -0.0735 354 ASN A CB  
2732 C CG  . ASN A 354 ? 0.5823 0.4589 0.7877 -0.1246 0.1762  -0.0811 354 ASN A CG  
2733 O OD1 . ASN A 354 ? 0.5791 0.4439 0.7852 -0.1267 0.1750  -0.0822 354 ASN A OD1 
2734 N ND2 . ASN A 354 ? 0.5773 0.4665 0.8122 -0.1302 0.1846  -0.0866 354 ASN A ND2 
2735 N N   . THR A 355 ? 0.5246 0.3596 0.6003 -0.1015 0.1658  -0.0471 355 THR A N   
2736 C CA  . THR A 355 ? 0.4931 0.3299 0.5439 -0.0949 0.1576  -0.0412 355 THR A CA  
2737 C C   . THR A 355 ? 0.5335 0.3605 0.5636 -0.0876 0.1473  -0.0351 355 THR A C   
2738 O O   . THR A 355 ? 0.5507 0.3566 0.5699 -0.0881 0.1524  -0.0309 355 THR A O   
2739 C CB  . THR A 355 ? 0.5411 0.3622 0.5705 -0.0980 0.1702  -0.0356 355 THR A CB  
2740 O OG1 . THR A 355 ? 0.5112 0.3448 0.5629 -0.1033 0.1794  -0.0417 355 THR A OG1 
2741 C CG2 . THR A 355 ? 0.4698 0.2905 0.4724 -0.0916 0.1601  -0.0300 355 THR A CG2 
2742 N N   . ILE A 356 ? 0.5033 0.3454 0.5298 -0.0807 0.1335  -0.0347 356 ILE A N   
2743 C CA  . ILE A 356 ? 0.4815 0.3188 0.4929 -0.0728 0.1229  -0.0294 356 ILE A CA  
2744 C C   . ILE A 356 ? 0.4905 0.3207 0.4766 -0.0698 0.1193  -0.0221 356 ILE A C   
2745 O O   . ILE A 356 ? 0.5137 0.3572 0.5006 -0.0701 0.1159  -0.0235 356 ILE A O   
2746 C CB  . ILE A 356 ? 0.4916 0.3506 0.5186 -0.0671 0.1110  -0.0343 356 ILE A CB  
2747 C CG1 . ILE A 356 ? 0.5361 0.3991 0.5841 -0.0694 0.1124  -0.0423 356 ILE A CG1 
2748 C CG2 . ILE A 356 ? 0.4560 0.3121 0.4706 -0.0585 0.1013  -0.0287 356 ILE A CG2 
2749 C CD1 . ILE A 356 ? 0.5459 0.4243 0.6030 -0.0629 0.1017  -0.0469 356 ILE A CD1 
2750 N N   . PHE A 357 ? 0.4893 0.2971 0.4520 -0.0667 0.1188  -0.0144 357 PHE A N   
2751 C CA  . PHE A 357 ? 0.5379 0.3364 0.4742 -0.0630 0.1120  -0.0077 357 PHE A CA  
2752 C C   . PHE A 357 ? 0.5370 0.3435 0.4740 -0.0539 0.0963  -0.0049 357 PHE A C   
2753 O O   . PHE A 357 ? 0.5706 0.3739 0.5146 -0.0497 0.0944  -0.0044 357 PHE A O   
2754 C CB  . PHE A 357 ? 0.5387 0.3035 0.4439 -0.0647 0.1209  -0.0003 357 PHE A CB  
2755 C CG  . PHE A 357 ? 0.5438 0.2977 0.4479 -0.0738 0.1396  -0.0024 357 PHE A CG  
2756 C CD1 . PHE A 357 ? 0.5451 0.2940 0.4662 -0.0793 0.1525  -0.0055 357 PHE A CD1 
2757 C CD2 . PHE A 357 ? 0.6209 0.3689 0.5078 -0.0768 0.1449  -0.0016 357 PHE A CD2 
2758 C CE1 . PHE A 357 ? 0.5993 0.3399 0.5243 -0.0880 0.1709  -0.0076 357 PHE A CE1 
2759 C CE2 . PHE A 357 ? 0.6062 0.3442 0.4939 -0.0847 0.1644  -0.0035 357 PHE A CE2 
2760 C CZ  . PHE A 357 ? 0.5827 0.3182 0.4912 -0.0904 0.1776  -0.0065 357 PHE A CZ  
2761 N N   . THR A 358 ? 0.5107 0.3267 0.4413 -0.0508 0.0855  -0.0032 358 THR A N   
2762 C CA  . THR A 358 ? 0.5488 0.3743 0.4835 -0.0423 0.0705  -0.0006 358 THR A CA  
2763 C C   . THR A 358 ? 0.5785 0.3888 0.4865 -0.0392 0.0610  0.0061  358 THR A C   
2764 O O   . THR A 358 ? 0.5568 0.3673 0.4538 -0.0432 0.0600  0.0054  358 THR A O   
2765 C CB  . THR A 358 ? 0.5352 0.3910 0.4945 -0.0416 0.0647  -0.0060 358 THR A CB  
2766 O OG1 . THR A 358 ? 0.5249 0.3919 0.5042 -0.0445 0.0728  -0.0125 358 THR A OG1 
2767 C CG2 . THR A 358 ? 0.5216 0.3883 0.4911 -0.0330 0.0525  -0.0038 358 THR A CG2 
2768 N N   . ASN A 359 ? 0.5994 0.3946 0.4957 -0.0318 0.0533  0.0121  359 ASN A N   
2769 C CA  . ASN A 359 ? 0.6395 0.4217 0.5125 -0.0263 0.0391  0.0183  359 ASN A CA  
2770 C C   . ASN A 359 ? 0.6653 0.4163 0.4991 -0.0305 0.0448  0.0225  359 ASN A C   
2771 O O   . ASN A 359 ? 0.6685 0.4109 0.4808 -0.0285 0.0332  0.0253  359 ASN A O   
2772 C CB  . ASN A 359 ? 0.5838 0.3918 0.4728 -0.0249 0.0251  0.0154  359 ASN A CB  
2773 C CG  . ASN A 359 ? 0.6024 0.4356 0.5246 -0.0181 0.0177  0.0135  359 ASN A CG  
2774 O OD1 . ASN A 359 ? 0.6027 0.4306 0.5308 -0.0121 0.0189  0.0155  359 ASN A OD1 
2775 N ND2 . ASN A 359 ? 0.6053 0.4646 0.5488 -0.0191 0.0114  0.0096  359 ASN A ND2 
2776 N N   . VAL A 360 ? 0.6647 0.3969 0.4880 -0.0361 0.0627  0.0229  360 VAL A N   
2777 C CA  . VAL A 360 ? 0.6569 0.3533 0.4394 -0.0386 0.0707  0.0285  360 VAL A CA  
2778 C C   . VAL A 360 ? 0.7391 0.4060 0.5012 -0.0326 0.0710  0.0363  360 VAL A C   
2779 O O   . VAL A 360 ? 0.6732 0.3484 0.4555 -0.0275 0.0670  0.0364  360 VAL A O   
2780 C CB  . VAL A 360 ? 0.6386 0.3306 0.4220 -0.0493 0.0928  0.0244  360 VAL A CB  
2781 C CG1 . VAL A 360 ? 0.6225 0.3434 0.4270 -0.0540 0.0918  0.0167  360 VAL A CG1 
2782 C CG2 . VAL A 360 ? 0.6256 0.3178 0.4305 -0.0530 0.1077  0.0223  360 VAL A CG2 
2783 N N   . ALA A 361 ? 0.7319 0.3610 0.4507 -0.0327 0.0763  0.0431  361 ALA A N   
2784 C CA  . ALA A 361 ? 0.7834 0.3790 0.4773 -0.0270 0.0778  0.0515  361 ALA A CA  
2785 C C   . ALA A 361 ? 0.7804 0.3638 0.4824 -0.0346 0.1019  0.0508  361 ALA A C   
2786 O O   . ALA A 361 ? 0.7662 0.3577 0.4810 -0.0448 0.1190  0.0452  361 ALA A O   
2787 C CB  . ALA A 361 ? 0.8240 0.3796 0.4630 -0.0232 0.0732  0.0598  361 ALA A CB  
2788 N N   . GLU A 362 ? 0.7800 0.3435 0.4761 -0.0296 0.1030  0.0563  362 GLU A N   
2789 C CA  . GLU A 362 ? 0.8288 0.3749 0.5296 -0.0368 0.1250  0.0564  362 GLU A CA  
2790 C C   . GLU A 362 ? 0.8910 0.3861 0.5423 -0.0350 0.1342  0.0673  362 GLU A C   
2791 O O   . GLU A 362 ? 0.8978 0.3720 0.5208 -0.0239 0.1188  0.0754  362 GLU A O   
2792 C CB  . GLU A 362 ? 0.8080 0.3686 0.5418 -0.0332 0.1213  0.0534  362 GLU A CB  
2793 C CG  . GLU A 362 ? 0.8485 0.3945 0.5934 -0.0419 0.1427  0.0517  362 GLU A CG  
2794 C CD  . GLU A 362 ? 0.8931 0.4511 0.6674 -0.0376 0.1373  0.0480  362 GLU A CD  
2795 O OE1 . GLU A 362 ? 0.9127 0.4936 0.7016 -0.0282 0.1189  0.0461  362 GLU A OE1 
2796 O OE2 . GLU A 362 ? 0.8936 0.4375 0.6768 -0.0437 0.1519  0.0464  362 GLU A OE2 
2797 N N   . THR A 363 ? 0.8751 0.3496 0.5167 -0.0457 0.1595  0.0676  363 THR A N   
2798 C CA  . THR A 363 ? 0.9298 0.3527 0.5255 -0.0452 0.1730  0.0782  363 THR A CA  
2799 C C   . THR A 363 ? 0.9371 0.3473 0.5476 -0.0459 0.1819  0.0800  363 THR A C   
2800 O O   . THR A 363 ? 0.8966 0.3365 0.5535 -0.0505 0.1841  0.0714  363 THR A O   
2801 C CB  . THR A 363 ? 0.9561 0.3593 0.5325 -0.0563 0.1988  0.0783  363 THR A CB  
2802 O OG1 . THR A 363 ? 0.9345 0.3623 0.5574 -0.0686 0.2176  0.0690  363 THR A OG1 
2803 C CG2 . THR A 363 ? 0.9503 0.3619 0.5079 -0.0551 0.1899  0.0763  363 THR A CG2 
2804 N N   . SER A 364 ? 1.0039 0.3666 0.5715 -0.0409 0.1866  0.0913  364 SER A N   
2805 C CA  . SER A 364 ? 1.0229 0.3686 0.5996 -0.0400 0.1930  0.0941  364 SER A CA  
2806 C C   . SER A 364 ? 1.0319 0.3765 0.6356 -0.0556 0.2214  0.0885  364 SER A C   
2807 O O   . SER A 364 ? 1.0825 0.4241 0.7078 -0.0573 0.2260  0.0869  364 SER A O   
2808 C CB  . SER A 364 ? 1.0722 0.3637 0.5929 -0.0302 0.1911  0.1084  364 SER A CB  
2809 O OG  . SER A 364 ? 1.1373 0.3902 0.6125 -0.0359 0.2101  0.1152  364 SER A OG  
2810 N N   . ASP A 365 ? 1.0091 0.3558 0.6137 -0.0671 0.2405  0.0852  365 ASP A N   
2811 C CA  . ASP A 365 ? 1.0055 0.3604 0.6464 -0.0820 0.2652  0.0778  365 ASP A CA  
2812 C C   . ASP A 365 ? 0.9205 0.3291 0.6182 -0.0878 0.2590  0.0638  365 ASP A C   
2813 O O   . ASP A 365 ? 0.9490 0.3718 0.6792 -0.1002 0.2770  0.0560  365 ASP A O   
2814 C CB  . ASP A 365 ? 1.0158 0.3585 0.6378 -0.0878 0.2866  0.0777  365 ASP A CB  
2815 C CG  . ASP A 365 ? 1.0599 0.4139 0.6704 -0.0890 0.2863  0.0757  365 ASP A CG  
2816 O OD1 . ASP A 365 ? 1.0523 0.4212 0.6626 -0.0843 0.2673  0.0758  365 ASP A OD1 
2817 O OD2 . ASP A 365 ? 1.0846 0.4342 0.6881 -0.0942 0.3050  0.0730  365 ASP A OD2 
2818 N N   . GLY A 366 ? 0.9140 0.3545 0.6253 -0.0782 0.2329  0.0600  366 GLY A N   
2819 C CA  . GLY A 366 ? 0.8824 0.3717 0.6445 -0.0816 0.2246  0.0472  366 GLY A CA  
2820 C C   . GLY A 366 ? 0.8631 0.3799 0.6370 -0.0860 0.2254  0.0411  366 GLY A C   
2821 O O   . GLY A 366 ? 0.8323 0.3839 0.6490 -0.0920 0.2256  0.0304  366 GLY A O   
2822 N N   . GLY A 367 ? 0.8646 0.3656 0.6006 -0.0829 0.2250  0.0473  367 GLY A N   
2823 C CA  . GLY A 367 ? 0.8453 0.3698 0.5885 -0.0859 0.2244  0.0419  367 GLY A CA  
2824 C C   . GLY A 367 ? 0.8135 0.3567 0.5474 -0.0755 0.1983  0.0422  367 GLY A C   
2825 O O   . GLY A 367 ? 0.7783 0.3240 0.5097 -0.0660 0.1797  0.0452  367 GLY A O   
2826 N N   . VAL A 368 ? 0.8121 0.3686 0.5431 -0.0777 0.1980  0.0388  368 VAL A N   
2827 C CA  . VAL A 368 ? 0.7761 0.3529 0.5029 -0.0702 0.1751  0.0376  368 VAL A CA  
2828 C C   . VAL A 368 ? 0.8390 0.3857 0.5150 -0.0674 0.1741  0.0443  368 VAL A C   
2829 O O   . VAL A 368 ? 0.8550 0.3739 0.5061 -0.0731 0.1946  0.0470  368 VAL A O   
2830 C CB  . VAL A 368 ? 0.7494 0.3686 0.5161 -0.0746 0.1725  0.0270  368 VAL A CB  
2831 C CG1 . VAL A 368 ? 0.6934 0.3422 0.5058 -0.0755 0.1686  0.0201  368 VAL A CG1 
2832 C CG2 . VAL A 368 ? 0.7505 0.3653 0.5183 -0.0841 0.1943  0.0235  368 VAL A CG2 
2833 N N   . TYR A 369 ? 0.8099 0.3621 0.4711 -0.0586 0.1502  0.0464  369 TYR A N   
2834 C CA  . TYR A 369 ? 0.8472 0.3734 0.4609 -0.0558 0.1453  0.0510  369 TYR A CA  
2835 C C   . TYR A 369 ? 0.8036 0.3582 0.4275 -0.0516 0.1218  0.0464  369 TYR A C   
2836 O O   . TYR A 369 ? 0.7885 0.3733 0.4448 -0.0471 0.1052  0.0437  369 TYR A O   
2837 C CB  . TYR A 369 ? 0.8892 0.3722 0.4547 -0.0477 0.1390  0.0621  369 TYR A CB  
2838 C CG  . TYR A 369 ? 0.9412 0.3805 0.4503 -0.0493 0.1510  0.0676  369 TYR A CG  
2839 C CD1 . TYR A 369 ? 0.9893 0.4076 0.4902 -0.0586 0.1822  0.0680  369 TYR A CD1 
2840 C CD2 . TYR A 369 ? 0.9774 0.3949 0.4413 -0.0415 0.1318  0.0721  369 TYR A CD2 
2841 C CE1 . TYR A 369 ? 1.0260 0.4011 0.4725 -0.0599 0.1963  0.0732  369 TYR A CE1 
2842 C CE2 . TYR A 369 ? 1.0526 0.4251 0.4585 -0.0425 0.1435  0.0770  369 TYR A CE2 
2843 C CZ  . TYR A 369 ? 1.0812 0.4321 0.4778 -0.0516 0.1770  0.0777  369 TYR A CZ  
2844 O OH  . TYR A 369 ? 1.1842 0.4885 0.5219 -0.0526 0.1918  0.0826  369 TYR A OH  
2845 N N   . TRP A 370 ? 0.8223 0.3655 0.4179 -0.0534 0.1216  0.0455  370 TRP A N   
2846 C CA  . TRP A 370 ? 0.8437 0.4082 0.4437 -0.0498 0.0986  0.0417  370 TRP A CA  
2847 C C   . TRP A 370 ? 0.9065 0.4395 0.4559 -0.0502 0.0981  0.0434  370 TRP A C   
2848 O O   . TRP A 370 ? 0.9192 0.4205 0.4372 -0.0544 0.1197  0.0459  370 TRP A O   
2849 C CB  . TRP A 370 ? 0.7478 0.3574 0.3979 -0.0552 0.0995  0.0319  370 TRP A CB  
2850 C CG  . TRP A 370 ? 0.7444 0.3558 0.4041 -0.0644 0.1242  0.0269  370 TRP A CG  
2851 C CD1 . TRP A 370 ? 0.7629 0.3580 0.3969 -0.0686 0.1348  0.0251  370 TRP A CD1 
2852 C CD2 . TRP A 370 ? 0.7083 0.3388 0.4075 -0.0702 0.1409  0.0225  370 TRP A CD2 
2853 N NE1 . TRP A 370 ? 0.7437 0.3480 0.4014 -0.0762 0.1579  0.0202  370 TRP A NE1 
2854 C CE2 . TRP A 370 ? 0.7116 0.3381 0.4100 -0.0775 0.1610  0.0184  370 TRP A CE2 
2855 C CE3 . TRP A 370 ? 0.7146 0.3645 0.4498 -0.0696 0.1402  0.0211  370 TRP A CE3 
2856 C CZ2 . TRP A 370 ? 0.6865 0.3300 0.4220 -0.0840 0.1787  0.0129  370 TRP A CZ2 
2857 C CZ3 . TRP A 370 ? 0.6623 0.3268 0.4305 -0.0766 0.1572  0.0154  370 TRP A CZ3 
2858 C CH2 . TRP A 370 ? 0.7020 0.3645 0.4719 -0.0837 0.1755  0.0113  370 TRP A CH2 
2859 N N   . GLU A 371 ? 0.8968 0.4382 0.4387 -0.0457 0.0736  0.0418  371 GLU A N   
2860 C CA  . GLU A 371 ? 0.9586 0.4724 0.4534 -0.0459 0.0691  0.0417  371 GLU A CA  
2861 C C   . GLU A 371 ? 0.9424 0.4570 0.4385 -0.0551 0.0926  0.0355  371 GLU A C   
2862 O O   . GLU A 371 ? 0.8623 0.4134 0.4045 -0.0603 0.0987  0.0284  371 GLU A O   
2863 C CB  . GLU A 371 ? 0.9466 0.4794 0.4480 -0.0414 0.0381  0.0383  371 GLU A CB  
2864 C CG  . GLU A 371 ? 1.0068 0.5258 0.4892 -0.0306 0.0120  0.0451  371 GLU A CG  
2865 C CD  . GLU A 371 ? 1.0044 0.5378 0.5184 -0.0254 0.0115  0.0495  371 GLU A CD  
2866 O OE1 . GLU A 371 ? 0.9275 0.4974 0.4923 -0.0293 0.0199  0.0448  371 GLU A OE1 
2867 O OE2 . GLU A 371 ? 0.9949 0.5007 0.4806 -0.0170 0.0022  0.0577  371 GLU A OE2 
2868 N N   . GLY A 372 ? 1.0085 0.4808 0.4526 -0.0565 0.1065  0.0383  372 GLY A N   
2869 C CA  . GLY A 372 ? 0.9451 0.4134 0.3863 -0.0642 0.1301  0.0328  372 GLY A CA  
2870 C C   . GLY A 372 ? 0.9891 0.4622 0.4569 -0.0707 0.1611  0.0324  372 GLY A C   
2871 O O   . GLY A 372 ? 0.9310 0.4046 0.4037 -0.0768 0.1821  0.0273  372 GLY A O   
2872 N N   . ILE A 373 ? 0.9123 0.3886 0.3987 -0.0695 0.1646  0.0372  373 ILE A N   
2873 C CA  . ILE A 373 ? 0.9021 0.3807 0.4141 -0.0764 0.1936  0.0365  373 ILE A CA  
2874 C C   . ILE A 373 ? 0.9571 0.3912 0.4241 -0.0801 0.2210  0.0401  373 ILE A C   
2875 O O   . ILE A 373 ? 0.9896 0.4275 0.4787 -0.0875 0.2484  0.0369  373 ILE A O   
2876 C CB  . ILE A 373 ? 0.9266 0.4102 0.4598 -0.0743 0.1908  0.0413  373 ILE A CB  
2877 C CG1 . ILE A 373 ? 0.9213 0.4201 0.4970 -0.0826 0.2159  0.0375  373 ILE A CG1 
2878 C CG2 . ILE A 373 ? 0.9844 0.4196 0.4635 -0.0689 0.1913  0.0522  373 ILE A CG2 
2879 C CD1 . ILE A 373 ? 0.9184 0.4324 0.5263 -0.0811 0.2097  0.0390  373 ILE A CD1 
2880 N N   . ASP A 374 ? 1.0360 0.4264 0.4396 -0.0747 0.2145  0.0469  374 ASP A N   
2881 C CA  . ASP A 374 ? 1.1186 0.4626 0.4695 -0.0772 0.2392  0.0499  374 ASP A CA  
2882 C C   . ASP A 374 ? 1.1945 0.5174 0.5467 -0.0813 0.2690  0.0543  374 ASP A C   
2883 O O   . ASP A 374 ? 1.2657 0.5753 0.6119 -0.0830 0.2908  0.0494  374 ASP A O   
2884 C CB  . ASP A 374 ? 1.1624 0.5207 0.5253 -0.0825 0.2513  0.0405  374 ASP A CB  
2885 C CG  . ASP A 374 ? 1.3453 0.6588 0.6477 -0.0808 0.2621  0.0409  374 ASP A CG  
2886 O OD1 . ASP A 374 ? 1.4672 0.7415 0.7220 -0.0747 0.2580  0.0470  374 ASP A OD1 
2887 O OD2 . ASP A 374 ? 1.4663 0.7888 0.7771 -0.0837 0.2713  0.0326  374 ASP A OD2 
2888 N N   . GLU A 375 ? 1.1133 0.4404 0.4840 -0.0807 0.2658  0.0600  375 GLU A N   
2889 C CA  . GLU A 375 ? 1.1684 0.4882 0.5564 -0.0832 0.2879  0.0600  375 GLU A CA  
2890 C C   . GLU A 375 ? 1.1844 0.4686 0.5314 -0.0755 0.2775  0.0706  375 GLU A C   
2891 O O   . GLU A 375 ? 1.1589 0.4476 0.5065 -0.0712 0.2554  0.0770  375 GLU A O   
2892 C CB  . GLU A 375 ? 1.1745 0.5360 0.6322 -0.0906 0.2959  0.0551  375 GLU A CB  
2893 C CG  . GLU A 375 ? 1.1779 0.5724 0.6830 -0.0979 0.3127  0.0437  375 GLU A CG  
2894 C CD  . GLU A 375 ? 1.1833 0.6120 0.7527 -0.1042 0.3208  0.0387  375 GLU A CD  
2895 O OE1 . GLU A 375 ? 1.1373 0.5533 0.7110 -0.1050 0.3322  0.0407  375 GLU A OE1 
2896 O OE2 . GLU A 375 ? 1.1184 0.5854 0.7327 -0.1081 0.3149  0.0324  375 GLU A OE2 
2897 N N   . PRO A 376 ? 1.1975 0.4451 0.5089 -0.0729 0.2922  0.0727  376 PRO A N   
2898 C CA  . PRO A 376 ? 1.2486 0.4625 0.5239 -0.0653 0.2836  0.0826  376 PRO A CA  
2899 C C   . PRO A 376 ? 1.2694 0.4990 0.5877 -0.0689 0.2916  0.0842  376 PRO A C   
2900 O O   . PRO A 376 ? 1.2494 0.5050 0.6176 -0.0778 0.3120  0.0770  376 PRO A O   
2901 C CB  . PRO A 376 ? 1.3068 0.4782 0.5357 -0.0631 0.3020  0.0826  376 PRO A CB  
2902 C CG  . PRO A 376 ? 1.3313 0.5210 0.5920 -0.0717 0.3278  0.0723  376 PRO A CG  
2903 C CD  . PRO A 376 ? 1.2294 0.4600 0.5246 -0.0752 0.3150  0.0666  376 PRO A CD  
2904 N N   . LEU A 377 ? 1.3301 0.5428 0.6286 -0.0612 0.2738  0.0934  377 LEU A N   
2905 C CA  . LEU A 377 ? 1.2617 0.4808 0.5919 -0.0631 0.2799  0.0958  377 LEU A CA  
2906 C C   . LEU A 377 ? 1.3295 0.5090 0.6265 -0.0607 0.2964  0.1003  377 LEU A C   
2907 O O   . LEU A 377 ? 1.3350 0.4765 0.5752 -0.0540 0.2945  0.1044  377 LEU A O   
2908 C CB  . LEU A 377 ? 1.2056 0.4299 0.5384 -0.0554 0.2515  0.1029  377 LEU A CB  
2909 C CG  . LEU A 377 ? 1.1758 0.4405 0.5478 -0.0591 0.2383  0.0980  377 LEU A CG  
2910 C CD1 . LEU A 377 ? 1.1128 0.4002 0.5044 -0.0485 0.2060  0.0987  377 LEU A CD1 
2911 C CD2 . LEU A 377 ? 1.1359 0.4385 0.5711 -0.0716 0.2593  0.0876  377 LEU A CD2 
2912 N N   . ALA A 378 ? 1.3233 0.5113 0.6565 -0.0665 0.3125  0.0988  378 ALA A N   
2913 C CA  . ALA A 378 ? 1.3323 0.4847 0.6398 -0.0654 0.3298  0.1029  378 ALA A CA  
2914 C C   . ALA A 378 ? 1.3911 0.5112 0.6561 -0.0534 0.3090  0.1145  378 ALA A C   
2915 O O   . ALA A 378 ? 1.3319 0.4653 0.6051 -0.0475 0.2837  0.1182  378 ALA A O   
2916 C CB  . ALA A 378 ? 1.3722 0.5461 0.7351 -0.0757 0.3513  0.0972  378 ALA A CB  
2917 N N   . PRO A 379 ? 1.4800 0.5565 0.6995 -0.0490 0.3193  0.1201  379 PRO A N   
2918 C CA  . PRO A 379 ? 1.4640 0.5090 0.6447 -0.0368 0.2999  0.1310  379 PRO A CA  
2919 C C   . PRO A 379 ? 1.4269 0.4922 0.6493 -0.0367 0.2911  0.1333  379 PRO A C   
2920 O O   . PRO A 379 ? 1.3932 0.4820 0.6655 -0.0472 0.3090  0.1275  379 PRO A O   
2921 C CB  . PRO A 379 ? 1.5346 0.5343 0.6735 -0.0361 0.3221  0.1344  379 PRO A CB  
2922 C CG  . PRO A 379 ? 1.5450 0.5427 0.6757 -0.0426 0.3422  0.1269  379 PRO A CG  
2923 C CD  . PRO A 379 ? 1.4698 0.5204 0.6649 -0.0531 0.3470  0.1170  379 PRO A CD  
2924 N N   . GLY A 380 ? 1.4343 0.4905 0.6371 -0.0242 0.2620  0.1411  380 GLY A N   
2925 C CA  . GLY A 380 ? 1.4052 0.4758 0.6421 -0.0216 0.2513  0.1437  380 GLY A CA  
2926 C C   . GLY A 380 ? 1.3338 0.4497 0.6224 -0.0250 0.2385  0.1379  380 GLY A C   
2927 O O   . GLY A 380 ? 1.3124 0.4377 0.6232 -0.0194 0.2235  0.1405  380 GLY A O   
2928 N N   . VAL A 381 ? 1.2986 0.4415 0.6067 -0.0334 0.2443  0.1301  381 VAL A N   
2929 C CA  . VAL A 381 ? 1.2327 0.4175 0.5885 -0.0370 0.2331  0.1243  381 VAL A CA  
2930 C C   . VAL A 381 ? 1.2480 0.4297 0.5796 -0.0240 0.2001  0.1304  381 VAL A C   
2931 O O   . VAL A 381 ? 1.3117 0.4746 0.5983 -0.0181 0.1895  0.1337  381 VAL A O   
2932 C CB  . VAL A 381 ? 1.2288 0.4430 0.6135 -0.0499 0.2504  0.1138  381 VAL A CB  
2933 C CG1 . VAL A 381 ? 1.1347 0.3888 0.5616 -0.0527 0.2367  0.1083  381 VAL A CG1 
2934 C CG2 . VAL A 381 ? 1.2282 0.4508 0.6466 -0.0619 0.2801  0.1068  381 VAL A CG2 
2935 N N   . THR A 382 ? 1.2027 0.4123 0.5722 -0.0186 0.1813  0.1284  382 THR A N   
2936 C CA  . THR A 382 ? 1.2001 0.4309 0.5711 -0.0048 0.1456  0.1281  382 THR A CA  
2937 C C   . THR A 382 ? 1.1098 0.4039 0.5409 -0.0092 0.1353  0.1147  382 THR A C   
2938 O O   . THR A 382 ? 1.0978 0.4189 0.5714 -0.0209 0.1529  0.1061  382 THR A O   
2939 C CB  . THR A 382 ? 1.1944 0.4120 0.5641 0.0085  0.1294  0.1351  382 THR A CB  
2940 O OG1 . THR A 382 ? 1.1768 0.4162 0.5962 0.0025  0.1415  0.1294  382 THR A OG1 
2941 C CG2 . THR A 382 ? 1.2972 0.4480 0.6009 0.0146  0.1369  0.1496  382 THR A CG2 
2942 N N   . ILE A 383 ? 1.0898 0.4064 0.5241 0.0004  0.1062  0.1129  383 ILE A N   
2943 C CA  . ILE A 383 ? 1.0777 0.4496 0.5608 -0.0033 0.0960  0.1012  383 ILE A CA  
2944 C C   . ILE A 383 ? 1.0953 0.4976 0.6112 0.0082  0.0696  0.0995  383 ILE A C   
2945 O O   . ILE A 383 ? 1.1636 0.5480 0.6546 0.0212  0.0484  0.1067  383 ILE A O   
2946 C CB  . ILE A 383 ? 1.0988 0.4721 0.5577 -0.0054 0.0889  0.0989  383 ILE A CB  
2947 C CG1 . ILE A 383 ? 1.0912 0.4353 0.5198 -0.0167 0.1180  0.0998  383 ILE A CG1 
2948 C CG2 . ILE A 383 ? 1.0433 0.4720 0.5520 -0.0087 0.0774  0.0875  383 ILE A CG2 
2949 C CD1 . ILE A 383 ? 1.1505 0.4919 0.5521 -0.0190 0.1138  0.0970  383 ILE A CD1 
2950 N N   . THR A 384 ? 0.9771 0.4247 0.5489 0.0038  0.0709  0.0898  384 THR A N   
2951 C CA  . THR A 384 ? 0.9694 0.4523 0.5783 0.0132  0.0488  0.0863  384 THR A CA  
2952 C C   . THR A 384 ? 0.9776 0.5027 0.6144 0.0087  0.0399  0.0772  384 THR A C   
2953 O O   . THR A 384 ? 0.9107 0.4557 0.5692 -0.0027 0.0555  0.0696  384 THR A O   
2954 C CB  . THR A 384 ? 0.9817 0.4801 0.6297 0.0127  0.0576  0.0823  384 THR A CB  
2955 O OG1 . THR A 384 ? 1.0093 0.4661 0.6316 0.0152  0.0683  0.0904  384 THR A OG1 
2956 C CG2 . THR A 384 ? 0.9686 0.4993 0.6509 0.0239  0.0362  0.0795  384 THR A CG2 
2957 N N   . SER A 385 ? 0.9643 0.5023 0.6015 0.0178  0.0147  0.0779  385 SER A N   
2958 C CA  . SER A 385 ? 0.9755 0.5489 0.6347 0.0139  0.0048  0.0703  385 SER A CA  
2959 C C   . SER A 385 ? 0.8853 0.5040 0.6006 0.0106  0.0086  0.0613  385 SER A C   
2960 O O   . SER A 385 ? 0.8730 0.4966 0.6100 0.0130  0.0152  0.0607  385 SER A O   
2961 C CB  . SER A 385 ? 0.9981 0.5734 0.6472 0.0247  -0.0243 0.0732  385 SER A CB  
2962 O OG  . SER A 385 ? 1.0442 0.6356 0.7223 0.0360  -0.0385 0.0745  385 SER A OG  
2963 N N   . TRP A 386 ? 0.8530 0.5027 0.5894 0.0053  0.0043  0.0542  386 TRP A N   
2964 C CA  . TRP A 386 ? 0.8053 0.4959 0.5906 0.0031  0.0064  0.0462  386 TRP A CA  
2965 C C   . TRP A 386 ? 0.8434 0.5523 0.6552 0.0148  -0.0102 0.0470  386 TRP A C   
2966 O O   . TRP A 386 ? 0.8288 0.5659 0.6781 0.0148  -0.0063 0.0414  386 TRP A O   
2967 C CB  . TRP A 386 ? 0.7744 0.4906 0.5730 -0.0047 0.0053  0.0393  386 TRP A CB  
2968 C CG  . TRP A 386 ? 0.7943 0.5202 0.5918 0.0006  -0.0171 0.0400  386 TRP A CG  
2969 C CD1 . TRP A 386 ? 0.8247 0.5254 0.5844 0.0036  -0.0301 0.0448  386 TRP A CD1 
2970 C CD2 . TRP A 386 ? 0.7981 0.5607 0.6342 0.0035  -0.0298 0.0353  386 TRP A CD2 
2971 N NE1 . TRP A 386 ? 0.8139 0.5349 0.5889 0.0078  -0.0518 0.0429  386 TRP A NE1 
2972 C CE2 . TRP A 386 ? 0.8287 0.5885 0.6523 0.0074  -0.0510 0.0372  386 TRP A CE2 
2973 C CE3 . TRP A 386 ? 0.7577 0.5536 0.6368 0.0030  -0.0249 0.0297  386 TRP A CE3 
2974 C CZ2 . TRP A 386 ? 0.7871 0.5786 0.6445 0.0100  -0.0666 0.0334  386 TRP A CZ2 
2975 C CZ3 . TRP A 386 ? 0.7275 0.5529 0.6367 0.0059  -0.0385 0.0266  386 TRP A CZ3 
2976 C CH2 . TRP A 386 ? 0.7474 0.5715 0.6480 0.0090  -0.0588 0.0284  386 TRP A CH2 
2977 N N   . LYS A 387 ? 0.8777 0.5706 0.6709 0.0252  -0.0286 0.0537  387 LYS A N   
2978 C CA  . LYS A 387 ? 0.8902 0.5979 0.7092 0.0378  -0.0441 0.0551  387 LYS A CA  
2979 C C   . LYS A 387 ? 0.9605 0.6469 0.7748 0.0449  -0.0369 0.0599  387 LYS A C   
2980 O O   . LYS A 387 ? 1.0032 0.6949 0.8335 0.0572  -0.0495 0.0624  387 LYS A O   
2981 C CB  . LYS A 387 ? 0.9662 0.6679 0.7709 0.0467  -0.0700 0.0596  387 LYS A CB  
2982 C CG  . LYS A 387 ? 0.9408 0.6705 0.7619 0.0417  -0.0818 0.0538  387 LYS A CG  
2983 C CD  . LYS A 387 ? 1.0639 0.7875 0.8739 0.0514  -0.1102 0.0576  387 LYS A CD  
2984 C CE  . LYS A 387 ? 1.0952 0.8456 0.9231 0.0456  -0.1230 0.0512  387 LYS A CE  
2985 N NZ  . LYS A 387 ? 1.1981 0.9334 0.9933 0.0334  -0.1132 0.0489  387 LYS A NZ  
2986 N N   . ASN A 388 ? 0.9537 0.6160 0.7483 0.0374  -0.0167 0.0610  388 ASN A N   
2987 C CA  . ASN A 388 ? 1.0142 0.6519 0.8017 0.0422  -0.0077 0.0653  388 ASN A CA  
2988 C C   . ASN A 388 ? 1.1013 0.7051 0.8553 0.0549  -0.0226 0.0759  388 ASN A C   
2989 O O   . ASN A 388 ? 1.1162 0.7145 0.8792 0.0665  -0.0292 0.0793  388 ASN A O   
2990 C CB  . ASN A 388 ? 0.9679 0.6325 0.7983 0.0465  -0.0053 0.0594  388 ASN A CB  
2991 C CG  . ASN A 388 ? 1.0069 0.6519 0.8354 0.0435  0.0128  0.0590  388 ASN A CG  
2992 O OD1 . ASN A 388 ? 0.9952 0.6214 0.8056 0.0327  0.0289  0.0589  388 ASN A OD1 
2993 N ND2 . ASN A 388 ? 1.1033 0.7521 0.9519 0.0530  0.0106  0.0584  388 ASN A ND2 
2994 N N   . LYS A 389 ? 1.1393 0.7186 0.8525 0.0533  -0.0283 0.0810  389 LYS A N   
2995 C CA  . LYS A 389 ? 1.2068 0.7502 0.8807 0.0653  -0.0445 0.0914  389 LYS A CA  
2996 C C   . LYS A 389 ? 1.2196 0.7170 0.8382 0.0587  -0.0310 0.0978  389 LYS A C   
2997 O O   . LYS A 389 ? 1.1765 0.6766 0.7882 0.0456  -0.0160 0.0934  389 LYS A O   
2998 C CB  . LYS A 389 ? 1.2378 0.7984 0.9158 0.0733  -0.0732 0.0911  389 LYS A CB  
2999 C CG  . LYS A 389 ? 1.2682 0.8710 1.0002 0.0820  -0.0878 0.0863  389 LYS A CG  
3000 C CD  . LYS A 389 ? 1.3195 0.9404 1.0590 0.0880  -0.1157 0.0853  389 LYS A CD  
3001 C CE  . LYS A 389 ? 1.3730 1.0378 1.1711 0.0958  -0.1272 0.0801  389 LYS A CE  
3002 N NZ  . LYS A 389 ? 1.4261 1.1138 1.2398 0.0990  -0.1528 0.0774  389 LYS A NZ  
3003 N N   . GLU A 390 ? 1.2805 0.7343 0.8594 0.0683  -0.0354 0.1083  390 GLU A N   
3004 C CA  . GLU A 390 ? 1.3444 0.7489 0.8632 0.0643  -0.0249 0.1160  390 GLU A CA  
3005 C C   . GLU A 390 ? 1.3089 0.7129 0.8018 0.0631  -0.0398 0.1150  390 GLU A C   
3006 O O   . GLU A 390 ? 1.3365 0.7547 0.8356 0.0732  -0.0681 0.1149  390 GLU A O   
3007 C CB  . GLU A 390 ? 1.4424 0.7992 0.9216 0.0774  -0.0309 0.1284  390 GLU A CB  
3008 C CG  . GLU A 390 ? 1.5416 0.8734 1.0179 0.0726  -0.0046 0.1316  390 GLU A CG  
3009 C CD  . GLU A 390 ? 1.6103 0.9014 1.0414 0.0606  0.0213  0.1359  390 GLU A CD  
3010 O OE1 . GLU A 390 ? 1.5258 0.8150 0.9344 0.0544  0.0218  0.1342  390 GLU A OE1 
3011 O OE2 . GLU A 390 ? 1.6404 0.9002 1.0587 0.0574  0.0421  0.1409  390 GLU A OE2 
3012 N N   . TRP A 391 ? 1.3146 0.7025 0.7802 0.0507  -0.0207 0.1137  391 TRP A N   
3013 C CA  . TRP A 391 ? 1.3844 0.7751 0.8294 0.0471  -0.0310 0.1104  391 TRP A CA  
3014 C C   . TRP A 391 ? 1.4659 0.8018 0.8427 0.0439  -0.0180 0.1176  391 TRP A C   
3015 O O   . TRP A 391 ? 1.3864 0.7036 0.7525 0.0339  0.0121  0.1187  391 TRP A O   
3016 C CB  . TRP A 391 ? 1.2939 0.7298 0.7828 0.0338  -0.0197 0.0985  391 TRP A CB  
3017 C CG  . TRP A 391 ? 1.2894 0.7289 0.7600 0.0296  -0.0293 0.0942  391 TRP A CG  
3018 C CD1 . TRP A 391 ? 1.3052 0.7736 0.7952 0.0336  -0.0555 0.0893  391 TRP A CD1 
3019 C CD2 . TRP A 391 ? 1.3321 0.7446 0.7620 0.0202  -0.0120 0.0940  391 TRP A CD2 
3020 N NE1 . TRP A 391 ? 1.3133 0.7733 0.7759 0.0271  -0.0567 0.0858  391 TRP A NE1 
3021 C CE2 . TRP A 391 ? 1.3289 0.7543 0.7533 0.0193  -0.0299 0.0886  391 TRP A CE2 
3022 C CE3 . TRP A 391 ? 1.3506 0.7290 0.7498 0.0123  0.0180  0.0976  391 TRP A CE3 
3023 C CZ2 . TRP A 391 ? 1.3605 0.7644 0.7472 0.0116  -0.0190 0.0865  391 TRP A CZ2 
3024 C CZ3 . TRP A 391 ? 1.4096 0.7680 0.7732 0.0047  0.0299  0.0958  391 TRP A CZ3 
3025 C CH2 . TRP A 391 ? 1.4283 0.7989 0.7847 0.0048  0.0114  0.0902  391 TRP A CH2 
3026 N N   . ARG A 392 ? 1.5317 0.8420 0.8631 0.0522  -0.0405 0.1220  392 ARG A N   
3027 C CA  . ARG A 392 ? 1.6590 0.9150 0.9195 0.0501  -0.0299 0.1285  392 ARG A CA  
3028 C C   . ARG A 392 ? 1.7105 0.9763 0.9593 0.0429  -0.0344 0.1208  392 ARG A C   
3029 O O   . ARG A 392 ? 1.6840 0.9865 0.9629 0.0452  -0.0592 0.1138  392 ARG A O   
3030 C CB  . ARG A 392 ? 1.7510 0.9585 0.9547 0.0660  -0.0517 0.1402  392 ARG A CB  
3031 C CG  . ARG A 392 ? 1.7770 0.9673 0.9850 0.0747  -0.0479 0.1490  392 ARG A CG  
3032 C CD  . ARG A 392 ? 1.8627 0.9972 1.0052 0.0903  -0.0672 0.1616  392 ARG A CD  
3033 N NE  . ARG A 392 ? 1.9650 1.0788 1.1083 0.0993  -0.0630 0.1706  392 ARG A NE  
3034 C CZ  . ARG A 392 ? 2.0389 1.1077 1.1340 0.1131  -0.0762 0.1811  392 ARG A CZ  
3035 N NH1 . ARG A 392 ? 2.0627 1.1095 1.1112 0.1188  -0.0944 0.1810  392 ARG A NH1 
3036 N NH2 . ARG A 392 ? 2.0467 1.1052 1.1532 0.1197  -0.0700 0.1867  392 ARG A NH2 
3037 N N   . PRO A 393 ? 1.7870 1.0195 0.9924 0.0339  -0.0100 0.1218  393 PRO A N   
3038 C CA  . PRO A 393 ? 1.8153 1.0556 1.0094 0.0266  -0.0115 0.1138  393 PRO A CA  
3039 C C   . PRO A 393 ? 1.9440 1.1640 1.0943 0.0362  -0.0452 0.1149  393 PRO A C   
3040 O O   . PRO A 393 ? 2.0222 1.2336 1.1459 0.0309  -0.0455 0.1097  393 PRO A O   
3041 C CB  . PRO A 393 ? 1.8327 1.0345 0.9867 0.0165  0.0258  0.1163  393 PRO A CB  
3042 C CG  . PRO A 393 ? 1.8143 1.0119 0.9892 0.0138  0.0502  0.1214  393 PRO A CG  
3043 C CD  . PRO A 393 ? 1.7802 0.9737 0.9575 0.0279  0.0249  0.1286  393 PRO A CD  
3044 N N   . GLN A 394 ? 2.0398 1.2518 1.1828 0.0505  -0.0744 0.1211  394 GLN A N   
3045 C CA  . GLN A 394 ? 2.1827 1.3767 1.2875 0.0607  -0.1107 0.1218  394 GLN A CA  
3046 C C   . GLN A 394 ? 2.1601 1.3984 1.3192 0.0703  -0.1457 0.1187  394 GLN A C   
3047 O O   . GLN A 394 ? 2.2438 1.4634 1.3781 0.0842  -0.1776 0.1237  394 GLN A O   
3048 C CB  . GLN A 394 ? 2.3345 1.4576 1.3556 0.0710  -0.1137 0.1344  394 GLN A CB  
3049 C CG  . GLN A 394 ? 2.4158 1.4964 1.3813 0.0615  -0.0820 0.1345  394 GLN A CG  
3050 C CD  . GLN A 394 ? 2.5737 1.6053 1.4817 0.0700  -0.0844 0.1378  394 GLN A CD  
3051 O OE1 . GLN A 394 ? 2.6651 1.6824 1.5669 0.0814  -0.0959 0.1451  394 GLN A OE1 
3052 N NE2 . GLN A 394 ? 2.6176 1.6219 1.4826 0.0650  -0.0732 0.1323  394 GLN A NE2 
3053 N N   . ASP A 395 ? 2.1167 1.4138 1.3508 0.0635  -0.1400 0.1103  395 ASP A N   
3054 C CA  . ASP A 395 ? 2.1355 1.4808 1.4275 0.0699  -0.1694 0.1049  395 ASP A CA  
3055 C C   . ASP A 395 ? 2.2063 1.5834 1.5197 0.0610  -0.1802 0.0934  395 ASP A C   
3056 O O   . ASP A 395 ? 2.2340 1.5864 1.5044 0.0537  -0.1728 0.0908  395 ASP A O   
3057 C CB  . ASP A 395 ? 1.9646 1.3501 1.3222 0.0690  -0.1550 0.1037  395 ASP A CB  
3058 C CG  . ASP A 395 ? 1.9083 1.2603 1.2446 0.0765  -0.1424 0.1145  395 ASP A CG  
3059 O OD1 . ASP A 395 ? 1.9957 1.2944 1.2680 0.0842  -0.1480 0.1239  395 ASP A OD1 
3060 O OD2 . ASP A 395 ? 1.7630 1.1398 1.1445 0.0747  -0.1267 0.1136  395 ASP A OD2 
3061 N N   . GLU A 396 ? 2.3495 1.7802 1.7289 0.0615  -0.1964 0.0863  396 GLU A N   
3062 C CA  . GLU A 396 ? 2.3562 1.8218 1.7655 0.0513  -0.2021 0.0750  396 GLU A CA  
3063 C C   . GLU A 396 ? 2.2888 1.8016 1.7601 0.0405  -0.1780 0.0682  396 GLU A C   
3064 O O   . GLU A 396 ? 2.2743 1.8026 1.7549 0.0290  -0.1684 0.0603  396 GLU A O   
3065 C CB  . GLU A 396 ? 2.3938 1.8833 1.8294 0.0591  -0.2417 0.0710  396 GLU A CB  
3066 C CG  . GLU A 396 ? 2.3841 1.8955 1.8333 0.0489  -0.2519 0.0601  396 GLU A CG  
3067 C CD  . GLU A 396 ? 2.3029 1.8448 1.7909 0.0551  -0.2894 0.0552  396 GLU A CD  
3068 O OE1 . GLU A 396 ? 2.2973 1.8554 1.8176 0.0665  -0.3036 0.0592  396 GLU A OE1 
3069 O OE2 . GLU A 396 ? 2.2975 1.8474 1.7856 0.0485  -0.3045 0.0469  396 GLU A OE2 
3070 N N   . GLU A 397 ? 1.9016 1.4351 1.4126 0.0445  -0.1686 0.0709  397 GLU A N   
3071 C CA  . GLU A 397 ? 1.6138 1.1869 1.1775 0.0350  -0.1453 0.0649  397 GLU A CA  
3072 C C   . GLU A 397 ? 1.4417 0.9934 0.9785 0.0241  -0.1124 0.0650  397 GLU A C   
3073 O O   . GLU A 397 ? 1.4657 0.9768 0.9599 0.0267  -0.1002 0.0727  397 GLU A O   
3074 C CB  . GLU A 397 ? 1.5853 1.1790 1.1907 0.0426  -0.1428 0.0678  397 GLU A CB  
3075 C CG  . GLU A 397 ? 1.6701 1.2941 1.3166 0.0530  -0.1711 0.0665  397 GLU A CG  
3076 C CD  . GLU A 397 ? 1.6559 1.3318 1.3615 0.0457  -0.1718 0.0567  397 GLU A CD  
3077 O OE1 . GLU A 397 ? 1.5888 1.2762 1.3013 0.0332  -0.1517 0.0511  397 GLU A OE1 
3078 O OE2 . GLU A 397 ? 1.6978 1.4025 1.4438 0.0529  -0.1919 0.0547  397 GLU A OE2 
3079 N N   . PRO A 398 ? 1.3118 0.8887 0.8729 0.0123  -0.0972 0.0569  398 PRO A N   
3080 C CA  . PRO A 398 ? 1.1676 0.7320 0.7172 0.0027  -0.0648 0.0565  398 PRO A CA  
3081 C C   . PRO A 398 ? 1.0920 0.6660 0.6702 0.0039  -0.0482 0.0592  398 PRO A C   
3082 O O   . PRO A 398 ? 1.0435 0.6430 0.6596 0.0104  -0.0591 0.0592  398 PRO A O   
3083 C CB  . PRO A 398 ? 1.0750 0.6721 0.6548 -0.0080 -0.0581 0.0466  398 PRO A CB  
3084 C CG  . PRO A 398 ? 1.1080 0.7457 0.7352 -0.0041 -0.0802 0.0425  398 PRO A CG  
3085 C CD  . PRO A 398 ? 1.2377 0.8572 0.8425 0.0074  -0.1081 0.0479  398 PRO A CD  
3086 N N   . CYS A 399 ? 1.0284 0.5809 0.5888 -0.0025 -0.0211 0.0611  399 CYS A N   
3087 C CA  . CYS A 399 ? 1.0182 0.5764 0.6037 -0.0024 -0.0051 0.0630  399 CYS A CA  
3088 C C   . CYS A 399 ? 0.9098 0.5120 0.5502 -0.0099 0.0061  0.0542  399 CYS A C   
3089 O O   . CYS A 399 ? 0.8743 0.4917 0.5458 -0.0078 0.0107  0.0538  399 CYS A O   
3090 C CB  . CYS A 399 ? 1.0240 0.5398 0.5706 -0.0064 0.0192  0.0690  399 CYS A CB  
3091 S SG  . CYS A 399 ? 1.0168 0.5277 0.5551 -0.0212 0.0489  0.0633  399 CYS A SG  
3092 N N   . ALA A 400 ? 0.8698 0.4908 0.5207 -0.0180 0.0097  0.0471  400 ALA A N   
3093 C CA  . ALA A 400 ? 0.8240 0.4850 0.5233 -0.0243 0.0181  0.0389  400 ALA A CA  
3094 C C   . ALA A 400 ? 0.8240 0.5152 0.5454 -0.0239 -0.0001 0.0336  400 ALA A C   
3095 O O   . ALA A 400 ? 0.7858 0.4657 0.4819 -0.0241 -0.0117 0.0335  400 ALA A O   
3096 C CB  . ALA A 400 ? 0.7816 0.4387 0.4786 -0.0351 0.0427  0.0348  400 ALA A CB  
3097 N N   . HIS A 401 ? 0.7463 0.4741 0.5137 -0.0237 -0.0019 0.0289  401 HIS A N   
3098 C CA  . HIS A 401 ? 0.6924 0.4490 0.4839 -0.0242 -0.0165 0.0239  401 HIS A CA  
3099 C C   . HIS A 401 ? 0.6919 0.4486 0.4730 -0.0335 -0.0091 0.0188  401 HIS A C   
3100 O O   . HIS A 401 ? 0.6961 0.4469 0.4732 -0.0399 0.0108  0.0168  401 HIS A O   
3101 C CB  . HIS A 401 ? 0.6747 0.4675 0.5145 -0.0230 -0.0149 0.0199  401 HIS A CB  
3102 C CG  . HIS A 401 ? 0.6646 0.4859 0.5314 -0.0226 -0.0297 0.0160  401 HIS A CG  
3103 N ND1 . HIS A 401 ? 0.6180 0.4556 0.4960 -0.0306 -0.0256 0.0101  401 HIS A ND1 
3104 C CD2 . HIS A 401 ? 0.6676 0.5032 0.5533 -0.0154 -0.0481 0.0171  401 HIS A CD2 
3105 C CE1 . HIS A 401 ? 0.6180 0.4782 0.5205 -0.0292 -0.0400 0.0079  401 HIS A CE1 
3106 N NE2 . HIS A 401 ? 0.5854 0.4462 0.4948 -0.0201 -0.0539 0.0118  401 HIS A NE2 
3107 N N   . PRO A 402 ? 0.6790 0.4409 0.4558 -0.0344 -0.0249 0.0164  402 PRO A N   
3108 C CA  . PRO A 402 ? 0.6864 0.4455 0.4511 -0.0428 -0.0179 0.0113  402 PRO A CA  
3109 C C   . PRO A 402 ? 0.6496 0.4349 0.4474 -0.0493 -0.0021 0.0054  402 PRO A C   
3110 O O   . PRO A 402 ? 0.6562 0.4343 0.4423 -0.0557 0.0102  0.0021  402 PRO A O   
3111 C CB  . PRO A 402 ? 0.6818 0.4474 0.4458 -0.0420 -0.0412 0.0090  402 PRO A CB  
3112 C CG  . PRO A 402 ? 0.6950 0.4481 0.4469 -0.0323 -0.0597 0.0151  402 PRO A CG  
3113 C CD  . PRO A 402 ? 0.6824 0.4460 0.4584 -0.0274 -0.0506 0.0185  402 PRO A CD  
3114 N N   . ASN A 403 ? 0.6265 0.4403 0.4637 -0.0471 -0.0020 0.0041  403 ASN A N   
3115 C CA  . ASN A 403 ? 0.5697 0.4061 0.4353 -0.0521 0.0114  -0.0012 403 ASN A CA  
3116 C C   . ASN A 403 ? 0.6149 0.4525 0.4926 -0.0506 0.0253  -0.0003 403 ASN A C   
3117 O O   . ASN A 403 ? 0.5091 0.3688 0.4159 -0.0514 0.0310  -0.0040 403 ASN A O   
3118 C CB  . ASN A 403 ? 0.5886 0.4558 0.4883 -0.0517 0.0016  -0.0045 403 ASN A CB  
3119 C CG  . ASN A 403 ? 0.5940 0.4809 0.5170 -0.0566 0.0143  -0.0097 403 ASN A CG  
3120 O OD1 . ASN A 403 ? 0.6110 0.4909 0.5231 -0.0621 0.0239  -0.0126 403 ASN A OD1 
3121 N ND2 . ASN A 403 ? 0.5752 0.4851 0.5290 -0.0538 0.0145  -0.0109 403 ASN A ND2 
3122 N N   . SER A 404 ? 0.5319 0.3438 0.3857 -0.0485 0.0304  0.0045  404 SER A N   
3123 C CA  . SER A 404 ? 0.5549 0.3652 0.4195 -0.0487 0.0443  0.0046  404 SER A CA  
3124 C C   . SER A 404 ? 0.5460 0.3604 0.4177 -0.0563 0.0613  -0.0006 404 SER A C   
3125 O O   . SER A 404 ? 0.5453 0.3542 0.4038 -0.0609 0.0649  -0.0026 404 SER A O   
3126 C CB  . SER A 404 ? 0.5984 0.3770 0.4341 -0.0455 0.0472  0.0113  404 SER A CB  
3127 O OG  . SER A 404 ? 0.5869 0.3381 0.3854 -0.0487 0.0516  0.0136  404 SER A OG  
3128 N N   . ARG A 405 ? 0.5361 0.3604 0.4302 -0.0573 0.0709  -0.0034 405 ARG A N   
3129 C CA  . ARG A 405 ? 0.5228 0.3588 0.4333 -0.0632 0.0829  -0.0095 405 ARG A CA  
3130 C C   . ARG A 405 ? 0.5206 0.3488 0.4385 -0.0659 0.0968  -0.0107 405 ARG A C   
3131 O O   . ARG A 405 ? 0.5043 0.3262 0.4243 -0.0627 0.0959  -0.0082 405 ARG A O   
3132 C CB  . ARG A 405 ? 0.4843 0.3501 0.4242 -0.0619 0.0768  -0.0145 405 ARG A CB  
3133 C CG  . ARG A 405 ? 0.5019 0.3789 0.4413 -0.0607 0.0645  -0.0143 405 ARG A CG  
3134 C CD  . ARG A 405 ? 0.5053 0.3879 0.4453 -0.0659 0.0693  -0.0185 405 ARG A CD  
3135 N NE  . ARG A 405 ? 0.4869 0.3761 0.4241 -0.0660 0.0582  -0.0185 405 ARG A NE  
3136 C CZ  . ARG A 405 ? 0.5152 0.4072 0.4506 -0.0700 0.0601  -0.0218 405 ARG A CZ  
3137 N NH1 . ARG A 405 ? 0.4911 0.3830 0.4302 -0.0732 0.0722  -0.0254 405 ARG A NH1 
3138 N NH2 . ARG A 405 ? 0.4898 0.3848 0.4212 -0.0709 0.0493  -0.0217 405 ARG A NH2 
3139 N N   . PHE A 406 ? 0.5087 0.3376 0.4330 -0.0718 0.1098  -0.0148 406 PHE A N   
3140 C CA  . PHE A 406 ? 0.5011 0.3326 0.4457 -0.0752 0.1209  -0.0186 406 PHE A CA  
3141 C C   . PHE A 406 ? 0.4923 0.3510 0.4669 -0.0755 0.1180  -0.0259 406 PHE A C   
3142 O O   . PHE A 406 ? 0.5008 0.3719 0.4774 -0.0751 0.1131  -0.0278 406 PHE A O   
3143 C CB  . PHE A 406 ? 0.4801 0.2927 0.4153 -0.0816 0.1390  -0.0184 406 PHE A CB  
3144 C CG  . PHE A 406 ? 0.4853 0.2987 0.4135 -0.0845 0.1446  -0.0206 406 PHE A CG  
3145 C CD1 . PHE A 406 ? 0.5126 0.3474 0.4676 -0.0867 0.1474  -0.0276 406 PHE A CD1 
3146 C CD2 . PHE A 406 ? 0.5437 0.3343 0.4368 -0.0846 0.1467  -0.0158 406 PHE A CD2 
3147 C CE1 . PHE A 406 ? 0.5216 0.3560 0.4704 -0.0887 0.1529  -0.0298 406 PHE A CE1 
3148 C CE2 . PHE A 406 ? 0.5841 0.3729 0.4688 -0.0871 0.1526  -0.0184 406 PHE A CE2 
3149 C CZ  . PHE A 406 ? 0.5289 0.3400 0.4425 -0.0891 0.1563  -0.0253 406 PHE A CZ  
3150 N N   . CYS A 407 ? 0.4512 0.3173 0.4473 -0.0762 0.1203  -0.0301 407 CYS A N   
3151 C CA  . CYS A 407 ? 0.4260 0.3147 0.4479 -0.0757 0.1165  -0.0372 407 CYS A CA  
3152 C C   . CYS A 407 ? 0.4517 0.3399 0.4928 -0.0812 0.1272  -0.0426 407 CYS A C   
3153 O O   . CYS A 407 ? 0.4671 0.3472 0.5137 -0.0826 0.1303  -0.0431 407 CYS A O   
3154 C CB  . CYS A 407 ? 0.5001 0.3988 0.5294 -0.0698 0.1055  -0.0378 407 CYS A CB  
3155 S SG  . CYS A 407 ? 0.4472 0.3688 0.4992 -0.0677 0.0993  -0.0457 407 CYS A SG  
3156 N N   . THR A 408 ? 0.4601 0.3565 0.5130 -0.0845 0.1329  -0.0468 408 THR A N   
3157 C CA  . THR A 408 ? 0.4072 0.3013 0.4790 -0.0905 0.1455  -0.0512 408 THR A CA  
3158 C C   . THR A 408 ? 0.4392 0.3541 0.5385 -0.0907 0.1430  -0.0592 408 THR A C   
3159 O O   . THR A 408 ? 0.4408 0.3653 0.5366 -0.0874 0.1375  -0.0595 408 THR A O   
3160 C CB  . THR A 408 ? 0.4686 0.3428 0.5223 -0.0950 0.1611  -0.0467 408 THR A CB  
3161 O OG1 . THR A 408 ? 0.4922 0.3607 0.5643 -0.1015 0.1756  -0.0498 408 THR A OG1 
3162 C CG2 . THR A 408 ? 0.4480 0.3262 0.4947 -0.0946 0.1636  -0.0471 408 THR A CG2 
3163 N N   . PRO A 409 ? 0.4357 0.3571 0.5631 -0.0943 0.1462  -0.0658 409 PRO A N   
3164 C CA  . PRO A 409 ? 0.4318 0.3729 0.5868 -0.0934 0.1415  -0.0737 409 PRO A CA  
3165 C C   . PRO A 409 ? 0.4626 0.4055 0.6223 -0.0952 0.1523  -0.0741 409 PRO A C   
3166 O O   . PRO A 409 ? 0.4491 0.3795 0.6066 -0.1005 0.1687  -0.0720 409 PRO A O   
3167 C CB  . PRO A 409 ? 0.4489 0.3937 0.6333 -0.0980 0.1429  -0.0808 409 PRO A CB  
3168 C CG  . PRO A 409 ? 0.4930 0.4221 0.6618 -0.0990 0.1430  -0.0768 409 PRO A CG  
3169 C CD  . PRO A 409 ? 0.4734 0.3850 0.6092 -0.0985 0.1509  -0.0669 409 PRO A CD  
3170 N N   . ALA A 410 ? 0.4133 0.3702 0.5790 -0.0905 0.1441  -0.0769 410 ALA A N   
3171 C CA  . ALA A 410 ? 0.4609 0.4194 0.6310 -0.0910 0.1537  -0.0777 410 ALA A CA  
3172 C C   . ALA A 410 ? 0.4721 0.4379 0.6780 -0.0953 0.1645  -0.0843 410 ALA A C   
3173 O O   . ALA A 410 ? 0.4850 0.4445 0.6928 -0.0982 0.1805  -0.0838 410 ALA A O   
3174 C CB  . ALA A 410 ? 0.4259 0.3962 0.5944 -0.0844 0.1420  -0.0790 410 ALA A CB  
3175 N N   . SER A 411 ? 0.4773 0.4555 0.7123 -0.0960 0.1564  -0.0910 411 SER A N   
3176 C CA  . SER A 411 ? 0.4657 0.4542 0.7415 -0.1004 0.1649  -0.0984 411 SER A CA  
3177 C C   . SER A 411 ? 0.5292 0.5024 0.8069 -0.1091 0.1871  -0.0959 411 SER A C   
3178 O O   . SER A 411 ? 0.5126 0.4921 0.8225 -0.1135 0.2003  -0.1007 411 SER A O   
3179 C CB  . SER A 411 ? 0.5045 0.5076 0.8091 -0.0998 0.1490  -0.1067 411 SER A CB  
3180 O OG  . SER A 411 ? 0.4867 0.4791 0.7799 -0.1031 0.1464  -0.1051 411 SER A OG  
3181 N N   . GLN A 412 ? 0.5117 0.4640 0.7555 -0.1113 0.1921  -0.0882 412 GLN A N   
3182 C CA  . GLN A 412 ? 0.5431 0.4756 0.7808 -0.1189 0.2135  -0.0843 412 GLN A CA  
3183 C C   . GLN A 412 ? 0.5422 0.4594 0.7568 -0.1194 0.2311  -0.0790 412 GLN A C   
3184 O O   . GLN A 412 ? 0.5901 0.4896 0.8005 -0.1256 0.2521  -0.0763 412 GLN A O   
3185 C CB  . GLN A 412 ? 0.5185 0.4322 0.7271 -0.1198 0.2101  -0.0778 412 GLN A CB  
3186 C CG  . GLN A 412 ? 0.5545 0.4761 0.7872 -0.1220 0.2003  -0.0835 412 GLN A CG  
3187 C CD  . GLN A 412 ? 0.5167 0.4191 0.7211 -0.1218 0.1971  -0.0772 412 GLN A CD  
3188 O OE1 . GLN A 412 ? 0.5681 0.4720 0.7865 -0.1235 0.1902  -0.0812 412 GLN A OE1 
3189 N NE2 . GLN A 412 ? 0.5310 0.4144 0.6953 -0.1191 0.2012  -0.0677 412 GLN A NE2 
3190 N N   . CYS A 413 ? 0.5707 0.4918 0.7680 -0.1132 0.2240  -0.0776 413 CYS A N   
3191 C CA  . CYS A 413 ? 0.5381 0.4422 0.7091 -0.1133 0.2394  -0.0733 413 CYS A CA  
3192 C C   . CYS A 413 ? 0.5478 0.4567 0.7509 -0.1171 0.2598  -0.0786 413 CYS A C   
3193 O O   . CYS A 413 ? 0.5103 0.4435 0.7535 -0.1150 0.2539  -0.0863 413 CYS A O   
3194 C CB  . CYS A 413 ? 0.4882 0.3972 0.6386 -0.1062 0.2258  -0.0720 413 CYS A CB  
3195 S SG  . CYS A 413 ? 0.5579 0.4419 0.6677 -0.1060 0.2410  -0.0669 413 CYS A SG  
3196 N N   . PRO A 414 ? 0.5762 0.4620 0.7618 -0.1209 0.2821  -0.0750 414 PRO A N   
3197 C CA  . PRO A 414 ? 0.5444 0.4336 0.7569 -0.1198 0.2967  -0.0804 414 PRO A CA  
3198 C C   . PRO A 414 ? 0.5577 0.4598 0.7839 -0.1149 0.2975  -0.0849 414 PRO A C   
3199 O O   . PRO A 414 ? 0.5360 0.4500 0.7984 -0.1133 0.3042  -0.0912 414 PRO A O   
3200 C CB  . PRO A 414 ? 0.5793 0.4343 0.7538 -0.1217 0.3165  -0.0742 414 PRO A CB  
3201 C CG  . PRO A 414 ? 0.6516 0.4881 0.7870 -0.1241 0.3102  -0.0660 414 PRO A CG  
3202 C CD  . PRO A 414 ? 0.5892 0.4423 0.7242 -0.1228 0.2903  -0.0657 414 PRO A CD  
3203 N N   . ILE A 415 ? 0.5083 0.4074 0.7070 -0.1124 0.2913  -0.0817 415 ILE A N   
3204 C CA  . ILE A 415 ? 0.5076 0.4151 0.7133 -0.1073 0.2928  -0.0853 415 ILE A CA  
3205 C C   . ILE A 415 ? 0.5067 0.4369 0.7236 -0.1009 0.2667  -0.0880 415 ILE A C   
3206 O O   . ILE A 415 ? 0.4865 0.4172 0.6914 -0.0954 0.2616  -0.0882 415 ILE A O   
3207 C CB  . ILE A 415 ? 0.5641 0.4427 0.7192 -0.1065 0.3042  -0.0800 415 ILE A CB  
3208 C CG1 . ILE A 415 ? 0.6023 0.4670 0.7118 -0.1059 0.2877  -0.0728 415 ILE A CG1 
3209 C CG2 . ILE A 415 ? 0.5766 0.4296 0.7172 -0.1079 0.3253  -0.0785 415 ILE A CG2 
3210 C CD1 . ILE A 415 ? 0.6818 0.5182 0.7399 -0.1048 0.2933  -0.0682 415 ILE A CD1 
3211 N N   . ILE A 416 ? 0.4679 0.4140 0.7039 -0.1011 0.2494  -0.0897 416 ILE A N   
3212 C CA  . ILE A 416 ? 0.4705 0.4354 0.7146 -0.0942 0.2251  -0.0922 416 ILE A CA  
3213 C C   . ILE A 416 ? 0.5097 0.4921 0.7888 -0.0890 0.2257  -0.0990 416 ILE A C   
3214 O O   . ILE A 416 ? 0.4833 0.4757 0.8016 -0.0915 0.2380  -0.1046 416 ILE A O   
3215 C CB  . ILE A 416 ? 0.4497 0.4262 0.7091 -0.0954 0.2090  -0.0940 416 ILE A CB  
3216 C CG1 . ILE A 416 ? 0.4990 0.4852 0.7472 -0.0883 0.1850  -0.0936 416 ILE A CG1 
3217 C CG2 . ILE A 416 ? 0.4784 0.4728 0.7895 -0.0983 0.2121  -0.1023 416 ILE A CG2 
3218 C CD1 . ILE A 416 ? 0.4699 0.4399 0.6714 -0.0870 0.1804  -0.0856 416 ILE A CD1 
3219 N N   . ASP A 417 ? 0.4898 0.4751 0.7554 -0.0818 0.2136  -0.0984 417 ASP A N   
3220 C CA  . ASP A 417 ? 0.5000 0.4980 0.7932 -0.0755 0.2146  -0.1039 417 ASP A CA  
3221 C C   . ASP A 417 ? 0.4763 0.4996 0.8154 -0.0721 0.1998  -0.1110 417 ASP A C   
3222 O O   . ASP A 417 ? 0.4857 0.5155 0.8217 -0.0710 0.1808  -0.1109 417 ASP A O   
3223 C CB  . ASP A 417 ? 0.4800 0.4717 0.7444 -0.0689 0.2049  -0.1009 417 ASP A CB  
3224 C CG  . ASP A 417 ? 0.5144 0.5125 0.8005 -0.0622 0.2105  -0.1055 417 ASP A CG  
3225 O OD1 . ASP A 417 ? 0.5087 0.5251 0.8241 -0.0554 0.1962  -0.1100 417 ASP A OD1 
3226 O OD2 . ASP A 417 ? 0.5190 0.5025 0.7921 -0.0632 0.2290  -0.1048 417 ASP A OD2 
3227 N N   . PRO A 418 ? 0.4686 0.5060 0.8510 -0.0700 0.2075  -0.1178 418 PRO A N   
3228 C CA  . PRO A 418 ? 0.4790 0.5409 0.9075 -0.0666 0.1911  -0.1255 418 PRO A CA  
3229 C C   . PRO A 418 ? 0.4910 0.5601 0.9099 -0.0570 0.1644  -0.1257 418 PRO A C   
3230 O O   . PRO A 418 ? 0.5382 0.6218 0.9800 -0.0547 0.1459  -0.1308 418 PRO A O   
3231 C CB  . PRO A 418 ? 0.4509 0.5255 0.9261 -0.0648 0.2062  -0.1321 418 PRO A CB  
3232 C CG  . PRO A 418 ? 0.4825 0.5375 0.9312 -0.0661 0.2303  -0.1276 418 PRO A CG  
3233 C CD  . PRO A 418 ? 0.4884 0.5192 0.8818 -0.0719 0.2337  -0.1191 418 PRO A CD  
3234 N N   . ALA A 419 ? 0.4533 0.5105 0.8372 -0.0515 0.1619  -0.1205 419 ALA A N   
3235 C CA  . ALA A 419 ? 0.5058 0.5658 0.8758 -0.0428 0.1391  -0.1195 419 ALA A CA  
3236 C C   . ALA A 419 ? 0.5139 0.5621 0.8415 -0.0451 0.1292  -0.1130 419 ALA A C   
3237 O O   . ALA A 419 ? 0.5728 0.6182 0.8804 -0.0386 0.1147  -0.1105 419 ALA A O   
3238 C CB  . ALA A 419 ? 0.4473 0.5014 0.8075 -0.0350 0.1418  -0.1180 419 ALA A CB  
3239 N N   . TRP A 420 ? 0.4806 0.5213 0.7949 -0.0538 0.1371  -0.1101 420 TRP A N   
3240 C CA  . TRP A 420 ? 0.5052 0.5341 0.7796 -0.0555 0.1300  -0.1035 420 TRP A CA  
3241 C C   . TRP A 420 ? 0.5186 0.5549 0.7922 -0.0510 0.1088  -0.1050 420 TRP A C   
3242 O O   . TRP A 420 ? 0.4496 0.4778 0.6921 -0.0496 0.1015  -0.0998 420 TRP A O   
3243 C CB  . TRP A 420 ? 0.4695 0.4872 0.7297 -0.0647 0.1429  -0.0998 420 TRP A CB  
3244 C CG  . TRP A 420 ? 0.4944 0.5183 0.7717 -0.0690 0.1383  -0.1029 420 TRP A CG  
3245 C CD1 . TRP A 420 ? 0.4764 0.5095 0.7909 -0.0731 0.1452  -0.1090 420 TRP A CD1 
3246 C CD2 . TRP A 420 ? 0.4818 0.5021 0.7404 -0.0699 0.1271  -0.1002 420 TRP A CD2 
3247 N NE1 . TRP A 420 ? 0.4806 0.5149 0.7993 -0.0769 0.1379  -0.1105 420 TRP A NE1 
3248 C CE2 . TRP A 420 ? 0.4827 0.5088 0.7665 -0.0745 0.1269  -0.1051 420 TRP A CE2 
3249 C CE3 . TRP A 420 ? 0.5096 0.5223 0.7345 -0.0672 0.1178  -0.0945 420 TRP A CE3 
3250 C CZ2 . TRP A 420 ? 0.4725 0.4955 0.7462 -0.0759 0.1175  -0.1046 420 TRP A CZ2 
3251 C CZ3 . TRP A 420 ? 0.4693 0.4805 0.6862 -0.0682 0.1094  -0.0937 420 TRP A CZ3 
3252 C CH2 . TRP A 420 ? 0.4717 0.4872 0.7114 -0.0722 0.1092  -0.0988 420 TRP A CH2 
3253 N N   . GLU A 421 ? 0.4626 0.5132 0.7695 -0.0486 0.0987  -0.1123 421 GLU A N   
3254 C CA  . GLU A 421 ? 0.5114 0.5663 0.8143 -0.0430 0.0775  -0.1146 421 GLU A CA  
3255 C C   . GLU A 421 ? 0.5788 0.6414 0.8953 -0.0326 0.0637  -0.1184 421 GLU A C   
3256 O O   . GLU A 421 ? 0.6064 0.6730 0.9255 -0.0270 0.0451  -0.1222 421 GLU A O   
3257 C CB  . GLU A 421 ? 0.5282 0.5899 0.8523 -0.0478 0.0723  -0.1204 421 GLU A CB  
3258 C CG  . GLU A 421 ? 0.5098 0.5606 0.8145 -0.0562 0.0828  -0.1157 421 GLU A CG  
3259 C CD  . GLU A 421 ? 0.5090 0.5631 0.8285 -0.0604 0.0758  -0.1210 421 GLU A CD  
3260 O OE1 . GLU A 421 ? 0.4606 0.5227 0.8150 -0.0658 0.0819  -0.1269 421 GLU A OE1 
3261 O OE2 . GLU A 421 ? 0.4670 0.5147 0.7636 -0.0585 0.0652  -0.1195 421 GLU A OE2 
3262 N N   . SER A 422 ? 0.5826 0.6451 0.9050 -0.0293 0.0722  -0.1174 422 SER A N   
3263 C CA  . SER A 422 ? 0.6138 0.6822 0.9494 -0.0184 0.0595  -0.1206 422 SER A CA  
3264 C C   . SER A 422 ? 0.6541 0.7099 0.9508 -0.0116 0.0472  -0.1149 422 SER A C   
3265 O O   . SER A 422 ? 0.6414 0.6844 0.9080 -0.0134 0.0564  -0.1079 422 SER A O   
3266 C CB  . SER A 422 ? 0.6059 0.6757 0.9579 -0.0166 0.0741  -0.1210 422 SER A CB  
3267 O OG  . SER A 422 ? 0.6664 0.7485 1.0584 -0.0221 0.0865  -0.1269 422 SER A OG  
3268 N N   . PRO A 423 ? 0.6720 0.7295 0.9671 -0.0041 0.0268  -0.1177 423 PRO A N   
3269 C CA  . PRO A 423 ? 0.7211 0.7639 0.9763 0.0021  0.0175  -0.1117 423 PRO A CA  
3270 C C   . PRO A 423 ? 0.7439 0.7779 0.9871 0.0087  0.0206  -0.1073 423 PRO A C   
3271 O O   . PRO A 423 ? 0.7776 0.7969 0.9858 0.0114  0.0187  -0.1008 423 PRO A O   
3272 C CB  . PRO A 423 ? 0.7677 0.8131 1.0270 0.0097  -0.0051 -0.1173 423 PRO A CB  
3273 C CG  . PRO A 423 ? 0.7114 0.7751 1.0194 0.0110  -0.0101 -0.1265 423 PRO A CG  
3274 C CD  . PRO A 423 ? 0.6904 0.7621 1.0199 -0.0005 0.0112  -0.1269 423 PRO A CD  
3275 N N   . GLU A 424 ? 0.6754 0.7172 0.9472 0.0113  0.0266  -0.1106 424 GLU A N   
3276 C CA  . GLU A 424 ? 0.7079 0.7399 0.9690 0.0179  0.0305  -0.1069 424 GLU A CA  
3277 C C   . GLU A 424 ? 0.6658 0.6871 0.9069 0.0098  0.0506  -0.1013 424 GLU A C   
3278 O O   . GLU A 424 ? 0.6781 0.6877 0.9040 0.0140  0.0545  -0.0976 424 GLU A O   
3279 C CB  . GLU A 424 ? 0.6893 0.7336 0.9906 0.0257  0.0279  -0.1133 424 GLU A CB  
3280 C CG  . GLU A 424 ? 0.6820 0.7382 1.0171 0.0184  0.0468  -0.1176 424 GLU A CG  
3281 C CD  . GLU A 424 ? 0.7997 0.8735 1.1685 0.0123  0.0445  -0.1245 424 GLU A CD  
3282 O OE1 . GLU A 424 ? 0.7792 0.8533 1.1370 0.0105  0.0315  -0.1250 424 GLU A OE1 
3283 O OE2 . GLU A 424 ? 0.9177 1.0039 1.3242 0.0091  0.0570  -0.1297 424 GLU A OE2 
3284 N N   . GLY A 425 ? 0.6166 0.6397 0.8554 -0.0012 0.0624  -0.1006 425 GLY A N   
3285 C CA  . GLY A 425 ? 0.5649 0.5768 0.7832 -0.0087 0.0793  -0.0959 425 GLY A CA  
3286 C C   . GLY A 425 ? 0.5280 0.5413 0.7665 -0.0095 0.0949  -0.0991 425 GLY A C   
3287 O O   . GLY A 425 ? 0.5502 0.5750 0.8224 -0.0038 0.0936  -0.1049 425 GLY A O   
3288 N N   . VAL A 426 ? 0.4798 0.4809 0.6975 -0.0166 0.1100  -0.0957 426 VAL A N   
3289 C CA  . VAL A 426 ? 0.4425 0.4392 0.6704 -0.0174 0.1274  -0.0982 426 VAL A CA  
3290 C C   . VAL A 426 ? 0.4837 0.4629 0.6847 -0.0149 0.1308  -0.0948 426 VAL A C   
3291 O O   . VAL A 426 ? 0.4365 0.4050 0.6064 -0.0177 0.1253  -0.0895 426 VAL A O   
3292 C CB  . VAL A 426 ? 0.4709 0.4640 0.6947 -0.0278 0.1435  -0.0980 426 VAL A CB  
3293 C CG1 . VAL A 426 ? 0.4698 0.4791 0.7237 -0.0306 0.1418  -0.1020 426 VAL A CG1 
3294 C CG2 . VAL A 426 ? 0.4497 0.4287 0.6336 -0.0349 0.1429  -0.0917 426 VAL A CG2 
3295 N N   . PRO A 427 ? 0.4665 0.4417 0.6794 -0.0098 0.1405  -0.0979 427 PRO A N   
3296 C CA  . PRO A 427 ? 0.4911 0.4476 0.6784 -0.0071 0.1433  -0.0952 427 PRO A CA  
3297 C C   . PRO A 427 ? 0.5073 0.4461 0.6653 -0.0165 0.1580  -0.0934 427 PRO A C   
3298 O O   . PRO A 427 ? 0.4777 0.4143 0.6427 -0.0200 0.1740  -0.0965 427 PRO A O   
3299 C CB  . PRO A 427 ? 0.5718 0.5318 0.7873 0.0032  0.1479  -0.1001 427 PRO A CB  
3300 C CG  . PRO A 427 ? 0.4939 0.4707 0.7461 0.0015  0.1573  -0.1057 427 PRO A CG  
3301 C CD  . PRO A 427 ? 0.4655 0.4545 0.7201 -0.0049 0.1474  -0.1045 427 PRO A CD  
3302 N N   . ILE A 428 ? 0.4444 0.4556 0.4759 -0.0614 0.0568  -0.0596 428 ILE A N   
3303 C CA  . ILE A 428 ? 0.4322 0.4016 0.4500 -0.0567 0.0685  -0.0505 428 ILE A CA  
3304 C C   . ILE A 428 ? 0.4892 0.4483 0.5043 -0.0421 0.0640  -0.0350 428 ILE A C   
3305 O O   . ILE A 428 ? 0.4542 0.4218 0.4612 -0.0341 0.0507  -0.0237 428 ILE A O   
3306 C CB  . ILE A 428 ? 0.4579 0.4087 0.4512 -0.0595 0.0685  -0.0472 428 ILE A CB  
3307 C CG1 . ILE A 428 ? 0.4442 0.4021 0.4425 -0.0735 0.0758  -0.0650 428 ILE A CG1 
3308 C CG2 . ILE A 428 ? 0.4730 0.3855 0.4527 -0.0533 0.0762  -0.0360 428 ILE A CG2 
3309 C CD1 . ILE A 428 ? 0.4538 0.3972 0.4708 -0.0809 0.0927  -0.0757 428 ILE A CD1 
3310 N N   . GLU A 429 ? 0.4370 0.3759 0.4578 -0.0389 0.0765  -0.0343 429 GLU A N   
3311 C CA  . GLU A 429 ? 0.4494 0.3756 0.4686 -0.0261 0.0756  -0.0236 429 GLU A CA  
3312 C C   . GLU A 429 ? 0.5148 0.4025 0.5091 -0.0235 0.0820  -0.0161 429 GLU A C   
3313 O O   . GLU A 429 ? 0.4862 0.3598 0.4752 -0.0140 0.0811  -0.0089 429 GLU A O   
3314 C CB  . GLU A 429 ? 0.4571 0.3956 0.5033 -0.0238 0.0851  -0.0304 429 GLU A CB  
3315 C CG  . GLU A 429 ? 0.4558 0.4379 0.5320 -0.0243 0.0756  -0.0370 429 GLU A CG  
3316 C CD  . GLU A 429 ? 0.5413 0.5386 0.6498 -0.0202 0.0849  -0.0429 429 GLU A CD  
3317 O OE1 . GLU A 429 ? 0.5626 0.5443 0.6719 -0.0086 0.0902  -0.0365 429 GLU A OE1 
3318 O OE2 . GLU A 429 ? 0.4952 0.5208 0.6303 -0.0294 0.0880  -0.0556 429 GLU A OE2 
3319 N N   . GLY A 430 ? 0.5046 0.3759 0.4854 -0.0314 0.0881  -0.0183 430 GLY A N   
3320 C CA  . GLY A 430 ? 0.4933 0.3333 0.4512 -0.0290 0.0908  -0.0106 430 GLY A CA  
3321 C C   . GLY A 430 ? 0.5149 0.3467 0.4632 -0.0358 0.0911  -0.0109 430 GLY A C   
3322 O O   . GLY A 430 ? 0.4724 0.3145 0.4320 -0.0437 0.0961  -0.0197 430 GLY A O   
3323 N N   . ILE A 431 ? 0.4778 0.2918 0.4083 -0.0330 0.0861  -0.0026 431 ILE A N   
3324 C CA  . ILE A 431 ? 0.5077 0.3142 0.4322 -0.0372 0.0860  -0.0016 431 ILE A CA  
3325 C C   . ILE A 431 ? 0.5014 0.2828 0.4114 -0.0344 0.0885  0.0055  431 ILE A C   
3326 O O   . ILE A 431 ? 0.4976 0.2689 0.3956 -0.0297 0.0839  0.0107  431 ILE A O   
3327 C CB  . ILE A 431 ? 0.4789 0.2948 0.3984 -0.0370 0.0757  0.0021  431 ILE A CB  
3328 C CG1 . ILE A 431 ? 0.5226 0.3662 0.4516 -0.0407 0.0722  -0.0045 431 ILE A CG1 
3329 C CG2 . ILE A 431 ? 0.5471 0.3547 0.4631 -0.0401 0.0770  0.0031  431 ILE A CG2 
3330 C CD1 . ILE A 431 ? 0.5435 0.3974 0.4632 -0.0413 0.0634  0.0010  431 ILE A CD1 
3331 N N   . ILE A 432 ? 0.4990 0.2702 0.4102 -0.0373 0.0954  0.0057  432 ILE A N   
3332 C CA  . ILE A 432 ? 0.5494 0.2995 0.4461 -0.0344 0.0966  0.0144  432 ILE A CA  
3333 C C   . ILE A 432 ? 0.5384 0.2848 0.4364 -0.0337 0.0914  0.0191  432 ILE A C   
3334 O O   . ILE A 432 ? 0.5413 0.2926 0.4544 -0.0368 0.0964  0.0145  432 ILE A O   
3335 C CB  . ILE A 432 ? 0.5383 0.2772 0.4358 -0.0364 0.1102  0.0151  432 ILE A CB  
3336 C CG1 . ILE A 432 ? 0.5324 0.2799 0.4358 -0.0381 0.1178  0.0082  432 ILE A CG1 
3337 C CG2 . ILE A 432 ? 0.5728 0.2917 0.4486 -0.0326 0.1093  0.0266  432 ILE A CG2 
3338 C CD1 . ILE A 432 ? 0.5509 0.2899 0.4607 -0.0431 0.1348  0.0075  432 ILE A CD1 
3339 N N   . PHE A 433 ? 0.5348 0.2731 0.4195 -0.0302 0.0823  0.0267  433 PHE A N   
3340 C CA  . PHE A 433 ? 0.5217 0.2576 0.4107 -0.0284 0.0771  0.0325  433 PHE A CA  
3341 C C   . PHE A 433 ? 0.5756 0.2960 0.4517 -0.0244 0.0762  0.0427  433 PHE A C   
3342 O O   . PHE A 433 ? 0.5529 0.2644 0.4095 -0.0238 0.0770  0.0450  433 PHE A O   
3343 C CB  . PHE A 433 ? 0.5080 0.2512 0.3953 -0.0286 0.0655  0.0336  433 PHE A CB  
3344 C CG  . PHE A 433 ? 0.5257 0.2837 0.4218 -0.0321 0.0656  0.0274  433 PHE A CG  
3345 C CD1 . PHE A 433 ? 0.5099 0.2793 0.4211 -0.0351 0.0718  0.0215  433 PHE A CD1 
3346 C CD2 . PHE A 433 ? 0.5294 0.2895 0.4180 -0.0326 0.0599  0.0278  433 PHE A CD2 
3347 C CE1 . PHE A 433 ? 0.5230 0.3082 0.4369 -0.0390 0.0714  0.0166  433 PHE A CE1 
3348 C CE2 . PHE A 433 ? 0.5351 0.3088 0.4290 -0.0351 0.0592  0.0259  433 PHE A CE2 
3349 C CZ  . PHE A 433 ? 0.5067 0.2945 0.4111 -0.0387 0.0645  0.0205  433 PHE A CZ  
3350 N N   . GLY A 434 ? 0.5384 0.2563 0.4248 -0.0212 0.0744  0.0494  434 GLY A N   
3351 C CA  . GLY A 434 ? 0.5580 0.2642 0.4309 -0.0160 0.0693  0.0626  434 GLY A CA  
3352 C C   . GLY A 434 ? 0.6061 0.3106 0.4994 -0.0104 0.0694  0.0708  434 GLY A C   
3353 O O   . GLY A 434 ? 0.6058 0.3139 0.5237 -0.0114 0.0780  0.0642  434 GLY A O   
3354 N N   . GLY A 435 ? 0.6258 0.3253 0.5085 -0.0043 0.0593  0.0849  435 GLY A N   
3355 C CA  . GLY A 435 ? 0.6059 0.3038 0.5095 0.0038  0.0570  0.0961  435 GLY A CA  
3356 C C   . GLY A 435 ? 0.6473 0.3351 0.5299 0.0108  0.0485  0.1156  435 GLY A C   
3357 O O   . GLY A 435 ? 0.6360 0.3168 0.4850 0.0079  0.0470  0.1186  435 GLY A O   
3358 N N   . ARG A 436 ? 0.6097 0.2980 0.5126 0.0206  0.0430  0.1290  436 ARG A N   
3359 C CA  . ARG A 436 ? 0.6625 0.3435 0.5476 0.0293  0.0325  0.1516  436 ARG A CA  
3360 C C   . ARG A 436 ? 0.6989 0.4001 0.5692 0.0296  0.0087  0.1533  436 ARG A C   
3361 O O   . ARG A 436 ? 0.6516 0.3713 0.5493 0.0342  -0.0035 0.1537  436 ARG A O   
3362 C CB  . ARG A 436 ? 0.6836 0.3568 0.6016 0.0415  0.0360  0.1667  436 ARG A CB  
3363 C CG  . ARG A 436 ? 0.7081 0.3549 0.6336 0.0410  0.0591  0.1694  436 ARG A CG  
3364 C CD  . ARG A 436 ? 0.6929 0.3366 0.6620 0.0507  0.0644  0.1743  436 ARG A CD  
3365 N NE  . ARG A 436 ? 0.7169 0.3494 0.6956 0.0445  0.0828  0.1652  436 ARG A NE  
3366 C CZ  . ARG A 436 ? 0.7411 0.3595 0.7073 0.0461  0.0862  0.1797  436 ARG A CZ  
3367 N NH1 . ARG A 436 ? 0.7685 0.3826 0.7114 0.0546  0.0716  0.2048  436 ARG A NH1 
3368 N NH2 . ARG A 436 ? 0.7502 0.3596 0.7271 0.0387  0.1044  0.1693  436 ARG A NH2 
3369 N N   . ARG A 437 ? 0.6506 0.3492 0.4790 0.0239  0.0028  0.1528  437 ARG A N   
3370 C CA  . ARG A 437 ? 0.7070 0.4236 0.5174 0.0220  -0.0197 0.1520  437 ARG A CA  
3371 C C   . ARG A 437 ? 0.6965 0.4050 0.4652 0.0255  -0.0274 0.1698  437 ARG A C   
3372 O O   . ARG A 437 ? 0.7197 0.4140 0.4521 0.0192  -0.0170 0.1662  437 ARG A O   
3373 C CB  . ARG A 437 ? 0.6032 0.3255 0.4005 0.0098  -0.0198 0.1299  437 ARG A CB  
3374 C CG  . ARG A 437 ? 0.6388 0.3718 0.4714 0.0053  -0.0151 0.1143  437 ARG A CG  
3375 C CD  . ARG A 437 ? 0.6764 0.4304 0.5443 0.0098  -0.0281 0.1175  437 ARG A CD  
3376 N NE  . ARG A 437 ? 0.6275 0.3991 0.4864 0.0079  -0.0506 0.1187  437 ARG A NE  
3377 C CZ  . ARG A 437 ? 0.6127 0.3966 0.4738 -0.0021 -0.0584 0.1039  437 ARG A CZ  
3378 N NH1 . ARG A 437 ? 0.5830 0.3611 0.4491 -0.0102 -0.0457 0.0893  437 ARG A NH1 
3379 N NH2 . ARG A 437 ? 0.6453 0.4480 0.5046 -0.0043 -0.0797 0.1045  437 ARG A NH2 
3380 N N   . PRO A 438 ? 0.7395 0.4576 0.5117 0.0358  -0.0449 0.1897  438 PRO A N   
3381 C CA  . PRO A 438 ? 0.7912 0.5026 0.5185 0.0396  -0.0534 0.2099  438 PRO A CA  
3382 C C   . PRO A 438 ? 0.7833 0.5075 0.4667 0.0298  -0.0690 0.1990  438 PRO A C   
3383 O O   . PRO A 438 ? 0.8205 0.5375 0.4565 0.0295  -0.0719 0.2110  438 PRO A O   
3384 C CB  . PRO A 438 ? 0.8120 0.5346 0.5643 0.0551  -0.0703 0.2346  438 PRO A CB  
3385 C CG  . PRO A 438 ? 0.7827 0.5299 0.5850 0.0552  -0.0794 0.2196  438 PRO A CG  
3386 C CD  . PRO A 438 ? 0.7254 0.4626 0.5444 0.0451  -0.0570 0.1955  438 PRO A CD  
3387 N N   . ALA A 439 ? 0.7617 0.5031 0.4581 0.0209  -0.0775 0.1761  439 ALA A N   
3388 C CA  . ALA A 439 ? 0.7971 0.5509 0.4576 0.0108  -0.0932 0.1629  439 ALA A CA  
3389 C C   . ALA A 439 ? 0.7239 0.4754 0.3918 -0.0018 -0.0836 0.1342  439 ALA A C   
3390 O O   . ALA A 439 ? 0.6782 0.4313 0.3870 -0.0021 -0.0753 0.1258  439 ALA A O   
3391 C CB  . ALA A 439 ? 0.7742 0.5590 0.4469 0.0136  -0.1238 0.1683  439 ALA A CB  
3392 N N   . GLY A 440 ? 0.7348 0.4819 0.3617 -0.0118 -0.0841 0.1197  440 GLY A N   
3393 C CA  . GLY A 440 ? 0.7566 0.5045 0.3890 -0.0236 -0.0818 0.0931  440 GLY A CA  
3394 C C   . GLY A 440 ? 0.8004 0.5288 0.4426 -0.0265 -0.0568 0.0804  440 GLY A C   
3395 O O   . GLY A 440 ? 0.7930 0.5147 0.4229 -0.0352 -0.0517 0.0607  440 GLY A O   
3396 N N   . VAL A 441 ? 0.7453 0.4654 0.4117 -0.0194 -0.0418 0.0906  441 VAL A N   
3397 C CA  . VAL A 441 ? 0.7071 0.4153 0.3905 -0.0216 -0.0214 0.0794  441 VAL A CA  
3398 C C   . VAL A 441 ? 0.7251 0.4155 0.3799 -0.0212 -0.0029 0.0813  441 VAL A C   
3399 O O   . VAL A 441 ? 0.7034 0.3873 0.3499 -0.0154 0.0025  0.0987  441 VAL A O   
3400 C CB  . VAL A 441 ? 0.7137 0.4263 0.4409 -0.0163 -0.0157 0.0854  441 VAL A CB  
3401 C CG1 . VAL A 441 ? 0.6760 0.3795 0.4167 -0.0188 0.0035  0.0747  441 VAL A CG1 
3402 C CG2 . VAL A 441 ? 0.6763 0.4082 0.4326 -0.0177 -0.0315 0.0822  441 VAL A CG2 
3403 N N   . PRO A 442 ? 0.7315 0.4133 0.3740 -0.0269 0.0087  0.0648  442 PRO A N   
3404 C CA  . PRO A 442 ? 0.7579 0.4258 0.3727 -0.0274 0.0270  0.0649  442 PRO A CA  
3405 C C   . PRO A 442 ? 0.7284 0.3899 0.3678 -0.0239 0.0459  0.0709  442 PRO A C   
3406 O O   . PRO A 442 ? 0.6957 0.3630 0.3717 -0.0216 0.0457  0.0715  442 PRO A O   
3407 C CB  . PRO A 442 ? 0.8015 0.4649 0.4052 -0.0338 0.0325  0.0425  442 PRO A CB  
3408 C CG  . PRO A 442 ? 0.7770 0.4476 0.4151 -0.0352 0.0239  0.0332  442 PRO A CG  
3409 C CD  . PRO A 442 ? 0.7668 0.4509 0.4211 -0.0329 0.0057  0.0455  442 PRO A CD  
3410 N N   . LEU A 443 ? 0.7251 0.3755 0.3426 -0.0248 0.0634  0.0736  443 LEU A N   
3411 C CA  . LEU A 443 ? 0.7192 0.3633 0.3570 -0.0233 0.0821  0.0803  443 LEU A CA  
3412 C C   . LEU A 443 ? 0.7114 0.3623 0.3876 -0.0242 0.0891  0.0662  443 LEU A C   
3413 O O   . LEU A 443 ? 0.6603 0.3135 0.3664 -0.0228 0.0943  0.0703  443 LEU A O   
3414 C CB  . LEU A 443 ? 0.7665 0.3990 0.3735 -0.0263 0.1014  0.0830  443 LEU A CB  
3415 C CG  . LEU A 443 ? 0.7609 0.3874 0.3892 -0.0277 0.1243  0.0859  443 LEU A CG  
3416 C CD1 . LEU A 443 ? 0.7529 0.3731 0.3994 -0.0241 0.1240  0.1051  443 LEU A CD1 
3417 C CD2 . LEU A 443 ? 0.8520 0.4692 0.4475 -0.0321 0.1442  0.0862  443 LEU A CD2 
3418 N N   . VAL A 444 ? 0.6216 0.2760 0.2978 -0.0264 0.0890  0.0496  444 VAL A N   
3419 C CA  . VAL A 444 ? 0.5970 0.2592 0.3073 -0.0261 0.0937  0.0389  444 VAL A CA  
3420 C C   . VAL A 444 ? 0.6493 0.3122 0.3571 -0.0269 0.0869  0.0249  444 VAL A C   
3421 O O   . VAL A 444 ? 0.6722 0.3276 0.3529 -0.0289 0.0890  0.0175  444 VAL A O   
3422 C CB  . VAL A 444 ? 0.6612 0.3232 0.3828 -0.0270 0.1146  0.0356  444 VAL A CB  
3423 C CG1 . VAL A 444 ? 0.6861 0.3401 0.3798 -0.0289 0.1277  0.0293  444 VAL A CG1 
3424 C CG2 . VAL A 444 ? 0.5851 0.2601 0.3431 -0.0260 0.1163  0.0259  444 VAL A CG2 
3425 N N   . TYR A 445 ? 0.5778 0.2487 0.3131 -0.0259 0.0797  0.0213  445 TYR A N   
3426 C CA  . TYR A 445 ? 0.6072 0.2759 0.3477 -0.0260 0.0774  0.0094  445 TYR A CA  
3427 C C   . TYR A 445 ? 0.5915 0.2703 0.3651 -0.0232 0.0789  0.0089  445 TYR A C   
3428 O O   . TYR A 445 ? 0.5830 0.2717 0.3729 -0.0228 0.0797  0.0154  445 TYR A O   
3429 C CB  . TYR A 445 ? 0.6028 0.2684 0.3328 -0.0296 0.0615  0.0068  445 TYR A CB  
3430 C CG  . TYR A 445 ? 0.6125 0.2881 0.3595 -0.0306 0.0478  0.0152  445 TYR A CG  
3431 C CD1 . TYR A 445 ? 0.6502 0.3306 0.3891 -0.0307 0.0394  0.0254  445 TYR A CD1 
3432 C CD2 . TYR A 445 ? 0.6381 0.3186 0.4096 -0.0311 0.0437  0.0137  445 TYR A CD2 
3433 C CE1 . TYR A 445 ? 0.6436 0.3348 0.4022 -0.0310 0.0284  0.0317  445 TYR A CE1 
3434 C CE2 . TYR A 445 ? 0.6260 0.3168 0.4130 -0.0329 0.0338  0.0202  445 TYR A CE2 
3435 C CZ  . TYR A 445 ? 0.6467 0.3434 0.4291 -0.0327 0.0265  0.0280  445 TYR A CZ  
3436 O OH  . TYR A 445 ? 0.6841 0.3930 0.4867 -0.0338 0.0182  0.0333  445 TYR A OH  
3437 N N   . GLU A 446 ? 0.5988 0.2747 0.3818 -0.0210 0.0801  0.0009  446 GLU A N   
3438 C CA  . GLU A 446 ? 0.6023 0.2886 0.4136 -0.0171 0.0804  0.0022  446 GLU A CA  
3439 C C   . GLU A 446 ? 0.5892 0.2713 0.4079 -0.0177 0.0696  0.0031  446 GLU A C   
3440 O O   . GLU A 446 ? 0.6161 0.2840 0.4237 -0.0197 0.0671  -0.0034 446 GLU A O   
3441 C CB  . GLU A 446 ? 0.6080 0.2956 0.4300 -0.0117 0.0931  -0.0050 446 GLU A CB  
3442 C CG  . GLU A 446 ? 0.5897 0.2906 0.4412 -0.0059 0.0916  -0.0028 446 GLU A CG  
3443 C CD  . GLU A 446 ? 0.6371 0.3378 0.5019 0.0012  0.1029  -0.0107 446 GLU A CD  
3444 O OE1 . GLU A 446 ? 0.6859 0.3864 0.5440 0.0003  0.1158  -0.0170 446 GLU A OE1 
3445 O OE2 . GLU A 446 ? 0.6500 0.3500 0.5326 0.0081  0.0999  -0.0100 446 GLU A OE2 
3446 N N   . ALA A 447 ? 0.5795 0.2739 0.4164 -0.0171 0.0643  0.0104  447 ALA A N   
3447 C CA  . ALA A 447 ? 0.5701 0.2610 0.4145 -0.0188 0.0558  0.0142  447 ALA A CA  
3448 C C   . ALA A 447 ? 0.5965 0.2768 0.4504 -0.0132 0.0590  0.0116  447 ALA A C   
3449 O O   . ALA A 447 ? 0.6103 0.2941 0.4731 -0.0064 0.0665  0.0090  447 ALA A O   
3450 C CB  . ALA A 447 ? 0.5635 0.2718 0.4211 -0.0200 0.0516  0.0231  447 ALA A CB  
3451 N N   . LEU A 448 ? 0.6105 0.2774 0.4661 -0.0162 0.0540  0.0125  448 LEU A N   
3452 C CA  . LEU A 448 ? 0.5981 0.2484 0.4642 -0.0109 0.0578  0.0101  448 LEU A CA  
3453 C C   . LEU A 448 ? 0.6610 0.3196 0.5471 -0.0039 0.0560  0.0236  448 LEU A C   
3454 O O   . LEU A 448 ? 0.6148 0.2626 0.5145 0.0044  0.0600  0.0245  448 LEU A O   
3455 C CB  . LEU A 448 ? 0.6070 0.2369 0.4683 -0.0187 0.0542  0.0047  448 LEU A CB  
3456 C CG  . LEU A 448 ? 0.6633 0.2875 0.5025 -0.0271 0.0520  -0.0083 448 LEU A CG  
3457 C CD1 . LEU A 448 ? 0.7303 0.3411 0.5703 -0.0372 0.0455  -0.0130 448 LEU A CD1 
3458 C CD2 . LEU A 448 ? 0.7064 0.3197 0.5345 -0.0229 0.0624  -0.0224 448 LEU A CD2 
3459 N N   . SER A 449 ? 0.6189 0.2961 0.5064 -0.0068 0.0502  0.0340  449 SER A N   
3460 C CA  . SER A 449 ? 0.6093 0.2965 0.5092 -0.0022 0.0465  0.0485  449 SER A CA  
3461 C C   . SER A 449 ? 0.5793 0.2909 0.4743 -0.0076 0.0426  0.0530  449 SER A C   
3462 O O   . SER A 449 ? 0.5538 0.2697 0.4401 -0.0139 0.0432  0.0460  449 SER A O   
3463 C CB  . SER A 449 ? 0.6509 0.3184 0.5549 -0.0046 0.0445  0.0571  449 SER A CB  
3464 O OG  . SER A 449 ? 0.5991 0.2659 0.4946 -0.0167 0.0414  0.0567  449 SER A OG  
3465 N N   . TRP A 450 ? 0.6280 0.3552 0.5285 -0.0049 0.0387  0.0648  450 TRP A N   
3466 C CA  . TRP A 450 ? 0.5777 0.3273 0.4723 -0.0113 0.0364  0.0670  450 TRP A CA  
3467 C C   . TRP A 450 ? 0.5494 0.2921 0.4371 -0.0214 0.0365  0.0676  450 TRP A C   
3468 O O   . TRP A 450 ? 0.5351 0.2882 0.4194 -0.0271 0.0378  0.0612  450 TRP A O   
3469 C CB  . TRP A 450 ? 0.5849 0.3527 0.4819 -0.0074 0.0314  0.0799  450 TRP A CB  
3470 C CG  . TRP A 450 ? 0.5962 0.3886 0.4855 -0.0146 0.0304  0.0783  450 TRP A CG  
3471 C CD1 . TRP A 450 ? 0.6014 0.4011 0.4811 -0.0212 0.0297  0.0868  450 TRP A CD1 
3472 C CD2 . TRP A 450 ? 0.5603 0.3721 0.4513 -0.0171 0.0323  0.0658  450 TRP A CD2 
3473 N NE1 . TRP A 450 ? 0.5801 0.4034 0.4547 -0.0272 0.0310  0.0785  450 TRP A NE1 
3474 C CE2 . TRP A 450 ? 0.5895 0.4194 0.4721 -0.0249 0.0324  0.0655  450 TRP A CE2 
3475 C CE3 . TRP A 450 ? 0.5851 0.4000 0.4847 -0.0143 0.0357  0.0543  450 TRP A CE3 
3476 C CZ2 . TRP A 450 ? 0.5880 0.4370 0.4722 -0.0298 0.0353  0.0525  450 TRP A CZ2 
3477 C CZ3 . TRP A 450 ? 0.5557 0.3892 0.4574 -0.0197 0.0386  0.0436  450 TRP A CZ3 
3478 C CH2 . TRP A 450 ? 0.5704 0.4199 0.4651 -0.0273 0.0381  0.0420  450 TRP A CH2 
3479 N N   . GLN A 451 ? 0.5851 0.3101 0.4742 -0.0236 0.0358  0.0752  451 GLN A N   
3480 C CA  . GLN A 451 ? 0.5631 0.2839 0.4509 -0.0340 0.0362  0.0762  451 GLN A CA  
3481 C C   . GLN A 451 ? 0.5629 0.2786 0.4492 -0.0385 0.0356  0.0628  451 GLN A C   
3482 O O   . GLN A 451 ? 0.5754 0.3022 0.4628 -0.0449 0.0352  0.0603  451 GLN A O   
3483 C CB  . GLN A 451 ? 0.6513 0.3509 0.5442 -0.0362 0.0370  0.0862  451 GLN A CB  
3484 C CG  . GLN A 451 ? 0.6626 0.3663 0.5549 -0.0324 0.0370  0.1051  451 GLN A CG  
3485 C CD  . GLN A 451 ? 0.7479 0.4527 0.6438 -0.0186 0.0342  0.1099  451 GLN A CD  
3486 O OE1 . GLN A 451 ? 0.6872 0.3802 0.5898 -0.0123 0.0352  0.1000  451 GLN A OE1 
3487 N NE2 . GLN A 451 ? 0.7486 0.4705 0.6403 -0.0141 0.0308  0.1248  451 GLN A NE2 
3488 N N   . HIS A 452 ? 0.5537 0.2539 0.4375 -0.0348 0.0357  0.0543  452 HIS A N   
3489 C CA  . HIS A 452 ? 0.5281 0.2255 0.4051 -0.0383 0.0338  0.0432  452 HIS A CA  
3490 C C   . HIS A 452 ? 0.5340 0.2490 0.4077 -0.0364 0.0349  0.0410  452 HIS A C   
3491 O O   . HIS A 452 ? 0.5402 0.2608 0.4128 -0.0403 0.0323  0.0384  452 HIS A O   
3492 C CB  . HIS A 452 ? 0.5967 0.2750 0.4671 -0.0349 0.0356  0.0337  452 HIS A CB  
3493 C CG  . HIS A 452 ? 0.5856 0.2616 0.4431 -0.0389 0.0325  0.0235  452 HIS A CG  
3494 N ND1 . HIS A 452 ? 0.6047 0.2774 0.4493 -0.0344 0.0365  0.0161  452 HIS A ND1 
3495 C CD2 . HIS A 452 ? 0.5488 0.2276 0.4043 -0.0468 0.0253  0.0207  452 HIS A CD2 
3496 C CE1 . HIS A 452 ? 0.6226 0.2951 0.4536 -0.0392 0.0314  0.0108  452 HIS A CE1 
3497 N NE2 . HIS A 452 ? 0.6108 0.2880 0.4494 -0.0463 0.0234  0.0131  452 HIS A NE2 
3498 N N   . GLY A 453 ? 0.5288 0.2534 0.4040 -0.0305 0.0387  0.0423  453 GLY A N   
3499 C CA  . GLY A 453 ? 0.5065 0.2452 0.3813 -0.0300 0.0417  0.0389  453 GLY A CA  
3500 C C   . GLY A 453 ? 0.5112 0.2646 0.3916 -0.0352 0.0414  0.0413  453 GLY A C   
3501 O O   . GLY A 453 ? 0.5042 0.2619 0.3861 -0.0363 0.0430  0.0378  453 GLY A O   
3502 N N   . VAL A 454 ? 0.4898 0.2503 0.3734 -0.0379 0.0405  0.0478  454 VAL A N   
3503 C CA  . VAL A 454 ? 0.4905 0.2652 0.3792 -0.0437 0.0426  0.0486  454 VAL A CA  
3504 C C   . VAL A 454 ? 0.4969 0.2664 0.3915 -0.0477 0.0402  0.0471  454 VAL A C   
3505 O O   . VAL A 454 ? 0.5105 0.2900 0.4131 -0.0492 0.0425  0.0438  454 VAL A O   
3506 C CB  . VAL A 454 ? 0.5345 0.3172 0.4212 -0.0467 0.0434  0.0575  454 VAL A CB  
3507 C CG1 . VAL A 454 ? 0.5063 0.3032 0.3978 -0.0539 0.0482  0.0567  454 VAL A CG1 
3508 C CG2 . VAL A 454 ? 0.5144 0.3090 0.3959 -0.0422 0.0430  0.0592  454 VAL A CG2 
3509 N N   . PHE A 455 ? 0.5370 0.2916 0.4300 -0.0494 0.0354  0.0484  455 PHE A N   
3510 C CA  . PHE A 455 ? 0.5198 0.2730 0.4195 -0.0540 0.0304  0.0457  455 PHE A CA  
3511 C C   . PHE A 455 ? 0.5220 0.2754 0.4180 -0.0497 0.0274  0.0410  455 PHE A C   
3512 O O   . PHE A 455 ? 0.5203 0.2825 0.4262 -0.0510 0.0238  0.0407  455 PHE A O   
3513 C CB  . PHE A 455 ? 0.5351 0.2714 0.4331 -0.0582 0.0258  0.0451  455 PHE A CB  
3514 C CG  . PHE A 455 ? 0.5505 0.2865 0.4521 -0.0629 0.0177  0.0392  455 PHE A CG  
3515 C CD1 . PHE A 455 ? 0.5607 0.3092 0.4798 -0.0703 0.0152  0.0402  455 PHE A CD1 
3516 C CD2 . PHE A 455 ? 0.5815 0.3079 0.4689 -0.0600 0.0125  0.0326  455 PHE A CD2 
3517 C CE1 . PHE A 455 ? 0.5236 0.2771 0.4488 -0.0744 0.0052  0.0347  455 PHE A CE1 
3518 C CE2 . PHE A 455 ? 0.5799 0.3097 0.4676 -0.0644 0.0025  0.0276  455 PHE A CE2 
3519 C CZ  . PHE A 455 ? 0.5789 0.3235 0.4868 -0.0713 -0.0024 0.0288  455 PHE A CZ  
3520 N N   . VAL A 456 ? 0.5125 0.2572 0.3957 -0.0441 0.0293  0.0385  456 VAL A N   
3521 C CA  . VAL A 456 ? 0.5119 0.2548 0.3885 -0.0402 0.0286  0.0368  456 VAL A CA  
3522 C C   . VAL A 456 ? 0.5285 0.2839 0.4174 -0.0384 0.0335  0.0383  456 VAL A C   
3523 O O   . VAL A 456 ? 0.4921 0.2494 0.3854 -0.0363 0.0305  0.0405  456 VAL A O   
3524 C CB  . VAL A 456 ? 0.5378 0.2697 0.3997 -0.0359 0.0334  0.0337  456 VAL A CB  
3525 C CG1 . VAL A 456 ? 0.5435 0.2740 0.3988 -0.0324 0.0365  0.0347  456 VAL A CG1 
3526 C CG2 . VAL A 456 ? 0.5514 0.2687 0.4012 -0.0371 0.0297  0.0295  456 VAL A CG2 
3527 N N   . GLY A 457 ? 0.4759 0.2400 0.3709 -0.0389 0.0409  0.0369  457 GLY A N   
3528 C CA  . GLY A 457 ? 0.4731 0.2484 0.3816 -0.0388 0.0472  0.0348  457 GLY A CA  
3529 C C   . GLY A 457 ? 0.4834 0.2683 0.4077 -0.0412 0.0451  0.0364  457 GLY A C   
3530 O O   . GLY A 457 ? 0.4839 0.2723 0.4214 -0.0381 0.0470  0.0363  457 GLY A O   
3531 N N   . ALA A 458 ? 0.4696 0.2586 0.3955 -0.0464 0.0420  0.0385  458 ALA A N   
3532 C CA  . ALA A 458 ? 0.4582 0.2593 0.4027 -0.0502 0.0415  0.0393  458 ALA A CA  
3533 C C   . ALA A 458 ? 0.4973 0.2977 0.4507 -0.0475 0.0316  0.0412  458 ALA A C   
3534 O O   . ALA A 458 ? 0.4759 0.2897 0.4516 -0.0470 0.0316  0.0414  458 ALA A O   
3535 C CB  . ALA A 458 ? 0.4857 0.2882 0.4291 -0.0579 0.0413  0.0424  458 ALA A CB  
3536 N N   . ALA A 459 ? 0.4680 0.2549 0.4043 -0.0454 0.0233  0.0425  459 ALA A N   
3537 C CA  . ALA A 459 ? 0.4981 0.2858 0.4358 -0.0438 0.0110  0.0447  459 ALA A CA  
3538 C C   . ALA A 459 ? 0.4755 0.2609 0.4116 -0.0348 0.0100  0.0493  459 ALA A C   
3539 O O   . ALA A 459 ? 0.4882 0.2768 0.4242 -0.0321 -0.0017 0.0538  459 ALA A O   
3540 C CB  . ALA A 459 ? 0.5204 0.2944 0.4364 -0.0475 0.0031  0.0419  459 ALA A CB  
3541 N N   . MET A 460 ? 0.4775 0.2581 0.4134 -0.0307 0.0218  0.0490  460 MET A N   
3542 C CA  . MET A 460 ? 0.5028 0.2763 0.4379 -0.0228 0.0236  0.0548  460 MET A CA  
3543 C C   . MET A 460 ? 0.4908 0.2750 0.4490 -0.0168 0.0167  0.0617  460 MET A C   
3544 O O   . MET A 460 ? 0.5182 0.3179 0.5031 -0.0178 0.0186  0.0588  460 MET A O   
3545 C CB  . MET A 460 ? 0.4961 0.2653 0.4364 -0.0218 0.0391  0.0504  460 MET A CB  
3546 C CG  . MET A 460 ? 0.5390 0.2986 0.4583 -0.0249 0.0444  0.0460  460 MET A CG  
3547 S SD  . MET A 460 ? 0.5539 0.3155 0.4835 -0.0267 0.0604  0.0375  460 MET A SD  
3548 C CE  . MET A 460 ? 0.5009 0.2515 0.4439 -0.0199 0.0667  0.0434  460 MET A CE  
3549 N N   . ARG A 461 ? 0.4550 0.2320 0.4026 -0.0101 0.0088  0.0718  461 ARG A N   
3550 C CA  . ARG A 461 ? 0.5255 0.3115 0.4945 -0.0012 0.0007  0.0823  461 ARG A CA  
3551 C C   . ARG A 461 ? 0.5343 0.3028 0.4924 0.0077  0.0047  0.0943  461 ARG A C   
3552 O O   . ARG A 461 ? 0.5443 0.2966 0.4724 0.0053  0.0090  0.0951  461 ARG A O   
3553 C CB  . ARG A 461 ? 0.5071 0.3076 0.4731 -0.0027 -0.0200 0.0858  461 ARG A CB  
3554 C CG  . ARG A 461 ? 0.4835 0.3001 0.4651 -0.0127 -0.0224 0.0747  461 ARG A CG  
3555 C CD  . ARG A 461 ? 0.5847 0.4143 0.5618 -0.0168 -0.0427 0.0753  461 ARG A CD  
3556 N NE  . ARG A 461 ? 0.5580 0.4096 0.5664 -0.0092 -0.0546 0.0836  461 ARG A NE  
3557 C CZ  . ARG A 461 ? 0.6165 0.4832 0.6224 -0.0089 -0.0760 0.0882  461 ARG A CZ  
3558 N NH1 . ARG A 461 ? 0.5693 0.4291 0.5392 -0.0164 -0.0868 0.0838  461 ARG A NH1 
3559 N NH2 . ARG A 461 ? 0.5949 0.4856 0.6363 -0.0006 -0.0871 0.0965  461 ARG A NH2 
3560 N N   . SER A 462 ? 0.5446 0.3160 0.5295 0.0181  0.0044  0.1045  462 SER A N   
3561 C CA  . SER A 462 ? 0.6101 0.3607 0.5903 0.0264  0.0128  0.1169  462 SER A CA  
3562 C C   . SER A 462 ? 0.6530 0.4087 0.6643 0.0404  0.0067  0.1323  462 SER A C   
3563 O O   . SER A 462 ? 0.6215 0.3947 0.6704 0.0435  0.0065  0.1271  462 SER A O   
3564 C CB  . SER A 462 ? 0.5833 0.3200 0.5712 0.0220  0.0355  0.1052  462 SER A CB  
3565 O OG  . SER A 462 ? 0.6012 0.3150 0.5844 0.0273  0.0459  0.1158  462 SER A OG  
3566 N N   . GLU A 463 ? 0.6785 0.4188 0.6746 0.0493  0.0027  0.1521  463 GLU A N   
3567 C CA  . GLU A 463 ? 0.7814 0.5208 0.8084 0.0652  -0.0008 0.1705  463 GLU A CA  
3568 C C   . GLU A 463 ? 0.7289 0.4590 0.7972 0.0684  0.0214  0.1611  463 GLU A C   
3569 O O   . GLU A 463 ? 0.7084 0.4203 0.7693 0.0605  0.0409  0.1493  463 GLU A O   
3570 C CB  . GLU A 463 ? 0.8280 0.5454 0.8269 0.0731  -0.0035 0.1949  463 GLU A CB  
3571 C CG  . GLU A 463 ? 0.9233 0.6537 0.8885 0.0754  -0.0290 0.2101  463 GLU A CG  
3572 C CD  . GLU A 463 ? 1.0260 0.7354 0.9680 0.0859  -0.0308 0.2389  463 GLU A CD  
3573 O OE1 . GLU A 463 ? 1.0398 0.7203 0.9872 0.0883  -0.0092 0.2447  463 GLU A OE1 
3574 O OE2 . GLU A 463 ? 1.1100 0.8322 1.0283 0.0912  -0.0536 0.2559  463 GLU A OE2 
3575 N N   . ALA A 464 ? 0.7694 0.5136 0.8829 0.0796  0.0185  0.1646  464 ALA A N   
3576 C CA  . ALA A 464 ? 0.7851 0.5195 0.9400 0.0837  0.0409  0.1544  464 ALA A CA  
3577 C C   . ALA A 464 ? 0.8201 0.5191 0.9747 0.0911  0.0551  0.1683  464 ALA A C   
3578 O O   . ALA A 464 ? 0.8332 0.5196 0.9677 0.0995  0.0445  0.1934  464 ALA A O   
3579 C CB  . ALA A 464 ? 0.8180 0.5758 1.0249 0.0959  0.0356  0.1561  464 ALA A CB  
3580 N N   . THR A 465 ? 0.7910 0.4757 0.9655 0.0862  0.0793  0.1504  465 THR A N   
3581 C CA  . THR A 465 ? 0.7354 0.3999 0.9060 0.0856  0.0925  0.1508  465 THR A CA  
3582 C C   . THR A 465 ? 0.7901 0.4548 1.0098 0.0926  0.1077  0.1406  465 THR A C   
3583 O O   . THR A 465 ? 0.7483 0.4299 1.0039 0.0984  0.1083  0.1331  465 THR A O   
3584 C CB  . THR A 465 ? 0.7715 0.4264 0.9131 0.0677  0.1061  0.1328  465 THR A CB  
3585 O OG1 . THR A 465 ? 0.7230 0.3869 0.8850 0.0584  0.1213  0.1051  465 THR A OG1 
3586 C CG2 . THR A 465 ? 0.7667 0.4236 0.8624 0.0598  0.0937  0.1384  465 THR A CG2 
3587 N N   . ALA A 466 ? 0.7502 0.3963 0.9732 0.0913  0.1216  0.1395  466 ALA A N   
3588 C CA  . ALA A 466 ? 0.7193 0.3614 0.9868 0.0969  0.1382  0.1297  466 ALA A CA  
3589 C C   . ALA A 466 ? 0.6950 0.3423 0.9764 0.0825  0.1596  0.0959  466 ALA A C   
3590 O O   . ALA A 466 ? 0.7382 0.3819 1.0544 0.0844  0.1762  0.0836  466 ALA A O   
3591 C CB  . ALA A 466 ? 0.7006 0.3184 0.9670 0.1015  0.1443  0.1447  466 ALA A CB  
3592 N N   . ALA A 467 ? 0.7434 0.3994 0.9979 0.0681  0.1595  0.0803  467 ALA A N   
3593 C CA  . ALA A 467 ? 0.6809 0.3433 0.9442 0.0539  0.1783  0.0488  467 ALA A CA  
3594 C C   . ALA A 467 ? 0.6764 0.3546 0.9765 0.0578  0.1863  0.0335  467 ALA A C   
3595 O O   . ALA A 467 ? 0.6872 0.3685 1.0035 0.0490  0.2052  0.0081  467 ALA A O   
3596 C CB  . ALA A 467 ? 0.6635 0.3327 0.8890 0.0386  0.1746  0.0378  467 ALA A CB  
3597 N N   . ALA A 468 ? 0.7020 0.3917 1.0169 0.0705  0.1729  0.0477  468 ALA A N   
3598 C CA  . ALA A 468 ? 0.7096 0.4178 1.0629 0.0751  0.1805  0.0341  468 ALA A CA  
3599 C C   . ALA A 468 ? 0.7140 0.4268 1.1051 0.0959  0.1708  0.0561  468 ALA A C   
3600 O O   . ALA A 468 ? 0.7654 0.4634 1.1547 0.1056  0.1635  0.0775  468 ALA A O   
3601 C CB  . ALA A 468 ? 0.6866 0.4109 1.0247 0.0676  0.1742  0.0262  468 ALA A CB  
3602 N N   . GLU A 469 ? 0.7506 0.4861 1.1775 0.1033  0.1705  0.0513  469 GLU A N   
3603 C CA  . GLU A 469 ? 0.8008 0.5474 1.2714 0.1233  0.1617  0.0693  469 GLU A CA  
3604 C C   . GLU A 469 ? 0.8445 0.6041 1.3080 0.1347  0.1317  0.0983  469 GLU A C   
3605 O O   . GLU A 469 ? 0.8704 0.6456 1.3698 0.1517  0.1196  0.1149  469 GLU A O   
3606 C CB  . GLU A 469 ? 0.7426 0.5125 1.2623 0.1256  0.1779  0.0477  469 GLU A CB  
3607 C CG  . GLU A 469 ? 0.7350 0.5342 1.2639 0.1234  0.1718  0.0409  469 GLU A CG  
3608 C CD  . GLU A 469 ? 0.7002 0.5037 1.1947 0.1007  0.1865  0.0124  469 GLU A CD  
3609 O OE1 . GLU A 469 ? 0.6651 0.4462 1.1163 0.0885  0.1892  0.0079  469 GLU A OE1 
3610 O OE2 . GLU A 469 ? 0.6437 0.4768 1.1521 0.0937  0.1944  -0.0046 469 GLU A OE2 
3611 N N   . HIS A 470 ? 0.9287 0.6836 1.3468 0.1254  0.1185  0.1049  470 HIS A N   
3612 C CA  . HIS A 470 ? 0.9813 0.7576 1.3837 0.1300  0.0881  0.1267  470 HIS A CA  
3613 C C   . HIS A 470 ? 1.0606 0.8187 1.4489 0.1439  0.0717  0.1590  470 HIS A C   
3614 O O   . HIS A 470 ? 1.0210 0.7524 1.3700 0.1370  0.0774  0.1620  470 HIS A O   
3615 C CB  . HIS A 470 ? 0.9713 0.7581 1.3195 0.1089  0.0793  0.1158  470 HIS A CB  
3616 C CG  . HIS A 470 ? 0.9059 0.7116 1.2589 0.0937  0.0940  0.0870  470 HIS A CG  
3617 N ND1 . HIS A 470 ? 0.9356 0.7752 1.3227 0.0946  0.0918  0.0793  470 HIS A ND1 
3618 C CD2 . HIS A 470 ? 0.8969 0.6937 1.2242 0.0771  0.1110  0.0650  470 HIS A CD2 
3619 C CE1 . HIS A 470 ? 0.8717 0.7202 1.2507 0.0790  0.1082  0.0550  470 HIS A CE1 
3620 N NE2 . HIS A 470 ? 0.8522 0.6759 1.1942 0.0686  0.1187  0.0463  470 HIS A NE2 
3621 N N   . LYS A 471 ? 1.1121 0.8920 1.5261 0.1603  0.0499  0.1804  471 LYS A N   
3622 C CA  . LYS A 471 ? 1.1560 0.9293 1.5494 0.1722  0.0298  0.2105  471 LYS A CA  
3623 C C   . LYS A 471 ? 1.2267 1.0207 1.5924 0.1719  -0.0019 0.2288  471 LYS A C   
3624 O O   . LYS A 471 ? 1.1773 0.9986 1.5328 0.1573  -0.0087 0.2104  471 LYS A O   
3625 C CB  . LYS A 471 ? 1.1160 0.9003 1.5596 0.1918  0.0275  0.2215  471 LYS A CB  
3626 C CG  . LYS A 471 ? 1.1265 0.8960 1.6069 0.1919  0.0584  0.2009  471 LYS A CG  
3627 C CD  . LYS A 471 ? 1.1405 0.8703 1.5880 0.1845  0.0753  0.1999  471 LYS A CD  
3628 C CE  . LYS A 471 ? 1.1125 0.8296 1.5999 0.1853  0.1033  0.1814  471 LYS A CE  
3629 N NZ  . LYS A 471 ? 1.1934 0.9184 1.7285 0.2063  0.0983  0.1971  471 LYS A NZ  
3630 N N   . GLY A 472 ? 1.2760 1.0649 1.6111 0.1802  -0.0213 0.2551  472 GLY A N   
3631 C CA  . GLY A 472 ? 1.3199 1.1341 1.6309 0.1817  -0.0548 0.2737  472 GLY A CA  
3632 C C   . GLY A 472 ? 1.3029 1.1030 1.5406 0.1645  -0.0603 0.2727  472 GLY A C   
3633 O O   . GLY A 472 ? 1.3204 1.1386 1.5255 0.1640  -0.0874 0.2864  472 GLY A O   
3634 N N   . LYS A 473 ? 1.3199 1.0911 1.5318 0.1500  -0.0355 0.2551  473 LYS A N   
3635 C CA  . LYS A 473 ? 1.2785 1.0366 1.4258 0.1331  -0.0363 0.2500  473 LYS A CA  
3636 C C   . LYS A 473 ? 1.2668 1.0564 1.3924 0.1183  -0.0539 0.2331  473 LYS A C   
3637 O O   . LYS A 473 ? 1.2852 1.0691 1.3584 0.1065  -0.0599 0.2308  473 LYS A O   
3638 C CB  . LYS A 473 ? 1.3300 1.0681 1.4364 0.1410  -0.0466 0.2808  473 LYS A CB  
3639 C CG  . LYS A 473 ? 1.3575 1.0588 1.4229 0.1297  -0.0241 0.2754  473 LYS A CG  
3640 C CD  . LYS A 473 ? 1.3950 1.0814 1.4153 0.1341  -0.0331 0.2989  473 LYS A CD  
3641 C CE  . LYS A 473 ? 1.4458 1.1006 1.4304 0.1203  -0.0112 0.2914  473 LYS A CE  
3642 N NZ  . LYS A 473 ? 1.4728 1.1085 1.4928 0.1189  0.0141  0.2782  473 LYS A NZ  
3643 N N   . VAL A 474 ? 1.0746 0.8961 1.2420 0.1182  -0.0599 0.2202  474 VAL A N   
3644 C CA  . VAL A 474 ? 0.9210 0.7711 1.0751 0.1034  -0.0746 0.2039  474 VAL A CA  
3645 C C   . VAL A 474 ? 0.8071 0.6412 0.9277 0.0841  -0.0574 0.1809  474 VAL A C   
3646 O O   . VAL A 474 ? 0.8131 0.6219 0.9318 0.0819  -0.0337 0.1737  474 VAL A O   
3647 C CB  . VAL A 474 ? 0.8916 0.7771 1.1048 0.1072  -0.0789 0.1950  474 VAL A CB  
3648 C CG1 . VAL A 474 ? 0.7593 0.6492 0.9842 0.0914  -0.0590 0.1667  474 VAL A CG1 
3649 C CG2 . VAL A 474 ? 0.8586 0.7806 1.0743 0.1076  -0.1109 0.2024  474 VAL A CG2 
3650 N N   . ILE A 475 ? 0.7766 0.6260 0.8719 0.0700  -0.0700 0.1694  475 ILE A N   
3651 C CA  . ILE A 475 ? 0.7254 0.5608 0.7885 0.0533  -0.0569 0.1505  475 ILE A CA  
3652 C C   . ILE A 475 ? 0.6624 0.5138 0.7566 0.0443  -0.0462 0.1305  475 ILE A C   
3653 O O   . ILE A 475 ? 0.6596 0.5378 0.7714 0.0391  -0.0589 0.1248  475 ILE A O   
3654 C CB  . ILE A 475 ? 0.6987 0.5354 0.7142 0.0433  -0.0734 0.1490  475 ILE A CB  
3655 C CG1 . ILE A 475 ? 0.7328 0.5484 0.7087 0.0501  -0.0768 0.1673  475 ILE A CG1 
3656 C CG2 . ILE A 475 ? 0.6330 0.4597 0.6266 0.0273  -0.0609 0.1287  475 ILE A CG2 
3657 C CD1 . ILE A 475 ? 0.8396 0.6542 0.7648 0.0403  -0.0899 0.1643  475 ILE A CD1 
3658 N N   . MET A 476 ? 0.6469 0.4825 0.7456 0.0409  -0.0227 0.1196  476 MET A N   
3659 C CA  . MET A 476 ? 0.5807 0.4286 0.7060 0.0335  -0.0083 0.1023  476 MET A CA  
3660 C C   . MET A 476 ? 0.5323 0.3697 0.6249 0.0186  0.0008  0.0884  476 MET A C   
3661 O O   . MET A 476 ? 0.5397 0.3561 0.5970 0.0162  0.0033  0.0900  476 MET A O   
3662 C CB  . MET A 476 ? 0.5725 0.4125 0.7306 0.0418  0.0124  0.0992  476 MET A CB  
3663 C CG  . MET A 476 ? 0.6654 0.5155 0.8664 0.0586  0.0072  0.1120  476 MET A CG  
3664 S SD  . MET A 476 ? 0.8233 0.6577 1.0616 0.0666  0.0361  0.1035  476 MET A SD  
3665 C CE  . MET A 476 ? 0.7451 0.6043 1.0049 0.0536  0.0512  0.0784  476 MET A CE  
3666 N N   . HIS A 477 ? 0.4916 0.3443 0.5982 0.0090  0.0071  0.0757  477 HIS A N   
3667 C CA  . HIS A 477 ? 0.4863 0.3301 0.5667 -0.0033 0.0169  0.0646  477 HIS A CA  
3668 C C   . HIS A 477 ? 0.4924 0.3246 0.5745 -0.0027 0.0375  0.0568  477 HIS A C   
3669 O O   . HIS A 477 ? 0.5287 0.3681 0.6421 0.0022  0.0488  0.0527  477 HIS A O   
3670 C CB  . HIS A 477 ? 0.5106 0.3735 0.6037 -0.0141 0.0170  0.0565  477 HIS A CB  
3671 C CG  . HIS A 477 ? 0.5127 0.3843 0.5995 -0.0193 -0.0021 0.0598  477 HIS A CG  
3672 N ND1 . HIS A 477 ? 0.4918 0.3519 0.5471 -0.0290 -0.0067 0.0564  477 HIS A ND1 
3673 C CD2 . HIS A 477 ? 0.5014 0.3928 0.6110 -0.0165 -0.0183 0.0648  477 HIS A CD2 
3674 C CE1 . HIS A 477 ? 0.5400 0.4105 0.5976 -0.0333 -0.0235 0.0573  477 HIS A CE1 
3675 N NE2 . HIS A 477 ? 0.5261 0.4175 0.6157 -0.0263 -0.0320 0.0623  477 HIS A NE2 
3676 N N   . ASP A 478 ? 0.4606 0.2763 0.5113 -0.0078 0.0426  0.0533  478 ASP A N   
3677 C CA  . ASP A 478 ? 0.4811 0.2889 0.5315 -0.0099 0.0605  0.0434  478 ASP A CA  
3678 C C   . ASP A 478 ? 0.4866 0.2904 0.5073 -0.0195 0.0624  0.0371  478 ASP A C   
3679 O O   . ASP A 478 ? 0.4794 0.2688 0.4802 -0.0196 0.0642  0.0376  478 ASP A O   
3680 C CB  . ASP A 478 ? 0.5086 0.2976 0.5615 -0.0014 0.0659  0.0490  478 ASP A CB  
3681 C CG  . ASP A 478 ? 0.4945 0.2790 0.5626 -0.0031 0.0856  0.0359  478 ASP A CG  
3682 O OD1 . ASP A 478 ? 0.5102 0.3049 0.5739 -0.0123 0.0940  0.0219  478 ASP A OD1 
3683 O OD2 . ASP A 478 ? 0.4572 0.2275 0.5404 0.0044  0.0927  0.0397  478 ASP A OD2 
3684 N N   . PRO A 479 ? 0.4546 0.2715 0.4736 -0.0274 0.0626  0.0322  479 PRO A N   
3685 C CA  . PRO A 479 ? 0.4575 0.2709 0.4502 -0.0346 0.0622  0.0297  479 PRO A CA  
3686 C C   . PRO A 479 ? 0.4635 0.2737 0.4487 -0.0364 0.0737  0.0211  479 PRO A C   
3687 O O   . PRO A 479 ? 0.4494 0.2678 0.4488 -0.0380 0.0853  0.0120  479 PRO A O   
3688 C CB  . PRO A 479 ? 0.4516 0.2799 0.4495 -0.0423 0.0633  0.0281  479 PRO A CB  
3689 C CG  . PRO A 479 ? 0.4714 0.3137 0.4998 -0.0403 0.0672  0.0264  479 PRO A CG  
3690 C CD  . PRO A 479 ? 0.4987 0.3344 0.5420 -0.0297 0.0634  0.0306  479 PRO A CD  
3691 N N   . PHE A 480 ? 0.4966 0.2965 0.4611 -0.0368 0.0707  0.0225  480 PHE A N   
3692 C CA  . PHE A 480 ? 0.4694 0.2690 0.4273 -0.0395 0.0790  0.0142  480 PHE A CA  
3693 C C   . PHE A 480 ? 0.4890 0.2823 0.4629 -0.0371 0.0897  0.0081  480 PHE A C   
3694 O O   . PHE A 480 ? 0.5155 0.3125 0.4909 -0.0418 0.0989  -0.0033 480 PHE A O   
3695 C CB  . PHE A 480 ? 0.4699 0.2862 0.4229 -0.0467 0.0829  0.0071  480 PHE A CB  
3696 C CG  . PHE A 480 ? 0.5183 0.3362 0.4543 -0.0486 0.0741  0.0145  480 PHE A CG  
3697 C CD1 . PHE A 480 ? 0.4892 0.3071 0.4266 -0.0496 0.0682  0.0221  480 PHE A CD1 
3698 C CD2 . PHE A 480 ? 0.5104 0.3302 0.4329 -0.0495 0.0720  0.0138  480 PHE A CD2 
3699 C CE1 . PHE A 480 ? 0.4853 0.3005 0.4097 -0.0516 0.0620  0.0291  480 PHE A CE1 
3700 C CE2 . PHE A 480 ? 0.5350 0.3539 0.4455 -0.0495 0.0647  0.0221  480 PHE A CE2 
3701 C CZ  . PHE A 480 ? 0.5047 0.3192 0.4157 -0.0507 0.0604  0.0298  480 PHE A CZ  
3702 N N   . ALA A 481 ? 0.4356 0.2198 0.4231 -0.0300 0.0884  0.0155  481 ALA A N   
3703 C CA  . ALA A 481 ? 0.4834 0.2585 0.4919 -0.0259 0.0995  0.0123  481 ALA A CA  
3704 C C   . ALA A 481 ? 0.4967 0.2842 0.5251 -0.0299 0.1122  -0.0029 481 ALA A C   
3705 O O   . ALA A 481 ? 0.4695 0.2489 0.5150 -0.0295 0.1253  -0.0119 481 ALA A O   
3706 C CB  . ALA A 481 ? 0.5149 0.2749 0.5158 -0.0274 0.1064  0.0104  481 ALA A CB  
3707 N N   . MET A 482 ? 0.4856 0.2913 0.5123 -0.0343 0.1102  -0.0064 482 MET A N   
3708 C CA  . MET A 482 ? 0.4776 0.2981 0.5144 -0.0406 0.1233  -0.0225 482 MET A CA  
3709 C C   . MET A 482 ? 0.4953 0.3265 0.5571 -0.0371 0.1273  -0.0224 482 MET A C   
3710 O O   . MET A 482 ? 0.5055 0.3512 0.5740 -0.0430 0.1396  -0.0360 482 MET A O   
3711 C CB  . MET A 482 ? 0.5002 0.3359 0.5111 -0.0504 0.1206  -0.0269 482 MET A CB  
3712 C CG  . MET A 482 ? 0.4659 0.2997 0.4599 -0.0554 0.1207  -0.0338 482 MET A CG  
3713 S SD  . MET A 482 ? 0.4942 0.3358 0.4994 -0.0633 0.1384  -0.0587 482 MET A SD  
3714 C CE  . MET A 482 ? 0.5030 0.3715 0.4928 -0.0719 0.1410  -0.0652 482 MET A CE  
3715 N N   . ARG A 483 ? 0.4751 0.3023 0.5517 -0.0280 0.1176  -0.0084 483 ARG A N   
3716 C CA  . ARG A 483 ? 0.4914 0.3335 0.5974 -0.0246 0.1206  -0.0084 483 ARG A CA  
3717 C C   . ARG A 483 ? 0.5133 0.3593 0.6476 -0.0233 0.1406  -0.0246 483 ARG A C   
3718 O O   . ARG A 483 ? 0.5109 0.3757 0.6560 -0.0283 0.1504  -0.0340 483 ARG A O   
3719 C CB  . ARG A 483 ? 0.5278 0.3665 0.6505 -0.0134 0.1060  0.0083  483 ARG A CB  
3720 C CG  . ARG A 483 ? 0.5085 0.3693 0.6625 -0.0116 0.1052  0.0091  483 ARG A CG  
3721 C CD  . ARG A 483 ? 0.5467 0.4086 0.7306 0.0023  0.0943  0.0223  483 ARG A CD  
3722 N NE  . ARG A 483 ? 0.5518 0.3972 0.7549 0.0134  0.1039  0.0224  483 ARG A NE  
3723 C CZ  . ARG A 483 ? 0.6012 0.4255 0.7935 0.0214  0.0960  0.0356  483 ARG A CZ  
3724 N NH1 . ARG A 483 ? 0.6096 0.4288 0.7715 0.0202  0.0778  0.0487  483 ARG A NH1 
3725 N NH2 . ARG A 483 ? 0.5920 0.3987 0.8044 0.0302  0.1082  0.0353  483 ARG A NH2 
3726 N N   . PRO A 484 ? 0.4839 0.3122 0.6316 -0.0176 0.1496  -0.0295 484 PRO A N   
3727 C CA  . PRO A 484 ? 0.4954 0.3254 0.6731 -0.0166 0.1708  -0.0477 484 PRO A CA  
3728 C C   . PRO A 484 ? 0.4674 0.3057 0.6265 -0.0309 0.1854  -0.0709 484 PRO A C   
3729 O O   . PRO A 484 ? 0.4873 0.3271 0.6679 -0.0322 0.2048  -0.0904 484 PRO A O   
3730 C CB  . PRO A 484 ? 0.5037 0.3067 0.7007 -0.0061 0.1745  -0.0426 484 PRO A CB  
3731 C CG  . PRO A 484 ? 0.5065 0.2963 0.6789 -0.0021 0.1545  -0.0201 484 PRO A CG  
3732 C CD  . PRO A 484 ? 0.5007 0.3050 0.6374 -0.0129 0.1435  -0.0196 484 PRO A CD  
3733 N N   . PHE A 485 ? 0.4681 0.3127 0.5887 -0.0411 0.1764  -0.0698 485 PHE A N   
3734 C CA  . PHE A 485 ? 0.5148 0.3662 0.6138 -0.0538 0.1856  -0.0893 485 PHE A CA  
3735 C C   . PHE A 485 ? 0.4951 0.3697 0.5630 -0.0646 0.1818  -0.0905 485 PHE A C   
3736 O O   . PHE A 485 ? 0.5093 0.3935 0.5548 -0.0752 0.1860  -0.1047 485 PHE A O   
3737 C CB  . PHE A 485 ? 0.4477 0.2830 0.5315 -0.0555 0.1789  -0.0874 485 PHE A CB  
3738 C CG  . PHE A 485 ? 0.4568 0.2661 0.5671 -0.0461 0.1841  -0.0839 485 PHE A CG  
3739 C CD1 . PHE A 485 ? 0.4603 0.2613 0.6015 -0.0447 0.2032  -0.1007 485 PHE A CD1 
3740 C CD2 . PHE A 485 ? 0.5144 0.3065 0.6184 -0.0389 0.1713  -0.0636 485 PHE A CD2 
3741 C CE1 . PHE A 485 ? 0.5134 0.2870 0.6814 -0.0353 0.2095  -0.0951 485 PHE A CE1 
3742 C CE2 . PHE A 485 ? 0.4624 0.2290 0.5884 -0.0304 0.1773  -0.0574 485 PHE A CE2 
3743 C CZ  . PHE A 485 ? 0.5077 0.2641 0.6669 -0.0282 0.1961  -0.0719 485 PHE A CZ  
3744 N N   . PHE A 486 ? 0.4411 0.3253 0.5072 -0.0629 0.1741  -0.0758 486 PHE A N   
3745 C CA  . PHE A 486 ? 0.5064 0.4089 0.5425 -0.0732 0.1718  -0.0739 486 PHE A CA  
3746 C C   . PHE A 486 ? 0.4458 0.3666 0.4804 -0.0823 0.1915  -0.0946 486 PHE A C   
3747 O O   . PHE A 486 ? 0.4797 0.4049 0.5441 -0.0794 0.2061  -0.1036 486 PHE A O   
3748 C CB  . PHE A 486 ? 0.4996 0.4064 0.5382 -0.0711 0.1621  -0.0549 486 PHE A CB  
3749 C CG  . PHE A 486 ? 0.4159 0.3074 0.4456 -0.0653 0.1424  -0.0368 486 PHE A CG  
3750 C CD1 . PHE A 486 ? 0.4699 0.3565 0.4692 -0.0685 0.1326  -0.0319 486 PHE A CD1 
3751 C CD2 . PHE A 486 ? 0.4483 0.3321 0.5006 -0.0565 0.1337  -0.0255 486 PHE A CD2 
3752 C CE1 . PHE A 486 ? 0.4842 0.3562 0.4759 -0.0632 0.1171  -0.0177 486 PHE A CE1 
3753 C CE2 . PHE A 486 ? 0.4648 0.3349 0.5050 -0.0524 0.1167  -0.0114 486 PHE A CE2 
3754 C CZ  . PHE A 486 ? 0.4721 0.3351 0.4822 -0.0558 0.1098  -0.0083 486 PHE A CZ  
3755 N N   . GLY A 487 ? 0.4690 0.4019 0.4696 -0.0931 0.1921  -0.1029 487 GLY A N   
3756 C CA  . GLY A 487 ? 0.4808 0.4343 0.4702 -0.1038 0.2098  -0.1219 487 GLY A CA  
3757 C C   . GLY A 487 ? 0.5583 0.5288 0.5319 -0.1097 0.2129  -0.1108 487 GLY A C   
3758 O O   . GLY A 487 ? 0.5280 0.5164 0.4919 -0.1188 0.2303  -0.1258 487 GLY A O   
3759 N N   . TYR A 488 ? 0.5156 0.4802 0.4856 -0.1057 0.1979  -0.0858 488 TYR A N   
3760 C CA  . TYR A 488 ? 0.5377 0.5150 0.4912 -0.1127 0.2003  -0.0725 488 TYR A CA  
3761 C C   . TYR A 488 ? 0.5139 0.4785 0.4815 -0.1064 0.1856  -0.0494 488 TYR A C   
3762 O O   . TYR A 488 ? 0.4817 0.4297 0.4661 -0.0968 0.1728  -0.0441 488 TYR A O   
3763 C CB  . TYR A 488 ? 0.5488 0.5379 0.4545 -0.1221 0.1957  -0.0685 488 TYR A CB  
3764 C CG  . TYR A 488 ? 0.5421 0.5192 0.4299 -0.1172 0.1731  -0.0532 488 TYR A CG  
3765 C CD1 . TYR A 488 ? 0.5103 0.4805 0.4010 -0.1132 0.1657  -0.0640 488 TYR A CD1 
3766 C CD2 . TYR A 488 ? 0.5486 0.5207 0.4199 -0.1168 0.1610  -0.0285 488 TYR A CD2 
3767 C CE1 . TYR A 488 ? 0.5326 0.4942 0.4105 -0.1085 0.1470  -0.0510 488 TYR A CE1 
3768 C CE2 . TYR A 488 ? 0.5202 0.4814 0.3790 -0.1111 0.1422  -0.0156 488 TYR A CE2 
3769 C CZ  . TYR A 488 ? 0.5455 0.5031 0.4079 -0.1068 0.1353  -0.0271 488 TYR A CZ  
3770 O OH  . TYR A 488 ? 0.5423 0.4914 0.3955 -0.1010 0.1185  -0.0152 488 TYR A OH  
3771 N N   . ASN A 489 ? 0.5007 0.4732 0.4593 -0.1132 0.1884  -0.0361 489 ASN A N   
3772 C CA  . ASN A 489 ? 0.5285 0.4918 0.5017 -0.1110 0.1777  -0.0171 489 ASN A CA  
3773 C C   . ASN A 489 ? 0.5145 0.4570 0.4791 -0.1034 0.1557  -0.0051 489 ASN A C   
3774 O O   . ASN A 489 ? 0.5071 0.4449 0.4404 -0.1046 0.1473  0.0019  489 ASN A O   
3775 C CB  . ASN A 489 ? 0.5118 0.4841 0.4643 -0.1225 0.1848  -0.0039 489 ASN A CB  
3776 C CG  . ASN A 489 ? 0.5476 0.5123 0.5204 -0.1239 0.1785  0.0123  489 ASN A CG  
3777 O OD1 . ASN A 489 ? 0.5432 0.4903 0.5186 -0.1182 0.1607  0.0223  489 ASN A OD1 
3778 N ND2 . ASN A 489 ? 0.5228 0.5019 0.5098 -0.1331 0.1945  0.0135  489 ASN A ND2 
3779 N N   . PHE A 490 ? 0.4914 0.4232 0.4844 -0.0951 0.1465  -0.0030 490 PHE A N   
3780 C CA  . PHE A 490 ? 0.4755 0.3876 0.4611 -0.0877 0.1280  0.0057  490 PHE A CA  
3781 C C   . PHE A 490 ? 0.4990 0.4019 0.4648 -0.0917 0.1179  0.0223  490 PHE A C   
3782 O O   . PHE A 490 ? 0.4722 0.3614 0.4205 -0.0875 0.1063  0.0281  490 PHE A O   
3783 C CB  . PHE A 490 ? 0.4919 0.3975 0.5091 -0.0791 0.1208  0.0056  490 PHE A CB  
3784 C CG  . PHE A 490 ? 0.4823 0.3689 0.4907 -0.0732 0.1028  0.0151  490 PHE A CG  
3785 C CD1 . PHE A 490 ? 0.4580 0.3325 0.4453 -0.0693 0.0977  0.0141  490 PHE A CD1 
3786 C CD2 . PHE A 490 ? 0.4994 0.3822 0.5218 -0.0724 0.0919  0.0231  490 PHE A CD2 
3787 C CE1 . PHE A 490 ? 0.4929 0.3506 0.4719 -0.0641 0.0839  0.0214  490 PHE A CE1 
3788 C CE2 . PHE A 490 ? 0.5070 0.3728 0.5184 -0.0678 0.0768  0.0292  490 PHE A CE2 
3789 C CZ  . PHE A 490 ? 0.4861 0.3386 0.4750 -0.0633 0.0739  0.0286  490 PHE A CZ  
3790 N N   . GLY A 491 ? 0.5199 0.4290 0.4911 -0.0998 0.1237  0.0299  491 GLY A N   
3791 C CA  . GLY A 491 ? 0.5234 0.4205 0.4768 -0.1042 0.1169  0.0461  491 GLY A CA  
3792 C C   . GLY A 491 ? 0.5439 0.4413 0.4619 -0.1054 0.1171  0.0524  491 GLY A C   
3793 O O   . GLY A 491 ? 0.5465 0.4289 0.4490 -0.1018 0.1059  0.0635  491 GLY A O   
3794 N N   . LYS A 492 ? 0.5320 0.4480 0.4373 -0.1101 0.1297  0.0445  492 LYS A N   
3795 C CA  . LYS A 492 ? 0.5408 0.4630 0.4111 -0.1111 0.1276  0.0488  492 LYS A CA  
3796 C C   . LYS A 492 ? 0.5312 0.4480 0.3967 -0.1022 0.1152  0.0416  492 LYS A C   
3797 O O   . LYS A 492 ? 0.5299 0.4460 0.3733 -0.0997 0.1058  0.0503  492 LYS A O   
3798 C CB  . LYS A 492 ? 0.5252 0.4711 0.3815 -0.1197 0.1443  0.0380  492 LYS A CB  
3799 C CG  . LYS A 492 ? 0.5640 0.5182 0.4219 -0.1303 0.1603  0.0457  492 LYS A CG  
3800 C CD  . LYS A 492 ? 0.5876 0.5254 0.4376 -0.1324 0.1534  0.0711  492 LYS A CD  
3801 C CE  . LYS A 492 ? 0.7272 0.6720 0.5809 -0.1447 0.1711  0.0799  492 LYS A CE  
3802 N NZ  . LYS A 492 ? 0.7791 0.7021 0.6469 -0.1464 0.1649  0.0984  492 LYS A NZ  
3803 N N   . TYR A 493 ? 0.4747 0.3882 0.3627 -0.0971 0.1155  0.0270  493 TYR A N   
3804 C CA  . TYR A 493 ? 0.5311 0.4380 0.4173 -0.0899 0.1061  0.0203  493 TYR A CA  
3805 C C   . TYR A 493 ? 0.5004 0.3883 0.3840 -0.0833 0.0915  0.0344  493 TYR A C   
3806 O O   . TYR A 493 ? 0.5259 0.4129 0.3970 -0.0793 0.0833  0.0363  493 TYR A O   
3807 C CB  . TYR A 493 ? 0.4894 0.3938 0.4015 -0.0862 0.1119  0.0045  493 TYR A CB  
3808 C CG  . TYR A 493 ? 0.4969 0.3890 0.4143 -0.0788 0.1044  -0.0005 493 TYR A CG  
3809 C CD1 . TYR A 493 ? 0.4743 0.3481 0.3982 -0.0718 0.0936  0.0090  493 TYR A CD1 
3810 C CD2 . TYR A 493 ? 0.4815 0.3803 0.3987 -0.0801 0.1102  -0.0167 493 TYR A CD2 
3811 C CE1 . TYR A 493 ? 0.4561 0.3188 0.3833 -0.0660 0.0894  0.0051  493 TYR A CE1 
3812 C CE2 . TYR A 493 ? 0.4697 0.3565 0.3943 -0.0748 0.1058  -0.0207 493 TYR A CE2 
3813 C CZ  . TYR A 493 ? 0.5106 0.3794 0.4392 -0.0675 0.0959  -0.0087 493 TYR A CZ  
3814 O OH  . TYR A 493 ? 0.4589 0.3157 0.3926 -0.0629 0.0938  -0.0117 493 TYR A OH  
3815 N N   . LEU A 494 ? 0.5325 0.4068 0.4295 -0.0825 0.0885  0.0427  494 LEU A N   
3816 C CA  . LEU A 494 ? 0.5102 0.3650 0.4040 -0.0777 0.0768  0.0540  494 LEU A CA  
3817 C C   . LEU A 494 ? 0.5366 0.3904 0.4099 -0.0784 0.0735  0.0685  494 LEU A C   
3818 O O   . LEU A 494 ? 0.5231 0.3674 0.3900 -0.0715 0.0646  0.0736  494 LEU A O   
3819 C CB  . LEU A 494 ? 0.4976 0.3414 0.4090 -0.0800 0.0752  0.0579  494 LEU A CB  
3820 C CG  . LEU A 494 ? 0.5178 0.3620 0.4504 -0.0767 0.0741  0.0475  494 LEU A CG  
3821 C CD1 . LEU A 494 ? 0.5221 0.3627 0.4732 -0.0809 0.0711  0.0508  494 LEU A CD1 
3822 C CD2 . LEU A 494 ? 0.4558 0.2873 0.3830 -0.0683 0.0657  0.0444  494 LEU A CD2 
3823 N N   . ALA A 495 ? 0.5368 0.4004 0.4003 -0.0860 0.0811  0.0766  495 ALA A N   
3824 C CA  . ALA A 495 ? 0.5693 0.4311 0.4120 -0.0858 0.0776  0.0945  495 ALA A CA  
3825 C C   . ALA A 495 ? 0.5979 0.4757 0.4226 -0.0811 0.0715  0.0920  495 ALA A C   
3826 O O   . ALA A 495 ? 0.6099 0.4830 0.4251 -0.0747 0.0620  0.1054  495 ALA A O   
3827 C CB  . ALA A 495 ? 0.5904 0.4597 0.4239 -0.0962 0.0891  0.1050  495 ALA A CB  
3828 N N   . HIS A 496 ? 0.5592 0.4560 0.3828 -0.0841 0.0765  0.0739  496 HIS A N   
3829 C CA  . HIS A 496 ? 0.5715 0.4860 0.3826 -0.0816 0.0701  0.0667  496 HIS A CA  
3830 C C   . HIS A 496 ? 0.5670 0.4695 0.3903 -0.0715 0.0590  0.0658  496 HIS A C   
3831 O O   . HIS A 496 ? 0.5624 0.4717 0.3775 -0.0659 0.0489  0.0739  496 HIS A O   
3832 C CB  . HIS A 496 ? 0.5394 0.4715 0.3529 -0.0883 0.0804  0.0436  496 HIS A CB  
3833 C CG  . HIS A 496 ? 0.6088 0.5632 0.4090 -0.0899 0.0758  0.0321  496 HIS A CG  
3834 N ND1 . HIS A 496 ? 0.5802 0.5549 0.3531 -0.0923 0.0690  0.0417  496 HIS A ND1 
3835 C CD2 . HIS A 496 ? 0.5267 0.4878 0.3382 -0.0906 0.0769  0.0113  496 HIS A CD2 
3836 C CE1 . HIS A 496 ? 0.5893 0.5852 0.3578 -0.0947 0.0646  0.0254  496 HIS A CE1 
3837 N NE2 . HIS A 496 ? 0.5488 0.5356 0.3416 -0.0944 0.0704  0.0061  496 HIS A NE2 
3838 N N   . TRP A 497 ? 0.5108 0.3967 0.3541 -0.0687 0.0610  0.0571  497 TRP A N   
3839 C CA  . TRP A 497 ? 0.5380 0.4109 0.3912 -0.0600 0.0533  0.0563  497 TRP A CA  
3840 C C   . TRP A 497 ? 0.5803 0.4388 0.4305 -0.0535 0.0454  0.0741  497 TRP A C   
3841 O O   . TRP A 497 ? 0.5578 0.4180 0.4092 -0.0460 0.0382  0.0769  497 TRP A O   
3842 C CB  . TRP A 497 ? 0.4934 0.3497 0.3632 -0.0587 0.0568  0.0475  497 TRP A CB  
3843 C CG  . TRP A 497 ? 0.5157 0.3797 0.3938 -0.0597 0.0619  0.0307  497 TRP A CG  
3844 C CD1 . TRP A 497 ? 0.5041 0.3788 0.3870 -0.0655 0.0713  0.0188  497 TRP A CD1 
3845 C CD2 . TRP A 497 ? 0.4891 0.3487 0.3737 -0.0551 0.0600  0.0238  497 TRP A CD2 
3846 N NE1 . TRP A 497 ? 0.4877 0.3623 0.3806 -0.0648 0.0750  0.0053  497 TRP A NE1 
3847 C CE2 . TRP A 497 ? 0.5135 0.3795 0.4070 -0.0590 0.0683  0.0089  497 TRP A CE2 
3848 C CE3 . TRP A 497 ? 0.5156 0.3658 0.4014 -0.0484 0.0540  0.0284  497 TRP A CE3 
3849 C CZ2 . TRP A 497 ? 0.5495 0.4117 0.4521 -0.0574 0.0706  0.0000  497 TRP A CZ2 
3850 C CZ3 . TRP A 497 ? 0.5560 0.4054 0.4501 -0.0467 0.0567  0.0188  497 TRP A CZ3 
3851 C CH2 . TRP A 497 ? 0.5429 0.3979 0.4450 -0.0517 0.0648  0.0056  497 TRP A CH2 
3852 N N   . LEU A 498 ? 0.5591 0.4028 0.4091 -0.0563 0.0478  0.0854  498 LEU A N   
3853 C CA  . LEU A 498 ? 0.6032 0.4277 0.4539 -0.0504 0.0424  0.1012  498 LEU A CA  
3854 C C   . LEU A 498 ? 0.6473 0.4840 0.4844 -0.0460 0.0365  0.1166  498 LEU A C   
3855 O O   . LEU A 498 ? 0.6562 0.4825 0.4984 -0.0363 0.0298  0.1265  498 LEU A O   
3856 C CB  . LEU A 498 ? 0.6222 0.4286 0.4776 -0.0569 0.0474  0.1090  498 LEU A CB  
3857 C CG  . LEU A 498 ? 0.5771 0.3702 0.4479 -0.0597 0.0491  0.0967  498 LEU A CG  
3858 C CD1 . LEU A 498 ? 0.5838 0.3717 0.4613 -0.0697 0.0552  0.1014  498 LEU A CD1 
3859 C CD2 . LEU A 498 ? 0.5696 0.3405 0.4469 -0.0524 0.0434  0.0946  498 LEU A CD2 
3860 N N   . SER A 499 ? 0.6278 0.4880 0.4481 -0.0524 0.0387  0.1185  499 SER A N   
3861 C CA  . SER A 499 ? 0.6786 0.5542 0.4815 -0.0486 0.0312  0.1354  499 SER A CA  
3862 C C   . SER A 499 ? 0.6943 0.5856 0.5027 -0.0390 0.0197  0.1309  499 SER A C   
3863 O O   . SER A 499 ? 0.7485 0.6494 0.5499 -0.0315 0.0098  0.1479  499 SER A O   
3864 C CB  . SER A 499 ? 0.6483 0.5494 0.4276 -0.0593 0.0367  0.1344  499 SER A CB  
3865 O OG  . SER A 499 ? 0.6707 0.5946 0.4500 -0.0636 0.0380  0.1107  499 SER A OG  
3866 N N   A MET A 500 ? 0.6699 0.5649 0.4926 -0.0390 0.0211  0.1095  500 MET A N   
3867 N N   B MET A 500 ? 0.6764 0.5715 0.4991 -0.0389 0.0210  0.1096  500 MET A N   
3868 C CA  A MET A 500 ? 0.6703 0.5828 0.5023 -0.0319 0.0122  0.1030  500 MET A CA  
3869 C CA  B MET A 500 ? 0.6702 0.5831 0.5020 -0.0317 0.0119  0.1036  500 MET A CA  
3870 C C   A MET A 500 ? 0.6998 0.5979 0.5458 -0.0181 0.0048  0.1176  500 MET A C   
3871 C C   B MET A 500 ? 0.6998 0.5979 0.5457 -0.0179 0.0046  0.1181  500 MET A C   
3872 O O   A MET A 500 ? 0.7293 0.6472 0.5819 -0.0101 -0.0053 0.1212  500 MET A O   
3873 O O   B MET A 500 ? 0.7301 0.6479 0.5824 -0.0099 -0.0055 0.1221  500 MET A O   
3874 C CB  A MET A 500 ? 0.6591 0.5720 0.5055 -0.0355 0.0184  0.0790  500 MET A CB  
3875 C CB  B MET A 500 ? 0.6535 0.5673 0.4995 -0.0353 0.0179  0.0796  500 MET A CB  
3876 C CG  A MET A 500 ? 0.6468 0.5753 0.4849 -0.0477 0.0262  0.0620  500 MET A CG  
3877 C CG  B MET A 500 ? 0.6466 0.5829 0.4838 -0.0466 0.0229  0.0627  500 MET A CG  
3878 S SD  A MET A 500 ? 0.6525 0.6222 0.4707 -0.0541 0.0193  0.0587  500 MET A SD  
3879 S SD  B MET A 500 ? 0.7307 0.6613 0.5881 -0.0495 0.0312  0.0385  500 MET A SD  
3880 C CE  A MET A 500 ? 0.6576 0.6327 0.4683 -0.0685 0.0347  0.0377  500 MET A CE  
3881 C CE  B MET A 500 ? 0.5507 0.4477 0.4133 -0.0493 0.0403  0.0413  500 MET A CE  
3882 N N   . ALA A 501 ? 0.6881 0.5531 0.5412 -0.0151 0.0098  0.1248  501 ALA A N   
3883 C CA  . ALA A 501 ? 0.7619 0.6087 0.6298 -0.0021 0.0055  0.1370  501 ALA A CA  
3884 C C   . ALA A 501 ? 0.8421 0.6919 0.7025 0.0049  -0.0022 0.1636  501 ALA A C   
3885 O O   . ALA A 501 ? 0.8771 0.7129 0.7529 0.0178  -0.0061 0.1757  501 ALA A O   
3886 C CB  . ALA A 501 ? 0.7547 0.5646 0.6312 -0.0032 0.0139  0.1337  501 ALA A CB  
3887 N N   . HIS A 502 ? 0.9132 0.7797 0.7500 -0.0030 -0.0035 0.1734  502 HIS A N   
3888 C CA  . HIS A 502 ? 0.9542 0.8275 0.7780 0.0032  -0.0118 0.2014  502 HIS A CA  
3889 C C   . HIS A 502 ? 0.9864 0.9014 0.8038 0.0086  -0.0265 0.2038  502 HIS A C   
3890 O O   . HIS A 502 ? 1.1444 1.0694 0.9508 0.0161  -0.0367 0.2291  502 HIS A O   
3891 C CB  . HIS A 502 ? 1.0149 0.8845 0.8125 -0.0093 -0.0039 0.2131  502 HIS A CB  
3892 C CG  . HIS A 502 ? 1.0863 0.9213 0.8918 -0.0173 0.0100  0.2095  502 HIS A CG  
3893 N ND1 . HIS A 502 ? 1.1259 0.9609 0.9161 -0.0318 0.0210  0.2090  502 HIS A ND1 
3894 C CD2 . HIS A 502 ? 1.0595 0.8617 0.8878 -0.0136 0.0144  0.2046  502 HIS A CD2 
3895 C CE1 . HIS A 502 ? 1.0985 0.9037 0.9042 -0.0366 0.0301  0.2047  502 HIS A CE1 
3896 N NE2 . HIS A 502 ? 1.1503 0.9349 0.9772 -0.0262 0.0259  0.2015  502 HIS A NE2 
3897 N N   . ARG A 503 ? 0.9456 0.8853 0.7699 0.0045  -0.0283 0.1788  503 ARG A N   
3898 C CA  . ARG A 503 ? 0.9997 0.9831 0.8189 0.0065  -0.0427 0.1771  503 ARG A CA  
3899 C C   . ARG A 503 ? 1.0916 1.0820 0.9376 0.0249  -0.0557 0.1895  503 ARG A C   
3900 O O   . ARG A 503 ? 1.0013 0.9688 0.8754 0.0330  -0.0501 0.1833  503 ARG A O   
3901 C CB  . ARG A 503 ? 0.9929 0.9981 0.8162 -0.0050 -0.0388 0.1449  503 ARG A CB  
3902 C CG  . ARG A 503 ? 0.9734 0.9802 0.7725 -0.0219 -0.0273 0.1317  503 ARG A CG  
3903 C CD  . ARG A 503 ? 1.0217 1.0655 0.8156 -0.0323 -0.0302 0.1076  503 ARG A CD  
3904 N NE  . ARG A 503 ? 1.1342 1.1812 0.9048 -0.0476 -0.0183 0.0949  503 ARG A NE  
3905 C CZ  . ARG A 503 ? 1.1280 1.2033 0.8896 -0.0596 -0.0170 0.0718  503 ARG A CZ  
3906 N NH1 . ARG A 503 ? 1.1132 1.2180 0.8864 -0.0598 -0.0279 0.0585  503 ARG A NH1 
3907 N NH2 . ARG A 503 ? 1.1078 1.1822 0.8508 -0.0723 -0.0034 0.0602  503 ARG A NH2 
3908 N N   . PRO A 504 ? 1.1820 1.2057 1.0202 0.0320  -0.0731 0.2065  504 PRO A N   
3909 C CA  . PRO A 504 ? 1.1729 1.2066 1.0417 0.0517  -0.0865 0.2201  504 PRO A CA  
3910 C C   . PRO A 504 ? 1.1722 1.2297 1.0723 0.0523  -0.0882 0.1931  504 PRO A C   
3911 O O   . PRO A 504 ? 1.1522 1.2413 1.0447 0.0391  -0.0903 0.1712  504 PRO A O   
3912 C CB  . PRO A 504 ? 1.1896 1.2591 1.0365 0.0568  -0.1065 0.2453  504 PRO A CB  
3913 C CG  . PRO A 504 ? 1.2212 1.2908 1.0220 0.0394  -0.1000 0.2475  504 PRO A CG  
3914 C CD  . PRO A 504 ? 1.1869 1.2431 0.9878 0.0226  -0.0818 0.2138  504 PRO A CD  
3915 N N   . ALA A 505 ? 1.0103 1.0512 0.9471 0.0669  -0.0854 0.1940  505 ALA A N   
3916 C CA  . ALA A 505 ? 0.9226 0.9829 0.8939 0.0691  -0.0842 0.1710  505 ALA A CA  
3917 C C   . ALA A 505 ? 0.8216 0.8723 0.7875 0.0514  -0.0679 0.1402  505 ALA A C   
3918 O O   . ALA A 505 ? 0.7762 0.8487 0.7640 0.0477  -0.0663 0.1192  505 ALA A O   
3919 C CB  . ALA A 505 ? 0.8972 1.0151 0.8805 0.0726  -0.1048 0.1712  505 ALA A CB  
3920 N N   . ALA A 506 ? 0.8374 0.8561 0.7770 0.0405  -0.0555 0.1380  506 ALA A N   
3921 C CA  . ALA A 506 ? 0.8033 0.8107 0.7387 0.0257  -0.0407 0.1123  506 ALA A CA  
3922 C C   . ALA A 506 ? 0.7099 0.6950 0.6720 0.0314  -0.0291 0.1005  506 ALA A C   
3923 O O   . ALA A 506 ? 0.6905 0.6424 0.6582 0.0402  -0.0233 0.1100  506 ALA A O   
3924 C CB  . ALA A 506 ? 0.7945 0.7740 0.7010 0.0154  -0.0311 0.1152  506 ALA A CB  
3925 N N   . LYS A 507 ? 0.6752 0.6785 0.6533 0.0253  -0.0247 0.0792  507 LYS A N   
3926 C CA  . LYS A 507 ? 0.6232 0.6069 0.6215 0.0276  -0.0108 0.0663  507 LYS A CA  
3927 C C   . LYS A 507 ? 0.5938 0.5490 0.5724 0.0151  0.0030  0.0548  507 LYS A C   
3928 O O   . LYS A 507 ? 0.5440 0.5091 0.5213 0.0035  0.0088  0.0385  507 LYS A O   
3929 C CB  . LYS A 507 ? 0.6254 0.6427 0.6525 0.0266  -0.0114 0.0509  507 LYS A CB  
3930 C CG  . LYS A 507 ? 0.6639 0.7159 0.7162 0.0400  -0.0272 0.0620  507 LYS A CG  
3931 C CD  . LYS A 507 ? 0.6959 0.7907 0.7756 0.0340  -0.0302 0.0443  507 LYS A CD  
3932 C CE  . LYS A 507 ? 0.6731 0.8101 0.7783 0.0473  -0.0501 0.0564  507 LYS A CE  
3933 N NZ  . LYS A 507 ? 0.7485 0.9326 0.8833 0.0394  -0.0546 0.0373  507 LYS A NZ  
3934 N N   . LEU A 508 ? 0.5921 0.5119 0.5573 0.0176  0.0080  0.0636  508 LEU A N   
3935 C CA  . LEU A 508 ? 0.5738 0.4696 0.5216 0.0070  0.0184  0.0551  508 LEU A CA  
3936 C C   . LEU A 508 ? 0.5767 0.4610 0.5345 0.0052  0.0306  0.0401  508 LEU A C   
3937 O O   . LEU A 508 ? 0.5814 0.4559 0.5526 0.0139  0.0347  0.0399  508 LEU A O   
3938 C CB  . LEU A 508 ? 0.5647 0.4293 0.4991 0.0092  0.0193  0.0675  508 LEU A CB  
3939 C CG  . LEU A 508 ? 0.6083 0.4795 0.5310 0.0104  0.0099  0.0856  508 LEU A CG  
3940 C CD1 . LEU A 508 ? 0.5827 0.4202 0.4997 0.0131  0.0126  0.0976  508 LEU A CD1 
3941 C CD2 . LEU A 508 ? 0.5987 0.4876 0.5035 -0.0021 0.0093  0.0808  508 LEU A CD2 
3942 N N   . PRO A 509 ? 0.5580 0.4419 0.5094 -0.0056 0.0378  0.0281  509 PRO A N   
3943 C CA  . PRO A 509 ? 0.5473 0.4173 0.5041 -0.0075 0.0503  0.0174  509 PRO A CA  
3944 C C   . PRO A 509 ? 0.5644 0.4004 0.5070 -0.0050 0.0555  0.0210  509 PRO A C   
3945 O O   . PRO A 509 ? 0.5388 0.3609 0.4678 -0.0056 0.0508  0.0287  509 PRO A O   
3946 C CB  . PRO A 509 ? 0.5118 0.3890 0.4655 -0.0193 0.0556  0.0068  509 PRO A CB  
3947 C CG  . PRO A 509 ? 0.5489 0.4314 0.4883 -0.0236 0.0481  0.0118  509 PRO A CG  
3948 C CD  . PRO A 509 ? 0.5235 0.4210 0.4641 -0.0162 0.0360  0.0235  509 PRO A CD  
3949 N N   . LYS A 510 ? 0.5393 0.3638 0.4855 -0.0033 0.0657  0.0143  510 LYS A N   
3950 C CA  . LYS A 510 ? 0.5273 0.3224 0.4558 -0.0037 0.0712  0.0140  510 LYS A CA  
3951 C C   . LYS A 510 ? 0.5603 0.3476 0.4736 -0.0123 0.0718  0.0137  510 LYS A C   
3952 O O   . LYS A 510 ? 0.5370 0.3365 0.4556 -0.0181 0.0747  0.0096  510 LYS A O   
3953 C CB  . LYS A 510 ? 0.5187 0.3067 0.4507 -0.0014 0.0839  0.0062  510 LYS A CB  
3954 C CG  . LYS A 510 ? 0.6476 0.4228 0.5833 0.0077  0.0862  0.0056  510 LYS A CG  
3955 C CD  . LYS A 510 ? 0.6178 0.3921 0.5595 0.0093  0.1016  -0.0041 510 LYS A CD  
3956 C CE  . LYS A 510 ? 0.7531 0.5065 0.6898 0.0159  0.1080  -0.0088 510 LYS A CE  
3957 N NZ  . LYS A 510 ? 0.6636 0.4154 0.6165 0.0258  0.0998  -0.0032 510 LYS A NZ  
3958 N N   . ILE A 511 ? 0.5495 0.3166 0.4467 -0.0131 0.0690  0.0173  511 ILE A N   
3959 C CA  . ILE A 511 ? 0.5143 0.2748 0.4006 -0.0191 0.0682  0.0185  511 ILE A CA  
3960 C C   . ILE A 511 ? 0.5512 0.2924 0.4214 -0.0193 0.0726  0.0169  511 ILE A C   
3961 O O   . ILE A 511 ? 0.5683 0.2963 0.4295 -0.0167 0.0714  0.0157  511 ILE A O   
3962 C CB  . ILE A 511 ? 0.5487 0.3090 0.4321 -0.0214 0.0592  0.0246  511 ILE A CB  
3963 C CG1 . ILE A 511 ? 0.5617 0.3434 0.4549 -0.0232 0.0566  0.0260  511 ILE A CG1 
3964 C CG2 . ILE A 511 ? 0.4820 0.2343 0.3575 -0.0256 0.0580  0.0257  511 ILE A CG2 
3965 C CD1 . ILE A 511 ? 0.5360 0.3196 0.4261 -0.0256 0.0500  0.0335  511 ILE A CD1 
3966 N N   . PHE A 512 ? 0.5079 0.2470 0.3739 -0.0224 0.0781  0.0169  512 PHE A N   
3967 C CA  . PHE A 512 ? 0.5589 0.2821 0.4059 -0.0228 0.0818  0.0184  512 PHE A CA  
3968 C C   . PHE A 512 ? 0.5861 0.3060 0.4285 -0.0249 0.0760  0.0250  512 PHE A C   
3969 O O   . PHE A 512 ? 0.5614 0.2910 0.4187 -0.0265 0.0749  0.0259  512 PHE A O   
3970 C CB  . PHE A 512 ? 0.5511 0.2733 0.3985 -0.0237 0.0960  0.0160  512 PHE A CB  
3971 C CG  . PHE A 512 ? 0.5391 0.2689 0.3976 -0.0211 0.1034  0.0087  512 PHE A CG  
3972 C CD1 . PHE A 512 ? 0.5579 0.2771 0.4036 -0.0180 0.1079  0.0047  512 PHE A CD1 
3973 C CD2 . PHE A 512 ? 0.5409 0.2903 0.4243 -0.0217 0.1057  0.0047  512 PHE A CD2 
3974 C CE1 . PHE A 512 ? 0.5718 0.2990 0.4332 -0.0139 0.1158  -0.0024 512 PHE A CE1 
3975 C CE2 . PHE A 512 ? 0.5278 0.2882 0.4267 -0.0179 0.1110  -0.0011 512 PHE A CE2 
3976 C CZ  . PHE A 512 ? 0.5571 0.3059 0.4469 -0.0132 0.1167  -0.0043 512 PHE A CZ  
3977 N N   . HIS A 513 ? 0.5503 0.2580 0.3725 -0.0246 0.0724  0.0289  513 HIS A N   
3978 C CA  . HIS A 513 ? 0.5588 0.2640 0.3777 -0.0245 0.0668  0.0372  513 HIS A CA  
3979 C C   . HIS A 513 ? 0.5902 0.2831 0.3876 -0.0234 0.0724  0.0433  513 HIS A C   
3980 O O   . HIS A 513 ? 0.5672 0.2526 0.3423 -0.0239 0.0739  0.0401  513 HIS A O   
3981 C CB  . HIS A 513 ? 0.5614 0.2686 0.3774 -0.0253 0.0521  0.0384  513 HIS A CB  
3982 C CG  . HIS A 513 ? 0.5621 0.2722 0.3822 -0.0238 0.0444  0.0472  513 HIS A CG  
3983 N ND1 . HIS A 513 ? 0.5689 0.2720 0.3700 -0.0215 0.0400  0.0552  513 HIS A ND1 
3984 C CD2 . HIS A 513 ? 0.5325 0.2532 0.3745 -0.0234 0.0402  0.0497  513 HIS A CD2 
3985 C CE1 . HIS A 513 ? 0.5678 0.2775 0.3821 -0.0186 0.0321  0.0635  513 HIS A CE1 
3986 N NE2 . HIS A 513 ? 0.6087 0.3289 0.4494 -0.0198 0.0333  0.0592  513 HIS A NE2 
3987 N N   . VAL A 514 ? 0.5993 0.2890 0.4027 -0.0221 0.0770  0.0521  514 VAL A N   
3988 C CA  . VAL A 514 ? 0.5961 0.2725 0.3790 -0.0210 0.0839  0.0621  514 VAL A CA  
3989 C C   . VAL A 514 ? 0.6439 0.3175 0.4236 -0.0166 0.0731  0.0763  514 VAL A C   
3990 O O   . VAL A 514 ? 0.6530 0.3354 0.4542 -0.0145 0.0644  0.0770  514 VAL A O   
3991 C CB  . VAL A 514 ? 0.5857 0.2570 0.3805 -0.0233 0.1026  0.0623  514 VAL A CB  
3992 C CG1 . VAL A 514 ? 0.5882 0.2681 0.3925 -0.0268 0.1114  0.0482  514 VAL A CG1 
3993 C CG2 . VAL A 514 ? 0.5708 0.2441 0.3948 -0.0228 0.1051  0.0647  514 VAL A CG2 
3994 N N   . ASN A 515 ? 0.5967 0.2589 0.3494 -0.0147 0.0742  0.0884  515 ASN A N   
3995 C CA  . ASN A 515 ? 0.6449 0.3042 0.3942 -0.0085 0.0640  0.1061  515 ASN A CA  
3996 C C   . ASN A 515 ? 0.6928 0.3344 0.4217 -0.0073 0.0770  0.1213  515 ASN A C   
3997 O O   . ASN A 515 ? 0.6786 0.3147 0.3702 -0.0093 0.0777  0.1246  515 ASN A O   
3998 C CB  . ASN A 515 ? 0.6737 0.3425 0.4033 -0.0076 0.0429  0.1071  515 ASN A CB  
3999 C CG  . ASN A 515 ? 0.7149 0.3857 0.4434 0.0002  0.0291  0.1268  515 ASN A CG  
4000 O OD1 . ASN A 515 ? 0.6774 0.3429 0.4298 0.0064  0.0343  0.1384  515 ASN A OD1 
4001 N ND2 . ASN A 515 ? 0.6835 0.3628 0.3862 0.0001  0.0108  0.1298  515 ASN A ND2 
4002 N N   . TRP A 516 ? 0.6802 0.3117 0.4329 -0.0050 0.0891  0.1297  516 TRP A N   
4003 C CA  . TRP A 516 ? 0.7454 0.3657 0.4859 -0.0039 0.0996  0.1448  516 TRP A CA  
4004 C C   . TRP A 516 ? 0.7550 0.3716 0.4800 0.0050  0.0851  0.1685  516 TRP A C   
4005 O O   . TRP A 516 ? 0.7746 0.3851 0.4887 0.0061  0.0912  0.1834  516 TRP A O   
4006 C CB  . TRP A 516 ? 0.7137 0.3342 0.4939 -0.0057 0.1151  0.1413  516 TRP A CB  
4007 C CG  . TRP A 516 ? 0.6954 0.3241 0.5015 -0.0131 0.1266  0.1192  516 TRP A CG  
4008 C CD1 . TRP A 516 ? 0.6972 0.3319 0.5421 -0.0144 0.1319  0.1094  516 TRP A CD1 
4009 C CD2 . TRP A 516 ? 0.7148 0.3473 0.5097 -0.0201 0.1344  0.1043  516 TRP A CD2 
4010 N NE1 . TRP A 516 ? 0.7155 0.3595 0.5720 -0.0221 0.1405  0.0902  516 TRP A NE1 
4011 C CE2 . TRP A 516 ? 0.6653 0.3081 0.4941 -0.0250 0.1420  0.0878  516 TRP A CE2 
4012 C CE3 . TRP A 516 ? 0.6748 0.3026 0.4340 -0.0226 0.1360  0.1028  516 TRP A CE3 
4013 C CZ2 . TRP A 516 ? 0.6682 0.3178 0.4991 -0.0315 0.1498  0.0727  516 TRP A CZ2 
4014 C CZ3 . TRP A 516 ? 0.6747 0.3079 0.4387 -0.0286 0.1456  0.0865  516 TRP A CZ3 
4015 C CH2 . TRP A 516 ? 0.6335 0.2777 0.4340 -0.0324 0.1516  0.0730  516 TRP A CH2 
4016 N N   . PHE A 517 ? 0.7512 0.3736 0.4782 0.0113  0.0658  0.1729  517 PHE A N   
4017 C CA  . PHE A 517 ? 0.7914 0.4130 0.5218 0.0226  0.0520  0.1965  517 PHE A CA  
4018 C C   . PHE A 517 ? 0.7859 0.4211 0.4805 0.0251  0.0280  0.2045  517 PHE A C   
4019 O O   . PHE A 517 ? 0.8008 0.4436 0.5033 0.0353  0.0106  0.2220  517 PHE A O   
4020 C CB  . PHE A 517 ? 0.7613 0.3907 0.5422 0.0291  0.0479  0.1932  517 PHE A CB  
4021 C CG  . PHE A 517 ? 0.7333 0.3584 0.5537 0.0249  0.0682  0.1809  517 PHE A CG  
4022 C CD1 . PHE A 517 ? 0.7820 0.3986 0.6222 0.0282  0.0767  0.1917  517 PHE A CD1 
4023 C CD2 . PHE A 517 ? 0.7041 0.3357 0.5401 0.0166  0.0770  0.1571  517 PHE A CD2 
4024 C CE1 . PHE A 517 ? 0.7416 0.3558 0.6149 0.0229  0.0941  0.1764  517 PHE A CE1 
4025 C CE2 . PHE A 517 ? 0.7109 0.3438 0.5796 0.0117  0.0929  0.1433  517 PHE A CE2 
4026 C CZ  . PHE A 517 ? 0.6907 0.3146 0.5774 0.0146  0.1017  0.1518  517 PHE A CZ  
4027 N N   . ARG A 518 ? 0.7916 0.4317 0.4495 0.0162  0.0263  0.1911  518 ARG A N   
4028 C CA  . ARG A 518 ? 0.8652 0.5198 0.4875 0.0161  0.0035  0.1945  518 ARG A CA  
4029 C C   . ARG A 518 ? 0.9975 0.6426 0.5849 0.0232  -0.0009 0.2241  518 ARG A C   
4030 O O   . ARG A 518 ? 0.9806 0.6081 0.5596 0.0229  0.0191  0.2356  518 ARG A O   
4031 C CB  . ARG A 518 ? 0.9648 0.6224 0.5551 0.0044  0.0068  0.1713  518 ARG A CB  
4032 C CG  . ARG A 518 ? 0.8887 0.5669 0.4605 0.0008  -0.0185 0.1614  518 ARG A CG  
4033 C CD  . ARG A 518 ? 0.9571 0.6336 0.4990 -0.0107 -0.0122 0.1368  518 ARG A CD  
4034 N NE  . ARG A 518 ? 0.9098 0.6037 0.4318 -0.0160 -0.0354 0.1261  518 ARG A NE  
4035 C CZ  . ARG A 518 ? 0.9841 0.6806 0.5003 -0.0257 -0.0356 0.1000  518 ARG A CZ  
4036 N NH1 . ARG A 518 ? 0.9189 0.6031 0.4486 -0.0295 -0.0153 0.0834  518 ARG A NH1 
4037 N NH2 . ARG A 518 ? 0.9841 0.6963 0.4829 -0.0318 -0.0572 0.0902  518 ARG A NH2 
4038 N N   . LYS A 519 ? 1.0493 0.7124 0.6238 0.0289  -0.0279 0.2359  519 LYS A N   
4039 C CA  . LYS A 519 ? 1.1180 0.7764 0.6587 0.0374  -0.0373 0.2675  519 LYS A CA  
4040 C C   . LYS A 519 ? 1.2468 0.9229 0.7326 0.0314  -0.0580 0.2640  519 LYS A C   
4041 O O   . LYS A 519 ? 1.2044 0.9014 0.6930 0.0239  -0.0728 0.2400  519 LYS A O   
4042 C CB  . LYS A 519 ? 1.1249 0.7906 0.7061 0.0535  -0.0529 0.2911  519 LYS A CB  
4043 C CG  . LYS A 519 ? 1.0724 0.7224 0.7085 0.0585  -0.0302 0.2958  519 LYS A CG  
4044 C CD  . LYS A 519 ? 1.0417 0.6983 0.7236 0.0743  -0.0444 0.3144  519 LYS A CD  
4045 C CE  . LYS A 519 ? 1.0837 0.7209 0.8149 0.0749  -0.0220 0.3115  519 LYS A CE  
4046 N NZ  . LYS A 519 ? 1.1491 0.7860 0.9203 0.0907  -0.0328 0.3264  519 LYS A NZ  
4047 N N   . ASP A 520 ? 1.3894 1.0693 0.8409 0.0329  -0.0560 0.2831  520 ASP A N   
4048 C CA  . ASP A 520 ? 1.5058 1.2054 0.9026 0.0275  -0.0738 0.2808  520 ASP A CA  
4049 C C   . ASP A 520 ? 1.5944 1.3219 0.9967 0.0390  -0.1083 0.3004  520 ASP A C   
4050 O O   . ASP A 520 ? 1.5804 1.3103 1.0305 0.0514  -0.1179 0.3144  520 ASP A O   
4051 C CB  . ASP A 520 ? 1.5630 1.2587 0.9226 0.0233  -0.0540 0.2914  520 ASP A CB  
4052 C CG  . ASP A 520 ? 1.5641 1.2566 0.9462 0.0339  -0.0476 0.3279  520 ASP A CG  
4053 O OD1 . ASP A 520 ? 1.5414 1.2359 0.9674 0.0460  -0.0595 0.3454  520 ASP A OD1 
4054 O OD2 . ASP A 520 ? 1.5768 1.2635 0.9341 0.0287  -0.0304 0.3389  520 ASP A OD2 
4055 N N   . LYS A 521 ? 1.6466 1.3982 1.0019 0.0353  -0.1267 0.2999  521 LYS A N   
4056 C CA  . LYS A 521 ? 1.6858 1.4696 1.0443 0.0475  -0.1597 0.3188  521 LYS A CA  
4057 C C   . LYS A 521 ? 1.6728 1.4554 1.0497 0.0679  -0.1549 0.3591  521 LYS A C   
4058 O O   . LYS A 521 ? 1.6874 1.4893 1.0792 0.0847  -0.1797 0.3761  521 LYS A O   
4059 C CB  . LYS A 521 ? 1.7646 1.5754 1.0652 0.0386  -0.1776 0.3068  521 LYS A CB  
4060 C CG  . LYS A 521 ? 1.7967 1.6056 1.0752 0.0175  -0.1778 0.2653  521 LYS A CG  
4061 C CD  . LYS A 521 ? 1.8827 1.7166 1.1036 0.0084  -0.1903 0.2518  521 LYS A CD  
4062 C CE  . LYS A 521 ? 1.9257 1.7541 1.1266 -0.0126 -0.1859 0.2085  521 LYS A CE  
4063 N NZ  . LYS A 521 ? 1.9924 1.8445 1.1392 -0.0217 -0.1954 0.1920  521 LYS A NZ  
4064 N N   . ASN A 522 ? 1.6493 1.4085 1.0278 0.0660  -0.1243 0.3734  522 ASN A N   
4065 C CA  . ASN A 522 ? 1.6239 1.3802 1.0288 0.0796  -0.1187 0.4122  522 ASN A CA  
4066 C C   . ASN A 522 ? 1.5567 1.2942 1.0348 0.0836  -0.1149 0.4163  522 ASN A C   
4067 O O   . ASN A 522 ? 1.5739 1.2517 1.0404 0.0872  -0.1355 0.4250  522 ASN A O   
4068 C CB  . ASN A 522 ? 1.6218 1.3587 1.0015 0.0627  -0.0952 0.4239  522 ASN A CB  
4069 C CG  . ASN A 522 ? 1.7064 1.4636 1.0158 0.0577  -0.0963 0.4203  522 ASN A CG  
4070 O OD1 . ASN A 522 ? 1.7157 1.4575 0.9963 0.0435  -0.0725 0.4120  522 ASN A OD1 
4071 N ND2 . ASN A 522 ? 1.7633 1.5508 1.0433 0.0708  -0.1234 0.4206  522 ASN A ND2 
4072 N N   . GLY A 523 ? 1.5197 1.2405 1.0203 0.0777  -0.1024 0.3914  523 GLY A N   
4073 C CA  . GLY A 523 ? 1.4281 1.1232 0.9887 0.0797  -0.0969 0.3891  523 GLY A CA  
4074 C C   . GLY A 523 ? 1.3523 1.0110 0.9266 0.0712  -0.0641 0.3828  523 GLY A C   
4075 O O   . GLY A 523 ? 1.2937 0.9306 0.9138 0.0775  -0.0551 0.3802  523 GLY A O   
4076 N N   . LYS A 524 ? 1.3530 1.0081 0.8910 0.0593  -0.0439 0.3770  524 LYS A N   
4077 C CA  . LYS A 524 ? 1.3322 0.9613 0.8870 0.0508  -0.0118 0.3668  524 LYS A CA  
4078 C C   . LYS A 524 ? 1.2245 0.8542 0.7745 0.0413  0.0056  0.3329  524 LYS A C   
4079 O O   . LYS A 524 ? 1.2487 0.8920 0.7624 0.0377  -0.0039 0.3186  524 LYS A O   
4080 C CB  . LYS A 524 ? 1.3600 0.9787 0.8805 0.0440  -0.0002 0.3858  524 LYS A CB  
4081 C CG  . LYS A 524 ? 1.4622 1.1031 0.9202 0.0393  -0.0099 0.3919  524 LYS A CG  
4082 C CD  . LYS A 524 ? 1.4486 1.0786 0.8769 0.0344  -0.0026 0.4187  524 LYS A CD  
4083 C CE  . LYS A 524 ? 1.4396 1.0968 0.8053 0.0308  -0.0146 0.4278  524 LYS A CE  
4084 N NZ  . LYS A 524 ? 1.4054 1.0514 0.7410 0.0257  -0.0106 0.4586  524 LYS A NZ  
4085 N N   . PHE A 525 ? 1.1238 0.7367 0.7095 0.0364  0.0295  0.3180  525 PHE A N   
4086 C CA  . PHE A 525 ? 1.1113 0.7232 0.6999 0.0276  0.0443  0.2864  525 PHE A CA  
4087 C C   . PHE A 525 ? 1.1013 0.7140 0.6397 0.0172  0.0554  0.2768  525 PHE A C   
4088 O O   . PHE A 525 ? 1.1844 0.7925 0.7009 0.0138  0.0657  0.2909  525 PHE A O   
4089 C CB  . PHE A 525 ? 1.0488 0.6476 0.6860 0.0239  0.0667  0.2737  525 PHE A CB  
4090 C CG  . PHE A 525 ? 1.0357 0.6323 0.7232 0.0329  0.0596  0.2773  525 PHE A CG  
4091 C CD1 . PHE A 525 ? 0.9588 0.5632 0.6728 0.0347  0.0545  0.2589  525 PHE A CD1 
4092 C CD2 . PHE A 525 ? 1.0914 0.6760 0.7987 0.0394  0.0594  0.2978  525 PHE A CD2 
4093 C CE1 . PHE A 525 ? 0.9437 0.5472 0.7039 0.0429  0.0506  0.2599  525 PHE A CE1 
4094 C CE2 . PHE A 525 ? 1.0720 0.6527 0.8252 0.0484  0.0551  0.2974  525 PHE A CE2 
4095 C CZ  . PHE A 525 ? 0.9975 0.5893 0.7777 0.0500  0.0513  0.2777  525 PHE A CZ  
4096 N N   . LEU A 526 ? 1.0474 0.6644 0.5677 0.0116  0.0536  0.2520  526 LEU A N   
4097 C CA  . LEU A 526 ? 1.1209 0.7370 0.5980 0.0013  0.0661  0.2370  526 LEU A CA  
4098 C C   . LEU A 526 ? 1.1027 0.7077 0.6020 -0.0064 0.0956  0.2216  526 LEU A C   
4099 O O   . LEU A 526 ? 1.1161 0.7186 0.5877 -0.0136 0.1121  0.2162  526 LEU A O   
4100 C CB  . LEU A 526 ? 1.0602 0.6824 0.5107 -0.0029 0.0518  0.2149  526 LEU A CB  
4101 C CG  . LEU A 526 ? 1.1955 0.8330 0.6148 0.0009  0.0206  0.2232  526 LEU A CG  
4102 C CD1 . LEU A 526 ? 1.1910 0.8349 0.6130 -0.0039 0.0055  0.1979  526 LEU A CD1 
4103 C CD2 . LEU A 526 ? 1.2876 0.9342 0.6518 -0.0038 0.0195  0.2279  526 LEU A CD2 
4104 N N   . TRP A 527 ? 0.9892 0.5901 0.5391 -0.0050 0.1025  0.2135  527 TRP A N   
4105 C CA  . TRP A 527 ? 0.9536 0.5491 0.5297 -0.0122 0.1271  0.1967  527 TRP A CA  
4106 C C   . TRP A 527 ? 0.9203 0.5090 0.5349 -0.0108 0.1381  0.2087  527 TRP A C   
4107 O O   . TRP A 527 ? 0.9353 0.5237 0.5780 -0.0035 0.1264  0.2191  527 TRP A O   
4108 C CB  . TRP A 527 ? 0.8937 0.4931 0.4954 -0.0139 0.1253  0.1734  527 TRP A CB  
4109 C CG  . TRP A 527 ? 0.8730 0.4719 0.5008 -0.0210 0.1470  0.1547  527 TRP A CG  
4110 C CD1 . TRP A 527 ? 0.8561 0.4584 0.5317 -0.0218 0.1530  0.1456  527 TRP A CD1 
4111 C CD2 . TRP A 527 ? 0.8649 0.4624 0.4736 -0.0285 0.1652  0.1417  527 TRP A CD2 
4112 N NE1 . TRP A 527 ? 0.8550 0.4593 0.5424 -0.0292 0.1721  0.1290  527 TRP A NE1 
4113 C CE2 . TRP A 527 ? 0.8404 0.4414 0.4895 -0.0330 0.1807  0.1269  527 TRP A CE2 
4114 C CE3 . TRP A 527 ? 0.9410 0.5363 0.5031 -0.0321 0.1705  0.1399  527 TRP A CE3 
4115 C CZ2 . TRP A 527 ? 0.8663 0.4690 0.5145 -0.0399 0.2009  0.1124  527 TRP A CZ2 
4116 C CZ3 . TRP A 527 ? 0.9173 0.5130 0.4785 -0.0389 0.1924  0.1238  527 TRP A CZ3 
4117 C CH2 . TRP A 527 ? 0.9027 0.5022 0.5083 -0.0423 0.2073  0.1112  527 TRP A CH2 
4118 N N   . PRO A 528 ? 0.9473 0.5296 0.5648 -0.0177 0.1606  0.2072  528 PRO A N   
4119 C CA  . PRO A 528 ? 0.9243 0.4972 0.5768 -0.0176 0.1711  0.2176  528 PRO A CA  
4120 C C   . PRO A 528 ? 0.9148 0.4899 0.6194 -0.0182 0.1751  0.2001  528 PRO A C   
4121 O O   . PRO A 528 ? 0.8590 0.4265 0.5943 -0.0155 0.1767  0.2079  528 PRO A O   
4122 C CB  . PRO A 528 ? 0.9238 0.4905 0.5616 -0.0266 0.1949  0.2176  528 PRO A CB  
4123 C CG  . PRO A 528 ? 0.9322 0.5074 0.5439 -0.0318 0.2003  0.1979  528 PRO A CG  
4124 C CD  . PRO A 528 ? 0.9416 0.5236 0.5252 -0.0256 0.1767  0.1995  528 PRO A CD  
4125 N N   . GLY A 529 ? 0.8469 0.4320 0.5613 -0.0220 0.1769  0.1763  529 GLY A N   
4126 C CA  . GLY A 529 ? 0.8226 0.4138 0.5821 -0.0231 0.1785  0.1594  529 GLY A CA  
4127 C C   . GLY A 529 ? 0.8003 0.3877 0.5910 -0.0303 0.1992  0.1518  529 GLY A C   
4128 O O   . GLY A 529 ? 0.8066 0.3876 0.5862 -0.0360 0.2154  0.1559  529 GLY A O   
4129 N N   . PHE A 530 ? 0.7472 0.3395 0.5775 -0.0307 0.1989  0.1395  530 PHE A N   
4130 C CA  . PHE A 530 ? 0.7517 0.3422 0.6168 -0.0381 0.2166  0.1285  530 PHE A CA  
4131 C C   . PHE A 530 ? 0.7468 0.3454 0.6106 -0.0481 0.2324  0.1131  530 PHE A C   
4132 O O   . PHE A 530 ? 0.7440 0.3560 0.6044 -0.0497 0.2276  0.0990  530 PHE A O   
4133 C CB  . PHE A 530 ? 0.7950 0.3667 0.6638 -0.0357 0.2233  0.1483  530 PHE A CB  
4134 C CG  . PHE A 530 ? 0.7818 0.3467 0.6561 -0.0248 0.2073  0.1630  530 PHE A CG  
4135 C CD1 . PHE A 530 ? 0.7801 0.3493 0.6898 -0.0227 0.2042  0.1504  530 PHE A CD1 
4136 C CD2 . PHE A 530 ? 0.8254 0.3814 0.6697 -0.0168 0.1953  0.1890  530 PHE A CD2 
4137 C CE1 . PHE A 530 ? 0.8133 0.3767 0.7315 -0.0120 0.1910  0.1629  530 PHE A CE1 
4138 C CE2 . PHE A 530 ? 0.8013 0.3525 0.6542 -0.0059 0.1797  0.2030  530 PHE A CE2 
4139 C CZ  . PHE A 530 ? 0.8118 0.3661 0.7032 -0.0031 0.1783  0.1897  530 PHE A CZ  
4140 N N   . GLY A 531 ? 0.7338 0.3247 0.6027 -0.0550 0.2515  0.1155  531 GLY A N   
4141 C CA  . GLY A 531 ? 0.7774 0.3779 0.6513 -0.0647 0.2678  0.1002  531 GLY A CA  
4142 C C   . GLY A 531 ? 0.7763 0.3817 0.6147 -0.0634 0.2655  0.1005  531 GLY A C   
4143 O O   . GLY A 531 ? 0.7499 0.3680 0.5968 -0.0694 0.2745  0.0840  531 GLY A O   
4144 N N   . GLU A 532 ? 0.7759 0.3723 0.5756 -0.0558 0.2537  0.1183  532 GLU A N   
4145 C CA  . GLU A 532 ? 0.7853 0.3851 0.5482 -0.0550 0.2520  0.1160  532 GLU A CA  
4146 C C   . GLU A 532 ? 0.7367 0.3480 0.5037 -0.0525 0.2390  0.1010  532 GLU A C   
4147 O O   . GLU A 532 ? 0.7876 0.4025 0.5335 -0.0537 0.2419  0.0928  532 GLU A O   
4148 C CB  . GLU A 532 ? 0.8482 0.4375 0.5658 -0.0489 0.2418  0.1379  532 GLU A CB  
4149 C CG  . GLU A 532 ? 0.8566 0.4336 0.5629 -0.0513 0.2540  0.1573  532 GLU A CG  
4150 C CD  . GLU A 532 ? 0.8654 0.4430 0.5714 -0.0611 0.2798  0.1496  532 GLU A CD  
4151 O OE1 . GLU A 532 ? 0.8747 0.4630 0.5835 -0.0655 0.2887  0.1302  532 GLU A OE1 
4152 O OE2 . GLU A 532 ? 0.9430 0.5102 0.6482 -0.0646 0.2921  0.1638  532 GLU A OE2 
4153 N N   . ASN A 533 ? 0.7143 0.3307 0.5075 -0.0493 0.2258  0.0968  533 ASN A N   
4154 C CA  . ASN A 533 ? 0.7013 0.3286 0.5006 -0.0481 0.2145  0.0831  533 ASN A CA  
4155 C C   . ASN A 533 ? 0.6882 0.3277 0.5069 -0.0557 0.2282  0.0646  533 ASN A C   
4156 O O   . ASN A 533 ? 0.6677 0.3143 0.4854 -0.0550 0.2215  0.0553  533 ASN A O   
4157 C CB  . ASN A 533 ? 0.6583 0.2909 0.4853 -0.0446 0.2007  0.0811  533 ASN A CB  
4158 C CG  . ASN A 533 ? 0.7372 0.3606 0.5496 -0.0359 0.1857  0.0992  533 ASN A CG  
4159 O OD1 . ASN A 533 ? 0.7553 0.3715 0.5318 -0.0320 0.1792  0.1118  533 ASN A OD1 
4160 N ND2 . ASN A 533 ? 0.6889 0.3136 0.5296 -0.0330 0.1803  0.1002  533 ASN A ND2 
4161 N N   . SER A 534 ? 0.7151 0.3575 0.5530 -0.0632 0.2474  0.0601  534 SER A N   
4162 C CA  . SER A 534 ? 0.7682 0.4256 0.6264 -0.0706 0.2617  0.0436  534 SER A CA  
4163 C C   . SER A 534 ? 0.6971 0.3541 0.5257 -0.0682 0.2653  0.0417  534 SER A C   
4164 O O   . SER A 534 ? 0.6718 0.3494 0.5205 -0.0678 0.2647  0.0259  534 SER A O   
4165 C CB  . SER A 534 ? 0.7149 0.3748 0.5947 -0.0790 0.2824  0.0406  534 SER A CB  
4166 O OG  . SER A 534 ? 0.7575 0.4023 0.6054 -0.0777 0.2916  0.0546  534 SER A OG  
4167 N N   . ARG A 535 ? 0.7139 0.3559 0.4991 -0.0635 0.2629  0.0542  535 ARG A N   
4168 C CA  . ARG A 535 ? 0.7434 0.3839 0.4962 -0.0618 0.2675  0.0495  535 ARG A CA  
4169 C C   . ARG A 535 ? 0.7453 0.3976 0.5011 -0.0534 0.2425  0.0391  535 ARG A C   
4170 O O   . ARG A 535 ? 0.6948 0.3577 0.4506 -0.0503 0.2425  0.0251  535 ARG A O   
4171 C CB  . ARG A 535 ? 0.7486 0.3743 0.4539 -0.0594 0.2661  0.0638  535 ARG A CB  
4172 C CG  . ARG A 535 ? 0.7657 0.3878 0.4730 -0.0644 0.2831  0.0724  535 ARG A CG  
4173 C CD  . ARG A 535 ? 0.8912 0.5001 0.5506 -0.0618 0.2780  0.0910  535 ARG A CD  
4174 N NE  . ARG A 535 ? 0.8469 0.4497 0.5092 -0.0660 0.2917  0.1044  535 ARG A NE  
4175 C CZ  . ARG A 535 ? 0.9423 0.5454 0.5908 -0.0719 0.3120  0.1033  535 ARG A CZ  
4176 N NH1 . ARG A 535 ? 0.9766 0.5874 0.6110 -0.0738 0.3220  0.0874  535 ARG A NH1 
4177 N NH2 . ARG A 535 ? 0.9265 0.5217 0.5758 -0.0759 0.3233  0.1185  535 ARG A NH2 
4178 N N   . VAL A 536 ? 0.6747 0.3242 0.4349 -0.0496 0.2227  0.0459  536 VAL A N   
4179 C CA  . VAL A 536 ? 0.6527 0.3131 0.4193 -0.0433 0.2006  0.0375  536 VAL A CA  
4180 C C   . VAL A 536 ? 0.6600 0.3425 0.4700 -0.0437 0.1995  0.0230  536 VAL A C   
4181 O O   . VAL A 536 ? 0.6334 0.3275 0.4507 -0.0391 0.1919  0.0125  536 VAL A O   
4182 C CB  . VAL A 536 ? 0.7074 0.3595 0.4658 -0.0397 0.1820  0.0500  536 VAL A CB  
4183 C CG1 . VAL A 536 ? 0.6767 0.3408 0.4465 -0.0351 0.1616  0.0417  536 VAL A CG1 
4184 C CG2 . VAL A 536 ? 0.7101 0.3451 0.4244 -0.0380 0.1791  0.0650  536 VAL A CG2 
4185 N N   . LEU A 537 ? 0.6845 0.3731 0.5241 -0.0494 0.2070  0.0223  537 LEU A N   
4186 C CA  . LEU A 537 ? 0.6495 0.3633 0.5287 -0.0509 0.2050  0.0081  537 LEU A CA  
4187 C C   . LEU A 537 ? 0.6199 0.3490 0.5115 -0.0500 0.2158  -0.0031 537 LEU A C   
4188 O O   . LEU A 537 ? 0.5749 0.3255 0.4904 -0.0459 0.2069  -0.0129 537 LEU A O   
4189 C CB  . LEU A 537 ? 0.6101 0.3275 0.5175 -0.0599 0.2142  0.0064  537 LEU A CB  
4190 C CG  . LEU A 537 ? 0.6843 0.4037 0.6037 -0.0600 0.2002  0.0063  537 LEU A CG  
4191 C CD1 . LEU A 537 ? 0.6917 0.3913 0.5821 -0.0533 0.1879  0.0201  537 LEU A CD1 
4192 C CD2 . LEU A 537 ? 0.7109 0.4274 0.6552 -0.0704 0.2144  0.0032  537 LEU A CD2 
4193 N N   . GLU A 538 ? 0.5883 0.3078 0.4660 -0.0536 0.2361  -0.0012 538 GLU A N   
4194 C CA  . GLU A 538 ? 0.5999 0.3341 0.4910 -0.0517 0.2488  -0.0131 538 GLU A CA  
4195 C C   . GLU A 538 ? 0.6387 0.3740 0.5184 -0.0411 0.2352  -0.0186 538 GLU A C   
4196 O O   . GLU A 538 ? 0.5855 0.3407 0.4942 -0.0355 0.2331  -0.0293 538 GLU A O   
4197 C CB  . GLU A 538 ? 0.6733 0.3940 0.5434 -0.0578 0.2747  -0.0094 538 GLU A CB  
4198 C CG  . GLU A 538 ? 0.7146 0.4517 0.6019 -0.0561 0.2915  -0.0234 538 GLU A CG  
4199 C CD  . GLU A 538 ? 0.8336 0.5581 0.6966 -0.0629 0.3200  -0.0206 538 GLU A CD  
4200 O OE1 . GLU A 538 ? 0.8261 0.5253 0.6401 -0.0644 0.3219  -0.0081 538 GLU A OE1 
4201 O OE2 . GLU A 538 ? 0.8367 0.5790 0.7302 -0.0667 0.3406  -0.0309 538 GLU A OE2 
4202 N N   . TRP A 539 ? 0.6446 0.3590 0.4847 -0.0382 0.2251  -0.0113 539 TRP A N   
4203 C CA  . TRP A 539 ? 0.6374 0.3493 0.4673 -0.0300 0.2131  -0.0176 539 TRP A CA  
4204 C C   . TRP A 539 ? 0.6561 0.3832 0.5153 -0.0246 0.1938  -0.0197 539 TRP A C   
4205 O O   . TRP A 539 ? 0.5977 0.3329 0.4730 -0.0172 0.1903  -0.0276 539 TRP A O   
4206 C CB  . TRP A 539 ? 0.6862 0.3757 0.4698 -0.0303 0.2042  -0.0101 539 TRP A CB  
4207 C CG  . TRP A 539 ? 0.6251 0.3092 0.3974 -0.0245 0.1942  -0.0192 539 TRP A CG  
4208 C CD1 . TRP A 539 ? 0.6862 0.3655 0.4483 -0.0222 0.2064  -0.0320 539 TRP A CD1 
4209 C CD2 . TRP A 539 ? 0.6495 0.3309 0.4215 -0.0212 0.1721  -0.0172 539 TRP A CD2 
4210 N NE1 . TRP A 539 ? 0.6624 0.3341 0.4191 -0.0177 0.1926  -0.0386 539 TRP A NE1 
4211 C CE2 . TRP A 539 ? 0.6418 0.3150 0.4044 -0.0175 0.1715  -0.0289 539 TRP A CE2 
4212 C CE3 . TRP A 539 ? 0.6432 0.3280 0.4235 -0.0216 0.1545  -0.0077 539 TRP A CE3 
4213 C CZ2 . TRP A 539 ? 0.6933 0.3606 0.4551 -0.0152 0.1537  -0.0301 539 TRP A CZ2 
4214 C CZ3 . TRP A 539 ? 0.6632 0.3448 0.4421 -0.0190 0.1374  -0.0086 539 TRP A CZ3 
4215 C CH2 . TRP A 539 ? 0.6743 0.3467 0.4444 -0.0163 0.1369  -0.0191 539 TRP A CH2 
4216 N N   . MET A 540 ? 0.5872 0.3176 0.4534 -0.0277 0.1821  -0.0123 540 MET A N   
4217 C CA  . MET A 540 ? 0.5884 0.3345 0.4780 -0.0240 0.1649  -0.0134 540 MET A CA  
4218 C C   . MET A 540 ? 0.5440 0.3169 0.4724 -0.0220 0.1688  -0.0219 540 MET A C   
4219 O O   . MET A 540 ? 0.5480 0.3332 0.4923 -0.0147 0.1574  -0.0237 540 MET A O   
4220 C CB  . MET A 540 ? 0.5458 0.2916 0.4362 -0.0291 0.1562  -0.0065 540 MET A CB  
4221 C CG  . MET A 540 ? 0.5501 0.2754 0.4103 -0.0290 0.1473  0.0032  540 MET A CG  
4222 S SD  . MET A 540 ? 0.6429 0.3687 0.5139 -0.0346 0.1445  0.0093  540 MET A SD  
4223 C CE  . MET A 540 ? 0.6225 0.3275 0.4616 -0.0318 0.1338  0.0218  540 MET A CE  
4224 N N   . PHE A 541 ? 0.5303 0.3136 0.4763 -0.0287 0.1843  -0.0262 541 PHE A N   
4225 C CA  . PHE A 541 ? 0.5674 0.3811 0.5543 -0.0277 0.1881  -0.0355 541 PHE A CA  
4226 C C   . PHE A 541 ? 0.5524 0.3708 0.5485 -0.0167 0.1910  -0.0407 541 PHE A C   
4227 O O   . PHE A 541 ? 0.5304 0.3703 0.5542 -0.0087 0.1800  -0.0429 541 PHE A O   
4228 C CB  . PHE A 541 ? 0.5542 0.3742 0.5565 -0.0385 0.2085  -0.0400 541 PHE A CB  
4229 C CG  . PHE A 541 ? 0.5899 0.4463 0.6392 -0.0417 0.2094  -0.0504 541 PHE A CG  
4230 C CD1 . PHE A 541 ? 0.5501 0.4292 0.6284 -0.0343 0.2140  -0.0580 541 PHE A CD1 
4231 C CD2 . PHE A 541 ? 0.5453 0.4141 0.6121 -0.0528 0.2070  -0.0539 541 PHE A CD2 
4232 C CE1 . PHE A 541 ? 0.5478 0.4655 0.6729 -0.0374 0.2132  -0.0676 541 PHE A CE1 
4233 C CE2 . PHE A 541 ? 0.5336 0.4394 0.6440 -0.0578 0.2066  -0.0656 541 PHE A CE2 
4234 C CZ  . PHE A 541 ? 0.5648 0.4972 0.7050 -0.0499 0.2086  -0.0718 541 PHE A CZ  
4235 N N   . GLY A 542 ? 0.5439 0.3420 0.5164 -0.0158 0.2060  -0.0425 542 GLY A N   
4236 C CA  . GLY A 542 ? 0.5726 0.3713 0.5538 -0.0054 0.2118  -0.0501 542 GLY A CA  
4237 C C   . GLY A 542 ? 0.5880 0.3787 0.5648 0.0047  0.1926  -0.0469 542 GLY A C   
4238 O O   . GLY A 542 ? 0.5936 0.3958 0.5982 0.0155  0.1901  -0.0506 542 GLY A O   
4239 N N   . ARG A 543 ? 0.5631 0.3340 0.5077 0.0014  0.1793  -0.0389 543 ARG A N   
4240 C CA  . ARG A 543 ? 0.5815 0.3435 0.5225 0.0087  0.1622  -0.0350 543 ARG A CA  
4241 C C   . ARG A 543 ? 0.5834 0.3699 0.5569 0.0141  0.1473  -0.0296 543 ARG A C   
4242 O O   . ARG A 543 ? 0.5982 0.3836 0.5833 0.0238  0.1385  -0.0269 543 ARG A O   
4243 C CB  . ARG A 543 ? 0.5783 0.3195 0.4833 0.0025  0.1513  -0.0278 543 ARG A CB  
4244 C CG  . ARG A 543 ? 0.6141 0.3305 0.4824 -0.0007 0.1594  -0.0323 543 ARG A CG  
4245 C CD  . ARG A 543 ? 0.6288 0.3335 0.4991 0.0068  0.1627  -0.0421 543 ARG A CD  
4246 N NE  . ARG A 543 ? 0.5766 0.2748 0.4523 0.0107  0.1455  -0.0374 543 ARG A NE  
4247 C CZ  . ARG A 543 ? 0.6803 0.3697 0.5700 0.0188  0.1456  -0.0427 543 ARG A CZ  
4248 N NH1 . ARG A 543 ? 0.6794 0.3673 0.5825 0.0253  0.1616  -0.0543 543 ARG A NH1 
4249 N NH2 . ARG A 543 ? 0.6971 0.3776 0.5892 0.0204  0.1309  -0.0362 543 ARG A NH2 
4250 N N   . ILE A 544 ? 0.5442 0.3520 0.5312 0.0076  0.1444  -0.0278 544 ILE A N   
4251 C CA  . ILE A 544 ? 0.5554 0.3910 0.5700 0.0114  0.1298  -0.0240 544 ILE A CA  
4252 C C   . ILE A 544 ? 0.5237 0.3823 0.5762 0.0216  0.1336  -0.0287 544 ILE A C   
4253 O O   . ILE A 544 ? 0.4940 0.3687 0.5662 0.0311  0.1195  -0.0223 544 ILE A O   
4254 C CB  . ILE A 544 ? 0.5268 0.3796 0.5458 -0.0002 0.1275  -0.0252 544 ILE A CB  
4255 C CG1 . ILE A 544 ? 0.5179 0.3510 0.5061 -0.0069 0.1201  -0.0188 544 ILE A CG1 
4256 C CG2 . ILE A 544 ? 0.4885 0.3772 0.5376 0.0022  0.1146  -0.0253 544 ILE A CG2 
4257 C CD1 . ILE A 544 ? 0.4966 0.3375 0.4872 -0.0189 0.1238  -0.0223 544 ILE A CD1 
4258 N N   . GLU A 545 ? 0.5185 0.3805 0.5833 0.0204  0.1530  -0.0385 545 GLU A N   
4259 C CA  . GLU A 545 ? 0.5367 0.4213 0.6421 0.0312  0.1593  -0.0444 545 GLU A CA  
4260 C C   . GLU A 545 ? 0.5626 0.4266 0.6674 0.0451  0.1619  -0.0444 545 GLU A C   
4261 O O   . GLU A 545 ? 0.5877 0.4688 0.7301 0.0575  0.1655  -0.0476 545 GLU A O   
4262 C CB  . GLU A 545 ? 0.5641 0.4598 0.6847 0.0238  0.1825  -0.0561 545 GLU A CB  
4263 C CG  . GLU A 545 ? 0.4973 0.4216 0.6378 0.0111  0.1819  -0.0592 545 GLU A CG  
4264 C CD  . GLU A 545 ? 0.6133 0.5508 0.7773 0.0044  0.2071  -0.0706 545 GLU A CD  
4265 O OE1 . GLU A 545 ? 0.6550 0.5681 0.7975 0.0032  0.2275  -0.0739 545 GLU A OE1 
4266 O OE2 . GLU A 545 ? 0.6142 0.5879 0.8182 -0.0005 0.2069  -0.0768 545 GLU A OE2 
4267 N N   . GLY A 546 ? 0.5763 0.4049 0.6427 0.0433  0.1607  -0.0420 546 GLY A N   
4268 C CA  . GLY A 546 ? 0.6016 0.4069 0.6664 0.0543  0.1638  -0.0445 546 GLY A CA  
4269 C C   . GLY A 546 ? 0.6389 0.4234 0.6876 0.0526  0.1868  -0.0591 546 GLY A C   
4270 O O   . GLY A 546 ? 0.6202 0.3913 0.6799 0.0631  0.1941  -0.0660 546 GLY A O   
4271 N N   . GLU A 547 ? 0.6262 0.4064 0.6483 0.0398  0.1992  -0.0639 547 GLU A N   
4272 C CA  . GLU A 547 ? 0.6745 0.4361 0.6744 0.0369  0.2217  -0.0772 547 GLU A CA  
4273 C C   . GLU A 547 ? 0.6993 0.4265 0.6609 0.0361  0.2170  -0.0804 547 GLU A C   
4274 O O   . GLU A 547 ? 0.6689 0.3847 0.6064 0.0307  0.1994  -0.0708 547 GLU A O   
4275 C CB  . GLU A 547 ? 0.6840 0.4487 0.6616 0.0230  0.2349  -0.0772 547 GLU A CB  
4276 C CG  . GLU A 547 ? 0.7495 0.5470 0.7683 0.0218  0.2459  -0.0794 547 GLU A CG  
4277 C CD  . GLU A 547 ? 0.8951 0.6902 0.8930 0.0079  0.2655  -0.0804 547 GLU A CD  
4278 O OE1 . GLU A 547 ? 0.9564 0.7270 0.9122 0.0031  0.2783  -0.0837 547 GLU A OE1 
4279 O OE2 . GLU A 547 ? 0.9300 0.7471 0.9524 0.0009  0.2684  -0.0778 547 GLU A OE2 
4280 N N   . ASP A 548 ? 0.7286 0.4405 0.6868 0.0407  0.2339  -0.0958 548 ASP A N   
4281 C CA  . ASP A 548 ? 0.7873 0.4670 0.7100 0.0380  0.2317  -0.1038 548 ASP A CA  
4282 C C   . ASP A 548 ? 0.7916 0.4587 0.6599 0.0236  0.2381  -0.1072 548 ASP A C   
4283 O O   . ASP A 548 ? 0.8601 0.5133 0.7025 0.0202  0.2553  -0.1228 548 ASP A O   
4284 C CB  . ASP A 548 ? 0.7932 0.4604 0.7353 0.0486  0.2478  -0.1214 548 ASP A CB  
4285 C CG  . ASP A 548 ? 0.9353 0.5691 0.8465 0.0449  0.2442  -0.1320 548 ASP A CG  
4286 O OD1 . ASP A 548 ? 1.0021 0.6262 0.9057 0.0425  0.2228  -0.1209 548 ASP A OD1 
4287 O OD2 . ASP A 548 ? 1.0225 0.6445 0.9187 0.0428  0.2609  -0.1508 548 ASP A OD2 
4288 N N   . SER A 549 ? 0.7474 0.4196 0.5976 0.0153  0.2235  -0.0918 549 SER A N   
4289 C CA  . SER A 549 ? 0.7616 0.4263 0.5654 0.0034  0.2280  -0.0891 549 SER A CA  
4290 C C   . SER A 549 ? 0.7515 0.4014 0.5211 -0.0030 0.2069  -0.0817 549 SER A C   
4291 O O   . SER A 549 ? 0.7549 0.4018 0.4902 -0.0113 0.2048  -0.0736 549 SER A O   
4292 C CB  . SER A 549 ? 0.7125 0.3962 0.5280 -0.0009 0.2331  -0.0772 549 SER A CB  
4293 O OG  . SER A 549 ? 0.6592 0.3557 0.5019 0.0017  0.2136  -0.0651 549 SER A OG  
4294 N N   . ALA A 550 ? 0.6788 0.3201 0.4593 0.0009  0.1916  -0.0831 550 ALA A N   
4295 C CA  . ALA A 550 ? 0.7018 0.3332 0.4583 -0.0055 0.1712  -0.0765 550 ALA A CA  
4296 C C   . ALA A 550 ? 0.7745 0.3848 0.5110 -0.0082 0.1702  -0.0927 550 ALA A C   
4297 O O   . ALA A 550 ? 0.7481 0.3491 0.5007 -0.0024 0.1819  -0.1073 550 ALA A O   
4298 C CB  . ALA A 550 ? 0.7497 0.3902 0.5358 -0.0019 0.1530  -0.0625 550 ALA A CB  
4299 N N   . LYS A 551 ? 0.7808 0.3848 0.4852 -0.0172 0.1555  -0.0903 551 LYS A N   
4300 C CA  . LYS A 551 ? 0.8045 0.3911 0.4883 -0.0234 0.1493  -0.1056 551 LYS A CA  
4301 C C   . LYS A 551 ? 0.7922 0.3790 0.4869 -0.0266 0.1265  -0.0956 551 LYS A C   
4302 O O   . LYS A 551 ? 0.7024 0.3026 0.3972 -0.0281 0.1142  -0.0781 551 LYS A O   
4303 C CB  . LYS A 551 ? 0.8476 0.4315 0.4795 -0.0329 0.1520  -0.1130 551 LYS A CB  
4304 C CG  . LYS A 551 ? 0.9591 0.5298 0.5643 -0.0423 0.1428  -0.1302 551 LYS A CG  
4305 C CD  . LYS A 551 ? 1.0284 0.6013 0.5778 -0.0513 0.1445  -0.1351 551 LYS A CD  
4306 C CE  . LYS A 551 ? 1.0258 0.6139 0.5592 -0.0531 0.1285  -0.1102 551 LYS A CE  
4307 N NZ  . LYS A 551 ? 1.1540 0.7444 0.6307 -0.0608 0.1283  -0.1112 551 LYS A NZ  
4308 N N   . LEU A 552 ? 0.7447 0.3158 0.4509 -0.0282 0.1227  -0.1070 552 LEU A N   
4309 C CA  . LEU A 552 ? 0.7818 0.3527 0.5025 -0.0321 0.1040  -0.0979 552 LEU A CA  
4310 C C   . LEU A 552 ? 0.7721 0.3445 0.4609 -0.0449 0.0889  -0.1024 552 LEU A C   
4311 O O   . LEU A 552 ? 0.8055 0.3675 0.4669 -0.0522 0.0920  -0.1216 552 LEU A O   
4312 C CB  . LEU A 552 ? 0.7391 0.2905 0.4887 -0.0290 0.1075  -0.1063 552 LEU A CB  
4313 C CG  . LEU A 552 ? 0.7340 0.2825 0.4985 -0.0351 0.0912  -0.0978 552 LEU A CG  
4314 C CD1 . LEU A 552 ? 0.8117 0.3808 0.5935 -0.0304 0.0821  -0.0733 552 LEU A CD1 
4315 C CD2 . LEU A 552 ? 0.8033 0.3263 0.5945 -0.0329 0.0972  -0.1064 552 LEU A CD2 
4316 N N   . THR A 553 ? 0.7279 0.3146 0.4216 -0.0476 0.0725  -0.0859 553 THR A N   
4317 C CA  . THR A 553 ? 0.7584 0.3521 0.4303 -0.0583 0.0551  -0.0873 553 THR A CA  
4318 C C   . THR A 553 ? 0.7535 0.3518 0.4542 -0.0618 0.0412  -0.0787 553 THR A C   
4319 O O   . THR A 553 ? 0.7067 0.3045 0.4379 -0.0555 0.0449  -0.0682 553 THR A O   
4320 C CB  . THR A 553 ? 0.7717 0.3823 0.4190 -0.0573 0.0497  -0.0731 553 THR A CB  
4321 O OG1 . THR A 553 ? 0.7390 0.3635 0.4115 -0.0524 0.0429  -0.0528 553 THR A OG1 
4322 C CG2 . THR A 553 ? 0.7708 0.3786 0.3977 -0.0521 0.0680  -0.0747 553 THR A CG2 
4323 N N   . PRO A 554 ? 0.7112 0.3166 0.4027 -0.0723 0.0248  -0.0826 554 PRO A N   
4324 C CA  . PRO A 554 ? 0.7001 0.3130 0.4209 -0.0768 0.0131  -0.0742 554 PRO A CA  
4325 C C   . PRO A 554 ? 0.7315 0.3611 0.4724 -0.0691 0.0110  -0.0516 554 PRO A C   
4326 O O   . PRO A 554 ? 0.6910 0.3229 0.4598 -0.0706 0.0085  -0.0443 554 PRO A O   
4327 C CB  . PRO A 554 ? 0.7737 0.3984 0.4780 -0.0888 -0.0048 -0.0827 554 PRO A CB  
4328 C CG  . PRO A 554 ? 0.8026 0.4142 0.4735 -0.0939 0.0003  -0.1044 554 PRO A CG  
4329 C CD  . PRO A 554 ? 0.7654 0.3705 0.4216 -0.0823 0.0176  -0.0997 554 PRO A CD  
4330 N N   . ILE A 555 ? 0.6357 0.2764 0.3635 -0.0620 0.0130  -0.0407 555 ILE A N   
4331 C CA  . ILE A 555 ? 0.6356 0.2909 0.3834 -0.0560 0.0121  -0.0227 555 ILE A CA  
4332 C C   . ILE A 555 ? 0.6926 0.3442 0.4530 -0.0470 0.0267  -0.0173 555 ILE A C   
4333 O O   . ILE A 555 ? 0.6603 0.3236 0.4385 -0.0432 0.0271  -0.0053 555 ILE A O   
4334 C CB  . ILE A 555 ? 0.7024 0.3722 0.4349 -0.0539 0.0047  -0.0124 555 ILE A CB  
4335 C CG1 . ILE A 555 ? 0.7070 0.3695 0.4109 -0.0495 0.0155  -0.0135 555 ILE A CG1 
4336 C CG2 . ILE A 555 ? 0.7013 0.3808 0.4254 -0.0618 -0.0134 -0.0159 555 ILE A CG2 
4337 C CD1 . ILE A 555 ? 0.7125 0.3846 0.4052 -0.0449 0.0133  0.0019  555 ILE A CD1 
4338 N N   . GLY A 556 ? 0.6787 0.3167 0.4320 -0.0438 0.0386  -0.0271 556 GLY A N   
4339 C CA  . GLY A 556 ? 0.7127 0.3515 0.4803 -0.0350 0.0513  -0.0228 556 GLY A CA  
4340 C C   . GLY A 556 ? 0.6767 0.3070 0.4266 -0.0319 0.0648  -0.0332 556 GLY A C   
4341 O O   . GLY A 556 ? 0.7226 0.3433 0.4478 -0.0369 0.0653  -0.0453 556 GLY A O   
4342 N N   . TYR A 557 ? 0.6636 0.2997 0.4271 -0.0244 0.0763  -0.0296 557 TYR A N   
4343 C CA  . TYR A 557 ? 0.7135 0.3450 0.4645 -0.0215 0.0921  -0.0388 557 TYR A CA  
4344 C C   . TYR A 557 ? 0.7018 0.3406 0.4297 -0.0243 0.0948  -0.0322 557 TYR A C   
4345 O O   . TYR A 557 ? 0.6472 0.2975 0.3838 -0.0240 0.0896  -0.0191 557 TYR A O   
4346 C CB  . TYR A 557 ? 0.6656 0.3036 0.4463 -0.0125 0.1034  -0.0381 557 TYR A CB  
4347 C CG  . TYR A 557 ? 0.7442 0.3733 0.5488 -0.0072 0.1022  -0.0415 557 TYR A CG  
4348 C CD1 . TYR A 557 ? 0.7491 0.3583 0.5479 -0.0073 0.1086  -0.0567 557 TYR A CD1 
4349 C CD2 . TYR A 557 ? 0.7285 0.3682 0.5610 -0.0022 0.0953  -0.0291 557 TYR A CD2 
4350 C CE1 . TYR A 557 ? 0.8171 0.4138 0.6410 -0.0016 0.1087  -0.0583 557 TYR A CE1 
4351 C CE2 . TYR A 557 ? 0.6719 0.3013 0.5258 0.0036  0.0941  -0.0283 557 TYR A CE2 
4352 C CZ  . TYR A 557 ? 0.7883 0.3950 0.6396 0.0044  0.1012  -0.0422 557 TYR A CZ  
4353 O OH  . TYR A 557 ? 0.8315 0.4245 0.7070 0.0110  0.1013  -0.0397 557 TYR A OH  
4354 N N   . VAL A 558 ? 0.7217 0.3525 0.4196 -0.0270 0.1043  -0.0413 558 VAL A N   
4355 C CA  . VAL A 558 ? 0.7146 0.3492 0.3883 -0.0290 0.1108  -0.0332 558 VAL A CA  
4356 C C   . VAL A 558 ? 0.7507 0.3820 0.4191 -0.0270 0.1335  -0.0430 558 VAL A C   
4357 O O   . VAL A 558 ? 0.7303 0.3548 0.4078 -0.0244 0.1420  -0.0584 558 VAL A O   
4358 C CB  . VAL A 558 ? 0.7516 0.3826 0.3860 -0.0355 0.0986  -0.0312 558 VAL A CB  
4359 C CG1 . VAL A 558 ? 0.7406 0.3775 0.3872 -0.0374 0.0767  -0.0242 558 VAL A CG1 
4360 C CG2 . VAL A 558 ? 0.8203 0.4397 0.4256 -0.0401 0.1037  -0.0505 558 VAL A CG2 
4361 N N   . PRO A 559 ? 0.7508 0.3862 0.4082 -0.0281 0.1453  -0.0344 559 PRO A N   
4362 C CA  . PRO A 559 ? 0.7324 0.3669 0.3873 -0.0274 0.1696  -0.0438 559 PRO A CA  
4363 C C   . PRO A 559 ? 0.7586 0.3806 0.3759 -0.0312 0.1773  -0.0601 559 PRO A C   
4364 O O   . PRO A 559 ? 0.8323 0.4482 0.4111 -0.0369 0.1660  -0.0587 559 PRO A O   
4365 C CB  . PRO A 559 ? 0.7269 0.3654 0.3714 -0.0306 0.1789  -0.0284 559 PRO A CB  
4366 C CG  . PRO A 559 ? 0.7044 0.3479 0.3626 -0.0301 0.1606  -0.0122 559 PRO A CG  
4367 C CD  . PRO A 559 ? 0.7409 0.3814 0.3937 -0.0298 0.1391  -0.0154 559 PRO A CD  
4368 N N   . LYS A 560 ? 0.8023 0.4224 0.4325 -0.0278 0.1965  -0.0766 560 LYS A N   
4369 C CA  . LYS A 560 ? 0.8639 0.4724 0.4576 -0.0321 0.2100  -0.0952 560 LYS A CA  
4370 C C   . LYS A 560 ? 0.9427 0.5512 0.4908 -0.0392 0.2219  -0.0873 560 LYS A C   
4371 O O   . LYS A 560 ? 0.9552 0.5712 0.5097 -0.0395 0.2259  -0.0691 560 LYS A O   
4372 C CB  . LYS A 560 ? 0.9185 0.5264 0.5417 -0.0255 0.2321  -0.1139 560 LYS A CB  
4373 C CG  . LYS A 560 ? 0.8371 0.4415 0.5032 -0.0171 0.2235  -0.1215 560 LYS A CG  
4374 C CD  . LYS A 560 ? 0.8321 0.4396 0.5324 -0.0083 0.2472  -0.1361 560 LYS A CD  
4375 C CE  . LYS A 560 ? 0.8780 0.4743 0.6121 0.0005  0.2427  -0.1473 560 LYS A CE  
4376 N NZ  . LYS A 560 ? 0.8355 0.4393 0.6114 0.0117  0.2637  -0.1583 560 LYS A NZ  
4377 N N   . GLU A 561 ? 1.0347 0.6337 0.5357 -0.0456 0.2289  -0.1018 561 GLU A N   
4378 C CA  . GLU A 561 ? 1.1396 0.7380 0.5927 -0.0524 0.2442  -0.0949 561 GLU A CA  
4379 C C   . GLU A 561 ? 1.1066 0.7121 0.5855 -0.0499 0.2732  -0.0934 561 GLU A C   
4380 O O   . GLU A 561 ? 1.1601 0.7707 0.6786 -0.0444 0.2872  -0.1098 561 GLU A O   
4381 C CB  . GLU A 561 ? 1.2423 0.8371 0.6520 -0.0594 0.2465  -0.1140 561 GLU A CB  
4382 C CG  . GLU A 561 ? 1.3301 0.9188 0.7096 -0.0646 0.2199  -0.1202 561 GLU A CG  
4383 C CD  . GLU A 561 ? 1.4951 1.0877 0.8394 -0.0723 0.2204  -0.1398 561 GLU A CD  
4384 O OE1 . GLU A 561 ? 1.4534 1.0533 0.7844 -0.0740 0.2401  -0.1429 561 GLU A OE1 
4385 O OE2 . GLU A 561 ? 1.5539 1.1433 0.8849 -0.0772 0.2014  -0.1531 561 GLU A OE2 
4386 N N   . ASP A 562 ? 1.1212 0.7311 0.5872 -0.0536 0.2786  -0.0716 562 ASP A N   
4387 C CA  . ASP A 562 ? 1.1688 0.7894 0.6648 -0.0537 0.3023  -0.0668 562 ASP A CA  
4388 C C   . ASP A 562 ? 1.0543 0.6829 0.6094 -0.0470 0.3074  -0.0679 562 ASP A C   
4389 O O   . ASP A 562 ? 1.0330 0.6747 0.6233 -0.0469 0.3265  -0.0695 562 ASP A O   
4390 C CB  . ASP A 562 ? 1.3056 0.9330 0.7992 -0.0559 0.3232  -0.0853 562 ASP A CB  
4391 C CG  . ASP A 562 ? 1.3875 1.0128 0.8231 -0.0639 0.3236  -0.0802 562 ASP A CG  
4392 O OD1 . ASP A 562 ? 1.4198 1.0419 0.8273 -0.0673 0.3135  -0.0564 562 ASP A OD1 
4393 O OD2 . ASP A 562 ? 1.3961 1.0241 0.8161 -0.0662 0.3339  -0.0994 562 ASP A OD2 
4394 N N   . ALA A 563 ? 1.0312 0.6620 0.6132 -0.0413 0.2809  -0.0647 563 ALA A N   
4395 C CA  . ALA A 563 ? 0.9505 0.5963 0.5929 -0.0352 0.2767  -0.0616 563 ALA A CA  
4396 C C   . ALA A 563 ? 0.9356 0.5863 0.5880 -0.0391 0.2739  -0.0404 563 ALA A C   
4397 O O   . ALA A 563 ? 0.9414 0.6074 0.6403 -0.0374 0.2786  -0.0396 563 ALA A O   
4398 C CB  . ALA A 563 ? 0.8723 0.5184 0.5376 -0.0283 0.2514  -0.0654 563 ALA A CB  
4399 N N   . LEU A 564 ? 0.9530 0.5918 0.5650 -0.0440 0.2655  -0.0237 564 LEU A N   
4400 C CA  . LEU A 564 ? 0.9403 0.5786 0.5603 -0.0475 0.2653  -0.0030 564 LEU A CA  
4401 C C   . LEU A 564 ? 0.9242 0.5573 0.5252 -0.0550 0.2937  0.0037  564 LEU A C   
4402 O O   . LEU A 564 ? 1.0059 0.6318 0.5640 -0.0579 0.3015  0.0022  564 LEU A O   
4403 C CB  . LEU A 564 ? 0.9580 0.5856 0.5486 -0.0471 0.2417  0.0142  564 LEU A CB  
4404 C CG  . LEU A 564 ? 0.9608 0.5941 0.5780 -0.0418 0.2148  0.0155  564 LEU A CG  
4405 C CD1 . LEU A 564 ? 1.0210 0.6455 0.6096 -0.0415 0.1958  0.0337  564 LEU A CD1 
4406 C CD2 . LEU A 564 ? 0.8869 0.5319 0.5554 -0.0409 0.2176  0.0169  564 LEU A CD2 
4407 N N   . ASN A 565 ? 0.9670 0.6066 0.6038 -0.0586 0.3064  0.0105  565 ASN A N   
4408 C CA  . ASN A 565 ? 0.9836 0.6222 0.6157 -0.0650 0.3234  0.0193  565 ASN A CA  
4409 C C   . ASN A 565 ? 1.0153 0.6392 0.6123 -0.0654 0.3093  0.0428  565 ASN A C   
4410 O O   . ASN A 565 ? 0.9513 0.5715 0.5672 -0.0644 0.2987  0.0563  565 ASN A O   
4411 C CB  . ASN A 565 ? 0.9469 0.5990 0.6339 -0.0694 0.3375  0.0169  565 ASN A CB  
4412 C CG  . ASN A 565 ? 1.0235 0.6761 0.7096 -0.0765 0.3578  0.0217  565 ASN A CG  
4413 O OD1 . ASN A 565 ? 1.0511 0.6926 0.6931 -0.0779 0.3598  0.0318  565 ASN A OD1 
4414 N ND2 . ASN A 565 ? 1.0017 0.6690 0.7365 -0.0817 0.3727  0.0146  565 ASN A ND2 
4415 N N   . LEU A 566 ? 1.0672 0.6849 0.6152 -0.0663 0.3087  0.0472  566 LEU A N   
4416 C CA  . LEU A 566 ? 1.1207 0.7290 0.6343 -0.0656 0.2956  0.0711  566 LEU A CA  
4417 C C   . LEU A 566 ? 1.1700 0.7772 0.6723 -0.0712 0.3138  0.0832  566 LEU A C   
4418 O O   . LEU A 566 ? 1.2720 0.8733 0.7406 -0.0707 0.3053  0.1042  566 LEU A O   
4419 C CB  . LEU A 566 ? 1.1266 0.7319 0.5892 -0.0631 0.2774  0.0698  566 LEU A CB  
4420 C CG  . LEU A 566 ? 1.0856 0.6892 0.5538 -0.0582 0.2564  0.0616  566 LEU A CG  
4421 C CD1 . LEU A 566 ? 1.1510 0.7538 0.5707 -0.0584 0.2427  0.0526  566 LEU A CD1 
4422 C CD2 . LEU A 566 ? 1.0487 0.6484 0.5348 -0.0537 0.2377  0.0821  566 LEU A CD2 
4423 N N   . LYS A 567 ? 1.1439 0.7582 0.6746 -0.0767 0.3385  0.0714  567 LYS A N   
4424 C CA  . LYS A 567 ? 1.1953 0.8087 0.7143 -0.0832 0.3585  0.0815  567 LYS A CA  
4425 C C   . LYS A 567 ? 1.2022 0.8061 0.7360 -0.0841 0.3557  0.1056  567 LYS A C   
4426 O O   . LYS A 567 ? 1.1041 0.7071 0.6790 -0.0822 0.3488  0.1057  567 LYS A O   
4427 C CB  . LYS A 567 ? 1.2336 0.8591 0.7872 -0.0888 0.3850  0.0615  567 LYS A CB  
4428 C CG  . LYS A 567 ? 1.3504 0.9858 0.8990 -0.0863 0.3884  0.0360  567 LYS A CG  
4429 C CD  . LYS A 567 ? 1.4205 1.0720 1.0148 -0.0897 0.4124  0.0164  567 LYS A CD  
4430 C CE  . LYS A 567 ? 1.4495 1.1109 1.0486 -0.0846 0.4136  -0.0088 567 LYS A CE  
4431 N NZ  . LYS A 567 ? 1.5181 1.1985 1.1630 -0.0865 0.4368  -0.0267 567 LYS A NZ  
4432 N N   . GLY A 568 ? 1.2524 0.8498 0.7523 -0.0871 0.3613  0.1260  568 GLY A N   
4433 C CA  . GLY A 568 ? 1.2364 0.8226 0.7453 -0.0869 0.3577  0.1517  568 GLY A CA  
4434 C C   . GLY A 568 ? 1.3212 0.9009 0.8060 -0.0785 0.3296  0.1724  568 GLY A C   
4435 O O   . GLY A 568 ? 1.3714 0.9420 0.8484 -0.0778 0.3266  0.1985  568 GLY A O   
4436 N N   . LEU A 569 ? 1.3595 0.9440 0.8354 -0.0721 0.3089  0.1621  569 LEU A N   
4437 C CA  . LEU A 569 ? 1.4252 1.0075 0.8747 -0.0644 0.2814  0.1806  569 LEU A CA  
4438 C C   . LEU A 569 ? 1.5981 1.1861 0.9855 -0.0655 0.2764  0.1872  569 LEU A C   
4439 O O   . LEU A 569 ? 1.6349 1.2213 0.9944 -0.0643 0.2699  0.2137  569 LEU A O   
4440 C CB  . LEU A 569 ? 1.3873 0.9726 0.8561 -0.0580 0.2613  0.1668  569 LEU A CB  
4441 C CG  . LEU A 569 ? 1.1779 0.7625 0.7059 -0.0574 0.2647  0.1556  569 LEU A CG  
4442 C CD1 . LEU A 569 ? 1.1155 0.7038 0.6537 -0.0514 0.2435  0.1450  569 LEU A CD1 
4443 C CD2 . LEU A 569 ? 1.1432 0.7196 0.7019 -0.0566 0.2666  0.1742  569 LEU A CD2 
4444 N N   . GLY A 570 ? 1.7949 1.3905 1.1608 -0.0680 0.2798  0.1628  570 GLY A N   
4445 C CA  . GLY A 570 ? 1.7172 1.3207 1.0253 -0.0710 0.2789  0.1622  570 GLY A CA  
4446 C C   . GLY A 570 ? 1.8106 1.4198 1.0809 -0.0654 0.2482  0.1746  570 GLY A C   
4447 O O   . GLY A 570 ? 1.7765 1.3936 1.0153 -0.0663 0.2382  0.1567  570 GLY A O   
4448 N N   . ASP A 571 ? 1.8395 1.4457 1.1159 -0.0597 0.2329  0.2045  571 ASP A N   
4449 C CA  . ASP A 571 ? 1.7924 1.4075 1.0379 -0.0534 0.2027  0.2219  571 ASP A CA  
4450 C C   . ASP A 571 ? 1.7405 1.3567 1.0056 -0.0472 0.1789  0.2099  571 ASP A C   
4451 O O   . ASP A 571 ? 1.7349 1.3607 0.9797 -0.0416 0.1519  0.2223  571 ASP A O   
4452 C CB  . ASP A 571 ? 1.8050 1.4161 1.0577 -0.0489 0.1966  0.2599  571 ASP A CB  
4453 C CG  . ASP A 571 ? 1.8629 1.4583 1.1769 -0.0467 0.2060  0.2644  571 ASP A CG  
4454 O OD1 . ASP A 571 ? 1.7575 1.3489 1.1071 -0.0476 0.2134  0.2394  571 ASP A OD1 
4455 O OD2 . ASP A 571 ? 1.8979 1.4853 1.2245 -0.0446 0.2059  0.2923  571 ASP A OD2 
4456 N N   . VAL A 572 ? 1.7122 1.3208 1.0168 -0.0480 0.1877  0.1874  572 VAL A N   
4457 C CA  . VAL A 572 ? 1.6408 1.2493 0.9680 -0.0425 0.1669  0.1785  572 VAL A CA  
4458 C C   . VAL A 572 ? 1.5517 1.1691 0.8387 -0.0446 0.1498  0.1608  572 VAL A C   
4459 O O   . VAL A 572 ? 1.5493 1.1684 0.8133 -0.0516 0.1628  0.1379  572 VAL A O   
4460 C CB  . VAL A 572 ? 1.5698 1.1703 0.9468 -0.0438 0.1822  0.1594  572 VAL A CB  
4461 C CG1 . VAL A 572 ? 1.4239 1.0252 0.8103 -0.0415 0.1652  0.1422  572 VAL A CG1 
4462 C CG2 . VAL A 572 ? 1.4606 1.0547 0.8845 -0.0403 0.1881  0.1764  572 VAL A CG2 
4463 N N   . ASN A 573 ? 1.5048 1.1289 0.7862 -0.0390 0.1205  0.1700  573 ASN A N   
4464 C CA  . ASN A 573 ? 1.4924 1.1261 0.7405 -0.0422 0.1005  0.1517  573 ASN A CA  
4465 C C   . ASN A 573 ? 1.4376 1.0621 0.7126 -0.0446 0.1023  0.1251  573 ASN A C   
4466 O O   . ASN A 573 ? 1.3988 1.0203 0.7053 -0.0394 0.0886  0.1298  573 ASN A O   
4467 C CB  . ASN A 573 ? 1.5029 1.1505 0.7389 -0.0355 0.0675  0.1722  573 ASN A CB  
4468 C CG  . ASN A 573 ? 1.5348 1.1954 0.7392 -0.0408 0.0442  0.1512  573 ASN A CG  
4469 O OD1 . ASN A 573 ? 1.5365 1.1940 0.7250 -0.0498 0.0541  0.1209  573 ASN A OD1 
4470 N ND2 . ASN A 573 ? 1.5688 1.2455 0.7680 -0.0354 0.0132  0.1662  573 ASN A ND2 
4471 N N   . VAL A 574 ? 1.4554 1.0763 0.7193 -0.0519 0.1199  0.0974  574 VAL A N   
4472 C CA  . VAL A 574 ? 1.4023 1.0143 0.6936 -0.0536 0.1255  0.0732  574 VAL A CA  
4473 C C   . VAL A 574 ? 1.3789 0.9988 0.6629 -0.0558 0.0990  0.0569  574 VAL A C   
4474 O O   . VAL A 574 ? 1.2821 0.9060 0.6140 -0.0535 0.0916  0.0443  574 VAL A O   
4475 C CB  . VAL A 574 ? 1.3676 0.9756 0.6613 -0.0586 0.1551  0.0499  574 VAL A CB  
4476 C CG1 . VAL A 574 ? 1.3751 0.9814 0.6899 -0.0573 0.1792  0.0645  574 VAL A CG1 
4477 C CG2 . VAL A 574 ? 1.3698 0.9856 0.6182 -0.0654 0.1553  0.0322  574 VAL A CG2 
4478 N N   . GLU A 575 ? 1.4415 1.0698 0.6757 -0.0605 0.0828  0.0557  575 GLU A N   
4479 C CA  . GLU A 575 ? 1.4355 1.0750 0.6685 -0.0646 0.0566  0.0376  575 GLU A CA  
4480 C C   . GLU A 575 ? 1.3061 0.9573 0.5809 -0.0573 0.0305  0.0545  575 GLU A C   
4481 O O   . GLU A 575 ? 1.1976 0.8545 0.5133 -0.0579 0.0201  0.0393  575 GLU A O   
4482 C CB  . GLU A 575 ? 1.5229 1.1761 0.6991 -0.0717 0.0437  0.0321  575 GLU A CB  
4483 C CG  . GLU A 575 ? 1.5960 1.2484 0.7485 -0.0781 0.0686  0.0104  575 GLU A CG  
4484 C CD  . GLU A 575 ? 1.7237 1.3974 0.8275 -0.0831 0.0564  0.0089  575 GLU A CD  
4485 O OE1 . GLU A 575 ? 1.7546 1.4449 0.8435 -0.0796 0.0304  0.0313  575 GLU A OE1 
4486 O OE2 . GLU A 575 ? 1.7684 1.4439 0.8505 -0.0897 0.0728  -0.0145 575 GLU A OE2 
4487 N N   . GLU A 576 ? 1.3044 0.9584 0.5713 -0.0500 0.0214  0.0868  576 GLU A N   
4488 C CA  . GLU A 576 ? 1.2849 0.9509 0.5927 -0.0418 -0.0020 0.1032  576 GLU A CA  
4489 C C   . GLU A 576 ? 1.2107 0.8692 0.5811 -0.0360 0.0110  0.1038  576 GLU A C   
4490 O O   . GLU A 576 ? 1.1784 0.8476 0.5913 -0.0323 -0.0047 0.1037  576 GLU A O   
4491 C CB  . GLU A 576 ? 1.3867 1.0560 0.6692 -0.0339 -0.0142 0.1386  576 GLU A CB  
4492 C CG  . GLU A 576 ? 1.4292 1.1162 0.7469 -0.0250 -0.0430 0.1546  576 GLU A CG  
4493 C CD  . GLU A 576 ? 1.5448 1.2373 0.8357 -0.0158 -0.0573 0.1901  576 GLU A CD  
4494 O OE1 . GLU A 576 ? 1.5724 1.2680 0.8305 -0.0170 -0.0452 0.1979  576 GLU A OE1 
4495 O OE2 . GLU A 576 ? 1.5854 1.2905 0.9074 -0.0058 -0.0788 0.2078  576 GLU A OE2 
4496 N N   . LEU A 577 ? 1.2050 0.8474 0.5821 -0.0360 0.0396  0.1034  577 LEU A N   
4497 C CA  . LEU A 577 ? 1.1224 0.7603 0.5561 -0.0315 0.0509  0.1035  577 LEU A CA  
4498 C C   . LEU A 577 ? 1.0360 0.6794 0.5031 -0.0348 0.0495  0.0771  577 LEU A C   
4499 O O   . LEU A 577 ? 0.9507 0.5971 0.4645 -0.0311 0.0490  0.0772  577 LEU A O   
4500 C CB  . LEU A 577 ? 1.1050 0.7275 0.5388 -0.0320 0.0809  0.1093  577 LEU A CB  
4501 C CG  . LEU A 577 ? 1.0995 0.7133 0.5498 -0.0254 0.0859  0.1372  577 LEU A CG  
4502 C CD1 . LEU A 577 ? 1.1118 0.7131 0.5663 -0.0287 0.1167  0.1388  577 LEU A CD1 
4503 C CD2 . LEU A 577 ? 0.9822 0.6030 0.4880 -0.0195 0.0748  0.1380  577 LEU A CD2 
4504 N N   . PHE A 578 ? 1.0274 0.6709 0.4710 -0.0419 0.0502  0.0545  578 PHE A N   
4505 C CA  . PHE A 578 ? 1.0311 0.6764 0.5054 -0.0447 0.0492  0.0313  578 PHE A CA  
4506 C C   . PHE A 578 ? 1.0329 0.6869 0.4944 -0.0509 0.0272  0.0173  578 PHE A C   
4507 O O   . PHE A 578 ? 1.0388 0.6904 0.5195 -0.0548 0.0276  -0.0032 578 PHE A O   
4508 C CB  . PHE A 578 ? 1.0228 0.6571 0.4950 -0.0471 0.0744  0.0130  578 PHE A CB  
4509 C CG  . PHE A 578 ? 0.9781 0.6089 0.4833 -0.0421 0.0939  0.0205  578 PHE A CG  
4510 C CD1 . PHE A 578 ? 0.9123 0.5474 0.4662 -0.0386 0.0930  0.0162  578 PHE A CD1 
4511 C CD2 . PHE A 578 ? 0.9813 0.6056 0.4683 -0.0420 0.1130  0.0319  578 PHE A CD2 
4512 C CE1 . PHE A 578 ? 0.8360 0.4717 0.4201 -0.0353 0.1087  0.0211  578 PHE A CE1 
4513 C CE2 . PHE A 578 ? 0.9403 0.5635 0.4611 -0.0393 0.1306  0.0365  578 PHE A CE2 
4514 C CZ  . PHE A 578 ? 0.8768 0.5069 0.4463 -0.0361 0.1275  0.0301  578 PHE A CZ  
4515 N N   . GLY A 579 ? 1.0650 0.7297 0.4972 -0.0520 0.0075  0.0285  579 GLY A N   
4516 C CA  . GLY A 579 ? 1.0460 0.7234 0.4696 -0.0593 -0.0156 0.0148  579 GLY A CA  
4517 C C   . GLY A 579 ? 1.0400 0.7257 0.5159 -0.0592 -0.0275 0.0099  579 GLY A C   
4518 O O   . GLY A 579 ? 1.0001 0.6925 0.5099 -0.0515 -0.0321 0.0278  579 GLY A O   
4519 N N   . ILE A 580 ? 0.9944 0.6780 0.4771 -0.0680 -0.0304 -0.0148 580 ILE A N   
4520 C CA  . ILE A 580 ? 0.9640 0.6548 0.4919 -0.0706 -0.0411 -0.0208 580 ILE A CA  
4521 C C   . ILE A 580 ? 0.9324 0.6392 0.4469 -0.0811 -0.0652 -0.0325 580 ILE A C   
4522 O O   . ILE A 580 ? 0.9564 0.6562 0.4488 -0.0917 -0.0643 -0.0565 580 ILE A O   
4523 C CB  . ILE A 580 ? 0.9805 0.6537 0.5333 -0.0725 -0.0236 -0.0382 580 ILE A CB  
4524 C CG1 . ILE A 580 ? 0.9721 0.6355 0.5415 -0.0624 -0.0026 -0.0267 580 ILE A CG1 
4525 C CG2 . ILE A 580 ? 0.9503 0.6297 0.5446 -0.0769 -0.0344 -0.0430 580 ILE A CG2 
4526 C CD1 . ILE A 580 ? 0.9689 0.6187 0.5666 -0.0618 0.0122  -0.0396 580 ILE A CD1 
4527 N N   . SER A 581 ? 0.9395 0.6688 0.4692 -0.0785 -0.0866 -0.0169 581 SER A N   
4528 C CA  . SER A 581 ? 0.9459 0.6968 0.4692 -0.0886 -0.1124 -0.0271 581 SER A CA  
4529 C C   . SER A 581 ? 0.9001 0.6567 0.4730 -0.0959 -0.1177 -0.0390 581 SER A C   
4530 O O   . SER A 581 ? 0.8458 0.6042 0.4608 -0.0889 -0.1127 -0.0262 581 SER A O   
4531 C CB  . SER A 581 ? 0.9284 0.7045 0.4442 -0.0810 -0.1343 -0.0025 581 SER A CB  
4532 O OG  . SER A 581 ? 0.9665 0.7703 0.4955 -0.0893 -0.1614 -0.0101 581 SER A OG  
4533 N N   . LYS A 582 ? 0.8966 0.6558 0.4634 -0.1110 -0.1268 -0.0642 582 LYS A N   
4534 C CA  . LYS A 582 ? 0.8551 0.6181 0.4682 -0.1203 -0.1308 -0.0759 582 LYS A CA  
4535 C C   . LYS A 582 ? 0.8685 0.6652 0.5151 -0.1190 -0.1532 -0.0616 582 LYS A C   
4536 O O   . LYS A 582 ? 0.8518 0.6525 0.5456 -0.1187 -0.1498 -0.0569 582 LYS A O   
4537 C CB  . LYS A 582 ? 0.9085 0.6638 0.5075 -0.1384 -0.1338 -0.1084 582 LYS A CB  
4538 C CG  . LYS A 582 ? 0.8813 0.6393 0.5282 -0.1505 -0.1376 -0.1208 582 LYS A CG  
4539 C CD  . LYS A 582 ? 0.9498 0.6962 0.5838 -0.1697 -0.1388 -0.1551 582 LYS A CD  
4540 C CE  . LYS A 582 ? 0.8880 0.6347 0.5722 -0.1832 -0.1407 -0.1661 582 LYS A CE  
4541 N NZ  . LYS A 582 ? 0.9993 0.7217 0.6773 -0.2004 -0.1330 -0.1999 582 LYS A NZ  
4542 N N   . GLU A 583 ? 0.8690 0.6915 0.4918 -0.1179 -0.1760 -0.0541 583 GLU A N   
4543 C CA  . GLU A 583 ? 0.8783 0.7359 0.5353 -0.1137 -0.1983 -0.0383 583 GLU A CA  
4544 C C   . GLU A 583 ? 0.8192 0.6744 0.5103 -0.0968 -0.1864 -0.0125 583 GLU A C   
4545 O O   . GLU A 583 ? 0.7974 0.6697 0.5382 -0.0959 -0.1905 -0.0073 583 GLU A O   
4546 C CB  . GLU A 583 ? 0.9685 0.8522 0.5881 -0.1115 -0.2242 -0.0297 583 GLU A CB  
4547 C CG  . GLU A 583 ? 1.0742 0.9589 0.6471 -0.1281 -0.2341 -0.0565 583 GLU A CG  
4548 C CD  . GLU A 583 ? 1.2923 1.1979 0.8139 -0.1238 -0.2558 -0.0440 583 GLU A CD  
4549 O OE1 . GLU A 583 ? 1.3094 1.2115 0.8172 -0.1065 -0.2520 -0.0143 583 GLU A OE1 
4550 O OE2 . GLU A 583 ? 1.3767 1.3021 0.8712 -0.1383 -0.2765 -0.0635 583 GLU A OE2 
4551 N N   . PHE A 584 ? 0.8375 0.6722 0.5034 -0.0842 -0.1704 0.0026  584 PHE A N   
4552 C CA  . PHE A 584 ? 0.7923 0.6234 0.4895 -0.0696 -0.1583 0.0242  584 PHE A CA  
4553 C C   . PHE A 584 ? 0.7487 0.5679 0.4852 -0.0733 -0.1404 0.0155  584 PHE A C   
4554 O O   . PHE A 584 ? 0.7030 0.5353 0.4827 -0.0689 -0.1403 0.0242  584 PHE A O   
4555 C CB  . PHE A 584 ? 0.7889 0.5982 0.4523 -0.0584 -0.1425 0.0390  584 PHE A CB  
4556 C CG  . PHE A 584 ? 0.7667 0.5684 0.4624 -0.0457 -0.1269 0.0564  584 PHE A CG  
4557 C CD1 . PHE A 584 ? 0.7536 0.5711 0.4706 -0.0336 -0.1366 0.0782  584 PHE A CD1 
4558 C CD2 . PHE A 584 ? 0.7352 0.5150 0.4416 -0.0460 -0.1031 0.0499  584 PHE A CD2 
4559 C CE1 . PHE A 584 ? 0.7256 0.5350 0.4731 -0.0233 -0.1211 0.0905  584 PHE A CE1 
4560 C CE2 . PHE A 584 ? 0.7281 0.5034 0.4630 -0.0363 -0.0897 0.0627  584 PHE A CE2 
4561 C CZ  . PHE A 584 ? 0.6924 0.4814 0.4473 -0.0256 -0.0978 0.0817  584 PHE A CZ  
4562 N N   . TRP A 585 ? 0.7557 0.5501 0.4775 -0.0809 -0.1248 -0.0014 585 TRP A N   
4563 C CA  . TRP A 585 ? 0.7653 0.5459 0.5187 -0.0826 -0.1071 -0.0059 585 TRP A CA  
4564 C C   . TRP A 585 ? 0.7154 0.5090 0.5054 -0.0947 -0.1148 -0.0166 585 TRP A C   
4565 O O   . TRP A 585 ? 0.6794 0.4694 0.5015 -0.0946 -0.1031 -0.0135 585 TRP A O   
4566 C CB  . TRP A 585 ? 0.7561 0.5066 0.4850 -0.0845 -0.0882 -0.0177 585 TRP A CB  
4567 C CG  . TRP A 585 ? 0.7796 0.5188 0.4913 -0.0720 -0.0744 -0.0041 585 TRP A CG  
4568 C CD1 . TRP A 585 ? 0.8061 0.5390 0.4770 -0.0682 -0.0727 -0.0010 585 TRP A CD1 
4569 C CD2 . TRP A 585 ? 0.7594 0.4943 0.4946 -0.0628 -0.0600 0.0085  585 TRP A CD2 
4570 N NE1 . TRP A 585 ? 0.7930 0.5164 0.4643 -0.0577 -0.0570 0.0127  585 TRP A NE1 
4571 C CE2 . TRP A 585 ? 0.7399 0.4650 0.4505 -0.0544 -0.0499 0.0177  585 TRP A CE2 
4572 C CE3 . TRP A 585 ? 0.7063 0.4451 0.4794 -0.0621 -0.0541 0.0121  585 TRP A CE3 
4573 C CZ2 . TRP A 585 ? 0.7297 0.4492 0.4555 -0.0461 -0.0350 0.0282  585 TRP A CZ2 
4574 C CZ3 . TRP A 585 ? 0.7550 0.4892 0.5387 -0.0533 -0.0400 0.0224  585 TRP A CZ3 
4575 C CH2 . TRP A 585 ? 0.7493 0.4741 0.5110 -0.0458 -0.0311 0.0295  585 TRP A CH2 
4576 N N   . GLU A 586 ? 0.7026 0.5125 0.4884 -0.1062 -0.1339 -0.0293 586 GLU A N   
4577 C CA  . GLU A 586 ? 0.7020 0.5289 0.5288 -0.1184 -0.1418 -0.0380 586 GLU A CA  
4578 C C   . GLU A 586 ? 0.7159 0.5713 0.5831 -0.1103 -0.1484 -0.0205 586 GLU A C   
4579 O O   . GLU A 586 ? 0.6665 0.5272 0.5735 -0.1150 -0.1407 -0.0205 586 GLU A O   
4580 C CB  . GLU A 586 ? 0.7916 0.6329 0.6059 -0.1338 -0.1622 -0.0576 586 GLU A CB  
4581 C CG  . GLU A 586 ? 0.8275 0.6389 0.6166 -0.1461 -0.1520 -0.0815 586 GLU A CG  
4582 C CD  . GLU A 586 ? 0.9279 0.7542 0.7062 -0.1639 -0.1716 -0.1050 586 GLU A CD  
4583 O OE1 . GLU A 586 ? 0.8935 0.7510 0.6593 -0.1629 -0.1952 -0.1009 586 GLU A OE1 
4584 O OE2 . GLU A 586 ? 1.0139 0.8206 0.7972 -0.1789 -0.1639 -0.1276 586 GLU A OE2 
4585 N N   . LYS A 587 ? 0.6621 0.5353 0.5201 -0.0979 -0.1612 -0.0048 587 LYS A N   
4586 C CA  . LYS A 587 ? 0.6417 0.5398 0.5407 -0.0875 -0.1653 0.0120  587 LYS A CA  
4587 C C   . LYS A 587 ? 0.5996 0.4796 0.5126 -0.0775 -0.1409 0.0227  587 LYS A C   
4588 O O   . LYS A 587 ? 0.5978 0.4921 0.5526 -0.0753 -0.1354 0.0278  587 LYS A O   
4589 C CB  . LYS A 587 ? 0.6698 0.5875 0.5547 -0.0750 -0.1848 0.0281  587 LYS A CB  
4590 C CG  . LYS A 587 ? 0.7883 0.7264 0.6503 -0.0845 -0.2114 0.0183  587 LYS A CG  
4591 C CD  . LYS A 587 ? 0.9167 0.8733 0.7606 -0.0698 -0.2309 0.0394  587 LYS A CD  
4592 C CE  . LYS A 587 ? 1.0040 0.9785 0.8099 -0.0794 -0.2571 0.0298  587 LYS A CE  
4593 N NZ  . LYS A 587 ? 1.0427 1.0509 0.8826 -0.0952 -0.2770 0.0116  587 LYS A NZ  
4594 N N   . GLU A 588 ? 0.6218 0.4726 0.5008 -0.0721 -0.1259 0.0248  588 GLU A N   
4595 C CA  . GLU A 588 ? 0.6199 0.4558 0.5098 -0.0635 -0.1044 0.0333  588 GLU A CA  
4596 C C   . GLU A 588 ? 0.5756 0.4071 0.4917 -0.0726 -0.0913 0.0250  588 GLU A C   
4597 O O   . GLU A 588 ? 0.5412 0.3792 0.4852 -0.0684 -0.0806 0.0315  588 GLU A O   
4598 C CB  . GLU A 588 ? 0.6377 0.4462 0.4879 -0.0581 -0.0920 0.0349  588 GLU A CB  
4599 C CG  . GLU A 588 ? 0.6086 0.4056 0.4676 -0.0485 -0.0730 0.0444  588 GLU A CG  
4600 C CD  . GLU A 588 ? 0.6181 0.4268 0.4931 -0.0360 -0.0756 0.0607  588 GLU A CD  
4601 O OE1 . GLU A 588 ? 0.5896 0.4119 0.4600 -0.0317 -0.0925 0.0689  588 GLU A OE1 
4602 O OE2 . GLU A 588 ? 0.5517 0.3558 0.4446 -0.0304 -0.0606 0.0651  588 GLU A OE2 
4603 N N   . VAL A 589 ? 0.5875 0.4065 0.4937 -0.0851 -0.0905 0.0106  589 VAL A N   
4604 C CA  . VAL A 589 ? 0.5956 0.4072 0.5245 -0.0936 -0.0774 0.0059  589 VAL A CA  
4605 C C   . VAL A 589 ? 0.5873 0.4263 0.5589 -0.1003 -0.0830 0.0066  589 VAL A C   
4606 O O   . VAL A 589 ? 0.5985 0.4392 0.5939 -0.1018 -0.0694 0.0107  589 VAL A O   
4607 C CB  . VAL A 589 ? 0.6778 0.4660 0.5896 -0.1049 -0.0745 -0.0089 589 VAL A CB  
4608 C CG1 . VAL A 589 ? 0.7162 0.4787 0.5926 -0.0971 -0.0645 -0.0094 589 VAL A CG1 
4609 C CG2 . VAL A 589 ? 0.6840 0.4834 0.5919 -0.1163 -0.0928 -0.0226 589 VAL A CG2 
4610 N N   . GLU A 590 ? 0.5618 0.4250 0.5440 -0.1048 -0.1030 0.0023  590 GLU A N   
4611 C CA  . GLU A 590 ? 0.5190 0.4139 0.5476 -0.1101 -0.1090 0.0030  590 GLU A CA  
4612 C C   . GLU A 590 ? 0.5694 0.4775 0.6224 -0.0965 -0.0995 0.0173  590 GLU A C   
4613 O O   . GLU A 590 ? 0.5539 0.4736 0.6413 -0.1008 -0.0883 0.0179  590 GLU A O   
4614 C CB  . GLU A 590 ? 0.5745 0.4979 0.6092 -0.1141 -0.1355 -0.0023 590 GLU A CB  
4615 C CG  . GLU A 590 ? 0.7292 0.6477 0.7531 -0.1326 -0.1453 -0.0218 590 GLU A CG  
4616 C CD  . GLU A 590 ? 0.8089 0.7641 0.8454 -0.1384 -0.1734 -0.0281 590 GLU A CD  
4617 O OE1 . GLU A 590 ? 0.8328 0.8194 0.8957 -0.1276 -0.1843 -0.0154 590 GLU A OE1 
4618 O OE2 . GLU A 590 ? 0.8597 0.8132 0.8811 -0.1534 -0.1848 -0.0462 590 GLU A OE2 
4619 N N   . GLU A 591 ? 0.5200 0.4251 0.5556 -0.0807 -0.1020 0.0282  591 GLU A N   
4620 C CA  . GLU A 591 ? 0.5360 0.4512 0.5966 -0.0678 -0.0921 0.0395  591 GLU A CA  
4621 C C   . GLU A 591 ? 0.5371 0.4329 0.5945 -0.0682 -0.0677 0.0393  591 GLU A C   
4622 O O   . GLU A 591 ? 0.5427 0.4508 0.6299 -0.0654 -0.0557 0.0419  591 GLU A O   
4623 C CB  . GLU A 591 ? 0.5039 0.4166 0.5473 -0.0514 -0.0999 0.0522  591 GLU A CB  
4624 C CG  . GLU A 591 ? 0.5363 0.4761 0.5902 -0.0475 -0.1256 0.0573  591 GLU A CG  
4625 C CD  . GLU A 591 ? 0.6195 0.5956 0.7304 -0.0475 -0.1312 0.0577  591 GLU A CD  
4626 O OE1 . GLU A 591 ? 0.5645 0.5446 0.7061 -0.0398 -0.1154 0.0624  591 GLU A OE1 
4627 O OE2 . GLU A 591 ? 0.5962 0.5984 0.7228 -0.0561 -0.1509 0.0516  591 GLU A OE2 
4628 N N   . ILE A 592 ? 0.4944 0.3620 0.5166 -0.0713 -0.0600 0.0358  592 ILE A N   
4629 C CA  . ILE A 592 ? 0.5437 0.3963 0.5619 -0.0720 -0.0397 0.0363  592 ILE A CA  
4630 C C   . ILE A 592 ? 0.5516 0.4123 0.5941 -0.0849 -0.0323 0.0322  592 ILE A C   
4631 O O   . ILE A 592 ? 0.5464 0.4130 0.6041 -0.0848 -0.0174 0.0349  592 ILE A O   
4632 C CB  . ILE A 592 ? 0.5364 0.3601 0.5159 -0.0714 -0.0352 0.0342  592 ILE A CB  
4633 C CG1 . ILE A 592 ? 0.5870 0.4030 0.5430 -0.0598 -0.0392 0.0392  592 ILE A CG1 
4634 C CG2 . ILE A 592 ? 0.5492 0.3610 0.5251 -0.0720 -0.0175 0.0356  592 ILE A CG2 
4635 C CD1 . ILE A 592 ? 0.5901 0.3817 0.5102 -0.0603 -0.0366 0.0349  592 ILE A CD1 
4636 N N   . ASP A 593 ? 0.5394 0.4004 0.5853 -0.0971 -0.0416 0.0248  593 ASP A N   
4637 C CA  . ASP A 593 ? 0.5058 0.3728 0.5768 -0.1114 -0.0343 0.0215  593 ASP A CA  
4638 C C   . ASP A 593 ? 0.5828 0.4812 0.6949 -0.1112 -0.0300 0.0243  593 ASP A C   
4639 O O   . ASP A 593 ? 0.5565 0.4574 0.6807 -0.1146 -0.0125 0.0275  593 ASP A O   
4640 C CB  . ASP A 593 ? 0.5797 0.4448 0.6522 -0.1248 -0.0479 0.0106  593 ASP A CB  
4641 C CG  . ASP A 593 ? 0.6410 0.4979 0.7301 -0.1414 -0.0371 0.0071  593 ASP A CG  
4642 O OD1 . ASP A 593 ? 0.6490 0.5160 0.7603 -0.1446 -0.0229 0.0134  593 ASP A OD1 
4643 O OD2 . ASP A 593 ? 0.6904 0.5296 0.7698 -0.1518 -0.0418 -0.0023 593 ASP A OD2 
4644 N N   . LYS A 594 ? 0.5181 0.4423 0.6520 -0.1065 -0.0458 0.0235  594 LYS A N   
4645 C CA  . LYS A 594 ? 0.4848 0.4415 0.6643 -0.1045 -0.0423 0.0253  594 LYS A CA  
4646 C C   . LYS A 594 ? 0.5081 0.4623 0.6891 -0.0936 -0.0229 0.0311  594 LYS A C   
4647 O O   . LYS A 594 ? 0.4565 0.4270 0.6667 -0.0975 -0.0077 0.0302  594 LYS A O   
4648 C CB  . LYS A 594 ? 0.4957 0.4788 0.6948 -0.0963 -0.0648 0.0266  594 LYS A CB  
4649 C CG  . LYS A 594 ? 0.5461 0.5422 0.7526 -0.1095 -0.0848 0.0177  594 LYS A CG  
4650 C CD  . LYS A 594 ? 0.5728 0.6065 0.8113 -0.1020 -0.1067 0.0204  594 LYS A CD  
4651 C CE  . LYS A 594 ? 0.4906 0.5162 0.6998 -0.0834 -0.1190 0.0312  594 LYS A CE  
4652 N NZ  . LYS A 594 ? 0.5626 0.6201 0.7863 -0.0804 -0.1486 0.0329  594 LYS A NZ  
4653 N N   . TYR A 595 ? 0.5058 0.4402 0.6557 -0.0813 -0.0220 0.0357  595 TYR A N   
4654 C CA  . TYR A 595 ? 0.5073 0.4396 0.6593 -0.0717 -0.0049 0.0385  595 TYR A CA  
4655 C C   . TYR A 595 ? 0.5088 0.4301 0.6477 -0.0807 0.0150  0.0365  595 TYR A C   
4656 O O   . TYR A 595 ? 0.5410 0.4761 0.7000 -0.0821 0.0312  0.0347  595 TYR A O   
4657 C CB  . TYR A 595 ? 0.4715 0.3849 0.5950 -0.0583 -0.0092 0.0433  595 TYR A CB  
4658 C CG  . TYR A 595 ? 0.5025 0.4083 0.6229 -0.0508 0.0088  0.0433  595 TYR A CG  
4659 C CD1 . TYR A 595 ? 0.4722 0.3920 0.6236 -0.0405 0.0146  0.0441  595 TYR A CD1 
4660 C CD2 . TYR A 595 ? 0.5270 0.4125 0.6156 -0.0539 0.0196  0.0415  595 TYR A CD2 
4661 C CE1 . TYR A 595 ? 0.4979 0.4095 0.6469 -0.0353 0.0322  0.0407  595 TYR A CE1 
4662 C CE2 . TYR A 595 ? 0.5074 0.3885 0.5929 -0.0490 0.0347  0.0390  595 TYR A CE2 
4663 C CZ  . TYR A 595 ? 0.5028 0.3960 0.6174 -0.0407 0.0417  0.0374  595 TYR A CZ  
4664 O OH  . TYR A 595 ? 0.6007 0.4881 0.7121 -0.0375 0.0578  0.0315  595 TYR A OH  
4665 N N   . LEU A 596 ? 0.4661 0.3637 0.5718 -0.0866 0.0142  0.0373  596 LEU A N   
4666 C CA  . LEU A 596 ? 0.5439 0.4311 0.6349 -0.0938 0.0305  0.0390  596 LEU A CA  
4667 C C   . LEU A 596 ? 0.5468 0.4496 0.6643 -0.1073 0.0398  0.0385  596 LEU A C   
4668 O O   . LEU A 596 ? 0.5523 0.4606 0.6704 -0.1111 0.0574  0.0403  596 LEU A O   
4669 C CB  . LEU A 596 ? 0.5757 0.4350 0.6323 -0.0962 0.0261  0.0411  596 LEU A CB  
4670 C CG  . LEU A 596 ? 0.5344 0.3765 0.5620 -0.0848 0.0212  0.0416  596 LEU A CG  
4671 C CD1 . LEU A 596 ? 0.6464 0.4639 0.6487 -0.0881 0.0170  0.0419  596 LEU A CD1 
4672 C CD2 . LEU A 596 ? 0.5556 0.3987 0.5742 -0.0784 0.0341  0.0428  596 LEU A CD2 
4673 N N   . GLU A 597 ? 0.5164 0.4278 0.6553 -0.1159 0.0289  0.0356  597 GLU A N   
4674 C CA  . GLU A 597 ? 0.5667 0.4927 0.7342 -0.1308 0.0388  0.0349  597 GLU A CA  
4675 C C   . GLU A 597 ? 0.5507 0.5074 0.7534 -0.1284 0.0510  0.0327  597 GLU A C   
4676 O O   . GLU A 597 ? 0.5660 0.5302 0.7772 -0.1373 0.0704  0.0344  597 GLU A O   
4677 C CB  . GLU A 597 ? 0.5275 0.4583 0.7140 -0.1417 0.0230  0.0292  597 GLU A CB  
4678 C CG  . GLU A 597 ? 0.5946 0.5556 0.8290 -0.1542 0.0280  0.0253  597 GLU A CG  
4679 C CD  . GLU A 597 ? 0.7369 0.6956 0.9850 -0.1709 0.0172  0.0188  597 GLU A CD  
4680 O OE1 . GLU A 597 ? 0.7778 0.7142 0.9992 -0.1706 0.0029  0.0153  597 GLU A OE1 
4681 O OE2 . GLU A 597 ? 0.7981 0.7771 1.0844 -0.1854 0.0246  0.0158  597 GLU A OE2 
4682 N N   . ASP A 598 ? 0.4997 0.4741 0.7232 -0.1158 0.0411  0.0297  598 ASP A N   
4683 C CA  . ASP A 598 ? 0.5274 0.5302 0.7892 -0.1115 0.0540  0.0264  598 ASP A CA  
4684 C C   . ASP A 598 ? 0.4940 0.4880 0.7353 -0.1051 0.0739  0.0260  598 ASP A C   
4685 O O   . ASP A 598 ? 0.5247 0.5319 0.7786 -0.1116 0.0949  0.0231  598 ASP A O   
4686 C CB  . ASP A 598 ? 0.5182 0.5416 0.8118 -0.0979 0.0373  0.0253  598 ASP A CB  
4687 C CG  . ASP A 598 ? 0.5924 0.6459 0.9335 -0.0920 0.0516  0.0212  598 ASP A CG  
4688 O OD1 . ASP A 598 ? 0.5900 0.6605 0.9548 -0.1045 0.0683  0.0172  598 ASP A OD1 
4689 O OD2 . ASP A 598 ? 0.5230 0.5824 0.8792 -0.0751 0.0480  0.0221  598 ASP A OD2 
4690 N N   . GLN A 599 ? 0.4918 0.4643 0.7001 -0.0942 0.0683  0.0279  599 GLN A N   
4691 C CA  . GLN A 599 ? 0.4719 0.4407 0.6686 -0.0866 0.0841  0.0242  599 GLN A CA  
4692 C C   . GLN A 599 ? 0.5224 0.4774 0.6817 -0.0952 0.0981  0.0255  599 GLN A C   
4693 O O   . GLN A 599 ? 0.4945 0.4557 0.6499 -0.0947 0.1157  0.0196  599 GLN A O   
4694 C CB  . GLN A 599 ? 0.4836 0.4372 0.6667 -0.0717 0.0728  0.0254  599 GLN A CB  
4695 C CG  . GLN A 599 ? 0.5088 0.4780 0.7297 -0.0598 0.0618  0.0263  599 GLN A CG  
4696 C CD  . GLN A 599 ? 0.5349 0.5240 0.7944 -0.0540 0.0793  0.0192  599 GLN A CD  
4697 O OE1 . GLN A 599 ? 0.5150 0.4955 0.7644 -0.0502 0.0952  0.0129  599 GLN A OE1 
4698 N NE2 . GLN A 599 ? 0.5358 0.5530 0.8420 -0.0539 0.0773  0.0183  599 GLN A NE2 
4699 N N   . VAL A 600 ? 0.4985 0.4350 0.6299 -0.1025 0.0908  0.0328  600 VAL A N   
4700 C CA  . VAL A 600 ? 0.5220 0.4472 0.6197 -0.1092 0.1021  0.0376  600 VAL A CA  
4701 C C   . VAL A 600 ? 0.5310 0.4606 0.6346 -0.1244 0.1117  0.0440  600 VAL A C   
4702 O O   . VAL A 600 ? 0.5448 0.4767 0.6307 -0.1308 0.1276  0.0476  600 VAL A O   
4703 C CB  . VAL A 600 ? 0.5527 0.4516 0.6137 -0.1042 0.0901  0.0430  600 VAL A CB  
4704 C CG1 . VAL A 600 ? 0.5339 0.4278 0.5624 -0.1054 0.1006  0.0460  600 VAL A CG1 
4705 C CG2 . VAL A 600 ? 0.5516 0.4446 0.6132 -0.0913 0.0778  0.0383  600 VAL A CG2 
4706 N N   . ASN A 601 ? 0.5171 0.4480 0.6438 -0.1314 0.1028  0.0455  601 ASN A N   
4707 C CA  . ASN A 601 ? 0.5464 0.4874 0.6939 -0.1473 0.1143  0.0489  601 ASN A CA  
4708 C C   . ASN A 601 ? 0.5489 0.4706 0.6616 -0.1554 0.1253  0.0614  601 ASN A C   
4709 O O   . ASN A 601 ? 0.5394 0.4348 0.6251 -0.1525 0.1145  0.0681  601 ASN A O   
4710 C CB  . ASN A 601 ? 0.5291 0.5028 0.7135 -0.1485 0.1295  0.0408  601 ASN A CB  
4711 C CG  . ASN A 601 ? 0.6110 0.6007 0.8281 -0.1650 0.1402  0.0422  601 ASN A CG  
4712 O OD1 . ASN A 601 ? 0.6448 0.6201 0.8606 -0.1760 0.1342  0.0484  601 ASN A OD1 
4713 N ND2 . ASN A 601 ? 0.5705 0.5897 0.8200 -0.1676 0.1579  0.0354  601 ASN A ND2 
4714 N N   . ALA A 602 ? 0.5114 0.4451 0.6220 -0.1645 0.1466  0.0656  602 ALA A N   
4715 C CA  . ALA A 602 ? 0.5677 0.4839 0.6457 -0.1729 0.1566  0.0816  602 ALA A CA  
4716 C C   . ALA A 602 ? 0.6033 0.5059 0.6358 -0.1625 0.1526  0.0871  602 ALA A C   
4717 O O   . ALA A 602 ? 0.5942 0.4796 0.5982 -0.1660 0.1552  0.1030  602 ALA A O   
4718 C CB  . ALA A 602 ? 0.6043 0.5399 0.6903 -0.1862 0.1817  0.0851  602 ALA A CB  
4719 N N   . ASP A 603 ? 0.5034 0.4136 0.5307 -0.1499 0.1464  0.0753  603 ASP A N   
4720 C CA  . ASP A 603 ? 0.5738 0.4754 0.5627 -0.1414 0.1422  0.0781  603 ASP A CA  
4721 C C   . ASP A 603 ? 0.5369 0.4167 0.5169 -0.1307 0.1220  0.0788  603 ASP A C   
4722 O O   . ASP A 603 ? 0.5075 0.3829 0.4626 -0.1225 0.1169  0.0785  603 ASP A O   
4723 C CB  . ASP A 603 ? 0.5632 0.4857 0.5507 -0.1364 0.1513  0.0631  603 ASP A CB  
4724 C CG  . ASP A 603 ? 0.6693 0.6124 0.6529 -0.1471 0.1741  0.0622  603 ASP A CG  
4725 O OD1 . ASP A 603 ? 0.6610 0.6001 0.6149 -0.1548 0.1809  0.0767  603 ASP A OD1 
4726 O OD2 . ASP A 603 ? 0.6414 0.6045 0.6519 -0.1476 0.1860  0.0478  603 ASP A OD2 
4727 N N   . LEU A 604 ? 0.5444 0.4121 0.5441 -0.1317 0.1111  0.0786  604 LEU A N   
4728 C CA  . LEU A 604 ? 0.5437 0.3905 0.5334 -0.1227 0.0941  0.0781  604 LEU A CA  
4729 C C   . LEU A 604 ? 0.5627 0.3867 0.5280 -0.1234 0.0927  0.0926  604 LEU A C   
4730 O O   . LEU A 604 ? 0.5737 0.3877 0.5445 -0.1333 0.0981  0.1025  604 LEU A O   
4731 C CB  . LEU A 604 ? 0.5574 0.4007 0.5732 -0.1250 0.0831  0.0713  604 LEU A CB  
4732 C CG  . LEU A 604 ? 0.5212 0.3447 0.5266 -0.1169 0.0668  0.0679  604 LEU A CG  
4733 C CD1 . LEU A 604 ? 0.5656 0.3937 0.5610 -0.1040 0.0616  0.0612  604 LEU A CD1 
4734 C CD2 . LEU A 604 ? 0.6070 0.4303 0.6359 -0.1231 0.0566  0.0610  604 LEU A CD2 
4735 N N   . PRO A 605 ? 0.5701 0.3856 0.5116 -0.1132 0.0863  0.0950  605 PRO A N   
4736 C CA  . PRO A 605 ? 0.5815 0.3765 0.5043 -0.1114 0.0843  0.1105  605 PRO A CA  
4737 C C   . PRO A 605 ? 0.5863 0.3552 0.5209 -0.1126 0.0768  0.1110  605 PRO A C   
4738 O O   . PRO A 605 ? 0.5834 0.3493 0.5293 -0.1100 0.0680  0.0979  605 PRO A O   
4739 C CB  . PRO A 605 ? 0.5789 0.3771 0.4814 -0.0992 0.0775  0.1086  605 PRO A CB  
4740 C CG  . PRO A 605 ? 0.5585 0.3814 0.4638 -0.0986 0.0819  0.0946  605 PRO A CG  
4741 C CD  . PRO A 605 ? 0.5453 0.3725 0.4780 -0.1035 0.0832  0.0848  605 PRO A CD  
4742 N N   . TYR A 606 ? 0.6023 0.3514 0.5328 -0.1167 0.0808  0.1265  606 TYR A N   
4743 C CA  . TYR A 606 ? 0.5936 0.3146 0.5369 -0.1195 0.0762  0.1252  606 TYR A CA  
4744 C C   . TYR A 606 ? 0.6348 0.3429 0.5720 -0.1072 0.0645  0.1153  606 TYR A C   
4745 O O   . TYR A 606 ? 0.6112 0.3084 0.5599 -0.1099 0.0584  0.1023  606 TYR A O   
4746 C CB  . TYR A 606 ? 0.6960 0.3972 0.6371 -0.1225 0.0823  0.1448  606 TYR A CB  
4747 C CG  . TYR A 606 ? 0.7470 0.4239 0.7042 -0.1219 0.0750  0.1393  606 TYR A CG  
4748 C CD1 . TYR A 606 ? 0.7405 0.4133 0.7205 -0.1346 0.0745  0.1259  606 TYR A CD1 
4749 C CD2 . TYR A 606 ? 0.7426 0.4016 0.6929 -0.1092 0.0687  0.1452  606 TYR A CD2 
4750 C CE1 . TYR A 606 ? 0.8201 0.4699 0.8120 -0.1358 0.0685  0.1177  606 TYR A CE1 
4751 C CE2 . TYR A 606 ? 0.7926 0.4279 0.7569 -0.1094 0.0641  0.1373  606 TYR A CE2 
4752 C CZ  . TYR A 606 ? 0.7299 0.3600 0.7130 -0.1230 0.0642  0.1228  606 TYR A CZ  
4753 O OH  . TYR A 606 ? 0.9641 0.5702 0.9585 -0.1245 0.0603  0.1123  606 TYR A OH  
4754 N N   . GLU A 607 ? 0.5863 0.2974 0.5054 -0.0947 0.0614  0.1204  607 GLU A N   
4755 C CA  . GLU A 607 ? 0.6751 0.3758 0.5901 -0.0834 0.0529  0.1111  607 GLU A CA  
4756 C C   . GLU A 607 ? 0.6380 0.3496 0.5577 -0.0834 0.0471  0.0923  607 GLU A C   
4757 O O   . GLU A 607 ? 0.6484 0.3465 0.5675 -0.0793 0.0415  0.0823  607 GLU A O   
4758 C CB  . GLU A 607 ? 0.6195 0.3291 0.5187 -0.0712 0.0510  0.1191  607 GLU A CB  
4759 C CG  . GLU A 607 ? 0.7901 0.4862 0.6841 -0.0679 0.0535  0.1406  607 GLU A CG  
4760 C CD  . GLU A 607 ? 0.8383 0.5445 0.7209 -0.0544 0.0480  0.1476  607 GLU A CD  
4761 O OE1 . GLU A 607 ? 0.8034 0.5365 0.6763 -0.0529 0.0460  0.1418  607 GLU A OE1 
4762 O OE2 . GLU A 607 ? 0.9631 0.6509 0.8495 -0.0451 0.0456  0.1578  607 GLU A OE2 
4763 N N   . ILE A 608 ? 0.5874 0.3228 0.5116 -0.0874 0.0490  0.0877  608 ILE A N   
4764 C CA  . ILE A 608 ? 0.6072 0.3520 0.5382 -0.0864 0.0429  0.0734  608 ILE A CA  
4765 C C   . ILE A 608 ? 0.6005 0.3379 0.5471 -0.0957 0.0382  0.0665  608 ILE A C   
4766 O O   . ILE A 608 ? 0.5739 0.3056 0.5189 -0.0937 0.0295  0.0561  608 ILE A O   
4767 C CB  . ILE A 608 ? 0.5477 0.3189 0.4839 -0.0865 0.0472  0.0707  608 ILE A CB  
4768 C CG1 . ILE A 608 ? 0.5584 0.3380 0.4785 -0.0792 0.0510  0.0736  608 ILE A CG1 
4769 C CG2 . ILE A 608 ? 0.5740 0.3531 0.5205 -0.0844 0.0404  0.0596  608 ILE A CG2 
4770 C CD1 . ILE A 608 ? 0.5638 0.3355 0.4734 -0.0688 0.0450  0.0682  608 ILE A CD1 
4771 N N   . GLU A 609 ? 0.5534 0.2923 0.5146 -0.1072 0.0440  0.0718  609 GLU A N   
4772 C CA  . GLU A 609 ? 0.6453 0.3781 0.6247 -0.1184 0.0396  0.0640  609 GLU A CA  
4773 C C   . GLU A 609 ? 0.6216 0.3245 0.5932 -0.1179 0.0352  0.0592  609 GLU A C   
4774 O O   . GLU A 609 ? 0.6282 0.3273 0.6052 -0.1229 0.0265  0.0456  609 GLU A O   
4775 C CB  . GLU A 609 ? 0.6367 0.3741 0.6348 -0.1322 0.0498  0.0718  609 GLU A CB  
4776 C CG  . GLU A 609 ? 0.7236 0.4536 0.7439 -0.1463 0.0457  0.0626  609 GLU A CG  
4777 C CD  . GLU A 609 ? 0.8270 0.5629 0.8698 -0.1616 0.0578  0.0700  609 GLU A CD  
4778 O OE1 . GLU A 609 ? 0.8681 0.6082 0.9032 -0.1609 0.0705  0.0846  609 GLU A OE1 
4779 O OE2 . GLU A 609 ? 0.9284 0.6661 0.9959 -0.1753 0.0548  0.0605  609 GLU A OE2 
4780 N N   . ARG A 610 ? 0.6251 0.3076 0.5844 -0.1115 0.0409  0.0696  610 ARG A N   
4781 C CA  . ARG A 610 ? 0.6184 0.2712 0.5735 -0.1091 0.0391  0.0640  610 ARG A CA  
4782 C C   . ARG A 610 ? 0.5958 0.2494 0.5369 -0.1003 0.0307  0.0497  610 ARG A C   
4783 O O   . ARG A 610 ? 0.6314 0.2681 0.5714 -0.1035 0.0271  0.0362  610 ARG A O   
4784 C CB  . ARG A 610 ? 0.6936 0.3298 0.6430 -0.1002 0.0459  0.0802  610 ARG A CB  
4785 C CG  . ARG A 610 ? 0.6843 0.2966 0.6394 -0.0950 0.0444  0.0737  610 ARG A CG  
4786 C CD  . ARG A 610 ? 0.7492 0.3537 0.7067 -0.0849 0.0478  0.0922  610 ARG A CD  
4787 N NE  . ARG A 610 ? 0.7307 0.3490 0.6723 -0.0724 0.0474  0.1022  610 ARG A NE  
4788 C CZ  . ARG A 610 ? 0.7785 0.3959 0.7174 -0.0630 0.0483  0.1206  610 ARG A CZ  
4789 N NH1 . ARG A 610 ? 0.8451 0.4467 0.7940 -0.0636 0.0495  0.1325  610 ARG A NH1 
4790 N NH2 . ARG A 610 ? 0.8247 0.4564 0.7487 -0.0533 0.0472  0.1272  610 ARG A NH2 
4791 N N   . GLU A 611 ? 0.5974 0.2695 0.5269 -0.0901 0.0290  0.0518  611 GLU A N   
4792 C CA  . GLU A 611 ? 0.6023 0.2751 0.5177 -0.0826 0.0232  0.0404  611 GLU A CA  
4793 C C   . GLU A 611 ? 0.6428 0.3267 0.5609 -0.0897 0.0137  0.0285  611 GLU A C   
4794 O O   . GLU A 611 ? 0.6431 0.3190 0.5488 -0.0889 0.0081  0.0167  611 GLU A O   
4795 C CB  . GLU A 611 ? 0.5925 0.2816 0.4984 -0.0717 0.0251  0.0460  611 GLU A CB  
4796 C CG  . GLU A 611 ? 0.6113 0.2931 0.5126 -0.0627 0.0310  0.0557  611 GLU A CG  
4797 C CD  . GLU A 611 ? 0.6140 0.2714 0.5119 -0.0575 0.0323  0.0504  611 GLU A CD  
4798 O OE1 . GLU A 611 ? 0.6082 0.2608 0.4976 -0.0562 0.0300  0.0373  611 GLU A OE1 
4799 O OE2 . GLU A 611 ? 0.6860 0.3287 0.5899 -0.0544 0.0364  0.0595  611 GLU A OE2 
4800 N N   . LEU A 612 ? 0.6276 0.3321 0.5617 -0.0965 0.0116  0.0314  612 LEU A N   
4801 C CA  . LEU A 612 ? 0.6079 0.3263 0.5501 -0.1033 0.0005  0.0217  612 LEU A CA  
4802 C C   . LEU A 612 ? 0.6474 0.3497 0.5933 -0.1149 -0.0042 0.0096  612 LEU A C   
4803 O O   . LEU A 612 ? 0.6489 0.3523 0.5847 -0.1170 -0.0149 -0.0028 612 LEU A O   
4804 C CB  . LEU A 612 ? 0.6041 0.3485 0.5703 -0.1082 0.0012  0.0272  612 LEU A CB  
4805 C CG  . LEU A 612 ? 0.6775 0.4417 0.6611 -0.1155 -0.0115 0.0188  612 LEU A CG  
4806 C CD1 . LEU A 612 ? 0.5683 0.3432 0.5385 -0.1053 -0.0224 0.0166  612 LEU A CD1 
4807 C CD2 . LEU A 612 ? 0.7047 0.4929 0.7198 -0.1222 -0.0068 0.0237  612 LEU A CD2 
4808 N N   . ARG A 613 ? 0.6298 0.3160 0.5888 -0.1232 0.0042  0.0131  613 ARG A N   
4809 C CA  . ARG A 613 ? 0.6077 0.2749 0.5735 -0.1358 0.0019  -0.0002 613 ARG A CA  
4810 C C   . ARG A 613 ? 0.6196 0.2631 0.5626 -0.1297 0.0012  -0.0119 613 ARG A C   
4811 O O   . ARG A 613 ? 0.6484 0.2854 0.5872 -0.1384 -0.0059 -0.0300 613 ARG A O   
4812 C CB  . ARG A 613 ? 0.6408 0.2894 0.6251 -0.1446 0.0142  0.0088  613 ARG A CB  
4813 C CG  . ARG A 613 ? 0.6270 0.2976 0.6363 -0.1551 0.0172  0.0168  613 ARG A CG  
4814 C CD  . ARG A 613 ? 0.7628 0.4124 0.7846 -0.1624 0.0320  0.0302  613 ARG A CD  
4815 N NE  . ARG A 613 ? 0.8290 0.4999 0.8766 -0.1758 0.0366  0.0349  613 ARG A NE  
4816 C CZ  . ARG A 613 ? 0.8216 0.4853 0.8948 -0.1942 0.0405  0.0297  613 ARG A CZ  
4817 N NH1 . ARG A 613 ? 0.8665 0.5044 0.9422 -0.1983 0.0386  0.0210  613 ARG A NH1 
4818 N NH2 . ARG A 613 ? 0.8981 0.5874 0.9970 -0.2057 0.0451  0.0331  613 ARG A NH2 
4819 N N   . ALA A 614 ? 0.6049 0.2362 0.5341 -0.1157 0.0094  -0.0031 614 ALA A N   
4820 C CA  . ALA A 614 ? 0.6366 0.2458 0.5480 -0.1092 0.0120  -0.0143 614 ALA A CA  
4821 C C   . ALA A 614 ? 0.6665 0.2896 0.5553 -0.1065 0.0024  -0.0262 614 ALA A C   
4822 O O   . ALA A 614 ? 0.6597 0.2703 0.5350 -0.1109 0.0000  -0.0439 614 ALA A O   
4823 C CB  . ALA A 614 ? 0.6321 0.2309 0.5395 -0.0942 0.0222  -0.0010 614 ALA A CB  
4824 N N   . LEU A 615 ? 0.6157 0.2641 0.4997 -0.1000 -0.0026 -0.0167 615 LEU A N   
4825 C CA  . LEU A 615 ? 0.6295 0.2906 0.4922 -0.0974 -0.0119 -0.0237 615 LEU A CA  
4826 C C   . LEU A 615 ? 0.6083 0.2772 0.4712 -0.1107 -0.0255 -0.0378 615 LEU A C   
4827 O O   . LEU A 615 ? 0.6544 0.3179 0.4939 -0.1130 -0.0307 -0.0519 615 LEU A O   
4828 C CB  . LEU A 615 ? 0.6500 0.3348 0.5143 -0.0890 -0.0143 -0.0097 615 LEU A CB  
4829 C CG  . LEU A 615 ? 0.6372 0.3334 0.4798 -0.0849 -0.0234 -0.0123 615 LEU A CG  
4830 C CD1 . LEU A 615 ? 0.6776 0.3554 0.4921 -0.0799 -0.0168 -0.0204 615 LEU A CD1 
4831 C CD2 . LEU A 615 ? 0.6167 0.3316 0.4652 -0.0759 -0.0236 0.0019  615 LEU A CD2 
4832 N N   . LYS A 616 ? 0.6486 0.3319 0.5382 -0.1205 -0.0310 -0.0353 616 LYS A N   
4833 C CA  . LYS A 616 ? 0.6417 0.3374 0.5381 -0.1348 -0.0454 -0.0494 616 LYS A CA  
4834 C C   . LYS A 616 ? 0.7194 0.3897 0.6050 -0.1452 -0.0438 -0.0705 616 LYS A C   
4835 O O   . LYS A 616 ? 0.7262 0.4042 0.5972 -0.1534 -0.0567 -0.0871 616 LYS A O   
4836 C CB  . LYS A 616 ? 0.6807 0.3932 0.6146 -0.1447 -0.0466 -0.0436 616 LYS A CB  
4837 C CG  . LYS A 616 ? 0.7421 0.4759 0.6915 -0.1599 -0.0631 -0.0573 616 LYS A CG  
4838 C CD  . LYS A 616 ? 0.8359 0.6021 0.8204 -0.1620 -0.0669 -0.0462 616 LYS A CD  
4839 C CE  . LYS A 616 ? 0.9033 0.7028 0.9012 -0.1707 -0.0888 -0.0564 616 LYS A CE  
4840 N NZ  . LYS A 616 ? 0.8608 0.6956 0.8805 -0.1613 -0.0953 -0.0420 616 LYS A NZ  
4841 N N   . GLN A 617 ? 0.7002 0.3402 0.5931 -0.1448 -0.0282 -0.0704 617 GLN A N   
4842 C CA  . GLN A 617 ? 0.7164 0.3280 0.6037 -0.1541 -0.0237 -0.0917 617 GLN A CA  
4843 C C   . GLN A 617 ? 0.7298 0.3319 0.5806 -0.1462 -0.0224 -0.1040 617 GLN A C   
4844 O O   . GLN A 617 ? 0.7715 0.3680 0.6064 -0.1564 -0.0278 -0.1270 617 GLN A O   
4845 C CB  . GLN A 617 ? 0.6962 0.2762 0.6044 -0.1534 -0.0065 -0.0848 617 GLN A CB  
4846 C CG  . GLN A 617 ? 0.7786 0.3244 0.6888 -0.1631 0.0009  -0.1068 617 GLN A CG  
4847 C CD  . GLN A 617 ? 0.8026 0.3529 0.7298 -0.1858 -0.0081 -0.1253 617 GLN A CD  
4848 O OE1 . GLN A 617 ? 0.8861 0.4646 0.8307 -0.1941 -0.0182 -0.1183 617 GLN A OE1 
4849 N NE2 . GLN A 617 ? 0.8249 0.3600 0.7546 -0.1913 -0.0057 -0.1475 617 GLN A NE2 
4850 N N   . ARG A 618 ? 0.7015 0.3029 0.5388 -0.1292 -0.0145 -0.0901 618 ARG A N   
4851 C CA  . ARG A 618 ? 0.7721 0.3656 0.5762 -0.1217 -0.0102 -0.1004 618 ARG A CA  
4852 C C   . ARG A 618 ? 0.7856 0.4021 0.5614 -0.1268 -0.0263 -0.1084 618 ARG A C   
4853 O O   . ARG A 618 ? 0.8158 0.4242 0.5625 -0.1307 -0.0261 -0.1273 618 ARG A O   
4854 C CB  . ARG A 618 ? 0.7207 0.3148 0.5214 -0.1040 0.0005  -0.0826 618 ARG A CB  
4855 C CG  . ARG A 618 ? 0.7270 0.2990 0.5498 -0.0968 0.0153  -0.0752 618 ARG A CG  
4856 C CD  . ARG A 618 ? 0.6887 0.2632 0.5056 -0.0803 0.0250  -0.0634 618 ARG A CD  
4857 N NE  . ARG A 618 ? 0.6789 0.2801 0.4935 -0.0753 0.0187  -0.0468 618 ARG A NE  
4858 C CZ  . ARG A 618 ? 0.7207 0.3323 0.5548 -0.0716 0.0189  -0.0292 618 ARG A CZ  
4859 N NH1 . ARG A 618 ? 0.7606 0.3598 0.6157 -0.0720 0.0241  -0.0226 618 ARG A NH1 
4860 N NH2 . ARG A 618 ? 0.6629 0.2970 0.4946 -0.0676 0.0147  -0.0180 618 ARG A NH2 
4861 N N   . ILE A 619 ? 0.7666 0.4122 0.5502 -0.1262 -0.0399 -0.0939 619 ILE A N   
4862 C CA  . ILE A 619 ? 0.7825 0.4518 0.5419 -0.1295 -0.0577 -0.0976 619 ILE A CA  
4863 C C   . ILE A 619 ? 0.8002 0.4730 0.5580 -0.1478 -0.0707 -0.1210 619 ILE A C   
4864 O O   . ILE A 619 ? 0.8193 0.4974 0.5428 -0.1528 -0.0799 -0.1353 619 ILE A O   
4865 C CB  . ILE A 619 ? 0.7738 0.4726 0.5495 -0.1229 -0.0686 -0.0758 619 ILE A CB  
4866 C CG1 . ILE A 619 ? 0.7394 0.4342 0.5090 -0.1062 -0.0560 -0.0572 619 ILE A CG1 
4867 C CG2 . ILE A 619 ? 0.8187 0.5446 0.5764 -0.1268 -0.0908 -0.0779 619 ILE A CG2 
4868 C CD1 . ILE A 619 ? 0.8158 0.5332 0.6077 -0.0992 -0.0611 -0.0374 619 ILE A CD1 
4869 N N   . SER A 620 ? 0.8032 0.4732 0.5970 -0.1594 -0.0710 -0.1258 620 SER A N   
4870 C CA  . SER A 620 ? 0.8136 0.4869 0.6125 -0.1794 -0.0824 -0.1503 620 SER A CA  
4871 C C   . SER A 620 ? 0.8302 0.4742 0.6026 -0.1863 -0.0733 -0.1774 620 SER A C   
4872 O O   . SER A 620 ? 0.8512 0.5014 0.6120 -0.2026 -0.0852 -0.2020 620 SER A O   
4873 C CB  . SER A 620 ? 0.8286 0.4987 0.6748 -0.1908 -0.0788 -0.1490 620 SER A CB  
4874 O OG  . SER A 620 ? 0.8588 0.4889 0.7142 -0.1926 -0.0585 -0.1563 620 SER A OG  
4875 N N   . GLN A 621 ? 0.8337 0.4475 0.5975 -0.1747 -0.0524 -0.1751 621 GLN A N   
4876 C CA  . GLN A 621 ? 0.9079 0.4927 0.6499 -0.1794 -0.0403 -0.2018 621 GLN A CA  
4877 C C   . GLN A 621 ? 0.9503 0.5432 0.6417 -0.1739 -0.0425 -0.2091 621 GLN A C   
4878 O O   . GLN A 621 ? 0.9448 0.5169 0.6128 -0.1785 -0.0320 -0.2340 621 GLN A O   
4879 C CB  . GLN A 621 ? 0.9126 0.4614 0.6752 -0.1687 -0.0160 -0.1963 621 GLN A CB  
4880 C CG  . GLN A 621 ? 0.9037 0.4351 0.7112 -0.1773 -0.0107 -0.1937 621 GLN A CG  
4881 C CD  . GLN A 621 ? 0.9647 0.4975 0.7874 -0.1941 -0.0166 -0.2192 621 GLN A CD  
4882 O OE1 . GLN A 621 ? 1.0331 0.5561 0.8432 -0.1945 -0.0113 -0.2416 621 GLN A OE1 
4883 N NE2 . GLN A 621 ? 0.9922 0.5383 0.8442 -0.2083 -0.0272 -0.2163 621 GLN A NE2 
4884 N N   . MET A 622 ? 0.9087 0.5301 0.5828 -0.1646 -0.0544 -0.1882 622 MET A N   
4885 C CA  . MET A 622 ? 0.9386 0.5696 0.5623 -0.1603 -0.0573 -0.1908 622 MET A CA  
4886 C C   . MET A 622 ? 0.9916 0.6363 0.5843 -0.1774 -0.0747 -0.2159 622 MET A C   
4887 O O   . MET A 622 ? 0.9940 0.6568 0.6068 -0.1906 -0.0933 -0.2224 622 MET A O   
4888 C CB  . MET A 622 ? 0.9413 0.5981 0.5590 -0.1469 -0.0669 -0.1599 622 MET A CB  
4889 C CG  . MET A 622 ? 0.8892 0.5362 0.5283 -0.1302 -0.0502 -0.1369 622 MET A CG  
4890 S SD  . MET A 622 ? 0.9190 0.5928 0.5474 -0.1166 -0.0600 -0.1055 622 MET A SD  
4891 C CE  . MET A 622 ? 0.8788 0.5512 0.4443 -0.1163 -0.0581 -0.1134 622 MET A CE  
4892 O OXT . MET A 622 ? 1.1073 0.7478 0.6539 -0.1788 -0.0706 -0.2303 622 MET A OXT 
# 
