data_9EJ1
# 
_entry.id   9EJ1 
# 
_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   9EJ1         pdb_00009ej1 10.2210/pdb9ej1/pdb 
WWPDB D_1000290518 ?            ?                   
# 
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                        9EJ1 
_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    170 ?        ? ? ? 
# 
_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   801 121  HOH HOH A . 
H 6 HOH 2   802 109  HOH HOH A . 
H 6 HOH 3   803 99   HOH HOH A . 
H 6 HOH 4   804 23   HOH HOH A . 
H 6 HOH 5   805 31   HOH HOH A . 
H 6 HOH 6   806 140  HOH HOH A . 
H 6 HOH 7   807 130  HOH HOH A . 
H 6 HOH 8   808 28   HOH HOH A . 
H 6 HOH 9   809 125  HOH HOH A . 
H 6 HOH 10  810 66   HOH HOH A . 
H 6 HOH 11  811 98   HOH HOH A . 
H 6 HOH 12  812 149  HOH HOH A . 
H 6 HOH 13  813 101  HOH HOH A . 
H 6 HOH 14  814 95   HOH HOH A . 
H 6 HOH 15  815 55   HOH HOH A . 
H 6 HOH 16  816 21   HOH HOH A . 
H 6 HOH 17  817 54   HOH HOH A . 
H 6 HOH 18  818 157  HOH HOH A . 
H 6 HOH 19  819 69   HOH HOH A . 
H 6 HOH 20  820 96   HOH HOH A . 
H 6 HOH 21  821 73   HOH HOH A . 
H 6 HOH 22  822 136  HOH HOH A . 
H 6 HOH 23  823 135  HOH HOH A . 
H 6 HOH 24  824 22   HOH HOH A . 
H 6 HOH 25  825 56   HOH HOH A . 
H 6 HOH 26  826 37   HOH HOH A . 
H 6 HOH 27  827 75   HOH HOH A . 
H 6 HOH 28  828 81   HOH HOH A . 
H 6 HOH 29  829 159  HOH HOH A . 
H 6 HOH 30  830 39   HOH HOH A . 
H 6 HOH 31  831 29   HOH HOH A . 
H 6 HOH 32  832 126  HOH HOH A . 
H 6 HOH 33  833 49   HOH HOH A . 
H 6 HOH 34  834 11   HOH HOH A . 
H 6 HOH 35  835 7    HOH HOH A . 
H 6 HOH 36  836 92   HOH HOH A . 
H 6 HOH 37  837 45   HOH HOH A . 
H 6 HOH 38  838 169  HOH HOH A . 
H 6 HOH 39  839 65   HOH HOH A . 
H 6 HOH 40  840 160  HOH HOH A . 
H 6 HOH 41  841 85   HOH HOH A . 
H 6 HOH 42  842 35   HOH HOH A . 
H 6 HOH 43  843 8    HOH HOH A . 
H 6 HOH 44  844 63   HOH HOH A . 
H 6 HOH 45  845 168  HOH HOH A . 
H 6 HOH 46  846 60   HOH HOH A . 
H 6 HOH 47  847 115  HOH HOH A . 
H 6 HOH 48  848 33   HOH HOH A . 
H 6 HOH 49  849 36   HOH HOH A . 
H 6 HOH 50  850 46   HOH HOH A . 
H 6 HOH 51  851 27   HOH HOH A . 
H 6 HOH 52  852 79   HOH HOH A . 
H 6 HOH 53  853 61   HOH HOH A . 
H 6 HOH 54  854 133  HOH HOH A . 
H 6 HOH 55  855 20   HOH HOH A . 
H 6 HOH 56  856 38   HOH HOH A . 
H 6 HOH 57  857 34   HOH HOH A . 
H 6 HOH 58  858 87   HOH HOH A . 
H 6 HOH 59  859 84   HOH HOH A . 
H 6 HOH 60  860 100  HOH HOH A . 
H 6 HOH 61  861 76   HOH HOH A . 
H 6 HOH 62  862 30   HOH HOH A . 
H 6 HOH 63  863 44   HOH HOH A . 
H 6 HOH 64  864 74   HOH HOH A . 
H 6 HOH 65  865 5    HOH HOH A . 
H 6 HOH 66  866 111  HOH HOH A . 
H 6 HOH 67  867 71   HOH HOH A . 
H 6 HOH 68  868 24   HOH HOH A . 
H 6 HOH 69  869 131  HOH HOH A . 
H 6 HOH 70  870 70   HOH HOH A . 
H 6 HOH 71  871 41   HOH HOH A . 
H 6 HOH 72  872 53   HOH HOH A . 
H 6 HOH 73  873 13   HOH HOH A . 
H 6 HOH 74  874 67   HOH HOH A . 
H 6 HOH 75  875 72   HOH HOH A . 
H 6 HOH 76  876 106  HOH HOH A . 
H 6 HOH 77  877 52   HOH HOH A . 
H 6 HOH 78  878 32   HOH HOH A . 
H 6 HOH 79  879 145  HOH HOH A . 
H 6 HOH 80  880 166  HOH HOH A . 
H 6 HOH 81  881 119  HOH HOH A . 
H 6 HOH 82  882 47   HOH HOH A . 
H 6 HOH 83  883 151  HOH HOH A . 
H 6 HOH 84  884 113  HOH HOH A . 
H 6 HOH 85  885 1    HOH HOH A . 
H 6 HOH 86  886 83   HOH HOH A . 
H 6 HOH 87  887 6    HOH HOH A . 
H 6 HOH 88  888 108  HOH HOH A . 
H 6 HOH 89  889 102  HOH HOH A . 
H 6 HOH 90  890 104  HOH HOH A . 
H 6 HOH 91  891 148  HOH HOH A . 
H 6 HOH 92  892 91   HOH HOH A . 
H 6 HOH 93  893 97   HOH HOH A . 
H 6 HOH 94  894 62   HOH HOH A . 
H 6 HOH 95  895 16   HOH HOH A . 
H 6 HOH 96  896 68   HOH HOH A . 
H 6 HOH 97  897 78   HOH HOH A . 
H 6 HOH 98  898 10   HOH HOH A . 
H 6 HOH 99  899 18   HOH HOH A . 
H 6 HOH 100 900 14   HOH HOH A . 
H 6 HOH 101 901 138  HOH HOH A . 
H 6 HOH 102 902 89   HOH HOH A . 
H 6 HOH 103 903 15   HOH HOH A . 
H 6 HOH 104 904 43   HOH HOH A . 
H 6 HOH 105 905 59   HOH HOH A . 
H 6 HOH 106 906 3    HOH HOH A . 
H 6 HOH 107 907 152  HOH HOH A . 
H 6 HOH 108 908 163  HOH HOH A . 
H 6 HOH 109 909 12   HOH HOH A . 
H 6 HOH 110 910 58   HOH HOH A . 
H 6 HOH 111 911 77   HOH HOH A . 
H 6 HOH 112 912 90   HOH HOH A . 
H 6 HOH 113 913 120  HOH HOH A . 
H 6 HOH 114 914 93   HOH HOH A . 
H 6 HOH 115 915 143  HOH HOH A . 
H 6 HOH 116 916 122  HOH HOH A . 
H 6 HOH 117 917 80   HOH HOH A . 
H 6 HOH 118 918 9    HOH HOH A . 
H 6 HOH 119 919 118  HOH HOH A . 
H 6 HOH 120 920 161  HOH HOH A . 
H 6 HOH 121 921 17   HOH HOH A . 
H 6 HOH 122 922 107  HOH HOH A . 
H 6 HOH 123 923 57   HOH HOH A . 
H 6 HOH 124 924 19   HOH HOH A . 
H 6 HOH 125 925 4    HOH HOH A . 
H 6 HOH 126 926 94   HOH HOH A . 
H 6 HOH 127 927 42   HOH HOH A . 
H 6 HOH 128 928 64   HOH HOH A . 
H 6 HOH 129 929 123  HOH HOH A . 
H 6 HOH 130 930 40   HOH HOH A . 
H 6 HOH 131 931 124  HOH HOH A . 
H 6 HOH 132 932 86   HOH HOH A . 
H 6 HOH 133 933 137  HOH HOH A . 
H 6 HOH 134 934 82   HOH HOH A . 
H 6 HOH 135 935 117  HOH HOH A . 
H 6 HOH 136 936 141  HOH HOH A . 
H 6 HOH 137 937 105  HOH HOH A . 
H 6 HOH 138 938 51   HOH HOH A . 
H 6 HOH 139 939 132  HOH HOH A . 
H 6 HOH 140 940 25   HOH HOH A . 
H 6 HOH 141 941 50   HOH HOH A . 
H 6 HOH 142 942 162  HOH HOH A . 
H 6 HOH 143 943 48   HOH HOH A . 
H 6 HOH 144 944 150  HOH HOH A . 
H 6 HOH 145 945 165  HOH HOH A . 
H 6 HOH 146 946 110  HOH HOH A . 
H 6 HOH 147 947 129  HOH HOH A . 
H 6 HOH 148 948 88   HOH HOH A . 
H 6 HOH 149 949 164  HOH HOH A . 
H 6 HOH 150 950 167  HOH HOH A . 
H 6 HOH 151 951 158  HOH HOH A . 
H 6 HOH 152 952 127  HOH HOH A . 
H 6 HOH 153 953 112  HOH HOH A . 
H 6 HOH 154 954 128  HOH HOH A . 
H 6 HOH 155 955 2    HOH HOH A . 
H 6 HOH 156 956 144  HOH HOH A . 
H 6 HOH 157 957 116  HOH HOH A . 
H 6 HOH 158 958 26   HOH HOH A . 
H 6 HOH 159 959 142  HOH HOH A . 
H 6 HOH 160 960 146  HOH HOH A . 
H 6 HOH 161 961 170  HOH HOH A . 
H 6 HOH 162 962 147  HOH HOH A . 
H 6 HOH 163 963 153  HOH HOH A . 
H 6 HOH 164 964 134  HOH HOH A . 
H 6 HOH 165 965 155  HOH HOH A . 
H 6 HOH 166 966 154  HOH HOH A . 
H 6 HOH 167 967 114  HOH HOH A . 
H 6 HOH 168 968 156  HOH HOH A . 
H 6 HOH 169 969 103  HOH HOH A . 
H 6 HOH 170 970 139  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                   111.66 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EJ1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.315 
_cell.length_a_esd                 ? 
_cell.length_b                     119.834 
_cell.length_b_esd                 ? 
_cell.length_c                     60.826 
_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                         9EJ1 
_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                   9EJ1 
_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          44.31 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, 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                     293 
_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                                       9EJ1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2 
_reflns.d_resolution_low                               120 
_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                                     40613 
_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                                6.82 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          2.9 
_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                                0.276 
_reflns.pdbx_Rpim_I_all                                0.105 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.972 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.255 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.00 
_reflns_shell.d_res_low                                     2.03 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.4000 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2065 
_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                               6.90 
_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                               1.9100 
_reflns_shell.pdbx_Rpim_I_all                               0.7230 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.6100 
_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                                  1.7650 
_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                                 9EJ1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             56.53 
_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                     40573 
_refine.ls_number_reflns_R_free                  2032 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1811 
_refine.ls_R_factor_R_free                       0.2124 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1794 
_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                 23.70 
_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                            0.26 
_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             170 
_refine_hist.number_atoms_total               5090 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        56.53 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.567  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.905 ? 1912 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044  ? 720  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 901  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.05  . . 159 2501 98.00  . . . . 0.2906 . . . . . . . . . . . 0.3267 
'X-RAY DIFFRACTION' 2.05 2.10  . . 130 2582 100.00 . . . . 0.2756 . . . . . . . . . . . 0.3344 
'X-RAY DIFFRACTION' 2.10 2.16  . . 143 2577 100.00 . . . . 0.2676 . . . . . . . . . . . 0.3133 
'X-RAY DIFFRACTION' 2.16 2.22  . . 127 2522 100.00 . . . . 0.2471 . . . . . . . . . . . 0.3199 
'X-RAY DIFFRACTION' 2.22 2.29  . . 117 2585 100.00 . . . . 0.2345 . . . . . . . . . . . 0.2676 
'X-RAY DIFFRACTION' 2.29 2.37  . . 117 2611 100.00 . . . . 0.2103 . . . . . . . . . . . 0.2394 
'X-RAY DIFFRACTION' 2.37 2.47  . . 121 2546 100.00 . . . . 0.2089 . . . . . . . . . . . 0.2155 
'X-RAY DIFFRACTION' 2.47 2.58  . . 153 2561 100.00 . . . . 0.2031 . . . . . . . . . . . 0.2668 
'X-RAY DIFFRACTION' 2.58 2.72  . . 129 2567 100.00 . . . . 0.1951 . . . . . . . . . . . 0.2584 
'X-RAY DIFFRACTION' 2.72 2.89  . . 127 2584 100.00 . . . . 0.1833 . . . . . . . . . . . 0.2333 
'X-RAY DIFFRACTION' 2.89 3.11  . . 140 2567 100.00 . . . . 0.1753 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 3.11 3.42  . . 162 2569 100.00 . . . . 0.1580 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 3.42 3.92  . . 124 2563 100.00 . . . . 0.1467 . . . . . . . . . . . 0.1564 
'X-RAY DIFFRACTION' 3.92 4.93  . . 145 2590 100.00 . . . . 0.1428 . . . . . . . . . . . 0.1476 
'X-RAY DIFFRACTION' 4.94 56.53 . . 138 2616 100.00 . . . . 0.1729 . . . . . . . . . . . 0.2134 
# 
_struct.entry_id                     9EJ1 
_struct.title                        'Rat cytosolic PEPCK in complex with GTP and oxalate (293K)' 
_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        9EJ1 
_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              9EJ1 
_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 PRO A 24  ? GLN A 39  ? PRO A 24  GLN A 39  1 ? 16 
HELX_P HELX_P3  AA3 SER A 49  ? GLU A 63  ? SER A 49  GLU A 63  1 ? 15 
HELX_P HELX_P4  AA4 ILE A 88  ? SER A 90  ? ILE A 88  SER A 90  5 ? 3  
HELX_P HELX_P5  AA5 GLU A 98  ? THR A 102 ? GLU A 98  THR A 102 5 ? 5  
HELX_P HELX_P6  AA6 SER A 118 ? ALA A 128 ? SER A 118 ALA A 128 1 ? 11 
HELX_P HELX_P7  AA7 SER A 163 ? THR A 174 ? SER A 163 THR A 174 1 ? 12 
HELX_P HELX_P8  AA8 GLY A 177 ? GLY A 185 ? GLY A 177 GLY A 185 1 ? 9  
HELX_P HELX_P9  AA9 ASN A 213 ? THR A 217 ? ASN A 213 THR A 217 5 ? 5  
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 LYS A 243 ? LEU A 248 ? LYS A 243 LEU A 248 1 ? 6  
HELX_P HELX_P13 AB4 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P14 AB5 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P15 AB6 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P16 AB7 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P17 AB8 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P18 AB9 PRO A 479 ? PHE A 486 ? PRO A 479 PHE A 486 5 ? 8  
HELX_P HELX_P19 AC1 ASN A 489 ? MET A 500 ? ASN A 489 MET A 500 1 ? 12 
HELX_P HELX_P20 AC2 ALA A 501 ? ARG A 503 ? ALA A 501 ARG A 503 5 ? 3  
HELX_P HELX_P21 AC3 GLY A 529 ? GLU A 532 ? GLY A 529 GLU A 532 5 ? 4  
HELX_P HELX_P22 AC4 ASN A 533 ? GLY A 546 ? ASN A 533 GLY A 546 1 ? 14 
HELX_P HELX_P23 AC5 ASN A 573 ? PHE A 578 ? ASN A 573 PHE A 578 1 ? 6  
HELX_P HELX_P24 AC6 SER A 581 ? VAL A 600 ? SER A 581 VAL A 600 1 ? 20 
HELX_P HELX_P25 AC7 ASN A 601 ? LEU A 604 ? ASN A 601 LEU A 604 5 ? 4  
HELX_P HELX_P26 AC8 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 ? ? ? ? ? ? ? 2.268 ? ? 
metalc2  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 C MN  . MN  ? ? A HIS 264 A MN  702 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc3  metalc ? ? A THR 291 OG1 ? ? ? 1_555 B MN  . MN  ? ? A THR 291 A MN  701 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc4  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 C MN  . MN  ? ? A ASP 311 A MN  702 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc5  metalc ? ? A HIS 502 NE2 ? ? ? 1_555 D MN  . MN  ? ? A HIS 502 A MN  703 1_555 ? ? ? ? ? ? ? 2.457 ? ? 
metalc6  metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1B ? ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.151 ? ? 
metalc7  metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1G ? ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc8  metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 810 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 816 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
metalc10 metalc ? ? B MN  .   MN  ? ? ? 1_555 H HOH . O   ? ? A MN  701 A HOH 855 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc11 metalc ? ? C MN  .   MN  ? ? ? 1_555 E OXL . O1  ? ? A MN  702 A OXL 704 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc12 metalc ? ? C MN  .   MN  ? ? ? 1_555 E OXL . O2  ? ? A MN  702 A OXL 704 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc13 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O3G ? ? A MN  702 A GTP 705 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
# 
_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 85.0  ? 
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_555 101.3 ? 
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 90.7  ? 
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 89.8  ? 
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_555 172.6 ? 
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 95.5  ? 
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 84.2  ? 
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 98.8  ? 
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_555 169.4 ? 
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 75.3  ? 
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_555 172.5 ? 
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 97.6  ? 
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 85.8  ? 
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 86.9  ? 
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 88.4  ? 
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 84.5  ? 
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_555 160.1 ? 
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 92.1  ? 
19 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 810 ? 1_555 85.7  ? 
20 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 810 ? 1_555 166.4 ? 
21 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 810 ? 1_555 100.3 ? 
22 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 816 ? 1_555 86.1  ? 
23 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 816 ? 1_555 84.6  ? 
24 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 816 ? 1_555 74.1  ? 
25 O   ? H HOH .   ? A HOH 810 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 816 ? 1_555 104.1 ? 
26 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 855 ? 1_555 108.0 ? 
27 O1B ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 855 ? 1_555 90.3  ? 
28 O1G ? F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 855 ? 1_555 91.6  ? 
29 O   ? H HOH .   ? A HOH 810 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 855 ? 1_555 83.9  ? 
30 O   ? H HOH .   ? A HOH 816 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? H HOH .   ? A HOH 855 ? 1_555 164.5 ? 
# 
_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       1.93 
# 
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 ARG A 115 ? MET A 117 ? ARG A 115 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 ILE A 16  ? N ILE A 16  O ILE A 43  ? O ILE A 43  
AA1 2 3 N TYR A 42  ? N TYR A 42  O MET A 139 ? O MET A 139 
AA1 3 4 N TYR A 140 ? N TYR A 140 O THR A 161 ? O THR A 161 
AA1 4 5 N LEU A 160 ? N LEU A 160 O HIS A 194 ? O HIS A 194 
AA1 5 6 N LYS A 191 ? N LYS A 191 O ILE A 228 ? O ILE A 228 
AA1 6 7 O ILE A 229 ? O ILE A 229 N ALA A 220 ? N ALA A 220 
AA1 7 8 O 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 ARG A 115 ? O ARG A 115 
AA2 1 2 N ILE A 16  ? N ILE A 16  O ILE A 43  ? O ILE A 43  
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 THR A 408 ? O THR A 408 N PHE A 332 ? N PHE A 332 
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 ILE A 431 ? N ILE A 431 O LYS A 510 ? O LYS A 510 
AA5 5 6 O HIS A 513 ? O HIS A 513 N TYR A 445 ? N TYR A 445 
AA6 1 2 O TYR A 369 ? O TYR A 369 N ALA A 361 ? N ALA A 361 
AA6 2 3 N GLU A 362 ? N GLU A 362 O THR A 384 ? O THR A 384 
AA6 3 4 N ILE A 383 ? N ILE A 383 O TRP A 391 ? O TRP A 391 
AA7 1 2 N SER A 462 ? N SER A 462 O MET A 476 ? O MET A 476 
AA8 1 2 N LYS A 551 ? N LYS A 551 O VAL A 558 ? O VAL A 558 
# 
_pdbx_entry_details.entry_id                   9EJ1 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 7   ? ? 51.68   -102.33 
2  1 SER A 108 ? ? -127.37 -78.93  
3  1 ARG A 129 ? ? -121.19 -50.16  
4  1 LYS A 243 ? ? -85.73  -91.99  
5  1 TRP A 260 ? ? -120.50 -162.02 
6  1 ASP A 311 ? ? -140.40 -40.95  
7  1 PHE A 333 ? ? -115.57 73.27   
8  1 ALA A 468 ? ? -121.26 -153.72 
9  1 PHE A 530 ? ? 53.36   -114.41 
10 1 LEU A 569 ? ? -114.01 -78.02  
11 1 ASN A 601 ? ? 59.49   -123.33 
# 
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 24.8000 -10.9028 -5.6369 0.1964 ? 0.0252  ? -0.0265 ? 0.3398 ? -0.0207 ? 0.2549 ? 1.6273 ? 1.1452 
? -0.7070 ? 4.6940 ? 0.5799 ? 2.2027 ? 0.0308  ? 0.0201  ? -0.0284 ? -0.2476 ? -0.0038 ? -0.2551 ? -0.0260 ? 0.3113 ? -0.0027 ? 
2 'X-RAY DIFFRACTION' ? refined 14.8123 -4.8338  11.9389 0.2682 ? -0.0671 ? 0.0468  ? 0.2652 ? -0.0330 ? 0.2461 ? 1.1271 ? 0.1066 
? -0.0120 ? 2.9494 ? 0.4961 ? 1.1565 ? 0.0402  ? -0.0912 ? -0.0953 ? 0.5618  ? -0.0819 ? 0.2508  ? 0.1136  ? 0.0867 ? 0.0452  ? 
3 'X-RAY DIFFRACTION' ? refined 18.6224 14.9376  17.7147 0.3656 ? -0.0271 ? -0.0144 ? 0.1722 ? 0.0388  ? 0.2122 ? 3.4323 ? 0.4601 
? -0.6588 ? 3.5873 ? 0.6302 ? 1.7921 ? -0.0487 ? -0.2197 ? -0.0703 ? 0.5425  ? -0.0342 ? -0.0150 ? -0.0062 ? 0.1551 ? 0.0538  ? 
# 
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 225 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 226 through 412 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 413 through 622 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A PRO 2 ? A PRO 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GTP PG     P  N N 137 
GTP O1G    O  N N 138 
GTP O2G    O  N N 139 
GTP O3G    O  N N 140 
GTP O3B    O  N N 141 
GTP PB     P  N N 142 
GTP O1B    O  N N 143 
GTP O2B    O  N N 144 
GTP O3A    O  N N 145 
GTP PA     P  N N 146 
GTP O1A    O  N N 147 
GTP O2A    O  N N 148 
GTP "O5'"  O  N N 149 
GTP "C5'"  C  N N 150 
GTP "C4'"  C  N R 151 
GTP "O4'"  O  N N 152 
GTP "C3'"  C  N S 153 
GTP "O3'"  O  N N 154 
GTP "C2'"  C  N R 155 
GTP "O2'"  O  N N 156 
GTP "C1'"  C  N R 157 
GTP N9     N  Y N 158 
GTP C8     C  Y N 159 
GTP N7     N  Y N 160 
GTP C5     C  Y N 161 
GTP C6     C  N N 162 
GTP O6     O  N N 163 
GTP N1     N  N N 164 
GTP C2     C  N N 165 
GTP N2     N  N N 166 
GTP N3     N  N N 167 
GTP C4     C  Y N 168 
GTP HOG2   H  N N 169 
GTP HOG3   H  N N 170 
GTP HOB2   H  N N 171 
GTP HOA2   H  N N 172 
GTP "H5'"  H  N N 173 
GTP "H5''" H  N N 174 
GTP "H4'"  H  N N 175 
GTP "H3'"  H  N N 176 
GTP "HO3'" H  N N 177 
GTP "H2'"  H  N N 178 
GTP "HO2'" H  N N 179 
GTP "H1'"  H  N N 180 
GTP H8     H  N N 181 
GTP HN1    H  N N 182 
GTP HN21   H  N N 183 
GTP HN22   H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
MN  MN     MN N N 298 
OXL C1     C  N N 299 
OXL C2     C  N N 300 
OXL O1     O  N N 301 
OXL O2     O  N N 302 
OXL O3     O  N N 303 
OXL O4     O  N N 304 
PGE C1     C  N N 305 
PGE O1     O  N N 306 
PGE C2     C  N N 307 
PGE O2     O  N N 308 
PGE C3     C  N N 309 
PGE C4     C  N N 310 
PGE O4     O  N N 311 
PGE C6     C  N N 312 
PGE C5     C  N N 313 
PGE O3     O  N N 314 
PGE H1     H  N N 315 
PGE H12    H  N N 316 
PGE HO1    H  N N 317 
PGE H2     H  N N 318 
PGE H22    H  N N 319 
PGE H3     H  N N 320 
PGE H32    H  N N 321 
PGE H4     H  N N 322 
PGE H42    H  N N 323 
PGE HO4    H  N N 324 
PGE H6     H  N N 325 
PGE H62    H  N N 326 
PGE H5     H  N N 327 
PGE H52    H  N N 328 
PHE N      N  N N 329 
PHE CA     C  N S 330 
PHE C      C  N N 331 
PHE O      O  N N 332 
PHE CB     C  N N 333 
PHE CG     C  Y N 334 
PHE CD1    C  Y N 335 
PHE CD2    C  Y N 336 
PHE CE1    C  Y N 337 
PHE CE2    C  Y N 338 
PHE CZ     C  Y N 339 
PHE OXT    O  N N 340 
PHE H      H  N N 341 
PHE H2     H  N N 342 
PHE HA     H  N N 343 
PHE HB2    H  N N 344 
PHE HB3    H  N N 345 
PHE HD1    H  N N 346 
PHE HD2    H  N N 347 
PHE HE1    H  N N 348 
PHE HE2    H  N N 349 
PHE HZ     H  N N 350 
PHE HXT    H  N N 351 
PRO N      N  N N 352 
PRO CA     C  N S 353 
PRO C      C  N N 354 
PRO O      O  N N 355 
PRO CB     C  N N 356 
PRO CG     C  N N 357 
PRO CD     C  N N 358 
PRO OXT    O  N N 359 
PRO H      H  N N 360 
PRO HA     H  N N 361 
PRO HB2    H  N N 362 
PRO HB3    H  N N 363 
PRO HG2    H  N N 364 
PRO HG3    H  N N 365 
PRO HD2    H  N N 366 
PRO HD3    H  N N 367 
PRO HXT    H  N N 368 
SER N      N  N N 369 
SER CA     C  N S 370 
SER C      C  N N 371 
SER O      O  N N 372 
SER CB     C  N N 373 
SER OG     O  N N 374 
SER OXT    O  N N 375 
SER H      H  N N 376 
SER H2     H  N N 377 
SER HA     H  N N 378 
SER HB2    H  N N 379 
SER HB3    H  N N 380 
SER HG     H  N N 381 
SER HXT    H  N N 382 
THR N      N  N N 383 
THR CA     C  N S 384 
THR C      C  N N 385 
THR O      O  N N 386 
THR CB     C  N R 387 
THR OG1    O  N N 388 
THR CG2    C  N N 389 
THR OXT    O  N N 390 
THR H      H  N N 391 
THR H2     H  N N 392 
THR HA     H  N N 393 
THR HB     H  N N 394 
THR HG1    H  N N 395 
THR HG21   H  N N 396 
THR HG22   H  N N 397 
THR HG23   H  N N 398 
THR HXT    H  N N 399 
TRP N      N  N N 400 
TRP CA     C  N S 401 
TRP C      C  N N 402 
TRP O      O  N N 403 
TRP CB     C  N N 404 
TRP CG     C  Y N 405 
TRP CD1    C  Y N 406 
TRP CD2    C  Y N 407 
TRP NE1    N  Y N 408 
TRP CE2    C  Y N 409 
TRP CE3    C  Y N 410 
TRP CZ2    C  Y N 411 
TRP CZ3    C  Y N 412 
TRP CH2    C  Y N 413 
TRP OXT    O  N N 414 
TRP H      H  N N 415 
TRP H2     H  N N 416 
TRP HA     H  N N 417 
TRP HB2    H  N N 418 
TRP HB3    H  N N 419 
TRP HD1    H  N N 420 
TRP HE1    H  N N 421 
TRP HE3    H  N N 422 
TRP HZ2    H  N N 423 
TRP HZ3    H  N N 424 
TRP HH2    H  N N 425 
TRP HXT    H  N N 426 
TYR N      N  N N 427 
TYR CA     C  N S 428 
TYR C      C  N N 429 
TYR O      O  N N 430 
TYR CB     C  N N 431 
TYR CG     C  Y N 432 
TYR CD1    C  Y N 433 
TYR CD2    C  Y N 434 
TYR CE1    C  Y N 435 
TYR CE2    C  Y N 436 
TYR CZ     C  Y N 437 
TYR OH     O  N N 438 
TYR OXT    O  N N 439 
TYR H      H  N N 440 
TYR H2     H  N N 441 
TYR HA     H  N N 442 
TYR HB2    H  N N 443 
TYR HB3    H  N N 444 
TYR HD1    H  N N 445 
TYR HD2    H  N N 446 
TYR HE1    H  N N 447 
TYR HE2    H  N N 448 
TYR HH     H  N N 449 
TYR HXT    H  N N 450 
VAL N      N  N N 451 
VAL CA     C  N S 452 
VAL C      C  N N 453 
VAL O      O  N N 454 
VAL CB     C  N N 455 
VAL CG1    C  N N 456 
VAL CG2    C  N N 457 
VAL OXT    O  N N 458 
VAL H      H  N N 459 
VAL H2     H  N N 460 
VAL HA     H  N N 461 
VAL HB     H  N N 462 
VAL HG11   H  N N 463 
VAL HG12   H  N N 464 
VAL HG13   H  N N 465 
VAL HG21   H  N N 466 
VAL HG22   H  N N 467 
VAL HG23   H  N N 468 
VAL HXT    H  N N 469 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GTP PG    O1G    doub N N 129 
GTP PG    O2G    sing N N 130 
GTP PG    O3G    sing N N 131 
GTP PG    O3B    sing N N 132 
GTP O2G   HOG2   sing N N 133 
GTP O3G   HOG3   sing N N 134 
GTP O3B   PB     sing N N 135 
GTP PB    O1B    doub N N 136 
GTP PB    O2B    sing N N 137 
GTP PB    O3A    sing N N 138 
GTP O2B   HOB2   sing N N 139 
GTP O3A   PA     sing N N 140 
GTP PA    O1A    doub N N 141 
GTP PA    O2A    sing N N 142 
GTP PA    "O5'"  sing N N 143 
GTP O2A   HOA2   sing N N 144 
GTP "O5'" "C5'"  sing N N 145 
GTP "C5'" "C4'"  sing N N 146 
GTP "C5'" "H5'"  sing N N 147 
GTP "C5'" "H5''" sing N N 148 
GTP "C4'" "O4'"  sing N N 149 
GTP "C4'" "C3'"  sing N N 150 
GTP "C4'" "H4'"  sing N N 151 
GTP "O4'" "C1'"  sing N N 152 
GTP "C3'" "O3'"  sing N N 153 
GTP "C3'" "C2'"  sing N N 154 
GTP "C3'" "H3'"  sing N N 155 
GTP "O3'" "HO3'" sing N N 156 
GTP "C2'" "O2'"  sing N N 157 
GTP "C2'" "C1'"  sing N N 158 
GTP "C2'" "H2'"  sing N N 159 
GTP "O2'" "HO2'" sing N N 160 
GTP "C1'" N9     sing N N 161 
GTP "C1'" "H1'"  sing N N 162 
GTP N9    C8     sing Y N 163 
GTP N9    C4     sing Y N 164 
GTP C8    N7     doub Y N 165 
GTP C8    H8     sing N N 166 
GTP N7    C5     sing Y N 167 
GTP C5    C6     sing N N 168 
GTP C5    C4     doub Y N 169 
GTP C6    O6     doub N N 170 
GTP C6    N1     sing N N 171 
GTP N1    C2     sing N N 172 
GTP N1    HN1    sing N N 173 
GTP C2    N2     sing N N 174 
GTP C2    N3     doub N N 175 
GTP N2    HN21   sing N N 176 
GTP N2    HN22   sing N N 177 
GTP N3    C4     sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
OXL C1    C2     sing N N 287 
OXL C1    O1     doub N N 288 
OXL C1    O3     sing N N 289 
OXL C2    O2     doub N N 290 
OXL C2    O4     sing N N 291 
PGE C1    O1     sing N N 292 
PGE C1    C2     sing N N 293 
PGE C1    H1     sing N N 294 
PGE C1    H12    sing N N 295 
PGE O1    HO1    sing N N 296 
PGE C2    O2     sing N N 297 
PGE C2    H2     sing N N 298 
PGE C2    H22    sing N N 299 
PGE O2    C3     sing N N 300 
PGE C3    C4     sing N N 301 
PGE C3    H3     sing N N 302 
PGE C3    H32    sing N N 303 
PGE C4    O3     sing N N 304 
PGE C4    H4     sing N N 305 
PGE C4    H42    sing N N 306 
PGE O4    C6     sing N N 307 
PGE O4    HO4    sing N N 308 
PGE C6    C5     sing N N 309 
PGE C6    H6     sing N N 310 
PGE C6    H62    sing N N 311 
PGE C5    O3     sing N N 312 
PGE C5    H5     sing N N 313 
PGE C5    H52    sing N N 314 
PHE N     CA     sing N N 315 
PHE N     H      sing N N 316 
PHE N     H2     sing N N 317 
PHE CA    C      sing N N 318 
PHE CA    CB     sing N N 319 
PHE CA    HA     sing N N 320 
PHE C     O      doub N N 321 
PHE C     OXT    sing N N 322 
PHE CB    CG     sing N N 323 
PHE CB    HB2    sing N N 324 
PHE CB    HB3    sing N N 325 
PHE CG    CD1    doub Y N 326 
PHE CG    CD2    sing Y N 327 
PHE CD1   CE1    sing Y N 328 
PHE CD1   HD1    sing N N 329 
PHE CD2   CE2    doub Y N 330 
PHE CD2   HD2    sing N N 331 
PHE CE1   CZ     doub Y N 332 
PHE CE1   HE1    sing N N 333 
PHE CE2   CZ     sing Y N 334 
PHE CE2   HE2    sing N N 335 
PHE CZ    HZ     sing N N 336 
PHE OXT   HXT    sing N N 337 
PRO N     CA     sing N N 338 
PRO N     CD     sing N N 339 
PRO N     H      sing N N 340 
PRO CA    C      sing N N 341 
PRO CA    CB     sing N N 342 
PRO CA    HA     sing N N 343 
PRO C     O      doub N N 344 
PRO C     OXT    sing N N 345 
PRO CB    CG     sing N N 346 
PRO CB    HB2    sing N N 347 
PRO CB    HB3    sing N N 348 
PRO CG    CD     sing N N 349 
PRO CG    HG2    sing N N 350 
PRO CG    HG3    sing N N 351 
PRO CD    HD2    sing N N 352 
PRO CD    HD3    sing N N 353 
PRO OXT   HXT    sing N N 354 
SER N     CA     sing N N 355 
SER N     H      sing N N 356 
SER N     H2     sing N N 357 
SER CA    C      sing N N 358 
SER CA    CB     sing N N 359 
SER CA    HA     sing N N 360 
SER C     O      doub N N 361 
SER C     OXT    sing N N 362 
SER CB    OG     sing N N 363 
SER CB    HB2    sing N N 364 
SER CB    HB3    sing N N 365 
SER OG    HG     sing N N 366 
SER OXT   HXT    sing N N 367 
THR N     CA     sing N N 368 
THR N     H      sing N N 369 
THR N     H2     sing N N 370 
THR CA    C      sing N N 371 
THR CA    CB     sing N N 372 
THR CA    HA     sing N N 373 
THR C     O      doub N N 374 
THR C     OXT    sing N N 375 
THR CB    OG1    sing N N 376 
THR CB    CG2    sing N N 377 
THR CB    HB     sing N N 378 
THR OG1   HG1    sing N N 379 
THR CG2   HG21   sing N N 380 
THR CG2   HG22   sing N N 381 
THR CG2   HG23   sing N N 382 
THR OXT   HXT    sing N N 383 
TRP N     CA     sing N N 384 
TRP N     H      sing N N 385 
TRP N     H2     sing N N 386 
TRP CA    C      sing N N 387 
TRP CA    CB     sing N N 388 
TRP CA    HA     sing N N 389 
TRP C     O      doub N N 390 
TRP C     OXT    sing N N 391 
TRP CB    CG     sing N N 392 
TRP CB    HB2    sing N N 393 
TRP CB    HB3    sing N N 394 
TRP CG    CD1    doub Y N 395 
TRP CG    CD2    sing Y N 396 
TRP CD1   NE1    sing Y N 397 
TRP CD1   HD1    sing N N 398 
TRP CD2   CE2    doub Y N 399 
TRP CD2   CE3    sing Y N 400 
TRP NE1   CE2    sing Y N 401 
TRP NE1   HE1    sing N N 402 
TRP CE2   CZ2    sing Y N 403 
TRP CE3   CZ3    doub Y N 404 
TRP CE3   HE3    sing N N 405 
TRP CZ2   CH2    doub Y N 406 
TRP CZ2   HZ2    sing N N 407 
TRP CZ3   CH2    sing Y N 408 
TRP CZ3   HZ3    sing N N 409 
TRP CH2   HH2    sing N N 410 
TRP OXT   HXT    sing N N 411 
TYR N     CA     sing N N 412 
TYR N     H      sing N N 413 
TYR N     H2     sing N N 414 
TYR CA    C      sing N N 415 
TYR CA    CB     sing N N 416 
TYR CA    HA     sing N N 417 
TYR C     O      doub N N 418 
TYR C     OXT    sing N N 419 
TYR CB    CG     sing N N 420 
TYR CB    HB2    sing N N 421 
TYR CB    HB3    sing N N 422 
TYR CG    CD1    doub Y N 423 
TYR CG    CD2    sing Y N 424 
TYR CD1   CE1    sing Y N 425 
TYR CD1   HD1    sing N N 426 
TYR CD2   CE2    doub Y N 427 
TYR CD2   HD2    sing N N 428 
TYR CE1   CZ     doub Y N 429 
TYR CE1   HE1    sing N N 430 
TYR CE2   CZ     sing Y N 431 
TYR CE2   HE2    sing N N 432 
TYR CZ    OH     sing N N 433 
TYR OH    HH     sing N N 434 
TYR OXT   HXT    sing N N 435 
VAL N     CA     sing N N 436 
VAL N     H      sing N N 437 
VAL N     H2     sing N N 438 
VAL CA    C      sing N N 439 
VAL CA    CB     sing N N 440 
VAL CA    HA     sing N N 441 
VAL C     O      doub N N 442 
VAL C     OXT    sing N N 443 
VAL CB    CG1    sing N N 444 
VAL CB    CG2    sing N N 445 
VAL CB    HB     sing N N 446 
VAL CG1   HG11   sing N N 447 
VAL CG1   HG12   sing N N 448 
VAL CG1   HG13   sing N N 449 
VAL CG2   HG21   sing N N 450 
VAL CG2   HG22   sing N N 451 
VAL CG2   HG23   sing N N 452 
VAL OXT   HXT    sing N N 453 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' DBI-2210041     1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 5R01GM127528-02 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3DT2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EJ1 
_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]   0.022068 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008764 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008345 
_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]   0.017689 
_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   ? 25.361  -15.514 -35.479 1.00 84.16  ? 3   PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? 25.897  -14.355 -34.756 1.00 76.89  ? 3   PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? 27.205  -14.660 -34.027 1.00 70.77  ? 3   PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? 27.783  -13.764 -33.415 1.00 70.38  ? 3   PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? 24.784  -14.017 -33.758 1.00 75.32  ? 3   PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? 24.027  -15.292 -33.586 1.00 85.49  ? 3   PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? 24.069  -15.959 -34.929 1.00 87.99  ? 3   PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? 27.659  -15.911 -34.096 1.00 65.21  ? 4   GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? 28.899  -16.326 -33.454 1.00 67.55  ? 4   GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? 29.601  -17.348 -34.339 1.00 63.22  ? 4   GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? 28.992  -17.955 -35.223 1.00 56.08  ? 4   GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? 28.642  -16.903 -32.053 1.00 68.03  ? 4   GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? 28.231  -15.855 -31.027 1.00 72.34  ? 4   GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? 27.524  -16.443 -29.823 1.00 77.80  ? 4   GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? 27.478  -17.659 -29.647 1.00 80.39  ? 4   GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? 26.956  -15.578 -28.991 1.00 77.08  ? 4   GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? 30.899  -17.528 -34.093 1.00 49.16  ? 5   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? 31.722  -18.421 -34.901 1.00 54.68  ? 5   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? 31.904  -19.802 -34.288 1.00 53.25  ? 5   LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? 32.111  -20.771 -35.026 1.00 51.86  ? 5   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? 33.102  -17.797 -35.144 1.00 48.52  ? 5   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? 33.130  -16.558 -36.041 1.00 54.66  ? 5   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? 34.550  -16.042 -36.213 1.00 44.08  ? 5   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? 32.501  -16.863 -37.393 1.00 49.01  ? 5   LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? 31.839  -19.917 -32.960 1.00 55.84  ? 6   HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? 31.980  -21.199 -32.280 1.00 57.05  ? 6   HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? 30.946  -21.352 -31.173 1.00 66.17  ? 6   HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? 31.181  -22.080 -30.200 1.00 69.31  ? 6   HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? 33.379  -21.363 -31.680 1.00 51.25  ? 6   HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? 34.490  -21.209 -32.669 1.00 57.48  ? 6   HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? 34.893  -22.232 -33.500 1.00 53.33  ? 6   HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? 35.297  -20.158 -32.948 1.00 53.46  ? 6   HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? 35.894  -21.815 -34.255 1.00 52.89  ? 6   HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? 36.158  -20.560 -33.940 1.00 48.79  ? 6   HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? 29.796  -20.688 -31.311 1.00 68.92  ? 7   ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? 28.896  -20.460 -30.186 1.00 79.78  ? 7   ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? 29.690  -19.849 -29.038 1.00 74.01  ? 7   ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? 30.001  -18.654 -29.062 1.00 76.33  ? 7   ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? 28.196  -21.752 -29.751 1.00 82.14  ? 7   ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? 27.075  -22.151 -30.691 1.00 91.67  ? 7   ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? 26.501  -21.309 -31.384 1.00 93.00  ? 7   ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? 26.751  -23.439 -30.714 1.00 89.60  ? 7   ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? 30.033  -20.654 -28.035 1.00 73.77  ? 8   GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? 30.899  -20.198 -26.964 1.00 73.18  ? 8   GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? 30.290  -19.159 -26.042 1.00 72.84  ? 8   GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? 30.481  -19.218 -24.824 1.00 77.27  ? 8   GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? 29.565  -18.196 -26.609 1.00 72.95  ? 9   LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? 28.920  -17.140 -25.842 1.00 71.30  ? 9   LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? 27.436  -17.395 -25.613 1.00 68.80  ? 9   LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? 26.779  -16.587 -24.950 1.00 68.49  ? 9   LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? 29.108  -15.792 -26.544 1.00 72.08  ? 9   LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? 30.539  -15.434 -26.948 1.00 73.64  ? 9   LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? 30.584  -14.076 -27.630 1.00 68.47  ? 9   LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? 31.456  -15.462 -25.739 1.00 67.06  ? 9   LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? 26.893  -18.487 -26.146 1.00 63.13  ? 10  ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? 25.490  -18.838 -25.954 1.00 64.09  ? 10  ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? 25.381  -19.752 -24.738 1.00 55.51  ? 10  ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? 25.748  -20.930 -24.802 1.00 56.88  ? 10  ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? 24.926  -19.506 -27.205 1.00 67.50  ? 10  ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? 23.422  -19.703 -27.138 1.00 63.51  ? 10  ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? 22.801  -19.251 -26.154 1.00 64.77  ? 10  ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? 22.859  -20.311 -28.071 1.00 78.71  ? 10  ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? 24.874  -19.210 -23.630 1.00 49.13  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 24.737  -19.948 -22.382 1.00 52.05  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 23.373  -20.615 -22.235 1.00 43.79  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 23.013  -21.023 -21.124 1.00 40.65  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 24.995  -19.020 -21.191 1.00 45.89  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 26.445  -18.901 -20.820 1.00 49.79  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 27.309  -18.127 -21.577 1.00 49.87  ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 26.944  -19.561 -19.707 1.00 51.76  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 28.647  -18.017 -21.234 1.00 55.07  ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 28.279  -19.456 -19.357 1.00 48.37  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 29.131  -18.683 -20.122 1.00 44.98  ? 11  PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? 22.617  -20.743 -23.329 1.00 45.83  ? 12  SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? 21.283  -21.331 -23.249 1.00 47.13  ? 12  SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? 21.331  -22.761 -22.726 1.00 46.49  ? 12  SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? 20.444  -23.184 -21.975 1.00 44.64  ? 12  SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? 20.606  -21.285 -24.620 1.00 52.53  ? 12  SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? 20.357  -19.949 -25.020 1.00 62.20  ? 12  SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? 22.362  -23.520 -23.103 1.00 47.42  ? 13  ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? 22.474  -24.911 -22.678 1.00 43.66  ? 13  ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? 22.746  -25.063 -21.186 1.00 42.97  ? 13  ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? 22.603  -26.172 -20.662 1.00 43.84  ? 13  ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? 23.573  -25.617 -23.474 1.00 44.93  ? 13  ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? 23.126  -23.992 -20.491 1.00 41.18  ? 14  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? 23.422  -24.057 -19.065 1.00 42.48  ? 14  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? 22.291  -23.517 -18.195 1.00 35.87  ? 14  LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? 22.464  -23.401 -16.977 1.00 33.85  ? 14  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? 24.720  -23.306 -18.762 1.00 39.42  ? 14  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? 25.978  -24.063 -19.159 1.00 43.93  ? 14  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? 27.227  -23.355 -18.658 1.00 50.98  ? 14  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? 28.355  -24.341 -18.394 1.00 52.38  ? 14  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? 28.725  -25.125 -19.603 1.00 64.01  ? 14  LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? 21.143  -23.193 -18.783 1.00 34.53  ? 15  VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? 20.024  -22.620 -18.042 1.00 36.70  ? 15  VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? 19.148  -23.750 -17.515 1.00 34.69  ? 15  VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? 18.538  -24.490 -18.294 1.00 40.41  ? 15  VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? 19.211  -21.656 -18.919 1.00 37.31  ? 15  VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? 18.009  -21.131 -18.148 1.00 34.00  ? 15  VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? 20.087  -20.504 -19.394 1.00 35.54  ? 15  VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? 19.074  -23.873 -16.187 1.00 31.62  ? 16  ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? 18.287  -24.927 -15.551 1.00 34.49  ? 16  ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? 16.891  -24.469 -15.141 1.00 34.96  ? 16  ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? 16.077  -25.309 -14.727 1.00 34.23  ? 16  ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? 19.026  -25.510 -14.327 1.00 35.52  ? 16  ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? 19.427  -24.396 -13.362 1.00 35.16  ? 16  ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? 20.244  -26.306 -14.778 1.00 33.68  ? 16  ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? 20.091  -24.896 -12.082 1.00 36.21  ? 16  ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? 16.591  -23.174 -15.228 1.00 33.43  ? 17  GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? 15.227  -22.693 -15.046 1.00 35.70  ? 17  GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? 15.075  -21.367 -15.773 1.00 37.10  ? 17  GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? 15.862  -20.444 -15.552 1.00 33.18  ? 17  GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? 14.863  -22.523 -13.565 1.00 32.72  ? 17  GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? 13.498  -21.871 -13.377 1.00 38.34  ? 17  GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? 13.057  -21.803 -11.931 1.00 39.84  ? 17  GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? 13.111  -22.795 -11.205 1.00 43.55  ? 17  GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? 12.610  -20.628 -11.507 1.00 36.85  ? 17  GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? 14.066  -21.277 -16.629 1.00 39.17  ? 18  GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? 13.814  -20.071 -17.387 1.00 32.88  ? 18  GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? 14.436  -20.121 -18.766 1.00 39.08  ? 18  GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? 14.953  -21.143 -19.226 1.00 45.34  ? 18  GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? 14.381  -18.974 -19.435 1.00 45.36  ? 19  SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? 14.886  -18.845 -20.793 1.00 44.19  ? 19  SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? 15.567  -17.497 -20.947 1.00 42.49  ? 19  SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? 15.034  -16.476 -20.502 1.00 45.55  ? 19  SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? 13.753  -18.984 -21.819 1.00 40.27  ? 19  SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? 14.226  -18.775 -23.138 1.00 51.94  ? 19  SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? 16.748  -17.497 -21.569 1.00 43.52  ? 20  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? 17.385  -16.234 -21.922 1.00 47.87  ? 20  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? 16.585  -15.495 -22.987 1.00 54.62  ? 20  LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? 16.649  -14.263 -23.068 1.00 54.67  ? 20  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? 18.817  -16.479 -22.399 1.00 49.25  ? 20  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? 19.793  -17.084 -21.387 1.00 52.09  ? 20  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? 21.149  -17.338 -22.030 1.00 50.27  ? 20  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? 19.938  -16.186 -20.171 1.00 49.03  ? 20  LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? 15.827  -16.230 -23.807 1.00 53.52  ? 21  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? 14.960  -15.598 -24.796 1.00 61.63  ? 21  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? 13.863  -14.777 -24.134 1.00 60.90  ? 21  ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? 13.459  -13.737 -24.666 1.00 66.51  ? 21  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? 14.347  -16.662 -25.706 1.00 62.40  ? 21  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? 15.391  -17.538 -26.364 1.00 73.27  ? 21  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? 16.299  -16.991 -27.025 1.00 76.54  ? 21  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? 15.309  -18.776 -26.212 1.00 78.12  ? 21  ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? 13.369  -15.225 -22.978 1.00 57.50  ? 22  SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? 12.345  -14.485 -22.252 1.00 60.50  ? 22  SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? 12.882  -13.226 -21.590 1.00 52.98  ? 22  SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? 12.087  -12.432 -21.075 1.00 60.22  ? 22  SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? 11.699  -15.381 -21.194 1.00 54.57  ? 22  SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? 11.027  -16.474 -21.795 1.00 72.75  ? 22  SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? 14.192  -13.023 -21.587 1.00 56.31  ? 23  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? 14.713  -11.847 -20.911 1.00 54.34  ? 23  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? 14.693  -10.634 -21.835 1.00 57.89  ? 23  LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? 14.816  -10.772 -23.057 1.00 55.73  ? 23  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? 16.142  -12.094 -20.435 1.00 51.35  ? 23  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? 16.337  -13.107 -19.308 1.00 50.39  ? 23  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? 17.817  -13.288 -19.011 1.00 53.31  ? 23  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? 15.588  -12.664 -18.060 1.00 50.99  ? 23  LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? 14.522  -9.440  -21.270 1.00 55.82  ? 24  PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? 14.733  -8.220  -22.053 1.00 58.94  ? 24  PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? 16.169  -8.141  -22.550 1.00 58.34  ? 24  PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? 17.086  -8.742  -21.985 1.00 56.18  ? 24  PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? 14.420  -7.098  -21.057 1.00 57.77  ? 24  PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? 13.520  -7.736  -20.048 1.00 56.07  ? 24  PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? 13.993  -9.153  -19.926 1.00 53.58  ? 24  PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? 16.353  -7.376  -23.630 1.00 61.66  ? 25  GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? 17.641  -7.320  -24.315 1.00 65.19  ? 25  GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? 18.772  -6.950  -23.361 1.00 54.60  ? 25  GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? 19.769  -7.671  -23.248 1.00 48.91  ? 25  GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? 17.569  -6.324  -25.474 1.00 68.97  ? 25  GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? 18.871  -6.179  -26.245 1.00 79.65  ? 25  GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? 18.809  -5.086  -27.294 1.00 90.45  ? 25  GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? 17.967  -4.190  -27.224 1.00 95.66  ? 25  GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? 19.700  -5.156  -28.276 1.00 94.92  ? 25  GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? 18.631  -5.821  -22.662 1.00 52.95  ? 26  GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? 19.682  -5.373  -21.757 1.00 51.39  ? 26  GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? 19.860  -6.302  -20.565 1.00 50.01  ? 26  GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? 20.940  -6.320  -19.965 1.00 48.23  ? 26  GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? 19.389  -3.953  -21.273 1.00 54.18  ? 26  GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? 19.411  -2.913  -22.381 1.00 64.83  ? 26  GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? 20.735  -2.878  -23.122 1.00 67.66  ? 26  GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? 21.789  -3.070  -22.478 1.00 60.73  ? 26  GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? 20.720  -2.666  -24.353 1.00 72.09  ? 26  GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? 18.832  -7.070  -20.206 1.00 52.82  ? 27  VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? 18.971  -8.012  -19.102 1.00 46.78  ? 27  VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? 19.756  -9.241  -19.541 1.00 43.18  ? 27  VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? 20.622  -9.729  -18.806 1.00 40.70  ? 27  VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? 17.588  -8.386  -18.540 1.00 49.11  ? 27  VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? 17.725  -9.406  -17.418 1.00 35.41  ? 27  VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? 16.867  -7.143  -18.044 1.00 48.79  ? 27  VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? 19.474  -9.761  -20.740 1.00 41.15  ? 28  ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? 20.221  -10.917 -21.225 1.00 46.22  ? 28  ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? 21.695  -10.582 -21.411 1.00 42.70  ? 28  ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? 22.569  -11.386 -21.064 1.00 49.37  ? 28  ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? 19.628  -11.440 -22.535 1.00 46.80  ? 28  ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? 20.411  -12.622 -23.093 1.00 48.11  ? 28  ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? 19.715  -13.324 -24.248 1.00 55.51  ? 28  ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? 20.438  -14.535 -24.622 1.00 50.34  ? 28  ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? 20.020  -15.421 -25.517 1.00 64.18  ? 28  ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? 18.879  -15.261 -26.168 1.00 51.81  ? 28  ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? 20.765  -16.496 -25.762 1.00 63.04  ? 28  ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? 21.991  -9.400  -21.958 1.00 41.74  ? 29  LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? 23.382  -8.977  -22.103 1.00 41.42  ? 29  LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? 24.089  -8.941  -20.754 1.00 40.39  ? 29  LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? 25.254  -9.342  -20.643 1.00 39.92  ? 29  LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? 23.447  -7.606  -22.777 1.00 46.43  ? 29  LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? 22.949  -7.587  -24.217 1.00 58.26  ? 29  LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? 23.030  -6.185  -24.806 1.00 62.91  ? 29  LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? 22.546  -6.154  -26.246 1.00 74.83  ? 29  LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? 23.393  -6.991  -27.142 1.00 86.82  ? 29  LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? 23.397  -8.467  -19.716 1.00 36.09  ? 30  PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? 23.981  -8.431  -18.378 1.00 34.45  ? 30  PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? 24.219  -9.839  -17.842 1.00 37.17  ? 30  PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? 25.265  -10.111 -17.240 1.00 40.05  ? 30  PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? 23.068  -7.631  -17.445 1.00 35.09  ? 30  PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? 23.563  -7.535  -16.028 1.00 32.30  ? 30  PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? 24.796  -6.972  -15.745 1.00 33.93  ? 30  PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? 22.778  -7.979  -14.976 1.00 35.41  ? 30  PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? 25.248  -6.876  -14.439 1.00 33.84  ? 30  PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? 23.223  -7.880  -13.665 1.00 31.33  ? 30  PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? 24.460  -7.329  -13.399 1.00 34.81  ? 30  PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? 23.266  -10.749 -18.060 1.00 38.42  ? 31  VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? 23.430  -12.125 -17.597 1.00 37.75  ? 31  VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? 24.559  -12.813 -18.356 1.00 39.67  ? 31  VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? 25.485  -13.369 -17.754 1.00 35.01  ? 31  VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? 22.108  -12.903 -17.735 1.00 38.97  ? 31  VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? 22.326  -14.379 -17.433 1.00 34.84  ? 31  VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? 21.046  -12.327 -16.812 1.00 35.22  ? 31  VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? 24.500  -12.783 -19.690 1.00 38.11  ? 32  GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? 25.463  -13.539 -20.486 1.00 43.38  ? 32  GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? 26.866  -12.955 -20.378 1.00 41.15  ? 32  GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? 27.852  -13.702 -20.389 1.00 40.91  ? 32  GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? 25.015  -13.595 -21.946 1.00 44.27  ? 32  GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? 23.971  -14.666 -22.219 1.00 56.26  ? 32  GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? 23.676  -14.839 -23.696 1.00 55.45  ? 32  GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? 23.810  -13.853 -24.450 1.00 57.64  ? 32  GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? 23.314  -15.963 -24.100 1.00 58.64  ? 32  GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? 26.978  -11.629 -20.276 1.00 41.65  ? 33  GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? 28.292  -11.015 -20.160 1.00 40.99  ? 33  GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? 29.034  -11.450 -18.911 1.00 38.05  ? 33  GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? 30.223  -11.773 -18.963 1.00 39.47  ? 33  GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? 28.341  -11.477 -17.773 1.00 35.52  ? 34  ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? 28.970  -11.911 -16.531 1.00 37.85  ? 34  ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? 29.062  -13.426 -16.417 1.00 39.07  ? 34  ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? 29.931  -13.926 -15.694 1.00 38.43  ? 34  ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? 28.213  -11.341 -15.333 1.00 35.18  ? 34  ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? 28.400  -9.848  -15.194 1.00 41.14  ? 34  ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? 29.439  -9.385  -14.722 1.00 43.44  ? 34  ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? 27.398  -9.082  -15.613 1.00 38.98  ? 34  ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? 28.191  -14.166 -17.107 1.00 38.69  ? 35  ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? 28.357  -15.613 -17.171 1.00 36.19  ? 35  ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? 29.632  -15.977 -17.919 1.00 42.70  ? 35  ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? 30.317  -16.943 -17.562 1.00 43.23  ? 35  ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? 27.140  -16.257 -17.834 1.00 39.33  ? 35  ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? 29.970  -15.209 -18.956 1.00 39.89  ? 36  GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? 31.232  -15.424 -19.653 1.00 44.74  ? 36  GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? 32.418  -15.125 -18.743 1.00 40.25  ? 36  GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? 33.446  -15.809 -18.804 1.00 43.43  ? 36  GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? 31.285  -14.556 -20.911 1.00 50.72  ? 36  GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? 32.510  -14.778 -21.779 1.00 62.71  ? 36  GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? 32.604  -13.777 -22.915 1.00 79.17  ? 36  GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? 31.793  -12.855 -23.014 1.00 82.68  ? 36  GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? 33.598  -13.953 -23.780 1.00 71.15  ? 36  GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? 32.286  -14.117 -17.880 1.00 39.85  ? 37  LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? 33.402  -13.705 -17.035 1.00 41.62  ? 37  LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? 33.553  -14.607 -15.815 1.00 40.48  ? 37  LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? 34.663  -15.039 -15.488 1.00 41.71  ? 37  LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? 33.214  -12.252 -16.596 1.00 43.69  ? 37  LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? 34.226  -11.754 -15.563 1.00 46.18  ? 37  LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? 35.531  -11.355 -16.231 1.00 48.22  ? 37  LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? 33.645  -10.605 -14.762 1.00 49.98  ? 37  LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? 32.450  -14.890 -15.123 1.00 42.26  ? 38  CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? 32.503  -15.665 -13.890 1.00 41.50  ? 38  CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? 32.480  -17.169 -14.127 1.00 41.72  ? 38  CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? 32.834  -17.928 -13.216 1.00 43.08  ? 38  CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? 31.341  -15.272 -12.973 1.00 36.06  ? 38  CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? 31.301  -13.515 -12.550 1.00 40.47  ? 38  CYS A SG    1 
ATOM   277  N  N     A GLN A 1 39  ? 32.075  -17.608 -15.314 0.50 41.94  ? 39  GLN A N     1 
ATOM   278  N  N     B GLN A 1 39  ? 32.075  -17.607 -15.315 0.50 41.94  ? 39  GLN A N     1 
ATOM   279  C  CA    A GLN A 1 39  ? 32.044  -19.021 -15.678 0.50 41.86  ? 39  GLN A CA    1 
ATOM   280  C  CA    B GLN A 1 39  ? 32.039  -19.018 -15.683 0.50 41.85  ? 39  GLN A CA    1 
ATOM   281  C  C     A GLN A 1 39  ? 31.250  -19.881 -14.689 0.50 41.23  ? 39  GLN A C     1 
ATOM   282  C  C     B GLN A 1 39  ? 31.249  -19.881 -14.693 0.50 41.23  ? 39  GLN A C     1 
ATOM   283  O  O     A GLN A 1 39  ? 31.802  -20.797 -14.075 0.50 41.65  ? 39  GLN A O     1 
ATOM   284  O  O     B GLN A 1 39  ? 31.802  -20.799 -14.083 0.50 41.65  ? 39  GLN A O     1 
ATOM   285  C  CB    A GLN A 1 39  ? 33.461  -19.558 -15.830 0.50 45.36  ? 39  GLN A CB    1 
ATOM   286  C  CB    B GLN A 1 39  ? 33.453  -19.558 -15.849 0.50 45.36  ? 39  GLN A CB    1 
ATOM   287  C  CG    A GLN A 1 39  ? 34.220  -18.996 -17.018 0.50 46.11  ? 39  GLN A CG    1 
ATOM   288  C  CG    B GLN A 1 39  ? 34.315  -18.753 -16.805 0.50 45.87  ? 39  GLN A CG    1 
ATOM   289  C  CD    A GLN A 1 39  ? 33.706  -19.531 -18.338 0.50 45.07  ? 39  GLN A CD    1 
ATOM   290  C  CD    B GLN A 1 39  ? 35.697  -19.348 -16.980 0.50 47.53  ? 39  GLN A CD    1 
ATOM   291  O  OE1   A GLN A 1 39  ? 33.535  -20.738 -18.507 0.50 51.37  ? 39  GLN A OE1   1 
ATOM   292  O  OE1   B GLN A 1 39  ? 35.842  -20.532 -17.281 0.50 51.21  ? 39  GLN A OE1   1 
ATOM   293  N  NE2   A GLN A 1 39  ? 33.450  -18.633 -19.281 0.50 48.40  ? 39  GLN A NE2   1 
ATOM   294  N  NE2   B GLN A 1 39  ? 36.722  -18.527 -16.785 0.50 48.50  ? 39  GLN A NE2   1 
ATOM   295  N  N     . PRO A 1 40  ? 29.954  -19.621 -14.521 1.00 41.19  ? 40  PRO A N     1 
ATOM   296  C  CA    . PRO A 1 40  ? 29.142  -20.506 -13.682 1.00 41.41  ? 40  PRO A CA    1 
ATOM   297  C  C     . PRO A 1 40  ? 28.838  -21.799 -14.421 1.00 37.93  ? 40  PRO A C     1 
ATOM   298  O  O     . PRO A 1 40  ? 28.869  -21.867 -15.651 1.00 36.67  ? 40  PRO A O     1 
ATOM   299  C  CB    . PRO A 1 40  ? 27.871  -19.692 -13.431 1.00 38.44  ? 40  PRO A CB    1 
ATOM   300  C  CG    . PRO A 1 40  ? 27.739  -18.859 -14.653 1.00 36.30  ? 40  PRO A CG    1 
ATOM   301  C  CD    . PRO A 1 40  ? 29.144  -18.526 -15.089 1.00 38.52  ? 40  PRO A CD    1 
ATOM   302  N  N     . GLU A 1 41  ? 28.552  -22.845 -13.646 1.00 37.54  ? 41  GLU A N     1 
ATOM   303  C  CA    . GLU A 1 41  ? 28.197  -24.122 -14.253 1.00 37.12  ? 41  GLU A CA    1 
ATOM   304  C  C     . GLU A 1 41  ? 26.736  -24.161 -14.684 1.00 41.17  ? 41  GLU A C     1 
ATOM   305  O  O     . GLU A 1 41  ? 26.410  -24.789 -15.698 1.00 40.55  ? 41  GLU A O     1 
ATOM   306  C  CB    . GLU A 1 41  ? 28.496  -25.267 -13.283 1.00 44.39  ? 41  GLU A CB    1 
ATOM   307  C  CG    . GLU A 1 41  ? 28.318  -26.661 -13.877 1.00 43.04  ? 41  GLU A CG    1 
ATOM   308  C  CD    . GLU A 1 41  ? 29.310  -26.965 -14.984 1.00 58.45  ? 41  GLU A CD    1 
ATOM   309  O  OE1   . GLU A 1 41  ? 30.352  -26.280 -15.062 1.00 59.24  ? 41  GLU A OE1   1 
ATOM   310  O  OE2   . GLU A 1 41  ? 29.048  -27.892 -15.779 1.00 67.57  ? 41  GLU A OE2   1 
ATOM   311  N  N     . TYR A 1 42  ? 25.853  -23.498 -13.938 1.00 35.92  ? 42  TYR A N     1 
ATOM   312  C  CA    . TYR A 1 42  ? 24.433  -23.452 -14.250 1.00 37.67  ? 42  TYR A CA    1 
ATOM   313  C  C     . TYR A 1 42  ? 23.935  -22.022 -14.109 1.00 35.30  ? 42  TYR A C     1 
ATOM   314  O  O     . TYR A 1 42  ? 24.513  -21.219 -13.373 1.00 35.40  ? 42  TYR A O     1 
ATOM   315  C  CB    . TYR A 1 42  ? 23.610  -24.363 -13.326 1.00 33.15  ? 42  TYR A CB    1 
ATOM   316  C  CG    . TYR A 1 42  ? 24.159  -25.762 -13.162 1.00 39.03  ? 42  TYR A CG    1 
ATOM   317  C  CD1   . TYR A 1 42  ? 23.852  -26.762 -14.075 1.00 43.64  ? 42  TYR A CD1   1 
ATOM   318  C  CD2   . TYR A 1 42  ? 24.973  -26.087 -12.084 1.00 42.35  ? 42  TYR A CD2   1 
ATOM   319  C  CE1   . TYR A 1 42  ? 24.346  -28.044 -13.923 1.00 44.99  ? 42  TYR A CE1   1 
ATOM   320  C  CE2   . TYR A 1 42  ? 25.471  -27.366 -11.925 1.00 41.32  ? 42  TYR A CE2   1 
ATOM   321  C  CZ    . TYR A 1 42  ? 25.154  -28.339 -12.846 1.00 44.70  ? 42  TYR A CZ    1 
ATOM   322  O  OH    . TYR A 1 42  ? 25.651  -29.611 -12.690 1.00 53.73  ? 42  TYR A OH    1 
ATOM   323  N  N     . ILE A 1 43  ? 22.850  -21.713 -14.815 1.00 38.30  ? 43  ILE A N     1 
ATOM   324  C  CA    . ILE A 1 43  ? 22.165  -20.432 -14.691 1.00 31.67  ? 43  ILE A CA    1 
ATOM   325  C  C     . ILE A 1 43  ? 20.713  -20.703 -14.322 1.00 29.56  ? 43  ILE A C     1 
ATOM   326  O  O     . ILE A 1 43  ? 20.034  -21.496 -14.984 1.00 34.77  ? 43  ILE A O     1 
ATOM   327  C  CB    . ILE A 1 43  ? 22.263  -19.599 -15.981 1.00 31.44  ? 43  ILE A CB    1 
ATOM   328  C  CG1   . ILE A 1 43  ? 23.728  -19.345 -16.336 1.00 33.61  ? 43  ILE A CG1   1 
ATOM   329  C  CG2   . ILE A 1 43  ? 21.523  -18.284 -15.817 1.00 28.39  ? 43  ILE A CG2   1 
ATOM   330  C  CD1   . ILE A 1 43  ? 23.921  -18.553 -17.609 1.00 37.92  ? 43  ILE A CD1   1 
ATOM   331  N  N     . HIS A 1 44  ? 20.248  -20.051 -13.260 1.00 30.54  ? 44  HIS A N     1 
ATOM   332  C  CA    . HIS A 1 44  ? 18.896  -20.219 -12.738 1.00 30.30  ? 44  HIS A CA    1 
ATOM   333  C  C     . HIS A 1 44  ? 18.228  -18.851 -12.719 1.00 29.17  ? 44  HIS A C     1 
ATOM   334  O  O     . HIS A 1 44  ? 18.609  -17.981 -11.928 1.00 24.96  ? 44  HIS A O     1 
ATOM   335  C  CB    . HIS A 1 44  ? 18.930  -20.842 -11.340 1.00 27.26  ? 44  HIS A CB    1 
ATOM   336  C  CG    . HIS A 1 44  ? 17.584  -20.987 -10.697 1.00 29.95  ? 44  HIS A CG    1 
ATOM   337  N  ND1   . HIS A 1 44  ? 17.050  -22.212 -10.358 1.00 32.19  ? 44  HIS A ND1   1 
ATOM   338  C  CD2   . HIS A 1 44  ? 16.672  -20.062 -10.314 1.00 26.80  ? 44  HIS A CD2   1 
ATOM   339  C  CE1   . HIS A 1 44  ? 15.863  -22.036 -9.804  1.00 29.99  ? 44  HIS A CE1   1 
ATOM   340  N  NE2   . HIS A 1 44  ? 15.610  -20.740 -9.765  1.00 31.66  ? 44  HIS A NE2   1 
ATOM   341  N  N     . ILE A 1 45  ? 17.237  -18.659 -13.584 1.00 29.18  ? 45  ILE A N     1 
ATOM   342  C  CA    . ILE A 1 45  ? 16.459  -17.426 -13.613 1.00 26.11  ? 45  ILE A CA    1 
ATOM   343  C  C     . ILE A 1 45  ? 15.321  -17.573 -12.608 1.00 30.98  ? 45  ILE A C     1 
ATOM   344  O  O     . ILE A 1 45  ? 14.416  -18.391 -12.794 1.00 32.42  ? 45  ILE A O     1 
ATOM   345  C  CB    . ILE A 1 45  ? 15.929  -17.126 -15.020 1.00 37.47  ? 45  ILE A CB    1 
ATOM   346  C  CG1   . ILE A 1 45  ? 17.093  -17.009 -16.009 1.00 34.08  ? 45  ILE A CG1   1 
ATOM   347  C  CG2   . ILE A 1 45  ? 15.091  -15.850 -15.014 1.00 33.57  ? 45  ILE A CG2   1 
ATOM   348  C  CD1   . ILE A 1 45  ? 16.657  -16.885 -17.454 1.00 41.59  ? 45  ILE A CD1   1 
ATOM   349  N  N     . CYS A 1 46  ? 15.362  -16.774 -11.545 1.00 26.11  ? 46  CYS A N     1 
ATOM   350  C  CA    . CYS A 1 46  ? 14.393  -16.911 -10.467 1.00 27.40  ? 46  CYS A CA    1 
ATOM   351  C  C     . CYS A 1 46  ? 13.008  -16.446 -10.902 1.00 33.54  ? 46  CYS A C     1 
ATOM   352  O  O     . CYS A 1 46  ? 12.862  -15.445 -11.610 1.00 28.59  ? 46  CYS A O     1 
ATOM   353  C  CB    . CYS A 1 46  ? 14.848  -16.119 -9.245  1.00 28.40  ? 46  CYS A CB    1 
ATOM   354  S  SG    . CYS A 1 46  ? 16.386  -16.723 -8.510  1.00 26.21  ? 46  CYS A SG    1 
ATOM   355  N  N     . ASP A 1 47  ? 11.984  -17.182 -10.470 1.00 31.19  ? 47  ASP A N     1 
ATOM   356  C  CA    . ASP A 1 47  ? 10.600  -16.791 -10.696 1.00 38.23  ? 47  ASP A CA    1 
ATOM   357  C  C     . ASP A 1 47  ? 9.878   -16.397 -9.414  1.00 33.22  ? 47  ASP A C     1 
ATOM   358  O  O     . ASP A 1 47  ? 8.709   -16.003 -9.475  1.00 30.69  ? 47  ASP A O     1 
ATOM   359  C  CB    . ASP A 1 47  ? 9.832   -17.913 -11.415 1.00 38.47  ? 47  ASP A CB    1 
ATOM   360  C  CG    . ASP A 1 47  ? 9.745   -19.205 -10.604 1.00 39.15  ? 47  ASP A CG    1 
ATOM   361  O  OD1   . ASP A 1 47  ? 10.128  -19.223 -9.415  1.00 33.32  ? 47  ASP A OD1   1 
ATOM   362  O  OD2   . ASP A 1 47  ? 9.284   -20.219 -11.173 1.00 37.34  ? 47  ASP A OD2   1 
ATOM   363  N  N     . GLY A 1 48  ? 10.539  -16.490 -8.261  1.00 29.61  ? 48  GLY A N     1 
ATOM   364  C  CA    . GLY A 1 48  ? 9.935   -16.090 -7.005  1.00 29.78  ? 48  GLY A CA    1 
ATOM   365  C  C     . GLY A 1 48  ? 8.803   -16.965 -6.519  1.00 32.38  ? 48  GLY A C     1 
ATOM   366  O  O     . GLY A 1 48  ? 8.059   -16.550 -5.625  1.00 27.98  ? 48  GLY A O     1 
ATOM   367  N  N     . SER A 1 49  ? 8.650   -18.165 -7.071  1.00 34.35  ? 49  SER A N     1 
ATOM   368  C  CA    . SER A 1 49  ? 7.524   -19.014 -6.718  1.00 39.02  ? 49  SER A CA    1 
ATOM   369  C  C     . SER A 1 49  ? 7.780   -19.752 -5.407  1.00 37.66  ? 49  SER A C     1 
ATOM   370  O  O     . SER A 1 49  ? 8.918   -19.886 -4.944  1.00 34.99  ? 49  SER A O     1 
ATOM   371  C  CB    . SER A 1 49  ? 7.240   -20.021 -7.831  1.00 35.79  ? 49  SER A CB    1 
ATOM   372  O  OG    . SER A 1 49  ? 8.281   -20.977 -7.936  1.00 34.33  ? 49  SER A OG    1 
ATOM   373  N  N     . GLU A 1 50  ? 6.688   -20.236 -4.808  1.00 41.25  ? 50  GLU A N     1 
ATOM   374  C  CA    . GLU A 1 50  ? 6.797   -21.053 -3.604  1.00 43.59  ? 50  GLU A CA    1 
ATOM   375  C  C     . GLU A 1 50  ? 7.541   -22.352 -3.883  1.00 39.93  ? 50  GLU A C     1 
ATOM   376  O  O     . GLU A 1 50  ? 8.302   -22.835 -3.036  1.00 39.82  ? 50  GLU A O     1 
ATOM   377  C  CB    . GLU A 1 50  ? 5.406   -21.347 -3.039  1.00 49.11  ? 50  GLU A CB    1 
ATOM   378  C  CG    . GLU A 1 50  ? 4.712   -20.149 -2.408  1.00 53.37  ? 50  GLU A CG    1 
ATOM   379  C  CD    . GLU A 1 50  ? 5.309   -19.765 -1.066  1.00 67.11  ? 50  GLU A CD    1 
ATOM   380  O  OE1   . GLU A 1 50  ? 6.127   -20.545 -0.530  1.00 65.75  ? 50  GLU A OE1   1 
ATOM   381  O  OE2   . GLU A 1 50  ? 4.959   -18.684 -0.546  1.00 77.27  ? 50  GLU A OE2   1 
ATOM   382  N  N     . GLU A 1 51  ? 7.326   -22.939 -5.064  1.00 41.40  ? 51  GLU A N     1 
ATOM   383  C  CA    . GLU A 1 51  ? 8.037   -24.162 -5.427  1.00 41.51  ? 51  GLU A CA    1 
ATOM   384  C  C     . GLU A 1 51  ? 9.538   -23.918 -5.518  1.00 48.05  ? 51  GLU A C     1 
ATOM   385  O  O     . GLU A 1 51  ? 10.340  -24.754 -5.088  1.00 43.09  ? 51  GLU A O     1 
ATOM   386  C  CB    . GLU A 1 51  ? 7.505   -24.709 -6.753  1.00 48.60  ? 51  GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 51  ? 6.076   -25.244 -6.702  1.00 59.64  ? 51  GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 51  ? 5.021   -24.149 -6.749  1.00 67.23  ? 51  GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 51  ? 5.392   -22.955 -6.769  1.00 56.91  ? 51  GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 51  ? 3.818   -24.486 -6.769  1.00 76.98  ? 51  GLU A OE2   1 
ATOM   391  N  N     . GLU A 1 52  ? 9.934   -22.773 -6.078  1.00 42.56  ? 52  GLU A N     1 
ATOM   392  C  CA    . GLU A 1 52  ? 11.351  -22.444 -6.186  1.00 38.61  ? 52  GLU A CA    1 
ATOM   393  C  C     . GLU A 1 52  ? 11.979  -22.259 -4.809  1.00 37.49  ? 52  GLU A C     1 
ATOM   394  O  O     . GLU A 1 52  ? 13.074  -22.765 -4.540  1.00 37.52  ? 52  GLU A O     1 
ATOM   395  C  CB    . GLU A 1 52  ? 11.517  -21.188 -7.038  1.00 34.67  ? 52  GLU A CB    1 
ATOM   396  C  CG    . GLU A 1 52  ? 12.848  -20.485 -6.886  1.00 31.71  ? 52  GLU A CG    1 
ATOM   397  C  CD    . GLU A 1 52  ? 12.952  -19.274 -7.790  1.00 32.32  ? 52  GLU A CD    1 
ATOM   398  O  OE1   . GLU A 1 52  ? 13.286  -19.452 -8.979  1.00 30.51  ? 52  GLU A OE1   1 
ATOM   399  O  OE2   . GLU A 1 52  ? 12.680  -18.149 -7.318  1.00 31.63  ? 52  GLU A OE2   1 
ATOM   400  N  N     . TYR A 1 53  ? 11.291  -21.533 -3.922  1.00 36.94  ? 53  TYR A N     1 
ATOM   401  C  CA    . TYR A 1 53  ? 11.799  -21.323 -2.568  1.00 40.10  ? 53  TYR A CA    1 
ATOM   402  C  C     . TYR A 1 53  ? 11.990  -22.649 -1.844  1.00 39.08  ? 53  TYR A C     1 
ATOM   403  O  O     . TYR A 1 53  ? 12.985  -22.840 -1.133  1.00 39.00  ? 53  TYR A O     1 
ATOM   404  C  CB    . TYR A 1 53  ? 10.842  -20.410 -1.797  1.00 36.24  ? 53  TYR A CB    1 
ATOM   405  C  CG    . TYR A 1 53  ? 11.347  -19.914 -0.457  1.00 39.41  ? 53  TYR A CG    1 
ATOM   406  C  CD1   . TYR A 1 53  ? 12.483  -19.121 -0.369  1.00 40.67  ? 53  TYR A CD1   1 
ATOM   407  C  CD2   . TYR A 1 53  ? 10.665  -20.210 0.716   1.00 43.22  ? 53  TYR A CD2   1 
ATOM   408  C  CE1   . TYR A 1 53  ? 12.937  -18.653 0.853   1.00 42.19  ? 53  TYR A CE1   1 
ATOM   409  C  CE2   . TYR A 1 53  ? 11.111  -19.747 1.941   1.00 42.71  ? 53  TYR A CE2   1 
ATOM   410  C  CZ    . TYR A 1 53  ? 12.248  -18.970 2.005   1.00 43.63  ? 53  TYR A CZ    1 
ATOM   411  O  OH    . TYR A 1 53  ? 12.696  -18.507 3.223   1.00 42.90  ? 53  TYR A OH    1 
ATOM   412  N  N     . GLY A 1 54  ? 11.055  -23.585 -2.028  1.00 39.32  ? 54  GLY A N     1 
ATOM   413  C  CA    . GLY A 1 54  ? 11.199  -24.895 -1.414  1.00 41.36  ? 54  GLY A CA    1 
ATOM   414  C  C     . GLY A 1 54  ? 12.428  -25.641 -1.898  1.00 49.04  ? 54  GLY A C     1 
ATOM   415  O  O     . GLY A 1 54  ? 13.154  -26.240 -1.102  1.00 44.31  ? 54  GLY A O     1 
ATOM   416  N  N     . ARG A 1 55  ? 12.683  -25.609 -3.209  1.00 45.88  ? 55  ARG A N     1 
ATOM   417  C  CA    . ARG A 1 55  ? 13.866  -26.278 -3.742  1.00 47.53  ? 55  ARG A CA    1 
ATOM   418  C  C     . ARG A 1 55  ? 15.148  -25.622 -3.244  1.00 51.13  ? 55  ARG A C     1 
ATOM   419  O  O     . ARG A 1 55  ? 16.141  -26.310 -2.980  1.00 55.31  ? 55  ARG A O     1 
ATOM   420  C  CB    . ARG A 1 55  ? 13.827  -26.287 -5.271  1.00 49.51  ? 55  ARG A CB    1 
ATOM   421  C  CG    . ARG A 1 55  ? 12.856  -27.295 -5.860  1.00 57.80  ? 55  ARG A CG    1 
ATOM   422  C  CD    . ARG A 1 55  ? 12.996  -27.388 -7.372  1.00 69.36  ? 55  ARG A CD    1 
ATOM   423  N  NE    . ARG A 1 55  ? 12.653  -26.133 -8.031  1.00 70.75  ? 55  ARG A NE    1 
ATOM   424  C  CZ    . ARG A 1 55  ? 11.436  -25.817 -8.450  1.00 68.71  ? 55  ARG A CZ    1 
ATOM   425  N  NH1   . ARG A 1 55  ? 10.415  -26.646 -8.298  1.00 67.31  ? 55  ARG A NH1   1 
ATOM   426  N  NH2   . ARG A 1 55  ? 11.237  -24.640 -9.038  1.00 60.69  ? 55  ARG A NH2   1 
ATOM   427  N  N     . LEU A 1 56  ? 15.150  -24.292 -3.111  1.00 43.29  ? 56  LEU A N     1 
ATOM   428  C  CA    . LEU A 1 56  ? 16.342  -23.601 -2.624  1.00 41.92  ? 56  LEU A CA    1 
ATOM   429  C  C     . LEU A 1 56  ? 16.642  -23.963 -1.175  1.00 41.84  ? 56  LEU A C     1 
ATOM   430  O  O     . LEU A 1 56  ? 17.810  -24.114 -0.797  1.00 44.48  ? 56  LEU A O     1 
ATOM   431  C  CB    . LEU A 1 56  ? 16.172  -22.090 -2.767  1.00 45.48  ? 56  LEU A CB    1 
ATOM   432  C  CG    . LEU A 1 56  ? 16.055  -21.538 -4.186  1.00 51.12  ? 56  LEU A CG    1 
ATOM   433  C  CD1   . LEU A 1 56  ? 15.792  -20.047 -4.139  1.00 41.58  ? 56  LEU A CD1   1 
ATOM   434  C  CD2   . LEU A 1 56  ? 17.310  -21.842 -4.982  1.00 50.05  ? 56  LEU A CD2   1 
ATOM   435  N  N     . LEU A 1 57  ? 15.603  -24.089 -0.347  1.00 44.04  ? 57  LEU A N     1 
ATOM   436  C  CA    . LEU A 1 57  ? 15.799  -24.481 1.045   1.00 42.03  ? 57  LEU A CA    1 
ATOM   437  C  C     . LEU A 1 57  ? 16.325  -25.906 1.141   1.00 48.37  ? 57  LEU A C     1 
ATOM   438  O  O     . LEU A 1 57  ? 17.325  -26.166 1.821   1.00 44.89  ? 57  LEU A O     1 
ATOM   439  C  CB    . LEU A 1 57  ? 14.489  -24.339 1.820   1.00 39.02  ? 57  LEU A CB    1 
ATOM   440  C  CG    . LEU A 1 57  ? 13.987  -22.921 2.092   1.00 41.08  ? 57  LEU A CG    1 
ATOM   441  C  CD1   . LEU A 1 57  ? 12.556  -22.961 2.602   1.00 47.08  ? 57  LEU A CD1   1 
ATOM   442  C  CD2   . LEU A 1 57  ? 14.892  -22.213 3.089   1.00 38.74  ? 57  LEU A CD2   1 
ATOM   443  N  N     . ALA A 1 58  ? 15.659  -26.846 0.464   1.00 49.84  ? 58  ALA A N     1 
ATOM   444  C  CA    . ALA A 1 58  ? 16.113  -28.233 0.477   1.00 56.36  ? 58  ALA A CA    1 
ATOM   445  C  C     . ALA A 1 58  ? 17.541  -28.348 -0.038  1.00 51.53  ? 58  ALA A C     1 
ATOM   446  O  O     . ALA A 1 58  ? 18.338  -29.128 0.493   1.00 51.66  ? 58  ALA A O     1 
ATOM   447  C  CB    . ALA A 1 58  ? 15.169  -29.102 -0.353  1.00 53.42  ? 58  ALA A CB    1 
ATOM   448  N  N     . HIS A 1 59  ? 17.881  -27.572 -1.069  1.00 52.01  ? 59  HIS A N     1 
ATOM   449  C  CA    . HIS A 1 59  ? 19.255  -27.529 -1.559  1.00 49.62  ? 59  HIS A CA    1 
ATOM   450  C  C     . HIS A 1 59  ? 20.215  -27.108 -0.453  1.00 53.99  ? 59  HIS A C     1 
ATOM   451  O  O     . HIS A 1 59  ? 21.162  -27.832 -0.125  1.00 56.32  ? 59  HIS A O     1 
ATOM   452  C  CB    . HIS A 1 59  ? 19.347  -26.573 -2.750  1.00 46.90  ? 59  HIS A CB    1 
ATOM   453  C  CG    . HIS A 1 59  ? 20.742  -26.355 -3.248  1.00 54.71  ? 59  HIS A CG    1 
ATOM   454  N  ND1   . HIS A 1 59  ? 21.615  -27.391 -3.498  1.00 52.09  ? 59  HIS A ND1   1 
ATOM   455  C  CD2   . HIS A 1 59  ? 21.411  -25.217 -3.554  1.00 49.51  ? 59  HIS A CD2   1 
ATOM   456  C  CE1   . HIS A 1 59  ? 22.763  -26.902 -3.933  1.00 58.07  ? 59  HIS A CE1   1 
ATOM   457  N  NE2   . HIS A 1 59  ? 22.666  -25.585 -3.975  1.00 50.45  ? 59  HIS A NE2   1 
ATOM   458  N  N     . MET A 1 60  ? 19.973  -25.934 0.142   1.00 54.32  ? 60  MET A N     1 
ATOM   459  C  CA    . MET A 1 60  ? 20.833  -25.441 1.215   1.00 47.73  ? 60  MET A CA    1 
ATOM   460  C  C     . MET A 1 60  ? 20.907  -26.428 2.371   1.00 48.57  ? 60  MET A C     1 
ATOM   461  O  O     . MET A 1 60  ? 21.965  -26.593 2.990   1.00 49.33  ? 60  MET A O     1 
ATOM   462  C  CB    . MET A 1 60  ? 20.331  -24.086 1.712   1.00 38.98  ? 60  MET A CB    1 
ATOM   463  C  CG    . MET A 1 60  ? 20.819  -22.903 0.910   1.00 33.42  ? 60  MET A CG    1 
ATOM   464  S  SD    . MET A 1 60  ? 20.220  -21.353 1.596   1.00 41.17  ? 60  MET A SD    1 
ATOM   465  C  CE    . MET A 1 60  ? 18.493  -21.411 1.120   1.00 38.46  ? 60  MET A CE    1 
ATOM   466  N  N     . GLN A 1 61  ? 19.789  -27.089 2.683   1.00 47.77  ? 61  GLN A N     1 
ATOM   467  C  CA    . GLN A 1 61  ? 19.785  -28.063 3.768   1.00 51.08  ? 61  GLN A CA    1 
ATOM   468  C  C     . GLN A 1 61  ? 20.602  -29.297 3.414   1.00 60.36  ? 61  GLN A C     1 
ATOM   469  O  O     . GLN A 1 61  ? 21.248  -29.883 4.290   1.00 58.93  ? 61  GLN A O     1 
ATOM   470  C  CB    . GLN A 1 61  ? 18.352  -28.456 4.117   1.00 52.39  ? 61  GLN A CB    1 
ATOM   471  C  CG    . GLN A 1 61  ? 18.227  -29.286 5.382   1.00 57.19  ? 61  GLN A CG    1 
ATOM   472  C  CD    . GLN A 1 61  ? 16.788  -29.609 5.723   1.00 61.64  ? 61  GLN A CD    1 
ATOM   473  O  OE1   . GLN A 1 61  ? 15.900  -29.488 4.880   1.00 54.67  ? 61  GLN A OE1   1 
ATOM   474  N  NE2   . GLN A 1 61  ? 16.548  -30.016 6.965   1.00 60.41  ? 61  GLN A NE2   1 
ATOM   475  N  N     . GLU A 1 62  ? 20.589  -29.705 2.144   1.00 61.73  ? 62  GLU A N     1 
ATOM   476  C  CA    . GLU A 1 62  ? 21.407  -30.833 1.718   1.00 68.47  ? 62  GLU A CA    1 
ATOM   477  C  C     . GLU A 1 62  ? 22.887  -30.481 1.671   1.00 68.33  ? 62  GLU A C     1 
ATOM   478  O  O     . GLU A 1 62  ? 23.728  -31.380 1.777   1.00 77.58  ? 62  GLU A O     1 
ATOM   479  C  CB    . GLU A 1 62  ? 20.936  -31.336 0.351   1.00 65.92  ? 62  GLU A CB    1 
ATOM   480  C  CG    . GLU A 1 62  ? 19.561  -31.995 0.383   1.00 64.86  ? 62  GLU A CG    1 
ATOM   481  C  CD    . GLU A 1 62  ? 18.925  -32.114 -0.991  1.00 58.46  ? 62  GLU A CD    1 
ATOM   482  O  OE1   . GLU A 1 62  ? 19.630  -31.896 -1.999  1.00 57.20  ? 62  GLU A OE1   1 
ATOM   483  O  OE2   . GLU A 1 62  ? 17.716  -32.422 -1.061  1.00 56.48  ? 62  GLU A OE2   1 
ATOM   484  N  N     . GLU A 1 63  ? 23.224  -29.201 1.524   1.00 60.22  ? 63  GLU A N     1 
ATOM   485  C  CA    . GLU A 1 63  ? 24.610  -28.753 1.511   1.00 64.11  ? 63  GLU A CA    1 
ATOM   486  C  C     . GLU A 1 63  ? 25.105  -28.324 2.887   1.00 61.83  ? 63  GLU A C     1 
ATOM   487  O  O     . GLU A 1 63  ? 26.198  -27.759 2.988   1.00 60.97  ? 63  GLU A O     1 
ATOM   488  C  CB    . GLU A 1 63  ? 24.784  -27.595 0.523   1.00 57.88  ? 63  GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 63  ? 24.215  -27.849 -0.866  1.00 71.22  ? 63  GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 63  ? 25.053  -28.804 -1.695  1.00 74.35  ? 63  GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 63  ? 26.126  -29.236 -1.221  1.00 71.92  ? 63  GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 63  ? 24.636  -29.119 -2.830  1.00 74.32  ? 63  GLU A OE2   1 
ATOM   493  N  N     . GLY A 1 64  ? 24.327  -28.568 3.939   1.00 58.01  ? 64  GLY A N     1 
ATOM   494  C  CA    . GLY A 1 64  ? 24.728  -28.176 5.278   1.00 56.77  ? 64  GLY A CA    1 
ATOM   495  C  C     . GLY A 1 64  ? 24.841  -26.684 5.499   1.00 56.33  ? 64  GLY A C     1 
ATOM   496  O  O     . GLY A 1 64  ? 25.600  -26.250 6.371   1.00 56.15  ? 64  GLY A O     1 
ATOM   497  N  N     . VAL A 1 65  ? 24.106  -25.884 4.732   1.00 53.32  ? 65  VAL A N     1 
ATOM   498  C  CA    . VAL A 1 65  ? 24.158  -24.433 4.886   1.00 51.44  ? 65  VAL A CA    1 
ATOM   499  C  C     . VAL A 1 65  ? 23.146  -23.947 5.915   1.00 50.45  ? 65  VAL A C     1 
ATOM   500  O  O     . VAL A 1 65  ? 23.430  -23.026 6.684   1.00 46.93  ? 65  VAL A O     1 
ATOM   501  C  CB    . VAL A 1 65  ? 23.944  -23.751 3.519   1.00 54.15  ? 65  VAL A CB    1 
ATOM   502  C  CG1   . VAL A 1 65  ? 24.154  -22.248 3.637   1.00 44.25  ? 65  VAL A CG1   1 
ATOM   503  C  CG2   . VAL A 1 65  ? 24.879  -24.346 2.480   1.00 58.49  ? 65  VAL A CG2   1 
ATOM   504  N  N     . ILE A 1 66  ? 21.956  -24.550 5.952   1.00 43.50  ? 66  ILE A N     1 
ATOM   505  C  CA    . ILE A 1 66  ? 20.927  -24.172 6.908   1.00 41.50  ? 66  ILE A CA    1 
ATOM   506  C  C     . ILE A 1 66  ? 20.418  -25.415 7.622   1.00 42.70  ? 66  ILE A C     1 
ATOM   507  O  O     . ILE A 1 66  ? 20.582  -26.545 7.159   1.00 45.24  ? 66  ILE A O     1 
ATOM   508  C  CB    . ILE A 1 66  ? 19.747  -23.420 6.251   1.00 37.18  ? 66  ILE A CB    1 
ATOM   509  C  CG1   . ILE A 1 66  ? 19.131  -24.260 5.132   1.00 41.38  ? 66  ILE A CG1   1 
ATOM   510  C  CG2   . ILE A 1 66  ? 20.193  -22.059 5.739   1.00 38.57  ? 66  ILE A CG2   1 
ATOM   511  C  CD1   . ILE A 1 66  ? 17.933  -23.608 4.479   1.00 40.54  ? 66  ILE A CD1   1 
ATOM   512  N  N     . ARG A 1 67  ? 19.793  -25.181 8.772   1.00 41.38  ? 67  ARG A N     1 
ATOM   513  C  CA    . ARG A 1 67  ? 19.139  -26.214 9.560   1.00 40.34  ? 67  ARG A CA    1 
ATOM   514  C  C     . ARG A 1 67  ? 17.692  -25.810 9.789   1.00 40.87  ? 67  ARG A C     1 
ATOM   515  O  O     . ARG A 1 67  ? 17.397  -24.627 9.982   1.00 35.88  ? 67  ARG A O     1 
ATOM   516  C  CB    . ARG A 1 67  ? 19.833  -26.420 10.912  1.00 47.01  ? 67  ARG A CB    1 
ATOM   517  C  CG    . ARG A 1 67  ? 21.196  -27.080 10.836  1.00 55.73  ? 67  ARG A CG    1 
ATOM   518  C  CD    . ARG A 1 67  ? 21.795  -27.236 12.226  1.00 63.80  ? 67  ARG A CD    1 
ATOM   519  N  NE    . ARG A 1 67  ? 20.825  -27.765 13.178  1.00 66.68  ? 67  ARG A NE    1 
ATOM   520  C  CZ    . ARG A 1 67  ? 20.606  -29.055 13.393  1.00 72.10  ? 67  ARG A CZ    1 
ATOM   521  N  NH1   . ARG A 1 67  ? 21.273  -29.989 12.733  1.00 74.49  ? 67  ARG A NH1   1 
ATOM   522  N  NH2   . ARG A 1 67  ? 19.696  -29.418 14.292  1.00 70.30  ? 67  ARG A NH2   1 
ATOM   523  N  N     . LYS A 1 68  ? 16.795  -26.791 9.776   1.00 37.93  ? 68  LYS A N     1 
ATOM   524  C  CA    . LYS A 1 68  ? 15.393  -26.518 10.052  1.00 43.83  ? 68  LYS A CA    1 
ATOM   525  C  C     . LYS A 1 68  ? 15.178  -26.388 11.552  1.00 36.98  ? 68  LYS A C     1 
ATOM   526  O  O     . LYS A 1 68  ? 15.656  -27.217 12.332  1.00 44.44  ? 68  LYS A O     1 
ATOM   527  C  CB    . LYS A 1 68  ? 14.498  -27.620 9.488   1.00 46.15  ? 68  LYS A CB    1 
ATOM   528  C  CG    . LYS A 1 68  ? 13.022  -27.252 9.487   1.00 46.99  ? 68  LYS A CG    1 
ATOM   529  C  CD    . LYS A 1 68  ? 12.191  -28.268 8.719   1.00 51.75  ? 68  LYS A CD    1 
ATOM   530  C  CE    . LYS A 1 68  ? 10.809  -27.717 8.393   1.00 56.06  ? 68  LYS A CE    1 
ATOM   531  N  NZ    . LYS A 1 68  ? 10.045  -27.333 9.615   1.00 61.22  ? 68  LYS A NZ    1 
ATOM   532  N  N     . LEU A 1 69  ? 14.468  -25.337 11.953  1.00 38.32  ? 69  LEU A N     1 
ATOM   533  C  CA    . LEU A 1 69  ? 14.076  -25.142 13.347  1.00 45.03  ? 69  LEU A CA    1 
ATOM   534  C  C     . LEU A 1 69  ? 12.709  -25.789 13.522  1.00 47.68  ? 69  LEU A C     1 
ATOM   535  O  O     . LEU A 1 69  ? 11.668  -25.167 13.308  1.00 47.24  ? 69  LEU A O     1 
ATOM   536  C  CB    . LEU A 1 69  ? 14.069  -23.660 13.698  1.00 42.57  ? 69  LEU A CB    1 
ATOM   537  C  CG    . LEU A 1 69  ? 15.438  -22.987 13.577  1.00 37.33  ? 69  LEU A CG    1 
ATOM   538  C  CD1   . LEU A 1 69  ? 15.295  -21.483 13.437  1.00 36.05  ? 69  LEU A CD1   1 
ATOM   539  C  CD2   . LEU A 1 69  ? 16.312  -23.338 14.777  1.00 41.31  ? 69  LEU A CD2   1 
ATOM   540  N  N     . LYS A 1 70  ? 12.718  -27.064 13.919  1.00 49.54  ? 70  LYS A N     1 
ATOM   541  C  CA    . LYS A 1 70  ? 11.510  -27.881 13.930  1.00 53.65  ? 70  LYS A CA    1 
ATOM   542  C  C     . LYS A 1 70  ? 10.455  -27.393 14.915  1.00 51.53  ? 70  LYS A C     1 
ATOM   543  O  O     . LYS A 1 70  ? 9.303   -27.830 14.821  1.00 56.32  ? 70  LYS A O     1 
ATOM   544  C  CB    . LYS A 1 70  ? 11.870  -29.337 14.236  1.00 62.39  ? 70  LYS A CB    1 
ATOM   545  C  CG    . LYS A 1 70  ? 12.697  -29.533 15.499  1.00 67.32  ? 70  LYS A CG    1 
ATOM   546  C  CD    . LYS A 1 70  ? 12.947  -31.012 15.766  1.00 79.14  ? 70  LYS A CD    1 
ATOM   547  C  CE    . LYS A 1 70  ? 13.729  -31.231 17.055  1.00 73.67  ? 70  LYS A CE    1 
ATOM   548  N  NZ    . LYS A 1 70  ? 15.114  -30.686 16.973  1.00 67.25  ? 70  LYS A NZ    1 
ATOM   549  N  N     . LYS A 1 71  ? 10.808  -26.506 15.846  1.00 50.33  ? 71  LYS A N     1 
ATOM   550  C  CA    . LYS A 1 71  ? 9.832   -26.014 16.811  1.00 49.91  ? 71  LYS A CA    1 
ATOM   551  C  C     . LYS A 1 71  ? 8.855   -25.021 16.193  1.00 52.56  ? 71  LYS A C     1 
ATOM   552  O  O     . LYS A 1 71  ? 7.750   -24.848 16.719  1.00 48.80  ? 71  LYS A O     1 
ATOM   553  C  CB    . LYS A 1 71  ? 10.555  -25.376 18.000  1.00 49.17  ? 71  LYS A CB    1 
ATOM   554  C  CG    . LYS A 1 71  ? 9.660   -24.983 19.159  1.00 51.88  ? 71  LYS A CG    1 
ATOM   555  C  CD    . LYS A 1 71  ? 10.482  -24.616 20.383  1.00 53.91  ? 71  LYS A CD    1 
ATOM   556  C  CE    . LYS A 1 71  ? 9.591   -24.335 21.575  1.00 57.25  ? 71  LYS A CE    1 
ATOM   557  N  NZ    . LYS A 1 71  ? 10.364  -24.298 22.845  1.00 72.86  ? 71  LYS A NZ    1 
ATOM   558  N  N     . TYR A 1 72  ? 9.223   -24.381 15.089  1.00 47.52  ? 72  TYR A N     1 
ATOM   559  C  CA    . TYR A 1 72  ? 8.411   -23.341 14.476  1.00 47.99  ? 72  TYR A CA    1 
ATOM   560  C  C     . TYR A 1 72  ? 7.975   -23.777 13.080  1.00 46.13  ? 72  TYR A C     1 
ATOM   561  O  O     . TYR A 1 72  ? 8.318   -24.862 12.604  1.00 48.34  ? 72  TYR A O     1 
ATOM   562  C  CB    . TYR A 1 72  ? 9.177   -22.014 14.434  1.00 47.25  ? 72  TYR A CB    1 
ATOM   563  C  CG    . TYR A 1 72  ? 9.831   -21.670 15.754  1.00 42.49  ? 72  TYR A CG    1 
ATOM   564  C  CD1   . TYR A 1 72  ? 9.064   -21.428 16.889  1.00 45.07  ? 72  TYR A CD1   1 
ATOM   565  C  CD2   . TYR A 1 72  ? 11.213  -21.600 15.869  1.00 42.39  ? 72  TYR A CD2   1 
ATOM   566  C  CE1   . TYR A 1 72  ? 9.656   -21.121 18.099  1.00 46.90  ? 72  TYR A CE1   1 
ATOM   567  C  CE2   . TYR A 1 72  ? 11.814  -21.292 17.077  1.00 43.66  ? 72  TYR A CE2   1 
ATOM   568  C  CZ    . TYR A 1 72  ? 11.031  -21.054 18.187  1.00 46.20  ? 72  TYR A CZ    1 
ATOM   569  O  OH    . TYR A 1 72  ? 11.625  -20.748 19.391  1.00 48.32  ? 72  TYR A OH    1 
ATOM   570  N  N     . ASP A 1 73  ? 7.206   -22.910 12.426  1.00 45.67  ? 73  ASP A N     1 
ATOM   571  C  CA    . ASP A 1 73  ? 6.626   -23.189 11.116  1.00 49.61  ? 73  ASP A CA    1 
ATOM   572  C  C     . ASP A 1 73  ? 7.518   -22.574 10.043  1.00 43.43  ? 73  ASP A C     1 
ATOM   573  O  O     . ASP A 1 73  ? 7.542   -21.351 9.877   1.00 42.51  ? 73  ASP A O     1 
ATOM   574  C  CB    . ASP A 1 73  ? 5.203   -22.636 11.035  1.00 57.11  ? 73  ASP A CB    1 
ATOM   575  C  CG    . ASP A 1 73  ? 4.575   -22.814 9.661   1.00 62.49  ? 73  ASP A CG    1 
ATOM   576  O  OD1   . ASP A 1 73  ? 5.072   -23.639 8.866   1.00 66.44  ? 73  ASP A OD1   1 
ATOM   577  O  OD2   . ASP A 1 73  ? 3.576   -22.120 9.375   1.00 75.80  ? 73  ASP A OD2   1 
ATOM   578  N  N     . ASN A 1 74  ? 8.248   -23.425 9.320   1.00 44.61  ? 74  ASN A N     1 
ATOM   579  C  CA    . ASN A 1 74  ? 9.070   -23.005 8.182   1.00 41.03  ? 74  ASN A CA    1 
ATOM   580  C  C     . ASN A 1 74  ? 10.107  -21.957 8.595   1.00 35.06  ? 74  ASN A C     1 
ATOM   581  O  O     . ASN A 1 74  ? 10.254  -20.909 7.965   1.00 34.85  ? 74  ASN A O     1 
ATOM   582  C  CB    . ASN A 1 74  ? 8.188   -22.490 7.038   1.00 42.69  ? 74  ASN A CB    1 
ATOM   583  C  CG    . ASN A 1 74  ? 8.968   -22.242 5.758   1.00 45.48  ? 74  ASN A CG    1 
ATOM   584  O  OD1   . ASN A 1 74  ? 9.911   -22.967 5.437   1.00 43.00  ? 74  ASN A OD1   1 
ATOM   585  N  ND2   . ASN A 1 74  ? 8.581   -21.204 5.023   1.00 39.19  ? 74  ASN A ND2   1 
ATOM   586  N  N     . CYS A 1 75  ? 10.833  -22.248 9.670   1.00 36.98  ? 75  CYS A N     1 
ATOM   587  C  CA    . CYS A 1 75  ? 11.919  -21.394 10.134  1.00 36.27  ? 75  CYS A CA    1 
ATOM   588  C  C     . CYS A 1 75  ? 13.243  -22.138 10.017  1.00 32.87  ? 75  CYS A C     1 
ATOM   589  O  O     . CYS A 1 75  ? 13.302  -23.354 10.227  1.00 35.99  ? 75  CYS A O     1 
ATOM   590  C  CB    . CYS A 1 75  ? 11.687  -20.935 11.574  1.00 34.09  ? 75  CYS A CB    1 
ATOM   591  S  SG    . CYS A 1 75  ? 10.341  -19.733 11.756  1.00 36.66  ? 75  CYS A SG    1 
ATOM   592  N  N     . TRP A 1 76  ? 14.303  -21.404 9.675   1.00 30.63  ? 76  TRP A N     1 
ATOM   593  C  CA    . TRP A 1 76  ? 15.585  -22.000 9.330   1.00 33.56  ? 76  TRP A CA    1 
ATOM   594  C  C     . TRP A 1 76  ? 16.717  -21.198 9.956   1.00 33.05  ? 76  TRP A C     1 
ATOM   595  O  O     . TRP A 1 76  ? 16.613  -19.981 10.129  1.00 32.75  ? 76  TRP A O     1 
ATOM   596  C  CB    . TRP A 1 76  ? 15.764  -22.070 7.808   1.00 34.28  ? 76  TRP A CB    1 
ATOM   597  C  CG    . TRP A 1 76  ? 14.629  -22.764 7.115   1.00 31.69  ? 76  TRP A CG    1 
ATOM   598  C  CD1   . TRP A 1 76  ? 13.427  -22.221 6.764   1.00 33.98  ? 76  TRP A CD1   1 
ATOM   599  C  CD2   . TRP A 1 76  ? 14.588  -24.133 6.701   1.00 35.95  ? 76  TRP A CD2   1 
ATOM   600  N  NE1   . TRP A 1 76  ? 12.640  -23.168 6.153   1.00 36.23  ? 76  TRP A NE1   1 
ATOM   601  C  CE2   . TRP A 1 76  ? 13.331  -24.351 6.100   1.00 41.29  ? 76  TRP A CE2   1 
ATOM   602  C  CE3   . TRP A 1 76  ? 15.493  -25.196 6.774   1.00 40.54  ? 76  TRP A CE3   1 
ATOM   603  C  CZ2   . TRP A 1 76  ? 12.956  -25.588 5.578   1.00 37.64  ? 76  TRP A CZ2   1 
ATOM   604  C  CZ3   . TRP A 1 76  ? 15.121  -26.423 6.254   1.00 40.46  ? 76  TRP A CZ3   1 
ATOM   605  C  CH2   . TRP A 1 76  ? 13.863  -26.609 5.665   1.00 42.41  ? 76  TRP A CH2   1 
ATOM   606  N  N     . LEU A 1 77  ? 17.809  -21.891 10.280  1.00 31.50  ? 77  LEU A N     1 
ATOM   607  C  CA    . LEU A 1 77  ? 18.968  -21.296 10.936  1.00 32.24  ? 77  LEU A CA    1 
ATOM   608  C  C     . LEU A 1 77  ? 20.211  -21.473 10.073  1.00 35.67  ? 77  LEU A C     1 
ATOM   609  O  O     . LEU A 1 77  ? 20.528  -22.591 9.656   1.00 34.30  ? 77  LEU A O     1 
ATOM   610  C  CB    . LEU A 1 77  ? 19.198  -21.923 12.313  1.00 34.88  ? 77  LEU A CB    1 
ATOM   611  C  CG    . LEU A 1 77  ? 20.471  -21.488 13.042  1.00 36.24  ? 77  LEU A CG    1 
ATOM   612  C  CD1   . LEU A 1 77  ? 20.455  -19.991 13.298  1.00 35.62  ? 77  LEU A CD1   1 
ATOM   613  C  CD2   . LEU A 1 77  ? 20.646  -22.254 14.345  1.00 39.22  ? 77  LEU A CD2   1 
ATOM   614  N  N     . ALA A 1 78  ? 20.918  -20.374 9.822   1.00 33.09  ? 78  ALA A N     1 
ATOM   615  C  CA    . ALA A 1 78  ? 22.182  -20.391 9.099   1.00 31.42  ? 78  ALA A CA    1 
ATOM   616  C  C     . ALA A 1 78  ? 23.308  -19.914 10.008  1.00 32.04  ? 78  ALA A C     1 
ATOM   617  O  O     . ALA A 1 78  ? 23.155  -18.925 10.730  1.00 32.33  ? 78  ALA A O     1 
ATOM   618  C  CB    . ALA A 1 78  ? 22.117  -19.506 7.851   1.00 28.26  ? 78  ALA A CB    1 
ATOM   619  N  N     . LEU A 1 79  ? 24.438  -20.617 9.965   1.00 35.30  ? 79  LEU A N     1 
ATOM   620  C  CA    . LEU A 1 79  ? 25.622  -20.273 10.743  1.00 35.30  ? 79  LEU A CA    1 
ATOM   621  C  C     . LEU A 1 79  ? 26.761  -19.936 9.790   1.00 40.18  ? 79  LEU A C     1 
ATOM   622  O  O     . LEU A 1 79  ? 27.069  -20.720 8.887   1.00 44.63  ? 79  LEU A O     1 
ATOM   623  C  CB    . LEU A 1 79  ? 26.023  -21.422 11.670  1.00 39.82  ? 79  LEU A CB    1 
ATOM   624  C  CG    . LEU A 1 79  ? 24.934  -21.944 12.610  1.00 42.67  ? 79  LEU A CG    1 
ATOM   625  C  CD1   . LEU A 1 79  ? 25.475  -23.061 13.490  1.00 42.40  ? 79  LEU A CD1   1 
ATOM   626  C  CD2   . LEU A 1 79  ? 24.351  -20.818 13.455  1.00 39.00  ? 79  LEU A CD2   1 
ATOM   627  N  N     . THR A 1 80  ? 27.386  -18.781 9.997   1.00 37.31  ? 80  THR A N     1 
ATOM   628  C  CA    . THR A 1 80  ? 28.365  -18.239 9.066   1.00 34.47  ? 80  THR A CA    1 
ATOM   629  C  C     . THR A 1 80  ? 29.781  -18.382 9.608   1.00 45.36  ? 80  THR A C     1 
ATOM   630  O  O     . THR A 1 80  ? 30.006  -18.727 10.770  1.00 39.44  ? 80  THR A O     1 
ATOM   631  C  CB    . THR A 1 80  ? 28.081  -16.761 8.774   1.00 40.26  ? 80  THR A CB    1 
ATOM   632  O  OG1   . THR A 1 80  ? 28.426  -15.971 9.920   1.00 37.66  ? 80  THR A OG1   1 
ATOM   633  C  CG2   . THR A 1 80  ? 26.612  -16.556 8.444   1.00 34.57  ? 80  THR A CG2   1 
ATOM   634  N  N     . ASP A 1 81  ? 30.737  -18.107 8.727   1.00 45.74  ? 81  ASP A N     1 
ATOM   635  C  CA    . ASP A 1 81  ? 32.119  -17.932 9.142   1.00 39.70  ? 81  ASP A CA    1 
ATOM   636  C  C     . ASP A 1 81  ? 32.194  -16.771 10.129  1.00 40.46  ? 81  ASP A C     1 
ATOM   637  O  O     . ASP A 1 81  ? 31.607  -15.710 9.873   1.00 38.52  ? 81  ASP A O     1 
ATOM   638  C  CB    . ASP A 1 81  ? 32.996  -17.655 7.919   1.00 41.86  ? 81  ASP A CB    1 
ATOM   639  C  CG    . ASP A 1 81  ? 34.484  -17.795 8.204   1.00 46.86  ? 81  ASP A CG    1 
ATOM   640  O  OD1   . ASP A 1 81  ? 34.982  -17.182 9.174   1.00 46.25  ? 81  ASP A OD1   1 
ATOM   641  O  OD2   . ASP A 1 81  ? 35.159  -18.522 7.445   1.00 43.31  ? 81  ASP A OD2   1 
ATOM   642  N  N     . PRO A 1 82  ? 32.888  -16.926 11.261  1.00 43.48  ? 82  PRO A N     1 
ATOM   643  C  CA    . PRO A 1 82  ? 32.976  -15.813 12.222  1.00 44.50  ? 82  PRO A CA    1 
ATOM   644  C  C     . PRO A 1 82  ? 33.606  -14.551 11.653  1.00 43.91  ? 82  PRO A C     1 
ATOM   645  O  O     . PRO A 1 82  ? 33.457  -13.482 12.256  1.00 44.10  ? 82  PRO A O     1 
ATOM   646  C  CB    . PRO A 1 82  ? 33.817  -16.397 13.369  1.00 48.40  ? 82  PRO A CB    1 
ATOM   647  C  CG    . PRO A 1 82  ? 34.457  -17.634 12.810  1.00 49.49  ? 82  PRO A CG    1 
ATOM   648  C  CD    . PRO A 1 82  ? 33.504  -18.156 11.782  1.00 46.32  ? 82  PRO A CD    1 
ATOM   649  N  N     . ARG A 1 83  ? 34.289  -14.631 10.511  1.00 43.36  ? 83  ARG A N     1 
ATOM   650  C  CA    . ARG A 1 83  ? 34.850  -13.450 9.866   1.00 42.81  ? 83  ARG A CA    1 
ATOM   651  C  C     . ARG A 1 83  ? 33.857  -12.729 8.959   1.00 45.23  ? 83  ARG A C     1 
ATOM   652  O  O     . ARG A 1 83  ? 34.151  -11.616 8.507   1.00 39.23  ? 83  ARG A O     1 
ATOM   653  C  CB    . ARG A 1 83  ? 36.088  -13.842 9.057   1.00 44.23  ? 83  ARG A CB    1 
ATOM   654  C  CG    . ARG A 1 83  ? 37.209  -14.436 9.897   1.00 48.10  ? 83  ARG A CG    1 
ATOM   655  C  CD    . ARG A 1 83  ? 38.251  -15.126 9.031   1.00 49.53  ? 83  ARG A CD    1 
ATOM   656  N  NE    . ARG A 1 83  ? 37.673  -16.216 8.253   1.00 49.69  ? 83  ARG A NE    1 
ATOM   657  C  CZ    . ARG A 1 83  ? 38.380  -17.123 7.594   1.00 59.04  ? 83  ARG A CZ    1 
ATOM   658  N  NH1   . ARG A 1 83  ? 39.703  -17.111 7.607   1.00 67.37  ? 83  ARG A NH1   1 
ATOM   659  N  NH2   . ARG A 1 83  ? 37.745  -18.072 6.912   1.00 51.11  ? 83  ARG A NH2   1 
ATOM   660  N  N     . ASP A 1 84  ? 32.699  -13.326 8.686   1.00 37.40  ? 84  ASP A N     1 
ATOM   661  C  CA    . ASP A 1 84  ? 31.688  -12.769 7.783   1.00 36.01  ? 84  ASP A CA    1 
ATOM   662  C  C     . ASP A 1 84  ? 30.397  -12.620 8.585   1.00 37.00  ? 84  ASP A C     1 
ATOM   663  O  O     . ASP A 1 84  ? 29.490  -13.446 8.480   1.00 33.49  ? 84  ASP A O     1 
ATOM   664  C  CB    . ASP A 1 84  ? 31.511  -13.696 6.551   1.00 33.17  ? 84  ASP A CB    1 
ATOM   665  C  CG    . ASP A 1 84  ? 30.620  -13.095 5.480   1.00 39.36  ? 84  ASP A CG    1 
ATOM   666  O  OD1   . ASP A 1 84  ? 30.404  -11.866 5.489   1.00 42.12  ? 84  ASP A OD1   1 
ATOM   667  O  OD2   . ASP A 1 84  ? 30.132  -13.862 4.624   1.00 32.18  ? 84  ASP A OD2   1 
ATOM   668  N  N     . VAL A 1 85  ? 30.323  -11.568 9.403   1.00 38.58  ? 85  VAL A N     1 
ATOM   669  C  CA    . VAL A 1 85  ? 29.256  -11.459 10.394  1.00 34.27  ? 85  VAL A CA    1 
ATOM   670  C  C     . VAL A 1 85  ? 28.596  -10.085 10.379  1.00 33.51  ? 85  VAL A C     1 
ATOM   671  O  O     . VAL A 1 85  ? 27.560  -9.885  11.024  1.00 34.76  ? 85  VAL A O     1 
ATOM   672  C  CB    . VAL A 1 85  ? 29.785  -11.770 11.808  1.00 37.16  ? 85  VAL A CB    1 
ATOM   673  C  CG1   . VAL A 1 85  ? 30.259  -13.213 11.901  1.00 38.45  ? 85  VAL A CG1   1 
ATOM   674  C  CG2   . VAL A 1 85  ? 30.902  -10.803 12.181  1.00 38.97  ? 85  VAL A CG2   1 
ATOM   675  N  N     . ALA A 1 86  ? 29.182  -9.128  9.666   1.00 37.54  ? 86  ALA A N     1 
ATOM   676  C  CA    . ALA A 1 86  ? 28.672  -7.761  9.697   1.00 37.53  ? 86  ALA A CA    1 
ATOM   677  C  C     . ALA A 1 86  ? 29.163  -7.015  8.463   1.00 38.34  ? 86  ALA A C     1 
ATOM   678  O  O     . ALA A 1 86  ? 29.828  -7.580  7.591   1.00 36.89  ? 86  ALA A O     1 
ATOM   679  C  CB    . ALA A 1 86  ? 29.094  -7.044  10.984  1.00 35.62  ? 86  ALA A CB    1 
ATOM   680  N  N     . ARG A 1 87  ? 28.813  -5.732  8.394   1.00 38.78  ? 87  ARG A N     1 
ATOM   681  C  CA    . ARG A 1 87  ? 29.323  -4.865  7.344   1.00 38.97  ? 87  ARG A CA    1 
ATOM   682  C  C     . ARG A 1 87  ? 30.797  -4.556  7.582   1.00 39.84  ? 87  ARG A C     1 
ATOM   683  O  O     . ARG A 1 87  ? 31.285  -4.586  8.713   1.00 43.74  ? 87  ARG A O     1 
ATOM   684  C  CB    . ARG A 1 87  ? 28.528  -3.560  7.287   1.00 38.16  ? 87  ARG A CB    1 
ATOM   685  C  CG    . ARG A 1 87  ? 27.097  -3.709  6.796   1.00 30.27  ? 87  ARG A CG    1 
ATOM   686  C  CD    . ARG A 1 87  ? 26.424  -2.351  6.613   1.00 30.84  ? 87  ARG A CD    1 
ATOM   687  N  NE    . ARG A 1 87  ? 26.053  -1.730  7.881   1.00 32.99  ? 87  ARG A NE    1 
ATOM   688  C  CZ    . ARG A 1 87  ? 26.778  -0.814  8.509   1.00 34.56  ? 87  ARG A CZ    1 
ATOM   689  N  NH1   . ARG A 1 87  ? 27.929  -0.386  8.017   1.00 37.86  ? 87  ARG A NH1   1 
ATOM   690  N  NH2   . ARG A 1 87  ? 26.335  -0.314  9.659   1.00 33.77  ? 87  ARG A NH2   1 
ATOM   691  N  N     . ILE A 1 88  ? 31.504  -4.255  6.500   1.00 39.28  ? 88  ILE A N     1 
ATOM   692  C  CA    . ILE A 1 88  ? 32.910  -3.859  6.554   1.00 40.79  ? 88  ILE A CA    1 
ATOM   693  C  C     . ILE A 1 88  ? 32.998  -2.496  5.879   1.00 38.81  ? 88  ILE A C     1 
ATOM   694  O  O     . ILE A 1 88  ? 33.127  -2.397  4.656   1.00 40.05  ? 88  ILE A O     1 
ATOM   695  C  CB    . ILE A 1 88  ? 33.834  -4.876  5.883   1.00 41.56  ? 88  ILE A CB    1 
ATOM   696  C  CG1   . ILE A 1 88  ? 33.604  -6.273  6.461   1.00 41.97  ? 88  ILE A CG1   1 
ATOM   697  C  CG2   . ILE A 1 88  ? 35.285  -4.463  6.054   1.00 46.10  ? 88  ILE A CG2   1 
ATOM   698  C  CD1   . ILE A 1 88  ? 34.410  -7.355  5.775   1.00 45.95  ? 88  ILE A CD1   1 
ATOM   699  N  N     . GLU A 1 89  ? 32.933  -1.429  6.679   1.00 38.46  ? 89  GLU A N     1 
ATOM   700  C  CA    . GLU A 1 89  ? 32.952  -0.082  6.118   1.00 42.17  ? 89  GLU A CA    1 
ATOM   701  C  C     . GLU A 1 89  ? 34.266  0.223   5.412   1.00 43.21  ? 89  GLU A C     1 
ATOM   702  O  O     . GLU A 1 89  ? 34.274  0.946   4.409   1.00 36.68  ? 89  GLU A O     1 
ATOM   703  C  CB    . GLU A 1 89  ? 32.680  0.946   7.216   1.00 41.98  ? 89  GLU A CB    1 
ATOM   704  C  CG    . GLU A 1 89  ? 31.286  0.825   7.823   1.00 49.76  ? 89  GLU A CG    1 
ATOM   705  C  CD    . GLU A 1 89  ? 31.038  1.799   8.960   1.00 46.48  ? 89  GLU A CD    1 
ATOM   706  O  OE1   . GLU A 1 89  ? 31.878  2.698   9.183   1.00 45.51  ? 89  GLU A OE1   1 
ATOM   707  O  OE2   . GLU A 1 89  ? 29.995  1.659   9.632   1.00 51.62  ? 89  GLU A OE2   1 
ATOM   708  N  N     . SER A 1 90  ? 35.380  -0.330  5.902   1.00 41.73  ? 90  SER A N     1 
ATOM   709  C  CA    . SER A 1 90  ? 36.682  -0.048  5.306   1.00 40.95  ? 90  SER A CA    1 
ATOM   710  C  C     . SER A 1 90  ? 36.853  -0.690  3.935   1.00 43.79  ? 90  SER A C     1 
ATOM   711  O  O     . SER A 1 90  ? 37.775  -0.313  3.204   1.00 48.31  ? 90  SER A O     1 
ATOM   712  C  CB    . SER A 1 90  ? 37.804  -0.513  6.240   1.00 48.17  ? 90  SER A CB    1 
ATOM   713  O  OG    . SER A 1 90  ? 37.682  -1.891  6.547   1.00 47.77  ? 90  SER A OG    1 
ATOM   714  N  N     . LYS A 1 91  ? 35.996  -1.645  3.568   1.00 41.08  ? 91  LYS A N     1 
ATOM   715  C  CA    . LYS A 1 91  ? 36.048  -2.289  2.261   1.00 35.75  ? 91  LYS A CA    1 
ATOM   716  C  C     . LYS A 1 91  ? 34.814  -1.981  1.419   1.00 38.04  ? 91  LYS A C     1 
ATOM   717  O  O     . LYS A 1 91  ? 34.528  -2.695  0.454   1.00 32.83  ? 91  LYS A O     1 
ATOM   718  C  CB    . LYS A 1 91  ? 36.229  -3.798  2.424   1.00 35.86  ? 91  LYS A CB    1 
ATOM   719  C  CG    . LYS A 1 91  ? 37.560  -4.181  3.064   1.00 48.81  ? 91  LYS A CG    1 
ATOM   720  C  CD    . LYS A 1 91  ? 37.624  -5.662  3.396   1.00 54.46  ? 91  LYS A CD    1 
ATOM   721  C  CE    . LYS A 1 91  ? 39.041  -6.081  3.751   1.00 57.93  ? 91  LYS A CE    1 
ATOM   722  N  NZ    . LYS A 1 91  ? 39.643  -5.189  4.781   1.00 65.75  ? 91  LYS A NZ    1 
ATOM   723  N  N     . THR A 1 92  ? 34.082  -0.927  1.768   1.00 33.69  ? 92  THR A N     1 
ATOM   724  C  CA    . THR A 1 92  ? 32.903  -0.482  1.034   1.00 39.26  ? 92  THR A CA    1 
ATOM   725  C  C     . THR A 1 92  ? 33.263  0.827   0.341   1.00 36.56  ? 92  THR A C     1 
ATOM   726  O  O     . THR A 1 92  ? 33.400  1.865   0.998   1.00 40.51  ? 92  THR A O     1 
ATOM   727  C  CB    . THR A 1 92  ? 31.712  -0.309  1.974   1.00 32.99  ? 92  THR A CB    1 
ATOM   728  O  OG1   . THR A 1 92  ? 31.546  -1.499  2.754   1.00 29.79  ? 92  THR A OG1   1 
ATOM   729  C  CG2   . THR A 1 92  ? 30.437  -0.050  1.184   1.00 34.33  ? 92  THR A CG2   1 
ATOM   730  N  N     . VAL A 1 93  ? 33.412  0.779   -0.980  1.00 40.58  ? 93  VAL A N     1 
ATOM   731  C  CA    . VAL A 1 93  ? 33.972  1.887   -1.740  1.00 39.43  ? 93  VAL A CA    1 
ATOM   732  C  C     . VAL A 1 93  ? 32.958  2.395   -2.755  1.00 36.58  ? 93  VAL A C     1 
ATOM   733  O  O     . VAL A 1 93  ? 32.053  1.671   -3.187  1.00 33.92  ? 93  VAL A O     1 
ATOM   734  C  CB    . VAL A 1 93  ? 35.283  1.478   -2.447  1.00 41.10  ? 93  VAL A CB    1 
ATOM   735  C  CG1   . VAL A 1 93  ? 36.322  1.041   -1.427  1.00 40.74  ? 93  VAL A CG1   1 
ATOM   736  C  CG2   . VAL A 1 93  ? 35.017  0.370   -3.456  1.00 35.22  ? 93  VAL A CG2   1 
ATOM   737  N  N     . ILE A 1 94  ? 33.123  3.661   -3.133  1.00 37.38  ? 94  ILE A N     1 
ATOM   738  C  CA    . ILE A 1 94  ? 32.343  4.300   -4.186  1.00 37.68  ? 94  ILE A CA    1 
ATOM   739  C  C     . ILE A 1 94  ? 33.316  4.811   -5.238  1.00 41.17  ? 94  ILE A C     1 
ATOM   740  O  O     . ILE A 1 94  ? 34.333  5.430   -4.900  1.00 39.86  ? 94  ILE A O     1 
ATOM   741  C  CB    . ILE A 1 94  ? 31.476  5.449   -3.638  1.00 38.97  ? 94  ILE A CB    1 
ATOM   742  C  CG1   . ILE A 1 94  ? 30.507  4.925   -2.578  1.00 35.33  ? 94  ILE A CG1   1 
ATOM   743  C  CG2   . ILE A 1 94  ? 30.720  6.139   -4.767  1.00 35.15  ? 94  ILE A CG2   1 
ATOM   744  C  CD1   . ILE A 1 94  ? 29.631  5.995   -1.992  1.00 44.29  ? 94  ILE A CD1   1 
ATOM   745  N  N     . ILE A 1 95  ? 33.010  4.551   -6.505  1.00 35.06  ? 95  ILE A N     1 
ATOM   746  C  CA    . ILE A 1 95  ? 33.884  4.908   -7.616  1.00 41.33  ? 95  ILE A CA    1 
ATOM   747  C  C     . ILE A 1 95  ? 33.220  6.020   -8.417  1.00 48.04  ? 95  ILE A C     1 
ATOM   748  O  O     . ILE A 1 95  ? 32.113  5.843   -8.942  1.00 42.95  ? 95  ILE A O     1 
ATOM   749  C  CB    . ILE A 1 95  ? 34.198  3.699   -8.509  1.00 43.37  ? 95  ILE A CB    1 
ATOM   750  C  CG1   . ILE A 1 95  ? 35.014  2.655   -7.741  1.00 42.19  ? 95  ILE A CG1   1 
ATOM   751  C  CG2   . ILE A 1 95  ? 34.944  4.143   -9.756  1.00 46.19  ? 95  ILE A CG2   1 
ATOM   752  C  CD1   . ILE A 1 95  ? 34.196  1.535   -7.169  1.00 41.77  ? 95  ILE A CD1   1 
ATOM   753  N  N     . THR A 1 96  ? 33.897  7.164   -8.504  1.00 45.55  ? 96  THR A N     1 
ATOM   754  C  CA    . THR A 1 96  ? 33.470  8.276   -9.340  1.00 50.15  ? 96  THR A CA    1 
ATOM   755  C  C     . THR A 1 96  ? 34.691  8.851   -10.044 1.00 56.31  ? 96  THR A C     1 
ATOM   756  O  O     . THR A 1 96  ? 35.831  8.642   -9.622  1.00 55.54  ? 96  THR A O     1 
ATOM   757  C  CB    . THR A 1 96  ? 32.764  9.379   -8.532  1.00 46.96  ? 96  THR A CB    1 
ATOM   758  O  OG1   . THR A 1 96  ? 33.609  9.809   -7.459  1.00 46.66  ? 96  THR A OG1   1 
ATOM   759  C  CG2   . THR A 1 96  ? 31.440  8.877   -7.965  1.00 44.66  ? 96  THR A CG2   1 
ATOM   760  N  N     . GLN A 1 97  ? 34.438  9.579   -11.134 1.00 57.05  ? 97  GLN A N     1 
ATOM   761  C  CA    . GLN A 1 97  ? 35.528  10.219  -11.862 1.00 64.50  ? 97  GLN A CA    1 
ATOM   762  C  C     . GLN A 1 97  ? 36.284  11.193  -10.966 1.00 61.15  ? 97  GLN A C     1 
ATOM   763  O  O     . GLN A 1 97  ? 37.520  11.196  -10.935 1.00 61.20  ? 97  GLN A O     1 
ATOM   764  C  CB    . GLN A 1 97  ? 34.985  10.932  -13.101 1.00 70.56  ? 97  GLN A CB    1 
ATOM   765  C  CG    . GLN A 1 97  ? 36.039  11.677  -13.907 1.00 81.55  ? 97  GLN A CG    1 
ATOM   766  C  CD    . GLN A 1 97  ? 37.082  10.753  -14.508 1.00 88.95  ? 97  GLN A CD    1 
ATOM   767  O  OE1   . GLN A 1 97  ? 36.827  9.569   -14.731 1.00 90.44  ? 97  GLN A OE1   1 
ATOM   768  N  NE2   . GLN A 1 97  ? 38.268  11.292  -14.771 1.00 87.41  ? 97  GLN A NE2   1 
ATOM   769  N  N     . GLU A 1 98  ? 35.556  12.017  -10.220 1.00 54.99  ? 98  GLU A N     1 
ATOM   770  C  CA    . GLU A 1 98  ? 36.140  12.978  -9.297  1.00 57.10  ? 98  GLU A CA    1 
ATOM   771  C  C     . GLU A 1 98  ? 35.858  12.555  -7.863  1.00 53.22  ? 98  GLU A C     1 
ATOM   772  O  O     . GLU A 1 98  ? 34.736  12.155  -7.533  1.00 48.17  ? 98  GLU A O     1 
ATOM   773  C  CB    . GLU A 1 98  ? 35.588  14.384  -9.548  1.00 62.57  ? 98  GLU A CB    1 
ATOM   774  C  CG    . GLU A 1 98  ? 35.887  14.920  -10.938 1.00 68.64  ? 98  GLU A CG    1 
ATOM   775  C  CD    . GLU A 1 98  ? 37.373  15.068  -11.194 1.00 76.44  ? 98  GLU A CD    1 
ATOM   776  O  OE1   . GLU A 1 98  ? 38.106  15.431  -10.248 1.00 81.02  ? 98  GLU A OE1   1 
ATOM   777  O  OE2   . GLU A 1 98  ? 37.810  14.816  -12.337 1.00 87.91  ? 98  GLU A OE2   1 
ATOM   778  N  N     . GLN A 1 99  ? 36.883  12.646  -7.011  1.00 49.30  ? 99  GLN A N     1 
ATOM   779  C  CA    . GLN A 1 99  ? 36.714  12.273  -5.611  1.00 52.30  ? 99  GLN A CA    1 
ATOM   780  C  C     . GLN A 1 99  ? 35.734  13.196  -4.896  1.00 50.97  ? 99  GLN A C     1 
ATOM   781  O  O     . GLN A 1 99  ? 35.005  12.752  -4.001  1.00 45.95  ? 99  GLN A O     1 
ATOM   782  C  CB    . GLN A 1 99  ? 38.067  12.283  -4.896  1.00 49.38  ? 99  GLN A CB    1 
ATOM   783  C  CG    . GLN A 1 99  ? 37.994  11.846  -3.439  1.00 49.04  ? 99  GLN A CG    1 
ATOM   784  C  CD    . GLN A 1 99  ? 39.307  12.024  -2.702  1.00 58.32  ? 99  GLN A CD    1 
ATOM   785  O  OE1   . GLN A 1 99  ? 40.307  12.448  -3.283  1.00 62.25  ? 99  GLN A OE1   1 
ATOM   786  N  NE2   . GLN A 1 99  ? 39.308  11.704  -1.413  1.00 61.55  ? 99  GLN A NE2   1 
ATOM   787  N  N     . ARG A 1 100 ? 35.694  14.475  -5.282  1.00 47.58  ? 100 ARG A N     1 
ATOM   788  C  CA    . ARG A 1 100 ? 34.826  15.437  -4.614  1.00 47.98  ? 100 ARG A CA    1 
ATOM   789  C  C     . ARG A 1 100 ? 33.348  15.111  -4.795  1.00 46.59  ? 100 ARG A C     1 
ATOM   790  O  O     . ARG A 1 100 ? 32.522  15.569  -3.998  1.00 45.47  ? 100 ARG A O     1 
ATOM   791  C  CB    . ARG A 1 100 ? 35.124  16.850  -5.126  1.00 51.54  ? 100 ARG A CB    1 
ATOM   792  C  CG    . ARG A 1 100 ? 34.541  17.962  -4.265  1.00 58.95  ? 100 ARG A CG    1 
ATOM   793  C  CD    . ARG A 1 100 ? 35.004  19.333  -4.732  1.00 67.09  ? 100 ARG A CD    1 
ATOM   794  N  NE    . ARG A 1 100 ? 34.573  20.389  -3.823  1.00 68.60  ? 100 ARG A NE    1 
ATOM   795  C  CZ    . ARG A 1 100 ? 34.966  21.653  -3.902  1.00 75.53  ? 100 ARG A CZ    1 
ATOM   796  N  NH1   . ARG A 1 100 ? 35.804  22.059  -4.842  1.00 76.96  ? 100 ARG A NH1   1 
ATOM   797  N  NH2   . ARG A 1 100 ? 34.510  22.532  -3.013  1.00 72.93  ? 100 ARG A NH2   1 
ATOM   798  N  N     . ASP A 1 101 ? 32.995  14.330  -5.819  1.00 46.58  ? 101 ASP A N     1 
ATOM   799  C  CA    . ASP A 1 101 ? 31.606  13.917  -5.982  1.00 48.96  ? 101 ASP A CA    1 
ATOM   800  C  C     . ASP A 1 101 ? 31.201  12.891  -4.932  1.00 43.23  ? 101 ASP A C     1 
ATOM   801  O  O     . ASP A 1 101 ? 30.016  12.787  -4.596  1.00 43.66  ? 101 ASP A O     1 
ATOM   802  C  CB    . ASP A 1 101 ? 31.380  13.353  -7.385  1.00 52.19  ? 101 ASP A CB    1 
ATOM   803  C  CG    . ASP A 1 101 ? 31.491  14.410  -8.463  1.00 63.20  ? 101 ASP A CG    1 
ATOM   804  O  OD1   . ASP A 1 101 ? 31.208  15.591  -8.170  1.00 66.36  ? 101 ASP A OD1   1 
ATOM   805  O  OD2   . ASP A 1 101 ? 31.860  14.060  -9.604  1.00 73.07  ? 101 ASP A OD2   1 
ATOM   806  N  N     . THR A 1 102 ? 32.162  12.134  -4.404  1.00 43.65  ? 102 THR A N     1 
ATOM   807  C  CA    . THR A 1 102 ? 31.888  11.098  -3.416  1.00 42.20  ? 102 THR A CA    1 
ATOM   808  C  C     . THR A 1 102 ? 32.020  11.618  -1.987  1.00 40.28  ? 102 THR A C     1 
ATOM   809  O  O     . THR A 1 102 ? 31.108  11.441  -1.174  1.00 40.59  ? 102 THR A O     1 
ATOM   810  C  CB    . THR A 1 102 ? 32.826  9.904   -3.631  1.00 41.73  ? 102 THR A CB    1 
ATOM   811  O  OG1   . THR A 1 102 ? 32.496  9.254   -4.864  1.00 44.40  ? 102 THR A OG1   1 
ATOM   812  C  CG2   . THR A 1 102 ? 32.704  8.907   -2.484  1.00 37.50  ? 102 THR A CG2   1 
ATOM   813  N  N     . VAL A 1 103 ? 33.145  12.247  -1.664  1.00 41.22  ? 103 VAL A N     1 
ATOM   814  C  CA    . VAL A 1 103 ? 33.383  12.760  -0.317  1.00 42.64  ? 103 VAL A CA    1 
ATOM   815  C  C     . VAL A 1 103 ? 33.929  14.179  -0.408  1.00 44.66  ? 103 VAL A C     1 
ATOM   816  O  O     . VAL A 1 103 ? 34.581  14.531  -1.403  1.00 49.21  ? 103 VAL A O     1 
ATOM   817  C  CB    . VAL A 1 103 ? 34.352  11.858  0.467   1.00 45.39  ? 103 VAL A CB    1 
ATOM   818  C  CG1   . VAL A 1 103 ? 33.742  10.486  0.708   1.00 41.18  ? 103 VAL A CG1   1 
ATOM   819  C  CG2   . VAL A 1 103 ? 35.686  11.739  -0.267  1.00 43.88  ? 103 VAL A CG2   1 
ATOM   820  N  N     . PRO A 1 104 ? 33.684  15.028  0.588   1.00 45.85  ? 104 PRO A N     1 
ATOM   821  C  CA    . PRO A 1 104 ? 34.399  16.306  0.645   1.00 48.61  ? 104 PRO A CA    1 
ATOM   822  C  C     . PRO A 1 104 ? 35.889  16.059  0.819   1.00 49.88  ? 104 PRO A C     1 
ATOM   823  O  O     . PRO A 1 104 ? 36.308  15.079  1.438   1.00 49.76  ? 104 PRO A O     1 
ATOM   824  C  CB    . PRO A 1 104 ? 33.798  17.003  1.874   1.00 49.05  ? 104 PRO A CB    1 
ATOM   825  C  CG    . PRO A 1 104 ? 32.514  16.287  2.146   1.00 46.78  ? 104 PRO A CG    1 
ATOM   826  C  CD    . PRO A 1 104 ? 32.724  14.876  1.693   1.00 44.84  ? 104 PRO A CD    1 
ATOM   827  N  N     . ILE A 1 105 ? 36.691  16.951  0.249   1.00 52.09  ? 105 ILE A N     1 
ATOM   828  C  CA    . ILE A 1 105 ? 38.141  16.858  0.393   1.00 54.12  ? 105 ILE A CA    1 
ATOM   829  C  C     . ILE A 1 105 ? 38.499  17.327  1.798   1.00 55.81  ? 105 ILE A C     1 
ATOM   830  O  O     . ILE A 1 105 ? 38.335  18.515  2.112   1.00 57.40  ? 105 ILE A O     1 
ATOM   831  C  CB    . ILE A 1 105 ? 38.870  17.680  -0.682  1.00 57.32  ? 105 ILE A CB    1 
ATOM   832  C  CG1   . ILE A 1 105 ? 38.449  17.220  -2.080  1.00 54.79  ? 105 ILE A CG1   1 
ATOM   833  C  CG2   . ILE A 1 105 ? 40.375  17.558  -0.512  1.00 58.63  ? 105 ILE A CG2   1 
ATOM   834  C  CD1   . ILE A 1 105 ? 38.673  15.746  -2.332  1.00 56.07  ? 105 ILE A CD1   1 
ATOM   835  N  N     . PRO A 1 106 ? 38.971  16.441  2.671   1.00 55.76  ? 106 PRO A N     1 
ATOM   836  C  CA    . PRO A 1 106 ? 39.230  16.837  4.058   1.00 57.53  ? 106 PRO A CA    1 
ATOM   837  C  C     . PRO A 1 106 ? 40.367  17.843  4.153   1.00 60.98  ? 106 PRO A C     1 
ATOM   838  O  O     . PRO A 1 106 ? 41.233  17.939  3.281   1.00 62.19  ? 106 PRO A O     1 
ATOM   839  C  CB    . PRO A 1 106 ? 39.599  15.517  4.748   1.00 56.93  ? 106 PRO A CB    1 
ATOM   840  C  CG    . PRO A 1 106 ? 39.128  14.443  3.823   1.00 54.15  ? 106 PRO A CG    1 
ATOM   841  C  CD    . PRO A 1 106 ? 39.253  15.014  2.448   1.00 54.28  ? 106 PRO A CD    1 
ATOM   842  N  N     . LYS A 1 107 ? 40.347  18.611  5.242   1.00 62.79  ? 107 LYS A N     1 
ATOM   843  C  CA    . LYS A 1 107 ? 41.365  19.636  5.430   1.00 66.32  ? 107 LYS A CA    1 
ATOM   844  C  C     . LYS A 1 107 ? 42.675  19.041  5.934   1.00 68.49  ? 107 LYS A C     1 
ATOM   845  O  O     . LYS A 1 107 ? 43.755  19.497  5.543   1.00 72.54  ? 107 LYS A O     1 
ATOM   846  C  CB    . LYS A 1 107 ? 40.859  20.713  6.391   1.00 67.77  ? 107 LYS A CB    1 
ATOM   847  C  CG    . LYS A 1 107 ? 41.702  21.976  6.401   1.00 71.34  ? 107 LYS A CG    1 
ATOM   848  C  CD    . LYS A 1 107 ? 41.096  23.054  7.284   1.00 72.75  ? 107 LYS A CD    1 
ATOM   849  C  CE    . LYS A 1 107 ? 41.940  24.322  7.253   1.00 89.58  ? 107 LYS A CE    1 
ATOM   850  N  NZ    . LYS A 1 107 ? 41.372  25.402  8.110   1.00 94.48  ? 107 LYS A NZ    1 
ATOM   851  N  N     . SER A 1 108 ? 42.606  18.020  6.789   1.00 71.85  ? 108 SER A N     1 
ATOM   852  C  CA    . SER A 1 108 ? 43.815  17.440  7.361   1.00 74.29  ? 108 SER A CA    1 
ATOM   853  C  C     . SER A 1 108 ? 43.873  15.930  7.168   1.00 72.38  ? 108 SER A C     1 
ATOM   854  O  O     . SER A 1 108 ? 44.579  15.440  6.281   1.00 73.44  ? 108 SER A O     1 
ATOM   855  C  CB    . SER A 1 108 ? 43.918  17.785  8.849   1.00 76.60  ? 108 SER A CB    1 
ATOM   856  O  OG    . SER A 1 108 ? 44.201  19.161  9.031   1.00 82.51  ? 108 SER A OG    1 
ATOM   857  N  N     . GLY A 1 109 ? 43.146  15.183  7.994   1.00 66.62  ? 109 GLY A N     1 
ATOM   858  C  CA    . GLY A 1 109 ? 43.209  13.736  7.942   1.00 65.13  ? 109 GLY A CA    1 
ATOM   859  C  C     . GLY A 1 109 ? 42.519  13.137  6.734   1.00 62.17  ? 109 GLY A C     1 
ATOM   860  O  O     . GLY A 1 109 ? 42.281  13.828  5.739   1.00 64.78  ? 109 GLY A O     1 
ATOM   861  N  N     . GLN A 1 110 ? 42.204  11.848  6.800   1.00 59.80  ? 110 GLN A N     1 
ATOM   862  C  CA    . GLN A 1 110 ? 41.442  11.207  5.743   1.00 56.57  ? 110 GLN A CA    1 
ATOM   863  C  C     . GLN A 1 110 ? 39.949  11.320  6.038   1.00 53.96  ? 110 GLN A C     1 
ATOM   864  O  O     . GLN A 1 110 ? 39.533  11.607  7.163   1.00 54.53  ? 110 GLN A O     1 
ATOM   865  C  CB    . GLN A 1 110 ? 41.848  9.741   5.584   1.00 58.80  ? 110 GLN A CB    1 
ATOM   866  C  CG    . GLN A 1 110 ? 41.436  8.837   6.733   1.00 61.47  ? 110 GLN A CG    1 
ATOM   867  C  CD    . GLN A 1 110 ? 41.826  7.388   6.498   1.00 57.30  ? 110 GLN A CD    1 
ATOM   868  O  OE1   . GLN A 1 110 ? 42.599  7.079   5.589   1.00 56.19  ? 110 GLN A OE1   1 
ATOM   869  N  NE2   . GLN A 1 110 ? 41.289  6.491   7.317   1.00 54.07  ? 110 GLN A NE2   1 
ATOM   870  N  N     . SER A 1 111 ? 39.143  11.093  5.006   1.00 51.35  ? 111 SER A N     1 
ATOM   871  C  CA    . SER A 1 111 ? 37.703  11.269  5.124   1.00 49.11  ? 111 SER A CA    1 
ATOM   872  C  C     . SER A 1 111 ? 37.067  10.101  5.866   1.00 47.53  ? 111 SER A C     1 
ATOM   873  O  O     . SER A 1 111 ? 37.377  8.935   5.605   1.00 46.89  ? 111 SER A O     1 
ATOM   874  C  CB    . SER A 1 111 ? 37.069  11.411  3.741   1.00 47.25  ? 111 SER A CB    1 
ATOM   875  O  OG    . SER A 1 111 ? 35.664  11.571  3.844   1.00 45.39  ? 111 SER A OG    1 
ATOM   876  N  N     . GLN A 1 112 ? 36.172  10.426  6.799   1.00 48.57  ? 112 GLN A N     1 
ATOM   877  C  CA    . GLN A 1 112 ? 35.352  9.438   7.486   1.00 45.78  ? 112 GLN A CA    1 
ATOM   878  C  C     . GLN A 1 112 ? 33.967  9.305   6.874   1.00 45.00  ? 112 GLN A C     1 
ATOM   879  O  O     . GLN A 1 112 ? 33.152  8.527   7.378   1.00 48.70  ? 112 GLN A O     1 
ATOM   880  C  CB    . GLN A 1 112 ? 35.205  9.795   8.969   1.00 47.51  ? 112 GLN A CB    1 
ATOM   881  C  CG    . GLN A 1 112 ? 36.504  9.913   9.742   1.00 56.40  ? 112 GLN A CG    1 
ATOM   882  C  CD    . GLN A 1 112 ? 36.267  10.096  11.229  1.00 52.30  ? 112 GLN A CD    1 
ATOM   883  O  OE1   . GLN A 1 112 ? 35.162  9.869   11.723  1.00 56.81  ? 112 GLN A OE1   1 
ATOM   884  N  NE2   . GLN A 1 112 ? 37.302  10.510  11.950  1.00 59.82  ? 112 GLN A NE2   1 
ATOM   885  N  N     . LEU A 1 113 ? 33.679  10.047  5.807   1.00 47.57  ? 113 LEU A N     1 
ATOM   886  C  CA    . LEU A 1 113 ? 32.342  10.126  5.241   1.00 40.64  ? 113 LEU A CA    1 
ATOM   887  C  C     . LEU A 1 113 ? 32.163  9.232   4.022   1.00 44.79  ? 113 LEU A C     1 
ATOM   888  O  O     . LEU A 1 113 ? 31.147  9.345   3.328   1.00 42.18  ? 113 LEU A O     1 
ATOM   889  C  CB    . LEU A 1 113 ? 32.017  11.578  4.888   1.00 45.53  ? 113 LEU A CB    1 
ATOM   890  C  CG    . LEU A 1 113 ? 32.047  12.514  6.097   1.00 45.26  ? 113 LEU A CG    1 
ATOM   891  C  CD1   . LEU A 1 113 ? 32.079  13.975  5.675   1.00 45.18  ? 113 LEU A CD1   1 
ATOM   892  C  CD2   . LEU A 1 113 ? 30.852  12.236  6.990   1.00 42.94  ? 113 LEU A CD2   1 
ATOM   893  N  N     . GLY A 1 114 ? 33.110  8.352   3.757   1.00 47.08  ? 114 GLY A N     1 
ATOM   894  C  CA    . GLY A 1 114 ? 33.031  7.429   2.642   1.00 43.67  ? 114 GLY A CA    1 
ATOM   895  C  C     . GLY A 1 114 ? 34.409  7.134   2.092   1.00 43.18  ? 114 GLY A C     1 
ATOM   896  O  O     . GLY A 1 114 ? 35.358  7.897   2.250   1.00 48.11  ? 114 GLY A O     1 
ATOM   897  N  N     . ARG A 1 115 ? 34.521  5.987   1.425   1.00 47.64  ? 115 ARG A N     1 
ATOM   898  C  CA    . ARG A 1 115 ? 35.765  5.553   0.799   1.00 45.78  ? 115 ARG A CA    1 
ATOM   899  C  C     . ARG A 1 115 ? 35.629  5.696   -0.712  1.00 44.92  ? 115 ARG A C     1 
ATOM   900  O  O     . ARG A 1 115 ? 34.837  4.986   -1.341  1.00 42.26  ? 115 ARG A O     1 
ATOM   901  C  CB    . ARG A 1 115 ? 36.102  4.115   1.184   1.00 47.99  ? 115 ARG A CB    1 
ATOM   902  C  CG    . ARG A 1 115 ? 36.847  3.983   2.498   1.00 55.85  ? 115 ARG A CG    1 
ATOM   903  C  CD    . ARG A 1 115 ? 37.795  2.796   2.458   1.00 68.20  ? 115 ARG A CD    1 
ATOM   904  N  NE    . ARG A 1 115 ? 38.637  2.820   1.268   1.00 79.67  ? 115 ARG A NE    1 
ATOM   905  C  CZ    . ARG A 1 115 ? 39.640  1.982   1.038   1.00 75.86  ? 115 ARG A CZ    1 
ATOM   906  N  NH1   . ARG A 1 115 ? 39.970  1.042   1.909   1.00 77.41  ? 115 ARG A NH1   1 
ATOM   907  N  NH2   . ARG A 1 115 ? 40.330  2.092   -0.094  1.00 66.91  ? 115 ARG A NH2   1 
ATOM   908  N  N     . TRP A 1 116 ? 36.400  6.612   -1.288  1.00 45.22  ? 116 TRP A N     1 
ATOM   909  C  CA    . TRP A 1 116 ? 36.427  6.803   -2.729  1.00 44.70  ? 116 TRP A CA    1 
ATOM   910  C  C     . TRP A 1 116 ? 37.560  5.995   -3.348  1.00 46.78  ? 116 TRP A C     1 
ATOM   911  O  O     . TRP A 1 116 ? 38.628  5.826   -2.753  1.00 46.73  ? 116 TRP A O     1 
ATOM   912  C  CB    . TRP A 1 116 ? 36.591  8.285   -3.077  1.00 45.65  ? 116 TRP A CB    1 
ATOM   913  C  CG    . TRP A 1 116 ? 36.727  8.545   -4.550  1.00 44.71  ? 116 TRP A CG    1 
ATOM   914  C  CD1   . TRP A 1 116 ? 35.718  8.638   -5.464  1.00 45.78  ? 116 TRP A CD1   1 
ATOM   915  C  CD2   . TRP A 1 116 ? 37.945  8.743   -5.276  1.00 47.51  ? 116 TRP A CD2   1 
ATOM   916  N  NE1   . TRP A 1 116 ? 36.232  8.883   -6.715  1.00 49.14  ? 116 TRP A NE1   1 
ATOM   917  C  CE2   . TRP A 1 116 ? 37.598  8.951   -6.626  1.00 48.21  ? 116 TRP A CE2   1 
ATOM   918  C  CE3   . TRP A 1 116 ? 39.296  8.766   -4.915  1.00 50.21  ? 116 TRP A CE3   1 
ATOM   919  C  CZ2   . TRP A 1 116 ? 38.552  9.179   -7.616  1.00 49.98  ? 116 TRP A CZ2   1 
ATOM   920  C  CZ3   . TRP A 1 116 ? 40.243  8.993   -5.900  1.00 51.66  ? 116 TRP A CZ3   1 
ATOM   921  C  CH2   . TRP A 1 116 ? 39.866  9.196   -7.234  1.00 48.74  ? 116 TRP A CH2   1 
ATOM   922  N  N     . MET A 1 117 ? 37.314  5.493   -4.555  1.00 43.66  ? 117 MET A N     1 
ATOM   923  C  CA    . MET A 1 117 ? 38.296  4.727   -5.307  1.00 47.77  ? 117 MET A CA    1 
ATOM   924  C  C     . MET A 1 117 ? 38.169  5.076   -6.781  1.00 44.09  ? 117 MET A C     1 
ATOM   925  O  O     . MET A 1 117 ? 37.057  5.168   -7.308  1.00 45.54  ? 117 MET A O     1 
ATOM   926  C  CB    . MET A 1 117 ? 38.107  3.218   -5.101  1.00 47.38  ? 117 MET A CB    1 
ATOM   927  C  CG    . MET A 1 117 ? 39.046  2.353   -5.923  1.00 50.72  ? 117 MET A CG    1 
ATOM   928  S  SD    . MET A 1 117 ? 38.705  0.592   -5.731  1.00 53.29  ? 117 MET A SD    1 
ATOM   929  C  CE    . MET A 1 117 ? 38.934  0.394   -3.967  1.00 58.32  ? 117 MET A CE    1 
ATOM   930  N  N     . SER A 1 118 ? 39.306  5.276   -7.439  1.00 44.70  ? 118 SER A N     1 
ATOM   931  C  CA    . SER A 1 118 ? 39.294  5.632   -8.848  1.00 51.71  ? 118 SER A CA    1 
ATOM   932  C  C     . SER A 1 118 ? 38.850  4.446   -9.701  1.00 53.49  ? 118 SER A C     1 
ATOM   933  O  O     . SER A 1 118 ? 38.869  3.289   -9.270  1.00 53.34  ? 118 SER A O     1 
ATOM   934  C  CB    . SER A 1 118 ? 40.676  6.103   -9.297  1.00 51.75  ? 118 SER A CB    1 
ATOM   935  O  OG    . SER A 1 118 ? 41.578  5.013   -9.380  1.00 53.67  ? 118 SER A OG    1 
ATOM   936  N  N     . GLU A 1 119 ? 38.440  4.752   -10.935 1.00 55.14  ? 119 GLU A N     1 
ATOM   937  C  CA    . GLU A 1 119 ? 38.080  3.697   -11.876 1.00 61.27  ? 119 GLU A CA    1 
ATOM   938  C  C     . GLU A 1 119 ? 39.275  2.806   -12.185 1.00 57.95  ? 119 GLU A C     1 
ATOM   939  O  O     . GLU A 1 119 ? 39.145  1.577   -12.237 1.00 54.82  ? 119 GLU A O     1 
ATOM   940  C  CB    . GLU A 1 119 ? 37.528  4.301   -13.167 1.00 69.69  ? 119 GLU A CB    1 
ATOM   941  C  CG    . GLU A 1 119 ? 36.176  4.972   -13.029 1.00 78.61  ? 119 GLU A CG    1 
ATOM   942  C  CD    . GLU A 1 119 ? 36.270  6.398   -12.524 1.00 86.00  ? 119 GLU A CD    1 
ATOM   943  O  OE1   . GLU A 1 119 ? 37.387  6.846   -12.185 1.00 75.57  ? 119 GLU A OE1   1 
ATOM   944  O  OE2   . GLU A 1 119 ? 35.221  7.074   -12.473 1.00 91.59  ? 119 GLU A OE2   1 
ATOM   945  N  N     . GLU A 1 120 ? 40.447  3.410   -12.393 1.00 58.82  ? 120 GLU A N     1 
ATOM   946  C  CA    . GLU A 1 120 ? 41.639  2.636   -12.727 1.00 66.58  ? 120 GLU A CA    1 
ATOM   947  C  C     . GLU A 1 120 ? 41.995  1.658   -11.615 1.00 58.88  ? 120 GLU A C     1 
ATOM   948  O  O     . GLU A 1 120 ? 42.374  0.512   -11.883 1.00 58.90  ? 120 GLU A O     1 
ATOM   949  C  CB    . GLU A 1 120 ? 42.814  3.575   -13.009 1.00 60.62  ? 120 GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 120 ? 42.684  4.397   -14.289 1.00 81.39  ? 120 GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 120 ? 41.700  5.548   -14.165 1.00 85.55  ? 120 GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 120 ? 41.206  5.798   -13.045 1.00 76.82  ? 120 GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 120 ? 41.423  6.204   -15.191 1.00 92.41  ? 120 GLU A OE2   1 
ATOM   954  N  N     . ASP A 1 121 ? 41.877  2.091   -10.358 1.00 52.41  ? 121 ASP A N     1 
ATOM   955  C  CA    . ASP A 1 121 ? 42.180  1.197   -9.246  1.00 56.21  ? 121 ASP A CA    1 
ATOM   956  C  C     . ASP A 1 121 ? 41.137  0.092   -9.123  1.00 54.97  ? 121 ASP A C     1 
ATOM   957  O  O     . ASP A 1 121 ? 41.480  -1.061  -8.836  1.00 52.36  ? 121 ASP A O     1 
ATOM   958  C  CB    . ASP A 1 121 ? 42.284  1.993   -7.946  1.00 50.07  ? 121 ASP A CB    1 
ATOM   959  C  CG    . ASP A 1 121 ? 43.472  2.937   -7.933  1.00 58.34  ? 121 ASP A CG    1 
ATOM   960  O  OD1   . ASP A 1 121 ? 44.453  2.672   -8.661  1.00 62.51  ? 121 ASP A OD1   1 
ATOM   961  O  OD2   . ASP A 1 121 ? 43.429  3.942   -7.192  1.00 58.03  ? 121 ASP A OD2   1 
ATOM   962  N  N     . PHE A 1 122 ? 39.859  0.417   -9.343  1.00 47.58  ? 122 PHE A N     1 
ATOM   963  C  CA    . PHE A 1 122 ? 38.823  -0.604  -9.228  1.00 48.51  ? 122 PHE A CA    1 
ATOM   964  C  C     . PHE A 1 122 ? 38.896  -1.619  -10.362 1.00 47.68  ? 122 PHE A C     1 
ATOM   965  O  O     . PHE A 1 122 ? 38.550  -2.788  -10.160 1.00 46.89  ? 122 PHE A O     1 
ATOM   966  C  CB    . PHE A 1 122 ? 37.434  0.031   -9.188  1.00 43.33  ? 122 PHE A CB    1 
ATOM   967  C  CG    . PHE A 1 122 ? 36.318  -0.974  -9.264  1.00 46.94  ? 122 PHE A CG    1 
ATOM   968  C  CD1   . PHE A 1 122 ? 36.072  -1.833  -8.206  1.00 42.31  ? 122 PHE A CD1   1 
ATOM   969  C  CD2   . PHE A 1 122 ? 35.531  -1.074  -10.399 1.00 44.22  ? 122 PHE A CD2   1 
ATOM   970  C  CE1   . PHE A 1 122 ? 35.060  -2.767  -8.274  1.00 42.42  ? 122 PHE A CE1   1 
ATOM   971  C  CE2   . PHE A 1 122 ? 34.511  -2.005  -10.471 1.00 45.89  ? 122 PHE A CE2   1 
ATOM   972  C  CZ    . PHE A 1 122 ? 34.276  -2.853  -9.406  1.00 40.41  ? 122 PHE A CZ    1 
ATOM   973  N  N     . GLU A 1 123 ? 39.326  -1.196  -11.555 1.00 47.05  ? 123 GLU A N     1 
ATOM   974  C  CA    . GLU A 1 123 ? 39.492  -2.141  -12.656 1.00 50.27  ? 123 GLU A CA    1 
ATOM   975  C  C     . GLU A 1 123 ? 40.476  -3.241  -12.285 1.00 48.18  ? 123 GLU A C     1 
ATOM   976  O  O     . GLU A 1 123 ? 40.229  -4.425  -12.540 1.00 46.53  ? 123 GLU A O     1 
ATOM   977  C  CB    . GLU A 1 123 ? 39.958  -1.413  -13.918 1.00 57.09  ? 123 GLU A CB    1 
ATOM   978  C  CG    . GLU A 1 123 ? 38.843  -0.791  -14.739 1.00 66.08  ? 123 GLU A CG    1 
ATOM   979  C  CD    . GLU A 1 123 ? 39.306  -0.385  -16.126 1.00 82.29  ? 123 GLU A CD    1 
ATOM   980  O  OE1   . GLU A 1 123 ? 40.497  -0.591  -16.442 1.00 83.25  ? 123 GLU A OE1   1 
ATOM   981  O  OE2   . GLU A 1 123 ? 38.478  0.138   -16.901 1.00 90.69  ? 123 GLU A OE2   1 
ATOM   982  N  N     . LYS A 1 124 ? 41.601  -2.863  -11.674 1.00 51.64  ? 124 LYS A N     1 
ATOM   983  C  CA    . LYS A 1 124 ? 42.579  -3.856  -11.244 1.00 48.97  ? 124 LYS A CA    1 
ATOM   984  C  C     . LYS A 1 124 ? 42.007  -4.760  -10.160 1.00 46.88  ? 124 LYS A C     1 
ATOM   985  O  O     . LYS A 1 124 ? 42.224  -5.977  -10.177 1.00 48.21  ? 124 LYS A O     1 
ATOM   986  C  CB    . LYS A 1 124 ? 43.847  -3.155  -10.756 1.00 51.76  ? 124 LYS A CB    1 
ATOM   987  C  CG    . LYS A 1 124 ? 44.426  -2.180  -11.767 1.00 58.80  ? 124 LYS A CG    1 
ATOM   988  C  CD    . LYS A 1 124 ? 45.650  -1.462  -11.223 1.00 70.11  ? 124 LYS A CD    1 
ATOM   989  C  CE    . LYS A 1 124 ? 46.270  -0.565  -12.283 1.00 76.50  ? 124 LYS A CE    1 
ATOM   990  N  NZ    . LYS A 1 124 ? 45.304  0.448   -12.793 1.00 78.77  ? 124 LYS A NZ    1 
ATOM   991  N  N     . ALA A 1 125 ? 41.262  -4.184  -9.213  1.00 46.65  ? 125 ALA A N     1 
ATOM   992  C  CA    . ALA A 1 125 ? 40.660  -4.988  -8.155  1.00 42.95  ? 125 ALA A CA    1 
ATOM   993  C  C     . ALA A 1 125 ? 39.592  -5.922  -8.711  1.00 45.86  ? 125 ALA A C     1 
ATOM   994  O  O     . ALA A 1 125 ? 39.478  -7.074  -8.275  1.00 44.02  ? 125 ALA A O     1 
ATOM   995  C  CB    . ALA A 1 125 ? 40.071  -4.078  -7.078  1.00 46.31  ? 125 ALA A CB    1 
ATOM   996  N  N     . PHE A 1 126 ? 38.801  -5.442  -9.672  1.00 46.19  ? 126 PHE A N     1 
ATOM   997  C  CA    . PHE A 1 126 ? 37.776  -6.280  -10.284 1.00 39.99  ? 126 PHE A CA    1 
ATOM   998  C  C     . PHE A 1 126 ? 38.401  -7.456  -11.025 1.00 45.63  ? 126 PHE A C     1 
ATOM   999  O  O     . PHE A 1 126 ? 37.970  -8.604  -10.869 1.00 44.64  ? 126 PHE A O     1 
ATOM   1000 C  CB    . PHE A 1 126 ? 36.919  -5.438  -11.230 1.00 40.62  ? 126 PHE A CB    1 
ATOM   1001 C  CG    . PHE A 1 126 ? 35.800  -6.197  -11.880 1.00 46.83  ? 126 PHE A CG    1 
ATOM   1002 C  CD1   . PHE A 1 126 ? 34.578  -6.333  -11.242 1.00 41.61  ? 126 PHE A CD1   1 
ATOM   1003 C  CD2   . PHE A 1 126 ? 35.962  -6.760  -13.135 1.00 46.43  ? 126 PHE A CD2   1 
ATOM   1004 C  CE1   . PHE A 1 126 ? 33.540  -7.024  -11.839 1.00 41.94  ? 126 PHE A CE1   1 
ATOM   1005 C  CE2   . PHE A 1 126 ? 34.928  -7.452  -13.736 1.00 47.24  ? 126 PHE A CE2   1 
ATOM   1006 C  CZ    . PHE A 1 126 ? 33.716  -7.583  -13.086 1.00 38.32  ? 126 PHE A CZ    1 
ATOM   1007 N  N     . ASN A 1 127 ? 39.431  -7.188  -11.833 1.00 46.65  ? 127 ASN A N     1 
ATOM   1008 C  CA    . ASN A 1 127 ? 40.039  -8.238  -12.642 1.00 49.12  ? 127 ASN A CA    1 
ATOM   1009 C  C     . ASN A 1 127 ? 40.817  -9.246  -11.806 1.00 48.41  ? 127 ASN A C     1 
ATOM   1010 O  O     . ASN A 1 127 ? 41.159  -10.320 -12.312 1.00 46.66  ? 127 ASN A O     1 
ATOM   1011 C  CB    . ASN A 1 127 ? 40.959  -7.626  -13.700 1.00 50.70  ? 127 ASN A CB    1 
ATOM   1012 C  CG    . ASN A 1 127 ? 40.193  -6.914  -14.800 1.00 54.88  ? 127 ASN A CG    1 
ATOM   1013 O  OD1   . ASN A 1 127 ? 39.060  -7.277  -15.119 1.00 57.22  ? 127 ASN A OD1   1 
ATOM   1014 N  ND2   . ASN A 1 127 ? 40.813  -5.898  -15.391 1.00 60.97  ? 127 ASN A ND2   1 
ATOM   1015 N  N     . ALA A 1 128 ? 41.106  -8.929  -10.550 1.00 48.04  ? 128 ALA A N     1 
ATOM   1016 C  CA    . ALA A 1 128 ? 41.816  -9.846  -9.672  1.00 48.54  ? 128 ALA A CA    1 
ATOM   1017 C  C     . ALA A 1 128 ? 40.883  -10.741 -8.866  1.00 48.20  ? 128 ALA A C     1 
ATOM   1018 O  O     . ALA A 1 128 ? 41.365  -11.617 -8.141  1.00 53.26  ? 128 ALA A O     1 
ATOM   1019 C  CB    . ALA A 1 128 ? 42.730  -9.064  -8.723  1.00 48.09  ? 128 ALA A CB    1 
ATOM   1020 N  N     . ARG A 1 129 ? 39.569  -10.555 -8.978  1.00 43.40  ? 129 ARG A N     1 
ATOM   1021 C  CA    . ARG A 1 129 ? 38.612  -11.286 -8.158  1.00 40.82  ? 129 ARG A CA    1 
ATOM   1022 C  C     . ARG A 1 129 ? 37.621  -12.102 -8.973  1.00 43.90  ? 129 ARG A C     1 
ATOM   1023 O  O     . ARG A 1 129 ? 37.438  -13.296 -8.705  1.00 42.72  ? 129 ARG A O     1 
ATOM   1024 C  CB    . ARG A 1 129 ? 37.847  -10.307 -7.250  1.00 45.35  ? 129 ARG A CB    1 
ATOM   1025 C  CG    . ARG A 1 129 ? 38.669  -9.719  -6.115  1.00 38.47  ? 129 ARG A CG    1 
ATOM   1026 C  CD    . ARG A 1 129 ? 38.015  -8.460  -5.560  1.00 37.51  ? 129 ARG A CD    1 
ATOM   1027 N  NE    . ARG A 1 129 ? 38.621  -8.030  -4.305  1.00 39.72  ? 129 ARG A NE    1 
ATOM   1028 C  CZ    . ARG A 1 129 ? 39.741  -7.324  -4.216  1.00 47.24  ? 129 ARG A CZ    1 
ATOM   1029 N  NH1   . ARG A 1 129 ? 40.410  -6.949  -5.295  1.00 41.92  ? 129 ARG A NH1   1 
ATOM   1030 N  NH2   . ARG A 1 129 ? 40.203  -6.988  -3.014  1.00 41.38  ? 129 ARG A NH2   1 
ATOM   1031 N  N     . PHE A 1 130 ? 36.980  -11.499 -9.966  1.00 41.72  ? 130 PHE A N     1 
ATOM   1032 C  CA    . PHE A 1 130 ? 35.792  -12.093 -10.570 1.00 40.10  ? 130 PHE A CA    1 
ATOM   1033 C  C     . PHE A 1 130 ? 36.036  -13.109 -11.685 1.00 43.92  ? 130 PHE A C     1 
ATOM   1034 O  O     . PHE A 1 130 ? 35.223  -14.031 -11.829 1.00 44.37  ? 130 PHE A O     1 
ATOM   1035 C  CB    . PHE A 1 130 ? 34.875  -10.979 -11.077 1.00 41.20  ? 130 PHE A CB    1 
ATOM   1036 C  CG    . PHE A 1 130 ? 34.031  -10.377 -9.996  1.00 41.75  ? 130 PHE A CG    1 
ATOM   1037 C  CD1   . PHE A 1 130 ? 32.805  -10.935 -9.670  1.00 35.61  ? 130 PHE A CD1   1 
ATOM   1038 C  CD2   . PHE A 1 130 ? 34.476  -9.278  -9.281  1.00 39.31  ? 130 PHE A CD2   1 
ATOM   1039 C  CE1   . PHE A 1 130 ? 32.029  -10.396 -8.662  1.00 37.82  ? 130 PHE A CE1   1 
ATOM   1040 C  CE2   . PHE A 1 130 ? 33.706  -8.737  -8.272  1.00 35.81  ? 130 PHE A CE2   1 
ATOM   1041 C  CZ    . PHE A 1 130 ? 32.480  -9.297  -7.963  1.00 32.90  ? 130 PHE A CZ    1 
ATOM   1042 N  N     . PRO A 1 131 ? 37.102  -12.989 -12.517 1.00 48.15  ? 131 PRO A N     1 
ATOM   1043 C  CA    . PRO A 1 131 ? 37.338  -14.029 -13.532 1.00 46.10  ? 131 PRO A CA    1 
ATOM   1044 C  C     . PRO A 1 131 ? 37.324  -15.443 -12.968 1.00 44.21  ? 131 PRO A C     1 
ATOM   1045 O  O     . PRO A 1 131 ? 38.160  -15.801 -12.132 1.00 43.78  ? 131 PRO A O     1 
ATOM   1046 C  CB    . PRO A 1 131 ? 38.717  -13.660 -14.088 1.00 43.87  ? 131 PRO A CB    1 
ATOM   1047 C  CG    . PRO A 1 131 ? 38.752  -12.187 -13.982 1.00 48.54  ? 131 PRO A CG    1 
ATOM   1048 C  CD    . PRO A 1 131 ? 38.005  -11.838 -12.718 1.00 43.65  ? 131 PRO A CD    1 
ATOM   1049 N  N     . GLY A 1 132 ? 36.357  -16.246 -13.411 1.00 44.73  ? 132 GLY A N     1 
ATOM   1050 C  CA    . GLY A 1 132 ? 36.240  -17.626 -12.984 1.00 43.34  ? 132 GLY A CA    1 
ATOM   1051 C  C     . GLY A 1 132 ? 35.773  -17.835 -11.562 1.00 41.69  ? 132 GLY A C     1 
ATOM   1052 O  O     . GLY A 1 132 ? 35.898  -18.949 -11.045 1.00 46.70  ? 132 GLY A O     1 
ATOM   1053 N  N     . CYS A 1 133 ? 35.222  -16.807 -10.912 1.00 41.09  ? 133 CYS A N     1 
ATOM   1054 C  CA    . CYS A 1 133 ? 34.896  -16.903 -9.494  1.00 39.35  ? 133 CYS A CA    1 
ATOM   1055 C  C     . CYS A 1 133 ? 33.690  -17.790 -9.207  1.00 35.90  ? 133 CYS A C     1 
ATOM   1056 O  O     . CYS A 1 133 ? 33.484  -18.156 -8.045  1.00 40.62  ? 133 CYS A O     1 
ATOM   1057 C  CB    . CYS A 1 133 ? 34.654  -15.507 -8.912  1.00 38.33  ? 133 CYS A CB    1 
ATOM   1058 S  SG    . CYS A 1 133 ? 33.152  -14.691 -9.499  1.00 36.11  ? 133 CYS A SG    1 
ATOM   1059 N  N     . MET A 1 134 ? 32.896  -18.148 -10.217 1.00 37.35  ? 134 MET A N     1 
ATOM   1060 C  CA    . MET A 1 134 ? 31.702  -18.961 -10.015 1.00 36.77  ? 134 MET A CA    1 
ATOM   1061 C  C     . MET A 1 134 ? 31.848  -20.375 -10.570 1.00 39.18  ? 134 MET A C     1 
ATOM   1062 O  O     . MET A 1 134 ? 30.839  -21.059 -10.769 1.00 40.72  ? 134 MET A O     1 
ATOM   1063 C  CB    . MET A 1 134 ? 30.484  -18.284 -10.644 1.00 37.19  ? 134 MET A CB    1 
ATOM   1064 C  CG    . MET A 1 134 ? 30.003  -17.032 -9.932  1.00 31.20  ? 134 MET A CG    1 
ATOM   1065 S  SD    . MET A 1 134 ? 28.457  -16.445 -10.655 1.00 34.35  ? 134 MET A SD    1 
ATOM   1066 C  CE    . MET A 1 134 ? 28.172  -14.956 -9.703  1.00 33.13  ? 134 MET A CE    1 
ATOM   1067 N  N     . LYS A 1 135 ? 33.076  -20.826 -10.829 1.00 40.88  ? 135 LYS A N     1 
ATOM   1068 C  CA    . LYS A 1 135 ? 33.278  -22.149 -11.407 1.00 43.21  ? 135 LYS A CA    1 
ATOM   1069 C  C     . LYS A 1 135 ? 32.662  -23.225 -10.521 1.00 44.01  ? 135 LYS A C     1 
ATOM   1070 O  O     . LYS A 1 135 ? 32.824  -23.209 -9.298  1.00 42.07  ? 135 LYS A O     1 
ATOM   1071 C  CB    . LYS A 1 135 ? 34.770  -22.417 -11.615 1.00 49.85  ? 135 LYS A CB    1 
ATOM   1072 C  CG    . LYS A 1 135 ? 35.360  -21.684 -12.812 1.00 56.79  ? 135 LYS A CG    1 
ATOM   1073 C  CD    . LYS A 1 135 ? 36.867  -21.867 -12.909 1.00 60.68  ? 135 LYS A CD    1 
ATOM   1074 C  CE    . LYS A 1 135 ? 37.442  -21.019 -14.035 1.00 60.13  ? 135 LYS A CE    1 
ATOM   1075 N  NZ    . LYS A 1 135 ? 38.929  -21.073 -14.088 1.00 68.67  ? 135 LYS A NZ    1 
ATOM   1076 N  N     . GLY A 1 136 ? 31.928  -24.145 -11.147 1.00 47.09  ? 136 GLY A N     1 
ATOM   1077 C  CA    . GLY A 1 136 ? 31.253  -25.214 -10.443 1.00 39.68  ? 136 GLY A CA    1 
ATOM   1078 C  C     . GLY A 1 136 ? 29.980  -24.822 -9.724  1.00 37.86  ? 136 GLY A C     1 
ATOM   1079 O  O     . GLY A 1 136 ? 29.330  -25.696 -9.137  1.00 43.68  ? 136 GLY A O     1 
ATOM   1080 N  N     . ARG A 1 137 ? 29.593  -23.552 -9.753  1.00 34.38  ? 137 ARG A N     1 
ATOM   1081 C  CA    . ARG A 1 137 ? 28.443  -23.072 -9.002  1.00 34.92  ? 137 ARG A CA    1 
ATOM   1082 C  C     . ARG A 1 137 ? 27.320  -22.644 -9.939  1.00 34.77  ? 137 ARG A C     1 
ATOM   1083 O  O     . ARG A 1 137 ? 27.488  -22.528 -11.155 1.00 34.68  ? 137 ARG A O     1 
ATOM   1084 C  CB    . ARG A 1 137 ? 28.836  -21.906 -8.087  1.00 35.56  ? 137 ARG A CB    1 
ATOM   1085 C  CG    . ARG A 1 137 ? 29.868  -22.269 -7.031  1.00 41.48  ? 137 ARG A CG    1 
ATOM   1086 C  CD    . ARG A 1 137 ? 29.988  -21.180 -5.977  1.00 39.52  ? 137 ARG A CD    1 
ATOM   1087 N  NE    . ARG A 1 137 ? 30.995  -21.506 -4.972  1.00 46.04  ? 137 ARG A NE    1 
ATOM   1088 C  CZ    . ARG A 1 137 ? 30.750  -22.186 -3.860  1.00 40.70  ? 137 ARG A CZ    1 
ATOM   1089 N  NH1   . ARG A 1 137 ? 29.538  -22.635 -3.577  1.00 42.52  ? 137 ARG A NH1   1 
ATOM   1090 N  NH2   . ARG A 1 137 ? 31.746  -22.420 -3.011  1.00 46.78  ? 137 ARG A NH2   1 
ATOM   1091 N  N     . THR A 1 138 ? 26.160  -22.409 -9.337  1.00 33.37  ? 138 THR A N     1 
ATOM   1092 C  CA    . THR A 1 138 ? 24.998  -21.884 -10.036 1.00 33.13  ? 138 THR A CA    1 
ATOM   1093 C  C     . THR A 1 138 ? 24.970  -20.369 -9.902  1.00 33.28  ? 138 THR A C     1 
ATOM   1094 O  O     . THR A 1 138 ? 25.212  -19.828 -8.820  1.00 35.08  ? 138 THR A O     1 
ATOM   1095 C  CB    . THR A 1 138 ? 23.710  -22.475 -9.455  1.00 32.85  ? 138 THR A CB    1 
ATOM   1096 O  OG1   . THR A 1 138 ? 23.756  -23.903 -9.543  1.00 36.30  ? 138 THR A OG1   1 
ATOM   1097 C  CG2   . THR A 1 138 ? 22.480  -21.966 -10.202 1.00 30.39  ? 138 THR A CG2   1 
ATOM   1098 N  N     A MET A 1 139 ? 24.704  -19.690 -11.016 0.50 31.59  ? 139 MET A N     1 
ATOM   1099 N  N     B MET A 1 139 ? 24.670  -19.682 -11.002 0.50 31.45  ? 139 MET A N     1 
ATOM   1100 C  CA    A MET A 1 139 ? 24.437  -18.259 -11.018 0.50 30.20  ? 139 MET A CA    1 
ATOM   1101 C  CA    B MET A 1 139 ? 24.467  -18.237 -10.978 0.50 30.20  ? 139 MET A CA    1 
ATOM   1102 C  C     A MET A 1 139 ? 22.931  -18.051 -10.978 0.50 30.83  ? 139 MET A C     1 
ATOM   1103 C  C     B MET A 1 139 ? 22.968  -17.967 -11.005 0.50 30.84  ? 139 MET A C     1 
ATOM   1104 O  O     A MET A 1 139 ? 22.225  -18.427 -11.922 0.50 30.18  ? 139 MET A O     1 
ATOM   1105 O  O     B MET A 1 139 ? 22.302  -18.217 -12.016 0.50 30.22  ? 139 MET A O     1 
ATOM   1106 C  CB    A MET A 1 139 ? 25.030  -17.572 -12.248 0.50 30.63  ? 139 MET A CB    1 
ATOM   1107 C  CB    B MET A 1 139 ? 25.170  -17.547 -12.145 0.50 30.63  ? 139 MET A CB    1 
ATOM   1108 C  CG    A MET A 1 139 ? 24.528  -16.139 -12.428 0.50 31.66  ? 139 MET A CG    1 
ATOM   1109 C  CG    B MET A 1 139 ? 25.190  -16.027 -12.013 0.50 31.32  ? 139 MET A CG    1 
ATOM   1110 S  SD    A MET A 1 139 ? 24.940  -15.382 -14.013 0.50 28.38  ? 139 MET A SD    1 
ATOM   1111 S  SD    B MET A 1 139 ? 26.131  -15.182 -13.299 0.50 37.92  ? 139 MET A SD    1 
ATOM   1112 C  CE    A MET A 1 139 ? 26.708  -15.161 -13.840 0.50 34.36  ? 139 MET A CE    1 
ATOM   1113 C  CE    B MET A 1 139 ? 25.054  -15.411 -14.710 0.50 30.22  ? 139 MET A CE    1 
ATOM   1114 N  N     . TYR A 1 140 ? 22.441  -17.464 -9.892  1.00 31.53  ? 140 TYR A N     1 
ATOM   1115 C  CA    . TYR A 1 140 ? 21.030  -17.131 -9.778  1.00 29.36  ? 140 TYR A CA    1 
ATOM   1116 C  C     . TYR A 1 140 ? 20.800  -15.719 -10.293 1.00 31.97  ? 140 TYR A C     1 
ATOM   1117 O  O     . TYR A 1 140 ? 21.600  -14.815 -10.039 1.00 26.84  ? 140 TYR A O     1 
ATOM   1118 C  CB    . TYR A 1 140 ? 20.557  -17.246 -8.327  1.00 30.97  ? 140 TYR A CB    1 
ATOM   1119 C  CG    . TYR A 1 140 ? 20.647  -18.646 -7.768  1.00 27.68  ? 140 TYR A CG    1 
ATOM   1120 C  CD1   . TYR A 1 140 ? 19.588  -19.533 -7.896  1.00 31.16  ? 140 TYR A CD1   1 
ATOM   1121 C  CD2   . TYR A 1 140 ? 21.790  -19.083 -7.115  1.00 29.18  ? 140 TYR A CD2   1 
ATOM   1122 C  CE1   . TYR A 1 140 ? 19.665  -20.814 -7.391  1.00 34.29  ? 140 TYR A CE1   1 
ATOM   1123 C  CE2   . TYR A 1 140 ? 21.875  -20.364 -6.603  1.00 31.51  ? 140 TYR A CE2   1 
ATOM   1124 C  CZ    . TYR A 1 140 ? 20.810  -21.225 -6.744  1.00 31.65  ? 140 TYR A CZ    1 
ATOM   1125 O  OH    . TYR A 1 140 ? 20.888  -22.504 -6.240  1.00 39.75  ? 140 TYR A OH    1 
ATOM   1126 N  N     . VAL A 1 141 ? 19.708  -15.541 -11.030 1.00 24.83  ? 141 VAL A N     1 
ATOM   1127 C  CA    . VAL A 1 141 ? 19.341  -14.253 -11.602 1.00 26.45  ? 141 VAL A CA    1 
ATOM   1128 C  C     . VAL A 1 141 ? 18.087  -13.782 -10.881 1.00 28.36  ? 141 VAL A C     1 
ATOM   1129 O  O     . VAL A 1 141 ? 16.992  -14.315 -11.105 1.00 28.34  ? 141 VAL A O     1 
ATOM   1130 C  CB    . VAL A 1 141 ? 19.121  -14.342 -13.118 1.00 31.39  ? 141 VAL A CB    1 
ATOM   1131 C  CG1   . VAL A 1 141 ? 18.858  -12.959 -13.697 1.00 26.89  ? 141 VAL A CG1   1 
ATOM   1132 C  CG2   . VAL A 1 141 ? 20.328  -14.988 -13.788 1.00 30.41  ? 141 VAL A CG2   1 
ATOM   1133 N  N     . ILE A 1 142 ? 18.246  -12.784 -10.018 1.00 28.82  ? 142 ILE A N     1 
ATOM   1134 C  CA    . ILE A 1 142 ? 17.174  -12.298 -9.153  1.00 24.90  ? 142 ILE A CA    1 
ATOM   1135 C  C     . ILE A 1 142 ? 16.598  -11.002 -9.707  1.00 25.73  ? 142 ILE A C     1 
ATOM   1136 O  O     . ILE A 1 142 ? 17.228  -9.944  -9.567  1.00 26.18  ? 142 ILE A O     1 
ATOM   1137 C  CB    . ILE A 1 142 ? 17.680  -12.068 -7.721  1.00 21.75  ? 142 ILE A CB    1 
ATOM   1138 C  CG1   . ILE A 1 142 ? 18.467  -13.276 -7.219  1.00 21.78  ? 142 ILE A CG1   1 
ATOM   1139 C  CG2   . ILE A 1 142 ? 16.519  -11.753 -6.788  1.00 22.98  ? 142 ILE A CG2   1 
ATOM   1140 C  CD1   . ILE A 1 142 ? 19.167  -13.019 -5.886  1.00 24.95  ? 142 ILE A CD1   1 
ATOM   1141 N  N     . PRO A 1 143 ? 15.423  -11.019 -10.326 1.00 28.06  ? 143 PRO A N     1 
ATOM   1142 C  CA    . PRO A 1 143 ? 14.769  -9.752  -10.669 1.00 24.56  ? 143 PRO A CA    1 
ATOM   1143 C  C     . PRO A 1 143 ? 13.962  -9.239  -9.489  1.00 27.83  ? 143 PRO A C     1 
ATOM   1144 O  O     . PRO A 1 143 ? 13.057  -9.942  -9.036  1.00 31.56  ? 143 PRO A O     1 
ATOM   1145 C  CB    . PRO A 1 143 ? 13.865  -10.126 -11.852 1.00 31.63  ? 143 PRO A CB    1 
ATOM   1146 C  CG    . PRO A 1 143 ? 13.836  -11.668 -11.891 1.00 32.96  ? 143 PRO A CG    1 
ATOM   1147 C  CD    . PRO A 1 143 ? 14.596  -12.177 -10.698 1.00 27.90  ? 143 PRO A CD    1 
ATOM   1148 N  N     . PHE A 1 144 ? 14.260  -8.052  -8.963  1.00 29.36  ? 144 PHE A N     1 
ATOM   1149 C  CA    . PHE A 1 144 ? 13.585  -7.598  -7.754  1.00 28.87  ? 144 PHE A CA    1 
ATOM   1150 C  C     . PHE A 1 144 ? 13.179  -6.136  -7.874  1.00 26.57  ? 144 PHE A C     1 
ATOM   1151 O  O     . PHE A 1 144 ? 13.778  -5.362  -8.624  1.00 28.86  ? 144 PHE A O     1 
ATOM   1152 C  CB    . PHE A 1 144 ? 14.461  -7.804  -6.507  1.00 29.27  ? 144 PHE A CB    1 
ATOM   1153 C  CG    . PHE A 1 144 ? 15.697  -6.953  -6.488  1.00 27.76  ? 144 PHE A CG    1 
ATOM   1154 C  CD1   . PHE A 1 144 ? 16.869  -7.402  -7.075  1.00 27.05  ? 144 PHE A CD1   1 
ATOM   1155 C  CD2   . PHE A 1 144 ? 15.687  -5.704  -5.882  1.00 27.22  ? 144 PHE A CD2   1 
ATOM   1156 C  CE1   . PHE A 1 144 ? 18.010  -6.622  -7.060  1.00 30.13  ? 144 PHE A CE1   1 
ATOM   1157 C  CE2   . PHE A 1 144 ? 16.828  -4.917  -5.861  1.00 29.62  ? 144 PHE A CE2   1 
ATOM   1158 C  CZ    . PHE A 1 144 ? 17.989  -5.376  -6.451  1.00 29.74  ? 144 PHE A CZ    1 
ATOM   1159 N  N     . SER A 1 145 ? 12.153  -5.768  -7.113  1.00 25.83  ? 145 SER A N     1 
ATOM   1160 C  CA    . SER A 1 145 ? 11.673  -4.400  -7.042  1.00 30.58  ? 145 SER A CA    1 
ATOM   1161 C  C     . SER A 1 145 ? 11.868  -3.853  -5.633  1.00 33.54  ? 145 SER A C     1 
ATOM   1162 O  O     . SER A 1 145 ? 11.634  -4.555  -4.644  1.00 32.61  ? 145 SER A O     1 
ATOM   1163 C  CB    . SER A 1 145 ? 10.191  -4.320  -7.438  1.00 29.26  ? 145 SER A CB    1 
ATOM   1164 O  OG    . SER A 1 145 ? 9.700   -2.994  -7.330  1.00 45.79  ? 145 SER A OG    1 
ATOM   1165 N  N     . MET A 1 146 ? 12.323  -2.606  -5.547  1.00 31.04  ? 146 MET A N     1 
ATOM   1166 C  CA    . MET A 1 146 ? 12.331  -1.859  -4.294  1.00 34.16  ? 146 MET A CA    1 
ATOM   1167 C  C     . MET A 1 146 ? 11.124  -0.932  -4.324  1.00 38.12  ? 146 MET A C     1 
ATOM   1168 O  O     . MET A 1 146 ? 11.056  -0.017  -5.151  1.00 40.98  ? 146 MET A O     1 
ATOM   1169 C  CB    . MET A 1 146 ? 13.630  -1.077  -4.117  1.00 31.08  ? 146 MET A CB    1 
ATOM   1170 C  CG    . MET A 1 146 ? 14.885  -1.935  -4.158  1.00 33.68  ? 146 MET A CG    1 
ATOM   1171 S  SD    . MET A 1 146 ? 14.860  -3.304  -2.985  1.00 34.76  ? 146 MET A SD    1 
ATOM   1172 C  CE    . MET A 1 146 ? 14.848  -2.434  -1.421  1.00 32.92  ? 146 MET A CE    1 
ATOM   1173 N  N     . GLY A 1 147 ? 10.166  -1.178  -3.436  1.00 40.77  ? 147 GLY A N     1 
ATOM   1174 C  CA    . GLY A 1 147 ? 8.915   -0.462  -3.458  1.00 42.41  ? 147 GLY A CA    1 
ATOM   1175 C  C     . GLY A 1 147 ? 7.834   -1.278  -4.136  1.00 49.81  ? 147 GLY A C     1 
ATOM   1176 O  O     . GLY A 1 147 ? 8.110   -2.287  -4.794  1.00 41.35  ? 147 GLY A O     1 
ATOM   1177 N  N     . PRO A 1 148 ? 6.578   -0.856  -3.984  1.00 51.15  ? 148 PRO A N     1 
ATOM   1178 C  CA    . PRO A 1 148 ? 5.462   -1.633  -4.539  1.00 57.02  ? 148 PRO A CA    1 
ATOM   1179 C  C     . PRO A 1 148 ? 5.621   -1.879  -6.034  1.00 61.66  ? 148 PRO A C     1 
ATOM   1180 O  O     . PRO A 1 148 ? 5.994   -0.986  -6.797  1.00 65.11  ? 148 PRO A O     1 
ATOM   1181 C  CB    . PRO A 1 148 ? 4.240   -0.757  -4.240  1.00 56.75  ? 148 PRO A CB    1 
ATOM   1182 C  CG    . PRO A 1 148 ? 4.639   0.032   -3.038  1.00 58.74  ? 148 PRO A CG    1 
ATOM   1183 C  CD    . PRO A 1 148 ? 6.111   0.303   -3.203  1.00 58.75  ? 148 PRO A CD    1 
ATOM   1184 N  N     . LEU A 1 149 ? 5.337   -3.113  -6.441  1.00 61.82  ? 149 LEU A N     1 
ATOM   1185 C  CA    . LEU A 1 149 ? 5.491   -3.499  -7.836  1.00 66.96  ? 149 LEU A CA    1 
ATOM   1186 C  C     . LEU A 1 149 ? 4.521   -2.724  -8.719  1.00 81.85  ? 149 LEU A C     1 
ATOM   1187 O  O     . LEU A 1 149 ? 3.359   -2.511  -8.362  1.00 77.59  ? 149 LEU A O     1 
ATOM   1188 C  CB    . LEU A 1 149 ? 5.261   -5.001  -7.993  1.00 73.19  ? 149 LEU A CB    1 
ATOM   1189 C  CG    . LEU A 1 149 ? 5.395   -5.562  -9.407  1.00 63.20  ? 149 LEU A CG    1 
ATOM   1190 C  CD1   . LEU A 1 149 ? 6.797   -5.326  -9.945  1.00 69.57  ? 149 LEU A CD1   1 
ATOM   1191 C  CD2   . LEU A 1 149 ? 5.052   -7.037  -9.417  1.00 65.11  ? 149 LEU A CD2   1 
ATOM   1192 N  N     . GLY A 1 150 ? 5.010   -2.300  -9.884  1.00 84.84  ? 150 GLY A N     1 
ATOM   1193 C  CA    . GLY A 1 150 ? 4.230   -1.491  -10.792 1.00 84.87  ? 150 GLY A CA    1 
ATOM   1194 C  C     . GLY A 1 150 ? 4.096   -0.038  -10.398 1.00 93.79  ? 150 GLY A C     1 
ATOM   1195 O  O     . GLY A 1 150 ? 3.677   0.774   -11.234 1.00 98.80  ? 150 GLY A O     1 
ATOM   1196 N  N     . SER A 1 151 ? 4.429   0.318   -9.163  1.00 80.87  ? 151 SER A N     1 
ATOM   1197 C  CA    . SER A 1 151 ? 4.356   1.709   -8.750  1.00 80.04  ? 151 SER A CA    1 
ATOM   1198 C  C     . SER A 1 151 ? 5.377   2.532   -9.533  1.00 84.07  ? 151 SER A C     1 
ATOM   1199 O  O     . SER A 1 151 ? 6.468   2.037   -9.841  1.00 80.57  ? 151 SER A O     1 
ATOM   1200 C  CB    . SER A 1 151 ? 4.611   1.837   -7.247  1.00 74.36  ? 151 SER A CB    1 
ATOM   1201 O  OG    . SER A 1 151 ? 4.629   3.194   -6.844  1.00 77.76  ? 151 SER A OG    1 
ATOM   1202 N  N     . PRO A 1 152 ? 5.052   3.778   -9.888  1.00 84.77  ? 152 PRO A N     1 
ATOM   1203 C  CA    . PRO A 1 152 ? 6.013   4.587   -10.655 1.00 85.98  ? 152 PRO A CA    1 
ATOM   1204 C  C     . PRO A 1 152 ? 7.282   4.909   -9.888  1.00 79.55  ? 152 PRO A C     1 
ATOM   1205 O  O     . PRO A 1 152 ? 8.350   5.016   -10.503 1.00 84.58  ? 152 PRO A O     1 
ATOM   1206 C  CB    . PRO A 1 152 ? 5.216   5.857   -10.987 1.00 84.50  ? 152 PRO A CB    1 
ATOM   1207 C  CG    . PRO A 1 152 ? 3.779   5.454   -10.863 1.00 88.34  ? 152 PRO A CG    1 
ATOM   1208 C  CD    . PRO A 1 152 ? 3.746   4.444   -9.758  1.00 86.34  ? 152 PRO A CD    1 
ATOM   1209 N  N     . LEU A 1 153 ? 7.205   5.065   -8.566  1.00 74.13  ? 153 LEU A N     1 
ATOM   1210 C  CA    . LEU A 1 153 ? 8.384   5.391   -7.773  1.00 75.13  ? 153 LEU A CA    1 
ATOM   1211 C  C     . LEU A 1 153 ? 9.259   4.181   -7.476  1.00 72.74  ? 153 LEU A C     1 
ATOM   1212 O  O     . LEU A 1 153 ? 10.383  4.354   -6.990  1.00 61.94  ? 153 LEU A O     1 
ATOM   1213 C  CB    . LEU A 1 153 ? 7.963   6.060   -6.462  1.00 68.42  ? 153 LEU A CB    1 
ATOM   1214 C  CG    . LEU A 1 153 ? 6.846   5.414   -5.637  1.00 72.07  ? 153 LEU A CG    1 
ATOM   1215 C  CD1   . LEU A 1 153 ? 7.351   4.268   -4.765  1.00 71.04  ? 153 LEU A CD1   1 
ATOM   1216 C  CD2   . LEU A 1 153 ? 6.168   6.470   -4.788  1.00 67.05  ? 153 LEU A CD2   1 
ATOM   1217 N  N     . ALA A 1 154 ? 8.776   2.972   -7.745  1.00 64.94  ? 154 ALA A N     1 
ATOM   1218 C  CA    . ALA A 1 154 ? 9.567   1.781   -7.489  1.00 59.53  ? 154 ALA A CA    1 
ATOM   1219 C  C     . ALA A 1 154 ? 10.782  1.736   -8.407  1.00 57.09  ? 154 ALA A C     1 
ATOM   1220 O  O     . ALA A 1 154 ? 10.754  2.218   -9.542  1.00 56.69  ? 154 ALA A O     1 
ATOM   1221 C  CB    . ALA A 1 154 ? 8.722   0.523   -7.681  1.00 53.48  ? 154 ALA A CB    1 
ATOM   1222 N  N     . LYS A 1 155 ? 11.863  1.158   -7.894  1.00 43.79  ? 155 LYS A N     1 
ATOM   1223 C  CA    . LYS A 1 155 ? 13.082  0.947   -8.656  1.00 40.32  ? 155 LYS A CA    1 
ATOM   1224 C  C     . LYS A 1 155 ? 13.356  -0.548  -8.744  1.00 36.04  ? 155 LYS A C     1 
ATOM   1225 O  O     . LYS A 1 155 ? 13.161  -1.284  -7.772  1.00 37.43  ? 155 LYS A O     1 
ATOM   1226 C  CB    . LYS A 1 155 ? 14.264  1.676   -8.016  1.00 41.22  ? 155 LYS A CB    1 
ATOM   1227 C  CG    . LYS A 1 155 ? 14.191  3.195   -8.080  1.00 48.29  ? 155 LYS A CG    1 
ATOM   1228 C  CD    . LYS A 1 155 ? 14.413  3.703   -9.497  1.00 51.15  ? 155 LYS A CD    1 
ATOM   1229 C  CE    . LYS A 1 155 ? 14.419  5.224   -9.549  1.00 59.37  ? 155 LYS A CE    1 
ATOM   1230 N  NZ    . LYS A 1 155 ? 13.101  5.808   -9.174  1.00 61.75  ? 155 LYS A NZ    1 
ATOM   1231 N  N     . ILE A 1 156 ? 13.800  -0.993  -9.915  1.00 34.20  ? 156 ILE A N     1 
ATOM   1232 C  CA    . ILE A 1 156 ? 13.966  -2.410  -10.214 1.00 34.39  ? 156 ILE A CA    1 
ATOM   1233 C  C     . ILE A 1 156 ? 15.443  -2.698  -10.433 1.00 37.17  ? 156 ILE A C     1 
ATOM   1234 O  O     . ILE A 1 156 ? 16.158  -1.901  -11.052 1.00 37.75  ? 156 ILE A O     1 
ATOM   1235 C  CB    . ILE A 1 156 ? 13.127  -2.817  -11.443 1.00 35.15  ? 156 ILE A CB    1 
ATOM   1236 C  CG1   . ILE A 1 156 ? 11.641  -2.849  -11.079 1.00 36.45  ? 156 ILE A CG1   1 
ATOM   1237 C  CG2   . ILE A 1 156 ? 13.581  -4.161  -12.004 1.00 29.54  ? 156 ILE A CG2   1 
ATOM   1238 C  CD1   . ILE A 1 156 ? 10.721  -3.068  -12.263 1.00 39.69  ? 156 ILE A CD1   1 
ATOM   1239 N  N     . GLY A 1 157 ? 15.904  -3.836  -9.911  1.00 33.41  ? 157 GLY A N     1 
ATOM   1240 C  CA    . GLY A 1 157 ? 17.265  -4.266  -10.123 1.00 34.50  ? 157 GLY A CA    1 
ATOM   1241 C  C     . GLY A 1 157 ? 17.324  -5.736  -10.493 1.00 27.82  ? 157 GLY A C     1 
ATOM   1242 O  O     . GLY A 1 157 ? 16.369  -6.491  -10.307 1.00 24.86  ? 157 GLY A O     1 
ATOM   1243 N  N     . ILE A 1 158 ? 18.472  -6.123  -11.041 1.00 30.94  ? 158 ILE A N     1 
ATOM   1244 C  CA    . ILE A 1 158 ? 18.815  -7.516  -11.298 1.00 30.34  ? 158 ILE A CA    1 
ATOM   1245 C  C     . ILE A 1 158 ? 20.072  -7.825  -10.497 1.00 27.60  ? 158 ILE A C     1 
ATOM   1246 O  O     . ILE A 1 158 ? 21.112  -7.191  -10.708 1.00 28.43  ? 158 ILE A O     1 
ATOM   1247 C  CB    . ILE A 1 158 ? 19.056  -7.786  -12.793 1.00 25.31  ? 158 ILE A CB    1 
ATOM   1248 C  CG1   . ILE A 1 158 ? 17.854  -7.346  -13.638 1.00 31.61  ? 158 ILE A CG1   1 
ATOM   1249 C  CG2   . ILE A 1 158 ? 19.366  -9.259  -13.022 1.00 25.02  ? 158 ILE A CG2   1 
ATOM   1250 C  CD1   . ILE A 1 158 ? 16.696  -8.306  -13.596 1.00 33.33  ? 158 ILE A CD1   1 
ATOM   1251 N  N     . GLU A 1 159 ? 19.984  -8.786  -9.579  1.00 26.51  ? 159 GLU A N     1 
ATOM   1252 C  CA    . GLU A 1 159 ? 21.161  -9.246  -8.848  1.00 21.51  ? 159 GLU A CA    1 
ATOM   1253 C  C     . GLU A 1 159 ? 21.557  -10.632 -9.338  1.00 24.90  ? 159 GLU A C     1 
ATOM   1254 O  O     . GLU A 1 159 ? 20.745  -11.564 -9.314  1.00 29.52  ? 159 GLU A O     1 
ATOM   1255 C  CB    . GLU A 1 159 ? 20.940  -9.271  -7.336  1.00 23.69  ? 159 GLU A CB    1 
ATOM   1256 C  CG    . GLU A 1 159 ? 22.093  -9.987  -6.623  1.00 22.19  ? 159 GLU A CG    1 
ATOM   1257 C  CD    . GLU A 1 159 ? 22.212  -9.657  -5.148  1.00 26.90  ? 159 GLU A CD    1 
ATOM   1258 O  OE1   . GLU A 1 159 ? 21.424  -8.832  -4.647  1.00 26.95  ? 159 GLU A OE1   1 
ATOM   1259 O  OE2   . GLU A 1 159 ? 23.110  -10.225 -4.490  1.00 23.05  ? 159 GLU A OE2   1 
ATOM   1260 N  N     . LEU A 1 160 ? 22.803  -10.759 -9.781  1.00 27.75  ? 160 LEU A N     1 
ATOM   1261 C  CA    . LEU A 1 160 ? 23.414  -12.047 -10.064 1.00 27.59  ? 160 LEU A CA    1 
ATOM   1262 C  C     . LEU A 1 160 ? 24.234  -12.470 -8.851  1.00 29.35  ? 160 LEU A C     1 
ATOM   1263 O  O     . LEU A 1 160 ? 25.057  -11.695 -8.353  1.00 29.85  ? 160 LEU A O     1 
ATOM   1264 C  CB    . LEU A 1 160 ? 24.302  -11.969 -11.308 1.00 24.73  ? 160 LEU A CB    1 
ATOM   1265 C  CG    . LEU A 1 160 ? 23.721  -11.252 -12.528 1.00 31.81  ? 160 LEU A CG    1 
ATOM   1266 C  CD1   . LEU A 1 160 ? 24.765  -11.144 -13.637 1.00 31.13  ? 160 LEU A CD1   1 
ATOM   1267 C  CD2   . LEU A 1 160 ? 22.468  -11.952 -13.035 1.00 28.80  ? 160 LEU A CD2   1 
ATOM   1268 N  N     . THR A 1 161 ? 24.004  -13.692 -8.376  1.00 27.02  ? 161 THR A N     1 
ATOM   1269 C  CA    . THR A 1 161 ? 24.715  -14.199 -7.212  1.00 26.87  ? 161 THR A CA    1 
ATOM   1270 C  C     . THR A 1 161 ? 24.896  -15.703 -7.362  1.00 28.22  ? 161 THR A C     1 
ATOM   1271 O  O     . THR A 1 161 ? 24.152  -16.368 -8.088  1.00 28.28  ? 161 THR A O     1 
ATOM   1272 C  CB    . THR A 1 161 ? 23.971  -13.872 -5.907  1.00 25.50  ? 161 THR A CB    1 
ATOM   1273 O  OG1   . THR A 1 161 ? 24.728  -14.341 -4.784  1.00 24.13  ? 161 THR A OG1   1 
ATOM   1274 C  CG2   . THR A 1 161 ? 22.604  -14.533 -5.888  1.00 21.31  ? 161 THR A CG2   1 
ATOM   1275 N  N     . ASP A 1 162 ? 25.903  -16.235 -6.669  1.00 22.70  ? 162 ASP A N     1 
ATOM   1276 C  CA    . ASP A 1 162 ? 26.121  -17.674 -6.626  1.00 23.41  ? 162 ASP A CA    1 
ATOM   1277 C  C     . ASP A 1 162 ? 25.713  -18.290 -5.293  1.00 23.11  ? 162 ASP A C     1 
ATOM   1278 O  O     . ASP A 1 162 ? 26.048  -19.448 -5.030  1.00 30.06  ? 162 ASP A O     1 
ATOM   1279 C  CB    . ASP A 1 162 ? 27.582  -18.006 -6.943  1.00 32.14  ? 162 ASP A CB    1 
ATOM   1280 C  CG    . ASP A 1 162 ? 28.567  -17.244 -6.070  1.00 31.91  ? 162 ASP A CG    1 
ATOM   1281 O  OD1   . ASP A 1 162 ? 28.133  -16.537 -5.136  1.00 24.71  ? 162 ASP A OD1   1 
ATOM   1282 O  OD2   . ASP A 1 162 ? 29.783  -17.349 -6.331  1.00 35.33  ? 162 ASP A OD2   1 
ATOM   1283 N  N     . SER A 1 163 ? 24.977  -17.555 -4.461  1.00 23.39  ? 163 SER A N     1 
ATOM   1284 C  CA    . SER A 1 163 ? 24.605  -18.016 -3.131  1.00 26.10  ? 163 SER A CA    1 
ATOM   1285 C  C     . SER A 1 163 ? 23.104  -18.242 -3.050  1.00 26.99  ? 163 SER A C     1 
ATOM   1286 O  O     . SER A 1 163 ? 22.329  -17.296 -3.257  1.00 26.91  ? 163 SER A O     1 
ATOM   1287 C  CB    . SER A 1 163 ? 25.043  -17.002 -2.078  1.00 29.21  ? 163 SER A CB    1 
ATOM   1288 O  OG    . SER A 1 163 ? 24.479  -17.309 -0.816  1.00 30.42  ? 163 SER A OG    1 
ATOM   1289 N  N     . PRO A 1 164 ? 22.646  -19.464 -2.764  1.00 29.00  ? 164 PRO A N     1 
ATOM   1290 C  CA    . PRO A 1 164 ? 21.207  -19.655 -2.530  1.00 29.28  ? 164 PRO A CA    1 
ATOM   1291 C  C     . PRO A 1 164 ? 20.723  -18.974 -1.263  1.00 27.67  ? 164 PRO A C     1 
ATOM   1292 O  O     . PRO A 1 164 ? 19.544  -18.609 -1.186  1.00 24.73  ? 164 PRO A O     1 
ATOM   1293 C  CB    . PRO A 1 164 ? 21.060  -21.181 -2.451  1.00 30.09  ? 164 PRO A CB    1 
ATOM   1294 C  CG    . PRO A 1 164 ? 22.415  -21.673 -2.069  1.00 35.80  ? 164 PRO A CG    1 
ATOM   1295 C  CD    . PRO A 1 164 ? 23.399  -20.726 -2.690  1.00 30.01  ? 164 PRO A CD    1 
ATOM   1296 N  N     . TYR A 1 165 ? 21.600  -18.787 -0.271  1.00 21.65  ? 165 TYR A N     1 
ATOM   1297 C  CA    . TYR A 1 165 ? 21.234  -18.022 0.916   1.00 23.11  ? 165 TYR A CA    1 
ATOM   1298 C  C     . TYR A 1 165 ? 20.850  -16.591 0.563   1.00 27.45  ? 165 TYR A C     1 
ATOM   1299 O  O     . TYR A 1 165 ? 19.969  -16.006 1.205   1.00 28.55  ? 165 TYR A O     1 
ATOM   1300 C  CB    . TYR A 1 165 ? 22.394  -18.037 1.919   1.00 26.46  ? 165 TYR A CB    1 
ATOM   1301 C  CG    . TYR A 1 165 ? 22.205  -17.119 3.108   1.00 25.35  ? 165 TYR A CG    1 
ATOM   1302 C  CD1   . TYR A 1 165 ? 21.568  -17.565 4.262   1.00 25.78  ? 165 TYR A CD1   1 
ATOM   1303 C  CD2   . TYR A 1 165 ? 22.671  -15.809 3.082   1.00 26.19  ? 165 TYR A CD2   1 
ATOM   1304 C  CE1   . TYR A 1 165 ? 21.394  -16.729 5.354   1.00 23.97  ? 165 TYR A CE1   1 
ATOM   1305 C  CE2   . TYR A 1 165 ? 22.504  -14.967 4.168   1.00 26.86  ? 165 TYR A CE2   1 
ATOM   1306 C  CZ    . TYR A 1 165 ? 21.866  -15.431 5.299   1.00 30.38  ? 165 TYR A CZ    1 
ATOM   1307 O  OH    . TYR A 1 165 ? 21.699  -14.592 6.375   1.00 28.37  ? 165 TYR A OH    1 
ATOM   1308 N  N     . VAL A 1 166 ? 21.502  -16.008 -0.444  1.00 22.79  ? 166 VAL A N     1 
ATOM   1309 C  CA    . VAL A 1 166 ? 21.159  -14.656 -0.869  1.00 19.80  ? 166 VAL A CA    1 
ATOM   1310 C  C     . VAL A 1 166 ? 19.808  -14.649 -1.571  1.00 24.83  ? 166 VAL A C     1 
ATOM   1311 O  O     . VAL A 1 166 ? 18.987  -13.749 -1.360  1.00 24.95  ? 166 VAL A O     1 
ATOM   1312 C  CB    . VAL A 1 166 ? 22.274  -14.085 -1.768  1.00 23.88  ? 166 VAL A CB    1 
ATOM   1313 C  CG1   . VAL A 1 166 ? 21.802  -12.832 -2.497  1.00 22.71  ? 166 VAL A CG1   1 
ATOM   1314 C  CG2   . VAL A 1 166 ? 23.511  -13.786 -0.938  1.00 28.16  ? 166 VAL A CG2   1 
ATOM   1315 N  N     . VAL A 1 167 ? 19.549  -15.660 -2.403  1.00 23.03  ? 167 VAL A N     1 
ATOM   1316 C  CA    . VAL A 1 167 ? 18.275  -15.732 -3.114  1.00 27.83  ? 167 VAL A CA    1 
ATOM   1317 C  C     . VAL A 1 167 ? 17.116  -15.808 -2.126  1.00 26.57  ? 167 VAL A C     1 
ATOM   1318 O  O     . VAL A 1 167 ? 16.146  -15.045 -2.218  1.00 24.95  ? 167 VAL A O     1 
ATOM   1319 C  CB    . VAL A 1 167 ? 18.268  -16.929 -4.080  1.00 24.47  ? 167 VAL A CB    1 
ATOM   1320 C  CG1   . VAL A 1 167 ? 17.062  -16.853 -5.005  1.00 29.22  ? 167 VAL A CG1   1 
ATOM   1321 C  CG2   . VAL A 1 167 ? 19.564  -16.971 -4.880  1.00 20.75  ? 167 VAL A CG2   1 
ATOM   1322 N  N     . ALA A 1 168 ? 17.208  -16.724 -1.159  1.00 20.95  ? 168 ALA A N     1 
ATOM   1323 C  CA    . ALA A 1 168 ? 16.128  -16.911 -0.194  1.00 24.29  ? 168 ALA A CA    1 
ATOM   1324 C  C     . ALA A 1 168 ? 15.896  -15.657 0.641   1.00 23.03  ? 168 ALA A C     1 
ATOM   1325 O  O     . ALA A 1 168 ? 14.752  -15.330 0.977   1.00 26.59  ? 168 ALA A O     1 
ATOM   1326 C  CB    . ALA A 1 168 ? 16.437  -18.104 0.709   1.00 27.82  ? 168 ALA A CB    1 
ATOM   1327 N  N     . SER A 1 169 ? 16.969  -14.945 0.993   1.00 24.76  ? 169 SER A N     1 
ATOM   1328 C  CA    . SER A 1 169 ? 16.810  -13.721 1.772   1.00 25.06  ? 169 SER A CA    1 
ATOM   1329 C  C     . SER A 1 169 ? 16.208  -12.602 0.928   1.00 27.64  ? 169 SER A C     1 
ATOM   1330 O  O     . SER A 1 169 ? 15.386  -11.819 1.420   1.00 27.73  ? 169 SER A O     1 
ATOM   1331 C  CB    . SER A 1 169 ? 18.156  -13.294 2.355   1.00 27.03  ? 169 SER A CB    1 
ATOM   1332 O  OG    . SER A 1 169 ? 18.692  -14.307 3.192   1.00 30.69  ? 169 SER A OG    1 
ATOM   1333 N  N     . MET A 1 170 ? 16.610  -12.506 -0.342  1.00 21.18  ? 170 MET A N     1 
ATOM   1334 C  CA    . MET A 1 170 ? 16.037  -11.492 -1.222  1.00 23.17  ? 170 MET A CA    1 
ATOM   1335 C  C     . MET A 1 170 ? 14.553  -11.735 -1.463  1.00 21.26  ? 170 MET A C     1 
ATOM   1336 O  O     . MET A 1 170 ? 13.796  -10.782 -1.681  1.00 24.06  ? 170 MET A O     1 
ATOM   1337 C  CB    . MET A 1 170 ? 16.798  -11.454 -2.552  1.00 19.59  ? 170 MET A CB    1 
ATOM   1338 C  CG    . MET A 1 170 ? 18.210  -10.866 -2.454  1.00 24.65  ? 170 MET A CG    1 
ATOM   1339 S  SD    . MET A 1 170 ? 18.241  -9.072  -2.236  1.00 26.02  ? 170 MET A SD    1 
ATOM   1340 C  CE    . MET A 1 170 ? 17.596  -8.521  -3.814  1.00 27.83  ? 170 MET A CE    1 
ATOM   1341 N  N     . ARG A 1 171 ? 14.118  -12.998 -1.432  1.00 26.27  ? 171 ARG A N     1 
ATOM   1342 C  CA    . ARG A 1 171 ? 12.691  -13.279 -1.553  1.00 25.37  ? 171 ARG A CA    1 
ATOM   1343 C  C     . ARG A 1 171 ? 11.914  -12.686 -0.391  1.00 30.12  ? 171 ARG A C     1 
ATOM   1344 O  O     . ARG A 1 171 ? 10.762  -12.271 -0.559  1.00 25.01  ? 171 ARG A O     1 
ATOM   1345 C  CB    . ARG A 1 171 ? 12.440  -14.787 -1.638  1.00 25.42  ? 171 ARG A CB    1 
ATOM   1346 C  CG    . ARG A 1 171 ? 10.985  -15.123 -1.958  1.00 29.23  ? 171 ARG A CG    1 
ATOM   1347 C  CD    . ARG A 1 171 ? 10.720  -16.614 -2.040  1.00 34.15  ? 171 ARG A CD    1 
ATOM   1348 N  NE    . ARG A 1 171 ? 9.405   -16.880 -2.618  1.00 40.20  ? 171 ARG A NE    1 
ATOM   1349 C  CZ    . ARG A 1 171 ? 8.288   -17.009 -1.915  1.00 42.72  ? 171 ARG A CZ    1 
ATOM   1350 N  NH1   . ARG A 1 171 ? 8.289   -16.930 -0.594  1.00 49.56  ? 171 ARG A NH1   1 
ATOM   1351 N  NH2   . ARG A 1 171 ? 7.141   -17.220 -2.553  1.00 48.95  ? 171 ARG A NH2   1 
ATOM   1352 N  N     . ILE A 1 172 ? 12.530  -12.628 0.789   1.00 22.62  ? 172 ILE A N     1 
ATOM   1353 C  CA    . ILE A 1 172 ? 11.859  -12.061 1.950   1.00 26.10  ? 172 ILE A CA    1 
ATOM   1354 C  C     . ILE A 1 172 ? 11.978  -10.543 1.954   1.00 26.74  ? 172 ILE A C     1 
ATOM   1355 O  O     . ILE A 1 172 ? 11.000  -9.832  2.210   1.00 27.98  ? 172 ILE A O     1 
ATOM   1356 C  CB    . ILE A 1 172 ? 12.433  -12.676 3.240   1.00 31.14  ? 172 ILE A CB    1 
ATOM   1357 C  CG1   . ILE A 1 172 ? 12.170  -14.182 3.283   1.00 27.98  ? 172 ILE A CG1   1 
ATOM   1358 C  CG2   . ILE A 1 172 ? 11.848  -11.995 4.465   1.00 30.90  ? 172 ILE A CG2   1 
ATOM   1359 C  CD1   . ILE A 1 172 ? 12.875  -14.889 4.426   1.00 32.58  ? 172 ILE A CD1   1 
ATOM   1360 N  N     . MET A 1 173 ? 13.167  -10.021 1.654   1.00 29.06  ? 173 MET A N     1 
ATOM   1361 C  CA    . MET A 1 173 ? 13.445  -8.603  1.833   1.00 25.20  ? 173 MET A CA    1 
ATOM   1362 C  C     . MET A 1 173 ? 13.009  -7.737  0.658   1.00 26.03  ? 173 MET A C     1 
ATOM   1363 O  O     . MET A 1 173 ? 12.961  -6.511  0.809   1.00 26.31  ? 173 MET A O     1 
ATOM   1364 C  CB    . MET A 1 173 ? 14.940  -8.397  2.091   1.00 25.07  ? 173 MET A CB    1 
ATOM   1365 C  CG    . MET A 1 173 ? 15.431  -9.018  3.391   1.00 22.44  ? 173 MET A CG    1 
ATOM   1366 S  SD    . MET A 1 173 ? 14.532  -8.387  4.821   1.00 24.88  ? 173 MET A SD    1 
ATOM   1367 C  CE    . MET A 1 173 ? 14.848  -6.630  4.675   1.00 25.33  ? 173 MET A CE    1 
ATOM   1368 N  N     . THR A 1 174 ? 12.710  -8.324  -0.502  1.00 26.75  ? 174 THR A N     1 
ATOM   1369 C  CA    . THR A 1 174 ? 12.269  -7.556  -1.660  1.00 25.18  ? 174 THR A CA    1 
ATOM   1370 C  C     . THR A 1 174 ? 11.099  -8.271  -2.324  1.00 26.72  ? 174 THR A C     1 
ATOM   1371 O  O     . THR A 1 174 ? 10.726  -9.386  -1.952  1.00 30.12  ? 174 THR A O     1 
ATOM   1372 C  CB    . THR A 1 174 ? 13.404  -7.346  -2.681  1.00 30.82  ? 174 THR A CB    1 
ATOM   1373 O  OG1   . THR A 1 174 ? 13.680  -8.577  -3.359  1.00 28.82  ? 174 THR A OG1   1 
ATOM   1374 C  CG2   . THR A 1 174 ? 14.689  -6.862  -1.999  1.00 29.63  ? 174 THR A CG2   1 
ATOM   1375 N  N     . ARG A 1 175 ? 10.509  -7.602  -3.312  1.00 28.55  ? 175 ARG A N     1 
ATOM   1376 C  CA    . ARG A 1 175 ? 9.527   -8.213  -4.203  1.00 29.34  ? 175 ARG A CA    1 
ATOM   1377 C  C     . ARG A 1 175 ? 10.278  -8.711  -5.432  1.00 26.27  ? 175 ARG A C     1 
ATOM   1378 O  O     . ARG A 1 175 ? 10.798  -7.909  -6.214  1.00 33.25  ? 175 ARG A O     1 
ATOM   1379 C  CB    . ARG A 1 175 ? 8.445   -7.207  -4.585  1.00 34.65  ? 175 ARG A CB    1 
ATOM   1380 C  CG    . ARG A 1 175 ? 7.612   -6.715  -3.413  1.00 37.27  ? 175 ARG A CG    1 
ATOM   1381 C  CD    . ARG A 1 175 ? 7.389   -5.216  -3.478  1.00 40.83  ? 175 ARG A CD    1 
ATOM   1382 N  NE    . ARG A 1 175 ? 6.489   -4.758  -2.425  1.00 44.54  ? 175 ARG A NE    1 
ATOM   1383 C  CZ    . ARG A 1 175 ? 6.879   -4.195  -1.290  1.00 46.54  ? 175 ARG A CZ    1 
ATOM   1384 N  NH1   . ARG A 1 175 ? 8.159   -3.979  -1.026  1.00 38.35  ? 175 ARG A NH1   1 
ATOM   1385 N  NH2   . ARG A 1 175 ? 5.961   -3.838  -0.396  1.00 46.83  ? 175 ARG A NH2   1 
ATOM   1386 N  N     A MET A 1 176 ? 10.347  -10.030 -5.599  0.50 29.78  ? 176 MET A N     1 
ATOM   1387 N  N     B MET A 1 176 ? 10.333  -10.029 -5.610  0.50 29.76  ? 176 MET A N     1 
ATOM   1388 C  CA    A MET A 1 176 ? 11.142  -10.626 -6.661  0.50 31.52  ? 176 MET A CA    1 
ATOM   1389 C  CA    B MET A 1 176 ? 11.144  -10.604 -6.671  0.50 31.50  ? 176 MET A CA    1 
ATOM   1390 C  C     A MET A 1 176 ? 10.354  -11.714 -7.376  0.50 32.14  ? 176 MET A C     1 
ATOM   1391 C  C     B MET A 1 176 ? 10.392  -11.734 -7.359  0.50 32.24  ? 176 MET A C     1 
ATOM   1392 O  O     A MET A 1 176 ? 9.421   -12.305 -6.825  0.50 31.82  ? 176 MET A O     1 
ATOM   1393 O  O     B MET A 1 176 ? 9.510   -12.366 -6.772  0.50 31.84  ? 176 MET A O     1 
ATOM   1394 C  CB    A MET A 1 176 ? 12.456  -11.209 -6.123  0.50 33.29  ? 176 MET A CB    1 
ATOM   1395 C  CB    B MET A 1 176 ? 12.490  -11.107 -6.126  0.50 33.32  ? 176 MET A CB    1 
ATOM   1396 C  CG    A MET A 1 176 ? 12.281  -12.273 -5.058  0.50 32.29  ? 176 MET A CG    1 
ATOM   1397 C  CG    B MET A 1 176 ? 12.468  -12.504 -5.539  0.50 32.25  ? 176 MET A CG    1 
ATOM   1398 S  SD    A MET A 1 176 ? 13.734  -13.334 -4.924  0.50 39.57  ? 176 MET A SD    1 
ATOM   1399 S  SD    B MET A 1 176 ? 13.009  -13.741 -6.733  0.50 30.34  ? 176 MET A SD    1 
ATOM   1400 C  CE    A MET A 1 176 ? 13.653  -14.196 -6.488  0.50 28.25  ? 176 MET A CE    1 
ATOM   1401 C  CE    B MET A 1 176 ? 13.429  -15.102 -5.648  0.50 26.27  ? 176 MET A CE    1 
ATOM   1402 N  N     . GLY A 1 177 ? 10.749  -11.975 -8.621  1.00 30.21  ? 177 GLY A N     1 
ATOM   1403 C  CA    . GLY A 1 177 ? 10.176  -13.042 -9.408  1.00 36.27  ? 177 GLY A CA    1 
ATOM   1404 C  C     . GLY A 1 177 ? 9.760   -12.582 -10.788 1.00 36.85  ? 177 GLY A C     1 
ATOM   1405 O  O     . GLY A 1 177 ? 10.080  -11.474 -11.232 1.00 34.58  ? 177 GLY A O     1 
ATOM   1406 N  N     . THR A 1 178 ? 9.014   -13.458 -11.468 1.00 38.78  ? 178 THR A N     1 
ATOM   1407 C  CA    . THR A 1 178 ? 8.678   -13.255 -12.875 1.00 36.25  ? 178 THR A CA    1 
ATOM   1408 C  C     . THR A 1 178 ? 7.959   -11.931 -13.105 1.00 38.95  ? 178 THR A C     1 
ATOM   1409 O  O     . THR A 1 178 ? 8.216   -11.244 -14.101 1.00 38.95  ? 178 THR A O     1 
ATOM   1410 C  CB    . THR A 1 178 ? 7.820   -14.419 -13.371 1.00 40.01  ? 178 THR A CB    1 
ATOM   1411 O  OG1   . THR A 1 178 ? 8.557   -15.641 -13.253 1.00 36.47  ? 178 THR A OG1   1 
ATOM   1412 C  CG2   . THR A 1 178 ? 7.406   -14.217 -14.827 1.00 41.33  ? 178 THR A CG2   1 
ATOM   1413 N  N     . SER A 1 179 ? 7.058   -11.552 -12.194 1.00 34.17  ? 179 SER A N     1 
ATOM   1414 C  CA    . SER A 1 179 ? 6.259   -10.347 -12.393 1.00 40.85  ? 179 SER A CA    1 
ATOM   1415 C  C     . SER A 1 179 ? 7.109   -9.084  -12.452 1.00 45.50  ? 179 SER A C     1 
ATOM   1416 O  O     . SER A 1 179 ? 6.681   -8.091  -13.051 1.00 40.86  ? 179 SER A O     1 
ATOM   1417 C  CB    . SER A 1 179 ? 5.216   -10.220 -11.283 1.00 44.96  ? 179 SER A CB    1 
ATOM   1418 O  OG    . SER A 1 179 ? 5.842   -10.053 -10.023 1.00 52.41  ? 179 SER A OG    1 
ATOM   1419 N  N     . VAL A 1 180 ? 8.302   -9.097  -11.852 1.00 35.28  ? 180 VAL A N     1 
ATOM   1420 C  CA    . VAL A 1 180 ? 9.170   -7.926  -11.911 1.00 38.03  ? 180 VAL A CA    1 
ATOM   1421 C  C     . VAL A 1 180 ? 9.767   -7.770  -13.305 1.00 36.44  ? 180 VAL A C     1 
ATOM   1422 O  O     . VAL A 1 180 ? 9.876   -6.654  -13.827 1.00 39.53  ? 180 VAL A O     1 
ATOM   1423 C  CB    . VAL A 1 180 ? 10.263  -8.015  -10.830 1.00 32.79  ? 180 VAL A CB    1 
ATOM   1424 C  CG1   . VAL A 1 180 ? 11.166  -6.796  -10.888 1.00 33.92  ? 180 VAL A CG1   1 
ATOM   1425 C  CG2   . VAL A 1 180 ? 9.634   -8.145  -9.450  1.00 35.31  ? 180 VAL A CG2   1 
ATOM   1426 N  N     . LEU A 1 181 ? 10.170  -8.883  -13.928 1.00 35.78  ? 181 LEU A N     1 
ATOM   1427 C  CA    . LEU A 1 181 ? 10.663  -8.824  -15.301 1.00 34.03  ? 181 LEU A CA    1 
ATOM   1428 C  C     . LEU A 1 181 ? 9.584   -8.314  -16.245 1.00 43.95  ? 181 LEU A C     1 
ATOM   1429 O  O     . LEU A 1 181 ? 9.875   -7.593  -17.207 1.00 41.92  ? 181 LEU A O     1 
ATOM   1430 C  CB    . LEU A 1 181 ? 11.148  -10.204 -15.749 1.00 37.60  ? 181 LEU A CB    1 
ATOM   1431 C  CG    . LEU A 1 181 ? 12.486  -10.725 -15.222 1.00 38.96  ? 181 LEU A CG    1 
ATOM   1432 C  CD1   . LEU A 1 181 ? 12.710  -12.159 -15.676 1.00 36.54  ? 181 LEU A CD1   1 
ATOM   1433 C  CD2   . LEU A 1 181 ? 13.625  -9.834  -15.688 1.00 38.78  ? 181 LEU A CD2   1 
ATOM   1434 N  N     . GLU A 1 182 ? 8.328   -8.680  -15.983 1.00 38.69  ? 182 GLU A N     1 
ATOM   1435 C  CA    . GLU A 1 182 ? 7.229   -8.199  -16.811 1.00 45.81  ? 182 GLU A CA    1 
ATOM   1436 C  C     . GLU A 1 182 ? 6.989   -6.710  -16.606 1.00 49.72  ? 182 GLU A C     1 
ATOM   1437 O  O     . GLU A 1 182 ? 6.622   -6.006  -17.553 1.00 57.05  ? 182 GLU A O     1 
ATOM   1438 C  CB    . GLU A 1 182 ? 5.963   -8.997  -16.504 1.00 42.58  ? 182 GLU A CB    1 
ATOM   1439 C  CG    . GLU A 1 182 ? 6.152   -10.502 -16.629 1.00 51.57  ? 182 GLU A CG    1 
ATOM   1440 C  CD    . GLU A 1 182 ? 4.919   -11.286 -16.220 1.00 66.80  ? 182 GLU A CD    1 
ATOM   1441 O  OE1   . GLU A 1 182 ? 3.942   -10.662 -15.756 1.00 66.35  ? 182 GLU A OE1   1 
ATOM   1442 O  OE2   . GLU A 1 182 ? 4.930   -12.528 -16.363 1.00 73.79  ? 182 GLU A OE2   1 
ATOM   1443 N  N     . ALA A 1 183 ? 7.196   -6.213  -15.385 1.00 51.75  ? 183 ALA A N     1 
ATOM   1444 C  CA    . ALA A 1 183 ? 7.043   -4.787  -15.128 1.00 48.68  ? 183 ALA A CA    1 
ATOM   1445 C  C     . ALA A 1 183 ? 8.224   -3.984  -15.655 1.00 48.66  ? 183 ALA A C     1 
ATOM   1446 O  O     . ALA A 1 183 ? 8.042   -2.848  -16.105 1.00 52.39  ? 183 ALA A O     1 
ATOM   1447 C  CB    . ALA A 1 183 ? 6.865   -4.537  -13.630 1.00 47.12  ? 183 ALA A CB    1 
ATOM   1448 N  N     . LEU A 1 184 ? 9.430   -4.554  -15.615 1.00 49.34  ? 184 LEU A N     1 
ATOM   1449 C  CA    . LEU A 1 184 ? 10.612  -3.828  -16.069 1.00 51.08  ? 184 LEU A CA    1 
ATOM   1450 C  C     . LEU A 1 184 ? 10.542  -3.534  -17.562 1.00 47.24  ? 184 LEU A C     1 
ATOM   1451 O  O     . LEU A 1 184 ? 10.709  -2.385  -17.986 1.00 49.64  ? 184 LEU A O     1 
ATOM   1452 C  CB    . LEU A 1 184 ? 11.876  -4.623  -15.739 1.00 47.82  ? 184 LEU A CB    1 
ATOM   1453 C  CG    . LEU A 1 184 ? 13.160  -4.105  -16.392 1.00 50.52  ? 184 LEU A CG    1 
ATOM   1454 C  CD1   . LEU A 1 184 ? 13.486  -2.697  -15.909 1.00 47.70  ? 184 LEU A CD1   1 
ATOM   1455 C  CD2   . LEU A 1 184 ? 14.322  -5.052  -16.135 1.00 47.92  ? 184 LEU A CD2   1 
ATOM   1456 N  N     . GLY A 1 185 ? 10.296  -4.560  -18.373 1.00 54.06  ? 185 GLY A N     1 
ATOM   1457 C  CA    . GLY A 1 185 ? 10.308  -4.367  -19.812 1.00 52.57  ? 185 GLY A CA    1 
ATOM   1458 C  C     . GLY A 1 185 ? 11.685  -3.957  -20.289 1.00 60.97  ? 185 GLY A C     1 
ATOM   1459 O  O     . GLY A 1 185 ? 12.709  -4.496  -19.853 1.00 60.56  ? 185 GLY A O     1 
ATOM   1460 N  N     . ASP A 1 186 ? 11.718  -2.981  -21.195 1.00 63.94  ? 186 ASP A N     1 
ATOM   1461 C  CA    . ASP A 1 186 ? 12.966  -2.410  -21.681 1.00 69.05  ? 186 ASP A CA    1 
ATOM   1462 C  C     . ASP A 1 186 ? 13.420  -1.208  -20.859 1.00 65.69  ? 186 ASP A C     1 
ATOM   1463 O  O     . ASP A 1 186 ? 14.259  -0.429  -21.327 1.00 65.77  ? 186 ASP A O     1 
ATOM   1464 C  CB    . ASP A 1 186 ? 12.832  -2.020  -23.155 1.00 71.56  ? 186 ASP A CB    1 
ATOM   1465 C  CG    . ASP A 1 186 ? 12.720  -3.225  -24.070 1.00 82.77  ? 186 ASP A CG    1 
ATOM   1466 O  OD1   . ASP A 1 186 ? 13.222  -4.307  -23.697 1.00 76.36  ? 186 ASP A OD1   1 
ATOM   1467 O  OD2   . ASP A 1 186 ? 12.132  -3.089  -25.163 1.00 95.71  ? 186 ASP A OD2   1 
ATOM   1468 N  N     . GLY A 1 187 ? 12.889  -1.043  -19.652 1.00 60.65  ? 187 GLY A N     1 
ATOM   1469 C  CA    . GLY A 1 187 ? 13.251  0.076   -18.811 1.00 48.23  ? 187 GLY A CA    1 
ATOM   1470 C  C     . GLY A 1 187 ? 14.626  -0.091  -18.191 1.00 55.27  ? 187 GLY A C     1 
ATOM   1471 O  O     . GLY A 1 187 ? 15.328  -1.084  -18.385 1.00 52.78  ? 187 GLY A O     1 
ATOM   1472 N  N     . GLU A 1 188 ? 15.014  0.921   -17.420 1.00 47.74  ? 188 GLU A N     1 
ATOM   1473 C  CA    . GLU A 1 188 ? 16.310  0.920   -16.759 1.00 53.19  ? 188 GLU A CA    1 
ATOM   1474 C  C     . GLU A 1 188 ? 16.258  0.091   -15.483 1.00 47.03  ? 188 GLU A C     1 
ATOM   1475 O  O     . GLU A 1 188 ? 15.250  0.080   -14.770 1.00 45.88  ? 188 GLU A O     1 
ATOM   1476 C  CB    . GLU A 1 188 ? 16.747  2.347   -16.431 1.00 57.94  ? 188 GLU A CB    1 
ATOM   1477 C  CG    . GLU A 1 188 ? 16.934  3.239   -17.645 1.00 73.47  ? 188 GLU A CG    1 
ATOM   1478 C  CD    . GLU A 1 188 ? 17.373  4.640   -17.271 1.00 89.23  ? 188 GLU A CD    1 
ATOM   1479 O  OE1   . GLU A 1 188 ? 17.505  4.918   -16.060 1.00 89.38  ? 188 GLU A OE1   1 
ATOM   1480 O  OE2   . GLU A 1 188 ? 17.586  5.463   -18.187 1.00 98.90  ? 188 GLU A OE2   1 
ATOM   1481 N  N     . PHE A 1 189 ? 17.355  -0.605  -15.197 1.00 45.00  ? 189 PHE A N     1 
ATOM   1482 C  CA    . PHE A 1 189 ? 17.464  -1.396  -13.984 1.00 40.36  ? 189 PHE A CA    1 
ATOM   1483 C  C     . PHE A 1 189 ? 18.851  -1.210  -13.388 1.00 43.20  ? 189 PHE A C     1 
ATOM   1484 O  O     . PHE A 1 189 ? 19.797  -0.806  -14.070 1.00 44.15  ? 189 PHE A O     1 
ATOM   1485 C  CB    . PHE A 1 189 ? 17.181  -2.886  -14.245 1.00 38.96  ? 189 PHE A CB    1 
ATOM   1486 C  CG    . PHE A 1 189 ? 18.086  -3.512  -15.270 1.00 40.56  ? 189 PHE A CG    1 
ATOM   1487 C  CD1   . PHE A 1 189 ? 17.795  -3.417  -16.622 1.00 42.53  ? 189 PHE A CD1   1 
ATOM   1488 C  CD2   . PHE A 1 189 ? 19.219  -4.210  -14.881 1.00 36.98  ? 189 PHE A CD2   1 
ATOM   1489 C  CE1   . PHE A 1 189 ? 18.621  -3.995  -17.567 1.00 46.83  ? 189 PHE A CE1   1 
ATOM   1490 C  CE2   . PHE A 1 189 ? 20.050  -4.792  -15.821 1.00 38.81  ? 189 PHE A CE2   1 
ATOM   1491 C  CZ    . PHE A 1 189 ? 19.750  -4.685  -17.166 1.00 43.00  ? 189 PHE A CZ    1 
ATOM   1492 N  N     . ILE A 1 190 ? 18.957  -1.501  -12.097 1.00 37.78  ? 190 ILE A N     1 
ATOM   1493 C  CA    . ILE A 1 190 ? 20.221  -1.410  -11.377 1.00 37.94  ? 190 ILE A CA    1 
ATOM   1494 C  C     . ILE A 1 190 ? 20.935  -2.751  -11.484 1.00 30.97  ? 190 ILE A C     1 
ATOM   1495 O  O     . ILE A 1 190 ? 20.384  -3.792  -11.108 1.00 28.97  ? 190 ILE A O     1 
ATOM   1496 C  CB    . ILE A 1 190 ? 19.997  -1.017  -9.910  1.00 40.21  ? 190 ILE A CB    1 
ATOM   1497 C  CG1   . ILE A 1 190 ? 19.293  0.338   -9.836  1.00 43.88  ? 190 ILE A CG1   1 
ATOM   1498 C  CG2   . ILE A 1 190 ? 21.320  -0.983  -9.159  1.00 31.93  ? 190 ILE A CG2   1 
ATOM   1499 C  CD1   . ILE A 1 190 ? 20.063  1.466   -10.476 1.00 50.01  ? 190 ILE A CD1   1 
ATOM   1500 N  N     . LYS A 1 191 ? 22.158  -2.727  -12.001 1.00 34.07  ? 191 LYS A N     1 
ATOM   1501 C  CA    . LYS A 1 191 ? 22.935  -3.943  -12.196 1.00 32.43  ? 191 LYS A CA    1 
ATOM   1502 C  C     . LYS A 1 191 ? 23.648  -4.309  -10.899 1.00 31.40  ? 191 LYS A C     1 
ATOM   1503 O  O     . LYS A 1 191 ? 24.480  -3.542  -10.402 1.00 31.19  ? 191 LYS A O     1 
ATOM   1504 C  CB    . LYS A 1 191 ? 23.937  -3.747  -13.330 1.00 33.06  ? 191 LYS A CB    1 
ATOM   1505 C  CG    . LYS A 1 191 ? 23.296  -3.324  -14.639 1.00 41.14  ? 191 LYS A CG    1 
ATOM   1506 C  CD    . LYS A 1 191 ? 24.323  -2.761  -15.607 1.00 41.00  ? 191 LYS A CD    1 
ATOM   1507 C  CE    . LYS A 1 191 ? 23.646  -2.117  -16.805 1.00 54.92  ? 191 LYS A CE    1 
ATOM   1508 N  NZ    . LYS A 1 191 ? 24.631  -1.495  -17.732 1.00 70.08  ? 191 LYS A NZ    1 
ATOM   1509 N  N     . CYS A 1 192 ? 23.324  -5.479  -10.355 1.00 26.01  ? 192 CYS A N     1 
ATOM   1510 C  CA    . CYS A 1 192 ? 23.914  -5.969  -9.116  1.00 29.40  ? 192 CYS A CA    1 
ATOM   1511 C  C     . CYS A 1 192 ? 24.585  -7.304  -9.394  1.00 27.04  ? 192 CYS A C     1 
ATOM   1512 O  O     . CYS A 1 192 ? 23.947  -8.228  -9.909  1.00 31.45  ? 192 CYS A O     1 
ATOM   1513 C  CB    . CYS A 1 192 ? 22.853  -6.111  -8.023  1.00 28.73  ? 192 CYS A CB    1 
ATOM   1514 S  SG    . CYS A 1 192 ? 21.857  -4.625  -7.757  1.00 29.16  ? 192 CYS A SG    1 
ATOM   1515 N  N     . LEU A 1 193 ? 25.870  -7.400  -9.062  1.00 25.46  ? 193 LEU A N     1 
ATOM   1516 C  CA    . LEU A 1 193 ? 26.656  -8.611  -9.271  1.00 26.81  ? 193 LEU A CA    1 
ATOM   1517 C  C     . LEU A 1 193 ? 27.313  -8.991  -7.953  1.00 32.78  ? 193 LEU A C     1 
ATOM   1518 O  O     . LEU A 1 193 ? 28.024  -8.177  -7.355  1.00 29.65  ? 193 LEU A O     1 
ATOM   1519 C  CB    . LEU A 1 193 ? 27.711  -8.402  -10.362 1.00 28.49  ? 193 LEU A CB    1 
ATOM   1520 C  CG    . LEU A 1 193 ? 28.798  -9.471  -10.508 1.00 30.98  ? 193 LEU A CG    1 
ATOM   1521 C  CD1   . LEU A 1 193 ? 28.202  -10.814 -10.896 1.00 29.83  ? 193 LEU A CD1   1 
ATOM   1522 C  CD2   . LEU A 1 193 ? 29.848  -9.031  -11.522 1.00 29.78  ? 193 LEU A CD2   1 
ATOM   1523 N  N     . HIS A 1 194 ? 27.075  -10.222 -7.504  1.00 28.93  ? 194 HIS A N     1 
ATOM   1524 C  CA    . HIS A 1 194 ? 27.592  -10.699 -6.233  1.00 30.47  ? 194 HIS A CA    1 
ATOM   1525 C  C     . HIS A 1 194 ? 28.202  -12.081 -6.402  1.00 31.26  ? 194 HIS A C     1 
ATOM   1526 O  O     . HIS A 1 194 ? 27.707  -12.898 -7.184  1.00 25.33  ? 194 HIS A O     1 
ATOM   1527 C  CB    . HIS A 1 194 ? 26.495  -10.750 -5.161  1.00 28.49  ? 194 HIS A CB    1 
ATOM   1528 C  CG    . HIS A 1 194 ? 26.929  -11.414 -3.892  1.00 27.07  ? 194 HIS A CG    1 
ATOM   1529 N  ND1   . HIS A 1 194 ? 26.576  -12.708 -3.571  1.00 23.52  ? 194 HIS A ND1   1 
ATOM   1530 C  CD2   . HIS A 1 194 ? 27.701  -10.970 -2.870  1.00 26.10  ? 194 HIS A CD2   1 
ATOM   1531 C  CE1   . HIS A 1 194 ? 27.103  -13.028 -2.402  1.00 30.65  ? 194 HIS A CE1   1 
ATOM   1532 N  NE2   . HIS A 1 194 ? 27.791  -11.992 -1.957  1.00 27.93  ? 194 HIS A NE2   1 
ATOM   1533 N  N     . SER A 1 195 ? 29.281  -12.333 -5.664  1.00 24.45  ? 195 SER A N     1 
ATOM   1534 C  CA    . SER A 1 195 ? 29.881  -13.656 -5.608  1.00 26.22  ? 195 SER A CA    1 
ATOM   1535 C  C     . SER A 1 195 ? 30.529  -13.856 -4.247  1.00 33.88  ? 195 SER A C     1 
ATOM   1536 O  O     . SER A 1 195 ? 31.173  -12.946 -3.718  1.00 30.42  ? 195 SER A O     1 
ATOM   1537 C  CB    . SER A 1 195 ? 30.924  -13.855 -6.713  1.00 30.88  ? 195 SER A CB    1 
ATOM   1538 O  OG    . SER A 1 195 ? 31.664  -15.043 -6.488  1.00 28.28  ? 195 SER A OG    1 
ATOM   1539 N  N     . VAL A 1 196 ? 30.358  -15.059 -3.693  1.00 32.45  ? 196 VAL A N     1 
ATOM   1540 C  CA    . VAL A 1 196 ? 31.038  -15.422 -2.456  1.00 33.71  ? 196 VAL A CA    1 
ATOM   1541 C  C     . VAL A 1 196 ? 32.541  -15.559 -2.660  1.00 35.56  ? 196 VAL A C     1 
ATOM   1542 O  O     . VAL A 1 196 ? 33.295  -15.583 -1.680  1.00 36.57  ? 196 VAL A O     1 
ATOM   1543 C  CB    . VAL A 1 196 ? 30.452  -16.728 -1.887  1.00 38.15  ? 196 VAL A CB    1 
ATOM   1544 C  CG1   . VAL A 1 196 ? 29.049  -16.491 -1.352  1.00 27.46  ? 196 VAL A CG1   1 
ATOM   1545 C  CG2   . VAL A 1 196 ? 30.440  -17.811 -2.957  1.00 36.54  ? 196 VAL A CG2   1 
ATOM   1546 N  N     . GLY A 1 197 ? 32.996  -15.659 -3.907  1.00 38.01  ? 197 GLY A N     1 
ATOM   1547 C  CA    . GLY A 1 197 ? 34.417  -15.732 -4.189  1.00 32.60  ? 197 GLY A CA    1 
ATOM   1548 C  C     . GLY A 1 197 ? 35.066  -17.044 -3.819  1.00 38.73  ? 197 GLY A C     1 
ATOM   1549 O  O     . GLY A 1 197 ? 36.233  -17.058 -3.408  1.00 45.95  ? 197 GLY A O     1 
ATOM   1550 N  N     A CYS A 1 198 ? 34.341  -18.154 -3.940  0.50 39.48  ? 198 CYS A N     1 
ATOM   1551 N  N     B CYS A 1 198 ? 34.350  -18.154 -3.977  0.50 39.48  ? 198 CYS A N     1 
ATOM   1552 C  CA    A CYS A 1 198 ? 34.848  -19.481 -3.591  0.50 42.00  ? 198 CYS A CA    1 
ATOM   1553 C  CA    B CYS A 1 198 ? 34.833  -19.478 -3.589  0.50 42.00  ? 198 CYS A CA    1 
ATOM   1554 C  C     A CYS A 1 198 ? 34.598  -20.438 -4.749  0.50 40.68  ? 198 CYS A C     1 
ATOM   1555 C  C     B CYS A 1 198 ? 34.609  -20.455 -4.738  0.50 40.68  ? 198 CYS A C     1 
ATOM   1556 O  O     A CYS A 1 198 ? 33.711  -21.298 -4.683  0.50 43.85  ? 198 CYS A O     1 
ATOM   1557 O  O     B CYS A 1 198 ? 33.753  -21.344 -4.657  0.50 43.83  ? 198 CYS A O     1 
ATOM   1558 C  CB    A CYS A 1 198 ? 34.198  -19.996 -2.307  0.50 42.37  ? 198 CYS A CB    1 
ATOM   1559 C  CB    B CYS A 1 198 ? 34.128  -19.951 -2.317  0.50 42.34  ? 198 CYS A CB    1 
ATOM   1560 S  SG    A CYS A 1 198 ? 34.697  -19.113 -0.817  0.50 39.63  ? 198 CYS A SG    1 
ATOM   1561 S  SG    B CYS A 1 198 ? 35.149  -20.954 -1.228  0.50 42.87  ? 198 CYS A SG    1 
ATOM   1562 N  N     . PRO A 1 199 ? 35.371  -20.322 -5.825  1.00 40.98  ? 199 PRO A N     1 
ATOM   1563 C  CA    . PRO A 1 199 ? 35.180  -21.224 -6.965  1.00 45.00  ? 199 PRO A CA    1 
ATOM   1564 C  C     . PRO A 1 199 ? 35.552  -22.656 -6.617  1.00 50.06  ? 199 PRO A C     1 
ATOM   1565 O  O     . PRO A 1 199 ? 36.450  -22.916 -5.813  1.00 52.67  ? 199 PRO A O     1 
ATOM   1566 C  CB    . PRO A 1 199 ? 36.118  -20.649 -8.033  1.00 47.63  ? 199 PRO A CB    1 
ATOM   1567 C  CG    . PRO A 1 199 ? 37.175  -19.946 -7.254  1.00 43.17  ? 199 PRO A CG    1 
ATOM   1568 C  CD    . PRO A 1 199 ? 36.473  -19.371 -6.052  1.00 39.92  ? 199 PRO A CD    1 
ATOM   1569 N  N     . LEU A 1 200 ? 34.838  -23.590 -7.237  1.00 51.36  ? 200 LEU A N     1 
ATOM   1570 C  CA    . LEU A 1 200 ? 35.052  -25.018 -7.045  1.00 55.54  ? 200 LEU A CA    1 
ATOM   1571 C  C     . LEU A 1 200 ? 36.077  -25.536 -8.052  1.00 56.13  ? 200 LEU A C     1 
ATOM   1572 O  O     . LEU A 1 200 ? 36.095  -25.088 -9.202  1.00 58.85  ? 200 LEU A O     1 
ATOM   1573 C  CB    . LEU A 1 200 ? 33.740  -25.781 -7.203  1.00 54.36  ? 200 LEU A CB    1 
ATOM   1574 C  CG    . LEU A 1 200 ? 32.639  -25.333 -6.239  1.00 54.75  ? 200 LEU A CG    1 
ATOM   1575 C  CD1   . LEU A 1 200 ? 31.310  -25.996 -6.562  1.00 54.91  ? 200 LEU A CD1   1 
ATOM   1576 C  CD2   . LEU A 1 200 ? 33.045  -25.622 -4.804  1.00 51.93  ? 200 LEU A CD2   1 
ATOM   1577 N  N     . PRO A 1 201 ? 36.956  -26.472 -7.661  1.00 68.41  ? 201 PRO A N     1 
ATOM   1578 C  CA    . PRO A 1 201 ? 37.063  -27.135 -6.351  1.00 66.01  ? 201 PRO A CA    1 
ATOM   1579 C  C     . PRO A 1 201 ? 37.660  -26.232 -5.275  1.00 69.04  ? 201 PRO A C     1 
ATOM   1580 O  O     . PRO A 1 201 ? 38.439  -25.329 -5.569  1.00 69.00  ? 201 PRO A O     1 
ATOM   1581 C  CB    . PRO A 1 201 ? 37.969  -28.334 -6.656  1.00 68.06  ? 201 PRO A CB    1 
ATOM   1582 C  CG    . PRO A 1 201 ? 38.871  -27.830 -7.742  1.00 69.92  ? 201 PRO A CG    1 
ATOM   1583 C  CD    . PRO A 1 201 ? 37.994  -26.946 -8.595  1.00 65.79  ? 201 PRO A CD    1 
ATOM   1584 N  N     . LEU A 1 202 ? 37.309  -26.474 -4.013  1.00 68.44  ? 202 LEU A N     1 
ATOM   1585 C  CA    . LEU A 1 202 ? 37.711  -25.589 -2.927  1.00 79.93  ? 202 LEU A CA    1 
ATOM   1586 C  C     . LEU A 1 202 ? 39.212  -25.685 -2.682  1.00 94.69  ? 202 LEU A C     1 
ATOM   1587 O  O     . LEU A 1 202 ? 39.741  -26.773 -2.432  1.00 89.71  ? 202 LEU A O     1 
ATOM   1588 C  CB    . LEU A 1 202 ? 36.942  -25.933 -1.655  1.00 76.64  ? 202 LEU A CB    1 
ATOM   1589 C  CG    . LEU A 1 202 ? 35.434  -25.694 -1.701  1.00 67.67  ? 202 LEU A CG    1 
ATOM   1590 C  CD1   . LEU A 1 202 ? 34.811  -25.891 -0.328  1.00 64.51  ? 202 LEU A CD1   1 
ATOM   1591 C  CD2   . LEU A 1 202 ? 35.145  -24.303 -2.228  1.00 61.63  ? 202 LEU A CD2   1 
ATOM   1592 N  N     . LYS A 1 203 ? 39.896  -24.542 -2.756  1.00 112.47 ? 203 LYS A N     1 
ATOM   1593 C  CA    . LYS A 1 203 ? 41.300  -24.490 -2.366  1.00 118.61 ? 203 LYS A CA    1 
ATOM   1594 C  C     . LYS A 1 203 ? 41.449  -24.479 -0.850  1.00 122.22 ? 203 LYS A C     1 
ATOM   1595 O  O     . LYS A 1 203 ? 42.379  -25.086 -0.309  1.00 124.36 ? 203 LYS A O     1 
ATOM   1596 C  CB    . LYS A 1 203 ? 41.972  -23.257 -2.973  1.00 121.94 ? 203 LYS A CB    1 
ATOM   1597 C  CG    . LYS A 1 203 ? 41.900  -23.182 -4.488  1.00 121.67 ? 203 LYS A CG    1 
ATOM   1598 C  CD    . LYS A 1 203 ? 42.642  -24.337 -5.137  1.00 124.65 ? 203 LYS A CD    1 
ATOM   1599 C  CE    . LYS A 1 203 ? 42.629  -24.215 -6.651  1.00 127.67 ? 203 LYS A CE    1 
ATOM   1600 N  NZ    . LYS A 1 203 ? 41.242  -24.146 -7.188  1.00 119.11 ? 203 LYS A NZ    1 
ATOM   1601 N  N     . LYS A 1 204 ? 40.539  -23.799 -0.154  1.00 127.49 ? 204 LYS A N     1 
ATOM   1602 C  CA    . LYS A 1 204 ? 40.551  -23.669 1.292   1.00 123.98 ? 204 LYS A CA    1 
ATOM   1603 C  C     . LYS A 1 204 ? 39.320  -24.338 1.893   1.00 123.51 ? 204 LYS A C     1 
ATOM   1604 O  O     . LYS A 1 204 ? 38.242  -24.320 1.289   1.00 120.88 ? 204 LYS A O     1 
ATOM   1605 C  CB    . LYS A 1 204 ? 40.576  -22.194 1.714   1.00 127.30 ? 204 LYS A CB    1 
ATOM   1606 C  CG    . LYS A 1 204 ? 41.505  -21.319 0.890   1.00 135.09 ? 204 LYS A CG    1 
ATOM   1607 C  CD    . LYS A 1 204 ? 41.266  -19.846 1.185   1.00 138.92 ? 204 LYS A CD    1 
ATOM   1608 C  CE    . LYS A 1 204 ? 42.082  -18.954 0.264   1.00 134.93 ? 204 LYS A CE    1 
ATOM   1609 N  NZ    . LYS A 1 204 ? 41.790  -17.512 0.492   1.00 116.92 ? 204 LYS A NZ    1 
ATOM   1610 N  N     . PRO A 1 205 ? 39.445  -24.936 3.076   1.00 103.57 ? 205 PRO A N     1 
ATOM   1611 C  CA    . PRO A 1 205 ? 38.268  -25.505 3.742   1.00 88.27  ? 205 PRO A CA    1 
ATOM   1612 C  C     . PRO A 1 205 ? 37.396  -24.415 4.348   1.00 82.86  ? 205 PRO A C     1 
ATOM   1613 O  O     . PRO A 1 205 ? 37.890  -23.407 4.861   1.00 78.06  ? 205 PRO A O     1 
ATOM   1614 C  CB    . PRO A 1 205 ? 38.876  -26.402 4.826   1.00 96.83  ? 205 PRO A CB    1 
ATOM   1615 C  CG    . PRO A 1 205 ? 40.190  -25.762 5.132   1.00 97.04  ? 205 PRO A CG    1 
ATOM   1616 C  CD    . PRO A 1 205 ? 40.686  -25.185 3.832   1.00 101.70 ? 205 PRO A CD    1 
ATOM   1617 N  N     . LEU A 1 206 ? 36.085  -24.628 4.284   1.00 70.12  ? 206 LEU A N     1 
ATOM   1618 C  CA    . LEU A 1 206 ? 35.121  -23.642 4.748   1.00 55.69  ? 206 LEU A CA    1 
ATOM   1619 C  C     . LEU A 1 206 ? 34.784  -23.850 6.220   1.00 57.79  ? 206 LEU A C     1 
ATOM   1620 O  O     . LEU A 1 206 ? 34.816  -24.971 6.736   1.00 60.43  ? 206 LEU A O     1 
ATOM   1621 C  CB    . LEU A 1 206 ? 33.840  -23.705 3.913   1.00 47.66  ? 206 LEU A CB    1 
ATOM   1622 C  CG    . LEU A 1 206 ? 33.994  -23.473 2.410   1.00 52.61  ? 206 LEU A CG    1 
ATOM   1623 C  CD1   . LEU A 1 206 ? 32.631  -23.396 1.739   1.00 48.24  ? 206 LEU A CD1   1 
ATOM   1624 C  CD2   . LEU A 1 206 ? 34.801  -22.214 2.141   1.00 51.52  ? 206 LEU A CD2   1 
ATOM   1625 N  N     . VAL A 1 207 ? 34.455  -22.750 6.891   1.00 53.07  ? 207 VAL A N     1 
ATOM   1626 C  CA    . VAL A 1 207 ? 34.034  -22.765 8.287   1.00 48.58  ? 207 VAL A CA    1 
ATOM   1627 C  C     . VAL A 1 207 ? 32.512  -22.768 8.317   1.00 53.07  ? 207 VAL A C     1 
ATOM   1628 O  O     . VAL A 1 207 ? 31.872  -21.883 7.735   1.00 44.96  ? 207 VAL A O     1 
ATOM   1629 C  CB    . VAL A 1 207 ? 34.600  -21.563 9.059   1.00 57.79  ? 207 VAL A CB    1 
ATOM   1630 C  CG1   . VAL A 1 207 ? 34.205  -21.639 10.528  1.00 54.81  ? 207 VAL A CG1   1 
ATOM   1631 C  CG2   . VAL A 1 207 ? 36.112  -21.499 8.909   1.00 51.37  ? 207 VAL A CG2   1 
ATOM   1632 N  N     . ASN A 1 208 ? 31.933  -23.765 8.991   1.00 48.31  ? 208 ASN A N     1 
ATOM   1633 C  CA    . ASN A 1 208 ? 30.481  -23.926 9.087   1.00 47.68  ? 208 ASN A CA    1 
ATOM   1634 C  C     . ASN A 1 208 ? 29.828  -24.013 7.709   1.00 48.99  ? 208 ASN A C     1 
ATOM   1635 O  O     . ASN A 1 208 ? 28.689  -23.576 7.526   1.00 47.96  ? 208 ASN A O     1 
ATOM   1636 C  CB    . ASN A 1 208 ? 29.844  -22.798 9.909   1.00 47.13  ? 208 ASN A CB    1 
ATOM   1637 C  CG    . ASN A 1 208 ? 30.006  -23.003 11.406  1.00 56.60  ? 208 ASN A CG    1 
ATOM   1638 O  OD1   . ASN A 1 208 ? 30.004  -24.133 11.892  1.00 62.47  ? 208 ASN A OD1   1 
ATOM   1639 N  ND2   . ASN A 1 208 ? 30.143  -21.905 12.145  1.00 58.08  ? 208 ASN A ND2   1 
ATOM   1640 N  N     . ASN A 1 209 ? 30.550  -24.575 6.735   1.00 46.82  ? 209 ASN A N     1 
ATOM   1641 C  CA    . ASN A 1 209 ? 30.075  -24.706 5.357   1.00 51.21  ? 209 ASN A CA    1 
ATOM   1642 C  C     . ASN A 1 209 ? 29.726  -23.352 4.743   1.00 44.65  ? 209 ASN A C     1 
ATOM   1643 O  O     . ASN A 1 209 ? 28.910  -23.268 3.821   1.00 45.23  ? 209 ASN A O     1 
ATOM   1644 C  CB    . ASN A 1 209 ? 28.871  -25.652 5.263   1.00 53.93  ? 209 ASN A CB    1 
ATOM   1645 C  CG    . ASN A 1 209 ? 29.195  -27.058 5.726   1.00 54.15  ? 209 ASN A CG    1 
ATOM   1646 O  OD1   . ASN A 1 209 ? 29.872  -27.812 5.029   1.00 62.17  ? 209 ASN A OD1   1 
ATOM   1647 N  ND2   . ASN A 1 209 ? 28.700  -27.423 6.904   1.00 58.14  ? 209 ASN A ND2   1 
ATOM   1648 N  N     . TRP A 1 210 ? 30.339  -22.281 5.241   1.00 40.46  ? 210 TRP A N     1 
ATOM   1649 C  CA    . TRP A 1 210 ? 30.008  -20.923 4.823   1.00 44.03  ? 210 TRP A CA    1 
ATOM   1650 C  C     . TRP A 1 210 ? 31.013  -20.463 3.774   1.00 40.87  ? 210 TRP A C     1 
ATOM   1651 O  O     . TRP A 1 210 ? 32.179  -20.206 4.091   1.00 35.67  ? 210 TRP A O     1 
ATOM   1652 C  CB    . TRP A 1 210 ? 29.991  -19.974 6.019   1.00 39.62  ? 210 TRP A CB    1 
ATOM   1653 C  CG    . TRP A 1 210 ? 29.408  -18.643 5.686   1.00 40.64  ? 210 TRP A CG    1 
ATOM   1654 C  CD1   . TRP A 1 210 ? 30.086  -17.475 5.494   1.00 37.03  ? 210 TRP A CD1   1 
ATOM   1655 C  CD2   . TRP A 1 210 ? 28.024  -18.343 5.485   1.00 37.55  ? 210 TRP A CD2   1 
ATOM   1656 N  NE1   . TRP A 1 210 ? 29.209  -16.463 5.198   1.00 36.02  ? 210 TRP A NE1   1 
ATOM   1657 C  CE2   . TRP A 1 210 ? 27.936  -16.970 5.183   1.00 40.85  ? 210 TRP A CE2   1 
ATOM   1658 C  CE3   . TRP A 1 210 ? 26.851  -19.102 5.532   1.00 39.93  ? 210 TRP A CE3   1 
ATOM   1659 C  CZ2   . TRP A 1 210 ? 26.720  -16.339 4.928   1.00 34.27  ? 210 TRP A CZ2   1 
ATOM   1660 C  CZ3   . TRP A 1 210 ? 25.646  -18.474 5.282   1.00 30.02  ? 210 TRP A CZ3   1 
ATOM   1661 C  CH2   . TRP A 1 210 ? 25.589  -17.106 4.985   1.00 31.83  ? 210 TRP A CH2   1 
ATOM   1662 N  N     . ALA A 1 211 ? 30.555  -20.351 2.530   1.00 32.03  ? 211 ALA A N     1 
ATOM   1663 C  CA    . ALA A 1 211 ? 31.408  -19.917 1.431   1.00 36.21  ? 211 ALA A CA    1 
ATOM   1664 C  C     . ALA A 1 211 ? 31.640  -18.414 1.526   1.00 40.31  ? 211 ALA A C     1 
ATOM   1665 O  O     . ALA A 1 211 ? 30.693  -17.626 1.430   1.00 38.42  ? 211 ALA A O     1 
ATOM   1666 C  CB    . ALA A 1 211 ? 30.775  -20.282 0.090   1.00 42.30  ? 211 ALA A CB    1 
ATOM   1667 N  N     . CYS A 1 212 ? 32.897  -18.017 1.710   1.00 36.07  ? 212 CYS A N     1 
ATOM   1668 C  CA    . CYS A 1 212 ? 33.249  -16.607 1.788   1.00 38.06  ? 212 CYS A CA    1 
ATOM   1669 C  C     . CYS A 1 212 ? 34.747  -16.468 1.559   1.00 43.96  ? 212 CYS A C     1 
ATOM   1670 O  O     . CYS A 1 212 ? 35.509  -17.425 1.720   1.00 37.66  ? 212 CYS A O     1 
ATOM   1671 C  CB    . CYS A 1 212 ? 32.852  -16.001 3.139   1.00 33.12  ? 212 CYS A CB    1 
ATOM   1672 S  SG    . CYS A 1 212 ? 33.849  -16.596 4.532   1.00 41.33  ? 212 CYS A SG    1 
ATOM   1673 N  N     . ASN A 1 213 ? 35.157  -15.256 1.189   1.00 40.74  ? 213 ASN A N     1 
ATOM   1674 C  CA    . ASN A 1 213 ? 36.559  -14.930 0.922   1.00 46.41  ? 213 ASN A CA    1 
ATOM   1675 C  C     . ASN A 1 213 ? 36.886  -13.643 1.668   1.00 41.55  ? 213 ASN A C     1 
ATOM   1676 O  O     . ASN A 1 213 ? 36.887  -12.552 1.080   1.00 45.05  ? 213 ASN A O     1 
ATOM   1677 C  CB    . ASN A 1 213 ? 36.814  -14.796 -0.580  1.00 48.46  ? 213 ASN A CB    1 
ATOM   1678 C  CG    . ASN A 1 213 ? 38.287  -14.821 -0.932  1.00 51.25  ? 213 ASN A CG    1 
ATOM   1679 O  OD1   . ASN A 1 213 ? 39.115  -14.225 -0.243  1.00 53.60  ? 213 ASN A OD1   1 
ATOM   1680 N  ND2   . ASN A 1 213 ? 38.623  -15.516 -2.012  1.00 50.59  ? 213 ASN A ND2   1 
ATOM   1681 N  N     . PRO A 1 214 ? 37.166  -13.732 2.972   1.00 46.20  ? 214 PRO A N     1 
ATOM   1682 C  CA    . PRO A 1 214 ? 37.381  -12.502 3.756   1.00 44.96  ? 214 PRO A CA    1 
ATOM   1683 C  C     . PRO A 1 214 ? 38.543  -11.659 3.262   1.00 48.43  ? 214 PRO A C     1 
ATOM   1684 O  O     . PRO A 1 214 ? 38.465  -10.425 3.301   1.00 50.56  ? 214 PRO A O     1 
ATOM   1685 C  CB    . PRO A 1 214 ? 37.630  -13.035 5.176   1.00 50.71  ? 214 PRO A CB    1 
ATOM   1686 C  CG    . PRO A 1 214 ? 37.041  -14.413 5.184   1.00 44.89  ? 214 PRO A CG    1 
ATOM   1687 C  CD    . PRO A 1 214 ? 37.259  -14.944 3.802   1.00 48.05  ? 214 PRO A CD    1 
ATOM   1688 N  N     . GLU A 1 215 ? 39.618  -12.295 2.786   1.00 46.91  ? 215 GLU A N     1 
ATOM   1689 C  CA    . GLU A 1 215 ? 40.798  -11.552 2.354   1.00 46.27  ? 215 GLU A CA    1 
ATOM   1690 C  C     . GLU A 1 215 ? 40.491  -10.609 1.197   1.00 50.98  ? 215 GLU A C     1 
ATOM   1691 O  O     . GLU A 1 215 ? 41.070  -9.520  1.116   1.00 46.08  ? 215 GLU A O     1 
ATOM   1692 C  CB    . GLU A 1 215 ? 41.909  -12.521 1.949   1.00 61.93  ? 215 GLU A CB    1 
ATOM   1693 C  CG    . GLU A 1 215 ? 42.346  -13.479 3.044   1.00 77.32  ? 215 GLU A CG    1 
ATOM   1694 C  CD    . GLU A 1 215 ? 43.461  -14.401 2.590   1.00 98.42  ? 215 GLU A CD    1 
ATOM   1695 O  OE1   . GLU A 1 215 ? 43.677  -14.513 1.364   1.00 99.46  ? 215 GLU A OE1   1 
ATOM   1696 O  OE2   . GLU A 1 215 ? 44.126  -15.008 3.456   1.00 104.89 ? 215 GLU A OE2   1 
ATOM   1697 N  N     . LEU A 1 216 ? 39.591  -11.003 0.296   1.00 41.97  ? 216 LEU A N     1 
ATOM   1698 C  CA    . LEU A 1 216 ? 39.336  -10.256 -0.927  1.00 45.11  ? 216 LEU A CA    1 
ATOM   1699 C  C     . LEU A 1 216 ? 38.015  -9.501  -0.898  1.00 43.17  ? 216 LEU A C     1 
ATOM   1700 O  O     . LEU A 1 216 ? 37.564  -9.028  -1.948  1.00 42.56  ? 216 LEU A O     1 
ATOM   1701 C  CB    . LEU A 1 216 ? 39.364  -11.197 -2.133  1.00 49.65  ? 216 LEU A CB    1 
ATOM   1702 C  CG    . LEU A 1 216 ? 40.694  -11.884 -2.440  1.00 43.72  ? 216 LEU A CG    1 
ATOM   1703 C  CD1   . LEU A 1 216 ? 40.546  -12.818 -3.633  1.00 45.28  ? 216 LEU A CD1   1 
ATOM   1704 C  CD2   . LEU A 1 216 ? 41.776  -10.849 -2.696  1.00 45.85  ? 216 LEU A CD2   1 
ATOM   1705 N  N     . THR A 1 217 ? 37.392  -9.367  0.272   1.00 39.64  ? 217 THR A N     1 
ATOM   1706 C  CA    . THR A 1 217 ? 36.067  -8.764  0.354   1.00 39.88  ? 217 THR A CA    1 
ATOM   1707 C  C     . THR A 1 217 ? 36.094  -7.316  -0.119  1.00 38.22  ? 217 THR A C     1 
ATOM   1708 O  O     . THR A 1 217 ? 36.902  -6.508  0.346   1.00 37.32  ? 217 THR A O     1 
ATOM   1709 C  CB    . THR A 1 217 ? 35.537  -8.840  1.786   1.00 40.76  ? 217 THR A CB    1 
ATOM   1710 O  OG1   . THR A 1 217 ? 35.440  -10.212 2.187   1.00 41.00  ? 217 THR A OG1   1 
ATOM   1711 C  CG2   . THR A 1 217 ? 34.158  -8.197  1.877   1.00 36.91  ? 217 THR A CG2   1 
ATOM   1712 N  N     . LEU A 1 218 ? 35.198  -6.991  -1.049  1.00 35.06  ? 218 LEU A N     1 
ATOM   1713 C  CA    . LEU A 1 218 ? 35.102  -5.640  -1.587  1.00 32.00  ? 218 LEU A CA    1 
ATOM   1714 C  C     . LEU A 1 218 ? 33.667  -5.402  -2.030  1.00 36.83  ? 218 LEU A C     1 
ATOM   1715 O  O     . LEU A 1 218 ? 33.136  -6.161  -2.847  1.00 32.42  ? 218 LEU A O     1 
ATOM   1716 C  CB    . LEU A 1 218 ? 36.072  -5.444  -2.755  1.00 33.42  ? 218 LEU A CB    1 
ATOM   1717 C  CG    . LEU A 1 218 ? 36.245  -4.016  -3.280  1.00 35.50  ? 218 LEU A CG    1 
ATOM   1718 C  CD1   . LEU A 1 218 ? 36.822  -3.115  -2.201  1.00 40.65  ? 218 LEU A CD1   1 
ATOM   1719 C  CD2   . LEU A 1 218 ? 37.127  -4.005  -4.517  1.00 42.71  ? 218 LEU A CD2   1 
ATOM   1720 N  N     . ILE A 1 219 ? 33.043  -4.364  -1.481  1.00 31.00  ? 219 ILE A N     1 
ATOM   1721 C  CA    . ILE A 1 219 ? 31.695  -3.955  -1.859  1.00 34.31  ? 219 ILE A CA    1 
ATOM   1722 C  C     . ILE A 1 219 ? 31.831  -2.604  -2.547  1.00 39.69  ? 219 ILE A C     1 
ATOM   1723 O  O     . ILE A 1 219 ? 32.187  -1.604  -1.910  1.00 36.45  ? 219 ILE A O     1 
ATOM   1724 C  CB    . ILE A 1 219 ? 30.749  -3.885  -0.651  1.00 30.35  ? 219 ILE A CB    1 
ATOM   1725 C  CG1   . ILE A 1 219 ? 30.711  -5.225  0.091   1.00 36.58  ? 219 ILE A CG1   1 
ATOM   1726 C  CG2   . ILE A 1 219 ? 29.345  -3.510  -1.097  1.00 31.94  ? 219 ILE A CG2   1 
ATOM   1727 C  CD1   . ILE A 1 219 ? 31.726  -5.353  1.220   1.00 32.99  ? 219 ILE A CD1   1 
ATOM   1728 N  N     . ALA A 1 220 ? 31.569  -2.574  -3.850  1.00 30.89  ? 220 ALA A N     1 
ATOM   1729 C  CA    . ALA A 1 220 ? 31.840  -1.407  -4.674  1.00 32.24  ? 220 ALA A CA    1 
ATOM   1730 C  C     . ALA A 1 220 ? 30.555  -0.870  -5.289  1.00 32.57  ? 220 ALA A C     1 
ATOM   1731 O  O     . ALA A 1 220 ? 29.642  -1.628  -5.629  1.00 30.44  ? 220 ALA A O     1 
ATOM   1732 C  CB    . ALA A 1 220 ? 32.842  -1.736  -5.785  1.00 31.22  ? 220 ALA A CB    1 
ATOM   1733 N  N     . HIS A 1 221 ? 30.508  0.452   -5.443  1.00 31.04  ? 221 HIS A N     1 
ATOM   1734 C  CA    . HIS A 1 221 ? 29.356  1.145   -5.999  1.00 31.77  ? 221 HIS A CA    1 
ATOM   1735 C  C     . HIS A 1 221 ? 29.823  2.052   -7.124  1.00 35.15  ? 221 HIS A C     1 
ATOM   1736 O  O     . HIS A 1 221 ? 30.784  2.810   -6.957  1.00 36.51  ? 221 HIS A O     1 
ATOM   1737 C  CB    . HIS A 1 221 ? 28.632  1.962   -4.924  1.00 30.64  ? 221 HIS A CB    1 
ATOM   1738 C  CG    . HIS A 1 221 ? 28.236  1.160   -3.724  1.00 32.76  ? 221 HIS A CG    1 
ATOM   1739 N  ND1   . HIS A 1 221 ? 29.148  0.719   -2.789  1.00 31.05  ? 221 HIS A ND1   1 
ATOM   1740 C  CD2   . HIS A 1 221 ? 27.026  0.719   -3.307  1.00 26.77  ? 221 HIS A CD2   1 
ATOM   1741 C  CE1   . HIS A 1 221 ? 28.516  0.044   -1.845  1.00 31.01  ? 221 HIS A CE1   1 
ATOM   1742 N  NE2   . HIS A 1 221 ? 27.227  0.027   -2.137  1.00 28.65  ? 221 HIS A NE2   1 
ATOM   1743 N  N     . LEU A 1 222 ? 29.150  1.965   -8.274  1.00 34.78  ? 222 LEU A N     1 
ATOM   1744 C  CA    . LEU A 1 222 ? 29.449  2.789   -9.444  1.00 36.83  ? 222 LEU A CA    1 
ATOM   1745 C  C     . LEU A 1 222 ? 28.171  3.522   -9.835  1.00 41.88  ? 222 LEU A C     1 
ATOM   1746 O  O     . LEU A 1 222 ? 27.460  3.105   -10.763 1.00 40.52  ? 222 LEU A O     1 
ATOM   1747 C  CB    . LEU A 1 222 ? 29.993  1.950   -10.600 1.00 40.31  ? 222 LEU A CB    1 
ATOM   1748 C  CG    . LEU A 1 222 ? 31.377  1.319   -10.401 1.00 45.82  ? 222 LEU A CG    1 
ATOM   1749 C  CD1   . LEU A 1 222 ? 31.285  -0.020  -9.674  1.00 42.27  ? 222 LEU A CD1   1 
ATOM   1750 C  CD2   . LEU A 1 222 ? 32.105  1.165   -11.728 1.00 43.28  ? 222 LEU A CD2   1 
ATOM   1751 N  N     . PRO A 1 223 ? 27.853  4.625   -9.154  1.00 40.98  ? 223 PRO A N     1 
ATOM   1752 C  CA    . PRO A 1 223 ? 26.580  5.312   -9.426  1.00 43.73  ? 223 PRO A CA    1 
ATOM   1753 C  C     . PRO A 1 223 ? 26.450  5.814   -10.851 1.00 54.15  ? 223 PRO A C     1 
ATOM   1754 O  O     . PRO A 1 223 ? 25.337  5.818   -11.394 1.00 54.20  ? 223 PRO A O     1 
ATOM   1755 C  CB    . PRO A 1 223 ? 26.587  6.469   -8.416  1.00 45.11  ? 223 PRO A CB    1 
ATOM   1756 C  CG    . PRO A 1 223 ? 28.035  6.693   -8.106  1.00 44.67  ? 223 PRO A CG    1 
ATOM   1757 C  CD    . PRO A 1 223 ? 28.664  5.331   -8.147  1.00 39.44  ? 223 PRO A CD    1 
ATOM   1758 N  N     . ASP A 1 224 ? 27.552  6.232   -11.480 1.00 50.57  ? 224 ASP A N     1 
ATOM   1759 C  CA    . ASP A 1 224 ? 27.482  6.690   -12.864 1.00 56.87  ? 224 ASP A CA    1 
ATOM   1760 C  C     . ASP A 1 224 ? 27.076  5.564   -13.806 1.00 53.84  ? 224 ASP A C     1 
ATOM   1761 O  O     . ASP A 1 224 ? 26.456  5.818   -14.845 1.00 62.03  ? 224 ASP A O     1 
ATOM   1762 C  CB    . ASP A 1 224 ? 28.824  7.284   -13.292 1.00 67.46  ? 224 ASP A CB    1 
ATOM   1763 C  CG    . ASP A 1 224 ? 29.219  8.491   -12.462 1.00 68.29  ? 224 ASP A CG    1 
ATOM   1764 O  OD1   . ASP A 1 224 ? 28.320  9.131   -11.880 1.00 62.48  ? 224 ASP A OD1   1 
ATOM   1765 O  OD2   . ASP A 1 224 ? 30.427  8.803   -12.396 1.00 73.36  ? 224 ASP A OD2   1 
ATOM   1766 N  N     . ARG A 1 225 ? 27.409  4.322   -13.464 1.00 51.42  ? 225 ARG A N     1 
ATOM   1767 C  CA    . ARG A 1 225 ? 27.057  3.162   -14.272 1.00 52.67  ? 225 ARG A CA    1 
ATOM   1768 C  C     . ARG A 1 225 ? 25.875  2.382   -13.709 1.00 49.94  ? 225 ARG A C     1 
ATOM   1769 O  O     . ARG A 1 225 ? 25.483  1.372   -14.303 1.00 48.26  ? 225 ARG A O     1 
ATOM   1770 C  CB    . ARG A 1 225 ? 28.270  2.236   -14.416 1.00 53.00  ? 225 ARG A CB    1 
ATOM   1771 C  CG    . ARG A 1 225 ? 29.324  2.745   -15.392 1.00 65.73  ? 225 ARG A CG    1 
ATOM   1772 C  CD    . ARG A 1 225 ? 30.715  2.228   -15.048 1.00 66.94  ? 225 ARG A CD    1 
ATOM   1773 N  NE    . ARG A 1 225 ? 30.773  0.773   -14.982 1.00 68.95  ? 225 ARG A NE    1 
ATOM   1774 C  CZ    . ARG A 1 225 ? 31.181  -0.008  -15.974 1.00 78.53  ? 225 ARG A CZ    1 
ATOM   1775 N  NH1   . ARG A 1 225 ? 31.569  0.495   -17.135 1.00 79.20  ? 225 ARG A NH1   1 
ATOM   1776 N  NH2   . ARG A 1 225 ? 31.205  -1.326  -15.795 1.00 67.25  ? 225 ARG A NH2   1 
ATOM   1777 N  N     . ARG A 1 226 ? 25.301  2.829   -12.589 1.00 43.59  ? 226 ARG A N     1 
ATOM   1778 C  CA    . ARG A 1 226 ? 24.183  2.144   -11.934 1.00 46.99  ? 226 ARG A CA    1 
ATOM   1779 C  C     . ARG A 1 226 ? 24.522  0.686   -11.637 1.00 42.77  ? 226 ARG A C     1 
ATOM   1780 O  O     . ARG A 1 226 ? 23.687  -0.210  -11.778 1.00 42.99  ? 226 ARG A O     1 
ATOM   1781 C  CB    . ARG A 1 226 ? 22.901  2.241   -12.766 1.00 50.76  ? 226 ARG A CB    1 
ATOM   1782 C  CG    . ARG A 1 226 ? 22.154  3.565   -12.650 1.00 57.97  ? 226 ARG A CG    1 
ATOM   1783 C  CD    . ARG A 1 226 ? 22.737  4.626   -13.567 1.00 67.90  ? 226 ARG A CD    1 
ATOM   1784 N  NE    . ARG A 1 226 ? 21.894  5.814   -13.634 1.00 73.51  ? 226 ARG A NE    1 
ATOM   1785 C  CZ    . ARG A 1 226 ? 22.012  6.865   -12.833 1.00 68.14  ? 226 ARG A CZ    1 
ATOM   1786 N  NH1   . ARG A 1 226 ? 22.930  6.909   -11.882 1.00 58.47  ? 226 ARG A NH1   1 
ATOM   1787 N  NH2   . ARG A 1 226 ? 21.189  7.898   -12.993 1.00 62.40  ? 226 ARG A NH2   1 
ATOM   1788 N  N     . GLU A 1 227 ? 25.761  0.443   -11.221 1.00 39.95  ? 227 GLU A N     1 
ATOM   1789 C  CA    . GLU A 1 227 ? 26.251  -0.902  -10.960 1.00 40.49  ? 227 GLU A CA    1 
ATOM   1790 C  C     . GLU A 1 227 ? 26.659  -1.044  -9.502  1.00 31.71  ? 227 GLU A C     1 
ATOM   1791 O  O     . GLU A 1 227 ? 27.278  -0.142  -8.927  1.00 36.66  ? 227 GLU A O     1 
ATOM   1792 C  CB    . GLU A 1 227 ? 27.446  -1.250  -11.855 1.00 37.69  ? 227 GLU A CB    1 
ATOM   1793 C  CG    . GLU A 1 227 ? 27.118  -1.363  -13.331 1.00 50.23  ? 227 GLU A CG    1 
ATOM   1794 C  CD    . GLU A 1 227 ? 28.316  -1.787  -14.157 1.00 49.83  ? 227 GLU A CD    1 
ATOM   1795 O  OE1   . GLU A 1 227 ? 29.370  -2.098  -13.563 1.00 51.65  ? 227 GLU A OE1   1 
ATOM   1796 O  OE2   . GLU A 1 227 ? 28.204  -1.809  -15.399 1.00 62.70  ? 227 GLU A OE2   1 
ATOM   1797 N  N     . ILE A 1 228 ? 26.309  -2.184  -8.915  1.00 32.83  ? 228 ILE A N     1 
ATOM   1798 C  CA    . ILE A 1 228 ? 26.774  -2.589  -7.595  1.00 29.00  ? 228 ILE A CA    1 
ATOM   1799 C  C     . ILE A 1 228 ? 27.503  -3.914  -7.764  1.00 34.22  ? 228 ILE A C     1 
ATOM   1800 O  O     . ILE A 1 228 ? 26.961  -4.851  -8.361  1.00 27.11  ? 228 ILE A O     1 
ATOM   1801 C  CB    . ILE A 1 228 ? 25.612  -2.722  -6.594  1.00 29.60  ? 228 ILE A CB    1 
ATOM   1802 C  CG1   . ILE A 1 228 ? 24.886  -1.386  -6.440  1.00 32.73  ? 228 ILE A CG1   1 
ATOM   1803 C  CG2   . ILE A 1 228 ? 26.113  -3.217  -5.248  1.00 29.22  ? 228 ILE A CG2   1 
ATOM   1804 C  CD1   . ILE A 1 228 ? 23.608  -1.478  -5.634  1.00 24.77  ? 228 ILE A CD1   1 
ATOM   1805 N  N     . ILE A 1 229 ? 28.730  -3.985  -7.256  1.00 25.23  ? 229 ILE A N     1 
ATOM   1806 C  CA    . ILE A 1 229 ? 29.609  -5.131  -7.465  1.00 26.70  ? 229 ILE A CA    1 
ATOM   1807 C  C     . ILE A 1 229 ? 30.159  -5.543  -6.106  1.00 33.69  ? 229 ILE A C     1 
ATOM   1808 O  O     . ILE A 1 229 ? 30.926  -4.792  -5.489  1.00 33.01  ? 229 ILE A O     1 
ATOM   1809 C  CB    . ILE A 1 229 ? 30.744  -4.815  -8.449  1.00 35.03  ? 229 ILE A CB    1 
ATOM   1810 C  CG1   . ILE A 1 229 ? 30.173  -4.389  -9.803  1.00 30.90  ? 229 ILE A CG1   1 
ATOM   1811 C  CG2   . ILE A 1 229 ? 31.642  -6.014  -8.632  1.00 30.86  ? 229 ILE A CG2   1 
ATOM   1812 C  CD1   . ILE A 1 229 ? 31.228  -4.042  -10.826 1.00 38.12  ? 229 ILE A CD1   1 
ATOM   1813 N  N     . SER A 1 230 ? 29.773  -6.728  -5.638  1.00 29.96  ? 230 SER A N     1 
ATOM   1814 C  CA    . SER A 1 230 ? 30.110  -7.192  -4.300  1.00 33.83  ? 230 SER A CA    1 
ATOM   1815 C  C     . SER A 1 230 ? 30.772  -8.558  -4.380  1.00 31.60  ? 230 SER A C     1 
ATOM   1816 O  O     . SER A 1 230 ? 30.309  -9.439  -5.110  1.00 35.16  ? 230 SER A O     1 
ATOM   1817 C  CB    . SER A 1 230 ? 28.862  -7.262  -3.409  1.00 30.75  ? 230 SER A CB    1 
ATOM   1818 O  OG    . SER A 1 230 ? 29.211  -7.527  -2.063  1.00 30.74  ? 230 SER A OG    1 
ATOM   1819 N  N     . PHE A 1 231 ? 31.846  -8.737  -3.611  1.00 28.02  ? 231 PHE A N     1 
ATOM   1820 C  CA    . PHE A 1 231 ? 32.682  -9.927  -3.705  1.00 29.79  ? 231 PHE A CA    1 
ATOM   1821 C  C     . PHE A 1 231 ? 33.154  -10.342 -2.321  1.00 36.58  ? 231 PHE A C     1 
ATOM   1822 O  O     . PHE A 1 231 ? 33.620  -9.502  -1.546  1.00 34.14  ? 231 PHE A O     1 
ATOM   1823 C  CB    . PHE A 1 231 ? 33.891  -9.666  -4.614  1.00 32.77  ? 231 PHE A CB    1 
ATOM   1824 C  CG    . PHE A 1 231 ? 34.742  -10.879 -4.870  1.00 35.33  ? 231 PHE A CG    1 
ATOM   1825 C  CD1   . PHE A 1 231 ? 34.468  -11.721 -5.935  1.00 33.15  ? 231 PHE A CD1   1 
ATOM   1826 C  CD2   . PHE A 1 231 ? 35.827  -11.168 -4.057  1.00 31.96  ? 231 PHE A CD2   1 
ATOM   1827 C  CE1   . PHE A 1 231 ? 35.253  -12.831 -6.178  1.00 39.77  ? 231 PHE A CE1   1 
ATOM   1828 C  CE2   . PHE A 1 231 ? 36.613  -12.277 -4.294  1.00 36.74  ? 231 PHE A CE2   1 
ATOM   1829 C  CZ    . PHE A 1 231 ? 36.330  -13.107 -5.356  1.00 36.45  ? 231 PHE A CZ    1 
ATOM   1830 N  N     . GLY A 1 232 ? 33.027  -11.634 -2.013  1.00 35.25  ? 232 GLY A N     1 
ATOM   1831 C  CA    . GLY A 1 232 ? 33.692  -12.235 -0.879  1.00 38.79  ? 232 GLY A CA    1 
ATOM   1832 C  C     . GLY A 1 232 ? 32.849  -12.404 0.371   1.00 36.85  ? 232 GLY A C     1 
ATOM   1833 O  O     . GLY A 1 232 ? 33.221  -13.201 1.238   1.00 39.93  ? 232 GLY A O     1 
ATOM   1834 N  N     . SER A 1 233 ? 31.737  -11.686 0.497   1.00 36.55  ? 233 SER A N     1 
ATOM   1835 C  CA    . SER A 1 233 ? 30.950  -11.693 1.722   1.00 32.59  ? 233 SER A CA    1 
ATOM   1836 C  C     . SER A 1 233 ? 29.542  -12.207 1.459   1.00 37.57  ? 233 SER A C     1 
ATOM   1837 O  O     . SER A 1 233 ? 28.950  -11.930 0.411   1.00 33.72  ? 233 SER A O     1 
ATOM   1838 C  CB    . SER A 1 233 ? 30.878  -10.297 2.341   1.00 32.66  ? 233 SER A CB    1 
ATOM   1839 O  OG    . SER A 1 233 ? 29.956  -10.270 3.416   1.00 35.35  ? 233 SER A OG    1 
ATOM   1840 N  N     . GLY A 1 234 ? 29.009  -12.950 2.427   1.00 35.62  ? 234 GLY A N     1 
ATOM   1841 C  CA    . GLY A 1 234 ? 27.654  -13.452 2.351   1.00 31.29  ? 234 GLY A CA    1 
ATOM   1842 C  C     . GLY A 1 234 ? 26.711  -12.772 3.322   1.00 32.23  ? 234 GLY A C     1 
ATOM   1843 O  O     . GLY A 1 234 ? 25.492  -12.944 3.223   1.00 36.34  ? 234 GLY A O     1 
ATOM   1844 N  N     . TYR A 1 235 ? 27.258  -12.003 4.265   1.00 34.29  ? 235 TYR A N     1 
ATOM   1845 C  CA    . TYR A 1 235 ? 26.430  -11.318 5.249   1.00 34.30  ? 235 TYR A CA    1 
ATOM   1846 C  C     . TYR A 1 235 ? 25.475  -10.344 4.564   1.00 30.63  ? 235 TYR A C     1 
ATOM   1847 O  O     . TYR A 1 235 ? 25.801  -9.737  3.539   1.00 38.18  ? 235 TYR A O     1 
ATOM   1848 C  CB    . TYR A 1 235 ? 27.302  -10.582 6.272   1.00 32.26  ? 235 TYR A CB    1 
ATOM   1849 C  CG    . TYR A 1 235 ? 26.518  -9.654  7.176   1.00 30.67  ? 235 TYR A CG    1 
ATOM   1850 C  CD1   . TYR A 1 235 ? 25.818  -10.143 8.272   1.00 32.95  ? 235 TYR A CD1   1 
ATOM   1851 C  CD2   . TYR A 1 235 ? 26.469  -8.286  6.923   1.00 34.98  ? 235 TYR A CD2   1 
ATOM   1852 C  CE1   . TYR A 1 235 ? 25.091  -9.293  9.094   1.00 36.33  ? 235 TYR A CE1   1 
ATOM   1853 C  CE2   . TYR A 1 235 ? 25.746  -7.430  7.735   1.00 35.52  ? 235 TYR A CE2   1 
ATOM   1854 C  CZ    . TYR A 1 235 ? 25.058  -7.936  8.818   1.00 37.46  ? 235 TYR A CZ    1 
ATOM   1855 O  OH    . TYR A 1 235 ? 24.340  -7.082  9.626   1.00 34.55  ? 235 TYR A OH    1 
ATOM   1856 N  N     . GLY A 1 236 ? 24.293  -10.183 5.167   1.00 27.24  ? 236 GLY A N     1 
ATOM   1857 C  CA    . GLY A 1 236 ? 23.183  -9.542  4.472   1.00 38.76  ? 236 GLY A CA    1 
ATOM   1858 C  C     . GLY A 1 236 ? 23.487  -8.136  3.989   1.00 34.74  ? 236 GLY A C     1 
ATOM   1859 O  O     . GLY A 1 236 ? 23.155  -7.777  2.857   1.00 32.56  ? 236 GLY A O     1 
ATOM   1860 N  N     . GLY A 1 237 ? 24.109  -7.317  4.839   1.00 25.54  ? 237 GLY A N     1 
ATOM   1861 C  CA    . GLY A 1 237 ? 24.432  -5.955  4.444   1.00 26.14  ? 237 GLY A CA    1 
ATOM   1862 C  C     . GLY A 1 237 ? 25.373  -5.861  3.259   1.00 31.66  ? 237 GLY A C     1 
ATOM   1863 O  O     . GLY A 1 237 ? 25.371  -4.846  2.552   1.00 29.80  ? 237 GLY A O     1 
ATOM   1864 N  N     . ASN A 1 238 ? 26.175  -6.899  3.020   1.00 31.27  ? 238 ASN A N     1 
ATOM   1865 C  CA    . ASN A 1 238 ? 27.107  -6.922  1.902   1.00 28.92  ? 238 ASN A CA    1 
ATOM   1866 C  C     . ASN A 1 238 ? 26.575  -7.662  0.680   1.00 33.80  ? 238 ASN A C     1 
ATOM   1867 O  O     . ASN A 1 238 ? 27.067  -7.423  -0.428  1.00 32.64  ? 238 ASN A O     1 
ATOM   1868 C  CB    . ASN A 1 238 ? 28.428  -7.578  2.322   1.00 29.98  ? 238 ASN A CB    1 
ATOM   1869 C  CG    . ASN A 1 238 ? 29.074  -6.895  3.515   1.00 34.57  ? 238 ASN A CG    1 
ATOM   1870 O  OD1   . ASN A 1 238 ? 28.916  -5.692  3.720   1.00 36.94  ? 238 ASN A OD1   1 
ATOM   1871 N  ND2   . ASN A 1 238 ? 29.817  -7.666  4.303   1.00 33.17  ? 238 ASN A ND2   1 
ATOM   1872 N  N     . SER A 1 239 ? 25.606  -8.561  0.854   1.00 28.12  ? 239 SER A N     1 
ATOM   1873 C  CA    . SER A 1 239 ? 25.187  -9.461  -0.211  1.00 27.07  ? 239 SER A CA    1 
ATOM   1874 C  C     . SER A 1 239 ? 23.775  -9.210  -0.711  1.00 30.06  ? 239 SER A C     1 
ATOM   1875 O  O     . SER A 1 239 ? 23.473  -9.547  -1.859  1.00 28.75  ? 239 SER A O     1 
ATOM   1876 C  CB    . SER A 1 239 ? 25.288  -10.920 0.256   1.00 25.39  ? 239 SER A CB    1 
ATOM   1877 O  OG    . SER A 1 239 ? 24.389  -11.173 1.326   1.00 26.55  ? 239 SER A OG    1 
ATOM   1878 N  N     . LEU A 1 240 ? 22.903  -8.650  0.122   1.00 29.14  ? 240 LEU A N     1 
ATOM   1879 C  CA    . LEU A 1 240 ? 21.555  -8.268  -0.291  1.00 32.13  ? 240 LEU A CA    1 
ATOM   1880 C  C     . LEU A 1 240 ? 21.665  -6.870  -0.880  1.00 29.08  ? 240 LEU A C     1 
ATOM   1881 O  O     . LEU A 1 240 ? 21.466  -5.864  -0.198  1.00 32.61  ? 240 LEU A O     1 
ATOM   1882 C  CB    . LEU A 1 240 ? 20.591  -8.335  0.888   1.00 39.88  ? 240 LEU A CB    1 
ATOM   1883 C  CG    . LEU A 1 240 ? 20.687  -9.593  1.759   1.00 35.07  ? 240 LEU A CG    1 
ATOM   1884 C  CD1   . LEU A 1 240 ? 19.638  -9.560  2.859   1.00 30.47  ? 240 LEU A CD1   1 
ATOM   1885 C  CD2   . LEU A 1 240 ? 20.558  -10.859 0.920   1.00 31.08  ? 240 LEU A CD2   1 
ATOM   1886 N  N     . LEU A 1 241 ? 21.999  -6.807  -2.169  1.00 26.34  ? 241 LEU A N     1 
ATOM   1887 C  CA    . LEU A 1 241 ? 22.429  -5.548  -2.764  1.00 28.95  ? 241 LEU A CA    1 
ATOM   1888 C  C     . LEU A 1 241 ? 21.289  -4.557  -2.955  1.00 30.81  ? 241 LEU A C     1 
ATOM   1889 O  O     . LEU A 1 241 ? 21.554  -3.373  -3.181  1.00 29.71  ? 241 LEU A O     1 
ATOM   1890 C  CB    . LEU A 1 241 ? 23.129  -5.820  -4.095  1.00 23.09  ? 241 LEU A CB    1 
ATOM   1891 C  CG    . LEU A 1 241 ? 24.337  -6.747  -3.944  1.00 27.29  ? 241 LEU A CG    1 
ATOM   1892 C  CD1   . LEU A 1 241 ? 25.074  -6.932  -5.262  1.00 26.82  ? 241 LEU A CD1   1 
ATOM   1893 C  CD2   . LEU A 1 241 ? 25.280  -6.219  -2.865  1.00 25.57  ? 241 LEU A CD2   1 
ATOM   1894 N  N     . GLY A 1 242 ? 20.034  -5.001  -2.867  1.00 29.36  ? 242 GLY A N     1 
ATOM   1895 C  CA    . GLY A 1 242 ? 18.926  -4.065  -2.943  1.00 28.54  ? 242 GLY A CA    1 
ATOM   1896 C  C     . GLY A 1 242 ? 18.786  -3.171  -1.724  1.00 31.33  ? 242 GLY A C     1 
ATOM   1897 O  O     . GLY A 1 242 ? 18.167  -2.106  -1.819  1.00 33.34  ? 242 GLY A O     1 
ATOM   1898 N  N     . LYS A 1 243 ? 19.370  -3.566  -0.592  1.00 24.51  ? 243 LYS A N     1 
ATOM   1899 C  CA    . LYS A 1 243 ? 19.100  -2.921  0.688   1.00 23.17  ? 243 LYS A CA    1 
ATOM   1900 C  C     . LYS A 1 243 ? 19.983  -1.698  0.918   1.00 32.33  ? 243 LYS A C     1 
ATOM   1901 O  O     . LYS A 1 243 ? 19.617  -0.583  0.529   1.00 30.18  ? 243 LYS A O     1 
ATOM   1902 C  CB    . LYS A 1 243 ? 19.277  -3.935  1.823   1.00 28.27  ? 243 LYS A CB    1 
ATOM   1903 C  CG    . LYS A 1 243 ? 18.837  -3.450  3.198   1.00 26.53  ? 243 LYS A CG    1 
ATOM   1904 C  CD    . LYS A 1 243 ? 18.790  -4.609  4.189   1.00 28.89  ? 243 LYS A CD    1 
ATOM   1905 C  CE    . LYS A 1 243 ? 18.566  -4.128  5.615   1.00 23.38  ? 243 LYS A CE    1 
ATOM   1906 N  NZ    . LYS A 1 243 ? 17.205  -3.544  5.831   1.00 21.55  ? 243 LYS A NZ    1 
ATOM   1907 N  N     . LYS A 1 244 ? 21.137  -1.889  1.566   1.00 22.83  ? 244 LYS A N     1 
ATOM   1908 C  CA    . LYS A 1 244 ? 22.021  -0.762  1.853   1.00 24.83  ? 244 LYS A CA    1 
ATOM   1909 C  C     . LYS A 1 244 ? 22.669  -0.222  0.584   1.00 26.22  ? 244 LYS A C     1 
ATOM   1910 O  O     . LYS A 1 244 ? 22.723  0.995   0.377   1.00 26.56  ? 244 LYS A O     1 
ATOM   1911 C  CB    . LYS A 1 244 ? 23.102  -1.181  2.850   1.00 21.96  ? 244 LYS A CB    1 
ATOM   1912 C  CG    . LYS A 1 244 ? 22.573  -1.738  4.150   1.00 20.82  ? 244 LYS A CG    1 
ATOM   1913 C  CD    . LYS A 1 244 ? 21.827  -0.672  4.932   1.00 27.49  ? 244 LYS A CD    1 
ATOM   1914 C  CE    . LYS A 1 244 ? 21.561  -1.131  6.353   1.00 25.92  ? 244 LYS A CE    1 
ATOM   1915 N  NZ    . LYS A 1 244 ? 20.830  -0.108  7.152   1.00 22.18  ? 244 LYS A NZ    1 
ATOM   1916 N  N     . CYS A 1 245 ? 23.170  -1.114  -0.270  1.00 26.39  ? 245 CYS A N     1 
ATOM   1917 C  CA    . CYS A 1 245 ? 23.915  -0.693  -1.452  1.00 23.23  ? 245 CYS A CA    1 
ATOM   1918 C  C     . CYS A 1 245 ? 23.024  0.062   -2.432  1.00 30.68  ? 245 CYS A C     1 
ATOM   1919 O  O     . CYS A 1 245 ? 23.391  1.136   -2.922  1.00 29.03  ? 245 CYS A O     1 
ATOM   1920 C  CB    . CYS A 1 245 ? 24.545  -1.915  -2.121  1.00 29.16  ? 245 CYS A CB    1 
ATOM   1921 S  SG    . CYS A 1 245 ? 25.742  -2.794  -1.079  1.00 30.69  ? 245 CYS A SG    1 
ATOM   1922 N  N     . PHE A 1 246 ? 21.848  -0.489  -2.727  1.00 26.09  ? 246 PHE A N     1 
ATOM   1923 C  CA    . PHE A 1 246 ? 20.930  0.133   -3.674  1.00 30.51  ? 246 PHE A CA    1 
ATOM   1924 C  C     . PHE A 1 246 ? 20.076  1.198   -2.991  1.00 27.62  ? 246 PHE A C     1 
ATOM   1925 O  O     . PHE A 1 246 ? 20.168  2.385   -3.319  1.00 31.54  ? 246 PHE A O     1 
ATOM   1926 C  CB    . PHE A 1 246 ? 20.066  -0.960  -4.319  1.00 27.79  ? 246 PHE A CB    1 
ATOM   1927 C  CG    . PHE A 1 246 ? 19.058  -0.468  -5.332  1.00 40.90  ? 246 PHE A CG    1 
ATOM   1928 C  CD1   . PHE A 1 246 ? 19.039  0.846   -5.776  1.00 39.59  ? 246 PHE A CD1   1 
ATOM   1929 C  CD2   . PHE A 1 246 ? 18.120  -1.352  -5.843  1.00 43.17  ? 246 PHE A CD2   1 
ATOM   1930 C  CE1   . PHE A 1 246 ? 18.102  1.268   -6.692  1.00 50.71  ? 246 PHE A CE1   1 
ATOM   1931 C  CE2   . PHE A 1 246 ? 17.186  -0.937  -6.765  1.00 46.52  ? 246 PHE A CE2   1 
ATOM   1932 C  CZ    . PHE A 1 246 ? 17.178  0.372   -7.188  1.00 50.57  ? 246 PHE A CZ    1 
ATOM   1933 N  N     . ALA A 1 247 ? 19.237  0.789   -2.038  1.00 27.64  ? 247 ALA A N     1 
ATOM   1934 C  CA    . ALA A 1 247 ? 18.204  1.678   -1.515  1.00 29.98  ? 247 ALA A CA    1 
ATOM   1935 C  C     . ALA A 1 247 ? 18.750  2.813   -0.656  1.00 29.94  ? 247 ALA A C     1 
ATOM   1936 O  O     . ALA A 1 247 ? 17.999  3.749   -0.363  1.00 31.06  ? 247 ALA A O     1 
ATOM   1937 C  CB    . ALA A 1 247 ? 17.173  0.875   -0.718  1.00 25.93  ? 247 ALA A CB    1 
ATOM   1938 N  N     . LEU A 1 248 ? 20.020  2.768   -0.251  1.00 29.05  ? 248 LEU A N     1 
ATOM   1939 C  CA    . LEU A 1 248 ? 20.624  3.869   0.489   1.00 27.42  ? 248 LEU A CA    1 
ATOM   1940 C  C     . LEU A 1 248 ? 21.759  4.537   -0.281  1.00 28.37  ? 248 LEU A C     1 
ATOM   1941 O  O     . LEU A 1 248 ? 21.671  5.725   -0.590  1.00 33.93  ? 248 LEU A O     1 
ATOM   1942 C  CB    . LEU A 1 248 ? 21.108  3.385   1.863   1.00 25.79  ? 248 LEU A CB    1 
ATOM   1943 C  CG    . LEU A 1 248 ? 20.021  3.322   2.944   1.00 25.08  ? 248 LEU A CG    1 
ATOM   1944 C  CD1   . LEU A 1 248 ? 20.559  2.740   4.238   1.00 22.91  ? 248 LEU A CD1   1 
ATOM   1945 C  CD2   . LEU A 1 248 ? 19.428  4.705   3.189   1.00 27.09  ? 248 LEU A CD2   1 
ATOM   1946 N  N     . ARG A 1 249 ? 22.827  3.811   -0.610  1.00 26.34  ? 249 ARG A N     1 
ATOM   1947 C  CA    . ARG A 1 249 ? 23.993  4.463   -1.205  1.00 26.84  ? 249 ARG A CA    1 
ATOM   1948 C  C     . ARG A 1 249 ? 23.708  4.933   -2.627  1.00 32.05  ? 249 ARG A C     1 
ATOM   1949 O  O     . ARG A 1 249 ? 23.851  6.120   -2.941  1.00 33.82  ? 249 ARG A O     1 
ATOM   1950 C  CB    . ARG A 1 249 ? 25.198  3.523   -1.170  1.00 31.09  ? 249 ARG A CB    1 
ATOM   1951 C  CG    . ARG A 1 249 ? 25.642  3.191   0.240   1.00 31.24  ? 249 ARG A CG    1 
ATOM   1952 C  CD    . ARG A 1 249 ? 27.071  2.685   0.297   1.00 30.27  ? 249 ARG A CD    1 
ATOM   1953 N  NE    . ARG A 1 249 ? 27.349  2.113   1.608   1.00 35.87  ? 249 ARG A NE    1 
ATOM   1954 C  CZ    . ARG A 1 249 ? 27.126  0.846   1.925   1.00 35.14  ? 249 ARG A CZ    1 
ATOM   1955 N  NH1   . ARG A 1 249 ? 26.686  -0.022  1.029   1.00 29.32  ? 249 ARG A NH1   1 
ATOM   1956 N  NH2   . ARG A 1 249 ? 27.348  0.438   3.172   1.00 33.15  ? 249 ARG A NH2   1 
ATOM   1957 N  N     . ILE A 1 250 ? 23.308  4.014   -3.508  1.00 34.02  ? 250 ILE A N     1 
ATOM   1958 C  CA    . ILE A 1 250 ? 23.003  4.405   -4.883  1.00 31.80  ? 250 ILE A CA    1 
ATOM   1959 C  C     . ILE A 1 250 ? 21.796  5.333   -4.917  1.00 30.76  ? 250 ILE A C     1 
ATOM   1960 O  O     . ILE A 1 250 ? 21.795  6.349   -5.625  1.00 31.28  ? 250 ILE A O     1 
ATOM   1961 C  CB    . ILE A 1 250 ? 22.782  3.161   -5.763  1.00 31.02  ? 250 ILE A CB    1 
ATOM   1962 C  CG1   . ILE A 1 250 ? 24.081  2.367   -5.908  1.00 35.17  ? 250 ILE A CG1   1 
ATOM   1963 C  CG2   . ILE A 1 250 ? 22.252  3.564   -7.136  1.00 32.13  ? 250 ILE A CG2   1 
ATOM   1964 C  CD1   . ILE A 1 250 ? 25.154  3.086   -6.692  1.00 36.71  ? 250 ILE A CD1   1 
ATOM   1965 N  N     . ALA A 1 251 ? 20.756  5.008   -4.145  1.00 33.53  ? 251 ALA A N     1 
ATOM   1966 C  CA    . ALA A 1 251 ? 19.516  5.778   -4.202  1.00 32.69  ? 251 ALA A CA    1 
ATOM   1967 C  C     . ALA A 1 251 ? 19.689  7.190   -3.659  1.00 30.86  ? 251 ALA A C     1 
ATOM   1968 O  O     . ALA A 1 251 ? 19.024  8.115   -4.138  1.00 32.09  ? 251 ALA A O     1 
ATOM   1969 C  CB    . ALA A 1 251 ? 18.406  5.052   -3.439  1.00 30.02  ? 251 ALA A CB    1 
ATOM   1970 N  N     . SER A 1 252 ? 20.563  7.383   -2.665  1.00 27.31  ? 252 SER A N     1 
ATOM   1971 C  CA    . SER A 1 252 ? 20.757  8.729   -2.134  1.00 31.56  ? 252 SER A CA    1 
ATOM   1972 C  C     . SER A 1 252 ? 21.284  9.675   -3.202  1.00 30.93  ? 252 SER A C     1 
ATOM   1973 O  O     . SER A 1 252 ? 20.949  10.865  -3.195  1.00 29.90  ? 252 SER A O     1 
ATOM   1974 C  CB    . SER A 1 252 ? 21.706  8.712   -0.932  1.00 27.47  ? 252 SER A CB    1 
ATOM   1975 O  OG    . SER A 1 252 ? 23.032  8.400   -1.321  1.00 31.05  ? 252 SER A OG    1 
ATOM   1976 N  N     . ARG A 1 253 ? 22.097  9.169   -4.131  1.00 32.00  ? 253 ARG A N     1 
ATOM   1977 C  CA    . ARG A 1 253 ? 22.594  10.017  -5.208  1.00 29.63  ? 253 ARG A CA    1 
ATOM   1978 C  C     . ARG A 1 253 ? 21.515  10.283  -6.250  1.00 38.65  ? 253 ARG A C     1 
ATOM   1979 O  O     . ARG A 1 253 ? 21.388  11.412  -6.737  1.00 40.05  ? 253 ARG A O     1 
ATOM   1980 C  CB    . ARG A 1 253 ? 23.823  9.384   -5.858  1.00 37.63  ? 253 ARG A CB    1 
ATOM   1981 C  CG    . ARG A 1 253 ? 24.279  10.115  -7.107  1.00 45.59  ? 253 ARG A CG    1 
ATOM   1982 C  CD    . ARG A 1 253 ? 25.734  9.851   -7.415  1.00 47.31  ? 253 ARG A CD    1 
ATOM   1983 N  NE    . ARG A 1 253 ? 26.085  10.328  -8.747  1.00 58.75  ? 253 ARG A NE    1 
ATOM   1984 C  CZ    . ARG A 1 253 ? 27.326  10.459  -9.192  1.00 56.42  ? 253 ARG A CZ    1 
ATOM   1985 N  NH1   . ARG A 1 253 ? 28.368  10.182  -8.426  1.00 61.28  ? 253 ARG A NH1   1 
ATOM   1986 N  NH2   . ARG A 1 253 ? 27.527  10.886  -10.436 1.00 67.38  ? 253 ARG A NH2   1 
ATOM   1987 N  N     . LEU A 1 254 ? 20.736  9.259   -6.607  1.00 35.98  ? 254 LEU A N     1 
ATOM   1988 C  CA    . LEU A 1 254 ? 19.601  9.475   -7.499  1.00 41.59  ? 254 LEU A CA    1 
ATOM   1989 C  C     . LEU A 1 254 ? 18.606  10.451  -6.885  1.00 42.93  ? 254 LEU A C     1 
ATOM   1990 O  O     . LEU A 1 254 ? 18.054  11.309  -7.584  1.00 42.81  ? 254 LEU A O     1 
ATOM   1991 C  CB    . LEU A 1 254 ? 18.915  8.145   -7.813  1.00 41.93  ? 254 LEU A CB    1 
ATOM   1992 C  CG    . LEU A 1 254 ? 19.768  7.048   -8.451  1.00 46.24  ? 254 LEU A CG    1 
ATOM   1993 C  CD1   . LEU A 1 254 ? 18.949  5.780   -8.649  1.00 46.95  ? 254 LEU A CD1   1 
ATOM   1994 C  CD2   . LEU A 1 254 ? 20.344  7.527   -9.770  1.00 46.63  ? 254 LEU A CD2   1 
ATOM   1995 N  N     . ALA A 1 255 ? 18.371  10.333  -5.575  1.00 34.87  ? 255 ALA A N     1 
ATOM   1996 C  CA    . ALA A 1 255 ? 17.478  11.259  -4.888  1.00 37.45  ? 255 ALA A CA    1 
ATOM   1997 C  C     . ALA A 1 255 ? 17.993  12.690  -4.979  1.00 40.42  ? 255 ALA A C     1 
ATOM   1998 O  O     . ALA A 1 255 ? 17.216  13.625  -5.211  1.00 38.85  ? 255 ALA A O     1 
ATOM   1999 C  CB    . ALA A 1 255 ? 17.314  10.835  -3.428  1.00 37.17  ? 255 ALA A CB    1 
ATOM   2000 N  N     . LYS A 1 256 ? 19.303  12.880  -4.797  1.00 35.94  ? 256 LYS A N     1 
ATOM   2001 C  CA    . LYS A 1 256 ? 19.893  14.203  -4.971  1.00 38.56  ? 256 LYS A CA    1 
ATOM   2002 C  C     . LYS A 1 256 ? 19.680  14.716  -6.390  1.00 43.12  ? 256 LYS A C     1 
ATOM   2003 O  O     . LYS A 1 256 ? 19.396  15.902  -6.595  1.00 45.41  ? 256 LYS A O     1 
ATOM   2004 C  CB    . LYS A 1 256 ? 21.384  14.157  -4.632  1.00 38.31  ? 256 LYS A CB    1 
ATOM   2005 C  CG    . LYS A 1 256 ? 22.200  15.303  -5.215  1.00 41.45  ? 256 LYS A CG    1 
ATOM   2006 C  CD    . LYS A 1 256 ? 21.845  16.634  -4.573  1.00 36.76  ? 256 LYS A CD    1 
ATOM   2007 C  CE    . LYS A 1 256 ? 22.255  17.792  -5.472  1.00 51.26  ? 256 LYS A CE    1 
ATOM   2008 N  NZ    . LYS A 1 256 ? 23.657  17.649  -5.959  1.00 59.32  ? 256 LYS A NZ    1 
ATOM   2009 N  N     . GLU A 1 257 ? 19.798  13.832  -7.382  1.00 42.65  ? 257 GLU A N     1 
ATOM   2010 C  CA    . GLU A 1 257 ? 19.644  14.248  -8.771  1.00 47.96  ? 257 GLU A CA    1 
ATOM   2011 C  C     . GLU A 1 257 ? 18.186  14.500  -9.135  1.00 45.45  ? 257 GLU A C     1 
ATOM   2012 O  O     . GLU A 1 257 ? 17.900  15.373  -9.963  1.00 46.29  ? 257 GLU A O     1 
ATOM   2013 C  CB    . GLU A 1 257 ? 20.242  13.193  -9.701  1.00 52.54  ? 257 GLU A CB    1 
ATOM   2014 C  CG    . GLU A 1 257 ? 21.744  13.012  -9.556  1.00 54.82  ? 257 GLU A CG    1 
ATOM   2015 C  CD    . GLU A 1 257 ? 22.265  11.817  -10.329 1.00 63.20  ? 257 GLU A CD    1 
ATOM   2016 O  OE1   . GLU A 1 257 ? 21.441  11.059  -10.884 1.00 60.74  ? 257 GLU A OE1   1 
ATOM   2017 O  OE2   . GLU A 1 257 ? 23.499  11.636  -10.381 1.00 72.46  ? 257 GLU A OE2   1 
ATOM   2018 N  N     . GLU A 1 258 ? 17.254  13.758  -8.537  1.00 46.49  ? 258 GLU A N     1 
ATOM   2019 C  CA    . GLU A 1 258 ? 15.848  13.836  -8.916  1.00 46.75  ? 258 GLU A CA    1 
ATOM   2020 C  C     . GLU A 1 258 ? 14.986  14.604  -7.922  1.00 45.94  ? 258 GLU A C     1 
ATOM   2021 O  O     . GLU A 1 258 ? 13.799  14.811  -8.192  1.00 52.24  ? 258 GLU A O     1 
ATOM   2022 C  CB    . GLU A 1 258 ? 15.277  12.427  -9.105  1.00 43.66  ? 258 GLU A CB    1 
ATOM   2023 C  CG    . GLU A 1 258 ? 16.021  11.604  -10.139 1.00 43.90  ? 258 GLU A CG    1 
ATOM   2024 C  CD    . GLU A 1 258 ? 15.708  10.127  -10.045 1.00 48.11  ? 258 GLU A CD    1 
ATOM   2025 O  OE1   . GLU A 1 258 ? 14.703  9.766   -9.398  1.00 55.10  ? 258 GLU A OE1   1 
ATOM   2026 O  OE2   . GLU A 1 258 ? 16.473  9.322   -10.616 1.00 59.72  ? 258 GLU A OE2   1 
ATOM   2027 N  N     . GLY A 1 259 ? 15.538  15.024  -6.788  1.00 42.78  ? 259 GLY A N     1 
ATOM   2028 C  CA    . GLY A 1 259 ? 14.809  15.876  -5.869  1.00 42.74  ? 259 GLY A CA    1 
ATOM   2029 C  C     . GLY A 1 259 ? 14.038  15.172  -4.777  1.00 43.00  ? 259 GLY A C     1 
ATOM   2030 O  O     . GLY A 1 259 ? 13.093  15.757  -4.236  1.00 47.22  ? 259 GLY A O     1 
ATOM   2031 N  N     . TRP A 1 260 ? 14.398  13.936  -4.433  1.00 36.10  ? 260 TRP A N     1 
ATOM   2032 C  CA    . TRP A 1 260 ? 13.771  13.268  -3.298  1.00 37.83  ? 260 TRP A CA    1 
ATOM   2033 C  C     . TRP A 1 260 ? 14.826  12.903  -2.259  1.00 33.31  ? 260 TRP A C     1 
ATOM   2034 O  O     . TRP A 1 260 ? 15.925  13.466  -2.270  1.00 34.16  ? 260 TRP A O     1 
ATOM   2035 C  CB    . TRP A 1 260 ? 12.974  12.037  -3.752  1.00 35.33  ? 260 TRP A CB    1 
ATOM   2036 C  CG    . TRP A 1 260 ? 13.676  11.104  -4.702  1.00 38.19  ? 260 TRP A CG    1 
ATOM   2037 C  CD1   . TRP A 1 260 ? 14.005  11.350  -6.004  1.00 41.93  ? 260 TRP A CD1   1 
ATOM   2038 C  CD2   . TRP A 1 260 ? 14.090  9.759   -4.433  1.00 34.32  ? 260 TRP A CD2   1 
ATOM   2039 N  NE1   . TRP A 1 260 ? 14.617  10.250  -6.555  1.00 39.66  ? 260 TRP A NE1   1 
ATOM   2040 C  CE2   . TRP A 1 260 ? 14.681  9.259   -5.611  1.00 38.83  ? 260 TRP A CE2   1 
ATOM   2041 C  CE3   . TRP A 1 260 ? 14.030  8.933   -3.306  1.00 39.60  ? 260 TRP A CE3   1 
ATOM   2042 C  CZ2   . TRP A 1 260 ? 15.205  7.970   -5.696  1.00 35.49  ? 260 TRP A CZ2   1 
ATOM   2043 C  CZ3   . TRP A 1 260 ? 14.553  7.653   -3.392  1.00 36.78  ? 260 TRP A CZ3   1 
ATOM   2044 C  CH2   . TRP A 1 260 ? 15.131  7.185   -4.579  1.00 32.51  ? 260 TRP A CH2   1 
ATOM   2045 N  N     . LEU A 1 261 ? 14.506  11.984  -1.350  1.00 33.06  ? 261 LEU A N     1 
ATOM   2046 C  CA    . LEU A 1 261 ? 15.392  11.647  -0.243  1.00 31.59  ? 261 LEU A CA    1 
ATOM   2047 C  C     . LEU A 1 261 ? 15.390  10.145  -0.014  1.00 34.10  ? 261 LEU A C     1 
ATOM   2048 O  O     . LEU A 1 261 ? 14.340  9.502   -0.084  1.00 31.58  ? 261 LEU A O     1 
ATOM   2049 C  CB    . LEU A 1 261 ? 14.972  12.347  1.058   1.00 32.02  ? 261 LEU A CB    1 
ATOM   2050 C  CG    . LEU A 1 261 ? 14.944  13.871  1.149   1.00 34.46  ? 261 LEU A CG    1 
ATOM   2051 C  CD1   . LEU A 1 261 ? 14.219  14.276  2.418   1.00 38.91  ? 261 LEU A CD1   1 
ATOM   2052 C  CD2   . LEU A 1 261 ? 16.348  14.454  1.130   1.00 33.14  ? 261 LEU A CD2   1 
ATOM   2053 N  N     . ALA A 1 262 ? 16.570  9.596   0.276   1.00 26.76  ? 262 ALA A N     1 
ATOM   2054 C  CA    . ALA A 1 262 ? 16.736  8.191   0.641   1.00 27.28  ? 262 ALA A CA    1 
ATOM   2055 C  C     . ALA A 1 262 ? 17.508  8.152   1.954   1.00 29.84  ? 262 ALA A C     1 
ATOM   2056 O  O     . ALA A 1 262 ? 18.682  8.534   1.993   1.00 24.74  ? 262 ALA A O     1 
ATOM   2057 C  CB    . ALA A 1 262 ? 17.468  7.415   -0.452  1.00 24.44  ? 262 ALA A CB    1 
ATOM   2058 N  N     . GLU A 1 263 ? 16.858  7.693   3.025   1.00 30.74  ? 263 GLU A N     1 
ATOM   2059 C  CA    . GLU A 1 263 ? 17.377  7.890   4.371   1.00 27.27  ? 263 GLU A CA    1 
ATOM   2060 C  C     . GLU A 1 263 ? 17.317  6.604   5.182   1.00 27.35  ? 263 GLU A C     1 
ATOM   2061 O  O     . GLU A 1 263 ? 16.498  5.717   4.926   1.00 25.39  ? 263 GLU A O     1 
ATOM   2062 C  CB    . GLU A 1 263 ? 16.601  8.991   5.112   1.00 25.76  ? 263 GLU A CB    1 
ATOM   2063 C  CG    . GLU A 1 263 ? 16.591  10.340  4.410   1.00 26.31  ? 263 GLU A CG    1 
ATOM   2064 C  CD    . GLU A 1 263 ? 17.967  10.973  4.313   1.00 29.11  ? 263 GLU A CD    1 
ATOM   2065 O  OE1   . GLU A 1 263 ? 18.867  10.596  5.092   1.00 26.17  ? 263 GLU A OE1   1 
ATOM   2066 O  OE2   . GLU A 1 263 ? 18.149  11.853  3.448   1.00 34.66  ? 263 GLU A OE2   1 
ATOM   2067 N  N     . HIS A 1 264 ? 18.191  6.535   6.188   1.00 24.81  ? 264 HIS A N     1 
ATOM   2068 C  CA    . HIS A 1 264 ? 18.285  5.397   7.106   1.00 27.43  ? 264 HIS A CA    1 
ATOM   2069 C  C     . HIS A 1 264 ? 17.291  5.593   8.255   1.00 26.90  ? 264 HIS A C     1 
ATOM   2070 O  O     . HIS A 1 264 ? 17.653  5.842   9.406   1.00 26.66  ? 264 HIS A O     1 
ATOM   2071 C  CB    . HIS A 1 264 ? 19.720  5.262   7.607   1.00 27.38  ? 264 HIS A CB    1 
ATOM   2072 C  CG    . HIS A 1 264 ? 19.993  4.007   8.376   1.00 25.29  ? 264 HIS A CG    1 
ATOM   2073 N  ND1   . HIS A 1 264 ? 21.001  3.918   9.313   1.00 26.51  ? 264 HIS A ND1   1 
ATOM   2074 C  CD2   . HIS A 1 264 ? 19.406  2.787   8.338   1.00 23.71  ? 264 HIS A CD2   1 
ATOM   2075 C  CE1   . HIS A 1 264 ? 21.016  2.701   9.827   1.00 23.96  ? 264 HIS A CE1   1 
ATOM   2076 N  NE2   . HIS A 1 264 ? 20.060  1.995   9.251   1.00 27.43  ? 264 HIS A NE2   1 
ATOM   2077 N  N     . MET A 1 265 ? 16.005  5.474   7.919   1.00 27.38  ? 265 MET A N     1 
ATOM   2078 C  CA    . MET A 1 265 ? 14.936  5.856   8.832   1.00 30.67  ? 265 MET A CA    1 
ATOM   2079 C  C     . MET A 1 265 ? 13.833  4.811   8.890   1.00 29.73  ? 265 MET A C     1 
ATOM   2080 O  O     . MET A 1 265 ? 13.485  4.201   7.875   1.00 31.39  ? 265 MET A O     1 
ATOM   2081 C  CB    . MET A 1 265 ? 14.300  7.192   8.424   1.00 27.76  ? 265 MET A CB    1 
ATOM   2082 C  CG    . MET A 1 265 ? 15.176  8.404   8.629   1.00 29.45  ? 265 MET A CG    1 
ATOM   2083 S  SD    . MET A 1 265 ? 14.373  9.906   8.043   1.00 30.08  ? 265 MET A SD    1 
ATOM   2084 C  CE    . MET A 1 265 ? 15.660  11.115  8.340   1.00 27.01  ? 265 MET A CE    1 
ATOM   2085 N  N     . LEU A 1 266 ? 13.269  4.637   10.083  1.00 30.44  ? 266 LEU A N     1 
ATOM   2086 C  CA    . LEU A 1 266 ? 12.006  3.935   10.242  1.00 27.72  ? 266 LEU A CA    1 
ATOM   2087 C  C     . LEU A 1 266 ? 10.846  4.862   9.887   1.00 31.03  ? 266 LEU A C     1 
ATOM   2088 O  O     . LEU A 1 266 ? 10.979  6.088   9.876   1.00 30.51  ? 266 LEU A O     1 
ATOM   2089 C  CB    . LEU A 1 266 ? 11.845  3.426   11.677  1.00 24.84  ? 266 LEU A CB    1 
ATOM   2090 C  CG    . LEU A 1 266 ? 11.664  4.473   12.790  1.00 30.06  ? 266 LEU A CG    1 
ATOM   2091 C  CD1   . LEU A 1 266 ? 10.194  4.806   13.056  1.00 30.90  ? 266 LEU A CD1   1 
ATOM   2092 C  CD2   . LEU A 1 266 ? 12.329  4.025   14.073  1.00 28.98  ? 266 LEU A CD2   1 
ATOM   2093 N  N     . ILE A 1 267 ? 9.694   4.260   9.602   1.00 29.97  ? 267 ILE A N     1 
ATOM   2094 C  CA    . ILE A 1 267 ? 8.444   4.989   9.412   1.00 29.38  ? 267 ILE A CA    1 
ATOM   2095 C  C     . ILE A 1 267 ? 7.381   4.298   10.252  1.00 29.88  ? 267 ILE A C     1 
ATOM   2096 O  O     . ILE A 1 267 ? 7.140   3.096   10.084  1.00 32.23  ? 267 ILE A O     1 
ATOM   2097 C  CB    . ILE A 1 267 ? 8.005   5.036   7.939   1.00 32.52  ? 267 ILE A CB    1 
ATOM   2098 C  CG1   . ILE A 1 267 ? 9.117   5.585   7.048   1.00 31.74  ? 267 ILE A CG1   1 
ATOM   2099 C  CG2   . ILE A 1 267 ? 6.750   5.880   7.790   1.00 29.85  ? 267 ILE A CG2   1 
ATOM   2100 C  CD1   . ILE A 1 267 ? 8.940   5.215   5.595   1.00 29.23  ? 267 ILE A CD1   1 
ATOM   2101 N  N     . LEU A 1 268 ? 6.748   5.045   11.151  1.00 31.59  ? 268 LEU A N     1 
ATOM   2102 C  CA    . LEU A 1 268 ? 5.661   4.511   11.955  1.00 33.73  ? 268 LEU A CA    1 
ATOM   2103 C  C     . LEU A 1 268 ? 4.464   5.447   11.896  1.00 34.63  ? 268 LEU A C     1 
ATOM   2104 O  O     . LEU A 1 268 ? 4.585   6.636   11.597  1.00 33.01  ? 268 LEU A O     1 
ATOM   2105 C  CB    . LEU A 1 268 ? 6.084   4.278   13.421  1.00 30.64  ? 268 LEU A CB    1 
ATOM   2106 C  CG    . LEU A 1 268 ? 6.650   5.402   14.300  1.00 36.94  ? 268 LEU A CG    1 
ATOM   2107 C  CD1   . LEU A 1 268 ? 5.567   6.326   14.849  1.00 36.64  ? 268 LEU A CD1   1 
ATOM   2108 C  CD2   . LEU A 1 268 ? 7.453   4.805   15.445  1.00 33.76  ? 268 LEU A CD2   1 
ATOM   2109 N  N     . GLY A 1 269 ? 3.298   4.883   12.177  1.00 34.31  ? 269 GLY A N     1 
ATOM   2110 C  CA    . GLY A 1 269 ? 2.090   5.654   12.417  1.00 36.07  ? 269 GLY A CA    1 
ATOM   2111 C  C     . GLY A 1 269 ? 1.703   5.503   13.876  1.00 35.44  ? 269 GLY A C     1 
ATOM   2112 O  O     . GLY A 1 269 ? 1.779   4.406   14.434  1.00 39.87  ? 269 GLY A O     1 
ATOM   2113 N  N     . ILE A 1 270 ? 1.306   6.610   14.495  1.00 34.57  ? 270 ILE A N     1 
ATOM   2114 C  CA    . ILE A 1 270 ? 0.894   6.613   15.891  1.00 38.56  ? 270 ILE A CA    1 
ATOM   2115 C  C     . ILE A 1 270 ? -0.485  7.252   15.987  1.00 40.47  ? 270 ILE A C     1 
ATOM   2116 O  O     . ILE A 1 270 ? -0.725  8.319   15.412  1.00 42.05  ? 270 ILE A O     1 
ATOM   2117 C  CB    . ILE A 1 270 ? 1.918   7.340   16.788  1.00 39.72  ? 270 ILE A CB    1 
ATOM   2118 C  CG1   . ILE A 1 270 ? 1.449   7.356   18.243  1.00 40.35  ? 270 ILE A CG1   1 
ATOM   2119 C  CG2   . ILE A 1 270 ? 2.202   8.752   16.279  1.00 43.12  ? 270 ILE A CG2   1 
ATOM   2120 C  CD1   . ILE A 1 270 ? 2.536   7.750   19.222  1.00 42.93  ? 270 ILE A CD1   1 
ATOM   2121 N  N     . THR A 1 271 ? -1.394  6.585   16.693  1.00 42.12  ? 271 THR A N     1 
ATOM   2122 C  CA    . THR A 1 271 ? -2.765  7.044   16.861  1.00 41.89  ? 271 THR A CA    1 
ATOM   2123 C  C     . THR A 1 271 ? -3.018  7.341   18.332  1.00 44.60  ? 271 THR A C     1 
ATOM   2124 O  O     . THR A 1 271 ? -2.636  6.555   19.205  1.00 45.07  ? 271 THR A O     1 
ATOM   2125 C  CB    . THR A 1 271 ? -3.764  5.997   16.353  1.00 45.07  ? 271 THR A CB    1 
ATOM   2126 O  OG1   . THR A 1 271 ? -3.524  5.737   14.964  1.00 44.52  ? 271 THR A OG1   1 
ATOM   2127 C  CG2   . THR A 1 271 ? -5.192  6.484   16.531  1.00 44.36  ? 271 THR A CG2   1 
ATOM   2128 N  N     . ASN A 1 272 ? -3.654  8.471   18.600  1.00 42.89  ? 272 ASN A N     1 
ATOM   2129 C  CA    . ASN A 1 272 ? -3.939  8.925   19.952  1.00 47.69  ? 272 ASN A CA    1 
ATOM   2130 C  C     . ASN A 1 272 ? -5.364  8.552   20.349  1.00 53.48  ? 272 ASN A C     1 
ATOM   2131 O  O     . ASN A 1 272 ? -6.175  8.152   19.510  1.00 48.68  ? 272 ASN A O     1 
ATOM   2132 C  CB    . ASN A 1 272 ? -3.698  10.439  20.054  1.00 52.75  ? 272 ASN A CB    1 
ATOM   2133 C  CG    . ASN A 1 272 ? -4.811  11.276  19.431  1.00 47.91  ? 272 ASN A CG    1 
ATOM   2134 O  OD1   . ASN A 1 272 ? -5.605  10.798  18.622  1.00 53.19  ? 272 ASN A OD1   1 
ATOM   2135 N  ND2   . ASN A 1 272 ? -4.853  12.550  19.802  1.00 46.22  ? 272 ASN A ND2   1 
ATOM   2136 N  N     . PRO A 1 273 ? -5.701  8.644   21.641  1.00 55.65  ? 273 PRO A N     1 
ATOM   2137 C  CA    . PRO A 1 273 ? -7.059  8.259   22.067  1.00 50.65  ? 273 PRO A CA    1 
ATOM   2138 C  C     . PRO A 1 273 ? -8.167  9.114   21.473  1.00 51.68  ? 273 PRO A C     1 
ATOM   2139 O  O     . PRO A 1 273 ? -9.335  8.711   21.533  1.00 55.22  ? 273 PRO A O     1 
ATOM   2140 C  CB    . PRO A 1 273 ? -7.001  8.405   23.594  1.00 51.63  ? 273 PRO A CB    1 
ATOM   2141 C  CG    . PRO A 1 273 ? -5.566  8.243   23.932  1.00 50.29  ? 273 PRO A CG    1 
ATOM   2142 C  CD    . PRO A 1 273 ? -4.816  8.876   22.797  1.00 49.70  ? 273 PRO A CD    1 
ATOM   2143 N  N     . GLU A 1 274 ? -7.851  10.277  20.909  1.00 49.60  ? 274 GLU A N     1 
ATOM   2144 C  CA    . GLU A 1 274 ? -8.853  11.135  20.291  1.00 54.08  ? 274 GLU A CA    1 
ATOM   2145 C  C     . GLU A 1 274 ? -9.118  10.777  18.833  1.00 53.13  ? 274 GLU A C     1 
ATOM   2146 O  O     . GLU A 1 274 ? -9.830  11.515  18.145  1.00 50.81  ? 274 GLU A O     1 
ATOM   2147 C  CB    . GLU A 1 274 ? -8.429  12.603  20.396  1.00 52.65  ? 274 GLU A CB    1 
ATOM   2148 C  CG    . GLU A 1 274 ? -8.129  13.072  21.814  1.00 57.18  ? 274 GLU A CG    1 
ATOM   2149 C  CD    . GLU A 1 274 ? -9.372  13.196  22.678  1.00 64.67  ? 274 GLU A CD    1 
ATOM   2150 O  OE1   . GLU A 1 274 ? -10.492 13.224  22.125  1.00 64.64  ? 274 GLU A OE1   1 
ATOM   2151 O  OE2   . GLU A 1 274 ? -9.225  13.270  23.916  1.00 71.79  ? 274 GLU A OE2   1 
ATOM   2152 N  N     . GLY A 1 275 ? -8.555  9.673   18.346  1.00 49.70  ? 275 GLY A N     1 
ATOM   2153 C  CA    . GLY A 1 275 ? -8.802  9.223   16.992  1.00 51.55  ? 275 GLY A CA    1 
ATOM   2154 C  C     . GLY A 1 275 ? -7.943  9.856   15.919  1.00 54.26  ? 275 GLY A C     1 
ATOM   2155 O  O     . GLY A 1 275 ? -8.228  9.660   14.732  1.00 55.99  ? 275 GLY A O     1 
ATOM   2156 N  N     . LYS A 1 276 ? -6.906  10.603  16.288  1.00 48.16  ? 276 LYS A N     1 
ATOM   2157 C  CA    . LYS A 1 276 ? -6.020  11.242  15.324  1.00 46.98  ? 276 LYS A CA    1 
ATOM   2158 C  C     . LYS A 1 276 ? -4.752  10.419  15.148  1.00 48.25  ? 276 LYS A C     1 
ATOM   2159 O  O     . LYS A 1 276 ? -4.203  9.886   16.118  1.00 47.24  ? 276 LYS A O     1 
ATOM   2160 C  CB    . LYS A 1 276 ? -5.654  12.663  15.758  1.00 50.91  ? 276 LYS A CB    1 
ATOM   2161 C  CG    . LYS A 1 276 ? -6.689  13.722  15.409  1.00 55.39  ? 276 LYS A CG    1 
ATOM   2162 C  CD    . LYS A 1 276 ? -7.838  13.730  16.397  1.00 53.44  ? 276 LYS A CD    1 
ATOM   2163 C  CE    . LYS A 1 276 ? -8.741  14.929  16.176  1.00 50.60  ? 276 LYS A CE    1 
ATOM   2164 N  NZ    . LYS A 1 276 ? -9.793  15.014  17.224  1.00 52.91  ? 276 LYS A NZ    1 
ATOM   2165 N  N     . LYS A 1 277 ? -4.282  10.331  13.906  1.00 46.18  ? 277 LYS A N     1 
ATOM   2166 C  CA    . LYS A 1 277 ? -3.121  9.525   13.559  1.00 39.82  ? 277 LYS A CA    1 
ATOM   2167 C  C     . LYS A 1 277 ? -2.116  10.375  12.797  1.00 42.38  ? 277 LYS A C     1 
ATOM   2168 O  O     . LYS A 1 277 ? -2.487  11.098  11.866  1.00 40.99  ? 277 LYS A O     1 
ATOM   2169 C  CB    . LYS A 1 277 ? -3.530  8.311   12.720  1.00 44.75  ? 277 LYS A CB    1 
ATOM   2170 C  CG    . LYS A 1 277 ? -2.369  7.466   12.240  1.00 38.09  ? 277 LYS A CG    1 
ATOM   2171 C  CD    . LYS A 1 277 ? -2.862  6.227   11.511  1.00 39.71  ? 277 LYS A CD    1 
ATOM   2172 C  CE    . LYS A 1 277 ? -1.704  5.380   11.020  1.00 40.51  ? 277 LYS A CE    1 
ATOM   2173 N  NZ    . LYS A 1 277 ? -2.172  4.126   10.363  1.00 36.93  ? 277 LYS A NZ    1 
ATOM   2174 N  N     . LYS A 1 278 ? -0.848  10.283  13.193  1.00 36.60  ? 278 LYS A N     1 
ATOM   2175 C  CA    . LYS A 1 278 ? 0.245   10.952  12.506  1.00 36.21  ? 278 LYS A CA    1 
ATOM   2176 C  C     . LYS A 1 278 ? 1.350   9.947   12.216  1.00 36.67  ? 278 LYS A C     1 
ATOM   2177 O  O     . LYS A 1 278 ? 1.501   8.943   12.917  1.00 37.46  ? 278 LYS A O     1 
ATOM   2178 C  CB    . LYS A 1 278 ? 0.806   12.118  13.331  1.00 39.53  ? 278 LYS A CB    1 
ATOM   2179 C  CG    . LYS A 1 278 ? -0.205  13.208  13.628  1.00 40.27  ? 278 LYS A CG    1 
ATOM   2180 C  CD    . LYS A 1 278 ? 0.427   14.361  14.389  1.00 41.47  ? 278 LYS A CD    1 
ATOM   2181 C  CE    . LYS A 1 278 ? -0.602  15.440  14.680  1.00 45.15  ? 278 LYS A CE    1 
ATOM   2182 N  NZ    . LYS A 1 278 ? -1.308  15.865  13.439  1.00 41.87  ? 278 LYS A NZ    1 
ATOM   2183 N  N     . TYR A 1 279 ? 2.115   10.221  11.166  1.00 37.69  ? 279 TYR A N     1 
ATOM   2184 C  CA    . TYR A 1 279 ? 3.254   9.398   10.793  1.00 34.04  ? 279 TYR A CA    1 
ATOM   2185 C  C     . TYR A 1 279 ? 4.547   10.120  11.145  1.00 33.26  ? 279 TYR A C     1 
ATOM   2186 O  O     . TYR A 1 279 ? 4.647   11.342  10.995  1.00 34.64  ? 279 TYR A O     1 
ATOM   2187 C  CB    . TYR A 1 279 ? 3.230   9.063   9.301   1.00 33.58  ? 279 TYR A CB    1 
ATOM   2188 C  CG    . TYR A 1 279 ? 2.170   8.055   8.918   1.00 39.48  ? 279 TYR A CG    1 
ATOM   2189 C  CD1   . TYR A 1 279 ? 0.872   8.460   8.627   1.00 37.00  ? 279 TYR A CD1   1 
ATOM   2190 C  CD2   . TYR A 1 279 ? 2.466   6.698   8.846   1.00 33.28  ? 279 TYR A CD2   1 
ATOM   2191 C  CE1   . TYR A 1 279 ? -0.103  7.541   8.273   1.00 40.27  ? 279 TYR A CE1   1 
ATOM   2192 C  CE2   . TYR A 1 279 ? 1.500   5.773   8.492   1.00 37.27  ? 279 TYR A CE2   1 
ATOM   2193 C  CZ    . TYR A 1 279 ? 0.218   6.201   8.207   1.00 38.70  ? 279 TYR A CZ    1 
ATOM   2194 O  OH    . TYR A 1 279 ? -0.746  5.283   7.856   1.00 41.10  ? 279 TYR A OH    1 
ATOM   2195 N  N     . LEU A 1 280 ? 5.534   9.356   11.608  1.00 32.27  ? 280 LEU A N     1 
ATOM   2196 C  CA    . LEU A 1 280 ? 6.821   9.894   12.017  1.00 26.74  ? 280 LEU A CA    1 
ATOM   2197 C  C     . LEU A 1 280 ? 7.942   9.054   11.425  1.00 26.59  ? 280 LEU A C     1 
ATOM   2198 O  O     . LEU A 1 280 ? 7.798   7.844   11.228  1.00 29.66  ? 280 LEU A O     1 
ATOM   2199 C  CB    . LEU A 1 280 ? 6.955   9.928   13.546  1.00 31.91  ? 280 LEU A CB    1 
ATOM   2200 C  CG    . LEU A 1 280 ? 5.871   10.670  14.332  1.00 38.21  ? 280 LEU A CG    1 
ATOM   2201 C  CD1   . LEU A 1 280 ? 6.101   10.532  15.829  1.00 40.82  ? 280 LEU A CD1   1 
ATOM   2202 C  CD2   . LEU A 1 280 ? 5.825   12.133  13.932  1.00 32.45  ? 280 LEU A CD2   1 
ATOM   2203 N  N     . ALA A 1 281 ? 9.059   9.712   11.133  1.00 27.47  ? 281 ALA A N     1 
ATOM   2204 C  CA    . ALA A 1 281 ? 10.274  9.050   10.684  1.00 28.94  ? 281 ALA A CA    1 
ATOM   2205 C  C     . ALA A 1 281 ? 11.376  9.279   11.710  1.00 26.49  ? 281 ALA A C     1 
ATOM   2206 O  O     . ALA A 1 281 ? 11.417  10.316  12.374  1.00 29.60  ? 281 ALA A O     1 
ATOM   2207 C  CB    . ALA A 1 281 ? 10.718  9.560   9.309   1.00 27.03  ? 281 ALA A CB    1 
ATOM   2208 N  N     . ALA A 1 282 ? 12.273  8.304   11.841  1.00 28.78  ? 282 ALA A N     1 
ATOM   2209 C  CA    . ALA A 1 282 ? 13.315  8.369   12.861  1.00 29.51  ? 282 ALA A CA    1 
ATOM   2210 C  C     . ALA A 1 282 ? 14.598  7.758   12.322  1.00 29.43  ? 282 ALA A C     1 
ATOM   2211 O  O     . ALA A 1 282 ? 14.607  6.592   11.916  1.00 30.11  ? 282 ALA A O     1 
ATOM   2212 C  CB    . ALA A 1 282 ? 12.877  7.652   14.139  1.00 29.96  ? 282 ALA A CB    1 
ATOM   2213 N  N     . ALA A 1 283 ? 15.677  8.539   12.336  1.00 23.18  ? 283 ALA A N     1 
ATOM   2214 C  CA    . ALA A 1 283 ? 16.998  8.074   11.929  1.00 27.03  ? 283 ALA A CA    1 
ATOM   2215 C  C     . ALA A 1 283 ? 17.848  7.853   13.176  1.00 23.34  ? 283 ALA A C     1 
ATOM   2216 O  O     . ALA A 1 283 ? 18.271  8.813   13.825  1.00 24.41  ? 283 ALA A O     1 
ATOM   2217 C  CB    . ALA A 1 283 ? 17.667  9.075   10.990  1.00 21.29  ? 283 ALA A CB    1 
ATOM   2218 N  N     . PHE A 1 284 ? 18.080  6.589   13.516  1.00 29.98  ? 284 PHE A N     1 
ATOM   2219 C  CA    . PHE A 1 284 ? 19.068  6.203   14.509  1.00 28.16  ? 284 PHE A CA    1 
ATOM   2220 C  C     . PHE A 1 284 ? 20.163  5.400   13.820  1.00 27.73  ? 284 PHE A C     1 
ATOM   2221 O  O     . PHE A 1 284 ? 19.903  4.749   12.800  1.00 23.69  ? 284 PHE A O     1 
ATOM   2222 C  CB    . PHE A 1 284 ? 18.459  5.354   15.633  1.00 29.99  ? 284 PHE A CB    1 
ATOM   2223 C  CG    . PHE A 1 284 ? 17.231  5.951   16.258  1.00 26.99  ? 284 PHE A CG    1 
ATOM   2224 C  CD1   . PHE A 1 284 ? 17.130  7.317   16.467  1.00 27.02  ? 284 PHE A CD1   1 
ATOM   2225 C  CD2   . PHE A 1 284 ? 16.176  5.136   16.643  1.00 30.26  ? 284 PHE A CD2   1 
ATOM   2226 C  CE1   . PHE A 1 284 ? 15.998  7.862   17.047  1.00 28.58  ? 284 PHE A CE1   1 
ATOM   2227 C  CE2   . PHE A 1 284 ? 15.041  5.672   17.224  1.00 33.08  ? 284 PHE A CE2   1 
ATOM   2228 C  CZ    . PHE A 1 284 ? 14.950  7.037   17.426  1.00 28.97  ? 284 PHE A CZ    1 
ATOM   2229 N  N     . PRO A 1 285 ? 21.394  5.437   14.331  1.00 28.98  ? 285 PRO A N     1 
ATOM   2230 C  CA    . PRO A 1 285 ? 22.459  4.624   13.734  1.00 28.74  ? 285 PRO A CA    1 
ATOM   2231 C  C     . PRO A 1 285 ? 22.141  3.142   13.846  1.00 31.94  ? 285 PRO A C     1 
ATOM   2232 O  O     . PRO A 1 285 ? 21.179  2.723   14.493  1.00 27.26  ? 285 PRO A O     1 
ATOM   2233 C  CB    . PRO A 1 285 ? 23.702  4.998   14.552  1.00 29.78  ? 285 PRO A CB    1 
ATOM   2234 C  CG    . PRO A 1 285 ? 23.384  6.338   15.134  1.00 28.36  ? 285 PRO A CG    1 
ATOM   2235 C  CD    . PRO A 1 285 ? 21.907  6.301   15.407  1.00 28.29  ? 285 PRO A CD    1 
ATOM   2236 N  N     . SER A 1 286 ? 22.973  2.341   13.189  1.00 28.47  ? 286 SER A N     1 
ATOM   2237 C  CA    . SER A 1 286 ? 22.796  0.898   13.225  1.00 32.52  ? 286 SER A CA    1 
ATOM   2238 C  C     . SER A 1 286 ? 22.833  0.389   14.662  1.00 33.20  ? 286 SER A C     1 
ATOM   2239 O  O     . SER A 1 286 ? 23.667  0.812   15.469  1.00 31.95  ? 286 SER A O     1 
ATOM   2240 C  CB    . SER A 1 286 ? 23.882  0.221   12.391  1.00 31.74  ? 286 SER A CB    1 
ATOM   2241 O  OG    . SER A 1 286 ? 23.949  0.769   11.086  1.00 30.67  ? 286 SER A OG    1 
ATOM   2242 N  N     . ALA A 1 287 ? 21.900  -0.513  14.979  1.00 33.56  ? 287 ALA A N     1 
ATOM   2243 C  CA    . ALA A 1 287 ? 21.794  -1.124  16.308  1.00 37.98  ? 287 ALA A CA    1 
ATOM   2244 C  C     . ALA A 1 287 ? 21.555  -0.076  17.394  1.00 38.57  ? 287 ALA A C     1 
ATOM   2245 O  O     . ALA A 1 287 ? 22.129  -0.145  18.483  1.00 37.17  ? 287 ALA A O     1 
ATOM   2246 C  CB    . ALA A 1 287 ? 23.028  -1.970  16.636  1.00 33.97  ? 287 ALA A CB    1 
ATOM   2247 N  N     . CYS A 1 288 ? 20.683  0.895   17.107  1.00 38.11  ? 288 CYS A N     1 
ATOM   2248 C  CA    . CYS A 1 288 ? 20.390  1.951   18.069  1.00 38.08  ? 288 CYS A CA    1 
ATOM   2249 C  C     . CYS A 1 288 ? 18.898  2.146   18.323  1.00 35.43  ? 288 CYS A C     1 
ATOM   2250 O  O     . CYS A 1 288 ? 18.521  3.127   18.975  1.00 32.85  ? 288 CYS A O     1 
ATOM   2251 C  CB    . CYS A 1 288 ? 21.028  3.272   17.624  1.00 37.14  ? 288 CYS A CB    1 
ATOM   2252 S  SG    . CYS A 1 288 ? 22.821  3.333   17.907  1.00 38.97  ? 288 CYS A SG    1 
ATOM   2253 N  N     . GLY A 1 289 ? 18.041  1.254   17.830  1.00 31.96  ? 289 GLY A N     1 
ATOM   2254 C  CA    . GLY A 1 289 ? 16.673  1.212   18.313  1.00 30.46  ? 289 GLY A CA    1 
ATOM   2255 C  C     . GLY A 1 289 ? 15.557  1.418   17.307  1.00 33.69  ? 289 GLY A C     1 
ATOM   2256 O  O     . GLY A 1 289 ? 14.393  1.526   17.703  1.00 33.05  ? 289 GLY A O     1 
ATOM   2257 N  N     . LYS A 1 290 ? 15.877  1.466   16.012  1.00 27.71  ? 290 LYS A N     1 
ATOM   2258 C  CA    . LYS A 1 290 ? 14.843  1.730   15.015  1.00 30.96  ? 290 LYS A CA    1 
ATOM   2259 C  C     . LYS A 1 290 ? 13.775  0.641   15.016  1.00 31.39  ? 290 LYS A C     1 
ATOM   2260 O  O     . LYS A 1 290 ? 12.575  0.933   15.067  1.00 28.10  ? 290 LYS A O     1 
ATOM   2261 C  CB    . LYS A 1 290 ? 15.467  1.871   13.626  1.00 34.12  ? 290 LYS A CB    1 
ATOM   2262 C  CG    . LYS A 1 290 ? 16.283  3.142   13.439  1.00 27.49  ? 290 LYS A CG    1 
ATOM   2263 C  CD    . LYS A 1 290 ? 16.699  3.320   11.982  1.00 27.66  ? 290 LYS A CD    1 
ATOM   2264 C  CE    . LYS A 1 290 ? 17.601  2.175   11.522  1.00 25.38  ? 290 LYS A CE    1 
ATOM   2265 N  NZ    . LYS A 1 290 ? 18.832  2.071   12.377  1.00 25.18  ? 290 LYS A NZ    1 
ATOM   2266 N  N     . THR A 1 291 ? 14.196  -0.626  14.970  1.00 31.78  ? 291 THR A N     1 
ATOM   2267 C  CA    . THR A 1 291 ? 13.237  -1.725  14.896  1.00 32.10  ? 291 THR A CA    1 
ATOM   2268 C  C     . THR A 1 291 ? 12.373  -1.801  16.152  1.00 33.64  ? 291 THR A C     1 
ATOM   2269 O  O     . THR A 1 291 ? 11.164  -2.052  16.070  1.00 32.69  ? 291 THR A O     1 
ATOM   2270 C  CB    . THR A 1 291 ? 13.974  -3.045  14.664  1.00 31.61  ? 291 THR A CB    1 
ATOM   2271 O  OG1   . THR A 1 291 ? 14.606  -3.016  13.379  1.00 32.29  ? 291 THR A OG1   1 
ATOM   2272 C  CG2   . THR A 1 291 ? 13.006  -4.223  14.720  1.00 26.30  ? 291 THR A CG2   1 
ATOM   2273 N  N     . ASN A 1 292 ? 12.970  -1.575  17.323  1.00 29.68  ? 292 ASN A N     1 
ATOM   2274 C  CA    . ASN A 1 292 ? 12.200  -1.635  18.560  1.00 29.43  ? 292 ASN A CA    1 
ATOM   2275 C  C     . ASN A 1 292 ? 11.221  -0.472  18.682  1.00 35.46  ? 292 ASN A C     1 
ATOM   2276 O  O     . ASN A 1 292 ? 10.160  -0.623  19.298  1.00 34.51  ? 292 ASN A O     1 
ATOM   2277 C  CB    . ASN A 1 292 ? 13.140  -1.666  19.763  1.00 39.60  ? 292 ASN A CB    1 
ATOM   2278 C  CG    . ASN A 1 292 ? 13.771  -3.026  19.967  1.00 42.81  ? 292 ASN A CG    1 
ATOM   2279 O  OD1   . ASN A 1 292 ? 13.318  -3.812  20.798  1.00 46.53  ? 292 ASN A OD1   1 
ATOM   2280 N  ND2   . ASN A 1 292 ? 14.817  -3.317  19.200  1.00 40.22  ? 292 ASN A ND2   1 
ATOM   2281 N  N     . LEU A 1 293 ? 11.552  0.689   18.112  1.00 33.04  ? 293 LEU A N     1 
ATOM   2282 C  CA    . LEU A 1 293 ? 10.631  1.819   18.167  1.00 34.70  ? 293 LEU A CA    1 
ATOM   2283 C  C     . LEU A 1 293 ? 9.501   1.668   17.153  1.00 33.96  ? 293 LEU A C     1 
ATOM   2284 O  O     . LEU A 1 293 ? 8.343   1.972   17.460  1.00 37.03  ? 293 LEU A O     1 
ATOM   2285 C  CB    . LEU A 1 293 ? 11.388  3.131   17.937  1.00 27.76  ? 293 LEU A CB    1 
ATOM   2286 C  CG    . LEU A 1 293 ? 10.572  4.419   18.089  1.00 30.50  ? 293 LEU A CG    1 
ATOM   2287 C  CD1   . LEU A 1 293 ? 10.014  4.537   19.501  1.00 30.59  ? 293 LEU A CD1   1 
ATOM   2288 C  CD2   . LEU A 1 293 ? 11.403  5.644   17.735  1.00 27.58  ? 293 LEU A CD2   1 
ATOM   2289 N  N     . ALA A 1 294 ? 9.814   1.181   15.950  1.00 33.88  ? 294 ALA A N     1 
ATOM   2290 C  CA    . ALA A 1 294 ? 8.808   1.066   14.898  1.00 34.78  ? 294 ALA A CA    1 
ATOM   2291 C  C     . ALA A 1 294 ? 7.791   -0.038  15.167  1.00 37.22  ? 294 ALA A C     1 
ATOM   2292 O  O     . ALA A 1 294 ? 6.710   -0.022  14.570  1.00 36.90  ? 294 ALA A O     1 
ATOM   2293 C  CB    . ALA A 1 294 ? 9.488   0.828   13.549  1.00 30.86  ? 294 ALA A CB    1 
ATOM   2294 N  N     . MET A 1 295 ? 8.111   -0.996  16.038  1.00 36.24  ? 295 MET A N     1 
ATOM   2295 C  CA    . MET A 1 295 ? 7.189   -2.063  16.410  1.00 39.81  ? 295 MET A CA    1 
ATOM   2296 C  C     . MET A 1 295 ? 6.704   -1.941  17.846  1.00 40.54  ? 295 MET A C     1 
ATOM   2297 O  O     . MET A 1 295 ? 6.126   -2.897  18.376  1.00 40.50  ? 295 MET A O     1 
ATOM   2298 C  CB    . MET A 1 295 ? 7.843   -3.433  16.221  1.00 37.37  ? 295 MET A CB    1 
ATOM   2299 C  CG    . MET A 1 295 ? 8.267   -3.750  14.811  1.00 40.06  ? 295 MET A CG    1 
ATOM   2300 S  SD    . MET A 1 295 ? 8.900   -5.433  14.709  1.00 43.24  ? 295 MET A SD    1 
ATOM   2301 C  CE    . MET A 1 295 ? 9.460   -5.461  13.014  1.00 39.39  ? 295 MET A CE    1 
ATOM   2302 N  N     . MET A 1 296 ? 6.921   -0.789  18.478  1.00 36.46  ? 296 MET A N     1 
ATOM   2303 C  CA    . MET A 1 296 ? 6.708   -0.644  19.912  1.00 39.40  ? 296 MET A CA    1 
ATOM   2304 C  C     . MET A 1 296 ? 5.284   -1.005  20.317  1.00 40.80  ? 296 MET A C     1 
ATOM   2305 O  O     . MET A 1 296 ? 4.318   -0.698  19.613  1.00 46.39  ? 296 MET A O     1 
ATOM   2306 C  CB    . MET A 1 296 ? 7.020   0.793   20.336  1.00 39.59  ? 296 MET A CB    1 
ATOM   2307 C  CG    . MET A 1 296 ? 6.272   1.258   21.570  1.00 46.03  ? 296 MET A CG    1 
ATOM   2308 S  SD    . MET A 1 296 ? 6.681   2.951   22.009  1.00 50.39  ? 296 MET A SD    1 
ATOM   2309 C  CE    . MET A 1 296 ? 6.474   3.758   20.429  1.00 47.95  ? 296 MET A CE    1 
ATOM   2310 N  N     . ASN A 1 297 ? 5.164   -1.687  21.457  1.00 34.78  ? 297 ASN A N     1 
ATOM   2311 C  CA    . ASN A 1 297 ? 3.880   -1.867  22.111  1.00 43.13  ? 297 ASN A CA    1 
ATOM   2312 C  C     . ASN A 1 297 ? 3.743   -0.793  23.180  1.00 42.63  ? 297 ASN A C     1 
ATOM   2313 O  O     . ASN A 1 297 ? 4.415   -0.880  24.219  1.00 44.75  ? 297 ASN A O     1 
ATOM   2314 C  CB    . ASN A 1 297 ? 3.775   -3.260  22.729  1.00 46.50  ? 297 ASN A CB    1 
ATOM   2315 C  CG    . ASN A 1 297 ? 2.366   -3.599  23.165  1.00 53.83  ? 297 ASN A CG    1 
ATOM   2316 O  OD1   . ASN A 1 297 ? 1.525   -3.975  22.349  1.00 61.22  ? 297 ASN A OD1   1 
ATOM   2317 N  ND2   . ASN A 1 297 ? 2.102   -3.477  24.459  1.00 52.75  ? 297 ASN A ND2   1 
ATOM   2318 N  N     . PRO A 1 298 ? 2.920   0.234   22.973  1.00 46.54  ? 298 PRO A N     1 
ATOM   2319 C  CA    . PRO A 1 298 ? 2.880   1.352   23.924  1.00 46.56  ? 298 PRO A CA    1 
ATOM   2320 C  C     . PRO A 1 298 ? 2.308   0.941   25.272  1.00 44.67  ? 298 PRO A C     1 
ATOM   2321 O  O     . PRO A 1 298 ? 1.403   0.108   25.360  1.00 51.57  ? 298 PRO A O     1 
ATOM   2322 C  CB    . PRO A 1 298 ? 1.975   2.378   23.229  1.00 47.41  ? 298 PRO A CB    1 
ATOM   2323 C  CG    . PRO A 1 298 ? 1.966   1.980   21.786  1.00 47.56  ? 298 PRO A CG    1 
ATOM   2324 C  CD    . PRO A 1 298 ? 2.087   0.488   21.787  1.00 47.55  ? 298 PRO A CD    1 
ATOM   2325 N  N     . THR A 1 299 ? 2.846   1.546   26.329  1.00 45.52  ? 299 THR A N     1 
ATOM   2326 C  CA    . THR A 1 299 ? 2.340   1.338   27.678  1.00 54.73  ? 299 THR A CA    1 
ATOM   2327 C  C     . THR A 1 299 ? 1.255   2.336   28.065  1.00 51.71  ? 299 THR A C     1 
ATOM   2328 O  O     . THR A 1 299 ? 0.618   2.158   29.108  1.00 54.99  ? 299 THR A O     1 
ATOM   2329 C  CB    . THR A 1 299 ? 3.484   1.416   28.696  1.00 49.43  ? 299 THR A CB    1 
ATOM   2330 O  OG1   . THR A 1 299 ? 4.067   2.724   28.664  1.00 50.12  ? 299 THR A OG1   1 
ATOM   2331 C  CG2   . THR A 1 299 ? 4.553   0.385   28.373  1.00 47.45  ? 299 THR A CG2   1 
ATOM   2332 N  N     . LEU A 1 300 ? 1.034   3.385   27.255  1.00 50.29  ? 300 LEU A N     1 
ATOM   2333 C  CA    . LEU A 1 300 ? -0.037  4.345   27.512  1.00 52.30  ? 300 LEU A CA    1 
ATOM   2334 C  C     . LEU A 1 300 ? -1.345  3.830   26.928  1.00 53.51  ? 300 LEU A C     1 
ATOM   2335 O  O     . LEU A 1 300 ? -1.386  3.462   25.747  1.00 53.71  ? 300 LEU A O     1 
ATOM   2336 C  CB    . LEU A 1 300 ? 0.287   5.703   26.907  1.00 49.00  ? 300 LEU A CB    1 
ATOM   2337 C  CG    . LEU A 1 300 ? 1.496   6.448   27.466  1.00 52.39  ? 300 LEU A CG    1 
ATOM   2338 C  CD1   . LEU A 1 300 ? 1.645   7.794   26.779  1.00 52.15  ? 300 LEU A CD1   1 
ATOM   2339 C  CD2   . LEU A 1 300 ? 1.369   6.620   28.972  1.00 54.02  ? 300 LEU A CD2   1 
ATOM   2340 N  N     . PRO A 1 301 ? -2.423  3.791   27.706  1.00 51.61  ? 301 PRO A N     1 
ATOM   2341 C  CA    . PRO A 1 301 ? -3.696  3.304   27.168  1.00 50.24  ? 301 PRO A CA    1 
ATOM   2342 C  C     . PRO A 1 301 ? -4.280  4.281   26.161  1.00 53.10  ? 301 PRO A C     1 
ATOM   2343 O  O     . PRO A 1 301 ? -4.125  5.499   26.274  1.00 51.82  ? 301 PRO A O     1 
ATOM   2344 C  CB    . PRO A 1 301 ? -4.584  3.185   28.412  1.00 53.37  ? 301 PRO A CB    1 
ATOM   2345 C  CG    . PRO A 1 301 ? -4.024  4.200   29.357  1.00 61.21  ? 301 PRO A CG    1 
ATOM   2346 C  CD    . PRO A 1 301 ? -2.537  4.223   29.109  1.00 54.24  ? 301 PRO A CD    1 
ATOM   2347 N  N     . GLY A 1 302 ? -4.956  3.725   25.157  1.00 51.46  ? 302 GLY A N     1 
ATOM   2348 C  CA    . GLY A 1 302 ? -5.537  4.515   24.096  1.00 50.75  ? 302 GLY A CA    1 
ATOM   2349 C  C     . GLY A 1 302 ? -4.605  4.829   22.947  1.00 56.03  ? 302 GLY A C     1 
ATOM   2350 O  O     . GLY A 1 302 ? -5.055  5.394   21.942  1.00 55.70  ? 302 GLY A O     1 
ATOM   2351 N  N     . TRP A 1 303 ? -3.328  4.481   23.057  1.00 51.87  ? 303 TRP A N     1 
ATOM   2352 C  CA    . TRP A 1 303 ? -2.343  4.768   22.025  1.00 49.31  ? 303 TRP A CA    1 
ATOM   2353 C  C     . TRP A 1 303 ? -2.022  3.509   21.231  1.00 49.26  ? 303 TRP A C     1 
ATOM   2354 O  O     . TRP A 1 303 ? -2.045  2.395   21.759  1.00 52.53  ? 303 TRP A O     1 
ATOM   2355 C  CB    . TRP A 1 303 ? -1.067  5.339   22.641  1.00 45.67  ? 303 TRP A CB    1 
ATOM   2356 C  CG    . TRP A 1 303 ? -1.247  6.727   23.161  1.00 50.01  ? 303 TRP A CG    1 
ATOM   2357 C  CD1   . TRP A 1 303 ? -1.773  7.093   24.366  1.00 49.45  ? 303 TRP A CD1   1 
ATOM   2358 C  CD2   . TRP A 1 303 ? -0.912  7.941   22.483  1.00 48.72  ? 303 TRP A CD2   1 
ATOM   2359 N  NE1   . TRP A 1 303 ? -1.782  8.462   24.482  1.00 45.40  ? 303 TRP A NE1   1 
ATOM   2360 C  CE2   . TRP A 1 303 ? -1.257  9.006   23.339  1.00 48.12  ? 303 TRP A CE2   1 
ATOM   2361 C  CE3   . TRP A 1 303 ? -0.351  8.232   21.236  1.00 47.17  ? 303 TRP A CE3   1 
ATOM   2362 C  CZ2   . TRP A 1 303 ? -1.059  10.338  22.987  1.00 47.07  ? 303 TRP A CZ2   1 
ATOM   2363 C  CZ3   . TRP A 1 303 ? -0.153  9.554   20.890  1.00 43.41  ? 303 TRP A CZ3   1 
ATOM   2364 C  CH2   . TRP A 1 303 ? -0.505  10.591  21.762  1.00 45.22  ? 303 TRP A CH2   1 
ATOM   2365 N  N     . LYS A 1 304 ? -1.722  3.700   19.949  1.00 42.03  ? 304 LYS A N     1 
ATOM   2366 C  CA    . LYS A 1 304 ? -1.441  2.590   19.051  1.00 44.65  ? 304 LYS A CA    1 
ATOM   2367 C  C     . LYS A 1 304 ? -0.322  2.977   18.098  1.00 42.61  ? 304 LYS A C     1 
ATOM   2368 O  O     . LYS A 1 304 ? -0.348  4.063   17.512  1.00 42.56  ? 304 LYS A O     1 
ATOM   2369 C  CB    . LYS A 1 304 ? -2.692  2.184   18.261  1.00 44.60  ? 304 LYS A CB    1 
ATOM   2370 C  CG    . LYS A 1 304 ? -2.483  0.974   17.365  1.00 52.50  ? 304 LYS A CG    1 
ATOM   2371 C  CD    . LYS A 1 304 ? -3.753  0.595   16.623  1.00 59.21  ? 304 LYS A CD    1 
ATOM   2372 C  CE    . LYS A 1 304 ? -3.564  -0.697  15.845  1.00 61.26  ? 304 LYS A CE    1 
ATOM   2373 N  NZ    . LYS A 1 304 ? -4.802  -1.097  15.122  1.00 70.84  ? 304 LYS A NZ    1 
ATOM   2374 N  N     . VAL A 1 305 ? 0.658   2.089   17.951  1.00 39.13  ? 305 VAL A N     1 
ATOM   2375 C  CA    . VAL A 1 305 ? 1.762   2.264   17.015  1.00 40.07  ? 305 VAL A CA    1 
ATOM   2376 C  C     . VAL A 1 305 ? 1.626   1.218   15.919  1.00 41.67  ? 305 VAL A C     1 
ATOM   2377 O  O     . VAL A 1 305 ? 1.367   0.041   16.202  1.00 43.63  ? 305 VAL A O     1 
ATOM   2378 C  CB    . VAL A 1 305 ? 3.126   2.152   17.718  1.00 40.55  ? 305 VAL A CB    1 
ATOM   2379 C  CG1   . VAL A 1 305 ? 4.253   2.064   16.691  1.00 40.92  ? 305 VAL A CG1   1 
ATOM   2380 C  CG2   . VAL A 1 305 ? 3.341   3.340   18.635  1.00 44.51  ? 305 VAL A CG2   1 
ATOM   2381 N  N     . GLU A 1 306 ? 1.786   1.648   14.671  1.00 36.46  ? 306 GLU A N     1 
ATOM   2382 C  CA    . GLU A 1 306 ? 1.775   0.758   13.523  1.00 41.43  ? 306 GLU A CA    1 
ATOM   2383 C  C     . GLU A 1 306 ? 3.037   0.993   12.707  1.00 38.78  ? 306 GLU A C     1 
ATOM   2384 O  O     . GLU A 1 306 ? 3.545   2.114   12.633  1.00 40.13  ? 306 GLU A O     1 
ATOM   2385 C  CB    . GLU A 1 306 ? 0.523   0.971   12.665  1.00 39.25  ? 306 GLU A CB    1 
ATOM   2386 C  CG    . GLU A 1 306 ? -0.765  0.589   13.374  1.00 44.87  ? 306 GLU A CG    1 
ATOM   2387 C  CD    . GLU A 1 306 ? -1.998  1.070   12.640  1.00 45.88  ? 306 GLU A CD    1 
ATOM   2388 O  OE1   . GLU A 1 306 ? -2.302  2.280   12.715  1.00 42.87  ? 306 GLU A OE1   1 
ATOM   2389 O  OE2   . GLU A 1 306 ? -2.654  0.239   11.979  1.00 49.12  ? 306 GLU A OE2   1 
ATOM   2390 N  N     . CYS A 1 307 ? 3.542   -0.077  12.100  1.00 39.54  ? 307 CYS A N     1 
ATOM   2391 C  CA    . CYS A 1 307 ? 4.853   -0.075  11.463  1.00 35.47  ? 307 CYS A CA    1 
ATOM   2392 C  C     . CYS A 1 307 ? 4.709   0.001   9.949   1.00 38.01  ? 307 CYS A C     1 
ATOM   2393 O  O     . CYS A 1 307 ? 4.094   -0.877  9.335   1.00 35.40  ? 307 CYS A O     1 
ATOM   2394 C  CB    . CYS A 1 307 ? 5.639   -1.325  11.857  1.00 36.44  ? 307 CYS A CB    1 
ATOM   2395 S  SG    . CYS A 1 307 ? 7.205   -1.503  11.002  1.00 37.95  ? 307 CYS A SG    1 
ATOM   2396 N  N     . VAL A 1 308 ? 5.282   1.044   9.353   1.00 33.07  ? 308 VAL A N     1 
ATOM   2397 C  CA    . VAL A 1 308 ? 5.392   1.131   7.900   1.00 34.42  ? 308 VAL A CA    1 
ATOM   2398 C  C     . VAL A 1 308 ? 6.702   0.523   7.414   1.00 32.84  ? 308 VAL A C     1 
ATOM   2399 O  O     . VAL A 1 308 ? 6.723   -0.213  6.425   1.00 33.27  ? 308 VAL A O     1 
ATOM   2400 C  CB    . VAL A 1 308 ? 5.252   2.599   7.449   1.00 32.03  ? 308 VAL A CB    1 
ATOM   2401 C  CG1   . VAL A 1 308 ? 5.392   2.710   5.939   1.00 30.89  ? 308 VAL A CG1   1 
ATOM   2402 C  CG2   . VAL A 1 308 ? 3.925   3.178   7.914   1.00 33.61  ? 308 VAL A CG2   1 
ATOM   2403 N  N     . GLY A 1 309 ? 7.793   0.822   8.110   1.00 29.86  ? 309 GLY A N     1 
ATOM   2404 C  CA    . GLY A 1 309 ? 9.091   0.242   7.821   1.00 27.77  ? 309 GLY A CA    1 
ATOM   2405 C  C     . GLY A 1 309 ? 10.022  0.511   8.980   1.00 29.09  ? 309 GLY A C     1 
ATOM   2406 O  O     . GLY A 1 309 ? 9.750   1.366   9.828   1.00 25.45  ? 309 GLY A O     1 
ATOM   2407 N  N     . ASP A 1 310 ? 11.130  -0.228  9.014   1.00 29.37  ? 310 ASP A N     1 
ATOM   2408 C  CA    . ASP A 1 310 ? 12.029  -0.143  10.157  1.00 25.97  ? 310 ASP A CA    1 
ATOM   2409 C  C     . ASP A 1 310 ? 13.461  0.260   9.822   1.00 27.78  ? 310 ASP A C     1 
ATOM   2410 O  O     . ASP A 1 310 ? 14.265  0.421   10.750  1.00 30.49  ? 310 ASP A O     1 
ATOM   2411 C  CB    . ASP A 1 310 ? 12.042  -1.476  10.926  1.00 27.29  ? 310 ASP A CB    1 
ATOM   2412 C  CG    . ASP A 1 310 ? 12.891  -2.549  10.248  1.00 32.70  ? 310 ASP A CG    1 
ATOM   2413 O  OD1   . ASP A 1 310 ? 12.989  -2.556  9.003   1.00 32.55  ? 310 ASP A OD1   1 
ATOM   2414 O  OD2   . ASP A 1 310 ? 13.459  -3.393  10.971  1.00 30.63  ? 310 ASP A OD2   1 
ATOM   2415 N  N     . ASP A 1 311 ? 13.813  0.447   8.547   1.00 28.97  ? 311 ASP A N     1 
ATOM   2416 C  CA    . ASP A 1 311 ? 15.223  0.678   8.247   1.00 26.85  ? 311 ASP A CA    1 
ATOM   2417 C  C     . ASP A 1 311 ? 15.491  1.728   7.170   1.00 24.59  ? 311 ASP A C     1 
ATOM   2418 O  O     . ASP A 1 311 ? 16.436  2.512   7.299   1.00 30.35  ? 311 ASP A O     1 
ATOM   2419 C  CB    . ASP A 1 311 ? 15.891  -0.640  7.850   1.00 26.96  ? 311 ASP A CB    1 
ATOM   2420 C  CG    . ASP A 1 311 ? 17.409  -0.553  7.880   1.00 25.71  ? 311 ASP A CG    1 
ATOM   2421 O  OD1   . ASP A 1 311 ? 17.971  -0.316  8.968   1.00 27.73  ? 311 ASP A OD1   1 
ATOM   2422 O  OD2   . ASP A 1 311 ? 18.040  -0.711  6.817   1.00 30.23  ? 311 ASP A OD2   1 
ATOM   2423 N  N     . ILE A 1 312 ? 14.707  1.747   6.094   1.00 26.35  ? 312 ILE A N     1 
ATOM   2424 C  CA    . ILE A 1 312 ? 14.972  2.625   4.958   1.00 26.48  ? 312 ILE A CA    1 
ATOM   2425 C  C     . ILE A 1 312 ? 13.686  3.342   4.575   1.00 28.40  ? 312 ILE A C     1 
ATOM   2426 O  O     . ILE A 1 312 ? 12.621  2.720   4.506   1.00 30.02  ? 312 ILE A O     1 
ATOM   2427 C  CB    . ILE A 1 312 ? 15.536  1.850   3.749   1.00 30.09  ? 312 ILE A CB    1 
ATOM   2428 C  CG1   . ILE A 1 312 ? 16.790  1.066   4.147   1.00 30.08  ? 312 ILE A CG1   1 
ATOM   2429 C  CG2   . ILE A 1 312 ? 15.860  2.808   2.606   1.00 22.17  ? 312 ILE A CG2   1 
ATOM   2430 C  CD1   . ILE A 1 312 ? 17.260  0.087   3.098   1.00 32.20  ? 312 ILE A CD1   1 
ATOM   2431 N  N     . ALA A 1 313 ? 13.791  4.645   4.317   1.00 31.73  ? 313 ALA A N     1 
ATOM   2432 C  CA    . ALA A 1 313 ? 12.667  5.461   3.883   1.00 29.25  ? 313 ALA A CA    1 
ATOM   2433 C  C     . ALA A 1 313 ? 13.044  6.227   2.623   1.00 29.70  ? 313 ALA A C     1 
ATOM   2434 O  O     . ALA A 1 313 ? 14.142  6.784   2.530   1.00 31.06  ? 313 ALA A O     1 
ATOM   2435 C  CB    . ALA A 1 313 ? 12.237  6.443   4.980   1.00 27.83  ? 313 ALA A CB    1 
ATOM   2436 N  N     . TRP A 1 314 ? 12.133  6.246   1.654   1.00 26.61  ? 314 TRP A N     1 
ATOM   2437 C  CA    . TRP A 1 314 ? 12.254  7.064   0.453   1.00 32.46  ? 314 TRP A CA    1 
ATOM   2438 C  C     . TRP A 1 314 ? 11.176  8.139   0.506   1.00 35.20  ? 314 TRP A C     1 
ATOM   2439 O  O     . TRP A 1 314 ? 9.981   7.821   0.507   1.00 32.76  ? 314 TRP A O     1 
ATOM   2440 C  CB    . TRP A 1 314 ? 12.110  6.219   -0.814  1.00 34.19  ? 314 TRP A CB    1 
ATOM   2441 C  CG    . TRP A 1 314 ? 13.278  5.322   -1.109  1.00 31.29  ? 314 TRP A CG    1 
ATOM   2442 C  CD1   . TRP A 1 314 ? 14.427  5.194   -0.380  1.00 30.95  ? 314 TRP A CD1   1 
ATOM   2443 C  CD2   . TRP A 1 314 ? 13.411  4.436   -2.227  1.00 28.17  ? 314 TRP A CD2   1 
ATOM   2444 N  NE1   . TRP A 1 314 ? 15.264  4.278   -0.976  1.00 30.57  ? 314 TRP A NE1   1 
ATOM   2445 C  CE2   . TRP A 1 314 ? 14.662  3.798   -2.109  1.00 28.82  ? 314 TRP A CE2   1 
ATOM   2446 C  CE3   . TRP A 1 314 ? 12.590  4.116   -3.315  1.00 36.53  ? 314 TRP A CE3   1 
ATOM   2447 C  CZ2   . TRP A 1 314 ? 15.113  2.862   -3.037  1.00 33.18  ? 314 TRP A CZ2   1 
ATOM   2448 C  CZ3   . TRP A 1 314 ? 13.040  3.184   -4.235  1.00 38.27  ? 314 TRP A CZ3   1 
ATOM   2449 C  CH2   . TRP A 1 314 ? 14.290  2.570   -4.090  1.00 33.74  ? 314 TRP A CH2   1 
ATOM   2450 N  N     . MET A 1 315 ? 11.592  9.403   0.545   1.00 33.86  ? 315 MET A N     1 
ATOM   2451 C  CA    . MET A 1 315 ? 10.684  10.506  0.822   1.00 37.03  ? 315 MET A CA    1 
ATOM   2452 C  C     . MET A 1 315 ? 10.740  11.549  -0.285  1.00 37.59  ? 315 MET A C     1 
ATOM   2453 O  O     . MET A 1 315 ? 11.787  11.779  -0.894  1.00 35.12  ? 315 MET A O     1 
ATOM   2454 C  CB    . MET A 1 315 ? 11.011  11.161  2.169   1.00 35.67  ? 315 MET A CB    1 
ATOM   2455 C  CG    . MET A 1 315 ? 11.129  10.164  3.314   1.00 38.95  ? 315 MET A CG    1 
ATOM   2456 S  SD    . MET A 1 315 ? 11.227  10.948  4.933   1.00 38.45  ? 315 MET A SD    1 
ATOM   2457 C  CE    . MET A 1 315 ? 12.764  11.849  4.785   1.00 36.92  ? 315 MET A CE    1 
ATOM   2458 N  N     . LYS A 1 316 ? 9.598   12.195  -0.518  1.00 38.82  ? 316 LYS A N     1 
ATOM   2459 C  CA    . LYS A 1 316 ? 9.467   13.202  -1.562  1.00 41.84  ? 316 LYS A CA    1 
ATOM   2460 C  C     . LYS A 1 316 ? 8.261   14.080  -1.253  1.00 41.86  ? 316 LYS A C     1 
ATOM   2461 O  O     . LYS A 1 316 ? 7.252   13.592  -0.737  1.00 41.45  ? 316 LYS A O     1 
ATOM   2462 C  CB    . LYS A 1 316 ? 9.323   12.541  -2.941  1.00 47.84  ? 316 LYS A CB    1 
ATOM   2463 C  CG    . LYS A 1 316 ? 8.404   13.268  -3.910  1.00 53.39  ? 316 LYS A CG    1 
ATOM   2464 C  CD    . LYS A 1 316 ? 8.231   12.491  -5.204  1.00 54.97  ? 316 LYS A CD    1 
ATOM   2465 C  CE    . LYS A 1 316 ? 9.537   12.412  -5.975  1.00 61.23  ? 316 LYS A CE    1 
ATOM   2466 N  NZ    . LYS A 1 316 ? 10.001  13.753  -6.433  1.00 64.28  ? 316 LYS A NZ    1 
ATOM   2467 N  N     . PHE A 1 317 ? 8.377   15.373  -1.550  1.00 43.83  ? 317 PHE A N     1 
ATOM   2468 C  CA    . PHE A 1 317 ? 7.246   16.282  -1.420  1.00 47.68  ? 317 PHE A CA    1 
ATOM   2469 C  C     . PHE A 1 317 ? 6.268   16.078  -2.571  1.00 49.96  ? 317 PHE A C     1 
ATOM   2470 O  O     . PHE A 1 317 ? 6.671   15.935  -3.729  1.00 51.26  ? 317 PHE A O     1 
ATOM   2471 C  CB    . PHE A 1 317 ? 7.719   17.736  -1.395  1.00 46.40  ? 317 PHE A CB    1 
ATOM   2472 C  CG    . PHE A 1 317 ? 8.394   18.135  -0.114  1.00 51.35  ? 317 PHE A CG    1 
ATOM   2473 C  CD1   . PHE A 1 317 ? 7.646   18.438  1.012   1.00 47.02  ? 317 PHE A CD1   1 
ATOM   2474 C  CD2   . PHE A 1 317 ? 9.774   18.217  -0.037  1.00 56.22  ? 317 PHE A CD2   1 
ATOM   2475 C  CE1   . PHE A 1 317 ? 8.261   18.805  2.192   1.00 49.69  ? 317 PHE A CE1   1 
ATOM   2476 C  CE2   . PHE A 1 317 ? 10.395  18.585  1.140   1.00 53.22  ? 317 PHE A CE2   1 
ATOM   2477 C  CZ    . PHE A 1 317 ? 9.638   18.879  2.256   1.00 50.28  ? 317 PHE A CZ    1 
ATOM   2478 N  N     . ASP A 1 318 ? 4.977   16.071  -2.250  1.00 50.50  ? 318 ASP A N     1 
ATOM   2479 C  CA    . ASP A 1 318 ? 3.954   15.921  -3.272  1.00 48.57  ? 318 ASP A CA    1 
ATOM   2480 C  C     . ASP A 1 318 ? 3.505   17.294  -3.773  1.00 52.99  ? 318 ASP A C     1 
ATOM   2481 O  O     . ASP A 1 318 ? 4.047   18.334  -3.388  1.00 49.11  ? 318 ASP A O     1 
ATOM   2482 C  CB    . ASP A 1 318 ? 2.778   15.094  -2.742  1.00 51.72  ? 318 ASP A CB    1 
ATOM   2483 C  CG    . ASP A 1 318 ? 2.097   15.724  -1.532  1.00 50.15  ? 318 ASP A CG    1 
ATOM   2484 O  OD1   . ASP A 1 318 ? 2.366   16.900  -1.210  1.00 52.39  ? 318 ASP A OD1   1 
ATOM   2485 O  OD2   . ASP A 1 318 ? 1.279   15.026  -0.896  1.00 52.86  ? 318 ASP A OD2   1 
ATOM   2486 N  N     . ALA A 1 319 ? 2.494   17.298  -4.647  1.00 58.21  ? 319 ALA A N     1 
ATOM   2487 C  CA    . ALA A 1 319 ? 1.983   18.556  -5.180  1.00 57.92  ? 319 ALA A CA    1 
ATOM   2488 C  C     . ALA A 1 319 ? 1.428   19.451  -4.079  1.00 56.14  ? 319 ALA A C     1 
ATOM   2489 O  O     . ALA A 1 319 ? 1.534   20.680  -4.165  1.00 60.45  ? 319 ALA A O     1 
ATOM   2490 C  CB    . ALA A 1 319 ? 0.909   18.284  -6.234  1.00 61.14  ? 319 ALA A CB    1 
ATOM   2491 N  N     . GLN A 1 320 ? 0.844   18.859  -3.038  1.00 54.63  ? 320 GLN A N     1 
ATOM   2492 C  CA    . GLN A 1 320 ? 0.270   19.619  -1.935  1.00 56.13  ? 320 GLN A CA    1 
ATOM   2493 C  C     . GLN A 1 320 ? 1.313   20.094  -0.932  1.00 56.83  ? 320 GLN A C     1 
ATOM   2494 O  O     . GLN A 1 320 ? 0.963   20.818  0.006   1.00 49.94  ? 320 GLN A O     1 
ATOM   2495 C  CB    . GLN A 1 320 ? -0.786  18.776  -1.213  1.00 55.48  ? 320 GLN A CB    1 
ATOM   2496 C  CG    . GLN A 1 320 ? -1.701  17.996  -2.143  1.00 59.60  ? 320 GLN A CG    1 
ATOM   2497 C  CD    . GLN A 1 320 ? -2.579  18.893  -2.994  1.00 64.09  ? 320 GLN A CD    1 
ATOM   2498 O  OE1   . GLN A 1 320 ? -2.878  20.027  -2.620  1.00 65.89  ? 320 GLN A OE1   1 
ATOM   2499 N  NE2   . GLN A 1 320 ? -3.000  18.385  -4.148  1.00 73.05  ? 320 GLN A NE2   1 
ATOM   2500 N  N     . GLY A 1 321 ? 2.574   19.708  -1.099  1.00 53.47  ? 321 GLY A N     1 
ATOM   2501 C  CA    . GLY A 1 321 ? 3.617   20.119  -0.184  1.00 54.50  ? 321 GLY A CA    1 
ATOM   2502 C  C     . GLY A 1 321 ? 3.797   19.239  1.032   1.00 51.11  ? 321 GLY A C     1 
ATOM   2503 O  O     . GLY A 1 321 ? 4.502   19.641  1.965   1.00 49.66  ? 321 GLY A O     1 
ATOM   2504 N  N     . ASN A 1 322 ? 3.177   18.061  1.059   1.00 45.43  ? 322 ASN A N     1 
ATOM   2505 C  CA    . ASN A 1 322 ? 3.371   17.110  2.144   1.00 49.11  ? 322 ASN A CA    1 
ATOM   2506 C  C     . ASN A 1 322 ? 4.585   16.243  1.845   1.00 47.87  ? 322 ASN A C     1 
ATOM   2507 O  O     . ASN A 1 322 ? 4.741   15.753  0.722   1.00 44.98  ? 322 ASN A O     1 
ATOM   2508 C  CB    . ASN A 1 322 ? 2.137   16.223  2.331   1.00 51.12  ? 322 ASN A CB    1 
ATOM   2509 C  CG    . ASN A 1 322 ? 0.885   17.016  2.636   1.00 53.80  ? 322 ASN A CG    1 
ATOM   2510 O  OD1   . ASN A 1 322 ? 0.727   17.553  3.732   1.00 56.84  ? 322 ASN A OD1   1 
ATOM   2511 N  ND2   . ASN A 1 322 ? -0.024  17.079  1.669   1.00 59.92  ? 322 ASN A ND2   1 
ATOM   2512 N  N     . LEU A 1 323 ? 5.440   16.058  2.846   1.00 43.33  ? 323 LEU A N     1 
ATOM   2513 C  CA    . LEU A 1 323 ? 6.538   15.105  2.733   1.00 41.31  ? 323 LEU A CA    1 
ATOM   2514 C  C     . LEU A 1 323 ? 5.974   13.696  2.864   1.00 38.83  ? 323 LEU A C     1 
ATOM   2515 O  O     . LEU A 1 323 ? 5.468   13.317  3.925   1.00 40.10  ? 323 LEU A O     1 
ATOM   2516 C  CB    . LEU A 1 323 ? 7.592   15.379  3.801   1.00 40.09  ? 323 LEU A CB    1 
ATOM   2517 C  CG    . LEU A 1 323 ? 8.864   14.534  3.720   1.00 40.15  ? 323 LEU A CG    1 
ATOM   2518 C  CD1   . LEU A 1 323 ? 9.545   14.721  2.370   1.00 36.58  ? 323 LEU A CD1   1 
ATOM   2519 C  CD2   . LEU A 1 323 ? 9.815   14.882  4.858   1.00 36.17  ? 323 LEU A CD2   1 
ATOM   2520 N  N     . ARG A 1 324 ? 6.039   12.923  1.785   1.00 36.49  ? 324 ARG A N     1 
ATOM   2521 C  CA    . ARG A 1 324 ? 5.480   11.581  1.751   1.00 42.42  ? 324 ARG A CA    1 
ATOM   2522 C  C     . ARG A 1 324 ? 6.604   10.555  1.719   1.00 35.29  ? 324 ARG A C     1 
ATOM   2523 O  O     . ARG A 1 324 ? 7.603   10.739  1.020   1.00 37.30  ? 324 ARG A O     1 
ATOM   2524 C  CB    . ARG A 1 324 ? 4.559   11.400  0.541   1.00 45.58  ? 324 ARG A CB    1 
ATOM   2525 C  CG    . ARG A 1 324 ? 3.496   12.479  0.420   1.00 47.97  ? 324 ARG A CG    1 
ATOM   2526 C  CD    . ARG A 1 324 ? 2.352   12.043  -0.481  1.00 54.81  ? 324 ARG A CD    1 
ATOM   2527 N  NE    . ARG A 1 324 ? 1.517   11.028  0.150   1.00 50.83  ? 324 ARG A NE    1 
ATOM   2528 C  CZ    . ARG A 1 324 ? 0.445   11.291  0.885   1.00 41.10  ? 324 ARG A CZ    1 
ATOM   2529 N  NH1   . ARG A 1 324 ? 0.042   12.532  1.100   1.00 42.05  ? 324 ARG A NH1   1 
ATOM   2530 N  NH2   . ARG A 1 324 ? -0.239  10.283  1.418   1.00 40.55  ? 324 ARG A NH2   1 
ATOM   2531 N  N     . ALA A 1 325 ? 6.435   9.477   2.478   1.00 34.03  ? 325 ALA A N     1 
ATOM   2532 C  CA    . ALA A 1 325 ? 7.459   8.454   2.631   1.00 35.43  ? 325 ALA A CA    1 
ATOM   2533 C  C     . ALA A 1 325 ? 6.903   7.085   2.269   1.00 34.14  ? 325 ALA A C     1 
ATOM   2534 O  O     . ALA A 1 325 ? 5.737   6.785   2.543   1.00 35.78  ? 325 ALA A O     1 
ATOM   2535 C  CB    . ALA A 1 325 ? 7.995   8.427   4.064   1.00 30.68  ? 325 ALA A CB    1 
ATOM   2536 N  N     . ILE A 1 326 ? 7.743   6.257   1.651   1.00 33.25  ? 326 ILE A N     1 
ATOM   2537 C  CA    . ILE A 1 326 ? 7.433   4.852   1.433   1.00 34.02  ? 326 ILE A CA    1 
ATOM   2538 C  C     . ILE A 1 326 ? 8.572   4.015   1.993   1.00 33.41  ? 326 ILE A C     1 
ATOM   2539 O  O     . ILE A 1 326 ? 9.712   4.475   2.107   1.00 34.05  ? 326 ILE A O     1 
ATOM   2540 C  CB    . ILE A 1 326 ? 7.203   4.507   -0.059  1.00 35.53  ? 326 ILE A CB    1 
ATOM   2541 C  CG1   . ILE A 1 326 ? 8.480   4.728   -0.874  1.00 38.24  ? 326 ILE A CG1   1 
ATOM   2542 C  CG2   . ILE A 1 326 ? 6.037   5.301   -0.630  1.00 42.28  ? 326 ILE A CG2   1 
ATOM   2543 C  CD1   . ILE A 1 326 ? 9.125   3.444   -1.349  1.00 37.82  ? 326 ILE A CD1   1 
ATOM   2544 N  N     . ASN A 1 327 ? 8.248   2.777   2.354   1.00 38.82  ? 327 ASN A N     1 
ATOM   2545 C  CA    . ASN A 1 327 ? 9.250   1.794   2.732   1.00 30.36  ? 327 ASN A CA    1 
ATOM   2546 C  C     . ASN A 1 327 ? 9.526   0.915   1.524   1.00 30.09  ? 327 ASN A C     1 
ATOM   2547 O  O     . ASN A 1 327 ? 8.647   0.137   1.127   1.00 30.27  ? 327 ASN A O     1 
ATOM   2548 C  CB    . ASN A 1 327 ? 8.761   0.950   3.909   1.00 31.58  ? 327 ASN A CB    1 
ATOM   2549 C  CG    . ASN A 1 327 ? 9.635   -0.270  4.164   1.00 29.89  ? 327 ASN A CG    1 
ATOM   2550 O  OD1   . ASN A 1 327 ? 10.818  -0.285  3.829   1.00 24.55  ? 327 ASN A OD1   1 
ATOM   2551 N  ND2   . ASN A 1 327 ? 9.047   -1.301  4.765   1.00 33.55  ? 327 ASN A ND2   1 
ATOM   2552 N  N     . PRO A 1 328 ? 10.710  0.992   0.908   1.00 31.40  ? 328 PRO A N     1 
ATOM   2553 C  CA    . PRO A 1 328 ? 10.959  0.196   -0.303  1.00 30.68  ? 328 PRO A CA    1 
ATOM   2554 C  C     . PRO A 1 328 ? 11.187  -1.280  -0.031  1.00 31.63  ? 328 PRO A C     1 
ATOM   2555 O  O     . PRO A 1 328 ? 11.200  -2.066  -0.986  1.00 30.25  ? 328 PRO A O     1 
ATOM   2556 C  CB    . PRO A 1 328 ? 12.214  0.851   -0.894  1.00 32.11  ? 328 PRO A CB    1 
ATOM   2557 C  CG    . PRO A 1 328 ? 12.945  1.361   0.304   1.00 29.53  ? 328 PRO A CG    1 
ATOM   2558 C  CD    . PRO A 1 328 ? 11.879  1.808   1.284   1.00 28.78  ? 328 PRO A CD    1 
ATOM   2559 N  N     . GLU A 1 329 ? 11.361  -1.680  1.227   1.00 35.37  ? 329 GLU A N     1 
ATOM   2560 C  CA    . GLU A 1 329 ? 11.647  -3.060  1.590   1.00 32.67  ? 329 GLU A CA    1 
ATOM   2561 C  C     . GLU A 1 329 ? 10.363  -3.867  1.746   1.00 28.90  ? 329 GLU A C     1 
ATOM   2562 O  O     . GLU A 1 329 ? 9.275   -3.322  1.939   1.00 28.71  ? 329 GLU A O     1 
ATOM   2563 C  CB    . GLU A 1 329 ? 12.444  -3.123  2.891   1.00 26.14  ? 329 GLU A CB    1 
ATOM   2564 C  CG    . GLU A 1 329 ? 13.823  -2.494  2.815   1.00 26.98  ? 329 GLU A CG    1 
ATOM   2565 C  CD    . GLU A 1 329 ? 14.684  -2.859  4.008   1.00 28.38  ? 329 GLU A CD    1 
ATOM   2566 O  OE1   . GLU A 1 329 ? 14.301  -2.519  5.145   1.00 29.88  ? 329 GLU A OE1   1 
ATOM   2567 O  OE2   . GLU A 1 329 ? 15.733  -3.505  3.814   1.00 30.43  ? 329 GLU A OE2   1 
ATOM   2568 N  N     . ASN A 1 330 ? 10.518  -5.190  1.694   1.00 30.39  ? 330 ASN A N     1 
ATOM   2569 C  CA    . ASN A 1 330 ? 9.406   -6.125  1.797   1.00 34.82  ? 330 ASN A CA    1 
ATOM   2570 C  C     . ASN A 1 330 ? 9.450   -6.954  3.074   1.00 31.33  ? 330 ASN A C     1 
ATOM   2571 O  O     . ASN A 1 330 ? 8.553   -7.776  3.294   1.00 25.22  ? 330 ASN A O     1 
ATOM   2572 C  CB    . ASN A 1 330 ? 9.389   -7.050  0.574   1.00 27.53  ? 330 ASN A CB    1 
ATOM   2573 C  CG    . ASN A 1 330 ? 8.036   -7.701  0.349   1.00 33.81  ? 330 ASN A CG    1 
ATOM   2574 O  OD1   . ASN A 1 330 ? 6.998   -7.149  0.711   1.00 35.89  ? 330 ASN A OD1   1 
ATOM   2575 N  ND2   . ASN A 1 330 ? 8.046   -8.883  -0.251  1.00 34.89  ? 330 ASN A ND2   1 
ATOM   2576 N  N     . GLY A 1 331 ? 10.457  -6.758  3.919   1.00 26.63  ? 331 GLY A N     1 
ATOM   2577 C  CA    . GLY A 1 331 ? 10.572  -7.491  5.160   1.00 21.67  ? 331 GLY A CA    1 
ATOM   2578 C  C     . GLY A 1 331 ? 11.486  -6.769  6.128   1.00 28.42  ? 331 GLY A C     1 
ATOM   2579 O  O     . GLY A 1 331 ? 11.916  -5.641  5.880   1.00 28.24  ? 331 GLY A O     1 
ATOM   2580 N  N     . PHE A 1 332 ? 11.784  -7.439  7.242   1.00 23.52  ? 332 PHE A N     1 
ATOM   2581 C  CA    . PHE A 1 332 ? 12.627  -6.885  8.296   1.00 27.79  ? 332 PHE A CA    1 
ATOM   2582 C  C     . PHE A 1 332 ? 13.871  -7.746  8.474   1.00 26.58  ? 332 PHE A C     1 
ATOM   2583 O  O     . PHE A 1 332 ? 13.775  -8.974  8.569   1.00 29.10  ? 332 PHE A O     1 
ATOM   2584 C  CB    . PHE A 1 332 ? 11.877  -6.794  9.629   1.00 29.42  ? 332 PHE A CB    1 
ATOM   2585 C  CG    . PHE A 1 332 ? 10.546  -6.108  9.539   1.00 32.15  ? 332 PHE A CG    1 
ATOM   2586 C  CD1   . PHE A 1 332 ? 10.457  -4.778  9.163   1.00 31.84  ? 332 PHE A CD1   1 
ATOM   2587 C  CD2   . PHE A 1 332 ? 9.381   -6.793  9.846   1.00 33.26  ? 332 PHE A CD2   1 
ATOM   2588 C  CE1   . PHE A 1 332 ? 9.228   -4.147  9.084   1.00 36.19  ? 332 PHE A CE1   1 
ATOM   2589 C  CE2   . PHE A 1 332 ? 8.153   -6.168  9.776   1.00 35.90  ? 332 PHE A CE2   1 
ATOM   2590 C  CZ    . PHE A 1 332 ? 8.075   -4.843  9.394   1.00 33.95  ? 332 PHE A CZ    1 
ATOM   2591 N  N     . PHE A 1 333 ? 15.028  -7.096  8.533   1.00 29.88  ? 333 PHE A N     1 
ATOM   2592 C  CA    . PHE A 1 333 ? 16.323  -7.733  8.764   1.00 28.00  ? 333 PHE A CA    1 
ATOM   2593 C  C     . PHE A 1 333 ? 16.866  -7.221  10.097  1.00 23.07  ? 333 PHE A C     1 
ATOM   2594 O  O     . PHE A 1 333 ? 17.791  -6.407  10.134  1.00 27.69  ? 333 PHE A O     1 
ATOM   2595 C  CB    . PHE A 1 333 ? 17.283  -7.426  7.583   1.00 26.62  ? 333 PHE A CB    1 
ATOM   2596 C  CG    . PHE A 1 333 ? 18.599  -8.152  7.647   1.00 27.92  ? 333 PHE A CG    1 
ATOM   2597 C  CD1   . PHE A 1 333 ? 18.660  -9.521  7.432   1.00 27.62  ? 333 PHE A CD1   1 
ATOM   2598 C  CD2   . PHE A 1 333 ? 19.780  -7.461  7.890   1.00 27.65  ? 333 PHE A CD2   1 
ATOM   2599 C  CE1   . PHE A 1 333 ? 19.868  -10.196 7.476   1.00 30.56  ? 333 PHE A CE1   1 
ATOM   2600 C  CE2   . PHE A 1 333 ? 20.999  -8.132  7.938   1.00 31.58  ? 333 PHE A CE2   1 
ATOM   2601 C  CZ    . PHE A 1 333 ? 21.042  -9.501  7.729   1.00 31.10  ? 333 PHE A CZ    1 
ATOM   2602 N  N     . GLY A 1 334 ? 16.276  -7.689  11.194  1.00 26.01  ? 334 GLY A N     1 
ATOM   2603 C  CA    . GLY A 1 334 ? 16.475  -7.086  12.499  1.00 28.74  ? 334 GLY A CA    1 
ATOM   2604 C  C     . GLY A 1 334 ? 17.456  -7.813  13.403  1.00 24.87  ? 334 GLY A C     1 
ATOM   2605 O  O     . GLY A 1 334 ? 17.656  -9.020  13.290  1.00 28.66  ? 334 GLY A O     1 
ATOM   2606 N  N     . VAL A 1 335 ? 18.055  -7.049  14.317  1.00 29.30  ? 335 VAL A N     1 
ATOM   2607 C  CA    . VAL A 1 335 ? 18.967  -7.603  15.313  1.00 26.82  ? 335 VAL A CA    1 
ATOM   2608 C  C     . VAL A 1 335 ? 18.193  -8.502  16.268  1.00 30.35  ? 335 VAL A C     1 
ATOM   2609 O  O     . VAL A 1 335 ? 17.158  -8.105  16.819  1.00 31.91  ? 335 VAL A O     1 
ATOM   2610 C  CB    . VAL A 1 335 ? 19.677  -6.472  16.074  1.00 31.61  ? 335 VAL A CB    1 
ATOM   2611 C  CG1   . VAL A 1 335 ? 20.512  -7.033  17.217  1.00 33.04  ? 335 VAL A CG1   1 
ATOM   2612 C  CG2   . VAL A 1 335 ? 20.538  -5.652  15.128  1.00 33.24  ? 335 VAL A CG2   1 
ATOM   2613 N  N     . ALA A 1 336 ? 18.699  -9.716  16.479  1.00 29.62  ? 336 ALA A N     1 
ATOM   2614 C  CA    . ALA A 1 336 ? 18.021  -10.677 17.342  1.00 29.82  ? 336 ALA A CA    1 
ATOM   2615 C  C     . ALA A 1 336 ? 18.297  -10.433 18.827  1.00 33.90  ? 336 ALA A C     1 
ATOM   2616 O  O     . ALA A 1 336 ? 17.336  -10.306 19.597  1.00 34.60  ? 336 ALA A O     1 
ATOM   2617 C  CB    . ALA A 1 336 ? 18.401  -12.111 16.952  1.00 35.20  ? 336 ALA A CB    1 
ATOM   2618 N  N     . PRO A 1 337 ? 19.555  -10.361 19.283  1.00 34.49  ? 337 PRO A N     1 
ATOM   2619 C  CA    . PRO A 1 337 ? 19.797  -10.232 20.727  1.00 35.60  ? 337 PRO A CA    1 
ATOM   2620 C  C     . PRO A 1 337 ? 19.100  -9.014  21.317  1.00 39.47  ? 337 PRO A C     1 
ATOM   2621 O  O     . PRO A 1 337 ? 19.056  -7.941  20.710  1.00 36.70  ? 337 PRO A O     1 
ATOM   2622 C  CB    . PRO A 1 337 ? 21.322  -10.111 20.823  1.00 31.31  ? 337 PRO A CB    1 
ATOM   2623 C  CG    . PRO A 1 337 ? 21.828  -10.776 19.601  1.00 34.02  ? 337 PRO A CG    1 
ATOM   2624 C  CD    . PRO A 1 337 ? 20.831  -10.406 18.540  1.00 33.10  ? 337 PRO A CD    1 
ATOM   2625 N  N     . GLY A 1 338 ? 18.545  -9.194  22.517  1.00 36.00  ? 338 GLY A N     1 
ATOM   2626 C  CA    . GLY A 1 338 ? 17.739  -8.178  23.157  1.00 33.67  ? 338 GLY A CA    1 
ATOM   2627 C  C     . GLY A 1 338 ? 16.256  -8.261  22.862  1.00 42.70  ? 338 GLY A C     1 
ATOM   2628 O  O     . GLY A 1 338 ? 15.465  -7.615  23.561  1.00 45.52  ? 338 GLY A O     1 
ATOM   2629 N  N     . THR A 1 339 ? 15.854  -9.034  21.856  1.00 36.33  ? 339 THR A N     1 
ATOM   2630 C  CA    . THR A 1 339 ? 14.446  -9.180  21.510  1.00 40.05  ? 339 THR A CA    1 
ATOM   2631 C  C     . THR A 1 339 ? 13.781  -10.146 22.482  1.00 41.96  ? 339 THR A C     1 
ATOM   2632 O  O     . THR A 1 339 ? 14.202  -11.302 22.600  1.00 43.01  ? 339 THR A O     1 
ATOM   2633 C  CB    . THR A 1 339 ? 14.297  -9.686  20.076  1.00 36.77  ? 339 THR A CB    1 
ATOM   2634 O  OG1   . THR A 1 339 ? 15.056  -8.851  19.194  1.00 30.97  ? 339 THR A OG1   1 
ATOM   2635 C  CG2   . THR A 1 339 ? 12.838  -9.673  19.650  1.00 40.69  ? 339 THR A CG2   1 
ATOM   2636 N  N     . SER A 1 340 ? 12.745  -9.678  23.174  1.00 40.64  ? 340 SER A N     1 
ATOM   2637 C  CA    . SER A 1 340 ? 11.987  -10.530 24.076  1.00 46.70  ? 340 SER A CA    1 
ATOM   2638 C  C     . SER A 1 340 ? 10.537  -10.070 24.095  1.00 47.85  ? 340 SER A C     1 
ATOM   2639 O  O     . SER A 1 340 ? 10.178  -9.043  23.514  1.00 46.99  ? 340 SER A O     1 
ATOM   2640 C  CB    . SER A 1 340 ? 12.574  -10.520 25.490  1.00 46.16  ? 340 SER A CB    1 
ATOM   2641 O  OG    . SER A 1 340 ? 12.373  -9.266  26.112  1.00 49.70  ? 340 SER A OG    1 
ATOM   2642 N  N     . VAL A 1 341 ? 9.702   -10.853 24.783  1.00 48.52  ? 341 VAL A N     1 
ATOM   2643 C  CA    . VAL A 1 341 ? 8.285   -10.523 24.907  1.00 50.13  ? 341 VAL A CA    1 
ATOM   2644 C  C     . VAL A 1 341 ? 8.098   -9.185  25.612  1.00 49.67  ? 341 VAL A C     1 
ATOM   2645 O  O     . VAL A 1 341 ? 7.087   -8.503  25.407  1.00 53.09  ? 341 VAL A O     1 
ATOM   2646 C  CB    . VAL A 1 341 ? 7.544   -11.662 25.639  1.00 56.40  ? 341 VAL A CB    1 
ATOM   2647 C  CG1   . VAL A 1 341 ? 6.040   -11.420 25.653  1.00 57.64  ? 341 VAL A CG1   1 
ATOM   2648 C  CG2   . VAL A 1 341 ? 7.861   -12.994 24.990  1.00 61.19  ? 341 VAL A CG2   1 
ATOM   2649 N  N     . LYS A 1 342 ? 9.063   -8.778  26.436  1.00 49.84  ? 342 LYS A N     1 
ATOM   2650 C  CA    . LYS A 1 342 ? 8.934   -7.527  27.171  1.00 49.78  ? 342 LYS A CA    1 
ATOM   2651 C  C     . LYS A 1 342 ? 9.477   -6.325  26.406  1.00 53.61  ? 342 LYS A C     1 
ATOM   2652 O  O     . LYS A 1 342 ? 8.976   -5.210  26.593  1.00 47.95  ? 342 LYS A O     1 
ATOM   2653 C  CB    . LYS A 1 342 ? 9.634   -7.635  28.530  1.00 60.66  ? 342 LYS A CB    1 
ATOM   2654 C  CG    . LYS A 1 342 ? 11.150  -7.550  28.481  1.00 67.30  ? 342 LYS A CG    1 
ATOM   2655 C  CD    . LYS A 1 342 ? 11.749  -7.625  29.878  1.00 85.42  ? 342 LYS A CD    1 
ATOM   2656 C  CE    . LYS A 1 342 ? 13.229  -7.275  29.868  1.00 93.66  ? 342 LYS A CE    1 
ATOM   2657 N  NZ    . LYS A 1 342 ? 13.462  -5.853  29.479  1.00 85.91  ? 342 LYS A NZ    1 
ATOM   2658 N  N     . THR A 1 343 ? 10.479  -6.517  25.547  1.00 48.38  ? 343 THR A N     1 
ATOM   2659 C  CA    . THR A 1 343 ? 11.060  -5.401  24.810  1.00 46.41  ? 343 THR A CA    1 
ATOM   2660 C  C     . THR A 1 343 ? 10.399  -5.194  23.454  1.00 47.40  ? 343 THR A C     1 
ATOM   2661 O  O     . THR A 1 343 ? 10.145  -4.052  23.059  1.00 50.65  ? 343 THR A O     1 
ATOM   2662 C  CB    . THR A 1 343 ? 12.564  -5.611  24.611  1.00 43.39  ? 343 THR A CB    1 
ATOM   2663 O  OG1   . THR A 1 343 ? 12.782  -6.762  23.783  1.00 40.83  ? 343 THR A OG1   1 
ATOM   2664 C  CG2   . THR A 1 343 ? 13.258  -5.806  25.947  1.00 53.49  ? 343 THR A CG2   1 
ATOM   2665 N  N     . ASN A 1 344 ? 10.117  -6.278  22.730  1.00 44.97  ? 344 ASN A N     1 
ATOM   2666 C  CA    . ASN A 1 344 ? 9.550   -6.190  21.384  1.00 40.80  ? 344 ASN A CA    1 
ATOM   2667 C  C     . ASN A 1 344 ? 8.630   -7.381  21.150  1.00 43.75  ? 344 ASN A C     1 
ATOM   2668 O  O     . ASN A 1 344 ? 8.916   -8.261  20.329  1.00 44.23  ? 344 ASN A O     1 
ATOM   2669 C  CB    . ASN A 1 344 ? 10.664  -6.138  20.338  1.00 37.25  ? 344 ASN A CB    1 
ATOM   2670 C  CG    . ASN A 1 344 ? 10.198  -5.573  19.014  1.00 36.27  ? 344 ASN A CG    1 
ATOM   2671 O  OD1   . ASN A 1 344 ? 8.999   -5.474  18.754  1.00 38.48  ? 344 ASN A OD1   1 
ATOM   2672 N  ND2   . ASN A 1 344 ? 11.149  -5.209  18.161  1.00 32.94  ? 344 ASN A ND2   1 
ATOM   2673 N  N     . PRO A 1 345 ? 7.498   -7.438  21.861  1.00 41.44  ? 345 PRO A N     1 
ATOM   2674 C  CA    . PRO A 1 345 ? 6.584   -8.578  21.678  1.00 45.28  ? 345 PRO A CA    1 
ATOM   2675 C  C     . PRO A 1 345 ? 6.034   -8.692  20.269  1.00 43.34  ? 345 PRO A C     1 
ATOM   2676 O  O     . PRO A 1 345 ? 5.751   -9.807  19.814  1.00 41.73  ? 345 PRO A O     1 
ATOM   2677 C  CB    . PRO A 1 345 ? 5.470   -8.304  22.699  1.00 47.30  ? 345 PRO A CB    1 
ATOM   2678 C  CG    . PRO A 1 345 ? 5.529   -6.829  22.938  1.00 44.20  ? 345 PRO A CG    1 
ATOM   2679 C  CD    . PRO A 1 345 ? 6.979   -6.468  22.842  1.00 45.98  ? 345 PRO A CD    1 
ATOM   2680 N  N     . ASN A 1 346 ? 5.877   -7.571  19.560  1.00 41.73  ? 346 ASN A N     1 
ATOM   2681 C  CA    . ASN A 1 346 ? 5.384   -7.629  18.188  1.00 43.13  ? 346 ASN A CA    1 
ATOM   2682 C  C     . ASN A 1 346 ? 6.387   -8.302  17.259  1.00 45.97  ? 346 ASN A C     1 
ATOM   2683 O  O     . ASN A 1 346 ? 5.989   -8.927  16.268  1.00 41.06  ? 346 ASN A O     1 
ATOM   2684 C  CB    . ASN A 1 346 ? 5.046   -6.221  17.697  1.00 42.03  ? 346 ASN A CB    1 
ATOM   2685 C  CG    . ASN A 1 346 ? 3.799   -5.661  18.357  1.00 45.43  ? 346 ASN A CG    1 
ATOM   2686 O  OD1   . ASN A 1 346 ? 2.793   -6.355  18.490  1.00 45.21  ? 346 ASN A OD1   1 
ATOM   2687 N  ND2   . ASN A 1 346 ? 3.864   -4.405  18.784  1.00 39.25  ? 346 ASN A ND2   1 
ATOM   2688 N  N     . ALA A 1 347 ? 7.683   -8.191  17.561  1.00 38.55  ? 347 ALA A N     1 
ATOM   2689 C  CA    . ALA A 1 347 ? 8.680   -8.920  16.785  1.00 42.17  ? 347 ALA A CA    1 
ATOM   2690 C  C     . ALA A 1 347 ? 8.601   -10.416 17.060  1.00 39.03  ? 347 ALA A C     1 
ATOM   2691 O  O     . ALA A 1 347 ? 8.745   -11.227 16.138  1.00 38.49  ? 347 ALA A O     1 
ATOM   2692 C  CB    . ALA A 1 347 ? 10.082  -8.394  17.089  1.00 34.81  ? 347 ALA A CB    1 
ATOM   2693 N  N     . ILE A 1 348 ? 8.372   -10.797 18.322  1.00 40.33  ? 348 ILE A N     1 
ATOM   2694 C  CA    . ILE A 1 348 ? 8.269   -12.211 18.678  1.00 36.88  ? 348 ILE A CA    1 
ATOM   2695 C  C     . ILE A 1 348 ? 7.134   -12.874 17.909  1.00 43.34  ? 348 ILE A C     1 
ATOM   2696 O  O     . ILE A 1 348 ? 7.277   -13.995 17.403  1.00 41.79  ? 348 ILE A O     1 
ATOM   2697 C  CB    . ILE A 1 348 ? 8.088   -12.369 20.199  1.00 43.93  ? 348 ILE A CB    1 
ATOM   2698 C  CG1   . ILE A 1 348 ? 9.317   -11.845 20.948  1.00 47.67  ? 348 ILE A CG1   1 
ATOM   2699 C  CG2   . ILE A 1 348 ? 7.834   -13.824 20.560  1.00 52.27  ? 348 ILE A CG2   1 
ATOM   2700 C  CD1   . ILE A 1 348 ? 10.564  -12.674 20.728  1.00 49.58  ? 348 ILE A CD1   1 
ATOM   2701 N  N     . LYS A 1 349 ? 5.989   -12.194 17.804  1.00 40.98  ? 349 LYS A N     1 
ATOM   2702 C  CA    . LYS A 1 349 ? 4.870   -12.747 17.047  1.00 43.23  ? 349 LYS A CA    1 
ATOM   2703 C  C     . LYS A 1 349 ? 5.206   -12.893 15.569  1.00 40.43  ? 349 LYS A C     1 
ATOM   2704 O  O     . LYS A 1 349 ? 4.675   -13.786 14.898  1.00 45.68  ? 349 LYS A O     1 
ATOM   2705 C  CB    . LYS A 1 349 ? 3.631   -11.869 17.219  1.00 43.68  ? 349 LYS A CB    1 
ATOM   2706 C  CG    . LYS A 1 349 ? 3.074   -11.834 18.632  1.00 57.73  ? 349 LYS A CG    1 
ATOM   2707 C  CD    . LYS A 1 349 ? 1.814   -10.984 18.704  1.00 59.54  ? 349 LYS A CD    1 
ATOM   2708 C  CE    . LYS A 1 349 ? 1.181   -11.050 20.084  1.00 69.76  ? 349 LYS A CE    1 
ATOM   2709 N  NZ    . LYS A 1 349 ? -0.085  -10.270 20.151  1.00 78.94  ? 349 LYS A NZ    1 
ATOM   2710 N  N     . THR A 1 350 ? 6.088   -12.039 15.046  1.00 40.57  ? 350 THR A N     1 
ATOM   2711 C  CA    . THR A 1 350 ? 6.360   -12.027 13.613  1.00 37.93  ? 350 THR A CA    1 
ATOM   2712 C  C     . THR A 1 350 ? 7.328   -13.132 13.201  1.00 37.28  ? 350 THR A C     1 
ATOM   2713 O  O     . THR A 1 350 ? 7.165   -13.733 12.133  1.00 35.28  ? 350 THR A O     1 
ATOM   2714 C  CB    . THR A 1 350 ? 6.919   -10.662 13.200  1.00 43.32  ? 350 THR A CB    1 
ATOM   2715 O  OG1   . THR A 1 350 ? 6.028   -9.627  13.633  1.00 43.31  ? 350 THR A OG1   1 
ATOM   2716 C  CG2   . THR A 1 350 ? 7.084   -10.581 11.687  1.00 37.12  ? 350 THR A CG2   1 
ATOM   2717 N  N     . ILE A 1 351 ? 8.332   -13.419 14.029  1.00 35.87  ? 351 ILE A N     1 
ATOM   2718 C  CA    . ILE A 1 351 ? 9.468   -14.232 13.603  1.00 35.92  ? 351 ILE A CA    1 
ATOM   2719 C  C     . ILE A 1 351 ? 9.216   -15.721 13.805  1.00 38.74  ? 351 ILE A C     1 
ATOM   2720 O  O     . ILE A 1 351 ? 10.128  -16.538 13.638  1.00 39.75  ? 351 ILE A O     1 
ATOM   2721 C  CB    . ILE A 1 351 ? 10.751  -13.805 14.342  1.00 31.79  ? 351 ILE A CB    1 
ATOM   2722 C  CG1   . ILE A 1 351 ? 10.587  -13.998 15.851  1.00 35.28  ? 351 ILE A CG1   1 
ATOM   2723 C  CG2   . ILE A 1 351 ? 11.101  -12.364 14.011  1.00 27.75  ? 351 ILE A CG2   1 
ATOM   2724 C  CD1   . ILE A 1 351 ? 11.840  -13.689 16.648  1.00 36.69  ? 351 ILE A CD1   1 
ATOM   2725 N  N     . GLN A 1 352 ? 7.989   -16.093 14.153  1.00 36.38  ? 352 GLN A N     1 
ATOM   2726 C  CA    . GLN A 1 352 ? 7.691   -17.487 14.458  1.00 41.98  ? 352 GLN A CA    1 
ATOM   2727 C  C     . GLN A 1 352 ? 7.310   -18.314 13.235  1.00 39.54  ? 352 GLN A C     1 
ATOM   2728 O  O     . GLN A 1 352 ? 7.018   -19.504 13.383  1.00 43.46  ? 352 GLN A O     1 
ATOM   2729 C  CB    . GLN A 1 352 ? 6.577   -17.571 15.504  1.00 44.72  ? 352 GLN A CB    1 
ATOM   2730 C  CG    . GLN A 1 352 ? 7.013   -17.102 16.877  1.00 51.42  ? 352 GLN A CG    1 
ATOM   2731 C  CD    . GLN A 1 352 ? 5.986   -17.389 17.948  1.00 60.86  ? 352 GLN A CD    1 
ATOM   2732 O  OE1   . GLN A 1 352 ? 4.900   -17.896 17.666  1.00 72.46  ? 352 GLN A OE1   1 
ATOM   2733 N  NE2   . GLN A 1 352 ? 6.325   -17.069 19.189  1.00 66.14  ? 352 GLN A NE2   1 
ATOM   2734 N  N     . LYS A 1 353 ? 7.314   -17.731 12.039  1.00 37.41  ? 353 LYS A N     1 
ATOM   2735 C  CA    . LYS A 1 353 ? 7.025   -18.499 10.838  1.00 38.40  ? 353 LYS A CA    1 
ATOM   2736 C  C     . LYS A 1 353 ? 7.654   -17.823 9.627   1.00 37.73  ? 353 LYS A C     1 
ATOM   2737 O  O     . LYS A 1 353 ? 7.764   -16.595 9.570   1.00 40.37  ? 353 LYS A O     1 
ATOM   2738 C  CB    . LYS A 1 353 ? 5.515   -18.682 10.630  1.00 43.60  ? 353 LYS A CB    1 
ATOM   2739 C  CG    . LYS A 1 353 ? 4.720   -17.389 10.566  1.00 47.21  ? 353 LYS A CG    1 
ATOM   2740 C  CD    . LYS A 1 353 ? 3.225   -17.672 10.491  1.00 61.45  ? 353 LYS A CD    1 
ATOM   2741 C  CE    . LYS A 1 353 ? 2.416   -16.385 10.427  1.00 61.87  ? 353 LYS A CE    1 
ATOM   2742 N  NZ    . LYS A 1 353 ? 0.951   -16.647 10.460  1.00 78.89  ? 353 LYS A NZ    1 
ATOM   2743 N  N     . ASN A 1 354 ? 8.082   -18.651 8.668   1.00 36.51  ? 354 ASN A N     1 
ATOM   2744 C  CA    . ASN A 1 354 ? 8.621   -18.184 7.387   1.00 36.72  ? 354 ASN A CA    1 
ATOM   2745 C  C     . ASN A 1 354 ? 9.817   -17.255 7.582   1.00 35.40  ? 354 ASN A C     1 
ATOM   2746 O  O     . ASN A 1 354 ? 9.999   -16.285 6.843   1.00 37.45  ? 354 ASN A O     1 
ATOM   2747 C  CB    . ASN A 1 354 ? 7.536   -17.496 6.555   1.00 42.27  ? 354 ASN A CB    1 
ATOM   2748 C  CG    . ASN A 1 354 ? 6.313   -18.367 6.357   1.00 42.02  ? 354 ASN A CG    1 
ATOM   2749 O  OD1   . ASN A 1 354 ? 6.422   -19.542 6.003   1.00 41.82  ? 354 ASN A OD1   1 
ATOM   2750 N  ND2   . ASN A 1 354 ? 5.137   -17.797 6.594   1.00 45.58  ? 354 ASN A ND2   1 
ATOM   2751 N  N     . THR A 1 355 ? 10.651  -17.559 8.574   1.00 31.91  ? 355 THR A N     1 
ATOM   2752 C  CA    . THR A 1 355 ? 11.721  -16.664 8.992   1.00 32.75  ? 355 THR A CA    1 
ATOM   2753 C  C     . THR A 1 355 ? 13.060  -17.385 8.951   1.00 31.90  ? 355 THR A C     1 
ATOM   2754 O  O     . THR A 1 355 ? 13.173  -18.533 9.389   1.00 30.04  ? 355 THR A O     1 
ATOM   2755 C  CB    . THR A 1 355 ? 11.457  -16.120 10.404  1.00 33.57  ? 355 THR A CB    1 
ATOM   2756 O  OG1   . THR A 1 355 ? 10.294  -15.288 10.378  1.00 33.04  ? 355 THR A OG1   1 
ATOM   2757 C  CG2   . THR A 1 355 ? 12.641  -15.305 10.913  1.00 27.88  ? 355 THR A CG2   1 
ATOM   2758 N  N     . ILE A 1 356 ? 14.072  -16.702 8.422   1.00 29.82  ? 356 ILE A N     1 
ATOM   2759 C  CA    . ILE A 1 356 ? 15.437  -17.211 8.382   1.00 28.85  ? 356 ILE A CA    1 
ATOM   2760 C  C     . ILE A 1 356 ? 16.245  -16.500 9.459   1.00 28.19  ? 356 ILE A C     1 
ATOM   2761 O  O     . ILE A 1 356 ? 16.324  -15.266 9.474   1.00 31.97  ? 356 ILE A O     1 
ATOM   2762 C  CB    . ILE A 1 356 ? 16.073  -17.013 6.997   1.00 30.88  ? 356 ILE A CB    1 
ATOM   2763 C  CG1   . ILE A 1 356 ? 15.293  -17.790 5.934   1.00 33.62  ? 356 ILE A CG1   1 
ATOM   2764 C  CG2   . ILE A 1 356 ? 17.536  -17.449 7.015   1.00 25.72  ? 356 ILE A CG2   1 
ATOM   2765 C  CD1   . ILE A 1 356 ? 15.888  -17.687 4.542   1.00 35.03  ? 356 ILE A CD1   1 
ATOM   2766 N  N     . PHE A 1 357 ? 16.841  -17.275 10.362  1.00 26.37  ? 357 PHE A N     1 
ATOM   2767 C  CA    . PHE A 1 357 ? 17.728  -16.749 11.391  1.00 27.26  ? 357 PHE A CA    1 
ATOM   2768 C  C     . PHE A 1 357 ? 19.175  -16.987 10.982  1.00 30.37  ? 357 PHE A C     1 
ATOM   2769 O  O     . PHE A 1 357 ? 19.499  -18.019 10.389  1.00 30.99  ? 357 PHE A O     1 
ATOM   2770 C  CB    . PHE A 1 357 ? 17.471  -17.411 12.749  1.00 26.98  ? 357 PHE A CB    1 
ATOM   2771 C  CG    . PHE A 1 357 ? 16.121  -17.111 13.336  1.00 28.76  ? 357 PHE A CG    1 
ATOM   2772 C  CD1   . PHE A 1 357 ? 15.934  -16.000 14.144  1.00 35.38  ? 357 PHE A CD1   1 
ATOM   2773 C  CD2   . PHE A 1 357 ? 15.044  -17.950 13.097  1.00 29.01  ? 357 PHE A CD2   1 
ATOM   2774 C  CE1   . PHE A 1 357 ? 14.692  -15.723 14.694  1.00 32.63  ? 357 PHE A CE1   1 
ATOM   2775 C  CE2   . PHE A 1 357 ? 13.799  -17.680 13.644  1.00 33.75  ? 357 PHE A CE2   1 
ATOM   2776 C  CZ    . PHE A 1 357 ? 13.623  -16.565 14.442  1.00 30.37  ? 357 PHE A CZ    1 
ATOM   2777 N  N     . THR A 1 358 ? 20.044  -16.034 11.309  1.00 29.06  ? 358 THR A N     1 
ATOM   2778 C  CA    . THR A 1 358 ? 21.470  -16.156 11.036  1.00 31.44  ? 358 THR A CA    1 
ATOM   2779 C  C     . THR A 1 358 ? 22.240  -15.888 12.320  1.00 26.39  ? 358 THR A C     1 
ATOM   2780 O  O     . THR A 1 358 ? 22.099  -14.816 12.917  1.00 28.89  ? 358 THR A O     1 
ATOM   2781 C  CB    . THR A 1 358 ? 21.910  -15.186 9.933   1.00 31.97  ? 358 THR A CB    1 
ATOM   2782 O  OG1   . THR A 1 358 ? 21.132  -15.419 8.750   1.00 32.99  ? 358 THR A OG1   1 
ATOM   2783 C  CG2   . THR A 1 358 ? 23.375  -15.384 9.604   1.00 31.74  ? 358 THR A CG2   1 
ATOM   2784 N  N     . ASN A 1 359 ? 23.021  -16.880 12.755  1.00 32.81  ? 359 ASN A N     1 
ATOM   2785 C  CA    . ASN A 1 359 ? 24.013  -16.739 13.826  1.00 32.53  ? 359 ASN A CA    1 
ATOM   2786 C  C     . ASN A 1 359 ? 23.386  -16.595 15.209  1.00 35.41  ? 359 ASN A C     1 
ATOM   2787 O  O     . ASN A 1 359 ? 24.001  -16.021 16.116  1.00 34.29  ? 359 ASN A O     1 
ATOM   2788 C  CB    . ASN A 1 359 ? 24.968  -15.568 13.551  1.00 30.00  ? 359 ASN A CB    1 
ATOM   2789 C  CG    . ASN A 1 359 ? 25.993  -15.885 12.479  1.00 30.01  ? 359 ASN A CG    1 
ATOM   2790 O  OD1   . ASN A 1 359 ? 26.228  -17.046 12.149  1.00 29.48  ? 359 ASN A OD1   1 
ATOM   2791 N  ND2   . ASN A 1 359 ? 26.619  -14.847 11.940  1.00 34.45  ? 359 ASN A ND2   1 
ATOM   2792 N  N     . VAL A 1 360 ? 22.173  -17.100 15.403  1.00 35.10  ? 360 VAL A N     1 
ATOM   2793 C  CA    . VAL A 1 360 ? 21.608  -17.226 16.734  1.00 35.21  ? 360 VAL A CA    1 
ATOM   2794 C  C     . VAL A 1 360 ? 21.840  -18.651 17.224  1.00 39.50  ? 360 VAL A C     1 
ATOM   2795 O  O     . VAL A 1 360 ? 22.315  -19.514 16.490  1.00 35.72  ? 360 VAL A O     1 
ATOM   2796 C  CB    . VAL A 1 360 ? 20.099  -16.851 16.773  1.00 30.70  ? 360 VAL A CB    1 
ATOM   2797 C  CG1   . VAL A 1 360 ? 19.886  -15.432 16.283  1.00 28.38  ? 360 VAL A CG1   1 
ATOM   2798 C  CG2   . VAL A 1 360 ? 19.257  -17.848 15.986  1.00 29.58  ? 360 VAL A CG2   1 
ATOM   2799 N  N     . ALA A 1 361 ? 21.520  -18.897 18.490  1.00 41.06  ? 361 ALA A N     1 
ATOM   2800 C  CA    . ALA A 1 361 ? 21.697  -20.211 19.081  1.00 37.19  ? 361 ALA A CA    1 
ATOM   2801 C  C     . ALA A 1 361 ? 20.470  -21.073 18.827  1.00 37.68  ? 361 ALA A C     1 
ATOM   2802 O  O     . ALA A 1 361 ? 19.352  -20.571 18.686  1.00 38.21  ? 361 ALA A O     1 
ATOM   2803 C  CB    . ALA A 1 361 ? 21.953  -20.098 20.588  1.00 39.60  ? 361 ALA A CB    1 
ATOM   2804 N  N     . GLU A 1 362 ? 20.693  -22.382 18.757  1.00 36.52  ? 362 GLU A N     1 
ATOM   2805 C  CA    . GLU A 1 362 ? 19.628  -23.354 18.561  1.00 44.57  ? 362 GLU A CA    1 
ATOM   2806 C  C     . GLU A 1 362 ? 19.426  -24.155 19.837  1.00 46.02  ? 362 GLU A C     1 
ATOM   2807 O  O     . GLU A 1 362 ? 20.396  -24.590 20.468  1.00 50.54  ? 362 GLU A O     1 
ATOM   2808 C  CB    . GLU A 1 362 ? 19.947  -24.303 17.401  1.00 41.97  ? 362 GLU A CB    1 
ATOM   2809 C  CG    . GLU A 1 362 ? 18.878  -25.355 17.153  1.00 43.11  ? 362 GLU A CG    1 
ATOM   2810 C  CD    . GLU A 1 362 ? 19.212  -26.274 15.990  1.00 51.56  ? 362 GLU A CD    1 
ATOM   2811 O  OE1   . GLU A 1 362 ? 20.305  -26.130 15.406  1.00 52.95  ? 362 GLU A OE1   1 
ATOM   2812 O  OE2   . GLU A 1 362 ? 18.377  -27.142 15.659  1.00 53.20  ? 362 GLU A OE2   1 
ATOM   2813 N  N     . THR A 1 363 ? 18.169  -24.341 20.221  1.00 42.74  ? 363 THR A N     1 
ATOM   2814 C  CA    . THR A 1 363 ? 17.852  -25.204 21.347  1.00 48.68  ? 363 THR A CA    1 
ATOM   2815 C  C     . THR A 1 363 ? 17.585  -26.623 20.855  1.00 47.79  ? 363 THR A C     1 
ATOM   2816 O  O     . THR A 1 363 ? 17.223  -26.850 19.698  1.00 45.69  ? 363 THR A O     1 
ATOM   2817 C  CB    . THR A 1 363 ? 16.645  -24.676 22.124  1.00 46.77  ? 363 THR A CB    1 
ATOM   2818 O  OG1   . THR A 1 363 ? 15.496  -24.652 21.272  1.00 47.06  ? 363 THR A OG1   1 
ATOM   2819 C  CG2   . THR A 1 363 ? 16.917  -23.272 22.634  1.00 51.46  ? 363 THR A CG2   1 
ATOM   2820 N  N     . SER A 1 364 ? 17.774  -27.586 21.761  1.00 52.14  ? 364 SER A N     1 
ATOM   2821 C  CA    . SER A 1 364 ? 17.675  -28.993 21.392  1.00 54.86  ? 364 SER A CA    1 
ATOM   2822 C  C     . SER A 1 364 ? 16.278  -29.382 20.931  1.00 52.48  ? 364 SER A C     1 
ATOM   2823 O  O     . SER A 1 364 ? 16.137  -30.353 20.179  1.00 52.03  ? 364 SER A O     1 
ATOM   2824 C  CB    . SER A 1 364 ? 18.100  -29.875 22.567  1.00 49.00  ? 364 SER A CB    1 
ATOM   2825 O  OG    . SER A 1 364 ? 17.338  -29.578 23.723  1.00 56.19  ? 364 SER A OG    1 
ATOM   2826 N  N     . ASP A 1 365 ? 15.245  -28.658 21.358  1.00 50.72  ? 365 ASP A N     1 
ATOM   2827 C  CA    . ASP A 1 365 ? 13.886  -28.934 20.914  1.00 55.10  ? 365 ASP A CA    1 
ATOM   2828 C  C     . ASP A 1 365 ? 13.524  -28.192 19.632  1.00 48.42  ? 365 ASP A C     1 
ATOM   2829 O  O     . ASP A 1 365 ? 12.344  -28.140 19.274  1.00 50.74  ? 365 ASP A O     1 
ATOM   2830 C  CB    . ASP A 1 365 ? 12.882  -28.597 22.022  1.00 53.45  ? 365 ASP A CB    1 
ATOM   2831 C  CG    . ASP A 1 365 ? 12.962  -27.149 22.469  1.00 58.29  ? 365 ASP A CG    1 
ATOM   2832 O  OD1   . ASP A 1 365 ? 13.887  -26.433 22.034  1.00 54.35  ? 365 ASP A OD1   1 
ATOM   2833 O  OD2   . ASP A 1 365 ? 12.091  -26.728 23.260  1.00 62.78  ? 365 ASP A OD2   1 
ATOM   2834 N  N     . GLY A 1 366 ? 14.507  -27.618 18.943  1.00 51.63  ? 366 GLY A N     1 
ATOM   2835 C  CA    . GLY A 1 366 ? 14.272  -26.994 17.657  1.00 48.33  ? 366 GLY A CA    1 
ATOM   2836 C  C     . GLY A 1 366 ? 13.937  -25.522 17.689  1.00 47.32  ? 366 GLY A C     1 
ATOM   2837 O  O     . GLY A 1 366 ? 13.432  -25.000 16.689  1.00 47.04  ? 366 GLY A O     1 
ATOM   2838 N  N     . GLY A 1 367 ? 14.198  -24.833 18.800  1.00 45.89  ? 367 GLY A N     1 
ATOM   2839 C  CA    . GLY A 1 367 ? 13.923  -23.419 18.916  1.00 45.15  ? 367 GLY A CA    1 
ATOM   2840 C  C     . GLY A 1 367 ? 15.177  -22.569 18.804  1.00 42.76  ? 367 GLY A C     1 
ATOM   2841 O  O     . GLY A 1 367 ? 16.274  -23.048 18.505  1.00 38.69  ? 367 GLY A O     1 
ATOM   2842 N  N     . VAL A 1 368 ? 15.000  -21.277 19.055  1.00 40.43  ? 368 VAL A N     1 
ATOM   2843 C  CA    . VAL A 1 368 ? 16.082  -20.308 18.965  1.00 42.65  ? 368 VAL A CA    1 
ATOM   2844 C  C     . VAL A 1 368 ? 16.378  -19.762 20.354  1.00 45.04  ? 368 VAL A C     1 
ATOM   2845 O  O     . VAL A 1 368 ? 15.549  -19.816 21.268  1.00 45.33  ? 368 VAL A O     1 
ATOM   2846 C  CB    . VAL A 1 368 ? 15.753  -19.161 17.986  1.00 42.04  ? 368 VAL A CB    1 
ATOM   2847 C  CG1   . VAL A 1 368 ? 15.692  -19.682 16.559  1.00 35.84  ? 368 VAL A CG1   1 
ATOM   2848 C  CG2   . VAL A 1 368 ? 14.440  -18.493 18.371  1.00 37.46  ? 368 VAL A CG2   1 
ATOM   2849 N  N     . TYR A 1 369 ? 17.586  -19.225 20.510  1.00 39.47  ? 369 TYR A N     1 
ATOM   2850 C  CA    . TYR A 1 369 ? 17.975  -18.617 21.772  1.00 41.99  ? 369 TYR A CA    1 
ATOM   2851 C  C     . TYR A 1 369 ? 19.015  -17.537 21.513  1.00 40.81  ? 369 TYR A C     1 
ATOM   2852 O  O     . TYR A 1 369 ? 19.817  -17.635 20.580  1.00 39.48  ? 369 TYR A O     1 
ATOM   2853 C  CB    . TYR A 1 369 ? 18.521  -19.656 22.756  1.00 42.52  ? 369 TYR A CB    1 
ATOM   2854 C  CG    . TYR A 1 369 ? 18.150  -19.365 24.189  1.00 43.14  ? 369 TYR A CG    1 
ATOM   2855 C  CD1   . TYR A 1 369 ? 16.865  -19.614 24.653  1.00 49.91  ? 369 TYR A CD1   1 
ATOM   2856 C  CD2   . TYR A 1 369 ? 19.080  -18.842 25.079  1.00 43.02  ? 369 TYR A CD2   1 
ATOM   2857 C  CE1   . TYR A 1 369 ? 16.512  -19.352 25.963  1.00 46.63  ? 369 TYR A CE1   1 
ATOM   2858 C  CE2   . TYR A 1 369 ? 18.736  -18.576 26.392  1.00 43.71  ? 369 TYR A CE2   1 
ATOM   2859 C  CZ    . TYR A 1 369 ? 17.450  -18.833 26.826  1.00 44.53  ? 369 TYR A CZ    1 
ATOM   2860 O  OH    . TYR A 1 369 ? 17.099  -18.572 28.130  1.00 55.62  ? 369 TYR A OH    1 
ATOM   2861 N  N     . TRP A 1 370 ? 18.985  -16.503 22.348  1.00 39.30  ? 370 TRP A N     1 
ATOM   2862 C  CA    . TRP A 1 370 ? 19.957  -15.421 22.271  1.00 45.97  ? 370 TRP A CA    1 
ATOM   2863 C  C     . TRP A 1 370 ? 19.937  -14.656 23.586  1.00 43.72  ? 370 TRP A C     1 
ATOM   2864 O  O     . TRP A 1 370 ? 19.021  -14.801 24.399  1.00 40.84  ? 370 TRP A O     1 
ATOM   2865 C  CB    . TRP A 1 370 ? 19.679  -14.485 21.088  1.00 36.52  ? 370 TRP A CB    1 
ATOM   2866 C  CG    . TRP A 1 370 ? 18.264  -13.999 20.995  1.00 39.53  ? 370 TRP A CG    1 
ATOM   2867 C  CD1   . TRP A 1 370 ? 17.639  -13.121 21.833  1.00 39.02  ? 370 TRP A CD1   1 
ATOM   2868 C  CD2   . TRP A 1 370 ? 17.304  -14.347 19.991  1.00 33.07  ? 370 TRP A CD2   1 
ATOM   2869 N  NE1   . TRP A 1 370 ? 16.345  -12.910 21.419  1.00 34.79  ? 370 TRP A NE1   1 
ATOM   2870 C  CE2   . TRP A 1 370 ? 16.115  -13.651 20.290  1.00 31.39  ? 370 TRP A CE2   1 
ATOM   2871 C  CE3   . TRP A 1 370 ? 17.331  -15.186 18.873  1.00 35.81  ? 370 TRP A CE3   1 
ATOM   2872 C  CZ2   . TRP A 1 370 ? 14.966  -13.765 19.509  1.00 33.20  ? 370 TRP A CZ2   1 
ATOM   2873 C  CZ3   . TRP A 1 370 ? 16.190  -15.297 18.098  1.00 30.90  ? 370 TRP A CZ3   1 
ATOM   2874 C  CH2   . TRP A 1 370 ? 15.024  -14.591 18.421  1.00 33.98  ? 370 TRP A CH2   1 
ATOM   2875 N  N     . GLU A 1 371 ? 20.966  -13.836 23.779  1.00 42.52  ? 371 GLU A N     1 
ATOM   2876 C  CA    . GLU A 1 371 ? 21.046  -12.995 24.965  1.00 47.03  ? 371 GLU A CA    1 
ATOM   2877 C  C     . GLU A 1 371 ? 19.885  -12.009 24.991  1.00 44.64  ? 371 GLU A C     1 
ATOM   2878 O  O     . GLU A 1 371 ? 19.583  -11.358 23.986  1.00 41.22  ? 371 GLU A O     1 
ATOM   2879 C  CB    . GLU A 1 371 ? 22.381  -12.248 24.993  1.00 43.60  ? 371 GLU A CB    1 
ATOM   2880 C  CG    . GLU A 1 371 ? 23.560  -13.067 25.515  1.00 41.71  ? 371 GLU A CG    1 
ATOM   2881 C  CD    . GLU A 1 371 ? 23.950  -14.219 24.603  1.00 49.80  ? 371 GLU A CD    1 
ATOM   2882 O  OE1   . GLU A 1 371 ? 23.598  -14.192 23.402  1.00 46.57  ? 371 GLU A OE1   1 
ATOM   2883 O  OE2   . GLU A 1 371 ? 24.612  -15.158 25.093  1.00 50.67  ? 371 GLU A OE2   1 
ATOM   2884 N  N     . GLY A 1 372 ? 19.226  -11.909 26.143  1.00 44.09  ? 372 GLY A N     1 
ATOM   2885 C  CA    . GLY A 1 372 ? 18.103  -11.011 26.307  1.00 43.19  ? 372 GLY A CA    1 
ATOM   2886 C  C     . GLY A 1 372 ? 16.753  -11.584 25.933  1.00 47.28  ? 372 GLY A C     1 
ATOM   2887 O  O     . GLY A 1 372 ? 15.747  -10.870 26.043  1.00 45.01  ? 372 GLY A O     1 
ATOM   2888 N  N     . ILE A 1 373 ? 16.691  -12.846 25.500  1.00 45.58  ? 373 ILE A N     1 
ATOM   2889 C  CA    . ILE A 1 373 ? 15.414  -13.452 25.140  1.00 45.77  ? 373 ILE A CA    1 
ATOM   2890 C  C     . ILE A 1 373 ? 14.500  -13.573 26.351  1.00 43.83  ? 373 ILE A C     1 
ATOM   2891 O  O     . ILE A 1 373 ? 13.274  -13.629 26.200  1.00 45.66  ? 373 ILE A O     1 
ATOM   2892 C  CB    . ILE A 1 373 ? 15.647  -14.822 24.464  1.00 42.21  ? 373 ILE A CB    1 
ATOM   2893 C  CG1   . ILE A 1 373 ? 14.370  -15.319 23.784  1.00 44.87  ? 373 ILE A CG1   1 
ATOM   2894 C  CG2   . ILE A 1 373 ? 16.148  -15.846 25.471  1.00 46.19  ? 373 ILE A CG2   1 
ATOM   2895 C  CD1   . ILE A 1 373 ? 14.585  -16.542 22.915  1.00 48.38  ? 373 ILE A CD1   1 
ATOM   2896 N  N     . ASP A 1 374 ? 15.071  -13.618 27.556  1.00 46.54  ? 374 ASP A N     1 
ATOM   2897 C  CA    . ASP A 1 374 ? 14.339  -13.512 28.817  1.00 52.96  ? 374 ASP A CA    1 
ATOM   2898 C  C     . ASP A 1 374 ? 13.326  -14.638 29.015  1.00 55.40  ? 374 ASP A C     1 
ATOM   2899 O  O     . ASP A 1 374 ? 12.402  -14.510 29.823  1.00 63.48  ? 374 ASP A O     1 
ATOM   2900 C  CB    . ASP A 1 374 ? 13.645  -12.148 28.931  1.00 56.64  ? 374 ASP A CB    1 
ATOM   2901 C  CG    . ASP A 1 374 ? 13.450  -11.710 30.368  1.00 77.34  ? 374 ASP A CG    1 
ATOM   2902 O  OD1   . ASP A 1 374 ? 13.781  -12.492 31.284  1.00 80.51  ? 374 ASP A OD1   1 
ATOM   2903 O  OD2   . ASP A 1 374 ? 12.968  -10.578 30.583  1.00 90.38  ? 374 ASP A OD2   1 
ATOM   2904 N  N     . GLU A 1 375 ? 13.478  -15.751 28.298  1.00 52.74  ? 375 GLU A N     1 
ATOM   2905 C  CA    . GLU A 1 375 ? 12.588  -16.892 28.458  1.00 52.93  ? 375 GLU A CA    1 
ATOM   2906 C  C     . GLU A 1 375 ? 13.363  -18.064 29.036  1.00 53.85  ? 375 GLU A C     1 
ATOM   2907 O  O     . GLU A 1 375 ? 14.383  -18.468 28.456  1.00 54.31  ? 375 GLU A O     1 
ATOM   2908 C  CB    . GLU A 1 375 ? 11.953  -17.289 27.126  1.00 56.01  ? 375 GLU A CB    1 
ATOM   2909 C  CG    . GLU A 1 375 ? 10.965  -16.282 26.571  1.00 59.06  ? 375 GLU A CG    1 
ATOM   2910 C  CD    . GLU A 1 375 ? 10.122  -16.861 25.451  1.00 59.18  ? 375 GLU A CD    1 
ATOM   2911 O  OE1   . GLU A 1 375 ? 9.606   -17.986 25.617  1.00 58.69  ? 375 GLU A OE1   1 
ATOM   2912 O  OE2   . GLU A 1 375 ? 9.983   -16.199 24.402  1.00 52.38  ? 375 GLU A OE2   1 
ATOM   2913 N  N     . PRO A 1 376 ? 12.932  -18.636 30.156  1.00 54.18  ? 376 PRO A N     1 
ATOM   2914 C  CA    . PRO A 1 376 ? 13.595  -19.838 30.665  1.00 53.85  ? 376 PRO A CA    1 
ATOM   2915 C  C     . PRO A 1 376 ? 13.272  -21.043 29.800  1.00 58.50  ? 376 PRO A C     1 
ATOM   2916 O  O     . PRO A 1 376 ? 12.205  -21.132 29.187  1.00 58.45  ? 376 PRO A O     1 
ATOM   2917 C  CB    . PRO A 1 376 ? 13.015  -19.993 32.074  1.00 55.72  ? 376 PRO A CB    1 
ATOM   2918 C  CG    . PRO A 1 376 ? 11.668  -19.359 31.981  1.00 58.03  ? 376 PRO A CG    1 
ATOM   2919 C  CD    . PRO A 1 376 ? 11.822  -18.206 31.024  1.00 55.16  ? 376 PRO A CD    1 
ATOM   2920 N  N     . LEU A 1 377 ? 14.216  -21.974 29.749  1.00 59.59  ? 377 LEU A N     1 
ATOM   2921 C  CA    . LEU A 1 377 ? 14.044  -23.214 29.012  1.00 62.15  ? 377 LEU A CA    1 
ATOM   2922 C  C     . LEU A 1 377 ? 13.576  -24.325 29.944  1.00 65.36  ? 377 LEU A C     1 
ATOM   2923 O  O     . LEU A 1 377 ? 13.795  -24.290 31.158  1.00 61.01  ? 377 LEU A O     1 
ATOM   2924 C  CB    . LEU A 1 377 ? 15.347  -23.622 28.320  1.00 59.49  ? 377 LEU A CB    1 
ATOM   2925 C  CG    . LEU A 1 377 ? 15.793  -22.741 27.153  1.00 54.37  ? 377 LEU A CG    1 
ATOM   2926 C  CD1   . LEU A 1 377 ? 17.126  -23.218 26.607  1.00 56.53  ? 377 LEU A CD1   1 
ATOM   2927 C  CD2   . LEU A 1 377 ? 14.737  -22.726 26.059  1.00 56.09  ? 377 LEU A CD2   1 
ATOM   2928 N  N     . ALA A 1 378 ? 12.913  -25.316 29.355  1.00 63.66  ? 378 ALA A N     1 
ATOM   2929 C  CA    . ALA A 1 378 ? 12.461  -26.462 30.121  1.00 70.97  ? 378 ALA A CA    1 
ATOM   2930 C  C     . ALA A 1 378 ? 13.658  -27.308 30.554  1.00 68.40  ? 378 ALA A C     1 
ATOM   2931 O  O     . ALA A 1 378 ? 14.718  -27.265 29.923  1.00 66.40  ? 378 ALA A O     1 
ATOM   2932 C  CB    . ALA A 1 378 ? 11.494  -27.309 29.297  1.00 66.23  ? 378 ALA A CB    1 
ATOM   2933 N  N     . PRO A 1 379 ? 13.522  -28.068 31.641  1.00 67.73  ? 379 PRO A N     1 
ATOM   2934 C  CA    . PRO A 1 379 ? 14.605  -28.973 32.043  1.00 64.98  ? 379 PRO A CA    1 
ATOM   2935 C  C     . PRO A 1 379 ? 14.965  -29.940 30.925  1.00 63.83  ? 379 PRO A C     1 
ATOM   2936 O  O     . PRO A 1 379 ? 14.101  -30.422 30.190  1.00 63.06  ? 379 PRO A O     1 
ATOM   2937 C  CB    . PRO A 1 379 ? 14.021  -29.705 33.256  1.00 68.58  ? 379 PRO A CB    1 
ATOM   2938 C  CG    . PRO A 1 379 ? 13.022  -28.753 33.817  1.00 70.10  ? 379 PRO A CG    1 
ATOM   2939 C  CD    . PRO A 1 379 ? 12.431  -28.036 32.632  1.00 65.50  ? 379 PRO A CD    1 
ATOM   2940 N  N     . GLY A 1 380 ? 16.262  -30.213 30.795  1.00 64.52  ? 380 GLY A N     1 
ATOM   2941 C  CA    . GLY A 1 380 ? 16.761  -31.099 29.768  1.00 62.93  ? 380 GLY A CA    1 
ATOM   2942 C  C     . GLY A 1 380 ? 17.035  -30.448 28.430  1.00 64.29  ? 380 GLY A C     1 
ATOM   2943 O  O     . GLY A 1 380 ? 17.712  -31.056 27.590  1.00 60.78  ? 380 GLY A O     1 
ATOM   2944 N  N     . VAL A 1 381 ? 16.536  -29.238 28.198  1.00 63.55  ? 381 VAL A N     1 
ATOM   2945 C  CA    . VAL A 1 381 ? 16.776  -28.544 26.939  1.00 59.64  ? 381 VAL A CA    1 
ATOM   2946 C  C     . VAL A 1 381 ? 18.190  -27.981 26.945  1.00 58.43  ? 381 VAL A C     1 
ATOM   2947 O  O     . VAL A 1 381 ? 18.583  -27.264 27.874  1.00 61.90  ? 381 VAL A O     1 
ATOM   2948 C  CB    . VAL A 1 381 ? 15.735  -27.436 26.719  1.00 63.89  ? 381 VAL A CB    1 
ATOM   2949 C  CG1   . VAL A 1 381 ? 16.065  -26.640 25.466  1.00 58.25  ? 381 VAL A CG1   1 
ATOM   2950 C  CG2   . VAL A 1 381 ? 14.340  -28.033 26.623  1.00 58.55  ? 381 VAL A CG2   1 
ATOM   2951 N  N     . THR A 1 382 ? 18.960  -28.309 25.913  1.00 59.95  ? 382 THR A N     1 
ATOM   2952 C  CA    . THR A 1 382 ? 20.332  -27.849 25.770  1.00 61.99  ? 382 THR A CA    1 
ATOM   2953 C  C     . THR A 1 382 ? 20.430  -26.827 24.644  1.00 55.35  ? 382 THR A C     1 
ATOM   2954 O  O     . THR A 1 382 ? 19.588  -26.776 23.744  1.00 50.04  ? 382 THR A O     1 
ATOM   2955 C  CB    . THR A 1 382 ? 21.282  -29.022 25.502  1.00 54.50  ? 382 THR A CB    1 
ATOM   2956 O  OG1   . THR A 1 382 ? 20.859  -29.726 24.327  1.00 63.04  ? 382 THR A OG1   1 
ATOM   2957 C  CG2   . THR A 1 382 ? 21.296  -29.978 26.686  1.00 60.29  ? 382 THR A CG2   1 
ATOM   2958 N  N     . ILE A 1 383 ? 21.480  -26.010 24.705  1.00 58.07  ? 383 ILE A N     1 
ATOM   2959 C  CA    . ILE A 1 383 ? 21.684  -24.905 23.776  1.00 52.49  ? 383 ILE A CA    1 
ATOM   2960 C  C     . ILE A 1 383 ? 22.939  -25.177 22.958  1.00 55.93  ? 383 ILE A C     1 
ATOM   2961 O  O     . ILE A 1 383 ? 23.975  -25.563 23.511  1.00 56.40  ? 383 ILE A O     1 
ATOM   2962 C  CB    . ILE A 1 383 ? 21.803  -23.559 24.513  1.00 55.15  ? 383 ILE A CB    1 
ATOM   2963 C  CG1   . ILE A 1 383 ? 20.582  -23.322 25.402  1.00 56.34  ? 383 ILE A CG1   1 
ATOM   2964 C  CG2   . ILE A 1 383 ? 21.969  -22.416 23.520  1.00 49.43  ? 383 ILE A CG2   1 
ATOM   2965 C  CD1   . ILE A 1 383 ? 20.640  -22.021 26.177  1.00 54.66  ? 383 ILE A CD1   1 
ATOM   2966 N  N     . THR A 1 384 ? 22.844  -24.974 21.647  1.00 43.47  ? 384 THR A N     1 
ATOM   2967 C  CA    . THR A 1 384 ? 23.992  -24.996 20.750  1.00 46.74  ? 384 THR A CA    1 
ATOM   2968 C  C     . THR A 1 384 ? 24.243  -23.574 20.265  1.00 51.54  ? 384 THR A C     1 
ATOM   2969 O  O     . THR A 1 384 ? 23.346  -22.945 19.694  1.00 48.05  ? 384 THR A O     1 
ATOM   2970 C  CB    . THR A 1 384 ? 23.757  -25.936 19.567  1.00 54.37  ? 384 THR A CB    1 
ATOM   2971 O  OG1   . THR A 1 384 ? 23.656  -27.286 20.038  1.00 56.39  ? 384 THR A OG1   1 
ATOM   2972 C  CG2   . THR A 1 384 ? 24.902  -25.834 18.567  1.00 54.32  ? 384 THR A CG2   1 
ATOM   2973 N  N     . SER A 1 385 ? 25.455  -23.073 20.493  1.00 50.35  ? 385 SER A N     1 
ATOM   2974 C  CA    . SER A 1 385 ? 25.771  -21.691 20.167  1.00 50.94  ? 385 SER A CA    1 
ATOM   2975 C  C     . SER A 1 385 ? 25.873  -21.497 18.655  1.00 46.39  ? 385 SER A C     1 
ATOM   2976 O  O     . SER A 1 385 ? 25.822  -22.445 17.866  1.00 50.39  ? 385 SER A O     1 
ATOM   2977 C  CB    . SER A 1 385 ? 27.079  -21.269 20.834  1.00 50.50  ? 385 SER A CB    1 
ATOM   2978 O  OG    . SER A 1 385 ? 28.188  -21.872 20.193  1.00 51.73  ? 385 SER A OG    1 
ATOM   2979 N  N     . TRP A 1 386 ? 26.028  -20.233 18.254  1.00 46.61  ? 386 TRP A N     1 
ATOM   2980 C  CA    . TRP A 1 386 ? 26.199  -19.909 16.843  1.00 44.66  ? 386 TRP A CA    1 
ATOM   2981 C  C     . TRP A 1 386 ? 27.514  -20.438 16.287  1.00 49.79  ? 386 TRP A C     1 
ATOM   2982 O  O     . TRP A 1 386 ? 27.654  -20.555 15.065  1.00 52.75  ? 386 TRP A O     1 
ATOM   2983 C  CB    . TRP A 1 386 ? 26.120  -18.396 16.637  1.00 43.23  ? 386 TRP A CB    1 
ATOM   2984 C  CG    . TRP A 1 386 ? 27.310  -17.663 17.167  1.00 45.33  ? 386 TRP A CG    1 
ATOM   2985 C  CD1   . TRP A 1 386 ? 27.594  -17.398 18.476  1.00 45.32  ? 386 TRP A CD1   1 
ATOM   2986 C  CD2   . TRP A 1 386 ? 28.380  -17.097 16.402  1.00 45.22  ? 386 TRP A CD2   1 
ATOM   2987 N  NE1   . TRP A 1 386 ? 28.775  -16.705 18.573  1.00 45.69  ? 386 TRP A NE1   1 
ATOM   2988 C  CE2   . TRP A 1 386 ? 29.278  -16.507 17.314  1.00 47.49  ? 386 TRP A CE2   1 
ATOM   2989 C  CE3   . TRP A 1 386 ? 28.667  -17.032 15.034  1.00 46.04  ? 386 TRP A CE3   1 
ATOM   2990 C  CZ2   . TRP A 1 386 ? 30.442  -15.859 16.903  1.00 43.23  ? 386 TRP A CZ2   1 
ATOM   2991 C  CZ3   . TRP A 1 386 ? 29.825  -16.388 14.628  1.00 41.20  ? 386 TRP A CZ3   1 
ATOM   2992 C  CH2   . TRP A 1 386 ? 30.696  -15.809 15.560  1.00 48.63  ? 386 TRP A CH2   1 
ATOM   2993 N  N     . LYS A 1 387 ? 28.478  -20.754 17.151  1.00 48.14  ? 387 LYS A N     1 
ATOM   2994 C  CA    . LYS A 1 387 ? 29.725  -21.383 16.735  1.00 55.76  ? 387 LYS A CA    1 
ATOM   2995 C  C     . LYS A 1 387 ? 29.589  -22.887 16.546  1.00 58.43  ? 387 LYS A C     1 
ATOM   2996 O  O     . LYS A 1 387 ? 30.608  -23.567 16.387  1.00 65.92  ? 387 LYS A O     1 
ATOM   2997 C  CB    . LYS A 1 387 ? 30.833  -21.094 17.751  1.00 56.29  ? 387 LYS A CB    1 
ATOM   2998 C  CG    . LYS A 1 387 ? 31.237  -19.633 17.849  1.00 58.94  ? 387 LYS A CG    1 
ATOM   2999 C  CD    . LYS A 1 387 ? 32.453  -19.469 18.748  1.00 58.14  ? 387 LYS A CD    1 
ATOM   3000 C  CE    . LYS A 1 387 ? 32.910  -18.022 18.815  1.00 64.40  ? 387 LYS A CE    1 
ATOM   3001 N  NZ    . LYS A 1 387 ? 31.897  -17.151 19.470  1.00 72.58  ? 387 LYS A NZ    1 
ATOM   3002 N  N     . ASN A 1 388 ? 28.361  -23.410 16.568  1.00 56.49  ? 388 ASN A N     1 
ATOM   3003 C  CA    . ASN A 1 388 ? 28.099  -24.841 16.411  1.00 60.13  ? 388 ASN A CA    1 
ATOM   3004 C  C     . ASN A 1 388 ? 28.813  -25.652 17.490  1.00 65.07  ? 388 ASN A C     1 
ATOM   3005 O  O     . ASN A 1 388 ? 29.423  -26.686 17.215  1.00 71.28  ? 388 ASN A O     1 
ATOM   3006 C  CB    . ASN A 1 388 ? 28.488  -25.328 15.013  1.00 56.10  ? 388 ASN A CB    1 
ATOM   3007 C  CG    . ASN A 1 388 ? 27.727  -26.567 14.598  1.00 59.79  ? 388 ASN A CG    1 
ATOM   3008 O  OD1   . ASN A 1 388 ? 26.511  -26.648 14.770  1.00 62.84  ? 388 ASN A OD1   1 
ATOM   3009 N  ND2   . ASN A 1 388 ? 28.440  -27.547 14.055  1.00 77.04  ? 388 ASN A ND2   1 
ATOM   3010 N  N     . LYS A 1 389 ? 28.742  -25.172 18.729  1.00 65.64  ? 389 LYS A N     1 
ATOM   3011 C  CA    . LYS A 1 389 ? 29.357  -25.837 19.867  1.00 72.46  ? 389 LYS A CA    1 
ATOM   3012 C  C     . LYS A 1 389 ? 28.361  -25.903 21.015  1.00 73.67  ? 389 LYS A C     1 
ATOM   3013 O  O     . LYS A 1 389 ? 27.405  -25.126 21.082  1.00 67.15  ? 389 LYS A O     1 
ATOM   3014 C  CB    . LYS A 1 389 ? 30.628  -25.111 20.336  1.00 73.94  ? 389 LYS A CB    1 
ATOM   3015 C  CG    . LYS A 1 389 ? 31.716  -24.985 19.285  1.00 80.88  ? 389 LYS A CG    1 
ATOM   3016 C  CD    . LYS A 1 389 ? 32.877  -24.154 19.810  1.00 85.97  ? 389 LYS A CD    1 
ATOM   3017 C  CE    . LYS A 1 389 ? 33.935  -23.935 18.741  1.00 92.28  ? 389 LYS A CE    1 
ATOM   3018 N  NZ    . LYS A 1 389 ? 35.039  -23.063 19.230  1.00 95.94  ? 389 LYS A NZ    1 
ATOM   3019 N  N     . GLU A 1 390 ? 28.596  -26.851 21.920  1.00 76.18  ? 390 GLU A N     1 
ATOM   3020 C  CA    . GLU A 1 390 ? 27.836  -26.893 23.161  1.00 79.35  ? 390 GLU A CA    1 
ATOM   3021 C  C     . GLU A 1 390 ? 28.109  -25.636 23.975  1.00 74.34  ? 390 GLU A C     1 
ATOM   3022 O  O     . GLU A 1 390 ? 29.248  -25.170 24.067  1.00 81.61  ? 390 GLU A O     1 
ATOM   3023 C  CB    . GLU A 1 390 ? 28.198  -28.140 23.969  1.00 78.47  ? 390 GLU A CB    1 
ATOM   3024 C  CG    . GLU A 1 390 ? 27.449  -29.392 23.543  1.00 90.56  ? 390 GLU A CG    1 
ATOM   3025 C  CD    . GLU A 1 390 ? 25.970  -29.324 23.875  1.00 95.83  ? 390 GLU A CD    1 
ATOM   3026 O  OE1   . GLU A 1 390 ? 25.599  -28.557 24.788  1.00 92.02  ? 390 GLU A OE1   1 
ATOM   3027 O  OE2   . GLU A 1 390 ? 25.179  -30.037 23.222  1.00 98.73  ? 390 GLU A OE2   1 
ATOM   3028 N  N     . TRP A 1 391 ? 27.054  -25.081 24.564  1.00 72.82  ? 391 TRP A N     1 
ATOM   3029 C  CA    . TRP A 1 391 ? 27.153  -23.811 25.268  1.00 77.72  ? 391 TRP A CA    1 
ATOM   3030 C  C     . TRP A 1 391 ? 26.374  -23.883 26.570  1.00 82.32  ? 391 TRP A C     1 
ATOM   3031 O  O     . TRP A 1 391 ? 25.218  -24.316 26.583  1.00 76.70  ? 391 TRP A O     1 
ATOM   3032 C  CB    . TRP A 1 391 ? 26.628  -22.662 24.400  1.00 69.53  ? 391 TRP A CB    1 
ATOM   3033 C  CG    . TRP A 1 391 ? 26.736  -21.322 25.050  1.00 71.39  ? 391 TRP A CG    1 
ATOM   3034 C  CD1   . TRP A 1 391 ? 27.781  -20.451 24.963  1.00 68.26  ? 391 TRP A CD1   1 
ATOM   3035 C  CD2   . TRP A 1 391 ? 25.759  -20.696 25.890  1.00 70.27  ? 391 TRP A CD2   1 
ATOM   3036 N  NE1   . TRP A 1 391 ? 27.515  -19.319 25.695  1.00 72.46  ? 391 TRP A NE1   1 
ATOM   3037 C  CE2   . TRP A 1 391 ? 26.280  -19.445 26.274  1.00 72.03  ? 391 TRP A CE2   1 
ATOM   3038 C  CE3   . TRP A 1 391 ? 24.494  -21.071 26.353  1.00 71.67  ? 391 TRP A CE3   1 
ATOM   3039 C  CZ2   . TRP A 1 391 ? 25.581  -18.568 27.099  1.00 70.81  ? 391 TRP A CZ2   1 
ATOM   3040 C  CZ3   . TRP A 1 391 ? 23.802  -20.200 27.172  1.00 71.92  ? 391 TRP A CZ3   1 
ATOM   3041 C  CH2   . TRP A 1 391 ? 24.346  -18.962 27.536  1.00 73.31  ? 391 TRP A CH2   1 
ATOM   3042 N  N     . ARG A 1 392 ? 27.010  -23.454 27.659  1.00 91.28  ? 392 ARG A N     1 
ATOM   3043 C  CA    . ARG A 1 392 ? 26.380  -23.410 28.966  1.00 101.17 ? 392 ARG A CA    1 
ATOM   3044 C  C     . ARG A 1 392 ? 26.245  -21.967 29.445  1.00 103.21 ? 392 ARG A C     1 
ATOM   3045 O  O     . ARG A 1 392 ? 27.064  -21.111 29.096  1.00 100.86 ? 392 ARG A O     1 
ATOM   3046 C  CB    . ARG A 1 392 ? 27.179  -24.216 29.997  1.00 109.20 ? 392 ARG A CB    1 
ATOM   3047 C  CG    . ARG A 1 392 ? 27.204  -25.710 29.721  1.00 111.54 ? 392 ARG A CG    1 
ATOM   3048 C  CD    . ARG A 1 392 ? 27.845  -26.474 30.866  1.00 123.26 ? 392 ARG A CD    1 
ATOM   3049 N  NE    . ARG A 1 392 ? 27.793  -27.915 30.654  1.00 132.62 ? 392 ARG A NE    1 
ATOM   3050 C  CZ    . ARG A 1 392 ? 28.227  -28.816 31.525  1.00 132.68 ? 392 ARG A CZ    1 
ATOM   3051 N  NH1   . ARG A 1 392 ? 28.754  -28.459 32.684  1.00 134.79 ? 392 ARG A NH1   1 
ATOM   3052 N  NH2   . ARG A 1 392 ? 28.128  -30.108 31.224  1.00 134.44 ? 392 ARG A NH2   1 
ATOM   3053 N  N     . PRO A 1 393 ? 25.215  -21.664 30.241  1.00 105.97 ? 393 PRO A N     1 
ATOM   3054 C  CA    . PRO A 1 393 ? 25.015  -20.277 30.697  1.00 107.68 ? 393 PRO A CA    1 
ATOM   3055 C  C     . PRO A 1 393 ? 26.143  -19.735 31.562  1.00 116.89 ? 393 PRO A C     1 
ATOM   3056 O  O     . PRO A 1 393 ? 26.167  -18.524 31.818  1.00 120.40 ? 393 PRO A O     1 
ATOM   3057 C  CB    . PRO A 1 393 ? 23.700  -20.352 31.485  1.00 108.25 ? 393 PRO A CB    1 
ATOM   3058 C  CG    . PRO A 1 393 ? 23.002  -21.560 30.946  1.00 103.41 ? 393 PRO A CG    1 
ATOM   3059 C  CD    . PRO A 1 393 ? 24.093  -22.538 30.625  1.00 101.73 ? 393 PRO A CD    1 
ATOM   3060 N  N     . GLN A 1 394 ? 27.071  -20.576 32.019  1.00 127.32 ? 394 GLN A N     1 
ATOM   3061 C  CA    . GLN A 1 394 ? 28.186  -20.134 32.847  1.00 138.38 ? 394 GLN A CA    1 
ATOM   3062 C  C     . GLN A 1 394 ? 29.508  -20.140 32.083  1.00 135.75 ? 394 GLN A C     1 
ATOM   3063 O  O     . GLN A 1 394 ? 30.563  -20.427 32.654  1.00 140.23 ? 394 GLN A O     1 
ATOM   3064 C  CB    . GLN A 1 394 ? 28.287  -20.989 34.109  1.00 149.83 ? 394 GLN A CB    1 
ATOM   3065 C  CG    . GLN A 1 394 ? 27.149  -20.759 35.093  1.00 157.46 ? 394 GLN A CG    1 
ATOM   3066 C  CD    . GLN A 1 394 ? 27.376  -21.443 36.426  1.00 176.22 ? 394 GLN A CD    1 
ATOM   3067 O  OE1   . GLN A 1 394 ? 28.206  -22.344 36.543  1.00 180.18 ? 394 GLN A OE1   1 
ATOM   3068 N  NE2   . GLN A 1 394 ? 26.638  -21.013 37.444  1.00 178.24 ? 394 GLN A NE2   1 
ATOM   3069 N  N     . ASP A 1 395 ? 29.461  -19.827 30.792  1.00 126.92 ? 395 ASP A N     1 
ATOM   3070 C  CA    . ASP A 1 395 ? 30.649  -19.635 29.979  1.00 124.66 ? 395 ASP A CA    1 
ATOM   3071 C  C     . ASP A 1 395 ? 30.882  -18.138 29.779  1.00 122.92 ? 395 ASP A C     1 
ATOM   3072 O  O     . ASP A 1 395 ? 30.180  -17.295 30.346  1.00 121.88 ? 395 ASP A O     1 
ATOM   3073 C  CB    . ASP A 1 395 ? 30.505  -20.373 28.645  1.00 116.64 ? 395 ASP A CB    1 
ATOM   3074 C  CG    . ASP A 1 395 ? 30.431  -21.878 28.813  1.00 116.21 ? 395 ASP A CG    1 
ATOM   3075 O  OD1   . ASP A 1 395 ? 30.566  -22.359 29.958  1.00 121.65 ? 395 ASP A OD1   1 
ATOM   3076 O  OD2   . ASP A 1 395 ? 30.238  -22.580 27.798  1.00 107.85 ? 395 ASP A OD2   1 
ATOM   3077 N  N     . GLU A 1 396 ? 31.878  -17.796 28.965  1.00 123.68 ? 396 GLU A N     1 
ATOM   3078 C  CA    . GLU A 1 396 ? 32.151  -16.405 28.629  1.00 124.13 ? 396 GLU A CA    1 
ATOM   3079 C  C     . GLU A 1 396 ? 31.661  -16.029 27.239  1.00 114.19 ? 396 GLU A C     1 
ATOM   3080 O  O     . GLU A 1 396 ? 31.208  -14.899 27.030  1.00 110.86 ? 396 GLU A O     1 
ATOM   3081 C  CB    . GLU A 1 396 ? 33.654  -16.113 28.733  1.00 127.13 ? 396 GLU A CB    1 
ATOM   3082 C  CG    . GLU A 1 396 ? 33.997  -14.634 28.633  1.00 127.54 ? 396 GLU A CG    1 
ATOM   3083 C  CD    . GLU A 1 396 ? 35.483  -14.385 28.464  1.00 124.24 ? 396 GLU A CD    1 
ATOM   3084 O  OE1   . GLU A 1 396 ? 36.203  -15.315 28.042  1.00 127.81 ? 396 GLU A OE1   1 
ATOM   3085 O  OE2   . GLU A 1 396 ? 35.931  -13.254 28.751  1.00 116.81 ? 396 GLU A OE2   1 
ATOM   3086 N  N     . GLU A 1 397 ? 31.740  -16.948 26.287  1.00 101.80 ? 397 GLU A N     1 
ATOM   3087 C  CA    . GLU A 1 397 ? 31.258  -16.673 24.940  1.00 88.49  ? 397 GLU A CA    1 
ATOM   3088 C  C     . GLU A 1 397 ? 29.736  -16.590 24.941  1.00 76.49  ? 397 GLU A C     1 
ATOM   3089 O  O     . GLU A 1 397 ? 29.073  -17.463 25.514  1.00 72.56  ? 397 GLU A O     1 
ATOM   3090 C  CB    . GLU A 1 397 ? 31.721  -17.762 23.974  1.00 88.29  ? 397 GLU A CB    1 
ATOM   3091 C  CG    . GLU A 1 397 ? 33.215  -17.765 23.699  1.00 101.73 ? 397 GLU A CG    1 
ATOM   3092 C  CD    . GLU A 1 397 ? 33.642  -16.641 22.773  1.00 109.45 ? 397 GLU A CD    1 
ATOM   3093 O  OE1   . GLU A 1 397 ? 32.778  -16.100 22.050  1.00 100.22 ? 397 GLU A OE1   1 
ATOM   3094 O  OE2   . GLU A 1 397 ? 34.844  -16.299 22.767  1.00 117.53 ? 397 GLU A OE2   1 
ATOM   3095 N  N     . PRO A 1 398 ? 29.147  -15.568 24.327  1.00 71.37  ? 398 PRO A N     1 
ATOM   3096 C  CA    . PRO A 1 398 ? 27.690  -15.549 24.175  1.00 61.03  ? 398 PRO A CA    1 
ATOM   3097 C  C     . PRO A 1 398 ? 27.233  -16.643 23.225  1.00 57.10  ? 398 PRO A C     1 
ATOM   3098 O  O     . PRO A 1 398 ? 27.966  -17.067 22.328  1.00 54.56  ? 398 PRO A O     1 
ATOM   3099 C  CB    . PRO A 1 398 ? 27.408  -14.156 23.601  1.00 52.98  ? 398 PRO A CB    1 
ATOM   3100 C  CG    . PRO A 1 398 ? 28.677  -13.776 22.912  1.00 63.01  ? 398 PRO A CG    1 
ATOM   3101 C  CD    . PRO A 1 398 ? 29.782  -14.377 23.737  1.00 66.23  ? 398 PRO A CD    1 
ATOM   3102 N  N     . CYS A 1 399 ? 26.002  -17.112 23.441  1.00 52.94  ? 399 CYS A N     1 
ATOM   3103 C  CA    . CYS A 1 399 ? 25.465  -18.176 22.601  1.00 54.04  ? 399 CYS A CA    1 
ATOM   3104 C  C     . CYS A 1 399 ? 25.084  -17.678 21.213  1.00 42.95  ? 399 CYS A C     1 
ATOM   3105 O  O     . CYS A 1 399 ? 25.059  -18.475 20.271  1.00 42.96  ? 399 CYS A O     1 
ATOM   3106 C  CB    . CYS A 1 399 ? 24.254  -18.827 23.276  1.00 53.19  ? 399 CYS A CB    1 
ATOM   3107 S  SG    . CYS A 1 399 ? 22.794  -17.763 23.419  1.00 52.73  ? 399 CYS A SG    1 
ATOM   3108 N  N     . ALA A 1 400 ? 24.797  -16.386 21.066  1.00 42.47  ? 400 ALA A N     1 
ATOM   3109 C  CA    . ALA A 1 400 ? 24.434  -15.793 19.788  1.00 43.48  ? 400 ALA A CA    1 
ATOM   3110 C  C     . ALA A 1 400 ? 25.369  -14.634 19.477  1.00 44.35  ? 400 ALA A C     1 
ATOM   3111 O  O     . ALA A 1 400 ? 25.796  -13.907 20.381  1.00 42.56  ? 400 ALA A O     1 
ATOM   3112 C  CB    . ALA A 1 400 ? 22.982  -15.304 19.793  1.00 39.29  ? 400 ALA A CB    1 
ATOM   3113 N  N     . HIS A 1 401 ? 25.687  -14.466 18.197  1.00 42.49  ? 401 HIS A N     1 
ATOM   3114 C  CA    . HIS A 1 401 ? 26.551  -13.367 17.799  1.00 40.60  ? 401 HIS A CA    1 
ATOM   3115 C  C     . HIS A 1 401 ? 25.848  -12.034 18.050  1.00 39.00  ? 401 HIS A C     1 
ATOM   3116 O  O     . HIS A 1 401 ? 24.636  -11.922 17.836  1.00 32.47  ? 401 HIS A O     1 
ATOM   3117 C  CB    . HIS A 1 401 ? 26.940  -13.489 16.327  1.00 36.29  ? 401 HIS A CB    1 
ATOM   3118 C  CG    . HIS A 1 401 ? 27.985  -12.506 15.900  1.00 38.39  ? 401 HIS A CG    1 
ATOM   3119 N  ND1   . HIS A 1 401 ? 27.678  -11.238 15.456  1.00 36.42  ? 401 HIS A ND1   1 
ATOM   3120 C  CD2   . HIS A 1 401 ? 29.336  -12.602 15.860  1.00 37.88  ? 401 HIS A CD2   1 
ATOM   3121 C  CE1   . HIS A 1 401 ? 28.793  -10.596 15.156  1.00 37.15  ? 401 HIS A CE1   1 
ATOM   3122 N  NE2   . HIS A 1 401 ? 29.813  -11.402 15.392  1.00 37.53  ? 401 HIS A NE2   1 
ATOM   3123 N  N     . PRO A 1 402 ? 26.573  -11.015 18.521  1.00 35.57  ? 402 PRO A N     1 
ATOM   3124 C  CA    . PRO A 1 402 ? 25.923  -9.730  18.834  1.00 33.03  ? 402 PRO A CA    1 
ATOM   3125 C  C     . PRO A 1 402 ? 25.232  -9.073  17.648  1.00 35.31  ? 402 PRO A C     1 
ATOM   3126 O  O     . PRO A 1 402 ? 24.316  -8.268  17.860  1.00 36.94  ? 402 PRO A O     1 
ATOM   3127 C  CB    . PRO A 1 402 ? 27.085  -8.872  19.355  1.00 34.91  ? 402 PRO A CB    1 
ATOM   3128 C  CG    . PRO A 1 402 ? 28.059  -9.867  19.907  1.00 33.04  ? 402 PRO A CG    1 
ATOM   3129 C  CD    . PRO A 1 402 ? 27.967  -11.063 18.998  1.00 39.22  ? 402 PRO A CD    1 
ATOM   3130 N  N     . ASN A 1 403 ? 25.632  -9.382  16.414  1.00 35.11  ? 403 ASN A N     1 
ATOM   3131 C  CA    . ASN A 1 403 ? 24.966  -8.869  15.223  1.00 33.25  ? 403 ASN A CA    1 
ATOM   3132 C  C     . ASN A 1 403 ? 24.153  -9.950  14.516  1.00 36.34  ? 403 ASN A C     1 
ATOM   3133 O  O     . ASN A 1 403 ? 23.912  -9.855  13.308  1.00 35.54  ? 403 ASN A O     1 
ATOM   3134 C  CB    . ASN A 1 403 ? 25.986  -8.249  14.262  1.00 33.04  ? 403 ASN A CB    1 
ATOM   3135 C  CG    . ASN A 1 403 ? 25.333  -7.392  13.176  1.00 38.33  ? 403 ASN A CG    1 
ATOM   3136 O  OD1   . ASN A 1 403 ? 24.411  -6.621  13.442  1.00 33.85  ? 403 ASN A OD1   1 
ATOM   3137 N  ND2   . ASN A 1 403 ? 25.805  -7.542  11.943  1.00 31.92  ? 403 ASN A ND2   1 
ATOM   3138 N  N     . SER A 1 404 ? 23.731  -10.983 15.243  1.00 30.59  ? 404 SER A N     1 
ATOM   3139 C  CA    . SER A 1 404 ? 22.862  -11.989 14.652  1.00 31.34  ? 404 SER A CA    1 
ATOM   3140 C  C     . SER A 1 404 ? 21.526  -11.361 14.266  1.00 28.36  ? 404 SER A C     1 
ATOM   3141 O  O     . SER A 1 404 ? 21.070  -10.387 14.873  1.00 33.45  ? 404 SER A O     1 
ATOM   3142 C  CB    . SER A 1 404 ? 22.653  -13.158 15.617  1.00 33.41  ? 404 SER A CB    1 
ATOM   3143 O  OG    . SER A 1 404 ? 22.124  -12.724 16.857  1.00 32.07  ? 404 SER A OG    1 
ATOM   3144 N  N     . ARG A 1 405 ? 20.900  -11.923 13.236  1.00 29.05  ? 405 ARG A N     1 
ATOM   3145 C  CA    . ARG A 1 405 ? 19.751  -11.290 12.606  1.00 31.58  ? 405 ARG A CA    1 
ATOM   3146 C  C     . ARG A 1 405 ? 18.647  -12.306 12.367  1.00 30.44  ? 405 ARG A C     1 
ATOM   3147 O  O     . ARG A 1 405 ? 18.905  -13.492 12.147  1.00 29.02  ? 405 ARG A O     1 
ATOM   3148 C  CB    . ARG A 1 405 ? 20.128  -10.644 11.262  1.00 25.32  ? 405 ARG A CB    1 
ATOM   3149 C  CG    . ARG A 1 405 ? 21.197  -9.568  11.350  1.00 27.16  ? 405 ARG A CG    1 
ATOM   3150 C  CD    . ARG A 1 405 ? 20.587  -8.185  11.479  1.00 28.45  ? 405 ARG A CD    1 
ATOM   3151 N  NE    . ARG A 1 405 ? 21.603  -7.166  11.706  1.00 28.37  ? 405 ARG A NE    1 
ATOM   3152 C  CZ    . ARG A 1 405 ? 21.356  -5.866  11.786  1.00 28.14  ? 405 ARG A CZ    1 
ATOM   3153 N  NH1   . ARG A 1 405 ? 20.134  -5.384  11.629  1.00 27.42  ? 405 ARG A NH1   1 
ATOM   3154 N  NH2   . ARG A 1 405 ? 22.360  -5.028  12.030  1.00 26.64  ? 405 ARG A NH2   1 
ATOM   3155 N  N     . PHE A 1 406 ? 17.411  -11.825 12.412  1.00 29.30  ? 406 PHE A N     1 
ATOM   3156 C  CA    . PHE A 1 406 ? 16.300  -12.538 11.807  1.00 29.97  ? 406 PHE A CA    1 
ATOM   3157 C  C     . PHE A 1 406 ? 15.934  -11.864 10.490  1.00 25.38  ? 406 PHE A C     1 
ATOM   3158 O  O     . PHE A 1 406 ? 16.214  -10.684 10.267  1.00 30.04  ? 406 PHE A O     1 
ATOM   3159 C  CB    . PHE A 1 406 ? 15.083  -12.611 12.744  1.00 30.93  ? 406 PHE A CB    1 
ATOM   3160 C  CG    . PHE A 1 406 ? 14.609  -11.276 13.266  1.00 27.03  ? 406 PHE A CG    1 
ATOM   3161 C  CD1   . PHE A 1 406 ? 13.774  -10.472 12.506  1.00 27.86  ? 406 PHE A CD1   1 
ATOM   3162 C  CD2   . PHE A 1 406 ? 14.964  -10.849 14.537  1.00 30.68  ? 406 PHE A CD2   1 
ATOM   3163 C  CE1   . PHE A 1 406 ? 13.327  -9.253  12.991  1.00 26.94  ? 406 PHE A CE1   1 
ATOM   3164 C  CE2   . PHE A 1 406 ? 14.520  -9.633  15.028  1.00 30.73  ? 406 PHE A CE2   1 
ATOM   3165 C  CZ    . PHE A 1 406 ? 13.699  -8.835  14.255  1.00 30.30  ? 406 PHE A CZ    1 
ATOM   3166 N  N     . CYS A 1 407 ? 15.323  -12.645 9.605   1.00 30.28  ? 407 CYS A N     1 
ATOM   3167 C  CA    . CYS A 1 407 ? 14.903  -12.170 8.291   1.00 24.10  ? 407 CYS A CA    1 
ATOM   3168 C  C     . CYS A 1 407 ? 13.478  -12.660 8.087   1.00 29.17  ? 407 CYS A C     1 
ATOM   3169 O  O     . CYS A 1 407 ? 13.263  -13.853 7.852   1.00 28.81  ? 407 CYS A O     1 
ATOM   3170 C  CB    . CYS A 1 407 ? 15.839  -12.686 7.195   1.00 31.69  ? 407 CYS A CB    1 
ATOM   3171 S  SG    . CYS A 1 407 ? 15.570  -11.990 5.554   1.00 28.44  ? 407 CYS A SG    1 
ATOM   3172 N  N     . THR A 1 408 ? 12.510  -11.754 8.192   1.00 27.56  ? 408 THR A N     1 
ATOM   3173 C  CA    . THR A 1 408 ? 11.111  -12.133 8.293   1.00 28.93  ? 408 THR A CA    1 
ATOM   3174 C  C     . THR A 1 408 ? 10.261  -11.240 7.401   1.00 27.90  ? 408 THR A C     1 
ATOM   3175 O  O     . THR A 1 408 ? 10.597  -10.069 7.188   1.00 31.59  ? 408 THR A O     1 
ATOM   3176 C  CB    . THR A 1 408 ? 10.624  -12.046 9.753   1.00 29.48  ? 408 THR A CB    1 
ATOM   3177 O  OG1   . THR A 1 408 ? 9.326   -12.637 9.871   1.00 32.72  ? 408 THR A OG1   1 
ATOM   3178 C  CG2   . THR A 1 408 ? 10.569  -10.598 10.231  1.00 30.18  ? 408 THR A CG2   1 
ATOM   3179 N  N     . PRO A 1 409 ? 9.170   -11.773 6.846   1.00 32.26  ? 409 PRO A N     1 
ATOM   3180 C  CA    . PRO A 1 409 ? 8.318   -10.958 5.970   1.00 31.53  ? 409 PRO A CA    1 
ATOM   3181 C  C     . PRO A 1 409 ? 7.595   -9.865  6.744   1.00 30.81  ? 409 PRO A C     1 
ATOM   3182 O  O     . PRO A 1 409 ? 7.127   -10.076 7.865   1.00 31.53  ? 409 PRO A O     1 
ATOM   3183 C  CB    . PRO A 1 409 ? 7.327   -11.975 5.388   1.00 33.73  ? 409 PRO A CB    1 
ATOM   3184 C  CG    . PRO A 1 409 ? 7.979   -13.309 5.580   1.00 36.40  ? 409 PRO A CG    1 
ATOM   3185 C  CD    . PRO A 1 409 ? 8.764   -13.188 6.848   1.00 32.45  ? 409 PRO A CD    1 
ATOM   3186 N  N     . ALA A 1 410 ? 7.501   -8.687  6.122   1.00 24.72  ? 410 ALA A N     1 
ATOM   3187 C  CA    . ALA A 1 410 ? 6.832   -7.562  6.766   1.00 31.07  ? 410 ALA A CA    1 
ATOM   3188 C  C     . ALA A 1 410 ? 5.335   -7.798  6.911   1.00 37.19  ? 410 ALA A C     1 
ATOM   3189 O  O     . ALA A 1 410 ? 4.729   -7.335  7.884   1.00 36.11  ? 410 ALA A O     1 
ATOM   3190 C  CB    . ALA A 1 410 ? 7.087   -6.275  5.981   1.00 27.39  ? 410 ALA A CB    1 
ATOM   3191 N  N     . SER A 1 411 ? 4.724   -8.518  5.968   1.00 35.22  ? 411 SER A N     1 
ATOM   3192 C  CA    . SER A 1 411 ? 3.281   -8.729  6.004   1.00 40.88  ? 411 SER A CA    1 
ATOM   3193 C  C     . SER A 1 411 ? 2.835   -9.585  7.182   1.00 42.64  ? 411 SER A C     1 
ATOM   3194 O  O     . SER A 1 411 ? 1.633   -9.640  7.462   1.00 48.00  ? 411 SER A O     1 
ATOM   3195 C  CB    . SER A 1 411 ? 2.808   -9.363  4.694   1.00 33.69  ? 411 SER A CB    1 
ATOM   3196 O  OG    . SER A 1 411 ? 3.352   -10.662 4.529   1.00 42.97  ? 411 SER A OG    1 
ATOM   3197 N  N     . GLN A 1 412 ? 3.761   -10.246 7.876   1.00 41.42  ? 412 GLN A N     1 
ATOM   3198 C  CA    . GLN A 1 412 ? 3.425   -11.060 9.035   1.00 45.70  ? 412 GLN A CA    1 
ATOM   3199 C  C     . GLN A 1 412 ? 3.397   -10.269 10.335  1.00 42.54  ? 412 GLN A C     1 
ATOM   3200 O  O     . GLN A 1 412 ? 2.932   -10.796 11.350  1.00 47.15  ? 412 GLN A O     1 
ATOM   3201 C  CB    . GLN A 1 412 ? 4.416   -12.221 9.178   1.00 39.44  ? 412 GLN A CB    1 
ATOM   3202 C  CG    . GLN A 1 412 ? 4.324   -13.258 8.076   1.00 43.15  ? 412 GLN A CG    1 
ATOM   3203 C  CD    . GLN A 1 412 ? 5.221   -14.452 8.330   1.00 39.46  ? 412 GLN A CD    1 
ATOM   3204 O  OE1   . GLN A 1 412 ? 5.100   -15.482 7.669   1.00 42.72  ? 412 GLN A OE1   1 
ATOM   3205 N  NE2   . GLN A 1 412 ? 6.130   -14.320 9.293   1.00 36.82  ? 412 GLN A NE2   1 
ATOM   3206 N  N     . CYS A 1 413 ? 3.884   -9.035  10.331  1.00 46.94  ? 413 CYS A N     1 
ATOM   3207 C  CA    . CYS A 1 413 ? 3.893   -8.234  11.548  1.00 47.04  ? 413 CYS A CA    1 
ATOM   3208 C  C     . CYS A 1 413 ? 2.461   -7.909  11.961  1.00 49.46  ? 413 CYS A C     1 
ATOM   3209 O  O     . CYS A 1 413 ? 1.681   -7.415  11.138  1.00 46.44  ? 413 CYS A O     1 
ATOM   3210 C  CB    . CYS A 1 413 ? 4.692   -6.952  11.333  1.00 42.39  ? 413 CYS A CB    1 
ATOM   3211 S  SG    . CYS A 1 413 ? 4.852   -5.903  12.794  1.00 45.26  ? 413 CYS A SG    1 
ATOM   3212 N  N     . PRO A 1 414 ? 2.073   -8.180  13.210  1.00 52.94  ? 414 PRO A N     1 
ATOM   3213 C  CA    . PRO A 1 414 ? 0.679   -7.936  13.618  1.00 51.99  ? 414 PRO A CA    1 
ATOM   3214 C  C     . PRO A 1 414 ? 0.258   -6.479  13.546  1.00 48.36  ? 414 PRO A C     1 
ATOM   3215 O  O     . PRO A 1 414 ? -0.943  -6.206  13.427  1.00 48.11  ? 414 PRO A O     1 
ATOM   3216 C  CB    . PRO A 1 414 ? 0.641   -8.454  15.064  1.00 50.67  ? 414 PRO A CB    1 
ATOM   3217 C  CG    . PRO A 1 414 ? 1.790   -9.403  15.161  1.00 51.00  ? 414 PRO A CG    1 
ATOM   3218 C  CD    . PRO A 1 414 ? 2.852   -8.846  14.267  1.00 49.27  ? 414 PRO A CD    1 
ATOM   3219 N  N     . ILE A 1 415 ? 1.196   -5.536  13.610  1.00 45.51  ? 415 ILE A N     1 
ATOM   3220 C  CA    . ILE A 1 415 ? 0.852   -4.119  13.617  1.00 48.43  ? 415 ILE A CA    1 
ATOM   3221 C  C     . ILE A 1 415 ? 1.363   -3.443  12.353  1.00 42.29  ? 415 ILE A C     1 
ATOM   3222 O  O     . ILE A 1 415 ? 1.668   -2.246  12.363  1.00 41.61  ? 415 ILE A O     1 
ATOM   3223 C  CB    . ILE A 1 415 ? 1.411   -3.416  14.867  1.00 46.36  ? 415 ILE A CB    1 
ATOM   3224 C  CG1   . ILE A 1 415 ? 2.916   -3.665  14.982  1.00 50.15  ? 415 ILE A CG1   1 
ATOM   3225 C  CG2   . ILE A 1 415 ? 0.675   -3.882  16.115  1.00 44.64  ? 415 ILE A CG2   1 
ATOM   3226 C  CD1   . ILE A 1 415 ? 3.613   -2.753  15.960  1.00 48.57  ? 415 ILE A CD1   1 
ATOM   3227 N  N     . ILE A 1 416 ? 1.461   -4.197  11.255  1.00 47.22  ? 416 ILE A N     1 
ATOM   3228 C  CA    . ILE A 1 416 ? 1.866   -3.593  9.993   1.00 44.27  ? 416 ILE A CA    1 
ATOM   3229 C  C     . ILE A 1 416 ? 0.818   -2.565  9.581   1.00 47.39  ? 416 ILE A C     1 
ATOM   3230 O  O     . ILE A 1 416 ? -0.391  -2.780  9.735   1.00 46.70  ? 416 ILE A O     1 
ATOM   3231 C  CB    . ILE A 1 416 ? 2.078   -4.674  8.918   1.00 44.39  ? 416 ILE A CB    1 
ATOM   3232 C  CG1   . ILE A 1 416 ? 2.814   -4.099  7.705   1.00 42.35  ? 416 ILE A CG1   1 
ATOM   3233 C  CG2   . ILE A 1 416 ? 0.760   -5.318  8.504   1.00 45.08  ? 416 ILE A CG2   1 
ATOM   3234 C  CD1   . ILE A 1 416 ? 4.283   -3.824  7.960   1.00 41.53  ? 416 ILE A CD1   1 
ATOM   3235 N  N     . ASP A 1 417 ? 1.284   -1.421  9.089   1.00 44.58  ? 417 ASP A N     1 
ATOM   3236 C  CA    . ASP A 1 417 ? 0.375   -0.327  8.782   1.00 42.95  ? 417 ASP A CA    1 
ATOM   3237 C  C     . ASP A 1 417 ? -0.439  -0.656  7.533   1.00 46.52  ? 417 ASP A C     1 
ATOM   3238 O  O     . ASP A 1 417 ? 0.100   -1.202  6.565   1.00 44.77  ? 417 ASP A O     1 
ATOM   3239 C  CB    . ASP A 1 417 ? 1.153   0.972   8.574   1.00 44.51  ? 417 ASP A CB    1 
ATOM   3240 C  CG    . ASP A 1 417 ? 0.260   2.201   8.583   1.00 46.98  ? 417 ASP A CG    1 
ATOM   3241 O  OD1   . ASP A 1 417 ? -0.050  2.710   9.681   1.00 44.05  ? 417 ASP A OD1   1 
ATOM   3242 O  OD2   . ASP A 1 417 ? -0.130  2.661   7.491   1.00 45.61  ? 417 ASP A OD2   1 
ATOM   3243 N  N     . PRO A 1 418 ? -1.738  -0.341  7.522   1.00 42.54  ? 418 PRO A N     1 
ATOM   3244 C  CA    . PRO A 1 418 ? -2.557  -0.639  6.335   1.00 50.85  ? 418 PRO A CA    1 
ATOM   3245 C  C     . PRO A 1 418 ? -2.127  0.109   5.082   1.00 48.42  ? 418 PRO A C     1 
ATOM   3246 O  O     . PRO A 1 418 ? -2.556  -0.269  3.984   1.00 59.57  ? 418 PRO A O     1 
ATOM   3247 C  CB    . PRO A 1 418 ? -3.974  -0.233  6.769   1.00 46.25  ? 418 PRO A CB    1 
ATOM   3248 C  CG    . PRO A 1 418 ? -3.784  0.674   7.942   1.00 53.30  ? 418 PRO A CG    1 
ATOM   3249 C  CD    . PRO A 1 418 ? -2.541  0.201   8.631   1.00 49.32  ? 418 PRO A CD    1 
ATOM   3250 N  N     . ALA A 1 419 ? -1.299  1.147   5.203   1.00 45.36  ? 419 ALA A N     1 
ATOM   3251 C  CA    . ALA A 1 419 ? -0.799  1.885   4.051   1.00 51.05  ? 419 ALA A CA    1 
ATOM   3252 C  C     . ALA A 1 419 ? 0.670   1.590   3.765   1.00 46.45  ? 419 ALA A C     1 
ATOM   3253 O  O     . ALA A 1 419 ? 1.328   2.371   3.071   1.00 50.04  ? 419 ALA A O     1 
ATOM   3254 C  CB    . ALA A 1 419 ? -1.008  3.386   4.253   1.00 43.56  ? 419 ALA A CB    1 
ATOM   3255 N  N     . TRP A 1 420 ? 1.196   0.473   4.277   1.00 44.90  ? 420 TRP A N     1 
ATOM   3256 C  CA    . TRP A 1 420 ? 2.616   0.180   4.114   1.00 46.58  ? 420 TRP A CA    1 
ATOM   3257 C  C     . TRP A 1 420 ? 2.977   -0.176  2.677   1.00 43.81  ? 420 TRP A C     1 
ATOM   3258 O  O     . TRP A 1 420 ? 4.150   -0.074  2.304   1.00 45.98  ? 420 TRP A O     1 
ATOM   3259 C  CB    . TRP A 1 420 ? 3.042   -0.948  5.060   1.00 43.21  ? 420 TRP A CB    1 
ATOM   3260 C  CG    . TRP A 1 420 ? 2.794   -2.342  4.549   1.00 45.68  ? 420 TRP A CG    1 
ATOM   3261 C  CD1   . TRP A 1 420 ? 1.627   -3.047  4.619   1.00 47.57  ? 420 TRP A CD1   1 
ATOM   3262 C  CD2   . TRP A 1 420 ? 3.748   -3.207  3.917   1.00 46.21  ? 420 TRP A CD2   1 
ATOM   3263 N  NE1   . TRP A 1 420 ? 1.791   -4.292  4.060   1.00 46.78  ? 420 TRP A NE1   1 
ATOM   3264 C  CE2   . TRP A 1 420 ? 3.084   -4.416  3.622   1.00 47.47  ? 420 TRP A CE2   1 
ATOM   3265 C  CE3   . TRP A 1 420 ? 5.096   -3.075  3.567   1.00 44.53  ? 420 TRP A CE3   1 
ATOM   3266 C  CZ2   . TRP A 1 420 ? 3.721   -5.485  2.993   1.00 48.28  ? 420 TRP A CZ2   1 
ATOM   3267 C  CZ3   . TRP A 1 420 ? 5.729   -4.138  2.942   1.00 43.21  ? 420 TRP A CZ3   1 
ATOM   3268 C  CH2   . TRP A 1 420 ? 5.040   -5.327  2.660   1.00 43.23  ? 420 TRP A CH2   1 
ATOM   3269 N  N     . GLU A 1 421 ? 2.006   -0.588  1.865   1.00 45.44  ? 421 GLU A N     1 
ATOM   3270 C  CA    . GLU A 1 421 ? 2.236   -0.848  0.450   1.00 46.81  ? 421 GLU A CA    1 
ATOM   3271 C  C     . GLU A 1 421 ? 1.542   0.167   -0.446  1.00 55.03  ? 421 GLU A C     1 
ATOM   3272 O  O     . GLU A 1 421 ? 1.485   -0.031  -1.665  1.00 54.77  ? 421 GLU A O     1 
ATOM   3273 C  CB    . GLU A 1 421 ? 1.791   -2.265  0.090   1.00 50.58  ? 421 GLU A CB    1 
ATOM   3274 C  CG    . GLU A 1 421 ? 2.830   -3.315  0.415   1.00 56.69  ? 421 GLU A CG    1 
ATOM   3275 C  CD    . GLU A 1 421 ? 2.440   -4.700  -0.055  1.00 51.03  ? 421 GLU A CD    1 
ATOM   3276 O  OE1   . GLU A 1 421 ? 1.308   -5.134  0.243   1.00 58.21  ? 421 GLU A OE1   1 
ATOM   3277 O  OE2   . GLU A 1 421 ? 3.268   -5.353  -0.724  1.00 55.15  ? 421 GLU A OE2   1 
ATOM   3278 N  N     . SER A 1 422 ? 1.018   1.243   0.124   1.00 51.56  ? 422 SER A N     1 
ATOM   3279 C  CA    . SER A 1 422 ? 0.372   2.282   -0.668  1.00 57.62  ? 422 SER A CA    1 
ATOM   3280 C  C     . SER A 1 422 ? 1.409   3.000   -1.520  1.00 55.24  ? 422 SER A C     1 
ATOM   3281 O  O     . SER A 1 422 ? 2.386   3.531   -0.975  1.00 55.63  ? 422 SER A O     1 
ATOM   3282 C  CB    . SER A 1 422 ? -0.347  3.270   0.243   1.00 59.55  ? 422 SER A CB    1 
ATOM   3283 O  OG    . SER A 1 422 ? -1.456  2.661   0.880   1.00 68.11  ? 422 SER A OG    1 
ATOM   3284 N  N     . PRO A 1 423 ? 1.248   3.043   -2.846  1.00 59.37  ? 423 PRO A N     1 
ATOM   3285 C  CA    . PRO A 1 423 ? 2.251   3.711   -3.688  1.00 63.00  ? 423 PRO A CA    1 
ATOM   3286 C  C     . PRO A 1 423 ? 2.265   5.223   -3.545  1.00 64.64  ? 423 PRO A C     1 
ATOM   3287 O  O     . PRO A 1 423 ? 3.201   5.859   -4.042  1.00 65.74  ? 423 PRO A O     1 
ATOM   3288 C  CB    . PRO A 1 423 ? 1.850   3.294   -5.107  1.00 61.57  ? 423 PRO A CB    1 
ATOM   3289 C  CG    . PRO A 1 423 ? 0.384   3.036   -5.012  1.00 57.73  ? 423 PRO A CG    1 
ATOM   3290 C  CD    . PRO A 1 423 ? 0.152   2.463   -3.641  1.00 59.33  ? 423 PRO A CD    1 
ATOM   3291 N  N     . GLU A 1 424 ? 1.268   5.822   -2.892  1.00 69.37  ? 424 GLU A N     1 
ATOM   3292 C  CA    . GLU A 1 424 ? 1.277   7.265   -2.693  1.00 65.21  ? 424 GLU A CA    1 
ATOM   3293 C  C     . GLU A 1 424 ? 2.108   7.683   -1.488  1.00 64.25  ? 424 GLU A C     1 
ATOM   3294 O  O     . GLU A 1 424 ? 2.451   8.864   -1.369  1.00 64.34  ? 424 GLU A O     1 
ATOM   3295 C  CB    . GLU A 1 424 ? -0.152  7.794   -2.540  1.00 68.70  ? 424 GLU A CB    1 
ATOM   3296 C  CG    . GLU A 1 424 ? -0.841  7.412   -1.237  1.00 66.33  ? 424 GLU A CG    1 
ATOM   3297 C  CD    . GLU A 1 424 ? -1.512  6.053   -1.296  1.00 79.05  ? 424 GLU A CD    1 
ATOM   3298 O  OE1   . GLU A 1 424 ? -1.206  5.270   -2.221  1.00 77.92  ? 424 GLU A OE1   1 
ATOM   3299 O  OE2   . GLU A 1 424 ? -2.354  5.768   -0.417  1.00 90.43  ? 424 GLU A OE2   1 
ATOM   3300 N  N     . GLY A 1 425 ? 2.442   6.747   -0.601  1.00 52.00  ? 425 GLY A N     1 
ATOM   3301 C  CA    . GLY A 1 425 ? 3.215   7.061   0.583   1.00 48.02  ? 425 GLY A CA    1 
ATOM   3302 C  C     . GLY A 1 425 ? 2.357   7.534   1.737   1.00 46.04  ? 425 GLY A C     1 
ATOM   3303 O  O     . GLY A 1 425 ? 1.136   7.689   1.641   1.00 43.65  ? 425 GLY A O     1 
ATOM   3304 N  N     . VAL A 1 426 ? 3.025   7.762   2.864   1.00 34.09  ? 426 VAL A N     1 
ATOM   3305 C  CA    . VAL A 1 426 ? 2.371   8.284   4.061   1.00 36.56  ? 426 VAL A CA    1 
ATOM   3306 C  C     . VAL A 1 426 ? 2.931   9.672   4.354   1.00 36.53  ? 426 VAL A C     1 
ATOM   3307 O  O     . VAL A 1 426 ? 4.113   9.932   4.090   1.00 35.89  ? 426 VAL A O     1 
ATOM   3308 C  CB    . VAL A 1 426 ? 2.548   7.337   5.259   1.00 38.87  ? 426 VAL A CB    1 
ATOM   3309 C  CG1   . VAL A 1 426 ? 1.933   5.980   4.954   1.00 38.44  ? 426 VAL A CG1   1 
ATOM   3310 C  CG2   . VAL A 1 426 ? 4.018   7.192   5.624   1.00 34.71  ? 426 VAL A CG2   1 
ATOM   3311 N  N     . PRO A 1 427 ? 2.125   10.594  4.883   1.00 38.75  ? 427 PRO A N     1 
ATOM   3312 C  CA    . PRO A 1 427 ? 2.614   11.959  5.121   1.00 33.78  ? 427 PRO A CA    1 
ATOM   3313 C  C     . PRO A 1 427 ? 3.369   12.051  6.440   1.00 34.27  ? 427 PRO A C     1 
ATOM   3314 O  O     . PRO A 1 427 ? 2.851   11.686  7.497   1.00 37.13  ? 427 PRO A O     1 
ATOM   3315 C  CB    . PRO A 1 427 ? 1.329   12.792  5.152   1.00 38.41  ? 427 PRO A CB    1 
ATOM   3316 C  CG    . PRO A 1 427 ? 0.294   11.840  5.664   1.00 40.55  ? 427 PRO A CG    1 
ATOM   3317 C  CD    . PRO A 1 427 ? 0.686   10.461  5.177   1.00 39.49  ? 427 PRO A CD    1 
ATOM   3318 N  N     . ILE A 1 428 ? 4.599   12.553  6.370   1.00 32.89  ? 428 ILE A N     1 
ATOM   3319 C  CA    . ILE A 1 428 ? 5.467   12.662  7.537   1.00 29.55  ? 428 ILE A CA    1 
ATOM   3320 C  C     . ILE A 1 428 ? 5.277   14.035  8.165   1.00 31.50  ? 428 ILE A C     1 
ATOM   3321 O  O     . ILE A 1 428 ? 5.390   15.062  7.486   1.00 34.53  ? 428 ILE A O     1 
ATOM   3322 C  CB    . ILE A 1 428 ? 6.938   12.430  7.151   1.00 34.03  ? 428 ILE A CB    1 
ATOM   3323 C  CG1   . ILE A 1 428 ? 7.115   11.049  6.516   1.00 33.31  ? 428 ILE A CG1   1 
ATOM   3324 C  CG2   . ILE A 1 428 ? 7.847   12.585  8.367   1.00 29.00  ? 428 ILE A CG2   1 
ATOM   3325 C  CD1   . ILE A 1 428 ? 6.717   9.899   7.419   1.00 31.51  ? 428 ILE A CD1   1 
ATOM   3326 N  N     . GLU A 1 429 ? 4.981   14.054  9.465   1.00 28.00  ? 429 GLU A N     1 
ATOM   3327 C  CA    . GLU A 1 429 ? 4.837   15.293  10.213  1.00 32.01  ? 429 GLU A CA    1 
ATOM   3328 C  C     . GLU A 1 429 ? 5.935   15.512  11.245  1.00 36.94  ? 429 GLU A C     1 
ATOM   3329 O  O     . GLU A 1 429 ? 5.978   16.587  11.857  1.00 32.91  ? 429 GLU A O     1 
ATOM   3330 C  CB    . GLU A 1 429 ? 3.469   15.333  10.914  1.00 37.92  ? 429 GLU A CB    1 
ATOM   3331 C  CG    . GLU A 1 429 ? 2.291   15.239  9.964   1.00 38.53  ? 429 GLU A CG    1 
ATOM   3332 C  CD    . GLU A 1 429 ? 0.961   15.358  10.679  1.00 42.63  ? 429 GLU A CD    1 
ATOM   3333 O  OE1   . GLU A 1 429 ? 0.812   16.269  11.519  1.00 44.81  ? 429 GLU A OE1   1 
ATOM   3334 O  OE2   . GLU A 1 429 ? 0.068   14.533  10.406  1.00 40.52  ? 429 GLU A OE2   1 
ATOM   3335 N  N     . GLY A 1 430 ? 6.820   14.537  11.449  1.00 30.25  ? 430 GLY A N     1 
ATOM   3336 C  CA    . GLY A 1 430 ? 7.927   14.686  12.379  1.00 35.86  ? 430 GLY A CA    1 
ATOM   3337 C  C     . GLY A 1 430 ? 9.112   13.793  12.065  1.00 28.57  ? 430 GLY A C     1 
ATOM   3338 O  O     . GLY A 1 430 ? 8.938   12.655  11.617  1.00 29.10  ? 430 GLY A O     1 
ATOM   3339 N  N     . ILE A 1 431 ? 10.323  14.297  12.289  1.00 29.01  ? 431 ILE A N     1 
ATOM   3340 C  CA    . ILE A 1 431 ? 11.552  13.544  12.068  1.00 29.95  ? 431 ILE A CA    1 
ATOM   3341 C  C     . ILE A 1 431 ? 12.320  13.491  13.382  1.00 28.71  ? 431 ILE A C     1 
ATOM   3342 O  O     . ILE A 1 431 ? 12.478  14.515  14.055  1.00 31.93  ? 431 ILE A O     1 
ATOM   3343 C  CB    . ILE A 1 431 ? 12.407  14.169  10.950  1.00 30.24  ? 431 ILE A CB    1 
ATOM   3344 C  CG1   . ILE A 1 431 ? 11.633  14.171  9.627   1.00 32.63  ? 431 ILE A CG1   1 
ATOM   3345 C  CG2   . ILE A 1 431 ? 13.715  13.415  10.789  1.00 24.29  ? 431 ILE A CG2   1 
ATOM   3346 C  CD1   . ILE A 1 431 ? 12.352  14.902  8.505   1.00 34.74  ? 431 ILE A CD1   1 
ATOM   3347 N  N     . ILE A 1 432 ? 12.802  12.303  13.740  1.00 28.17  ? 432 ILE A N     1 
ATOM   3348 C  CA    . ILE A 1 432 ? 13.484  12.082  15.009  1.00 31.13  ? 432 ILE A CA    1 
ATOM   3349 C  C     . ILE A 1 432 ? 14.920  11.660  14.729  1.00 30.19  ? 432 ILE A C     1 
ATOM   3350 O  O     . ILE A 1 432 ? 15.160  10.734  13.947  1.00 32.14  ? 432 ILE A O     1 
ATOM   3351 C  CB    . ILE A 1 432 ? 12.765  11.023  15.863  1.00 32.77  ? 432 ILE A CB    1 
ATOM   3352 C  CG1   . ILE A 1 432 ? 11.286  11.379  16.029  1.00 27.49  ? 432 ILE A CG1   1 
ATOM   3353 C  CG2   . ILE A 1 432 ? 13.437  10.890  17.225  1.00 27.84  ? 432 ILE A CG2   1 
ATOM   3354 C  CD1   . ILE A 1 432 ? 10.484  10.296  16.721  1.00 31.09  ? 432 ILE A CD1   1 
ATOM   3355 N  N     . PHE A 1 433 ? 15.868  12.344  15.359  1.00 25.56  ? 433 PHE A N     1 
ATOM   3356 C  CA    . PHE A 1 433 ? 17.261  11.925  15.372  1.00 25.62  ? 433 PHE A CA    1 
ATOM   3357 C  C     . PHE A 1 433 ? 17.624  11.439  16.767  1.00 29.38  ? 433 PHE A C     1 
ATOM   3358 O  O     . PHE A 1 433 ? 16.950  11.751  17.751  1.00 27.78  ? 433 PHE A O     1 
ATOM   3359 C  CB    . PHE A 1 433 ? 18.201  13.067  14.960  1.00 26.15  ? 433 PHE A CB    1 
ATOM   3360 C  CG    . PHE A 1 433 ? 18.005  13.545  13.549  1.00 26.62  ? 433 PHE A CG    1 
ATOM   3361 C  CD1   . PHE A 1 433 ? 18.194  12.687  12.476  1.00 27.65  ? 433 PHE A CD1   1 
ATOM   3362 C  CD2   . PHE A 1 433 ? 17.656  14.861  13.295  1.00 25.85  ? 433 PHE A CD2   1 
ATOM   3363 C  CE1   . PHE A 1 433 ? 18.018  13.131  11.171  1.00 25.45  ? 433 PHE A CE1   1 
ATOM   3364 C  CE2   . PHE A 1 433 ? 17.482  15.311  11.996  1.00 30.10  ? 433 PHE A CE2   1 
ATOM   3365 C  CZ    . PHE A 1 433 ? 17.666  14.444  10.933  1.00 26.12  ? 433 PHE A CZ    1 
ATOM   3366 N  N     . GLY A 1 434 ? 18.702  10.664  16.846  1.00 28.26  ? 434 GLY A N     1 
ATOM   3367 C  CA    . GLY A 1 434 ? 19.171  10.186  18.130  1.00 27.73  ? 434 GLY A CA    1 
ATOM   3368 C  C     . GLY A 1 434 ? 20.205  9.086   18.030  1.00 31.36  ? 434 GLY A C     1 
ATOM   3369 O  O     . GLY A 1 434 ? 20.276  8.384   17.019  1.00 31.75  ? 434 GLY A O     1 
ATOM   3370 N  N     . GLY A 1 435 ? 21.014  8.931   19.075  1.00 30.27  ? 435 GLY A N     1 
ATOM   3371 C  CA    . GLY A 1 435 ? 22.015  7.883   19.116  1.00 27.92  ? 435 GLY A CA    1 
ATOM   3372 C  C     . GLY A 1 435 ? 22.342  7.450   20.530  1.00 37.44  ? 435 GLY A C     1 
ATOM   3373 O  O     . GLY A 1 435 ? 21.683  7.874   21.483  1.00 39.63  ? 435 GLY A O     1 
ATOM   3374 N  N     . ARG A 1 436 ? 23.360  6.607   20.680  1.00 33.95  ? 436 ARG A N     1 
ATOM   3375 C  CA    . ARG A 1 436 ? 23.777  6.123   21.994  1.00 36.59  ? 436 ARG A CA    1 
ATOM   3376 C  C     . ARG A 1 436 ? 24.728  7.139   22.614  1.00 40.86  ? 436 ARG A C     1 
ATOM   3377 O  O     . ARG A 1 436 ? 25.909  7.197   22.266  1.00 41.88  ? 436 ARG A O     1 
ATOM   3378 C  CB    . ARG A 1 436 ? 24.429  4.751   21.874  1.00 34.75  ? 436 ARG A CB    1 
ATOM   3379 C  CG    . ARG A 1 436 ? 23.439  3.630   21.618  1.00 39.62  ? 436 ARG A CG    1 
ATOM   3380 C  CD    . ARG A 1 436 ? 24.134  2.339   21.226  1.00 36.21  ? 436 ARG A CD    1 
ATOM   3381 N  NE    . ARG A 1 436 ? 23.171  1.274   20.972  1.00 41.52  ? 436 ARG A NE    1 
ATOM   3382 C  CZ    . ARG A 1 436 ? 22.696  0.459   21.903  1.00 45.31  ? 436 ARG A CZ    1 
ATOM   3383 N  NH1   . ARG A 1 436 ? 23.095  0.542   23.163  1.00 52.62  ? 436 ARG A NH1   1 
ATOM   3384 N  NH2   . ARG A 1 436 ? 21.799  -0.462  21.562  1.00 46.54  ? 436 ARG A NH2   1 
ATOM   3385 N  N     . ARG A 1 437 ? 24.208  7.950   23.529  1.00 39.63  ? 437 ARG A N     1 
ATOM   3386 C  CA    . ARG A 1 437 ? 25.016  8.902   24.293  1.00 40.09  ? 437 ARG A CA    1 
ATOM   3387 C  C     . ARG A 1 437 ? 24.849  8.598   25.774  1.00 39.81  ? 437 ARG A C     1 
ATOM   3388 O  O     . ARG A 1 437 ? 23.771  8.866   26.339  1.00 37.00  ? 437 ARG A O     1 
ATOM   3389 C  CB    . ARG A 1 437 ? 24.609  10.346  23.997  1.00 35.15  ? 437 ARG A CB    1 
ATOM   3390 C  CG    . ARG A 1 437 ? 24.800  10.793  22.553  1.00 34.34  ? 437 ARG A CG    1 
ATOM   3391 C  CD    . ARG A 1 437 ? 26.252  10.684  22.098  1.00 43.84  ? 437 ARG A CD    1 
ATOM   3392 N  NE    . ARG A 1 437 ? 27.188  11.375  22.979  1.00 33.58  ? 437 ARG A NE    1 
ATOM   3393 C  CZ    . ARG A 1 437 ? 27.581  12.634  22.831  1.00 33.55  ? 437 ARG A CZ    1 
ATOM   3394 N  NH1   . ARG A 1 437 ? 27.095  13.404  21.871  1.00 31.42  ? 437 ARG A NH1   1 
ATOM   3395 N  NH2   . ARG A 1 437 ? 28.488  13.133  23.670  1.00 37.20  ? 437 ARG A NH2   1 
ATOM   3396 N  N     . PRO A 1 438 ? 25.864  8.044   26.443  1.00 43.98  ? 438 PRO A N     1 
ATOM   3397 C  CA    . PRO A 1 438 ? 25.699  7.687   27.861  1.00 44.46  ? 438 PRO A CA    1 
ATOM   3398 C  C     . PRO A 1 438 ? 25.697  8.880   28.801  1.00 46.61  ? 438 PRO A C     1 
ATOM   3399 O  O     . PRO A 1 438 ? 25.270  8.731   29.954  1.00 47.45  ? 438 PRO A O     1 
ATOM   3400 C  CB    . PRO A 1 438 ? 26.901  6.771   28.132  1.00 46.66  ? 438 PRO A CB    1 
ATOM   3401 C  CG    . PRO A 1 438 ? 27.940  7.234   27.162  1.00 42.34  ? 438 PRO A CG    1 
ATOM   3402 C  CD    . PRO A 1 438 ? 27.188  7.659   25.921  1.00 45.19  ? 438 PRO A CD    1 
ATOM   3403 N  N     . ALA A 1 439 ? 26.154  10.051  28.361  1.00 44.51  ? 439 ALA A N     1 
ATOM   3404 C  CA    . ALA A 1 439 ? 26.227  11.217  29.229  1.00 45.45  ? 439 ALA A CA    1 
ATOM   3405 C  C     . ALA A 1 439 ? 25.915  12.482  28.444  1.00 40.55  ? 439 ALA A C     1 
ATOM   3406 O  O     . ALA A 1 439 ? 26.083  12.534  27.222  1.00 43.41  ? 439 ALA A O     1 
ATOM   3407 C  CB    . ALA A 1 439 ? 27.609  11.342  29.890  1.00 44.09  ? 439 ALA A CB    1 
ATOM   3408 N  N     . GLY A 1 440 ? 25.442  13.496  29.165  1.00 39.45  ? 440 GLY A N     1 
ATOM   3409 C  CA    . GLY A 1 440 ? 25.253  14.854  28.664  1.00 37.87  ? 440 GLY A CA    1 
ATOM   3410 C  C     . GLY A 1 440 ? 24.008  15.195  27.859  1.00 43.13  ? 440 GLY A C     1 
ATOM   3411 O  O     . GLY A 1 440 ? 23.460  16.291  28.008  1.00 42.86  ? 440 GLY A O     1 
ATOM   3412 N  N     . VAL A 1 441 ? 23.556  14.285  27.004  1.00 39.46  ? 441 VAL A N     1 
ATOM   3413 C  CA    . VAL A 1 441 ? 22.492  14.570  26.046  1.00 36.98  ? 441 VAL A CA    1 
ATOM   3414 C  C     . VAL A 1 441 ? 21.156  14.237  26.702  1.00 34.39  ? 441 VAL A C     1 
ATOM   3415 O  O     . VAL A 1 441 ? 20.951  13.081  27.107  1.00 33.48  ? 441 VAL A O     1 
ATOM   3416 C  CB    . VAL A 1 441 ? 22.681  13.780  24.747  1.00 36.63  ? 441 VAL A CB    1 
ATOM   3417 C  CG1   . VAL A 1 441 ? 21.643  14.200  23.716  1.00 34.07  ? 441 VAL A CG1   1 
ATOM   3418 C  CG2   . VAL A 1 441 ? 24.087  13.992  24.210  1.00 37.55  ? 441 VAL A CG2   1 
ATOM   3419 N  N     . PRO A 1 442 ? 20.235  15.191  26.822  1.00 36.09  ? 442 PRO A N     1 
ATOM   3420 C  CA    . PRO A 1 442 ? 18.972  14.929  27.523  1.00 39.45  ? 442 PRO A CA    1 
ATOM   3421 C  C     . PRO A 1 442 ? 18.081  13.959  26.758  1.00 36.05  ? 442 PRO A C     1 
ATOM   3422 O  O     . PRO A 1 442 ? 18.362  13.557  25.628  1.00 33.67  ? 442 PRO A O     1 
ATOM   3423 C  CB    . PRO A 1 442 ? 18.328  16.314  27.632  1.00 38.27  ? 442 PRO A CB    1 
ATOM   3424 C  CG    . PRO A 1 442 ? 18.979  17.128  26.569  1.00 35.00  ? 442 PRO A CG    1 
ATOM   3425 C  CD    . PRO A 1 442 ? 20.376  16.604  26.436  1.00 35.65  ? 442 PRO A CD    1 
ATOM   3426 N  N     . LEU A 1 443 ? 16.975  13.592  27.414  1.00 35.24  ? 443 LEU A N     1 
ATOM   3427 C  CA    . LEU A 1 443 ? 16.097  12.542  26.903  1.00 33.47  ? 443 LEU A CA    1 
ATOM   3428 C  C     . LEU A 1 443 ? 15.470  12.930  25.569  1.00 32.74  ? 443 LEU A C     1 
ATOM   3429 O  O     . LEU A 1 443 ? 15.345  12.092  24.669  1.00 35.05  ? 443 LEU A O     1 
ATOM   3430 C  CB    . LEU A 1 443 ? 15.011  12.230  27.934  1.00 36.72  ? 443 LEU A CB    1 
ATOM   3431 C  CG    . LEU A 1 443 ? 13.915  11.236  27.547  1.00 37.73  ? 443 LEU A CG    1 
ATOM   3432 C  CD1   . LEU A 1 443 ? 14.493  9.844   27.336  1.00 38.61  ? 443 LEU A CD1   1 
ATOM   3433 C  CD2   . LEU A 1 443 ? 12.822  11.213  28.607  1.00 43.20  ? 443 LEU A CD2   1 
ATOM   3434 N  N     . VAL A 1 444 ? 15.067  14.189  25.423  1.00 29.86  ? 444 VAL A N     1 
ATOM   3435 C  CA    . VAL A 1 444 ? 14.425  14.652  24.197  1.00 33.64  ? 444 VAL A CA    1 
ATOM   3436 C  C     . VAL A 1 444 ? 14.480  16.173  24.172  1.00 31.21  ? 444 VAL A C     1 
ATOM   3437 O  O     . VAL A 1 444 ? 14.310  16.833  25.200  1.00 36.95  ? 444 VAL A O     1 
ATOM   3438 C  CB    . VAL A 1 444 ? 12.970  14.128  24.090  1.00 33.62  ? 444 VAL A CB    1 
ATOM   3439 C  CG1   . VAL A 1 444 ? 12.148  14.559  25.299  1.00 38.33  ? 444 VAL A CG1   1 
ATOM   3440 C  CG2   . VAL A 1 444 ? 12.320  14.601  22.795  1.00 28.70  ? 444 VAL A CG2   1 
ATOM   3441 N  N     . TYR A 1 445 ? 14.747  16.725  22.990  1.00 31.94  ? 445 TYR A N     1 
ATOM   3442 C  CA    . TYR A 1 445 ? 14.561  18.148  22.757  1.00 32.68  ? 445 TYR A CA    1 
ATOM   3443 C  C     . TYR A 1 445 ? 14.091  18.361  21.324  1.00 30.64  ? 445 TYR A C     1 
ATOM   3444 O  O     . TYR A 1 445 ? 14.140  17.458  20.486  1.00 31.79  ? 445 TYR A O     1 
ATOM   3445 C  CB    . TYR A 1 445 ? 15.828  18.965  23.064  1.00 31.60  ? 445 TYR A CB    1 
ATOM   3446 C  CG    . TYR A 1 445 ? 17.048  18.645  22.231  1.00 30.42  ? 445 TYR A CG    1 
ATOM   3447 C  CD1   . TYR A 1 445 ? 17.931  17.647  22.616  1.00 31.54  ? 445 TYR A CD1   1 
ATOM   3448 C  CD2   . TYR A 1 445 ? 17.338  19.368  21.080  1.00 34.15  ? 445 TYR A CD2   1 
ATOM   3449 C  CE1   . TYR A 1 445 ? 19.055  17.358  21.866  1.00 28.36  ? 445 TYR A CE1   1 
ATOM   3450 C  CE2   . TYR A 1 445 ? 18.463  19.086  20.323  1.00 32.46  ? 445 TYR A CE2   1 
ATOM   3451 C  CZ    . TYR A 1 445 ? 19.318  18.080  20.724  1.00 34.16  ? 445 TYR A CZ    1 
ATOM   3452 O  OH    . TYR A 1 445 ? 20.439  17.791  19.978  1.00 37.57  ? 445 TYR A OH    1 
ATOM   3453 N  N     . GLU A 1 446 ? 13.610  19.572  21.058  1.00 34.15  ? 446 GLU A N     1 
ATOM   3454 C  CA    . GLU A 1 446 ? 13.038  19.940  19.771  1.00 34.99  ? 446 GLU A CA    1 
ATOM   3455 C  C     . GLU A 1 446 ? 13.877  21.037  19.130  1.00 28.27  ? 446 GLU A C     1 
ATOM   3456 O  O     . GLU A 1 446 ? 14.328  21.965  19.809  1.00 31.88  ? 446 GLU A O     1 
ATOM   3457 C  CB    . GLU A 1 446 ? 11.587  20.407  19.939  1.00 35.23  ? 446 GLU A CB    1 
ATOM   3458 C  CG    . GLU A 1 446 ? 10.909  20.866  18.661  1.00 34.03  ? 446 GLU A CG    1 
ATOM   3459 C  CD    . GLU A 1 446 ? 9.531   21.448  18.920  1.00 39.77  ? 446 GLU A CD    1 
ATOM   3460 O  OE1   . GLU A 1 446 ? 8.831   20.946  19.823  1.00 41.04  ? 446 GLU A OE1   1 
ATOM   3461 O  OE2   . GLU A 1 446 ? 9.153   22.416  18.230  1.00 39.02  ? 446 GLU A OE2   1 
ATOM   3462 N  N     . ALA A 1 447 ? 14.089  20.921  17.821  1.00 28.86  ? 447 ALA A N     1 
ATOM   3463 C  CA    . ALA A 1 447 ? 14.881  21.904  17.097  1.00 31.08  ? 447 ALA A CA    1 
ATOM   3464 C  C     . ALA A 1 447 ? 14.160  23.246  17.045  1.00 34.05  ? 447 ALA A C     1 
ATOM   3465 O  O     . ALA A 1 447 ? 12.931  23.322  17.111  1.00 34.50  ? 447 ALA A O     1 
ATOM   3466 C  CB    . ALA A 1 447 ? 15.180  21.412  15.681  1.00 30.91  ? 447 ALA A CB    1 
ATOM   3467 N  N     . LEU A 1 448 ? 14.949  24.317  16.927  1.00 33.76  ? 448 LEU A N     1 
ATOM   3468 C  CA    . LEU A 1 448 ? 14.407  25.670  16.897  1.00 33.43  ? 448 LEU A CA    1 
ATOM   3469 C  C     . LEU A 1 448 ? 13.855  26.053  15.533  1.00 36.68  ? 448 LEU A C     1 
ATOM   3470 O  O     . LEU A 1 448 ? 13.025  26.965  15.447  1.00 34.07  ? 448 LEU A O     1 
ATOM   3471 C  CB    . LEU A 1 448 ? 15.484  26.676  17.303  1.00 31.32  ? 448 LEU A CB    1 
ATOM   3472 C  CG    . LEU A 1 448 ? 16.191  26.433  18.638  1.00 37.59  ? 448 LEU A CG    1 
ATOM   3473 C  CD1   . LEU A 1 448 ? 17.455  27.274  18.731  1.00 32.88  ? 448 LEU A CD1   1 
ATOM   3474 C  CD2   . LEU A 1 448 ? 15.256  26.745  19.789  1.00 40.53  ? 448 LEU A CD2   1 
ATOM   3475 N  N     . SER A 1 449 ? 14.299  25.387  14.475  1.00 32.04  ? 449 SER A N     1 
ATOM   3476 C  CA    . SER A 1 449 ? 13.908  25.720  13.111  1.00 33.87  ? 449 SER A CA    1 
ATOM   3477 C  C     . SER A 1 449 ? 14.326  24.558  12.221  1.00 33.15  ? 449 SER A C     1 
ATOM   3478 O  O     . SER A 1 449 ? 14.888  23.564  12.689  1.00 31.13  ? 449 SER A O     1 
ATOM   3479 C  CB    . SER A 1 449 ? 14.548  27.028  12.647  1.00 37.04  ? 449 SER A CB    1 
ATOM   3480 O  OG    . SER A 1 449 ? 15.959  26.899  12.585  1.00 37.76  ? 449 SER A OG    1 
ATOM   3481 N  N     . TRP A 1 450 ? 14.057  24.700  10.923  1.00 36.54  ? 450 TRP A N     1 
ATOM   3482 C  CA    . TRP A 1 450 ? 14.485  23.677  9.977   1.00 35.24  ? 450 TRP A CA    1 
ATOM   3483 C  C     . TRP A 1 450 ? 16.003  23.625  9.866   1.00 27.27  ? 450 TRP A C     1 
ATOM   3484 O  O     . TRP A 1 450 ? 16.590  22.538  9.815   1.00 28.62  ? 450 TRP A O     1 
ATOM   3485 C  CB    . TRP A 1 450 ? 13.864  23.932  8.607   1.00 31.23  ? 450 TRP A CB    1 
ATOM   3486 C  CG    . TRP A 1 450 ? 14.229  22.880  7.621   1.00 30.95  ? 450 TRP A CG    1 
ATOM   3487 C  CD1   . TRP A 1 450 ? 15.094  22.998  6.571   1.00 32.47  ? 450 TRP A CD1   1 
ATOM   3488 C  CD2   . TRP A 1 450 ? 13.758  21.531  7.605   1.00 28.89  ? 450 TRP A CD2   1 
ATOM   3489 N  NE1   . TRP A 1 450 ? 15.179  21.806  5.893   1.00 30.86  ? 450 TRP A NE1   1 
ATOM   3490 C  CE2   . TRP A 1 450 ? 14.368  20.889  6.509   1.00 31.29  ? 450 TRP A CE2   1 
ATOM   3491 C  CE3   . TRP A 1 450 ? 12.871  20.804  8.406   1.00 31.48  ? 450 TRP A CE3   1 
ATOM   3492 C  CZ2   . TRP A 1 450 ? 14.120  19.556  6.196   1.00 30.32  ? 450 TRP A CZ2   1 
ATOM   3493 C  CZ3   . TRP A 1 450 ? 12.627  19.480  8.093   1.00 33.15  ? 450 TRP A CZ3   1 
ATOM   3494 C  CH2   . TRP A 1 450 ? 13.251  18.869  6.999   1.00 33.32  ? 450 TRP A CH2   1 
ATOM   3495 N  N     . GLN A 1 451 ? 16.654  24.791  9.831   1.00 28.55  ? 451 GLN A N     1 
ATOM   3496 C  CA    . GLN A 1 451 ? 18.104  24.832  9.675   1.00 32.54  ? 451 GLN A CA    1 
ATOM   3497 C  C     . GLN A 1 451 ? 18.812  24.320  10.923  1.00 29.80  ? 451 GLN A C     1 
ATOM   3498 O  O     . GLN A 1 451 ? 19.843  23.644  10.825  1.00 26.84  ? 451 GLN A O     1 
ATOM   3499 C  CB    . GLN A 1 451 ? 18.558  26.255  9.340   1.00 35.26  ? 451 GLN A CB    1 
ATOM   3500 C  CG    . GLN A 1 451 ? 18.046  26.788  8.002   1.00 39.96  ? 451 GLN A CG    1 
ATOM   3501 C  CD    . GLN A 1 451 ? 16.599  27.252  8.063   1.00 45.87  ? 451 GLN A CD    1 
ATOM   3502 O  OE1   . GLN A 1 451 ? 16.118  27.689  9.108   1.00 42.13  ? 451 GLN A OE1   1 
ATOM   3503 N  NE2   . GLN A 1 451 ? 15.897  27.151  6.939   1.00 45.00  ? 451 GLN A NE2   1 
ATOM   3504 N  N     . HIS A 1 452 ? 18.278  24.631  12.106  1.00 29.04  ? 452 HIS A N     1 
ATOM   3505 C  CA    . HIS A 1 452 ? 18.837  24.058  13.327  1.00 26.00  ? 452 HIS A CA    1 
ATOM   3506 C  C     . HIS A 1 452 ? 18.632  22.550  13.365  1.00 28.43  ? 452 HIS A C     1 
ATOM   3507 O  O     . HIS A 1 452 ? 19.499  21.811  13.847  1.00 28.81  ? 452 HIS A O     1 
ATOM   3508 C  CB    . HIS A 1 452 ? 18.216  24.717  14.558  1.00 27.10  ? 452 HIS A CB    1 
ATOM   3509 C  CG    . HIS A 1 452 ? 18.736  24.178  15.855  1.00 32.13  ? 452 HIS A CG    1 
ATOM   3510 N  ND1   . HIS A 1 452 ? 17.917  23.625  16.816  1.00 33.03  ? 452 HIS A ND1   1 
ATOM   3511 C  CD2   . HIS A 1 452 ? 19.997  24.095  16.344  1.00 27.87  ? 452 HIS A CD2   1 
ATOM   3512 C  CE1   . HIS A 1 452 ? 18.649  23.229  17.843  1.00 30.13  ? 452 HIS A CE1   1 
ATOM   3513 N  NE2   . HIS A 1 452 ? 19.915  23.503  17.582  1.00 26.77  ? 452 HIS A NE2   1 
ATOM   3514 N  N     . GLY A 1 453 ? 17.496  22.073  12.853  1.00 26.37  ? 453 GLY A N     1 
ATOM   3515 C  CA    . GLY A 1 453 ? 17.254  20.642  12.824  1.00 25.65  ? 453 GLY A CA    1 
ATOM   3516 C  C     . GLY A 1 453 ? 18.214  19.904  11.912  1.00 27.72  ? 453 GLY A C     1 
ATOM   3517 O  O     . GLY A 1 453 ? 18.655  18.796  12.230  1.00 27.18  ? 453 GLY A O     1 
ATOM   3518 N  N     . VAL A 1 454 ? 18.544  20.499  10.763  1.00 27.45  ? 454 VAL A N     1 
ATOM   3519 C  CA    . VAL A 1 454 ? 19.550  19.907  9.886   1.00 27.12  ? 454 VAL A CA    1 
ATOM   3520 C  C     . VAL A 1 454 ? 20.902  19.871  10.587  1.00 27.11  ? 454 VAL A C     1 
ATOM   3521 O  O     . VAL A 1 454 ? 21.652  18.894  10.476  1.00 24.88  ? 454 VAL A O     1 
ATOM   3522 C  CB    . VAL A 1 454 ? 19.618  20.674  8.551   1.00 31.40  ? 454 VAL A CB    1 
ATOM   3523 C  CG1   . VAL A 1 454 ? 20.754  20.148  7.685   1.00 25.95  ? 454 VAL A CG1   1 
ATOM   3524 C  CG2   . VAL A 1 454 ? 18.290  20.562  7.810   1.00 28.95  ? 454 VAL A CG2   1 
ATOM   3525 N  N     . PHE A 1 455 ? 21.228  20.930  11.331  1.00 28.41  ? 455 PHE A N     1 
ATOM   3526 C  CA    . PHE A 1 455 ? 22.461  20.929  12.111  1.00 26.74  ? 455 PHE A CA    1 
ATOM   3527 C  C     . PHE A 1 455 ? 22.443  19.834  13.172  1.00 25.50  ? 455 PHE A C     1 
ATOM   3528 O  O     . PHE A 1 455 ? 23.462  19.175  13.408  1.00 30.11  ? 455 PHE A O     1 
ATOM   3529 C  CB    . PHE A 1 455 ? 22.678  22.298  12.755  1.00 24.54  ? 455 PHE A CB    1 
ATOM   3530 C  CG    . PHE A 1 455 ? 23.756  22.307  13.802  1.00 26.42  ? 455 PHE A CG    1 
ATOM   3531 C  CD1   . PHE A 1 455 ? 25.087  22.418  13.441  1.00 27.48  ? 455 PHE A CD1   1 
ATOM   3532 C  CD2   . PHE A 1 455 ? 23.437  22.197  15.146  1.00 29.01  ? 455 PHE A CD2   1 
ATOM   3533 C  CE1   . PHE A 1 455 ? 26.086  22.421  14.404  1.00 33.09  ? 455 PHE A CE1   1 
ATOM   3534 C  CE2   . PHE A 1 455 ? 24.429  22.199  16.114  1.00 35.75  ? 455 PHE A CE2   1 
ATOM   3535 C  CZ    . PHE A 1 455 ? 25.754  22.311  15.741  1.00 30.62  ? 455 PHE A CZ    1 
ATOM   3536 N  N     . VAL A 1 456 ? 21.294  19.629  13.824  1.00 27.58  ? 456 VAL A N     1 
ATOM   3537 C  CA    . VAL A 1 456 ? 21.179  18.575  14.832  1.00 24.28  ? 456 VAL A CA    1 
ATOM   3538 C  C     . VAL A 1 456 ? 21.483  17.216  14.216  1.00 29.39  ? 456 VAL A C     1 
ATOM   3539 O  O     . VAL A 1 456 ? 22.227  16.407  14.785  1.00 21.92  ? 456 VAL A O     1 
ATOM   3540 C  CB    . VAL A 1 456 ? 19.783  18.596  15.481  1.00 29.44  ? 456 VAL A CB    1 
ATOM   3541 C  CG1   . VAL A 1 456 ? 19.566  17.335  16.313  1.00 28.04  ? 456 VAL A CG1   1 
ATOM   3542 C  CG2   . VAL A 1 456 ? 19.613  19.836  16.340  1.00 29.94  ? 456 VAL A CG2   1 
ATOM   3543 N  N     . GLY A 1 457 ? 20.907  16.941  13.043  1.00 22.42  ? 457 GLY A N     1 
ATOM   3544 C  CA    . GLY A 1 457 ? 21.235  15.706  12.349  1.00 23.28  ? 457 GLY A CA    1 
ATOM   3545 C  C     . GLY A 1 457 ? 22.711  15.609  12.009  1.00 27.29  ? 457 GLY A C     1 
ATOM   3546 O  O     . GLY A 1 457 ? 23.330  14.558  12.184  1.00 28.54  ? 457 GLY A O     1 
ATOM   3547 N  N     . ALA A 1 458 ? 23.301  16.717  11.546  1.00 23.28  ? 458 ALA A N     1 
ATOM   3548 C  CA    . ALA A 1 458 ? 24.706  16.707  11.159  1.00 23.24  ? 458 ALA A CA    1 
ATOM   3549 C  C     . ALA A 1 458 ? 25.627  16.505  12.358  1.00 28.18  ? 458 ALA A C     1 
ATOM   3550 O  O     . ALA A 1 458 ? 26.749  16.007  12.197  1.00 27.18  ? 458 ALA A O     1 
ATOM   3551 C  CB    . ALA A 1 458 ? 25.060  18.007  10.432  1.00 25.20  ? 458 ALA A CB    1 
ATOM   3552 N  N     . ALA A 1 459 ? 25.175  16.870  13.556  1.00 26.51  ? 459 ALA A N     1 
ATOM   3553 C  CA    . ALA A 1 459 ? 25.996  16.786  14.756  1.00 27.92  ? 459 ALA A CA    1 
ATOM   3554 C  C     . ALA A 1 459 ? 25.826  15.476  15.512  1.00 27.63  ? 459 ALA A C     1 
ATOM   3555 O  O     . ALA A 1 459 ? 26.432  15.318  16.577  1.00 29.83  ? 459 ALA A O     1 
ATOM   3556 C  CB    . ALA A 1 459 ? 25.686  17.959  15.694  1.00 29.21  ? 459 ALA A CB    1 
ATOM   3557 N  N     . MET A 1 460 ? 25.038  14.537  14.986  1.00 22.75  ? 460 MET A N     1 
ATOM   3558 C  CA    . MET A 1 460 ? 24.776  13.280  15.681  1.00 23.60  ? 460 MET A CA    1 
ATOM   3559 C  C     . MET A 1 460 ? 26.064  12.532  15.998  1.00 29.14  ? 460 MET A C     1 
ATOM   3560 O  O     . MET A 1 460 ? 26.953  12.402  15.151  1.00 30.43  ? 460 MET A O     1 
ATOM   3561 C  CB    . MET A 1 460 ? 23.860  12.390  14.837  1.00 23.24  ? 460 MET A CB    1 
ATOM   3562 C  CG    . MET A 1 460 ? 22.404  12.814  14.821  1.00 26.60  ? 460 MET A CG    1 
ATOM   3563 S  SD    . MET A 1 460 ? 21.415  11.773  13.724  1.00 28.59  ? 460 MET A SD    1 
ATOM   3564 C  CE    . MET A 1 460 ? 21.733  10.151  14.410  1.00 22.89  ? 460 MET A CE    1 
ATOM   3565 N  N     . ARG A 1 461 ? 26.155  12.047  17.234  1.00 24.47  ? 461 ARG A N     1 
ATOM   3566 C  CA    . ARG A 1 461 ? 27.233  11.178  17.678  1.00 31.86  ? 461 ARG A CA    1 
ATOM   3567 C  C     . ARG A 1 461 ? 26.633  10.017  18.455  1.00 33.50  ? 461 ARG A C     1 
ATOM   3568 O  O     . ARG A 1 461 ? 25.534  10.126  19.006  1.00 35.68  ? 461 ARG A O     1 
ATOM   3569 C  CB    . ARG A 1 461 ? 28.255  11.932  18.546  1.00 31.13  ? 461 ARG A CB    1 
ATOM   3570 C  CG    . ARG A 1 461 ? 28.964  13.066  17.821  1.00 28.85  ? 461 ARG A CG    1 
ATOM   3571 C  CD    . ARG A 1 461 ? 29.824  13.875  18.776  1.00 32.23  ? 461 ARG A CD    1 
ATOM   3572 N  NE    . ARG A 1 461 ? 31.053  13.180  19.135  1.00 36.78  ? 461 ARG A NE    1 
ATOM   3573 C  CZ    . ARG A 1 461 ? 31.827  13.510  20.160  1.00 38.33  ? 461 ARG A CZ    1 
ATOM   3574 N  NH1   . ARG A 1 461 ? 31.505  14.497  20.979  1.00 37.14  ? 461 ARG A NH1   1 
ATOM   3575 N  NH2   . ARG A 1 461 ? 32.949  12.828  20.372  1.00 41.10  ? 461 ARG A NH2   1 
ATOM   3576 N  N     . SER A 1 462 ? 27.356  8.900   18.494  1.00 35.43  ? 462 SER A N     1 
ATOM   3577 C  CA    . SER A 1 462 ? 26.809  7.694   19.099  1.00 37.35  ? 462 SER A CA    1 
ATOM   3578 C  C     . SER A 1 462 ? 27.929  6.705   19.384  1.00 41.95  ? 462 SER A C     1 
ATOM   3579 O  O     . SER A 1 462 ? 28.972  6.716   18.723  1.00 42.40  ? 462 SER A O     1 
ATOM   3580 C  CB    . SER A 1 462 ? 25.753  7.052   18.192  1.00 35.70  ? 462 SER A CB    1 
ATOM   3581 O  OG    . SER A 1 462 ? 25.200  5.891   18.786  1.00 36.01  ? 462 SER A OG    1 
ATOM   3582 N  N     . GLU A 1 463 ? 27.697  5.851   20.379  1.00 41.97  ? 463 GLU A N     1 
ATOM   3583 C  CA    . GLU A 1 463 ? 28.619  4.758   20.653  1.00 50.25  ? 463 GLU A CA    1 
ATOM   3584 C  C     . GLU A 1 463 ? 28.655  3.792   19.475  1.00 46.79  ? 463 GLU A C     1 
ATOM   3585 O  O     . GLU A 1 463 ? 27.660  3.597   18.772  1.00 37.52  ? 463 GLU A O     1 
ATOM   3586 C  CB    . GLU A 1 463 ? 28.206  4.007   21.920  1.00 52.05  ? 463 GLU A CB    1 
ATOM   3587 C  CG    . GLU A 1 463 ? 28.311  4.810   23.203  1.00 59.91  ? 463 GLU A CG    1 
ATOM   3588 C  CD    . GLU A 1 463 ? 28.123  3.946   24.437  1.00 71.89  ? 463 GLU A CD    1 
ATOM   3589 O  OE1   . GLU A 1 463 ? 27.595  2.822   24.302  1.00 70.99  ? 463 GLU A OE1   1 
ATOM   3590 O  OE2   . GLU A 1 463 ? 28.512  4.385   25.540  1.00 79.63  ? 463 GLU A OE2   1 
ATOM   3591 N  N     . ALA A 1 464 ? 29.818  3.185   19.261  1.00 50.38  ? 464 ALA A N     1 
ATOM   3592 C  CA    . ALA A 1 464 ? 29.947  2.175   18.221  1.00 53.41  ? 464 ALA A CA    1 
ATOM   3593 C  C     . ALA A 1 464 ? 29.169  0.919   18.602  1.00 51.83  ? 464 ALA A C     1 
ATOM   3594 O  O     . ALA A 1 464 ? 28.991  0.603   19.781  1.00 53.18  ? 464 ALA A O     1 
ATOM   3595 C  CB    . ALA A 1 464 ? 31.418  1.835   17.983  1.00 56.94  ? 464 ALA A CB    1 
ATOM   3596 N  N     . THR A 1 465 ? 28.696  0.203   17.584  1.00 49.38  ? 465 THR A N     1 
ATOM   3597 C  CA    . THR A 1 465 ? 27.891  -0.996  17.771  1.00 45.16  ? 465 THR A CA    1 
ATOM   3598 C  C     . THR A 1 465 ? 28.533  -2.158  17.020  1.00 50.20  ? 465 THR A C     1 
ATOM   3599 O  O     . THR A 1 465 ? 29.594  -2.022  16.404  1.00 50.14  ? 465 THR A O     1 
ATOM   3600 C  CB    . THR A 1 465 ? 26.448  -0.781  17.294  1.00 48.12  ? 465 THR A CB    1 
ATOM   3601 O  OG1   . THR A 1 465 ? 26.440  -0.564  15.878  1.00 49.28  ? 465 THR A OG1   1 
ATOM   3602 C  CG2   . THR A 1 465 ? 25.823  0.424   17.989  1.00 43.05  ? 465 THR A CG2   1 
ATOM   3603 N  N     . ALA A 1 466 ? 27.871  -3.312  17.073  1.00 46.51  ? 466 ALA A N     1 
ATOM   3604 C  CA    . ALA A 1 466 ? 28.347  -4.527  16.429  1.00 48.64  ? 466 ALA A CA    1 
ATOM   3605 C  C     . ALA A 1 466 ? 27.896  -4.647  14.978  1.00 47.91  ? 466 ALA A C     1 
ATOM   3606 O  O     . ALA A 1 466 ? 28.127  -5.688  14.355  1.00 48.75  ? 466 ALA A O     1 
ATOM   3607 C  CB    . ALA A 1 466 ? 27.882  -5.755  17.216  1.00 48.04  ? 466 ALA A CB    1 
ATOM   3608 N  N     . ALA A 1 467 ? 27.261  -3.613  14.426  1.00 51.04  ? 467 ALA A N     1 
ATOM   3609 C  CA    . ALA A 1 467 ? 26.763  -3.707  13.059  1.00 50.02  ? 467 ALA A CA    1 
ATOM   3610 C  C     . ALA A 1 467 ? 27.878  -3.574  12.031  1.00 49.71  ? 467 ALA A C     1 
ATOM   3611 O  O     . ALA A 1 467 ? 27.741  -4.076  10.909  1.00 46.61  ? 467 ALA A O     1 
ATOM   3612 C  CB    . ALA A 1 467 ? 25.693  -2.646  12.816  1.00 40.73  ? 467 ALA A CB    1 
ATOM   3613 N  N     . ALA A 1 468 ? 28.975  -2.908  12.387  1.00 48.25  ? 468 ALA A N     1 
ATOM   3614 C  CA    . ALA A 1 468 ? 30.122  -2.783  11.497  1.00 55.97  ? 468 ALA A CA    1 
ATOM   3615 C  C     . ALA A 1 468 ? 31.363  -3.368  12.158  1.00 51.70  ? 468 ALA A C     1 
ATOM   3616 O  O     . ALA A 1 468 ? 31.255  -4.248  13.018  1.00 59.43  ? 468 ALA A O     1 
ATOM   3617 C  CB    . ALA A 1 468 ? 30.347  -1.319  11.109  1.00 50.27  ? 468 ALA A CB    1 
ATOM   3618 N  N     . GLU A 1 469 ? 32.546  -2.889  11.773  1.00 60.17  ? 469 GLU A N     1 
ATOM   3619 C  CA    . GLU A 1 469 ? 33.803  -3.429  12.276  1.00 64.33  ? 469 GLU A CA    1 
ATOM   3620 C  C     . GLU A 1 469 ? 34.417  -2.565  13.376  1.00 68.54  ? 469 GLU A C     1 
ATOM   3621 O  O     . GLU A 1 469 ? 35.608  -2.704  13.671  1.00 74.25  ? 469 GLU A O     1 
ATOM   3622 C  CB    . GLU A 1 469 ? 34.798  -3.613  11.126  1.00 61.83  ? 469 GLU A CB    1 
ATOM   3623 C  CG    . GLU A 1 469 ? 35.384  -2.323  10.554  1.00 60.77  ? 469 GLU A CG    1 
ATOM   3624 C  CD    . GLU A 1 469 ? 34.498  -1.670  9.507   1.00 59.56  ? 469 GLU A CD    1 
ATOM   3625 O  OE1   . GLU A 1 469 ? 33.257  -1.752  9.625   1.00 51.98  ? 469 GLU A OE1   1 
ATOM   3626 O  OE2   . GLU A 1 469 ? 35.049  -1.072  8.557   1.00 57.48  ? 469 GLU A OE2   1 
ATOM   3627 N  N     . HIS A 1 470 ? 33.628  -1.695  14.000  1.00 76.47  ? 470 HIS A N     1 
ATOM   3628 C  CA    . HIS A 1 470 ? 34.138  -0.787  15.018  1.00 81.17  ? 470 HIS A CA    1 
ATOM   3629 C  C     . HIS A 1 470 ? 34.029  -1.411  16.403  1.00 89.35  ? 470 HIS A C     1 
ATOM   3630 O  O     . HIS A 1 470 ? 33.020  -2.037  16.740  1.00 88.16  ? 470 HIS A O     1 
ATOM   3631 C  CB    . HIS A 1 470 ? 33.379  0.540   14.976  1.00 80.02  ? 470 HIS A CB    1 
ATOM   3632 C  CG    . HIS A 1 470 ? 33.349  1.172   13.618  1.00 77.26  ? 470 HIS A CG    1 
ATOM   3633 N  ND1   . HIS A 1 470 ? 34.428  1.843   13.085  1.00 81.68  ? 470 HIS A ND1   1 
ATOM   3634 C  CD2   . HIS A 1 470 ? 32.372  1.227   12.682  1.00 74.59  ? 470 HIS A CD2   1 
ATOM   3635 C  CE1   . HIS A 1 470 ? 34.116  2.287   11.880  1.00 73.38  ? 470 HIS A CE1   1 
ATOM   3636 N  NE2   . HIS A 1 470 ? 32.874  1.928   11.612  1.00 72.57  ? 470 HIS A NE2   1 
ATOM   3637 N  N     . LYS A 1 471 ? 35.078  -1.234  17.204  1.00 95.90  ? 471 LYS A N     1 
ATOM   3638 C  CA    . LYS A 1 471 ? 35.145  -1.784  18.549  1.00 104.65 ? 471 LYS A CA    1 
ATOM   3639 C  C     . LYS A 1 471 ? 35.490  -0.681  19.541  1.00 112.41 ? 471 LYS A C     1 
ATOM   3640 O  O     . LYS A 1 471 ? 35.967  0.393   19.168  1.00 107.18 ? 471 LYS A O     1 
ATOM   3641 C  CB    . LYS A 1 471 ? 36.188  -2.908  18.649  1.00 105.93 ? 471 LYS A CB    1 
ATOM   3642 C  CG    . LYS A 1 471 ? 35.954  -4.078  17.708  1.00 104.03 ? 471 LYS A CG    1 
ATOM   3643 C  CD    . LYS A 1 471 ? 34.674  -4.820  18.048  1.00 105.59 ? 471 LYS A CD    1 
ATOM   3644 C  CE    . LYS A 1 471 ? 34.570  -6.120  17.267  1.00 102.02 ? 471 LYS A CE    1 
ATOM   3645 N  NZ    . LYS A 1 471 ? 35.693  -7.047  17.588  1.00 106.09 ? 471 LYS A NZ    1 
ATOM   3646 N  N     . GLY A 1 472 ? 35.240  -0.964  20.820  1.00 120.84 ? 472 GLY A N     1 
ATOM   3647 C  CA    . GLY A 1 472 ? 35.634  -0.090  21.903  1.00 120.48 ? 472 GLY A CA    1 
ATOM   3648 C  C     . GLY A 1 472 ? 34.534  0.782   22.472  1.00 113.66 ? 472 GLY A C     1 
ATOM   3649 O  O     . GLY A 1 472 ? 34.775  1.473   23.470  1.00 116.76 ? 472 GLY A O     1 
ATOM   3650 N  N     . LYS A 1 473 ? 33.341  0.775   21.870  1.00 114.21 ? 473 LYS A N     1 
ATOM   3651 C  CA    . LYS A 1 473 ? 32.229  1.632   22.291  1.00 111.86 ? 473 LYS A CA    1 
ATOM   3652 C  C     . LYS A 1 473 ? 32.617  3.110   22.292  1.00 113.19 ? 473 LYS A C     1 
ATOM   3653 O  O     . LYS A 1 473 ? 32.032  3.918   23.018  1.00 114.05 ? 473 LYS A O     1 
ATOM   3654 C  CB    . LYS A 1 473 ? 31.689  1.220   23.665  1.00 114.75 ? 473 LYS A CB    1 
ATOM   3655 C  CG    . LYS A 1 473 ? 30.434  0.361   23.611  1.00 116.76 ? 473 LYS A CG    1 
ATOM   3656 C  CD    . LYS A 1 473 ? 29.897  0.078   25.005  1.00 119.75 ? 473 LYS A CD    1 
ATOM   3657 C  CE    . LYS A 1 473 ? 28.524  -0.575  24.951  1.00 121.19 ? 473 LYS A CE    1 
ATOM   3658 N  NZ    . LYS A 1 473 ? 28.544  -1.863  24.205  1.00 124.57 ? 473 LYS A NZ    1 
ATOM   3659 N  N     . VAL A 1 474 ? 33.610  3.468   21.476  1.00 92.79  ? 474 VAL A N     1 
ATOM   3660 C  CA    . VAL A 1 474 ? 34.039  4.856   21.363  1.00 72.81  ? 474 VAL A CA    1 
ATOM   3661 C  C     . VAL A 1 474 ? 32.944  5.673   20.690  1.00 63.02  ? 474 VAL A C     1 
ATOM   3662 O  O     . VAL A 1 474 ? 32.257  5.195   19.777  1.00 59.15  ? 474 VAL A O     1 
ATOM   3663 C  CB    . VAL A 1 474 ? 35.372  4.928   20.594  1.00 69.25  ? 474 VAL A CB    1 
ATOM   3664 C  CG1   . VAL A 1 474 ? 35.434  6.153   19.692  1.00 60.09  ? 474 VAL A CG1   1 
ATOM   3665 C  CG2   . VAL A 1 474 ? 36.541  4.922   21.569  1.00 69.41  ? 474 VAL A CG2   1 
ATOM   3666 N  N     . ILE A 1 475 ? 32.761  6.907   21.155  1.00 56.91  ? 475 ILE A N     1 
ATOM   3667 C  CA    . ILE A 1 475 ? 31.724  7.789   20.626  1.00 52.64  ? 475 ILE A CA    1 
ATOM   3668 C  C     . ILE A 1 475 ? 32.197  8.344   19.285  1.00 48.80  ? 475 ILE A C     1 
ATOM   3669 O  O     . ILE A 1 475 ? 33.158  9.116   19.222  1.00 47.46  ? 475 ILE A O     1 
ATOM   3670 C  CB    . ILE A 1 475 ? 31.392  8.916   21.610  1.00 48.74  ? 475 ILE A CB    1 
ATOM   3671 C  CG1   . ILE A 1 475 ? 30.880  8.327   22.928  1.00 48.07  ? 475 ILE A CG1   1 
ATOM   3672 C  CG2   . ILE A 1 475 ? 30.368  9.868   21.007  1.00 42.48  ? 475 ILE A CG2   1 
ATOM   3673 C  CD1   . ILE A 1 475 ? 30.451  9.362   23.940  1.00 54.62  ? 475 ILE A CD1   1 
ATOM   3674 N  N     . MET A 1 476 ? 31.520  7.950   18.210  1.00 42.86  ? 476 MET A N     1 
ATOM   3675 C  CA    . MET A 1 476 ? 31.855  8.358   16.855  1.00 37.60  ? 476 MET A CA    1 
ATOM   3676 C  C     . MET A 1 476 ? 30.820  9.338   16.323  1.00 39.37  ? 476 MET A C     1 
ATOM   3677 O  O     . MET A 1 476 ? 29.714  9.460   16.856  1.00 35.80  ? 476 MET A O     1 
ATOM   3678 C  CB    . MET A 1 476 ? 31.922  7.152   15.911  1.00 43.98  ? 476 MET A CB    1 
ATOM   3679 C  CG    . MET A 1 476 ? 32.914  6.077   16.292  1.00 50.59  ? 476 MET A CG    1 
ATOM   3680 S  SD    . MET A 1 476 ? 32.847  4.713   15.111  1.00 60.69  ? 476 MET A SD    1 
ATOM   3681 C  CE    . MET A 1 476 ? 33.276  5.565   13.593  1.00 56.79  ? 476 MET A CE    1 
ATOM   3682 N  N     . HIS A 1 477 ? 31.192  10.027  15.248  1.00 30.31  ? 477 HIS A N     1 
ATOM   3683 C  CA    . HIS A 1 477 ? 30.247  10.856  14.516  1.00 34.53  ? 477 HIS A CA    1 
ATOM   3684 C  C     . HIS A 1 477 ? 29.478  10.001  13.518  1.00 32.42  ? 477 HIS A C     1 
ATOM   3685 O  O     . HIS A 1 477 ? 30.051  9.142   12.842  1.00 33.66  ? 477 HIS A O     1 
ATOM   3686 C  CB    . HIS A 1 477 ? 30.971  11.986  13.784  1.00 32.75  ? 477 HIS A CB    1 
ATOM   3687 C  CG    . HIS A 1 477 ? 31.567  13.014  14.694  1.00 34.67  ? 477 HIS A CG    1 
ATOM   3688 N  ND1   . HIS A 1 477 ? 30.949  14.216  14.964  1.00 27.52  ? 477 HIS A ND1   1 
ATOM   3689 C  CD2   . HIS A 1 477 ? 32.725  13.020  15.396  1.00 34.68  ? 477 HIS A CD2   1 
ATOM   3690 C  CE1   . HIS A 1 477 ? 31.700  14.919  15.792  1.00 36.77  ? 477 HIS A CE1   1 
ATOM   3691 N  NE2   . HIS A 1 477 ? 32.783  14.215  16.071  1.00 35.06  ? 477 HIS A NE2   1 
ATOM   3692 N  N     . ASP A 1 478 ? 28.168  10.235  13.436  1.00 30.80  ? 478 ASP A N     1 
ATOM   3693 C  CA    . ASP A 1 478 ? 27.301  9.516   12.501  1.00 29.44  ? 478 ASP A CA    1 
ATOM   3694 C  C     . ASP A 1 478 ? 26.158  10.434  12.096  1.00 28.95  ? 478 ASP A C     1 
ATOM   3695 O  O     . ASP A 1 478 ? 25.004  10.238  12.496  1.00 29.94  ? 478 ASP A O     1 
ATOM   3696 C  CB    . ASP A 1 478 ? 26.777  8.224   13.127  1.00 30.24  ? 478 ASP A CB    1 
ATOM   3697 C  CG    . ASP A 1 478 ? 26.237  7.247   12.096  1.00 29.09  ? 478 ASP A CG    1 
ATOM   3698 O  OD1   . ASP A 1 478 ? 25.891  7.674   10.974  1.00 34.14  ? 478 ASP A OD1   1 
ATOM   3699 O  OD2   . ASP A 1 478 ? 26.155  6.044   12.410  1.00 28.33  ? 478 ASP A OD2   1 
ATOM   3700 N  N     . PRO A 1 479 ? 26.447  11.460  11.295  1.00 28.33  ? 479 PRO A N     1 
ATOM   3701 C  CA    . PRO A 1 479 ? 25.404  12.429  10.932  1.00 28.25  ? 479 PRO A CA    1 
ATOM   3702 C  C     . PRO A 1 479 ? 24.263  11.764  10.178  1.00 28.97  ? 479 PRO A C     1 
ATOM   3703 O  O     . PRO A 1 479 ? 24.483  10.990  9.245   1.00 25.95  ? 479 PRO A O     1 
ATOM   3704 C  CB    . PRO A 1 479 ? 26.149  13.444  10.054  1.00 25.82  ? 479 PRO A CB    1 
ATOM   3705 C  CG    . PRO A 1 479 ? 27.371  12.733  9.579   1.00 31.00  ? 479 PRO A CG    1 
ATOM   3706 C  CD    . PRO A 1 479 ? 27.745  11.785  10.678  1.00 32.30  ? 479 PRO A CD    1 
ATOM   3707 N  N     . PHE A 1 480 ? 23.035  12.064  10.609  1.00 28.01  ? 480 PHE A N     1 
ATOM   3708 C  CA    . PHE A 1 480 ? 21.804  11.563  10.001  1.00 24.91  ? 480 PHE A CA    1 
ATOM   3709 C  C     . PHE A 1 480 ? 21.713  10.044  10.033  1.00 28.45  ? 480 PHE A C     1 
ATOM   3710 O  O     . PHE A 1 480 ? 20.898  9.453   9.308   1.00 27.79  ? 480 PHE A O     1 
ATOM   3711 C  CB    . PHE A 1 480 ? 21.654  12.064  8.557   1.00 26.44  ? 480 PHE A CB    1 
ATOM   3712 C  CG    . PHE A 1 480 ? 21.318  13.525  8.454   1.00 28.82  ? 480 PHE A CG    1 
ATOM   3713 C  CD1   . PHE A 1 480 ? 22.291  14.492  8.657   1.00 22.70  ? 480 PHE A CD1   1 
ATOM   3714 C  CD2   . PHE A 1 480 ? 20.030  13.931  8.138   1.00 28.47  ? 480 PHE A CD2   1 
ATOM   3715 C  CE1   . PHE A 1 480 ? 21.985  15.833  8.562   1.00 23.46  ? 480 PHE A CE1   1 
ATOM   3716 C  CE2   . PHE A 1 480 ? 19.718  15.273  8.035   1.00 30.23  ? 480 PHE A CE2   1 
ATOM   3717 C  CZ    . PHE A 1 480 ? 20.696  16.226  8.247   1.00 28.76  ? 480 PHE A CZ    1 
ATOM   3718 N  N     . ALA A 1 481 ? 22.534  9.400   10.865  1.00 20.75  ? 481 ALA A N     1 
ATOM   3719 C  CA    . ALA A 1 481 ? 22.685  7.947   10.891  1.00 27.18  ? 481 ALA A CA    1 
ATOM   3720 C  C     . ALA A 1 481 ? 23.122  7.396   9.538   1.00 29.46  ? 481 ALA A C     1 
ATOM   3721 O  O     . ALA A 1 481 ? 22.882  6.222   9.232   1.00 30.84  ? 481 ALA A O     1 
ATOM   3722 C  CB    . ALA A 1 481 ? 21.394  7.259   11.349  1.00 25.24  ? 481 ALA A CB    1 
ATOM   3723 N  N     . MET A 1 482 ? 23.775  8.226   8.724   1.00 26.69  ? 482 MET A N     1 
ATOM   3724 C  CA    . MET A 1 482 ? 24.061  7.892   7.335   1.00 25.34  ? 482 MET A CA    1 
ATOM   3725 C  C     . MET A 1 482 ? 25.549  7.808   7.026   1.00 29.62  ? 482 MET A C     1 
ATOM   3726 O  O     . MET A 1 482 ? 25.910  7.671   5.851   1.00 32.65  ? 482 MET A O     1 
ATOM   3727 C  CB    . MET A 1 482 ? 23.398  8.915   6.409   1.00 29.58  ? 482 MET A CB    1 
ATOM   3728 C  CG    . MET A 1 482 ? 21.909  8.705   6.222   1.00 26.63  ? 482 MET A CG    1 
ATOM   3729 S  SD    . MET A 1 482 ? 21.578  7.413   5.017   1.00 29.42  ? 482 MET A SD    1 
ATOM   3730 C  CE    . MET A 1 482 ? 22.182  8.194   3.521   1.00 29.61  ? 482 MET A CE    1 
ATOM   3731 N  N     . ARG A 1 483 ? 26.416  7.881   8.035   1.00 30.02  ? 483 ARG A N     1 
ATOM   3732 C  CA    . ARG A 1 483 ? 27.855  7.838   7.785   1.00 27.92  ? 483 ARG A CA    1 
ATOM   3733 C  C     . ARG A 1 483 ? 28.303  6.655   6.933   1.00 31.44  ? 483 ARG A C     1 
ATOM   3734 O  O     . ARG A 1 483 ? 29.105  6.873   6.008   1.00 31.22  ? 483 ARG A O     1 
ATOM   3735 C  CB    . ARG A 1 483 ? 28.629  7.843   9.113   1.00 31.95  ? 483 ARG A CB    1 
ATOM   3736 C  CG    . ARG A 1 483 ? 30.133  7.989   8.915   1.00 36.33  ? 483 ARG A CG    1 
ATOM   3737 C  CD    . ARG A 1 483 ? 30.939  7.553   10.131  1.00 39.25  ? 483 ARG A CD    1 
ATOM   3738 N  NE    . ARG A 1 483 ? 30.907  6.108   10.327  1.00 41.53  ? 483 ARG A NE    1 
ATOM   3739 C  CZ    . ARG A 1 483 ? 30.263  5.500   11.314  1.00 43.61  ? 483 ARG A CZ    1 
ATOM   3740 N  NH1   . ARG A 1 483 ? 29.603  6.185   12.234  1.00 41.43  ? 483 ARG A NH1   1 
ATOM   3741 N  NH2   . ARG A 1 483 ? 30.288  4.172   11.384  1.00 46.02  ? 483 ARG A NH2   1 
ATOM   3742 N  N     . PRO A 1 484 ? 27.860  5.415   7.164   1.00 32.57  ? 484 PRO A N     1 
ATOM   3743 C  CA    . PRO A 1 484 ? 28.313  4.310   6.312   1.00 32.64  ? 484 PRO A CA    1 
ATOM   3744 C  C     . PRO A 1 484 ? 27.573  4.205   4.989   1.00 28.38  ? 484 PRO A C     1 
ATOM   3745 O  O     . PRO A 1 484 ? 27.846  3.273   4.223   1.00 31.57  ? 484 PRO A O     1 
ATOM   3746 C  CB    . PRO A 1 484 ? 28.043  3.063   7.180   1.00 33.38  ? 484 PRO A CB    1 
ATOM   3747 C  CG    . PRO A 1 484 ? 27.513  3.572   8.507   1.00 34.11  ? 484 PRO A CG    1 
ATOM   3748 C  CD    . PRO A 1 484 ? 26.968  4.925   8.231   1.00 30.22  ? 484 PRO A CD    1 
ATOM   3749 N  N     . PHE A 1 485 ? 26.658  5.129   4.696   1.00 27.73  ? 485 PHE A N     1 
ATOM   3750 C  CA    . PHE A 1 485 ? 25.716  4.944   3.604   1.00 32.03  ? 485 PHE A CA    1 
ATOM   3751 C  C     . PHE A 1 485 ? 25.614  6.122   2.645   1.00 31.03  ? 485 PHE A C     1 
ATOM   3752 O  O     . PHE A 1 485 ? 24.767  6.085   1.744   1.00 32.68  ? 485 PHE A O     1 
ATOM   3753 C  CB    . PHE A 1 485 ? 24.319  4.637   4.165   1.00 26.13  ? 485 PHE A CB    1 
ATOM   3754 C  CG    . PHE A 1 485 ? 24.300  3.509   5.157   1.00 27.85  ? 485 PHE A CG    1 
ATOM   3755 C  CD1   . PHE A 1 485 ? 24.741  2.246   4.795   1.00 28.64  ? 485 PHE A CD1   1 
ATOM   3756 C  CD2   . PHE A 1 485 ? 23.831  3.707   6.448   1.00 30.62  ? 485 PHE A CD2   1 
ATOM   3757 C  CE1   . PHE A 1 485 ? 24.724  1.198   5.703   1.00 30.09  ? 485 PHE A CE1   1 
ATOM   3758 C  CE2   . PHE A 1 485 ? 23.808  2.663   7.363   1.00 27.98  ? 485 PHE A CE2   1 
ATOM   3759 C  CZ    . PHE A 1 485 ? 24.256  1.407   6.988   1.00 29.16  ? 485 PHE A CZ    1 
ATOM   3760 N  N     . PHE A 1 486 ? 26.436  7.158   2.801   1.00 29.30  ? 486 PHE A N     1 
ATOM   3761 C  CA    . PHE A 1 486 ? 26.397  8.282   1.874   1.00 31.66  ? 486 PHE A CA    1 
ATOM   3762 C  C     . PHE A 1 486 ? 26.844  7.834   0.490   1.00 30.87  ? 486 PHE A C     1 
ATOM   3763 O  O     . PHE A 1 486 ? 27.897  7.208   0.337   1.00 32.29  ? 486 PHE A O     1 
ATOM   3764 C  CB    . PHE A 1 486 ? 27.289  9.425   2.363   1.00 32.52  ? 486 PHE A CB    1 
ATOM   3765 C  CG    . PHE A 1 486 ? 26.759  10.136  3.572   1.00 28.41  ? 486 PHE A CG    1 
ATOM   3766 C  CD1   . PHE A 1 486 ? 25.551  10.812  3.521   1.00 25.66  ? 486 PHE A CD1   1 
ATOM   3767 C  CD2   . PHE A 1 486 ? 27.476  10.144  4.757   1.00 28.86  ? 486 PHE A CD2   1 
ATOM   3768 C  CE1   . PHE A 1 486 ? 25.060  11.469  4.631   1.00 27.15  ? 486 PHE A CE1   1 
ATOM   3769 C  CE2   . PHE A 1 486 ? 26.992  10.802  5.870   1.00 25.67  ? 486 PHE A CE2   1 
ATOM   3770 C  CZ    . PHE A 1 486 ? 25.783  11.464  5.809   1.00 29.38  ? 486 PHE A CZ    1 
ATOM   3771 N  N     . GLY A 1 487 ? 26.037  8.145   -0.519  1.00 33.81  ? 487 GLY A N     1 
ATOM   3772 C  CA    . GLY A 1 487 ? 26.399  7.859   -1.887  1.00 31.37  ? 487 GLY A CA    1 
ATOM   3773 C  C     . GLY A 1 487 ? 27.039  9.007   -2.625  1.00 36.44  ? 487 GLY A C     1 
ATOM   3774 O  O     . GLY A 1 487 ? 27.383  8.857   -3.803  1.00 34.46  ? 487 GLY A O     1 
ATOM   3775 N  N     . TYR A 1 488 ? 27.208  10.154  -1.970  1.00 35.22  ? 488 TYR A N     1 
ATOM   3776 C  CA    . TYR A 1 488 ? 27.802  11.326  -2.599  1.00 37.17  ? 488 TYR A CA    1 
ATOM   3777 C  C     . TYR A 1 488 ? 28.250  12.295  -1.508  1.00 33.96  ? 488 TYR A C     1 
ATOM   3778 O  O     . TYR A 1 488 ? 28.066  12.045  -0.312  1.00 30.42  ? 488 TYR A O     1 
ATOM   3779 C  CB    . TYR A 1 488 ? 26.827  11.984  -3.582  1.00 35.48  ? 488 TYR A CB    1 
ATOM   3780 C  CG    . TYR A 1 488 ? 25.592  12.586  -2.949  1.00 34.48  ? 488 TYR A CG    1 
ATOM   3781 C  CD1   . TYR A 1 488 ? 24.529  11.785  -2.539  1.00 31.11  ? 488 TYR A CD1   1 
ATOM   3782 C  CD2   . TYR A 1 488 ? 25.480  13.958  -2.781  1.00 36.68  ? 488 TYR A CD2   1 
ATOM   3783 C  CE1   . TYR A 1 488 ? 23.397  12.339  -1.964  1.00 28.50  ? 488 TYR A CE1   1 
ATOM   3784 C  CE2   . TYR A 1 488 ? 24.354  14.519  -2.214  1.00 32.77  ? 488 TYR A CE2   1 
ATOM   3785 C  CZ    . TYR A 1 488 ? 23.316  13.708  -1.807  1.00 31.65  ? 488 TYR A CZ    1 
ATOM   3786 O  OH    . TYR A 1 488 ? 22.196  14.276  -1.241  1.00 30.03  ? 488 TYR A OH    1 
ATOM   3787 N  N     . ASN A 1 489 ? 28.839  13.409  -1.947  1.00 33.64  ? 489 ASN A N     1 
ATOM   3788 C  CA    . ASN A 1 489 ? 29.453  14.399  -1.066  1.00 38.54  ? 489 ASN A CA    1 
ATOM   3789 C  C     . ASN A 1 489 ? 28.515  14.812  0.064   1.00 34.95  ? 489 ASN A C     1 
ATOM   3790 O  O     . ASN A 1 489 ? 27.379  15.234  -0.175  1.00 31.83  ? 489 ASN A O     1 
ATOM   3791 C  CB    . ASN A 1 489 ? 29.862  15.620  -1.901  1.00 37.63  ? 489 ASN A CB    1 
ATOM   3792 C  CG    . ASN A 1 489 ? 30.736  16.601  -1.138  1.00 39.70  ? 489 ASN A CG    1 
ATOM   3793 O  OD1   . ASN A 1 489 ? 30.361  17.099  -0.078  1.00 40.48  ? 489 ASN A OD1   1 
ATOM   3794 N  ND2   . ASN A 1 489 ? 31.911  16.890  -1.687  1.00 39.28  ? 489 ASN A ND2   1 
ATOM   3795 N  N     . PHE A 1 490 ? 29.005  14.693  1.303   1.00 30.66  ? 490 PHE A N     1 
ATOM   3796 C  CA    . PHE A 1 490 ? 28.170  14.972  2.467   1.00 27.57  ? 490 PHE A CA    1 
ATOM   3797 C  C     . PHE A 1 490 ? 27.818  16.450  2.577   1.00 28.79  ? 490 PHE A C     1 
ATOM   3798 O  O     . PHE A 1 490 ? 26.739  16.789  3.079   1.00 32.42  ? 490 PHE A O     1 
ATOM   3799 C  CB    . PHE A 1 490 ? 28.866  14.494  3.744   1.00 32.47  ? 490 PHE A CB    1 
ATOM   3800 C  CG    . PHE A 1 490 ? 28.159  14.898  5.010   1.00 30.49  ? 490 PHE A CG    1 
ATOM   3801 C  CD1   . PHE A 1 490 ? 26.817  14.606  5.196   1.00 31.36  ? 490 PHE A CD1   1 
ATOM   3802 C  CD2   . PHE A 1 490 ? 28.844  15.557  6.021   1.00 37.45  ? 490 PHE A CD2   1 
ATOM   3803 C  CE1   . PHE A 1 490 ? 26.165  14.975  6.361   1.00 28.66  ? 490 PHE A CE1   1 
ATOM   3804 C  CE2   . PHE A 1 490 ? 28.200  15.924  7.190   1.00 32.60  ? 490 PHE A CE2   1 
ATOM   3805 C  CZ    . PHE A 1 490 ? 26.859  15.633  7.360   1.00 33.92  ? 490 PHE A CZ    1 
ATOM   3806 N  N     . GLY A 1 491 ? 28.704  17.341  2.129   1.00 31.61  ? 491 GLY A N     1 
ATOM   3807 C  CA    . GLY A 1 491 ? 28.354  18.752  2.087   1.00 30.75  ? 491 GLY A CA    1 
ATOM   3808 C  C     . GLY A 1 491 ? 27.182  19.026  1.164   1.00 35.87  ? 491 GLY A C     1 
ATOM   3809 O  O     . GLY A 1 491 ? 26.290  19.814  1.489   1.00 31.64  ? 491 GLY A O     1 
ATOM   3810 N  N     . LYS A 1 492 ? 27.161  18.367  0.003   1.00 30.28  ? 492 LYS A N     1 
ATOM   3811 C  CA    . LYS A 1 492 ? 26.035  18.517  -0.913  1.00 34.16  ? 492 LYS A CA    1 
ATOM   3812 C  C     . LYS A 1 492 ? 24.775  17.866  -0.357  1.00 29.85  ? 492 LYS A C     1 
ATOM   3813 O  O     . LYS A 1 492 ? 23.664  18.333  -0.633  1.00 34.69  ? 492 LYS A O     1 
ATOM   3814 C  CB    . LYS A 1 492 ? 26.386  17.927  -2.277  1.00 32.82  ? 492 LYS A CB    1 
ATOM   3815 C  CG    . LYS A 1 492 ? 27.698  18.440  -2.855  1.00 42.72  ? 492 LYS A CG    1 
ATOM   3816 C  CD    . LYS A 1 492 ? 27.747  19.959  -2.855  1.00 46.98  ? 492 LYS A CD    1 
ATOM   3817 C  CE    . LYS A 1 492 ? 29.105  20.471  -3.307  1.00 51.54  ? 492 LYS A CE    1 
ATOM   3818 N  NZ    . LYS A 1 492 ? 29.242  21.937  -3.082  1.00 60.10  ? 492 LYS A NZ    1 
ATOM   3819 N  N     . TYR A 1 493 ? 24.928  16.794  0.423   1.00 28.89  ? 493 TYR A N     1 
ATOM   3820 C  CA    . TYR A 1 493 ? 23.789  16.193  1.111   1.00 28.85  ? 493 TYR A CA    1 
ATOM   3821 C  C     . TYR A 1 493 ? 23.151  17.185  2.078   1.00 29.84  ? 493 TYR A C     1 
ATOM   3822 O  O     . TYR A 1 493 ? 21.920  17.292  2.150   1.00 28.54  ? 493 TYR A O     1 
ATOM   3823 C  CB    . TYR A 1 493 ? 24.257  14.924  1.832   1.00 26.05  ? 493 TYR A CB    1 
ATOM   3824 C  CG    . TYR A 1 493 ? 23.264  14.244  2.755   1.00 30.94  ? 493 TYR A CG    1 
ATOM   3825 C  CD1   . TYR A 1 493 ? 23.134  14.638  4.084   1.00 29.01  ? 493 TYR A CD1   1 
ATOM   3826 C  CD2   . TYR A 1 493 ? 22.501  13.168  2.317   1.00 25.62  ? 493 TYR A CD2   1 
ATOM   3827 C  CE1   . TYR A 1 493 ? 22.248  14.004  4.937   1.00 29.40  ? 493 TYR A CE1   1 
ATOM   3828 C  CE2   . TYR A 1 493 ? 21.614  12.525  3.165   1.00 28.81  ? 493 TYR A CE2   1 
ATOM   3829 C  CZ    . TYR A 1 493 ? 21.492  12.949  4.474   1.00 31.92  ? 493 TYR A CZ    1 
ATOM   3830 O  OH    . TYR A 1 493 ? 20.612  12.314  5.324   1.00 29.76  ? 493 TYR A OH    1 
ATOM   3831 N  N     . LEU A 1 494 ? 23.975  17.935  2.817   1.00 28.44  ? 494 LEU A N     1 
ATOM   3832 C  CA    . LEU A 1 494 ? 23.449  18.934  3.742   1.00 29.36  ? 494 LEU A CA    1 
ATOM   3833 C  C     . LEU A 1 494 ? 22.729  20.057  3.004   1.00 23.75  ? 494 LEU A C     1 
ATOM   3834 O  O     . LEU A 1 494 ? 21.675  20.525  3.450   1.00 28.27  ? 494 LEU A O     1 
ATOM   3835 C  CB    . LEU A 1 494 ? 24.583  19.502  4.598   1.00 25.69  ? 494 LEU A CB    1 
ATOM   3836 C  CG    . LEU A 1 494 ? 25.272  18.544  5.574   1.00 25.72  ? 494 LEU A CG    1 
ATOM   3837 C  CD1   . LEU A 1 494 ? 26.489  19.210  6.206   1.00 29.21  ? 494 LEU A CD1   1 
ATOM   3838 C  CD2   . LEU A 1 494 ? 24.296  18.085  6.644   1.00 28.32  ? 494 LEU A CD2   1 
ATOM   3839 N  N     . ALA A 1 495 ? 23.292  20.516  1.883   1.00 28.12  ? 495 ALA A N     1 
ATOM   3840 C  CA    . ALA A 1 495 ? 22.635  21.565  1.108   1.00 31.79  ? 495 ALA A CA    1 
ATOM   3841 C  C     . ALA A 1 495 ? 21.337  21.066  0.487   1.00 33.36  ? 495 ALA A C     1 
ATOM   3842 O  O     . ALA A 1 495 ? 20.385  21.840  0.330   1.00 35.00  ? 495 ALA A O     1 
ATOM   3843 C  CB    . ALA A 1 495 ? 23.578  22.092  0.025   1.00 28.61  ? 495 ALA A CB    1 
ATOM   3844 N  N     . HIS A 1 496 ? 21.285  19.781  0.133   1.00 30.87  ? 496 HIS A N     1 
ATOM   3845 C  CA    . HIS A 1 496 ? 20.050  19.177  -0.357  1.00 33.82  ? 496 HIS A CA    1 
ATOM   3846 C  C     . HIS A 1 496 ? 18.962  19.226  0.712   1.00 34.34  ? 496 HIS A C     1 
ATOM   3847 O  O     . HIS A 1 496 ? 17.823  19.622  0.440   1.00 35.69  ? 496 HIS A O     1 
ATOM   3848 C  CB    . HIS A 1 496 ? 20.338  17.740  -0.792  1.00 31.78  ? 496 HIS A CB    1 
ATOM   3849 C  CG    . HIS A 1 496 ? 19.227  17.089  -1.554  1.00 37.82  ? 496 HIS A CG    1 
ATOM   3850 N  ND1   . HIS A 1 496 ? 18.677  17.641  -2.691  1.00 34.02  ? 496 HIS A ND1   1 
ATOM   3851 C  CD2   . HIS A 1 496 ? 18.582  15.916  -1.354  1.00 31.72  ? 496 HIS A CD2   1 
ATOM   3852 C  CE1   . HIS A 1 496 ? 17.732  16.841  -3.151  1.00 33.73  ? 496 HIS A CE1   1 
ATOM   3853 N  NE2   . HIS A 1 496 ? 17.656  15.786  -2.361  1.00 36.60  ? 496 HIS A NE2   1 
ATOM   3854 N  N     . TRP A 1 497 ? 19.308  18.840  1.945   1.00 30.61  ? 497 TRP A N     1 
ATOM   3855 C  CA    . TRP A 1 497 ? 18.360  18.918  3.054   1.00 29.66  ? 497 TRP A CA    1 
ATOM   3856 C  C     . TRP A 1 497 ? 17.927  20.353  3.319   1.00 34.57  ? 497 TRP A C     1 
ATOM   3857 O  O     . TRP A 1 497 ? 16.741  20.618  3.549   1.00 36.41  ? 497 TRP A O     1 
ATOM   3858 C  CB    . TRP A 1 497 ? 18.978  18.317  4.317   1.00 24.69  ? 497 TRP A CB    1 
ATOM   3859 C  CG    . TRP A 1 497 ? 18.678  16.866  4.514   1.00 29.98  ? 497 TRP A CG    1 
ATOM   3860 C  CD1   . TRP A 1 497 ? 19.343  15.806  3.969   1.00 28.82  ? 497 TRP A CD1   1 
ATOM   3861 C  CD2   . TRP A 1 497 ? 17.635  16.313  5.325   1.00 29.71  ? 497 TRP A CD2   1 
ATOM   3862 N  NE1   . TRP A 1 497 ? 18.775  14.625  4.387   1.00 29.00  ? 497 TRP A NE1   1 
ATOM   3863 C  CE2   . TRP A 1 497 ? 17.726  14.910  5.222   1.00 32.61  ? 497 TRP A CE2   1 
ATOM   3864 C  CE3   . TRP A 1 497 ? 16.634  16.868  6.129   1.00 28.82  ? 497 TRP A CE3   1 
ATOM   3865 C  CZ2   . TRP A 1 497 ? 16.851  14.054  5.892   1.00 33.49  ? 497 TRP A CZ2   1 
ATOM   3866 C  CZ3   . TRP A 1 497 ? 15.766  16.017  6.793   1.00 33.40  ? 497 TRP A CZ3   1 
ATOM   3867 C  CH2   . TRP A 1 497 ? 15.880  14.626  6.670   1.00 36.64  ? 497 TRP A CH2   1 
ATOM   3868 N  N     . LEU A 1 498 ? 18.878  21.292  3.305   1.00 32.62  ? 498 LEU A N     1 
ATOM   3869 C  CA    . LEU A 1 498 ? 18.545  22.688  3.567   1.00 33.25  ? 498 LEU A CA    1 
ATOM   3870 C  C     . LEU A 1 498 ? 17.640  23.265  2.488   1.00 35.85  ? 498 LEU A C     1 
ATOM   3871 O  O     . LEU A 1 498 ? 16.788  24.109  2.784   1.00 39.64  ? 498 LEU A O     1 
ATOM   3872 C  CB    . LEU A 1 498 ? 19.821  23.524  3.686   1.00 33.48  ? 498 LEU A CB    1 
ATOM   3873 C  CG    . LEU A 1 498 ? 20.687  23.297  4.926   1.00 35.50  ? 498 LEU A CG    1 
ATOM   3874 C  CD1   . LEU A 1 498 ? 22.014  24.021  4.785   1.00 35.40  ? 498 LEU A CD1   1 
ATOM   3875 C  CD2   . LEU A 1 498 ? 19.959  23.756  6.180   1.00 28.35  ? 498 LEU A CD2   1 
ATOM   3876 N  N     . SER A 1 499 ? 17.796  22.813  1.240   1.00 38.40  ? 499 SER A N     1 
ATOM   3877 C  CA    . SER A 1 499 ? 17.034  23.375  0.130   1.00 42.13  ? 499 SER A CA    1 
ATOM   3878 C  C     . SER A 1 499 ? 15.545  23.067  0.221   1.00 41.90  ? 499 SER A C     1 
ATOM   3879 O  O     . SER A 1 499 ? 14.748  23.734  -0.447  1.00 49.19  ? 499 SER A O     1 
ATOM   3880 C  CB    . SER A 1 499 ? 17.578  22.855  -1.200  1.00 36.44  ? 499 SER A CB    1 
ATOM   3881 O  OG    . SER A 1 499 ? 17.243  21.490  -1.379  1.00 39.89  ? 499 SER A OG    1 
ATOM   3882 N  N     A MET A 1 500 ? 15.158  22.071  1.023   0.50 43.13  ? 500 MET A N     1 
ATOM   3883 N  N     B MET A 1 500 ? 15.149  22.078  1.023   0.50 43.13  ? 500 MET A N     1 
ATOM   3884 C  CA    A MET A 1 500 ? 13.746  21.729  1.160   0.50 44.75  ? 500 MET A CA    1 
ATOM   3885 C  CA    B MET A 1 500 ? 13.733  21.750  1.131   0.50 44.76  ? 500 MET A CA    1 
ATOM   3886 C  C     A MET A 1 500 ? 12.948  22.864  1.789   0.50 47.23  ? 500 MET A C     1 
ATOM   3887 C  C     B MET A 1 500 ? 12.937  22.848  1.820   0.50 47.23  ? 500 MET A C     1 
ATOM   3888 O  O     A MET A 1 500 ? 11.738  22.970  1.557   0.50 50.67  ? 500 MET A O     1 
ATOM   3889 O  O     B MET A 1 500 ? 11.714  22.906  1.654   0.50 50.69  ? 500 MET A O     1 
ATOM   3890 C  CB    A MET A 1 500 ? 13.593  20.449  1.982   0.50 42.89  ? 500 MET A CB    1 
ATOM   3891 C  CB    B MET A 1 500 ? 13.559  20.422  1.863   0.50 42.91  ? 500 MET A CB    1 
ATOM   3892 C  CG    A MET A 1 500 ? 14.254  19.227  1.359   0.50 43.17  ? 500 MET A CG    1 
ATOM   3893 C  CG    B MET A 1 500 ? 14.055  19.236  1.061   0.50 43.83  ? 500 MET A CG    1 
ATOM   3894 S  SD    A MET A 1 500 ? 13.592  18.829  -0.272  0.50 41.45  ? 500 MET A SD    1 
ATOM   3895 S  SD    B MET A 1 500 ? 13.787  17.676  1.906   0.50 49.09  ? 500 MET A SD    1 
ATOM   3896 C  CE    A MET A 1 500 ? 14.634  17.448  -0.734  0.50 42.73  ? 500 MET A CE    1 
ATOM   3897 C  CE    B MET A 1 500 ? 14.866  17.872  3.314   0.50 33.33  ? 500 MET A CE    1 
ATOM   3898 N  N     . ALA A 1 501 ? 13.599  23.721  2.579   1.00 46.24  ? 501 ALA A N     1 
ATOM   3899 C  CA    . ALA A 1 501 ? 12.931  24.892  3.131   1.00 48.39  ? 501 ALA A CA    1 
ATOM   3900 C  C     . ALA A 1 501 ? 12.657  25.953  2.074   1.00 54.06  ? 501 ALA A C     1 
ATOM   3901 O  O     . ALA A 1 501 ? 11.964  26.932  2.369   1.00 60.62  ? 501 ALA A O     1 
ATOM   3902 C  CB    . ALA A 1 501 ? 13.765  25.492  4.265   1.00 45.51  ? 501 ALA A CB    1 
ATOM   3903 N  N     . HIS A 1 502 ? 13.191  25.787  0.862   1.00 59.81  ? 502 HIS A N     1 
ATOM   3904 C  CA    . HIS A 1 502 ? 12.897  26.663  -0.263  1.00 66.17  ? 502 HIS A CA    1 
ATOM   3905 C  C     . HIS A 1 502 ? 11.714  26.185  -1.094  1.00 67.98  ? 502 HIS A C     1 
ATOM   3906 O  O     . HIS A 1 502 ? 11.256  26.925  -1.971  1.00 81.65  ? 502 HIS A O     1 
ATOM   3907 C  CB    . HIS A 1 502 ? 14.119  26.788  -1.183  1.00 70.64  ? 502 HIS A CB    1 
ATOM   3908 C  CG    . HIS A 1 502 ? 15.370  27.221  -0.484  1.00 71.84  ? 502 HIS A CG    1 
ATOM   3909 N  ND1   . HIS A 1 502 ? 16.622  27.060  -1.038  1.00 74.87  ? 502 HIS A ND1   1 
ATOM   3910 C  CD2   . HIS A 1 502 ? 15.565  27.815  0.717   1.00 73.34  ? 502 HIS A CD2   1 
ATOM   3911 C  CE1   . HIS A 1 502 ? 17.534  27.531  -0.207  1.00 75.94  ? 502 HIS A CE1   1 
ATOM   3912 N  NE2   . HIS A 1 502 ? 16.919  27.996  0.865   1.00 81.78  ? 502 HIS A NE2   1 
ATOM   3913 N  N     . ARG A 1 503 ? 11.219  24.975  -0.849  1.00 62.72  ? 503 ARG A N     1 
ATOM   3914 C  CA    . ARG A 1 503 ? 10.165  24.416  -1.682  1.00 76.51  ? 503 ARG A CA    1 
ATOM   3915 C  C     . ARG A 1 503 ? 8.870   25.206  -1.506  1.00 85.94  ? 503 ARG A C     1 
ATOM   3916 O  O     . ARG A 1 503 ? 8.531   25.606  -0.387  1.00 77.64  ? 503 ARG A O     1 
ATOM   3917 C  CB    . ARG A 1 503 ? 9.929   22.946  -1.337  1.00 74.57  ? 503 ARG A CB    1 
ATOM   3918 C  CG    . ARG A 1 503 ? 11.098  22.034  -1.660  1.00 66.81  ? 503 ARG A CG    1 
ATOM   3919 C  CD    . ARG A 1 503 ? 10.712  21.003  -2.708  1.00 78.84  ? 503 ARG A CD    1 
ATOM   3920 N  NE    . ARG A 1 503 ? 11.841  20.166  -3.091  1.00 86.86  ? 503 ARG A NE    1 
ATOM   3921 C  CZ    . ARG A 1 503 ? 11.775  19.176  -3.971  1.00 85.01  ? 503 ARG A CZ    1 
ATOM   3922 N  NH1   . ARG A 1 503 ? 10.640  18.866  -4.578  1.00 92.12  ? 503 ARG A NH1   1 
ATOM   3923 N  NH2   . ARG A 1 503 ? 12.874  18.480  -4.249  1.00 80.01  ? 503 ARG A NH2   1 
ATOM   3924 N  N     . PRO A 1 504 ? 8.131   25.450  -2.589  1.00 97.85  ? 504 PRO A N     1 
ATOM   3925 C  CA    . PRO A 1 504 ? 6.864   26.185  -2.471  1.00 100.99 ? 504 PRO A CA    1 
ATOM   3926 C  C     . PRO A 1 504 ? 5.818   25.358  -1.737  1.00 98.83  ? 504 PRO A C     1 
ATOM   3927 O  O     . PRO A 1 504 ? 5.604   24.184  -2.050  1.00 95.61  ? 504 PRO A O     1 
ATOM   3928 C  CB    . PRO A 1 504 ? 6.459   26.440  -3.930  1.00 97.05  ? 504 PRO A CB    1 
ATOM   3929 C  CG    . PRO A 1 504 ? 7.706   26.205  -4.735  1.00 99.50  ? 504 PRO A CG    1 
ATOM   3930 C  CD    . PRO A 1 504 ? 8.471   25.159  -3.990  1.00 98.09  ? 504 PRO A CD    1 
ATOM   3931 N  N     . ALA A 1 505 ? 5.172   25.984  -0.750  1.00 79.22  ? 505 ALA A N     1 
ATOM   3932 C  CA    . ALA A 1 505 ? 4.102   25.360  0.031   1.00 75.93  ? 505 ALA A CA    1 
ATOM   3933 C  C     . ALA A 1 505 ? 4.573   24.092  0.738   1.00 67.56  ? 505 ALA A C     1 
ATOM   3934 O  O     . ALA A 1 505 ? 3.776   23.193  1.018   1.00 64.53  ? 505 ALA A O     1 
ATOM   3935 C  CB    . ALA A 1 505 ? 2.876   25.064  -0.838  1.00 71.16  ? 505 ALA A CB    1 
ATOM   3936 N  N     . ALA A 1 506 ? 5.867   24.008  1.035   1.00 66.34  ? 506 ALA A N     1 
ATOM   3937 C  CA    . ALA A 1 506 ? 6.396   22.849  1.741   1.00 62.56  ? 506 ALA A CA    1 
ATOM   3938 C  C     . ALA A 1 506 ? 5.940   22.866  3.194   1.00 49.57  ? 506 ALA A C     1 
ATOM   3939 O  O     . ALA A 1 506 ? 6.096   23.871  3.895   1.00 52.82  ? 506 ALA A O     1 
ATOM   3940 C  CB    . ALA A 1 506 ? 7.921   22.826  1.665   1.00 58.04  ? 506 ALA A CB    1 
ATOM   3941 N  N     . LYS A 1 507 ? 5.363   21.753  3.640   1.00 45.18  ? 507 LYS A N     1 
ATOM   3942 C  CA    . LYS A 1 507 ? 4.944   21.579  5.029   1.00 48.09  ? 507 LYS A CA    1 
ATOM   3943 C  C     . LYS A 1 507 ? 6.075   20.846  5.741   1.00 42.93  ? 507 LYS A C     1 
ATOM   3944 O  O     . LYS A 1 507 ? 6.084   19.619  5.837   1.00 43.08  ? 507 LYS A O     1 
ATOM   3945 C  CB    . LYS A 1 507 ? 3.623   20.823  5.110   1.00 48.43  ? 507 LYS A CB    1 
ATOM   3946 C  CG    . LYS A 1 507 ? 2.487   21.498  4.361   1.00 58.55  ? 507 LYS A CG    1 
ATOM   3947 C  CD    . LYS A 1 507 ? 1.259   20.609  4.302   1.00 57.18  ? 507 LYS A CD    1 
ATOM   3948 C  CE    . LYS A 1 507 ? 0.182   21.214  3.418   1.00 63.00  ? 507 LYS A CE    1 
ATOM   3949 N  NZ    . LYS A 1 507 ? -0.993  20.307  3.298   1.00 70.46  ? 507 LYS A NZ    1 
ATOM   3950 N  N     . LEU A 1 508 ? 7.039   21.613  6.231   1.00 40.47  ? 508 LEU A N     1 
ATOM   3951 C  CA    . LEU A 1 508 ? 8.228   21.026  6.836   1.00 41.32  ? 508 LEU A CA    1 
ATOM   3952 C  C     . LEU A 1 508 ? 7.874   20.371  8.166   1.00 33.98  ? 508 LEU A C     1 
ATOM   3953 O  O     . LEU A 1 508 ? 7.248   21.008  9.019   1.00 39.79  ? 508 LEU A O     1 
ATOM   3954 C  CB    . LEU A 1 508 ? 9.299   22.092  7.039   1.00 33.84  ? 508 LEU A CB    1 
ATOM   3955 C  CG    . LEU A 1 508 ? 9.817   22.756  5.762   1.00 37.26  ? 508 LEU A CG    1 
ATOM   3956 C  CD1   . LEU A 1 508 ? 10.821  23.848  6.093   1.00 38.53  ? 508 LEU A CD1   1 
ATOM   3957 C  CD2   . LEU A 1 508 ? 10.430  21.720  4.832   1.00 38.77  ? 508 LEU A CD2   1 
ATOM   3958 N  N     . PRO A 1 509 ? 8.247   19.114  8.378   1.00 36.60  ? 509 PRO A N     1 
ATOM   3959 C  CA    . PRO A 1 509 ? 7.967   18.467  9.662   1.00 36.59  ? 509 PRO A CA    1 
ATOM   3960 C  C     . PRO A 1 509 ? 8.812   19.052  10.783  1.00 34.32  ? 509 PRO A C     1 
ATOM   3961 O  O     . PRO A 1 509 ? 9.814   19.734  10.560  1.00 31.43  ? 509 PRO A O     1 
ATOM   3962 C  CB    . PRO A 1 509 ? 8.330   17.000  9.406   1.00 32.87  ? 509 PRO A CB    1 
ATOM   3963 C  CG    . PRO A 1 509 ? 9.321   17.048  8.291   1.00 33.28  ? 509 PRO A CG    1 
ATOM   3964 C  CD    . PRO A 1 509 ? 8.906   18.203  7.425   1.00 32.27  ? 509 PRO A CD    1 
ATOM   3965 N  N     . LYS A 1 510 ? 8.376   18.780  12.010  1.00 34.29  ? 510 LYS A N     1 
ATOM   3966 C  CA    . LYS A 1 510 ? 9.160   19.111  13.190  1.00 36.76  ? 510 LYS A CA    1 
ATOM   3967 C  C     . LYS A 1 510 ? 10.304  18.118  13.352  1.00 31.44  ? 510 LYS A C     1 
ATOM   3968 O  O     . LYS A 1 510 ? 10.201  16.951  12.965  1.00 32.51  ? 510 LYS A O     1 
ATOM   3969 C  CB    . LYS A 1 510 ? 8.283   19.103  14.443  1.00 32.22  ? 510 LYS A CB    1 
ATOM   3970 C  CG    . LYS A 1 510 ? 7.729   20.461  14.830  1.00 41.29  ? 510 LYS A CG    1 
ATOM   3971 C  CD    . LYS A 1 510 ? 6.717   20.336  15.956  1.00 40.06  ? 510 LYS A CD    1 
ATOM   3972 C  CE    . LYS A 1 510 ? 6.544   21.651  16.696  1.00 44.39  ? 510 LYS A CE    1 
ATOM   3973 N  NZ    . LYS A 1 510 ? 6.492   22.809  15.774  1.00 44.23  ? 510 LYS A NZ    1 
ATOM   3974 N  N     . ILE A 1 511 ? 11.403  18.589  13.933  1.00 30.63  ? 511 ILE A N     1 
ATOM   3975 C  CA    . ILE A 1 511 ? 12.605  17.783  14.108  1.00 28.65  ? 511 ILE A CA    1 
ATOM   3976 C  C     . ILE A 1 511 ? 12.899  17.661  15.596  1.00 31.09  ? 511 ILE A C     1 
ATOM   3977 O  O     . ILE A 1 511 ? 12.977  18.671  16.304  1.00 31.18  ? 511 ILE A O     1 
ATOM   3978 C  CB    . ILE A 1 511 ? 13.803  18.383  13.350  1.00 31.65  ? 511 ILE A CB    1 
ATOM   3979 C  CG1   . ILE A 1 511 ? 13.621  18.180  11.845  1.00 30.35  ? 511 ILE A CG1   1 
ATOM   3980 C  CG2   . ILE A 1 511 ? 15.110  17.761  13.826  1.00 26.61  ? 511 ILE A CG2   1 
ATOM   3981 C  CD1   . ILE A 1 511 ? 14.617  18.940  10.993  1.00 32.15  ? 511 ILE A CD1   1 
ATOM   3982 N  N     . PHE A 1 512 ? 13.051  16.425  16.065  1.00 26.70  ? 512 PHE A N     1 
ATOM   3983 C  CA    . PHE A 1 512 ? 13.345  16.124  17.456  1.00 30.63  ? 512 PHE A CA    1 
ATOM   3984 C  C     . PHE A 1 512 ? 14.641  15.331  17.548  1.00 28.35  ? 512 PHE A C     1 
ATOM   3985 O  O     . PHE A 1 512 ? 15.062  14.677  16.590  1.00 26.03  ? 512 PHE A O     1 
ATOM   3986 C  CB    . PHE A 1 512 ? 12.211  15.318  18.112  1.00 29.17  ? 512 PHE A CB    1 
ATOM   3987 C  CG    . PHE A 1 512 ? 10.870  15.994  18.062  1.00 29.16  ? 512 PHE A CG    1 
ATOM   3988 C  CD1   . PHE A 1 512 ? 10.493  16.887  19.052  1.00 31.05  ? 512 PHE A CD1   1 
ATOM   3989 C  CD2   . PHE A 1 512 ? 9.982   15.726  17.030  1.00 29.86  ? 512 PHE A CD2   1 
ATOM   3990 C  CE1   . PHE A 1 512 ? 9.257   17.510  19.010  1.00 34.28  ? 512 PHE A CE1   1 
ATOM   3991 C  CE2   . PHE A 1 512 ? 8.746   16.345  16.982  1.00 30.84  ? 512 PHE A CE2   1 
ATOM   3992 C  CZ    . PHE A 1 512 ? 8.382   17.239  17.974  1.00 29.89  ? 512 PHE A CZ    1 
ATOM   3993 N  N     . HIS A 1 513 ? 15.269  15.390  18.721  1.00 31.01  ? 513 HIS A N     1 
ATOM   3994 C  CA    . HIS A 1 513 ? 16.431  14.568  19.035  1.00 25.92  ? 513 HIS A CA    1 
ATOM   3995 C  C     . HIS A 1 513 ? 16.184  13.864  20.360  1.00 27.39  ? 513 HIS A C     1 
ATOM   3996 O  O     . HIS A 1 513 ? 15.783  14.504  21.337  1.00 28.82  ? 513 HIS A O     1 
ATOM   3997 C  CB    . HIS A 1 513 ? 17.713  15.405  19.108  1.00 29.52  ? 513 HIS A CB    1 
ATOM   3998 C  CG    . HIS A 1 513 ? 18.957  14.588  19.274  1.00 26.91  ? 513 HIS A CG    1 
ATOM   3999 N  ND1   . HIS A 1 513 ? 19.408  14.157  20.503  1.00 28.63  ? 513 HIS A ND1   1 
ATOM   4000 C  CD2   . HIS A 1 513 ? 19.841  14.117  18.363  1.00 26.35  ? 513 HIS A CD2   1 
ATOM   4001 C  CE1   . HIS A 1 513 ? 20.516  13.456  20.343  1.00 27.32  ? 513 HIS A CE1   1 
ATOM   4002 N  NE2   . HIS A 1 513 ? 20.800  13.417  19.054  1.00 32.93  ? 513 HIS A NE2   1 
ATOM   4003 N  N     . VAL A 1 514 ? 16.417  12.550  20.394  1.00 28.49  ? 514 VAL A N     1 
ATOM   4004 C  CA    . VAL A 1 514 ? 16.169  11.757  21.589  1.00 30.92  ? 514 VAL A CA    1 
ATOM   4005 C  C     . VAL A 1 514 ? 17.447  11.042  22.001  1.00 28.97  ? 514 VAL A C     1 
ATOM   4006 O  O     . VAL A 1 514 ? 18.407  10.924  21.237  1.00 31.82  ? 514 VAL A O     1 
ATOM   4007 C  CB    . VAL A 1 514 ? 15.031  10.731  21.402  1.00 29.20  ? 514 VAL A CB    1 
ATOM   4008 C  CG1   . VAL A 1 514 ? 13.798  11.410  20.874  1.00 24.43  ? 514 VAL A CG1   1 
ATOM   4009 C  CG2   . VAL A 1 514 ? 15.468  9.599   20.485  1.00 30.08  ? 514 VAL A CG2   1 
ATOM   4010 N  N     . ASN A 1 515 ? 17.435  10.555  23.241  1.00 29.21  ? 515 ASN A N     1 
ATOM   4011 C  CA    . ASN A 1 515 ? 18.532  9.758   23.784  1.00 35.48  ? 515 ASN A CA    1 
ATOM   4012 C  C     . ASN A 1 515 ? 17.916  8.785   24.786  1.00 37.71  ? 515 ASN A C     1 
ATOM   4013 O  O     . ASN A 1 515 ? 17.567  9.184   25.901  1.00 36.39  ? 515 ASN A O     1 
ATOM   4014 C  CB    . ASN A 1 515 ? 19.586  10.645  24.433  1.00 32.79  ? 515 ASN A CB    1 
ATOM   4015 C  CG    . ASN A 1 515 ? 20.734  9.850   25.029  1.00 37.97  ? 515 ASN A CG    1 
ATOM   4016 O  OD1   . ASN A 1 515 ? 21.027  8.738   24.589  1.00 36.07  ? 515 ASN A OD1   1 
ATOM   4017 N  ND2   . ASN A 1 515 ? 21.391  10.419  26.034  1.00 35.14  ? 515 ASN A ND2   1 
ATOM   4018 N  N     . TRP A 1 516 ? 17.766  7.522   24.379  1.00 31.92  ? 516 TRP A N     1 
ATOM   4019 C  CA    . TRP A 1 516 ? 17.286  6.495   25.294  1.00 38.01  ? 516 TRP A CA    1 
ATOM   4020 C  C     . TRP A 1 516 ? 18.387  5.939   26.186  1.00 37.82  ? 516 TRP A C     1 
ATOM   4021 O  O     . TRP A 1 516 ? 18.090  5.114   27.054  1.00 39.67  ? 516 TRP A O     1 
ATOM   4022 C  CB    . TRP A 1 516 ? 16.663  5.305   24.546  1.00 31.85  ? 516 TRP A CB    1 
ATOM   4023 C  CG    . TRP A 1 516 ? 15.719  5.591   23.407  1.00 36.21  ? 516 TRP A CG    1 
ATOM   4024 C  CD1   . TRP A 1 516 ? 15.682  4.939   22.208  1.00 36.59  ? 516 TRP A CD1   1 
ATOM   4025 C  CD2   . TRP A 1 516 ? 14.665  6.565   23.363  1.00 33.76  ? 516 TRP A CD2   1 
ATOM   4026 N  NE1   . TRP A 1 516 ? 14.685  5.451   21.417  1.00 37.82  ? 516 TRP A NE1   1 
ATOM   4027 C  CE2   . TRP A 1 516 ? 14.044  6.449   22.101  1.00 34.73  ? 516 TRP A CE2   1 
ATOM   4028 C  CE3   . TRP A 1 516 ? 14.188  7.523   24.262  1.00 36.88  ? 516 TRP A CE3   1 
ATOM   4029 C  CZ2   . TRP A 1 516 ? 12.974  7.254   21.718  1.00 30.68  ? 516 TRP A CZ2   1 
ATOM   4030 C  CZ3   . TRP A 1 516 ? 13.128  8.324   23.878  1.00 39.79  ? 516 TRP A CZ3   1 
ATOM   4031 C  CH2   . TRP A 1 516 ? 12.534  8.185   22.617  1.00 31.84  ? 516 TRP A CH2   1 
ATOM   4032 N  N     . PHE A 1 517 ? 19.639  6.357   25.996  1.00 37.18  ? 517 PHE A N     1 
ATOM   4033 C  CA    . PHE A 1 517 ? 20.783  5.596   26.484  1.00 43.75  ? 517 PHE A CA    1 
ATOM   4034 C  C     . PHE A 1 517 ? 21.615  6.355   27.512  1.00 40.19  ? 517 PHE A C     1 
ATOM   4035 O  O     . PHE A 1 517 ? 22.750  5.958   27.796  1.00 48.10  ? 517 PHE A O     1 
ATOM   4036 C  CB    . PHE A 1 517 ? 21.652  5.163   25.301  1.00 41.49  ? 517 PHE A CB    1 
ATOM   4037 C  CG    . PHE A 1 517 ? 20.909  4.356   24.272  1.00 38.85  ? 517 PHE A CG    1 
ATOM   4038 C  CD1   . PHE A 1 517 ? 20.758  2.986   24.426  1.00 43.70  ? 517 PHE A CD1   1 
ATOM   4039 C  CD2   . PHE A 1 517 ? 20.348  4.968   23.160  1.00 38.14  ? 517 PHE A CD2   1 
ATOM   4040 C  CE1   . PHE A 1 517 ? 20.070  2.239   23.487  1.00 41.08  ? 517 PHE A CE1   1 
ATOM   4041 C  CE2   . PHE A 1 517 ? 19.658  4.227   22.217  1.00 37.91  ? 517 PHE A CE2   1 
ATOM   4042 C  CZ    . PHE A 1 517 ? 19.519  2.861   22.381  1.00 39.51  ? 517 PHE A CZ    1 
ATOM   4043 N  N     . ARG A 1 518 ? 21.078  7.428   28.087  1.00 40.70  ? 518 ARG A N     1 
ATOM   4044 C  CA    . ARG A 1 518 ? 21.811  8.171   29.102  1.00 45.90  ? 518 ARG A CA    1 
ATOM   4045 C  C     . ARG A 1 518 ? 21.889  7.363   30.392  1.00 54.68  ? 518 ARG A C     1 
ATOM   4046 O  O     . ARG A 1 518 ? 20.940  6.668   30.765  1.00 56.80  ? 518 ARG A O     1 
ATOM   4047 C  CB    . ARG A 1 518 ? 21.146  9.524   29.358  1.00 52.15  ? 518 ARG A CB    1 
ATOM   4048 C  CG    . ARG A 1 518 ? 21.992  10.489  30.177  1.00 53.49  ? 518 ARG A CG    1 
ATOM   4049 C  CD    . ARG A 1 518 ? 21.373  11.877  30.218  1.00 52.89  ? 518 ARG A CD    1 
ATOM   4050 N  NE    . ARG A 1 518 ? 22.209  12.818  30.953  1.00 49.77  ? 518 ARG A NE    1 
ATOM   4051 C  CZ    . ARG A 1 518 ? 22.029  14.132  30.964  1.00 52.18  ? 518 ARG A CZ    1 
ATOM   4052 N  NH1   . ARG A 1 518 ? 21.045  14.702  30.287  1.00 50.92  ? 518 ARG A NH1   1 
ATOM   4053 N  NH2   . ARG A 1 518 ? 22.861  14.895  31.669  1.00 54.49  ? 518 ARG A NH2   1 
ATOM   4054 N  N     . LYS A 1 519 ? 23.029  7.453   31.072  1.00 56.31  ? 519 LYS A N     1 
ATOM   4055 C  CA    . LYS A 1 519 ? 23.290  6.663   32.265  1.00 67.63  ? 519 LYS A CA    1 
ATOM   4056 C  C     . LYS A 1 519 ? 23.616  7.567   33.448  1.00 69.71  ? 519 LYS A C     1 
ATOM   4057 O  O     . LYS A 1 519 ? 23.961  8.741   33.289  1.00 74.75  ? 519 LYS A O     1 
ATOM   4058 C  CB    . LYS A 1 519 ? 24.439  5.673   32.034  1.00 67.85  ? 519 LYS A CB    1 
ATOM   4059 C  CG    . LYS A 1 519 ? 24.166  4.659   30.935  1.00 64.21  ? 519 LYS A CG    1 
ATOM   4060 C  CD    . LYS A 1 519 ? 25.317  3.680   30.784  1.00 66.07  ? 519 LYS A CD    1 
ATOM   4061 C  CE    . LYS A 1 519 ? 25.020  2.648   29.709  1.00 71.06  ? 519 LYS A CE    1 
ATOM   4062 N  NZ    . LYS A 1 519 ? 26.120  1.655   29.571  1.00 75.04  ? 519 LYS A NZ    1 
ATOM   4063 N  N     . ASP A 1 520 ? 23.502  6.997   34.645  1.00 79.42  ? 520 ASP A N     1 
ATOM   4064 C  CA    . ASP A 1 520 ? 23.775  7.717   35.879  1.00 88.84  ? 520 ASP A CA    1 
ATOM   4065 C  C     . ASP A 1 520 ? 25.235  7.516   36.284  1.00 94.23  ? 520 ASP A C     1 
ATOM   4066 O  O     . ASP A 1 520 ? 26.050  6.988   35.523  1.00 93.81  ? 520 ASP A O     1 
ATOM   4067 C  CB    . ASP A 1 520 ? 22.811  7.268   36.978  1.00 89.57  ? 520 ASP A CB    1 
ATOM   4068 C  CG    . ASP A 1 520 ? 22.872  5.771   37.244  1.00 86.53  ? 520 ASP A CG    1 
ATOM   4069 O  OD1   . ASP A 1 520 ? 23.663  5.066   36.582  1.00 85.78  ? 520 ASP A OD1   1 
ATOM   4070 O  OD2   . ASP A 1 520 ? 22.122  5.296   38.121  1.00 93.48  ? 520 ASP A OD2   1 
ATOM   4071 N  N     . LYS A 1 521 ? 25.579  7.939   37.503  1.00 96.12  ? 521 LYS A N     1 
ATOM   4072 C  CA    . LYS A 1 521 ? 26.939  7.746   37.996  1.00 103.27 ? 521 LYS A CA    1 
ATOM   4073 C  C     . LYS A 1 521 ? 27.254  6.271   38.211  1.00 104.85 ? 521 LYS A C     1 
ATOM   4074 O  O     . LYS A 1 521 ? 28.421  5.871   38.133  1.00 107.16 ? 521 LYS A O     1 
ATOM   4075 C  CB    . LYS A 1 521 ? 27.141  8.522   39.298  1.00 103.76 ? 521 LYS A CB    1 
ATOM   4076 C  CG    . LYS A 1 521 ? 26.761  9.992   39.221  1.00 104.25 ? 521 LYS A CG    1 
ATOM   4077 C  CD    . LYS A 1 521 ? 26.835  10.642  40.594  1.00 109.19 ? 521 LYS A CD    1 
ATOM   4078 C  CE    . LYS A 1 521 ? 26.371  12.088  40.553  1.00 109.88 ? 521 LYS A CE    1 
ATOM   4079 N  NZ    . LYS A 1 521 ? 26.360  12.701  41.911  1.00 103.02 ? 521 LYS A NZ    1 
ATOM   4080 N  N     . ASN A 1 522 ? 26.235  5.452   38.479  1.00 103.67 ? 522 ASN A N     1 
ATOM   4081 C  CA    . ASN A 1 522 ? 26.448  4.031   38.721  1.00 102.28 ? 522 ASN A CA    1 
ATOM   4082 C  C     . ASN A 1 522 ? 26.705  3.245   37.443  1.00 104.01 ? 522 ASN A C     1 
ATOM   4083 O  O     . ASN A 1 522 ? 27.300  2.163   37.508  1.00 104.22 ? 522 ASN A O     1 
ATOM   4084 C  CB    . ASN A 1 522 ? 25.243  3.437   39.453  1.00 104.08 ? 522 ASN A CB    1 
ATOM   4085 C  CG    . ASN A 1 522 ? 24.973  4.117   40.781  1.00 112.72 ? 522 ASN A CG    1 
ATOM   4086 O  OD1   . ASN A 1 522 ? 25.871  4.703   41.384  1.00 122.17 ? 522 ASN A OD1   1 
ATOM   4087 N  ND2   . ASN A 1 522 ? 23.730  4.040   41.244  1.00 105.31 ? 522 ASN A ND2   1 
ATOM   4088 N  N     . GLY A 1 523 ? 26.272  3.753   36.294  1.00 98.90  ? 523 GLY A N     1 
ATOM   4089 C  CA    . GLY A 1 523 ? 26.467  3.074   35.032  1.00 95.63  ? 523 GLY A CA    1 
ATOM   4090 C  C     . GLY A 1 523 ? 25.245  2.389   34.462  1.00 88.12  ? 523 GLY A C     1 
ATOM   4091 O  O     . GLY A 1 523 ? 25.377  1.654   33.476  1.00 85.25  ? 523 GLY A O     1 
ATOM   4092 N  N     . LYS A 1 524 ? 24.068  2.602   35.042  1.00 83.19  ? 524 LYS A N     1 
ATOM   4093 C  CA    . LYS A 1 524 ? 22.834  2.001   34.563  1.00 79.89  ? 524 LYS A CA    1 
ATOM   4094 C  C     . LYS A 1 524 ? 21.961  3.054   33.892  1.00 67.60  ? 524 LYS A C     1 
ATOM   4095 O  O     . LYS A 1 524 ? 22.092  4.255   34.142  1.00 70.81  ? 524 LYS A O     1 
ATOM   4096 C  CB    . LYS A 1 524 ? 22.068  1.331   35.708  1.00 81.80  ? 524 LYS A CB    1 
ATOM   4097 C  CG    . LYS A 1 524 ? 21.689  2.267   36.844  1.00 81.98  ? 524 LYS A CG    1 
ATOM   4098 C  CD    . LYS A 1 524 ? 21.034  1.500   37.982  1.00 92.15  ? 524 LYS A CD    1 
ATOM   4099 C  CE    . LYS A 1 524 ? 20.680  2.417   39.141  1.00 89.76  ? 524 LYS A CE    1 
ATOM   4100 N  NZ    . LYS A 1 524 ? 20.072  1.659   40.271  1.00 91.37  ? 524 LYS A NZ    1 
ATOM   4101 N  N     . PHE A 1 525 ? 21.058  2.582   33.034  1.00 69.41  ? 525 PHE A N     1 
ATOM   4102 C  CA    . PHE A 1 525 ? 20.223  3.483   32.250  1.00 57.14  ? 525 PHE A CA    1 
ATOM   4103 C  C     . PHE A 1 525 ? 19.252  4.247   33.141  1.00 56.36  ? 525 PHE A C     1 
ATOM   4104 O  O     . PHE A 1 525 ? 18.679  3.697   34.085  1.00 68.09  ? 525 PHE A O     1 
ATOM   4105 C  CB    . PHE A 1 525 ? 19.447  2.704   31.189  1.00 58.72  ? 525 PHE A CB    1 
ATOM   4106 C  CG    . PHE A 1 525 ? 20.317  2.053   30.155  1.00 57.71  ? 525 PHE A CG    1 
ATOM   4107 C  CD1   . PHE A 1 525 ? 20.810  2.782   29.088  1.00 52.03  ? 525 PHE A CD1   1 
ATOM   4108 C  CD2   . PHE A 1 525 ? 20.638  0.709   30.247  1.00 59.82  ? 525 PHE A CD2   1 
ATOM   4109 C  CE1   . PHE A 1 525 ? 21.610  2.186   28.132  1.00 55.67  ? 525 PHE A CE1   1 
ATOM   4110 C  CE2   . PHE A 1 525 ? 21.437  0.107   29.294  1.00 64.53  ? 525 PHE A CE2   1 
ATOM   4111 C  CZ    . PHE A 1 525 ? 21.923  0.848   28.234  1.00 59.38  ? 525 PHE A CZ    1 
ATOM   4112 N  N     . LEU A 1 526 ? 19.070  5.530   32.828  1.00 54.92  ? 526 LEU A N     1 
ATOM   4113 C  CA    . LEU A 1 526 ? 18.124  6.369   33.551  1.00 58.61  ? 526 LEU A CA    1 
ATOM   4114 C  C     . LEU A 1 526 ? 16.701  6.245   33.023  1.00 61.60  ? 526 LEU A C     1 
ATOM   4115 O  O     . LEU A 1 526 ? 15.757  6.596   33.738  1.00 64.32  ? 526 LEU A O     1 
ATOM   4116 C  CB    . LEU A 1 526 ? 18.568  7.832   33.482  1.00 52.84  ? 526 LEU A CB    1 
ATOM   4117 C  CG    . LEU A 1 526 ? 19.826  8.229   34.253  1.00 68.21  ? 526 LEU A CG    1 
ATOM   4118 C  CD1   . LEU A 1 526 ? 20.322  9.590   33.792  1.00 72.49  ? 526 LEU A CD1   1 
ATOM   4119 C  CD2   . LEU A 1 526 ? 19.546  8.241   35.745  1.00 70.99  ? 526 LEU A CD2   1 
ATOM   4120 N  N     . TRP A 1 527 ? 16.527  5.756   31.797  1.00 50.60  ? 527 TRP A N     1 
ATOM   4121 C  CA    . TRP A 1 527 ? 15.229  5.671   31.152  1.00 51.44  ? 527 TRP A CA    1 
ATOM   4122 C  C     . TRP A 1 527 ? 14.900  4.218   30.837  1.00 51.86  ? 527 TRP A C     1 
ATOM   4123 O  O     . TRP A 1 527 ? 15.748  3.503   30.282  1.00 52.75  ? 527 TRP A O     1 
ATOM   4124 C  CB    . TRP A 1 527 ? 15.219  6.509   29.860  1.00 48.19  ? 527 TRP A CB    1 
ATOM   4125 C  CG    . TRP A 1 527 ? 13.891  6.585   29.167  1.00 47.30  ? 527 TRP A CG    1 
ATOM   4126 C  CD1   . TRP A 1 527 ? 13.577  6.081   27.937  1.00 46.23  ? 527 TRP A CD1   1 
ATOM   4127 C  CD2   . TRP A 1 527 ? 12.699  7.214   29.658  1.00 46.28  ? 527 TRP A CD2   1 
ATOM   4128 N  NE1   . TRP A 1 527 ? 12.266  6.353   27.634  1.00 46.18  ? 527 TRP A NE1   1 
ATOM   4129 C  CE2   . TRP A 1 527 ? 11.704  7.047   28.673  1.00 44.86  ? 527 TRP A CE2   1 
ATOM   4130 C  CE3   . TRP A 1 527 ? 12.377  7.901   30.833  1.00 49.38  ? 527 TRP A CE3   1 
ATOM   4131 C  CZ2   . TRP A 1 527 ? 10.410  7.541   28.828  1.00 41.97  ? 527 TRP A CZ2   1 
ATOM   4132 C  CZ3   . TRP A 1 527 ? 11.090  8.390   30.986  1.00 49.51  ? 527 TRP A CZ3   1 
ATOM   4133 C  CH2   . TRP A 1 527 ? 10.123  8.207   29.988  1.00 46.75  ? 527 TRP A CH2   1 
ATOM   4134 N  N     . PRO A 1 528 ? 13.700  3.738   31.179  1.00 54.23  ? 528 PRO A N     1 
ATOM   4135 C  CA    . PRO A 1 528 ? 13.365  2.334   30.881  1.00 54.22  ? 528 PRO A CA    1 
ATOM   4136 C  C     . PRO A 1 528 ? 13.252  2.038   29.394  1.00 51.58  ? 528 PRO A C     1 
ATOM   4137 O  O     . PRO A 1 528 ? 13.551  0.912   28.977  1.00 45.67  ? 528 PRO A O     1 
ATOM   4138 C  CB    . PRO A 1 528 ? 12.027  2.128   31.608  1.00 49.39  ? 528 PRO A CB    1 
ATOM   4139 C  CG    . PRO A 1 528 ? 11.474  3.506   31.801  1.00 57.27  ? 528 PRO A CG    1 
ATOM   4140 C  CD    . PRO A 1 528 ? 12.657  4.405   31.977  1.00 51.12  ? 528 PRO A CD    1 
ATOM   4141 N  N     . GLY A 1 529 ? 12.828  3.004   28.582  1.00 46.47  ? 529 GLY A N     1 
ATOM   4142 C  CA    . GLY A 1 529 ? 12.813  2.806   27.147  1.00 45.35  ? 529 GLY A CA    1 
ATOM   4143 C  C     . GLY A 1 529 ? 11.785  1.787   26.673  1.00 43.35  ? 529 GLY A C     1 
ATOM   4144 O  O     . GLY A 1 529 ? 10.853  1.404   27.387  1.00 43.38  ? 529 GLY A O     1 
ATOM   4145 N  N     . PHE A 1 530 ? 11.984  1.347   25.429  1.00 41.78  ? 530 PHE A N     1 
ATOM   4146 C  CA    . PHE A 1 530 ? 11.102  0.402   24.753  1.00 42.91  ? 530 PHE A CA    1 
ATOM   4147 C  C     . PHE A 1 530 ? 9.655   0.884   24.781  1.00 45.58  ? 530 PHE A C     1 
ATOM   4148 O  O     . PHE A 1 530 ? 9.329   1.912   24.176  1.00 44.80  ? 530 PHE A O     1 
ATOM   4149 C  CB    . PHE A 1 530 ? 11.232  -0.990  25.376  1.00 43.14  ? 530 PHE A CB    1 
ATOM   4150 C  CG    . PHE A 1 530 ? 12.638  -1.523  25.362  1.00 42.63  ? 530 PHE A CG    1 
ATOM   4151 C  CD1   . PHE A 1 530 ? 13.220  -1.952  24.177  1.00 41.16  ? 530 PHE A CD1   1 
ATOM   4152 C  CD2   . PHE A 1 530 ? 13.381  -1.585  26.529  1.00 43.40  ? 530 PHE A CD2   1 
ATOM   4153 C  CE1   . PHE A 1 530 ? 14.515  -2.438  24.160  1.00 44.43  ? 530 PHE A CE1   1 
ATOM   4154 C  CE2   . PHE A 1 530 ? 14.677  -2.070  26.519  1.00 44.09  ? 530 PHE A CE2   1 
ATOM   4155 C  CZ    . PHE A 1 530 ? 15.244  -2.498  25.334  1.00 44.53  ? 530 PHE A CZ    1 
ATOM   4156 N  N     . GLY A 1 531 ? 8.783   0.153   25.479  1.00 42.62  ? 531 GLY A N     1 
ATOM   4157 C  CA    . GLY A 1 531 ? 7.385   0.542   25.537  1.00 45.98  ? 531 GLY A CA    1 
ATOM   4158 C  C     . GLY A 1 531 ? 7.161   1.896   26.180  1.00 44.96  ? 531 GLY A C     1 
ATOM   4159 O  O     . GLY A 1 531 ? 6.221   2.610   25.821  1.00 43.44  ? 531 GLY A O     1 
ATOM   4160 N  N     . GLU A 1 532 ? 8.022   2.275   27.128  1.00 45.95  ? 532 GLU A N     1 
ATOM   4161 C  CA    . GLU A 1 532 ? 7.861   3.558   27.803  1.00 42.78  ? 532 GLU A CA    1 
ATOM   4162 C  C     . GLU A 1 532 ? 8.218   4.738   26.911  1.00 42.68  ? 532 GLU A C     1 
ATOM   4163 O  O     . GLU A 1 532 ? 7.864   5.874   27.243  1.00 42.01  ? 532 GLU A O     1 
ATOM   4164 C  CB    . GLU A 1 532 ? 8.704   3.597   29.080  1.00 47.27  ? 532 GLU A CB    1 
ATOM   4165 C  CG    . GLU A 1 532 ? 8.365   2.505   30.084  1.00 48.01  ? 532 GLU A CG    1 
ATOM   4166 C  CD    . GLU A 1 532 ? 6.899   2.501   30.493  1.00 48.13  ? 532 GLU A CD    1 
ATOM   4167 O  OE1   . GLU A 1 532 ? 6.262   3.574   30.493  1.00 51.01  ? 532 GLU A OE1   1 
ATOM   4168 O  OE2   . GLU A 1 532 ? 6.378   1.416   30.813  1.00 55.20  ? 532 GLU A OE2   1 
ATOM   4169 N  N     . ASN A 1 533 ? 8.903   4.501   25.788  1.00 40.07  ? 533 ASN A N     1 
ATOM   4170 C  CA    . ASN A 1 533 ? 9.176   5.575   24.842  1.00 38.66  ? 533 ASN A CA    1 
ATOM   4171 C  C     . ASN A 1 533 ? 7.904   6.179   24.263  1.00 40.51  ? 533 ASN A C     1 
ATOM   4172 O  O     . ASN A 1 533 ? 7.970   7.253   23.655  1.00 35.66  ? 533 ASN A O     1 
ATOM   4173 C  CB    . ASN A 1 533 ? 10.073  5.069   23.709  1.00 35.14  ? 533 ASN A CB    1 
ATOM   4174 C  CG    . ASN A 1 533 ? 11.450  4.667   24.193  1.00 40.49  ? 533 ASN A CG    1 
ATOM   4175 O  OD1   . ASN A 1 533 ? 11.934  5.175   25.205  1.00 42.67  ? 533 ASN A OD1   1 
ATOM   4176 N  ND2   . ASN A 1 533 ? 12.093  3.753   23.472  1.00 37.06  ? 533 ASN A ND2   1 
ATOM   4177 N  N     . SER A 1 534 ? 6.755   5.519   24.436  1.00 41.47  ? 534 SER A N     1 
ATOM   4178 C  CA    . SER A 1 534 ? 5.489   6.111   24.022  1.00 47.30  ? 534 SER A CA    1 
ATOM   4179 C  C     . SER A 1 534 ? 5.210   7.410   24.765  1.00 40.46  ? 534 SER A C     1 
ATOM   4180 O  O     . SER A 1 534 ? 4.536   8.297   24.230  1.00 41.62  ? 534 SER A O     1 
ATOM   4181 C  CB    . SER A 1 534 ? 4.349   5.117   24.243  1.00 41.88  ? 534 SER A CB    1 
ATOM   4182 O  OG    . SER A 1 534 ? 4.274   4.729   25.603  1.00 42.53  ? 534 SER A OG    1 
ATOM   4183 N  N     . ARG A 1 535 ? 5.716   7.540   25.995  1.00 41.10  ? 535 ARG A N     1 
ATOM   4184 C  CA    . ARG A 1 535 ? 5.544   8.782   26.742  1.00 38.45  ? 535 ARG A CA    1 
ATOM   4185 C  C     . ARG A 1 535 ? 6.265   9.941   26.065  1.00 43.01  ? 535 ARG A C     1 
ATOM   4186 O  O     . ARG A 1 535 ? 5.780   11.079  26.094  1.00 35.64  ? 535 ARG A O     1 
ATOM   4187 C  CB    . ARG A 1 535 ? 6.048   8.605   28.175  1.00 44.58  ? 535 ARG A CB    1 
ATOM   4188 C  CG    . ARG A 1 535 ? 5.407   7.446   28.922  1.00 46.01  ? 535 ARG A CG    1 
ATOM   4189 C  CD    . ARG A 1 535 ? 6.159   7.139   30.206  1.00 50.54  ? 535 ARG A CD    1 
ATOM   4190 N  NE    . ARG A 1 535 ? 5.671   5.927   30.852  1.00 51.65  ? 535 ARG A NE    1 
ATOM   4191 C  CZ    . ARG A 1 535 ? 4.661   5.888   31.711  1.00 54.55  ? 535 ARG A CZ    1 
ATOM   4192 N  NH1   . ARG A 1 535 ? 3.997   6.981   32.048  1.00 57.76  ? 535 ARG A NH1   1 
ATOM   4193 N  NH2   . ARG A 1 535 ? 4.311   4.722   32.247  1.00 52.16  ? 535 ARG A NH2   1 
ATOM   4194 N  N     . VAL A 1 536 ? 7.419   9.673   25.454  1.00 39.70  ? 536 VAL A N     1 
ATOM   4195 C  CA    . VAL A 1 536 ? 8.120   10.717  24.716  1.00 35.52  ? 536 VAL A CA    1 
ATOM   4196 C  C     . VAL A 1 536 ? 7.393   11.024  23.414  1.00 35.56  ? 536 VAL A C     1 
ATOM   4197 O  O     . VAL A 1 536 ? 7.236   12.190  23.034  1.00 38.73  ? 536 VAL A O     1 
ATOM   4198 C  CB    . VAL A 1 536 ? 9.583   10.307  24.473  1.00 37.66  ? 536 VAL A CB    1 
ATOM   4199 C  CG1   . VAL A 1 536 ? 10.312  11.382  23.689  1.00 37.40  ? 536 VAL A CG1   1 
ATOM   4200 C  CG2   . VAL A 1 536 ? 10.289  10.040  25.797  1.00 40.33  ? 536 VAL A CG2   1 
ATOM   4201 N  N     . LEU A 1 537 ? 6.931   9.986   22.712  1.00 40.12  ? 537 LEU A N     1 
ATOM   4202 C  CA    . LEU A 1 537 ? 6.184   10.206  21.478  1.00 38.46  ? 537 LEU A CA    1 
ATOM   4203 C  C     . LEU A 1 537 ? 4.899   10.985  21.729  1.00 38.85  ? 537 LEU A C     1 
ATOM   4204 O  O     . LEU A 1 537 ? 4.478   11.774  20.876  1.00 39.24  ? 537 LEU A O     1 
ATOM   4205 C  CB    . LEU A 1 537 ? 5.874   8.871   20.802  1.00 38.07  ? 537 LEU A CB    1 
ATOM   4206 C  CG    . LEU A 1 537 ? 6.831   8.440   19.686  1.00 41.24  ? 537 LEU A CG    1 
ATOM   4207 C  CD1   . LEU A 1 537 ? 8.265   8.373   20.183  1.00 45.38  ? 537 LEU A CD1   1 
ATOM   4208 C  CD2   . LEU A 1 537 ? 6.400   7.105   19.105  1.00 50.67  ? 537 LEU A CD2   1 
ATOM   4209 N  N     . GLU A 1 538 ? 4.265   10.780  22.888  1.00 38.55  ? 538 GLU A N     1 
ATOM   4210 C  CA    . GLU A 1 538 ? 3.076   11.558  23.222  1.00 38.68  ? 538 GLU A CA    1 
ATOM   4211 C  C     . GLU A 1 538 ? 3.387   13.049  23.251  1.00 42.39  ? 538 GLU A C     1 
ATOM   4212 O  O     . GLU A 1 538 ? 2.615   13.864  22.730  1.00 37.50  ? 538 GLU A O     1 
ATOM   4213 C  CB    . GLU A 1 538 ? 2.504   11.106  24.566  1.00 41.66  ? 538 GLU A CB    1 
ATOM   4214 C  CG    . GLU A 1 538 ? 1.301   11.926  25.015  1.00 47.59  ? 538 GLU A CG    1 
ATOM   4215 C  CD    . GLU A 1 538 ? 0.737   11.477  26.352  1.00 55.77  ? 538 GLU A CD    1 
ATOM   4216 O  OE1   . GLU A 1 538 ? 1.510   10.983  27.199  1.00 54.07  ? 538 GLU A OE1   1 
ATOM   4217 O  OE2   . GLU A 1 538 ? -0.486  11.621  26.555  1.00 63.10  ? 538 GLU A OE2   1 
ATOM   4218 N  N     . TRP A 1 539 ? 4.522   13.423  23.845  1.00 39.98  ? 539 TRP A N     1 
ATOM   4219 C  CA    . TRP A 1 539 ? 4.902   14.830  23.893  1.00 38.67  ? 539 TRP A CA    1 
ATOM   4220 C  C     . TRP A 1 539 ? 5.151   15.384  22.495  1.00 40.91  ? 539 TRP A C     1 
ATOM   4221 O  O     . TRP A 1 539 ? 4.753   16.515  22.190  1.00 37.35  ? 539 TRP A O     1 
ATOM   4222 C  CB    . TRP A 1 539 ? 6.137   15.007  24.776  1.00 39.85  ? 539 TRP A CB    1 
ATOM   4223 C  CG    . TRP A 1 539 ? 6.561   16.434  24.931  1.00 39.82  ? 539 TRP A CG    1 
ATOM   4224 C  CD1   . TRP A 1 539 ? 6.000   17.372  25.751  1.00 40.87  ? 539 TRP A CD1   1 
ATOM   4225 C  CD2   . TRP A 1 539 ? 7.640   17.087  24.254  1.00 36.23  ? 539 TRP A CD2   1 
ATOM   4226 N  NE1   . TRP A 1 539 ? 6.661   18.568  25.622  1.00 37.31  ? 539 TRP A NE1   1 
ATOM   4227 C  CE2   . TRP A 1 539 ? 7.673   18.421  24.710  1.00 39.26  ? 539 TRP A CE2   1 
ATOM   4228 C  CE3   . TRP A 1 539 ? 8.583   16.674  23.306  1.00 35.53  ? 539 TRP A CE3   1 
ATOM   4229 C  CZ2   . TRP A 1 539 ? 8.610   19.345  24.250  1.00 41.24  ? 539 TRP A CZ2   1 
ATOM   4230 C  CZ3   . TRP A 1 539 ? 9.513   17.592  22.851  1.00 33.41  ? 539 TRP A CZ3   1 
ATOM   4231 C  CH2   . TRP A 1 539 ? 9.519   18.913  23.322  1.00 40.20  ? 539 TRP A CH2   1 
ATOM   4232 N  N     . MET A 1 540 ? 5.807   14.603  21.631  1.00 36.31  ? 540 MET A N     1 
ATOM   4233 C  CA    . MET A 1 540 ? 6.028   15.046  20.256  1.00 36.68  ? 540 MET A CA    1 
ATOM   4234 C  C     . MET A 1 540 ? 4.709   15.228  19.517  1.00 35.50  ? 540 MET A C     1 
ATOM   4235 O  O     . MET A 1 540 ? 4.551   16.178  18.741  1.00 36.30  ? 540 MET A O     1 
ATOM   4236 C  CB    . MET A 1 540 ? 6.904   14.043  19.507  1.00 33.38  ? 540 MET A CB    1 
ATOM   4237 C  CG    . MET A 1 540 ? 8.265   13.797  20.114  1.00 35.17  ? 540 MET A CG    1 
ATOM   4238 S  SD    . MET A 1 540 ? 9.105   12.495  19.193  1.00 38.88  ? 540 MET A SD    1 
ATOM   4239 C  CE    . MET A 1 540 ? 10.550  12.260  20.203  1.00 37.27  ? 540 MET A CE    1 
ATOM   4240 N  N     . PHE A 1 541 ? 3.761   14.313  19.732  1.00 36.36  ? 541 PHE A N     1 
ATOM   4241 C  CA    . PHE A 1 541 ? 2.456   14.413  19.086  1.00 38.64  ? 541 PHE A CA    1 
ATOM   4242 C  C     . PHE A 1 541 ? 1.783   15.736  19.428  1.00 39.54  ? 541 PHE A C     1 
ATOM   4243 O  O     . PHE A 1 541 ? 1.270   16.436  18.545  1.00 38.08  ? 541 PHE A O     1 
ATOM   4244 C  CB    . PHE A 1 541 ? 1.582   13.230  19.510  1.00 36.01  ? 541 PHE A CB    1 
ATOM   4245 C  CG    . PHE A 1 541 ? 0.380   13.004  18.632  1.00 40.80  ? 541 PHE A CG    1 
ATOM   4246 C  CD1   . PHE A 1 541 ? -0.743  13.810  18.744  1.00 40.66  ? 541 PHE A CD1   1 
ATOM   4247 C  CD2   . PHE A 1 541 ? 0.366   11.968  17.710  1.00 43.04  ? 541 PHE A CD2   1 
ATOM   4248 C  CE1   . PHE A 1 541 ? -1.852  13.598  17.941  1.00 44.12  ? 541 PHE A CE1   1 
ATOM   4249 C  CE2   . PHE A 1 541 ? -0.737  11.749  16.904  1.00 39.81  ? 541 PHE A CE2   1 
ATOM   4250 C  CZ    . PHE A 1 541 ? -1.849  12.565  17.020  1.00 43.90  ? 541 PHE A CZ    1 
ATOM   4251 N  N     . GLY A 1 542 ? 1.785   16.099  20.713  1.00 39.69  ? 542 GLY A N     1 
ATOM   4252 C  CA    . GLY A 1 542 ? 1.213   17.370  21.122  1.00 41.91  ? 542 GLY A CA    1 
ATOM   4253 C  C     . GLY A 1 542 ? 1.956   18.569  20.570  1.00 42.28  ? 542 GLY A C     1 
ATOM   4254 O  O     . GLY A 1 542 ? 1.338   19.587  20.248  1.00 41.06  ? 542 GLY A O     1 
ATOM   4255 N  N     . ARG A 1 543 ? 3.282   18.470  20.448  1.00 40.86  ? 543 ARG A N     1 
ATOM   4256 C  CA    . ARG A 1 543 ? 4.053   19.570  19.876  1.00 38.76  ? 543 ARG A CA    1 
ATOM   4257 C  C     . ARG A 1 543 ? 3.697   19.789  18.411  1.00 39.73  ? 543 ARG A C     1 
ATOM   4258 O  O     . ARG A 1 543 ? 3.645   20.932  17.942  1.00 41.56  ? 543 ARG A O     1 
ATOM   4259 C  CB    . ARG A 1 543 ? 5.550   19.303  20.033  1.00 36.08  ? 543 ARG A CB    1 
ATOM   4260 C  CG    . ARG A 1 543 ? 6.059   19.500  21.452  1.00 42.66  ? 543 ARG A CG    1 
ATOM   4261 C  CD    . ARG A 1 543 ? 5.830   20.932  21.910  1.00 41.14  ? 543 ARG A CD    1 
ATOM   4262 N  NE    . ARG A 1 543 ? 6.655   21.879  21.168  1.00 38.37  ? 543 ARG A NE    1 
ATOM   4263 C  CZ    . ARG A 1 543 ? 6.445   23.188  21.133  1.00 41.38  ? 543 ARG A CZ    1 
ATOM   4264 N  NH1   . ARG A 1 543 ? 5.424   23.741  21.766  1.00 45.83  ? 543 ARG A NH1   1 
ATOM   4265 N  NH2   . ARG A 1 543 ? 7.279   23.960  20.443  1.00 41.09  ? 543 ARG A NH2   1 
ATOM   4266 N  N     . ILE A 1 544 ? 3.452   18.706  17.670  1.00 39.37  ? 544 ILE A N     1 
ATOM   4267 C  CA    . ILE A 1 544 ? 3.041   18.844  16.276  1.00 40.65  ? 544 ILE A CA    1 
ATOM   4268 C  C     . ILE A 1 544 ? 1.668   19.499  16.190  1.00 40.25  ? 544 ILE A C     1 
ATOM   4269 O  O     . ILE A 1 544 ? 1.413   20.326  15.307  1.00 36.27  ? 544 ILE A O     1 
ATOM   4270 C  CB    . ILE A 1 544 ? 3.072   17.474  15.574  1.00 40.82  ? 544 ILE A CB    1 
ATOM   4271 C  CG1   . ILE A 1 544 ? 4.509   16.948  15.508  1.00 37.53  ? 544 ILE A CG1   1 
ATOM   4272 C  CG2   . ILE A 1 544 ? 2.479   17.567  14.176  1.00 39.01  ? 544 ILE A CG2   1 
ATOM   4273 C  CD1   . ILE A 1 544 ? 4.631   15.580  14.865  1.00 36.50  ? 544 ILE A CD1   1 
ATOM   4274 N  N     . GLU A 1 545 ? 0.769   19.158  17.116  1.00 41.59  ? 545 GLU A N     1 
ATOM   4275 C  CA    . GLU A 1 545 ? -0.532  19.811  17.178  1.00 39.87  ? 545 GLU A CA    1 
ATOM   4276 C  C     . GLU A 1 545 ? -0.446  21.255  17.655  1.00 42.81  ? 545 GLU A C     1 
ATOM   4277 O  O     . GLU A 1 545 ? -1.434  21.987  17.536  1.00 49.30  ? 545 GLU A O     1 
ATOM   4278 C  CB    . GLU A 1 545 ? -1.477  19.024  18.088  1.00 43.35  ? 545 GLU A CB    1 
ATOM   4279 C  CG    . GLU A 1 545 ? -1.953  17.702  17.499  1.00 39.54  ? 545 GLU A CG    1 
ATOM   4280 C  CD    . GLU A 1 545 ? -3.165  17.149  18.225  1.00 46.72  ? 545 GLU A CD    1 
ATOM   4281 O  OE1   . GLU A 1 545 ? -3.398  17.544  19.386  1.00 52.17  ? 545 GLU A OE1   1 
ATOM   4282 O  OE2   . GLU A 1 545 ? -3.894  16.329  17.632  1.00 55.53  ? 545 GLU A OE2   1 
ATOM   4283 N  N     . GLY A 1 546 ? 0.696   21.681  18.187  1.00 46.88  ? 546 GLY A N     1 
ATOM   4284 C  CA    . GLY A 1 546 ? 0.865   23.053  18.616  1.00 45.33  ? 546 GLY A CA    1 
ATOM   4285 C  C     . GLY A 1 546 ? 0.608   23.313  20.081  1.00 42.70  ? 546 GLY A C     1 
ATOM   4286 O  O     . GLY A 1 546 ? 0.291   24.451  20.444  1.00 49.03  ? 546 GLY A O     1 
ATOM   4287 N  N     . GLU A 1 547 ? 0.731   22.303  20.937  1.00 47.10  ? 547 GLU A N     1 
ATOM   4288 C  CA    . GLU A 1 547 ? 0.517   22.508  22.361  1.00 50.02  ? 547 GLU A CA    1 
ATOM   4289 C  C     . GLU A 1 547 ? 1.674   23.292  22.968  1.00 49.61  ? 547 GLU A C     1 
ATOM   4290 O  O     . GLU A 1 547 ? 2.834   23.117  22.586  1.00 45.52  ? 547 GLU A O     1 
ATOM   4291 C  CB    . GLU A 1 547 ? 0.355   21.165  23.075  1.00 48.45  ? 547 GLU A CB    1 
ATOM   4292 C  CG    . GLU A 1 547 ? -0.863  20.374  22.628  1.00 59.13  ? 547 GLU A CG    1 
ATOM   4293 C  CD    . GLU A 1 547 ? -1.088  19.127  23.460  1.00 70.87  ? 547 GLU A CD    1 
ATOM   4294 O  OE1   . GLU A 1 547 ? -0.361  18.940  24.459  1.00 74.23  ? 547 GLU A OE1   1 
ATOM   4295 O  OE2   . GLU A 1 547 ? -1.992  18.336  23.117  1.00 77.17  ? 547 GLU A OE2   1 
ATOM   4296 N  N     . ASP A 1 548 ? 1.348   24.165  23.921  1.00 57.57  ? 548 ASP A N     1 
ATOM   4297 C  CA    . ASP A 1 548 ? 2.343   25.010  24.582  1.00 58.73  ? 548 ASP A CA    1 
ATOM   4298 C  C     . ASP A 1 548 ? 2.924   24.262  25.784  1.00 55.51  ? 548 ASP A C     1 
ATOM   4299 O  O     . ASP A 1 548 ? 2.666   24.570  26.949  1.00 58.32  ? 548 ASP A O     1 
ATOM   4300 C  CB    . ASP A 1 548 ? 1.719   26.340  24.987  1.00 63.36  ? 548 ASP A CB    1 
ATOM   4301 C  CG    . ASP A 1 548 ? 2.724   27.296  25.596  1.00 67.31  ? 548 ASP A CG    1 
ATOM   4302 O  OD1   . ASP A 1 548 ? 3.637   27.741  24.869  1.00 72.40  ? 548 ASP A OD1   1 
ATOM   4303 O  OD2   . ASP A 1 548 ? 2.598   27.605  26.799  1.00 67.88  ? 548 ASP A OD2   1 
ATOM   4304 N  N     . SER A 1 549 ? 3.736   23.251  25.469  1.00 51.71  ? 549 SER A N     1 
ATOM   4305 C  CA    . SER A 1 549 ? 4.289   22.352  26.476  1.00 48.47  ? 549 SER A CA    1 
ATOM   4306 C  C     . SER A 1 549 ? 5.814   22.326  26.459  1.00 45.74  ? 549 SER A C     1 
ATOM   4307 O  O     . SER A 1 549 ? 6.420   21.415  27.034  1.00 44.33  ? 549 SER A O     1 
ATOM   4308 C  CB    . SER A 1 549 ? 3.736   20.939  26.281  1.00 43.90  ? 549 SER A CB    1 
ATOM   4309 O  OG    . SER A 1 549 ? 4.023   20.464  24.978  1.00 45.49  ? 549 SER A OG    1 
ATOM   4310 N  N     . ALA A 1 550 ? 6.448   23.306  25.822  1.00 43.00  ? 550 ALA A N     1 
ATOM   4311 C  CA    . ALA A 1 550 ? 7.892   23.324  25.658  1.00 44.77  ? 550 ALA A CA    1 
ATOM   4312 C  C     . ALA A 1 550 ? 8.514   24.495  26.409  1.00 46.13  ? 550 ALA A C     1 
ATOM   4313 O  O     . ALA A 1 550 ? 7.883   25.536  26.615  1.00 41.87  ? 550 ALA A O     1 
ATOM   4314 C  CB    . ALA A 1 550 ? 8.277   23.398  24.178  1.00 43.28  ? 550 ALA A CB    1 
ATOM   4315 N  N     . LYS A 1 551 ? 9.767   24.304  26.812  1.00 45.04  ? 551 LYS A N     1 
ATOM   4316 C  CA    . LYS A 1 551 ? 10.572  25.319  27.476  1.00 42.35  ? 551 LYS A CA    1 
ATOM   4317 C  C     . LYS A 1 551 ? 11.843  25.543  26.668  1.00 45.19  ? 551 LYS A C     1 
ATOM   4318 O  O     . LYS A 1 551 ? 12.431  24.589  26.147  1.00 41.47  ? 551 LYS A O     1 
ATOM   4319 C  CB    . LYS A 1 551 ? 10.911  24.890  28.910  1.00 43.99  ? 551 LYS A CB    1 
ATOM   4320 C  CG    . LYS A 1 551 ? 11.765  25.874  29.688  1.00 60.41  ? 551 LYS A CG    1 
ATOM   4321 C  CD    . LYS A 1 551 ? 12.082  25.340  31.080  1.00 66.59  ? 551 LYS A CD    1 
ATOM   4322 C  CE    . LYS A 1 551 ? 12.830  24.018  31.006  1.00 61.54  ? 551 LYS A CE    1 
ATOM   4323 N  NZ    . LYS A 1 551 ? 13.177  23.491  32.356  1.00 72.70  ? 551 LYS A NZ    1 
ATOM   4324 N  N     . LEU A 1 552 ? 12.263  26.802  26.558  1.00 41.08  ? 552 LEU A N     1 
ATOM   4325 C  CA    . LEU A 1 552 ? 13.404  27.167  25.725  1.00 43.40  ? 552 LEU A CA    1 
ATOM   4326 C  C     . LEU A 1 552 ? 14.710  26.988  26.490  1.00 42.36  ? 552 LEU A C     1 
ATOM   4327 O  O     . LEU A 1 552 ? 14.855  27.490  27.608  1.00 45.20  ? 552 LEU A O     1 
ATOM   4328 C  CB    . LEU A 1 552 ? 13.272  28.612  25.239  1.00 43.38  ? 552 LEU A CB    1 
ATOM   4329 C  CG    . LEU A 1 552 ? 14.353  29.096  24.272  1.00 42.60  ? 552 LEU A CG    1 
ATOM   4330 C  CD1   . LEU A 1 552 ? 14.457  28.160  23.080  1.00 48.17  ? 552 LEU A CD1   1 
ATOM   4331 C  CD2   . LEU A 1 552 ? 14.066  30.515  23.811  1.00 51.11  ? 552 LEU A CD2   1 
ATOM   4332 N  N     . THR A 1 553 ? 15.650  26.275  25.884  1.00 41.44  ? 553 THR A N     1 
ATOM   4333 C  CA    . THR A 1 553 ? 16.981  26.038  26.425  1.00 39.21  ? 553 THR A CA    1 
ATOM   4334 C  C     . THR A 1 553 ? 18.009  26.393  25.366  1.00 40.55  ? 553 THR A C     1 
ATOM   4335 O  O     . THR A 1 553 ? 17.668  26.582  24.194  1.00 39.92  ? 553 THR A O     1 
ATOM   4336 C  CB    . THR A 1 553 ? 17.153  24.570  26.860  1.00 36.73  ? 553 THR A CB    1 
ATOM   4337 O  OG1   . THR A 1 553 ? 17.304  23.736  25.705  1.00 38.99  ? 553 THR A OG1   1 
ATOM   4338 C  CG2   . THR A 1 553 ? 15.959  24.099  27.675  1.00 37.27  ? 553 THR A CG2   1 
ATOM   4339 N  N     . PRO A 1 554 ? 19.287  26.510  25.747  1.00 35.83  ? 554 PRO A N     1 
ATOM   4340 C  CA    . PRO A 1 554 ? 20.326  26.799  24.742  1.00 35.10  ? 554 PRO A CA    1 
ATOM   4341 C  C     . PRO A 1 554 ? 20.437  25.763  23.630  1.00 38.94  ? 554 PRO A C     1 
ATOM   4342 O  O     . PRO A 1 554 ? 20.946  26.092  22.552  1.00 39.34  ? 554 PRO A O     1 
ATOM   4343 C  CB    . PRO A 1 554 ? 21.610  26.854  25.579  1.00 44.64  ? 554 PRO A CB    1 
ATOM   4344 C  CG    . PRO A 1 554 ? 21.152  27.299  26.917  1.00 39.49  ? 554 PRO A CG    1 
ATOM   4345 C  CD    . PRO A 1 554 ? 19.804  26.664  27.121  1.00 37.35  ? 554 PRO A CD    1 
ATOM   4346 N  N     . ILE A 1 555 ? 19.987  24.525  23.847  1.00 33.82  ? 555 ILE A N     1 
ATOM   4347 C  CA    . ILE A 1 555 ? 20.106  23.487  22.826  1.00 35.41  ? 555 ILE A CA    1 
ATOM   4348 C  C     . ILE A 1 555 ? 18.812  23.259  22.057  1.00 35.36  ? 555 ILE A C     1 
ATOM   4349 O  O     . ILE A 1 555 ? 18.811  22.477  21.093  1.00 32.70  ? 555 ILE A O     1 
ATOM   4350 C  CB    . ILE A 1 555 ? 20.576  22.150  23.438  1.00 38.13  ? 555 ILE A CB    1 
ATOM   4351 C  CG1   . ILE A 1 555 ? 19.476  21.562  24.326  1.00 43.27  ? 555 ILE A CG1   1 
ATOM   4352 C  CG2   . ILE A 1 555 ? 21.867  22.350  24.221  1.00 35.40  ? 555 ILE A CG2   1 
ATOM   4353 C  CD1   . ILE A 1 555 ? 19.714  20.125  24.721  1.00 42.12  ? 555 ILE A CD1   1 
ATOM   4354 N  N     . GLY A 1 556 ? 17.720  23.900  22.447  1.00 35.20  ? 556 GLY A N     1 
ATOM   4355 C  CA    . GLY A 1 556 ? 16.431  23.721  21.821  1.00 38.92  ? 556 GLY A CA    1 
ATOM   4356 C  C     . GLY A 1 556 ? 15.341  23.686  22.870  1.00 37.34  ? 556 GLY A C     1 
ATOM   4357 O  O     . GLY A 1 556 ? 15.564  24.003  24.037  1.00 37.28  ? 556 GLY A O     1 
ATOM   4358 N  N     . TYR A 1 557 ? 14.144  23.291  22.445  1.00 38.36  ? 557 TYR A N     1 
ATOM   4359 C  CA    . TYR A 1 557 ? 12.999  23.195  23.341  1.00 40.16  ? 557 TYR A CA    1 
ATOM   4360 C  C     . TYR A 1 557 ? 12.982  21.844  24.041  1.00 36.40  ? 557 TYR A C     1 
ATOM   4361 O  O     . TYR A 1 557 ? 13.213  20.807  23.417  1.00 37.33  ? 557 TYR A O     1 
ATOM   4362 C  CB    . TYR A 1 557 ? 11.687  23.385  22.577  1.00 40.37  ? 557 TYR A CB    1 
ATOM   4363 C  CG    . TYR A 1 557 ? 11.512  24.744  21.946  1.00 41.17  ? 557 TYR A CG    1 
ATOM   4364 C  CD1   . TYR A 1 557 ? 11.298  25.870  22.727  1.00 44.33  ? 557 TYR A CD1   1 
ATOM   4365 C  CD2   . TYR A 1 557 ? 11.535  24.898  20.566  1.00 39.31  ? 557 TYR A CD2   1 
ATOM   4366 C  CE1   . TYR A 1 557 ? 11.128  27.116  22.153  1.00 49.26  ? 557 TYR A CE1   1 
ATOM   4367 C  CE2   . TYR A 1 557 ? 11.366  26.139  19.983  1.00 39.55  ? 557 TYR A CE2   1 
ATOM   4368 C  CZ    . TYR A 1 557 ? 11.162  27.244  20.782  1.00 48.20  ? 557 TYR A CZ    1 
ATOM   4369 O  OH    . TYR A 1 557 ? 10.991  28.481  20.207  1.00 54.36  ? 557 TYR A OH    1 
ATOM   4370 N  N     . VAL A 1 558 ? 12.698  21.862  25.336  1.00 38.85  ? 558 VAL A N     1 
ATOM   4371 C  CA    . VAL A 1 558 ? 12.537  20.640  26.119  1.00 37.64  ? 558 VAL A CA    1 
ATOM   4372 C  C     . VAL A 1 558 ? 11.153  20.683  26.749  1.00 44.13  ? 558 VAL A C     1 
ATOM   4373 O  O     . VAL A 1 558 ? 10.538  21.760  26.852  1.00 43.23  ? 558 VAL A O     1 
ATOM   4374 C  CB    . VAL A 1 558 ? 13.651  20.487  27.183  1.00 42.74  ? 558 VAL A CB    1 
ATOM   4375 C  CG1   . VAL A 1 558 ? 15.028  20.609  26.541  1.00 39.76  ? 558 VAL A CG1   1 
ATOM   4376 C  CG2   . VAL A 1 558 ? 13.469  21.503  28.297  1.00 41.69  ? 558 VAL A CG2   1 
ATOM   4377 N  N     . PRO A 1 559 ? 10.617  19.534  27.168  1.00 41.34  ? 559 PRO A N     1 
ATOM   4378 C  CA    . PRO A 1 559 ? 9.286   19.534  27.786  1.00 43.71  ? 559 PRO A CA    1 
ATOM   4379 C  C     . PRO A 1 559 ? 9.260   20.365  29.060  1.00 41.51  ? 559 PRO A C     1 
ATOM   4380 O  O     . PRO A 1 559 ? 10.228  20.402  29.822  1.00 47.44  ? 559 PRO A O     1 
ATOM   4381 C  CB    . PRO A 1 559 ? 9.029   18.052  28.082  1.00 38.94  ? 559 PRO A CB    1 
ATOM   4382 C  CG    . PRO A 1 559 ? 9.920   17.312  27.156  1.00 41.41  ? 559 PRO A CG    1 
ATOM   4383 C  CD    . PRO A 1 559 ? 11.139  18.167  26.991  1.00 45.12  ? 559 PRO A CD    1 
ATOM   4384 N  N     . LYS A 1 560 ? 8.132   21.034  29.285  1.00 47.00  ? 560 LYS A N     1 
ATOM   4385 C  CA    . LYS A 1 560 ? 7.930   21.756  30.529  1.00 49.67  ? 560 LYS A CA    1 
ATOM   4386 C  C     . LYS A 1 560 ? 7.886   20.785  31.708  1.00 56.02  ? 560 LYS A C     1 
ATOM   4387 O  O     . LYS A 1 560 ? 7.806   19.564  31.548  1.00 58.65  ? 560 LYS A O     1 
ATOM   4388 C  CB    . LYS A 1 560 ? 6.633   22.562  30.483  1.00 53.62  ? 560 LYS A CB    1 
ATOM   4389 C  CG    . LYS A 1 560 ? 6.647   23.756  29.549  1.00 50.52  ? 560 LYS A CG    1 
ATOM   4390 C  CD    . LYS A 1 560 ? 5.333   24.513  29.649  1.00 49.07  ? 560 LYS A CD    1 
ATOM   4391 C  CE    . LYS A 1 560 ? 5.324   25.733  28.751  1.00 53.15  ? 560 LYS A CE    1 
ATOM   4392 N  NZ    . LYS A 1 560 ? 4.063   26.513  28.898  1.00 53.99  ? 560 LYS A NZ    1 
ATOM   4393 N  N     . GLU A 1 561 ? 7.938   21.348  32.911  1.00 62.19  ? 561 GLU A N     1 
ATOM   4394 C  CA    . GLU A 1 561 ? 7.745   20.544  34.108  1.00 70.56  ? 561 GLU A CA    1 
ATOM   4395 C  C     . GLU A 1 561 ? 6.332   19.975  34.121  1.00 69.40  ? 561 GLU A C     1 
ATOM   4396 O  O     . GLU A 1 561 ? 5.361   20.686  33.843  1.00 74.99  ? 561 GLU A O     1 
ATOM   4397 C  CB    . GLU A 1 561 ? 7.997   21.384  35.360  1.00 78.11  ? 561 GLU A CB    1 
ATOM   4398 C  CG    . GLU A 1 561 ? 9.390   21.991  35.427  1.00 92.16  ? 561 GLU A CG    1 
ATOM   4399 C  CD    . GLU A 1 561 ? 9.645   22.719  36.732  1.00 106.37 ? 561 GLU A CD    1 
ATOM   4400 O  OE1   . GLU A 1 561 ? 8.839   22.556  37.673  1.00 101.19 ? 561 GLU A OE1   1 
ATOM   4401 O  OE2   . GLU A 1 561 ? 10.651  23.455  36.817  1.00 112.25 ? 561 GLU A OE2   1 
ATOM   4402 N  N     . ASP A 1 562 ? 6.225   18.682  34.426  1.00 66.04  ? 562 ASP A N     1 
ATOM   4403 C  CA    . ASP A 1 562 ? 4.958   17.951  34.430  1.00 76.94  ? 562 ASP A CA    1 
ATOM   4404 C  C     . ASP A 1 562 ? 4.284   17.943  33.060  1.00 66.27  ? 562 ASP A C     1 
ATOM   4405 O  O     . ASP A 1 562 ? 3.069   17.744  32.965  1.00 69.95  ? 562 ASP A O     1 
ATOM   4406 C  CB    . ASP A 1 562 ? 3.994   18.502  35.489  1.00 87.39  ? 562 ASP A CB    1 
ATOM   4407 C  CG    . ASP A 1 562 ? 4.440   18.188  36.904  1.00 98.76  ? 562 ASP A CG    1 
ATOM   4408 O  OD1   . ASP A 1 562 ? 5.038   17.111  37.116  1.00 101.29 ? 562 ASP A OD1   1 
ATOM   4409 O  OD2   . ASP A 1 562 ? 4.193   19.018  37.805  1.00 105.87 ? 562 ASP A OD2   1 
ATOM   4410 N  N     . ALA A 1 563 ? 5.048   18.154  31.989  1.00 64.97  ? 563 ALA A N     1 
ATOM   4411 C  CA    . ALA A 1 563 ? 4.511   18.043  30.640  1.00 57.61  ? 563 ALA A CA    1 
ATOM   4412 C  C     . ALA A 1 563 ? 4.596   16.627  30.092  1.00 57.89  ? 563 ALA A C     1 
ATOM   4413 O  O     . ALA A 1 563 ? 3.843   16.285  29.173  1.00 61.50  ? 563 ALA A O     1 
ATOM   4414 C  CB    . ALA A 1 563 ? 5.241   19.000  29.693  1.00 53.31  ? 563 ALA A CB    1 
ATOM   4415 N  N     . LEU A 1 564 ? 5.495   15.804  30.625  1.00 56.43  ? 564 LEU A N     1 
ATOM   4416 C  CA    . LEU A 1 564 ? 5.573   14.399  30.259  1.00 56.06  ? 564 LEU A CA    1 
ATOM   4417 C  C     . LEU A 1 564 ? 4.698   13.571  31.187  1.00 54.68  ? 564 LEU A C     1 
ATOM   4418 O  O     . LEU A 1 564 ? 4.621   13.837  32.389  1.00 61.08  ? 564 LEU A O     1 
ATOM   4419 C  CB    . LEU A 1 564 ? 7.016   13.896  30.330  1.00 55.08  ? 564 LEU A CB    1 
ATOM   4420 C  CG    . LEU A 1 564 ? 7.890   14.102  29.094  1.00 52.25  ? 564 LEU A CG    1 
ATOM   4421 C  CD1   . LEU A 1 564 ? 9.296   13.586  29.349  1.00 57.23  ? 564 LEU A CD1   1 
ATOM   4422 C  CD2   . LEU A 1 564 ? 7.271   13.403  27.900  1.00 53.21  ? 564 LEU A CD2   1 
ATOM   4423 N  N     . ASN A 1 565 ? 4.034   12.568  30.619  1.00 61.27  ? 565 ASN A N     1 
ATOM   4424 C  CA    . ASN A 1 565 ? 3.276   11.605  31.412  1.00 58.44  ? 565 ASN A CA    1 
ATOM   4425 C  C     . ASN A 1 565 ? 4.272   10.640  32.040  1.00 59.17  ? 565 ASN A C     1 
ATOM   4426 O  O     . ASN A 1 565 ? 4.798   9.748   31.372  1.00 56.44  ? 565 ASN A O     1 
ATOM   4427 C  CB    . ASN A 1 565 ? 2.256   10.870  30.549  1.00 57.09  ? 565 ASN A CB    1 
ATOM   4428 C  CG    . ASN A 1 565 ? 1.261   10.072  31.372  1.00 63.14  ? 565 ASN A CG    1 
ATOM   4429 O  OD1   . ASN A 1 565 ? 1.429   9.900   32.579  1.00 63.43  ? 565 ASN A OD1   1 
ATOM   4430 N  ND2   . ASN A 1 565 ? 0.219   9.574   30.718  1.00 62.83  ? 565 ASN A ND2   1 
ATOM   4431 N  N     . LEU A 1 566 ? 4.549   10.828  33.329  1.00 63.56  ? 566 LEU A N     1 
ATOM   4432 C  CA    . LEU A 1 566 ? 5.451   9.956   34.070  1.00 67.85  ? 566 LEU A CA    1 
ATOM   4433 C  C     . LEU A 1 566 ? 4.714   9.128   35.115  1.00 72.99  ? 566 LEU A C     1 
ATOM   4434 O  O     . LEU A 1 566 ? 5.337   8.615   36.051  1.00 79.22  ? 566 LEU A O     1 
ATOM   4435 C  CB    . LEU A 1 566 ? 6.563   10.777  34.723  1.00 63.23  ? 566 LEU A CB    1 
ATOM   4436 C  CG    . LEU A 1 566 ? 7.458   11.558  33.760  1.00 60.19  ? 566 LEU A CG    1 
ATOM   4437 C  CD1   . LEU A 1 566 ? 8.468   12.396  34.524  1.00 57.84  ? 566 LEU A CD1   1 
ATOM   4438 C  CD2   . LEU A 1 566 ? 8.161   10.615  32.794  1.00 62.48  ? 566 LEU A CD2   1 
ATOM   4439 N  N     . LYS A 1 567 ? 3.398   8.989   34.973  1.00 72.25  ? 567 LYS A N     1 
ATOM   4440 C  CA    . LYS A 1 567 ? 2.620   8.196   35.913  1.00 81.32  ? 567 LYS A CA    1 
ATOM   4441 C  C     . LYS A 1 567 ? 2.928   6.715   35.735  1.00 84.26  ? 567 LYS A C     1 
ATOM   4442 O  O     . LYS A 1 567 ? 3.053   6.218   34.611  1.00 79.39  ? 567 LYS A O     1 
ATOM   4443 C  CB    . LYS A 1 567 ? 1.128   8.462   35.717  1.00 83.96  ? 567 LYS A CB    1 
ATOM   4444 C  CG    . LYS A 1 567 ? 0.758   9.934   35.832  1.00 94.30  ? 567 LYS A CG    1 
ATOM   4445 C  CD    . LYS A 1 567 ? -0.716  10.173  35.556  1.00 102.01 ? 567 LYS A CD    1 
ATOM   4446 C  CE    . LYS A 1 567 ? -1.044  11.657  35.603  1.00 103.80 ? 567 LYS A CE    1 
ATOM   4447 N  NZ    . LYS A 1 567 ? -2.492  11.919  35.374  1.00 112.25 ? 567 LYS A NZ    1 
ATOM   4448 N  N     . GLY A 1 568 ? 3.053   6.008   36.856  1.00 82.63  ? 568 GLY A N     1 
ATOM   4449 C  CA    . GLY A 1 568 ? 3.507   4.637   36.848  1.00 83.66  ? 568 GLY A CA    1 
ATOM   4450 C  C     . GLY A 1 568 ? 5.002   4.470   37.005  1.00 90.02  ? 568 GLY A C     1 
ATOM   4451 O  O     . GLY A 1 568 ? 5.473   3.332   37.123  1.00 90.38  ? 568 GLY A O     1 
ATOM   4452 N  N     . LEU A 1 569 ? 5.761   5.565   37.005  1.00 92.66  ? 569 LEU A N     1 
ATOM   4453 C  CA    . LEU A 1 569 ? 7.200   5.516   37.226  1.00 93.00  ? 569 LEU A CA    1 
ATOM   4454 C  C     . LEU A 1 569 ? 7.548   6.212   38.536  1.00 101.44 ? 569 LEU A C     1 
ATOM   4455 O  O     . LEU A 1 569 ? 7.797   5.551   39.550  1.00 99.36  ? 569 LEU A O     1 
ATOM   4456 C  CB    . LEU A 1 569 ? 7.947   6.160   36.054  1.00 93.12  ? 569 LEU A CB    1 
ATOM   4457 C  CG    . LEU A 1 569 ? 7.693   5.562   34.667  1.00 78.56  ? 569 LEU A CG    1 
ATOM   4458 C  CD1   . LEU A 1 569 ? 8.416   6.358   33.591  1.00 72.80  ? 569 LEU A CD1   1 
ATOM   4459 C  CD2   . LEU A 1 569 ? 8.112   4.101   34.624  1.00 78.70  ? 569 LEU A CD2   1 
ATOM   4460 N  N     . GLY A 1 570 ? 7.569   7.544   38.526  1.00 108.27 ? 570 GLY A N     1 
ATOM   4461 C  CA    . GLY A 1 570 ? 7.817   8.314   39.731  1.00 107.26 ? 570 GLY A CA    1 
ATOM   4462 C  C     . GLY A 1 570 ? 9.264   8.315   40.179  1.00 111.58 ? 570 GLY A C     1 
ATOM   4463 O  O     . GLY A 1 570 ? 9.809   9.361   40.547  1.00 105.44 ? 570 GLY A O     1 
ATOM   4464 N  N     . ASP A 1 571 ? 9.896   7.141   40.153  1.00 120.17 ? 571 ASP A N     1 
ATOM   4465 C  CA    . ASP A 1 571 ? 11.289  6.994   40.553  1.00 118.05 ? 571 ASP A CA    1 
ATOM   4466 C  C     . ASP A 1 571 ? 12.262  7.644   39.578  1.00 117.69 ? 571 ASP A C     1 
ATOM   4467 O  O     . ASP A 1 571 ? 13.466  7.667   39.858  1.00 117.46 ? 571 ASP A O     1 
ATOM   4468 C  CB    . ASP A 1 571 ? 11.626  5.510   40.693  1.00 119.89 ? 571 ASP A CB    1 
ATOM   4469 C  CG    . ASP A 1 571 ? 11.262  4.712   39.455  1.00 125.16 ? 571 ASP A CG    1 
ATOM   4470 O  OD1   . ASP A 1 571 ? 10.598  5.274   38.558  1.00 114.20 ? 571 ASP A OD1   1 
ATOM   4471 O  OD2   . ASP A 1 571 ? 11.642  3.525   39.376  1.00 136.44 ? 571 ASP A OD2   1 
ATOM   4472 N  N     . VAL A 1 572 ? 11.778  8.162   38.452  1.00 109.21 ? 572 VAL A N     1 
ATOM   4473 C  CA    . VAL A 1 572 ? 12.652  8.718   37.425  1.00 101.16 ? 572 VAL A CA    1 
ATOM   4474 C  C     . VAL A 1 572 ? 13.311  9.986   37.954  1.00 93.74  ? 572 VAL A C     1 
ATOM   4475 O  O     . VAL A 1 572 ? 12.631  10.923  38.388  1.00 95.26  ? 572 VAL A O     1 
ATOM   4476 C  CB    . VAL A 1 572 ? 11.869  8.996   36.136  1.00 94.69  ? 572 VAL A CB    1 
ATOM   4477 C  CG1   . VAL A 1 572 ? 12.739  9.735   35.139  1.00 81.78  ? 572 VAL A CG1   1 
ATOM   4478 C  CG2   . VAL A 1 572 ? 11.350  7.695   35.541  1.00 90.43  ? 572 VAL A CG2   1 
ATOM   4479 N  N     . ASN A 1 573 ? 14.644  10.020  37.916  1.00 89.39  ? 573 ASN A N     1 
ATOM   4480 C  CA    . ASN A 1 573 ? 15.408  11.199  38.322  1.00 89.31  ? 573 ASN A CA    1 
ATOM   4481 C  C     . ASN A 1 573 ? 15.346  12.216  37.187  1.00 81.94  ? 573 ASN A C     1 
ATOM   4482 O  O     . ASN A 1 573 ? 16.237  12.312  36.339  1.00 80.51  ? 573 ASN A O     1 
ATOM   4483 C  CB    . ASN A 1 573 ? 16.844  10.824  38.668  1.00 94.30  ? 573 ASN A CB    1 
ATOM   4484 C  CG    . ASN A 1 573 ? 17.673  12.022  39.092  1.00 97.72  ? 573 ASN A CG    1 
ATOM   4485 O  OD1   . ASN A 1 573 ? 17.137  13.070  39.455  1.00 96.32  ? 573 ASN A OD1   1 
ATOM   4486 N  ND2   . ASN A 1 573 ? 18.992  11.871  39.049  1.00 101.95 ? 573 ASN A ND2   1 
ATOM   4487 N  N     . VAL A 1 574 ? 14.264  13.000  37.189  1.00 83.92  ? 574 VAL A N     1 
ATOM   4488 C  CA    . VAL A 1 574 ? 14.006  13.924  36.088  1.00 77.90  ? 574 VAL A CA    1 
ATOM   4489 C  C     . VAL A 1 574 ? 15.091  14.988  35.996  1.00 77.52  ? 574 VAL A C     1 
ATOM   4490 O  O     . VAL A 1 574 ? 15.323  15.558  34.922  1.00 60.78  ? 574 VAL A O     1 
ATOM   4491 C  CB    . VAL A 1 574 ? 12.607  14.555  36.249  1.00 72.96  ? 574 VAL A CB    1 
ATOM   4492 C  CG1   . VAL A 1 574 ? 11.538  13.484  36.148  1.00 74.76  ? 574 VAL A CG1   1 
ATOM   4493 C  CG2   . VAL A 1 574 ? 12.508  15.287  37.576  1.00 73.71  ? 574 VAL A CG2   1 
ATOM   4494 N  N     . GLU A 1 575 ? 15.773  15.272  37.108  1.00 77.63  ? 575 GLU A N     1 
ATOM   4495 C  CA    . GLU A 1 575 ? 16.829  16.278  37.089  1.00 82.41  ? 575 GLU A CA    1 
ATOM   4496 C  C     . GLU A 1 575 ? 17.978  15.856  36.182  1.00 72.43  ? 575 GLU A C     1 
ATOM   4497 O  O     . GLU A 1 575 ? 18.492  16.665  35.400  1.00 65.80  ? 575 GLU A O     1 
ATOM   4498 C  CB    . GLU A 1 575 ? 17.332  16.538  38.510  1.00 89.51  ? 575 GLU A CB    1 
ATOM   4499 C  CG    . GLU A 1 575 ? 16.339  17.272  39.395  1.00 95.49  ? 575 GLU A CG    1 
ATOM   4500 C  CD    . GLU A 1 575 ? 16.834  17.423  40.820  1.00 105.82 ? 575 GLU A CD    1 
ATOM   4501 O  OE1   . GLU A 1 575 ? 17.757  16.678  41.211  1.00 106.93 ? 575 GLU A OE1   1 
ATOM   4502 O  OE2   . GLU A 1 575 ? 16.303  18.287  41.549  1.00 109.09 ? 575 GLU A OE2   1 
ATOM   4503 N  N     . GLU A 1 576 ? 18.387  14.589  36.261  1.00 76.33  ? 576 GLU A N     1 
ATOM   4504 C  CA    . GLU A 1 576 ? 19.498  14.109  35.451  1.00 80.21  ? 576 GLU A CA    1 
ATOM   4505 C  C     . GLU A 1 576 ? 19.077  13.734  34.035  1.00 70.24  ? 576 GLU A C     1 
ATOM   4506 O  O     . GLU A 1 576 ? 19.929  13.695  33.141  1.00 68.85  ? 576 GLU A O     1 
ATOM   4507 C  CB    . GLU A 1 576 ? 20.165  12.911  36.133  1.00 86.46  ? 576 GLU A CB    1 
ATOM   4508 C  CG    . GLU A 1 576 ? 21.557  12.588  35.612  1.00 87.75  ? 576 GLU A CG    1 
ATOM   4509 C  CD    . GLU A 1 576 ? 22.242  11.497  36.411  1.00 97.79  ? 576 GLU A CD    1 
ATOM   4510 O  OE1   . GLU A 1 576 ? 21.716  11.121  37.481  1.00 100.39 ? 576 GLU A OE1   1 
ATOM   4511 O  OE2   . GLU A 1 576 ? 23.306  11.015  35.969  1.00 101.32 ? 576 GLU A OE2   1 
ATOM   4512 N  N     . LEU A 1 577 ? 17.788  13.466  33.806  1.00 65.89  ? 577 LEU A N     1 
ATOM   4513 C  CA    . LEU A 1 577 ? 17.339  13.135  32.457  1.00 61.37  ? 577 LEU A CA    1 
ATOM   4514 C  C     . LEU A 1 577 ? 17.348  14.351  31.541  1.00 53.72  ? 577 LEU A C     1 
ATOM   4515 O  O     . LEU A 1 577 ? 17.461  14.200  30.319  1.00 50.05  ? 577 LEU A O     1 
ATOM   4516 C  CB    . LEU A 1 577 ? 15.940  12.523  32.492  1.00 56.28  ? 577 LEU A CB    1 
ATOM   4517 C  CG    . LEU A 1 577 ? 15.859  10.996  32.483  1.00 62.63  ? 577 LEU A CG    1 
ATOM   4518 C  CD1   . LEU A 1 577 ? 16.218  10.429  33.841  1.00 73.22  ? 577 LEU A CD1   1 
ATOM   4519 C  CD2   . LEU A 1 577 ? 14.478  10.534  32.053  1.00 65.23  ? 577 LEU A CD2   1 
ATOM   4520 N  N     . PHE A 1 578 ? 17.223  15.555  32.100  1.00 48.28  ? 578 PHE A N     1 
ATOM   4521 C  CA    . PHE A 1 578 ? 17.203  16.779  31.306  1.00 52.91  ? 578 PHE A CA    1 
ATOM   4522 C  C     . PHE A 1 578 ? 18.259  17.785  31.738  1.00 52.74  ? 578 PHE A C     1 
ATOM   4523 O  O     . PHE A 1 578 ? 18.201  18.946  31.317  1.00 57.02  ? 578 PHE A O     1 
ATOM   4524 C  CB    . PHE A 1 578 ? 15.814  17.424  31.356  1.00 50.97  ? 578 PHE A CB    1 
ATOM   4525 C  CG    . PHE A 1 578 ? 14.766  16.660  30.603  1.00 47.34  ? 578 PHE A CG    1 
ATOM   4526 C  CD1   . PHE A 1 578 ? 14.539  16.912  29.259  1.00 49.34  ? 578 PHE A CD1   1 
ATOM   4527 C  CD2   . PHE A 1 578 ? 14.009  15.688  31.237  1.00 51.57  ? 578 PHE A CD2   1 
ATOM   4528 C  CE1   . PHE A 1 578 ? 13.577  16.208  28.559  1.00 44.24  ? 578 PHE A CE1   1 
ATOM   4529 C  CE2   . PHE A 1 578 ? 13.044  14.981  30.546  1.00 51.35  ? 578 PHE A CE2   1 
ATOM   4530 C  CZ    . PHE A 1 578 ? 12.826  15.242  29.204  1.00 46.66  ? 578 PHE A CZ    1 
ATOM   4531 N  N     . GLY A 1 579 ? 19.220  17.372  32.560  1.00 55.02  ? 579 GLY A N     1 
ATOM   4532 C  CA    . GLY A 1 579 ? 20.313  18.240  32.957  1.00 55.97  ? 579 GLY A CA    1 
ATOM   4533 C  C     . GLY A 1 579 ? 21.157  18.713  31.791  1.00 62.29  ? 579 GLY A C     1 
ATOM   4534 O  O     . GLY A 1 579 ? 21.629  17.904  30.986  1.00 58.93  ? 579 GLY A O     1 
ATOM   4535 N  N     . ILE A 1 580 ? 21.346  20.024  31.685  1.00 63.02  ? 580 ILE A N     1 
ATOM   4536 C  CA    . ILE A 1 580 ? 22.147  20.625  30.627  1.00 58.41  ? 580 ILE A CA    1 
ATOM   4537 C  C     . ILE A 1 580 ? 23.375  21.234  31.292  1.00 57.88  ? 580 ILE A C     1 
ATOM   4538 O  O     . ILE A 1 580 ? 23.307  22.316  31.884  1.00 64.80  ? 580 ILE A O     1 
ATOM   4539 C  CB    . ILE A 1 580 ? 21.359  21.668  29.829  1.00 63.21  ? 580 ILE A CB    1 
ATOM   4540 C  CG1   . ILE A 1 580 ? 20.128  21.024  29.189  1.00 60.33  ? 580 ILE A CG1   1 
ATOM   4541 C  CG2   . ILE A 1 580 ? 22.243  22.296  28.759  1.00 59.33  ? 580 ILE A CG2   1 
ATOM   4542 C  CD1   . ILE A 1 580 ? 19.249  22.001  28.445  1.00 58.23  ? 580 ILE A CD1   1 
ATOM   4543 N  N     . SER A 1 581 ? 24.503  20.539  31.197  1.00 54.67  ? 581 SER A N     1 
ATOM   4544 C  CA    . SER A 1 581 ? 25.752  21.012  31.773  1.00 56.42  ? 581 SER A CA    1 
ATOM   4545 C  C     . SER A 1 581 ? 26.479  21.894  30.768  1.00 51.77  ? 581 SER A C     1 
ATOM   4546 O  O     . SER A 1 581 ? 26.725  21.477  29.631  1.00 49.51  ? 581 SER A O     1 
ATOM   4547 C  CB    . SER A 1 581 ? 26.639  19.835  32.181  1.00 46.61  ? 581 SER A CB    1 
ATOM   4548 O  OG    . SER A 1 581 ? 27.937  20.277  32.536  1.00 59.86  ? 581 SER A OG    1 
ATOM   4549 N  N     . LYS A 1 582 ? 26.814  23.115  31.188  1.00 53.52  ? 582 LYS A N     1 
ATOM   4550 C  CA    . LYS A 1 582 ? 27.601  23.995  30.331  1.00 52.67  ? 582 LYS A CA    1 
ATOM   4551 C  C     . LYS A 1 582 ? 28.968  23.392  30.040  1.00 53.43  ? 582 LYS A C     1 
ATOM   4552 O  O     . LYS A 1 582 ? 29.477  23.498  28.918  1.00 45.86  ? 582 LYS A O     1 
ATOM   4553 C  CB    . LYS A 1 582 ? 27.749  25.370  30.984  1.00 55.01  ? 582 LYS A CB    1 
ATOM   4554 C  CG    . LYS A 1 582 ? 28.577  26.355  30.171  1.00 55.92  ? 582 LYS A CG    1 
ATOM   4555 C  CD    . LYS A 1 582 ? 28.686  27.700  30.871  1.00 59.72  ? 582 LYS A CD    1 
ATOM   4556 C  CE    . LYS A 1 582 ? 29.522  28.674  30.056  1.00 60.28  ? 582 LYS A CE    1 
ATOM   4557 N  NZ    . LYS A 1 582 ? 29.472  30.056  30.604  1.00 59.31  ? 582 LYS A NZ    1 
ATOM   4558 N  N     . GLU A 1 583 ? 29.572  22.743  31.040  1.00 47.90  ? 583 GLU A N     1 
ATOM   4559 C  CA    . GLU A 1 583 ? 30.886  22.138  30.850  1.00 49.74  ? 583 GLU A CA    1 
ATOM   4560 C  C     . GLU A 1 583 ? 30.843  21.031  29.804  1.00 51.58  ? 583 GLU A C     1 
ATOM   4561 O  O     . GLU A 1 583 ? 31.756  20.913  28.978  1.00 54.71  ? 583 GLU A O     1 
ATOM   4562 C  CB    . GLU A 1 583 ? 31.409  21.601  32.184  1.00 58.12  ? 583 GLU A CB    1 
ATOM   4563 C  CG    . GLU A 1 583 ? 31.444  22.641  33.289  1.00 63.70  ? 583 GLU A CG    1 
ATOM   4564 C  CD    . GLU A 1 583 ? 31.899  22.067  34.616  1.00 85.24  ? 583 GLU A CD    1 
ATOM   4565 O  OE1   . GLU A 1 583 ? 32.104  20.838  34.696  1.00 88.02  ? 583 GLU A OE1   1 
ATOM   4566 O  OE2   . GLU A 1 583 ? 32.051  22.847  35.580  1.00 88.49  ? 583 GLU A OE2   1 
ATOM   4567 N  N     . PHE A 1 584 ? 29.792  20.209  29.821  1.00 51.85  ? 584 PHE A N     1 
ATOM   4568 C  CA    . PHE A 1 584 ? 29.666  19.162  28.812  1.00 44.87  ? 584 PHE A CA    1 
ATOM   4569 C  C     . PHE A 1 584 ? 29.498  19.758  27.422  1.00 45.78  ? 584 PHE A C     1 
ATOM   4570 O  O     . PHE A 1 584 ? 30.186  19.361  26.473  1.00 44.17  ? 584 PHE A O     1 
ATOM   4571 C  CB    . PHE A 1 584 ? 28.488  18.242  29.141  1.00 41.66  ? 584 PHE A CB    1 
ATOM   4572 C  CG    . PHE A 1 584 ? 28.151  17.279  28.034  1.00 44.85  ? 584 PHE A CG    1 
ATOM   4573 C  CD1   . PHE A 1 584 ? 28.830  16.079  27.916  1.00 45.58  ? 584 PHE A CD1   1 
ATOM   4574 C  CD2   . PHE A 1 584 ? 27.164  17.579  27.106  1.00 40.82  ? 584 PHE A CD2   1 
ATOM   4575 C  CE1   . PHE A 1 584 ? 28.530  15.193  26.894  1.00 41.76  ? 584 PHE A CE1   1 
ATOM   4576 C  CE2   . PHE A 1 584 ? 26.860  16.699  26.078  1.00 44.01  ? 584 PHE A CE2   1 
ATOM   4577 C  CZ    . PHE A 1 584 ? 27.543  15.504  25.973  1.00 43.91  ? 584 PHE A CZ    1 
ATOM   4578 N  N     . TRP A 1 585 ? 28.582  20.716  27.281  1.00 47.73  ? 585 TRP A N     1 
ATOM   4579 C  CA    . TRP A 1 585 ? 28.229  21.236  25.966  1.00 43.91  ? 585 TRP A CA    1 
ATOM   4580 C  C     . TRP A 1 585 ? 29.284  22.167  25.382  1.00 41.75  ? 585 TRP A C     1 
ATOM   4581 O  O     . TRP A 1 585 ? 29.311  22.357  24.163  1.00 42.51  ? 585 TRP A O     1 
ATOM   4582 C  CB    . TRP A 1 585 ? 26.876  21.944  26.036  1.00 40.09  ? 585 TRP A CB    1 
ATOM   4583 C  CG    . TRP A 1 585 ? 25.740  20.980  26.081  1.00 36.56  ? 585 TRP A CG    1 
ATOM   4584 C  CD1   . TRP A 1 585 ? 25.084  20.531  27.190  1.00 41.93  ? 585 TRP A CD1   1 
ATOM   4585 C  CD2   . TRP A 1 585 ? 25.138  20.317  24.963  1.00 45.98  ? 585 TRP A CD2   1 
ATOM   4586 N  NE1   . TRP A 1 585 ? 24.105  19.638  26.831  1.00 44.64  ? 585 TRP A NE1   1 
ATOM   4587 C  CE2   . TRP A 1 585 ? 24.117  19.490  25.469  1.00 40.73  ? 585 TRP A CE2   1 
ATOM   4588 C  CE3   . TRP A 1 585 ? 25.360  20.349  23.583  1.00 35.65  ? 585 TRP A CE3   1 
ATOM   4589 C  CZ2   . TRP A 1 585 ? 23.318  18.701  24.644  1.00 42.50  ? 585 TRP A CZ2   1 
ATOM   4590 C  CZ3   . TRP A 1 585 ? 24.565  19.565  22.765  1.00 41.49  ? 585 TRP A CZ3   1 
ATOM   4591 C  CH2   . TRP A 1 585 ? 23.558  18.751  23.298  1.00 38.86  ? 585 TRP A CH2   1 
ATOM   4592 N  N     . GLU A 1 586 ? 30.153  22.748  26.212  1.00 40.67  ? 586 GLU A N     1 
ATOM   4593 C  CA    . GLU A 1 586 ? 31.275  23.501  25.665  1.00 39.89  ? 586 GLU A CA    1 
ATOM   4594 C  C     . GLU A 1 586 ? 32.260  22.577  24.961  1.00 44.50  ? 586 GLU A C     1 
ATOM   4595 O  O     . GLU A 1 586 ? 32.811  22.932  23.912  1.00 45.56  ? 586 GLU A O     1 
ATOM   4596 C  CB    . GLU A 1 586 ? 31.974  24.293  26.771  1.00 49.66  ? 586 GLU A CB    1 
ATOM   4597 C  CG    . GLU A 1 586 ? 31.226  25.543  27.197  1.00 50.14  ? 586 GLU A CG    1 
ATOM   4598 C  CD    . GLU A 1 586 ? 32.037  26.413  28.130  1.00 62.07  ? 586 GLU A CD    1 
ATOM   4599 O  OE1   . GLU A 1 586 ? 32.885  25.867  28.868  1.00 61.63  ? 586 GLU A OE1   1 
ATOM   4600 O  OE2   . GLU A 1 586 ? 31.831  27.645  28.119  1.00 71.22  ? 586 GLU A OE2   1 
ATOM   4601 N  N     . LYS A 1 587 ? 32.492  21.387  25.520  1.00 40.44  ? 587 LYS A N     1 
ATOM   4602 C  CA    . LYS A 1 587 ? 33.341  20.408  24.853  1.00 40.30  ? 587 LYS A CA    1 
ATOM   4603 C  C     . LYS A 1 587 ? 32.656  19.818  23.628  1.00 37.54  ? 587 LYS A C     1 
ATOM   4604 O  O     . LYS A 1 587 ? 33.322  19.523  22.630  1.00 37.05  ? 587 LYS A O     1 
ATOM   4605 C  CB    . LYS A 1 587 ? 33.723  19.290  25.820  1.00 42.30  ? 587 LYS A CB    1 
ATOM   4606 C  CG    . LYS A 1 587 ? 34.242  19.772  27.162  1.00 56.27  ? 587 LYS A CG    1 
ATOM   4607 C  CD    . LYS A 1 587 ? 34.483  18.605  28.105  1.00 65.91  ? 587 LYS A CD    1 
ATOM   4608 C  CE    . LYS A 1 587 ? 34.894  19.093  29.482  1.00 69.47  ? 587 LYS A CE    1 
ATOM   4609 N  NZ    . LYS A 1 587 ? 36.108  19.954  29.424  1.00 83.59  ? 587 LYS A NZ    1 
ATOM   4610 N  N     . GLU A 1 588 ? 31.334  19.644  23.686  1.00 39.51  ? 588 GLU A N     1 
ATOM   4611 C  CA    . GLU A 1 588 ? 30.618  19.017  22.579  1.00 39.12  ? 588 GLU A CA    1 
ATOM   4612 C  C     . GLU A 1 588 ? 30.696  19.864  21.315  1.00 35.93  ? 588 GLU A C     1 
ATOM   4613 O  O     . GLU A 1 588 ? 30.955  19.339  20.226  1.00 39.14  ? 588 GLU A O     1 
ATOM   4614 C  CB    . GLU A 1 588 ? 29.164  18.764  22.973  1.00 38.04  ? 588 GLU A CB    1 
ATOM   4615 C  CG    . GLU A 1 588 ? 28.371  17.922  21.983  1.00 33.66  ? 588 GLU A CG    1 
ATOM   4616 C  CD    . GLU A 1 588 ? 28.817  16.468  21.946  1.00 38.71  ? 588 GLU A CD    1 
ATOM   4617 O  OE1   . GLU A 1 588 ? 29.591  16.045  22.833  1.00 34.97  ? 588 GLU A OE1   1 
ATOM   4618 O  OE2   . GLU A 1 588 ? 28.392  15.745  21.022  1.00 30.78  ? 588 GLU A OE2   1 
ATOM   4619 N  N     . VAL A 1 589 ? 30.485  21.176  21.437  1.00 38.98  ? 589 VAL A N     1 
ATOM   4620 C  CA    . VAL A 1 589 ? 30.526  22.036  20.256  1.00 38.15  ? 589 VAL A CA    1 
ATOM   4621 C  C     . VAL A 1 589 ? 31.942  22.122  19.697  1.00 40.64  ? 589 VAL A C     1 
ATOM   4622 O  O     . VAL A 1 589 ? 32.132  22.227  18.479  1.00 38.43  ? 589 VAL A O     1 
ATOM   4623 C  CB    . VAL A 1 589 ? 29.956  23.430  20.578  1.00 44.95  ? 589 VAL A CB    1 
ATOM   4624 C  CG1   . VAL A 1 589 ? 28.471  23.331  20.880  1.00 44.69  ? 589 VAL A CG1   1 
ATOM   4625 C  CG2   . VAL A 1 589 ? 30.700  24.062  21.742  1.00 43.99  ? 589 VAL A CG2   1 
ATOM   4626 N  N     . GLU A 1 590 ? 32.956  22.083  20.569  1.00 37.18  ? 590 GLU A N     1 
ATOM   4627 C  CA    . GLU A 1 590 ? 34.335  22.061  20.089  1.00 35.93  ? 590 GLU A CA    1 
ATOM   4628 C  C     . GLU A 1 590 ? 34.594  20.839  19.218  1.00 37.91  ? 590 GLU A C     1 
ATOM   4629 O  O     . GLU A 1 590 ? 35.233  20.944  18.165  1.00 41.63  ? 590 GLU A O     1 
ATOM   4630 C  CB    . GLU A 1 590 ? 35.313  22.093  21.268  1.00 38.78  ? 590 GLU A CB    1 
ATOM   4631 C  CG    . GLU A 1 590 ? 35.386  23.428  21.989  1.00 46.77  ? 590 GLU A CG    1 
ATOM   4632 C  CD    . GLU A 1 590 ? 36.475  23.461  23.049  1.00 61.08  ? 590 GLU A CD    1 
ATOM   4633 O  OE1   . GLU A 1 590 ? 37.236  22.476  23.156  1.00 54.34  ? 590 GLU A OE1   1 
ATOM   4634 O  OE2   . GLU A 1 590 ? 36.570  24.473  23.775  1.00 59.96  ? 590 GLU A OE2   1 
ATOM   4635 N  N     . GLU A 1 591 ? 34.099  19.670  19.637  1.00 34.39  ? 591 GLU A N     1 
ATOM   4636 C  CA    . GLU A 1 591 ? 34.297  18.459  18.848  1.00 38.22  ? 591 GLU A CA    1 
ATOM   4637 C  C     . GLU A 1 591 ? 33.490  18.503  17.556  1.00 38.01  ? 591 GLU A C     1 
ATOM   4638 O  O     . GLU A 1 591 ? 33.955  18.029  16.512  1.00 37.35  ? 591 GLU A O     1 
ATOM   4639 C  CB    . GLU A 1 591 ? 33.931  17.224  19.673  1.00 33.93  ? 591 GLU A CB    1 
ATOM   4640 C  CG    . GLU A 1 591 ? 34.910  16.923  20.795  1.00 43.26  ? 591 GLU A CG    1 
ATOM   4641 C  CD    . GLU A 1 591 ? 36.320  16.682  20.288  1.00 44.77  ? 591 GLU A CD    1 
ATOM   4642 O  OE1   . GLU A 1 591 ? 36.482  15.942  19.293  1.00 43.17  ? 591 GLU A OE1   1 
ATOM   4643 O  OE2   . GLU A 1 591 ? 37.266  17.240  20.879  1.00 52.21  ? 591 GLU A OE2   1 
ATOM   4644 N  N     . ILE A 1 592 ? 32.280  19.062  17.606  1.00 31.99  ? 592 ILE A N     1 
ATOM   4645 C  CA    . ILE A 1 592 ? 31.494  19.222  16.386  1.00 35.59  ? 592 ILE A CA    1 
ATOM   4646 C  C     . ILE A 1 592 ? 32.178  20.205  15.446  1.00 41.16  ? 592 ILE A C     1 
ATOM   4647 O  O     . ILE A 1 592 ? 32.199  20.009  14.225  1.00 36.02  ? 592 ILE A O     1 
ATOM   4648 C  CB    . ILE A 1 592 ? 30.061  19.670  16.729  1.00 33.15  ? 592 ILE A CB    1 
ATOM   4649 C  CG1   . ILE A 1 592 ? 29.381  18.644  17.634  1.00 39.36  ? 592 ILE A CG1   1 
ATOM   4650 C  CG2   . ILE A 1 592 ? 29.244  19.870  15.458  1.00 30.83  ? 592 ILE A CG2   1 
ATOM   4651 C  CD1   . ILE A 1 592 ? 28.095  19.141  18.257  1.00 40.39  ? 592 ILE A CD1   1 
ATOM   4652 N  N     . ASP A 1 593 ? 32.764  21.267  16.002  1.00 36.25  ? 593 ASP A N     1 
ATOM   4653 C  CA    . ASP A 1 593 ? 33.460  22.252  15.182  1.00 33.10  ? 593 ASP A CA    1 
ATOM   4654 C  C     . ASP A 1 593 ? 34.660  21.626  14.480  1.00 42.43  ? 593 ASP A C     1 
ATOM   4655 O  O     . ASP A 1 593 ? 34.815  21.754  13.260  1.00 39.02  ? 593 ASP A O     1 
ATOM   4656 C  CB    . ASP A 1 593 ? 33.891  23.434  16.053  1.00 41.82  ? 593 ASP A CB    1 
ATOM   4657 C  CG    . ASP A 1 593 ? 34.419  24.603  15.242  1.00 51.05  ? 593 ASP A CG    1 
ATOM   4658 O  OD1   . ASP A 1 593 ? 34.225  24.619  14.009  1.00 51.70  ? 593 ASP A OD1   1 
ATOM   4659 O  OD2   . ASP A 1 593 ? 35.031  25.510  15.842  1.00 53.03  ? 593 ASP A OD2   1 
ATOM   4660 N  N     . LYS A 1 594 ? 35.519  20.938  15.240  1.00 41.53  ? 594 LYS A N     1 
ATOM   4661 C  CA    . LYS A 1 594 ? 36.695  20.306  14.649  1.00 36.81  ? 594 LYS A CA    1 
ATOM   4662 C  C     . LYS A 1 594 ? 36.300  19.275  13.599  1.00 39.13  ? 594 LYS A C     1 
ATOM   4663 O  O     . LYS A 1 594 ? 36.969  19.136  12.568  1.00 40.49  ? 594 LYS A O     1 
ATOM   4664 C  CB    . LYS A 1 594 ? 37.550  19.655  15.739  1.00 38.55  ? 594 LYS A CB    1 
ATOM   4665 C  CG    . LYS A 1 594 ? 38.136  20.639  16.736  1.00 44.65  ? 594 LYS A CG    1 
ATOM   4666 C  CD    . LYS A 1 594 ? 39.217  20.003  17.602  1.00 50.36  ? 594 LYS A CD    1 
ATOM   4667 C  CE    . LYS A 1 594 ? 38.665  18.881  18.467  1.00 42.26  ? 594 LYS A CE    1 
ATOM   4668 N  NZ    . LYS A 1 594 ? 39.591  18.567  19.597  1.00 50.07  ? 594 LYS A NZ    1 
ATOM   4669 N  N     . TYR A 1 595 ? 35.210  18.548  13.841  1.00 36.69  ? 595 TYR A N     1 
ATOM   4670 C  CA    . TYR A 1 595 ? 34.776  17.523  12.898  1.00 38.53  ? 595 TYR A CA    1 
ATOM   4671 C  C     . TYR A 1 595 ? 34.268  18.143  11.602  1.00 36.82  ? 595 TYR A C     1 
ATOM   4672 O  O     . TYR A 1 595 ? 34.700  17.761  10.508  1.00 37.04  ? 595 TYR A O     1 
ATOM   4673 C  CB    . TYR A 1 595 ? 33.699  16.651  13.543  1.00 38.19  ? 595 TYR A CB    1 
ATOM   4674 C  CG    . TYR A 1 595 ? 33.105  15.616  12.620  1.00 33.85  ? 595 TYR A CG    1 
ATOM   4675 C  CD1   . TYR A 1 595 ? 33.745  14.405  12.399  1.00 36.38  ? 595 TYR A CD1   1 
ATOM   4676 C  CD2   . TYR A 1 595 ? 31.896  15.845  11.976  1.00 33.75  ? 595 TYR A CD2   1 
ATOM   4677 C  CE1   . TYR A 1 595 ? 33.203  13.456  11.559  1.00 36.61  ? 595 TYR A CE1   1 
ATOM   4678 C  CE2   . TYR A 1 595 ? 31.348  14.903  11.137  1.00 33.33  ? 595 TYR A CE2   1 
ATOM   4679 C  CZ    . TYR A 1 595 ? 32.003  13.710  10.932  1.00 36.38  ? 595 TYR A CZ    1 
ATOM   4680 O  OH    . TYR A 1 595 ? 31.454  12.768  10.095  1.00 51.25  ? 595 TYR A OH    1 
ATOM   4681 N  N     . LEU A 1 596 ? 33.348  19.106  11.704  1.00 37.89  ? 596 LEU A N     1 
ATOM   4682 C  CA    . LEU A 1 596 ? 32.780  19.717  10.505  1.00 34.84  ? 596 LEU A CA    1 
ATOM   4683 C  C     . LEU A 1 596 ? 33.837  20.481  9.717   1.00 41.67  ? 596 LEU A C     1 
ATOM   4684 O  O     . LEU A 1 596 ? 33.835  20.458  8.481   1.00 39.62  ? 596 LEU A O     1 
ATOM   4685 C  CB    . LEU A 1 596 ? 31.623  20.645  10.879  1.00 34.56  ? 596 LEU A CB    1 
ATOM   4686 C  CG    . LEU A 1 596 ? 30.340  20.006  11.417  1.00 33.90  ? 596 LEU A CG    1 
ATOM   4687 C  CD1   . LEU A 1 596 ? 29.310  21.082  11.725  1.00 38.62  ? 596 LEU A CD1   1 
ATOM   4688 C  CD2   . LEU A 1 596 ? 29.778  18.995  10.433  1.00 31.08  ? 596 LEU A CD2   1 
ATOM   4689 N  N     . GLU A 1 597 ? 34.750  21.161  10.415  1.00 36.07  ? 597 GLU A N     1 
ATOM   4690 C  CA    . GLU A 1 597 ? 35.784  21.925  9.724   1.00 40.70  ? 597 GLU A CA    1 
ATOM   4691 C  C     . GLU A 1 597 ? 36.714  21.012  8.937   1.00 46.47  ? 597 GLU A C     1 
ATOM   4692 O  O     . GLU A 1 597 ? 37.080  21.319  7.796   1.00 47.26  ? 597 GLU A O     1 
ATOM   4693 C  CB    . GLU A 1 597 ? 36.580  22.765  10.724  1.00 42.14  ? 597 GLU A CB    1 
ATOM   4694 C  CG    . GLU A 1 597 ? 37.756  23.504  10.104  1.00 54.23  ? 597 GLU A CG    1 
ATOM   4695 C  CD    . GLU A 1 597 ? 38.568  24.279  11.125  1.00 68.01  ? 597 GLU A CD    1 
ATOM   4696 O  OE1   . GLU A 1 597 ? 38.213  24.248  12.322  1.00 71.30  ? 597 GLU A OE1   1 
ATOM   4697 O  OE2   . GLU A 1 597 ? 39.564  24.920  10.728  1.00 72.06  ? 597 GLU A OE2   1 
ATOM   4698 N  N     . ASP A 1 598 ? 37.104  19.880  9.525   1.00 42.11  ? 598 ASP A N     1 
ATOM   4699 C  CA    . ASP A 1 598 ? 38.049  18.996  8.854   1.00 44.65  ? 598 ASP A CA    1 
ATOM   4700 C  C     . ASP A 1 598 ? 37.373  18.135  7.793   1.00 39.90  ? 598 ASP A C     1 
ATOM   4701 O  O     . ASP A 1 598 ? 37.909  17.976  6.693   1.00 44.18  ? 598 ASP A O     1 
ATOM   4702 C  CB    . ASP A 1 598 ? 38.760  18.107  9.874   1.00 41.12  ? 598 ASP A CB    1 
ATOM   4703 C  CG    . ASP A 1 598 ? 39.652  17.072  9.217   1.00 50.80  ? 598 ASP A CG    1 
ATOM   4704 O  OD1   . ASP A 1 598 ? 40.570  17.469  8.470   1.00 57.56  ? 598 ASP A OD1   1 
ATOM   4705 O  OD2   . ASP A 1 598 ? 39.435  15.862  9.445   1.00 54.88  ? 598 ASP A OD2   1 
ATOM   4706 N  N     . GLN A 1 599 ? 36.202  17.579  8.098   1.00 36.84  ? 599 GLN A N     1 
ATOM   4707 C  CA    . GLN A 1 599 ? 35.606  16.563  7.239   1.00 37.52  ? 599 GLN A CA    1 
ATOM   4708 C  C     . GLN A 1 599 ? 34.780  17.137  6.095   1.00 42.85  ? 599 GLN A C     1 
ATOM   4709 O  O     . GLN A 1 599 ? 34.726  16.527  5.020   1.00 44.60  ? 599 GLN A O     1 
ATOM   4710 C  CB    . GLN A 1 599 ? 34.738  15.617  8.073   1.00 37.58  ? 599 GLN A CB    1 
ATOM   4711 C  CG    . GLN A 1 599 ? 35.537  14.702  8.985   1.00 40.29  ? 599 GLN A CG    1 
ATOM   4712 C  CD    . GLN A 1 599 ? 36.428  13.749  8.213   1.00 45.48  ? 599 GLN A CD    1 
ATOM   4713 O  OE1   . GLN A 1 599 ? 35.976  13.066  7.294   1.00 45.65  ? 599 GLN A OE1   1 
ATOM   4714 N  NE2   . GLN A 1 599 ? 37.705  13.704  8.577   1.00 47.84  ? 599 GLN A NE2   1 
ATOM   4715 N  N     . VAL A 1 600 ? 34.128  18.278  6.289   1.00 36.26  ? 600 VAL A N     1 
ATOM   4716 C  CA    . VAL A 1 600 ? 33.308  18.880  5.245   1.00 39.66  ? 600 VAL A CA    1 
ATOM   4717 C  C     . VAL A 1 600 ? 34.023  20.044  4.571   1.00 41.99  ? 600 VAL A C     1 
ATOM   4718 O  O     . VAL A 1 600 ? 33.875  20.248  3.365   1.00 40.05  ? 600 VAL A O     1 
ATOM   4719 C  CB    . VAL A 1 600 ? 31.941  19.311  5.818   1.00 41.51  ? 600 VAL A CB    1 
ATOM   4720 C  CG1   . VAL A 1 600 ? 30.937  19.496  4.694   1.00 39.70  ? 600 VAL A CG1   1 
ATOM   4721 C  CG2   . VAL A 1 600 ? 31.437  18.277  6.808   1.00 37.49  ? 600 VAL A CG2   1 
ATOM   4722 N  N     . ASN A 1 601 ? 34.793  20.817  5.339   1.00 41.40  ? 601 ASN A N     1 
ATOM   4723 C  CA    . ASN A 1 601 ? 35.786  21.761  4.813   1.00 42.36  ? 601 ASN A CA    1 
ATOM   4724 C  C     . ASN A 1 601 ? 35.093  22.784  3.918   1.00 45.99  ? 601 ASN A C     1 
ATOM   4725 O  O     . ASN A 1 601 ? 34.163  23.459  4.392   1.00 43.92  ? 601 ASN A O     1 
ATOM   4726 C  CB    . ASN A 1 601 ? 36.902  20.946  4.155   1.00 44.51  ? 601 ASN A CB    1 
ATOM   4727 C  CG    . ASN A 1 601 ? 38.120  21.784  3.823   1.00 56.55  ? 601 ASN A CG    1 
ATOM   4728 O  OD1   . ASN A 1 601 ? 38.293  22.884  4.349   1.00 60.26  ? 601 ASN A OD1   1 
ATOM   4729 N  ND2   . ASN A 1 601 ? 38.975  21.265  2.948   1.00 53.30  ? 601 ASN A ND2   1 
ATOM   4730 N  N     . ALA A 1 602 ? 35.490  22.939  2.653   1.00 44.59  ? 602 ALA A N     1 
ATOM   4731 C  CA    . ALA A 1 602 ? 34.939  23.975  1.788   1.00 42.91  ? 602 ALA A CA    1 
ATOM   4732 C  C     . ALA A 1 602 ? 33.553  23.642  1.253   1.00 44.01  ? 602 ALA A C     1 
ATOM   4733 O  O     . ALA A 1 602 ? 32.950  24.484  0.579   1.00 44.14  ? 602 ALA A O     1 
ATOM   4734 C  CB    . ALA A 1 602 ? 35.887  24.237  0.615   1.00 44.10  ? 602 ALA A CB    1 
ATOM   4735 N  N     . ASP A 1 603 ? 33.036  22.446  1.526   1.00 41.37  ? 603 ASP A N     1 
ATOM   4736 C  CA    . ASP A 1 603 ? 31.698  22.057  1.106   1.00 41.67  ? 603 ASP A CA    1 
ATOM   4737 C  C     . ASP A 1 603 ? 30.666  22.230  2.212   1.00 37.99  ? 603 ASP A C     1 
ATOM   4738 O  O     . ASP A 1 603 ? 29.504  21.860  2.024   1.00 31.22  ? 603 ASP A O     1 
ATOM   4739 C  CB    . ASP A 1 603 ? 31.698  20.609  0.611   1.00 41.84  ? 603 ASP A CB    1 
ATOM   4740 C  CG    . ASP A 1 603 ? 32.303  20.466  -0.776  1.00 52.04  ? 603 ASP A CG    1 
ATOM   4741 O  OD1   . ASP A 1 603 ? 31.968  21.283  -1.661  1.00 51.23  ? 603 ASP A OD1   1 
ATOM   4742 O  OD2   . ASP A 1 603 ? 33.115  19.540  -0.979  1.00 45.72  ? 603 ASP A OD2   1 
ATOM   4743 N  N     . LEU A 1 604 ? 31.060  22.783  3.354   1.00 35.66  ? 604 LEU A N     1 
ATOM   4744 C  CA    . LEU A 1 604 ? 30.132  22.974  4.461   1.00 34.97  ? 604 LEU A CA    1 
ATOM   4745 C  C     . LEU A 1 604 ? 29.217  24.155  4.166   1.00 34.45  ? 604 LEU A C     1 
ATOM   4746 O  O     . LEU A 1 604 ? 29.709  25.275  3.992   1.00 35.65  ? 604 LEU A O     1 
ATOM   4747 C  CB    . LEU A 1 604 ? 30.891  23.211  5.762   1.00 38.73  ? 604 LEU A CB    1 
ATOM   4748 C  CG    . LEU A 1 604 ? 30.048  23.451  7.018   1.00 37.44  ? 604 LEU A CG    1 
ATOM   4749 C  CD1   . LEU A 1 604 ? 29.211  22.228  7.360   1.00 32.68  ? 604 LEU A CD1   1 
ATOM   4750 C  CD2   . LEU A 1 604 ? 30.931  23.847  8.192   1.00 38.57  ? 604 LEU A CD2   1 
ATOM   4751 N  N     . PRO A 1 605 ? 27.901  23.955  4.087   1.00 37.53  ? 605 PRO A N     1 
ATOM   4752 C  CA    . PRO A 1 605 ? 27.003  25.081  3.810   1.00 34.12  ? 605 PRO A CA    1 
ATOM   4753 C  C     . PRO A 1 605 ? 27.063  26.118  4.920   1.00 36.12  ? 605 PRO A C     1 
ATOM   4754 O  O     . PRO A 1 605 ? 27.237  25.793  6.097   1.00 37.36  ? 605 PRO A O     1 
ATOM   4755 C  CB    . PRO A 1 605 ? 25.619  24.424  3.729   1.00 36.93  ? 605 PRO A CB    1 
ATOM   4756 C  CG    . PRO A 1 605 ? 25.895  22.977  3.447   1.00 30.79  ? 605 PRO A CG    1 
ATOM   4757 C  CD    . PRO A 1 605 ? 27.177  22.676  4.163   1.00 32.76  ? 605 PRO A CD    1 
ATOM   4758 N  N     . TYR A 1 606 ? 26.921  27.386  4.527   1.00 36.49  ? 606 TYR A N     1 
ATOM   4759 C  CA    . TYR A 1 606 ? 27.055  28.478  5.486   1.00 39.06  ? 606 TYR A CA    1 
ATOM   4760 C  C     . TYR A 1 606 ? 25.982  28.413  6.567   1.00 38.96  ? 606 TYR A C     1 
ATOM   4761 O  O     . TYR A 1 606 ? 26.241  28.753  7.727   1.00 37.25  ? 606 TYR A O     1 
ATOM   4762 C  CB    . TYR A 1 606 ? 27.004  29.822  4.763   1.00 40.44  ? 606 TYR A CB    1 
ATOM   4763 C  CG    . TYR A 1 606 ? 26.821  30.997  5.695   1.00 45.63  ? 606 TYR A CG    1 
ATOM   4764 C  CD1   . TYR A 1 606 ? 27.873  31.462  6.472   1.00 48.12  ? 606 TYR A CD1   1 
ATOM   4765 C  CD2   . TYR A 1 606 ? 25.593  31.635  5.804   1.00 46.25  ? 606 TYR A CD2   1 
ATOM   4766 C  CE1   . TYR A 1 606 ? 27.706  32.536  7.329   1.00 55.29  ? 606 TYR A CE1   1 
ATOM   4767 C  CE2   . TYR A 1 606 ? 25.418  32.708  6.654   1.00 49.91  ? 606 TYR A CE2   1 
ATOM   4768 C  CZ    . TYR A 1 606 ? 26.476  33.155  7.415   1.00 48.90  ? 606 TYR A CZ    1 
ATOM   4769 O  OH    . TYR A 1 606 ? 26.299  34.224  8.263   1.00 64.71  ? 606 TYR A OH    1 
ATOM   4770 N  N     . GLU A 1 607 ? 24.771  27.980  6.209   1.00 31.00  ? 607 GLU A N     1 
ATOM   4771 C  CA    . GLU A 1 607 ? 23.698  27.918  7.196   1.00 39.88  ? 607 GLU A CA    1 
ATOM   4772 C  C     . GLU A 1 607 ? 23.989  26.896  8.288   1.00 37.34  ? 607 GLU A C     1 
ATOM   4773 O  O     . GLU A 1 607 ? 23.484  27.031  9.408   1.00 35.57  ? 607 GLU A O     1 
ATOM   4774 C  CB    . GLU A 1 607 ? 22.367  27.613  6.511   1.00 40.08  ? 607 GLU A CB    1 
ATOM   4775 C  CG    . GLU A 1 607 ? 21.831  28.778  5.691   1.00 49.00  ? 607 GLU A CG    1 
ATOM   4776 C  CD    . GLU A 1 607 ? 20.423  28.544  5.181   1.00 54.87  ? 607 GLU A CD    1 
ATOM   4777 O  OE1   . GLU A 1 607 ? 20.100  27.395  4.817   1.00 49.77  ? 607 GLU A OE1   1 
ATOM   4778 O  OE2   . GLU A 1 607 ? 19.637  29.513  5.147   1.00 73.06  ? 607 GLU A OE2   1 
ATOM   4779 N  N     . ILE A 1 608 ? 24.795  25.875  7.990   1.00 32.78  ? 608 ILE A N     1 
ATOM   4780 C  CA    . ILE A 1 608 ? 25.219  24.948  9.034   1.00 31.48  ? 608 ILE A CA    1 
ATOM   4781 C  C     . ILE A 1 608 ? 26.257  25.604  9.934   1.00 33.49  ? 608 ILE A C     1 
ATOM   4782 O  O     . ILE A 1 608 ? 26.207  25.471  11.164  1.00 35.30  ? 608 ILE A O     1 
ATOM   4783 C  CB    . ILE A 1 608 ? 25.751  23.643  8.413   1.00 32.59  ? 608 ILE A CB    1 
ATOM   4784 C  CG1   . ILE A 1 608 ? 24.670  22.972  7.563   1.00 27.20  ? 608 ILE A CG1   1 
ATOM   4785 C  CG2   . ILE A 1 608 ? 26.228  22.694  9.501   1.00 31.24  ? 608 ILE A CG2   1 
ATOM   4786 C  CD1   . ILE A 1 608 ? 23.479  22.493  8.364   1.00 29.16  ? 608 ILE A CD1   1 
ATOM   4787 N  N     . GLU A 1 609 ? 27.214  26.324  9.341   1.00 31.66  ? 609 GLU A N     1 
ATOM   4788 C  CA    . GLU A 1 609 ? 28.202  27.041  10.139  1.00 38.15  ? 609 GLU A CA    1 
ATOM   4789 C  C     . GLU A 1 609 ? 27.540  28.098  11.015  1.00 34.57  ? 609 GLU A C     1 
ATOM   4790 O  O     . GLU A 1 609 ? 27.958  28.321  12.157  1.00 37.46  ? 609 GLU A O     1 
ATOM   4791 C  CB    . GLU A 1 609 ? 29.252  27.683  9.231   1.00 35.72  ? 609 GLU A CB    1 
ATOM   4792 C  CG    . GLU A 1 609 ? 30.349  28.419  9.986   1.00 49.71  ? 609 GLU A CG    1 
ATOM   4793 C  CD    . GLU A 1 609 ? 31.253  29.225  9.072   1.00 58.05  ? 609 GLU A CD    1 
ATOM   4794 O  OE1   . GLU A 1 609 ? 31.151  29.067  7.837   1.00 59.58  ? 609 GLU A OE1   1 
ATOM   4795 O  OE2   . GLU A 1 609 ? 32.062  30.023  9.590   1.00 63.99  ? 609 GLU A OE2   1 
ATOM   4796 N  N     . ARG A 1 610 ? 26.498  28.755  10.497  1.00 32.03  ? 610 ARG A N     1 
ATOM   4797 C  CA    . ARG A 1 610 ? 25.799  29.770  11.278  1.00 36.09  ? 610 ARG A CA    1 
ATOM   4798 C  C     . ARG A 1 610 ? 25.108  29.155  12.489  1.00 33.74  ? 610 ARG A C     1 
ATOM   4799 O  O     . ARG A 1 610 ? 25.074  29.760  13.568  1.00 37.49  ? 610 ARG A O     1 
ATOM   4800 C  CB    . ARG A 1 610 ? 24.791  30.507  10.398  1.00 39.67  ? 610 ARG A CB    1 
ATOM   4801 C  CG    . ARG A 1 610 ? 23.997  31.583  11.123  1.00 40.40  ? 610 ARG A CG    1 
ATOM   4802 C  CD    . ARG A 1 610 ? 23.152  32.394  10.152  1.00 42.00  ? 610 ARG A CD    1 
ATOM   4803 N  NE    . ARG A 1 610 ? 22.193  31.563  9.432   1.00 45.65  ? 610 ARG A NE    1 
ATOM   4804 C  CZ    . ARG A 1 610 ? 21.424  31.996  8.442   1.00 47.92  ? 610 ARG A CZ    1 
ATOM   4805 N  NH1   . ARG A 1 610 ? 21.482  33.248  8.019   1.00 49.20  ? 610 ARG A NH1   1 
ATOM   4806 N  NH2   . ARG A 1 610 ? 20.578  31.151  7.860   1.00 48.60  ? 610 ARG A NH2   1 
ATOM   4807 N  N     . GLU A 1 611 ? 24.551  27.952  12.330  1.00 33.74  ? 611 GLU A N     1 
ATOM   4808 C  CA    . GLU A 1 611 ? 23.940  27.269  13.465  1.00 32.95  ? 611 GLU A CA    1 
ATOM   4809 C  C     . GLU A 1 611 ? 24.992  26.850  14.483  1.00 36.62  ? 611 GLU A C     1 
ATOM   4810 O  O     . GLU A 1 611 ? 24.760  26.931  15.694  1.00 34.45  ? 611 GLU A O     1 
ATOM   4811 C  CB    . GLU A 1 611 ? 23.142  26.058  12.986  1.00 32.20  ? 611 GLU A CB    1 
ATOM   4812 C  CG    . GLU A 1 611 ? 21.901  26.416  12.189  1.00 32.19  ? 611 GLU A CG    1 
ATOM   4813 C  CD    . GLU A 1 611 ? 20.947  27.296  12.972  1.00 33.80  ? 611 GLU A CD    1 
ATOM   4814 O  OE1   . GLU A 1 611 ? 20.783  27.071  14.190  1.00 34.16  ? 611 GLU A OE1   1 
ATOM   4815 O  OE2   . GLU A 1 611 ? 20.368  28.222  12.371  1.00 40.42  ? 611 GLU A OE2   1 
ATOM   4816 N  N     . LEU A 1 612 ? 26.154  26.397  14.007  1.00 34.60  ? 612 LEU A N     1 
ATOM   4817 C  CA    . LEU A 1 612 ? 27.254  26.084  14.912  1.00 33.51  ? 612 LEU A CA    1 
ATOM   4818 C  C     . LEU A 1 612 ? 27.655  27.308  15.726  1.00 39.17  ? 612 LEU A C     1 
ATOM   4819 O  O     . LEU A 1 612 ? 27.849  27.222  16.944  1.00 34.63  ? 612 LEU A O     1 
ATOM   4820 C  CB    . LEU A 1 612 ? 28.444  25.547  14.116  1.00 32.12  ? 612 LEU A CB    1 
ATOM   4821 C  CG    . LEU A 1 612 ? 29.687  25.169  14.924  1.00 46.28  ? 612 LEU A CG    1 
ATOM   4822 C  CD1   . LEU A 1 612 ? 29.384  24.010  15.860  1.00 35.75  ? 612 LEU A CD1   1 
ATOM   4823 C  CD2   . LEU A 1 612 ? 30.849  24.835  14.001  1.00 46.29  ? 612 LEU A CD2   1 
ATOM   4824 N  N     . ARG A 1 613 ? 27.771  28.466  15.068  1.00 37.18  ? 613 ARG A N     1 
ATOM   4825 C  CA    . ARG A 1 613 ? 28.149  29.682  15.781  1.00 36.46  ? 613 ARG A CA    1 
ATOM   4826 C  C     . ARG A 1 613 ? 27.060  30.118  16.751  1.00 35.84  ? 613 ARG A C     1 
ATOM   4827 O  O     . ARG A 1 613 ? 27.359  30.618  17.842  1.00 35.89  ? 613 ARG A O     1 
ATOM   4828 C  CB    . ARG A 1 613 ? 28.450  30.808  14.792  1.00 35.65  ? 613 ARG A CB    1 
ATOM   4829 C  CG    . ARG A 1 613 ? 29.651  30.563  13.902  1.00 39.21  ? 613 ARG A CG    1 
ATOM   4830 C  CD    . ARG A 1 613 ? 30.024  31.828  13.160  1.00 51.76  ? 613 ARG A CD    1 
ATOM   4831 N  NE    . ARG A 1 613 ? 31.206  31.650  12.328  1.00 63.15  ? 613 ARG A NE    1 
ATOM   4832 C  CZ    . ARG A 1 613 ? 31.971  32.643  11.897  1.00 63.06  ? 613 ARG A CZ    1 
ATOM   4833 N  NH1   . ARG A 1 613 ? 31.721  33.900  12.228  1.00 59.49  ? 613 ARG A NH1   1 
ATOM   4834 N  NH2   . ARG A 1 613 ? 33.015  32.368  11.121  1.00 70.03  ? 613 ARG A NH2   1 
ATOM   4835 N  N     . ALA A 1 614 ? 25.794  29.953  16.366  1.00 32.01  ? 614 ALA A N     1 
ATOM   4836 C  CA    . ALA A 1 614 ? 24.695  30.338  17.246  1.00 33.85  ? 614 ALA A CA    1 
ATOM   4837 C  C     . ALA A 1 614 ? 24.662  29.467  18.497  1.00 38.80  ? 614 ALA A C     1 
ATOM   4838 O  O     . ALA A 1 614 ? 24.509  29.974  19.614  1.00 38.74  ? 614 ALA A O     1 
ATOM   4839 C  CB    . ALA A 1 614 ? 23.365  30.256  16.494  1.00 33.60  ? 614 ALA A CB    1 
ATOM   4840 N  N     . LEU A 1 615 ? 24.810  28.149  18.329  1.00 36.43  ? 615 LEU A N     1 
ATOM   4841 C  CA    . LEU A 1 615 ? 24.836  27.257  19.483  1.00 30.38  ? 615 LEU A CA    1 
ATOM   4842 C  C     . LEU A 1 615 ? 26.025  27.560  20.386  1.00 39.63  ? 615 LEU A C     1 
ATOM   4843 O  O     . LEU A 1 615 ? 25.892  27.578  21.616  1.00 35.48  ? 615 LEU A O     1 
ATOM   4844 C  CB    . LEU A 1 615 ? 24.870  25.799  19.023  1.00 37.67  ? 615 LEU A CB    1 
ATOM   4845 C  CG    . LEU A 1 615 ? 24.954  24.747  20.133  1.00 39.03  ? 615 LEU A CG    1 
ATOM   4846 C  CD1   . LEU A 1 615 ? 23.833  24.940  21.142  1.00 38.14  ? 615 LEU A CD1   1 
ATOM   4847 C  CD2   . LEU A 1 615 ? 24.916  23.340  19.551  1.00 33.63  ? 615 LEU A CD2   1 
ATOM   4848 N  N     . LYS A 1 616 ? 27.195  27.809  19.792  1.00 36.07  ? 616 LYS A N     1 
ATOM   4849 C  CA    . LYS A 1 616 ? 28.371  28.133  20.590  1.00 39.42  ? 616 LYS A CA    1 
ATOM   4850 C  C     . LYS A 1 616 ? 28.148  29.401  21.404  1.00 44.87  ? 616 LYS A C     1 
ATOM   4851 O  O     . LYS A 1 616 ? 28.632  29.516  22.536  1.00 42.42  ? 616 LYS A O     1 
ATOM   4852 C  CB    . LYS A 1 616 ? 29.592  28.277  19.678  1.00 43.76  ? 616 LYS A CB    1 
ATOM   4853 C  CG    . LYS A 1 616 ? 30.908  28.433  20.415  1.00 45.81  ? 616 LYS A CG    1 
ATOM   4854 C  CD    . LYS A 1 616 ? 31.997  27.592  19.769  1.00 61.40  ? 616 LYS A CD    1 
ATOM   4855 C  CE    . LYS A 1 616 ? 33.255  27.568  20.628  1.00 67.37  ? 616 LYS A CE    1 
ATOM   4856 N  NZ    . LYS A 1 616 ? 34.220  26.525  20.177  1.00 65.60  ? 616 LYS A NZ    1 
ATOM   4857 N  N     . GLN A 1 617 ? 27.399  30.357  20.850  1.00 40.10  ? 617 GLN A N     1 
ATOM   4858 C  CA    . GLN A 1 617 ? 27.141  31.599  21.568  1.00 43.11  ? 617 GLN A CA    1 
ATOM   4859 C  C     . GLN A 1 617 ? 26.142  31.393  22.702  1.00 41.97  ? 617 GLN A C     1 
ATOM   4860 O  O     . GLN A 1 617 ? 26.332  31.918  23.804  1.00 41.99  ? 617 GLN A O     1 
ATOM   4861 C  CB    . GLN A 1 617 ? 26.646  32.672  20.598  1.00 40.83  ? 617 GLN A CB    1 
ATOM   4862 C  CG    . GLN A 1 617 ? 26.420  34.027  21.240  1.00 43.38  ? 617 GLN A CG    1 
ATOM   4863 C  CD    . GLN A 1 617 ? 27.714  34.718  21.626  1.00 44.77  ? 617 GLN A CD    1 
ATOM   4864 O  OE1   . GLN A 1 617 ? 28.796  34.333  21.184  1.00 52.91  ? 617 GLN A OE1   1 
ATOM   4865 N  NE2   . GLN A 1 617 ? 27.607  35.748  22.453  1.00 44.60  ? 617 GLN A NE2   1 
ATOM   4866 N  N     . ARG A 1 618 ? 25.072  30.632  22.454  1.00 40.23  ? 618 ARG A N     1 
ATOM   4867 C  CA    . ARG A 1 618 ? 24.076  30.388  23.495  1.00 46.14  ? 618 ARG A CA    1 
ATOM   4868 C  C     . ARG A 1 618 ? 24.665  29.637  24.683  1.00 46.36  ? 618 ARG A C     1 
ATOM   4869 O  O     . ARG A 1 618 ? 24.258  29.869  25.827  1.00 46.69  ? 618 ARG A O     1 
ATOM   4870 C  CB    . ARG A 1 618 ? 22.892  29.612  22.923  1.00 37.38  ? 618 ARG A CB    1 
ATOM   4871 C  CG    . ARG A 1 618 ? 22.143  30.344  21.824  1.00 39.91  ? 618 ARG A CG    1 
ATOM   4872 C  CD    . ARG A 1 618 ? 20.787  29.710  21.548  1.00 32.24  ? 618 ARG A CD    1 
ATOM   4873 N  NE    . ARG A 1 618 ? 20.895  28.348  21.039  1.00 34.99  ? 618 ARG A NE    1 
ATOM   4874 C  CZ    . ARG A 1 618 ? 21.083  28.037  19.764  1.00 34.36  ? 618 ARG A CZ    1 
ATOM   4875 N  NH1   . ARG A 1 618 ? 21.224  28.972  18.838  1.00 39.49  ? 618 ARG A NH1   1 
ATOM   4876 N  NH2   . ARG A 1 618 ? 21.133  26.757  19.408  1.00 33.77  ? 618 ARG A NH2   1 
ATOM   4877 N  N     . ILE A 1 619 ? 25.612  28.732  24.434  1.00 44.79  ? 619 ILE A N     1 
ATOM   4878 C  CA    . ILE A 1 619 ? 26.219  27.977  25.525  1.00 47.95  ? 619 ILE A CA    1 
ATOM   4879 C  C     . ILE A 1 619 ? 27.144  28.869  26.343  1.00 47.25  ? 619 ILE A C     1 
ATOM   4880 O  O     . ILE A 1 619 ? 27.208  28.759  27.574  1.00 52.28  ? 619 ILE A O     1 
ATOM   4881 C  CB    . ILE A 1 619 ? 26.953  26.744  24.967  1.00 46.32  ? 619 ILE A CB    1 
ATOM   4882 C  CG1   . ILE A 1 619 ? 25.944  25.789  24.325  1.00 41.17  ? 619 ILE A CG1   1 
ATOM   4883 C  CG2   . ILE A 1 619 ? 27.752  26.040  26.060  1.00 48.99  ? 619 ILE A CG2   1 
ATOM   4884 C  CD1   . ILE A 1 619 ? 26.571  24.603  23.651  1.00 53.09  ? 619 ILE A CD1   1 
ATOM   4885 N  N     . SER A 1 620 ? 27.866  29.775  25.678  1.00 47.20  ? 620 SER A N     1 
ATOM   4886 C  CA    . SER A 1 620 ? 28.769  30.669  26.396  1.00 51.61  ? 620 SER A CA    1 
ATOM   4887 C  C     . SER A 1 620 ? 28.012  31.624  27.310  1.00 51.52  ? 620 SER A C     1 
ATOM   4888 O  O     . SER A 1 620 ? 28.565  32.086  28.315  1.00 56.23  ? 620 SER A O     1 
ATOM   4889 C  CB    . SER A 1 620 ? 29.629  31.455  25.405  1.00 53.96  ? 620 SER A CB    1 
ATOM   4890 O  OG    . SER A 1 620 ? 28.838  32.344  24.636  1.00 51.86  ? 620 SER A OG    1 
ATOM   4891 N  N     . GLN A 1 621 ? 26.756  31.929  26.984  1.00 53.56  ? 621 GLN A N     1 
ATOM   4892 C  CA    . GLN A 1 621 ? 25.958  32.836  27.798  1.00 53.14  ? 621 GLN A CA    1 
ATOM   4893 C  C     . GLN A 1 621 ? 25.391  32.176  29.048  1.00 58.33  ? 621 GLN A C     1 
ATOM   4894 O  O     . GLN A 1 621 ? 24.852  32.882  29.907  1.00 65.92  ? 621 GLN A O     1 
ATOM   4895 C  CB    . GLN A 1 621 ? 24.814  33.420  26.964  1.00 51.78  ? 621 GLN A CB    1 
ATOM   4896 C  CG    . GLN A 1 621 ? 25.274  34.269  25.789  1.00 50.28  ? 621 GLN A CG    1 
ATOM   4897 C  CD    . GLN A 1 621 ? 26.028  35.509  26.222  1.00 61.17  ? 621 GLN A CD    1 
ATOM   4898 O  OE1   . GLN A 1 621 ? 25.605  36.222  27.133  1.00 68.50  ? 621 GLN A OE1   1 
ATOM   4899 N  NE2   . GLN A 1 621 ? 27.156  35.773  25.573  1.00 66.07  ? 621 GLN A NE2   1 
ATOM   4900 N  N     . MET A 1 622 ? 25.495  30.855  29.171  1.00 60.24  ? 622 MET A N     1 
ATOM   4901 C  CA    . MET A 1 622 ? 24.992  30.147  30.346  1.00 61.25  ? 622 MET A CA    1 
ATOM   4902 C  C     . MET A 1 622 ? 25.754  30.550  31.602  1.00 63.89  ? 622 MET A C     1 
ATOM   4903 O  O     . MET A 1 622 ? 26.959  30.794  31.556  1.00 67.41  ? 622 MET A O     1 
ATOM   4904 C  CB    . MET A 1 622 ? 25.090  28.632  30.149  1.00 61.71  ? 622 MET A CB    1 
ATOM   4905 C  CG    . MET A 1 622 ? 24.235  28.084  29.025  1.00 54.90  ? 622 MET A CG    1 
ATOM   4906 S  SD    . MET A 1 622 ? 24.375  26.293  28.891  1.00 58.79  ? 622 MET A SD    1 
ATOM   4907 C  CE    . MET A 1 622 ? 23.740  25.782  30.487  1.00 55.59  ? 622 MET A CE    1 
ATOM   4908 O  OXT   . MET A 1 622 ? 25.185  30.633  32.690  1.00 73.78  ? 622 MET A OXT   1 
HETATM 4909 MN MN    . MN  B 2 .   ? 16.649  -2.662  12.421  1.00 32.22  ? 701 MN  A MN    1 
HETATM 4910 MN MN    . MN  C 2 .   ? 20.065  -0.282  9.280   1.00 26.20  ? 702 MN  A MN    1 
HETATM 4911 MN MN    . MN  D 2 .   ? 18.245  28.476  2.877   1.00 98.96  ? 703 MN  A MN    1 
HETATM 4912 C  C1    . OXL E 3 .   ? 21.467  -2.800  9.216   1.00 31.80  ? 704 OXL A C1    1 
HETATM 4913 C  C2    . OXL E 3 .   ? 22.639  -1.857  9.554   1.00 28.30  ? 704 OXL A C2    1 
HETATM 4914 O  O1    . OXL E 3 .   ? 20.318  -2.377  9.193   1.00 25.48  ? 704 OXL A O1    1 
HETATM 4915 O  O2    . OXL E 3 .   ? 22.283  -0.624  9.803   1.00 27.45  ? 704 OXL A O2    1 
HETATM 4916 O  O3    . OXL E 3 .   ? 21.824  -4.033  8.956   1.00 30.22  ? 704 OXL A O3    1 
HETATM 4917 O  O4    . OXL E 3 .   ? 23.784  -2.274  9.564   1.00 33.68  ? 704 OXL A O4    1 
HETATM 4918 P  PG    . GTP F 4 .   ? 19.708  -1.758  12.421  1.00 30.76  ? 705 GTP A PG    1 
HETATM 4919 O  O1G   . GTP F 4 .   ? 18.677  -2.803  12.066  1.00 37.25  ? 705 GTP A O1G   1 
HETATM 4920 O  O2G   . GTP F 4 .   ? 21.089  -2.349  12.268  1.00 29.84  ? 705 GTP A O2G   1 
HETATM 4921 O  O3G   . GTP F 4 .   ? 19.565  -0.560  11.510  1.00 26.06  ? 705 GTP A O3G   1 
HETATM 4922 O  O3B   . GTP F 4 .   ? 19.552  -1.315  13.965  1.00 35.77  ? 705 GTP A O3B   1 
HETATM 4923 P  PB    . GTP F 4 .   ? 18.217  -0.757  14.678  1.00 31.23  ? 705 GTP A PB    1 
HETATM 4924 O  O1B   . GTP F 4 .   ? 16.951  -1.303  14.061  1.00 32.69  ? 705 GTP A O1B   1 
HETATM 4925 O  O2B   . GTP F 4 .   ? 18.218  0.755   14.666  1.00 31.14  ? 705 GTP A O2B   1 
HETATM 4926 O  O3A   . GTP F 4 .   ? 18.400  -1.276  16.192  1.00 34.97  ? 705 GTP A O3A   1 
HETATM 4927 P  PA    . GTP F 4 .   ? 17.387  -2.261  16.964  1.00 34.46  ? 705 GTP A PA    1 
HETATM 4928 O  O1A   . GTP F 4 .   ? 17.466  -3.648  16.369  1.00 33.93  ? 705 GTP A O1A   1 
HETATM 4929 O  O2A   . GTP F 4 .   ? 15.972  -1.731  16.986  1.00 32.81  ? 705 GTP A O2A   1 
HETATM 4930 O  "O5'" . GTP F 4 .   ? 18.021  -2.308  18.440  1.00 36.37  ? 705 GTP A "O5'" 1 
HETATM 4931 C  "C5'" . GTP F 4 .   ? 19.404  -2.499  18.637  1.00 28.22  ? 705 GTP A "C5'" 1 
HETATM 4932 C  "C4'" . GTP F 4 .   ? 19.589  -2.993  20.065  1.00 34.65  ? 705 GTP A "C4'" 1 
HETATM 4933 O  "O4'" . GTP F 4 .   ? 19.296  -1.910  20.928  1.00 37.01  ? 705 GTP A "O4'" 1 
HETATM 4934 C  "C3'" . GTP F 4 .   ? 18.614  -4.113  20.387  1.00 37.27  ? 705 GTP A "C3'" 1 
HETATM 4935 O  "O3'" . GTP F 4 .   ? 19.304  -5.237  20.884  1.00 37.53  ? 705 GTP A "O3'" 1 
HETATM 4936 C  "C2'" . GTP F 4 .   ? 17.708  -3.561  21.467  1.00 41.55  ? 705 GTP A "C2'" 1 
HETATM 4937 O  "O2'" . GTP F 4 .   ? 17.543  -4.487  22.515  1.00 47.30  ? 705 GTP A "O2'" 1 
HETATM 4938 C  "C1'" . GTP F 4 .   ? 18.397  -2.292  21.949  1.00 42.16  ? 705 GTP A "C1'" 1 
HETATM 4939 N  N9    . GTP F 4 .   ? 17.370  -1.258  22.173  1.00 39.47  ? 705 GTP A N9    1 
HETATM 4940 C  C8    . GTP F 4 .   ? 16.370  -0.907  21.303  1.00 39.13  ? 705 GTP A C8    1 
HETATM 4941 N  N7    . GTP F 4 .   ? 15.624  0.067   21.873  1.00 33.56  ? 705 GTP A N7    1 
HETATM 4942 C  C5    . GTP F 4 .   ? 16.130  0.338   23.098  1.00 35.88  ? 705 GTP A C5    1 
HETATM 4943 C  C6    . GTP F 4 .   ? 15.750  1.233   24.090  1.00 37.19  ? 705 GTP A C6    1 
HETATM 4944 O  O6    . GTP F 4 .   ? 14.779  1.970   23.926  1.00 34.83  ? 705 GTP A O6    1 
HETATM 4945 N  N1    . GTP F 4 .   ? 16.469  1.294   25.265  1.00 34.84  ? 705 GTP A N1    1 
HETATM 4946 C  C2    . GTP F 4 .   ? 17.555  0.465   25.448  1.00 34.33  ? 705 GTP A C2    1 
HETATM 4947 N  N2    . GTP F 4 .   ? 18.246  0.526   26.584  1.00 43.77  ? 705 GTP A N2    1 
HETATM 4948 N  N3    . GTP F 4 .   ? 17.926  -0.424  24.459  1.00 38.06  ? 705 GTP A N3    1 
HETATM 4949 C  C4    . GTP F 4 .   ? 17.226  -0.489  23.301  1.00 36.68  ? 705 GTP A C4    1 
HETATM 4950 C  C1    . PGE G 5 .   ? 4.744   10.516  -3.145  1.00 55.02  ? 706 PGE A C1    1 
HETATM 4951 O  O1    . PGE G 5 .   ? 4.326   11.040  -4.394  1.00 72.25  ? 706 PGE A O1    1 
HETATM 4952 C  C2    . PGE G 5 .   ? 6.018   9.742   -3.279  1.00 56.14  ? 706 PGE A C2    1 
HETATM 4953 O  O2    . PGE G 5 .   ? 6.344   9.149   -2.031  1.00 55.17  ? 706 PGE A O2    1 
HETATM 4954 C  C3    . PGE G 5 .   ? 7.728   9.233   -1.721  1.00 50.86  ? 706 PGE A C3    1 
HETATM 4955 C  C4    . PGE G 5 .   ? 8.493   8.182   -2.454  1.00 44.80  ? 706 PGE A C4    1 
HETATM 4956 O  O4    . PGE G 5 .   ? 10.740  9.452   -5.778  1.00 50.22  ? 706 PGE A O4    1 
HETATM 4957 C  C6    . PGE G 5 .   ? 10.702  8.124   -5.282  1.00 51.08  ? 706 PGE A C6    1 
HETATM 4958 C  C5    . PGE G 5 .   ? 10.425  8.138   -3.815  1.00 43.08  ? 706 PGE A C5    1 
HETATM 4959 O  O3    . PGE G 5 .   ? 9.171   8.753   -3.563  1.00 49.93  ? 706 PGE A O3    1 
HETATM 4960 O  O     . HOH H 6 .   ? 24.597  -22.915 -24.959 1.00 51.85  ? 801 HOH A O     1 
HETATM 4961 O  O     . HOH H 6 .   ? -2.368  -2.045  11.540  1.00 45.77  ? 802 HOH A O     1 
HETATM 4962 O  O     . HOH H 6 .   ? 21.661  -32.050 -3.242  1.00 46.25  ? 803 HOH A O     1 
HETATM 4963 O  O     . HOH H 6 .   ? 23.595  -4.563  7.440   1.00 38.30  ? 804 HOH A O     1 
HETATM 4964 O  O     . HOH H 6 .   ? 29.854  6.865   3.718   1.00 36.86  ? 805 HOH A O     1 
HETATM 4965 O  O     . HOH H 6 .   ? 43.365  15.165  4.026   1.00 54.52  ? 806 HOH A O     1 
HETATM 4966 O  O     . HOH H 6 .   ? 14.888  -5.578  21.375  1.00 40.21  ? 807 HOH A O     1 
HETATM 4967 O  O     . HOH H 6 .   ? 3.134   3.838   1.320   1.00 44.39  ? 808 HOH A O     1 
HETATM 4968 O  O     . HOH H 6 .   ? 28.711  9.916   -6.020  1.00 45.00  ? 809 HOH A O     1 
HETATM 4969 O  O     . HOH H 6 .   ? 15.831  -3.885  10.641  1.00 29.77  ? 810 HOH A O     1 
HETATM 4970 O  O     . HOH H 6 .   ? 39.410  11.724  11.660  1.00 45.56  ? 811 HOH A O     1 
HETATM 4971 O  O     . HOH H 6 .   ? 6.563   -17.113 -9.889  1.00 46.21  ? 812 HOH A O     1 
HETATM 4972 O  O     . HOH H 6 .   ? 11.280  -15.277 -13.552 1.00 44.92  ? 813 HOH A O     1 
HETATM 4973 O  O     . HOH H 6 .   ? 41.474  5.334   -6.170  1.00 49.61  ? 814 HOH A O     1 
HETATM 4974 O  O     . HOH H 6 .   ? 35.580  19.456  -1.486  1.00 48.83  ? 815 HOH A O     1 
HETATM 4975 O  O     . HOH H 6 .   ? 17.374  -4.132  13.766  1.00 31.04  ? 816 HOH A O     1 
HETATM 4976 O  O     . HOH H 6 .   ? 30.597  5.846   -10.961 1.00 50.39  ? 817 HOH A O     1 
HETATM 4977 O  O     . HOH H 6 .   ? 16.198  -21.704 31.293  1.00 60.36  ? 818 HOH A O     1 
HETATM 4978 O  O     . HOH H 6 .   ? 22.387  16.368  20.773  1.00 32.05  ? 819 HOH A O     1 
HETATM 4979 O  O     . HOH H 6 .   ? 26.291  4.113   16.693  1.00 39.38  ? 820 HOH A O     1 
HETATM 4980 O  O     . HOH H 6 .   ? 10.448  23.719  16.468  1.00 36.80  ? 821 HOH A O     1 
HETATM 4981 O  O     . HOH H 6 .   ? 24.032  32.708  33.621  1.00 61.13  ? 822 HOH A O     1 
HETATM 4982 O  O     . HOH H 6 .   ? 41.125  4.300   8.618   1.00 45.61  ? 823 HOH A O     1 
HETATM 4983 O  O     . HOH H 6 .   ? 24.967  -4.536  9.701   1.00 33.94  ? 824 HOH A O     1 
HETATM 4984 O  O     . HOH H 6 .   ? 5.329   2.191   2.183   1.00 39.90  ? 825 HOH A O     1 
HETATM 4985 O  O     . HOH H 6 .   ? -1.838  10.890  9.395   1.00 44.64  ? 826 HOH A O     1 
HETATM 4986 O  O     . HOH H 6 .   ? 27.684  5.278   14.322  1.00 42.12  ? 827 HOH A O     1 
HETATM 4987 O  O     . HOH H 6 .   ? 30.677  -8.998  -0.542  1.00 38.38  ? 828 HOH A O     1 
HETATM 4988 O  O     . HOH H 6 .   ? 31.149  -3.903  -15.623 1.00 52.78  ? 829 HOH A O     1 
HETATM 4989 O  O     . HOH H 6 .   ? 12.562  -0.591  5.712   1.00 21.29  ? 830 HOH A O     1 
HETATM 4990 O  O     . HOH H 6 .   ? 34.340  -20.246 5.511   1.00 41.76  ? 831 HOH A O     1 
HETATM 4991 O  O     . HOH H 6 .   ? 6.616   -4.704  20.160  1.00 35.69  ? 832 HOH A O     1 
HETATM 4992 O  O     . HOH H 6 .   ? 22.089  26.730  16.401  1.00 34.76  ? 833 HOH A O     1 
HETATM 4993 O  O     . HOH H 6 .   ? 23.809  34.944  8.160   1.00 47.74  ? 834 HOH A O     1 
HETATM 4994 O  O     . HOH H 6 .   ? 10.446  -24.968 10.648  1.00 40.35  ? 835 HOH A O     1 
HETATM 4995 O  O     . HOH H 6 .   ? 30.524  -23.840 -1.188  1.00 50.97  ? 836 HOH A O     1 
HETATM 4996 O  O     . HOH H 6 .   ? 18.133  8.597   28.385  1.00 42.68  ? 837 HOH A O     1 
HETATM 4997 O  O     . HOH H 6 .   ? 23.273  -23.435 -5.338  1.00 42.43  ? 838 HOH A O     1 
HETATM 4998 O  O     . HOH H 6 .   ? 22.880  15.881  17.268  1.00 32.84  ? 839 HOH A O     1 
HETATM 4999 O  O     . HOH H 6 .   ? 22.454  -28.820 22.435  1.00 61.43  ? 840 HOH A O     1 
HETATM 5000 O  O     . HOH H 6 .   ? 17.193  26.210  4.846   1.00 43.21  ? 841 HOH A O     1 
HETATM 5001 O  O     . HOH H 6 .   ? 35.535  14.206  3.884   1.00 38.28  ? 842 HOH A O     1 
HETATM 5002 O  O     . HOH H 6 .   ? 26.312  15.864  19.162  1.00 32.52  ? 843 HOH A O     1 
HETATM 5003 O  O     . HOH H 6 .   ? 20.908  29.043  9.425   1.00 45.52  ? 844 HOH A O     1 
HETATM 5004 O  O     . HOH H 6 .   ? 30.806  -25.936 -21.025 1.00 60.46  ? 845 HOH A O     1 
HETATM 5005 O  O     . HOH H 6 .   ? 3.248   18.158  23.928  1.00 38.68  ? 846 HOH A O     1 
HETATM 5006 O  O     . HOH H 6 .   ? 15.668  -5.949  16.418  1.00 36.42  ? 847 HOH A O     1 
HETATM 5007 O  O     . HOH H 6 .   ? 18.980  10.994  1.031   1.00 28.25  ? 848 HOH A O     1 
HETATM 5008 O  O     . HOH H 6 .   ? 0.822   12.247  9.128   1.00 36.11  ? 849 HOH A O     1 
HETATM 5009 O  O     . HOH H 6 .   ? 18.751  5.675   29.574  1.00 46.57  ? 850 HOH A O     1 
HETATM 5010 O  O     . HOH H 6 .   ? 10.732  -4.473  -2.036  1.00 32.09  ? 851 HOH A O     1 
HETATM 5011 O  O     . HOH H 6 .   ? 28.099  -17.906 2.010   1.00 35.63  ? 852 HOH A O     1 
HETATM 5012 O  O     . HOH H 6 .   ? 30.993  16.384  25.085  1.00 43.81  ? 853 HOH A O     1 
HETATM 5013 O  O     . HOH H 6 .   ? 26.333  -18.658 0.567   1.00 39.47  ? 854 HOH A O     1 
HETATM 5014 O  O     . HOH H 6 .   ? 16.473  -1.055  11.109  1.00 31.38  ? 855 HOH A O     1 
HETATM 5015 O  O     . HOH H 6 .   ? 32.269  -18.501 -5.680  1.00 37.94  ? 856 HOH A O     1 
HETATM 5016 O  O     . HOH H 6 .   ? 18.865  9.131   7.345   1.00 24.83  ? 857 HOH A O     1 
HETATM 5017 O  O     . HOH H 6 .   ? 10.958  -13.584 24.837  1.00 44.47  ? 858 HOH A O     1 
HETATM 5018 O  O     . HOH H 6 .   ? 21.316  22.455  19.625  1.00 31.97  ? 859 HOH A O     1 
HETATM 5019 O  O     . HOH H 6 .   ? 32.237  4.977   7.792   1.00 47.34  ? 860 HOH A O     1 
HETATM 5020 O  O     . HOH H 6 .   ? 16.553  2.838   27.480  1.00 42.31  ? 861 HOH A O     1 
HETATM 5021 O  O     . HOH H 6 .   ? 30.069  1.789   4.628   1.00 31.54  ? 862 HOH A O     1 
HETATM 5022 O  O     . HOH H 6 .   ? 28.018  10.991  25.526  1.00 43.84  ? 863 HOH A O     1 
HETATM 5023 O  O     . HOH H 6 .   ? 8.250   -12.612 0.399   1.00 41.54  ? 864 HOH A O     1 
HETATM 5024 O  O     . HOH H 6 .   ? 21.072  10.552  21.575  1.00 35.29  ? 865 HOH A O     1 
HETATM 5025 O  O     . HOH H 6 .   ? 19.867  19.553  -4.211  1.00 51.59  ? 866 HOH A O     1 
HETATM 5026 O  O     . HOH H 6 .   ? 33.935  9.273   14.074  1.00 42.42  ? 867 HOH A O     1 
HETATM 5027 O  O     . HOH H 6 .   ? 23.193  -4.093  0.935   1.00 27.09  ? 868 HOH A O     1 
HETATM 5028 O  O     . HOH H 6 .   ? 11.863  -30.943 28.727  1.00 44.68  ? 869 HOH A O     1 
HETATM 5029 O  O     . HOH H 6 .   ? 6.384   -1.365  0.672   1.00 38.40  ? 870 HOH A O     1 
HETATM 5030 O  O     . HOH H 6 .   ? 18.025  14.258  22.872  1.00 25.39  ? 871 HOH A O     1 
HETATM 5031 O  O     . HOH H 6 .   ? 28.926  5.036   1.631   1.00 33.11  ? 872 HOH A O     1 
HETATM 5032 O  O     . HOH H 6 .   ? -1.452  3.972   14.736  1.00 37.30  ? 873 HOH A O     1 
HETATM 5033 O  O     . HOH H 6 .   ? 7.307   -2.361  23.014  1.00 37.42  ? 874 HOH A O     1 
HETATM 5034 O  O     . HOH H 6 .   ? 8.414   -14.059 -4.550  1.00 41.07  ? 875 HOH A O     1 
HETATM 5035 O  O     . HOH H 6 .   ? 15.437  -4.293  -19.780 1.00 54.56  ? 876 HOH A O     1 
HETATM 5036 O  O     . HOH H 6 .   ? 3.898   12.142  27.866  1.00 45.88  ? 877 HOH A O     1 
HETATM 5037 O  O     . HOH H 6 .   ? 20.010  12.571  -1.268  1.00 29.99  ? 878 HOH A O     1 
HETATM 5038 O  O     . HOH H 6 .   ? 10.359  -20.510 -13.682 1.00 49.02  ? 879 HOH A O     1 
HETATM 5039 O  O     . HOH H 6 .   ? 7.922   -2.774  25.882  1.00 45.53  ? 880 HOH A O     1 
HETATM 5040 O  O     . HOH H 6 .   ? 28.289  22.274  -0.409  1.00 49.64  ? 881 HOH A O     1 
HETATM 5041 O  O     . HOH H 6 .   ? 28.494  14.257  13.718  1.00 28.24  ? 882 HOH A O     1 
HETATM 5042 O  O     . HOH H 6 .   ? 27.744  1.255   11.433  1.00 46.04  ? 883 HOH A O     1 
HETATM 5043 O  O     . HOH H 6 .   ? 9.375   -22.911 -10.582 1.00 49.14  ? 884 HOH A O     1 
HETATM 5044 O  O     . HOH H 6 .   ? 30.113  11.891  1.533   1.00 30.72  ? 885 HOH A O     1 
HETATM 5045 O  O     . HOH H 6 .   ? 4.760   16.922  5.538   1.00 46.93  ? 886 HOH A O     1 
HETATM 5046 O  O     . HOH H 6 .   ? 11.299  2.540   6.930   1.00 30.02  ? 887 HOH A O     1 
HETATM 5047 O  O     . HOH H 6 .   ? 25.675  -23.076 8.465   1.00 45.89  ? 888 HOH A O     1 
HETATM 5048 O  O     . HOH H 6 .   ? 25.266  -21.787 -6.307  1.00 40.71  ? 889 HOH A O     1 
HETATM 5049 O  O     . HOH H 6 .   ? 5.698   25.777  24.786  1.00 44.89  ? 890 HOH A O     1 
HETATM 5050 O  O     . HOH H 6 .   ? -1.347  7.608   2.899   1.00 47.03  ? 891 HOH A O     1 
HETATM 5051 O  O     . HOH H 6 .   ? 30.186  -7.551  14.604  1.00 42.50  ? 892 HOH A O     1 
HETATM 5052 O  O     . HOH H 6 .   ? 25.934  2.243   14.702  1.00 38.00  ? 893 HOH A O     1 
HETATM 5053 O  O     . HOH H 6 .   ? 14.777  -4.157  7.578   1.00 29.83  ? 894 HOH A O     1 
HETATM 5054 O  O     . HOH H 6 .   ? 26.092  -11.844 12.367  1.00 38.46  ? 895 HOH A O     1 
HETATM 5055 O  O     . HOH H 6 .   ? 11.356  1.775   21.644  1.00 38.35  ? 896 HOH A O     1 
HETATM 5056 O  O     . HOH H 6 .   ? 24.380  4.434   10.786  1.00 29.75  ? 897 HOH A O     1 
HETATM 5057 O  O     . HOH H 6 .   ? 29.213  -2.921  3.387   1.00 31.56  ? 898 HOH A O     1 
HETATM 5058 O  O     . HOH H 6 .   ? 18.694  -13.942 8.762   1.00 27.95  ? 899 HOH A O     1 
HETATM 5059 O  O     . HOH H 6 .   ? 13.922  -6.447  18.281  1.00 35.75  ? 900 HOH A O     1 
HETATM 5060 O  O     . HOH H 6 .   ? 37.427  8.687   0.508   1.00 49.01  ? 901 HOH A O     1 
HETATM 5061 O  O     . HOH H 6 .   ? 8.398   -10.891 2.495   1.00 35.02  ? 902 HOH A O     1 
HETATM 5062 O  O     . HOH H 6 .   ? 11.151  -18.154 -4.885  1.00 33.96  ? 903 HOH A O     1 
HETATM 5063 O  O     . HOH H 6 .   ? 18.315  5.949   19.172  1.00 35.80  ? 904 HOH A O     1 
HETATM 5064 O  O     . HOH H 6 .   ? 39.195  15.117  19.371  1.00 40.69  ? 905 HOH A O     1 
HETATM 5065 O  O     . HOH H 6 .   ? 13.924  2.157   20.436  1.00 33.87  ? 906 HOH A O     1 
HETATM 5066 O  O     . HOH H 6 .   ? 16.088  -4.571  -22.391 1.00 58.98  ? 907 HOH A O     1 
HETATM 5067 O  O     . HOH H 6 .   ? 31.746  -24.030 -14.006 1.00 42.29  ? 908 HOH A O     1 
HETATM 5068 O  O     . HOH H 6 .   ? 26.817  -2.386  2.677   1.00 30.23  ? 909 HOH A O     1 
HETATM 5069 O  O     . HOH H 6 .   ? 23.393  -12.245 6.934   1.00 32.47  ? 910 HOH A O     1 
HETATM 5070 O  O     . HOH H 6 .   ? 24.699  13.569  20.308  1.00 32.24  ? 911 HOH A O     1 
HETATM 5071 O  O     . HOH H 6 .   ? 4.574   19.046  11.382  1.00 45.45  ? 912 HOH A O     1 
HETATM 5072 O  O     . HOH H 6 .   ? 9.740   -29.346 19.371  1.00 54.89  ? 913 HOH A O     1 
HETATM 5073 O  O     . HOH H 6 .   ? 1.814   18.835  10.707  1.00 44.48  ? 914 HOH A O     1 
HETATM 5074 O  O     . HOH H 6 .   ? 27.661  -27.137 -21.359 1.00 53.64  ? 915 HOH A O     1 
HETATM 5075 O  O     . HOH H 6 .   ? 12.081  -23.323 -17.015 1.00 49.14  ? 916 HOH A O     1 
HETATM 5076 O  O     . HOH H 6 .   ? 24.969  17.952  30.015  1.00 49.53  ? 917 HOH A O     1 
HETATM 5077 O  O     . HOH H 6 .   ? 21.057  31.838  19.133  1.00 43.07  ? 918 HOH A O     1 
HETATM 5078 O  O     . HOH H 6 .   ? 31.695  -9.466  6.455   1.00 41.75  ? 919 HOH A O     1 
HETATM 5079 O  O     . HOH H 6 .   ? 24.374  -11.771 22.016  1.00 43.73  ? 920 HOH A O     1 
HETATM 5080 O  O     . HOH H 6 .   ? 19.010  -13.560 6.054   1.00 26.44  ? 921 HOH A O     1 
HETATM 5081 O  O     . HOH H 6 .   ? 32.033  4.393   1.405   1.00 43.95  ? 922 HOH A O     1 
HETATM 5082 O  O     . HOH H 6 .   ? 10.859  -2.833  6.440   1.00 33.22  ? 923 HOH A O     1 
HETATM 5083 O  O     . HOH H 6 .   ? 17.828  -3.816  8.738   1.00 24.43  ? 924 HOH A O     1 
HETATM 5084 O  O     . HOH H 6 .   ? 5.963   -9.102  3.120   1.00 30.81  ? 925 HOH A O     1 
HETATM 5085 O  O     . HOH H 6 .   ? 23.423  -7.008  20.333  1.00 42.39  ? 926 HOH A O     1 
HETATM 5086 O  O     . HOH H 6 .   ? 18.438  7.317   21.549  1.00 32.68  ? 927 HOH A O     1 
HETATM 5087 O  O     . HOH H 6 .   ? 29.119  -0.385  5.341   1.00 31.89  ? 928 HOH A O     1 
HETATM 5088 O  O     . HOH H 6 .   ? 3.981   -19.502 -5.639  1.00 53.19  ? 929 HOH A O     1 
HETATM 5089 O  O     . HOH H 6 .   ? 23.355  12.058  18.624  1.00 33.69  ? 930 HOH A O     1 
HETATM 5090 O  O     . HOH H 6 .   ? 14.544  0.926   -11.996 1.00 49.90  ? 931 HOH A O     1 
HETATM 5091 O  O     . HOH H 6 .   ? 12.081  -18.303 -14.559 1.00 39.44  ? 932 HOH A O     1 
HETATM 5092 O  O     . HOH H 6 .   ? 21.010  -1.510  24.182  1.00 44.23  ? 933 HOH A O     1 
HETATM 5093 O  O     . HOH H 6 .   ? 9.216   -11.814 -3.023  1.00 33.27  ? 934 HOH A O     1 
HETATM 5094 O  O     . HOH H 6 .   ? 3.061   14.727  26.757  1.00 46.25  ? 935 HOH A O     1 
HETATM 5095 O  O     . HOH H 6 .   ? 29.503  -27.978 -19.972 1.00 56.90  ? 936 HOH A O     1 
HETATM 5096 O  O     . HOH H 6 .   ? 32.383  -9.266  9.007   1.00 40.48  ? 937 HOH A O     1 
HETATM 5097 O  O     . HOH H 6 .   ? 11.998  26.654  9.931   1.00 46.40  ? 938 HOH A O     1 
HETATM 5098 O  O     . HOH H 6 .   ? 7.355   -26.495 8.555   1.00 50.26  ? 939 HOH A O     1 
HETATM 5099 O  O     . HOH H 6 .   ? 15.581  -5.052  1.134   1.00 28.61  ? 940 HOH A O     1 
HETATM 5100 O  O     . HOH H 6 .   ? 32.413  3.231   3.520   1.00 43.40  ? 941 HOH A O     1 
HETATM 5101 O  O     . HOH H 6 .   ? 24.316  -5.357  16.201  1.00 45.31  ? 942 HOH A O     1 
HETATM 5102 O  O     . HOH H 6 .   ? 36.671  20.830  0.810   1.00 47.50  ? 943 HOH A O     1 
HETATM 5103 O  O     . HOH H 6 .   ? 24.056  -11.728 10.918  1.00 40.86  ? 944 HOH A O     1 
HETATM 5104 O  O     . HOH H 6 .   ? 9.833   -17.131 3.905   1.00 42.28  ? 945 HOH A O     1 
HETATM 5105 O  O     . HOH H 6 .   ? 26.653  6.034   -4.745  1.00 43.44  ? 946 HOH A O     1 
HETATM 5106 O  O     . HOH H 6 .   ? 17.782  -20.218 -22.546 1.00 49.40  ? 947 HOH A O     1 
HETATM 5107 O  O     . HOH H 6 .   ? 22.485  19.961  19.221  1.00 38.45  ? 948 HOH A O     1 
HETATM 5108 O  O     . HOH H 6 .   ? 6.888   27.019  20.373  1.00 49.76  ? 949 HOH A O     1 
HETATM 5109 O  O     . HOH H 6 .   ? 13.285  -16.383 -17.950 1.00 49.88  ? 950 HOH A O     1 
HETATM 5110 O  O     . HOH H 6 .   ? 29.219  -21.683 -35.685 1.00 55.31  ? 951 HOH A O     1 
HETATM 5111 O  O     . HOH H 6 .   ? 39.738  13.435  -8.473  1.00 55.55  ? 952 HOH A O     1 
HETATM 5112 O  O     . HOH H 6 .   ? 26.542  -22.513 -4.491  1.00 45.24  ? 953 HOH A O     1 
HETATM 5113 O  O     . HOH H 6 .   ? 37.999  15.816  -6.975  1.00 55.35  ? 954 HOH A O     1 
HETATM 5114 O  O     . HOH H 6 .   ? 11.693  21.733  14.035  1.00 37.11  ? 955 HOH A O     1 
HETATM 5115 O  O     . HOH H 6 .   ? 28.724  1.006   14.227  1.00 50.36  ? 956 HOH A O     1 
HETATM 5116 O  O     . HOH H 6 .   ? -1.666  24.252  25.090  1.00 61.16  ? 957 HOH A O     1 
HETATM 5117 O  O     . HOH H 6 .   ? 17.518  -6.217  -0.556  1.00 32.57  ? 958 HOH A O     1 
HETATM 5118 O  O     . HOH H 6 .   ? 28.303  15.394  -5.702  1.00 54.53  ? 959 HOH A O     1 
HETATM 5119 O  O     . HOH H 6 .   ? -0.432  23.323  26.858  1.00 56.92  ? 960 HOH A O     1 
HETATM 5120 O  O     . HOH H 6 .   ? 10.447  22.844  11.781  1.00 47.88  ? 961 HOH A O     1 
HETATM 5121 O  O     . HOH H 6 .   ? 41.093  13.072  -6.548  1.00 58.62  ? 962 HOH A O     1 
HETATM 5122 O  O     . HOH H 6 .   ? 33.063  -3.747  -14.185 1.00 53.55  ? 963 HOH A O     1 
HETATM 5123 O  O     . HOH H 6 .   ? 29.675  17.383  -5.566  1.00 50.46  ? 964 HOH A O     1 
HETATM 5124 O  O     . HOH H 6 .   ? 28.496  -7.443  -18.825 1.00 52.79  ? 965 HOH A O     1 
HETATM 5125 O  O     . HOH H 6 .   ? 27.909  -5.047  -17.355 1.00 61.27  ? 966 HOH A O     1 
HETATM 5126 O  O     . HOH H 6 .   ? 24.432  -25.185 9.908   1.00 54.08  ? 967 HOH A O     1 
HETATM 5127 O  O     . HOH H 6 .   ? 5.116   -21.495 19.197  1.00 56.01  ? 968 HOH A O     1 
HETATM 5128 O  O     . HOH H 6 .   ? 24.280  17.410  19.163  1.00 37.49  ? 969 HOH A O     1 
HETATM 5129 O  O     . HOH H 6 .   ? 26.001  -23.412 -1.930  1.00 47.94  ? 970 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  ? 1.1253 0.7533 0.5201 -0.0970 0.1856  -0.1194 10  ASP A N   
56   C CA  . ASP A 10  ? 1.1440 0.7704 0.5205 -0.0958 0.1450  -0.1150 10  ASP A CA  
57   C C   . ASP A 10  ? 0.9992 0.6669 0.4429 -0.0776 0.1429  -0.1201 10  ASP A C   
58   O O   . ASP A 10  ? 1.0158 0.6764 0.4691 -0.0755 0.1658  -0.1338 10  ASP A O   
59   C CB  . ASP A 10  ? 1.2198 0.8037 0.5411 -0.1116 0.1374  -0.1183 10  ASP A CB  
60   C CG  . ASP A 10  ? 1.1743 0.7587 0.4799 -0.1127 0.0917  -0.1124 10  ASP A CG  
61   O OD1 . ASP A 10  ? 1.1698 0.7854 0.5058 -0.1017 0.0653  -0.1050 10  ASP A OD1 
62   O OD2 . ASP A 10  ? 1.3902 0.9446 0.6559 -0.1254 0.0822  -0.1155 10  ASP A OD2 
63   N N   . PHE A 11  ? 0.8856 0.5979 0.3832 -0.0638 0.1143  -0.1070 11  PHE A N   
64   C CA  . PHE A 11  ? 0.8849 0.6399 0.4531 -0.0461 0.1077  -0.1070 11  PHE A CA  
65   C C   . PHE A 11  ? 0.7836 0.5363 0.3441 -0.0473 0.0766  -0.1068 11  PHE A C   
66   O O   . PHE A 11  ? 0.7144 0.5012 0.3287 -0.0343 0.0648  -0.1037 11  PHE A O   
67   C CB  . PHE A 11  ? 0.7705 0.5730 0.4000 -0.0324 0.0977  -0.0947 11  PHE A CB  
68   C CG  . PHE A 11  ? 0.7987 0.6223 0.4709 -0.0251 0.1296  -0.0983 11  PHE A CG  
69   C CD1 . PHE A 11  ? 0.8141 0.6200 0.4607 -0.0354 0.1534  -0.1004 11  PHE A CD1 
70   C CD2 . PHE A 11  ? 0.7891 0.6497 0.5278 -0.0084 0.1351  -0.0993 11  PHE A CD2 
71   C CE1 . PHE A 11  ? 0.8561 0.6859 0.5503 -0.0295 0.1829  -0.1051 11  PHE A CE1 
72   C CE2 . PHE A 11  ? 0.7231 0.6071 0.5077 -0.0010 0.1607  -0.1025 11  PHE A CE2 
73   C CZ  . PHE A 11  ? 0.6906 0.5618 0.4568 -0.0117 0.1849  -0.1062 11  PHE A CZ  
74   N N   . SER A 12  ? 0.8453 0.5573 0.3388 -0.0639 0.0631  -0.1103 12  SER A N   
75   C CA  . SER A 12  ? 0.8633 0.5752 0.3524 -0.0673 0.0316  -0.1112 12  SER A CA  
76   C C   . SER A 12  ? 0.8424 0.5612 0.3627 -0.0611 0.0461  -0.1227 12  SER A C   
77   O O   . SER A 12  ? 0.8002 0.5413 0.3546 -0.0559 0.0252  -0.1209 12  SER A O   
78   C CB  . SER A 12  ? 0.9752 0.6384 0.3822 -0.0883 0.0152  -0.1145 12  SER A CB  
79   O OG  . SER A 12  ? 1.1095 0.7652 0.4886 -0.0925 -0.0058 -0.1007 12  SER A OG  
80   N N   . ALA A 13  ? 0.8645 0.5624 0.3750 -0.0616 0.0837  -0.1349 13  ALA A N   
81   C CA  . ALA A 13  ? 0.8082 0.5057 0.3450 -0.0549 0.0998  -0.1456 13  ALA A CA  
82   C C   . ALA A 13  ? 0.7576 0.5020 0.3730 -0.0332 0.0990  -0.1376 13  ALA A C   
83   O O   . ALA A 13  ? 0.7606 0.5058 0.3995 -0.0266 0.1045  -0.1429 13  ALA A O   
84   C CB  . ALA A 13  ? 0.8447 0.5071 0.3555 -0.0593 0.1428  -0.1608 13  ALA A CB  
85   N N   . LYS A 14  ? 0.7111 0.4904 0.3630 -0.0231 0.0922  -0.1249 14  LYS A N   
86   C CA  . LYS A 14  ? 0.6913 0.5121 0.4107 -0.0044 0.0897  -0.1168 14  LYS A CA  
87   C C   . LYS A 14  ? 0.5915 0.4389 0.3325 -0.0023 0.0559  -0.1058 14  LYS A C   
88   O O   . LYS A 14  ? 0.5390 0.4185 0.3287 0.0107  0.0516  -0.0980 14  LYS A O   
89   C CB  . LYS A 14  ? 0.6343 0.4776 0.3857 0.0049  0.1077  -0.1121 14  LYS A CB  
90   C CG  . LYS A 14  ? 0.6925 0.5231 0.4535 0.0098  0.1449  -0.1232 14  LYS A CG  
91   C CD  . LYS A 14  ? 0.7553 0.6181 0.5636 0.0203  0.1592  -0.1184 14  LYS A CD  
92   C CE  . LYS A 14  ? 0.7560 0.6252 0.6091 0.0347  0.1872  -0.1259 14  LYS A CE  
93   N NZ  . LYS A 14  ? 0.9295 0.7565 0.7460 0.0261  0.2197  -0.1425 14  LYS A NZ  
94   N N   . VAL A 15  ? 0.5903 0.4246 0.2972 -0.0152 0.0319  -0.1054 15  VAL A N   
95   C CA  . VAL A 15  ? 0.6009 0.4608 0.3327 -0.0135 0.0017  -0.0965 15  VAL A CA  
96   C C   . VAL A 15  ? 0.5697 0.4307 0.3178 -0.0142 -0.0054 -0.1023 15  VAL A C   
97   O O   . VAL A 15  ? 0.6618 0.4966 0.3770 -0.0265 -0.0095 -0.1121 15  VAL A O   
98   C CB  . VAL A 15  ? 0.6249 0.4728 0.3199 -0.0253 -0.0232 -0.0922 15  VAL A CB  
99   C CG1 . VAL A 15  ? 0.5620 0.4378 0.2919 -0.0223 -0.0525 -0.0847 15  VAL A CG1 
100  C CG2 . VAL A 15  ? 0.6107 0.4531 0.2866 -0.0256 -0.0141 -0.0855 15  VAL A CG2 
101  N N   . ILE A 16  ? 0.5057 0.3944 0.3015 -0.0028 -0.0067 -0.0967 16  ILE A N   
102  C CA  . ILE A 16  ? 0.5366 0.4248 0.3490 -0.0038 -0.0100 -0.1015 16  ILE A CA  
103  C C   . ILE A 16  ? 0.5305 0.4368 0.3609 -0.0097 -0.0360 -0.0988 16  ILE A C   
104  O O   . ILE A 16  ? 0.5178 0.4223 0.3603 -0.0144 -0.0391 -0.1045 16  ILE A O   
105  C CB  . ILE A 16  ? 0.5338 0.4338 0.3818 0.0110  0.0059  -0.0973 16  ILE A CB  
106  C CG1 . ILE A 16  ? 0.5080 0.4400 0.3878 0.0210  0.0001  -0.0850 16  ILE A CG1 
107  C CG2 . ILE A 16  ? 0.5208 0.4004 0.3584 0.0173  0.0320  -0.1028 16  ILE A CG2 
108  C CD1 . ILE A 16  ? 0.5071 0.4504 0.4184 0.0345  0.0096  -0.0791 16  ILE A CD1 
109  N N   . GLN A 17  ? 0.5039 0.4268 0.3394 -0.0097 -0.0530 -0.0909 17  GLN A N   
110  C CA  . GLN A 17  ? 0.5210 0.4598 0.3758 -0.0153 -0.0781 -0.0897 17  GLN A CA  
111  C C   . GLN A 17  ? 0.5430 0.4836 0.3828 -0.0170 -0.0964 -0.0823 17  GLN A C   
112  O O   . GLN A 17  ? 0.4898 0.4383 0.3328 -0.0091 -0.0897 -0.0738 17  GLN A O   
113  C CB  . GLN A 17  ? 0.4579 0.4243 0.3611 -0.0077 -0.0769 -0.0852 17  GLN A CB  
114  C CG  . GLN A 17  ? 0.5133 0.4990 0.4444 -0.0123 -0.0996 -0.0847 17  GLN A CG  
115  C CD  . GLN A 17  ? 0.5105 0.5180 0.4854 -0.0079 -0.0938 -0.0831 17  GLN A CD  
116  O OE1 . GLN A 17  ? 0.5570 0.5592 0.5386 -0.0083 -0.0792 -0.0871 17  GLN A OE1 
117  N NE2 . GLN A 17  ? 0.4568 0.4849 0.4585 -0.0041 -0.1040 -0.0772 17  GLN A NE2 
118  N N   . GLY A 18  ? 0.5776 0.5097 0.4009 -0.0275 -0.1205 -0.0852 18  GLY A N   
119  C CA  . GLY A 18  ? 0.5054 0.4337 0.3102 -0.0290 -0.1420 -0.0767 18  GLY A CA  
120  C C   . GLY A 18  ? 0.6187 0.5090 0.3573 -0.0383 -0.1393 -0.0783 18  GLY A C   
121  O O   . GLY A 18  ? 0.7161 0.5828 0.4239 -0.0449 -0.1213 -0.0882 18  GLY A O   
122  N N   . SER A 19  ? 0.7096 0.5901 0.4237 -0.0393 -0.1561 -0.0685 19  SER A N   
123  C CA  . SER A 19  ? 0.7325 0.5713 0.3754 -0.0503 -0.1553 -0.0686 19  SER A CA  
124  C C   . SER A 19  ? 0.7175 0.5506 0.3463 -0.0449 -0.1517 -0.0558 19  SER A C   
125  O O   . SER A 19  ? 0.7393 0.5921 0.3992 -0.0369 -0.1705 -0.0451 19  SER A O   
126  C CB  . SER A 19  ? 0.7010 0.5198 0.3092 -0.0639 -0.1905 -0.0703 19  SER A CB  
127  O OG  . SER A 19  ? 0.8886 0.6630 0.4221 -0.0757 -0.1892 -0.0688 19  SER A OG  
128  N N   . LEU A 20  ? 0.7550 0.5599 0.3388 -0.0498 -0.1251 -0.0579 20  LEU A N   
129  C CA  . LEU A 20  ? 0.8228 0.6138 0.3821 -0.0490 -0.1207 -0.0468 20  LEU A CA  
130  C C   . LEU A 20  ? 0.9357 0.6956 0.4440 -0.0579 -0.1542 -0.0374 20  LEU A C   
131  O O   . LEU A 20  ? 0.9403 0.6948 0.4421 -0.0542 -0.1630 -0.0243 20  LEU A O   
132  C CB  . LEU A 20  ? 0.8598 0.6269 0.3844 -0.0545 -0.0816 -0.0534 20  LEU A CB  
133  C CG  . LEU A 20  ? 0.8684 0.6657 0.4452 -0.0438 -0.0494 -0.0605 20  LEU A CG  
134  C CD1 . LEU A 20  ? 0.8643 0.6368 0.4092 -0.0499 -0.0115 -0.0684 20  LEU A CD1 
135  C CD2 . LEU A 20  ? 0.7966 0.6339 0.4323 -0.0301 -0.0519 -0.0509 20  LEU A CD2 
136  N N   . ASP A 21  ? 0.9387 0.6792 0.4155 -0.0693 -0.1725 -0.0431 21  ASP A N   
137  C CA  . ASP A 21  ? 1.0528 0.7784 0.5103 -0.0738 -0.2011 -0.0317 21  ASP A CA  
138  C C   . ASP A 21  ? 1.0122 0.7727 0.5289 -0.0609 -0.2329 -0.0206 21  ASP A C   
139  O O   . ASP A 21  ? 1.0901 0.8394 0.5975 -0.0586 -0.2517 -0.0068 21  ASP A O   
140  C CB  . ASP A 21  ? 1.0771 0.7859 0.5080 -0.0871 -0.2099 -0.0407 21  ASP A CB  
141  C CG  . ASP A 21  ? 1.2443 0.9178 0.6217 -0.0996 -0.1751 -0.0532 21  ASP A CG  
142  O OD1 . ASP A 21  ? 1.3117 0.9532 0.6435 -0.1048 -0.1552 -0.0491 21  ASP A OD1 
143  O OD2 . ASP A 21  ? 1.3026 0.9795 0.6863 -0.1043 -0.1653 -0.0678 21  ASP A OD2 
144  N N   . SER A 22  ? 0.9350 0.7357 0.5139 -0.0525 -0.2373 -0.0269 22  SER A N   
145  C CA  . SER A 22  ? 0.9393 0.7758 0.5835 -0.0400 -0.2608 -0.0186 22  SER A CA  
146  C C   . SER A 22  ? 0.8363 0.6795 0.4973 -0.0280 -0.2547 -0.0075 22  SER A C   
147  O O   . SER A 22  ? 0.9031 0.7703 0.6149 -0.0172 -0.2711 0.0002  22  SER A O   
148  C CB  . SER A 22  ? 0.8311 0.7058 0.5364 -0.0367 -0.2620 -0.0302 22  SER A CB  
149  O OG  . SER A 22  ? 1.0663 0.9364 0.7615 -0.0484 -0.2707 -0.0402 22  SER A OG  
150  N N   . LEU A 23  ? 0.8979 0.7209 0.5207 -0.0301 -0.2287 -0.0075 23  LEU A N   
151  C CA  . LEU A 23  ? 0.8605 0.6950 0.5092 -0.0195 -0.2165 0.0020  23  LEU A CA  
152  C C   . LEU A 23  ? 0.9340 0.7315 0.5342 -0.0217 -0.2333 0.0172  23  LEU A C   
153  O O   . LEU A 23  ? 0.9374 0.6991 0.4809 -0.0331 -0.2335 0.0186  23  LEU A O   
154  C CB  . LEU A 23  ? 0.8211 0.6602 0.4697 -0.0199 -0.1742 -0.0045 23  LEU A CB  
155  C CG  . LEU A 23  ? 0.7794 0.6548 0.4804 -0.0145 -0.1550 -0.0161 23  LEU A CG  
156  C CD1 . LEU A 23  ? 0.8170 0.6937 0.5148 -0.0145 -0.1178 -0.0208 23  LEU A CD1 
157  C CD2 . LEU A 23  ? 0.7515 0.6654 0.5205 -0.0028 -0.1653 -0.0132 23  LEU A CD2 
158  N N   . PRO A 24  ? 0.8932 0.7017 0.5259 -0.0105 -0.2398 0.0282  24  PRO A N   
159  C CA  . PRO A 24  ? 0.9592 0.7308 0.5495 -0.0119 -0.2450 0.0428  24  PRO A CA  
160  C C   . PRO A 24  ? 0.9845 0.7212 0.5109 -0.0236 -0.2133 0.0414  24  PRO A C   
161  O O   . PRO A 24  ? 0.9441 0.7008 0.4898 -0.0253 -0.1795 0.0296  24  PRO A O   
162  C CB  . PRO A 24  ? 0.9193 0.7126 0.5632 0.0030  -0.2521 0.0516  24  PRO A CB  
163  C CG  . PRO A 24  ? 0.8563 0.6982 0.5758 0.0119  -0.2604 0.0424  24  PRO A CG  
164  C CD  . PRO A 24  ? 0.8225 0.6766 0.5368 0.0034  -0.2401 0.0269  24  PRO A CD  
165  N N   . GLN A 25  ? 1.0596 0.7525 0.5306 -0.0310 -0.2155 0.0518  25  GLN A N   
166  C CA  . GLN A 25  ? 1.1385 0.7931 0.5453 -0.0453 -0.1827 0.0492  25  GLN A CA  
167  C C   . GLN A 25  ? 0.9878 0.6630 0.4238 -0.0425 -0.1477 0.0450  25  GLN A C   
168  O O   . GLN A 25  ? 0.9123 0.5964 0.3497 -0.0488 -0.1138 0.0319  25  GLN A O   
169  C CB  . GLN A 25  ? 1.2197 0.8265 0.5743 -0.0521 -0.1909 0.0625  25  GLN A CB  
170  C CG  . GLN A 25  ? 1.3900 0.9550 0.6812 -0.0686 -0.1541 0.0592  25  GLN A CG  
171  C CD  . GLN A 25  ? 1.5606 1.0756 0.8003 -0.0752 -0.1622 0.0728  25  GLN A CD  
172  O OE1 . GLN A 25  ? 1.6217 1.1353 0.8778 -0.0647 -0.1918 0.0867  25  GLN A OE1 
173  N NE2 . GLN A 25  ? 1.6517 1.1243 0.8307 -0.0927 -0.1347 0.0683  25  GLN A NE2 
174  N N   . GLU A 26  ? 0.9499 0.6385 0.4234 -0.0322 -0.1526 0.0547  26  GLU A N   
175  C CA  . GLU A 26  ? 0.9092 0.6222 0.4210 -0.0307 -0.1188 0.0497  26  GLU A CA  
176  C C   . GLU A 26  ? 0.8503 0.6188 0.4312 -0.0232 -0.1056 0.0358  26  GLU A C   
177  O O   . GLU A 26  ? 0.8132 0.6014 0.4180 -0.0251 -0.0754 0.0284  26  GLU A O   
178  C CB  . GLU A 26  ? 0.9380 0.6490 0.4716 -0.0224 -0.1284 0.0625  26  GLU A CB  
179  C CG  . GLU A 26  ? 1.1165 0.7674 0.5793 -0.0298 -0.1368 0.0779  26  GLU A CG  
180  C CD  . GLU A 26  ? 1.1834 0.7998 0.5877 -0.0480 -0.1006 0.0735  26  GLU A CD  
181  O OE1 . GLU A 26  ? 1.0750 0.7199 0.5127 -0.0516 -0.0662 0.0615  26  GLU A OE1 
182  O OE2 . GLU A 26  ? 1.2848 0.8446 0.6096 -0.0594 -0.1068 0.0819  26  GLU A OE2 
183  N N   . VAL A 27  ? 0.8669 0.6597 0.4801 -0.0154 -0.1283 0.0325  27  VAL A N   
184  C CA  . VAL A 27  ? 0.7561 0.5944 0.4267 -0.0094 -0.1158 0.0203  27  VAL A CA  
185  C C   . VAL A 27  ? 0.7200 0.5533 0.3674 -0.0176 -0.0940 0.0082  27  VAL A C   
186  O O   . VAL A 27  ? 0.6691 0.5284 0.3490 -0.0155 -0.0694 -0.0003 27  VAL A O   
187  C CB  . VAL A 27  ? 0.7626 0.6265 0.4769 0.0001  -0.1440 0.0200  27  VAL A CB  
188  C CG1 . VAL A 27  ? 0.5590 0.4626 0.3237 0.0046  -0.1299 0.0081  27  VAL A CG1 
189  C CG2 . VAL A 27  ? 0.7462 0.6162 0.4914 0.0096  -0.1610 0.0304  27  VAL A CG2 
190  N N   . ARG A 28  ? 0.7249 0.5230 0.3156 -0.0270 -0.1030 0.0073  28  ARG A N   
191  C CA  . ARG A 28  ? 0.8010 0.5886 0.3665 -0.0355 -0.0789 -0.0055 28  ARG A CA  
192  C C   . ARG A 28  ? 0.7648 0.5421 0.3155 -0.0420 -0.0413 -0.0091 28  ARG A C   
193  O O   . ARG A 28  ? 0.8353 0.6306 0.4101 -0.0411 -0.0144 -0.0204 28  ARG A O   
194  C CB  . ARG A 28  ? 0.8448 0.5901 0.3434 -0.0473 -0.0954 -0.0065 28  ARG A CB  
195  C CG  . ARG A 28  ? 0.8770 0.6054 0.3454 -0.0572 -0.0666 -0.0214 28  ARG A CG  
196  C CD  . ARG A 28  ? 1.0051 0.6941 0.4101 -0.0702 -0.0842 -0.0253 28  ARG A CD  
197  N NE  . ARG A 28  ? 0.9505 0.6263 0.3358 -0.0782 -0.0532 -0.0417 28  ARG A NE  
198  C CZ  . ARG A 28  ? 1.1501 0.7968 0.4917 -0.0899 -0.0588 -0.0496 28  ARG A CZ  
199  N NH1 . ARG A 28  ? 1.0017 0.6383 0.3286 -0.0940 -0.0944 -0.0413 28  ARG A NH1 
200  N NH2 . ARG A 28  ? 1.1425 0.7784 0.4742 -0.0955 -0.0257 -0.0651 28  ARG A NH2 
201  N N   . LYS A 29  ? 0.7747 0.5226 0.2885 -0.0485 -0.0389 0.0005  29  LYS A N   
202  C CA  . LYS A 29  ? 0.7763 0.5162 0.2814 -0.0565 -0.0015 -0.0035 29  LYS A CA  
203  C C   . LYS A 29  ? 0.7202 0.5125 0.3018 -0.0465 0.0146  -0.0086 29  LYS A C   
204  O O   . LYS A 29  ? 0.7044 0.5090 0.3033 -0.0496 0.0460  -0.0187 29  LYS A O   
205  C CB  . LYS A 29  ? 0.8698 0.5688 0.3256 -0.0650 -0.0041 0.0092  29  LYS A CB  
206  C CG  . LYS A 29  ? 1.0694 0.7076 0.4364 -0.0777 -0.0179 0.0152  29  LYS A CG  
207  C CD  . LYS A 29  ? 1.1597 0.7539 0.4768 -0.0852 -0.0208 0.0301  29  LYS A CD  
208  C CE  . LYS A 29  ? 1.3545 0.8926 0.5962 -0.0967 -0.0364 0.0364  29  LYS A CE  
209  N NZ  . LYS A 29  ? 1.5250 1.0409 0.7330 -0.1120 -0.0031 0.0220  29  LYS A NZ  
210  N N   . PHE A 30  ? 0.6401 0.4627 0.2684 -0.0349 -0.0070 -0.0020 30  PHE A N   
211  C CA  . PHE A 30  ? 0.5818 0.4509 0.2763 -0.0268 0.0042  -0.0063 30  PHE A CA  
212  C C   . PHE A 30  ? 0.5951 0.4930 0.3240 -0.0204 0.0118  -0.0172 30  PHE A C   
213  O O   . PHE A 30  ? 0.6109 0.5348 0.3759 -0.0185 0.0326  -0.0238 30  PHE A O   
214  C CB  . PHE A 30  ? 0.5725 0.4601 0.3007 -0.0175 -0.0196 0.0023  30  PHE A CB  
215  C CG  . PHE A 30  ? 0.5032 0.4332 0.2908 -0.0113 -0.0111 -0.0017 30  PHE A CG  
216  C CD1 . PHE A 30  ? 0.5162 0.4559 0.3170 -0.0171 0.0118  -0.0046 30  PHE A CD1 
217  C CD2 . PHE A 30  ? 0.5195 0.4781 0.3478 -0.0014 -0.0265 -0.0028 30  PHE A CD2 
218  C CE1 . PHE A 30  ? 0.4856 0.4629 0.3372 -0.0129 0.0157  -0.0081 30  PHE A CE1 
219  C CE2 . PHE A 30  ? 0.4415 0.4334 0.3154 0.0025  -0.0200 -0.0060 30  PHE A CE2 
220  C CZ  . PHE A 30  ? 0.4790 0.4803 0.3634 -0.0031 -0.0008 -0.0083 30  PHE A CZ  
221  N N   . VAL A 31  ? 0.6159 0.5087 0.3352 -0.0173 -0.0056 -0.0190 31  VAL A N   
222  C CA  . VAL A 31  ? 0.5913 0.5047 0.3384 -0.0116 0.0019  -0.0287 31  VAL A CA  
223  C C   . VAL A 31  ? 0.6277 0.5255 0.3541 -0.0181 0.0321  -0.0387 31  VAL A C   
224  O O   . VAL A 31  ? 0.5471 0.4700 0.3130 -0.0124 0.0512  -0.0453 31  VAL A O   
225  C CB  . VAL A 31  ? 0.6113 0.5192 0.3502 -0.0095 -0.0226 -0.0294 31  VAL A CB  
226  C CG1 . VAL A 31  ? 0.5492 0.4682 0.3065 -0.0056 -0.0115 -0.0399 31  VAL A CG1 
227  C CG2 . VAL A 31  ? 0.5445 0.4747 0.3188 -0.0018 -0.0475 -0.0221 31  VAL A CG2 
228  N N   . GLU A 32  ? 0.6432 0.4977 0.3071 -0.0302 0.0369  -0.0400 32  GLU A N   
229  C CA  . GLU A 32  ? 0.7246 0.5589 0.3648 -0.0377 0.0687  -0.0518 32  GLU A CA  
230  C C   . GLU A 32  ? 0.6856 0.5308 0.3472 -0.0405 0.1002  -0.0550 32  GLU A C   
231  O O   . GLU A 32  ? 0.6716 0.5264 0.3564 -0.0391 0.1285  -0.0662 32  GLU A O   
232  C CB  . GLU A 32  ? 0.7813 0.5606 0.3402 -0.0529 0.0661  -0.0527 32  GLU A CB  
233  C CG  . GLU A 32  ? 0.9432 0.7113 0.4833 -0.0530 0.0456  -0.0568 32  GLU A CG  
234  C CD  . GLU A 32  ? 0.9805 0.6914 0.4351 -0.0704 0.0449  -0.0599 32  GLU A CD  
235  O OE1 . GLU A 32  ? 1.0361 0.7138 0.4401 -0.0810 0.0451  -0.0525 32  GLU A OE1 
236  O OE2 . GLU A 32  ? 1.0327 0.7285 0.4669 -0.0747 0.0444  -0.0698 32  GLU A OE2 
237  N N   . GLY A 33  ? 0.6936 0.5376 0.3514 -0.0446 0.0965  -0.0460 33  GLY A N   
238  C CA  . GLY A 33  ? 0.6735 0.5294 0.3544 -0.0496 0.1261  -0.0499 33  GLY A CA  
239  C C   . GLY A 33  ? 0.5918 0.5018 0.3521 -0.0371 0.1329  -0.0551 33  GLY A C   
240  O O   . GLY A 33  ? 0.5958 0.5193 0.3844 -0.0385 0.1621  -0.0650 33  GLY A O   
241  N N   . ASN A 34  ? 0.5373 0.4778 0.3346 -0.0251 0.1058  -0.0486 34  ASN A N   
242  C CA  . ASN A 34  ? 0.5285 0.5160 0.3936 -0.0136 0.1072  -0.0516 34  ASN A CA  
243  C C   . ASN A 34  ? 0.5350 0.5305 0.4188 -0.0038 0.1120  -0.0591 34  ASN A C   
244  O O   . ASN A 34  ? 0.4988 0.5264 0.4348 0.0048  0.1210  -0.0632 34  ASN A O   
245  C CB  . ASN A 34  ? 0.4784 0.4894 0.3691 -0.0067 0.0795  -0.0424 34  ASN A CB  
246  C CG  . ASN A 34  ? 0.5553 0.5652 0.4428 -0.0147 0.0792  -0.0366 34  ASN A CG  
247  O OD1 . ASN A 34  ? 0.5656 0.5986 0.4865 -0.0176 0.0927  -0.0397 34  ASN A OD1 
248  N ND2 . ASN A 34  ? 0.5498 0.5323 0.3988 -0.0184 0.0632  -0.0283 34  ASN A ND2 
249  N N   . ALA A 35  ? 0.5536 0.5198 0.3967 -0.0051 0.1049  -0.0607 35  ALA A N   
250  C CA  . ALA A 35  ? 0.5184 0.4839 0.3727 0.0020  0.1149  -0.0694 35  ALA A CA  
251  C C   . ALA A 35  ? 0.6027 0.5596 0.4601 -0.0021 0.1517  -0.0810 35  ALA A C   
252  O O   . ALA A 35  ? 0.5899 0.5642 0.4884 0.0083  0.1655  -0.0878 35  ALA A O   
253  C CB  . ALA A 35  ? 0.5851 0.5181 0.3911 -0.0020 0.1000  -0.0702 35  ALA A CB  
254  N N   . GLN A 36  ? 0.5910 0.5190 0.4057 -0.0172 0.1693  -0.0833 36  GLN A N   
255  C CA  . GLN A 36  ? 0.6531 0.5732 0.4737 -0.0233 0.2094  -0.0958 36  GLN A CA  
256  C C   . GLN A 36  ? 0.5544 0.5233 0.4516 -0.0153 0.2207  -0.0974 36  GLN A C   
257  O O   . GLN A 36  ? 0.5764 0.5594 0.5145 -0.0102 0.2475  -0.1083 36  GLN A O   
258  C CB  . GLN A 36  ? 0.7671 0.6413 0.5187 -0.0437 0.2256  -0.0967 36  GLN A CB  
259  C CG  . GLN A 36  ? 0.9259 0.7832 0.6736 -0.0538 0.2725  -0.1117 36  GLN A CG  
260  C CD  . GLN A 36  ? 1.1742 0.9836 0.8502 -0.0759 0.2892  -0.1110 36  GLN A CD  
261  O OE1 . GLN A 36  ? 1.2391 1.0300 0.8724 -0.0818 0.2631  -0.0977 36  GLN A OE1 
262  N NE2 . GLN A 36  ? 1.0812 0.8710 0.7513 -0.0869 0.3267  -0.1226 36  GLN A NE2 
263  N N   . LEU A 37  ? 0.5329 0.5284 0.4530 -0.0141 0.1998  -0.0871 37  LEU A N   
264  C CA  . LEU A 37  ? 0.5173 0.5582 0.5059 -0.0099 0.2073  -0.0887 37  LEU A CA  
265  C C   . LEU A 37  ? 0.4687 0.5501 0.5191 0.0093  0.1906  -0.0869 37  LEU A C   
266  O O   . LEU A 37  ? 0.4546 0.5663 0.5638 0.0167  0.2054  -0.0935 37  LEU A O   
267  C CB  . LEU A 37  ? 0.5426 0.5912 0.5262 -0.0184 0.1927  -0.0796 37  LEU A CB  
268  C CG  . LEU A 37  ? 0.5348 0.6323 0.5877 -0.0158 0.1930  -0.0805 37  LEU A CG  
269  C CD1 . LEU A 37  ? 0.5528 0.6540 0.6253 -0.0278 0.2300  -0.0918 37  LEU A CD1 
270  C CD2 . LEU A 37  ? 0.5818 0.6875 0.6296 -0.0194 0.1676  -0.0699 37  LEU A CD2 
271  N N   . CYS A 38  ? 0.4951 0.5765 0.5341 0.0172  0.1597  -0.0777 38  CYS A N   
272  C CA  . CYS A 38  ? 0.4586 0.5719 0.5463 0.0337  0.1417  -0.0738 38  CYS A CA  
273  C C   . CYS A 38  ? 0.4638 0.5655 0.5559 0.0451  0.1499  -0.0794 38  CYS A C   
274  O O   . CYS A 38  ? 0.4578 0.5837 0.5953 0.0599  0.1412  -0.0771 38  CYS A O   
275  C CB  . CYS A 38  ? 0.3934 0.5098 0.4671 0.0354  0.1089  -0.0626 38  CYS A CB  
276  S SG  . CYS A 38  ? 0.4464 0.5740 0.5171 0.0235  0.0987  -0.0561 38  CYS A SG  
277  N N   A GLN A 39  ? 0.4961 0.5582 0.5393 0.0378  0.1656  -0.0864 39  GLN A N   
278  N N   B GLN A 39  ? 0.4961 0.5582 0.5392 0.0378  0.1656  -0.0864 39  GLN A N   
279  C CA  A GLN A 39  ? 0.5019 0.5458 0.5426 0.0460  0.1775  -0.0938 39  GLN A CA  
280  C CA  B GLN A 39  ? 0.5020 0.5458 0.5424 0.0459  0.1775  -0.0938 39  GLN A CA  
281  C C   A GLN A 39  ? 0.4880 0.5386 0.5400 0.0590  0.1516  -0.0865 39  GLN A C   
282  C C   B GLN A 39  ? 0.4881 0.5385 0.5400 0.0589  0.1516  -0.0865 39  GLN A C   
283  O O   A GLN A 39  ? 0.4735 0.5397 0.5692 0.0741  0.1538  -0.0869 39  GLN A O   
284  O O   B GLN A 39  ? 0.4737 0.5396 0.5691 0.0741  0.1540  -0.0870 39  GLN A O   
285  C CB  A GLN A 39  ? 0.5233 0.5839 0.6163 0.0539  0.2075  -0.1039 39  GLN A CB  
286  C CB  B GLN A 39  ? 0.5239 0.5838 0.6159 0.0537  0.2077  -0.1040 39  GLN A CB  
287  C CG  A GLN A 39  ? 0.5444 0.5880 0.6196 0.0390  0.2428  -0.1153 39  GLN A CG  
288  C CG  B GLN A 39  ? 0.5349 0.5882 0.6199 0.0392  0.2390  -0.1133 39  GLN A CG  
289  C CD  A GLN A 39  ? 0.5722 0.5618 0.5786 0.0274  0.2622  -0.1249 39  GLN A CD  
290  C CD  B GLN A 39  ? 0.5298 0.6014 0.6747 0.0474  0.2718  -0.1255 39  GLN A CD  
291  O OE1 A GLN A 39  ? 0.6584 0.6313 0.6621 0.0352  0.2692  -0.1310 39  GLN A OE1 
292  O OE1 B GLN A 39  ? 0.5788 0.6356 0.7313 0.0567  0.2875  -0.1334 39  GLN A OE1 
293  N NE2 A GLN A 39  ? 0.6447 0.6033 0.5912 0.0079  0.2704  -0.1259 39  GLN A NE2 
294  N NE2 B GLN A 39  ? 0.5156 0.6199 0.7072 0.0438  0.2831  -0.1278 39  GLN A NE2 
295  N N   . PRO A 40  ? 0.5043 0.5418 0.5190 0.0535  0.1274  -0.0796 40  PRO A N   
296  C CA  . PRO A 40  ? 0.5050 0.5429 0.5255 0.0629  0.1078  -0.0747 40  PRO A CA  
297  C C   . PRO A 40  ? 0.4801 0.4852 0.4760 0.0636  0.1210  -0.0837 40  PRO A C   
298  O O   . PRO A 40  ? 0.4864 0.4624 0.4445 0.0531  0.1392  -0.0931 40  PRO A O   
299  C CB  . PRO A 40  ? 0.4783 0.5127 0.4695 0.0542  0.0826  -0.0671 40  PRO A CB  
300  C CG  . PRO A 40  ? 0.4728 0.4851 0.4214 0.0398  0.0907  -0.0704 40  PRO A CG  
301  C CD  . PRO A 40  ? 0.4919 0.5123 0.4595 0.0386  0.1172  -0.0761 40  PRO A CD  
302  N N   . GLU A 41  ? 0.4689 0.4749 0.4827 0.0750  0.1125  -0.0811 41  GLU A N   
303  C CA  . GLU A 41  ? 0.4824 0.4550 0.4731 0.0752  0.1245  -0.0900 41  GLU A CA  
304  C C   . GLU A 41  ? 0.5588 0.5063 0.4993 0.0616  0.1090  -0.0913 41  GLU A C   
305  O O   . GLU A 41  ? 0.5749 0.4886 0.4773 0.0527  0.1207  -0.1018 41  GLU A O   
306  C CB  . GLU A 41  ? 0.5600 0.5386 0.5882 0.0928  0.1228  -0.0863 41  GLU A CB  
307  C CG  . GLU A 41  ? 0.5610 0.5031 0.5712 0.0946  0.1399  -0.0965 41  GLU A CG  
308  C CD  . GLU A 41  ? 0.7611 0.6877 0.7720 0.0944  0.1738  -0.1099 41  GLU A CD  
309  O OE1 . GLU A 41  ? 0.7528 0.7033 0.7948 0.0978  0.1852  -0.1102 41  GLU A OE1 
310  O OE2 . GLU A 41  ? 0.8993 0.7884 0.8796 0.0895  0.1910  -0.1215 41  GLU A OE2 
311  N N   . TYR A 42  ? 0.4866 0.4501 0.4281 0.0590  0.0831  -0.0819 42  TYR A N   
312  C CA  . TYR A 42  ? 0.5261 0.4731 0.4321 0.0471  0.0655  -0.0827 42  TYR A CA  
313  C C   . TYR A 42  ? 0.4919 0.4556 0.3939 0.0406  0.0470  -0.0748 42  TYR A C   
314  O O   . TYR A 42  ? 0.4748 0.4648 0.4054 0.0464  0.0444  -0.0675 42  TYR A O   
315  C CB  . TYR A 42  ? 0.4651 0.4113 0.3832 0.0515  0.0539  -0.0806 42  TYR A CB  
316  C CG  . TYR A 42  ? 0.5408 0.4717 0.4706 0.0614  0.0706  -0.0853 42  TYR A CG  
317  C CD1 . TYR A 42  ? 0.6208 0.5173 0.5202 0.0546  0.0830  -0.0970 42  TYR A CD1 
318  C CD2 . TYR A 42  ? 0.5637 0.5121 0.5334 0.0775  0.0726  -0.0777 42  TYR A CD2 
319  C CE1 . TYR A 42  ? 0.6400 0.5188 0.5507 0.0645  0.1000  -0.1015 42  TYR A CE1 
320  C CE2 . TYR A 42  ? 0.5520 0.4839 0.5342 0.0887  0.0864  -0.0804 42  TYR A CE2 
321  C CZ  . TYR A 42  ? 0.6160 0.5126 0.5697 0.0826  0.1014  -0.0924 42  TYR A CZ  
322  O OH  . TYR A 42  ? 0.7326 0.6094 0.6995 0.0946  0.1169  -0.0953 42  TYR A OH  
323  N N   . ILE A 43  ? 0.5469 0.4942 0.4141 0.0286  0.0329  -0.0764 43  ILE A N   
324  C CA  . ILE A 43  ? 0.4598 0.4191 0.3244 0.0238  0.0128  -0.0686 43  ILE A CA  
325  C C   . ILE A 43  ? 0.4319 0.3924 0.2988 0.0203  -0.0087 -0.0682 43  ILE A C   
326  O O   . ILE A 43  ? 0.5129 0.4524 0.3559 0.0128  -0.0123 -0.0756 43  ILE A O   
327  C CB  . ILE A 43  ? 0.4780 0.4162 0.3003 0.0130  0.0138  -0.0692 43  ILE A CB  
328  C CG1 . ILE A 43  ? 0.5054 0.4427 0.3290 0.0146  0.0400  -0.0715 43  ILE A CG1 
329  C CG2 . ILE A 43  ? 0.4359 0.3843 0.2585 0.0103  -0.0083 -0.0597 43  ILE A CG2 
330  C CD1 . ILE A 43  ? 0.5852 0.4951 0.3605 0.0020  0.0460  -0.0723 43  ILE A CD1 
331  N N   . HIS A 44  ? 0.4262 0.4109 0.3231 0.0245  -0.0214 -0.0610 44  HIS A N   
332  C CA  . HIS A 44  ? 0.4169 0.4076 0.3266 0.0215  -0.0383 -0.0613 44  HIS A CA  
333  C C   . HIS A 44  ? 0.3965 0.3991 0.3127 0.0192  -0.0555 -0.0549 44  HIS A C   
334  O O   . HIS A 44  ? 0.3304 0.3505 0.2674 0.0244  -0.0540 -0.0485 44  HIS A O   
335  C CB  . HIS A 44  ? 0.3636 0.3678 0.3042 0.0285  -0.0330 -0.0597 44  HIS A CB  
336  C CG  . HIS A 44  ? 0.3902 0.4006 0.3471 0.0240  -0.0450 -0.0613 44  HIS A CG  
337  N ND1 . HIS A 44  ? 0.4211 0.4213 0.3806 0.0214  -0.0411 -0.0671 44  HIS A ND1 
338  C CD2 . HIS A 44  ? 0.3394 0.3647 0.3142 0.0214  -0.0583 -0.0586 44  HIS A CD2 
339  C CE1 . HIS A 44  ? 0.3837 0.3936 0.3623 0.0161  -0.0506 -0.0686 44  HIS A CE1 
340  N NE2 . HIS A 44  ? 0.3955 0.4216 0.3858 0.0167  -0.0610 -0.0638 44  HIS A NE2 
341  N N   . ILE A 45  ? 0.4060 0.3978 0.3050 0.0115  -0.0728 -0.0566 45  ILE A N   
342  C CA  . ILE A 45  ? 0.3606 0.3616 0.2697 0.0111  -0.0918 -0.0502 45  ILE A CA  
343  C C   . ILE A 45  ? 0.4021 0.4231 0.3521 0.0122  -0.1007 -0.0522 45  ILE A C   
344  O O   . ILE A 45  ? 0.4198 0.4381 0.3740 0.0065  -0.1088 -0.0591 45  ILE A O   
345  C CB  . ILE A 45  ? 0.5241 0.5032 0.3962 0.0031  -0.1099 -0.0497 45  ILE A CB  
346  C CG1 . ILE A 45  ? 0.5050 0.4589 0.3309 -0.0005 -0.0957 -0.0490 45  ILE A CG1 
347  C CG2 . ILE A 45  ? 0.4664 0.4546 0.3545 0.0054  -0.1320 -0.0414 45  ILE A CG2 
348  C CD1 . ILE A 45  ? 0.6275 0.5504 0.4025 -0.0111 -0.1118 -0.0491 45  ILE A CD1 
349  N N   . CYS A 46  ? 0.3243 0.3638 0.3038 0.0180  -0.0973 -0.0473 46  CYS A N   
350  C CA  . CYS A 46  ? 0.3227 0.3786 0.3400 0.0180  -0.0990 -0.0505 46  CYS A CA  
351  C C   . CYS A 46  ? 0.3917 0.4539 0.4287 0.0150  -0.1201 -0.0520 46  CYS A C   
352  O O   . CYS A 46  ? 0.3324 0.3914 0.3624 0.0168  -0.1346 -0.0459 46  CYS A O   
353  C CB  . CYS A 46  ? 0.3241 0.3936 0.3614 0.0232  -0.0885 -0.0458 46  CYS A CB  
354  S SG  . CYS A 46  ? 0.3010 0.3688 0.3260 0.0273  -0.0687 -0.0437 46  CYS A SG  
355  N N   . ASP A 47  ? 0.3502 0.4209 0.4139 0.0103  -0.1220 -0.0599 47  ASP A N   
356  C CA  . ASP A 47  ? 0.4238 0.5076 0.5212 0.0080  -0.1414 -0.0629 47  ASP A CA  
357  C C   . ASP A 47  ? 0.3374 0.4411 0.4837 0.0096  -0.1321 -0.0661 47  ASP A C   
358  O O   . ASP A 47  ? 0.2871 0.4058 0.4731 0.0090  -0.1455 -0.0695 47  ASP A O   
359  C CB  . ASP A 47  ? 0.4297 0.5086 0.5234 -0.0019 -0.1530 -0.0721 47  ASP A CB  
360  C CG  . ASP A 47  ? 0.4363 0.5137 0.5376 -0.0080 -0.1334 -0.0813 47  ASP A CG  
361  O OD1 . ASP A 47  ? 0.3576 0.4387 0.4698 -0.0045 -0.1133 -0.0801 47  ASP A OD1 
362  O OD2 . ASP A 47  ? 0.4190 0.4881 0.5117 -0.0174 -0.1389 -0.0897 47  ASP A OD2 
363  N N   . GLY A 48  ? 0.2925 0.3955 0.4370 0.0112  -0.1097 -0.0655 48  GLY A N   
364  C CA  . GLY A 48  ? 0.2782 0.3936 0.4596 0.0107  -0.0971 -0.0693 48  GLY A CA  
365  C C   . GLY A 48  ? 0.2985 0.4208 0.5110 0.0020  -0.0911 -0.0806 48  GLY A C   
366  O O   . GLY A 48  ? 0.2269 0.3601 0.4763 0.0000  -0.0808 -0.0858 48  GLY A O   
367  N N   . SER A 49  ? 0.3307 0.4451 0.5294 -0.0047 -0.0947 -0.0859 49  SER A N   
368  C CA  . SER A 49  ? 0.3774 0.4980 0.6071 -0.0152 -0.0893 -0.0978 49  SER A CA  
369  C C   . SER A 49  ? 0.3677 0.4753 0.5880 -0.0204 -0.0617 -0.1008 49  SER A C   
370  O O   . SER A 49  ? 0.3510 0.4431 0.5352 -0.0157 -0.0512 -0.0931 49  SER A O   
371  C CB  . SER A 49  ? 0.3436 0.4573 0.5589 -0.0226 -0.1038 -0.1033 49  SER A CB  
372  O OG  . SER A 49  ? 0.3491 0.4385 0.5167 -0.0229 -0.0928 -0.1010 49  SER A OG  
373  N N   . GLU A 50  ? 0.3999 0.5133 0.6542 -0.0310 -0.0505 -0.1120 50  GLU A N   
374  C CA  . GLU A 50  ? 0.4406 0.5351 0.6803 -0.0388 -0.0240 -0.1151 50  GLU A CA  
375  C C   . GLU A 50  ? 0.4177 0.4867 0.6130 -0.0405 -0.0210 -0.1127 50  GLU A C   
376  O O   . GLU A 50  ? 0.4343 0.4812 0.5973 -0.0394 -0.0055 -0.1070 50  GLU A O   
377  C CB  . GLU A 50  ? 0.4918 0.5962 0.7781 -0.0521 -0.0106 -0.1295 50  GLU A CB  
378  C CG  . GLU A 50  ? 0.5238 0.6481 0.8558 -0.0507 -0.0035 -0.1334 50  GLU A CG  
379  C CD  . GLU A 50  ? 0.7127 0.8186 1.0187 -0.0507 0.0207  -0.1290 50  GLU A CD  
380  O OE1 . GLU A 50  ? 0.7210 0.7995 0.9777 -0.0531 0.0313  -0.1233 50  GLU A OE1 
381  O OE2 . GLU A 50  ? 0.8282 0.9453 1.1624 -0.0485 0.0282  -0.1313 50  GLU A OE2 
382  N N   . GLU A 51  ? 0.4371 0.5067 0.6294 -0.0433 -0.0365 -0.1169 51  GLU A N   
383  C CA  . GLU A 51  ? 0.4611 0.5040 0.6122 -0.0444 -0.0321 -0.1158 51  GLU A CA  
384  C C   . GLU A 51  ? 0.5605 0.5921 0.6730 -0.0305 -0.0325 -0.1029 51  GLU A C   
385  O O   . GLU A 51  ? 0.5152 0.5235 0.5985 -0.0276 -0.0200 -0.0985 51  GLU A O   
386  C CB  . GLU A 51  ? 0.5499 0.5944 0.7023 -0.0518 -0.0492 -0.1243 51  GLU A CB  
387  C CG  . GLU A 51  ? 0.6734 0.7280 0.8648 -0.0681 -0.0486 -0.1391 51  GLU A CG  
388  C CD  . GLU A 51  ? 0.7391 0.8290 0.9863 -0.0687 -0.0626 -0.1431 51  GLU A CD  
389  O OE1 . GLU A 51  ? 0.6026 0.7054 0.8543 -0.0563 -0.0716 -0.1337 51  GLU A OE1 
390  O OE2 . GLU A 51  ? 0.8435 0.9483 1.1331 -0.0816 -0.0644 -0.1561 51  GLU A OE2 
391  N N   . GLU A 52  ? 0.4850 0.5323 0.5996 -0.0217 -0.0468 -0.0964 52  GLU A N   
392  C CA  . GLU A 52  ? 0.4473 0.4877 0.5320 -0.0100 -0.0461 -0.0855 52  GLU A CA  
393  C C   . GLU A 52  ? 0.4363 0.4724 0.5159 -0.0055 -0.0317 -0.0785 52  GLU A C   
394  O O   . GLU A 52  ? 0.4496 0.4716 0.5043 0.0011  -0.0253 -0.0719 52  GLU A O   
395  C CB  . GLU A 52  ? 0.3910 0.4469 0.4794 -0.0042 -0.0627 -0.0809 52  GLU A CB  
396  C CG  . GLU A 52  ? 0.3599 0.4156 0.4296 0.0061  -0.0594 -0.0705 52  GLU A CG  
397  C CD  . GLU A 52  ? 0.3644 0.4298 0.4337 0.0098  -0.0742 -0.0661 52  GLU A CD  
398  O OE1 . GLU A 52  ? 0.3527 0.4083 0.3983 0.0096  -0.0819 -0.0661 52  GLU A OE1 
399  O OE2 . GLU A 52  ? 0.3445 0.4231 0.4341 0.0122  -0.0768 -0.0630 52  GLU A OE2 
400  N N   . TYR A 53  ? 0.4176 0.4649 0.5211 -0.0095 -0.0268 -0.0803 53  TYR A N   
401  C CA  . TYR A 53  ? 0.4641 0.5033 0.5565 -0.0085 -0.0137 -0.0747 53  TYR A CA  
402  C C   . TYR A 53  ? 0.4679 0.4803 0.5366 -0.0124 -0.0004 -0.0740 53  TYR A C   
403  O O   . TYR A 53  ? 0.4800 0.4787 0.5231 -0.0068 0.0033  -0.0648 53  TYR A O   
404  C CB  . TYR A 53  ? 0.4014 0.4525 0.5230 -0.0149 -0.0067 -0.0801 53  TYR A CB  
405  C CG  . TYR A 53  ? 0.4500 0.4919 0.5557 -0.0158 0.0055  -0.0751 53  TYR A CG  
406  C CD1 . TYR A 53  ? 0.4699 0.5160 0.5594 -0.0075 -0.0014 -0.0658 53  TYR A CD1 
407  C CD2 . TYR A 53  ? 0.5032 0.5305 0.6085 -0.0271 0.0244  -0.0808 53  TYR A CD2 
408  C CE1 . TYR A 53  ? 0.4980 0.5349 0.5703 -0.0104 0.0072  -0.0620 53  TYR A CE1 
409  C CE2 . TYR A 53  ? 0.5086 0.5226 0.5914 -0.0302 0.0349  -0.0767 53  TYR A CE2 
410  C CZ  . TYR A 53  ? 0.5241 0.5435 0.5901 -0.0218 0.0246  -0.0672 53  TYR A CZ  
411  O OH  . TYR A 53  ? 0.5280 0.5333 0.5688 -0.0269 0.0326  -0.0638 53  TYR A OH  
412  N N   . GLY A 54  ? 0.4712 0.4745 0.5481 -0.0222 0.0056  -0.0834 54  GLY A N   
413  C CA  . GLY A 54  ? 0.5159 0.4882 0.5674 -0.0265 0.0191  -0.0824 54  GLY A CA  
414  C C   . GLY A 54  ? 0.6280 0.5845 0.6507 -0.0149 0.0144  -0.0742 54  GLY A C   
415  O O   . GLY A 54  ? 0.5843 0.5177 0.5815 -0.0103 0.0210  -0.0655 54  GLY A O   
416  N N   . ARG A 55  ? 0.5833 0.5503 0.6095 -0.0100 0.0032  -0.0767 55  ARG A N   
417  C CA  . ARG A 55  ? 0.6166 0.5692 0.6201 0.0011  0.0024  -0.0709 55  ARG A CA  
418  C C   . ARG A 55  ? 0.6620 0.6222 0.6586 0.0143  -0.0012 -0.0584 55  ARG A C   
419  O O   . ARG A 55  ? 0.7252 0.6696 0.7067 0.0240  0.0020  -0.0510 55  ARG A O   
420  C CB  . ARG A 55  ? 0.6393 0.5985 0.6432 0.0008  -0.0065 -0.0777 55  ARG A CB  
421  C CG  . ARG A 55  ? 0.7495 0.6940 0.7524 -0.0119 -0.0037 -0.0900 55  ARG A CG  
422  C CD  . ARG A 55  ? 0.9001 0.8437 0.8914 -0.0130 -0.0128 -0.0961 55  ARG A CD  
423  N NE  . ARG A 55  ? 0.9047 0.8743 0.9092 -0.0139 -0.0299 -0.0962 55  ARG A NE  
424  C CZ  . ARG A 55  ? 0.8676 0.8511 0.8919 -0.0249 -0.0428 -0.1041 55  ARG A CZ  
425  N NH1 . ARG A 55  ? 0.8479 0.8253 0.8843 -0.0378 -0.0394 -0.1145 55  ARG A NH1 
426  N NH2 . ARG A 55  ? 0.7559 0.7597 0.7902 -0.0229 -0.0599 -0.1014 55  ARG A NH2 
427  N N   . LEU A 56  ? 0.5500 0.5345 0.5603 0.0149  -0.0085 -0.0563 56  LEU A N   
428  C CA  . LEU A 56  ? 0.5311 0.5248 0.5370 0.0247  -0.0125 -0.0460 56  LEU A CA  
429  C C   . LEU A 56  ? 0.5404 0.5178 0.5315 0.0249  -0.0075 -0.0383 56  LEU A C   
430  O O   . LEU A 56  ? 0.5779 0.5524 0.5598 0.0349  -0.0116 -0.0288 56  LEU A O   
431  C CB  . LEU A 56  ? 0.5625 0.5813 0.5842 0.0231  -0.0196 -0.0464 56  LEU A CB  
432  C CG  . LEU A 56  ? 0.6269 0.6589 0.6564 0.0240  -0.0279 -0.0505 56  LEU A CG  
433  C CD1 . LEU A 56  ? 0.4947 0.5460 0.5392 0.0226  -0.0343 -0.0495 56  LEU A CD1 
434  C CD2 . LEU A 56  ? 0.6184 0.6478 0.6356 0.0332  -0.0281 -0.0469 56  LEU A CD2 
435  N N   . LEU A 57  ? 0.5730 0.5388 0.5616 0.0131  0.0010  -0.0425 57  LEU A N   
436  C CA  . LEU A 57  ? 0.5636 0.5056 0.5279 0.0104  0.0068  -0.0352 57  LEU A CA  
437  C C   . LEU A 57  ? 0.6609 0.5732 0.6039 0.0169  0.0092  -0.0289 57  LEU A C   
438  O O   . LEU A 57  ? 0.6267 0.5269 0.5518 0.0258  0.0029  -0.0168 57  LEU A O   
439  C CB  . LEU A 57  ? 0.5283 0.4607 0.4937 -0.0060 0.0205  -0.0433 57  LEU A CB  
440  C CG  . LEU A 57  ? 0.5403 0.4954 0.5251 -0.0120 0.0214  -0.0485 57  LEU A CG  
441  C CD1 . LEU A 57  ? 0.6146 0.5623 0.6119 -0.0278 0.0387  -0.0601 57  LEU A CD1 
442  C CD2 . LEU A 57  ? 0.5188 0.4709 0.4820 -0.0099 0.0170  -0.0391 57  LEU A CD2 
443  N N   . ALA A 58  ? 0.6828 0.5821 0.6286 0.0126  0.0170  -0.0370 58  ALA A N   
444  C CA  . ALA A 58  ? 0.7827 0.6498 0.7089 0.0190  0.0215  -0.0320 58  ALA A CA  
445  C C   . ALA A 58  ? 0.7179 0.5926 0.6476 0.0379  0.0116  -0.0235 58  ALA A C   
446  O O   . ALA A 58  ? 0.7321 0.5840 0.6468 0.0484  0.0099  -0.0126 58  ALA A O   
447  C CB  . ALA A 58  ? 0.7477 0.6029 0.6790 0.0097  0.0315  -0.0448 58  ALA A CB  
448  N N   . HIS A 59  ? 0.7068 0.6120 0.6573 0.0423  0.0053  -0.0281 59  HIS A N   
449  C CA  . HIS A 59  ? 0.6698 0.5863 0.6292 0.0586  -0.0009 -0.0219 59  HIS A CA  
450  C C   . HIS A 59  ? 0.7239 0.6462 0.6812 0.0669  -0.0114 -0.0083 59  HIS A C   
451  O O   . HIS A 59  ? 0.7584 0.6680 0.7136 0.0802  -0.0151 0.0012  59  HIS A O   
452  C CB  . HIS A 59  ? 0.6198 0.5657 0.5964 0.0578  -0.0040 -0.0293 59  HIS A CB  
453  C CG  . HIS A 59  ? 0.7096 0.6702 0.6987 0.0717  -0.0068 -0.0248 59  HIS A CG  
454  N ND1 . HIS A 59  ? 0.6809 0.6263 0.6720 0.0845  -0.0012 -0.0221 59  HIS A ND1 
455  C CD2 . HIS A 59  ? 0.6297 0.6183 0.6331 0.0744  -0.0125 -0.0235 59  HIS A CD2 
456  C CE1 . HIS A 59  ? 0.7434 0.7098 0.7534 0.0944  -0.0027 -0.0201 59  HIS A CE1 
457  N NE2 . HIS A 59  ? 0.6362 0.6286 0.6522 0.0876  -0.0094 -0.0209 59  HIS A NE2 
458  N N   . MET A 60  ? 0.7216 0.6622 0.6803 0.0590  -0.0172 -0.0076 60  MET A N   
459  C CA  . MET A 60  ? 0.6383 0.5842 0.5912 0.0635  -0.0290 0.0039  60  MET A CA  
460  C C   . MET A 60  ? 0.6704 0.5803 0.5946 0.0648  -0.0308 0.0144  60  MET A C   
461  O O   . MET A 60  ? 0.6819 0.5896 0.6026 0.0756  -0.0444 0.0268  60  MET A O   
462  C CB  . MET A 60  ? 0.5218 0.4849 0.4746 0.0511  -0.0308 0.0005  60  MET A CB  
463  C CG  . MET A 60  ? 0.4315 0.4295 0.4090 0.0536  -0.0357 -0.0033 60  MET A CG  
464  S SD  . MET A 60  ? 0.5256 0.5371 0.5016 0.0398  -0.0361 -0.0071 60  MET A SD  
465  C CE  . MET A 60  ? 0.4917 0.4962 0.4733 0.0285  -0.0228 -0.0195 60  MET A CE  
466  N N   . GLN A 61  ? 0.6771 0.5576 0.5804 0.0535  -0.0181 0.0101  61  GLN A N   
467  C CA  . GLN A 61  ? 0.7446 0.5831 0.6131 0.0529  -0.0176 0.0205  61  GLN A CA  
468  C C   . GLN A 61  ? 0.8679 0.6873 0.7382 0.0704  -0.0207 0.0285  61  GLN A C   
469  O O   . GLN A 61  ? 0.8654 0.6592 0.7145 0.0787  -0.0310 0.0433  61  GLN A O   
470  C CB  . GLN A 61  ? 0.7769 0.5883 0.6255 0.0343  0.0011  0.0118  61  GLN A CB  
471  C CG  . GLN A 61  ? 0.8692 0.6314 0.6723 0.0288  0.0045  0.0224  61  GLN A CG  
472  C CD  . GLN A 61  ? 0.9393 0.6763 0.7264 0.0077  0.0273  0.0116  61  GLN A CD  
473  O OE1 . GLN A 61  ? 0.8353 0.5911 0.6509 -0.0001 0.0387  -0.0038 61  GLN A OE1 
474  N NE2 . GLN A 61  ? 0.9536 0.6470 0.6949 -0.0025 0.0337  0.0193  61  GLN A NE2 
475  N N   . GLU A 62  ? 0.8742 0.7030 0.7681 0.0761  -0.0124 0.0191  62  GLU A N   
476  C CA  . GLU A 62  ? 0.9635 0.7746 0.8637 0.0935  -0.0120 0.0247  62  GLU A CA  
477  C C   . GLU A 62  ? 0.9441 0.7813 0.8709 0.1126  -0.0278 0.0341  62  GLU A C   
478  O O   . GLU A 62  ? 1.0650 0.8852 0.9975 0.1299  -0.0322 0.0438  62  GLU A O   
479  C CB  . GLU A 62  ? 0.9269 0.7375 0.8401 0.0912  0.0038  0.0096  62  GLU A CB  
480  C CG  . GLU A 62  ? 0.9307 0.7116 0.8221 0.0736  0.0189  0.0003  62  GLU A CG  
481  C CD  . GLU A 62  ? 0.8422 0.6324 0.7467 0.0656  0.0296  -0.0171 62  GLU A CD  
482  O OE1 . GLU A 62  ? 0.8134 0.6234 0.7365 0.0751  0.0281  -0.0210 62  GLU A OE1 
483  O OE2 . GLU A 62  ? 0.8246 0.6015 0.7199 0.0485  0.0395  -0.0273 62  GLU A OE2 
484  N N   . GLU A 63  ? 0.8215 0.6991 0.7677 0.1100  -0.0360 0.0314  63  GLU A N   
485  C CA  . GLU A 63  ? 0.8508 0.7580 0.8270 0.1251  -0.0505 0.0387  63  GLU A CA  
486  C C   . GLU A 63  ? 0.8266 0.7340 0.7888 0.1252  -0.0718 0.0529  63  GLU A C   
487  O O   . GLU A 63  ? 0.7967 0.7341 0.7859 0.1343  -0.0868 0.0581  63  GLU A O   
488  C CB  . GLU A 63  ? 0.7491 0.6975 0.7527 0.1209  -0.0465 0.0274  63  GLU A CB  
489  C CG  . GLU A 63  ? 0.9168 0.8636 0.9256 0.1170  -0.0280 0.0128  63  GLU A CG  
490  C CD  . GLU A 63  ? 0.9522 0.8919 0.9809 0.1330  -0.0188 0.0111  63  GLU A CD  
491  O OE1 . GLU A 63  ? 0.9149 0.8557 0.9622 0.1495  -0.0274 0.0216  63  GLU A OE1 
492  O OE2 . GLU A 63  ? 0.9551 0.8873 0.9814 0.1288  -0.0033 -0.0011 63  GLU A OE2 
493  N N   . GLY A 64  ? 0.8036 0.6774 0.7231 0.1137  -0.0728 0.0584  64  GLY A N   
494  C CA  . GLY A 64  ? 0.7985 0.6650 0.6934 0.1106  -0.0930 0.0716  64  GLY A CA  
495  C C   . GLY A 64  ? 0.7787 0.6804 0.6811 0.0993  -0.1002 0.0667  64  GLY A C   
496  O O   . GLY A 64  ? 0.7766 0.6847 0.6720 0.1003  -0.1215 0.0768  64  GLY A O   
497  N N   . VAL A 65  ? 0.7290 0.6521 0.6448 0.0884  -0.0845 0.0516  65  VAL A N   
498  C CA  . VAL A 65  ? 0.6927 0.6457 0.6159 0.0777  -0.0888 0.0463  65  VAL A CA  
499  C C   . VAL A 65  ? 0.7010 0.6315 0.5843 0.0579  -0.0830 0.0440  65  VAL A C   
500  O O   . VAL A 65  ? 0.6579 0.5960 0.5292 0.0494  -0.0929 0.0459  65  VAL A O   
501  C CB  . VAL A 65  ? 0.7050 0.6899 0.6624 0.0772  -0.0763 0.0327  65  VAL A CB  
502  C CG1 . VAL A 65  ? 0.5666 0.5807 0.5338 0.0682  -0.0811 0.0286  65  VAL A CG1 
503  C CG2 . VAL A 65  ? 0.7438 0.7436 0.7350 0.0947  -0.0761 0.0331  65  VAL A CG2 
504  N N   . ILE A 66  ? 0.6293 0.5311 0.4924 0.0490  -0.0652 0.0385  66  ILE A N   
505  C CA  . ILE A 66  ? 0.6234 0.5015 0.4519 0.0294  -0.0541 0.0343  66  ILE A CA  
506  C C   . ILE A 66  ? 0.6685 0.4970 0.4569 0.0252  -0.0466 0.0406  66  ILE A C   
507  O O   . ILE A 66  ? 0.7040 0.5182 0.4969 0.0366  -0.0458 0.0449  66  ILE A O   
508  C CB  . ILE A 66  ? 0.5555 0.4513 0.4058 0.0181  -0.0350 0.0175  66  ILE A CB  
509  C CG1 . ILE A 66  ? 0.6016 0.4974 0.4732 0.0228  -0.0235 0.0102  66  ILE A CG1 
510  C CG2 . ILE A 66  ? 0.5498 0.4860 0.4296 0.0195  -0.0418 0.0127  66  ILE A CG2 
511  C CD1 . ILE A 66  ? 0.5773 0.4903 0.4728 0.0124  -0.0094 -0.0050 66  ILE A CD1 
512  N N   . ARG A 67  ? 0.6758 0.4744 0.4220 0.0075  -0.0388 0.0404  67  ARG A N   
513  C CA  . ARG A 67  ? 0.6956 0.4413 0.3960 -0.0020 -0.0264 0.0447  67  ARG A CA  
514  C C   . ARG A 67  ? 0.7073 0.4435 0.4020 -0.0238 0.0022  0.0286  67  ARG A C   
515  O O   . ARG A 67  ? 0.6345 0.3909 0.3380 -0.0338 0.0072  0.0195  67  ARG A O   
516  C CB  . ARG A 67  ? 0.8115 0.5195 0.4553 -0.0047 -0.0439 0.0617  67  ARG A CB  
517  C CG  . ARG A 67  ? 0.9195 0.6291 0.5689 0.0179  -0.0731 0.0798  67  ARG A CG  
518  C CD  . ARG A 67  ? 1.0548 0.7249 0.6445 0.0137  -0.0944 0.0973  67  ARG A CD  
519  N NE  . ARG A 67  ? 1.1327 0.7424 0.6582 -0.0061 -0.0751 0.0982  67  ARG A NE  
520  C CZ  . ARG A 67  ? 1.2279 0.7893 0.7224 -0.0028 -0.0696 0.1079  67  ARG A CZ  
521  N NH1 . ARG A 67  ? 1.2475 0.8126 0.7701 0.0206  -0.0821 0.1176  67  ARG A NH1 
522  N NH2 . ARG A 67  ? 1.2442 0.7494 0.6776 -0.0243 -0.0487 0.1072  67  ARG A NH2 
523  N N   . LYS A 68  ? 0.6843 0.3895 0.3673 -0.0314 0.0221  0.0242  68  LYS A N   
524  C CA  . LYS A 68  ? 0.7623 0.4579 0.4451 -0.0529 0.0513  0.0081  68  LYS A CA  
525  C C   . LYS A 68  ? 0.7117 0.3610 0.3324 -0.0716 0.0614  0.0121  68  LYS A C   
526  O O   . LYS A 68  ? 0.8394 0.4425 0.4064 -0.0714 0.0539  0.0273  68  LYS A O   
527  C CB  . LYS A 68  ? 0.7926 0.4729 0.4880 -0.0568 0.0700  0.0002  68  LYS A CB  
528  C CG  . LYS A 68  ? 0.7937 0.4800 0.5118 -0.0769 0.0988  -0.0197 68  LYS A CG  
529  C CD  . LYS A 68  ? 0.8474 0.5293 0.5896 -0.0805 0.1131  -0.0294 68  LYS A CD  
530  C CE  . LYS A 68  ? 0.8779 0.5858 0.6664 -0.0959 0.1344  -0.0508 68  LYS A CE  
531  N NZ  . LYS A 68  ? 0.9603 0.6416 0.7242 -0.1176 0.1606  -0.0579 68  LYS A NZ  
532  N N   . LEU A 69  ? 0.7238 0.3825 0.3497 -0.0877 0.0785  -0.0014 69  LEU A N   
533  C CA  . LEU A 69  ? 0.8445 0.4563 0.4102 -0.1099 0.0957  -0.0022 69  LEU A CA  
534  C C   . LEU A 69  ? 0.8881 0.4717 0.4517 -0.1283 0.1322  -0.0156 69  LEU A C   
535  O O   . LEU A 69  ? 0.8618 0.4672 0.4658 -0.1394 0.1564  -0.0347 69  LEU A O   
536  C CB  . LEU A 69  ? 0.8034 0.4376 0.3766 -0.1181 0.0980  -0.0112 69  LEU A CB  
537  C CG  . LEU A 69  ? 0.7273 0.3889 0.3023 -0.1029 0.0629  0.0008  69  LEU A CG  
538  C CD1 . LEU A 69  ? 0.6886 0.3860 0.2953 -0.1074 0.0675  -0.0120 69  LEU A CD1 
539  C CD2 . LEU A 69  ? 0.8182 0.4337 0.3179 -0.1078 0.0445  0.0184  69  LEU A CD2 
540  N N   . LYS A 70  ? 0.9431 0.4772 0.4619 -0.1314 0.1363  -0.0054 70  LYS A N   
541  C CA  . LYS A 70  ? 1.0032 0.5110 0.5245 -0.1476 0.1697  -0.0174 70  LYS A CA  
542  C C   . LYS A 70  ? 0.9935 0.4735 0.4910 -0.1762 0.2070  -0.0327 70  LYS A C   
543  O O   . LYS A 70  ? 1.0497 0.5215 0.5685 -0.1915 0.2389  -0.0481 70  LYS A O   
544  C CB  . LYS A 70  ? 1.1496 0.6021 0.6188 -0.1449 0.1655  -0.0010 70  LYS A CB  
545  C CG  . LYS A 70  ? 1.2601 0.6555 0.6423 -0.1483 0.1513  0.0196  70  LYS A CG  
546  C CD  . LYS A 70  ? 1.4459 0.7824 0.7787 -0.1449 0.1485  0.0363  70  LYS A CD  
547  C CE  . LYS A 70  ? 1.4278 0.7023 0.6690 -0.1487 0.1312  0.0588  70  LYS A CE  
548  N NZ  . LYS A 70  ? 1.3337 0.6397 0.5818 -0.1258 0.0863  0.0749  70  LYS A NZ  
549  N N   . LYS A 71  ? 0.9971 0.4622 0.4529 -0.1850 0.2055  -0.0302 71  LYS A N   
550  C CA  . LYS A 71  ? 1.0106 0.4452 0.4407 -0.2133 0.2449  -0.0462 71  LYS A CA  
551  C C   . LYS A 71  ? 0.9982 0.4873 0.5115 -0.2164 0.2660  -0.0705 71  LYS A C   
552  O O   . LYS A 71  ? 0.9551 0.4267 0.4724 -0.2388 0.3064  -0.0886 71  LYS A O   
553  C CB  . LYS A 71  ? 1.0393 0.4365 0.3926 -0.2230 0.2357  -0.0365 71  LYS A CB  
554  C CG  . LYS A 71  ? 1.0928 0.4560 0.4222 -0.2470 0.2674  -0.0559 71  LYS A CG  
555  C CD  . LYS A 71  ? 1.1560 0.4797 0.4128 -0.2533 0.2469  -0.0457 71  LYS A CD  
556  C CE  . LYS A 71  ? 1.2215 0.5029 0.4507 -0.2781 0.2785  -0.0653 71  LYS A CE  
557  N NZ  . LYS A 71  ? 1.4635 0.6937 0.6113 -0.2872 0.2584  -0.0534 71  LYS A NZ  
558  N N   . TYR A 72  ? 0.8908 0.4436 0.4711 -0.1946 0.2407  -0.0711 72  TYR A N   
559  C CA  . TYR A 72  ? 0.8537 0.4581 0.5116 -0.1941 0.2540  -0.0908 72  TYR A CA  
560  C C   . TYR A 72  ? 0.7892 0.4407 0.5226 -0.1798 0.2447  -0.0962 72  TYR A C   
561  O O   . TYR A 72  ? 0.8232 0.4662 0.5471 -0.1712 0.2307  -0.0861 72  TYR A O   
562  C CB  . TYR A 72  ? 0.8320 0.4658 0.4974 -0.1838 0.2332  -0.0877 72  TYR A CB  
563  C CG  . TYR A 72  ? 0.8152 0.4014 0.3977 -0.1971 0.2337  -0.0797 72  TYR A CG  
564  C CD1 . TYR A 72  ? 0.8758 0.4180 0.4187 -0.2237 0.2718  -0.0924 72  TYR A CD1 
565  C CD2 . TYR A 72  ? 0.8276 0.4117 0.3712 -0.1844 0.1961  -0.0601 72  TYR A CD2 
566  C CE1 . TYR A 72  ? 0.9433 0.4369 0.4019 -0.2383 0.2712  -0.0854 72  TYR A CE1 
567  C CE2 . TYR A 72  ? 0.8842 0.4246 0.3501 -0.1979 0.1923  -0.0526 72  TYR A CE2 
568  C CZ  . TYR A 72  ? 0.9475 0.4407 0.3670 -0.2254 0.2292  -0.0651 72  TYR A CZ  
569  O OH  . TYR A 72  ? 1.0126 0.4632 0.3602 -0.2381 0.2196  -0.0583 72  TYR A OH  
570  N N   . ASP A 73  ? 0.7428 0.4420 0.5504 -0.1774 0.2521  -0.1124 73  ASP A N   
571  C CA  . ASP A 73  ? 0.7533 0.4977 0.6341 -0.1671 0.2435  -0.1200 73  ASP A CA  
572  C C   . ASP A 73  ? 0.6510 0.4396 0.5595 -0.1425 0.2058  -0.1101 73  ASP A C   
573  O O   . ASP A 73  ? 0.6197 0.4374 0.5580 -0.1369 0.2009  -0.1142 73  ASP A O   
574  C CB  . ASP A 73  ? 0.8174 0.5867 0.7658 -0.1790 0.2719  -0.1430 73  ASP A CB  
575  C CG  . ASP A 73  ? 0.8431 0.6620 0.8693 -0.1688 0.2579  -0.1509 73  ASP A CG  
576  O OD1 . ASP A 73  ? 0.8940 0.7171 0.9131 -0.1581 0.2348  -0.1411 73  ASP A OD1 
577  O OD2 . ASP A 73  ? 0.9776 0.8303 1.0724 -0.1716 0.2696  -0.1672 73  ASP A OD2 
578  N N   . ASN A 74  ? 0.6690 0.4594 0.5667 -0.1288 0.1818  -0.0976 74  ASN A N   
579  C CA  . ASN A 74  ? 0.6017 0.4315 0.5257 -0.1069 0.1494  -0.0894 74  ASN A CA  
580  C C   . ASN A 74  ? 0.5323 0.3670 0.4327 -0.0993 0.1346  -0.0797 74  ASN A C   
581  O O   . ASN A 74  ? 0.5055 0.3766 0.4419 -0.0899 0.1227  -0.0819 74  ASN A O   
582  C CB  . ASN A 74  ? 0.5828 0.4593 0.5801 -0.1027 0.1463  -0.1026 74  ASN A CB  
583  C CG  . ASN A 74  ? 0.6006 0.5100 0.6174 -0.0826 0.1152  -0.0945 74  ASN A CG  
584  O OD1 . ASN A 74  ? 0.5823 0.4811 0.5704 -0.0728 0.0999  -0.0826 74  ASN A OD1 
585  N ND2 . ASN A 74  ? 0.4922 0.4392 0.5577 -0.0765 0.1068  -0.1008 74  ASN A ND2 
586  N N   . CYS A 75  ? 0.5907 0.3863 0.4281 -0.1045 0.1344  -0.0686 75  CYS A N   
587  C CA  . CYS A 75  ? 0.5903 0.3877 0.3999 -0.0991 0.1174  -0.0586 75  CYS A CA  
588  C C   . CYS A 75  ? 0.5609 0.3491 0.3389 -0.0846 0.0900  -0.0397 75  CYS A C   
589  O O   . CYS A 75  ? 0.6204 0.3774 0.3697 -0.0850 0.0912  -0.0325 75  CYS A O   
590  C CB  . CYS A 75  ? 0.5914 0.3510 0.3528 -0.1190 0.1375  -0.0623 75  CYS A CB  
591  S SG  . CYS A 75  ? 0.6038 0.3789 0.4100 -0.1333 0.1700  -0.0854 75  CYS A SG  
592  N N   . TRP A 76  ? 0.5206 0.3359 0.3072 -0.0717 0.0663  -0.0321 76  TRP A N   
593  C CA  . TRP A 76  ? 0.5599 0.3791 0.3363 -0.0547 0.0397  -0.0163 76  TRP A CA  
594  C C   . TRP A 76  ? 0.5597 0.3830 0.3130 -0.0529 0.0205  -0.0072 76  TRP A C   
595  O O   . TRP A 76  ? 0.5475 0.3867 0.3102 -0.0598 0.0243  -0.0147 76  TRP A O   
596  C CB  . TRP A 76  ? 0.5384 0.3973 0.3668 -0.0380 0.0293  -0.0184 76  TRP A CB  
597  C CG  . TRP A 76  ? 0.4972 0.3559 0.3510 -0.0414 0.0451  -0.0290 76  TRP A CG  
598  C CD1 . TRP A 76  ? 0.5089 0.3843 0.3980 -0.0503 0.0607  -0.0441 76  TRP A CD1 
599  C CD2 . TRP A 76  ? 0.5590 0.3998 0.4072 -0.0366 0.0459  -0.0257 76  TRP A CD2 
600  N NE1 . TRP A 76  ? 0.5328 0.4043 0.4393 -0.0525 0.0694  -0.0508 76  TRP A NE1 
601  C CE2 . TRP A 76  ? 0.6136 0.4622 0.4930 -0.0449 0.0617  -0.0402 76  TRP A CE2 
602  C CE3 . TRP A 76  ? 0.6332 0.4517 0.4556 -0.0256 0.0344  -0.0121 76  TRP A CE3 
603  C CZ2 . TRP A 76  ? 0.5718 0.4054 0.4531 -0.0449 0.0672  -0.0425 76  TRP A CZ2 
604  C CZ3 . TRP A 76  ? 0.6374 0.4385 0.4615 -0.0239 0.0417  -0.0139 76  TRP A CZ3 
605  C CH2 . TRP A 76  ? 0.6507 0.4587 0.5019 -0.0347 0.0584  -0.0295 76  TRP A CH2 
606  N N   . LEU A 77  ? 0.5540 0.3631 0.2797 -0.0434 -0.0010 0.0088  77  LEU A N   
607  C CA  . LEU A 77  ? 0.5698 0.3821 0.2732 -0.0421 -0.0239 0.0188  77  LEU A CA  
608  C C   . LEU A 77  ? 0.5900 0.4368 0.3286 -0.0204 -0.0492 0.0282  77  LEU A C   
609  O O   . LEU A 77  ? 0.5730 0.4128 0.3175 -0.0067 -0.0555 0.0363  77  LEU A O   
610  C CB  . LEU A 77  ? 0.6434 0.4038 0.2780 -0.0522 -0.0299 0.0307  77  LEU A CB  
611  C CG  . LEU A 77  ? 0.6693 0.4304 0.2772 -0.0507 -0.0602 0.0432  77  LEU A CG  
612  C CD1 . LEU A 77  ? 0.6534 0.4343 0.2656 -0.0639 -0.0564 0.0320  77  LEU A CD1 
613  C CD2 . LEU A 77  ? 0.7509 0.4544 0.2848 -0.0600 -0.0692 0.0571  77  LEU A CD2 
614  N N   . ALA A 78  ? 0.5378 0.4195 0.3001 -0.0180 -0.0611 0.0262  78  ALA A N   
615  C CA  . ALA A 78  ? 0.4936 0.4095 0.2909 0.0000  -0.0828 0.0336  78  ALA A CA  
616  C C   . ALA A 78  ? 0.5073 0.4254 0.2846 -0.0028 -0.1076 0.0429  78  ALA A C   
617  O O   . ALA A 78  ? 0.5203 0.4335 0.2748 -0.0191 -0.1057 0.0376  78  ALA A O   
618  C CB  . ALA A 78  ? 0.4228 0.3806 0.2704 0.0047  -0.0756 0.0227  78  ALA A CB  
619  N N   . LEU A 79  ? 0.5425 0.4680 0.3306 0.0131  -0.1312 0.0561  79  LEU A N   
620  C CA  . LEU A 79  ? 0.5431 0.4765 0.3214 0.0129  -0.1606 0.0661  79  LEU A CA  
621  C C   . LEU A 79  ? 0.5672 0.5519 0.4076 0.0283  -0.1733 0.0657  79  LEU A C   
622  O O   . LEU A 79  ? 0.6071 0.6049 0.4839 0.0467  -0.1713 0.0682  79  LEU A O   
623  C CB  . LEU A 79  ? 0.6265 0.5219 0.3646 0.0185  -0.1811 0.0838  79  LEU A CB  
624  C CG  . LEU A 79  ? 0.7046 0.5414 0.3754 0.0028  -0.1661 0.0854  79  LEU A CG  
625  C CD1 . LEU A 79  ? 0.7288 0.5252 0.3569 0.0097  -0.1902 0.1057  79  LEU A CD1 
626  C CD2 . LEU A 79  ? 0.6765 0.4987 0.3067 -0.0231 -0.1553 0.0753  79  LEU A CD2 
627  N N   . THR A 80  ? 0.5182 0.5295 0.3698 0.0195  -0.1839 0.0616  80  THR A N   
628  C CA  . THR A 80  ? 0.4460 0.5065 0.3570 0.0292  -0.1896 0.0577  80  THR A CA  
629  C C   . THR A 80  ? 0.5719 0.6517 0.4998 0.0363  -0.2233 0.0688  80  THR A C   
630  O O   . THR A 80  ? 0.5189 0.5733 0.4065 0.0316  -0.2459 0.0800  80  THR A O   
631  C CB  . THR A 80  ? 0.5102 0.5897 0.4296 0.0139  -0.1755 0.0436  80  THR A CB  
632  O OG1 . THR A 80  ? 0.4900 0.5628 0.3780 -0.0034 -0.1911 0.0441  80  THR A OG1 
633  C CG2 . THR A 80  ? 0.4512 0.5096 0.3528 0.0060  -0.1462 0.0335  80  THR A CG2 
634  N N   . ASP A 81  ? 0.5415 0.6663 0.5303 0.0471  -0.2265 0.0655  81  ASP A N   
635  C CA  . ASP A 81  ? 0.4445 0.5998 0.4640 0.0510  -0.2571 0.0720  81  ASP A CA  
636  C C   . ASP A 81  ? 0.4661 0.6190 0.4522 0.0274  -0.2657 0.0670  81  ASP A C   
637  O O   . ASP A 81  ? 0.4439 0.5987 0.4208 0.0116  -0.2488 0.0552  81  ASP A O   
638  C CB  . ASP A 81  ? 0.4312 0.6355 0.5238 0.0623  -0.2479 0.0642  81  ASP A CB  
639  C CG  . ASP A 81  ? 0.4700 0.7072 0.6033 0.0706  -0.2636 0.0679  81  ASP A CG  
640  O OD1 . ASP A 81  ? 0.4662 0.7081 0.5831 0.0580  -0.2806 0.0680  81  ASP A OD1 
641  O OD2 . ASP A 81  ? 0.4019 0.6595 0.5844 0.0895  -0.2582 0.0697  81  ASP A OD2 
642  N N   . PRO A 82  ? 0.5133 0.6594 0.4795 0.0246  -0.2869 0.0740  82  PRO A N   
643  C CA  . PRO A 82  ? 0.5397 0.6798 0.4714 0.0013  -0.2940 0.0674  82  PRO A CA  
644  C C   . PRO A 82  ? 0.5032 0.6861 0.4790 -0.0071 -0.2892 0.0537  82  PRO A C   
645  O O   . PRO A 82  ? 0.5182 0.6927 0.4648 -0.0284 -0.2886 0.0452  82  PRO A O   
646  C CB  . PRO A 82  ? 0.5977 0.7289 0.5125 0.0048  -0.3211 0.0789  82  PRO A CB  
647  C CG  . PRO A 82  ? 0.5906 0.7385 0.5511 0.0317  -0.3281 0.0899  82  PRO A CG  
648  C CD  . PRO A 82  ? 0.5523 0.6885 0.5191 0.0412  -0.3051 0.0889  82  PRO A CD  
649  N N   . ARG A 83  ? 0.4601 0.6848 0.5027 0.0077  -0.2832 0.0505  83  ARG A N   
650  C CA  . ARG A 83  ? 0.4269 0.6890 0.5108 -0.0014 -0.2748 0.0371  83  ARG A CA  
651  C C   . ARG A 83  ? 0.4599 0.7176 0.5411 -0.0104 -0.2496 0.0286  83  ARG A C   
652  O O   . ARG A 83  ? 0.3688 0.6490 0.4728 -0.0223 -0.2404 0.0180  83  ARG A O   
653  C CB  . ARG A 83  ? 0.4057 0.7136 0.5614 0.0161  -0.2762 0.0369  83  ARG A CB  
654  C CG  . ARG A 83  ? 0.4460 0.7669 0.6145 0.0243  -0.3023 0.0455  83  ARG A CG  
655  C CD  . ARG A 83  ? 0.4281 0.7876 0.6664 0.0448  -0.2992 0.0479  83  ARG A CD  
656  N NE  . ARG A 83  ? 0.4336 0.7768 0.6776 0.0635  -0.2842 0.0545  83  ARG A NE  
657  C CZ  . ARG A 83  ? 0.5294 0.8914 0.8226 0.0840  -0.2799 0.0588  83  ARG A CZ  
658  N NH1 . ARG A 83  ? 0.6052 1.0051 0.9495 0.0895  -0.2896 0.0581  83  ARG A NH1 
659  N NH2 . ARG A 83  ? 0.4363 0.7774 0.7281 0.0990  -0.2649 0.0629  83  ARG A NH2 
660  N N   . ASP A 84  ? 0.3800 0.6079 0.4331 -0.0051 -0.2346 0.0321  84  ASP A N   
661  C CA  . ASP A 84  ? 0.3668 0.5855 0.4159 -0.0083 -0.2008 0.0215  84  ASP A CA  
662  C C   . ASP A 84  ? 0.4145 0.5890 0.4022 -0.0214 -0.1908 0.0199  84  ASP A C   
663  O O   . ASP A 84  ? 0.3851 0.5340 0.3532 -0.0137 -0.1796 0.0231  84  ASP A O   
664  C CB  . ASP A 84  ? 0.3182 0.5433 0.3988 0.0125  -0.1851 0.0231  84  ASP A CB  
665  C CG  . ASP A 84  ? 0.3979 0.6181 0.4796 0.0099  -0.1553 0.0131  84  ASP A CG  
666  O OD1 . ASP A 84  ? 0.4350 0.6564 0.5091 -0.0051 -0.1464 0.0049  84  ASP A OD1 
667  O OD2 . ASP A 84  ? 0.3068 0.5199 0.3959 0.0228  -0.1419 0.0137  84  ASP A OD2 
668  N N   . VAL A 85  ? 0.4477 0.6123 0.4058 -0.0424 -0.1931 0.0136  85  VAL A N   
669  C CA  . VAL A 85  ? 0.4282 0.5485 0.3254 -0.0569 -0.1848 0.0116  85  VAL A CA  
670  C C   . VAL A 85  ? 0.4255 0.5369 0.3108 -0.0743 -0.1623 -0.0025 85  VAL A C   
671  O O   . VAL A 85  ? 0.4674 0.5430 0.3103 -0.0859 -0.1469 -0.0075 85  VAL A O   
672  C CB  . VAL A 85  ? 0.4859 0.5867 0.3391 -0.0675 -0.2138 0.0200  85  VAL A CB  
673  C CG1 . VAL A 85  ? 0.5004 0.6005 0.3599 -0.0485 -0.2354 0.0359  85  VAL A CG1 
674  C CG2 . VAL A 85  ? 0.4959 0.6228 0.3620 -0.0812 -0.2341 0.0160  85  VAL A CG2 
675  N N   . ALA A 86  ? 0.4542 0.5955 0.3768 -0.0766 -0.1583 -0.0094 86  ALA A N   
676  C CA  . ALA A 86  ? 0.4613 0.5920 0.3728 -0.0929 -0.1387 -0.0220 86  ALA A CA  
677  C C   . ALA A 86  ? 0.4450 0.6070 0.4047 -0.0881 -0.1291 -0.0269 86  ALA A C   
678  O O   . ALA A 86  ? 0.4041 0.5944 0.4033 -0.0731 -0.1348 -0.0217 86  ALA A O   
679  C CB  . ALA A 86  ? 0.4547 0.5710 0.3276 -0.1164 -0.1516 -0.0266 86  ALA A CB  
680  N N   . ARG A 87  ? 0.4558 0.6083 0.4095 -0.1014 -0.1122 -0.0372 87  ARG A N   
681  C CA  . ARG A 87  ? 0.4386 0.6136 0.4287 -0.1011 -0.1026 -0.0419 87  ARG A CA  
682  C C   . ARG A 87  ? 0.4323 0.6377 0.4439 -0.1105 -0.1217 -0.0429 87  ARG A C   
683  O O   . ARG A 87  ? 0.4894 0.6927 0.4798 -0.1231 -0.1416 -0.0427 87  ARG A O   
684  C CB  . ARG A 87  ? 0.4411 0.5923 0.4165 -0.1127 -0.0799 -0.0518 87  ARG A CB  
685  C CG  . ARG A 87  ? 0.3503 0.4792 0.3206 -0.1016 -0.0603 -0.0518 87  ARG A CG  
686  C CD  . ARG A 87  ? 0.3656 0.4742 0.3319 -0.1101 -0.0391 -0.0608 87  ARG A CD  
687  N NE  . ARG A 87  ? 0.4138 0.4948 0.3449 -0.1285 -0.0329 -0.0696 87  ARG A NE  
688  C CZ  . ARG A 87  ? 0.4393 0.5172 0.3567 -0.1480 -0.0356 -0.0769 87  ARG A CZ  
689  N NH1 . ARG A 87  ? 0.4649 0.5685 0.4051 -0.1521 -0.0446 -0.0766 87  ARG A NH1 
690  N NH2 . ARG A 87  ? 0.4523 0.4993 0.3316 -0.1655 -0.0274 -0.0861 87  ARG A NH2 
691  N N   . ILE A 88  ? 0.4020 0.6350 0.4557 -0.1056 -0.1157 -0.0442 88  ILE A N   
692  C CA  . ILE A 88  ? 0.3990 0.6658 0.4850 -0.1153 -0.1293 -0.0475 88  ILE A CA  
693  C C   . ILE A 88  ? 0.3715 0.6364 0.4668 -0.1278 -0.1077 -0.0571 88  ILE A C   
694  O O   . ILE A 88  ? 0.3750 0.6497 0.4969 -0.1192 -0.0917 -0.0570 88  ILE A O   
695  C CB  . ILE A 88  ? 0.3805 0.6839 0.5147 -0.0980 -0.1398 -0.0408 88  ILE A CB  
696  C CG1 . ILE A 88  ? 0.3918 0.6893 0.5136 -0.0829 -0.1586 -0.0297 88  ILE A CG1 
697  C CG2 . ILE A 88  ? 0.4117 0.7537 0.5864 -0.1091 -0.1549 -0.0454 88  ILE A CG2 
698  C CD1 . ILE A 88  ? 0.4157 0.7443 0.5858 -0.0630 -0.1662 -0.0232 88  ILE A CD1 
699  N N   . GLU A 89  ? 0.3816 0.6294 0.4504 -0.1494 -0.1062 -0.0658 89  GLU A N   
700  C CA  . GLU A 89  ? 0.4304 0.6690 0.5028 -0.1622 -0.0846 -0.0748 89  GLU A CA  
701  C C   . GLU A 89  ? 0.4158 0.6911 0.5347 -0.1674 -0.0850 -0.0781 89  GLU A C   
702  O O   . GLU A 89  ? 0.3310 0.6011 0.4613 -0.1689 -0.0629 -0.0813 89  GLU A O   
703  C CB  . GLU A 89  ? 0.4501 0.6609 0.4839 -0.1857 -0.0827 -0.0846 89  GLU A CB  
704  C CG  . GLU A 89  ? 0.5769 0.7470 0.5669 -0.1824 -0.0733 -0.0842 89  GLU A CG  
705  C CD  . GLU A 89  ? 0.5593 0.6983 0.5083 -0.2068 -0.0685 -0.0956 89  GLU A CD  
706  O OE1 . GLU A 89  ? 0.5433 0.6896 0.4962 -0.2269 -0.0710 -0.1044 89  GLU A OE1 
707  O OE2 . GLU A 89  ? 0.6475 0.7536 0.5602 -0.2070 -0.0604 -0.0971 89  GLU A OE2 
708  N N   . SER A 90  ? 0.3754 0.6872 0.5229 -0.1702 -0.1097 -0.0773 90  SER A N   
709  C CA  . SER A 90  ? 0.3347 0.6861 0.5350 -0.1767 -0.1093 -0.0825 90  SER A CA  
710  C C   . SER A 90  ? 0.3534 0.7207 0.5897 -0.1568 -0.0934 -0.0777 90  SER A C   
711  O O   . SER A 90  ? 0.3889 0.7810 0.6657 -0.1629 -0.0821 -0.0836 90  SER A O   
712  C CB  . SER A 90  ? 0.4099 0.7869 0.6336 -0.1782 -0.1408 -0.0804 90  SER A CB  
713  O OG  . SER A 90  ? 0.4021 0.7852 0.6279 -0.1573 -0.1609 -0.0688 90  SER A OG  
714  N N   . LYS A 91  ? 0.3294 0.6810 0.5504 -0.1350 -0.0907 -0.0682 91  LYS A N   
715  C CA  . LYS A 91  ? 0.2509 0.6106 0.4966 -0.1172 -0.0746 -0.0643 91  LYS A CA  
716  C C   . LYS A 91  ? 0.3052 0.6253 0.5150 -0.1105 -0.0518 -0.0617 91  LYS A C   
717  O O   . LYS A 91  ? 0.2387 0.5555 0.4533 -0.0943 -0.0420 -0.0568 91  LYS A O   
718  C CB  . LYS A 91  ? 0.2398 0.6179 0.5048 -0.0966 -0.0924 -0.0557 91  LYS A CB  
719  C CG  . LYS A 91  ? 0.3736 0.7953 0.6856 -0.0993 -0.1168 -0.0567 91  LYS A CG  
720  C CD  . LYS A 91  ? 0.4376 0.8697 0.7619 -0.0778 -0.1374 -0.0462 91  LYS A CD  
721  C CE  . LYS A 91  ? 0.4540 0.9166 0.8306 -0.0742 -0.1571 -0.0428 91  LYS A CE  
722  N NZ  . LYS A 91  ? 0.5536 1.0182 0.9264 -0.0945 -0.1760 -0.0470 91  LYS A NZ  
723  N N   . THR A 92  ? 0.2718 0.5613 0.4469 -0.1227 -0.0440 -0.0651 92  THR A N   
724  C CA  . THR A 92  ? 0.3646 0.6170 0.5100 -0.1167 -0.0254 -0.0624 92  THR A CA  
725  C C   . THR A 92  ? 0.3340 0.5751 0.4799 -0.1312 -0.0055 -0.0682 92  THR A C   
726  O O   . THR A 92  ? 0.3906 0.6222 0.5264 -0.1493 -0.0036 -0.0752 92  THR A O   
727  C CB  . THR A 92  ? 0.3072 0.5302 0.4161 -0.1175 -0.0299 -0.0619 92  THR A CB  
728  O OG1 . THR A 92  ? 0.2646 0.4971 0.3703 -0.1081 -0.0484 -0.0571 92  THR A OG1 
729  C CG2 . THR A 92  ? 0.3417 0.5321 0.4304 -0.1069 -0.0146 -0.0579 92  THR A CG2 
730  N N   . VAL A 93  ? 0.3835 0.6213 0.5369 -0.1247 0.0105  -0.0655 93  VAL A N   
731  C CA  . VAL A 93  ? 0.3717 0.5996 0.5269 -0.1392 0.0309  -0.0704 93  VAL A CA  
732  C C   . VAL A 93  ? 0.3615 0.5462 0.4824 -0.1323 0.0463  -0.0638 93  VAL A C   
733  O O   . VAL A 93  ? 0.3367 0.5090 0.4432 -0.1147 0.0421  -0.0560 93  VAL A O   
734  C CB  . VAL A 93  ? 0.3686 0.6297 0.5636 -0.1420 0.0390  -0.0743 93  VAL A CB  
735  C CG1 . VAL A 93  ? 0.3350 0.6417 0.5711 -0.1482 0.0198  -0.0802 93  VAL A CG1 
736  C CG2 . VAL A 93  ? 0.2943 0.5543 0.4897 -0.1223 0.0437  -0.0675 93  VAL A CG2 
737  N N   . ILE A 94  ? 0.3839 0.5445 0.4917 -0.1469 0.0630  -0.0669 94  ILE A N   
738  C CA  . ILE A 94  ? 0.4134 0.5301 0.4883 -0.1422 0.0770  -0.0596 94  ILE A CA  
739  C C   . ILE A 94  ? 0.4587 0.5700 0.5356 -0.1549 0.0985  -0.0620 94  ILE A C   
740  O O   . ILE A 94  ? 0.4303 0.5570 0.5271 -0.1743 0.1069  -0.0716 94  ILE A O   
741  C CB  . ILE A 94  ? 0.4497 0.5307 0.5004 -0.1472 0.0791  -0.0596 94  ILE A CB  
742  C CG1 . ILE A 94  ? 0.4028 0.4877 0.4518 -0.1364 0.0623  -0.0591 94  ILE A CG1 
743  C CG2 . ILE A 94  ? 0.4273 0.4618 0.4466 -0.1408 0.0905  -0.0502 94  ILE A CG2 
744  C CD1 . ILE A 94  ? 0.5341 0.5846 0.5642 -0.1405 0.0674  -0.0610 94  ILE A CD1 
745  N N   . ILE A 95  ? 0.3963 0.4844 0.4512 -0.1457 0.1077  -0.0541 95  ILE A N   
746  C CA  . ILE A 95  ? 0.4813 0.5584 0.5308 -0.1578 0.1315  -0.0561 95  ILE A CA  
747  C C   . ILE A 95  ? 0.6017 0.6206 0.6031 -0.1612 0.1432  -0.0476 95  ILE A C   
748  O O   . ILE A 95  ? 0.5577 0.5466 0.5276 -0.1454 0.1339  -0.0363 95  ILE A O   
749  C CB  . ILE A 95  ? 0.5001 0.5916 0.5563 -0.1473 0.1357  -0.0546 95  ILE A CB  
750  C CG1 . ILE A 95  ? 0.4483 0.5968 0.5577 -0.1439 0.1255  -0.0627 95  ILE A CG1 
751  C CG2 . ILE A 95  ? 0.5490 0.6176 0.5884 -0.1610 0.1646  -0.0565 95  ILE A CG2 
752  C CD1 . ILE A 95  ? 0.4373 0.5996 0.5501 -0.1234 0.1013  -0.0573 95  ILE A CD1 
753  N N   . THR A 96  ? 0.5772 0.5795 0.5740 -0.1819 0.1623  -0.0529 96  THR A N   
754  C CA  . THR A 96  ? 0.6711 0.6137 0.6206 -0.1874 0.1765  -0.0444 96  THR A CA  
755  C C   . THR A 96  ? 0.7527 0.6867 0.7003 -0.2108 0.2062  -0.0514 96  THR A C   
756  O O   . THR A 96  ? 0.7136 0.6915 0.7052 -0.2248 0.2146  -0.0650 96  THR A O   
757  C CB  . THR A 96  ? 0.6429 0.5594 0.5819 -0.1896 0.1708  -0.0432 96  THR A CB  
758  O OG1 . THR A 96  ? 0.6179 0.5646 0.5902 -0.2085 0.1749  -0.0578 96  THR A OG1 
759  C CG2 . THR A 96  ? 0.6133 0.5314 0.5520 -0.1667 0.1460  -0.0363 96  THR A CG2 
760  N N   . GLN A 97  ? 0.7984 0.6743 0.6949 -0.2152 0.2219  -0.0417 97  GLN A N   
761  C CA  . GLN A 97  ? 0.9021 0.7599 0.7886 -0.2397 0.2546  -0.0480 97  GLN A CA  
762  C C   . GLN A 97  ? 0.8450 0.7171 0.7614 -0.2625 0.2655  -0.0612 97  GLN A C   
763  O O   . GLN A 97  ? 0.8232 0.7269 0.7753 -0.2825 0.2846  -0.0753 97  GLN A O   
764  C CB  . GLN A 97  ? 1.0277 0.8099 0.8432 -0.2405 0.2665  -0.0328 97  GLN A CB  
765  C CG  . GLN A 97  ? 1.1839 0.9360 0.9786 -0.2679 0.3040  -0.0383 97  GLN A CG  
766  C CD  . GLN A 97  ? 1.2583 1.0444 1.0770 -0.2736 0.3213  -0.0496 97  GLN A CD  
767  O OE1 . GLN A 97  ? 1.2673 1.0762 1.0930 -0.2593 0.3117  -0.0474 97  GLN A OE1 
768  N NE2 . GLN A 97  ? 1.2319 1.0226 1.0668 -0.2891 0.3419  -0.0633 97  GLN A NE2 
769  N N   . GLU A 98  ? 0.7780 0.6282 0.6833 -0.2603 0.2540  -0.0580 98  GLU A N   
770  C CA  . GLU A 98  ? 0.7946 0.6528 0.7220 -0.2824 0.2624  -0.0709 98  GLU A CA  
771  C C   . GLU A 98  ? 0.7178 0.6215 0.6829 -0.2748 0.2361  -0.0782 98  GLU A C   
772  O O   . GLU A 98  ? 0.6593 0.5573 0.6137 -0.2523 0.2147  -0.0693 98  GLU A O   
773  C CB  . GLU A 98  ? 0.9031 0.6913 0.7830 -0.2893 0.2747  -0.0632 98  GLU A CB  
774  C CG  . GLU A 98  ? 1.0128 0.7486 0.8465 -0.2959 0.2981  -0.0552 98  GLU A CG  
775  C CD  . GLU A 98  ? 1.0937 0.8574 0.9533 -0.3127 0.3161  -0.0718 98  GLU A CD  
776  O OE1 . GLU A 98  ? 1.1260 0.9261 1.0262 -0.3250 0.3147  -0.0876 98  GLU A OE1 
777  O OE2 . GLU A 98  ? 1.2513 0.9991 1.0898 -0.3138 0.3314  -0.0693 98  GLU A OE2 
778  N N   . GLN A 99  ? 0.6389 0.5868 0.6473 -0.2949 0.2377  -0.0948 99  GLN A N   
779  C CA  . GLN A 99  ? 0.6542 0.6414 0.6914 -0.2915 0.2124  -0.1021 99  GLN A CA  
780  C C   . GLN A 99  ? 0.6611 0.6071 0.6684 -0.2905 0.2080  -0.1002 99  GLN A C   
781  O O   . GLN A 99  ? 0.5922 0.5508 0.6030 -0.2772 0.1869  -0.0995 99  GLN A O   
782  C CB  . GLN A 99  ? 0.5844 0.6228 0.6689 -0.3105 0.2098  -0.1189 99  GLN A CB  
783  C CG  . GLN A 99  ? 0.5590 0.6364 0.6678 -0.3100 0.1818  -0.1259 99  GLN A CG  
784  C CD  . GLN A 99  ? 0.6500 0.7691 0.7967 -0.3237 0.1728  -0.1393 99  GLN A CD  
785  O OE1 . GLN A 99  ? 0.6932 0.8170 0.8552 -0.3337 0.1888  -0.1447 99  GLN A OE1 
786  N NE2 . GLN A 99  ? 0.6770 0.8243 0.8372 -0.3246 0.1468  -0.1442 99  GLN A NE2 
787  N N   . ARG A 100 ? 0.6455 0.5393 0.6228 -0.3046 0.2297  -0.0997 100 ARG A N   
788  C CA  . ARG A 100 ? 0.6731 0.5245 0.6255 -0.3046 0.2296  -0.0994 100 ARG A CA  
789  C C   . ARG A 100 ? 0.6720 0.4964 0.6019 -0.2734 0.2152  -0.0838 100 ARG A C   
790  O O   . ARG A 100 ? 0.6670 0.4713 0.5894 -0.2683 0.2103  -0.0854 100 ARG A O   
791  C CB  . ARG A 100 ? 0.7450 0.5449 0.6684 -0.3174 0.2528  -0.1000 100 ARG A CB  
792  C CG  . ARG A 100 ? 0.8567 0.6204 0.7629 -0.3205 0.2551  -0.1051 100 ARG A CG  
793  C CD  . ARG A 100 ? 0.9828 0.7026 0.8637 -0.3321 0.2767  -0.1073 100 ARG A CD  
794  N NE  . ARG A 100 ? 1.0159 0.7064 0.8843 -0.3363 0.2806  -0.1148 100 ARG A NE  
795  C CZ  . ARG A 100 ? 1.1215 0.7775 0.9709 -0.3484 0.2984  -0.1203 100 ARG A CZ  
796  N NH1 . ARG A 100 ? 1.1466 0.7913 0.9863 -0.3583 0.3142  -0.1195 100 ARG A NH1 
797  N NH2 . ARG A 100 ? 1.1005 0.7313 0.9394 -0.3511 0.3022  -0.1276 100 ARG A NH2 
798  N N   . ASP A 101 ? 0.6753 0.4989 0.5957 -0.2535 0.2093  -0.0699 101 ASP A N   
799  C CA  . ASP A 101 ? 0.7162 0.5218 0.6224 -0.2245 0.1923  -0.0561 101 ASP A CA  
800  C C   . ASP A 101 ? 0.6186 0.4705 0.5533 -0.2126 0.1702  -0.0614 101 ASP A C   
801  O O   . ASP A 101 ? 0.6300 0.4685 0.5605 -0.1941 0.1588  -0.0558 101 ASP A O   
802  C CB  . ASP A 101 ? 0.7695 0.5599 0.6535 -0.2096 0.1907  -0.0408 101 ASP A CB  
803  C CG  . ASP A 101 ? 0.9430 0.6729 0.7855 -0.2180 0.2105  -0.0315 101 ASP A CG  
804  O OD1 . ASP A 101 ? 1.0017 0.6904 0.8294 -0.2247 0.2201  -0.0315 101 ASP A OD1 
805  O OD2 . ASP A 101 ? 1.0785 0.7980 0.8998 -0.2186 0.2176  -0.0242 101 ASP A OD2 
806  N N   . THR A 102 ? 0.5961 0.5012 0.5611 -0.2229 0.1642  -0.0720 102 THR A N   
807  C CA  . THR A 102 ? 0.5565 0.5029 0.5439 -0.2130 0.1427  -0.0760 102 THR A CA  
808  C C   . THR A 102 ? 0.5279 0.4809 0.5217 -0.2294 0.1401  -0.0897 102 THR A C   
809  O O   . THR A 102 ? 0.5354 0.4829 0.5240 -0.2198 0.1303  -0.0902 102 THR A O   
810  C CB  . THR A 102 ? 0.5237 0.5219 0.5401 -0.2123 0.1345  -0.0781 102 THR A CB  
811  O OG1 . THR A 102 ? 0.5641 0.5535 0.5694 -0.1949 0.1354  -0.0659 102 THR A OG1 
812  C CG2 . THR A 102 ? 0.4496 0.4881 0.4873 -0.2055 0.1119  -0.0824 102 THR A CG2 
813  N N   . VAL A 103 ? 0.5328 0.4965 0.5367 -0.2558 0.1494  -0.1019 103 VAL A N   
814  C CA  . VAL A 103 ? 0.5487 0.5175 0.5541 -0.2757 0.1458  -0.1165 103 VAL A CA  
815  C C   . VAL A 103 ? 0.5889 0.5254 0.5826 -0.3014 0.1684  -0.1254 103 VAL A C   
816  O O   . VAL A 103 ? 0.6481 0.5776 0.6442 -0.3090 0.1841  -0.1231 103 VAL A O   
817  C CB  . VAL A 103 ? 0.5533 0.5813 0.5901 -0.2850 0.1256  -0.1250 103 VAL A CB  
818  C CG1 . VAL A 103 ? 0.4895 0.5424 0.5329 -0.2605 0.1039  -0.1165 103 VAL A CG1 
819  C CG2 . VAL A 103 ? 0.5128 0.5733 0.5810 -0.2973 0.1322  -0.1284 103 VAL A CG2 
820  N N   . PRO A 104 ? 0.6173 0.5296 0.5953 -0.3164 0.1730  -0.1364 104 PRO A N   
821  C CA  . PRO A 104 ? 0.6627 0.5541 0.6300 -0.3328 0.1882  -0.1446 104 PRO A CA  
822  C C   . PRO A 104 ? 0.6520 0.5943 0.6490 -0.3476 0.1793  -0.1534 104 PRO A C   
823  O O   . PRO A 104 ? 0.6262 0.6170 0.6476 -0.3470 0.1569  -0.1563 104 PRO A O   
824  C CB  . PRO A 104 ? 0.6846 0.5497 0.6294 -0.3379 0.1888  -0.1540 104 PRO A CB  
825  C CG  . PRO A 104 ? 0.6610 0.5165 0.6001 -0.3204 0.1812  -0.1479 104 PRO A CG  
826  C CD  . PRO A 104 ? 0.6125 0.5146 0.5766 -0.3091 0.1631  -0.1397 104 PRO A CD  
827  N N   . ILE A 105 ? 0.6843 0.6140 0.6807 -0.3600 0.1967  -0.1572 105 ILE A N   
828  C CA  . ILE A 105 ? 0.6839 0.6592 0.7134 -0.3750 0.1909  -0.1668 105 ILE A CA  
829  C C   . ILE A 105 ? 0.7027 0.6881 0.7297 -0.3909 0.1784  -0.1799 105 ILE A C   
830  O O   . ILE A 105 ? 0.7452 0.6911 0.7446 -0.4020 0.1932  -0.1864 105 ILE A O   
831  C CB  . ILE A 105 ? 0.7314 0.6870 0.7595 -0.3845 0.2160  -0.1677 105 ILE A CB  
832  C CG1 . ILE A 105 ? 0.7080 0.6457 0.7280 -0.3693 0.2286  -0.1534 105 ILE A CG1 
833  C CG2 . ILE A 105 ? 0.7174 0.7230 0.7873 -0.3999 0.2106  -0.1787 105 ILE A CG2 
834  C CD1 . ILE A 105 ? 0.6959 0.6845 0.7502 -0.3572 0.2130  -0.1486 105 ILE A CD1 
835  N N   . PRO A 106 ? 0.6775 0.7117 0.7294 -0.3921 0.1511  -0.1833 106 PRO A N   
836  C CA  . PRO A 106 ? 0.7020 0.7405 0.7433 -0.4074 0.1368  -0.1941 106 PRO A CA  
837  C C   . PRO A 106 ? 0.7410 0.7830 0.7928 -0.4300 0.1454  -0.2057 106 PRO A C   
838  O O   . PRO A 106 ? 0.7410 0.8002 0.8217 -0.4341 0.1557  -0.2063 106 PRO A O   
839  C CB  . PRO A 106 ? 0.6677 0.7589 0.7366 -0.4010 0.1031  -0.1917 106 PRO A CB  
840  C CG  . PRO A 106 ? 0.6224 0.7276 0.7074 -0.3792 0.1025  -0.1794 106 PRO A CG  
841  C CD  . PRO A 106 ? 0.6302 0.7143 0.7181 -0.3785 0.1312  -0.1764 106 PRO A CD  
842  N N   . LYS A 107 ? 0.7785 0.8022 0.8049 -0.4457 0.1428  -0.2158 107 LYS A N   
843  C CA  . LYS A 107 ? 0.8209 0.8449 0.8540 -0.4694 0.1510  -0.2281 107 LYS A CA  
844  C C   . LYS A 107 ? 0.8127 0.8972 0.8925 -0.4801 0.1231  -0.2331 107 LYS A C   
845  O O   . LYS A 107 ? 0.8477 0.9506 0.9579 -0.4942 0.1300  -0.2399 107 LYS A O   
846  C CB  . LYS A 107 ? 0.8694 0.8489 0.8565 -0.4831 0.1603  -0.2376 107 LYS A CB  
847  C CG  . LYS A 107 ? 0.9197 0.8857 0.9052 -0.5071 0.1769  -0.2502 107 LYS A CG  
848  C CD  . LYS A 107 ? 0.9700 0.8869 0.9071 -0.5190 0.1901  -0.2593 107 LYS A CD  
849  C CE  . LYS A 107 ? 1.1889 1.0910 1.1238 -0.5435 0.2079  -0.2723 107 LYS A CE  
850  N NZ  . LYS A 107 ? 1.2832 1.1361 1.1706 -0.5556 0.2231  -0.2820 107 LYS A NZ  
851  N N   . SER A 108 ? 0.8425 0.9573 0.9302 -0.4730 0.0911  -0.2294 108 SER A N   
852  C CA  . SER A 108 ? 0.8400 1.0096 0.9731 -0.4812 0.0598  -0.2327 108 SER A CA  
853  C C   . SER A 108 ? 0.7896 1.0024 0.9581 -0.4595 0.0355  -0.2209 108 SER A C   
854  O O   . SER A 108 ? 0.7751 1.0226 0.9926 -0.4525 0.0379  -0.2173 108 SER A O   
855  C CB  . SER A 108 ? 0.8806 1.0431 0.9865 -0.4983 0.0383  -0.2412 108 SER A CB  
856  O OG  . SER A 108 ? 0.9721 1.1052 1.0575 -0.5215 0.0583  -0.2540 108 SER A OG  
857  N N   . GLY A 109 ? 0.7263 0.9355 0.8695 -0.4490 0.0140  -0.2152 109 GLY A N   
858  C CA  . GLY A 109 ? 0.6842 0.9322 0.8580 -0.4286 -0.0113 -0.2041 109 GLY A CA  
859  C C   . GLY A 109 ? 0.6460 0.8904 0.8258 -0.4070 0.0076  -0.1940 109 GLY A C   
860  O O   . GLY A 109 ? 0.6896 0.9093 0.8623 -0.4083 0.0394  -0.1952 109 GLY A O   
861  N N   . GLN A 110 ? 0.6048 0.8716 0.7959 -0.3870 -0.0124 -0.1837 110 GLN A N   
862  C CA  . GLN A 110 ? 0.5651 0.8271 0.7573 -0.3667 0.0033  -0.1742 110 GLN A CA  
863  C C   . GLN A 110 ? 0.5660 0.7820 0.7022 -0.3607 0.0121  -0.1714 110 GLN A C   
864  O O   . GLN A 110 ? 0.5928 0.7869 0.6920 -0.3690 0.0024  -0.1754 110 GLN A O   
865  C CB  . GLN A 110 ? 0.5634 0.8720 0.7985 -0.3472 -0.0201 -0.1648 110 GLN A CB  
866  C CG  . GLN A 110 ? 0.6017 0.9154 0.8183 -0.3382 -0.0526 -0.1591 110 GLN A CG  
867  C CD  . GLN A 110 ? 0.5207 0.8763 0.7800 -0.3166 -0.0740 -0.1487 110 GLN A CD  
868  O OE1 . GLN A 110 ? 0.4795 0.8662 0.7895 -0.3103 -0.0666 -0.1471 110 GLN A OE1 
869  N NE2 . GLN A 110 ? 0.4880 0.8411 0.7252 -0.3050 -0.0985 -0.1415 110 GLN A NE2 
870  N N   . SER A 111 ? 0.5402 0.7402 0.6708 -0.3466 0.0316  -0.1645 111 SER A N   
871  C CA  . SER A 111 ? 0.5418 0.6971 0.6272 -0.3403 0.0431  -0.1619 111 SER A CA  
872  C C   . SER A 111 ? 0.5215 0.6880 0.5962 -0.3270 0.0194  -0.1558 111 SER A C   
873  O O   . SER A 111 ? 0.4909 0.6952 0.5955 -0.3127 0.0026  -0.1484 111 SER A O   
874  C CB  . SER A 111 ? 0.5259 0.6588 0.6106 -0.3298 0.0691  -0.1554 111 SER A CB  
875  O OG  . SER A 111 ? 0.5287 0.6189 0.5770 -0.3224 0.0787  -0.1524 111 SER A OG  
876  N N   . GLN A 112 ? 0.5614 0.6919 0.5920 -0.3313 0.0202  -0.1592 112 GLN A N   
877  C CA  . GLN A 112 ? 0.5337 0.6620 0.5436 -0.3198 0.0042  -0.1539 112 GLN A CA  
878  C C   . GLN A 112 ? 0.5392 0.6373 0.5335 -0.3065 0.0227  -0.1498 112 GLN A C   
879  O O   . GLN A 112 ? 0.5944 0.6857 0.5704 -0.2952 0.0139  -0.1455 112 GLN A O   
880  C CB  . GLN A 112 ? 0.5772 0.6822 0.5457 -0.3334 -0.0049 -0.1607 112 GLN A CB  
881  C CG  . GLN A 112 ? 0.6772 0.8085 0.6572 -0.3477 -0.0277 -0.1648 112 GLN A CG  
882  C CD  . GLN A 112 ? 0.6498 0.7552 0.5822 -0.3603 -0.0385 -0.1697 112 GLN A CD  
883  O OE1 . GLN A 112 ? 0.7304 0.8040 0.6241 -0.3556 -0.0312 -0.1686 112 GLN A OE1 
884  N NE2 . GLN A 112 ? 0.7400 0.8578 0.6751 -0.3771 -0.0548 -0.1758 112 GLN A NE2 
885  N N   . LEU A 113 ? 0.5770 0.6532 0.5771 -0.3037 0.0477  -0.1487 113 LEU A N   
886  C CA  . LEU A 113 ? 0.5066 0.5463 0.4911 -0.2815 0.0646  -0.1400 113 LEU A CA  
887  C C   . LEU A 113 ? 0.5453 0.6037 0.5529 -0.2547 0.0622  -0.1250 113 LEU A C   
888  O O   . LEU A 113 ? 0.5242 0.5548 0.5235 -0.2364 0.0743  -0.1167 113 LEU A O   
889  C CB  . LEU A 113 ? 0.5892 0.5828 0.5581 -0.2916 0.0919  -0.1455 113 LEU A CB  
890  C CG  . LEU A 113 ? 0.6041 0.5709 0.5447 -0.3163 0.0982  -0.1610 113 LEU A CG  
891  C CD1 . LEU A 113 ? 0.6195 0.5472 0.5500 -0.3243 0.1238  -0.1650 113 LEU A CD1 
892  C CD2 . LEU A 113 ? 0.5923 0.5332 0.5060 -0.3099 0.0994  -0.1636 113 LEU A CD2 
893  N N   . GLY A 114 ? 0.5495 0.6529 0.5864 -0.2521 0.0466  -0.1218 114 GLY A N   
894  C CA  . GLY A 114 ? 0.4939 0.6147 0.5507 -0.2289 0.0452  -0.1094 114 GLY A CA  
895  C C   . GLY A 114 ? 0.4614 0.6233 0.5559 -0.2358 0.0419  -0.1113 114 GLY A C   
896  O O   . GLY A 114 ? 0.5164 0.6879 0.6238 -0.2586 0.0468  -0.1214 114 GLY A O   
897  N N   . ARG A 115 ? 0.5026 0.6895 0.6180 -0.2164 0.0350  -0.1025 115 ARG A N   
898  C CA  . ARG A 115 ? 0.4519 0.6786 0.6091 -0.2189 0.0350  -0.1042 115 ARG A CA  
899  C C   . ARG A 115 ? 0.4482 0.6563 0.6023 -0.2101 0.0584  -0.0982 115 ARG A C   
900  O O   . ARG A 115 ? 0.4230 0.6188 0.5641 -0.1888 0.0584  -0.0880 115 ARG A O   
901  C CB  . ARG A 115 ? 0.4575 0.7246 0.6415 -0.2042 0.0111  -0.0996 115 ARG A CB  
902  C CG  . ARG A 115 ? 0.5418 0.8390 0.7413 -0.2182 -0.0142 -0.1064 115 ARG A CG  
903  C CD  . ARG A 115 ? 0.6654 1.0125 0.9134 -0.2076 -0.0325 -0.1036 115 ARG A CD  
904  N NE  . ARG A 115 ? 0.7900 1.1583 1.0789 -0.2074 -0.0131 -0.1064 115 ARG A NE  
905  C CZ  . ARG A 115 ? 0.7103 1.1209 1.0511 -0.1989 -0.0212 -0.1060 115 ARG A CZ  
906  N NH1 . ARG A 115 ? 0.7170 1.1501 1.0742 -0.1873 -0.0515 -0.1000 115 ARG A NH1 
907  N NH2 . ARG A 115 ? 0.5837 1.0040 0.9547 -0.1992 0.0027  -0.1093 115 ARG A NH2 
908  N N   . TRP A 116 ? 0.4506 0.6540 0.6134 -0.2282 0.0783  -0.1048 116 TRP A N   
909  C CA  . TRP A 116 ? 0.4540 0.6359 0.6083 -0.2242 0.1021  -0.0997 116 TRP A CA  
910  C C   . TRP A 116 ? 0.4517 0.6756 0.6500 -0.2234 0.1068  -0.1030 116 TRP A C   
911  O O   . TRP A 116 ? 0.4214 0.6897 0.6643 -0.2352 0.0982  -0.1126 116 TRP A O   
912  C CB  . TRP A 116 ? 0.4853 0.6302 0.6189 -0.2453 0.1256  -0.1046 116 TRP A CB  
913  C CG  . TRP A 116 ? 0.4877 0.6053 0.6059 -0.2448 0.1510  -0.0992 116 TRP A CG  
914  C CD1 . TRP A 116 ? 0.5307 0.6021 0.6066 -0.2296 0.1580  -0.0862 116 TRP A CD1 
915  C CD2 . TRP A 116 ? 0.5098 0.6425 0.6527 -0.2617 0.1729  -0.1070 116 TRP A CD2 
916  N NE1 . TRP A 116 ? 0.5834 0.6356 0.6480 -0.2366 0.1821  -0.0845 116 TRP A NE1 
917  C CE2 . TRP A 116 ? 0.5458 0.6345 0.6515 -0.2567 0.1942  -0.0978 116 TRP A CE2 
918  C CE3 . TRP A 116 ? 0.5118 0.6904 0.7055 -0.2805 0.1759  -0.1210 116 TRP A CE3 
919  C CZ2 . TRP A 116 ? 0.5667 0.6524 0.6798 -0.2719 0.2227  -0.1029 116 TRP A CZ2 
920  C CZ3 . TRP A 116 ? 0.5279 0.7036 0.7316 -0.2867 0.1992  -0.1246 116 TRP A CZ3 
921  C CH2 . TRP A 116 ? 0.5196 0.6493 0.6830 -0.2850 0.2250  -0.1168 116 TRP A CH2 
922  N N   . MET A 117 ? 0.4212 0.6300 0.6076 -0.2097 0.1202  -0.0954 117 MET A N   
923  C CA  . MET A 117 ? 0.4502 0.6906 0.6742 -0.2079 0.1314  -0.0991 117 MET A CA  
924  C C   . MET A 117 ? 0.4284 0.6277 0.6191 -0.2095 0.1607  -0.0949 117 MET A C   
925  O O   . MET A 117 ? 0.4780 0.6332 0.6193 -0.1976 0.1604  -0.0837 117 MET A O   
926  C CB  . MET A 117 ? 0.4287 0.6986 0.6729 -0.1844 0.1114  -0.0939 117 MET A CB  
927  C CG  . MET A 117 ? 0.4481 0.7470 0.7319 -0.1797 0.1254  -0.0980 117 MET A CG  
928  S SD  . MET A 117 ? 0.4668 0.7902 0.7678 -0.1507 0.1037  -0.0909 117 MET A SD  
929  C CE  . MET A 117 ? 0.5072 0.8698 0.8391 -0.1516 0.0670  -0.0924 117 MET A CE  
930  N N   . SER A 118 ? 0.4226 0.6355 0.6402 -0.2251 0.1855  -0.1042 118 SER A N   
931  C CA  . SER A 118 ? 0.5384 0.7078 0.7186 -0.2304 0.2163  -0.1010 118 SER A CA  
932  C C   . SER A 118 ? 0.5687 0.7308 0.7328 -0.2092 0.2165  -0.0933 118 SER A C   
933  O O   . SER A 118 ? 0.5435 0.7431 0.7402 -0.1926 0.1985  -0.0935 118 SER A O   
934  C CB  . SER A 118 ? 0.5239 0.7069 0.7356 -0.2504 0.2426  -0.1137 118 SER A CB  
935  O OG  . SER A 118 ? 0.5147 0.7445 0.7801 -0.2402 0.2408  -0.1201 118 SER A OG  
936  N N   . GLU A 119 ? 0.6257 0.7347 0.7348 -0.2108 0.2367  -0.0863 119 GLU A N   
937  C CA  . GLU A 119 ? 0.7150 0.8110 0.8018 -0.1951 0.2402  -0.0807 119 GLU A CA  
938  C C   . GLU A 119 ? 0.6412 0.7793 0.7811 -0.1974 0.2587  -0.0933 119 GLU A C   
939  O O   . GLU A 119 ? 0.5895 0.7480 0.7456 -0.1794 0.2492  -0.0925 119 GLU A O   
940  C CB  . GLU A 119 ? 0.8695 0.8964 0.8819 -0.2005 0.2584  -0.0712 119 GLU A CB  
941  C CG  . GLU A 119 ? 1.0143 0.9972 0.9754 -0.1916 0.2370  -0.0563 119 GLU A CG  
942  C CD  . GLU A 119 ? 1.1159 1.0804 1.0714 -0.2078 0.2420  -0.0572 119 GLU A CD  
943  O OE1 . GLU A 119 ? 0.9625 0.9529 0.9559 -0.2274 0.2595  -0.0701 119 GLU A OE1 
944  O OE2 . GLU A 119 ? 1.2133 1.1375 1.1290 -0.2012 0.2287  -0.0455 119 GLU A OE2 
945  N N   . GLU A 120 ? 0.6385 0.7883 0.8079 -0.2181 0.2847  -0.1053 120 GLU A N   
946  C CA  . GLU A 120 ? 0.7091 0.8921 0.9287 -0.2138 0.2960  -0.1162 120 GLU A CA  
947  C C   . GLU A 120 ? 0.5661 0.8146 0.8566 -0.1987 0.2692  -0.1197 120 GLU A C   
948  O O   . GLU A 120 ? 0.5489 0.8196 0.8696 -0.1843 0.2710  -0.1225 120 GLU A O   
949  C CB  . GLU A 120 ? 0.6296 0.8086 0.8649 -0.2324 0.3161  -0.1265 120 GLU A CB  
950  C CG  . GLU A 120 ? 0.9384 1.0496 1.1043 -0.2462 0.3454  -0.1242 120 GLU A CG  
951  C CD  . GLU A 120 ? 1.0270 1.0907 1.1329 -0.2549 0.3398  -0.1132 120 GLU A CD  
952  O OE1 . GLU A 120 ? 0.9036 0.9890 1.0261 -0.2528 0.3163  -0.1099 120 GLU A OE1 
953  O OE2 . GLU A 120 ? 1.1562 1.1580 1.1971 -0.2634 0.3583  -0.1077 120 GLU A OE2 
954  N N   . ASP A 121 ? 0.4673 0.7428 0.7811 -0.2016 0.2432  -0.1192 121 ASP A N   
955  C CA  . ASP A 121 ? 0.4775 0.8087 0.8495 -0.1873 0.2128  -0.1202 121 ASP A CA  
956  C C   . ASP A 121 ? 0.4666 0.7983 0.8237 -0.1664 0.1965  -0.1119 121 ASP A C   
957  O O   . ASP A 121 ? 0.4074 0.7746 0.8074 -0.1498 0.1843  -0.1127 121 ASP A O   
958  C CB  . ASP A 121 ? 0.3881 0.7388 0.7756 -0.1978 0.1882  -0.1216 121 ASP A CB  
959  C CG  . ASP A 121 ? 0.4821 0.8403 0.8944 -0.2162 0.1999  -0.1310 121 ASP A CG  
960  O OD1 . ASP A 121 ? 0.5221 0.8901 0.9629 -0.2166 0.2198  -0.1373 121 ASP A OD1 
961  O OD2 . ASP A 121 ? 0.4828 0.8363 0.8860 -0.2309 0.1903  -0.1329 121 ASP A OD2 
962  N N   . PHE A 122 ? 0.4129 0.6946 0.7003 -0.1609 0.1893  -0.1001 122 PHE A N   
963  C CA  . PHE A 122 ? 0.4361 0.7079 0.6991 -0.1373 0.1679  -0.0896 122 PHE A CA  
964  C C   . PHE A 122 ? 0.4316 0.6926 0.6874 -0.1267 0.1864  -0.0903 122 PHE A C   
965  O O   . PHE A 122 ? 0.4143 0.6876 0.6795 -0.1075 0.1712  -0.0866 122 PHE A O   
966  C CB  . PHE A 122 ? 0.4078 0.6323 0.6064 -0.1344 0.1557  -0.0781 122 PHE A CB  
967  C CG  . PHE A 122 ? 0.4670 0.6775 0.6389 -0.1127 0.1380  -0.0685 122 PHE A CG  
968  C CD1 . PHE A 122 ? 0.3898 0.6302 0.5875 -0.0986 0.1118  -0.0664 122 PHE A CD1 
969  C CD2 . PHE A 122 ? 0.4650 0.6309 0.5843 -0.1078 0.1471  -0.0616 122 PHE A CD2 
970  C CE1 . PHE A 122 ? 0.4033 0.6303 0.5781 -0.0806 0.0980  -0.0587 122 PHE A CE1 
971  C CE2 . PHE A 122 ? 0.4966 0.6519 0.5950 -0.0898 0.1304  -0.0542 122 PHE A CE2 
972  C CZ  . PHE A 122 ? 0.4070 0.5935 0.5348 -0.0765 0.1072  -0.0533 122 PHE A CZ  
973  N N   . GLU A 123 ? 0.4398 0.6735 0.6744 -0.1402 0.2204  -0.0953 123 GLU A N   
974  C CA  . GLU A 123 ? 0.4881 0.7085 0.7133 -0.1334 0.2423  -0.0984 123 GLU A CA  
975  C C   . GLU A 123 ? 0.4177 0.6930 0.7199 -0.1230 0.2436  -0.1080 123 GLU A C   
976  O O   . GLU A 123 ? 0.3963 0.6720 0.6995 -0.1057 0.2408  -0.1067 123 GLU A O   
977  C CB  . GLU A 123 ? 0.5990 0.7806 0.7894 -0.1539 0.2823  -0.1040 123 GLU A CB  
978  C CG  . GLU A 123 ? 0.7659 0.8792 0.8656 -0.1575 0.2826  -0.0917 123 GLU A CG  
979  C CD  . GLU A 123 ? 1.0011 1.0689 1.0568 -0.1761 0.3233  -0.0965 123 GLU A CD  
980  O OE1 . GLU A 123 ? 0.9937 1.0798 1.0897 -0.1811 0.3433  -0.1088 123 GLU A OE1 
981  O OE2 . GLU A 123 ? 1.1536 1.1610 1.1310 -0.1802 0.3237  -0.0856 123 GLU A OE2 
982  N N   . LYS A 124 ? 0.4270 0.7441 0.7909 -0.1313 0.2433  -0.1162 124 LYS A N   
983  C CA  . LYS A 124 ? 0.3556 0.7175 0.7876 -0.1164 0.2331  -0.1203 124 LYS A CA  
984  C C   . LYS A 124 ? 0.3120 0.7029 0.7661 -0.0966 0.1978  -0.1130 124 LYS A C   
985  O O   . LYS A 124 ? 0.3151 0.7205 0.7963 -0.0778 0.1930  -0.1122 124 LYS A O   
986  C CB  . LYS A 124 ? 0.3639 0.7567 0.8460 -0.1282 0.2312  -0.1269 124 LYS A CB  
987  C CG  . LYS A 124 ? 0.4706 0.8330 0.9304 -0.1492 0.2660  -0.1350 124 LYS A CG  
988  C CD  . LYS A 124 ? 0.5855 0.9810 1.0973 -0.1618 0.2634  -0.1426 124 LYS A CD  
989  C CE  . LYS A 124 ? 0.6844 1.0474 1.1749 -0.1823 0.3003  -0.1520 124 LYS A CE  
990  N NZ  . LYS A 124 ? 0.7578 1.0649 1.1702 -0.1967 0.3122  -0.1469 124 LYS A NZ  
991  N N   . ALA A 125 ? 0.3141 0.7075 0.7511 -0.1005 0.1723  -0.1071 125 ALA A N   
992  C CA  . ALA A 125 ? 0.2614 0.6686 0.7018 -0.0816 0.1352  -0.0975 125 ALA A CA  
993  C C   . ALA A 125 ? 0.3262 0.6977 0.7186 -0.0642 0.1341  -0.0893 125 ALA A C   
994  O O   . ALA A 125 ? 0.2914 0.6778 0.7032 -0.0455 0.1174  -0.0853 125 ALA A O   
995  C CB  . ALA A 125 ? 0.3141 0.7161 0.7293 -0.0903 0.1092  -0.0916 125 ALA A CB  
996  N N   . PHE A 126 ? 0.3679 0.6906 0.6965 -0.0706 0.1505  -0.0863 126 PHE A N   
997  C CA  . PHE A 126 ? 0.3166 0.6047 0.5983 -0.0568 0.1488  -0.0797 126 PHE A CA  
998  C C   . PHE A 126 ? 0.3765 0.6726 0.6845 -0.0470 0.1689  -0.0868 126 PHE A C   
999  O O   . PHE A 126 ? 0.3638 0.6600 0.6725 -0.0295 0.1568  -0.0831 126 PHE A O   
1000 C CB  . PHE A 126 ? 0.3659 0.6009 0.5766 -0.0673 0.1606  -0.0752 126 PHE A CB  
1001 C CG  . PHE A 126 ? 0.4733 0.6723 0.6337 -0.0557 0.1554  -0.0685 126 PHE A CG  
1002 C CD1 . PHE A 126 ? 0.4186 0.6077 0.5549 -0.0458 0.1271  -0.0588 126 PHE A CD1 
1003 C CD2 . PHE A 126 ? 0.4846 0.6584 0.6213 -0.0566 0.1800  -0.0733 126 PHE A CD2 
1004 C CE1 . PHE A 126 ? 0.4466 0.6055 0.5413 -0.0366 0.1211  -0.0537 126 PHE A CE1 
1005 C CE2 . PHE A 126 ? 0.5220 0.6623 0.6107 -0.0480 0.1730  -0.0680 126 PHE A CE2 
1006 C CZ  . PHE A 126 ? 0.4170 0.5518 0.4871 -0.0380 0.1425  -0.0582 126 PHE A CZ  
1007 N N   . ASN A 127 ? 0.3801 0.6813 0.7110 -0.0588 0.2022  -0.0981 127 ASN A N   
1008 C CA  . ASN A 127 ? 0.4028 0.7064 0.7571 -0.0512 0.2280  -0.1072 127 ASN A CA  
1009 C C   . ASN A 127 ? 0.3502 0.7053 0.7841 -0.0336 0.2146  -0.1100 127 ASN A C   
1010 O O   . ASN A 127 ? 0.3255 0.6755 0.7720 -0.0211 0.2261  -0.1130 127 ASN A O   
1011 C CB  . ASN A 127 ? 0.4272 0.7175 0.7816 -0.0697 0.2680  -0.1185 127 ASN A CB  
1012 C CG  . ASN A 127 ? 0.5286 0.7590 0.7976 -0.0854 0.2880  -0.1162 127 ASN A CG  
1013 O OD1 . ASN A 127 ? 0.5910 0.7839 0.7992 -0.0778 0.2743  -0.1071 127 ASN A OD1 
1014 N ND2 . ASN A 127 ? 0.6165 0.8288 0.8714 -0.1053 0.3103  -0.1208 127 ASN A ND2 
1015 N N   . ALA A 128 ? 0.3198 0.7125 0.7932 -0.0317 0.1843  -0.1052 128 ALA A N   
1016 C CA  . ALA A 128 ? 0.2951 0.7239 0.8251 -0.0138 0.1603  -0.1010 128 ALA A CA  
1017 C C   . ALA A 128 ? 0.2935 0.7234 0.8146 0.0046  0.1307  -0.0915 128 ALA A C   
1018 O O   . ALA A 128 ? 0.3382 0.7896 0.8959 0.0210  0.1096  -0.0853 128 ALA A O   
1019 C CB  . ALA A 128 ? 0.2636 0.7284 0.8352 -0.0229 0.1412  -0.1000 128 ALA A CB  
1020 N N   . ARG A 129 ? 0.2685 0.6597 0.7209 0.0028  0.1236  -0.0845 129 ARG A N   
1021 C CA  . ARG A 129 ? 0.2472 0.6283 0.6753 0.0175  0.0932  -0.0729 129 ARG A CA  
1022 C C   . ARG A 129 ? 0.3173 0.6565 0.6944 0.0259  0.1027  -0.0706 129 ARG A C   
1023 O O   . ARG A 129 ? 0.2993 0.6382 0.6859 0.0429  0.0932  -0.0670 129 ARG A O   
1024 C CB  . ARG A 129 ? 0.3185 0.6925 0.7120 0.0074  0.0688  -0.0652 129 ARG A CB  
1025 C CG  . ARG A 129 ? 0.2031 0.6172 0.6415 0.0006  0.0492  -0.0657 129 ARG A CG  
1026 C CD  . ARG A 129 ? 0.2093 0.6083 0.6077 -0.0156 0.0383  -0.0627 129 ARG A CD  
1027 N NE  . ARG A 129 ? 0.2156 0.6474 0.6461 -0.0223 0.0140  -0.0624 129 ARG A NE  
1028 C CZ  . ARG A 129 ? 0.2851 0.7491 0.7607 -0.0358 0.0189  -0.0709 129 ARG A CZ  
1029 N NH1 . ARG A 129 ? 0.2097 0.6775 0.7055 -0.0444 0.0505  -0.0806 129 ARG A NH1 
1030 N NH2 . ARG A 129 ? 0.1941 0.6852 0.6928 -0.0425 -0.0079 -0.0700 129 ARG A NH2 
1031 N N   . PHE A 130 ? 0.3205 0.6223 0.6424 0.0140  0.1199  -0.0723 130 PHE A N   
1032 C CA  . PHE A 130 ? 0.3326 0.5934 0.5975 0.0191  0.1193  -0.0684 130 PHE A CA  
1033 C C   . PHE A 130 ? 0.3889 0.6311 0.6488 0.0248  0.1452  -0.0763 130 PHE A C   
1034 O O   . PHE A 130 ? 0.4113 0.6311 0.6434 0.0341  0.1383  -0.0734 130 PHE A O   
1035 C CB  . PHE A 130 ? 0.3780 0.6047 0.5828 0.0048  0.1195  -0.0646 130 PHE A CB  
1036 C CG  . PHE A 130 ? 0.3881 0.6177 0.5805 0.0043  0.0910  -0.0554 130 PHE A CG  
1037 C CD1 . PHE A 130 ? 0.3257 0.5380 0.4893 0.0130  0.0722  -0.0486 130 PHE A CD1 
1038 C CD2 . PHE A 130 ? 0.3443 0.5937 0.5557 -0.0059 0.0848  -0.0552 130 PHE A CD2 
1039 C CE1 . PHE A 130 ? 0.3563 0.5702 0.5106 0.0118  0.0501  -0.0419 130 PHE A CE1 
1040 C CE2 . PHE A 130 ? 0.3047 0.5534 0.5027 -0.0073 0.0619  -0.0484 130 PHE A CE2 
1041 C CZ  . PHE A 130 ? 0.2831 0.5138 0.4531 0.0019  0.0456  -0.0419 130 PHE A CZ  
1042 N N   . PRO A 131 ? 0.4329 0.6802 0.7163 0.0178  0.1776  -0.0877 131 PRO A N   
1043 C CA  . PRO A 131 ? 0.4157 0.6422 0.6935 0.0230  0.2050  -0.0969 131 PRO A CA  
1044 C C   . PRO A 131 ? 0.3768 0.6155 0.6873 0.0446  0.1930  -0.0950 131 PRO A C   
1045 O O   . PRO A 131 ? 0.3353 0.6148 0.7135 0.0567  0.1840  -0.0945 131 PRO A O   
1046 C CB  . PRO A 131 ? 0.3660 0.6116 0.6890 0.0140  0.2396  -0.1100 131 PRO A CB  
1047 C CG  . PRO A 131 ? 0.4295 0.6775 0.7373 -0.0042 0.2370  -0.1074 131 PRO A CG  
1048 C CD  . PRO A 131 ? 0.3634 0.6265 0.6685 0.0014  0.1951  -0.0939 131 PRO A CD  
1049 N N   . GLY A 132 ? 0.4120 0.6140 0.6736 0.0492  0.1908  -0.0933 132 GLY A N   
1050 C CA  . GLY A 132 ? 0.3868 0.5905 0.6695 0.0683  0.1824  -0.0917 132 GLY A CA  
1051 C C   . GLY A 132 ? 0.3535 0.5777 0.6528 0.0799  0.1445  -0.0784 132 GLY A C   
1052 O O   . GLY A 132 ? 0.4061 0.6358 0.7326 0.0969  0.1366  -0.0757 132 GLY A O   
1053 N N   . CYS A 133 ? 0.3501 0.5810 0.6303 0.0709  0.1222  -0.0702 133 CYS A N   
1054 C CA  . CYS A 133 ? 0.3168 0.5664 0.6118 0.0792  0.0890  -0.0588 133 CYS A CA  
1055 C C   . CYS A 133 ? 0.2947 0.5169 0.5525 0.0865  0.0742  -0.0525 133 CYS A C   
1056 O O   . CYS A 133 ? 0.3474 0.5796 0.6165 0.0949  0.0506  -0.0437 133 CYS A O   
1057 C CB  . CYS A 133 ? 0.3040 0.5649 0.5874 0.0655  0.0740  -0.0540 133 CYS A CB  
1058 S SG  . CYS A 133 ? 0.3136 0.5350 0.5234 0.0515  0.0717  -0.0513 133 CYS A SG  
1059 N N   . MET A 134 ? 0.3402 0.5267 0.5521 0.0820  0.0871  -0.0571 134 MET A N   
1060 C CA  . MET A 134 ? 0.3527 0.5136 0.5307 0.0862  0.0744  -0.0530 134 MET A CA  
1061 C C   . MET A 134 ? 0.3891 0.5304 0.5693 0.0966  0.0899  -0.0590 134 MET A C   
1062 O O   . MET A 134 ? 0.4297 0.5429 0.5745 0.0960  0.0861  -0.0591 134 MET A O   
1063 C CB  . MET A 134 ? 0.3851 0.5197 0.5081 0.0722  0.0708  -0.0530 134 MET A CB  
1064 C CG  . MET A 134 ? 0.3073 0.4541 0.4239 0.0641  0.0525  -0.0459 134 MET A CG  
1065 S SD  . MET A 134 ? 0.3767 0.4918 0.4366 0.0523  0.0450  -0.0448 134 MET A SD  
1066 C CE  . MET A 134 ? 0.3534 0.4859 0.4196 0.0456  0.0285  -0.0375 134 MET A CE  
1067 N N   . LYS A 135 ? 0.3914 0.5469 0.6151 0.1055  0.1085  -0.0651 135 LYS A N   
1068 C CA  . LYS A 135 ? 0.4266 0.5606 0.6545 0.1157  0.1275  -0.0723 135 LYS A CA  
1069 C C   . LYS A 135 ? 0.4409 0.5641 0.6671 0.1285  0.1083  -0.0639 135 LYS A C   
1070 O O   . LYS A 135 ? 0.4002 0.5452 0.6530 0.1373  0.0849  -0.0528 135 LYS A O   
1071 C CB  . LYS A 135 ? 0.4823 0.6400 0.7719 0.1261  0.1491  -0.0795 135 LYS A CB  
1072 C CG  . LYS A 135 ? 0.5734 0.7277 0.8566 0.1117  0.1804  -0.0923 135 LYS A CG  
1073 C CD  . LYS A 135 ? 0.5883 0.7730 0.9442 0.1213  0.2028  -0.1004 135 LYS A CD  
1074 C CE  . LYS A 135 ? 0.5859 0.7661 0.9326 0.1037  0.2362  -0.1134 135 LYS A CE  
1075 N NZ  . LYS A 135 ? 0.6651 0.8731 1.0711 0.1072  0.2475  -0.1170 135 LYS A NZ  
1076 N N   . GLY A 136 ? 0.5045 0.5905 0.6941 0.1274  0.1182  -0.0695 136 GLY A N   
1077 C CA  . GLY A 136 ? 0.4195 0.4877 0.6004 0.1366  0.1045  -0.0631 136 GLY A CA  
1078 C C   . GLY A 136 ? 0.4096 0.4728 0.5562 0.1275  0.0791  -0.0545 136 GLY A C   
1079 O O   . GLY A 136 ? 0.4931 0.5383 0.6283 0.1324  0.0698  -0.0499 136 GLY A O   
1080 N N   . ARG A 137 ? 0.3664 0.4428 0.4973 0.1143  0.0699  -0.0528 137 ARG A N   
1081 C CA  . ARG A 137 ? 0.3815 0.4569 0.4886 0.1065  0.0478  -0.0455 137 ARG A CA  
1082 C C   . ARG A 137 ? 0.4011 0.4559 0.4640 0.0911  0.0493  -0.0515 137 ARG A C   
1083 O O   . ARG A 137 ? 0.4107 0.4520 0.4551 0.0844  0.0651  -0.0601 137 ARG A O   
1084 C CB  . ARG A 137 ? 0.3720 0.4791 0.5001 0.1048  0.0325  -0.0375 137 ARG A CB  
1085 C CG  . ARG A 137 ? 0.4256 0.5546 0.5959 0.1188  0.0234  -0.0299 137 ARG A CG  
1086 C CD  . ARG A 137 ? 0.3894 0.5433 0.5688 0.1136  0.0041  -0.0222 137 ARG A CD  
1087 N NE  . ARG A 137 ? 0.4524 0.6272 0.6698 0.1258  -0.0091 -0.0143 137 ARG A NE  
1088 C CZ  . ARG A 137 ? 0.3898 0.5551 0.6016 0.1329  -0.0266 -0.0044 137 ARG A CZ  
1089 N NH1 . ARG A 137 ? 0.4355 0.5717 0.6083 0.1283  -0.0296 -0.0023 137 ARG A NH1 
1090 N NH2 . ARG A 137 ? 0.4491 0.6334 0.6951 0.1441  -0.0420 0.0038  137 ARG A NH2 
1091 N N   . THR A 138 ? 0.3900 0.4417 0.4363 0.0850  0.0320  -0.0469 138 THR A N   
1092 C CA  . THR A 138 ? 0.4025 0.4408 0.4154 0.0716  0.0265  -0.0506 138 THR A CA  
1093 C C   . THR A 138 ? 0.3976 0.4544 0.4124 0.0651  0.0178  -0.0461 138 THR A C   
1094 O O   . THR A 138 ? 0.4065 0.4838 0.4425 0.0680  0.0087  -0.0394 138 THR A O   
1095 C CB  . THR A 138 ? 0.4066 0.4330 0.4085 0.0686  0.0146  -0.0496 138 THR A CB  
1096 O OG1 . THR A 138 ? 0.4583 0.4639 0.4570 0.0740  0.0239  -0.0537 138 THR A OG1 
1097 C CG2 . THR A 138 ? 0.3875 0.4038 0.3632 0.0556  0.0060  -0.0537 138 THR A CG2 
1098 N N   A MET A 139 ? 0.3886 0.4342 0.3776 0.0555  0.0207  -0.0499 139 MET A N   
1099 N N   B MET A 139 ? 0.3869 0.4325 0.3757 0.0554  0.0202  -0.0498 139 MET A N   
1100 C CA  A MET A 139 ? 0.3695 0.4244 0.3536 0.0485  0.0116  -0.0454 139 MET A CA  
1101 C CA  B MET A 139 ? 0.3687 0.4246 0.3540 0.0487  0.0116  -0.0451 139 MET A CA  
1102 C C   A MET A 139 ? 0.3854 0.4318 0.3541 0.0428  -0.0056 -0.0441 139 MET A C   
1103 C C   B MET A 139 ? 0.3856 0.4323 0.3540 0.0425  -0.0055 -0.0439 139 MET A C   
1104 O O   A MET A 139 ? 0.3931 0.4186 0.3349 0.0370  -0.0083 -0.0486 139 MET A O   
1105 O O   B MET A 139 ? 0.3941 0.4199 0.3342 0.0363  -0.0081 -0.0480 139 MET A O   
1106 C CB  A MET A 139 ? 0.3858 0.4295 0.3483 0.0414  0.0241  -0.0485 139 MET A CB  
1107 C CB  B MET A 139 ? 0.3833 0.4302 0.3503 0.0422  0.0250  -0.0482 139 MET A CB  
1108 C CG  A MET A 139 ? 0.4039 0.4471 0.3521 0.0335  0.0132  -0.0431 139 MET A CG  
1109 C CG  B MET A 139 ? 0.3888 0.4454 0.3558 0.0364  0.0186  -0.0425 139 MET A CG  
1110 S SD  A MET A 139 ? 0.3854 0.4016 0.2911 0.0222  0.0258  -0.0454 139 MET A SD  
1111 S SD  B MET A 139 ? 0.4851 0.5272 0.4283 0.0270  0.0380  -0.0454 139 MET A SD  
1112 C CE  A MET A 139 ? 0.4444 0.4802 0.3808 0.0241  0.0510  -0.0487 139 MET A CE  
1113 C CE  B MET A 139 ? 0.4207 0.4218 0.3056 0.0179  0.0322  -0.0477 139 MET A CE  
1114 N N   . TYR A 140 ? 0.3831 0.4451 0.3698 0.0436  -0.0170 -0.0388 140 TYR A N   
1115 C CA  . TYR A 140 ? 0.3582 0.4167 0.3409 0.0387  -0.0315 -0.0383 140 TYR A CA  
1116 C C   . TYR A 140 ? 0.3942 0.4523 0.3682 0.0340  -0.0383 -0.0347 140 TYR A C   
1117 O O   . TYR A 140 ? 0.3236 0.3915 0.3046 0.0342  -0.0333 -0.0311 140 TYR A O   
1118 C CB  . TYR A 140 ? 0.3669 0.4379 0.3720 0.0410  -0.0362 -0.0360 140 TYR A CB  
1119 C CG  . TYR A 140 ? 0.3259 0.3910 0.3348 0.0453  -0.0311 -0.0379 140 TYR A CG  
1120 C CD1 . TYR A 140 ? 0.3763 0.4283 0.3792 0.0418  -0.0337 -0.0428 140 TYR A CD1 
1121 C CD2 . TYR A 140 ? 0.3392 0.4108 0.3588 0.0528  -0.0246 -0.0344 140 TYR A CD2 
1122 C CE1 . TYR A 140 ? 0.4193 0.4609 0.4225 0.0451  -0.0276 -0.0441 140 TYR A CE1 
1123 C CE2 . TYR A 140 ? 0.3715 0.4332 0.3927 0.0582  -0.0211 -0.0343 140 TYR A CE2 
1124 C CZ  . TYR A 140 ? 0.3824 0.4270 0.3930 0.0540  -0.0213 -0.0391 140 TYR A CZ  
1125 O OH  . TYR A 140 ? 0.4905 0.5202 0.4995 0.0587  -0.0164 -0.0386 140 TYR A OH  
1126 N N   . VAL A 141 ? 0.3127 0.3585 0.2721 0.0295  -0.0509 -0.0354 141 VAL A N   
1127 C CA  . VAL A 141 ? 0.3387 0.3787 0.2874 0.0263  -0.0609 -0.0304 141 VAL A CA  
1128 C C   . VAL A 141 ? 0.3508 0.4017 0.3252 0.0275  -0.0750 -0.0289 141 VAL A C   
1129 O O   . VAL A 141 ? 0.3499 0.3983 0.3285 0.0258  -0.0867 -0.0323 141 VAL A O   
1130 C CB  . VAL A 141 ? 0.4231 0.4372 0.3323 0.0203  -0.0670 -0.0312 141 VAL A CB  
1131 C CG1 . VAL A 141 ? 0.3748 0.3781 0.2688 0.0180  -0.0780 -0.0234 141 VAL A CG1 
1132 C CG2 . VAL A 141 ? 0.4228 0.4242 0.3085 0.0182  -0.0474 -0.0356 141 VAL A CG2 
1133 N N   . ILE A 142 ? 0.3462 0.4090 0.3397 0.0294  -0.0725 -0.0252 142 ILE A N   
1134 C CA  . ILE A 142 ? 0.2835 0.3568 0.3058 0.0306  -0.0796 -0.0255 142 ILE A CA  
1135 C C   . ILE A 142 ? 0.2963 0.3625 0.3189 0.0314  -0.0914 -0.0201 142 ILE A C   
1136 O O   . ILE A 142 ? 0.3041 0.3680 0.3228 0.0314  -0.0857 -0.0156 142 ILE A O   
1137 C CB  . ILE A 142 ? 0.2330 0.3198 0.2734 0.0311  -0.0678 -0.0261 142 ILE A CB  
1138 C CG1 . ILE A 142 ? 0.2335 0.3241 0.2700 0.0319  -0.0584 -0.0285 142 ILE A CG1 
1139 C CG2 . ILE A 142 ? 0.2371 0.3309 0.3050 0.0306  -0.0699 -0.0290 142 ILE A CG2 
1140 C CD1 . ILE A 142 ? 0.2668 0.3679 0.3133 0.0315  -0.0506 -0.0273 142 ILE A CD1 
1141 N N   . PRO A 143 ? 0.3253 0.3872 0.3537 0.0322  -0.1088 -0.0200 143 PRO A N   
1142 C CA  . PRO A 143 ? 0.2801 0.3361 0.3171 0.0356  -0.1223 -0.0136 143 PRO A CA  
1143 C C   . PRO A 143 ? 0.3010 0.3733 0.3831 0.0391  -0.1191 -0.0168 143 PRO A C   
1144 O O   . PRO A 143 ? 0.3347 0.4198 0.4447 0.0387  -0.1212 -0.0237 143 PRO A O   
1145 C CB  . PRO A 143 ? 0.3768 0.4226 0.4026 0.0350  -0.1456 -0.0123 143 PRO A CB  
1146 C CG  . PRO A 143 ? 0.3941 0.4443 0.4141 0.0299  -0.1416 -0.0211 143 PRO A CG  
1147 C CD  . PRO A 143 ? 0.3220 0.3848 0.3535 0.0299  -0.1183 -0.0259 143 PRO A CD  
1148 N N   . PHE A 144 ? 0.3185 0.3888 0.4082 0.0411  -0.1114 -0.0133 144 PHE A N   
1149 C CA  . PHE A 144 ? 0.2952 0.3775 0.4242 0.0426  -0.1028 -0.0186 144 PHE A CA  
1150 C C   . PHE A 144 ? 0.2643 0.3374 0.4077 0.0483  -0.1078 -0.0130 144 PHE A C   
1151 O O   . PHE A 144 ? 0.3082 0.3639 0.4245 0.0492  -0.1123 -0.0044 144 PHE A O   
1152 C CB  . PHE A 144 ? 0.2996 0.3884 0.4241 0.0370  -0.0816 -0.0234 144 PHE A CB  
1153 C CG  . PHE A 144 ? 0.2910 0.3717 0.3922 0.0344  -0.0733 -0.0186 144 PHE A CG  
1154 C CD1 . PHE A 144 ? 0.2929 0.3706 0.3641 0.0317  -0.0712 -0.0157 144 PHE A CD1 
1155 C CD2 . PHE A 144 ? 0.2823 0.3580 0.3942 0.0337  -0.0658 -0.0184 144 PHE A CD2 
1156 C CE1 . PHE A 144 ? 0.3387 0.4118 0.3942 0.0277  -0.0624 -0.0127 144 PHE A CE1 
1157 C CE2 . PHE A 144 ? 0.3219 0.3902 0.4134 0.0291  -0.0577 -0.0152 144 PHE A CE2 
1158 C CZ  . PHE A 144 ? 0.3321 0.4007 0.3971 0.0257  -0.0563 -0.0124 144 PHE A CZ  
1159 N N   . SER A 145 ? 0.2373 0.3198 0.4243 0.0517  -0.1046 -0.0185 145 SER A N   
1160 C CA  . SER A 145 ? 0.2928 0.3665 0.5024 0.0585  -0.1060 -0.0149 145 SER A CA  
1161 C C   . SER A 145 ? 0.3250 0.4003 0.5490 0.0539  -0.0807 -0.0230 145 SER A C   
1162 O O   . SER A 145 ? 0.3046 0.3920 0.5424 0.0482  -0.0666 -0.0330 145 SER A O   
1163 C CB  . SER A 145 ? 0.2577 0.3402 0.5139 0.0678  -0.1244 -0.0153 145 SER A CB  
1164 O OG  . SER A 145 ? 0.4609 0.5341 0.7448 0.0767  -0.1251 -0.0117 145 SER A OG  
1165 N N   . MET A 146 ? 0.3016 0.3606 0.5170 0.0549  -0.0741 -0.0187 146 MET A N   
1166 C CA  . MET A 146 ? 0.3375 0.3927 0.5678 0.0504  -0.0514 -0.0269 146 MET A CA  
1167 C C   . MET A 146 ? 0.3739 0.4241 0.6504 0.0614  -0.0539 -0.0275 146 MET A C   
1168 O O   . MET A 146 ? 0.4160 0.4500 0.6909 0.0700  -0.0666 -0.0172 146 MET A O   
1169 C CB  . MET A 146 ? 0.3158 0.3557 0.5094 0.0426  -0.0408 -0.0237 146 MET A CB  
1170 C CG  . MET A 146 ? 0.3587 0.4062 0.5147 0.0336  -0.0397 -0.0227 146 MET A CG  
1171 S SD  . MET A 146 ? 0.3650 0.4312 0.5244 0.0261  -0.0298 -0.0331 146 MET A SD  
1172 C CE  . MET A 146 ? 0.3428 0.4001 0.5081 0.0164  -0.0068 -0.0433 146 MET A CE  
1173 N N   . GLY A 147 ? 0.3894 0.4518 0.7077 0.0612  -0.0410 -0.0393 147 GLY A N   
1174 C CA  . GLY A 147 ? 0.3911 0.4545 0.7659 0.0730  -0.0427 -0.0418 147 GLY A CA  
1175 C C   . GLY A 147 ? 0.4647 0.5499 0.8780 0.0809  -0.0643 -0.0415 147 GLY A C   
1176 O O   . GLY A 147 ? 0.3631 0.4569 0.7510 0.0777  -0.0805 -0.0373 147 GLY A O   
1177 N N   . PRO A 148 ? 0.4568 0.5516 0.9351 0.0909  -0.0642 -0.0470 148 PRO A N   
1178 C CA  . PRO A 148 ? 0.5115 0.6283 1.0266 0.0944  -0.0835 -0.0484 148 PRO A CA  
1179 C C   . PRO A 148 ? 0.5818 0.6948 1.0661 0.0997  -0.1204 -0.0328 148 PRO A C   
1180 O O   . PRO A 148 ? 0.6387 0.7319 1.1032 0.1086  -0.1367 -0.0191 148 PRO A O   
1181 C CB  . PRO A 148 ? 0.4913 0.6072 1.0579 0.1005  -0.0757 -0.0527 148 PRO A CB  
1182 C CG  . PRO A 148 ? 0.5193 0.6214 1.0913 0.0974  -0.0413 -0.0622 148 PRO A CG  
1183 C CD  . PRO A 148 ? 0.5439 0.6279 1.0604 0.0959  -0.0422 -0.0540 148 PRO A CD  
1184 N N   . LEU A 149 ? 0.5818 0.7096 1.0577 0.0927  -0.1318 -0.0353 149 LEU A N   
1185 C CA  . LEU A 149 ? 0.6612 0.7825 1.1004 0.0940  -0.1635 -0.0231 149 LEU A CA  
1186 C C   . LEU A 149 ? 0.8453 0.9603 1.3043 0.1038  -0.1868 -0.0138 149 LEU A C   
1187 O O   . LEU A 149 ? 0.7697 0.8975 1.2811 0.1068  -0.1828 -0.0206 149 LEU A O   
1188 C CB  . LEU A 149 ? 0.7375 0.8745 1.1688 0.0835  -0.1671 -0.0304 149 LEU A CB  
1189 C CG  . LEU A 149 ? 0.6276 0.7563 1.0173 0.0818  -0.1963 -0.0208 149 LEU A CG  
1190 C CD1 . LEU A 149 ? 0.7354 0.8426 1.0655 0.0819  -0.2019 -0.0102 149 LEU A CD1 
1191 C CD2 . LEU A 149 ? 0.6466 0.7905 1.0369 0.0711  -0.1959 -0.0306 149 LEU A CD2 
1192 N N   . GLY A 150 ? 0.9049 0.9982 1.3203 0.1083  -0.2110 0.0017  150 GLY A N   
1193 C CA  . GLY A 150 ? 0.9056 0.9880 1.3309 0.1180  -0.2354 0.0129  150 GLY A CA  
1194 C C   . GLY A 150 ? 1.0146 1.0831 1.4658 0.1299  -0.2275 0.0178  150 GLY A C   
1195 O O   . GLY A 150 ? 1.0843 1.1366 1.5332 0.1393  -0.2491 0.0304  150 GLY A O   
1196 N N   . SER A 151 ? 0.8424 0.9142 1.3163 0.1293  -0.1967 0.0080  151 SER A N   
1197 C CA  . SER A 151 ? 0.8301 0.8847 1.3263 0.1396  -0.1854 0.0113  151 SER A CA  
1198 C C   . SER A 151 ? 0.9114 0.9297 1.3534 0.1449  -0.1982 0.0288  151 SER A C   
1199 O O   . SER A 151 ? 0.8872 0.8959 1.2781 0.1379  -0.2011 0.0330  151 SER A O   
1200 C CB  . SER A 151 ? 0.7472 0.8085 1.2695 0.1345  -0.1466 -0.0046 151 SER A CB  
1201 O OG  . SER A 151 ? 0.7921 0.8320 1.3304 0.1430  -0.1325 -0.0026 151 SER A OG  
1202 N N   . PRO A 152 ? 0.9252 0.9205 1.3754 0.1568  -0.2057 0.0395  152 PRO A N   
1203 C CA  . PRO A 152 ? 0.9734 0.9271 1.3665 0.1603  -0.2163 0.0571  152 PRO A CA  
1204 C C   . PRO A 152 ? 0.9056 0.8408 1.2759 0.1552  -0.1903 0.0539  152 PRO A C   
1205 O O   . PRO A 152 ? 1.0006 0.9086 1.3043 0.1474  -0.1931 0.0640  152 PRO A O   
1206 C CB  . PRO A 152 ? 0.9527 0.8877 1.3704 0.1749  -0.2254 0.0669  152 PRO A CB  
1207 C CG  . PRO A 152 ? 0.9689 0.9393 1.4483 0.1787  -0.2331 0.0578  152 PRO A CG  
1208 C CD  . PRO A 152 ? 0.9227 0.9267 1.4311 0.1673  -0.2081 0.0375  152 PRO A CD  
1209 N N   . LEU A 153 ? 0.8189 0.7676 1.2303 0.1529  -0.1582 0.0375  153 LEU A N   
1210 C CA  . LEU A 153 ? 0.8502 0.7846 1.2197 0.1370  -0.1239 0.0301  153 LEU A CA  
1211 C C   . LEU A 153 ? 0.8263 0.7812 1.1563 0.1186  -0.1133 0.0215  153 LEU A C   
1212 O O   . LEU A 153 ? 0.7064 0.6511 0.9958 0.1045  -0.0913 0.0175  153 LEU A O   
1213 C CB  . LEU A 153 ? 0.7487 0.6847 1.1662 0.1381  -0.0917 0.0148  153 LEU A CB  
1214 C CG  . LEU A 153 ? 0.7603 0.7314 1.2465 0.1413  -0.0821 -0.0016 153 LEU A CG  
1215 C CD1 . LEU A 153 ? 0.7467 0.7408 1.2118 0.1220  -0.0614 -0.0166 153 LEU A CD1 
1216 C CD2 . LEU A 153 ? 0.6847 0.6454 1.2174 0.1470  -0.0569 -0.0110 153 LEU A CD2 
1217 N N   . ALA A 154 ? 0.7138 0.6969 1.0569 0.1183  -0.1287 0.0184  154 ALA A N   
1218 C CA  . ALA A 154 ? 0.6513 0.6513 0.9593 0.1028  -0.1194 0.0111  154 ALA A CA  
1219 C C   . ALA A 154 ? 0.6502 0.6296 0.8892 0.0952  -0.1267 0.0224  154 ALA A C   
1220 O O   . ALA A 154 ? 0.6609 0.6168 0.8762 0.1017  -0.1484 0.0370  154 ALA A O   
1221 C CB  . ALA A 154 ? 0.5552 0.5850 0.8918 0.1043  -0.1349 0.0057  154 ALA A CB  
1222 N N   . LYS A 155 ? 0.4901 0.4769 0.6968 0.0809  -0.1077 0.0153  155 LYS A N   
1223 C CA  . LYS A 155 ? 0.4701 0.4434 0.6186 0.0719  -0.1091 0.0224  155 LYS A CA  
1224 C C   . LYS A 155 ? 0.4125 0.4083 0.5486 0.0654  -0.1116 0.0167  155 LYS A C   
1225 O O   . LYS A 155 ? 0.4144 0.4336 0.5743 0.0619  -0.1002 0.0053  155 LYS A O   
1226 C CB  . LYS A 155 ? 0.4931 0.4549 0.6181 0.0609  -0.0844 0.0193  155 LYS A CB  
1227 C CG  . LYS A 155 ? 0.5924 0.5239 0.7183 0.0652  -0.0800 0.0258  155 LYS A CG  
1228 C CD  . LYS A 155 ? 0.6526 0.5518 0.7390 0.0687  -0.0974 0.0422  155 LYS A CD  
1229 C CE  . LYS A 155 ? 0.7699 0.6334 0.8526 0.0724  -0.0914 0.0497  155 LYS A CE  
1230 N NZ  . LYS A 155 ? 0.7824 0.6451 0.9188 0.0887  -0.0987 0.0498  155 LYS A NZ  
1231 N N   . ILE A 156 ? 0.4066 0.3909 0.5020 0.0632  -0.1252 0.0246  156 ILE A N   
1232 C CA  . ILE A 156 ? 0.4083 0.4082 0.4903 0.0583  -0.1296 0.0200  156 ILE A CA  
1233 C C   . ILE A 156 ? 0.4601 0.4537 0.4984 0.0477  -0.1143 0.0198  156 ILE A C   
1234 O O   . ILE A 156 ? 0.4865 0.4560 0.4919 0.0442  -0.1109 0.0273  156 ILE A O   
1235 C CB  . ILE A 156 ? 0.4234 0.4152 0.4969 0.0637  -0.1589 0.0271  156 ILE A CB  
1236 C CG1 . ILE A 156 ? 0.4144 0.4246 0.5457 0.0736  -0.1735 0.0237  156 ILE A CG1 
1237 C CG2 . ILE A 156 ? 0.3612 0.3577 0.4036 0.0560  -0.1606 0.0233  156 ILE A CG2 
1238 C CD1 . ILE A 156 ? 0.4585 0.4617 0.5880 0.0794  -0.2077 0.0315  156 ILE A CD1 
1239 N N   . GLY A 157 ? 0.4049 0.4194 0.4453 0.0425  -0.1041 0.0110  157 GLY A N   
1240 C CA  . GLY A 157 ? 0.4294 0.4430 0.4385 0.0342  -0.0905 0.0097  157 GLY A CA  
1241 C C   . GLY A 157 ? 0.3447 0.3679 0.3445 0.0330  -0.0937 0.0053  157 GLY A C   
1242 O O   . GLY A 157 ? 0.2966 0.3311 0.3169 0.0366  -0.1036 0.0013  157 GLY A O   
1243 N N   . ILE A 158 ? 0.3961 0.4133 0.3660 0.0271  -0.0833 0.0050  158 ILE A N   
1244 C CA  . ILE A 158 ? 0.3893 0.4138 0.3498 0.0255  -0.0800 -0.0006 158 ILE A CA  
1245 C C   . ILE A 158 ? 0.3456 0.3874 0.3156 0.0224  -0.0608 -0.0055 158 ILE A C   
1246 O O   . ILE A 158 ? 0.3618 0.3987 0.3198 0.0174  -0.0489 -0.0040 158 ILE A O   
1247 C CB  . ILE A 158 ? 0.3487 0.3476 0.2652 0.0214  -0.0840 0.0026  158 ILE A CB  
1248 C CG1 . ILE A 158 ? 0.4396 0.4187 0.3428 0.0241  -0.1084 0.0097  158 ILE A CG1 
1249 C CG2 . ILE A 158 ? 0.3459 0.3501 0.2547 0.0199  -0.0781 -0.0049 158 ILE A CG2 
1250 C CD1 . ILE A 158 ? 0.4512 0.4418 0.3734 0.0275  -0.1252 0.0052  158 ILE A CD1 
1251 N N   . GLU A 159 ? 0.3181 0.3791 0.3099 0.0249  -0.0585 -0.0111 159 GLU A N   
1252 C CA  . GLU A 159 ? 0.2462 0.3236 0.2474 0.0235  -0.0453 -0.0146 159 GLU A CA  
1253 C C   . GLU A 159 ? 0.2920 0.3695 0.2848 0.0256  -0.0414 -0.0181 159 GLU A C   
1254 O O   . GLU A 159 ? 0.3502 0.4263 0.3452 0.0285  -0.0483 -0.0206 159 GLU A O   
1255 C CB  . GLU A 159 ? 0.2600 0.3538 0.2865 0.0241  -0.0449 -0.0170 159 GLU A CB  
1256 C CG  . GLU A 159 ? 0.2330 0.3426 0.2675 0.0241  -0.0373 -0.0192 159 GLU A CG  
1257 C CD  . GLU A 159 ? 0.2841 0.4050 0.3329 0.0211  -0.0368 -0.0202 159 GLU A CD  
1258 O OE1 . GLU A 159 ? 0.2852 0.4010 0.3380 0.0182  -0.0383 -0.0208 159 GLU A OE1 
1259 O OE2 . GLU A 159 ? 0.2291 0.3624 0.2843 0.0214  -0.0353 -0.0205 159 GLU A OE2 
1260 N N   . LEU A 160 ? 0.3300 0.4086 0.3157 0.0236  -0.0287 -0.0194 160 LEU A N   
1261 C CA  . LEU A 160 ? 0.3275 0.4082 0.3127 0.0268  -0.0204 -0.0238 160 LEU A CA  
1262 C C   . LEU A 160 ? 0.3318 0.4364 0.3469 0.0310  -0.0164 -0.0247 160 LEU A C   
1263 O O   . LEU A 160 ? 0.3288 0.4473 0.3580 0.0280  -0.0123 -0.0237 160 LEU A O   
1264 C CB  . LEU A 160 ? 0.3033 0.3699 0.2663 0.0223  -0.0061 -0.0259 160 LEU A CB  
1265 C CG  . LEU A 160 ? 0.4156 0.4532 0.3399 0.0157  -0.0106 -0.0227 160 LEU A CG  
1266 C CD1 . LEU A 160 ? 0.4211 0.4418 0.3198 0.0087  0.0090  -0.0256 160 LEU A CD1 
1267 C CD2 . LEU A 160 ? 0.3886 0.4108 0.2948 0.0171  -0.0260 -0.0231 160 LEU A CD2 
1268 N N   . THR A 161 ? 0.2988 0.4061 0.3218 0.0370  -0.0190 -0.0263 161 THR A N   
1269 C CA  . THR A 161 ? 0.2830 0.4082 0.3296 0.0420  -0.0192 -0.0252 161 THR A CA  
1270 C C   . THR A 161 ? 0.3014 0.4211 0.3499 0.0498  -0.0153 -0.0274 161 THR A C   
1271 O O   . THR A 161 ? 0.3138 0.4157 0.3448 0.0496  -0.0145 -0.0305 161 THR A O   
1272 C CB  . THR A 161 ? 0.2623 0.3920 0.3146 0.0401  -0.0296 -0.0225 161 THR A CB  
1273 O OG1 . THR A 161 ? 0.2356 0.3784 0.3030 0.0436  -0.0324 -0.0201 161 THR A OG1 
1274 C CG2 . THR A 161 ? 0.2170 0.3327 0.2599 0.0406  -0.0348 -0.0241 161 THR A CG2 
1275 N N   . ASP A 162 ? 0.2192 0.3534 0.2900 0.0565  -0.0139 -0.0256 162 ASP A N   
1276 C CA  . ASP A 162 ? 0.2286 0.3559 0.3049 0.0660  -0.0107 -0.0263 162 ASP A CA  
1277 C C   . ASP A 162 ? 0.2244 0.3502 0.3033 0.0698  -0.0223 -0.0208 162 ASP A C   
1278 O O   . ASP A 162 ? 0.3123 0.4320 0.3979 0.0790  -0.0215 -0.0191 162 ASP A O   
1279 C CB  . ASP A 162 ? 0.3259 0.4670 0.4282 0.0734  0.0000  -0.0280 162 ASP A CB  
1280 C CG  . ASP A 162 ? 0.3041 0.4733 0.4350 0.0733  -0.0070 -0.0240 162 ASP A CG  
1281 O OD1 . ASP A 162 ? 0.2131 0.3874 0.3384 0.0674  -0.0199 -0.0197 162 ASP A OD1 
1282 O OD2 . ASP A 162 ? 0.3318 0.5181 0.4925 0.0782  0.0014  -0.0262 162 ASP A OD2 
1283 N N   . SER A 163 ? 0.2301 0.3571 0.3013 0.0626  -0.0314 -0.0183 163 SER A N   
1284 C CA  . SER A 163 ? 0.2678 0.3891 0.3346 0.0631  -0.0401 -0.0135 163 SER A CA  
1285 C C   . SER A 163 ? 0.2910 0.3941 0.3404 0.0569  -0.0393 -0.0166 163 SER A C   
1286 O O   . SER A 163 ? 0.2905 0.3952 0.3368 0.0493  -0.0395 -0.0198 163 SER A O   
1287 C CB  . SER A 163 ? 0.3007 0.4365 0.3725 0.0575  -0.0485 -0.0098 163 SER A CB  
1288 O OG  . SER A 163 ? 0.3252 0.4484 0.3821 0.0542  -0.0552 -0.0061 163 SER A OG  
1289 N N   . PRO A 164 ? 0.3252 0.4106 0.3660 0.0599  -0.0379 -0.0162 164 PRO A N   
1290 C CA  . PRO A 164 ? 0.3374 0.4081 0.3670 0.0519  -0.0362 -0.0203 164 PRO A CA  
1291 C C   . PRO A 164 ? 0.3186 0.3892 0.3435 0.0440  -0.0387 -0.0185 164 PRO A C   
1292 O O   . PRO A 164 ? 0.2826 0.3491 0.3077 0.0360  -0.0354 -0.0239 164 PRO A O   
1293 C CB  . PRO A 164 ? 0.3576 0.4073 0.3784 0.0565  -0.0321 -0.0199 164 PRO A CB  
1294 C CG  . PRO A 164 ? 0.4270 0.4794 0.4537 0.0678  -0.0353 -0.0122 164 PRO A CG  
1295 C CD  . PRO A 164 ? 0.3398 0.4167 0.3836 0.0707  -0.0366 -0.0125 164 PRO A CD  
1296 N N   . TYR A 165 ? 0.2423 0.3166 0.2637 0.0454  -0.0445 -0.0118 165 TYR A N   
1297 C CA  . TYR A 165 ? 0.2656 0.3365 0.2762 0.0355  -0.0457 -0.0113 165 TYR A CA  
1298 C C   . TYR A 165 ? 0.3123 0.3970 0.3336 0.0290  -0.0433 -0.0167 165 TYR A C   
1299 O O   . TYR A 165 ? 0.3301 0.4079 0.3468 0.0198  -0.0380 -0.0208 165 TYR A O   
1300 C CB  . TYR A 165 ? 0.3099 0.3831 0.3125 0.0375  -0.0566 -0.0028 165 TYR A CB  
1301 C CG  . TYR A 165 ? 0.3029 0.3713 0.2887 0.0251  -0.0583 -0.0031 165 TYR A CG  
1302 C CD1 . TYR A 165 ? 0.3272 0.3687 0.2838 0.0168  -0.0552 -0.0018 165 TYR A CD1 
1303 C CD2 . TYR A 165 ? 0.3043 0.3910 0.2997 0.0200  -0.0608 -0.0056 165 TYR A CD2 
1304 C CE1 . TYR A 165 ? 0.3143 0.3466 0.2499 0.0035  -0.0540 -0.0036 165 TYR A CE1 
1305 C CE2 . TYR A 165 ? 0.3215 0.4004 0.2986 0.0072  -0.0607 -0.0074 165 TYR A CE2 
1306 C CZ  . TYR A 165 ? 0.3854 0.4369 0.3319 -0.0011 -0.0571 -0.0067 165 TYR A CZ  
1307 O OH  . TYR A 165 ? 0.3718 0.4111 0.2949 -0.0156 -0.0544 -0.0100 165 TYR A OH  
1308 N N   . VAL A 166 ? 0.2432 0.3445 0.2782 0.0333  -0.0452 -0.0170 166 VAL A N   
1309 C CA  . VAL A 166 ? 0.2001 0.3096 0.2426 0.0281  -0.0432 -0.0207 166 VAL A CA  
1310 C C   . VAL A 166 ? 0.2644 0.3670 0.3118 0.0268  -0.0399 -0.0260 166 VAL A C   
1311 O O   . VAL A 166 ? 0.2641 0.3660 0.3181 0.0215  -0.0376 -0.0294 166 VAL A O   
1312 C CB  . VAL A 166 ? 0.2438 0.3683 0.2953 0.0316  -0.0446 -0.0191 166 VAL A CB  
1313 C CG1 . VAL A 166 ? 0.2275 0.3531 0.2821 0.0275  -0.0422 -0.0217 166 VAL A CG1 
1314 C CG2 . VAL A 166 ? 0.2928 0.4296 0.3478 0.0303  -0.0495 -0.0154 166 VAL A CG2 
1315 N N   . VAL A 167 ? 0.2439 0.3410 0.2903 0.0314  -0.0402 -0.0272 167 VAL A N   
1316 C CA  . VAL A 167 ? 0.3040 0.3965 0.3568 0.0292  -0.0409 -0.0325 167 VAL A CA  
1317 C C   . VAL A 167 ? 0.2877 0.3741 0.3476 0.0226  -0.0359 -0.0370 167 VAL A C   
1318 O O   . VAL A 167 ? 0.2605 0.3508 0.3367 0.0193  -0.0359 -0.0412 167 VAL A O   
1319 C CB  . VAL A 167 ? 0.2666 0.3511 0.3122 0.0330  -0.0417 -0.0343 167 VAL A CB  
1320 C CG1 . VAL A 167 ? 0.3254 0.4077 0.3772 0.0296  -0.0473 -0.0397 167 VAL A CG1 
1321 C CG2 . VAL A 167 ? 0.2209 0.3087 0.2589 0.0389  -0.0410 -0.0311 167 VAL A CG2 
1322 N N   . ALA A 168 ? 0.2242 0.2993 0.2726 0.0206  -0.0305 -0.0361 168 ALA A N   
1323 C CA  . ALA A 168 ? 0.2692 0.3337 0.3199 0.0119  -0.0212 -0.0414 168 ALA A CA  
1324 C C   . ALA A 168 ? 0.2508 0.3182 0.3063 0.0057  -0.0159 -0.0435 168 ALA A C   
1325 O O   . ALA A 168 ? 0.2911 0.3566 0.3627 -0.0007 -0.0070 -0.0510 168 ALA A O   
1326 C CB  . ALA A 168 ? 0.3281 0.3730 0.3558 0.0103  -0.0164 -0.0379 168 ALA A CB  
1327 N N   . SER A 169 ? 0.2749 0.3468 0.3191 0.0068  -0.0200 -0.0382 169 SER A N   
1328 C CA  . SER A 169 ? 0.2786 0.3499 0.3236 -0.0005 -0.0138 -0.0412 169 SER A CA  
1329 C C   . SER A 169 ? 0.2988 0.3815 0.3700 0.0020  -0.0146 -0.0449 169 SER A C   
1330 O O   . SER A 169 ? 0.2965 0.3760 0.3810 -0.0033 -0.0051 -0.0512 169 SER A O   
1331 C CB  . SER A 169 ? 0.3093 0.3826 0.3352 -0.0018 -0.0199 -0.0352 169 SER A CB  
1332 O OG  . SER A 169 ? 0.3678 0.4286 0.3694 -0.0030 -0.0229 -0.0301 169 SER A OG  
1333 N N   . MET A 170 ? 0.2113 0.3045 0.2889 0.0100  -0.0252 -0.0409 170 MET A N   
1334 C CA  . MET A 170 ? 0.2280 0.3272 0.3251 0.0132  -0.0292 -0.0421 170 MET A CA  
1335 C C   . MET A 170 ? 0.1950 0.2950 0.3178 0.0133  -0.0286 -0.0484 170 MET A C   
1336 O O   . MET A 170 ? 0.2216 0.3247 0.3679 0.0148  -0.0294 -0.0508 170 MET A O   
1337 C CB  . MET A 170 ? 0.1837 0.2877 0.2729 0.0197  -0.0398 -0.0362 170 MET A CB  
1338 C CG  . MET A 170 ? 0.2513 0.3590 0.3264 0.0190  -0.0391 -0.0315 170 MET A CG  
1339 S SD  . MET A 170 ? 0.2673 0.3731 0.3483 0.0149  -0.0355 -0.0316 170 MET A SD  
1340 C CE  . MET A 170 ? 0.2895 0.3907 0.3771 0.0215  -0.0449 -0.0283 170 MET A CE  
1341 N N   . ARG A 171 ? 0.2597 0.3569 0.3817 0.0117  -0.0275 -0.0513 171 ARG A N   
1342 C CA  . ARG A 171 ? 0.2371 0.3378 0.3889 0.0094  -0.0258 -0.0592 171 ARG A CA  
1343 C C   . ARG A 171 ? 0.2920 0.3898 0.4627 0.0026  -0.0092 -0.0668 171 ARG A C   
1344 O O   . ARG A 171 ? 0.2118 0.3179 0.4205 0.0030  -0.0079 -0.0734 171 ARG A O   
1345 C CB  . ARG A 171 ? 0.2421 0.3371 0.3864 0.0063  -0.0247 -0.0620 171 ARG A CB  
1346 C CG  . ARG A 171 ? 0.2762 0.3785 0.4557 0.0027  -0.0255 -0.0711 171 ARG A CG  
1347 C CD  . ARG A 171 ? 0.3442 0.4383 0.5152 -0.0025 -0.0227 -0.0751 171 ARG A CD  
1348 N NE  . ARG A 171 ? 0.4047 0.5103 0.6126 -0.0064 -0.0284 -0.0841 171 ARG A NE  
1349 C CZ  . ARG A 171 ? 0.4244 0.5339 0.6648 -0.0148 -0.0148 -0.0944 171 ARG A CZ  
1350 N NH1 . ARG A 171 ? 0.5173 0.6149 0.7507 -0.0214 0.0075  -0.0972 171 ARG A NH1 
1351 N NH2 . ARG A 171 ? 0.4848 0.6097 0.7653 -0.0179 -0.0236 -0.1027 171 ARG A NH2 
1352 N N   . ILE A 172 ? 0.2097 0.2949 0.3548 -0.0039 0.0034  -0.0663 172 ILE A N   
1353 C CA  . ILE A 172 ? 0.2536 0.3300 0.4080 -0.0128 0.0229  -0.0748 172 ILE A CA  
1354 C C   . ILE A 172 ? 0.2569 0.3363 0.4230 -0.0103 0.0240  -0.0750 172 ILE A C   
1355 O O   . ILE A 172 ? 0.2613 0.3418 0.4600 -0.0116 0.0354  -0.0833 172 ILE A O   
1356 C CB  . ILE A 172 ? 0.3384 0.3935 0.4514 -0.0231 0.0348  -0.0742 172 ILE A CB  
1357 C CG1 . ILE A 172 ? 0.3047 0.3512 0.4072 -0.0258 0.0364  -0.0742 172 ILE A CG1 
1358 C CG2 . ILE A 172 ? 0.3405 0.3805 0.4530 -0.0349 0.0574  -0.0837 172 ILE A CG2 
1359 C CD1 . ILE A 172 ? 0.3870 0.4086 0.4423 -0.0336 0.0425  -0.0696 172 ILE A CD1 
1360 N N   . MET A 173 ? 0.2936 0.3740 0.4366 -0.0067 0.0135  -0.0666 173 MET A N   
1361 C CA  . MET A 173 ? 0.2449 0.3224 0.3904 -0.0073 0.0173  -0.0669 173 MET A CA  
1362 C C   . MET A 173 ? 0.2423 0.3292 0.4176 0.0034  0.0063  -0.0640 173 MET A C   
1363 O O   . MET A 173 ? 0.2446 0.3260 0.4290 0.0037  0.0120  -0.0654 173 MET A O   
1364 C CB  . MET A 173 ? 0.2562 0.3308 0.3655 -0.0105 0.0117  -0.0601 173 MET A CB  
1365 C CG  . MET A 173 ? 0.2383 0.2998 0.3145 -0.0214 0.0192  -0.0614 173 MET A CG  
1366 S SD  . MET A 173 ? 0.2774 0.3173 0.3507 -0.0356 0.0446  -0.0741 173 MET A SD  
1367 C CE  . MET A 173 ? 0.2801 0.3196 0.3627 -0.0359 0.0474  -0.0761 173 MET A CE  
1368 N N   . THR A 174 ? 0.2441 0.3414 0.4310 0.0115  -0.0097 -0.0597 174 THR A N   
1369 C CA  . THR A 174 ? 0.2153 0.3174 0.4242 0.0213  -0.0241 -0.0552 174 THR A CA  
1370 C C   . THR A 174 ? 0.2207 0.3337 0.4606 0.0256  -0.0348 -0.0582 174 THR A C   
1371 O O   . THR A 174 ? 0.2618 0.3784 0.5042 0.0204  -0.0294 -0.0639 174 THR A O   
1372 C CB  . THR A 174 ? 0.2976 0.3970 0.4764 0.0252  -0.0380 -0.0446 174 THR A CB  
1373 O OG1 . THR A 174 ? 0.2760 0.3799 0.4391 0.0262  -0.0477 -0.0420 174 THR A OG1 
1374 C CG2 . THR A 174 ? 0.2940 0.3874 0.4444 0.0188  -0.0283 -0.0428 174 THR A CG2 
1375 N N   . ARG A 175 ? 0.2350 0.3516 0.4981 0.0346  -0.0511 -0.0540 175 ARG A N   
1376 C CA  . ARG A 175 ? 0.2325 0.3605 0.5217 0.0388  -0.0692 -0.0548 175 ARG A CA  
1377 C C   . ARG A 175 ? 0.2086 0.3310 0.4584 0.0405  -0.0882 -0.0456 175 ARG A C   
1378 O O   . ARG A 175 ? 0.3070 0.4190 0.5371 0.0455  -0.0991 -0.0362 175 ARG A O   
1379 C CB  . ARG A 175 ? 0.2819 0.4158 0.6189 0.0482  -0.0799 -0.0545 175 ARG A CB  
1380 C CG  . ARG A 175 ? 0.2982 0.4373 0.6807 0.0467  -0.0575 -0.0658 175 ARG A CG  
1381 C CD  . ARG A 175 ? 0.3380 0.4696 0.7438 0.0564  -0.0581 -0.0620 175 ARG A CD  
1382 N NE  . ARG A 175 ? 0.3671 0.5030 0.8222 0.0555  -0.0345 -0.0749 175 ARG A NE  
1383 C CZ  . ARG A 175 ? 0.4015 0.5230 0.8438 0.0483  -0.0065 -0.0815 175 ARG A CZ  
1384 N NH1 . ARG A 175 ? 0.3222 0.4270 0.7080 0.0418  -0.0012 -0.0760 175 ARG A NH1 
1385 N NH2 . ARG A 175 ? 0.3893 0.5127 0.8773 0.0465  0.0172  -0.0949 175 ARG A NH2 
1386 N N   A MET A 176 ? 0.2569 0.3821 0.4927 0.0354  -0.0895 -0.0489 176 MET A N   
1387 N N   B MET A 176 ? 0.2564 0.3817 0.4926 0.0354  -0.0898 -0.0489 176 MET A N   
1388 C CA  A MET A 176 ? 0.2953 0.4119 0.4905 0.0352  -0.1015 -0.0427 176 MET A CA  
1389 C CA  B MET A 176 ? 0.2950 0.4115 0.4902 0.0353  -0.1016 -0.0426 176 MET A CA  
1390 C C   A MET A 176 ? 0.2990 0.4204 0.5017 0.0324  -0.1152 -0.0474 176 MET A C   
1391 C C   B MET A 176 ? 0.3008 0.4219 0.5023 0.0323  -0.1147 -0.0473 176 MET A C   
1392 O O   A MET A 176 ? 0.2804 0.4129 0.5157 0.0284  -0.1104 -0.0565 176 MET A O   
1393 O O   B MET A 176 ? 0.2818 0.4136 0.5142 0.0280  -0.1089 -0.0565 176 MET A O   
1394 C CB  A MET A 176 ? 0.3316 0.4418 0.4915 0.0312  -0.0858 -0.0418 176 MET A CB  
1395 C CB  B MET A 176 ? 0.3322 0.4421 0.4918 0.0315  -0.0859 -0.0413 176 MET A CB  
1396 C CG  A MET A 176 ? 0.3159 0.4293 0.4816 0.0253  -0.0711 -0.0494 176 MET A CG  
1397 C CG  B MET A 176 ? 0.3194 0.4307 0.4751 0.0260  -0.0762 -0.0477 176 MET A CG  
1398 S SD  A MET A 176 ? 0.4247 0.5294 0.5494 0.0238  -0.0633 -0.0461 176 MET A SD  
1399 S SD  B MET A 176 ? 0.3091 0.4117 0.4320 0.0254  -0.0852 -0.0463 176 MET A SD  
1400 C CE  A MET A 176 ? 0.2888 0.3877 0.3970 0.0249  -0.0780 -0.0457 176 MET A CE  
1401 C CE  B MET A 176 ? 0.2619 0.3605 0.3756 0.0212  -0.0678 -0.0507 176 MET A CE  
1402 N N   . GLY A 177 ? 0.2892 0.3998 0.4589 0.0327  -0.1310 -0.0420 177 GLY A N   
1403 C CA  . GLY A 177 ? 0.3675 0.4777 0.5329 0.0278  -0.1446 -0.0467 177 GLY A CA  
1404 C C   . GLY A 177 ? 0.3815 0.4836 0.5352 0.0299  -0.1730 -0.0404 177 GLY A C   
1405 O O   . GLY A 177 ? 0.3606 0.4526 0.5010 0.0357  -0.1809 -0.0307 177 GLY A O   
1406 N N   . THR A 178 ? 0.4045 0.5083 0.5606 0.0239  -0.1892 -0.0461 178 THR A N   
1407 C CA  . THR A 178 ? 0.3848 0.4756 0.5169 0.0229  -0.2194 -0.0404 178 THR A CA  
1408 C C   . THR A 178 ? 0.4086 0.5033 0.5679 0.0319  -0.2366 -0.0311 178 THR A C   
1409 O O   . THR A 178 ? 0.4282 0.5013 0.5505 0.0340  -0.2514 -0.0199 178 THR A O   
1410 C CB  . THR A 178 ? 0.4282 0.5243 0.5678 0.0131  -0.2341 -0.0504 178 THR A CB  
1411 O OG1 . THR A 178 ? 0.3983 0.4827 0.5047 0.0051  -0.2135 -0.0575 178 THR A OG1 
1412 C CG2 . THR A 178 ? 0.4617 0.5401 0.5686 0.0097  -0.2597 -0.0429 178 THR A CG2 
1413 N N   . SER A 179 ? 0.3209 0.4377 0.5396 0.0363  -0.2287 -0.0353 179 SER A N   
1414 C CA  . SER A 179 ? 0.3956 0.5137 0.6427 0.0452  -0.2399 -0.0274 179 SER A CA  
1415 C C   . SER A 179 ? 0.4680 0.5687 0.6921 0.0537  -0.2386 -0.0157 179 SER A C   
1416 O O   . SER A 179 ? 0.4121 0.5022 0.6383 0.0606  -0.2542 -0.0057 179 SER A O   
1417 C CB  . SER A 179 ? 0.4166 0.5596 0.7319 0.0476  -0.2260 -0.0368 179 SER A CB  
1418 O OG  . SER A 179 ? 0.5051 0.6538 0.8325 0.0486  -0.1994 -0.0420 179 SER A OG  
1419 N N   . VAL A 180 ? 0.3470 0.4437 0.5498 0.0532  -0.2215 -0.0167 180 VAL A N   
1420 C CA  . VAL A 180 ? 0.3968 0.4746 0.5736 0.0588  -0.2162 -0.0061 180 VAL A CA  
1421 C C   . VAL A 180 ? 0.4076 0.4551 0.5217 0.0563  -0.2336 0.0050  180 VAL A C   
1422 O O   . VAL A 180 ? 0.4588 0.4861 0.5569 0.0621  -0.2445 0.0169  180 VAL A O   
1423 C CB  . VAL A 180 ? 0.3338 0.4136 0.4987 0.0546  -0.1821 -0.0109 180 VAL A CB  
1424 C CG1 . VAL A 180 ? 0.3631 0.4237 0.5018 0.0575  -0.1741 -0.0015 180 VAL A CG1 
1425 C CG2 . VAL A 180 ? 0.3405 0.4431 0.5580 0.0549  -0.1644 -0.0217 180 VAL A CG2 
1426 N N   . LEU A 181 ? 0.4151 0.4548 0.4896 0.0468  -0.2344 0.0010  181 LEU A N   
1427 C CA  . LEU A 181 ? 0.4254 0.4322 0.4354 0.0418  -0.2491 0.0096  181 LEU A CA  
1428 C C   . LEU A 181 ? 0.5534 0.5504 0.5660 0.0443  -0.2772 0.0179  181 LEU A C   
1429 O O   . LEU A 181 ? 0.5533 0.5190 0.5204 0.0440  -0.2883 0.0297  181 LEU A O   
1430 C CB  . LEU A 181 ? 0.4853 0.4855 0.4579 0.0304  -0.2413 0.0008  181 LEU A CB  
1431 C CG  . LEU A 181 ? 0.5097 0.5091 0.4617 0.0263  -0.2066 -0.0047 181 LEU A CG  
1432 C CD1 . LEU A 181 ? 0.4902 0.4832 0.4151 0.0170  -0.2015 -0.0142 181 LEU A CD1 
1433 C CD2 . LEU A 181 ? 0.5302 0.5045 0.4387 0.0255  -0.1952 0.0042  181 LEU A CD2 
1434 N N   . GLU A 182 ? 0.4610 0.4833 0.5258 0.0457  -0.2851 0.0115  182 GLU A N   
1435 C CA  . GLU A 182 ? 0.5493 0.5667 0.6245 0.0487  -0.3100 0.0185  182 GLU A CA  
1436 C C   . GLU A 182 ? 0.5929 0.6048 0.6915 0.0614  -0.3142 0.0293  182 GLU A C   
1437 O O   . GLU A 182 ? 0.6993 0.6901 0.7781 0.0645  -0.3355 0.0408  182 GLU A O   
1438 C CB  . GLU A 182 ? 0.4801 0.5281 0.6095 0.0464  -0.3157 0.0075  182 GLU A CB  
1439 C CG  . GLU A 182 ? 0.5991 0.6517 0.7088 0.0335  -0.3107 -0.0041 182 GLU A CG  
1440 C CD  . GLU A 182 ? 0.7634 0.8458 0.9288 0.0300  -0.3137 -0.0157 182 GLU A CD  
1441 O OE1 . GLU A 182 ? 0.7323 0.8338 0.9548 0.0380  -0.3171 -0.0156 182 GLU A OE1 
1442 O OE2 . GLU A 182 ? 0.8555 0.9406 1.0076 0.0188  -0.3116 -0.0256 182 GLU A OE2 
1443 N N   . ALA A 183 ? 0.6000 0.6279 0.7386 0.0684  -0.2942 0.0257  183 ALA A N   
1444 C CA  . ALA A 183 ? 0.5566 0.5762 0.7167 0.0803  -0.2952 0.0348  183 ALA A CA  
1445 C C   . ALA A 183 ? 0.5887 0.5716 0.6884 0.0807  -0.2950 0.0478  183 ALA A C   
1446 O O   . ALA A 183 ? 0.6455 0.6066 0.7384 0.0883  -0.3064 0.0601  183 ALA A O   
1447 C CB  . ALA A 183 ? 0.5079 0.5537 0.7285 0.0859  -0.2715 0.0250  183 ALA A CB  
1448 N N   . LEU A 184 ? 0.6151 0.5891 0.6704 0.0724  -0.2816 0.0452  184 LEU A N   
1449 C CA  . LEU A 184 ? 0.6691 0.6067 0.6651 0.0707  -0.2778 0.0564  184 LEU A CA  
1450 C C   . LEU A 184 ? 0.6527 0.5523 0.5897 0.0661  -0.2971 0.0686  184 LEU A C   
1451 O O   . LEU A 184 ? 0.7013 0.5702 0.6146 0.0704  -0.3026 0.0819  184 LEU A O   
1452 C CB  . LEU A 184 ? 0.6371 0.5782 0.6015 0.0586  -0.2457 0.0467  184 LEU A CB  
1453 C CG  . LEU A 184 ? 0.7052 0.6104 0.6038 0.0507  -0.2306 0.0541  184 LEU A CG  
1454 C CD1 . LEU A 184 ? 0.6700 0.5638 0.5787 0.0561  -0.2189 0.0614  184 LEU A CD1 
1455 C CD2 . LEU A 184 ? 0.6763 0.5905 0.5541 0.0399  -0.2013 0.0430  184 LEU A CD2 
1456 N N   . GLY A 185 ? 0.7486 0.6465 0.6589 0.0564  -0.3066 0.0639  185 GLY A N   
1457 C CA  . GLY A 185 ? 0.7637 0.6225 0.6113 0.0495  -0.3230 0.0739  185 GLY A CA  
1458 C C   . GLY A 185 ? 0.9082 0.7257 0.6825 0.0414  -0.3074 0.0809  185 GLY A C   
1459 O O   . GLY A 185 ? 0.9083 0.7285 0.6640 0.0351  -0.2853 0.0736  185 GLY A O   
1460 N N   . ASP A 186 ? 0.9734 0.7509 0.7050 0.0410  -0.3178 0.0950  186 ASP A N   
1461 C CA  . ASP A 186 ? 1.0764 0.8095 0.7377 0.0321  -0.3000 0.1026  186 ASP A CA  
1462 C C   . ASP A 186 ? 1.0300 0.7571 0.7089 0.0410  -0.2881 0.1106  186 ASP A C   
1463 O O   . ASP A 186 ? 1.0636 0.7484 0.6872 0.0344  -0.2756 0.1199  186 ASP A O   
1464 C CB  . ASP A 186 ? 1.1453 0.8314 0.7424 0.0240  -0.3146 0.1131  186 ASP A CB  
1465 C CG  . ASP A 186 ? 1.3015 0.9814 0.8619 0.0107  -0.3199 0.1047  186 ASP A CG  
1466 O OD1 . ASP A 186 ? 1.2133 0.9124 0.7755 0.0041  -0.3023 0.0913  186 ASP A OD1 
1467 O OD2 . ASP A 186 ? 1.4847 1.1386 1.0133 0.0068  -0.3419 0.1116  186 ASP A OD2 
1468 N N   . GLY A 187 ? 0.9283 0.6941 0.6819 0.0543  -0.2889 0.1062  187 GLY A N   
1469 C CA  . GLY A 187 ? 0.7629 0.5270 0.5426 0.0613  -0.2712 0.1098  187 GLY A CA  
1470 C C   . GLY A 187 ? 0.8521 0.6262 0.6219 0.0493  -0.2279 0.0982  187 GLY A C   
1471 O O   . GLY A 187 ? 0.8262 0.6080 0.5712 0.0379  -0.2128 0.0886  187 GLY A O   
1472 N N   . GLU A 188 ? 0.7492 0.5231 0.5417 0.0521  -0.2083 0.0988  188 GLU A N   
1473 C CA  . GLU A 188 ? 0.8153 0.6006 0.6049 0.0407  -0.1703 0.0884  188 GLU A CA  
1474 C C   . GLU A 188 ? 0.7003 0.5380 0.5486 0.0427  -0.1571 0.0720  188 GLU A C   
1475 O O   . GLU A 188 ? 0.6601 0.5217 0.5615 0.0537  -0.1683 0.0691  188 GLU A O   
1476 C CB  . GLU A 188 ? 0.8840 0.6459 0.6716 0.0405  -0.1551 0.0946  188 GLU A CB  
1477 C CG  . GLU A 188 ? 1.1219 0.8249 0.8446 0.0368  -0.1637 0.1116  188 GLU A CG  
1478 C CD  . GLU A 188 ? 1.3302 1.0081 1.0521 0.0356  -0.1462 0.1169  188 GLU A CD  
1479 O OE1 . GLU A 188 ? 1.3053 1.0130 1.0778 0.0373  -0.1284 0.1063  188 GLU A OE1 
1480 O OE2 . GLU A 188 ? 1.4886 1.1136 1.1554 0.0316  -0.1496 0.1313  188 GLU A OE2 
1481 N N   . PHE A 189 ? 0.6725 0.5262 0.5112 0.0317  -0.1326 0.0615  189 PHE A N   
1482 C CA  . PHE A 189 ? 0.5836 0.4811 0.4687 0.0323  -0.1196 0.0477  189 PHE A CA  
1483 C C   . PHE A 189 ? 0.6177 0.5239 0.4997 0.0220  -0.0901 0.0407  189 PHE A C   
1484 O O   . PHE A 189 ? 0.6504 0.5333 0.4937 0.0126  -0.0774 0.0441  189 PHE A O   
1485 C CB  . PHE A 189 ? 0.5600 0.4753 0.4450 0.0319  -0.1279 0.0409  189 PHE A CB  
1486 C CG  . PHE A 189 ? 0.6037 0.5005 0.4368 0.0216  -0.1195 0.0404  189 PHE A CG  
1487 C CD1 . PHE A 189 ? 0.6579 0.5178 0.4402 0.0187  -0.1363 0.0495  189 PHE A CD1 
1488 C CD2 . PHE A 189 ? 0.5519 0.4665 0.3868 0.0147  -0.0951 0.0305  189 PHE A CD2 
1489 C CE1 . PHE A 189 ? 0.7367 0.5752 0.4673 0.0074  -0.1246 0.0473  189 PHE A CE1 
1490 C CE2 . PHE A 189 ? 0.5950 0.4924 0.3873 0.0056  -0.0835 0.0283  189 PHE A CE2 
1491 C CZ  . PHE A 189 ? 0.6792 0.5372 0.4174 0.0011  -0.0962 0.0359  189 PHE A CZ  
1492 N N   . ILE A 190 ? 0.5242 0.4636 0.4475 0.0227  -0.0794 0.0308  190 ILE A N   
1493 C CA  . ILE A 190 ? 0.5196 0.4739 0.4479 0.0132  -0.0561 0.0235  190 ILE A CA  
1494 C C   . ILE A 190 ? 0.4262 0.4001 0.3502 0.0097  -0.0492 0.0165  190 ILE A C   
1495 O O   . ILE A 190 ? 0.3883 0.3816 0.3310 0.0152  -0.0569 0.0119  190 ILE A O   
1496 C CB  . ILE A 190 ? 0.5283 0.5033 0.4962 0.0145  -0.0497 0.0168  190 ILE A CB  
1497 C CG1 . ILE A 190 ? 0.5802 0.5325 0.5545 0.0188  -0.0536 0.0228  190 ILE A CG1 
1498 C CG2 . ILE A 190 ? 0.4163 0.4083 0.3886 0.0035  -0.0305 0.0093  190 ILE A CG2 
1499 C CD1 . ILE A 190 ? 0.6788 0.6002 0.6213 0.0112  -0.0441 0.0295  190 ILE A CD1 
1500 N N   . LYS A 191 ? 0.4751 0.4427 0.3766 0.0004  -0.0330 0.0151  191 LYS A N   
1501 C CA  . LYS A 191 ? 0.4496 0.4330 0.3494 -0.0021 -0.0236 0.0083  191 LYS A CA  
1502 C C   . LYS A 191 ? 0.4119 0.4311 0.3498 -0.0029 -0.0142 0.0002  191 LYS A C   
1503 O O   . LYS A 191 ? 0.4037 0.4298 0.3516 -0.0103 -0.0024 -0.0020 191 LYS A O   
1504 C CB  . LYS A 191 ? 0.4775 0.4381 0.3405 -0.0121 -0.0076 0.0091  191 LYS A CB  
1505 C CG  . LYS A 191 ? 0.6105 0.5281 0.4245 -0.0134 -0.0181 0.0187  191 LYS A CG  
1506 C CD  . LYS A 191 ? 0.6323 0.5200 0.4054 -0.0265 0.0025  0.0201  191 LYS A CD  
1507 C CE  . LYS A 191 ? 0.8439 0.6815 0.5613 -0.0286 -0.0108 0.0324  191 LYS A CE  
1508 N NZ  . LYS A 191 ? 1.0635 0.8651 0.7343 -0.0436 0.0122  0.0341  191 LYS A NZ  
1509 N N   . CYS A 192 ? 0.3305 0.3703 0.2874 0.0036  -0.0204 -0.0041 192 CYS A N   
1510 C CA  . CYS A 192 ? 0.3532 0.4230 0.3409 0.0039  -0.0158 -0.0100 192 CYS A CA  
1511 C C   . CYS A 192 ? 0.3183 0.4000 0.3090 0.0067  -0.0103 -0.0141 192 CYS A C   
1512 O O   . CYS A 192 ? 0.3803 0.4542 0.3605 0.0119  -0.0166 -0.0143 192 CYS A O   
1513 C CB  . CYS A 192 ? 0.3353 0.4139 0.3424 0.0091  -0.0268 -0.0108 192 CYS A CB  
1514 S SG  . CYS A 192 ? 0.3456 0.4075 0.3548 0.0085  -0.0318 -0.0072 192 CYS A SG  
1515 N N   . LEU A 193 ? 0.2865 0.3869 0.2941 0.0031  0.0012  -0.0180 193 LEU A N   
1516 C CA  . LEU A 193 ? 0.2956 0.4088 0.3141 0.0073  0.0086  -0.0222 193 LEU A CA  
1517 C C   . LEU A 193 ? 0.3497 0.4929 0.4027 0.0099  0.0050  -0.0242 193 LEU A C   
1518 O O   . LEU A 193 ? 0.3001 0.4576 0.3688 0.0031  0.0072  -0.0253 193 LEU A O   
1519 C CB  . LEU A 193 ? 0.3227 0.4284 0.3313 0.0006  0.0278  -0.0254 193 LEU A CB  
1520 C CG  . LEU A 193 ? 0.3408 0.4640 0.3722 0.0045  0.0408  -0.0316 193 LEU A CG  
1521 C CD1 . LEU A 193 ? 0.3337 0.4462 0.3534 0.0134  0.0372  -0.0328 193 LEU A CD1 
1522 C CD2 . LEU A 193 ? 0.3304 0.4459 0.3552 -0.0050 0.0644  -0.0365 193 LEU A CD2 
1523 N N   . HIS A 194 ? 0.2956 0.4459 0.3577 0.0189  -0.0017 -0.0244 194 HIS A N   
1524 C CA  . HIS A 194 ? 0.2989 0.4718 0.3869 0.0224  -0.0092 -0.0241 194 HIS A CA  
1525 C C   . HIS A 194 ? 0.3013 0.4821 0.4043 0.0324  -0.0060 -0.0254 194 HIS A C   
1526 O O   . HIS A 194 ? 0.2368 0.4012 0.3247 0.0373  -0.0018 -0.0267 194 HIS A O   
1527 C CB  . HIS A 194 ? 0.2780 0.4455 0.3590 0.0232  -0.0222 -0.0214 194 HIS A CB  
1528 C CG  . HIS A 194 ? 0.2501 0.4322 0.3461 0.0265  -0.0314 -0.0197 194 HIS A CG  
1529 N ND1 . HIS A 194 ? 0.2075 0.3844 0.3019 0.0351  -0.0363 -0.0178 194 HIS A ND1 
1530 C CD2 . HIS A 194 ? 0.2278 0.4266 0.3373 0.0215  -0.0379 -0.0191 194 HIS A CD2 
1531 C CE1 . HIS A 194 ? 0.2911 0.4786 0.3949 0.0362  -0.0461 -0.0147 194 HIS A CE1 
1532 N NE2 . HIS A 194 ? 0.2488 0.4507 0.3618 0.0278  -0.0485 -0.0155 194 HIS A NE2 
1533 N N   . SER A 195 ? 0.1967 0.4019 0.3304 0.0352  -0.0090 -0.0253 195 SER A N   
1534 C CA  . SER A 195 ? 0.2093 0.4229 0.3638 0.0473  -0.0085 -0.0252 195 SER A CA  
1535 C C   . SER A 195 ? 0.2905 0.5262 0.4706 0.0508  -0.0249 -0.0207 195 SER A C   
1536 O O   . SER A 195 ? 0.2353 0.4899 0.4307 0.0427  -0.0298 -0.0212 195 SER A O   
1537 C CB  . SER A 195 ? 0.2598 0.4803 0.4333 0.0490  0.0110  -0.0314 195 SER A CB  
1538 O OG  . SER A 195 ? 0.2123 0.4455 0.4168 0.0621  0.0110  -0.0314 195 SER A OG  
1539 N N   . VAL A 196 ? 0.2736 0.5039 0.4552 0.0619  -0.0340 -0.0162 196 VAL A N   
1540 C CA  . VAL A 196 ? 0.2772 0.5241 0.4795 0.0670  -0.0522 -0.0100 196 VAL A CA  
1541 C C   . VAL A 196 ? 0.2740 0.5517 0.5254 0.0734  -0.0505 -0.0119 196 VAL A C   
1542 O O   . VAL A 196 ? 0.2719 0.5703 0.5472 0.0755  -0.0690 -0.0071 196 VAL A O   
1543 C CB  . VAL A 196 ? 0.3452 0.5720 0.5324 0.0777  -0.0611 -0.0035 196 VAL A CB  
1544 C CG1 . VAL A 196 ? 0.2317 0.4337 0.3779 0.0690  -0.0647 -0.0021 196 VAL A CG1 
1545 C CG2 . VAL A 196 ? 0.3270 0.5418 0.5195 0.0889  -0.0457 -0.0069 196 VAL A CG2 
1546 N N   . GLY A 197 ? 0.2986 0.5794 0.5661 0.0757  -0.0288 -0.0193 197 GLY A N   
1547 C CA  . GLY A 197 ? 0.2020 0.5137 0.5229 0.0806  -0.0218 -0.0236 197 GLY A CA  
1548 C C   . GLY A 197 ? 0.2645 0.5858 0.6212 0.0997  -0.0300 -0.0191 197 GLY A C   
1549 O O   . GLY A 197 ? 0.3275 0.6822 0.7362 0.1051  -0.0387 -0.0186 197 GLY A O   
1550 N N   A CYS A 198 ? 0.2915 0.5843 0.6241 0.1102  -0.0285 -0.0157 198 CYS A N   
1551 N N   B CYS A 198 ? 0.2915 0.5843 0.6244 0.1102  -0.0277 -0.0160 198 CYS A N   
1552 C CA  A CYS A 198 ? 0.3136 0.6073 0.6749 0.1298  -0.0357 -0.0102 198 CYS A CA  
1553 C CA  B CYS A 198 ? 0.3139 0.6073 0.6746 0.1297  -0.0358 -0.0101 198 CYS A CA  
1554 C C   A CYS A 198 ? 0.3076 0.5766 0.6615 0.1378  -0.0101 -0.0172 198 CYS A C   
1555 C C   B CYS A 198 ? 0.3073 0.5764 0.6618 0.1381  -0.0103 -0.0171 198 CYS A C   
1556 O O   A CYS A 198 ? 0.3695 0.6068 0.6898 0.1426  -0.0114 -0.0137 198 CYS A O   
1557 O O   B CYS A 198 ? 0.3684 0.6062 0.6906 0.1434  -0.0119 -0.0134 198 CYS A O   
1558 C CB  A CYS A 198 ? 0.3335 0.6099 0.6666 0.1339  -0.0625 0.0027  198 CYS A CB  
1559 C CB  B CYS A 198 ? 0.3345 0.6097 0.6645 0.1329  -0.0621 0.0025  198 CYS A CB  
1560 S SG  A CYS A 198 ? 0.2874 0.5894 0.6290 0.1258  -0.0953 0.0112  198 CYS A SG  
1561 S SG  B CYS A 198 ? 0.3222 0.6120 0.6945 0.1531  -0.0889 0.0151  198 CYS A SG  
1562 N N   . PRO A 199 ? 0.2978 0.5783 0.6809 0.1378  0.0155  -0.0283 199 PRO A N   
1563 C CA  . PRO A 199 ? 0.3617 0.6147 0.7332 0.1433  0.0424  -0.0368 199 PRO A CA  
1564 C C   . PRO A 199 ? 0.4185 0.6651 0.8185 0.1649  0.0390  -0.0323 199 PRO A C   
1565 O O   . PRO A 199 ? 0.4257 0.6992 0.8763 0.1784  0.0225  -0.0253 199 PRO A O   
1566 C CB  . PRO A 199 ? 0.3799 0.6495 0.7805 0.1367  0.0711  -0.0498 199 PRO A CB  
1567 C CG  . PRO A 199 ? 0.2897 0.6049 0.7457 0.1372  0.0566  -0.0469 199 PRO A CG  
1568 C CD  . PRO A 199 ? 0.2576 0.5745 0.6847 0.1308  0.0234  -0.0348 199 PRO A CD  
1569 N N   . LEU A 200 ? 0.4588 0.6675 0.8251 0.1679  0.0534  -0.0360 200 LEU A N   
1570 C CA  . LEU A 200 ? 0.5111 0.7032 0.8960 0.1877  0.0548  -0.0328 200 LEU A CA  
1571 C C   . LEU A 200 ? 0.5021 0.6991 0.9315 0.1973  0.0865  -0.0455 200 LEU A C   
1572 O O   . LEU A 200 ? 0.5441 0.7340 0.9578 0.1844  0.1141  -0.0592 200 LEU A O   
1573 C CB  . LEU A 200 ? 0.5310 0.6776 0.8568 0.1838  0.0564  -0.0322 200 LEU A CB  
1574 C CG  . LEU A 200 ? 0.5527 0.6917 0.8360 0.1735  0.0301  -0.0217 200 LEU A CG  
1575 C CD1 . LEU A 200 ? 0.5862 0.6838 0.8163 0.1664  0.0357  -0.0244 200 LEU A CD1 
1576 C CD2 . LEU A 200 ? 0.5054 0.6566 0.8110 0.1860  0.0017  -0.0062 200 LEU A CD2 
1577 N N   . PRO A 201 ? 0.6414 0.8448 1.1129 0.2163  0.0820  -0.0408 201 PRO A N   
1578 C CA  . PRO A 201 ? 0.6071 0.8117 1.0893 0.2319  0.0493  -0.0236 201 PRO A CA  
1579 C C   . PRO A 201 ? 0.6245 0.8692 1.1294 0.2288  0.0182  -0.0127 201 PRO A C   
1580 O O   . PRO A 201 ? 0.6040 0.8816 1.1360 0.2196  0.0244  -0.0191 201 PRO A O   
1581 C CB  . PRO A 201 ? 0.6257 0.8218 1.1384 0.2488  0.0618  -0.0263 201 PRO A CB  
1582 C CG  . PRO A 201 ? 0.6331 0.8496 1.1739 0.2405  0.0907  -0.0418 201 PRO A CG  
1583 C CD  . PRO A 201 ? 0.5983 0.8032 1.0983 0.2201  0.1100  -0.0526 201 PRO A CD  
1584 N N   . LEU A 202 ? 0.6241 0.8626 1.1136 0.2346  -0.0144 0.0037  202 LEU A N   
1585 C CA  . LEU A 202 ? 0.7570 1.0263 1.2536 0.2277  -0.0448 0.0139  202 LEU A CA  
1586 C C   . LEU A 202 ? 0.9154 1.2182 1.4642 0.2367  -0.0517 0.0157  202 LEU A C   
1587 O O   . LEU A 202 ? 0.8490 1.1430 1.4165 0.2551  -0.0567 0.0218  202 LEU A O   
1588 C CB  . LEU A 202 ? 0.7363 0.9820 1.1939 0.2301  -0.0757 0.0307  202 LEU A CB  
1589 C CG  . LEU A 202 ? 0.6499 0.8656 1.0555 0.2184  -0.0738 0.0291  202 LEU A CG  
1590 C CD1 . LEU A 202 ? 0.6320 0.8249 0.9941 0.2163  -0.1039 0.0452  202 LEU A CD1 
1591 C CD2 . LEU A 202 ? 0.5720 0.8066 0.9631 0.1963  -0.0627 0.0180  202 LEU A CD2 
1592 N N   . LYS A 203 ? 1.1196 1.4601 1.6935 0.2237  -0.0518 0.0100  203 LYS A N   
1593 C CA  . LYS A 203 ? 1.1681 1.5447 1.7938 0.2298  -0.0632 0.0122  203 LYS A CA  
1594 C C   . LYS A 203 ? 1.2147 1.5983 1.8307 0.2325  -0.1043 0.0294  203 LYS A C   
1595 O O   . LYS A 203 ? 1.2262 1.6232 1.8757 0.2469  -0.1204 0.0367  203 LYS A O   
1596 C CB  . LYS A 203 ? 1.1889 1.6006 1.8435 0.2129  -0.0477 -0.0004 203 LYS A CB  
1597 C CG  . LYS A 203 ? 1.1874 1.5894 1.8460 0.2073  -0.0054 -0.0176 203 LYS A CG  
1598 C CD  . LYS A 203 ? 1.2156 1.6111 1.9096 0.2245  0.0146  -0.0233 203 LYS A CD  
1599 C CE  . LYS A 203 ? 1.2591 1.6412 1.9504 0.2153  0.0584  -0.0415 203 LYS A CE  
1600 N NZ  . LYS A 203 ? 1.1830 1.5280 1.8145 0.2067  0.0712  -0.0450 203 LYS A NZ  
1601 N N   . LYS A 204 ? 1.3009 1.6736 1.8695 0.2182  -0.1214 0.0355  204 LYS A N   
1602 C CA  . LYS A 204 ? 1.2640 1.6367 1.8098 0.2156  -0.1583 0.0505  204 LYS A CA  
1603 C C   . LYS A 204 ? 1.2931 1.6193 1.7803 0.2185  -0.1692 0.0619  204 LYS A C   
1604 O O   . LYS A 204 ? 1.2778 1.5796 1.7356 0.2133  -0.1516 0.0562  204 LYS A O   
1605 C CB  . LYS A 204 ? 1.3012 1.6983 1.8373 0.1925  -0.1688 0.0468  204 LYS A CB  
1606 C CG  . LYS A 204 ? 1.3701 1.8070 1.9556 0.1838  -0.1501 0.0328  204 LYS A CG  
1607 C CD  . LYS A 204 ? 1.4201 1.8715 1.9867 0.1594  -0.1557 0.0282  204 LYS A CD  
1608 C CE  . LYS A 204 ? 1.3437 1.8284 1.9545 0.1488  -0.1327 0.0140  204 LYS A CE  
1609 N NZ  . LYS A 204 ? 1.1194 1.6135 1.7097 0.1246  -0.1358 0.0093  204 LYS A NZ  
1610 N N   . PRO A 205 ? 1.0518 1.3633 1.5201 0.2260  -0.1978 0.0779  205 PRO A N   
1611 C CA  . PRO A 205 ? 0.8943 1.1580 1.3016 0.2254  -0.2079 0.0893  205 PRO A CA  
1612 C C   . PRO A 205 ? 0.8443 1.1011 1.2028 0.2018  -0.2178 0.0888  205 PRO A C   
1613 O O   . PRO A 205 ? 0.7728 1.0571 1.1359 0.1883  -0.2314 0.0868  205 PRO A O   
1614 C CB  . PRO A 205 ? 1.0075 1.2595 1.4120 0.2396  -0.2353 0.1066  205 PRO A CB  
1615 C CG  . PRO A 205 ? 0.9792 1.2787 1.4293 0.2381  -0.2505 0.1047  205 PRO A CG  
1616 C CD  . PRO A 205 ? 1.0089 1.3443 1.5111 0.2358  -0.2218 0.0863  205 PRO A CD  
1617 N N   . LEU A 206 ? 0.7113 0.9299 1.0230 0.1968  -0.2104 0.0893  206 LEU A N   
1618 C CA  . LEU A 206 ? 0.5481 0.7557 0.8123 0.1752  -0.2157 0.0866  206 LEU A CA  
1619 C C   . LEU A 206 ? 0.6038 0.7797 0.8124 0.1683  -0.2416 0.1011  206 LEU A C   
1620 O O   . LEU A 206 ? 0.6524 0.7988 0.8450 0.1808  -0.2512 0.1141  206 LEU A O   
1621 C CB  . LEU A 206 ? 0.4624 0.6451 0.7035 0.1723  -0.1941 0.0771  206 LEU A CB  
1622 C CG  . LEU A 206 ? 0.5049 0.7098 0.7841 0.1743  -0.1627 0.0611  206 LEU A CG  
1623 C CD1 . LEU A 206 ? 0.4743 0.6506 0.7082 0.1618  -0.1365 0.0515  206 LEU A CD1 
1624 C CD2 . LEU A 206 ? 0.4628 0.7139 0.7807 0.1649  -0.1635 0.0526  206 LEU A CD2 
1625 N N   . VAL A 207 ? 0.5539 0.7324 0.7299 0.1472  -0.2510 0.0983  207 VAL A N   
1626 C CA  . VAL A 207 ? 0.5294 0.6736 0.6429 0.1353  -0.2713 0.1089  207 VAL A CA  
1627 C C   . VAL A 207 ? 0.6197 0.7205 0.6763 0.1244  -0.2598 0.1066  207 VAL A C   
1628 O O   . VAL A 207 ? 0.5141 0.6250 0.5690 0.1117  -0.2407 0.0929  207 VAL A O   
1629 C CB  . VAL A 207 ? 0.6398 0.8083 0.7477 0.1175  -0.2866 0.1053  207 VAL A CB  
1630 C CG1 . VAL A 207 ? 0.6385 0.7666 0.6773 0.1045  -0.3057 0.1154  207 VAL A CG1 
1631 C CG2 . VAL A 207 ? 0.5224 0.7374 0.6922 0.1280  -0.2969 0.1049  207 VAL A CG2 
1632 N N   . ASN A 208 ? 0.5919 0.6435 0.6001 0.1276  -0.2651 0.1185  208 ASN A N   
1633 C CA  . ASN A 208 ? 0.6176 0.6251 0.5690 0.1146  -0.2437 0.1142  208 ASN A CA  
1634 C C   . ASN A 208 ? 0.6214 0.6396 0.6004 0.1177  -0.2090 0.0991  208 ASN A C   
1635 O O   . ASN A 208 ? 0.6216 0.6270 0.5738 0.1020  -0.1866 0.0883  208 ASN A O   
1636 C CB  . ASN A 208 ? 0.6302 0.6274 0.5331 0.0878  -0.2427 0.1082  208 ASN A CB  
1637 C CG  . ASN A 208 ? 0.7821 0.7423 0.6260 0.0793  -0.2705 0.1233  208 ASN A CG  
1638 O OD1 . ASN A 208 ? 0.8768 0.8013 0.6956 0.0884  -0.2771 0.1366  208 ASN A OD1 
1639 N ND2 . ASN A 208 ? 0.8051 0.7740 0.6277 0.0595  -0.2779 0.1184  208 ASN A ND2 
1640 N N   . ASN A 209 ? 0.5682 0.6093 0.6015 0.1378  -0.2049 0.0981  209 ASN A N   
1641 C CA  . ASN A 209 ? 0.6128 0.6627 0.6703 0.1408  -0.1743 0.0840  209 ASN A CA  
1642 C C   . ASN A 209 ? 0.5172 0.5958 0.5835 0.1248  -0.1596 0.0689  209 ASN A C   
1643 O O   . ASN A 209 ? 0.5266 0.6016 0.5905 0.1198  -0.1357 0.0575  209 ASN A O   
1644 C CB  . ASN A 209 ? 0.6757 0.6798 0.6935 0.1382  -0.1556 0.0830  209 ASN A CB  
1645 C CG  . ASN A 209 ? 0.6930 0.6629 0.7014 0.1551  -0.1662 0.0978  209 ASN A CG  
1646 O OD1 . ASN A 209 ? 0.7790 0.7563 0.8271 0.1746  -0.1630 0.0988  209 ASN A OD1 
1647 N ND2 . ASN A 209 ? 0.7757 0.7040 0.7294 0.1473  -0.1770 0.1091  209 ASN A ND2 
1648 N N   . TRP A 210 ? 0.4520 0.5577 0.5276 0.1163  -0.1750 0.0690  210 TRP A N   
1649 C CA  . TRP A 210 ? 0.4891 0.6163 0.5675 0.1000  -0.1627 0.0562  210 TRP A CA  
1650 C C   . TRP A 210 ? 0.4160 0.5855 0.5515 0.1073  -0.1570 0.0490  210 TRP A C   
1651 O O   . TRP A 210 ? 0.3293 0.5275 0.4985 0.1118  -0.1750 0.0529  210 TRP A O   
1652 C CB  . TRP A 210 ? 0.4441 0.5693 0.4921 0.0828  -0.1791 0.0587  210 TRP A CB  
1653 C CG  . TRP A 210 ? 0.4551 0.5913 0.4977 0.0656  -0.1634 0.0459  210 TRP A CG  
1654 C CD1 . TRP A 210 ? 0.3902 0.5589 0.4580 0.0580  -0.1663 0.0397  210 TRP A CD1 
1655 C CD2 . TRP A 210 ? 0.4332 0.5472 0.4465 0.0546  -0.1421 0.0377  210 TRP A CD2 
1656 N NE1 . TRP A 210 ? 0.3840 0.5483 0.4363 0.0438  -0.1483 0.0293  210 TRP A NE1 
1657 C CE2 . TRP A 210 ? 0.4658 0.5987 0.4876 0.0423  -0.1341 0.0280  210 TRP A CE2 
1658 C CE3 . TRP A 210 ? 0.4842 0.5647 0.4683 0.0536  -0.1288 0.0374  210 TRP A CE3 
1659 C CZ2 . TRP A 210 ? 0.3924 0.5123 0.3971 0.0315  -0.1153 0.0190  210 TRP A CZ2 
1660 C CZ3 . TRP A 210 ? 0.3662 0.4377 0.3367 0.0415  -0.1099 0.0271  210 TRP A CZ3 
1661 C CH2 . TRP A 210 ? 0.3786 0.4701 0.3606 0.0317  -0.1042 0.0186  210 TRP A CH2 
1662 N N   . ALA A 211 ? 0.2998 0.4722 0.4451 0.1072  -0.1320 0.0382  211 ALA A N   
1663 C CA  . ALA A 211 ? 0.3264 0.5316 0.5177 0.1114  -0.1206 0.0299  211 ALA A CA  
1664 C C   . ALA A 211 ? 0.3688 0.5979 0.5648 0.0954  -0.1222 0.0240  211 ALA A C   
1665 O O   . ALA A 211 ? 0.3589 0.5760 0.5249 0.0816  -0.1127 0.0185  211 ALA A O   
1666 C CB  . ALA A 211 ? 0.4090 0.6013 0.5968 0.1138  -0.0943 0.0207  211 ALA A CB  
1667 N N   . CYS A 212 ? 0.2902 0.5531 0.5272 0.0973  -0.1340 0.0246  212 CYS A N   
1668 C CA  . CYS A 212 ? 0.3051 0.5911 0.5501 0.0812  -0.1348 0.0182  212 CYS A CA  
1669 C C   . CYS A 212 ? 0.3455 0.6730 0.6517 0.0869  -0.1406 0.0161  212 CYS A C   
1670 O O   . CYS A 212 ? 0.2505 0.5894 0.5912 0.1036  -0.1521 0.0224  212 CYS A O   
1671 C CB  . CYS A 212 ? 0.2593 0.5333 0.4659 0.0668  -0.1542 0.0228  212 CYS A CB  
1672 S SG  . CYS A 212 ? 0.3567 0.6401 0.5735 0.0731  -0.1923 0.0361  212 CYS A SG  
1673 N N   . ASN A 213 ? 0.2919 0.6416 0.6143 0.0729  -0.1319 0.0071  213 ASN A N   
1674 C CA  . ASN A 213 ? 0.3288 0.7213 0.7134 0.0739  -0.1333 0.0021  213 ASN A CA  
1675 C C   . ASN A 213 ? 0.2639 0.6715 0.6435 0.0533  -0.1462 -0.0003 213 ASN A C   
1676 O O   . ASN A 213 ? 0.3053 0.7200 0.6865 0.0390  -0.1287 -0.0106 213 ASN A O   
1677 C CB  . ASN A 213 ? 0.3441 0.7437 0.7534 0.0753  -0.0998 -0.0089 213 ASN A CB  
1678 C CG  . ASN A 213 ? 0.3472 0.7822 0.8181 0.0786  -0.0936 -0.0121 213 ASN A CG  
1679 O OD1 . ASN A 213 ? 0.3631 0.8213 0.8521 0.0692  -0.1082 -0.0100 213 ASN A OD1 
1680 N ND2 . ASN A 213 ? 0.3302 0.7653 0.8267 0.0903  -0.0693 -0.0176 213 ASN A ND2 
1681 N N   . PRO A 214 ? 0.3280 0.7350 0.6924 0.0495  -0.1738 0.0095  214 PRO A N   
1682 C CA  . PRO A 214 ? 0.3137 0.7299 0.6647 0.0276  -0.1861 0.0059  214 PRO A CA  
1683 C C   . PRO A 214 ? 0.3294 0.7816 0.7290 0.0175  -0.1769 -0.0019 214 PRO A C   
1684 O O   . PRO A 214 ? 0.3586 0.8119 0.7507 -0.0024 -0.1726 -0.0102 214 PRO A O   
1685 C CB  . PRO A 214 ? 0.3975 0.8064 0.7228 0.0303  -0.2161 0.0149  214 PRO A CB  
1686 C CG  . PRO A 214 ? 0.3386 0.7204 0.6465 0.0499  -0.2180 0.0255  214 PRO A CG  
1687 C CD  . PRO A 214 ? 0.3600 0.7541 0.7115 0.0645  -0.1939 0.0223  214 PRO A CD  
1688 N N   . GLU A 215 ? 0.2848 0.7633 0.7343 0.0306  -0.1718 -0.0009 215 GLU A N   
1689 C CA  . GLU A 215 ? 0.2489 0.7622 0.7470 0.0207  -0.1623 -0.0088 215 GLU A CA  
1690 C C   . GLU A 215 ? 0.3087 0.8172 0.8110 0.0088  -0.1309 -0.0215 215 GLU A C   
1691 O O   . GLU A 215 ? 0.2358 0.7603 0.7548 -0.0091 -0.1249 -0.0293 215 GLU A O   
1692 C CB  . GLU A 215 ? 0.4211 0.9596 0.9723 0.0393  -0.1587 -0.0071 215 GLU A CB  
1693 C CG  . GLU A 215 ? 0.6141 1.1577 1.1660 0.0534  -0.1896 0.0040  215 GLU A CG  
1694 C CD  . GLU A 215 ? 0.8538 1.4217 1.4641 0.0725  -0.1849 0.0046  215 GLU A CD  
1695 O OE1 . GLU A 215 ? 0.8552 1.4278 1.4961 0.0773  -0.1543 -0.0035 215 GLU A OE1 
1696 O OE2 . GLU A 215 ? 0.9268 1.5071 1.5514 0.0826  -0.2112 0.0125  215 GLU A OE2 
1697 N N   . LEU A 216 ? 0.2081 0.6941 0.6924 0.0181  -0.1102 -0.0251 216 LEU A N   
1698 C CA  . LEU A 216 ? 0.2494 0.7313 0.7333 0.0092  -0.0777 -0.0383 216 LEU A CA  
1699 C C   . LEU A 216 ? 0.2572 0.7047 0.6783 -0.0019 -0.0726 -0.0395 216 LEU A C   
1700 O O   . LEU A 216 ? 0.2638 0.6905 0.6629 -0.0070 -0.0458 -0.0443 216 LEU A O   
1701 C CB  . LEU A 216 ? 0.3030 0.7797 0.8037 0.0255  -0.0528 -0.0413 216 LEU A CB  
1702 C CG  . LEU A 216 ? 0.2019 0.7027 0.7564 0.0359  -0.0464 -0.0405 216 LEU A CG  
1703 C CD1 . LEU A 216 ? 0.2247 0.7111 0.7848 0.0505  -0.0190 -0.0451 216 LEU A CD1 
1704 C CD2 . LEU A 216 ? 0.2093 0.7354 0.7976 0.0190  -0.0345 -0.0490 216 LEU A CD2 
1705 N N   . THR A 217 ? 0.2294 0.6626 0.6143 -0.0064 -0.0962 -0.0331 217 THR A N   
1706 C CA  . THR A 217 ? 0.2660 0.6596 0.5897 -0.0147 -0.0892 -0.0320 217 THR A CA  
1707 C C   . THR A 217 ? 0.2493 0.6383 0.5645 -0.0338 -0.0709 -0.0406 217 THR A C   
1708 O O   . THR A 217 ? 0.2236 0.6343 0.5602 -0.0488 -0.0772 -0.0462 217 THR A O   
1709 C CB  . THR A 217 ? 0.2930 0.6729 0.5826 -0.0186 -0.1149 -0.0256 217 THR A CB  
1710 O OG1 . THR A 217 ? 0.2968 0.6735 0.5874 -0.0008 -0.1304 -0.0161 217 THR A OG1 
1711 C CG2 . THR A 217 ? 0.2758 0.6166 0.5101 -0.0269 -0.1042 -0.0263 217 THR A CG2 
1712 N N   . LEU A 218 ? 0.2301 0.5888 0.5131 -0.0336 -0.0495 -0.0414 218 LEU A N   
1713 C CA  . LEU A 218 ? 0.2007 0.5462 0.4691 -0.0498 -0.0314 -0.0475 218 LEU A CA  
1714 C C   . LEU A 218 ? 0.2917 0.5961 0.5114 -0.0468 -0.0224 -0.0437 218 LEU A C   
1715 O O   . LEU A 218 ? 0.2439 0.5347 0.4531 -0.0340 -0.0150 -0.0403 218 LEU A O   
1716 C CB  . LEU A 218 ? 0.2028 0.5636 0.5034 -0.0531 -0.0088 -0.0541 218 LEU A CB  
1717 C CG  . LEU A 218 ? 0.2370 0.5854 0.5264 -0.0724 0.0106  -0.0605 218 LEU A CG  
1718 C CD1 . LEU A 218 ? 0.2914 0.6581 0.5951 -0.0900 -0.0022 -0.0657 218 LEU A CD1 
1719 C CD2 . LEU A 218 ? 0.3166 0.6741 0.6320 -0.0752 0.0369  -0.0669 218 LEU A CD2 
1720 N N   . ILE A 219 ? 0.2335 0.5186 0.4259 -0.0585 -0.0236 -0.0448 219 ILE A N   
1721 C CA  . ILE A 219 ? 0.3003 0.5489 0.4546 -0.0561 -0.0158 -0.0418 219 ILE A CA  
1722 C C   . ILE A 219 ? 0.3764 0.6097 0.5218 -0.0691 0.0015  -0.0456 219 ILE A C   
1723 O O   . ILE A 219 ? 0.3348 0.5693 0.4809 -0.0844 0.0017  -0.0506 219 ILE A O   
1724 C CB  . ILE A 219 ? 0.2628 0.4967 0.3937 -0.0576 -0.0282 -0.0404 219 ILE A CB  
1725 C CG1 . ILE A 219 ? 0.3365 0.5817 0.4718 -0.0468 -0.0450 -0.0360 219 ILE A CG1 
1726 C CG2 . ILE A 219 ? 0.3032 0.5040 0.4062 -0.0531 -0.0197 -0.0380 219 ILE A CG2 
1727 C CD1 . ILE A 219 ? 0.2775 0.5471 0.4290 -0.0542 -0.0627 -0.0372 219 ILE A CD1 
1728 N N   . ALA A 220 ? 0.2751 0.4903 0.4082 -0.0642 0.0160  -0.0430 220 ALA A N   
1729 C CA  . ALA A 220 ? 0.3021 0.4990 0.4239 -0.0761 0.0339  -0.0451 220 ALA A CA  
1730 C C   . ALA A 220 ? 0.3324 0.4886 0.4166 -0.0713 0.0371  -0.0387 220 ALA A C   
1731 O O   . ALA A 220 ? 0.3133 0.4590 0.3845 -0.0575 0.0301  -0.0333 220 ALA A O   
1732 C CB  . ALA A 220 ? 0.2806 0.4878 0.4178 -0.0775 0.0505  -0.0479 220 ALA A CB  
1733 N N   . HIS A 221 ? 0.3258 0.4590 0.3947 -0.0830 0.0471  -0.0394 221 HIS A N   
1734 C CA  . HIS A 221 ? 0.3588 0.4520 0.3961 -0.0783 0.0487  -0.0324 221 HIS A CA  
1735 C C   . HIS A 221 ? 0.4173 0.4839 0.4344 -0.0882 0.0665  -0.0305 221 HIS A C   
1736 O O   . HIS A 221 ? 0.4297 0.5016 0.4561 -0.1044 0.0790  -0.0368 221 HIS A O   
1737 C CB  . HIS A 221 ? 0.3494 0.4311 0.3838 -0.0816 0.0435  -0.0342 221 HIS A CB  
1738 C CG  . HIS A 221 ? 0.3646 0.4674 0.4127 -0.0759 0.0293  -0.0371 221 HIS A CG  
1739 N ND1 . HIS A 221 ? 0.3258 0.4600 0.3938 -0.0833 0.0232  -0.0433 221 HIS A ND1 
1740 C CD2 . HIS A 221 ? 0.2928 0.3878 0.3364 -0.0645 0.0201  -0.0344 221 HIS A CD2 
1741 C CE1 . HIS A 221 ? 0.3234 0.4634 0.3914 -0.0770 0.0110  -0.0434 221 HIS A CE1 
1742 N NE2 . HIS A 221 ? 0.3056 0.4227 0.3601 -0.0662 0.0110  -0.0389 221 HIS A NE2 
1743 N N   . LEU A 222 ? 0.4328 0.4690 0.4199 -0.0798 0.0671  -0.0219 222 LEU A N   
1744 C CA  . LEU A 222 ? 0.4812 0.4815 0.4367 -0.0887 0.0830  -0.0175 222 LEU A CA  
1745 C C   . LEU A 222 ? 0.5698 0.5274 0.4939 -0.0804 0.0738  -0.0065 222 LEU A C   
1746 O O   . LEU A 222 ? 0.5685 0.5046 0.4665 -0.0701 0.0652  0.0021  222 LEU A O   
1747 C CB  . LEU A 222 ? 0.5298 0.5291 0.4725 -0.0882 0.0929  -0.0173 222 LEU A CB  
1748 C CG  . LEU A 222 ? 0.5741 0.6136 0.5534 -0.0961 0.1063  -0.0285 222 LEU A CG  
1749 C CD1 . LEU A 222 ? 0.5052 0.5838 0.5172 -0.0826 0.0905  -0.0315 222 LEU A CD1 
1750 C CD2 . LEU A 222 ? 0.5549 0.5766 0.5131 -0.1041 0.1292  -0.0300 222 LEU A CD2 
1751 N N   . PRO A 223 ? 0.5622 0.5057 0.4890 -0.0847 0.0746  -0.0068 223 PRO A N   
1752 C CA  . PRO A 223 ? 0.6164 0.5220 0.5233 -0.0737 0.0643  0.0037  223 PRO A CA  
1753 C C   . PRO A 223 ? 0.7786 0.6377 0.6410 -0.0739 0.0676  0.0157  223 PRO A C   
1754 O O   . PRO A 223 ? 0.7930 0.6276 0.6385 -0.0598 0.0509  0.0267  223 PRO A O   
1755 C CB  . PRO A 223 ? 0.6321 0.5303 0.5514 -0.0823 0.0718  -0.0018 223 PRO A CB  
1756 C CG  . PRO A 223 ? 0.6167 0.5344 0.5461 -0.1027 0.0892  -0.0124 223 PRO A CG  
1757 C CD  . PRO A 223 ? 0.5302 0.4896 0.4786 -0.1004 0.0852  -0.0172 223 PRO A CD  
1758 N N   . ASP A 224 ? 0.7446 0.5898 0.5868 -0.0904 0.0883  0.0138  224 ASP A N   
1759 C CA  . ASP A 224 ? 0.8589 0.6531 0.6489 -0.0931 0.0933  0.0256  224 ASP A CA  
1760 C C   . ASP A 224 ? 0.8287 0.6206 0.5963 -0.0831 0.0809  0.0313  224 ASP A C   
1761 O O   . ASP A 224 ? 0.9627 0.7098 0.6845 -0.0785 0.0717  0.0445  224 ASP A O   
1762 C CB  . ASP A 224 ? 1.0022 0.7838 0.7770 -0.1158 0.1229  0.0199  224 ASP A CB  
1763 C CG  . ASP A 224 ? 1.0089 0.7859 0.7997 -0.1286 0.1356  0.0141  224 ASP A CG  
1764 O OD1 . ASP A 224 ? 0.9384 0.7012 0.7345 -0.1193 0.1234  0.0188  224 ASP A OD1 
1765 O OD2 . ASP A 224 ? 1.0665 0.8540 0.8667 -0.1487 0.1589  0.0039  224 ASP A OD2 
1766 N N   . ARG A 225 ? 0.7734 0.6100 0.5702 -0.0799 0.0795  0.0219  225 ARG A N   
1767 C CA  . ARG A 225 ? 0.7956 0.6318 0.5738 -0.0716 0.0695  0.0247  225 ARG A CA  
1768 C C   . ARG A 225 ? 0.7454 0.6041 0.5481 -0.0533 0.0430  0.0264  225 ARG A C   
1769 O O   . ARG A 225 ? 0.7281 0.5878 0.5179 -0.0465 0.0327  0.0278  225 ARG A O   
1770 C CB  . ARG A 225 ? 0.7851 0.6509 0.5778 -0.0805 0.0893  0.0127  225 ARG A CB  
1771 C CG  . ARG A 225 ? 0.9674 0.8038 0.7263 -0.0989 0.1179  0.0111  225 ARG A CG  
1772 C CD  . ARG A 225 ? 0.9549 0.8333 0.7551 -0.1094 0.1415  -0.0042 225 ARG A CD  
1773 N NE  . ARG A 225 ? 0.9615 0.8732 0.7852 -0.0989 0.1361  -0.0104 225 ARG A NE  
1774 C CZ  . ARG A 225 ? 1.0940 0.9944 0.8956 -0.1020 0.1509  -0.0139 225 ARG A CZ  
1775 N NH1 . ARG A 225 ? 1.1342 0.9896 0.8855 -0.1163 0.1726  -0.0120 225 ARG A NH1 
1776 N NH2 . ARG A 225 ? 0.9324 0.8632 0.7598 -0.0913 0.1457  -0.0199 225 ARG A NH2 
1777 N N   . ARG A 226 ? 0.5670 0.6544 0.4347 -0.0917 0.0738  -0.0242 226 ARG A N   
1778 C CA  . ARG A 226 ? 0.6049 0.6955 0.4852 -0.0829 0.0559  -0.0272 226 ARG A CA  
1779 C C   . ARG A 226 ? 0.5386 0.6470 0.4396 -0.0770 0.0579  -0.0373 226 ARG A C   
1780 O O   . ARG A 226 ? 0.5435 0.6486 0.4412 -0.0701 0.0477  -0.0420 226 ARG A O   
1781 C CB  . ARG A 226 ? 0.6705 0.7382 0.5200 -0.0787 0.0418  -0.0245 226 ARG A CB  
1782 C CG  . ARG A 226 ? 0.7707 0.8219 0.6101 -0.0807 0.0320  -0.0148 226 ARG A CG  
1783 C CD  . ARG A 226 ? 0.9130 0.9456 0.7211 -0.0885 0.0426  -0.0069 226 ARG A CD  
1784 N NE  . ARG A 226 ? 0.9959 1.0077 0.7894 -0.0888 0.0308  0.0025  226 ARG A NE  
1785 C CZ  . ARG A 226 ? 0.9225 0.9351 0.7316 -0.0932 0.0315  0.0082  226 ARG A CZ  
1786 N NH1 . ARG A 226 ? 0.7832 0.8163 0.6221 -0.0982 0.0422  0.0056  226 ARG A NH1 
1787 N NH2 . ARG A 226 ? 0.8617 0.8531 0.6562 -0.0922 0.0202  0.0163  226 ARG A NH2 
1788 N N   . GLU A 227 ? 0.4887 0.6161 0.4132 -0.0797 0.0706  -0.0410 227 GLU A N   
1789 C CA  . GLU A 227 ? 0.4831 0.6269 0.4286 -0.0737 0.0736  -0.0503 227 GLU A CA  
1790 C C   . GLU A 227 ? 0.3532 0.5160 0.3357 -0.0725 0.0691  -0.0509 227 GLU A C   
1791 O O   . GLU A 227 ? 0.4091 0.5790 0.4049 -0.0787 0.0725  -0.0469 227 GLU A O   
1792 C CB  . GLU A 227 ? 0.4467 0.5964 0.3888 -0.0762 0.0929  -0.0559 227 GLU A CB  
1793 C CG  . GLU A 227 ? 0.6263 0.7552 0.5271 -0.0765 0.0985  -0.0571 227 GLU A CG  
1794 C CD  . GLU A 227 ? 0.6200 0.7549 0.5186 -0.0789 0.1203  -0.0640 227 GLU A CD  
1795 O OE1 . GLU A 227 ? 0.6233 0.7812 0.5579 -0.0790 0.1297  -0.0687 227 GLU A OE1 
1796 O OE2 . GLU A 227 ? 0.8019 0.9179 0.6626 -0.0804 0.1281  -0.0652 227 GLU A OE2 
1797 N N   . ILE A 228 ? 0.3604 0.5294 0.3576 -0.0647 0.0610  -0.0561 228 ILE A N   
1798 C CA  . ILE A 228 ? 0.2963 0.4811 0.3246 -0.0621 0.0565  -0.0576 228 ILE A CA  
1799 C C   . ILE A 228 ? 0.3535 0.5498 0.3970 -0.0558 0.0619  -0.0662 228 ILE A C   
1800 O O   . ILE A 228 ? 0.2698 0.4584 0.3019 -0.0503 0.0604  -0.0710 228 ILE A O   
1801 C CB  . ILE A 228 ? 0.3052 0.4832 0.3362 -0.0587 0.0417  -0.0547 228 ILE A CB  
1802 C CG1 . ILE A 228 ? 0.3528 0.5194 0.3713 -0.0641 0.0371  -0.0471 228 ILE A CG1 
1803 C CG2 . ILE A 228 ? 0.2877 0.4779 0.3445 -0.0558 0.0371  -0.0560 228 ILE A CG2 
1804 C CD1 . ILE A 228 ? 0.2542 0.4127 0.2741 -0.0609 0.0250  -0.0452 228 ILE A CD1 
1805 N N   . ILE A 229 ? 0.2247 0.4390 0.2950 -0.0563 0.0676  -0.0687 229 ILE A N   
1806 C CA  . ILE A 229 ? 0.2328 0.4598 0.3219 -0.0500 0.0743  -0.0773 229 ILE A CA  
1807 C C   . ILE A 229 ? 0.3062 0.5471 0.4268 -0.0458 0.0649  -0.0778 229 ILE A C   
1808 O O   . ILE A 229 ? 0.2876 0.5403 0.4263 -0.0506 0.0649  -0.0755 229 ILE A O   
1809 C CB  . ILE A 229 ? 0.3339 0.5703 0.4266 -0.0548 0.0932  -0.0814 229 ILE A CB  
1810 C CG1 . ILE A 229 ? 0.3008 0.5184 0.3548 -0.0592 0.1018  -0.0800 229 ILE A CG1 
1811 C CG2 . ILE A 229 ? 0.2687 0.5190 0.3848 -0.0472 0.1006  -0.0914 229 ILE A CG2 
1812 C CD1 . ILE A 229 ? 0.3915 0.6140 0.4428 -0.0650 0.1233  -0.0835 229 ILE A CD1 
1813 N N   . SER A 230 ? 0.2583 0.4960 0.3841 -0.0370 0.0563  -0.0807 230 SER A N   
1814 C CA  . SER A 230 ? 0.2976 0.5421 0.4457 -0.0321 0.0448  -0.0797 230 SER A CA  
1815 C C   . SER A 230 ? 0.2603 0.5124 0.4278 -0.0223 0.0460  -0.0874 230 SER A C   
1816 O O   . SER A 230 ? 0.3121 0.5553 0.4685 -0.0176 0.0495  -0.0922 230 SER A O   
1817 C CB  . SER A 230 ? 0.2688 0.4972 0.4023 -0.0312 0.0317  -0.0739 230 SER A CB  
1818 O OG  . SER A 230 ? 0.2626 0.4941 0.4113 -0.0279 0.0209  -0.0717 230 SER A OG  
1819 N N   . PHE A 231 ? 0.1999 0.4674 0.3971 -0.0190 0.0418  -0.0890 231 PHE A N   
1820 C CA  . PHE A 231 ? 0.2109 0.4883 0.4327 -0.0090 0.0433  -0.0968 231 PHE A CA  
1821 C C   . PHE A 231 ? 0.2884 0.5701 0.5315 -0.0028 0.0271  -0.0944 231 PHE A C   
1822 O O   . PHE A 231 ? 0.2512 0.5412 0.5048 -0.0075 0.0202  -0.0905 231 PHE A O   
1823 C CB  . PHE A 231 ? 0.2348 0.5321 0.4780 -0.0111 0.0599  -0.1041 231 PHE A CB  
1824 C CG  . PHE A 231 ? 0.2546 0.5625 0.5250 -0.0003 0.0642  -0.1137 231 PHE A CG  
1825 C CD1 . PHE A 231 ? 0.2342 0.5336 0.4918 0.0042  0.0754  -0.1210 231 PHE A CD1 
1826 C CD2 . PHE A 231 ? 0.1931 0.5188 0.5024 0.0057  0.0562  -0.1162 231 PHE A CD2 
1827 C CE1 . PHE A 231 ? 0.3064 0.6147 0.5899 0.0146  0.0802  -0.1307 231 PHE A CE1 
1828 C CE2 . PHE A 231 ? 0.2410 0.5766 0.5785 0.0167  0.0597  -0.1254 231 PHE A CE2 
1829 C CZ  . PHE A 231 ? 0.2444 0.5712 0.5692 0.0212  0.0727  -0.1328 231 PHE A CZ  
1830 N N   . GLY A 232 ? 0.2729 0.5465 0.5201 0.0076  0.0202  -0.0966 232 GLY A N   
1831 C CA  . GLY A 232 ? 0.3092 0.5865 0.5783 0.0158  0.0053  -0.0956 232 GLY A CA  
1832 C C   . GLY A 232 ? 0.2982 0.5549 0.5471 0.0167  -0.0106 -0.0868 232 GLY A C   
1833 O O   . GLY A 232 ? 0.3352 0.5873 0.5945 0.0253  -0.0235 -0.0856 232 GLY A O   
1834 N N   . SER A 233 ? 0.3084 0.5514 0.5287 0.0083  -0.0099 -0.0807 233 SER A N   
1835 C CA  . SER A 233 ? 0.2714 0.4950 0.4721 0.0075  -0.0221 -0.0727 233 SER A CA  
1836 C C   . SER A 233 ? 0.3495 0.5525 0.5254 0.0067  -0.0183 -0.0709 233 SER A C   
1837 O O   . SER A 233 ? 0.3037 0.5071 0.4704 0.0023  -0.0080 -0.0736 233 SER A O   
1838 C CB  . SER A 233 ? 0.2743 0.4999 0.4667 -0.0021 -0.0255 -0.0673 233 SER A CB  
1839 O OG  . SER A 233 ? 0.3233 0.5276 0.4921 -0.0037 -0.0337 -0.0604 233 SER A OG  
1840 N N   . GLY A 234 ? 0.3348 0.5187 0.4998 0.0106  -0.0272 -0.0662 234 GLY A N   
1841 C CA  . GLY A 234 ? 0.2932 0.4573 0.4382 0.0089  -0.0240 -0.0644 234 GLY A CA  
1842 C C   . GLY A 234 ? 0.3169 0.4663 0.4413 0.0020  -0.0271 -0.0569 234 GLY A C   
1843 O O   . GLY A 234 ? 0.3780 0.5139 0.4888 -0.0014 -0.0228 -0.0558 234 GLY A O   
1844 N N   . TYR A 235 ? 0.3426 0.4945 0.4657 -0.0003 -0.0343 -0.0526 235 TYR A N   
1845 C CA  . TYR A 235 ? 0.3549 0.4916 0.4568 -0.0068 -0.0362 -0.0463 235 TYR A CA  
1846 C C   . TYR A 235 ? 0.3098 0.4493 0.4046 -0.0150 -0.0267 -0.0470 235 TYR A C   
1847 O O   . TYR A 235 ? 0.3970 0.5524 0.5011 -0.0174 -0.0214 -0.0507 235 TYR A O   
1848 C CB  . TYR A 235 ? 0.3281 0.4680 0.4296 -0.0081 -0.0464 -0.0432 235 TYR A CB  
1849 C CG  . TYR A 235 ? 0.3203 0.4458 0.3991 -0.0158 -0.0463 -0.0382 235 TYR A CG  
1850 C CD1 . TYR A 235 ? 0.3651 0.4655 0.4214 -0.0154 -0.0489 -0.0330 235 TYR A CD1 
1851 C CD2 . TYR A 235 ? 0.3715 0.5070 0.4507 -0.0236 -0.0423 -0.0390 235 TYR A CD2 
1852 C CE1 . TYR A 235 ? 0.4196 0.5061 0.4548 -0.0225 -0.0465 -0.0296 235 TYR A CE1 
1853 C CE2 . TYR A 235 ? 0.3894 0.5111 0.4490 -0.0301 -0.0414 -0.0355 235 TYR A CE2 
1854 C CZ  . TYR A 235 ? 0.4292 0.5270 0.4671 -0.0294 -0.0430 -0.0313 235 TYR A CZ  
1855 O OH  . TYR A 235 ? 0.4037 0.4873 0.4218 -0.0359 -0.0399 -0.0289 235 TYR A OH  
1856 N N   . GLY A 236 ? 0.2783 0.4006 0.3561 -0.0192 -0.0244 -0.0433 236 GLY A N   
1857 C CA  . GLY A 236 ? 0.4254 0.5478 0.4993 -0.0250 -0.0164 -0.0444 236 GLY A CA  
1858 C C   . GLY A 236 ? 0.3694 0.5051 0.4456 -0.0304 -0.0145 -0.0448 236 GLY A C   
1859 O O   . GLY A 236 ? 0.3383 0.4813 0.4174 -0.0323 -0.0094 -0.0475 236 GLY A O   
1860 N N   . GLY A 237 ? 0.2534 0.3904 0.3267 -0.0333 -0.0190 -0.0420 237 GLY A N   
1861 C CA  . GLY A 237 ? 0.2565 0.4043 0.3324 -0.0393 -0.0169 -0.0421 237 GLY A CA  
1862 C C   . GLY A 237 ? 0.3152 0.4817 0.4061 -0.0386 -0.0137 -0.0459 237 GLY A C   
1863 O O   . GLY A 237 ? 0.2897 0.4624 0.3803 -0.0439 -0.0088 -0.0460 237 GLY A O   
1864 N N   . ASN A 238 ? 0.3034 0.4777 0.4070 -0.0321 -0.0155 -0.0491 238 ASN A N   
1865 C CA  . ASN A 238 ? 0.2626 0.4546 0.3816 -0.0311 -0.0100 -0.0538 238 ASN A CA  
1866 C C   . ASN A 238 ? 0.3259 0.5165 0.4420 -0.0280 -0.0027 -0.0579 238 ASN A C   
1867 O O   . ASN A 238 ? 0.3061 0.5072 0.4268 -0.0293 0.0050  -0.0616 238 ASN A O   
1868 C CB  . ASN A 238 ? 0.2654 0.4690 0.4048 -0.0252 -0.0159 -0.0565 238 ASN A CB  
1869 C CG  . ASN A 238 ? 0.3217 0.5272 0.4647 -0.0279 -0.0258 -0.0535 238 ASN A CG  
1870 O OD1 . ASN A 238 ? 0.3542 0.5591 0.4902 -0.0358 -0.0249 -0.0511 238 ASN A OD1 
1871 N ND2 . ASN A 238 ? 0.3001 0.5065 0.4537 -0.0211 -0.0364 -0.0539 238 ASN A ND2 
1872 N N   . SER A 239 ? 0.2615 0.4380 0.3691 -0.0245 -0.0047 -0.0578 239 SER A N   
1873 C CA  . SER A 239 ? 0.2494 0.4235 0.3557 -0.0208 -0.0001 -0.0630 239 SER A CA  
1874 C C   . SER A 239 ? 0.2956 0.4587 0.3878 -0.0245 0.0015  -0.0625 239 SER A C   
1875 O O   . SER A 239 ? 0.2805 0.4433 0.3686 -0.0235 0.0050  -0.0672 239 SER A O   
1876 C CB  . SER A 239 ? 0.2283 0.3952 0.3410 -0.0129 -0.0041 -0.0649 239 SER A CB  
1877 O OG  . SER A 239 ? 0.2517 0.4021 0.3550 -0.0138 -0.0089 -0.0600 239 SER A OG  
1878 N N   . LEU A 240 ? 0.2894 0.4432 0.3746 -0.0284 -0.0014 -0.0575 240 LEU A N   
1879 C CA  . LEU A 240 ? 0.3327 0.4783 0.4098 -0.0318 -0.0008 -0.0573 240 LEU A CA  
1880 C C   . LEU A 240 ? 0.2940 0.4454 0.3653 -0.0369 0.0012  -0.0552 240 LEU A C   
1881 O O   . LEU A 240 ? 0.3405 0.4895 0.4091 -0.0411 0.0004  -0.0508 240 LEU A O   
1882 C CB  . LEU A 240 ? 0.4358 0.5688 0.5107 -0.0334 -0.0025 -0.0537 240 LEU A CB  
1883 C CG  . LEU A 240 ? 0.3771 0.5011 0.4543 -0.0293 -0.0041 -0.0534 240 LEU A CG  
1884 C CD1 . LEU A 240 ? 0.3256 0.4348 0.3974 -0.0325 -0.0027 -0.0498 240 LEU A CD1 
1885 C CD2 . LEU A 240 ? 0.3253 0.4478 0.4077 -0.0247 -0.0037 -0.0591 240 LEU A CD2 
1886 N N   . LEU A 241 ? 0.2589 0.4156 0.3262 -0.0367 0.0045  -0.0585 241 LEU A N   
1887 C CA  . LEU A 241 ? 0.2926 0.4540 0.3532 -0.0416 0.0079  -0.0559 241 LEU A CA  
1888 C C   . LEU A 241 ? 0.3227 0.4747 0.3732 -0.0453 0.0049  -0.0523 241 LEU A C   
1889 O O   . LEU A 241 ? 0.3106 0.4631 0.3550 -0.0499 0.0068  -0.0486 241 LEU A O   
1890 C CB  . LEU A 241 ? 0.2184 0.3851 0.2737 -0.0406 0.0142  -0.0604 241 LEU A CB  
1891 C CG  . LEU A 241 ? 0.2631 0.4409 0.3330 -0.0362 0.0181  -0.0649 241 LEU A CG  
1892 C CD1 . LEU A 241 ? 0.2569 0.4401 0.3220 -0.0357 0.0275  -0.0701 241 LEU A CD1 
1893 C CD2 . LEU A 241 ? 0.2332 0.4209 0.3176 -0.0382 0.0171  -0.0615 241 LEU A CD2 
1894 N N   . GLY A 242 ? 0.3071 0.4505 0.3579 -0.0434 0.0002  -0.0536 242 GLY A N   
1895 C CA  . GLY A 242 ? 0.3006 0.4364 0.3473 -0.0459 -0.0036 -0.0508 242 GLY A CA  
1896 C C   . GLY A 242 ? 0.3351 0.4688 0.3864 -0.0491 -0.0030 -0.0462 242 GLY A C   
1897 O O   . GLY A 242 ? 0.3634 0.4919 0.4115 -0.0515 -0.0047 -0.0434 242 GLY A O   
1898 N N   . LYS A 243 ? 0.2461 0.3821 0.3030 -0.0490 -0.0011 -0.0456 243 LYS A N   
1899 C CA  . LYS A 243 ? 0.2307 0.3611 0.2887 -0.0517 -0.0006 -0.0425 243 LYS A CA  
1900 C C   . LYS A 243 ? 0.3469 0.4807 0.4010 -0.0562 0.0003  -0.0393 243 LYS A C   
1901 O O   . LYS A 243 ? 0.3222 0.4525 0.3721 -0.0592 0.0005  -0.0371 243 LYS A O   
1902 C CB  . LYS A 243 ? 0.2955 0.4226 0.3562 -0.0496 -0.0004 -0.0430 243 LYS A CB  
1903 C CG  . LYS A 243 ? 0.2781 0.3950 0.3349 -0.0523 0.0011  -0.0406 243 LYS A CG  
1904 C CD  . LYS A 243 ? 0.3113 0.4200 0.3662 -0.0499 0.0016  -0.0405 243 LYS A CD  
1905 C CE  . LYS A 243 ? 0.2492 0.3453 0.2939 -0.0530 0.0039  -0.0380 243 LYS A CE  
1906 N NZ  . LYS A 243 ? 0.2281 0.3160 0.2747 -0.0558 0.0099  -0.0387 243 LYS A NZ  
1907 N N   . LYS A 244 ? 0.2237 0.3635 0.2802 -0.0568 0.0001  -0.0391 244 LYS A N   
1908 C CA  . LYS A 244 ? 0.2480 0.3916 0.3040 -0.0619 0.0003  -0.0370 244 LYS A CA  
1909 C C   . LYS A 244 ? 0.2629 0.4146 0.3188 -0.0645 0.0039  -0.0367 244 LYS A C   
1910 O O   . LYS A 244 ? 0.2696 0.4184 0.3211 -0.0697 0.0055  -0.0339 244 LYS A O   
1911 C CB  . LYS A 244 ? 0.2080 0.3570 0.2693 -0.0614 -0.0031 -0.0376 244 LYS A CB  
1912 C CG  . LYS A 244 ? 0.1995 0.3366 0.2549 -0.0593 -0.0063 -0.0371 244 LYS A CG  
1913 C CD  . LYS A 244 ? 0.2913 0.4159 0.3371 -0.0637 -0.0051 -0.0353 244 LYS A CD  
1914 C CE  . LYS A 244 ? 0.2793 0.3906 0.3149 -0.0628 -0.0069 -0.0348 244 LYS A CE  
1915 N NZ  . LYS A 244 ? 0.2400 0.3377 0.2652 -0.0671 -0.0038 -0.0343 244 LYS A NZ  
1916 N N   . CYS A 245 ? 0.2611 0.4211 0.3205 -0.0612 0.0063  -0.0396 245 CYS A N   
1917 C CA  . CYS A 245 ? 0.2195 0.3863 0.2769 -0.0641 0.0123  -0.0399 245 CYS A CA  
1918 C C   . CYS A 245 ? 0.3227 0.4786 0.3646 -0.0660 0.0131  -0.0370 245 CYS A C   
1919 O O   . CYS A 245 ? 0.3047 0.4585 0.3400 -0.0716 0.0170  -0.0338 245 CYS A O   
1920 C CB  . CYS A 245 ? 0.2894 0.4656 0.3528 -0.0592 0.0157  -0.0449 245 CYS A CB  
1921 S SG  . CYS A 245 ? 0.2974 0.4869 0.3818 -0.0555 0.0129  -0.0480 245 CYS A SG  
1922 N N   . PHE A 246 ? 0.2690 0.4168 0.3055 -0.0616 0.0088  -0.0382 246 PHE A N   
1923 C CA  . PHE A 246 ? 0.3332 0.4700 0.3559 -0.0620 0.0063  -0.0360 246 PHE A CA  
1924 C C   . PHE A 246 ? 0.2995 0.4270 0.3229 -0.0639 0.0023  -0.0321 246 PHE A C   
1925 O O   . PHE A 246 ? 0.3540 0.4751 0.3692 -0.0680 0.0032  -0.0277 246 PHE A O   
1926 C CB  . PHE A 246 ? 0.3009 0.4342 0.3209 -0.0563 0.0018  -0.0403 246 PHE A CB  
1927 C CG  . PHE A 246 ? 0.4754 0.5970 0.4816 -0.0555 -0.0042 -0.0389 246 PHE A CG  
1928 C CD1 . PHE A 246 ? 0.4658 0.5788 0.4595 -0.0591 -0.0046 -0.0331 246 PHE A CD1 
1929 C CD2 . PHE A 246 ? 0.5054 0.6233 0.5115 -0.0509 -0.0109 -0.0434 246 PHE A CD2 
1930 C CE1 . PHE A 246 ? 0.6154 0.7158 0.5956 -0.0573 -0.0126 -0.0313 246 PHE A CE1 
1931 C CE2 . PHE A 246 ? 0.5554 0.6623 0.5498 -0.0495 -0.0195 -0.0425 246 PHE A CE2 
1932 C CZ  . PHE A 246 ? 0.6143 0.7122 0.5951 -0.0522 -0.0209 -0.0362 246 PHE A CZ  
1933 N N   . ALA A 247 ? 0.2972 0.4226 0.3305 -0.0612 -0.0010 -0.0338 247 ALA A N   
1934 C CA  . ALA A 247 ? 0.3292 0.4451 0.3648 -0.0618 -0.0039 -0.0317 247 ALA A CA  
1935 C C   . ALA A 247 ? 0.3296 0.4431 0.3647 -0.0669 -0.0010 -0.0287 247 ALA A C   
1936 O O   . ALA A 247 ? 0.3468 0.4510 0.3824 -0.0676 -0.0023 -0.0270 247 ALA A O   
1937 C CB  . ALA A 247 ? 0.2747 0.3888 0.3218 -0.0583 -0.0052 -0.0351 247 ALA A CB  
1938 N N   . LEU A 248 ? 0.3155 0.4369 0.3515 -0.0703 0.0024  -0.0287 248 LEU A N   
1939 C CA  . LEU A 248 ? 0.2958 0.4148 0.3314 -0.0761 0.0039  -0.0266 248 LEU A CA  
1940 C C   . LEU A 248 ? 0.3073 0.4312 0.3396 -0.0816 0.0077  -0.0243 248 LEU A C   
1941 O O   . LEU A 248 ? 0.3828 0.4978 0.4086 -0.0859 0.0087  -0.0206 248 LEU A O   
1942 C CB  . LEU A 248 ? 0.2722 0.3946 0.3132 -0.0764 0.0031  -0.0291 248 LEU A CB  
1943 C CG  . LEU A 248 ? 0.2672 0.3787 0.3072 -0.0743 0.0025  -0.0303 248 LEU A CG  
1944 C CD1 . LEU A 248 ? 0.2400 0.3515 0.2789 -0.0745 0.0012  -0.0321 248 LEU A CD1 
1945 C CD2 . LEU A 248 ? 0.2976 0.3975 0.3342 -0.0775 0.0036  -0.0289 248 LEU A CD2 
1946 N N   . ARG A 249 ? 0.2753 0.4124 0.3129 -0.0819 0.0106  -0.0264 249 ARG A N   
1947 C CA  . ARG A 249 ? 0.2795 0.4225 0.3180 -0.0884 0.0167  -0.0249 249 ARG A CA  
1948 C C   . ARG A 249 ? 0.3535 0.4879 0.3764 -0.0897 0.0208  -0.0213 249 ARG A C   
1949 O O   . ARG A 249 ? 0.3814 0.5069 0.3966 -0.0958 0.0237  -0.0169 249 ARG A O   
1950 C CB  . ARG A 249 ? 0.3226 0.4834 0.3752 -0.0875 0.0195  -0.0292 249 ARG A CB  
1951 C CG  . ARG A 249 ? 0.3181 0.4852 0.3836 -0.0867 0.0133  -0.0318 249 ARG A CG  
1952 C CD  . ARG A 249 ? 0.2935 0.4789 0.3775 -0.0875 0.0150  -0.0356 249 ARG A CD  
1953 N NE  . ARG A 249 ? 0.3605 0.5491 0.4532 -0.0842 0.0058  -0.0379 249 ARG A NE  
1954 C CZ  . ARG A 249 ? 0.3504 0.5400 0.4446 -0.0762 0.0017  -0.0398 249 ARG A CZ  
1955 N NH1 . ARG A 249 ? 0.2778 0.4676 0.3687 -0.0710 0.0059  -0.0409 249 ARG A NH1 
1956 N NH2 . ARG A 249 ? 0.3248 0.5128 0.4219 -0.0737 -0.0073 -0.0407 249 ARG A NH2 
1957 N N   . ILE A 250 ? 0.3808 0.5154 0.3965 -0.0843 0.0208  -0.0230 250 ILE A N   
1958 C CA  . ILE A 250 ? 0.3632 0.4864 0.3586 -0.0851 0.0231  -0.0196 250 ILE A CA  
1959 C C   . ILE A 250 ? 0.3594 0.4651 0.3444 -0.0841 0.0156  -0.0148 250 ILE A C   
1960 O O   . ILE A 250 ? 0.3754 0.4680 0.3449 -0.0881 0.0172  -0.0092 250 ILE A O   
1961 C CB  . ILE A 250 ? 0.3548 0.4805 0.3432 -0.0791 0.0230  -0.0239 250 ILE A CB  
1962 C CG1 . ILE A 250 ? 0.3985 0.5404 0.3972 -0.0800 0.0323  -0.0287 250 ILE A CG1 
1963 C CG2 . ILE A 250 ? 0.3832 0.4926 0.3451 -0.0791 0.0221  -0.0203 250 ILE A CG2 
1964 C CD1 . ILE A 250 ? 0.4203 0.5629 0.4118 -0.0876 0.0446  -0.0264 250 ILE A CD1 
1965 N N   . ALA A 251 ? 0.3918 0.4961 0.3861 -0.0788 0.0078  -0.0170 251 ALA A N   
1966 C CA  . ALA A 251 ? 0.3876 0.4772 0.3774 -0.0763 0.0004  -0.0138 251 ALA A CA  
1967 C C   . ALA A 251 ? 0.3673 0.4481 0.3571 -0.0817 0.0020  -0.0095 251 ALA A C   
1968 O O   . ALA A 251 ? 0.3912 0.4567 0.3715 -0.0811 -0.0023 -0.0049 251 ALA A O   
1969 C CB  . ALA A 251 ? 0.3480 0.4402 0.3523 -0.0701 -0.0056 -0.0183 251 ALA A CB  
1970 N N   . SER A 252 ? 0.3162 0.4051 0.3162 -0.0868 0.0070  -0.0111 252 SER A N   
1971 C CA  . SER A 252 ? 0.3734 0.4527 0.3731 -0.0926 0.0084  -0.0080 252 SER A CA  
1972 C C   . SER A 252 ? 0.3738 0.4428 0.3585 -0.0985 0.0125  -0.0018 252 SER A C   
1973 O O   . SER A 252 ? 0.3681 0.4213 0.3468 -0.1010 0.0112  0.0025  252 SER A O   
1974 C CB  . SER A 252 ? 0.3140 0.4038 0.3260 -0.0975 0.0113  -0.0117 252 SER A CB  
1975 O OG  . SER A 252 ? 0.3538 0.4566 0.3692 -0.1024 0.0171  -0.0123 252 SER A OG  
1976 N N   . ARG A 253 ? 0.3875 0.4634 0.3650 -0.1008 0.0187  -0.0013 253 ARG A N   
1977 C CA  . ARG A 253 ? 0.3676 0.4312 0.3269 -0.1071 0.0249  0.0051  253 ARG A CA  
1978 C C   . ARG A 253 ? 0.4960 0.5397 0.4330 -0.1018 0.0178  0.0104  253 ARG A C   
1979 O O   . ARG A 253 ? 0.5255 0.5496 0.4469 -0.1052 0.0177  0.0175  253 ARG A O   
1980 C CB  . ARG A 253 ? 0.4646 0.5415 0.4235 -0.1115 0.0361  0.0031  253 ARG A CB  
1981 C CG  . ARG A 253 ? 0.5783 0.6402 0.5137 -0.1182 0.0452  0.0097  253 ARG A CG  
1982 C CD  . ARG A 253 ? 0.5923 0.6692 0.5359 -0.1260 0.0603  0.0070  253 ARG A CD  
1983 N NE  . ARG A 253 ? 0.7517 0.8125 0.6681 -0.1318 0.0713  0.0130  253 ARG A NE  
1984 C CZ  . ARG A 253 ? 0.7187 0.7866 0.6385 -0.1411 0.0881  0.0124  253 ARG A CZ  
1985 N NH1 . ARG A 253 ? 0.7608 0.8536 0.7138 -0.1453 0.0940  0.0059  253 ARG A NH1 
1986 N NH2 . ARG A 253 ? 0.8740 0.9229 0.7633 -0.1464 0.0991  0.0185  253 ARG A NH2 
1987 N N   . LEU A 254 ? 0.4616 0.5087 0.3966 -0.0934 0.0107  0.0070  254 LEU A N   
1988 C CA  . LEU A 254 ? 0.5447 0.5737 0.4618 -0.0873 0.0001  0.0109  254 LEU A CA  
1989 C C   . LEU A 254 ? 0.5630 0.5798 0.4883 -0.0843 -0.0088 0.0136  254 LEU A C   
1990 O O   . LEU A 254 ? 0.5739 0.5700 0.4826 -0.0827 -0.0154 0.0201  254 LEU A O   
1991 C CB  . LEU A 254 ? 0.5453 0.5826 0.4651 -0.0792 -0.0071 0.0049  254 LEU A CB  
1992 C CG  . LEU A 254 ? 0.5989 0.6471 0.5111 -0.0804 0.0010  0.0008  254 LEU A CG  
1993 C CD1 . LEU A 254 ? 0.6043 0.6585 0.5212 -0.0724 -0.0077 -0.0058 254 LEU A CD1 
1994 C CD2 . LEU A 254 ? 0.6195 0.6522 0.4998 -0.0851 0.0073  0.0064  254 LEU A CD2 
1995 N N   . ALA A 255 ? 0.4491 0.4771 0.3989 -0.0831 -0.0088 0.0084  255 ALA A N   
1996 C CA  . ALA A 255 ? 0.4820 0.4992 0.4418 -0.0804 -0.0145 0.0094  255 ALA A CA  
1997 C C   . ALA A 255 ? 0.5288 0.5293 0.4777 -0.0872 -0.0106 0.0161  255 ALA A C   
1998 O O   . ALA A 255 ? 0.5166 0.4986 0.4609 -0.0840 -0.0176 0.0205  255 ALA A O   
1999 C CB  . ALA A 255 ? 0.4661 0.4968 0.4493 -0.0795 -0.0119 0.0022  255 ALA A CB  
2000 N N   . LYS A 256 ? 0.4707 0.4774 0.4177 -0.0967 0.0001  0.0166  256 LYS A N   
2001 C CA  . LYS A 256 ? 0.5127 0.5031 0.4493 -0.1049 0.0051  0.0230  256 LYS A CA  
2002 C C   . LYS A 256 ? 0.5871 0.5556 0.4958 -0.1046 0.0026  0.0320  256 LYS A C   
2003 O O   . LYS A 256 ? 0.6270 0.5730 0.5255 -0.1059 0.0000  0.0387  256 LYS A O   
2004 C CB  . LYS A 256 ? 0.5028 0.5070 0.4459 -0.1157 0.0171  0.0209  256 LYS A CB  
2005 C CG  . LYS A 256 ? 0.5523 0.5410 0.4817 -0.1262 0.0254  0.0280  256 LYS A CG  
2006 C CD  . LYS A 256 ? 0.4980 0.4684 0.4302 -0.1287 0.0223  0.0304  256 LYS A CD  
2007 C CE  . LYS A 256 ? 0.6967 0.6428 0.6081 -0.1368 0.0280  0.0401  256 LYS A CE  
2008 N NZ  . LYS A 256 ? 0.7964 0.7522 0.7056 -0.1483 0.0422  0.0409  256 LYS A NZ  
2009 N N   . GLU A 257 ? 0.5846 0.5572 0.4785 -0.1024 0.0030  0.0324  257 GLU A N   
2010 C CA  . GLU A 257 ? 0.6708 0.6199 0.5316 -0.1023 0.0006  0.0411  257 GLU A CA  
2011 C C   . GLU A 257 ? 0.6468 0.5789 0.5012 -0.0914 -0.0172 0.0440  257 GLU A C   
2012 O O   . GLU A 257 ? 0.6747 0.5799 0.5041 -0.0910 -0.0226 0.0531  257 GLU A O   
2013 C CB  . GLU A 257 ? 0.7313 0.6888 0.5761 -0.1035 0.0072  0.0393  257 GLU A CB  
2014 C CG  . GLU A 257 ? 0.7528 0.7259 0.6042 -0.1142 0.0255  0.0369  257 GLU A CG  
2015 C CD  . GLU A 257 ? 0.8583 0.8430 0.7001 -0.1136 0.0326  0.0325  257 GLU A CD  
2016 O OE1 . GLU A 257 ? 0.8320 0.8136 0.6623 -0.1049 0.0225  0.0306  257 GLU A OE1 
2017 O OE2 . GLU A 257 ? 0.9696 0.9668 0.8170 -0.1218 0.0484  0.0303  257 GLU A OE2 
2018 N N   . GLU A 258 ? 0.6475 0.5941 0.5250 -0.0825 -0.0266 0.0366  258 GLU A N   
2019 C CA  . GLU A 258 ? 0.6544 0.5895 0.5323 -0.0716 -0.0442 0.0375  258 GLU A CA  
2020 C C   . GLU A 258 ? 0.6366 0.5687 0.5403 -0.0669 -0.0499 0.0358  258 GLU A C   
2021 O O   . GLU A 258 ? 0.7177 0.6403 0.6270 -0.0575 -0.0647 0.0364  258 GLU A O   
2022 C CB  . GLU A 258 ? 0.6067 0.5587 0.4936 -0.0648 -0.0510 0.0298  258 GLU A CB  
2023 C CG  . GLU A 258 ? 0.6180 0.5714 0.4787 -0.0680 -0.0459 0.0301  258 GLU A CG  
2024 C CD  . GLU A 258 ? 0.6597 0.6335 0.5346 -0.0633 -0.0488 0.0206  258 GLU A CD  
2025 O OE1 . GLU A 258 ? 0.7363 0.7194 0.6379 -0.0567 -0.0576 0.0150  258 GLU A OE1 
2026 O OE2 . GLU A 258 ? 0.8096 0.7895 0.6699 -0.0664 -0.0410 0.0184  258 GLU A OE2 
2027 N N   . GLY A 259 ? 0.5885 0.5282 0.5085 -0.0729 -0.0390 0.0329  259 GLY A N   
2028 C CA  . GLY A 259 ? 0.5836 0.5167 0.5238 -0.0694 -0.0421 0.0310  259 GLY A CA  
2029 C C   . GLY A 259 ? 0.5703 0.5220 0.5414 -0.0637 -0.0427 0.0208  259 GLY A C   
2030 O O   . GLY A 259 ? 0.6201 0.5652 0.6088 -0.0578 -0.0473 0.0185  259 GLY A O   
2031 N N   . TRP A 260 ? 0.4733 0.4468 0.4517 -0.0652 -0.0372 0.0147  260 TRP A N   
2032 C CA  . TRP A 260 ? 0.4813 0.4701 0.4860 -0.0616 -0.0350 0.0057  260 TRP A CA  
2033 C C   . TRP A 260 ? 0.4188 0.4205 0.4262 -0.0694 -0.0228 0.0016  260 TRP A C   
2034 O O   . TRP A 260 ? 0.4349 0.4329 0.4302 -0.0775 -0.0167 0.0051  260 TRP A O   
2035 C CB  . TRP A 260 ? 0.4427 0.4433 0.4565 -0.0546 -0.0425 0.0015  260 TRP A CB  
2036 C CG  . TRP A 260 ? 0.4828 0.4901 0.4783 -0.0568 -0.0427 0.0030  260 TRP A CG  
2037 C CD1 . TRP A 260 ? 0.5430 0.5380 0.5122 -0.0575 -0.0477 0.0097  260 TRP A CD1 
2038 C CD2 . TRP A 260 ? 0.4258 0.4516 0.4266 -0.0580 -0.0374 -0.0027 260 TRP A CD2 
2039 N NE1 . TRP A 260 ? 0.5143 0.5200 0.4728 -0.0594 -0.0445 0.0077  260 TRP A NE1 
2040 C CE2 . TRP A 260 ? 0.4903 0.5154 0.4694 -0.0594 -0.0388 0.0000  260 TRP A CE2 
2041 C CE3 . TRP A 260 ? 0.4814 0.5221 0.5012 -0.0582 -0.0311 -0.0096 260 TRP A CE3 
2042 C CZ2 . TRP A 260 ? 0.4431 0.4831 0.4223 -0.0602 -0.0343 -0.0047 260 TRP A CZ2 
2043 C CZ3 . TRP A 260 ? 0.4414 0.4958 0.4601 -0.0590 -0.0278 -0.0131 260 TRP A CZ3 
2044 C CH2 . TRP A 260 ? 0.3935 0.4481 0.3936 -0.0597 -0.0296 -0.0110 260 TRP A CH2 
2045 N N   . LEU A 261 ? 0.4055 0.4214 0.4291 -0.0673 -0.0195 -0.0057 261 LEU A N   
2046 C CA  . LEU A 261 ? 0.3830 0.4086 0.4085 -0.0734 -0.0104 -0.0097 261 LEU A CA  
2047 C C   . LEU A 261 ? 0.4071 0.4492 0.4392 -0.0712 -0.0091 -0.0144 261 LEU A C   
2048 O O   . LEU A 261 ? 0.3703 0.4156 0.4141 -0.0649 -0.0125 -0.0175 261 LEU A O   
2049 C CB  . LEU A 261 ? 0.3878 0.4059 0.4230 -0.0740 -0.0059 -0.0140 261 LEU A CB  
2050 C CG  . LEU A 261 ? 0.4259 0.4259 0.4573 -0.0763 -0.0058 -0.0113 261 LEU A CG  
2051 C CD1 . LEU A 261 ? 0.4804 0.4740 0.5238 -0.0743 -0.0009 -0.0179 261 LEU A CD1 
2052 C CD2 . LEU A 261 ? 0.4147 0.4121 0.4323 -0.0862 -0.0021 -0.0078 261 LEU A CD2 
2053 N N   . ALA A 262 ? 0.3126 0.3649 0.3392 -0.0764 -0.0043 -0.0151 262 ALA A N   
2054 C CA  . ALA A 262 ? 0.3128 0.3789 0.3448 -0.0746 -0.0027 -0.0193 262 ALA A CA  
2055 C C   . ALA A 262 ? 0.3441 0.4132 0.3765 -0.0793 0.0022  -0.0221 262 ALA A C   
2056 O O   . ALA A 262 ? 0.2803 0.3523 0.3073 -0.0852 0.0037  -0.0206 262 ALA A O   
2057 C CB  . ALA A 262 ? 0.2762 0.3517 0.3008 -0.0748 -0.0037 -0.0176 262 ALA A CB  
2058 N N   . GLU A 263 ? 0.3541 0.4216 0.3924 -0.0769 0.0046  -0.0264 263 GLU A N   
2059 C CA  . GLU A 263 ? 0.3129 0.3767 0.3466 -0.0811 0.0080  -0.0290 263 GLU A CA  
2060 C C   . GLU A 263 ? 0.3123 0.3805 0.3463 -0.0789 0.0099  -0.0322 263 GLU A C   
2061 O O   . GLU A 263 ? 0.2841 0.3553 0.3254 -0.0741 0.0106  -0.0333 263 GLU A O   
2062 C CB  . GLU A 263 ? 0.2986 0.3473 0.3327 -0.0816 0.0114  -0.0311 263 GLU A CB  
2063 C CG  . GLU A 263 ? 0.3088 0.3489 0.3420 -0.0834 0.0093  -0.0277 263 GLU A CG  
2064 C CD  . GLU A 263 ? 0.3467 0.3878 0.3714 -0.0911 0.0082  -0.0252 263 GLU A CD  
2065 O OE1 . GLU A 263 ? 0.3089 0.3556 0.3299 -0.0952 0.0085  -0.0276 263 GLU A OE1 
2066 O OE2 . GLU A 263 ? 0.4197 0.4553 0.4419 -0.0933 0.0068  -0.0207 263 GLU A OE2 
2067 N N   . HIS A 264 ? 0.2834 0.3504 0.3089 -0.0826 0.0098  -0.0335 264 HIS A N   
2068 C CA  . HIS A 264 ? 0.3183 0.3851 0.3388 -0.0810 0.0106  -0.0354 264 HIS A CA  
2069 C C   . HIS A 264 ? 0.3190 0.3700 0.3331 -0.0809 0.0174  -0.0386 264 HIS A C   
2070 O O   . HIS A 264 ? 0.3243 0.3647 0.3241 -0.0841 0.0182  -0.0404 264 HIS A O   
2071 C CB  . HIS A 264 ? 0.3183 0.3901 0.3320 -0.0845 0.0050  -0.0352 264 HIS A CB  
2072 C CG  . HIS A 264 ? 0.2940 0.3655 0.3016 -0.0818 0.0029  -0.0359 264 HIS A CG  
2073 N ND1 . HIS A 264 ? 0.3134 0.3825 0.3112 -0.0841 -0.0033 -0.0366 264 HIS A ND1 
2074 C CD2 . HIS A 264 ? 0.2733 0.3449 0.2827 -0.0770 0.0053  -0.0357 264 HIS A CD2 
2075 C CE1 . HIS A 264 ? 0.2840 0.3505 0.2760 -0.0802 -0.0049 -0.0361 264 HIS A CE1 
2076 N NE2 . HIS A 264 ? 0.3252 0.3929 0.3242 -0.0762 0.0011  -0.0355 264 HIS A NE2 
2077 N N   . MET A 265 ? 0.3220 0.3710 0.3473 -0.0772 0.0224  -0.0398 265 MET A N   
2078 C CA  . MET A 265 ? 0.3685 0.4037 0.3933 -0.0771 0.0316  -0.0436 265 MET A CA  
2079 C C   . MET A 265 ? 0.3526 0.3885 0.3884 -0.0735 0.0381  -0.0455 265 MET A C   
2080 O O   . MET A 265 ? 0.3649 0.4121 0.4156 -0.0701 0.0342  -0.0445 265 MET A O   
2081 C CB  . MET A 265 ? 0.3300 0.3604 0.3645 -0.0766 0.0327  -0.0446 265 MET A CB  
2082 C CG  . MET A 265 ? 0.3572 0.3812 0.3805 -0.0814 0.0294  -0.0439 265 MET A CG  
2083 S SD  . MET A 265 ? 0.3639 0.3798 0.3991 -0.0797 0.0301  -0.0442 265 MET A SD  
2084 C CE  . MET A 265 ? 0.3328 0.3409 0.3526 -0.0873 0.0262  -0.0431 265 MET A CE  
2085 N N   . LEU A 266 ? 0.3688 0.3912 0.3965 -0.0750 0.0485  -0.0487 266 LEU A N   
2086 C CA  . LEU A 266 ? 0.3301 0.3509 0.3724 -0.0730 0.0585  -0.0517 266 LEU A CA  
2087 C C   . LEU A 266 ? 0.3643 0.3856 0.4293 -0.0705 0.0630  -0.0556 266 LEU A C   
2088 O O   . LEU A 266 ? 0.3598 0.3764 0.4229 -0.0709 0.0613  -0.0562 266 LEU A O   
2089 C CB  . LEU A 266 ? 0.3059 0.3094 0.3284 -0.0762 0.0703  -0.0535 266 LEU A CB  
2090 C CG  . LEU A 266 ? 0.3834 0.3688 0.3899 -0.0794 0.0797  -0.0574 266 LEU A CG  
2091 C CD1 . LEU A 266 ? 0.3894 0.3696 0.4153 -0.0784 0.0953  -0.0634 266 LEU A CD1 
2092 C CD2 . LEU A 266 ? 0.3875 0.3548 0.3588 -0.0832 0.0826  -0.0565 266 LEU A CD2 
2093 N N   . ILE A 267 ? 0.3411 0.3678 0.4299 -0.0679 0.0684  -0.0585 267 ILE A N   
2094 C CA  . ILE A 267 ? 0.3243 0.3518 0.4401 -0.0648 0.0736  -0.0635 267 ILE A CA  
2095 C C   . ILE A 267 ? 0.3284 0.3507 0.4563 -0.0663 0.0903  -0.0688 267 ILE A C   
2096 O O   . ILE A 267 ? 0.3538 0.3818 0.4890 -0.0668 0.0915  -0.0685 267 ILE A O   
2097 C CB  . ILE A 267 ? 0.3506 0.3932 0.4917 -0.0596 0.0602  -0.0624 267 ILE A CB  
2098 C CG1 . ILE A 267 ? 0.3448 0.3909 0.4702 -0.0592 0.0457  -0.0563 267 ILE A CG1 
2099 C CG2 . ILE A 267 ? 0.3069 0.3498 0.4776 -0.0554 0.0633  -0.0675 267 ILE A CG2 
2100 C CD1 . ILE A 267 ? 0.3045 0.3631 0.4431 -0.0551 0.0323  -0.0541 267 ILE A CD1 
2101 N N   . LEU A 268 ? 0.3532 0.3638 0.4832 -0.0673 0.1045  -0.0741 268 LEU A N   
2102 C CA  . LEU A 268 ? 0.3777 0.3826 0.5214 -0.0693 0.1239  -0.0800 268 LEU A CA  
2103 C C   . LEU A 268 ? 0.3768 0.3843 0.5548 -0.0655 0.1317  -0.0874 268 LEU A C   
2104 O O   . LEU A 268 ? 0.3557 0.3621 0.5363 -0.0621 0.1248  -0.0878 268 LEU A O   
2105 C CB  . LEU A 268 ? 0.3585 0.3412 0.4645 -0.0754 0.1390  -0.0802 268 LEU A CB  
2106 C CG  . LEU A 268 ? 0.4542 0.4189 0.5304 -0.0775 0.1428  -0.0817 268 LEU A CG  
2107 C CD1 . LEU A 268 ? 0.4473 0.4039 0.5408 -0.0766 0.1600  -0.0905 268 LEU A CD1 
2108 C CD2 . LEU A 268 ? 0.4355 0.3804 0.4668 -0.0832 0.1480  -0.0788 268 LEU A CD2 
2109 N N   . GLY A 269 ? 0.3621 0.3730 0.5685 -0.0661 0.1465  -0.0935 269 GLY A N   
2110 C CA  . GLY A 269 ? 0.3725 0.3844 0.6135 -0.0631 0.1592  -0.1023 269 GLY A CA  
2111 C C   . GLY A 269 ? 0.3757 0.3689 0.6019 -0.0691 0.1869  -0.1077 269 GLY A C   
2112 O O   . GLY A 269 ? 0.4395 0.4258 0.6495 -0.0750 0.1974  -0.1059 269 GLY A O   
2113 N N   . ILE A 270 ? 0.3673 0.3500 0.5964 -0.0677 0.1992  -0.1143 270 ILE A N   
2114 C CA  . ILE A 270 ? 0.4302 0.3923 0.6426 -0.0733 0.2276  -0.1207 270 ILE A CA  
2115 C C   . ILE A 270 ? 0.4361 0.4044 0.6972 -0.0693 0.2440  -0.1320 270 ILE A C   
2116 O O   . ILE A 270 ? 0.4453 0.4212 0.7311 -0.0619 0.2337  -0.1349 270 ILE A O   
2117 C CB  . ILE A 270 ? 0.4712 0.4085 0.6296 -0.0765 0.2291  -0.1190 270 ILE A CB  
2118 C CG1 . ILE A 270 ? 0.4948 0.4073 0.6311 -0.0824 0.2592  -0.1263 270 ILE A CG1 
2119 C CG2 . ILE A 270 ? 0.5113 0.4507 0.6764 -0.0706 0.2150  -0.1201 270 ILE A CG2 
2120 C CD1 . ILE A 270 ? 0.5571 0.4422 0.6318 -0.0871 0.2593  -0.1240 270 ILE A CD1 
2121 N N   . THR A 271 ? 0.4577 0.4172 0.7257 -0.0734 0.2606  -0.1353 271 THR A N   
2122 C CA  . THR A 271 ? 0.4406 0.4016 0.7494 -0.0706 0.2703  -0.1437 271 THR A CA  
2123 C C   . THR A 271 ? 0.4946 0.4269 0.7730 -0.0769 0.2946  -0.1478 271 THR A C   
2124 O O   . THR A 271 ? 0.5212 0.4338 0.7577 -0.0844 0.3053  -0.1440 271 THR A O   
2125 C CB  . THR A 271 ? 0.4633 0.4383 0.8107 -0.0705 0.2672  -0.1447 271 THR A CB  
2126 O OG1 . THR A 271 ? 0.4397 0.4397 0.8122 -0.0647 0.2426  -0.1408 271 THR A OG1 
2127 C CG2 . THR A 271 ? 0.4388 0.4160 0.8308 -0.0682 0.2772  -0.1539 271 THR A CG2 
2128 N N   . ASN A 272 ? 0.4673 0.3965 0.7657 -0.0737 0.3025  -0.1551 272 ASN A N   
2129 C CA  . ASN A 272 ? 0.5458 0.4485 0.8178 -0.0793 0.3251  -0.1597 272 ASN A CA  
2130 C C   . ASN A 272 ? 0.6073 0.5098 0.9148 -0.0820 0.3416  -0.1659 272 ASN A C   
2131 O O   . ASN A 272 ? 0.5227 0.4468 0.8800 -0.0782 0.3334  -0.1679 272 ASN A O   
2132 C CB  . ASN A 272 ? 0.6125 0.5101 0.8818 -0.0744 0.3244  -0.1643 272 ASN A CB  
2133 C CG  . ASN A 272 ? 0.5246 0.4403 0.8554 -0.0664 0.3215  -0.1713 272 ASN A CG  
2134 O OD1 . ASN A 272 ? 0.5686 0.5056 0.9469 -0.0629 0.3131  -0.1721 272 ASN A OD1 
2135 N ND2 . ASN A 272 ? 0.5071 0.4131 0.8359 -0.0632 0.3268  -0.1766 272 ASN A ND2 
2136 N N   . PRO A 273 ? 0.6520 0.5288 0.9337 -0.0889 0.3650  -0.1695 273 PRO A N   
2137 C CA  . PRO A 273 ? 0.5780 0.4531 0.8933 -0.0923 0.3832  -0.1763 273 PRO A CA  
2138 C C   . PRO A 273 ? 0.5629 0.4585 0.9424 -0.0855 0.3812  -0.1848 273 PRO A C   
2139 O O   . PRO A 273 ? 0.5928 0.4938 1.0114 -0.0873 0.3917  -0.1907 273 PRO A O   
2140 C CB  . PRO A 273 ? 0.6180 0.4586 0.8851 -0.1006 0.4081  -0.1781 273 PRO A CB  
2141 C CG  . PRO A 273 ? 0.6281 0.4519 0.8310 -0.1031 0.3998  -0.1696 273 PRO A CG  
2142 C CD  . PRO A 273 ? 0.6087 0.4548 0.8248 -0.0949 0.3754  -0.1669 273 PRO A CD  
2143 N N   . GLU A 274 ? 0.5289 0.4351 0.9207 -0.0776 0.3679  -0.1858 274 GLU A N   
2144 C CA  . GLU A 274 ? 0.5590 0.4843 1.0113 -0.0698 0.3628  -0.1931 274 GLU A CA  
2145 C C   . GLU A 274 ? 0.5216 0.4765 1.0204 -0.0622 0.3371  -0.1910 274 GLU A C   
2146 O O   . GLU A 274 ? 0.4704 0.4421 1.0181 -0.0541 0.3265  -0.1957 274 GLU A O   
2147 C CB  . GLU A 274 ? 0.5459 0.4657 0.9889 -0.0639 0.3604  -0.1954 274 GLU A CB  
2148 C CG  . GLU A 274 ? 0.6297 0.5190 1.0238 -0.0708 0.3836  -0.1981 274 GLU A CG  
2149 C CD  . GLU A 274 ? 0.7197 0.6005 1.1369 -0.0751 0.4089  -0.2072 274 GLU A CD  
2150 O OE1 . GLU A 274 ? 0.6927 0.5932 1.1703 -0.0710 0.4072  -0.2128 274 GLU A OE1 
2151 O OE2 . GLU A 274 ? 0.8333 0.6867 1.2076 -0.0826 0.4303  -0.2090 274 GLU A OE2 
2152 N N   . GLY A 275 ? 0.4815 0.4420 0.9648 -0.0642 0.3257  -0.1839 275 GLY A N   
2153 C CA  . GLY A 275 ? 0.4832 0.4695 1.0058 -0.0578 0.3012  -0.1819 275 GLY A CA  
2154 C C   . GLY A 275 ? 0.5133 0.5130 1.0352 -0.0489 0.2757  -0.1765 275 GLY A C   
2155 O O   . GLY A 275 ? 0.5167 0.5372 1.0734 -0.0424 0.2534  -0.1753 275 GLY A O   
2156 N N   . LYS A 276 ? 0.4536 0.4405 0.9358 -0.0486 0.2777  -0.1737 276 LYS A N   
2157 C CA  . LYS A 276 ? 0.4365 0.4330 0.9154 -0.0404 0.2555  -0.1690 276 LYS A CA  
2158 C C   . LYS A 276 ? 0.4673 0.4623 0.9036 -0.0445 0.2487  -0.1606 276 LYS A C   
2159 O O   . LYS A 276 ? 0.4755 0.4524 0.8669 -0.0533 0.2640  -0.1585 276 LYS A O   
2160 C CB  . LYS A 276 ? 0.4959 0.4783 0.9600 -0.0364 0.2606  -0.1722 276 LYS A CB  
2161 C CG  . LYS A 276 ? 0.5336 0.5241 1.0469 -0.0276 0.2560  -0.1785 276 LYS A CG  
2162 C CD  . LYS A 276 ? 0.5054 0.4889 1.0363 -0.0330 0.2795  -0.1865 276 LYS A CD  
2163 C CE  . LYS A 276 ? 0.4527 0.4420 1.0278 -0.0241 0.2765  -0.1933 276 LYS A CE  
2164 N NZ  . LYS A 276 ? 0.4797 0.4607 1.0701 -0.0298 0.3022  -0.2020 276 LYS A NZ  
2165 N N   . LYS A 277 ? 0.4305 0.4439 0.8803 -0.0382 0.2248  -0.1556 277 LYS A N   
2166 C CA  . LYS A 277 ? 0.3595 0.3768 0.7768 -0.0420 0.2161  -0.1475 277 LYS A CA  
2167 C C   . LYS A 277 ? 0.4003 0.4152 0.7947 -0.0371 0.1916  -0.1396 277 LYS A C   
2168 O O   . LYS A 277 ? 0.3692 0.3939 0.7943 -0.0281 0.1738  -0.1396 277 LYS A O   
2169 C CB  . LYS A 277 ? 0.4081 0.4436 0.8486 -0.0426 0.2022  -0.1439 277 LYS A CB  
2170 C CG  . LYS A 277 ? 0.3326 0.3732 0.7415 -0.0468 0.1897  -0.1344 277 LYS A CG  
2171 C CD  . LYS A 277 ? 0.3409 0.3962 0.7718 -0.0475 0.1787  -0.1327 277 LYS A CD  
2172 C CE  . LYS A 277 ? 0.3606 0.4194 0.7591 -0.0516 0.1654  -0.1233 277 LYS A CE  
2173 N NZ  . LYS A 277 ? 0.3053 0.3756 0.7223 -0.0523 0.1561  -0.1227 277 LYS A NZ  
2174 N N   . LYS A 278 ? 0.3510 0.3506 0.6890 -0.0434 0.1888  -0.1321 278 LYS A N   
2175 C CA  . LYS A 278 ? 0.3567 0.3524 0.6669 -0.0413 0.1656  -0.1232 278 LYS A CA  
2176 C C   . LYS A 278 ? 0.3734 0.3718 0.6482 -0.0472 0.1538  -0.1133 278 LYS A C   
2177 O O   . LYS A 278 ? 0.3908 0.3851 0.6475 -0.0539 0.1664  -0.1132 278 LYS A O   
2178 C CB  . LYS A 278 ? 0.4168 0.3896 0.6954 -0.0429 0.1732  -0.1254 278 LYS A CB  
2179 C CG  . LYS A 278 ? 0.4170 0.3846 0.7287 -0.0364 0.1850  -0.1357 278 LYS A CG  
2180 C CD  . LYS A 278 ? 0.4518 0.3948 0.7292 -0.0383 0.1909  -0.1381 278 LYS A CD  
2181 C CE  . LYS A 278 ? 0.4888 0.4258 0.8010 -0.0309 0.2035  -0.1492 278 LYS A CE  
2182 N NZ  . LYS A 278 ? 0.4250 0.3793 0.7865 -0.0199 0.1848  -0.1478 278 LYS A NZ  
2183 N N   . TYR A 279 ? 0.3877 0.3918 0.6527 -0.0446 0.1303  -0.1050 279 TYR A N   
2184 C CA  . TYR A 279 ? 0.3509 0.3583 0.5843 -0.0491 0.1182  -0.0961 279 TYR A CA  
2185 C C   . TYR A 279 ? 0.3599 0.3527 0.5513 -0.0530 0.1135  -0.0913 279 TYR A C   
2186 O O   . TYR A 279 ? 0.3799 0.3650 0.5714 -0.0503 0.1089  -0.0917 279 TYR A O   
2187 C CB  . TYR A 279 ? 0.3330 0.3579 0.5848 -0.0442 0.0962  -0.0906 279 TYR A CB  
2188 C CG  . TYR A 279 ? 0.3902 0.4309 0.6789 -0.0422 0.0976  -0.0948 279 TYR A CG  
2189 C CD1 . TYR A 279 ? 0.3406 0.3896 0.6758 -0.0357 0.0984  -0.1018 279 TYR A CD1 
2190 C CD2 . TYR A 279 ? 0.3126 0.3598 0.5922 -0.0467 0.0975  -0.0922 279 TYR A CD2 
2191 C CE1 . TYR A 279 ? 0.3641 0.4289 0.7371 -0.0346 0.0988  -0.1066 279 TYR A CE1 
2192 C CE2 . TYR A 279 ? 0.3470 0.4079 0.6614 -0.0458 0.0986  -0.0966 279 TYR A CE2 
2193 C CZ  . TYR A 279 ? 0.3462 0.4165 0.7079 -0.0401 0.0991  -0.1040 279 TYR A CZ  
2194 O OH  . TYR A 279 ? 0.3588 0.4439 0.7588 -0.0399 0.0994  -0.1093 279 TYR A OH  
2195 N N   . LEU A 280 ? 0.3602 0.3487 0.5174 -0.0594 0.1139  -0.0870 280 LEU A N   
2196 C CA  . LEU A 280 ? 0.3068 0.2832 0.4260 -0.0640 0.1087  -0.0832 280 LEU A CA  
2197 C C   . LEU A 280 ? 0.3076 0.2937 0.4090 -0.0665 0.0944  -0.0750 280 LEU A C   
2198 O O   . LEU A 280 ? 0.3416 0.3370 0.4483 -0.0666 0.0945  -0.0734 280 LEU A O   
2199 C CB  . LEU A 280 ? 0.3887 0.3447 0.4792 -0.0696 0.1259  -0.0883 280 LEU A CB  
2200 C CG  . LEU A 280 ? 0.4681 0.4116 0.5720 -0.0681 0.1449  -0.0980 280 LEU A CG  
2201 C CD1 . LEU A 280 ? 0.5212 0.4418 0.5881 -0.0746 0.1619  -0.1024 280 LEU A CD1 
2202 C CD2 . LEU A 280 ? 0.3930 0.3323 0.5079 -0.0641 0.1384  -0.1000 280 LEU A CD2 
2203 N N   . ALA A 281 ? 0.3258 0.3095 0.4083 -0.0686 0.0829  -0.0705 281 ALA A N   
2204 C CA  . ALA A 281 ? 0.3474 0.3396 0.4127 -0.0714 0.0710  -0.0637 281 ALA A CA  
2205 C C   . ALA A 281 ? 0.3316 0.3109 0.3640 -0.0776 0.0717  -0.0638 281 ALA A C   
2206 O O   . ALA A 281 ? 0.3793 0.3440 0.4015 -0.0798 0.0762  -0.0676 281 ALA A O   
2207 C CB  . ALA A 281 ? 0.3169 0.3195 0.3907 -0.0691 0.0560  -0.0581 281 ALA A CB  
2208 N N   . ALA A 282 ? 0.3644 0.3485 0.3808 -0.0800 0.0663  -0.0600 282 ALA A N   
2209 C CA  . ALA A 282 ? 0.3876 0.3599 0.3736 -0.0853 0.0645  -0.0602 282 ALA A CA  
2210 C C   . ALA A 282 ? 0.3841 0.3696 0.3645 -0.0865 0.0507  -0.0546 282 ALA A C   
2211 O O   . ALA A 282 ? 0.3873 0.3833 0.3736 -0.0839 0.0485  -0.0516 282 ALA A O   
2212 C CB  . ALA A 282 ? 0.4048 0.3613 0.3720 -0.0869 0.0767  -0.0635 282 ALA A CB  
2213 N N   . ALA A 283 ? 0.3083 0.2932 0.2791 -0.0905 0.0420  -0.0538 283 ALA A N   
2214 C CA  . ALA A 283 ? 0.3537 0.3516 0.3218 -0.0922 0.0299  -0.0497 283 ALA A CA  
2215 C C   . ALA A 283 ? 0.3191 0.3057 0.2620 -0.0960 0.0257  -0.0514 283 ALA A C   
2216 O O   . ALA A 283 ? 0.3408 0.3159 0.2707 -0.1008 0.0236  -0.0548 283 ALA A O   
2217 C CB  . ALA A 283 ? 0.2746 0.2812 0.2532 -0.0948 0.0230  -0.0475 283 ALA A CB  
2218 N N   . PHE A 284 ? 0.4054 0.3936 0.3403 -0.0938 0.0234  -0.0493 284 PHE A N   
2219 C CA  . PHE A 284 ? 0.3927 0.3726 0.3047 -0.0960 0.0147  -0.0494 284 PHE A CA  
2220 C C   . PHE A 284 ? 0.3764 0.3764 0.3010 -0.0939 0.0025  -0.0455 284 PHE A C   
2221 O O   . PHE A 284 ? 0.3137 0.3289 0.2574 -0.0899 0.0044  -0.0427 284 PHE A O   
2222 C CB  . PHE A 284 ? 0.4307 0.3904 0.3184 -0.0948 0.0221  -0.0499 284 PHE A CB  
2223 C CG  . PHE A 284 ? 0.4019 0.3429 0.2807 -0.0962 0.0382  -0.0544 284 PHE A CG  
2224 C CD1 . PHE A 284 ? 0.4057 0.3387 0.2821 -0.0997 0.0407  -0.0593 284 PHE A CD1 
2225 C CD2 . PHE A 284 ? 0.4482 0.3791 0.3224 -0.0942 0.0519  -0.0544 284 PHE A CD2 
2226 C CE1 . PHE A 284 ? 0.4333 0.3491 0.3037 -0.1003 0.0567  -0.0645 284 PHE A CE1 
2227 C CE2 . PHE A 284 ? 0.4908 0.4058 0.3604 -0.0956 0.0689  -0.0595 284 PHE A CE2 
2228 C CZ  . PHE A 284 ? 0.4417 0.3494 0.3096 -0.0981 0.0714  -0.0649 284 PHE A CZ  
2229 N N   . PRO A 285 ? 0.3948 0.3956 0.3106 -0.0964 -0.0103 -0.0459 285 PRO A N   
2230 C CA  . PRO A 285 ? 0.3801 0.4008 0.3112 -0.0936 -0.0211 -0.0431 285 PRO A CA  
2231 C C   . PRO A 285 ? 0.4228 0.4414 0.3494 -0.0873 -0.0199 -0.0399 285 PRO A C   
2232 O O   . PRO A 285 ? 0.3752 0.3759 0.2848 -0.0861 -0.0111 -0.0395 285 PRO A O   
2233 C CB  . PRO A 285 ? 0.3975 0.4154 0.3187 -0.0975 -0.0357 -0.0455 285 PRO A CB  
2234 C CG  . PRO A 285 ? 0.3893 0.3913 0.2969 -0.1039 -0.0321 -0.0498 285 PRO A CG  
2235 C CD  . PRO A 285 ? 0.3985 0.3834 0.2932 -0.1019 -0.0163 -0.0500 285 PRO A CD  
2236 N N   . SER A 286 ? 0.3672 0.4041 0.3106 -0.0836 -0.0278 -0.0378 286 SER A N   
2237 C CA  . SER A 286 ? 0.4198 0.4548 0.3609 -0.0773 -0.0280 -0.0348 286 SER A CA  
2238 C C   . SER A 286 ? 0.4468 0.4575 0.3569 -0.0766 -0.0328 -0.0336 286 SER A C   
2239 O O   . SER A 286 ? 0.4379 0.4418 0.3344 -0.0790 -0.0445 -0.0349 286 SER A O   
2240 C CB  . SER A 286 ? 0.3948 0.4525 0.3589 -0.0733 -0.0369 -0.0340 286 SER A CB  
2241 O OG  . SER A 286 ? 0.3668 0.4441 0.3543 -0.0749 -0.0320 -0.0351 286 SER A OG  
2242 N N   . ALA A 287 ? 0.4606 0.4564 0.3583 -0.0739 -0.0237 -0.0311 287 ALA A N   
2243 C CA  . ALA A 287 ? 0.5374 0.5053 0.4006 -0.0734 -0.0255 -0.0286 287 ALA A CA  
2244 C C   . ALA A 287 ? 0.5615 0.5078 0.3961 -0.0793 -0.0228 -0.0317 287 ALA A C   
2245 O O   . ALA A 287 ? 0.5601 0.4873 0.3651 -0.0800 -0.0332 -0.0310 287 ALA A O   
2246 C CB  . ALA A 287 ? 0.4875 0.4566 0.3465 -0.0684 -0.0439 -0.0257 287 ALA A CB  
2247 N N   . CYS A 288 ? 0.5528 0.5003 0.3951 -0.0834 -0.0094 -0.0354 288 CYS A N   
2248 C CA  . CYS A 288 ? 0.5677 0.4945 0.3847 -0.0889 -0.0047 -0.0396 288 CYS A CA  
2249 C C   . CYS A 288 ? 0.5411 0.4530 0.3520 -0.0907 0.0170  -0.0418 288 CYS A C   
2250 O O   . CYS A 288 ? 0.5190 0.4153 0.3138 -0.0950 0.0241  -0.0466 288 CYS A O   
2251 C CB  . CYS A 288 ? 0.5456 0.4869 0.3785 -0.0928 -0.0119 -0.0438 288 CYS A CB  
2252 S SG  . CYS A 288 ? 0.5664 0.5163 0.3978 -0.0934 -0.0371 -0.0439 288 CYS A SG  
2253 N N   . GLY A 289 ? 0.4908 0.4073 0.3162 -0.0878 0.0280  -0.0393 289 GLY A N   
2254 C CA  . GLY A 289 ? 0.4801 0.3796 0.2978 -0.0898 0.0487  -0.0414 289 GLY A CA  
2255 C C   . GLY A 289 ? 0.5031 0.4195 0.3573 -0.0886 0.0612  -0.0439 289 GLY A C   
2256 O O   . GLY A 289 ? 0.4991 0.4038 0.3529 -0.0905 0.0791  -0.0472 289 GLY A O   
2257 N N   . LYS A 290 ? 0.4079 0.3512 0.2937 -0.0855 0.0521  -0.0429 290 LYS A N   
2258 C CA  . LYS A 290 ? 0.4331 0.3914 0.3518 -0.0840 0.0605  -0.0452 290 LYS A CA  
2259 C C   . LYS A 290 ? 0.4367 0.3914 0.3645 -0.0828 0.0730  -0.0449 290 LYS A C   
2260 O O   . LYS A 290 ? 0.3915 0.3432 0.3330 -0.0838 0.0873  -0.0490 290 LYS A O   
2261 C CB  . LYS A 290 ? 0.4562 0.4402 0.4001 -0.0810 0.0478  -0.0434 290 LYS A CB  
2262 C CG  . LYS A 290 ? 0.3708 0.3599 0.3137 -0.0834 0.0392  -0.0445 290 LYS A CG  
2263 C CD  . LYS A 290 ? 0.3571 0.3693 0.3245 -0.0812 0.0308  -0.0426 290 LYS A CD  
2264 C CE  . LYS A 290 ? 0.3232 0.3477 0.2936 -0.0783 0.0215  -0.0392 290 LYS A CE  
2265 N NZ  . LYS A 290 ? 0.3287 0.3477 0.2802 -0.0800 0.0120  -0.0382 290 LYS A NZ  
2266 N N   . THR A 291 ? 0.4434 0.3981 0.3659 -0.0809 0.0678  -0.0405 291 THR A N   
2267 C CA  . THR A 291 ? 0.4451 0.3965 0.3782 -0.0805 0.0789  -0.0401 291 THR A CA  
2268 C C   . THR A 291 ? 0.4802 0.4055 0.3925 -0.0851 0.0976  -0.0417 291 THR A C   
2269 O O   . THR A 291 ? 0.4620 0.3869 0.3933 -0.0866 0.1130  -0.0449 291 THR A O   
2270 C CB  . THR A 291 ? 0.4398 0.3931 0.3683 -0.0773 0.0689  -0.0350 291 THR A CB  
2271 O OG1 . THR A 291 ? 0.4322 0.4106 0.3838 -0.0733 0.0554  -0.0349 291 THR A OG1 
2272 C CG2 . THR A 291 ? 0.3726 0.3180 0.3087 -0.0782 0.0811  -0.0345 291 THR A CG2 
2273 N N   . ASN A 292 ? 0.4508 0.3532 0.3239 -0.0875 0.0970  -0.0401 292 ASN A N   
2274 C CA  . ASN A 292 ? 0.4659 0.3397 0.3125 -0.0924 0.1163  -0.0416 292 ASN A CA  
2275 C C   . ASN A 292 ? 0.5377 0.4116 0.3980 -0.0949 0.1318  -0.0493 292 ASN A C   
2276 O O   . ASN A 292 ? 0.5313 0.3905 0.3896 -0.0985 0.1534  -0.0525 292 ASN A O   
2277 C CB  . ASN A 292 ? 0.6205 0.4673 0.4169 -0.0941 0.1092  -0.0380 292 ASN A CB  
2278 C CG  . ASN A 292 ? 0.6704 0.5074 0.4487 -0.0917 0.0998  -0.0302 292 ASN A CG  
2279 O OD1 . ASN A 292 ? 0.7351 0.5455 0.4873 -0.0945 0.1122  -0.0270 292 ASN A OD1 
2280 N ND2 . ASN A 292 ? 0.6263 0.4833 0.4187 -0.0866 0.0788  -0.0271 292 ASN A ND2 
2281 N N   . LEU A 293 ? 0.4967 0.3864 0.3721 -0.0931 0.1222  -0.0525 293 LEU A N   
2282 C CA  . LEU A 293 ? 0.5125 0.4022 0.4039 -0.0943 0.1356  -0.0599 293 LEU A CA  
2283 C C   . LEU A 293 ? 0.4800 0.3911 0.4194 -0.0916 0.1424  -0.0628 293 LEU A C   
2284 O O   . LEU A 293 ? 0.5154 0.4217 0.4699 -0.0930 0.1611  -0.0689 293 LEU A O   
2285 C CB  . LEU A 293 ? 0.4233 0.3191 0.3125 -0.0936 0.1225  -0.0619 293 LEU A CB  
2286 C CG  . LEU A 293 ? 0.4551 0.3471 0.3566 -0.0942 0.1347  -0.0696 293 LEU A CG  
2287 C CD1 . LEU A 293 ? 0.4766 0.3386 0.3471 -0.0987 0.1551  -0.0745 293 LEU A CD1 
2288 C CD2 . LEU A 293 ? 0.4165 0.3145 0.3172 -0.0938 0.1201  -0.0705 293 LEU A CD2 
2289 N N   . ALA A 294 ? 0.4631 0.3972 0.4269 -0.0877 0.1276  -0.0593 294 ALA A N   
2290 C CA  . ALA A 294 ? 0.4531 0.4074 0.4611 -0.0848 0.1298  -0.0623 294 ALA A CA  
2291 C C   . ALA A 294 ? 0.4812 0.4310 0.5019 -0.0871 0.1455  -0.0638 294 ALA A C   
2292 O O   . ALA A 294 ? 0.4599 0.4230 0.5191 -0.0858 0.1514  -0.0686 294 ALA A O   
2293 C CB  . ALA A 294 ? 0.3905 0.3673 0.4146 -0.0804 0.1095  -0.0584 294 ALA A CB  
2294 N N   . MET A 295 ? 0.4854 0.4159 0.4756 -0.0906 0.1517  -0.0598 295 MET A N   
2295 C CA  . MET A 295 ? 0.5309 0.4526 0.5290 -0.0943 0.1689  -0.0605 295 MET A CA  
2296 C C   . MET A 295 ? 0.5596 0.4521 0.5288 -0.1003 0.1922  -0.0626 295 MET A C   
2297 O O   . MET A 295 ? 0.5653 0.4436 0.5297 -0.1049 0.2082  -0.0616 295 MET A O   
2298 C CB  . MET A 295 ? 0.5051 0.4241 0.4906 -0.0938 0.1594  -0.0535 295 MET A CB  
2299 C CG  . MET A 295 ? 0.5217 0.4669 0.5337 -0.0885 0.1394  -0.0522 295 MET A CG  
2300 S SD  . MET A 295 ? 0.5685 0.5071 0.5673 -0.0878 0.1321  -0.0455 295 MET A SD  
2301 C CE  . MET A 295 ? 0.4998 0.4696 0.5274 -0.0811 0.1097  -0.0461 295 MET A CE  
2302 N N   . MET A 296 ? 0.5183 0.4001 0.4671 -0.1008 0.1952  -0.0657 296 MET A N   
2303 C CA  . MET A 296 ? 0.5795 0.4289 0.4887 -0.1065 0.2151  -0.0673 296 MET A CA  
2304 C C   . MET A 296 ? 0.5925 0.4352 0.5224 -0.1112 0.2441  -0.0729 296 MET A C   
2305 O O   . MET A 296 ? 0.6392 0.5039 0.6195 -0.1094 0.2501  -0.0795 296 MET A O   
2306 C CB  . MET A 296 ? 0.5894 0.4321 0.4825 -0.1059 0.2136  -0.0722 296 MET A CB  
2307 C CG  . MET A 296 ? 0.6877 0.5030 0.5583 -0.1111 0.2406  -0.0788 296 MET A CG  
2308 S SD  . MET A 296 ? 0.7519 0.5585 0.6040 -0.1101 0.2372  -0.0855 296 MET A SD  
2309 C CE  . MET A 296 ? 0.6873 0.5336 0.6009 -0.1028 0.2209  -0.0882 296 MET A CE  
2310 N N   . ASN A 297 ? 0.5396 0.3510 0.4307 -0.1173 0.2613  -0.0702 297 ASN A N   
2311 C CA  . ASN A 297 ? 0.6449 0.4441 0.5498 -0.1192 0.2814  -0.0758 297 ASN A CA  
2312 C C   . ASN A 297 ? 0.6554 0.4320 0.5323 -0.1206 0.2922  -0.0812 297 ASN A C   
2313 O O   . ASN A 297 ? 0.7112 0.4570 0.5321 -0.1237 0.2924  -0.0768 297 ASN A O   
2314 C CB  . ASN A 297 ? 0.7031 0.4797 0.5841 -0.1231 0.2887  -0.0694 297 ASN A CB  
2315 C CG  . ASN A 297 ? 0.7901 0.5598 0.6955 -0.1255 0.3096  -0.0758 297 ASN A CG  
2316 O OD1 . ASN A 297 ? 0.8587 0.6518 0.8154 -0.1239 0.3109  -0.0799 297 ASN A OD1 
2317 N ND2 . ASN A 297 ? 0.7997 0.5365 0.6682 -0.1296 0.3254  -0.0770 297 ASN A ND2 
2318 N N   . PRO A 298 ? 0.6887 0.4781 0.6015 -0.1184 0.2998  -0.0905 298 PRO A N   
2319 C CA  . PRO A 298 ? 0.7047 0.4731 0.5912 -0.1198 0.3090  -0.0958 298 PRO A CA  
2320 C C   . PRO A 298 ? 0.7027 0.4366 0.5580 -0.1254 0.3286  -0.0964 298 PRO A C   
2321 O O   . PRO A 298 ? 0.7837 0.5162 0.6595 -0.1275 0.3415  -0.0973 298 PRO A O   
2322 C CB  . PRO A 298 ? 0.6886 0.4816 0.6310 -0.1155 0.3130  -0.1054 298 PRO A CB  
2323 C CG  . PRO A 298 ? 0.6633 0.4917 0.6520 -0.1108 0.2983  -0.1035 298 PRO A CG  
2324 C CD  . PRO A 298 ? 0.6680 0.4920 0.6465 -0.1137 0.2971  -0.0962 298 PRO A CD  
2325 N N   . THR A 299 ? 0.7399 0.4451 0.5447 -0.1281 0.3306  -0.0963 299 THR A N   
2326 C CA  . THR A 299 ? 0.8797 0.5493 0.6503 -0.1336 0.3496  -0.0974 299 THR A CA  
2327 C C   . THR A 299 ? 0.8340 0.5015 0.6293 -0.1346 0.3691  -0.1081 299 THR A C   
2328 O O   . THR A 299 ? 0.8911 0.5314 0.6669 -0.1396 0.3888  -0.1105 299 THR A O   
2329 C CB  . THR A 299 ? 0.8473 0.4837 0.5470 -0.1361 0.3402  -0.0916 299 THR A CB  
2330 O OG1 . THR A 299 ? 0.8577 0.4979 0.5488 -0.1339 0.3303  -0.0958 299 THR A OG1 
2331 C CG2 . THR A 299 ? 0.8304 0.4670 0.5054 -0.1348 0.3206  -0.0807 299 THR A CG2 
2332 N N   . LEU A 300 ? 0.7930 0.4873 0.6304 -0.1298 0.3644  -0.1146 300 LEU A N   
2333 C CA  . LEU A 300 ? 0.8082 0.5034 0.6757 -0.1298 0.3818  -0.1248 300 LEU A CA  
2334 C C   . LEU A 300 ? 0.7963 0.5122 0.7246 -0.1288 0.3931  -0.1294 300 LEU A C   
2335 O O   . LEU A 300 ? 0.7751 0.5214 0.7441 -0.1242 0.3799  -0.1279 300 LEU A O   
2336 C CB  . LEU A 300 ? 0.7542 0.4673 0.6404 -0.1244 0.3710  -0.1297 300 LEU A CB  
2337 C CG  . LEU A 300 ? 0.8216 0.5155 0.6534 -0.1252 0.3597  -0.1278 300 LEU A CG  
2338 C CD1 . LEU A 300 ? 0.8035 0.5161 0.6617 -0.1197 0.3513  -0.1340 300 LEU A CD1 
2339 C CD2 . LEU A 300 ? 0.8716 0.5266 0.6545 -0.1313 0.3756  -0.1294 300 LEU A CD2 
2340 N N   . PRO A 301 ? 0.7748 0.4750 0.7111 -0.1331 0.4167  -0.1354 301 PRO A N   
2341 C CA  . PRO A 301 ? 0.7311 0.4507 0.7271 -0.1325 0.4267  -0.1408 301 PRO A CA  
2342 C C   . PRO A 301 ? 0.7358 0.4883 0.7935 -0.1256 0.4199  -0.1481 301 PRO A C   
2343 O O   . PRO A 301 ? 0.7203 0.4725 0.7763 -0.1231 0.4191  -0.1522 301 PRO A O   
2344 C CB  . PRO A 301 ? 0.7856 0.4754 0.7669 -0.1396 0.4552  -0.1460 301 PRO A CB  
2345 C CG  . PRO A 301 ? 0.9092 0.5737 0.8427 -0.1416 0.4596  -0.1470 301 PRO A CG  
2346 C CD  . PRO A 301 ? 0.8352 0.4989 0.7268 -0.1390 0.4352  -0.1382 301 PRO A CD  
2347 N N   . GLY A 302 ? 0.6876 0.4680 0.7998 -0.1221 0.4136  -0.1498 302 GLY A N   
2348 C CA  . GLY A 302 ? 0.6478 0.4599 0.8205 -0.1148 0.4037  -0.1558 302 GLY A CA  
2349 C C   . GLY A 302 ? 0.7046 0.5405 0.8837 -0.1078 0.3770  -0.1509 302 GLY A C   
2350 O O   . GLY A 302 ? 0.6747 0.5374 0.9042 -0.1010 0.3656  -0.1549 302 GLY A O   
2351 N N   . TRP A 303 ? 0.6716 0.4977 0.8014 -0.1093 0.3663  -0.1423 303 TRP A N   
2352 C CA  . TRP A 303 ? 0.6319 0.4783 0.7632 -0.1037 0.3428  -0.1376 303 TRP A CA  
2353 C C   . TRP A 303 ? 0.6237 0.4854 0.7625 -0.1032 0.3292  -0.1307 303 TRP A C   
2354 O O   . TRP A 303 ? 0.6773 0.5243 0.7943 -0.1083 0.3368  -0.1267 303 TRP A O   
2355 C CB  . TRP A 303 ? 0.6120 0.4384 0.6847 -0.1057 0.3386  -0.1336 303 TRP A CB  
2356 C CG  . TRP A 303 ? 0.6716 0.4878 0.7409 -0.1045 0.3468  -0.1407 303 TRP A CG  
2357 C CD1 . TRP A 303 ? 0.6797 0.4700 0.7289 -0.1093 0.3672  -0.1454 303 TRP A CD1 
2358 C CD2 . TRP A 303 ? 0.6447 0.4753 0.7310 -0.0981 0.3353  -0.1441 303 TRP A CD2 
2359 N NE1 . TRP A 303 ? 0.6277 0.4164 0.6810 -0.1062 0.3686  -0.1516 303 TRP A NE1 
2360 C CE2 . TRP A 303 ? 0.6467 0.4592 0.7226 -0.0991 0.3490  -0.1509 303 TRP A CE2 
2361 C CE3 . TRP A 303 ? 0.6093 0.4649 0.7179 -0.0915 0.3150  -0.1423 303 TRP A CE3 
2362 C CZ2 . TRP A 303 ? 0.6275 0.4457 0.7150 -0.0934 0.3425  -0.1559 303 TRP A CZ2 
2363 C CZ3 . TRP A 303 ? 0.5567 0.4167 0.6759 -0.0859 0.3091  -0.1473 303 TRP A CZ3 
2364 C CH2 . TRP A 303 ? 0.5895 0.4305 0.6982 -0.0867 0.3223  -0.1540 303 TRP A CH2 
2365 N N   . LYS A 304 ? 0.5125 0.4027 0.6818 -0.0969 0.3091  -0.1292 304 LYS A N   
2366 C CA  . LYS A 304 ? 0.5359 0.4436 0.7172 -0.0960 0.2944  -0.1232 304 LYS A CA  
2367 C C   . LYS A 304 ? 0.5057 0.4309 0.6824 -0.0920 0.2731  -0.1181 304 LYS A C   
2368 O O   . LYS A 304 ? 0.4928 0.4318 0.6926 -0.0866 0.2654  -0.1218 304 LYS A O   
2369 C CB  . LYS A 304 ? 0.5083 0.4372 0.7490 -0.0925 0.2919  -0.1284 304 LYS A CB  
2370 C CG  . LYS A 304 ? 0.5993 0.5440 0.8515 -0.0919 0.2771  -0.1230 304 LYS A CG  
2371 C CD  . LYS A 304 ? 0.6593 0.6227 0.9678 -0.0886 0.2737  -0.1292 304 LYS A CD  
2372 C CE  . LYS A 304 ? 0.6790 0.6541 0.9944 -0.0890 0.2607  -0.1244 304 LYS A CE  
2373 N NZ  . LYS A 304 ? 0.7772 0.7691 1.1454 -0.0860 0.2561  -0.1311 304 LYS A NZ  
2374 N N   . VAL A 305 ? 0.4718 0.3955 0.6194 -0.0950 0.2640  -0.1096 305 VAL A N   
2375 C CA  . VAL A 305 ? 0.4795 0.4201 0.6230 -0.0929 0.2437  -0.1040 305 VAL A CA  
2376 C C   . VAL A 305 ? 0.4826 0.4448 0.6559 -0.0913 0.2294  -0.1004 305 VAL A C   
2377 O O   . VAL A 305 ? 0.5118 0.4663 0.6796 -0.0946 0.2351  -0.0982 305 VAL A O   
2378 C CB  . VAL A 305 ? 0.5138 0.4323 0.5948 -0.0958 0.2363  -0.0961 305 VAL A CB  
2379 C CG1 . VAL A 305 ? 0.5150 0.4489 0.5907 -0.0914 0.2063  -0.0883 305 VAL A CG1 
2380 C CG2 . VAL A 305 ? 0.5802 0.4788 0.6324 -0.0967 0.2452  -0.1005 305 VAL A CG2 
2381 N N   . GLU A 306 ? 0.4008 0.3851 0.5995 -0.0845 0.2063  -0.0995 306 GLU A N   
2382 C CA  . GLU A 306 ? 0.4494 0.4531 0.6715 -0.0823 0.1894  -0.0966 306 GLU A CA  
2383 C C   . GLU A 306 ? 0.4216 0.4313 0.6207 -0.0781 0.1635  -0.0890 306 GLU A C   
2384 O O   . GLU A 306 ? 0.4433 0.4512 0.6304 -0.0751 0.1557  -0.0881 306 GLU A O   
2385 C CB  . GLU A 306 ? 0.3949 0.4204 0.6761 -0.0779 0.1866  -0.1041 306 GLU A CB  
2386 C CG  . GLU A 306 ? 0.4636 0.4793 0.7620 -0.0788 0.2042  -0.1105 306 GLU A CG  
2387 C CD  . GLU A 306 ? 0.4534 0.4856 0.8041 -0.0720 0.1973  -0.1181 306 GLU A CD  
2388 O OE1 . GLU A 306 ? 0.4102 0.4437 0.7749 -0.0681 0.1994  -0.1225 306 GLU A OE1 
2389 O OE2 . GLU A 306 ? 0.4819 0.5247 0.8595 -0.0706 0.1892  -0.1198 306 GLU A OE2 
2390 N N   . CYS A 307 ? 0.4308 0.4469 0.6248 -0.0784 0.1515  -0.0840 307 CYS A N   
2391 C CA  . CYS A 307 ? 0.3865 0.4062 0.5551 -0.0756 0.1308  -0.0768 307 CYS A CA  
2392 C C   . CYS A 307 ? 0.4021 0.4432 0.5988 -0.0700 0.1114  -0.0771 307 CYS A C   
2393 O O   . CYS A 307 ? 0.3573 0.4086 0.5792 -0.0698 0.1086  -0.0795 307 CYS A O   
2394 C CB  . CYS A 307 ? 0.4118 0.4215 0.5514 -0.0790 0.1308  -0.0710 307 CYS A CB  
2395 S SG  . CYS A 307 ? 0.4358 0.4535 0.5526 -0.0752 0.1069  -0.0637 307 CYS A SG  
2396 N N   . VAL A 308 ? 0.3403 0.3859 0.5304 -0.0661 0.0978  -0.0747 308 VAL A N   
2397 C CA  . VAL A 308 ? 0.3474 0.4085 0.5519 -0.0611 0.0780  -0.0733 308 VAL A CA  
2398 C C   . VAL A 308 ? 0.3360 0.3987 0.5130 -0.0614 0.0662  -0.0669 308 VAL A C   
2399 O O   . VAL A 308 ? 0.3351 0.4078 0.5210 -0.0594 0.0554  -0.0666 308 VAL A O   
2400 C CB  . VAL A 308 ? 0.3139 0.3770 0.5263 -0.0567 0.0705  -0.0737 308 VAL A CB  
2401 C CG1 . VAL A 308 ? 0.2926 0.3676 0.5133 -0.0518 0.0499  -0.0711 308 VAL A CG1 
2402 C CG2 . VAL A 308 ? 0.3233 0.3860 0.5679 -0.0553 0.0824  -0.0811 308 VAL A CG2 
2403 N N   . GLY A 309 ? 0.3123 0.3650 0.4572 -0.0638 0.0680  -0.0625 309 GLY A N   
2404 C CA  . GLY A 309 ? 0.2931 0.3475 0.4146 -0.0640 0.0586  -0.0572 309 GLY A CA  
2405 C C   . GLY A 309 ? 0.3246 0.3654 0.4152 -0.0674 0.0637  -0.0543 309 GLY A C   
2406 O O   . GLY A 309 ? 0.2842 0.3143 0.3685 -0.0694 0.0724  -0.0563 309 GLY A O   
2407 N N   . ASP A 310 ? 0.3345 0.3752 0.4063 -0.0678 0.0574  -0.0502 310 ASP A N   
2408 C CA  . ASP A 310 ? 0.3057 0.3329 0.3481 -0.0706 0.0596  -0.0476 310 ASP A CA  
2409 C C   . ASP A 310 ? 0.3309 0.3645 0.3599 -0.0702 0.0468  -0.0440 310 ASP A C   
2410 O O   . ASP A 310 ? 0.3762 0.3996 0.3826 -0.0725 0.0457  -0.0424 310 ASP A O   
2411 C CB  . ASP A 310 ? 0.3306 0.3463 0.3602 -0.0718 0.0654  -0.0459 310 ASP A CB  
2412 C CG  . ASP A 310 ? 0.3962 0.4210 0.4254 -0.0688 0.0545  -0.0427 310 ASP A CG  
2413 O OD1 . ASP A 310 ? 0.3830 0.4243 0.4293 -0.0659 0.0461  -0.0435 310 ASP A OD1 
2414 O OD2 . ASP A 310 ? 0.3801 0.3936 0.3902 -0.0690 0.0543  -0.0396 310 ASP A OD2 
2415 N N   . ASP A 311 ? 0.3365 0.3858 0.3782 -0.0678 0.0373  -0.0431 311 ASP A N   
2416 C CA  . ASP A 311 ? 0.3107 0.3671 0.3423 -0.0681 0.0276  -0.0402 311 ASP A CA  
2417 C C   . ASP A 311 ? 0.2761 0.3424 0.3156 -0.0682 0.0218  -0.0394 311 ASP A C   
2418 O O   . ASP A 311 ? 0.3518 0.4186 0.3826 -0.0710 0.0180  -0.0379 311 ASP A O   
2419 C CB  . ASP A 311 ? 0.3096 0.3734 0.3413 -0.0653 0.0224  -0.0386 311 ASP A CB  
2420 C CG  . ASP A 311 ? 0.2948 0.3647 0.3174 -0.0658 0.0141  -0.0364 311 ASP A CG  
2421 O OD1 . ASP A 311 ? 0.3286 0.3891 0.3358 -0.0680 0.0129  -0.0356 311 ASP A OD1 
2422 O OD2 . ASP A 311 ? 0.3446 0.4284 0.3757 -0.0640 0.0089  -0.0361 311 ASP A OD2 
2423 N N   . ILE A 312 ? 0.2911 0.3641 0.3461 -0.0654 0.0203  -0.0402 312 ILE A N   
2424 C CA  . ILE A 312 ? 0.2895 0.3689 0.3476 -0.0652 0.0142  -0.0383 312 ILE A CA  
2425 C C   . ILE A 312 ? 0.3107 0.3863 0.3823 -0.0630 0.0148  -0.0400 312 ILE A C   
2426 O O   . ILE A 312 ? 0.3260 0.4025 0.4120 -0.0603 0.0168  -0.0430 312 ILE A O   
2427 C CB  . ILE A 312 ? 0.3310 0.4218 0.3904 -0.0629 0.0081  -0.0372 312 ILE A CB  
2428 C CG1 . ILE A 312 ? 0.3319 0.4277 0.3831 -0.0637 0.0074  -0.0365 312 ILE A CG1 
2429 C CG2 . ILE A 312 ? 0.2306 0.3242 0.2874 -0.0636 0.0034  -0.0345 312 ILE A CG2 
2430 C CD1 . ILE A 312 ? 0.3545 0.4606 0.4085 -0.0607 0.0039  -0.0370 312 ILE A CD1 
2431 N N   . ALA A 313 ? 0.3551 0.4265 0.4242 -0.0643 0.0127  -0.0381 313 ALA A N   
2432 C CA  . ALA A 313 ? 0.3206 0.3876 0.4030 -0.0612 0.0111  -0.0390 313 ALA A CA  
2433 C C   . ALA A 313 ? 0.3281 0.3954 0.4051 -0.0605 0.0024  -0.0344 313 ALA A C   
2434 O O   . ALA A 313 ? 0.3504 0.4165 0.4133 -0.0647 0.0020  -0.0309 313 ALA A O   
2435 C CB  . ALA A 313 ? 0.3062 0.3615 0.3898 -0.0628 0.0187  -0.0415 313 ALA A CB  
2436 N N   . TRP A 314 ? 0.2850 0.3531 0.3729 -0.0556 -0.0047 -0.0345 314 TRP A N   
2437 C CA  . TRP A 314 ? 0.3634 0.4266 0.4433 -0.0543 -0.0136 -0.0296 314 TRP A CA  
2438 C C   . TRP A 314 ? 0.3969 0.4504 0.4903 -0.0504 -0.0166 -0.0301 314 TRP A C   
2439 O O   . TRP A 314 ? 0.3579 0.4142 0.4727 -0.0453 -0.0192 -0.0345 314 TRP A O   
2440 C CB  . TRP A 314 ? 0.3843 0.4533 0.4616 -0.0510 -0.0224 -0.0292 314 TRP A CB  
2441 C CG  . TRP A 314 ? 0.3497 0.4267 0.4126 -0.0542 -0.0198 -0.0284 314 TRP A CG  
2442 C CD1 . TRP A 314 ? 0.3466 0.4277 0.4017 -0.0592 -0.0121 -0.0278 314 TRP A CD1 
2443 C CD2 . TRP A 314 ? 0.3109 0.3926 0.3667 -0.0522 -0.0255 -0.0289 314 TRP A CD2 
2444 N NE1 . TRP A 314 ? 0.3419 0.4311 0.3886 -0.0598 -0.0121 -0.0279 314 TRP A NE1 
2445 C CE2 . TRP A 314 ? 0.3201 0.4092 0.3658 -0.0557 -0.0192 -0.0288 314 TRP A CE2 
2446 C CE3 . TRP A 314 ? 0.4171 0.4968 0.4740 -0.0475 -0.0360 -0.0302 314 TRP A CE3 
2447 C CZ2 . TRP A 314 ? 0.3765 0.4707 0.4134 -0.0546 -0.0210 -0.0302 314 TRP A CZ2 
2448 C CZ3 . TRP A 314 ? 0.4420 0.5254 0.4867 -0.0470 -0.0387 -0.0315 314 TRP A CZ3 
2449 C CH2 . TRP A 314 ? 0.3856 0.4760 0.4204 -0.0505 -0.0302 -0.0316 314 TRP A CH2 
2450 N N   . MET A 315 ? 0.3870 0.4293 0.4704 -0.0527 -0.0163 -0.0261 315 MET A N   
2451 C CA  . MET A 315 ? 0.4263 0.4576 0.5229 -0.0489 -0.0173 -0.0272 315 MET A CA  
2452 C C   . MET A 315 ? 0.4413 0.4599 0.5270 -0.0470 -0.0275 -0.0201 315 MET A C   
2453 O O   . MET A 315 ? 0.4187 0.4336 0.4820 -0.0519 -0.0285 -0.0141 315 MET A O   
2454 C CB  . MET A 315 ? 0.4121 0.4365 0.5067 -0.0535 -0.0058 -0.0301 315 MET A CB  
2455 C CG  . MET A 315 ? 0.4503 0.4827 0.5470 -0.0564 0.0045  -0.0356 315 MET A CG  
2456 S SD  . MET A 315 ? 0.4495 0.4696 0.5417 -0.0606 0.0171  -0.0405 315 MET A SD  
2457 C CE  . MET A 315 ? 0.4403 0.4538 0.5085 -0.0681 0.0140  -0.0350 315 MET A CE  
2458 N N   . LYS A 316 ? 0.4537 0.4647 0.5565 -0.0398 -0.0346 -0.0210 316 LYS A N   
2459 C CA  . LYS A 316 ? 0.5006 0.4960 0.5933 -0.0364 -0.0465 -0.0138 316 LYS A CA  
2460 C C   . LYS A 316 ? 0.4954 0.4820 0.6131 -0.0286 -0.0504 -0.0168 316 LYS A C   
2461 O O   . LYS A 316 ? 0.4770 0.4739 0.6238 -0.0238 -0.0485 -0.0246 316 LYS A O   
2462 C CB  . LYS A 316 ? 0.5793 0.5768 0.6617 -0.0329 -0.0600 -0.0101 316 LYS A CB  
2463 C CG  . LYS A 316 ? 0.6533 0.6366 0.7387 -0.0243 -0.0771 -0.0060 316 LYS A CG  
2464 C CD  . LYS A 316 ? 0.6771 0.6619 0.7497 -0.0211 -0.0913 -0.0038 316 LYS A CD  
2465 C CE  . LYS A 316 ? 0.7719 0.7498 0.8048 -0.0284 -0.0879 0.0036  316 LYS A CE  
2466 N NZ  . LYS A 316 ? 0.8262 0.7807 0.8354 -0.0304 -0.0897 0.0134  316 LYS A NZ  
2467 N N   . PHE A 317 ? 0.5301 0.4973 0.6379 -0.0277 -0.0547 -0.0109 317 PHE A N   
2468 C CA  . PHE A 317 ? 0.5743 0.5311 0.7061 -0.0188 -0.0605 -0.0131 317 PHE A CA  
2469 C C   . PHE A 317 ? 0.5996 0.5560 0.7426 -0.0088 -0.0801 -0.0111 317 PHE A C   
2470 O O   . PHE A 317 ? 0.6268 0.5766 0.7442 -0.0092 -0.0916 -0.0033 317 PHE A O   
2471 C CB  . PHE A 317 ? 0.5711 0.5044 0.6873 -0.0209 -0.0597 -0.0071 317 PHE A CB  
2472 C CG  . PHE A 317 ? 0.6356 0.5671 0.7484 -0.0290 -0.0425 -0.0116 317 PHE A CG  
2473 C CD1 . PHE A 317 ? 0.5723 0.5042 0.7101 -0.0256 -0.0332 -0.0210 317 PHE A CD1 
2474 C CD2 . PHE A 317 ? 0.7074 0.6364 0.7922 -0.0400 -0.0356 -0.0072 317 PHE A CD2 
2475 C CE1 . PHE A 317 ? 0.6102 0.5376 0.7403 -0.0331 -0.0184 -0.0258 317 PHE A CE1 
2476 C CE2 . PHE A 317 ? 0.6714 0.5981 0.7528 -0.0475 -0.0225 -0.0120 317 PHE A CE2 
2477 C CZ  . PHE A 317 ? 0.6281 0.5528 0.7296 -0.0440 -0.0144 -0.0212 317 PHE A CZ  
2478 N N   . ASP A 318 ? 0.5914 0.5544 0.7728 0.0001  -0.0839 -0.0186 318 ASP A N   
2479 C CA  . ASP A 318 ? 0.5614 0.5248 0.7593 0.0104  -0.1050 -0.0180 318 ASP A CA  
2480 C C   . ASP A 318 ? 0.6247 0.5651 0.8237 0.0187  -0.1186 -0.0121 318 ASP A C   
2481 O O   . ASP A 318 ? 0.5860 0.5093 0.7707 0.0156  -0.1108 -0.0080 318 ASP A O   
2482 C CB  . ASP A 318 ? 0.5786 0.5638 0.8226 0.0154  -0.1030 -0.0300 318 ASP A CB  
2483 C CG  . ASP A 318 ? 0.5469 0.5332 0.8252 0.0184  -0.0889 -0.0384 318 ASP A CG  
2484 O OD1 . ASP A 318 ? 0.5842 0.5527 0.8536 0.0188  -0.0847 -0.0353 318 ASP A OD1 
2485 O OD2 . ASP A 318 ? 0.5634 0.5674 0.8776 0.0199  -0.0807 -0.0487 318 ASP A OD2 
2486 N N   . ALA A 319 ? 0.6855 0.6242 0.9021 0.0297  -0.1405 -0.0117 319 ALA A N   
2487 C CA  . ALA A 319 ? 0.6887 0.6040 0.9077 0.0394  -0.1566 -0.0056 319 ALA A CA  
2488 C C   . ALA A 319 ? 0.6556 0.5685 0.9090 0.0438  -0.1449 -0.0126 319 ALA A C   
2489 O O   . ALA A 319 ? 0.7215 0.6102 0.9651 0.0470  -0.1484 -0.0065 319 ALA A O   
2490 C CB  . ALA A 319 ? 0.7233 0.6398 0.9601 0.0513  -0.1843 -0.0057 319 ALA A CB  
2491 N N   . GLN A 320 ? 0.6161 0.5515 0.9081 0.0435  -0.1299 -0.0255 320 GLN A N   
2492 C CA  . GLN A 320 ? 0.6246 0.5584 0.9497 0.0474  -0.1158 -0.0340 320 GLN A CA  
2493 C C   . GLN A 320 ? 0.6456 0.5697 0.9442 0.0365  -0.0929 -0.0338 320 GLN A C   
2494 O O   . GLN A 320 ? 0.5535 0.4718 0.8721 0.0387  -0.0800 -0.0408 320 GLN A O   
2495 C CB  . GLN A 320 ? 0.5907 0.5511 0.9663 0.0505  -0.1064 -0.0483 320 GLN A CB  
2496 C CG  . GLN A 320 ? 0.6287 0.6045 1.0313 0.0583  -0.1279 -0.0503 320 GLN A CG  
2497 C CD  . GLN A 320 ? 0.6826 0.6457 1.1069 0.0730  -0.1538 -0.0473 320 GLN A CD  
2498 O OE1 . GLN A 320 ? 0.7055 0.6541 1.1440 0.0795  -0.1515 -0.0480 320 GLN A OE1 
2499 N NE2 . GLN A 320 ? 0.7943 0.7611 1.2201 0.0787  -0.1796 -0.0441 320 GLN A NE2 
2500 N N   . GLY A 321 ? 0.6179 0.5401 0.8736 0.0249  -0.0878 -0.0267 321 GLY A N   
2501 C CA  . GLY A 321 ? 0.6418 0.5558 0.8731 0.0141  -0.0688 -0.0267 321 GLY A CA  
2502 C C   . GLY A 321 ? 0.5903 0.5227 0.8288 0.0066  -0.0480 -0.0366 321 GLY A C   
2503 O O   . GLY A 321 ? 0.5797 0.5046 0.8024 -0.0012 -0.0327 -0.0388 321 GLY A O   
2504 N N   . ASN A 322 ? 0.5039 0.4581 0.7642 0.0084  -0.0475 -0.0425 322 ASN A N   
2505 C CA  . ASN A 322 ? 0.5446 0.5140 0.8072 0.0010  -0.0283 -0.0504 322 ASN A CA  
2506 C C   . ASN A 322 ? 0.5387 0.5144 0.7657 -0.0087 -0.0283 -0.0441 322 ASN A C   
2507 O O   . ASN A 322 ? 0.5039 0.4840 0.7211 -0.0074 -0.0429 -0.0378 322 ASN A O   
2508 C CB  . ASN A 322 ? 0.5496 0.5385 0.8540 0.0066  -0.0262 -0.0598 322 ASN A CB  
2509 C CG  . ASN A 322 ? 0.5705 0.5565 0.9173 0.0168  -0.0252 -0.0675 322 ASN A CG  
2510 O OD1 . ASN A 322 ? 0.6086 0.5878 0.9632 0.0156  -0.0072 -0.0747 322 ASN A OD1 
2511 N ND2 . ASN A 322 ? 0.6370 0.6277 1.0120 0.0272  -0.0448 -0.0669 322 ASN A ND2 
2512 N N   . LEU A 323 ? 0.4878 0.4632 0.6955 -0.0180 -0.0124 -0.0462 323 LEU A N   
2513 C CA  . LEU A 323 ? 0.4682 0.4526 0.6489 -0.0265 -0.0107 -0.0422 323 LEU A CA  
2514 C C   . LEU A 323 ? 0.4246 0.4281 0.6226 -0.0256 -0.0078 -0.0476 323 LEU A C   
2515 O O   . LEU A 323 ? 0.4341 0.4421 0.6474 -0.0265 0.0064  -0.0556 323 LEU A O   
2516 C CB  . LEU A 323 ? 0.4630 0.4404 0.6200 -0.0359 0.0028  -0.0433 323 LEU A CB  
2517 C CG  . LEU A 323 ? 0.4697 0.4556 0.6003 -0.0443 0.0035  -0.0391 323 LEU A CG  
2518 C CD1 . LEU A 323 ? 0.4308 0.4146 0.5443 -0.0451 -0.0095 -0.0294 323 LEU A CD1 
2519 C CD2 . LEU A 323 ? 0.4282 0.4066 0.5394 -0.0528 0.0145  -0.0413 323 LEU A CD2 
2520 N N   . ARG A 324 ? 0.3931 0.4057 0.5876 -0.0241 -0.0204 -0.0434 324 ARG A N   
2521 C CA  . ARG A 324 ? 0.4568 0.4863 0.6686 -0.0231 -0.0197 -0.0483 324 ARG A CA  
2522 C C   . ARG A 324 ? 0.3731 0.4095 0.5583 -0.0305 -0.0165 -0.0452 324 ARG A C   
2523 O O   . ARG A 324 ? 0.4089 0.4410 0.5672 -0.0335 -0.0230 -0.0381 324 ARG A O   
2524 C CB  . ARG A 324 ? 0.4885 0.5231 0.7203 -0.0149 -0.0382 -0.0479 324 ARG A CB  
2525 C CG  . ARG A 324 ? 0.5120 0.5392 0.7715 -0.0060 -0.0452 -0.0501 324 ARG A CG  
2526 C CD  . ARG A 324 ? 0.5853 0.6220 0.8752 0.0024  -0.0624 -0.0531 324 ARG A CD  
2527 N NE  . ARG A 324 ? 0.5175 0.5719 0.8420 0.0018  -0.0527 -0.0632 324 ARG A NE  
2528 C CZ  . ARG A 324 ? 0.3789 0.4385 0.7441 0.0059  -0.0437 -0.0721 324 ARG A CZ  
2529 N NH1 . ARG A 324 ? 0.3901 0.4390 0.7685 0.0119  -0.0439 -0.0728 324 ARG A NH1 
2530 N NH2 . ARG A 324 ? 0.3570 0.4322 0.7514 0.0037  -0.0330 -0.0807 324 ARG A NH2 
2531 N N   . ALA A 325 ? 0.3511 0.3974 0.5446 -0.0334 -0.0058 -0.0507 325 ALA A N   
2532 C CA  . ALA A 325 ? 0.3742 0.4264 0.5456 -0.0395 -0.0018 -0.0487 325 ALA A CA  
2533 C C   . ALA A 325 ? 0.3485 0.4135 0.5351 -0.0380 -0.0045 -0.0522 325 ALA A C   
2534 O O   . ALA A 325 ? 0.3577 0.4277 0.5740 -0.0351 -0.0012 -0.0585 325 ALA A O   
2535 C CB  . ALA A 325 ? 0.3198 0.3670 0.4791 -0.0456 0.0142  -0.0510 325 ALA A CB  
2536 N N   . ILE A 326 ? 0.3418 0.4119 0.5097 -0.0404 -0.0096 -0.0488 326 ILE A N   
2537 C CA  . ILE A 326 ? 0.3449 0.4252 0.5224 -0.0403 -0.0105 -0.0524 326 ILE A CA  
2538 C C   . ILE A 326 ? 0.3441 0.4257 0.4997 -0.0457 -0.0025 -0.0506 326 ILE A C   
2539 O O   . ILE A 326 ? 0.3612 0.4389 0.4937 -0.0488 -0.0014 -0.0459 326 ILE A O   
2540 C CB  . ILE A 326 ? 0.3623 0.4469 0.5407 -0.0362 -0.0274 -0.0513 326 ILE A CB  
2541 C CG1 . ILE A 326 ? 0.4090 0.4896 0.5543 -0.0381 -0.0331 -0.0444 326 ILE A CG1 
2542 C CG2 . ILE A 326 ? 0.4409 0.5235 0.6422 -0.0297 -0.0387 -0.0530 326 ILE A CG2 
2543 C CD1 . ILE A 326 ? 0.4054 0.4929 0.5386 -0.0399 -0.0342 -0.0451 326 ILE A CD1 
2544 N N   . ASN A 327 ? 0.4077 0.4946 0.5727 -0.0468 0.0028  -0.0545 327 ASN A N   
2545 C CA  . ASN A 327 ? 0.3063 0.3943 0.4529 -0.0503 0.0075  -0.0528 327 ASN A CA  
2546 C C   . ASN A 327 ? 0.3016 0.3968 0.4449 -0.0484 -0.0030 -0.0527 327 ASN A C   
2547 O O   . ASN A 327 ? 0.2963 0.3960 0.4580 -0.0465 -0.0064 -0.0573 327 ASN A O   
2548 C CB  . ASN A 327 ? 0.3199 0.4051 0.4749 -0.0530 0.0205  -0.0565 327 ASN A CB  
2549 C CG  . ASN A 327 ? 0.3038 0.3891 0.4428 -0.0551 0.0226  -0.0549 327 ASN A CG  
2550 O OD1 . ASN A 327 ? 0.2420 0.3290 0.3619 -0.0553 0.0174  -0.0510 327 ASN A OD1 
2551 N ND2 . ASN A 327 ? 0.3478 0.4306 0.4963 -0.0567 0.0308  -0.0579 327 ASN A ND2 
2552 N N   . PRO A 328 ? 0.3252 0.4214 0.4466 -0.0490 -0.0076 -0.0484 328 PRO A N   
2553 C CA  . PRO A 328 ? 0.3162 0.4174 0.4322 -0.0469 -0.0164 -0.0492 328 PRO A CA  
2554 C C   . PRO A 328 ? 0.3264 0.4313 0.4440 -0.0476 -0.0124 -0.0524 328 PRO A C   
2555 O O   . PRO A 328 ? 0.3084 0.4164 0.4245 -0.0456 -0.0190 -0.0549 328 PRO A O   
2556 C CB  . PRO A 328 ? 0.3424 0.4426 0.4350 -0.0483 -0.0185 -0.0439 328 PRO A CB  
2557 C CG  . PRO A 328 ? 0.3126 0.4105 0.3991 -0.0521 -0.0095 -0.0413 328 PRO A CG  
2558 C CD  . PRO A 328 ? 0.2996 0.3924 0.4016 -0.0521 -0.0044 -0.0436 328 PRO A CD  
2559 N N   . GLU A 329 ? 0.3745 0.4766 0.4927 -0.0501 -0.0023 -0.0523 329 GLU A N   
2560 C CA  . GLU A 329 ? 0.3407 0.4428 0.4579 -0.0505 0.0016  -0.0540 329 GLU A CA  
2561 C C   . GLU A 329 ? 0.2859 0.3871 0.4250 -0.0506 0.0041  -0.0592 329 GLU A C   
2562 O O   . GLU A 329 ? 0.2776 0.3784 0.4347 -0.0509 0.0058  -0.0616 329 GLU A O   
2563 C CB  . GLU A 329 ? 0.2643 0.3605 0.3685 -0.0530 0.0100  -0.0507 329 GLU A CB  
2564 C CG  . GLU A 329 ? 0.2798 0.3788 0.3665 -0.0536 0.0074  -0.0466 329 GLU A CG  
2565 C CD  . GLU A 329 ? 0.3033 0.3970 0.3779 -0.0552 0.0118  -0.0442 329 GLU A CD  
2566 O OE1 . GLU A 329 ? 0.3267 0.4107 0.3978 -0.0576 0.0182  -0.0436 329 GLU A OE1 
2567 O OE2 . GLU A 329 ? 0.3300 0.4282 0.3981 -0.0536 0.0087  -0.0433 329 GLU A OE2 
2568 N N   . ASN A 330 ? 0.3049 0.4054 0.4444 -0.0506 0.0049  -0.0614 330 ASN A N   
2569 C CA  . ASN A 330 ? 0.3545 0.4536 0.5151 -0.0518 0.0077  -0.0667 330 ASN A CA  
2570 C C   . ASN A 330 ? 0.3146 0.4035 0.4721 -0.0551 0.0203  -0.0653 330 ASN A C   
2571 O O   . ASN A 330 ? 0.2325 0.3183 0.4073 -0.0575 0.0254  -0.0692 330 ASN A O   
2572 C CB  . ASN A 330 ? 0.2595 0.3630 0.4235 -0.0495 -0.0024 -0.0712 330 ASN A CB  
2573 C CG  . ASN A 330 ? 0.3293 0.4341 0.5212 -0.0510 -0.0039 -0.0782 330 ASN A CG  
2574 O OD1 . ASN A 330 ? 0.3479 0.4546 0.5611 -0.0525 -0.0009 -0.0803 330 ASN A OD1 
2575 N ND2 . ASN A 330 ? 0.3424 0.4465 0.5366 -0.0506 -0.0084 -0.0827 330 ASN A ND2 
2576 N N   . GLY A 331 ? 0.2646 0.3471 0.4000 -0.0555 0.0248  -0.0598 331 GLY A N   
2577 C CA  . GLY A 331 ? 0.2095 0.2784 0.3353 -0.0582 0.0353  -0.0572 331 GLY A CA  
2578 C C   . GLY A 331 ? 0.3051 0.3672 0.4074 -0.0589 0.0380  -0.0517 331 GLY A C   
2579 O O   . GLY A 331 ? 0.3023 0.3708 0.3997 -0.0581 0.0334  -0.0505 331 GLY A O   
2580 N N   . PHE A 332 ? 0.2534 0.3004 0.3398 -0.0605 0.0448  -0.0484 332 PHE A N   
2581 C CA  . PHE A 332 ? 0.3190 0.3562 0.3805 -0.0614 0.0461  -0.0436 332 PHE A CA  
2582 C C   . PHE A 332 ? 0.3106 0.3438 0.3556 -0.0581 0.0388  -0.0397 332 PHE A C   
2583 O O   . PHE A 332 ? 0.3452 0.3703 0.3902 -0.0571 0.0404  -0.0391 332 PHE A O   
2584 C CB  . PHE A 332 ? 0.3492 0.3676 0.4008 -0.0662 0.0605  -0.0427 332 PHE A CB  
2585 C CG  . PHE A 332 ? 0.3754 0.3975 0.4487 -0.0691 0.0699  -0.0477 332 PHE A CG  
2586 C CD1 . PHE A 332 ? 0.3657 0.3978 0.4463 -0.0682 0.0665  -0.0496 332 PHE A CD1 
2587 C CD2 . PHE A 332 ? 0.3868 0.4019 0.4751 -0.0726 0.0825  -0.0506 332 PHE A CD2 
2588 C CE1 . PHE A 332 ? 0.4119 0.4475 0.5155 -0.0696 0.0741  -0.0544 332 PHE A CE1 
2589 C CE2 . PHE A 332 ? 0.4100 0.4305 0.5237 -0.0748 0.0912  -0.0561 332 PHE A CE2 
2590 C CZ  . PHE A 332 ? 0.3791 0.4100 0.5008 -0.0727 0.0863  -0.0581 332 PHE A CZ  
2591 N N   . PHE A 333 ? 0.3545 0.3932 0.3878 -0.0563 0.0307  -0.0373 333 PHE A N   
2592 C CA  . PHE A 333 ? 0.3352 0.3725 0.3563 -0.0525 0.0221  -0.0341 333 PHE A CA  
2593 C C   . PHE A 333 ? 0.2855 0.3084 0.2824 -0.0545 0.0215  -0.0301 333 PHE A C   
2594 O O   . PHE A 333 ? 0.3430 0.3737 0.3354 -0.0542 0.0140  -0.0296 333 PHE A O   
2595 C CB  . PHE A 333 ? 0.3069 0.3653 0.3392 -0.0490 0.0127  -0.0359 333 PHE A CB  
2596 C CG  . PHE A 333 ? 0.3239 0.3848 0.3520 -0.0441 0.0042  -0.0343 333 PHE A CG  
2597 C CD1 . PHE A 333 ? 0.3203 0.3769 0.3524 -0.0398 0.0031  -0.0348 333 PHE A CD1 
2598 C CD2 . PHE A 333 ? 0.3196 0.3879 0.3432 -0.0437 -0.0031 -0.0329 333 PHE A CD2 
2599 C CE1 . PHE A 333 ? 0.3568 0.4160 0.3883 -0.0340 -0.0051 -0.0337 333 PHE A CE1 
2600 C CE2 . PHE A 333 ? 0.3672 0.4402 0.3926 -0.0384 -0.0117 -0.0321 333 PHE A CE2 
2601 C CZ  . PHE A 333 ? 0.3612 0.4296 0.3907 -0.0331 -0.0127 -0.0325 333 PHE A CZ  
2602 N N   . GLY A 334 ? 0.3359 0.3364 0.3160 -0.0570 0.0297  -0.0276 334 GLY A N   
2603 C CA  . GLY A 334 ? 0.3855 0.3680 0.3384 -0.0601 0.0316  -0.0249 334 GLY A CA  
2604 C C   . GLY A 334 ? 0.3505 0.3165 0.2781 -0.0572 0.0226  -0.0196 334 GLY A C   
2605 O O   . GLY A 334 ? 0.4000 0.3608 0.3283 -0.0533 0.0196  -0.0171 334 GLY A O   
2606 N N   . VAL A 335 ? 0.4175 0.3737 0.3221 -0.0589 0.0173  -0.0181 335 VAL A N   
2607 C CA  . VAL A 335 ? 0.4017 0.3391 0.2784 -0.0560 0.0063  -0.0130 335 VAL A CA  
2608 C C   . VAL A 335 ? 0.4657 0.3714 0.3161 -0.0580 0.0172  -0.0085 335 VAL A C   
2609 O O   . VAL A 335 ? 0.4942 0.3854 0.3329 -0.0642 0.0333  -0.0096 335 VAL A O   
2610 C CB  . VAL A 335 ? 0.4701 0.4034 0.3276 -0.0585 -0.0022 -0.0136 335 VAL A CB  
2611 C CG1 . VAL A 335 ? 0.5070 0.4168 0.3315 -0.0556 -0.0152 -0.0084 335 VAL A CG1 
2612 C CG2 . VAL A 335 ? 0.4716 0.4353 0.3562 -0.0572 -0.0126 -0.0175 335 VAL A CG2 
2613 N N   . ALA A 336 ? 0.4636 0.3573 0.3047 -0.0529 0.0093  -0.0034 336 ALA A N   
2614 C CA  . ALA A 336 ? 0.4859 0.3466 0.3004 -0.0550 0.0198  0.0021  336 ALA A CA  
2615 C C   . ALA A 336 ? 0.5647 0.3923 0.3310 -0.0573 0.0173  0.0071  336 ALA A C   
2616 O O   . ALA A 336 ? 0.5892 0.3930 0.3324 -0.0641 0.0350  0.0080  336 ALA A O   
2617 C CB  . ALA A 336 ? 0.5523 0.4100 0.3751 -0.0484 0.0126  0.0059  336 ALA A CB  
2618 N N   . PRO A 337 ? 0.5790 0.4030 0.3287 -0.0521 -0.0039 0.0100  337 PRO A N   
2619 C CA  . PRO A 337 ? 0.6221 0.4100 0.3206 -0.0540 -0.0083 0.0150  337 PRO A CA  
2620 C C   . PRO A 337 ? 0.6800 0.4592 0.3604 -0.0626 0.0059  0.0105  337 PRO A C   
2621 O O   . PRO A 337 ? 0.6275 0.4332 0.3338 -0.0648 0.0074  0.0036  337 PRO A O   
2622 C CB  . PRO A 337 ? 0.5646 0.3620 0.2629 -0.0467 -0.0366 0.0159  337 PRO A CB  
2623 C CG  . PRO A 337 ? 0.5741 0.4018 0.3166 -0.0395 -0.0442 0.0144  337 PRO A CG  
2624 C CD  . PRO A 337 ? 0.5433 0.3948 0.3197 -0.0443 -0.0250 0.0084  337 PRO A CD  
2625 N N   . GLY A 338 ? 0.6648 0.4045 0.2987 -0.0674 0.0173  0.0146  338 GLY A N   
2626 C CA  . GLY A 338 ? 0.6463 0.3727 0.2602 -0.0757 0.0351  0.0100  338 GLY A CA  
2627 C C   . GLY A 338 ? 0.7541 0.4816 0.3865 -0.0819 0.0645  0.0068  338 GLY A C   
2628 O O   . GLY A 338 ? 0.8026 0.5124 0.4144 -0.0888 0.0832  0.0034  338 GLY A O   
2629 N N   . THR A 339 ? 0.6536 0.4012 0.3254 -0.0797 0.0689  0.0069  339 THR A N   
2630 C CA  . THR A 339 ? 0.6916 0.4429 0.3872 -0.0856 0.0945  0.0032  339 THR A CA  
2631 C C   . THR A 339 ? 0.7409 0.4522 0.4012 -0.0905 0.1121  0.0094  339 THR A C   
2632 O O   . THR A 339 ? 0.7639 0.4597 0.4107 -0.0871 0.1040  0.0171  339 THR A O   
2633 C CB  . THR A 339 ? 0.6211 0.4067 0.3692 -0.0816 0.0906  0.0005  339 THR A CB  
2634 O OG1 . THR A 339 ? 0.5277 0.3466 0.3025 -0.0770 0.0737  -0.0040 339 THR A OG1 
2635 C CG2 . THR A 339 ? 0.6578 0.4517 0.4367 -0.0876 0.1140  -0.0051 339 THR A CG2 
2636 N N   . SER A 340 ? 0.7350 0.4285 0.3807 -0.0987 0.1371  0.0062  340 SER A N   
2637 C CA  . SER A 340 ? 0.8353 0.4902 0.4488 -0.1053 0.1589  0.0115  340 SER A CA  
2638 C C   . SER A 340 ? 0.8410 0.4997 0.4773 -0.1139 0.1902  0.0036  340 SER A C   
2639 O O   . SER A 340 ? 0.8087 0.4967 0.4803 -0.1137 0.1926  -0.0054 340 SER A O   
2640 C CB  . SER A 340 ? 0.8669 0.4769 0.4101 -0.1066 0.1550  0.0184  340 SER A CB  
2641 O OG  . SER A 340 ? 0.9204 0.5241 0.4439 -0.1108 0.1636  0.0119  340 SER A OG  
2642 N N   . VAL A 341 ? 0.8665 0.4941 0.4829 -0.1213 0.2145  0.0073  341 VAL A N   
2643 C CA  . VAL A 341 ? 0.8767 0.5084 0.5197 -0.1286 0.2443  -0.0014 341 VAL A CA  
2644 C C   . VAL A 341 ? 0.8769 0.5050 0.5054 -0.1292 0.2500  -0.0094 341 VAL A C   
2645 O O   . VAL A 341 ? 0.9012 0.5477 0.5680 -0.1310 0.2652  -0.0197 341 VAL A O   
2646 C CB  . VAL A 341 ? 0.9699 0.5732 0.6000 -0.1322 0.2605  0.0016  341 VAL A CB  
2647 C CG1 . VAL A 341 ? 0.9674 0.5833 0.6394 -0.1365 0.2852  -0.0098 341 VAL A CG1 
2648 C CG2 . VAL A 341 ? 1.0275 0.6301 0.6673 -0.1313 0.2525  0.0102  341 VAL A CG2 
2649 N N   . LYS A 342 ? 0.9048 0.5090 0.4798 -0.1272 0.2362  -0.0052 342 LYS A N   
2650 C CA  . LYS A 342 ? 0.9120 0.5090 0.4702 -0.1282 0.2408  -0.0128 342 LYS A CA  
2651 C C   . LYS A 342 ? 0.9437 0.5710 0.5220 -0.1254 0.2278  -0.0183 342 LYS A C   
2652 O O   . LYS A 342 ? 0.8659 0.4998 0.4562 -0.1266 0.2371  -0.0276 342 LYS A O   
2653 C CB  . LYS A 342 ? 1.0864 0.6408 0.5774 -0.1280 0.2320  -0.0071 342 LYS A CB  
2654 C CG  . LYS A 342 ? 1.1825 0.7338 0.6409 -0.1225 0.2007  -0.0002 342 LYS A CG  
2655 C CD  . LYS A 342 ? 1.4466 0.9562 0.8426 -0.1220 0.1907  0.0044  342 LYS A CD  
2656 C CE  . LYS A 342 ? 1.5588 1.0700 0.9298 -0.1160 0.1570  0.0081  342 LYS A CE  
2657 N NZ  . LYS A 342 ? 1.4460 0.9826 0.8356 -0.1161 0.1514  -0.0014 342 LYS A NZ  
2658 N N   . THR A 343 ? 0.8660 0.5152 0.4570 -0.1195 0.2022  -0.0140 343 THR A N   
2659 C CA  . THR A 343 ? 0.8206 0.5029 0.4400 -0.1145 0.1834  -0.0200 343 THR A CA  
2660 C C   . THR A 343 ? 0.7962 0.5209 0.4837 -0.1124 0.1863  -0.0260 343 THR A C   
2661 O O   . THR A 343 ? 0.8226 0.5669 0.5351 -0.1118 0.1876  -0.0338 343 THR A O   
2662 C CB  . THR A 343 ? 0.7848 0.4730 0.3906 -0.1075 0.1499  -0.0139 343 THR A CB  
2663 O OG1 . THR A 343 ? 0.7383 0.4421 0.3710 -0.1029 0.1401  -0.0082 343 THR A OG1 
2664 C CG2 . THR A 343 ? 0.9496 0.5953 0.4875 -0.1087 0.1427  -0.0079 343 THR A CG2 
2665 N N   . ASN A 344 ? 0.7517 0.4888 0.4682 -0.1110 0.1862  -0.0226 344 ASN A N   
2666 C CA  . ASN A 344 ? 0.6654 0.4413 0.4436 -0.1085 0.1851  -0.0279 344 ASN A CA  
2667 C C   . ASN A 344 ? 0.6963 0.4698 0.4960 -0.1120 0.2006  -0.0266 344 ASN A C   
2668 O O   . ASN A 344 ? 0.6907 0.4785 0.5114 -0.1083 0.1880  -0.0234 344 ASN A O   
2669 C CB  . ASN A 344 ? 0.6048 0.4088 0.4018 -0.1007 0.1560  -0.0259 344 ASN A CB  
2670 C CG  . ASN A 344 ? 0.5617 0.4033 0.4131 -0.0979 0.1527  -0.0325 344 ASN A CG  
2671 O OD1 . ASN A 344 ? 0.5770 0.4263 0.4588 -0.1010 0.1697  -0.0381 344 ASN A OD1 
2672 N ND2 . ASN A 344 ? 0.5076 0.3721 0.3718 -0.0922 0.1306  -0.0320 344 ASN A ND2 
2673 N N   . PRO A 345 ? 0.6745 0.4295 0.4707 -0.1196 0.2293  -0.0298 345 PRO A N   
2674 C CA  . PRO A 345 ? 0.7165 0.4685 0.5356 -0.1244 0.2457  -0.0290 345 PRO A CA  
2675 C C   . PRO A 345 ? 0.6571 0.4486 0.5409 -0.1215 0.2393  -0.0351 345 PRO A C   
2676 O O   . PRO A 345 ? 0.6296 0.4235 0.5323 -0.1229 0.2400  -0.0330 345 PRO A O   
2677 C CB  . PRO A 345 ? 0.7510 0.4832 0.5631 -0.1291 0.2710  -0.0349 345 PRO A CB  
2678 C CG  . PRO A 345 ? 0.7110 0.4491 0.5192 -0.1275 0.2710  -0.0416 345 PRO A CG  
2679 C CD  . PRO A 345 ? 0.7457 0.4821 0.5194 -0.1246 0.2495  -0.0352 345 PRO A CD  
2680 N N   . ASN A 346 ? 0.6162 0.4366 0.5327 -0.1176 0.2321  -0.0425 346 ASN A N   
2681 C CA  . ASN A 346 ? 0.6030 0.4589 0.5768 -0.1143 0.2231  -0.0480 346 ASN A CA  
2682 C C   . ASN A 346 ? 0.6337 0.5032 0.6096 -0.1078 0.1969  -0.0428 346 ASN A C   
2683 O O   . ASN A 346 ? 0.5529 0.4414 0.5658 -0.1067 0.1916  -0.0454 346 ASN A O   
2684 C CB  . ASN A 346 ? 0.5719 0.4509 0.5740 -0.1110 0.2201  -0.0559 346 ASN A CB  
2685 C CG  . ASN A 346 ? 0.6121 0.4846 0.6295 -0.1159 0.2463  -0.0637 346 ASN A CG  
2686 O OD1 . ASN A 346 ? 0.6035 0.4729 0.6413 -0.1171 0.2571  -0.0669 346 ASN A OD1 
2687 N ND2 . ASN A 346 ? 0.5385 0.4081 0.5449 -0.1146 0.2496  -0.0675 346 ASN A ND2 
2688 N N   . ALA A 347 ? 0.5556 0.4158 0.4934 -0.1036 0.1805  -0.0363 347 ALA A N   
2689 C CA  . ALA A 347 ? 0.5975 0.4683 0.5364 -0.0974 0.1582  -0.0316 347 ALA A CA  
2690 C C   . ALA A 347 ? 0.5679 0.4190 0.4961 -0.0996 0.1633  -0.0262 347 ALA A C   
2691 O O   . ALA A 347 ? 0.5490 0.4137 0.4998 -0.0964 0.1529  -0.0263 347 ALA A O   
2692 C CB  . ALA A 347 ? 0.5167 0.3836 0.4223 -0.0925 0.1397  -0.0269 347 ALA A CB  
2693 N N   . ILE A 348 ? 0.6081 0.4247 0.4997 -0.1054 0.1797  -0.0215 348 ILE A N   
2694 C CA  . ILE A 348 ? 0.5772 0.3698 0.4545 -0.1082 0.1861  -0.0152 348 ILE A CA  
2695 C C   . ILE A 348 ? 0.6383 0.4455 0.5631 -0.1125 0.1976  -0.0210 348 ILE A C   
2696 O O   . ILE A 348 ? 0.6155 0.4221 0.5502 -0.1112 0.1909  -0.0186 348 ILE A O   
2697 C CB  . ILE A 348 ? 0.6975 0.4474 0.5241 -0.1149 0.2048  -0.0092 348 ILE A CB  
2698 C CG1 . ILE A 348 ? 0.7670 0.5004 0.5440 -0.1100 0.1887  -0.0034 348 ILE A CG1 
2699 C CG2 . ILE A 348 ? 0.8169 0.5391 0.6299 -0.1190 0.2145  -0.0024 348 ILE A CG2 
2700 C CD1 . ILE A 348 ? 0.7977 0.5271 0.5587 -0.1020 0.1637  0.0045  348 ILE A CD1 
2701 N N   . LYS A 349 ? 0.5933 0.4139 0.5500 -0.1176 0.2143  -0.0294 349 LYS A N   
2702 C CA  . LYS A 349 ? 0.5994 0.4367 0.6066 -0.1218 0.2233  -0.0364 349 LYS A CA  
2703 C C   . LYS A 349 ? 0.5414 0.4110 0.5837 -0.1146 0.1994  -0.0402 349 LYS A C   
2704 O O   . LYS A 349 ? 0.5952 0.4723 0.6679 -0.1167 0.1995  -0.0435 349 LYS A O   
2705 C CB  . LYS A 349 ? 0.5911 0.4397 0.6288 -0.1260 0.2419  -0.0457 349 LYS A CB  
2706 C CG  . LYS A 349 ? 0.7894 0.6083 0.7959 -0.1292 0.2628  -0.0450 349 LYS A CG  
2707 C CD  . LYS A 349 ? 0.7958 0.6293 0.8370 -0.1280 0.2742  -0.0563 349 LYS A CD  
2708 C CE  . LYS A 349 ? 0.9448 0.7477 0.9580 -0.1322 0.2970  -0.0570 349 LYS A CE  
2709 N NZ  . LYS A 349 ? 1.0445 0.8600 1.0948 -0.1314 0.3093  -0.0686 349 LYS A NZ  
2710 N N   . THR A 350 ? 0.5391 0.4263 0.5762 -0.1066 0.1795  -0.0401 350 THR A N   
2711 C CA  . THR A 350 ? 0.4854 0.4024 0.5534 -0.1001 0.1589  -0.0444 350 THR A CA  
2712 C C   . THR A 350 ? 0.4834 0.3954 0.5378 -0.0954 0.1437  -0.0393 350 THR A C   
2713 O O   . THR A 350 ? 0.4436 0.3711 0.5258 -0.0934 0.1347  -0.0436 350 THR A O   
2714 C CB  . THR A 350 ? 0.5475 0.4836 0.6151 -0.0944 0.1457  -0.0461 350 THR A CB  
2715 O OG1 . THR A 350 ? 0.5424 0.4810 0.6223 -0.0980 0.1600  -0.0510 350 THR A OG1 
2716 C CG2 . THR A 350 ? 0.4493 0.4141 0.5470 -0.0885 0.1267  -0.0506 350 THR A CG2 
2717 N N   . ILE A 351 ? 0.4869 0.3768 0.4992 -0.0931 0.1400  -0.0307 351 ILE A N   
2718 C CA  . ILE A 351 ? 0.4918 0.3807 0.4923 -0.0861 0.1221  -0.0262 351 ILE A CA  
2719 C C   . ILE A 351 ? 0.5358 0.4032 0.5330 -0.0888 0.1285  -0.0230 351 ILE A C   
2720 O O   . ILE A 351 ? 0.5552 0.4155 0.5397 -0.0828 0.1158  -0.0186 351 ILE A O   
2721 C CB  . ILE A 351 ? 0.4566 0.3340 0.4173 -0.0811 0.1112  -0.0191 351 ILE A CB  
2722 C CG1 . ILE A 351 ? 0.5264 0.3672 0.4469 -0.0864 0.1254  -0.0121 351 ILE A CG1 
2723 C CG2 . ILE A 351 ? 0.3961 0.2956 0.3625 -0.0786 0.1033  -0.0227 351 ILE A CG2 
2724 C CD1 . ILE A 351 ? 0.5630 0.3890 0.4420 -0.0816 0.1123  -0.0051 351 ILE A CD1 
2725 N N   . GLN A 352 ? 0.5050 0.3617 0.5157 -0.0977 0.1485  -0.0254 352 GLN A N   
2726 C CA  . GLN A 352 ? 0.5858 0.4178 0.5915 -0.1020 0.1573  -0.0217 352 GLN A CA  
2727 C C   . GLN A 352 ? 0.5361 0.3852 0.5812 -0.1014 0.1505  -0.0288 352 GLN A C   
2728 O O   . GLN A 352 ? 0.5921 0.4216 0.6375 -0.1054 0.1574  -0.0268 352 GLN A O   
2729 C CB  . GLN A 352 ? 0.6304 0.4391 0.6298 -0.1134 0.1848  -0.0206 352 GLN A CB  
2730 C CG  . GLN A 352 ? 0.7418 0.5217 0.6902 -0.1146 0.1929  -0.0121 352 GLN A CG  
2731 C CD  . GLN A 352 ? 0.8755 0.6260 0.8110 -0.1264 0.2225  -0.0101 352 GLN A CD  
2732 O OE1 . GLN A 352 ? 1.0095 0.7639 0.9798 -0.1342 0.2382  -0.0156 352 GLN A OE1 
2733 N NE2 . GLN A 352 ? 0.9694 0.6893 0.8542 -0.1281 0.2307  -0.0026 352 GLN A NE2 
2734 N N   . LYS A 353 ? 0.4877 0.3701 0.5635 -0.0968 0.1369  -0.0369 353 LYS A N   
2735 C CA  . LYS A 353 ? 0.4846 0.3815 0.5929 -0.0958 0.1282  -0.0443 353 LYS A CA  
2736 C C   . LYS A 353 ? 0.4622 0.3889 0.5826 -0.0873 0.1080  -0.0495 353 LYS A C   
2737 O O   . LYS A 353 ? 0.4906 0.4328 0.6106 -0.0852 0.1048  -0.0503 353 LYS A O   
2738 C CB  . LYS A 353 ? 0.5353 0.4383 0.6830 -0.1054 0.1424  -0.0526 353 LYS A CB  
2739 C CG  . LYS A 353 ? 0.5664 0.4903 0.7370 -0.1079 0.1479  -0.0584 353 LYS A CG  
2740 C CD  . LYS A 353 ? 0.7311 0.6598 0.9439 -0.1176 0.1630  -0.0667 353 LYS A CD  
2741 C CE  . LYS A 353 ? 0.7205 0.6703 0.9600 -0.1187 0.1679  -0.0730 353 LYS A CE  
2742 N NZ  . LYS A 353 ? 0.9234 0.8793 1.1947 -0.1200 0.1769  -0.0800 353 LYS A NZ  
2743 N N   . ASN A 354 ? 0.4419 0.3741 0.5711 -0.0825 0.0953  -0.0530 354 ASN A N   
2744 C CA  . ASN A 354 ? 0.4324 0.3902 0.5724 -0.0752 0.0777  -0.0587 354 ASN A CA  
2745 C C   . ASN A 354 ? 0.4216 0.3862 0.5371 -0.0683 0.0692  -0.0531 354 ASN A C   
2746 O O   . ASN A 354 ? 0.4380 0.4241 0.5610 -0.0652 0.0607  -0.0566 354 ASN A O   
2747 C CB  . ASN A 354 ? 0.4840 0.4642 0.6578 -0.0786 0.0764  -0.0680 354 ASN A CB  
2748 C CG  . ASN A 354 ? 0.4722 0.4483 0.6760 -0.0862 0.0839  -0.0748 354 ASN A CG  
2749 O OD1 . ASN A 354 ? 0.4720 0.4385 0.6784 -0.0862 0.0810  -0.0770 354 ASN A OD1 
2750 N ND2 . ASN A 354 ? 0.5065 0.4898 0.7354 -0.0928 0.0940  -0.0789 354 ASN A ND2 
2751 N N   . THR A 355 ? 0.3939 0.3389 0.4795 -0.0660 0.0706  -0.0444 355 THR A N   
2752 C CA  . THR A 355 ? 0.4108 0.3598 0.4737 -0.0610 0.0635  -0.0390 355 THR A CA  
2753 C C   . THR A 355 ? 0.4074 0.3504 0.4544 -0.0526 0.0516  -0.0351 355 THR A C   
2754 O O   . THR A 355 ? 0.3942 0.3156 0.4317 -0.0518 0.0535  -0.0313 355 THR A O   
2755 C CB  . THR A 355 ? 0.4351 0.3654 0.4749 -0.0661 0.0754  -0.0325 355 THR A CB  
2756 O OG1 . THR A 355 ? 0.4190 0.3589 0.4775 -0.0726 0.0863  -0.0374 355 THR A OG1 
2757 C CG2 . THR A 355 ? 0.3711 0.3026 0.3855 -0.0611 0.0661  -0.0272 355 THR A CG2 
2758 N N   . ILE A 356 ? 0.3751 0.3369 0.4210 -0.0464 0.0398  -0.0359 356 ILE A N   
2759 C CA  . ILE A 356 ? 0.3666 0.3273 0.4023 -0.0377 0.0282  -0.0331 356 ILE A CA  
2760 C C   . ILE A 356 ? 0.3685 0.3224 0.3800 -0.0363 0.0243  -0.0258 356 ILE A C   
2761 O O   . ILE A 356 ? 0.4122 0.3797 0.4230 -0.0384 0.0237  -0.0265 356 ILE A O   
2762 C CB  . ILE A 356 ? 0.3777 0.3643 0.4311 -0.0322 0.0189  -0.0402 356 ILE A CB  
2763 C CG1 . ILE A 356 ? 0.4046 0.3947 0.4780 -0.0334 0.0209  -0.0482 356 ILE A CG1 
2764 C CG2 . ILE A 356 ? 0.3142 0.3020 0.3612 -0.0231 0.0083  -0.0380 356 ILE A CG2 
2765 C CD1 . ILE A 356 ? 0.4115 0.4228 0.4969 -0.0282 0.0130  -0.0556 356 ILE A CD1 
2766 N N   . PHE A 357 ? 0.3601 0.2912 0.3508 -0.0326 0.0206  -0.0188 357 PHE A N   
2767 C CA  . PHE A 357 ? 0.3825 0.3049 0.3484 -0.0302 0.0130  -0.0121 357 PHE A CA  
2768 C C   . PHE A 357 ? 0.4154 0.3507 0.3880 -0.0200 -0.0032 -0.0127 357 PHE A C   
2769 O O   . PHE A 357 ? 0.4189 0.3545 0.4040 -0.0140 -0.0071 -0.0149 357 PHE A O   
2770 C CB  . PHE A 357 ? 0.4019 0.2871 0.3361 -0.0324 0.0179  -0.0033 357 PHE A CB  
2771 C CG  . PHE A 357 ? 0.4322 0.3027 0.3577 -0.0430 0.0363  -0.0026 357 PHE A CG  
2772 C CD1 . PHE A 357 ? 0.5237 0.3900 0.4305 -0.0480 0.0413  -0.0008 357 PHE A CD1 
2773 C CD2 . PHE A 357 ? 0.4346 0.2954 0.3723 -0.0481 0.0494  -0.0045 357 PHE A CD2 
2774 C CE1 . PHE A 357 ? 0.4953 0.3484 0.3962 -0.0574 0.0603  -0.0011 357 PHE A CE1 
2775 C CE2 . PHE A 357 ? 0.4996 0.3486 0.4341 -0.0582 0.0679  -0.0047 357 PHE A CE2 
2776 C CZ  . PHE A 357 ? 0.4641 0.3095 0.3804 -0.0625 0.0741  -0.0030 357 PHE A CZ  
2777 N N   . THR A 358 ? 0.3972 0.3433 0.3635 -0.0183 -0.0122 -0.0114 358 THR A N   
2778 C CA  . THR A 358 ? 0.4195 0.3796 0.3955 -0.0093 -0.0273 -0.0123 358 THR A CA  
2779 C C   . THR A 358 ? 0.3691 0.3135 0.3199 -0.0071 -0.0387 -0.0053 358 THR A C   
2780 O O   . THR A 358 ? 0.4060 0.3495 0.3423 -0.0129 -0.0375 -0.0040 358 THR A O   
2781 C CB  . THR A 358 ? 0.4067 0.4010 0.4070 -0.0096 -0.0286 -0.0195 358 THR A CB  
2782 O OG1 . THR A 358 ? 0.4098 0.4153 0.4284 -0.0117 -0.0194 -0.0259 358 THR A OG1 
2783 C CG2 . THR A 358 ? 0.3935 0.4038 0.4088 -0.0006 -0.0416 -0.0215 358 THR A CG2 
2784 N N   . ASN A 359 ? 0.4574 0.3873 0.4018 0.0015  -0.0506 -0.0010 359 ASN A N   
2785 C CA  . ASN A 359 ? 0.4645 0.3824 0.3892 0.0063  -0.0672 0.0048  359 ASN A CA  
2786 C C   . ASN A 359 ? 0.5273 0.4096 0.4086 0.0003  -0.0638 0.0130  359 ASN A C   
2787 O O   . ASN A 359 ? 0.5230 0.3969 0.3830 0.0008  -0.0758 0.0165  359 ASN A O   
2788 C CB  . ASN A 359 ? 0.4167 0.3646 0.3584 0.0067  -0.0768 -0.0001 359 ASN A CB  
2789 C CG  . ASN A 359 ? 0.3945 0.3717 0.3740 0.0151  -0.0840 -0.0066 359 ASN A CG  
2790 O OD1 . ASN A 359 ? 0.3860 0.3582 0.3760 0.0231  -0.0867 -0.0068 359 ASN A OD1 
2791 N ND2 . ASN A 359 ? 0.4340 0.4408 0.4342 0.0131  -0.0862 -0.0123 359 ASN A ND2 
2792 N N   . VAL A 360 ? 0.5353 0.3958 0.4026 -0.0059 -0.0473 0.0157  360 VAL A N   
2793 C CA  . VAL A 360 ? 0.5644 0.3857 0.3878 -0.0110 -0.0419 0.0241  360 VAL A CA  
2794 C C   . VAL A 360 ? 0.6352 0.4247 0.4409 -0.0043 -0.0483 0.0321  360 VAL A C   
2795 O O   . VAL A 360 ? 0.5758 0.3750 0.4064 0.0038  -0.0552 0.0300  360 VAL A O   
2796 C CB  . VAL A 360 ? 0.5112 0.3257 0.3297 -0.0230 -0.0175 0.0223  360 VAL A CB  
2797 C CG1 . VAL A 360 ? 0.4659 0.3101 0.3022 -0.0284 -0.0127 0.0148  360 VAL A CG1 
2798 C CG2 . VAL A 360 ? 0.4895 0.3043 0.3302 -0.0245 -0.0047 0.0199  360 VAL A CG2 
2799 N N   . ALA A 361 ? 0.6838 0.4325 0.4439 -0.0077 -0.0459 0.0413  361 ALA A N   
2800 C CA  . ALA A 361 ? 0.6550 0.3668 0.3911 -0.0019 -0.0519 0.0507  361 ALA A CA  
2801 C C   . ALA A 361 ? 0.6659 0.3610 0.4048 -0.0089 -0.0297 0.0517  361 ALA A C   
2802 O O   . ALA A 361 ? 0.6692 0.3696 0.4130 -0.0200 -0.0086 0.0476  361 ALA A O   
2803 C CB  . ALA A 361 ? 0.7180 0.3889 0.3977 -0.0025 -0.0604 0.0611  361 ALA A CB  
2804 N N   . GLU A 362 ? 0.6580 0.3332 0.3965 -0.0021 -0.0349 0.0565  362 GLU A N   
2805 C CA  . GLU A 362 ? 0.7656 0.4211 0.5067 -0.0084 -0.0158 0.0578  362 GLU A CA  
2806 C C   . GLU A 362 ? 0.8195 0.4196 0.5092 -0.0101 -0.0132 0.0715  362 GLU A C   
2807 O O   . GLU A 362 ? 0.8926 0.4706 0.5571 0.0000  -0.0336 0.0797  362 GLU A O   
2808 C CB  . GLU A 362 ? 0.7135 0.3863 0.4947 -0.0002 -0.0215 0.0519  362 GLU A CB  
2809 C CG  . GLU A 362 ? 0.7330 0.3854 0.5197 -0.0070 -0.0033 0.0523  362 GLU A CG  
2810 C CD  . GLU A 362 ? 0.8220 0.4904 0.6467 0.0011  -0.0094 0.0452  362 GLU A CD  
2811 O OE1 . GLU A 362 ? 0.8239 0.5181 0.6697 0.0126  -0.0269 0.0403  362 GLU A OE1 
2812 O OE2 . GLU A 362 ? 0.8442 0.4989 0.6783 -0.0043 0.0039  0.0437  362 GLU A OE2 
2813 N N   . THR A 363 ? 0.7910 0.3679 0.4651 -0.0229 0.0119  0.0740  363 THR A N   
2814 C CA  . THR A 363 ? 0.9012 0.4222 0.5261 -0.0263 0.0190  0.0872  363 THR A CA  
2815 C C   . THR A 363 ? 0.8897 0.3950 0.5310 -0.0245 0.0233  0.0890  363 THR A C   
2816 O O   . THR A 363 ? 0.8370 0.3729 0.5262 -0.0254 0.0291  0.0787  363 THR A O   
2817 C CB  . THR A 363 ? 0.8931 0.3936 0.4901 -0.0421 0.0465  0.0891  363 THR A CB  
2818 O OG1 . THR A 363 ? 0.8745 0.3993 0.5144 -0.0521 0.0691  0.0792  363 THR A OG1 
2819 C CG2 . THR A 363 ? 0.9543 0.4677 0.5334 -0.0437 0.0422  0.0866  363 THR A CG2 
2820 N N   . SER A 364 ? 0.9762 0.4304 0.5744 -0.0219 0.0197  0.1025  364 SER A N   
2821 C CA  . SER A 364 ? 1.0139 0.4473 0.6232 -0.0186 0.0207  0.1056  364 SER A CA  
2822 C C   . SER A 364 ? 0.9761 0.4094 0.6086 -0.0334 0.0502  0.1002  364 SER A C   
2823 O O   . SER A 364 ? 0.9602 0.3947 0.6220 -0.0313 0.0512  0.0966  364 SER A O   
2824 C CB  . SER A 364 ? 0.9788 0.3519 0.5310 -0.0138 0.0116  0.1228  364 SER A CB  
2825 O OG  . SER A 364 ? 1.1001 0.4345 0.6004 -0.0267 0.0308  0.1318  364 SER A OG  
2826 N N   . ASP A 365 ? 0.9575 0.3897 0.5799 -0.0481 0.0740  0.0987  365 ASP A N   
2827 C CA  . ASP A 365 ? 1.0020 0.4387 0.6530 -0.0625 0.1017  0.0921  365 ASP A CA  
2828 C C   . ASP A 365 ? 0.8779 0.3731 0.5885 -0.0641 0.1033  0.0752  365 ASP A C   
2829 O O   . ASP A 365 ? 0.8949 0.4006 0.6325 -0.0765 0.1251  0.0679  365 ASP A O   
2830 C CB  . ASP A 365 ? 1.0043 0.4090 0.6177 -0.0780 0.1292  0.0983  365 ASP A CB  
2831 C CG  . ASP A 365 ? 1.0644 0.4874 0.6631 -0.0797 0.1296  0.0954  365 ASP A CG  
2832 O OD1 . ASP A 365 ? 0.9989 0.4551 0.6110 -0.0687 0.1067  0.0905  365 ASP A OD1 
2833 O OD2 . ASP A 365 ? 1.1359 0.5393 0.7100 -0.0924 0.1540  0.0976  365 ASP A OD2 
2834 N N   . GLY A 366 ? 0.8993 0.4317 0.6307 -0.0519 0.0807  0.0689  366 GLY A N   
2835 C CA  . GLY A 366 ? 0.8228 0.4070 0.6066 -0.0521 0.0800  0.0539  366 GLY A CA  
2836 C C   . GLY A 366 ? 0.7984 0.4114 0.5880 -0.0576 0.0861  0.0481  366 GLY A C   
2837 O O   . GLY A 366 ? 0.7685 0.4192 0.5995 -0.0606 0.0901  0.0363  366 GLY A O   
2838 N N   . GLY A 367 ? 0.8003 0.3950 0.5485 -0.0587 0.0860  0.0558  367 GLY A N   
2839 C CA  . GLY A 367 ? 0.7822 0.4005 0.5328 -0.0635 0.0917  0.0504  367 GLY A CA  
2840 C C   . GLY A 367 ? 0.7454 0.3867 0.4927 -0.0526 0.0677  0.0493  367 GLY A C   
2841 O O   . GLY A 367 ? 0.6914 0.3366 0.4419 -0.0408 0.0464  0.0512  367 GLY A O   
2842 N N   . VAL A 368 ? 0.7121 0.3688 0.4552 -0.0569 0.0721  0.0456  368 VAL A N   
2843 C CA  . VAL A 368 ? 0.7327 0.4127 0.4752 -0.0491 0.0519  0.0435  368 VAL A CA  
2844 C C   . VAL A 368 ? 0.7907 0.4401 0.4804 -0.0510 0.0500  0.0514  368 VAL A C   
2845 O O   . VAL A 368 ? 0.8158 0.4330 0.4735 -0.0602 0.0692  0.0561  368 VAL A O   
2846 C CB  . VAL A 368 ? 0.6964 0.4217 0.4791 -0.0517 0.0552  0.0317  368 VAL A CB  
2847 C CG1 . VAL A 368 ? 0.5924 0.3473 0.4221 -0.0480 0.0517  0.0238  368 VAL A CG1 
2848 C CG2 . VAL A 368 ? 0.6406 0.3614 0.4213 -0.0641 0.0797  0.0287  368 VAL A CG2 
2849 N N   . TYR A 369 ? 0.7199 0.3792 0.4006 -0.0424 0.0269  0.0522  369 TYR A N   
2850 C CA  . TYR A 369 ? 0.7774 0.4100 0.4083 -0.0435 0.0210  0.0583  369 TYR A CA  
2851 C C   . TYR A 369 ? 0.7475 0.4116 0.3915 -0.0376 0.0003  0.0528  369 TYR A C   
2852 O O   . TYR A 369 ? 0.7077 0.4036 0.3888 -0.0291 -0.0156 0.0484  369 TYR A O   
2853 C CB  . TYR A 369 ? 0.8151 0.4012 0.3993 -0.0382 0.0094  0.0710  369 TYR A CB  
2854 C CG  . TYR A 369 ? 0.8588 0.3997 0.3806 -0.0455 0.0190  0.0786  369 TYR A CG  
2855 C CD1 . TYR A 369 ? 0.9598 0.4737 0.4627 -0.0577 0.0494  0.0809  369 TYR A CD1 
2856 C CD2 . TYR A 369 ? 0.8761 0.4008 0.3577 -0.0408 -0.0018 0.0828  369 TYR A CD2 
2857 C CE1 . TYR A 369 ? 0.9528 0.4232 0.3956 -0.0650 0.0609  0.0874  369 TYR A CE1 
2858 C CE2 . TYR A 369 ? 0.9204 0.4007 0.3397 -0.0478 0.0071  0.0893  369 TYR A CE2 
2859 C CZ  . TYR A 369 ? 0.9469 0.3995 0.3456 -0.0599 0.0396  0.0916  369 TYR A CZ  
2860 O OH  . TYR A 369 ? 1.1243 0.5307 0.4582 -0.0673 0.0511  0.0976  369 TYR A OH  
2861 N N   . TRP A 370 ? 0.7420 0.3960 0.3553 -0.0427 0.0019  0.0525  370 TRP A N   
2862 C CA  . TRP A 370 ? 0.8157 0.4945 0.4365 -0.0387 -0.0173 0.0476  370 TRP A CA  
2863 C C   . TRP A 370 ? 0.8151 0.4631 0.3830 -0.0441 -0.0168 0.0505  370 TRP A C   
2864 O O   . TRP A 370 ? 0.8024 0.4158 0.3335 -0.0521 0.0032  0.0545  370 TRP A O   
2865 C CB  . TRP A 370 ? 0.6635 0.3894 0.3348 -0.0415 -0.0102 0.0364  370 TRP A CB  
2866 C CG  . TRP A 370 ? 0.6993 0.4258 0.3767 -0.0522 0.0176  0.0319  370 TRP A CG  
2867 C CD1 . TRP A 370 ? 0.7078 0.4176 0.3570 -0.0604 0.0315  0.0307  370 TRP A CD1 
2868 C CD2 . TRP A 370 ? 0.5979 0.3437 0.3149 -0.0554 0.0341  0.0270  370 TRP A CD2 
2869 N NE1 . TRP A 370 ? 0.6438 0.3626 0.3156 -0.0681 0.0563  0.0254  370 TRP A NE1 
2870 C CE2 . TRP A 370 ? 0.5793 0.3204 0.2930 -0.0653 0.0572  0.0231  370 TRP A CE2 
2871 C CE3 . TRP A 370 ? 0.6133 0.3792 0.3682 -0.0507 0.0312  0.0248  370 TRP A CE3 
2872 C CZ2 . TRP A 370 ? 0.5848 0.3421 0.3346 -0.0704 0.0755  0.0174  370 TRP A CZ2 
2873 C CZ3 . TRP A 370 ? 0.5359 0.3160 0.3223 -0.0563 0.0490  0.0190  370 TRP A CZ3 
2874 C CH2 . TRP A 370 ? 0.5765 0.3530 0.3617 -0.0659 0.0701  0.0155  370 TRP A CH2 
2875 N N   . GLU A 371 ? 0.7966 0.4573 0.3614 -0.0401 -0.0385 0.0477  371 GLU A N   
2876 C CA  . GLU A 371 ? 0.8791 0.5131 0.3948 -0.0451 -0.0409 0.0485  371 GLU A CA  
2877 C C   . GLU A 371 ? 0.8472 0.4852 0.3638 -0.0564 -0.0135 0.0416  371 GLU A C   
2878 O O   . GLU A 371 ? 0.7753 0.4520 0.3389 -0.0582 -0.0058 0.0332  371 GLU A O   
2879 C CB  . GLU A 371 ? 0.8265 0.4803 0.3497 -0.0392 -0.0703 0.0448  371 GLU A CB  
2880 C CG  . GLU A 371 ? 0.8154 0.4510 0.3186 -0.0285 -0.1003 0.0525  371 GLU A CG  
2881 C CD  . GLU A 371 ? 0.8984 0.5521 0.4418 -0.0188 -0.1076 0.0550  371 GLU A CD  
2882 O OE1 . GLU A 371 ? 0.8286 0.5185 0.4222 -0.0196 -0.0950 0.0486  371 GLU A OE1 
2883 O OE2 . GLU A 371 ? 0.9242 0.5539 0.4471 -0.0101 -0.1266 0.0631  371 GLU A OE2 
2884 N N   . GLY A 372 ? 0.8717 0.4680 0.3353 -0.0636 0.0018  0.0451  372 GLY A N   
2885 C CA  . GLY A 372 ? 0.8612 0.4569 0.3230 -0.0739 0.0293  0.0383  372 GLY A CA  
2886 C C   . GLY A 372 ? 0.9068 0.5012 0.3883 -0.0802 0.0599  0.0380  372 GLY A C   
2887 O O   . GLY A 372 ? 0.8763 0.4719 0.3619 -0.0883 0.0842  0.0316  372 GLY A O   
2888 N N   . ILE A 373 ? 0.8812 0.4733 0.3771 -0.0766 0.0595  0.0440  373 ILE A N   
2889 C CA  . ILE A 373 ? 0.8770 0.4677 0.3943 -0.0832 0.0876  0.0432  373 ILE A CA  
2890 C C   . ILE A 373 ? 0.8847 0.4291 0.3517 -0.0931 0.1138  0.0473  373 ILE A C   
2891 O O   . ILE A 373 ? 0.9011 0.4469 0.3871 -0.1015 0.1425  0.0433  373 ILE A O   
2892 C CB  . ILE A 373 ? 0.8230 0.4175 0.3632 -0.0771 0.0793  0.0487  373 ILE A CB  
2893 C CG1 . ILE A 373 ? 0.8405 0.4458 0.4185 -0.0839 0.1050  0.0448  373 ILE A CG1 
2894 C CG2 . ILE A 373 ? 0.9077 0.4541 0.3934 -0.0741 0.0704  0.0614  373 ILE A CG2 
2895 C CD1 . ILE A 373 ? 0.8713 0.4868 0.4800 -0.0780 0.0964  0.0474  373 ILE A CD1 
2896 N N   . ASP A 374 ? 0.9544 0.4568 0.3571 -0.0926 0.1047  0.0547  374 ASP A N   
2897 C CA  . ASP A 374 ? 1.0672 0.5266 0.4185 -0.1012 0.1274  0.0564  374 ASP A CA  
2898 C C   . ASP A 374 ? 1.1028 0.5432 0.4589 -0.1063 0.1514  0.0596  374 ASP A C   
2899 O O   . ASP A 374 ? 1.2147 0.6382 0.5591 -0.1128 0.1745  0.0547  374 ASP A O   
2900 C CB  . ASP A 374 ? 1.1029 0.5798 0.4693 -0.1074 0.1449  0.0437  374 ASP A CB  
2901 C CG  . ASP A 374 ? 1.3910 0.8347 0.7127 -0.1104 0.1512  0.0409  374 ASP A CG  
2902 O OD1 . ASP A 374 ? 1.4578 0.8649 0.7364 -0.1084 0.1439  0.0487  374 ASP A OD1 
2903 O OD2 . ASP A 374 ? 1.5506 1.0036 0.8798 -0.1146 0.1634  0.0310  374 ASP A OD2 
2904 N N   . GLU A 375 ? 1.0627 0.5047 0.4366 -0.1033 0.1464  0.0672  375 GLU A N   
2905 C CA  . GLU A 375 ? 1.0689 0.4933 0.4489 -0.1080 0.1669  0.0700  375 GLU A CA  
2906 C C   . GLU A 375 ? 1.1063 0.4940 0.4458 -0.1013 0.1486  0.0827  375 GLU A C   
2907 O O   . GLU A 375 ? 1.1096 0.5019 0.4519 -0.0924 0.1226  0.0898  375 GLU A O   
2908 C CB  . GLU A 375 ? 1.0772 0.5331 0.5179 -0.1112 0.1789  0.0667  375 GLU A CB  
2909 C CG  . GLU A 375 ? 1.0882 0.5802 0.5755 -0.1179 0.1995  0.0534  375 GLU A CG  
2910 C CD  . GLU A 375 ? 1.0606 0.5796 0.6086 -0.1218 0.2130  0.0487  375 GLU A CD  
2911 O OE1 . GLU A 375 ? 1.0597 0.5611 0.6092 -0.1245 0.2234  0.0521  375 GLU A OE1 
2912 O OE2 . GLU A 375 ? 0.9407 0.5065 0.5431 -0.1190 0.2073  0.0383  375 GLU A OE2 
2913 N N   . PRO A 376 ? 1.1352 0.4860 0.4375 -0.1047 0.1604  0.0857  376 PRO A N   
2914 C CA  . PRO A 376 ? 1.1546 0.4702 0.4213 -0.0983 0.1438  0.0979  376 PRO A CA  
2915 C C   . PRO A 376 ? 1.2006 0.5209 0.5013 -0.0982 0.1498  0.1026  376 PRO A C   
2916 O O   . PRO A 376 ? 1.1791 0.5194 0.5222 -0.1063 0.1747  0.0959  376 PRO A O   
2917 C CB  . PRO A 376 ? 1.2072 0.4830 0.4269 -0.1043 0.1607  0.0981  376 PRO A CB  
2918 C CG  . PRO A 376 ? 1.2206 0.5142 0.4701 -0.1152 0.1947  0.0863  376 PRO A CG  
2919 C CD  . PRO A 376 ? 1.1557 0.4937 0.4464 -0.1141 0.1893  0.0779  376 PRO A CD  
2920 N N   . LEU A 377 ? 1.2255 0.5281 0.5105 -0.0885 0.1252  0.1133  377 LEU A N   
2921 C CA  . LEU A 377 ? 1.2493 0.5503 0.5619 -0.0871 0.1275  0.1184  377 LEU A CA  
2922 C C   . LEU A 377 ? 1.3144 0.5746 0.5943 -0.0906 0.1398  0.1251  377 LEU A C   
2923 O O   . LEU A 377 ? 1.2876 0.5152 0.5154 -0.0900 0.1361  0.1290  377 LEU A O   
2924 C CB  . LEU A 377 ? 1.2113 0.5175 0.5317 -0.0731 0.0931  0.1256  377 LEU A CB  
2925 C CG  . LEU A 377 ? 1.1139 0.4696 0.4823 -0.0686 0.0805  0.1169  377 LEU A CG  
2926 C CD1 . LEU A 377 ? 1.1293 0.5015 0.5173 -0.0518 0.0444  0.1187  377 LEU A CD1 
2927 C CD2 . LEU A 377 ? 1.1018 0.4958 0.5336 -0.0764 0.1039  0.1055  377 LEU A CD2 
2928 N N   . ALA A 378 ? 1.2820 0.5436 0.5933 -0.0947 0.1545  0.1258  378 ALA A N   
2929 C CA  . ALA A 378 ? 1.3961 0.6199 0.6804 -0.0983 0.1665  0.1327  378 ALA A CA  
2930 C C   . ALA A 378 ? 1.3872 0.5786 0.6332 -0.0857 0.1362  0.1457  378 ALA A C   
2931 O O   . ALA A 378 ? 1.3533 0.5581 0.6117 -0.0739 0.1077  0.1485  378 ALA A O   
2932 C CB  . ALA A 378 ? 1.3157 0.5524 0.6486 -0.1057 0.1875  0.1293  378 ALA A CB  
2933 N N   . PRO A 379 ? 1.4082 0.5568 0.6084 -0.0875 0.1411  0.1533  379 PRO A N   
2934 C CA  . PRO A 379 ? 1.3947 0.5121 0.5620 -0.0751 0.1121  0.1657  379 PRO A CA  
2935 C C   . PRO A 379 ? 1.3623 0.4913 0.5715 -0.0676 0.1001  0.1693  379 PRO A C   
2936 O O   . PRO A 379 ? 1.3347 0.4771 0.5842 -0.0754 0.1213  0.1653  379 PRO A O   
2937 C CB  . PRO A 379 ? 1.4719 0.5427 0.5911 -0.0822 0.1293  0.1720  379 PRO A CB  
2938 C CG  . PRO A 379 ? 1.4929 0.5679 0.6028 -0.0951 0.1582  0.1624  379 PRO A CG  
2939 C CD  . PRO A 379 ? 1.3967 0.5222 0.5697 -0.1001 0.1719  0.1506  379 PRO A CD  
2940 N N   . GLY A 380 ? 1.3748 0.4997 0.5770 -0.0519 0.0648  0.1758  380 GLY A N   
2941 C CA  . GLY A 380 ? 1.3388 0.4729 0.5792 -0.0421 0.0497  0.1785  380 GLY A CA  
2942 C C   . GLY A 380 ? 1.3235 0.5022 0.6170 -0.0380 0.0422  0.1699  380 GLY A C   
2943 O O   . GLY A 380 ? 1.2665 0.4533 0.5896 -0.0264 0.0233  0.1711  380 GLY A O   
2944 N N   . VAL A 381 ? 1.3003 0.5071 0.6072 -0.0466 0.0564  0.1607  381 VAL A N   
2945 C CA  . VAL A 381 ? 1.2214 0.4689 0.5758 -0.0436 0.0499  0.1526  381 VAL A CA  
2946 C C   . VAL A 381 ? 1.2064 0.4631 0.5507 -0.0281 0.0132  0.1549  381 VAL A C   
2947 O O   . VAL A 381 ? 1.2651 0.5148 0.5721 -0.0272 0.0035  0.1562  381 VAL A O   
2948 C CB  . VAL A 381 ? 1.2599 0.5345 0.6331 -0.0582 0.0777  0.1420  381 VAL A CB  
2949 C CG1 . VAL A 381 ? 1.1485 0.4830 0.5816 -0.0531 0.0671  0.1286  381 VAL A CG1 
2950 C CG2 . VAL A 381 ? 1.1860 0.4584 0.5804 -0.0724 0.1118  0.1378  381 VAL A CG2 
2951 N N   . THR A 382 ? 1.1970 0.4887 0.5919 -0.0152 -0.0075 0.1488  382 THR A N   
2952 C CA  . THR A 382 ? 1.2105 0.5280 0.6169 0.0004  -0.0424 0.1462  382 THR A CA  
2953 C C   . THR A 382 ? 1.0832 0.4685 0.5513 0.0003  -0.0422 0.1292  382 THR A C   
2954 O O   . THR A 382 ? 0.9925 0.4062 0.5026 -0.0077 -0.0209 0.1195  382 THR A O   
2955 C CB  . THR A 382 ? 1.1157 0.4216 0.5336 0.0170  -0.0676 0.1517  382 THR A CB  
2956 O OG1 . THR A 382 ? 1.1978 0.5276 0.6699 0.0166  -0.0554 0.1436  382 THR A OG1 
2957 C CG2 . THR A 382 ? 1.2334 0.4708 0.5867 0.0185  -0.0716 0.1694  382 THR A CG2 
2958 N N   . ILE A 383 ? 1.1080 0.5176 0.5806 0.0093  -0.0671 0.1257  383 ILE A N   
2959 C CA  . ILE A 383 ? 1.0007 0.4702 0.5236 0.0089  -0.0684 0.1110  383 ILE A CA  
2960 C C   . ILE A 383 ? 1.0183 0.5212 0.5855 0.0250  -0.0953 0.1057  383 ILE A C   
2961 O O   . ILE A 383 ? 1.0366 0.5211 0.5852 0.0372  -0.1220 0.1128  383 ILE A O   
2962 C CB  . ILE A 383 ? 1.0428 0.5155 0.5370 0.0034  -0.0713 0.1096  383 ILE A CB  
2963 C CG1 . ILE A 383 ? 1.0857 0.5218 0.5330 -0.0120 -0.0431 0.1146  383 ILE A CG1 
2964 C CG2 . ILE A 383 ? 0.9331 0.4656 0.4794 0.0023  -0.0712 0.0950  383 ILE A CG2 
2965 C CD1 . ILE A 383 ? 1.0758 0.5104 0.4907 -0.0177 -0.0441 0.1125  383 ILE A CD1 
2966 N N   . THR A 384 ? 0.8252 0.3761 0.4506 0.0250  -0.0883 0.0930  384 THR A N   
2967 C CA  . THR A 384 ? 0.8377 0.4280 0.5102 0.0384  -0.1090 0.0851  384 THR A CA  
2968 C C   . THR A 384 ? 0.8741 0.5111 0.5730 0.0347  -0.1098 0.0743  384 THR A C   
2969 O O   . THR A 384 ? 0.8172 0.4755 0.5328 0.0237  -0.0886 0.0670  384 THR A O   
2970 C CB  . THR A 384 ? 0.9148 0.5207 0.6305 0.0418  -0.1004 0.0786  384 THR A CB  
2971 O OG1 . THR A 384 ? 0.9632 0.5240 0.6552 0.0465  -0.1023 0.0889  384 THR A OG1 
2972 C CG2 . THR A 384 ? 0.8827 0.5326 0.6486 0.0544  -0.1176 0.0686  384 THR A CG2 
2973 N N   . SER A 385 ? 0.8524 0.5044 0.5562 0.0437  -0.1346 0.0733  385 SER A N   
2974 C CA  . SER A 385 ? 0.8399 0.5314 0.5643 0.0396  -0.1366 0.0642  385 SER A CA  
2975 C C   . SER A 385 ? 0.7459 0.4869 0.5297 0.0408  -0.1290 0.0516  385 SER A C   
2976 O O   . SER A 385 ? 0.7864 0.5323 0.5960 0.0462  -0.1249 0.0490  385 SER A O   
2977 C CB  . SER A 385 ? 0.8364 0.5298 0.5526 0.0486  -0.1664 0.0661  385 SER A CB  
2978 O OG  . SER A 385 ? 0.8309 0.5465 0.5882 0.0629  -0.1849 0.0623  385 SER A OG  
2979 N N   . TRP A 386 ? 0.7307 0.5066 0.5336 0.0356  -0.1272 0.0435  386 TRP A N   
2980 C CA  . TRP A 386 ? 0.6738 0.4952 0.5278 0.0362  -0.1207 0.0319  386 TRP A CA  
2981 C C   . TRP A 386 ? 0.7199 0.5624 0.6095 0.0502  -0.1392 0.0279  386 TRP A C   
2982 O O   . TRP A 386 ? 0.7339 0.6071 0.6635 0.0525  -0.1323 0.0189  386 TRP A O   
2983 C CB  . TRP A 386 ? 0.6436 0.4930 0.5058 0.0274  -0.1155 0.0256  386 TRP A CB  
2984 C CG  . TRP A 386 ? 0.6667 0.5268 0.5289 0.0317  -0.1370 0.0252  386 TRP A CG  
2985 C CD1 . TRP A 386 ? 0.6891 0.5215 0.5114 0.0314  -0.1510 0.0322  386 TRP A CD1 
2986 C CD2 . TRP A 386 ? 0.6377 0.5385 0.5419 0.0362  -0.1472 0.0167  386 TRP A CD2 
2987 N NE1 . TRP A 386 ? 0.6807 0.5354 0.5200 0.0357  -0.1711 0.0282  386 TRP A NE1 
2988 C CE2 . TRP A 386 ? 0.6719 0.5693 0.5631 0.0383  -0.1681 0.0188  386 TRP A CE2 
2989 C CE3 . TRP A 386 ? 0.6202 0.5587 0.5704 0.0381  -0.1399 0.0074  386 TRP A CE3 
2990 C CZ2 . TRP A 386 ? 0.5942 0.5268 0.5217 0.0418  -0.1815 0.0115  386 TRP A CZ2 
2991 C CZ3 . TRP A 386 ? 0.5369 0.5086 0.5199 0.0415  -0.1513 0.0008  386 TRP A CZ3 
2992 C CH2 . TRP A 386 ? 0.6347 0.6043 0.6086 0.0431  -0.1717 0.0028  386 TRP A CH2 
2993 N N   . LYS A 387 ? 0.7089 0.5353 0.5849 0.0598  -0.1626 0.0338  387 LYS A N   
2994 C CA  . LYS A 387 ? 0.7880 0.6313 0.6994 0.0746  -0.1811 0.0303  387 LYS A CA  
2995 C C   . LYS A 387 ? 0.8289 0.6490 0.7419 0.0836  -0.1804 0.0340  387 LYS A C   
2996 O O   . LYS A 387 ? 0.9136 0.7397 0.8513 0.0976  -0.1974 0.0325  387 LYS A O   
2997 C CB  . LYS A 387 ? 0.8011 0.6372 0.7006 0.0820  -0.2096 0.0347  387 LYS A CB  
2998 C CG  . LYS A 387 ? 0.8229 0.6866 0.7300 0.0748  -0.2140 0.0291  387 LYS A CG  
2999 C CD  . LYS A 387 ? 0.8153 0.6750 0.7186 0.0835  -0.2454 0.0317  387 LYS A CD  
3000 C CE  . LYS A 387 ? 0.8815 0.7694 0.7960 0.0758  -0.2504 0.0250  387 LYS A CE  
3001 N NZ  . LYS A 387 ? 1.0075 0.8744 0.8758 0.0614  -0.2373 0.0287  387 LYS A NZ  
3002 N N   . ASN A 388 ? 0.8209 0.6149 0.7105 0.0758  -0.1612 0.0382  388 ASN A N   
3003 C CA  . ASN A 388 ? 0.8761 0.6440 0.7645 0.0823  -0.1584 0.0419  388 ASN A CA  
3004 C C   . ASN A 388 ? 0.9600 0.6906 0.8218 0.0942  -0.1817 0.0532  388 ASN A C   
3005 O O   . ASN A 388 ? 1.0341 0.7592 0.9151 0.1073  -0.1923 0.0531  388 ASN A O   
3006 C CB  . ASN A 388 ? 0.7971 0.5976 0.7368 0.0895  -0.1539 0.0300  388 ASN A CB  
3007 C CG  . ASN A 388 ? 0.8518 0.6292 0.7907 0.0898  -0.1410 0.0306  388 ASN A CG  
3008 O OD1 . ASN A 388 ? 0.9050 0.6621 0.8205 0.0779  -0.1235 0.0342  388 ASN A OD1 
3009 N ND2 . ASN A 388 ? 1.0601 0.8404 1.0265 0.1032  -0.1493 0.0266  388 ASN A ND2 
3010 N N   . LYS A 389 ? 0.9918 0.6948 0.8075 0.0899  -0.1903 0.0629  389 LYS A N   
3011 C CA  . LYS A 389 ? 1.1034 0.7656 0.8842 0.1002  -0.2141 0.0750  389 LYS A CA  
3012 C C   . LYS A 389 ? 1.1576 0.7686 0.8731 0.0895  -0.2040 0.0878  389 LYS A C   
3013 O O   . LYS A 389 ? 1.0795 0.6931 0.7791 0.0745  -0.1827 0.0861  389 LYS A O   
3014 C CB  . LYS A 389 ? 1.1135 0.7936 0.9024 0.1084  -0.2428 0.0735  389 LYS A CB  
3015 C CG  . LYS A 389 ? 1.1623 0.8937 1.0173 0.1188  -0.2526 0.0607  389 LYS A CG  
3016 C CD  . LYS A 389 ? 1.2175 0.9674 1.0815 0.1242  -0.2794 0.0586  389 LYS A CD  
3017 C CE  . LYS A 389 ? 1.2565 1.0602 1.1896 0.1325  -0.2854 0.0449  389 LYS A CE  
3018 N NZ  . LYS A 389 ? 1.2913 1.1159 1.2381 0.1360  -0.3105 0.0417  389 LYS A NZ  
3019 N N   . GLU A 390 ? 1.2180 0.7809 0.8956 0.0976  -0.2189 0.1007  390 GLU A N   
3020 C CA  . GLU A 390 ? 1.2991 0.8083 0.9075 0.0883  -0.2122 0.1140  390 GLU A CA  
3021 C C   . GLU A 390 ? 1.2445 0.7564 0.8237 0.0829  -0.2225 0.1143  390 GLU A C   
3022 O O   . GLU A 390 ? 1.3236 0.8572 0.9202 0.0925  -0.2493 0.1106  390 GLU A O   
3023 C CB  . GLU A 390 ? 1.3182 0.7735 0.8897 0.0996  -0.2301 0.1285  390 GLU A CB  
3024 C CG  . GLU A 390 ? 1.4782 0.9094 1.0534 0.0985  -0.2114 0.1322  390 GLU A CG  
3025 C CD  . GLU A 390 ? 1.5664 0.9700 1.1048 0.0795  -0.1780 0.1368  390 GLU A CD  
3026 O OE1 . GLU A 390 ? 1.5400 0.9244 1.0320 0.0696  -0.1731 0.1419  390 GLU A OE1 
3027 O OE2 . GLU A 390 ? 1.5976 0.9990 1.1549 0.0742  -0.1563 0.1344  390 GLU A OE2 
3028 N N   . TRP A 391 ? 1.2467 0.7368 0.7835 0.0673  -0.2005 0.1177  391 TRP A N   
3029 C CA  . TRP A 391 ? 1.3169 0.8099 0.8260 0.0602  -0.2054 0.1160  391 TRP A CA  
3030 C C   . TRP A 391 ? 1.4208 0.8543 0.8529 0.0507  -0.1950 0.1284  391 TRP A C   
3031 O O   . TRP A 391 ? 1.3627 0.7736 0.7780 0.0403  -0.1660 0.1321  391 TRP A O   
3032 C CB  . TRP A 391 ? 1.1837 0.7260 0.7320 0.0490  -0.1842 0.1023  391 TRP A CB  
3033 C CG  . TRP A 391 ? 1.2138 0.7608 0.7380 0.0416  -0.1885 0.0993  391 TRP A CG  
3034 C CD1 . TRP A 391 ? 1.1557 0.7350 0.7029 0.0466  -0.2110 0.0921  391 TRP A CD1 
3035 C CD2 . TRP A 391 ? 1.2263 0.7441 0.6995 0.0276  -0.1688 0.1025  391 TRP A CD2 
3036 N NE1 . TRP A 391 ? 1.2232 0.7941 0.7357 0.0365  -0.2077 0.0907  391 TRP A NE1 
3037 C CE2 . TRP A 391 ? 1.2458 0.7790 0.7121 0.0252  -0.1815 0.0968  391 TRP A CE2 
3038 C CE3 . TRP A 391 ? 1.2694 0.7496 0.7042 0.0165  -0.1404 0.1090  391 TRP A CE3 
3039 C CZ2 . TRP A 391 ? 1.2530 0.7642 0.6733 0.0128  -0.1672 0.0971  391 TRP A CZ2 
3040 C CZ3 . TRP A 391 ? 1.2940 0.7537 0.6849 0.0042  -0.1249 0.1093  391 TRP A CZ3 
3041 C CH2 . TRP A 391 ? 1.3092 0.7840 0.6922 0.0028  -0.1384 0.1032  391 TRP A CH2 
3042 N N   . ARG A 392 ? 1.5582 0.9660 0.9439 0.0538  -0.2183 0.1341  392 ARG A N   
3043 C CA  . ARG A 392 ? 1.7214 1.0820 1.0406 0.0436  -0.2060 0.1411  392 ARG A CA  
3044 C C   . ARG A 392 ? 1.7488 1.1217 1.0508 0.0333  -0.2014 0.1335  392 ARG A C   
3045 O O   . ARG A 392 ? 1.6969 1.1067 1.0288 0.0378  -0.2211 0.1253  392 ARG A O   
3046 C CB  . ARG A 392 ? 1.8423 1.1725 1.1343 0.0531  -0.2294 0.1475  392 ARG A CB  
3047 C CG  . ARG A 392 ? 1.8759 1.1858 1.1763 0.0620  -0.2310 0.1557  392 ARG A CG  
3048 C CD  . ARG A 392 ? 2.0484 1.3220 1.3128 0.0693  -0.2511 0.1630  392 ARG A CD  
3049 N NE  . ARG A 392 ? 2.1728 1.4239 1.4423 0.0768  -0.2506 0.1712  392 ARG A NE  
3050 C CZ  . ARG A 392 ? 2.1955 1.4110 1.4347 0.0836  -0.2653 0.1792  392 ARG A CZ  
3051 N NH1 . ARG A 392 ? 2.2417 1.4380 1.4418 0.0841  -0.2826 0.1804  392 ARG A NH1 
3052 N NH2 . ARG A 392 ? 2.2210 1.4182 1.4689 0.0899  -0.2629 0.1861  392 ARG A NH2 
3053 N N   . PRO A 393 ? 1.8085 1.1522 1.0658 0.0192  -0.1746 0.1348  393 PRO A N   
3054 C CA  . PRO A 393 ? 1.8317 1.1857 1.0738 0.0094  -0.1678 0.1264  393 PRO A CA  
3055 C C   . PRO A 393 ? 1.9530 1.3070 1.1812 0.0153  -0.1983 0.1230  393 PRO A C   
3056 O O   . PRO A 393 ? 1.9941 1.3621 1.2183 0.0087  -0.1972 0.1148  393 PRO A O   
3057 C CB  . PRO A 393 ? 1.8661 1.1830 1.0638 -0.0049 -0.1325 0.1290  393 PRO A CB  
3058 C CG  . PRO A 393 ? 1.8060 1.1093 1.0136 -0.0054 -0.1143 0.1364  393 PRO A CG  
3059 C CD  . PRO A 393 ? 1.7778 1.0828 1.0048 0.0109  -0.1454 0.1422  393 PRO A CD  
3060 N N   . GLN A 394 ? 2.0921 1.4308 1.3147 0.0272  -0.2251 0.1285  394 GLN A N   
3061 C CA  . GLN A 394 ? 2.2358 1.5738 1.4481 0.0331  -0.2554 0.1253  394 GLN A CA  
3062 C C   . GLN A 394 ? 2.1689 1.5497 1.4394 0.0469  -0.2873 0.1205  394 GLN A C   
3063 O O   . GLN A 394 ? 2.2275 1.6029 1.4976 0.0566  -0.3160 0.1212  394 GLN A O   
3064 C CB  . GLN A 394 ? 2.4161 1.7021 1.5747 0.0356  -0.2628 0.1343  394 GLN A CB  
3065 C CG  . GLN A 394 ? 2.5464 1.7909 1.6455 0.0215  -0.2338 0.1365  394 GLN A CG  
3066 C CD  . GLN A 394 ? 2.8200 2.0130 1.8625 0.0239  -0.2446 0.1443  394 GLN A CD  
3067 O OE1 . GLN A 394 ? 2.8719 2.0556 1.9184 0.0361  -0.2699 0.1503  394 GLN A OE1 
3068 N NE2 . GLN A 394 ? 2.8746 2.0333 1.8643 0.0126  -0.2254 0.1439  394 GLN A NE2 
3069 N N   . ASP A 395 ? 2.0254 1.4492 1.3477 0.0478  -0.2821 0.1149  395 ASP A N   
3070 C CA  . ASP A 395 ? 1.9603 1.4318 1.3445 0.0590  -0.3077 0.1075  395 ASP A CA  
3071 C C   . ASP A 395 ? 1.9194 1.4270 1.3240 0.0515  -0.3089 0.0958  395 ASP A C   
3072 O O   . ASP A 395 ? 1.9233 1.4161 1.2916 0.0391  -0.2924 0.0939  395 ASP A O   
3073 C CB  . ASP A 395 ? 1.8356 1.3302 1.2660 0.0661  -0.3019 0.1085  395 ASP A CB  
3074 C CG  . ASP A 395 ? 1.8459 1.3067 1.2627 0.0747  -0.3035 0.1191  395 ASP A CG  
3075 O OD1 . ASP A 395 ? 1.9427 1.3641 1.3155 0.0757  -0.3110 0.1258  395 ASP A OD1 
3076 O OD2 . ASP A 395 ? 1.7250 1.1978 1.1752 0.0806  -0.2972 0.1206  395 ASP A OD2 
3077 N N   . GLU A 396 ? 1.8926 1.4487 1.3581 0.0589  -0.3272 0.0873  396 GLU A N   
3078 C CA  . GLU A 396 ? 1.8764 1.4709 1.3692 0.0517  -0.3277 0.0757  396 GLU A CA  
3079 C C   . GLU A 396 ? 1.7240 1.3566 1.2583 0.0482  -0.3116 0.0701  396 GLU A C   
3080 O O   . GLU A 396 ? 1.6766 1.3247 1.2108 0.0370  -0.2985 0.0634  396 GLU A O   
3081 C CB  . GLU A 396 ? 1.8904 1.5151 1.4249 0.0601  -0.3575 0.0683  396 GLU A CB  
3082 C CG  . GLU A 396 ? 1.8774 1.5349 1.4334 0.0513  -0.3586 0.0568  396 GLU A CG  
3083 C CD  . GLU A 396 ? 1.8050 1.5002 1.4155 0.0591  -0.3843 0.0487  396 GLU A CD  
3084 O OE1 . GLU A 396 ? 1.8337 1.5420 1.4805 0.0716  -0.3976 0.0498  396 GLU A OE1 
3085 O OE2 . GLU A 396 ? 1.7028 1.4143 1.3212 0.0525  -0.3899 0.0407  396 GLU A OE2 
3086 N N   . GLU A 397 ? 1.5489 1.1975 1.1214 0.0571  -0.3104 0.0717  397 GLU A N   
3087 C CA  . GLU A 397 ? 1.3471 1.0405 0.9745 0.0517  -0.2832 0.0626  397 GLU A CA  
3088 C C   . GLU A 397 ? 1.2121 0.8852 0.8091 0.0388  -0.2476 0.0653  397 GLU A C   
3089 O O   . GLU A 397 ? 1.1909 0.8207 0.7452 0.0387  -0.2394 0.0755  397 GLU A O   
3090 C CB  . GLU A 397 ? 1.3205 1.0356 0.9985 0.0640  -0.2863 0.0617  397 GLU A CB  
3091 C CG  . GLU A 397 ? 1.4640 1.2115 1.1900 0.0765  -0.3166 0.0557  397 GLU A CG  
3092 C CD  . GLU A 397 ? 1.5251 1.3277 1.3058 0.0708  -0.3106 0.0422  397 GLU A CD  
3093 O OE1 . GLU A 397 ? 1.3991 1.2189 1.1900 0.0599  -0.2818 0.0375  397 GLU A OE1 
3094 O OE2 . GLU A 397 ? 1.6077 1.4360 1.4219 0.0772  -0.3351 0.0363  397 GLU A OE2 
3095 N N   . PRO A 398 ? 1.1305 0.8325 0.7486 0.0277  -0.2259 0.0565  398 PRO A N   
3096 C CA  . PRO A 398 ? 1.0097 0.6985 0.6108 0.0166  -0.1919 0.0577  398 PRO A CA  
3097 C C   . PRO A 398 ? 0.9464 0.6440 0.5789 0.0206  -0.1772 0.0589  398 PRO A C   
3098 O O   . PRO A 398 ? 0.8880 0.6165 0.5684 0.0297  -0.1870 0.0546  398 PRO A O   
3099 C CB  . PRO A 398 ? 0.8870 0.6116 0.5143 0.0067  -0.1783 0.0469  398 PRO A CB  
3100 C CG  . PRO A 398 ? 0.9830 0.7503 0.6608 0.0137  -0.1992 0.0394  398 PRO A CG  
3101 C CD  . PRO A 398 ? 1.0363 0.7838 0.6964 0.0248  -0.2317 0.0451  398 PRO A CD  
3102 N N   . CYS A 399 ? 0.9125 0.5815 0.5175 0.0132  -0.1527 0.0640  399 CYS A N   
3103 C CA  . CYS A 399 ? 0.9163 0.5894 0.5477 0.0156  -0.1381 0.0648  399 CYS A CA  
3104 C C   . CYS A 399 ? 0.7416 0.4624 0.4281 0.0115  -0.1218 0.0535  399 CYS A C   
3105 O O   . CYS A 399 ? 0.7250 0.4612 0.4461 0.0164  -0.1177 0.0511  399 CYS A O   
3106 C CB  . CYS A 399 ? 0.9352 0.5630 0.5227 0.0078  -0.1164 0.0734  399 CYS A CB  
3107 S SG  . CYS A 399 ? 0.9340 0.5615 0.5079 -0.0097 -0.0830 0.0686  399 CYS A SG  
3108 N N   . ALA A 400 ? 0.7261 0.4682 0.4193 0.0028  -0.1131 0.0466  400 ALA A N   
3109 C CA  . ALA A 400 ? 0.7091 0.4934 0.4494 -0.0013 -0.0990 0.0366  400 ALA A CA  
3110 C C   . ALA A 400 ? 0.7010 0.5193 0.4650 -0.0005 -0.1126 0.0294  400 ALA A C   
3111 O O   . ALA A 400 ? 0.6909 0.4979 0.4282 -0.0025 -0.1243 0.0306  400 ALA A O   
3112 C CB  . ALA A 400 ? 0.6618 0.4392 0.3917 -0.0137 -0.0715 0.0349  400 ALA A CB  
3113 N N   . HIS A 401 ? 0.6478 0.5062 0.4604 0.0018  -0.1108 0.0216  401 HIS A N   
3114 C CA  . HIS A 401 ? 0.6042 0.4958 0.4426 0.0014  -0.1207 0.0146  401 HIS A CA  
3115 C C   . HIS A 401 ? 0.5884 0.4810 0.4125 -0.0102 -0.1083 0.0116  401 HIS A C   
3116 O O   . HIS A 401 ? 0.5095 0.3961 0.3282 -0.0171 -0.0873 0.0112  401 HIS A O   
3117 C CB  . HIS A 401 ? 0.5194 0.4503 0.4091 0.0052  -0.1173 0.0071  401 HIS A CB  
3118 C CG  . HIS A 401 ? 0.5253 0.4895 0.4440 0.0053  -0.1278 0.0005  401 HIS A CG  
3119 N ND1 . HIS A 401 ? 0.4908 0.4741 0.4188 -0.0038 -0.1175 -0.0047 401 HIS A ND1 
3120 C CD2 . HIS A 401 ? 0.5052 0.4866 0.4473 0.0131  -0.1472 -0.0020 401 HIS A CD2 
3121 C CE1 . HIS A 401 ? 0.4825 0.4923 0.4369 -0.0026 -0.1291 -0.0098 401 HIS A CE1 
3122 N NE2 . HIS A 401 ? 0.4834 0.4940 0.4487 0.0075  -0.1470 -0.0086 401 HIS A NE2 
3123 N N   . PRO A 402 ? 0.5442 0.4436 0.3635 -0.0124 -0.1213 0.0090  402 PRO A N   
3124 C CA  . PRO A 402 ? 0.5181 0.4151 0.3217 -0.0230 -0.1099 0.0058  402 PRO A CA  
3125 C C   . PRO A 402 ? 0.5270 0.4519 0.3627 -0.0286 -0.0911 -0.0003 402 PRO A C   
3126 O O   . PRO A 402 ? 0.5548 0.4722 0.3767 -0.0367 -0.0765 -0.0019 402 PRO A O   
3127 C CB  . PRO A 402 ? 0.5398 0.4445 0.3422 -0.0229 -0.1311 0.0029  402 PRO A CB  
3128 C CG  . PRO A 402 ? 0.5226 0.4151 0.3176 -0.0127 -0.1542 0.0077  402 PRO A CG  
3129 C CD  . PRO A 402 ? 0.5881 0.4913 0.4108 -0.0052 -0.1482 0.0093  402 PRO A CD  
3130 N N   . ASN A 403 ? 0.5007 0.4559 0.3773 -0.0242 -0.0911 -0.0040 403 ASN A N   
3131 C CA  . ASN A 403 ? 0.4604 0.4390 0.3639 -0.0287 -0.0748 -0.0090 403 ASN A CA  
3132 C C   . ASN A 403 ? 0.4968 0.4734 0.4104 -0.0260 -0.0626 -0.0081 403 ASN A C   
3133 O O   . ASN A 403 ? 0.4699 0.4692 0.4114 -0.0264 -0.0545 -0.0127 403 ASN A O   
3134 C CB  . ASN A 403 ? 0.4340 0.4478 0.3737 -0.0275 -0.0818 -0.0148 403 ASN A CB  
3135 C CG  . ASN A 403 ? 0.4881 0.5214 0.4468 -0.0336 -0.0667 -0.0193 403 ASN A CG  
3136 O OD1 . ASN A 403 ? 0.4395 0.4631 0.3837 -0.0404 -0.0563 -0.0195 403 ASN A OD1 
3137 N ND2 . ASN A 403 ? 0.3877 0.4471 0.3780 -0.0307 -0.0654 -0.0232 403 ASN A ND2 
3138 N N   . SER A 404 ? 0.4414 0.3894 0.3312 -0.0237 -0.0613 -0.0024 404 SER A N   
3139 C CA  . SER A 404 ? 0.4496 0.3930 0.3482 -0.0227 -0.0488 -0.0020 404 SER A CA  
3140 C C   . SER A 404 ? 0.4094 0.3560 0.3122 -0.0312 -0.0297 -0.0052 404 SER A C   
3141 O O   . SER A 404 ? 0.4818 0.4208 0.3683 -0.0377 -0.0237 -0.0054 404 SER A O   
3142 C CB  . SER A 404 ? 0.4974 0.4053 0.3666 -0.0198 -0.0503 0.0056  404 SER A CB  
3143 O OG  . SER A 404 ? 0.5031 0.3821 0.3333 -0.0260 -0.0452 0.0101  404 SER A OG  
3144 N N   . ARG A 405 ? 0.4068 0.3644 0.3327 -0.0307 -0.0208 -0.0085 405 ARG A N   
3145 C CA  . ARG A 405 ? 0.4310 0.3987 0.3703 -0.0372 -0.0063 -0.0130 405 ARG A CA  
3146 C C   . ARG A 405 ? 0.4185 0.3749 0.3631 -0.0388 0.0056  -0.0131 405 ARG A C   
3147 O O   . ARG A 405 ? 0.4011 0.3517 0.3497 -0.0337 0.0019  -0.0118 405 ARG A O   
3148 C CB  . ARG A 405 ? 0.3311 0.3312 0.2999 -0.0360 -0.0093 -0.0191 405 ARG A CB  
3149 C CG  . ARG A 405 ? 0.3494 0.3637 0.3188 -0.0360 -0.0193 -0.0198 405 ARG A CG  
3150 C CD  . ARG A 405 ? 0.3661 0.3830 0.3318 -0.0432 -0.0122 -0.0216 405 ARG A CD  
3151 N NE  . ARG A 405 ? 0.3625 0.3890 0.3265 -0.0443 -0.0217 -0.0222 405 ARG A NE  
3152 C CZ  . ARG A 405 ? 0.3591 0.3890 0.3210 -0.0500 -0.0181 -0.0241 405 ARG A CZ  
3153 N NH1 . ARG A 405 ? 0.3511 0.3769 0.3137 -0.0543 -0.0057 -0.0256 405 ARG A NH1 
3154 N NH2 . ARG A 405 ? 0.3378 0.3754 0.2989 -0.0514 -0.0277 -0.0249 405 ARG A NH2 
3155 N N   . PHE A 406 ? 0.4043 0.3577 0.3513 -0.0458 0.0198  -0.0153 406 PHE A N   
3156 C CA  . PHE A 406 ? 0.4068 0.3600 0.3718 -0.0482 0.0305  -0.0184 406 PHE A CA  
3157 C C   . PHE A 406 ? 0.3296 0.3109 0.3240 -0.0487 0.0304  -0.0255 406 PHE A C   
3158 O O   . PHE A 406 ? 0.3829 0.3784 0.3800 -0.0495 0.0272  -0.0272 406 PHE A O   
3159 C CB  . PHE A 406 ? 0.4310 0.3612 0.3829 -0.0557 0.0474  -0.0166 406 PHE A CB  
3160 C CG  . PHE A 406 ? 0.3837 0.3146 0.3287 -0.0611 0.0551  -0.0181 406 PHE A CG  
3161 C CD1 . PHE A 406 ? 0.3790 0.3292 0.3503 -0.0640 0.0610  -0.0245 406 PHE A CD1 
3162 C CD2 . PHE A 406 ? 0.4485 0.3582 0.3592 -0.0630 0.0560  -0.0134 406 PHE A CD2 
3163 C CE1 . PHE A 406 ? 0.3692 0.3188 0.3357 -0.0682 0.0684  -0.0263 406 PHE A CE1 
3164 C CE2 . PHE A 406 ? 0.4518 0.3603 0.3554 -0.0679 0.0639  -0.0158 406 PHE A CE2 
3165 C CZ  . PHE A 406 ? 0.4300 0.3587 0.3627 -0.0703 0.0707  -0.0223 406 PHE A CZ  
3166 N N   . CYS A 407 ? 0.3829 0.3699 0.3977 -0.0483 0.0331  -0.0297 407 CYS A N   
3167 C CA  . CYS A 407 ? 0.2888 0.2986 0.3284 -0.0484 0.0314  -0.0364 407 CYS A CA  
3168 C C   . CYS A 407 ? 0.3490 0.3541 0.4053 -0.0532 0.0414  -0.0403 407 CYS A C   
3169 O O   . CYS A 407 ? 0.3448 0.3426 0.4074 -0.0525 0.0423  -0.0417 407 CYS A O   
3170 C CB  . CYS A 407 ? 0.3770 0.4013 0.4259 -0.0418 0.0208  -0.0393 407 CYS A CB  
3171 S SG  . CYS A 407 ? 0.3206 0.3697 0.3901 -0.0415 0.0168  -0.0465 407 CYS A SG  
3172 N N   . THR A 408 ? 0.3241 0.3333 0.3897 -0.0581 0.0488  -0.0427 408 THR A N   
3173 C CA  . THR A 408 ? 0.3375 0.3410 0.4208 -0.0636 0.0603  -0.0463 408 THR A CA  
3174 C C   . THR A 408 ? 0.3094 0.3321 0.4187 -0.0647 0.0587  -0.0527 408 THR A C   
3175 O O   . THR A 408 ? 0.3537 0.3869 0.4598 -0.0630 0.0537  -0.0524 408 THR A O   
3176 C CB  . THR A 408 ? 0.3572 0.3389 0.4239 -0.0693 0.0755  -0.0421 408 THR A CB  
3177 O OG1 . THR A 408 ? 0.3940 0.3691 0.4802 -0.0753 0.0888  -0.0458 408 THR A OG1 
3178 C CG2 . THR A 408 ? 0.3673 0.3527 0.4268 -0.0708 0.0787  -0.0418 408 THR A CG2 
3179 N N   . PRO A 409 ? 0.3544 0.3812 0.4901 -0.0674 0.0614  -0.0588 409 PRO A N   
3180 C CA  . PRO A 409 ? 0.3307 0.3750 0.4926 -0.0674 0.0570  -0.0650 409 PRO A CA  
3181 C C   . PRO A 409 ? 0.3200 0.3631 0.4876 -0.0708 0.0677  -0.0650 409 PRO A C   
3182 O O   . PRO A 409 ? 0.3354 0.3638 0.4988 -0.0758 0.0832  -0.0634 409 PRO A O   
3183 C CB  . PRO A 409 ? 0.3488 0.3949 0.5381 -0.0702 0.0574  -0.0718 409 PRO A CB  
3184 C CG  . PRO A 409 ? 0.3920 0.4245 0.5665 -0.0696 0.0579  -0.0692 409 PRO A CG  
3185 C CD  . PRO A 409 ? 0.3576 0.3738 0.5015 -0.0697 0.0656  -0.0606 409 PRO A CD  
3186 N N   . ALA A 410 ? 0.2354 0.2924 0.4113 -0.0680 0.0600  -0.0668 410 ALA A N   
3187 C CA  . ALA A 410 ? 0.3135 0.3701 0.4970 -0.0701 0.0692  -0.0677 410 ALA A CA  
3188 C C   . ALA A 410 ? 0.3788 0.4373 0.5970 -0.0743 0.0797  -0.0744 410 ALA A C   
3189 O O   . ALA A 410 ? 0.3663 0.4174 0.5884 -0.0779 0.0954  -0.0752 410 ALA A O   
3190 C CB  . ALA A 410 ? 0.2621 0.3314 0.4472 -0.0657 0.0571  -0.0678 410 ALA A CB  
3191 N N   . SER A 411 ? 0.3418 0.4101 0.5863 -0.0740 0.0719  -0.0800 411 SER A N   
3192 C CA  . SER A 411 ? 0.3984 0.4720 0.6829 -0.0781 0.0801  -0.0875 411 SER A CA  
3193 C C   . SER A 411 ? 0.4261 0.4834 0.7106 -0.0858 0.1018  -0.0870 411 SER A C   
3194 O O   . SER A 411 ? 0.4841 0.5426 0.7969 -0.0884 0.1123  -0.0923 411 SER A O   
3195 C CB  . SER A 411 ? 0.2942 0.3809 0.6049 -0.0764 0.0641  -0.0942 411 SER A CB  
3196 O OG  . SER A 411 ? 0.4191 0.4975 0.7160 -0.0779 0.0622  -0.0930 411 SER A OG  
3197 N N   . GLN A 412 ? 0.4287 0.4681 0.6770 -0.0871 0.1070  -0.0798 412 GLN A N   
3198 C CA  . GLN A 412 ? 0.4926 0.5112 0.7326 -0.0944 0.1276  -0.0775 412 GLN A CA  
3199 C C   . GLN A 412 ? 0.4644 0.4685 0.6833 -0.0973 0.1452  -0.0740 412 GLN A C   
3200 O O   . GLN A 412 ? 0.5313 0.5165 0.7436 -0.1043 0.1655  -0.0727 412 GLN A O   
3201 C CB  . GLN A 412 ? 0.4289 0.4315 0.6382 -0.0937 0.1235  -0.0710 412 GLN A CB  
3202 C CG  . GLN A 412 ? 0.4665 0.4774 0.6955 -0.0925 0.1112  -0.0755 412 GLN A CG  
3203 C CD  . GLN A 412 ? 0.4353 0.4277 0.6364 -0.0917 0.1096  -0.0694 412 GLN A CD  
3204 O OE1 . GLN A 412 ? 0.4720 0.4648 0.6863 -0.0921 0.1039  -0.0730 412 GLN A OE1 
3205 N NE2 . GLN A 412 ? 0.4203 0.3956 0.5829 -0.0902 0.1135  -0.0606 412 GLN A NE2 
3206 N N   . CYS A 413 ? 0.5228 0.3390 0.9218 -0.1276 0.2350  -0.1584 413 CYS A N   
3207 C CA  . CYS A 413 ? 0.5390 0.3393 0.9090 -0.1210 0.2373  -0.1324 413 CYS A CA  
3208 C C   . CYS A 413 ? 0.5595 0.3721 0.9478 -0.1284 0.2466  -0.1381 413 CYS A C   
3209 O O   . CYS A 413 ? 0.5034 0.3484 0.9128 -0.1350 0.2366  -0.1595 413 CYS A O   
3210 C CB  . CYS A 413 ? 0.4881 0.2971 0.8254 -0.1140 0.2170  -0.1248 413 CYS A CB  
3211 S SG  . CYS A 413 ? 0.5443 0.3336 0.8416 -0.1057 0.2184  -0.0941 413 CYS A SG  
3212 N N   . PRO A 414 ? 0.6139 0.4023 0.9954 -0.1274 0.2653  -0.1202 414 PRO A N   
3213 C CA  . PRO A 414 ? 0.5907 0.3905 0.9941 -0.1347 0.2777  -0.1277 414 PRO A CA  
3214 C C   . PRO A 414 ? 0.5393 0.3631 0.9351 -0.1337 0.2647  -0.1302 414 PRO A C   
3215 O O   . PRO A 414 ? 0.5188 0.3642 0.9451 -0.1403 0.2688  -0.1453 414 PRO A O   
3216 C CB  . PRO A 414 ? 0.5924 0.3555 0.9772 -0.1323 0.3002  -0.1035 414 PRO A CB  
3217 C CG  . PRO A 414 ? 0.6106 0.3462 0.9810 -0.1264 0.3006  -0.0899 414 PRO A CG  
3218 C CD  . PRO A 414 ? 0.5887 0.3382 0.9450 -0.1202 0.2767  -0.0938 414 PRO A CD  
3219 N N   . ILE A 415 ? 0.5162 0.3371 0.8756 -0.1254 0.2493  -0.1165 415 ILE A N   
3220 C CA  . ILE A 415 ? 0.5493 0.3896 0.9013 -0.1240 0.2381  -0.1169 415 ILE A CA  
3221 C C   . ILE A 415 ? 0.4632 0.3291 0.8146 -0.1232 0.2120  -0.1295 415 ILE A C   
3222 O O   . ILE A 415 ? 0.4589 0.3316 0.7904 -0.1189 0.1990  -0.1228 415 ILE A O   
3223 C CB  . ILE A 415 ? 0.5465 0.3611 0.8540 -0.1159 0.2433  -0.0902 415 ILE A CB  
3224 C CG1 . ILE A 415 ? 0.6144 0.4057 0.8852 -0.1072 0.2343  -0.0728 415 ILE A CG1 
3225 C CG2 . ILE A 415 ? 0.5321 0.3256 0.8383 -0.1182 0.2693  -0.0803 415 ILE A CG2 
3226 C CD1 . ILE A 415 ? 0.6160 0.3890 0.8404 -0.0987 0.2308  -0.0498 415 ILE A CD1 
3227 N N   . ILE A 416 ? 0.5143 0.3938 0.8860 -0.1280 0.2047  -0.1485 416 ILE A N   
3228 C CA  . ILE A 416 ? 0.4694 0.3748 0.8380 -0.1287 0.1803  -0.1627 416 ILE A CA  
3229 C C   . ILE A 416 ? 0.4908 0.4303 0.8795 -0.1325 0.1671  -0.1748 416 ILE A C   
3230 O O   . ILE A 416 ? 0.4663 0.4193 0.8889 -0.1379 0.1755  -0.1852 416 ILE A O   
3231 C CB  . ILE A 416 ? 0.4625 0.3763 0.8479 -0.1340 0.1775  -0.1831 416 ILE A CB  
3232 C CG1 . ILE A 416 ? 0.4358 0.3694 0.8041 -0.1336 0.1542  -0.1941 416 ILE A CG1 
3233 C CG2 . ILE A 416 ? 0.4498 0.3848 0.8782 -0.1440 0.1831  -0.2057 416 ILE A CG2 
3234 C CD1 . ILE A 416 ? 0.4454 0.3557 0.7769 -0.1244 0.1515  -0.1761 416 ILE A CD1 
3235 N N   . ASP A 417 ? 0.4569 0.4103 0.8268 -0.1291 0.1464  -0.1728 417 ASP A N   
3236 C CA  . ASP A 417 ? 0.4192 0.4045 0.8083 -0.1306 0.1319  -0.1802 417 ASP A CA  
3237 C C   . ASP A 417 ? 0.4414 0.4645 0.8617 -0.1379 0.1158  -0.2064 417 ASP A C   
3238 O O   . ASP A 417 ? 0.4206 0.4496 0.8310 -0.1409 0.1060  -0.2185 417 ASP A O   
3239 C CB  . ASP A 417 ? 0.4474 0.4362 0.8076 -0.1250 0.1134  -0.1699 417 ASP A CB  
3240 C CG  . ASP A 417 ? 0.4624 0.4788 0.8437 -0.1234 0.1016  -0.1709 417 ASP A CG  
3241 O OD1 . ASP A 417 ? 0.4304 0.4326 0.8107 -0.1186 0.1163  -0.1568 417 ASP A OD1 
3242 O OD2 . ASP A 417 ? 0.4293 0.4822 0.8214 -0.1231 0.0766  -0.1831 417 ASP A OD2 
3243 N N   . PRO A 418 ? 0.3698 0.4193 0.8274 -0.1405 0.1128  -0.2162 418 PRO A N   
3244 C CA  . PRO A 418 ? 0.4531 0.5401 0.9390 -0.1468 0.0946  -0.2405 418 PRO A CA  
3245 C C   . PRO A 418 ? 0.4198 0.5351 0.8850 -0.1455 0.0617  -0.2466 418 PRO A C   
3246 O O   . PRO A 418 ? 0.5485 0.6910 1.0237 -0.1509 0.0452  -0.2659 418 PRO A O   
3247 C CB  . PRO A 418 ? 0.3732 0.4812 0.9028 -0.1470 0.0977  -0.2450 418 PRO A CB  
3248 C CG  . PRO A 418 ? 0.4727 0.5614 0.9911 -0.1396 0.1104  -0.2233 418 PRO A CG  
3249 C CD  . PRO A 418 ? 0.4508 0.4960 0.9272 -0.1377 0.1281  -0.2063 418 PRO A CD  
3250 N N   . ALA A 419 ? 0.3931 0.5025 0.8278 -0.1387 0.0517  -0.2307 419 ALA A N   
3251 C CA  . ALA A 419 ? 0.4656 0.5993 0.8746 -0.1369 0.0215  -0.2340 419 ALA A CA  
3252 C C   . ALA A 419 ? 0.4303 0.5399 0.7946 -0.1370 0.0243  -0.2300 419 ALA A C   
3253 O O   . ALA A 419 ? 0.4840 0.6039 0.8135 -0.1319 0.0045  -0.2243 419 ALA A O   
3254 C CB  . ALA A 419 ? 0.3660 0.5153 0.7739 -0.1268 0.0049  -0.2186 419 ALA A CB  
3255 N N   . TRP A 420 ? 0.4228 0.4998 0.7836 -0.1391 0.0490  -0.2292 420 TRP A N   
3256 C CA  . TRP A 420 ? 0.4641 0.5171 0.7884 -0.1370 0.0537  -0.2241 420 TRP A CA  
3257 C C   . TRP A 420 ? 0.4278 0.5014 0.7353 -0.1419 0.0386  -0.2433 420 TRP A C   
3258 O O   . TRP A 420 ? 0.4697 0.5330 0.7442 -0.1397 0.0369  -0.2406 420 TRP A O   
3259 C CB  . TRP A 420 ? 0.4328 0.4474 0.7617 -0.1354 0.0822  -0.2158 420 TRP A CB  
3260 C CG  . TRP A 420 ? 0.4570 0.4728 0.8060 -0.1418 0.0922  -0.2344 420 TRP A CG  
3261 C CD1 . TRP A 420 ? 0.4652 0.4911 0.8512 -0.1481 0.1004  -0.2469 420 TRP A CD1 
3262 C CD2 . TRP A 420 ? 0.4712 0.4771 0.8075 -0.1427 0.0968  -0.2434 420 TRP A CD2 
3263 N NE1 . TRP A 420 ? 0.4530 0.4752 0.8493 -0.1534 0.1091  -0.2633 420 TRP A NE1 
3264 C CE2 . TRP A 420 ? 0.4755 0.4857 0.8424 -0.1500 0.1074  -0.2614 420 TRP A CE2 
3265 C CE3 . TRP A 420 ? 0.4641 0.4587 0.7690 -0.1382 0.0941  -0.2390 420 TRP A CE3 
3266 C CZ2 . TRP A 420 ? 0.4878 0.4912 0.8554 -0.1527 0.1155  -0.2751 420 TRP A CZ2 
3267 C CZ3 . TRP A 420 ? 0.4488 0.4377 0.7554 -0.1404 0.1026  -0.2526 420 TRP A CZ3 
3268 C CH2 . TRP A 420 ? 0.4372 0.4303 0.7750 -0.1476 0.1131  -0.2705 420 TRP A CH2 
3269 N N   . GLU A 421 ? 0.4319 0.5342 0.7603 -0.1486 0.0286  -0.2629 421 GLU A N   
3270 C CA  . GLU A 421 ? 0.4490 0.5730 0.7567 -0.1538 0.0129  -0.2813 421 GLU A CA  
3271 C C   . GLU A 421 ? 0.5427 0.7066 0.8418 -0.1538 -0.0190 -0.2844 421 GLU A C   
3272 O O   . GLU A 421 ? 0.5381 0.7235 0.8194 -0.1589 -0.0344 -0.2994 421 GLU A O   
3273 C CB  . GLU A 421 ? 0.4882 0.6120 0.8215 -0.1621 0.0259  -0.3027 421 GLU A CB  
3274 C CG  . GLU A 421 ? 0.5784 0.6684 0.9072 -0.1614 0.0509  -0.3025 421 GLU A CG  
3275 C CD  . GLU A 421 ? 0.4976 0.5891 0.8523 -0.1698 0.0629  -0.3252 421 GLU A CD  
3276 O OE1 . GLU A 421 ? 0.5737 0.6727 0.9652 -0.1745 0.0676  -0.3327 421 GLU A OE1 
3277 O OE2 . GLU A 421 ? 0.5564 0.6421 0.8968 -0.1720 0.0687  -0.3366 421 GLU A OE2 
3278 N N   . SER A 422 ? 0.4914 0.6651 0.8025 -0.1475 -0.0294 -0.2695 422 SER A N   
3279 C CA  . SER A 422 ? 0.5576 0.7689 0.8628 -0.1442 -0.0617 -0.2677 422 SER A CA  
3280 C C   . SER A 422 ? 0.5445 0.7603 0.7941 -0.1412 -0.0787 -0.2605 422 SER A C   
3281 O O   . SER A 422 ? 0.5661 0.7579 0.7898 -0.1338 -0.0696 -0.2417 422 SER A O   
3282 C CB  . SER A 422 ? 0.5693 0.7876 0.9056 -0.1359 -0.0657 -0.2523 422 SER A CB  
3283 O OG  . SER A 422 ? 0.6605 0.8803 1.0471 -0.1391 -0.0511 -0.2601 422 SER A OG  
3284 N N   . PRO A 423 ? 0.5972 0.8382 0.8205 -0.1444 -0.1007 -0.2695 423 PRO A N   
3285 C CA  . PRO A 423 ? 0.6621 0.9052 0.8265 -0.1419 -0.1136 -0.2607 423 PRO A CA  
3286 C C   . PRO A 423 ? 0.6858 0.9375 0.8327 -0.1292 -0.1332 -0.2339 423 PRO A C   
3287 O O   . PRO A 423 ? 0.7199 0.9631 0.8150 -0.1244 -0.1374 -0.2178 423 PRO A O   
3288 C CB  . PRO A 423 ? 0.6432 0.9095 0.7868 -0.1491 -0.1309 -0.2763 423 PRO A CB  
3289 C CG  . PRO A 423 ? 0.5705 0.8591 0.7638 -0.1511 -0.1414 -0.2857 423 PRO A CG  
3290 C CD  . PRO A 423 ? 0.5811 0.8485 0.8247 -0.1512 -0.1137 -0.2877 423 PRO A CD  
3291 N N   . GLU A 424 ? 0.7293 0.9908 0.9157 -0.1207 -0.1412 -0.2228 424 GLU A N   
3292 C CA  . GLU A 424 ? 0.6828 0.9417 0.8530 -0.1041 -0.1547 -0.1908 424 GLU A CA  
3293 C C   . GLU A 424 ? 0.6868 0.9055 0.8490 -0.0947 -0.1298 -0.1683 424 GLU A C   
3294 O O   . GLU A 424 ? 0.6989 0.9081 0.8377 -0.0824 -0.1371 -0.1422 424 GLU A O   
3295 C CB  . GLU A 424 ? 0.7009 0.9890 0.9205 -0.0976 -0.1742 -0.1896 424 GLU A CB  
3296 C CG  . GLU A 424 ? 0.6545 0.9326 0.9333 -0.0975 -0.1515 -0.1949 424 GLU A CG  
3297 C CD  . GLU A 424 ? 0.7960 1.0894 1.1179 -0.1144 -0.1428 -0.2283 424 GLU A CD  
3298 O OE1 . GLU A 424 ? 0.7897 1.0862 1.0845 -0.1244 -0.1455 -0.2433 424 GLU A OE1 
3299 O OE2 . GLU A 424 ? 0.9229 1.2157 1.2975 -0.1153 -0.1277 -0.2333 424 GLU A OE2 
3300 N N   . GLY A 425 ? 0.5338 0.7280 0.7141 -0.1004 -0.1015 -0.1775 425 GLY A N   
3301 C CA  . GLY A 425 ? 0.4985 0.6560 0.6699 -0.0922 -0.0797 -0.1575 425 GLY A CA  
3302 C C   . GLY A 425 ? 0.4624 0.6148 0.6720 -0.0847 -0.0725 -0.1479 425 GLY A C   
3303 O O   . GLY A 425 ? 0.4106 0.5888 0.6590 -0.0845 -0.0839 -0.1554 425 GLY A O   
3304 N N   . VAL A 426 ? 0.3257 0.4449 0.5246 -0.0787 -0.0527 -0.1319 426 VAL A N   
3305 C CA  . VAL A 426 ? 0.3514 0.4605 0.5773 -0.0716 -0.0418 -0.1219 426 VAL A CA  
3306 C C   . VAL A 426 ? 0.3652 0.4605 0.5623 -0.0585 -0.0480 -0.0975 426 VAL A C   
3307 O O   . VAL A 426 ? 0.3757 0.4564 0.5316 -0.0568 -0.0495 -0.0870 426 VAL A O   
3308 C CB  . VAL A 426 ? 0.3861 0.4666 0.6242 -0.0769 -0.0120 -0.1252 426 VAL A CB  
3309 C CG1 . VAL A 426 ? 0.3656 0.4575 0.6374 -0.0908 -0.0044 -0.1497 426 VAL A CG1 
3310 C CG2 . VAL A 426 ? 0.3579 0.4069 0.5539 -0.0747 -0.0012 -0.1130 426 VAL A CG2 
3311 N N   . PRO A 427 ? 0.3839 0.4836 0.6047 -0.0495 -0.0508 -0.0892 427 PRO A N   
3312 C CA  . PRO A 427 ? 0.3338 0.4192 0.5306 -0.0376 -0.0568 -0.0677 427 PRO A CA  
3313 C C   . PRO A 427 ? 0.3576 0.4073 0.5370 -0.0358 -0.0336 -0.0586 427 PRO A C   
3314 O O   . PRO A 427 ? 0.3898 0.4294 0.5916 -0.0375 -0.0144 -0.0637 427 PRO A O   
3315 C CB  . PRO A 427 ? 0.3720 0.4778 0.6096 -0.0287 -0.0680 -0.0663 427 PRO A CB  
3316 C CG  . PRO A 427 ? 0.3792 0.4973 0.6642 -0.0362 -0.0539 -0.0855 427 PRO A CG  
3317 C CD  . PRO A 427 ? 0.3681 0.4889 0.6434 -0.0502 -0.0494 -0.1011 427 PRO A CD  
3318 N N   . ILE A 428 ? 0.3600 0.3914 0.4985 -0.0332 -0.0357 -0.0451 428 ILE A N   
3319 C CA  . ILE A 428 ? 0.3351 0.3350 0.4526 -0.0319 -0.0182 -0.0365 428 ILE A CA  
3320 C C   . ILE A 428 ? 0.3632 0.3523 0.4813 -0.0222 -0.0190 -0.0245 428 ILE A C   
3321 O O   . ILE A 428 ? 0.4025 0.3972 0.5125 -0.0161 -0.0351 -0.0143 428 ILE A O   
3322 C CB  . ILE A 428 ? 0.4084 0.3968 0.4879 -0.0350 -0.0195 -0.0309 428 ILE A CB  
3323 C CG1 . ILE A 428 ? 0.3952 0.3930 0.4775 -0.0442 -0.0167 -0.0454 428 ILE A CG1 
3324 C CG2 . ILE A 428 ? 0.3610 0.3202 0.4207 -0.0331 -0.0055 -0.0219 428 ILE A CG2 
3325 C CD1 . ILE A 428 ? 0.3690 0.3558 0.4725 -0.0492 0.0025  -0.0552 428 ILE A CD1 
3326 N N   . GLU A 429 ? 0.3217 0.2936 0.4485 -0.0213 -0.0005 -0.0258 429 GLU A N   
3327 C CA  . GLU A 429 ? 0.3772 0.3351 0.5042 -0.0133 0.0030  -0.0182 429 GLU A CA  
3328 C C   . GLU A 429 ? 0.4612 0.3892 0.5531 -0.0143 0.0146  -0.0113 429 GLU A C   
3329 O O   . GLU A 429 ? 0.4164 0.3304 0.5035 -0.0089 0.0173  -0.0066 429 GLU A O   
3330 C CB  . GLU A 429 ? 0.4362 0.4008 0.6037 -0.0111 0.0158  -0.0277 429 GLU A CB  
3331 C CG  . GLU A 429 ? 0.4185 0.4166 0.6288 -0.0091 0.0020  -0.0353 429 GLU A CG  
3332 C CD  . GLU A 429 ? 0.4520 0.4587 0.7092 -0.0065 0.0161  -0.0454 429 GLU A CD  
3333 O OE1 . GLU A 429 ? 0.4838 0.4750 0.7438 0.0001  0.0269  -0.0424 429 GLU A OE1 
3334 O OE2 . GLU A 429 ? 0.4056 0.4351 0.6988 -0.0120 0.0178  -0.0582 429 GLU A OE2 
3335 N N   . GLY A 430 ? 0.3874 0.3055 0.4565 -0.0207 0.0204  -0.0114 430 GLY A N   
3336 C CA  . GLY A 430 ? 0.4776 0.3710 0.5140 -0.0214 0.0272  -0.0046 430 GLY A CA  
3337 C C   . GLY A 430 ? 0.3933 0.2835 0.4089 -0.0258 0.0243  -0.0020 430 GLY A C   
3338 O O   . GLY A 430 ? 0.3933 0.2924 0.4200 -0.0301 0.0268  -0.0084 430 GLY A O   
3339 N N   . ILE A 431 ? 0.4114 0.2897 0.4012 -0.0249 0.0195  0.0060  431 ILE A N   
3340 C CA  . ILE A 431 ? 0.4291 0.3051 0.4036 -0.0277 0.0170  0.0085  431 ILE A CA  
3341 C C   . ILE A 431 ? 0.4278 0.2824 0.3807 -0.0272 0.0229  0.0140  431 ILE A C   
3342 O O   . ILE A 431 ? 0.4762 0.3204 0.4166 -0.0255 0.0219  0.0171  431 ILE A O   
3343 C CB  . ILE A 431 ? 0.4318 0.3186 0.3984 -0.0280 0.0038  0.0128  431 ILE A CB  
3344 C CG1 . ILE A 431 ? 0.4501 0.3584 0.4312 -0.0288 -0.0041 0.0085  431 ILE A CG1 
3345 C CG2 . ILE A 431 ? 0.3603 0.2460 0.3165 -0.0306 0.0036  0.0137  431 ILE A CG2 
3346 C CD1 . ILE A 431 ? 0.4783 0.3954 0.4464 -0.0296 -0.0156 0.0150  431 ILE A CD1 
3347 N N   . ILE A 432 ? 0.4247 0.2724 0.3734 -0.0286 0.0283  0.0148  432 ILE A N   
3348 C CA  . ILE A 432 ? 0.4760 0.3041 0.4025 -0.0274 0.0319  0.0218  432 ILE A CA  
3349 C C   . ILE A 432 ? 0.4653 0.2956 0.3861 -0.0263 0.0227  0.0264  432 ILE A C   
3350 O O   . ILE A 432 ? 0.4822 0.3209 0.4179 -0.0269 0.0233  0.0233  432 ILE A O   
3351 C CB  . ILE A 432 ? 0.5015 0.3154 0.4282 -0.0287 0.0472  0.0223  432 ILE A CB  
3352 C CG1 . ILE A 432 ? 0.4290 0.2452 0.3701 -0.0306 0.0586  0.0153  432 ILE A CG1 
3353 C CG2 . ILE A 432 ? 0.4564 0.2488 0.3525 -0.0271 0.0489  0.0320  432 ILE A CG2 
3354 C CD1 . ILE A 432 ? 0.4769 0.2810 0.4236 -0.0340 0.0770  0.0147  432 ILE A CD1 
3355 N N   . PHE A 433 ? 0.4149 0.2389 0.3175 -0.0250 0.0147  0.0318  433 PHE A N   
3356 C CA  . PHE A 433 ? 0.4157 0.2418 0.3161 -0.0232 0.0061  0.0366  433 PHE A CA  
3357 C C   . PHE A 433 ? 0.4761 0.2842 0.3559 -0.0202 0.0059  0.0448  433 PHE A C   
3358 O O   . PHE A 433 ? 0.4672 0.2610 0.3273 -0.0211 0.0118  0.0461  433 PHE A O   
3359 C CB  . PHE A 433 ? 0.4195 0.2555 0.3184 -0.0250 -0.0051 0.0363  433 PHE A CB  
3360 C CG  . PHE A 433 ? 0.4154 0.2674 0.3286 -0.0279 -0.0057 0.0318  433 PHE A CG  
3361 C CD1 . PHE A 433 ? 0.4190 0.2842 0.3475 -0.0286 -0.0034 0.0279  433 PHE A CD1 
3362 C CD2 . PHE A 433 ? 0.4066 0.2592 0.3163 -0.0299 -0.0085 0.0317  433 PHE A CD2 
3363 C CE1 . PHE A 433 ? 0.3842 0.2642 0.3187 -0.0320 -0.0046 0.0244  433 PHE A CE1 
3364 C CE2 . PHE A 433 ? 0.4532 0.3188 0.3715 -0.0321 -0.0104 0.0310  433 PHE A CE2 
3365 C CZ  . PHE A 433 ? 0.3948 0.2749 0.3226 -0.0335 -0.0089 0.0275  433 PHE A CZ  
3366 N N   . GLY A 434 ? 0.4601 0.2692 0.3444 -0.0164 -0.0009 0.0504  434 GLY A N   
3367 C CA  . GLY A 434 ? 0.4659 0.2590 0.3289 -0.0123 -0.0053 0.0612  434 GLY A CA  
3368 C C   . GLY A 434 ? 0.5059 0.3009 0.3846 -0.0058 -0.0117 0.0682  434 GLY A C   
3369 O O   . GLY A 434 ? 0.4985 0.3027 0.4053 -0.0050 -0.0064 0.0632  434 GLY A O   
3370 N N   . GLY A 435 ? 0.5006 0.2876 0.3618 -0.0009 -0.0238 0.0792  435 GLY A N   
3371 C CA  . GLY A 435 ? 0.4648 0.2526 0.3436 0.0077  -0.0319 0.0881  435 GLY A CA  
3372 C C   . GLY A 435 ? 0.6014 0.3707 0.4507 0.0138  -0.0416 0.1050  435 GLY A C   
3373 O O   . GLY A 435 ? 0.6470 0.4008 0.4581 0.0100  -0.0386 0.1087  435 GLY A O   
3374 N N   . ARG A 436 ? 0.5509 0.3217 0.4172 0.0237  -0.0534 0.1155  436 ARG A N   
3375 C CA  . ARG A 436 ? 0.5995 0.3533 0.4374 0.0314  -0.0666 0.1349  436 ARG A CA  
3376 C C   . ARG A 436 ? 0.6538 0.4233 0.4752 0.0307  -0.0906 0.1337  436 ARG A C   
3377 O O   . ARG A 436 ? 0.6491 0.4406 0.5016 0.0356  -0.1068 0.1316  436 ARG A O   
3378 C CB  . ARG A 436 ? 0.5681 0.3159 0.4362 0.0439  -0.0699 0.1479  436 ARG A CB  
3379 C CG  . ARG A 436 ? 0.6351 0.3590 0.5114 0.0441  -0.0466 0.1520  436 ARG A CG  
3380 C CD  . ARG A 436 ? 0.5794 0.2991 0.4975 0.0561  -0.0474 0.1597  436 ARG A CD  
3381 N NE  . ARG A 436 ? 0.6513 0.3465 0.5797 0.0545  -0.0238 0.1616  436 ARG A NE  
3382 C CZ  . ARG A 436 ? 0.7182 0.3801 0.6231 0.0579  -0.0172 0.1822  436 ARG A CZ  
3383 N NH1 . ARG A 436 ? 0.8234 0.4809 0.6950 0.0623  -0.0335 0.2018  436 ARG A NH1 
3384 N NH2 . ARG A 436 ? 0.7324 0.3811 0.6547 0.0518  0.0038  0.1763  436 ARG A NH2 
3385 N N   . ARG A 437 ? 0.6572 0.4163 0.4321 0.0237  -0.0917 0.1330  437 ARG A N   
3386 C CA  . ARG A 437 ? 0.6667 0.4372 0.4193 0.0213  -0.1144 0.1304  437 ARG A CA  
3387 C C   . ARG A 437 ? 0.6893 0.4369 0.3864 0.0238  -0.1224 0.1466  437 ARG A C   
3388 O O   . ARG A 437 ? 0.6739 0.4010 0.3308 0.0167  -0.1059 0.1453  437 ARG A O   
3389 C CB  . ARG A 437 ? 0.6033 0.3828 0.3495 0.0088  -0.1084 0.1104  437 ARG A CB  
3390 C CG  . ARG A 437 ? 0.5700 0.3711 0.3635 0.0052  -0.1016 0.0962  437 ARG A CG  
3391 C CD  . ARG A 437 ? 0.6688 0.4955 0.5013 0.0099  -0.1198 0.0956  437 ARG A CD  
3392 N NE  . ARG A 437 ? 0.5401 0.3773 0.3586 0.0082  -0.1439 0.0944  437 ARG A NE  
3393 C CZ  . ARG A 437 ? 0.5332 0.3847 0.3567 -0.0017 -0.1499 0.0797  437 ARG A CZ  
3394 N NH1 . ARG A 437 ? 0.5003 0.3550 0.3386 -0.0101 -0.1336 0.0675  437 ARG A NH1 
3395 N NH2 . ARG A 437 ? 0.5791 0.4415 0.3930 -0.0036 -0.1737 0.0775  437 ARG A NH2 
3396 N N   . PRO A 438 ? 0.7419 0.4935 0.4355 0.0338  -0.1463 0.1618  438 PRO A N   
3397 C CA  . PRO A 438 ? 0.7657 0.5077 0.4159 0.0358  -0.1475 0.1743  438 PRO A CA  
3398 C C   . PRO A 438 ? 0.8064 0.5528 0.4116 0.0256  -0.1566 0.1624  438 PRO A C   
3399 O O   . PRO A 438 ? 0.8355 0.5704 0.3970 0.0240  -0.1516 0.1694  438 PRO A O   
3400 C CB  . PRO A 438 ? 0.7810 0.5361 0.4559 0.0507  -0.1694 0.1910  438 PRO A CB  
3401 C CG  . PRO A 438 ? 0.7016 0.4824 0.4246 0.0525  -0.1879 0.1796  438 PRO A CG  
3402 C CD  . PRO A 438 ? 0.7330 0.5083 0.4757 0.0439  -0.1675 0.1650  438 PRO A CD  
3403 N N   . ALA A 439 ? 0.7715 0.5335 0.3862 0.0179  -0.1689 0.1441  439 ALA A N   
3404 C CA  . ALA A 439 ? 0.7947 0.5609 0.3711 0.0075  -0.1778 0.1296  439 ALA A CA  
3405 C C   . ALA A 439 ? 0.7296 0.4972 0.3140 -0.0045 -0.1719 0.1081  439 ALA A C   
3406 O O   . ALA A 439 ? 0.7428 0.5258 0.3808 -0.0036 -0.1650 0.1017  439 ALA A O   
3407 C CB  . ALA A 439 ? 0.7673 0.5592 0.3485 0.0117  -0.2105 0.1308  439 ALA A CB  
3408 N N   . GLY A 440 ? 0.7312 0.4909 0.2766 -0.0156 -0.1666 0.0929  440 GLY A N   
3409 C CA  . GLY A 440 ? 0.7043 0.4706 0.2641 -0.0272 -0.1594 0.0689  440 GLY A CA  
3410 C C   . GLY A 440 ? 0.7690 0.5242 0.3454 -0.0310 -0.1277 0.0603  440 GLY A C   
3411 O O   . GLY A 440 ? 0.7717 0.5203 0.3365 -0.0403 -0.1169 0.0427  440 GLY A O   
3412 N N   . VAL A 441 ? 0.7131 0.4669 0.3192 -0.0238 -0.1135 0.0715  441 VAL A N   
3413 C CA  . VAL A 441 ? 0.6743 0.4247 0.3059 -0.0265 -0.0883 0.0634  441 VAL A CA  
3414 C C   . VAL A 441 ? 0.6615 0.3869 0.2582 -0.0279 -0.0652 0.0666  441 VAL A C   
3415 O O   . VAL A 441 ? 0.6596 0.3724 0.2402 -0.0222 -0.0612 0.0833  441 VAL A O   
3416 C CB  . VAL A 441 ? 0.6488 0.4126 0.3302 -0.0198 -0.0850 0.0704  441 VAL A CB  
3417 C CG1 . VAL A 441 ? 0.6081 0.3721 0.3143 -0.0233 -0.0636 0.0610  441 VAL A CG1 
3418 C CG2 . VAL A 441 ? 0.6409 0.4298 0.3559 -0.0185 -0.1061 0.0682  441 VAL A CG2 
3419 N N   . PRO A 442 ? 0.6890 0.4059 0.2763 -0.0351 -0.0483 0.0513  442 PRO A N   
3420 C CA  . PRO A 442 ? 0.7494 0.4442 0.3054 -0.0374 -0.0240 0.0521  442 PRO A CA  
3421 C C   . PRO A 442 ? 0.6973 0.3897 0.2828 -0.0330 -0.0050 0.0609  442 PRO A C   
3422 O O   . PRO A 442 ? 0.6478 0.3552 0.2764 -0.0285 -0.0097 0.0643  442 PRO A O   
3423 C CB  . PRO A 442 ? 0.7363 0.4277 0.2902 -0.0451 -0.0120 0.0304  442 PRO A CB  
3424 C CG  . PRO A 442 ? 0.6740 0.3847 0.2713 -0.0455 -0.0248 0.0220  442 PRO A CG  
3425 C CD  . PRO A 442 ? 0.6749 0.4006 0.2791 -0.0418 -0.0507 0.0324  442 PRO A CD  
3426 N N   . LEU A 443 ? 0.7015 0.3748 0.2625 -0.0356 0.0182  0.0629  443 LEU A N   
3427 C CA  . LEU A 443 ? 0.6727 0.3412 0.2578 -0.0331 0.0372  0.0714  443 LEU A CA  
3428 C C   . LEU A 443 ? 0.6397 0.3255 0.2789 -0.0330 0.0449  0.0595  443 LEU A C   
3429 O O   . LEU A 443 ? 0.6549 0.3484 0.3283 -0.0295 0.0469  0.0651  443 LEU A O   
3430 C CB  . LEU A 443 ? 0.7337 0.3789 0.2825 -0.0383 0.0631  0.0736  443 LEU A CB  
3431 C CG  . LEU A 443 ? 0.7402 0.3789 0.3146 -0.0387 0.0876  0.0792  443 LEU A CG  
3432 C CD1 . LEU A 443 ? 0.7489 0.3846 0.3336 -0.0324 0.0790  0.0989  443 LEU A CD1 
3433 C CD2 . LEU A 443 ? 0.8274 0.4458 0.3682 -0.0459 0.1162  0.0770  443 LEU A CD2 
3434 N N   . VAL A 444 ? 0.5988 0.2900 0.2457 -0.0366 0.0487  0.0431  444 VAL A N   
3435 C CA  . VAL A 444 ? 0.6256 0.3324 0.3202 -0.0356 0.0540  0.0337  444 VAL A CA  
3436 C C   . VAL A 444 ? 0.5928 0.3029 0.2901 -0.0381 0.0499  0.0191  444 VAL A C   
3437 O O   . VAL A 444 ? 0.6804 0.3769 0.3465 -0.0423 0.0565  0.0106  444 VAL A O   
3438 C CB  . VAL A 444 ? 0.6206 0.3237 0.3332 -0.0367 0.0790  0.0315  444 VAL A CB  
3439 C CG1 . VAL A 444 ? 0.6964 0.3818 0.3782 -0.0417 0.0995  0.0239  444 VAL A CG1 
3440 C CG2 . VAL A 444 ? 0.5354 0.2576 0.2973 -0.0348 0.0799  0.0227  444 VAL A CG2 
3441 N N   . TYR A 445 ? 0.5847 0.3110 0.3177 -0.0361 0.0398  0.0163  445 TYR A N   
3442 C CA  . TYR A 445 ? 0.5896 0.3169 0.3353 -0.0377 0.0396  0.0040  445 TYR A CA  
3443 C C   . TYR A 445 ? 0.5438 0.2868 0.3336 -0.0339 0.0387  0.0048  445 TYR A C   
3444 O O   . TYR A 445 ? 0.5483 0.3037 0.3559 -0.0314 0.0352  0.0127  445 TYR A O   
3445 C CB  . TYR A 445 ? 0.5813 0.3080 0.3112 -0.0414 0.0218  0.0003  445 TYR A CB  
3446 C CG  . TYR A 445 ? 0.5558 0.2987 0.3015 -0.0402 0.0025  0.0091  445 TYR A CG  
3447 C CD1 . TYR A 445 ? 0.5743 0.3202 0.3040 -0.0387 -0.0087 0.0189  445 TYR A CD1 
3448 C CD2 . TYR A 445 ? 0.5888 0.3432 0.3657 -0.0404 -0.0037 0.0079  445 TYR A CD2 
3449 C CE1 . TYR A 445 ? 0.5218 0.2842 0.2714 -0.0373 -0.0243 0.0250  445 TYR A CE1 
3450 C CE2 . TYR A 445 ? 0.5574 0.3271 0.3489 -0.0405 -0.0178 0.0145  445 TYR A CE2 
3451 C CZ  . TYR A 445 ? 0.5810 0.3557 0.3611 -0.0388 -0.0276 0.0217  445 TYR A CZ  
3452 O OH  . TYR A 445 ? 0.6120 0.4035 0.4121 -0.0385 -0.0397 0.0265  445 TYR A OH  
3453 N N   . GLU A 446 ? 0.5831 0.3246 0.3898 -0.0334 0.0419  -0.0038 446 GLU A N   
3454 C CA  . GLU A 446 ? 0.5765 0.3312 0.4216 -0.0291 0.0401  -0.0020 446 GLU A CA  
3455 C C   . GLU A 446 ? 0.4882 0.2444 0.3416 -0.0302 0.0266  -0.0010 446 GLU A C   
3456 O O   . GLU A 446 ? 0.5427 0.2859 0.3827 -0.0339 0.0256  -0.0085 446 GLU A O   
3457 C CB  . GLU A 446 ? 0.5741 0.3252 0.4393 -0.0257 0.0565  -0.0105 446 GLU A CB  
3458 C CG  . GLU A 446 ? 0.5407 0.3061 0.4460 -0.0197 0.0518  -0.0077 446 GLU A CG  
3459 C CD  . GLU A 446 ? 0.6057 0.3687 0.5368 -0.0150 0.0666  -0.0170 446 GLU A CD  
3460 O OE1 . GLU A 446 ? 0.6257 0.3833 0.5505 -0.0167 0.0842  -0.0244 446 GLU A OE1 
3461 O OE2 . GLU A 446 ? 0.5860 0.3518 0.5448 -0.0092 0.0614  -0.0163 446 GLU A OE2 
3462 N N   . ALA A 447 ? 0.4836 0.2549 0.3580 -0.0282 0.0173  0.0075  447 ALA A N   
3463 C CA  . ALA A 447 ? 0.5088 0.2810 0.3912 -0.0302 0.0068  0.0110  447 ALA A CA  
3464 C C   . ALA A 447 ? 0.5449 0.3053 0.4436 -0.0274 0.0116  0.0068  447 ALA A C   
3465 O O   . ALA A 447 ? 0.5458 0.3053 0.4599 -0.0216 0.0209  0.0034  447 ALA A O   
3466 C CB  . ALA A 447 ? 0.4958 0.2864 0.3924 -0.0292 -0.0015 0.0214  447 ALA A CB  
3467 N N   . LEU A 448 ? 0.5441 0.2953 0.4434 -0.0315 0.0059  0.0068  448 LEU A N   
3468 C CA  . LEU A 448 ? 0.5393 0.2748 0.4560 -0.0288 0.0105  0.0033  448 LEU A CA  
3469 C C   . LEU A 448 ? 0.5696 0.3121 0.5122 -0.0221 0.0056  0.0168  448 LEU A C   
3470 O O   . LEU A 448 ? 0.5330 0.2648 0.4967 -0.0157 0.0100  0.0162  448 LEU A O   
3471 C CB  . LEU A 448 ? 0.5201 0.2406 0.4294 -0.0373 0.0069  -0.0024 448 LEU A CB  
3472 C CG  . LEU A 448 ? 0.6109 0.3257 0.4915 -0.0451 0.0071  -0.0161 448 LEU A CG  
3473 C CD1 . LEU A 448 ? 0.5541 0.2622 0.4331 -0.0551 -0.0011 -0.0203 448 LEU A CD1 
3474 C CD2 . LEU A 448 ? 0.6564 0.3553 0.5282 -0.0433 0.0212  -0.0316 448 LEU A CD2 
3475 N N   . SER A 449 ? 0.5055 0.2656 0.4464 -0.0230 -0.0034 0.0287  449 SER A N   
3476 C CA  . SER A 449 ? 0.5207 0.2886 0.4775 -0.0180 -0.0104 0.0430  449 SER A CA  
3477 C C   . SER A 449 ? 0.5072 0.2977 0.4546 -0.0206 -0.0170 0.0497  449 SER A C   
3478 O O   . SER A 449 ? 0.4837 0.2816 0.4177 -0.0249 -0.0154 0.0437  449 SER A O   
3479 C CB  . SER A 449 ? 0.5646 0.3165 0.5261 -0.0211 -0.0136 0.0515  449 SER A CB  
3480 O OG  . SER A 449 ? 0.5782 0.3320 0.5244 -0.0318 -0.0163 0.0523  449 SER A OG  
3481 N N   . TRP A 450 ? 0.5447 0.3452 0.4984 -0.0176 -0.0244 0.0623  450 TRP A N   
3482 C CA  . TRP A 450 ? 0.5249 0.3461 0.4681 -0.0212 -0.0294 0.0665  450 TRP A CA  
3483 C C   . TRP A 450 ? 0.4290 0.2497 0.3577 -0.0309 -0.0288 0.0679  450 TRP A C   
3484 O O   . TRP A 450 ? 0.4440 0.2781 0.3653 -0.0346 -0.0279 0.0631  450 TRP A O   
3485 C CB  . TRP A 450 ? 0.4691 0.3008 0.4167 -0.0167 -0.0385 0.0794  450 TRP A CB  
3486 C CG  . TRP A 450 ? 0.4628 0.3160 0.3973 -0.0213 -0.0421 0.0803  450 TRP A CG  
3487 C CD1 . TRP A 450 ? 0.4859 0.3440 0.4040 -0.0276 -0.0446 0.0897  450 TRP A CD1 
3488 C CD2 . TRP A 450 ? 0.4297 0.3010 0.3669 -0.0210 -0.0414 0.0696  450 TRP A CD2 
3489 N NE1 . TRP A 450 ? 0.4613 0.3403 0.3709 -0.0309 -0.0454 0.0840  450 TRP A NE1 
3490 C CE2 . TRP A 450 ? 0.4600 0.3467 0.3824 -0.0268 -0.0441 0.0715  450 TRP A CE2 
3491 C CE3 . TRP A 450 ? 0.4566 0.3314 0.4080 -0.0172 -0.0367 0.0581  450 TRP A CE3 
3492 C CZ2 . TRP A 450 ? 0.4415 0.3460 0.3647 -0.0286 -0.0432 0.0609  450 TRP A CZ2 
3493 C CZ3 . TRP A 450 ? 0.4716 0.3635 0.4243 -0.0194 -0.0358 0.0497  450 TRP A CZ3 
3494 C CH2 . TRP A 450 ? 0.4734 0.3796 0.4131 -0.0249 -0.0395 0.0504  450 TRP A CH2 
3495 N N   . GLN A 451 ? 0.4501 0.2554 0.3791 -0.0351 -0.0284 0.0738  451 GLN A N   
3496 C CA  . GLN A 451 ? 0.5026 0.3096 0.4242 -0.0453 -0.0272 0.0747  451 GLN A CA  
3497 C C   . GLN A 451 ? 0.4688 0.2758 0.3877 -0.0491 -0.0255 0.0609  451 GLN A C   
3498 O O   . GLN A 451 ? 0.4280 0.2477 0.3440 -0.0545 -0.0261 0.0586  451 GLN A O   
3499 C CB  . GLN A 451 ? 0.5416 0.3303 0.4676 -0.0501 -0.0259 0.0843  451 GLN A CB  
3500 C CG  . GLN A 451 ? 0.6024 0.3898 0.5261 -0.0469 -0.0290 0.1027  451 GLN A CG  
3501 C CD  . GLN A 451 ? 0.6762 0.4552 0.6114 -0.0345 -0.0334 0.1068  451 GLN A CD  
3502 O OE1 . GLN A 451 ? 0.6292 0.3942 0.5774 -0.0303 -0.0302 0.0972  451 GLN A OE1 
3503 N NE2 . GLN A 451 ? 0.6632 0.4522 0.5943 -0.0286 -0.0408 0.1201  451 GLN A NE2 
3504 N N   . HIS A 452 ? 0.4636 0.2567 0.3831 -0.0460 -0.0235 0.0518  452 HIS A N   
3505 C CA  . HIS A 452 ? 0.4282 0.2214 0.3382 -0.0488 -0.0238 0.0402  452 HIS A CA  
3506 C C   . HIS A 452 ? 0.4558 0.2646 0.3600 -0.0448 -0.0238 0.0389  452 HIS A C   
3507 O O   . HIS A 452 ? 0.4602 0.2760 0.3583 -0.0474 -0.0269 0.0354  452 HIS A O   
3508 C CB  . HIS A 452 ? 0.4498 0.2237 0.3561 -0.0471 -0.0195 0.0298  452 HIS A CB  
3509 C CG  . HIS A 452 ? 0.5197 0.2924 0.4088 -0.0502 -0.0211 0.0190  452 HIS A CG  
3510 N ND1 . HIS A 452 ? 0.5372 0.3046 0.4133 -0.0458 -0.0153 0.0123  452 HIS A ND1 
3511 C CD2 . HIS A 452 ? 0.4665 0.2435 0.3488 -0.0573 -0.0286 0.0148  452 HIS A CD2 
3512 C CE1 . HIS A 452 ? 0.5072 0.2736 0.3639 -0.0498 -0.0198 0.0060  452 HIS A CE1 
3513 N NE2 . HIS A 452 ? 0.4605 0.2341 0.3223 -0.0563 -0.0294 0.0070  452 HIS A NE2 
3514 N N   . GLY A 453 ? 0.4263 0.2407 0.3352 -0.0384 -0.0210 0.0416  453 GLY A N   
3515 C CA  . GLY A 453 ? 0.4135 0.2406 0.3203 -0.0358 -0.0195 0.0394  453 GLY A CA  
3516 C C   . GLY A 453 ? 0.4338 0.2774 0.3420 -0.0393 -0.0225 0.0426  453 GLY A C   
3517 O O   . GLY A 453 ? 0.4253 0.2753 0.3319 -0.0390 -0.0219 0.0394  453 GLY A O   
3518 N N   . VAL A 454 ? 0.4274 0.2769 0.3387 -0.0425 -0.0245 0.0494  454 VAL A N   
3519 C CA  . VAL A 454 ? 0.4177 0.2828 0.3299 -0.0473 -0.0242 0.0506  454 VAL A CA  
3520 C C   . VAL A 454 ? 0.4165 0.2818 0.3317 -0.0518 -0.0256 0.0470  454 VAL A C   
3521 O O   . VAL A 454 ? 0.3821 0.2600 0.3030 -0.0523 -0.0249 0.0436  454 VAL A O   
3522 C CB  . VAL A 454 ? 0.4716 0.3404 0.3809 -0.0511 -0.0243 0.0599  454 VAL A CB  
3523 C CG1 . VAL A 454 ? 0.3975 0.2817 0.3066 -0.0577 -0.0203 0.0594  454 VAL A CG1 
3524 C CG2 . VAL A 454 ? 0.4400 0.3132 0.3467 -0.0457 -0.0270 0.0634  454 VAL A CG2 
3525 N N   . PHE A 455 ? 0.4376 0.2897 0.3522 -0.0549 -0.0282 0.0465  455 PHE A N   
3526 C CA  . PHE A 455 ? 0.4141 0.2688 0.3332 -0.0595 -0.0326 0.0414  455 PHE A CA  
3527 C C   . PHE A 455 ? 0.3999 0.2557 0.3131 -0.0539 -0.0364 0.0365  455 PHE A C   
3528 O O   . PHE A 455 ? 0.4520 0.3192 0.3729 -0.0543 -0.0411 0.0347  455 PHE A O   
3529 C CB  . PHE A 455 ? 0.3915 0.2305 0.3102 -0.0650 -0.0350 0.0390  455 PHE A CB  
3530 C CG  . PHE A 455 ? 0.4136 0.2554 0.3349 -0.0694 -0.0429 0.0309  455 PHE A CG  
3531 C CD1 . PHE A 455 ? 0.4164 0.2726 0.3552 -0.0769 -0.0455 0.0299  455 PHE A CD1 
3532 C CD2 . PHE A 455 ? 0.4549 0.2864 0.3608 -0.0665 -0.0478 0.0239  455 PHE A CD2 
3533 C CE1 . PHE A 455 ? 0.4832 0.3458 0.4281 -0.0808 -0.0559 0.0218  455 PHE A CE1 
3534 C CE2 . PHE A 455 ? 0.5393 0.3751 0.4440 -0.0706 -0.0585 0.0168  455 PHE A CE2 
3535 C CZ  . PHE A 455 ? 0.4615 0.3140 0.3877 -0.0773 -0.0640 0.0156  455 PHE A CZ  
3536 N N   . VAL A 456 ? 0.4344 0.2783 0.3352 -0.0483 -0.0338 0.0352  456 VAL A N   
3537 C CA  . VAL A 456 ? 0.3969 0.2380 0.2877 -0.0435 -0.0352 0.0333  456 VAL A CA  
3538 C C   . VAL A 456 ? 0.4534 0.3084 0.3550 -0.0400 -0.0337 0.0357  456 VAL A C   
3539 O O   . VAL A 456 ? 0.3572 0.2157 0.2600 -0.0374 -0.0388 0.0364  456 VAL A O   
3540 C CB  . VAL A 456 ? 0.4715 0.2977 0.3495 -0.0395 -0.0280 0.0315  456 VAL A CB  
3541 C CG1 . VAL A 456 ? 0.4587 0.2811 0.3256 -0.0351 -0.0259 0.0325  456 VAL A CG1 
3542 C CG2 . VAL A 456 ? 0.4867 0.2973 0.3538 -0.0426 -0.0284 0.0260  456 VAL A CG2 
3543 N N   . GLY A 457 ? 0.3597 0.2227 0.2696 -0.0396 -0.0274 0.0364  457 GLY A N   
3544 C CA  . GLY A 457 ? 0.3623 0.2382 0.2840 -0.0378 -0.0243 0.0352  457 GLY A CA  
3545 C C   . GLY A 457 ? 0.4040 0.2934 0.3396 -0.0405 -0.0276 0.0345  457 GLY A C   
3546 O O   . GLY A 457 ? 0.4140 0.3094 0.3609 -0.0367 -0.0282 0.0333  457 GLY A O   
3547 N N   . ALA A 458 ? 0.3508 0.2444 0.2892 -0.0472 -0.0289 0.0355  458 ALA A N   
3548 C CA  . ALA A 458 ? 0.3390 0.2481 0.2958 -0.0514 -0.0297 0.0337  458 ALA A CA  
3549 C C   . ALA A 458 ? 0.3985 0.3088 0.3632 -0.0490 -0.0405 0.0324  458 ALA A C   
3550 O O   . ALA A 458 ? 0.3731 0.2994 0.3603 -0.0487 -0.0423 0.0300  458 ALA A O   
3551 C CB  . ALA A 458 ? 0.3632 0.2736 0.3208 -0.0606 -0.0267 0.0361  458 ALA A CB  
3552 N N   . ALA A 459 ? 0.3885 0.2836 0.3353 -0.0470 -0.0480 0.0335  459 ALA A N   
3553 C CA  . ALA A 459 ? 0.4058 0.3018 0.3530 -0.0454 -0.0613 0.0326  459 ALA A CA  
3554 C C   . ALA A 459 ? 0.4059 0.2973 0.3465 -0.0355 -0.0653 0.0370  459 ALA A C   
3555 O O   . ALA A 459 ? 0.4356 0.3267 0.3711 -0.0326 -0.0787 0.0388  459 ALA A O   
3556 C CB  . ALA A 459 ? 0.4340 0.3150 0.3608 -0.0503 -0.0670 0.0297  459 ALA A CB  
3557 N N   . MET A 460 ? 0.3454 0.2329 0.2861 -0.0306 -0.0547 0.0391  460 MET A N   
3558 C CA  . MET A 460 ? 0.3611 0.2395 0.2962 -0.0218 -0.0556 0.0447  460 MET A CA  
3559 C C   . MET A 460 ? 0.4203 0.3104 0.3764 -0.0157 -0.0666 0.0480  460 MET A C   
3560 O O   . MET A 460 ? 0.4202 0.3293 0.4067 -0.0165 -0.0653 0.0435  460 MET A O   
3561 C CB  . MET A 460 ? 0.3553 0.2311 0.2967 -0.0197 -0.0412 0.0434  460 MET A CB  
3562 C CG  . MET A 460 ? 0.4084 0.2714 0.3307 -0.0226 -0.0324 0.0420  460 MET A CG  
3563 S SD  . MET A 460 ? 0.4284 0.2942 0.3639 -0.0219 -0.0183 0.0372  460 MET A SD  
3564 C CE  . MET A 460 ? 0.3567 0.2126 0.3006 -0.0138 -0.0168 0.0426  460 MET A CE  
3565 N N   . ARG A 461 ? 0.3704 0.2493 0.3103 -0.0093 -0.0773 0.0562  461 ARG A N   
3566 C CA  . ARG A 461 ? 0.4548 0.3419 0.4138 -0.0002 -0.0903 0.0628  461 ARG A CA  
3567 C C   . ARG A 461 ? 0.4888 0.3543 0.4300 0.0089  -0.0888 0.0752  461 ARG A C   
3568 O O   . ARG A 461 ? 0.5344 0.3795 0.4419 0.0064  -0.0815 0.0782  461 ARG A O   
3569 C CB  . ARG A 461 ? 0.4429 0.3408 0.3991 -0.0020 -0.1118 0.0627  461 ARG A CB  
3570 C CG  . ARG A 461 ? 0.3995 0.3182 0.3784 -0.0123 -0.1123 0.0509  461 ARG A CG  
3571 C CD  . ARG A 461 ? 0.4408 0.3685 0.4153 -0.0163 -0.1335 0.0482  461 ARG A CD  
3572 N NE  . ARG A 461 ? 0.4820 0.4290 0.4863 -0.0078 -0.1517 0.0525  461 ARG A NE  
3573 C CZ  . ARG A 461 ? 0.5000 0.4562 0.5000 -0.0076 -0.1758 0.0527  461 ARG A CZ  
3574 N NH1 . ARG A 461 ? 0.5005 0.4465 0.4641 -0.0165 -0.1834 0.0475  461 ARG A NH1 
3575 N NH2 . ARG A 461 ? 0.5167 0.4938 0.5512 0.0017  -0.1932 0.0573  461 ARG A NH2 
3576 N N   . SER A 462 ? 0.5037 0.3727 0.4700 0.0195  -0.0943 0.0826  462 SER A N   
3577 C CA  . SER A 462 ? 0.5399 0.3853 0.4940 0.0283  -0.0903 0.0961  462 SER A CA  
3578 C C   . SER A 462 ? 0.5864 0.4375 0.5699 0.0418  -0.1041 0.1067  462 SER A C   
3579 O O   . SER A 462 ? 0.5700 0.4456 0.5952 0.0443  -0.1091 0.0993  462 SER A O   
3580 C CB  . SER A 462 ? 0.5194 0.3547 0.4824 0.0257  -0.0665 0.0901  462 SER A CB  
3581 O OG  . SER A 462 ? 0.5348 0.3448 0.4885 0.0326  -0.0602 0.1030  462 SER A OG  
3582 N N   . GLU A 463 ? 0.6016 0.4292 0.5640 0.0507  -0.1092 0.1249  463 GLU A N   
3583 C CA  . GLU A 463 ? 0.6965 0.5242 0.6884 0.0661  -0.1215 0.1385  463 GLU A CA  
3584 C C   . GLU A 463 ? 0.6357 0.4657 0.6764 0.0704  -0.1028 0.1303  463 GLU A C   
3585 O O   . GLU A 463 ? 0.5226 0.3422 0.5606 0.0630  -0.0802 0.1208  463 GLU A O   
3586 C CB  . GLU A 463 ? 0.7426 0.5387 0.6962 0.0742  -0.1278 0.1625  463 GLU A CB  
3587 C CG  . GLU A 463 ? 0.8605 0.6537 0.7623 0.0714  -0.1485 0.1714  463 GLU A CG  
3588 C CD  . GLU A 463 ? 1.0341 0.7985 0.8988 0.0810  -0.1559 0.1977  463 GLU A CD  
3589 O OE1 . GLU A 463 ? 1.0266 0.7697 0.9011 0.0866  -0.1372 0.2070  463 GLU A OE1 
3590 O OE2 . GLU A 463 ? 1.1412 0.9130 0.9713 0.0813  -0.1731 0.2034  463 GLU A OE2 
3591 N N   . ALA A 464 ? 0.6604 0.5056 0.7482 0.0824  -0.1128 0.1324  464 ALA A N   
3592 C CA  . ALA A 464 ? 0.6824 0.5283 0.8187 0.0877  -0.0947 0.1234  464 ALA A CA  
3593 C C   . ALA A 464 ? 0.6773 0.4864 0.8056 0.0949  -0.0832 0.1378  464 ALA A C   
3594 O O   . ALA A 464 ? 0.7125 0.4986 0.8094 0.1017  -0.0951 0.1606  464 ALA A O   
3595 C CB  . ALA A 464 ? 0.6995 0.5709 0.8929 0.1000  -0.1075 0.1219  464 ALA A CB  
3596 N N   . THR A 465 ? 0.6393 0.4422 0.7947 0.0921  -0.0591 0.1238  465 THR A N   
3597 C CA  . THR A 465 ? 0.5979 0.3656 0.7525 0.0960  -0.0437 0.1331  465 THR A CA  
3598 C C   . THR A 465 ? 0.6414 0.4090 0.8568 0.1067  -0.0335 0.1255  465 THR A C   
3599 O O   . THR A 465 ? 0.6176 0.4134 0.8741 0.1114  -0.0382 0.1136  465 THR A O   
3600 C CB  . THR A 465 ? 0.6479 0.4047 0.7756 0.0797  -0.0218 0.1201  465 THR A CB  
3601 O OG1 . THR A 465 ? 0.6459 0.4260 0.8007 0.0708  -0.0077 0.0928  465 THR A OG1 
3602 C CG2 . THR A 465 ? 0.6014 0.3596 0.6748 0.0697  -0.0298 0.1250  465 THR A CG2 
3603 N N   . ALA A 466 ? 0.6032 0.3400 0.8239 0.1089  -0.0172 0.1300  466 ALA A N   
3604 C CA  . ALA A 466 ? 0.6144 0.3503 0.8832 0.1160  -0.0047 0.1188  466 ALA A CA  
3605 C C   . ALA A 466 ? 0.5928 0.3381 0.8896 0.1043  0.0203  0.0877  466 ALA A C   
3606 O O   . ALA A 466 ? 0.5917 0.3354 0.9251 0.1068  0.0344  0.0744  466 ALA A O   
3607 C CB  . ALA A 466 ? 0.6231 0.3258 0.8764 0.1205  0.0002  0.1349  466 ALA A CB  
3608 N N   . ALA A 467 ? 0.6359 0.3947 0.9088 0.0896  0.0252  0.0736  467 ALA A N   
3609 C CA  . ALA A 467 ? 0.6142 0.3849 0.9013 0.0765  0.0468  0.0429  467 ALA A CA  
3610 C C   . ALA A 467 ? 0.5867 0.3889 0.9132 0.0784  0.0501  0.0223  467 ALA A C   
3611 O O   . ALA A 467 ? 0.5378 0.3451 0.8879 0.0720  0.0699  -0.0032 467 ALA A O   
3612 C CB  . ALA A 467 ? 0.5088 0.2892 0.7496 0.0591  0.0484  0.0351  467 ALA A CB  
3613 N N   . ALA A 468 ? 0.5583 0.3825 0.8924 0.0860  0.0320  0.0312  468 ALA A N   
3614 C CA  . ALA A 468 ? 0.6317 0.4870 1.0079 0.0881  0.0365  0.0129  468 ALA A CA  
3615 C C   . ALA A 468 ? 0.5615 0.4185 0.9843 0.1087  0.0226  0.0276  468 ALA A C   
3616 O O   . ALA A 468 ? 0.6667 0.4946 1.0967 0.1221  0.0161  0.0479  468 ALA A O   
3617 C CB  . ALA A 468 ? 0.5576 0.4444 0.9080 0.0755  0.0298  0.0057  468 ALA A CB  
3618 N N   . GLU A 469 ? 0.6463 0.5372 1.1026 0.1116  0.0176  0.0186  469 GLU A N   
3619 C CA  . GLU A 469 ? 0.6779 0.5774 1.1890 0.1318  0.0039  0.0293  469 GLU A CA  
3620 C C   . GLU A 469 ? 0.7314 0.6459 1.2269 0.1374  -0.0287 0.0514  469 GLU A C   
3621 O O   . GLU A 469 ? 0.7810 0.7156 1.3244 0.1516  -0.0437 0.0567  469 GLU A O   
3622 C CB  . GLU A 469 ? 0.6164 0.5458 1.1871 0.1325  0.0218  0.0022  469 GLU A CB  
3623 C CG  . GLU A 469 ? 0.5914 0.5607 1.1568 0.1189  0.0212  -0.0115 469 GLU A CG  
3624 C CD  . GLU A 469 ? 0.5900 0.5625 1.1105 0.0962  0.0418  -0.0314 469 GLU A CD  
3625 O OE1 . GLU A 469 ? 0.5181 0.4648 0.9921 0.0888  0.0448  -0.0271 469 GLU A OE1 
3626 O OE2 . GLU A 469 ? 0.5499 0.5514 1.0826 0.0857  0.0551  -0.0509 469 GLU A OE2 
3627 N N   . HIS A 470 ? 0.8558 0.7617 1.2879 0.1266  -0.0401 0.0631  470 HIS A N   
3628 C CA  . HIS A 470 ? 0.9177 0.8376 1.3287 0.1288  -0.0700 0.0800  470 HIS A CA  
3629 C C   . HIS A 470 ? 1.0366 0.9286 1.4296 0.1443  -0.0920 0.1111  470 HIS A C   
3630 O O   . HIS A 470 ? 1.0440 0.8997 1.4061 0.1444  -0.0829 0.1221  470 HIS A O   
3631 C CB  . HIS A 470 ? 0.9210 0.8457 1.2736 0.1089  -0.0698 0.0747  470 HIS A CB  
3632 C CG  . HIS A 470 ? 0.8760 0.8230 1.2364 0.0930  -0.0482 0.0483  470 HIS A CG  
3633 N ND1 . HIS A 470 ? 0.9089 0.8917 1.3029 0.0893  -0.0496 0.0356  470 HIS A ND1 
3634 C CD2 . HIS A 470 ? 0.8524 0.7912 1.1903 0.0795  -0.0250 0.0330  470 HIS A CD2 
3635 C CE1 . HIS A 470 ? 0.8026 0.7957 1.1899 0.0741  -0.0269 0.0152  470 HIS A CE1 
3636 N NE2 . HIS A 470 ? 0.8123 0.7799 1.1649 0.0684  -0.0133 0.0133  470 HIS A NE2 
3637 N N   . LYS A 471 ? 1.1073 1.0171 1.5194 0.1568  -0.1212 0.1254  471 LYS A N   
3638 C CA  . LYS A 471 ? 1.2358 1.1261 1.6145 0.1676  -0.1414 0.1519  471 LYS A CA  
3639 C C   . LYS A 471 ? 1.3405 1.2473 1.6832 0.1645  -0.1724 0.1628  471 LYS A C   
3640 O O   . LYS A 471 ? 1.2581 1.1964 1.6180 0.1566  -0.1812 0.1496  471 LYS A O   
3641 C CB  . LYS A 471 ? 1.2334 1.1302 1.6612 0.1847  -0.1453 0.1559  471 LYS A CB  
3642 C CG  . LYS A 471 ? 1.2022 1.0831 1.6673 0.1873  -0.1152 0.1429  471 LYS A CG  
3643 C CD  . LYS A 471 ? 1.2526 1.0880 1.6714 0.1842  -0.1004 0.1542  471 LYS A CD  
3644 C CE  . LYS A 471 ? 1.1995 1.0193 1.6574 0.1875  -0.0744 0.1420  471 LYS A CE  
3645 N NZ  . LYS A 471 ? 1.2349 1.0599 1.7361 0.2056  -0.0849 0.1507  471 LYS A NZ  
3646 N N   . GLY A 472 ? 1.4716 1.3568 1.7628 0.1700  -0.1875 0.1856  472 GLY A N   
3647 C CA  . GLY A 472 ? 1.4750 1.3747 1.7281 0.1681  -0.2170 0.1952  472 GLY A CA  
3648 C C   . GLY A 472 ? 1.4193 1.2999 1.5993 0.1533  -0.2169 0.1993  472 GLY A C   
3649 O O   . GLY A 472 ? 1.4688 1.3581 1.6094 0.1505  -0.2392 0.2059  472 GLY A O   
3650 N N   . LYS A 473 ? 1.4406 1.2966 1.6021 0.1431  -0.1916 0.1937  473 LYS A N   
3651 C CA  . LYS A 473 ? 1.4386 1.2767 1.5349 0.1280  -0.1876 0.1947  473 LYS A CA  
3652 C C   . LYS A 473 ? 1.4492 1.3170 1.5346 0.1152  -0.2022 0.1796  473 LYS A C   
3653 O O   . LYS A 473 ? 1.4824 1.3408 1.5104 0.1048  -0.2074 0.1811  473 LYS A O   
3654 C CB  . LYS A 473 ? 1.5054 1.3159 1.5388 0.1313  -0.1905 0.2156  473 LYS A CB  
3655 C CG  . LYS A 473 ? 1.5515 1.3228 1.5620 0.1294  -0.1618 0.2226  473 LYS A CG  
3656 C CD  . LYS A 473 ? 1.6187 1.3651 1.5661 0.1316  -0.1625 0.2433  473 LYS A CD  
3657 C CE  . LYS A 473 ? 1.6575 1.3665 1.5808 0.1259  -0.1315 0.2475  473 LYS A CE  
3658 N NZ  . LYS A 473 ? 1.6914 1.3829 1.6588 0.1344  -0.1161 0.2461  473 LYS A NZ  
3659 N N   . VAL A 474 ? 1.1602 1.0642 1.3013 0.1147  -0.2052 0.1624  474 VAL A N   
3660 C CA  . VAL A 474 ? 0.8985 0.8317 1.0364 0.1007  -0.2142 0.1453  474 VAL A CA  
3661 C C   . VAL A 474 ? 0.7880 0.7118 0.8944 0.0821  -0.1882 0.1293  474 VAL A C   
3662 O O   . VAL A 474 ? 0.7397 0.6520 0.8558 0.0797  -0.1617 0.1225  474 VAL A O   
3663 C CB  . VAL A 474 ? 0.8156 0.7889 1.0266 0.1044  -0.2196 0.1316  474 VAL A CB  
3664 C CG1 . VAL A 474 ? 0.6893 0.6852 0.9085 0.0853  -0.2055 0.1074  474 VAL A CG1 
3665 C CG2 . VAL A 474 ? 0.8042 0.7992 1.0341 0.1160  -0.2573 0.1430  474 VAL A CG2 
3666 N N   . ILE A 475 ? 0.7215 0.6499 0.7907 0.0692  -0.1966 0.1228  475 ILE A N   
3667 C CA  . ILE A 475 ? 0.6805 0.5995 0.7200 0.0530  -0.1751 0.1095  475 ILE A CA  
3668 C C   . ILE A 475 ? 0.6086 0.5538 0.6917 0.0444  -0.1614 0.0901  475 ILE A C   
3669 O O   . ILE A 475 ? 0.5748 0.5465 0.6817 0.0394  -0.1737 0.0813  475 ILE A O   
3670 C CB  . ILE A 475 ? 0.6505 0.5631 0.6383 0.0430  -0.1876 0.1084  475 ILE A CB  
3671 C CG1 . ILE A 475 ? 0.6679 0.5529 0.6056 0.0504  -0.1981 0.1280  475 ILE A CG1 
3672 C CG2 . ILE A 475 ? 0.5814 0.4854 0.5473 0.0280  -0.1657 0.0946  475 ILE A CG2 
3673 C CD1 . ILE A 475 ? 0.7730 0.6485 0.6540 0.0400  -0.2070 0.1250  475 ILE A CD1 
3674 N N   . MET A 476 ? 0.5328 0.4706 0.6253 0.0417  -0.1356 0.0832  476 MET A N   
3675 C CA  . MET A 476 ? 0.4480 0.4068 0.5740 0.0332  -0.1192 0.0664  476 MET A CA  
3676 C C   . MET A 476 ? 0.4845 0.4342 0.5770 0.0186  -0.1039 0.0581  476 MET A C   
3677 O O   . MET A 476 ? 0.4611 0.3874 0.5118 0.0166  -0.1012 0.0637  476 MET A O   
3678 C CB  . MET A 476 ? 0.5161 0.4758 0.6790 0.0408  -0.1015 0.0624  476 MET A CB  
3679 C CG  . MET A 476 ? 0.5833 0.5504 0.7885 0.0574  -0.1136 0.0704  476 MET A CG  
3680 S SD  . MET A 476 ? 0.6983 0.6619 0.9458 0.0644  -0.0877 0.0612  476 MET A SD  
3681 C CE  . MET A 476 ? 0.6313 0.6247 0.9019 0.0489  -0.0679 0.0371  476 MET A CE  
3682 N N   . HIS A 477 ? 0.3567 0.3252 0.4696 0.0087  -0.0929 0.0453  477 HIS A N   
3683 C CA  . HIS A 477 ? 0.4213 0.3821 0.5086 -0.0034 -0.0776 0.0390  477 HIS A CA  
3684 C C   . HIS A 477 ? 0.3962 0.3498 0.4858 -0.0021 -0.0575 0.0348  477 HIS A C   
3685 O O   . HIS A 477 ? 0.3968 0.3618 0.5201 0.0026  -0.0492 0.0293  477 HIS A O   
3686 C CB  . HIS A 477 ? 0.3864 0.3675 0.4905 -0.0153 -0.0741 0.0296  477 HIS A CB  
3687 C CG  . HIS A 477 ? 0.4103 0.3969 0.5101 -0.0204 -0.0923 0.0302  477 HIS A CG  
3688 N ND1 . HIS A 477 ? 0.3345 0.3084 0.4028 -0.0303 -0.0930 0.0292  477 HIS A ND1 
3689 C CD2 . HIS A 477 ? 0.3960 0.4003 0.5215 -0.0171 -0.1110 0.0301  477 HIS A CD2 
3690 C CE1 . HIS A 477 ? 0.4474 0.4296 0.5202 -0.0341 -0.1103 0.0269  477 HIS A CE1 
3691 N NE2 . HIS A 477 ? 0.4077 0.4098 0.5145 -0.0266 -0.1227 0.0275  477 HIS A NE2 
3692 N N   . ASP A 478 ? 0.3928 0.3285 0.4489 -0.0064 -0.0496 0.0358  478 ASP A N   
3693 C CA  . ASP A 478 ? 0.3776 0.3076 0.4333 -0.0071 -0.0325 0.0300  478 ASP A CA  
3694 C C   . ASP A 478 ? 0.3838 0.3067 0.4097 -0.0162 -0.0266 0.0281  478 ASP A C   
3695 O O   . ASP A 478 ? 0.4089 0.3148 0.4138 -0.0151 -0.0242 0.0313  478 ASP A O   
3696 C CB  . ASP A 478 ? 0.3942 0.3056 0.4491 0.0026  -0.0313 0.0363  478 ASP A CB  
3697 C CG  . ASP A 478 ? 0.3754 0.2855 0.4443 0.0022  -0.0139 0.0264  478 ASP A CG  
3698 O OD1 . ASP A 478 ? 0.4371 0.3576 0.5025 -0.0067 -0.0039 0.0156  478 ASP A OD1 
3699 O OD2 . ASP A 478 ? 0.3655 0.2631 0.4479 0.0103  -0.0106 0.0294  478 ASP A OD2 
3700 N N   . PRO A 479 ? 0.3718 0.3071 0.3974 -0.0252 -0.0236 0.0236  479 PRO A N   
3701 C CA  . PRO A 479 ? 0.3820 0.3098 0.3817 -0.0321 -0.0204 0.0243  479 PRO A CA  
3702 C C   . PRO A 479 ? 0.3947 0.3187 0.3873 -0.0321 -0.0102 0.0198  479 PRO A C   
3703 O O   . PRO A 479 ? 0.3483 0.2826 0.3551 -0.0328 -0.0010 0.0116  479 PRO A O   
3704 C CB  . PRO A 479 ? 0.3443 0.2865 0.3503 -0.0412 -0.0173 0.0218  479 PRO A CB  
3705 C CG  . PRO A 479 ? 0.3934 0.3539 0.4306 -0.0401 -0.0125 0.0156  479 PRO A CG  
3706 C CD  . PRO A 479 ? 0.4065 0.3629 0.4579 -0.0293 -0.0220 0.0185  479 PRO A CD  
3707 N N   . PHE A 480 ? 0.3938 0.3040 0.3665 -0.0318 -0.0114 0.0232  480 PHE A N   
3708 C CA  . PHE A 480 ? 0.3568 0.2649 0.3249 -0.0326 -0.0041 0.0183  480 PHE A CA  
3709 C C   . PHE A 480 ? 0.3975 0.3027 0.3808 -0.0282 0.0027  0.0130  480 PHE A C   
3710 O O   . PHE A 480 ? 0.3873 0.2952 0.3735 -0.0306 0.0099  0.0048  480 PHE A O   
3711 C CB  . PHE A 480 ? 0.3726 0.2949 0.3369 -0.0396 -0.0001 0.0133  480 PHE A CB  
3712 C CG  . PHE A 480 ? 0.4090 0.3287 0.3574 -0.0432 -0.0055 0.0205  480 PHE A CG  
3713 C CD1 . PHE A 480 ? 0.3314 0.2515 0.2797 -0.0464 -0.0091 0.0257  480 PHE A CD1 
3714 C CD2 . PHE A 480 ? 0.4089 0.3258 0.3468 -0.0435 -0.0069 0.0217  480 PHE A CD2 
3715 C CE1 . PHE A 480 ? 0.3469 0.2610 0.2834 -0.0498 -0.0127 0.0325  480 PHE A CE1 
3716 C CE2 . PHE A 480 ? 0.4364 0.3486 0.3635 -0.0453 -0.0118 0.0295  480 PHE A CE2 
3717 C CZ  . PHE A 480 ? 0.4195 0.3283 0.3451 -0.0485 -0.0139 0.0351  480 PHE A CZ  
3718 N N   . ALA A 481 ? 0.2982 0.1976 0.2927 -0.0217 -0.0003 0.0176  481 ALA A N   
3719 C CA  . ALA A 481 ? 0.3747 0.2690 0.3891 -0.0162 0.0063  0.0143  481 ALA A CA  
3720 C C   . ALA A 481 ? 0.3915 0.3020 0.4260 -0.0195 0.0162  0.0002  481 ALA A C   
3721 O O   . ALA A 481 ? 0.4051 0.3111 0.4557 -0.0177 0.0255  -0.0079 481 ALA A O   
3722 C CB  . ALA A 481 ? 0.3584 0.2351 0.3657 -0.0155 0.0125  0.0153  481 ALA A CB  
3723 N N   . MET A 482 ? 0.3509 0.2788 0.3844 -0.0252 0.0161  -0.0037 482 MET A N   
3724 C CA  . MET A 482 ? 0.3253 0.2692 0.3682 -0.0309 0.0275  -0.0182 482 MET A CA  
3725 C C   . MET A 482 ? 0.3663 0.3250 0.4340 -0.0298 0.0315  -0.0222 482 MET A C   
3726 O O   . MET A 482 ? 0.3982 0.3714 0.4712 -0.0359 0.0434  -0.0348 482 MET A O   
3727 C CB  . MET A 482 ? 0.3849 0.3372 0.4017 -0.0404 0.0275  -0.0196 482 MET A CB  
3728 C CG  . MET A 482 ? 0.3544 0.3004 0.3571 -0.0424 0.0270  -0.0228 482 MET A CG  
3729 S SD  . MET A 482 ? 0.3832 0.3384 0.3964 -0.0471 0.0397  -0.0443 482 MET A SD  
3730 C CE  . MET A 482 ? 0.3845 0.3608 0.3796 -0.0568 0.0442  -0.0503 482 MET A CE  
3731 N N   . ARG A 483 ? 0.3668 0.3237 0.4501 -0.0226 0.0220  -0.0127 483 ARG A N   
3732 C CA  . ARG A 483 ? 0.3239 0.2985 0.4383 -0.0211 0.0247  -0.0171 483 ARG A CA  
3733 C C   . ARG A 483 ? 0.3558 0.3387 0.5002 -0.0189 0.0407  -0.0328 483 ARG A C   
3734 O O   . ARG A 483 ? 0.3421 0.3441 0.5002 -0.0249 0.0521  -0.0433 483 ARG A O   
3735 C CB  . ARG A 483 ? 0.3705 0.3423 0.5012 -0.0115 0.0085  -0.0050 483 ARG A CB  
3736 C CG  . ARG A 483 ? 0.4059 0.4006 0.5739 -0.0106 0.0085  -0.0093 483 ARG A CG  
3737 C CD  . ARG A 483 ? 0.4344 0.4291 0.6280 0.0021  -0.0087 0.0005  483 ARG A CD  
3738 N NE  . ARG A 483 ? 0.4592 0.4433 0.6754 0.0147  -0.0054 0.0006  483 ARG A NE  
3739 C CZ  . ARG A 483 ? 0.4985 0.4590 0.6993 0.0234  -0.0146 0.0133  483 ARG A CZ  
3740 N NH1 . ARG A 483 ? 0.4886 0.4351 0.6506 0.0211  -0.0274 0.0256  483 ARG A NH1 
3741 N NH2 . ARG A 483 ? 0.5246 0.4737 0.7501 0.0343  -0.0091 0.0136  483 ARG A NH2 
3742 N N   . PRO A 484 ? 0.3707 0.3395 0.5274 -0.0114 0.0447  -0.0362 484 PRO A N   
3743 C CA  . PRO A 484 ? 0.3588 0.3342 0.5471 -0.0098 0.0619  -0.0542 484 PRO A CA  
3744 C C   . PRO A 484 ? 0.3098 0.2904 0.4781 -0.0217 0.0771  -0.0722 484 PRO A C   
3745 O O   . PRO A 484 ? 0.3413 0.3264 0.5319 -0.0222 0.0933  -0.0909 484 PRO A O   
3746 C CB  . PRO A 484 ? 0.3689 0.3222 0.5772 0.0027  0.0592  -0.0486 484 PRO A CB  
3747 C CG  . PRO A 484 ? 0.3921 0.3290 0.5748 0.0070  0.0406  -0.0265 484 PRO A CG  
3748 C CD  . PRO A 484 ? 0.3529 0.2974 0.4979 -0.0045 0.0359  -0.0244 484 PRO A CD  
3749 N N   . PHE A 485 ? 0.3149 0.2956 0.4430 -0.0311 0.0718  -0.0679 485 PHE A N   
3750 C CA  . PHE A 485 ? 0.3760 0.3597 0.4815 -0.0411 0.0807  -0.0826 485 PHE A CA  
3751 C C   . PHE A 485 ? 0.3697 0.3681 0.4412 -0.0529 0.0811  -0.0823 485 PHE A C   
3752 O O   . PHE A 485 ? 0.3974 0.3998 0.4445 -0.0611 0.0843  -0.0922 485 PHE A O   
3753 C CB  . PHE A 485 ? 0.3118 0.2778 0.4033 -0.0398 0.0728  -0.0779 485 PHE A CB  
3754 C CG  . PHE A 485 ? 0.3307 0.2773 0.4500 -0.0291 0.0732  -0.0744 485 PHE A CG  
3755 C CD1 . PHE A 485 ? 0.3308 0.2747 0.4828 -0.0257 0.0870  -0.0900 485 PHE A CD1 
3756 C CD2 . PHE A 485 ? 0.3742 0.3034 0.4858 -0.0226 0.0610  -0.0553 485 PHE A CD2 
3757 C CE1 . PHE A 485 ? 0.3476 0.2700 0.5257 -0.0152 0.0875  -0.0839 485 PHE A CE1 
3758 C CE2 . PHE A 485 ? 0.3408 0.2494 0.4731 -0.0131 0.0619  -0.0490 485 PHE A CE2 
3759 C CZ  . PHE A 485 ? 0.3458 0.2500 0.5120 -0.0090 0.0746  -0.0620 485 PHE A CZ  
3760 N N   . PHE A 486 ? 0.3459 0.3521 0.4153 -0.0543 0.0775  -0.0709 486 PHE A N   
3761 C CA  . PHE A 486 ? 0.3830 0.3996 0.4203 -0.0656 0.0797  -0.0679 486 PHE A CA  
3762 C C   . PHE A 486 ? 0.3688 0.4010 0.4030 -0.0745 0.0994  -0.0873 486 PHE A C   
3763 O O   . PHE A 486 ? 0.3730 0.4143 0.4397 -0.0726 0.1133  -0.0991 486 PHE A O   
3764 C CB  . PHE A 486 ? 0.3912 0.4112 0.4333 -0.0665 0.0744  -0.0532 486 PHE A CB  
3765 C CG  . PHE A 486 ? 0.3469 0.3519 0.3806 -0.0610 0.0557  -0.0355 486 PHE A CG  
3766 C CD1 . PHE A 486 ? 0.3261 0.3214 0.3274 -0.0635 0.0468  -0.0271 486 PHE A CD1 
3767 C CD2 . PHE A 486 ? 0.3454 0.3471 0.4042 -0.0532 0.0467  -0.0282 486 PHE A CD2 
3768 C CE1 . PHE A 486 ? 0.3518 0.3330 0.3467 -0.0588 0.0326  -0.0135 486 PHE A CE1 
3769 C CE2 . PHE A 486 ? 0.3138 0.3013 0.3604 -0.0494 0.0309  -0.0144 486 PHE A CE2 
3770 C CZ  . PHE A 486 ? 0.3749 0.3515 0.3900 -0.0524 0.0255  -0.0079 486 PHE A CZ  
3771 N N   . GLY A 487 ? 0.4177 0.4538 0.4131 -0.0840 0.1005  -0.0913 487 GLY A N   
3772 C CA  . GLY A 487 ? 0.3869 0.4375 0.3676 -0.0946 0.1189  -0.1092 487 GLY A CA  
3773 C C   . GLY A 487 ? 0.4564 0.5166 0.4116 -0.1049 0.1263  -0.0999 487 GLY A C   
3774 O O   . GLY A 487 ? 0.4336 0.5058 0.3700 -0.1153 0.1438  -0.1136 487 GLY A O   
3775 N N   . TYR A 488 ? 0.4439 0.4976 0.3967 -0.1033 0.1150  -0.0775 488 TYR A N   
3776 C CA  . TYR A 488 ? 0.4743 0.5330 0.4052 -0.1137 0.1226  -0.0659 488 TYR A CA  
3777 C C   . TYR A 488 ? 0.4298 0.4803 0.3801 -0.1095 0.1114  -0.0467 488 TYR A C   
3778 O O   . TYR A 488 ? 0.3797 0.4217 0.3545 -0.0986 0.0973  -0.0430 488 TYR A O   
3779 C CB  . TYR A 488 ? 0.4723 0.5285 0.3475 -0.1219 0.1171  -0.0576 488 TYR A CB  
3780 C CG  . TYR A 488 ? 0.4693 0.5111 0.3296 -0.1150 0.0926  -0.0403 488 TYR A CG  
3781 C CD1 . TYR A 488 ? 0.4259 0.4641 0.2921 -0.1074 0.0803  -0.0484 488 TYR A CD1 
3782 C CD2 . TYR A 488 ? 0.5063 0.5378 0.3496 -0.1166 0.0836  -0.0169 488 TYR A CD2 
3783 C CE1 . TYR A 488 ? 0.3996 0.4268 0.2565 -0.1013 0.0603  -0.0342 488 TYR A CE1 
3784 C CE2 . TYR A 488 ? 0.4642 0.4829 0.2982 -0.1096 0.0631  -0.0029 488 TYR A CE2 
3785 C CZ  . TYR A 488 ? 0.4479 0.4657 0.2891 -0.1019 0.0518  -0.0119 488 TYR A CZ  
3786 O OH  . TYR A 488 ? 0.4325 0.4396 0.2687 -0.0951 0.0337  0.0008  488 TYR A OH  
3787 N N   . ASN A 489 ? 0.4297 0.4818 0.3667 -0.1193 0.1187  -0.0351 489 ASN A N   
3788 C CA  . ASN A 489 ? 0.4867 0.5331 0.4445 -0.1189 0.1118  -0.0205 489 ASN A CA  
3789 C C   . ASN A 489 ? 0.4484 0.4770 0.4025 -0.1092 0.0877  -0.0075 489 ASN A C   
3790 O O   . ASN A 489 ? 0.4239 0.4412 0.3444 -0.1086 0.0776  0.0019  489 ASN A O   
3791 C CB  . ASN A 489 ? 0.4839 0.5292 0.4166 -0.1329 0.1234  -0.0076 489 ASN A CB  
3792 C CG  . ASN A 489 ? 0.5017 0.5440 0.4628 -0.1360 0.1216  0.0026  489 ASN A CG  
3793 O OD1 . ASN A 489 ? 0.5132 0.5425 0.4822 -0.1293 0.1028  0.0120  489 ASN A OD1 
3794 N ND2 . ASN A 489 ? 0.4866 0.5418 0.4640 -0.1475 0.1425  -0.0010 489 ASN A ND2 
3795 N N   . PHE A 490 ? 0.3829 0.4099 0.3721 -0.1016 0.0784  -0.0075 490 PHE A N   
3796 C CA  . PHE A 490 ? 0.3507 0.3609 0.3361 -0.0927 0.0582  0.0020  490 PHE A CA  
3797 C C   . PHE A 490 ? 0.3778 0.3738 0.3423 -0.0978 0.0510  0.0186  490 PHE A C   
3798 O O   . PHE A 490 ? 0.4342 0.4152 0.3823 -0.0923 0.0379  0.0263  490 PHE A O   
3799 C CB  . PHE A 490 ? 0.3995 0.4120 0.4223 -0.0841 0.0497  -0.0015 490 PHE A CB  
3800 C CG  . PHE A 490 ? 0.3826 0.3776 0.3982 -0.0770 0.0311  0.0079  490 PHE A CG  
3801 C CD1 . PHE A 490 ? 0.4055 0.3872 0.3988 -0.0712 0.0242  0.0104  490 PHE A CD1 
3802 C CD2 . PHE A 490 ? 0.4659 0.4591 0.4980 -0.0769 0.0213  0.0124  490 PHE A CD2 
3803 C CE1 . PHE A 490 ? 0.3789 0.3447 0.3654 -0.0654 0.0106  0.0176  490 PHE A CE1 
3804 C CE2 . PHE A 490 ? 0.4136 0.3903 0.4349 -0.0714 0.0061  0.0189  490 PHE A CE2 
3805 C CZ  . PHE A 490 ? 0.4428 0.4052 0.4407 -0.0655 0.0021  0.0216  490 PHE A CZ  
3806 N N   . GLY A 491 ? 0.4112 0.4109 0.3791 -0.1085 0.0610  0.0238  491 GLY A N   
3807 C CA  . GLY A 491 ? 0.4125 0.3954 0.3605 -0.1141 0.0567  0.0403  491 GLY A CA  
3808 C C   . GLY A 491 ? 0.4941 0.4677 0.4009 -0.1144 0.0549  0.0501  491 GLY A C   
3809 O O   . GLY A 491 ? 0.4512 0.4074 0.3436 -0.1105 0.0429  0.0624  491 GLY A O   
3810 N N   . LYS A 492 ? 0.4252 0.4114 0.3137 -0.1186 0.0662  0.0438  492 LYS A N   
3811 C CA  . LYS A 492 ? 0.4895 0.4709 0.3374 -0.1185 0.0613  0.0518  492 LYS A CA  
3812 C C   . LYS A 492 ? 0.4360 0.4146 0.2836 -0.1066 0.0446  0.0468  492 LYS A C   
3813 O O   . LYS A 492 ? 0.5076 0.4781 0.3322 -0.1032 0.0328  0.0574  492 LYS A O   
3814 C CB  . LYS A 492 ? 0.4748 0.4719 0.3002 -0.1276 0.0779  0.0432  492 LYS A CB  
3815 C CG  . LYS A 492 ? 0.5974 0.5998 0.4261 -0.1408 0.0995  0.0456  492 LYS A CG  
3816 C CD  . LYS A 492 ? 0.6619 0.6452 0.4781 -0.1465 0.0975  0.0695  492 LYS A CD  
3817 C CE  . LYS A 492 ? 0.7143 0.7026 0.5412 -0.1611 0.1209  0.0712  492 LYS A CE  
3818 N NZ  . LYS A 492 ? 0.8304 0.7972 0.6560 -0.1668 0.1195  0.0928  492 LYS A NZ  
3819 N N   . TYR A 493 ? 0.4126 0.3974 0.2878 -0.1000 0.0438  0.0316  493 TYR A N   
3820 C CA  . TYR A 493 ? 0.4124 0.3920 0.2916 -0.0897 0.0305  0.0275  493 TYR A CA  
3821 C C   . TYR A 493 ? 0.4306 0.3923 0.3110 -0.0840 0.0171  0.0411  493 TYR A C   
3822 O O   . TYR A 493 ? 0.4192 0.3754 0.2897 -0.0784 0.0066  0.0449  493 TYR A O   
3823 C CB  . TYR A 493 ? 0.3649 0.3505 0.2743 -0.0842 0.0342  0.0120  493 TYR A CB  
3824 C CG  . TYR A 493 ? 0.4267 0.4041 0.3449 -0.0745 0.0240  0.0085  493 TYR A CG  
3825 C CD1 . TYR A 493 ? 0.4031 0.3670 0.3322 -0.0681 0.0147  0.0159  493 TYR A CD1 
3826 C CD2 . TYR A 493 ? 0.3580 0.3413 0.2742 -0.0730 0.0254  -0.0038 493 TYR A CD2 
3827 C CE1 . TYR A 493 ? 0.4089 0.3643 0.3438 -0.0605 0.0086  0.0133  493 TYR A CE1 
3828 C CE2 . TYR A 493 ? 0.3976 0.3725 0.3245 -0.0657 0.0189  -0.0068 493 TYR A CE2 
3829 C CZ  . TYR A 493 ? 0.4390 0.3996 0.3742 -0.0594 0.0114  0.0027  493 TYR A CZ  
3830 O OH  . TYR A 493 ? 0.4121 0.3634 0.3553 -0.0533 0.0079  0.0006  493 TYR A OH  
3831 N N   . LEU A 494 ? 0.4106 0.3644 0.3057 -0.0857 0.0177  0.0467  494 LEU A N   
3832 C CA  . LEU A 494 ? 0.4279 0.3635 0.3242 -0.0816 0.0071  0.0568  494 LEU A CA  
3833 C C   . LEU A 494 ? 0.3679 0.2929 0.2417 -0.0834 0.0036  0.0723  494 LEU A C   
3834 O O   . LEU A 494 ? 0.4299 0.3429 0.3014 -0.0763 -0.0065 0.0781  494 LEU A O   
3835 C CB  . LEU A 494 ? 0.3762 0.3074 0.2927 -0.0854 0.0086  0.0567  494 LEU A CB  
3836 C CG  . LEU A 494 ? 0.3658 0.3052 0.3063 -0.0811 0.0068  0.0448  494 LEU A CG  
3837 C CD1 . LEU A 494 ? 0.4029 0.3432 0.3638 -0.0868 0.0065  0.0445  494 LEU A CD1 
3838 C CD2 . LEU A 494 ? 0.4028 0.3320 0.3414 -0.0710 -0.0033 0.0426  494 LEU A CD2 
3839 N N   . ALA A 495 ? 0.4273 0.3558 0.2854 -0.0925 0.0124  0.0801  495 ALA A N   
3840 C CA  . ALA A 495 ? 0.4858 0.4026 0.3197 -0.0935 0.0080  0.0985  495 ALA A CA  
3841 C C   . ALA A 495 ? 0.5094 0.4337 0.3245 -0.0868 -0.0026 0.0988  495 ALA A C   
3842 O O   . ALA A 495 ? 0.5368 0.4504 0.3426 -0.0812 -0.0138 0.1127  495 ALA A O   
3843 C CB  . ALA A 495 ? 0.4507 0.3688 0.2677 -0.1061 0.0220  0.1080  495 ALA A CB  
3844 N N   . HIS A 496 ? 0.4722 0.4152 0.2855 -0.0872 0.0003  0.0826  496 HIS A N   
3845 C CA  . HIS A 496 ? 0.5101 0.4633 0.3116 -0.0819 -0.0107 0.0782  496 HIS A CA  
3846 C C   . HIS A 496 ? 0.5124 0.4576 0.3347 -0.0708 -0.0230 0.0773  496 HIS A C   
3847 O O   . HIS A 496 ? 0.5317 0.4764 0.3480 -0.0649 -0.0358 0.0852  496 HIS A O   
3848 C CB  . HIS A 496 ? 0.4777 0.4500 0.2798 -0.0859 -0.0023 0.0571  496 HIS A CB  
3849 C CG  . HIS A 496 ? 0.5548 0.5408 0.3415 -0.0845 -0.0119 0.0495  496 HIS A CG  
3850 N ND1 . HIS A 496 ? 0.5162 0.5071 0.2694 -0.0872 -0.0208 0.0610  496 HIS A ND1 
3851 C CD2 . HIS A 496 ? 0.4692 0.4657 0.2702 -0.0816 -0.0145 0.0312  496 HIS A CD2 
3852 C CE1 . HIS A 496 ? 0.5089 0.5154 0.2571 -0.0860 -0.0303 0.0484  496 HIS A CE1 
3853 N NE2 . HIS A 496 ? 0.5341 0.5438 0.3127 -0.0833 -0.0255 0.0294  496 HIS A NE2 
3854 N N   . TRP A 497 ? 0.4589 0.3983 0.3060 -0.0677 -0.0190 0.0681  497 TRP A N   
3855 C CA  . TRP A 497 ? 0.4442 0.3740 0.3086 -0.0586 -0.0266 0.0668  497 TRP A CA  
3856 C C   . TRP A 497 ? 0.5123 0.4248 0.3765 -0.0547 -0.0332 0.0825  497 TRP A C   
3857 O O   . TRP A 497 ? 0.5342 0.4436 0.4057 -0.0469 -0.0419 0.0851  497 TRP A O   
3858 C CB  . TRP A 497 ? 0.3767 0.3015 0.2601 -0.0573 -0.0206 0.0565  497 TRP A CB  
3859 C CG  . TRP A 497 ? 0.4370 0.3719 0.3301 -0.0552 -0.0179 0.0418  497 TRP A CG  
3860 C CD1 . TRP A 497 ? 0.4177 0.3652 0.3123 -0.0593 -0.0102 0.0309  497 TRP A CD1 
3861 C CD2 . TRP A 497 ? 0.4309 0.3621 0.3360 -0.0488 -0.0206 0.0359  497 TRP A CD2 
3862 N NE1 . TRP A 497 ? 0.4148 0.3648 0.3222 -0.0557 -0.0088 0.0193  497 TRP A NE1 
3863 C CE2 . TRP A 497 ? 0.4619 0.4021 0.3751 -0.0499 -0.0148 0.0228  497 TRP A CE2 
3864 C CE3 . TRP A 497 ? 0.4209 0.3413 0.3327 -0.0428 -0.0253 0.0397  497 TRP A CE3 
3865 C CZ2 . TRP A 497 ? 0.4695 0.4070 0.3960 -0.0460 -0.0135 0.0151  497 TRP A CZ2 
3866 C CZ3 . TRP A 497 ? 0.4748 0.3949 0.3993 -0.0391 -0.0231 0.0312  497 TRP A CZ3 
3867 C CH2 . TRP A 497 ? 0.5110 0.4390 0.4421 -0.0412 -0.0173 0.0199  497 TRP A CH2 
3868 N N   . LEU A 498 ? 0.4929 0.3934 0.3532 -0.0603 -0.0280 0.0921  498 LEU A N   
3869 C CA  . LEU A 498 ? 0.5068 0.3868 0.3699 -0.0571 -0.0324 0.1065  498 LEU A CA  
3870 C C   . LEU A 498 ? 0.5446 0.4247 0.3927 -0.0531 -0.0420 0.1223  498 LEU A C   
3871 O O   . LEU A 498 ? 0.5938 0.4605 0.4519 -0.0448 -0.0497 0.1313  498 LEU A O   
3872 C CB  . LEU A 498 ? 0.5135 0.3810 0.3776 -0.0663 -0.0235 0.1123  498 LEU A CB  
3873 C CG  . LEU A 498 ? 0.5338 0.3987 0.4163 -0.0691 -0.0186 0.0990  498 LEU A CG  
3874 C CD1 . LEU A 498 ? 0.5331 0.3924 0.4194 -0.0804 -0.0101 0.1033  498 LEU A CD1 
3875 C CD2 . LEU A 498 ? 0.4444 0.2932 0.3396 -0.0616 -0.0238 0.0950  498 LEU A CD2 
3876 N N   . SER A 499 ? 0.5798 0.4752 0.4040 -0.0583 -0.0422 0.1254  499 SER A N   
3877 C CA  . SER A 499 ? 0.6336 0.5300 0.4370 -0.0551 -0.0537 0.1429  499 SER A CA  
3878 C C   . SER A 499 ? 0.6231 0.5300 0.4390 -0.0435 -0.0697 0.1393  499 SER A C   
3879 O O   . SER A 499 ? 0.7185 0.6242 0.5263 -0.0371 -0.0835 0.1557  499 SER A O   
3880 C CB  . SER A 499 ? 0.5677 0.4799 0.3371 -0.0650 -0.0493 0.1439  499 SER A CB  
3881 O OG  . SER A 499 ? 0.6035 0.5393 0.3731 -0.0655 -0.0508 0.1234  499 SER A OG  
3882 N N   A MET A 500 ? 0.6281 0.5456 0.4652 -0.0408 -0.0680 0.1191  500 MET A N   
3883 N N   B MET A 500 ? 0.6281 0.5455 0.4652 -0.0407 -0.0681 0.1192  500 MET A N   
3884 C CA  A MET A 500 ? 0.6387 0.5680 0.4937 -0.0314 -0.0806 0.1134  500 MET A CA  
3885 C CA  B MET A 500 ? 0.6389 0.5683 0.4935 -0.0313 -0.0809 0.1139  500 MET A CA  
3886 C C   A MET A 500 ? 0.6681 0.5808 0.5456 -0.0203 -0.0872 0.1248  500 MET A C   
3887 C C   B MET A 500 ? 0.6678 0.5806 0.5461 -0.0202 -0.0870 0.1243  500 MET A C   
3888 O O   A MET A 500 ? 0.7035 0.6263 0.5954 -0.0112 -0.1008 0.1274  500 MET A O   
3889 O O   B MET A 500 ? 0.7030 0.6260 0.5971 -0.0111 -0.1001 0.1256  500 MET A O   
3890 C CB  A MET A 500 ? 0.6054 0.5449 0.4794 -0.0324 -0.0732 0.0905  500 MET A CB  
3891 C CB  B MET A 500 ? 0.6057 0.5468 0.4780 -0.0326 -0.0741 0.0908  500 MET A CB  
3892 C CG  A MET A 500 ? 0.6086 0.5644 0.4672 -0.0418 -0.0664 0.0768  500 MET A CG  
3893 C CG  B MET A 500 ? 0.6169 0.5767 0.4719 -0.0416 -0.0699 0.0780  500 MET A CG  
3894 S SD  A MET A 500 ? 0.5865 0.5674 0.4210 -0.0449 -0.0804 0.0764  500 MET A SD  
3895 S SD  B MET A 500 ? 0.6724 0.6412 0.5517 -0.0424 -0.0614 0.0532  500 MET A SD  
3896 C CE  A MET A 500 ? 0.6032 0.5965 0.4240 -0.0569 -0.0651 0.0561  500 MET A CE  
3897 C CE  B MET A 500 ? 0.4767 0.4233 0.3662 -0.0424 -0.0472 0.0535  500 MET A CE  
3898 N N   . ALA A 501 ? 0.6615 0.5498 0.5457 -0.0209 -0.0778 0.1299  501 ALA A N   
3899 C CA  . ALA A 501 ? 0.6879 0.5569 0.5937 -0.0109 -0.0816 0.1397  501 ALA A CA  
3900 C C   . ALA A 501 ? 0.7661 0.6272 0.6608 -0.0061 -0.0935 0.1647  501 ALA A C   
3901 O O   . ALA A 501 ? 0.8470 0.6928 0.7634 0.0044  -0.0988 0.1746  501 ALA A O   
3902 C CB  . ALA A 501 ? 0.6567 0.5015 0.5708 -0.0149 -0.0679 0.1352  501 ALA A CB  
3903 N N   . HIS A 502 ? 0.8472 0.7169 0.7081 -0.0135 -0.0968 0.1756  502 HIS A N   
3904 C CA  . HIS A 502 ? 0.9362 0.7998 0.7781 -0.0093 -0.1097 0.2021  502 HIS A CA  
3905 C C   . HIS A 502 ? 0.9515 0.8415 0.7900 -0.0013 -0.1311 0.2043  502 HIS A C   
3906 O O   . HIS A 502 ? 1.1293 1.0169 0.9562 0.0059  -0.1445 0.2251  502 HIS A O   
3907 C CB  . HIS A 502 ? 1.0078 0.8665 0.8098 -0.0229 -0.1001 0.2132  502 HIS A CB  
3908 C CG  . HIS A 502 ? 1.0279 0.8659 0.8360 -0.0325 -0.0798 0.2095  502 HIS A CG  
3909 N ND1 . HIS A 502 ? 1.0736 0.9133 0.8578 -0.0463 -0.0649 0.2091  502 HIS A ND1 
3910 C CD2 . HIS A 502 ? 1.0442 0.8610 0.8813 -0.0309 -0.0722 0.2042  502 HIS A CD2 
3911 C CE1 . HIS A 502 ? 1.0873 0.9096 0.8884 -0.0527 -0.0508 0.2046  502 HIS A CE1 
3912 N NE2 . HIS A 502 ? 1.1561 0.9640 0.9871 -0.0438 -0.0553 0.2009  502 HIS A NE2 
3913 N N   . ARG A 503 ? 0.8723 0.7881 0.7226 -0.0021 -0.1328 0.1809  503 ARG A N   
3914 C CA  . ARG A 503 ? 1.0381 0.9829 0.8860 0.0027  -0.1534 0.1789  503 ARG A CA  
3915 C C   . ARG A 503 ? 1.1459 1.0904 1.0291 0.0198  -0.1712 0.1904  503 ARG A C   
3916 O O   . ARG A 503 ? 1.0325 0.9633 0.9542 0.0272  -0.1631 0.1846  503 ARG A O   
3917 C CB  . ARG A 503 ? 1.0012 0.9707 0.8616 -0.0031 -0.1484 0.1491  503 ARG A CB  
3918 C CG  . ARG A 503 ? 0.9116 0.8856 0.7411 -0.0183 -0.1331 0.1365  503 ARG A CG  
3919 C CD  . ARG A 503 ? 1.0605 1.0647 0.8703 -0.0242 -0.1438 0.1241  503 ARG A CD  
3920 N NE  . ARG A 503 ? 1.1702 1.1780 0.9522 -0.0382 -0.1275 0.1111  503 ARG A NE  
3921 C CZ  . ARG A 503 ? 1.1458 1.1767 0.9073 -0.0464 -0.1307 0.0957  503 ARG A CZ  
3922 N NH1 . ARG A 503 ? 1.2274 1.2818 0.9909 -0.0433 -0.1516 0.0906  503 ARG A NH1 
3923 N NH2 . ARG A 503 ? 1.0892 1.1206 0.8303 -0.0583 -0.1126 0.0833  503 ARG A NH2 
3924 N N   . PRO A 504 ? 1.2954 1.2556 1.1669 0.0266  -0.1956 0.2061  504 PRO A N   
3925 C CA  . PRO A 504 ? 1.3208 1.2840 1.2323 0.0449  -0.2148 0.2175  504 PRO A CA  
3926 C C   . PRO A 504 ? 1.2688 1.2575 1.2287 0.0495  -0.2164 0.1909  504 PRO A C   
3927 O O   . PRO A 504 ? 1.2205 1.2378 1.1745 0.0413  -0.2199 0.1712  504 PRO A O   
3928 C CB  . PRO A 504 ? 1.2754 1.2552 1.1568 0.0495  -0.2325 0.2301  504 PRO A CB  
3929 C CG  . PRO A 504 ? 1.3284 1.3012 1.1510 0.0341  -0.2194 0.2330  504 PRO A CG  
3930 C CD  . PRO A 504 ? 1.3106 1.2851 1.1311 0.0188  -0.2041 0.2133  504 PRO A CD  
3931 N N   . ALA A 505 ? 1.0080 0.9849 1.0171 0.0617  -0.2116 0.1894  505 ALA A N   
3932 C CA  . ALA A 505 ? 0.9421 0.9404 1.0027 0.0669  -0.2099 0.1660  505 ALA A CA  
3933 C C   . ALA A 505 ? 0.8357 0.8401 0.8910 0.0522  -0.1882 0.1380  505 ALA A C   
3934 O O   . ALA A 505 ? 0.7794 0.8085 0.8640 0.0510  -0.1885 0.1174  505 ALA A O   
3935 C CB  . ALA A 505 ? 0.8620 0.8985 0.9433 0.0751  -0.2393 0.1668  505 ALA A CB  
3936 N N   . ALA A 506 ? 0.8394 0.8210 0.8602 0.0409  -0.1695 0.1375  506 ALA A N   
3937 C CA  . ALA A 506 ? 0.7924 0.7763 0.8083 0.0287  -0.1498 0.1141  506 ALA A CA  
3938 C C   . ALA A 506 ? 0.6186 0.5917 0.6731 0.0330  -0.1328 0.1001  506 ALA A C   
3939 O O   . ALA A 506 ? 0.6650 0.6127 0.7294 0.0389  -0.1246 0.1077  506 ALA A O   
3940 C CB  . ALA A 506 ? 0.7558 0.7203 0.7294 0.0170  -0.1361 0.1184  506 ALA A CB  
3941 N N   . LYS A 507 ? 0.5500 0.5413 0.6253 0.0290  -0.1262 0.0791  507 LYS A N   
3942 C CA  . LYS A 507 ? 0.5799 0.5617 0.6855 0.0305  -0.1068 0.0645  507 LYS A CA  
3943 C C   . LYS A 507 ? 0.5295 0.4950 0.6068 0.0187  -0.0874 0.0555  507 LYS A C   
3944 O O   . LYS A 507 ? 0.5279 0.5050 0.6039 0.0106  -0.0807 0.0412  507 LYS A O   
3945 C CB  . LYS A 507 ? 0.5609 0.5708 0.7083 0.0325  -0.1096 0.0487  507 LYS A CB  
3946 C CG  . LYS A 507 ? 0.6708 0.7022 0.8515 0.0453  -0.1326 0.0573  507 LYS A CG  
3947 C CD  . LYS A 507 ? 0.6279 0.6932 0.8515 0.0446  -0.1371 0.0392  507 LYS A CD  
3948 C CE  . LYS A 507 ? 0.6816 0.7739 0.9383 0.0575  -0.1655 0.0482  507 LYS A CE  
3949 N NZ  . LYS A 507 ? 0.7483 0.8782 1.0508 0.0550  -0.1715 0.0283  507 LYS A NZ  
3950 N N   . LEU A 508 ? 0.5140 0.4525 0.5711 0.0178  -0.0791 0.0640  508 LEU A N   
3951 C CA  . LEU A 508 ? 0.5382 0.4629 0.5687 0.0078  -0.0647 0.0579  508 LEU A CA  
3952 C C   . LEU A 508 ? 0.4424 0.3612 0.4875 0.0062  -0.0473 0.0424  508 LEU A C   
3953 O O   . LEU A 508 ? 0.5129 0.4209 0.5782 0.0122  -0.0397 0.0397  508 LEU A O   
3954 C CB  . LEU A 508 ? 0.4587 0.3583 0.4688 0.0067  -0.0618 0.0697  508 LEU A CB  
3955 C CG  . LEU A 508 ? 0.5085 0.4090 0.4984 0.0062  -0.0749 0.0875  508 LEU A CG  
3956 C CD1 . LEU A 508 ? 0.5378 0.4113 0.5149 0.0039  -0.0690 0.0977  508 LEU A CD1 
3957 C CD2 . LEU A 508 ? 0.5298 0.4482 0.4949 -0.0029 -0.0781 0.0846  508 LEU A CD2 
3958 N N   . PRO A 509 ? 0.4773 0.4010 0.5123 -0.0018 -0.0395 0.0325  509 PRO A N   
3959 C CA  . PRO A 509 ? 0.4776 0.3921 0.5207 -0.0039 -0.0220 0.0211  509 PRO A CA  
3960 C C   . PRO A 509 ? 0.4642 0.3523 0.4874 -0.0048 -0.0118 0.0234  509 PRO A C   
3961 O O   . PRO A 509 ? 0.4375 0.3155 0.4411 -0.0060 -0.0173 0.0319  509 PRO A O   
3962 C CB  . PRO A 509 ? 0.4300 0.3541 0.4648 -0.0119 -0.0186 0.0135  509 PRO A CB  
3963 C CG  . PRO A 509 ? 0.4408 0.3709 0.4529 -0.0151 -0.0302 0.0205  509 PRO A CG  
3964 C CD  . PRO A 509 ? 0.4241 0.3613 0.4405 -0.0091 -0.0451 0.0312  509 PRO A CD  
3965 N N   . LYS A 510 ? 0.4658 0.3431 0.4939 -0.0053 0.0037  0.0150  510 LYS A N   
3966 C CA  . LYS A 510 ? 0.5130 0.3668 0.5171 -0.0078 0.0133  0.0144  510 LYS A CA  
3967 C C   . LYS A 510 ? 0.4552 0.3058 0.4335 -0.0144 0.0135  0.0159  510 LYS A C   
3968 O O   . LYS A 510 ? 0.4636 0.3255 0.4462 -0.0171 0.0145  0.0134  510 LYS A O   
3969 C CB  . LYS A 510 ? 0.4561 0.2994 0.4687 -0.0068 0.0311  0.0048  510 LYS A CB  
3970 C CG  . LYS A 510 ? 0.5695 0.4027 0.5968 -0.0007 0.0348  0.0022  510 LYS A CG  
3971 C CD  . LYS A 510 ? 0.5519 0.3788 0.5915 -0.0003 0.0557  -0.0098 510 LYS A CD  
3972 C CE  . LYS A 510 ? 0.6118 0.4204 0.6543 0.0037  0.0639  -0.0157 510 LYS A CE  
3973 N NZ  . LYS A 510 ? 0.6016 0.4127 0.6661 0.0116  0.0491  -0.0084 510 LYS A NZ  
3974 N N   . ILE A 511 ? 0.4579 0.2934 0.4126 -0.0167 0.0124  0.0189  511 ILE A N   
3975 C CA  . ILE A 511 ? 0.4402 0.2738 0.3746 -0.0213 0.0102  0.0214  511 ILE A CA  
3976 C C   . ILE A 511 ? 0.4843 0.2995 0.3974 -0.0230 0.0185  0.0186  511 ILE A C   
3977 O O   . ILE A 511 ? 0.4929 0.2949 0.3967 -0.0231 0.0201  0.0159  511 ILE A O   
3978 C CB  . ILE A 511 ? 0.4796 0.3165 0.4065 -0.0235 -0.0015 0.0279  511 ILE A CB  
3979 C CG1 . ILE A 511 ? 0.4529 0.3086 0.3915 -0.0233 -0.0087 0.0314  511 ILE A CG1 
3980 C CG2 . ILE A 511 ? 0.4224 0.2561 0.3327 -0.0272 -0.0034 0.0290  511 ILE A CG2 
3981 C CD1 . ILE A 511 ? 0.4774 0.3355 0.4087 -0.0262 -0.0170 0.0390  511 ILE A CD1 
3982 N N   . PHE A 512 ? 0.4323 0.2454 0.3367 -0.0245 0.0238  0.0192  512 PHE A N   
3983 C CA  . PHE A 512 ? 0.4966 0.2922 0.3749 -0.0260 0.0304  0.0196  512 PHE A CA  
3984 C C   . PHE A 512 ? 0.4724 0.2680 0.3367 -0.0268 0.0214  0.0264  512 PHE A C   
3985 O O   . PHE A 512 ? 0.4337 0.2423 0.3128 -0.0262 0.0161  0.0288  512 PHE A O   
3986 C CB  . PHE A 512 ? 0.4798 0.2686 0.3600 -0.0265 0.0477  0.0168  512 PHE A CB  
3987 C CG  . PHE A 512 ? 0.4715 0.2632 0.3731 -0.0251 0.0581  0.0087  512 PHE A CG  
3988 C CD1 . PHE A 512 ? 0.5043 0.2819 0.3937 -0.0253 0.0677  0.0026  512 PHE A CD1 
3989 C CD2 . PHE A 512 ? 0.4628 0.2728 0.3988 -0.0235 0.0580  0.0057  512 PHE A CD2 
3990 C CE1 . PHE A 512 ? 0.5352 0.3166 0.4508 -0.0228 0.0784  -0.0058 512 PHE A CE1 
3991 C CE2 . PHE A 512 ? 0.4647 0.2805 0.4267 -0.0209 0.0657  -0.0015 512 PHE A CE2 
3992 C CZ  . PHE A 512 ? 0.4601 0.2614 0.4142 -0.0199 0.0767  -0.0070 512 PHE A CZ  
3993 N N   . HIS A 513 ? 0.5199 0.3018 0.3564 -0.0277 0.0195  0.0286  513 HIS A N   
3994 C CA  . HIS A 513 ? 0.4599 0.2409 0.2842 -0.0266 0.0101  0.0364  513 HIS A CA  
3995 C C   . HIS A 513 ? 0.4941 0.2566 0.2898 -0.0263 0.0178  0.0416  513 HIS A C   
3996 O O   . HIS A 513 ? 0.5248 0.2742 0.2960 -0.0288 0.0238  0.0375  513 HIS A O   
3997 C CB  . HIS A 513 ? 0.5061 0.2919 0.3238 -0.0283 -0.0058 0.0359  513 HIS A CB  
3998 C CG  . HIS A 513 ? 0.4720 0.2628 0.2875 -0.0258 -0.0178 0.0434  513 HIS A CG  
3999 N ND1 . HIS A 513 ? 0.5068 0.2861 0.2949 -0.0242 -0.0235 0.0494  513 HIS A ND1 
4000 C CD2 . HIS A 513 ? 0.4520 0.2586 0.2907 -0.0241 -0.0252 0.0458  513 HIS A CD2 
4001 C CE1 . HIS A 513 ? 0.4837 0.2722 0.2822 -0.0203 -0.0357 0.0562  513 HIS A CE1 
4002 N NE2 . HIS A 513 ? 0.5383 0.3436 0.3693 -0.0203 -0.0355 0.0530  513 HIS A NE2 
4003 N N   . VAL A 514 ? 0.5086 0.2679 0.3060 -0.0234 0.0190  0.0506  514 VAL A N   
4004 C CA  . VAL A 514 ? 0.5558 0.2946 0.3245 -0.0229 0.0273  0.0596  514 VAL A CA  
4005 C C   . VAL A 514 ? 0.5362 0.2721 0.2926 -0.0180 0.0116  0.0722  514 VAL A C   
4006 O O   . VAL A 514 ? 0.5594 0.3109 0.3387 -0.0148 -0.0018 0.0726  514 VAL A O   
4007 C CB  . VAL A 514 ? 0.5312 0.2632 0.3151 -0.0239 0.0470  0.0610  514 VAL A CB  
4008 C CG1 . VAL A 514 ? 0.4607 0.2014 0.2660 -0.0276 0.0594  0.0480  514 VAL A CG1 
4009 C CG2 . VAL A 514 ? 0.5300 0.2698 0.3431 -0.0206 0.0434  0.0652  514 VAL A CG2 
4010 N N   . ASN A 515 ? 0.5580 0.2738 0.2780 -0.0172 0.0141  0.0830  515 ASN A N   
4011 C CA  . ASN A 515 ? 0.6438 0.3540 0.3502 -0.0107 -0.0016 0.0986  515 ASN A CA  
4012 C C   . ASN A 515 ? 0.6914 0.3744 0.3670 -0.0102 0.0124  0.1134  515 ASN A C   
4013 O O   . ASN A 515 ? 0.6946 0.3624 0.3257 -0.0142 0.0173  0.1153  515 ASN A O   
4014 C CB  . ASN A 515 ? 0.6155 0.3324 0.2978 -0.0109 -0.0236 0.0972  515 ASN A CB  
4015 C CG  . ASN A 515 ? 0.6858 0.4002 0.3566 -0.0029 -0.0436 0.1140  515 ASN A CG  
4016 O OD1 . ASN A 515 ? 0.6537 0.3674 0.3496 0.0044  -0.0439 0.1247  515 ASN A OD1 
4017 N ND2 . ASN A 515 ? 0.6625 0.3759 0.2970 -0.0039 -0.0612 0.1155  515 ASN A ND2 
4018 N N   . TRP A 516 ? 0.6129 0.2884 0.3116 -0.0061 0.0206  0.1231  516 TRP A N   
4019 C CA  . TRP A 516 ? 0.7013 0.3591 0.3838 -0.0054 0.0331  0.1369  516 TRP A CA  
4020 C C   . TRP A 516 ? 0.7064 0.3614 0.3692 0.0029  0.0135  0.1552  516 TRP A C   
4021 O O   . TRP A 516 ? 0.7393 0.3815 0.3866 0.0036  0.0213  0.1690  516 TRP A O   
4022 C CB  . TRP A 516 ? 0.6107 0.2654 0.3341 -0.0053 0.0498  0.1377  516 TRP A CB  
4023 C CG  . TRP A 516 ? 0.6521 0.3153 0.4083 -0.0117 0.0651  0.1200  516 TRP A CG  
4024 C CD1 . TRP A 516 ? 0.6398 0.3107 0.4396 -0.0109 0.0686  0.1136  516 TRP A CD1 
4025 C CD2 . TRP A 516 ? 0.6223 0.2880 0.3725 -0.0199 0.0789  0.1062  516 TRP A CD2 
4026 N NE1 . TRP A 516 ? 0.6432 0.3281 0.4658 -0.0181 0.0799  0.0959  516 TRP A NE1 
4027 C CE2 . TRP A 516 ? 0.6134 0.2965 0.4098 -0.0228 0.0859  0.0917  516 TRP A CE2 
4028 C CE3 . TRP A 516 ? 0.6760 0.3348 0.3903 -0.0246 0.0852  0.1025  516 TRP A CE3 
4029 C CZ2 . TRP A 516 ? 0.5528 0.2489 0.3640 -0.0288 0.0963  0.0758  516 TRP A CZ2 
4030 C CZ3 . TRP A 516 ? 0.7030 0.3735 0.4352 -0.0305 0.0982  0.0853  516 TRP A CZ3 
4031 C CH2 . TRP A 516 ? 0.5797 0.2691 0.3610 -0.0318 0.1025  0.0733  516 TRP A CH2 
4032 N N   . PHE A 517 ? 0.6932 0.3610 0.3585 0.0089  -0.0121 0.1563  517 PHE A N   
4033 C CA  . PHE A 517 ? 0.7750 0.4453 0.4419 0.0196  -0.0322 0.1741  517 PHE A CA  
4034 C C   . PHE A 517 ? 0.7396 0.4184 0.3688 0.0206  -0.0554 0.1765  517 PHE A C   
4035 O O   . PHE A 517 ? 0.8344 0.5226 0.4704 0.0302  -0.0778 0.1883  517 PHE A O   
4036 C CB  . PHE A 517 ? 0.7269 0.4077 0.4417 0.0278  -0.0432 0.1733  517 PHE A CB  
4037 C CG  . PHE A 517 ? 0.6836 0.3566 0.4359 0.0265  -0.0214 0.1686  517 PHE A CG  
4038 C CD1 . PHE A 517 ? 0.7433 0.4033 0.5137 0.0315  -0.0120 0.1821  517 PHE A CD1 
4039 C CD2 . PHE A 517 ? 0.6627 0.3483 0.4382 0.0191  -0.0105 0.1482  517 PHE A CD2 
4040 C CE1 . PHE A 517 ? 0.6999 0.3541 0.5067 0.0284  0.0075  0.1740  517 PHE A CE1 
4041 C CE2 . PHE A 517 ? 0.6483 0.3325 0.4597 0.0167  0.0082  0.1406  517 PHE A CE2 
4042 C CZ  . PHE A 517 ? 0.6710 0.3349 0.4951 0.0214  0.0180  0.1534  517 PHE A CZ  
4043 N N   . ARG A 518 ? 0.7593 0.4356 0.3514 0.0108  -0.0505 0.1642  518 ARG A N   
4044 C CA  . ARG A 518 ? 0.8349 0.5191 0.3899 0.0097  -0.0716 0.1630  518 ARG A CA  
4045 C C   . ARG A 518 ? 0.9599 0.6353 0.4823 0.0140  -0.0737 0.1823  518 ARG A C   
4046 O O   . ARG A 518 ? 0.9963 0.6542 0.5077 0.0118  -0.0513 0.1911  518 ARG A O   
4047 C CB  . ARG A 518 ? 0.9253 0.6058 0.4502 -0.0025 -0.0626 0.1427  518 ARG A CB  
4048 C CG  . ARG A 518 ? 0.9487 0.6405 0.4430 -0.0059 -0.0859 0.1345  518 ARG A CG  
4049 C CD  . ARG A 518 ? 0.9497 0.6367 0.4234 -0.0180 -0.0758 0.1115  518 ARG A CD  
4050 N NE  . ARG A 518 ? 0.9144 0.6130 0.3636 -0.0227 -0.0980 0.1003  518 ARG A NE  
4051 C CZ  . ARG A 518 ? 0.9490 0.6472 0.3864 -0.0330 -0.0961 0.0781  518 ARG A CZ  
4052 N NH1 . ARG A 518 ? 0.9343 0.6205 0.3799 -0.0387 -0.0736 0.0661  518 ARG A NH1 
4053 N NH2 . ARG A 518 ? 0.9800 0.6908 0.3996 -0.0377 -0.1172 0.0670  518 ARG A NH2 
4054 N N   . LYS A 519 ? 0.9806 0.6696 0.4893 0.0198  -0.1014 0.1894  519 LYS A N   
4055 C CA  . LYS A 519 ? 1.1356 0.8195 0.6144 0.0259  -0.1083 0.2110  519 LYS A CA  
4056 C C   . LYS A 519 ? 1.1766 0.8677 0.6044 0.0201  -0.1231 0.2038  519 LYS A C   
4057 O O   . LYS A 519 ? 1.2369 0.9410 0.6621 0.0134  -0.1344 0.1828  519 LYS A O   
4058 C CB  . LYS A 519 ? 1.1229 0.8180 0.6369 0.0417  -0.1293 0.2303  519 LYS A CB  
4059 C CG  . LYS A 519 ? 1.0629 0.7491 0.6276 0.0479  -0.1140 0.2375  519 LYS A CG  
4060 C CD  . LYS A 519 ? 1.0716 0.7668 0.6718 0.0650  -0.1332 0.2559  519 LYS A CD  
4061 C CE  . LYS A 519 ? 1.1217 0.8055 0.7726 0.0705  -0.1157 0.2608  519 LYS A CE  
4062 N NZ  . LYS A 519 ? 1.1580 0.8472 0.8458 0.0891  -0.1312 0.2777  519 LYS A NZ  
4063 N N   . ASP A 520 ? 1.3160 0.9984 0.7033 0.0221  -0.1226 0.2215  520 ASP A N   
4064 C CA  . ASP A 520 ? 1.4511 1.1397 0.7849 0.0168  -0.1357 0.2161  520 ASP A CA  
4065 C C   . ASP A 520 ? 1.5098 1.2221 0.8484 0.0281  -0.1726 0.2274  520 ASP A C   
4066 O O   . ASP A 520 ? 1.4842 1.2088 0.8713 0.0395  -0.1874 0.2354  520 ASP A O   
4067 C CB  . ASP A 520 ? 1.4843 1.1514 0.7675 0.0117  -0.1140 0.2283  520 ASP A CB  
4068 C CG  . ASP A 520 ? 1.4472 1.1039 0.7366 0.0226  -0.1120 0.2617  520 ASP A CG  
4069 O OD1 . ASP A 520 ? 1.4197 1.0854 0.7541 0.0353  -0.1270 0.2747  520 ASP A OD1 
4070 O OD2 . ASP A 520 ? 1.5543 1.1929 0.8047 0.0183  -0.0943 0.2750  520 ASP A OD2 
4071 N N   . LYS A 521 ? 1.5477 1.2676 0.8366 0.0253  -0.1875 0.2269  521 LYS A N   
4072 C CA  . LYS A 521 ? 1.6292 1.3740 0.9205 0.0363  -0.2237 0.2376  521 LYS A CA  
4073 C C   . LYS A 521 ? 1.6477 1.3867 0.9493 0.0529  -0.2285 0.2729  521 LYS A C   
4074 O O   . LYS A 521 ? 1.6606 1.4199 0.9909 0.0666  -0.2563 0.2838  521 LYS A O   
4075 C CB  . LYS A 521 ? 1.6522 1.4065 0.8836 0.0287  -0.2374 0.2282  521 LYS A CB  
4076 C CG  . LYS A 521 ? 1.6622 1.4188 0.8800 0.0118  -0.2299 0.1928  521 LYS A CG  
4077 C CD  . LYS A 521 ? 1.7439 1.5067 0.8982 0.0041  -0.2390 0.1835  521 LYS A CD  
4078 C CE  . LYS A 521 ? 1.7573 1.5187 0.8991 -0.0126 -0.2277 0.1474  521 LYS A CE  
4079 N NZ  . LYS A 521 ? 1.6900 1.4558 0.7685 -0.0206 -0.2332 0.1360  521 LYS A NZ  
4080 N N   . ASN A 522 ? 1.6483 1.3600 0.9307 0.0518  -0.2012 0.2909  522 ASN A N   
4081 C CA  . ASN A 522 ? 1.6307 1.3328 0.9226 0.0666  -0.2026 0.3261  522 ASN A CA  
4082 C C   . ASN A 522 ? 1.6296 1.3301 0.9922 0.0776  -0.1987 0.3324  522 ASN A C   
4083 O O   . ASN A 522 ? 1.6253 1.3249 1.0096 0.0940  -0.2086 0.3588  522 ASN A O   
4084 C CB  . ASN A 522 ? 1.6774 1.3504 0.9268 0.0592  -0.1732 0.3426  522 ASN A CB  
4085 C CG  . ASN A 522 ? 1.8115 1.4844 0.9870 0.0491  -0.1747 0.3376  522 ASN A CG  
4086 O OD1 . ASN A 522 ? 1.9315 1.6268 1.0837 0.0520  -0.2036 0.3319  522 ASN A OD1 
4087 N ND2 . ASN A 522 ? 1.7375 1.3863 0.8773 0.0369  -0.1432 0.3382  522 ASN A ND2 
4088 N N   . GLY A 523 ? 1.5533 1.2528 0.9516 0.0697  -0.1840 0.3091  523 GLY A N   
4089 C CA  . GLY A 523 ? 1.4908 1.1890 0.9539 0.0785  -0.1785 0.3115  523 GLY A CA  
4090 C C   . GLY A 523 ? 1.3989 1.0710 0.8783 0.0725  -0.1438 0.3154  523 GLY A C   
4091 O O   . GLY A 523 ? 1.3459 1.0147 0.8784 0.0803  -0.1378 0.3195  523 GLY A O   
4092 N N   . LYS A 524 ? 1.3563 1.0103 0.7942 0.0586  -0.1206 0.3125  524 LYS A N   
4093 C CA  . LYS A 524 ? 1.3169 0.9478 0.7707 0.0505  -0.0877 0.3133  524 LYS A CA  
4094 C C   . LYS A 524 ? 1.1608 0.7917 0.6160 0.0368  -0.0696 0.2821  524 LYS A C   
4095 O O   . LYS A 524 ? 1.2067 0.8489 0.6351 0.0306  -0.0779 0.2630  524 LYS A O   
4096 C CB  . LYS A 524 ? 1.3630 0.9718 0.7734 0.0452  -0.0718 0.3343  524 LYS A CB  
4097 C CG  . LYS A 524 ? 1.3874 0.9963 0.7310 0.0349  -0.0699 0.3251  524 LYS A CG  
4098 C CD  . LYS A 524 ? 1.5378 1.1250 0.8383 0.0307  -0.0547 0.3489  524 LYS A CD  
4099 C CE  . LYS A 524 ? 1.5305 1.1177 0.7623 0.0206  -0.0515 0.3386  524 LYS A CE  
4100 N NZ  . LYS A 524 ? 1.5730 1.1394 0.7594 0.0164  -0.0361 0.3631  524 LYS A NZ  
4101 N N   . PHE A 525 ? 1.1767 0.7948 0.6657 0.0319  -0.0447 0.2768  525 PHE A N   
4102 C CA  . PHE A 525 ? 1.0175 0.6371 0.5164 0.0213  -0.0273 0.2491  525 PHE A CA  
4103 C C   . PHE A 525 ? 1.0276 0.6376 0.4762 0.0089  -0.0099 0.2382  525 PHE A C   
4104 O O   . PHE A 525 ? 1.1919 0.7858 0.6093 0.0053  0.0036  0.2519  525 PHE A O   
4105 C CB  . PHE A 525 ? 1.0250 0.6347 0.5715 0.0192  -0.0051 0.2461  525 PHE A CB  
4106 C CG  . PHE A 525 ? 0.9917 0.6099 0.5913 0.0301  -0.0185 0.2509  525 PHE A CG  
4107 C CD1 . PHE A 525 ? 0.9045 0.5402 0.5322 0.0320  -0.0282 0.2328  525 PHE A CD1 
4108 C CD2 . PHE A 525 ? 1.0145 0.6216 0.6368 0.0378  -0.0205 0.2734  525 PHE A CD2 
4109 C CE1 . PHE A 525 ? 0.9320 0.5748 0.6083 0.0420  -0.0382 0.2356  525 PHE A CE1 
4110 C CE2 . PHE A 525 ? 1.0549 0.6682 0.7289 0.0481  -0.0311 0.2758  525 PHE A CE2 
4111 C CZ  . PHE A 525 ? 0.9746 0.6064 0.6752 0.0505  -0.0389 0.2561  525 PHE A CZ  
4112 N N   . LEU A 526 ? 1.0087 0.6274 0.4506 0.0021  -0.0094 0.2134  526 LEU A N   
4113 C CA  . LEU A 526 ? 1.0723 0.6817 0.4730 -0.0095 0.0093  0.1988  526 LEU A CA  
4114 C C   . LEU A 526 ? 1.1075 0.7045 0.5287 -0.0174 0.0433  0.1881  526 LEU A C   
4115 O O   . LEU A 526 ? 1.1558 0.7414 0.5467 -0.0263 0.0648  0.1806  526 LEU A O   
4116 C CB  . LEU A 526 ? 0.9992 0.6220 0.3863 -0.0136 -0.0051 0.1764  526 LEU A CB  
4117 C CG  . LEU A 526 ? 1.1988 0.8358 0.5572 -0.0096 -0.0371 0.1803  526 LEU A CG  
4118 C CD1 . LEU A 526 ? 1.2460 0.8977 0.6105 -0.0141 -0.0517 0.1564  526 LEU A CD1 
4119 C CD2 . LEU A 526 ? 1.2570 0.8844 0.5561 -0.0144 -0.0322 0.1864  526 LEU A CD2 
4120 N N   . TRP A 527 ? 0.9494 0.5501 0.4229 -0.0144 0.0487  0.1860  527 TRP A N   
4121 C CA  . TRP A 527 ? 0.9530 0.5475 0.4540 -0.0214 0.0779  0.1735  527 TRP A CA  
4122 C C   . TRP A 527 ? 0.9506 0.5362 0.4838 -0.0191 0.0891  0.1881  527 TRP A C   
4123 O O   . TRP A 527 ? 0.9507 0.5414 0.5121 -0.0106 0.0727  0.1993  527 TRP A O   
4124 C CB  . TRP A 527 ? 0.8951 0.5041 0.4317 -0.0219 0.0749  0.1539  527 TRP A CB  
4125 C CG  . TRP A 527 ? 0.8743 0.4819 0.4411 -0.0289 0.1024  0.1392  527 TRP A CG  
4126 C CD1 . TRP A 527 ? 0.8410 0.4564 0.4591 -0.0278 0.1081  0.1346  527 TRP A CD1 
4127 C CD2 . TRP A 527 ? 0.8692 0.4692 0.4200 -0.0379 0.1275  0.1260  527 TRP A CD2 
4128 N NE1 . TRP A 527 ? 0.8343 0.4497 0.4705 -0.0355 0.1333  0.1200  527 TRP A NE1 
4129 C CE2 . TRP A 527 ? 0.8337 0.4394 0.4313 -0.0414 0.1464  0.1148  527 TRP A CE2 
4130 C CE3 . TRP A 527 ? 0.9274 0.5176 0.4311 -0.0436 0.1363  0.1211  527 TRP A CE3 
4131 C CZ2 . TRP A 527 ? 0.7963 0.3993 0.3990 -0.0494 0.1735  0.1001  527 TRP A CZ2 
4132 C CZ3 . TRP A 527 ? 0.9296 0.5149 0.4366 -0.0519 0.1652  0.1055  527 TRP A CZ3 
4133 C CH2 . TRP A 527 ? 0.8754 0.4675 0.4335 -0.0543 0.1834  0.0957  527 TRP A CH2 
4134 N N   . PRO A 528 ? 0.9855 0.5574 0.5177 -0.0267 0.1172  0.1875  528 PRO A N   
4135 C CA  . PRO A 528 ? 0.9779 0.5397 0.5424 -0.0259 0.1282  0.1998  528 PRO A CA  
4136 C C   . PRO A 528 ? 0.9208 0.4941 0.5448 -0.0243 0.1294  0.1875  528 PRO A C   
4137 O O   . PRO A 528 ? 0.8378 0.4061 0.4913 -0.0202 0.1264  0.1979  528 PRO A O   
4138 C CB  . PRO A 528 ? 0.9273 0.4738 0.4756 -0.0363 0.1597  0.1972  528 PRO A CB  
4139 C CG  . PRO A 528 ? 1.0316 0.5848 0.5594 -0.0424 0.1688  0.1762  528 PRO A CG  
4140 C CD  . PRO A 528 ? 0.9596 0.5231 0.4597 -0.0365 0.1402  0.1763  528 PRO A CD  
4141 N N   . GLY A 529 ? 0.8451 0.4331 0.4874 -0.0277 0.1337  0.1656  529 GLY A N   
4142 C CA  . GLY A 529 ? 0.8088 0.4106 0.5037 -0.0262 0.1319  0.1538  529 GLY A CA  
4143 C C   . GLY A 529 ? 0.7720 0.3697 0.5055 -0.0318 0.1541  0.1489  529 GLY A C   
4144 O O   . GLY A 529 ? 0.7799 0.3650 0.5031 -0.0383 0.1754  0.1511  529 GLY A O   
4145 N N   . PHE A 530 ? 0.7331 0.3422 0.5120 -0.0296 0.1490  0.1407  530 PHE A N   
4146 C CA  . PHE A 530 ? 0.7329 0.3427 0.5549 -0.0351 0.1668  0.1315  530 PHE A CA  
4147 C C   . PHE A 530 ? 0.7616 0.3774 0.5928 -0.0450 0.1901  0.1154  530 PHE A C   
4148 O O   . PHE A 530 ? 0.7424 0.3755 0.5844 -0.0472 0.1888  0.0998  530 PHE A O   
4149 C CB  . PHE A 530 ? 0.7437 0.3317 0.5638 -0.0336 0.1722  0.1494  530 PHE A CB  
4150 C CG  . PHE A 530 ? 0.7404 0.3219 0.5576 -0.0229 0.1493  0.1658  530 PHE A CG  
4151 C CD1 . PHE A 530 ? 0.7051 0.2962 0.5626 -0.0183 0.1400  0.1573  530 PHE A CD1 
4152 C CD2 . PHE A 530 ? 0.7688 0.3360 0.5444 -0.0174 0.1369  0.1890  530 PHE A CD2 
4153 C CE1 . PHE A 530 ? 0.7478 0.3328 0.6074 -0.0076 0.1201  0.1710  530 PHE A CE1 
4154 C CE2 . PHE A 530 ? 0.7779 0.3410 0.5564 -0.0067 0.1143  0.2044  530 PHE A CE2 
4155 C CZ  . PHE A 530 ? 0.7663 0.3374 0.5883 -0.0014 0.1065  0.1951  530 PHE A CZ  
4156 N N   . GLY A 531 ? 0.7294 0.3310 0.5589 -0.0509 0.2117  0.1196  531 GLY A N   
4157 C CA  . GLY A 531 ? 0.7649 0.3730 0.6092 -0.0602 0.2355  0.1037  531 GLY A CA  
4158 C C   . GLY A 531 ? 0.7625 0.3725 0.5731 -0.0615 0.2383  0.0990  531 GLY A C   
4159 O O   . GLY A 531 ? 0.7313 0.3552 0.5642 -0.0669 0.2507  0.0812  531 GLY A O   
4160 N N   . GLU A 532 ? 0.7967 0.3937 0.5554 -0.0569 0.2262  0.1140  532 GLU A N   
4161 C CA  . GLU A 532 ? 0.7688 0.3653 0.4916 -0.0588 0.2292  0.1078  532 GLU A CA  
4162 C C   . GLU A 532 ? 0.7571 0.3722 0.4924 -0.0561 0.2142  0.0945  532 GLU A C   
4163 O O   . GLU A 532 ? 0.7538 0.3704 0.4719 -0.0590 0.2206  0.0843  532 GLU A O   
4164 C CB  . GLU A 532 ? 0.8514 0.4307 0.5140 -0.0554 0.2186  0.1263  532 GLU A CB  
4165 C CG  . GLU A 532 ? 0.8744 0.4327 0.5172 -0.0587 0.2334  0.1427  532 GLU A CG  
4166 C CD  . GLU A 532 ? 0.8749 0.4278 0.5260 -0.0689 0.2669  0.1311  532 GLU A CD  
4167 O OE1 . GLU A 532 ? 0.9084 0.4697 0.5602 -0.0730 0.2779  0.1130  532 GLU A OE1 
4168 O OE2 . GLU A 532 ? 0.9659 0.5057 0.6256 -0.0729 0.2831  0.1399  532 GLU A OE2 
4169 N N   . ASN A 533 ? 0.7099 0.3378 0.4749 -0.0510 0.1957  0.0940  533 ASN A N   
4170 C CA  . ASN A 533 ? 0.6813 0.3263 0.4613 -0.0494 0.1826  0.0820  533 ASN A CA  
4171 C C   . ASN A 533 ? 0.6882 0.3471 0.5039 -0.0562 0.2000  0.0632  533 ASN A C   
4172 O O   . ASN A 533 ? 0.6202 0.2904 0.4443 -0.0559 0.1921  0.0540  533 ASN A O   
4173 C CB  . ASN A 533 ? 0.6237 0.2797 0.4316 -0.0437 0.1626  0.0840  533 ASN A CB  
4174 C CG  . ASN A 533 ? 0.7043 0.3506 0.4837 -0.0355 0.1425  0.1017  533 ASN A CG  
4175 O OD1 . ASN A 533 ? 0.7497 0.3865 0.4852 -0.0335 0.1356  0.1102  533 ASN A OD1 
4176 N ND2 . ASN A 533 ? 0.6506 0.3004 0.4571 -0.0308 0.1326  0.1059  533 ASN A ND2 
4177 N N   . SER A 534 ? 0.6923 0.3512 0.5323 -0.0624 0.2229  0.0575  534 SER A N   
4178 C CA  . SER A 534 ? 0.7481 0.4229 0.6262 -0.0688 0.2399  0.0393  534 SER A CA  
4179 C C   . SER A 534 ? 0.6723 0.3418 0.5231 -0.0703 0.2494  0.0338  534 SER A C   
4180 O O   . SER A 534 ? 0.6703 0.3575 0.5535 -0.0719 0.2535  0.0190  534 SER A O   
4181 C CB  . SER A 534 ? 0.6699 0.3445 0.5770 -0.0752 0.2633  0.0343  534 SER A CB  
4182 O OG  . SER A 534 ? 0.7000 0.3505 0.5655 -0.0768 0.2780  0.0455  534 SER A OG  
4183 N N   . ARG A 535 ? 0.7064 0.3547 0.5005 -0.0690 0.2507  0.0442  535 ARG A N   
4184 C CA  . ARG A 535 ? 0.6852 0.3274 0.4484 -0.0709 0.2595  0.0365  535 ARG A CA  
4185 C C   . ARG A 535 ? 0.7378 0.3935 0.5029 -0.0650 0.2357  0.0304  535 ARG A C   
4186 O O   . ARG A 535 ? 0.6373 0.3037 0.4133 -0.0642 0.2394  0.0147  535 ARG A O   
4187 C CB  . ARG A 535 ? 0.7916 0.4108 0.4914 -0.0709 0.2601  0.0480  535 ARG A CB  
4188 C CG  . ARG A 535 ? 0.8149 0.4217 0.5114 -0.0751 0.2790  0.0555  535 ARG A CG  
4189 C CD  . ARG A 535 ? 0.9006 0.4863 0.5336 -0.0740 0.2721  0.0723  535 ARG A CD  
4190 N NE  . ARG A 535 ? 0.9206 0.4924 0.5496 -0.0777 0.2883  0.0839  535 ARG A NE  
4191 C CZ  . ARG A 535 ? 0.9640 0.5257 0.5829 -0.0855 0.3161  0.0787  535 ARG A CZ  
4192 N NH1 . ARG A 535 ? 1.0050 0.5698 0.6198 -0.0901 0.3316  0.0605  535 ARG A NH1 
4193 N NH2 . ARG A 535 ? 0.9400 0.4874 0.5545 -0.0890 0.3296  0.0918  535 ARG A NH2 
4194 N N   . VAL A 536 ? 0.6956 0.3557 0.4572 -0.0587 0.2076  0.0401  536 VAL A N   
4195 C CA  . VAL A 536 ? 0.6329 0.3120 0.4047 -0.0520 0.1812  0.0326  536 VAL A CA  
4196 C C   . VAL A 536 ? 0.6038 0.3110 0.4361 -0.0502 0.1777  0.0192  536 VAL A C   
4197 O O   . VAL A 536 ? 0.6344 0.3555 0.4818 -0.0468 0.1700  0.0082  536 VAL A O   
4198 C CB  . VAL A 536 ? 0.6672 0.3440 0.4198 -0.0465 0.1547  0.0464  536 VAL A CB  
4199 C CG1 . VAL A 536 ? 0.6533 0.3494 0.4182 -0.0414 0.1304  0.0388  536 VAL A CG1 
4200 C CG2 . VAL A 536 ? 0.7298 0.3808 0.4219 -0.0473 0.1543  0.0609  536 VAL A CG2 
4201 N N   . LEU A 537 ? 0.6472 0.3624 0.5148 -0.0525 0.1828  0.0198  537 LEU A N   
4202 C CA  . LEU A 537 ? 0.5982 0.3420 0.5210 -0.0515 0.1777  0.0067  537 LEU A CA  
4203 C C   . LEU A 537 ? 0.5914 0.3447 0.5400 -0.0531 0.1951  -0.0073 537 LEU A C   
4204 O O   . LEU A 537 ? 0.5767 0.3533 0.5608 -0.0486 0.1840  -0.0173 537 LEU A O   
4205 C CB  . LEU A 537 ? 0.5810 0.3302 0.5352 -0.0558 0.1820  0.0071  537 LEU A CB  
4206 C CG  . LEU A 537 ? 0.6146 0.3749 0.5773 -0.0520 0.1584  0.0101  537 LEU A CG  
4207 C CD1 . LEU A 537 ? 0.6878 0.4302 0.6065 -0.0472 0.1455  0.0249  537 LEU A CD1 
4208 C CD2 . LEU A 537 ? 0.7221 0.4855 0.7175 -0.0578 0.1667  0.0067  537 LEU A CD2 
4209 N N   . GLU A 538 ? 0.5992 0.3345 0.5310 -0.0592 0.2228  -0.0077 538 GLU A N   
4210 C CA  . GLU A 538 ? 0.5893 0.3332 0.5473 -0.0605 0.2424  -0.0228 538 GLU A CA  
4211 C C   . GLU A 538 ? 0.6381 0.3857 0.5867 -0.0530 0.2297  -0.0295 538 GLU A C   
4212 O O   . GLU A 538 ? 0.5550 0.3225 0.5473 -0.0484 0.2288  -0.0419 538 GLU A O   
4213 C CB  . GLU A 538 ? 0.6438 0.3640 0.5749 -0.0694 0.2770  -0.0214 538 GLU A CB  
4214 C CG  . GLU A 538 ? 0.7072 0.4356 0.6656 -0.0710 0.3015  -0.0389 538 GLU A CG  
4215 C CD  . GLU A 538 ? 0.8289 0.5332 0.7569 -0.0815 0.3395  -0.0381 538 GLU A CD  
4216 O OE1 . GLU A 538 ? 0.8374 0.5140 0.7031 -0.0842 0.3393  -0.0233 538 GLU A OE1 
4217 O OE2 . GLU A 538 ? 0.9049 0.6199 0.8730 -0.0852 0.3641  -0.0527 538 GLU A OE2 
4218 N N   . TRP A 539 ? 0.6319 0.3606 0.5268 -0.0515 0.2187  -0.0216 539 TRP A N   
4219 C CA  . TRP A 539 ? 0.6179 0.3473 0.5039 -0.0460 0.2070  -0.0289 539 TRP A CA  
4220 C C   . TRP A 539 ? 0.6261 0.3786 0.5498 -0.0383 0.1804  -0.0295 539 TRP A C   
4221 O O   . TRP A 539 ? 0.5697 0.3310 0.5185 -0.0329 0.1772  -0.0387 539 TRP A O   
4222 C CB  . TRP A 539 ? 0.6616 0.3685 0.4840 -0.0476 0.1980  -0.0209 539 TRP A CB  
4223 C CG  . TRP A 539 ? 0.6654 0.3700 0.4774 -0.0443 0.1881  -0.0305 539 TRP A CG  
4224 C CD1 . TRP A 539 ? 0.6848 0.3795 0.4886 -0.0459 0.2063  -0.0456 539 TRP A CD1 
4225 C CD2 . TRP A 539 ? 0.6184 0.3293 0.4290 -0.0398 0.1598  -0.0271 539 TRP A CD2 
4226 N NE1 . TRP A 539 ? 0.6420 0.3350 0.4406 -0.0426 0.1901  -0.0519 539 TRP A NE1 
4227 C CE2 . TRP A 539 ? 0.6621 0.3650 0.4648 -0.0392 0.1617  -0.0399 539 TRP A CE2 
4228 C CE3 . TRP A 539 ? 0.6037 0.3257 0.4206 -0.0369 0.1351  -0.0154 539 TRP A CE3 
4229 C CZ2 . TRP A 539 ? 0.6869 0.3916 0.4886 -0.0365 0.1395  -0.0402 539 TRP A CZ2 
4230 C CZ3 . TRP A 539 ? 0.5763 0.3019 0.3912 -0.0342 0.1142  -0.0156 539 TRP A CZ3 
4231 C CH2 . TRP A 539 ? 0.6678 0.3842 0.4755 -0.0343 0.1163  -0.0273 539 TRP A CH2 
4232 N N   . MET A 540 ? 0.5635 0.3249 0.4911 -0.0376 0.1622  -0.0194 540 MET A N   
4233 C CA  . MET A 540 ? 0.5506 0.3339 0.5089 -0.0317 0.1387  -0.0192 540 MET A CA  
4234 C C   . MET A 540 ? 0.5095 0.3160 0.5232 -0.0291 0.1429  -0.0290 540 MET A C   
4235 O O   . MET A 540 ? 0.5070 0.3275 0.5448 -0.0223 0.1286  -0.0313 540 MET A O   
4236 C CB  . MET A 540 ? 0.5091 0.2976 0.4614 -0.0328 0.1230  -0.0093 540 MET A CB  
4237 C CG  . MET A 540 ? 0.5533 0.3236 0.4593 -0.0337 0.1149  0.0014  540 MET A CG  
4238 S SD  . MET A 540 ? 0.5958 0.3739 0.5076 -0.0340 0.1015  0.0103  540 MET A SD  
4239 C CE  . MET A 540 ? 0.5994 0.3556 0.4611 -0.0335 0.0941  0.0229  540 MET A CE  
4240 N N   . PHE A 541 ? 0.5113 0.3225 0.5475 -0.0344 0.1616  -0.0339 541 PHE A N   
4241 C CA  . PHE A 541 ? 0.5122 0.3492 0.6068 -0.0326 0.1653  -0.0448 541 PHE A CA  
4242 C C   . PHE A 541 ? 0.5163 0.3555 0.6307 -0.0259 0.1720  -0.0538 541 PHE A C   
4243 O O   . PHE A 541 ? 0.4770 0.3378 0.6319 -0.0180 0.1576  -0.0573 541 PHE A O   
4244 C CB  . PHE A 541 ? 0.4721 0.3099 0.5861 -0.0417 0.1895  -0.0499 541 PHE A CB  
4245 C CG  . PHE A 541 ? 0.5004 0.3705 0.6792 -0.0419 0.1881  -0.0614 541 PHE A CG  
4246 C CD1 . PHE A 541 ? 0.4788 0.3647 0.7014 -0.0373 0.1973  -0.0732 541 PHE A CD1 
4247 C CD2 . PHE A 541 ? 0.5171 0.4028 0.7155 -0.0466 0.1774  -0.0620 541 PHE A CD2 
4248 C CE1 . PHE A 541 ? 0.4903 0.4097 0.7765 -0.0370 0.1931  -0.0839 541 PHE A CE1 
4249 C CE2 . PHE A 541 ? 0.4456 0.3635 0.7035 -0.0479 0.1735  -0.0744 541 PHE A CE2 
4250 C CZ  . PHE A 541 ? 0.4765 0.4126 0.7790 -0.0428 0.1802  -0.0847 541 PHE A CZ  
4251 N N   . GLY A 542 ? 0.5355 0.3516 0.6208 -0.0286 0.1937  -0.0576 542 GLY A N   
4252 C CA  . GLY A 542 ? 0.5583 0.3728 0.6613 -0.0225 0.2030  -0.0686 542 GLY A CA  
4253 C C   . GLY A 542 ? 0.5659 0.3783 0.6621 -0.0137 0.1788  -0.0644 542 GLY A C   
4254 O O   . GLY A 542 ? 0.5348 0.3562 0.6692 -0.0049 0.1763  -0.0709 542 GLY A O   
4255 N N   . ARG A 543 ? 0.5669 0.3671 0.6184 -0.0157 0.1613  -0.0530 543 ARG A N   
4256 C CA  . ARG A 543 ? 0.5431 0.3406 0.5890 -0.0093 0.1395  -0.0482 543 ARG A CA  
4257 C C   . ARG A 543 ? 0.5326 0.3554 0.6215 -0.0016 0.1182  -0.0427 543 ARG A C   
4258 O O   . ARG A 543 ? 0.5494 0.3731 0.6565 0.0065  0.1074  -0.0415 543 ARG A O   
4259 C CB  . ARG A 543 ? 0.5311 0.3142 0.5255 -0.0143 0.1261  -0.0380 543 ARG A CB  
4260 C CG  . ARG A 543 ? 0.6387 0.3961 0.5860 -0.0202 0.1400  -0.0430 543 ARG A CG  
4261 C CD  . ARG A 543 ? 0.6214 0.3672 0.5745 -0.0168 0.1465  -0.0550 543 ARG A CD  
4262 N NE  . ARG A 543 ? 0.5854 0.3307 0.5418 -0.0128 0.1243  -0.0497 543 ARG A NE  
4263 C CZ  . ARG A 543 ? 0.6196 0.3574 0.5953 -0.0077 0.1249  -0.0572 543 ARG A CZ  
4264 N NH1 . ARG A 543 ? 0.6709 0.4028 0.6678 -0.0047 0.1460  -0.0719 543 ARG A NH1 
4265 N NH2 . ARG A 543 ? 0.6167 0.3517 0.5929 -0.0056 0.1055  -0.0499 543 ARG A NH2 
4266 N N   . ILE A 544 ? 0.5166 0.3588 0.6205 -0.0043 0.1117  -0.0392 544 ILE A N   
4267 C CA  . ILE A 544 ? 0.5117 0.3803 0.6524 0.0020  0.0906  -0.0352 544 ILE A CA  
4268 C C   . ILE A 544 ? 0.4833 0.3674 0.6786 0.0103  0.0961  -0.0440 544 ILE A C   
4269 O O   . ILE A 544 ? 0.4200 0.3166 0.6415 0.0200  0.0777  -0.0389 544 ILE A O   
4270 C CB  . ILE A 544 ? 0.5072 0.3928 0.6508 -0.0044 0.0841  -0.0335 544 ILE A CB  
4271 C CG1 . ILE A 544 ? 0.4860 0.3577 0.5822 -0.0099 0.0759  -0.0240 544 ILE A CG1 
4272 C CG2 . ILE A 544 ? 0.4619 0.3776 0.6428 0.0009  0.0628  -0.0324 544 ILE A CG2 
4273 C CD1 . ILE A 544 ? 0.4680 0.3524 0.5665 -0.0162 0.0719  -0.0240 544 ILE A CD1 
4274 N N   . GLU A 545 ? 0.4943 0.3776 0.7085 0.0069  0.1222  -0.0565 545 GLU A N   
4275 C CA  . GLU A 545 ? 0.4484 0.3467 0.7197 0.0151  0.1311  -0.0672 545 GLU A CA  
4276 C C   . GLU A 545 ? 0.4917 0.3714 0.7634 0.0239  0.1352  -0.0695 545 GLU A C   
4277 O O   . GLU A 545 ? 0.5524 0.4443 0.8765 0.0341  0.1381  -0.0765 545 GLU A O   
4278 C CB  . GLU A 545 ? 0.4847 0.3864 0.7760 0.0072  0.1624  -0.0812 545 GLU A CB  
4279 C CG  . GLU A 545 ? 0.4207 0.3463 0.7353 -0.0004 0.1598  -0.0827 545 GLU A CG  
4280 C CD  . GLU A 545 ? 0.4954 0.4302 0.8497 -0.0067 0.1907  -0.0978 545 GLU A CD  
4281 O OE1 . GLU A 545 ? 0.5740 0.4898 0.9184 -0.0083 0.2188  -0.1054 545 GLU A OE1 
4282 O OE2 . GLU A 545 ? 0.5839 0.5457 0.9802 -0.0109 0.1879  -0.1033 545 GLU A OE2 
4283 N N   . GLY A 546 ? 0.5704 0.4216 0.7894 0.0204  0.1353  -0.0651 546 GLY A N   
4284 C CA  . GLY A 546 ? 0.5576 0.3887 0.7759 0.0271  0.1389  -0.0690 546 GLY A CA  
4285 C C   . GLY A 546 ? 0.5364 0.3462 0.7398 0.0222  0.1708  -0.0860 546 GLY A C   
4286 O O   . GLY A 546 ? 0.6139 0.4120 0.8369 0.0292  0.1796  -0.0955 546 GLY A O   
4287 N N   . GLU A 547 ? 0.6064 0.4088 0.7745 0.0104  0.1891  -0.0900 547 GLU A N   
4288 C CA  . GLU A 547 ? 0.6584 0.4394 0.8025 0.0042  0.2205  -0.1055 547 GLU A CA  
4289 C C   . GLU A 547 ? 0.6805 0.4328 0.7715 0.0010  0.2158  -0.1065 547 GLU A C   
4290 O O   . GLU A 547 ? 0.6422 0.3896 0.6978 -0.0019 0.1933  -0.0932 547 GLU A O   
4291 C CB  . GLU A 547 ? 0.6485 0.4276 0.7647 -0.0080 0.2404  -0.1057 547 GLU A CB  
4292 C CG  . GLU A 547 ? 0.7560 0.5624 0.9280 -0.0077 0.2503  -0.1088 547 GLU A CG  
4293 C CD  . GLU A 547 ? 0.9159 0.7149 1.0617 -0.0209 0.2759  -0.1096 547 GLU A CD  
4294 O OE1 . GLU A 547 ? 0.9888 0.7606 1.0708 -0.0290 0.2867  -0.1072 547 GLU A OE1 
4295 O OE2 . GLU A 547 ? 0.9742 0.7943 1.1635 -0.0236 0.2847  -0.1121 547 GLU A OE2 
4296 N N   . ASP A 548 ? 0.7880 0.5227 0.8766 0.0009  0.2380  -0.1245 548 ASP A N   
4297 C CA  . ASP A 548 ? 0.8271 0.5348 0.8695 -0.0033 0.2355  -0.1306 548 ASP A CA  
4298 C C   . ASP A 548 ? 0.8155 0.5062 0.7876 -0.0172 0.2490  -0.1335 548 ASP A C   
4299 O O   . ASP A 548 ? 0.8644 0.5403 0.8112 -0.0235 0.2730  -0.1497 548 ASP A O   
4300 C CB  . ASP A 548 ? 0.8765 0.5804 0.9505 0.0021  0.2475  -0.1464 548 ASP A CB  
4301 C CG  . ASP A 548 ? 0.9481 0.6283 0.9811 -0.0031 0.2420  -0.1536 548 ASP A CG  
4302 O OD1 . ASP A 548 ? 1.0163 0.6889 1.0455 -0.0003 0.2182  -0.1440 548 ASP A OD1 
4303 O OD2 . ASP A 548 ? 0.9679 0.6378 0.9734 -0.0111 0.2615  -0.1691 548 ASP A OD2 
4304 N N   . SER A 549 ? 0.7763 0.4720 0.7164 -0.0220 0.2307  -0.1153 549 SER A N   
4305 C CA  . SER A 549 ? 0.7612 0.4430 0.6374 -0.0332 0.2389  -0.1118 549 SER A CA  
4306 C C   . SER A 549 ? 0.7453 0.4184 0.5741 -0.0370 0.2118  -0.1007 549 SER A C   
4307 O O   . SER A 549 ? 0.7460 0.4119 0.5265 -0.0439 0.2098  -0.0913 549 SER A O   
4308 C CB  . SER A 549 ? 0.6961 0.3907 0.5813 -0.0358 0.2471  -0.1004 549 SER A CB  
4309 O OG  . SER A 549 ? 0.6996 0.4142 0.6148 -0.0304 0.2213  -0.0849 549 SER A OG  
4310 N N   . ALA A 550 ? 0.7055 0.3790 0.5495 -0.0325 0.1914  -0.1010 550 ALA A N   
4311 C CA  . ALA A 550 ? 0.7401 0.4101 0.5510 -0.0360 0.1652  -0.0912 550 ALA A CA  
4312 C C   . ALA A 550 ? 0.7724 0.4232 0.5572 -0.0410 0.1645  -0.1073 550 ALA A C   
4313 O O   . ALA A 550 ? 0.7138 0.3554 0.5216 -0.0386 0.1789  -0.1242 550 ALA A O   
4314 C CB  . ALA A 550 ? 0.7028 0.3903 0.5515 -0.0291 0.1407  -0.0764 550 ALA A CB  
4315 N N   . LYS A 551 ? 0.7753 0.4209 0.5150 -0.0480 0.1472  -0.1029 551 LYS A N   
4316 C CA  . LYS A 551 ? 0.7554 0.3856 0.4680 -0.0550 0.1411  -0.1181 551 LYS A CA  
4317 C C   . LYS A 551 ? 0.7859 0.4246 0.5065 -0.0555 0.1115  -0.1069 551 LYS A C   
4318 O O   . LYS A 551 ? 0.7353 0.3883 0.4519 -0.0541 0.0955  -0.0883 551 LYS A O   
4319 C CB  . LYS A 551 ? 0.8028 0.4199 0.4485 -0.0649 0.1479  -0.1260 551 LYS A CB  
4320 C CG  . LYS A 551 ? 1.0264 0.6296 0.6392 -0.0741 0.1399  -0.1449 551 LYS A CG  
4321 C CD  . LYS A 551 ? 1.1324 0.7249 0.6727 -0.0837 0.1438  -0.1502 551 LYS A CD  
4322 C CE  . LYS A 551 ? 1.0736 0.6776 0.5871 -0.0827 0.1236  -0.1244 551 LYS A CE  
4323 N NZ  . LYS A 551 ? 1.2435 0.8360 0.6829 -0.0910 0.1241  -0.1256 551 LYS A NZ  
4324 N N   . LEU A 552 ? 0.7324 0.3616 0.4669 -0.0579 0.1061  -0.1191 552 LEU A N   
4325 C CA  . LEU A 552 ? 0.7543 0.3908 0.5037 -0.0594 0.0820  -0.1096 552 LEU A CA  
4326 C C   . LEU A 552 ? 0.7561 0.3923 0.4612 -0.0699 0.0651  -0.1135 552 LEU A C   
4327 O O   . LEU A 552 ? 0.8079 0.4297 0.4798 -0.0781 0.0705  -0.1332 552 LEU A O   
4328 C CB  . LEU A 552 ? 0.7455 0.3696 0.5331 -0.0580 0.0847  -0.1194 552 LEU A CB  
4329 C CG  . LEU A 552 ? 0.7271 0.3565 0.5351 -0.0603 0.0640  -0.1086 552 LEU A CG  
4330 C CD1 . LEU A 552 ? 0.7845 0.4362 0.6095 -0.0535 0.0521  -0.0834 552 LEU A CD1 
4331 C CD2 . LEU A 552 ? 0.8276 0.4399 0.6744 -0.0580 0.0701  -0.1157 552 LEU A CD2 
4332 N N   . THR A 553 ? 0.7384 0.3917 0.4443 -0.0696 0.0444  -0.0959 553 THR A N   
4333 C CA  . THR A 553 ? 0.7185 0.3777 0.3935 -0.0776 0.0237  -0.0964 553 THR A CA  
4334 C C   . THR A 553 ? 0.7201 0.3923 0.4285 -0.0789 0.0055  -0.0880 553 THR A C   
4335 O O   . THR A 553 ? 0.6976 0.3745 0.4448 -0.0730 0.0086  -0.0776 553 THR A O   
4336 C CB  . THR A 553 ? 0.6950 0.3635 0.3370 -0.0749 0.0179  -0.0815 553 THR A CB  
4337 O OG1 . THR A 553 ? 0.7077 0.3937 0.3798 -0.0675 0.0104  -0.0608 553 THR A OG1 
4338 C CG2 . THR A 553 ? 0.7151 0.3708 0.3303 -0.0730 0.0411  -0.0852 553 THR A CG2 
4339 N N   . PRO A 554 ? 0.6626 0.3417 0.3569 -0.0873 -0.0139 -0.0925 554 PRO A N   
4340 C CA  . PRO A 554 ? 0.6373 0.3306 0.3658 -0.0899 -0.0289 -0.0847 554 PRO A CA  
4341 C C   . PRO A 554 ? 0.6724 0.3849 0.4220 -0.0815 -0.0335 -0.0618 554 PRO A C   
4342 O O   . PRO A 554 ? 0.6637 0.3851 0.4460 -0.0824 -0.0381 -0.0544 554 PRO A O   
4343 C CB  . PRO A 554 ? 0.7628 0.4642 0.4693 -0.1000 -0.0493 -0.0947 554 PRO A CB  
4344 C CG  . PRO A 554 ? 0.7171 0.4001 0.3834 -0.1058 -0.0420 -0.1153 554 PRO A CG  
4345 C CD  . PRO A 554 ? 0.6988 0.3716 0.3486 -0.0965 -0.0214 -0.1090 554 PRO A CD  
4346 N N   . ILE A 555 ? 0.6119 0.3297 0.3432 -0.0742 -0.0309 -0.0509 555 ILE A N   
4347 C CA  . ILE A 555 ? 0.6196 0.3547 0.3709 -0.0670 -0.0345 -0.0323 555 ILE A CA  
4348 C C   . ILE A 555 ? 0.6138 0.3462 0.3835 -0.0591 -0.0181 -0.0254 555 ILE A C   
4349 O O   . ILE A 555 ? 0.5694 0.3158 0.3573 -0.0540 -0.0199 -0.0124 555 ILE A O   
4350 C CB  . ILE A 555 ? 0.6597 0.4033 0.3859 -0.0638 -0.0443 -0.0230 555 ILE A CB  
4351 C CG1 . ILE A 555 ? 0.7404 0.4691 0.4347 -0.0603 -0.0296 -0.0230 555 ILE A CG1 
4352 C CG2 . ILE A 555 ? 0.6284 0.3784 0.3381 -0.0705 -0.0645 -0.0293 555 ILE A CG2 
4353 C CD1 . ILE A 555 ? 0.7311 0.4642 0.4052 -0.0552 -0.0353 -0.0086 555 ILE A CD1 
4354 N N   . GLY A 556 ? 0.6177 0.3343 0.3854 -0.0581 -0.0025 -0.0351 556 GLY A N   
4355 C CA  . GLY A 556 ? 0.6578 0.3743 0.4466 -0.0504 0.0118  -0.0304 556 GLY A CA  
4356 C C   . GLY A 556 ? 0.6487 0.3510 0.4189 -0.0494 0.0299  -0.0410 556 GLY A C   
4357 O O   . GLY A 556 ? 0.6628 0.3523 0.4012 -0.0553 0.0324  -0.0533 556 GLY A O   
4358 N N   . TYR A 557 ? 0.6539 0.3596 0.4442 -0.0427 0.0431  -0.0372 557 TYR A N   
4359 C CA  . TYR A 557 ? 0.6837 0.3784 0.4636 -0.0419 0.0642  -0.0472 557 TYR A CA  
4360 C C   . TYR A 557 ? 0.6466 0.3418 0.3945 -0.0435 0.0687  -0.0404 557 TYR A C   
4361 O O   . TYR A 557 ? 0.6517 0.3596 0.4072 -0.0408 0.0610  -0.0263 557 TYR A O   
4362 C CB  . TYR A 557 ? 0.6701 0.3710 0.4930 -0.0340 0.0762  -0.0470 557 TYR A CB  
4363 C CG  . TYR A 557 ? 0.6707 0.3671 0.5264 -0.0303 0.0739  -0.0515 557 TYR A CG  
4364 C CD1 . TYR A 557 ? 0.7180 0.3953 0.5710 -0.0324 0.0849  -0.0686 557 TYR A CD1 
4365 C CD2 . TYR A 557 ? 0.6319 0.3415 0.5204 -0.0247 0.0615  -0.0384 557 TYR A CD2 
4366 C CE1 . TYR A 557 ? 0.7719 0.4414 0.6582 -0.0283 0.0836  -0.0714 557 TYR A CE1 
4367 C CE2 . TYR A 557 ? 0.6278 0.3303 0.5448 -0.0206 0.0591  -0.0389 557 TYR A CE2 
4368 C CZ  . TYR A 557 ? 0.7439 0.4255 0.6621 -0.0220 0.0702  -0.0548 557 TYR A CZ  
4369 O OH  . TYR A 557 ? 0.8149 0.4859 0.7646 -0.0171 0.0686  -0.0541 557 TYR A OH  
4370 N N   . VAL A 558 ? 0.6951 0.3746 0.4063 -0.0482 0.0823  -0.0505 558 VAL A N   
4371 C CA  . VAL A 558 ? 0.6929 0.3677 0.3696 -0.0501 0.0904  -0.0426 558 VAL A CA  
4372 C C   . VAL A 558 ? 0.7785 0.4431 0.4550 -0.0509 0.1201  -0.0533 558 VAL A C   
4373 O O   . VAL A 558 ? 0.7632 0.4222 0.4571 -0.0506 0.1323  -0.0697 558 VAL A O   
4374 C CB  . VAL A 558 ? 0.7787 0.4443 0.4009 -0.0562 0.0771  -0.0418 558 VAL A CB  
4375 C CG1 . VAL A 558 ? 0.7331 0.4119 0.3655 -0.0557 0.0485  -0.0347 558 VAL A CG1 
4376 C CG2 . VAL A 558 ? 0.7818 0.4303 0.3720 -0.0632 0.0880  -0.0625 558 VAL A CG2 
4377 N N   . PRO A 559 ? 0.7495 0.4108 0.4105 -0.0519 0.1343  -0.0446 559 PRO A N   
4378 C CA  . PRO A 559 ? 0.7815 0.4344 0.4449 -0.0541 0.1660  -0.0553 559 PRO A CA  
4379 C C   . PRO A 559 ? 0.7745 0.4081 0.3945 -0.0609 0.1797  -0.0731 559 PRO A C   
4380 O O   . PRO A 559 ? 0.8702 0.4937 0.4385 -0.0662 0.1669  -0.0722 559 PRO A O   
4381 C CB  . PRO A 559 ? 0.7282 0.3777 0.3738 -0.0562 0.1760  -0.0394 559 PRO A CB  
4382 C CG  . PRO A 559 ? 0.7505 0.4128 0.4100 -0.0516 0.1501  -0.0219 559 PRO A CG  
4383 C CD  . PRO A 559 ? 0.8001 0.4654 0.4491 -0.0508 0.1241  -0.0245 559 PRO A CD  
4384 N N   . LYS A 560 ? 0.8375 0.4675 0.4807 -0.0608 0.2056  -0.0909 560 LYS A N   
4385 C CA  . LYS A 560 ? 0.8913 0.5020 0.4940 -0.0682 0.2251  -0.1114 560 LYS A CA  
4386 C C   . LYS A 560 ? 0.9981 0.5938 0.5365 -0.0766 0.2406  -0.1045 560 LYS A C   
4387 O O   . LYS A 560 ? 1.0316 0.6305 0.5663 -0.0760 0.2409  -0.0844 560 LYS A O   
4388 C CB  . LYS A 560 ? 0.9257 0.5368 0.5748 -0.0650 0.2533  -0.1318 560 LYS A CB  
4389 C CG  . LYS A 560 ? 0.8653 0.4843 0.5701 -0.0568 0.2404  -0.1403 560 LYS A CG  
4390 C CD  . LYS A 560 ? 0.8295 0.4517 0.5834 -0.0524 0.2668  -0.1580 560 LYS A CD  
4391 C CE  . LYS A 560 ? 0.8608 0.4885 0.6701 -0.0429 0.2534  -0.1633 560 LYS A CE  
4392 N NZ  . LYS A 560 ? 0.8503 0.4882 0.7130 -0.0374 0.2733  -0.1761 560 LYS A NZ  
4393 N N   . GLU A 561 ? 1.0920 0.6783 0.5927 -0.0841 0.2473  -0.1172 561 GLU A N   
4394 C CA  . GLU A 561 ? 1.2162 0.7949 0.6700 -0.0912 0.2583  -0.1080 561 GLU A CA  
4395 C C   . GLU A 561 ? 1.1899 0.7706 0.6765 -0.0915 0.2908  -0.1072 561 GLU A C   
4396 O O   . GLU A 561 ? 1.2419 0.8295 0.7778 -0.0894 0.3102  -0.1242 561 GLU A O   
4397 C CB  . GLU A 561 ? 1.3276 0.8994 0.7407 -0.0988 0.2591  -0.1247 561 GLU A CB  
4398 C CG  . GLU A 561 ? 1.5146 1.0874 0.8998 -0.1000 0.2262  -0.1282 561 GLU A CG  
4399 C CD  . GLU A 561 ? 1.7101 1.2784 1.0529 -0.1082 0.2268  -0.1453 561 GLU A CD  
4400 O OE1 . GLU A 561 ? 1.6533 1.2155 0.9762 -0.1132 0.2513  -0.1501 561 GLU A OE1 
4401 O OE2 . GLU A 561 ? 1.7878 1.3592 1.1181 -0.1103 0.2030  -0.1548 561 GLU A OE2 
4402 N N   . ASP A 562 ? 1.1559 0.7320 0.6211 -0.0938 0.2952  -0.0868 562 ASP A N   
4403 C CA  . ASP A 562 ? 1.2827 0.8607 0.7797 -0.0956 0.3241  -0.0838 562 ASP A CA  
4404 C C   . ASP A 562 ? 1.1177 0.7125 0.6878 -0.0885 0.3302  -0.0868 562 ASP A C   
4405 O O   . ASP A 562 ? 1.1469 0.7494 0.7614 -0.0896 0.3549  -0.0929 562 ASP A O   
4406 C CB  . ASP A 562 ? 1.4184 0.9913 0.9108 -0.1028 0.3528  -0.1019 562 ASP A CB  
4407 C CG  . ASP A 562 ? 1.5920 1.1494 1.0111 -0.1107 0.3520  -0.0959 562 ASP A CG  
4408 O OD1 . ASP A 562 ? 1.6379 1.1888 1.0218 -0.1106 0.3387  -0.0728 562 ASP A OD1 
4409 O OD2 . ASP A 562 ? 1.6904 1.2433 1.0890 -0.1163 0.3643  -0.1143 562 ASP A OD2 
4410 N N   . ALA A 563 ? 1.0938 0.6961 0.6789 -0.0811 0.3072  -0.0830 563 ALA A N   
4411 C CA  . ALA A 563 ? 0.9712 0.5929 0.6248 -0.0732 0.3071  -0.0831 563 ALA A CA  
4412 C C   . ALA A 563 ? 0.9693 0.5971 0.6332 -0.0730 0.2999  -0.0604 563 ALA A C   
4413 O O   . ALA A 563 ? 0.9879 0.6351 0.7138 -0.0693 0.3032  -0.0603 563 ALA A O   
4414 C CB  . ALA A 563 ? 0.9027 0.5373 0.5856 -0.0645 0.2747  -0.0863 563 ALA A CB  
4415 N N   . LEU A 564 ? 0.9750 0.5870 0.5819 -0.0766 0.2892  -0.0418 564 LEU A N   
4416 C CA  . LEU A 564 ? 0.9683 0.5802 0.5816 -0.0770 0.2864  -0.0204 564 LEU A CA  
4417 C C   . LEU A 564 ? 0.9565 0.5583 0.5626 -0.0835 0.3104  -0.0170 564 LEU A C   
4418 O O   . LEU A 564 ? 1.0561 0.6444 0.6202 -0.0884 0.3192  -0.0213 564 LEU A O   
4419 C CB  . LEU A 564 ? 0.9731 0.5766 0.5429 -0.0742 0.2553  -0.0005 564 LEU A CB  
4420 C CG  . LEU A 564 ? 0.9182 0.5424 0.5245 -0.0653 0.2201  0.0029  564 LEU A CG  
4421 C CD1 . LEU A 564 ? 0.9984 0.6143 0.5619 -0.0630 0.1931  0.0212  564 LEU A CD1 
4422 C CD2 . LEU A 564 ? 0.9033 0.5457 0.5728 -0.0622 0.2219  0.0059  564 LEU A CD2 
4423 N N   . ASN A 565 ? 1.0234 0.6327 0.6718 -0.0841 0.3202  -0.0103 565 ASN A N   
4424 C CA  . ASN A 565 ? 0.9928 0.5915 0.6362 -0.0901 0.3409  -0.0049 565 ASN A CA  
4425 C C   . ASN A 565 ? 1.0250 0.6068 0.6163 -0.0889 0.3237  0.0185  565 ASN A C   
4426 O O   . ASN A 565 ? 0.9846 0.5696 0.5903 -0.0845 0.3079  0.0333  565 ASN A O   
4427 C CB  . ASN A 565 ? 0.9481 0.5623 0.6590 -0.0914 0.3549  -0.0082 565 ASN A CB  
4428 C CG  . ASN A 565 ? 1.0275 0.6313 0.7403 -0.0988 0.3816  -0.0079 565 ASN A CG  
4429 O OD1 . ASN A 565 ? 1.0561 0.6394 0.7148 -0.1028 0.3887  -0.0008 565 ASN A OD1 
4430 N ND2 . ASN A 565 ? 0.9977 0.6166 0.7731 -0.1013 0.3960  -0.0159 565 ASN A ND2 
4431 N N   . LEU A 566 ? 1.1056 0.6712 0.6384 -0.0925 0.3260  0.0215  566 LEU A N   
4432 C CA  . LEU A 566 ? 1.1811 0.7328 0.6640 -0.0908 0.3099  0.0444  566 LEU A CA  
4433 C C   . LEU A 566 ? 1.2583 0.7946 0.7204 -0.0978 0.3343  0.0524  566 LEU A C   
4434 O O   . LEU A 566 ? 1.3589 0.8820 0.7692 -0.0979 0.3255  0.0701  566 LEU A O   
4435 C CB  . LEU A 566 ? 1.1421 0.6903 0.5700 -0.0891 0.2868  0.0446  566 LEU A CB  
4436 C CG  . LEU A 566 ? 1.0945 0.6557 0.5370 -0.0827 0.2603  0.0389  566 LEU A CG  
4437 C CD1 . LEU A 566 ? 1.0831 0.6415 0.4731 -0.0828 0.2392  0.0356  566 LEU A CD1 
4438 C CD2 . LEU A 566 ? 1.1123 0.6804 0.5812 -0.0750 0.2391  0.0570  566 LEU A CD2 
4439 N N   . LYS A 567 ? 1.2345 0.7732 0.7374 -0.1036 0.3645  0.0402  567 LYS A N   
4440 C CA  . LYS A 567 ? 1.3598 0.8832 0.8468 -0.1113 0.3906  0.0469  567 LYS A CA  
4441 C C   . LYS A 567 ? 1.3980 0.9137 0.8896 -0.1088 0.3838  0.0711  567 LYS A C   
4442 O O   . LYS A 567 ? 1.3170 0.8439 0.8555 -0.1038 0.3730  0.0733  567 LYS A O   
4443 C CB  . LYS A 567 ? 1.3734 0.9046 0.9122 -0.1181 0.4236  0.0255  567 LYS A CB  
4444 C CG  . LYS A 567 ? 1.4994 1.0396 1.0441 -0.1197 0.4316  0.0007  567 LYS A CG  
4445 C CD  . LYS A 567 ? 1.5724 1.1243 1.1793 -0.1249 0.4617  -0.0199 567 LYS A CD  
4446 C CE  . LYS A 567 ? 1.5870 1.1496 1.2075 -0.1248 0.4677  -0.0441 567 LYS A CE  
4447 N NZ  . LYS A 567 ? 1.6671 1.2439 1.3538 -0.1289 0.4953  -0.0640 567 LYS A NZ  
4448 N N   . GLY A 568 ? 1.4002 0.8965 0.8429 -0.1126 0.3904  0.0893  568 GLY A N   
4449 C CA  . GLY A 568 ? 1.4178 0.9038 0.8572 -0.1096 0.3816  0.1154  568 GLY A CA  
4450 C C   . GLY A 568 ? 1.5118 0.9962 0.9122 -0.1006 0.3457  0.1363  568 GLY A C   
4451 O O   . GLY A 568 ? 1.5217 0.9962 0.9161 -0.0974 0.3369  0.1605  568 GLY A O   
4452 N N   . LEU A 569 ? 1.5498 1.0439 0.9271 -0.0965 0.3245  0.1274  569 LEU A N   
4453 C CA  . LEU A 569 ? 1.5656 1.0612 0.9069 -0.0882 0.2893  0.1450  569 LEU A CA  
4454 C C   . LEU A 569 ? 1.6973 1.1867 0.9701 -0.0919 0.2858  0.1450  569 LEU A C   
4455 O O   . LEU A 569 ? 1.6903 1.1670 0.9178 -0.0932 0.2852  0.1660  569 LEU A O   
4456 C CB  . LEU A 569 ? 1.5500 1.0643 0.9239 -0.0802 0.2635  0.1349  569 LEU A CB  
4457 C CG  . LEU A 569 ? 1.3401 0.8641 0.7809 -0.0765 0.2640  0.1328  569 LEU A CG  
4458 C CD1 . LEU A 569 ? 1.2528 0.7950 0.7182 -0.0699 0.2403  0.1220  569 LEU A CD1 
4459 C CD2 . LEU A 569 ? 1.3418 0.8574 0.7911 -0.0721 0.2565  0.1579  569 LEU A CD2 
4460 N N   . GLY A 570 ? 1.7835 1.2820 1.0482 -0.0938 0.2834  0.1215  570 GLY A N   
4461 C CA  . GLY A 570 ? 1.7926 1.2870 0.9957 -0.0987 0.2819  0.1157  570 GLY A CA  
4462 C C   . GLY A 570 ? 1.8597 1.3595 1.0202 -0.0918 0.2445  0.1314  570 GLY A C   
4463 O O   . GLY A 570 ? 1.7890 1.2964 0.9207 -0.0927 0.2301  0.1172  570 GLY A O   
4464 N N   . ASP A 571 ? 1.9698 1.4665 1.1297 -0.0849 0.2285  0.1602  571 ASP A N   
4465 C CA  . ASP A 571 ? 1.9512 1.4555 1.0786 -0.0768 0.1917  0.1782  571 ASP A CA  
4466 C C   . ASP A 571 ? 1.9302 1.4533 1.0880 -0.0689 0.1614  0.1682  571 ASP A C   
4467 O O   . ASP A 571 ? 1.9309 1.4643 1.0675 -0.0621 0.1292  0.1791  571 ASP A O   
4468 C CB  . ASP A 571 ? 1.9769 1.4724 1.1060 -0.0708 0.1850  0.2125  571 ASP A CB  
4469 C CG  . ASP A 571 ? 2.0217 1.5162 1.2178 -0.0671 0.1928  0.2158  571 ASP A CG  
4470 O OD1 . ASP A 571 ? 1.8670 1.3674 1.1047 -0.0700 0.2067  0.1923  571 ASP A OD1 
4471 O OD2 . ASP A 571 ? 2.1626 1.6508 1.3707 -0.0613 0.1846  0.2418  571 ASP A OD2 
4472 N N   . VAL A 572 ? 1.8044 1.3334 1.0118 -0.0696 0.1707  0.1483  572 VAL A N   
4473 C CA  . VAL A 572 ? 1.6863 1.2320 0.9252 -0.0628 0.1443  0.1402  572 VAL A CA  
4474 C C   . VAL A 572 ? 1.6013 1.1557 0.8047 -0.0654 0.1268  0.1235  572 VAL A C   
4475 O O   . VAL A 572 ? 1.6278 1.1780 0.8137 -0.0740 0.1452  0.1019  572 VAL A O   
4476 C CB  . VAL A 572 ? 1.5840 1.1334 0.8805 -0.0639 0.1609  0.1236  572 VAL A CB  
4477 C CG1 . VAL A 572 ? 1.4066 0.9720 0.7285 -0.0585 0.1355  0.1140  572 VAL A CG1 
4478 C CG2 . VAL A 572 ? 1.5185 1.0626 0.8548 -0.0613 0.1740  0.1386  572 VAL A CG2 
4479 N N   . ASN A 573 ? 1.5439 1.1118 0.7407 -0.0580 0.0913  0.1322  573 ASN A N   
4480 C CA  . ASN A 573 ? 1.5481 1.1275 0.7180 -0.0606 0.0705  0.1151  573 ASN A CA  
4481 C C   . ASN A 573 ? 1.4386 1.0255 0.6490 -0.0622 0.0701  0.0920  573 ASN A C   
4482 O O   . ASN A 573 ? 1.4063 1.0066 0.6462 -0.0560 0.0458  0.0937  573 ASN A O   
4483 C CB  . ASN A 573 ? 1.6115 1.2053 0.7663 -0.0521 0.0327  0.1325  573 ASN A CB  
4484 C CG  . ASN A 573 ? 1.6578 1.2664 0.7890 -0.0556 0.0096  0.1132  573 ASN A CG  
4485 O OD1 . ASN A 573 ? 1.6477 1.2521 0.7600 -0.0653 0.0240  0.0887  573 ASN A OD1 
4486 N ND2 . ASN A 573 ? 1.7036 1.3305 0.8397 -0.0478 -0.0258 0.1230  573 ASN A ND2 
4487 N N   . VAL A 574 ? 1.4658 1.0442 0.6784 -0.0706 0.0984  0.0702  574 VAL A N   
4488 C CA  . VAL A 574 ? 1.3747 0.9577 0.6275 -0.0719 0.1030  0.0500  574 VAL A CA  
4489 C C   . VAL A 574 ? 1.3676 0.9635 0.6144 -0.0726 0.0748  0.0360  574 VAL A C   
4490 O O   . VAL A 574 ? 1.1415 0.7442 0.4237 -0.0711 0.0673  0.0267  574 VAL A O   
4491 C CB  . VAL A 574 ? 1.3138 0.8863 0.5719 -0.0800 0.1401  0.0296  574 VAL A CB  
4492 C CG1 . VAL A 574 ? 1.3337 0.8967 0.6103 -0.0798 0.1673  0.0421  574 VAL A CG1 
4493 C CG2 . VAL A 574 ? 1.3411 0.9088 0.5505 -0.0881 0.1465  0.0149  574 VAL A CG2 
4494 N N   . GLU A 575 ? 1.3822 0.9823 0.5849 -0.0754 0.0586  0.0340  575 GLU A N   
4495 C CA  . GLU A 575 ? 1.4389 1.0534 0.6390 -0.0773 0.0312  0.0187  575 GLU A CA  
4496 C C   . GLU A 575 ? 1.2965 0.9266 0.5291 -0.0687 0.0001  0.0328  575 GLU A C   
4497 O O   . GLU A 575 ? 1.2002 0.8397 0.4603 -0.0700 -0.0130 0.0192  575 GLU A O   
4498 C CB  . GLU A 575 ? 1.5453 1.1641 0.6917 -0.0817 0.0193  0.0146  575 GLU A CB  
4499 C CG  . GLU A 575 ? 1.6354 1.2416 0.7511 -0.0917 0.0481  -0.0067 575 GLU A CG  
4500 C CD  . GLU A 575 ? 1.7840 1.3952 0.8416 -0.0958 0.0362  -0.0095 575 GLU A CD  
4501 O OE1 . GLU A 575 ? 1.8010 1.4229 0.8391 -0.0895 0.0097  0.0114  575 GLU A OE1 
4502 O OE2 . GLU A 575 ? 1.8357 1.4410 0.8684 -0.1047 0.0534  -0.0330 575 GLU A OE2 
4503 N N   . GLU A 576 ? 1.3448 0.9778 0.5777 -0.0599 -0.0107 0.0598  576 GLU A N   
4504 C CA  . GLU A 576 ? 1.3770 1.0262 0.6445 -0.0506 -0.0390 0.0733  576 GLU A CA  
4505 C C   . GLU A 576 ? 1.2349 0.8812 0.5526 -0.0463 -0.0279 0.0776  576 GLU A C   
4506 O O   . GLU A 576 ? 1.2010 0.8615 0.5534 -0.0410 -0.0483 0.0808  576 GLU A O   
4507 C CB  . GLU A 576 ? 1.4599 1.1141 0.7111 -0.0416 -0.0556 0.1003  576 GLU A CB  
4508 C CG  . GLU A 576 ? 1.4586 1.1346 0.7408 -0.0321 -0.0898 0.1108  576 GLU A CG  
4509 C CD  . GLU A 576 ? 1.5898 1.2714 0.8543 -0.0223 -0.1070 0.1369  576 GLU A CD  
4510 O OE1 . GLU A 576 ? 1.6417 1.3111 0.8616 -0.0244 -0.0951 0.1461  576 GLU A OE1 
4511 O OE2 . GLU A 576 ? 1.6185 1.3169 0.9144 -0.0123 -0.1319 0.1487  576 GLU A OE2 
4512 N N   . LEU A 577 ? 1.1831 0.8134 0.5073 -0.0488 0.0042  0.0767  577 LEU A N   
4513 C CA  . LEU A 577 ? 1.1099 0.7399 0.4819 -0.0453 0.0149  0.0792  577 LEU A CA  
4514 C C   . LEU A 577 ? 1.0042 0.6392 0.3976 -0.0495 0.0133  0.0588  577 LEU A C   
4515 O O   . LEU A 577 ? 0.9421 0.5840 0.3757 -0.0454 0.0099  0.0619  577 LEU A O   
4516 C CB  . LEU A 577 ? 1.0488 0.6635 0.4262 -0.0475 0.0494  0.0823  577 LEU A CB  
4517 C CG  . LEU A 577 ? 1.1259 0.7370 0.5169 -0.0409 0.0530  0.1061  577 LEU A CG  
4518 C CD1 . LEU A 577 ? 1.2767 0.8823 0.6231 -0.0400 0.0462  0.1211  577 LEU A CD1 
4519 C CD2 . LEU A 577 ? 1.1537 0.7548 0.5701 -0.0442 0.0861  0.1038  577 LEU A CD2 
4520 N N   . PHE A 578 ? 0.9444 0.5764 0.3136 -0.0577 0.0163  0.0376  578 PHE A N   
4521 C CA  . PHE A 578 ? 0.9923 0.6301 0.3882 -0.0616 0.0160  0.0168  578 PHE A CA  
4522 C C   . PHE A 578 ? 0.9933 0.6390 0.3715 -0.0672 -0.0086 0.0020  578 PHE A C   
4523 O O   . PHE A 578 ? 1.0365 0.6879 0.4420 -0.0715 -0.0064 -0.0183 578 PHE A O   
4524 C CB  . PHE A 578 ? 0.9687 0.5957 0.3722 -0.0665 0.0494  -0.0007 578 PHE A CB  
4525 C CG  . PHE A 578 ? 0.9096 0.5370 0.3521 -0.0617 0.0715  0.0084  578 PHE A CG  
4526 C CD1 . PHE A 578 ? 0.9080 0.5525 0.4141 -0.0569 0.0706  0.0050  578 PHE A CD1 
4527 C CD2 . PHE A 578 ? 0.9781 0.5887 0.3927 -0.0629 0.0930  0.0203  578 PHE A CD2 
4528 C CE1 . PHE A 578 ? 0.8304 0.4780 0.3727 -0.0535 0.0884  0.0112  578 PHE A CE1 
4529 C CE2 . PHE A 578 ? 0.9612 0.5737 0.4161 -0.0601 0.1132  0.0264  578 PHE A CE2 
4530 C CZ  . PHE A 578 ? 0.8736 0.5060 0.3931 -0.0554 0.1097  0.0208  578 PHE A CZ  
4531 N N   . GLY A 579 ? 1.0271 0.6821 0.3812 -0.0655 -0.0318 0.0116  579 GLY A N   
4532 C CA  . GLY A 579 ? 1.0364 0.7059 0.3841 -0.0705 -0.0576 -0.0023 579 GLY A CA  
4533 C C   . GLY A 579 ? 1.0978 0.7814 0.4877 -0.0704 -0.0772 -0.0069 579 GLY A C   
4534 O O   . GLY A 579 ? 1.0400 0.7356 0.4633 -0.0618 -0.0878 0.0107  579 GLY A O   
4535 N N   . ILE A 580 ? 1.1025 0.7886 0.5035 -0.0795 -0.0793 -0.0312 580 ILE A N   
4536 C CA  . ILE A 580 ? 1.0180 0.7247 0.4768 -0.0799 -0.0934 -0.0368 580 ILE A CA  
4537 C C   . ILE A 580 ? 1.0126 0.7313 0.4553 -0.0881 -0.1223 -0.0497 580 ILE A C   
4538 O O   . ILE A 580 ? 1.1065 0.8198 0.5357 -0.0982 -0.1185 -0.0730 580 ILE A O   
4539 C CB  . ILE A 580 ? 1.0680 0.7685 0.5652 -0.0831 -0.0711 -0.0523 580 ILE A CB  
4540 C CG1 . ILE A 580 ? 1.0281 0.7208 0.5433 -0.0749 -0.0456 -0.0403 580 ILE A CG1 
4541 C CG2 . ILE A 580 ? 0.9945 0.7138 0.5460 -0.0848 -0.0848 -0.0557 580 ILE A CG2 
4542 C CD1 . ILE A 580 ? 0.9911 0.6780 0.5434 -0.0760 -0.0253 -0.0531 580 ILE A CD1 
4543 N N   . SER A 581 ? 0.9608 0.7006 0.4157 -0.0827 -0.1497 -0.0352 581 SER A N   
4544 C CA  . SER A 581 ? 0.9729 0.7368 0.4341 -0.0874 -0.1766 -0.0453 581 SER A CA  
4545 C C   . SER A 581 ? 0.8927 0.6695 0.4046 -0.0953 -0.1866 -0.0590 581 SER A C   
4546 O O   . SER A 581 ? 0.8437 0.6330 0.4044 -0.0885 -0.1851 -0.0463 581 SER A O   
4547 C CB  . SER A 581 ? 0.8423 0.6264 0.3022 -0.0762 -0.2001 -0.0231 581 SER A CB  
4548 O OG  . SER A 581 ? 0.9949 0.8075 0.4720 -0.0800 -0.2281 -0.0332 581 SER A OG  
4549 N N   . LYS A 582 ? 0.9125 0.6931 0.4278 -0.1074 -0.1895 -0.0840 582 LYS A N   
4550 C CA  . LYS A 582 ? 0.8802 0.6738 0.4472 -0.1165 -0.1981 -0.0971 582 LYS A CA  
4551 C C   . LYS A 582 ? 0.8668 0.6943 0.4689 -0.1123 -0.2265 -0.0859 582 LYS A C   
4552 O O   . LYS A 582 ? 0.7483 0.5896 0.4045 -0.1128 -0.2267 -0.0826 582 LYS A O   
4553 C CB  . LYS A 582 ? 0.9110 0.7029 0.4762 -0.1300 -0.1955 -0.1265 582 LYS A CB  
4554 C CG  . LYS A 582 ? 0.8999 0.7037 0.5212 -0.1410 -0.2013 -0.1404 582 LYS A CG  
4555 C CD  . LYS A 582 ? 0.9494 0.7495 0.5701 -0.1539 -0.1971 -0.1705 582 LYS A CD  
4556 C CE  . LYS A 582 ? 0.9332 0.7437 0.6133 -0.1655 -0.2003 -0.1829 582 LYS A CE  
4557 N NZ  . LYS A 582 ? 0.9226 0.7230 0.6079 -0.1775 -0.1914 -0.2129 582 LYS A NZ  
4558 N N   . GLU A 583 ? 0.7982 0.6437 0.3781 -0.1058 -0.2459 -0.0788 583 GLU A N   
4559 C CA  . GLU A 583 ? 0.7977 0.6775 0.4149 -0.0998 -0.2729 -0.0686 583 GLU A CA  
4560 C C   . GLU A 583 ? 0.8115 0.6923 0.4560 -0.0875 -0.2712 -0.0442 583 GLU A C   
4561 O O   . GLU A 583 ? 0.8252 0.7299 0.5235 -0.0868 -0.2831 -0.0418 583 GLU A O   
4562 C CB  . GLU A 583 ? 0.9098 0.8057 0.4930 -0.0935 -0.2930 -0.0635 583 GLU A CB  
4563 C CG  . GLU A 583 ? 0.9904 0.8876 0.5423 -0.1057 -0.2956 -0.0892 583 GLU A CG  
4564 C CD  . GLU A 583 ? 1.2710 1.1844 0.7834 -0.0993 -0.3158 -0.0828 583 GLU A CD  
4565 O OE1 . GLU A 583 ? 1.3055 1.2250 0.8136 -0.0846 -0.3257 -0.0561 583 GLU A OE1 
4566 O OE2 . GLU A 583 ? 1.3188 1.2385 0.8048 -0.1087 -0.3217 -0.1046 583 GLU A OE2 
4567 N N   . PHE A 584 ? 0.8342 0.6905 0.4454 -0.0781 -0.2547 -0.0271 584 PHE A N   
4568 C CA  . PHE A 584 ? 0.7342 0.5929 0.3777 -0.0655 -0.2464 -0.0058 584 PHE A CA  
4569 C C   . PHE A 584 ? 0.7266 0.5895 0.4234 -0.0698 -0.2251 -0.0129 584 PHE A C   
4570 O O   . PHE A 584 ? 0.6823 0.5661 0.4299 -0.0651 -0.2279 -0.0060 584 PHE A O   
4571 C CB  . PHE A 584 ? 0.7169 0.5482 0.3179 -0.0562 -0.2279 0.0114  584 PHE A CB  
4572 C CG  . PHE A 584 ? 0.7446 0.5763 0.3831 -0.0449 -0.2114 0.0286  584 PHE A CG  
4573 C CD1 . PHE A 584 ? 0.7433 0.5875 0.4010 -0.0320 -0.2260 0.0479  584 PHE A CD1 
4574 C CD2 . PHE A 584 ? 0.6916 0.5116 0.3478 -0.0470 -0.1823 0.0244  584 PHE A CD2 
4575 C CE1 . PHE A 584 ? 0.6834 0.5271 0.3760 -0.0227 -0.2098 0.0603  584 PHE A CE1 
4576 C CE2 . PHE A 584 ? 0.7205 0.5425 0.4092 -0.0381 -0.1685 0.0374  584 PHE A CE2 
4577 C CZ  . PHE A 584 ? 0.7096 0.5428 0.4159 -0.0266 -0.1812 0.0541  584 PHE A CZ  
4578 N N   . TRP A 585 ? 0.7618 0.6044 0.4472 -0.0784 -0.2031 -0.0263 585 TRP A N   
4579 C CA  . TRP A 585 ? 0.6997 0.5412 0.4275 -0.0808 -0.1818 -0.0287 585 TRP A CA  
4580 C C   . TRP A 585 ? 0.6505 0.5118 0.4240 -0.0916 -0.1903 -0.0415 585 TRP A C   
4581 O O   . TRP A 585 ? 0.6451 0.5117 0.4584 -0.0921 -0.1767 -0.0381 585 TRP A O   
4582 C CB  . TRP A 585 ? 0.6687 0.4818 0.3728 -0.0846 -0.1568 -0.0370 585 TRP A CB  
4583 C CG  . TRP A 585 ? 0.6373 0.4346 0.3175 -0.0741 -0.1403 -0.0224 585 TRP A CG  
4584 C CD1 . TRP A 585 ? 0.7280 0.5081 0.3570 -0.0717 -0.1372 -0.0199 585 TRP A CD1 
4585 C CD2 . TRP A 585 ? 0.7474 0.5453 0.4544 -0.0657 -0.1240 -0.0090 585 TRP A CD2 
4586 N NE1 . TRP A 585 ? 0.7667 0.5362 0.3932 -0.0628 -0.1187 -0.0056 585 TRP A NE1 
4587 C CE2 . TRP A 585 ? 0.6973 0.4782 0.3719 -0.0590 -0.1116 0.0003  585 TRP A CE2 
4588 C CE3 . TRP A 585 ? 0.5968 0.4078 0.3499 -0.0645 -0.1181 -0.0047 585 TRP A CE3 
4589 C CZ2 . TRP A 585 ? 0.7150 0.4933 0.4065 -0.0514 -0.0950 0.0120  585 TRP A CZ2 
4590 C CZ3 . TRP A 585 ? 0.6680 0.4762 0.4324 -0.0565 -0.1026 0.0068  585 TRP A CZ3 
4591 C CH2 . TRP A 585 ? 0.6493 0.4420 0.3853 -0.0501 -0.0920 0.0142  585 TRP A CH2 
4592 N N   . GLU A 586 ? 0.6350 0.5073 0.4030 -0.1011 -0.2120 -0.0564 586 GLU A N   
4593 C CA  . GLU A 586 ? 0.6010 0.4956 0.4191 -0.1120 -0.2208 -0.0680 586 GLU A CA  
4594 C C   . GLU A 586 ? 0.6341 0.5593 0.4973 -0.1038 -0.2315 -0.0544 586 GLU A C   
4595 O O   . GLU A 586 ? 0.6265 0.5658 0.5389 -0.1090 -0.2233 -0.0562 586 GLU A O   
4596 C CB  . GLU A 586 ? 0.7272 0.6288 0.5308 -0.1250 -0.2434 -0.0896 586 GLU A CB  
4597 C CG  . GLU A 586 ? 0.7513 0.6247 0.5293 -0.1375 -0.2289 -0.1102 586 GLU A CG  
4598 C CD  . GLU A 586 ? 0.8993 0.7844 0.6748 -0.1516 -0.2475 -0.1349 586 GLU A CD  
4599 O OE1 . GLU A 586 ? 0.8855 0.7988 0.6574 -0.1469 -0.2708 -0.1333 586 GLU A OE1 
4600 O OE2 . GLU A 586 ? 1.0171 0.8876 0.8015 -0.1642 -0.2339 -0.1548 586 GLU A OE2 
4601 N N   . LYS A 587 ? 0.5848 0.5194 0.4323 -0.0907 -0.2483 -0.0404 587 LYS A N   
4602 C CA  . LYS A 587 ? 0.5590 0.5204 0.4520 -0.0804 -0.2561 -0.0272 587 LYS A CA  
4603 C C   . LYS A 587 ? 0.5215 0.4736 0.4312 -0.0724 -0.2288 -0.0141 587 LYS A C   
4604 O O   . LYS A 587 ? 0.4919 0.4647 0.4509 -0.0707 -0.2240 -0.0112 587 LYS A O   
4605 C CB  . LYS A 587 ? 0.5887 0.5585 0.4600 -0.0671 -0.2819 -0.0138 587 LYS A CB  
4606 C CG  . LYS A 587 ? 0.7737 0.7504 0.6138 -0.0740 -0.3116 -0.0253 587 LYS A CG  
4607 C CD  . LYS A 587 ? 0.9027 0.8847 0.7167 -0.0577 -0.3302 -0.0069 587 LYS A CD  
4608 C CE  . LYS A 587 ? 0.9557 0.9474 0.7366 -0.0624 -0.3465 -0.0181 587 LYS A CE  
4609 N NZ  . LYS A 587 ? 1.1072 1.1335 0.9354 -0.0737 -0.3620 -0.0383 587 LYS A NZ  
4610 N N   . GLU A 588 ? 0.5693 0.4921 0.4396 -0.0684 -0.2102 -0.0077 588 GLU A N   
4611 C CA  . GLU A 588 ? 0.5625 0.4778 0.4460 -0.0610 -0.1869 0.0036  588 GLU A CA  
4612 C C   . GLU A 588 ? 0.5086 0.4289 0.4276 -0.0703 -0.1697 -0.0034 588 GLU A C   
4613 O O   . GLU A 588 ? 0.5342 0.4672 0.4860 -0.0665 -0.1599 0.0029  588 GLU A O   
4614 C CB  . GLU A 588 ? 0.5744 0.4594 0.4117 -0.0565 -0.1715 0.0094  588 GLU A CB  
4615 C CG  . GLU A 588 ? 0.5175 0.3959 0.3655 -0.0481 -0.1510 0.0209  588 GLU A CG  
4616 C CD  . GLU A 588 ? 0.5739 0.4621 0.4348 -0.0353 -0.1583 0.0351  588 GLU A CD  
4617 O OE1 . GLU A 588 ? 0.5259 0.4224 0.3805 -0.0306 -0.1801 0.0396  588 GLU A OE1 
4618 O OE2 . GLU A 588 ? 0.4680 0.3553 0.3464 -0.0296 -0.1429 0.0415  588 GLU A OE2 
4619 N N   . VAL A 589 ? 0.5534 0.4625 0.4653 -0.0828 -0.1650 -0.0163 589 VAL A N   
4620 C CA  . VAL A 589 ? 0.5327 0.4421 0.4746 -0.0918 -0.1483 -0.0198 589 VAL A CA  
4621 C C   . VAL A 589 ? 0.5380 0.4773 0.5288 -0.0980 -0.1557 -0.0236 589 VAL A C   
4622 O O   . VAL A 589 ? 0.4980 0.4445 0.5176 -0.1010 -0.1402 -0.0198 589 VAL A O   
4623 C CB  . VAL A 589 ? 0.6320 0.5186 0.5574 -0.1029 -0.1411 -0.0320 589 VAL A CB  
4624 C CG1 . VAL A 589 ? 0.6508 0.5099 0.5374 -0.0959 -0.1281 -0.0280 589 VAL A CG1 
4625 C CG2 . VAL A 589 ? 0.6203 0.5120 0.5390 -0.1125 -0.1609 -0.0483 589 VAL A CG2 
4626 N N   . GLU A 590 ? 0.4843 0.4429 0.4855 -0.1005 -0.1792 -0.0314 590 GLU A N   
4627 C CA  . GLU A 590 ? 0.4395 0.4311 0.4944 -0.1056 -0.1869 -0.0358 590 GLU A CA  
4628 C C   . GLU A 590 ? 0.4503 0.4584 0.5317 -0.0933 -0.1795 -0.0232 590 GLU A C   
4629 O O   . GLU A 590 ? 0.4778 0.5029 0.6009 -0.0986 -0.1670 -0.0245 590 GLU A O   
4630 C CB  . GLU A 590 ? 0.4665 0.4789 0.5279 -0.1080 -0.2179 -0.0459 590 GLU A CB  
4631 C CG  . GLU A 590 ? 0.5749 0.5782 0.6238 -0.1246 -0.2252 -0.0647 590 GLU A CG  
4632 C CD  . GLU A 590 ? 0.7435 0.7734 0.8039 -0.1286 -0.2583 -0.0768 590 GLU A CD  
4633 O OE1 . GLU A 590 ? 0.6409 0.6985 0.7251 -0.1176 -0.2760 -0.0688 590 GLU A OE1 
4634 O OE2 . GLU A 590 ? 0.7357 0.7594 0.7830 -0.1426 -0.2675 -0.0950 590 GLU A OE2 
4635 N N   . GLU A 591 ? 0.4158 0.4173 0.4733 -0.0777 -0.1850 -0.0114 591 GLU A N   
4636 C CA  . GLU A 591 ? 0.4517 0.4656 0.5350 -0.0657 -0.1770 -0.0012 591 GLU A CA  
4637 C C   . GLU A 591 ? 0.4543 0.4550 0.5350 -0.0676 -0.1481 0.0025  591 GLU A C   
4638 O O   . GLU A 591 ? 0.4294 0.4461 0.5439 -0.0663 -0.1357 0.0034  591 GLU A O   
4639 C CB  . GLU A 591 ? 0.4085 0.4141 0.4664 -0.0492 -0.1895 0.0112  591 GLU A CB  
4640 C CG  . GLU A 591 ? 0.5178 0.5421 0.5840 -0.0440 -0.2210 0.0115  591 GLU A CG  
4641 C CD  . GLU A 591 ? 0.5023 0.5644 0.6344 -0.0430 -0.2293 0.0068  591 GLU A CD  
4642 O OE1 . GLU A 591 ? 0.4681 0.5387 0.6333 -0.0364 -0.2132 0.0108  591 GLU A OE1 
4643 O OE2 . GLU A 591 ? 0.5823 0.6666 0.7349 -0.0495 -0.2512 -0.0028 591 GLU A OE2 
4644 N N   . ILE A 592 ? 0.4006 0.3732 0.4417 -0.0707 -0.1374 0.0039  592 ILE A N   
4645 C CA  . ILE A 592 ? 0.4510 0.4126 0.4887 -0.0729 -0.1136 0.0077  592 ILE A CA  
4646 C C   . ILE A 592 ? 0.5082 0.4806 0.5752 -0.0866 -0.1031 0.0021  592 ILE A C   
4647 O O   . ILE A 592 ? 0.4363 0.4148 0.5174 -0.0880 -0.0860 0.0055  592 ILE A O   
4648 C CB  . ILE A 592 ? 0.4444 0.3759 0.4392 -0.0723 -0.1068 0.0101  592 ILE A CB  
4649 C CG1 . ILE A 592 ? 0.5365 0.4567 0.5024 -0.0602 -0.1135 0.0164  592 ILE A CG1 
4650 C CG2 . ILE A 592 ? 0.4187 0.3413 0.4113 -0.0738 -0.0862 0.0149  592 ILE A CG2 
4651 C CD1 . ILE A 592 ? 0.5717 0.4648 0.4980 -0.0606 -0.1080 0.0158  592 ILE A CD1 
4652 N N   . ASP A 593 ? 0.4424 0.4168 0.5180 -0.0979 -0.1122 -0.0071 593 ASP A N   
4653 C CA  . ASP A 593 ? 0.3899 0.3723 0.4955 -0.1127 -0.1010 -0.0120 593 ASP A CA  
4654 C C   . ASP A 593 ? 0.4819 0.4966 0.6338 -0.1134 -0.0976 -0.0136 593 ASP A C   
4655 O O   . ASP A 593 ? 0.4323 0.4515 0.5989 -0.1192 -0.0771 -0.0106 593 ASP A O   
4656 C CB  . ASP A 593 ? 0.5004 0.4787 0.6098 -0.1254 -0.1129 -0.0242 593 ASP A CB  
4657 C CG  . ASP A 593 ? 0.6084 0.5864 0.7450 -0.1425 -0.0981 -0.0281 593 ASP A CG  
4658 O OD1 . ASP A 593 ? 0.6162 0.5910 0.7570 -0.1442 -0.0775 -0.0186 593 ASP A OD1 
4659 O OD2 . ASP A 593 ? 0.6275 0.6076 0.7799 -0.1551 -0.1070 -0.0406 593 ASP A OD2 
4660 N N   . LYS A 594 ? 0.4548 0.4929 0.6302 -0.1070 -0.1172 -0.0182 594 LYS A N   
4661 C CA  . LYS A 594 ? 0.3667 0.4381 0.5940 -0.1059 -0.1144 -0.0214 594 LYS A CA  
4662 C C   . LYS A 594 ? 0.3965 0.4676 0.6227 -0.0964 -0.0952 -0.0137 594 LYS A C   
4663 O O   . LYS A 594 ? 0.3962 0.4859 0.6564 -0.1013 -0.0779 -0.0169 594 LYS A O   
4664 C CB  . LYS A 594 ? 0.3729 0.4679 0.6239 -0.0970 -0.1428 -0.0252 594 LYS A CB  
4665 C CG  . LYS A 594 ? 0.4454 0.5477 0.7035 -0.1083 -0.1641 -0.0367 594 LYS A CG  
4666 C CD  . LYS A 594 ? 0.4954 0.6300 0.7881 -0.1003 -0.1934 -0.0408 594 LYS A CD  
4667 C CE  . LYS A 594 ? 0.4081 0.5319 0.6655 -0.0806 -0.2112 -0.0284 594 LYS A CE  
4668 N NZ  . LYS A 594 ? 0.4922 0.6414 0.7688 -0.0745 -0.2467 -0.0313 594 LYS A NZ  
4669 N N   . TYR A 595 ? 0.3853 0.4358 0.5729 -0.0839 -0.0964 -0.0051 595 TYR A N   
4670 C CA  . TYR A 595 ? 0.4095 0.4589 0.5954 -0.0755 -0.0794 -0.0004 595 TYR A CA  
4671 C C   . TYR A 595 ? 0.3957 0.4355 0.5679 -0.0860 -0.0549 0.0010  595 TYR A C   
4672 O O   . TYR A 595 ? 0.3866 0.4408 0.5797 -0.0885 -0.0372 -0.0017 595 TYR A O   
4673 C CB  . TYR A 595 ? 0.4243 0.4528 0.5740 -0.0616 -0.0867 0.0077  595 TYR A CB  
4674 C CG  . TYR A 595 ? 0.3720 0.3963 0.5178 -0.0542 -0.0696 0.0106  595 TYR A CG  
4675 C CD1 . TYR A 595 ? 0.3874 0.4281 0.5665 -0.0442 -0.0682 0.0087  595 TYR A CD1 
4676 C CD2 . TYR A 595 ? 0.3888 0.3933 0.5001 -0.0572 -0.0557 0.0139  595 TYR A CD2 
4677 C CE1 . TYR A 595 ? 0.3930 0.4288 0.5693 -0.0388 -0.0518 0.0081  595 TYR A CE1 
4678 C CE2 . TYR A 595 ? 0.3853 0.3878 0.4931 -0.0520 -0.0417 0.0139  595 TYR A CE2 
4679 C CZ  . TYR A 595 ? 0.4087 0.4259 0.5479 -0.0435 -0.0390 0.0100  595 TYR A CZ  
4680 O OH  . TYR A 595 ? 0.5990 0.6131 0.7354 -0.0395 -0.0242 0.0070  595 TYR A OH  
4681 N N   . LEU A 596 ? 0.4294 0.4445 0.5657 -0.0920 -0.0534 0.0054  596 LEU A N   
4682 C CA  . LEU A 596 ? 0.4003 0.4040 0.5195 -0.1003 -0.0333 0.0102  596 LEU A CA  
4683 C C   . LEU A 596 ? 0.4719 0.4905 0.6209 -0.1152 -0.0200 0.0067  596 LEU A C   
4684 O O   . LEU A 596 ? 0.4458 0.4673 0.5923 -0.1205 -0.0001 0.0097  596 LEU A O   
4685 C CB  . LEU A 596 ? 0.4190 0.3934 0.5008 -0.1019 -0.0364 0.0161  596 LEU A CB  
4686 C CG  . LEU A 596 ? 0.4273 0.3844 0.4764 -0.0894 -0.0426 0.0203  596 LEU A CG  
4687 C CD1 . LEU A 596 ? 0.5051 0.4359 0.5262 -0.0922 -0.0432 0.0241  596 LEU A CD1 
4688 C CD2 . LEU A 596 ? 0.3928 0.3535 0.4346 -0.0829 -0.0308 0.0236  596 LEU A CD2 
4689 N N   . GLU A 597 ? 0.3886 0.4170 0.5650 -0.1233 -0.0302 -0.0002 597 GLU A N   
4690 C CA  . GLU A 597 ? 0.4313 0.4740 0.6409 -0.1394 -0.0160 -0.0042 597 GLU A CA  
4691 C C   . GLU A 597 ? 0.4820 0.5548 0.7287 -0.1383 -0.0028 -0.0097 597 GLU A C   
4692 O O   . GLU A 597 ? 0.4875 0.5657 0.7423 -0.1494 0.0207  -0.0087 597 GLU A O   
4693 C CB  . GLU A 597 ? 0.4383 0.4880 0.6749 -0.1487 -0.0318 -0.0136 597 GLU A CB  
4694 C CG  . GLU A 597 ? 0.5709 0.6385 0.8512 -0.1667 -0.0171 -0.0197 597 GLU A CG  
4695 C CD  . GLU A 597 ? 0.7315 0.8094 1.0434 -0.1769 -0.0347 -0.0322 597 GLU A CD  
4696 O OE1 . GLU A 597 ? 0.7813 0.8519 1.0760 -0.1696 -0.0591 -0.0361 597 GLU A OE1 
4697 O OE2 . GLU A 597 ? 0.7636 0.8573 1.1171 -0.1932 -0.0235 -0.0390 597 GLU A OE2 
4698 N N   . ASP A 598 ? 0.4132 0.5047 0.6823 -0.1247 -0.0165 -0.0152 598 ASP A N   
4699 C CA  . ASP A 598 ? 0.4210 0.5421 0.7336 -0.1223 -0.0038 -0.0227 598 ASP A CA  
4700 C C   . ASP A 598 ? 0.3712 0.4852 0.6597 -0.1161 0.0157  -0.0198 598 ASP A C   
4701 O O   . ASP A 598 ? 0.4146 0.5432 0.7209 -0.1233 0.0396  -0.0249 598 ASP A O   
4702 C CB  . ASP A 598 ? 0.3561 0.4994 0.7068 -0.1086 -0.0270 -0.0286 598 ASP A CB  
4703 C CG  . ASP A 598 ? 0.4526 0.6251 0.8525 -0.1026 -0.0139 -0.0368 598 ASP A CG  
4704 O OD1 . ASP A 598 ? 0.5184 0.7124 0.9564 -0.1152 0.0048  -0.0450 598 ASP A OD1 
4705 O OD2 . ASP A 598 ? 0.5033 0.6763 0.9056 -0.0855 -0.0205 -0.0355 598 ASP A OD2 
4706 N N   . GLN A 599 ? 0.3531 0.4455 0.6013 -0.1042 0.0071  -0.0130 599 GLN A N   
4707 C CA  . GLN A 599 ? 0.3683 0.4574 0.6001 -0.0971 0.0217  -0.0136 599 GLN A CA  
4708 C C   . GLN A 599 ? 0.4552 0.5281 0.6448 -0.1069 0.0400  -0.0077 599 GLN A C   
4709 O O   . GLN A 599 ? 0.4768 0.5560 0.6616 -0.1081 0.0588  -0.0124 599 GLN A O   
4710 C CB  . GLN A 599 ? 0.3802 0.4548 0.5929 -0.0806 0.0050  -0.0097 599 GLN A CB  
4711 C CG  . GLN A 599 ? 0.3959 0.4865 0.6486 -0.0677 -0.0109 -0.0134 599 GLN A CG  
4712 C CD  . GLN A 599 ? 0.4384 0.5532 0.7362 -0.0640 0.0049  -0.0241 599 GLN A CD  
4713 O OE1 . GLN A 599 ? 0.4457 0.5563 0.7325 -0.0626 0.0231  -0.0284 599 GLN A OE1 
4714 N NE2 . GLN A 599 ? 0.4416 0.5831 0.7929 -0.0627 -0.0019 -0.0301 599 GLN A NE2 
4715 N N   . VAL A 600 ? 0.3891 0.4409 0.5477 -0.1136 0.0345  0.0022  600 VAL A N   
4716 C CA  . VAL A 600 ? 0.4511 0.4864 0.5694 -0.1212 0.0482  0.0111  600 VAL A CA  
4717 C C   . VAL A 600 ? 0.4776 0.5147 0.6032 -0.1384 0.0636  0.0150  600 VAL A C   
4718 O O   . VAL A 600 ? 0.4612 0.4957 0.5647 -0.1465 0.0824  0.0201  600 VAL A O   
4719 C CB  . VAL A 600 ? 0.4966 0.5045 0.5761 -0.1150 0.0334  0.0211  600 VAL A CB  
4720 C CG1 . VAL A 600 ? 0.4912 0.4864 0.5309 -0.1173 0.0438  0.0297  600 VAL A CG1 
4721 C CG2 . VAL A 600 ? 0.4461 0.4521 0.5261 -0.0998 0.0175  0.0172  600 VAL A CG2 
4722 N N   . ASN A 601 ? 0.4591 0.4998 0.6139 -0.1451 0.0559  0.0129  601 ASN A N   
4723 C CA  . ASN A 601 ? 0.4610 0.5092 0.6393 -0.1628 0.0723  0.0128  601 ASN A CA  
4724 C C   . ASN A 601 ? 0.5294 0.5517 0.6664 -0.1727 0.0855  0.0287  601 ASN A C   
4725 O O   . ASN A 601 ? 0.5210 0.5171 0.6308 -0.1693 0.0727  0.0383  601 ASN A O   
4726 C CB  . ASN A 601 ? 0.4646 0.5449 0.6816 -0.1657 0.0900  0.0007  601 ASN A CB  
4727 C CG  . ASN A 601 ? 0.5994 0.6942 0.8550 -0.1841 0.1066  -0.0030 601 ASN A CG  
4728 O OD1 . ASN A 601 ? 0.6474 0.7314 0.9108 -0.1936 0.0997  0.0007  601 ASN A OD1 
4729 N ND2 . ASN A 601 ? 0.5412 0.6604 0.8235 -0.1899 0.1303  -0.0118 601 ASN A ND2 
4730 N N   . ALA A 602 ? 0.5122 0.5395 0.6424 -0.1844 0.1109  0.0328  602 ALA A N   
4731 C CA  . ALA A 602 ? 0.5127 0.5143 0.6033 -0.1944 0.1230  0.0513  602 ALA A CA  
4732 C C   . ALA A 602 ? 0.5502 0.5351 0.5870 -0.1838 0.1172  0.0622  602 ALA A C   
4733 O O   . ALA A 602 ? 0.5713 0.5336 0.5722 -0.1889 0.1224  0.0802  602 ALA A O   
4734 C CB  . ALA A 602 ? 0.5216 0.5345 0.6196 -0.2118 0.1537  0.0529  602 ALA A CB  
4735 N N   . ASP A 603 ? 0.5147 0.5101 0.5472 -0.1693 0.1061  0.0524  603 ASP A N   
4736 C CA  . ASP A 603 ? 0.5374 0.5205 0.5256 -0.1594 0.0986  0.0595  603 ASP A CA  
4737 C C   . ASP A 603 ? 0.4989 0.4643 0.4803 -0.1468 0.0746  0.0630  603 ASP A C   
4738 O O   . ASP A 603 ? 0.4255 0.3829 0.3779 -0.1376 0.0662  0.0670  603 ASP A O   
4739 C CB  . ASP A 603 ? 0.5329 0.5367 0.5202 -0.1531 0.1047  0.0451  603 ASP A CB  
4740 C CG  . ASP A 603 ? 0.6620 0.6783 0.6368 -0.1655 0.1310  0.0432  603 ASP A CG  
4741 O OD1 . ASP A 603 ? 0.6690 0.6713 0.6061 -0.1744 0.1394  0.0591  603 ASP A OD1 
4742 O OD2 . ASP A 603 ? 0.5650 0.6046 0.5674 -0.1660 0.1438  0.0261  603 ASP A OD2 
4743 N N   . LEU A 604 ? 0.4622 0.4224 0.4701 -0.1471 0.0640  0.0600  604 LEU A N   
4744 C CA  . LEU A 604 ? 0.4617 0.4049 0.4621 -0.1364 0.0441  0.0612  604 LEU A CA  
4745 C C   . LEU A 604 ? 0.4735 0.3888 0.4468 -0.1381 0.0428  0.0778  604 LEU A C   
4746 O O   . LEU A 604 ? 0.4904 0.3938 0.4704 -0.1494 0.0503  0.0854  604 LEU A O   
4747 C CB  . LEU A 604 ? 0.4970 0.4441 0.5304 -0.1376 0.0332  0.0510  604 LEU A CB  
4748 C CG  . LEU A 604 ? 0.4898 0.4192 0.5138 -0.1284 0.0147  0.0499  604 LEU A CG  
4749 C CD1 . LEU A 604 ? 0.4328 0.3660 0.4428 -0.1136 0.0060  0.0463  604 LEU A CD1 
4750 C CD2 . LEU A 604 ? 0.4930 0.4271 0.5454 -0.1330 0.0043  0.0393  604 LEU A CD2 
4751 N N   . PRO A 605 ? 0.5250 0.4293 0.4715 -0.1272 0.0339  0.0839  605 PRO A N   
4752 C CA  . PRO A 605 ? 0.4972 0.3758 0.4233 -0.1265 0.0311  0.1005  605 PRO A CA  
4753 C C   . PRO A 605 ? 0.5234 0.3821 0.4669 -0.1280 0.0245  0.0993  605 PRO A C   
4754 O O   . PRO A 605 ? 0.5322 0.3952 0.4922 -0.1242 0.0154  0.0853  605 PRO A O   
4755 C CB  . PRO A 605 ? 0.5401 0.4182 0.4450 -0.1129 0.0204  0.1018  605 PRO A CB  
4756 C CG  . PRO A 605 ? 0.4534 0.3567 0.3597 -0.1106 0.0235  0.0888  605 PRO A CG  
4757 C CD  . PRO A 605 ? 0.4638 0.3795 0.4012 -0.1155 0.0271  0.0760  605 PRO A CD  
4758 N N   . TYR A 606 ? 0.5377 0.3729 0.4757 -0.1338 0.0294  0.1142  606 TYR A N   
4759 C CA  . TYR A 606 ? 0.5712 0.3850 0.5279 -0.1376 0.0260  0.1112  606 TYR A CA  
4760 C C   . TYR A 606 ? 0.5744 0.3775 0.5286 -0.1243 0.0120  0.1037  606 TYR A C   
4761 O O   . TYR A 606 ? 0.5495 0.3462 0.5197 -0.1262 0.0067  0.0905  606 TYR A O   
4762 C CB  . TYR A 606 ? 0.5994 0.3860 0.5511 -0.1453 0.0354  0.1308  606 TYR A CB  
4763 C CG  . TYR A 606 ? 0.6688 0.4272 0.6379 -0.1468 0.0319  0.1279  606 TYR A CG  
4764 C CD1 . TYR A 606 ? 0.6907 0.4491 0.6885 -0.1595 0.0347  0.1131  606 TYR A CD1 
4765 C CD2 . TYR A 606 ? 0.6876 0.4219 0.6478 -0.1345 0.0258  0.1372  606 TYR A CD2 
4766 C CE1 . TYR A 606 ? 0.7852 0.5171 0.7983 -0.1621 0.0322  0.1071  606 TYR A CE1 
4767 C CE2 . TYR A 606 ? 0.7356 0.4463 0.7147 -0.1336 0.0257  0.1303  606 TYR A CE2 
4768 C CZ  . TYR A 606 ? 0.7153 0.4236 0.7189 -0.1480 0.0292  0.1148  606 TYR A CZ  
4769 O OH  . TYR A 606 ? 0.9179 0.6022 0.9388 -0.1484 0.0301  0.1049  606 TYR A OH  
4770 N N   . GLU A 607 ? 0.4804 0.2826 0.4148 -0.1117 0.0062  0.1108  607 GLU A N   
4771 C CA  . GLU A 607 ? 0.5960 0.3888 0.5304 -0.0997 -0.0039 0.1036  607 GLU A CA  
4772 C C   . GLU A 607 ? 0.5564 0.3655 0.4969 -0.0970 -0.0097 0.0847  607 GLU A C   
4773 O O   . GLU A 607 ? 0.5366 0.3356 0.4792 -0.0918 -0.0154 0.0752  607 GLU A O   
4774 C CB  . GLU A 607 ? 0.6041 0.3972 0.5216 -0.0877 -0.0087 0.1145  607 GLU A CB  
4775 C CG  . GLU A 607 ? 0.7263 0.4976 0.6379 -0.0864 -0.0076 0.1352  607 GLU A CG  
4776 C CD  . GLU A 607 ? 0.8036 0.5770 0.7041 -0.0728 -0.0168 0.1445  607 GLU A CD  
4777 O OE1 . GLU A 607 ? 0.7349 0.5314 0.6245 -0.0690 -0.0207 0.1394  607 GLU A OE1 
4778 O OE2 . GLU A 607 ? 1.0392 0.7914 0.9455 -0.0657 -0.0205 0.1561  607 GLU A OE2 
4779 N N   . ILE A 608 ? 0.4897 0.3231 0.4328 -0.1001 -0.0078 0.0795  608 ILE A N   
4780 C CA  . ILE A 608 ? 0.4660 0.3131 0.4171 -0.0972 -0.0144 0.0645  608 ILE A CA  
4781 C C   . ILE A 608 ? 0.4863 0.3307 0.4554 -0.1064 -0.0174 0.0548  608 ILE A C   
4782 O O   . ILE A 608 ? 0.5103 0.3518 0.4792 -0.1034 -0.0265 0.0440  608 ILE A O   
4783 C CB  . ILE A 608 ? 0.4707 0.3434 0.4242 -0.0962 -0.0112 0.0617  608 ILE A CB  
4784 C CG1 . ILE A 608 ? 0.4074 0.2833 0.3426 -0.0884 -0.0095 0.0678  608 ILE A CG1 
4785 C CG2 . ILE A 608 ? 0.4461 0.3307 0.4100 -0.0918 -0.0194 0.0494  608 ILE A CG2 
4786 C CD1 . ILE A 608 ? 0.4373 0.3061 0.3646 -0.0772 -0.0171 0.0639  608 ILE A CD1 
4787 N N   . GLU A 609 ? 0.4578 0.3035 0.4418 -0.1188 -0.0097 0.0582  609 GLU A N   
4788 C CA  . GLU A 609 ? 0.5332 0.3775 0.5390 -0.1297 -0.0128 0.0475  609 GLU A CA  
4789 C C   . GLU A 609 ? 0.4988 0.3152 0.4994 -0.1295 -0.0171 0.0433  609 GLU A C   
4790 O O   . GLU A 609 ? 0.5330 0.3488 0.5414 -0.1333 -0.0259 0.0284  609 GLU A O   
4791 C CB  . GLU A 609 ? 0.4944 0.3433 0.5197 -0.1445 -0.0001 0.0528  609 GLU A CB  
4792 C CG  . GLU A 609 ? 0.6611 0.5119 0.7156 -0.1579 -0.0031 0.0397  609 GLU A CG  
4793 C CD  . GLU A 609 ? 0.7600 0.6102 0.8354 -0.1745 0.0130  0.0462  609 GLU A CD  
4794 O OE1 . GLU A 609 ? 0.7828 0.6343 0.8467 -0.1752 0.0268  0.0610  609 GLU A OE1 
4795 O OE2 . GLU A 609 ? 0.8270 0.6750 0.9293 -0.1877 0.0125  0.0359  609 GLU A OE2 
4796 N N   . ARG A 610 ? 0.4785 0.2721 0.4664 -0.1247 -0.0115 0.0556  610 ARG A N   
4797 C CA  . ARG A 610 ? 0.5396 0.3052 0.5266 -0.1232 -0.0131 0.0508  610 ARG A CA  
4798 C C   . ARG A 610 ? 0.5138 0.2805 0.4875 -0.1133 -0.0222 0.0375  610 ARG A C   
4799 O O   . ARG A 610 ? 0.5656 0.3183 0.5406 -0.1163 -0.0254 0.0234  610 ARG A O   
4800 C CB  . ARG A 610 ? 0.5946 0.3377 0.5749 -0.1175 -0.0062 0.0689  610 ARG A CB  
4801 C CG  . ARG A 610 ? 0.6125 0.3250 0.5976 -0.1141 -0.0057 0.0641  610 ARG A CG  
4802 C CD  . ARG A 610 ? 0.6402 0.3305 0.6251 -0.1080 -0.0002 0.0852  610 ARG A CD  
4803 N NE  . ARG A 610 ? 0.6875 0.3912 0.6559 -0.0946 -0.0044 0.0976  610 ARG A NE  
4804 C CZ  . ARG A 610 ? 0.7211 0.4144 0.6852 -0.0871 -0.0038 0.1182  610 ARG A CZ  
4805 N NH1 . ARG A 610 ? 0.7405 0.4142 0.7149 -0.0874 0.0045  0.1280  610 ARG A NH1 
4806 N NH2 . ARG A 610 ? 0.7289 0.4386 0.6790 -0.0762 -0.0101 0.1258  610 ARG A NH2 
4807 N N   . GLU A 611 ? 0.5134 0.2956 0.4731 -0.1025 -0.0252 0.0410  611 GLU A N   
4808 C CA  . GLU A 611 ? 0.5078 0.2908 0.4533 -0.0942 -0.0315 0.0302  611 GLU A CA  
4809 C C   . GLU A 611 ? 0.5494 0.3455 0.4965 -0.0999 -0.0411 0.0165  611 GLU A C   
4810 O O   . GLU A 611 ? 0.5289 0.3165 0.4636 -0.0990 -0.0464 0.0044  611 GLU A O   
4811 C CB  . GLU A 611 ? 0.4978 0.2936 0.4320 -0.0830 -0.0311 0.0376  611 GLU A CB  
4812 C CG  . GLU A 611 ? 0.5022 0.2872 0.4338 -0.0755 -0.0258 0.0488  611 GLU A CG  
4813 C CD  . GLU A 611 ? 0.5304 0.2919 0.4620 -0.0712 -0.0236 0.0433  611 GLU A CD  
4814 O OE1 . GLU A 611 ? 0.5390 0.2965 0.4624 -0.0700 -0.0249 0.0298  611 GLU A OE1 
4815 O OE2 . GLU A 611 ? 0.6166 0.3629 0.5563 -0.0688 -0.0199 0.0525  611 GLU A OE2 
4816 N N   . LEU A 612 ? 0.5115 0.3293 0.4737 -0.1057 -0.0436 0.0180  612 LEU A N   
4817 C CA  . LEU A 612 ? 0.4898 0.3231 0.4602 -0.1109 -0.0555 0.0059  612 LEU A CA  
4818 C C   . LEU A 612 ? 0.5641 0.3835 0.5406 -0.1221 -0.0595 -0.0075 612 LEU A C   
4819 O O   . LEU A 612 ? 0.5101 0.3302 0.4756 -0.1229 -0.0713 -0.0206 612 LEU A O   
4820 C CB  . LEU A 612 ? 0.4551 0.3149 0.4503 -0.1156 -0.0550 0.0093  612 LEU A CB  
4821 C CG  . LEU A 612 ? 0.6213 0.5030 0.6341 -0.1197 -0.0695 -0.0020 612 LEU A CG  
4822 C CD1 . LEU A 612 ? 0.4926 0.3800 0.4858 -0.1075 -0.0820 -0.0033 612 LEU A CD1 
4823 C CD2 . LEU A 612 ? 0.6018 0.5094 0.6478 -0.1255 -0.0646 0.0003  612 LEU A CD2 
4824 N N   . ARG A 613 ? 0.5385 0.3435 0.5307 -0.1314 -0.0495 -0.0045 613 ARG A N   
4825 C CA  . ARG A 613 ? 0.5314 0.3205 0.5336 -0.1435 -0.0513 -0.0190 613 ARG A CA  
4826 C C   . ARG A 613 ? 0.5396 0.3036 0.5187 -0.1380 -0.0513 -0.0286 613 ARG A C   
4827 O O   . ARG A 613 ? 0.5435 0.3012 0.5189 -0.1454 -0.0585 -0.0474 613 ARG A O   
4828 C CB  . ARG A 613 ? 0.5182 0.2929 0.5434 -0.1544 -0.0378 -0.0109 613 ARG A CB  
4829 C CG  . ARG A 613 ? 0.5469 0.3455 0.5976 -0.1637 -0.0341 -0.0048 613 ARG A CG  
4830 C CD  . ARG A 613 ? 0.7049 0.4848 0.7770 -0.1777 -0.0198 0.0013  613 ARG A CD  
4831 N NE  . ARG A 613 ? 0.8329 0.6355 0.9308 -0.1888 -0.0127 0.0058  613 ARG A NE  
4832 C CZ  . ARG A 613 ? 0.8255 0.6199 0.9505 -0.2059 -0.0012 0.0062  613 ARG A CZ  
4833 N NH1 . ARG A 613 ? 0.7889 0.5513 0.9203 -0.2139 0.0032  0.0020  613 ARG A NH1 
4834 N NH2 . ARG A 613 ? 0.8981 0.7161 1.0467 -0.2157 0.0077  0.0100  613 ARG A NH2 
4835 N N   . ALA A 614 ? 0.5004 0.2510 0.4650 -0.1257 -0.0428 -0.0175 614 ALA A N   
4836 C CA  . ALA A 614 ? 0.5369 0.2651 0.4840 -0.1197 -0.0395 -0.0271 614 ALA A CA  
4837 C C   . ALA A 614 ? 0.6051 0.3434 0.5257 -0.1162 -0.0495 -0.0395 614 ALA A C   
4838 O O   . ALA A 614 ? 0.6135 0.3381 0.5201 -0.1203 -0.0510 -0.0572 614 ALA A O   
4839 C CB  . ALA A 614 ? 0.5384 0.2557 0.4823 -0.1066 -0.0294 -0.0119 614 ALA A CB  
4840 N N   . LEU A 615 ? 0.5707 0.3312 0.4824 -0.1089 -0.0558 -0.0302 615 LEU A N   
4841 C CA  . LEU A 615 ? 0.5002 0.2687 0.3852 -0.1051 -0.0658 -0.0376 615 LEU A CA  
4842 C C   . LEU A 615 ? 0.6146 0.3919 0.4992 -0.1163 -0.0812 -0.0530 615 LEU A C   
4843 O O   . LEU A 615 ? 0.5736 0.3441 0.4305 -0.1178 -0.0877 -0.0662 615 LEU A O   
4844 C CB  . LEU A 615 ? 0.5867 0.3756 0.4689 -0.0954 -0.0691 -0.0233 615 LEU A CB  
4845 C CG  . LEU A 615 ? 0.6106 0.4065 0.4657 -0.0902 -0.0797 -0.0257 615 LEU A CG  
4846 C CD1 . LEU A 615 ? 0.6174 0.3914 0.4405 -0.0874 -0.0723 -0.0337 615 LEU A CD1 
4847 C CD2 . LEU A 615 ? 0.5358 0.3474 0.3944 -0.0802 -0.0799 -0.0110 615 LEU A CD2 
4848 N N   . LYS A 616 ? 0.5539 0.3476 0.4690 -0.1251 -0.0870 -0.0522 616 LYS A N   
4849 C CA  . LYS A 616 ? 0.5896 0.3960 0.5120 -0.1367 -0.1035 -0.0682 616 LYS A CA  
4850 C C   . LYS A 616 ? 0.6695 0.4523 0.5833 -0.1474 -0.1013 -0.0886 616 LYS A C   
4851 O O   . LYS A 616 ? 0.6422 0.4294 0.5401 -0.1541 -0.1162 -0.1060 616 LYS A O   
4852 C CB  . LYS A 616 ? 0.6234 0.4514 0.5881 -0.1454 -0.1055 -0.0644 616 LYS A CB  
4853 C CG  . LYS A 616 ? 0.6365 0.4862 0.6178 -0.1567 -0.1252 -0.0803 616 LYS A CG  
4854 C CD  . LYS A 616 ? 0.8115 0.6957 0.8258 -0.1552 -0.1324 -0.0715 616 LYS A CD  
4855 C CE  . LYS A 616 ? 0.8723 0.7832 0.9044 -0.1634 -0.1567 -0.0869 616 LYS A CE  
4856 N NZ  . LYS A 616 ? 0.8274 0.7738 0.8912 -0.1573 -0.1657 -0.0782 616 LYS A NZ  
4857 N N   . GLN A 617 ? 0.6144 0.3712 0.5379 -0.1486 -0.0834 -0.0872 617 GLN A N   
4858 C CA  . GLN A 617 ? 0.6623 0.3932 0.5825 -0.1583 -0.0783 -0.1079 617 GLN A CA  
4859 C C   . GLN A 617 ? 0.6666 0.3826 0.5455 -0.1515 -0.0761 -0.1191 617 GLN A C   
4860 O O   . GLN A 617 ? 0.6753 0.3832 0.5368 -0.1607 -0.0818 -0.1423 617 GLN A O   
4861 C CB  . GLN A 617 ? 0.6329 0.3386 0.5799 -0.1599 -0.0596 -0.1004 617 GLN A CB  
4862 C CG  . GLN A 617 ? 0.6736 0.3492 0.6256 -0.1699 -0.0519 -0.1222 617 GLN A CG  
4863 C CD  . GLN A 617 ? 0.6820 0.3642 0.6548 -0.1896 -0.0619 -0.1416 617 GLN A CD  
4864 O OE1 . GLN A 617 ? 0.7695 0.4785 0.7624 -0.1959 -0.0720 -0.1354 617 GLN A OE1 
4865 N NE2 . GLN A 617 ? 0.6830 0.3515 0.6601 -0.1934 -0.0591 -0.1632 617 GLN A NE2 
4866 N N   . ARG A 618 ? 0.6511 0.3638 0.5135 -0.1365 -0.0669 -0.1042 618 ARG A N   
4867 C CA  . ARG A 618 ? 0.7432 0.4421 0.5678 -0.1306 -0.0609 -0.1138 618 ARG A CA  
4868 C C   . ARG A 618 ? 0.7534 0.4670 0.5412 -0.1335 -0.0785 -0.1227 618 ARG A C   
4869 O O   . ARG A 618 ? 0.7737 0.4736 0.5269 -0.1367 -0.0763 -0.1402 618 ARG A O   
4870 C CB  . ARG A 618 ? 0.6341 0.3314 0.4547 -0.1150 -0.0483 -0.0952 618 ARG A CB  
4871 C CG  . ARG A 618 ? 0.6606 0.3431 0.5128 -0.1100 -0.0331 -0.0855 618 ARG A CG  
4872 C CD  . ARG A 618 ? 0.5662 0.2459 0.4127 -0.0956 -0.0211 -0.0741 618 ARG A CD  
4873 N NE  . ARG A 618 ? 0.5952 0.2981 0.4362 -0.0884 -0.0277 -0.0566 618 ARG A NE  
4874 C CZ  . ARG A 618 ? 0.5755 0.2913 0.4386 -0.0849 -0.0295 -0.0389 618 ARG A CZ  
4875 N NH1 . ARG A 618 ? 0.6342 0.3425 0.5236 -0.0878 -0.0260 -0.0330 618 ARG A NH1 
4876 N NH2 . ARG A 618 ? 0.5636 0.2986 0.4208 -0.0787 -0.0339 -0.0268 618 ARG A NH2 
4877 N N   . ILE A 619 ? 0.7223 0.4632 0.5162 -0.1320 -0.0957 -0.1106 619 ILE A N   
4878 C CA  . ILE A 619 ? 0.7686 0.5242 0.5291 -0.1329 -0.1158 -0.1152 619 ILE A CA  
4879 C C   . ILE A 619 ? 0.7595 0.5179 0.5178 -0.1488 -0.1311 -0.1398 619 ILE A C   
4880 O O   . ILE A 619 ? 0.8378 0.5945 0.5541 -0.1524 -0.1423 -0.1531 619 ILE A O   
4881 C CB  . ILE A 619 ? 0.7336 0.5174 0.5089 -0.1247 -0.1295 -0.0947 619 ILE A CB  
4882 C CG1 . ILE A 619 ? 0.6712 0.4505 0.4424 -0.1101 -0.1144 -0.0742 619 ILE A CG1 
4883 C CG2 . ILE A 619 ? 0.7710 0.5717 0.5185 -0.1250 -0.1546 -0.0974 619 ILE A CG2 
4884 C CD1 . ILE A 619 ? 0.8078 0.6113 0.5981 -0.1019 -0.1235 -0.0557 619 ILE A CD1 
4885 N N   . SER A 620 ? 0.7431 0.5052 0.5451 -0.1595 -0.1315 -0.1466 620 SER A N   
4886 C CA  . SER A 620 ? 0.7961 0.5618 0.6031 -0.1767 -0.1457 -0.1724 620 SER A CA  
4887 C C   . SER A 620 ? 0.8117 0.5517 0.5942 -0.1811 -0.1325 -0.1957 620 SER A C   
4888 O O   . SER A 620 ? 0.8704 0.6216 0.6445 -0.1880 -0.1436 -0.2169 620 SER A O   
4889 C CB  . SER A 620 ? 0.8043 0.5774 0.6688 -0.1878 -0.1436 -0.1733 620 SER A CB  
4890 O OG  . SER A 620 ? 0.7809 0.5250 0.6648 -0.1879 -0.1184 -0.1704 620 SER A OG  
4891 N N   . GLN A 621 ? 0.8494 0.5596 0.6261 -0.1748 -0.1081 -0.1921 621 GLN A N   
4892 C CA  . GLN A 621 ? 0.8557 0.5446 0.6187 -0.1752 -0.0918 -0.2129 621 GLN A CA  
4893 C C   . GLN A 621 ? 0.9406 0.6295 0.6461 -0.1697 -0.0930 -0.2191 621 GLN A C   
4894 O O   . GLN A 621 ? 1.0463 0.7219 0.7366 -0.1710 -0.0815 -0.2392 621 GLN A O   
4895 C CB  . GLN A 621 ? 0.8402 0.5007 0.6264 -0.1681 -0.0654 -0.2053 621 GLN A CB  
4896 C CG  . GLN A 621 ? 0.8045 0.4605 0.6455 -0.1729 -0.0607 -0.1979 621 GLN A CG  
4897 C CD  . GLN A 621 ? 0.9342 0.5891 0.8009 -0.1845 -0.0649 -0.2200 621 GLN A CD  
4898 O OE1 . GLN A 621 ? 1.0359 0.6768 0.8901 -0.1850 -0.0589 -0.2404 621 GLN A OE1 
4899 N NE2 . GLN A 621 ? 0.9796 0.6483 0.8824 -0.1942 -0.0749 -0.2158 621 GLN A NE2 
4900 N N   . MET A 622 ? 0.9705 0.6732 0.6450 -0.1631 -0.1056 -0.2014 622 MET A N   
4901 C CA  . MET A 622 ? 1.0022 0.7047 0.6203 -0.1576 -0.1058 -0.2025 622 MET A CA  
4902 C C   . MET A 622 ? 1.0373 0.7557 0.6344 -0.1652 -0.1222 -0.2236 622 MET A C   
4903 O O   . MET A 622 ? 1.0662 0.8073 0.6878 -0.1723 -0.1438 -0.2297 622 MET A O   
4904 C CB  . MET A 622 ? 1.0116 0.7260 0.6071 -0.1480 -0.1181 -0.1759 622 MET A CB  
4905 C CG  . MET A 622 ? 0.9207 0.6268 0.5383 -0.1362 -0.1004 -0.1537 622 MET A CG  
4906 S SD  . MET A 622 ? 0.9687 0.6944 0.5708 -0.1219 -0.1119 -0.1224 622 MET A SD  
4907 C CE  . MET A 622 ? 0.9590 0.6689 0.4842 -0.1221 -0.1089 -0.1285 622 MET A CE  
4908 O OXT . MET A 622 ? 1.1788 0.8893 0.7353 -0.1644 -0.1141 -0.2356 622 MET A OXT 
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