data_9EIW
# 
_entry.id   9EIW 
# 
_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   9EIW         pdb_00009eiw 10.2210/pdb9eiw/pdb 
WWPDB D_1000290521 ?            ?                   
# 
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                        9EIW 
_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 '2-PHOSPHOGLYCOLIC ACID'                             156.031   1  ?        ? ? ? 
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                           443.201   1  ?        ? ? ? 
5 water       nat water                                                18.015    82 ?        ? ? ? 
# 
_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 '2-PHOSPHOGLYCOLIC ACID'   PGA 
4 "GUANOSINE-5'-DIPHOSPHATE" GDP 
5 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O11 P2' 443.201 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                      ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'     149.211 
MN  non-polymer         . 'MANGANESE (II) ION'       ? 'Mn 2'              54.938  
PGA non-polymer         . '2-PHOSPHOGLYCOLIC ACID'   ? 'C2 H5 O6 P'        156.031 
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 GDP ? ? GDP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PGA ? ? PGA ? ? '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 PGA 1  704 800 PGA PGA A . 
F 4 GDP 1  705 900 GDP GDP A . 
G 5 HOH 1  801 803 HOH HOH A . 
G 5 HOH 2  802 802 HOH HOH A . 
G 5 HOH 3  803 801 HOH HOH A . 
G 5 HOH 4  804 45  HOH HOH A . 
G 5 HOH 5  805 32  HOH HOH A . 
G 5 HOH 6  806 54  HOH HOH A . 
G 5 HOH 7  807 7   HOH HOH A . 
G 5 HOH 8  808 18  HOH HOH A . 
G 5 HOH 9  809 53  HOH HOH A . 
G 5 HOH 10 810 75  HOH HOH A . 
G 5 HOH 11 811 9   HOH HOH A . 
G 5 HOH 12 812 40  HOH HOH A . 
G 5 HOH 13 813 12  HOH HOH A . 
G 5 HOH 14 814 28  HOH HOH A . 
G 5 HOH 15 815 52  HOH HOH A . 
G 5 HOH 16 816 14  HOH HOH A . 
G 5 HOH 17 817 38  HOH HOH A . 
G 5 HOH 18 818 34  HOH HOH A . 
G 5 HOH 19 819 20  HOH HOH A . 
G 5 HOH 20 820 25  HOH HOH A . 
G 5 HOH 21 821 21  HOH HOH A . 
G 5 HOH 22 822 8   HOH HOH A . 
G 5 HOH 23 823 19  HOH HOH A . 
G 5 HOH 24 824 55  HOH HOH A . 
G 5 HOH 25 825 6   HOH HOH A . 
G 5 HOH 26 826 57  HOH HOH A . 
G 5 HOH 27 827 24  HOH HOH A . 
G 5 HOH 28 828 29  HOH HOH A . 
G 5 HOH 29 829 74  HOH HOH A . 
G 5 HOH 30 830 56  HOH HOH A . 
G 5 HOH 31 831 30  HOH HOH A . 
G 5 HOH 32 832 62  HOH HOH A . 
G 5 HOH 33 833 16  HOH HOH A . 
G 5 HOH 34 834 43  HOH HOH A . 
G 5 HOH 35 835 76  HOH HOH A . 
G 5 HOH 36 836 59  HOH HOH A . 
G 5 HOH 37 837 11  HOH HOH A . 
G 5 HOH 38 838 68  HOH HOH A . 
G 5 HOH 39 839 1   HOH HOH A . 
G 5 HOH 40 840 4   HOH HOH A . 
G 5 HOH 41 841 17  HOH HOH A . 
G 5 HOH 42 842 66  HOH HOH A . 
G 5 HOH 43 843 63  HOH HOH A . 
G 5 HOH 44 844 26  HOH HOH A . 
G 5 HOH 45 845 46  HOH HOH A . 
G 5 HOH 46 846 73  HOH HOH A . 
G 5 HOH 47 847 3   HOH HOH A . 
G 5 HOH 48 848 47  HOH HOH A . 
G 5 HOH 49 849 33  HOH HOH A . 
G 5 HOH 50 850 15  HOH HOH A . 
G 5 HOH 51 851 48  HOH HOH A . 
G 5 HOH 52 852 77  HOH HOH A . 
G 5 HOH 53 853 2   HOH HOH A . 
G 5 HOH 54 854 71  HOH HOH A . 
G 5 HOH 55 855 42  HOH HOH A . 
G 5 HOH 56 856 36  HOH HOH A . 
G 5 HOH 57 857 50  HOH HOH A . 
G 5 HOH 58 858 65  HOH HOH A . 
G 5 HOH 59 859 10  HOH HOH A . 
G 5 HOH 60 860 13  HOH HOH A . 
G 5 HOH 61 861 22  HOH HOH A . 
G 5 HOH 62 862 37  HOH HOH A . 
G 5 HOH 63 863 5   HOH HOH A . 
G 5 HOH 64 864 27  HOH HOH A . 
G 5 HOH 65 865 72  HOH HOH A . 
G 5 HOH 66 866 64  HOH HOH A . 
G 5 HOH 67 867 51  HOH HOH A . 
G 5 HOH 68 868 39  HOH HOH A . 
G 5 HOH 69 869 49  HOH HOH A . 
G 5 HOH 70 870 35  HOH HOH A . 
G 5 HOH 71 871 44  HOH HOH A . 
G 5 HOH 72 872 61  HOH HOH A . 
G 5 HOH 73 873 31  HOH HOH A . 
G 5 HOH 74 874 58  HOH HOH A . 
G 5 HOH 75 875 41  HOH HOH A . 
G 5 HOH 76 876 70  HOH HOH A . 
G 5 HOH 77 877 60  HOH HOH A . 
G 5 HOH 78 878 67  HOH HOH A . 
G 5 HOH 79 879 23  HOH HOH A . 
G 5 HOH 80 880 69  HOH HOH A . 
G 5 HOH 81 881 78  HOH HOH A . 
G 5 HOH 82 882 79  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 ? ? ? '(1.21.2_5419: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.39 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EIW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.128 
_cell.length_a_esd                 ? 
_cell.length_b                     120.194 
_cell.length_b_esd                 ? 
_cell.length_c                     60.551 
_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                         9EIW 
_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                   9EIW 
_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             2.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.09 
_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, 100 mM GDP, and 18-28% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     273 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.1271 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CHESS BEAMLINE 7B2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1271 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   7B2 
_diffrn_source.pdbx_synchrotron_site       CHESS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EIW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               120.28 
_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                                     30501 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.94 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.73 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.0 
_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                                0.1440 
_reflns.pdbx_Rpim_I_all                                0.0550 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9970 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1330 
_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                                    2.20 
_reflns_shell.d_res_low                                     2.24 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1539 
_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                               6.49 
_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                               2.1370 
_reflns_shell.pdbx_Rpim_I_all                               0.8330 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.6250 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.74 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.9650 
_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                                 9EIW 
_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                            2.20 
_refine.ls_d_res_low                             56.38 
_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                     29665 
_refine.ls_number_reflns_R_free                  1413 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.07 
_refine.ls_percent_reflns_R_free                 4.76 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2033 
_refine.ls_R_factor_R_free                       0.2635 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2004 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.17 
_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                            0.42 
_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         40 
_refine_hist.number_atoms_solvent             82 
_refine_hist.number_atoms_total               4991 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        56.38 
# 
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' ? 0.518  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.368 ? 1909 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 719  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 900  ? 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' 2.20 2.28  . . 127 2271 78.00  . . . . 0.3768 . . . . . . . . . . . 0.4177 
'X-RAY DIFFRACTION' 2.28 2.37  . . 152 2790 97.00  . . . . 0.3609 . . . . . . . . . . . 0.4112 
'X-RAY DIFFRACTION' 2.37 2.48  . . 116 2878 99.00  . . . . 0.3345 . . . . . . . . . . . 0.3793 
'X-RAY DIFFRACTION' 2.48 2.61  . . 132 2892 99.00  . . . . 0.3100 . . . . . . . . . . . 0.3662 
'X-RAY DIFFRACTION' 2.61 2.77  . . 152 2886 99.00  . . . . 0.2703 . . . . . . . . . . . 0.3187 
'X-RAY DIFFRACTION' 2.77 2.98  . . 155 2883 100.00 . . . . 0.2355 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 2.98 3.28  . . 135 2901 100.00 . . . . 0.2066 . . . . . . . . . . . 0.2883 
'X-RAY DIFFRACTION' 3.28 3.76  . . 151 2903 99.00  . . . . 0.1769 . . . . . . . . . . . 0.2823 
'X-RAY DIFFRACTION' 3.76 4.74  . . 157 2884 100.00 . . . . 0.1537 . . . . . . . . . . . 0.2035 
'X-RAY DIFFRACTION' 4.74 56.38 . . 136 2964 100.00 . . . . 0.1545 . . . . . . . . . . . 0.2047 
# 
_struct.entry_id                     9EIW 
_struct.title                        'Rat cytosolic PEPCK in complex with GDP and phosphoglycolic acid (273K)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EIW 
_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 ? 
# 
_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              9EIW 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 10  ? ALA A 13  ? ASP A 10  ALA A 13  5 ? 4  
HELX_P HELX_P2  AA2 SER A 19  ? LEU A 23  ? SER A 19  LEU A 23  5 ? 5  
HELX_P HELX_P3  AA3 PRO A 24  ? GLN A 39  ? PRO A 24  GLN A 39  1 ? 16 
HELX_P HELX_P4  AA4 SER A 49  ? GLU A 63  ? SER A 49  GLU A 63  1 ? 15 
HELX_P HELX_P5  AA5 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 LEU A 206 ? TRP A 210 ? LEU A 206 TRP A 210 5 ? 5  
HELX_P HELX_P10 AB1 TYR A 235 ? LEU A 240 ? TYR A 235 LEU A 240 1 ? 6  
HELX_P HELX_P11 AB2 LYS A 243 ? LEU A 248 ? LYS A 243 LEU A 248 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P13 AB4 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P14 AB5 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P15 AB6 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P16 AB7 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P17 AB8 PRO A 479 ? MET A 482 ? PRO A 479 MET A 482 5 ? 4  
HELX_P HELX_P18 AB9 ASN A 489 ? MET A 500 ? ASN A 489 MET A 500 1 ? 12 
HELX_P HELX_P19 AC1 ALA A 501 ? ARG A 503 ? ALA A 501 ARG A 503 5 ? 3  
HELX_P HELX_P20 AC2 GLY A 529 ? GLY A 531 ? GLY A 529 GLY A 531 5 ? 3  
HELX_P HELX_P21 AC3 GLU A 532 ? GLY A 546 ? GLU A 532 GLY A 546 1 ? 15 
HELX_P HELX_P22 AC4 ASN A 573 ? GLY A 579 ? ASN A 573 GLY A 579 1 ? 7  
HELX_P HELX_P23 AC5 SER A 581 ? VAL A 600 ? SER A 581 VAL A 600 1 ? 20 
HELX_P HELX_P24 AC6 ASN A 601 ? LEU A 604 ? ASN A 601 LEU A 604 5 ? 4  
HELX_P HELX_P25 AC7 PRO A 605 ? GLN A 621 ? PRO A 605 GLN A 621 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A LYS 244 NZ  ? ? ? 1_555 B MN  . MN  ? ? A LYS 244 A MN  701 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc2  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 B MN  . MN  ? ? A HIS 264 A MN  701 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc3  metalc ? ? A THR 291 OG1 ? ? ? 1_555 C MN  . MN  ? ? A THR 291 A MN  702 1_555 ? ? ? ? ? ? ? 2.591 ? ? 
metalc4  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 B MN  . MN  ? ? A ASP 311 A MN  701 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc5  metalc ? ? A GLU 607 OE1 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 1_555 ? ? ? ? ? ? ? 2.630 ? ? 
metalc6  metalc ? ? A GLU 607 OE2 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc7  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O4P B ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.702 ? ? 
metalc8  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O1P A ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O4P A ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.777 ? ? 
metalc10 metalc ? ? B MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  701 A HOH 802 1_555 ? ? ? ? ? ? ? 2.387 ? ? 
metalc11 metalc ? ? B MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  701 A HOH 803 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc12 metalc ? ? C MN  .   MN  ? ? ? 1_555 E PGA . O3P A ? A MN  702 A PGA 704 1_555 ? ? ? ? ? ? ? 2.476 ? ? 
metalc13 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GDP . O3B ? ? A MN  702 A GDP 705 1_555 ? ? ? ? ? ? ? 2.511 ? ? 
metalc14 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 811 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc15 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 834 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
# 
_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 ? B MN . ? A MN 701 ? 1_555 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 98.9  ? 
2  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 95.2  ? 
3  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 89.3  ? 
4  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P B E PGA .   ? A PGA 704 ? 1_555 85.4  ? 
5  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P B E PGA .   ? A PGA 704 ? 1_555 119.0 ? 
6  OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P B E PGA .   ? A PGA 704 ? 1_555 151.3 ? 
7  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 110.9 ? 
8  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 144.1 ? 
9  OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 106.8 ? 
10 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 47.5  ? 
11 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 144.3 ? 
12 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 105.2 ? 
13 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 59.8  ? 
14 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 104.6 ? 
15 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 60.4  ? 
16 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 165.2 ? 
17 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 86.2  ? 
18 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 98.7  ? 
19 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 80.0  ? 
20 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 60.2  ? 
21 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 44.4  ? 
22 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 89.8  ? 
23 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 87.9  ? 
24 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 174.6 ? 
25 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 31.1  ? 
26 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 73.1  ? 
27 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 116.6 ? 
28 O   ? G HOH .   ? A HOH 802 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 76.5  ? 
29 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3P A E PGA .   ? A PGA 704 ? 1_555 158.8 ? 
30 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3B ? F GDP .   ? A GDP 705 ? 1_555 65.7  ? 
31 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3B ? F GDP .   ? A GDP 705 ? 1_555 93.6  ? 
32 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 811 ? 1_555 75.1  ? 
33 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 811 ? 1_555 99.1  ? 
34 O3B ? F GDP .   ? A GDP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 811 ? 1_555 59.7  ? 
35 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 834 ? 1_555 86.7  ? 
36 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 834 ? 1_555 82.9  ? 
37 O3B ? F GDP .   ? A GDP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 834 ? 1_555 74.4  ? 
38 O   ? G HOH .   ? A HOH 811 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 834 ? 1_555 134.0 ? 
39 OE1 ? A GLU 607 ? A GLU 607 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 52.0  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           200 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            200 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    201 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     201 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       5.78 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 7 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA1 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA1 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA1 4 LYS A 155 ? THR A 161 ? LYS A 155 THR A 161 
AA1 5 ILE A 190 ? SER A 195 ? ILE A 190 SER A 195 
AA1 6 GLU A 227 ? PHE A 231 ? GLU A 227 PHE A 231 
AA1 7 LEU A 218 ? LEU A 222 ? LEU A 218 LEU A 222 
AA1 8 THR A 92  ? ILE A 95  ? THR A 92  ILE A 95  
AA1 9 TRP A 116 ? MET A 117 ? TRP A 116 MET A 117 
AA2 1 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA2 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA2 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA2 4 ARG A 175 ? MET A 176 ? ARG A 175 MET A 176 
AA3 1 ARG A 67  ? LYS A 68  ? ARG A 67  LYS A 68  
AA3 2 TRP A 76  ? ALA A 78  ? TRP A 76  ALA A 78  
AA3 3 ILE A 356 ? THR A 358 ? ILE A 356 THR A 358 
AA3 4 ARG A 405 ? PRO A 409 ? ARG A 405 PRO A 409 
AA3 5 GLY A 331 ? VAL A 335 ? GLY A 331 VAL A 335 
AA4 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA4 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA4 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA4 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA4 5 LYS A 277 ? ALA A 283 ? LYS A 277 ALA A 283 
AA4 6 LEU A 266 ? THR A 271 ? LEU A 266 THR A 271 
AA4 7 LYS A 304 ? GLY A 309 ? LYS A 304 GLY A 309 
AA5 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA5 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA5 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA5 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA5 5 LYS A 510 ? VAL A 514 ? LYS A 510 VAL A 514 
AA5 6 VAL A 444 ? GLU A 446 ? VAL A 444 GLU A 446 
AA6 1 VAL A 368 ? TYR A 369 ? VAL A 368 TYR A 369 
AA6 2 ALA A 361 ? THR A 363 ? ALA A 361 THR A 363 
AA6 3 ILE A 383 ? THR A 384 ? ILE A 383 THR A 384 
AA6 4 GLU A 390 ? TRP A 391 ? GLU A 390 TRP A 391 
AA7 1 ARG A 461 ? GLU A 463 ? ARG A 461 GLU A 463 
AA7 2 ILE A 475 ? HIS A 477 ? ILE A 475 HIS A 477 
AA8 1 ALA A 550 ? THR A 553 ? ALA A 550 THR A 553 
AA8 2 GLY A 556 ? PRO A 559 ? GLY A 556 PRO A 559 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 17  ? N GLN A 17  O ILE A 45  ? O ILE A 45  
AA1 2 3 N HIS A 44  ? N HIS A 44  O MET A 139 ? O MET A 139 
AA1 3 4 N ILE A 142 ? N ILE A 142 O GLU A 159 ? O GLU A 159 
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 MET A 117 ? O MET A 117 
AA2 1 2 N GLN A 17  ? N GLN A 17  O ILE A 45  ? O ILE A 45  
AA2 2 3 N HIS A 44  ? N HIS A 44  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 PHE A 433 ? N PHE A 433 O VAL A 514 ? O VAL A 514 
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                   9EIW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NE2 A HIS 452 ? ? O A HOH 804 ? ? 2.12 
2 1 O   A GLU 463 ? ? O A HOH 805 ? ? 2.12 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS A 6   ? ? -132.55 -131.86 
2  1 ASN A 7   ? ? -141.66 56.38   
3  1 ASP A 84  ? ? -117.13 73.33   
4  1 ARG A 129 ? ? -132.88 -59.49  
5  1 PRO A 131 ? ? -48.21  108.83  
6  1 LEU A 153 ? ? -85.07  30.14   
7  1 LYS A 243 ? ? -88.11  -94.49  
8  1 TRP A 260 ? ? -109.34 -156.71 
9  1 ASP A 311 ? ? -156.16 -40.27  
10 1 ALA A 336 ? ? -91.10  -61.27  
11 1 THR A 343 ? ? -90.53  -64.07  
12 1 PRO A 393 ? ? -66.69  1.35    
13 1 ALA A 419 ? ? -144.16 17.17   
14 1 VAL A 444 ? ? -174.82 140.91  
15 1 THR A 465 ? ? -110.83 -153.89 
16 1 ALA A 468 ? ? -99.00  -144.25 
17 1 ASP A 478 ? ? -153.17 64.48   
18 1 PHE A 480 ? ? 59.86   14.38   
19 1 PHE A 530 ? ? 47.22   -121.05 
20 1 LEU A 569 ? ? -126.03 -73.15  
21 1 ASN A 601 ? ? 50.61   -118.58 
# 
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 1.7841   -11.3492 -6.6269 0.6290 ? 0.0542  ? 0.2414  ? 0.3124 ? 0.0392  ? 0.5272 ? 1.8681 ? 0.8066 
? -0.2202 ? 3.5167 ? 0.9335  ? 2.8437 ? -0.0991 ? 0.1566  ? -0.1471 ? -0.3457 ? 0.0260  ? -0.1116 ? 0.1643  ? 0.1887  ? 0.0742  ? 
2 'X-RAY DIFFRACTION' ? refined -5.6154  1.1884   5.9056  0.8226 ? -0.0895 ? 0.3704  ? 0.3579 ? -0.0585 ? 0.7483 ? 1.9409 ? 
-1.5807 ? -0.9517 ? 1.8867 ? 0.9909  ? 1.2236 ? -0.0094 ? -0.0188 ? -0.1473 ? 0.2071  ? -0.1504 ? 0.1924  ? 0.0060  ? -0.0441 ? 
0.1491  ? 
3 'X-RAY DIFFRACTION' ? refined -10.0994 -9.7392  15.0535 1.1739 ? -0.1510 ? 0.4253  ? 0.4217 ? -0.0805 ? 0.6908 ? 1.5313 ? 0.3692 
? -0.1601 ? 0.3029 ? -0.6044 ? 1.5272 ? 0.1204  ? -0.1804 ? -0.1043 ? 1.0788  ? -0.1079 ? 0.4740  ? -0.3653 ? -0.1211 ? -0.0331 ? 
4 'X-RAY DIFFRACTION' ? refined -5.6441  -12.9957 15.8397 0.8490 ? -0.2327 ? 0.2920  ? 0.4440 ? -0.0817 ? 0.4805 ? 1.3190 ? 0.9113 
? -0.9125 ? 4.6065 ? -0.9332 ? 1.4096 ? 0.3339  ? -0.3421 ? -0.1961 ? 0.8407  ? -0.4680 ? 0.2965  ? -0.0179 ? 0.0624  ? 0.1477  ? 
5 'X-RAY DIFFRACTION' ? refined -0.6390  12.1202  17.3432 0.3132 ? 0.0288  ? -0.0815 ? 0.2246 ? 0.0580  ? 0.2394 ? 3.7032 ? 0.0379 
? -0.7241 ? 3.2083 ? 0.2926  ? 3.2497 ? -0.3681 ? -0.4027 ? -0.6451 ? 1.1374  ? 0.1911  ? 0.1204  ? 0.2244  ? 0.1690  ? 0.0067  ? 
6 'X-RAY DIFFRACTION' ? refined -3.1123  17.2934  18.9974 0.9683 ? -0.0152 ? 0.3149  ? 0.3050 ? 0.0244  ? 0.6463 ? 3.3197 ? 0.0112 
? -0.3035 ? 2.4609 ? -0.0327 ? 1.2995 ? -0.0604 ? -0.3447 ? 0.0844  ? 0.4895  ? -0.0450 ? -0.0051 ? -0.1222 ? 0.0899  ? 0.0662  ? 
# 
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 3 through 206 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 207 through 317 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 318 through 378 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 379 through 427 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 428 through 474 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 475 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  
GDP PB     P  N N 88  
GDP O1B    O  N N 89  
GDP O2B    O  N N 90  
GDP O3B    O  N N 91  
GDP O3A    O  N N 92  
GDP PA     P  N N 93  
GDP O1A    O  N N 94  
GDP O2A    O  N N 95  
GDP "O5'"  O  N N 96  
GDP "C5'"  C  N N 97  
GDP "C4'"  C  N R 98  
GDP "O4'"  O  N N 99  
GDP "C3'"  C  N S 100 
GDP "O3'"  O  N N 101 
GDP "C2'"  C  N R 102 
GDP "O2'"  O  N N 103 
GDP "C1'"  C  N R 104 
GDP N9     N  Y N 105 
GDP C8     C  Y N 106 
GDP N7     N  Y N 107 
GDP C5     C  Y N 108 
GDP C6     C  N N 109 
GDP O6     O  N N 110 
GDP N1     N  N N 111 
GDP C2     C  N N 112 
GDP N2     N  N N 113 
GDP N3     N  N N 114 
GDP C4     C  Y N 115 
GDP HOB2   H  N N 116 
GDP HOB3   H  N N 117 
GDP HOA2   H  N N 118 
GDP "H5'"  H  N N 119 
GDP "H5''" H  N N 120 
GDP "H4'"  H  N N 121 
GDP "H3'"  H  N N 122 
GDP "HO3'" H  N N 123 
GDP "H2'"  H  N N 124 
GDP "HO2'" H  N N 125 
GDP "H1'"  H  N N 126 
GDP H8     H  N N 127 
GDP HN1    H  N N 128 
GDP HN21   H  N N 129 
GDP HN22   H  N N 130 
GLN N      N  N N 131 
GLN CA     C  N S 132 
GLN C      C  N N 133 
GLN O      O  N N 134 
GLN CB     C  N N 135 
GLN CG     C  N N 136 
GLN CD     C  N N 137 
GLN OE1    O  N N 138 
GLN NE2    N  N N 139 
GLN OXT    O  N N 140 
GLN H      H  N N 141 
GLN H2     H  N N 142 
GLN HA     H  N N 143 
GLN HB2    H  N N 144 
GLN HB3    H  N N 145 
GLN HG2    H  N N 146 
GLN HG3    H  N N 147 
GLN HE21   H  N N 148 
GLN HE22   H  N N 149 
GLN HXT    H  N N 150 
GLU N      N  N N 151 
GLU CA     C  N S 152 
GLU C      C  N N 153 
GLU O      O  N N 154 
GLU CB     C  N N 155 
GLU CG     C  N N 156 
GLU CD     C  N N 157 
GLU OE1    O  N N 158 
GLU OE2    O  N N 159 
GLU OXT    O  N N 160 
GLU H      H  N N 161 
GLU H2     H  N N 162 
GLU HA     H  N N 163 
GLU HB2    H  N N 164 
GLU HB3    H  N N 165 
GLU HG2    H  N N 166 
GLU HG3    H  N N 167 
GLU HE2    H  N N 168 
GLU HXT    H  N N 169 
GLY N      N  N N 170 
GLY CA     C  N N 171 
GLY C      C  N N 172 
GLY O      O  N N 173 
GLY OXT    O  N N 174 
GLY H      H  N N 175 
GLY H2     H  N N 176 
GLY HA2    H  N N 177 
GLY HA3    H  N N 178 
GLY HXT    H  N N 179 
HIS N      N  N N 180 
HIS CA     C  N S 181 
HIS C      C  N N 182 
HIS O      O  N N 183 
HIS CB     C  N N 184 
HIS CG     C  Y N 185 
HIS ND1    N  Y N 186 
HIS CD2    C  Y N 187 
HIS CE1    C  Y N 188 
HIS NE2    N  Y N 189 
HIS OXT    O  N N 190 
HIS H      H  N N 191 
HIS H2     H  N N 192 
HIS HA     H  N N 193 
HIS HB2    H  N N 194 
HIS HB3    H  N N 195 
HIS HD1    H  N N 196 
HIS HD2    H  N N 197 
HIS HE1    H  N N 198 
HIS HE2    H  N N 199 
HIS HXT    H  N N 200 
HOH O      O  N N 201 
HOH H1     H  N N 202 
HOH H2     H  N N 203 
ILE N      N  N N 204 
ILE CA     C  N S 205 
ILE C      C  N N 206 
ILE O      O  N N 207 
ILE CB     C  N S 208 
ILE CG1    C  N N 209 
ILE CG2    C  N N 210 
ILE CD1    C  N N 211 
ILE OXT    O  N N 212 
ILE H      H  N N 213 
ILE H2     H  N N 214 
ILE HA     H  N N 215 
ILE HB     H  N N 216 
ILE HG12   H  N N 217 
ILE HG13   H  N N 218 
ILE HG21   H  N N 219 
ILE HG22   H  N N 220 
ILE HG23   H  N N 221 
ILE HD11   H  N N 222 
ILE HD12   H  N N 223 
ILE HD13   H  N N 224 
ILE HXT    H  N N 225 
LEU N      N  N N 226 
LEU CA     C  N S 227 
LEU C      C  N N 228 
LEU O      O  N N 229 
LEU CB     C  N N 230 
LEU CG     C  N N 231 
LEU CD1    C  N N 232 
LEU CD2    C  N N 233 
LEU OXT    O  N N 234 
LEU H      H  N N 235 
LEU H2     H  N N 236 
LEU HA     H  N N 237 
LEU HB2    H  N N 238 
LEU HB3    H  N N 239 
LEU HG     H  N N 240 
LEU HD11   H  N N 241 
LEU HD12   H  N N 242 
LEU HD13   H  N N 243 
LEU HD21   H  N N 244 
LEU HD22   H  N N 245 
LEU HD23   H  N N 246 
LEU HXT    H  N N 247 
LYS N      N  N N 248 
LYS CA     C  N S 249 
LYS C      C  N N 250 
LYS O      O  N N 251 
LYS CB     C  N N 252 
LYS CG     C  N N 253 
LYS CD     C  N N 254 
LYS CE     C  N N 255 
LYS NZ     N  N N 256 
LYS OXT    O  N N 257 
LYS H      H  N N 258 
LYS H2     H  N N 259 
LYS HA     H  N N 260 
LYS HB2    H  N N 261 
LYS HB3    H  N N 262 
LYS HG2    H  N N 263 
LYS HG3    H  N N 264 
LYS HD2    H  N N 265 
LYS HD3    H  N N 266 
LYS HE2    H  N N 267 
LYS HE3    H  N N 268 
LYS HZ1    H  N N 269 
LYS HZ2    H  N N 270 
LYS HZ3    H  N N 271 
LYS HXT    H  N N 272 
MET N      N  N N 273 
MET CA     C  N S 274 
MET C      C  N N 275 
MET O      O  N N 276 
MET CB     C  N N 277 
MET CG     C  N N 278 
MET SD     S  N N 279 
MET CE     C  N N 280 
MET OXT    O  N N 281 
MET H      H  N N 282 
MET H2     H  N N 283 
MET HA     H  N N 284 
MET HB2    H  N N 285 
MET HB3    H  N N 286 
MET HG2    H  N N 287 
MET HG3    H  N N 288 
MET HE1    H  N N 289 
MET HE2    H  N N 290 
MET HE3    H  N N 291 
MET HXT    H  N N 292 
MN  MN     MN N N 293 
PGA P      P  N N 294 
PGA O1P    O  N N 295 
PGA O2P    O  N N 296 
PGA O3P    O  N N 297 
PGA O4P    O  N N 298 
PGA C2     C  N N 299 
PGA C1     C  N N 300 
PGA O1     O  N N 301 
PGA O2     O  N N 302 
PGA HOP3   H  N N 303 
PGA HOP4   H  N N 304 
PGA H21    H  N N 305 
PGA H22    H  N N 306 
PGA HO2    H  N N 307 
PHE N      N  N N 308 
PHE CA     C  N S 309 
PHE C      C  N N 310 
PHE O      O  N N 311 
PHE CB     C  N N 312 
PHE CG     C  Y N 313 
PHE CD1    C  Y N 314 
PHE CD2    C  Y N 315 
PHE CE1    C  Y N 316 
PHE CE2    C  Y N 317 
PHE CZ     C  Y N 318 
PHE OXT    O  N N 319 
PHE H      H  N N 320 
PHE H2     H  N N 321 
PHE HA     H  N N 322 
PHE HB2    H  N N 323 
PHE HB3    H  N N 324 
PHE HD1    H  N N 325 
PHE HD2    H  N N 326 
PHE HE1    H  N N 327 
PHE HE2    H  N N 328 
PHE HZ     H  N N 329 
PHE HXT    H  N N 330 
PRO N      N  N N 331 
PRO CA     C  N S 332 
PRO C      C  N N 333 
PRO O      O  N N 334 
PRO CB     C  N N 335 
PRO CG     C  N N 336 
PRO CD     C  N N 337 
PRO OXT    O  N N 338 
PRO H      H  N N 339 
PRO HA     H  N N 340 
PRO HB2    H  N N 341 
PRO HB3    H  N N 342 
PRO HG2    H  N N 343 
PRO HG3    H  N N 344 
PRO HD2    H  N N 345 
PRO HD3    H  N N 346 
PRO HXT    H  N N 347 
SER N      N  N N 348 
SER CA     C  N S 349 
SER C      C  N N 350 
SER O      O  N N 351 
SER CB     C  N N 352 
SER OG     O  N N 353 
SER OXT    O  N N 354 
SER H      H  N N 355 
SER H2     H  N N 356 
SER HA     H  N N 357 
SER HB2    H  N N 358 
SER HB3    H  N N 359 
SER HG     H  N N 360 
SER HXT    H  N N 361 
THR N      N  N N 362 
THR CA     C  N S 363 
THR C      C  N N 364 
THR O      O  N N 365 
THR CB     C  N R 366 
THR OG1    O  N N 367 
THR CG2    C  N N 368 
THR OXT    O  N N 369 
THR H      H  N N 370 
THR H2     H  N N 371 
THR HA     H  N N 372 
THR HB     H  N N 373 
THR HG1    H  N N 374 
THR HG21   H  N N 375 
THR HG22   H  N N 376 
THR HG23   H  N N 377 
THR HXT    H  N N 378 
TRP N      N  N N 379 
TRP CA     C  N S 380 
TRP C      C  N N 381 
TRP O      O  N N 382 
TRP CB     C  N N 383 
TRP CG     C  Y N 384 
TRP CD1    C  Y N 385 
TRP CD2    C  Y N 386 
TRP NE1    N  Y N 387 
TRP CE2    C  Y N 388 
TRP CE3    C  Y N 389 
TRP CZ2    C  Y N 390 
TRP CZ3    C  Y N 391 
TRP CH2    C  Y N 392 
TRP OXT    O  N N 393 
TRP H      H  N N 394 
TRP H2     H  N N 395 
TRP HA     H  N N 396 
TRP HB2    H  N N 397 
TRP HB3    H  N N 398 
TRP HD1    H  N N 399 
TRP HE1    H  N N 400 
TRP HE3    H  N N 401 
TRP HZ2    H  N N 402 
TRP HZ3    H  N N 403 
TRP HH2    H  N N 404 
TRP HXT    H  N N 405 
TYR N      N  N N 406 
TYR CA     C  N S 407 
TYR C      C  N N 408 
TYR O      O  N N 409 
TYR CB     C  N N 410 
TYR CG     C  Y N 411 
TYR CD1    C  Y N 412 
TYR CD2    C  Y N 413 
TYR CE1    C  Y N 414 
TYR CE2    C  Y N 415 
TYR CZ     C  Y N 416 
TYR OH     O  N N 417 
TYR OXT    O  N N 418 
TYR H      H  N N 419 
TYR H2     H  N N 420 
TYR HA     H  N N 421 
TYR HB2    H  N N 422 
TYR HB3    H  N N 423 
TYR HD1    H  N N 424 
TYR HD2    H  N N 425 
TYR HE1    H  N N 426 
TYR HE2    H  N N 427 
TYR HH     H  N N 428 
TYR HXT    H  N N 429 
VAL N      N  N N 430 
VAL CA     C  N S 431 
VAL C      C  N N 432 
VAL O      O  N N 433 
VAL CB     C  N N 434 
VAL CG1    C  N N 435 
VAL CG2    C  N N 436 
VAL OXT    O  N N 437 
VAL H      H  N N 438 
VAL H2     H  N N 439 
VAL HA     H  N N 440 
VAL HB     H  N N 441 
VAL HG11   H  N N 442 
VAL HG12   H  N N 443 
VAL HG13   H  N N 444 
VAL HG21   H  N N 445 
VAL HG22   H  N N 446 
VAL HG23   H  N N 447 
VAL HXT    H  N N 448 
# 
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  
GDP PB    O1B    doub N N 83  
GDP PB    O2B    sing N N 84  
GDP PB    O3B    sing N N 85  
GDP PB    O3A    sing N N 86  
GDP O2B   HOB2   sing N N 87  
GDP O3B   HOB3   sing N N 88  
GDP O3A   PA     sing N N 89  
GDP PA    O1A    doub N N 90  
GDP PA    O2A    sing N N 91  
GDP PA    "O5'"  sing N N 92  
GDP O2A   HOA2   sing N N 93  
GDP "O5'" "C5'"  sing N N 94  
GDP "C5'" "C4'"  sing N N 95  
GDP "C5'" "H5'"  sing N N 96  
GDP "C5'" "H5''" sing N N 97  
GDP "C4'" "O4'"  sing N N 98  
GDP "C4'" "C3'"  sing N N 99  
GDP "C4'" "H4'"  sing N N 100 
GDP "O4'" "C1'"  sing N N 101 
GDP "C3'" "O3'"  sing N N 102 
GDP "C3'" "C2'"  sing N N 103 
GDP "C3'" "H3'"  sing N N 104 
GDP "O3'" "HO3'" sing N N 105 
GDP "C2'" "O2'"  sing N N 106 
GDP "C2'" "C1'"  sing N N 107 
GDP "C2'" "H2'"  sing N N 108 
GDP "O2'" "HO2'" sing N N 109 
GDP "C1'" N9     sing N N 110 
GDP "C1'" "H1'"  sing N N 111 
GDP N9    C8     sing Y N 112 
GDP N9    C4     sing Y N 113 
GDP C8    N7     doub Y N 114 
GDP C8    H8     sing N N 115 
GDP N7    C5     sing Y N 116 
GDP C5    C6     sing N N 117 
GDP C5    C4     doub Y N 118 
GDP C6    O6     doub N N 119 
GDP C6    N1     sing N N 120 
GDP N1    C2     sing N N 121 
GDP N1    HN1    sing N N 122 
GDP C2    N2     sing N N 123 
GDP C2    N3     doub N N 124 
GDP N2    HN21   sing N N 125 
GDP N2    HN22   sing N N 126 
GDP N3    C4     sing N N 127 
GLN N     CA     sing N N 128 
GLN N     H      sing N N 129 
GLN N     H2     sing N N 130 
GLN CA    C      sing N N 131 
GLN CA    CB     sing N N 132 
GLN CA    HA     sing N N 133 
GLN C     O      doub N N 134 
GLN C     OXT    sing N N 135 
GLN CB    CG     sing N N 136 
GLN CB    HB2    sing N N 137 
GLN CB    HB3    sing N N 138 
GLN CG    CD     sing N N 139 
GLN CG    HG2    sing N N 140 
GLN CG    HG3    sing N N 141 
GLN CD    OE1    doub N N 142 
GLN CD    NE2    sing N N 143 
GLN NE2   HE21   sing N N 144 
GLN NE2   HE22   sing N N 145 
GLN OXT   HXT    sing N N 146 
GLU N     CA     sing N N 147 
GLU N     H      sing N N 148 
GLU N     H2     sing N N 149 
GLU CA    C      sing N N 150 
GLU CA    CB     sing N N 151 
GLU CA    HA     sing N N 152 
GLU C     O      doub N N 153 
GLU C     OXT    sing N N 154 
GLU CB    CG     sing N N 155 
GLU CB    HB2    sing N N 156 
GLU CB    HB3    sing N N 157 
GLU CG    CD     sing N N 158 
GLU CG    HG2    sing N N 159 
GLU CG    HG3    sing N N 160 
GLU CD    OE1    doub N N 161 
GLU CD    OE2    sing N N 162 
GLU OE2   HE2    sing N N 163 
GLU OXT   HXT    sing N N 164 
GLY N     CA     sing N N 165 
GLY N     H      sing N N 166 
GLY N     H2     sing N N 167 
GLY CA    C      sing N N 168 
GLY CA    HA2    sing N N 169 
GLY CA    HA3    sing N N 170 
GLY C     O      doub N N 171 
GLY C     OXT    sing N N 172 
GLY OXT   HXT    sing N N 173 
HIS N     CA     sing N N 174 
HIS N     H      sing N N 175 
HIS N     H2     sing N N 176 
HIS CA    C      sing N N 177 
HIS CA    CB     sing N N 178 
HIS CA    HA     sing N N 179 
HIS C     O      doub N N 180 
HIS C     OXT    sing N N 181 
HIS CB    CG     sing N N 182 
HIS CB    HB2    sing N N 183 
HIS CB    HB3    sing N N 184 
HIS CG    ND1    sing Y N 185 
HIS CG    CD2    doub Y N 186 
HIS ND1   CE1    doub Y N 187 
HIS ND1   HD1    sing N N 188 
HIS CD2   NE2    sing Y N 189 
HIS CD2   HD2    sing N N 190 
HIS CE1   NE2    sing Y N 191 
HIS CE1   HE1    sing N N 192 
HIS NE2   HE2    sing N N 193 
HIS OXT   HXT    sing N N 194 
HOH O     H1     sing N N 195 
HOH O     H2     sing N N 196 
ILE N     CA     sing N N 197 
ILE N     H      sing N N 198 
ILE N     H2     sing N N 199 
ILE CA    C      sing N N 200 
ILE CA    CB     sing N N 201 
ILE CA    HA     sing N N 202 
ILE C     O      doub N N 203 
ILE C     OXT    sing N N 204 
ILE CB    CG1    sing N N 205 
ILE CB    CG2    sing N N 206 
ILE CB    HB     sing N N 207 
ILE CG1   CD1    sing N N 208 
ILE CG1   HG12   sing N N 209 
ILE CG1   HG13   sing N N 210 
ILE CG2   HG21   sing N N 211 
ILE CG2   HG22   sing N N 212 
ILE CG2   HG23   sing N N 213 
ILE CD1   HD11   sing N N 214 
ILE CD1   HD12   sing N N 215 
ILE CD1   HD13   sing N N 216 
ILE OXT   HXT    sing N N 217 
LEU N     CA     sing N N 218 
LEU N     H      sing N N 219 
LEU N     H2     sing N N 220 
LEU CA    C      sing N N 221 
LEU CA    CB     sing N N 222 
LEU CA    HA     sing N N 223 
LEU C     O      doub N N 224 
LEU C     OXT    sing N N 225 
LEU CB    CG     sing N N 226 
LEU CB    HB2    sing N N 227 
LEU CB    HB3    sing N N 228 
LEU CG    CD1    sing N N 229 
LEU CG    CD2    sing N N 230 
LEU CG    HG     sing N N 231 
LEU CD1   HD11   sing N N 232 
LEU CD1   HD12   sing N N 233 
LEU CD1   HD13   sing N N 234 
LEU CD2   HD21   sing N N 235 
LEU CD2   HD22   sing N N 236 
LEU CD2   HD23   sing N N 237 
LEU OXT   HXT    sing N N 238 
LYS N     CA     sing N N 239 
LYS N     H      sing N N 240 
LYS N     H2     sing N N 241 
LYS CA    C      sing N N 242 
LYS CA    CB     sing N N 243 
LYS CA    HA     sing N N 244 
LYS C     O      doub N N 245 
LYS C     OXT    sing N N 246 
LYS CB    CG     sing N N 247 
LYS CB    HB2    sing N N 248 
LYS CB    HB3    sing N N 249 
LYS CG    CD     sing N N 250 
LYS CG    HG2    sing N N 251 
LYS CG    HG3    sing N N 252 
LYS CD    CE     sing N N 253 
LYS CD    HD2    sing N N 254 
LYS CD    HD3    sing N N 255 
LYS CE    NZ     sing N N 256 
LYS CE    HE2    sing N N 257 
LYS CE    HE3    sing N N 258 
LYS NZ    HZ1    sing N N 259 
LYS NZ    HZ2    sing N N 260 
LYS NZ    HZ3    sing N N 261 
LYS OXT   HXT    sing N N 262 
MET N     CA     sing N N 263 
MET N     H      sing N N 264 
MET N     H2     sing N N 265 
MET CA    C      sing N N 266 
MET CA    CB     sing N N 267 
MET CA    HA     sing N N 268 
MET C     O      doub N N 269 
MET C     OXT    sing N N 270 
MET CB    CG     sing N N 271 
MET CB    HB2    sing N N 272 
MET CB    HB3    sing N N 273 
MET CG    SD     sing N N 274 
MET CG    HG2    sing N N 275 
MET CG    HG3    sing N N 276 
MET SD    CE     sing N N 277 
MET CE    HE1    sing N N 278 
MET CE    HE2    sing N N 279 
MET CE    HE3    sing N N 280 
MET OXT   HXT    sing N N 281 
PGA P     O1P    sing N N 282 
PGA P     O2P    doub N N 283 
PGA P     O3P    sing N N 284 
PGA P     O4P    sing N N 285 
PGA O1P   C2     sing N N 286 
PGA O3P   HOP3   sing N N 287 
PGA O4P   HOP4   sing N N 288 
PGA C2    C1     sing N N 289 
PGA C2    H21    sing N N 290 
PGA C2    H22    sing N N 291 
PGA C1    O1     doub N N 292 
PGA C1    O2     sing N N 293 
PGA O2    HO2    sing N N 294 
PHE N     CA     sing N N 295 
PHE N     H      sing N N 296 
PHE N     H2     sing N N 297 
PHE CA    C      sing N N 298 
PHE CA    CB     sing N N 299 
PHE CA    HA     sing N N 300 
PHE C     O      doub N N 301 
PHE C     OXT    sing N N 302 
PHE CB    CG     sing N N 303 
PHE CB    HB2    sing N N 304 
PHE CB    HB3    sing N N 305 
PHE CG    CD1    doub Y N 306 
PHE CG    CD2    sing Y N 307 
PHE CD1   CE1    sing Y N 308 
PHE CD1   HD1    sing N N 309 
PHE CD2   CE2    doub Y N 310 
PHE CD2   HD2    sing N N 311 
PHE CE1   CZ     doub Y N 312 
PHE CE1   HE1    sing N N 313 
PHE CE2   CZ     sing Y N 314 
PHE CE2   HE2    sing N N 315 
PHE CZ    HZ     sing N N 316 
PHE OXT   HXT    sing N N 317 
PRO N     CA     sing N N 318 
PRO N     CD     sing N N 319 
PRO N     H      sing N N 320 
PRO CA    C      sing N N 321 
PRO CA    CB     sing N N 322 
PRO CA    HA     sing N N 323 
PRO C     O      doub N N 324 
PRO C     OXT    sing N N 325 
PRO CB    CG     sing N N 326 
PRO CB    HB2    sing N N 327 
PRO CB    HB3    sing N N 328 
PRO CG    CD     sing N N 329 
PRO CG    HG2    sing N N 330 
PRO CG    HG3    sing N N 331 
PRO CD    HD2    sing N N 332 
PRO CD    HD3    sing N N 333 
PRO OXT   HXT    sing N N 334 
SER N     CA     sing N N 335 
SER N     H      sing N N 336 
SER N     H2     sing N N 337 
SER CA    C      sing N N 338 
SER CA    CB     sing N N 339 
SER CA    HA     sing N N 340 
SER C     O      doub N N 341 
SER C     OXT    sing N N 342 
SER CB    OG     sing N N 343 
SER CB    HB2    sing N N 344 
SER CB    HB3    sing N N 345 
SER OG    HG     sing N N 346 
SER OXT   HXT    sing N N 347 
THR N     CA     sing N N 348 
THR N     H      sing N N 349 
THR N     H2     sing N N 350 
THR CA    C      sing N N 351 
THR CA    CB     sing N N 352 
THR CA    HA     sing N N 353 
THR C     O      doub N N 354 
THR C     OXT    sing N N 355 
THR CB    OG1    sing N N 356 
THR CB    CG2    sing N N 357 
THR CB    HB     sing N N 358 
THR OG1   HG1    sing N N 359 
THR CG2   HG21   sing N N 360 
THR CG2   HG22   sing N N 361 
THR CG2   HG23   sing N N 362 
THR OXT   HXT    sing N N 363 
TRP N     CA     sing N N 364 
TRP N     H      sing N N 365 
TRP N     H2     sing N N 366 
TRP CA    C      sing N N 367 
TRP CA    CB     sing N N 368 
TRP CA    HA     sing N N 369 
TRP C     O      doub N N 370 
TRP C     OXT    sing N N 371 
TRP CB    CG     sing N N 372 
TRP CB    HB2    sing N N 373 
TRP CB    HB3    sing N N 374 
TRP CG    CD1    doub Y N 375 
TRP CG    CD2    sing Y N 376 
TRP CD1   NE1    sing Y N 377 
TRP CD1   HD1    sing N N 378 
TRP CD2   CE2    doub Y N 379 
TRP CD2   CE3    sing Y N 380 
TRP NE1   CE2    sing Y N 381 
TRP NE1   HE1    sing N N 382 
TRP CE2   CZ2    sing Y N 383 
TRP CE3   CZ3    doub Y N 384 
TRP CE3   HE3    sing N N 385 
TRP CZ2   CH2    doub Y N 386 
TRP CZ2   HZ2    sing N N 387 
TRP CZ3   CH2    sing Y N 388 
TRP CZ3   HZ3    sing N N 389 
TRP CH2   HH2    sing N N 390 
TRP OXT   HXT    sing N N 391 
TYR N     CA     sing N N 392 
TYR N     H      sing N N 393 
TYR N     H2     sing N N 394 
TYR CA    C      sing N N 395 
TYR CA    CB     sing N N 396 
TYR CA    HA     sing N N 397 
TYR C     O      doub N N 398 
TYR C     OXT    sing N N 399 
TYR CB    CG     sing N N 400 
TYR CB    HB2    sing N N 401 
TYR CB    HB3    sing N N 402 
TYR CG    CD1    doub Y N 403 
TYR CG    CD2    sing Y N 404 
TYR CD1   CE1    sing Y N 405 
TYR CD1   HD1    sing N N 406 
TYR CD2   CE2    doub Y N 407 
TYR CD2   HD2    sing N N 408 
TYR CE1   CZ     doub Y N 409 
TYR CE1   HE1    sing N N 410 
TYR CE2   CZ     sing Y N 411 
TYR CE2   HE2    sing N N 412 
TYR CZ    OH     sing N N 413 
TYR OH    HH     sing N N 414 
TYR OXT   HXT    sing N N 415 
VAL N     CA     sing N N 416 
VAL N     H      sing N N 417 
VAL N     H2     sing N N 418 
VAL CA    C      sing N N 419 
VAL CA    CB     sing N N 420 
VAL CA    HA     sing N N 421 
VAL C     O      doub N N 422 
VAL C     OXT    sing N N 423 
VAL CB    CG1    sing N N 424 
VAL CB    CG2    sing N N 425 
VAL CB    HB     sing N N 426 
VAL CG1   HG11   sing N N 427 
VAL CG1   HG12   sing N N 428 
VAL CG1   HG13   sing N N 429 
VAL CG2   HG21   sing N N 430 
VAL CG2   HG22   sing N N 431 
VAL CG2   HG23   sing N N 432 
VAL OXT   HXT    sing N N 433 
# 
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                    9EIW 
_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]   0.022159 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008678 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008320 
_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]   0.017736 
_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  
H  
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   ? 2.710   -13.221 -32.425 1.00 153.33 ? 3   PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? 3.433   -14.150 -33.299 1.00 141.86 ? 3   PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? 4.740   -14.631 -32.679 1.00 140.35 ? 3   PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? 5.277   -13.973 -31.788 1.00 141.30 ? 3   PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? 3.701   -13.310 -34.546 1.00 144.75 ? 3   PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? 3.830   -11.922 -34.019 1.00 143.26 ? 3   PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? 2.855   -11.823 -32.870 1.00 148.48 ? 3   PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? 5.243   -15.769 -33.150 1.00 112.39 ? 4   GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? 6.506   -16.301 -32.657 1.00 102.24 ? 4   GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? 7.090   -17.225 -33.713 1.00 93.03  ? 4   GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? 6.399   -17.657 -34.639 1.00 95.81  ? 4   GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? 6.329   -17.039 -31.324 1.00 101.45 ? 4   GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? 5.357   -18.211 -31.370 1.00 102.19 ? 4   GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? 5.170   -18.865 -30.012 1.00 107.43 ? 4   GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? 5.839   -18.511 -29.040 1.00 107.88 ? 4   GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? 4.254   -19.824 -29.939 1.00 98.95  ? 4   GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? 8.384   -17.514 -33.565 1.00 94.27  ? 5   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? 9.078   -18.431 -34.458 1.00 95.28  ? 5   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? 9.209   -19.835 -33.889 1.00 89.96  ? 5   LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? 9.467   -20.775 -34.650 1.00 92.89  ? 5   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? 10.475  -17.894 -34.795 1.00 92.75  ? 5   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? 10.513  -16.657 -35.690 1.00 94.80  ? 5   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? 11.945  -16.190 -35.897 1.00 96.95  ? 5   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? 9.840   -16.951 -37.021 1.00 98.05  ? 5   LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? 9.038   -19.999 -32.579 1.00 94.69  ? 6   HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? 9.112   -21.311 -31.952 1.00 108.68 ? 6   HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? 7.928   -21.515 -31.015 1.00 118.81 ? 6   HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? 6.781   -21.259 -31.395 1.00 116.27 ? 6   HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? 10.440  -21.470 -31.208 1.00 103.55 ? 6   HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? 11.643  -21.274 -32.078 1.00 98.73  ? 6   HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? 12.224  -20.040 -32.278 1.00 92.76  ? 6   HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? 12.366  -22.154 -32.813 1.00 92.73  ? 6   HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? 13.257  -20.169 -33.091 1.00 93.18  ? 6   HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? 13.364  -21.441 -33.432 1.00 95.17  ? 6   HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? 8.191   -21.973 -29.791 1.00 162.47 ? 7   ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? 7.145   -22.198 -28.799 1.00 160.88 ? 7   ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? 7.658   -21.786 -27.418 1.00 157.67 ? 7   ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? 7.665   -22.558 -26.464 1.00 162.34 ? 7   ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? 6.683   -23.654 -28.808 1.00 162.16 ? 7   ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? 5.833   -23.989 -30.018 1.00 169.30 ? 7   ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? 4.604   -23.960 -29.954 1.00 167.57 ? 7   ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? 6.485   -24.310 -31.130 1.00 166.60 ? 7   ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? 8.095   -20.535 -27.305 1.00 122.42 ? 8   GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? 8.643   -20.052 -26.054 1.00 114.00 ? 8   GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? 7.959   -18.813 -25.515 1.00 110.17 ? 8   GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? 8.413   -18.236 -24.523 1.00 113.78 ? 8   GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? 6.862   -18.394 -26.150 1.00 111.67 ? 9   LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? 6.168   -17.175 -25.760 1.00 104.89 ? 9   LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? 4.700   -17.372 -25.406 1.00 96.71  ? 9   LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? 4.132   -16.509 -24.729 1.00 92.37  ? 9   LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? 6.266   -16.122 -26.876 1.00 106.38 ? 9   LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? 7.681   -15.704 -27.281 1.00 103.95 ? 9   LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? 7.647   -14.755 -28.472 1.00 95.79  ? 9   LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? 8.417   -15.073 -26.106 1.00 96.97  ? 9   LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? 4.074   -18.466 -25.836 1.00 98.15  ? 10  ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? 2.663   -18.735 -25.552 1.00 89.24  ? 10  ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? 2.592   -19.700 -24.373 1.00 75.49  ? 10  ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? 2.857   -20.897 -24.518 1.00 76.52  ? 10  ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? 1.960   -19.298 -26.783 1.00 89.86  ? 10  ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? 0.458   -19.419 -26.596 1.00 78.85  ? 10  ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? 0.010   -19.619 -25.449 1.00 79.62  ? 10  ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? -0.279  -19.312 -27.600 1.00 80.44  ? 10  ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? 2.227   -19.176 -23.203 1.00 70.60  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 2.123   -19.962 -21.980 1.00 72.53  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 0.747   -20.596 -21.793 1.00 65.66  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 0.405   -20.987 -20.671 1.00 68.55  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 2.467   -19.095 -20.766 1.00 66.43  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 3.928   -19.097 -20.412 1.00 71.75  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 4.856   -18.473 -21.230 1.00 76.96  ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 4.372   -19.717 -19.255 1.00 71.61  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 6.202   -18.473 -20.904 1.00 74.78  ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 5.716   -19.721 -18.922 1.00 70.20  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 6.632   -19.098 -19.748 1.00 72.43  ? 11  PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? -0.044  -20.711 -22.863 1.00 61.30  ? 12  SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? -1.370  -21.310 -22.739 1.00 65.07  ? 12  SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? -1.291  -22.726 -22.182 1.00 71.88  ? 12  SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? -2.115  -23.119 -21.347 1.00 73.14  ? 12  SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? -2.076  -21.311 -24.095 1.00 70.10  ? 12  SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? -2.399  -19.998 -24.512 1.00 76.90  ? 12  SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? -0.304  -23.507 -22.627 1.00 71.67  ? 13  ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? -0.190  -24.898 -22.204 1.00 72.03  ? 13  ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? 0.123   -25.047 -20.721 1.00 67.83  ? 13  ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? 0.088   -26.174 -20.214 1.00 64.46  ? 13  ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? 0.881   -25.614 -23.030 1.00 65.78  ? 13  ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? 0.426   -23.955 -20.019 1.00 62.91  ? 14  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? 0.697   -23.995 -18.588 1.00 63.63  ? 14  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? -0.465  -23.472 -17.752 1.00 60.59  ? 14  LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? -0.338  -23.376 -16.526 1.00 58.77  ? 14  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? 1.964   -23.201 -18.265 1.00 67.37  ? 14  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? 3.251   -23.837 -18.766 1.00 66.79  ? 14  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? 4.468   -23.092 -18.226 1.00 77.75  ? 14  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? 5.777   -23.739 -18.663 1.00 86.86  ? 14  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? 6.027   -23.593 -20.126 1.00 102.61 ? 14  LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? -1.590  -23.139 -18.378 1.00 62.18  ? 15  VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? -2.737  -22.572 -17.676 1.00 62.88  ? 15  VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? -3.569  -23.720 -17.116 1.00 61.70  ? 15  VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? -4.216  -24.456 -17.867 1.00 61.56  ? 15  VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? -3.573  -21.678 -18.599 1.00 59.56  ? 15  VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? -4.749  -21.094 -17.840 1.00 57.53  ? 15  VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? -2.714  -20.569 -19.196 1.00 54.84  ? 15  VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? -3.562  -23.873 -15.787 1.00 56.85  ? 16  ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? -4.346  -24.925 -15.144 1.00 58.90  ? 16  ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? -5.736  -24.460 -14.734 1.00 54.80  ? 16  ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? -6.566  -25.294 -14.341 1.00 63.03  ? 16  ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? -3.607  -25.497 -13.918 1.00 58.97  ? 16  ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? -3.370  -24.409 -12.872 1.00 56.56  ? 16  ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? -2.289  -26.129 -14.338 1.00 56.31  ? 16  ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? -2.576  -24.888 -11.676 1.00 59.47  ? 16  ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? -6.020  -23.162 -14.808 1.00 59.67  ? 17  GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? -7.371  -22.657 -14.564 1.00 58.73  ? 17  GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? -7.495  -21.284 -15.199 1.00 58.57  ? 17  GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? -6.764  -20.361 -14.824 1.00 58.54  ? 17  GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? -7.687  -22.583 -13.072 1.00 55.18  ? 17  GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? -9.008  -21.881 -12.786 1.00 53.21  ? 17  GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? -9.409  -21.935 -11.326 1.00 58.12  ? 17  GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? -9.341  -22.985 -10.686 1.00 63.02  ? 17  GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? -9.835  -20.797 -10.791 1.00 53.82  ? 17  GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? -8.419  -21.146 -16.137 1.00 56.69  ? 18  GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? -8.643  -19.902 -16.840 1.00 56.48  ? 18  GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? -8.194  -19.989 -18.287 1.00 63.68  ? 18  GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? -7.797  -21.043 -18.791 1.00 72.59  ? 18  GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? -8.262  -18.842 -18.958 1.00 68.56  ? 19  SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? -7.898  -18.743 -20.365 1.00 64.48  ? 19  SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? -7.229  -17.400 -20.603 1.00 72.20  ? 19  SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? -7.832  -16.352 -20.352 1.00 74.80  ? 19  SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? -9.128  -18.895 -21.264 1.00 68.37  ? 19  SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? -8.768  -18.832 -22.632 1.00 81.14  ? 19  SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? -5.981  -17.431 -21.077 1.00 71.58  ? 20  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? -5.324  -16.192 -21.475 1.00 74.32  ? 20  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? -6.123  -15.468 -22.548 1.00 79.00  ? 20  LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? -6.073  -14.235 -22.636 1.00 78.02  ? 20  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? -3.904  -16.475 -21.967 1.00 66.15  ? 20  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? -2.916  -17.056 -20.952 1.00 66.12  ? 20  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? -1.537  -17.200 -21.572 1.00 72.42  ? 20  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? -2.850  -16.200 -19.698 1.00 58.99  ? 20  LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? -6.870  -16.214 -23.367 1.00 80.10  ? 21  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? -7.703  -15.590 -24.390 1.00 88.31  ? 21  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? -8.745  -14.669 -23.768 1.00 88.00  ? 21  ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? -9.011  -13.579 -24.287 1.00 97.23  ? 21  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? -8.382  -16.664 -25.241 1.00 92.82  ? 21  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? -7.388  -17.556 -25.961 1.00 101.00 ? 21  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? -6.290  -17.069 -26.302 1.00 97.68  ? 21  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? -7.706  -18.744 -26.187 1.00 103.74 ? 21  ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? -9.344  -15.089 -22.657 1.00 81.53  ? 22  SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? -10.371 -14.301 -21.988 1.00 79.81  ? 22  SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? -9.807  -13.120 -21.211 1.00 78.28  ? 22  SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? -10.585 -12.351 -20.636 1.00 85.50  ? 22  SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? -11.182 -15.194 -21.047 1.00 78.88  ? 22  SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? -10.347 -15.782 -20.065 1.00 82.53  ? 22  SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? -8.489  -12.954 -21.175 1.00 74.16  ? 23  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? -7.923  -11.831 -20.443 1.00 75.08  ? 23  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? -7.956  -10.567 -21.299 1.00 78.10  ? 23  LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? -7.748  -10.633 -22.514 1.00 80.79  ? 23  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? -6.486  -12.126 -20.024 1.00 69.60  ? 23  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? -6.284  -13.123 -18.885 1.00 73.21  ? 23  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? -4.802  -13.280 -18.580 1.00 70.68  ? 23  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? -7.049  -12.682 -17.646 1.00 65.20  ? 23  LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? -8.223  -9.408  -20.694 1.00 73.12  ? 24  PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? -8.099  -8.146  -21.435 1.00 78.24  ? 24  PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? -6.731  -8.015  -22.083 1.00 81.82  ? 24  PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? -5.771  -8.662  -21.652 1.00 83.39  ? 24  PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? -8.320  -7.082  -20.353 1.00 76.83  ? 24  PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? -9.158  -7.766  -19.329 1.00 75.76  ? 24  PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? -8.707  -9.201  -19.319 1.00 75.60  ? 24  PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? -6.636  -7.183  -23.119 1.00 102.30 ? 25  GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? -5.396  -7.009  -23.866 1.00 101.27 ? 25  GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? -4.198  -6.830  -22.941 1.00 96.71  ? 25  GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? -3.347  -7.720  -22.837 1.00 94.06  ? 25  GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? -5.514  -5.811  -24.810 1.00 108.58 ? 25  GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? -4.316  -5.616  -25.725 1.00 110.22 ? 25  GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? -4.157  -6.747  -26.721 1.00 125.96 ? 25  GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? -4.956  -7.684  -26.748 1.00 126.21 ? 25  GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? -3.123  -6.665  -27.550 1.00 132.01 ? 25  GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? -4.128  -5.686  -22.258 1.00 84.53  ? 26  GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? -2.967  -5.388  -21.428 1.00 80.39  ? 26  GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? -2.818  -6.353  -20.259 1.00 74.18  ? 26  GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? -1.706  -6.516  -19.744 1.00 71.08  ? 26  GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? -3.048  -3.949  -20.918 1.00 83.83  ? 26  GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? -3.006  -2.909  -22.028 1.00 92.72  ? 26  GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? -1.774  -3.042  -22.903 1.00 89.46  ? 26  GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? -0.726  -3.489  -22.391 1.00 84.62  ? 26  GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? -1.853  -2.709  -24.105 1.00 92.15  ? 26  GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? -3.901  -6.996  -19.825 1.00 73.34  ? 27  VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? -3.789  -7.969  -18.744 1.00 71.41  ? 27  VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? -2.977  -9.176  -19.201 1.00 67.93  ? 27  VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? -2.055  -9.624  -18.508 1.00 56.51  ? 27  VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? -5.183  -8.381  -18.239 1.00 70.59  ? 27  VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? -5.056  -9.410  -17.127 1.00 62.43  ? 27  VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? -5.952  -7.162  -17.755 1.00 63.53  ? 27  VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? -3.301  -9.717  -20.378 1.00 67.20  ? 28  ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? -2.549  -10.860 -20.886 1.00 69.63  ? 28  ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? -1.068  -10.528 -21.036 1.00 65.28  ? 28  ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? -0.205  -11.332 -20.662 1.00 65.14  ? 28  ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? -3.124  -11.331 -22.221 1.00 68.70  ? 28  ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? -2.272  -12.402 -22.885 1.00 70.68  ? 28  ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? -3.051  -13.206 -23.912 1.00 80.48  ? 28  ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? -2.277  -14.343 -24.398 1.00 76.51  ? 28  ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? -2.784  -15.352 -25.094 1.00 79.18  ? 28  ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? -4.069  -15.400 -25.405 1.00 82.77  ? 28  ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? -1.982  -16.340 -25.481 1.00 74.59  ? 28  ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? -0.753  -9.351  -21.582 1.00 63.73  ? 29  LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? 0.647   -8.972  -21.756 1.00 66.70  ? 29  LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? 1.385   -8.950  -20.422 1.00 61.42  ? 29  LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? 2.525   -9.422  -20.327 1.00 58.71  ? 29  LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? 0.745   -7.608  -22.442 1.00 73.59  ? 29  LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? 0.352   -7.599  -23.913 1.00 74.01  ? 29  LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? 0.418   -6.183  -24.477 1.00 85.40  ? 29  LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? 0.064   -6.133  -25.959 1.00 100.20 ? 29  LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? 1.165   -6.629  -26.835 1.00 103.23 ? 29  LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? 0.753   -8.402  -19.382 1.00 61.45  ? 30  PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? 1.387   -8.345  -18.068 1.00 56.30  ? 30  PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? 1.627   -9.742  -17.508 1.00 55.90  ? 30  PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? 2.646   -9.990  -16.853 1.00 55.32  ? 30  PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? 0.522   -7.514  -17.116 1.00 56.58  ? 30  PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? 1.015   -7.492  -15.696 1.00 48.71  ? 30  PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? 2.295   -7.058  -15.397 1.00 53.94  ? 30  PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? 0.186   -7.881  -14.658 1.00 50.59  ? 30  PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? 2.744   -7.032  -14.089 1.00 50.50  ? 30  PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? 0.629   -7.854  -13.348 1.00 50.78  ? 30  PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? 1.911   -7.428  -13.064 1.00 53.19  ? 30  PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? 0.703   -10.669 -17.764 1.00 56.90  ? 31  VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? 0.849   -12.035 -17.261 1.00 58.02  ? 31  VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? 1.959   -12.762 -18.011 1.00 57.69  ? 31  VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? 2.921   -13.257 -17.410 1.00 54.75  ? 31  VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? -0.486  -12.795 -17.362 1.00 59.97  ? 31  VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? -0.298  -14.260 -16.981 1.00 55.66  ? 31  VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? -1.541  -12.140 -16.480 1.00 57.73  ? 31  VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? 1.842   -12.840 -19.339 1.00 62.54  ? 32  GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? 2.808   -13.612 -20.115 1.00 62.35  ? 32  GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? 4.205   -13.013 -20.038 1.00 62.46  ? 32  GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? 5.197   -13.748 -20.110 1.00 61.21  ? 32  GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? 2.351   -13.721 -21.571 1.00 69.70  ? 32  GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? 1.310   -14.806 -21.803 1.00 75.99  ? 32  GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? 0.960   -14.984 -23.267 1.00 75.11  ? 32  GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? 1.094   -14.009 -24.037 1.00 82.89  ? 32  GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? 0.554   -16.101 -23.648 1.00 69.95  ? 32  GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? 4.307   -11.692 -19.887 1.00 59.73  ? 33  GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? 5.619   -11.072 -19.788 1.00 53.80  ? 33  GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? 6.391   -11.543 -18.571 1.00 57.62  ? 33  GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? 7.572   -11.887 -18.661 1.00 56.68  ? 33  GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? 5.732   -11.564 -17.411 1.00 52.23  ? 34  ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? 6.389   -12.024 -16.194 1.00 53.75  ? 34  ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? 6.445   -13.543 -16.114 1.00 58.03  ? 34  ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? 7.374   -14.091 -15.510 1.00 58.85  ? 34  ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? 5.681   -11.449 -14.971 1.00 50.67  ? 34  ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? 5.782   -9.945  -14.907 1.00 54.76  ? 34  ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? 6.773   -9.400  -14.420 1.00 56.33  ? 34  ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? 4.762   -9.260  -15.413 1.00 54.67  ? 34  ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? 5.468   -14.237 -16.702 1.00 56.23  ? 35  ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? 5.604   -15.679 -16.872 1.00 56.39  ? 35  ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? 6.924   -16.005 -17.554 1.00 61.21  ? 35  ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? 7.723   -16.799 -17.047 1.00 66.28  ? 35  ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? 4.427   -16.232 -17.678 1.00 51.76  ? 35  ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? 7.179   -15.369 -18.700 1.00 59.05  ? 36  GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? 8.431   -15.585 -19.415 1.00 62.93  ? 36  GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? 9.640   -15.178 -18.581 1.00 59.69  ? 36  GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? 10.714  -15.774 -18.716 1.00 58.74  ? 36  GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? 8.411   -14.814 -20.734 1.00 68.43  ? 36  GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? 7.256   -15.191 -21.648 1.00 76.53  ? 36  GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? 7.123   -14.258 -22.833 1.00 86.55  ? 36  GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? 6.582   -14.631 -23.874 1.00 102.88 ? 36  GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? 7.613   -13.032 -22.679 1.00 77.38  ? 36  GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? 9.492   -14.169 -17.723 1.00 59.38  ? 37  LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? 10.613  -13.746 -16.891 1.00 60.79  ? 37  LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? 10.806  -14.666 -15.689 1.00 63.87  ? 37  LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? 11.937  -15.055 -15.380 1.00 60.96  ? 37  LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? 10.410  -12.305 -16.423 1.00 59.28  ? 37  LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? 11.297  -11.891 -15.244 1.00 63.72  ? 37  LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? 12.762  -11.854 -15.649 1.00 64.35  ? 37  LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? 10.858  -10.555 -14.665 1.00 60.69  ? 37  LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? 9.718   -15.020 -15.002 1.00 59.03  ? 38  CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? 9.805   -15.805 -13.777 1.00 61.63  ? 38  CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? 9.851   -17.306 -14.022 1.00 59.75  ? 38  CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? 10.323  -18.047 -13.150 1.00 62.43  ? 38  CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? 8.622   -15.486 -12.858 1.00 62.05  ? 38  CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? 8.563   -13.773 -12.295 1.00 60.86  ? 38  CYS A SG    1 
ATOM   277  N  N     A GLN A 1 39  ? 9.368   -17.769 -15.172 0.53 63.99  ? 39  GLN A N     1 
ATOM   278  N  N     B GLN A 1 39  ? 9.370   -17.770 -15.171 0.47 64.41  ? 39  GLN A N     1 
ATOM   279  C  CA    A GLN A 1 39  ? 9.379   -19.186 -15.517 0.53 68.43  ? 39  GLN A CA    1 
ATOM   280  C  CA    B GLN A 1 39  ? 9.382   -19.187 -15.512 0.47 62.79  ? 39  GLN A CA    1 
ATOM   281  C  C     A GLN A 1 39  ? 8.602   -20.005 -14.492 0.53 69.56  ? 39  GLN A C     1 
ATOM   282  C  C     B GLN A 1 39  ? 8.601   -20.006 -14.490 0.47 63.75  ? 39  GLN A C     1 
ATOM   283  O  O     A GLN A 1 39  ? 9.168   -20.905 -13.859 0.53 61.03  ? 39  GLN A O     1 
ATOM   284  O  O     B GLN A 1 39  ? 9.164   -20.909 -13.857 0.47 67.59  ? 39  GLN A O     1 
ATOM   285  C  CB    A GLN A 1 39  ? 10.817  -19.699 -15.628 0.53 66.70  ? 39  GLN A CB    1 
ATOM   286  C  CB    B GLN A 1 39  ? 10.817  -19.707 -15.608 0.47 61.05  ? 39  GLN A CB    1 
ATOM   287  C  CG    A GLN A 1 39  ? 11.609  -19.099 -16.781 0.53 61.75  ? 39  GLN A CG    1 
ATOM   288  C  CG    B GLN A 1 39  ? 11.673  -18.990 -16.632 0.47 61.70  ? 39  GLN A CG    1 
ATOM   289  C  CD    A GLN A 1 39  ? 11.112  -19.563 -18.136 0.53 63.13  ? 39  GLN A CD    1 
ATOM   290  C  CD    B GLN A 1 39  ? 13.020  -19.654 -16.817 0.47 63.06  ? 39  GLN A CD    1 
ATOM   291  O  OE1   A GLN A 1 39  ? 10.275  -20.459 -18.231 0.53 70.62  ? 39  GLN A OE1   1 
ATOM   292  O  OE1   B GLN A 1 39  ? 13.129  -20.880 -16.789 0.47 66.37  ? 39  GLN A OE1   1 
ATOM   293  N  NE2   A GLN A 1 39  ? 11.629  -18.953 -19.195 0.53 64.82  ? 39  GLN A NE2   1 
ATOM   294  N  NE2   B GLN A 1 39  ? 14.057  -18.847 -16.997 0.47 62.99  ? 39  GLN A NE2   1 
ATOM   295  N  N     . PRO A 1 40  ? 7.317   -19.728 -14.294 1.00 63.37  ? 40  PRO A N     1 
ATOM   296  C  CA    . PRO A 1 40  ? 6.506   -20.589 -13.435 1.00 67.99  ? 40  PRO A CA    1 
ATOM   297  C  C     . PRO A 1 40  ? 6.113   -21.855 -14.178 1.00 63.45  ? 40  PRO A C     1 
ATOM   298  O  O     . PRO A 1 40  ? 5.905   -21.854 -15.393 1.00 63.20  ? 40  PRO A O     1 
ATOM   299  C  CB    . PRO A 1 40  ? 5.281   -19.722 -13.127 1.00 56.62  ? 40  PRO A CB    1 
ATOM   300  C  CG    . PRO A 1 40  ? 5.135   -18.879 -14.349 1.00 54.24  ? 40  PRO A CG    1 
ATOM   301  C  CD    . PRO A 1 40  ? 6.540   -18.593 -14.826 1.00 58.01  ? 40  PRO A CD    1 
ATOM   302  N  N     A GLU A 1 41  ? 6.026   -22.952 -13.424 0.60 62.72  ? 41  GLU A N     1 
ATOM   303  N  N     B GLU A 1 41  ? 6.019   -22.952 -13.426 0.40 62.85  ? 41  GLU A N     1 
ATOM   304  C  CA    A GLU A 1 41  ? 5.613   -24.217 -14.023 0.60 61.37  ? 41  GLU A CA    1 
ATOM   305  C  CA    B GLU A 1 41  ? 5.614   -24.213 -14.037 0.40 64.69  ? 41  GLU A CA    1 
ATOM   306  C  C     A GLU A 1 41  ? 4.146   -24.175 -14.434 0.60 63.36  ? 41  GLU A C     1 
ATOM   307  C  C     B GLU A 1 41  ? 4.139   -24.202 -14.416 0.40 63.42  ? 41  GLU A C     1 
ATOM   308  O  O     A GLU A 1 41  ? 3.765   -24.759 -15.455 0.60 63.86  ? 41  GLU A O     1 
ATOM   309  O  O     B GLU A 1 41  ? 3.749   -24.841 -15.400 0.40 64.05  ? 41  GLU A O     1 
ATOM   310  C  CB    A GLU A 1 41  ? 5.871   -25.367 -13.049 0.60 61.35  ? 41  GLU A CB    1 
ATOM   311  C  CB    B GLU A 1 41  ? 5.916   -25.380 -13.098 0.40 62.82  ? 41  GLU A CB    1 
ATOM   312  C  CG    A GLU A 1 41  ? 5.594   -26.756 -13.620 0.60 64.40  ? 41  GLU A CG    1 
ATOM   313  C  CG    B GLU A 1 41  ? 5.654   -26.747 -13.715 0.40 64.43  ? 41  GLU A CG    1 
ATOM   314  C  CD    A GLU A 1 41  ? 6.671   -27.226 -14.582 0.60 65.33  ? 41  GLU A CD    1 
ATOM   315  C  CD    B GLU A 1 41  ? 6.010   -27.887 -12.782 0.40 63.16  ? 41  GLU A CD    1 
ATOM   316  O  OE1   A GLU A 1 41  ? 7.493   -26.392 -15.014 0.60 64.09  ? 41  GLU A OE1   1 
ATOM   317  O  OE1   B GLU A 1 41  ? 6.433   -27.609 -11.642 0.40 62.99  ? 41  GLU A OE1   1 
ATOM   318  O  OE2   A GLU A 1 41  ? 6.701   -28.435 -14.901 0.60 69.85  ? 41  GLU A OE2   1 
ATOM   319  O  OE2   B GLU A 1 41  ? 5.866   -29.059 -13.189 0.40 66.29  ? 41  GLU A OE2   1 
ATOM   320  N  N     . TYR A 1 42  ? 3.311   -23.484 -13.660 1.00 61.83  ? 42  TYR A N     1 
ATOM   321  C  CA    . TYR A 1 42  ? 1.885   -23.391 -13.937 1.00 57.27  ? 42  TYR A CA    1 
ATOM   322  C  C     . TYR A 1 42  ? 1.428   -21.951 -13.761 1.00 55.78  ? 42  TYR A C     1 
ATOM   323  O  O     . TYR A 1 42  ? 2.029   -21.178 -13.011 1.00 52.69  ? 42  TYR A O     1 
ATOM   324  C  CB    . TYR A 1 42  ? 1.055   -24.304 -13.017 1.00 56.85  ? 42  TYR A CB    1 
ATOM   325  C  CG    . TYR A 1 42  ? 1.500   -25.747 -13.018 1.00 61.30  ? 42  TYR A CG    1 
ATOM   326  C  CD1   . TYR A 1 42  ? 1.134   -26.606 -14.046 1.00 55.98  ? 42  TYR A CD1   1 
ATOM   327  C  CD2   . TYR A 1 42  ? 2.285   -26.251 -11.991 1.00 59.57  ? 42  TYR A CD2   1 
ATOM   328  C  CE1   . TYR A 1 42  ? 1.541   -27.924 -14.053 1.00 63.48  ? 42  TYR A CE1   1 
ATOM   329  C  CE2   . TYR A 1 42  ? 2.696   -27.569 -11.989 1.00 66.60  ? 42  TYR A CE2   1 
ATOM   330  C  CZ    . TYR A 1 42  ? 2.321   -28.401 -13.022 1.00 64.89  ? 42  TYR A CZ    1 
ATOM   331  O  OH    . TYR A 1 42  ? 2.729   -29.715 -13.025 1.00 69.52  ? 42  TYR A OH    1 
ATOM   332  N  N     . ILE A 1 43  ? 0.351   -21.604 -14.460 1.00 52.93  ? 43  ILE A N     1 
ATOM   333  C  CA    . ILE A 1 43  ? -0.290  -20.302 -14.340 1.00 54.35  ? 43  ILE A CA    1 
ATOM   334  C  C     . ILE A 1 43  ? -1.750  -20.541 -13.987 1.00 53.34  ? 43  ILE A C     1 
ATOM   335  O  O     . ILE A 1 43  ? -2.458  -21.254 -14.710 1.00 52.52  ? 43  ILE A O     1 
ATOM   336  C  CB    . ILE A 1 43  ? -0.168  -19.471 -15.628 1.00 51.84  ? 43  ILE A CB    1 
ATOM   337  C  CG1   . ILE A 1 43  ? 1.305   -19.247 -15.980 1.00 53.15  ? 43  ILE A CG1   1 
ATOM   338  C  CG2   . ILE A 1 43  ? -0.885  -18.144 -15.466 1.00 48.37  ? 43  ILE A CG2   1 
ATOM   339  C  CD1   . ILE A 1 43  ? 1.518   -18.441 -17.244 1.00 54.74  ? 43  ILE A CD1   1 
ATOM   340  N  N     . HIS A 1 44  ? -2.197  -19.946 -12.884 1.00 50.48  ? 44  HIS A N     1 
ATOM   341  C  CA    . HIS A 1 44  ? -3.533  -20.155 -12.341 1.00 47.09  ? 44  HIS A CA    1 
ATOM   342  C  C     . HIS A 1 44  ? -4.228  -18.804 -12.246 1.00 49.57  ? 44  HIS A C     1 
ATOM   343  O  O     . HIS A 1 44  ? -3.806  -17.937 -11.472 1.00 44.62  ? 44  HIS A O     1 
ATOM   344  C  CB    . HIS A 1 44  ? -3.447  -20.838 -10.972 1.00 47.97  ? 44  HIS A CB    1 
ATOM   345  C  CG    . HIS A 1 44  ? -4.774  -21.151 -10.355 1.00 53.19  ? 44  HIS A CG    1 
ATOM   346  N  ND1   . HIS A 1 44  ? -5.464  -20.248 -9.576  1.00 59.65  ? 44  HIS A ND1   1 
ATOM   347  C  CD2   . HIS A 1 44  ? -5.525  -22.277 -10.378 1.00 52.60  ? 44  HIS A CD2   1 
ATOM   348  C  CE1   . HIS A 1 44  ? -6.589  -20.800 -9.156  1.00 49.95  ? 44  HIS A CE1   1 
ATOM   349  N  NE2   . HIS A 1 44  ? -6.650  -22.031 -9.630  1.00 48.79  ? 44  HIS A NE2   1 
ATOM   350  N  N     . ILE A 1 45  ? -5.281  -18.624 -13.038 1.00 47.17  ? 45  ILE A N     1 
ATOM   351  C  CA    . ILE A 1 45  ? -6.014  -17.365 -13.112 1.00 51.20  ? 45  ILE A CA    1 
ATOM   352  C  C     . ILE A 1 45  ? -7.196  -17.467 -12.155 1.00 51.26  ? 45  ILE A C     1 
ATOM   353  O  O     . ILE A 1 45  ? -8.214  -18.089 -12.473 1.00 47.55  ? 45  ILE A O     1 
ATOM   354  C  CB    . ILE A 1 45  ? -6.469  -17.060 -14.540 1.00 51.87  ? 45  ILE A CB    1 
ATOM   355  C  CG1   . ILE A 1 45  ? -5.277  -17.086 -15.497 1.00 48.56  ? 45  ILE A CG1   1 
ATOM   356  C  CG2   . ILE A 1 45  ? -7.167  -15.711 -14.591 1.00 50.74  ? 45  ILE A CG2   1 
ATOM   357  C  CD1   . ILE A 1 45  ? -5.655  -16.847 -16.936 1.00 53.87  ? 45  ILE A CD1   1 
ATOM   358  N  N     . CYS A 1 46  ? -7.070  -16.835 -10.989 1.00 55.66  ? 46  CYS A N     1 
ATOM   359  C  CA    . CYS A 1 46  ? -8.090  -16.947 -9.954  1.00 49.61  ? 46  CYS A CA    1 
ATOM   360  C  C     . CYS A 1 46  ? -9.433  -16.421 -10.444 1.00 53.97  ? 46  CYS A C     1 
ATOM   361  O  O     . CYS A 1 46  ? -9.505  -15.435 -11.183 1.00 50.14  ? 46  CYS A O     1 
ATOM   362  C  CB    . CYS A 1 46  ? -7.659  -16.183 -8.702  1.00 43.33  ? 46  CYS A CB    1 
ATOM   363  S  SG    . CYS A 1 46  ? -6.070  -16.710 -8.030  1.00 50.31  ? 46  CYS A SG    1 
ATOM   364  N  N     . ASP A 1 47  ? -10.506 -17.094 -10.027 1.00 53.39  ? 47  ASP A N     1 
ATOM   365  C  CA    . ASP A 1 47  ? -11.860 -16.638 -10.299 1.00 56.87  ? 47  ASP A CA    1 
ATOM   366  C  C     . ASP A 1 47  ? -12.632 -16.290 -9.035  1.00 52.58  ? 47  ASP A C     1 
ATOM   367  O  O     . ASP A 1 47  ? -13.821 -15.968 -9.124  1.00 55.61  ? 47  ASP A O     1 
ATOM   368  C  CB    . ASP A 1 47  ? -12.634 -17.693 -11.105 1.00 54.70  ? 47  ASP A CB    1 
ATOM   369  C  CG    . ASP A 1 47  ? -12.899 -18.970 -10.320 1.00 56.33  ? 47  ASP A CG    1 
ATOM   370  O  OD1   . ASP A 1 47  ? -12.554 -19.044 -9.121  1.00 55.62  ? 47  ASP A OD1   1 
ATOM   371  O  OD2   . ASP A 1 47  ? -13.460 -19.911 -10.917 1.00 62.21  ? 47  ASP A OD2   1 
ATOM   372  N  N     . GLY A 1 48  ? -11.996 -16.356 -7.865  1.00 55.43  ? 48  GLY A N     1 
ATOM   373  C  CA    . GLY A 1 48  ? -12.626 -15.989 -6.614  1.00 55.68  ? 48  GLY A CA    1 
ATOM   374  C  C     . GLY A 1 48  ? -13.675 -16.949 -6.096  1.00 58.30  ? 48  GLY A C     1 
ATOM   375  O  O     . GLY A 1 48  ? -14.262 -16.681 -5.040  1.00 55.56  ? 48  GLY A O     1 
ATOM   376  N  N     . SER A 1 49  ? -13.920 -18.061 -6.783  1.00 53.60  ? 49  SER A N     1 
ATOM   377  C  CA    . SER A 1 49  ? -15.010 -18.952 -6.418  1.00 61.52  ? 49  SER A CA    1 
ATOM   378  C  C     . SER A 1 49  ? -14.740 -19.646 -5.084  1.00 58.42  ? 49  SER A C     1 
ATOM   379  O  O     . SER A 1 49  ? -13.598 -19.791 -4.640  1.00 59.82  ? 49  SER A O     1 
ATOM   380  C  CB    . SER A 1 49  ? -15.227 -20.001 -7.507  1.00 59.71  ? 49  SER A CB    1 
ATOM   381  O  OG    . SER A 1 49  ? -14.097 -20.847 -7.620  1.00 59.01  ? 49  SER A OG    1 
ATOM   382  N  N     . GLU A 1 50  ? -15.826 -20.083 -4.442  1.00 61.04  ? 50  GLU A N     1 
ATOM   383  C  CA    . GLU A 1 50  ? -15.693 -20.877 -3.225  1.00 67.31  ? 50  GLU A CA    1 
ATOM   384  C  C     . GLU A 1 50  ? -14.960 -22.185 -3.503  1.00 71.44  ? 50  GLU A C     1 
ATOM   385  O  O     . GLU A 1 50  ? -14.180 -22.659 -2.668  1.00 66.62  ? 50  GLU A O     1 
ATOM   386  C  CB    . GLU A 1 50  ? -17.073 -21.153 -2.625  1.00 72.12  ? 50  GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 50  ? -17.811 -19.913 -2.143  1.00 82.76  ? 50  GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 50  ? -17.251 -19.366 -0.844  1.00 97.11  ? 50  GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 50  ? -16.365 -20.022 -0.256  1.00 97.32  ? 50  GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 50  ? -17.698 -18.283 -0.408  1.00 98.03  ? 50  GLU A OE2   1 
ATOM   391  N  N     . GLU A 1 51  ? -15.203 -22.786 -4.671  1.00 66.98  ? 51  GLU A N     1 
ATOM   392  C  CA    . GLU A 1 51  ? -14.483 -23.998 -5.052  1.00 60.18  ? 51  GLU A CA    1 
ATOM   393  C  C     . GLU A 1 51  ? -12.983 -23.740 -5.117  1.00 66.46  ? 51  GLU A C     1 
ATOM   394  O  O     . GLU A 1 51  ? -12.184 -24.482 -4.533  1.00 63.72  ? 51  GLU A O     1 
ATOM   395  C  CB    . GLU A 1 51  ? -14.999 -24.515 -6.396  1.00 60.95  ? 51  GLU A CB    1 
ATOM   396  C  CG    . GLU A 1 51  ? -16.409 -25.093 -6.356  1.00 78.65  ? 51  GLU A CG    1 
ATOM   397  C  CD    . GLU A 1 51  ? -17.474 -24.046 -6.077  1.00 84.27  ? 51  GLU A CD    1 
ATOM   398  O  OE1   . GLU A 1 51  ? -17.157 -22.839 -6.143  1.00 72.55  ? 51  GLU A OE1   1 
ATOM   399  O  OE2   . GLU A 1 51  ? -18.628 -24.430 -5.788  1.00 93.39  ? 51  GLU A OE2   1 
ATOM   400  N  N     . GLU A 1 52  ? -12.584 -22.688 -5.833  1.00 64.30  ? 52  GLU A N     1 
ATOM   401  C  CA    . GLU A 1 52  ? -11.183 -22.287 -5.873  1.00 60.31  ? 52  GLU A CA    1 
ATOM   402  C  C     . GLU A 1 52  ? -10.612 -22.158 -4.465  1.00 62.69  ? 52  GLU A C     1 
ATOM   403  O  O     . GLU A 1 52  ? -9.607  -22.791 -4.124  1.00 61.43  ? 52  GLU A O     1 
ATOM   404  C  CB    . GLU A 1 52  ? -11.056 -20.974 -6.645  1.00 50.75  ? 52  GLU A CB    1 
ATOM   405  C  CG    . GLU A 1 52  ? -9.735  -20.256 -6.475  1.00 50.64  ? 52  GLU A CG    1 
ATOM   406  C  CD    . GLU A 1 52  ? -9.638  -19.034 -7.365  1.00 51.37  ? 52  GLU A CD    1 
ATOM   407  O  OE1   . GLU A 1 52  ? -9.418  -19.202 -8.582  1.00 51.15  ? 52  GLU A OE1   1 
ATOM   408  O  OE2   . GLU A 1 52  ? -9.802  -17.906 -6.851  1.00 57.65  ? 52  GLU A OE2   1 
ATOM   409  N  N     . TYR A 1 53  ? -11.254 -21.336 -3.630  1.00 61.09  ? 53  TYR A N     1 
ATOM   410  C  CA    . TYR A 1 53  ? -10.840 -21.216 -2.235  1.00 61.18  ? 53  TYR A CA    1 
ATOM   411  C  C     . TYR A 1 53  ? -10.736 -22.583 -1.570  1.00 62.64  ? 53  TYR A C     1 
ATOM   412  O  O     . TYR A 1 53  ? -9.813  -22.835 -0.786  1.00 61.68  ? 53  TYR A O     1 
ATOM   413  C  CB    . TYR A 1 53  ? -11.825 -20.321 -1.480  1.00 58.52  ? 53  TYR A CB    1 
ATOM   414  C  CG    . TYR A 1 53  ? -11.314 -19.805 -0.155  1.00 61.00  ? 53  TYR A CG    1 
ATOM   415  C  CD1   . TYR A 1 53  ? -10.103 -19.129 -0.073  1.00 62.25  ? 53  TYR A CD1   1 
ATOM   416  C  CD2   . TYR A 1 53  ? -12.054 -19.967 1.009   1.00 59.07  ? 53  TYR A CD2   1 
ATOM   417  C  CE1   . TYR A 1 53  ? -9.634  -18.646 1.134   1.00 59.38  ? 53  TYR A CE1   1 
ATOM   418  C  CE2   . TYR A 1 53  ? -11.594 -19.486 2.220   1.00 58.55  ? 53  TYR A CE2   1 
ATOM   419  C  CZ    . TYR A 1 53  ? -10.383 -18.826 2.277   1.00 61.91  ? 53  TYR A CZ    1 
ATOM   420  O  OH    . TYR A 1 53  ? -9.917  -18.345 3.478   1.00 53.63  ? 53  TYR A OH    1 
ATOM   421  N  N     . GLY A 1 54  ? -11.668 -23.483 -1.879  1.00 61.58  ? 54  GLY A N     1 
ATOM   422  C  CA    . GLY A 1 54  ? -11.660 -24.820 -1.319  1.00 67.90  ? 54  GLY A CA    1 
ATOM   423  C  C     . GLY A 1 54  ? -10.449 -25.637 -1.721  1.00 72.72  ? 54  GLY A C     1 
ATOM   424  O  O     . GLY A 1 54  ? -9.684  -26.082 -0.860  1.00 65.08  ? 54  GLY A O     1 
ATOM   425  N  N     . ARG A 1 55  ? -10.265 -25.850 -3.027  1.00 75.98  ? 55  ARG A N     1 
ATOM   426  C  CA    . ARG A 1 55  ? -9.089  -26.582 -3.486  1.00 75.94  ? 55  ARG A CA    1 
ATOM   427  C  C     . ARG A 1 55  ? -7.810  -25.900 -3.021  1.00 75.71  ? 55  ARG A C     1 
ATOM   428  O  O     . ARG A 1 55  ? -6.823  -26.569 -2.694  1.00 77.36  ? 55  ARG A O     1 
ATOM   429  C  CB    . ARG A 1 55  ? -9.099  -26.711 -5.010  1.00 77.15  ? 55  ARG A CB    1 
ATOM   430  C  CG    . ARG A 1 55  ? -10.424 -27.161 -5.609  1.00 81.23  ? 55  ARG A CG    1 
ATOM   431  C  CD    . ARG A 1 55  ? -10.886 -28.520 -5.079  1.00 100.22 ? 55  ARG A CD    1 
ATOM   432  N  NE    . ARG A 1 55  ? -9.983  -29.613 -5.427  1.00 94.62  ? 55  ARG A NE    1 
ATOM   433  C  CZ    . ARG A 1 55  ? -9.374  -30.395 -4.544  1.00 89.59  ? 55  ARG A CZ    1 
ATOM   434  N  NH1   . ARG A 1 55  ? -9.563  -30.247 -3.243  1.00 87.13  ? 55  ARG A NH1   1 
ATOM   435  N  NH2   . ARG A 1 55  ? -8.561  -31.354 -4.979  1.00 84.60  ? 55  ARG A NH2   1 
ATOM   436  N  N     . LEU A 1 56  ? -7.815  -24.565 -2.973  1.00 64.75  ? 56  LEU A N     1 
ATOM   437  C  CA    . LEU A 1 56  ? -6.630  -23.825 -2.551  1.00 60.17  ? 56  LEU A CA    1 
ATOM   438  C  C     . LEU A 1 56  ? -6.234  -24.186 -1.125  1.00 66.84  ? 56  LEU A C     1 
ATOM   439  O  O     . LEU A 1 56  ? -5.077  -24.530 -0.857  1.00 68.25  ? 56  LEU A O     1 
ATOM   440  C  CB    . LEU A 1 56  ? -6.882  -22.324 -2.677  1.00 62.13  ? 56  LEU A CB    1 
ATOM   441  C  CG    . LEU A 1 56  ? -5.714  -21.415 -2.301  1.00 60.28  ? 56  LEU A CG    1 
ATOM   442  C  CD1   . LEU A 1 56  ? -4.529  -21.665 -3.226  1.00 60.71  ? 56  LEU A CD1   1 
ATOM   443  C  CD2   . LEU A 1 56  ? -6.141  -19.955 -2.342  1.00 60.45  ? 56  LEU A CD2   1 
ATOM   444  N  N     . LEU A 1 57  ? -7.182  -24.100 -0.189  1.00 63.64  ? 57  LEU A N     1 
ATOM   445  C  CA    . LEU A 1 57  ? -6.896  -24.474 1.192   1.00 66.40  ? 57  LEU A CA    1 
ATOM   446  C  C     . LEU A 1 57  ? -6.433  -25.923 1.280   1.00 67.75  ? 57  LEU A C     1 
ATOM   447  O  O     . LEU A 1 57  ? -5.419  -26.225 1.921   1.00 73.62  ? 57  LEU A O     1 
ATOM   448  C  CB    . LEU A 1 57  ? -8.131  -24.248 2.065   1.00 66.75  ? 57  LEU A CB    1 
ATOM   449  C  CG    . LEU A 1 57  ? -8.495  -22.791 2.353   1.00 66.90  ? 57  LEU A CG    1 
ATOM   450  C  CD1   . LEU A 1 57  ? -9.852  -22.701 3.033   1.00 56.81  ? 57  LEU A CD1   1 
ATOM   451  C  CD2   . LEU A 1 57  ? -7.420  -22.130 3.205   1.00 56.42  ? 57  LEU A CD2   1 
ATOM   452  N  N     . ALA A 1 58  ? -7.166  -26.836 0.639   1.00 68.30  ? 58  ALA A N     1 
ATOM   453  C  CA    . ALA A 1 58  ? -6.781  -28.245 0.668   1.00 75.08  ? 58  ALA A CA    1 
ATOM   454  C  C     . ALA A 1 58  ? -5.354  -28.438 0.172   1.00 70.91  ? 58  ALA A C     1 
ATOM   455  O  O     . ALA A 1 58  ? -4.585  -29.209 0.757   1.00 73.96  ? 58  ALA A O     1 
ATOM   456  C  CB    . ALA A 1 58  ? -7.758  -29.078 -0.164  1.00 76.22  ? 58  ALA A CB    1 
ATOM   457  N  N     . HIS A 1 59  ? -4.980  -27.745 -0.906  1.00 66.62  ? 59  HIS A N     1 
ATOM   458  C  CA    . HIS A 1 59  ? -3.612  -27.839 -1.405  1.00 70.05  ? 59  HIS A CA    1 
ATOM   459  C  C     . HIS A 1 59  ? -2.611  -27.395 -0.344  1.00 72.76  ? 59  HIS A C     1 
ATOM   460  O  O     . HIS A 1 59  ? -1.625  -28.090 -0.072  1.00 71.26  ? 59  HIS A O     1 
ATOM   461  C  CB    . HIS A 1 59  ? -3.458  -27.000 -2.674  1.00 73.21  ? 59  HIS A CB    1 
ATOM   462  C  CG    . HIS A 1 59  ? -2.080  -27.037 -3.258  1.00 76.97  ? 59  HIS A CG    1 
ATOM   463  N  ND1   . HIS A 1 59  ? -1.450  -28.214 -3.602  1.00 72.34  ? 59  HIS A ND1   1 
ATOM   464  C  CD2   . HIS A 1 59  ? -1.213  -26.043 -3.561  1.00 78.11  ? 59  HIS A CD2   1 
ATOM   465  C  CE1   . HIS A 1 59  ? -0.254  -27.943 -4.093  1.00 78.34  ? 59  HIS A CE1   1 
ATOM   466  N  NE2   . HIS A 1 59  ? -0.085  -26.632 -4.078  1.00 84.04  ? 59  HIS A NE2   1 
ATOM   467  N  N     . MET A 1 60  ? -2.852  -26.232 0.268   1.00 72.63  ? 60  MET A N     1 
ATOM   468  C  CA    . MET A 1 60  ? -1.942  -25.737 1.296   1.00 68.74  ? 60  MET A CA    1 
ATOM   469  C  C     . MET A 1 60  ? -1.861  -26.688 2.478   1.00 68.26  ? 60  MET A C     1 
ATOM   470  O  O     . MET A 1 60  ? -0.800  -26.811 3.101   1.00 69.44  ? 60  MET A O     1 
ATOM   471  C  CB    . MET A 1 60  ? -2.380  -24.351 1.765   1.00 68.53  ? 60  MET A CB    1 
ATOM   472  C  CG    . MET A 1 60  ? -1.889  -23.219 0.889   1.00 59.65  ? 60  MET A CG    1 
ATOM   473  S  SD    . MET A 1 60  ? -2.361  -21.614 1.545   1.00 58.25  ? 60  MET A SD    1 
ATOM   474  C  CE    . MET A 1 60  ? -4.094  -21.554 1.099   1.00 57.59  ? 60  MET A CE    1 
ATOM   475  N  N     . GLN A 1 61  ? -2.966  -27.361 2.808   1.00 68.76  ? 61  GLN A N     1 
ATOM   476  C  CA    . GLN A 1 61  ? -2.958  -28.299 3.924   1.00 72.98  ? 61  GLN A CA    1 
ATOM   477  C  C     . GLN A 1 61  ? -2.213  -29.580 3.574   1.00 81.24  ? 61  GLN A C     1 
ATOM   478  O  O     . GLN A 1 61  ? -1.589  -30.192 4.449   1.00 81.43  ? 61  GLN A O     1 
ATOM   479  C  CB    . GLN A 1 61  ? -4.390  -28.616 4.351   1.00 70.87  ? 61  GLN A CB    1 
ATOM   480  C  CG    . GLN A 1 61  ? -4.501  -29.482 5.592   1.00 65.30  ? 61  GLN A CG    1 
ATOM   481  C  CD    . GLN A 1 61  ? -5.938  -29.839 5.909   1.00 74.67  ? 61  GLN A CD    1 
ATOM   482  O  OE1   . GLN A 1 61  ? -6.813  -29.739 5.048   1.00 72.11  ? 61  GLN A OE1   1 
ATOM   483  N  NE2   . GLN A 1 61  ? -6.193  -30.249 7.148   1.00 67.72  ? 61  GLN A NE2   1 
ATOM   484  N  N     . GLU A 1 62  ? -2.272  -30.003 2.309   1.00 82.89  ? 62  GLU A N     1 
ATOM   485  C  CA    . GLU A 1 62  ? -1.507  -31.155 1.850   1.00 80.69  ? 62  GLU A CA    1 
ATOM   486  C  C     . GLU A 1 62  ? -0.025  -30.840 1.689   1.00 80.86  ? 62  GLU A C     1 
ATOM   487  O  O     . GLU A 1 62  ? 0.789   -31.767 1.613   1.00 86.00  ? 62  GLU A O     1 
ATOM   488  C  CB    . GLU A 1 62  ? -2.077  -31.665 0.522   1.00 74.21  ? 62  GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 62  ? -3.548  -32.051 0.591   1.00 76.40  ? 62  GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 62  ? -4.181  -32.209 -0.780  1.00 68.89  ? 62  GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 62  ? -3.469  -32.045 -1.792  1.00 68.13  ? 62  GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 62  ? -5.396  -32.492 -0.845  1.00 74.48  ? 62  GLU A OE2   1 
ATOM   493  N  N     . GLU A 1 63  ? 0.338   -29.559 1.640   1.00 76.50  ? 63  GLU A N     1 
ATOM   494  C  CA    . GLU A 1 63  ? 1.723   -29.126 1.517   1.00 80.67  ? 63  GLU A CA    1 
ATOM   495  C  C     . GLU A 1 63  ? 2.335   -28.732 2.854   1.00 83.59  ? 63  GLU A C     1 
ATOM   496  O  O     . GLU A 1 63  ? 3.457   -28.216 2.881   1.00 86.07  ? 63  GLU A O     1 
ATOM   497  C  CB    . GLU A 1 63  ? 1.823   -27.951 0.544   1.00 77.05  ? 63  GLU A CB    1 
ATOM   498  C  CG    . GLU A 1 63  ? 1.476   -28.284 -0.896  1.00 85.45  ? 63  GLU A CG    1 
ATOM   499  C  CD    . GLU A 1 63  ? 2.581   -29.044 -1.599  1.00 89.00  ? 63  GLU A CD    1 
ATOM   500  O  OE1   . GLU A 1 63  ? 3.174   -29.945 -0.971  1.00 91.01  ? 63  GLU A OE1   1 
ATOM   501  O  OE2   . GLU A 1 63  ? 2.862   -28.732 -2.777  1.00 90.29  ? 63  GLU A OE2   1 
ATOM   502  N  N     . GLY A 1 64  ? 1.625   -28.951 3.959   1.00 80.61  ? 64  GLY A N     1 
ATOM   503  C  CA    . GLY A 1 64  ? 2.113   -28.515 5.251   1.00 74.10  ? 64  GLY A CA    1 
ATOM   504  C  C     . GLY A 1 64  ? 2.198   -27.017 5.422   1.00 78.26  ? 64  GLY A C     1 
ATOM   505  O  O     . GLY A 1 64  ? 2.885   -26.546 6.333   1.00 83.41  ? 64  GLY A O     1 
ATOM   506  N  N     . VAL A 1 65  ? 1.516   -26.248 4.574   1.00 73.76  ? 65  VAL A N     1 
ATOM   507  C  CA    . VAL A 1 65  ? 1.586   -24.793 4.667   1.00 71.69  ? 65  VAL A CA    1 
ATOM   508  C  C     . VAL A 1 65  ? 0.742   -24.283 5.827   1.00 73.84  ? 65  VAL A C     1 
ATOM   509  O  O     . VAL A 1 65  ? 1.221   -23.515 6.669   1.00 76.89  ? 65  VAL A O     1 
ATOM   510  C  CB    . VAL A 1 65  ? 1.162   -24.149 3.334   1.00 73.99  ? 65  VAL A CB    1 
ATOM   511  C  CG1   . VAL A 1 65  ? 1.076   -22.636 3.480   1.00 62.30  ? 65  VAL A CG1   1 
ATOM   512  C  CG2   . VAL A 1 65  ? 2.141   -24.522 2.235   1.00 75.31  ? 65  VAL A CG2   1 
ATOM   513  N  N     . ILE A 1 66  ? -0.525  -24.692 5.891   1.00 71.08  ? 66  ILE A N     1 
ATOM   514  C  CA    . ILE A 1 66  ? -1.436  -24.229 6.929   1.00 70.95  ? 66  ILE A CA    1 
ATOM   515  C  C     . ILE A 1 66  ? -2.101  -25.424 7.596   1.00 68.92  ? 66  ILE A C     1 
ATOM   516  O  O     . ILE A 1 66  ? -2.232  -26.501 7.006   1.00 71.64  ? 66  ILE A O     1 
ATOM   517  C  CB    . ILE A 1 66  ? -2.508  -23.263 6.376   1.00 68.57  ? 66  ILE A CB    1 
ATOM   518  C  CG1   . ILE A 1 66  ? -3.374  -23.963 5.327   1.00 63.79  ? 66  ILE A CG1   1 
ATOM   519  C  CG2   . ILE A 1 66  ? -1.859  -22.013 5.803   1.00 67.36  ? 66  ILE A CG2   1 
ATOM   520  C  CD1   . ILE A 1 66  ? -4.439  -23.068 4.728   1.00 63.52  ? 66  ILE A CD1   1 
ATOM   521  N  N     . ARG A 1 67  ? -2.521  -25.222 8.839   1.00 71.73  ? 67  ARG A N     1 
ATOM   522  C  CA    . ARG A 1 67  ? -3.286  -26.201 9.595   1.00 61.49  ? 67  ARG A CA    1 
ATOM   523  C  C     . ARG A 1 67  ? -4.747  -25.779 9.666   1.00 60.11  ? 67  ARG A C     1 
ATOM   524  O  O     . ARG A 1 67  ? -5.087  -24.602 9.519   1.00 65.23  ? 67  ARG A O     1 
ATOM   525  C  CB    . ARG A 1 67  ? -2.726  -26.358 11.010  1.00 67.41  ? 67  ARG A CB    1 
ATOM   526  C  CG    . ARG A 1 67  ? -1.357  -27.005 11.084  1.00 80.45  ? 67  ARG A CG    1 
ATOM   527  C  CD    . ARG A 1 67  ? -0.901  -27.164 12.530  1.00 89.78  ? 67  ARG A CD    1 
ATOM   528  N  NE    . ARG A 1 67  ? -1.801  -28.007 13.310  1.00 89.33  ? 67  ARG A NE    1 
ATOM   529  C  CZ    . ARG A 1 67  ? -1.624  -29.305 13.519  1.00 100.65 ? 67  ARG A CZ    1 
ATOM   530  N  NH1   . ARG A 1 67  ? -0.588  -29.953 13.010  1.00 107.75 ? 67  ARG A NH1   1 
ATOM   531  N  NH2   . ARG A 1 67  ? -2.507  -29.971 14.259  1.00 97.49  ? 67  ARG A NH2   1 
ATOM   532  N  N     . LYS A 1 68  ? -5.615  -26.758 9.897   1.00 62.80  ? 68  LYS A N     1 
ATOM   533  C  CA    . LYS A 1 68  ? -7.032  -26.501 10.112  1.00 64.83  ? 68  LYS A CA    1 
ATOM   534  C  C     . LYS A 1 68  ? -7.305  -26.436 11.606  1.00 64.26  ? 68  LYS A C     1 
ATOM   535  O  O     . LYS A 1 68  ? -6.897  -27.329 12.355  1.00 64.00  ? 68  LYS A O     1 
ATOM   536  C  CB    . LYS A 1 68  ? -7.906  -27.578 9.470   1.00 63.25  ? 68  LYS A CB    1 
ATOM   537  C  CG    . LYS A 1 68  ? -9.369  -27.175 9.369   1.00 61.58  ? 68  LYS A CG    1 
ATOM   538  C  CD    . LYS A 1 68  ? -10.204 -28.235 8.676   1.00 64.76  ? 68  LYS A CD    1 
ATOM   539  C  CE    . LYS A 1 68  ? -11.467 -27.632 8.079   1.00 72.59  ? 68  LYS A CE    1 
ATOM   540  N  NZ    . LYS A 1 68  ? -12.251 -26.855 9.080   1.00 78.80  ? 68  LYS A NZ    1 
ATOM   541  N  N     . LEU A 1 69  ? -7.991  -25.378 12.033  1.00 62.11  ? 69  LEU A N     1 
ATOM   542  C  CA    . LEU A 1 69  ? -8.387  -25.216 13.431  1.00 66.19  ? 69  LEU A CA    1 
ATOM   543  C  C     . LEU A 1 69  ? -9.730  -25.910 13.604  1.00 70.29  ? 69  LEU A C     1 
ATOM   544  O  O     . LEU A 1 69  ? -10.793 -25.329 13.381  1.00 71.18  ? 69  LEU A O     1 
ATOM   545  C  CB    . LEU A 1 69  ? -8.442  -23.741 13.803  1.00 60.51  ? 69  LEU A CB    1 
ATOM   546  C  CG    . LEU A 1 69  ? -7.109  -23.017 13.588  1.00 66.83  ? 69  LEU A CG    1 
ATOM   547  C  CD1   . LEU A 1 69  ? -7.295  -21.509 13.525  1.00 56.62  ? 69  LEU A CD1   1 
ATOM   548  C  CD2   . LEU A 1 69  ? -6.122  -23.402 14.684  1.00 68.32  ? 69  LEU A CD2   1 
ATOM   549  N  N     . LYS A 1 70  ? -9.677  -27.184 14.002  1.00 79.18  ? 70  LYS A N     1 
ATOM   550  C  CA    . LYS A 1 70  ? -10.882 -28.004 14.066  1.00 80.32  ? 70  LYS A CA    1 
ATOM   551  C  C     . LYS A 1 70  ? -11.929 -27.443 15.021  1.00 80.69  ? 70  LYS A C     1 
ATOM   552  O  O     . LYS A 1 70  ? -13.111 -27.780 14.891  1.00 82.96  ? 70  LYS A O     1 
ATOM   553  C  CB    . LYS A 1 70  ? -10.514 -29.434 14.467  1.00 82.13  ? 70  LYS A CB    1 
ATOM   554  C  CG    . LYS A 1 70  ? -9.601  -29.524 15.681  1.00 90.99  ? 70  LYS A CG    1 
ATOM   555  C  CD    . LYS A 1 70  ? -9.451  -30.964 16.155  1.00 96.96  ? 70  LYS A CD    1 
ATOM   556  C  CE    . LYS A 1 70  ? -8.760  -31.034 17.510  1.00 93.29  ? 70  LYS A CE    1 
ATOM   557  N  NZ    . LYS A 1 70  ? -8.758  -32.414 18.072  1.00 94.55  ? 70  LYS A NZ    1 
ATOM   558  N  N     . LYS A 1 71  ? -11.535 -26.588 15.967  1.00 76.63  ? 71  LYS A N     1 
ATOM   559  C  CA    . LYS A 1 71  ? -12.486 -26.088 16.951  1.00 71.94  ? 71  LYS A CA    1 
ATOM   560  C  C     . LYS A 1 71  ? -13.461 -25.071 16.371  1.00 72.31  ? 71  LYS A C     1 
ATOM   561  O  O     . LYS A 1 71  ? -14.559 -24.909 16.913  1.00 72.20  ? 71  LYS A O     1 
ATOM   562  C  CB    . LYS A 1 71  ? -11.741 -25.467 18.133  1.00 74.23  ? 71  LYS A CB    1 
ATOM   563  C  CG    . LYS A 1 71  ? -12.644 -24.916 19.221  1.00 74.44  ? 71  LYS A CG    1 
ATOM   564  C  CD    . LYS A 1 71  ? -11.835 -24.531 20.443  1.00 75.55  ? 71  LYS A CD    1 
ATOM   565  C  CE    . LYS A 1 71  ? -12.734 -24.072 21.571  1.00 80.87  ? 71  LYS A CE    1 
ATOM   566  N  NZ    . LYS A 1 71  ? -12.001 -24.034 22.863  1.00 93.95  ? 71  LYS A NZ    1 
ATOM   567  N  N     . TYR A 1 72  ? -13.096 -24.386 15.295  1.00 71.54  ? 72  TYR A N     1 
ATOM   568  C  CA    . TYR A 1 72  ? -13.922 -23.320 14.744  1.00 73.77  ? 72  TYR A CA    1 
ATOM   569  C  C     . TYR A 1 72  ? -14.411 -23.702 13.350  1.00 72.05  ? 72  TYR A C     1 
ATOM   570  O  O     . TYR A 1 72  ? -14.101 -24.775 12.826  1.00 76.46  ? 72  TYR A O     1 
ATOM   571  C  CB    . TYR A 1 72  ? -13.153 -21.997 14.718  1.00 65.48  ? 72  TYR A CB    1 
ATOM   572  C  CG    . TYR A 1 72  ? -12.515 -21.651 16.042  1.00 64.26  ? 72  TYR A CG    1 
ATOM   573  C  CD1   . TYR A 1 72  ? -13.291 -21.301 17.138  1.00 66.42  ? 72  TYR A CD1   1 
ATOM   574  C  CD2   . TYR A 1 72  ? -11.135 -21.677 16.197  1.00 63.30  ? 72  TYR A CD2   1 
ATOM   575  C  CE1   . TYR A 1 72  ? -12.711 -20.986 18.352  1.00 67.56  ? 72  TYR A CE1   1 
ATOM   576  C  CE2   . TYR A 1 72  ? -10.546 -21.363 17.405  1.00 64.46  ? 72  TYR A CE2   1 
ATOM   577  C  CZ    . TYR A 1 72  ? -11.338 -21.018 18.479  1.00 68.74  ? 72  TYR A CZ    1 
ATOM   578  O  OH    . TYR A 1 72  ? -10.753 -20.704 19.684  1.00 68.16  ? 72  TYR A OH    1 
ATOM   579  N  N     . ASP A 1 73  ? -15.187 -22.800 12.754  1.00 67.82  ? 73  ASP A N     1 
ATOM   580  C  CA    . ASP A 1 73  ? -15.793 -23.022 11.446  1.00 70.94  ? 73  ASP A CA    1 
ATOM   581  C  C     . ASP A 1 73  ? -14.886 -22.431 10.372  1.00 69.69  ? 73  ASP A C     1 
ATOM   582  O  O     . ASP A 1 73  ? -14.807 -21.207 10.220  1.00 68.92  ? 73  ASP A O     1 
ATOM   583  C  CB    . ASP A 1 73  ? -17.188 -22.402 11.396  1.00 77.01  ? 73  ASP A CB    1 
ATOM   584  C  CG    . ASP A 1 73  ? -17.915 -22.684 10.090  1.00 84.55  ? 73  ASP A CG    1 
ATOM   585  O  OD1   . ASP A 1 73  ? -17.248 -22.909 9.057   1.00 82.83  ? 73  ASP A OD1   1 
ATOM   586  O  OD2   . ASP A 1 73  ? -19.164 -22.672 10.099  1.00 92.92  ? 73  ASP A OD2   1 
ATOM   587  N  N     . ASN A 1 74  ? -14.203 -23.301 9.627   1.00 64.20  ? 74  ASN A N     1 
ATOM   588  C  CA    . ASN A 1 74  ? -13.389 -22.889 8.483   1.00 62.78  ? 74  ASN A CA    1 
ATOM   589  C  C     . ASN A 1 74  ? -12.341 -21.852 8.887   1.00 55.08  ? 74  ASN A C     1 
ATOM   590  O  O     . ASN A 1 74  ? -12.237 -20.776 8.297   1.00 56.27  ? 74  ASN A O     1 
ATOM   591  C  CB    . ASN A 1 74  ? -14.274 -22.363 7.349   1.00 61.52  ? 74  ASN A CB    1 
ATOM   592  C  CG    . ASN A 1 74  ? -13.483 -22.021 6.097   1.00 69.08  ? 74  ASN A CG    1 
ATOM   593  O  OD1   . ASN A 1 74  ? -12.379 -22.529 5.883   1.00 68.58  ? 74  ASN A OD1   1 
ATOM   594  N  ND2   . ASN A 1 74  ? -14.045 -21.155 5.263   1.00 70.04  ? 74  ASN A ND2   1 
ATOM   595  N  N     . CYS A 1 75  ? -11.552 -22.187 9.902   1.00 57.22  ? 75  CYS A N     1 
ATOM   596  C  CA    . CYS A 1 75  ? -10.459 -21.341 10.360  1.00 55.49  ? 75  CYS A CA    1 
ATOM   597  C  C     . CYS A 1 75  ? -9.151  -22.109 10.264  1.00 59.44  ? 75  CYS A C     1 
ATOM   598  O  O     . CYS A 1 75  ? -9.107  -23.317 10.522  1.00 58.02  ? 75  CYS A O     1 
ATOM   599  C  CB    . CYS A 1 75  ? -10.686 -20.861 11.793  1.00 56.74  ? 75  CYS A CB    1 
ATOM   600  S  SG    . CYS A 1 75  ? -12.061 -19.706 11.955  1.00 60.08  ? 75  CYS A SG    1 
ATOM   601  N  N     . TRP A 1 76  ? -8.087  -21.400 9.898   1.00 55.87  ? 76  TRP A N     1 
ATOM   602  C  CA    . TRP A 1 76  ? -6.817  -22.019 9.564   1.00 52.95  ? 76  TRP A CA    1 
ATOM   603  C  C     . TRP A 1 76  ? -5.676  -21.290 10.254  1.00 54.62  ? 76  TRP A C     1 
ATOM   604  O  O     . TRP A 1 76  ? -5.720  -20.073 10.447  1.00 63.19  ? 76  TRP A O     1 
ATOM   605  C  CB    . TRP A 1 76  ? -6.611  -22.017 8.053   1.00 51.68  ? 76  TRP A CB    1 
ATOM   606  C  CG    . TRP A 1 76  ? -7.786  -22.590 7.346   1.00 56.00  ? 76  TRP A CG    1 
ATOM   607  C  CD1   . TRP A 1 76  ? -8.918  -21.930 6.969   1.00 54.23  ? 76  TRP A CD1   1 
ATOM   608  C  CD2   . TRP A 1 76  ? -7.966  -23.954 6.956   1.00 56.11  ? 76  TRP A CD2   1 
ATOM   609  N  NE1   . TRP A 1 76  ? -9.789  -22.797 6.356   1.00 55.91  ? 76  TRP A NE1   1 
ATOM   610  C  CE2   . TRP A 1 76  ? -9.227  -24.046 6.334   1.00 55.93  ? 76  TRP A CE2   1 
ATOM   611  C  CE3   . TRP A 1 76  ? -7.181  -25.105 7.064   1.00 59.35  ? 76  TRP A CE3   1 
ATOM   612  C  CZ2   . TRP A 1 76  ? -9.720  -25.244 5.823   1.00 62.32  ? 76  TRP A CZ2   1 
ATOM   613  C  CZ3   . TRP A 1 76  ? -7.671  -26.293 6.554   1.00 62.79  ? 76  TRP A CZ3   1 
ATOM   614  C  CH2   . TRP A 1 76  ? -8.930  -26.354 5.943   1.00 62.43  ? 76  TRP A CH2   1 
ATOM   615  N  N     . LEU A 1 77  ? -4.658  -22.052 10.633  1.00 58.52  ? 77  LEU A N     1 
ATOM   616  C  CA    . LEU A 1 77  ? -3.436  -21.506 11.199  1.00 57.72  ? 77  LEU A CA    1 
ATOM   617  C  C     . LEU A 1 77  ? -2.304  -21.617 10.186  1.00 62.99  ? 77  LEU A C     1 
ATOM   618  O  O     . LEU A 1 77  ? -2.256  -22.551 9.380   1.00 63.22  ? 77  LEU A O     1 
ATOM   619  C  CB    . LEU A 1 77  ? -3.050  -22.228 12.491  1.00 55.16  ? 77  LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 77  ? -1.755  -21.750 13.149  1.00 55.49  ? 77  LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 77  ? -1.855  -20.277 13.489  1.00 66.16  ? 77  LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 77  ? -1.445  -22.566 14.393  1.00 69.18  ? 77  LEU A CD2   1 
ATOM   623  N  N     . ALA A 1 78  ? -1.396  -20.646 10.231  1.00 64.98  ? 78  ALA A N     1 
ATOM   624  C  CA    . ALA A 1 78  ? -0.236  -20.619 9.348   1.00 62.04  ? 78  ALA A CA    1 
ATOM   625  C  C     . ALA A 1 78  ? 0.938   -20.043 10.120  1.00 61.62  ? 78  ALA A C     1 
ATOM   626  O  O     . ALA A 1 78  ? 0.887   -18.890 10.559  1.00 71.60  ? 78  ALA A O     1 
ATOM   627  C  CB    . ALA A 1 78  ? -0.511  -19.795 8.088   1.00 54.36  ? 78  ALA A CB    1 
ATOM   628  N  N     . LEU A 1 79  ? 1.983   -20.844 10.295  1.00 66.51  ? 79  LEU A N     1 
ATOM   629  C  CA    . LEU A 1 79  ? 3.190   -20.422 10.990  1.00 67.89  ? 79  LEU A CA    1 
ATOM   630  C  C     . LEU A 1 79  ? 4.258   -20.069 9.966   1.00 74.19  ? 79  LEU A C     1 
ATOM   631  O  O     . LEU A 1 79  ? 4.570   -20.875 9.083   1.00 76.40  ? 79  LEU A O     1 
ATOM   632  C  CB    . LEU A 1 79  ? 3.691   -21.521 11.926  1.00 74.37  ? 79  LEU A CB    1 
ATOM   633  C  CG    . LEU A 1 79  ? 2.629   -22.091 12.868  1.00 70.65  ? 79  LEU A CG    1 
ATOM   634  C  CD1   . LEU A 1 79  ? 3.271   -22.962 13.932  1.00 73.72  ? 79  LEU A CD1   1 
ATOM   635  C  CD2   . LEU A 1 79  ? 1.808   -20.973 13.496  1.00 68.90  ? 79  LEU A CD2   1 
ATOM   636  N  N     . THR A 1 80  ? 4.811   -18.869 10.084  1.00 65.51  ? 80  THR A N     1 
ATOM   637  C  CA    . THR A 1 80  ? 5.792   -18.372 9.135   1.00 68.65  ? 80  THR A CA    1 
ATOM   638  C  C     . THR A 1 80  ? 7.207   -18.601 9.652   1.00 78.47  ? 80  THR A C     1 
ATOM   639  O  O     . THR A 1 80  ? 7.430   -18.968 10.809  1.00 73.16  ? 80  THR A O     1 
ATOM   640  C  CB    . THR A 1 80  ? 5.570   -16.882 8.857   1.00 71.33  ? 80  THR A CB    1 
ATOM   641  O  OG1   . THR A 1 80  ? 5.871   -16.124 10.037  1.00 71.66  ? 80  THR A OG1   1 
ATOM   642  C  CG2   . THR A 1 80  ? 4.126   -16.625 8.449   1.00 71.55  ? 80  THR A CG2   1 
ATOM   643  N  N     . ASP A 1 81  ? 8.169   -18.388 8.762   1.00 80.92  ? 81  ASP A N     1 
ATOM   644  C  CA    . ASP A 1 81  ? 9.565   -18.392 9.162   1.00 79.10  ? 81  ASP A CA    1 
ATOM   645  C  C     . ASP A 1 81  ? 9.802   -17.265 10.165  1.00 75.13  ? 81  ASP A C     1 
ATOM   646  O  O     . ASP A 1 81  ? 9.304   -16.150 9.972   1.00 73.70  ? 81  ASP A O     1 
ATOM   647  C  CB    . ASP A 1 81  ? 10.466  -18.221 7.936   1.00 76.40  ? 81  ASP A CB    1 
ATOM   648  C  CG    . ASP A 1 81  ? 11.935  -18.420 8.251   1.00 80.01  ? 81  ASP A CG    1 
ATOM   649  O  OD1   . ASP A 1 81  ? 12.434  -17.803 9.216   1.00 81.91  ? 81  ASP A OD1   1 
ATOM   650  O  OD2   . ASP A 1 81  ? 12.592  -19.198 7.529   1.00 77.97  ? 81  ASP A OD2   1 
ATOM   651  N  N     . PRO A 1 82  ? 10.536  -17.519 11.251  1.00 77.04  ? 82  PRO A N     1 
ATOM   652  C  CA    . PRO A 1 82  ? 10.754  -16.457 12.247  1.00 77.78  ? 82  PRO A CA    1 
ATOM   653  C  C     . PRO A 1 82  ? 11.429  -15.218 11.682  1.00 79.50  ? 82  PRO A C     1 
ATOM   654  O  O     . PRO A 1 82  ? 11.338  -14.148 12.299  1.00 78.88  ? 82  PRO A O     1 
ATOM   655  C  CB    . PRO A 1 82  ? 11.625  -17.141 13.311  1.00 79.95  ? 82  PRO A CB    1 
ATOM   656  C  CG    . PRO A 1 82  ? 12.212  -18.338 12.628  1.00 78.04  ? 82  PRO A CG    1 
ATOM   657  C  CD    . PRO A 1 82  ? 11.185  -18.782 11.635  1.00 80.11  ? 82  PRO A CD    1 
ATOM   658  N  N     . ARG A 1 83  ? 12.097  -15.322 10.531  1.00 80.71  ? 83  ARG A N     1 
ATOM   659  C  CA    . ARG A 1 83  ? 12.721  -14.160 9.910   1.00 76.85  ? 83  ARG A CA    1 
ATOM   660  C  C     . ARG A 1 83  ? 11.743  -13.337 9.084   1.00 76.65  ? 83  ARG A C     1 
ATOM   661  O  O     . ARG A 1 83  ? 12.013  -12.160 8.821   1.00 80.27  ? 83  ARG A O     1 
ATOM   662  C  CB    . ARG A 1 83  ? 13.887  -14.602 9.022   1.00 77.69  ? 83  ARG A CB    1 
ATOM   663  C  CG    . ARG A 1 83  ? 14.961  -15.386 9.752   1.00 84.84  ? 83  ARG A CG    1 
ATOM   664  C  CD    . ARG A 1 83  ? 15.954  -15.999 8.778   1.00 91.53  ? 83  ARG A CD    1 
ATOM   665  N  NE    . ARG A 1 83  ? 15.308  -16.922 7.852   1.00 92.11  ? 83  ARG A NE    1 
ATOM   666  C  CZ    . ARG A 1 83  ? 15.947  -17.643 6.941   1.00 95.50  ? 83  ARG A CZ    1 
ATOM   667  N  NH1   . ARG A 1 83  ? 17.262  -17.580 6.806   1.00 104.14 ? 83  ARG A NH1   1 
ATOM   668  N  NH2   . ARG A 1 83  ? 15.249  -18.449 6.146   1.00 91.41  ? 83  ARG A NH2   1 
ATOM   669  N  N     . ASP A 1 84  ? 10.621  -13.920 8.679   1.00 78.72  ? 84  ASP A N     1 
ATOM   670  C  CA    . ASP A 1 84  ? 9.637   -13.267 7.816   1.00 74.16  ? 84  ASP A CA    1 
ATOM   671  C  C     . ASP A 1 84  ? 8.323   -13.139 8.585   1.00 72.32  ? 84  ASP A C     1 
ATOM   672  O  O     . ASP A 1 84  ? 7.352   -13.845 8.304   1.00 70.42  ? 84  ASP A O     1 
ATOM   673  C  CB    . ASP A 1 84  ? 9.459   -14.065 6.517   1.00 65.33  ? 84  ASP A CB    1 
ATOM   674  C  CG    . ASP A 1 84  ? 8.491   -13.412 5.558   1.00 65.95  ? 84  ASP A CG    1 
ATOM   675  O  OD1   . ASP A 1 84  ? 8.227   -12.200 5.711   1.00 68.74  ? 84  ASP A OD1   1 
ATOM   676  O  OD2   . ASP A 1 84  ? 7.989   -14.112 4.654   1.00 64.38  ? 84  ASP A OD2   1 
ATOM   677  N  N     . VAL A 1 85  ? 8.288   -12.221 9.549   1.00 68.84  ? 85  VAL A N     1 
ATOM   678  C  CA    . VAL A 1 85  ? 7.179   -12.174 10.495  1.00 70.55  ? 85  VAL A CA    1 
ATOM   679  C  C     . VAL A 1 85  ? 6.637   -10.762 10.661  1.00 73.20  ? 85  VAL A C     1 
ATOM   680  O  O     . VAL A 1 85  ? 6.002   -10.454 11.676  1.00 74.35  ? 85  VAL A O     1 
ATOM   681  C  CB    . VAL A 1 85  ? 7.611   -12.743 11.858  1.00 75.16  ? 85  VAL A CB    1 
ATOM   682  C  CG1   . VAL A 1 85  ? 7.897   -14.234 11.747  1.00 73.72  ? 85  VAL A CG1   1 
ATOM   683  C  CG2   . VAL A 1 85  ? 8.834   -11.996 12.371  1.00 73.95  ? 85  VAL A CG2   1 
ATOM   684  N  N     . ALA A 1 86  ? 6.872   -9.893  9.678   1.00 73.66  ? 86  ALA A N     1 
ATOM   685  C  CA    . ALA A 1 86  ? 6.337   -8.538  9.765   1.00 73.79  ? 86  ALA A CA    1 
ATOM   686  C  C     . ALA A 1 86  ? 6.687   -7.675  8.559   1.00 76.54  ? 86  ALA A C     1 
ATOM   687  O  O     . ALA A 1 86  ? 7.389   -8.113  7.641   1.00 72.09  ? 86  ALA A O     1 
ATOM   688  C  CB    . ALA A 1 86  ? 6.832   -7.852  11.041  1.00 73.18  ? 86  ALA A CB    1 
ATOM   689  N  N     . ARG A 1 87  ? 6.195   -6.440  8.570   1.00 78.06  ? 87  ARG A N     1 
ATOM   690  C  CA    . ARG A 1 87  ? 6.436   -5.483  7.498   1.00 72.71  ? 87  ARG A CA    1 
ATOM   691  C  C     . ARG A 1 87  ? 7.835   -4.894  7.649   1.00 78.58  ? 87  ARG A C     1 
ATOM   692  O  O     . ARG A 1 87  ? 8.169   -4.337  8.701   1.00 85.62  ? 87  ARG A O     1 
ATOM   693  C  CB    . ARG A 1 87  ? 5.364   -4.396  7.546   1.00 71.12  ? 87  ARG A CB    1 
ATOM   694  C  CG    . ARG A 1 87  ? 5.455   -3.328  6.481   1.00 67.82  ? 87  ARG A CG    1 
ATOM   695  C  CD    . ARG A 1 87  ? 4.213   -2.445  6.507   1.00 61.02  ? 87  ARG A CD    1 
ATOM   696  N  NE    . ARG A 1 87  ? 3.871   -2.011  7.858   1.00 64.71  ? 87  ARG A NE    1 
ATOM   697  C  CZ    . ARG A 1 87  ? 4.398   -0.956  8.466   1.00 71.66  ? 87  ARG A CZ    1 
ATOM   698  N  NH1   . ARG A 1 87  ? 5.316   -0.206  7.879   1.00 65.25  ? 87  ARG A NH1   1 
ATOM   699  N  NH2   . ARG A 1 87  ? 3.996   -0.648  9.696   1.00 70.26  ? 87  ARG A NH2   1 
ATOM   700  N  N     . ILE A 1 88  ? 8.654   -5.021  6.606   1.00 83.13  ? 88  ILE A N     1 
ATOM   701  C  CA    . ILE A 1 88  ? 10.035  -4.545  6.632   1.00 82.39  ? 88  ILE A CA    1 
ATOM   702  C  C     . ILE A 1 88  ? 10.035  -3.112  6.110   1.00 82.26  ? 88  ILE A C     1 
ATOM   703  O  O     . ILE A 1 88  ? 9.940   -2.873  4.905   1.00 80.16  ? 88  ILE A O     1 
ATOM   704  C  CB    . ILE A 1 88  ? 10.963  -5.441  5.812   1.00 76.68  ? 88  ILE A CB    1 
ATOM   705  C  CG1   . ILE A 1 88  ? 10.808  -6.901  6.235   1.00 78.59  ? 88  ILE A CG1   1 
ATOM   706  C  CG2   . ILE A 1 88  ? 12.405  -4.997  5.981   1.00 81.79  ? 88  ILE A CG2   1 
ATOM   707  C  CD1   . ILE A 1 88  ? 11.649  -7.862  5.423   1.00 78.09  ? 88  ILE A CD1   1 
ATOM   708  N  N     . GLU A 1 89  ? 10.153  -2.150  7.027   1.00 90.29  ? 89  GLU A N     1 
ATOM   709  C  CA    . GLU A 1 89  ? 10.144  -0.746  6.632   1.00 84.99  ? 89  GLU A CA    1 
ATOM   710  C  C     . GLU A 1 89  ? 11.458  -0.335  5.980   1.00 88.20  ? 89  GLU A C     1 
ATOM   711  O  O     . GLU A 1 89  ? 11.472  0.564   5.131   1.00 87.03  ? 89  GLU A O     1 
ATOM   712  C  CB    . GLU A 1 89  ? 9.850   0.132   7.849   1.00 90.74  ? 89  GLU A CB    1 
ATOM   713  C  CG    . GLU A 1 89  ? 9.867   1.629   7.574   1.00 95.41  ? 89  GLU A CG    1 
ATOM   714  C  CD    . GLU A 1 89  ? 9.394   2.444   8.767   1.00 97.25  ? 89  GLU A CD    1 
ATOM   715  O  OE1   . GLU A 1 89  ? 8.583   1.921   9.562   1.00 95.94  ? 89  GLU A OE1   1 
ATOM   716  O  OE2   . GLU A 1 89  ? 9.834   3.604   8.915   1.00 90.34  ? 89  GLU A OE2   1 
ATOM   717  N  N     . SER A 1 90  ? 12.564  -0.983  6.350   1.00 91.16  ? 90  SER A N     1 
ATOM   718  C  CA    . SER A 1 90  ? 13.873  -0.598  5.837   1.00 86.13  ? 90  SER A CA    1 
ATOM   719  C  C     . SER A 1 90  ? 14.132  -1.104  4.424   1.00 81.79  ? 90  SER A C     1 
ATOM   720  O  O     . SER A 1 90  ? 15.030  -0.585  3.752   1.00 82.64  ? 90  SER A O     1 
ATOM   721  C  CB    . SER A 1 90  ? 14.971  -1.102  6.776   1.00 85.47  ? 90  SER A CB    1 
ATOM   722  O  OG    . SER A 1 90  ? 14.791  -2.474  7.084   1.00 89.21  ? 90  SER A OG    1 
ATOM   723  N  N     . LYS A 1 91  ? 13.375  -2.096  3.957   1.00 78.75  ? 91  LYS A N     1 
ATOM   724  C  CA    . LYS A 1 91  ? 13.541  -2.640  2.616   1.00 69.58  ? 91  LYS A CA    1 
ATOM   725  C  C     . LYS A 1 91  ? 12.446  -2.181  1.660   1.00 64.46  ? 91  LYS A C     1 
ATOM   726  O  O     . LYS A 1 91  ? 12.281  -2.770  0.587   1.00 60.17  ? 91  LYS A O     1 
ATOM   727  C  CB    . LYS A 1 91  ? 13.591  -4.167  2.669   1.00 70.58  ? 91  LYS A CB    1 
ATOM   728  C  CG    . LYS A 1 91  ? 14.849  -4.723  3.314   1.00 72.96  ? 91  LYS A CG    1 
ATOM   729  C  CD    . LYS A 1 91  ? 14.856  -6.242  3.274   1.00 78.91  ? 91  LYS A CD    1 
ATOM   730  C  CE    . LYS A 1 91  ? 16.199  -6.809  3.714   1.00 86.96  ? 91  LYS A CE    1 
ATOM   731  N  NZ    . LYS A 1 91  ? 16.524  -6.454  5.123   1.00 97.09  ? 91  LYS A NZ    1 
ATOM   732  N  N     . THR A 1 92  ? 11.691  -1.153  2.029   1.00 63.67  ? 92  THR A N     1 
ATOM   733  C  CA    . THR A 1 92  ? 10.677  -0.573  1.161   1.00 64.96  ? 92  THR A CA    1 
ATOM   734  C  C     . THR A 1 92  ? 11.246  0.673   0.497   1.00 65.17  ? 92  THR A C     1 
ATOM   735  O  O     . THR A 1 92  ? 11.891  1.496   1.152   1.00 66.46  ? 92  THR A O     1 
ATOM   736  C  CB    . THR A 1 92  ? 9.416   -0.218  1.951   1.00 62.84  ? 92  THR A CB    1 
ATOM   737  O  OG1   . THR A 1 92  ? 9.061   -1.315  2.797   1.00 67.62  ? 92  THR A OG1   1 
ATOM   738  C  CG2   . THR A 1 92  ? 8.261   0.075   1.009   1.00 61.25  ? 92  THR A CG2   1 
ATOM   739  N  N     . VAL A 1 93  ? 11.013  0.804   -0.808  1.00 59.61  ? 93  VAL A N     1 
ATOM   740  C  CA    . VAL A 1 93  ? 11.611  1.876   -1.594  1.00 59.88  ? 93  VAL A CA    1 
ATOM   741  C  C     . VAL A 1 93  ? 10.623  2.357   -2.646  1.00 59.37  ? 93  VAL A C     1 
ATOM   742  O  O     . VAL A 1 93  ? 9.769   1.601   -3.121  1.00 56.44  ? 93  VAL A O     1 
ATOM   743  C  CB    . VAL A 1 93  ? 12.927  1.428   -2.265  1.00 60.53  ? 93  VAL A CB    1 
ATOM   744  C  CG1   . VAL A 1 93  ? 13.946  1.030   -1.214  1.00 65.90  ? 93  VAL A CG1   1 
ATOM   745  C  CG2   . VAL A 1 93  ? 12.663  0.282   -3.228  1.00 59.46  ? 93  VAL A CG2   1 
ATOM   746  N  N     . ILE A 1 94  ? 10.749  3.632   -3.005  1.00 58.22  ? 94  ILE A N     1 
ATOM   747  C  CA    . ILE A 1 94  ? 9.956   4.254   -4.058  1.00 60.30  ? 94  ILE A CA    1 
ATOM   748  C  C     . ILE A 1 94  ? 10.913  4.739   -5.136  1.00 55.74  ? 94  ILE A C     1 
ATOM   749  O  O     . ILE A 1 94  ? 11.909  5.408   -4.834  1.00 61.41  ? 94  ILE A O     1 
ATOM   750  C  CB    . ILE A 1 94  ? 9.102   5.416   -3.519  1.00 56.99  ? 94  ILE A CB    1 
ATOM   751  C  CG1   . ILE A 1 94  ? 8.183   4.923   -2.398  1.00 53.22  ? 94  ILE A CG1   1 
ATOM   752  C  CG2   . ILE A 1 94  ? 8.296   6.049   -4.647  1.00 52.84  ? 94  ILE A CG2   1 
ATOM   753  C  CD1   . ILE A 1 94  ? 7.206   5.963   -1.906  1.00 57.03  ? 94  ILE A CD1   1 
ATOM   754  N  N     . ILE A 1 95  ? 10.618  4.399   -6.386  1.00 56.13  ? 95  ILE A N     1 
ATOM   755  C  CA    . ILE A 1 95  ? 11.483  4.725   -7.514  1.00 60.03  ? 95  ILE A CA    1 
ATOM   756  C  C     . ILE A 1 95  ? 10.870  5.896   -8.268  1.00 58.80  ? 95  ILE A C     1 
ATOM   757  O  O     . ILE A 1 95  ? 9.766   5.785   -8.814  1.00 59.09  ? 95  ILE A O     1 
ATOM   758  C  CB    . ILE A 1 95  ? 11.686  3.517   -8.443  1.00 63.08  ? 95  ILE A CB    1 
ATOM   759  C  CG1   . ILE A 1 95  ? 12.521  2.435   -7.755  1.00 62.78  ? 95  ILE A CG1   1 
ATOM   760  C  CG2   . ILE A 1 95  ? 12.344  3.949   -9.747  1.00 62.92  ? 95  ILE A CG2   1 
ATOM   761  C  CD1   . ILE A 1 95  ? 11.757  1.623   -6.750  1.00 60.08  ? 95  ILE A CD1   1 
ATOM   762  N  N     . THR A 1 96  ? 11.586  7.016   -8.295  1.00 59.21  ? 96  THR A N     1 
ATOM   763  C  CA    . THR A 1 96  ? 11.194  8.178   -9.077  1.00 66.80  ? 96  THR A CA    1 
ATOM   764  C  C     . THR A 1 96  ? 12.425  8.742   -9.766  1.00 68.31  ? 96  THR A C     1 
ATOM   765  O  O     . THR A 1 96  ? 13.534  8.693   -9.226  1.00 65.52  ? 96  THR A O     1 
ATOM   766  C  CB    . THR A 1 96  ? 10.545  9.271   -8.215  1.00 60.47  ? 96  THR A CB    1 
ATOM   767  O  OG1   . THR A 1 96  ? 11.481  9.716   -7.226  1.00 58.38  ? 96  THR A OG1   1 
ATOM   768  C  CG2   . THR A 1 96  ? 9.299   8.743   -7.525  1.00 59.84  ? 96  THR A CG2   1 
ATOM   769  N  N     . GLN A 1 97  ? 12.221  9.270   -10.973 1.00 70.42  ? 97  GLN A N     1 
ATOM   770  C  CA    . GLN A 1 97  ? 13.313  9.927   -11.682 1.00 74.49  ? 97  GLN A CA    1 
ATOM   771  C  C     . GLN A 1 97  ? 14.004  10.944  -10.783 1.00 72.78  ? 97  GLN A C     1 
ATOM   772  O  O     . GLN A 1 97  ? 15.236  10.978  -10.692 1.00 72.42  ? 97  GLN A O     1 
ATOM   773  C  CB    . GLN A 1 97  ? 12.784  10.596  -12.952 1.00 84.07  ? 97  GLN A CB    1 
ATOM   774  C  CG    . GLN A 1 97  ? 13.844  11.332  -13.753 1.00 97.35  ? 97  GLN A CG    1 
ATOM   775  C  CD    . GLN A 1 97  ? 13.262  12.080  -14.935 1.00 110.22 ? 97  GLN A CD    1 
ATOM   776  O  OE1   . GLN A 1 97  ? 12.151  11.791  -15.379 1.00 114.89 ? 97  GLN A OE1   1 
ATOM   777  N  NE2   . GLN A 1 97  ? 14.008  13.053  -15.447 1.00 108.71 ? 97  GLN A NE2   1 
ATOM   778  N  N     . GLU A 1 98  ? 13.219  11.770  -10.097 1.00 70.97  ? 98  GLU A N     1 
ATOM   779  C  CA    . GLU A 1 98  ? 13.729  12.797  -9.199  1.00 73.00  ? 98  GLU A CA    1 
ATOM   780  C  C     . GLU A 1 98  ? 13.459  12.385  -7.758  1.00 66.28  ? 98  GLU A C     1 
ATOM   781  O  O     . GLU A 1 98  ? 12.321  12.060  -7.404  1.00 64.44  ? 98  GLU A O     1 
ATOM   782  C  CB    . GLU A 1 98  ? 13.077  14.151  -9.493  1.00 82.42  ? 98  GLU A CB    1 
ATOM   783  C  CG    . GLU A 1 98  ? 13.195  14.604  -10.945 1.00 92.80  ? 98  GLU A CG    1 
ATOM   784  C  CD    . GLU A 1 98  ? 14.508  15.300  -11.240 1.00 96.99  ? 98  GLU A CD    1 
ATOM   785  O  OE1   . GLU A 1 98  ? 14.998  16.040  -10.360 1.00 100.02 ? 98  GLU A OE1   1 
ATOM   786  O  OE2   . GLU A 1 98  ? 15.050  15.108  -12.350 1.00 102.24 ? 98  GLU A OE2   1 
ATOM   787  N  N     . GLN A 1 99  ? 14.506  12.402  -6.930  1.00 61.26  ? 99  GLN A N     1 
ATOM   788  C  CA    . GLN A 1 99  ? 14.337  12.047  -5.524  1.00 61.16  ? 99  GLN A CA    1 
ATOM   789  C  C     . GLN A 1 99  ? 13.372  12.995  -4.822  1.00 67.51  ? 99  GLN A C     1 
ATOM   790  O  O     . GLN A 1 99  ? 12.611  12.579  -3.940  1.00 64.27  ? 99  GLN A O     1 
ATOM   791  C  CB    . GLN A 1 99  ? 15.691  12.045  -4.818  1.00 60.89  ? 99  GLN A CB    1 
ATOM   792  C  CG    . GLN A 1 99  ? 15.598  11.792  -3.321  1.00 62.21  ? 99  GLN A CG    1 
ATOM   793  C  CD    . GLN A 1 99  ? 16.943  11.861  -2.629  1.00 63.20  ? 99  GLN A CD    1 
ATOM   794  O  OE1   . GLN A 1 99  ? 17.916  12.370  -3.184  1.00 67.48  ? 99  GLN A OE1   1 
ATOM   795  N  NE2   . GLN A 1 99  ? 17.005  11.344  -1.407  1.00 66.67  ? 99  GLN A NE2   1 
ATOM   796  N  N     . ARG A 1 100 ? 13.391  14.276  -5.199  1.00 65.57  ? 100 ARG A N     1 
ATOM   797  C  CA    . ARG A 1 100 ? 12.530  15.259  -4.551  1.00 62.19  ? 100 ARG A CA    1 
ATOM   798  C  C     . ARG A 1 100 ? 11.056  14.909  -4.708  1.00 62.64  ? 100 ARG A C     1 
ATOM   799  O  O     . ARG A 1 100 ? 10.231  15.323  -3.886  1.00 65.28  ? 100 ARG A O     1 
ATOM   800  C  CB    . ARG A 1 100 ? 12.814  16.650  -5.121  1.00 65.46  ? 100 ARG A CB    1 
ATOM   801  C  CG    . ARG A 1 100 ? 12.270  17.798  -4.290  1.00 69.68  ? 100 ARG A CG    1 
ATOM   802  C  CD    . ARG A 1 100 ? 12.681  19.132  -4.891  1.00 79.84  ? 100 ARG A CD    1 
ATOM   803  N  NE    . ARG A 1 100 ? 12.455  20.244  -3.977  1.00 77.36  ? 100 ARG A NE    1 
ATOM   804  C  CZ    . ARG A 1 100 ? 12.817  21.496  -4.219  1.00 88.00  ? 100 ARG A CZ    1 
ATOM   805  N  NH1   . ARG A 1 100 ? 13.421  21.836  -5.347  1.00 93.35  ? 100 ARG A NH1   1 
ATOM   806  N  NH2   . ARG A 1 100 ? 12.570  22.431  -3.306  1.00 95.44  ? 100 ARG A NH2   1 
ATOM   807  N  N     . ASP A 1 101 ? 10.706  14.155  -5.754  1.00 62.92  ? 101 ASP A N     1 
ATOM   808  C  CA    . ASP A 1 101 ? 9.319   13.738  -5.932  1.00 61.54  ? 101 ASP A CA    1 
ATOM   809  C  C     . ASP A 1 101 ? 8.865   12.807  -4.819  1.00 58.65  ? 101 ASP A C     1 
ATOM   810  O  O     . ASP A 1 101 ? 7.668   12.745  -4.516  1.00 62.48  ? 101 ASP A O     1 
ATOM   811  C  CB    . ASP A 1 101 ? 9.140   13.048  -7.284  1.00 62.30  ? 101 ASP A CB    1 
ATOM   812  C  CG    . ASP A 1 101 ? 9.440   13.962  -8.449  1.00 80.13  ? 101 ASP A CG    1 
ATOM   813  O  OD1   . ASP A 1 101 ? 9.177   15.178  -8.336  1.00 90.45  ? 101 ASP A OD1   1 
ATOM   814  O  OD2   . ASP A 1 101 ? 9.939   13.460  -9.480  1.00 85.63  ? 101 ASP A OD2   1 
ATOM   815  N  N     . THR A 1 102 ? 9.796   12.079  -4.203  1.00 55.59  ? 102 THR A N     1 
ATOM   816  C  CA    . THR A 1 102 ? 9.474   11.063  -3.208  1.00 65.72  ? 102 THR A CA    1 
ATOM   817  C  C     . THR A 1 102 ? 9.592   11.574  -1.778  1.00 61.72  ? 102 THR A C     1 
ATOM   818  O  O     . THR A 1 102 ? 8.666   11.404  -0.981  1.00 60.00  ? 102 THR A O     1 
ATOM   819  C  CB    . THR A 1 102 ? 10.383  9.843   -3.399  1.00 60.87  ? 102 THR A CB    1 
ATOM   820  O  OG1   . THR A 1 102 ? 10.115  9.243   -4.672  1.00 65.01  ? 102 THR A OG1   1 
ATOM   821  C  CG2   . THR A 1 102 ? 10.149  8.826   -2.298  1.00 50.65  ? 102 THR A CG2   1 
ATOM   822  N  N     . VAL A 1 103 ? 10.720  12.189  -1.432  1.00 57.34  ? 103 VAL A N     1 
ATOM   823  C  CA    . VAL A 1 103 ? 10.931  12.700  -0.078  1.00 59.95  ? 103 VAL A CA    1 
ATOM   824  C  C     . VAL A 1 103 ? 11.572  14.068  -0.154  1.00 68.58  ? 103 VAL A C     1 
ATOM   825  O  O     . VAL A 1 103 ? 12.361  14.366  -1.062  1.00 74.28  ? 103 VAL A O     1 
ATOM   826  C  CB    . VAL A 1 103 ? 11.826  11.763  0.758   1.00 59.91  ? 103 VAL A CB    1 
ATOM   827  C  CG1   . VAL A 1 103 ? 11.260  10.352  0.768   1.00 58.75  ? 103 VAL A CG1   1 
ATOM   828  C  CG2   . VAL A 1 103 ? 13.255  11.784  0.225   1.00 56.46  ? 103 VAL A CG2   1 
ATOM   829  N  N     . PRO A 1 104 ? 11.243  14.936  0.798   1.00 67.29  ? 104 PRO A N     1 
ATOM   830  C  CA    . PRO A 1 104 ? 11.951  16.215  0.886   1.00 65.48  ? 104 PRO A CA    1 
ATOM   831  C  C     . PRO A 1 104 ? 13.435  15.971  1.105   1.00 62.38  ? 104 PRO A C     1 
ATOM   832  O  O     . PRO A 1 104 ? 13.831  15.060  1.833   1.00 70.20  ? 104 PRO A O     1 
ATOM   833  C  CB    . PRO A 1 104 ? 11.301  16.904  2.092   1.00 65.45  ? 104 PRO A CB    1 
ATOM   834  C  CG    . PRO A 1 104 ? 9.985   16.200  2.285   1.00 63.62  ? 104 PRO A CG    1 
ATOM   835  C  CD    . PRO A 1 104 ? 10.222  14.787  1.849   1.00 62.00  ? 104 PRO A CD    1 
ATOM   836  N  N     . ILE A 1 105 ? 14.258  16.781  0.454   1.00 66.47  ? 105 ILE A N     1 
ATOM   837  C  CA    . ILE A 1 105 ? 15.702  16.647  0.604   1.00 68.66  ? 105 ILE A CA    1 
ATOM   838  C  C     . ILE A 1 105 ? 16.071  17.139  1.997   1.00 67.49  ? 105 ILE A C     1 
ATOM   839  O  O     . ILE A 1 105 ? 16.008  18.348  2.262   1.00 68.05  ? 105 ILE A O     1 
ATOM   840  C  CB    . ILE A 1 105 ? 16.455  17.415  -0.492  1.00 72.89  ? 105 ILE A CB    1 
ATOM   841  C  CG1   . ILE A 1 105 ? 15.984  16.955  -1.873  1.00 66.82  ? 105 ILE A CG1   1 
ATOM   842  C  CG2   . ILE A 1 105 ? 17.955  17.215  -0.344  1.00 71.68  ? 105 ILE A CG2   1 
ATOM   843  C  CD1   . ILE A 1 105 ? 16.194  15.482  -2.125  1.00 64.95  ? 105 ILE A CD1   1 
ATOM   844  N  N     . PRO A 1 106 ? 16.447  16.250  2.914   1.00 68.49  ? 106 PRO A N     1 
ATOM   845  C  CA    . PRO A 1 106 ? 16.754  16.691  4.280   1.00 71.82  ? 106 PRO A CA    1 
ATOM   846  C  C     . PRO A 1 106 ? 17.850  17.744  4.282   1.00 74.09  ? 106 PRO A C     1 
ATOM   847  O  O     . PRO A 1 106 ? 18.797  17.687  3.495   1.00 80.73  ? 106 PRO A O     1 
ATOM   848  C  CB    . PRO A 1 106 ? 17.210  15.403  4.977   1.00 68.61  ? 106 PRO A CB    1 
ATOM   849  C  CG    . PRO A 1 106 ? 16.685  14.292  4.128   1.00 69.95  ? 106 PRO A CG    1 
ATOM   850  C  CD    . PRO A 1 106 ? 16.681  14.810  2.728   1.00 65.13  ? 106 PRO A CD    1 
ATOM   851  N  N     . LYS A 1 107 ? 17.711  18.721  5.180   1.00 77.08  ? 107 LYS A N     1 
ATOM   852  C  CA    . LYS A 1 107 ? 18.738  19.749  5.303   1.00 85.63  ? 107 LYS A CA    1 
ATOM   853  C  C     . LYS A 1 107 ? 20.072  19.142  5.720   1.00 93.27  ? 107 LYS A C     1 
ATOM   854  O  O     . LYS A 1 107 ? 21.129  19.535  5.210   1.00 96.70  ? 107 LYS A O     1 
ATOM   855  C  CB    . LYS A 1 107 ? 18.295  20.821  6.299   1.00 85.63  ? 107 LYS A CB    1 
ATOM   856  C  CG    . LYS A 1 107 ? 19.363  21.858  6.599   1.00 89.16  ? 107 LYS A CG    1 
ATOM   857  C  CD    . LYS A 1 107 ? 18.831  22.989  7.466   1.00 95.09  ? 107 LYS A CD    1 
ATOM   858  C  CE    . LYS A 1 107 ? 17.811  23.832  6.717   1.00 98.00  ? 107 LYS A CE    1 
ATOM   859  N  NZ    . LYS A 1 107 ? 17.501  25.097  7.442   1.00 110.31 ? 107 LYS A NZ    1 
ATOM   860  N  N     . SER A 1 108 ? 20.044  18.178  6.638   1.00 83.58  ? 108 SER A N     1 
ATOM   861  C  CA    . SER A 1 108 ? 21.269  17.534  7.106   1.00 86.03  ? 108 SER A CA    1 
ATOM   862  C  C     . SER A 1 108 ? 20.892  16.181  7.693   1.00 87.95  ? 108 SER A C     1 
ATOM   863  O  O     . SER A 1 108 ? 20.188  16.120  8.706   1.00 85.04  ? 108 SER A O     1 
ATOM   864  C  CB    . SER A 1 108 ? 21.980  18.403  8.136   1.00 89.29  ? 108 SER A CB    1 
ATOM   865  O  OG    . SER A 1 108 ? 21.240  18.467  9.343   1.00 93.74  ? 108 SER A OG    1 
ATOM   866  N  N     . GLY A 1 109 ? 21.359  15.114  7.070   1.00 84.34  ? 109 GLY A N     1 
ATOM   867  C  CA    . GLY A 1 109 ? 21.062  13.773  7.522   1.00 75.33  ? 109 GLY A CA    1 
ATOM   868  C  C     . GLY A 1 109 ? 20.167  13.039  6.541   1.00 74.90  ? 109 GLY A C     1 
ATOM   869  O  O     . GLY A 1 109 ? 19.907  13.492  5.422   1.00 73.05  ? 109 GLY A O     1 
ATOM   870  N  N     . GLN A 1 110 ? 19.685  11.885  6.988   1.00 69.90  ? 110 GLN A N     1 
ATOM   871  C  CA    . GLN A 1 110 ? 18.901  10.998  6.143   1.00 68.70  ? 110 GLN A CA    1 
ATOM   872  C  C     . GLN A 1 110 ? 17.413  11.257  6.333   1.00 66.83  ? 110 GLN A C     1 
ATOM   873  O  O     . GLN A 1 110 ? 16.950  11.510  7.449   1.00 66.90  ? 110 GLN A O     1 
ATOM   874  C  CB    . GLN A 1 110 ? 19.227  9.539   6.461   1.00 72.68  ? 110 GLN A CB    1 
ATOM   875  C  CG    . GLN A 1 110 ? 19.168  8.616   5.260   1.00 76.63  ? 110 GLN A CG    1 
ATOM   876  C  CD    . GLN A 1 110 ? 19.851  7.292   5.523   1.00 81.48  ? 110 GLN A CD    1 
ATOM   877  O  OE1   . GLN A 1 110 ? 19.630  6.661   6.557   1.00 78.01  ? 110 GLN A OE1   1 
ATOM   878  N  NE2   . GLN A 1 110 ? 20.700  6.868   4.591   1.00 81.46  ? 110 GLN A NE2   1 
ATOM   879  N  N     . SER A 1 111 ? 16.668  11.188  5.234   1.00 62.66  ? 111 SER A N     1 
ATOM   880  C  CA    . SER A 1 111 ? 15.228  11.395  5.290   1.00 60.74  ? 111 SER A CA    1 
ATOM   881  C  C     . SER A 1 111 ? 14.542  10.239  6.007   1.00 65.07  ? 111 SER A C     1 
ATOM   882  O  O     . SER A 1 111 ? 14.886  9.070   5.809   1.00 68.30  ? 111 SER A O     1 
ATOM   883  C  CB    . SER A 1 111 ? 14.660  11.543  3.879   1.00 60.48  ? 111 SER A CB    1 
ATOM   884  O  OG    . SER A 1 111 ? 13.248  11.421  3.881   1.00 60.05  ? 111 SER A OG    1 
ATOM   885  N  N     . GLN A 1 112 ? 13.563  10.573  6.844   1.00 61.06  ? 112 GLN A N     1 
ATOM   886  C  CA    . GLN A 1 112 ? 12.746  9.586   7.536   1.00 59.13  ? 112 GLN A CA    1 
ATOM   887  C  C     . GLN A 1 112 ? 11.365  9.429   6.919   1.00 58.33  ? 112 GLN A C     1 
ATOM   888  O  O     . GLN A 1 112 ? 10.555  8.656   7.437   1.00 68.52  ? 112 GLN A O     1 
ATOM   889  C  CB    . GLN A 1 112 ? 12.586  9.961   9.013   1.00 60.92  ? 112 GLN A CB    1 
ATOM   890  C  CG    . GLN A 1 112 ? 13.876  10.218  9.758   1.00 62.52  ? 112 GLN A CG    1 
ATOM   891  C  CD    . GLN A 1 112 ? 13.651  10.339  11.250  1.00 64.51  ? 112 GLN A CD    1 
ATOM   892  O  OE1   . GLN A 1 112 ? 12.559  10.059  11.748  1.00 64.11  ? 112 GLN A OE1   1 
ATOM   893  N  NE2   . GLN A 1 112 ? 14.684  10.754  11.974  1.00 68.35  ? 112 GLN A NE2   1 
ATOM   894  N  N     . LEU A 1 113 ? 11.073  10.148  5.840   1.00 58.25  ? 113 LEU A N     1 
ATOM   895  C  CA    . LEU A 1 113 ? 9.736   10.197  5.269   1.00 60.23  ? 113 LEU A CA    1 
ATOM   896  C  C     . LEU A 1 113 ? 9.599   9.315   4.039   1.00 58.24  ? 113 LEU A C     1 
ATOM   897  O  O     . LEU A 1 113 ? 8.617   9.442   3.301   1.00 59.96  ? 113 LEU A O     1 
ATOM   898  C  CB    . LEU A 1 113 ? 9.373   11.645  4.931   1.00 66.39  ? 113 LEU A CB    1 
ATOM   899  C  CG    . LEU A 1 113 ? 9.747   12.645  6.028   1.00 57.02  ? 113 LEU A CG    1 
ATOM   900  C  CD1   . LEU A 1 113 ? 9.330   14.055  5.652   1.00 64.69  ? 113 LEU A CD1   1 
ATOM   901  C  CD2   . LEU A 1 113 ? 9.124   12.232  7.347   1.00 63.15  ? 113 LEU A CD2   1 
ATOM   902  N  N     . GLY A 1 114 ? 10.552  8.430   3.812   1.00 66.18  ? 114 GLY A N     1 
ATOM   903  C  CA    . GLY A 1 114 ? 10.548  7.565   2.649   1.00 59.46  ? 114 GLY A CA    1 
ATOM   904  C  C     . GLY A 1 114 ? 11.958  7.152   2.292   1.00 62.26  ? 114 GLY A C     1 
ATOM   905  O  O     . GLY A 1 114 ? 12.942  7.711   2.773   1.00 64.67  ? 114 GLY A O     1 
ATOM   906  N  N     . ARG A 1 115 ? 12.043  6.141   1.433   1.00 62.90  ? 115 ARG A N     1 
ATOM   907  C  CA    . ARG A 1 115 ? 13.321  5.641   0.939   1.00 65.45  ? 115 ARG A CA    1 
ATOM   908  C  C     . ARG A 1 115 ? 13.254  5.617   -0.581  1.00 63.28  ? 115 ARG A C     1 
ATOM   909  O  O     . ARG A 1 115 ? 12.468  4.861   -1.160  1.00 67.07  ? 115 ARG A O     1 
ATOM   910  C  CB    . ARG A 1 115 ? 13.634  4.254   1.501   1.00 71.98  ? 115 ARG A CB    1 
ATOM   911  C  CG    . ARG A 1 115 ? 15.043  3.771   1.191   1.00 86.57  ? 115 ARG A CG    1 
ATOM   912  C  CD    . ARG A 1 115 ? 15.348  2.456   1.889   1.00 95.23  ? 115 ARG A CD    1 
ATOM   913  N  NE    . ARG A 1 115 ? 15.193  2.557   3.335   1.00 107.17 ? 115 ARG A NE    1 
ATOM   914  C  CZ    . ARG A 1 115 ? 16.147  2.958   4.166   1.00 112.55 ? 115 ARG A CZ    1 
ATOM   915  N  NH1   . ARG A 1 115 ? 17.343  3.313   3.726   1.00 104.89 ? 115 ARG A NH1   1 
ATOM   916  N  NH2   . ARG A 1 115 ? 15.892  3.006   5.471   1.00 112.13 ? 115 ARG A NH2   1 
ATOM   917  N  N     . TRP A 1 116 ? 14.067  6.449   -1.221  1.00 64.51  ? 116 TRP A N     1 
ATOM   918  C  CA    . TRP A 1 116 ? 14.046  6.607   -2.665  1.00 64.94  ? 116 TRP A CA    1 
ATOM   919  C  C     . TRP A 1 116 ? 15.162  5.794   -3.307  1.00 67.46  ? 116 TRP A C     1 
ATOM   920  O  O     . TRP A 1 116 ? 16.244  5.629   -2.737  1.00 71.85  ? 116 TRP A O     1 
ATOM   921  C  CB    . TRP A 1 116 ? 14.186  8.083   -3.048  1.00 65.27  ? 116 TRP A CB    1 
ATOM   922  C  CG    . TRP A 1 116 ? 14.295  8.316   -4.523  1.00 63.26  ? 116 TRP A CG    1 
ATOM   923  C  CD1   . TRP A 1 116 ? 13.276  8.330   -5.428  1.00 64.35  ? 116 TRP A CD1   1 
ATOM   924  C  CD2   . TRP A 1 116 ? 15.492  8.574   -5.263  1.00 59.06  ? 116 TRP A CD2   1 
ATOM   925  N  NE1   . TRP A 1 116 ? 13.763  8.579   -6.687  1.00 59.61  ? 116 TRP A NE1   1 
ATOM   926  C  CE2   . TRP A 1 116 ? 15.122  8.732   -6.613  1.00 59.69  ? 116 TRP A CE2   1 
ATOM   927  C  CE3   . TRP A 1 116 ? 16.841  8.686   -4.915  1.00 61.38  ? 116 TRP A CE3   1 
ATOM   928  C  CZ2   . TRP A 1 116 ? 16.053  8.995   -7.616  1.00 63.45  ? 116 TRP A CZ2   1 
ATOM   929  C  CZ3   . TRP A 1 116 ? 17.765  8.948   -5.912  1.00 61.16  ? 116 TRP A CZ3   1 
ATOM   930  C  CH2   . TRP A 1 116 ? 17.367  9.100   -7.246  1.00 61.83  ? 116 TRP A CH2   1 
ATOM   931  N  N     . MET A 1 117 ? 14.885  5.284   -4.504  1.00 67.00  ? 117 MET A N     1 
ATOM   932  C  CA    . MET A 1 117 ? 15.859  4.518   -5.271  1.00 67.03  ? 117 MET A CA    1 
ATOM   933  C  C     . MET A 1 117 ? 15.694  4.847   -6.746  1.00 59.47  ? 117 MET A C     1 
ATOM   934  O  O     . MET A 1 117 ? 14.571  4.879   -7.255  1.00 63.42  ? 117 MET A O     1 
ATOM   935  C  CB    . MET A 1 117 ? 15.688  3.011   -5.041  1.00 64.08  ? 117 MET A CB    1 
ATOM   936  C  CG    . MET A 1 117 ? 16.683  2.152   -5.801  1.00 72.56  ? 117 MET A CG    1 
ATOM   937  S  SD    . MET A 1 117 ? 16.418  0.384   -5.556  1.00 65.68  ? 117 MET A SD    1 
ATOM   938  C  CE    . MET A 1 117 ? 16.644  0.246   -3.786  1.00 75.08  ? 117 MET A CE    1 
ATOM   939  N  N     . SER A 1 118 ? 16.809  5.091   -7.425  1.00 66.13  ? 118 SER A N     1 
ATOM   940  C  CA    . SER A 1 118 ? 16.760  5.413   -8.842  1.00 75.56  ? 118 SER A CA    1 
ATOM   941  C  C     . SER A 1 118 ? 16.317  4.200   -9.656  1.00 69.20  ? 118 SER A C     1 
ATOM   942  O  O     . SER A 1 118 ? 16.377  3.055   -9.200  1.00 74.20  ? 118 SER A O     1 
ATOM   943  C  CB    . SER A 1 118 ? 18.125  5.892   -9.332  1.00 69.06  ? 118 SER A CB    1 
ATOM   944  O  OG    . SER A 1 118 ? 19.096  4.874   -9.175  1.00 71.71  ? 118 SER A OG    1 
ATOM   945  N  N     . GLU A 1 119 ? 15.862  4.468   -10.883 1.00 71.34  ? 119 GLU A N     1 
ATOM   946  C  CA    . GLU A 1 119 ? 15.507  3.375   -11.783 1.00 80.39  ? 119 GLU A CA    1 
ATOM   947  C  C     . GLU A 1 119 ? 16.725  2.521   -12.107 1.00 76.97  ? 119 GLU A C     1 
ATOM   948  O  O     . GLU A 1 119 ? 16.615  1.299   -12.259 1.00 78.75  ? 119 GLU A O     1 
ATOM   949  C  CB    . GLU A 1 119 ? 14.882  3.919   -13.068 1.00 82.05  ? 119 GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 119 ? 13.627  4.750   -12.868 1.00 88.41  ? 119 GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 119 ? 13.928  6.181   -12.460 1.00 88.97  ? 119 GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 119 ? 15.007  6.428   -11.879 1.00 81.79  ? 119 GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 119 ? 13.085  7.062   -12.727 1.00 97.42  ? 119 GLU A OE2   1 
ATOM   954  N  N     . GLU A 1 120 ? 17.899  3.149   -12.215 1.00 79.17  ? 120 GLU A N     1 
ATOM   955  C  CA    . GLU A 1 120 ? 19.116  2.400   -12.512 1.00 84.08  ? 120 GLU A CA    1 
ATOM   956  C  C     . GLU A 1 120 ? 19.442  1.424   -11.389 1.00 74.45  ? 120 GLU A C     1 
ATOM   957  O  O     . GLU A 1 120 ? 19.731  0.247   -11.636 1.00 77.04  ? 120 GLU A O     1 
ATOM   958  C  CB    . GLU A 1 120 ? 20.282  3.361   -12.749 1.00 81.64  ? 120 GLU A CB    1 
ATOM   959  C  CG    . GLU A 1 120 ? 20.073  4.336   -13.901 1.00 93.91  ? 120 GLU A CG    1 
ATOM   960  C  CD    . GLU A 1 120 ? 19.434  5.642   -13.462 1.00 94.56  ? 120 GLU A CD    1 
ATOM   961  O  OE1   . GLU A 1 120 ? 19.240  5.831   -12.244 1.00 86.47  ? 120 GLU A OE1   1 
ATOM   962  O  OE2   . GLU A 1 120 ? 19.132  6.482   -14.337 1.00 104.17 ? 120 GLU A OE2   1 
ATOM   963  N  N     . ASP A 1 121 ? 19.401  1.896   -10.142 1.00 71.95  ? 121 ASP A N     1 
ATOM   964  C  CA    . ASP A 1 121 ? 19.667  1.011   -9.013  1.00 75.87  ? 121 ASP A CA    1 
ATOM   965  C  C     . ASP A 1 121 ? 18.624  -0.095  -8.922  1.00 73.29  ? 121 ASP A C     1 
ATOM   966  O  O     . ASP A 1 121 ? 18.951  -1.242  -8.598  1.00 68.67  ? 121 ASP A O     1 
ATOM   967  C  CB    . ASP A 1 121 ? 19.711  1.815   -7.714  1.00 75.43  ? 121 ASP A CB    1 
ATOM   968  C  CG    . ASP A 1 121 ? 20.820  2.848   -7.706  1.00 81.51  ? 121 ASP A CG    1 
ATOM   969  O  OD1   . ASP A 1 121 ? 21.576  2.919   -8.698  1.00 79.06  ? 121 ASP A OD1   1 
ATOM   970  O  OD2   . ASP A 1 121 ? 20.935  3.590   -6.706  1.00 80.27  ? 121 ASP A OD2   1 
ATOM   971  N  N     . PHE A 1 122 ? 17.360  0.229   -9.203  1.00 69.52  ? 122 PHE A N     1 
ATOM   972  C  CA    . PHE A 1 122 ? 16.313  -0.783  -9.122  1.00 67.26  ? 122 PHE A CA    1 
ATOM   973  C  C     . PHE A 1 122 ? 16.464  -1.826  -10.220 1.00 73.83  ? 122 PHE A C     1 
ATOM   974  O  O     . PHE A 1 122 ? 16.326  -3.028  -9.962  1.00 70.96  ? 122 PHE A O     1 
ATOM   975  C  CB    . PHE A 1 122 ? 14.934  -0.132  -9.195  1.00 68.80  ? 122 PHE A CB    1 
ATOM   976  C  CG    . PHE A 1 122 ? 13.804  -1.121  -9.189  1.00 60.58  ? 122 PHE A CG    1 
ATOM   977  C  CD1   . PHE A 1 122 ? 13.592  -1.939  -8.092  1.00 60.46  ? 122 PHE A CD1   1 
ATOM   978  C  CD2   . PHE A 1 122 ? 12.955  -1.233  -10.277 1.00 56.24  ? 122 PHE A CD2   1 
ATOM   979  C  CE1   . PHE A 1 122 ? 12.556  -2.851  -8.079  1.00 56.96  ? 122 PHE A CE1   1 
ATOM   980  C  CE2   . PHE A 1 122 ? 11.916  -2.141  -10.270 1.00 57.61  ? 122 PHE A CE2   1 
ATOM   981  C  CZ    . PHE A 1 122 ? 11.716  -2.952  -9.169  1.00 54.65  ? 122 PHE A CZ    1 
ATOM   982  N  N     . GLU A 1 123 ? 16.739  -1.389  -11.452 1.00 72.12  ? 123 GLU A N     1 
ATOM   983  C  CA    . GLU A 1 123 ? 16.902  -2.343  -12.543 1.00 72.11  ? 123 GLU A CA    1 
ATOM   984  C  C     . GLU A 1 123 ? 17.958  -3.386  -12.202 1.00 69.43  ? 123 GLU A C     1 
ATOM   985  O  O     . GLU A 1 123 ? 17.793  -4.572  -12.510 1.00 66.42  ? 123 GLU A O     1 
ATOM   986  C  CB    . GLU A 1 123 ? 17.264  -1.618  -13.837 1.00 77.48  ? 123 GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 123 ? 17.388  -2.552  -15.032 1.00 88.74  ? 123 GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 123 ? 17.925  -1.862  -16.271 1.00 101.02 ? 123 GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 123 ? 18.005  -0.616  -16.275 1.00 112.41 ? 123 GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 123 ? 18.270  -2.571  -17.241 1.00 97.75  ? 123 GLU A OE2   1 
ATOM   991  N  N     . LYS A 1 124 ? 19.050  -2.963  -11.566 1.00 69.02  ? 124 LYS A N     1 
ATOM   992  C  CA    . LYS A 1 124 ? 20.057  -3.913  -11.109 1.00 68.48  ? 124 LYS A CA    1 
ATOM   993  C  C     . LYS A 1 124 ? 19.469  -4.871  -10.081 1.00 67.65  ? 124 LYS A C     1 
ATOM   994  O  O     . LYS A 1 124 ? 19.507  -6.094  -10.254 1.00 72.52  ? 124 LYS A O     1 
ATOM   995  C  CB    . LYS A 1 124 ? 21.256  -3.163  -10.527 1.00 65.50  ? 124 LYS A CB    1 
ATOM   996  C  CG    . LYS A 1 124 ? 21.903  -2.198  -11.501 1.00 76.24  ? 124 LYS A CG    1 
ATOM   997  C  CD    . LYS A 1 124 ? 22.949  -1.328  -10.826 1.00 79.77  ? 124 LYS A CD    1 
ATOM   998  C  CE    . LYS A 1 124 ? 23.500  -0.295  -11.796 1.00 88.65  ? 124 LYS A CE    1 
ATOM   999  N  NZ    . LYS A 1 124 ? 24.320  0.740   -11.110 1.00 99.52  ? 124 LYS A NZ    1 
ATOM   1000 N  N     . ALA A 1 125 ? 18.913  -4.324  -8.997  1.00 68.78  ? 125 ALA A N     1 
ATOM   1001 C  CA    . ALA A 1 125 ? 18.344  -5.167  -7.951  1.00 64.25  ? 125 ALA A CA    1 
ATOM   1002 C  C     . ALA A 1 125 ? 17.263  -6.084  -8.508  1.00 63.85  ? 125 ALA A C     1 
ATOM   1003 O  O     . ALA A 1 125 ? 17.222  -7.276  -8.185  1.00 67.22  ? 125 ALA A O     1 
ATOM   1004 C  CB    . ALA A 1 125 ? 17.786  -4.299  -6.825  1.00 63.12  ? 125 ALA A CB    1 
ATOM   1005 N  N     . PHE A 1 126 ? 16.379  -5.545  -9.348  1.00 64.96  ? 126 PHE A N     1 
ATOM   1006 C  CA    . PHE A 1 126 ? 15.332  -6.361  -9.953  1.00 58.27  ? 126 PHE A CA    1 
ATOM   1007 C  C     . PHE A 1 126 ? 15.929  -7.527  -10.730 1.00 64.49  ? 126 PHE A C     1 
ATOM   1008 O  O     . PHE A 1 126 ? 15.583  -8.690  -10.493 1.00 66.64  ? 126 PHE A O     1 
ATOM   1009 C  CB    . PHE A 1 126 ? 14.465  -5.489  -10.860 1.00 60.89  ? 126 PHE A CB    1 
ATOM   1010 C  CG    . PHE A 1 126 ? 13.373  -6.236  -11.568 1.00 58.50  ? 126 PHE A CG    1 
ATOM   1011 C  CD1   . PHE A 1 126 ? 13.615  -6.866  -12.776 1.00 60.07  ? 126 PHE A CD1   1 
ATOM   1012 C  CD2   . PHE A 1 126 ? 12.095  -6.285  -11.040 1.00 59.53  ? 126 PHE A CD2   1 
ATOM   1013 C  CE1   . PHE A 1 126 ? 12.608  -7.545  -13.434 1.00 60.08  ? 126 PHE A CE1   1 
ATOM   1014 C  CE2   . PHE A 1 126 ? 11.084  -6.960  -11.694 1.00 60.92  ? 126 PHE A CE2   1 
ATOM   1015 C  CZ    . PHE A 1 126 ? 11.341  -7.591  -12.892 1.00 57.78  ? 126 PHE A CZ    1 
ATOM   1016 N  N     . ASN A 1 127 ? 16.836  -7.234  -11.664 1.00 62.51  ? 127 ASN A N     1 
ATOM   1017 C  CA    . ASN A 1 127 ? 17.434  -8.288  -12.475 1.00 68.22  ? 127 ASN A CA    1 
ATOM   1018 C  C     . ASN A 1 127 ? 18.168  -9.320  -11.633 1.00 67.38  ? 127 ASN A C     1 
ATOM   1019 O  O     . ASN A 1 127 ? 18.418  -10.431 -12.115 1.00 60.51  ? 127 ASN A O     1 
ATOM   1020 C  CB    . ASN A 1 127 ? 18.391  -7.686  -13.506 1.00 65.85  ? 127 ASN A CB    1 
ATOM   1021 C  CG    . ASN A 1 127 ? 17.669  -6.897  -14.581 1.00 73.53  ? 127 ASN A CG    1 
ATOM   1022 O  OD1   . ASN A 1 127 ? 16.515  -7.179  -14.907 1.00 69.29  ? 127 ASN A OD1   1 
ATOM   1023 N  ND2   . ASN A 1 127 ? 18.349  -5.904  -15.143 1.00 79.13  ? 127 ASN A ND2   1 
ATOM   1024 N  N     . ALA A 1 128 ? 18.521  -8.985  -10.395 1.00 65.17  ? 128 ALA A N     1 
ATOM   1025 C  CA    . ALA A 1 128 ? 19.212  -9.909  -9.509  1.00 65.52  ? 128 ALA A CA    1 
ATOM   1026 C  C     . ALA A 1 128 ? 18.258  -10.732 -8.654  1.00 71.02  ? 128 ALA A C     1 
ATOM   1027 O  O     . ALA A 1 128 ? 18.709  -11.417 -7.730  1.00 75.85  ? 128 ALA A O     1 
ATOM   1028 C  CB    . ALA A 1 128 ? 20.188  -9.145  -8.609  1.00 63.61  ? 128 ALA A CB    1 
ATOM   1029 N  N     . ARG A 1 129 ? 16.957  -10.692 -8.942  1.00 61.99  ? 129 ARG A N     1 
ATOM   1030 C  CA    . ARG A 1 129 ? 15.982  -11.365 -8.094  1.00 57.00  ? 129 ARG A CA    1 
ATOM   1031 C  C     . ARG A 1 129 ? 14.983  -12.194 -8.893  1.00 61.93  ? 129 ARG A C     1 
ATOM   1032 O  O     . ARG A 1 129 ? 14.887  -13.411 -8.704  1.00 61.25  ? 129 ARG A O     1 
ATOM   1033 C  CB    . ARG A 1 129 ? 15.233  -10.340 -7.239  1.00 62.87  ? 129 ARG A CB    1 
ATOM   1034 C  CG    . ARG A 1 129 ? 16.057  -9.745  -6.112  1.00 57.30  ? 129 ARG A CG    1 
ATOM   1035 C  CD    . ARG A 1 129 ? 15.332  -8.580  -5.461  1.00 62.31  ? 129 ARG A CD    1 
ATOM   1036 N  NE    . ARG A 1 129 ? 15.845  -8.300  -4.125  1.00 65.50  ? 129 ARG A NE    1 
ATOM   1037 C  CZ    . ARG A 1 129 ? 16.979  -7.661  -3.879  1.00 64.90  ? 129 ARG A CZ    1 
ATOM   1038 N  NH1   . ARG A 1 129 ? 17.748  -7.215  -4.859  1.00 66.90  ? 129 ARG A NH1   1 
ATOM   1039 N  NH2   . ARG A 1 129 ? 17.355  -7.469  -2.617  1.00 66.70  ? 129 ARG A NH2   1 
ATOM   1040 N  N     . PHE A 1 130 ? 14.241  -11.549 -9.788  1.00 56.93  ? 130 PHE A N     1 
ATOM   1041 C  CA    . PHE A 1 130 ? 13.053  -12.162 -10.371 1.00 60.83  ? 130 PHE A CA    1 
ATOM   1042 C  C     . PHE A 1 130 ? 13.341  -13.182 -11.471 1.00 62.04  ? 130 PHE A C     1 
ATOM   1043 O  O     . PHE A 1 130 ? 12.582  -14.149 -11.608 1.00 60.94  ? 130 PHE A O     1 
ATOM   1044 C  CB    . PHE A 1 130 ? 12.118  -11.072 -10.896 1.00 57.92  ? 130 PHE A CB    1 
ATOM   1045 C  CG    . PHE A 1 130 ? 11.298  -10.424 -9.819  1.00 65.51  ? 130 PHE A CG    1 
ATOM   1046 C  CD1   . PHE A 1 130 ? 11.792  -9.345  -9.106  1.00 61.66  ? 130 PHE A CD1   1 
ATOM   1047 C  CD2   . PHE A 1 130 ? 10.039  -10.912 -9.502  1.00 63.03  ? 130 PHE A CD2   1 
ATOM   1048 C  CE1   . PHE A 1 130 ? 11.041  -8.759  -8.106  1.00 61.77  ? 130 PHE A CE1   1 
ATOM   1049 C  CE2   . PHE A 1 130 ? 9.284   -10.330 -8.504  1.00 51.75  ? 130 PHE A CE2   1 
ATOM   1050 C  CZ    . PHE A 1 130 ? 9.785   -9.252  -7.805  1.00 57.69  ? 130 PHE A CZ    1 
ATOM   1051 N  N     . PRO A 1 131 ? 14.396  -13.011 -12.287 1.00 63.92  ? 131 PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 131 ? 14.672  -14.007 -13.333 1.00 67.51  ? 131 PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 131 ? 14.646  -15.444 -12.827 1.00 60.80  ? 131 PRO A C     1 
ATOM   1054 O  O     . PRO A 1 131 ? 15.539  -15.870 -12.088 1.00 59.67  ? 131 PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 131 ? 16.068  -13.609 -13.827 1.00 61.67  ? 131 PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 131 ? 16.090  -12.129 -13.650 1.00 63.49  ? 131 PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 131 ? 15.296  -11.847 -12.394 1.00 61.66  ? 131 PRO A CD    1 
ATOM   1058 N  N     . GLY A 1 132 ? 13.613  -16.190 -13.218 1.00 62.35  ? 132 GLY A N     1 
ATOM   1059 C  CA    . GLY A 1 132 ? 13.511  -17.597 -12.879 1.00 58.61  ? 132 GLY A CA    1 
ATOM   1060 C  C     . GLY A 1 132 ? 13.159  -17.895 -11.441 1.00 60.95  ? 132 GLY A C     1 
ATOM   1061 O  O     . GLY A 1 132 ? 13.406  -19.009 -10.975 1.00 67.71  ? 132 GLY A O     1 
ATOM   1062 N  N     . CYS A 1 133 ? 12.572  -16.934 -10.725 1.00 60.67  ? 133 CYS A N     1 
ATOM   1063 C  CA    . CYS A 1 133 ? 12.314  -17.106 -9.300  1.00 59.67  ? 133 CYS A CA    1 
ATOM   1064 C  C     . CYS A 1 133 ? 11.133  -18.024 -9.009  1.00 60.32  ? 133 CYS A C     1 
ATOM   1065 O  O     . CYS A 1 133 ? 11.073  -18.599 -7.918  1.00 65.24  ? 133 CYS A O     1 
ATOM   1066 C  CB    . CYS A 1 133 ? 12.084  -15.745 -8.639  1.00 58.13  ? 133 CYS A CB    1 
ATOM   1067 S  SG    . CYS A 1 133 ? 10.726  -14.775 -9.339  1.00 63.30  ? 133 CYS A SG    1 
ATOM   1068 N  N     . MET A 1 134 ? 10.199  -18.180 -9.946  1.00 58.34  ? 134 MET A N     1 
ATOM   1069 C  CA    . MET A 1 134 ? 9.040   -19.042 -9.755  1.00 59.00  ? 134 MET A CA    1 
ATOM   1070 C  C     . MET A 1 134 ? 9.225   -20.426 -10.365 1.00 63.15  ? 134 MET A C     1 
ATOM   1071 O  O     . MET A 1 134 ? 8.243   -21.163 -10.509 1.00 62.72  ? 134 MET A O     1 
ATOM   1072 C  CB    . MET A 1 134 ? 7.790   -18.386 -10.341 1.00 54.01  ? 134 MET A CB    1 
ATOM   1073 C  CG    . MET A 1 134 ? 7.422   -17.055 -9.712  1.00 54.89  ? 134 MET A CG    1 
ATOM   1074 S  SD    . MET A 1 134 ? 5.861   -16.436 -10.360 1.00 51.75  ? 134 MET A SD    1 
ATOM   1075 C  CE    . MET A 1 134 ? 5.699   -14.911 -9.436  1.00 54.42  ? 134 MET A CE    1 
ATOM   1076 N  N     . LYS A 1 135 ? 10.451  -20.794 -10.725 1.00 62.15  ? 135 LYS A N     1 
ATOM   1077 C  CA    . LYS A 1 135 ? 10.704  -22.076 -11.370 1.00 61.85  ? 135 LYS A CA    1 
ATOM   1078 C  C     . LYS A 1 135 ? 10.093  -23.213 -10.563 1.00 66.51  ? 135 LYS A C     1 
ATOM   1079 O  O     . LYS A 1 135 ? 10.388  -23.375 -9.375  1.00 65.15  ? 135 LYS A O     1 
ATOM   1080 C  CB    . LYS A 1 135 ? 12.212  -22.282 -11.531 1.00 65.25  ? 135 LYS A CB    1 
ATOM   1081 C  CG    . LYS A 1 135 ? 12.599  -23.247 -12.643 1.00 71.17  ? 135 LYS A CG    1 
ATOM   1082 C  CD    . LYS A 1 135 ? 12.368  -22.624 -14.012 1.00 72.10  ? 135 LYS A CD    1 
ATOM   1083 C  CE    . LYS A 1 135 ? 12.637  -23.615 -15.137 1.00 80.61  ? 135 LYS A CE    1 
ATOM   1084 N  NZ    . LYS A 1 135 ? 14.052  -24.079 -15.166 1.00 98.82  ? 135 LYS A NZ    1 
ATOM   1085 N  N     . GLY A 1 136 ? 9.232   -23.996 -11.210 1.00 68.16  ? 136 GLY A N     1 
ATOM   1086 C  CA    . GLY A 1 136 ? 8.601   -25.124 -10.559 1.00 60.74  ? 136 GLY A CA    1 
ATOM   1087 C  C     . GLY A 1 136 ? 7.446   -24.783 -9.646  1.00 61.83  ? 136 GLY A C     1 
ATOM   1088 O  O     . GLY A 1 136 ? 6.930   -25.679 -8.968  1.00 58.02  ? 136 GLY A O     1 
ATOM   1089 N  N     . ARG A 1 137 ? 7.026   -23.523 -9.597  1.00 64.40  ? 137 ARG A N     1 
ATOM   1090 C  CA    . ARG A 1 137 ? 5.886   -23.102 -8.799  1.00 54.82  ? 137 ARG A CA    1 
ATOM   1091 C  C     . ARG A 1 137 ? 4.755   -22.639 -9.707  1.00 58.60  ? 137 ARG A C     1 
ATOM   1092 O  O     . ARG A 1 137 ? 4.926   -22.449 -10.915 1.00 59.75  ? 137 ARG A O     1 
ATOM   1093 C  CB    . ARG A 1 137 ? 6.277   -21.982 -7.828  1.00 55.29  ? 137 ARG A CB    1 
ATOM   1094 C  CG    . ARG A 1 137 ? 7.408   -22.330 -6.874  1.00 59.51  ? 137 ARG A CG    1 
ATOM   1095 C  CD    . ARG A 1 137 ? 7.572   -21.248 -5.815  1.00 52.87  ? 137 ARG A CD    1 
ATOM   1096 N  NE    . ARG A 1 137 ? 8.636   -21.553 -4.865  1.00 57.12  ? 137 ARG A NE    1 
ATOM   1097 C  CZ    . ARG A 1 137 ? 8.483   -22.308 -3.785  1.00 63.82  ? 137 ARG A CZ    1 
ATOM   1098 N  NH1   . ARG A 1 137 ? 7.322   -22.871 -3.495  1.00 52.86  ? 137 ARG A NH1   1 
ATOM   1099 N  NH2   . ARG A 1 137 ? 9.522   -22.504 -2.978  1.00 66.88  ? 137 ARG A NH2   1 
ATOM   1100 N  N     . THR A 1 138 ? 3.583   -22.458 -9.105  1.00 49.17  ? 138 THR A N     1 
ATOM   1101 C  CA    . THR A 1 138 ? 2.427   -21.921 -9.806  1.00 54.83  ? 138 THR A CA    1 
ATOM   1102 C  C     . THR A 1 138 ? 2.408   -20.402 -9.684  1.00 52.66  ? 138 THR A C     1 
ATOM   1103 O  O     . THR A 1 138 ? 2.740   -19.848 -8.633  1.00 55.01  ? 138 THR A O     1 
ATOM   1104 C  CB    . THR A 1 138 ? 1.129   -22.507 -9.243  1.00 48.74  ? 138 THR A CB    1 
ATOM   1105 O  OG1   . THR A 1 138 ? 0.994   -23.869 -9.660  1.00 58.18  ? 138 THR A OG1   1 
ATOM   1106 C  CG2   . THR A 1 138 ? -0.077  -21.718 -9.724  1.00 54.26  ? 138 THR A CG2   1 
ATOM   1107 N  N     . MET A 1 139 ? 2.032   -19.731 -10.771 1.00 51.59  ? 139 MET A N     1 
ATOM   1108 C  CA    . MET A 1 139 ? 1.823   -18.287 -10.761 1.00 48.69  ? 139 MET A CA    1 
ATOM   1109 C  C     . MET A 1 139 ? 0.322   -18.037 -10.715 1.00 51.01  ? 139 MET A C     1 
ATOM   1110 O  O     . MET A 1 139 ? -0.389  -18.306 -11.689 1.00 55.45  ? 139 MET A O     1 
ATOM   1111 C  CB    . MET A 1 139 ? 2.452   -17.611 -11.979 1.00 49.01  ? 139 MET A CB    1 
ATOM   1112 C  CG    . MET A 1 139 ? 2.133   -16.116 -12.069 1.00 44.39  ? 139 MET A CG    1 
ATOM   1113 S  SD    . MET A 1 139 ? 2.692   -15.296 -13.587 1.00 51.15  ? 139 MET A SD    1 
ATOM   1114 C  CE    . MET A 1 139 ? 4.462   -15.251 -13.321 1.00 52.25  ? 139 MET A CE    1 
ATOM   1115 N  N     . TYR A 1 140 ? -0.158  -17.531 -9.585  1.00 44.77  ? 140 TYR A N     1 
ATOM   1116 C  CA    . TYR A 1 140 ? -1.558  -17.171 -9.439  1.00 42.65  ? 140 TYR A CA    1 
ATOM   1117 C  C     . TYR A 1 140 ? -1.763  -15.744 -9.927  1.00 46.37  ? 140 TYR A C     1 
ATOM   1118 O  O     . TYR A 1 140 ? -0.977  -14.849 -9.601  1.00 48.83  ? 140 TYR A O     1 
ATOM   1119 C  CB    . TYR A 1 140 ? -2.002  -17.314 -7.982  1.00 43.11  ? 140 TYR A CB    1 
ATOM   1120 C  CG    . TYR A 1 140 ? -1.778  -18.704 -7.440  1.00 43.67  ? 140 TYR A CG    1 
ATOM   1121 C  CD1   . TYR A 1 140 ? -2.709  -19.711 -7.656  1.00 49.35  ? 140 TYR A CD1   1 
ATOM   1122 C  CD2   . TYR A 1 140 ? -0.625  -19.019 -6.734  1.00 43.59  ? 140 TYR A CD2   1 
ATOM   1123 C  CE1   . TYR A 1 140 ? -2.504  -20.992 -7.177  1.00 49.04  ? 140 TYR A CE1   1 
ATOM   1124 C  CE2   . TYR A 1 140 ? -0.411  -20.296 -6.249  1.00 48.44  ? 140 TYR A CE2   1 
ATOM   1125 C  CZ    . TYR A 1 140 ? -1.356  -21.279 -6.473  1.00 52.11  ? 140 TYR A CZ    1 
ATOM   1126 O  OH    . TYR A 1 140 ? -1.155  -22.556 -5.996  1.00 57.29  ? 140 TYR A OH    1 
ATOM   1127 N  N     . VAL A 1 141 ? -2.810  -15.541 -10.717 1.00 46.60  ? 141 VAL A N     1 
ATOM   1128 C  CA    . VAL A 1 141 ? -3.165  -14.227 -11.235 1.00 46.74  ? 141 VAL A CA    1 
ATOM   1129 C  C     . VAL A 1 141 ? -4.368  -13.741 -10.441 1.00 47.94  ? 141 VAL A C     1 
ATOM   1130 O  O     . VAL A 1 141 ? -5.489  -14.228 -10.633 1.00 47.84  ? 141 VAL A O     1 
ATOM   1131 C  CB    . VAL A 1 141 ? -3.458  -14.268 -12.740 1.00 48.15  ? 141 VAL A CB    1 
ATOM   1132 C  CG1   . VAL A 1 141 ? -3.748  -12.872 -13.264 1.00 44.04  ? 141 VAL A CG1   1 
ATOM   1133 C  CG2   . VAL A 1 141 ? -2.284  -14.885 -13.481 1.00 44.60  ? 141 VAL A CG2   1 
ATOM   1134 N  N     . ILE A 1 142 ? -4.136  -12.784 -9.547  1.00 50.62  ? 142 ILE A N     1 
ATOM   1135 C  CA    . ILE A 1 142 ? -5.167  -12.286 -8.640  1.00 44.76  ? 142 ILE A CA    1 
ATOM   1136 C  C     . ILE A 1 142 ? -5.745  -10.984 -9.181  1.00 48.99  ? 142 ILE A C     1 
ATOM   1137 O  O     . ILE A 1 142 ? -5.098  -9.932  -9.076  1.00 52.34  ? 142 ILE A O     1 
ATOM   1138 C  CB    . ILE A 1 142 ? -4.607  -12.073 -7.226  1.00 44.64  ? 142 ILE A CB    1 
ATOM   1139 C  CG1   . ILE A 1 142 ? -3.825  -13.302 -6.763  1.00 47.12  ? 142 ILE A CG1   1 
ATOM   1140 C  CG2   . ILE A 1 142 ? -5.730  -11.769 -6.254  1.00 47.04  ? 142 ILE A CG2   1 
ATOM   1141 C  CD1   . ILE A 1 142 ? -3.167  -13.124 -5.410  1.00 42.12  ? 142 ILE A CD1   1 
ATOM   1142 N  N     . PRO A 1 143 ? -6.945  -10.998 -9.759  1.00 51.04  ? 143 PRO A N     1 
ATOM   1143 C  CA    . PRO A 1 143 ? -7.601  -9.737  -10.122 1.00 51.74  ? 143 PRO A CA    1 
ATOM   1144 C  C     . PRO A 1 143 ? -8.487  -9.236  -8.993  1.00 58.51  ? 143 PRO A C     1 
ATOM   1145 O  O     . PRO A 1 143 ? -9.440  -9.919  -8.606  1.00 60.41  ? 143 PRO A O     1 
ATOM   1146 C  CB    . PRO A 1 143 ? -8.419  -10.121 -11.359 1.00 51.90  ? 143 PRO A CB    1 
ATOM   1147 C  CG    . PRO A 1 143 ? -8.665  -11.622 -11.212 1.00 46.81  ? 143 PRO A CG    1 
ATOM   1148 C  CD    . PRO A 1 143 ? -7.782  -12.156 -10.103 1.00 47.94  ? 143 PRO A CD    1 
ATOM   1149 N  N     . PHE A 1 144 ? -8.191  -8.056  -8.450  1.00 53.50  ? 144 PHE A N     1 
ATOM   1150 C  CA    . PHE A 1 144 ? -8.886  -7.585  -7.261  1.00 53.20  ? 144 PHE A CA    1 
ATOM   1151 C  C     . PHE A 1 144 ? -9.213  -6.105  -7.386  1.00 54.23  ? 144 PHE A C     1 
ATOM   1152 O  O     . PHE A 1 144 ? -8.446  -5.324  -7.956  1.00 56.42  ? 144 PHE A O     1 
ATOM   1153 C  CB    . PHE A 1 144 ? -8.055  -7.824  -5.996  1.00 52.27  ? 144 PHE A CB    1 
ATOM   1154 C  CG    . PHE A 1 144 ? -6.786  -7.025  -5.943  1.00 50.95  ? 144 PHE A CG    1 
ATOM   1155 C  CD1   . PHE A 1 144 ? -5.640  -7.475  -6.578  1.00 55.96  ? 144 PHE A CD1   1 
ATOM   1156 C  CD2   . PHE A 1 144 ? -6.735  -5.828  -5.250  1.00 47.45  ? 144 PHE A CD2   1 
ATOM   1157 C  CE1   . PHE A 1 144 ? -4.467  -6.741  -6.527  1.00 51.85  ? 144 PHE A CE1   1 
ATOM   1158 C  CE2   . PHE A 1 144 ? -5.568  -5.091  -5.193  1.00 47.01  ? 144 PHE A CE2   1 
ATOM   1159 C  CZ    . PHE A 1 144 ? -4.432  -5.549  -5.831  1.00 46.99  ? 144 PHE A CZ    1 
ATOM   1160 N  N     . SER A 1 145 ? -10.362 -5.732  -6.831  1.00 55.83  ? 145 SER A N     1 
ATOM   1161 C  CA    . SER A 1 145 ? -10.836 -4.356  -6.816  1.00 59.18  ? 145 SER A CA    1 
ATOM   1162 C  C     . SER A 1 145 ? -10.682 -3.781  -5.415  1.00 56.93  ? 145 SER A C     1 
ATOM   1163 O  O     . SER A 1 145 ? -11.054 -4.427  -4.430  1.00 54.67  ? 145 SER A O     1 
ATOM   1164 C  CB    . SER A 1 145 ? -12.298 -4.280  -7.257  1.00 62.60  ? 145 SER A CB    1 
ATOM   1165 O  OG    . SER A 1 145 ? -12.840 -2.996  -7.013  1.00 58.26  ? 145 SER A OG    1 
ATOM   1166 N  N     . MET A 1 146 ? -10.131 -2.573  -5.328  1.00 55.42  ? 146 MET A N     1 
ATOM   1167 C  CA    . MET A 1 146 ? -10.022 -1.861  -4.059  1.00 59.56  ? 146 MET A CA    1 
ATOM   1168 C  C     . MET A 1 146 ? -11.230 -0.943  -3.926  1.00 65.16  ? 146 MET A C     1 
ATOM   1169 O  O     . MET A 1 146 ? -11.386 0.008   -4.700  1.00 65.58  ? 146 MET A O     1 
ATOM   1170 C  CB    . MET A 1 146 ? -8.714  -1.082  -3.983  1.00 57.91  ? 146 MET A CB    1 
ATOM   1171 C  CG    . MET A 1 146 ? -7.482  -1.968  -4.018  1.00 50.63  ? 146 MET A CG    1 
ATOM   1172 S  SD    . MET A 1 146 ? -7.484  -3.186  -2.690  1.00 49.39  ? 146 MET A SD    1 
ATOM   1173 C  CE    . MET A 1 146 ? -7.305  -2.125  -1.258  1.00 57.91  ? 146 MET A CE    1 
ATOM   1174 N  N     . GLY A 1 147 ? -12.087 -1.231  -2.950  1.00 68.60  ? 147 GLY A N     1 
ATOM   1175 C  CA    . GLY A 1 147 ? -13.341 -0.533  -2.805  1.00 70.55  ? 147 GLY A CA    1 
ATOM   1176 C  C     . GLY A 1 147 ? -14.446 -1.226  -3.575  1.00 74.74  ? 147 GLY A C     1 
ATOM   1177 O  O     . GLY A 1 147 ? -14.198 -2.117  -4.393  1.00 71.08  ? 147 GLY A O     1 
ATOM   1178 N  N     . PRO A 1 148 ? -15.694 -0.831  -3.327  1.00 83.71  ? 148 PRO A N     1 
ATOM   1179 C  CA    . PRO A 1 148 ? -16.816 -1.469  -4.026  1.00 84.33  ? 148 PRO A CA    1 
ATOM   1180 C  C     . PRO A 1 148 ? -16.651 -1.384  -5.536  1.00 85.23  ? 148 PRO A C     1 
ATOM   1181 O  O     . PRO A 1 148 ? -16.115 -0.412  -6.072  1.00 91.66  ? 148 PRO A O     1 
ATOM   1182 C  CB    . PRO A 1 148 ? -18.033 -0.666  -3.551  1.00 83.19  ? 148 PRO A CB    1 
ATOM   1183 C  CG    . PRO A 1 148 ? -17.607 -0.067  -2.248  1.00 84.75  ? 148 PRO A CG    1 
ATOM   1184 C  CD    . PRO A 1 148 ? -16.141 0.214   -2.392  1.00 83.84  ? 148 PRO A CD    1 
ATOM   1185 N  N     . LEU A 1 149 ? -17.117 -2.424  -6.223  1.00 81.11  ? 149 LEU A N     1 
ATOM   1186 C  CA    . LEU A 1 149 ? -17.067 -2.424  -7.678  1.00 86.47  ? 149 LEU A CA    1 
ATOM   1187 C  C     . LEU A 1 149 ? -17.921 -1.295  -8.239  1.00 96.15  ? 149 LEU A C     1 
ATOM   1188 O  O     . LEU A 1 149 ? -18.971 -0.953  -7.688  1.00 99.51  ? 149 LEU A O     1 
ATOM   1189 C  CB    . LEU A 1 149 ? -17.534 -3.766  -8.233  1.00 81.16  ? 149 LEU A CB    1 
ATOM   1190 C  CG    . LEU A 1 149 ? -16.422 -4.810  -8.306  1.00 84.75  ? 149 LEU A CG    1 
ATOM   1191 C  CD1   . LEU A 1 149 ? -16.886 -6.052  -9.053  1.00 81.57  ? 149 LEU A CD1   1 
ATOM   1192 C  CD2   . LEU A 1 149 ? -15.188 -4.203  -8.959  1.00 82.63  ? 149 LEU A CD2   1 
ATOM   1193 N  N     . GLY A 1 150 ? -17.460 -0.712  -9.345  1.00 97.37  ? 150 GLY A N     1 
ATOM   1194 C  CA    . GLY A 1 150 ? -18.098 0.452   -9.914  1.00 97.28  ? 150 GLY A CA    1 
ATOM   1195 C  C     . GLY A 1 150 ? -18.020 1.701   -9.069  1.00 108.90 ? 150 GLY A C     1 
ATOM   1196 O  O     . GLY A 1 150 ? -18.310 2.790   -9.579  1.00 114.24 ? 150 GLY A O     1 
ATOM   1197 N  N     . SER A 1 151 ? -17.647 1.587   -7.799  1.00 105.60 ? 151 SER A N     1 
ATOM   1198 C  CA    . SER A 1 151 ? -17.486 2.763   -6.961  1.00 108.29 ? 151 SER A CA    1 
ATOM   1199 C  C     . SER A 1 151 ? -16.526 3.743   -7.632  1.00 117.54 ? 151 SER A C     1 
ATOM   1200 O  O     . SER A 1 151 ? -15.516 3.322   -8.212  1.00 112.45 ? 151 SER A O     1 
ATOM   1201 C  CB    . SER A 1 151 ? -16.959 2.364   -5.580  1.00 103.66 ? 151 SER A CB    1 
ATOM   1202 O  OG    . SER A 1 151 ? -16.700 3.505   -4.779  1.00 105.79 ? 151 SER A OG    1 
ATOM   1203 N  N     . PRO A 1 152 ? -16.800 5.049   -7.575  1.00 131.74 ? 152 PRO A N     1 
ATOM   1204 C  CA    . PRO A 1 152 ? -15.907 6.000   -8.259  1.00 131.65 ? 152 PRO A CA    1 
ATOM   1205 C  C     . PRO A 1 152 ? -14.476 5.931   -7.760  1.00 129.41 ? 152 PRO A C     1 
ATOM   1206 O  O     . PRO A 1 152 ? -13.539 5.863   -8.564  1.00 133.63 ? 152 PRO A O     1 
ATOM   1207 C  CB    . PRO A 1 152 ? -16.560 7.357   -7.965  1.00 134.60 ? 152 PRO A CB    1 
ATOM   1208 C  CG    . PRO A 1 152 ? -17.322 7.138   -6.699  1.00 131.27 ? 152 PRO A CG    1 
ATOM   1209 C  CD    . PRO A 1 152 ? -17.833 5.730   -6.778  1.00 131.07 ? 152 PRO A CD    1 
ATOM   1210 N  N     . LEU A 1 153 ? -14.282 5.939   -6.443  1.00 114.57 ? 153 LEU A N     1 
ATOM   1211 C  CA    . LEU A 1 153 ? -12.942 5.874   -5.873  1.00 108.76 ? 153 LEU A CA    1 
ATOM   1212 C  C     . LEU A 1 153 ? -12.474 4.429   -5.754  1.00 97.25  ? 153 LEU A C     1 
ATOM   1213 O  O     . LEU A 1 153 ? -11.691 4.094   -4.860  1.00 91.25  ? 153 LEU A O     1 
ATOM   1214 C  CB    . LEU A 1 153 ? -12.904 6.566   -4.510  1.00 101.51 ? 153 LEU A CB    1 
ATOM   1215 C  CG    . LEU A 1 153 ? -13.114 8.082   -4.478  1.00 98.49  ? 153 LEU A CG    1 
ATOM   1216 C  CD1   . LEU A 1 153 ? -13.247 8.567   -3.041  1.00 79.61  ? 153 LEU A CD1   1 
ATOM   1217 C  CD2   . LEU A 1 153 ? -11.982 8.811   -5.191  1.00 80.67  ? 153 LEU A CD2   1 
ATOM   1218 N  N     . ALA A 1 154 ? -12.945 3.570   -6.653  1.00 94.18  ? 154 ALA A N     1 
ATOM   1219 C  CA    . ALA A 1 154 ? -12.563 2.166   -6.673  1.00 92.47  ? 154 ALA A CA    1 
ATOM   1220 C  C     . ALA A 1 154 ? -11.575 1.942   -7.809  1.00 83.39  ? 154 ALA A C     1 
ATOM   1221 O  O     . ALA A 1 154 ? -11.871 2.257   -8.967  1.00 84.12  ? 154 ALA A O     1 
ATOM   1222 C  CB    . ALA A 1 154 ? -13.789 1.268   -6.840  1.00 91.31  ? 154 ALA A CB    1 
ATOM   1223 N  N     . LYS A 1 155 ? -10.405 1.404   -7.478  1.00 71.60  ? 155 LYS A N     1 
ATOM   1224 C  CA    . LYS A 1 155 ? -9.369  1.128   -8.459  1.00 68.17  ? 155 LYS A CA    1 
ATOM   1225 C  C     . LYS A 1 155 ? -9.022  -0.355  -8.445  1.00 64.32  ? 155 LYS A C     1 
ATOM   1226 O  O     . LYS A 1 155 ? -9.072  -1.018  -7.404  1.00 58.59  ? 155 LYS A O     1 
ATOM   1227 C  CB    . LYS A 1 155 ? -8.124  1.983   -8.198  1.00 68.36  ? 155 LYS A CB    1 
ATOM   1228 C  CG    . LYS A 1 155 ? -8.414  3.482   -8.179  1.00 76.95  ? 155 LYS A CG    1 
ATOM   1229 C  CD    . LYS A 1 155 ? -7.141  4.315   -8.239  1.00 82.80  ? 155 LYS A CD    1 
ATOM   1230 C  CE    . LYS A 1 155 ? -6.594  4.403   -9.658  1.00 92.51  ? 155 LYS A CE    1 
ATOM   1231 N  NZ    . LYS A 1 155 ? -7.514  5.144   -10.568 1.00 88.76  ? 155 LYS A NZ    1 
ATOM   1232 N  N     . ILE A 1 156 ? -8.669  -0.869  -9.620  1.00 61.96  ? 156 ILE A N     1 
ATOM   1233 C  CA    . ILE A 1 156 ? -8.493  -2.298  -9.842  1.00 62.01  ? 156 ILE A CA    1 
ATOM   1234 C  C     . ILE A 1 156 ? -7.011  -2.609  -9.995  1.00 56.64  ? 156 ILE A C     1 
ATOM   1235 O  O     . ILE A 1 156 ? -6.264  -1.848  -10.622 1.00 57.86  ? 156 ILE A O     1 
ATOM   1236 C  CB    . ILE A 1 156 ? -9.283  -2.765  -11.080 1.00 55.34  ? 156 ILE A CB    1 
ATOM   1237 C  CG1   . ILE A 1 156 ? -10.787 -2.662  -10.821 1.00 55.60  ? 156 ILE A CG1   1 
ATOM   1238 C  CG2   . ILE A 1 156 ? -8.885  -4.176  -11.465 1.00 54.78  ? 156 ILE A CG2   1 
ATOM   1239 C  CD1   . ILE A 1 156 ? -11.640 -3.090  -11.994 1.00 61.60  ? 156 ILE A CD1   1 
ATOM   1240 N  N     . GLY A 1 157 ? -6.589  -3.735  -9.419  1.00 47.42  ? 157 GLY A N     1 
ATOM   1241 C  CA    . GLY A 1 157 ? -5.221  -4.179  -9.538  1.00 55.11  ? 157 GLY A CA    1 
ATOM   1242 C  C     . GLY A 1 157 ? -5.151  -5.645  -9.922  1.00 56.97  ? 157 GLY A C     1 
ATOM   1243 O  O     . GLY A 1 157 ? -6.114  -6.400  -9.782  1.00 52.69  ? 157 GLY A O     1 
ATOM   1244 N  N     . ILE A 1 158 ? -3.981  -6.036  -10.420 1.00 56.05  ? 158 ILE A N     1 
ATOM   1245 C  CA    . ILE A 1 158 ? -3.691  -7.416  -10.797 1.00 48.38  ? 158 ILE A CA    1 
ATOM   1246 C  C     . ILE A 1 158 ? -2.427  -7.827  -10.059 1.00 47.41  ? 158 ILE A C     1 
ATOM   1247 O  O     . ILE A 1 158 ? -1.346  -7.288  -10.329 1.00 47.88  ? 158 ILE A O     1 
ATOM   1248 C  CB    . ILE A 1 158 ? -3.509  -7.582  -12.313 1.00 48.76  ? 158 ILE A CB    1 
ATOM   1249 C  CG1   . ILE A 1 158 ? -4.829  -7.347  -13.047 1.00 54.15  ? 158 ILE A CG1   1 
ATOM   1250 C  CG2   . ILE A 1 158 ? -2.959  -8.962  -12.631 1.00 53.27  ? 158 ILE A CG2   1 
ATOM   1251 C  CD1   . ILE A 1 158 ? -5.901  -8.359  -12.715 1.00 57.96  ? 158 ILE A CD1   1 
ATOM   1252 N  N     . GLU A 1 159 ? -2.550  -8.772  -9.132  1.00 47.98  ? 159 GLU A N     1 
ATOM   1253 C  CA    . GLU A 1 159 ? -1.389  -9.301  -8.430  1.00 44.68  ? 159 GLU A CA    1 
ATOM   1254 C  C     . GLU A 1 159 ? -1.001  -10.649 -9.019  1.00 46.09  ? 159 GLU A C     1 
ATOM   1255 O  O     . GLU A 1 159 ? -1.841  -11.546 -9.145  1.00 48.69  ? 159 GLU A O     1 
ATOM   1256 C  CB    . GLU A 1 159 ? -1.639  -9.440  -6.928  1.00 39.04  ? 159 GLU A CB    1 
ATOM   1257 C  CG    . GLU A 1 159 ? -0.463  -10.102 -6.214  1.00 45.37  ? 159 GLU A CG    1 
ATOM   1258 C  CD    . GLU A 1 159 ? -0.324  -9.689  -4.764  1.00 47.36  ? 159 GLU A CD    1 
ATOM   1259 O  OE1   . GLU A 1 159 ? -1.178  -8.920  -4.281  1.00 49.77  ? 159 GLU A OE1   1 
ATOM   1260 O  OE2   . GLU A 1 159 ? 0.644   -10.134 -4.108  1.00 43.72  ? 159 GLU A OE2   1 
ATOM   1261 N  N     . LEU A 1 160 ? 0.267   -10.774 -9.396  1.00 45.66  ? 160 LEU A N     1 
ATOM   1262 C  CA    . LEU A 1 160 ? 0.865   -12.048 -9.761  1.00 44.47  ? 160 LEU A CA    1 
ATOM   1263 C  C     . LEU A 1 160 ? 1.706   -12.523 -8.587  1.00 47.05  ? 160 LEU A C     1 
ATOM   1264 O  O     . LEU A 1 160 ? 2.529   -11.765 -8.061  1.00 43.16  ? 160 LEU A O     1 
ATOM   1265 C  CB    . LEU A 1 160 ? 1.732   -11.921 -11.016 1.00 43.17  ? 160 LEU A CB    1 
ATOM   1266 C  CG    . LEU A 1 160 ? 1.124   -11.235 -12.239 1.00 43.77  ? 160 LEU A CG    1 
ATOM   1267 C  CD1   . LEU A 1 160 ? 2.118   -11.236 -13.387 1.00 44.66  ? 160 LEU A CD1   1 
ATOM   1268 C  CD2   . LEU A 1 160 ? -0.176  -11.905 -12.648 1.00 48.56  ? 160 LEU A CD2   1 
ATOM   1269 N  N     . THR A 1 161 ? 1.499   -13.771 -8.180  1.00 41.97  ? 161 THR A N     1 
ATOM   1270 C  CA    . THR A 1 161 ? 2.150   -14.287 -6.989  1.00 42.02  ? 161 THR A CA    1 
ATOM   1271 C  C     . THR A 1 161 ? 2.338   -15.788 -7.134  1.00 46.41  ? 161 THR A C     1 
ATOM   1272 O  O     . THR A 1 161 ? 1.574   -16.462 -7.830  1.00 45.29  ? 161 THR A O     1 
ATOM   1273 C  CB    . THR A 1 161 ? 1.334   -13.964 -5.728  1.00 45.03  ? 161 THR A CB    1 
ATOM   1274 O  OG1   . THR A 1 161 ? 2.025   -14.433 -4.563  1.00 48.02  ? 161 THR A OG1   1 
ATOM   1275 C  CG2   . THR A 1 161 ? -0.042  -14.614 -5.800  1.00 43.25  ? 161 THR A CG2   1 
ATOM   1276 N  N     . ASP A 1 162 ? 3.373   -16.302 -6.473  1.00 41.61  ? 162 ASP A N     1 
ATOM   1277 C  CA    . ASP A 1 162 ? 3.636   -17.733 -6.424  1.00 46.70  ? 162 ASP A CA    1 
ATOM   1278 C  C     . ASP A 1 162 ? 3.287   -18.329 -5.063  1.00 50.83  ? 162 ASP A C     1 
ATOM   1279 O  O     . ASP A 1 162 ? 3.816   -19.381 -4.694  1.00 45.97  ? 162 ASP A O     1 
ATOM   1280 C  CB    . ASP A 1 162 ? 5.099   -18.011 -6.775  1.00 56.11  ? 162 ASP A CB    1 
ATOM   1281 C  CG    . ASP A 1 162 ? 6.066   -17.258 -5.882  1.00 52.95  ? 162 ASP A CG    1 
ATOM   1282 O  OD1   . ASP A 1 162 ? 5.598   -16.488 -5.016  1.00 48.59  ? 162 ASP A OD1   1 
ATOM   1283 O  OD2   . ASP A 1 162 ? 7.292   -17.437 -6.045  1.00 53.57  ? 162 ASP A OD2   1 
ATOM   1284 N  N     . SER A 1 163 ? 2.400   -17.683 -4.316  1.00 48.68  ? 163 SER A N     1 
ATOM   1285 C  CA    . SER A 1 163 ? 2.103   -18.066 -2.938  1.00 49.25  ? 163 SER A CA    1 
ATOM   1286 C  C     . SER A 1 163 ? 0.608   -18.287 -2.765  1.00 46.31  ? 163 SER A C     1 
ATOM   1287 O  O     . SER A 1 163 ? -0.169  -17.312 -2.834  1.00 44.51  ? 163 SER A O     1 
ATOM   1288 C  CB    . SER A 1 163 ? 2.599   -16.997 -1.970  1.00 47.58  ? 163 SER A CB    1 
ATOM   1289 O  OG    . SER A 1 163 ? 2.086   -17.216 -0.667  1.00 51.23  ? 163 SER A OG    1 
ATOM   1290 N  N     . PRO A 1 164 ? 0.161   -19.524 -2.532  1.00 44.93  ? 164 PRO A N     1 
ATOM   1291 C  CA    . PRO A 1 164 ? -1.269  -19.739 -2.253  1.00 52.16  ? 164 PRO A CA    1 
ATOM   1292 C  C     . PRO A 1 164 ? -1.731  -19.073 -0.970  1.00 48.81  ? 164 PRO A C     1 
ATOM   1293 O  O     . PRO A 1 164 ? -2.903  -18.688 -0.868  1.00 50.54  ? 164 PRO A O     1 
ATOM   1294 C  CB    . PRO A 1 164 ? -1.383  -21.269 -2.174  1.00 51.76  ? 164 PRO A CB    1 
ATOM   1295 C  CG    . PRO A 1 164 ? -0.013  -21.726 -1.792  1.00 52.80  ? 164 PRO A CG    1 
ATOM   1296 C  CD    . PRO A 1 164 ? 0.938   -20.772 -2.460  1.00 44.68  ? 164 PRO A CD    1 
ATOM   1297 N  N     . TYR A 1 165 ? -0.844  -18.930 0.018   1.00 45.83  ? 165 TYR A N     1 
ATOM   1298 C  CA    . TYR A 1 165 ? -1.197  -18.192 1.225   1.00 46.92  ? 165 TYR A CA    1 
ATOM   1299 C  C     . TYR A 1 165 ? -1.603  -16.762 0.892   1.00 51.08  ? 165 TYR A C     1 
ATOM   1300 O  O     . TYR A 1 165 ? -2.505  -16.200 1.524   1.00 46.69  ? 165 TYR A O     1 
ATOM   1301 C  CB    . TYR A 1 165 ? -0.023  -18.205 2.206   1.00 44.83  ? 165 TYR A CB    1 
ATOM   1302 C  CG    . TYR A 1 165 ? -0.194  -17.272 3.386   1.00 48.51  ? 165 TYR A CG    1 
ATOM   1303 C  CD1   . TYR A 1 165 ? 0.236   -15.952 3.321   1.00 44.44  ? 165 TYR A CD1   1 
ATOM   1304 C  CD2   . TYR A 1 165 ? -0.779  -17.713 4.567   1.00 48.48  ? 165 TYR A CD2   1 
ATOM   1305 C  CE1   . TYR A 1 165 ? 0.083   -15.096 4.396   1.00 52.50  ? 165 TYR A CE1   1 
ATOM   1306 C  CE2   . TYR A 1 165 ? -0.935  -16.865 5.647   1.00 48.35  ? 165 TYR A CE2   1 
ATOM   1307 C  CZ    . TYR A 1 165 ? -0.503  -15.557 5.557   1.00 55.84  ? 165 TYR A CZ    1 
ATOM   1308 O  OH    . TYR A 1 165 ? -0.657  -14.708 6.630   1.00 59.19  ? 165 TYR A OH    1 
ATOM   1309 N  N     . VAL A 1 166 ? -0.946  -16.158 -0.101  1.00 48.79  ? 166 VAL A N     1 
ATOM   1310 C  CA    . VAL A 1 166 ? -1.272  -14.790 -0.491  1.00 40.82  ? 166 VAL A CA    1 
ATOM   1311 C  C     . VAL A 1 166 ? -2.631  -14.737 -1.176  1.00 44.11  ? 166 VAL A C     1 
ATOM   1312 O  O     . VAL A 1 166 ? -3.442  -13.842 -0.908  1.00 49.69  ? 166 VAL A O     1 
ATOM   1313 C  CB    . VAL A 1 166 ? -0.159  -14.214 -1.389  1.00 50.83  ? 166 VAL A CB    1 
ATOM   1314 C  CG1   . VAL A 1 166 ? -0.688  -13.062 -2.237  1.00 42.43  ? 166 VAL A CG1   1 
ATOM   1315 C  CG2   . VAL A 1 166 ? 1.030   -13.768 -0.545  1.00 46.75  ? 166 VAL A CG2   1 
ATOM   1316 N  N     . VAL A 1 167 ? -2.906  -15.689 -2.068  1.00 43.85  ? 167 VAL A N     1 
ATOM   1317 C  CA    . VAL A 1 167 ? -4.175  -15.679 -2.793  1.00 43.52  ? 167 VAL A CA    1 
ATOM   1318 C  C     . VAL A 1 167 ? -5.341  -15.807 -1.821  1.00 47.54  ? 167 VAL A C     1 
ATOM   1319 O  O     . VAL A 1 167 ? -6.339  -15.083 -1.920  1.00 42.92  ? 167 VAL A O     1 
ATOM   1320 C  CB    . VAL A 1 167 ? -4.197  -16.796 -3.853  1.00 52.48  ? 167 VAL A CB    1 
ATOM   1321 C  CG1   . VAL A 1 167 ? -5.540  -16.821 -4.563  1.00 50.91  ? 167 VAL A CG1   1 
ATOM   1322 C  CG2   . VAL A 1 167 ? -3.055  -16.614 -4.855  1.00 42.83  ? 167 VAL A CG2   1 
ATOM   1323 N  N     . ALA A 1 168 ? -5.234  -16.735 -0.868  1.00 49.82  ? 168 ALA A N     1 
ATOM   1324 C  CA    . ALA A 1 168 ? -6.301  -16.920 0.110   1.00 46.81  ? 168 ALA A CA    1 
ATOM   1325 C  C     . ALA A 1 168 ? -6.531  -15.647 0.911   1.00 45.85  ? 168 ALA A C     1 
ATOM   1326 O  O     . ALA A 1 168 ? -7.673  -15.205 1.086   1.00 47.30  ? 168 ALA A O     1 
ATOM   1327 C  CB    . ALA A 1 168 ? -5.965  -18.087 1.036   1.00 47.48  ? 168 ALA A CB    1 
ATOM   1328 N  N     . SER A 1 169 ? -5.450  -15.037 1.400   1.00 45.44  ? 169 SER A N     1 
ATOM   1329 C  CA    . SER A 1 169 ? -5.577  -13.801 2.164   1.00 46.15  ? 169 SER A CA    1 
ATOM   1330 C  C     . SER A 1 169 ? -6.179  -12.690 1.311   1.00 45.10  ? 169 SER A C     1 
ATOM   1331 O  O     . SER A 1 169 ? -7.091  -11.980 1.750   1.00 50.96  ? 169 SER A O     1 
ATOM   1332 C  CB    . SER A 1 169 ? -4.211  -13.388 2.713   1.00 46.73  ? 169 SER A CB    1 
ATOM   1333 O  OG    . SER A 1 169 ? -3.597  -14.468 3.399   1.00 49.16  ? 169 SER A OG    1 
ATOM   1334 N  N     . MET A 1 170 ? -5.682  -12.528 0.081   1.00 43.63  ? 170 MET A N     1 
ATOM   1335 C  CA    . MET A 1 170 ? -6.222  -11.497 -0.799  1.00 45.22  ? 170 MET A CA    1 
ATOM   1336 C  C     . MET A 1 170 ? -7.704  -11.713 -1.075  1.00 42.95  ? 170 MET A C     1 
ATOM   1337 O  O     . MET A 1 170 ? -8.442  -10.744 -1.281  1.00 49.38  ? 170 MET A O     1 
ATOM   1338 C  CB    . MET A 1 170 ? -5.436  -11.454 -2.112  1.00 41.80  ? 170 MET A CB    1 
ATOM   1339 C  CG    . MET A 1 170 ? -4.039  -10.846 -1.995  1.00 42.10  ? 170 MET A CG    1 
ATOM   1340 S  SD    . MET A 1 170 ? -4.013  -9.037  -1.897  1.00 40.99  ? 170 MET A SD    1 
ATOM   1341 C  CE    . MET A 1 170 ? -4.639  -8.580  -3.515  1.00 39.63  ? 170 MET A CE    1 
ATOM   1342 N  N     . ARG A 1 171 ? -8.163  -12.967 -1.082  1.00 50.43  ? 171 ARG A N     1 
ATOM   1343 C  CA    . ARG A 1 171 ? -9.591  -13.206 -1.261  1.00 52.16  ? 171 ARG A CA    1 
ATOM   1344 C  C     . ARG A 1 171 ? -10.393 -12.625 -0.108  1.00 46.91  ? 171 ARG A C     1 
ATOM   1345 O  O     . ARG A 1 171 ? -11.556 -12.245 -0.287  1.00 50.29  ? 171 ARG A O     1 
ATOM   1346 C  CB    . ARG A 1 171 ? -9.877  -14.703 -1.399  1.00 47.86  ? 171 ARG A CB    1 
ATOM   1347 C  CG    . ARG A 1 171 ? -11.335 -15.010 -1.737  1.00 51.44  ? 171 ARG A CG    1 
ATOM   1348 C  CD    . ARG A 1 171 ? -11.591 -16.505 -1.886  1.00 53.24  ? 171 ARG A CD    1 
ATOM   1349 N  NE    . ARG A 1 171 ? -12.939 -16.779 -2.371  1.00 56.62  ? 171 ARG A NE    1 
ATOM   1350 C  CZ    . ARG A 1 171 ? -14.016 -16.859 -1.598  1.00 68.14  ? 171 ARG A CZ    1 
ATOM   1351 N  NH1   . ARG A 1 171 ? -13.943 -16.681 -0.289  1.00 69.12  ? 171 ARG A NH1   1 
ATOM   1352 N  NH2   . ARG A 1 171 ? -15.196 -17.120 -2.154  1.00 62.55  ? 171 ARG A NH2   1 
ATOM   1353 N  N     . ILE A 1 172 ? -9.793  -12.544 1.074   1.00 41.91  ? 172 ILE A N     1 
ATOM   1354 C  CA    . ILE A 1 172 ? -10.461 -11.965 2.232   1.00 50.06  ? 172 ILE A CA    1 
ATOM   1355 C  C     . ILE A 1 172 ? -10.302 -10.452 2.259   1.00 49.80  ? 172 ILE A C     1 
ATOM   1356 O  O     . ILE A 1 172 ? -11.267 -9.715  2.477   1.00 54.45  ? 172 ILE A O     1 
ATOM   1357 C  CB    . ILE A 1 172 ? -9.920  -12.610 3.527   1.00 45.42  ? 172 ILE A CB    1 
ATOM   1358 C  CG1   . ILE A 1 172 ? -10.161 -14.121 3.510   1.00 44.68  ? 172 ILE A CG1   1 
ATOM   1359 C  CG2   . ILE A 1 172 ? -10.569 -11.980 4.742   1.00 49.79  ? 172 ILE A CG2   1 
ATOM   1360 C  CD1   . ILE A 1 172 ? -9.471  -14.864 4.638   1.00 49.83  ? 172 ILE A CD1   1 
ATOM   1361 N  N     . MET A 1 173 ? -9.086  -9.964  2.016   1.00 50.83  ? 173 MET A N     1 
ATOM   1362 C  CA    . MET A 1 173 ? -8.809  -8.547  2.209   1.00 46.48  ? 173 MET A CA    1 
ATOM   1363 C  C     . MET A 1 173 ? -9.351  -7.681  1.076   1.00 48.15  ? 173 MET A C     1 
ATOM   1364 O  O     . MET A 1 173 ? -9.647  -6.502  1.299   1.00 55.95  ? 173 MET A O     1 
ATOM   1365 C  CB    . MET A 1 173 ? -7.304  -8.332  2.379   1.00 45.41  ? 173 MET A CB    1 
ATOM   1366 C  CG    . MET A 1 173 ? -6.751  -8.927  3.671   1.00 41.73  ? 173 MET A CG    1 
ATOM   1367 S  SD    . MET A 1 173 ? -7.644  -8.340  5.134   1.00 51.28  ? 173 MET A SD    1 
ATOM   1368 C  CE    . MET A 1 173 ? -7.285  -6.589  5.060   1.00 47.83  ? 173 MET A CE    1 
ATOM   1369 N  N     . THR A 1 174 ? -9.501  -8.224  -0.126  1.00 44.11  ? 174 THR A N     1 
ATOM   1370 C  CA    . THR A 1 174 ? -9.987  -7.443  -1.257  1.00 48.61  ? 174 THR A CA    1 
ATOM   1371 C  C     . THR A 1 174 ? -11.219 -8.105  -1.864  1.00 53.54  ? 174 THR A C     1 
ATOM   1372 O  O     . THR A 1 174 ? -11.702 -9.137  -1.389  1.00 49.24  ? 174 THR A O     1 
ATOM   1373 C  CB    . THR A 1 174 ? -8.903  -7.275  -2.327  1.00 47.11  ? 174 THR A CB    1 
ATOM   1374 O  OG1   . THR A 1 174 ? -8.680  -8.529  -2.985  1.00 48.74  ? 174 THR A OG1   1 
ATOM   1375 C  CG2   . THR A 1 174 ? -7.602  -6.790  -1.707  1.00 43.61  ? 174 THR A CG2   1 
ATOM   1376 N  N     . ARG A 1 175 ? -11.729 -7.483  -2.926  1.00 48.68  ? 175 ARG A N     1 
ATOM   1377 C  CA    . ARG A 1 175 ? -12.744 -8.077  -3.788  1.00 53.97  ? 175 ARG A CA    1 
ATOM   1378 C  C     . ARG A 1 175 ? -12.019 -8.723  -4.965  1.00 59.99  ? 175 ARG A C     1 
ATOM   1379 O  O     . ARG A 1 175 ? -11.517 -8.025  -5.853  1.00 55.05  ? 175 ARG A O     1 
ATOM   1380 C  CB    . ARG A 1 175 ? -13.750 -7.033  -4.267  1.00 53.02  ? 175 ARG A CB    1 
ATOM   1381 C  CG    . ARG A 1 175 ? -14.795 -6.623  -3.238  1.00 57.79  ? 175 ARG A CG    1 
ATOM   1382 C  CD    . ARG A 1 175 ? -14.317 -5.488  -2.352  1.00 58.73  ? 175 ARG A CD    1 
ATOM   1383 N  NE    . ARG A 1 175 ? -15.408 -4.959  -1.541  1.00 65.46  ? 175 ARG A NE    1 
ATOM   1384 C  CZ    . ARG A 1 175 ? -15.290 -3.955  -0.683  1.00 67.34  ? 175 ARG A CZ    1 
ATOM   1385 N  NH1   . ARG A 1 175 ? -14.136 -3.333  -0.500  1.00 59.61  ? 175 ARG A NH1   1 
ATOM   1386 N  NH2   . ARG A 1 175 ? -16.355 -3.568  0.013   1.00 70.16  ? 175 ARG A NH2   1 
ATOM   1387 N  N     . MET A 1 176 ? -11.963 -10.051 -4.970  1.00 56.88  ? 176 MET A N     1 
ATOM   1388 C  CA    . MET A 1 176 ? -11.142 -10.804 -5.908  1.00 60.91  ? 176 MET A CA    1 
ATOM   1389 C  C     . MET A 1 176 ? -12.003 -11.792 -6.680  1.00 58.88  ? 176 MET A C     1 
ATOM   1390 O  O     . MET A 1 176 ? -12.912 -12.407 -6.116  1.00 64.89  ? 176 MET A O     1 
ATOM   1391 C  CB    . MET A 1 176 ? -10.023 -11.545 -5.163  1.00 55.66  ? 176 MET A CB    1 
ATOM   1392 C  CG    . MET A 1 176 ? -9.026  -12.255 -6.058  1.00 60.94  ? 176 MET A CG    1 
ATOM   1393 S  SD    . MET A 1 176 ? -9.425  -13.992 -6.279  1.00 62.17  ? 176 MET A SD    1 
ATOM   1394 C  CE    . MET A 1 176 ? -9.212  -14.611 -4.610  1.00 55.31  ? 176 MET A CE    1 
ATOM   1395 N  N     . GLY A 1 177 ? -11.724 -11.938 -7.967  1.00 59.91  ? 177 GLY A N     1 
ATOM   1396 C  CA    . GLY A 1 177 ? -12.381 -12.953 -8.762  1.00 62.51  ? 177 GLY A CA    1 
ATOM   1397 C  C     . GLY A 1 177 ? -12.613 -12.488 -10.186 1.00 62.38  ? 177 GLY A C     1 
ATOM   1398 O  O     . GLY A 1 177 ? -12.118 -11.450 -10.616 1.00 60.44  ? 177 GLY A O     1 
ATOM   1399 N  N     . THR A 1 178 ? -13.399 -13.294 -10.904 1.00 64.96  ? 178 THR A N     1 
ATOM   1400 C  CA    . THR A 1 178 ? -13.615 -13.068 -12.330 1.00 67.91  ? 178 THR A CA    1 
ATOM   1401 C  C     . THR A 1 178 ? -14.432 -11.808 -12.581 1.00 67.87  ? 178 THR A C     1 
ATOM   1402 O  O     . THR A 1 178 ? -14.205 -11.103 -13.572 1.00 70.58  ? 178 THR A O     1 
ATOM   1403 C  CB    . THR A 1 178 ? -14.304 -14.285 -12.947 1.00 63.98  ? 178 THR A CB    1 
ATOM   1404 O  OG1   . THR A 1 178 ? -13.483 -15.442 -12.758 1.00 61.65  ? 178 THR A OG1   1 
ATOM   1405 C  CG2   . THR A 1 178 ? -14.539 -14.075 -14.434 1.00 70.83  ? 178 THR A CG2   1 
ATOM   1406 N  N     . SER A 1 179 ? -15.394 -11.512 -11.704 1.00 69.39  ? 179 SER A N     1 
ATOM   1407 C  CA    . SER A 1 179 ? -16.208 -10.316 -11.890 1.00 73.19  ? 179 SER A CA    1 
ATOM   1408 C  C     . SER A 1 179 ? -15.353 -9.057  -11.918 1.00 69.93  ? 179 SER A C     1 
ATOM   1409 O  O     . SER A 1 179 ? -15.747 -8.053  -12.522 1.00 72.06  ? 179 SER A O     1 
ATOM   1410 C  CB    . SER A 1 179 ? -17.264 -10.219 -10.789 1.00 68.92  ? 179 SER A CB    1 
ATOM   1411 O  OG    . SER A 1 179 ? -16.658 -10.097 -9.515  1.00 74.16  ? 179 SER A OG    1 
ATOM   1412 N  N     . VAL A 1 180 ? -14.186 -9.088  -11.271 1.00 69.12  ? 180 VAL A N     1 
ATOM   1413 C  CA    . VAL A 1 180 ? -13.276 -7.950  -11.332 1.00 69.98  ? 180 VAL A CA    1 
ATOM   1414 C  C     . VAL A 1 180 ? -12.699 -7.805  -12.735 1.00 72.55  ? 180 VAL A C     1 
ATOM   1415 O  O     . VAL A 1 180 ? -12.526 -6.688  -13.237 1.00 71.43  ? 180 VAL A O     1 
ATOM   1416 C  CB    . VAL A 1 180 ? -12.166 -8.092  -10.274 1.00 61.91  ? 180 VAL A CB    1 
ATOM   1417 C  CG1   . VAL A 1 180 ? -11.148 -6.974  -10.423 1.00 65.49  ? 180 VAL A CG1   1 
ATOM   1418 C  CG2   . VAL A 1 180 ? -12.762 -8.078  -8.881  1.00 58.79  ? 180 VAL A CG2   1 
ATOM   1419 N  N     . LEU A 1 181 ? -12.394 -8.927  -13.392 1.00 71.52  ? 181 LEU A N     1 
ATOM   1420 C  CA    . LEU A 1 181 ? -11.883 -8.867  -14.758 1.00 72.22  ? 181 LEU A CA    1 
ATOM   1421 C  C     . LEU A 1 181 ? -12.881 -8.199  -15.693 1.00 74.88  ? 181 LEU A C     1 
ATOM   1422 O  O     . LEU A 1 181 ? -12.501 -7.377  -16.536 1.00 73.75  ? 181 LEU A O     1 
ATOM   1423 C  CB    . LEU A 1 181 ? -11.548 -10.272 -15.262 1.00 73.39  ? 181 LEU A CB    1 
ATOM   1424 C  CG    . LEU A 1 181 ? -10.128 -10.793 -15.042 1.00 71.85  ? 181 LEU A CG    1 
ATOM   1425 C  CD1   . LEU A 1 181 ? -9.981  -12.195 -15.615 1.00 68.38  ? 181 LEU A CD1   1 
ATOM   1426 C  CD2   . LEU A 1 181 ? -9.122  -9.851  -15.674 1.00 73.28  ? 181 LEU A CD2   1 
ATOM   1427 N  N     . GLU A 1 182 ? -14.163 -8.544  -15.566 1.00 81.60  ? 182 GLU A N     1 
ATOM   1428 C  CA    . GLU A 1 182 ? -15.165 -7.986  -16.466 1.00 85.01  ? 182 GLU A CA    1 
ATOM   1429 C  C     . GLU A 1 182 ? -15.371 -6.498  -16.210 1.00 86.36  ? 182 GLU A C     1 
ATOM   1430 O  O     . GLU A 1 182 ? -15.501 -5.712  -17.156 1.00 86.44  ? 182 GLU A O     1 
ATOM   1431 C  CB    . GLU A 1 182 ? -16.476 -8.757  -16.324 1.00 88.94  ? 182 GLU A CB    1 
ATOM   1432 C  CG    . GLU A 1 182 ? -16.347 -10.227 -16.694 1.00 96.13  ? 182 GLU A CG    1 
ATOM   1433 C  CD    . GLU A 1 182 ? -17.632 -11.004 -16.491 1.00 109.32 ? 182 GLU A CD    1 
ATOM   1434 O  OE1   . GLU A 1 182 ? -18.518 -10.514 -15.760 1.00 114.90 ? 182 GLU A OE1   1 
ATOM   1435 O  OE2   . GLU A 1 182 ? -17.754 -12.106 -17.065 1.00 114.90 ? 182 GLU A OE2   1 
ATOM   1436 N  N     . ALA A 1 183 ? -15.398 -6.091  -14.939 1.00 82.48  ? 183 ALA A N     1 
ATOM   1437 C  CA    . ALA A 1 183 ? -15.515 -4.671  -14.627 1.00 74.06  ? 183 ALA A CA    1 
ATOM   1438 C  C     . ALA A 1 183 ? -14.348 -3.885  -15.210 1.00 73.94  ? 183 ALA A C     1 
ATOM   1439 O  O     . ALA A 1 183 ? -14.542 -2.813  -15.794 1.00 79.79  ? 183 ALA A O     1 
ATOM   1440 C  CB    . ALA A 1 183 ? -15.599 -4.468  -13.114 1.00 74.17  ? 183 ALA A CB    1 
ATOM   1441 N  N     . LEU A 1 184 ? -13.128 -4.410  -15.073 1.00 73.59  ? 184 LEU A N     1 
ATOM   1442 C  CA    . LEU A 1 184 ? -11.956 -3.705  -15.581 1.00 75.00  ? 184 LEU A CA    1 
ATOM   1443 C  C     . LEU A 1 184 ? -12.060 -3.468  -17.082 1.00 76.49  ? 184 LEU A C     1 
ATOM   1444 O  O     . LEU A 1 184 ? -11.806 -2.359  -17.567 1.00 77.36  ? 184 LEU A O     1 
ATOM   1445 C  CB    . LEU A 1 184 ? -10.686 -4.489  -15.253 1.00 69.75  ? 184 LEU A CB    1 
ATOM   1446 C  CG    . LEU A 1 184 ? -9.420  -3.973  -15.941 1.00 75.14  ? 184 LEU A CG    1 
ATOM   1447 C  CD1   . LEU A 1 184 ? -9.090  -2.563  -15.474 1.00 70.19  ? 184 LEU A CD1   1 
ATOM   1448 C  CD2   . LEU A 1 184 ? -8.246  -4.912  -15.705 1.00 65.35  ? 184 LEU A CD2   1 
ATOM   1449 N  N     . GLY A 1 185 ? -12.430 -4.496  -17.832 1.00 75.55  ? 185 GLY A N     1 
ATOM   1450 C  CA    . GLY A 1 185 ? -12.456 -4.366  -19.279 1.00 78.67  ? 185 GLY A CA    1 
ATOM   1451 C  C     . GLY A 1 185 ? -11.075 -4.002  -19.784 1.00 85.05  ? 185 GLY A C     1 
ATOM   1452 O  O     . GLY A 1 185 ? -10.088 -4.700  -19.520 1.00 85.88  ? 185 GLY A O     1 
ATOM   1453 N  N     . ASP A 1 186 ? -10.989 -2.892  -20.514 1.00 87.71  ? 186 ASP A N     1 
ATOM   1454 C  CA    . ASP A 1 186 ? -9.717  -2.362  -20.985 1.00 88.42  ? 186 ASP A CA    1 
ATOM   1455 C  C     . ASP A 1 186 ? -9.250  -1.156  -20.182 1.00 83.41  ? 186 ASP A C     1 
ATOM   1456 O  O     . ASP A 1 186 ? -8.302  -0.480  -20.593 1.00 83.28  ? 186 ASP A O     1 
ATOM   1457 C  CB    . ASP A 1 186 ? -9.809  -1.998  -22.468 1.00 90.58  ? 186 ASP A CB    1 
ATOM   1458 C  CG    . ASP A 1 186 ? -9.687  -3.208  -23.371 1.00 96.46  ? 186 ASP A CG    1 
ATOM   1459 O  OD1   . ASP A 1 186 ? -9.054  -4.202  -22.954 1.00 94.42  ? 186 ASP A OD1   1 
ATOM   1460 O  OD2   . ASP A 1 186 ? -10.219 -3.165  -24.500 1.00 105.10 ? 186 ASP A OD2   1 
ATOM   1461 N  N     . GLY A 1 187 ? -9.889  -0.868  -19.054 1.00 78.25  ? 187 GLY A N     1 
ATOM   1462 C  CA    . GLY A 1 187 ? -9.437  0.211   -18.200 1.00 79.14  ? 187 GLY A CA    1 
ATOM   1463 C  C     . GLY A 1 187 ? -8.044  -0.047  -17.660 1.00 78.40  ? 187 GLY A C     1 
ATOM   1464 O  O     . GLY A 1 187 ? -7.477  -1.133  -17.773 1.00 78.92  ? 187 GLY A O     1 
ATOM   1465 N  N     . GLU A 1 188 ? -7.476  0.996   -17.062 1.00 81.13  ? 188 GLU A N     1 
ATOM   1466 C  CA    . GLU A 1 188 ? -6.161  0.864   -16.458 1.00 78.64  ? 188 GLU A CA    1 
ATOM   1467 C  C     . GLU A 1 188 ? -6.238  0.011   -15.194 1.00 72.22  ? 188 GLU A C     1 
ATOM   1468 O  O     . GLU A 1 188 ? -7.311  -0.224  -14.632 1.00 73.83  ? 188 GLU A O     1 
ATOM   1469 C  CB    . GLU A 1 188 ? -5.577  2.239   -16.132 1.00 84.03  ? 188 GLU A CB    1 
ATOM   1470 C  CG    . GLU A 1 188 ? -5.382  3.135   -17.345 1.00 96.16  ? 188 GLU A CG    1 
ATOM   1471 C  CD    . GLU A 1 188 ? -4.689  4.438   -16.999 1.00 109.32 ? 188 GLU A CD    1 
ATOM   1472 O  OE1   . GLU A 1 188 ? -4.306  4.614   -15.823 1.00 103.03 ? 188 GLU A OE1   1 
ATOM   1473 O  OE2   . GLU A 1 188 ? -4.527  5.284   -17.904 1.00 118.93 ? 188 GLU A OE2   1 
ATOM   1474 N  N     . PHE A 1 189 ? -5.075  -0.458  -14.750 1.00 60.61  ? 189 PHE A N     1 
ATOM   1475 C  CA    . PHE A 1 189 ? -4.992  -1.233  -13.522 1.00 59.66  ? 189 PHE A CA    1 
ATOM   1476 C  C     . PHE A 1 189 ? -3.595  -1.093  -12.938 1.00 56.37  ? 189 PHE A C     1 
ATOM   1477 O  O     . PHE A 1 189 ? -2.652  -0.679  -13.617 1.00 60.38  ? 189 PHE A O     1 
ATOM   1478 C  CB    . PHE A 1 189 ? -5.330  -2.710  -13.759 1.00 63.50  ? 189 PHE A CB    1 
ATOM   1479 C  CG    . PHE A 1 189 ? -4.378  -3.411  -14.687 1.00 63.65  ? 189 PHE A CG    1 
ATOM   1480 C  CD1   . PHE A 1 189 ? -4.543  -3.329  -16.060 1.00 60.83  ? 189 PHE A CD1   1 
ATOM   1481 C  CD2   . PHE A 1 189 ? -3.323  -4.156  -14.186 1.00 54.86  ? 189 PHE A CD2   1 
ATOM   1482 C  CE1   . PHE A 1 189 ? -3.671  -3.973  -16.918 1.00 58.07  ? 189 PHE A CE1   1 
ATOM   1483 C  CE2   . PHE A 1 189 ? -2.447  -4.801  -15.037 1.00 51.81  ? 189 PHE A CE2   1 
ATOM   1484 C  CZ    . PHE A 1 189 ? -2.622  -4.709  -16.405 1.00 62.33  ? 189 PHE A CZ    1 
ATOM   1485 N  N     . ILE A 1 190 ? -3.478  -1.438  -11.662 1.00 54.01  ? 190 ILE A N     1 
ATOM   1486 C  CA    . ILE A 1 190 ? -2.196  -1.437  -10.968 1.00 55.20  ? 190 ILE A CA    1 
ATOM   1487 C  C     . ILE A 1 190 ? -1.529  -2.788  -11.183 1.00 56.16  ? 190 ILE A C     1 
ATOM   1488 O  O     . ILE A 1 190 ? -2.135  -3.838  -10.937 1.00 59.81  ? 190 ILE A O     1 
ATOM   1489 C  CB    . ILE A 1 190 ? -2.383  -1.147  -9.470  1.00 52.81  ? 190 ILE A CB    1 
ATOM   1490 C  CG1   . ILE A 1 190 ? -3.144  0.166   -9.275  1.00 58.41  ? 190 ILE A CG1   1 
ATOM   1491 C  CG2   . ILE A 1 190 ? -1.037  -1.114  -8.761  1.00 50.13  ? 190 ILE A CG2   1 
ATOM   1492 C  CD1   . ILE A 1 190 ? -2.467  1.366   -9.895  1.00 60.31  ? 190 ILE A CD1   1 
ATOM   1493 N  N     . LYS A 1 191 ? -0.284  -2.765  -11.650 1.00 56.06  ? 191 LYS A N     1 
ATOM   1494 C  CA    . LYS A 1 191 ? 0.488   -3.982  -11.863 1.00 49.17  ? 191 LYS A CA    1 
ATOM   1495 C  C     . LYS A 1 191 ? 1.199   -4.351  -10.568 1.00 51.41  ? 191 LYS A C     1 
ATOM   1496 O  O     . LYS A 1 191 ? 2.011   -3.573  -10.055 1.00 55.07  ? 191 LYS A O     1 
ATOM   1497 C  CB    . LYS A 1 191 ? 1.494   -3.794  -12.996 1.00 50.71  ? 191 LYS A CB    1 
ATOM   1498 C  CG    . LYS A 1 191 ? 0.870   -3.361  -14.309 1.00 57.30  ? 191 LYS A CG    1 
ATOM   1499 C  CD    . LYS A 1 191 ? 1.916   -2.794  -15.254 1.00 59.21  ? 191 LYS A CD    1 
ATOM   1500 C  CE    . LYS A 1 191 ? 1.275   -2.233  -16.510 1.00 64.97  ? 191 LYS A CE    1 
ATOM   1501 N  NZ    . LYS A 1 191 ? 2.291   -1.657  -17.432 1.00 77.91  ? 191 LYS A NZ    1 
ATOM   1502 N  N     . CYS A 1 192 ? 0.893   -5.533  -10.042 1.00 45.43  ? 192 CYS A N     1 
ATOM   1503 C  CA    . CYS A 1 192 ? 1.481   -6.021  -8.804  1.00 49.38  ? 192 CYS A CA    1 
ATOM   1504 C  C     . CYS A 1 192 ? 2.179   -7.343  -9.074  1.00 50.76  ? 192 CYS A C     1 
ATOM   1505 O  O     . CYS A 1 192 ? 1.586   -8.253  -9.661  1.00 49.63  ? 192 CYS A O     1 
ATOM   1506 C  CB    . CYS A 1 192 ? 0.418   -6.193  -7.720  1.00 47.10  ? 192 CYS A CB    1 
ATOM   1507 S  SG    . CYS A 1 192 ? -0.541  -4.700  -7.418  1.00 48.98  ? 192 CYS A SG    1 
ATOM   1508 N  N     . LEU A 1 193 ? 3.435   -7.440  -8.649  1.00 45.36  ? 193 LEU A N     1 
ATOM   1509 C  CA    . LEU A 1 193 ? 4.247   -8.630  -8.853  1.00 46.74  ? 193 LEU A CA    1 
ATOM   1510 C  C     . LEU A 1 193 ? 4.848   -9.041  -7.522  1.00 50.78  ? 193 LEU A C     1 
ATOM   1511 O  O     . LEU A 1 193 ? 5.506   -8.232  -6.859  1.00 48.46  ? 193 LEU A O     1 
ATOM   1512 C  CB    . LEU A 1 193 ? 5.355   -8.381  -9.881  1.00 46.95  ? 193 LEU A CB    1 
ATOM   1513 C  CG    . LEU A 1 193 ? 6.327   -9.532  -10.144 1.00 49.61  ? 193 LEU A CG    1 
ATOM   1514 C  CD1   . LEU A 1 193 ? 5.597   -10.733 -10.724 1.00 45.84  ? 193 LEU A CD1   1 
ATOM   1515 C  CD2   . LEU A 1 193 ? 7.441   -9.081  -11.076 1.00 55.47  ? 193 LEU A CD2   1 
ATOM   1516 N  N     . HIS A 1 194 ? 4.621   -10.292 -7.130  1.00 49.33  ? 194 HIS A N     1 
ATOM   1517 C  CA    . HIS A 1 194 ? 5.160   -10.799 -5.881  1.00 46.89  ? 194 HIS A CA    1 
ATOM   1518 C  C     . HIS A 1 194 ? 5.733   -12.191 -6.085  1.00 48.10  ? 194 HIS A C     1 
ATOM   1519 O  O     . HIS A 1 194 ? 5.175   -13.003 -6.828  1.00 51.81  ? 194 HIS A O     1 
ATOM   1520 C  CB    . HIS A 1 194 ? 4.100   -10.847 -4.775  1.00 46.20  ? 194 HIS A CB    1 
ATOM   1521 C  CG    . HIS A 1 194 ? 4.575   -11.528 -3.532  1.00 42.12  ? 194 HIS A CG    1 
ATOM   1522 N  ND1   . HIS A 1 194 ? 4.237   -12.828 -3.220  1.00 43.10  ? 194 HIS A ND1   1 
ATOM   1523 C  CD2   . HIS A 1 194 ? 5.394   -11.104 -2.541  1.00 45.75  ? 194 HIS A CD2   1 
ATOM   1524 C  CE1   . HIS A 1 194 ? 4.813   -13.168 -2.081  1.00 52.51  ? 194 HIS A CE1   1 
ATOM   1525 N  NE2   . HIS A 1 194 ? 5.522   -12.140 -1.649  1.00 56.20  ? 194 HIS A NE2   1 
ATOM   1526 N  N     . SER A 1 195 ? 6.847   -12.459 -5.408  1.00 43.68  ? 195 SER A N     1 
ATOM   1527 C  CA    . SER A 1 195 ? 7.423   -13.791 -5.361  1.00 51.70  ? 195 SER A CA    1 
ATOM   1528 C  C     . SER A 1 195 ? 8.100   -13.979 -4.014  1.00 54.82  ? 195 SER A C     1 
ATOM   1529 O  O     . SER A 1 195 ? 8.786   -13.077 -3.524  1.00 51.74  ? 195 SER A O     1 
ATOM   1530 C  CB    . SER A 1 195 ? 8.429   -14.017 -6.496  1.00 50.27  ? 195 SER A CB    1 
ATOM   1531 O  OG    . SER A 1 195 ? 9.068   -15.275 -6.363  1.00 53.18  ? 195 SER A OG    1 
ATOM   1532 N  N     . VAL A 1 196 ? 7.894   -15.156 -3.416  1.00 50.46  ? 196 VAL A N     1 
ATOM   1533 C  CA    . VAL A 1 196 ? 8.615   -15.502 -2.200  1.00 51.97  ? 196 VAL A CA    1 
ATOM   1534 C  C     . VAL A 1 196 ? 10.105  -15.661 -2.470  1.00 62.41  ? 196 VAL A C     1 
ATOM   1535 O  O     . VAL A 1 196 ? 10.912  -15.589 -1.535  1.00 68.73  ? 196 VAL A O     1 
ATOM   1536 C  CB    . VAL A 1 196 ? 8.033   -16.784 -1.574  1.00 62.85  ? 196 VAL A CB    1 
ATOM   1537 C  CG1   . VAL A 1 196 ? 6.570   -16.578 -1.198  1.00 52.97  ? 196 VAL A CG1   1 
ATOM   1538 C  CG2   . VAL A 1 196 ? 8.185   -17.962 -2.531  1.00 54.16  ? 196 VAL A CG2   1 
ATOM   1539 N  N     . GLY A 1 197 ? 10.492  -15.883 -3.725  1.00 56.70  ? 197 GLY A N     1 
ATOM   1540 C  CA    . GLY A 1 197 ? 11.895  -15.953 -4.081  1.00 58.87  ? 197 GLY A CA    1 
ATOM   1541 C  C     . GLY A 1 197 ? 12.576  -17.270 -3.788  1.00 66.72  ? 197 GLY A C     1 
ATOM   1542 O  O     . GLY A 1 197 ? 13.797  -17.297 -3.603  1.00 69.77  ? 197 GLY A O     1 
ATOM   1543 N  N     . CYS A 1 198 ? 11.824  -18.369 -3.739  1.00 62.19  ? 198 CYS A N     1 
ATOM   1544 C  CA    . CYS A 1 198 ? 12.376  -19.699 -3.493  1.00 62.33  ? 198 CYS A CA    1 
ATOM   1545 C  C     . CYS A 1 198 ? 11.998  -20.614 -4.651  1.00 69.64  ? 198 CYS A C     1 
ATOM   1546 O  O     . CYS A 1 198 ? 11.149  -21.504 -4.506  1.00 68.96  ? 198 CYS A O     1 
ATOM   1547 C  CB    . CYS A 1 198 ? 11.887  -20.274 -2.166  1.00 67.84  ? 198 CYS A CB    1 
ATOM   1548 S  SG    . CYS A 1 198 ? 12.622  -19.491 -0.719  1.00 83.84  ? 198 CYS A SG    1 
ATOM   1549 N  N     . PRO A 1 199 ? 12.612  -20.420 -5.816  1.00 70.57  ? 199 PRO A N     1 
ATOM   1550 C  CA    . PRO A 1 199 ? 12.346  -21.321 -6.940  1.00 67.10  ? 199 PRO A CA    1 
ATOM   1551 C  C     . PRO A 1 199 ? 12.827  -22.728 -6.627  1.00 72.03  ? 199 PRO A C     1 
ATOM   1552 O  O     . PRO A 1 199 ? 13.744  -22.934 -5.830  1.00 75.03  ? 199 PRO A O     1 
ATOM   1553 C  CB    . PRO A 1 199 ? 13.144  -20.697 -8.091  1.00 70.16  ? 199 PRO A CB    1 
ATOM   1554 C  CG    . PRO A 1 199 ? 14.237  -19.934 -7.411  1.00 70.17  ? 199 PRO A CG    1 
ATOM   1555 C  CD    . PRO A 1 199 ? 13.620  -19.400 -6.148  1.00 64.54  ? 199 PRO A CD    1 
ATOM   1556 N  N     . LEU A 1 200 ? 12.188  -23.702 -7.263  1.00 74.06  ? 200 LEU A N     1 
ATOM   1557 C  CA    . LEU A 1 200 ? 12.570  -25.088 -7.037  1.00 79.81  ? 200 LEU A CA    1 
ATOM   1558 C  C     . LEU A 1 200 ? 13.547  -25.551 -8.109  1.00 83.79  ? 200 LEU A C     1 
ATOM   1559 O  O     . LEU A 1 200 ? 13.429  -25.145 -9.271  1.00 83.84  ? 200 LEU A O     1 
ATOM   1560 C  CB    . LEU A 1 200 ? 11.336  -25.991 -7.045  1.00 74.11  ? 200 LEU A CB    1 
ATOM   1561 C  CG    . LEU A 1 200 ? 10.197  -25.503 -6.147  1.00 72.11  ? 200 LEU A CG    1 
ATOM   1562 C  CD1   . LEU A 1 200 ? 8.970   -26.392 -6.284  1.00 71.55  ? 200 LEU A CD1   1 
ATOM   1563 C  CD2   . LEU A 1 200 ? 10.657  -25.431 -4.699  1.00 74.47  ? 200 LEU A CD2   1 
ATOM   1564 N  N     . PRO A 1 201 ? 14.519  -26.409 -7.766  1.00 87.91  ? 201 PRO A N     1 
ATOM   1565 C  CA    . PRO A 1 201 ? 14.718  -27.082 -6.471  1.00 92.90  ? 201 PRO A CA    1 
ATOM   1566 C  C     . PRO A 1 201 ? 15.116  -26.128 -5.349  1.00 93.63  ? 201 PRO A C     1 
ATOM   1567 O  O     . PRO A 1 201 ? 15.859  -25.173 -5.563  1.00 94.99  ? 201 PRO A O     1 
ATOM   1568 C  CB    . PRO A 1 201 ? 15.837  -28.086 -6.781  1.00 93.62  ? 201 PRO A CB    1 
ATOM   1569 C  CG    . PRO A 1 201 ? 16.643  -27.406 -7.847  1.00 96.50  ? 201 PRO A CG    1 
ATOM   1570 C  CD    . PRO A 1 201 ? 15.621  -26.698 -8.703  1.00 94.26  ? 201 PRO A CD    1 
ATOM   1571 N  N     . LEU A 1 202 ? 14.633  -26.379 -4.134  1.00 90.17  ? 202 LEU A N     1 
ATOM   1572 C  CA    . LEU A 1 202 ? 14.960  -25.537 -2.989  1.00 104.72 ? 202 LEU A CA    1 
ATOM   1573 C  C     . LEU A 1 202 ? 16.432  -25.701 -2.636  1.00 112.98 ? 202 LEU A C     1 
ATOM   1574 O  O     . LEU A 1 202 ? 16.860  -26.777 -2.206  1.00 111.27 ? 202 LEU A O     1 
ATOM   1575 C  CB    . LEU A 1 202 ? 14.075  -25.891 -1.798  1.00 99.02  ? 202 LEU A CB    1 
ATOM   1576 C  CG    . LEU A 1 202 ? 12.618  -25.432 -1.851  1.00 92.94  ? 202 LEU A CG    1 
ATOM   1577 C  CD1   . LEU A 1 202 ? 11.885  -25.843 -0.585  1.00 91.13  ? 202 LEU A CD1   1 
ATOM   1578 C  CD2   . LEU A 1 202 ? 12.539  -23.928 -2.051  1.00 90.49  ? 202 LEU A CD2   1 
ATOM   1579 N  N     . LYS A 1 203 ? 17.209  -24.637 -2.817  1.00 121.56 ? 203 LYS A N     1 
ATOM   1580 C  CA    . LYS A 1 203 ? 18.600  -24.616 -2.390  1.00 128.71 ? 203 LYS A CA    1 
ATOM   1581 C  C     . LYS A 1 203 ? 18.759  -24.199 -0.935  1.00 142.57 ? 203 LYS A C     1 
ATOM   1582 O  O     . LYS A 1 203 ? 19.841  -24.382 -0.367  1.00 141.75 ? 203 LYS A O     1 
ATOM   1583 C  CB    . LYS A 1 203 ? 19.409  -23.681 -3.294  1.00 132.10 ? 203 LYS A CB    1 
ATOM   1584 C  CG    . LYS A 1 203 ? 19.313  -24.040 -4.769  1.00 128.48 ? 203 LYS A CG    1 
ATOM   1585 C  CD    . LYS A 1 203 ? 20.018  -23.026 -5.650  1.00 129.50 ? 203 LYS A CD    1 
ATOM   1586 C  CE    . LYS A 1 203 ? 19.875  -23.394 -7.118  1.00 131.20 ? 203 LYS A CE    1 
ATOM   1587 N  NZ    . LYS A 1 203 ? 18.445  -23.544 -7.513  1.00 115.48 ? 203 LYS A NZ    1 
ATOM   1588 N  N     . LYS A 1 204 ? 17.710  -23.651 -0.323  1.00 156.88 ? 204 LYS A N     1 
ATOM   1589 C  CA    . LYS A 1 204 ? 17.704  -23.284 1.087   1.00 158.20 ? 204 LYS A CA    1 
ATOM   1590 C  C     . LYS A 1 204 ? 16.546  -23.996 1.773   1.00 157.56 ? 204 LYS A C     1 
ATOM   1591 O  O     . LYS A 1 204 ? 15.390  -23.839 1.342   1.00 150.94 ? 204 LYS A O     1 
ATOM   1592 C  CB    . LYS A 1 204 ? 17.571  -21.768 1.261   1.00 160.07 ? 204 LYS A CB    1 
ATOM   1593 C  CG    . LYS A 1 204 ? 18.623  -20.946 0.534   1.00 161.69 ? 204 LYS A CG    1 
ATOM   1594 C  CD    . LYS A 1 204 ? 18.356  -19.458 0.706   1.00 167.84 ? 204 LYS A CD    1 
ATOM   1595 C  CE    . LYS A 1 204 ? 19.369  -18.616 -0.051  1.00 157.59 ? 204 LYS A CE    1 
ATOM   1596 N  NZ    . LYS A 1 204 ? 19.090  -17.161 0.091   1.00 151.24 ? 204 LYS A NZ    1 
ATOM   1597 N  N     . PRO A 1 205 ? 16.789  -24.784 2.821   1.00 147.24 ? 205 PRO A N     1 
ATOM   1598 C  CA    . PRO A 1 205 ? 15.677  -25.444 3.516   1.00 135.42 ? 205 PRO A CA    1 
ATOM   1599 C  C     . PRO A 1 205 ? 14.644  -24.435 3.997   1.00 123.15 ? 205 PRO A C     1 
ATOM   1600 O  O     . PRO A 1 205 ? 14.946  -23.262 4.229   1.00 123.03 ? 205 PRO A O     1 
ATOM   1601 C  CB    . PRO A 1 205 ? 16.362  -26.150 4.691   1.00 135.54 ? 205 PRO A CB    1 
ATOM   1602 C  CG    . PRO A 1 205 ? 17.765  -26.368 4.225   1.00 140.59 ? 205 PRO A CG    1 
ATOM   1603 C  CD    . PRO A 1 205 ? 18.097  -25.173 3.373   1.00 146.66 ? 205 PRO A CD    1 
ATOM   1604 N  N     . LEU A 1 206 ? 13.410  -24.909 4.146   1.00 110.26 ? 206 LEU A N     1 
ATOM   1605 C  CA    . LEU A 1 206 ? 12.284  -24.066 4.526   1.00 101.26 ? 206 LEU A CA    1 
ATOM   1606 C  C     . LEU A 1 206 ? 11.930  -24.292 5.990   1.00 96.83  ? 206 LEU A C     1 
ATOM   1607 O  O     . LEU A 1 206 ? 11.686  -25.428 6.409   1.00 98.42  ? 206 LEU A O     1 
ATOM   1608 C  CB    . LEU A 1 206 ? 11.069  -24.351 3.642   1.00 93.43  ? 206 LEU A CB    1 
ATOM   1609 C  CG    . LEU A 1 206 ? 11.205  -24.004 2.158   1.00 92.12  ? 206 LEU A CG    1 
ATOM   1610 C  CD1   . LEU A 1 206 ? 9.916   -24.321 1.416   1.00 88.79  ? 206 LEU A CD1   1 
ATOM   1611 C  CD2   . LEU A 1 206 ? 11.582  -22.542 1.981   1.00 87.40  ? 206 LEU A CD2   1 
ATOM   1612 N  N     . VAL A 1 207 ? 11.900  -23.209 6.760   1.00 90.32  ? 207 VAL A N     1 
ATOM   1613 C  CA    . VAL A 1 207 ? 11.516  -23.260 8.166   1.00 90.61  ? 207 VAL A CA    1 
ATOM   1614 C  C     . VAL A 1 207 ? 10.009  -23.074 8.267   1.00 92.30  ? 207 VAL A C     1 
ATOM   1615 O  O     . VAL A 1 207 ? 9.445   -22.153 7.663   1.00 87.58  ? 207 VAL A O     1 
ATOM   1616 C  CB    . VAL A 1 207 ? 12.262  -22.190 8.979   1.00 87.01  ? 207 VAL A CB    1 
ATOM   1617 C  CG1   . VAL A 1 207 ? 11.677  -22.086 10.379  1.00 86.03  ? 207 VAL A CG1   1 
ATOM   1618 C  CG2   . VAL A 1 207 ? 13.747  -22.514 9.039   1.00 93.34  ? 207 VAL A CG2   1 
ATOM   1619 N  N     . ASN A 1 208 ? 9.355   -23.949 9.033   1.00 91.56  ? 208 ASN A N     1 
ATOM   1620 C  CA    . ASN A 1 208 ? 7.898   -23.949 9.158   1.00 88.29  ? 208 ASN A CA    1 
ATOM   1621 C  C     . ASN A 1 208 ? 7.217   -24.042 7.796   1.00 88.66  ? 208 ASN A C     1 
ATOM   1622 O  O     . ASN A 1 208 ? 6.117   -23.517 7.603   1.00 87.23  ? 208 ASN A O     1 
ATOM   1623 C  CB    . ASN A 1 208 ? 7.402   -22.715 9.920   1.00 88.47  ? 208 ASN A CB    1 
ATOM   1624 C  CG    . ASN A 1 208 ? 7.582   -22.843 11.422  1.00 93.97  ? 208 ASN A CG    1 
ATOM   1625 O  OD1   . ASN A 1 208 ? 7.798   -23.938 11.941  1.00 96.08  ? 208 ASN A OD1   1 
ATOM   1626 N  ND2   . ASN A 1 208 ? 7.481   -21.722 12.129  1.00 87.88  ? 208 ASN A ND2   1 
ATOM   1627 N  N     . ASN A 1 209 ? 7.866   -24.714 6.843   1.00 91.60  ? 209 ASN A N     1 
ATOM   1628 C  CA    . ASN A 1 209 ? 7.354   -24.823 5.476   1.00 89.85  ? 209 ASN A CA    1 
ATOM   1629 C  C     . ASN A 1 209 ? 7.023   -23.452 4.894   1.00 79.45  ? 209 ASN A C     1 
ATOM   1630 O  O     . ASN A 1 209 ? 6.136   -23.316 4.048   1.00 79.22  ? 209 ASN A O     1 
ATOM   1631 C  CB    . ASN A 1 209 ? 6.132   -25.743 5.415   1.00 80.06  ? 209 ASN A CB    1 
ATOM   1632 C  CG    . ASN A 1 209 ? 6.498   -27.202 5.577   1.00 88.00  ? 209 ASN A CG    1 
ATOM   1633 O  OD1   . ASN A 1 209 ? 7.548   -27.642 5.111   1.00 97.32  ? 209 ASN A OD1   1 
ATOM   1634 N  ND2   . ASN A 1 209 ? 5.635   -27.961 6.244   1.00 92.34  ? 209 ASN A ND2   1 
ATOM   1635 N  N     . TRP A 1 210 ? 7.738   -22.426 5.345   1.00 75.48  ? 210 TRP A N     1 
ATOM   1636 C  CA    . TRP A 1 210 ? 7.476   -21.048 4.948   1.00 75.03  ? 210 TRP A CA    1 
ATOM   1637 C  C     . TRP A 1 210 ? 8.537   -20.623 3.941   1.00 71.51  ? 210 TRP A C     1 
ATOM   1638 O  O     . TRP A 1 210 ? 9.697   -20.405 4.304   1.00 76.68  ? 210 TRP A O     1 
ATOM   1639 C  CB    . TRP A 1 210 ? 7.469   -20.130 6.168   1.00 69.98  ? 210 TRP A CB    1 
ATOM   1640 C  CG    . TRP A 1 210 ? 6.945   -18.762 5.891   1.00 68.66  ? 210 TRP A CG    1 
ATOM   1641 C  CD1   . TRP A 1 210 ? 7.664   -17.605 5.833   1.00 68.21  ? 210 TRP A CD1   1 
ATOM   1642 C  CD2   . TRP A 1 210 ? 5.583   -18.403 5.628   1.00 65.19  ? 210 TRP A CD2   1 
ATOM   1643 N  NE1   . TRP A 1 210 ? 6.835   -16.547 5.555   1.00 61.00  ? 210 TRP A NE1   1 
ATOM   1644 C  CE2   . TRP A 1 210 ? 5.552   -17.010 5.423   1.00 63.78  ? 210 TRP A CE2   1 
ATOM   1645 C  CE3   . TRP A 1 210 ? 4.388   -19.123 5.547   1.00 61.05  ? 210 TRP A CE3   1 
ATOM   1646 C  CZ2   . TRP A 1 210 ? 4.372   -16.322 5.142   1.00 62.69  ? 210 TRP A CZ2   1 
ATOM   1647 C  CZ3   . TRP A 1 210 ? 3.218   -18.440 5.268   1.00 58.53  ? 210 TRP A CZ3   1 
ATOM   1648 C  CH2   . TRP A 1 210 ? 3.218   -17.054 5.070   1.00 57.21  ? 210 TRP A CH2   1 
ATOM   1649 N  N     . ALA A 1 211 ? 8.142   -20.516 2.677   1.00 67.95  ? 211 ALA A N     1 
ATOM   1650 C  CA    . ALA A 1 211 ? 9.053   -20.073 1.633   1.00 73.34  ? 211 ALA A CA    1 
ATOM   1651 C  C     . ALA A 1 211 ? 9.269   -18.568 1.736   1.00 71.31  ? 211 ALA A C     1 
ATOM   1652 O  O     . ALA A 1 211 ? 8.307   -17.792 1.754   1.00 71.39  ? 211 ALA A O     1 
ATOM   1653 C  CB    . ALA A 1 211 ? 8.508   -20.438 0.253   1.00 67.22  ? 211 ALA A CB    1 
ATOM   1654 N  N     . CYS A 1 212 ? 10.532  -18.159 1.805   1.00 74.85  ? 212 CYS A N     1 
ATOM   1655 C  CA    . CYS A 1 212 ? 10.872  -16.750 1.932   1.00 72.85  ? 212 CYS A CA    1 
ATOM   1656 C  C     . CYS A 1 212 ? 12.363  -16.595 1.679   1.00 70.93  ? 212 CYS A C     1 
ATOM   1657 O  O     . CYS A 1 212 ? 13.124  -17.563 1.746   1.00 70.70  ? 212 CYS A O     1 
ATOM   1658 C  CB    . CYS A 1 212 ? 10.500  -16.202 3.313   1.00 69.02  ? 212 CYS A CB    1 
ATOM   1659 S  SG    . CYS A 1 212 ? 11.521  -16.852 4.654   1.00 78.44  ? 212 CYS A SG    1 
ATOM   1660 N  N     . ASN A 1 213 ? 12.770  -15.359 1.393   1.00 69.23  ? 213 ASN A N     1 
ATOM   1661 C  CA    . ASN A 1 213 ? 14.172  -15.038 1.132   1.00 72.86  ? 213 ASN A CA    1 
ATOM   1662 C  C     . ASN A 1 213 ? 14.496  -13.727 1.831   1.00 76.79  ? 213 ASN A C     1 
ATOM   1663 O  O     . ASN A 1 213 ? 14.416  -12.649 1.230   1.00 79.16  ? 213 ASN A O     1 
ATOM   1664 C  CB    . ASN A 1 213 ? 14.454  -14.951 -0.368  1.00 75.99  ? 213 ASN A CB    1 
ATOM   1665 C  CG    . ASN A 1 213 ? 15.927  -15.097 -0.693  1.00 81.89  ? 213 ASN A CG    1 
ATOM   1666 O  OD1   . ASN A 1 213 ? 16.790  -14.695 0.086   1.00 84.77  ? 213 ASN A OD1   1 
ATOM   1667 N  ND2   . ASN A 1 213 ? 16.221  -15.679 -1.850  1.00 82.58  ? 213 ASN A ND2   1 
ATOM   1668 N  N     . PRO A 1 214 ? 14.862  -13.782 3.114   1.00 82.53  ? 214 PRO A N     1 
ATOM   1669 C  CA    . PRO A 1 214 ? 15.102  -12.531 3.854   1.00 81.48  ? 214 PRO A CA    1 
ATOM   1670 C  C     . PRO A 1 214 ? 16.234  -11.691 3.285   1.00 83.76  ? 214 PRO A C     1 
ATOM   1671 O  O     . PRO A 1 214 ? 16.100  -10.464 3.195   1.00 78.80  ? 214 PRO A O     1 
ATOM   1672 C  CB    . PRO A 1 214 ? 15.419  -13.025 5.273   1.00 81.08  ? 214 PRO A CB    1 
ATOM   1673 C  CG    . PRO A 1 214 ? 14.801  -14.383 5.353   1.00 82.16  ? 214 PRO A CG    1 
ATOM   1674 C  CD    . PRO A 1 214 ? 14.943  -14.967 3.983   1.00 83.26  ? 214 PRO A CD    1 
ATOM   1675 N  N     . GLU A 1 215 ? 17.349  -12.316 2.899   1.00 96.52  ? 215 GLU A N     1 
ATOM   1676 C  CA    . GLU A 1 215 ? 18.502  -11.550 2.433   1.00 98.20  ? 215 GLU A CA    1 
ATOM   1677 C  C     . GLU A 1 215 ? 18.144  -10.673 1.239   1.00 95.53  ? 215 GLU A C     1 
ATOM   1678 O  O     . GLU A 1 215 ? 18.592  -9.524  1.146   1.00 96.33  ? 215 GLU A O     1 
ATOM   1679 C  CB    . GLU A 1 215 ? 19.654  -12.491 2.076   1.00 101.21 ? 215 GLU A CB    1 
ATOM   1680 C  CG    . GLU A 1 215 ? 20.102  -13.411 3.204   1.00 111.39 ? 215 GLU A CG    1 
ATOM   1681 C  CD    . GLU A 1 215 ? 19.210  -14.630 3.361   1.00 113.77 ? 215 GLU A CD    1 
ATOM   1682 O  OE1   . GLU A 1 215 ? 18.233  -14.758 2.593   1.00 107.93 ? 215 GLU A OE1   1 
ATOM   1683 O  OE2   . GLU A 1 215 ? 19.489  -15.462 4.250   1.00 122.67 ? 215 GLU A OE2   1 
ATOM   1684 N  N     . LEU A 1 216 ? 17.334  -11.194 0.317   1.00 82.20  ? 216 LEU A N     1 
ATOM   1685 C  CA    . LEU A 1 216 ? 16.989  -10.503 -0.917  1.00 67.41  ? 216 LEU A CA    1 
ATOM   1686 C  C     . LEU A 1 216 ? 15.632  -9.811  -0.849  1.00 68.28  ? 216 LEU A C     1 
ATOM   1687 O  O     . LEU A 1 216 ? 15.078  -9.450  -1.893  1.00 62.62  ? 216 LEU A O     1 
ATOM   1688 C  CB    . LEU A 1 216 ? 17.010  -11.483 -2.091  1.00 66.21  ? 216 LEU A CB    1 
ATOM   1689 C  CG    . LEU A 1 216 ? 18.274  -12.317 -2.290  1.00 70.84  ? 216 LEU A CG    1 
ATOM   1690 C  CD1   . LEU A 1 216 ? 18.045  -13.351 -3.375  1.00 68.73  ? 216 LEU A CD1   1 
ATOM   1691 C  CD2   . LEU A 1 216 ? 19.456  -11.429 -2.639  1.00 72.81  ? 216 LEU A CD2   1 
ATOM   1692 N  N     . THR A 1 217 ? 15.083  -9.622  0.348   1.00 67.71  ? 217 THR A N     1 
ATOM   1693 C  CA    . THR A 1 217 ? 13.772  -8.997  0.462   1.00 61.47  ? 217 THR A CA    1 
ATOM   1694 C  C     . THR A 1 217 ? 13.816  -7.566  -0.060  1.00 67.42  ? 217 THR A C     1 
ATOM   1695 O  O     . THR A 1 217 ? 14.771  -6.823  0.184   1.00 67.18  ? 217 THR A O     1 
ATOM   1696 C  CB    . THR A 1 217 ? 13.293  -9.016  1.913   1.00 63.11  ? 217 THR A CB    1 
ATOM   1697 O  OG1   . THR A 1 217 ? 13.108  -10.372 2.337   1.00 71.81  ? 217 THR A OG1   1 
ATOM   1698 C  CG2   . THR A 1 217 ? 11.974  -8.265  2.045   1.00 59.57  ? 217 THR A CG2   1 
ATOM   1699 N  N     . LEU A 1 218 ? 12.771  -7.183  -0.790  1.00 56.86  ? 218 LEU A N     1 
ATOM   1700 C  CA    . LEU A 1 218 ? 12.704  -5.856  -1.383  1.00 54.78  ? 218 LEU A CA    1 
ATOM   1701 C  C     . LEU A 1 218 ? 11.265  -5.571  -1.780  1.00 61.27  ? 218 LEU A C     1 
ATOM   1702 O  O     . LEU A 1 218 ? 10.651  -6.363  -2.501  1.00 57.76  ? 218 LEU A O     1 
ATOM   1703 C  CB    . LEU A 1 218 ? 13.630  -5.751  -2.599  1.00 59.77  ? 218 LEU A CB    1 
ATOM   1704 C  CG    . LEU A 1 218 ? 13.767  -4.360  -3.220  1.00 56.66  ? 218 LEU A CG    1 
ATOM   1705 C  CD1   . LEU A 1 218 ? 14.341  -3.380  -2.210  1.00 59.64  ? 218 LEU A CD1   1 
ATOM   1706 C  CD2   . LEU A 1 218 ? 14.630  -4.410  -4.467  1.00 59.09  ? 218 LEU A CD2   1 
ATOM   1707 N  N     . ILE A 1 219 ? 10.732  -4.450  -1.302  1.00 58.67  ? 219 ILE A N     1 
ATOM   1708 C  CA    . ILE A 1 219 ? 9.376   -4.011  -1.615  1.00 59.53  ? 219 ILE A CA    1 
ATOM   1709 C  C     . ILE A 1 219 ? 9.513   -2.664  -2.312  1.00 55.35  ? 219 ILE A C     1 
ATOM   1710 O  O     . ILE A 1 219 ? 9.782   -1.646  -1.662  1.00 63.45  ? 219 ILE A O     1 
ATOM   1711 C  CB    . ILE A 1 219 ? 8.490   -3.908  -0.367  1.00 58.79  ? 219 ILE A CB    1 
ATOM   1712 C  CG1   . ILE A 1 219 ? 8.397   -5.258  0.353   1.00 58.11  ? 219 ILE A CG1   1 
ATOM   1713 C  CG2   . ILE A 1 219 ? 7.103   -3.399  -0.737  1.00 55.05  ? 219 ILE A CG2   1 
ATOM   1714 C  CD1   . ILE A 1 219 ? 9.577   -5.560  1.256   1.00 58.82  ? 219 ILE A CD1   1 
ATOM   1715 N  N     . ALA A 1 220 ? 9.331   -2.647  -3.629  1.00 52.92  ? 220 ALA A N     1 
ATOM   1716 C  CA    . ALA A 1 220 ? 9.548   -1.454  -4.432  1.00 57.53  ? 220 ALA A CA    1 
ATOM   1717 C  C     . ALA A 1 220 ? 8.233   -0.936  -4.999  1.00 54.32  ? 220 ALA A C     1 
ATOM   1718 O  O     . ALA A 1 220 ? 7.303   -1.703  -5.265  1.00 54.59  ? 220 ALA A O     1 
ATOM   1719 C  CB    . ALA A 1 220 ? 10.527  -1.728  -5.578  1.00 57.56  ? 220 ALA A CB    1 
ATOM   1720 N  N     . HIS A 1 221 ? 8.174   0.380   -5.186  1.00 52.91  ? 221 HIS A N     1 
ATOM   1721 C  CA    . HIS A 1 221 ? 7.006   1.050   -5.738  1.00 55.78  ? 221 HIS A CA    1 
ATOM   1722 C  C     . HIS A 1 221 ? 7.445   1.940   -6.890  1.00 60.29  ? 221 HIS A C     1 
ATOM   1723 O  O     . HIS A 1 221 ? 8.435   2.669   -6.773  1.00 61.92  ? 221 HIS A O     1 
ATOM   1724 C  CB    . HIS A 1 221 ? 6.286   1.879   -4.669  1.00 51.52  ? 221 HIS A CB    1 
ATOM   1725 C  CG    . HIS A 1 221 ? 5.890   1.089   -3.462  1.00 53.32  ? 221 HIS A CG    1 
ATOM   1726 N  ND1   . HIS A 1 221 ? 6.780   0.767   -2.459  1.00 56.77  ? 221 HIS A ND1   1 
ATOM   1727 C  CD2   . HIS A 1 221 ? 4.704   0.545   -3.101  1.00 51.55  ? 221 HIS A CD2   1 
ATOM   1728 C  CE1   . HIS A 1 221 ? 6.157   0.065   -1.530  1.00 55.38  ? 221 HIS A CE1   1 
ATOM   1729 N  NE2   . HIS A 1 221 ? 4.896   -0.084  -1.895  1.00 57.15  ? 221 HIS A NE2   1 
ATOM   1730 N  N     . LEU A 1 222 ? 6.714   1.871   -8.001  1.00 60.93  ? 222 LEU A N     1 
ATOM   1731 C  CA    . LEU A 1 222 ? 6.978   2.693   -9.180  1.00 59.89  ? 222 LEU A CA    1 
ATOM   1732 C  C     . LEU A 1 222 ? 5.688   3.409   -9.553  1.00 60.64  ? 222 LEU A C     1 
ATOM   1733 O  O     . LEU A 1 222 ? 4.907   2.922   -10.382 1.00 63.81  ? 222 LEU A O     1 
ATOM   1734 C  CB    . LEU A 1 222 ? 7.511   1.852   -10.339 1.00 63.42  ? 222 LEU A CB    1 
ATOM   1735 C  CG    . LEU A 1 222 ? 8.909   1.252   -10.154 1.00 66.37  ? 222 LEU A CG    1 
ATOM   1736 C  CD1   . LEU A 1 222 ? 8.901   0.146   -9.104  1.00 66.89  ? 222 LEU A CD1   1 
ATOM   1737 C  CD2   . LEU A 1 222 ? 9.463   0.741   -11.476 1.00 65.73  ? 222 LEU A CD2   1 
ATOM   1738 N  N     . PRO A 1 223 ? 5.429   4.575   -8.957  1.00 58.63  ? 223 PRO A N     1 
ATOM   1739 C  CA    . PRO A 1 223 ? 4.164   5.267   -9.254  1.00 63.19  ? 223 PRO A CA    1 
ATOM   1740 C  C     . PRO A 1 223 ? 4.061   5.736   -10.692 1.00 66.82  ? 223 PRO A C     1 
ATOM   1741 O  O     . PRO A 1 223 ? 2.971   5.683   -11.274 1.00 69.81  ? 223 PRO A O     1 
ATOM   1742 C  CB    . PRO A 1 223 ? 4.165   6.438   -8.261  1.00 57.45  ? 223 PRO A CB    1 
ATOM   1743 C  CG    . PRO A 1 223 ? 5.603   6.640   -7.904  1.00 62.10  ? 223 PRO A CG    1 
ATOM   1744 C  CD    . PRO A 1 223 ? 6.232   5.282   -7.945  1.00 64.16  ? 223 PRO A CD    1 
ATOM   1745 N  N     . ASP A 1 224 ? 5.164   6.196   -11.288 1.00 68.02  ? 224 ASP A N     1 
ATOM   1746 C  CA    . ASP A 1 224 ? 5.117   6.616   -12.685 1.00 79.18  ? 224 ASP A CA    1 
ATOM   1747 C  C     . ASP A 1 224 ? 4.681   5.478   -13.599 1.00 80.22  ? 224 ASP A C     1 
ATOM   1748 O  O     . ASP A 1 224 ? 4.057   5.723   -14.638 1.00 85.73  ? 224 ASP A O     1 
ATOM   1749 C  CB    . ASP A 1 224 ? 6.478   7.155   -13.124 1.00 90.56  ? 224 ASP A CB    1 
ATOM   1750 C  CG    . ASP A 1 224 ? 6.865   8.428   -12.397 1.00 93.53  ? 224 ASP A CG    1 
ATOM   1751 O  OD1   . ASP A 1 224 ? 5.969   9.097   -11.837 1.00 81.88  ? 224 ASP A OD1   1 
ATOM   1752 O  OD2   . ASP A 1 224 ? 8.068   8.764   -12.393 1.00 103.14 ? 224 ASP A OD2   1 
ATOM   1753 N  N     . ARG A 1 225 ? 4.994   4.234   -13.234 1.00 82.87  ? 225 ARG A N     1 
ATOM   1754 C  CA    . ARG A 1 225 ? 4.612   3.070   -14.021 1.00 81.83  ? 225 ARG A CA    1 
ATOM   1755 C  C     . ARG A 1 225 ? 3.383   2.349   -13.485 1.00 78.57  ? 225 ARG A C     1 
ATOM   1756 O  O     . ARG A 1 225 ? 2.904   1.414   -14.136 1.00 78.33  ? 225 ARG A O     1 
ATOM   1757 C  CB    . ARG A 1 225 ? 5.768   2.068   -14.097 1.00 82.28  ? 225 ARG A CB    1 
ATOM   1758 C  CG    . ARG A 1 225 ? 6.976   2.540   -14.874 1.00 91.13  ? 225 ARG A CG    1 
ATOM   1759 C  CD    . ARG A 1 225 ? 7.936   1.384   -15.067 1.00 98.94  ? 225 ARG A CD    1 
ATOM   1760 N  NE    . ARG A 1 225 ? 9.300   1.825   -15.327 1.00 109.78 ? 225 ARG A NE    1 
ATOM   1761 C  CZ    . ARG A 1 225 ? 10.341  1.009   -15.408 1.00 119.57 ? 225 ARG A CZ    1 
ATOM   1762 N  NH1   . ARG A 1 225 ? 10.207  -0.300  -15.261 1.00 110.08 ? 225 ARG A NH1   1 
ATOM   1763 N  NH2   . ARG A 1 225 ? 11.548  1.519   -15.638 1.00 123.20 ? 225 ARG A NH2   1 
ATOM   1764 N  N     . ARG A 1 226 ? 2.871   2.739   -12.318 1.00 72.03  ? 226 ARG A N     1 
ATOM   1765 C  CA    . ARG A 1 226 ? 1.721   2.062   -11.723 1.00 69.95  ? 226 ARG A CA    1 
ATOM   1766 C  C     . ARG A 1 226 ? 2.045   0.600   -11.420 1.00 66.45  ? 226 ARG A C     1 
ATOM   1767 O  O     . ARG A 1 226 ? 1.213   -0.290  -11.608 1.00 61.43  ? 226 ARG A O     1 
ATOM   1768 C  CB    . ARG A 1 226 ? 0.495   2.162   -12.632 1.00 74.23  ? 226 ARG A CB    1 
ATOM   1769 C  CG    . ARG A 1 226 ? 0.107   3.576   -13.017 1.00 78.63  ? 226 ARG A CG    1 
ATOM   1770 C  CD    . ARG A 1 226 ? -0.434  4.334   -11.824 1.00 78.92  ? 226 ARG A CD    1 
ATOM   1771 N  NE    . ARG A 1 226 ? -1.011  5.615   -12.214 1.00 91.24  ? 226 ARG A NE    1 
ATOM   1772 C  CZ    . ARG A 1 226 ? -0.333  6.752   -12.275 1.00 82.26  ? 226 ARG A CZ    1 
ATOM   1773 N  NH1   . ARG A 1 226 ? 0.956   6.804   -11.982 1.00 80.53  ? 226 ARG A NH1   1 
ATOM   1774 N  NH2   . ARG A 1 226 ? -0.966  7.866   -12.635 1.00 81.26  ? 226 ARG A NH2   1 
ATOM   1775 N  N     . GLU A 1 227 ? 3.265   0.346   -10.956 1.00 60.62  ? 227 GLU A N     1 
ATOM   1776 C  CA    . GLU A 1 227 ? 3.737   -1.006  -10.700 1.00 59.39  ? 227 GLU A CA    1 
ATOM   1777 C  C     . GLU A 1 227 ? 4.192   -1.140  -9.256  1.00 58.86  ? 227 GLU A C     1 
ATOM   1778 O  O     . GLU A 1 227 ? 4.770   -0.209  -8.686  1.00 58.93  ? 227 GLU A O     1 
ATOM   1779 C  CB    . GLU A 1 227 ? 4.892   -1.380  -11.632 1.00 64.66  ? 227 GLU A CB    1 
ATOM   1780 C  CG    . GLU A 1 227 ? 4.545   -1.342  -13.107 1.00 74.95  ? 227 GLU A CG    1 
ATOM   1781 C  CD    . GLU A 1 227 ? 5.704   -1.773  -13.980 1.00 71.76  ? 227 GLU A CD    1 
ATOM   1782 O  OE1   . GLU A 1 227 ? 6.717   -2.253  -13.428 1.00 66.46  ? 227 GLU A OE1   1 
ATOM   1783 O  OE2   . GLU A 1 227 ? 5.602   -1.631  -15.216 1.00 80.37  ? 227 GLU A OE2   1 
ATOM   1784 N  N     . ILE A 1 228 ? 3.930   -2.308  -8.675  1.00 51.48  ? 228 ILE A N     1 
ATOM   1785 C  CA    . ILE A 1 228 ? 4.405   -2.666  -7.346  1.00 50.90  ? 228 ILE A CA    1 
ATOM   1786 C  C     . ILE A 1 228 ? 5.153   -3.985  -7.465  1.00 54.32  ? 228 ILE A C     1 
ATOM   1787 O  O     . ILE A 1 228 ? 4.606   -4.968  -7.978  1.00 50.89  ? 228 ILE A O     1 
ATOM   1788 C  CB    . ILE A 1 228 ? 3.252   -2.786  -6.332  1.00 54.11  ? 228 ILE A CB    1 
ATOM   1789 C  CG1   . ILE A 1 228 ? 2.432   -1.495  -6.303  1.00 51.78  ? 228 ILE A CG1   1 
ATOM   1790 C  CG2   . ILE A 1 228 ? 3.793   -3.119  -4.951  1.00 52.05  ? 228 ILE A CG2   1 
ATOM   1791 C  CD1   . ILE A 1 228 ? 1.293   -1.514  -5.304  1.00 50.41  ? 228 ILE A CD1   1 
ATOM   1792 N  N     . ILE A 1 229 ? 6.397   -4.006  -6.995  1.00 51.13  ? 229 ILE A N     1 
ATOM   1793 C  CA    . ILE A 1 229 ? 7.286   -5.149  -7.161  1.00 50.59  ? 229 ILE A CA    1 
ATOM   1794 C  C     . ILE A 1 229 ? 7.821   -5.519  -5.786  1.00 51.80  ? 229 ILE A C     1 
ATOM   1795 O  O     . ILE A 1 229 ? 8.585   -4.751  -5.186  1.00 57.94  ? 229 ILE A O     1 
ATOM   1796 C  CB    . ILE A 1 229 ? 8.433   -4.845  -8.135  1.00 55.44  ? 229 ILE A CB    1 
ATOM   1797 C  CG1   . ILE A 1 229 ? 7.872   -4.351  -9.471  1.00 51.58  ? 229 ILE A CG1   1 
ATOM   1798 C  CG2   . ILE A 1 229 ? 9.303   -6.073  -8.341  1.00 51.07  ? 229 ILE A CG2   1 
ATOM   1799 C  CD1   . ILE A 1 229 ? 8.932   -3.908  -10.460 1.00 58.12  ? 229 ILE A CD1   1 
ATOM   1800 N  N     . SER A 1 230 ? 7.424   -6.689  -5.285  1.00 50.14  ? 230 SER A N     1 
ATOM   1801 C  CA    . SER A 1 230 ? 7.816   -7.171  -3.968  1.00 53.81  ? 230 SER A CA    1 
ATOM   1802 C  C     . SER A 1 230 ? 8.423   -8.560  -4.095  1.00 50.55  ? 230 SER A C     1 
ATOM   1803 O  O     . SER A 1 230 ? 7.924   -9.396  -4.853  1.00 50.38  ? 230 SER A O     1 
ATOM   1804 C  CB    . SER A 1 230 ? 6.619   -7.208  -3.010  1.00 56.01  ? 230 SER A CB    1 
ATOM   1805 O  OG    . SER A 1 230 ? 6.955   -7.870  -1.804  1.00 58.64  ? 230 SER A OG    1 
ATOM   1806 N  N     . PHE A 1 231 ? 9.492   -8.807  -3.338  1.00 53.80  ? 231 PHE A N     1 
ATOM   1807 C  CA    . PHE A 1 231 ? 10.276  -10.024 -3.498  1.00 52.27  ? 231 PHE A CA    1 
ATOM   1808 C  C     . PHE A 1 231 ? 10.870  -10.450 -2.164  1.00 56.26  ? 231 PHE A C     1 
ATOM   1809 O  O     . PHE A 1 231 ? 11.465  -9.631  -1.459  1.00 58.98  ? 231 PHE A O     1 
ATOM   1810 C  CB    . PHE A 1 231 ? 11.395  -9.811  -4.524  1.00 50.80  ? 231 PHE A CB    1 
ATOM   1811 C  CG    . PHE A 1 231 ? 12.299  -11.000 -4.700  1.00 57.43  ? 231 PHE A CG    1 
ATOM   1812 C  CD1   . PHE A 1 231 ? 13.420  -11.160 -3.902  1.00 59.66  ? 231 PHE A CD1   1 
ATOM   1813 C  CD2   . PHE A 1 231 ? 12.034  -11.951 -5.671  1.00 55.09  ? 231 PHE A CD2   1 
ATOM   1814 C  CE1   . PHE A 1 231 ? 14.254  -12.249 -4.066  1.00 60.68  ? 231 PHE A CE1   1 
ATOM   1815 C  CE2   . PHE A 1 231 ? 12.866  -13.041 -5.840  1.00 55.12  ? 231 PHE A CE2   1 
ATOM   1816 C  CZ    . PHE A 1 231 ? 13.977  -13.189 -5.037  1.00 56.38  ? 231 PHE A CZ    1 
ATOM   1817 N  N     . GLY A 1 232 ? 10.723  -11.734 -1.834  1.00 55.07  ? 232 GLY A N     1 
ATOM   1818 C  CA    . GLY A 1 232 ? 11.405  -12.329 -0.704  1.00 62.85  ? 232 GLY A CA    1 
ATOM   1819 C  C     . GLY A 1 232 ? 10.588  -12.449 0.566   1.00 68.70  ? 232 GLY A C     1 
ATOM   1820 O  O     . GLY A 1 232 ? 11.062  -13.065 1.529   1.00 70.08  ? 232 GLY A O     1 
ATOM   1821 N  N     . SER A 1 233 ? 9.384   -11.887 0.602   1.00 63.01  ? 233 SER A N     1 
ATOM   1822 C  CA    . SER A 1 233 ? 8.550   -11.924 1.792   1.00 60.77  ? 233 SER A CA    1 
ATOM   1823 C  C     . SER A 1 233 ? 7.147   -12.378 1.422   1.00 64.35  ? 233 SER A C     1 
ATOM   1824 O  O     . SER A 1 233 ? 6.654   -12.097 0.327   1.00 64.10  ? 233 SER A O     1 
ATOM   1825 C  CB    . SER A 1 233 ? 8.488   -10.554 2.478   1.00 67.59  ? 233 SER A CB    1 
ATOM   1826 O  OG    . SER A 1 233 ? 7.579   -10.574 3.564   1.00 69.99  ? 233 SER A OG    1 
ATOM   1827 N  N     . GLY A 1 234 ? 6.509   -13.087 2.350   1.00 70.08  ? 234 GLY A N     1 
ATOM   1828 C  CA    . GLY A 1 234 ? 5.145   -13.531 2.151   1.00 58.73  ? 234 GLY A CA    1 
ATOM   1829 C  C     . GLY A 1 234 ? 4.199   -13.020 3.216   1.00 61.67  ? 234 GLY A C     1 
ATOM   1830 O  O     . GLY A 1 234 ? 3.039   -13.440 3.272   1.00 68.15  ? 234 GLY A O     1 
ATOM   1831 N  N     . TYR A 1 235 ? 4.669   -12.100 4.056   1.00 61.85  ? 235 TYR A N     1 
ATOM   1832 C  CA    . TYR A 1 235 ? 3.930   -11.666 5.235   1.00 63.23  ? 235 TYR A CA    1 
ATOM   1833 C  C     . TYR A 1 235 ? 3.168   -10.379 4.942   1.00 67.05  ? 235 TYR A C     1 
ATOM   1834 O  O     . TYR A 1 235 ? 3.764   -9.378  4.523   1.00 66.86  ? 235 TYR A O     1 
ATOM   1835 C  CB    . TYR A 1 235 ? 4.869   -11.469 6.426   1.00 70.64  ? 235 TYR A CB    1 
ATOM   1836 C  CG    . TYR A 1 235 ? 4.153   -11.486 7.757   1.00 74.37  ? 235 TYR A CG    1 
ATOM   1837 C  CD1   . TYR A 1 235 ? 3.878   -12.687 8.401   1.00 67.60  ? 235 TYR A CD1   1 
ATOM   1838 C  CD2   . TYR A 1 235 ? 3.740   -10.305 8.367   1.00 69.66  ? 235 TYR A CD2   1 
ATOM   1839 C  CE1   . TYR A 1 235 ? 3.220   -12.714 9.615   1.00 69.73  ? 235 TYR A CE1   1 
ATOM   1840 C  CE2   . TYR A 1 235 ? 3.078   -10.323 9.587   1.00 69.02  ? 235 TYR A CE2   1 
ATOM   1841 C  CZ    . TYR A 1 235 ? 2.822   -11.532 10.206  1.00 69.88  ? 235 TYR A CZ    1 
ATOM   1842 O  OH    . TYR A 1 235 ? 2.166   -11.570 11.417  1.00 63.28  ? 235 TYR A OH    1 
ATOM   1843 N  N     . GLY A 1 236 ? 1.855   -10.417 5.166   1.00 61.47  ? 236 GLY A N     1 
ATOM   1844 C  CA    . GLY A 1 236 ? 0.969   -9.267  5.114   1.00 61.32  ? 236 GLY A CA    1 
ATOM   1845 C  C     . GLY A 1 236 ? 1.416   -8.071  4.301   1.00 60.69  ? 236 GLY A C     1 
ATOM   1846 O  O     . GLY A 1 236 ? 1.299   -8.069  3.072   1.00 66.31  ? 236 GLY A O     1 
ATOM   1847 N  N     . GLY A 1 237 ? 1.922   -7.042  4.982   1.00 56.49  ? 237 GLY A N     1 
ATOM   1848 C  CA    . GLY A 1 237 ? 2.262   -5.804  4.297   1.00 62.33  ? 237 GLY A CA    1 
ATOM   1849 C  C     . GLY A 1 237 ? 3.127   -6.015  3.071   1.00 67.62  ? 237 GLY A C     1 
ATOM   1850 O  O     . GLY A 1 237 ? 2.985   -5.308  2.070   1.00 65.69  ? 237 GLY A O     1 
ATOM   1851 N  N     . ASN A 1 238 ? 4.027   -6.998  3.124   1.00 64.67  ? 238 ASN A N     1 
ATOM   1852 C  CA    . ASN A 1 238 ? 4.947   -7.227  2.015   1.00 62.12  ? 238 ASN A CA    1 
ATOM   1853 C  C     . ASN A 1 238 ? 4.276   -7.962  0.860   1.00 65.00  ? 238 ASN A C     1 
ATOM   1854 O  O     . ASN A 1 238 ? 4.578   -7.689  -0.307  1.00 65.58  ? 238 ASN A O     1 
ATOM   1855 C  CB    . ASN A 1 238 ? 6.168   -8.011  2.499   1.00 63.24  ? 238 ASN A CB    1 
ATOM   1856 C  CG    . ASN A 1 238 ? 6.822   -7.380  3.713   1.00 67.76  ? 238 ASN A CG    1 
ATOM   1857 O  OD1   . ASN A 1 238 ? 6.773   -6.164  3.897   1.00 69.01  ? 238 ASN A OD1   1 
ATOM   1858 N  ND2   . ASN A 1 238 ? 7.438   -8.207  4.551   1.00 68.45  ? 238 ASN A ND2   1 
ATOM   1859 N  N     . SER A 1 239 ? 3.368   -8.890  1.159   1.00 62.66  ? 239 SER A N     1 
ATOM   1860 C  CA    . SER A 1 239 ? 2.790   -9.769  0.147   1.00 59.05  ? 239 SER A CA    1 
ATOM   1861 C  C     . SER A 1 239 ? 1.405   -9.335  -0.315  1.00 59.70  ? 239 SER A C     1 
ATOM   1862 O  O     . SER A 1 239 ? 1.087   -9.467  -1.502  1.00 54.15  ? 239 SER A O     1 
ATOM   1863 C  CB    . SER A 1 239 ? 2.719   -11.203 0.678   1.00 60.06  ? 239 SER A CB    1 
ATOM   1864 O  OG    . SER A 1 239 ? 1.862   -11.283 1.805   1.00 64.39  ? 239 SER A OG    1 
ATOM   1865 N  N     . LEU A 1 240 ? 0.565   -8.838  0.594   1.00 63.09  ? 240 LEU A N     1 
ATOM   1866 C  CA    . LEU A 1 240 ? -0.759  -8.327  0.236   1.00 55.24  ? 240 LEU A CA    1 
ATOM   1867 C  C     . LEU A 1 240 ? -0.566  -6.940  -0.368  1.00 60.93  ? 240 LEU A C     1 
ATOM   1868 O  O     . LEU A 1 240 ? -0.695  -5.905  0.292   1.00 67.58  ? 240 LEU A O     1 
ATOM   1869 C  CB    . LEU A 1 240 ? -1.676  -8.302  1.452   1.00 59.88  ? 240 LEU A CB    1 
ATOM   1870 C  CG    . LEU A 1 240 ? -1.690  -9.586  2.289   1.00 60.35  ? 240 LEU A CG    1 
ATOM   1871 C  CD1   . LEU A 1 240 ? -2.742  -9.512  3.386   1.00 57.68  ? 240 LEU A CD1   1 
ATOM   1872 C  CD2   . LEU A 1 240 ? -1.900  -10.818 1.414   1.00 53.09  ? 240 LEU A CD2   1 
ATOM   1873 N  N     . LEU A 1 241 ? -0.244  -6.928  -1.662  1.00 65.68  ? 241 LEU A N     1 
ATOM   1874 C  CA    . LEU A 1 241 ? 0.201   -5.693  -2.298  1.00 65.93  ? 241 LEU A CA    1 
ATOM   1875 C  C     . LEU A 1 241 ? -0.905  -4.648  -2.367  1.00 61.36  ? 241 LEU A C     1 
ATOM   1876 O  O     . LEU A 1 241 ? -0.614  -3.447  -2.407  1.00 62.94  ? 241 LEU A O     1 
ATOM   1877 C  CB    . LEU A 1 241 ? 0.753   -5.998  -3.689  1.00 54.01  ? 241 LEU A CB    1 
ATOM   1878 C  CG    . LEU A 1 241 ? 2.053   -6.799  -3.622  1.00 55.18  ? 241 LEU A CG    1 
ATOM   1879 C  CD1   . LEU A 1 241 ? 2.705   -6.931  -4.993  1.00 53.49  ? 241 LEU A CD1   1 
ATOM   1880 C  CD2   . LEU A 1 241 ? 3.004   -6.153  -2.623  1.00 56.83  ? 241 LEU A CD2   1 
ATOM   1881 N  N     . GLY A 1 242 ? -2.165  -5.072  -2.376  1.00 56.86  ? 242 GLY A N     1 
ATOM   1882 C  CA    . GLY A 1 242 ? -3.258  -4.120  -2.389  1.00 58.70  ? 242 GLY A CA    1 
ATOM   1883 C  C     . GLY A 1 242 ? -3.488  -3.380  -1.089  1.00 68.60  ? 242 GLY A C     1 
ATOM   1884 O  O     . GLY A 1 242 ? -4.323  -2.471  -1.050  1.00 58.02  ? 242 GLY A O     1 
ATOM   1885 N  N     . LYS A 1 243 ? -2.774  -3.736  -0.022  1.00 63.90  ? 243 LYS A N     1 
ATOM   1886 C  CA    . LYS A 1 243 ? -2.984  -3.093  1.268   1.00 57.01  ? 243 LYS A CA    1 
ATOM   1887 C  C     . LYS A 1 243 ? -2.114  -1.849  1.394   1.00 59.31  ? 243 LYS A C     1 
ATOM   1888 O  O     . LYS A 1 243 ? -2.507  -0.768  0.946   1.00 63.06  ? 243 LYS A O     1 
ATOM   1889 C  CB    . LYS A 1 243 ? -2.705  -4.074  2.412   1.00 60.62  ? 243 LYS A CB    1 
ATOM   1890 C  CG    . LYS A 1 243 ? -3.155  -3.578  3.783   1.00 60.95  ? 243 LYS A CG    1 
ATOM   1891 C  CD    . LYS A 1 243 ? -3.250  -4.720  4.789   1.00 52.51  ? 243 LYS A CD    1 
ATOM   1892 C  CE    . LYS A 1 243 ? -3.568  -4.206  6.190   1.00 59.40  ? 243 LYS A CE    1 
ATOM   1893 N  NZ    . LYS A 1 243 ? -4.836  -3.422  6.250   1.00 51.86  ? 243 LYS A NZ    1 
ATOM   1894 N  N     . LYS A 1 244 ? -0.932  -1.986  1.996   1.00 59.35  ? 244 LYS A N     1 
ATOM   1895 C  CA    . LYS A 1 244 ? -0.057  -0.832  2.172   1.00 49.65  ? 244 LYS A CA    1 
ATOM   1896 C  C     . LYS A 1 244 ? 0.460   -0.326  0.831   1.00 51.92  ? 244 LYS A C     1 
ATOM   1897 O  O     . LYS A 1 244 ? 0.284   0.847   0.485   1.00 54.16  ? 244 LYS A O     1 
ATOM   1898 C  CB    . LYS A 1 244 ? 1.108   -1.191  3.094   1.00 54.09  ? 244 LYS A CB    1 
ATOM   1899 C  CG    . LYS A 1 244 ? 0.685   -1.678  4.466   1.00 59.15  ? 244 LYS A CG    1 
ATOM   1900 C  CD    . LYS A 1 244 ? -0.254  -0.692  5.131   1.00 56.81  ? 244 LYS A CD    1 
ATOM   1901 C  CE    . LYS A 1 244 ? -0.607  -1.132  6.540   1.00 53.75  ? 244 LYS A CE    1 
ATOM   1902 N  NZ    . LYS A 1 244 ? -1.533  -0.166  7.185   1.00 61.46  ? 244 LYS A NZ    1 
ATOM   1903 N  N     . CYS A 1 245 ? 1.098   -1.208  0.059   1.00 57.07  ? 245 CYS A N     1 
ATOM   1904 C  CA    . CYS A 1 245 ? 1.765   -0.798  -1.174  1.00 57.34  ? 245 CYS A CA    1 
ATOM   1905 C  C     . CYS A 1 245 ? 0.819   -0.048  -2.101  1.00 51.75  ? 245 CYS A C     1 
ATOM   1906 O  O     . CYS A 1 245 ? 1.164   1.011   -2.636  1.00 55.52  ? 245 CYS A O     1 
ATOM   1907 C  CB    . CYS A 1 245 ? 2.345   -2.025  -1.881  1.00 57.34  ? 245 CYS A CB    1 
ATOM   1908 S  SG    . CYS A 1 245 ? 3.488   -2.988  -0.873  1.00 54.43  ? 245 CYS A SG    1 
ATOM   1909 N  N     . PHE A 1 246 ? -0.380  -0.589  -2.310  1.00 51.15  ? 246 PHE A N     1 
ATOM   1910 C  CA    . PHE A 1 246 ? -1.350  0.009   -3.222  1.00 52.19  ? 246 PHE A CA    1 
ATOM   1911 C  C     . PHE A 1 246 ? -2.232  1.036   -2.511  1.00 58.09  ? 246 PHE A C     1 
ATOM   1912 O  O     . PHE A 1 246 ? -2.271  2.208   -2.901  1.00 53.72  ? 246 PHE A O     1 
ATOM   1913 C  CB    . PHE A 1 246 ? -2.202  -1.100  -3.855  1.00 52.27  ? 246 PHE A CB    1 
ATOM   1914 C  CG    . PHE A 1 246 ? -3.215  -0.612  -4.862  1.00 57.15  ? 246 PHE A CG    1 
ATOM   1915 C  CD1   . PHE A 1 246 ? -3.238  0.710   -5.283  1.00 58.81  ? 246 PHE A CD1   1 
ATOM   1916 C  CD2   . PHE A 1 246 ? -4.152  -1.491  -5.388  1.00 60.94  ? 246 PHE A CD2   1 
ATOM   1917 C  CE1   . PHE A 1 246 ? -4.176  1.147   -6.202  1.00 61.79  ? 246 PHE A CE1   1 
ATOM   1918 C  CE2   . PHE A 1 246 ? -5.091  -1.062  -6.309  1.00 61.45  ? 246 PHE A CE2   1 
ATOM   1919 C  CZ    . PHE A 1 246 ? -5.103  0.259   -6.715  1.00 69.26  ? 246 PHE A CZ    1 
ATOM   1920 N  N     . ALA A 1 247 ? -2.938  0.608   -1.461  1.00 54.14  ? 247 ALA A N     1 
ATOM   1921 C  CA    . ALA A 1 247 ? -4.004  1.424   -0.891  1.00 53.68  ? 247 ALA A CA    1 
ATOM   1922 C  C     . ALA A 1 247 ? -3.497  2.695   -0.218  1.00 50.17  ? 247 ALA A C     1 
ATOM   1923 O  O     . ALA A 1 247 ? -4.289  3.618   -0.005  1.00 50.36  ? 247 ALA A O     1 
ATOM   1924 C  CB    . ALA A 1 247 ? -4.818  0.595   0.104   1.00 51.36  ? 247 ALA A CB    1 
ATOM   1925 N  N     . LEU A 1 248 ? -2.210  2.768   0.126   1.00 55.60  ? 248 LEU A N     1 
ATOM   1926 C  CA    . LEU A 1 248 ? -1.645  3.968   0.738   1.00 50.04  ? 248 LEU A CA    1 
ATOM   1927 C  C     . LEU A 1 248 ? -0.558  4.601   -0.121  1.00 55.82  ? 248 LEU A C     1 
ATOM   1928 O  O     . LEU A 1 248 ? -0.703  5.758   -0.529  1.00 59.21  ? 248 LEU A O     1 
ATOM   1929 C  CB    . LEU A 1 248 ? -1.108  3.646   2.139   1.00 49.92  ? 248 LEU A CB    1 
ATOM   1930 C  CG    . LEU A 1 248 ? -2.192  3.373   3.184   1.00 56.46  ? 248 LEU A CG    1 
ATOM   1931 C  CD1   . LEU A 1 248 ? -1.610  3.327   4.591   1.00 52.67  ? 248 LEU A CD1   1 
ATOM   1932 C  CD2   . LEU A 1 248 ? -3.297  4.417   3.085   1.00 50.10  ? 248 LEU A CD2   1 
ATOM   1933 N  N     . ARG A 1 249 ? 0.531   3.888   -0.413  1.00 51.41  ? 249 ARG A N     1 
ATOM   1934 C  CA    . ARG A 1 249 ? 1.669   4.529   -1.064  1.00 54.20  ? 249 ARG A CA    1 
ATOM   1935 C  C     . ARG A 1 249 ? 1.330   4.949   -2.490  1.00 52.17  ? 249 ARG A C     1 
ATOM   1936 O  O     . ARG A 1 249 ? 1.411   6.133   -2.836  1.00 57.04  ? 249 ARG A O     1 
ATOM   1937 C  CB    . ARG A 1 249 ? 2.886   3.604   -1.032  1.00 50.45  ? 249 ARG A CB    1 
ATOM   1938 C  CG    . ARG A 1 249 ? 3.343   3.295   0.385   1.00 57.08  ? 249 ARG A CG    1 
ATOM   1939 C  CD    . ARG A 1 249 ? 4.744   2.706   0.432   1.00 59.90  ? 249 ARG A CD    1 
ATOM   1940 N  NE    . ARG A 1 249 ? 5.021   2.122   1.740   1.00 57.33  ? 249 ARG A NE    1 
ATOM   1941 C  CZ    . ARG A 1 249 ? 4.887   0.834   2.025   1.00 58.41  ? 249 ARG A CZ    1 
ATOM   1942 N  NH1   . ARG A 1 249 ? 4.525   -0.043  1.103   1.00 55.60  ? 249 ARG A NH1   1 
ATOM   1943 N  NH2   . ARG A 1 249 ? 5.121   0.417   3.267   1.00 58.22  ? 249 ARG A NH2   1 
ATOM   1944 N  N     . ILE A 1 250 ? 0.943   3.996   -3.337  1.00 52.90  ? 250 ILE A N     1 
ATOM   1945 C  CA    . ILE A 1 250 ? 0.565   4.357   -4.700  1.00 54.83  ? 250 ILE A CA    1 
ATOM   1946 C  C     . ILE A 1 250 ? -0.688  5.223   -4.693  1.00 57.17  ? 250 ILE A C     1 
ATOM   1947 O  O     . ILE A 1 250 ? -0.786  6.205   -5.439  1.00 58.35  ? 250 ILE A O     1 
ATOM   1948 C  CB    . ILE A 1 250 ? 0.375   3.098   -5.563  1.00 56.85  ? 250 ILE A CB    1 
ATOM   1949 C  CG1   . ILE A 1 250 ? 1.690   2.326   -5.679  1.00 57.09  ? 250 ILE A CG1   1 
ATOM   1950 C  CG2   . ILE A 1 250 ? -0.148  3.481   -6.939  1.00 59.20  ? 250 ILE A CG2   1 
ATOM   1951 C  CD1   . ILE A 1 250 ? 2.798   3.108   -6.341  1.00 53.02  ? 250 ILE A CD1   1 
ATOM   1952 N  N     . ALA A 1 251 ? -1.664  4.879   -3.850  1.00 58.74  ? 251 ALA A N     1 
ATOM   1953 C  CA    . ALA A 1 251 ? -2.916  5.626   -3.820  1.00 57.40  ? 251 ALA A CA    1 
ATOM   1954 C  C     . ALA A 1 251 ? -2.696  7.068   -3.380  1.00 52.62  ? 251 ALA A C     1 
ATOM   1955 O  O     . ALA A 1 251 ? -3.352  7.985   -3.887  1.00 57.02  ? 251 ALA A O     1 
ATOM   1956 C  CB    . ALA A 1 251 ? -3.918  4.931   -2.900  1.00 54.65  ? 251 ALA A CB    1 
ATOM   1957 N  N     . SER A 1 252 ? -1.785  7.290   -2.430  1.00 51.70  ? 252 SER A N     1 
ATOM   1958 C  CA    . SER A 1 252 ? -1.519  8.651   -1.980  1.00 52.14  ? 252 SER A CA    1 
ATOM   1959 C  C     . SER A 1 252 ? -0.993  9.506   -3.124  1.00 63.20  ? 252 SER A C     1 
ATOM   1960 O  O     . SER A 1 252 ? -1.408  10.659  -3.293  1.00 57.14  ? 252 SER A O     1 
ATOM   1961 C  CB    . SER A 1 252 ? -0.530  8.641   -0.815  1.00 51.89  ? 252 SER A CB    1 
ATOM   1962 O  OG    . SER A 1 252 ? 0.765   8.261   -1.243  1.00 55.11  ? 252 SER A OG    1 
ATOM   1963 N  N     . ARG A 1 253 ? -0.078  8.954   -3.924  1.00 54.41  ? 253 ARG A N     1 
ATOM   1964 C  CA    . ARG A 1 253 ? 0.398   9.660   -5.108  1.00 55.16  ? 253 ARG A CA    1 
ATOM   1965 C  C     . ARG A 1 253 ? -0.756  9.977   -6.050  1.00 58.10  ? 253 ARG A C     1 
ATOM   1966 O  O     . ARG A 1 253 ? -0.911  11.117  -6.502  1.00 62.36  ? 253 ARG A O     1 
ATOM   1967 C  CB    . ARG A 1 253 ? 1.468   8.824   -5.811  1.00 64.06  ? 253 ARG A CB    1 
ATOM   1968 C  CG    . ARG A 1 253 ? 1.886   9.324   -7.188  1.00 66.80  ? 253 ARG A CG    1 
ATOM   1969 C  CD    . ARG A 1 253 ? 2.774   10.551  -7.104  1.00 70.34  ? 253 ARG A CD    1 
ATOM   1970 N  NE    . ARG A 1 253 ? 3.714   10.610  -8.217  1.00 78.31  ? 253 ARG A NE    1 
ATOM   1971 C  CZ    . ARG A 1 253 ? 4.980   10.220  -8.147  1.00 76.62  ? 253 ARG A CZ    1 
ATOM   1972 N  NH1   . ARG A 1 253 ? 5.496   9.748   -7.023  1.00 68.59  ? 253 ARG A NH1   1 
ATOM   1973 N  NH2   . ARG A 1 253 ? 5.748   10.312  -9.230  1.00 76.56  ? 253 ARG A NH2   1 
ATOM   1974 N  N     . LEU A 1 254 ? -1.587  8.976   -6.350  1.00 59.10  ? 254 LEU A N     1 
ATOM   1975 C  CA    . LEU A 1 254 ? -2.736  9.202   -7.221  1.00 60.21  ? 254 LEU A CA    1 
ATOM   1976 C  C     . LEU A 1 254 ? -3.653  10.276  -6.649  1.00 67.40  ? 254 LEU A C     1 
ATOM   1977 O  O     . LEU A 1 254 ? -4.034  11.221  -7.348  1.00 65.35  ? 254 LEU A O     1 
ATOM   1978 C  CB    . LEU A 1 254 ? -3.506  7.897   -7.429  1.00 65.28  ? 254 LEU A CB    1 
ATOM   1979 C  CG    . LEU A 1 254 ? -2.811  6.747   -8.159  1.00 69.29  ? 254 LEU A CG    1 
ATOM   1980 C  CD1   . LEU A 1 254 ? -3.724  5.530   -8.210  1.00 69.70  ? 254 LEU A CD1   1 
ATOM   1981 C  CD2   . LEU A 1 254 ? -2.401  7.166   -9.560  1.00 73.23  ? 254 LEU A CD2   1 
ATOM   1982 N  N     . ALA A 1 255 ? -4.021  10.142  -5.371  1.00 58.35  ? 255 ALA A N     1 
ATOM   1983 C  CA    . ALA A 1 255 ? -4.930  11.105  -4.757  1.00 62.62  ? 255 ALA A CA    1 
ATOM   1984 C  C     . ALA A 1 255 ? -4.397  12.526  -4.883  1.00 65.33  ? 255 ALA A C     1 
ATOM   1985 O  O     . ALA A 1 255 ? -5.149  13.452  -5.213  1.00 63.07  ? 255 ALA A O     1 
ATOM   1986 C  CB    . ALA A 1 255 ? -5.164  10.744  -3.291  1.00 61.16  ? 255 ALA A CB    1 
ATOM   1987 N  N     . LYS A 1 256 ? -3.102  12.720  -4.624  1.00 63.49  ? 256 LYS A N     1 
ATOM   1988 C  CA    . LYS A 1 256 ? -2.495  14.026  -4.858  1.00 58.69  ? 256 LYS A CA    1 
ATOM   1989 C  C     . LYS A 1 256 ? -2.714  14.479  -6.295  1.00 65.92  ? 256 LYS A C     1 
ATOM   1990 O  O     . LYS A 1 256 ? -3.053  15.641  -6.544  1.00 68.13  ? 256 LYS A O     1 
ATOM   1991 C  CB    . LYS A 1 256 ? -1.002  13.976  -4.529  1.00 60.38  ? 256 LYS A CB    1 
ATOM   1992 C  CG    . LYS A 1 256 ? -0.222  15.207  -4.971  1.00 62.84  ? 256 LYS A CG    1 
ATOM   1993 C  CD    . LYS A 1 256 ? -0.712  16.463  -4.266  1.00 63.55  ? 256 LYS A CD    1 
ATOM   1994 C  CE    . LYS A 1 256 ? 0.112   17.685  -4.659  1.00 67.71  ? 256 LYS A CE    1 
ATOM   1995 N  NZ    . LYS A 1 256 ? -0.063  18.051  -6.093  1.00 71.01  ? 256 LYS A NZ    1 
ATOM   1996 N  N     . GLU A 1 257 ? -2.534  13.567  -7.256  1.00 65.63  ? 257 GLU A N     1 
ATOM   1997 C  CA    . GLU A 1 257 ? -2.761  13.909  -8.657  1.00 65.29  ? 257 GLU A CA    1 
ATOM   1998 C  C     . GLU A 1 257 ? -4.231  14.204  -8.930  1.00 67.39  ? 257 GLU A C     1 
ATOM   1999 O  O     . GLU A 1 257 ? -4.558  15.179  -9.617  1.00 69.55  ? 257 GLU A O     1 
ATOM   2000 C  CB    . GLU A 1 257 ? -2.286  12.773  -9.566  1.00 74.96  ? 257 GLU A CB    1 
ATOM   2001 C  CG    . GLU A 1 257 ? -0.817  12.402  -9.448  1.00 70.73  ? 257 GLU A CG    1 
ATOM   2002 C  CD    . GLU A 1 257 ? -0.480  11.159  -10.253 1.00 76.75  ? 257 GLU A CD    1 
ATOM   2003 O  OE1   . GLU A 1 257 ? -1.285  10.787  -11.134 1.00 74.06  ? 257 GLU A OE1   1 
ATOM   2004 O  OE2   . GLU A 1 257 ? 0.581   10.547  -10.001 1.00 76.57  ? 257 GLU A OE2   1 
ATOM   2005 N  N     . GLU A 1 258 ? -5.128  13.370  -8.405  1.00 67.26  ? 258 GLU A N     1 
ATOM   2006 C  CA    . GLU A 1 258 ? -6.538  13.406  -8.771  1.00 66.94  ? 258 GLU A CA    1 
ATOM   2007 C  C     . GLU A 1 258 ? -7.388  14.263  -7.841  1.00 69.15  ? 258 GLU A C     1 
ATOM   2008 O  O     . GLU A 1 258 ? -8.545  14.543  -8.174  1.00 72.79  ? 258 GLU A O     1 
ATOM   2009 C  CB    . GLU A 1 258 ? -7.102  11.980  -8.808  1.00 72.40  ? 258 GLU A CB    1 
ATOM   2010 C  CG    . GLU A 1 258 ? -6.338  11.042  -9.730  1.00 68.96  ? 258 GLU A CG    1 
ATOM   2011 C  CD    . GLU A 1 258 ? -6.732  9.589   -9.542  1.00 83.09  ? 258 GLU A CD    1 
ATOM   2012 O  OE1   . GLU A 1 258 ? -7.827  9.334   -8.999  1.00 79.54  ? 258 GLU A OE1   1 
ATOM   2013 O  OE2   . GLU A 1 258 ? -5.941  8.702   -9.932  1.00 82.70  ? 258 GLU A OE2   1 
ATOM   2014 N  N     . GLY A 1 259 ? -6.864  14.669  -6.690  1.00 67.88  ? 259 GLY A N     1 
ATOM   2015 C  CA    . GLY A 1 259 ? -7.556  15.600  -5.824  1.00 65.80  ? 259 GLY A CA    1 
ATOM   2016 C  C     . GLY A 1 259 ? -8.258  15.008  -4.622  1.00 62.28  ? 259 GLY A C     1 
ATOM   2017 O  O     . GLY A 1 259 ? -8.996  15.733  -3.946  1.00 70.30  ? 259 GLY A O     1 
ATOM   2018 N  N     . TRP A 1 260 ? -8.062  13.727  -4.330  1.00 63.75  ? 260 TRP A N     1 
ATOM   2019 C  CA    . TRP A 1 260 ? -8.659  13.120  -3.156  1.00 62.63  ? 260 TRP A CA    1 
ATOM   2020 C  C     . TRP A 1 260 ? -7.567  12.824  -2.125  1.00 60.84  ? 260 TRP A C     1 
ATOM   2021 O  O     . TRP A 1 260 ? -6.499  13.454  -2.135  1.00 58.88  ? 260 TRP A O     1 
ATOM   2022 C  CB    . TRP A 1 260 ? -9.460  11.878  -3.569  1.00 65.76  ? 260 TRP A CB    1 
ATOM   2023 C  CG    . TRP A 1 260 ? -8.750  10.941  -4.513  1.00 66.94  ? 260 TRP A CG    1 
ATOM   2024 C  CD1   . TRP A 1 260 ? -8.497  11.148  -5.839  1.00 62.87  ? 260 TRP A CD1   1 
ATOM   2025 C  CD2   . TRP A 1 260 ? -8.236  9.637   -4.209  1.00 59.68  ? 260 TRP A CD2   1 
ATOM   2026 N  NE1   . TRP A 1 260 ? -7.845  10.066  -6.372  1.00 63.99  ? 260 TRP A NE1   1 
ATOM   2027 C  CE2   . TRP A 1 260 ? -7.673  9.123   -5.394  1.00 61.22  ? 260 TRP A CE2   1 
ATOM   2028 C  CE3   . TRP A 1 260 ? -8.191  8.858   -3.048  1.00 60.64  ? 260 TRP A CE3   1 
ATOM   2029 C  CZ2   . TRP A 1 260 ? -7.072  7.867   -5.453  1.00 62.30  ? 260 TRP A CZ2   1 
ATOM   2030 C  CZ3   . TRP A 1 260 ? -7.594  7.609   -3.110  1.00 59.31  ? 260 TRP A CZ3   1 
ATOM   2031 C  CH2   . TRP A 1 260 ? -7.042  7.127   -4.304  1.00 58.86  ? 260 TRP A CH2   1 
ATOM   2032 N  N     . LEU A 1 261 ? -7.833  11.871  -1.234  1.00 63.07  ? 261 LEU A N     1 
ATOM   2033 C  CA    . LEU A 1 261 ? -6.930  11.561  -0.136  1.00 57.27  ? 261 LEU A CA    1 
ATOM   2034 C  C     . LEU A 1 261 ? -6.903  10.061  0.113   1.00 57.94  ? 261 LEU A C     1 
ATOM   2035 O  O     . LEU A 1 261 ? -7.933  9.387   0.022   1.00 57.11  ? 261 LEU A O     1 
ATOM   2036 C  CB    . LEU A 1 261 ? -7.349  12.291  1.149   1.00 52.96  ? 261 LEU A CB    1 
ATOM   2037 C  CG    . LEU A 1 261 ? -7.292  13.820  1.134   1.00 56.03  ? 261 LEU A CG    1 
ATOM   2038 C  CD1   . LEU A 1 261 ? -7.930  14.401  2.393   1.00 53.70  ? 261 LEU A CD1   1 
ATOM   2039 C  CD2   . LEU A 1 261 ? -5.855  14.296  0.991   1.00 54.01  ? 261 LEU A CD2   1 
ATOM   2040 N  N     . ALA A 1 262 ? -5.716  9.547   0.431   1.00 55.49  ? 262 ALA A N     1 
ATOM   2041 C  CA    . ALA A 1 262 ? -5.521  8.154   0.823   1.00 51.30  ? 262 ALA A CA    1 
ATOM   2042 C  C     . ALA A 1 262 ? -4.783  8.164   2.153   1.00 51.02  ? 262 ALA A C     1 
ATOM   2043 O  O     . ALA A 1 262 ? -3.618  8.570   2.214   1.00 51.12  ? 262 ALA A O     1 
ATOM   2044 C  CB    . ALA A 1 262 ? -4.739  7.376   -0.238  1.00 51.23  ? 262 ALA A CB    1 
ATOM   2045 N  N     . GLU A 1 263 ? -5.448  7.710   3.215   1.00 50.85  ? 263 GLU A N     1 
ATOM   2046 C  CA    . GLU A 1 263 ? -4.972  7.976   4.564   1.00 55.36  ? 263 GLU A CA    1 
ATOM   2047 C  C     . GLU A 1 263 ? -5.011  6.719   5.418   1.00 50.69  ? 263 GLU A C     1 
ATOM   2048 O  O     . GLU A 1 263 ? -5.847  5.833   5.223   1.00 50.61  ? 263 GLU A O     1 
ATOM   2049 C  CB    . GLU A 1 263 ? -5.800  9.081   5.230   1.00 51.20  ? 263 GLU A CB    1 
ATOM   2050 C  CG    . GLU A 1 263 ? -5.844  10.371  4.425   1.00 51.59  ? 263 GLU A CG    1 
ATOM   2051 C  CD    . GLU A 1 263 ? -4.488  11.039  4.325   1.00 51.88  ? 263 GLU A CD    1 
ATOM   2052 O  OE1   . GLU A 1 263 ? -3.599  10.708  5.135   1.00 51.82  ? 263 GLU A OE1   1 
ATOM   2053 O  OE2   . GLU A 1 263 ? -4.309  11.899  3.437   1.00 53.77  ? 263 GLU A OE2   1 
ATOM   2054 N  N     . HIS A 1 264 ? -4.098  6.675   6.389   1.00 50.77  ? 264 HIS A N     1 
ATOM   2055 C  CA    . HIS A 1 264 ? -3.956  5.557   7.320   1.00 51.35  ? 264 HIS A CA    1 
ATOM   2056 C  C     . HIS A 1 264 ? -4.924  5.742   8.492   1.00 55.53  ? 264 HIS A C     1 
ATOM   2057 O  O     . HIS A 1 264 ? -4.538  5.954   9.643   1.00 51.58  ? 264 HIS A O     1 
ATOM   2058 C  CB    . HIS A 1 264 ? -2.509  5.472   7.789   1.00 50.99  ? 264 HIS A CB    1 
ATOM   2059 C  CG    . HIS A 1 264 ? -2.204  4.264   8.618   1.00 51.18  ? 264 HIS A CG    1 
ATOM   2060 N  ND1   . HIS A 1 264 ? -1.080  4.175   9.410   1.00 51.62  ? 264 HIS A ND1   1 
ATOM   2061 C  CD2   . HIS A 1 264 ? -2.866  3.093   8.770   1.00 51.19  ? 264 HIS A CD2   1 
ATOM   2062 C  CE1   . HIS A 1 264 ? -1.065  3.004   10.020  1.00 51.87  ? 264 HIS A CE1   1 
ATOM   2063 N  NE2   . HIS A 1 264 ? -2.138  2.329   9.648   1.00 51.62  ? 264 HIS A NE2   1 
ATOM   2064 N  N     . MET A 1 265 ? -6.216  5.648   8.179   1.00 51.16  ? 265 MET A N     1 
ATOM   2065 C  CA    . MET A 1 265 ? -7.262  6.007   9.126   1.00 52.66  ? 265 MET A CA    1 
ATOM   2066 C  C     . MET A 1 265 ? -8.336  4.932   9.208   1.00 55.40  ? 265 MET A C     1 
ATOM   2067 O  O     . MET A 1 265 ? -8.768  4.390   8.187   1.00 59.17  ? 265 MET A O     1 
ATOM   2068 C  CB    . MET A 1 265 ? -7.925  7.336   8.742   1.00 51.59  ? 265 MET A CB    1 
ATOM   2069 C  CG    . MET A 1 265 ? -6.996  8.529   8.702   1.00 51.62  ? 265 MET A CG    1 
ATOM   2070 S  SD    . MET A 1 265 ? -7.865  9.994   8.104   1.00 58.82  ? 265 MET A SD    1 
ATOM   2071 C  CE    . MET A 1 265 ? -6.562  11.219  8.190   1.00 53.10  ? 265 MET A CE    1 
ATOM   2072 N  N     . LEU A 1 266 ? -8.775  4.646   10.432  1.00 54.27  ? 266 LEU A N     1 
ATOM   2073 C  CA    . LEU A 1 266 ? -10.015 3.916   10.630  1.00 52.85  ? 266 LEU A CA    1 
ATOM   2074 C  C     . LEU A 1 266 ? -11.201 4.830   10.336  1.00 56.76  ? 266 LEU A C     1 
ATOM   2075 O  O     . LEU A 1 266 ? -11.102 6.059   10.397  1.00 53.22  ? 266 LEU A O     1 
ATOM   2076 C  CB    . LEU A 1 266 ? -10.104 3.388   12.062  1.00 53.61  ? 266 LEU A CB    1 
ATOM   2077 C  CG    . LEU A 1 266 ? -10.425 4.432   13.141  1.00 54.01  ? 266 LEU A CG    1 
ATOM   2078 C  CD1   . LEU A 1 266 ? -11.929 4.567   13.344  1.00 54.53  ? 266 LEU A CD1   1 
ATOM   2079 C  CD2   . LEU A 1 266 ? -9.729  4.111   14.454  1.00 54.66  ? 266 LEU A CD2   1 
ATOM   2080 N  N     . ILE A 1 267 ? -12.336 4.218   10.009  1.00 53.84  ? 267 ILE A N     1 
ATOM   2081 C  CA    . ILE A 1 267 ? -13.587 4.944   9.813   1.00 55.06  ? 267 ILE A CA    1 
ATOM   2082 C  C     . ILE A 1 267 ? -14.652 4.263   10.657  1.00 57.88  ? 267 ILE A C     1 
ATOM   2083 O  O     . ILE A 1 267 ? -14.885 3.056   10.513  1.00 55.35  ? 267 ILE A O     1 
ATOM   2084 C  CB    . ILE A 1 267 ? -14.019 4.988   8.338   1.00 55.68  ? 267 ILE A CB    1 
ATOM   2085 C  CG1   . ILE A 1 267 ? -12.908 5.569   7.464   1.00 52.85  ? 267 ILE A CG1   1 
ATOM   2086 C  CG2   . ILE A 1 267 ? -15.299 5.804   8.182   1.00 54.09  ? 267 ILE A CG2   1 
ATOM   2087 C  CD1   . ILE A 1 267 ? -13.156 5.384   5.982   1.00 52.88  ? 267 ILE A CD1   1 
ATOM   2088 N  N     . LEU A 1 268 ? -15.293 5.029   11.535  1.00 55.06  ? 268 LEU A N     1 
ATOM   2089 C  CA    . LEU A 1 268 ? -16.368 4.521   12.371  1.00 59.12  ? 268 LEU A CA    1 
ATOM   2090 C  C     . LEU A 1 268 ? -17.535 5.495   12.350  1.00 62.66  ? 268 LEU A C     1 
ATOM   2091 O  O     . LEU A 1 268 ? -17.343 6.713   12.280  1.00 61.87  ? 268 LEU A O     1 
ATOM   2092 C  CB    . LEU A 1 268 ? -15.894 4.287   13.818  1.00 58.42  ? 268 LEU A CB    1 
ATOM   2093 C  CG    . LEU A 1 268 ? -15.469 5.494   14.660  1.00 56.43  ? 268 LEU A CG    1 
ATOM   2094 C  CD1   . LEU A 1 268 ? -16.674 6.160   15.311  1.00 57.09  ? 268 LEU A CD1   1 
ATOM   2095 C  CD2   . LEU A 1 268 ? -14.441 5.089   15.709  1.00 56.64  ? 268 LEU A CD2   1 
ATOM   2096 N  N     . GLY A 1 269 ? -18.744 4.947   12.388  1.00 64.37  ? 269 GLY A N     1 
ATOM   2097 C  CA    . GLY A 1 269 ? -19.947 5.731   12.569  1.00 61.75  ? 269 GLY A CA    1 
ATOM   2098 C  C     . GLY A 1 269 ? -20.426 5.600   14.001  1.00 58.96  ? 269 GLY A C     1 
ATOM   2099 O  O     . GLY A 1 269 ? -20.247 4.564   14.637  1.00 59.58  ? 269 GLY A O     1 
ATOM   2100 N  N     . ILE A 1 270 ? -21.032 6.668   14.510  1.00 61.20  ? 270 ILE A N     1 
ATOM   2101 C  CA    . ILE A 1 270 ? -21.448 6.730   15.905  1.00 60.08  ? 270 ILE A CA    1 
ATOM   2102 C  C     . ILE A 1 270 ? -22.811 7.400   15.989  1.00 60.84  ? 270 ILE A C     1 
ATOM   2103 O  O     . ILE A 1 270 ? -23.075 8.390   15.299  1.00 60.35  ? 270 ILE A O     1 
ATOM   2104 C  CB    . ILE A 1 270 ? -20.409 7.474   16.769  1.00 59.53  ? 270 ILE A CB    1 
ATOM   2105 C  CG1   . ILE A 1 270 ? -20.875 7.543   18.222  1.00 60.66  ? 270 ILE A CG1   1 
ATOM   2106 C  CG2   . ILE A 1 270 ? -20.157 8.868   16.216  1.00 58.64  ? 270 ILE A CG2   1 
ATOM   2107 C  CD1   . ILE A 1 270 ? -19.815 8.042   19.169  1.00 60.76  ? 270 ILE A CD1   1 
ATOM   2108 N  N     . THR A 1 271 ? -23.676 6.855   16.841  1.00 62.19  ? 271 THR A N     1 
ATOM   2109 C  CA    . THR A 1 271 ? -25.036 7.339   17.024  1.00 65.22  ? 271 THR A CA    1 
ATOM   2110 C  C     . THR A 1 271 ? -25.275 7.603   18.502  1.00 67.32  ? 271 THR A C     1 
ATOM   2111 O  O     . THR A 1 271 ? -24.824 6.834   19.356  1.00 64.60  ? 271 THR A O     1 
ATOM   2112 C  CB    . THR A 1 271 ? -26.065 6.324   16.504  1.00 64.39  ? 271 THR A CB    1 
ATOM   2113 O  OG1   . THR A 1 271 ? -25.868 6.110   15.101  1.00 65.74  ? 271 THR A OG1   1 
ATOM   2114 C  CG2   . THR A 1 271 ? -27.480 6.823   16.745  1.00 65.59  ? 271 THR A CG2   1 
ATOM   2115 N  N     . ASN A 1 272 ? -25.980 8.683   18.800  1.00 64.27  ? 272 ASN A N     1 
ATOM   2116 C  CA    . ASN A 1 272 ? -26.266 9.077   20.169  1.00 67.61  ? 272 ASN A CA    1 
ATOM   2117 C  C     . ASN A 1 272 ? -27.695 8.719   20.543  1.00 68.90  ? 272 ASN A C     1 
ATOM   2118 O  O     . ASN A 1 272 ? -28.481 8.261   19.709  1.00 69.61  ? 272 ASN A O     1 
ATOM   2119 C  CB    . ASN A 1 272 ? -26.015 10.580  20.351  1.00 73.40  ? 272 ASN A CB    1 
ATOM   2120 C  CG    . ASN A 1 272 ? -26.947 11.449  19.516  1.00 66.49  ? 272 ASN A CG    1 
ATOM   2121 O  OD1   . ASN A 1 272 ? -27.869 10.960  18.865  1.00 70.99  ? 272 ASN A OD1   1 
ATOM   2122 N  ND2   . ASN A 1 272 ? -26.709 12.755  19.545  1.00 72.93  ? 272 ASN A ND2   1 
ATOM   2123 N  N     . PRO A 1 273 ? -28.069 8.908   21.811  1.00 73.49  ? 273 PRO A N     1 
ATOM   2124 C  CA    . PRO A 1 273 ? -29.432 8.546   22.235  1.00 71.61  ? 273 PRO A CA    1 
ATOM   2125 C  C     . PRO A 1 273 ? -30.523 9.385   21.588  1.00 74.49  ? 273 PRO A C     1 
ATOM   2126 O  O     . PRO A 1 273 ? -31.695 8.991   21.646  1.00 71.76  ? 273 PRO A O     1 
ATOM   2127 C  CB    . PRO A 1 273 ? -29.394 8.759   23.754  1.00 73.81  ? 273 PRO A CB    1 
ATOM   2128 C  CG    . PRO A 1 273 ? -27.938 8.703   24.113  1.00 69.74  ? 273 PRO A CG    1 
ATOM   2129 C  CD    . PRO A 1 273 ? -27.223 9.304   22.948  1.00 67.82  ? 273 PRO A CD    1 
ATOM   2130 N  N     . GLU A 1 274 ? -30.188 10.520  20.982  1.00 80.35  ? 274 GLU A N     1 
ATOM   2131 C  CA    . GLU A 1 274 ? -31.176 11.378  20.340  1.00 81.64  ? 274 GLU A CA    1 
ATOM   2132 C  C     . GLU A 1 274 ? -31.488 10.958  18.909  1.00 79.68  ? 274 GLU A C     1 
ATOM   2133 O  O     . GLU A 1 274 ? -32.305 11.613  18.252  1.00 76.79  ? 274 GLU A O     1 
ATOM   2134 C  CB    . GLU A 1 274 ? -30.699 12.835  20.351  1.00 77.72  ? 274 GLU A CB    1 
ATOM   2135 C  CG    . GLU A 1 274 ? -30.382 13.373  21.735  1.00 77.85  ? 274 GLU A CG    1 
ATOM   2136 C  CD    . GLU A 1 274 ? -31.583 13.347  22.656  1.00 84.50  ? 274 GLU A CD    1 
ATOM   2137 O  OE1   . GLU A 1 274 ? -32.721 13.258  22.148  1.00 81.73  ? 274 GLU A OE1   1 
ATOM   2138 O  OE2   . GLU A 1 274 ? -31.388 13.412  23.888  1.00 94.65  ? 274 GLU A OE2   1 
ATOM   2139 N  N     . GLY A 1 275 ? -30.862 9.893   18.412  1.00 79.51  ? 275 GLY A N     1 
ATOM   2140 C  CA    . GLY A 1 275 ? -31.070 9.444   17.053  1.00 80.59  ? 275 GLY A CA    1 
ATOM   2141 C  C     . GLY A 1 275 ? -30.152 10.056  16.016  1.00 79.91  ? 275 GLY A C     1 
ATOM   2142 O  O     . GLY A 1 275 ? -30.309 9.758   14.825  1.00 81.37  ? 275 GLY A O     1 
ATOM   2143 N  N     . LYS A 1 276 ? -29.202 10.898  16.422  1.00 78.55  ? 276 LYS A N     1 
ATOM   2144 C  CA    . LYS A 1 276 ? -28.278 11.533  15.492  1.00 73.34  ? 276 LYS A CA    1 
ATOM   2145 C  C     . LYS A 1 276 ? -27.011 10.692  15.378  1.00 73.66  ? 276 LYS A C     1 
ATOM   2146 O  O     . LYS A 1 276 ? -26.452 10.260  16.392  1.00 74.71  ? 276 LYS A O     1 
ATOM   2147 C  CB    . LYS A 1 276 ? -27.935 12.952  15.950  1.00 72.53  ? 276 LYS A CB    1 
ATOM   2148 C  CG    . LYS A 1 276 ? -29.105 13.739  16.547  1.00 77.91  ? 276 LYS A CG    1 
ATOM   2149 C  CD    . LYS A 1 276 ? -30.295 13.814  15.600  1.00 71.46  ? 276 LYS A CD    1 
ATOM   2150 C  CE    . LYS A 1 276 ? -31.231 14.959  15.976  1.00 75.77  ? 276 LYS A CE    1 
ATOM   2151 N  NZ    . LYS A 1 276 ? -31.775 14.852  17.362  1.00 75.16  ? 276 LYS A NZ    1 
ATOM   2152 N  N     . LYS A 1 277 ? -26.561 10.462  14.145  1.00 71.10  ? 277 LYS A N     1 
ATOM   2153 C  CA    . LYS A 1 277 ? -25.394 9.635   13.870  1.00 64.33  ? 277 LYS A CA    1 
ATOM   2154 C  C     . LYS A 1 277 ? -24.359 10.428  13.083  1.00 64.44  ? 277 LYS A C     1 
ATOM   2155 O  O     . LYS A 1 277 ? -24.700 11.151  12.141  1.00 64.13  ? 277 LYS A O     1 
ATOM   2156 C  CB    . LYS A 1 277 ? -25.788 8.376   13.092  1.00 61.96  ? 277 LYS A CB    1 
ATOM   2157 C  CG    . LYS A 1 277 ? -24.620 7.484   12.715  1.00 61.17  ? 277 LYS A CG    1 
ATOM   2158 C  CD    . LYS A 1 277 ? -25.087 6.299   11.887  1.00 61.95  ? 277 LYS A CD    1 
ATOM   2159 C  CE    . LYS A 1 277 ? -23.926 5.387   11.514  1.00 66.35  ? 277 LYS A CE    1 
ATOM   2160 N  NZ    . LYS A 1 277 ? -24.393 4.154   10.820  1.00 64.24  ? 277 LYS A NZ    1 
ATOM   2161 N  N     . LYS A 1 278 ? -23.093 10.284  13.467  1.00 59.18  ? 278 LYS A N     1 
ATOM   2162 C  CA    . LYS A 1 278 ? -21.996 10.972  12.806  1.00 62.18  ? 278 LYS A CA    1 
ATOM   2163 C  C     . LYS A 1 278 ? -20.882 9.987   12.486  1.00 61.60  ? 278 LYS A C     1 
ATOM   2164 O  O     . LYS A 1 278 ? -20.723 8.963   13.156  1.00 57.90  ? 278 LYS A O     1 
ATOM   2165 C  CB    . LYS A 1 278 ? -21.451 12.112  13.670  1.00 57.81  ? 278 LYS A CB    1 
ATOM   2166 C  CG    . LYS A 1 278 ? -22.459 13.217  13.915  1.00 59.75  ? 278 LYS A CG    1 
ATOM   2167 C  CD    . LYS A 1 278 ? -21.850 14.371  14.687  1.00 59.94  ? 278 LYS A CD    1 
ATOM   2168 C  CE    . LYS A 1 278 ? -22.836 15.521  14.790  1.00 60.74  ? 278 LYS A CE    1 
ATOM   2169 N  NZ    . LYS A 1 278 ? -23.364 15.881  13.445  1.00 58.78  ? 278 LYS A NZ    1 
ATOM   2170 N  N     . TYR A 1 279 ? -20.110 10.311  11.452  1.00 63.14  ? 279 TYR A N     1 
ATOM   2171 C  CA    . TYR A 1 279 ? -18.995 9.487   11.007  1.00 56.04  ? 279 TYR A CA    1 
ATOM   2172 C  C     . TYR A 1 279 ? -17.680 10.173  11.346  1.00 55.31  ? 279 TYR A C     1 
ATOM   2173 O  O     . TYR A 1 279 ? -17.489 11.352  11.032  1.00 56.00  ? 279 TYR A O     1 
ATOM   2174 C  CB    . TYR A 1 279 ? -19.075 9.220   9.506   1.00 56.66  ? 279 TYR A CB    1 
ATOM   2175 C  CG    . TYR A 1 279 ? -20.093 8.171   9.141   1.00 63.08  ? 279 TYR A CG    1 
ATOM   2176 C  CD1   . TYR A 1 279 ? -19.781 6.820   9.216   1.00 56.85  ? 279 TYR A CD1   1 
ATOM   2177 C  CD2   . TYR A 1 279 ? -21.368 8.529   8.727   1.00 59.92  ? 279 TYR A CD2   1 
ATOM   2178 C  CE1   . TYR A 1 279 ? -20.710 5.854   8.886   1.00 57.82  ? 279 TYR A CE1   1 
ATOM   2179 C  CE2   . TYR A 1 279 ? -22.305 7.570   8.393   1.00 63.17  ? 279 TYR A CE2   1 
ATOM   2180 C  CZ    . TYR A 1 279 ? -21.971 6.234   8.475   1.00 62.65  ? 279 TYR A CZ    1 
ATOM   2181 O  OH    . TYR A 1 279 ? -22.904 5.278   8.144   1.00 64.00  ? 279 TYR A OH    1 
ATOM   2182 N  N     . LEU A 1 280 ? -16.781 9.431   11.980  1.00 55.15  ? 280 LEU A N     1 
ATOM   2183 C  CA    . LEU A 1 280 ? -15.475 9.935   12.360  1.00 54.60  ? 280 LEU A CA    1 
ATOM   2184 C  C     . LEU A 1 280 ? -14.394 9.117   11.671  1.00 54.03  ? 280 LEU A C     1 
ATOM   2185 O  O     . LEU A 1 280 ? -14.639 8.016   11.170  1.00 55.65  ? 280 LEU A O     1 
ATOM   2186 C  CB    . LEU A 1 280 ? -15.278 9.885   13.879  1.00 55.08  ? 280 LEU A CB    1 
ATOM   2187 C  CG    . LEU A 1 280 ? -16.391 10.538  14.696  1.00 56.42  ? 280 LEU A CG    1 
ATOM   2188 C  CD1   . LEU A 1 280 ? -16.110 10.416  16.183  1.00 59.39  ? 280 LEU A CD1   1 
ATOM   2189 C  CD2   . LEU A 1 280 ? -16.556 11.993  14.296  1.00 55.63  ? 280 LEU A CD2   1 
ATOM   2190 N  N     . ALA A 1 281 ? -13.190 9.678   11.651  1.00 53.61  ? 281 ALA A N     1 
ATOM   2191 C  CA    . ALA A 1 281 ? -12.018 9.007   11.110  1.00 53.11  ? 281 ALA A CA    1 
ATOM   2192 C  C     . ALA A 1 281 ? -10.854 9.259   12.053  1.00 53.19  ? 281 ALA A C     1 
ATOM   2193 O  O     . ALA A 1 281 ? -10.657 10.391  12.506  1.00 53.40  ? 281 ALA A O     1 
ATOM   2194 C  CB    . ALA A 1 281 ? -11.685 9.509   9.701   1.00 52.68  ? 281 ALA A CB    1 
ATOM   2195 N  N     . ALA A 1 282 ? -10.096 8.208   12.356  1.00 53.16  ? 282 ALA A N     1 
ATOM   2196 C  CA    . ALA A 1 282 ? -8.967  8.309   13.268  1.00 53.43  ? 282 ALA A CA    1 
ATOM   2197 C  C     . ALA A 1 282 ? -7.724  7.760   12.588  1.00 53.00  ? 282 ALA A C     1 
ATOM   2198 O  O     . ALA A 1 282 ? -7.765  6.685   11.983  1.00 52.70  ? 282 ALA A O     1 
ATOM   2199 C  CB    . ALA A 1 282 ? -9.234  7.559   14.579  1.00 54.18  ? 282 ALA A CB    1 
ATOM   2200 N  N     . ALA A 1 283 ? -6.630  8.506   12.684  1.00 53.07  ? 283 ALA A N     1 
ATOM   2201 C  CA    . ALA A 1 283 ? -5.330  8.077   12.191  1.00 52.84  ? 283 ALA A CA    1 
ATOM   2202 C  C     . ALA A 1 283 ? -4.435  7.842   13.400  1.00 53.55  ? 283 ALA A C     1 
ATOM   2203 O  O     . ALA A 1 283 ? -4.008  8.794   14.061  1.00 54.13  ? 283 ALA A O     1 
ATOM   2204 C  CB    . ALA A 1 283 ? -4.725  9.110   11.241  1.00 52.63  ? 283 ALA A CB    1 
ATOM   2205 N  N     . PHE A 1 284 ? -4.179  6.573   13.701  1.00 53.66  ? 284 PHE A N     1 
ATOM   2206 C  CA    . PHE A 1 284 ? -3.231  6.192   14.728  1.00 54.46  ? 284 PHE A CA    1 
ATOM   2207 C  C     . PHE A 1 284 ? -2.115  5.371   14.101  1.00 55.79  ? 284 PHE A C     1 
ATOM   2208 O  O     . PHE A 1 284 ? -2.330  4.706   13.081  1.00 53.93  ? 284 PHE A O     1 
ATOM   2209 C  CB    . PHE A 1 284 ? -3.888  5.363   15.840  1.00 55.19  ? 284 PHE A CB    1 
ATOM   2210 C  CG    . PHE A 1 284 ? -5.103  6.002   16.449  1.00 55.51  ? 284 PHE A CG    1 
ATOM   2211 C  CD1   . PHE A 1 284 ? -5.266  7.378   16.444  1.00 55.46  ? 284 PHE A CD1   1 
ATOM   2212 C  CD2   . PHE A 1 284 ? -6.084  5.217   17.040  1.00 60.18  ? 284 PHE A CD2   1 
ATOM   2213 C  CE1   . PHE A 1 284 ? -6.385  7.959   17.008  1.00 55.79  ? 284 PHE A CE1   1 
ATOM   2214 C  CE2   . PHE A 1 284 ? -7.207  5.794   17.612  1.00 56.37  ? 284 PHE A CE2   1 
ATOM   2215 C  CZ    . PHE A 1 284 ? -7.357  7.165   17.595  1.00 56.22  ? 284 PHE A CZ    1 
ATOM   2216 N  N     . PRO A 1 285 ? -0.915  5.397   14.675  1.00 60.30  ? 285 PRO A N     1 
ATOM   2217 C  CA    . PRO A 1 285 ? 0.136   4.478   14.220  1.00 60.74  ? 285 PRO A CA    1 
ATOM   2218 C  C     . PRO A 1 285 ? -0.286  3.031   14.433  1.00 66.73  ? 285 PRO A C     1 
ATOM   2219 O  O     . PRO A 1 285 ? -1.251  2.727   15.138  1.00 67.96  ? 285 PRO A O     1 
ATOM   2220 C  CB    . PRO A 1 285 ? 1.343   4.852   15.089  1.00 60.21  ? 285 PRO A CB    1 
ATOM   2221 C  CG    . PRO A 1 285 ? 1.064   6.256   15.544  1.00 62.50  ? 285 PRO A CG    1 
ATOM   2222 C  CD    . PRO A 1 285 ? -0.428  6.336   15.700  1.00 59.18  ? 285 PRO A CD    1 
ATOM   2223 N  N     . SER A 1 286 ? 0.455   2.121   13.802  1.00 64.46  ? 286 SER A N     1 
ATOM   2224 C  CA    . SER A 1 286 ? 0.150   0.702   13.934  1.00 57.39  ? 286 SER A CA    1 
ATOM   2225 C  C     . SER A 1 286 ? 0.270   0.262   15.386  1.00 62.05  ? 286 SER A C     1 
ATOM   2226 O  O     . SER A 1 286 ? 1.144   0.724   16.125  1.00 61.80  ? 286 SER A O     1 
ATOM   2227 C  CB    . SER A 1 286 ? 1.083   -0.133  13.056  1.00 65.02  ? 286 SER A CB    1 
ATOM   2228 O  OG    . SER A 1 286 ? 0.841   0.091   11.676  1.00 66.96  ? 286 SER A OG    1 
ATOM   2229 N  N     . ALA A 1 287 ? -0.623  -0.642  15.794  1.00 66.02  ? 287 ALA A N     1 
ATOM   2230 C  CA    . ALA A 1 287 ? -0.648  -1.164  17.158  1.00 62.04  ? 287 ALA A CA    1 
ATOM   2231 C  C     . ALA A 1 287 ? -0.912  -0.062  18.177  1.00 63.57  ? 287 ALA A C     1 
ATOM   2232 O  O     . ALA A 1 287 ? -0.407  -0.111  19.301  1.00 70.19  ? 287 ALA A O     1 
ATOM   2233 C  CB    . ALA A 1 287 ? 0.653   -1.896  17.496  1.00 70.21  ? 287 ALA A CB    1 
ATOM   2234 N  N     . CYS A 1 288 ? -1.700  0.944   17.792  1.00 63.34  ? 288 CYS A N     1 
ATOM   2235 C  CA    . CYS A 1 288 ? -2.009  2.062   18.672  1.00 59.55  ? 288 CYS A CA    1 
ATOM   2236 C  C     . CYS A 1 288 ? -3.499  2.252   18.918  1.00 58.45  ? 288 CYS A C     1 
ATOM   2237 O  O     . CYS A 1 288 ? -3.882  3.243   19.550  1.00 59.08  ? 288 CYS A O     1 
ATOM   2238 C  CB    . CYS A 1 288 ? -1.409  3.359   18.119  1.00 63.71  ? 288 CYS A CB    1 
ATOM   2239 S  SG    . CYS A 1 288 ? 0.375   3.490   18.371  1.00 71.49  ? 288 CYS A SG    1 
ATOM   2240 N  N     . GLY A 1 289 ? -4.348  1.348   18.433  1.00 61.63  ? 289 GLY A N     1 
ATOM   2241 C  CA    . GLY A 1 289 ? -5.726  1.310   18.882  1.00 58.58  ? 289 GLY A CA    1 
ATOM   2242 C  C     . GLY A 1 289 ? -6.803  1.489   17.831  1.00 57.57  ? 289 GLY A C     1 
ATOM   2243 O  O     . GLY A 1 289 ? -7.986  1.561   18.176  1.00 58.00  ? 289 GLY A O     1 
ATOM   2244 N  N     . LYS A 1 290 ? -6.431  1.559   16.552  1.00 56.39  ? 290 LYS A N     1 
ATOM   2245 C  CA    . LYS A 1 290 ? -7.435  1.802   15.520  1.00 55.66  ? 290 LYS A CA    1 
ATOM   2246 C  C     . LYS A 1 290 ? -8.513  0.723   15.534  1.00 64.12  ? 290 LYS A C     1 
ATOM   2247 O  O     . LYS A 1 290 ? -9.712  1.027   15.572  1.00 56.41  ? 290 LYS A O     1 
ATOM   2248 C  CB    . LYS A 1 290 ? -6.770  1.896   14.145  1.00 54.50  ? 290 LYS A CB    1 
ATOM   2249 C  CG    . LYS A 1 290 ? -5.848  3.101   13.985  1.00 55.19  ? 290 LYS A CG    1 
ATOM   2250 C  CD    . LYS A 1 290 ? -5.540  3.392   12.520  1.00 55.60  ? 290 LYS A CD    1 
ATOM   2251 C  CE    . LYS A 1 290 ? -4.863  2.207   11.837  1.00 55.95  ? 290 LYS A CE    1 
ATOM   2252 N  NZ    . LYS A 1 290 ? -3.563  1.857   12.474  1.00 53.20  ? 290 LYS A NZ    1 
ATOM   2253 N  N     . THR A 1 291 ? -8.104  -0.549  15.519  1.00 62.44  ? 291 THR A N     1 
ATOM   2254 C  CA    . THR A 1 291 ? -9.073  -1.639  15.446  1.00 57.37  ? 291 THR A CA    1 
ATOM   2255 C  C     . THR A 1 291 ? -9.952  -1.688  16.692  1.00 63.75  ? 291 THR A C     1 
ATOM   2256 O  O     . THR A 1 291 ? -11.180 -1.803  16.593  1.00 62.53  ? 291 THR A O     1 
ATOM   2257 C  CB    . THR A 1 291 ? -8.353  -2.972  15.241  1.00 60.41  ? 291 THR A CB    1 
ATOM   2258 O  OG1   . THR A 1 291 ? -7.725  -2.985  13.954  1.00 64.29  ? 291 THR A OG1   1 
ATOM   2259 C  CG2   . THR A 1 291 ? -9.343  -4.127  15.324  1.00 64.64  ? 291 THR A CG2   1 
ATOM   2260 N  N     . ASN A 1 292 ? -9.343  -1.612  17.878  1.00 67.34  ? 292 ASN A N     1 
ATOM   2261 C  CA    . ASN A 1 292 ? -10.136 -1.616  19.102  1.00 63.86  ? 292 ASN A CA    1 
ATOM   2262 C  C     . ASN A 1 292 ? -11.105 -0.441  19.151  1.00 63.06  ? 292 ASN A C     1 
ATOM   2263 O  O     . ASN A 1 292 ? -12.154 -0.533  19.797  1.00 65.78  ? 292 ASN A O     1 
ATOM   2264 C  CB    . ASN A 1 292 ? -9.219  -1.610  20.326  1.00 66.24  ? 292 ASN A CB    1 
ATOM   2265 C  CG    . ASN A 1 292 ? -8.526  -2.947  20.542  1.00 83.46  ? 292 ASN A CG    1 
ATOM   2266 O  OD1   . ASN A 1 292 ? -9.028  -3.811  21.263  1.00 82.45  ? 292 ASN A OD1   1 
ATOM   2267 N  ND2   . ASN A 1 292 ? -7.370  -3.124  19.910  1.00 68.21  ? 292 ASN A ND2   1 
ATOM   2268 N  N     . LEU A 1 293 ? -10.779 0.664   18.474  1.00 66.19  ? 293 LEU A N     1 
ATOM   2269 C  CA    . LEU A 1 293 ? -11.672 1.820   18.454  1.00 62.18  ? 293 LEU A CA    1 
ATOM   2270 C  C     . LEU A 1 293 ? -12.763 1.678   17.395  1.00 60.96  ? 293 LEU A C     1 
ATOM   2271 O  O     . LEU A 1 293 ? -13.927 2.007   17.654  1.00 64.11  ? 293 LEU A O     1 
ATOM   2272 C  CB    . LEU A 1 293 ? -10.873 3.104   18.219  1.00 58.01  ? 293 LEU A CB    1 
ATOM   2273 C  CG    . LEU A 1 293 ? -11.706 4.387   18.141  1.00 57.70  ? 293 LEU A CG    1 
ATOM   2274 C  CD1   . LEU A 1 293 ? -12.248 4.753   19.511  1.00 58.88  ? 293 LEU A CD1   1 
ATOM   2275 C  CD2   . LEU A 1 293 ? -10.905 5.538   17.553  1.00 56.73  ? 293 LEU A CD2   1 
ATOM   2276 N  N     . ALA A 1 294 ? -12.412 1.193   16.201  1.00 57.71  ? 294 ALA A N     1 
ATOM   2277 C  CA    . ALA A 1 294 ? -13.401 1.053   15.137  1.00 57.47  ? 294 ALA A CA    1 
ATOM   2278 C  C     . ALA A 1 294 ? -14.438 -0.023  15.442  1.00 65.92  ? 294 ALA A C     1 
ATOM   2279 O  O     . ALA A 1 294 ? -15.527 0.003   14.859  1.00 67.27  ? 294 ALA A O     1 
ATOM   2280 C  CB    . ALA A 1 294 ? -12.704 0.752   13.809  1.00 56.46  ? 294 ALA A CB    1 
ATOM   2281 N  N     . MET A 1 295 ? -14.124 -0.966  16.332  1.00 63.06  ? 295 MET A N     1 
ATOM   2282 C  CA    . MET A 1 295 ? -15.057 -2.002  16.762  1.00 67.51  ? 295 MET A CA    1 
ATOM   2283 C  C     . MET A 1 295 ? -15.388 -1.863  18.241  1.00 67.34  ? 295 MET A C     1 
ATOM   2284 O  O     . MET A 1 295 ? -15.704 -2.848  18.909  1.00 64.23  ? 295 MET A O     1 
ATOM   2285 C  CB    . MET A 1 295 ? -14.494 -3.396  16.496  1.00 68.51  ? 295 MET A CB    1 
ATOM   2286 C  CG    . MET A 1 295 ? -14.128 -3.683  15.065  1.00 65.07  ? 295 MET A CG    1 
ATOM   2287 S  SD    . MET A 1 295 ? -13.508 -5.368  14.937  1.00 66.79  ? 295 MET A SD    1 
ATOM   2288 C  CE    . MET A 1 295 ? -12.946 -5.376  13.233  1.00 64.51  ? 295 MET A CE    1 
ATOM   2289 N  N     A MET A 1 296 ? -15.316 -0.644  18.767  0.38 65.91  ? 296 MET A N     1 
ATOM   2290 N  N     B MET A 1 296 ? -15.321 -0.640  18.758  0.62 66.25  ? 296 MET A N     1 
ATOM   2291 C  CA    A MET A 1 296 ? -15.464 -0.447  20.202  0.38 66.75  ? 296 MET A CA    1 
ATOM   2292 C  CA    B MET A 1 296 ? -15.518 -0.409  20.181  0.62 66.86  ? 296 MET A CA    1 
ATOM   2293 C  C     A MET A 1 296 ? -16.847 -0.876  20.677  0.38 65.05  ? 296 MET A C     1 
ATOM   2294 C  C     B MET A 1 296 ? -16.869 -0.935  20.650  0.62 65.08  ? 296 MET A C     1 
ATOM   2295 O  O     A MET A 1 296 ? -17.851 -0.688  19.985  0.38 64.91  ? 296 MET A O     1 
ATOM   2296 O  O     B MET A 1 296 ? -17.869 -0.869  19.931  0.62 65.88  ? 296 MET A O     1 
ATOM   2297 C  CB    A MET A 1 296 ? -15.220 1.018   20.562  0.38 65.89  ? 296 MET A CB    1 
ATOM   2298 C  CB    B MET A 1 296 ? -15.410 1.084   20.484  0.62 66.43  ? 296 MET A CB    1 
ATOM   2299 C  CG    A MET A 1 296 ? -15.302 1.305   22.049  0.38 65.71  ? 296 MET A CG    1 
ATOM   2300 C  CG    B MET A 1 296 ? -16.060 1.497   21.786  0.62 66.07  ? 296 MET A CG    1 
ATOM   2301 S  SD    A MET A 1 296 ? -15.243 3.069   22.401  0.38 63.39  ? 296 MET A SD    1 
ATOM   2302 S  SD    B MET A 1 296 ? -16.231 3.282   21.899  0.62 63.37  ? 296 MET A SD    1 
ATOM   2303 C  CE    A MET A 1 296 ? -16.629 3.639   21.422  0.38 64.98  ? 296 MET A CE    1 
ATOM   2304 C  CE    B MET A 1 296 ? -14.520 3.792   21.767  0.62 62.77  ? 296 MET A CE    1 
ATOM   2305 N  N     . ASN A 1 297 ? -16.888 -1.466  21.873  1.00 66.76  ? 297 ASN A N     1 
ATOM   2306 C  CA    . ASN A 1 297 ? -18.131 -1.787  22.555  1.00 69.71  ? 297 ASN A CA    1 
ATOM   2307 C  C     . ASN A 1 297 ? -18.352 -0.693  23.591  1.00 68.90  ? 297 ASN A C     1 
ATOM   2308 O  O     . ASN A 1 297 ? -17.760 -0.749  24.678  1.00 69.86  ? 297 ASN A O     1 
ATOM   2309 C  CB    . ASN A 1 297 ? -18.061 -3.164  23.222  1.00 74.20  ? 297 ASN A CB    1 
ATOM   2310 C  CG    . ASN A 1 297 ? -19.364 -3.555  23.890  1.00 83.49  ? 297 ASN A CG    1 
ATOM   2311 O  OD1   . ASN A 1 297 ? -20.447 -3.260  23.386  1.00 88.95  ? 297 ASN A OD1   1 
ATOM   2312 N  ND2   . ASN A 1 297 ? -19.266 -4.217  25.038  1.00 89.62  ? 297 ASN A ND2   1 
ATOM   2313 N  N     . PRO A 1 298 ? -19.157 0.326   23.304  1.00 68.26  ? 298 PRO A N     1 
ATOM   2314 C  CA    . PRO A 1 298 ? -19.214 1.493   24.192  1.00 70.39  ? 298 PRO A CA    1 
ATOM   2315 C  C     . PRO A 1 298 ? -19.899 1.183   25.513  1.00 70.55  ? 298 PRO A C     1 
ATOM   2316 O  O     . PRO A 1 298 ? -20.774 0.319   25.603  1.00 75.52  ? 298 PRO A O     1 
ATOM   2317 C  CB    . PRO A 1 298 ? -20.014 2.518   23.380  1.00 69.79  ? 298 PRO A CB    1 
ATOM   2318 C  CG    . PRO A 1 298 ? -20.853 1.693   22.462  1.00 74.85  ? 298 PRO A CG    1 
ATOM   2319 C  CD    . PRO A 1 298 ? -20.035 0.472   22.130  1.00 69.73  ? 298 PRO A CD    1 
ATOM   2320 N  N     . THR A 1 299 ? -19.486 1.916   26.549  1.00 80.96  ? 299 THR A N     1 
ATOM   2321 C  CA    . THR A 1 299 ? -20.044 1.775   27.887  1.00 73.15  ? 299 THR A CA    1 
ATOM   2322 C  C     . THR A 1 299 ? -21.132 2.795   28.192  1.00 74.94  ? 299 THR A C     1 
ATOM   2323 O  O     . THR A 1 299 ? -21.818 2.658   29.210  1.00 82.67  ? 299 THR A O     1 
ATOM   2324 C  CB    . THR A 1 299 ? -18.936 1.895   28.943  1.00 73.88  ? 299 THR A CB    1 
ATOM   2325 O  OG1   . THR A 1 299 ? -18.358 3.204   28.885  1.00 72.52  ? 299 THR A OG1   1 
ATOM   2326 C  CG2   . THR A 1 299 ? -17.851 0.862   28.697  1.00 73.84  ? 299 THR A CG2   1 
ATOM   2327 N  N     . LEU A 1 300 ? -21.300 3.809   27.355  1.00 74.98  ? 300 LEU A N     1 
ATOM   2328 C  CA    . LEU A 1 300 ? -22.365 4.781   27.574  1.00 71.83  ? 300 LEU A CA    1 
ATOM   2329 C  C     . LEU A 1 300 ? -23.671 4.250   26.994  1.00 76.09  ? 300 LEU A C     1 
ATOM   2330 O  O     . LEU A 1 300 ? -23.719 3.900   25.811  1.00 78.07  ? 300 LEU A O     1 
ATOM   2331 C  CB    . LEU A 1 300 ? -22.016 6.122   26.934  1.00 69.93  ? 300 LEU A CB    1 
ATOM   2332 C  CG    . LEU A 1 300 ? -20.752 6.831   27.428  1.00 70.60  ? 300 LEU A CG    1 
ATOM   2333 C  CD1   . LEU A 1 300 ? -20.503 8.109   26.633  1.00 67.65  ? 300 LEU A CD1   1 
ATOM   2334 C  CD2   . LEU A 1 300 ? -20.846 7.129   28.917  1.00 71.13  ? 300 LEU A CD2   1 
ATOM   2335 N  N     . PRO A 1 301 ? -24.737 4.170   27.785  1.00 74.21  ? 301 PRO A N     1 
ATOM   2336 C  CA    . PRO A 1 301 ? -26.007 3.666   27.253  1.00 75.02  ? 301 PRO A CA    1 
ATOM   2337 C  C     . PRO A 1 301 ? -26.592 4.615   26.221  1.00 77.11  ? 301 PRO A C     1 
ATOM   2338 O  O     . PRO A 1 301 ? -26.375 5.829   26.259  1.00 75.23  ? 301 PRO A O     1 
ATOM   2339 C  CB    . PRO A 1 301 ? -26.900 3.573   28.495  1.00 77.36  ? 301 PRO A CB    1 
ATOM   2340 C  CG    . PRO A 1 301 ? -26.321 4.567   29.446  1.00 77.18  ? 301 PRO A CG    1 
ATOM   2341 C  CD    . PRO A 1 301 ? -24.838 4.551   29.203  1.00 77.25  ? 301 PRO A CD    1 
ATOM   2342 N  N     . GLY A 1 302 ? -27.348 4.042   25.288  1.00 73.74  ? 302 GLY A N     1 
ATOM   2343 C  CA    . GLY A 1 302 ? -27.926 4.818   24.212  1.00 73.21  ? 302 GLY A CA    1 
ATOM   2344 C  C     . GLY A 1 302 ? -26.955 5.231   23.130  1.00 75.18  ? 302 GLY A C     1 
ATOM   2345 O  O     . GLY A 1 302 ? -27.318 6.041   22.269  1.00 74.78  ? 302 GLY A O     1 
ATOM   2346 N  N     . TRP A 1 303 ? -25.733 4.710   23.149  1.00 76.28  ? 303 TRP A N     1 
ATOM   2347 C  CA    . TRP A 1 303 ? -24.730 4.998   22.135  1.00 72.95  ? 303 TRP A CA    1 
ATOM   2348 C  C     . TRP A 1 303 ? -24.433 3.739   21.336  1.00 74.91  ? 303 TRP A C     1 
ATOM   2349 O  O     . TRP A 1 303 ? -24.331 2.645   21.900  1.00 73.43  ? 303 TRP A O     1 
ATOM   2350 C  CB    . TRP A 1 303 ? -23.443 5.531   22.769  1.00 69.07  ? 303 TRP A CB    1 
ATOM   2351 C  CG    . TRP A 1 303 ? -23.556 6.940   23.255  1.00 69.13  ? 303 TRP A CG    1 
ATOM   2352 C  CD1   . TRP A 1 303 ? -23.949 7.354   24.494  1.00 73.39  ? 303 TRP A CD1   1 
ATOM   2353 C  CD2   . TRP A 1 303 ? -23.272 8.127   22.506  1.00 68.39  ? 303 TRP A CD2   1 
ATOM   2354 N  NE1   . TRP A 1 303 ? -23.928 8.727   24.563  1.00 68.17  ? 303 TRP A NE1   1 
ATOM   2355 C  CE2   . TRP A 1 303 ? -23.515 9.225   23.355  1.00 67.67  ? 303 TRP A CE2   1 
ATOM   2356 C  CE3   . TRP A 1 303 ? -22.836 8.368   21.199  1.00 63.65  ? 303 TRP A CE3   1 
ATOM   2357 C  CZ2   . TRP A 1 303 ? -23.336 10.543  22.941  1.00 66.68  ? 303 TRP A CZ2   1 
ATOM   2358 C  CZ3   . TRP A 1 303 ? -22.658 9.677   20.789  1.00 64.70  ? 303 TRP A CZ3   1 
ATOM   2359 C  CH2   . TRP A 1 303 ? -22.908 10.748  21.656  1.00 64.73  ? 303 TRP A CH2   1 
ATOM   2360 N  N     . LYS A 1 304 ? -24.296 3.896   20.022  1.00 70.36  ? 304 LYS A N     1 
ATOM   2361 C  CA    . LYS A 1 304 ? -24.023 2.782   19.127  1.00 66.37  ? 304 LYS A CA    1 
ATOM   2362 C  C     . LYS A 1 304 ? -22.851 3.136   18.225  1.00 71.97  ? 304 LYS A C     1 
ATOM   2363 O  O     . LYS A 1 304 ? -22.870 4.172   17.553  1.00 68.65  ? 304 LYS A O     1 
ATOM   2364 C  CB    . LYS A 1 304 ? -25.253 2.431   18.282  1.00 67.21  ? 304 LYS A CB    1 
ATOM   2365 C  CG    . LYS A 1 304 ? -25.042 1.247   17.352  1.00 77.27  ? 304 LYS A CG    1 
ATOM   2366 C  CD    . LYS A 1 304 ? -26.318 0.884   16.607  1.00 82.63  ? 304 LYS A CD    1 
ATOM   2367 C  CE    . LYS A 1 304 ? -26.103 -0.326  15.707  1.00 87.66  ? 304 LYS A CE    1 
ATOM   2368 N  NZ    . LYS A 1 304 ? -27.343 -0.716  14.978  1.00 86.54  ? 304 LYS A NZ    1 
ATOM   2369 N  N     . VAL A 1 305 ? -21.837 2.278   18.215  1.00 71.95  ? 305 VAL A N     1 
ATOM   2370 C  CA    . VAL A 1 305 ? -20.678 2.429   17.346  1.00 68.65  ? 305 VAL A CA    1 
ATOM   2371 C  C     . VAL A 1 305 ? -20.748 1.354   16.274  1.00 69.63  ? 305 VAL A C     1 
ATOM   2372 O  O     . VAL A 1 305 ? -21.000 0.181   16.575  1.00 75.70  ? 305 VAL A O     1 
ATOM   2373 C  CB    . VAL A 1 305 ? -19.359 2.334   18.131  1.00 74.87  ? 305 VAL A CB    1 
ATOM   2374 C  CG1   . VAL A 1 305 ? -18.180 2.248   17.168  1.00 68.17  ? 305 VAL A CG1   1 
ATOM   2375 C  CG2   . VAL A 1 305 ? -19.212 3.527   19.067  1.00 65.47  ? 305 VAL A CG2   1 
ATOM   2376 N  N     . GLU A 1 306 ? -20.532 1.757   15.026  1.00 70.66  ? 306 GLU A N     1 
ATOM   2377 C  CA    . GLU A 1 306 ? -20.505 0.843   13.897  1.00 67.68  ? 306 GLU A CA    1 
ATOM   2378 C  C     . GLU A 1 306 ? -19.206 1.047   13.133  1.00 61.63  ? 306 GLU A C     1 
ATOM   2379 O  O     . GLU A 1 306 ? -18.635 2.141   13.127  1.00 61.88  ? 306 GLU A O     1 
ATOM   2380 C  CB    . GLU A 1 306 ? -21.720 1.050   12.983  1.00 67.70  ? 306 GLU A CB    1 
ATOM   2381 C  CG    . GLU A 1 306 ? -23.041 0.669   13.642  1.00 67.70  ? 306 GLU A CG    1 
ATOM   2382 C  CD    . GLU A 1 306 ? -24.243 1.302   12.969  1.00 72.63  ? 306 GLU A CD    1 
ATOM   2383 O  OE1   . GLU A 1 306 ? -24.262 2.543   12.824  1.00 77.78  ? 306 GLU A OE1   1 
ATOM   2384 O  OE2   . GLU A 1 306 ? -25.169 0.560   12.583  1.00 77.72  ? 306 GLU A OE2   1 
ATOM   2385 N  N     . CYS A 1 307 ? -18.738 -0.020  12.497  1.00 60.03  ? 307 CYS A N     1 
ATOM   2386 C  CA    . CYS A 1 307 ? -17.404 -0.067  11.915  1.00 60.99  ? 307 CYS A CA    1 
ATOM   2387 C  C     . CYS A 1 307 ? -17.501 -0.058  10.396  1.00 63.18  ? 307 CYS A C     1 
ATOM   2388 O  O     . CYS A 1 307 ? -18.133 -0.941  9.806   1.00 59.15  ? 307 CYS A O     1 
ATOM   2389 C  CB    . CYS A 1 307 ? -16.654 -1.310  12.391  1.00 67.82  ? 307 CYS A CB    1 
ATOM   2390 S  SG    . CYS A 1 307 ? -15.032 -1.509  11.644  1.00 57.85  ? 307 CYS A SG    1 
ATOM   2391 N  N     . VAL A 1 308 ? -16.862 0.930   9.771   1.00 61.98  ? 308 VAL A N     1 
ATOM   2392 C  CA    . VAL A 1 308 ? -16.788 1.015   8.317   1.00 58.52  ? 308 VAL A CA    1 
ATOM   2393 C  C     . VAL A 1 308 ? -15.444 0.468   7.857   1.00 55.85  ? 308 VAL A C     1 
ATOM   2394 O  O     . VAL A 1 308 ? -15.343 -0.139  6.786   1.00 56.69  ? 308 VAL A O     1 
ATOM   2395 C  CB    . VAL A 1 308 ? -16.994 2.460   7.828   1.00 62.92  ? 308 VAL A CB    1 
ATOM   2396 C  CG1   . VAL A 1 308 ? -16.854 2.535   6.309   1.00 61.38  ? 308 VAL A CG1   1 
ATOM   2397 C  CG2   . VAL A 1 308 ? -18.351 2.985   8.278   1.00 58.28  ? 308 VAL A CG2   1 
ATOM   2398 N  N     . GLY A 1 309 ? -14.409 0.678   8.665   1.00 56.14  ? 309 GLY A N     1 
ATOM   2399 C  CA    . GLY A 1 309 ? -13.071 0.206   8.349   1.00 54.57  ? 309 GLY A CA    1 
ATOM   2400 C  C     . GLY A 1 309 ? -12.141 0.480   9.508   1.00 54.30  ? 309 GLY A C     1 
ATOM   2401 O  O     . GLY A 1 309 ? -12.461 1.246   10.422  1.00 60.66  ? 309 GLY A O     1 
ATOM   2402 N  N     . ASP A 1 310 ? -10.962 -0.148  9.454   1.00 53.96  ? 310 ASP A N     1 
ATOM   2403 C  CA    . ASP A 1 310 ? -10.031 -0.091  10.574  1.00 53.99  ? 310 ASP A CA    1 
ATOM   2404 C  C     . ASP A 1 310 ? -8.596  0.251   10.180  1.00 55.50  ? 310 ASP A C     1 
ATOM   2405 O  O     . ASP A 1 310 ? -7.699  0.129   11.023  1.00 57.24  ? 310 ASP A O     1 
ATOM   2406 C  CB    . ASP A 1 310 ? -10.035 -1.424  11.334  1.00 54.94  ? 310 ASP A CB    1 
ATOM   2407 C  CG    . ASP A 1 310 ? -9.174  -2.482  10.662  1.00 61.44  ? 310 ASP A CG    1 
ATOM   2408 O  OD1   . ASP A 1 310 ? -9.185  -2.570  9.415   1.00 54.21  ? 310 ASP A OD1   1 
ATOM   2409 O  OD2   . ASP A 1 310 ? -8.471  -3.218  11.385  1.00 62.90  ? 310 ASP A OD2   1 
ATOM   2410 N  N     . ASP A 1 311 ? -8.337  0.680   8.943   1.00 58.24  ? 311 ASP A N     1 
ATOM   2411 C  CA    . ASP A 1 311 ? -6.940  0.866   8.562   1.00 52.33  ? 311 ASP A CA    1 
ATOM   2412 C  C     . ASP A 1 311 ? -6.720  1.853   7.421   1.00 51.28  ? 311 ASP A C     1 
ATOM   2413 O  O     . ASP A 1 311 ? -5.759  2.630   7.448   1.00 50.99  ? 311 ASP A O     1 
ATOM   2414 C  CB    . ASP A 1 311 ? -6.326  -0.485  8.191   1.00 51.94  ? 311 ASP A CB    1 
ATOM   2415 C  CG    . ASP A 1 311 ? -4.824  -0.413  8.031   1.00 54.45  ? 311 ASP A CG    1 
ATOM   2416 O  OD1   . ASP A 1 311 ? -4.143  0.027   8.979   1.00 51.71  ? 311 ASP A OD1   1 
ATOM   2417 O  OD2   . ASP A 1 311 ? -4.321  -0.799  6.958   1.00 57.97  ? 311 ASP A OD2   1 
ATOM   2418 N  N     . ILE A 1 312 ? -7.578  1.825   6.407   1.00 51.27  ? 312 ILE A N     1 
ATOM   2419 C  CA    . ILE A 1 312 ? -7.359  2.592   5.189   1.00 50.91  ? 312 ILE A CA    1 
ATOM   2420 C  C     . ILE A 1 312 ? -8.630  3.355   4.854   1.00 51.19  ? 312 ILE A C     1 
ATOM   2421 O  O     . ILE A 1 312 ? -9.727  2.786   4.869   1.00 51.66  ? 312 ILE A O     1 
ATOM   2422 C  CB    . ILE A 1 312 ? -6.936  1.689   4.014   1.00 54.14  ? 312 ILE A CB    1 
ATOM   2423 C  CG1   . ILE A 1 312 ? -5.561  1.078   4.294   1.00 50.51  ? 312 ILE A CG1   1 
ATOM   2424 C  CG2   . ILE A 1 312 ? -6.911  2.476   2.707   1.00 55.83  ? 312 ILE A CG2   1 
ATOM   2425 C  CD1   . ILE A 1 312 ? -5.071  0.157   3.212   1.00 60.72  ? 312 ILE A CD1   1 
ATOM   2426 N  N     . ALA A 1 313 ? -8.479  4.641   4.553   1.00 54.63  ? 313 ALA A N     1 
ATOM   2427 C  CA    . ALA A 1 313 ? -9.593  5.500   4.186   1.00 51.41  ? 313 ALA A CA    1 
ATOM   2428 C  C     . ALA A 1 313 ? -9.240  6.250   2.912   1.00 51.41  ? 313 ALA A C     1 
ATOM   2429 O  O     . ALA A 1 313 ? -8.159  6.838   2.813   1.00 51.18  ? 313 ALA A O     1 
ATOM   2430 C  CB    . ALA A 1 313 ? -9.930  6.487   5.307   1.00 51.53  ? 313 ALA A CB    1 
ATOM   2431 N  N     . TRP A 1 314 ? -10.147 6.214   1.943   1.00 53.19  ? 314 TRP A N     1 
ATOM   2432 C  CA    . TRP A 1 314 ? -10.037 6.994   0.718   1.00 57.40  ? 314 TRP A CA    1 
ATOM   2433 C  C     . TRP A 1 314 ? -11.125 8.057   0.744   1.00 55.06  ? 314 TRP A C     1 
ATOM   2434 O  O     . TRP A 1 314 ? -12.316 7.729   0.771   1.00 60.99  ? 314 TRP A O     1 
ATOM   2435 C  CB    . TRP A 1 314 ? -10.167 6.104   -0.520  1.00 53.11  ? 314 TRP A CB    1 
ATOM   2436 C  CG    . TRP A 1 314 ? -8.973  5.220   -0.762  1.00 52.02  ? 314 TRP A CG    1 
ATOM   2437 C  CD1   . TRP A 1 314 ? -7.876  5.083   0.039   1.00 56.17  ? 314 TRP A CD1   1 
ATOM   2438 C  CD2   . TRP A 1 314 ? -8.757  4.358   -1.886  1.00 52.26  ? 314 TRP A CD2   1 
ATOM   2439 N  NE1   . TRP A 1 314 ? -6.992  4.187   -0.516  1.00 54.20  ? 314 TRP A NE1   1 
ATOM   2440 C  CE2   . TRP A 1 314 ? -7.510  3.729   -1.698  1.00 51.67  ? 314 TRP A CE2   1 
ATOM   2441 C  CE3   . TRP A 1 314 ? -9.497  4.057   -3.031  1.00 55.02  ? 314 TRP A CE3   1 
ATOM   2442 C  CZ2   . TRP A 1 314 ? -6.990  2.818   -2.611  1.00 52.62  ? 314 TRP A CZ2   1 
ATOM   2443 C  CZ3   . TRP A 1 314 ? -8.979  3.151   -3.938  1.00 56.11  ? 314 TRP A CZ3   1 
ATOM   2444 C  CH2   . TRP A 1 314 ? -7.738  2.542   -3.723  1.00 57.98  ? 314 TRP A CH2   1 
ATOM   2445 N  N     . MET A 1 315 ? -10.718 9.325   0.736   1.00 61.48  ? 315 MET A N     1 
ATOM   2446 C  CA    . MET A 1 315 ? -11.630 10.430  0.987   1.00 65.11  ? 315 MET A CA    1 
ATOM   2447 C  C     . MET A 1 315 ? -11.558 11.456  -0.134  1.00 65.69  ? 315 MET A C     1 
ATOM   2448 O  O     . MET A 1 315 ? -10.540 11.588  -0.820  1.00 61.83  ? 315 MET A O     1 
ATOM   2449 C  CB    . MET A 1 315 ? -11.324 11.100  2.332   1.00 58.69  ? 315 MET A CB    1 
ATOM   2450 C  CG    . MET A 1 315 ? -11.333 10.129  3.505   1.00 60.63  ? 315 MET A CG    1 
ATOM   2451 S  SD    . MET A 1 315 ? -11.048 10.921  5.098   1.00 65.85  ? 315 MET A SD    1 
ATOM   2452 C  CE    . MET A 1 315 ? -9.535  11.818  4.768   1.00 58.99  ? 315 MET A CE    1 
ATOM   2453 N  N     . LYS A 1 316 ? -12.655 12.189  -0.302  1.00 68.37  ? 316 LYS A N     1 
ATOM   2454 C  CA    . LYS A 1 316 ? -12.771 13.196  -1.345  1.00 71.34  ? 316 LYS A CA    1 
ATOM   2455 C  C     . LYS A 1 316 ? -14.032 14.008  -1.100  1.00 72.97  ? 316 LYS A C     1 
ATOM   2456 O  O     . LYS A 1 316 ? -15.068 13.450  -0.732  1.00 76.01  ? 316 LYS A O     1 
ATOM   2457 C  CB    . LYS A 1 316 ? -12.814 12.550  -2.736  1.00 71.29  ? 316 LYS A CB    1 
ATOM   2458 C  CG    . LYS A 1 316 ? -13.062 13.526  -3.872  1.00 76.66  ? 316 LYS A CG    1 
ATOM   2459 C  CD    . LYS A 1 316 ? -12.926 12.844  -5.225  1.00 82.23  ? 316 LYS A CD    1 
ATOM   2460 C  CE    . LYS A 1 316 ? -13.905 11.691  -5.363  1.00 82.67  ? 316 LYS A CE    1 
ATOM   2461 N  NZ    . LYS A 1 316 ? -15.314 12.139  -5.190  1.00 77.87  ? 316 LYS A NZ    1 
ATOM   2462 N  N     . PHE A 1 317 ? -13.935 15.320  -1.294  1.00 78.99  ? 317 PHE A N     1 
ATOM   2463 C  CA    . PHE A 1 317 ? -15.108 16.173  -1.177  1.00 76.34  ? 317 PHE A CA    1 
ATOM   2464 C  C     . PHE A 1 317 ? -16.050 15.933  -2.347  1.00 80.84  ? 317 PHE A C     1 
ATOM   2465 O  O     . PHE A 1 317 ? -15.622 15.847  -3.502  1.00 83.22  ? 317 PHE A O     1 
ATOM   2466 C  CB    . PHE A 1 317 ? -14.699 17.644  -1.128  1.00 74.98  ? 317 PHE A CB    1 
ATOM   2467 C  CG    . PHE A 1 317 ? -13.958 18.025  0.118   1.00 77.87  ? 317 PHE A CG    1 
ATOM   2468 C  CD1   . PHE A 1 317 ? -14.645 18.355  1.274   1.00 80.51  ? 317 PHE A CD1   1 
ATOM   2469 C  CD2   . PHE A 1 317 ? -12.575 18.055  0.134   1.00 75.18  ? 317 PHE A CD2   1 
ATOM   2470 C  CE1   . PHE A 1 317 ? -13.967 18.707  2.426   1.00 75.36  ? 317 PHE A CE1   1 
ATOM   2471 C  CE2   . PHE A 1 317 ? -11.891 18.406  1.280   1.00 75.25  ? 317 PHE A CE2   1 
ATOM   2472 C  CZ    . PHE A 1 317 ? -12.589 18.733  2.429   1.00 74.83  ? 317 PHE A CZ    1 
ATOM   2473 N  N     . ASP A 1 318 ? -17.339 15.814  -2.046  1.00 80.95  ? 318 ASP A N     1 
ATOM   2474 C  CA    . ASP A 1 318 ? -18.338 15.594  -3.078  1.00 83.61  ? 318 ASP A CA    1 
ATOM   2475 C  C     . ASP A 1 318 ? -18.857 16.942  -3.576  1.00 85.34  ? 318 ASP A C     1 
ATOM   2476 O  O     . ASP A 1 318 ? -18.368 18.006  -3.185  1.00 83.95  ? 318 ASP A O     1 
ATOM   2477 C  CB    . ASP A 1 318 ? -19.459 14.691  -2.559  1.00 88.84  ? 318 ASP A CB    1 
ATOM   2478 C  CG    . ASP A 1 318 ? -20.273 15.330  -1.443  1.00 86.94  ? 318 ASP A CG    1 
ATOM   2479 O  OD1   . ASP A 1 318 ? -20.066 16.525  -1.144  1.00 80.51  ? 318 ASP A OD1   1 
ATOM   2480 O  OD2   . ASP A 1 318 ? -21.126 14.627  -0.860  1.00 83.06  ? 318 ASP A OD2   1 
ATOM   2481 N  N     . ALA A 1 319 ? -19.863 16.910  -4.453  1.00 93.60  ? 319 ALA A N     1 
ATOM   2482 C  CA    . ALA A 1 319 ? -20.392 18.150  -5.010  1.00 95.49  ? 319 ALA A CA    1 
ATOM   2483 C  C     . ALA A 1 319 ? -20.939 19.058  -3.917  1.00 97.03  ? 319 ALA A C     1 
ATOM   2484 O  O     . ALA A 1 319 ? -20.759 20.280  -3.967  1.00 96.74  ? 319 ALA A O     1 
ATOM   2485 C  CB    . ALA A 1 319 ? -21.474 17.841  -6.045  1.00 96.55  ? 319 ALA A CB    1 
ATOM   2486 N  N     . GLN A 1 320 ? -21.603 18.480  -2.917  1.00 94.46  ? 320 GLN A N     1 
ATOM   2487 C  CA    . GLN A 1 320 ? -22.213 19.252  -1.842  1.00 86.19  ? 320 GLN A CA    1 
ATOM   2488 C  C     . GLN A 1 320 ? -21.200 19.776  -0.832  1.00 83.87  ? 320 GLN A C     1 
ATOM   2489 O  O     . GLN A 1 320 ? -21.602 20.405  0.153   1.00 84.19  ? 320 GLN A O     1 
ATOM   2490 C  CB    . GLN A 1 320 ? -23.265 18.404  -1.123  1.00 85.86  ? 320 GLN A CB    1 
ATOM   2491 C  CG    . GLN A 1 320 ? -24.211 17.670  -2.063  1.00 88.66  ? 320 GLN A CG    1 
ATOM   2492 C  CD    . GLN A 1 320 ? -24.968 18.609  -2.984  1.00 87.43  ? 320 GLN A CD    1 
ATOM   2493 O  OE1   . GLN A 1 320 ? -25.357 19.708  -2.588  1.00 91.08  ? 320 GLN A OE1   1 
ATOM   2494 N  NE2   . GLN A 1 320 ? -25.178 18.180  -4.224  1.00 89.00  ? 320 GLN A NE2   1 
ATOM   2495 N  N     . GLY A 1 321 ? -19.907 19.532  -1.043  1.00 82.97  ? 321 GLY A N     1 
ATOM   2496 C  CA    . GLY A 1 321 ? -18.874 20.039  -0.167  1.00 81.45  ? 321 GLY A CA    1 
ATOM   2497 C  C     . GLY A 1 321 ? -18.534 19.164  1.020   1.00 81.05  ? 321 GLY A C     1 
ATOM   2498 O  O     . GLY A 1 321 ? -17.695 19.563  1.838   1.00 80.90  ? 321 GLY A O     1 
ATOM   2499 N  N     . ASN A 1 322 ? -19.152 17.993  1.145   1.00 78.01  ? 322 ASN A N     1 
ATOM   2500 C  CA    . ASN A 1 322 ? -18.871 17.105  2.262   1.00 76.17  ? 322 ASN A CA    1 
ATOM   2501 C  C     . ASN A 1 322 ? -17.661 16.227  1.963   1.00 80.42  ? 322 ASN A C     1 
ATOM   2502 O  O     . ASN A 1 322 ? -17.405 15.854  0.814   1.00 77.31  ? 322 ASN A O     1 
ATOM   2503 C  CB    . ASN A 1 322 ? -20.084 16.226  2.570   1.00 76.42  ? 322 ASN A CB    1 
ATOM   2504 C  CG    . ASN A 1 322 ? -21.329 17.034  2.873   1.00 86.80  ? 322 ASN A CG    1 
ATOM   2505 O  OD1   . ASN A 1 322 ? -22.098 17.371  1.973   1.00 93.17  ? 322 ASN A OD1   1 
ATOM   2506 N  ND2   . ASN A 1 322 ? -21.536 17.347  4.146   1.00 81.25  ? 322 ASN A ND2   1 
ATOM   2507 N  N     . LEU A 1 323 ? -16.914 15.899  3.015   1.00 77.86  ? 323 LEU A N     1 
ATOM   2508 C  CA    . LEU A 1 323 ? -15.772 14.999  2.898   1.00 70.89  ? 323 LEU A CA    1 
ATOM   2509 C  C     . LEU A 1 323 ? -16.274 13.565  2.999   1.00 69.53  ? 323 LEU A C     1 
ATOM   2510 O  O     . LEU A 1 323 ? -16.762 13.145  4.052   1.00 74.73  ? 323 LEU A O     1 
ATOM   2511 C  CB    . LEU A 1 323 ? -14.742 15.300  3.982   1.00 71.53  ? 323 LEU A CB    1 
ATOM   2512 C  CG    . LEU A 1 323 ? -13.440 14.503  3.907   1.00 69.28  ? 323 LEU A CG    1 
ATOM   2513 C  CD1   . LEU A 1 323 ? -12.695 14.816  2.614   1.00 67.75  ? 323 LEU A CD1   1 
ATOM   2514 C  CD2   . LEU A 1 323 ? -12.570 14.786  5.122   1.00 70.27  ? 323 LEU A CD2   1 
ATOM   2515 N  N     . ARG A 1 324 ? -16.159 12.811  1.909   1.00 67.38  ? 324 ARG A N     1 
ATOM   2516 C  CA    . ARG A 1 324 ? -16.675 11.451  1.838   1.00 70.19  ? 324 ARG A CA    1 
ATOM   2517 C  C     . ARG A 1 324 ? -15.535 10.444  1.901   1.00 65.70  ? 324 ARG A C     1 
ATOM   2518 O  O     . ARG A 1 324 ? -14.476 10.650  1.301   1.00 68.05  ? 324 ARG A O     1 
ATOM   2519 C  CB    . ARG A 1 324 ? -17.495 11.240  0.562   1.00 71.61  ? 324 ARG A CB    1 
ATOM   2520 C  CG    . ARG A 1 324 ? -18.805 12.013  0.549   1.00 79.16  ? 324 ARG A CG    1 
ATOM   2521 C  CD    . ARG A 1 324 ? -19.788 11.432  -0.452  1.00 80.58  ? 324 ARG A CD    1 
ATOM   2522 N  NE    . ARG A 1 324 ? -21.098 12.063  -0.349  1.00 84.16  ? 324 ARG A NE    1 
ATOM   2523 C  CZ    . ARG A 1 324 ? -22.036 11.703  0.517   1.00 82.61  ? 324 ARG A CZ    1 
ATOM   2524 N  NH1   . ARG A 1 324 ? -21.843 10.712  1.372   1.00 79.56  ? 324 ARG A NH1   1 
ATOM   2525 N  NH2   . ARG A 1 324 ? -23.196 12.354  0.525   1.00 87.53  ? 324 ARG A NH2   1 
ATOM   2526 N  N     . ALA A 1 325 ? -15.764 9.349   2.625   1.00 63.67  ? 325 ALA A N     1 
ATOM   2527 C  CA    . ALA A 1 325 ? -14.742 8.345   2.871   1.00 61.98  ? 325 ALA A CA    1 
ATOM   2528 C  C     . ALA A 1 325 ? -15.301 6.950   2.629   1.00 64.96  ? 325 ALA A C     1 
ATOM   2529 O  O     . ALA A 1 325 ? -16.485 6.688   2.861   1.00 61.78  ? 325 ALA A O     1 
ATOM   2530 C  CB    . ALA A 1 325 ? -14.201 8.439   4.304   1.00 63.05  ? 325 ALA A CB    1 
ATOM   2531 N  N     . ILE A 1 326 ? -14.428 6.056   2.158   1.00 59.31  ? 326 ILE A N     1 
ATOM   2532 C  CA    . ILE A 1 326 ? -14.753 4.644   2.003   1.00 57.70  ? 326 ILE A CA    1 
ATOM   2533 C  C     . ILE A 1 326 ? -13.580 3.809   2.493   1.00 56.54  ? 326 ILE A C     1 
ATOM   2534 O  O     . ILE A 1 326 ? -12.420 4.228   2.431   1.00 55.95  ? 326 ILE A O     1 
ATOM   2535 C  CB    . ILE A 1 326 ? -15.087 4.263   0.545   1.00 56.37  ? 326 ILE A CB    1 
ATOM   2536 C  CG1   . ILE A 1 326 ? -13.820 4.280   -0.311  1.00 60.15  ? 326 ILE A CG1   1 
ATOM   2537 C  CG2   . ILE A 1 326 ? -16.148 5.188   -0.021  1.00 64.97  ? 326 ILE A CG2   1 
ATOM   2538 C  CD1   . ILE A 1 326 ? -14.055 3.911   -1.758  1.00 68.92  ? 326 ILE A CD1   1 
ATOM   2539 N  N     . ASN A 1 327 ? -13.898 2.615   2.990   1.00 56.30  ? 327 ASN A N     1 
ATOM   2540 C  CA    . ASN A 1 327 ? -12.887 1.614   3.295   1.00 55.10  ? 327 ASN A CA    1 
ATOM   2541 C  C     . ASN A 1 327 ? -12.634 0.807   2.031   1.00 53.25  ? 327 ASN A C     1 
ATOM   2542 O  O     . ASN A 1 327 ? -13.521 0.052   1.607   1.00 57.54  ? 327 ASN A O     1 
ATOM   2543 C  CB    . ASN A 1 327 ? -13.353 0.706   4.424   1.00 57.37  ? 327 ASN A CB    1 
ATOM   2544 C  CG    . ASN A 1 327 ? -12.418 -0.463  4.657   1.00 54.67  ? 327 ASN A CG    1 
ATOM   2545 O  OD1   . ASN A 1 327 ? -11.214 -0.370  4.419   1.00 53.69  ? 327 ASN A OD1   1 
ATOM   2546 N  ND2   . ASN A 1 327 ? -12.970 -1.575  5.127   1.00 57.29  ? 327 ASN A ND2   1 
ATOM   2547 N  N     . PRO A 1 328 ? -11.471 0.937   1.387   1.00 51.96  ? 328 PRO A N     1 
ATOM   2548 C  CA    . PRO A 1 328 ? -11.241 0.190   0.143   1.00 57.98  ? 328 PRO A CA    1 
ATOM   2549 C  C     . PRO A 1 328 ? -11.004 -1.292  0.366   1.00 54.72  ? 328 PRO A C     1 
ATOM   2550 O  O     . PRO A 1 328 ? -11.017 -2.052  -0.610  1.00 60.44  ? 328 PRO A O     1 
ATOM   2551 C  CB    . PRO A 1 328 ? -10.000 0.870   -0.447  1.00 54.03  ? 328 PRO A CB    1 
ATOM   2552 C  CG    . PRO A 1 328 ? -9.251  1.359   0.751   1.00 50.24  ? 328 PRO A CG    1 
ATOM   2553 C  CD    . PRO A 1 328 ? -10.299 1.743   1.775   1.00 53.40  ? 328 PRO A CD    1 
ATOM   2554 N  N     . GLU A 1 329 ? -10.795 -1.720  1.609   1.00 51.44  ? 329 GLU A N     1 
ATOM   2555 C  CA    . GLU A 1 329 ? -10.521 -3.110  1.924   1.00 50.01  ? 329 GLU A CA    1 
ATOM   2556 C  C     . GLU A 1 329 ? -11.819 -3.902  2.049   1.00 53.14  ? 329 GLU A C     1 
ATOM   2557 O  O     . GLU A 1 329 ? -12.922 -3.353  2.077   1.00 57.85  ? 329 GLU A O     1 
ATOM   2558 C  CB    . GLU A 1 329 ? -9.709  -3.219  3.214   1.00 50.16  ? 329 GLU A CB    1 
ATOM   2559 C  CG    . GLU A 1 329 ? -8.319  -2.611  3.131   1.00 49.55  ? 329 GLU A CG    1 
ATOM   2560 C  CD    . GLU A 1 329 ? -7.488  -2.904  4.364   1.00 52.90  ? 329 GLU A CD    1 
ATOM   2561 O  OE1   . GLU A 1 329 ? -7.967  -2.629  5.483   1.00 59.36  ? 329 GLU A OE1   1 
ATOM   2562 O  OE2   . GLU A 1 329 ? -6.363  -3.426  4.221   1.00 53.24  ? 329 GLU A OE2   1 
ATOM   2563 N  N     . ASN A 1 330 ? -11.667 -5.222  2.128   1.00 51.37  ? 330 ASN A N     1 
ATOM   2564 C  CA    . ASN A 1 330 ? -12.793 -6.138  2.231   1.00 55.84  ? 330 ASN A CA    1 
ATOM   2565 C  C     . ASN A 1 330 ? -12.758 -6.983  3.498   1.00 55.54  ? 330 ASN A C     1 
ATOM   2566 O  O     . ASN A 1 330 ? -13.675 -7.781  3.719   1.00 51.59  ? 330 ASN A O     1 
ATOM   2567 C  CB    . ASN A 1 330 ? -12.837 -7.052  0.998   1.00 59.17  ? 330 ASN A CB    1 
ATOM   2568 C  CG    . ASN A 1 330 ? -14.158 -7.782  0.861   1.00 59.07  ? 330 ASN A CG    1 
ATOM   2569 O  OD1   . ASN A 1 330 ? -15.171 -7.370  1.430   1.00 63.43  ? 330 ASN A OD1   1 
ATOM   2570 N  ND2   . ASN A 1 330 ? -14.155 -8.869  0.099   1.00 50.22  ? 330 ASN A ND2   1 
ATOM   2571 N  N     . GLY A 1 331 ? -11.731 -6.839  4.325   1.00 55.28  ? 331 GLY A N     1 
ATOM   2572 C  CA    . GLY A 1 331 ? -11.632 -7.570  5.565   1.00 51.89  ? 331 GLY A CA    1 
ATOM   2573 C  C     . GLY A 1 331 ? -10.736 -6.839  6.540   1.00 52.43  ? 331 GLY A C     1 
ATOM   2574 O  O     . GLY A 1 331 ? -10.349 -5.691  6.317   1.00 52.76  ? 331 GLY A O     1 
ATOM   2575 N  N     . PHE A 1 332 ? -10.409 -7.521  7.633   1.00 53.07  ? 332 PHE A N     1 
ATOM   2576 C  CA    . PHE A 1 332 ? -9.578  -6.952  8.685   1.00 53.79  ? 332 PHE A CA    1 
ATOM   2577 C  C     . PHE A 1 332 ? -8.330  -7.800  8.852   1.00 53.04  ? 332 PHE A C     1 
ATOM   2578 O  O     . PHE A 1 332 ? -8.417  -9.028  8.933   1.00 53.18  ? 332 PHE A O     1 
ATOM   2579 C  CB    . PHE A 1 332 ? -10.337 -6.866  10.012  1.00 56.00  ? 332 PHE A CB    1 
ATOM   2580 C  CG    . PHE A 1 332 ? -11.656 -6.160  9.909   1.00 59.87  ? 332 PHE A CG    1 
ATOM   2581 C  CD1   . PHE A 1 332 ? -11.711 -4.812  9.595   1.00 56.80  ? 332 PHE A CD1   1 
ATOM   2582 C  CD2   . PHE A 1 332 ? -12.841 -6.841  10.140  1.00 57.30  ? 332 PHE A CD2   1 
ATOM   2583 C  CE1   . PHE A 1 332 ? -12.921 -4.157  9.500   1.00 57.80  ? 332 PHE A CE1   1 
ATOM   2584 C  CE2   . PHE A 1 332 ? -14.059 -6.193  10.049  1.00 61.91  ? 332 PHE A CE2   1 
ATOM   2585 C  CZ    . PHE A 1 332 ? -14.099 -4.845  9.729   1.00 66.64  ? 332 PHE A CZ    1 
ATOM   2586 N  N     . PHE A 1 333 ? -7.178  -7.137  8.916   1.00 52.70  ? 333 PHE A N     1 
ATOM   2587 C  CA    . PHE A 1 333 ? -5.893  -7.800  9.089   1.00 52.79  ? 333 PHE A CA    1 
ATOM   2588 C  C     . PHE A 1 333 ? -5.250  -7.280  10.368  1.00 53.81  ? 333 PHE A C     1 
ATOM   2589 O  O     . PHE A 1 333 ? -4.203  -6.627  10.327  1.00 56.96  ? 333 PHE A O     1 
ATOM   2590 C  CB    . PHE A 1 333 ? -5.004  -7.549  7.865   1.00 55.27  ? 333 PHE A CB    1 
ATOM   2591 C  CG    . PHE A 1 333 ? -3.726  -8.344  7.852   1.00 55.61  ? 333 PHE A CG    1 
ATOM   2592 C  CD1   . PHE A 1 333 ? -3.726  -9.674  7.459   1.00 52.93  ? 333 PHE A CD1   1 
ATOM   2593 C  CD2   . PHE A 1 333 ? -2.519  -7.755  8.203   1.00 56.08  ? 333 PHE A CD2   1 
ATOM   2594 C  CE1   . PHE A 1 333 ? -2.555  -10.408 7.435   1.00 51.75  ? 333 PHE A CE1   1 
ATOM   2595 C  CE2   . PHE A 1 333 ? -1.341  -8.482  8.182   1.00 56.34  ? 333 PHE A CE2   1 
ATOM   2596 C  CZ    . PHE A 1 333 ? -1.360  -9.813  7.797   1.00 57.17  ? 333 PHE A CZ    1 
ATOM   2597 N  N     . GLY A 1 334 ? -5.891  -7.548  11.515  1.00 56.30  ? 334 GLY A N     1 
ATOM   2598 C  CA    . GLY A 1 334 ? -5.492  -6.931  12.762  1.00 58.20  ? 334 GLY A CA    1 
ATOM   2599 C  C     . GLY A 1 334 ? -4.551  -7.782  13.598  1.00 57.47  ? 334 GLY A C     1 
ATOM   2600 O  O     . GLY A 1 334 ? -4.417  -8.988  13.399  1.00 61.31  ? 334 GLY A O     1 
ATOM   2601 N  N     . VAL A 1 335 ? -3.893  -7.122  14.553  1.00 58.72  ? 335 VAL A N     1 
ATOM   2602 C  CA    . VAL A 1 335 ? -2.986  -7.818  15.457  1.00 65.27  ? 335 VAL A CA    1 
ATOM   2603 C  C     . VAL A 1 335 ? -3.781  -8.746  16.369  1.00 68.92  ? 335 VAL A C     1 
ATOM   2604 O  O     . VAL A 1 335 ? -4.942  -8.481  16.711  1.00 66.17  ? 335 VAL A O     1 
ATOM   2605 C  CB    . VAL A 1 335 ? -2.157  -6.811  16.274  1.00 69.99  ? 335 VAL A CB    1 
ATOM   2606 C  CG1   . VAL A 1 335 ? -1.180  -7.541  17.186  1.00 73.00  ? 335 VAL A CG1   1 
ATOM   2607 C  CG2   . VAL A 1 335 ? -1.424  -5.861  15.347  1.00 66.06  ? 335 VAL A CG2   1 
ATOM   2608 N  N     . ALA A 1 336 ? -3.146  -9.844  16.779  1.00 69.51  ? 336 ALA A N     1 
ATOM   2609 C  CA    . ALA A 1 336 ? -3.826  -10.870 17.559  1.00 66.16  ? 336 ALA A CA    1 
ATOM   2610 C  C     . ALA A 1 336 ? -3.690  -10.614 19.057  1.00 67.70  ? 336 ALA A C     1 
ATOM   2611 O  O     . ALA A 1 336 ? -4.703  -10.421 19.743  1.00 64.34  ? 336 ALA A O     1 
ATOM   2612 C  CB    . ALA A 1 336 ? -3.284  -12.256 17.203  1.00 66.50  ? 336 ALA A CB    1 
ATOM   2613 N  N     . PRO A 1 337 ? -2.471  -10.601 19.600  1.00 69.19  ? 337 PRO A N     1 
ATOM   2614 C  CA    . PRO A 1 337 ? -2.313  -10.452 21.052  1.00 67.93  ? 337 PRO A CA    1 
ATOM   2615 C  C     . PRO A 1 337 ? -3.048  -9.227  21.579  1.00 67.11  ? 337 PRO A C     1 
ATOM   2616 O  O     . PRO A 1 337 ? -3.187  -8.212  20.892  1.00 73.79  ? 337 PRO A O     1 
ATOM   2617 C  CB    . PRO A 1 337 ? -0.796  -10.320 21.231  1.00 66.30  ? 337 PRO A CB    1 
ATOM   2618 C  CG    . PRO A 1 337 ? -0.221  -11.012 20.045  1.00 71.23  ? 337 PRO A CG    1 
ATOM   2619 C  CD    . PRO A 1 337 ? -1.172  -10.725 18.916  1.00 68.31  ? 337 PRO A CD    1 
ATOM   2620 N  N     . GLY A 1 338 ? -3.520  -9.331  22.819  1.00 67.33  ? 338 GLY A N     1 
ATOM   2621 C  CA    . GLY A 1 338 ? -4.300  -8.279  23.427  1.00 68.81  ? 338 GLY A CA    1 
ATOM   2622 C  C     . GLY A 1 338 ? -5.768  -8.283  23.067  1.00 68.86  ? 338 GLY A C     1 
ATOM   2623 O  O     . GLY A 1 338 ? -6.550  -7.582  23.724  1.00 74.73  ? 338 GLY A O     1 
ATOM   2624 N  N     . THR A 1 339 ? -6.172  -9.042  22.051  1.00 67.35  ? 339 THR A N     1 
ATOM   2625 C  CA    . THR A 1 339 ? -7.578  -9.155  21.670  1.00 67.41  ? 339 THR A CA    1 
ATOM   2626 C  C     . THR A 1 339 ? -8.263  -10.126 22.624  1.00 71.22  ? 339 THR A C     1 
ATOM   2627 O  O     . THR A 1 339 ? -8.143  -11.345 22.485  1.00 69.91  ? 339 THR A O     1 
ATOM   2628 C  CB    . THR A 1 339 ? -7.708  -9.624  20.227  1.00 65.39  ? 339 THR A CB    1 
ATOM   2629 O  OG1   . THR A 1 339 ? -6.884  -8.813  19.382  1.00 73.12  ? 339 THR A OG1   1 
ATOM   2630 C  CG2   . THR A 1 339 ? -9.153  -9.523  19.765  1.00 65.52  ? 339 THR A CG2   1 
ATOM   2631 N  N     . SER A 1 340 ? -8.985  -9.591  23.602  1.00 75.04  ? 340 SER A N     1 
ATOM   2632 C  CA    . SER A 1 340 ? -9.729  -10.400 24.552  1.00 79.26  ? 340 SER A CA    1 
ATOM   2633 C  C     . SER A 1 340 ? -11.206 -10.037 24.487  1.00 73.91  ? 340 SER A C     1 
ATOM   2634 O  O     . SER A 1 340 ? -11.607 -9.063  23.846  1.00 79.72  ? 340 SER A O     1 
ATOM   2635 C  CB    . SER A 1 340 ? -9.193  -10.217 25.978  1.00 78.62  ? 340 SER A CB    1 
ATOM   2636 O  OG    . SER A 1 340 ? -9.424  -8.903  26.452  1.00 91.98  ? 340 SER A OG    1 
ATOM   2637 N  N     . VAL A 1 341 ? -12.025 -10.851 25.154  1.00 79.12  ? 341 VAL A N     1 
ATOM   2638 C  CA    . VAL A 1 341 ? -13.454 -10.568 25.216  1.00 89.33  ? 341 VAL A CA    1 
ATOM   2639 C  C     . VAL A 1 341 ? -13.717 -9.271  25.963  1.00 93.99  ? 341 VAL A C     1 
ATOM   2640 O  O     . VAL A 1 341 ? -14.742 -8.616  25.741  1.00 85.69  ? 341 VAL A O     1 
ATOM   2641 C  CB    . VAL A 1 341 ? -14.200 -11.750 25.861  1.00 94.18  ? 341 VAL A CB    1 
ATOM   2642 C  CG1   . VAL A 1 341 ? -15.689 -11.449 25.964  1.00 91.71  ? 341 VAL A CG1   1 
ATOM   2643 C  CG2   . VAL A 1 341 ? -13.954 -13.016 25.062  1.00 90.47  ? 341 VAL A CG2   1 
ATOM   2644 N  N     . LYS A 1 342 ? -12.801 -8.874  26.851  1.00 124.50 ? 342 LYS A N     1 
ATOM   2645 C  CA    . LYS A 1 342 ? -12.990 -7.648  27.620  1.00 126.32 ? 342 LYS A CA    1 
ATOM   2646 C  C     . LYS A 1 342 ? -12.506 -6.413  26.871  1.00 125.41 ? 342 LYS A C     1 
ATOM   2647 O  O     . LYS A 1 342 ? -12.992 -5.308  27.134  1.00 126.72 ? 342 LYS A O     1 
ATOM   2648 C  CB    . LYS A 1 342 ? -12.271 -7.754  28.966  1.00 128.27 ? 342 LYS A CB    1 
ATOM   2649 C  CG    . LYS A 1 342 ? -10.756 -7.765  28.868  1.00 129.44 ? 342 LYS A CG    1 
ATOM   2650 C  CD    . LYS A 1 342 ? -10.120 -7.767  30.245  1.00 139.12 ? 342 LYS A CD    1 
ATOM   2651 C  CE    . LYS A 1 342 ? -8.604  -7.706  30.159  1.00 140.36 ? 342 LYS A CE    1 
ATOM   2652 N  NZ    . LYS A 1 342 ? -8.126  -6.408  29.605  1.00 148.91 ? 342 LYS A NZ    1 
ATOM   2653 N  N     . THR A 1 343 ? -11.557 -6.571  25.948  1.00 91.74  ? 343 THR A N     1 
ATOM   2654 C  CA    . THR A 1 343 ? -11.046 -5.442  25.175  1.00 84.77  ? 343 THR A CA    1 
ATOM   2655 C  C     . THR A 1 343 ? -11.839 -5.242  23.886  1.00 78.87  ? 343 THR A C     1 
ATOM   2656 O  O     . THR A 1 343 ? -12.498 -4.213  23.706  1.00 80.60  ? 343 THR A O     1 
ATOM   2657 C  CB    . THR A 1 343 ? -9.557  -5.640  24.864  1.00 79.58  ? 343 THR A CB    1 
ATOM   2658 O  OG1   . THR A 1 343 ? -9.382  -6.829  24.082  1.00 80.70  ? 343 THR A OG1   1 
ATOM   2659 C  CG2   . THR A 1 343 ? -8.754  -5.757  26.150  1.00 79.48  ? 343 THR A CG2   1 
ATOM   2660 N  N     . ASN A 1 344 ? -11.789 -6.217  22.982  1.00 73.62  ? 344 ASN A N     1 
ATOM   2661 C  CA    . ASN A 1 344 ? -12.429 -6.115  21.672  1.00 73.46  ? 344 ASN A CA    1 
ATOM   2662 C  C     . ASN A 1 344 ? -13.341 -7.316  21.469  1.00 75.23  ? 344 ASN A C     1 
ATOM   2663 O  O     . ASN A 1 344 ? -13.043 -8.217  20.674  1.00 72.03  ? 344 ASN A O     1 
ATOM   2664 C  CB    . ASN A 1 344 ? -11.385 -6.016  20.560  1.00 69.16  ? 344 ASN A CB    1 
ATOM   2665 C  CG    . ASN A 1 344 ? -11.983 -5.585  19.238  1.00 71.34  ? 344 ASN A CG    1 
ATOM   2666 O  OD1   . ASN A 1 344 ? -13.203 -5.499  19.097  1.00 68.60  ? 344 ASN A OD1   1 
ATOM   2667 N  ND2   . ASN A 1 344 ? -11.127 -5.319  18.256  1.00 77.65  ? 344 ASN A ND2   1 
ATOM   2668 N  N     . PRO A 1 345 ? -14.474 -7.357  22.172  1.00 77.07  ? 345 PRO A N     1 
ATOM   2669 C  CA    . PRO A 1 345 ? -15.385 -8.501  22.013  1.00 76.97  ? 345 PRO A CA    1 
ATOM   2670 C  C     . PRO A 1 345 ? -15.980 -8.602  20.621  1.00 71.11  ? 345 PRO A C     1 
ATOM   2671 O  O     . PRO A 1 345 ? -16.280 -9.712  20.164  1.00 75.53  ? 345 PRO A O     1 
ATOM   2672 C  CB    . PRO A 1 345 ? -16.461 -8.239  23.076  1.00 80.15  ? 345 PRO A CB    1 
ATOM   2673 C  CG    . PRO A 1 345 ? -16.453 -6.758  23.253  1.00 76.49  ? 345 PRO A CG    1 
ATOM   2674 C  CD    . PRO A 1 345 ? -15.018 -6.334  23.081  1.00 82.25  ? 345 PRO A CD    1 
ATOM   2675 N  N     . ASN A 1 346 ? -16.169 -7.474  19.932  1.00 70.81  ? 346 ASN A N     1 
ATOM   2676 C  CA    . ASN A 1 346 ? -16.644 -7.526  18.554  1.00 69.36  ? 346 ASN A CA    1 
ATOM   2677 C  C     . ASN A 1 346 ? -15.640 -8.223  17.646  1.00 70.47  ? 346 ASN A C     1 
ATOM   2678 O  O     . ASN A 1 346 ? -16.030 -8.852  16.656  1.00 69.14  ? 346 ASN A O     1 
ATOM   2679 C  CB    . ASN A 1 346 ? -16.931 -6.114  18.044  1.00 74.75  ? 346 ASN A CB    1 
ATOM   2680 C  CG    . ASN A 1 346 ? -18.138 -5.492  18.713  1.00 78.55  ? 346 ASN A CG    1 
ATOM   2681 O  OD1   . ASN A 1 346 ? -19.224 -6.072  18.714  1.00 79.33  ? 346 ASN A OD1   1 
ATOM   2682 N  ND2   . ASN A 1 346 ? -17.952 -4.315  19.299  1.00 72.96  ? 346 ASN A ND2   1 
ATOM   2683 N  N     . ALA A 1 347 ? -14.347 -8.115  17.959  1.00 69.15  ? 347 ALA A N     1 
ATOM   2684 C  CA    . ALA A 1 347 ? -13.342 -8.847  17.198  1.00 64.90  ? 347 ALA A CA    1 
ATOM   2685 C  C     . ALA A 1 347 ? -13.497 -10.349 17.395  1.00 65.73  ? 347 ALA A C     1 
ATOM   2686 O  O     . ALA A 1 347 ? -13.389 -11.122 16.437  1.00 69.67  ? 347 ALA A O     1 
ATOM   2687 C  CB    . ALA A 1 347 ? -11.942 -8.394  17.606  1.00 64.68  ? 347 ALA A CB    1 
ATOM   2688 N  N     . ILE A 1 348 ? -13.758 -10.775 18.633  1.00 71.81  ? 348 ILE A N     1 
ATOM   2689 C  CA    . ILE A 1 348 ? -13.907 -12.199 18.922  1.00 66.54  ? 348 ILE A CA    1 
ATOM   2690 C  C     . ILE A 1 348 ? -15.056 -12.789 18.115  1.00 68.92  ? 348 ILE A C     1 
ATOM   2691 O  O     . ILE A 1 348 ? -14.936 -13.871 17.528  1.00 65.30  ? 348 ILE A O     1 
ATOM   2692 C  CB    . ILE A 1 348 ? -14.106 -12.419 20.432  1.00 68.52  ? 348 ILE A CB    1 
ATOM   2693 C  CG1   . ILE A 1 348 ? -12.911 -11.873 21.215  1.00 68.91  ? 348 ILE A CG1   1 
ATOM   2694 C  CG2   . ILE A 1 348 ? -14.308 -13.893 20.730  1.00 83.47  ? 348 ILE A CG2   1 
ATOM   2695 C  CD1   . ILE A 1 348 ? -11.601 -12.553 20.885  1.00 74.83  ? 348 ILE A CD1   1 
ATOM   2696 N  N     . LYS A 1 349 ? -16.192 -12.087 18.075  1.00 71.76  ? 349 LYS A N     1 
ATOM   2697 C  CA    . LYS A 1 349 ? -17.347 -12.585 17.337  1.00 67.13  ? 349 LYS A CA    1 
ATOM   2698 C  C     . LYS A 1 349 ? -17.077 -12.708 15.844  1.00 68.93  ? 349 LYS A C     1 
ATOM   2699 O  O     . LYS A 1 349 ? -17.735 -13.508 15.171  1.00 71.58  ? 349 LYS A O     1 
ATOM   2700 C  CB    . LYS A 1 349 ? -18.557 -11.676 17.563  1.00 68.27  ? 349 LYS A CB    1 
ATOM   2701 C  CG    . LYS A 1 349 ? -19.126 -11.720 18.971  1.00 89.79  ? 349 LYS A CG    1 
ATOM   2702 C  CD    . LYS A 1 349 ? -20.431 -10.942 19.049  1.00 95.47  ? 349 LYS A CD    1 
ATOM   2703 C  CE    . LYS A 1 349 ? -21.075 -11.057 20.419  1.00 104.30 ? 349 LYS A CE    1 
ATOM   2704 N  NZ    . LYS A 1 349 ? -22.425 -10.427 20.445  1.00 105.28 ? 349 LYS A NZ    1 
ATOM   2705 N  N     . THR A 1 350 ? -16.127 -11.940 15.310  1.00 68.61  ? 350 THR A N     1 
ATOM   2706 C  CA    . THR A 1 350 ? -15.875 -11.935 13.874  1.00 63.11  ? 350 THR A CA    1 
ATOM   2707 C  C     . THR A 1 350 ? -14.925 -13.038 13.427  1.00 60.77  ? 350 THR A C     1 
ATOM   2708 O  O     . THR A 1 350 ? -15.077 -13.560 12.316  1.00 60.16  ? 350 THR A O     1 
ATOM   2709 C  CB    . THR A 1 350 ? -15.303 -10.579 13.441  1.00 63.35  ? 350 THR A CB    1 
ATOM   2710 O  OG1   . THR A 1 350 ? -16.201 -9.532  13.826  1.00 67.58  ? 350 THR A OG1   1 
ATOM   2711 C  CG2   . THR A 1 350 ? -15.105 -10.533 11.930  1.00 59.68  ? 350 THR A CG2   1 
ATOM   2712 N  N     . ILE A 1 351 ? -13.954 -13.408 14.260  1.00 60.99  ? 351 ILE A N     1 
ATOM   2713 C  CA    . ILE A 1 351 ? -12.855 -14.265 13.825  1.00 59.80  ? 351 ILE A CA    1 
ATOM   2714 C  C     . ILE A 1 351 ? -13.160 -15.737 14.071  1.00 67.57  ? 351 ILE A C     1 
ATOM   2715 O  O     . ILE A 1 351 ? -12.289 -16.596 13.894  1.00 68.58  ? 351 ILE A O     1 
ATOM   2716 C  CB    . ILE A 1 351 ? -11.543 -13.865 14.522  1.00 62.97  ? 351 ILE A CB    1 
ATOM   2717 C  CG1   . ILE A 1 351 ? -11.726 -13.858 16.040  1.00 61.60  ? 351 ILE A CG1   1 
ATOM   2718 C  CG2   . ILE A 1 351 ? -11.074 -12.507 14.029  1.00 59.09  ? 351 ILE A CG2   1 
ATOM   2719 C  CD1   . ILE A 1 351 ? -10.470 -13.507 16.804  1.00 61.82  ? 351 ILE A CD1   1 
ATOM   2720 N  N     . GLN A 1 352 ? -14.390 -16.046 14.470  1.00 67.27  ? 352 GLN A N     1 
ATOM   2721 C  CA    . GLN A 1 352 ? -14.740 -17.424 14.789  1.00 68.55  ? 352 GLN A CA    1 
ATOM   2722 C  C     . GLN A 1 352 ? -15.130 -18.246 13.567  1.00 67.21  ? 352 GLN A C     1 
ATOM   2723 O  O     . GLN A 1 352 ? -15.594 -19.379 13.731  1.00 72.45  ? 352 GLN A O     1 
ATOM   2724 C  CB    . GLN A 1 352 ? -15.870 -17.459 15.819  1.00 69.10  ? 352 GLN A CB    1 
ATOM   2725 C  CG    . GLN A 1 352 ? -15.420 -17.094 17.220  1.00 72.05  ? 352 GLN A CG    1 
ATOM   2726 C  CD    . GLN A 1 352 ? -16.431 -17.488 18.269  1.00 90.44  ? 352 GLN A CD    1 
ATOM   2727 O  OE1   . GLN A 1 352 ? -17.598 -17.732 17.961  1.00 105.82 ? 352 GLN A OE1   1 
ATOM   2728 N  NE2   . GLN A 1 352 ? -15.989 -17.562 19.519  1.00 97.33  ? 352 GLN A NE2   1 
ATOM   2729 N  N     . LYS A 1 353 ? -14.958 -17.723 12.357  1.00 60.47  ? 353 LYS A N     1 
ATOM   2730 C  CA    . LYS A 1 353 ? -15.198 -18.544 11.179  1.00 66.28  ? 353 LYS A CA    1 
ATOM   2731 C  C     . LYS A 1 353 ? -14.628 -17.845 9.954   1.00 66.53  ? 353 LYS A C     1 
ATOM   2732 O  O     . LYS A 1 353 ? -14.512 -16.615 9.922   1.00 65.98  ? 353 LYS A O     1 
ATOM   2733 C  CB    . LYS A 1 353 ? -16.692 -18.840 10.986  1.00 65.91  ? 353 LYS A CB    1 
ATOM   2734 C  CG    . LYS A 1 353 ? -17.538 -17.635 10.621  1.00 71.01  ? 353 LYS A CG    1 
ATOM   2735 C  CD    . LYS A 1 353 ? -19.002 -18.029 10.474  1.00 79.51  ? 353 LYS A CD    1 
ATOM   2736 C  CE    . LYS A 1 353 ? -19.880 -16.818 10.196  1.00 93.40  ? 353 LYS A CE    1 
ATOM   2737 N  NZ    . LYS A 1 353 ? -21.327 -17.178 10.171  1.00 112.77 ? 353 LYS A NZ    1 
ATOM   2738 N  N     . ASN A 1 354 ? -14.261 -18.647 8.955   1.00 63.87  ? 354 ASN A N     1 
ATOM   2739 C  CA    . ASN A 1 354 ? -13.733 -18.134 7.694   1.00 54.84  ? 354 ASN A CA    1 
ATOM   2740 C  C     . ASN A 1 354 ? -12.511 -17.250 7.916   1.00 54.11  ? 354 ASN A C     1 
ATOM   2741 O  O     . ASN A 1 354 ? -12.242 -16.338 7.131   1.00 59.96  ? 354 ASN A O     1 
ATOM   2742 C  CB    . ASN A 1 354 ? -14.815 -17.373 6.924   1.00 54.73  ? 354 ASN A CB    1 
ATOM   2743 C  CG    . ASN A 1 354 ? -16.091 -18.180 6.767   1.00 60.67  ? 354 ASN A CG    1 
ATOM   2744 O  OD1   . ASN A 1 354 ? -16.051 -19.398 6.602   1.00 71.18  ? 354 ASN A OD1   1 
ATOM   2745 N  ND2   . ASN A 1 354 ? -17.232 -17.503 6.824   1.00 56.98  ? 354 ASN A ND2   1 
ATOM   2746 N  N     . THR A 1 355 ? -11.754 -17.521 8.975   1.00 54.66  ? 355 THR A N     1 
ATOM   2747 C  CA    . THR A 1 355 ? -10.681 -16.646 9.427   1.00 55.64  ? 355 THR A CA    1 
ATOM   2748 C  C     . THR A 1 355 ? -9.349  -17.377 9.360   1.00 56.20  ? 355 THR A C     1 
ATOM   2749 O  O     . THR A 1 355 ? -9.237  -18.514 9.828   1.00 57.91  ? 355 THR A O     1 
ATOM   2750 C  CB    . THR A 1 355 ? -10.947 -16.161 10.853  1.00 55.76  ? 355 THR A CB    1 
ATOM   2751 O  OG1   . THR A 1 355 ? -12.211 -15.489 10.895  1.00 56.45  ? 355 THR A OG1   1 
ATOM   2752 C  CG2   . THR A 1 355 ? -9.856  -15.207 11.313  1.00 55.55  ? 355 THR A CG2   1 
ATOM   2753 N  N     . ILE A 1 356 ? -8.343  -16.719 8.787   1.00 52.58  ? 356 ILE A N     1 
ATOM   2754 C  CA    . ILE A 1 356 ? -6.997  -17.266 8.668   1.00 52.18  ? 356 ILE A CA    1 
ATOM   2755 C  C     . ILE A 1 356 ? -6.101  -16.562 9.676   1.00 52.40  ? 356 ILE A C     1 
ATOM   2756 O  O     . ILE A 1 356 ? -6.029  -15.328 9.696   1.00 56.85  ? 356 ILE A O     1 
ATOM   2757 C  CB    . ILE A 1 356 ? -6.449  -17.109 7.239   1.00 56.98  ? 356 ILE A CB    1 
ATOM   2758 C  CG1   . ILE A 1 356 ? -7.361  -17.818 6.237   1.00 56.77  ? 356 ILE A CG1   1 
ATOM   2759 C  CG2   . ILE A 1 356 ? -5.032  -17.658 7.145   1.00 51.59  ? 356 ILE A CG2   1 
ATOM   2760 C  CD1   . ILE A 1 356 ? -6.793  -17.886 4.839   1.00 57.34  ? 356 ILE A CD1   1 
ATOM   2761 N  N     . PHE A 1 357 ? -5.419  -17.344 10.506  1.00 53.07  ? 357 PHE A N     1 
ATOM   2762 C  CA    . PHE A 1 357 ? -4.527  -16.830 11.534  1.00 53.65  ? 357 PHE A CA    1 
ATOM   2763 C  C     . PHE A 1 357 ? -3.077  -17.093 11.147  1.00 58.91  ? 357 PHE A C     1 
ATOM   2764 O  O     . PHE A 1 357 ? -2.772  -18.054 10.436  1.00 56.44  ? 357 PHE A O     1 
ATOM   2765 C  CB    . PHE A 1 357 ? -4.821  -17.475 12.895  1.00 62.74  ? 357 PHE A CB    1 
ATOM   2766 C  CG    . PHE A 1 357 ? -6.220  -17.244 13.389  1.00 56.25  ? 357 PHE A CG    1 
ATOM   2767 C  CD1   . PHE A 1 357 ? -7.266  -18.033 12.939  1.00 56.36  ? 357 PHE A CD1   1 
ATOM   2768 C  CD2   . PHE A 1 357 ? -6.489  -16.240 14.306  1.00 57.19  ? 357 PHE A CD2   1 
ATOM   2769 C  CE1   . PHE A 1 357 ? -8.557  -17.825 13.393  1.00 60.34  ? 357 PHE A CE1   1 
ATOM   2770 C  CE2   . PHE A 1 357 ? -7.779  -16.024 14.767  1.00 59.85  ? 357 PHE A CE2   1 
ATOM   2771 C  CZ    . PHE A 1 357 ? -8.814  -16.818 14.309  1.00 58.41  ? 357 PHE A CZ    1 
ATOM   2772 N  N     . THR A 1 358 ? -2.179  -16.234 11.631  1.00 55.85  ? 358 THR A N     1 
ATOM   2773 C  CA    . THR A 1 358 ? -0.756  -16.354 11.331  1.00 60.25  ? 358 THR A CA    1 
ATOM   2774 C  C     . THR A 1 358 ? 0.047   -16.156 12.607  1.00 58.67  ? 358 THR A C     1 
ATOM   2775 O  O     . THR A 1 358 ? -0.037  -15.099 13.239  1.00 64.69  ? 358 THR A O     1 
ATOM   2776 C  CB    . THR A 1 358 ? -0.316  -15.338 10.269  1.00 62.90  ? 358 THR A CB    1 
ATOM   2777 O  OG1   . THR A 1 358 ? -1.095  -15.510 9.076   1.00 57.75  ? 358 THR A OG1   1 
ATOM   2778 C  CG2   . THR A 1 358 ? 1.155   -15.528 9.938   1.00 59.26  ? 358 THR A CG2   1 
ATOM   2779 N  N     . ASN A 1 359 ? 0.823   -17.171 12.982  1.00 63.51  ? 359 ASN A N     1 
ATOM   2780 C  CA    . ASN A 1 359 ? 1.780   -17.127 14.085  1.00 66.48  ? 359 ASN A CA    1 
ATOM   2781 C  C     . ASN A 1 359 ? 1.130   -17.023 15.459  1.00 67.09  ? 359 ASN A C     1 
ATOM   2782 O  O     . ASN A 1 359 ? 1.814   -16.684 16.432  1.00 73.05  ? 359 ASN A O     1 
ATOM   2783 C  CB    . ASN A 1 359 ? 2.778   -15.981 13.910  1.00 64.62  ? 359 ASN A CB    1 
ATOM   2784 C  CG    . ASN A 1 359 ? 3.658   -16.164 12.692  1.00 68.47  ? 359 ASN A CG    1 
ATOM   2785 O  OD1   . ASN A 1 359 ? 3.968   -17.288 12.300  1.00 69.27  ? 359 ASN A OD1   1 
ATOM   2786 N  ND2   . ASN A 1 359 ? 4.061   -15.057 12.083  1.00 69.60  ? 359 ASN A ND2   1 
ATOM   2787 N  N     . VAL A 1 360 ? -0.162  -17.302 15.577  1.00 64.81  ? 360 VAL A N     1 
ATOM   2788 C  CA    . VAL A 1 360 ? -0.791  -17.408 16.884  1.00 67.87  ? 360 VAL A CA    1 
ATOM   2789 C  C     . VAL A 1 360 ? -0.631  -18.839 17.380  1.00 68.15  ? 360 VAL A C     1 
ATOM   2790 O  O     . VAL A 1 360 ? -0.340  -19.759 16.613  1.00 68.79  ? 360 VAL A O     1 
ATOM   2791 C  CB    . VAL A 1 360 ? -2.276  -16.997 16.852  1.00 66.25  ? 360 VAL A CB    1 
ATOM   2792 C  CG1   . VAL A 1 360 ? -2.423  -15.556 16.385  1.00 58.06  ? 360 VAL A CG1   1 
ATOM   2793 C  CG2   . VAL A 1 360 ? -3.073  -17.948 15.969  1.00 58.10  ? 360 VAL A CG2   1 
ATOM   2794 N  N     . ALA A 1 361 ? -0.820  -19.030 18.683  1.00 65.56  ? 361 ALA A N     1 
ATOM   2795 C  CA    . ALA A 1 361 ? -0.688  -20.354 19.271  1.00 67.37  ? 361 ALA A CA    1 
ATOM   2796 C  C     . ALA A 1 361 ? -1.927  -21.195 18.989  1.00 64.28  ? 361 ALA A C     1 
ATOM   2797 O  O     . ALA A 1 361 ? -3.023  -20.674 18.770  1.00 68.77  ? 361 ALA A O     1 
ATOM   2798 C  CB    . ALA A 1 361 ? -0.456  -20.257 20.779  1.00 68.72  ? 361 ALA A CB    1 
ATOM   2799 N  N     . GLU A 1 362 ? -1.741  -22.511 18.991  1.00 62.58  ? 362 GLU A N     1 
ATOM   2800 C  CA    . GLU A 1 362 ? -2.826  -23.458 18.784  1.00 66.07  ? 362 GLU A CA    1 
ATOM   2801 C  C     . GLU A 1 362 ? -3.035  -24.289 20.042  1.00 68.24  ? 362 GLU A C     1 
ATOM   2802 O  O     . GLU A 1 362 ? -2.070  -24.761 20.652  1.00 67.83  ? 362 GLU A O     1 
ATOM   2803 C  CB    . GLU A 1 362 ? -2.537  -24.378 17.595  1.00 66.30  ? 362 GLU A CB    1 
ATOM   2804 C  CG    . GLU A 1 362 ? -3.660  -25.354 17.281  1.00 68.18  ? 362 GLU A CG    1 
ATOM   2805 C  CD    . GLU A 1 362 ? -3.302  -26.321 16.165  1.00 77.48  ? 362 GLU A CD    1 
ATOM   2806 O  OE1   . GLU A 1 362 ? -2.203  -26.191 15.587  1.00 77.29  ? 362 GLU A OE1   1 
ATOM   2807 O  OE2   . GLU A 1 362 ? -4.119  -27.217 15.866  1.00 84.41  ? 362 GLU A OE2   1 
ATOM   2808 N  N     . THR A 1 363 ? -4.295  -24.463 20.430  1.00 67.62  ? 363 THR A N     1 
ATOM   2809 C  CA    . THR A 1 363 ? -4.632  -25.285 21.581  1.00 67.61  ? 363 THR A CA    1 
ATOM   2810 C  C     . THR A 1 363 ? -4.852  -26.731 21.152  1.00 71.32  ? 363 THR A C     1 
ATOM   2811 O  O     . THR A 1 363 ? -5.286  -27.011 20.031  1.00 70.81  ? 363 THR A O     1 
ATOM   2812 C  CB    . THR A 1 363 ? -5.879  -24.756 22.293  1.00 68.60  ? 363 THR A CB    1 
ATOM   2813 O  OG1   . THR A 1 363 ? -6.991  -24.762 21.389  1.00 67.87  ? 363 THR A OG1   1 
ATOM   2814 C  CG2   . THR A 1 363 ? -5.643  -23.341 22.790  1.00 72.82  ? 363 THR A CG2   1 
ATOM   2815 N  N     . SER A 1 364 ? -4.550  -27.653 22.068  1.00 70.02  ? 364 SER A N     1 
ATOM   2816 C  CA    . SER A 1 364 ? -4.611  -29.075 21.751  1.00 70.02  ? 364 SER A CA    1 
ATOM   2817 C  C     . SER A 1 364 ? -5.993  -29.519 21.290  1.00 70.17  ? 364 SER A C     1 
ATOM   2818 O  O     . SER A 1 364 ? -6.111  -30.580 20.666  1.00 71.55  ? 364 SER A O     1 
ATOM   2819 C  CB    . SER A 1 364 ? -4.177  -29.894 22.965  1.00 71.93  ? 364 SER A CB    1 
ATOM   2820 O  OG    . SER A 1 364 ? -4.820  -29.429 24.137  1.00 73.21  ? 364 SER A OG    1 
ATOM   2821 N  N     . ASP A 1 365 ? -7.036  -28.743 21.579  1.00 70.31  ? 365 ASP A N     1 
ATOM   2822 C  CA    . ASP A 1 365 ? -8.392  -29.083 21.173  1.00 70.53  ? 365 ASP A CA    1 
ATOM   2823 C  C     . ASP A 1 365 ? -8.806  -28.406 19.873  1.00 68.77  ? 365 ASP A C     1 
ATOM   2824 O  O     . ASP A 1 365 ? -9.971  -28.510 19.476  1.00 73.31  ? 365 ASP A O     1 
ATOM   2825 C  CB    . ASP A 1 365 ? -9.381  -28.734 22.289  1.00 71.99  ? 365 ASP A CB    1 
ATOM   2826 C  CG    . ASP A 1 365 ? -9.381  -27.257 22.630  1.00 78.77  ? 365 ASP A CG    1 
ATOM   2827 O  OD1   . ASP A 1 365 ? -8.396  -26.565 22.294  1.00 77.03  ? 365 ASP A OD1   1 
ATOM   2828 O  OD2   . ASP A 1 365 ? -10.367 -26.790 23.241  1.00 76.28  ? 365 ASP A OD2   1 
ATOM   2829 N  N     . GLY A 1 366 ? -7.886  -27.719 19.205  1.00 67.73  ? 366 GLY A N     1 
ATOM   2830 C  CA    . GLY A 1 366 ? -8.167  -27.102 17.927  1.00 67.14  ? 366 GLY A CA    1 
ATOM   2831 C  C     . GLY A 1 366 ? -8.520  -25.632 17.961  1.00 70.96  ? 366 GLY A C     1 
ATOM   2832 O  O     . GLY A 1 366 ? -9.164  -25.152 17.022  1.00 70.79  ? 366 GLY A O     1 
ATOM   2833 N  N     . GLY A 1 367 ? -8.124  -24.903 19.005  1.00 67.00  ? 367 GLY A N     1 
ATOM   2834 C  CA    . GLY A 1 367 ? -8.412  -23.494 19.126  1.00 70.41  ? 367 GLY A CA    1 
ATOM   2835 C  C     . GLY A 1 367 ? -7.166  -22.633 18.989  1.00 64.23  ? 367 GLY A C     1 
ATOM   2836 O  O     . GLY A 1 367 ? -6.066  -23.106 18.714  1.00 65.96  ? 367 GLY A O     1 
ATOM   2837 N  N     . VAL A 1 368 ? -7.370  -21.335 19.194  1.00 64.10  ? 368 VAL A N     1 
ATOM   2838 C  CA    . VAL A 1 368 ? -6.301  -20.351 19.083  1.00 70.55  ? 368 VAL A CA    1 
ATOM   2839 C  C     . VAL A 1 368 ? -5.951  -19.841 20.473  1.00 64.72  ? 368 VAL A C     1 
ATOM   2840 O  O     . VAL A 1 368 ? -6.759  -19.879 21.404  1.00 66.17  ? 368 VAL A O     1 
ATOM   2841 C  CB    . VAL A 1 368 ? -6.679  -19.177 18.154  1.00 62.06  ? 368 VAL A CB    1 
ATOM   2842 C  CG1   . VAL A 1 368 ? -6.883  -19.661 16.729  1.00 60.63  ? 368 VAL A CG1   1 
ATOM   2843 C  CG2   . VAL A 1 368 ? -7.925  -18.474 18.667  1.00 63.03  ? 368 VAL A CG2   1 
ATOM   2844 N  N     . TYR A 1 369 ? -4.721  -19.351 20.607  1.00 64.36  ? 369 TYR A N     1 
ATOM   2845 C  CA    . TYR A 1 369 ? -4.297  -18.726 21.848  1.00 69.56  ? 369 TYR A CA    1 
ATOM   2846 C  C     . TYR A 1 369 ? -3.258  -17.655 21.549  1.00 68.48  ? 369 TYR A C     1 
ATOM   2847 O  O     . TYR A 1 369 ? -2.476  -17.771 20.602  1.00 73.33  ? 369 TYR A O     1 
ATOM   2848 C  CB    . TYR A 1 369 ? -3.731  -19.751 22.835  1.00 66.99  ? 369 TYR A CB    1 
ATOM   2849 C  CG    . TYR A 1 369 ? -4.099  -19.458 24.268  1.00 68.94  ? 369 TYR A CG    1 
ATOM   2850 C  CD1   . TYR A 1 369 ? -5.409  -19.599 24.706  1.00 70.09  ? 369 TYR A CD1   1 
ATOM   2851 C  CD2   . TYR A 1 369 ? -3.142  -19.044 25.184  1.00 69.85  ? 369 TYR A CD2   1 
ATOM   2852 C  CE1   . TYR A 1 369 ? -5.758  -19.337 26.014  1.00 71.83  ? 369 TYR A CE1   1 
ATOM   2853 C  CE2   . TYR A 1 369 ? -3.482  -18.780 26.500  1.00 72.15  ? 369 TYR A CE2   1 
ATOM   2854 C  CZ    . TYR A 1 369 ? -4.793  -18.928 26.907  1.00 72.73  ? 369 TYR A CZ    1 
ATOM   2855 O  OH    . TYR A 1 369 ? -5.146  -18.666 28.212  1.00 80.96  ? 369 TYR A OH    1 
ATOM   2856 N  N     . TRP A 1 370 ? -3.269  -16.605 22.364  1.00 65.80  ? 370 TRP A N     1 
ATOM   2857 C  CA    . TRP A 1 370 ? -2.271  -15.549 22.281  1.00 77.84  ? 370 TRP A CA    1 
ATOM   2858 C  C     . TRP A 1 370 ? -2.248  -14.812 23.611  1.00 81.76  ? 370 TRP A C     1 
ATOM   2859 O  O     . TRP A 1 370 ? -3.149  -14.956 24.442  1.00 74.83  ? 370 TRP A O     1 
ATOM   2860 C  CB    . TRP A 1 370 ? -2.551  -14.587 21.121  1.00 63.91  ? 370 TRP A CB    1 
ATOM   2861 C  CG    . TRP A 1 370 ? -3.943  -14.044 21.107  1.00 64.33  ? 370 TRP A CG    1 
ATOM   2862 C  CD1   . TRP A 1 370 ? -4.477  -13.132 21.969  1.00 65.72  ? 370 TRP A CD1   1 
ATOM   2863 C  CD2   . TRP A 1 370 ? -4.979  -14.368 20.172  1.00 63.46  ? 370 TRP A CD2   1 
ATOM   2864 N  NE1   . TRP A 1 370 ? -5.784  -12.874 21.634  1.00 65.78  ? 370 TRP A NE1   1 
ATOM   2865 C  CE2   . TRP A 1 370 ? -6.116  -13.620 20.534  1.00 64.39  ? 370 TRP A CE2   1 
ATOM   2866 C  CE3   . TRP A 1 370 ? -5.056  -15.222 19.067  1.00 62.10  ? 370 TRP A CE3   1 
ATOM   2867 C  CZ2   . TRP A 1 370 ? -7.316  -13.698 19.830  1.00 63.98  ? 370 TRP A CZ2   1 
ATOM   2868 C  CZ3   . TRP A 1 370 ? -6.249  -15.299 18.369  1.00 61.69  ? 370 TRP A CZ3   1 
ATOM   2869 C  CH2   . TRP A 1 370 ? -7.362  -14.542 18.753  1.00 62.62  ? 370 TRP A CH2   1 
ATOM   2870 N  N     . GLU A 1 371 ? -1.197  -14.022 23.803  1.00 77.36  ? 371 GLU A N     1 
ATOM   2871 C  CA    . GLU A 1 371 ? -1.049  -13.270 25.040  1.00 80.09  ? 371 GLU A CA    1 
ATOM   2872 C  C     . GLU A 1 371 ? -2.152  -12.226 25.156  1.00 75.76  ? 371 GLU A C     1 
ATOM   2873 O  O     . GLU A 1 371 ? -2.487  -11.540 24.187  1.00 68.59  ? 371 GLU A O     1 
ATOM   2874 C  CB    . GLU A 1 371 ? 0.324   -12.602 25.097  1.00 80.40  ? 371 GLU A CB    1 
ATOM   2875 C  CG    . GLU A 1 371 ? 1.484   -13.571 25.307  1.00 84.47  ? 371 GLU A CG    1 
ATOM   2876 C  CD    . GLU A 1 371 ? 1.673   -14.539 24.151  1.00 88.28  ? 371 GLU A CD    1 
ATOM   2877 O  OE1   . GLU A 1 371 ? 0.861   -14.515 23.201  1.00 81.48  ? 371 GLU A OE1   1 
ATOM   2878 O  OE2   . GLU A 1 371 ? 2.640   -15.326 24.195  1.00 91.59  ? 371 GLU A OE2   1 
ATOM   2879 N  N     . GLY A 1 372 ? -2.726  -12.119 26.353  1.00 74.33  ? 372 GLY A N     1 
ATOM   2880 C  CA    . GLY A 1 372 ? -3.808  -11.192 26.595  1.00 72.41  ? 372 GLY A CA    1 
ATOM   2881 C  C     . GLY A 1 372 ? -5.176  -11.667 26.161  1.00 73.09  ? 372 GLY A C     1 
ATOM   2882 O  O     . GLY A 1 372 ? -6.145  -10.910 26.301  1.00 80.97  ? 372 GLY A O     1 
ATOM   2883 N  N     . ILE A 1 373 ? -5.294  -12.891 25.640  1.00 77.74  ? 373 ILE A N     1 
ATOM   2884 C  CA    . ILE A 1 373 ? -6.604  -13.408 25.261  1.00 78.10  ? 373 ILE A CA    1 
ATOM   2885 C  C     . ILE A 1 373 ? -7.532  -13.477 26.464  1.00 73.96  ? 373 ILE A C     1 
ATOM   2886 O  O     . ILE A 1 373 ? -8.753  -13.572 26.299  1.00 73.43  ? 373 ILE A O     1 
ATOM   2887 C  CB    . ILE A 1 373 ? -6.473  -14.788 24.584  1.00 69.89  ? 373 ILE A CB    1 
ATOM   2888 C  CG1   . ILE A 1 373 ? -7.755  -15.123 23.822  1.00 69.34  ? 373 ILE A CG1   1 
ATOM   2889 C  CG2   . ILE A 1 373 ? -6.170  -15.862 25.618  1.00 71.19  ? 373 ILE A CG2   1 
ATOM   2890 C  CD1   . ILE A 1 373 ? -7.656  -16.370 22.976  1.00 76.99  ? 373 ILE A CD1   1 
ATOM   2891 N  N     . ASP A 1 374 ? -6.978  -13.433 27.675  1.00 80.31  ? 374 ASP A N     1 
ATOM   2892 C  CA    . ASP A 1 374 ? -7.763  -13.302 28.899  1.00 86.16  ? 374 ASP A CA    1 
ATOM   2893 C  C     . ASP A 1 374 ? -8.870  -14.350 28.953  1.00 91.34  ? 374 ASP A C     1 
ATOM   2894 O  O     . ASP A 1 374 ? -10.053 -14.041 29.113  1.00 95.92  ? 374 ASP A O     1 
ATOM   2895 C  CB    . ASP A 1 374 ? -8.334  -11.888 29.023  1.00 94.26  ? 374 ASP A CB    1 
ATOM   2896 C  CG    . ASP A 1 374 ? -8.970  -11.631 30.373  1.00 108.89 ? 374 ASP A CG    1 
ATOM   2897 O  OD1   . ASP A 1 374 ? -8.941  -12.537 31.230  1.00 114.76 ? 374 ASP A OD1   1 
ATOM   2898 O  OD2   . ASP A 1 374 ? -9.501  -10.520 30.577  1.00 118.88 ? 374 ASP A OD2   1 
ATOM   2899 N  N     . GLU A 1 375 ? -8.474  -15.609 28.818  1.00 87.10  ? 375 GLU A N     1 
ATOM   2900 C  CA    . GLU A 1 375 ? -9.454  -16.680 28.753  1.00 81.47  ? 375 GLU A CA    1 
ATOM   2901 C  C     . GLU A 1 375 ? -8.843  -17.982 29.255  1.00 82.97  ? 375 GLU A C     1 
ATOM   2902 O  O     . GLU A 1 375 ? -7.910  -18.511 28.637  1.00 82.25  ? 375 GLU A O     1 
ATOM   2903 C  CB    . GLU A 1 375 ? -9.969  -16.831 27.321  1.00 80.55  ? 375 GLU A CB    1 
ATOM   2904 C  CG    . GLU A 1 375 ? -11.283 -17.577 27.205  1.00 91.00  ? 375 GLU A CG    1 
ATOM   2905 C  CD    . GLU A 1 375 ? -12.011 -17.259 25.915  1.00 88.12  ? 375 GLU A CD    1 
ATOM   2906 O  OE1   . GLU A 1 375 ? -11.566 -16.340 25.197  1.00 85.46  ? 375 GLU A OE1   1 
ATOM   2907 O  OE2   . GLU A 1 375 ? -13.026 -17.921 25.620  1.00 93.79  ? 375 GLU A OE2   1 
ATOM   2908 N  N     . PRO A 1 376 ? -9.329  -18.516 30.374  1.00 87.73  ? 376 PRO A N     1 
ATOM   2909 C  CA    . PRO A 1 376 ? -8.784  -19.777 30.886  1.00 87.57  ? 376 PRO A CA    1 
ATOM   2910 C  C     . PRO A 1 376 ? -9.129  -20.943 29.978  1.00 82.05  ? 376 PRO A C     1 
ATOM   2911 O  O     . PRO A 1 376 ? -10.208 -21.004 29.383  1.00 90.03  ? 376 PRO A O     1 
ATOM   2912 C  CB    . PRO A 1 376 ? -9.458  -19.930 32.256  1.00 82.55  ? 376 PRO A CB    1 
ATOM   2913 C  CG    . PRO A 1 376 ? -9.953  -18.566 32.602  1.00 83.23  ? 376 PRO A CG    1 
ATOM   2914 C  CD    . PRO A 1 376 ? -10.313 -17.929 31.297  1.00 81.54  ? 376 PRO A CD    1 
ATOM   2915 N  N     . LEU A 1 377 ? -8.192  -21.876 29.880  1.00 81.17  ? 377 LEU A N     1 
ATOM   2916 C  CA    . LEU A 1 377 ? -8.377  -23.095 29.110  1.00 81.14  ? 377 LEU A CA    1 
ATOM   2917 C  C     . LEU A 1 377 ? -8.819  -24.229 30.029  1.00 85.07  ? 377 LEU A C     1 
ATOM   2918 O  O     . LEU A 1 377 ? -8.556  -24.224 31.234  1.00 82.51  ? 377 LEU A O     1 
ATOM   2919 C  CB    . LEU A 1 377 ? -7.087  -23.474 28.377  1.00 81.12  ? 377 LEU A CB    1 
ATOM   2920 C  CG    . LEU A 1 377 ? -6.610  -22.463 27.332  1.00 75.38  ? 377 LEU A CG    1 
ATOM   2921 C  CD1   . LEU A 1 377 ? -5.193  -22.772 26.882  1.00 73.66  ? 377 LEU A CD1   1 
ATOM   2922 C  CD2   . LEU A 1 377 ? -7.556  -22.441 26.141  1.00 77.94  ? 377 LEU A CD2   1 
ATOM   2923 N  N     . ALA A 1 378 ? -9.507  -25.205 29.441  1.00 85.52  ? 378 ALA A N     1 
ATOM   2924 C  CA    . ALA A 1 378 ? -10.034 -26.321 30.206  1.00 86.09  ? 378 ALA A CA    1 
ATOM   2925 C  C     . ALA A 1 378 ? -8.893  -27.186 30.728  1.00 82.09  ? 378 ALA A C     1 
ATOM   2926 O  O     . ALA A 1 378 ? -7.739  -27.031 30.321  1.00 81.02  ? 378 ALA A O     1 
ATOM   2927 C  CB    . ALA A 1 378 ? -10.988 -27.152 29.349  1.00 80.94  ? 378 ALA A CB    1 
ATOM   2928 N  N     . PRO A 1 379 ? -9.187  -28.104 31.646  1.00 79.38  ? 379 PRO A N     1 
ATOM   2929 C  CA    . PRO A 1 379 ? -8.153  -29.038 32.104  1.00 80.93  ? 379 PRO A CA    1 
ATOM   2930 C  C     . PRO A 1 379 ? -7.721  -29.967 30.981  1.00 78.94  ? 379 PRO A C     1 
ATOM   2931 O  O     . PRO A 1 379 ? -8.544  -30.479 30.219  1.00 77.59  ? 379 PRO A O     1 
ATOM   2932 C  CB    . PRO A 1 379 ? -8.844  -29.811 33.236  1.00 84.10  ? 379 PRO A CB    1 
ATOM   2933 C  CG    . PRO A 1 379 ? -10.018 -28.961 33.633  1.00 84.70  ? 379 PRO A CG    1 
ATOM   2934 C  CD    . PRO A 1 379 ? -10.454 -28.277 32.375  1.00 84.60  ? 379 PRO A CD    1 
ATOM   2935 N  N     . GLY A 1 380 ? -6.411  -30.178 30.881  1.00 79.01  ? 380 GLY A N     1 
ATOM   2936 C  CA    . GLY A 1 380 ? -5.873  -31.065 29.872  1.00 77.53  ? 380 GLY A CA    1 
ATOM   2937 C  C     . GLY A 1 380 ? -5.729  -30.469 28.491  1.00 77.97  ? 380 GLY A C     1 
ATOM   2938 O  O     . GLY A 1 380 ? -5.520  -31.220 27.532  1.00 84.06  ? 380 GLY A O     1 
ATOM   2939 N  N     . VAL A 1 381 ? -5.834  -29.151 28.352  1.00 78.36  ? 381 VAL A N     1 
ATOM   2940 C  CA    . VAL A 1 381 ? -5.647  -28.475 27.073  1.00 70.05  ? 381 VAL A CA    1 
ATOM   2941 C  C     . VAL A 1 381 ? -4.230  -27.922 27.036  1.00 70.12  ? 381 VAL A C     1 
ATOM   2942 O  O     . VAL A 1 381 ? -3.832  -27.154 27.921  1.00 72.16  ? 381 VAL A O     1 
ATOM   2943 C  CB    . VAL A 1 381 ? -6.683  -27.360 26.866  1.00 71.49  ? 381 VAL A CB    1 
ATOM   2944 C  CG1   . VAL A 1 381 ? -6.386  -26.592 25.592  1.00 73.54  ? 381 VAL A CG1   1 
ATOM   2945 C  CG2   . VAL A 1 381 ? -8.084  -27.946 26.817  1.00 78.14  ? 381 VAL A CG2   1 
ATOM   2946 N  N     . THR A 1 382 ? -3.466  -28.316 26.022  1.00 76.58  ? 382 THR A N     1 
ATOM   2947 C  CA    . THR A 1 382 ? -2.098  -27.855 25.841  1.00 74.86  ? 382 THR A CA    1 
ATOM   2948 C  C     . THR A 1 382 ? -2.029  -26.805 24.739  1.00 65.76  ? 382 THR A C     1 
ATOM   2949 O  O     . THR A 1 382 ? -2.940  -26.666 23.919  1.00 69.88  ? 382 THR A O     1 
ATOM   2950 C  CB    . THR A 1 382 ? -1.163  -29.022 25.507  1.00 70.97  ? 382 THR A CB    1 
ATOM   2951 O  OG1   . THR A 1 382 ? -1.740  -29.820 24.465  1.00 67.71  ? 382 THR A OG1   1 
ATOM   2952 C  CG2   . THR A 1 382 ? -0.923  -29.879 26.735  1.00 72.38  ? 382 THR A CG2   1 
ATOM   2953 N  N     . ILE A 1 383 ? -0.923  -26.066 24.728  1.00 70.22  ? 383 ILE A N     1 
ATOM   2954 C  CA    . ILE A 1 383 ? -0.711  -24.965 23.795  1.00 71.17  ? 383 ILE A CA    1 
ATOM   2955 C  C     . ILE A 1 383 ? 0.578   -25.215 23.027  1.00 72.25  ? 383 ILE A C     1 
ATOM   2956 O  O     . ILE A 1 383 ? 1.628   -25.469 23.629  1.00 80.33  ? 383 ILE A O     1 
ATOM   2957 C  CB    . ILE A 1 383 ? -0.649  -23.608 24.520  1.00 74.33  ? 383 ILE A CB    1 
ATOM   2958 C  CG1   . ILE A 1 383 ? -1.936  -23.357 25.307  1.00 72.95  ? 383 ILE A CG1   1 
ATOM   2959 C  CG2   . ILE A 1 383 ? -0.395  -22.482 23.525  1.00 70.56  ? 383 ILE A CG2   1 
ATOM   2960 C  CD1   . ILE A 1 383 ? -1.906  -22.086 26.132  1.00 74.15  ? 383 ILE A CD1   1 
ATOM   2961 N  N     . THR A 1 384 ? 0.498   -25.139 21.702  1.00 67.76  ? 384 THR A N     1 
ATOM   2962 C  CA    . THR A 1 384 ? 1.674   -25.150 20.844  1.00 76.03  ? 384 THR A CA    1 
ATOM   2963 C  C     . THR A 1 384 ? 1.944   -23.722 20.387  1.00 74.77  ? 384 THR A C     1 
ATOM   2964 O  O     . THR A 1 384 ? 1.073   -23.084 19.784  1.00 74.59  ? 384 THR A O     1 
ATOM   2965 C  CB    . THR A 1 384 ? 1.480   -26.072 19.641  1.00 68.91  ? 384 THR A CB    1 
ATOM   2966 O  OG1   . THR A 1 384 ? 1.258   -27.411 20.096  1.00 80.71  ? 384 THR A OG1   1 
ATOM   2967 C  CG2   . THR A 1 384 ? 2.713   -26.052 18.754  1.00 70.71  ? 384 THR A CG2   1 
ATOM   2968 N  N     . SER A 1 385 ? 3.140   -23.222 20.683  1.00 76.96  ? 385 SER A N     1 
ATOM   2969 C  CA    . SER A 1 385 ? 3.490   -21.856 20.333  1.00 79.83  ? 385 SER A CA    1 
ATOM   2970 C  C     . SER A 1 385 ? 3.533   -21.684 18.815  1.00 77.18  ? 385 SER A C     1 
ATOM   2971 O  O     . SER A 1 385 ? 3.368   -22.634 18.044  1.00 73.60  ? 385 SER A O     1 
ATOM   2972 C  CB    . SER A 1 385 ? 4.837   -21.475 20.947  1.00 87.69  ? 385 SER A CB    1 
ATOM   2973 O  OG    . SER A 1 385 ? 5.880   -22.283 20.430  1.00 91.74  ? 385 SER A OG    1 
ATOM   2974 N  N     . TRP A 1 386 ? 3.753   -20.440 18.388  1.00 75.75  ? 386 TRP A N     1 
ATOM   2975 C  CA    . TRP A 1 386 ? 3.883   -20.158 16.965  1.00 79.39  ? 386 TRP A CA    1 
ATOM   2976 C  C     . TRP A 1 386 ? 5.181   -20.709 16.390  1.00 82.69  ? 386 TRP A C     1 
ATOM   2977 O  O     . TRP A 1 386 ? 5.284   -20.875 15.170  1.00 88.05  ? 386 TRP A O     1 
ATOM   2978 C  CB    . TRP A 1 386 ? 3.798   -18.653 16.716  1.00 77.27  ? 386 TRP A CB    1 
ATOM   2979 C  CG    . TRP A 1 386 ? 5.024   -17.924 17.143  1.00 78.74  ? 386 TRP A CG    1 
ATOM   2980 C  CD1   . TRP A 1 386 ? 5.314   -17.467 18.395  1.00 78.31  ? 386 TRP A CD1   1 
ATOM   2981 C  CD2   . TRP A 1 386 ? 6.138   -17.574 16.317  1.00 83.07  ? 386 TRP A CD2   1 
ATOM   2982 N  NE1   . TRP A 1 386 ? 6.543   -16.852 18.400  1.00 81.70  ? 386 TRP A NE1   1 
ATOM   2983 C  CE2   . TRP A 1 386 ? 7.069   -16.903 17.135  1.00 85.54  ? 386 TRP A CE2   1 
ATOM   2984 C  CE3   . TRP A 1 386 ? 6.440   -17.761 14.965  1.00 81.06  ? 386 TRP A CE3   1 
ATOM   2985 C  CZ2   . TRP A 1 386 ? 8.278   -16.419 16.646  1.00 83.31  ? 386 TRP A CZ2   1 
ATOM   2986 C  CZ3   . TRP A 1 386 ? 7.640   -17.279 14.481  1.00 81.03  ? 386 TRP A CZ3   1 
ATOM   2987 C  CH2   . TRP A 1 386 ? 8.545   -16.616 15.319  1.00 84.16  ? 386 TRP A CH2   1 
ATOM   2988 N  N     . LYS A 1 387 ? 6.172   -20.987 17.237  1.00 84.67  ? 387 LYS A N     1 
ATOM   2989 C  CA    . LYS A 1 387 ? 7.404   -21.638 16.811  1.00 88.52  ? 387 LYS A CA    1 
ATOM   2990 C  C     . LYS A 1 387 ? 7.228   -23.135 16.594  1.00 95.30  ? 387 LYS A C     1 
ATOM   2991 O  O     . LYS A 1 387 ? 8.220   -23.837 16.370  1.00 102.19 ? 387 LYS A O     1 
ATOM   2992 C  CB    . LYS A 1 387 ? 8.516   -21.393 17.836  1.00 91.13  ? 387 LYS A CB    1 
ATOM   2993 C  CG    . LYS A 1 387 ? 9.030   -19.961 17.883  1.00 92.64  ? 387 LYS A CG    1 
ATOM   2994 C  CD    . LYS A 1 387 ? 10.116  -19.807 18.937  1.00 96.73  ? 387 LYS A CD    1 
ATOM   2995 C  CE    . LYS A 1 387 ? 10.683  -18.396 18.954  1.00 103.50 ? 387 LYS A CE    1 
ATOM   2996 N  NZ    . LYS A 1 387 ? 11.390  -18.064 17.686  1.00 103.73 ? 387 LYS A NZ    1 
ATOM   2997 N  N     . ASN A 1 388 ? 5.994   -23.634 16.657  1.00 92.93  ? 388 ASN A N     1 
ATOM   2998 C  CA    . ASN A 1 388 ? 5.702   -25.055 16.489  1.00 89.17  ? 388 ASN A CA    1 
ATOM   2999 C  C     . ASN A 1 388 ? 6.473   -25.888 17.515  1.00 97.71  ? 388 ASN A C     1 
ATOM   3000 O  O     . ASN A 1 388 ? 7.294   -26.743 17.178  1.00 100.54 ? 388 ASN A O     1 
ATOM   3001 C  CB    . ASN A 1 388 ? 6.007   -25.513 15.060  1.00 88.94  ? 388 ASN A CB    1 
ATOM   3002 C  CG    . ASN A 1 388 ? 5.277   -26.787 14.691  1.00 93.18  ? 388 ASN A CG    1 
ATOM   3003 O  OD1   . ASN A 1 388 ? 4.130   -26.994 15.085  1.00 90.88  ? 388 ASN A OD1   1 
ATOM   3004 N  ND2   . ASN A 1 388 ? 5.942   -27.654 13.936  1.00 101.70 ? 388 ASN A ND2   1 
ATOM   3005 N  N     . LYS A 1 389 ? 6.193   -25.612 18.786  1.00 97.53  ? 389 LYS A N     1 
ATOM   3006 C  CA    . LYS A 1 389 ? 6.821   -26.322 19.890  1.00 100.00 ? 389 LYS A CA    1 
ATOM   3007 C  C     . LYS A 1 389 ? 5.856   -26.353 21.064  1.00 98.08  ? 389 LYS A C     1 
ATOM   3008 O  O     . LYS A 1 389 ? 5.040   -25.445 21.237  1.00 93.15  ? 389 LYS A O     1 
ATOM   3009 C  CB    . LYS A 1 389 ? 8.142   -25.665 20.312  1.00 102.80 ? 389 LYS A CB    1 
ATOM   3010 C  CG    . LYS A 1 389 ? 9.195   -25.603 19.215  1.00 106.40 ? 389 LYS A CG    1 
ATOM   3011 C  CD    . LYS A 1 389 ? 10.444  -24.868 19.684  1.00 114.53 ? 389 LYS A CD    1 
ATOM   3012 C  CE    . LYS A 1 389 ? 11.436  -24.674 18.545  1.00 115.47 ? 389 LYS A CE    1 
ATOM   3013 N  NZ    . LYS A 1 389 ? 12.617  -23.864 18.957  1.00 109.50 ? 389 LYS A NZ    1 
ATOM   3014 N  N     . GLU A 1 390 ? 5.951   -27.413 21.864  1.00 107.52 ? 390 GLU A N     1 
ATOM   3015 C  CA    . GLU A 1 390 ? 5.175   -27.486 23.094  1.00 107.46 ? 390 GLU A CA    1 
ATOM   3016 C  C     . GLU A 1 390 ? 5.526   -26.304 23.987  1.00 107.21 ? 390 GLU A C     1 
ATOM   3017 O  O     . GLU A 1 390 ? 6.689   -26.124 24.364  1.00 111.42 ? 390 GLU A O     1 
ATOM   3018 C  CB    . GLU A 1 390 ? 5.447   -28.807 23.812  1.00 113.33 ? 390 GLU A CB    1 
ATOM   3019 C  CG    . GLU A 1 390 ? 4.936   -30.032 23.071  1.00 119.24 ? 390 GLU A CG    1 
ATOM   3020 C  CD    . GLU A 1 390 ? 3.423   -30.152 23.110  1.00 121.02 ? 390 GLU A CD    1 
ATOM   3021 O  OE1   . GLU A 1 390 ? 2.806   -29.622 24.057  1.00 111.10 ? 390 GLU A OE1   1 
ATOM   3022 O  OE2   . GLU A 1 390 ? 2.851   -30.777 22.193  1.00 128.88 ? 390 GLU A OE2   1 
ATOM   3023 N  N     . TRP A 1 391 ? 4.525   -25.494 24.318  1.00 101.06 ? 391 TRP A N     1 
ATOM   3024 C  CA    . TRP A 1 391 ? 4.731   -24.250 25.043  1.00 108.11 ? 391 TRP A CA    1 
ATOM   3025 C  C     . TRP A 1 391 ? 3.962   -24.269 26.356  1.00 109.22 ? 391 TRP A C     1 
ATOM   3026 O  O     . TRP A 1 391 ? 2.793   -24.666 26.396  1.00 102.54 ? 391 TRP A O     1 
ATOM   3027 C  CB    . TRP A 1 391 ? 4.294   -23.046 24.199  1.00 100.52 ? 391 TRP A CB    1 
ATOM   3028 C  CG    . TRP A 1 391 ? 4.370   -21.742 24.929  1.00 105.13 ? 391 TRP A CG    1 
ATOM   3029 C  CD1   . TRP A 1 391 ? 5.443   -20.903 25.000  1.00 106.84 ? 391 TRP A CD1   1 
ATOM   3030 C  CD2   . TRP A 1 391 ? 3.327   -21.126 25.695  1.00 110.27 ? 391 TRP A CD2   1 
ATOM   3031 N  NE1   . TRP A 1 391 ? 5.133   -19.802 25.763  1.00 110.11 ? 391 TRP A NE1   1 
ATOM   3032 C  CE2   . TRP A 1 391 ? 3.840   -19.916 26.202  1.00 111.22 ? 391 TRP A CE2   1 
ATOM   3033 C  CE3   . TRP A 1 391 ? 2.010   -21.482 26.003  1.00 108.52 ? 391 TRP A CE3   1 
ATOM   3034 C  CZ2   . TRP A 1 391 ? 3.082   -19.059 26.998  1.00 112.78 ? 391 TRP A CZ2   1 
ATOM   3035 C  CZ3   . TRP A 1 391 ? 1.260   -20.630 26.793  1.00 110.75 ? 391 TRP A CZ3   1 
ATOM   3036 C  CH2   . TRP A 1 391 ? 1.797   -19.434 27.282  1.00 110.22 ? 391 TRP A CH2   1 
ATOM   3037 N  N     . ARG A 1 392 ? 4.626   -23.834 27.427  1.00 117.40 ? 392 ARG A N     1 
ATOM   3038 C  CA    . ARG A 1 392 ? 4.021   -23.698 28.741  1.00 131.06 ? 392 ARG A CA    1 
ATOM   3039 C  C     . ARG A 1 392 ? 4.113   -22.253 29.218  1.00 137.76 ? 392 ARG A C     1 
ATOM   3040 O  O     . ARG A 1 392 ? 5.043   -21.529 28.849  1.00 136.81 ? 392 ARG A O     1 
ATOM   3041 C  CB    . ARG A 1 392 ? 4.695   -24.615 29.772  1.00 143.10 ? 392 ARG A CB    1 
ATOM   3042 C  CG    . ARG A 1 392 ? 4.545   -26.101 29.484  1.00 138.87 ? 392 ARG A CG    1 
ATOM   3043 C  CD    . ARG A 1 392 ? 4.980   -26.941 30.677  1.00 143.35 ? 392 ARG A CD    1 
ATOM   3044 N  NE    . ARG A 1 392 ? 6.360   -26.676 31.065  1.00 148.88 ? 392 ARG A NE    1 
ATOM   3045 C  CZ    . ARG A 1 392 ? 6.991   -27.292 32.056  1.00 154.90 ? 392 ARG A CZ    1 
ATOM   3046 N  NH1   . ARG A 1 392 ? 6.394   -28.221 32.785  1.00 154.67 ? 392 ARG A NH1   1 
ATOM   3047 N  NH2   . ARG A 1 392 ? 8.254   -26.970 32.320  1.00 156.94 ? 392 ARG A NH2   1 
ATOM   3048 N  N     . PRO A 1 393 ? 3.160   -21.804 30.039  1.00 144.65 ? 393 PRO A N     1 
ATOM   3049 C  CA    . PRO A 1 393 ? 3.185   -20.411 30.514  1.00 147.19 ? 393 PRO A CA    1 
ATOM   3050 C  C     . PRO A 1 393 ? 4.361   -20.105 31.432  1.00 158.25 ? 393 PRO A C     1 
ATOM   3051 O  O     . PRO A 1 393 ? 4.487   -18.983 31.933  1.00 160.54 ? 393 PRO A O     1 
ATOM   3052 C  CB    . PRO A 1 393 ? 1.848   -20.274 31.258  1.00 148.12 ? 393 PRO A CB    1 
ATOM   3053 C  CG    . PRO A 1 393 ? 0.979   -21.351 30.689  1.00 145.64 ? 393 PRO A CG    1 
ATOM   3054 C  CD    . PRO A 1 393 ? 1.912   -22.490 30.409  1.00 145.00 ? 393 PRO A CD    1 
ATOM   3055 N  N     . GLN A 1 394 ? 5.224   -21.093 31.672  1.00 168.40 ? 394 GLN A N     1 
ATOM   3056 C  CA    . GLN A 1 394 ? 6.386   -20.891 32.527  1.00 170.99 ? 394 GLN A CA    1 
ATOM   3057 C  C     . GLN A 1 394 ? 7.623   -20.435 31.764  1.00 170.33 ? 394 GLN A C     1 
ATOM   3058 O  O     . GLN A 1 394 ? 8.572   -19.944 32.387  1.00 173.77 ? 394 GLN A O     1 
ATOM   3059 C  CB    . GLN A 1 394 ? 6.710   -22.177 33.297  1.00 176.30 ? 394 GLN A CB    1 
ATOM   3060 C  CG    . GLN A 1 394 ? 5.788   -22.443 34.480  1.00 186.02 ? 394 GLN A CG    1 
ATOM   3061 C  CD    . GLN A 1 394 ? 4.376   -22.798 34.057  1.00 179.25 ? 394 GLN A CD    1 
ATOM   3062 O  OE1   . GLN A 1 394 ? 4.112   -23.055 32.883  1.00 170.07 ? 394 GLN A OE1   1 
ATOM   3063 N  NE2   . GLN A 1 394 ? 3.459   -22.816 35.017  1.00 187.97 ? 394 GLN A NE2   1 
ATOM   3064 N  N     . ASP A 1 395 ? 7.640   -20.584 30.443  1.00 164.59 ? 395 ASP A N     1 
ATOM   3065 C  CA    . ASP A 1 395 ? 8.760   -20.113 29.647  1.00 162.50 ? 395 ASP A CA    1 
ATOM   3066 C  C     . ASP A 1 395 ? 8.617   -18.622 29.357  1.00 159.82 ? 395 ASP A C     1 
ATOM   3067 O  O     . ASP A 1 395 ? 7.529   -18.046 29.444  1.00 157.47 ? 395 ASP A O     1 
ATOM   3068 C  CB    . ASP A 1 395 ? 8.852   -20.891 28.333  1.00 154.55 ? 395 ASP A CB    1 
ATOM   3069 C  CG    . ASP A 1 395 ? 8.849   -22.393 28.540  1.00 156.91 ? 395 ASP A CG    1 
ATOM   3070 O  OD1   . ASP A 1 395 ? 8.946   -22.837 29.704  1.00 160.27 ? 395 ASP A OD1   1 
ATOM   3071 O  OD2   . ASP A 1 395 ? 8.743   -23.130 27.537  1.00 145.84 ? 395 ASP A OD2   1 
ATOM   3072 N  N     . GLU A 1 396 ? 9.742   -17.992 29.012  1.00 159.52 ? 396 GLU A N     1 
ATOM   3073 C  CA    . GLU A 1 396 ? 9.702   -16.599 28.585  1.00 157.94 ? 396 GLU A CA    1 
ATOM   3074 C  C     . GLU A 1 396 ? 9.255   -16.453 27.138  1.00 149.23 ? 396 GLU A C     1 
ATOM   3075 O  O     . GLU A 1 396 ? 8.811   -15.369 26.746  1.00 147.60 ? 396 GLU A O     1 
ATOM   3076 C  CB    . GLU A 1 396 ? 11.071  -15.939 28.768  1.00 165.23 ? 396 GLU A CB    1 
ATOM   3077 C  CG    . GLU A 1 396 ? 11.064  -14.437 28.503  1.00 167.41 ? 396 GLU A CG    1 
ATOM   3078 C  CD    . GLU A 1 396 ? 12.442  -13.809 28.606  1.00 160.01 ? 396 GLU A CD    1 
ATOM   3079 O  OE1   . GLU A 1 396 ? 13.442  -14.557 28.608  1.00 158.36 ? 396 GLU A OE1   1 
ATOM   3080 O  OE2   . GLU A 1 396 ? 12.525  -12.564 28.684  1.00 155.83 ? 396 GLU A OE2   1 
ATOM   3081 N  N     . GLU A 1 397 ? 9.361   -17.516 26.343  1.00 139.76 ? 397 GLU A N     1 
ATOM   3082 C  CA    . GLU A 1 397 ? 8.917   -17.512 24.956  1.00 127.36 ? 397 GLU A CA    1 
ATOM   3083 C  C     . GLU A 1 397 ? 7.412   -17.285 24.890  1.00 118.94 ? 397 GLU A C     1 
ATOM   3084 O  O     . GLU A 1 397 ? 6.636   -18.138 25.341  1.00 118.52 ? 397 GLU A O     1 
ATOM   3085 C  CB    . GLU A 1 397 ? 9.280   -18.832 24.271  1.00 128.83 ? 397 GLU A CB    1 
ATOM   3086 C  CG    . GLU A 1 397 ? 10.764  -19.162 24.268  1.00 132.77 ? 397 GLU A CG    1 
ATOM   3087 C  CD    . GLU A 1 397 ? 11.475  -18.647 23.032  1.00 138.43 ? 397 GLU A CD    1 
ATOM   3088 O  OE1   . GLU A 1 397 ? 10.788  -18.323 22.041  1.00 132.55 ? 397 GLU A OE1   1 
ATOM   3089 O  OE2   . GLU A 1 397 ? 12.722  -18.568 23.052  1.00 142.96 ? 397 GLU A OE2   1 
ATOM   3090 N  N     . PRO A 1 398 ? 6.957   -16.158 24.348  1.00 110.04 ? 398 PRO A N     1 
ATOM   3091 C  CA    . PRO A 1 398 ? 5.514   -15.968 24.163  1.00 102.98 ? 398 PRO A CA    1 
ATOM   3092 C  C     . PRO A 1 398 ? 4.966   -16.946 23.135  1.00 99.05  ? 398 PRO A C     1 
ATOM   3093 O  O     . PRO A 1 398 ? 5.598   -17.220 22.111  1.00 97.52  ? 398 PRO A O     1 
ATOM   3094 C  CB    . PRO A 1 398 ? 5.404   -14.518 23.678  1.00 98.70  ? 398 PRO A CB    1 
ATOM   3095 C  CG    . PRO A 1 398 ? 6.734   -14.226 23.063  1.00 100.05 ? 398 PRO A CG    1 
ATOM   3096 C  CD    . PRO A 1 398 ? 7.736   -15.001 23.874  1.00 112.66 ? 398 PRO A CD    1 
ATOM   3097 N  N     . CYS A 1 399 ? 3.775   -17.479 23.418  1.00 98.07  ? 399 CYS A N     1 
ATOM   3098 C  CA    . CYS A 1 399 ? 3.198   -18.491 22.538  1.00 95.99  ? 399 CYS A CA    1 
ATOM   3099 C  C     . CYS A 1 399 ? 2.691   -17.885 21.236  1.00 80.88  ? 399 CYS A C     1 
ATOM   3100 O  O     . CYS A 1 399 ? 2.637   -18.576 20.213  1.00 76.97  ? 399 CYS A O     1 
ATOM   3101 C  CB    . CYS A 1 399 ? 2.067   -19.233 23.251  1.00 90.90  ? 399 CYS A CB    1 
ATOM   3102 S  SG    . CYS A 1 399 ? 0.520   -18.308 23.365  1.00 85.70  ? 399 CYS A SG    1 
ATOM   3103 N  N     . ALA A 1 400 ? 2.312   -16.610 21.251  1.00 80.78  ? 400 ALA A N     1 
ATOM   3104 C  CA    . ALA A 1 400 ? 1.819   -15.917 20.070  1.00 79.10  ? 400 ALA A CA    1 
ATOM   3105 C  C     . ALA A 1 400 ? 2.773   -14.785 19.726  1.00 76.50  ? 400 ALA A C     1 
ATOM   3106 O  O     . ALA A 1 400 ? 3.079   -13.947 20.581  1.00 81.23  ? 400 ALA A O     1 
ATOM   3107 C  CB    . ALA A 1 400 ? 0.405   -15.377 20.298  1.00 78.62  ? 400 ALA A CB    1 
ATOM   3108 N  N     . HIS A 1 401 ? 3.243   -14.762 18.484  1.00 79.61  ? 401 HIS A N     1 
ATOM   3109 C  CA    . HIS A 1 401 ? 4.194   -13.737 18.089  1.00 67.89  ? 401 HIS A CA    1 
ATOM   3110 C  C     . HIS A 1 401 ? 3.563   -12.356 18.240  1.00 72.16  ? 401 HIS A C     1 
ATOM   3111 O  O     . HIS A 1 401 ? 2.370   -12.183 17.959  1.00 72.31  ? 401 HIS A O     1 
ATOM   3112 C  CB    . HIS A 1 401 ? 4.657   -13.944 16.647  1.00 69.62  ? 401 HIS A CB    1 
ATOM   3113 C  CG    . HIS A 1 401 ? 5.682   -12.948 16.202  1.00 72.80  ? 401 HIS A CG    1 
ATOM   3114 N  ND1   . HIS A 1 401 ? 5.347   -11.748 15.612  1.00 64.53  ? 401 HIS A ND1   1 
ATOM   3115 C  CD2   . HIS A 1 401 ? 7.034   -12.966 16.277  1.00 71.03  ? 401 HIS A CD2   1 
ATOM   3116 C  CE1   . HIS A 1 401 ? 6.449   -11.074 15.335  1.00 67.49  ? 401 HIS A CE1   1 
ATOM   3117 N  NE2   . HIS A 1 401 ? 7.486   -11.791 15.729  1.00 63.32  ? 401 HIS A NE2   1 
ATOM   3118 N  N     . PRO A 1 402 ? 4.328   -11.353 18.682  1.00 72.55  ? 402 PRO A N     1 
ATOM   3119 C  CA    . PRO A 1 402 ? 3.747   -10.016 18.882  1.00 60.48  ? 402 PRO A CA    1 
ATOM   3120 C  C     . PRO A 1 402 ? 2.992   -9.487  17.675  1.00 64.63  ? 402 PRO A C     1 
ATOM   3121 O  O     . PRO A 1 402 ? 1.895   -8.938  17.832  1.00 68.43  ? 402 PRO A O     1 
ATOM   3122 C  CB    . PRO A 1 402 ? 4.976   -9.159  19.208  1.00 66.53  ? 402 PRO A CB    1 
ATOM   3123 C  CG    . PRO A 1 402 ? 5.937   -10.116 19.828  1.00 60.10  ? 402 PRO A CG    1 
ATOM   3124 C  CD    . PRO A 1 402 ? 5.742   -11.411 19.091  1.00 72.62  ? 402 PRO A CD    1 
ATOM   3125 N  N     . ASN A 1 403 ? 3.541   -9.640  16.473  1.00 63.33  ? 403 ASN A N     1 
ATOM   3126 C  CA    . ASN A 1 403 ? 2.885   -9.165  15.264  1.00 67.68  ? 403 ASN A CA    1 
ATOM   3127 C  C     . ASN A 1 403 ? 1.983   -10.218 14.629  1.00 69.45  ? 403 ASN A C     1 
ATOM   3128 O  O     . ASN A 1 403 ? 1.489   -10.003 13.517  1.00 59.42  ? 403 ASN A O     1 
ATOM   3129 C  CB    . ASN A 1 403 ? 3.928   -8.689  14.247  1.00 71.03  ? 403 ASN A CB    1 
ATOM   3130 C  CG    . ASN A 1 403 ? 3.319   -7.857  13.128  1.00 72.84  ? 403 ASN A CG    1 
ATOM   3131 O  OD1   . ASN A 1 403 ? 2.401   -7.068  13.353  1.00 64.00  ? 403 ASN A OD1   1 
ATOM   3132 N  ND2   . ASN A 1 403 ? 3.823   -8.041  11.912  1.00 76.13  ? 403 ASN A ND2   1 
ATOM   3133 N  N     . SER A 1 404 ? 1.760   -11.349 15.303  1.00 66.26  ? 404 SER A N     1 
ATOM   3134 C  CA    . SER A 1 404 ? 0.849   -12.356 14.778  1.00 62.01  ? 404 SER A CA    1 
ATOM   3135 C  C     . SER A 1 404 ? -0.498  -11.719 14.465  1.00 62.52  ? 404 SER A C     1 
ATOM   3136 O  O     . SER A 1 404 ? -0.897  -10.725 15.079  1.00 61.80  ? 404 SER A O     1 
ATOM   3137 C  CB    . SER A 1 404 ? 0.680   -13.506 15.774  1.00 65.63  ? 404 SER A CB    1 
ATOM   3138 O  OG    . SER A 1 404 ? 0.083   -13.061 16.979  1.00 69.00  ? 404 SER A OG    1 
ATOM   3139 N  N     . ARG A 1 405 ? -1.203  -12.292 13.494  1.00 58.69  ? 405 ARG A N     1 
ATOM   3140 C  CA    . ARG A 1 405 ? -2.344  -11.624 12.892  1.00 62.08  ? 405 ARG A CA    1 
ATOM   3141 C  C     . ARG A 1 405 ? -3.525  -12.572 12.756  1.00 56.20  ? 405 ARG A C     1 
ATOM   3142 O  O     . ARG A 1 405 ? -3.386  -13.795 12.821  1.00 57.87  ? 405 ARG A O     1 
ATOM   3143 C  CB    . ARG A 1 405 ? -1.988  -11.066 11.509  1.00 57.81  ? 405 ARG A CB    1 
ATOM   3144 C  CG    . ARG A 1 405 ? -0.912  -10.008 11.532  1.00 56.52  ? 405 ARG A CG    1 
ATOM   3145 C  CD    . ARG A 1 405 ? -1.518  -8.630  11.681  1.00 57.84  ? 405 ARG A CD    1 
ATOM   3146 N  NE    . ARG A 1 405 ? -0.504  -7.623  11.966  1.00 61.75  ? 405 ARG A NE    1 
ATOM   3147 C  CZ    . ARG A 1 405 ? -0.732  -6.318  11.988  1.00 58.38  ? 405 ARG A CZ    1 
ATOM   3148 N  NH1   . ARG A 1 405 ? -1.924  -5.821  11.703  1.00 55.03  ? 405 ARG A NH1   1 
ATOM   3149 N  NH2   . ARG A 1 405 ? 0.260   -5.493  12.306  1.00 62.91  ? 405 ARG A NH2   1 
ATOM   3150 N  N     . PHE A 1 406 ? -4.697  -11.975 12.565  1.00 51.28  ? 406 PHE A N     1 
ATOM   3151 C  CA    . PHE A 1 406 ? -5.869  -12.678 12.075  1.00 50.81  ? 406 PHE A CA    1 
ATOM   3152 C  C     . PHE A 1 406 ? -6.376  -11.949 10.842  1.00 49.78  ? 406 PHE A C     1 
ATOM   3153 O  O     . PHE A 1 406 ? -6.246  -10.728 10.725  1.00 59.32  ? 406 PHE A O     1 
ATOM   3154 C  CB    . PHE A 1 406 ? -6.979  -12.779 13.137  1.00 58.78  ? 406 PHE A CB    1 
ATOM   3155 C  CG    . PHE A 1 406 ? -7.485  -11.449 13.629  1.00 59.46  ? 406 PHE A CG    1 
ATOM   3156 C  CD1   . PHE A 1 406 ? -8.489  -10.779 12.948  1.00 55.25  ? 406 PHE A CD1   1 
ATOM   3157 C  CD2   . PHE A 1 406 ? -6.970  -10.881 14.783  1.00 56.45  ? 406 PHE A CD2   1 
ATOM   3158 C  CE1   . PHE A 1 406 ? -8.960  -9.560  13.401  1.00 53.71  ? 406 PHE A CE1   1 
ATOM   3159 C  CE2   . PHE A 1 406 ? -7.438  -9.661  15.243  1.00 60.87  ? 406 PHE A CE2   1 
ATOM   3160 C  CZ    . PHE A 1 406 ? -8.434  -9.000  14.552  1.00 57.15  ? 406 PHE A CZ    1 
ATOM   3161 N  N     . CYS A 1 407 ? -6.942  -12.708 9.914   1.00 46.53  ? 407 CYS A N     1 
ATOM   3162 C  CA    . CYS A 1 407 ? -7.404  -12.174 8.636   1.00 48.75  ? 407 CYS A CA    1 
ATOM   3163 C  C     . CYS A 1 407 ? -8.848  -12.626 8.462   1.00 46.64  ? 407 CYS A C     1 
ATOM   3164 O  O     . CYS A 1 407 ? -9.101  -13.780 8.108   1.00 49.73  ? 407 CYS A O     1 
ATOM   3165 C  CB    . CYS A 1 407 ? -6.513  -12.655 7.492   1.00 53.15  ? 407 CYS A CB    1 
ATOM   3166 S  SG    . CYS A 1 407 ? -7.031  -12.135 5.844   1.00 53.10  ? 407 CYS A SG    1 
ATOM   3167 N  N     . THR A 1 408 ? -9.792  -11.724 8.710   1.00 48.29  ? 408 THR A N     1 
ATOM   3168 C  CA    . THR A 1 408 ? -11.194 -12.101 8.767   1.00 49.85  ? 408 THR A CA    1 
ATOM   3169 C  C     . THR A 1 408 ? -12.029 -11.252 7.819   1.00 51.84  ? 408 THR A C     1 
ATOM   3170 O  O     . THR A 1 408 ? -11.747 -10.064 7.626   1.00 54.63  ? 408 THR A O     1 
ATOM   3171 C  CB    . THR A 1 408 ? -11.741 -11.955 10.195  1.00 52.25  ? 408 THR A CB    1 
ATOM   3172 O  OG1   . THR A 1 408 ? -13.014 -12.605 10.289  1.00 58.63  ? 408 THR A OG1   1 
ATOM   3173 C  CG2   . THR A 1 408 ? -11.902 -10.483 10.558  1.00 48.16  ? 408 THR A CG2   1 
ATOM   3174 N  N     . PRO A 1 409 ? -13.069 -11.836 7.221   1.00 48.06  ? 409 PRO A N     1 
ATOM   3175 C  CA    . PRO A 1 409 ? -13.954 -11.054 6.347   1.00 50.29  ? 409 PRO A CA    1 
ATOM   3176 C  C     . PRO A 1 409 ? -14.643 -9.928  7.106   1.00 61.75  ? 409 PRO A C     1 
ATOM   3177 O  O     . PRO A 1 409 ? -15.108 -10.103 8.235   1.00 55.13  ? 409 PRO A O     1 
ATOM   3178 C  CB    . PRO A 1 409 ? -14.966 -12.092 5.848   1.00 56.93  ? 409 PRO A CB    1 
ATOM   3179 C  CG    . PRO A 1 409 ? -14.275 -13.410 6.008   1.00 51.22  ? 409 PRO A CG    1 
ATOM   3180 C  CD    . PRO A 1 409 ? -13.425 -13.263 7.235   1.00 55.41  ? 409 PRO A CD    1 
ATOM   3181 N  N     . ALA A 1 410 ? -14.714 -8.759  6.462   1.00 54.87  ? 410 ALA A N     1 
ATOM   3182 C  CA    . ALA A 1 410 ? -15.350 -7.610  7.096   1.00 61.28  ? 410 ALA A CA    1 
ATOM   3183 C  C     . ALA A 1 410 ? -16.841 -7.837  7.303   1.00 63.03  ? 410 ALA A C     1 
ATOM   3184 O  O     . ALA A 1 410 ? -17.402 -7.380  8.306   1.00 61.57  ? 410 ALA A O     1 
ATOM   3185 C  CB    . ALA A 1 410 ? -15.119 -6.349  6.262   1.00 57.88  ? 410 ALA A CB    1 
ATOM   3186 N  N     . SER A 1 411 ? -17.493 -8.548  6.381   1.00 58.78  ? 411 SER A N     1 
ATOM   3187 C  CA    . SER A 1 411 ? -18.941 -8.708  6.458   1.00 64.90  ? 411 SER A CA    1 
ATOM   3188 C  C     . SER A 1 411 ? -19.370 -9.421  7.735   1.00 66.48  ? 411 SER A C     1 
ATOM   3189 O  O     . SER A 1 411 ? -20.474 -9.181  8.236   1.00 66.70  ? 411 SER A O     1 
ATOM   3190 C  CB    . SER A 1 411 ? -19.449 -9.469  5.234   1.00 60.92  ? 411 SER A CB    1 
ATOM   3191 O  OG    . SER A 1 411 ? -18.867 -10.758 5.167   1.00 67.02  ? 411 SER A OG    1 
ATOM   3192 N  N     . GLN A 1 412 ? -18.521 -10.299 8.273   1.00 67.63  ? 412 GLN A N     1 
ATOM   3193 C  CA    . GLN A 1 412 ? -18.883 -11.056 9.464   1.00 66.30  ? 412 GLN A CA    1 
ATOM   3194 C  C     . GLN A 1 412 ? -18.884 -10.212 10.730  1.00 68.55  ? 412 GLN A C     1 
ATOM   3195 O  O     . GLN A 1 412 ? -19.431 -10.659 11.744  1.00 68.88  ? 412 GLN A O     1 
ATOM   3196 C  CB    . GLN A 1 412 ? -17.935 -12.239 9.645   1.00 59.35  ? 412 GLN A CB    1 
ATOM   3197 C  CG    . GLN A 1 412 ? -18.083 -13.307 8.589   1.00 61.30  ? 412 GLN A CG    1 
ATOM   3198 C  CD    . GLN A 1 412 ? -17.004 -14.359 8.684   1.00 58.55  ? 412 GLN A CD    1 
ATOM   3199 O  OE1   . GLN A 1 412 ? -16.998 -15.324 7.923   1.00 67.29  ? 412 GLN A OE1   1 
ATOM   3200 N  NE2   . GLN A 1 412 ? -16.079 -14.178 9.621   1.00 55.60  ? 412 GLN A NE2   1 
ATOM   3201 N  N     . CYS A 1 413 ? -18.289 -9.026  10.704  1.00 66.19  ? 413 CYS A N     1 
ATOM   3202 C  CA    . CYS A 1 413 ? -18.289 -8.175  11.884  1.00 64.11  ? 413 CYS A CA    1 
ATOM   3203 C  C     . CYS A 1 413 ? -19.727 -7.902  12.313  1.00 70.83  ? 413 CYS A C     1 
ATOM   3204 O  O     . CYS A 1 413 ? -20.561 -7.541  11.470  1.00 70.98  ? 413 CYS A O     1 
ATOM   3205 C  CB    . CYS A 1 413 ? -17.563 -6.861  11.604  1.00 69.76  ? 413 CYS A CB    1 
ATOM   3206 S  SG    . CYS A 1 413 ? -17.269 -5.838  13.067  1.00 70.39  ? 413 CYS A SG    1 
ATOM   3207 N  N     . PRO A 1 414 ? -20.064 -8.074  13.595  1.00 71.70  ? 414 PRO A N     1 
ATOM   3208 C  CA    . PRO A 1 414 ? -21.454 -7.845  14.021  1.00 72.40  ? 414 PRO A CA    1 
ATOM   3209 C  C     . PRO A 1 414 ? -21.853 -6.378  14.038  1.00 69.56  ? 414 PRO A C     1 
ATOM   3210 O  O     . PRO A 1 414 ? -23.052 -6.083  13.953  1.00 66.94  ? 414 PRO A O     1 
ATOM   3211 C  CB    . PRO A 1 414 ? -21.495 -8.454  15.429  1.00 69.03  ? 414 PRO A CB    1 
ATOM   3212 C  CG    . PRO A 1 414 ? -20.090 -8.353  15.915  1.00 75.47  ? 414 PRO A CG    1 
ATOM   3213 C  CD    . PRO A 1 414 ? -19.208 -8.528  14.705  1.00 69.03  ? 414 PRO A CD    1 
ATOM   3214 N  N     . ILE A 1 415 ? -20.901 -5.456  14.141  1.00 69.38  ? 415 ILE A N     1 
ATOM   3215 C  CA    . ILE A 1 415 ? -21.190 -4.028  14.132  1.00 67.48  ? 415 ILE A CA    1 
ATOM   3216 C  C     . ILE A 1 415 ? -20.694 -3.368  12.845  1.00 69.15  ? 415 ILE A C     1 
ATOM   3217 O  O     . ILE A 1 415 ? -20.448 -2.163  12.823  1.00 68.24  ? 415 ILE A O     1 
ATOM   3218 C  CB    . ILE A 1 415 ? -20.612 -3.330  15.374  1.00 67.24  ? 415 ILE A CB    1 
ATOM   3219 C  CG1   . ILE A 1 415 ? -19.113 -3.615  15.504  1.00 73.83  ? 415 ILE A CG1   1 
ATOM   3220 C  CG2   . ILE A 1 415 ? -21.356 -3.766  16.625  1.00 65.25  ? 415 ILE A CG2   1 
ATOM   3221 C  CD1   . ILE A 1 415 ? -18.446 -2.875  16.648  1.00 69.17  ? 415 ILE A CD1   1 
ATOM   3222 N  N     . ILE A 1 416 ? -20.538 -4.144  11.769  1.00 68.89  ? 416 ILE A N     1 
ATOM   3223 C  CA    . ILE A 1 416 ? -20.168 -3.564  10.484  1.00 68.28  ? 416 ILE A CA    1 
ATOM   3224 C  C     . ILE A 1 416 ? -21.227 -2.552  10.076  1.00 68.76  ? 416 ILE A C     1 
ATOM   3225 O  O     . ILE A 1 416 ? -22.431 -2.835  10.113  1.00 68.54  ? 416 ILE A O     1 
ATOM   3226 C  CB    . ILE A 1 416 ? -20.001 -4.663  9.424   1.00 60.36  ? 416 ILE A CB    1 
ATOM   3227 C  CG1   . ILE A 1 416 ? -19.280 -4.116  8.191   1.00 61.53  ? 416 ILE A CG1   1 
ATOM   3228 C  CG2   . ILE A 1 416 ? -21.352 -5.223  9.026   1.00 62.83  ? 416 ILE A CG2   1 
ATOM   3229 C  CD1   . ILE A 1 416 ? -17.829 -3.765  8.438   1.00 56.15  ? 416 ILE A CD1   1 
ATOM   3230 N  N     . ASP A 1 417 ? -20.785 -1.363  9.689   1.00 66.01  ? 417 ASP A N     1 
ATOM   3231 C  CA    . ASP A 1 417 ? -21.731 -0.301  9.389   1.00 71.80  ? 417 ASP A CA    1 
ATOM   3232 C  C     . ASP A 1 417 ? -22.588 -0.688  8.187   1.00 71.09  ? 417 ASP A C     1 
ATOM   3233 O  O     . ASP A 1 417 ? -22.080 -1.272  7.222   1.00 72.24  ? 417 ASP A O     1 
ATOM   3234 C  CB    . ASP A 1 417 ? -21.001 1.012   9.112   1.00 67.20  ? 417 ASP A CB    1 
ATOM   3235 C  CG    . ASP A 1 417 ? -21.950 2.187   9.006   1.00 69.41  ? 417 ASP A CG    1 
ATOM   3236 O  OD1   . ASP A 1 417 ? -22.464 2.632   10.053  1.00 65.94  ? 417 ASP A OD1   1 
ATOM   3237 O  OD2   . ASP A 1 417 ? -22.190 2.658   7.875   1.00 73.31  ? 417 ASP A OD2   1 
ATOM   3238 N  N     . PRO A 1 418 ? -23.887 -0.371  8.202   1.00 74.00  ? 418 PRO A N     1 
ATOM   3239 C  CA    . PRO A 1 418 ? -24.748 -0.720  7.064   1.00 78.46  ? 418 PRO A CA    1 
ATOM   3240 C  C     . PRO A 1 418 ? -24.460 0.105   5.817   1.00 79.95  ? 418 PRO A C     1 
ATOM   3241 O  O     . PRO A 1 418 ? -25.304 0.198   4.920   1.00 89.67  ? 418 PRO A O     1 
ATOM   3242 C  CB    . PRO A 1 418 ? -26.160 -0.450  7.600   1.00 72.74  ? 418 PRO A CB    1 
ATOM   3243 C  CG    . PRO A 1 418 ? -25.965 0.586   8.654   1.00 72.13  ? 418 PRO A CG    1 
ATOM   3244 C  CD    . PRO A 1 418 ? -24.637 0.280   9.290   1.00 73.32  ? 418 PRO A CD    1 
ATOM   3245 N  N     . ALA A 1 419 ? -23.270 0.713   5.749   1.00 75.49  ? 419 ALA A N     1 
ATOM   3246 C  CA    . ALA A 1 419 ? -22.879 1.481   4.574   1.00 72.24  ? 419 ALA A CA    1 
ATOM   3247 C  C     . ALA A 1 419 ? -21.391 1.342   4.272   1.00 73.43  ? 419 ALA A C     1 
ATOM   3248 O  O     . ALA A 1 419 ? -20.843 2.161   3.524   1.00 78.68  ? 419 ALA A O     1 
ATOM   3249 C  CB    . ALA A 1 419 ? -23.230 2.963   4.739   1.00 77.54  ? 419 ALA A CB    1 
ATOM   3250 N  N     . TRP A 1 420 ? -20.723 0.330   4.832   1.00 69.93  ? 420 TRP A N     1 
ATOM   3251 C  CA    . TRP A 1 420 ? -19.294 0.163   4.593   1.00 71.29  ? 420 TRP A CA    1 
ATOM   3252 C  C     . TRP A 1 420 ? -18.987 -0.190  3.145   1.00 64.08  ? 420 TRP A C     1 
ATOM   3253 O  O     . TRP A 1 420 ? -17.852 0.009   2.701   1.00 67.33  ? 420 TRP A O     1 
ATOM   3254 C  CB    . TRP A 1 420 ? -18.720 -0.906  5.525   1.00 71.32  ? 420 TRP A CB    1 
ATOM   3255 C  CG    . TRP A 1 420 ? -19.028 -2.315  5.111   1.00 73.38  ? 420 TRP A CG    1 
ATOM   3256 C  CD1   . TRP A 1 420 ? -20.201 -2.986  5.295   1.00 68.45  ? 420 TRP A CD1   1 
ATOM   3257 C  CD2   . TRP A 1 420 ? -18.140 -3.230  4.455   1.00 68.01  ? 420 TRP A CD2   1 
ATOM   3258 N  NE1   . TRP A 1 420 ? -20.101 -4.260  4.788   1.00 68.86  ? 420 TRP A NE1   1 
ATOM   3259 C  CE2   . TRP A 1 420 ? -18.846 -4.435  4.268   1.00 67.77  ? 420 TRP A CE2   1 
ATOM   3260 C  CE3   . TRP A 1 420 ? -16.818 -3.145  4.006   1.00 67.04  ? 420 TRP A CE3   1 
ATOM   3261 C  CZ2   . TRP A 1 420 ? -18.275 -5.548  3.650   1.00 68.86  ? 420 TRP A CZ2   1 
ATOM   3262 C  CZ3   . TRP A 1 420 ? -16.252 -4.251  3.392   1.00 67.49  ? 420 TRP A CZ3   1 
ATOM   3263 C  CH2   . TRP A 1 420 ? -16.980 -5.436  3.220   1.00 66.15  ? 420 TRP A CH2   1 
ATOM   3264 N  N     . GLU A 1 421 ? -19.963 -0.712  2.404   1.00 69.77  ? 421 GLU A N     1 
ATOM   3265 C  CA    . GLU A 1 421 ? -19.803 -0.991  0.984   1.00 69.22  ? 421 GLU A CA    1 
ATOM   3266 C  C     . GLU A 1 421 ? -20.583 -0.015  0.116   1.00 73.70  ? 421 GLU A C     1 
ATOM   3267 O  O     . GLU A 1 421 ? -20.672 -0.213  -1.100  1.00 76.70  ? 421 GLU A O     1 
ATOM   3268 C  CB    . GLU A 1 421 ? -20.223 -2.428  0.670   1.00 67.92  ? 421 GLU A CB    1 
ATOM   3269 C  CG    . GLU A 1 421 ? -19.276 -3.473  1.226   1.00 72.86  ? 421 GLU A CG    1 
ATOM   3270 C  CD    . GLU A 1 421 ? -19.608 -4.878  0.761   1.00 74.71  ? 421 GLU A CD    1 
ATOM   3271 O  OE1   . GLU A 1 421 ? -20.808 -5.187  0.609   1.00 70.48  ? 421 GLU A OE1   1 
ATOM   3272 O  OE2   . GLU A 1 421 ? -18.666 -5.670  0.543   1.00 74.40  ? 421 GLU A OE2   1 
ATOM   3273 N  N     . SER A 1 422 ? -21.150 1.025   0.708   1.00 75.48  ? 422 SER A N     1 
ATOM   3274 C  CA    . SER A 1 422 ? -21.857 2.037   -0.062  1.00 82.38  ? 422 SER A CA    1 
ATOM   3275 C  C     . SER A 1 422 ? -20.872 2.759   -0.971  1.00 82.80  ? 422 SER A C     1 
ATOM   3276 O  O     . SER A 1 422 ? -19.929 3.388   -0.472  1.00 81.71  ? 422 SER A O     1 
ATOM   3277 C  CB    . SER A 1 422 ? -22.551 3.024   0.872   1.00 80.94  ? 422 SER A CB    1 
ATOM   3278 O  OG    . SER A 1 422 ? -23.464 2.357   1.727   1.00 84.20  ? 422 SER A OG    1 
ATOM   3279 N  N     . PRO A 1 423 ? -21.042 2.701   -2.294  1.00 86.38  ? 423 PRO A N     1 
ATOM   3280 C  CA    . PRO A 1 423 ? -20.048 3.313   -3.189  1.00 87.18  ? 423 PRO A CA    1 
ATOM   3281 C  C     . PRO A 1 423 ? -19.946 4.820   -3.050  1.00 88.29  ? 423 PRO A C     1 
ATOM   3282 O  O     . PRO A 1 423 ? -18.980 5.401   -3.560  1.00 93.92  ? 423 PRO A O     1 
ATOM   3283 C  CB    . PRO A 1 423 ? -20.544 2.918   -4.586  1.00 88.77  ? 423 PRO A CB    1 
ATOM   3284 C  CG    . PRO A 1 423 ? -22.014 2.718   -4.411  1.00 85.75  ? 423 PRO A CG    1 
ATOM   3285 C  CD    . PRO A 1 423 ? -22.178 2.130   -3.036  1.00 84.15  ? 423 PRO A CD    1 
ATOM   3286 N  N     . GLU A 1 424 ? -20.895 5.472   -2.382  1.00 90.90  ? 424 GLU A N     1 
ATOM   3287 C  CA    . GLU A 1 424 ? -20.856 6.920   -2.230  1.00 90.47  ? 424 GLU A CA    1 
ATOM   3288 C  C     . GLU A 1 424 ? -20.064 7.371   -1.010  1.00 83.73  ? 424 GLU A C     1 
ATOM   3289 O  O     . GLU A 1 424 ? -19.859 8.577   -0.838  1.00 83.78  ? 424 GLU A O     1 
ATOM   3290 C  CB    . GLU A 1 424 ? -22.278 7.489   -2.153  1.00 93.75  ? 424 GLU A CB    1 
ATOM   3291 C  CG    . GLU A 1 424 ? -22.878 7.533   -0.752  1.00 99.56  ? 424 GLU A CG    1 
ATOM   3292 C  CD    . GLU A 1 424 ? -23.348 6.179   -0.258  1.00 102.36 ? 424 GLU A CD    1 
ATOM   3293 O  OE1   . GLU A 1 424 ? -23.107 5.169   -0.954  1.00 97.91  ? 424 GLU A OE1   1 
ATOM   3294 O  OE2   . GLU A 1 424 ? -23.965 6.130   0.829   1.00 100.47 ? 424 GLU A OE2   1 
ATOM   3295 N  N     . GLY A 1 425 ? -19.612 6.445   -0.169  1.00 81.51  ? 425 GLY A N     1 
ATOM   3296 C  CA    . GLY A 1 425 ? -18.865 6.806   1.016   1.00 69.77  ? 425 GLY A CA    1 
ATOM   3297 C  C     . GLY A 1 425 ? -19.764 7.276   2.142   1.00 76.29  ? 425 GLY A C     1 
ATOM   3298 O  O     . GLY A 1 425 ? -20.991 7.319   2.040   1.00 80.00  ? 425 GLY A O     1 
ATOM   3299 N  N     . VAL A 1 426 ? -19.124 7.635   3.251   1.00 69.56  ? 426 VAL A N     1 
ATOM   3300 C  CA    . VAL A 1 426 ? -19.801 8.136   4.438   1.00 68.34  ? 426 VAL A CA    1 
ATOM   3301 C  C     . VAL A 1 426 ? -19.264 9.533   4.729   1.00 70.71  ? 426 VAL A C     1 
ATOM   3302 O  O     . VAL A 1 426 ? -18.049 9.735   4.687   1.00 65.13  ? 426 VAL A O     1 
ATOM   3303 C  CB    . VAL A 1 426 ? -19.604 7.220   5.659   1.00 61.70  ? 426 VAL A CB    1 
ATOM   3304 C  CG1   . VAL A 1 426 ? -20.428 5.954   5.501   1.00 62.40  ? 426 VAL A CG1   1 
ATOM   3305 C  CG2   . VAL A 1 426 ? -18.133 6.878   5.833   1.00 58.64  ? 426 VAL A CG2   1 
ATOM   3306 N  N     . PRO A 1 427 ? -20.119 10.513  5.017   1.00 68.19  ? 427 PRO A N     1 
ATOM   3307 C  CA    . PRO A 1 427 ? -19.628 11.876  5.273   1.00 65.71  ? 427 PRO A CA    1 
ATOM   3308 C  C     . PRO A 1 427 ? -18.871 11.937  6.591   1.00 64.65  ? 427 PRO A C     1 
ATOM   3309 O  O     . PRO A 1 427 ? -19.435 11.686  7.658   1.00 69.37  ? 427 PRO A O     1 
ATOM   3310 C  CB    . PRO A 1 427 ? -20.912 12.712  5.316   1.00 69.32  ? 427 PRO A CB    1 
ATOM   3311 C  CG    . PRO A 1 427 ? -21.964 11.744  5.740   1.00 70.82  ? 427 PRO A CG    1 
ATOM   3312 C  CD    . PRO A 1 427 ? -21.585 10.422  5.132   1.00 69.21  ? 427 PRO A CD    1 
ATOM   3313 N  N     . ILE A 1 428 ? -17.587 12.267  6.510   1.00 60.24  ? 428 ILE A N     1 
ATOM   3314 C  CA    . ILE A 1 428 ? -16.746 12.377  7.696   1.00 58.43  ? 428 ILE A CA    1 
ATOM   3315 C  C     . ILE A 1 428 ? -16.926 13.764  8.297   1.00 61.49  ? 428 ILE A C     1 
ATOM   3316 O  O     . ILE A 1 428 ? -16.690 14.776  7.629   1.00 63.03  ? 428 ILE A O     1 
ATOM   3317 C  CB    . ILE A 1 428 ? -15.273 12.112  7.358   1.00 54.71  ? 428 ILE A CB    1 
ATOM   3318 C  CG1   . ILE A 1 428 ? -15.079 10.662  6.909   1.00 62.89  ? 428 ILE A CG1   1 
ATOM   3319 C  CG2   . ILE A 1 428 ? -14.392 12.442  8.549   1.00 50.49  ? 428 ILE A CG2   1 
ATOM   3320 C  CD1   . ILE A 1 428 ? -15.492 9.636   7.943   1.00 58.51  ? 428 ILE A CD1   1 
ATOM   3321 N  N     . GLU A 1 429 ? -17.342 13.815  9.562   1.00 59.61  ? 429 GLU A N     1 
ATOM   3322 C  CA    . GLU A 1 429 ? -17.503 15.073  10.274  1.00 51.81  ? 429 GLU A CA    1 
ATOM   3323 C  C     . GLU A 1 429 ? -16.419 15.310  11.314  1.00 54.59  ? 429 GLU A C     1 
ATOM   3324 O  O     . GLU A 1 429 ? -16.448 16.340  11.996  1.00 56.36  ? 429 GLU A O     1 
ATOM   3325 C  CB    . GLU A 1 429 ? -18.879 15.133  10.943  1.00 50.03  ? 429 GLU A CB    1 
ATOM   3326 C  CG    . GLU A 1 429 ? -20.037 15.038  9.970   1.00 58.26  ? 429 GLU A CG    1 
ATOM   3327 C  CD    . GLU A 1 429 ? -21.375 15.206  10.650  1.00 61.31  ? 429 GLU A CD    1 
ATOM   3328 O  OE1   . GLU A 1 429 ? -21.391 15.640  11.820  1.00 66.08  ? 429 GLU A OE1   1 
ATOM   3329 O  OE2   . GLU A 1 429 ? -22.407 14.904  10.017  1.00 68.23  ? 429 GLU A OE2   1 
ATOM   3330 N  N     . GLY A 1 430 ? -15.466 14.395  11.453  1.00 49.99  ? 430 GLY A N     1 
ATOM   3331 C  CA    . GLY A 1 430 ? -14.405 14.561  12.426  1.00 47.47  ? 430 GLY A CA    1 
ATOM   3332 C  C     . GLY A 1 430 ? -13.196 13.746  12.041  1.00 49.42  ? 430 GLY A C     1 
ATOM   3333 O  O     . GLY A 1 430 ? -13.309 12.720  11.363  1.00 54.40  ? 430 GLY A O     1 
ATOM   3334 N  N     . ILE A 1 431 ? -12.028 14.207  12.479  1.00 39.19  ? 431 ILE A N     1 
ATOM   3335 C  CA    . ILE A 1 431 ? -10.767 13.526  12.216  1.00 42.79  ? 431 ILE A CA    1 
ATOM   3336 C  C     . ILE A 1 431 ? -9.967  13.499  13.508  1.00 44.29  ? 431 ILE A C     1 
ATOM   3337 O  O     . ILE A 1 431 ? -9.825  14.526  14.179  1.00 43.97  ? 431 ILE A O     1 
ATOM   3338 C  CB    . ILE A 1 431 ? -9.966  14.210  11.092  1.00 47.48  ? 431 ILE A CB    1 
ATOM   3339 C  CG1   . ILE A 1 431 ? -10.722 14.106  9.766   1.00 46.62  ? 431 ILE A CG1   1 
ATOM   3340 C  CG2   . ILE A 1 431 ? -8.579  13.602  10.977  1.00 45.76  ? 431 ILE A CG2   1 
ATOM   3341 C  CD1   . ILE A 1 431 ? -10.000 14.766  8.606   1.00 55.05  ? 431 ILE A CD1   1 
ATOM   3342 N  N     . ILE A 1 432 ? -9.443  12.330  13.858  1.00 46.65  ? 432 ILE A N     1 
ATOM   3343 C  CA    . ILE A 1 432 ? -8.789  12.116  15.141  1.00 48.85  ? 432 ILE A CA    1 
ATOM   3344 C  C     . ILE A 1 432 ? -7.350  11.704  14.885  1.00 45.20  ? 432 ILE A C     1 
ATOM   3345 O  O     . ILE A 1 432 ? -7.092  10.812  14.070  1.00 50.53  ? 432 ILE A O     1 
ATOM   3346 C  CB    . ILE A 1 432 ? -9.520  11.050  15.976  1.00 44.00  ? 432 ILE A CB    1 
ATOM   3347 C  CG1   . ILE A 1 432 ? -11.017 11.357  16.028  1.00 39.45  ? 432 ILE A CG1   1 
ATOM   3348 C  CG2   . ILE A 1 432 ? -8.936  10.990  17.377  1.00 45.52  ? 432 ILE A CG2   1 
ATOM   3349 C  CD1   . ILE A 1 432 ? -11.849 10.256  16.648  1.00 51.98  ? 432 ILE A CD1   1 
ATOM   3350 N  N     . PHE A 1 433 ? -6.420  12.362  15.568  1.00 40.83  ? 433 PHE A N     1 
ATOM   3351 C  CA    . PHE A 1 433 ? -5.017  11.984  15.575  1.00 41.59  ? 433 PHE A CA    1 
ATOM   3352 C  C     . PHE A 1 433 ? -4.631  11.526  16.971  1.00 48.99  ? 433 PHE A C     1 
ATOM   3353 O  O     . PHE A 1 433 ? -5.260  11.899  17.962  1.00 49.71  ? 433 PHE A O     1 
ATOM   3354 C  CB    . PHE A 1 433 ? -4.111  13.148  15.153  1.00 42.67  ? 433 PHE A CB    1 
ATOM   3355 C  CG    . PHE A 1 433 ? -4.343  13.630  13.751  1.00 48.36  ? 433 PHE A CG    1 
ATOM   3356 C  CD1   . PHE A 1 433 ? -4.144  12.786  12.669  1.00 54.66  ? 433 PHE A CD1   1 
ATOM   3357 C  CD2   . PHE A 1 433 ? -4.731  14.937  13.512  1.00 45.62  ? 433 PHE A CD2   1 
ATOM   3358 C  CE1   . PHE A 1 433 ? -4.351  13.234  11.375  1.00 50.56  ? 433 PHE A CE1   1 
ATOM   3359 C  CE2   . PHE A 1 433 ? -4.937  15.388  12.224  1.00 47.59  ? 433 PHE A CE2   1 
ATOM   3360 C  CZ    . PHE A 1 433 ? -4.748  14.538  11.154  1.00 45.27  ? 433 PHE A CZ    1 
ATOM   3361 N  N     . GLY A 1 434 ? -3.582  10.720  17.042  1.00 51.21  ? 434 GLY A N     1 
ATOM   3362 C  CA    . GLY A 1 434 ? -3.100  10.264  18.328  1.00 47.35  ? 434 GLY A CA    1 
ATOM   3363 C  C     . GLY A 1 434 ? -2.020  9.224   18.171  1.00 49.07  ? 434 GLY A C     1 
ATOM   3364 O  O     . GLY A 1 434 ? -1.803  8.662   17.094  1.00 51.81  ? 434 GLY A O     1 
ATOM   3365 N  N     . GLY A 1 435 ? -1.340  8.983   19.277  1.00 50.29  ? 435 GLY A N     1 
ATOM   3366 C  CA    . GLY A 1 435 ? -0.335  7.953   19.346  1.00 54.44  ? 435 GLY A CA    1 
ATOM   3367 C  C     . GLY A 1 435 ? -0.121  7.544   20.782  1.00 55.13  ? 435 GLY A C     1 
ATOM   3368 O  O     . GLY A 1 435 ? -0.945  7.819   21.655  1.00 51.13  ? 435 GLY A O     1 
ATOM   3369 N  N     . ARG A 1 436 ? 1.009   6.889   21.026  1.00 48.69  ? 436 ARG A N     1 
ATOM   3370 C  CA    . ARG A 1 436 ? 1.370   6.433   22.366  1.00 57.23  ? 436 ARG A CA    1 
ATOM   3371 C  C     . ARG A 1 436 ? 2.327   7.452   22.976  1.00 60.24  ? 436 ARG A C     1 
ATOM   3372 O  O     . ARG A 1 436 ? 3.544   7.372   22.810  1.00 63.87  ? 436 ARG A O     1 
ATOM   3373 C  CB    . ARG A 1 436 ? 1.974   5.034   22.321  1.00 69.76  ? 436 ARG A CB    1 
ATOM   3374 C  CG    . ARG A 1 436 ? 0.950   3.941   22.076  1.00 66.55  ? 436 ARG A CG    1 
ATOM   3375 C  CD    . ARG A 1 436 ? 1.597   2.598   21.816  1.00 58.43  ? 436 ARG A CD    1 
ATOM   3376 N  NE    . ARG A 1 436 ? 0.584   1.581   21.570  1.00 71.07  ? 436 ARG A NE    1 
ATOM   3377 C  CZ    . ARG A 1 436 ? 0.083   0.784   22.503  1.00 66.33  ? 436 ARG A CZ    1 
ATOM   3378 N  NH1   . ARG A 1 436 ? 0.519   0.821   23.752  1.00 58.96  ? 436 ARG A NH1   1 
ATOM   3379 N  NH2   . ARG A 1 436 ? -0.879  -0.073  22.174  1.00 65.41  ? 436 ARG A NH2   1 
ATOM   3380 N  N     . ARG A 1 437 ? 1.762   8.426   23.684  1.00 61.70  ? 437 ARG A N     1 
ATOM   3381 C  CA    . ARG A 1 437 ? 2.560   9.387   24.434  1.00 58.15  ? 437 ARG A CA    1 
ATOM   3382 C  C     . ARG A 1 437 ? 2.490   9.028   25.910  1.00 63.38  ? 437 ARG A C     1 
ATOM   3383 O  O     . ARG A 1 437 ? 1.445   9.239   26.546  1.00 57.15  ? 437 ARG A O     1 
ATOM   3384 C  CB    . ARG A 1 437 ? 2.073   10.820  24.208  1.00 54.05  ? 437 ARG A CB    1 
ATOM   3385 C  CG    . ARG A 1 437 ? 2.247   11.329  22.781  1.00 54.32  ? 437 ARG A CG    1 
ATOM   3386 C  CD    . ARG A 1 437 ? 3.662   11.102  22.266  1.00 54.41  ? 437 ARG A CD    1 
ATOM   3387 N  NE    . ARG A 1 437 ? 4.681   11.752  23.084  1.00 59.04  ? 437 ARG A NE    1 
ATOM   3388 C  CZ    . ARG A 1 437 ? 5.201   12.945  22.824  1.00 56.13  ? 437 ARG A CZ    1 
ATOM   3389 N  NH1   . ARG A 1 437 ? 4.797   13.663  21.789  1.00 41.91  ? 437 ARG A NH1   1 
ATOM   3390 N  NH2   . ARG A 1 437 ? 6.152   13.427  23.621  1.00 47.38  ? 437 ARG A NH2   1 
ATOM   3391 N  N     . PRO A 1 438 ? 3.555   8.474   26.489  1.00 58.32  ? 438 PRO A N     1 
ATOM   3392 C  CA    . PRO A 1 438 ? 3.507   8.110   27.915  1.00 68.31  ? 438 PRO A CA    1 
ATOM   3393 C  C     . PRO A 1 438 ? 3.342   9.298   28.846  1.00 70.72  ? 438 PRO A C     1 
ATOM   3394 O  O     . PRO A 1 438 ? 2.874   9.115   29.976  1.00 72.80  ? 438 PRO A O     1 
ATOM   3395 C  CB    . PRO A 1 438 ? 4.852   7.403   28.142  1.00 62.42  ? 438 PRO A CB    1 
ATOM   3396 C  CG    . PRO A 1 438 ? 5.739   7.898   27.031  1.00 57.49  ? 438 PRO A CG    1 
ATOM   3397 C  CD    . PRO A 1 438 ? 4.831   8.100   25.857  1.00 54.72  ? 438 PRO A CD    1 
ATOM   3398 N  N     . ALA A 1 439 ? 3.706   10.505  28.418  1.00 61.71  ? 439 ALA A N     1 
ATOM   3399 C  CA    . ALA A 1 439 ? 3.677   11.657  29.307  1.00 64.59  ? 439 ALA A CA    1 
ATOM   3400 C  C     . ALA A 1 439 ? 3.393   12.917  28.507  1.00 60.10  ? 439 ALA A C     1 
ATOM   3401 O  O     . ALA A 1 439 ? 3.557   12.954  27.285  1.00 62.74  ? 439 ALA A O     1 
ATOM   3402 C  CB    . ALA A 1 439 ? 4.994   11.809  30.078  1.00 64.19  ? 439 ALA A CB    1 
ATOM   3403 N  N     . GLY A 1 440 ? 2.962   13.949  29.219  1.00 67.29  ? 440 GLY A N     1 
ATOM   3404 C  CA    . GLY A 1 440 ? 2.742   15.266  28.627  1.00 58.74  ? 440 GLY A CA    1 
ATOM   3405 C  C     . GLY A 1 440 ? 1.448   15.516  27.887  1.00 63.20  ? 440 GLY A C     1 
ATOM   3406 O  O     . GLY A 1 440 ? 0.758   16.501  28.166  1.00 68.22  ? 440 GLY A O     1 
ATOM   3407 N  N     . VAL A 1 441 ? 1.097   14.647  26.948  1.00 62.60  ? 441 VAL A N     1 
ATOM   3408 C  CA    . VAL A 1 441 ? -0.027  14.918  26.048  1.00 62.39  ? 441 VAL A CA    1 
ATOM   3409 C  C     . VAL A 1 441 ? -1.334  14.647  26.787  1.00 65.07  ? 441 VAL A C     1 
ATOM   3410 O  O     . VAL A 1 441 ? -1.500  13.557  27.358  1.00 62.00  ? 441 VAL A O     1 
ATOM   3411 C  CB    . VAL A 1 441 ? 0.076   14.071  24.786  1.00 58.65  ? 441 VAL A CB    1 
ATOM   3412 C  CG1   . VAL A 1 441 ? -1.001  14.479  23.784  1.00 52.50  ? 441 VAL A CG1   1 
ATOM   3413 C  CG2   . VAL A 1 441 ? 1.463   14.204  24.179  1.00 53.72  ? 441 VAL A CG2   1 
ATOM   3414 N  N     . PRO A 1 442 ? -2.276  15.588  26.789  1.00 65.90  ? 442 PRO A N     1 
ATOM   3415 C  CA    . PRO A 1 442 ? -3.541  15.366  27.491  1.00 66.03  ? 442 PRO A CA    1 
ATOM   3416 C  C     . PRO A 1 442 ? -4.419  14.365  26.756  1.00 56.31  ? 442 PRO A C     1 
ATOM   3417 O  O     . PRO A 1 442 ? -4.205  14.044  25.585  1.00 53.10  ? 442 PRO A O     1 
ATOM   3418 C  CB    . PRO A 1 442 ? -4.180  16.759  27.510  1.00 66.19  ? 442 PRO A CB    1 
ATOM   3419 C  CG    . PRO A 1 442 ? -3.643  17.415  26.284  1.00 55.68  ? 442 PRO A CG    1 
ATOM   3420 C  CD    . PRO A 1 442 ? -2.228  16.910  26.140  1.00 60.26  ? 442 PRO A CD    1 
ATOM   3421 N  N     . LEU A 1 443 ? -5.436  13.882  27.474  1.00 64.95  ? 443 LEU A N     1 
ATOM   3422 C  CA    . LEU A 1 443 ? -6.304  12.838  26.938  1.00 58.97  ? 443 LEU A CA    1 
ATOM   3423 C  C     . LEU A 1 443 ? -6.944  13.237  25.615  1.00 52.50  ? 443 LEU A C     1 
ATOM   3424 O  O     . LEU A 1 443 ? -7.217  12.372  24.777  1.00 60.18  ? 443 LEU A O     1 
ATOM   3425 C  CB    . LEU A 1 443 ? -7.391  12.486  27.952  1.00 56.87  ? 443 LEU A CB    1 
ATOM   3426 C  CG    . LEU A 1 443 ? -8.476  11.558  27.403  1.00 58.22  ? 443 LEU A CG    1 
ATOM   3427 C  CD1   . LEU A 1 443 ? -7.933  10.149  27.198  1.00 60.24  ? 443 LEU A CD1   1 
ATOM   3428 C  CD2   . LEU A 1 443 ? -9.691  11.548  28.310  1.00 64.26  ? 443 LEU A CD2   1 
ATOM   3429 N  N     . VAL A 1 444 ? -7.205  14.525  25.409  1.00 50.57  ? 444 VAL A N     1 
ATOM   3430 C  CA    . VAL A 1 444 ? -7.903  14.956  24.202  1.00 56.09  ? 444 VAL A CA    1 
ATOM   3431 C  C     . VAL A 1 444 ? -7.965  16.476  24.143  1.00 54.88  ? 444 VAL A C     1 
ATOM   3432 O  O     . VAL A 1 444 ? -8.162  17.143  25.165  1.00 59.43  ? 444 VAL A O     1 
ATOM   3433 C  CB    . VAL A 1 444 ? -9.317  14.349  24.142  1.00 45.63  ? 444 VAL A CB    1 
ATOM   3434 C  CG1   . VAL A 1 444 ? -10.171 14.896  25.276  1.00 55.93  ? 444 VAL A CG1   1 
ATOM   3435 C  CG2   . VAL A 1 444 ? -9.968  14.629  22.799  1.00 47.63  ? 444 VAL A CG2   1 
ATOM   3436 N  N     . TYR A 1 445 ? -7.795  17.032  22.947  1.00 48.20  ? 445 TYR A N     1 
ATOM   3437 C  CA    . TYR A 1 445 ? -7.998  18.455  22.726  1.00 54.85  ? 445 TYR A CA    1 
ATOM   3438 C  C     . TYR A 1 445 ? -8.381  18.666  21.270  1.00 47.40  ? 445 TYR A C     1 
ATOM   3439 O  O     . TYR A 1 445 ? -8.232  17.775  20.430  1.00 49.40  ? 445 TYR A O     1 
ATOM   3440 C  CB    . TYR A 1 445 ? -6.761  19.281  23.105  1.00 52.99  ? 445 TYR A CB    1 
ATOM   3441 C  CG    . TYR A 1 445 ? -5.500  18.935  22.351  1.00 53.60  ? 445 TYR A CG    1 
ATOM   3442 C  CD1   . TYR A 1 445 ? -5.238  19.486  21.104  1.00 57.54  ? 445 TYR A CD1   1 
ATOM   3443 C  CD2   . TYR A 1 445 ? -4.557  18.073  22.897  1.00 58.41  ? 445 TYR A CD2   1 
ATOM   3444 C  CE1   . TYR A 1 445 ? -4.077  19.178  20.412  1.00 53.70  ? 445 TYR A CE1   1 
ATOM   3445 C  CE2   . TYR A 1 445 ? -3.395  17.759  22.217  1.00 51.71  ? 445 TYR A CE2   1 
ATOM   3446 C  CZ    . TYR A 1 445 ? -3.159  18.314  20.976  1.00 58.67  ? 445 TYR A CZ    1 
ATOM   3447 O  OH    . TYR A 1 445 ? -2.004  18.002  20.296  1.00 54.55  ? 445 TYR A OH    1 
ATOM   3448 N  N     . GLU A 1 446 ? -8.894  19.857  20.981  1.00 51.78  ? 446 GLU A N     1 
ATOM   3449 C  CA    . GLU A 1 446 ? -9.406  20.195  19.662  1.00 55.43  ? 446 GLU A CA    1 
ATOM   3450 C  C     . GLU A 1 446 ? -8.523  21.250  19.010  1.00 55.67  ? 446 GLU A C     1 
ATOM   3451 O  O     . GLU A 1 446 ? -8.010  22.150  19.684  1.00 54.75  ? 446 GLU A O     1 
ATOM   3452 C  CB    . GLU A 1 446 ? -10.849 20.699  19.752  1.00 50.78  ? 446 GLU A CB    1 
ATOM   3453 C  CG    . GLU A 1 446 ? -11.462 21.068  18.416  1.00 51.29  ? 446 GLU A CG    1 
ATOM   3454 C  CD    . GLU A 1 446 ? -12.883 21.576  18.554  1.00 57.94  ? 446 GLU A CD    1 
ATOM   3455 O  OE1   . GLU A 1 446 ? -13.548 21.217  19.547  1.00 55.88  ? 446 GLU A OE1   1 
ATOM   3456 O  OE2   . GLU A 1 446 ? -13.336 22.339  17.675  1.00 59.30  ? 446 GLU A OE2   1 
ATOM   3457 N  N     . ALA A 1 447 ? -8.344  21.130  17.698  1.00 52.14  ? 447 ALA A N     1 
ATOM   3458 C  CA    . ALA A 1 447 ? -7.544  22.095  16.961  1.00 51.14  ? 447 ALA A CA    1 
ATOM   3459 C  C     . ALA A 1 447 ? -8.265  23.434  16.881  1.00 52.46  ? 447 ALA A C     1 
ATOM   3460 O  O     . ALA A 1 447 ? -9.498  23.502  16.873  1.00 51.84  ? 447 ALA A O     1 
ATOM   3461 C  CB    . ALA A 1 447 ? -7.240  21.579  15.554  1.00 44.66  ? 447 ALA A CB    1 
ATOM   3462 N  N     . LEU A 1 448 ? -7.477  24.511  16.819  1.00 57.12  ? 448 LEU A N     1 
ATOM   3463 C  CA    . LEU A 1 448 ? -8.032  25.858  16.755  1.00 50.75  ? 448 LEU A CA    1 
ATOM   3464 C  C     . LEU A 1 448 ? -8.524  26.222  15.362  1.00 47.65  ? 448 LEU A C     1 
ATOM   3465 O  O     . LEU A 1 448 ? -9.365  27.117  15.230  1.00 50.23  ? 448 LEU A O     1 
ATOM   3466 C  CB    . LEU A 1 448 ? -6.991  26.877  17.220  1.00 40.21  ? 448 LEU A CB    1 
ATOM   3467 C  CG    . LEU A 1 448 ? -6.365  26.542  18.576  1.00 54.14  ? 448 LEU A CG    1 
ATOM   3468 C  CD1   . LEU A 1 448 ? -5.218  27.479  18.910  1.00 52.12  ? 448 LEU A CD1   1 
ATOM   3469 C  CD2   . LEU A 1 448 ? -7.422  26.572  19.668  1.00 58.37  ? 448 LEU A CD2   1 
ATOM   3470 N  N     . SER A 1 449 ? -8.031  25.547  14.330  1.00 48.53  ? 449 SER A N     1 
ATOM   3471 C  CA    . SER A 1 449 ? -8.445  25.796  12.956  1.00 52.15  ? 449 SER A CA    1 
ATOM   3472 C  C     . SER A 1 449 ? -7.859  24.693  12.091  1.00 50.28  ? 449 SER A C     1 
ATOM   3473 O  O     . SER A 1 449 ? -6.987  23.936  12.527  1.00 46.28  ? 449 SER A O     1 
ATOM   3474 C  CB    . SER A 1 449 ? -7.987  27.169  12.462  1.00 47.27  ? 449 SER A CB    1 
ATOM   3475 O  OG    . SER A 1 449 ? -6.571  27.246  12.456  1.00 51.20  ? 449 SER A OG    1 
ATOM   3476 N  N     . TRP A 1 450 ? -8.340  24.620  10.848  1.00 48.92  ? 450 TRP A N     1 
ATOM   3477 C  CA    . TRP A 1 450 ? -7.819  23.633  9.909   1.00 47.88  ? 450 TRP A CA    1 
ATOM   3478 C  C     . TRP A 1 450 ? -6.295  23.634  9.901   1.00 45.89  ? 450 TRP A C     1 
ATOM   3479 O  O     . TRP A 1 450 ? -5.656  22.598  10.109  1.00 47.26  ? 450 TRP A O     1 
ATOM   3480 C  CB    . TRP A 1 450 ? -8.359  23.900  8.507   1.00 48.90  ? 450 TRP A CB    1 
ATOM   3481 C  CG    . TRP A 1 450 ? -7.909  22.872  7.528   1.00 62.05  ? 450 TRP A CG    1 
ATOM   3482 C  CD1   . TRP A 1 450 ? -6.920  23.000  6.595   1.00 62.38  ? 450 TRP A CD1   1 
ATOM   3483 C  CD2   . TRP A 1 450 ? -8.414  21.539  7.398   1.00 66.73  ? 450 TRP A CD2   1 
ATOM   3484 N  NE1   . TRP A 1 450 ? -6.789  21.830  5.882   1.00 61.01  ? 450 TRP A NE1   1 
ATOM   3485 C  CE2   . TRP A 1 450 ? -7.695  20.918  6.357   1.00 61.93  ? 450 TRP A CE2   1 
ATOM   3486 C  CE3   . TRP A 1 450 ? -9.411  20.812  8.058   1.00 63.71  ? 450 TRP A CE3   1 
ATOM   3487 C  CZ2   . TRP A 1 450 ? -7.940  19.606  5.961   1.00 60.36  ? 450 TRP A CZ2   1 
ATOM   3488 C  CZ3   . TRP A 1 450 ? -9.653  19.510  7.663   1.00 59.55  ? 450 TRP A CZ3   1 
ATOM   3489 C  CH2   . TRP A 1 450 ? -8.921  18.921  6.625   1.00 62.91  ? 450 TRP A CH2   1 
ATOM   3490 N  N     . GLN A 1 451 ? -5.696  24.803  9.669   1.00 47.27  ? 451 GLN A N     1 
ATOM   3491 C  CA    . GLN A 1 451 ? -4.241  24.892  9.613   1.00 49.27  ? 451 GLN A CA    1 
ATOM   3492 C  C     . GLN A 1 451 ? -3.607  24.311  10.871  1.00 46.17  ? 451 GLN A C     1 
ATOM   3493 O  O     . GLN A 1 451 ? -2.667  23.510  10.795  1.00 48.02  ? 451 GLN A O     1 
ATOM   3494 C  CB    . GLN A 1 451 ? -3.810  26.347  9.405   1.00 48.63  ? 451 GLN A CB    1 
ATOM   3495 C  CG    . GLN A 1 451 ? -4.229  26.933  8.060   1.00 45.91  ? 451 GLN A CG    1 
ATOM   3496 C  CD    . GLN A 1 451 ? -5.700  27.305  8.015   1.00 54.07  ? 451 GLN A CD    1 
ATOM   3497 O  OE1   . GLN A 1 451 ? -6.252  27.802  8.995   1.00 58.55  ? 451 GLN A OE1   1 
ATOM   3498 N  NE2   . GLN A 1 451 ? -6.343  27.062  6.877   1.00 53.44  ? 451 GLN A NE2   1 
ATOM   3499 N  N     . HIS A 1 452 ? -4.108  24.704  12.043  1.00 45.60  ? 452 HIS A N     1 
ATOM   3500 C  CA    . HIS A 1 452 ? -3.580  24.138  13.279  1.00 46.60  ? 452 HIS A CA    1 
ATOM   3501 C  C     . HIS A 1 452 ? -3.784  22.630  13.313  1.00 48.64  ? 452 HIS A C     1 
ATOM   3502 O  O     . HIS A 1 452 ? -2.918  21.887  13.791  1.00 39.77  ? 452 HIS A O     1 
ATOM   3503 C  CB    . HIS A 1 452 ? -4.241  24.795  14.489  1.00 47.23  ? 452 HIS A CB    1 
ATOM   3504 C  CG    . HIS A 1 452 ? -3.725  24.295  15.801  1.00 44.39  ? 452 HIS A CG    1 
ATOM   3505 N  ND1   . HIS A 1 452 ? -4.551  23.788  16.780  1.00 51.36  ? 452 HIS A ND1   1 
ATOM   3506 C  CD2   . HIS A 1 452 ? -2.467  24.219  16.293  1.00 45.96  ? 452 HIS A CD2   1 
ATOM   3507 C  CE1   . HIS A 1 452 ? -3.824  23.425  17.822  1.00 47.51  ? 452 HIS A CE1   1 
ATOM   3508 N  NE2   . HIS A 1 452 ? -2.556  23.675  17.552  1.00 40.49  ? 452 HIS A NE2   1 
ATOM   3509 N  N     . GLY A 1 453 ? -4.923  22.161  12.808  1.00 40.21  ? 453 GLY A N     1 
ATOM   3510 C  CA    . GLY A 1 453 ? -5.165  20.738  12.702  1.00 47.95  ? 453 GLY A CA    1 
ATOM   3511 C  C     . GLY A 1 453 ? -4.075  20.057  11.902  1.00 50.83  ? 453 GLY A C     1 
ATOM   3512 O  O     . GLY A 1 453 ? -3.357  19.197  12.425  1.00 40.08  ? 453 GLY A O     1 
ATOM   3513 N  N     . VAL A 1 454 ? -3.935  20.461  10.633  1.00 46.58  ? 454 VAL A N     1 
ATOM   3514 C  CA    . VAL A 1 454 ? -2.888  19.913  9.773   1.00 44.03  ? 454 VAL A CA    1 
ATOM   3515 C  C     . VAL A 1 454 ? -1.550  19.915  10.499  1.00 41.75  ? 454 VAL A C     1 
ATOM   3516 O  O     . VAL A 1 454 ? -0.792  18.940  10.442  1.00 49.33  ? 454 VAL A O     1 
ATOM   3517 C  CB    . VAL A 1 454 ? -2.816  20.697  8.449   1.00 41.92  ? 454 VAL A CB    1 
ATOM   3518 C  CG1   . VAL A 1 454 ? -1.642  20.215  7.617   1.00 41.97  ? 454 VAL A CG1   1 
ATOM   3519 C  CG2   . VAL A 1 454 ? -4.121  20.555  7.670   1.00 45.27  ? 454 VAL A CG2   1 
ATOM   3520 N  N     . PHE A 1 455 ? -1.237  21.004  11.201  1.00 42.91  ? 455 PHE A N     1 
ATOM   3521 C  CA    . PHE A 1 455 ? 0.001   21.023  11.971  1.00 48.77  ? 455 PHE A CA    1 
ATOM   3522 C  C     . PHE A 1 455 ? 0.008   19.940  13.040  1.00 46.68  ? 455 PHE A C     1 
ATOM   3523 O  O     . PHE A 1 455 ? 1.065   19.375  13.347  1.00 46.99  ? 455 PHE A O     1 
ATOM   3524 C  CB    . PHE A 1 455 ? 0.214   22.392  12.611  1.00 41.91  ? 455 PHE A CB    1 
ATOM   3525 C  CG    . PHE A 1 455 ? 1.284   22.397  13.660  1.00 40.45  ? 455 PHE A CG    1 
ATOM   3526 C  CD1   . PHE A 1 455 ? 2.619   22.383  13.301  1.00 37.39  ? 455 PHE A CD1   1 
ATOM   3527 C  CD2   . PHE A 1 455 ? 0.955   22.397  15.004  1.00 37.97  ? 455 PHE A CD2   1 
ATOM   3528 C  CE1   . PHE A 1 455 ? 3.613   22.379  14.261  1.00 44.76  ? 455 PHE A CE1   1 
ATOM   3529 C  CE2   . PHE A 1 455 ? 1.946   22.394  15.971  1.00 42.46  ? 455 PHE A CE2   1 
ATOM   3530 C  CZ    . PHE A 1 455 ? 3.277   22.384  15.598  1.00 36.08  ? 455 PHE A CZ    1 
ATOM   3531 N  N     . VAL A 1 456 ? -1.154  19.641  13.624  1.00 44.18  ? 456 VAL A N     1 
ATOM   3532 C  CA    . VAL A 1 456 ? -1.210  18.644  14.689  1.00 45.28  ? 456 VAL A CA    1 
ATOM   3533 C  C     . VAL A 1 456 ? -0.867  17.263  14.143  1.00 44.08  ? 456 VAL A C     1 
ATOM   3534 O  O     . VAL A 1 456 ? -0.011  16.556  14.686  1.00 39.64  ? 456 VAL A O     1 
ATOM   3535 C  CB    . VAL A 1 456 ? -2.589  18.659  15.370  1.00 43.13  ? 456 VAL A CB    1 
ATOM   3536 C  CG1   . VAL A 1 456 ? -2.792  17.376  16.173  1.00 50.01  ? 456 VAL A CG1   1 
ATOM   3537 C  CG2   . VAL A 1 456 ? -2.716  19.883  16.269  1.00 38.54  ? 456 VAL A CG2   1 
ATOM   3538 N  N     . GLY A 1 457 ? -1.525  16.860  13.062  1.00 41.02  ? 457 GLY A N     1 
ATOM   3539 C  CA    . GLY A 1 457 ? -1.187  15.611  12.412  1.00 43.11  ? 457 GLY A CA    1 
ATOM   3540 C  C     . GLY A 1 457 ? 0.299   15.527  12.137  1.00 44.57  ? 457 GLY A C     1 
ATOM   3541 O  O     . GLY A 1 457 ? 0.967   14.575  12.554  1.00 38.45  ? 457 GLY A O     1 
ATOM   3542 N  N     . ALA A 1 458 ? 0.831   16.542  11.450  1.00 45.81  ? 458 ALA A N     1 
ATOM   3543 C  CA    . ALA A 1 458 ? 2.244   16.558  11.096  1.00 41.12  ? 458 ALA A CA    1 
ATOM   3544 C  C     . ALA A 1 458 ? 3.152   16.457  12.312  1.00 38.78  ? 458 ALA A C     1 
ATOM   3545 O  O     . ALA A 1 458 ? 4.297   16.009  12.181  1.00 41.87  ? 458 ALA A O     1 
ATOM   3546 C  CB    . ALA A 1 458 ? 2.564   17.827  10.308  1.00 50.69  ? 458 ALA A CB    1 
ATOM   3547 N  N     . ALA A 1 459 ? 2.678   16.860  13.488  1.00 41.29  ? 459 ALA A N     1 
ATOM   3548 C  CA    . ALA A 1 459 ? 3.495   16.853  14.694  1.00 43.52  ? 459 ALA A CA    1 
ATOM   3549 C  C     . ALA A 1 459 ? 3.316   15.592  15.528  1.00 44.70  ? 459 ALA A C     1 
ATOM   3550 O  O     . ALA A 1 459 ? 3.943   15.471  16.588  1.00 43.13  ? 459 ALA A O     1 
ATOM   3551 C  CB    . ALA A 1 459 ? 3.186   18.088  15.546  1.00 41.38  ? 459 ALA A CB    1 
ATOM   3552 N  N     . MET A 1 460 ? 2.488   14.652  15.075  1.00 38.74  ? 460 MET A N     1 
ATOM   3553 C  CA    . MET A 1 460 ? 2.251   13.425  15.829  1.00 43.67  ? 460 MET A CA    1 
ATOM   3554 C  C     . MET A 1 460 ? 3.558   12.716  16.145  1.00 39.34  ? 460 MET A C     1 
ATOM   3555 O  O     . MET A 1 460 ? 4.470   12.657  15.317  1.00 53.35  ? 460 MET A O     1 
ATOM   3556 C  CB    . MET A 1 460 ? 1.336   12.488  15.042  1.00 28.84  ? 460 MET A CB    1 
ATOM   3557 C  CG    . MET A 1 460 ? -0.037  13.054  14.794  1.00 40.58  ? 460 MET A CG    1 
ATOM   3558 S  SD    . MET A 1 460 ? -1.016  11.955  13.775  1.00 39.12  ? 460 MET A SD    1 
ATOM   3559 C  CE    . MET A 1 460 ? -0.746  10.395  14.625  1.00 39.39  ? 460 MET A CE    1 
ATOM   3560 N  N     . ARG A 1 461 ? 3.642   12.182  17.357  1.00 36.20  ? 461 ARG A N     1 
ATOM   3561 C  CA    . ARG A 1 461 ? 4.767   11.359  17.770  1.00 51.75  ? 461 ARG A CA    1 
ATOM   3562 C  C     . ARG A 1 461 ? 4.241   10.226  18.638  1.00 58.01  ? 461 ARG A C     1 
ATOM   3563 O  O     . ARG A 1 461 ? 3.175   10.337  19.248  1.00 60.72  ? 461 ARG A O     1 
ATOM   3564 C  CB    . ARG A 1 461 ? 5.818   12.180  18.522  1.00 47.66  ? 461 ARG A CB    1 
ATOM   3565 C  CG    . ARG A 1 461 ? 6.450   13.285  17.688  1.00 47.59  ? 461 ARG A CG    1 
ATOM   3566 C  CD    . ARG A 1 461 ? 7.349   14.161  18.545  1.00 44.87  ? 461 ARG A CD    1 
ATOM   3567 N  NE    . ARG A 1 461 ? 8.473   13.417  19.098  1.00 43.16  ? 461 ARG A NE    1 
ATOM   3568 C  CZ    . ARG A 1 461 ? 9.153   13.782  20.177  1.00 57.68  ? 461 ARG A CZ    1 
ATOM   3569 N  NH1   . ARG A 1 461 ? 8.829   14.865  20.865  1.00 60.49  ? 461 ARG A NH1   1 
ATOM   3570 N  NH2   . ARG A 1 461 ? 10.179  13.039  20.581  1.00 55.14  ? 461 ARG A NH2   1 
ATOM   3571 N  N     . SER A 1 462 ? 4.994   9.130   18.685  1.00 56.67  ? 462 SER A N     1 
ATOM   3572 C  CA    . SER A 1 462 ? 4.519   7.930   19.360  1.00 60.58  ? 462 SER A CA    1 
ATOM   3573 C  C     . SER A 1 462 ? 5.701   7.028   19.676  1.00 64.12  ? 462 SER A C     1 
ATOM   3574 O  O     . SER A 1 462 ? 6.728   7.064   18.993  1.00 69.37  ? 462 SER A O     1 
ATOM   3575 C  CB    . SER A 1 462 ? 3.490   7.184   18.503  1.00 54.88  ? 462 SER A CB    1 
ATOM   3576 O  OG    . SER A 1 462 ? 3.056   6.000   19.144  1.00 59.11  ? 462 SER A OG    1 
ATOM   3577 N  N     . GLU A 1 463 ? 5.541   6.216   20.716  1.00 66.16  ? 463 GLU A N     1 
ATOM   3578 C  CA    . GLU A 1 463 ? 6.603   5.310   21.122  1.00 78.72  ? 463 GLU A CA    1 
ATOM   3579 C  C     . GLU A 1 463 ? 6.659   4.097   20.196  1.00 78.88  ? 463 GLU A C     1 
ATOM   3580 O  O     . GLU A 1 463 ? 5.684   3.745   19.527  1.00 74.26  ? 463 GLU A O     1 
ATOM   3581 C  CB    . GLU A 1 463 ? 6.407   4.863   22.571  1.00 74.65  ? 463 GLU A CB    1 
ATOM   3582 C  CG    . GLU A 1 463 ? 5.058   4.226   22.846  1.00 78.73  ? 463 GLU A CG    1 
ATOM   3583 C  CD    . GLU A 1 463 ? 4.986   3.584   24.218  1.00 85.82  ? 463 GLU A CD    1 
ATOM   3584 O  OE1   . GLU A 1 463 ? 5.982   3.668   24.967  1.00 85.61  ? 463 GLU A OE1   1 
ATOM   3585 O  OE2   . GLU A 1 463 ? 3.936   2.993   24.544  1.00 86.66  ? 463 GLU A OE2   1 
ATOM   3586 N  N     . ALA A 1 464 ? 7.826   3.458   20.166  1.00 87.12  ? 464 ALA A N     1 
ATOM   3587 C  CA    . ALA A 1 464 ? 8.038   2.318   19.283  1.00 104.02 ? 464 ALA A CA    1 
ATOM   3588 C  C     . ALA A 1 464 ? 7.201   1.128   19.733  1.00 111.57 ? 464 ALA A C     1 
ATOM   3589 O  O     . ALA A 1 464 ? 7.270   0.708   20.893  1.00 112.82 ? 464 ALA A O     1 
ATOM   3590 C  CB    . ALA A 1 464 ? 9.518   1.942   19.249  1.00 112.14 ? 464 ALA A CB    1 
ATOM   3591 N  N     . THR A 1 465 ? 6.411   0.581   18.810  1.00 123.72 ? 465 THR A N     1 
ATOM   3592 C  CA    . THR A 1 465 ? 5.554   -0.567  19.044  1.00 130.95 ? 465 THR A CA    1 
ATOM   3593 C  C     . THR A 1 465 ? 6.099   -1.769  18.267  1.00 141.88 ? 465 THR A C     1 
ATOM   3594 O  O     . THR A 1 465 ? 7.311   -1.830  17.989  1.00 141.69 ? 465 THR A O     1 
ATOM   3595 C  CB    . THR A 1 465 ? 4.118   -0.198  18.678  1.00 121.70 ? 465 THR A CB    1 
ATOM   3596 O  OG1   . THR A 1 465 ? 4.073   0.270   17.324  1.00 119.38 ? 465 THR A OG1   1 
ATOM   3597 C  CG2   . THR A 1 465 ? 3.596   0.889   19.605  1.00 116.88 ? 465 THR A CG2   1 
ATOM   3598 N  N     . ALA A 1 466 ? 5.223   -2.712  17.918  1.00 143.72 ? 466 ALA A N     1 
ATOM   3599 C  CA    . ALA A 1 466 ? 5.639   -3.920  17.217  1.00 147.13 ? 466 ALA A CA    1 
ATOM   3600 C  C     . ALA A 1 466 ? 4.942   -4.043  15.868  1.00 144.67 ? 466 ALA A C     1 
ATOM   3601 O  O     . ALA A 1 466 ? 4.301   -5.060  15.584  1.00 138.32 ? 466 ALA A O     1 
ATOM   3602 C  CB    . ALA A 1 466 ? 5.359   -5.158  18.073  1.00 141.46 ? 466 ALA A CB    1 
ATOM   3603 N  N     . ALA A 1 467 ? 5.063   -3.013  15.031  1.00 131.79 ? 467 ALA A N     1 
ATOM   3604 C  CA    . ALA A 1 467 ? 4.484   -3.007  13.693  1.00 114.78 ? 467 ALA A CA    1 
ATOM   3605 C  C     . ALA A 1 467 ? 5.530   -3.164  12.601  1.00 114.34 ? 467 ALA A C     1 
ATOM   3606 O  O     . ALA A 1 467 ? 5.379   -4.010  11.715  1.00 100.75 ? 467 ALA A O     1 
ATOM   3607 C  CB    . ALA A 1 467 ? 3.692   -1.712  13.470  1.00 99.48  ? 467 ALA A CB    1 
ATOM   3608 N  N     . ALA A 1 468 ? 6.588   -2.355  12.638  1.00 122.27 ? 468 ALA A N     1 
ATOM   3609 C  CA    . ALA A 1 468 ? 7.713   -2.518  11.727  1.00 120.27 ? 468 ALA A CA    1 
ATOM   3610 C  C     . ALA A 1 468 ? 8.836   -3.264  12.437  1.00 128.32 ? 468 ALA A C     1 
ATOM   3611 O  O     . ALA A 1 468 ? 8.571   -4.154  13.252  1.00 128.13 ? 468 ALA A O     1 
ATOM   3612 C  CB    . ALA A 1 468 ? 8.197   -1.159  11.214  1.00 112.28 ? 468 ALA A CB    1 
ATOM   3613 N  N     . GLU A 1 469 ? 10.089  -2.912  12.146  1.00 128.51 ? 469 GLU A N     1 
ATOM   3614 C  CA    . GLU A 1 469 ? 11.238  -3.531  12.794  1.00 128.41 ? 469 GLU A CA    1 
ATOM   3615 C  C     . GLU A 1 469 ? 11.807  -2.672  13.918  1.00 131.66 ? 469 GLU A C     1 
ATOM   3616 O  O     . GLU A 1 469 ? 12.931  -2.916  14.370  1.00 125.69 ? 469 GLU A O     1 
ATOM   3617 C  CB    . GLU A 1 469 ? 12.327  -3.846  11.766  1.00 124.06 ? 469 GLU A CB    1 
ATOM   3618 C  CG    . GLU A 1 469 ? 12.855  -2.638  11.009  1.00 117.39 ? 469 GLU A CG    1 
ATOM   3619 C  CD    . GLU A 1 469 ? 12.272  -2.521  9.615   1.00 107.32 ? 469 GLU A CD    1 
ATOM   3620 O  OE1   . GLU A 1 469 ? 11.284  -3.225  9.319   1.00 106.69 ? 469 GLU A OE1   1 
ATOM   3621 O  OE2   . GLU A 1 469 ? 12.807  -1.728  8.812   1.00 102.29 ? 469 GLU A OE2   1 
ATOM   3622 N  N     . HIS A 1 470 ? 11.053  -1.678  14.383  1.00 139.14 ? 470 HIS A N     1 
ATOM   3623 C  CA    . HIS A 1 470 ? 11.528  -0.794  15.438  1.00 141.20 ? 470 HIS A CA    1 
ATOM   3624 C  C     . HIS A 1 470 ? 11.398  -1.467  16.799  1.00 141.35 ? 470 HIS A C     1 
ATOM   3625 O  O     . HIS A 1 470 ? 10.409  -2.148  17.081  1.00 143.06 ? 470 HIS A O     1 
ATOM   3626 C  CB    . HIS A 1 470 ? 10.745  0.519   15.424  1.00 138.78 ? 470 HIS A CB    1 
ATOM   3627 C  CG    . HIS A 1 470 ? 10.721  1.194   14.088  1.00 137.07 ? 470 HIS A CG    1 
ATOM   3628 N  ND1   . HIS A 1 470 ? 11.765  1.966   13.624  1.00 136.90 ? 470 HIS A ND1   1 
ATOM   3629 C  CD2   . HIS A 1 470 ? 9.780   1.209   13.114  1.00 135.55 ? 470 HIS A CD2   1 
ATOM   3630 C  CE1   . HIS A 1 470 ? 11.468  2.428   12.423  1.00 130.33 ? 470 HIS A CE1   1 
ATOM   3631 N  NE2   . HIS A 1 470 ? 10.269  1.984   12.090  1.00 130.06 ? 470 HIS A NE2   1 
ATOM   3632 N  N     . LYS A 1 471 ? 12.408  -1.270  17.643  1.00 132.79 ? 471 LYS A N     1 
ATOM   3633 C  CA    . LYS A 1 471 ? 12.441  -1.845  18.978  1.00 132.29 ? 471 LYS A CA    1 
ATOM   3634 C  C     . LYS A 1 471 ? 12.797  -0.764  19.992  1.00 135.72 ? 471 LYS A C     1 
ATOM   3635 O  O     . LYS A 1 471 ? 13.136  0.369   19.638  1.00 129.95 ? 471 LYS A O     1 
ATOM   3636 C  CB    . LYS A 1 471 ? 13.439  -3.009  19.063  1.00 122.25 ? 471 LYS A CB    1 
ATOM   3637 C  CG    . LYS A 1 471 ? 13.092  -4.190  18.170  1.00 116.56 ? 471 LYS A CG    1 
ATOM   3638 C  CD    . LYS A 1 471 ? 14.042  -5.354  18.403  1.00 107.73 ? 471 LYS A CD    1 
ATOM   3639 C  CE    . LYS A 1 471 ? 13.668  -6.554  17.548  1.00 99.00  ? 471 LYS A CE    1 
ATOM   3640 N  NZ    . LYS A 1 471 ? 14.541  -7.728  17.827  1.00 94.27  ? 471 LYS A NZ    1 
ATOM   3641 N  N     . GLY A 1 472 ? 12.710  -1.130  21.268  1.00 141.59 ? 472 GLY A N     1 
ATOM   3642 C  CA    . GLY A 1 472 ? 13.032  -0.223  22.348  1.00 139.95 ? 472 GLY A CA    1 
ATOM   3643 C  C     . GLY A 1 472 ? 11.884  0.708   22.696  1.00 135.51 ? 472 GLY A C     1 
ATOM   3644 O  O     . GLY A 1 472 ? 10.873  0.806   21.998  1.00 128.97 ? 472 GLY A O     1 
ATOM   3645 N  N     . LYS A 1 473 ? 12.056  1.410   23.817  1.00 137.30 ? 473 LYS A N     1 
ATOM   3646 C  CA    . LYS A 1 473 ? 11.071  2.380   24.294  1.00 133.65 ? 473 LYS A CA    1 
ATOM   3647 C  C     . LYS A 1 473 ? 11.566  3.777   23.926  1.00 125.00 ? 473 LYS A C     1 
ATOM   3648 O  O     . LYS A 1 473 ? 12.163  4.493   24.729  1.00 123.64 ? 473 LYS A O     1 
ATOM   3649 C  CB    . LYS A 1 473 ? 10.849  2.226   25.797  1.00 143.30 ? 473 LYS A CB    1 
ATOM   3650 C  CG    . LYS A 1 473 ? 10.525  0.805   26.239  1.00 143.95 ? 473 LYS A CG    1 
ATOM   3651 C  CD    . LYS A 1 473 ? 9.290   0.269   25.532  1.00 142.78 ? 473 LYS A CD    1 
ATOM   3652 C  CE    . LYS A 1 473 ? 8.065   1.118   25.831  1.00 134.52 ? 473 LYS A CE    1 
ATOM   3653 N  NZ    . LYS A 1 473 ? 6.853   0.604   25.135  1.00 123.48 ? 473 LYS A NZ    1 
ATOM   3654 N  N     . VAL A 1 474 ? 11.308  4.161   22.678  1.00 110.98 ? 474 VAL A N     1 
ATOM   3655 C  CA    . VAL A 1 474 ? 11.738  5.444   22.142  1.00 90.67  ? 474 VAL A CA    1 
ATOM   3656 C  C     . VAL A 1 474 ? 10.560  6.106   21.446  1.00 81.77  ? 474 VAL A C     1 
ATOM   3657 O  O     . VAL A 1 474 ? 9.705   5.436   20.857  1.00 85.52  ? 474 VAL A O     1 
ATOM   3658 C  CB    . VAL A 1 474 ? 12.931  5.286   21.174  1.00 87.71  ? 474 VAL A CB    1 
ATOM   3659 C  CG1   . VAL A 1 474 ? 13.024  6.477   20.237  1.00 81.84  ? 474 VAL A CG1   1 
ATOM   3660 C  CG2   . VAL A 1 474 ? 14.221  5.124   21.957  1.00 87.55  ? 474 VAL A CG2   1 
ATOM   3661 N  N     . ILE A 1 475 ? 10.515  7.433   21.522  1.00 74.96  ? 475 ILE A N     1 
ATOM   3662 C  CA    . ILE A 1 475 ? 9.443   8.226   20.934  1.00 66.76  ? 475 ILE A CA    1 
ATOM   3663 C  C     . ILE A 1 475 ? 9.957   8.840   19.640  1.00 68.15  ? 475 ILE A C     1 
ATOM   3664 O  O     . ILE A 1 475 ? 10.964  9.559   19.638  1.00 69.83  ? 475 ILE A O     1 
ATOM   3665 C  CB    . ILE A 1 475 ? 8.949   9.307   21.908  1.00 67.22  ? 475 ILE A CB    1 
ATOM   3666 C  CG1   . ILE A 1 475 ? 8.417   8.654   23.189  1.00 64.41  ? 475 ILE A CG1   1 
ATOM   3667 C  CG2   . ILE A 1 475 ? 7.884   10.168  21.247  1.00 57.74  ? 475 ILE A CG2   1 
ATOM   3668 C  CD1   . ILE A 1 475 ? 8.075   9.633   24.286  1.00 66.98  ? 475 ILE A CD1   1 
ATOM   3669 N  N     . MET A 1 476 ? 9.263   8.562   18.540  1.00 61.56  ? 476 MET A N     1 
ATOM   3670 C  CA    . MET A 1 476 ? 9.681   8.994   17.217  1.00 64.09  ? 476 MET A CA    1 
ATOM   3671 C  C     . MET A 1 476 ? 8.502   9.628   16.495  1.00 58.83  ? 476 MET A C     1 
ATOM   3672 O  O     . MET A 1 476 ? 7.343   9.447   16.874  1.00 54.02  ? 476 MET A O     1 
ATOM   3673 C  CB    . MET A 1 476 ? 10.233  7.822   16.397  1.00 69.78  ? 476 MET A CB    1 
ATOM   3674 C  CG    . MET A 1 476 ? 9.222   6.719   16.160  1.00 65.97  ? 476 MET A CG    1 
ATOM   3675 S  SD    . MET A 1 476 ? 9.946   5.304   15.317  1.00 96.58  ? 476 MET A SD    1 
ATOM   3676 C  CE    . MET A 1 476 ? 10.712  6.109   13.909  1.00 84.78  ? 476 MET A CE    1 
ATOM   3677 N  N     . HIS A 1 477 ? 8.815   10.379  15.444  1.00 54.35  ? 477 HIS A N     1 
ATOM   3678 C  CA    . HIS A 1 477 ? 7.787   11.079  14.692  1.00 52.66  ? 477 HIS A CA    1 
ATOM   3679 C  C     . HIS A 1 477 ? 7.065   10.124  13.753  1.00 54.03  ? 477 HIS A C     1 
ATOM   3680 O  O     . HIS A 1 477 ? 7.657   9.192   13.202  1.00 59.17  ? 477 HIS A O     1 
ATOM   3681 C  CB    . HIS A 1 477 ? 8.397   12.233  13.897  1.00 54.66  ? 477 HIS A CB    1 
ATOM   3682 C  CG    . HIS A 1 477 ? 8.988   13.308  14.753  1.00 54.14  ? 477 HIS A CG    1 
ATOM   3683 N  ND1   . HIS A 1 477 ? 10.237  13.201  15.326  1.00 60.49  ? 477 HIS A ND1   1 
ATOM   3684 C  CD2   . HIS A 1 477 ? 8.497   14.509  15.140  1.00 52.88  ? 477 HIS A CD2   1 
ATOM   3685 C  CE1   . HIS A 1 477 ? 10.492  14.291  16.026  1.00 58.11  ? 477 HIS A CE1   1 
ATOM   3686 N  NE2   . HIS A 1 477 ? 9.453   15.101  15.930  1.00 54.05  ? 477 HIS A NE2   1 
ATOM   3687 N  N     . ASP A 1 478 ? 5.766   10.363  13.582  1.00 51.14  ? 478 ASP A N     1 
ATOM   3688 C  CA    . ASP A 1 478 ? 4.930   9.582   12.681  1.00 51.63  ? 478 ASP A CA    1 
ATOM   3689 C  C     . ASP A 1 478 ? 3.773   10.454  12.213  1.00 49.73  ? 478 ASP A C     1 
ATOM   3690 O  O     . ASP A 1 478 ? 2.608   10.164  12.514  1.00 49.37  ? 478 ASP A O     1 
ATOM   3691 C  CB    . ASP A 1 478 ? 4.415   8.313   13.368  1.00 55.09  ? 478 ASP A CB    1 
ATOM   3692 C  CG    . ASP A 1 478 ? 3.890   7.284   12.379  1.00 52.24  ? 478 ASP A CG    1 
ATOM   3693 O  OD1   . ASP A 1 478 ? 3.502   7.677   11.259  1.00 53.71  ? 478 ASP A OD1   1 
ATOM   3694 O  OD2   . ASP A 1 478 ? 3.866   6.082   12.720  1.00 51.98  ? 478 ASP A OD2   1 
ATOM   3695 N  N     . PRO A 1 479 ? 4.055   11.525  11.475  1.00 49.46  ? 479 PRO A N     1 
ATOM   3696 C  CA    . PRO A 1 479 ? 2.996   12.480  11.123  1.00 51.57  ? 479 PRO A CA    1 
ATOM   3697 C  C     . PRO A 1 479 ? 1.873   11.809  10.350  1.00 48.44  ? 479 PRO A C     1 
ATOM   3698 O  O     . PRO A 1 479 ? 2.108   11.061  9.400   1.00 48.76  ? 479 PRO A O     1 
ATOM   3699 C  CB    . PRO A 1 479 ? 3.728   13.524  10.268  1.00 49.31  ? 479 PRO A CB    1 
ATOM   3700 C  CG    . PRO A 1 479 ? 4.973   12.842  9.796   1.00 49.63  ? 479 PRO A CG    1 
ATOM   3701 C  CD    . PRO A 1 479 ? 5.356   11.898  10.896  1.00 53.44  ? 479 PRO A CD    1 
ATOM   3702 N  N     . PHE A 1 480 ? 0.640   12.093  10.758  1.00 48.00  ? 480 PHE A N     1 
ATOM   3703 C  CA    . PHE A 1 480 ? -0.561  11.526  10.155  1.00 47.85  ? 480 PHE A CA    1 
ATOM   3704 C  C     . PHE A 1 480 ? -0.598  10.006  10.242  1.00 48.29  ? 480 PHE A C     1 
ATOM   3705 O  O     . PHE A 1 480 ? -1.408  9.370   9.556   1.00 48.44  ? 480 PHE A O     1 
ATOM   3706 C  CB    . PHE A 1 480 ? -0.716  11.971  8.693   1.00 47.88  ? 480 PHE A CB    1 
ATOM   3707 C  CG    . PHE A 1 480 ? -1.131  13.408  8.542   1.00 50.94  ? 480 PHE A CG    1 
ATOM   3708 C  CD1   . PHE A 1 480 ? -0.228  14.434  8.777   1.00 51.08  ? 480 PHE A CD1   1 
ATOM   3709 C  CD2   . PHE A 1 480 ? -2.427  13.735  8.170   1.00 48.35  ? 480 PHE A CD2   1 
ATOM   3710 C  CE1   . PHE A 1 480 ? -0.609  15.760  8.644   1.00 50.73  ? 480 PHE A CE1   1 
ATOM   3711 C  CE2   . PHE A 1 480 ? -2.815  15.056  8.034   1.00 48.00  ? 480 PHE A CE2   1 
ATOM   3712 C  CZ    . PHE A 1 480 ? -1.905  16.071  8.270   1.00 52.34  ? 480 PHE A CZ    1 
ATOM   3713 N  N     . ALA A 1 481 ? 0.255   9.408   11.073  1.00 48.71  ? 481 ALA A N     1 
ATOM   3714 C  CA    . ALA A 1 481 ? 0.407   7.957   11.155  1.00 54.80  ? 481 ALA A CA    1 
ATOM   3715 C  C     . ALA A 1 481 ? 0.829   7.350   9.822   1.00 52.67  ? 481 ALA A C     1 
ATOM   3716 O  O     . ALA A 1 481 ? 0.656   6.146   9.603   1.00 51.61  ? 481 ALA A O     1 
ATOM   3717 C  CB    . ALA A 1 481 ? -0.879  7.286   11.654  1.00 49.51  ? 481 ALA A CB    1 
ATOM   3718 N  N     . MET A 1 482 ? 1.392   8.166   8.928   1.00 51.46  ? 482 MET A N     1 
ATOM   3719 C  CA    . MET A 1 482 ? 1.693   7.759   7.561   1.00 50.29  ? 482 MET A CA    1 
ATOM   3720 C  C     . MET A 1 482 ? 3.182   7.754   7.247   1.00 50.93  ? 482 MET A C     1 
ATOM   3721 O  O     . MET A 1 482 ? 3.551   7.671   6.072   1.00 51.54  ? 482 MET A O     1 
ATOM   3722 C  CB    . MET A 1 482 ? 0.968   8.673   6.573   1.00 49.94  ? 482 MET A CB    1 
ATOM   3723 C  CG    . MET A 1 482 ? -0.511  8.386   6.427   1.00 55.57  ? 482 MET A CG    1 
ATOM   3724 S  SD    . MET A 1 482 ? -0.863  7.476   4.918   1.00 57.82  ? 482 MET A SD    1 
ATOM   3725 C  CE    . MET A 1 482 ? -0.419  8.685   3.674   1.00 53.94  ? 482 MET A CE    1 
ATOM   3726 N  N     . ARG A 1 483 ? 4.045   7.848   8.254   1.00 51.01  ? 483 ARG A N     1 
ATOM   3727 C  CA    . ARG A 1 483 ? 5.480   7.846   7.986   1.00 51.80  ? 483 ARG A CA    1 
ATOM   3728 C  C     . ARG A 1 483 ? 5.920   6.677   7.116   1.00 58.23  ? 483 ARG A C     1 
ATOM   3729 O  O     . ARG A 1 483 ? 6.714   6.899   6.187   1.00 62.35  ? 483 ARG A O     1 
ATOM   3730 C  CB    . ARG A 1 483 ? 6.266   7.843   9.304   1.00 52.05  ? 483 ARG A CB    1 
ATOM   3731 C  CG    . ARG A 1 483 ? 7.752   8.104   9.109   1.00 57.19  ? 483 ARG A CG    1 
ATOM   3732 C  CD    . ARG A 1 483 ? 8.576   7.735   10.331  1.00 62.05  ? 483 ARG A CD    1 
ATOM   3733 N  NE    . ARG A 1 483 ? 8.631   6.293   10.538  1.00 67.42  ? 483 ARG A NE    1 
ATOM   3734 C  CZ    . ARG A 1 483 ? 7.878   5.631   11.406  1.00 76.46  ? 483 ARG A CZ    1 
ATOM   3735 N  NH1   . ARG A 1 483 ? 7.010   6.256   12.185  1.00 74.01  ? 483 ARG A NH1   1 
ATOM   3736 N  NH2   . ARG A 1 483 ? 8.000   4.310   11.497  1.00 83.92  ? 483 ARG A NH2   1 
ATOM   3737 N  N     . PRO A 1 484 ? 5.467   5.442   7.342   1.00 58.73  ? 484 PRO A N     1 
ATOM   3738 C  CA    . PRO A 1 484 ? 5.918   4.323   6.507   1.00 56.39  ? 484 PRO A CA    1 
ATOM   3739 C  C     . PRO A 1 484 ? 5.237   4.232   5.151   1.00 55.13  ? 484 PRO A C     1 
ATOM   3740 O  O     . PRO A 1 484 ? 5.608   3.359   4.358   1.00 57.42  ? 484 PRO A O     1 
ATOM   3741 C  CB    . PRO A 1 484 ? 5.575   3.088   7.366   1.00 55.31  ? 484 PRO A CB    1 
ATOM   3742 C  CG    . PRO A 1 484 ? 5.198   3.614   8.721   1.00 57.10  ? 484 PRO A CG    1 
ATOM   3743 C  CD    . PRO A 1 484 ? 4.660   4.983   8.483   1.00 56.71  ? 484 PRO A CD    1 
ATOM   3744 N  N     . PHE A 1 485 ? 4.260   5.091   4.848   1.00 54.04  ? 485 PHE A N     1 
ATOM   3745 C  CA    . PHE A 1 485 ? 3.420   4.888   3.677   1.00 54.49  ? 485 PHE A CA    1 
ATOM   3746 C  C     . PHE A 1 485 ? 3.329   6.085   2.739   1.00 54.58  ? 485 PHE A C     1 
ATOM   3747 O  O     . PHE A 1 485 ? 2.574   6.020   1.762   1.00 54.75  ? 485 PHE A O     1 
ATOM   3748 C  CB    . PHE A 1 485 ? 1.999   4.490   4.107   1.00 54.00  ? 485 PHE A CB    1 
ATOM   3749 C  CG    . PHE A 1 485 ? 1.966   3.496   5.229   1.00 55.34  ? 485 PHE A CG    1 
ATOM   3750 C  CD1   . PHE A 1 485 ? 2.394   2.191   5.032   1.00 55.58  ? 485 PHE A CD1   1 
ATOM   3751 C  CD2   . PHE A 1 485 ? 1.501   3.864   6.482   1.00 53.18  ? 485 PHE A CD2   1 
ATOM   3752 C  CE1   . PHE A 1 485 ? 2.364   1.270   6.065   1.00 59.27  ? 485 PHE A CE1   1 
ATOM   3753 C  CE2   . PHE A 1 485 ? 1.466   2.953   7.517   1.00 55.61  ? 485 PHE A CE2   1 
ATOM   3754 C  CZ    . PHE A 1 485 ? 1.898   1.652   7.311   1.00 55.01  ? 485 PHE A CZ    1 
ATOM   3755 N  N     . PHE A 1 486 ? 4.062   7.168   2.993   1.00 53.72  ? 486 PHE A N     1 
ATOM   3756 C  CA    . PHE A 1 486 ? 3.980   8.329   2.115   1.00 54.96  ? 486 PHE A CA    1 
ATOM   3757 C  C     . PHE A 1 486 ? 4.322   7.932   0.686   1.00 55.25  ? 486 PHE A C     1 
ATOM   3758 O  O     . PHE A 1 486 ? 5.375   7.345   0.427   1.00 56.31  ? 486 PHE A O     1 
ATOM   3759 C  CB    . PHE A 1 486 ? 4.916   9.439   2.599   1.00 55.21  ? 486 PHE A CB    1 
ATOM   3760 C  CG    . PHE A 1 486 ? 4.404   10.177  3.800   1.00 51.97  ? 486 PHE A CG    1 
ATOM   3761 C  CD1   . PHE A 1 486 ? 3.133   10.721  3.802   1.00 51.25  ? 486 PHE A CD1   1 
ATOM   3762 C  CD2   . PHE A 1 486 ? 5.184   10.304  4.937   1.00 54.06  ? 486 PHE A CD2   1 
ATOM   3763 C  CE1   . PHE A 1 486 ? 2.653   11.392  4.912   1.00 52.29  ? 486 PHE A CE1   1 
ATOM   3764 C  CE2   . PHE A 1 486 ? 4.712   10.970  6.050   1.00 50.74  ? 486 PHE A CE2   1 
ATOM   3765 C  CZ    . PHE A 1 486 ? 3.444   11.515  6.038   1.00 51.08  ? 486 PHE A CZ    1 
ATOM   3766 N  N     . GLY A 1 487 ? 3.415   8.241   -0.242  1.00 55.59  ? 487 GLY A N     1 
ATOM   3767 C  CA    . GLY A 1 487 ? 3.663   7.934   -1.637  1.00 57.32  ? 487 GLY A CA    1 
ATOM   3768 C  C     . GLY A 1 487 ? 4.530   8.942   -2.359  1.00 58.82  ? 487 GLY A C     1 
ATOM   3769 O  O     . GLY A 1 487 ? 5.037   8.638   -3.443  1.00 59.73  ? 487 GLY A O     1 
ATOM   3770 N  N     . TYR A 1 488 ? 4.713   10.129  -1.785  1.00 58.33  ? 488 TYR A N     1 
ATOM   3771 C  CA    . TYR A 1 488 ? 5.455   11.199  -2.441  1.00 57.76  ? 488 TYR A CA    1 
ATOM   3772 C  C     . TYR A 1 488 ? 5.959   12.167  -1.378  1.00 56.58  ? 488 TYR A C     1 
ATOM   3773 O  O     . TYR A 1 488 ? 5.738   11.976  -0.179  1.00 55.28  ? 488 TYR A O     1 
ATOM   3774 C  CB    . TYR A 1 488 ? 4.584   11.910  -3.481  1.00 58.45  ? 488 TYR A CB    1 
ATOM   3775 C  CG    . TYR A 1 488 ? 3.340   12.541  -2.900  1.00 57.09  ? 488 TYR A CG    1 
ATOM   3776 C  CD1   . TYR A 1 488 ? 2.223   11.773  -2.596  1.00 57.91  ? 488 TYR A CD1   1 
ATOM   3777 C  CD2   . TYR A 1 488 ? 3.281   13.905  -2.654  1.00 56.60  ? 488 TYR A CD2   1 
ATOM   3778 C  CE1   . TYR A 1 488 ? 1.081   12.348  -2.061  1.00 62.95  ? 488 TYR A CE1   1 
ATOM   3779 C  CE2   . TYR A 1 488 ? 2.146   14.490  -2.122  1.00 56.72  ? 488 TYR A CE2   1 
ATOM   3780 C  CZ    . TYR A 1 488 ? 1.048   13.708  -1.826  1.00 63.43  ? 488 TYR A CZ    1 
ATOM   3781 O  OH    . TYR A 1 488 ? -0.083  14.289  -1.294  1.00 59.12  ? 488 TYR A OH    1 
ATOM   3782 N  N     . ASN A 1 489 ? 6.647   13.212  -1.839  1.00 58.74  ? 489 ASN A N     1 
ATOM   3783 C  CA    . ASN A 1 489 ? 7.209   14.242  -0.973  1.00 56.61  ? 489 ASN A CA    1 
ATOM   3784 C  C     . ASN A 1 489 ? 6.228   14.640  0.121   1.00 56.52  ? 489 ASN A C     1 
ATOM   3785 O  O     . ASN A 1 489 ? 5.055   14.912  -0.147  1.00 55.90  ? 489 ASN A O     1 
ATOM   3786 C  CB    . ASN A 1 489 ? 7.586   15.465  -1.816  1.00 60.15  ? 489 ASN A CB    1 
ATOM   3787 C  CG    . ASN A 1 489 ? 8.289   16.536  -1.012  1.00 57.43  ? 489 ASN A CG    1 
ATOM   3788 O  OD1   . ASN A 1 489 ? 7.656   17.289  -0.274  1.00 60.62  ? 489 ASN A OD1   1 
ATOM   3789 N  ND2   . ASN A 1 489 ? 9.606   16.618  -1.160  1.00 58.54  ? 489 ASN A ND2   1 
ATOM   3790 N  N     . PHE A 1 490 ? 6.717   14.670  1.362   1.00 56.11  ? 490 PHE A N     1 
ATOM   3791 C  CA    . PHE A 1 490 ? 5.844   14.944  2.498   1.00 52.76  ? 490 PHE A CA    1 
ATOM   3792 C  C     . PHE A 1 490 ? 5.447   16.412  2.566   1.00 54.93  ? 490 PHE A C     1 
ATOM   3793 O  O     . PHE A 1 490 ? 4.314   16.731  2.944   1.00 55.05  ? 490 PHE A O     1 
ATOM   3794 C  CB    . PHE A 1 490 ? 6.522   14.516  3.797   1.00 55.78  ? 490 PHE A CB    1 
ATOM   3795 C  CG    . PHE A 1 490 ? 5.770   14.912  5.032   1.00 57.35  ? 490 PHE A CG    1 
ATOM   3796 C  CD1   . PHE A 1 490 ? 4.442   14.556  5.195   1.00 50.53  ? 490 PHE A CD1   1 
ATOM   3797 C  CD2   . PHE A 1 490 ? 6.395   15.627  6.038   1.00 52.69  ? 490 PHE A CD2   1 
ATOM   3798 C  CE1   . PHE A 1 490 ? 3.751   14.913  6.332   1.00 50.59  ? 490 PHE A CE1   1 
ATOM   3799 C  CE2   . PHE A 1 490 ? 5.708   15.983  7.179   1.00 53.27  ? 490 PHE A CE2   1 
ATOM   3800 C  CZ    . PHE A 1 490 ? 4.385   15.628  7.325   1.00 49.61  ? 490 PHE A CZ    1 
ATOM   3801 N  N     . GLY A 1 491 ? 6.363   17.317  2.221   1.00 56.03  ? 491 GLY A N     1 
ATOM   3802 C  CA    . GLY A 1 491 ? 5.996   18.721  2.141   1.00 53.65  ? 491 GLY A CA    1 
ATOM   3803 C  C     . GLY A 1 491 ? 4.820   18.947  1.214   1.00 53.85  ? 491 GLY A C     1 
ATOM   3804 O  O     . GLY A 1 491 ? 3.874   19.663  1.548   1.00 54.23  ? 491 GLY A O     1 
ATOM   3805 N  N     . LYS A 1 492 ? 4.862   18.329  0.031   1.00 54.76  ? 492 LYS A N     1 
ATOM   3806 C  CA    . LYS A 1 492 ? 3.729   18.410  -0.883  1.00 56.21  ? 492 LYS A CA    1 
ATOM   3807 C  C     . LYS A 1 492 ? 2.503   17.717  -0.305  1.00 53.99  ? 492 LYS A C     1 
ATOM   3808 O  O     . LYS A 1 492 ? 1.371   18.051  -0.672  1.00 56.88  ? 492 LYS A O     1 
ATOM   3809 C  CB    . LYS A 1 492 ? 4.098   17.803  -2.238  1.00 56.70  ? 492 LYS A CB    1 
ATOM   3810 C  CG    . LYS A 1 492 ? 5.336   18.416  -2.873  1.00 58.16  ? 492 LYS A CG    1 
ATOM   3811 C  CD    . LYS A 1 492 ? 5.221   19.930  -2.940  1.00 63.22  ? 492 LYS A CD    1 
ATOM   3812 C  CE    . LYS A 1 492 ? 6.540   20.571  -3.338  1.00 69.75  ? 492 LYS A CE    1 
ATOM   3813 N  NZ    . LYS A 1 492 ? 6.519   22.043  -3.122  1.00 63.81  ? 492 LYS A NZ    1 
ATOM   3814 N  N     . TYR A 1 493 ? 2.709   16.747  0.585   1.00 53.43  ? 493 TYR A N     1 
ATOM   3815 C  CA    . TYR A 1 493 ? 1.596   16.148  1.312   1.00 53.46  ? 493 TYR A CA    1 
ATOM   3816 C  C     . TYR A 1 493 ? 0.912   17.188  2.192   1.00 53.55  ? 493 TYR A C     1 
ATOM   3817 O  O     . TYR A 1 493 ? -0.293  17.435  2.069   1.00 54.63  ? 493 TYR A O     1 
ATOM   3818 C  CB    . TYR A 1 493 ? 2.112   14.968  2.140   1.00 51.40  ? 493 TYR A CB    1 
ATOM   3819 C  CG    . TYR A 1 493 ? 1.085   14.241  2.982   1.00 50.50  ? 493 TYR A CG    1 
ATOM   3820 C  CD1   . TYR A 1 493 ? 0.335   13.201  2.452   1.00 52.75  ? 493 TYR A CD1   1 
ATOM   3821 C  CD2   . TYR A 1 493 ? 0.900   14.564  4.320   1.00 53.85  ? 493 TYR A CD2   1 
ATOM   3822 C  CE1   . TYR A 1 493 ? -0.588  12.514  3.222   1.00 50.16  ? 493 TYR A CE1   1 
ATOM   3823 C  CE2   . TYR A 1 493 ? -0.025  13.882  5.101   1.00 55.01  ? 493 TYR A CE2   1 
ATOM   3824 C  CZ    . TYR A 1 493 ? -0.764  12.858  4.543   1.00 49.43  ? 493 TYR A CZ    1 
ATOM   3825 O  OH    . TYR A 1 493 ? -1.686  12.174  5.305   1.00 52.15  ? 493 TYR A OH    1 
ATOM   3826 N  N     . LEU A 1 494 ? 1.680   17.823  3.081   1.00 52.04  ? 494 LEU A N     1 
ATOM   3827 C  CA    . LEU A 1 494 ? 1.133   18.873  3.934   1.00 50.48  ? 494 LEU A CA    1 
ATOM   3828 C  C     . LEU A 1 494 ? 0.423   19.940  3.108   1.00 55.38  ? 494 LEU A C     1 
ATOM   3829 O  O     . LEU A 1 494 ? -0.697  20.350  3.430   1.00 53.32  ? 494 LEU A O     1 
ATOM   3830 C  CB    . LEU A 1 494 ? 2.252   19.493  4.771   1.00 52.42  ? 494 LEU A CB    1 
ATOM   3831 C  CG    . LEU A 1 494 ? 2.891   18.559  5.799   1.00 49.99  ? 494 LEU A CG    1 
ATOM   3832 C  CD1   . LEU A 1 494 ? 4.126   19.185  6.426   1.00 50.46  ? 494 LEU A CD1   1 
ATOM   3833 C  CD2   . LEU A 1 494 ? 1.876   18.201  6.864   1.00 51.44  ? 494 LEU A CD2   1 
ATOM   3834 N  N     . ALA A 1 495 ? 1.066   20.405  2.034   1.00 60.95  ? 495 ALA A N     1 
ATOM   3835 C  CA    . ALA A 1 495 ? 0.433   21.404  1.178   1.00 61.96  ? 495 ALA A CA    1 
ATOM   3836 C  C     . ALA A 1 495 ? -0.881  20.884  0.608   1.00 64.00  ? 495 ALA A C     1 
ATOM   3837 O  O     . ALA A 1 495 ? -1.871  21.620  0.533   1.00 64.15  ? 495 ALA A O     1 
ATOM   3838 C  CB    . ALA A 1 495 ? 1.384   21.813  0.055   1.00 58.39  ? 495 ALA A CB    1 
ATOM   3839 N  N     . HIS A 1 496 ? -0.906  19.615  0.197   1.00 57.10  ? 496 HIS A N     1 
ATOM   3840 C  CA    . HIS A 1 496 ? -2.138  19.020  -0.308  1.00 54.38  ? 496 HIS A CA    1 
ATOM   3841 C  C     . HIS A 1 496 ? -3.259  19.126  0.721   1.00 59.80  ? 496 HIS A C     1 
ATOM   3842 O  O     . HIS A 1 496 ? -4.394  19.484  0.383   1.00 55.60  ? 496 HIS A O     1 
ATOM   3843 C  CB    . HIS A 1 496 ? -1.875  17.561  -0.690  1.00 57.55  ? 496 HIS A CB    1 
ATOM   3844 C  CG    . HIS A 1 496 ? -2.987  16.919  -1.459  1.00 62.43  ? 496 HIS A CG    1 
ATOM   3845 N  ND1   . HIS A 1 496 ? -3.620  17.540  -2.514  1.00 58.56  ? 496 HIS A ND1   1 
ATOM   3846 C  CD2   . HIS A 1 496 ? -3.568  15.702  -1.335  1.00 54.39  ? 496 HIS A CD2   1 
ATOM   3847 C  CE1   . HIS A 1 496 ? -4.549  16.737  -3.001  1.00 58.90  ? 496 HIS A CE1   1 
ATOM   3848 N  NE2   . HIS A 1 496 ? -4.538  15.615  -2.304  1.00 56.96  ? 496 HIS A NE2   1 
ATOM   3849 N  N     . TRP A 1 497 ? -2.953  18.835  1.987   1.00 55.90  ? 497 TRP A N     1 
ATOM   3850 C  CA    . TRP A 1 497 ? -3.964  18.912  3.036   1.00 52.30  ? 497 TRP A CA    1 
ATOM   3851 C  C     . TRP A 1 497 ? -4.450  20.342  3.234   1.00 60.86  ? 497 TRP A C     1 
ATOM   3852 O  O     . TRP A 1 497 ? -5.659  20.599  3.284   1.00 56.66  ? 497 TRP A O     1 
ATOM   3853 C  CB    . TRP A 1 497 ? -3.400  18.349  4.339   1.00 49.48  ? 497 TRP A CB    1 
ATOM   3854 C  CG    . TRP A 1 497 ? -3.649  16.884  4.500   1.00 51.94  ? 497 TRP A CG    1 
ATOM   3855 C  CD1   . TRP A 1 497 ? -2.977  15.864  3.892   1.00 49.70  ? 497 TRP A CD1   1 
ATOM   3856 C  CD2   . TRP A 1 497 ? -4.646  16.274  5.325   1.00 48.60  ? 497 TRP A CD2   1 
ATOM   3857 N  NE1   . TRP A 1 497 ? -3.495  14.655  4.287   1.00 54.73  ? 497 TRP A NE1   1 
ATOM   3858 C  CE2   . TRP A 1 497 ? -4.521  14.880  5.167   1.00 48.59  ? 497 TRP A CE2   1 
ATOM   3859 C  CE3   . TRP A 1 497 ? -5.632  16.771  6.182   1.00 48.36  ? 497 TRP A CE3   1 
ATOM   3860 C  CZ2   . TRP A 1 497 ? -5.345  13.978  5.834   1.00 48.87  ? 497 TRP A CZ2   1 
ATOM   3861 C  CZ3   . TRP A 1 497 ? -6.449  15.873  6.842   1.00 49.48  ? 497 TRP A CZ3   1 
ATOM   3862 C  CH2   . TRP A 1 497 ? -6.300  14.492  6.665   1.00 48.11  ? 497 TRP A CH2   1 
ATOM   3863 N  N     . LEU A 1 498 ? -3.515  21.290  3.353   1.00 60.32  ? 498 LEU A N     1 
ATOM   3864 C  CA    . LEU A 1 498 ? -3.894  22.686  3.546   1.00 54.73  ? 498 LEU A CA    1 
ATOM   3865 C  C     . LEU A 1 498 ? -4.762  23.191  2.404   1.00 59.04  ? 498 LEU A C     1 
ATOM   3866 O  O     . LEU A 1 498 ? -5.647  24.027  2.620   1.00 62.25  ? 498 LEU A O     1 
ATOM   3867 C  CB    . LEU A 1 498 ? -2.642  23.551  3.694   1.00 52.25  ? 498 LEU A CB    1 
ATOM   3868 C  CG    . LEU A 1 498 ? -1.755  23.185  4.888   1.00 52.40  ? 498 LEU A CG    1 
ATOM   3869 C  CD1   . LEU A 1 498 ? -0.403  23.859  4.794   1.00 52.05  ? 498 LEU A CD1   1 
ATOM   3870 C  CD2   . LEU A 1 498 ? -2.437  23.543  6.199   1.00 50.93  ? 498 LEU A CD2   1 
ATOM   3871 N  N     . SER A 1 499 ? -4.540  22.686  1.188   1.00 59.88  ? 499 SER A N     1 
ATOM   3872 C  CA    . SER A 1 499 ? -5.321  23.133  0.041   1.00 63.79  ? 499 SER A CA    1 
ATOM   3873 C  C     . SER A 1 499 ? -6.805  22.840  0.202   1.00 63.00  ? 499 SER A C     1 
ATOM   3874 O  O     . SER A 1 499 ? -7.630  23.509  -0.430  1.00 68.53  ? 499 SER A O     1 
ATOM   3875 C  CB    . SER A 1 499 ? -4.802  22.479  -1.243  1.00 60.69  ? 499 SER A CB    1 
ATOM   3876 O  OG    . SER A 1 499 ? -5.070  21.087  -1.257  1.00 69.29  ? 499 SER A OG    1 
ATOM   3877 N  N     A MET A 1 500 ? -7.170  21.863  1.033   0.66 64.30  ? 500 MET A N     1 
ATOM   3878 N  N     B MET A 1 500 ? -7.161  21.848  1.023   0.34 63.55  ? 500 MET A N     1 
ATOM   3879 C  CA    A MET A 1 500 ? -8.584  21.549  1.204   0.66 63.66  ? 500 MET A CA    1 
ATOM   3880 C  CA    B MET A 1 500 ? -8.569  21.533  1.241   0.34 66.25  ? 500 MET A CA    1 
ATOM   3881 C  C     A MET A 1 500 ? -9.354  22.730  1.784   0.66 70.32  ? 500 MET A C     1 
ATOM   3882 C  C     B MET A 1 500 ? -9.337  22.740  1.761   0.34 69.22  ? 500 MET A C     1 
ATOM   3883 O  O     A MET A 1 500 ? -10.553 22.875  1.523   0.66 73.70  ? 500 MET A O     1 
ATOM   3884 O  O     B MET A 1 500 ? -10.519 22.910  1.440   0.34 71.38  ? 500 MET A O     1 
ATOM   3885 C  CB    A MET A 1 500 ? -8.743  20.310  2.083   0.66 63.32  ? 500 MET A CB    1 
ATOM   3886 C  CB    B MET A 1 500 ? -8.699  20.361  2.215   0.34 63.49  ? 500 MET A CB    1 
ATOM   3887 C  CG    A MET A 1 500 ? -8.055  19.070  1.529   0.66 63.67  ? 500 MET A CG    1 
ATOM   3888 C  CG    B MET A 1 500 ? -8.102  19.059  1.706   0.34 63.86  ? 500 MET A CG    1 
ATOM   3889 S  SD    A MET A 1 500 ? -8.574  18.670  -0.154  0.66 74.83  ? 500 MET A SD    1 
ATOM   3890 S  SD    B MET A 1 500 ? -7.995  17.785  2.981   0.34 57.46  ? 500 MET A SD    1 
ATOM   3891 C  CE    A MET A 1 500 ? -7.573  17.222  -0.487  0.66 60.15  ? 500 MET A CE    1 
ATOM   3892 C  CE    B MET A 1 500 ? -9.707  17.633  3.476   0.34 62.29  ? 500 MET A CE    1 
ATOM   3893 N  N     . ALA A 1 501 ? -8.688  23.588  2.561   1.00 65.88  ? 501 ALA A N     1 
ATOM   3894 C  CA    . ALA A 1 501 ? -9.339  24.778  3.094   1.00 68.21  ? 501 ALA A CA    1 
ATOM   3895 C  C     . ALA A 1 501 ? -9.651  25.813  2.020   1.00 77.75  ? 501 ALA A C     1 
ATOM   3896 O  O     . ALA A 1 501 ? -10.320 26.807  2.320   1.00 73.05  ? 501 ALA A O     1 
ATOM   3897 C  CB    . ALA A 1 501 ? -8.469  25.413  4.180   1.00 67.94  ? 501 ALA A CB    1 
ATOM   3898 N  N     . HIS A 1 502 ? -9.182  25.610  0.788   1.00 78.35  ? 502 HIS A N     1 
ATOM   3899 C  CA    . HIS A 1 502 ? -9.443  26.527  -0.312  1.00 80.33  ? 502 HIS A CA    1 
ATOM   3900 C  C     . HIS A 1 502 ? -10.622 26.105  -1.181  1.00 86.85  ? 502 HIS A C     1 
ATOM   3901 O  O     . HIS A 1 502 ? -11.046 26.886  -2.040  1.00 96.24  ? 502 HIS A O     1 
ATOM   3902 C  CB    . HIS A 1 502 ? -8.196  26.664  -1.197  1.00 82.81  ? 502 HIS A CB    1 
ATOM   3903 C  CG    . HIS A 1 502 ? -6.982  27.150  -0.467  1.00 83.30  ? 502 HIS A CG    1 
ATOM   3904 N  ND1   . HIS A 1 502 ? -5.702  26.959  -0.945  1.00 87.85  ? 502 HIS A ND1   1 
ATOM   3905 C  CD2   . HIS A 1 502 ? -6.851  27.822  0.700   1.00 83.43  ? 502 HIS A CD2   1 
ATOM   3906 C  CE1   . HIS A 1 502 ? -4.836  27.491  -0.101  1.00 89.00  ? 502 HIS A CE1   1 
ATOM   3907 N  NE2   . HIS A 1 502 ? -5.507  28.021  0.906   1.00 88.27  ? 502 HIS A NE2   1 
ATOM   3908 N  N     . ARG A 1 503 ? -11.156 24.903  -0.985  1.00 86.98  ? 503 ARG A N     1 
ATOM   3909 C  CA    . ARG A 1 503 ? -12.212 24.410  -1.852  1.00 99.09  ? 503 ARG A CA    1 
ATOM   3910 C  C     . ARG A 1 503 ? -13.515 25.170  -1.606  1.00 111.28 ? 503 ARG A C     1 
ATOM   3911 O  O     . ARG A 1 503 ? -13.765 25.654  -0.498  1.00 105.72 ? 503 ARG A O     1 
ATOM   3912 C  CB    . ARG A 1 503 ? -12.434 22.916  -1.631  1.00 96.67  ? 503 ARG A CB    1 
ATOM   3913 C  CG    . ARG A 1 503 ? -11.192 22.068  -1.836  1.00 87.30  ? 503 ARG A CG    1 
ATOM   3914 C  CD    . ARG A 1 503 ? -11.499 20.591  -1.657  1.00 94.10  ? 503 ARG A CD    1 
ATOM   3915 N  NE    . ARG A 1 503 ? -12.341 20.069  -2.728  1.00 101.68 ? 503 ARG A NE    1 
ATOM   3916 C  CZ    . ARG A 1 503 ? -11.883 19.425  -3.793  1.00 97.52  ? 503 ARG A CZ    1 
ATOM   3917 N  NH1   . ARG A 1 503 ? -10.590 19.201  -3.962  1.00 91.48  ? 503 ARG A NH1   1 
ATOM   3918 N  NH2   . ARG A 1 503 ? -12.745 18.991  -4.709  1.00 101.36 ? 503 ARG A NH2   1 
ATOM   3919 N  N     . PRO A 1 504 ? -14.364 25.288  -2.628  1.00 127.11 ? 504 PRO A N     1 
ATOM   3920 C  CA    . PRO A 1 504 ? -15.637 26.002  -2.456  1.00 129.65 ? 504 PRO A CA    1 
ATOM   3921 C  C     . PRO A 1 504 ? -16.608 25.202  -1.598  1.00 128.88 ? 504 PRO A C     1 
ATOM   3922 O  O     . PRO A 1 504 ? -16.787 23.998  -1.794  1.00 128.98 ? 504 PRO A O     1 
ATOM   3923 C  CB    . PRO A 1 504 ? -16.156 26.161  -3.893  1.00 134.30 ? 504 PRO A CB    1 
ATOM   3924 C  CG    . PRO A 1 504 ? -14.967 25.895  -4.778  1.00 133.27 ? 504 PRO A CG    1 
ATOM   3925 C  CD    . PRO A 1 504 ? -14.131 24.906  -4.030  1.00 129.78 ? 504 PRO A CD    1 
ATOM   3926 N  N     . ALA A 1 505 ? -17.239 25.888  -0.644  1.00 109.09 ? 505 ALA A N     1 
ATOM   3927 C  CA    . ALA A 1 505 ? -18.251 25.282  0.220   1.00 94.97  ? 505 ALA A CA    1 
ATOM   3928 C  C     . ALA A 1 505 ? -17.728 24.006  0.874   1.00 91.44  ? 505 ALA A C     1 
ATOM   3929 O  O     . ALA A 1 505 ? -18.460 23.033  1.068   1.00 89.63  ? 505 ALA A O     1 
ATOM   3930 C  CB    . ALA A 1 505 ? -19.540 25.008  -0.555  1.00 91.82  ? 505 ALA A CB    1 
ATOM   3931 N  N     . ALA A 1 506 ? -16.444 24.012  1.220   1.00 92.11  ? 506 ALA A N     1 
ATOM   3932 C  CA    . ALA A 1 506 ? -15.816 22.855  1.843   1.00 85.57  ? 506 ALA A CA    1 
ATOM   3933 C  C     . ALA A 1 506 ? -16.243 22.765  3.303   1.00 81.05  ? 506 ALA A C     1 
ATOM   3934 O  O     . ALA A 1 506 ? -15.970 23.676  4.092   1.00 82.06  ? 506 ALA A O     1 
ATOM   3935 C  CB    . ALA A 1 506 ? -14.297 22.946  1.730   1.00 87.33  ? 506 ALA A CB    1 
ATOM   3936 N  N     . LYS A 1 507 ? -16.918 21.671  3.659   1.00 80.19  ? 507 LYS A N     1 
ATOM   3937 C  CA    . LYS A 1 507 ? -17.319 21.421  5.043   1.00 73.31  ? 507 LYS A CA    1 
ATOM   3938 C  C     . LYS A 1 507 ? -16.173 20.699  5.744   1.00 70.03  ? 507 LYS A C     1 
ATOM   3939 O  O     . LYS A 1 507 ? -16.182 19.482  5.937   1.00 70.88  ? 507 LYS A O     1 
ATOM   3940 C  CB    . LYS A 1 507 ? -18.612 20.618  5.092   1.00 74.38  ? 507 LYS A CB    1 
ATOM   3941 C  CG    . LYS A 1 507 ? -19.787 21.292  4.403   1.00 82.54  ? 507 LYS A CG    1 
ATOM   3942 C  CD    . LYS A 1 507 ? -20.973 20.349  4.288   1.00 82.30  ? 507 LYS A CD    1 
ATOM   3943 C  CE    . LYS A 1 507 ? -22.089 20.963  3.458   1.00 83.46  ? 507 LYS A CE    1 
ATOM   3944 N  NZ    . LYS A 1 507 ? -23.156 19.970  3.146   1.00 88.19  ? 507 LYS A NZ    1 
ATOM   3945 N  N     . LEU A 1 508 ? -15.166 21.472  6.127   1.00 72.00  ? 508 LEU A N     1 
ATOM   3946 C  CA    . LEU A 1 508 ? -13.993 20.898  6.776   1.00 67.39  ? 508 LEU A CA    1 
ATOM   3947 C  C     . LEU A 1 508 ? -14.383 20.292  8.122   1.00 64.28  ? 508 LEU A C     1 
ATOM   3948 O  O     . LEU A 1 508 ? -15.014 20.970  8.941   1.00 68.30  ? 508 LEU A O     1 
ATOM   3949 C  CB    . LEU A 1 508 ? -12.919 21.966  6.969   1.00 57.14  ? 508 LEU A CB    1 
ATOM   3950 C  CG    . LEU A 1 508 ? -12.461 22.718  5.715   1.00 65.60  ? 508 LEU A CG    1 
ATOM   3951 C  CD1   . LEU A 1 508 ? -11.535 23.862  6.097   1.00 58.25  ? 508 LEU A CD1   1 
ATOM   3952 C  CD2   . LEU A 1 508 ? -11.780 21.780  4.724   1.00 63.03  ? 508 LEU A CD2   1 
ATOM   3953 N  N     . PRO A 1 509 ? -14.037 19.038  8.386   1.00 59.35  ? 509 PRO A N     1 
ATOM   3954 C  CA    . PRO A 1 509 ? -14.369 18.434  9.678   1.00 60.04  ? 509 PRO A CA    1 
ATOM   3955 C  C     . PRO A 1 509 ? -13.435 18.912  10.781  1.00 62.48  ? 509 PRO A C     1 
ATOM   3956 O  O     . PRO A 1 509 ? -12.309 19.352  10.540  1.00 53.59  ? 509 PRO A O     1 
ATOM   3957 C  CB    . PRO A 1 509 ? -14.187 16.935  9.421   1.00 52.87  ? 509 PRO A CB    1 
ATOM   3958 C  CG    . PRO A 1 509 ? -13.141 16.877  8.365   1.00 53.99  ? 509 PRO A CG    1 
ATOM   3959 C  CD    . PRO A 1 509 ? -13.362 18.086  7.487   1.00 61.96  ? 509 PRO A CD    1 
ATOM   3960 N  N     . LYS A 1 510 ? -13.931 18.816  12.013  1.00 53.79  ? 510 LYS A N     1 
ATOM   3961 C  CA    . LYS A 1 510 ? -13.105 19.151  13.160  1.00 50.53  ? 510 LYS A CA    1 
ATOM   3962 C  C     . LYS A 1 510 ? -11.941 18.173  13.266  1.00 49.67  ? 510 LYS A C     1 
ATOM   3963 O  O     . LYS A 1 510 ? -11.953 17.084  12.689  1.00 49.35  ? 510 LYS A O     1 
ATOM   3964 C  CB    . LYS A 1 510 ? -13.929 19.143  14.448  1.00 51.29  ? 510 LYS A CB    1 
ATOM   3965 C  CG    . LYS A 1 510 ? -14.899 20.305  14.553  1.00 57.65  ? 510 LYS A CG    1 
ATOM   3966 C  CD    . LYS A 1 510 ? -15.208 20.651  15.998  1.00 55.13  ? 510 LYS A CD    1 
ATOM   3967 C  CE    . LYS A 1 510 ? -15.825 22.038  16.099  1.00 54.37  ? 510 LYS A CE    1 
ATOM   3968 N  NZ    . LYS A 1 510 ? -14.962 23.058  15.442  1.00 65.04  ? 510 LYS A NZ    1 
ATOM   3969 N  N     . ILE A 1 511 ? -10.918 18.580  14.010  1.00 49.50  ? 511 ILE A N     1 
ATOM   3970 C  CA    . ILE A 1 511 ? -9.694  17.803  14.152  1.00 48.89  ? 511 ILE A CA    1 
ATOM   3971 C  C     . ILE A 1 511 ? -9.364  17.706  15.632  1.00 49.29  ? 511 ILE A C     1 
ATOM   3972 O  O     . ILE A 1 511 ? -9.205  18.731  16.304  1.00 49.81  ? 511 ILE A O     1 
ATOM   3973 C  CB    . ILE A 1 511 ? -8.525  18.426  13.373  1.00 48.50  ? 511 ILE A CB    1 
ATOM   3974 C  CG1   . ILE A 1 511 ? -8.761  18.295  11.864  1.00 50.12  ? 511 ILE A CG1   1 
ATOM   3975 C  CG2   . ILE A 1 511 ? -7.206  17.788  13.787  1.00 48.14  ? 511 ILE A CG2   1 
ATOM   3976 C  CD1   . ILE A 1 511 ? -7.692  18.959  11.014  1.00 53.48  ? 511 ILE A CD1   1 
ATOM   3977 N  N     . PHE A 1 512 ? -9.262  16.482  16.137  1.00 50.13  ? 512 PHE A N     1 
ATOM   3978 C  CA    . PHE A 1 512 ? -8.974  16.231  17.538  1.00 49.91  ? 512 PHE A CA    1 
ATOM   3979 C  C     . PHE A 1 512 ? -7.668  15.460  17.665  1.00 49.62  ? 512 PHE A C     1 
ATOM   3980 O  O     . PHE A 1 512 ? -7.229  14.784  16.732  1.00 49.09  ? 512 PHE A O     1 
ATOM   3981 C  CB    . PHE A 1 512 ? -10.107 15.440  18.206  1.00 50.61  ? 512 PHE A CB    1 
ATOM   3982 C  CG    . PHE A 1 512 ? -11.463 16.071  18.055  1.00 51.08  ? 512 PHE A CG    1 
ATOM   3983 C  CD1   . PHE A 1 512 ? -11.931 16.976  18.999  1.00 52.04  ? 512 PHE A CD1   1 
ATOM   3984 C  CD2   . PHE A 1 512 ? -12.276 15.751  16.978  1.00 50.78  ? 512 PHE A CD2   1 
ATOM   3985 C  CE1   . PHE A 1 512 ? -13.184 17.558  18.870  1.00 52.66  ? 512 PHE A CE1   1 
ATOM   3986 C  CE2   . PHE A 1 512 ? -13.529 16.325  16.840  1.00 51.41  ? 512 PHE A CE2   1 
ATOM   3987 C  CZ    . PHE A 1 512 ? -13.984 17.233  17.790  1.00 52.33  ? 512 PHE A CZ    1 
ATOM   3988 N  N     . HIS A 1 513 ? -7.045  15.575  18.835  1.00 50.31  ? 513 HIS A N     1 
ATOM   3989 C  CA    . HIS A 1 513 ? -5.891  14.762  19.195  1.00 50.42  ? 513 HIS A CA    1 
ATOM   3990 C  C     . HIS A 1 513 ? -6.184  14.063  20.515  1.00 51.56  ? 513 HIS A C     1 
ATOM   3991 O  O     . HIS A 1 513 ? -6.471  14.722  21.521  1.00 52.51  ? 513 HIS A O     1 
ATOM   3992 C  CB    . HIS A 1 513 ? -4.621  15.606  19.301  1.00 50.48  ? 513 HIS A CB    1 
ATOM   3993 C  CG    . HIS A 1 513 ? -3.365  14.794  19.360  1.00 50.54  ? 513 HIS A CG    1 
ATOM   3994 N  ND1   . HIS A 1 513 ? -2.755  14.449  20.547  1.00 54.00  ? 513 HIS A ND1   1 
ATOM   3995 C  CD2   . HIS A 1 513 ? -2.608  14.250  18.377  1.00 49.88  ? 513 HIS A CD2   1 
ATOM   3996 C  CE1   . HIS A 1 513 ? -1.674  13.733  20.293  1.00 51.58  ? 513 HIS A CE1   1 
ATOM   3997 N  NE2   . HIS A 1 513 ? -1.562  13.598  18.984  1.00 50.53  ? 513 HIS A NE2   1 
ATOM   3998 N  N     . VAL A 1 514 ? -6.116  12.735  20.506  1.00 51.67  ? 514 VAL A N     1 
ATOM   3999 C  CA    . VAL A 1 514 ? -6.385  11.927  21.686  1.00 52.95  ? 514 VAL A CA    1 
ATOM   4000 C  C     . VAL A 1 514 ? -5.098  11.239  22.115  1.00 53.47  ? 514 VAL A C     1 
ATOM   4001 O  O     . VAL A 1 514 ? -4.162  11.060  21.331  1.00 52.74  ? 514 VAL A O     1 
ATOM   4002 C  CB    . VAL A 1 514 ? -7.498  10.891  21.434  1.00 53.10  ? 514 VAL A CB    1 
ATOM   4003 C  CG1   . VAL A 1 514 ? -8.750  11.576  20.917  1.00 52.69  ? 514 VAL A CG1   1 
ATOM   4004 C  CG2   . VAL A 1 514 ? -7.021  9.833   20.457  1.00 52.47  ? 514 VAL A CG2   1 
ATOM   4005 N  N     . ASN A 1 515 ? -5.053  10.859  23.390  1.00 54.98  ? 515 ASN A N     1 
ATOM   4006 C  CA    . ASN A 1 515 ? -3.930  10.103  23.943  1.00 55.91  ? 515 ASN A CA    1 
ATOM   4007 C  C     . ASN A 1 515 ? -4.508  9.079   24.916  1.00 59.27  ? 515 ASN A C     1 
ATOM   4008 O  O     . ASN A 1 515 ? -4.835  9.416   26.058  1.00 62.52  ? 515 ASN A O     1 
ATOM   4009 C  CB    . ASN A 1 515 ? -2.920  11.016  24.628  1.00 56.58  ? 515 ASN A CB    1 
ATOM   4010 C  CG    . ASN A 1 515 ? -1.766  10.246  25.249  1.00 57.82  ? 515 ASN A CG    1 
ATOM   4011 O  OD1   . ASN A 1 515 ? -1.512  9.095   24.894  1.00 60.68  ? 515 ASN A OD1   1 
ATOM   4012 N  ND2   . ASN A 1 515 ? -1.063  10.878  26.183  1.00 59.08  ? 515 ASN A ND2   1 
ATOM   4013 N  N     . TRP A 1 516 ? -4.645  7.835   24.458  1.00 57.47  ? 516 TRP A N     1 
ATOM   4014 C  CA    . TRP A 1 516 ? -5.121  6.765   25.323  1.00 59.18  ? 516 TRP A CA    1 
ATOM   4015 C  C     . TRP A 1 516 ? -4.076  6.302   26.326  1.00 61.58  ? 516 TRP A C     1 
ATOM   4016 O  O     . TRP A 1 516 ? -4.420  5.554   27.248  1.00 67.60  ? 516 TRP A O     1 
ATOM   4017 C  CB    . TRP A 1 516 ? -5.553  5.539   24.506  1.00 58.90  ? 516 TRP A CB    1 
ATOM   4018 C  CG    . TRP A 1 516 ? -6.621  5.746   23.469  1.00 57.58  ? 516 TRP A CG    1 
ATOM   4019 C  CD1   . TRP A 1 516 ? -6.828  4.979   22.358  1.00 57.07  ? 516 TRP A CD1   1 
ATOM   4020 C  CD2   . TRP A 1 516 ? -7.630  6.764   23.444  1.00 57.04  ? 516 TRP A CD2   1 
ATOM   4021 N  NE1   . TRP A 1 516 ? -7.897  5.455   21.643  1.00 56.00  ? 516 TRP A NE1   1 
ATOM   4022 C  CE2   . TRP A 1 516 ? -8.407  6.552   22.286  1.00 56.05  ? 516 TRP A CE2   1 
ATOM   4023 C  CE3   . TRP A 1 516 ? -7.951  7.835   24.282  1.00 58.96  ? 516 TRP A CE3   1 
ATOM   4024 C  CZ2   . TRP A 1 516 ? -9.482  7.370   21.947  1.00 55.50  ? 516 TRP A CZ2   1 
ATOM   4025 C  CZ3   . TRP A 1 516 ? -9.020  8.646   23.942  1.00 60.78  ? 516 TRP A CZ3   1 
ATOM   4026 C  CH2   . TRP A 1 516 ? -9.773  8.408   22.786  1.00 55.93  ? 516 TRP A CH2   1 
ATOM   4027 N  N     . PHE A 1 517 ? -2.817  6.719   26.178  1.00 60.55  ? 517 PHE A N     1 
ATOM   4028 C  CA    . PHE A 1 517 ? -1.706  6.013   26.806  1.00 62.50  ? 517 PHE A CA    1 
ATOM   4029 C  C     . PHE A 1 517 ? -0.878  6.890   27.737  1.00 63.19  ? 517 PHE A C     1 
ATOM   4030 O  O     . PHE A 1 517 ? 0.274   6.555   28.028  1.00 64.90  ? 517 PHE A O     1 
ATOM   4031 C  CB    . PHE A 1 517 ? -0.813  5.393   25.730  1.00 65.87  ? 517 PHE A CB    1 
ATOM   4032 C  CG    . PHE A 1 517 ? -1.554  4.502   24.773  1.00 67.54  ? 517 PHE A CG    1 
ATOM   4033 C  CD1   . PHE A 1 517 ? -1.709  3.150   25.041  1.00 64.50  ? 517 PHE A CD1   1 
ATOM   4034 C  CD2   . PHE A 1 517 ? -2.105  5.017   23.610  1.00 62.36  ? 517 PHE A CD2   1 
ATOM   4035 C  CE1   . PHE A 1 517 ? -2.394  2.327   24.165  1.00 61.23  ? 517 PHE A CE1   1 
ATOM   4036 C  CE2   . PHE A 1 517 ? -2.792  4.199   22.728  1.00 63.39  ? 517 PHE A CE2   1 
ATOM   4037 C  CZ    . PHE A 1 517 ? -2.937  2.851   23.007  1.00 59.48  ? 517 PHE A CZ    1 
ATOM   4038 N  N     . ARG A 1 518 ? -1.431  7.996   28.225  1.00 63.55  ? 518 ARG A N     1 
ATOM   4039 C  CA    . ARG A 1 518 ? -0.701  8.797   29.196  1.00 72.06  ? 518 ARG A CA    1 
ATOM   4040 C  C     . ARG A 1 518 ? -0.522  8.010   30.488  1.00 82.91  ? 518 ARG A C     1 
ATOM   4041 O  O     . ARG A 1 518 ? -1.451  7.357   30.972  1.00 78.07  ? 518 ARG A O     1 
ATOM   4042 C  CB    . ARG A 1 518 ? -1.424  10.115  29.471  1.00 70.26  ? 518 ARG A CB    1 
ATOM   4043 C  CG    . ARG A 1 518 ? -0.600  11.099  30.293  1.00 71.69  ? 518 ARG A CG    1 
ATOM   4044 C  CD    . ARG A 1 518 ? -1.270  12.460  30.382  1.00 71.07  ? 518 ARG A CD    1 
ATOM   4045 N  NE    . ARG A 1 518 ? -0.377  13.473  30.931  1.00 71.41  ? 518 ARG A NE    1 
ATOM   4046 C  CZ    . ARG A 1 518 ? -0.600  14.779  30.866  1.00 76.71  ? 518 ARG A CZ    1 
ATOM   4047 N  NH1   . ARG A 1 518 ? -1.687  15.267  30.290  1.00 72.16  ? 518 ARG A NH1   1 
ATOM   4048 N  NH2   . ARG A 1 518 ? 0.295   15.618  31.383  1.00 74.05  ? 518 ARG A NH2   1 
ATOM   4049 N  N     . LYS A 1 519 ? 0.687   8.062   31.039  1.00 87.49  ? 519 LYS A N     1 
ATOM   4050 C  CA    . LYS A 1 519 ? 1.030   7.333   32.248  1.00 97.91  ? 519 LYS A CA    1 
ATOM   4051 C  C     . LYS A 1 519 ? 1.352   8.305   33.376  1.00 116.22 ? 519 LYS A C     1 
ATOM   4052 O  O     . LYS A 1 519 ? 1.611   9.491   33.151  1.00 112.18 ? 519 LYS A O     1 
ATOM   4053 C  CB    . LYS A 1 519 ? 2.223   6.395   32.014  1.00 102.51 ? 519 LYS A CB    1 
ATOM   4054 C  CG    . LYS A 1 519 ? 1.959   5.276   31.019  1.00 92.85  ? 519 LYS A CG    1 
ATOM   4055 C  CD    . LYS A 1 519 ? 3.104   4.274   31.009  1.00 95.65  ? 519 LYS A CD    1 
ATOM   4056 C  CE    . LYS A 1 519 ? 2.756   3.039   30.195  1.00 92.30  ? 519 LYS A CE    1 
ATOM   4057 N  NZ    . LYS A 1 519 ? 3.776   1.965   30.357  1.00 104.63 ? 519 LYS A NZ    1 
ATOM   4058 N  N     . ASP A 1 520 ? 1.335   7.784   34.597  1.00 149.57 ? 520 ASP A N     1 
ATOM   4059 C  CA    . ASP A 1 520 ? 1.671   8.547   35.785  1.00 153.61 ? 520 ASP A CA    1 
ATOM   4060 C  C     . ASP A 1 520 ? 3.119   8.260   36.183  1.00 156.89 ? 520 ASP A C     1 
ATOM   4061 O  O     . ASP A 1 520 ? 3.889   7.658   35.429  1.00 156.02 ? 520 ASP A O     1 
ATOM   4062 C  CB    . ASP A 1 520 ? 0.689   8.221   36.911  1.00 154.53 ? 520 ASP A CB    1 
ATOM   4063 C  CG    . ASP A 1 520 ? 0.632   6.739   37.225  1.00 154.16 ? 520 ASP A CG    1 
ATOM   4064 O  OD1   . ASP A 1 520 ? 1.363   5.963   36.573  1.00 153.21 ? 520 ASP A OD1   1 
ATOM   4065 O  OD2   . ASP A 1 520 ? -0.143  6.348   38.122  1.00 154.95 ? 520 ASP A OD2   1 
ATOM   4066 N  N     . LYS A 1 521 ? 3.499   8.692   37.387  1.00 132.86 ? 521 LYS A N     1 
ATOM   4067 C  CA    . LYS A 1 521 ? 4.863   8.493   37.857  1.00 126.00 ? 521 LYS A CA    1 
ATOM   4068 C  C     . LYS A 1 521 ? 5.160   7.044   38.221  1.00 124.77 ? 521 LYS A C     1 
ATOM   4069 O  O     . LYS A 1 521 ? 6.329   6.707   38.442  1.00 120.01 ? 521 LYS A O     1 
ATOM   4070 C  CB    . LYS A 1 521 ? 5.138   9.400   39.059  1.00 118.91 ? 521 LYS A CB    1 
ATOM   4071 C  CG    . LYS A 1 521 ? 4.994   10.883  38.753  1.00 118.85 ? 521 LYS A CG    1 
ATOM   4072 C  CD    . LYS A 1 521 ? 5.309   11.736  39.971  1.00 109.00 ? 521 LYS A CD    1 
ATOM   4073 C  CE    . LYS A 1 521 ? 5.217   13.218  39.642  1.00 108.23 ? 521 LYS A CE    1 
ATOM   4074 N  NZ    . LYS A 1 521 ? 5.485   14.074  40.830  1.00 119.08 ? 521 LYS A NZ    1 
ATOM   4075 N  N     . ASN A 1 522 ? 4.145   6.184   38.283  1.00 123.78 ? 522 ASN A N     1 
ATOM   4076 C  CA    . ASN A 1 522 ? 4.329   4.777   38.608  1.00 119.50 ? 522 ASN A CA    1 
ATOM   4077 C  C     . ASN A 1 522 ? 4.310   3.878   37.380  1.00 118.69 ? 522 ASN A C     1 
ATOM   4078 O  O     . ASN A 1 522 ? 4.559   2.676   37.506  1.00 112.05 ? 522 ASN A O     1 
ATOM   4079 C  CB    . ASN A 1 522 ? 3.247   4.314   39.592  1.00 126.04 ? 522 ASN A CB    1 
ATOM   4080 C  CG    . ASN A 1 522 ? 3.170   5.183   40.830  1.00 121.79 ? 522 ASN A CG    1 
ATOM   4081 O  OD1   . ASN A 1 522 ? 4.097   5.934   41.133  1.00 118.21 ? 522 ASN A OD1   1 
ATOM   4082 N  ND2   . ASN A 1 522 ? 2.063   5.081   41.558  1.00 112.08 ? 522 ASN A ND2   1 
ATOM   4083 N  N     . GLY A 1 523 ? 4.024   4.428   36.202  1.00 123.24 ? 523 GLY A N     1 
ATOM   4084 C  CA    . GLY A 1 523 ? 3.857   3.609   35.020  1.00 117.09 ? 523 GLY A CA    1 
ATOM   4085 C  C     . GLY A 1 523 ? 2.465   3.051   34.842  1.00 116.96 ? 523 GLY A C     1 
ATOM   4086 O  O     . GLY A 1 523 ? 2.280   2.102   34.074  1.00 107.20 ? 523 GLY A O     1 
ATOM   4087 N  N     . LYS A 1 524 ? 1.478   3.614   35.532  1.00 124.85 ? 524 LYS A N     1 
ATOM   4088 C  CA    . LYS A 1 524 ? 0.101   3.143   35.485  1.00 122.14 ? 524 LYS A CA    1 
ATOM   4089 C  C     . LYS A 1 524 ? -0.704  4.007   34.524  1.00 117.54 ? 524 LYS A C     1 
ATOM   4090 O  O     . LYS A 1 524 ? -0.672  5.239   34.612  1.00 115.49 ? 524 LYS A O     1 
ATOM   4091 C  CB    . LYS A 1 524 ? -0.526  3.175   36.881  1.00 127.11 ? 524 LYS A CB    1 
ATOM   4092 C  CG    . LYS A 1 524 ? -1.980  2.727   36.936  1.00 131.40 ? 524 LYS A CG    1 
ATOM   4093 C  CD    . LYS A 1 524 ? -2.532  2.846   38.350  1.00 131.13 ? 524 LYS A CD    1 
ATOM   4094 C  CE    . LYS A 1 524 ? -3.992  2.427   38.420  1.00 125.05 ? 524 LYS A CE    1 
ATOM   4095 N  NZ    . LYS A 1 524 ? -4.564  2.626   39.782  1.00 116.02 ? 524 LYS A NZ    1 
ATOM   4096 N  N     . PHE A 1 525 ? -1.422  3.358   33.609  1.00 101.75 ? 525 PHE A N     1 
ATOM   4097 C  CA    . PHE A 1 525 ? -2.271  4.082   32.672  1.00 90.24  ? 525 PHE A CA    1 
ATOM   4098 C  C     . PHE A 1 525 ? -3.295  4.925   33.422  1.00 86.62  ? 525 PHE A C     1 
ATOM   4099 O  O     . PHE A 1 525 ? -3.950  4.449   34.354  1.00 96.17  ? 525 PHE A O     1 
ATOM   4100 C  CB    . PHE A 1 525 ? -2.973  3.102   31.731  1.00 77.17  ? 525 PHE A CB    1 
ATOM   4101 C  CG    . PHE A 1 525 ? -2.130  2.670   30.562  1.00 80.46  ? 525 PHE A CG    1 
ATOM   4102 C  CD1   . PHE A 1 525 ? -1.206  3.535   29.997  1.00 81.87  ? 525 PHE A CD1   1 
ATOM   4103 C  CD2   . PHE A 1 525 ? -2.264  1.401   30.026  1.00 75.44  ? 525 PHE A CD2   1 
ATOM   4104 C  CE1   . PHE A 1 525 ? -0.433  3.141   28.920  1.00 74.55  ? 525 PHE A CE1   1 
ATOM   4105 C  CE2   . PHE A 1 525 ? -1.494  1.001   28.949  1.00 72.41  ? 525 PHE A CE2   1 
ATOM   4106 C  CZ    . PHE A 1 525 ? -0.578  1.872   28.396  1.00 74.82  ? 525 PHE A CZ    1 
ATOM   4107 N  N     . LEU A 1 526 ? -3.428  6.184   33.014  1.00 83.89  ? 526 LEU A N     1 
ATOM   4108 C  CA    . LEU A 1 526 ? -4.345  7.121   33.649  1.00 83.08  ? 526 LEU A CA    1 
ATOM   4109 C  C     . LEU A 1 526 ? -5.762  7.043   33.094  1.00 79.08  ? 526 LEU A C     1 
ATOM   4110 O  O     . LEU A 1 526 ? -6.637  7.770   33.574  1.00 86.78  ? 526 LEU A O     1 
ATOM   4111 C  CB    . LEU A 1 526 ? -3.820  8.554   33.498  1.00 82.32  ? 526 LEU A CB    1 
ATOM   4112 C  CG    . LEU A 1 526 ? -2.496  8.901   34.183  1.00 92.39  ? 526 LEU A CG    1 
ATOM   4113 C  CD1   . LEU A 1 526 ? -1.971  10.233  33.678  1.00 93.78  ? 526 LEU A CD1   1 
ATOM   4114 C  CD2   . LEU A 1 526 ? -2.668  8.937   35.691  1.00 102.29 ? 526 LEU A CD2   1 
ATOM   4115 N  N     . TRP A 1 527 ? -6.015  6.182   32.105  1.00 76.46  ? 527 TRP A N     1 
ATOM   4116 C  CA    . TRP A 1 527 ? -7.314  6.110   31.445  1.00 71.58  ? 527 TRP A CA    1 
ATOM   4117 C  C     . TRP A 1 527 ? -7.620  4.656   31.097  1.00 75.16  ? 527 TRP A C     1 
ATOM   4118 O  O     . TRP A 1 527 ? -6.795  3.989   30.444  1.00 69.19  ? 527 TRP A O     1 
ATOM   4119 C  CB    . TRP A 1 527 ? -7.327  6.987   30.187  1.00 66.75  ? 527 TRP A CB    1 
ATOM   4120 C  CG    . TRP A 1 527 ? -8.636  7.022   29.445  1.00 65.64  ? 527 TRP A CG    1 
ATOM   4121 C  CD1   . TRP A 1 527 ? -8.895  6.480   28.221  1.00 64.08  ? 527 TRP A CD1   1 
ATOM   4122 C  CD2   . TRP A 1 527 ? -9.857  7.645   29.874  1.00 66.32  ? 527 TRP A CD2   1 
ATOM   4123 N  NE1   . TRP A 1 527 ? -10.200 6.722   27.861  1.00 63.62  ? 527 TRP A NE1   1 
ATOM   4124 C  CE2   . TRP A 1 527 ? -10.811 7.434   28.858  1.00 65.00  ? 527 TRP A CE2   1 
ATOM   4125 C  CE3   . TRP A 1 527 ? -10.235 8.356   31.017  1.00 68.11  ? 527 TRP A CE3   1 
ATOM   4126 C  CZ2   . TRP A 1 527 ? -12.120 7.908   28.952  1.00 65.38  ? 527 TRP A CZ2   1 
ATOM   4127 C  CZ3   . TRP A 1 527 ? -11.535 8.827   31.107  1.00 71.15  ? 527 TRP A CZ3   1 
ATOM   4128 C  CH2   . TRP A 1 527 ? -12.461 8.600   30.080  1.00 67.11  ? 527 TRP A CH2   1 
ATOM   4129 N  N     . PRO A 1 528 ? -8.775  4.130   31.517  1.00 74.84  ? 528 PRO A N     1 
ATOM   4130 C  CA    . PRO A 1 528 ? -9.103  2.737   31.171  1.00 71.90  ? 528 PRO A CA    1 
ATOM   4131 C  C     . PRO A 1 528 ? -9.146  2.490   29.673  1.00 72.06  ? 528 PRO A C     1 
ATOM   4132 O  O     . PRO A 1 528 ? -8.641  1.463   29.202  1.00 75.51  ? 528 PRO A O     1 
ATOM   4133 C  CB    . PRO A 1 528 ? -10.476 2.530   31.828  1.00 73.67  ? 528 PRO A CB    1 
ATOM   4134 C  CG    . PRO A 1 528 ? -11.025 3.901   32.018  1.00 73.04  ? 528 PRO A CG    1 
ATOM   4135 C  CD    . PRO A 1 528 ? -9.842  4.770   32.302  1.00 72.59  ? 528 PRO A CD    1 
ATOM   4136 N  N     . GLY A 1 529 ? -9.734  3.404   28.907  1.00 71.48  ? 529 GLY A N     1 
ATOM   4137 C  CA    . GLY A 1 529 ? -9.729  3.265   27.465  1.00 69.03  ? 529 GLY A CA    1 
ATOM   4138 C  C     . GLY A 1 529 ? -10.718 2.224   26.964  1.00 65.82  ? 529 GLY A C     1 
ATOM   4139 O  O     . GLY A 1 529 ? -11.724 1.918   27.606  1.00 67.42  ? 529 GLY A O     1 
ATOM   4140 N  N     . PHE A 1 530 ? -10.413 1.681   25.785  1.00 65.08  ? 530 PHE A N     1 
ATOM   4141 C  CA    . PHE A 1 530 ? -11.282 0.730   25.104  1.00 64.93  ? 530 PHE A CA    1 
ATOM   4142 C  C     . PHE A 1 530 ? -12.721 1.230   25.091  1.00 68.57  ? 530 PHE A C     1 
ATOM   4143 O  O     . PHE A 1 530 ? -13.001 2.314   24.564  1.00 63.44  ? 530 PHE A O     1 
ATOM   4144 C  CB    . PHE A 1 530 ? -11.176 -0.647  25.761  1.00 67.24  ? 530 PHE A CB    1 
ATOM   4145 C  CG    . PHE A 1 530 ? -9.795  -1.237  25.699  1.00 68.34  ? 530 PHE A CG    1 
ATOM   4146 C  CD1   . PHE A 1 530 ? -9.315  -1.792  24.521  1.00 66.96  ? 530 PHE A CD1   1 
ATOM   4147 C  CD2   . PHE A 1 530 ? -8.972  -1.229  26.814  1.00 68.74  ? 530 PHE A CD2   1 
ATOM   4148 C  CE1   . PHE A 1 530 ? -8.043  -2.332  24.459  1.00 66.73  ? 530 PHE A CE1   1 
ATOM   4149 C  CE2   . PHE A 1 530 ? -7.698  -1.768  26.758  1.00 69.07  ? 530 PHE A CE2   1 
ATOM   4150 C  CZ    . PHE A 1 530 ? -7.233  -2.319  25.580  1.00 68.04  ? 530 PHE A CZ    1 
ATOM   4151 N  N     . GLY A 1 531 ? -13.641 0.452   25.665  1.00 66.99  ? 531 GLY A N     1 
ATOM   4152 C  CA    . GLY A 1 531 ? -15.033 0.858   25.698  1.00 67.38  ? 531 GLY A CA    1 
ATOM   4153 C  C     . GLY A 1 531 ? -15.262 2.198   26.362  1.00 69.89  ? 531 GLY A C     1 
ATOM   4154 O  O     . GLY A 1 531 ? -16.257 2.870   26.062  1.00 66.97  ? 531 GLY A O     1 
ATOM   4155 N  N     . GLU A 1 532 ? -14.366 2.604   27.265  1.00 67.52  ? 532 GLU A N     1 
ATOM   4156 C  CA    . GLU A 1 532 ? -14.523 3.890   27.930  1.00 67.52  ? 532 GLU A CA    1 
ATOM   4157 C  C     . GLU A 1 532 ? -14.189 5.057   27.013  1.00 65.09  ? 532 GLU A C     1 
ATOM   4158 O  O     . GLU A 1 532 ? -14.635 6.182   27.269  1.00 66.35  ? 532 GLU A O     1 
ATOM   4159 C  CB    . GLU A 1 532 ? -13.654 3.947   29.185  1.00 69.01  ? 532 GLU A CB    1 
ATOM   4160 C  CG    . GLU A 1 532 ? -13.955 2.858   30.204  1.00 71.80  ? 532 GLU A CG    1 
ATOM   4161 C  CD    . GLU A 1 532 ? -15.399 2.865   30.683  1.00 73.44  ? 532 GLU A CD    1 
ATOM   4162 O  OE1   . GLU A 1 532 ? -16.239 3.562   30.076  1.00 75.78  ? 532 GLU A OE1   1 
ATOM   4163 O  OE2   . GLU A 1 532 ? -15.697 2.167   31.672  1.00 76.05  ? 532 GLU A OE2   1 
ATOM   4164 N  N     . ASN A 1 533 ? -13.418 4.820   25.951  1.00 63.37  ? 533 ASN A N     1 
ATOM   4165 C  CA    . ASN A 1 533 ? -13.153 5.875   24.981  1.00 61.24  ? 533 ASN A CA    1 
ATOM   4166 C  C     . ASN A 1 533 ? -14.431 6.441   24.378  1.00 60.82  ? 533 ASN A C     1 
ATOM   4167 O  O     . ASN A 1 533 ? -14.384 7.504   23.750  1.00 65.93  ? 533 ASN A O     1 
ATOM   4168 C  CB    . ASN A 1 533 ? -12.232 5.349   23.877  1.00 59.83  ? 533 ASN A CB    1 
ATOM   4169 C  CG    . ASN A 1 533 ? -10.856 4.982   24.398  1.00 60.89  ? 533 ASN A CG    1 
ATOM   4170 O  OD1   . ASN A 1 533 ? -10.393 5.533   25.398  1.00 60.90  ? 533 ASN A OD1   1 
ATOM   4171 N  ND2   . ASN A 1 533 ? -10.192 4.048   23.722  1.00 59.84  ? 533 ASN A ND2   1 
ATOM   4172 N  N     . SER A 1 534 ? -15.566 5.760   24.550  1.00 63.16  ? 534 SER A N     1 
ATOM   4173 C  CA    . SER A 1 534 ? -16.841 6.335   24.148  1.00 62.58  ? 534 SER A CA    1 
ATOM   4174 C  C     . SER A 1 534 ? -17.154 7.613   24.915  1.00 62.57  ? 534 SER A C     1 
ATOM   4175 O  O     . SER A 1 534 ? -17.919 8.448   24.422  1.00 63.60  ? 534 SER A O     1 
ATOM   4176 C  CB    . SER A 1 534 ? -17.958 5.313   24.347  1.00 63.89  ? 534 SER A CB    1 
ATOM   4177 O  OG    . SER A 1 534 ? -18.013 4.885   25.696  1.00 70.81  ? 534 SER A OG    1 
ATOM   4178 N  N     . ARG A 1 535 ? -16.584 7.784   26.110  1.00 63.63  ? 535 ARG A N     1 
ATOM   4179 C  CA    . ARG A 1 535 ? -16.767 9.038   26.834  1.00 67.50  ? 535 ARG A CA    1 
ATOM   4180 C  C     . ARG A 1 535 ? -16.050 10.181  26.127  1.00 64.64  ? 535 ARG A C     1 
ATOM   4181 O  O     . ARG A 1 535 ? -16.549 11.312  26.093  1.00 62.25  ? 535 ARG A O     1 
ATOM   4182 C  CB    . ARG A 1 535 ? -16.269 8.897   28.273  1.00 66.05  ? 535 ARG A CB    1 
ATOM   4183 C  CG    . ARG A 1 535 ? -16.901 7.750   29.043  1.00 68.24  ? 535 ARG A CG    1 
ATOM   4184 C  CD    . ARG A 1 535 ? -16.181 7.511   30.362  1.00 75.62  ? 535 ARG A CD    1 
ATOM   4185 N  NE    . ARG A 1 535 ? -16.614 6.281   31.015  1.00 72.26  ? 535 ARG A NE    1 
ATOM   4186 C  CZ    . ARG A 1 535 ? -17.523 6.220   31.978  1.00 74.71  ? 535 ARG A CZ    1 
ATOM   4187 N  NH1   . ARG A 1 535 ? -18.125 7.308   32.431  1.00 78.06  ? 535 ARG A NH1   1 
ATOM   4188 N  NH2   . ARG A 1 535 ? -17.834 5.039   32.503  1.00 81.09  ? 535 ARG A NH2   1 
ATOM   4189 N  N     . VAL A 1 536 ? -14.878 9.903   25.553  1.00 62.61  ? 536 VAL A N     1 
ATOM   4190 C  CA    . VAL A 1 536 ? -14.174 10.925  24.789  1.00 59.89  ? 536 VAL A CA    1 
ATOM   4191 C  C     . VAL A 1 536 ? -14.918 11.227  23.494  1.00 58.00  ? 536 VAL A C     1 
ATOM   4192 O  O     . VAL A 1 536 ? -15.065 12.391  23.105  1.00 60.25  ? 536 VAL A O     1 
ATOM   4193 C  CB    . VAL A 1 536 ? -12.722 10.488  24.525  1.00 60.74  ? 536 VAL A CB    1 
ATOM   4194 C  CG1   . VAL A 1 536 ? -12.030 11.482  23.603  1.00 60.50  ? 536 VAL A CG1   1 
ATOM   4195 C  CG2   . VAL A 1 536 ? -11.964 10.354  25.837  1.00 59.66  ? 536 VAL A CG2   1 
ATOM   4196 N  N     . LEU A 1 537 ? -15.404 10.188  22.810  1.00 60.05  ? 537 LEU A N     1 
ATOM   4197 C  CA    . LEU A 1 537 ? -16.167 10.411  21.586  1.00 57.07  ? 537 LEU A CA    1 
ATOM   4198 C  C     . LEU A 1 537 ? -17.424 11.227  21.853  1.00 58.00  ? 537 LEU A C     1 
ATOM   4199 O  O     . LEU A 1 537 ? -17.837 12.025  21.004  1.00 57.36  ? 537 LEU A O     1 
ATOM   4200 C  CB    . LEU A 1 537 ? -16.535 9.078   20.932  1.00 61.95  ? 537 LEU A CB    1 
ATOM   4201 C  CG    . LEU A 1 537 ? -15.427 8.111   20.502  1.00 61.07  ? 537 LEU A CG    1 
ATOM   4202 C  CD1   . LEU A 1 537 ? -16.012 7.010   19.630  1.00 63.94  ? 537 LEU A CD1   1 
ATOM   4203 C  CD2   . LEU A 1 537 ? -14.309 8.827   19.775  1.00 54.93  ? 537 LEU A CD2   1 
ATOM   4204 N  N     . GLU A 1 538 ? -18.052 11.042  23.018  1.00 59.72  ? 538 GLU A N     1 
ATOM   4205 C  CA    . GLU A 1 538 ? -19.235 11.832  23.345  1.00 60.86  ? 538 GLU A CA    1 
ATOM   4206 C  C     . GLU A 1 538 ? -18.925 13.323  23.293  1.00 60.31  ? 538 GLU A C     1 
ATOM   4207 O  O     . GLU A 1 538 ? -19.665 14.104  22.682  1.00 60.25  ? 538 GLU A O     1 
ATOM   4208 C  CB    . GLU A 1 538 ? -19.771 11.445  24.724  1.00 63.00  ? 538 GLU A CB    1 
ATOM   4209 C  CG    . GLU A 1 538 ? -20.947 12.298  25.180  1.00 64.47  ? 538 GLU A CG    1 
ATOM   4210 C  CD    . GLU A 1 538 ? -21.509 11.863  26.521  1.00 69.35  ? 538 GLU A CD    1 
ATOM   4211 O  OE1   . GLU A 1 538 ? -20.730 11.385  27.373  1.00 67.42  ? 538 GLU A OE1   1 
ATOM   4212 O  OE2   . GLU A 1 538 ? -22.735 11.994  26.721  1.00 77.14  ? 538 GLU A OE2   1 
ATOM   4213 N  N     . TRP A 1 539 ? -17.826 13.735  23.927  1.00 60.09  ? 539 TRP A N     1 
ATOM   4214 C  CA    . TRP A 1 539 ? -17.435 15.140  23.895  1.00 59.73  ? 539 TRP A CA    1 
ATOM   4215 C  C     . TRP A 1 539 ? -17.223 15.614  22.464  1.00 60.78  ? 539 TRP A C     1 
ATOM   4216 O  O     . TRP A 1 539 ? -17.695 16.691  22.079  1.00 58.14  ? 539 TRP A O     1 
ATOM   4217 C  CB    . TRP A 1 539 ? -16.171 15.350  24.730  1.00 59.84  ? 539 TRP A CB    1 
ATOM   4218 C  CG    . TRP A 1 539 ? -15.752 16.788  24.837  1.00 59.84  ? 539 TRP A CG    1 
ATOM   4219 C  CD1   . TRP A 1 539 ? -16.315 17.750  25.626  1.00 61.41  ? 539 TRP A CD1   1 
ATOM   4220 C  CD2   . TRP A 1 539 ? -14.674 17.421  24.139  1.00 58.45  ? 539 TRP A CD2   1 
ATOM   4221 N  NE1   . TRP A 1 539 ? -15.658 18.944  25.458  1.00 62.19  ? 539 TRP A NE1   1 
ATOM   4222 C  CE2   . TRP A 1 539 ? -14.645 18.769  24.550  1.00 60.15  ? 539 TRP A CE2   1 
ATOM   4223 C  CE3   . TRP A 1 539 ? -13.730 16.980  23.203  1.00 56.76  ? 539 TRP A CE3   1 
ATOM   4224 C  CZ2   . TRP A 1 539 ? -13.710 19.681  24.059  1.00 59.76  ? 539 TRP A CZ2   1 
ATOM   4225 C  CZ3   . TRP A 1 539 ? -12.803 17.885  22.716  1.00 57.00  ? 539 TRP A CZ3   1 
ATOM   4226 C  CH2   . TRP A 1 539 ? -12.800 19.222  23.145  1.00 59.76  ? 539 TRP A CH2   1 
ATOM   4227 N  N     . MET A 1 540 ? -16.509 14.819  21.660  1.00 57.64  ? 540 MET A N     1 
ATOM   4228 C  CA    . MET A 1 540 ? -16.289 15.183  20.264  1.00 55.33  ? 540 MET A CA    1 
ATOM   4229 C  C     . MET A 1 540 ? -17.610 15.377  19.532  1.00 55.75  ? 540 MET A C     1 
ATOM   4230 O  O     . MET A 1 540 ? -17.776 16.340  18.773  1.00 58.02  ? 540 MET A O     1 
ATOM   4231 C  CB    . MET A 1 540 ? -15.452 14.112  19.563  1.00 54.21  ? 540 MET A CB    1 
ATOM   4232 C  CG    . MET A 1 540 ? -14.047 13.922  20.109  1.00 53.80  ? 540 MET A CG    1 
ATOM   4233 S  SD    . MET A 1 540 ? -13.227 12.539  19.280  1.00 65.71  ? 540 MET A SD    1 
ATOM   4234 C  CE    . MET A 1 540 ? -11.620 12.568  20.067  1.00 61.81  ? 540 MET A CE    1 
ATOM   4235 N  N     . PHE A 1 541 ? -18.562 14.466  19.747  1.00 56.67  ? 541 PHE A N     1 
ATOM   4236 C  CA    . PHE A 1 541 ? -19.862 14.572  19.093  1.00 57.33  ? 541 PHE A CA    1 
ATOM   4237 C  C     . PHE A 1 541 ? -20.538 15.898  19.424  1.00 61.78  ? 541 PHE A C     1 
ATOM   4238 O  O     . PHE A 1 541 ? -21.124 16.543  18.545  1.00 62.75  ? 541 PHE A O     1 
ATOM   4239 C  CB    . PHE A 1 541 ? -20.737 13.390  19.514  1.00 59.79  ? 541 PHE A CB    1 
ATOM   4240 C  CG    . PHE A 1 541 ? -21.943 13.173  18.644  1.00 65.47  ? 541 PHE A CG    1 
ATOM   4241 C  CD1   . PHE A 1 541 ? -23.056 13.993  18.754  1.00 60.38  ? 541 PHE A CD1   1 
ATOM   4242 C  CD2   . PHE A 1 541 ? -21.977 12.122  17.740  1.00 58.83  ? 541 PHE A CD2   1 
ATOM   4243 C  CE1   . PHE A 1 541 ? -24.172 13.785  17.964  1.00 62.59  ? 541 PHE A CE1   1 
ATOM   4244 C  CE2   . PHE A 1 541 ? -23.090 11.907  16.947  1.00 60.25  ? 541 PHE A CE2   1 
ATOM   4245 C  CZ    . PHE A 1 541 ? -24.190 12.740  17.059  1.00 70.11  ? 541 PHE A CZ    1 
ATOM   4246 N  N     . GLY A 1 542 ? -20.465 16.326  20.686  1.00 59.22  ? 542 GLY A N     1 
ATOM   4247 C  CA    . GLY A 1 542 ? -21.088 17.583  21.067  1.00 60.36  ? 542 GLY A CA    1 
ATOM   4248 C  C     . GLY A 1 542 ? -20.377 18.785  20.477  1.00 66.51  ? 542 GLY A C     1 
ATOM   4249 O  O     . GLY A 1 542 ? -21.018 19.759  20.071  1.00 65.09  ? 542 GLY A O     1 
ATOM   4250 N  N     . ARG A 1 543 ? -19.044 18.735  20.421  1.00 62.57  ? 543 ARG A N     1 
ATOM   4251 C  CA    . ARG A 1 543 ? -18.292 19.820  19.802  1.00 59.39  ? 543 ARG A CA    1 
ATOM   4252 C  C     . ARG A 1 543 ? -18.638 19.965  18.326  1.00 58.65  ? 543 ARG A C     1 
ATOM   4253 O  O     . ARG A 1 543 ? -18.657 21.081  17.798  1.00 61.15  ? 543 ARG A O     1 
ATOM   4254 C  CB    . ARG A 1 543 ? -16.790 19.585  19.978  1.00 56.34  ? 543 ARG A CB    1 
ATOM   4255 C  CG    . ARG A 1 543 ? -16.297 19.759  21.406  1.00 59.92  ? 543 ARG A CG    1 
ATOM   4256 C  CD    . ARG A 1 543 ? -16.497 21.188  21.872  1.00 59.11  ? 543 ARG A CD    1 
ATOM   4257 N  NE    . ARG A 1 543 ? -15.719 22.122  21.068  1.00 57.67  ? 543 ARG A NE    1 
ATOM   4258 C  CZ    . ARG A 1 543 ? -16.078 23.373  20.820  1.00 63.75  ? 543 ARG A CZ    1 
ATOM   4259 N  NH1   . ARG A 1 543 ? -17.217 23.868  21.278  1.00 62.07  ? 543 ARG A NH1   1 
ATOM   4260 N  NH2   . ARG A 1 543 ? -15.280 24.145  20.087  1.00 68.16  ? 543 ARG A NH2   1 
ATOM   4261 N  N     . ILE A 1 544 ? -18.917 18.853  17.643  1.00 64.08  ? 544 ILE A N     1 
ATOM   4262 C  CA    . ILE A 1 544 ? -19.281 18.939  16.233  1.00 67.29  ? 544 ILE A CA    1 
ATOM   4263 C  C     . ILE A 1 544 ? -20.632 19.622  16.066  1.00 57.30  ? 544 ILE A C     1 
ATOM   4264 O  O     . ILE A 1 544 ? -20.870 20.309  15.065  1.00 57.51  ? 544 ILE A O     1 
ATOM   4265 C  CB    . ILE A 1 544 ? -19.269 17.540  15.589  1.00 60.50  ? 544 ILE A CB    1 
ATOM   4266 C  CG1   . ILE A 1 544 ? -17.831 17.052  15.396  1.00 54.82  ? 544 ILE A CG1   1 
ATOM   4267 C  CG2   . ILE A 1 544 ? -20.022 17.549  14.267  1.00 57.10  ? 544 ILE A CG2   1 
ATOM   4268 C  CD1   . ILE A 1 544 ? -17.738 15.664  14.787  1.00 53.55  ? 544 ILE A CD1   1 
ATOM   4269 N  N     . GLU A 1 545 ? -21.536 19.448  17.028  1.00 58.58  ? 545 GLU A N     1 
ATOM   4270 C  CA    . GLU A 1 545 ? -22.830 20.111  16.969  1.00 63.15  ? 545 GLU A CA    1 
ATOM   4271 C  C     . GLU A 1 545 ? -22.781 21.546  17.476  1.00 62.18  ? 545 GLU A C     1 
ATOM   4272 O  O     . GLU A 1 545 ? -23.779 22.263  17.348  1.00 62.50  ? 545 GLU A O     1 
ATOM   4273 C  CB    . GLU A 1 545 ? -23.867 19.317  17.768  1.00 66.24  ? 545 GLU A CB    1 
ATOM   4274 C  CG    . GLU A 1 545 ? -24.157 17.933  17.205  1.00 61.14  ? 545 GLU A CG    1 
ATOM   4275 C  CD    . GLU A 1 545 ? -25.363 17.285  17.856  1.00 70.86  ? 545 GLU A CD    1 
ATOM   4276 O  OE1   . GLU A 1 545 ? -25.490 17.370  19.096  1.00 75.65  ? 545 GLU A OE1   1 
ATOM   4277 O  OE2   . GLU A 1 545 ? -26.192 16.703  17.127  1.00 75.67  ? 545 GLU A OE2   1 
ATOM   4278 N  N     . GLY A 1 546 ? -21.654 21.978  18.034  1.00 63.17  ? 546 GLY A N     1 
ATOM   4279 C  CA    . GLY A 1 546 ? -21.521 23.329  18.535  1.00 65.15  ? 546 GLY A CA    1 
ATOM   4280 C  C     . GLY A 1 546 ? -22.042 23.488  19.947  1.00 70.68  ? 546 GLY A C     1 
ATOM   4281 O  O     . GLY A 1 546 ? -23.037 24.181  20.174  1.00 64.79  ? 546 GLY A O     1 
ATOM   4282 N  N     . GLU A 1 547 ? -21.386 22.838  20.904  1.00 72.00  ? 547 GLU A N     1 
ATOM   4283 C  CA    . GLU A 1 547 ? -21.731 22.950  22.312  1.00 72.79  ? 547 GLU A CA    1 
ATOM   4284 C  C     . GLU A 1 547 ? -20.603 23.647  23.059  1.00 74.15  ? 547 GLU A C     1 
ATOM   4285 O  O     . GLU A 1 547 ? -19.424 23.360  22.832  1.00 67.60  ? 547 GLU A O     1 
ATOM   4286 C  CB    . GLU A 1 547 ? -22.002 21.574  22.929  1.00 70.35  ? 547 GLU A CB    1 
ATOM   4287 C  CG    . GLU A 1 547 ? -23.315 20.953  22.484  1.00 75.72  ? 547 GLU A CG    1 
ATOM   4288 C  CD    . GLU A 1 547 ? -23.597 19.629  23.164  1.00 98.12  ? 547 GLU A CD    1 
ATOM   4289 O  OE1   . GLU A 1 547 ? -22.878 19.287  24.126  1.00 106.58 ? 547 GLU A OE1   1 
ATOM   4290 O  OE2   . GLU A 1 547 ? -24.537 18.926  22.734  1.00 102.10 ? 547 GLU A OE2   1 
ATOM   4291 N  N     . ASP A 1 548 ? -20.973 24.569  23.949  1.00 90.31  ? 548 ASP A N     1 
ATOM   4292 C  CA    . ASP A 1 548 ? -19.998 25.356  24.704  1.00 91.55  ? 548 ASP A CA    1 
ATOM   4293 C  C     . ASP A 1 548 ? -19.417 24.490  25.822  1.00 90.03  ? 548 ASP A C     1 
ATOM   4294 O  O     . ASP A 1 548 ? -19.612 24.724  27.017  1.00 89.71  ? 548 ASP A O     1 
ATOM   4295 C  CB    . ASP A 1 548 ? -20.639 26.625  25.248  1.00 91.10  ? 548 ASP A CB    1 
ATOM   4296 C  CG    . ASP A 1 548 ? -19.616 27.679  25.624  1.00 97.71  ? 548 ASP A CG    1 
ATOM   4297 O  OD1   . ASP A 1 548 ? -18.434 27.517  25.256  1.00 100.36 ? 548 ASP A OD1   1 
ATOM   4298 O  OD2   . ASP A 1 548 ? -19.993 28.669  26.287  1.00 101.58 ? 548 ASP A OD2   1 
ATOM   4299 N  N     . SER A 1 549 ? -18.681 23.460  25.404  1.00 73.20  ? 549 SER A N     1 
ATOM   4300 C  CA    . SER A 1 549 ? -18.088 22.501  26.326  1.00 69.30  ? 549 SER A CA    1 
ATOM   4301 C  C     . SER A 1 549 ? -16.567 22.533  26.306  1.00 64.45  ? 549 SER A C     1 
ATOM   4302 O  O     . SER A 1 549 ? -15.931 21.672  26.925  1.00 64.42  ? 549 SER A O     1 
ATOM   4303 C  CB    . SER A 1 549 ? -18.582 21.088  26.005  1.00 68.19  ? 549 SER A CB    1 
ATOM   4304 O  OG    . SER A 1 549 ? -18.252 20.726  24.677  1.00 71.05  ? 549 SER A OG    1 
ATOM   4305 N  N     . ALA A 1 550 ? -15.967 23.501  25.622  1.00 65.37  ? 550 ALA A N     1 
ATOM   4306 C  CA    . ALA A 1 550 ? -14.529 23.536  25.417  1.00 69.00  ? 550 ALA A CA    1 
ATOM   4307 C  C     . ALA A 1 550 ? -13.900 24.693  26.181  1.00 64.95  ? 550 ALA A C     1 
ATOM   4308 O  O     . ALA A 1 550 ? -14.493 25.765  26.324  1.00 65.45  ? 550 ALA A O     1 
ATOM   4309 C  CB    . ALA A 1 550 ? -14.189 23.656  23.928  1.00 60.63  ? 550 ALA A CB    1 
ATOM   4310 N  N     . LYS A 1 551 ? -12.685 24.456  26.663  1.00 68.56  ? 551 LYS A N     1 
ATOM   4311 C  CA    . LYS A 1 551 ? -11.865 25.464  27.319  1.00 65.37  ? 551 LYS A CA    1 
ATOM   4312 C  C     . LYS A 1 551 ? -10.642 25.740  26.453  1.00 67.21  ? 551 LYS A C     1 
ATOM   4313 O  O     . LYS A 1 551 ? -10.004 24.804  25.960  1.00 62.25  ? 551 LYS A O     1 
ATOM   4314 C  CB    . LYS A 1 551 ? -11.443 24.991  28.712  1.00 67.02  ? 551 LYS A CB    1 
ATOM   4315 C  CG    . LYS A 1 551 ? -10.591 25.980  29.476  1.00 77.55  ? 551 LYS A CG    1 
ATOM   4316 C  CD    . LYS A 1 551 ? -10.166 25.411  30.821  1.00 87.47  ? 551 LYS A CD    1 
ATOM   4317 C  CE    . LYS A 1 551 ? -9.265  24.199  30.648  1.00 76.82  ? 551 LYS A CE    1 
ATOM   4318 N  NZ    . LYS A 1 551 ? -8.837  23.630  31.958  1.00 94.26  ? 551 LYS A NZ    1 
ATOM   4319 N  N     . LEU A 1 552 ? -10.323 27.017  26.261  1.00 64.61  ? 552 LEU A N     1 
ATOM   4320 C  CA    . LEU A 1 552 ? -9.184  27.388  25.431  1.00 63.50  ? 552 LEU A CA    1 
ATOM   4321 C  C     . LEU A 1 552 ? -7.879  27.200  26.193  1.00 64.87  ? 552 LEU A C     1 
ATOM   4322 O  O     . LEU A 1 552 ? -7.781  27.522  27.380  1.00 72.07  ? 552 LEU A O     1 
ATOM   4323 C  CB    . LEU A 1 552 ? -9.308  28.837  24.961  1.00 64.35  ? 552 LEU A CB    1 
ATOM   4324 C  CG    . LEU A 1 552 ? -8.193  29.303  24.024  1.00 66.50  ? 552 LEU A CG    1 
ATOM   4325 C  CD1   . LEU A 1 552 ? -8.052  28.342  22.851  1.00 66.13  ? 552 LEU A CD1   1 
ATOM   4326 C  CD2   . LEU A 1 552 ? -8.450  30.719  23.534  1.00 67.91  ? 552 LEU A CD2   1 
ATOM   4327 N  N     . THR A 1 553 ? -6.870  26.682  25.498  1.00 65.90  ? 553 THR A N     1 
ATOM   4328 C  CA    . THR A 1 553 ? -5.583  26.400  26.120  1.00 63.58  ? 553 THR A CA    1 
ATOM   4329 C  C     . THR A 1 553 ? -4.463  26.673  25.121  1.00 61.92  ? 553 THR A C     1 
ATOM   4330 O  O     . THR A 1 553 ? -4.735  26.888  23.933  1.00 62.37  ? 553 THR A O     1 
ATOM   4331 C  CB    . THR A 1 553 ? -5.537  24.952  26.624  1.00 63.30  ? 553 THR A CB    1 
ATOM   4332 O  OG1   . THR A 1 553 ? -4.925  24.913  27.918  1.00 74.93  ? 553 THR A OG1   1 
ATOM   4333 C  CG2   . THR A 1 553 ? -4.746  24.064  25.671  1.00 60.59  ? 553 THR A CG2   1 
ATOM   4334 N  N     . PRO A 1 554 ? -3.200  26.685  25.557  1.00 62.62  ? 554 PRO A N     1 
ATOM   4335 C  CA    . PRO A 1 554 ? -2.106  26.995  24.621  1.00 61.80  ? 554 PRO A CA    1 
ATOM   4336 C  C     . PRO A 1 554 ? -1.920  25.963  23.517  1.00 65.46  ? 554 PRO A C     1 
ATOM   4337 O  O     . PRO A 1 554 ? -1.294  26.282  22.499  1.00 70.08  ? 554 PRO A O     1 
ATOM   4338 C  CB    . PRO A 1 554 ? -0.871  27.059  25.532  1.00 63.62  ? 554 PRO A CB    1 
ATOM   4339 C  CG    . PRO A 1 554 ? -1.415  27.310  26.900  1.00 65.43  ? 554 PRO A CG    1 
ATOM   4340 C  CD    . PRO A 1 554 ? -2.727  26.592  26.947  1.00 64.60  ? 554 PRO A CD    1 
ATOM   4341 N  N     . ILE A 1 555 ? -2.436  24.746  23.673  1.00 58.70  ? 555 ILE A N     1 
ATOM   4342 C  CA    . ILE A 1 555 ? -2.287  23.707  22.657  1.00 60.37  ? 555 ILE A CA    1 
ATOM   4343 C  C     . ILE A 1 555 ? -3.571  23.448  21.886  1.00 55.66  ? 555 ILE A C     1 
ATOM   4344 O  O     . ILE A 1 555 ? -3.533  22.726  20.876  1.00 54.22  ? 555 ILE A O     1 
ATOM   4345 C  CB    . ILE A 1 555 ? -1.775  22.388  23.271  1.00 56.78  ? 555 ILE A CB    1 
ATOM   4346 C  CG1   . ILE A 1 555 ? -2.794  21.841  24.273  1.00 62.86  ? 555 ILE A CG1   1 
ATOM   4347 C  CG2   . ILE A 1 555 ? -0.419  22.602  23.932  1.00 58.01  ? 555 ILE A CG2   1 
ATOM   4348 C  CD1   . ILE A 1 555 ? -2.548  20.401  24.685  1.00 57.41  ? 555 ILE A CD1   1 
ATOM   4349 N  N     . GLY A 1 556 ? -4.690  24.005  22.312  1.00 58.01  ? 556 GLY A N     1 
ATOM   4350 C  CA    . GLY A 1 556 ? -5.958  23.786  21.650  1.00 59.31  ? 556 GLY A CA    1 
ATOM   4351 C  C     . GLY A 1 556 ? -7.089  23.829  22.659  1.00 61.41  ? 556 GLY A C     1 
ATOM   4352 O  O     . GLY A 1 556 ? -6.896  24.156  23.827  1.00 60.44  ? 556 GLY A O     1 
ATOM   4353 N  N     . TYR A 1 557 ? -8.281  23.496  22.180  1.00 59.45  ? 557 TYR A N     1 
ATOM   4354 C  CA    . TYR A 1 557 ? -9.442  23.415  23.051  1.00 59.81  ? 557 TYR A CA    1 
ATOM   4355 C  C     . TYR A 1 557 ? -9.451  22.086  23.797  1.00 58.54  ? 557 TYR A C     1 
ATOM   4356 O  O     . TYR A 1 557 ? -9.181  21.030  23.218  1.00 58.95  ? 557 TYR A O     1 
ATOM   4357 C  CB    . TYR A 1 557 ? -10.735 23.566  22.249  1.00 57.14  ? 557 TYR A CB    1 
ATOM   4358 C  CG    . TYR A 1 557 ? -10.940 24.931  21.640  1.00 57.57  ? 557 TYR A CG    1 
ATOM   4359 C  CD1   . TYR A 1 557 ? -11.205 26.036  22.439  1.00 63.47  ? 557 TYR A CD1   1 
ATOM   4360 C  CD2   . TYR A 1 557 ? -10.887 25.112  20.266  1.00 59.89  ? 557 TYR A CD2   1 
ATOM   4361 C  CE1   . TYR A 1 557 ? -11.399 27.286  21.885  1.00 59.98  ? 557 TYR A CE1   1 
ATOM   4362 C  CE2   . TYR A 1 557 ? -11.080 26.358  19.702  1.00 60.73  ? 557 TYR A CE2   1 
ATOM   4363 C  CZ    . TYR A 1 557 ? -11.337 27.441  20.518  1.00 63.00  ? 557 TYR A CZ    1 
ATOM   4364 O  OH    . TYR A 1 557 ? -11.531 28.683  19.965  1.00 65.93  ? 557 TYR A OH    1 
ATOM   4365 N  N     . VAL A 1 558 ? -9.757  22.148  25.088  1.00 59.28  ? 558 VAL A N     1 
ATOM   4366 C  CA    . VAL A 1 558 ? -9.908  20.949  25.908  1.00 59.81  ? 558 VAL A CA    1 
ATOM   4367 C  C     . VAL A 1 558 ? -11.252 21.028  26.616  1.00 65.95  ? 558 VAL A C     1 
ATOM   4368 O  O     . VAL A 1 558 ? -11.843 22.112  26.741  1.00 62.25  ? 558 VAL A O     1 
ATOM   4369 C  CB    . VAL A 1 558 ? -8.751  20.799  26.923  1.00 60.90  ? 558 VAL A CB    1 
ATOM   4370 C  CG1   . VAL A 1 558 ? -7.415  20.776  26.203  1.00 59.61  ? 558 VAL A CG1   1 
ATOM   4371 C  CG2   . VAL A 1 558 ? -8.795  21.925  27.943  1.00 63.71  ? 558 VAL A CG2   1 
ATOM   4372 N  N     . PRO A 1 559 ? -11.765 19.894  27.093  1.00 65.25  ? 559 PRO A N     1 
ATOM   4373 C  CA    . PRO A 1 559 ? -13.099 19.895  27.704  1.00 63.18  ? 559 PRO A CA    1 
ATOM   4374 C  C     . PRO A 1 559 ? -13.148 20.792  28.932  1.00 65.53  ? 559 PRO A C     1 
ATOM   4375 O  O     . PRO A 1 559 ? -12.191 20.876  29.704  1.00 66.47  ? 559 PRO A O     1 
ATOM   4376 C  CB    . PRO A 1 559 ? -13.325 18.423  28.073  1.00 63.37  ? 559 PRO A CB    1 
ATOM   4377 C  CG    . PRO A 1 559 ? -12.350 17.651  27.231  1.00 61.45  ? 559 PRO A CG    1 
ATOM   4378 C  CD    . PRO A 1 559 ? -11.163 18.550  27.073  1.00 64.99  ? 559 PRO A CD    1 
ATOM   4379 N  N     . LYS A 1 560 ? -14.280 21.470  29.103  1.00 66.71  ? 560 LYS A N     1 
ATOM   4380 C  CA    . LYS A 1 560 ? -14.497 22.271  30.295  1.00 77.52  ? 560 LYS A CA    1 
ATOM   4381 C  C     . LYS A 1 560 ? -14.546 21.383  31.537  1.00 89.81  ? 560 LYS A C     1 
ATOM   4382 O  O     . LYS A 1 560 ? -14.583 20.152  31.463  1.00 74.19  ? 560 LYS A O     1 
ATOM   4383 C  CB    . LYS A 1 560 ? -15.802 23.058  30.192  1.00 76.45  ? 560 LYS A CB    1 
ATOM   4384 C  CG    . LYS A 1 560 ? -15.791 24.212  29.215  1.00 79.31  ? 560 LYS A CG    1 
ATOM   4385 C  CD    . LYS A 1 560 ? -17.091 24.993  29.321  1.00 71.06  ? 560 LYS A CD    1 
ATOM   4386 C  CE    . LYS A 1 560 ? -17.133 26.147  28.341  1.00 76.89  ? 560 LYS A CE    1 
ATOM   4387 N  NZ    . LYS A 1 560 ? -18.400 26.918  28.458  1.00 72.26  ? 560 LYS A NZ    1 
ATOM   4388 N  N     . GLU A 1 561 ? -14.556 22.037  32.696  1.00 118.88 ? 561 GLU A N     1 
ATOM   4389 C  CA    . GLU A 1 561 ? -14.806 21.330  33.943  1.00 120.77 ? 561 GLU A CA    1 
ATOM   4390 C  C     . GLU A 1 561 ? -16.150 20.619  33.870  1.00 120.17 ? 561 GLU A C     1 
ATOM   4391 O  O     . GLU A 1 561 ? -17.155 21.207  33.460  1.00 119.68 ? 561 GLU A O     1 
ATOM   4392 C  CB    . GLU A 1 561 ? -14.787 22.306  35.118  1.00 126.14 ? 561 GLU A CB    1 
ATOM   4393 C  CG    . GLU A 1 561 ? -15.182 21.678  36.446  1.00 134.98 ? 561 GLU A CG    1 
ATOM   4394 C  CD    . GLU A 1 561 ? -15.514 22.710  37.508  1.00 140.53 ? 561 GLU A CD    1 
ATOM   4395 O  OE1   . GLU A 1 561 ? -15.591 23.910  37.172  1.00 141.59 ? 561 GLU A OE1   1 
ATOM   4396 O  OE2   . GLU A 1 561 ? -15.701 22.319  38.679  1.00 145.96 ? 561 GLU A OE2   1 
ATOM   4397 N  N     . ASP A 1 562 ? -16.165 19.348  34.261  1.00 89.89  ? 562 ASP A N     1 
ATOM   4398 C  CA    . ASP A 1 562 ? -17.382 18.542  34.261  1.00 91.43  ? 562 ASP A CA    1 
ATOM   4399 C  C     . ASP A 1 562 ? -17.990 18.412  32.870  1.00 88.12  ? 562 ASP A C     1 
ATOM   4400 O  O     . ASP A 1 562 ? -19.182 18.119  32.735  1.00 81.04  ? 562 ASP A O     1 
ATOM   4401 C  CB    . ASP A 1 562 ? -18.420 19.111  35.235  1.00 104.30 ? 562 ASP A CB    1 
ATOM   4402 C  CG    . ASP A 1 562 ? -18.058 18.859  36.685  1.00 110.73 ? 562 ASP A CG    1 
ATOM   4403 O  OD1   . ASP A 1 562 ? -17.767 17.694  37.034  1.00 103.76 ? 562 ASP A OD1   1 
ATOM   4404 O  OD2   . ASP A 1 562 ? -18.060 19.827  37.475  1.00 116.61 ? 562 ASP A OD2   1 
ATOM   4405 N  N     . ALA A 1 563 ? -17.191 18.630  31.825  1.00 87.82  ? 563 ALA A N     1 
ATOM   4406 C  CA    . ALA A 1 563 ? -17.684 18.453  30.465  1.00 75.16  ? 563 ALA A CA    1 
ATOM   4407 C  C     . ALA A 1 563 ? -17.654 16.991  30.034  1.00 72.83  ? 563 ALA A C     1 
ATOM   4408 O  O     . ALA A 1 563 ? -18.511 16.562  29.255  1.00 73.75  ? 563 ALA A O     1 
ATOM   4409 C  CB    . ALA A 1 563 ? -16.867 19.307  29.495  1.00 70.89  ? 563 ALA A CB    1 
ATOM   4410 N  N     . LEU A 1 564 ? -16.690 16.216  30.526  1.00 68.96  ? 564 LEU A N     1 
ATOM   4411 C  CA    . LEU A 1 564 ? -16.590 14.802  30.194  1.00 75.31  ? 564 LEU A CA    1 
ATOM   4412 C  C     . LEU A 1 564 ? -17.448 13.973  31.141  1.00 75.89  ? 564 LEU A C     1 
ATOM   4413 O  O     . LEU A 1 564 ? -17.303 14.064  32.364  1.00 72.99  ? 564 LEU A O     1 
ATOM   4414 C  CB    . LEU A 1 564 ? -15.139 14.328  30.263  1.00 72.13  ? 564 LEU A CB    1 
ATOM   4415 C  CG    . LEU A 1 564 ? -14.333 14.361  28.964  1.00 72.20  ? 564 LEU A CG    1 
ATOM   4416 C  CD1   . LEU A 1 564 ? -13.042 13.574  29.127  1.00 73.65  ? 564 LEU A CD1   1 
ATOM   4417 C  CD2   . LEU A 1 564 ? -15.159 13.813  27.812  1.00 73.32  ? 564 LEU A CD2   1 
ATOM   4418 N  N     . ASN A 1 565 ? -18.340 13.165  30.570  1.00 75.53  ? 565 ASN A N     1 
ATOM   4419 C  CA    . ASN A 1 565 ? -19.108 12.208  31.352  1.00 72.37  ? 565 ASN A CA    1 
ATOM   4420 C  C     . ASN A 1 565 ? -18.162 11.199  31.987  1.00 73.02  ? 565 ASN A C     1 
ATOM   4421 O  O     . ASN A 1 565 ? -17.702 10.266  31.320  1.00 71.70  ? 565 ASN A O     1 
ATOM   4422 C  CB    . ASN A 1 565 ? -20.146 11.506  30.474  1.00 71.82  ? 565 ASN A CB    1 
ATOM   4423 C  CG    . ASN A 1 565 ? -21.110 10.650  31.271  1.00 80.96  ? 565 ASN A CG    1 
ATOM   4424 O  OD1   . ASN A 1 565 ? -20.770 10.123  32.331  1.00 80.34  ? 565 ASN A OD1   1 
ATOM   4425 N  ND2   . ASN A 1 565 ? -22.325 10.502  30.756  1.00 84.18  ? 565 ASN A ND2   1 
ATOM   4426 N  N     . LEU A 1 566 ? -17.850 11.390  33.268  1.00 75.24  ? 566 LEU A N     1 
ATOM   4427 C  CA    . LEU A 1 566 ? -16.966 10.496  34.003  1.00 80.40  ? 566 LEU A CA    1 
ATOM   4428 C  C     . LEU A 1 566 ? -17.715 9.625   35.005  1.00 88.06  ? 566 LEU A C     1 
ATOM   4429 O  O     . LEU A 1 566 ? -17.078 8.940   35.812  1.00 93.87  ? 566 LEU A O     1 
ATOM   4430 C  CB    . LEU A 1 566 ? -15.878 11.300  34.717  1.00 76.97  ? 566 LEU A CB    1 
ATOM   4431 C  CG    . LEU A 1 566 ? -14.863 12.010  33.822  1.00 80.41  ? 566 LEU A CG    1 
ATOM   4432 C  CD1   . LEU A 1 566 ? -13.905 12.846  34.657  1.00 83.96  ? 566 LEU A CD1   1 
ATOM   4433 C  CD2   . LEU A 1 566 ? -14.104 10.993  32.986  1.00 72.46  ? 566 LEU A CD2   1 
ATOM   4434 N  N     . LYS A 1 567 ? -19.046 9.635   34.975  1.00 85.86  ? 567 LYS A N     1 
ATOM   4435 C  CA    . LYS A 1 567 ? -19.819 8.862   35.939  1.00 90.74  ? 567 LYS A CA    1 
ATOM   4436 C  C     . LYS A 1 567 ? -19.556 7.371   35.766  1.00 87.59  ? 567 LYS A C     1 
ATOM   4437 O  O     . LYS A 1 567 ? -19.441 6.866   34.646  1.00 81.16  ? 567 LYS A O     1 
ATOM   4438 C  CB    . LYS A 1 567 ? -21.310 9.169   35.788  1.00 99.22  ? 567 LYS A CB    1 
ATOM   4439 C  CG    . LYS A 1 567 ? -21.648 10.636  36.032  1.00 108.84 ? 567 LYS A CG    1 
ATOM   4440 C  CD    . LYS A 1 567 ? -23.147 10.877  36.078  1.00 119.72 ? 567 LYS A CD    1 
ATOM   4441 C  CE    . LYS A 1 567 ? -23.456 12.326  36.428  1.00 125.65 ? 567 LYS A CE    1 
ATOM   4442 N  NZ    . LYS A 1 567 ? -24.917 12.568  36.585  1.00 122.92 ? 567 LYS A NZ    1 
ATOM   4443 N  N     . GLY A 1 568 ? -19.462 6.665   36.889  1.00 92.05  ? 568 GLY A N     1 
ATOM   4444 C  CA    . GLY A 1 568 ? -19.041 5.282   36.883  1.00 88.16  ? 568 GLY A CA    1 
ATOM   4445 C  C     . GLY A 1 568 ? -17.551 5.081   37.023  1.00 99.31  ? 568 GLY A C     1 
ATOM   4446 O  O     . GLY A 1 568 ? -17.081 3.943   36.901  1.00 98.25  ? 568 GLY A O     1 
ATOM   4447 N  N     . LEU A 1 569 ? -16.792 6.149   37.264  1.00 95.09  ? 569 LEU A N     1 
ATOM   4448 C  CA    . LEU A 1 569 ? -15.353 6.052   37.471  1.00 104.24 ? 569 LEU A CA    1 
ATOM   4449 C  C     . LEU A 1 569 ? -14.978 6.720   38.788  1.00 113.91 ? 569 LEU A C     1 
ATOM   4450 O  O     . LEU A 1 569 ? -14.658 6.039   39.768  1.00 115.49 ? 569 LEU A O     1 
ATOM   4451 C  CB    . LEU A 1 569 ? -14.596 6.691   36.303  1.00 105.80 ? 569 LEU A CB    1 
ATOM   4452 C  CG    . LEU A 1 569 ? -14.956 6.209   34.894  1.00 91.84  ? 569 LEU A CG    1 
ATOM   4453 C  CD1   . LEU A 1 569 ? -14.136 6.941   33.844  1.00 83.93  ? 569 LEU A CD1   1 
ATOM   4454 C  CD2   . LEU A 1 569 ? -14.766 4.707   34.767  1.00 95.44  ? 569 LEU A CD2   1 
ATOM   4455 N  N     . GLY A 1 570 ? -15.016 8.050   38.820  1.00 129.57 ? 570 GLY A N     1 
ATOM   4456 C  CA    . GLY A 1 570 ? -14.792 8.793   40.046  1.00 128.78 ? 570 GLY A CA    1 
ATOM   4457 C  C     . GLY A 1 570 ? -13.352 8.827   40.514  1.00 135.75 ? 570 GLY A C     1 
ATOM   4458 O  O     . GLY A 1 570 ? -12.862 9.869   40.958  1.00 130.12 ? 570 GLY A O     1 
ATOM   4459 N  N     . ASP A 1 571 ? -12.666 7.691   40.426  1.00 144.64 ? 571 ASP A N     1 
ATOM   4460 C  CA    . ASP A 1 571 ? -11.287 7.570   40.879  1.00 142.51 ? 571 ASP A CA    1 
ATOM   4461 C  C     . ASP A 1 571 ? -10.271 8.006   39.830  1.00 138.80 ? 571 ASP A C     1 
ATOM   4462 O  O     . ASP A 1 571 ? -9.065  7.898   40.075  1.00 138.63 ? 571 ASP A O     1 
ATOM   4463 C  CB    . ASP A 1 571 ? -11.004 6.125   41.301  1.00 141.77 ? 571 ASP A CB    1 
ATOM   4464 C  CG    . ASP A 1 571 ? -11.363 5.125   40.221  1.00 142.62 ? 571 ASP A CG    1 
ATOM   4465 O  OD1   . ASP A 1 571 ? -12.097 5.503   39.283  1.00 139.39 ? 571 ASP A OD1   1 
ATOM   4466 O  OD2   . ASP A 1 571 ? -10.919 3.962   40.314  1.00 144.24 ? 571 ASP A OD2   1 
ATOM   4467 N  N     . VAL A 1 572 ? -10.725 8.496   38.677  1.00 120.51 ? 572 VAL A N     1 
ATOM   4468 C  CA    . VAL A 1 572 ? -9.807  8.918   37.626  1.00 113.07 ? 572 VAL A CA    1 
ATOM   4469 C  C     . VAL A 1 572 ? -9.095  10.193  38.053  1.00 108.21 ? 572 VAL A C     1 
ATOM   4470 O  O     . VAL A 1 572 ? -9.733  11.192  38.410  1.00 110.62 ? 572 VAL A O     1 
ATOM   4471 C  CB    . VAL A 1 572 ? -10.561 9.124   36.304  1.00 97.49  ? 572 VAL A CB    1 
ATOM   4472 C  CG1   . VAL A 1 572 ? -9.601  9.569   35.213  1.00 97.40  ? 572 VAL A CG1   1 
ATOM   4473 C  CG2   . VAL A 1 572 ? -11.284 7.850   35.902  1.00 107.94 ? 572 VAL A CG2   1 
ATOM   4474 N  N     . ASN A 1 573 ? -7.763  10.167  38.016  1.00 103.82 ? 573 ASN A N     1 
ATOM   4475 C  CA    . ASN A 1 573 ? -6.979  11.358  38.320  1.00 105.89 ? 573 ASN A CA    1 
ATOM   4476 C  C     . ASN A 1 573 ? -7.080  12.360  37.178  1.00 99.45  ? 573 ASN A C     1 
ATOM   4477 O  O     . ASN A 1 573 ? -6.313  12.291  36.212  1.00 102.48 ? 573 ASN A O     1 
ATOM   4478 C  CB    . ASN A 1 573 ? -5.517  10.994  38.584  1.00 108.91 ? 573 ASN A CB    1 
ATOM   4479 C  CG    . ASN A 1 573 ? -4.643  12.216  38.795  1.00 112.57 ? 573 ASN A CG    1 
ATOM   4480 O  OD1   . ASN A 1 573 ? -5.137  13.304  39.090  1.00 110.41 ? 573 ASN A OD1   1 
ATOM   4481 N  ND2   . ASN A 1 573 ? -3.335  12.041  38.643  1.00 116.96 ? 573 ASN A ND2   1 
ATOM   4482 N  N     . VAL A 1 574 ? -8.024  13.297  37.281  1.00 96.11  ? 574 VAL A N     1 
ATOM   4483 C  CA    . VAL A 1 574 ? -8.228  14.260  36.204  1.00 98.04  ? 574 VAL A CA    1 
ATOM   4484 C  C     . VAL A 1 574 ? -7.114  15.298  36.179  1.00 99.89  ? 574 VAL A C     1 
ATOM   4485 O  O     . VAL A 1 574 ? -6.808  15.863  35.121  1.00 92.27  ? 574 VAL A O     1 
ATOM   4486 C  CB    . VAL A 1 574 ? -9.612  14.918  36.340  1.00 95.81  ? 574 VAL A CB    1 
ATOM   4487 C  CG1   . VAL A 1 574 ? -10.701 13.943  35.919  1.00 87.66  ? 574 VAL A CG1   1 
ATOM   4488 C  CG2   . VAL A 1 574 ? -9.835  15.391  37.773  1.00 92.66  ? 574 VAL A CG2   1 
ATOM   4489 N  N     . GLU A 1 575 ? -6.492  15.570  37.328  1.00 106.36 ? 575 GLU A N     1 
ATOM   4490 C  CA    . GLU A 1 575 ? -5.416  16.555  37.382  1.00 105.80 ? 575 GLU A CA    1 
ATOM   4491 C  C     . GLU A 1 575 ? -4.297  16.198  36.411  1.00 101.84 ? 575 GLU A C     1 
ATOM   4492 O  O     . GLU A 1 575 ? -3.985  16.960  35.489  1.00 91.93  ? 575 GLU A O     1 
ATOM   4493 C  CB    . GLU A 1 575 ? -4.879  16.661  38.811  1.00 113.07 ? 575 GLU A CB    1 
ATOM   4494 C  CG    . GLU A 1 575 ? -5.910  17.093  39.843  1.00 118.91 ? 575 GLU A CG    1 
ATOM   4495 C  CD    . GLU A 1 575 ? -6.362  18.527  39.652  1.00 132.02 ? 575 GLU A CD    1 
ATOM   4496 O  OE1   . GLU A 1 575 ? -5.917  19.168  38.675  1.00 120.59 ? 575 GLU A OE1   1 
ATOM   4497 O  OE2   . GLU A 1 575 ? -7.159  19.013  40.481  1.00 133.70 ? 575 GLU A OE2   1 
ATOM   4498 N  N     . GLU A 1 576 ? -3.680  15.030  36.606  1.00 107.43 ? 576 GLU A N     1 
ATOM   4499 C  CA    . GLU A 1 576 ? -2.565  14.618  35.764  1.00 108.46 ? 576 GLU A CA    1 
ATOM   4500 C  C     . GLU A 1 576 ? -3.009  14.210  34.365  1.00 105.08 ? 576 GLU A C     1 
ATOM   4501 O  O     . GLU A 1 576 ? -2.201  14.263  33.431  1.00 100.34 ? 576 GLU A O     1 
ATOM   4502 C  CB    . GLU A 1 576 ? -1.812  13.465  36.431  1.00 115.11 ? 576 GLU A CB    1 
ATOM   4503 C  CG    . GLU A 1 576 ? -0.549  13.028  35.706  1.00 120.49 ? 576 GLU A CG    1 
ATOM   4504 C  CD    . GLU A 1 576 ? 0.192   11.931  36.446  1.00 128.03 ? 576 GLU A CD    1 
ATOM   4505 O  OE1   . GLU A 1 576 ? -0.418  11.290  37.327  1.00 131.12 ? 576 GLU A OE1   1 
ATOM   4506 O  OE2   . GLU A 1 576 ? 1.386   11.713  36.151  1.00 129.60 ? 576 GLU A OE2   1 
ATOM   4507 N  N     . LEU A 1 577 ? -4.271  13.809  34.197  1.00 100.30 ? 577 LEU A N     1 
ATOM   4508 C  CA    . LEU A 1 577 ? -4.743  13.351  32.896  1.00 87.83  ? 577 LEU A CA    1 
ATOM   4509 C  C     . LEU A 1 577 ? -4.871  14.486  31.888  1.00 82.73  ? 577 LEU A C     1 
ATOM   4510 O  O     . LEU A 1 577 ? -4.876  14.225  30.680  1.00 73.23  ? 577 LEU A O     1 
ATOM   4511 C  CB    . LEU A 1 577 ? -6.084  12.632  33.053  1.00 84.89  ? 577 LEU A CB    1 
ATOM   4512 C  CG    . LEU A 1 577 ? -6.658  11.954  31.809  1.00 79.47  ? 577 LEU A CG    1 
ATOM   4513 C  CD1   . LEU A 1 577 ? -5.619  11.046  31.167  1.00 79.80  ? 577 LEU A CD1   1 
ATOM   4514 C  CD2   . LEU A 1 577 ? -7.910  11.167  32.168  1.00 78.61  ? 577 LEU A CD2   1 
ATOM   4515 N  N     . PHE A 1 578 ? -4.976  15.732  32.352  1.00 85.41  ? 578 PHE A N     1 
ATOM   4516 C  CA    . PHE A 1 578 ? -5.047  16.888  31.468  1.00 77.72  ? 578 PHE A CA    1 
ATOM   4517 C  C     . PHE A 1 578 ? -3.950  17.910  31.722  1.00 77.56  ? 578 PHE A C     1 
ATOM   4518 O  O     . PHE A 1 578 ? -3.951  18.966  31.078  1.00 79.03  ? 578 PHE A O     1 
ATOM   4519 C  CB    . PHE A 1 578 ? -6.414  17.576  31.590  1.00 72.30  ? 578 PHE A CB    1 
ATOM   4520 C  CG    . PHE A 1 578 ? -7.467  16.988  30.700  1.00 71.65  ? 578 PHE A CG    1 
ATOM   4521 C  CD1   . PHE A 1 578 ? -7.551  17.360  29.367  1.00 69.97  ? 578 PHE A CD1   1 
ATOM   4522 C  CD2   . PHE A 1 578 ? -8.375  16.067  31.194  1.00 71.14  ? 578 PHE A CD2   1 
ATOM   4523 C  CE1   . PHE A 1 578 ? -8.520  16.823  28.540  1.00 67.67  ? 578 PHE A CE1   1 
ATOM   4524 C  CE2   . PHE A 1 578 ? -9.347  15.526  30.374  1.00 76.50  ? 578 PHE A CE2   1 
ATOM   4525 C  CZ    . PHE A 1 578 ? -9.419  15.904  29.044  1.00 74.57  ? 578 PHE A CZ    1 
ATOM   4526 N  N     . GLY A 1 579 ? -3.019  17.633  32.631  1.00 80.53  ? 579 GLY A N     1 
ATOM   4527 C  CA    . GLY A 1 579 ? -1.954  18.567  32.935  1.00 82.20  ? 579 GLY A CA    1 
ATOM   4528 C  C     . GLY A 1 579 ? -1.206  19.060  31.713  1.00 81.32  ? 579 GLY A C     1 
ATOM   4529 O  O     . GLY A 1 579 ? -0.648  18.264  30.951  1.00 79.37  ? 579 GLY A O     1 
ATOM   4530 N  N     . ILE A 1 580 ? -1.197  20.378  31.512  1.00 79.61  ? 580 ILE A N     1 
ATOM   4531 C  CA    . ILE A 1 580 ? -0.449  20.993  30.421  1.00 77.37  ? 580 ILE A CA    1 
ATOM   4532 C  C     . ILE A 1 580 ? 0.791   21.666  30.991  1.00 73.35  ? 580 ILE A C     1 
ATOM   4533 O  O     . ILE A 1 580 ? 0.773   22.860  31.309  1.00 86.23  ? 580 ILE A O     1 
ATOM   4534 C  CB    . ILE A 1 580 ? -1.315  21.997  29.639  1.00 71.94  ? 580 ILE A CB    1 
ATOM   4535 C  CG1   . ILE A 1 580 ? -2.460  21.274  28.925  1.00 75.77  ? 580 ILE A CG1   1 
ATOM   4536 C  CG2   . ILE A 1 580 ? -0.466  22.771  28.645  1.00 72.88  ? 580 ILE A CG2   1 
ATOM   4537 C  CD1   . ILE A 1 580 ? -3.320  22.182  28.068  1.00 74.52  ? 580 ILE A CD1   1 
ATOM   4538 N  N     . SER A 1 581 ? 1.871   20.904  31.132  1.00 73.78  ? 581 SER A N     1 
ATOM   4539 C  CA    . SER A 1 581 ? 3.102   21.431  31.700  1.00 76.00  ? 581 SER A CA    1 
ATOM   4540 C  C     . SER A 1 581 ? 3.830   22.286  30.672  1.00 80.34  ? 581 SER A C     1 
ATOM   4541 O  O     . SER A 1 581 ? 4.122   21.827  29.563  1.00 86.05  ? 581 SER A O     1 
ATOM   4542 C  CB    . SER A 1 581 ? 4.004   20.291  32.169  1.00 81.64  ? 581 SER A CB    1 
ATOM   4543 O  OG    . SER A 1 581 ? 5.258   20.785  32.604  1.00 88.70  ? 581 SER A OG    1 
ATOM   4544 N  N     . LYS A 1 582 ? 4.120   23.534  31.040  1.00 86.49  ? 582 LYS A N     1 
ATOM   4545 C  CA    . LYS A 1 582 ? 4.903   24.393  30.160  1.00 85.36  ? 582 LYS A CA    1 
ATOM   4546 C  C     . LYS A 1 582 ? 6.291   23.813  29.929  1.00 84.57  ? 582 LYS A C     1 
ATOM   4547 O  O     . LYS A 1 582 ? 6.826   23.881  28.816  1.00 83.00  ? 582 LYS A O     1 
ATOM   4548 C  CB    . LYS A 1 582 ? 4.997   25.799  30.752  1.00 85.96  ? 582 LYS A CB    1 
ATOM   4549 C  CG    . LYS A 1 582 ? 5.834   26.768  29.939  1.00 77.02  ? 582 LYS A CG    1 
ATOM   4550 C  CD    . LYS A 1 582 ? 5.811   28.154  30.561  1.00 82.82  ? 582 LYS A CD    1 
ATOM   4551 C  CE    . LYS A 1 582 ? 6.650   29.136  29.765  1.00 81.88  ? 582 LYS A CE    1 
ATOM   4552 N  NZ    . LYS A 1 582 ? 6.621   30.492  30.376  1.00 83.75  ? 582 LYS A NZ    1 
ATOM   4553 N  N     . GLU A 1 583 ? 6.887   23.232  30.971  1.00 93.89  ? 583 GLU A N     1 
ATOM   4554 C  CA    . GLU A 1 583 ? 8.219   22.652  30.842  1.00 95.86  ? 583 GLU A CA    1 
ATOM   4555 C  C     . GLU A 1 583 ? 8.240   21.555  29.786  1.00 93.39  ? 583 GLU A C     1 
ATOM   4556 O  O     . GLU A 1 583 ? 9.219   21.413  29.044  1.00 92.88  ? 583 GLU A O     1 
ATOM   4557 C  CB    . GLU A 1 583 ? 8.686   22.108  32.193  1.00 102.47 ? 583 GLU A CB    1 
ATOM   4558 C  CG    . GLU A 1 583 ? 8.731   23.142  33.317  1.00 109.42 ? 583 GLU A CG    1 
ATOM   4559 C  CD    . GLU A 1 583 ? 7.350   23.565  33.794  1.00 111.38 ? 583 GLU A CD    1 
ATOM   4560 O  OE1   . GLU A 1 583 ? 6.363   22.893  33.427  1.00 107.30 ? 583 GLU A OE1   1 
ATOM   4561 O  OE2   . GLU A 1 583 ? 7.250   24.571  34.529  1.00 113.29 ? 583 GLU A OE2   1 
ATOM   4562 N  N     . PHE A 1 584 ? 7.165   20.769  29.700  1.00 82.86  ? 584 PHE A N     1 
ATOM   4563 C  CA    . PHE A 1 584 ? 7.127   19.687  28.723  1.00 75.75  ? 584 PHE A CA    1 
ATOM   4564 C  C     . PHE A 1 584 ? 6.932   20.219  27.310  1.00 70.82  ? 584 PHE A C     1 
ATOM   4565 O  O     . PHE A 1 584 ? 7.567   19.735  26.366  1.00 70.44  ? 584 PHE A O     1 
ATOM   4566 C  CB    . PHE A 1 584 ? 6.018   18.696  29.074  1.00 73.21  ? 584 PHE A CB    1 
ATOM   4567 C  CG    . PHE A 1 584 ? 5.748   17.688  27.992  1.00 68.06  ? 584 PHE A CG    1 
ATOM   4568 C  CD1   . PHE A 1 584 ? 6.601   16.617  27.797  1.00 64.85  ? 584 PHE A CD1   1 
ATOM   4569 C  CD2   . PHE A 1 584 ? 4.642   17.815  27.167  1.00 68.16  ? 584 PHE A CD2   1 
ATOM   4570 C  CE1   . PHE A 1 584 ? 6.357   15.691  26.800  1.00 66.23  ? 584 PHE A CE1   1 
ATOM   4571 C  CE2   . PHE A 1 584 ? 4.391   16.891  26.168  1.00 60.94  ? 584 PHE A CE2   1 
ATOM   4572 C  CZ    . PHE A 1 584 ? 5.250   15.829  25.985  1.00 61.21  ? 584 PHE A CZ    1 
ATOM   4573 N  N     . TRP A 1 585 ? 6.058   21.211  27.142  1.00 69.34  ? 585 TRP A N     1 
ATOM   4574 C  CA    . TRP A 1 585 ? 5.724   21.683  25.805  1.00 71.04  ? 585 TRP A CA    1 
ATOM   4575 C  C     . TRP A 1 585 ? 6.777   22.615  25.221  1.00 72.15  ? 585 TRP A C     1 
ATOM   4576 O  O     . TRP A 1 585 ? 6.812   22.796  23.998  1.00 65.64  ? 585 TRP A O     1 
ATOM   4577 C  CB    . TRP A 1 585 ? 4.356   22.363  25.826  1.00 69.71  ? 585 TRP A CB    1 
ATOM   4578 C  CG    . TRP A 1 585 ? 3.253   21.372  25.992  1.00 71.91  ? 585 TRP A CG    1 
ATOM   4579 C  CD1   . TRP A 1 585 ? 2.708   20.938  27.165  1.00 71.29  ? 585 TRP A CD1   1 
ATOM   4580 C  CD2   . TRP A 1 585 ? 2.579   20.662  24.949  1.00 66.97  ? 585 TRP A CD2   1 
ATOM   4581 N  NE1   . TRP A 1 585 ? 1.725   20.011  26.915  1.00 64.54  ? 585 TRP A NE1   1 
ATOM   4582 C  CE2   . TRP A 1 585 ? 1.626   19.824  25.562  1.00 63.64  ? 585 TRP A CE2   1 
ATOM   4583 C  CE3   . TRP A 1 585 ? 2.682   20.659  23.554  1.00 63.30  ? 585 TRP A CE3   1 
ATOM   4584 C  CZ2   . TRP A 1 585 ? 0.783   18.993  24.830  1.00 65.46  ? 585 TRP A CZ2   1 
ATOM   4585 C  CZ3   . TRP A 1 585 ? 1.844   19.832  22.830  1.00 67.96  ? 585 TRP A CZ3   1 
ATOM   4586 C  CH2   . TRP A 1 585 ? 0.907   19.010  23.468  1.00 63.54  ? 585 TRP A CH2   1 
ATOM   4587 N  N     . GLU A 1 586 ? 7.637   23.205  26.054  1.00 73.14  ? 586 GLU A N     1 
ATOM   4588 C  CA    . GLU A 1 586 ? 8.754   23.969  25.514  1.00 69.72  ? 586 GLU A CA    1 
ATOM   4589 C  C     . GLU A 1 586 ? 9.787   23.054  24.872  1.00 70.78  ? 586 GLU A C     1 
ATOM   4590 O  O     . GLU A 1 586 ? 10.444  23.447  23.900  1.00 67.67  ? 586 GLU A O     1 
ATOM   4591 C  CB    . GLU A 1 586 ? 9.399   24.820  26.607  1.00 81.37  ? 586 GLU A CB    1 
ATOM   4592 C  CG    . GLU A 1 586 ? 8.548   25.997  27.056  1.00 76.89  ? 586 GLU A CG    1 
ATOM   4593 C  CD    . GLU A 1 586 ? 9.332   26.996  27.882  1.00 91.61  ? 586 GLU A CD    1 
ATOM   4594 O  OE1   . GLU A 1 586 ? 10.452  26.654  28.316  1.00 90.81  ? 586 GLU A OE1   1 
ATOM   4595 O  OE2   . GLU A 1 586 ? 8.833   28.125  28.090  1.00 86.95  ? 586 GLU A OE2   1 
ATOM   4596 N  N     . LYS A 1 587 ? 9.944   21.838  25.398  1.00 76.41  ? 587 LYS A N     1 
ATOM   4597 C  CA    . LYS A 1 587 ? 10.806  20.848  24.761  1.00 65.27  ? 587 LYS A CA    1 
ATOM   4598 C  C     . LYS A 1 587 ? 10.129  20.225  23.547  1.00 65.02  ? 587 LYS A C     1 
ATOM   4599 O  O     . LYS A 1 587 ? 10.794  19.913  22.553  1.00 65.59  ? 587 LYS A O     1 
ATOM   4600 C  CB    . LYS A 1 587 ? 11.193  19.767  25.770  1.00 67.01  ? 587 LYS A CB    1 
ATOM   4601 C  CG    . LYS A 1 587 ? 11.739  18.487  25.148  1.00 78.35  ? 587 LYS A CG    1 
ATOM   4602 C  CD    . LYS A 1 587 ? 13.112  18.693  24.527  1.00 81.51  ? 587 LYS A CD    1 
ATOM   4603 C  CE    . LYS A 1 587 ? 13.692  17.373  24.036  1.00 82.90  ? 587 LYS A CE    1 
ATOM   4604 N  NZ    . LYS A 1 587 ? 15.068  17.532  23.487  1.00 87.41  ? 587 LYS A NZ    1 
ATOM   4605 N  N     . GLU A 1 588 ? 8.809   20.045  23.608  1.00 65.19  ? 588 GLU A N     1 
ATOM   4606 C  CA    . GLU A 1 588 ? 8.091   19.432  22.495  1.00 62.81  ? 588 GLU A CA    1 
ATOM   4607 C  C     . GLU A 1 588 ? 8.217   20.269  21.228  1.00 62.65  ? 588 GLU A C     1 
ATOM   4608 O  O     . GLU A 1 588 ? 8.445   19.729  20.139  1.00 59.02  ? 588 GLU A O     1 
ATOM   4609 C  CB    . GLU A 1 588 ? 6.623   19.235  22.871  1.00 61.39  ? 588 GLU A CB    1 
ATOM   4610 C  CG    . GLU A 1 588 ? 5.881   18.246  21.989  1.00 60.93  ? 588 GLU A CG    1 
ATOM   4611 C  CD    . GLU A 1 588 ? 6.412   16.834  22.128  1.00 57.01  ? 588 GLU A CD    1 
ATOM   4612 O  OE1   . GLU A 1 588 ? 6.927   16.499  23.216  1.00 61.26  ? 588 GLU A OE1   1 
ATOM   4613 O  OE2   . GLU A 1 588 ? 6.321   16.064  21.149  1.00 55.81  ? 588 GLU A OE2   1 
ATOM   4614 N  N     . VAL A 1 589 ? 8.073   21.592  21.348  1.00 71.23  ? 589 VAL A N     1 
ATOM   4615 C  CA    . VAL A 1 589 ? 8.185   22.465  20.180  1.00 66.94  ? 589 VAL A CA    1 
ATOM   4616 C  C     . VAL A 1 589 ? 9.593   22.407  19.600  1.00 66.10  ? 589 VAL A C     1 
ATOM   4617 O  O     . VAL A 1 589 ? 9.775   22.374  18.376  1.00 66.61  ? 589 VAL A O     1 
ATOM   4618 C  CB    . VAL A 1 589 ? 7.783   23.905  20.547  1.00 63.52  ? 589 VAL A CB    1 
ATOM   4619 C  CG1   . VAL A 1 589 ? 6.279   24.005  20.731  1.00 58.48  ? 589 VAL A CG1   1 
ATOM   4620 C  CG2   . VAL A 1 589 ? 8.510   24.347  21.806  1.00 67.70  ? 589 VAL A CG2   1 
ATOM   4621 N  N     . GLU A 1 590 ? 10.610  22.398  20.465  1.00 70.70  ? 590 GLU A N     1 
ATOM   4622 C  CA    . GLU A 1 590 ? 11.986  22.287  19.994  1.00 70.55  ? 590 GLU A CA    1 
ATOM   4623 C  C     . GLU A 1 590 ? 12.172  21.040  19.137  1.00 74.46  ? 590 GLU A C     1 
ATOM   4624 O  O     . GLU A 1 590 ? 12.740  21.103  18.040  1.00 73.79  ? 590 GLU A O     1 
ATOM   4625 C  CB    . GLU A 1 590 ? 12.945  22.275  21.186  1.00 77.64  ? 590 GLU A CB    1 
ATOM   4626 C  CG    . GLU A 1 590 ? 14.419  22.186  20.810  1.00 84.15  ? 590 GLU A CG    1 
ATOM   4627 C  CD    . GLU A 1 590 ? 14.967  23.495  20.272  1.00 111.03 ? 590 GLU A CD    1 
ATOM   4628 O  OE1   . GLU A 1 590 ? 14.427  24.560  20.638  1.00 116.52 ? 590 GLU A OE1   1 
ATOM   4629 O  OE2   . GLU A 1 590 ? 15.936  23.459  19.485  1.00 109.90 ? 590 GLU A OE2   1 
ATOM   4630 N  N     . GLU A 1 591 ? 11.690  19.891  19.622  1.00 71.12  ? 591 GLU A N     1 
ATOM   4631 C  CA    . GLU A 1 591 ? 11.838  18.653  18.862  1.00 64.50  ? 591 GLU A CA    1 
ATOM   4632 C  C     . GLU A 1 591 ? 11.049  18.703  17.560  1.00 62.16  ? 591 GLU A C     1 
ATOM   4633 O  O     . GLU A 1 591 ? 11.545  18.275  16.512  1.00 65.89  ? 591 GLU A O     1 
ATOM   4634 C  CB    . GLU A 1 591 ? 11.406  17.456  19.709  1.00 65.34  ? 591 GLU A CB    1 
ATOM   4635 C  CG    . GLU A 1 591 ? 12.397  17.103  20.801  1.00 72.43  ? 591 GLU A CG    1 
ATOM   4636 C  CD    . GLU A 1 591 ? 13.798  16.878  20.260  1.00 79.02  ? 591 GLU A CD    1 
ATOM   4637 O  OE1   . GLU A 1 591 ? 13.936  16.204  19.215  1.00 78.56  ? 591 GLU A OE1   1 
ATOM   4638 O  OE2   . GLU A 1 591 ? 14.762  17.382  20.875  1.00 73.72  ? 591 GLU A OE2   1 
ATOM   4639 N  N     . ILE A 1 592 ? 9.821   19.218  17.603  1.00 59.57  ? 592 ILE A N     1 
ATOM   4640 C  CA    . ILE A 1 592 ? 9.038   19.336  16.377  1.00 60.56  ? 592 ILE A CA    1 
ATOM   4641 C  C     . ILE A 1 592 ? 9.703   20.315  15.417  1.00 67.11  ? 592 ILE A C     1 
ATOM   4642 O  O     . ILE A 1 592 ? 9.764   20.075  14.204  1.00 64.53  ? 592 ILE A O     1 
ATOM   4643 C  CB    . ILE A 1 592 ? 7.590   19.745  16.703  1.00 59.97  ? 592 ILE A CB    1 
ATOM   4644 C  CG1   . ILE A 1 592 ? 6.943   18.707  17.621  1.00 66.31  ? 592 ILE A CG1   1 
ATOM   4645 C  CG2   . ILE A 1 592 ? 6.774   19.894  15.431  1.00 54.63  ? 592 ILE A CG2   1 
ATOM   4646 C  CD1   . ILE A 1 592 ? 5.482   18.977  17.922  1.00 57.03  ? 592 ILE A CD1   1 
ATOM   4647 N  N     . ASP A 1 593 ? 10.225  21.426  15.940  1.00 68.25  ? 593 ASP A N     1 
ATOM   4648 C  CA    . ASP A 1 593 ? 10.927  22.382  15.089  1.00 65.91  ? 593 ASP A CA    1 
ATOM   4649 C  C     . ASP A 1 593 ? 12.130  21.729  14.420  1.00 66.65  ? 593 ASP A C     1 
ATOM   4650 O  O     . ASP A 1 593 ? 12.252  21.729  13.189  1.00 67.13  ? 593 ASP A O     1 
ATOM   4651 C  CB    . ASP A 1 593 ? 11.355  23.603  15.906  1.00 64.71  ? 593 ASP A CB    1 
ATOM   4652 C  CG    . ASP A 1 593 ? 12.031  24.666  15.055  1.00 72.87  ? 593 ASP A CG    1 
ATOM   4653 O  OD1   . ASP A 1 593 ? 11.398  25.146  14.090  1.00 71.88  ? 593 ASP A OD1   1 
ATOM   4654 O  OD2   . ASP A 1 593 ? 13.192  25.028  15.348  1.00 69.99  ? 593 ASP A OD2   1 
ATOM   4655 N  N     . LYS A 1 594 ? 13.034  21.160  15.222  1.00 68.63  ? 594 LYS A N     1 
ATOM   4656 C  CA    . LYS A 1 594 ? 14.216  20.516  14.658  1.00 66.92  ? 594 LYS A CA    1 
ATOM   4657 C  C     . LYS A 1 594 ? 13.830  19.446  13.646  1.00 66.26  ? 594 LYS A C     1 
ATOM   4658 O  O     . LYS A 1 594 ? 14.475  19.309  12.599  1.00 65.69  ? 594 LYS A O     1 
ATOM   4659 C  CB    . LYS A 1 594 ? 15.070  19.914  15.774  1.00 66.39  ? 594 LYS A CB    1 
ATOM   4660 C  CG    . LYS A 1 594 ? 15.641  20.936  16.741  1.00 67.60  ? 594 LYS A CG    1 
ATOM   4661 C  CD    . LYS A 1 594 ? 16.550  20.271  17.760  1.00 73.08  ? 594 LYS A CD    1 
ATOM   4662 C  CE    . LYS A 1 594 ? 15.832  19.137  18.478  1.00 71.61  ? 594 LYS A CE    1 
ATOM   4663 N  NZ    . LYS A 1 594 ? 16.703  18.475  19.487  1.00 69.10  ? 594 LYS A NZ    1 
ATOM   4664 N  N     . TYR A 1 595 ? 12.778  18.680  13.937  1.00 64.24  ? 595 TYR A N     1 
ATOM   4665 C  CA    . TYR A 1 595 ? 12.344  17.639  13.011  1.00 61.46  ? 595 TYR A CA    1 
ATOM   4666 C  C     . TYR A 1 595 ? 11.867  18.242  11.695  1.00 63.73  ? 595 TYR A C     1 
ATOM   4667 O  O     . TYR A 1 595 ? 12.326  17.851  10.615  1.00 60.05  ? 595 TYR A O     1 
ATOM   4668 C  CB    . TYR A 1 595 ? 11.243  16.793  13.653  1.00 62.90  ? 595 TYR A CB    1 
ATOM   4669 C  CG    . TYR A 1 595 ? 10.753  15.659  12.780  1.00 59.91  ? 595 TYR A CG    1 
ATOM   4670 C  CD1   . TYR A 1 595 ? 11.480  14.483  12.665  1.00 54.55  ? 595 TYR A CD1   1 
ATOM   4671 C  CD2   . TYR A 1 595 ? 9.562   15.763  12.072  1.00 57.78  ? 595 TYR A CD2   1 
ATOM   4672 C  CE1   . TYR A 1 595 ? 11.039  13.446  11.869  1.00 59.62  ? 595 TYR A CE1   1 
ATOM   4673 C  CE2   . TYR A 1 595 ? 9.111   14.729  11.274  1.00 52.25  ? 595 TYR A CE2   1 
ATOM   4674 C  CZ    . TYR A 1 595 ? 9.854   13.575  11.176  1.00 58.60  ? 595 TYR A CZ    1 
ATOM   4675 O  OH    . TYR A 1 595 ? 9.409   12.542  10.383  1.00 64.28  ? 595 TYR A OH    1 
ATOM   4676 N  N     . LEU A 1 596 ? 10.951  19.209  11.767  1.00 62.23  ? 596 LEU A N     1 
ATOM   4677 C  CA    . LEU A 1 596 ? 10.383  19.786  10.552  1.00 67.58  ? 596 LEU A CA    1 
ATOM   4678 C  C     . LEU A 1 596 ? 11.433  20.536  9.738   1.00 68.12  ? 596 LEU A C     1 
ATOM   4679 O  O     . LEU A 1 596 ? 11.416  20.497  8.502   1.00 67.65  ? 596 LEU A O     1 
ATOM   4680 C  CB    . LEU A 1 596 ? 9.218   20.709  10.908  1.00 66.42  ? 596 LEU A CB    1 
ATOM   4681 C  CG    . LEU A 1 596 ? 7.971   20.014  11.457  1.00 60.03  ? 596 LEU A CG    1 
ATOM   4682 C  CD1   . LEU A 1 596 ? 6.950   21.040  11.918  1.00 53.47  ? 596 LEU A CD1   1 
ATOM   4683 C  CD2   . LEU A 1 596 ? 7.373   19.090  10.406  1.00 53.50  ? 596 LEU A CD2   1 
ATOM   4684 N  N     . GLU A 1 597 ? 12.351  21.234  10.409  1.00 68.32  ? 597 GLU A N     1 
ATOM   4685 C  CA    . GLU A 1 597 ? 13.388  21.956  9.679   1.00 70.68  ? 597 GLU A CA    1 
ATOM   4686 C  C     . GLU A 1 597 ? 14.289  20.996  8.915   1.00 68.93  ? 597 GLU A C     1 
ATOM   4687 O  O     . GLU A 1 597 ? 14.695  21.280  7.782   1.00 71.73  ? 597 GLU A O     1 
ATOM   4688 C  CB    . GLU A 1 597 ? 14.214  22.811  10.640  1.00 76.23  ? 597 GLU A CB    1 
ATOM   4689 C  CG    . GLU A 1 597 ? 15.362  23.547  9.973   1.00 83.01  ? 597 GLU A CG    1 
ATOM   4690 C  CD    . GLU A 1 597 ? 16.249  24.264  10.969  1.00 88.12  ? 597 GLU A CD    1 
ATOM   4691 O  OE1   . GLU A 1 597 ? 15.946  24.219  12.181  1.00 83.70  ? 597 GLU A OE1   1 
ATOM   4692 O  OE2   . GLU A 1 597 ? 17.252  24.869  10.537  1.00 94.16  ? 597 GLU A OE2   1 
ATOM   4693 N  N     . ASP A 1 598 ? 14.607  19.852  9.519   1.00 74.18  ? 598 ASP A N     1 
ATOM   4694 C  CA    . ASP A 1 598 ? 15.509  18.897  8.888   1.00 70.68  ? 598 ASP A CA    1 
ATOM   4695 C  C     . ASP A 1 598 ? 14.800  18.077  7.817   1.00 68.83  ? 598 ASP A C     1 
ATOM   4696 O  O     . ASP A 1 598 ? 15.297  17.951  6.692   1.00 73.15  ? 598 ASP A O     1 
ATOM   4697 C  CB    . ASP A 1 598 ? 16.117  17.977  9.948   1.00 71.61  ? 598 ASP A CB    1 
ATOM   4698 C  CG    . ASP A 1 598 ? 16.863  16.804  9.341   1.00 83.36  ? 598 ASP A CG    1 
ATOM   4699 O  OD1   . ASP A 1 598 ? 17.829  17.043  8.588   1.00 89.60  ? 598 ASP A OD1   1 
ATOM   4700 O  OD2   . ASP A 1 598 ? 16.485  15.645  9.618   1.00 81.88  ? 598 ASP A OD2   1 
ATOM   4701 N  N     . GLN A 1 599 ? 13.632  17.524  8.143   1.00 62.81  ? 599 GLN A N     1 
ATOM   4702 C  CA    . GLN A 1 599 ? 13.024  16.519  7.278   1.00 60.17  ? 599 GLN A CA    1 
ATOM   4703 C  C     . GLN A 1 599 ? 12.215  17.140  6.146   1.00 63.70  ? 599 GLN A C     1 
ATOM   4704 O  O     . GLN A 1 599 ? 12.287  16.669  5.005   1.00 65.40  ? 599 GLN A O     1 
ATOM   4705 C  CB    . GLN A 1 599 ? 12.155  15.580  8.112   1.00 58.41  ? 599 GLN A CB    1 
ATOM   4706 C  CG    . GLN A 1 599 ? 12.946  14.765  9.122   1.00 60.65  ? 599 GLN A CG    1 
ATOM   4707 C  CD    . GLN A 1 599 ? 13.827  13.716  8.467   1.00 62.35  ? 599 GLN A CD    1 
ATOM   4708 O  OE1   . GLN A 1 599 ? 13.372  12.941  7.624   1.00 56.43  ? 599 GLN A OE1   1 
ATOM   4709 N  NE2   . GLN A 1 599 ? 15.097  13.686  8.854   1.00 63.44  ? 599 GLN A NE2   1 
ATOM   4710 N  N     . VAL A 1 600 ? 11.433  18.180  6.427   1.00 59.48  ? 600 VAL A N     1 
ATOM   4711 C  CA    . VAL A 1 600 ? 10.672  18.821  5.360   1.00 55.07  ? 600 VAL A CA    1 
ATOM   4712 C  C     . VAL A 1 600 ? 11.443  19.991  4.754   1.00 63.52  ? 600 VAL A C     1 
ATOM   4713 O  O     . VAL A 1 600 ? 11.257  20.308  3.575   1.00 62.34  ? 600 VAL A O     1 
ATOM   4714 C  CB    . VAL A 1 600 ? 9.288   19.268  5.857   1.00 62.06  ? 600 VAL A CB    1 
ATOM   4715 C  CG1   . VAL A 1 600 ? 8.386   19.591  4.673   1.00 58.51  ? 600 VAL A CG1   1 
ATOM   4716 C  CG2   . VAL A 1 600 ? 8.662   18.191  6.738   1.00 61.02  ? 600 VAL A CG2   1 
ATOM   4717 N  N     . ASN A 1 601 ? 12.302  20.640  5.539   1.00 61.11  ? 601 ASN A N     1 
ATOM   4718 C  CA    . ASN A 1 601 ? 13.264  21.601  5.013   1.00 67.33  ? 601 ASN A CA    1 
ATOM   4719 C  C     . ASN A 1 601 ? 12.611  22.641  4.110   1.00 65.77  ? 601 ASN A C     1 
ATOM   4720 O  O     . ASN A 1 601 ? 11.735  23.392  4.550   1.00 65.02  ? 601 ASN A O     1 
ATOM   4721 C  CB    . ASN A 1 601 ? 14.372  20.861  4.259   1.00 65.29  ? 601 ASN A CB    1 
ATOM   4722 C  CG    . ASN A 1 601 ? 15.587  21.726  4.011   1.00 74.58  ? 601 ASN A CG    1 
ATOM   4723 O  OD1   . ASN A 1 601 ? 15.728  22.803  4.592   1.00 79.25  ? 601 ASN A OD1   1 
ATOM   4724 N  ND2   . ASN A 1 601 ? 16.479  21.255  3.146   1.00 70.65  ? 601 ASN A ND2   1 
ATOM   4725 N  N     . ALA A 1 602 ? 13.023  22.681  2.842   1.00 65.30  ? 602 ALA A N     1 
ATOM   4726 C  CA    . ALA A 1 602 ? 12.611  23.725  1.911   1.00 61.15  ? 602 ALA A CA    1 
ATOM   4727 C  C     . ALA A 1 602 ? 11.249  23.475  1.276   1.00 61.06  ? 602 ALA A C     1 
ATOM   4728 O  O     . ALA A 1 602 ? 10.776  24.326  0.517   1.00 69.69  ? 602 ALA A O     1 
ATOM   4729 C  CB    . ALA A 1 602 ? 13.662  23.889  0.811   1.00 63.15  ? 602 ALA A CB    1 
ATOM   4730 N  N     . ASP A 1 603 ? 10.616  22.338  1.544   1.00 63.45  ? 603 ASP A N     1 
ATOM   4731 C  CA    . ASP A 1 603 ? 9.273   22.068  1.052   1.00 63.36  ? 603 ASP A CA    1 
ATOM   4732 C  C     . ASP A 1 603 ? 8.215   22.223  2.135   1.00 58.52  ? 603 ASP A C     1 
ATOM   4733 O  O     . ASP A 1 603 ? 7.030   22.001  1.866   1.00 55.80  ? 603 ASP A O     1 
ATOM   4734 C  CB    . ASP A 1 603 ? 9.207   20.663  0.445   1.00 58.15  ? 603 ASP A CB    1 
ATOM   4735 C  CG    . ASP A 1 603 ? 9.898   20.580  -0.904  1.00 64.90  ? 603 ASP A CG    1 
ATOM   4736 O  OD1   . ASP A 1 603 ? 9.489   21.316  -1.828  1.00 66.09  ? 603 ASP A OD1   1 
ATOM   4737 O  OD2   . ASP A 1 603 ? 10.859  19.792  -1.039  1.00 60.97  ? 603 ASP A OD2   1 
ATOM   4738 N  N     . LEU A 1 604 ? 8.616   22.601  3.340   1.00 56.16  ? 604 LEU A N     1 
ATOM   4739 C  CA    . LEU A 1 604 ? 7.676   22.858  4.419   1.00 57.32  ? 604 LEU A CA    1 
ATOM   4740 C  C     . LEU A 1 604 ? 6.798   24.051  4.068   1.00 56.43  ? 604 LEU A C     1 
ATOM   4741 O  O     . LEU A 1 604 ? 7.325   25.147  3.832   1.00 63.77  ? 604 LEU A O     1 
ATOM   4742 C  CB    . LEU A 1 604 ? 8.426   23.128  5.718   1.00 57.81  ? 604 LEU A CB    1 
ATOM   4743 C  CG    . LEU A 1 604 ? 7.547   23.398  6.939   1.00 59.19  ? 604 LEU A CG    1 
ATOM   4744 C  CD1   . LEU A 1 604 ? 6.715   22.170  7.267   1.00 54.99  ? 604 LEU A CD1   1 
ATOM   4745 C  CD2   . LEU A 1 604 ? 8.391   23.821  8.133   1.00 57.27  ? 604 LEU A CD2   1 
ATOM   4746 N  N     . PRO A 1 605 ? 5.476   23.897  4.019   1.00 57.25  ? 605 PRO A N     1 
ATOM   4747 C  CA    . PRO A 1 605 ? 4.616   25.057  3.761   1.00 60.50  ? 605 PRO A CA    1 
ATOM   4748 C  C     . PRO A 1 605 ? 4.746   26.087  4.874   1.00 55.41  ? 605 PRO A C     1 
ATOM   4749 O  O     . PRO A 1 605 ? 4.939   25.749  6.043   1.00 61.55  ? 605 PRO A O     1 
ATOM   4750 C  CB    . PRO A 1 605 ? 3.207   24.453  3.713   1.00 61.21  ? 605 PRO A CB    1 
ATOM   4751 C  CG    . PRO A 1 605 ? 3.421   22.984  3.469   1.00 53.39  ? 605 PRO A CG    1 
ATOM   4752 C  CD    . PRO A 1 605 ? 4.705   22.652  4.157   1.00 53.35  ? 605 PRO A CD    1 
ATOM   4753 N  N     . TYR A 1 606 ? 4.642   27.364  4.498   1.00 59.11  ? 606 TYR A N     1 
ATOM   4754 C  CA    . TYR A 1 606 ? 4.794   28.429  5.486   1.00 64.32  ? 606 TYR A CA    1 
ATOM   4755 C  C     . TYR A 1 606 ? 3.707   28.362  6.551   1.00 57.89  ? 606 TYR A C     1 
ATOM   4756 O  O     . TYR A 1 606 ? 3.971   28.610  7.733   1.00 58.53  ? 606 TYR A O     1 
ATOM   4757 C  CB    . TYR A 1 606 ? 4.783   29.795  4.803   1.00 62.69  ? 606 TYR A CB    1 
ATOM   4758 C  CG    . TYR A 1 606 ? 4.644   30.959  5.767   1.00 70.25  ? 606 TYR A CG    1 
ATOM   4759 C  CD1   . TYR A 1 606 ? 5.699   31.339  6.588   1.00 74.40  ? 606 TYR A CD1   1 
ATOM   4760 C  CD2   . TYR A 1 606 ? 3.460   31.678  5.853   1.00 65.40  ? 606 TYR A CD2   1 
ATOM   4761 C  CE1   . TYR A 1 606 ? 5.576   32.402  7.468   1.00 72.52  ? 606 TYR A CE1   1 
ATOM   4762 C  CE2   . TYR A 1 606 ? 3.328   32.742  6.727   1.00 70.29  ? 606 TYR A CE2   1 
ATOM   4763 C  CZ    . TYR A 1 606 ? 4.389   33.100  7.533   1.00 74.37  ? 606 TYR A CZ    1 
ATOM   4764 O  OH    . TYR A 1 606 ? 4.263   34.161  8.407   1.00 72.20  ? 606 TYR A OH    1 
ATOM   4765 N  N     . GLU A 1 607 ? 2.476   28.033  6.154   1.00 55.63  ? 607 GLU A N     1 
ATOM   4766 C  CA    . GLU A 1 607 ? 1.389   27.972  7.124   1.00 58.07  ? 607 GLU A CA    1 
ATOM   4767 C  C     . GLU A 1 607 ? 1.678   26.970  8.235   1.00 60.47  ? 607 GLU A C     1 
ATOM   4768 O  O     . GLU A 1 607 ? 1.259   27.179  9.379   1.00 59.28  ? 607 GLU A O     1 
ATOM   4769 C  CB    . GLU A 1 607 ? 0.076   27.636  6.419   1.00 59.49  ? 607 GLU A CB    1 
ATOM   4770 C  CG    . GLU A 1 607 ? -0.425  28.759  5.527   1.00 62.85  ? 607 GLU A CG    1 
ATOM   4771 C  CD    . GLU A 1 607 ? -1.842  28.539  5.043   1.00 63.63  ? 607 GLU A CD    1 
ATOM   4772 O  OE1   . GLU A 1 607 ? -2.259  27.370  4.931   1.00 64.08  ? 607 GLU A OE1   1 
ATOM   4773 O  OE2   . GLU A 1 607 ? -2.543  29.539  4.779   1.00 84.44  ? 607 GLU A OE2   1 
ATOM   4774 N  N     . ILE A 1 608 ? 2.391   25.884  7.929   1.00 56.17  ? 608 ILE A N     1 
ATOM   4775 C  CA    . ILE A 1 608 ? 2.817   24.972  8.986   1.00 56.83  ? 608 ILE A CA    1 
ATOM   4776 C  C     . ILE A 1 608 ? 3.872   25.635  9.861   1.00 55.00  ? 608 ILE A C     1 
ATOM   4777 O  O     . ILE A 1 608 ? 3.866   25.484  11.088  1.00 59.18  ? 608 ILE A O     1 
ATOM   4778 C  CB    . ILE A 1 608 ? 3.327   23.647  8.390   1.00 55.15  ? 608 ILE A CB    1 
ATOM   4779 C  CG1   . ILE A 1 608 ? 2.211   22.939  7.621   1.00 51.04  ? 608 ILE A CG1   1 
ATOM   4780 C  CG2   . ILE A 1 608 ? 3.861   22.744  9.490   1.00 53.04  ? 608 ILE A CG2   1 
ATOM   4781 C  CD1   . ILE A 1 608 ? 1.007   22.601  8.472   1.00 50.27  ? 608 ILE A CD1   1 
ATOM   4782 N  N     . GLU A 1 609 ? 4.792   26.382  9.248   1.00 54.38  ? 609 GLU A N     1 
ATOM   4783 C  CA    . GLU A 1 609 ? 5.787   27.111  10.028  1.00 60.70  ? 609 GLU A CA    1 
ATOM   4784 C  C     . GLU A 1 609 ? 5.144   28.195  10.883  1.00 59.65  ? 609 GLU A C     1 
ATOM   4785 O  O     . GLU A 1 609 ? 5.657   28.521  11.959  1.00 58.44  ? 609 GLU A O     1 
ATOM   4786 C  CB    . GLU A 1 609 ? 6.837   27.723  9.102   1.00 61.15  ? 609 GLU A CB    1 
ATOM   4787 C  CG    . GLU A 1 609 ? 7.853   28.603  9.812   1.00 63.97  ? 609 GLU A CG    1 
ATOM   4788 C  CD    . GLU A 1 609 ? 8.818   29.266  8.852   1.00 76.41  ? 609 GLU A CD    1 
ATOM   4789 O  OE1   . GLU A 1 609 ? 8.824   28.889  7.661   1.00 77.67  ? 609 GLU A OE1   1 
ATOM   4790 O  OE2   . GLU A 1 609 ? 9.566   30.168  9.286   1.00 79.47  ? 609 GLU A OE2   1 
ATOM   4791 N  N     . ARG A 1 610 ? 4.030   28.768  10.421  1.00 56.54  ? 610 ARG A N     1 
ATOM   4792 C  CA    . ARG A 1 610 ? 3.345   29.796  11.197  1.00 57.04  ? 610 ARG A CA    1 
ATOM   4793 C  C     . ARG A 1 610 ? 2.650   29.194  12.411  1.00 58.09  ? 610 ARG A C     1 
ATOM   4794 O  O     . ARG A 1 610 ? 2.684   29.771  13.505  1.00 57.16  ? 610 ARG A O     1 
ATOM   4795 C  CB    . ARG A 1 610 ? 2.346   30.536  10.309  1.00 63.96  ? 610 ARG A CB    1 
ATOM   4796 C  CG    . ARG A 1 610 ? 1.704   31.746  10.951  1.00 59.69  ? 610 ARG A CG    1 
ATOM   4797 C  CD    . ARG A 1 610 ? 0.914   32.541  9.925   1.00 59.47  ? 610 ARG A CD    1 
ATOM   4798 N  NE    . ARG A 1 610 ? -0.145  31.747  9.314   1.00 58.63  ? 610 ARG A NE    1 
ATOM   4799 C  CZ    . ARG A 1 610 ? -0.945  32.183  8.351   1.00 64.36  ? 610 ARG A CZ    1 
ATOM   4800 N  NH1   . ARG A 1 610 ? -0.836  33.408  7.863   1.00 75.00  ? 610 ARG A NH1   1 
ATOM   4801 N  NH2   . ARG A 1 610 ? -1.878  31.369  7.863   1.00 57.88  ? 610 ARG A NH2   1 
ATOM   4802 N  N     . GLU A 1 611 ? 2.014   28.031  12.237  1.00 61.31  ? 611 GLU A N     1 
ATOM   4803 C  CA    . GLU A 1 611 ? 1.426   27.326  13.372  1.00 54.16  ? 611 GLU A CA    1 
ATOM   4804 C  C     . GLU A 1 611 ? 2.494   26.954  14.390  1.00 54.54  ? 611 GLU A C     1 
ATOM   4805 O  O     . GLU A 1 611 ? 2.318   27.159  15.597  1.00 59.96  ? 611 GLU A O     1 
ATOM   4806 C  CB    . GLU A 1 611 ? 0.682   26.082  12.887  1.00 52.72  ? 611 GLU A CB    1 
ATOM   4807 C  CG    . GLU A 1 611 ? -0.498  26.389  11.984  1.00 52.52  ? 611 GLU A CG    1 
ATOM   4808 C  CD    . GLU A 1 611 ? -1.516  27.295  12.652  1.00 59.42  ? 611 GLU A CD    1 
ATOM   4809 O  OE1   . GLU A 1 611 ? -1.536  27.354  13.901  1.00 54.73  ? 611 GLU A OE1   1 
ATOM   4810 O  OE2   . GLU A 1 611 ? -2.295  27.950  11.928  1.00 63.27  ? 611 GLU A OE2   1 
ATOM   4811 N  N     . LEU A 1 612 ? 3.614   26.403  13.920  1.00 54.38  ? 612 LEU A N     1 
ATOM   4812 C  CA    . LEU A 1 612 ? 4.740   26.142  14.810  1.00 55.30  ? 612 LEU A CA    1 
ATOM   4813 C  C     . LEU A 1 612 ? 5.147   27.408  15.557  1.00 62.30  ? 612 LEU A C     1 
ATOM   4814 O  O     . LEU A 1 612 ? 5.353   27.386  16.776  1.00 61.33  ? 612 LEU A O     1 
ATOM   4815 C  CB    . LEU A 1 612 ? 5.916   25.578  14.010  1.00 54.96  ? 612 LEU A CB    1 
ATOM   4816 C  CG    . LEU A 1 612 ? 7.222   25.375  14.779  1.00 57.60  ? 612 LEU A CG    1 
ATOM   4817 C  CD1   . LEU A 1 612 ? 6.980   24.530  16.013  1.00 59.93  ? 612 LEU A CD1   1 
ATOM   4818 C  CD2   . LEU A 1 612 ? 8.273   24.736  13.885  1.00 65.23  ? 612 LEU A CD2   1 
ATOM   4819 N  N     . ARG A 1 613 ? 5.258   28.528  14.836  1.00 57.57  ? 613 ARG A N     1 
ATOM   4820 C  CA    . ARG A 1 613 ? 5.596   29.793  15.479  1.00 59.41  ? 613 ARG A CA    1 
ATOM   4821 C  C     . ARG A 1 613 ? 4.530   30.194  16.489  1.00 59.80  ? 613 ARG A C     1 
ATOM   4822 O  O     . ARG A 1 613 ? 4.844   30.577  17.621  1.00 61.13  ? 613 ARG A O     1 
ATOM   4823 C  CB    . ARG A 1 613 ? 5.770   30.894  14.431  1.00 62.76  ? 613 ARG A CB    1 
ATOM   4824 C  CG    . ARG A 1 613 ? 7.007   30.766  13.562  1.00 62.82  ? 613 ARG A CG    1 
ATOM   4825 C  CD    . ARG A 1 613 ? 7.254   32.060  12.800  1.00 67.37  ? 613 ARG A CD    1 
ATOM   4826 N  NE    . ARG A 1 613 ? 8.353   31.946  11.850  1.00 67.24  ? 613 ARG A NE    1 
ATOM   4827 C  CZ    . ARG A 1 613 ? 8.936   32.978  11.256  1.00 76.17  ? 613 ARG A CZ    1 
ATOM   4828 N  NH1   . ARG A 1 613 ? 8.564   34.223  11.511  1.00 67.50  ? 613 ARG A NH1   1 
ATOM   4829 N  NH2   . ARG A 1 613 ? 9.918   32.757  10.386  1.00 77.72  ? 613 ARG A NH2   1 
ATOM   4830 N  N     . ALA A 1 614 ? 3.258   30.119  16.089  1.00 58.87  ? 614 ALA A N     1 
ATOM   4831 C  CA    . ALA A 1 614 ? 2.178   30.529  16.980  1.00 63.33  ? 614 ALA A CA    1 
ATOM   4832 C  C     . ALA A 1 614 ? 2.138   29.668  18.237  1.00 60.57  ? 614 ALA A C     1 
ATOM   4833 O  O     . ALA A 1 614 ? 1.987   30.187  19.349  1.00 66.36  ? 614 ALA A O     1 
ATOM   4834 C  CB    . ALA A 1 614 ? 0.839   30.473  16.243  1.00 58.43  ? 614 ALA A CB    1 
ATOM   4835 N  N     . LEU A 1 615 ? 2.275   28.348  18.083  1.00 58.42  ? 615 LEU A N     1 
ATOM   4836 C  CA    . LEU A 1 615 ? 2.261   27.469  19.248  1.00 60.40  ? 615 LEU A CA    1 
ATOM   4837 C  C     . LEU A 1 615 ? 3.432   27.762  20.176  1.00 66.46  ? 615 LEU A C     1 
ATOM   4838 O  O     . LEU A 1 615 ? 3.264   27.821  21.400  1.00 66.26  ? 615 LEU A O     1 
ATOM   4839 C  CB    . LEU A 1 615 ? 2.282   26.006  18.808  1.00 62.90  ? 615 LEU A CB    1 
ATOM   4840 C  CG    . LEU A 1 615 ? 2.462   24.973  19.926  1.00 59.38  ? 615 LEU A CG    1 
ATOM   4841 C  CD1   . LEU A 1 615 ? 1.389   25.132  20.986  1.00 62.09  ? 615 LEU A CD1   1 
ATOM   4842 C  CD2   . LEU A 1 615 ? 2.443   23.567  19.362  1.00 54.88  ? 615 LEU A CD2   1 
ATOM   4843 N  N     . LYS A 1 616 ? 4.629   27.944  19.614  1.00 66.62  ? 616 LYS A N     1 
ATOM   4844 C  CA    . LYS A 1 616 ? 5.776   28.301  20.442  1.00 66.21  ? 616 LYS A CA    1 
ATOM   4845 C  C     . LYS A 1 616 ? 5.503   29.578  21.225  1.00 67.82  ? 616 LYS A C     1 
ATOM   4846 O  O     . LYS A 1 616 ? 5.925   29.710  22.381  1.00 68.52  ? 616 LYS A O     1 
ATOM   4847 C  CB    . LYS A 1 616 ? 7.025   28.455  19.576  1.00 67.55  ? 616 LYS A CB    1 
ATOM   4848 C  CG    . LYS A 1 616 ? 8.253   28.916  20.347  1.00 74.85  ? 616 LYS A CG    1 
ATOM   4849 C  CD    . LYS A 1 616 ? 9.429   29.172  19.417  1.00 91.68  ? 616 LYS A CD    1 
ATOM   4850 C  CE    . LYS A 1 616 ? 10.574  29.862  20.146  1.00 106.36 ? 616 LYS A CE    1 
ATOM   4851 N  NZ    . LYS A 1 616 ? 11.633  30.340  19.211  1.00 98.49  ? 616 LYS A NZ    1 
ATOM   4852 N  N     . GLN A 1 617 ? 4.784   30.523  20.616  1.00 69.71  ? 617 GLN A N     1 
ATOM   4853 C  CA    . GLN A 1 617 ? 4.491   31.787  21.285  1.00 67.56  ? 617 GLN A CA    1 
ATOM   4854 C  C     . GLN A 1 617 ? 3.499   31.588  22.425  1.00 68.64  ? 617 GLN A C     1 
ATOM   4855 O  O     . GLN A 1 617 ? 3.736   32.037  23.553  1.00 68.21  ? 617 GLN A O     1 
ATOM   4856 C  CB    . GLN A 1 617 ? 3.955   32.800  20.271  1.00 65.58  ? 617 GLN A CB    1 
ATOM   4857 C  CG    . GLN A 1 617 ? 3.823   34.218  20.809  1.00 71.81  ? 617 GLN A CG    1 
ATOM   4858 C  CD    . GLN A 1 617 ? 5.168   34.875  21.041  1.00 69.93  ? 617 GLN A CD    1 
ATOM   4859 O  OE1   . GLN A 1 617 ? 6.189   34.418  20.529  1.00 83.81  ? 617 GLN A OE1   1 
ATOM   4860 N  NE2   . GLN A 1 617 ? 5.176   35.950  21.818  1.00 72.58  ? 617 GLN A NE2   1 
ATOM   4861 N  N     . ARG A 1 618 ? 2.379   30.914  22.152  1.00 64.95  ? 618 ARG A N     1 
ATOM   4862 C  CA    . ARG A 1 618 ? 1.376   30.707  23.190  1.00 64.87  ? 618 ARG A CA    1 
ATOM   4863 C  C     . ARG A 1 618 ? 1.941   29.929  24.369  1.00 65.70  ? 618 ARG A C     1 
ATOM   4864 O  O     . ARG A 1 618 ? 1.490   30.113  25.505  1.00 74.26  ? 618 ARG A O     1 
ATOM   4865 C  CB    . ARG A 1 618 ? 0.156   29.989  22.613  1.00 62.96  ? 618 ARG A CB    1 
ATOM   4866 C  CG    . ARG A 1 618 ? -0.546  30.753  21.503  1.00 62.46  ? 618 ARG A CG    1 
ATOM   4867 C  CD    . ARG A 1 618 ? -1.859  30.094  21.117  1.00 61.03  ? 618 ARG A CD    1 
ATOM   4868 N  NE    . ARG A 1 618 ? -1.681  28.692  20.763  1.00 60.84  ? 618 ARG A NE    1 
ATOM   4869 C  CZ    . ARG A 1 618 ? -1.458  28.246  19.533  1.00 68.27  ? 618 ARG A CZ    1 
ATOM   4870 N  NH1   . ARG A 1 618 ? -1.388  29.070  18.499  1.00 65.77  ? 618 ARG A NH1   1 
ATOM   4871 N  NH2   . ARG A 1 618 ? -1.303  26.940  19.335  1.00 60.05  ? 618 ARG A NH2   1 
ATOM   4872 N  N     . ILE A 1 619 ? 2.927   29.066  24.127  1.00 66.43  ? 619 ILE A N     1 
ATOM   4873 C  CA    . ILE A 1 619 ? 3.510   28.293  25.218  1.00 72.99  ? 619 ILE A CA    1 
ATOM   4874 C  C     . ILE A 1 619 ? 4.438   29.160  26.059  1.00 73.06  ? 619 ILE A C     1 
ATOM   4875 O  O     . ILE A 1 619 ? 4.492   29.020  27.286  1.00 75.08  ? 619 ILE A O     1 
ATOM   4876 C  CB    . ILE A 1 619 ? 4.236   27.051  24.668  1.00 68.63  ? 619 ILE A CB    1 
ATOM   4877 C  CG1   . ILE A 1 619 ? 3.228   26.067  24.070  1.00 64.73  ? 619 ILE A CG1   1 
ATOM   4878 C  CG2   . ILE A 1 619 ? 5.057   26.382  25.764  1.00 70.58  ? 619 ILE A CG2   1 
ATOM   4879 C  CD1   . ILE A 1 619 ? 3.856   24.793  23.549  1.00 67.63  ? 619 ILE A CD1   1 
ATOM   4880 N  N     . SER A 1 620 ? 5.181   30.068  25.423  1.00 71.66  ? 620 SER A N     1 
ATOM   4881 C  CA    . SER A 1 620 ? 6.077   30.941  26.170  1.00 75.21  ? 620 SER A CA    1 
ATOM   4882 C  C     . SER A 1 620 ? 5.321   31.954  27.021  1.00 75.94  ? 620 SER A C     1 
ATOM   4883 O  O     . SER A 1 620 ? 5.906   32.532  27.944  1.00 76.26  ? 620 SER A O     1 
ATOM   4884 C  CB    . SER A 1 620 ? 7.026   31.665  25.214  1.00 73.11  ? 620 SER A CB    1 
ATOM   4885 O  OG    . SER A 1 620 ? 6.308   32.457  24.286  1.00 78.84  ? 620 SER A OG    1 
ATOM   4886 N  N     . GLN A 1 621 ? 4.042   32.181  26.738  1.00 75.35  ? 621 GLN A N     1 
ATOM   4887 C  CA    . GLN A 1 621 ? 3.226   33.099  27.519  1.00 77.55  ? 621 GLN A CA    1 
ATOM   4888 C  C     . GLN A 1 621 ? 2.600   32.440  28.740  1.00 82.79  ? 621 GLN A C     1 
ATOM   4889 O  O     . GLN A 1 621 ? 1.872   33.107  29.483  1.00 86.54  ? 621 GLN A O     1 
ATOM   4890 C  CB    . GLN A 1 621 ? 2.130   33.705  26.639  1.00 80.58  ? 621 GLN A CB    1 
ATOM   4891 C  CG    . GLN A 1 621 ? 2.665   34.496  25.455  1.00 77.90  ? 621 GLN A CG    1 
ATOM   4892 C  CD    . GLN A 1 621 ? 3.535   35.664  25.879  1.00 88.96  ? 621 GLN A CD    1 
ATOM   4893 O  OE1   . GLN A 1 621 ? 3.224   36.373  26.839  1.00 90.23  ? 621 GLN A OE1   1 
ATOM   4894 N  NE2   . GLN A 1 621 ? 4.635   35.870  25.164  1.00 92.00  ? 621 GLN A NE2   1 
ATOM   4895 N  N     . MET A 1 622 ? 2.862   31.157  28.965  1.00 81.58  ? 622 MET A N     1 
ATOM   4896 C  CA    . MET A 1 622 ? 2.337   30.460  30.131  1.00 85.18  ? 622 MET A CA    1 
ATOM   4897 C  C     . MET A 1 622 ? 3.041   30.923  31.399  1.00 88.49  ? 622 MET A C     1 
ATOM   4898 O  O     . MET A 1 622 ? 4.209   31.311  31.365  1.00 87.85  ? 622 MET A O     1 
ATOM   4899 C  CB    . MET A 1 622 ? 2.489   28.947  29.966  1.00 80.82  ? 622 MET A CB    1 
ATOM   4900 C  CG    . MET A 1 622 ? 1.722   28.372  28.790  1.00 71.94  ? 622 MET A CG    1 
ATOM   4901 S  SD    . MET A 1 622 ? 1.854   26.580  28.690  1.00 76.13  ? 622 MET A SD    1 
ATOM   4902 C  CE    . MET A 1 622 ? 1.158   26.089  30.266  1.00 78.80  ? 622 MET A CE    1 
ATOM   4903 O  OXT   . MET A 1 622 ? 2.461   30.919  32.485  1.00 97.47  ? 622 MET A OXT   1 
HETATM 4904 MN MN    . MN  B 2 .   ? -2.162  -0.064  9.364   1.00 61.90  ? 701 MN  A MN    1 
HETATM 4905 MN MN    . MN  C 2 .   ? -5.404  -3.143  12.814  1.00 76.07  ? 702 MN  A MN    1 
HETATM 4906 MN MN    . MN  D 2 .   ? -3.917  28.474  3.214   1.00 106.41 ? 703 MN  A MN    1 
HETATM 4907 P  P     A PGA E 3 .   ? -2.690  -1.623  11.670  0.16 57.69  ? 704 PGA A P     1 
HETATM 4908 P  P     B PGA E 3 .   ? -0.473  -2.842  10.119  0.55 61.12  ? 704 PGA A P     1 
HETATM 4909 P  P     C PGA E 3 .   ? 0.637   -2.985  10.238  0.29 61.92  ? 704 PGA A P     1 
HETATM 4910 O  O1P   A PGA E 3 .   ? -1.790  -2.021  10.398  0.16 59.58  ? 704 PGA A O1P   1 
HETATM 4911 O  O1P   B PGA E 3 .   ? 0.513   -3.935  9.470   0.55 61.97  ? 704 PGA A O1P   1 
HETATM 4912 O  O1P   C PGA E 3 .   ? 1.011   -4.464  9.729   0.29 62.38  ? 704 PGA A O1P   1 
HETATM 4913 O  O2P   A PGA E 3 .   ? -1.905  -0.623  12.486  0.16 57.23  ? 704 PGA A O2P   1 
HETATM 4914 O  O2P   B PGA E 3 .   ? -0.568  -3.077  11.609  0.55 59.72  ? 704 PGA A O2P   1 
HETATM 4915 O  O2P   C PGA E 3 .   ? -0.866  -2.860  10.333  0.29 58.97  ? 704 PGA A O2P   1 
HETATM 4916 O  O3P   A PGA E 3 .   ? -2.966  -2.858  12.493  0.16 59.07  ? 704 PGA A O3P   1 
HETATM 4917 O  O3P   B PGA E 3 .   ? -1.837  -2.952  9.480   0.55 57.37  ? 704 PGA A O3P   1 
HETATM 4918 O  O3P   C PGA E 3 .   ? 1.192   -1.954  9.285   0.29 62.24  ? 704 PGA A O3P   1 
HETATM 4919 O  O4P   A PGA E 3 .   ? -3.993  -1.001  11.230  0.16 55.70  ? 704 PGA A O4P   1 
HETATM 4920 O  O4P   B PGA E 3 .   ? 0.094   -1.466  9.857   0.55 61.62  ? 704 PGA A O4P   1 
HETATM 4921 O  O4P   C PGA E 3 .   ? 1.253   -2.786  11.602  0.29 61.54  ? 704 PGA A O4P   1 
HETATM 4922 C  C2    A PGA E 3 .   ? -0.760  -2.973  10.552  0.16 62.24  ? 704 PGA A C2    1 
HETATM 4923 C  C2    B PGA E 3 .   ? 0.022   -4.943  8.615   0.55 59.67  ? 704 PGA A C2    1 
HETATM 4924 C  C2    C PGA E 3 .   ? 2.014   -4.673  8.760   0.29 63.38  ? 704 PGA A C2    1 
HETATM 4925 C  C1    A PGA E 3 .   ? 0.476   -2.514  9.815   0.16 61.85  ? 704 PGA A C1    1 
HETATM 4926 C  C1    B PGA E 3 .   ? 1.188   -5.555  7.876   0.55 61.57  ? 704 PGA A C1    1 
HETATM 4927 C  C1    C PGA E 3 .   ? 2.259   -6.158  8.637   0.29 64.05  ? 704 PGA A C1    1 
HETATM 4928 O  O1    A PGA E 3 .   ? 0.516   -1.379  9.292   0.16 60.65  ? 704 PGA A O1    1 
HETATM 4929 O  O1    B PGA E 3 .   ? 1.497   -6.755  8.051   0.55 64.93  ? 704 PGA A O1    1 
HETATM 4930 O  O1    C PGA E 3 .   ? 3.168   -6.709  9.296   0.29 64.07  ? 704 PGA A O1    1 
HETATM 4931 O  O2    A PGA E 3 .   ? 1.476   -3.260  9.733   0.16 63.33  ? 704 PGA A O2    1 
HETATM 4932 O  O2    B PGA E 3 .   ? 1.854   -4.859  7.080   0.55 61.70  ? 704 PGA A O2    1 
HETATM 4933 O  O2    C PGA E 3 .   ? 1.551   -6.854  7.878   0.29 64.91  ? 704 PGA A O2    1 
HETATM 4934 H  H21   A PGA E 3 .   ? -1.087  -3.936  10.160  0.16 74.81  ? 704 PGA A H21   1 
HETATM 4935 H  H21   B PGA E 3 .   ? -0.689  -4.519  7.906   0.55 71.73  ? 704 PGA A H21   1 
HETATM 4936 H  H21   C PGA E 3 .   ? 2.932   -4.165  9.055   0.29 76.18  ? 704 PGA A H21   1 
HETATM 4937 H  H22   A PGA E 3 .   ? -0.532  -3.101  11.610  0.16 74.81  ? 704 PGA A H22   1 
HETATM 4938 H  H22   B PGA E 3 .   ? -0.497  -5.706  9.194   0.55 71.73  ? 704 PGA A H22   1 
HETATM 4939 H  H22   C PGA E 3 .   ? 1.698   -4.265  7.800   0.29 76.18  ? 704 PGA A H22   1 
HETATM 4940 P  PB    . GDP F 4 .   ? -4.251  -0.925  15.328  1.00 63.56  ? 705 GDP A PB    1 
HETATM 4941 O  O1B   . GDP F 4 .   ? -4.288  0.561   15.059  1.00 62.63  ? 705 GDP A O1B   1 
HETATM 4942 O  O2B   . GDP F 4 .   ? -3.026  -1.529  14.686  1.00 58.54  ? 705 GDP A O2B   1 
HETATM 4943 O  O3B   . GDP F 4 .   ? -5.497  -1.551  14.754  1.00 58.44  ? 705 GDP A O3B   1 
HETATM 4944 O  O3A   . GDP F 4 .   ? -4.152  -1.163  16.920  1.00 62.22  ? 705 GDP A O3A   1 
HETATM 4945 P  PA    . GDP F 4 .   ? -5.071  -2.225  17.716  1.00 56.81  ? 705 GDP A PA    1 
HETATM 4946 O  O1A   . GDP F 4 .   ? -6.514  -1.784  17.790  1.00 49.77  ? 705 GDP A O1A   1 
HETATM 4947 O  O2A   . GDP F 4 .   ? -4.981  -3.597  17.091  1.00 71.15  ? 705 GDP A O2A   1 
HETATM 4948 O  "O5'" . GDP F 4 .   ? -4.361  -2.229  19.160  1.00 55.30  ? 705 GDP A "O5'" 1 
HETATM 4949 C  "C5'" . GDP F 4 .   ? -3.137  -2.945  19.322  1.00 61.48  ? 705 GDP A "C5'" 1 
HETATM 4950 C  "C4'" . GDP F 4 .   ? -2.797  -3.065  20.800  1.00 67.72  ? 705 GDP A "C4'" 1 
HETATM 4951 O  "O4'" . GDP F 4 .   ? -3.089  -1.828  21.450  1.00 69.51  ? 705 GDP A "O4'" 1 
HETATM 4952 C  "C3'" . GDP F 4 .   ? -3.625  -4.147  21.476  1.00 69.13  ? 705 GDP A "C3'" 1 
HETATM 4953 O  "O3'" . GDP F 4 .   ? -2.774  -5.220  21.890  1.00 77.92  ? 705 GDP A "O3'" 1 
HETATM 4954 C  "C2'" . GDP F 4 .   ? -4.266  -3.491  22.683  1.00 70.06  ? 705 GDP A "C2'" 1 
HETATM 4955 O  "O2'" . GDP F 4 .   ? -3.868  -4.163  23.884  1.00 68.52  ? 705 GDP A "O2'" 1 
HETATM 4956 C  "C1'" . GDP F 4 .   ? -3.776  -2.049  22.683  1.00 65.40  ? 705 GDP A "C1'" 1 
HETATM 4957 N  N9    . GDP F 4 .   ? -4.939  -1.133  22.781  1.00 64.49  ? 705 GDP A N9    1 
HETATM 4958 C  C8    . GDP F 4 .   ? -5.931  -1.014  21.876  1.00 64.34  ? 705 GDP A C8    1 
HETATM 4959 N  N7    . GDP F 4 .   ? -6.843  -0.087  22.268  1.00 60.26  ? 705 GDP A N7    1 
HETATM 4960 C  C5    . GDP F 4 .   ? -6.429  0.409   23.450  1.00 56.69  ? 705 GDP A C5    1 
HETATM 4961 C  C6    . GDP F 4 .   ? -6.918  1.418   24.418  1.00 55.37  ? 705 GDP A C6    1 
HETATM 4962 O  O6    . GDP F 4 .   ? -7.978  2.048   24.206  1.00 54.09  ? 705 GDP A O6    1 
HETATM 4963 N  N1    . GDP F 4 .   ? -6.190  1.631   25.523  1.00 54.63  ? 705 GDP A N1    1 
HETATM 4964 C  C2    . GDP F 4 .   ? -5.044  0.964   25.773  1.00 52.71  ? 705 GDP A C2    1 
HETATM 4965 N  N2    . GDP F 4 .   ? -4.358  1.232   26.911  1.00 53.24  ? 705 GDP A N2    1 
HETATM 4966 N  N3    . GDP F 4 .   ? -4.541  0.030   24.931  1.00 57.56  ? 705 GDP A N3    1 
HETATM 4967 C  C4    . GDP F 4 .   ? -5.175  -0.283  23.780  1.00 57.88  ? 705 GDP A C4    1 
HETATM 4968 O  O     . HOH G 5 .   ? -2.545  -3.000  9.423   0.55 56.25  ? 801 HOH A O     1 
HETATM 4969 O  O     . HOH G 5 .   ? -2.261  -0.185  11.746  0.55 52.91  ? 802 HOH A O     1 
HETATM 4970 O  O     . HOH G 5 .   ? -0.125  -0.077  9.945   0.55 54.28  ? 803 HOH A O     1 
HETATM 4971 O  O     . HOH G 5 .   ? -1.236  22.992  19.060  1.00 53.77  ? 804 HOH A O     1 
HETATM 4972 O  O     . HOH G 5 .   ? 4.038   3.900   18.195  1.00 68.88  ? 805 HOH A O     1 
HETATM 4973 O  O     . HOH G 5 .   ? -10.783 -13.517 25.434  1.00 75.19  ? 806 HOH A O     1 
HETATM 4974 O  O     . HOH G 5 .   ? -3.315  6.646   29.983  1.00 71.23  ? 807 HOH A O     1 
HETATM 4975 O  O     . HOH G 5 .   ? -0.412  16.401  20.356  1.00 47.90  ? 808 HOH A O     1 
HETATM 4976 O  O     . HOH G 5 .   ? 8.642   16.607  24.693  1.00 67.76  ? 809 HOH A O     1 
HETATM 4977 O  O     . HOH G 5 .   ? 13.062  19.361  -0.632  1.00 65.22  ? 810 HOH A O     1 
HETATM 4978 O  O     . HOH G 5 .   ? -5.984  -1.249  12.539  1.00 58.60  ? 811 HOH A O     1 
HETATM 4979 O  O     . HOH G 5 .   ? -10.492 1.985   22.556  1.00 57.21  ? 812 HOH A O     1 
HETATM 4980 O  O     . HOH G 5 .   ? 6.999   6.515   3.839   1.00 58.18  ? 813 HOH A O     1 
HETATM 4981 O  O     . HOH G 5 .   ? -6.298  2.949   27.554  1.00 58.43  ? 814 HOH A O     1 
HETATM 4982 O  O     . HOH G 5 .   ? -15.027 -2.081  23.313  1.00 59.75  ? 815 HOH A O     1 
HETATM 4983 O  O     . HOH G 5 .   ? 2.739   13.381  20.522  1.00 42.60  ? 816 HOH A O     1 
HETATM 4984 O  O     . HOH G 5 .   ? 0.710   12.710  19.022  1.00 42.31  ? 817 HOH A O     1 
HETATM 4985 O  O     . HOH G 5 .   ? -4.300  9.275   28.437  1.00 60.48  ? 818 HOH A O     1 
HETATM 4986 O  O     . HOH G 5 .   ? 0.283   16.139  17.084  1.00 43.70  ? 819 HOH A O     1 
HETATM 4987 O  O     . HOH G 5 .   ? -16.284 2.111   2.674   1.00 56.16  ? 820 HOH A O     1 
HETATM 4988 O  O     . HOH G 5 .   ? -3.090  10.789  1.277   1.00 47.98  ? 821 HOH A O     1 
HETATM 4989 O  O     . HOH G 5 .   ? 4.490   16.082  19.483  1.00 40.70  ? 822 HOH A O     1 
HETATM 4990 O  O     . HOH G 5 .   ? -12.241 -25.111 10.838  1.00 62.97  ? 823 HOH A O     1 
HETATM 4991 O  O     . HOH G 5 .   ? -11.924 23.603  16.067  1.00 43.17  ? 824 HOH A O     1 
HETATM 4992 O  O     . HOH G 5 .   ? 0.739   -4.070  1.187   1.00 53.59  ? 825 HOH A O     1 
HETATM 4993 O  O     . HOH G 5 .   ? -3.965  -14.174 8.885   1.00 51.03  ? 826 HOH A O     1 
HETATM 4994 O  O     . HOH G 5 .   ? -18.917 18.428  23.837  1.00 60.08  ? 827 HOH A O     1 
HETATM 4995 O  O     . HOH G 5 .   ? 4.188   -12.516 13.491  1.00 68.85  ? 828 HOH A O     1 
HETATM 4996 O  O     . HOH G 5 .   ? -6.728  -4.529  -21.997 1.00 79.97  ? 829 HOH A O     1 
HETATM 4997 O  O     . HOH G 5 .   ? -10.630 -30.919 28.825  1.00 65.93  ? 830 HOH A O     1 
HETATM 4998 O  O     . HOH G 5 .   ? 11.918  -20.747 5.539   1.00 75.54  ? 831 HOH A O     1 
HETATM 4999 O  O     . HOH G 5 .   ? 1.015   35.165  8.195   1.00 62.98  ? 832 HOH A O     1 
HETATM 5000 O  O     . HOH G 5 .   ? 5.443   11.408  25.527  1.00 51.76  ? 833 HOH A O     1 
HETATM 5001 O  O     . HOH G 5 .   ? -4.739  -4.349  14.631  1.00 60.16  ? 834 HOH A O     1 
HETATM 5002 O  O     . HOH G 5 .   ? 9.238   -9.848  7.110   1.00 70.46  ? 835 HOH A O     1 
HETATM 5003 O  O     . HOH G 5 .   ? 7.882   5.946   -10.586 1.00 63.75  ? 836 HOH A O     1 
HETATM 5004 O  O     . HOH G 5 .   ? -9.000  -0.340  6.521   1.00 42.63  ? 837 HOH A O     1 
HETATM 5005 O  O     . HOH G 5 .   ? 8.574   -9.302  -0.361  1.00 61.04  ? 838 HOH A O     1 
HETATM 5006 O  O     . HOH G 5 .   ? -4.221  14.366  22.795  1.00 47.60  ? 839 HOH A O     1 
HETATM 5007 O  O     . HOH G 5 .   ? 9.558   -18.692 -5.708  1.00 51.17  ? 840 HOH A O     1 
HETATM 5008 O  O     . HOH G 5 .   ? -16.516 25.917  24.482  1.00 66.43  ? 841 HOH A O     1 
HETATM 5009 O  O     . HOH G 5 .   ? 11.112  9.693   14.397  1.00 65.92  ? 842 HOH A O     1 
HETATM 5010 O  O     . HOH G 5 .   ? -10.800 -2.714  7.331   1.00 56.32  ? 843 HOH A O     1 
HETATM 5011 O  O     . HOH G 5 .   ? -10.494 16.362  -1.863  1.00 66.14  ? 844 HOH A O     1 
HETATM 5012 O  O     . HOH G 5 .   ? 3.202   -30.962 -15.323 1.00 58.48  ? 845 HOH A O     1 
HETATM 5013 O  O     . HOH G 5 .   ? 6.044   34.509  10.688  1.00 63.78  ? 846 HOH A O     1 
HETATM 5014 O  O     . HOH G 5 .   ? 6.025   14.599  13.688  1.00 39.88  ? 847 HOH A O     1 
HETATM 5015 O  O     . HOH G 5 .   ? -1.054  29.023  9.787   1.00 56.76  ? 848 HOH A O     1 
HETATM 5016 O  O     . HOH G 5 .   ? -0.412  26.787  16.299  1.00 53.54  ? 849 HOH A O     1 
HETATM 5017 O  O     . HOH G 5 .   ? 7.819   11.902  1.557   1.00 51.65  ? 850 HOH A O     1 
HETATM 5018 O  O     . HOH G 5 .   ? -18.233 12.494  27.934  1.00 61.70  ? 851 HOH A O     1 
HETATM 5019 O  O     . HOH G 5 .   ? 2.107   18.185  29.826  1.00 70.00  ? 852 HOH A O     1 
HETATM 5020 O  O     . HOH G 5 .   ? -11.453 -17.929 -4.666  1.00 48.48  ? 853 HOH A O     1 
HETATM 5021 O  O     . HOH G 5 .   ? -7.763  0.920   -11.505 1.00 65.95  ? 854 HOH A O     1 
HETATM 5022 O  O     . HOH G 5 .   ? -7.407  -4.056  7.927   1.00 54.79  ? 855 HOH A O     1 
HETATM 5023 O  O     . HOH G 5 .   ? 7.720   1.616   4.766   1.00 59.47  ? 856 HOH A O     1 
HETATM 5024 O  O     . HOH G 5 .   ? -3.963  7.432   21.804  1.00 51.78  ? 857 HOH A O     1 
HETATM 5025 O  O     . HOH G 5 .   ? -13.243 -11.975 -2.503  1.00 57.56  ? 858 HOH A O     1 
HETATM 5026 O  O     . HOH G 5 .   ? 16.619  15.460  19.568  1.00 59.85  ? 859 HOH A O     1 
HETATM 5027 O  O     . HOH G 5 .   ? -3.571  9.312   7.575   1.00 44.10  ? 860 HOH A O     1 
HETATM 5028 O  O     . HOH G 5 .   ? -1.286  10.632  21.622  1.00 51.51  ? 861 HOH A O     1 
HETATM 5029 O  O     . HOH G 5 .   ? 2.257   4.183   11.350  1.00 55.83  ? 862 HOH A O     1 
HETATM 5030 O  O     . HOH G 5 .   ? -2.225  12.292  -1.110  1.00 53.46  ? 863 HOH A O     1 
HETATM 5031 O  O     . HOH G 5 .   ? 1.015   -12.385 7.044   1.00 59.50  ? 864 HOH A O     1 
HETATM 5032 O  O     . HOH G 5 .   ? 9.534   -3.013  -14.700 1.00 70.49  ? 865 HOH A O     1 
HETATM 5033 O  O     . HOH G 5 .   ? 12.623  26.153  11.683  1.00 80.76  ? 866 HOH A O     1 
HETATM 5034 O  O     . HOH G 5 .   ? -10.512 -17.968 -14.254 1.00 49.47  ? 867 HOH A O     1 
HETATM 5035 O  O     . HOH G 5 .   ? -4.715  -3.471  9.157   1.00 55.99  ? 868 HOH A O     1 
HETATM 5036 O  O     . HOH G 5 .   ? 14.052  20.623  1.053   1.00 64.93  ? 869 HOH A O     1 
HETATM 5037 O  O     . HOH G 5 .   ? -16.452 -8.873  3.668   1.00 56.29  ? 870 HOH A O     1 
HETATM 5038 O  O     . HOH G 5 .   ? 4.690   -2.592  2.562   1.00 56.34  ? 871 HOH A O     1 
HETATM 5039 O  O     . HOH G 5 .   ? 6.896   -3.034  3.880   1.00 60.57  ? 872 HOH A O     1 
HETATM 5040 O  O     . HOH G 5 .   ? 6.975   -0.529  5.438   1.00 65.35  ? 873 HOH A O     1 
HETATM 5041 O  O     . HOH G 5 .   ? -10.022 27.024  10.225  1.00 57.93  ? 874 HOH A O     1 
HETATM 5042 O  O     . HOH G 5 .   ? -3.845  -13.662 6.288   1.00 57.64  ? 875 HOH A O     1 
HETATM 5043 O  O     . HOH G 5 .   ? -15.152 -26.412 8.319   1.00 63.44  ? 876 HOH A O     1 
HETATM 5044 O  O     . HOH G 5 .   ? -7.044  -6.325  16.005  1.00 57.92  ? 877 HOH A O     1 
HETATM 5045 O  O     . HOH G 5 .   ? -4.358  6.390   19.330  1.00 53.68  ? 878 HOH A O     1 
HETATM 5046 O  O     . HOH G 5 .   ? -10.411 21.821  14.270  1.00 49.10  ? 879 HOH A O     1 
HETATM 5047 O  O     . HOH G 5 .   ? -11.172 22.567  12.345  1.00 50.57  ? 880 HOH A O     1 
HETATM 5048 O  O     . HOH G 5 .   ? 7.723   11.778  26.773  1.00 62.34  ? 881 HOH A O     1 
HETATM 5049 O  O     . HOH G 5 .   ? 4.723   -5.007  -17.641 1.00 51.71  ? 882 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . PRO A 3   ? 2.5750 1.7712 1.4796 -0.1654 0.3401  -0.0649 3   PRO A N   
2    C CA  . PRO A 3   ? 2.4365 1.6261 1.3275 -0.1758 0.3678  -0.0871 3   PRO A CA  
3    C C   . PRO A 3   ? 2.3797 1.6067 1.3461 -0.1655 0.4057  -0.0994 3   PRO A C   
4    O O   . PRO A 3   ? 2.3663 1.6203 1.3823 -0.1558 0.4133  -0.0885 3   PRO A O   
5    C CB  . PRO A 3   ? 2.5050 1.6644 1.3305 -0.1958 0.3657  -0.0778 3   PRO A CB  
6    C CG  . PRO A 3   ? 2.4808 1.6452 1.3171 -0.1924 0.3568  -0.0533 3   PRO A CG  
7    C CD  . PRO A 3   ? 2.5338 1.7102 1.3977 -0.1753 0.3312  -0.0427 3   PRO A CD  
8    N N   . GLN A 4   ? 2.0221 1.2507 0.9976 -0.1674 0.4274  -0.1217 4   GLN A N   
9    C CA  . GLN A 4   ? 1.8583 1.1219 0.9045 -0.1565 0.4605  -0.1340 4   GLN A CA  
10   C C   . GLN A 4   ? 1.7521 1.0038 0.7790 -0.1665 0.4832  -0.1554 4   GLN A C   
11   O O   . GLN A 4   ? 1.8185 1.0370 0.7848 -0.1794 0.4722  -0.1627 4   GLN A O   
12   C CB  . GLN A 4   ? 1.8161 1.1072 0.9316 -0.1333 0.4589  -0.1383 4   GLN A CB  
13   C CG  . GLN A 4   ? 1.8364 1.1089 0.9375 -0.1303 0.4458  -0.1520 4   GLN A CG  
14   C CD  . GLN A 4   ? 1.8725 1.1685 1.0409 -0.1081 0.4435  -0.1543 4   GLN A CD  
15   O OE1 . GLN A 4   ? 1.8476 1.1759 1.0754 -0.0938 0.4525  -0.1463 4   GLN A OE1 
16   N NE2 . GLN A 4   ? 1.7738 1.0528 0.9329 -0.1063 0.4305  -0.1655 4   GLN A NE2 
17   N N   . LEU A 5   ? 1.7406 1.0209 0.8203 -0.1605 0.5142  -0.1660 5   LEU A N   
18   C CA  . LEU A 5   ? 1.7581 1.0320 0.8303 -0.1671 0.5398  -0.1877 5   LEU A CA  
19   C C   . LEU A 5   ? 1.6678 0.9568 0.7935 -0.1482 0.5486  -0.2051 5   LEU A C   
20   O O   . LEU A 5   ? 1.7143 0.9897 0.8253 -0.1530 0.5643  -0.2241 5   LEU A O   
21   C CB  . LEU A 5   ? 1.7121 1.0066 0.8055 -0.1738 0.5696  -0.1907 5   LEU A CB  
22   C CG  . LEU A 5   ? 1.7673 1.0375 0.7971 -0.1973 0.5674  -0.1778 5   LEU A CG  
23   C CD1 . LEU A 5   ? 1.7762 1.0709 0.8364 -0.2037 0.5992  -0.1830 5   LEU A CD1 
24   C CD2 . LEU A 5   ? 1.8530 1.0761 0.7963 -0.2170 0.5600  -0.1837 5   LEU A CD2 
25   N N   . HIS A 6   ? 1.6993 1.0134 0.8849 -0.1272 0.5389  -0.1986 6   HIS A N   
26   C CA  . HIS A 6   ? 1.8563 1.1809 1.0923 -0.1080 0.5440  -0.2123 6   HIS A CA  
27   C C   . HIS A 6   ? 1.9837 1.3023 1.2281 -0.0975 0.5166  -0.2037 6   HIS A C   
28   O O   . HIS A 6   ? 1.9799 1.2702 1.1678 -0.1100 0.4944  -0.1989 6   HIS A O   
29   C CB  . HIS A 6   ? 1.7503 1.1180 1.0662 -0.0897 0.5652  -0.2158 6   HIS A CB  
30   C CG  . HIS A 6   ? 1.6866 1.0643 1.0005 -0.1000 0.5937  -0.2264 6   HIS A CG  
31   N ND1 . HIS A 6   ? 1.6087 0.9998 0.9159 -0.1119 0.6007  -0.2160 6   HIS A ND1 
32   C CD2 . HIS A 6   ? 1.6106 0.9855 0.9274 -0.1010 0.6179  -0.2472 6   HIS A CD2 
33   C CE1 . HIS A 6   ? 1.6120 1.0093 0.9191 -0.1206 0.6284  -0.2303 6   HIS A CE1 
34   N NE2 . HIS A 6   ? 1.6383 1.0266 0.9512 -0.1136 0.6397  -0.2495 6   HIS A NE2 
35   N N   . ASN A 7   ? 2.5048 1.8498 1.8184 -0.0749 0.5169  -0.2021 7   ASN A N   
36   C CA  . ASN A 7   ? 2.4813 1.8221 1.8093 -0.0644 0.4938  -0.1945 7   ASN A CA  
37   C C   . ASN A 7   ? 2.4050 1.7833 1.8024 -0.0442 0.4930  -0.1813 7   ASN A C   
38   O O   . ASN A 7   ? 2.4444 1.8330 1.8906 -0.0259 0.4900  -0.1825 7   ASN A O   
39   C CB  . ASN A 7   ? 2.5028 1.8237 1.8349 -0.0591 0.4922  -0.2102 7   ASN A CB  
40   C CG  . ASN A 7   ? 2.6306 1.9125 1.8896 -0.0807 0.4845  -0.2216 7   ASN A CG  
41   O OD1 . ASN A 7   ? 2.6259 1.8880 1.8530 -0.0881 0.4608  -0.2192 7   ASN A OD1 
42   N ND2 . ASN A 7   ? 2.6087 1.8802 1.8412 -0.0913 0.5039  -0.2350 7   ASN A ND2 
43   N N   . GLY A 8   ? 1.9513 1.3487 1.3514 -0.0486 0.4946  -0.1678 8   GLY A N   
44   C CA  . GLY A 8   ? 1.8113 1.2456 1.2745 -0.0320 0.4938  -0.1558 8   GLY A CA  
45   C C   . GLY A 8   ? 1.7668 1.2030 1.2163 -0.0358 0.4759  -0.1362 8   GLY A C   
46   O O   . GLY A 8   ? 1.7866 1.2532 1.2834 -0.0250 0.4750  -0.1252 8   GLY A O   
47   N N   . LEU A 9   ? 1.8182 1.2222 1.2026 -0.0509 0.4602  -0.1318 9   LEU A N   
48   C CA  . LEU A 9   ? 1.7340 1.1421 1.1092 -0.0550 0.4349  -0.1101 9   LEU A CA  
49   C C   . LEU A 9   ? 1.6340 1.0339 1.0068 -0.0532 0.3976  -0.1022 9   LEU A C   
50   O O   . LEU A 9   ? 1.5679 0.9822 0.9597 -0.0500 0.3732  -0.0838 9   LEU A O   
51   C CB  . LEU A 9   ? 1.7821 1.1685 1.0915 -0.0760 0.4387  -0.1037 9   LEU A CB  
52   C CG  . LEU A 9   ? 1.7407 1.1443 1.0648 -0.0822 0.4658  -0.1070 9   LEU A CG  
53   C CD1 . LEU A 9   ? 1.6689 1.0455 0.9252 -0.1050 0.4638  -0.0996 9   LEU A CD1 
54   C CD2 . LEU A 9   ? 1.6170 1.0605 1.0070 -0.0700 0.4706  -0.0969 9   LEU A CD2 
55   N N   . ASP A 10  ? 1.6664 1.0445 1.0185 -0.0560 0.3935  -0.1167 10  ASP A N   
56   C CA  . ASP A 10  ? 1.5552 0.9279 0.9076 -0.0568 0.3598  -0.1123 10  ASP A CA  
57   C C   . ASP A 10  ? 1.3559 0.7439 0.7683 -0.0403 0.3605  -0.1161 10  ASP A C   
58   O O   . ASP A 10  ? 1.3733 0.7467 0.7874 -0.0371 0.3772  -0.1335 10  ASP A O   
59   C CB  . ASP A 10  ? 1.5960 0.9338 0.8847 -0.0735 0.3527  -0.1261 10  ASP A CB  
60   C CG  . ASP A 10  ? 1.4569 0.7935 0.7458 -0.0772 0.3152  -0.1217 10  ASP A CG  
61   O OD1 . ASP A 10  ? 1.4408 0.7994 0.7848 -0.0655 0.3035  -0.1155 10  ASP A OD1 
62   O OD2 . ASP A 10  ? 1.5028 0.8172 0.7365 -0.0925 0.2974  -0.1248 10  ASP A OD2 
63   N N   . PHE A 11  ? 1.2700 0.6839 0.7284 -0.0303 0.3428  -0.0999 11  PHE A N   
64   C CA  . PHE A 11  ? 1.2726 0.6995 0.7839 -0.0157 0.3415  -0.0999 11  PHE A CA  
65   C C   . PHE A 11  ? 1.1894 0.6060 0.6994 -0.0212 0.3186  -0.1028 11  PHE A C   
66   O O   . PHE A 11  ? 1.2085 0.6365 0.7596 -0.0123 0.3120  -0.0981 11  PHE A O   
67   C CB  . PHE A 11  ? 1.1686 0.6278 0.7276 -0.0039 0.3361  -0.0822 11  PHE A CB  
68   C CG  . PHE A 11  ? 1.2209 0.6963 0.8089 0.0079  0.3617  -0.0839 11  PHE A CG  
69   C CD1 . PHE A 11  ? 1.2938 0.7704 0.8599 0.0014  0.3806  -0.0867 11  PHE A CD1 
70   C CD2 . PHE A 11  ? 1.1980 0.6879 0.8351 0.0248  0.3663  -0.0826 11  PHE A CD2 
71   C CE1 . PHE A 11  ? 1.2481 0.7454 0.8477 0.0116  0.4043  -0.0901 11  PHE A CE1 
72   C CE2 . PHE A 11  ? 1.1633 0.6722 0.8319 0.0369  0.3867  -0.0847 11  PHE A CE2 
73   C CZ  . PHE A 11  ? 1.1944 0.7098 0.8477 0.0303  0.4060  -0.0893 11  PHE A CZ  
74   N N   . SER A 12  ? 1.1570 0.5525 0.6196 -0.0370 0.3065  -0.1109 12  SER A N   
75   C CA  . SER A 12  ? 1.2062 0.5957 0.6705 -0.0446 0.2843  -0.1158 12  SER A CA  
76   C C   . SER A 12  ? 1.2889 0.6657 0.7765 -0.0392 0.2982  -0.1284 12  SER A C   
77   O O   . SER A 12  ? 1.2927 0.6763 0.8099 -0.0387 0.2854  -0.1259 12  SER A O   
78   C CB  . SER A 12  ? 1.2968 0.6640 0.7028 -0.0630 0.2702  -0.1254 12  SER A CB  
79   O OG  . SER A 12  ? 1.3870 0.7629 0.7719 -0.0674 0.2502  -0.1109 12  SER A OG  
80   N N   . ALA A 13  ? 1.2975 0.6540 0.7718 -0.0352 0.3257  -0.1423 13  ALA A N   
81   C CA  . ALA A 13  ? 1.3032 0.6397 0.7941 -0.0291 0.3394  -0.1549 13  ALA A CA  
82   C C   . ALA A 13  ? 1.2257 0.5796 0.7721 -0.0111 0.3414  -0.1422 13  ALA A C   
83   O O   . ALA A 13  ? 1.1846 0.5192 0.7455 -0.0056 0.3489  -0.1491 13  ALA A O   
84   C CB  . ALA A 13  ? 1.2402 0.5519 0.7072 -0.0260 0.3697  -0.1733 13  ALA A CB  
85   N N   . LYS A 14  ? 1.1434 0.5295 0.7174 -0.0025 0.3347  -0.1240 14  LYS A N   
86   C CA  . LYS A 14  ? 1.1310 0.5341 0.7527 0.0131  0.3340  -0.1111 14  LYS A CA  
87   C C   . LYS A 14  ? 1.0804 0.5009 0.7207 0.0074  0.3099  -0.0982 14  LYS A C   
88   O O   . LYS A 14  ? 1.0409 0.4759 0.7161 0.0179  0.3078  -0.0864 14  LYS A O   
89   C CB  . LYS A 14  ? 1.1625 0.5908 0.8065 0.0270  0.3458  -0.1018 14  LYS A CB  
90   C CG  . LYS A 14  ? 1.1589 0.5768 0.8021 0.0374  0.3730  -0.1149 14  LYS A CG  
91   C CD  . LYS A 14  ? 1.2758 0.7255 0.9530 0.0515  0.3826  -0.1056 14  LYS A CD  
92   C CE  . LYS A 14  ? 1.3894 0.8350 1.0758 0.0637  0.4106  -0.1202 14  LYS A CE  
93   N NZ  . LYS A 14  ? 1.6070 1.0405 1.2512 0.0498  0.4265  -0.1347 14  LYS A NZ  
94   N N   . VAL A 15  ? 1.1080 0.5281 0.7263 -0.0087 0.2916  -0.1010 15  VAL A N   
95   C CA  . VAL A 15  ? 1.1029 0.5437 0.7427 -0.0140 0.2692  -0.0911 15  VAL A CA  
96   C C   . VAL A 15  ? 1.0887 0.5149 0.7406 -0.0205 0.2676  -0.0986 15  VAL A C   
97   O O   . VAL A 15  ? 1.1014 0.5077 0.7300 -0.0343 0.2644  -0.1132 15  VAL A O   
98   C CB  . VAL A 15  ? 1.0662 0.5154 0.6814 -0.0265 0.2480  -0.0907 15  VAL A CB  
99   C CG1 . VAL A 15  ? 1.0222 0.4962 0.6674 -0.0295 0.2260  -0.0822 15  VAL A CG1 
100  C CG2 . VAL A 15  ? 1.0105 0.4665 0.6067 -0.0222 0.2519  -0.0826 15  VAL A CG2 
101  N N   . ILE A 16  ? 1.0133 0.4477 0.6990 -0.0123 0.2700  -0.0888 16  ILE A N   
102  C CA  . ILE A 16  ? 1.0413 0.4594 0.7373 -0.0201 0.2703  -0.0941 16  ILE A CA  
103  C C   . ILE A 16  ? 0.9757 0.4165 0.6899 -0.0333 0.2516  -0.0919 16  ILE A C   
104  O O   . ILE A 16  ? 1.0814 0.5108 0.8026 -0.0451 0.2516  -0.0986 16  ILE A O   
105  C CB  . ILE A 16  ? 1.0388 0.4464 0.7554 -0.0055 0.2840  -0.0851 16  ILE A CB  
106  C CG1 . ILE A 16  ? 0.9884 0.4281 0.7325 0.0046  0.2779  -0.0674 16  ILE A CG1 
107  C CG2 . ILE A 16  ? 1.0165 0.4017 0.7213 0.0089  0.3024  -0.0903 16  ILE A CG2 
108  C CD1 . ILE A 16  ? 1.0229 0.4533 0.7834 0.0195  0.2880  -0.0572 16  ILE A CD1 
109  N N   . GLN A 17  ? 1.0238 0.4958 0.7475 -0.0318 0.2367  -0.0833 17  GLN A N   
110  C CA  . GLN A 17  ? 0.9967 0.4936 0.7411 -0.0427 0.2179  -0.0836 17  GLN A CA  
111  C C   . GLN A 17  ? 0.9885 0.5085 0.7284 -0.0394 0.2006  -0.0772 17  GLN A C   
112  O O   . GLN A 17  ? 0.9818 0.5137 0.7287 -0.0268 0.2033  -0.0643 17  GLN A O   
113  C CB  . GLN A 17  ? 0.9353 0.4462 0.7150 -0.0399 0.2217  -0.0747 17  GLN A CB  
114  C CG  . GLN A 17  ? 0.8905 0.4332 0.6981 -0.0488 0.2045  -0.0756 17  GLN A CG  
115  C CD  . GLN A 17  ? 0.9387 0.4923 0.7775 -0.0498 0.2120  -0.0700 17  GLN A CD  
116  O OE1 . GLN A 17  ? 1.0089 0.5400 0.8457 -0.0548 0.2263  -0.0719 17  GLN A OE1 
117  N NE2 . GLN A 17  ? 0.8650 0.4499 0.7299 -0.0454 0.2029  -0.0632 17  GLN A NE2 
118  N N   . GLY A 18  ? 0.9671 0.4919 0.6948 -0.0511 0.1817  -0.0859 18  GLY A N   
119  C CA  . GLY A 18  ? 0.9625 0.5031 0.6805 -0.0483 0.1618  -0.0794 18  GLY A CA  
120  C C   . GLY A 18  ? 1.0784 0.5958 0.7456 -0.0532 0.1596  -0.0854 18  GLY A C   
121  O O   . GLY A 18  ? 1.2085 0.6994 0.8501 -0.0595 0.1733  -0.0972 18  GLY A O   
122  N N   . SER A 19  ? 1.1436 0.6681 0.7934 -0.0504 0.1425  -0.0771 19  SER A N   
123  C CA  . SER A 19  ? 1.1180 0.6192 0.7128 -0.0566 0.1385  -0.0808 19  SER A CA  
124  C C   . SER A 19  ? 1.2206 0.7232 0.7996 -0.0473 0.1363  -0.0646 19  SER A C   
125  O O   . SER A 19  ? 1.2411 0.7625 0.8384 -0.0419 0.1160  -0.0538 19  SER A O   
126  C CB  . SER A 19  ? 1.1725 0.6746 0.7505 -0.0702 0.1101  -0.0910 19  SER A CB  
127  O OG  . SER A 19  ? 1.3635 0.8389 0.8805 -0.0777 0.1062  -0.0947 19  SER A OG  
128  N N   . LEU A 20  ? 1.2302 0.7126 0.7768 -0.0458 0.1583  -0.0637 20  LEU A N   
129  C CA  . LEU A 20  ? 1.2740 0.7525 0.7973 -0.0415 0.1580  -0.0497 20  LEU A CA  
130  C C   . LEU A 20  ? 1.3494 0.8184 0.8339 -0.0488 0.1288  -0.0458 20  LEU A C   
131  O O   . LEU A 20  ? 1.3391 0.8093 0.8160 -0.0437 0.1175  -0.0307 20  LEU A O   
132  C CB  . LEU A 20  ? 1.1873 0.6460 0.6802 -0.0423 0.1883  -0.0534 20  LEU A CB  
133  C CG  . LEU A 20  ? 1.1709 0.6394 0.7019 -0.0318 0.2159  -0.0551 20  LEU A CG  
134  C CD1 . LEU A 20  ? 1.2647 0.7181 0.7686 -0.0322 0.2442  -0.0599 20  LEU A CD1 
135  C CD2 . LEU A 20  ? 1.0562 0.5516 0.6337 -0.0202 0.2122  -0.0403 20  LEU A CD2 
136  N N   . ASP A 21  ? 1.3759 0.8333 0.8341 -0.0608 0.1148  -0.0591 21  ASP A N   
137  C CA  . ASP A 21  ? 1.4954 0.9441 0.9158 -0.0674 0.0822  -0.0556 21  ASP A CA  
138  C C   . ASP A 21  ? 1.4674 0.9448 0.9316 -0.0575 0.0526  -0.0445 21  ASP A C   
139  O O   . ASP A 21  ? 1.5939 1.0648 1.0354 -0.0539 0.0300  -0.0315 21  ASP A O   
140  C CB  . ASP A 21  ? 1.5664 1.0022 0.9580 -0.0829 0.0712  -0.0743 21  ASP A CB  
141  C CG  . ASP A 21  ? 1.6967 1.1003 1.0406 -0.0927 0.1007  -0.0874 21  ASP A CG  
142  O OD1 . ASP A 21  ? 1.6707 1.0573 0.9833 -0.0906 0.1210  -0.0803 21  ASP A OD1 
143  O OD2 . ASP A 21  ? 1.7360 1.1310 1.0748 -0.1031 0.1048  -0.1061 21  ASP A OD2 
144  N N   . SER A 22  ? 1.3550 0.8619 0.8810 -0.0529 0.0532  -0.0496 22  SER A N   
145  C CA  . SER A 22  ? 1.3066 0.8444 0.8813 -0.0435 0.0288  -0.0427 22  SER A CA  
146  C C   . SER A 22  ? 1.2779 0.8228 0.8736 -0.0288 0.0365  -0.0254 22  SER A C   
147  O O   . SER A 22  ? 1.3484 0.9164 0.9839 -0.0192 0.0185  -0.0195 22  SER A O   
148  C CB  . SER A 22  ? 1.2667 0.8324 0.8980 -0.0467 0.0314  -0.0558 22  SER A CB  
149  O OG  . SER A 22  ? 1.3063 0.8712 0.9582 -0.0440 0.0644  -0.0567 22  SER A OG  
150  N N   . LEU A 23  ? 1.2396 0.7663 0.8120 -0.0271 0.0631  -0.0187 23  LEU A N   
151  C CA  . LEU A 23  ? 1.2429 0.7757 0.8341 -0.0155 0.0705  -0.0035 23  LEU A CA  
152  C C   . LEU A 23  ? 1.3009 0.8140 0.8526 -0.0133 0.0509  0.0108  23  LEU A C   
153  O O   . LEU A 23  ? 1.3636 0.8488 0.8571 -0.0225 0.0458  0.0108  23  LEU A O   
154  C CB  . LEU A 23  ? 1.1773 0.7026 0.7646 -0.0151 0.1057  -0.0027 23  LEU A CB  
155  C CG  . LEU A 23  ? 1.2025 0.7455 0.8335 -0.0125 0.1256  -0.0113 23  LEU A CG  
156  C CD1 . LEU A 23  ? 1.1743 0.7106 0.8006 -0.0097 0.1560  -0.0092 23  LEU A CD1 
157  C CD2 . LEU A 23  ? 1.0735 0.6448 0.7590 -0.0042 0.1164  -0.0074 23  LEU A CD2 
158  N N   . PRO A 24  ? 1.2254 0.7487 0.8042 -0.0016 0.0398  0.0231  24  PRO A N   
159  C CA  . PRO A 24  ? 1.3124 0.8096 0.8506 0.0013  0.0243  0.0391  24  PRO A CA  
160  C C   . PRO A 24  ? 1.3864 0.8523 0.8700 -0.0082 0.0492  0.0445  24  PRO A C   
161  O O   . PRO A 24  ? 1.4011 0.8731 0.8944 -0.0120 0.0802  0.0377  24  PRO A O   
162  C CB  . PRO A 24  ? 1.2732 0.7872 0.8589 0.0156  0.0204  0.0486  24  PRO A CB  
163  C CG  . PRO A 24  ? 1.2256 0.7779 0.8750 0.0202  0.0190  0.0360  24  PRO A CG  
164  C CD  . PRO A 24  ? 1.2240 0.7796 0.8689 0.0089  0.0410  0.0223  24  PRO A CD  
165  N N   . GLN A 25  ? 1.6760 1.1083 1.1025 -0.0120 0.0358  0.0567  25  GLN A N   
166  C CA  . GLN A 25  ? 1.6928 1.0932 1.0616 -0.0242 0.0601  0.0613  25  GLN A CA  
167  C C   . GLN A 25  ? 1.6208 1.0338 1.0200 -0.0228 0.0946  0.0623  25  GLN A C   
168  O O   . GLN A 25  ? 1.5833 1.0039 0.9866 -0.0287 0.1232  0.0509  25  GLN A O   
169  C CB  . GLN A 25  ? 1.8182 1.1793 1.1282 -0.0264 0.0398  0.0791  25  GLN A CB  
170  C CG  . GLN A 25  ? 1.8741 1.1981 1.1157 -0.0427 0.0651  0.0835  25  GLN A CG  
171  C CD  . GLN A 25  ? 2.0933 1.4042 1.2884 -0.0573 0.0739  0.0690  25  GLN A CD  
172  O OE1 . GLN A 25  ? 2.0850 1.4128 1.2975 -0.0557 0.0594  0.0560  25  GLN A OE1 
173  N NE2 . GLN A 25  ? 2.2003 1.4801 1.3355 -0.0729 0.0994  0.0699  25  GLN A NE2 
174  N N   . GLU A 26  ? 1.4580 0.8736 0.8802 -0.0144 0.0911  0.0750  26  GLU A N   
175  C CA  . GLU A 26  ? 1.3935 0.8201 0.8408 -0.0148 0.1210  0.0765  26  GLU A CA  
176  C C   . GLU A 26  ? 1.2821 0.7469 0.7896 -0.0086 0.1364  0.0637  26  GLU A C   
177  O O   . GLU A 26  ? 1.2340 0.7096 0.7573 -0.0108 0.1635  0.0608  26  GLU A O   
178  C CB  . GLU A 26  ? 1.4358 0.8549 0.8946 -0.0077 0.1114  0.0916  26  GLU A CB  
179  C CG  . GLU A 26  ? 1.5851 0.9587 0.9791 -0.0145 0.0995  0.1070  26  GLU A CG  
180  C CD  . GLU A 26  ? 1.5700 0.9192 0.9098 -0.0329 0.1277  0.1067  26  GLU A CD  
181  O OE1 . GLU A 26  ? 1.4937 0.8635 0.8579 -0.0377 0.1591  0.0979  26  GLU A OE1 
182  O OE2 . GLU A 26  ? 1.6397 0.9494 0.9123 -0.0425 0.1184  0.1148  26  GLU A OE2 
183  N N   . VAL A 27  ? 1.2533 0.7386 0.7945 -0.0015 0.1195  0.0561  27  VAL A N   
184  C CA  . VAL A 27  ? 1.2024 0.7176 0.7933 0.0028  0.1343  0.0450  27  VAL A CA  
185  C C   . VAL A 27  ? 1.1662 0.6764 0.7385 -0.0051 0.1572  0.0334  27  VAL A C   
186  O O   . VAL A 27  ? 1.0092 0.5325 0.6053 -0.0031 0.1806  0.0294  27  VAL A O   
187  C CB  . VAL A 27  ? 1.1727 0.7085 0.8009 0.0092  0.1127  0.0388  27  VAL A CB  
188  C CG1 . VAL A 27  ? 1.0467 0.6068 0.7185 0.0114  0.1293  0.0287  27  VAL A CG1 
189  C CG2 . VAL A 27  ? 1.0731 0.6156 0.7251 0.0191  0.0921  0.0485  27  VAL A CG2 
190  N N   . ARG A 28  ? 1.1781 0.6683 0.7071 -0.0137 0.1500  0.0273  28  ARG A N   
191  C CA  . ARG A 28  ? 1.2183 0.7001 0.7271 -0.0211 0.1731  0.0143  28  ARG A CA  
192  C C   . ARG A 28  ? 1.1703 0.6454 0.6645 -0.0247 0.2023  0.0167  28  ARG A C   
193  O O   . ARG A 28  ? 1.1584 0.6442 0.6725 -0.0226 0.2267  0.0074  28  ARG A O   
194  C CB  . ARG A 28  ? 1.2324 0.6894 0.6884 -0.0319 0.1600  0.0073  28  ARG A CB  
195  C CG  . ARG A 28  ? 1.2719 0.7144 0.6992 -0.0405 0.1866  -0.0073 28  ARG A CG  
196  C CD  . ARG A 28  ? 1.4157 0.8392 0.8031 -0.0509 0.1726  -0.0192 28  ARG A CD  
197  N NE  . ARG A 28  ? 1.3767 0.7867 0.7438 -0.0576 0.2004  -0.0360 28  ARG A NE  
198  C CZ  . ARG A 28  ? 1.4244 0.8191 0.7648 -0.0667 0.1959  -0.0514 28  ARG A CZ  
199  N NH1 . ARG A 28  ? 1.4729 0.8669 0.8049 -0.0713 0.1637  -0.0525 28  ARG A NH1 
200  N NH2 . ARG A 28  ? 1.3764 0.7571 0.7006 -0.0711 0.2245  -0.0674 28  ARG A NH2 
201  N N   . LYS A 29  ? 1.1678 0.6251 0.6284 -0.0301 0.2001  0.0290  29  LYS A N   
202  C CA  . LYS A 29  ? 1.2111 0.6639 0.6591 -0.0365 0.2292  0.0304  29  LYS A CA  
203  C C   . LYS A 29  ? 1.1137 0.5986 0.6215 -0.0271 0.2448  0.0302  29  LYS A C   
204  O O   . LYS A 29  ? 1.0719 0.5674 0.5915 -0.0284 0.2718  0.0222  29  LYS A O   
205  C CB  . LYS A 29  ? 1.3227 0.7480 0.7255 -0.0451 0.2224  0.0456  29  LYS A CB  
206  C CG  . LYS A 29  ? 1.3649 0.7523 0.6949 -0.0574 0.2121  0.0466  29  LYS A CG  
207  C CD  . LYS A 29  ? 1.5350 0.8905 0.8193 -0.0648 0.2034  0.0648  29  LYS A CD  
208  C CE  . LYS A 29  ? 1.7637 1.0765 0.9668 -0.0780 0.1919  0.0677  29  LYS A CE  
209  N NZ  . LYS A 29  ? 1.8226 1.1189 0.9808 -0.0951 0.2267  0.0571  29  LYS A NZ  
210  N N   . PHE A 30  ? 1.0957 0.5970 0.6420 -0.0174 0.2276  0.0382  30  PHE A N   
211  C CA  . PHE A 30  ? 1.0034 0.5335 0.6021 -0.0094 0.2392  0.0384  30  PHE A CA  
212  C C   . PHE A 30  ? 0.9820 0.5303 0.6118 -0.0025 0.2508  0.0259  30  PHE A C   
213  O O   . PHE A 30  ? 0.9589 0.5256 0.6175 0.0016  0.2689  0.0228  30  PHE A O   
214  C CB  . PHE A 30  ? 0.9939 0.5340 0.6219 -0.0014 0.2183  0.0477  30  PHE A CB  
215  C CG  . PHE A 30  ? 0.8683 0.4363 0.5460 0.0062  0.2270  0.0474  30  PHE A CG  
216  C CD1 . PHE A 30  ? 0.9285 0.5056 0.6154 0.0028  0.2461  0.0489  30  PHE A CD1 
217  C CD2 . PHE A 30  ? 0.8744 0.4594 0.5884 0.0151  0.2156  0.0454  30  PHE A CD2 
218  C CE1 . PHE A 30  ? 0.8621 0.4647 0.5920 0.0093  0.2510  0.0486  30  PHE A CE1 
219  C CE2 . PHE A 30  ? 0.8565 0.4635 0.6092 0.0209  0.2226  0.0457  30  PHE A CE2 
220  C CZ  . PHE A 30  ? 0.8818 0.4974 0.6416 0.0184  0.2388  0.0476  30  PHE A CZ  
221  N N   . VAL A 31  ? 0.9984 0.5407 0.6227 -0.0014 0.2396  0.0185  31  VAL A N   
222  C CA  . VAL A 31  ? 1.0010 0.5531 0.6503 0.0045  0.2499  0.0072  31  VAL A CA  
223  C C   . VAL A 31  ? 1.0060 0.5494 0.6365 0.0012  0.2751  -0.0034 31  VAL A C   
224  O O   . VAL A 31  ? 0.9540 0.5124 0.6139 0.0086  0.2928  -0.0077 31  VAL A O   
225  C CB  . VAL A 31  ? 1.0283 0.5745 0.6759 0.0037  0.2318  0.0013  31  VAL A CB  
226  C CG1 . VAL A 31  ? 0.9676 0.5148 0.6324 0.0077  0.2444  -0.0106 31  VAL A CG1 
227  C CG2 . VAL A 31  ? 0.9853 0.5463 0.6619 0.0084  0.2105  0.0093  31  VAL A CG2 
228  N N   . GLU A 32  ? 1.0921 0.6110 0.6732 -0.0096 0.2766  -0.0085 32  GLU A N   
229  C CA  . GLU A 32  ? 1.0998 0.6085 0.6610 -0.0136 0.3027  -0.0217 32  GLU A CA  
230  C C   . GLU A 32  ? 1.0931 0.6150 0.6653 -0.0141 0.3265  -0.0199 32  GLU A C   
231  O O   . GLU A 32  ? 1.0703 0.5994 0.6561 -0.0104 0.3508  -0.0317 32  GLU A O   
232  C CB  . GLU A 32  ? 1.2241 0.7012 0.7230 -0.0275 0.2989  -0.0275 32  GLU A CB  
233  C CG  . GLU A 32  ? 1.3107 0.7759 0.8008 -0.0284 0.2850  -0.0379 32  GLU A CG  
234  C CD  . GLU A 32  ? 1.3317 0.7653 0.7568 -0.0433 0.2817  -0.0456 32  GLU A CD  
235  O OE1 . GLU A 32  ? 1.4493 0.8680 0.8323 -0.0528 0.2787  -0.0370 32  GLU A OE1 
236  O OE2 . GLU A 32  ? 1.2747 0.6954 0.6875 -0.0466 0.2821  -0.0602 32  GLU A OE2 
237  N N   . GLY A 33  ? 1.0582 0.5839 0.6274 -0.0187 0.3202  -0.0063 33  GLY A N   
238  C CA  . GLY A 33  ? 0.9739 0.5141 0.5560 -0.0221 0.3428  -0.0053 33  GLY A CA  
239  C C   . GLY A 33  ? 0.9904 0.5648 0.6339 -0.0081 0.3523  -0.0090 33  GLY A C   
240  O O   . GLY A 33  ? 0.9677 0.5571 0.6288 -0.0069 0.3767  -0.0185 33  GLY A O   
241  N N   . ASN A 34  ? 0.9066 0.4942 0.5837 0.0026  0.3328  -0.0020 34  ASN A N   
242  C CA  . ASN A 34  ? 0.8986 0.5150 0.6285 0.0160  0.3378  -0.0038 34  ASN A CA  
243  C C   . ASN A 34  ? 0.9493 0.5635 0.6921 0.0268  0.3445  -0.0155 34  ASN A C   
244  O O   . ASN A 34  ? 0.9410 0.5749 0.7201 0.0380  0.3560  -0.0204 34  ASN A O   
245  C CB  . ASN A 34  ? 0.8476 0.4753 0.6025 0.0214  0.3164  0.0079  34  ASN A CB  
246  C CG  . ASN A 34  ? 0.9009 0.5306 0.6492 0.0126  0.3118  0.0186  34  ASN A CG  
247  O OD1 . ASN A 34  ? 0.9062 0.5561 0.6780 0.0117  0.3218  0.0200  34  ASN A OD1 
248  N ND2 . ASN A 34  ? 0.9173 0.5255 0.6343 0.0061  0.2958  0.0259  34  ASN A ND2 
249  N N   . ALA A 35  ? 0.9442 0.5338 0.6584 0.0240  0.3364  -0.0204 35  ALA A N   
250  C CA  . ALA A 35  ? 0.9484 0.5281 0.6661 0.0315  0.3468  -0.0337 35  ALA A CA  
251  C C   . ALA A 35  ? 1.0078 0.5918 0.7260 0.0324  0.3750  -0.0460 35  ALA A C   
252  O O   . ALA A 35  ? 1.0561 0.6529 0.8093 0.0464  0.3870  -0.0530 35  ALA A O   
253  C CB  . ALA A 35  ? 0.9125 0.4631 0.5912 0.0230  0.3361  -0.0394 35  ALA A CB  
254  N N   . GLN A 36  ? 0.9971 0.5701 0.6766 0.0177  0.3862  -0.0488 36  GLN A N   
255  C CA  . GLN A 36  ? 1.0447 0.6231 0.7233 0.0157  0.4167  -0.0622 36  GLN A CA  
256  C C   . GLN A 36  ? 0.9732 0.5899 0.7049 0.0244  0.4279  -0.0602 36  GLN A C   
257  O O   . GLN A 36  ? 0.9477 0.5793 0.7050 0.0320  0.4510  -0.0736 36  GLN A O   
258  C CB  . GLN A 36  ? 1.1407 0.6977 0.7617 -0.0051 0.4257  -0.0628 36  GLN A CB  
259  C CG  . GLN A 36  ? 1.2743 0.7942 0.8394 -0.0147 0.4125  -0.0655 36  GLN A CG  
260  C CD  . GLN A 36  ? 1.4301 0.9257 0.9329 -0.0352 0.4144  -0.0611 36  GLN A CD  
261  O OE1 . GLN A 36  ? 1.6649 1.1295 1.1144 -0.0457 0.4126  -0.0682 36  GLN A OE1 
262  N NE2 . GLN A 36  ? 1.3093 0.8158 0.8151 -0.0418 0.4172  -0.0492 36  GLN A NE2 
263  N N   . LEU A 37  ? 0.9573 0.5911 0.7078 0.0235  0.4117  -0.0449 37  LEU A N   
264  C CA  . LEU A 37  ? 0.9459 0.6174 0.7465 0.0300  0.4194  -0.0435 37  LEU A CA  
265  C C   . LEU A 37  ? 0.9624 0.6522 0.8121 0.0517  0.4107  -0.0441 37  LEU A C   
266  O O   . LEU A 37  ? 0.9029 0.6195 0.7939 0.0627  0.4243  -0.0522 37  LEU A O   
267  C CB  . LEU A 37  ? 0.9247 0.6042 0.7237 0.0196  0.4060  -0.0282 37  LEU A CB  
268  C CG  . LEU A 37  ? 0.9497 0.6682 0.8031 0.0270  0.4047  -0.0248 37  LEU A CG  
269  C CD1 . LEU A 37  ? 0.9401 0.6859 0.8190 0.0240  0.4324  -0.0372 37  LEU A CD1 
270  C CD2 . LEU A 37  ? 0.9126 0.6321 0.7612 0.0176  0.3881  -0.0100 37  LEU A CD2 
271  N N   . CYS A 38  ? 0.9071 0.5826 0.7530 0.0578  0.3880  -0.0356 38  CYS A N   
272  C CA  . CYS A 38  ? 0.9236 0.6103 0.8079 0.0762  0.3776  -0.0329 38  CYS A CA  
273  C C   . CYS A 38  ? 0.9051 0.5739 0.7912 0.0891  0.3858  -0.0445 38  CYS A C   
274  O O   . CYS A 38  ? 0.9243 0.6027 0.8451 0.1068  0.3829  -0.0443 38  CYS A O   
275  C CB  . CYS A 38  ? 0.9333 0.6119 0.8123 0.0749  0.3523  -0.0190 38  CYS A CB  
276  S SG  . CYS A 38  ? 0.9103 0.6083 0.7940 0.0637  0.3409  -0.0056 38  CYS A SG  
277  N N   A GLN A 39  ? 0.9815 0.6215 0.8285 0.0805  0.3950  -0.0543 39  GLN A N   
278  N N   B GLN A 39  ? 0.9867 0.6267 0.8337 0.0806  0.3950  -0.0543 39  GLN A N   
279  C CA  A GLN A 39  ? 1.0464 0.6638 0.8899 0.0906  0.4048  -0.0675 39  GLN A CA  
280  C CA  B GLN A 39  ? 0.9749 0.5924 0.8186 0.0907  0.4047  -0.0674 39  GLN A CA  
281  C C   A GLN A 39  ? 1.0623 0.6649 0.9159 0.1012  0.3863  -0.0602 39  GLN A C   
282  C C   B GLN A 39  ? 0.9887 0.5912 0.8423 0.1012  0.3863  -0.0602 39  GLN A C   
283  O O   A GLN A 39  ? 0.9442 0.5476 0.8273 0.1195  0.3890  -0.0627 39  GLN A O   
284  O O   B GLN A 39  ? 1.0272 0.6305 0.9103 0.1195  0.3890  -0.0626 39  GLN A O   
285  C CB  A GLN A 39  ? 1.0060 0.6430 0.8854 0.1052  0.4273  -0.0802 39  GLN A CB  
286  C CB  B GLN A 39  ? 0.9341 0.5712 0.8141 0.1055  0.4271  -0.0801 39  GLN A CB  
287  C CG  A GLN A 39  ? 0.9428 0.5929 0.8106 0.0913  0.4480  -0.0901 39  GLN A CG  
288  C CG  B GLN A 39  ? 0.9389 0.5935 0.8120 0.0922  0.4470  -0.0885 39  GLN A CG  
289  C CD  A GLN A 39  ? 0.9885 0.6049 0.8052 0.0773  0.4573  -0.1018 39  GLN A CD  
290  C CD  B GLN A 39  ? 0.9339 0.6139 0.8482 0.1036  0.4605  -0.1012 39  GLN A CD  
291  O OE1 A GLN A 39  ? 1.1008 0.6860 0.8963 0.0797  0.4504  -0.1052 39  GLN A OE1 
292  O OE1 B GLN A 39  ? 0.9760 0.6441 0.9017 0.1174  0.4602  -0.1089 39  GLN A OE1 
293  N NE2 A GLN A 39  ? 1.0156 0.6368 0.8106 0.0611  0.4728  -0.1081 39  GLN A NE2 
294  N NE2 B GLN A 39  ? 0.9135 0.6286 0.8513 0.0976  0.4723  -0.1039 39  GLN A NE2 
295  N N   . PRO A 40  ? 0.9964 0.5845 0.8268 0.0902  0.3677  -0.0514 40  PRO A N   
296  C CA  . PRO A 40  ? 1.0595 0.6296 0.8944 0.0963  0.3542  -0.0468 40  PRO A CA  
297  C C   . PRO A 40  ? 1.0217 0.5562 0.8330 0.0955  0.3628  -0.0608 40  PRO A C   
298  O O   . PRO A 40  ? 1.0340 0.5545 0.8128 0.0836  0.3714  -0.0719 40  PRO A O   
299  C CB  . PRO A 40  ? 0.9195 0.4915 0.7402 0.0825  0.3345  -0.0356 40  PRO A CB  
300  C CG  . PRO A 40  ? 0.8996 0.4712 0.6899 0.0677  0.3380  -0.0394 40  PRO A CG  
301  C CD  . PRO A 40  ? 0.9385 0.5265 0.7392 0.0720  0.3580  -0.0453 40  PRO A CD  
302  N N   A GLU A 41  ? 1.0140 0.5306 0.8385 0.1075  0.3604  -0.0603 41  GLU A N   
303  N N   B GLU A 41  ? 1.0157 0.5322 0.8400 0.1074  0.3604  -0.0603 41  GLU A N   
304  C CA  A GLU A 41  ? 1.0172 0.4953 0.8195 0.1062  0.3684  -0.0738 41  GLU A CA  
305  C CA  B GLU A 41  ? 1.0593 0.5374 0.8613 0.1061  0.3686  -0.0739 41  GLU A CA  
306  C C   A GLU A 41  ? 1.0595 0.5195 0.8285 0.0854  0.3562  -0.0750 41  GLU A C   
307  C C   B GLU A 41  ? 1.0603 0.5197 0.8295 0.0856  0.3562  -0.0750 41  GLU A C   
308  O O   A GLU A 41  ? 1.0842 0.5189 0.8231 0.0757  0.3632  -0.0895 41  GLU A O   
309  O O   B GLU A 41  ? 1.0869 0.5200 0.8267 0.0763  0.3631  -0.0895 41  GLU A O   
310  C CB  A GLU A 41  ? 1.0149 0.4774 0.8387 0.1227  0.3656  -0.0698 41  GLU A CB  
311  C CB  B GLU A 41  ? 1.0334 0.4962 0.8573 0.1229  0.3663  -0.0704 41  GLU A CB  
312  C CG  A GLU A 41  ? 1.0706 0.4994 0.8768 0.1200  0.3702  -0.0816 41  GLU A CG  
313  C CG  B GLU A 41  ? 1.0709 0.5004 0.8766 0.1199  0.3714  -0.0827 41  GLU A CG  
314  C CD  A GLU A 41  ? 1.0790 0.5127 0.8904 0.1271  0.3864  -0.0960 41  GLU A CD  
315  C CD  B GLU A 41  ? 1.0524 0.4689 0.8785 0.1358  0.3655  -0.0764 41  GLU A CD  
316  O OE1 A GLU A 41  ? 1.0499 0.5127 0.8725 0.1290  0.3956  -0.0985 41  GLU A OE1 
317  O OE1 B GLU A 41  ? 1.0362 0.4691 0.8881 0.1488  0.3560  -0.0620 41  GLU A OE1 
318  O OE2 A GLU A 41  ? 1.1470 0.5552 0.9519 0.1299  0.3908  -0.1053 41  GLU A OE2 
319  O OE2 B GLU A 41  ? 1.1058 0.4934 0.9194 0.1351  0.3698  -0.0858 41  GLU A OE2 
320  N N   . TYR A 42  ? 1.0333 0.5074 0.8086 0.0783  0.3379  -0.0614 42  TYR A N   
321  C CA  . TYR A 42  ? 0.9861 0.4503 0.7395 0.0600  0.3243  -0.0626 42  TYR A CA  
322  C C   . TYR A 42  ? 0.9561 0.4497 0.7138 0.0524  0.3095  -0.0511 42  TYR A C   
323  O O   . TYR A 42  ? 0.9012 0.4190 0.6819 0.0607  0.3078  -0.0398 42  TYR A O   
324  C CB  . TYR A 42  ? 0.9853 0.4297 0.7451 0.0583  0.3177  -0.0600 42  TYR A CB  
325  C CG  . TYR A 42  ? 1.0545 0.4638 0.8109 0.0676  0.3312  -0.0690 42  TYR A CG  
326  C CD1 . TYR A 42  ? 1.0065 0.3852 0.7353 0.0580  0.3389  -0.0861 42  TYR A CD1 
327  C CD2 . TYR A 42  ? 1.0267 0.4310 0.8057 0.0862  0.3350  -0.0606 42  TYR A CD2 
328  C CE1 . TYR A 42  ? 1.1136 0.4588 0.8396 0.0665  0.3509  -0.0945 42  TYR A CE1 
329  C CE2 . TYR A 42  ? 1.1251 0.5020 0.9033 0.0951  0.3424  -0.0663 42  TYR A CE2 
330  C CZ  . TYR A 42  ? 1.1204 0.4712 0.8740 0.0846  0.3496  -0.0824 42  TYR A CZ  
331  O OH  . TYR A 42  ? 1.1861 0.5143 0.9409 0.0923  0.3544  -0.0869 42  TYR A OH  
332  N N   . ILE A 43  ? 0.9283 0.4188 0.6639 0.0367  0.2978  -0.0547 43  ILE A N   
333  C CA  . ILE A 43  ? 0.9376 0.4509 0.6764 0.0301  0.2813  -0.0446 43  ILE A CA  
334  C C   . ILE A 43  ? 0.9242 0.4354 0.6670 0.0196  0.2657  -0.0456 43  ILE A C   
335  O O   . ILE A 43  ? 0.9264 0.4196 0.6496 0.0089  0.2628  -0.0572 43  ILE A O   
336  C CB  . ILE A 43  ? 0.9157 0.4297 0.6243 0.0221  0.2797  -0.0472 43  ILE A CB  
337  C CG1 . ILE A 43  ? 0.9316 0.4496 0.6384 0.0299  0.2991  -0.0481 43  ILE A CG1 
338  C CG2 . ILE A 43  ? 0.8642 0.3969 0.5767 0.0174  0.2607  -0.0359 43  ILE A CG2 
339  C CD1 . ILE A 43  ? 0.9649 0.4789 0.6360 0.0200  0.3012  -0.0500 43  ILE A CD1 
340  N N   . HIS A 44  ? 0.8730 0.4035 0.6418 0.0216  0.2567  -0.0350 44  HIS A N   
341  C CA  . HIS A 44  ? 0.8249 0.3586 0.6059 0.0121  0.2453  -0.0363 44  HIS A CA  
342  C C   . HIS A 44  ? 0.8437 0.4033 0.6363 0.0094  0.2291  -0.0294 44  HIS A C   
343  O O   . HIS A 44  ? 0.7699 0.3461 0.5793 0.0172  0.2292  -0.0187 44  HIS A O   
344  C CB  . HIS A 44  ? 0.8311 0.3596 0.6321 0.0170  0.2528  -0.0312 44  HIS A CB  
345  C CG  . HIS A 44  ? 0.8923 0.4228 0.7058 0.0049  0.2461  -0.0339 44  HIS A CG  
346  N ND1 . HIS A 44  ? 0.9585 0.5140 0.7941 0.0026  0.2374  -0.0276 44  HIS A ND1 
347  C CD2 . HIS A 44  ? 0.8932 0.4037 0.7018 -0.0066 0.2489  -0.0435 44  HIS A CD2 
348  C CE1 . HIS A 44  ? 0.8327 0.3866 0.6785 -0.0099 0.2359  -0.0337 44  HIS A CE1 
349  N NE2 . HIS A 44  ? 0.8327 0.3593 0.6619 -0.0166 0.2425  -0.0430 44  HIS A NE2 
350  N N   . ILE A 45  ? 0.8154 0.3776 0.5993 -0.0010 0.2143  -0.0360 45  ILE A N   
351  C CA  . ILE A 45  ? 0.8557 0.4395 0.6500 -0.0017 0.1963  -0.0305 45  ILE A CA  
352  C C   . ILE A 45  ? 0.8398 0.4404 0.6673 -0.0068 0.1897  -0.0328 45  ILE A C   
353  O O   . ILE A 45  ? 0.7918 0.3924 0.6226 -0.0179 0.1820  -0.0435 45  ILE A O   
354  C CB  . ILE A 45  ? 0.8757 0.4535 0.6415 -0.0086 0.1810  -0.0357 45  ILE A CB  
355  C CG1 . ILE A 45  ? 0.8528 0.4107 0.5814 -0.0066 0.1925  -0.0355 45  ILE A CG1 
356  C CG2 . ILE A 45  ? 0.8511 0.4483 0.6284 -0.0060 0.1606  -0.0282 45  ILE A CG2 
357  C CD1 . ILE A 45  ? 0.9370 0.4828 0.6271 -0.0151 0.1786  -0.0403 45  ILE A CD1 
358  N N   . CYS A 46  ? 0.8823 0.4981 0.7344 0.0000  0.1933  -0.0240 46  CYS A N   
359  C CA  . CYS A 46  ? 0.7904 0.4214 0.6733 -0.0055 0.1924  -0.0267 46  CYS A CA  
360  C C   . CYS A 46  ? 0.8331 0.4845 0.7330 -0.0116 0.1732  -0.0338 46  CYS A C   
361  O O   . CYS A 46  ? 0.7842 0.4428 0.6782 -0.0064 0.1582  -0.0303 46  CYS A O   
362  C CB  . CYS A 46  ? 0.7010 0.3439 0.6016 0.0028  0.1990  -0.0164 46  CYS A CB  
363  S SG  . CYS A 46  ? 0.8001 0.4250 0.6865 0.0119  0.2168  -0.0075 46  CYS A SG  
364  N N   . ASP A 47  ? 0.8155 0.4757 0.7373 -0.0230 0.1735  -0.0439 47  ASP A N   
365  C CA  . ASP A 47  ? 0.8413 0.5283 0.7911 -0.0284 0.1557  -0.0525 47  ASP A CA  
366  C C   . ASP A 47  ? 0.7651 0.4766 0.7559 -0.0302 0.1616  -0.0545 47  ASP A C   
367  O O   . ASP A 47  ? 0.7836 0.5223 0.8070 -0.0345 0.1490  -0.0638 47  ASP A O   
368  C CB  . ASP A 47  ? 0.8171 0.4995 0.7617 -0.0438 0.1487  -0.0671 47  ASP A CB  
369  C CG  . ASP A 47  ? 0.8390 0.5105 0.7909 -0.0576 0.1675  -0.0747 47  ASP A CG  
370  O OD1 . ASP A 47  ? 0.8284 0.4961 0.7886 -0.0553 0.1847  -0.0680 47  ASP A OD1 
371  O OD2 . ASP A 47  ? 0.9179 0.5817 0.8639 -0.0722 0.1646  -0.0874 47  ASP A OD2 
372  N N   . GLY A 48  ? 0.8040 0.5076 0.7945 -0.0273 0.1803  -0.0470 48  GLY A N   
373  C CA  . GLY A 48  ? 0.7899 0.5130 0.8124 -0.0298 0.1891  -0.0489 48  GLY A CA  
374  C C   . GLY A 48  ? 0.8141 0.5440 0.8572 -0.0478 0.1987  -0.0616 48  GLY A C   
375  O O   . GLY A 48  ? 0.7650 0.5116 0.8344 -0.0522 0.2090  -0.0649 48  GLY A O   
376  N N   . SER A 49  ? 0.7634 0.4793 0.7940 -0.0598 0.1978  -0.0697 49  SER A N   
377  C CA  . SER A 49  ? 0.8541 0.5774 0.9060 -0.0800 0.2061  -0.0836 49  SER A CA  
378  C C   . SER A 49  ? 0.8251 0.5272 0.8673 -0.0883 0.2314  -0.0790 49  SER A C   
379  O O   . SER A 49  ? 0.8623 0.5366 0.8741 -0.0788 0.2404  -0.0654 49  SER A O   
380  C CB  . SER A 49  ? 0.8420 0.5497 0.8770 -0.0920 0.1992  -0.0935 49  SER A CB  
381  O OG  . SER A 49  ? 0.8616 0.5266 0.8537 -0.0893 0.2105  -0.0857 49  SER A OG  
382  N N   . GLU A 50  ? 0.8449 0.5608 0.9136 -0.1069 0.2426  -0.0907 50  GLU A N   
383  C CA  . GLU A 50  ? 0.9382 0.6280 0.9912 -0.1190 0.2672  -0.0867 50  GLU A CA  
384  C C   . GLU A 50  ? 1.0207 0.6623 1.0314 -0.1235 0.2741  -0.0817 50  GLU A C   
385  O O   . GLU A 50  ? 0.9809 0.5885 0.9618 -0.1209 0.2880  -0.0693 50  GLU A O   
386  C CB  . GLU A 50  ? 0.9792 0.6928 1.0683 -0.1418 0.2795  -0.1026 50  GLU A CB  
387  C CG  . GLU A 50  ? 1.0834 0.8435 1.2178 -0.1368 0.2775  -0.1090 50  GLU A CG  
388  C CD  . GLU A 50  ? 1.2729 1.0233 1.3936 -0.1300 0.2937  -0.0975 50  GLU A CD  
389  O OE1 . GLU A 50  ? 1.3038 1.0128 1.3811 -0.1309 0.3057  -0.0843 50  GLU A OE1 
390  O OE2 . GLU A 50  ? 1.2628 1.0460 1.4158 -0.1234 0.2934  -0.1021 50  GLU A OE2 
391  N N   . GLU A 51  ? 0.9673 0.6037 0.9739 -0.1298 0.2636  -0.0916 51  GLU A N   
392  C CA  . GLU A 51  ? 0.9102 0.4990 0.8772 -0.1322 0.2700  -0.0887 51  GLU A CA  
393  C C   . GLU A 51  ? 1.0075 0.5736 0.9439 -0.1082 0.2683  -0.0721 51  GLU A C   
394  O O   . GLU A 51  ? 0.9950 0.5227 0.9033 -0.1045 0.2809  -0.0622 51  GLU A O   
395  C CB  . GLU A 51  ? 0.9194 0.5098 0.8868 -0.1424 0.2572  -0.1042 51  GLU A CB  
396  C CG  . GLU A 51  ? 1.1287 0.7355 1.1243 -0.1699 0.2606  -0.1226 51  GLU A CG  
397  C CD  . GLU A 51  ? 1.1638 0.8272 1.2108 -0.1725 0.2523  -0.1304 51  GLU A CD  
398  O OE1 . GLU A 51  ? 1.0036 0.6914 1.0616 -0.1521 0.2399  -0.1223 51  GLU A OE1 
399  O OE2 . GLU A 51  ? 1.2623 0.9455 1.3404 -0.1951 0.2590  -0.1456 51  GLU A OE2 
400  N N   . GLU A 52  ? 0.9706 0.5600 0.9126 -0.0919 0.2522  -0.0689 52  GLU A N   
401  C CA  . GLU A 52  ? 0.9320 0.5079 0.8517 -0.0706 0.2514  -0.0545 52  GLU A CA  
402  C C   . GLU A 52  ? 0.9667 0.5334 0.8819 -0.0643 0.2638  -0.0410 52  GLU A C   
403  O O   . GLU A 52  ? 0.9696 0.5046 0.8598 -0.0560 0.2716  -0.0314 52  GLU A O   
404  C CB  . GLU A 52  ? 0.7972 0.4033 0.7277 -0.0580 0.2341  -0.0530 52  GLU A CB  
405  C CG  . GLU A 52  ? 0.8015 0.4041 0.7186 -0.0385 0.2344  -0.0385 52  GLU A CG  
406  C CD  . GLU A 52  ? 0.8017 0.4268 0.7235 -0.0290 0.2183  -0.0373 52  GLU A CD  
407  O OE1 . GLU A 52  ? 0.8078 0.4244 0.7114 -0.0283 0.2107  -0.0415 52  GLU A OE1 
408  O OE2 . GLU A 52  ? 0.8672 0.5153 0.8080 -0.0231 0.2137  -0.0323 52  GLU A OE2 
409  N N   . TYR A 53  ? 0.9293 0.5234 0.8686 -0.0679 0.2652  -0.0408 53  TYR A N   
410  C CA  . TYR A 53  ? 0.9363 0.5209 0.8676 -0.0654 0.2771  -0.0295 53  TYR A CA  
411  C C   . TYR A 53  ? 0.9774 0.5201 0.8826 -0.0760 0.2921  -0.0261 53  TYR A C   
412  O O   . TYR A 53  ? 0.9817 0.4992 0.8629 -0.0670 0.2974  -0.0124 53  TYR A O   
413  C CB  . TYR A 53  ? 0.8813 0.4993 0.8430 -0.0732 0.2801  -0.0351 53  TYR A CB  
414  C CG  . TYR A 53  ? 0.9170 0.5314 0.8692 -0.0681 0.2889  -0.0240 53  TYR A CG  
415  C CD1 . TYR A 53  ? 0.9378 0.5505 0.8770 -0.0494 0.2816  -0.0116 53  TYR A CD1 
416  C CD2 . TYR A 53  ? 0.8916 0.5054 0.8473 -0.0837 0.3049  -0.0271 53  TYR A CD2 
417  C CE1 . TYR A 53  ? 0.9058 0.5158 0.8348 -0.0460 0.2876  -0.0024 53  TYR A CE1 
418  C CE2 . TYR A 53  ? 0.8915 0.5000 0.8331 -0.0804 0.3124  -0.0177 53  TYR A CE2 
419  C CZ  . TYR A 53  ? 0.9391 0.5458 0.8673 -0.0613 0.3025  -0.0053 53  TYR A CZ  
420  O OH  . TYR A 53  ? 0.8412 0.4429 0.7537 -0.0592 0.3080  0.0031  53  TYR A OH  
421  N N   . GLY A 54  ? 0.9660 0.4991 0.8747 -0.0953 0.2980  -0.0382 54  GLY A N   
422  C CA  . GLY A 54  ? 1.0702 0.5578 0.9518 -0.1077 0.3130  -0.0355 54  GLY A CA  
423  C C   . GLY A 54  ? 1.1559 0.6019 1.0051 -0.0928 0.3115  -0.0265 54  GLY A C   
424  O O   . GLY A 54  ? 1.0786 0.4920 0.9022 -0.0852 0.3179  -0.0123 54  GLY A O   
425  N N   . ARG A 55  ? 1.1971 0.6433 1.0466 -0.0881 0.3027  -0.0351 55  ARG A N   
426  C CA  . ARG A 55  ? 1.2175 0.6273 1.0406 -0.0724 0.3030  -0.0292 55  ARG A CA  
427  C C   . ARG A 55  ? 1.2140 0.6298 1.0328 -0.0480 0.2983  -0.0134 55  ARG A C   
428  O O   . ARG A 55  ? 1.2528 0.6353 1.0512 -0.0347 0.3019  -0.0035 55  ARG A O   
429  C CB  . ARG A 55  ? 1.2310 0.6457 1.0547 -0.0717 0.2949  -0.0427 55  ARG A CB  
430  C CG  . ARG A 55  ? 1.2776 0.6977 1.1111 -0.0965 0.2943  -0.0607 55  ARG A CG  
431  C CD  . ARG A 55  ? 1.5382 0.9145 1.3551 -0.1151 0.3097  -0.0641 55  ARG A CD  
432  N NE  . ARG A 55  ? 1.4950 0.8199 1.2804 -0.1059 0.3162  -0.0621 55  ARG A NE  
433  C CZ  . ARG A 55  ? 1.4523 0.7364 1.2154 -0.0991 0.3261  -0.0493 55  ARG A CZ  
434  N NH1 . ARG A 55  ? 1.4198 0.7078 1.1831 -0.1024 0.3305  -0.0369 55  ARG A NH1 
435  N NH2 . ARG A 55  ? 1.4056 0.6608 1.1480 -0.0864 0.3262  -0.0485 55  ARG A NH2 
436  N N   . LEU A 56  ? 1.0542 0.5123 0.8938 -0.0418 0.2896  -0.0113 56  LEU A N   
437  C CA  . LEU A 56  ? 0.9934 0.4613 0.8317 -0.0213 0.2848  0.0020  56  LEU A CA  
438  C C   . LEU A 56  ? 1.0908 0.5357 0.9131 -0.0189 0.2911  0.0158  56  LEU A C   
439  O O   . LEU A 56  ? 1.1196 0.5453 0.9282 -0.0022 0.2895  0.0264  56  LEU A O   
440  C CB  . LEU A 56  ? 0.9952 0.5083 0.8572 -0.0190 0.2756  0.0007  56  LEU A CB  
441  C CG  . LEU A 56  ? 0.9666 0.4938 0.8299 -0.0010 0.2703  0.0124  56  LEU A CG  
442  C CD1 . LEU A 56  ? 0.9776 0.4964 0.8327 0.0145  0.2678  0.0135  56  LEU A CD1 
443  C CD2 . LEU A 56  ? 0.9488 0.5144 0.8337 -0.0016 0.2628  0.0103  56  LEU A CD2 
444  N N   . LEU A 57  ? 1.0490 0.4962 0.8728 -0.0356 0.2982  0.0155  57  LEU A N   
445  C CA  . LEU A 57  ? 1.1007 0.5211 0.9011 -0.0365 0.3047  0.0289  57  LEU A CA  
446  C C   . LEU A 57  ? 1.1456 0.5123 0.9162 -0.0340 0.3098  0.0353  57  LEU A C   
447  O O   . LEU A 57  ? 1.2313 0.5821 0.9841 -0.0181 0.3037  0.0488  57  LEU A O   
448  C CB  . LEU A 57  ? 1.1007 0.5299 0.9056 -0.0591 0.3157  0.0242  57  LEU A CB  
449  C CG  . LEU A 57  ? 1.0781 0.5543 0.9094 -0.0591 0.3122  0.0204  57  LEU A CG  
450  C CD1 . LEU A 57  ? 0.9432 0.4299 0.7852 -0.0827 0.3262  0.0108  57  LEU A CD1 
451  C CD2 . LEU A 57  ? 0.9493 0.4269 0.7674 -0.0436 0.3061  0.0347  57  LEU A CD2 
452  N N   . ALA A 58  ? 1.1593 0.5082 0.9275 -0.0483 0.3164  0.0239  58  ALA A N   
453  C CA  . ALA A 58  ? 1.2659 0.5774 1.0093 -0.0447 0.3167  0.0270  58  ALA A CA  
454  C C   . ALA A 58  ? 1.2163 0.5210 0.9569 -0.0170 0.3068  0.0335  58  ALA A C   
455  O O   . ALA A 58  ? 1.2697 0.5489 0.9914 -0.0045 0.3026  0.0447  58  ALA A O   
456  C CB  . ALA A 58  ? 1.2843 0.5826 1.0293 -0.0645 0.3244  0.0108  58  ALA A CB  
457  N N   . HIS A 59  ? 1.1481 0.4750 0.9081 -0.0072 0.3032  0.0261  59  HIS A N   
458  C CA  . HIS A 59  ? 1.1909 0.5175 0.9531 0.0182  0.2965  0.0301  59  HIS A CA  
459  C C   . HIS A 59  ? 1.2234 0.5568 0.9844 0.0356  0.2884  0.0468  59  HIS A C   
460  O O   . HIS A 59  ? 1.2128 0.5288 0.9660 0.0531  0.2830  0.0549  59  HIS A O   
461  C CB  . HIS A 59  ? 1.2166 0.5680 0.9971 0.0226  0.2958  0.0190  59  HIS A CB  
462  C CG  . HIS A 59  ? 1.2609 0.6168 1.0468 0.0464  0.2924  0.0203  59  HIS A CG  
463  N ND1 . HIS A 59  ? 1.2135 0.5447 0.9903 0.0566  0.2941  0.0180  59  HIS A ND1 
464  C CD2 . HIS A 59  ? 1.2587 0.6475 1.0615 0.0606  0.2873  0.0223  59  HIS A CD2 
465  C CE1 . HIS A 59  ? 1.2806 0.6260 1.0700 0.0769  0.2925  0.0179  59  HIS A CE1 
466  N NE2 . HIS A 59  ? 1.3373 0.7144 1.1414 0.0793  0.2898  0.0205  59  HIS A NE2 
467  N N   . MET A 60  ? 1.2108 0.5688 0.9802 0.0312  0.2869  0.0517  60  MET A N   
468  C CA  . MET A 60  ? 1.1604 0.5247 0.9267 0.0454  0.2786  0.0668  60  MET A CA  
469  C C   . MET A 60  ? 1.1747 0.5063 0.9127 0.0445  0.2758  0.0788  60  MET A C   
470  O O   . MET A 60  ? 1.1943 0.5184 0.9257 0.0627  0.2654  0.0914  60  MET A O   
471  C CB  . MET A 60  ? 1.1403 0.5435 0.9199 0.0365  0.2764  0.0667  60  MET A CB  
472  C CG  . MET A 60  ? 1.0039 0.4515 0.8112 0.0456  0.2698  0.0602  60  MET A CG  
473  S SD  . MET A 60  ? 0.9677 0.4566 0.7890 0.0367  0.2662  0.0604  60  MET A SD  
474  C CE  . MET A 60  ? 0.9540 0.4499 0.7841 0.0135  0.2749  0.0461  60  MET A CE  
475  N N   . GLN A 61  ? 1.1934 0.5047 0.9145 0.0234  0.2845  0.0751  61  GLN A N   
476  C CA  . GLN A 61  ? 1.2694 0.5451 0.9584 0.0203  0.2828  0.0866  61  GLN A CA  
477  C C   . GLN A 61  ? 1.3883 0.6313 1.0673 0.0357  0.2773  0.0897  61  GLN A C   
478  O O   . GLN A 61  ? 1.4070 0.6229 1.0641 0.0462  0.2684  0.1038  61  GLN A O   
479  C CB  . GLN A 61  ? 1.2506 0.5160 0.9263 -0.0089 0.2963  0.0800  61  GLN A CB  
480  C CG  . GLN A 61  ? 1.2051 0.4330 0.8429 -0.0160 0.2965  0.0918  61  GLN A CG  
481  C CD  . GLN A 61  ? 1.3296 0.5497 0.9577 -0.0463 0.3128  0.0825  61  GLN A CD  
482  O OE1 . GLN A 61  ? 1.2841 0.5210 0.9348 -0.0605 0.3226  0.0666  61  GLN A OE1 
483  N NE2 . GLN A 61  ? 1.2613 0.4560 0.8557 -0.0571 0.3158  0.0919  61  GLN A NE2 
484  N N   . GLU A 62  ? 1.4041 0.6477 1.0978 0.0373  0.2822  0.0764  62  GLU A N   
485  C CA  . GLU A 62  ? 1.3872 0.6026 1.0759 0.0536  0.2784  0.0767  62  GLU A CA  
486  C C   . GLU A 62  ? 1.3785 0.6085 1.0853 0.0836  0.2668  0.0829  62  GLU A C   
487  O O   . GLU A 62  ? 1.4523 0.6589 1.1565 0.1014  0.2611  0.0864  62  GLU A O   
488  C CB  . GLU A 62  ? 1.3039 0.5155 1.0004 0.0436  0.2887  0.0585  62  GLU A CB  
489  C CG  . GLU A 62  ? 1.3402 0.5389 1.0237 0.0132  0.3001  0.0501  62  GLU A CG  
490  C CD  . GLU A 62  ? 1.2394 0.4437 0.9345 0.0012  0.3080  0.0306  62  GLU A CD  
491  O OE1 . GLU A 62  ? 1.2214 0.4370 0.9302 0.0163  0.3056  0.0237  62  GLU A OE1 
492  O OE2 . GLU A 62  ? 1.3139 0.5119 1.0042 -0.0242 0.3168  0.0213  62  GLU A OE2 
493  N N   . GLU A 63  ? 1.3036 0.5720 1.0309 0.0896  0.2636  0.0836  63  GLU A N   
494  C CA  . GLU A 63  ? 1.3427 0.6309 1.0916 0.1162  0.2539  0.0883  63  GLU A CA  
495  C C   . GLU A 63  ? 1.3828 0.6706 1.1228 0.1263  0.2404  0.1064  63  GLU A C   
496  O O   . GLU A 63  ? 1.4002 0.7091 1.1610 0.1474  0.2314  0.1108  63  GLU A O   
497  C CB  . GLU A 63  ? 1.2739 0.6033 1.0504 0.1164  0.2593  0.0773  63  GLU A CB  
498  C CG  . GLU A 63  ? 1.3774 0.7079 1.1615 0.1104  0.2701  0.0596  63  GLU A CG  
499  C CD  . GLU A 63  ? 1.4206 0.7446 1.2164 0.1316  0.2698  0.0545  63  GLU A CD  
500  O OE1 . GLU A 63  ? 1.4564 0.7559 1.2456 0.1455  0.2625  0.0633  63  GLU A OE1 
501  O OE2 . GLU A 63  ? 1.4256 0.7682 1.2368 0.1345  0.2771  0.0414  63  GLU A OE2 
502  N N   . GLY A 64  ? 1.3629 0.6278 1.0721 0.1108  0.2394  0.1160  64  GLY A N   
503  C CA  . GLY A 64  ? 1.2864 0.5489 0.9801 0.1171  0.2265  0.1329  64  GLY A CA  
504  C C   . GLY A 64  ? 1.3213 0.6220 1.0303 0.1148  0.2262  0.1332  64  GLY A C   
505  O O   . GLY A 64  ? 1.3881 0.6916 1.0896 0.1249  0.2136  0.1464  64  GLY A O   
506  N N   . VAL A 65  ? 1.2483 0.5768 0.9772 0.1018  0.2387  0.1192  65  VAL A N   
507  C CA  . VAL A 65  ? 1.2014 0.5736 0.9490 0.0984  0.2366  0.1169  65  VAL A CA  
508  C C   . VAL A 65  ? 1.2375 0.6068 0.9611 0.0783  0.2391  0.1222  65  VAL A C   
509  O O   . VAL A 65  ? 1.2710 0.6589 0.9917 0.0810  0.2288  0.1293  65  VAL A O   
510  C CB  . VAL A 65  ? 1.2090 0.6159 0.9863 0.0918  0.2453  0.0996  65  VAL A CB  
511  C CG1 . VAL A 65  ? 1.0396 0.4932 0.8345 0.0850  0.2418  0.0962  65  VAL A CG1 
512  C CG2 . VAL A 65  ? 1.2166 0.6296 1.0155 0.1114  0.2441  0.0937  65  VAL A CG2 
513  N N   . ILE A 66  ? 1.2156 0.5626 0.9225 0.0566  0.2538  0.1173  66  ILE A N   
514  C CA  . ILE A 66  ? 1.2208 0.5672 0.9078 0.0352  0.2609  0.1188  66  ILE A CA  
515  C C   . ILE A 66  ? 1.2185 0.5279 0.8724 0.0213  0.2657  0.1217  66  ILE A C   
516  O O   . ILE A 66  ? 1.2602 0.5490 0.9129 0.0224  0.2678  0.1179  66  ILE A O   
517  C CB  . ILE A 66  ? 1.1686 0.5537 0.8830 0.0182  0.2718  0.1022  66  ILE A CB  
518  C CG1 . ILE A 66  ? 1.1077 0.4831 0.8328 0.0081  0.2831  0.0899  66  ILE A CG1 
519  C CG2 . ILE A 66  ? 1.1258 0.5599 0.8737 0.0304  0.2619  0.0969  66  ILE A CG2 
520  C CD1 . ILE A 66  ? 1.0812 0.4960 0.8362 -0.0063 0.2899  0.0736  66  ILE A CD1 
521  N N   . ARG A 67  ? 1.2668 0.5666 0.8920 0.0070  0.2684  0.1278  67  ARG A N   
522  C CA  . ARG A 67  ? 1.1596 0.4259 0.7509 -0.0107 0.2759  0.1296  67  ARG A CA  
523  C C   . ARG A 67  ? 1.1334 0.4174 0.7333 -0.0382 0.2961  0.1143  67  ARG A C   
524  O O   . ARG A 67  ? 1.1783 0.4976 0.8025 -0.0431 0.3018  0.1060  67  ARG A O   
525  C CB  . ARG A 67  ? 1.2579 0.4974 0.8059 -0.0083 0.2649  0.1471  67  ARG A CB  
526  C CG  . ARG A 67  ? 1.4345 0.6505 0.9717 0.0187  0.2433  0.1634  67  ARG A CG  
527  C CD  . ARG A 67  ? 1.5780 0.7653 1.0682 0.0191  0.2303  0.1813  67  ARG A CD  
528  N NE  . ARG A 67  ? 1.5969 0.7493 1.0480 -0.0029 0.2407  0.1827  67  ARG A NE  
529  C CZ  . ARG A 67  ? 1.7632 0.8725 1.1887 0.0015  0.2345  0.1923  67  ARG A CZ  
530  N NH1 . ARG A 67  ? 1.8536 0.9498 1.2906 0.0281  0.2176  0.2006  67  ARG A NH1 
531  N NH2 . ARG A 67  ? 1.7457 0.8241 1.1345 -0.0213 0.2465  0.1927  67  ARG A NH2 
532  N N   . LYS A 68  ? 1.1817 0.4407 0.7636 -0.0560 0.3073  0.1101  68  LYS A N   
533  C CA  . LYS A 68  ? 1.1999 0.4738 0.7896 -0.0832 0.3274  0.0952  68  LYS A CA  
534  C C   . LYS A 68  ? 1.2110 0.4687 0.7619 -0.0974 0.3328  0.1013  68  LYS A C   
535  O O   . LYS A 68  ? 1.2352 0.4523 0.7444 -0.0959 0.3264  0.1149  68  LYS A O   
536  C CB  . LYS A 68  ? 1.1833 0.4418 0.7780 -0.0977 0.3387  0.0845  68  LYS A CB  
537  C CG  . LYS A 68  ? 1.1449 0.4306 0.7643 -0.1236 0.3587  0.0654  68  LYS A CG  
538  C CD  . LYS A 68  ? 1.1875 0.4595 0.8138 -0.1389 0.3687  0.0542  68  LYS A CD  
539  C CE  . LYS A 68  ? 1.2586 0.5709 0.9288 -0.1579 0.3830  0.0331  68  LYS A CE  
540  N NZ  . LYS A 68  ? 1.3284 0.6632 1.0025 -0.1742 0.3967  0.0263  68  LYS A NZ  
541  N N   . LEU A 69  ? 1.1692 0.4575 0.7331 -0.1108 0.3445  0.0910  69  LEU A N   
542  C CA  . LEU A 69  ? 1.2367 0.5132 0.7651 -0.1272 0.3532  0.0927  69  LEU A CA  
543  C C   . LEU A 69  ? 1.2920 0.5604 0.8184 -0.1535 0.3745  0.0792  69  LEU A C   
544  O O   . LEU A 69  ? 1.2808 0.5827 0.8411 -0.1687 0.3912  0.0607  69  LEU A O   
545  C CB  . LEU A 69  ? 1.1473 0.4602 0.6918 -0.1282 0.3565  0.0862  69  LEU A CB  
546  C CG  . LEU A 69  ? 1.2229 0.5451 0.7712 -0.1038 0.3361  0.0987  69  LEU A CG  
547  C CD1 . LEU A 69  ? 1.0695 0.4337 0.6479 -0.1046 0.3416  0.0881  69  LEU A CD1 
548  C CD2 . LEU A 69  ? 1.2714 0.5576 0.7668 -0.0964 0.3205  0.1186  69  LEU A CD2 
549  N N   . LYS A 70  ? 1.4325 0.6558 0.9203 -0.1586 0.3738  0.0886  70  LYS A N   
550  C CA  . LYS A 70  ? 1.4520 0.6631 0.9367 -0.1836 0.3939  0.0765  70  LYS A CA  
551  C C   . LYS A 70  ? 1.4530 0.6794 0.9336 -0.2080 0.4148  0.0633  70  LYS A C   
552  O O   . LYS A 70  ? 1.4733 0.7082 0.9706 -0.2298 0.4345  0.0469  70  LYS A O   
553  C CB  . LYS A 70  ? 1.5100 0.6638 0.9468 -0.1838 0.3884  0.0914  70  LYS A CB  
554  C CG  . LYS A 70  ? 1.6518 0.7709 1.0347 -0.1752 0.3747  0.1122  70  LYS A CG  
555  C CD  . LYS A 70  ? 1.7630 0.8231 1.0978 -0.1791 0.3721  0.1258  70  LYS A CD  
556  C CE  . LYS A 70  ? 1.7477 0.7722 1.0248 -0.1758 0.3604  0.1453  70  LYS A CE  
557  N NZ  . LYS A 70  ? 1.8006 0.7647 1.0274 -0.1826 0.3600  0.1582  70  LYS A NZ  
558  N N   . LYS A 71  ? 1.4066 0.6379 0.8670 -0.2052 0.4115  0.0686  71  LYS A N   
559  C CA  . LYS A 71  ? 1.3462 0.5883 0.7988 -0.2281 0.4323  0.0552  71  LYS A CA  
560  C C   . LYS A 71  ? 1.3117 0.6098 0.8260 -0.2355 0.4474  0.0314  71  LYS A C   
561  O O   . LYS A 71  ? 1.3036 0.6143 0.8254 -0.2574 0.4692  0.0146  71  LYS A O   
562  C CB  . LYS A 71  ? 1.3939 0.6226 0.8037 -0.2233 0.4236  0.0672  71  LYS A CB  
563  C CG  . LYS A 71  ? 1.3983 0.6348 0.7952 -0.2464 0.4453  0.0528  71  LYS A CG  
564  C CD  . LYS A 71  ? 1.4387 0.6509 0.7810 -0.2436 0.4350  0.0669  71  LYS A CD  
565  C CE  . LYS A 71  ? 1.5116 0.7257 0.8353 -0.2680 0.4581  0.0518  71  LYS A CE  
566  N NZ  . LYS A 71  ? 1.7124 0.8892 0.9681 -0.2698 0.4483  0.0673  71  LYS A NZ  
567  N N   . TYR A 72  ? 1.2758 0.6073 0.8349 -0.2179 0.4365  0.0292  72  TYR A N   
568  C CA  . TYR A 72  ? 1.2667 0.6513 0.8851 -0.2217 0.4475  0.0086  72  TYR A CA  
569  C C   . TYR A 72  ? 1.2228 0.6268 0.8879 -0.2213 0.4475  -0.0007 72  TYR A C   
570  O O   . TYR A 72  ? 1.2931 0.6688 0.9433 -0.2184 0.4401  0.0078  72  TYR A O   
571  C CB  . TYR A 72  ? 1.1491 0.5583 0.7805 -0.2033 0.4359  0.0125  72  TYR A CB  
572  C CG  . TYR A 72  ? 1.1578 0.5449 0.7389 -0.2031 0.4323  0.0231  72  TYR A CG  
573  C CD1 . TYR A 72  ? 1.1890 0.5784 0.7563 -0.2223 0.4508  0.0110  72  TYR A CD1 
574  C CD2 . TYR A 72  ? 1.1645 0.5285 0.7122 -0.1842 0.4102  0.0444  72  TYR A CD2 
575  C CE1 . TYR A 72  ? 1.2276 0.5945 0.7449 -0.2238 0.4472  0.0201  72  TYR A CE1 
576  C CE2 . TYR A 72  ? 1.2015 0.5456 0.7020 -0.1853 0.4051  0.0541  72  TYR A CE2 
577  C CZ  . TYR A 72  ? 1.2614 0.6058 0.7446 -0.2056 0.4236  0.0420  72  TYR A CZ  
578  O OH  . TYR A 72  ? 1.2783 0.6008 0.7106 -0.2081 0.4182  0.0511  72  TYR A OH  
579  N N   . ASP A 73  ? 1.1340 0.5865 0.8564 -0.2242 0.4555  -0.0189 73  ASP A N   
580  C CA  . ASP A 73  ? 1.1491 0.6260 0.9205 -0.2268 0.4559  -0.0305 73  ASP A CA  
581  C C   . ASP A 73  ? 1.1222 0.6115 0.9143 -0.2031 0.4368  -0.0218 73  ASP A C   
582  O O   . ASP A 73  ? 1.0916 0.6138 0.9132 -0.1936 0.4347  -0.0260 73  ASP A O   
583  C CB  . ASP A 73  ? 1.1918 0.7165 1.0177 -0.2434 0.4740  -0.0558 73  ASP A CB  
584  C CG  . ASP A 73  ? 1.2608 0.8128 1.1389 -0.2496 0.4736  -0.0692 73  ASP A CG  
585  O OD1 . ASP A 73  ? 1.2411 0.7842 1.1219 -0.2364 0.4577  -0.0600 73  ASP A OD1 
586  O OD2 . ASP A 73  ? 1.3432 0.9266 1.2607 -0.2681 0.4889  -0.0902 73  ASP A OD2 
587  N N   . ASN A 74  ? 1.0673 0.5287 0.8433 -0.1935 0.4236  -0.0105 74  ASN A N   
588  C CA  . ASN A 74  ? 1.0401 0.5099 0.8352 -0.1725 0.4067  -0.0039 74  ASN A CA  
589  C C   . ASN A 74  ? 0.9445 0.4197 0.7286 -0.1528 0.3957  0.0085  74  ASN A C   
590  O O   . ASN A 74  ? 0.9369 0.4457 0.7555 -0.1417 0.3892  0.0041  74  ASN A O   
591  C CB  . ASN A 74  ? 0.9909 0.5014 0.8452 -0.1790 0.4104  -0.0213 74  ASN A CB  
592  C CG  . ASN A 74  ? 1.0765 0.6008 0.9474 -0.1537 0.3853  -0.0175 74  ASN A CG  
593  O OD1 . ASN A 74  ? 1.0913 0.5834 0.9312 -0.1389 0.3741  -0.0025 74  ASN A OD1 
594  N ND2 . ASN A 74  ? 1.0563 0.6288 0.9761 -0.1479 0.3758  -0.0317 74  ASN A ND2 
595  N N   . CYS A 75  ? 0.9981 0.4420 0.7340 -0.1474 0.3902  0.0233  75  CYS A N   
596  C CA  . CYS A 75  ? 0.9809 0.4260 0.7012 -0.1301 0.3780  0.0358  75  CYS A CA  
597  C C   . CYS A 75  ? 1.0534 0.4639 0.7409 -0.1116 0.3595  0.0550  75  CYS A C   
598  O O   . CYS A 75  ? 1.0569 0.4328 0.7148 -0.1156 0.3588  0.0612  75  CYS A O   
599  C CB  . CYS A 75  ? 1.0061 0.4496 0.7004 -0.1411 0.3872  0.0347  75  CYS A CB  
600  S SG  . CYS A 75  ? 1.0174 0.5079 0.7573 -0.1571 0.4082  0.0104  75  CYS A SG  
601  N N   . TRP A 76  ? 1.0024 0.4229 0.6973 -0.0912 0.3449  0.0639  76  TRP A N   
602  C CA  . TRP A 76  ? 0.9789 0.3760 0.6571 -0.0703 0.3269  0.0791  76  TRP A CA  
603  C C   . TRP A 76  ? 1.0056 0.4032 0.6664 -0.0561 0.3140  0.0924  76  TRP A C   
604  O O   . TRP A 76  ? 1.0972 0.5283 0.7754 -0.0561 0.3135  0.0859  76  TRP A O   
605  C CB  . TRP A 76  ? 0.9458 0.3582 0.6596 -0.0578 0.3209  0.0736  76  TRP A CB  
606  C CG  . TRP A 76  ? 0.9941 0.4076 0.7263 -0.0742 0.3336  0.0595  76  TRP A CG  
607  C CD1 . TRP A 76  ? 0.9474 0.3974 0.7155 -0.0872 0.3424  0.0423  76  TRP A CD1 
608  C CD2 . TRP A 76  ? 1.0092 0.3941 0.7287 -0.0782 0.3347  0.0585  76  TRP A CD2 
609  N NE1 . TRP A 76  ? 0.9690 0.4093 0.7462 -0.1019 0.3516  0.0324  76  TRP A NE1 
610  C CE2 . TRP A 76  ? 0.9931 0.3929 0.7391 -0.0972 0.3474  0.0417  76  TRP A CE2 
611  C CE3 . TRP A 76  ? 1.0724 0.4203 0.7624 -0.0673 0.3258  0.0699  76  TRP A CE3 
612  C CZ2 . TRP A 76  ? 1.0828 0.4611 0.8240 -0.1074 0.3519  0.0354  76  TRP A CZ2 
613  C CZ3 . TRP A 76  ? 1.1253 0.4504 0.8102 -0.0761 0.3311  0.0639  76  TRP A CZ3 
614  C CH2 . TRP A 76  ? 1.1077 0.4478 0.8167 -0.0968 0.3442  0.0467  76  TRP A CH2 
615  N N   . LEU A 77  ? 1.0752 0.4424 0.7057 -0.0426 0.2995  0.1083  77  LEU A N   
616  C CA  . LEU A 77  ? 1.0698 0.4374 0.6857 -0.0267 0.2829  0.1218  77  LEU A CA  
617  C C   . LEU A 77  ? 1.1224 0.5047 0.7663 -0.0008 0.2651  0.1247  77  LEU A C   
618  O O   . LEU A 77  ? 1.1292 0.4934 0.7795 0.0059  0.2660  0.1248  77  LEU A O   
619  C CB  . LEU A 77  ? 1.0685 0.3960 0.6312 -0.0289 0.2754  0.1373  77  LEU A CB  
620  C CG  . LEU A 77  ? 1.0797 0.4050 0.6237 -0.0126 0.2550  0.1524  77  LEU A CG  
621  C CD1 . LEU A 77  ? 1.1952 0.5634 0.7554 -0.0193 0.2560  0.1417  77  LEU A CD1 
622  C CD2 . LEU A 77  ? 1.2867 0.5678 0.7741 -0.0151 0.2453  0.1688  77  LEU A CD2 
623  N N   . ALA A 78  ? 1.1311 0.5463 0.7917 0.0123  0.2505  0.1256  78  ALA A N   
624  C CA  . ALA A 78  ? 1.0777 0.5125 0.7672 0.0356  0.2352  0.1271  78  ALA A CA  
625  C C   . ALA A 78  ? 1.0701 0.5181 0.7532 0.0474  0.2164  0.1364  78  ALA A C   
626  O O   . ALA A 78  ? 1.1859 0.6608 0.8739 0.0398  0.2156  0.1312  78  ALA A O   
627  C CB  . ALA A 78  ? 0.9519 0.4277 0.6859 0.0363  0.2402  0.1116  78  ALA A CB  
628  N N   . LEU A 79  ? 1.1415 0.5706 0.8149 0.0660  0.2006  0.1492  79  LEU A N   
629  C CA  . LEU A 79  ? 1.1548 0.5986 0.8261 0.0791  0.1789  0.1581  79  LEU A CA  
630  C C   . LEU A 79  ? 1.2051 0.6887 0.9252 0.0986  0.1697  0.1521  79  LEU A C   
631  O O   . LEU A 79  ? 1.2298 0.7054 0.9675 0.1127  0.1711  0.1513  79  LEU A O   
632  C CB  . LEU A 79  ? 1.2659 0.6640 0.8959 0.0886  0.1645  0.1769  79  LEU A CB  
633  C CG  . LEU A 79  ? 1.2536 0.6024 0.8285 0.0677  0.1769  0.1842  79  LEU A CG  
634  C CD1 . LEU A 79  ? 1.3235 0.6269 0.8507 0.0774  0.1580  0.2054  79  LEU A CD1 
635  C CD2 . LEU A 79  ? 1.2288 0.5963 0.7927 0.0437  0.1893  0.1749  79  LEU A CD2 
636  N N   . THR A 80  ? 1.0746 0.5991 0.8152 0.0980  0.1620  0.1469  80  THR A N   
637  C CA  . THR A 80  ? 1.0852 0.6507 0.8723 0.1119  0.1564  0.1396  80  THR A CA  
638  C C   . THR A 80  ? 1.2031 0.7796 0.9987 0.1311  0.1330  0.1488  80  THR A C   
639  O O   . THR A 80  ? 1.1542 0.7084 0.9170 0.1330  0.1180  0.1614  80  THR A O   
640  C CB  . THR A 80  ? 1.0998 0.7032 0.9072 0.0987  0.1630  0.1274  80  THR A CB  
641  O OG1 . THR A 80  ? 1.1069 0.7189 0.8971 0.0914  0.1514  0.1308  80  THR A OG1 
642  C CG2 . THR A 80  ? 1.1079 0.7019 0.9089 0.0814  0.1830  0.1186  80  THR A CG2 
643  N N   . ASP A 81  ? 1.2076 0.8193 1.0479 0.1452  0.1298  0.1419  81  ASP A N   
644  C CA  . ASP A 81  ? 1.1693 0.8052 1.0308 0.1628  0.1076  0.1468  81  ASP A CA  
645  C C   . ASP A 81  ? 1.1148 0.7732 0.9665 0.1501  0.0951  0.1472  81  ASP A C   
646  O O   . ASP A 81  ? 1.0892 0.7661 0.9450 0.1322  0.1069  0.1372  81  ASP A O   
647  C CB  . ASP A 81  ? 1.1041 0.7792 1.0195 0.1757  0.1123  0.1355  81  ASP A CB  
648  C CG  . ASP A 81  ? 1.1301 0.8331 1.0769 0.1968  0.0902  0.1389  81  ASP A CG  
649  O OD1 . ASP A 81  ? 1.1493 0.8709 1.0921 0.1933  0.0716  0.1430  81  ASP A OD1 
650  O OD2 . ASP A 81  ? 1.0927 0.8001 1.0697 0.2171  0.0915  0.1363  81  ASP A OD2 
651  N N   . PRO A 82  ? 1.1454 0.8001 0.9818 0.1588  0.0704  0.1585  82  PRO A N   
652  C CA  . PRO A 82  ? 1.1530 0.8268 0.9753 0.1447  0.0578  0.1577  82  PRO A CA  
653  C C   . PRO A 82  ? 1.1413 0.8695 1.0098 0.1395  0.0594  0.1433  82  PRO A C   
654  O O   . PRO A 82  ? 1.1329 0.8746 0.9897 0.1222  0.0568  0.1384  82  PRO A O   
655  C CB  . PRO A 82  ? 1.1905 0.8529 0.9944 0.1602  0.0268  0.1728  82  PRO A CB  
656  C CG  . PRO A 82  ? 1.1597 0.8148 0.9907 0.1873  0.0222  0.1780  82  PRO A CG  
657  C CD  . PRO A 82  ? 1.1950 0.8252 1.0237 0.1820  0.0515  0.1725  82  PRO A CD  
658  N N   . ARG A 83  ? 1.1303 0.8876 1.0485 0.1523  0.0653  0.1356  83  ARG A N   
659  C CA  . ARG A 83  ? 1.0514 0.8571 1.0115 0.1449  0.0702  0.1219  83  ARG A CA  
660  C C   . ARG A 83  ? 1.0505 0.8534 1.0084 0.1267  0.0962  0.1116  83  ARG A C   
661  O O   . ARG A 83  ? 1.0802 0.9125 1.0573 0.1142  0.1008  0.1018  83  ARG A O   
662  C CB  . ARG A 83  ? 1.0330 0.8718 1.0469 0.1650  0.0678  0.1169  83  ARG A CB  
663  C CG  . ARG A 83  ? 1.1162 0.9642 1.1432 0.1870  0.0397  0.1259  83  ARG A CG  
664  C CD  . ARG A 83  ? 1.1730 1.0493 1.2556 0.2094  0.0421  0.1194  83  ARG A CD  
665  N NE  . ARG A 83  ? 1.1939 1.0365 1.2693 0.2178  0.0626  0.1193  83  ARG A NE  
666  C CZ  . ARG A 83  ? 1.2200 1.0742 1.3344 0.2375  0.0698  0.1132  83  ARG A CZ  
667  N NH1 . ARG A 83  ? 1.2955 1.1973 1.4639 0.2523  0.0592  0.1064  83  ARG A NH1 
668  N NH2 . ARG A 83  ? 1.1848 1.0033 1.2851 0.2418  0.0888  0.1124  83  ARG A NH2 
669  N N   . ASP A 84  ? 1.0960 0.8638 1.0312 0.1246  0.1121  0.1137  84  ASP A N   
670  C CA  . ASP A 84  ? 1.0394 0.8038 0.9744 0.1104  0.1341  0.1046  84  ASP A CA  
671  C C   . ASP A 84  ? 1.0407 0.7732 0.9340 0.0954  0.1402  0.1073  84  ASP A C   
672  O O   . ASP A 84  ? 1.0318 0.7355 0.9084 0.0944  0.1517  0.1090  84  ASP A O   
673  C CB  . ASP A 84  ? 0.9250 0.6812 0.8758 0.1205  0.1480  0.1016  84  ASP A CB  
674  C CG  . ASP A 84  ? 0.9339 0.6874 0.8843 0.1072  0.1670  0.0929  84  ASP A CG  
675  O OD1 . ASP A 84  ? 0.9654 0.7314 0.9150 0.0931  0.1696  0.0879  84  ASP A OD1 
676  O OD2 . ASP A 84  ? 0.9196 0.6569 0.8697 0.1113  0.1782  0.0908  84  ASP A OD2 
677  N N   . VAL A 85  ? 0.9998 0.7384 0.8775 0.0825  0.1340  0.1059  85  VAL A N   
678  C CA  . VAL A 85  ? 1.0452 0.7541 0.8815 0.0688  0.1394  0.1081  85  VAL A CA  
679  C C   . VAL A 85  ? 1.0754 0.7952 0.9107 0.0512  0.1487  0.0971  85  VAL A C   
680  O O   . VAL A 85  ? 1.1062 0.8094 0.9095 0.0386  0.1510  0.0964  85  VAL A O   
681  C CB  . VAL A 85  ? 1.1206 0.8123 0.9227 0.0713  0.1209  0.1196  85  VAL A CB  
682  C CG1 . VAL A 85  ? 1.1119 0.7808 0.9082 0.0891  0.1134  0.1318  85  VAL A CG1 
683  C CG2 . VAL A 85  ? 1.0899 0.8138 0.9061 0.0722  0.1011  0.1181  85  VAL A CG2 
684  N N   . ALA A 86  ? 1.0621 0.8066 0.9298 0.0498  0.1552  0.0882  86  ALA A N   
685  C CA  . ALA A 86  ? 1.0621 0.8121 0.9294 0.0348  0.1640  0.0781  86  ALA A CA  
686  C C   . ALA A 86  ? 1.0786 0.8506 0.9789 0.0345  0.1703  0.0707  86  ALA A C   
687  O O   . ALA A 86  ? 1.0097 0.7956 0.9336 0.0447  0.1692  0.0725  86  ALA A O   
688  C CB  . ALA A 86  ? 1.0589 0.8140 0.9077 0.0249  0.1524  0.0766  86  ALA A CB  
689  N N   . ARG A 87  ? 1.0980 0.8703 0.9977 0.0224  0.1780  0.0623  87  ARG A N   
690  C CA  . ARG A 87  ? 1.0180 0.8035 0.9411 0.0195  0.1844  0.0563  87  ARG A CA  
691  C C   . ARG A 87  ? 1.0781 0.8899 1.0177 0.0159  0.1747  0.0542  87  ARG A C   
692  O O   . ARG A 87  ? 1.1695 0.9853 1.0982 0.0070  0.1666  0.0512  87  ARG A O   
693  C CB  . ARG A 87  ? 1.0052 0.7767 0.9204 0.0094  0.1947  0.0486  87  ARG A CB  
694  C CG  . ARG A 87  ? 0.9563 0.7322 0.8883 0.0058  0.2009  0.0440  87  ARG A CG  
695  C CD  . ARG A 87  ? 0.8785 0.6362 0.8038 0.0006  0.2097  0.0374  87  ARG A CD  
696  N NE  . ARG A 87  ? 0.9335 0.6837 0.8415 -0.0079 0.2100  0.0315  87  ARG A NE  
697  C CZ  . ARG A 87  ? 1.0222 0.7745 0.9259 -0.0184 0.2078  0.0252  87  ARG A CZ  
698  N NH1 . ARG A 87  ? 0.9331 0.6958 0.8504 -0.0228 0.2053  0.0242  87  ARG A NH1 
699  N NH2 . ARG A 87  ? 1.0146 0.7570 0.8982 -0.0265 0.2094  0.0186  87  ARG A NH2 
700  N N   . ILE A 88  ? 1.1208 0.9512 1.0865 0.0215  0.1763  0.0545  88  ILE A N   
701  C CA  . ILE A 88  ? 1.0935 0.9543 1.0824 0.0176  0.1690  0.0510  88  ILE A CA  
702  C C   . ILE A 88  ? 1.0899 0.9514 1.0841 0.0026  0.1787  0.0434  88  ILE A C   
703  O O   . ILE A 88  ? 1.0613 0.9199 1.0645 0.0025  0.1904  0.0426  88  ILE A O   
704  C CB  . ILE A 88  ? 1.0049 0.8868 1.0217 0.0307  0.1683  0.0535  88  ILE A CB  
705  C CG1 . ILE A 88  ? 1.0354 0.9070 1.0435 0.0472  0.1599  0.0619  88  ILE A CG1 
706  C CG2 . ILE A 88  ? 1.0473 0.9667 1.0937 0.0265  0.1600  0.0484  88  ILE A CG2 
707  C CD1 . ILE A 88  ? 1.0141 0.9027 1.0503 0.0628  0.1606  0.0631  88  ILE A CD1 
708  N N   . GLU A 89  ? 1.1946 1.0565 1.1794 -0.0107 0.1737  0.0378  89  GLU A N   
709  C CA  . GLU A 89  ? 1.1288 0.9852 1.1154 -0.0257 0.1827  0.0305  89  GLU A CA  
710  C C   . GLU A 89  ? 1.1504 1.0354 1.1656 -0.0328 0.1840  0.0268  89  GLU A C   
711  O O   . GLU A 89  ? 1.1372 1.0142 1.1554 -0.0425 0.1959  0.0237  89  GLU A O   
712  C CB  . GLU A 89  ? 1.2121 1.0571 1.1783 -0.0385 0.1783  0.0238  89  GLU A CB  
713  C CG  . GLU A 89  ? 1.2749 1.1093 1.2409 -0.0545 0.1869  0.0155  89  GLU A CG  
714  C CD  . GLU A 89  ? 1.3118 1.1288 1.2544 -0.0659 0.1852  0.0071  89  GLU A CD  
715  O OE1 . GLU A 89  ? 1.3064 1.1103 1.2286 -0.0603 0.1833  0.0082  89  GLU A OE1 
716  O OE2 . GLU A 89  ? 1.2249 1.0397 1.1681 -0.0817 0.1870  -0.0014 89  GLU A OE2 
717  N N   . SER A 90  ? 1.1697 1.0874 1.2064 -0.0281 0.1722  0.0270  90  SER A N   
718  C CA  . SER A 90  ? 1.0835 1.0352 1.1537 -0.0362 0.1740  0.0210  90  SER A CA  
719  C C   . SER A 90  ? 1.0198 0.9787 1.1091 -0.0284 0.1882  0.0230  90  SER A C   
720  O O   . SER A 90  ? 1.0155 0.9958 1.1285 -0.0390 0.1972  0.0169  90  SER A O   
721  C CB  . SER A 90  ? 1.0556 1.0443 1.1474 -0.0326 0.1539  0.0192  90  SER A CB  
722  O OG  . SER A 90  ? 1.1045 1.0920 1.1930 -0.0115 0.1435  0.0281  90  SER A OG  
723  N N   . LYS A 91  ? 0.9911 0.9319 1.0692 -0.0121 0.1918  0.0302  91  LYS A N   
724  C CA  . LYS A 91  ? 0.8701 0.8133 0.9603 -0.0048 0.2057  0.0311  91  LYS A CA  
725  C C   . LYS A 91  ? 0.8262 0.7333 0.8898 -0.0089 0.2195  0.0339  91  LYS A C   
726  O O   . LYS A 91  ? 0.7744 0.6746 0.8370 -0.0016 0.2295  0.0358  91  LYS A O   
727  C CB  . LYS A 91  ? 0.8781 0.8272 0.9765 0.0167  0.1993  0.0360  91  LYS A CB  
728  C CG  . LYS A 91  ? 0.8841 0.8722 1.0159 0.0248  0.1856  0.0336  91  LYS A CG  
729  C CD  . LYS A 91  ? 0.9579 0.9443 1.0958 0.0480  0.1801  0.0393  91  LYS A CD  
730  C CE  . LYS A 91  ? 1.0327 1.0604 1.2110 0.0594  0.1664  0.0364  91  LYS A CE  
731  N NZ  . LYS A 91  ? 1.1579 1.1980 1.3331 0.0550  0.1435  0.0381  91  LYS A NZ  
732  N N   . THR A 92  ? 0.8314 0.7147 0.8733 -0.0195 0.2192  0.0336  92  THR A N   
733  C CA  . THR A 92  ? 0.8664 0.7160 0.8855 -0.0227 0.2290  0.0363  92  THR A CA  
734  C C   . THR A 92  ? 0.8701 0.7163 0.8897 -0.0403 0.2394  0.0329  92  THR A C   
735  O O   . THR A 92  ? 0.8800 0.7375 0.9077 -0.0538 0.2369  0.0273  92  THR A O   
736  C CB  . THR A 92  ? 0.8556 0.6789 0.8530 -0.0213 0.2231  0.0374  92  THR A CB  
737  O OG1 . THR A 92  ? 0.9151 0.7432 0.9109 -0.0093 0.2141  0.0399  92  THR A OG1 
738  C CG2 . THR A 92  ? 0.8519 0.6441 0.8312 -0.0184 0.2295  0.0410  92  THR A CG2 
739  N N   . VAL A 93  ? 0.8095 0.6381 0.8173 -0.0416 0.2509  0.0361  93  VAL A N   
740  C CA  . VAL A 93  ? 0.8169 0.6380 0.8204 -0.0594 0.2632  0.0344  93  VAL A CA  
741  C C   . VAL A 93  ? 0.8351 0.6143 0.8063 -0.0594 0.2685  0.0414  93  VAL A C   
742  O O   . VAL A 93  ? 0.8061 0.5728 0.7657 -0.0456 0.2656  0.0461  93  VAL A O   
743  C CB  . VAL A 93  ? 0.8062 0.6598 0.8339 -0.0643 0.2748  0.0298  93  VAL A CB  
744  C CG1 . VAL A 93  ? 0.8474 0.7452 0.9113 -0.0633 0.2661  0.0228  93  VAL A CG1 
745  C CG2 . VAL A 93  ? 0.7950 0.6462 0.8181 -0.0501 0.2806  0.0331  93  VAL A CG2 
746  N N   . ILE A 94  ? 0.8334 0.5895 0.7894 -0.0755 0.2752  0.0420  94  ILE A N   
747  C CA  . ILE A 94  ? 0.8852 0.5981 0.8079 -0.0770 0.2788  0.0499  94  ILE A CA  
748  C C   . ILE A 94  ? 0.8323 0.5403 0.7452 -0.0949 0.2957  0.0506  94  ILE A C   
749  O O   . ILE A 94  ? 0.8953 0.6168 0.8213 -0.1127 0.3036  0.0447  94  ILE A O   
750  C CB  . ILE A 94  ? 0.8598 0.5388 0.7669 -0.0789 0.2713  0.0515  94  ILE A CB  
751  C CG1 . ILE A 94  ? 0.8059 0.4926 0.7238 -0.0633 0.2582  0.0486  94  ILE A CG1 
752  C CG2 . ILE A 94  ? 0.8339 0.4669 0.7069 -0.0779 0.2717  0.0611  94  ILE A CG2 
753  C CD1 . ILE A 94  ? 0.8691 0.5232 0.7746 -0.0620 0.2523  0.0482  94  ILE A CD1 
754  N N   . ILE A 95  ? 0.8518 0.5405 0.7404 -0.0920 0.3017  0.0569  95  ILE A N   
755  C CA  . ILE A 95  ? 0.9087 0.5902 0.7820 -0.1096 0.3207  0.0576  95  ILE A CA  
756  C C   . ILE A 95  ? 0.9268 0.5525 0.7550 -0.1189 0.3211  0.0680  95  ILE A C   
757  O O   . ILE A 95  ? 0.9501 0.5447 0.7506 -0.1062 0.3104  0.0767  95  ILE A O   
758  C CB  . ILE A 95  ? 0.9430 0.6390 0.8149 -0.1020 0.3293  0.0565  95  ILE A CB  
759  C CG1 . ILE A 95  ? 0.9056 0.6554 0.8243 -0.0938 0.3309  0.0460  95  ILE A CG1 
760  C CG2 . ILE A 95  ? 0.9565 0.6340 0.8003 -0.1212 0.3504  0.0582  95  ILE A CG2 
761  C CD1 . ILE A 95  ? 0.8619 0.6238 0.7972 -0.0725 0.3118  0.0462  95  ILE A CD1 
762  N N   . THR A 96  ? 0.9388 0.5511 0.7599 -0.1410 0.3324  0.0672  96  THR A N   
763  C CA  . THR A 96  ? 1.0698 0.6240 0.8444 -0.1525 0.3350  0.0781  96  THR A CA  
764  C C   . THR A 96  ? 1.0918 0.6465 0.8573 -0.1793 0.3564  0.0747  96  THR A C   
765  O O   . THR A 96  ? 1.0310 0.6260 0.8325 -0.1934 0.3690  0.0634  96  THR A O   
766  C CB  . THR A 96  ? 1.0004 0.5257 0.7717 -0.1509 0.3221  0.0799  96  THR A CB  
767  O OG1 . THR A 96  ? 0.9543 0.5074 0.7566 -0.1665 0.3287  0.0685  96  THR A OG1 
768  C CG2 . THR A 96  ? 0.9867 0.5165 0.7705 -0.1241 0.3009  0.0804  96  THR A CG2 
769  N N   . GLN A 97  ? 1.1466 0.6622 0.8667 -0.1841 0.3559  0.0826  97  GLN A N   
770  C CA  . GLN A 97  ? 1.2026 0.7169 0.9108 -0.2082 0.3722  0.0782  97  GLN A CA  
771  C C   . GLN A 97  ? 1.1713 0.6926 0.9015 -0.2261 0.3764  0.0708  97  GLN A C   
772  O O   . GLN A 97  ? 1.1459 0.7027 0.9030 -0.2451 0.3930  0.0592  97  GLN A O   
773  C CB  . GLN A 97  ? 1.3621 0.8212 1.0110 -0.2104 0.3668  0.0906  97  GLN A CB  
774  C CG  . GLN A 97  ? 1.5396 0.9899 1.1692 -0.2363 0.3845  0.0871  97  GLN A CG  
775  C CD  . GLN A 97  ? 1.7436 1.1339 1.3103 -0.2383 0.3773  0.1011  97  GLN A CD  
776  O OE1 . GLN A 97  ? 1.8214 1.1841 1.3597 -0.2200 0.3602  0.1123  97  GLN A OE1 
777  N NE2 . GLN A 97  ? 1.7388 1.1084 1.2833 -0.2611 0.3896  0.1005  97  GLN A NE2 
778  N N   . GLU A 98  ? 1.1622 0.6511 0.8833 -0.2202 0.3615  0.0759  98  GLU A N   
779  C CA  . GLU A 98  ? 1.1830 0.6711 0.9197 -0.2367 0.3637  0.0685  98  GLU A CA  
780  C C   . GLU A 98  ? 1.0756 0.5912 0.8514 -0.2271 0.3561  0.0616  98  GLU A C   
781  O O   . GLU A 98  ? 1.0591 0.5590 0.8301 -0.2052 0.3417  0.0679  98  GLU A O   
782  C CB  . GLU A 98  ? 1.3369 0.7630 1.0317 -0.2381 0.3538  0.0778  98  GLU A CB  
783  C CG  . GLU A 98  ? 1.4959 0.8862 1.1439 -0.2464 0.3589  0.0873  98  GLU A CG  
784  C CD  . GLU A 98  ? 1.5467 0.9439 1.1947 -0.2765 0.3784  0.0792  98  GLU A CD  
785  O OE1 . GLU A 98  ? 1.5764 0.9792 1.2446 -0.2906 0.3815  0.0705  98  GLU A OE1 
786  O OE2 . GLU A 98  ? 1.6202 1.0168 1.2476 -0.2870 0.3912  0.0806  98  GLU A OE2 
787  N N   . GLN A 99  ? 0.9852 0.5426 0.7998 -0.2444 0.3656  0.0482  99  GLN A N   
788  C CA  . GLN A 99  ? 0.9628 0.5485 0.8124 -0.2369 0.3564  0.0405  99  GLN A CA  
789  C C   . GLN A 99  ? 1.0648 0.6051 0.8951 -0.2310 0.3430  0.0429  99  GLN A C   
790  O O   . GLN A 99  ? 1.0153 0.5673 0.8593 -0.2099 0.3263  0.0402  99  GLN A O   
791  C CB  . GLN A 99  ? 0.9265 0.5669 0.8200 -0.2573 0.3641  0.0245  99  GLN A CB  
792  C CG  . GLN A 99  ? 0.9212 0.5956 0.8469 -0.2469 0.3454  0.0143  99  GLN A CG  
793  C CD  . GLN A 99  ? 0.9017 0.6296 0.8699 -0.2677 0.3493  -0.0015 99  GLN A CD  
794  O OE1 . GLN A 99  ? 0.9518 0.6862 0.9259 -0.2942 0.3678  -0.0064 99  GLN A OE1 
795  N NE2 . GLN A 99  ? 0.9228 0.6900 0.9204 -0.2567 0.3316  -0.0098 99  GLN A NE2 
796  N N   . ARG A 100 ? 1.0652 0.5605 0.8657 -0.2444 0.3453  0.0455  100 ARG A N   
797  C CA  . ARG A 100 ? 1.0424 0.4938 0.8267 -0.2382 0.3338  0.0459  100 ARG A CA  
798  C C   . ARG A 100 ? 1.0626 0.4862 0.8311 -0.2077 0.3186  0.0566  100 ARG A C   
799  O O   . ARG A 100 ? 1.1025 0.5053 0.8724 -0.1964 0.3089  0.0537  100 ARG A O   
800  C CB  . ARG A 100 ? 1.1083 0.5170 0.8617 -0.2543 0.3373  0.0480  100 ARG A CB  
801  C CG  . ARG A 100 ? 1.1777 0.5477 0.9219 -0.2540 0.3294  0.0435  100 ARG A CG  
802  C CD  . ARG A 100 ? 1.3301 0.6591 1.0443 -0.2718 0.3349  0.0460  100 ARG A CD  
803  N NE  . ARG A 100 ? 1.3097 0.6088 1.0209 -0.2770 0.3311  0.0376  100 ARG A NE  
804  C CZ  . ARG A 100 ? 1.4644 0.7263 1.1529 -0.2937 0.3359  0.0372  100 ARG A CZ  
805  N NH1 . ARG A 100 ? 1.5446 0.7929 1.2095 -0.3079 0.3451  0.0452  100 ARG A NH1 
806  N NH2 . ARG A 100 ? 1.5675 0.8036 1.2552 -0.2969 0.3326  0.0280  100 ARG A NH2 
807  N N   . ASP A 101 ? 1.0707 0.4948 0.8253 -0.1945 0.3166  0.0675  101 ASP A N   
808  C CA  . ASP A 101 ? 1.0635 0.4673 0.8076 -0.1663 0.3011  0.0766  101 ASP A CA  
809  C C   . ASP A 101 ? 1.0018 0.4451 0.7814 -0.1494 0.2928  0.0682  101 ASP A C   
810  O O   . ASP A 101 ? 1.0548 0.4845 0.8348 -0.1275 0.2788  0.0700  101 ASP A O   
811  C CB  . ASP A 101 ? 1.0814 0.4826 0.8032 -0.1585 0.3001  0.0879  101 ASP A CB  
812  C CG  . ASP A 101 ? 1.3324 0.6974 1.0149 -0.1708 0.3026  0.0958  101 ASP A CG  
813  O OD1 . ASP A 101 ? 1.4816 0.8080 1.1472 -0.1738 0.2968  0.0980  101 ASP A OD1 
814  O OD2 . ASP A 101 ? 1.4042 0.7778 1.0715 -0.1775 0.3109  0.0996  101 ASP A OD2 
815  N N   . THR A 102 ? 0.9338 0.4324 0.7459 -0.1570 0.2979  0.0576  102 THR A N   
816  C CA  . THR A 102 ? 1.0371 0.5796 0.8804 -0.1399 0.2871  0.0500  102 THR A CA  
817  C C   . THR A 102 ? 0.9775 0.5299 0.8376 -0.1458 0.2831  0.0374  102 THR A C   
818  O O   . THR A 102 ? 0.9543 0.5056 0.8199 -0.1297 0.2727  0.0340  102 THR A O   
819  C CB  . THR A 102 ? 0.9501 0.5454 0.8174 -0.1410 0.2923  0.0471  102 THR A CB  
820  O OG1 . THR A 102 ? 1.0119 0.5971 0.8613 -0.1331 0.2956  0.0572  102 THR A OG1 
821  C CG2 . THR A 102 ? 0.7976 0.4334 0.6933 -0.1252 0.2808  0.0403  102 THR A CG2 
822  N N   . VAL A 103 ? 0.9159 0.4789 0.7839 -0.1702 0.2917  0.0292  103 VAL A N   
823  C CA  . VAL A 103 ? 0.9417 0.5140 0.8222 -0.1791 0.2874  0.0158  103 VAL A CA  
824  C C   . VAL A 103 ? 1.0661 0.6068 0.9328 -0.2061 0.2981  0.0113  103 VAL A C   
825  O O   . VAL A 103 ? 1.1425 0.6776 1.0024 -0.2241 0.3109  0.0154  103 VAL A O   
826  C CB  . VAL A 103 ? 0.9090 0.5441 0.8232 -0.1818 0.2824  0.0064  103 VAL A CB  
827  C CG1 . VAL A 103 ? 0.8817 0.5438 0.8069 -0.1564 0.2734  0.0118  103 VAL A CG1 
828  C CG2 . VAL A 103 ? 0.8501 0.5144 0.7809 -0.2038 0.2938  0.0033  103 VAL A CG2 
829  N N   . PRO A 104 ? 1.0597 0.5768 0.9203 -0.2111 0.2947  0.0019  104 PRO A N   
830  C CA  . PRO A 104 ? 1.0498 0.5388 0.8993 -0.2398 0.3050  -0.0051 104 PRO A CA  
831  C C   . PRO A 104 ? 0.9842 0.5253 0.8607 -0.2644 0.3105  -0.0147 104 PRO A C   
832  O O   . PRO A 104 ? 1.0552 0.6515 0.9604 -0.2589 0.3012  -0.0217 104 PRO A O   
833  C CB  . PRO A 104 ? 1.0591 0.5248 0.9029 -0.2370 0.2985  -0.0170 104 PRO A CB  
834  C CG  . PRO A 104 ? 1.0362 0.5007 0.8804 -0.2045 0.2879  -0.0119 104 PRO A CG  
835  C CD  . PRO A 104 ? 0.9928 0.5071 0.8557 -0.1924 0.2836  -0.0042 104 PRO A CD  
836  N N   . ILE A 105 ? 1.0450 0.5679 0.9127 -0.2917 0.3255  -0.0149 105 ILE A N   
837  C CA  . ILE A 105 ? 1.0452 0.6197 0.9438 -0.3176 0.3324  -0.0260 105 ILE A CA  
838  C C   . ILE A 105 ? 1.0205 0.6109 0.9329 -0.3321 0.3237  -0.0439 105 ILE A C   
839  O O   . ILE A 105 ? 1.0499 0.5947 0.9411 -0.3505 0.3293  -0.0501 105 ILE A O   
840  C CB  . ILE A 105 ? 1.1118 0.6619 0.9959 -0.3449 0.3529  -0.0223 105 ILE A CB  
841  C CG1 . ILE A 105 ? 1.0482 0.5809 0.9100 -0.3258 0.3562  -0.0047 105 ILE A CG1 
842  C CG2 . ILE A 105 ? 1.0625 0.6738 0.9871 -0.3722 0.3617  -0.0358 105 ILE A CG2 
843  C CD1 . ILE A 105 ? 0.9974 0.5828 0.8876 -0.3125 0.3573  -0.0018 105 ILE A CD1 
844  N N   . PRO A 106 ? 1.0026 0.6530 0.9468 -0.3246 0.3093  -0.0526 106 PRO A N   
845  C CA  . PRO A 106 ? 1.0378 0.7017 0.9894 -0.3383 0.2985  -0.0697 106 PRO A CA  
846  C C   . PRO A 106 ? 1.0647 0.7274 1.0228 -0.3773 0.3095  -0.0824 106 PRO A C   
847  O O   . PRO A 106 ? 1.1337 0.8217 1.1119 -0.3944 0.3218  -0.0818 106 PRO A O   
848  C CB  . PRO A 106 ? 0.9623 0.6964 0.9483 -0.3248 0.2813  -0.0732 106 PRO A CB  
849  C CG  . PRO A 106 ? 0.9754 0.7180 0.9644 -0.2964 0.2821  -0.0572 106 PRO A CG  
850  C CD  . PRO A 106 ? 0.9317 0.6383 0.9047 -0.3047 0.3020  -0.0473 106 PRO A CD  
851  N N   . LYS A 107 ? 1.1185 0.7508 1.0595 -0.3928 0.3067  -0.0953 107 LYS A N   
852  C CA  . LYS A 107 ? 1.2256 0.8556 1.1724 -0.4326 0.3162  -0.1098 107 LYS A CA  
853  C C   . LYS A 107 ? 1.2787 0.9910 1.2741 -0.4484 0.3076  -0.1220 107 LYS A C   
854  O O   . LYS A 107 ? 1.3085 1.0407 1.3250 -0.4775 0.3206  -0.1284 107 LYS A O   
855  C CB  . LYS A 107 ? 1.2507 0.8335 1.1694 -0.4445 0.3131  -0.1235 107 LYS A CB  
856  C CG  . LYS A 107 ? 1.2935 0.8759 1.2185 -0.4879 0.3207  -0.1415 107 LYS A CG  
857  C CD  . LYS A 107 ? 1.3980 0.9259 1.2890 -0.4946 0.3183  -0.1540 107 LYS A CD  
858  C CE  . LYS A 107 ? 1.4731 0.9265 1.3238 -0.4734 0.3272  -0.1397 107 LYS A CE  
859  N NZ  . LYS A 107 ? 1.6549 1.0591 1.4773 -0.4815 0.3272  -0.1528 107 LYS A NZ  
860  N N   . SER A 108 ? 1.1334 0.8944 1.1478 -0.4294 0.2855  -0.1254 108 SER A N   
861  C CA  . SER A 108 ? 1.1217 0.9626 1.1845 -0.4394 0.2722  -0.1363 108 SER A CA  
862  C C   . SER A 108 ? 1.1296 1.0089 1.2034 -0.4051 0.2502  -0.1293 108 SER A C   
863  O O   . SER A 108 ? 1.1064 0.9689 1.1557 -0.3937 0.2355  -0.1318 108 SER A O   
864  C CB  . SER A 108 ? 1.1579 1.0092 1.2256 -0.4724 0.2638  -0.1580 108 SER A CB  
865  O OG  . SER A 108 ? 1.2311 1.0611 1.2694 -0.4621 0.2468  -0.1635 108 SER A OG  
866  N N   . GLY A 109 ? 1.0561 0.9837 1.1646 -0.3898 0.2494  -0.1213 109 GLY A N   
867  C CA  . GLY A 109 ? 0.9272 0.8884 1.0465 -0.3573 0.2298  -0.1134 109 GLY A CA  
868  C C   . GLY A 109 ? 0.9346 0.8714 1.0398 -0.3283 0.2403  -0.0947 109 GLY A C   
869  O O   . GLY A 109 ? 0.9278 0.8291 1.0188 -0.3329 0.2616  -0.0873 109 GLY A O   
870  N N   . GLN A 110 ? 0.8654 0.8192 0.9713 -0.2990 0.2242  -0.0868 110 GLN A N   
871  C CA  . GLN A 110 ? 0.8578 0.7973 0.9553 -0.2708 0.2308  -0.0705 110 GLN A CA  
872  C C   . GLN A 110 ? 0.8692 0.7490 0.9210 -0.2565 0.2322  -0.0630 110 GLN A C   
873  O O   . GLN A 110 ? 0.8813 0.7472 0.9136 -0.2567 0.2208  -0.0690 110 GLN A O   
874  C CB  . GLN A 110 ? 0.8819 0.8720 1.0077 -0.2471 0.2138  -0.0662 110 GLN A CB  
875  C CG  . GLN A 110 ? 0.9243 0.9233 1.0639 -0.2283 0.2255  -0.0549 110 GLN A CG  
876  C CD  . GLN A 110 ? 0.9543 1.0096 1.1322 -0.2096 0.2103  -0.0542 110 GLN A CD  
877  O OE1 . GLN A 110 ? 0.9084 0.9738 1.0817 -0.1953 0.1887  -0.0525 110 GLN A OE1 
878  N NE2 . GLN A 110 ? 0.9299 1.0203 1.1448 -0.2099 0.2220  -0.0557 110 GLN A NE2 
879  N N   . SER A 111 ? 0.8331 0.6790 0.8688 -0.2443 0.2464  -0.0507 111 SER A N   
880  C CA  . SER A 111 ? 0.8381 0.6319 0.8377 -0.2285 0.2475  -0.0438 111 SER A CA  
881  C C   . SER A 111 ? 0.8887 0.6971 0.8866 -0.2030 0.2328  -0.0392 111 SER A C   
882  O O   . SER A 111 ? 0.9104 0.7554 0.9292 -0.1888 0.2267  -0.0335 111 SER A O   
883  C CB  . SER A 111 ? 0.8519 0.6099 0.8363 -0.2215 0.2630  -0.0312 111 SER A CB  
884  O OG  . SER A 111 ? 0.8673 0.5876 0.8268 -0.2000 0.2604  -0.0236 111 SER A OG  
885  N N   . GLN A 112 ? 0.8568 0.6343 0.8290 -0.1978 0.2286  -0.0425 112 GLN A N   
886  C CA  . GLN A 112 ? 0.8336 0.6158 0.7973 -0.1762 0.2182  -0.0384 112 GLN A CA  
887  C C   . GLN A 112 ? 0.8410 0.5869 0.7881 -0.1567 0.2261  -0.0291 112 GLN A C   
888  O O   . GLN A 112 ? 0.9727 0.7186 0.9121 -0.1402 0.2205  -0.0263 112 GLN A O   
889  C CB  . GLN A 112 ? 0.8638 0.6408 0.8100 -0.1847 0.2089  -0.0503 112 GLN A CB  
890  C CG  . GLN A 112 ? 0.8682 0.6795 0.8277 -0.2056 0.1975  -0.0613 112 GLN A CG  
891  C CD  . GLN A 112 ? 0.9028 0.7097 0.8386 -0.2113 0.1857  -0.0717 112 GLN A CD  
892  O OE1 . GLN A 112 ? 0.9139 0.6966 0.8254 -0.1982 0.1872  -0.0700 112 GLN A OE1 
893  N NE2 . GLN A 112 ? 0.9412 0.7722 0.8834 -0.2323 0.1744  -0.0835 112 GLN A NE2 
894  N N   . LEU A 113 ? 0.8527 0.5671 0.7932 -0.1590 0.2381  -0.0244 113 LEU A N   
895  C CA  . LEU A 113 ? 0.8951 0.5730 0.8205 -0.1415 0.2429  -0.0169 113 LEU A CA  
896  C C   . LEU A 113 ? 0.8648 0.5510 0.7972 -0.1271 0.2451  -0.0037 113 LEU A C   
897  O O   . LEU A 113 ? 0.9004 0.5566 0.8210 -0.1148 0.2482  0.0035  113 LEU A O   
898  C CB  . LEU A 113 ? 0.9952 0.6244 0.9030 -0.1514 0.2520  -0.0198 113 LEU A CB  
899  C CG  . LEU A 113 ? 0.8824 0.5013 0.7827 -0.1709 0.2523  -0.0351 113 LEU A CG  
900  C CD1 . LEU A 113 ? 1.0040 0.5682 0.8859 -0.1787 0.2618  -0.0375 113 LEU A CD1 
901  C CD2 . LEU A 113 ? 0.9590 0.5862 0.8541 -0.1628 0.2452  -0.0437 113 LEU A CD2 
902  N N   . GLY A 114 ? 0.9456 0.6717 0.8973 -0.1278 0.2427  -0.0012 114 GLY A N   
903  C CA  . GLY A 114 ? 0.8556 0.5905 0.8133 -0.1161 0.2465  0.0091  114 GLY A CA  
904  C C   . GLY A 114 ? 0.8697 0.6443 0.8515 -0.1260 0.2496  0.0073  114 GLY A C   
905  O O   . GLY A 114 ? 0.8898 0.6828 0.8845 -0.1442 0.2496  -0.0013 114 GLY A O   
906  N N   . ARG A 115 ? 0.8701 0.6594 0.8603 -0.1137 0.2526  0.0142  115 ARG A N   
907  C CA  . ARG A 115 ? 0.8806 0.7086 0.8975 -0.1198 0.2584  0.0118  115 ARG A CA  
908  C C   . ARG A 115 ? 0.8632 0.6732 0.8681 -0.1203 0.2734  0.0187  115 ARG A C   
909  O O   . ARG A 115 ? 0.9194 0.7167 0.9124 -0.1033 0.2726  0.0262  115 ARG A O   
910  C CB  . ARG A 115 ? 0.9424 0.8096 0.9828 -0.1030 0.2471  0.0116  115 ARG A CB  
911  C CG  . ARG A 115 ? 1.0996 1.0133 1.1764 -0.1076 0.2511  0.0063  115 ARG A CG  
912  C CD  . ARG A 115 ? 1.1902 1.1385 1.2898 -0.0888 0.2363  0.0065  115 ARG A CD  
913  N NE  . ARG A 115 ? 1.3416 1.2939 1.4366 -0.0886 0.2180  0.0042  115 ARG A NE  
914  C CZ  . ARG A 115 ? 1.3928 1.3755 1.5080 -0.1011 0.2081  -0.0044 115 ARG A CZ  
915  N NH1 . ARG A 115 ? 1.2741 1.2899 1.4214 -0.1152 0.2151  -0.0123 115 ARG A NH1 
916  N NH2 . ARG A 115 ? 1.3926 1.3732 1.4948 -0.1007 0.1911  -0.0060 115 ARG A NH2 
917  N N   . TRP A 116 ? 0.8795 0.6867 0.8849 -0.1415 0.2874  0.0158  116 TRP A N   
918  C CA  . TRP A 116 ? 0.8996 0.6829 0.8849 -0.1467 0.3034  0.0224  116 TRP A CA  
919  C C   . TRP A 116 ? 0.9084 0.7334 0.9213 -0.1492 0.3154  0.0178  116 TRP A C   
920  O O   . TRP A 116 ? 0.9363 0.8068 0.9869 -0.1566 0.3151  0.0078  116 TRP A O   
921  C CB  . TRP A 116 ? 0.9245 0.6698 0.8858 -0.1704 0.3142  0.0231  116 TRP A CB  
922  C CG  . TRP A 116 ? 0.9170 0.6349 0.8517 -0.1796 0.3315  0.0305  116 TRP A CG  
923  C CD1 . TRP A 116 ? 0.9584 0.6317 0.8547 -0.1690 0.3306  0.0427  116 TRP A CD1 
924  C CD2 . TRP A 116 ? 0.8562 0.5891 0.7988 -0.2027 0.3525  0.0258  116 TRP A CD2 
925  N NE1 . TRP A 116 ? 0.9118 0.5675 0.7856 -0.1841 0.3489  0.0470  116 TRP A NE1 
926  C CE2 . TRP A 116 ? 0.8916 0.5830 0.7932 -0.2056 0.3646  0.0364  116 TRP A CE2 
927  C CE3 . TRP A 116 ? 0.8574 0.6363 0.8386 -0.2219 0.3622  0.0128  116 TRP A CE3 
928  C CZ2 . TRP A 116 ? 0.9418 0.6333 0.8358 -0.2284 0.3887  0.0346  116 TRP A CZ2 
929  C CZ3 . TRP A 116 ? 0.8531 0.6368 0.8338 -0.2441 0.3866  0.0098  116 TRP A CZ3 
930  C CH2 . TRP A 116 ? 0.8917 0.6303 0.8270 -0.2478 0.4010  0.0207  116 TRP A CH2 
931  N N   . MET A 117 ? 0.9138 0.7234 0.9084 -0.1427 0.3257  0.0242  117 MET A N   
932  C CA  . MET A 117 ? 0.8956 0.7390 0.9124 -0.1447 0.3412  0.0187  117 MET A CA  
933  C C   . MET A 117 ? 0.8251 0.6312 0.8032 -0.1550 0.3598  0.0251  117 MET A C   
934  O O   . MET A 117 ? 0.9026 0.6656 0.8414 -0.1454 0.3538  0.0359  117 MET A O   
935  C CB  . MET A 117 ? 0.8418 0.7131 0.8799 -0.1186 0.3316  0.0180  117 MET A CB  
936  C CG  . MET A 117 ? 0.9286 0.8350 0.9932 -0.1174 0.3481  0.0105  117 MET A CG  
937  S SD  . MET A 117 ? 0.8271 0.7561 0.9123 -0.0856 0.3367  0.0103  117 MET A SD  
938  C CE  . MET A 117 ? 0.9240 0.8856 1.0433 -0.0766 0.3116  0.0077  117 MET A CE  
939  N N   . SER A 118 ? 0.9001 0.7235 0.8890 -0.1753 0.3822  0.0182  118 SER A N   
940  C CA  . SER A 118 ? 1.0459 0.8323 0.9928 -0.1885 0.4023  0.0240  118 SER A CA  
941  C C   . SER A 118 ? 0.9701 0.7546 0.9044 -0.1693 0.4043  0.0266  118 SER A C   
942  O O   . SER A 118 ? 1.0105 0.8309 0.9781 -0.1489 0.3960  0.0212  118 SER A O   
943  C CB  . SER A 118 ? 0.9500 0.7597 0.9144 -0.2169 0.4294  0.0137  118 SER A CB  
944  O OG  . SER A 118 ? 0.9444 0.8170 0.9634 -0.2098 0.4367  -0.0002 118 SER A OG  
945  N N   . GLU A 119 ? 1.0301 0.7684 0.9121 -0.1767 0.4148  0.0354  119 GLU A N   
946  C CA  . GLU A 119 ? 1.1521 0.8856 1.0167 -0.1628 0.4191  0.0362  119 GLU A CA  
947  C C   . GLU A 119 ? 1.0791 0.8624 0.9829 -0.1645 0.4386  0.0207  119 GLU A C   
948  O O   . GLU A 119 ? 1.0915 0.8922 1.0085 -0.1465 0.4399  0.0164  119 GLU A O   
949  C CB  . GLU A 119 ? 1.2130 0.8911 1.0133 -0.1693 0.4170  0.0460  119 GLU A CB  
950  C CG  . GLU A 119 ? 1.3229 0.9506 1.0858 -0.1642 0.3961  0.0612  119 GLU A CG  
951  C CD  . GLU A 119 ? 1.3367 0.9478 1.0958 -0.1815 0.3941  0.0631  119 GLU A CD  
952  O OE1 . GLU A 119 ? 1.2210 0.8683 1.0184 -0.1952 0.4055  0.0524  119 GLU A OE1 
953  O OE2 . GLU A 119 ? 1.4736 1.0356 1.1925 -0.1810 0.3805  0.0747  119 GLU A OE2 
954  N N   . GLU A 120 ? 1.0919 0.8991 1.0169 -0.1850 0.4522  0.0109  120 GLU A N   
955  C CA  . GLU A 120 ? 1.1223 0.9809 1.0912 -0.1863 0.4703  -0.0056 120 GLU A CA  
956  C C   . GLU A 120 ? 0.9610 0.8740 0.9937 -0.1674 0.4662  -0.0136 120 GLU A C   
957  O O   . GLU A 120 ? 0.9767 0.9164 1.0339 -0.1509 0.4727  -0.0218 120 GLU A O   
958  C CB  . GLU A 120 ? 1.0816 0.9566 1.0639 -0.2134 0.4847  -0.0147 120 GLU A CB  
959  C CG  . GLU A 120 ? 1.2764 1.0966 1.1950 -0.2326 0.4906  -0.0071 120 GLU A CG  
960  C CD  . GLU A 120 ? 1.3099 1.0867 1.1961 -0.2430 0.4766  0.0056  120 GLU A CD  
961  O OE1 . GLU A 120 ? 1.1929 0.9846 1.1079 -0.2382 0.4642  0.0067  120 GLU A OE1 
962  O OE2 . GLU A 120 ? 1.4667 1.1932 1.2981 -0.2556 0.4779  0.0140  120 GLU A OE2 
963  N N   . ASP A 121 ? 0.9158 0.8439 0.9741 -0.1662 0.4477  -0.0118 121 ASP A N   
964  C CA  . ASP A 121 ? 0.9317 0.9073 1.0438 -0.1435 0.4284  -0.0179 121 ASP A CA  
965  C C   . ASP A 121 ? 0.9107 0.8678 1.0062 -0.1143 0.4111  -0.0102 121 ASP A C   
966  O O   . ASP A 121 ? 0.8289 0.8193 0.9608 -0.0937 0.4060  -0.0165 121 ASP A O   
967  C CB  . ASP A 121 ? 0.9164 0.9031 1.0466 -0.1494 0.4082  -0.0167 121 ASP A CB  
968  C CG  . ASP A 121 ? 0.9778 0.9881 1.1312 -0.1795 0.4243  -0.0266 121 ASP A CG  
969  O OD1 . ASP A 121 ? 0.9419 0.9622 1.0996 -0.1959 0.4526  -0.0344 121 ASP A OD1 
970  O OD2 . ASP A 121 ? 0.9552 0.9733 1.1213 -0.1884 0.4098  -0.0276 121 ASP A OD2 
971  N N   . PHE A 122 ? 0.8986 0.8023 0.9406 -0.1122 0.4015  0.0031  122 PHE A N   
972  C CA  . PHE A 122 ? 0.8808 0.7672 0.9077 -0.0874 0.3857  0.0094  122 PHE A CA  
973  C C   . PHE A 122 ? 0.9665 0.8525 0.9861 -0.0799 0.4023  0.0039  122 PHE A C   
974  O O   . PHE A 122 ? 0.9193 0.8194 0.9576 -0.0583 0.3948  0.0010  122 PHE A O   
975  C CB  . PHE A 122 ? 0.9344 0.7683 0.9114 -0.0877 0.3715  0.0231  122 PHE A CB  
976  C CG  . PHE A 122 ? 0.8413 0.6578 0.8028 -0.0657 0.3567  0.0285  122 PHE A CG  
977  C CD1 . PHE A 122 ? 0.8228 0.6611 0.8133 -0.0469 0.3399  0.0273  122 PHE A CD1 
978  C CD2 . PHE A 122 ? 0.8145 0.5916 0.7307 -0.0653 0.3591  0.0346  122 PHE A CD2 
979  C CE1 . PHE A 122 ? 0.7889 0.6102 0.7652 -0.0295 0.3283  0.0316  122 PHE A CE1 
980  C CE2 . PHE A 122 ? 0.8402 0.6039 0.7450 -0.0474 0.3455  0.0379  122 PHE A CE2 
981  C CZ  . PHE A 122 ? 0.7849 0.5706 0.7208 -0.0301 0.3313  0.0361  122 PHE A CZ  
982  N N   . GLU A 123 ? 0.9617 0.8279 0.9505 -0.0983 0.4256  0.0023  123 GLU A N   
983  C CA  . GLU A 123 ? 0.9665 0.8299 0.9436 -0.0934 0.4439  -0.0047 123 GLU A CA  
984  C C   . GLU A 123 ? 0.8941 0.8116 0.9323 -0.0797 0.4525  -0.0200 123 GLU A C   
985  O O   . GLU A 123 ? 0.8546 0.7730 0.8960 -0.0617 0.4541  -0.0248 123 GLU A O   
986  C CB  . GLU A 123 ? 1.0562 0.8947 0.9930 -0.1182 0.4663  -0.0060 123 GLU A CB  
987  C CG  . GLU A 123 ? 1.2077 1.0388 1.1252 -0.1138 0.4790  -0.0145 123 GLU A CG  
988  C CD  . GLU A 123 ? 1.3814 1.1936 1.2635 -0.1375 0.4944  -0.0179 123 GLU A CD  
989  O OE1 . GLU A 123 ? 1.5377 1.3327 1.4007 -0.1564 0.4927  -0.0109 123 GLU A OE1 
990  O OE2 . GLU A 123 ? 1.3434 1.1555 1.2152 -0.1373 0.5086  -0.0279 123 GLU A OE2 
991  N N   . LYS A 124 ? 0.8571 0.8198 0.9456 -0.0876 0.4571  -0.0282 124 LYS A N   
992  C CA  . LYS A 124 ? 0.8101 0.8282 0.9638 -0.0714 0.4599  -0.0422 124 LYS A CA  
993  C C   . LYS A 124 ? 0.7929 0.8147 0.9629 -0.0420 0.4307  -0.0363 124 LYS A C   
994  O O   . LYS A 124 ? 0.8477 0.8761 1.0318 -0.0211 0.4321  -0.0417 124 LYS A O   
995  C CB  . LYS A 124 ? 0.7387 0.8059 0.9440 -0.0867 0.4652  -0.0514 124 LYS A CB  
996  C CG  . LYS A 124 ? 0.8816 0.9445 1.0708 -0.1183 0.4932  -0.0576 124 LYS A CG  
997  C CD  . LYS A 124 ? 0.8955 1.0031 1.1325 -0.1367 0.4950  -0.0659 124 LYS A CD  
998  C CE  . LYS A 124 ? 1.0228 1.1144 1.2310 -0.1671 0.5112  -0.0692 124 LYS A CE  
999  N NZ  . LYS A 124 ? 1.1382 1.2617 1.3814 -0.1891 0.5108  -0.0750 124 LYS A NZ  
1000 N N   . ALA A 125 ? 0.8111 0.8256 0.9767 -0.0411 0.4052  -0.0256 125 ALA A N   
1001 C CA  . ALA A 125 ? 0.7500 0.7651 0.9260 -0.0164 0.3785  -0.0193 125 ALA A CA  
1002 C C   . ALA A 125 ? 0.7709 0.7462 0.9088 -0.0020 0.3764  -0.0136 125 ALA A C   
1003 O O   . ALA A 125 ? 0.8056 0.7877 0.9608 0.0202  0.3686  -0.0153 125 ALA A O   
1004 C CB  . ALA A 125 ? 0.7425 0.7479 0.9081 -0.0221 0.3556  -0.0093 125 ALA A CB  
1005 N N   . PHE A 126 ? 0.8169 0.7490 0.9022 -0.0145 0.3823  -0.0070 126 PHE A N   
1006 C CA  . PHE A 126 ? 0.7566 0.6523 0.8051 -0.0036 0.3797  -0.0029 126 PHE A CA  
1007 C C   . PHE A 126 ? 0.8270 0.7339 0.8895 0.0068  0.3979  -0.0151 126 PHE A C   
1008 O O   . PHE A 126 ? 0.8537 0.7560 0.9225 0.0266  0.3897  -0.0160 126 PHE A O   
1009 C CB  . PHE A 126 ? 0.8232 0.6750 0.8154 -0.0204 0.3834  0.0050  126 PHE A CB  
1010 C CG  . PHE A 126 ? 0.8179 0.6336 0.7711 -0.0121 0.3793  0.0081  126 PHE A CG  
1011 C CD1 . PHE A 126 ? 0.8473 0.6532 0.7818 -0.0141 0.3989  -0.0002 126 PHE A CD1 
1012 C CD2 . PHE A 126 ? 0.8447 0.6372 0.7799 -0.0040 0.3568  0.0180  126 PHE A CD2 
1013 C CE1 . PHE A 126 ? 0.8710 0.6436 0.7681 -0.0084 0.3938  0.0016  126 PHE A CE1 
1014 C CE2 . PHE A 126 ? 0.8831 0.6458 0.7857 0.0018  0.3521  0.0196  126 PHE A CE2 
1015 C CZ  . PHE A 126 ? 0.8535 0.6057 0.7361 -0.0007 0.3695  0.0115  126 PHE A CZ  
1016 N N   . ASN A 127 ? 0.7962 0.7160 0.8630 -0.0073 0.4245  -0.0255 127 ASN A N   
1017 C CA  . ASN A 127 ? 0.8609 0.7907 0.9405 0.0015  0.4459  -0.0398 127 ASN A CA  
1018 C C   . ASN A 127 ? 0.8169 0.7863 0.9571 0.0260  0.4390  -0.0476 127 ASN A C   
1019 O O   . ASN A 127 ? 0.7258 0.6965 0.8766 0.0406  0.4506  -0.0580 127 ASN A O   
1020 C CB  . ASN A 127 ? 0.8271 0.7693 0.9056 -0.0204 0.4784  -0.0510 127 ASN A CB  
1021 C CG  . ASN A 127 ? 0.9640 0.8575 0.9724 -0.0424 0.4841  -0.0431 127 ASN A CG  
1022 O OD1 . ASN A 127 ? 0.9394 0.7916 0.9016 -0.0378 0.4747  -0.0347 127 ASN A OD1 
1023 N ND2 . ASN A 127 ? 1.0364 0.9338 1.0363 -0.0662 0.4957  -0.0457 127 ASN A ND2 
1024 N N   . ALA A 128 ? 0.7662 0.7656 0.9442 0.0311  0.4196  -0.0430 128 ALA A N   
1025 C CA  . ALA A 128 ? 0.7403 0.7757 0.9736 0.0553  0.4079  -0.0480 128 ALA A CA  
1026 C C   . ALA A 128 ? 0.8235 0.8330 1.0422 0.0757  0.3813  -0.0361 128 ALA A C   
1027 O O   . ALA A 128 ? 0.8643 0.8965 1.1212 0.0959  0.3656  -0.0359 128 ALA A O   
1028 C CB  . ALA A 128 ? 0.6836 0.7676 0.9656 0.0492  0.3996  -0.0503 128 ALA A CB  
1029 N N   . ARG A 129 ? 0.7427 0.7052 0.9074 0.0706  0.3756  -0.0264 129 ARG A N   
1030 C CA  . ARG A 129 ? 0.6928 0.6307 0.8424 0.0855  0.3522  -0.0154 129 ARG A CA  
1031 C C   . ARG A 129 ? 0.7828 0.6781 0.8920 0.0896  0.3574  -0.0153 129 ARG A C   
1032 O O   . ARG A 129 ? 0.7749 0.6606 0.8915 0.1083  0.3535  -0.0171 129 ARG A O   
1033 C CB  . ARG A 129 ? 0.7770 0.7049 0.9069 0.0739  0.3333  -0.0026 129 ARG A CB  
1034 C CG  . ARG A 129 ? 0.6814 0.6470 0.8488 0.0731  0.3207  -0.0015 129 ARG A CG  
1035 C CD  . ARG A 129 ? 0.7575 0.7093 0.9005 0.0579  0.3076  0.0082  129 ARG A CD  
1036 N NE  . ARG A 129 ? 0.7797 0.7588 0.9503 0.0607  0.2892  0.0107  129 ARG A NE  
1037 C CZ  . ARG A 129 ? 0.7471 0.7656 0.9532 0.0524  0.2913  0.0039  129 ARG A CZ  
1038 N NH1 . ARG A 129 ? 0.7617 0.7979 0.9822 0.0398  0.3133  -0.0060 129 ARG A NH1 
1039 N NH2 . ARG A 129 ? 0.7555 0.7963 0.9823 0.0552  0.2710  0.0064  129 ARG A NH2 
1040 N N   . PHE A 130 ? 0.7432 0.6111 0.8088 0.0721  0.3650  -0.0132 130 PHE A N   
1041 C CA  . PHE A 130 ? 0.8204 0.6471 0.8439 0.0733  0.3625  -0.0110 130 PHE A CA  
1042 C C   . PHE A 130 ? 0.8418 0.6574 0.8579 0.0788  0.3824  -0.0241 130 PHE A C   
1043 O O   . PHE A 130 ? 0.8434 0.6314 0.8406 0.0874  0.3777  -0.0247 130 PHE A O   
1044 C CB  . PHE A 130 ? 0.8064 0.6080 0.7863 0.0542  0.3590  -0.0033 130 PHE A CB  
1045 C CG  . PHE A 130 ? 0.9050 0.7021 0.8821 0.0529  0.3366  0.0092  130 PHE A CG  
1046 C CD1 . PHE A 130 ? 0.8430 0.6615 0.8383 0.0453  0.3319  0.0134  130 PHE A CD1 
1047 C CD2 . PHE A 130 ? 0.8884 0.6605 0.8459 0.0583  0.3217  0.0150  130 PHE A CD2 
1048 C CE1 . PHE A 130 ? 0.8476 0.6603 0.8390 0.0440  0.3134  0.0229  130 PHE A CE1 
1049 C CE2 . PHE A 130 ? 0.7468 0.5161 0.7034 0.0569  0.3041  0.0244  130 PHE A CE2 
1050 C CZ  . PHE A 130 ? 0.8103 0.5989 0.7828 0.0503  0.3002  0.0282  130 PHE A CZ  
1051 N N   . PRO A 131 ? 0.8551 0.6897 0.8840 0.0728  0.4065  -0.0362 131 PRO A N   
1052 C CA  . PRO A 131 ? 0.9073 0.7298 0.9278 0.0781  0.4279  -0.0510 131 PRO A CA  
1053 C C   . PRO A 131 ? 0.8169 0.6338 0.8593 0.1028  0.4212  -0.0549 131 PRO A C   
1054 O O   . PRO A 131 ? 0.7759 0.6230 0.8683 0.1201  0.4188  -0.0580 131 PRO A O   
1055 C CB  . PRO A 131 ? 0.8107 0.6694 0.8629 0.0718  0.4537  -0.0641 131 PRO A CB  
1056 C CG  . PRO A 131 ? 0.8335 0.7019 0.8770 0.0510  0.4496  -0.0545 131 PRO A CG  
1057 C CD  . PRO A 131 ? 0.8111 0.6749 0.8568 0.0573  0.4179  -0.0381 131 PRO A CD  
1058 N N   . GLY A 132 ? 0.8626 0.6394 0.8671 0.1043  0.4168  -0.0545 132 GLY A N   
1059 C CA  . GLY A 132 ? 0.8162 0.5777 0.8329 0.1251  0.4131  -0.0587 132 GLY A CA  
1060 C C   . GLY A 132 ? 0.8390 0.6018 0.8750 0.1390  0.3872  -0.0449 132 GLY A C   
1061 O O   . GLY A 132 ? 0.9202 0.6763 0.9762 0.1591  0.3840  -0.0472 132 GLY A O   
1062 N N   . CYS A 133 ? 0.8367 0.6045 0.8641 0.1285  0.3692  -0.0307 133 CYS A N   
1063 C CA  . CYS A 133 ? 0.8177 0.5885 0.8610 0.1392  0.3464  -0.0179 133 CYS A CA  
1064 C C   . CYS A 133 ? 0.8483 0.5796 0.8642 0.1430  0.3355  -0.0127 133 CYS A C   
1065 O O   . CYS A 133 ? 0.9081 0.6346 0.9360 0.1558  0.3213  -0.0046 133 CYS A O   
1066 C CB  . CYS A 133 ? 0.7928 0.5809 0.8350 0.1255  0.3335  -0.0068 133 CYS A CB  
1067 S SG  . CYS A 133 ? 0.8834 0.6455 0.8762 0.1024  0.3313  -0.0017 133 CYS A SG  
1068 N N   . MET A 134 ? 0.8455 0.5477 0.8236 0.1312  0.3415  -0.0171 134 MET A N   
1069 C CA  . MET A 134 ? 0.8740 0.5404 0.8275 0.1314  0.3327  -0.0144 134 MET A CA  
1070 C C   . MET A 134 ? 0.9366 0.5774 0.8856 0.1421  0.3453  -0.0265 134 MET A C   
1071 O O   . MET A 134 ? 0.9508 0.5582 0.8741 0.1381  0.3421  -0.0278 134 MET A O   
1072 C CB  . MET A 134 ? 0.8279 0.4792 0.7451 0.1116  0.3277  -0.0124 134 MET A CB  
1073 C CG  . MET A 134 ? 0.8322 0.5018 0.7517 0.1018  0.3146  -0.0009 134 MET A CG  
1074 S SD  . MET A 134 ? 0.8113 0.4614 0.6934 0.0834  0.3054  0.0012  134 MET A SD  
1075 C CE  . MET A 134 ? 0.8336 0.5063 0.7277 0.0773  0.2923  0.0136  134 MET A CE  
1076 N N   . LYS A 135 ? 0.9102 0.5660 0.8852 0.1553  0.3603  -0.0366 135 LYS A N   
1077 C CA  . LYS A 135 ? 0.9158 0.5463 0.8879 0.1666  0.3751  -0.0505 135 LYS A CA  
1078 C C   . LYS A 135 ? 0.9881 0.5845 0.9545 0.1776  0.3627  -0.0441 135 LYS A C   
1079 O O   . LYS A 135 ? 0.9609 0.5645 0.9500 0.1913  0.3486  -0.0324 135 LYS A O   
1080 C CB  . LYS A 135 ? 0.9343 0.5962 0.9488 0.1820  0.3869  -0.0600 135 LYS A CB  
1081 C CG  . LYS A 135 ? 1.0154 0.6650 1.0236 0.1830  0.4015  -0.0770 135 LYS A CG  
1082 C CD  . LYS A 135 ? 1.0398 0.6862 1.0136 0.1606  0.4186  -0.0874 135 LYS A CD  
1083 C CE  . LYS A 135 ? 1.1578 0.7866 1.1185 0.1598  0.4334  -0.1049 135 LYS A CE  
1084 N NZ  . LYS A 135 ? 1.3627 1.0214 1.3704 0.1768  0.4431  -0.1155 135 LYS A NZ  
1085 N N   . GLY A 136 ? 1.0320 0.5927 0.9652 0.1680  0.3650  -0.0508 136 GLY A N   
1086 C CA  . GLY A 136 ? 0.9523 0.4796 0.8759 0.1727  0.3538  -0.0453 136 GLY A CA  
1087 C C   . GLY A 136 ? 0.9763 0.4893 0.8835 0.1634  0.3396  -0.0316 136 GLY A C   
1088 O O   . GLY A 136 ? 0.9398 0.4259 0.8387 0.1652  0.3305  -0.0253 136 GLY A O   
1089 N N   . ARG A 137 ? 1.0019 0.5398 0.9052 0.1491  0.3328  -0.0253 137 ARG A N   
1090 C CA  . ARG A 137 ? 0.8858 0.4203 0.7768 0.1363  0.3171  -0.0134 137 ARG A CA  
1091 C C   . ARG A 137 ? 0.9448 0.4737 0.8082 0.1149  0.3166  -0.0194 137 ARG A C   
1092 O O   . ARG A 137 ? 0.9633 0.4932 0.8137 0.1090  0.3266  -0.0305 137 ARG A O   
1093 C CB  . ARG A 137 ? 0.8731 0.4426 0.7851 0.1381  0.3057  -0.0004 137 ARG A CB  
1094 C CG  . ARG A 137 ? 0.9135 0.4936 0.8539 0.1588  0.3015  0.0064  137 ARG A CG  
1095 C CD  . ARG A 137 ? 0.8149 0.4249 0.7691 0.1565  0.2878  0.0190  137 ARG A CD  
1096 N NE  . ARG A 137 ? 0.8561 0.4780 0.8363 0.1757  0.2798  0.0260  137 ARG A NE  
1097 C CZ  . ARG A 137 ? 0.9507 0.5497 0.9247 0.1848  0.2684  0.0366  137 ARG A CZ  
1098 N NH1 . ARG A 137 ? 0.8337 0.3966 0.7780 0.1750  0.2667  0.0406  137 ARG A NH1 
1099 N NH2 . ARG A 137 ? 0.9769 0.5894 0.9747 0.2033  0.2581  0.0433  137 ARG A NH2 
1100 N N   . THR A 138 ? 0.8303 0.3533 0.6846 0.1032  0.3046  -0.0124 138 THR A N   
1101 C CA  . THR A 138 ? 0.9084 0.4317 0.7432 0.0845  0.2993  -0.0166 138 THR A CA  
1102 C C   . THR A 138 ? 0.8675 0.4230 0.7103 0.0793  0.2911  -0.0089 138 THR A C   
1103 O O   . THR A 138 ? 0.8851 0.4584 0.7465 0.0849  0.2854  0.0017  138 THR A O   
1104 C CB  . THR A 138 ? 0.8406 0.3443 0.6670 0.0738  0.2919  -0.0154 138 THR A CB  
1105 O OG1 . THR A 138 ? 0.9767 0.4451 0.7887 0.0738  0.3003  -0.0253 138 THR A OG1 
1106 C CG2 . THR A 138 ? 0.9096 0.4249 0.7271 0.0566  0.2818  -0.0178 138 THR A CG2 
1107 N N   . MET A 139 ? 0.8583 0.4180 0.6839 0.0684  0.2899  -0.0141 139 MET A N   
1108 C CA  . MET A 139 ? 0.8131 0.3956 0.6411 0.0622  0.2809  -0.0067 139 MET A CA  
1109 C C   . MET A 139 ? 0.8459 0.4254 0.6668 0.0504  0.2668  -0.0062 139 MET A C   
1110 O O   . MET A 139 ? 0.9134 0.4799 0.7136 0.0412  0.2635  -0.0143 139 MET A O   
1111 C CB  . MET A 139 ? 0.8211 0.4082 0.6328 0.0584  0.2882  -0.0109 139 MET A CB  
1112 C CG  . MET A 139 ? 0.7587 0.3611 0.5669 0.0509  0.2779  -0.0027 139 MET A CG  
1113 S SD  . MET A 139 ? 0.8560 0.4544 0.6330 0.0421  0.2859  -0.0059 139 MET A SD  
1114 C CE  . MET A 139 ? 0.8557 0.4731 0.6564 0.0513  0.3060  -0.0071 139 MET A CE  
1115 N N   . TYR A 140 ? 0.7565 0.3490 0.5955 0.0504  0.2584  0.0022  140 TYR A N   
1116 C CA  . TYR A 140 ? 0.7277 0.3240 0.5686 0.0404  0.2460  0.0018  140 TYR A CA  
1117 C C   . TYR A 140 ? 0.7706 0.3821 0.6091 0.0374  0.2364  0.0058  140 TYR A C   
1118 O O   . TYR A 140 ? 0.7952 0.4193 0.6409 0.0424  0.2384  0.0130  140 TYR A O   
1119 C CB  . TYR A 140 ? 0.7257 0.3269 0.5855 0.0409  0.2444  0.0073  140 TYR A CB  
1120 C CG  . TYR A 140 ? 0.7407 0.3206 0.5981 0.0440  0.2531  0.0060  140 TYR A CG  
1121 C CD1 . TYR A 140 ? 0.8216 0.3825 0.6709 0.0345  0.2540  -0.0020 140 TYR A CD1 
1122 C CD2 . TYR A 140 ? 0.7386 0.3160 0.6016 0.0563  0.2593  0.0127  140 TYR A CD2 
1123 C CE1 . TYR A 140 ? 0.8284 0.3631 0.6718 0.0368  0.2624  -0.0026 140 TYR A CE1 
1124 C CE2 . TYR A 140 ? 0.8097 0.3626 0.6682 0.0611  0.2653  0.0129  140 TYR A CE2 
1125 C CZ  . TYR A 140 ? 0.8681 0.3970 0.7149 0.0512  0.2677  0.0057  140 TYR A CZ  
1126 O OH  . TYR A 140 ? 0.9466 0.4448 0.7855 0.0553  0.2742  0.0067  140 TYR A OH  
1127 N N   . VAL A 141 ? 0.7778 0.3868 0.6059 0.0293  0.2250  0.0010  141 VAL A N   
1128 C CA  . VAL A 141 ? 0.7783 0.3961 0.6014 0.0274  0.2126  0.0055  141 VAL A CA  
1129 C C   . VAL A 141 ? 0.7803 0.4131 0.6282 0.0258  0.2006  0.0066  141 VAL A C   
1130 O O   . VAL A 141 ? 0.7770 0.4106 0.6300 0.0195  0.1921  -0.0008 141 VAL A O   
1131 C CB  . VAL A 141 ? 0.8113 0.4152 0.6030 0.0209  0.2055  0.0001  141 VAL A CB  
1132 C CG1 . VAL A 141 ? 0.7613 0.3687 0.5434 0.0205  0.1913  0.0074  141 VAL A CG1 
1133 C CG2 . VAL A 141 ? 0.7794 0.3679 0.5472 0.0215  0.2219  -0.0040 141 VAL A CG2 
1134 N N   . ILE A 142 ? 0.8042 0.4501 0.6692 0.0307  0.2008  0.0142  142 ILE A N   
1135 C CA  . ILE A 142 ? 0.7162 0.3771 0.6074 0.0301  0.1936  0.0139  142 ILE A CA  
1136 C C   . ILE A 142 ? 0.7673 0.4341 0.6600 0.0321  0.1783  0.0167  142 ILE A C   
1137 O O   . ILE A 142 ? 0.8110 0.4775 0.7001 0.0364  0.1789  0.0244  142 ILE A O   
1138 C CB  . ILE A 142 ? 0.7069 0.3756 0.6137 0.0339  0.2036  0.0192  142 ILE A CB  
1139 C CG1 . ILE A 142 ? 0.7436 0.4022 0.6444 0.0349  0.2163  0.0192  142 ILE A CG1 
1140 C CG2 . ILE A 142 ? 0.7245 0.4066 0.6562 0.0313  0.2005  0.0159  142 ILE A CG2 
1141 C CD1 . ILE A 142 ? 0.6751 0.3395 0.5858 0.0389  0.2231  0.0256  142 ILE A CD1 
1142 N N   . PRO A 143 ? 0.7898 0.4611 0.6884 0.0292  0.1634  0.0108  143 PRO A N   
1143 C CA  . PRO A 143 ? 0.7946 0.4715 0.6997 0.0341  0.1461  0.0141  143 PRO A CA  
1144 C C   . PRO A 143 ? 0.8604 0.5578 0.8048 0.0373  0.1446  0.0107  143 PRO A C   
1145 O O   . PRO A 143 ? 0.8721 0.5835 0.8399 0.0324  0.1443  0.0011  143 PRO A O   
1146 C CB  . PRO A 143 ? 0.8024 0.4752 0.6944 0.0300  0.1288  0.0084  143 PRO A CB  
1147 C CG  . PRO A 143 ? 0.7363 0.4101 0.6320 0.0210  0.1379  -0.0021 143 PRO A CG  
1148 C CD  . PRO A 143 ? 0.7496 0.4211 0.6508 0.0214  0.1602  0.0002  143 PRO A CD  
1149 N N   . PHE A 144 ? 0.7941 0.4928 0.7459 0.0440  0.1453  0.0171  144 PHE A N   
1150 C CA  . PHE A 144 ? 0.7728 0.4890 0.7596 0.0466  0.1487  0.0124  144 PHE A CA  
1151 C C   . PHE A 144 ? 0.7829 0.4984 0.7790 0.0562  0.1363  0.0163  144 PHE A C   
1152 O O   . PHE A 144 ? 0.8251 0.5225 0.7962 0.0595  0.1326  0.0261  144 PHE A O   
1153 C CB  . PHE A 144 ? 0.7607 0.4770 0.7481 0.0438  0.1684  0.0143  144 PHE A CB  
1154 C CG  . PHE A 144 ? 0.7544 0.4588 0.7226 0.0470  0.1731  0.0242  144 PHE A CG  
1155 C CD1 . PHE A 144 ? 0.8311 0.5229 0.7721 0.0450  0.1782  0.0298  144 PHE A CD1 
1156 C CD2 . PHE A 144 ? 0.7059 0.4122 0.6849 0.0510  0.1739  0.0261  144 PHE A CD2 
1157 C CE1 . PHE A 144 ? 0.7858 0.4707 0.7135 0.0460  0.1837  0.0373  144 PHE A CE1 
1158 C CE2 . PHE A 144 ? 0.7093 0.4051 0.6716 0.0514  0.1785  0.0339  144 PHE A CE2 
1159 C CZ  . PHE A 144 ? 0.7201 0.4070 0.6581 0.0483  0.1834  0.0395  144 PHE A CZ  
1160 N N   . SER A 145 ? 0.7846 0.5190 0.8178 0.0603  0.1314  0.0079  145 SER A N   
1161 C CA  . SER A 145 ? 0.8216 0.5559 0.8711 0.0718  0.1199  0.0094  145 SER A CA  
1162 C C   . SER A 145 ? 0.7849 0.5250 0.8531 0.0726  0.1366  0.0059  145 SER A C   
1163 O O   . SER A 145 ? 0.7441 0.5008 0.8324 0.0661  0.1508  -0.0033 145 SER A O   
1164 C CB  . SER A 145 ? 0.8471 0.6010 0.9305 0.0781  0.1009  0.0003  145 SER A CB  
1165 O OG  . SER A 145 ? 0.7832 0.5393 0.8911 0.0915  0.0919  -0.0004 145 SER A OG  
1166 N N   . MET A 146 ? 0.7747 0.4984 0.8327 0.0789  0.1354  0.0130  146 MET A N   
1167 C CA  . MET A 146 ? 0.8212 0.5474 0.8944 0.0798  0.1493  0.0085  146 MET A CA  
1168 C C   . MET A 146 ? 0.8767 0.6123 0.9869 0.0921  0.1397  0.0001  146 MET A C   
1169 O O   . MET A 146 ? 0.8884 0.6086 0.9948 0.1032  0.1228  0.0063  146 MET A O   
1170 C CB  . MET A 146 ? 0.8181 0.5210 0.8611 0.0780  0.1549  0.0190  146 MET A CB  
1171 C CG  . MET A 146 ? 0.7369 0.4357 0.7512 0.0675  0.1653  0.0254  146 MET A CG  
1172 S SD  . MET A 146 ? 0.7112 0.4286 0.7367 0.0585  0.1832  0.0174  146 MET A SD  
1173 C CE  . MET A 146 ? 0.8162 0.5330 0.8509 0.0578  0.1947  0.0126  146 MET A CE  
1174 N N   . GLY A 147 ? 0.9002 0.6601 1.0461 0.0904  0.1509  -0.0141 147 GLY A N   
1175 C CA  . GLY A 147 ? 0.9046 0.6809 1.0950 0.1024  0.1436  -0.0257 147 GLY A CA  
1176 C C   . GLY A 147 ? 0.9405 0.7408 1.1583 0.1048  0.1279  -0.0323 147 GLY A C   
1177 O O   . GLY A 147 ? 0.9025 0.7001 1.0980 0.0979  0.1200  -0.0263 147 GLY A O   
1178 N N   . PRO A 148 ? 1.0287 0.8543 1.2976 0.1145  0.1234  -0.0464 148 PRO A N   
1179 C CA  . PRO A 148 ? 1.0158 0.8704 1.3181 0.1160  0.1069  -0.0550 148 PRO A CA  
1180 C C   . PRO A 148 ? 1.0419 0.8794 1.3170 0.1233  0.0768  -0.0414 148 PRO A C   
1181 O O   . PRO A 148 ? 1.1421 0.9498 1.3907 0.1343  0.0640  -0.0281 148 PRO A O   
1182 C CB  . PRO A 148 ? 0.9718 0.8533 1.3356 0.1304  0.1046  -0.0712 148 PRO A CB  
1183 C CG  . PRO A 148 ? 0.9954 0.8672 1.3576 0.1283  0.1314  -0.0759 148 PRO A CG  
1184 C CD  . PRO A 148 ? 1.0179 0.8486 1.3192 0.1242  0.1337  -0.0571 148 PRO A CD  
1185 N N   . LEU A 149 ? 0.9831 0.8372 1.2616 0.1151  0.0662  -0.0451 149 LEU A N   
1186 C CA  . LEU A 149 ? 1.0653 0.9043 1.3158 0.1202  0.0369  -0.0342 149 LEU A CA  
1187 C C   . LEU A 149 ? 1.1769 1.0201 1.4561 0.1421  0.0079  -0.0338 149 LEU A C   
1188 O O   . LEU A 149 ? 1.1891 1.0640 1.5277 0.1517  0.0066  -0.0485 149 LEU A O   
1189 C CB  . LEU A 149 ? 0.9907 0.8491 1.2437 0.1062  0.0312  -0.0419 149 LEU A CB  
1190 C CG  . LEU A 149 ? 1.0604 0.8968 1.2629 0.0886  0.0488  -0.0348 149 LEU A CG  
1191 C CD1 . LEU A 149 ? 1.0172 0.8655 1.2166 0.0759  0.0397  -0.0420 149 LEU A CD1 
1192 C CD2 . LEU A 149 ? 1.0660 0.8616 1.2119 0.0930  0.0445  -0.0158 149 LEU A CD2 
1193 N N   . GLY A 150 ? 1.2181 1.0275 1.4542 0.1503  -0.0151 -0.0168 150 GLY A N   
1194 C CA  . GLY A 150 ? 1.2143 1.0157 1.4661 0.1729  -0.0445 -0.0119 150 GLY A CA  
1195 C C   . GLY A 150 ? 1.3591 1.1483 1.6304 0.1874  -0.0342 -0.0119 150 GLY A C   
1196 O O   . GLY A 150 ? 1.4331 1.2022 1.7055 0.2072  -0.0577 -0.0037 150 GLY A O   
1197 N N   . SER A 151 ? 1.3101 1.1078 1.5943 0.1782  -0.0008 -0.0208 151 SER A N   
1198 C CA  . SER A 151 ? 1.3450 1.1275 1.6419 0.1894  0.0114  -0.0221 151 SER A CA  
1199 C C   . SER A 151 ? 1.4985 1.2277 1.7398 0.1952  0.0008  -0.0009 151 SER A C   
1200 O O   . SER A 151 ? 1.4605 1.1656 1.6464 0.1814  0.0032  0.0128  151 SER A O   
1201 C CB  . SER A 151 ? 1.2823 1.0742 1.5820 0.1734  0.0492  -0.0317 151 SER A CB  
1202 O OG  . SER A 151 ? 1.3139 1.0871 1.6186 0.1817  0.0617  -0.0334 151 SER A OG  
1203 N N   . PRO A 152 ? 1.6811 1.3892 1.9352 0.2146  -0.0095 0.0017  152 PRO A N   
1204 C CA  . PRO A 152 ? 1.7174 1.3698 1.9150 0.2181  -0.0193 0.0226  152 PRO A CA  
1205 C C   . PRO A 152 ? 1.7121 1.3411 1.8637 0.1978  0.0092  0.0294  152 PRO A C   
1206 O O   . PRO A 152 ? 1.7946 1.3928 1.8901 0.1875  0.0059  0.0458  152 PRO A O   
1207 C CB  . PRO A 152 ? 1.7487 1.3862 1.9794 0.2425  -0.0294 0.0194  152 PRO A CB  
1208 C CG  . PRO A 152 ? 1.6696 1.3523 1.9658 0.2448  -0.0086 -0.0052 152 PRO A CG  
1209 C CD  . PRO A 152 ? 1.6435 1.3742 1.9624 0.2326  -0.0075 -0.0155 152 PRO A CD  
1210 N N   . LEU A 153 ? 1.5117 1.1557 1.6857 0.1911  0.0372  0.0164  153 LEU A N   
1211 C CA  . LEU A 153 ? 1.4567 1.0833 1.5925 0.1724  0.0622  0.0213  153 LEU A CA  
1212 C C   . LEU A 153 ? 1.3064 0.9584 1.4304 0.1535  0.0757  0.0192  153 LEU A C   
1213 O O   . LEU A 153 ? 1.2322 0.8885 1.3465 0.1394  0.0993  0.0158  153 LEU A O   
1214 C CB  . LEU A 153 ? 1.3568 0.9842 1.5159 0.1731  0.0842  0.0086  153 LEU A CB  
1215 C CG  . LEU A 153 ? 1.3282 0.9214 1.4925 0.1899  0.0765  0.0102  153 LEU A CG  
1216 C CD1 . LEU A 153 ? 1.0769 0.6782 1.2698 0.1894  0.1006  -0.0076 153 LEU A CD1 
1217 C CD2 . LEU A 153 ? 1.1385 0.6812 1.2453 0.1838  0.0716  0.0300  153 LEU A CD2 
1218 N N   . ALA A 154 ? 1.2628 0.9295 1.3862 0.1532  0.0597  0.0211  154 ALA A N   
1219 C CA  . ALA A 154 ? 1.2389 0.9248 1.3498 0.1366  0.0706  0.0192  154 ALA A CA  
1220 C C   . ALA A 154 ? 1.1518 0.8096 1.2071 0.1285  0.0638  0.0355  154 ALA A C   
1221 O O   . ALA A 154 ? 1.1728 0.8134 1.2098 0.1359  0.0402  0.0445  154 ALA A O   
1222 C CB  . ALA A 154 ? 1.1988 0.9217 1.3488 0.1388  0.0606  0.0069  154 ALA A CB  
1223 N N   . LYS A 155 ? 1.0129 0.6662 1.0412 0.1135  0.0841  0.0387  155 LYS A N   
1224 C CA  . LYS A 155 ? 0.9937 0.6240 0.9725 0.1042  0.0836  0.0514  155 LYS A CA  
1225 C C   . LYS A 155 ? 0.9405 0.5898 0.9138 0.0920  0.0951  0.0466  155 LYS A C   
1226 O O   . LYS A 155 ? 0.8524 0.5243 0.8495 0.0873  0.1106  0.0371  155 LYS A O   
1227 C CB  . LYS A 155 ? 1.0140 0.6182 0.9652 0.0981  0.0972  0.0601  155 LYS A CB  
1228 C CG  . LYS A 155 ? 1.1306 0.7090 1.0839 0.1092  0.0875  0.0649  155 LYS A CG  
1229 C CD  . LYS A 155 ? 1.2273 0.7739 1.1446 0.0997  0.0987  0.0751  155 LYS A CD  
1230 C CE  . LYS A 155 ? 1.3770 0.8931 1.2447 0.0941  0.0896  0.0899  155 LYS A CE  
1231 N NZ  . LYS A 155 ? 1.3415 0.8316 1.1993 0.1084  0.0628  0.0982  155 LYS A NZ  
1232 N N   . ILE A 156 ? 0.9265 0.5628 0.8649 0.0868  0.0877  0.0533  156 ILE A N   
1233 C CA  . ILE A 156 ? 0.9249 0.5745 0.8565 0.0773  0.0950  0.0481  156 ILE A CA  
1234 C C   . ILE A 156 ? 0.8729 0.5087 0.7705 0.0670  0.1129  0.0544  156 ILE A C   
1235 O O   . ILE A 156 ? 0.9072 0.5183 0.7729 0.0651  0.1126  0.0645  156 ILE A O   
1236 C CB  . ILE A 156 ? 0.8452 0.4927 0.7647 0.0784  0.0733  0.0475  156 ILE A CB  
1237 C CG1 . ILE A 156 ? 0.8253 0.4971 0.7900 0.0881  0.0562  0.0379  156 ILE A CG1 
1238 C CG2 . ILE A 156 ? 0.8426 0.4944 0.7445 0.0669  0.0828  0.0428  156 ILE A CG2 
1239 C CD1 . ILE A 156 ? 0.9031 0.5770 0.8603 0.0892  0.0310  0.0360  156 ILE A CD1 
1240 N N   . GLY A 157 ? 0.7485 0.3996 0.6536 0.0604  0.1290  0.0481  157 GLY A N   
1241 C CA  . GLY A 157 ? 0.8564 0.5002 0.7375 0.0527  0.1455  0.0518  157 GLY A CA  
1242 C C   . GLY A 157 ? 0.8805 0.5296 0.7543 0.0477  0.1507  0.0459  157 GLY A C   
1243 O O   . GLY A 157 ? 0.8164 0.4776 0.7079 0.0479  0.1450  0.0380  157 GLY A O   
1244 N N   . ILE A 158 ? 0.8806 0.5200 0.7291 0.0424  0.1629  0.0487  158 ILE A N   
1245 C CA  . ILE A 158 ? 0.7865 0.4264 0.6255 0.0384  0.1711  0.0426  158 ILE A CA  
1246 C C   . ILE A 158 ? 0.7696 0.4165 0.6151 0.0379  0.1903  0.0429  158 ILE A C   
1247 O O   . ILE A 158 ? 0.7816 0.4235 0.6139 0.0357  0.1989  0.0477  158 ILE A O   
1248 C CB  . ILE A 158 ? 0.8109 0.4311 0.6109 0.0335  0.1670  0.0435  158 ILE A CB  
1249 C CG1 . ILE A 158 ? 0.8830 0.4978 0.6766 0.0346  0.1438  0.0426  158 ILE A CG1 
1250 C CG2 . ILE A 158 ? 0.8719 0.4902 0.6618 0.0296  0.1805  0.0359  158 ILE A CG2 
1251 C CD1 . ILE A 158 ? 0.9177 0.5482 0.7361 0.0343  0.1374  0.0320  158 ILE A CD1 
1252 N N   . GLU A 159 ? 0.7663 0.4245 0.6321 0.0394  0.1965  0.0380  159 GLU A N   
1253 C CA  . GLU A 159 ? 0.7203 0.3848 0.5927 0.0411  0.2110  0.0386  159 GLU A CA  
1254 C C   . GLU A 159 ? 0.7446 0.4012 0.6055 0.0410  0.2191  0.0332  159 GLU A C   
1255 O O   . GLU A 159 ? 0.7793 0.4307 0.6400 0.0393  0.2156  0.0274  159 GLU A O   
1256 C CB  . GLU A 159 ? 0.6368 0.3133 0.5334 0.0434  0.2128  0.0385  159 GLU A CB  
1257 C CG  . GLU A 159 ? 0.7136 0.3952 0.6152 0.0466  0.2237  0.0400  159 GLU A CG  
1258 C CD  . GLU A 159 ? 0.7300 0.4223 0.6472 0.0476  0.2242  0.0430  159 GLU A CD  
1259 O OE1 . GLU A 159 ? 0.7570 0.4523 0.6819 0.0453  0.2189  0.0424  159 GLU A OE1 
1260 O OE2 . GLU A 159 ? 0.6807 0.3782 0.6021 0.0510  0.2295  0.0453  159 GLU A OE2 
1261 N N   . LEU A 160 ? 0.7420 0.3979 0.5948 0.0421  0.2308  0.0337  160 LEU A N   
1262 C CA  . LEU A 160 ? 0.7309 0.3805 0.5784 0.0447  0.2418  0.0276  160 LEU A CA  
1263 C C   . LEU A 160 ? 0.7521 0.4135 0.6223 0.0524  0.2488  0.0296  160 LEU A C   
1264 O O   . LEU A 160 ? 0.6939 0.3699 0.5763 0.0540  0.2512  0.0342  160 LEU A O   
1265 C CB  . LEU A 160 ? 0.7242 0.3665 0.5496 0.0415  0.2518  0.0249  160 LEU A CB  
1266 C CG  . LEU A 160 ? 0.7471 0.3744 0.5414 0.0331  0.2439  0.0257  160 LEU A CG  
1267 C CD1 . LEU A 160 ? 0.7701 0.3881 0.5387 0.0281  0.2585  0.0223  160 LEU A CD1 
1268 C CD2 . LEU A 160 ? 0.8151 0.4310 0.5992 0.0305  0.2315  0.0204  160 LEU A CD2 
1269 N N   . THR A 161 ? 0.6890 0.3424 0.5634 0.0566  0.2510  0.0262  161 THR A N   
1270 C CA  . THR A 161 ? 0.6817 0.3414 0.5737 0.0649  0.2538  0.0299  161 THR A CA  
1271 C C   . THR A 161 ? 0.7443 0.3868 0.6325 0.0711  0.2606  0.0249  161 THR A C   
1272 O O   . THR A 161 ? 0.7409 0.3658 0.6143 0.0662  0.2612  0.0184  161 THR A O   
1273 C CB  . THR A 161 ? 0.7154 0.3791 0.6164 0.0623  0.2455  0.0351  161 THR A CB  
1274 O OG1 . THR A 161 ? 0.7487 0.4157 0.6602 0.0697  0.2465  0.0400  161 THR A OG1 
1275 C CG2 . THR A 161 ? 0.6998 0.3494 0.5940 0.0559  0.2420  0.0307  161 THR A CG2 
1276 N N   . ASP A 162 ? 0.6773 0.3243 0.5793 0.0823  0.2646  0.0276  162 ASP A N   
1277 C CA  . ASP A 162 ? 0.7488 0.3761 0.6494 0.0914  0.2700  0.0244  162 ASP A CA  
1278 C C   . ASP A 162 ? 0.8040 0.4202 0.7070 0.0948  0.2635  0.0322  162 ASP A C   
1279 O O   . ASP A 162 ? 0.7468 0.3478 0.6518 0.1060  0.2657  0.0336  162 ASP A O   
1280 C CB  . ASP A 162 ? 0.8596 0.4972 0.7749 0.1042  0.2792  0.0210  162 ASP A CB  
1281 C CG  . ASP A 162 ? 0.8024 0.4683 0.7413 0.1105  0.2742  0.0282  162 ASP A CG  
1282 O OD1 . ASP A 162 ? 0.7443 0.4185 0.6835 0.1042  0.2643  0.0358  162 ASP A OD1 
1283 O OD2 . ASP A 162 ? 0.7986 0.4796 0.7572 0.1214  0.2805  0.0250  162 ASP A OD2 
1284 N N   . SER A 163 ? 0.7759 0.3970 0.6769 0.0853  0.2561  0.0371  163 SER A N   
1285 C CA  . SER A 163 ? 0.7870 0.3985 0.6859 0.0858  0.2514  0.0451  163 SER A CA  
1286 C C   . SER A 163 ? 0.7581 0.3556 0.6460 0.0719  0.2515  0.0424  163 SER A C   
1287 O O   . SER A 163 ? 0.7287 0.3415 0.6210 0.0623  0.2482  0.0402  163 SER A O   
1288 C CB  . SER A 163 ? 0.7545 0.3892 0.6640 0.0868  0.2445  0.0524  163 SER A CB  
1289 O OG  . SER A 163 ? 0.8074 0.4312 0.7079 0.0830  0.2406  0.0591  163 SER A OG  
1290 N N   . PRO A 164 ? 0.7541 0.3230 0.6299 0.0701  0.2554  0.0418  164 PRO A N   
1291 C CA  . PRO A 164 ? 0.8513 0.4101 0.7203 0.0544  0.2570  0.0382  164 PRO A CA  
1292 C C   . PRO A 164 ? 0.8049 0.3736 0.6760 0.0478  0.2547  0.0443  164 PRO A C   
1293 O O   . PRO A 164 ? 0.8226 0.3990 0.6986 0.0347  0.2559  0.0389  164 PRO A O   
1294 C CB  . PRO A 164 ? 0.8639 0.3854 0.7172 0.0544  0.2632  0.0376  164 PRO A CB  
1295 C CG  . PRO A 164 ? 0.8807 0.3927 0.7326 0.0727  0.2619  0.0460  164 PRO A CG  
1296 C CD  . PRO A 164 ? 0.7617 0.3052 0.6307 0.0823  0.2589  0.0442  164 PRO A CD  
1297 N N   . TYR A 165 ? 0.7679 0.3373 0.6360 0.0564  0.2513  0.0544  165 TYR A N   
1298 C CA  . TYR A 165 ? 0.7793 0.3581 0.6454 0.0494  0.2495  0.0591  165 TYR A CA  
1299 C C   . TYR A 165 ? 0.8162 0.4254 0.6994 0.0444  0.2471  0.0533  165 TYR A C   
1300 O O   . TYR A 165 ? 0.7573 0.3734 0.6430 0.0340  0.2495  0.0506  165 TYR A O   
1301 C CB  . TYR A 165 ? 0.7559 0.3326 0.6148 0.0605  0.2428  0.0704  165 TYR A CB  
1302 C CG  . TYR A 165 ? 0.8000 0.3887 0.6545 0.0534  0.2401  0.0741  165 TYR A CG  
1303 C CD1 . TYR A 165 ? 0.7333 0.3517 0.6034 0.0548  0.2352  0.0720  165 TYR A CD1 
1304 C CD2 . TYR A 165 ? 0.8144 0.3816 0.6460 0.0439  0.2439  0.0789  165 TYR A CD2 
1305 C CE1 . TYR A 165 ? 0.8345 0.4613 0.6989 0.0478  0.2336  0.0735  165 TYR A CE1 
1306 C CE2 . TYR A 165 ? 0.8123 0.3885 0.6362 0.0364  0.2431  0.0806  165 TYR A CE2 
1307 C CZ  . TYR A 165 ? 0.8915 0.4978 0.7326 0.0388  0.2377  0.0773  165 TYR A CZ  
1308 O OH  . TYR A 165 ? 0.9347 0.5476 0.7666 0.0307  0.2378  0.0772  165 TYR A OH  
1309 N N   . VAL A 166 ? 0.7778 0.4035 0.6724 0.0516  0.2434  0.0510  166 VAL A N   
1310 C CA  . VAL A 166 ? 0.6651 0.3135 0.5723 0.0479  0.2401  0.0471  166 VAL A CA  
1311 C C   . VAL A 166 ? 0.7048 0.3539 0.6173 0.0387  0.2406  0.0383  166 VAL A C   
1312 O O   . VAL A 166 ? 0.7675 0.4296 0.6907 0.0330  0.2389  0.0349  166 VAL A O   
1313 C CB  . VAL A 166 ? 0.7857 0.4469 0.6987 0.0560  0.2375  0.0478  166 VAL A CB  
1314 C CG1 . VAL A 166 ? 0.6732 0.3467 0.5923 0.0513  0.2343  0.0433  166 VAL A CG1 
1315 C CG2 . VAL A 166 ? 0.7289 0.4014 0.6460 0.0623  0.2345  0.0545  166 VAL A CG2 
1316 N N   . VAL A 167 ? 0.7079 0.3437 0.6146 0.0375  0.2424  0.0335  167 VAL A N   
1317 C CA  . VAL A 167 ? 0.7003 0.3396 0.6135 0.0284  0.2400  0.0243  167 VAL A CA  
1318 C C   . VAL A 167 ? 0.7479 0.3889 0.6696 0.0174  0.2443  0.0207  167 VAL A C   
1319 O O   . VAL A 167 ? 0.6778 0.3361 0.6167 0.0120  0.2407  0.0142  167 VAL A O   
1320 C CB  . VAL A 167 ? 0.8235 0.4452 0.7252 0.0272  0.2416  0.0187  167 VAL A CB  
1321 C CG1 . VAL A 167 ? 0.7993 0.4266 0.7084 0.0164  0.2365  0.0083  167 VAL A CG1 
1322 C CG2 . VAL A 167 ? 0.7043 0.3255 0.5975 0.0369  0.2406  0.0202  167 VAL A CG2 
1323 N N   . ALA A 168 ? 0.7871 0.4092 0.6965 0.0141  0.2524  0.0246  168 ALA A N   
1324 C CA  . ALA A 168 ? 0.7481 0.3691 0.6614 0.0009  0.2603  0.0210  168 ALA A CA  
1325 C C   . ALA A 168 ? 0.7247 0.3670 0.6506 0.0004  0.2601  0.0209  168 ALA A C   
1326 O O   . ALA A 168 ? 0.7315 0.3894 0.6764 -0.0084 0.2631  0.0118  168 ALA A O   
1327 C CB  . ALA A 168 ? 0.7749 0.3650 0.6641 -0.0022 0.2688  0.0283  168 ALA A CB  
1328 N N   . SER A 169 ? 0.7216 0.3657 0.6393 0.0096  0.2567  0.0297  169 SER A N   
1329 C CA  . SER A 169 ? 0.7220 0.3829 0.6484 0.0088  0.2568  0.0287  169 SER A CA  
1330 C C   . SER A 169 ? 0.6934 0.3762 0.6441 0.0111  0.2502  0.0211  169 SER A C   
1331 O O   . SER A 169 ? 0.7574 0.4537 0.7250 0.0062  0.2534  0.0136  169 SER A O   
1332 C CB  . SER A 169 ? 0.7344 0.3936 0.6476 0.0174  0.2522  0.0387  169 SER A CB  
1333 O OG  . SER A 169 ? 0.7800 0.4173 0.6706 0.0184  0.2543  0.0471  169 SER A OG  
1334 N N   . MET A 170 ? 0.6737 0.3587 0.6253 0.0189  0.2412  0.0228  170 MET A N   
1335 C CA  . MET A 170 ? 0.6832 0.3832 0.6516 0.0218  0.2323  0.0179  170 MET A CA  
1336 C C   . MET A 170 ? 0.6446 0.3542 0.6330 0.0149  0.2314  0.0070  170 MET A C   
1337 O O   . MET A 170 ? 0.7138 0.4390 0.7232 0.0171  0.2251  0.0015  170 MET A O   
1338 C CB  . MET A 170 ? 0.6450 0.3403 0.6028 0.0288  0.2244  0.0219  170 MET A CB  
1339 C CG  . MET A 170 ? 0.6525 0.3471 0.6002 0.0354  0.2244  0.0303  170 MET A CG  
1340 S SD  . MET A 170 ? 0.6316 0.3370 0.5888 0.0378  0.2189  0.0312  170 MET A SD  
1341 C CE  . MET A 170 ? 0.6148 0.3188 0.5723 0.0402  0.2073  0.0291  170 MET A CE  
1342 N N   . ARG A 171 ? 0.7436 0.4442 0.7281 0.0065  0.2371  0.0031  171 ARG A N   
1343 C CA  . ARG A 171 ? 0.7532 0.4672 0.7613 -0.0027 0.2371  -0.0090 171 ARG A CA  
1344 C C   . ARG A 171 ? 0.6747 0.4039 0.7038 -0.0082 0.2466  -0.0156 171 ARG A C   
1345 O O   . ARG A 171 ? 0.6999 0.4508 0.7602 -0.0112 0.2439  -0.0269 171 ARG A O   
1346 C CB  . ARG A 171 ? 0.7076 0.4057 0.7053 -0.0136 0.2438  -0.0125 171 ARG A CB  
1347 C CG  . ARG A 171 ? 0.7382 0.4532 0.7630 -0.0252 0.2426  -0.0268 171 ARG A CG  
1348 C CD  . ARG A 171 ? 0.7718 0.4671 0.7838 -0.0385 0.2503  -0.0309 171 ARG A CD  
1349 N NE  . ARG A 171 ? 0.7986 0.5136 0.8391 -0.0508 0.2468  -0.0461 171 ARG A NE  
1350 C CZ  . ARG A 171 ? 0.9302 0.6619 0.9969 -0.0644 0.2580  -0.0566 171 ARG A CZ  
1351 N NH1 . ARG A 171 ? 0.9450 0.6729 1.0082 -0.0681 0.2745  -0.0533 171 ARG A NH1 
1352 N NH2 . ARG A 171 ? 0.8418 0.5958 0.9390 -0.0754 0.2527  -0.0716 171 ARG A NH2 
1353 N N   . ILE A 172 ? 0.6202 0.3392 0.6331 -0.0096 0.2574  -0.0096 172 ILE A N   
1354 C CA  . ILE A 172 ? 0.7151 0.4452 0.7416 -0.0159 0.2692  -0.0165 172 ILE A CA  
1355 C C   . ILE A 172 ? 0.7027 0.4465 0.7430 -0.0051 0.2625  -0.0172 172 ILE A C   
1356 O O   . ILE A 172 ? 0.7453 0.5083 0.8152 -0.0054 0.2651  -0.0284 172 ILE A O   
1357 C CB  . ILE A 172 ? 0.6739 0.3823 0.6695 -0.0241 0.2833  -0.0097 172 ILE A CB  
1358 C CG1 . ILE A 172 ? 0.6761 0.3650 0.6566 -0.0353 0.2907  -0.0088 172 ILE A CG1 
1359 C CG2 . ILE A 172 ? 0.7236 0.4410 0.7273 -0.0323 0.2976  -0.0179 172 ILE A CG2 
1360 C CD1 . ILE A 172 ? 0.7640 0.4232 0.7062 -0.0408 0.3003  0.0019  172 ILE A CD1 
1361 N N   . MET A 173 ? 0.7253 0.4595 0.7464 0.0045  0.2543  -0.0063 173 MET A N   
1362 C CA  . MET A 173 ? 0.6657 0.4064 0.6938 0.0121  0.2503  -0.0062 173 MET A CA  
1363 C C   . MET A 173 ? 0.6753 0.4277 0.7266 0.0215  0.2363  -0.0099 173 MET A C   
1364 O O   . MET A 173 ? 0.7666 0.5258 0.8335 0.0270  0.2348  -0.0142 173 MET A O   
1365 C CB  . MET A 173 ? 0.6655 0.3932 0.6666 0.0166  0.2472  0.0058  173 MET A CB  
1366 C CG  . MET A 173 ? 0.6305 0.3467 0.6081 0.0094  0.2574  0.0101  173 MET A CG  
1367 S SD  . MET A 173 ? 0.7479 0.4690 0.7315 -0.0004 0.2726  -0.0009 173 MET A SD  
1368 C CE  . MET A 173 ? 0.6981 0.4267 0.6927 0.0080  0.2661  -0.0035 173 MET A CE  
1369 N N   . THR A 174 ? 0.6241 0.3763 0.6757 0.0237  0.2255  -0.0083 174 THR A N   
1370 C CA  . THR A 174 ? 0.6735 0.4330 0.7405 0.0326  0.2090  -0.0098 174 THR A CA  
1371 C C   . THR A 174 ? 0.7233 0.4975 0.8134 0.0289  0.2028  -0.0197 174 THR A C   
1372 O O   . THR A 174 ? 0.6657 0.4441 0.7610 0.0179  0.2136  -0.0261 174 THR A O   
1373 C CB  . THR A 174 ? 0.6688 0.4126 0.7086 0.0384  0.1986  0.0017  174 THR A CB  
1374 O OG1 . THR A 174 ? 0.6971 0.4338 0.7211 0.0336  0.1982  0.0033  174 THR A OG1 
1375 C CG2 . THR A 174 ? 0.6348 0.3677 0.6545 0.0395  0.2057  0.0103  174 THR A CG2 
1376 N N   . ARG A 175 ? 0.6554 0.4361 0.7581 0.0375  0.1843  -0.0207 175 ARG A N   
1377 C CA  . ARG A 175 ? 0.7119 0.5063 0.8325 0.0348  0.1721  -0.0288 175 ARG A CA  
1378 C C   . ARG A 175 ? 0.8061 0.5816 0.8914 0.0335  0.1628  -0.0206 175 ARG A C   
1379 O O   . ARG A 175 ? 0.7539 0.5174 0.8204 0.0418  0.1495  -0.0120 175 ARG A O   
1380 C CB  . ARG A 175 ? 0.6825 0.4949 0.8370 0.0462  0.1541  -0.0347 175 ARG A CB  
1381 C CG  . ARG A 175 ? 0.7191 0.5573 0.9194 0.0465  0.1639  -0.0487 175 ARG A CG  
1382 C CD  . ARG A 175 ? 0.7342 0.5641 0.9333 0.0540  0.1737  -0.0456 175 ARG A CD  
1383 N NE  . ARG A 175 ? 0.7957 0.6504 1.0413 0.0567  0.1817  -0.0611 175 ARG A NE  
1384 C CZ  . ARG A 175 ? 0.8181 0.6694 1.0710 0.0627  0.1919  -0.0638 175 ARG A CZ  
1385 N NH1 . ARG A 175 ? 0.7408 0.5656 0.9585 0.0658  0.1939  -0.0517 175 ARG A NH1 
1386 N NH2 . ARG A 175 ? 0.8305 0.7065 1.1287 0.0647  0.2013  -0.0805 175 ARG A NH2 
1387 N N   . MET A 176 ? 0.7722 0.5424 0.8465 0.0223  0.1713  -0.0237 176 MET A N   
1388 C CA  . MET A 176 ? 0.8420 0.5914 0.8809 0.0202  0.1685  -0.0177 176 MET A CA  
1389 C C   . MET A 176 ? 0.8129 0.5672 0.8570 0.0109  0.1607  -0.0278 176 MET A C   
1390 O O   . MET A 176 ? 0.8759 0.6445 0.9451 0.0010  0.1674  -0.0385 176 MET A O   
1391 C CB  . MET A 176 ? 0.7894 0.5207 0.8048 0.0167  0.1870  -0.0112 176 MET A CB  
1392 C CG  . MET A 176 ? 0.8746 0.5846 0.8564 0.0171  0.1871  -0.0058 176 MET A CG  
1393 S SD  . MET A 176 ? 0.8965 0.5948 0.8708 0.0048  0.1939  -0.0145 176 MET A SD  
1394 C CE  . MET A 176 ? 0.8103 0.5026 0.7886 -0.0001 0.2140  -0.0121 176 MET A CE  
1395 N N   . GLY A 177 ? 0.8384 0.5804 0.8574 0.0122  0.1474  -0.0254 177 GLY A N   
1396 C CA  . GLY A 177 ? 0.8722 0.6143 0.8885 0.0017  0.1400  -0.0354 177 GLY A CA  
1397 C C   . GLY A 177 ? 0.8766 0.6163 0.8773 0.0058  0.1158  -0.0347 177 GLY A C   
1398 O O   . GLY A 177 ? 0.8598 0.5918 0.8451 0.0165  0.1067  -0.0244 177 GLY A O   
1399 N N   . THR A 178 ? 0.9070 0.6517 0.9096 -0.0045 0.1051  -0.0459 178 THR A N   
1400 C CA  . THR A 178 ? 0.9542 0.6925 0.9334 -0.0034 0.0809  -0.0460 178 THR A CA  
1401 C C   . THR A 178 ? 0.9385 0.6975 0.9429 0.0083  0.0559  -0.0438 178 THR A C   
1402 O O   . THR A 178 ? 0.9872 0.7319 0.9625 0.0156  0.0373  -0.0353 178 THR A O   
1403 C CB  . THR A 178 ? 0.9049 0.6446 0.8816 -0.0192 0.0751  -0.0607 178 THR A CB  
1404 O OG1 . THR A 178 ? 0.8927 0.6069 0.8429 -0.0279 0.0984  -0.0621 178 THR A OG1 
1405 C CG2 . THR A 178 ? 1.0042 0.7358 0.9510 -0.0194 0.0482  -0.0613 178 THR A CG2 
1406 N N   . SER A 179 ? 0.9295 0.7201 0.9869 0.0104  0.0557  -0.0516 179 SER A N   
1407 C CA  . SER A 179 ? 0.9605 0.7717 1.0485 0.0243  0.0320  -0.0508 179 SER A CA  
1408 C C   . SER A 179 ? 0.9343 0.7241 0.9987 0.0397  0.0305  -0.0339 179 SER A C   
1409 O O   . SER A 179 ? 0.9604 0.7504 1.0272 0.0524  0.0061  -0.0284 179 SER A O   
1410 C CB  . SER A 179 ? 0.8724 0.7218 1.0244 0.0240  0.0391  -0.0637 179 SER A CB  
1411 O OG  . SER A 179 ? 0.9391 0.7832 1.0955 0.0242  0.0676  -0.0600 179 SER A OG  
1412 N N   . VAL A 180 ? 0.9382 0.7084 0.9798 0.0386  0.0554  -0.0256 180 VAL A N   
1413 C CA  . VAL A 180 ? 0.9646 0.7130 0.9812 0.0496  0.0559  -0.0106 180 VAL A CA  
1414 C C   . VAL A 180 ? 1.0242 0.7439 0.9883 0.0495  0.0414  -0.0009 180 VAL A C   
1415 O O   . VAL A 180 ? 1.0211 0.7251 0.9679 0.0594  0.0276  0.0102  180 VAL A O   
1416 C CB  . VAL A 180 ? 0.8683 0.6072 0.8767 0.0468  0.0849  -0.0058 180 VAL A CB  
1417 C CG1 . VAL A 180 ? 0.9303 0.6467 0.9113 0.0549  0.0862  0.0085  180 VAL A CG1 
1418 C CG2 . VAL A 180 ? 0.8057 0.5689 0.8592 0.0466  0.0985  -0.0144 180 VAL A CG2 
1419 N N   . LEU A 181 ? 1.0246 0.7335 0.9595 0.0376  0.0456  -0.0052 181 LEU A N   
1420 C CA  . LEU A 181 ? 1.0609 0.7415 0.9418 0.0351  0.0341  0.0018  181 LEU A CA  
1421 C C   . LEU A 181 ? 1.0942 0.7772 0.9735 0.0415  -0.0008 0.0033  181 LEU A C   
1422 O O   . LEU A 181 ? 1.1018 0.7589 0.9414 0.0464  -0.0138 0.0158  181 LEU A O   
1423 C CB  . LEU A 181 ? 1.0878 0.7582 0.9424 0.0210  0.0450  -0.0070 181 LEU A CB  
1424 C CG  . LEU A 181 ? 1.0841 0.7345 0.9113 0.0170  0.0739  -0.0033 181 LEU A CG  
1425 C CD1 . LEU A 181 ? 1.0516 0.6905 0.8559 0.0047  0.0820  -0.0143 181 LEU A CD1 
1426 C CD2 . LEU A 181 ? 1.1239 0.7498 0.9107 0.0212  0.0752  0.0103  181 LEU A CD2 
1427 N N   . GLU A 182 ? 1.1549 0.8685 1.0769 0.0410  -0.0169 -0.0092 182 GLU A N   
1428 C CA  . GLU A 182 ? 1.1948 0.9149 1.1201 0.0482  -0.0540 -0.0089 182 GLU A CA  
1429 C C   . GLU A 182 ? 1.2065 0.9255 1.1494 0.0675  -0.0676 0.0024  182 GLU A C   
1430 O O   . GLU A 182 ? 1.2241 0.9228 1.1372 0.0759  -0.0944 0.0134  182 GLU A O   
1431 C CB  . GLU A 182 ? 1.2151 0.9743 1.1901 0.0420  -0.0665 -0.0275 182 GLU A CB  
1432 C CG  . GLU A 182 ? 1.3147 1.0695 1.2682 0.0219  -0.0557 -0.0394 182 GLU A CG  
1433 C CD  . GLU A 182 ? 1.4518 1.2455 1.4564 0.0124  -0.0654 -0.0589 182 GLU A CD  
1434 O OE1 . GLU A 182 ? 1.4904 1.3197 1.5557 0.0207  -0.0711 -0.0649 182 GLU A OE1 
1435 O OE2 . GLU A 182 ? 1.5307 1.3195 1.5156 -0.0043 -0.0661 -0.0697 182 GLU A OE2 
1436 N N   . ALA A 183 ? 1.1364 0.8733 1.1240 0.0743  -0.0494 0.0001  183 ALA A N   
1437 C CA  . ALA A 183 ? 1.0263 0.7579 1.0297 0.0924  -0.0587 0.0097  183 ALA A CA  
1438 C C   . ALA A 183 ? 1.0605 0.7461 1.0027 0.0945  -0.0562 0.0288  183 ALA A C   
1439 O O   . ALA A 183 ? 1.1464 0.8119 1.0733 0.1071  -0.0792 0.0404  183 ALA A O   
1440 C CB  . ALA A 183 ? 1.0030 0.7579 1.0572 0.0958  -0.0341 0.0022  183 ALA A CB  
1441 N N   . LEU A 184 ? 1.0736 0.7415 0.9809 0.0820  -0.0285 0.0322  184 LEU A N   
1442 C CA  . LEU A 184 ? 1.1230 0.7509 0.9758 0.0809  -0.0216 0.0483  184 LEU A CA  
1443 C C   . LEU A 184 ? 1.1696 0.7679 0.9689 0.0800  -0.0476 0.0578  184 LEU A C   
1444 O O   . LEU A 184 ? 1.2013 0.7684 0.9696 0.0870  -0.0590 0.0726  184 LEU A O   
1445 C CB  . LEU A 184 ? 1.0661 0.6871 0.8970 0.0674  0.0114  0.0471  184 LEU A CB  
1446 C CG  . LEU A 184 ? 1.1660 0.7494 0.9395 0.0620  0.0213  0.0608  184 LEU A CG  
1447 C CD1 . LEU A 184 ? 1.1071 0.6759 0.8841 0.0708  0.0225  0.0722  184 LEU A CD1 
1448 C CD2 . LEU A 184 ? 1.0469 0.6300 0.8059 0.0499  0.0518  0.0566  184 LEU A CD2 
1449 N N   . GLY A 185 ? 1.1609 0.7650 0.9448 0.0703  -0.0571 0.0494  185 GLY A N   
1450 C CA  . GLY A 185 ? 1.2307 0.8038 0.9548 0.0667  -0.0805 0.0576  185 GLY A CA  
1451 C C   . GLY A 185 ? 1.3465 0.8778 1.0073 0.0583  -0.0608 0.0708  185 GLY A C   
1452 O O   . GLY A 185 ? 1.3608 0.8911 1.0109 0.0469  -0.0296 0.0661  185 GLY A O   
1453 N N   . ASP A 186 ? 1.4060 0.9016 1.0251 0.0639  -0.0788 0.0874  186 ASP A N   
1454 C CA  . ASP A 186 ? 1.4485 0.9028 1.0083 0.0547  -0.0596 0.1007  186 ASP A CA  
1455 C C   . ASP A 186 ? 1.3826 0.8270 0.9597 0.0635  -0.0486 0.1114  186 ASP A C   
1456 O O   . ASP A 186 ? 1.4091 0.8166 0.9384 0.0562  -0.0363 0.1241  186 ASP A O   
1457 C CB  . ASP A 186 ? 1.5149 0.9261 1.0006 0.0500  -0.0839 0.1130  186 ASP A CB  
1458 C CG  . ASP A 186 ? 1.6038 1.0119 1.0494 0.0337  -0.0810 0.1026  186 ASP A CG  
1459 O OD1 . ASP A 186 ? 1.5671 0.9933 1.0271 0.0237  -0.0505 0.0895  186 ASP A OD1 
1460 O OD2 . ASP A 186 ? 1.7367 1.1220 1.1347 0.0312  -0.1100 0.1073  186 ASP A OD2 
1461 N N   . GLY A 187 ? 1.2850 0.7603 0.9279 0.0771  -0.0511 0.1055  187 GLY A N   
1462 C CA  . GLY A 187 ? 1.2930 0.7598 0.9541 0.0840  -0.0384 0.1127  187 GLY A CA  
1463 C C   . GLY A 187 ? 1.2868 0.7529 0.9391 0.0702  -0.0002 0.1112  187 GLY A C   
1464 O O   . GLY A 187 ? 1.2924 0.7704 0.9357 0.0581  0.0181  0.1030  187 GLY A O   
1465 N N   . GLU A 188 ? 1.3248 0.7764 0.9812 0.0726  0.0113  0.1188  188 GLU A N   
1466 C CA  . GLU A 188 ? 1.2925 0.7478 0.9475 0.0603  0.0452  0.1168  188 GLU A CA  
1467 C C   . GLU A 188 ? 1.1774 0.6775 0.8891 0.0620  0.0608  0.1017  188 GLU A C   
1468 O O   . GLU A 188 ? 1.1748 0.7006 0.9299 0.0726  0.0484  0.0934  188 GLU A O   
1469 C CB  . GLU A 188 ? 1.3734 0.8010 1.0184 0.0606  0.0519  0.1278  188 GLU A CB  
1470 C CG  . GLU A 188 ? 1.5654 0.9410 1.1473 0.0565  0.0397  0.1449  188 GLU A CG  
1471 C CD  . GLU A 188 ? 1.7462 1.0913 1.3162 0.0531  0.0506  0.1550  188 GLU A CD  
1472 O OE1 . GLU A 188 ? 1.6456 1.0127 1.2564 0.0533  0.0680  0.1474  188 GLU A OE1 
1473 O OE2 . GLU A 188 ? 1.9019 1.1985 1.4185 0.0492  0.0417  0.1704  188 GLU A OE2 
1474 N N   . PHE A 189 ? 1.0277 0.5367 0.7385 0.0512  0.0884  0.0981  189 PHE A N   
1475 C CA  . PHE A 189 ? 0.9885 0.5336 0.7449 0.0520  0.1038  0.0863  189 PHE A CA  
1476 C C   . PHE A 189 ? 0.9468 0.4937 0.7014 0.0432  0.1295  0.0872  189 PHE A C   
1477 O O   . PHE A 189 ? 1.0169 0.5417 0.7356 0.0339  0.1388  0.0944  189 PHE A O   
1478 C CB  . PHE A 189 ? 1.0286 0.5930 0.7909 0.0491  0.1045  0.0759  189 PHE A CB  
1479 C CG  . PHE A 189 ? 1.0486 0.5997 0.7703 0.0376  0.1175  0.0762  189 PHE A CG  
1480 C CD1 . PHE A 189 ? 1.0372 0.5619 0.7121 0.0332  0.1049  0.0814  189 PHE A CD1 
1481 C CD2 . PHE A 189 ? 0.9300 0.4944 0.6598 0.0317  0.1420  0.0707  189 PHE A CD2 
1482 C CE1 . PHE A 189 ? 1.0196 0.5313 0.6556 0.0217  0.1198  0.0797  189 PHE A CE1 
1483 C CE2 . PHE A 189 ? 0.9059 0.4597 0.6030 0.0226  0.1559  0.0688  189 PHE A CE2 
1484 C CZ  . PHE A 189 ? 1.0637 0.5911 0.7134 0.0168  0.1465  0.0726  189 PHE A CZ  
1485 N N   . ILE A 190 ? 0.8950 0.4687 0.6884 0.0453  0.1408  0.0795  190 ILE A N   
1486 C CA  . ILE A 190 ? 0.9054 0.4878 0.7042 0.0380  0.1624  0.0787  190 ILE A CA  
1487 C C   . ILE A 190 ? 0.9143 0.5104 0.7092 0.0329  0.1757  0.0728  190 ILE A C   
1488 O O   . ILE A 190 ? 0.9500 0.5612 0.7612 0.0367  0.1730  0.0656  190 ILE A O   
1489 C CB  . ILE A 190 ? 0.8560 0.4576 0.6931 0.0426  0.1662  0.0737  190 ILE A CB  
1490 C CG1 . ILE A 190 ? 0.9297 0.5163 0.7733 0.0495  0.1535  0.0772  190 ILE A CG1 
1491 C CG2 . ILE A 190 ? 0.8170 0.4287 0.6589 0.0348  0.1848  0.0729  190 ILE A CG2 
1492 C CD1 . ILE A 190 ? 0.9746 0.5298 0.7872 0.0439  0.1543  0.0876  190 ILE A CD1 
1493 N N   . LYS A 191 ? 0.9219 0.5118 0.6964 0.0240  0.1911  0.0751  191 LYS A N   
1494 C CA  . LYS A 191 ? 0.8310 0.4331 0.6043 0.0208  0.2058  0.0686  191 LYS A CA  
1495 C C   . LYS A 191 ? 0.8390 0.4673 0.6470 0.0231  0.2174  0.0641  191 LYS A C   
1496 O O   . LYS A 191 ? 0.8811 0.5145 0.6969 0.0189  0.2249  0.0667  191 LYS A O   
1497 C CB  . LYS A 191 ? 0.8676 0.4535 0.6057 0.0102  0.2188  0.0712  191 LYS A CB  
1498 C CG  . LYS A 191 ? 0.9763 0.5306 0.6703 0.0064  0.2065  0.0774  191 LYS A CG  
1499 C CD  . LYS A 191 ? 1.0202 0.5537 0.6759 -0.0071 0.2216  0.0822  191 LYS A CD  
1500 C CE  . LYS A 191 ? 1.1228 0.6185 0.7272 -0.0114 0.2069  0.0910  191 LYS A CE  
1501 N NZ  . LYS A 191 ? 1.3094 0.7803 0.8703 -0.0273 0.2242  0.0962  191 LYS A NZ  
1502 N N   . CYS A 192 ? 0.7522 0.3952 0.5788 0.0288  0.2179  0.0577  192 CYS A N   
1503 C CA  . CYS A 192 ? 0.7858 0.4500 0.6405 0.0322  0.2257  0.0547  192 CYS A CA  
1504 C C   . CYS A 192 ? 0.8010 0.4713 0.6562 0.0343  0.2367  0.0494  192 CYS A C   
1505 O O   . CYS A 192 ? 0.7931 0.4547 0.6380 0.0359  0.2343  0.0452  192 CYS A O   
1506 C CB  . CYS A 192 ? 0.7474 0.4191 0.6232 0.0375  0.2166  0.0529  192 CYS A CB  
1507 S SG  . CYS A 192 ? 0.7722 0.4365 0.6524 0.0380  0.2043  0.0563  192 CYS A SG  
1508 N N   . LEU A 193 ? 0.7230 0.4084 0.5919 0.0346  0.2481  0.0485  193 LEU A N   
1509 C CA  . LEU A 193 ? 0.7361 0.4288 0.6109 0.0393  0.2592  0.0428  193 LEU A CA  
1510 C C   . LEU A 193 ? 0.7711 0.4836 0.6748 0.0464  0.2595  0.0431  193 LEU A C   
1511 O O   . LEU A 193 ? 0.7321 0.4594 0.6496 0.0438  0.2597  0.0456  193 LEU A O   
1512 C CB  . LEU A 193 ? 0.7423 0.4358 0.6059 0.0331  0.2741  0.0402  193 LEU A CB  
1513 C CG  . LEU A 193 ? 0.7689 0.4724 0.6436 0.0392  0.2883  0.0321  193 LEU A CG  
1514 C CD1 . LEU A 193 ? 0.7325 0.4178 0.5913 0.0437  0.2874  0.0268  193 LEU A CD1 
1515 C CD2 . LEU A 193 ? 0.8439 0.5523 0.7112 0.0308  0.3059  0.0282  193 LEU A CD2 
1516 N N   . HIS A 194 ? 0.7514 0.4615 0.6614 0.0547  0.2587  0.0406  194 HIS A N   
1517 C CA  . HIS A 194 ? 0.7089 0.4325 0.6404 0.0626  0.2566  0.0424  194 HIS A CA  
1518 C C   . HIS A 194 ? 0.7232 0.4441 0.6603 0.0729  0.2634  0.0381  194 HIS A C   
1519 O O   . HIS A 194 ? 0.7813 0.4838 0.7036 0.0735  0.2666  0.0337  194 HIS A O   
1520 C CB  . HIS A 194 ? 0.7020 0.4195 0.6338 0.0625  0.2463  0.0461  194 HIS A CB  
1521 C CG  . HIS A 194 ? 0.6440 0.3679 0.5883 0.0701  0.2432  0.0492  194 HIS A CG  
1522 N ND1 . HIS A 194 ? 0.6627 0.3720 0.6029 0.0765  0.2430  0.0494  194 HIS A ND1 
1523 C CD2 . HIS A 194 ? 0.6798 0.4208 0.6377 0.0719  0.2392  0.0526  194 HIS A CD2 
1524 C CE1 . HIS A 194 ? 0.7774 0.4921 0.7258 0.0829  0.2382  0.0542  194 HIS A CE1 
1525 N NE2 . HIS A 194 ? 0.8134 0.5490 0.7731 0.0804  0.2349  0.0559  194 HIS A NE2 
1526 N N   . SER A 195 ? 0.6538 0.3926 0.6132 0.0814  0.2645  0.0388  195 SER A N   
1527 C CA  . SER A 195 ? 0.7531 0.4887 0.7226 0.0949  0.2684  0.0358  195 SER A CA  
1528 C C   . SER A 195 ? 0.7807 0.5313 0.7711 0.1045  0.2587  0.0416  195 SER A C   
1529 O O   . SER A 195 ? 0.7283 0.5032 0.7343 0.1014  0.2550  0.0434  195 SER A O   
1530 C CB  . SER A 195 ? 0.7292 0.4739 0.7070 0.0979  0.2837  0.0267  195 SER A CB  
1531 O OG  . SER A 195 ? 0.7616 0.5045 0.7546 0.1139  0.2872  0.0230  195 SER A OG  
1532 N N   . VAL A 196 ? 0.7322 0.4654 0.7197 0.1153  0.2538  0.0448  196 VAL A N   
1533 C CA  . VAL A 196 ? 0.7429 0.4859 0.7459 0.1267  0.2427  0.0513  196 VAL A CA  
1534 C C   . VAL A 196 ? 0.8551 0.6256 0.8908 0.1392  0.2461  0.0463  196 VAL A C   
1535 O O   . VAL A 196 ? 0.9219 0.7122 0.9774 0.1472  0.2344  0.0508  196 VAL A O   
1536 C CB  . VAL A 196 ? 0.8968 0.6075 0.8837 0.1350  0.2374  0.0570  196 VAL A CB  
1537 C CG1 . VAL A 196 ? 0.7877 0.4771 0.7478 0.1207  0.2353  0.0605  196 VAL A CG1 
1538 C CG2 . VAL A 196 ? 0.7930 0.4850 0.7799 0.1451  0.2481  0.0499  196 VAL A CG2 
1539 N N   . GLY A 197 ? 0.7795 0.5529 0.8219 0.1406  0.2618  0.0362  197 GLY A N   
1540 C CA  . GLY A 197 ? 0.7849 0.5890 0.8629 0.1507  0.2690  0.0285  197 GLY A CA  
1541 C C   . GLY A 197 ? 0.8788 0.6791 0.9773 0.1740  0.2660  0.0274  197 GLY A C   
1542 O O   . GLY A 197 ? 0.8938 0.7265 1.0308 0.1860  0.2646  0.0235  197 GLY A O   
1543 N N   . CYS A 198 ? 0.8422 0.6033 0.9176 0.1810  0.2647  0.0304  198 CYS A N   
1544 C CA  . CYS A 198 ? 0.8437 0.5911 0.9335 0.2043  0.2619  0.0302  198 CYS A CA  
1545 C C   . CYS A 198 ? 0.9516 0.6685 1.0260 0.2063  0.2798  0.0194  198 CYS A C   
1546 O O   . CYS A 198 ? 0.9658 0.6414 1.0129 0.2075  0.2776  0.0231  198 CYS A O   
1547 C CB  . CYS A 198 ? 0.9282 0.6491 1.0002 0.2110  0.2422  0.0453  198 CYS A CB  
1548 S SG  . CYS A 198 ? 1.1130 0.8681 1.2045 0.2143  0.2187  0.0566  198 CYS A SG  
1549 N N   . PRO A 199 ? 0.9524 0.6873 1.0416 0.2048  0.2988  0.0050  199 PRO A N   
1550 C CA  . PRO A 199 ? 0.9237 0.6291 0.9966 0.2067  0.3168  -0.0074 199 PRO A CA  
1551 C C   . PRO A 199 ? 0.9881 0.6723 1.0763 0.2322  0.3152  -0.0091 199 PRO A C   
1552 O O   . PRO A 199 ? 1.0079 0.7122 1.1308 0.2516  0.3040  -0.0044 199 PRO A O   
1553 C CB  . PRO A 199 ? 0.9470 0.6825 1.0361 0.2002  0.3377  -0.0222 199 PRO A CB  
1554 C CG  . PRO A 199 ? 0.9168 0.7005 1.0488 0.2057  0.3305  -0.0192 199 PRO A CG  
1555 C CD  . PRO A 199 ? 0.8500 0.6319 0.9704 0.2000  0.3063  -0.0017 199 PRO A CD  
1556 N N   . LEU A 200 ? 1.0369 0.6787 1.0983 0.2321  0.3253  -0.0159 200 LEU A N   
1557 C CA  . LEU A 200 ? 1.1146 0.7330 1.1847 0.2521  0.3207  -0.0174 200 LEU A CA  
1558 C C   . LEU A 200 ? 1.1513 0.7871 1.2453 0.2597  0.3366  -0.0363 200 LEU A C   
1559 O O   . LEU A 200 ? 1.1541 0.7964 1.2349 0.2435  0.3545  -0.0490 200 LEU A O   
1560 C CB  . LEU A 200 ? 1.0742 0.6410 1.1006 0.2416  0.3168  -0.0140 200 LEU A CB  
1561 C CG  . LEU A 200 ? 1.0639 0.6132 1.0626 0.2283  0.3049  0.0017  200 LEU A CG  
1562 C CD1 . LEU A 200 ? 1.0850 0.5889 1.0446 0.2144  0.3040  0.0017  200 LEU A CD1 
1563 C CD2 . LEU A 200 ? 1.0865 0.6416 1.1014 0.2442  0.2863  0.0186  200 LEU A CD2 
1564 N N   . PRO A 201 ? 1.1903 0.8321 1.3179 0.2843  0.3303  -0.0389 201 PRO A N   
1565 C CA  . PRO A 201 ? 1.2548 0.8816 1.3934 0.3057  0.3074  -0.0239 201 PRO A CA  
1566 C C   . PRO A 201 ? 1.2455 0.9039 1.4081 0.3130  0.2924  -0.0093 201 PRO A C   
1567 O O   . PRO A 201 ? 1.2353 0.9418 1.4320 0.3122  0.2999  -0.0154 201 PRO A O   
1568 C CB  . PRO A 201 ? 1.2494 0.8838 1.4240 0.3300  0.3088  -0.0365 201 PRO A CB  
1569 C CG  . PRO A 201 ? 1.2607 0.9413 1.4647 0.3244  0.3303  -0.0553 201 PRO A CG  
1570 C CD  . PRO A 201 ? 1.2508 0.9194 1.4111 0.2933  0.3462  -0.0584 201 PRO A CD  
1571 N N   . LEU A 202 ? 1.2170 0.8481 1.3608 0.3185  0.2717  0.0100  202 LEU A N   
1572 C CA  . LEU A 202 ? 1.3868 1.0460 1.5461 0.3224  0.2528  0.0249  202 LEU A CA  
1573 C C   . LEU A 202 ? 1.4590 1.1576 1.6761 0.3508  0.2425  0.0223  202 LEU A C   
1574 O O   . LEU A 202 ? 1.4414 1.1180 1.6683 0.3757  0.2300  0.0265  202 LEU A O   
1575 C CB  . LEU A 202 ? 1.3426 0.9594 1.4601 0.3185  0.2324  0.0455  202 LEU A CB  
1576 C CG  . LEU A 202 ? 1.2901 0.8826 1.3587 0.2878  0.2378  0.0497  202 LEU A CG  
1577 C CD1 . LEU A 202 ? 1.2926 0.8457 1.3242 0.2851  0.2197  0.0690  202 LEU A CD1 
1578 C CD2 . LEU A 202 ? 1.2412 0.8800 1.3171 0.2663  0.2405  0.0464  202 LEU A CD2 
1579 N N   . LYS A 203 ? 1.5350 1.2938 1.7900 0.3446  0.2452  0.0147  203 LYS A N   
1580 C CA  . LYS A 203 ? 1.5892 1.3962 1.9050 0.3682  0.2327  0.0117  203 LYS A CA  
1581 C C   . LYS A 203 ? 1.7602 1.5808 2.0759 0.3710  0.1989  0.0307  203 LYS A C   
1582 O O   . LYS A 203 ? 1.7234 1.5767 2.0857 0.3944  0.1807  0.0318  203 LYS A O   
1583 C CB  . LYS A 203 ? 1.5978 1.4647 1.9565 0.3576  0.2537  -0.0074 203 LYS A CB  
1584 C CG  . LYS A 203 ? 1.5576 1.4117 1.9123 0.3530  0.2886  -0.0273 203 LYS A CG  
1585 C CD  . LYS A 203 ? 1.5418 1.4500 1.9285 0.3371  0.3113  -0.0446 203 LYS A CD  
1586 C CE  . LYS A 203 ? 1.5756 1.4686 1.9408 0.3239  0.3386  -0.0634 203 LYS A CE  
1587 N NZ  . LYS A 203 ? 1.4180 1.2545 1.7152 0.3049  0.3435  -0.0570 203 LYS A NZ  
1588 N N   . LYS A 204 ? 1.9661 1.7634 2.2313 0.3478  0.1900  0.0447  204 LYS A N   
1589 C CA  . LYS A 204 ? 1.9858 1.7868 2.2383 0.3470  0.1597  0.0627  204 LYS A CA  
1590 C C   . LYS A 204 ? 2.0203 1.7548 2.2114 0.3433  0.1508  0.0798  204 LYS A C   
1591 O O   . LYS A 204 ? 1.9597 1.6649 2.1104 0.3208  0.1671  0.0787  204 LYS A O   
1592 C CB  . LYS A 204 ? 1.9970 1.8372 2.2477 0.3191  0.1595  0.0615  204 LYS A CB  
1593 C CG  . LYS A 204 ? 1.9778 1.8815 2.2840 0.3160  0.1721  0.0441  204 LYS A CG  
1594 C CD  . LYS A 204 ? 2.0502 1.9810 2.3458 0.2861  0.1729  0.0441  204 LYS A CD  
1595 C CE  . LYS A 204 ? 1.8838 1.8735 2.2303 0.2791  0.1881  0.0269  204 LYS A CE  
1596 N NZ  . LYS A 204 ? 1.8015 1.8108 2.1343 0.2493  0.1897  0.0271  204 LYS A NZ  
1597 N N   . PRO A 205 ? 1.9017 1.6098 2.0830 0.3636  0.1257  0.0956  205 PRO A N   
1598 C CA  . PRO A 205 ? 1.7948 1.4368 1.9135 0.3566  0.1194  0.1124  205 PRO A CA  
1599 C C   . PRO A 205 ? 1.6537 1.2943 1.7313 0.3236  0.1208  0.1182  205 PRO A C   
1600 O O   . PRO A 205 ? 1.6313 1.3182 1.7252 0.3110  0.1156  0.1153  205 PRO A O   
1601 C CB  . PRO A 205 ? 1.8017 1.4277 1.9204 0.3830  0.0872  0.1297  205 PRO A CB  
1602 C CG  . PRO A 205 ? 1.8275 1.4988 2.0154 0.4124  0.0829  0.1180  205 PRO A CG  
1603 C CD  . PRO A 205 ? 1.8698 1.6054 2.0973 0.3947  0.1019  0.0987  205 PRO A CD  
1604 N N   . LEU A 206 ? 1.5257 1.1122 1.5512 0.3091  0.1288  0.1254  206 LEU A N   
1605 C CA  . LEU A 206 ? 1.4262 1.0074 1.4140 0.2784  0.1339  0.1288  206 LEU A CA  
1606 C C   . LEU A 206 ? 1.3959 0.9435 1.3397 0.2754  0.1136  0.1485  206 LEU A C   
1607 O O   . LEU A 206 ? 1.4437 0.9383 1.3574 0.2854  0.1084  0.1599  206 LEU A O   
1608 C CB  . LEU A 206 ? 1.3457 0.8955 1.3086 0.2608  0.1586  0.1206  206 LEU A CB  
1609 C CG  . LEU A 206 ? 1.3096 0.8876 1.3030 0.2573  0.1801  0.1013  206 LEU A CG  
1610 C CD1 . LEU A 206 ? 1.2888 0.8328 1.2519 0.2388  0.1994  0.0948  206 LEU A CD1 
1611 C CD2 . LEU A 206 ? 1.2225 0.8570 1.2413 0.2452  0.1806  0.0944  206 LEU A CD2 
1612 N N   . VAL A 207 ? 1.4139 0.8000 1.2179 0.0617  0.4270  0.0829  207 VAL A N   
1613 C CA  . VAL A 207 ? 1.4345 0.7991 1.2089 0.0742  0.4394  0.0949  207 VAL A CA  
1614 C C   . VAL A 207 ? 1.4562 0.8052 1.2455 0.0594  0.4561  0.0924  207 VAL A C   
1615 O O   . VAL A 207 ? 1.3829 0.7506 1.1941 0.0422  0.4471  0.0801  207 VAL A O   
1616 C CB  . VAL A 207 ? 1.3897 0.7763 1.1401 0.0846  0.4204  0.0945  207 VAL A CB  
1617 C CG1 . VAL A 207 ? 1.3941 0.7603 1.1143 0.0966  0.4328  0.1049  207 VAL A CG1 
1618 C CG2 . VAL A 207 ? 1.4701 0.8707 1.2057 0.1023  0.4061  0.0967  207 VAL A CG2 
1619 N N   . ASN A 208 ? 1.4623 0.7765 1.2402 0.0670  0.4815  0.1041  208 ASN A N   
1620 C CA  . ASN A 208 ? 1.4207 0.7173 1.2165 0.0533  0.5014  0.1017  208 ASN A CA  
1621 C C   . ASN A 208 ? 1.4067 0.7139 1.2480 0.0314  0.5007  0.0847  208 ASN A C   
1622 O O   . ASN A 208 ? 1.3802 0.6911 1.2430 0.0162  0.5048  0.0751  208 ASN A O   
1623 C CB  . ASN A 208 ? 1.4241 0.7307 1.2066 0.0510  0.4953  0.1007  208 ASN A CB  
1624 C CG  . ASN A 208 ? 1.5152 0.8011 1.2541 0.0731  0.5058  0.1176  208 ASN A CG  
1625 O OD1 . ASN A 208 ? 1.5578 0.8151 1.2779 0.0893  0.5241  0.1319  208 ASN A OD1 
1626 N ND2 . ASN A 208 ? 1.4393 0.7388 1.1610 0.0754  0.4950  0.1161  208 ASN A ND2 
1627 N N   . ASN A 209 ? 1.4371 0.7504 1.2928 0.0311  0.4948  0.0800  209 ASN A N   
1628 C CA  . ASN A 209 ? 1.3970 0.7237 1.2932 0.0138  0.4910  0.0622  209 ASN A CA  
1629 C C   . ASN A 209 ? 1.2506 0.6087 1.1592 0.0009  0.4714  0.0488  209 ASN A C   
1630 O O   . ASN A 209 ? 1.2345 0.6012 1.1742 -0.0133 0.4718  0.0337  209 ASN A O   
1631 C CB  . ASN A 209 ? 1.2659 0.5850 1.1911 0.0062  0.5107  0.0548  209 ASN A CB  
1632 C CG  . ASN A 209 ? 1.3731 0.6740 1.2965 0.0169  0.5260  0.0626  209 ASN A CG  
1633 O OD1 . ASN A 209 ? 1.4951 0.7918 1.4109 0.0245  0.5196  0.0663  209 ASN A OD1 
1634 N ND2 . ASN A 209 ? 1.4294 0.7186 1.3604 0.0182  0.5475  0.0651  209 ASN A ND2 
1635 N N   . TRP A 210 ? 1.2024 0.5781 1.0874 0.0067  0.4543  0.0534  210 TRP A N   
1636 C CA  . TRP A 210 ? 1.1853 0.5872 1.0781 -0.0039 0.4379  0.0432  210 TRP A CA  
1637 C C   . TRP A 210 ? 1.1301 0.5590 1.0279 -0.0038 0.4171  0.0372  210 TRP A C   
1638 O O   . TRP A 210 ? 1.1990 0.6369 1.0775 0.0065  0.4062  0.0437  210 TRP A O   
1639 C CB  . TRP A 210 ? 1.1302 0.5321 0.9968 0.0015  0.4352  0.0508  210 TRP A CB  
1640 C CG  . TRP A 210 ? 1.1034 0.5257 0.9796 -0.0102 0.4235  0.0409  210 TRP A CG  
1641 C CD1 . TRP A 210 ? 1.0924 0.5381 0.9611 -0.0100 0.4046  0.0381  210 TRP A CD1 
1642 C CD2 . TRP A 210 ? 1.0530 0.4739 0.9499 -0.0234 0.4310  0.0318  210 TRP A CD2 
1643 N NE1 . TRP A 210 ? 0.9935 0.4499 0.8743 -0.0217 0.4006  0.0294  210 TRP A NE1 
1644 C CE2 . TRP A 210 ? 1.0278 0.4704 0.9251 -0.0294 0.4157  0.0253  210 TRP A CE2 
1645 C CE3 . TRP A 210 ? 0.9994 0.4032 0.9170 -0.0306 0.4498  0.0275  210 TRP A CE3 
1646 C CZ2 . TRP A 210 ? 1.0067 0.4544 0.9207 -0.0407 0.4175  0.0157  210 TRP A CZ2 
1647 C CZ3 . TRP A 210 ? 0.9584 0.3699 0.8955 -0.0426 0.4508  0.0161  210 TRP A CZ3 
1648 C CH2 . TRP A 210 ? 0.9357 0.3689 0.8692 -0.0468 0.4342  0.0108  210 TRP A CH2 
1649 N N   . ALA A 211 ? 1.0717 0.5141 0.9958 -0.0142 0.4121  0.0241  211 ALA A N   
1650 C CA  . ALA A 211 ? 1.1302 0.5969 1.0595 -0.0140 0.3950  0.0188  211 ALA A CA  
1651 C C   . ALA A 211 ? 1.1002 0.5868 1.0226 -0.0175 0.3813  0.0173  211 ALA A C   
1652 O O   . ALA A 211 ? 1.0980 0.5874 1.0270 -0.0259 0.3821  0.0117  211 ALA A O   
1653 C CB  . ALA A 211 ? 1.0412 0.5153 0.9976 -0.0210 0.3946  0.0050  211 ALA A CB  
1654 N N   . CYS A 212 ? 1.1440 0.6447 1.0552 -0.0110 0.3694  0.0215  212 CYS A N   
1655 C CA  . CYS A 212 ? 1.1138 0.6327 1.0216 -0.0144 0.3577  0.0194  212 CYS A CA  
1656 C C   . CYS A 212 ? 1.0847 0.6205 0.9899 -0.0078 0.3463  0.0210  212 CYS A C   
1657 O O   . CYS A 212 ? 1.0849 0.6167 0.9847 0.0015  0.3471  0.0256  212 CYS A O   
1658 C CB  . CYS A 212 ? 1.0735 0.5845 0.9643 -0.0128 0.3601  0.0240  212 CYS A CB  
1659 S SG  . CYS A 212 ? 1.2047 0.7074 1.0682 0.0045  0.3600  0.0349  212 CYS A SG  
1660 N N   . ASN A 213 ? 1.0551 0.6095 0.9660 -0.0126 0.3369  0.0168  213 ASN A N   
1661 C CA  . ASN A 213 ? 1.0938 0.6667 1.0081 -0.0084 0.3271  0.0162  213 ASN A CA  
1662 C C   . ASN A 213 ? 1.1398 0.7250 1.0527 -0.0113 0.3198  0.0131  213 ASN A C   
1663 O O   . ASN A 213 ? 1.1623 0.7578 1.0874 -0.0197 0.3176  0.0085  213 ASN A O   
1664 C CB  . ASN A 213 ? 1.1242 0.7082 1.0550 -0.0120 0.3258  0.0123  213 ASN A CB  
1665 C CG  . ASN A 213 ? 1.1922 0.7915 1.1278 -0.0058 0.3194  0.0130  213 ASN A CG  
1666 O OD1 . ASN A 213 ? 1.2262 0.8357 1.1590 -0.0022 0.3129  0.0127  213 ASN A OD1 
1667 N ND2 . ASN A 213 ? 1.1970 0.7995 1.1411 -0.0039 0.3208  0.0123  213 ASN A ND2 
1668 N N   . PRO A 214 ? 1.2181 0.8020 1.1157 -0.0033 0.3163  0.0151  214 PRO A N   
1669 C CA  . PRO A 214 ? 1.2007 0.7968 1.0983 -0.0058 0.3087  0.0095  214 PRO A CA  
1670 C C   . PRO A 214 ? 1.2152 0.8347 1.1326 -0.0095 0.3004  0.0023  214 PRO A C   
1671 O O   . PRO A 214 ? 1.1460 0.7734 1.0747 -0.0185 0.2988  -0.0035 214 PRO A O   
1672 C CB  . PRO A 214 ? 1.2048 0.7962 1.0796 0.0084  0.3058  0.0125  214 PRO A CB  
1673 C CG  . PRO A 214 ? 1.2310 0.7988 1.0917 0.0148  0.3174  0.0223  214 PRO A CG  
1674 C CD  . PRO A 214 ? 1.2389 0.8078 1.1167 0.0096  0.3205  0.0225  214 PRO A CD  
1675 N N   . GLU A 215 ? 1.3713 1.0013 1.2946 -0.0027 0.2965  0.0024  215 GLU A N   
1676 C CA  . GLU A 215 ? 1.3777 1.0306 1.3230 -0.0060 0.2903  -0.0051 215 GLU A CA  
1677 C C   . GLU A 215 ? 1.3374 0.9917 1.3004 -0.0186 0.2966  -0.0061 215 GLU A C   
1678 O O   . GLU A 215 ? 1.3376 1.0046 1.3178 -0.0254 0.2952  -0.0126 215 GLU A O   
1679 C CB  . GLU A 215 ? 1.4112 1.0738 1.3604 0.0036  0.2869  -0.0041 215 GLU A CB  
1680 C CG  . GLU A 215 ? 1.5474 1.2084 1.4765 0.0197  0.2808  -0.0022 215 GLU A CG  
1681 C CD  . GLU A 215 ? 1.5939 1.2285 1.5005 0.0260  0.2897  0.0089  215 GLU A CD  
1682 O OE1 . GLU A 215 ? 1.5235 1.1439 1.4334 0.0168  0.2990  0.0126  215 GLU A OE1 
1683 O OE2 . GLU A 215 ? 1.7155 1.3436 1.6019 0.0410  0.2880  0.0132  215 GLU A OE2 
1684 N N   . LEU A 216 ? 1.1742 0.8153 1.1335 -0.0206 0.3043  -0.0004 216 LEU A N   
1685 C CA  . LEU A 216 ? 0.9828 0.6246 0.9540 -0.0280 0.3104  -0.0004 216 LEU A CA  
1686 C C   . LEU A 216 ? 0.9996 0.6297 0.9650 -0.0348 0.3146  -0.0006 216 LEU A C   
1687 O O   . LEU A 216 ? 0.9275 0.5548 0.8969 -0.0377 0.3200  0.0001  216 LEU A O   
1688 C CB  . LEU A 216 ? 0.9685 0.6071 0.9401 -0.0235 0.3143  0.0033  216 LEU A CB  
1689 C CG  . LEU A 216 ? 1.0222 0.6709 0.9986 -0.0158 0.3111  0.0042  216 LEU A CG  
1690 C CD1 . LEU A 216 ? 0.9984 0.6406 0.9726 -0.0110 0.3153  0.0071  216 LEU A CD1 
1691 C CD2 . LEU A 216 ? 1.0345 0.7017 1.0303 -0.0184 0.3102  0.0007  216 LEU A CD2 
1692 N N   . THR A 217 ? 0.9980 0.6218 0.9529 -0.0358 0.3123  -0.0018 217 THR A N   
1693 C CA  . THR A 217 ? 0.9241 0.5373 0.8740 -0.0419 0.3165  -0.0024 217 THR A CA  
1694 C C   . THR A 217 ? 0.9931 0.6129 0.9556 -0.0491 0.3183  -0.0056 217 THR A C   
1695 O O   . THR A 217 ? 0.9824 0.6137 0.9564 -0.0513 0.3154  -0.0093 217 THR A O   
1696 C CB  . THR A 217 ? 0.9522 0.5579 0.8878 -0.0405 0.3145  -0.0028 217 THR A CB  
1697 O OG1 . THR A 217 ? 1.0704 0.6651 0.9929 -0.0329 0.3168  0.0021  217 THR A OG1 
1698 C CG2 . THR A 217 ? 0.9115 0.5079 0.8442 -0.0473 0.3189  -0.0042 217 THR A CG2 
1699 N N   . LEU A 218 ? 0.8623 0.4745 0.8236 -0.0519 0.3238  -0.0048 218 LEU A N   
1700 C CA  . LEU A 218 ? 0.8323 0.4468 0.8022 -0.0565 0.3279  -0.0058 218 LEU A CA  
1701 C C   . LEU A 218 ? 0.9203 0.5250 0.8828 -0.0572 0.3319  -0.0059 218 LEU A C   
1702 O O   . LEU A 218 ? 0.8783 0.4797 0.8366 -0.0527 0.3331  -0.0056 218 LEU A O   
1703 C CB  . LEU A 218 ? 0.8893 0.5114 0.8702 -0.0538 0.3320  -0.0031 218 LEU A CB  
1704 C CG  . LEU A 218 ? 0.8467 0.4688 0.8373 -0.0571 0.3398  -0.0023 218 LEU A CG  
1705 C CD1 . LEU A 218 ? 0.8786 0.5057 0.8816 -0.0648 0.3382  -0.0076 218 LEU A CD1 
1706 C CD2 . LEU A 218 ? 0.8730 0.5003 0.8717 -0.0523 0.3465  0.0021  218 LEU A CD2 
1707 N N   . ILE A 219 ? 0.8886 0.4897 0.8508 -0.0623 0.3333  -0.0080 219 ILE A N   
1708 C CA  . ILE A 219 ? 0.9042 0.4976 0.8603 -0.0625 0.3366  -0.0091 219 ILE A CA  
1709 C C   . ILE A 219 ? 0.8495 0.4426 0.8109 -0.0631 0.3424  -0.0076 219 ILE A C   
1710 O O   . ILE A 219 ? 0.9505 0.5429 0.9174 -0.0689 0.3435  -0.0092 219 ILE A O   
1711 C CB  . ILE A 219 ? 0.8994 0.4862 0.8483 -0.0667 0.3347  -0.0122 219 ILE A CB  
1712 C CG1 . ILE A 219 ? 0.8940 0.4775 0.8363 -0.0646 0.3324  -0.0116 219 ILE A CG1 
1713 C CG2 . ILE A 219 ? 0.8551 0.4361 0.8004 -0.0666 0.3380  -0.0145 219 ILE A CG2 
1714 C CD1 . ILE A 219 ? 0.9019 0.4902 0.8427 -0.0634 0.3275  -0.0105 219 ILE A CD1 
1715 N N   . ALA A 220 ? 0.8196 0.4124 0.7789 -0.0559 0.3469  -0.0047 220 ALA A N   
1716 C CA  . ALA A 220 ? 0.8782 0.4679 0.8399 -0.0533 0.3555  -0.0006 220 ALA A CA  
1717 C C   . ALA A 220 ? 0.8433 0.4267 0.7938 -0.0469 0.3580  -0.0013 220 ALA A C   
1718 O O   . ALA A 220 ? 0.8485 0.4336 0.7919 -0.0418 0.3533  -0.0056 220 ALA A O   
1719 C CB  . ALA A 220 ? 0.8759 0.4700 0.8412 -0.0464 0.3607  0.0047  220 ALA A CB  
1720 N N   . HIS A 221 ? 0.8278 0.4040 0.7784 -0.0467 0.3661  0.0020  221 HIS A N   
1721 C CA  . HIS A 221 ? 0.8703 0.4400 0.8090 -0.0385 0.3692  0.0021  221 HIS A CA  
1722 C C   . HIS A 221 ? 0.9312 0.4940 0.8656 -0.0285 0.3818  0.0108  221 HIS A C   
1723 O O   . HIS A 221 ? 0.9496 0.5076 0.8954 -0.0343 0.3910  0.0157  221 HIS A O   
1724 C CB  . HIS A 221 ? 0.8181 0.3817 0.7576 -0.0467 0.3683  -0.0018 221 HIS A CB  
1725 C CG  . HIS A 221 ? 0.8388 0.4067 0.7805 -0.0554 0.3588  -0.0086 221 HIS A CG  
1726 N ND1 . HIS A 221 ? 0.8785 0.4499 0.8286 -0.0646 0.3551  -0.0098 221 HIS A ND1 
1727 C CD2 . HIS A 221 ? 0.8178 0.3867 0.7542 -0.0549 0.3535  -0.0145 221 HIS A CD2 
1728 C CE1 . HIS A 221 ? 0.8619 0.4340 0.8082 -0.0681 0.3488  -0.0144 221 HIS A CE1 
1729 N NE2 . HIS A 221 ? 0.8872 0.4573 0.8269 -0.0635 0.3487  -0.0172 221 HIS A NE2 
1730 N N   . LEU A 222 ? 0.9447 0.5071 0.8634 -0.0124 0.3829  0.0121  222 LEU A N   
1731 C CA  . LEU A 222 ? 0.9379 0.4915 0.8460 0.0019  0.3963  0.0219  222 LEU A CA  
1732 C C   . LEU A 222 ? 0.9551 0.5027 0.8462 0.0144  0.3970  0.0208  222 LEU A C   
1733 O O   . LEU A 222 ? 0.9978 0.5524 0.8743 0.0305  0.3910  0.0165  222 LEU A O   
1734 C CB  . LEU A 222 ? 0.9829 0.5431 0.8838 0.0150  0.3969  0.0250  222 LEU A CB  
1735 C CG  . LEU A 222 ? 1.0130 0.5785 0.9302 0.0054  0.3986  0.0277  222 LEU A CG  
1736 C CD1 . LEU A 222 ? 1.0122 0.5885 0.9407 -0.0080 0.3840  0.0182  222 LEU A CD1 
1737 C CD2 . LEU A 222 ? 1.0071 0.5757 0.9146 0.0212  0.4037  0.0334  222 LEU A CD2 
1738 N N   . PRO A 223 ? 0.9328 0.4687 0.8263 0.0083  0.4038  0.0230  223 PRO A N   
1739 C CA  . PRO A 223 ? 0.9977 0.5284 0.8748 0.0210  0.4039  0.0216  223 PRO A CA  
1740 C C   . PRO A 223 ? 1.0534 0.5769 0.9085 0.0455  0.4142  0.0306  223 PRO A C   
1741 O O   . PRO A 223 ? 1.0954 0.6240 0.9331 0.0628  0.4079  0.0255  223 PRO A O   
1742 C CB  . PRO A 223 ? 0.9261 0.4440 0.8128 0.0077  0.4109  0.0232  223 PRO A CB  
1743 C CG  . PRO A 223 ? 0.9800 0.4936 0.8859 -0.0060 0.4197  0.0283  223 PRO A CG  
1744 C CD  . PRO A 223 ? 0.9989 0.5276 0.9114 -0.0098 0.4101  0.0247  223 PRO A CD  
1745 N N   . ASP A 224 ? 1.0723 0.5844 0.9275 0.0491  0.4304  0.0434  224 ASP A N   
1746 C CA  . ASP A 224 ? 1.2250 0.7281 1.0554 0.0753  0.4425  0.0540  224 ASP A CA  
1747 C C   . ASP A 224 ? 1.2376 0.7581 1.0523 0.0933  0.4294  0.0470  224 ASP A C   
1748 O O   . ASP A 224 ? 1.3166 0.8357 1.1051 0.1195  0.4313  0.0493  224 ASP A O   
1749 C CB  . ASP A 224 ? 1.3718 0.8601 1.2091 0.0742  0.4642  0.0689  224 ASP A CB  
1750 C CG  . ASP A 224 ? 1.4101 0.8796 1.2640 0.0595  0.4800  0.0747  224 ASP A CG  
1751 O OD1 . ASP A 224 ? 1.2657 0.7294 1.1162 0.0576  0.4771  0.0708  224 ASP A OD1 
1752 O OD2 . ASP A 224 ? 1.5284 0.9895 1.4009 0.0500  0.4957  0.0819  224 ASP A OD2 
1753 N N   . ARG A 225 ? 1.2606 0.7976 1.0905 0.0810  0.4160  0.0376  225 ARG A N   
1754 C CA  . ARG A 225 ? 1.2449 0.7992 1.0652 0.0955  0.4030  0.0281  225 ARG A CA  
1755 C C   . ARG A 225 ? 1.1960 0.7662 1.0229 0.0911  0.3840  0.0098  225 ARG A C   
1756 O O   . ARG A 225 ? 1.1893 0.7752 1.0116 0.1034  0.3725  -0.0016 225 ARG A O   
1757 C CB  . ARG A 225 ? 1.2440 0.8053 1.0771 0.0869  0.4021  0.0294  225 ARG A CB  
1758 C CG  . ARG A 225 ? 1.3618 0.9115 1.1893 0.0948  0.4207  0.0455  225 ARG A CG  
1759 C CD  . ARG A 225 ? 1.4535 1.0142 1.2916 0.0899  0.4165  0.0439  225 ARG A CD  
1760 N NE  . ARG A 225 ? 1.5917 1.1421 1.4374 0.0867  0.4348  0.0580  225 ARG A NE  
1761 C CZ  . ARG A 225 ? 1.7088 1.2671 1.5671 0.0806  0.4344  0.0585  225 ARG A CZ  
1762 N NH1 . ARG A 225 ? 1.5817 1.1561 1.4446 0.0774  0.4174  0.0470  225 ARG A NH1 
1763 N NH2 . ARG A 225 ? 1.7545 1.3038 1.6227 0.0774  0.4527  0.0705  225 ARG A NH2 
1764 N N   . ARG A 226 ? 1.1101 0.6771 0.9495 0.0740  0.3811  0.0056  226 ARG A N   
1765 C CA  . ARG A 226 ? 1.0761 0.6567 0.9249 0.0680  0.3660  -0.0112 226 ARG A CA  
1766 C C   . ARG A 226 ? 1.0221 0.6153 0.8876 0.0567  0.3564  -0.0200 226 ARG A C   
1767 O O   . ARG A 226 ? 0.9520 0.5595 0.8226 0.0611  0.3451  -0.0350 226 ARG A O   
1768 C CB  . ARG A 226 ? 1.1323 0.7229 0.9651 0.0918  0.3590  -0.0212 226 ARG A CB  
1769 C CG  . ARG A 226 ? 1.1993 0.7766 1.0117 0.1073  0.3689  -0.0120 226 ARG A CG  
1770 C CD  . ARG A 226 ? 1.2024 0.7714 1.0248 0.0909  0.3703  -0.0127 226 ARG A CD  
1771 N NE  . ARG A 226 ? 1.3688 0.9262 1.1716 0.1076  0.3782  -0.0064 226 ARG A NE  
1772 C CZ  . ARG A 226 ? 1.2652 0.8006 1.0595 0.1086  0.3956  0.0106  226 ARG A CZ  
1773 N NH1 . ARG A 226 ? 1.2430 0.7677 1.0488 0.0935  0.4062  0.0214  226 ARG A NH1 
1774 N NH2 . ARG A 226 ? 1.2628 0.7865 1.0381 0.1256  0.4031  0.0159  226 ARG A NH2 
1775 N N   . GLU A 227 ? 0.9466 0.5345 0.8221 0.0427  0.3613  -0.0115 227 GLU A N   
1776 C CA  . GLU A 227 ? 0.9236 0.5205 0.8124 0.0337  0.3542  -0.0171 227 GLU A CA  
1777 C C   . GLU A 227 ? 0.9132 0.5053 0.8178 0.0112  0.3540  -0.0154 227 GLU A C   
1778 O O   . GLU A 227 ? 0.9167 0.4991 0.8234 0.0027  0.3614  -0.0068 227 GLU A O   
1779 C CB  . GLU A 227 ? 0.9917 0.5896 0.8756 0.0423  0.3591  -0.0093 227 GLU A CB  
1780 C CG  . GLU A 227 ? 1.1267 0.7298 0.9913 0.0678  0.3592  -0.0107 227 GLU A CG  
1781 C CD  . GLU A 227 ? 1.0876 0.6916 0.9472 0.0763  0.3649  -0.0028 227 GLU A CD  
1782 O OE1 . GLU A 227 ? 1.0160 0.6190 0.8900 0.0613  0.3667  0.0015  227 GLU A OE1 
1783 O OE2 . GLU A 227 ? 1.2025 0.8086 1.0426 0.0993  0.3675  -0.0012 227 GLU A OE2 
1784 N N   . ILE A 228 ? 0.8139 0.4126 0.7296 0.0027  0.3462  -0.0242 228 ILE A N   
1785 C CA  . ILE A 228 ? 0.8041 0.3989 0.7309 -0.0147 0.3454  -0.0225 228 ILE A CA  
1786 C C   . ILE A 228 ? 0.8436 0.4435 0.7769 -0.0161 0.3422  -0.0234 228 ILE A C   
1787 O O   . ILE A 228 ? 0.7969 0.4037 0.7331 -0.0103 0.3374  -0.0324 228 ILE A O   
1788 C CB  . ILE A 228 ? 0.8434 0.4370 0.7756 -0.0231 0.3419  -0.0307 228 ILE A CB  
1789 C CG1 . ILE A 228 ? 0.8176 0.4069 0.7428 -0.0200 0.3445  -0.0309 228 ILE A CG1 
1790 C CG2 . ILE A 228 ? 0.8170 0.4053 0.7556 -0.0376 0.3420  -0.0276 228 ILE A CG2 
1791 C CD1 . ILE A 228 ? 0.7988 0.3871 0.7295 -0.0279 0.3422  -0.0387 228 ILE A CD1 
1792 N N   . ILE A 229 ? 0.8025 0.4001 0.7399 -0.0233 0.3448  -0.0155 229 ILE A N   
1793 C CA  . ILE A 229 ? 0.7926 0.3947 0.7349 -0.0230 0.3426  -0.0146 229 ILE A CA  
1794 C C   . ILE A 229 ? 0.8068 0.4059 0.7554 -0.0352 0.3407  -0.0128 229 ILE A C   
1795 O O   . ILE A 229 ? 0.8843 0.4818 0.8355 -0.0412 0.3429  -0.0078 229 ILE A O   
1796 C CB  . ILE A 229 ? 0.8539 0.4586 0.7940 -0.0157 0.3478  -0.0067 229 ILE A CB  
1797 C CG1 . ILE A 229 ? 0.8085 0.4144 0.7369 -0.0001 0.3509  -0.0070 229 ILE A CG1 
1798 C CG2 . ILE A 229 ? 0.7950 0.4053 0.7402 -0.0145 0.3450  -0.0067 229 ILE A CG2 
1799 C CD1 . ILE A 229 ? 0.8930 0.4983 0.8168 0.0090  0.3597  0.0027  229 ILE A CD1 
1800 N N   . SER A 230 ? 0.7853 0.3833 0.7367 -0.0376 0.3373  -0.0176 230 SER A N   
1801 C CA  . SER A 230 ? 0.8328 0.4263 0.7855 -0.0454 0.3362  -0.0153 230 SER A CA  
1802 C C   . SER A 230 ? 0.7902 0.3847 0.7456 -0.0424 0.3348  -0.0149 230 SER A C   
1803 O O   . SER A 230 ? 0.7866 0.3823 0.7454 -0.0375 0.3347  -0.0204 230 SER A O   
1804 C CB  . SER A 230 ? 0.8636 0.4497 0.8150 -0.0508 0.3371  -0.0196 230 SER A CB  
1805 O OG  . SER A 230 ? 0.8998 0.4797 0.8485 -0.0546 0.3373  -0.0167 230 SER A OG  
1806 N N   . PHE A 231 ? 0.8317 0.4264 0.7862 -0.0443 0.3334  -0.0098 231 PHE A N   
1807 C CA  . PHE A 231 ? 0.8114 0.4074 0.7674 -0.0400 0.3322  -0.0080 231 PHE A CA  
1808 C C   . PHE A 231 ? 0.8649 0.4568 0.8158 -0.0413 0.3306  -0.0041 231 PHE A C   
1809 O O   . PHE A 231 ? 0.8984 0.4946 0.8481 -0.0439 0.3279  -0.0025 231 PHE A O   
1810 C CB  . PHE A 231 ? 0.7879 0.3941 0.7482 -0.0352 0.3317  -0.0052 231 PHE A CB  
1811 C CG  . PHE A 231 ? 0.8704 0.4792 0.8326 -0.0301 0.3301  -0.0034 231 PHE A CG  
1812 C CD1 . PHE A 231 ? 0.8972 0.5097 0.8598 -0.0304 0.3273  0.0004  231 PHE A CD1 
1813 C CD2 . PHE A 231 ? 0.8402 0.4489 0.8040 -0.0240 0.3307  -0.0068 231 PHE A CD2 
1814 C CE1 . PHE A 231 ? 0.9090 0.5239 0.8726 -0.0244 0.3258  0.0022  231 PHE A CE1 
1815 C CE2 . PHE A 231 ? 0.8395 0.4497 0.8050 -0.0191 0.3297  -0.0052 231 PHE A CE2 
1816 C CZ  . PHE A 231 ? 0.8550 0.4676 0.8197 -0.0192 0.3276  0.0001  231 PHE A CZ  
1817 N N   . GLY A 232 ? 0.8536 0.4372 0.8018 -0.0383 0.3327  -0.0034 232 GLY A N   
1818 C CA  . GLY A 232 ? 0.9565 0.5354 0.8959 -0.0349 0.3317  0.0016  232 GLY A CA  
1819 C C   . GLY A 232 ? 1.0387 0.6040 0.9677 -0.0362 0.3360  0.0033  232 GLY A C   
1820 O O   . GLY A 232 ? 1.0621 0.6210 0.9796 -0.0302 0.3365  0.0084  232 GLY A O   
1821 N N   . SER A 233 ? 0.9674 0.5280 0.8987 -0.0424 0.3396  -0.0005 233 SER A N   
1822 C CA  . SER A 233 ? 0.9466 0.4941 0.8684 -0.0438 0.3454  0.0013  233 SER A CA  
1823 C C   . SER A 233 ? 0.9918 0.5300 0.9233 -0.0482 0.3539  -0.0039 233 SER A C   
1824 O O   . SER A 233 ? 0.9818 0.5279 0.9258 -0.0511 0.3521  -0.0112 233 SER A O   
1825 C CB  . SER A 233 ? 1.0331 0.5859 0.9492 -0.0475 0.3410  0.0003  233 SER A CB  
1826 O OG  . SER A 233 ? 1.0710 0.6110 0.9773 -0.0482 0.3473  0.0017  233 SER A OG  
1827 N N   . GLY A 234 ? 1.0717 0.5933 0.9977 -0.0476 0.3639  -0.0008 234 GLY A N   
1828 C CA  . GLY A 234 ? 0.9263 0.4391 0.8660 -0.0528 0.3739  -0.0074 234 GLY A CA  
1829 C C   . GLY A 234 ? 0.9688 0.4721 0.9021 -0.0563 0.3810  -0.0062 234 GLY A C   
1830 O O   . GLY A 234 ? 1.0497 0.5442 0.9956 -0.0608 0.3918  -0.0114 234 GLY A O   
1831 N N   . TYR A 235 ? 0.9758 0.4821 0.8919 -0.0543 0.3753  -0.0010 235 TYR A N   
1832 C CA  . TYR A 235 ? 1.0004 0.4965 0.9054 -0.0552 0.3820  0.0017  235 TYR A CA  
1833 C C   . TYR A 235 ? 1.0429 0.5492 0.9555 -0.0625 0.3772  -0.0060 235 TYR A C   
1834 O O   . TYR A 235 ? 1.0361 0.5563 0.9481 -0.0635 0.3659  -0.0081 235 TYR A O   
1835 C CB  . TYR A 235 ? 1.1034 0.5969 0.9835 -0.0462 0.3780  0.0102  235 TYR A CB  
1836 C CG  . TYR A 235 ? 1.1616 0.6390 1.0253 -0.0427 0.3888  0.0155  235 TYR A CG  
1837 C CD1 . TYR A 235 ? 1.0859 0.5419 0.9406 -0.0360 0.4045  0.0239  235 TYR A CD1 
1838 C CD2 . TYR A 235 ? 1.1027 0.5847 0.9595 -0.0452 0.3850  0.0126  235 TYR A CD2 
1839 C CE1 . TYR A 235 ? 1.1240 0.5635 0.9618 -0.0311 0.4169  0.0301  235 TYR A CE1 
1840 C CE2 . TYR A 235 ? 1.1050 0.5722 0.9451 -0.0407 0.3955  0.0176  235 TYR A CE2 
1841 C CZ  . TYR A 235 ? 1.1265 0.5723 0.9564 -0.0332 0.4119  0.0268  235 TYR A CZ  
1842 O OH  . TYR A 235 ? 1.0547 0.4838 0.8660 -0.0271 0.4249  0.0334  235 TYR A OH  
1843 N N   . GLY A 236 ? 0.9719 0.4707 0.8928 -0.0674 0.3871  -0.0103 236 GLY A N   
1844 C CA  . GLY A 236 ? 0.9661 0.4716 0.8920 -0.0729 0.3847  -0.0170 236 GLY A CA  
1845 C C   . GLY A 236 ? 0.9521 0.4740 0.8797 -0.0741 0.3715  -0.0210 236 GLY A C   
1846 O O   . GLY A 236 ? 1.0155 0.5473 0.9566 -0.0747 0.3674  -0.0273 236 GLY A O   
1847 N N   . GLY A 237 ? 0.9026 0.4271 0.8167 -0.0735 0.3656  -0.0177 237 GLY A N   
1848 C CA  . GLY A 237 ? 0.9714 0.5080 0.8889 -0.0754 0.3566  -0.0211 237 GLY A CA  
1849 C C   . GLY A 237 ? 1.0327 0.5788 0.9579 -0.0732 0.3510  -0.0211 237 GLY A C   
1850 O O   . GLY A 237 ? 1.0033 0.5571 0.9354 -0.0734 0.3479  -0.0247 237 GLY A O   
1851 N N   . ASN A 238 ? 0.9965 0.5415 0.9192 -0.0695 0.3504  -0.0166 238 ASN A N   
1852 C CA  . ASN A 238 ? 0.9589 0.5130 0.8883 -0.0667 0.3455  -0.0161 238 ASN A CA  
1853 C C   . ASN A 238 ? 0.9908 0.5467 0.9322 -0.0655 0.3481  -0.0215 238 ASN A C   
1854 O O   . ASN A 238 ? 0.9933 0.5584 0.9401 -0.0627 0.3443  -0.0237 238 ASN A O   
1855 C CB  . ASN A 238 ? 0.9755 0.5291 0.8981 -0.0621 0.3433  -0.0102 238 ASN A CB  
1856 C CG  . ASN A 238 ? 1.0363 0.5909 0.9474 -0.0610 0.3391  -0.0078 238 ASN A CG  
1857 O OD1 . ASN A 238 ? 1.0502 0.6096 0.9623 -0.0648 0.3359  -0.0109 238 ASN A OD1 
1858 N ND2 . ASN A 238 ? 1.0503 0.6004 0.9501 -0.0544 0.3390  -0.0032 238 ASN A ND2 
1859 N N   . SER A 239 ? 0.9623 0.5095 0.9089 -0.0667 0.3553  -0.0247 239 SER A N   
1860 C CA  . SER A 239 ? 0.9106 0.4606 0.8726 -0.0654 0.3575  -0.0329 239 SER A CA  
1861 C C   . SER A 239 ? 0.9131 0.4682 0.8871 -0.0675 0.3586  -0.0442 239 SER A C   
1862 O O   . SER A 239 ? 0.8358 0.4013 0.8205 -0.0636 0.3546  -0.0534 239 SER A O   
1863 C CB  . SER A 239 ? 0.9263 0.4635 0.8923 -0.0655 0.3665  -0.0312 239 SER A CB  
1864 O OG  . SER A 239 ? 0.9860 0.5103 0.9501 -0.0694 0.3763  -0.0298 239 SER A OG  
1865 N N   . LEU A 240 ? 0.9586 0.5075 0.9308 -0.0721 0.3635  -0.0447 240 LEU A N   
1866 C CA  . LEU A 240 ? 0.8532 0.4084 0.8371 -0.0736 0.3640  -0.0561 240 LEU A CA  
1867 C C   . LEU A 240 ? 0.9251 0.4900 0.9000 -0.0698 0.3555  -0.0554 240 LEU A C   
1868 O O   . LEU A 240 ? 1.0135 0.5754 0.9789 -0.0723 0.3555  -0.0515 240 LEU A O   
1869 C CB  . LEU A 240 ? 0.9153 0.4597 0.9002 -0.0795 0.3738  -0.0559 240 LEU A CB  
1870 C CG  . LEU A 240 ? 0.9255 0.4541 0.9135 -0.0820 0.3861  -0.0517 240 LEU A CG  
1871 C CD1 . LEU A 240 ? 0.8945 0.4122 0.8846 -0.0867 0.3982  -0.0520 240 LEU A CD1 
1872 C CD2 . LEU A 240 ? 0.8255 0.3566 0.8353 -0.0816 0.3893  -0.0611 240 LEU A CD2 
1873 N N   . LEU A 241 ? 0.9808 0.5565 0.9583 -0.0628 0.3492  -0.0591 241 LEU A N   
1874 C CA  . LEU A 241 ? 0.9857 0.5670 0.9522 -0.0574 0.3440  -0.0549 241 LEU A CA  
1875 C C   . LEU A 241 ? 0.9270 0.5114 0.8931 -0.0557 0.3435  -0.0609 241 LEU A C   
1876 O O   . LEU A 241 ? 0.9512 0.5340 0.9065 -0.0538 0.3427  -0.0549 241 LEU A O   
1877 C CB  . LEU A 241 ? 0.8315 0.4221 0.7985 -0.0478 0.3394  -0.0567 241 LEU A CB  
1878 C CG  . LEU A 241 ? 0.8480 0.4357 0.8130 -0.0489 0.3396  -0.0487 241 LEU A CG  
1879 C CD1 . LEU A 241 ? 0.8244 0.4208 0.7873 -0.0387 0.3359  -0.0488 241 LEU A CD1 
1880 C CD2 . LEU A 241 ? 0.8746 0.4551 0.8297 -0.0549 0.3409  -0.0371 241 LEU A CD2 
1881 N N   . GLY A 242 ? 0.8640 0.4527 0.8437 -0.0561 0.3449  -0.0733 242 GLY A N   
1882 C CA  . GLY A 242 ? 0.8857 0.4787 0.8660 -0.0538 0.3441  -0.0800 242 GLY A CA  
1883 C C   . GLY A 242 ? 1.0169 0.5993 0.9903 -0.0621 0.3490  -0.0738 242 GLY A C   
1884 O O   . GLY A 242 ? 0.8825 0.4673 0.8547 -0.0601 0.3485  -0.0781 242 GLY A O   
1885 N N   . LYS A 243 ? 0.9631 0.5343 0.9306 -0.0698 0.3532  -0.0643 243 LYS A N   
1886 C CA  . LYS A 243 ? 0.8816 0.4434 0.8410 -0.0760 0.3573  -0.0595 243 LYS A CA  
1887 C C   . LYS A 243 ? 0.9163 0.4757 0.8614 -0.0753 0.3535  -0.0513 243 LYS A C   
1888 O O   . LYS A 243 ? 0.9637 0.5259 0.9063 -0.0718 0.3517  -0.0533 243 LYS A O   
1889 C CB  . LYS A 243 ? 0.9316 0.4825 0.8891 -0.0814 0.3641  -0.0541 243 LYS A CB  
1890 C CG  . LYS A 243 ? 0.9419 0.4833 0.8906 -0.0856 0.3696  -0.0510 243 LYS A CG  
1891 C CD  . LYS A 243 ? 0.8394 0.3686 0.7870 -0.0879 0.3798  -0.0469 243 LYS A CD  
1892 C CE  . LYS A 243 ? 0.9347 0.4539 0.8683 -0.0893 0.3854  -0.0424 243 LYS A CE  
1893 N NZ  . LYS A 243 ? 0.8356 0.3579 0.7768 -0.0918 0.3880  -0.0503 243 LYS A NZ  
1894 N N   . LYS A 244 ? 0.9210 0.4756 0.8583 -0.0780 0.3527  -0.0430 244 LYS A N   
1895 C CA  . LYS A 244 ? 0.8011 0.3546 0.7307 -0.0788 0.3498  -0.0379 244 LYS A CA  
1896 C C   . LYS A 244 ? 0.8273 0.3864 0.7590 -0.0732 0.3478  -0.0364 244 LYS A C   
1897 O O   . LYS A 244 ? 0.8570 0.4147 0.7862 -0.0711 0.3488  -0.0361 244 LYS A O   
1898 C CB  . LYS A 244 ? 0.8602 0.4110 0.7841 -0.0815 0.3481  -0.0325 244 LYS A CB  
1899 C CG  . LYS A 244 ? 0.9292 0.4726 0.8456 -0.0837 0.3514  -0.0320 244 LYS A CG  
1900 C CD  . LYS A 244 ? 0.9021 0.4416 0.8147 -0.0861 0.3536  -0.0355 244 LYS A CD  
1901 C CE  . LYS A 244 ? 0.8697 0.4009 0.7718 -0.0864 0.3582  -0.0339 244 LYS A CE  
1902 N NZ  . LYS A 244 ? 0.9696 0.4974 0.8680 -0.0883 0.3606  -0.0376 244 LYS A NZ  
1903 N N   . CYS A 245 ? 0.8899 0.4536 0.8250 -0.0697 0.3462  -0.0348 245 CYS A N   
1904 C CA  . CYS A 245 ? 0.8920 0.4599 0.8268 -0.0630 0.3458  -0.0315 245 CYS A CA  
1905 C C   . CYS A 245 ? 0.8215 0.3912 0.7535 -0.0546 0.3468  -0.0351 245 CYS A C   
1906 O O   . CYS A 245 ? 0.8720 0.4386 0.7990 -0.0502 0.3499  -0.0303 245 CYS A O   
1907 C CB  . CYS A 245 ? 0.8889 0.4623 0.8275 -0.0592 0.3438  -0.0311 245 CYS A CB  
1908 S SG  . CYS A 245 ? 0.8524 0.4237 0.7920 -0.0656 0.3425  -0.0264 245 CYS A SG  
1909 N N   . PHE A 246 ? 0.8108 0.3856 0.7469 -0.0513 0.3449  -0.0442 246 PHE A N   
1910 C CA  . PHE A 246 ? 0.8232 0.4032 0.7565 -0.0403 0.3439  -0.0502 246 PHE A CA  
1911 C C   . PHE A 246 ? 0.9005 0.4755 0.8312 -0.0432 0.3460  -0.0522 246 PHE A C   
1912 O O   . PHE A 246 ? 0.8495 0.4203 0.7712 -0.0369 0.3483  -0.0483 246 PHE A O   
1913 C CB  . PHE A 246 ? 0.8169 0.4087 0.7605 -0.0346 0.3396  -0.0628 246 PHE A CB  
1914 C CG  . PHE A 246 ? 0.8763 0.4778 0.8175 -0.0201 0.3360  -0.0722 246 PHE A CG  
1915 C CD1 . PHE A 246 ? 0.9037 0.5007 0.8301 -0.0109 0.3381  -0.0660 246 PHE A CD1 
1916 C CD2 . PHE A 246 ? 0.9150 0.5306 0.8697 -0.0145 0.3309  -0.0882 246 PHE A CD2 
1917 C CE1 . PHE A 246 ? 0.9403 0.5463 0.8612 0.0057  0.3344  -0.0744 246 PHE A CE1 
1918 C CE2 . PHE A 246 ? 0.9181 0.5459 0.8706 0.0013  0.3257  -0.0993 246 PHE A CE2 
1919 C CZ  . PHE A 246 ? 1.0251 0.6480 0.9585 0.0125  0.3271  -0.0917 246 PHE A CZ  
1920 N N   . ALA A 247 ? 0.8484 0.4224 0.7862 -0.0520 0.3466  -0.0575 247 ALA A N   
1921 C CA  . ALA A 247 ? 0.8435 0.4154 0.7806 -0.0531 0.3483  -0.0620 247 ALA A CA  
1922 C C   . ALA A 247 ? 0.8060 0.3669 0.7333 -0.0574 0.3512  -0.0539 247 ALA A C   
1923 O O   . ALA A 247 ? 0.8103 0.3687 0.7345 -0.0555 0.3527  -0.0566 247 ALA A O   
1924 C CB  . ALA A 247 ? 0.8105 0.3826 0.7584 -0.0616 0.3507  -0.0688 247 ALA A CB  
1925 N N   . LEU A 248 ? 0.8775 0.4329 0.8020 -0.0629 0.3521  -0.0457 248 LEU A N   
1926 C CA  . LEU A 248 ? 0.8116 0.3581 0.7316 -0.0675 0.3548  -0.0408 248 LEU A CA  
1927 C C   . LEU A 248 ? 0.8862 0.4297 0.8052 -0.0637 0.3578  -0.0337 248 LEU A C   
1928 O O   . LEU A 248 ? 0.9326 0.4693 0.8477 -0.0590 0.3627  -0.0312 248 LEU A O   
1929 C CB  . LEU A 248 ? 0.8109 0.3546 0.7313 -0.0776 0.3535  -0.0403 248 LEU A CB  
1930 C CG  . LEU A 248 ? 0.8948 0.4368 0.8135 -0.0810 0.3543  -0.0454 248 LEU A CG  
1931 C CD1 . LEU A 248 ? 0.8500 0.3877 0.7635 -0.0873 0.3535  -0.0441 248 LEU A CD1 
1932 C CD2 . LEU A 248 ? 0.8155 0.3554 0.7326 -0.0781 0.3564  -0.0496 248 LEU A CD2 
1933 N N   . ARG A 249 ? 0.8278 0.3749 0.7506 -0.0649 0.3566  -0.0298 249 ARG A N   
1934 C CA  . ARG A 249 ? 0.8636 0.4071 0.7886 -0.0632 0.3618  -0.0230 249 ARG A CA  
1935 C C   . ARG A 249 ? 0.8411 0.3826 0.7586 -0.0494 0.3667  -0.0192 249 ARG A C   
1936 O O   . ARG A 249 ? 0.9070 0.4388 0.8214 -0.0456 0.3747  -0.0145 249 ARG A O   
1937 C CB  . ARG A 249 ? 0.8119 0.3614 0.7435 -0.0671 0.3591  -0.0206 249 ARG A CB  
1938 C CG  . ARG A 249 ? 0.8939 0.4452 0.8296 -0.0772 0.3543  -0.0239 249 ARG A CG  
1939 C CD  . ARG A 249 ? 0.9251 0.4824 0.8683 -0.0799 0.3521  -0.0218 249 ARG A CD  
1940 N NE  . ARG A 249 ? 0.8919 0.4524 0.8340 -0.0850 0.3458  -0.0254 249 ARG A NE  
1941 C CZ  . ARG A 249 ? 0.9065 0.4695 0.8434 -0.0831 0.3421  -0.0250 249 ARG A CZ  
1942 N NH1 . ARG A 249 ? 0.8707 0.4351 0.8067 -0.0782 0.3431  -0.0231 249 ARG A NH1 
1943 N NH2 . ARG A 249 ? 0.9055 0.4690 0.8375 -0.0851 0.3380  -0.0269 249 ARG A NH2 
1944 N N   . ILE A 250 ? 0.8486 0.3988 0.7626 -0.0404 0.3625  -0.0215 250 ILE A N   
1945 C CA  . ILE A 250 ? 0.8767 0.4269 0.7799 -0.0235 0.3658  -0.0192 250 ILE A CA  
1946 C C   . ILE A 250 ? 0.9099 0.4568 0.8054 -0.0164 0.3664  -0.0231 250 ILE A C   
1947 O O   . ILE A 250 ? 0.9313 0.4701 0.8157 -0.0043 0.3735  -0.0173 250 ILE A O   
1948 C CB  . ILE A 250 ? 0.8982 0.4611 0.8007 -0.0145 0.3591  -0.0244 250 ILE A CB  
1949 C CG1 . ILE A 250 ? 0.8986 0.4636 0.8071 -0.0195 0.3596  -0.0191 250 ILE A CG1 
1950 C CG2 . ILE A 250 ? 0.9319 0.4971 0.8202 0.0066  0.3606  -0.0242 250 ILE A CG2 
1951 C CD1 . ILE A 250 ? 0.8510 0.4078 0.7559 -0.0151 0.3697  -0.0077 250 ILE A CD1 
1952 N N   . ALA A 251 ? 0.9262 0.4785 0.8272 -0.0230 0.3603  -0.0325 251 ALA A N   
1953 C CA  . ALA A 251 ? 0.9113 0.4629 0.8069 -0.0162 0.3601  -0.0379 251 ALA A CA  
1954 C C   . ALA A 251 ? 0.8575 0.3936 0.7481 -0.0190 0.3684  -0.0308 251 ALA A C   
1955 O O   . ALA A 251 ? 0.9185 0.4493 0.7988 -0.0068 0.3721  -0.0297 251 ALA A O   
1956 C CB  . ALA A 251 ? 0.8702 0.4301 0.7761 -0.0247 0.3541  -0.0493 251 ALA A CB  
1957 N N   . SER A 252 ? 0.8456 0.3746 0.7441 -0.0340 0.3712  -0.0270 252 SER A N   
1958 C CA  . SER A 252 ? 0.8561 0.3707 0.7544 -0.0380 0.3794  -0.0227 252 SER A CA  
1959 C C   . SER A 252 ? 1.0024 0.5056 0.8935 -0.0262 0.3906  -0.0126 252 SER A C   
1960 O O   . SER A 252 ? 0.9321 0.4228 0.8162 -0.0196 0.3986  -0.0093 252 SER A O   
1961 C CB  . SER A 252 ? 0.8494 0.3622 0.7600 -0.0548 0.3787  -0.0235 252 SER A CB  
1962 O OG  . SER A 252 ? 0.8874 0.4017 0.8049 -0.0571 0.3811  -0.0182 252 SER A OG  
1963 N N   . ARG A 253 ? 0.8899 0.3957 0.7817 -0.0225 0.3929  -0.0068 253 ARG A N   
1964 C CA  . ARG A 253 ? 0.9064 0.4006 0.7890 -0.0087 0.4058  0.0043  253 ARG A CA  
1965 C C   . ARG A 253 ? 0.9506 0.4441 0.8127 0.0131  0.4060  0.0047  253 ARG A C   
1966 O O   . ARG A 253 ? 1.0136 0.4911 0.8647 0.0240  0.4180  0.0125  253 ARG A O   
1967 C CB  . ARG A 253 ? 1.0160 0.5161 0.9019 -0.0072 0.4069  0.0092  253 ARG A CB  
1968 C CG  . ARG A 253 ? 1.0587 0.5480 0.9312 0.0108  0.4206  0.0213  253 ARG A CG  
1969 C CD  . ARG A 253 ? 1.1072 0.5766 0.9888 0.0052  0.4392  0.0309  253 ARG A CD  
1970 N NE  . ARG A 253 ? 1.2121 0.6737 1.0898 0.0156  0.4535  0.0429  253 ARG A NE  
1971 C CZ  . ARG A 253 ? 1.1834 0.6484 1.0793 0.0045  0.4575  0.0448  253 ARG A CZ  
1972 N NH1 . ARG A 253 ? 1.0706 0.5469 0.9885 -0.0161 0.4473  0.0353  253 ARG A NH1 
1973 N NH2 . ARG A 253 ? 1.1870 0.6440 1.0780 0.0158  0.4723  0.0565  253 ARG A NH2 
1974 N N   . LEU A 254 ? 0.9590 0.4699 0.8166 0.0205  0.3931  -0.0046 254 LEU A N   
1975 C CA  . LEU A 254 ? 0.9774 0.4928 0.8176 0.0428  0.3902  -0.0081 254 LEU A CA  
1976 C C   . LEU A 254 ? 1.0726 0.5793 0.9090 0.0435  0.3927  -0.0102 254 LEU A C   
1977 O O   . LEU A 254 ? 1.0561 0.5520 0.8749 0.0619  0.4006  -0.0040 254 LEU A O   
1978 C CB  . LEU A 254 ? 1.0324 0.5710 0.8770 0.0465  0.3747  -0.0226 254 LEU A CB  
1979 C CG  . LEU A 254 ? 1.0790 0.6282 0.9255 0.0499  0.3706  -0.0230 254 LEU A CG  
1980 C CD1 . LEU A 254 ? 1.0736 0.6448 0.9298 0.0514  0.3561  -0.0404 254 LEU A CD1 
1981 C CD2 . LEU A 254 ? 1.1380 0.6811 0.9634 0.0733  0.3784  -0.0130 254 LEU A CD2 
1982 N N   . ALA A 255 ? 0.9518 0.4624 0.8028 0.0251  0.3868  -0.0184 255 ALA A N   
1983 C CA  . ALA A 255 ? 1.0091 0.5128 0.8574 0.0251  0.3885  -0.0216 255 ALA A CA  
1984 C C   . ALA A 255 ? 1.0538 0.5336 0.8948 0.0283  0.4042  -0.0092 255 ALA A C   
1985 O O   . ALA A 255 ? 1.0327 0.5036 0.8602 0.0428  0.4091  -0.0072 255 ALA A O   
1986 C CB  . ALA A 255 ? 0.9834 0.4924 0.8479 0.0039  0.3821  -0.0302 255 ALA A CB  
1987 N N   . LYS A 256 ? 1.0306 0.4996 0.8822 0.0154  0.4129  -0.0016 256 LYS A N   
1988 C CA  . LYS A 256 ? 0.9785 0.4236 0.8279 0.0180  0.4308  0.0098  256 LYS A CA  
1989 C C   . LYS A 256 ? 1.0812 0.5163 0.9071 0.0447  0.4410  0.0206  256 LYS A C   
1990 O O   . LYS A 256 ? 1.1193 0.5355 0.9338 0.0559  0.4534  0.0276  256 LYS A O   
1991 C CB  . LYS A 256 ? 0.9952 0.4350 0.8639 0.0011  0.4381  0.0139  256 LYS A CB  
1992 C CG  . LYS A 256 ? 1.0338 0.4487 0.9052 0.0039  0.4599  0.0258  256 LYS A CG  
1993 C CD  . LYS A 256 ? 1.0470 0.4458 0.9216 -0.0003 0.4672  0.0237  256 LYS A CD  
1994 C CE  . LYS A 256 ? 1.1063 0.4780 0.9884 0.0006  0.4916  0.0348  256 LYS A CE  
1995 N NZ  . LYS A 256 ? 1.1615 0.5178 1.0186 0.0266  0.5067  0.0504  256 LYS A NZ  
1996 N N   . GLU A 257 ? 1.0767 0.5237 0.8935 0.0570  0.4362  0.0222  257 GLU A N   
1997 C CA  . GLU A 257 ? 1.0836 0.5232 0.8739 0.0862  0.4446  0.0318  257 GLU A CA  
1998 C C   . GLU A 257 ? 1.1142 0.5603 0.8861 0.1062  0.4365  0.0248  257 GLU A C   
1999 O O   . GLU A 257 ? 1.1544 0.5838 0.9042 0.1281  0.4484  0.0344  257 GLU A O   
2000 C CB  . GLU A 257 ? 1.2029 0.6571 0.9880 0.0952  0.4387  0.0321  257 GLU A CB  
2001 C CG  . GLU A 257 ? 1.1451 0.5952 0.9473 0.0786  0.4463  0.0390  257 GLU A CG  
2002 C CD  . GLU A 257 ? 1.2171 0.6845 1.0147 0.0868  0.4377  0.0368  257 GLU A CD  
2003 O OE1 . GLU A 257 ? 1.1859 0.6644 0.9636 0.1098  0.4296  0.0325  257 GLU A OE1 
2004 O OE2 . GLU A 257 ? 1.2078 0.6789 1.0225 0.0712  0.4382  0.0381  257 GLU A OE2 
2005 N N   . GLU A 258 ? 1.1015 0.5715 0.8826 0.1000  0.4174  0.0079  258 GLU A N   
2006 C CA  . GLU A 258 ? 1.0973 0.5809 0.8652 0.1199  0.4068  -0.0028 258 GLU A CA  
2007 C C   . GLU A 258 ? 1.1260 0.6033 0.8982 0.1133  0.4071  -0.0075 258 GLU A C   
2008 O O   . GLU A 258 ? 1.1733 0.6588 0.9333 0.1322  0.4010  -0.0149 258 GLU A O   
2009 C CB  . GLU A 258 ? 1.1522 0.6666 0.9320 0.1177  0.3873  -0.0206 258 GLU A CB  
2010 C CG  . GLU A 258 ? 1.1071 0.6300 0.8832 0.1250  0.3851  -0.0183 258 GLU A CG  
2011 C CD  . GLU A 258 ? 1.2707 0.8207 1.0657 0.1161  0.3680  -0.0363 258 GLU A CD  
2012 O OE1 . GLU A 258 ? 1.2167 0.7817 1.0238 0.1121  0.3576  -0.0519 258 GLU A OE1 
2013 O OE2 . GLU A 258 ? 1.2623 0.8181 1.0617 0.1130  0.3662  -0.0350 258 GLU A OE2 
2014 N N   . GLY A 259 ? 1.1083 0.5732 0.8976 0.0884  0.4132  -0.0049 259 GLY A N   
2015 C CA  . GLY A 259 ? 1.0842 0.5399 0.8760 0.0828  0.4156  -0.0080 259 GLY A CA  
2016 C C   . GLY A 259 ? 1.0277 0.5007 0.8381 0.0644  0.4022  -0.0233 259 GLY A C   
2017 O O   . GLY A 259 ? 1.1306 0.5987 0.9416 0.0623  0.4029  -0.0275 259 GLY A O   
2018 N N   . TRP A 260 ? 1.0353 0.5266 0.8601 0.0518  0.3916  -0.0313 260 TRP A N   
2019 C CA  . TRP A 260 ? 1.0111 0.5156 0.8529 0.0344  0.3823  -0.0439 260 TRP A CA  
2020 C C   . TRP A 260 ? 0.9859 0.4841 0.8417 0.0104  0.3845  -0.0404 260 TRP A C   
2021 O O   . TRP A 260 ? 0.9666 0.4485 0.8220 0.0056  0.3941  -0.0302 260 TRP A O   
2022 C CB  . TRP A 260 ? 1.0401 0.5702 0.8885 0.0406  0.3695  -0.0574 260 TRP A CB  
2023 C CG  . TRP A 260 ? 1.0526 0.5908 0.8998 0.0463  0.3665  -0.0553 260 TRP A CG  
2024 C CD1 . TRP A 260 ? 1.0076 0.5439 0.8373 0.0680  0.3689  -0.0489 260 TRP A CD1 
2025 C CD2 . TRP A 260 ? 0.9520 0.5010 0.8146 0.0319  0.3609  -0.0594 260 TRP A CD2 
2026 N NE1 . TRP A 260 ? 1.0169 0.5632 0.8511 0.0672  0.3647  -0.0496 260 TRP A NE1 
2027 C CE2 . TRP A 260 ? 0.9724 0.5263 0.8274 0.0448  0.3596  -0.0561 260 TRP A CE2 
2028 C CE3 . TRP A 260 ? 0.9569 0.5104 0.8369 0.0110  0.3579  -0.0648 260 TRP A CE3 
2029 C CZ2 . TRP A 260 ? 0.9791 0.5427 0.8453 0.0362  0.3548  -0.0588 260 TRP A CZ2 
2030 C CZ3 . TRP A 260 ? 0.9340 0.4958 0.8238 0.0035  0.3541  -0.0664 260 TRP A CZ3 
2031 C CH2 . TRP A 260 ? 0.9285 0.4955 0.8124 0.0154  0.3522  -0.0638 260 TRP A CH2 
2032 N N   . LEU A 261 ? 1.0054 0.5165 0.8745 -0.0036 0.3765  -0.0496 261 LEU A N   
2033 C CA  . LEU A 261 ? 0.9298 0.4368 0.8093 -0.0235 0.3769  -0.0479 261 LEU A CA  
2034 C C   . LEU A 261 ? 0.9300 0.4522 0.8192 -0.0309 0.3692  -0.0537 261 LEU A C   
2035 O O   . LEU A 261 ? 0.9136 0.4491 0.8073 -0.0271 0.3640  -0.0631 261 LEU A O   
2036 C CB  . LEU A 261 ? 0.8767 0.3767 0.7589 -0.0335 0.3785  -0.0519 261 LEU A CB  
2037 C CG  . LEU A 261 ? 0.9237 0.4057 0.7994 -0.0294 0.3874  -0.0470 261 LEU A CG  
2038 C CD1 . LEU A 261 ? 0.8946 0.3731 0.7727 -0.0376 0.3870  -0.0537 261 LEU A CD1 
2039 C CD2 . LEU A 261 ? 0.9012 0.3700 0.7811 -0.0355 0.3953  -0.0384 261 LEU A CD2 
2040 N N   . ALA A 262 ? 0.8980 0.4183 0.7923 -0.0414 0.3694  -0.0489 262 ALA A N   
2041 C CA  . ALA A 262 ? 0.8387 0.3694 0.7411 -0.0493 0.3640  -0.0524 262 ALA A CA  
2042 C C   . ALA A 262 ? 0.8361 0.3609 0.7416 -0.0635 0.3645  -0.0509 262 ALA A C   
2043 O O   . ALA A 262 ? 0.8390 0.3577 0.7456 -0.0677 0.3666  -0.0455 262 ALA A O   
2044 C CB  . ALA A 262 ? 0.8358 0.3720 0.7389 -0.0439 0.3625  -0.0484 262 ALA A CB  
2045 N N   . GLU A 263 ? 0.8324 0.3599 0.7398 -0.0698 0.3629  -0.0564 263 GLU A N   
2046 C CA  . GLU A 263 ? 0.8921 0.4136 0.7976 -0.0792 0.3631  -0.0563 263 GLU A CA  
2047 C C   . GLU A 263 ? 0.8314 0.3570 0.7375 -0.0844 0.3616  -0.0577 263 GLU A C   
2048 O O   . GLU A 263 ? 0.8270 0.3582 0.7377 -0.0826 0.3626  -0.0610 263 GLU A O   
2049 C CB  . GLU A 263 ? 0.8428 0.3581 0.7444 -0.0794 0.3656  -0.0604 263 GLU A CB  
2050 C CG  . GLU A 263 ? 0.8509 0.3588 0.7505 -0.0729 0.3693  -0.0581 263 GLU A CG  
2051 C CD  . GLU A 263 ? 0.8561 0.3560 0.7588 -0.0768 0.3719  -0.0533 263 GLU A CD  
2052 O OE1 . GLU A 263 ? 0.8536 0.3552 0.7602 -0.0852 0.3689  -0.0544 263 GLU A OE1 
2053 O OE2 . GLU A 263 ? 0.8831 0.3750 0.7851 -0.0706 0.3778  -0.0487 263 GLU A OE2 
2054 N N   . HIS A 264 ? 0.8347 0.3573 0.7370 -0.0898 0.3599  -0.0559 264 HIS A N   
2055 C CA  . HIS A 264 ? 0.8432 0.3665 0.7412 -0.0922 0.3597  -0.0551 264 HIS A CA  
2056 C C   . HIS A 264 ? 0.9001 0.4189 0.7910 -0.0931 0.3634  -0.0585 264 HIS A C   
2057 O O   . HIS A 264 ? 0.8544 0.3697 0.7356 -0.0940 0.3622  -0.0590 264 HIS A O   
2058 C CB  . HIS A 264 ? 0.8394 0.3634 0.7346 -0.0943 0.3549  -0.0526 264 HIS A CB  
2059 C CG  . HIS A 264 ? 0.8443 0.3685 0.7319 -0.0934 0.3547  -0.0501 264 HIS A CG  
2060 N ND1 . HIS A 264 ? 0.8514 0.3773 0.7326 -0.0927 0.3495  -0.0499 264 HIS A ND1 
2061 C CD2 . HIS A 264 ? 0.8457 0.3678 0.7315 -0.0920 0.3599  -0.0477 264 HIS A CD2 
2062 C CE1 . HIS A 264 ? 0.8585 0.3822 0.7302 -0.0891 0.3515  -0.0460 264 HIS A CE1 
2063 N NE2 . HIS A 264 ? 0.8554 0.3753 0.7306 -0.0895 0.3591  -0.0441 264 HIS A NE2 
2064 N N   . MET A 265 ? 0.8424 0.3627 0.7388 -0.0915 0.3679  -0.0621 265 MET A N   
2065 C CA  . MET A 265 ? 0.8641 0.3806 0.7562 -0.0920 0.3729  -0.0659 265 MET A CA  
2066 C C   . MET A 265 ? 0.8954 0.4138 0.7956 -0.0922 0.3805  -0.0683 265 MET A C   
2067 O O   . MET A 265 ? 0.9361 0.4620 0.8502 -0.0910 0.3806  -0.0717 265 MET A O   
2068 C CB  . MET A 265 ? 0.8500 0.3662 0.7439 -0.0898 0.3722  -0.0704 265 MET A CB  
2069 C CG  . MET A 265 ? 0.8535 0.3649 0.7430 -0.0904 0.3680  -0.0691 265 MET A CG  
2070 S SD  . MET A 265 ? 0.9452 0.4532 0.8363 -0.0857 0.3699  -0.0728 265 MET A SD  
2071 C CE  . MET A 265 ? 0.8760 0.3753 0.7662 -0.0887 0.3684  -0.0711 265 MET A CE  
2072 N N   . LEU A 266 ? 0.8859 0.3977 0.7785 -0.0932 0.3877  -0.0674 266 LEU A N   
2073 C CA  . LEU A 266 ? 0.8641 0.3761 0.7678 -0.0942 0.3984  -0.0711 266 LEU A CA  
2074 C C   . LEU A 266 ? 0.9086 0.4265 0.8215 -0.0933 0.3989  -0.0797 266 LEU A C   
2075 O O   . LEU A 266 ? 0.8670 0.3838 0.7713 -0.0914 0.3934  -0.0807 266 LEU A O   
2076 C CB  . LEU A 266 ? 0.8821 0.3827 0.7720 -0.0937 0.4086  -0.0656 266 LEU A CB  
2077 C CG  . LEU A 266 ? 0.8941 0.3894 0.7684 -0.0916 0.4096  -0.0666 266 LEU A CG  
2078 C CD1 . LEU A 266 ? 0.8966 0.3928 0.7824 -0.0927 0.4200  -0.0728 266 LEU A CD1 
2079 C CD2 . LEU A 266 ? 0.9139 0.3990 0.7641 -0.0869 0.4124  -0.0592 266 LEU A CD2 
2080 N N   . ILE A 267 ? 0.8629 0.3874 0.7953 -0.0942 0.4059  -0.0872 267 ILE A N   
2081 C CA  . ILE A 267 ? 0.8722 0.4043 0.8155 -0.0922 0.4071  -0.0971 267 ILE A CA  
2082 C C   . ILE A 267 ? 0.9048 0.4346 0.8597 -0.0957 0.4219  -0.1008 267 ILE A C   
2083 O O   . ILE A 267 ? 0.8666 0.3978 0.8385 -0.0990 0.4301  -0.1029 267 ILE A O   
2084 C CB  . ILE A 267 ? 0.8690 0.4168 0.8299 -0.0875 0.3996  -0.1067 267 ILE A CB  
2085 C CG1 . ILE A 267 ? 0.8374 0.3848 0.7859 -0.0830 0.3882  -0.1008 267 ILE A CG1 
2086 C CG2 . ILE A 267 ? 0.8427 0.3995 0.8130 -0.0831 0.3997  -0.1176 267 ILE A CG2 
2087 C CD1 . ILE A 267 ? 0.8287 0.3904 0.7900 -0.0757 0.3813  -0.1084 267 ILE A CD1 
2088 N N   . LEU A 268 ? 0.8732 0.3985 0.8203 -0.0950 0.4269  -0.1018 268 LEU A N   
2089 C CA  . LEU A 268 ? 0.9219 0.4443 0.8800 -0.0977 0.4431  -0.1050 268 LEU A CA  
2090 C C   . LEU A 268 ? 0.9609 0.4920 0.9280 -0.0954 0.4431  -0.1153 268 LEU A C   
2091 O O   . LEU A 268 ? 0.9559 0.4869 0.9081 -0.0912 0.4332  -0.1150 268 LEU A O   
2092 C CB  . LEU A 268 ? 0.9274 0.4316 0.8606 -0.0973 0.4531  -0.0928 268 LEU A CB  
2093 C CG  . LEU A 268 ? 0.9141 0.4111 0.8190 -0.0930 0.4467  -0.0885 268 LEU A CG  
2094 C CD1 . LEU A 268 ? 0.9214 0.4187 0.8289 -0.0918 0.4551  -0.0944 268 LEU A CD1 
2095 C CD2 . LEU A 268 ? 0.9305 0.4136 0.8081 -0.0896 0.4490  -0.0769 268 LEU A CD2 
2096 N N   . GLY A 269 ? 0.9711 0.5098 0.9647 -0.0980 0.4549  -0.1253 269 GLY A N   
2097 C CA  . GLY A 269 ? 0.9318 0.4788 0.9358 -0.0958 0.4578  -0.1355 269 GLY A CA  
2098 C C   . GLY A 269 ? 0.9036 0.4370 0.8997 -0.0982 0.4757  -0.1300 269 GLY A C   
2099 O O   . GLY A 269 ? 0.9154 0.4370 0.9115 -0.1019 0.4903  -0.1226 269 GLY A O   
2100 N N   . ILE A 270 ? 0.9346 0.4683 0.9223 -0.0946 0.4756  -0.1329 270 ILE A N   
2101 C CA  . ILE A 270 ? 0.9292 0.4496 0.9038 -0.0945 0.4916  -0.1271 270 ILE A CA  
2102 C C   . ILE A 270 ? 0.9293 0.4608 0.9217 -0.0930 0.4965  -0.1396 270 ILE A C   
2103 O O   . ILE A 270 ? 0.9182 0.4616 0.9133 -0.0886 0.4826  -0.1478 270 ILE A O   
2104 C CB  . ILE A 270 ? 0.9412 0.4460 0.8749 -0.0897 0.4847  -0.1148 270 ILE A CB  
2105 C CG1 . ILE A 270 ? 0.9653 0.4570 0.8824 -0.0867 0.5009  -0.1095 270 ILE A CG1 
2106 C CG2 . ILE A 270 ? 0.9309 0.4418 0.8553 -0.0859 0.4664  -0.1193 270 ILE A CG2 
2107 C CD1 . ILE A 270 ? 0.9846 0.4621 0.8620 -0.0805 0.4948  -0.0992 270 ILE A CD1 
2108 N N   . THR A 271 ? 0.9438 0.4706 0.9483 -0.0958 0.5178  -0.1404 271 THR A N   
2109 C CA  . THR A 271 ? 0.9715 0.5094 0.9971 -0.0951 0.5259  -0.1528 271 THR A CA  
2110 C C   . THR A 271 ? 1.0116 0.5322 1.0139 -0.0924 0.5421  -0.1433 271 THR A C   
2111 O O   . THR A 271 ? 0.9887 0.4910 0.9747 -0.0927 0.5568  -0.1302 271 THR A O   
2112 C CB  . THR A 271 ? 0.9397 0.4929 1.0140 -0.1017 0.5391  -0.1673 271 THR A CB  
2113 O OG1 . THR A 271 ? 0.9438 0.5154 1.0385 -0.1019 0.5221  -0.1781 271 THR A OG1 
2114 C CG2 . THR A 271 ? 0.9423 0.5089 1.0410 -0.1008 0.5480  -0.1814 271 THR A CG2 
2115 N N   . ASN A 272 ? 0.9724 0.4983 0.9711 -0.0879 0.5398  -0.1497 272 ASN A N   
2116 C CA  . ASN A 272 ? 1.0275 0.5387 1.0027 -0.0835 0.5536  -0.1424 272 ASN A CA  
2117 C C   . ASN A 272 ? 1.0310 0.5489 1.0378 -0.0864 0.5761  -0.1514 272 ASN A C   
2118 O O   . ASN A 272 ? 1.0196 0.5561 1.0693 -0.0919 0.5786  -0.1658 272 ASN A O   
2119 C CB  . ASN A 272 ? 1.1102 0.6206 1.0580 -0.0763 0.5367  -0.1433 272 ASN A CB  
2120 C CG  . ASN A 272 ? 1.0082 0.5383 0.9797 -0.0746 0.5270  -0.1590 272 ASN A CG  
2121 O OD1 . ASN A 272 ? 1.0470 0.5943 1.0562 -0.0780 0.5323  -0.1713 272 ASN A OD1 
2122 N ND2 . ASN A 272 ? 1.0977 0.6257 1.0477 -0.0684 0.5128  -0.1598 272 ASN A ND2 
2123 N N   . PRO A 273 ? 1.1002 0.6040 1.0881 -0.0820 0.5933  -0.1443 273 PRO A N   
2124 C CA  . PRO A 273 ? 1.0634 0.5739 1.0835 -0.0861 0.6106  -0.1491 273 PRO A CA  
2125 C C   . PRO A 273 ? 1.0814 0.6173 1.1316 -0.0864 0.6012  -0.1680 273 PRO A C   
2126 O O   . PRO A 273 ? 1.0302 0.5781 1.1182 -0.0917 0.6134  -0.1767 273 PRO A O   
2127 C CB  . PRO A 273 ? 1.1110 0.5996 1.0938 -0.0784 0.6228  -0.1337 273 PRO A CB  
2128 C CG  . PRO A 273 ? 1.0808 0.5509 1.0181 -0.0719 0.6161  -0.1196 273 PRO A CG  
2129 C CD  . PRO A 273 ? 1.0521 0.5346 0.9901 -0.0735 0.5930  -0.1289 273 PRO A CD  
2130 N N   . GLU A 274 ? 1.1579 0.7016 1.1933 -0.0803 0.5801  -0.1747 274 GLU A N   
2131 C CA  . GLU A 274 ? 1.1585 0.7257 1.2178 -0.0774 0.5690  -0.1914 274 GLU A CA  
2132 C C   . GLU A 274 ? 1.1122 0.7044 1.2110 -0.0804 0.5578  -0.2076 274 GLU A C   
2133 O O   . GLU A 274 ? 1.0613 0.6759 1.1806 -0.0756 0.5465  -0.2227 274 GLU A O   
2134 C CB  . GLU A 274 ? 1.1226 0.6838 1.1465 -0.0678 0.5518  -0.1902 274 GLU A CB  
2135 C CG  . GLU A 274 ? 1.1446 0.6841 1.1291 -0.0632 0.5593  -0.1776 274 GLU A CG  
2136 C CD  . GLU A 274 ? 1.2235 0.7664 1.2209 -0.0632 0.5759  -0.1788 274 GLU A CD  
2137 O OE1 . GLU A 274 ? 1.1678 0.7325 1.2051 -0.0660 0.5779  -0.1922 274 GLU A OE1 
2138 O OE2 . GLU A 274 ? 1.3679 0.8926 1.3358 -0.0594 0.5865  -0.1670 274 GLU A OE2 
2139 N N   . GLY A 275 ? 1.1075 0.6971 1.2163 -0.0864 0.5599  -0.2052 275 GLY A N   
2140 C CA  . GLY A 275 ? 1.1014 0.7149 1.2456 -0.0880 0.5479  -0.2211 275 GLY A CA  
2141 C C   . GLY A 275 ? 1.0993 0.7148 1.2219 -0.0807 0.5234  -0.2205 275 GLY A C   
2142 O O   . GLY A 275 ? 1.1026 0.7386 1.2504 -0.0789 0.5115  -0.2339 275 GLY A O   
2143 N N   . LYS A 276 ? 1.1034 0.6997 1.1814 -0.0762 0.5139  -0.2048 276 LYS A N   
2144 C CA  . LYS A 276 ? 1.0444 0.6406 1.1017 -0.0702 0.4914  -0.2010 276 LYS A CA  
2145 C C   . LYS A 276 ? 1.0573 0.6404 1.1010 -0.0760 0.4894  -0.1880 276 LYS A C   
2146 O O   . LYS A 276 ? 1.0833 0.6473 1.1081 -0.0806 0.5007  -0.1746 276 LYS A O   
2147 C CB  . LYS A 276 ? 1.0502 0.6334 1.0721 -0.0630 0.4829  -0.1935 276 LYS A CB  
2148 C CG  . LYS A 276 ? 1.1146 0.7033 1.1424 -0.0582 0.4900  -0.2021 276 LYS A CG  
2149 C CD  . LYS A 276 ? 1.0117 0.6282 1.0754 -0.0525 0.4856  -0.2220 276 LYS A CD  
2150 C CE  . LYS A 276 ? 1.0655 0.6866 1.1267 -0.0441 0.4862  -0.2294 276 LYS A CE  
2151 N NZ  . LYS A 276 ? 1.0611 0.6736 1.1212 -0.0497 0.5046  -0.2252 276 LYS A NZ  
2152 N N   . LYS A 277 ? 1.0185 0.6125 1.0705 -0.0740 0.4751  -0.1920 277 LYS A N   
2153 C CA  . LYS A 277 ? 0.9389 0.5236 0.9818 -0.0789 0.4721  -0.1815 277 LYS A CA  
2154 C C   . LYS A 277 ? 0.9498 0.5307 0.9681 -0.0725 0.4529  -0.1748 277 LYS A C   
2155 O O   . LYS A 277 ? 0.9401 0.5337 0.9628 -0.0635 0.4408  -0.1833 277 LYS A O   
2156 C CB  . LYS A 277 ? 0.8908 0.4918 0.9716 -0.0836 0.4759  -0.1931 277 LYS A CB  
2157 C CG  . LYS A 277 ? 0.8861 0.4786 0.9593 -0.0879 0.4725  -0.1833 277 LYS A CG  
2158 C CD  . LYS A 277 ? 0.8767 0.4867 0.9903 -0.0920 0.4755  -0.1978 277 LYS A CD  
2159 C CE  . LYS A 277 ? 0.9380 0.5390 1.0440 -0.0960 0.4726  -0.1880 277 LYS A CE  
2160 N NZ  . LYS A 277 ? 0.8923 0.5086 1.0397 -0.1009 0.4778  -0.2030 277 LYS A NZ  
2161 N N   . LYS A 278 ? 0.8976 0.4608 0.8903 -0.0760 0.4510  -0.1598 278 LYS A N   
2162 C CA  . LYS A 278 ? 0.9444 0.5019 0.9161 -0.0717 0.4357  -0.1527 278 LYS A CA  
2163 C C   . LYS A 278 ? 0.9396 0.4924 0.9084 -0.0767 0.4335  -0.1444 278 LYS A C   
2164 O O   . LYS A 278 ? 0.8940 0.4404 0.8654 -0.0832 0.4443  -0.1397 278 LYS A O   
2165 C CB  . LYS A 278 ? 0.9046 0.4454 0.8467 -0.0700 0.4337  -0.1444 278 LYS A CB  
2166 C CG  . LYS A 278 ? 0.9280 0.4718 0.8703 -0.0639 0.4346  -0.1520 278 LYS A CG  
2167 C CD  . LYS A 278 ? 0.9450 0.4723 0.8601 -0.0623 0.4316  -0.1455 278 LYS A CD  
2168 C CE  . LYS A 278 ? 0.9542 0.4840 0.8697 -0.0552 0.4318  -0.1532 278 LYS A CE  
2169 N NZ  . LYS A 278 ? 0.9203 0.4636 0.8495 -0.0465 0.4239  -0.1606 278 LYS A NZ  
2170 N N   . TYR A 279 ? 0.9606 0.5154 0.9230 -0.0725 0.4206  -0.1420 279 TYR A N   
2171 C CA  . TYR A 279 ? 0.8729 0.4244 0.8321 -0.0760 0.4167  -0.1346 279 TYR A CA  
2172 C C   . TYR A 279 ? 0.8777 0.4137 0.8101 -0.0765 0.4106  -0.1226 279 TYR A C   
2173 O O   . TYR A 279 ? 0.8911 0.4237 0.8130 -0.0713 0.4040  -0.1220 279 TYR A O   
2174 C CB  . TYR A 279 ? 0.8705 0.4375 0.8450 -0.0700 0.4074  -0.1419 279 TYR A CB  
2175 C CG  . TYR A 279 ? 0.9353 0.5196 0.9417 -0.0715 0.4127  -0.1556 279 TYR A CG  
2176 C CD1 . TYR A 279 ? 0.8523 0.4359 0.8717 -0.0793 0.4192  -0.1544 279 TYR A CD1 
2177 C CD2 . TYR A 279 ? 0.8831 0.4848 0.9089 -0.0649 0.4114  -0.1712 279 TYR A CD2 
2178 C CE1 . TYR A 279 ? 0.8480 0.4472 0.9017 -0.0819 0.4254  -0.1690 279 TYR A CE1 
2179 C CE2 . TYR A 279 ? 0.9064 0.5266 0.9671 -0.0669 0.4161  -0.1872 279 TYR A CE2 
2180 C CZ  . TYR A 279 ? 0.8954 0.5138 0.9713 -0.0761 0.4236  -0.1864 279 TYR A CZ  
2181 O OH  . TYR A 279 ? 0.8934 0.5297 1.0087 -0.0792 0.4297  -0.2042 279 TYR A OH  
2182 N N   . LEU A 280 ? 0.8818 0.4087 0.8048 -0.0822 0.4136  -0.1140 280 LEU A N   
2183 C CA  . LEU A 280 ? 0.8858 0.4013 0.7876 -0.0830 0.4074  -0.1053 280 LEU A CA  
2184 C C   . LEU A 280 ? 0.8776 0.3942 0.7809 -0.0850 0.4024  -0.0996 280 LEU A C   
2185 O O   . LEU A 280 ? 0.8911 0.4146 0.8090 -0.0866 0.4055  -0.1012 280 LEU A O   
2186 C CB  . LEU A 280 ? 0.9013 0.4057 0.7859 -0.0848 0.4139  -0.1009 280 LEU A CB  
2187 C CG  . LEU A 280 ? 0.9195 0.4222 0.8019 -0.0827 0.4211  -0.1062 280 LEU A CG  
2188 C CD1 . LEU A 280 ? 0.9679 0.4594 0.8294 -0.0818 0.4274  -0.1013 280 LEU A CD1 
2189 C CD2 . LEU A 280 ? 0.9103 0.4132 0.7902 -0.0790 0.4135  -0.1110 280 LEU A CD2 
2190 N N   . ALA A 281 ? 0.8788 0.3890 0.7691 -0.0853 0.3950  -0.0941 281 ALA A N   
2191 C CA  . ALA A 281 ? 0.8724 0.3831 0.7626 -0.0871 0.3901  -0.0883 281 ALA A CA  
2192 C C   . ALA A 281 ? 0.8814 0.3839 0.7555 -0.0891 0.3869  -0.0836 281 ALA A C   
2193 O O   . ALA A 281 ? 0.8884 0.3859 0.7548 -0.0885 0.3840  -0.0860 281 ALA A O   
2194 C CB  . ALA A 281 ? 0.8634 0.3786 0.7597 -0.0834 0.3834  -0.0884 281 ALA A CB  
2195 N N   . ALA A 282 ? 0.8827 0.3843 0.7527 -0.0905 0.3871  -0.0783 282 ALA A N   
2196 C CA  . ALA A 282 ? 0.8928 0.3898 0.7476 -0.0901 0.3827  -0.0757 282 ALA A CA  
2197 C C   . ALA A 282 ? 0.8848 0.3854 0.7434 -0.0914 0.3764  -0.0714 282 ALA A C   
2198 O O   . ALA A 282 ? 0.8777 0.3812 0.7436 -0.0918 0.3790  -0.0678 282 ALA A O   
2199 C CB  . ALA A 282 ? 0.9090 0.4003 0.7491 -0.0870 0.3900  -0.0727 282 ALA A CB  
2200 N N   . ALA A 283 ? 0.8865 0.3874 0.7426 -0.0922 0.3686  -0.0732 283 ALA A N   
2201 C CA  . ALA A 283 ? 0.8809 0.3860 0.7409 -0.0933 0.3626  -0.0702 283 ALA A CA  
2202 C C   . ALA A 283 ? 0.8941 0.3998 0.7407 -0.0903 0.3578  -0.0715 283 ALA A C   
2203 O O   . ALA A 283 ? 0.9024 0.4086 0.7458 -0.0901 0.3526  -0.0787 283 ALA A O   
2204 C CB  . ALA A 283 ? 0.8738 0.3799 0.7459 -0.0961 0.3590  -0.0722 283 ALA A CB  
2205 N N   . PHE A 284 ? 0.8983 0.4040 0.7367 -0.0868 0.3596  -0.0656 284 PHE A N   
2206 C CA  . PHE A 284 ? 0.9128 0.4203 0.7361 -0.0805 0.3542  -0.0660 284 PHE A CA  
2207 C C   . PHE A 284 ? 0.9257 0.4390 0.7550 -0.0804 0.3494  -0.0619 284 PHE A C   
2208 O O   . PHE A 284 ? 0.8987 0.4116 0.7387 -0.0838 0.3536  -0.0563 284 PHE A O   
2209 C CB  . PHE A 284 ? 0.9318 0.4311 0.7342 -0.0725 0.3626  -0.0608 284 PHE A CB  
2210 C CG  . PHE A 284 ? 0.9397 0.4330 0.7363 -0.0721 0.3697  -0.0636 284 PHE A CG  
2211 C CD1 . PHE A 284 ? 0.9363 0.4321 0.7389 -0.0757 0.3645  -0.0726 284 PHE A CD1 
2212 C CD2 . PHE A 284 ? 1.0056 0.4894 0.7917 -0.0680 0.3831  -0.0573 284 PHE A CD2 
2213 C CE1 . PHE A 284 ? 0.9440 0.4345 0.7410 -0.0747 0.3709  -0.0754 284 PHE A CE1 
2214 C CE2 . PHE A 284 ? 0.9604 0.4392 0.7422 -0.0674 0.3906  -0.0601 284 PHE A CE2 
2215 C CZ  . PHE A 284 ? 0.9556 0.4383 0.7421 -0.0705 0.3836  -0.0693 284 PHE A CZ  
2216 N N   . PRO A 285 ? 0.9825 0.5028 0.8061 -0.0759 0.3401  -0.0660 285 PRO A N   
2217 C CA  . PRO A 285 ? 0.9850 0.5110 0.8120 -0.0740 0.3360  -0.0618 285 PRO A CA  
2218 C C   . PRO A 285 ? 1.0681 0.5858 0.8814 -0.0679 0.3446  -0.0510 285 PRO A C   
2219 O O   . PRO A 285 ? 1.0917 0.5994 0.8912 -0.0639 0.3538  -0.0472 285 PRO A O   
2220 C CB  . PRO A 285 ? 0.9764 0.5131 0.7980 -0.0679 0.3239  -0.0711 285 PRO A CB  
2221 C CG  . PRO A 285 ? 1.0035 0.5416 0.8296 -0.0712 0.3208  -0.0824 285 PRO A CG  
2222 C CD  . PRO A 285 ? 0.9687 0.4943 0.7856 -0.0721 0.3316  -0.0771 285 PRO A CD  
2223 N N   . SER A 286 ? 1.0366 0.5574 0.8552 -0.0673 0.3431  -0.0459 286 SER A N   
2224 C CA  . SER A 286 ? 0.9537 0.4650 0.7620 -0.0618 0.3525  -0.0357 286 SER A CA  
2225 C C   . SER A 286 ? 1.0243 0.5291 0.8043 -0.0482 0.3545  -0.0326 286 SER A C   
2226 O O   . SER A 286 ? 1.0219 0.5353 0.7909 -0.0406 0.3434  -0.0389 286 SER A O   
2227 C CB  . SER A 286 ? 1.0452 0.5619 0.8633 -0.0623 0.3490  -0.0319 286 SER A CB  
2228 O OG  . SER A 286 ? 1.0611 0.5816 0.9015 -0.0721 0.3495  -0.0331 286 SER A OG  
2229 N N   . ALA A 287 ? 1.0834 0.5729 0.8522 -0.0440 0.3695  -0.0234 287 ALA A N   
2230 C CA  . ALA A 287 ? 1.0469 0.5256 0.7848 -0.0286 0.3759  -0.0173 287 ALA A CA  
2231 C C   . ALA A 287 ? 1.0702 0.5516 0.7933 -0.0235 0.3712  -0.0248 287 ALA A C   
2232 O O   . ALA A 287 ? 1.1632 0.6444 0.8592 -0.0078 0.3671  -0.0250 287 ALA A O   
2233 C CB  . ALA A 287 ? 1.1543 0.6368 0.8764 -0.0155 0.3682  -0.0139 287 ALA A CB  
2234 N N   . CYS A 288 ? 1.0609 0.5452 0.8004 -0.0352 0.3713  -0.0318 288 CYS A N   
2235 C CA  . CYS A 288 ? 1.0159 0.5025 0.7444 -0.0318 0.3670  -0.0401 288 CYS A CA  
2236 C C   . CYS A 288 ? 1.0059 0.4809 0.7340 -0.0354 0.3818  -0.0374 288 CYS A C   
2237 O O   . CYS A 288 ? 1.0157 0.4923 0.7369 -0.0339 0.3791  -0.0447 288 CYS A O   
2238 C CB  . CYS A 288 ? 1.0566 0.5587 0.8053 -0.0412 0.3516  -0.0535 288 CYS A CB  
2239 S SG  . CYS A 288 ? 1.1500 0.6691 0.8970 -0.0338 0.3328  -0.0626 288 CYS A SG  
2240 N N   . GLY A 289 ? 1.0464 0.5109 0.7843 -0.0403 0.3974  -0.0289 289 GLY A N   
2241 C CA  . GLY A 289 ? 1.0123 0.4653 0.7484 -0.0411 0.4141  -0.0261 289 GLY A CA  
2242 C C   . GLY A 289 ? 0.9884 0.4439 0.7552 -0.0554 0.4202  -0.0300 289 GLY A C   
2243 O O   . GLY A 289 ? 0.9951 0.4438 0.7647 -0.0569 0.4334  -0.0301 289 GLY A O   
2244 N N   . LYS A 290 ? 0.9624 0.4284 0.7520 -0.0645 0.4110  -0.0340 290 LYS A N   
2245 C CA  . LYS A 290 ? 0.9424 0.4134 0.7590 -0.0749 0.4144  -0.0396 290 LYS A CA  
2246 C C   . LYS A 290 ? 1.0488 0.5108 0.8767 -0.0768 0.4332  -0.0362 290 LYS A C   
2247 O O   . LYS A 290 ? 0.9472 0.4091 0.7869 -0.0806 0.4419  -0.0411 290 LYS A O   
2248 C CB  . LYS A 290 ? 0.9178 0.4002 0.7527 -0.0809 0.4027  -0.0429 290 LYS A CB  
2249 C CG  . LYS A 290 ? 0.9249 0.4157 0.7564 -0.0813 0.3873  -0.0478 290 LYS A CG  
2250 C CD  . LYS A 290 ? 0.9204 0.4205 0.7717 -0.0871 0.3800  -0.0508 290 LYS A CD  
2251 C CE  . LYS A 290 ? 0.9222 0.4241 0.7796 -0.0869 0.3797  -0.0457 290 LYS A CE  
2252 N NZ  . LYS A 290 ? 0.8923 0.3939 0.7351 -0.0818 0.3737  -0.0415 290 LYS A NZ  
2253 N N   . THR A 291 ? 1.0305 0.4848 0.8571 -0.0742 0.4408  -0.0285 291 THR A N   
2254 C CA  . THR A 291 ? 0.9639 0.4087 0.8072 -0.0774 0.4605  -0.0264 291 THR A CA  
2255 C C   . THR A 291 ? 1.0539 0.4843 0.8839 -0.0724 0.4788  -0.0218 291 THR A C   
2256 O O   . THR A 291 ? 1.0317 0.4609 0.8830 -0.0785 0.4924  -0.0268 291 THR A O   
2257 C CB  . THR A 291 ? 1.0054 0.4421 0.8480 -0.0747 0.4658  -0.0183 291 THR A CB  
2258 O OG1 . THR A 291 ? 1.0442 0.4950 0.9037 -0.0802 0.4510  -0.0238 291 THR A OG1 
2259 C CG2 . THR A 291 ? 1.0572 0.4807 0.9180 -0.0779 0.4896  -0.0162 291 THR A CG2 
2260 N N   . ASN A 292 ? 1.1145 0.5346 0.9095 -0.0601 0.4796  -0.0129 292 ASN A N   
2261 C CA  . ASN A 292 ? 1.0811 0.4866 0.8588 -0.0527 0.4976  -0.0074 292 ASN A CA  
2262 C C   . ASN A 292 ? 1.0648 0.4790 0.8522 -0.0584 0.4952  -0.0176 292 ASN A C   
2263 O O   . ASN A 292 ? 1.1022 0.5067 0.8905 -0.0574 0.5138  -0.0159 292 ASN A O   
2264 C CB  . ASN A 292 ? 1.1287 0.5250 0.8631 -0.0351 0.4947  0.0020  292 ASN A CB  
2265 C CG  . ASN A 292 ? 1.3564 0.7381 1.0767 -0.0256 0.5045  0.0149  292 ASN A CG  
2266 O OD1 . ASN A 292 ? 1.3544 0.7150 1.0632 -0.0178 0.5286  0.0263  292 ASN A OD1 
2267 N ND2 . ASN A 292 ? 1.1595 0.5512 0.8809 -0.0257 0.4874  0.0138  292 ASN A ND2 
2268 N N   . LEU A 293 ? 1.0961 0.5274 0.8914 -0.0640 0.4742  -0.0277 293 LEU A N   
2269 C CA  . LEU A 293 ? 1.0398 0.4788 0.8440 -0.0685 0.4714  -0.0373 293 LEU A CA  
2270 C C   . LEU A 293 ? 1.0089 0.4566 0.8506 -0.0797 0.4769  -0.0460 293 LEU A C   
2271 O O   . LEU A 293 ? 1.0452 0.4932 0.8975 -0.0819 0.4871  -0.0511 293 LEU A O   
2272 C CB  . LEU A 293 ? 0.9855 0.4365 0.7821 -0.0685 0.4490  -0.0442 293 LEU A CB  
2273 C CG  . LEU A 293 ? 0.9767 0.4344 0.7813 -0.0722 0.4451  -0.0539 293 LEU A CG  
2274 C CD1 . LEU A 293 ? 1.0021 0.4505 0.7845 -0.0642 0.4546  -0.0523 293 LEU A CD1 
2275 C CD2 . LEU A 293 ? 0.9604 0.4286 0.7665 -0.0747 0.4254  -0.0607 293 LEU A CD2 
2276 N N   . ALA A 294 ? 0.9580 0.4144 0.8204 -0.0856 0.4697  -0.0491 294 ALA A N   
2277 C CA  . ALA A 294 ? 0.9392 0.4072 0.8371 -0.0938 0.4722  -0.0602 294 ALA A CA  
2278 C C   . ALA A 294 ? 1.0422 0.5023 0.9602 -0.0970 0.4955  -0.0606 294 ALA A C   
2279 O O   . ALA A 294 ? 1.0453 0.5163 0.9942 -0.1029 0.4999  -0.0728 294 ALA A O   
2280 C CB  . ALA A 294 ? 0.9179 0.3972 0.8301 -0.0970 0.4587  -0.0635 294 ALA A CB  
2281 N N   . MET A 295 ? 1.0175 0.4589 0.9197 -0.0924 0.5112  -0.0482 295 MET A N   
2282 C CA  . MET A 295 ? 1.0721 0.5009 0.9922 -0.0950 0.5380  -0.0465 295 MET A CA  
2283 C C   . MET A 295 ? 1.0852 0.4958 0.9778 -0.0865 0.5553  -0.0359 295 MET A C   
2284 O O   . MET A 295 ? 1.0511 0.4460 0.9433 -0.0813 0.5749  -0.0286 295 MET A O   
2285 C CB  . MET A 295 ? 1.0855 0.5053 1.0122 -0.0944 0.5456  -0.0401 295 MET A CB  
2286 C CG  . MET A 295 ? 1.0280 0.4640 0.9802 -0.1016 0.5309  -0.0498 295 MET A CG  
2287 S SD  . MET A 295 ? 1.0503 0.4795 1.0080 -0.0966 0.5380  -0.0433 295 MET A SD  
2288 C CE  . MET A 295 ? 1.0070 0.4565 0.9875 -0.1044 0.5172  -0.0545 295 MET A CE  
2289 N N   A MET A 296 ? 1.0732 0.4884 0.9426 -0.0813 0.5435  -0.0369 296 MET A N   
2290 N N   B MET A 296 ? 1.0773 0.4927 0.9471 -0.0814 0.5434  -0.0371 296 MET A N   
2291 C CA  A MET A 296 ? 1.1002 0.4991 0.9370 -0.0702 0.5567  -0.0269 296 MET A CA  
2292 C CA  B MET A 296 ? 1.1010 0.5005 0.9390 -0.0707 0.5566  -0.0275 296 MET A CA  
2293 C C   A MET A 296 ? 1.0753 0.4647 0.9317 -0.0734 0.5850  -0.0276 296 MET A C   
2294 C C   B MET A 296 ? 1.0752 0.4644 0.9332 -0.0738 0.5858  -0.0276 296 MET A C   
2295 O O   A MET A 296 ? 1.0563 0.4593 0.9506 -0.0843 0.5871  -0.0412 296 MET A O   
2296 O O   B MET A 296 ? 1.0676 0.4701 0.9654 -0.0846 0.5883  -0.0412 296 MET A O   
2297 C CB  A MET A 296 ? 1.0935 0.5019 0.9082 -0.0656 0.5375  -0.0318 296 MET A CB  
2298 C CB  B MET A 296 ? 1.0981 0.5081 0.9177 -0.0672 0.5382  -0.0336 296 MET A CB  
2299 C CG  A MET A 296 ? 1.1085 0.5023 0.8861 -0.0519 0.5479  -0.0233 296 MET A CG  
2300 C CG  B MET A 296 ? 1.1049 0.5034 0.9019 -0.0582 0.5526  -0.0294 296 MET A CG  
2301 S SD  A MET A 296 ? 1.0805 0.4869 0.8412 -0.0488 0.5269  -0.0335 296 MET A SD  
2302 S SD  B MET A 296 ? 1.0686 0.4819 0.8571 -0.0578 0.5323  -0.0412 296 MET A SD  
2303 C CE  A MET A 296 ? 1.0808 0.5023 0.8857 -0.0635 0.5286  -0.0480 296 MET A CE  
2304 C CE  B MET A 296 ? 1.0675 0.4869 0.8305 -0.0522 0.5044  -0.0404 296 MET A CE  
2305 N N   . ASN A 297 ? 1.1120 0.4805 0.9439 -0.0604 0.6009  -0.0146 297 ASN A N   
2306 C CA  . ASN A 297 ? 1.1477 0.5068 0.9942 -0.0580 0.6200  -0.0152 297 ASN A CA  
2307 C C   . ASN A 297 ? 1.1496 0.5050 0.9633 -0.0495 0.6212  -0.0117 297 ASN A C   
2308 O O   . ASN A 297 ? 1.1816 0.5209 0.9517 -0.0333 0.6250  0.0021  297 ASN A O   
2309 C CB  . ASN A 297 ? 1.2144 0.5503 1.0545 -0.0469 0.6375  -0.0023 297 ASN A CB  
2310 C CG  . ASN A 297 ? 1.3298 0.6539 1.1887 -0.0450 0.6597  -0.0030 297 ASN A CG  
2311 O OD1 . ASN A 297 ? 1.3812 0.7191 1.2793 -0.0572 0.6628  -0.0182 297 ASN A OD1 
2312 N ND2 . ASN A 297 ? 1.4255 0.7236 1.2561 -0.0287 0.6761  0.0134  297 ASN A ND2 
2313 N N   . PRO A 298 ? 1.1305 0.5014 0.9617 -0.0579 0.6175  -0.0246 298 PRO A N   
2314 C CA  . PRO A 298 ? 1.1686 0.5390 0.9667 -0.0492 0.6149  -0.0237 298 PRO A CA  
2315 C C   . PRO A 298 ? 1.1826 0.5340 0.9641 -0.0369 0.6330  -0.0134 298 PRO A C   
2316 O O   . PRO A 298 ? 1.2393 0.5817 1.0482 -0.0396 0.6498  -0.0120 298 PRO A O   
2317 C CB  . PRO A 298 ? 1.1434 0.5360 0.9724 -0.0615 0.6054  -0.0416 298 PRO A CB  
2318 C CG  . PRO A 298 ? 1.1880 0.5881 1.0680 -0.0745 0.6146  -0.0502 298 PRO A CG  
2319 C CD  . PRO A 298 ? 1.1257 0.5167 1.0069 -0.0740 0.6148  -0.0420 298 PRO A CD  
2320 N N   . THR A 299 ? 1.3316 0.6769 1.0678 -0.0223 0.6298  -0.0074 299 THR A N   
2321 C CA  . THR A 299 ? 1.2464 0.5740 0.9589 -0.0074 0.6454  0.0034  299 THR A CA  
2322 C C   . THR A 299 ? 1.2631 0.5992 0.9851 -0.0106 0.6477  -0.0060 299 THR A C   
2323 O O   . THR A 299 ? 1.3693 0.6918 1.0798 -0.0006 0.6629  0.0020  299 THR A O   
2324 C CB  . THR A 299 ? 1.2792 0.5955 0.9326 0.0147  0.6404  0.0151  299 THR A CB  
2325 O OG1 . THR A 299 ? 1.2636 0.5955 0.8962 0.0160  0.6211  0.0031  299 THR A OG1 
2326 C CG2 . THR A 299 ? 1.2853 0.5929 0.9273 0.0198  0.6387  0.0251  299 THR A CG2 
2327 N N   . LEU A 300 ? 1.2501 0.6074 0.9914 -0.0228 0.6336  -0.0222 300 LEU A N   
2328 C CA  . LEU A 300 ? 1.2033 0.5697 0.9560 -0.0256 0.6352  -0.0321 300 LEU A CA  
2329 C C   . LEU A 300 ? 1.2378 0.6098 1.0435 -0.0395 0.6486  -0.0390 300 LEU A C   
2330 O O   . LEU A 300 ? 1.2464 0.6311 1.0886 -0.0529 0.6439  -0.0484 300 LEU A O   
2331 C CB  . LEU A 300 ? 1.1738 0.5587 0.9245 -0.0303 0.6146  -0.0476 300 LEU A CB  
2332 C CG  . LEU A 300 ? 1.1971 0.5810 0.9045 -0.0183 0.5929  -0.0463 300 LEU A CG  
2333 C CD1 . LEU A 300 ? 1.1492 0.5521 0.8692 -0.0262 0.5645  -0.0614 300 LEU A CD1 
2334 C CD2 . LEU A 300 ? 1.2227 0.5928 0.8871 0.0002  0.6037  -0.0396 300 LEU A CD2 
2335 N N   . PRO A 301 ? 1.2145 0.5784 1.0266 -0.0360 0.6652  -0.0361 301 PRO A N   
2336 C CA  . PRO A 301 ? 1.2047 0.5752 1.0706 -0.0492 0.6786  -0.0457 301 PRO A CA  
2337 C C   . PRO A 301 ? 1.2109 0.6094 1.1097 -0.0618 0.6656  -0.0660 301 PRO A C   
2338 O O   . PRO A 301 ? 1.1906 0.5990 1.0688 -0.0582 0.6513  -0.0714 301 PRO A O   
2339 C CB  . PRO A 301 ? 1.2428 0.5972 1.0995 -0.0400 0.6985  -0.0370 301 PRO A CB  
2340 C CG  . PRO A 301 ? 1.2598 0.6101 1.0628 -0.0246 0.6893  -0.0300 301 PRO A CG  
2341 C CD  . PRO A 301 ? 1.2716 0.6209 1.0426 -0.0191 0.6727  -0.0252 301 PRO A CD  
2342 N N   . GLY A 302 ? 1.1465 0.5578 1.0976 -0.0753 0.6707  -0.0786 302 GLY A N   
2343 C CA  . GLY A 302 ? 1.1190 0.5590 1.1038 -0.0851 0.6583  -0.0989 302 GLY A CA  
2344 C C   . GLY A 302 ? 1.1412 0.5950 1.1203 -0.0874 0.6371  -0.1052 302 GLY A C   
2345 O O   . GLY A 302 ? 1.1225 0.5984 1.1205 -0.0908 0.6239  -0.1214 302 GLY A O   
2346 N N   . TRP A 303 ? 1.1683 0.6090 1.1208 -0.0840 0.6329  -0.0932 303 TRP A N   
2347 C CA  . TRP A 303 ? 1.1245 0.5759 1.0714 -0.0861 0.6135  -0.0979 303 TRP A CA  
2348 C C   . TRP A 303 ? 1.1402 0.5923 1.1137 -0.0940 0.6181  -0.0980 303 TRP A C   
2349 O O   . TRP A 303 ? 1.1283 0.5620 1.0997 -0.0925 0.6315  -0.0863 303 TRP A O   
2350 C CB  . TRP A 303 ? 1.0968 0.5356 0.9918 -0.0757 0.5983  -0.0851 303 TRP A CB  
2351 C CG  . TRP A 303 ? 1.1040 0.5464 0.9764 -0.0691 0.5858  -0.0893 303 TRP A CG  
2352 C CD1 . TRP A 303 ? 1.1700 0.6010 1.0172 -0.0600 0.5985  -0.0844 303 TRP A CD1 
2353 C CD2 . TRP A 303 ? 1.0895 0.5467 0.9623 -0.0703 0.5595  -0.0993 303 TRP A CD2 
2354 N NE1 . TRP A 303 ? 1.1060 0.5447 0.9395 -0.0563 0.5804  -0.0920 303 TRP A NE1 
2355 C CE2 . TRP A 303 ? 1.0893 0.5430 0.9388 -0.0628 0.5573  -0.1007 303 TRP A CE2 
2356 C CE3 . TRP A 303 ? 1.0191 0.4905 0.9089 -0.0760 0.5389  -0.1066 303 TRP A CE3 
2357 C CZ2 . TRP A 303 ? 1.0752 0.5381 0.9200 -0.0618 0.5361  -0.1093 303 TRP A CZ2 
2358 C CZ3 . TRP A 303 ? 1.0319 0.5116 0.9148 -0.0739 0.5191  -0.1136 303 TRP A CZ3 
2359 C CH2 . TRP A 303 ? 1.0409 0.5157 0.9026 -0.0675 0.5182  -0.1150 303 TRP A CH2 
2360 N N   . LYS A 304 ? 1.0677 0.5403 1.0654 -0.1000 0.5974  -0.1105 304 LYS A N   
2361 C CA  . LYS A 304 ? 1.0066 0.4834 1.0317 -0.1072 0.5983  -0.1137 304 LYS A CA  
2362 C C   . LYS A 304 ? 1.0804 0.5647 1.0896 -0.1055 0.5698  -0.1127 304 LYS A C   
2363 O O   . LYS A 304 ? 1.0330 0.5332 1.0421 -0.1039 0.5489  -0.1217 304 LYS A O   
2364 C CB  . LYS A 304 ? 0.9912 0.4896 1.0728 -0.1160 0.6047  -0.1348 304 LYS A CB  
2365 C CG  . LYS A 304 ? 1.1060 0.6102 1.2199 -0.1234 0.6060  -0.1412 304 LYS A CG  
2366 C CD  . LYS A 304 ? 1.1460 0.6739 1.3195 -0.1313 0.6129  -0.1656 304 LYS A CD  
2367 C CE  . LYS A 304 ? 1.1965 0.7303 1.4038 -0.1385 0.6144  -0.1740 304 LYS A CE  
2368 N NZ  . LYS A 304 ? 1.1528 0.7132 1.4220 -0.1462 0.6188  -0.2007 304 LYS A NZ  
2369 N N   . VAL A 305 ? 1.0887 0.5607 1.0844 -0.1052 0.5705  -0.1011 305 VAL A N   
2370 C CA  . VAL A 305 ? 1.0487 0.5270 1.0328 -0.1044 0.5466  -0.0995 305 VAL A CA  
2371 C C   . VAL A 305 ? 1.0460 0.5336 1.0659 -0.1116 0.5480  -0.1077 305 VAL A C   
2372 O O   . VAL A 305 ? 1.1212 0.5978 1.1572 -0.1155 0.5693  -0.1046 305 VAL A O   
2373 C CB  . VAL A 305 ? 1.1483 0.6079 1.0884 -0.0971 0.5432  -0.0817 305 VAL A CB  
2374 C CG1 . VAL A 305 ? 1.0626 0.5290 0.9984 -0.0978 0.5224  -0.0807 305 VAL A CG1 
2375 C CG2 . VAL A 305 ? 1.0422 0.4969 0.9483 -0.0892 0.5369  -0.0777 305 VAL A CG2 
2376 N N   . GLU A 306 ? 1.0486 0.5554 1.0808 -0.1124 0.5265  -0.1183 306 GLU A N   
2377 C CA  . GLU A 306 ? 0.9964 0.5150 1.0600 -0.1172 0.5234  -0.1280 306 GLU A CA  
2378 C C   . GLU A 306 ? 0.9261 0.4468 0.9688 -0.1137 0.5017  -0.1219 306 GLU A C   
2379 O O   . GLU A 306 ? 0.9380 0.4593 0.9540 -0.1085 0.4862  -0.1171 306 GLU A O   
2380 C CB  . GLU A 306 ? 0.9743 0.5186 1.0794 -0.1195 0.5195  -0.1509 306 GLU A CB  
2381 C CG  . GLU A 306 ? 0.9640 0.5086 1.0998 -0.1248 0.5431  -0.1598 306 GLU A CG  
2382 C CD  . GLU A 306 ? 1.0065 0.5783 1.1748 -0.1238 0.5357  -0.1825 306 GLU A CD  
2383 O OE1 . GLU A 306 ? 1.0759 0.6552 1.2241 -0.1166 0.5196  -0.1832 306 GLU A OE1 
2384 O OE2 . GLU A 306 ? 1.0505 0.6367 1.2658 -0.1297 0.5463  -0.2006 306 GLU A OE2 
2385 N N   . CYS A 307 ? 0.9009 0.4221 0.9577 -0.1168 0.5023  -0.1224 307 CYS A N   
2386 C CA  . CYS A 307 ? 0.9203 0.4401 0.9570 -0.1138 0.4862  -0.1142 307 CYS A CA  
2387 C C   . CYS A 307 ? 0.9330 0.4748 0.9929 -0.1130 0.4704  -0.1288 307 CYS A C   
2388 O O   . CYS A 307 ? 0.8667 0.4188 0.9617 -0.1170 0.4765  -0.1422 307 CYS A O   
2389 C CB  . CYS A 307 ? 1.0153 0.5169 1.0445 -0.1154 0.4985  -0.1015 307 CYS A CB  
2390 S SG  . CYS A 307 ? 0.8957 0.3973 0.9051 -0.1121 0.4800  -0.0928 307 CYS A SG  
2391 N N   . VAL A 308 ? 0.9219 0.4705 0.9627 -0.1071 0.4512  -0.1269 308 VAL A N   
2392 C CA  . VAL A 308 ? 0.8673 0.4346 0.9214 -0.1026 0.4357  -0.1378 308 VAL A CA  
2393 C C   . VAL A 308 ? 0.8401 0.4014 0.8806 -0.1020 0.4286  -0.1276 308 VAL A C   
2394 O O   . VAL A 308 ? 0.8413 0.4144 0.8985 -0.1004 0.4223  -0.1360 308 VAL A O   
2395 C CB  . VAL A 308 ? 0.9240 0.5009 0.9660 -0.0945 0.4217  -0.1414 308 VAL A CB  
2396 C CG1 . VAL A 308 ? 0.8959 0.4902 0.9461 -0.0864 0.4067  -0.1507 308 VAL A CG1 
2397 C CG2 . VAL A 308 ? 0.8579 0.4420 0.9143 -0.0944 0.4284  -0.1523 308 VAL A CG2 
2398 N N   . GLY A 309 ? 0.8593 0.4037 0.8701 -0.1025 0.4290  -0.1110 309 GLY A N   
2399 C CA  . GLY A 309 ? 0.8458 0.3847 0.8430 -0.1017 0.4226  -0.1010 309 GLY A CA  
2400 C C   . GLY A 309 ? 0.8580 0.3802 0.8250 -0.1014 0.4245  -0.0857 309 GLY A C   
2401 O O   . GLY A 309 ? 0.9451 0.4612 0.8987 -0.1007 0.4277  -0.0833 309 GLY A O   
2402 N N   . ASP A 310 ? 0.8594 0.3755 0.8154 -0.1007 0.4215  -0.0767 310 ASP A N   
2403 C CA  . ASP A 310 ? 0.8734 0.3759 0.8021 -0.0985 0.4227  -0.0641 310 ASP A CA  
2404 C C   . ASP A 310 ? 0.8964 0.4014 0.8108 -0.0959 0.4087  -0.0584 310 ASP A C   
2405 O O   . ASP A 310 ? 0.9279 0.4246 0.8223 -0.0929 0.4080  -0.0499 310 ASP A O   
2406 C CB  . ASP A 310 ? 0.8905 0.3790 0.8178 -0.0985 0.4384  -0.0570 310 ASP A CB  
2407 C CG  . ASP A 310 ? 0.9712 0.4595 0.9036 -0.0984 0.4361  -0.0535 310 ASP A CG  
2408 O OD1 . ASP A 310 ? 0.8691 0.3704 0.8202 -0.1004 0.4279  -0.0615 310 ASP A OD1 
2409 O OD2 . ASP A 310 ? 0.9995 0.4749 0.9157 -0.0946 0.4422  -0.0428 310 ASP A OD2 
2410 N N   . ASP A 311 ? 0.9242 0.4406 0.8481 -0.0957 0.3979  -0.0630 311 ASP A N   
2411 C CA  . ASP A 311 ? 0.8522 0.3701 0.7660 -0.0940 0.3877  -0.0572 311 ASP A CA  
2412 C C   . ASP A 311 ? 0.8343 0.3614 0.7525 -0.0922 0.3779  -0.0608 311 ASP A C   
2413 O O   . ASP A 311 ? 0.8343 0.3604 0.7429 -0.0916 0.3714  -0.0570 311 ASP A O   
2414 C CB  . ASP A 311 ? 0.8459 0.3628 0.7647 -0.0938 0.3895  -0.0534 311 ASP A CB  
2415 C CG  . ASP A 311 ? 0.8810 0.3989 0.7889 -0.0917 0.3804  -0.0469 311 ASP A CG  
2416 O OD1 . ASP A 311 ? 0.8532 0.3666 0.7448 -0.0902 0.3778  -0.0425 311 ASP A OD1 
2417 O OD2 . ASP A 311 ? 0.9205 0.4451 0.8370 -0.0909 0.3757  -0.0474 311 ASP A OD2 
2418 N N   . ILE A 312 ? 0.8262 0.3622 0.7594 -0.0902 0.3775  -0.0686 312 ILE A N   
2419 C CA  . ILE A 312 ? 0.8188 0.3623 0.7533 -0.0850 0.3698  -0.0705 312 ILE A CA  
2420 C C   . ILE A 312 ? 0.8183 0.3677 0.7591 -0.0809 0.3700  -0.0793 312 ILE A C   
2421 O O   . ILE A 312 ? 0.8174 0.3729 0.7726 -0.0814 0.3742  -0.0883 312 ILE A O   
2422 C CB  . ILE A 312 ? 0.8541 0.4054 0.7976 -0.0816 0.3662  -0.0717 312 ILE A CB  
2423 C CG1 . ILE A 312 ? 0.8124 0.3582 0.7485 -0.0844 0.3651  -0.0624 312 ILE A CG1 
2424 C CG2 . ILE A 312 ? 0.8735 0.4321 0.8159 -0.0727 0.3601  -0.0738 312 ILE A CG2 
2425 C CD1 . ILE A 312 ? 0.9368 0.4894 0.8807 -0.0811 0.3621  -0.0630 312 ILE A CD1 
2426 N N   . ALA A 313 ? 0.8656 0.4129 0.7971 -0.0767 0.3665  -0.0774 313 ALA A N   
2427 C CA  . ALA A 313 ? 0.8224 0.3745 0.7564 -0.0703 0.3661  -0.0846 313 ALA A CA  
2428 C C   . ALA A 313 ? 0.8238 0.3780 0.7516 -0.0598 0.3615  -0.0824 313 ALA A C   
2429 O O   . ALA A 313 ? 0.8270 0.3724 0.7451 -0.0604 0.3613  -0.0734 313 ALA A O   
2430 C CB  . ALA A 313 ? 0.8298 0.3728 0.7553 -0.0740 0.3696  -0.0835 313 ALA A CB  
2431 N N   . TRP A 314 ? 0.8402 0.4064 0.7745 -0.0491 0.3584  -0.0914 314 TRP A N   
2432 C CA  . TRP A 314 ? 0.8963 0.4640 0.8208 -0.0345 0.3552  -0.0894 314 TRP A CA  
2433 C C   . TRP A 314 ? 0.8677 0.4361 0.7884 -0.0263 0.3557  -0.0948 314 TRP A C   
2434 O O   . TRP A 314 ? 0.9342 0.5158 0.8673 -0.0233 0.3536  -0.1077 314 TRP A O   
2435 C CB  . TRP A 314 ? 0.8347 0.4175 0.7659 -0.0241 0.3494  -0.0965 314 TRP A CB  
2436 C CG  . TRP A 314 ? 0.8214 0.4021 0.7531 -0.0293 0.3490  -0.0895 314 TRP A CG  
2437 C CD1 . TRP A 314 ? 0.8790 0.4478 0.8072 -0.0418 0.3525  -0.0790 314 TRP A CD1 
2438 C CD2 . TRP A 314 ? 0.8192 0.4114 0.7551 -0.0207 0.3440  -0.0939 314 TRP A CD2 
2439 N NE1 . TRP A 314 ? 0.8525 0.4242 0.7827 -0.0419 0.3505  -0.0757 314 TRP A NE1 
2440 C CE2 . TRP A 314 ? 0.8144 0.3997 0.7492 -0.0294 0.3457  -0.0844 314 TRP A CE2 
2441 C CE3 . TRP A 314 ? 0.8470 0.4561 0.7875 -0.0052 0.3374  -0.1063 314 TRP A CE3 
2442 C CZ2 . TRP A 314 ? 0.8228 0.4158 0.7607 -0.0241 0.3420  -0.0858 314 TRP A CZ2 
2443 C CZ3 . TRP A 314 ? 0.8571 0.4745 0.8004 0.0006  0.3331  -0.1087 314 TRP A CZ3 
2444 C CH2 . TRP A 314 ? 0.8842 0.4928 0.8261 -0.0093 0.3359  -0.0979 314 TRP A CH2 
2445 N N   . MET A 315 ? 0.9586 0.5128 0.8645 -0.0225 0.3592  -0.0858 315 MET A N   
2446 C CA  . MET A 315 ? 1.0076 0.5582 0.9082 -0.0164 0.3612  -0.0890 315 MET A CA  
2447 C C   . MET A 315 ? 1.0224 0.5665 0.9071 0.0018  0.3627  -0.0832 315 MET A C   
2448 O O   . MET A 315 ? 0.9792 0.5148 0.8552 0.0057  0.3655  -0.0730 315 MET A O   
2449 C CB  . MET A 315 ? 0.9321 0.4679 0.8300 -0.0300 0.3665  -0.0842 315 MET A CB  
2450 C CG  . MET A 315 ? 0.9521 0.4913 0.8602 -0.0451 0.3668  -0.0876 315 MET A CG  
2451 S SD  . MET A 315 ? 1.0253 0.5498 0.9269 -0.0569 0.3714  -0.0843 315 MET A SD  
2452 C CE  . MET A 315 ? 0.9461 0.4560 0.8392 -0.0579 0.3728  -0.0737 315 MET A CE  
2453 N N   . LYS A 316 ? 1.0567 0.6040 0.9372 0.0139  0.3620  -0.0894 316 LYS A N   
2454 C CA  . LYS A 316 ? 1.1027 0.6429 0.9650 0.0351  0.3644  -0.0839 316 LYS A CA  
2455 C C   . LYS A 316 ? 1.1233 0.6661 0.9831 0.0444  0.3639  -0.0917 316 LYS A C   
2456 O O   . LYS A 316 ? 1.1507 0.7119 1.0254 0.0423  0.3578  -0.1063 316 LYS A O   
2457 C CB  . LYS A 316 ? 1.0988 0.6536 0.9563 0.0535  0.3581  -0.0873 316 LYS A CB  
2458 C CG  . LYS A 316 ? 1.1766 0.7251 1.0110 0.0805  0.3607  -0.0819 316 LYS A CG  
2459 C CD  . LYS A 316 ? 1.2452 0.8075 1.0717 0.0997  0.3544  -0.0845 316 LYS A CD  
2460 C CE  . LYS A 316 ? 1.2337 0.8273 1.0800 0.1016  0.3405  -0.1063 316 LYS A CE  
2461 N NZ  . LYS A 316 ? 1.1670 0.7739 1.0179 0.1118  0.3352  -0.1207 316 LYS A NZ  
2462 N N   . PHE A 317 ? 1.2115 0.7354 1.0544 0.0546  0.3716  -0.0822 317 PHE A N   
2463 C CA  . PHE A 317 ? 1.1792 0.7044 1.0169 0.0667  0.3713  -0.0886 317 PHE A CA  
2464 C C   . PHE A 317 ? 1.2312 0.7771 1.0632 0.0925  0.3626  -0.0989 317 PHE A C   
2465 O O   . PHE A 317 ? 1.2662 0.8118 1.0839 0.1096  0.3620  -0.0932 317 PHE A O   
2466 C CB  . PHE A 317 ? 1.1772 0.6739 0.9979 0.0719  0.3834  -0.0751 317 PHE A CB  
2467 C CG  . PHE A 317 ? 1.2167 0.6963 1.0457 0.0482  0.3904  -0.0700 317 PHE A CG  
2468 C CD1 . PHE A 317 ? 1.2473 0.7276 1.0840 0.0380  0.3897  -0.0778 317 PHE A CD1 
2469 C CD2 . PHE A 317 ? 1.1873 0.6519 1.0173 0.0371  0.3972  -0.0590 317 PHE A CD2 
2470 C CE1 . PHE A 317 ? 1.1846 0.6511 1.0276 0.0185  0.3947  -0.0750 317 PHE A CE1 
2471 C CE2 . PHE A 317 ? 1.1892 0.6414 1.0285 0.0169  0.4017  -0.0575 317 PHE A CE2 
2472 C CZ  . PHE A 317 ? 1.1817 0.6351 1.0264 0.0083  0.3999  -0.0658 317 PHE A CZ  
2473 N N   . ASP A 318 ? 1.1804 0.6722 1.2232 0.0690  0.4848  0.0323  318 ASP A N   
2474 C CA  . ASP A 318 ? 1.1651 0.7331 1.2786 0.0824  0.4935  0.0468  318 ASP A CA  
2475 C C   . ASP A 318 ? 1.1809 0.7431 1.3184 0.0994  0.5048  0.0628  318 ASP A C   
2476 O O   . ASP A 318 ? 1.1964 0.6966 1.2967 0.0993  0.5035  0.0620  318 ASP A O   
2477 C CB  . ASP A 318 ? 1.2230 0.8049 1.3476 0.0926  0.5201  0.0415  318 ASP A CB  
2478 C CG  . ASP A 318 ? 1.2328 0.7475 1.3231 0.1099  0.5542  0.0369  318 ASP A CG  
2479 O OD1 . ASP A 318 ? 1.1792 0.6381 1.2418 0.1159  0.5590  0.0384  318 ASP A OD1 
2480 O OD2 . ASP A 318 ? 1.1824 0.7002 1.2734 0.1174  0.5765  0.0316  318 ASP A OD2 
2481 N N   . ALA A 319 ? 1.2428 0.8702 1.4434 0.1139  0.5161  0.0780  319 ALA A N   
2482 C CA  . ALA A 319 ? 1.2565 0.8857 1.4862 0.1311  0.5267  0.0958  319 ALA A CA  
2483 C C   . ALA A 319 ? 1.3173 0.8634 1.5059 0.1481  0.5568  0.0911  319 ALA A C   
2484 O O   . ALA A 319 ? 1.3307 0.8364 1.5086 0.1549  0.5583  0.0983  319 ALA A O   
2485 C CB  . ALA A 319 ? 1.2160 0.9325 1.5201 0.1440  0.5362  0.1129  319 ALA A CB  
2486 N N   . GLN A 320 ? 1.3019 0.8209 1.4664 0.1550  0.5812  0.0788  320 GLN A N   
2487 C CA  . GLN A 320 ? 1.2351 0.6787 1.3610 0.1723  0.6126  0.0730  320 GLN A CA  
2488 C C   . GLN A 320 ? 1.2611 0.6140 1.3116 0.1599  0.6052  0.0564  320 GLN A C   
2489 O O   . GLN A 320 ? 1.3016 0.5851 1.3121 0.1721  0.6304  0.0484  320 GLN A O   
2490 C CB  . GLN A 320 ? 1.2285 0.6790 1.3549 0.1828  0.6407  0.0658  320 GLN A CB  
2491 C CG  . GLN A 320 ? 1.2091 0.7530 1.4067 0.1904  0.6457  0.0801  320 GLN A CG  
2492 C CD  . GLN A 320 ? 1.1638 0.7451 1.4129 0.2075  0.6510  0.1035  320 GLN A CD  
2493 O OE1 . GLN A 320 ? 1.2319 0.7645 1.4641 0.2223  0.6671  0.1083  320 GLN A OE1 
2494 N NE2 . GLN A 320 ? 1.1343 0.8030 1.4443 0.2033  0.6343  0.1184  320 GLN A NE2 
2495 N N   . GLY A 321 ? 1.2567 0.6095 1.2863 0.1359  0.5718  0.0510  321 GLY A N   
2496 C CA  . GLY A 321 ? 1.2875 0.5600 1.2471 0.1216  0.5618  0.0368  321 GLY A CA  
2497 C C   . GLY A 321 ? 1.3135 0.5476 1.2183 0.1091  0.5642  0.0164  321 GLY A C   
2498 O O   . GLY A 321 ? 1.3551 0.5210 1.1979 0.0964  0.5570  0.0040  321 GLY A O   
2499 N N   . ASN A 322 ? 1.2544 0.5301 1.1794 0.1114  0.5738  0.0132  322 ASN A N   
2500 C CA  . ASN A 322 ? 1.2584 0.5013 1.1344 0.0999  0.5765  -0.0044 322 ASN A CA  
2501 C C   . ASN A 322 ? 1.3052 0.5763 1.1742 0.0747  0.5413  -0.0089 322 ASN A C   
2502 O O   . ASN A 322 ? 1.2268 0.5661 1.1445 0.0692  0.5202  0.0015  322 ASN A O   
2503 C CB  . ASN A 322 ? 1.2435 0.5165 1.1434 0.1133  0.6030  -0.0054 322 ASN A CB  
2504 C CG  . ASN A 322 ? 1.3764 0.6358 1.2858 0.1359  0.6331  0.0021  322 ASN A CG  
2505 O OD1 . ASN A 322 ? 1.4235 0.7276 1.3890 0.1525  0.6427  0.0175  322 ASN A OD1 
2506 N ND2 . ASN A 322 ? 1.3410 0.5493 1.1969 0.1337  0.6431  -0.0061 322 ASN A ND2 
2507 N N   . LEU A 323 ? 1.3107 0.5296 1.1181 0.0596  0.5355  -0.0242 323 LEU A N   
2508 C CA  . LEU A 323 ? 1.2192 0.4598 1.0145 0.0366  0.5045  -0.0292 323 LEU A CA  
2509 C C   . LEU A 323 ? 1.1797 0.4647 0.9973 0.0363  0.5104  -0.0326 323 LEU A C   
2510 O O   . LEU A 323 ? 1.2670 0.5184 1.0539 0.0398  0.5314  -0.0424 323 LEU A O   
2511 C CB  . LEU A 323 ? 1.2771 0.4438 0.9970 0.0200  0.4953  -0.0425 323 LEU A CB  
2512 C CG  . LEU A 323 ? 1.2486 0.4324 0.9511 -0.0040 0.4620  -0.0464 323 LEU A CG  
2513 C CD1 . LEU A 323 ? 1.2009 0.4328 0.9405 -0.0118 0.4321  -0.0343 323 LEU A CD1 
2514 C CD2 . LEU A 323 ? 1.3119 0.4209 0.9371 -0.0193 0.4574  -0.0594 323 LEU A CD2 
2515 N N   . ARG A 324 ? 1.1098 0.4700 0.9802 0.0316  0.4923  -0.0248 324 ARG A N   
2516 C CA  . ARG A 324 ? 1.1200 0.5280 1.0189 0.0312  0.4970  -0.0270 324 ARG A CA  
2517 C C   . ARG A 324 ? 1.0653 0.4849 0.9462 0.0101  0.4693  -0.0344 324 ARG A C   
2518 O O   . ARG A 324 ? 1.0905 0.5235 0.9716 -0.0023 0.4409  -0.0316 324 ARG A O   
2519 C CB  . ARG A 324 ? 1.0864 0.5741 1.0605 0.0419  0.4993  -0.0137 324 ARG A CB  
2520 C CG  . ARG A 324 ? 1.1753 0.6597 1.1728 0.0649  0.5305  -0.0053 324 ARG A CG  
2521 C CD  . ARG A 324 ? 1.1426 0.7083 1.2107 0.0741  0.5375  0.0058  324 ARG A CD  
2522 N NE  . ARG A 324 ? 1.1818 0.7452 1.2707 0.0967  0.5695  0.0142  324 ARG A NE  
2523 C CZ  . ARG A 324 ? 1.1727 0.7166 1.2496 0.1069  0.5981  0.0093  324 ARG A CZ  
2524 N NH1 . ARG A 324 ? 1.1515 0.6757 1.1957 0.0963  0.5987  -0.0035 324 ARG A NH1 
2525 N NH2 . ARG A 324 ? 1.2271 0.7751 1.3235 0.1241  0.6156  0.0209  324 ARG A NH2 
2526 N N   . ALA A 325 ? 1.0457 0.4612 0.9122 0.0066  0.4780  -0.0429 325 ALA A N   
2527 C CA  . ALA A 325 ? 1.0305 0.4494 0.8751 -0.0119 0.4553  -0.0501 325 ALA A CA  
2528 C C   . ALA A 325 ? 1.0387 0.5088 0.9205 -0.0118 0.4595  -0.0511 325 ALA A C   
2529 O O   . ALA A 325 ? 0.9897 0.4678 0.8898 0.0006  0.4856  -0.0502 325 ALA A O   
2530 C CB  . ALA A 325 ? 1.0933 0.4374 0.8649 -0.0205 0.4596  -0.0613 325 ALA A CB  
2531 N N   . ILE A 326 ? 0.9523 0.4567 0.8445 -0.0258 0.4335  -0.0528 326 ILE A N   
2532 C CA  . ILE A 326 ? 0.9087 0.4546 0.8289 -0.0289 0.4341  -0.0556 326 ILE A CA  
2533 C C   . ILE A 326 ? 0.9110 0.4408 0.7964 -0.0456 0.4129  -0.0630 326 ILE A C   
2534 O O   . ILE A 326 ? 0.9172 0.4317 0.7771 -0.0560 0.3900  -0.0632 326 ILE A O   
2535 C CB  . ILE A 326 ? 0.8419 0.4683 0.8318 -0.0264 0.4246  -0.0484 326 ILE A CB  
2536 C CG1 . ILE A 326 ? 0.8775 0.5324 0.8755 -0.0387 0.3905  -0.0468 326 ILE A CG1 
2537 C CG2 . ILE A 326 ? 0.9323 0.5782 0.9580 -0.0101 0.4429  -0.0386 326 ILE A CG2 
2538 C CD1 . ILE A 326 ? 0.9399 0.6749 1.0038 -0.0376 0.3795  -0.0406 326 ILE A CD1 
2539 N N   . ASN A 327 ? 0.9067 0.4409 0.7917 -0.0483 0.4208  -0.0680 327 ASN A N   
2540 C CA  . ASN A 327 ? 0.8994 0.4308 0.7635 -0.0627 0.4010  -0.0733 327 ASN A CA  
2541 C C   . ASN A 327 ? 0.8348 0.4357 0.7528 -0.0666 0.3817  -0.0714 327 ASN A C   
2542 O O   . ASN A 327 ? 0.8619 0.5025 0.8218 -0.0617 0.3930  -0.0711 327 ASN A O   
2543 C CB  . ASN A 327 ? 0.9461 0.4485 0.7851 -0.0636 0.4188  -0.0789 327 ASN A CB  
2544 C CG  . ASN A 327 ? 0.9152 0.4213 0.7408 -0.0770 0.3996  -0.0827 327 ASN A CG  
2545 O OD1 . ASN A 327 ? 0.9075 0.4139 0.7185 -0.0869 0.3740  -0.0826 327 ASN A OD1 
2546 N ND2 . ASN A 327 ? 0.9453 0.4548 0.7765 -0.0773 0.4120  -0.0854 327 ASN A ND2 
2547 N N   . PRO A 328 ? 0.8119 0.4313 0.7312 -0.0757 0.3530  -0.0700 328 PRO A N   
2548 C CA  . PRO A 328 ? 0.8480 0.5357 0.8192 -0.0789 0.3352  -0.0690 328 PRO A CA  
2549 C C   . PRO A 328 ? 0.8019 0.5013 0.7760 -0.0859 0.3302  -0.0754 328 PRO A C   
2550 O O   . PRO A 328 ? 0.8406 0.5960 0.8600 -0.0875 0.3202  -0.0764 328 PRO A O   
2551 C CB  . PRO A 328 ? 0.7978 0.4940 0.7611 -0.0866 0.3068  -0.0655 328 PRO A CB  
2552 C CG  . PRO A 328 ? 0.7945 0.4226 0.6917 -0.0933 0.3043  -0.0677 328 PRO A CG  
2553 C CD  . PRO A 328 ? 0.8589 0.4386 0.7314 -0.0843 0.3353  -0.0696 328 PRO A CD  
2554 N N   . GLU A 329 ? 0.7928 0.4414 0.7203 -0.0902 0.3370  -0.0797 329 GLU A N   
2555 C CA  . GLU A 329 ? 0.7735 0.4270 0.6999 -0.0968 0.3324  -0.0846 329 GLU A CA  
2556 C C   . GLU A 329 ? 0.7991 0.4665 0.7534 -0.0906 0.3566  -0.0864 329 GLU A C   
2557 O O   . GLU A 329 ? 0.8545 0.5215 0.8218 -0.0810 0.3786  -0.0838 329 GLU A O   
2558 C CB  . GLU A 329 ? 0.8155 0.4105 0.6798 -0.1048 0.3285  -0.0865 329 GLU A CB  
2559 C CG  . GLU A 329 ? 0.8213 0.4048 0.6565 -0.1136 0.3023  -0.0844 329 GLU A CG  
2560 C CD  . GLU A 329 ? 0.8999 0.4331 0.6771 -0.1230 0.2970  -0.0858 329 GLU A CD  
2561 O OE1 . GLU A 329 ? 1.0107 0.4949 0.7498 -0.1217 0.3164  -0.0872 329 GLU A OE1 
2562 O OE2 . GLU A 329 ? 0.9029 0.4472 0.6727 -0.1317 0.2737  -0.0851 329 GLU A OE2 
2563 N N   . ASN A 330 ? 0.7695 0.4493 0.7329 -0.0963 0.3523  -0.0905 330 ASN A N   
2564 C CA  . ASN A 330 ? 0.8123 0.5070 0.8023 -0.0932 0.3724  -0.0924 330 ASN A CA  
2565 C C   . ASN A 330 ? 0.8356 0.4863 0.7882 -0.0978 0.3815  -0.0947 330 ASN A C   
2566 O O   . ASN A 330 ? 0.7775 0.4353 0.7473 -0.0964 0.3987  -0.0956 330 ASN A O   
2567 C CB  . ASN A 330 ? 0.8150 0.5726 0.8604 -0.0959 0.3608  -0.0954 330 ASN A CB  
2568 C CG  . ASN A 330 ? 0.7937 0.5758 0.8750 -0.0926 0.3821  -0.0964 330 ASN A CG  
2569 O OD1 . ASN A 330 ? 0.8572 0.6209 0.9320 -0.0858 0.4061  -0.0930 330 ASN A OD1 
2570 N ND2 . ASN A 330 ? 0.6548 0.4793 0.7741 -0.0977 0.3736  -0.1011 330 ASN A ND2 
2571 N N   . GLY A 331 ? 0.8634 0.4711 0.7659 -0.1041 0.3702  -0.0947 331 GLY A N   
2572 C CA  . GLY A 331 ? 0.8472 0.4129 0.7114 -0.1090 0.3779  -0.0953 331 GLY A CA  
2573 C C   . GLY A 331 ? 0.8918 0.4053 0.6951 -0.1139 0.3711  -0.0939 331 GLY A C   
2574 O O   . GLY A 331 ? 0.9031 0.4086 0.6930 -0.1128 0.3640  -0.0927 331 GLY A O   
2575 N N   . PHE A 332 ? 0.9241 0.4022 0.6903 -0.1202 0.3732  -0.0935 332 PHE A N   
2576 C CA  . PHE A 332 ? 0.9704 0.3981 0.6753 -0.1268 0.3677  -0.0921 332 PHE A CA  
2577 C C   . PHE A 332 ? 0.9660 0.3935 0.6557 -0.1367 0.3444  -0.0901 332 PHE A C   
2578 O O   . PHE A 332 ? 0.9585 0.3977 0.6644 -0.1385 0.3449  -0.0897 332 PHE A O   
2579 C CB  . PHE A 332 ? 1.0266 0.4080 0.6932 -0.1253 0.3936  -0.0922 332 PHE A CB  
2580 C CG  . PHE A 332 ? 1.0695 0.4522 0.7530 -0.1139 0.4192  -0.0935 332 PHE A CG  
2581 C CD1 . PHE A 332 ? 1.0353 0.4101 0.7128 -0.1085 0.4208  -0.0942 332 PHE A CD1 
2582 C CD2 . PHE A 332 ? 1.0267 0.4184 0.7320 -0.1086 0.4421  -0.0932 332 PHE A CD2 
2583 C CE1 . PHE A 332 ? 1.0419 0.4183 0.7359 -0.0966 0.4450  -0.0944 332 PHE A CE1 
2584 C CE2 . PHE A 332 ? 1.0784 0.4739 0.7999 -0.0973 0.4661  -0.0933 332 PHE A CE2 
2585 C CZ  . PHE A 332 ? 1.1427 0.5305 0.8589 -0.0906 0.4678  -0.0938 332 PHE A CZ  
2586 N N   . PHE A 333 ? 0.9767 0.3905 0.6352 -0.1433 0.3244  -0.0883 333 PHE A N   
2587 C CA  . PHE A 333 ? 0.9837 0.3976 0.6245 -0.1525 0.3010  -0.0850 333 PHE A CA  
2588 C C   . PHE A 333 ? 1.0363 0.3975 0.6108 -0.1613 0.2999  -0.0821 333 PHE A C   
2589 O O   . PHE A 333 ? 1.0871 0.4412 0.6358 -0.1683 0.2804  -0.0798 333 PHE A O   
2590 C CB  . PHE A 333 ? 0.9922 0.4474 0.6605 -0.1537 0.2748  -0.0845 333 PHE A CB  
2591 C CG  . PHE A 333 ? 0.9957 0.4612 0.6561 -0.1610 0.2506  -0.0808 333 PHE A CG  
2592 C CD1 . PHE A 333 ? 0.9408 0.4349 0.6356 -0.1589 0.2470  -0.0817 333 PHE A CD1 
2593 C CD2 . PHE A 333 ? 1.0212 0.4689 0.6407 -0.1698 0.2312  -0.0762 333 PHE A CD2 
2594 C CE1 . PHE A 333 ? 0.9245 0.4283 0.6135 -0.1640 0.2255  -0.0778 333 PHE A CE1 
2595 C CE2 . PHE A 333 ? 1.0224 0.4825 0.6359 -0.1757 0.2091  -0.0715 333 PHE A CE2 
2596 C CZ  . PHE A 333 ? 1.0117 0.5000 0.6606 -0.1719 0.2066  -0.0722 333 PHE A CZ  
2597 N N   . GLY A 334 ? 1.0894 0.4145 0.6352 -0.1616 0.3210  -0.0821 334 GLY A N   
2598 C CA  . GLY A 334 ? 1.1519 0.4257 0.6337 -0.1696 0.3244  -0.0807 334 GLY A CA  
2599 C C   . GLY A 334 ? 1.1587 0.4173 0.6077 -0.1801 0.3120  -0.0745 334 GLY A C   
2600 O O   . GLY A 334 ? 1.1911 0.4724 0.6661 -0.1795 0.3064  -0.0711 334 GLY A O   
2601 N N   . VAL A 335 ? 1.2072 0.4261 0.5977 -0.1900 0.3079  -0.0727 335 VAL A N   
2602 C CA  . VAL A 335 ? 1.3079 0.5103 0.6616 -0.2008 0.2967  -0.0653 335 VAL A CA  
2603 C C   . VAL A 335 ? 1.3615 0.5477 0.7096 -0.1991 0.3178  -0.0633 335 VAL A C   
2604 O O   . VAL A 335 ? 1.3317 0.5024 0.6802 -0.1928 0.3432  -0.0683 335 VAL A O   
2605 C CB  . VAL A 335 ? 1.4016 0.5657 0.6922 -0.2132 0.2883  -0.0643 335 VAL A CB  
2606 C CG1 . VAL A 335 ? 1.4561 0.6078 0.7098 -0.2250 0.2755  -0.0550 335 VAL A CG1 
2607 C CG2 . VAL A 335 ? 1.3440 0.5243 0.6416 -0.2154 0.2678  -0.0657 335 VAL A CG2 
2608 N N   . ALA A 336 ? 1.3693 0.5597 0.7122 -0.2046 0.3074  -0.0551 336 ALA A N   
2609 C CA  . ALA A 336 ? 1.3304 0.5102 0.6734 -0.2035 0.3249  -0.0512 336 ALA A CA  
2610 C C   . ALA A 336 ? 1.3861 0.5209 0.6654 -0.2134 0.3341  -0.0474 336 ALA A C   
2611 O O   . ALA A 336 ? 1.3560 0.4678 0.6208 -0.2108 0.3589  -0.0509 336 ALA A O   
2612 C CB  . ALA A 336 ? 1.3150 0.5225 0.6891 -0.2033 0.3105  -0.0437 336 ALA A CB  
2613 N N   . PRO A 337 ? 1.4220 0.5452 0.6619 -0.2250 0.3149  -0.0400 337 PRO A N   
2614 C CA  . PRO A 337 ? 1.4396 0.5230 0.6185 -0.2359 0.3230  -0.0357 337 PRO A CA  
2615 C C   . PRO A 337 ? 1.4521 0.5011 0.5968 -0.2359 0.3432  -0.0459 337 PRO A C   
2616 O O   . PRO A 337 ? 1.5333 0.5838 0.6865 -0.2317 0.3425  -0.0545 337 PRO A O   
2617 C CB  . PRO A 337 ? 1.4296 0.5131 0.5764 -0.2483 0.2952  -0.0276 337 PRO A CB  
2618 C CG  . PRO A 337 ? 1.4605 0.5873 0.6587 -0.2422 0.2748  -0.0238 337 PRO A CG  
2619 C CD  . PRO A 337 ? 1.3993 0.5478 0.6485 -0.2291 0.2850  -0.0347 337 PRO A CD  
2620 N N   . GLY A 338 ? 1.4777 0.4965 0.5841 -0.2402 0.3613  -0.0449 338 GLY A N   
2621 C CA  . GLY A 338 ? 1.5183 0.5039 0.5923 -0.2386 0.3831  -0.0554 338 GLY A CA  
2622 C C   . GLY A 338 ? 1.5055 0.4959 0.6151 -0.2246 0.4105  -0.0617 338 GLY A C   
2623 O O   . GLY A 338 ? 1.5988 0.5601 0.6807 -0.2222 0.4333  -0.0689 338 GLY A O   
2624 N N   . THR A 339 ? 1.4529 0.4818 0.6243 -0.2145 0.4084  -0.0599 339 THR A N   
2625 C CA  . THR A 339 ? 1.4362 0.4777 0.6473 -0.2010 0.4326  -0.0649 339 THR A CA  
2626 C C   . THR A 339 ? 1.4897 0.5225 0.6936 -0.2022 0.4510  -0.0588 339 THR A C   
2627 O O   . THR A 339 ? 1.4570 0.5110 0.6883 -0.2033 0.4443  -0.0506 339 THR A O   
2628 C CB  . THR A 339 ? 1.3729 0.4605 0.6513 -0.1920 0.4223  -0.0653 339 THR A CB  
2629 O OG1 . THR A 339 ? 1.4659 0.5638 0.7484 -0.1930 0.4014  -0.0687 339 THR A OG1 
2630 C CG2 . THR A 339 ? 1.3565 0.4586 0.6744 -0.1788 0.4467  -0.0708 339 THR A CG2 
2631 N N   . SER A 340 ? 1.5602 0.5628 0.7283 -0.2015 0.4739  -0.0632 340 SER A N   
2632 C CA  . SER A 340 ? 1.6151 0.6154 0.7811 -0.1998 0.4888  -0.0598 340 SER A CA  
2633 C C   . SER A 340 ? 1.5400 0.5411 0.7270 -0.1872 0.5173  -0.0664 340 SER A C   
2634 O O   . SER A 340 ? 1.6108 0.6106 0.8076 -0.1795 0.5258  -0.0740 340 SER A O   
2635 C CB  . SER A 340 ? 1.6365 0.6062 0.7445 -0.2100 0.4843  -0.0591 340 SER A CB  
2636 O OG  . SER A 340 ? 1.8284 0.7663 0.9003 -0.2095 0.4945  -0.0695 340 SER A OG  
2637 N N   . VAL A 341 ? 1.6010 0.6073 0.7979 -0.1846 0.5310  -0.0623 341 VAL A N   
2638 C CA  . VAL A 341 ? 1.7221 0.7319 0.9401 -0.1726 0.5563  -0.0668 341 VAL A CA  
2639 C C   . VAL A 341 ? 1.8055 0.7815 0.9842 -0.1703 0.5664  -0.0748 341 VAL A C   
2640 O O   . VAL A 341 ? 1.6927 0.6716 0.8913 -0.1586 0.5829  -0.0790 341 VAL A O   
2641 C CB  . VAL A 341 ? 1.7742 0.7964 1.0078 -0.1723 0.5665  -0.0593 341 VAL A CB  
2642 C CG1 . VAL A 341 ? 1.7333 0.7619 0.9892 -0.1601 0.5909  -0.0626 341 VAL A CG1 
2643 C CG2 . VAL A 341 ? 1.7019 0.7566 0.9791 -0.1746 0.5552  -0.0511 341 VAL A CG2 
2644 N N   . LYS A 342 ? 2.2197 1.1654 1.3452 -0.1815 0.5552  -0.0759 342 LYS A N   
2645 C CA  . LYS A 342 ? 2.2667 1.1787 1.3542 -0.1814 0.5634  -0.0829 342 LYS A CA  
2646 C C   . LYS A 342 ? 2.2602 1.1619 1.3428 -0.1803 0.5552  -0.0888 342 LYS A C   
2647 O O   . LYS A 342 ? 2.2868 1.1702 1.3580 -0.1751 0.5656  -0.0933 342 LYS A O   
2648 C CB  . LYS A 342 ? 2.3181 1.2039 1.3516 -0.1952 0.5552  -0.0813 342 LYS A CB  
2649 C CG  . LYS A 342 ? 2.3440 1.2239 1.3503 -0.2090 0.5284  -0.0793 342 LYS A CG  
2650 C CD  . LYS A 342 ? 2.4914 1.3482 1.4463 -0.2226 0.5207  -0.0776 342 LYS A CD  
2651 C CE  . LYS A 342 ? 2.5164 1.3706 1.4460 -0.2364 0.4923  -0.0748 342 LYS A CE  
2652 N NZ  . LYS A 342 ? 2.6355 1.4717 1.5508 -0.2385 0.4848  -0.0827 342 LYS A NZ  
2653 N N   . THR A 343 ? 1.8261 0.7414 0.9180 -0.1851 0.5362  -0.0876 343 THR A N   
2654 C CA  . THR A 343 ? 1.7404 0.6505 0.8301 -0.1847 0.5262  -0.0919 343 THR A CA  
2655 C C   . THR A 343 ? 1.6358 0.5782 0.7825 -0.1697 0.5345  -0.0931 343 THR A C   
2656 O O   . THR A 343 ? 1.6553 0.5951 0.8122 -0.1601 0.5444  -0.0956 343 THR A O   
2657 C CB  . THR A 343 ? 1.6818 0.5918 0.7500 -0.1982 0.4994  -0.0899 343 THR A CB  
2658 O OG1 . THR A 343 ? 1.6724 0.6170 0.7769 -0.1972 0.4929  -0.0838 343 THR A OG1 
2659 C CG2 . THR A 343 ? 1.7073 0.5904 0.7222 -0.2131 0.4885  -0.0879 343 THR A CG2 
2660 N N   . ASN A 344 ? 1.5455 0.5208 0.7310 -0.1674 0.5300  -0.0908 344 ASN A N   
2661 C CA  . ASN A 344 ? 1.5120 0.5235 0.7556 -0.1544 0.5341  -0.0926 344 ASN A CA  
2662 C C   . ASN A 344 ? 1.5104 0.5515 0.7963 -0.1486 0.5479  -0.0883 344 ASN A C   
2663 O O   . ASN A 344 ? 1.4459 0.5204 0.7706 -0.1502 0.5342  -0.0840 344 ASN A O   
2664 C CB  . ASN A 344 ? 1.4456 0.4760 0.7062 -0.1577 0.5082  -0.0941 344 ASN A CB  
2665 C CG  . ASN A 344 ? 1.4432 0.5077 0.7596 -0.1446 0.5100  -0.0970 344 ASN A CG  
2666 O OD1 . ASN A 344 ? 1.3936 0.4728 0.7401 -0.1329 0.5307  -0.0964 344 ASN A OD1 
2667 N ND2 . ASN A 344 ? 1.5098 0.5949 0.8456 -0.1470 0.4851  -0.0968 344 ASN A ND2 
2668 N N   . PRO A 345 ? 1.5335 0.5702 0.8245 -0.1419 0.5672  -0.0866 345 PRO A N   
2669 C CA  . PRO A 345 ? 1.5082 0.5750 0.8412 -0.1372 0.5783  -0.0818 345 PRO A CA  
2670 C C   . PRO A 345 ? 1.3987 0.5089 0.7944 -0.1273 0.5800  -0.0822 345 PRO A C   
2671 O O   . PRO A 345 ? 1.4319 0.5725 0.8654 -0.1281 0.5806  -0.0779 345 PRO A O   
2672 C CB  . PRO A 345 ? 1.5582 0.6088 0.8784 -0.1312 0.5976  -0.0812 345 PRO A CB  
2673 C CG  . PRO A 345 ? 1.5282 0.5541 0.8239 -0.1269 0.5998  -0.0860 345 PRO A CG  
2674 C CD  . PRO A 345 ? 1.6188 0.6259 0.8805 -0.1379 0.5793  -0.0889 345 PRO A CD  
2675 N N   . ASN A 346 ? 1.3882 0.5040 0.7983 -0.1185 0.5796  -0.0861 346 ASN A N   
2676 C CA  . ASN A 346 ? 1.3348 0.4954 0.8052 -0.1097 0.5783  -0.0863 346 ASN A CA  
2677 C C   . ASN A 346 ? 1.3351 0.5185 0.8238 -0.1172 0.5581  -0.0872 346 ASN A C   
2678 O O   . ASN A 346 ? 1.2855 0.5122 0.8292 -0.1138 0.5544  -0.0852 346 ASN A O   
2679 C CB  . ASN A 346 ? 1.4000 0.5612 0.8789 -0.0996 0.5792  -0.0885 346 ASN A CB  
2680 C CG  . ASN A 346 ? 1.4521 0.6029 0.9294 -0.0894 0.5986  -0.0860 346 ASN A CG  
2681 O OD1 . ASN A 346 ? 1.4434 0.6174 0.9535 -0.0830 0.6109  -0.0821 346 ASN A OD1 
2682 N ND2 . ASN A 346 ? 1.4057 0.5221 0.8444 -0.0881 0.6009  -0.0881 346 ASN A ND2 
2683 N N   . ALA A 347 ? 1.3381 0.4994 0.7899 -0.1277 0.5362  -0.0873 347 ALA A N   
2684 C CA  . ALA A 347 ? 1.2676 0.4553 0.7432 -0.1349 0.5076  -0.0844 347 ALA A CA  
2685 C C   . ALA A 347 ? 1.2662 0.4697 0.7617 -0.1400 0.5075  -0.0782 347 ALA A C   
2686 O O   . ALA A 347 ? 1.2879 0.5290 0.8303 -0.1398 0.4950  -0.0769 347 ALA A O   
2687 C CB  . ALA A 347 ? 1.2899 0.4497 0.7181 -0.1454 0.4856  -0.0845 347 ALA A CB  
2688 N N   . ILE A 348 ? 1.3644 0.5392 0.8246 -0.1447 0.5216  -0.0743 348 ILE A N   
2689 C CA  . ILE A 348 ? 1.2889 0.4744 0.7648 -0.1502 0.5222  -0.0671 348 ILE A CA  
2690 C C   . ILE A 348 ? 1.2865 0.5107 0.8216 -0.1428 0.5349  -0.0671 348 ILE A C   
2691 O O   . ILE A 348 ? 1.2192 0.4703 0.7915 -0.1460 0.5244  -0.0643 348 ILE A O   
2692 C CB  . ILE A 348 ? 1.3430 0.4913 0.7692 -0.1561 0.5378  -0.0622 348 ILE A CB  
2693 C CG1 . ILE A 348 ? 1.3795 0.4921 0.7466 -0.1653 0.5235  -0.0619 348 ILE A CG1 
2694 C CG2 . ILE A 348 ? 1.5227 0.6818 0.9670 -0.1617 0.5391  -0.0534 348 ILE A CG2 
2695 C CD1 . ILE A 348 ? 1.4501 0.5725 0.8205 -0.1740 0.4939  -0.0566 348 ILE A CD1 
2696 N N   . LYS A 349 ? 1.3182 0.5458 0.8625 -0.1331 0.5582  -0.0704 349 LYS A N   
2697 C CA  . LYS A 349 ? 1.2282 0.4947 0.8278 -0.1267 0.5715  -0.0696 349 LYS A CA  
2698 C C   . LYS A 349 ? 1.2193 0.5287 0.8711 -0.1245 0.5532  -0.0729 349 LYS A C   
2699 O O   . LYS A 349 ? 1.2250 0.5700 0.9246 -0.1239 0.5568  -0.0717 349 LYS A O   
2700 C CB  . LYS A 349 ? 1.2412 0.5074 0.8455 -0.1137 0.5899  -0.0719 349 LYS A CB  
2701 C CG  . LYS A 349 ? 1.5356 0.7715 1.1045 -0.1133 0.6037  -0.0689 349 LYS A CG  
2702 C CD  . LYS A 349 ? 1.5991 0.8435 1.1849 -0.1000 0.6189  -0.0688 349 LYS A CD  
2703 C CE  . LYS A 349 ? 1.7295 0.9491 1.2844 -0.0995 0.6335  -0.0656 349 LYS A CE  
2704 N NZ  . LYS A 349 ? 1.7300 0.9635 1.3066 -0.0863 0.6484  -0.0638 349 LYS A NZ  
2705 N N   . THR A 350 ? 1.2184 0.5264 0.8620 -0.1241 0.5337  -0.0770 350 THR A N   
2706 C CA  . THR A 350 ? 1.1184 0.4691 0.8104 -0.1215 0.5168  -0.0803 350 THR A CA  
2707 C C   . THR A 350 ? 1.0779 0.4447 0.7863 -0.1301 0.4926  -0.0792 350 THR A C   
2708 O O   . THR A 350 ? 1.0397 0.4481 0.7981 -0.1291 0.4847  -0.0814 350 THR A O   
2709 C CB  . THR A 350 ? 1.1281 0.4727 0.8063 -0.1171 0.5066  -0.0844 350 THR A CB  
2710 O OG1 . THR A 350 ? 1.1918 0.5199 0.8561 -0.1077 0.5301  -0.0857 350 THR A OG1 
2711 C CG2 . THR A 350 ? 1.0483 0.4409 0.7782 -0.1142 0.4900  -0.0870 350 THR A CG2 
2712 N N   . ILE A 351 ? 1.1047 0.4405 0.7724 -0.1383 0.4809  -0.0758 351 ILE A N   
2713 C CA  . ILE A 351 ? 1.0817 0.4302 0.7603 -0.1449 0.4556  -0.0745 351 ILE A CA  
2714 C C   . ILE A 351 ? 1.1719 0.5260 0.8693 -0.1497 0.4597  -0.0701 351 ILE A C   
2715 O O   . ILE A 351 ? 1.1812 0.5402 0.8844 -0.1549 0.4413  -0.0679 351 ILE A O   
2716 C CB  . ILE A 351 ? 1.1502 0.4658 0.7766 -0.1514 0.4385  -0.0717 351 ILE A CB  
2717 C CG1 . ILE A 351 ? 1.1651 0.4363 0.7393 -0.1560 0.4539  -0.0666 351 ILE A CG1 
2718 C CG2 . ILE A 351 ? 1.1048 0.4204 0.7200 -0.1482 0.4289  -0.0764 351 ILE A CG2 
2719 C CD1 . ILE A 351 ? 1.1962 0.4357 0.7169 -0.1641 0.4378  -0.0631 351 ILE A CD1 
2720 N N   . GLN A 352 ? 1.1649 0.5186 0.8724 -0.1479 0.4838  -0.0682 352 GLN A N   
2721 C CA  . GLN A 352 ? 1.1754 0.5310 0.8982 -0.1535 0.4891  -0.0631 352 GLN A CA  
2722 C C   . GLN A 352 ? 1.1237 0.5228 0.9071 -0.1531 0.4844  -0.0673 352 GLN A C   
2723 O O   . GLN A 352 ? 1.1827 0.5856 0.9844 -0.1578 0.4910  -0.0639 352 GLN A O   
2724 C CB  . GLN A 352 ? 1.1946 0.5309 0.8999 -0.1532 0.5169  -0.0582 352 GLN A CB  
2725 C CG  . GLN A 352 ? 1.2679 0.5585 0.9111 -0.1571 0.5211  -0.0528 352 GLN A CG  
2726 C CD  . GLN A 352 ? 1.5109 0.7857 1.1397 -0.1585 0.5456  -0.0467 352 GLN A CD  
2727 O OE1 . GLN A 352 ? 1.6860 0.9851 1.3496 -0.1535 0.5602  -0.0479 352 GLN A OE1 
2728 N NE2 . GLN A 352 ? 1.6253 0.8670 1.2056 -0.1628 0.5446  -0.0415 352 GLN A NE2 
2729 N N   . LYS A 353 ? 1.0170 0.4491 0.8316 -0.1484 0.4732  -0.0745 353 LYS A N   
2730 C CA  . LYS A 353 ? 1.0581 0.5322 0.9279 -0.1495 0.4664  -0.0794 353 LYS A CA  
2731 C C   . LYS A 353 ? 1.0431 0.5490 0.9358 -0.1452 0.4486  -0.0865 353 LYS A C   
2732 O O   . LYS A 353 ? 1.0435 0.5446 0.9189 -0.1399 0.4486  -0.0873 353 LYS A O   
2733 C CB  . LYS A 353 ? 1.0348 0.5309 0.9385 -0.1485 0.4894  -0.0794 353 LYS A CB  
2734 C CG  . LYS A 353 ? 1.0904 0.6037 1.0039 -0.1399 0.5035  -0.0814 353 LYS A CG  
2735 C CD  . LYS A 353 ? 1.1787 0.7161 1.1260 -0.1395 0.5261  -0.0797 353 LYS A CD  
2736 C CE  . LYS A 353 ? 1.3461 0.9003 1.3023 -0.1281 0.5378  -0.0802 353 LYS A CE  
2737 N NZ  . LYS A 353 ? 1.5738 1.1518 1.5590 -0.1236 0.5467  -0.0776 353 LYS A NZ  
2738 N N   . ASN A 354 ? 0.9859 0.5236 0.9172 -0.1477 0.4334  -0.0916 354 ASN A N   
2739 C CA  . ASN A 354 ? 0.8503 0.4247 0.8087 -0.1444 0.4157  -0.0984 354 ASN A CA  
2740 C C   . ASN A 354 ? 0.8601 0.4151 0.7808 -0.1430 0.3982  -0.0967 354 ASN A C   
2741 O O   . ASN A 354 ? 0.9234 0.5006 0.8544 -0.1390 0.3887  -0.1000 354 ASN A O   
2742 C CB  . ASN A 354 ? 0.8265 0.4354 0.8177 -0.1389 0.4288  -0.1014 354 ASN A CB  
2743 C CG  . ASN A 354 ? 0.8833 0.5123 0.9096 -0.1414 0.4475  -0.1019 354 ASN A CG  
2744 O OD1 . ASN A 354 ? 1.0077 0.6434 1.0534 -0.1478 0.4436  -0.1041 354 ASN A OD1 
2745 N ND2 . ASN A 354 ? 0.8307 0.4689 0.8653 -0.1364 0.4681  -0.0995 354 ASN A ND2 
2746 N N   . THR A 355 ? 0.8948 0.4099 0.7721 -0.1469 0.3931  -0.0909 355 THR A N   
2747 C CA  . THR A 355 ? 0.9299 0.4205 0.7635 -0.1474 0.3794  -0.0879 355 THR A CA  
2748 C C   . THR A 355 ? 0.9398 0.4292 0.7662 -0.1515 0.3556  -0.0859 355 THR A C   
2749 O O   . THR A 355 ? 0.9658 0.4431 0.7915 -0.1551 0.3562  -0.0823 355 THR A O   
2750 C CB  . THR A 355 ? 0.9646 0.4077 0.7462 -0.1489 0.3954  -0.0816 355 THR A CB  
2751 O OG1 . THR A 355 ? 0.9698 0.4154 0.7597 -0.1435 0.4186  -0.0834 355 THR A OG1 
2752 C CG2 . THR A 355 ? 0.9861 0.4036 0.7209 -0.1509 0.3812  -0.0792 355 THR A CG2 
2753 N N   . ILE A 356 ? 0.8913 0.3935 0.7129 -0.1508 0.3348  -0.0875 356 ILE A N   
2754 C CA  . ILE A 356 ? 0.8879 0.3926 0.7021 -0.1536 0.3109  -0.0850 356 ILE A CA  
2755 C C   . ILE A 356 ? 0.9223 0.3898 0.6788 -0.1578 0.3032  -0.0774 356 ILE A C   
2756 O O   . ILE A 356 ? 0.9879 0.4485 0.7237 -0.1575 0.3025  -0.0781 356 ILE A O   
2757 C CB  . ILE A 356 ? 0.9206 0.4718 0.7727 -0.1506 0.2916  -0.0917 356 ILE A CB  
2758 C CG1 . ILE A 356 ? 0.8864 0.4757 0.7947 -0.1478 0.2996  -0.1000 356 ILE A CG1 
2759 C CG2 . ILE A 356 ? 0.8541 0.4087 0.6974 -0.1525 0.2673  -0.0886 356 ILE A CG2 
2760 C CD1 . ILE A 356 ? 0.8646 0.5020 0.8119 -0.1456 0.2804  -0.1072 356 ILE A CD1 
2761 N N   . PHE A 357 ? 0.9473 0.3910 0.6780 -0.1623 0.2972  -0.0698 357 PHE A N   
2762 C CA  . PHE A 357 ? 0.9847 0.3943 0.6596 -0.1681 0.2892  -0.0615 357 PHE A CA  
2763 C C   . PHE A 357 ? 1.0471 0.4717 0.7196 -0.1697 0.2617  -0.0576 357 PHE A C   
2764 O O   . PHE A 357 ? 0.9951 0.4461 0.7035 -0.1665 0.2519  -0.0594 357 PHE A O   
2765 C CB  . PHE A 357 ? 1.1232 0.4946 0.7661 -0.1726 0.3035  -0.0532 357 PHE A CB  
2766 C CG  . PHE A 357 ? 1.0466 0.4025 0.6881 -0.1711 0.3312  -0.0558 357 PHE A CG  
2767 C CD1 . PHE A 357 ? 1.0274 0.4016 0.7122 -0.1674 0.3455  -0.0597 357 PHE A CD1 
2768 C CD2 . PHE A 357 ? 1.0844 0.4078 0.6809 -0.1736 0.3433  -0.0544 357 PHE A CD2 
2769 C CE1 . PHE A 357 ? 1.0818 0.4447 0.7661 -0.1660 0.3710  -0.0610 357 PHE A CE1 
2770 C CE2 . PHE A 357 ? 1.1226 0.4332 0.7181 -0.1711 0.3696  -0.0566 357 PHE A CE2 
2771 C CZ  . PHE A 357 ? 1.0825 0.4141 0.7225 -0.1671 0.3834  -0.0592 357 PHE A CZ  
2772 N N   . THR A 358 ? 1.0284 0.4359 0.6577 -0.1750 0.2494  -0.0524 358 THR A N   
2773 C CA  . THR A 358 ? 1.0814 0.5038 0.7040 -0.1773 0.2228  -0.0472 358 THR A CA  
2774 C C   . THR A 358 ? 1.0930 0.4792 0.6571 -0.1860 0.2172  -0.0358 358 THR A C   
2775 O O   . THR A 358 ? 1.1912 0.5513 0.7153 -0.1916 0.2225  -0.0355 358 THR A O   
2776 C CB  . THR A 358 ? 1.1006 0.5525 0.7367 -0.1759 0.2075  -0.0527 358 THR A CB  
2777 O OG1 . THR A 358 ? 1.0051 0.4935 0.6959 -0.1684 0.2130  -0.0629 358 THR A OG1 
2778 C CG2 . THR A 358 ? 1.0498 0.5209 0.6810 -0.1780 0.1800  -0.0466 358 THR A CG2 
2779 N N   . ASN A 359 ? 1.1563 0.5412 0.7155 -0.1873 0.2068  -0.0265 359 ASN A N   
2780 C CA  . ASN A 359 ? 1.2196 0.5786 0.7276 -0.1960 0.1972  -0.0136 359 ASN A CA  
2781 C C   . ASN A 359 ? 1.2556 0.5716 0.7219 -0.2022 0.2173  -0.0090 359 ASN A C   
2782 O O   . ASN A 359 ? 1.3555 0.6477 0.7723 -0.2114 0.2113  0.0002  359 ASN A O   
2783 C CB  . ASN A 359 ? 1.2037 0.5679 0.6835 -0.2021 0.1778  -0.0120 359 ASN A CB  
2784 C CG  . ASN A 359 ? 1.2264 0.6342 0.7412 -0.1971 0.1549  -0.0132 359 ASN A CG  
2785 O OD1 . ASN A 359 ? 1.2195 0.6474 0.7649 -0.1910 0.1484  -0.0107 359 ASN A OD1 
2786 N ND2 . ASN A 359 ? 1.2372 0.6596 0.7477 -0.1996 0.1427  -0.0171 359 ASN A ND2 
2787 N N   . VAL A 360 ? 1.2237 0.5308 0.7078 -0.1982 0.2407  -0.0149 360 VAL A N   
2788 C CA  . VAL A 360 ? 1.2868 0.5567 0.7354 -0.2034 0.2603  -0.0096 360 VAL A CA  
2789 C C   . VAL A 360 ? 1.2889 0.5549 0.7457 -0.2034 0.2607  0.0012  360 VAL A C   
2790 O O   . VAL A 360 ? 1.2751 0.5662 0.7724 -0.1974 0.2510  0.0015  360 VAL A O   
2791 C CB  . VAL A 360 ? 1.2645 0.5267 0.7261 -0.1992 0.2863  -0.0196 360 VAL A CB  
2792 C CG1 . VAL A 360 ? 1.1629 0.4269 0.6162 -0.1984 0.2864  -0.0292 360 VAL A CG1 
2793 C CG2 . VAL A 360 ? 1.1324 0.4217 0.6534 -0.1908 0.2940  -0.0251 360 VAL A CG2 
2794 N N   . ALA A 361 ? 1.2799 0.5136 0.6975 -0.2101 0.2723  0.0104  361 ALA A N   
2795 C CA  . ALA A 361 ? 1.3037 0.5305 0.7256 -0.2109 0.2736  0.0228  361 ALA A CA  
2796 C C   . ALA A 361 ? 1.2490 0.4804 0.7128 -0.2049 0.2930  0.0179  361 ALA A C   
2797 O O   . ALA A 361 ? 1.3023 0.5334 0.7772 -0.2024 0.3106  0.0074  361 ALA A O   
2798 C CB  . ALA A 361 ? 1.3510 0.5442 0.7158 -0.2212 0.2789  0.0355  361 ALA A CB  
2799 N N   . GLU A 362 ? 1.2182 0.4541 0.7055 -0.2026 0.2898  0.0260  362 GLU A N   
2800 C CA  . GLU A 362 ? 1.2486 0.4873 0.7746 -0.1988 0.3067  0.0231  362 GLU A CA  
2801 C C   . GLU A 362 ? 1.2929 0.5040 0.7959 -0.2046 0.3177  0.0382  362 GLU A C   
2802 O O   . GLU A 362 ? 1.2982 0.5001 0.7790 -0.2078 0.3052  0.0524  362 GLU A O   
2803 C CB  . GLU A 362 ? 1.2240 0.4916 0.8035 -0.1912 0.2949  0.0183  362 GLU A CB  
2804 C CG  . GLU A 362 ? 1.2325 0.5042 0.8540 -0.1886 0.3115  0.0138  362 GLU A CG  
2805 C CD  . GLU A 362 ? 1.3252 0.6224 0.9962 -0.1820 0.2995  0.0085  362 GLU A CD  
2806 O OE1 . GLU A 362 ? 1.3160 0.6303 0.9903 -0.1781 0.2787  0.0078  362 GLU A OE1 
2807 O OE2 . GLU A 362 ? 1.4003 0.7006 1.1064 -0.1809 0.3110  0.0048  362 GLU A OE2 
2808 N N   . THR A 363 ? 1.2867 0.4869 0.7955 -0.2059 0.3409  0.0361  363 THR A N   
2809 C CA  . THR A 363 ? 1.2965 0.4812 0.7913 -0.2089 0.3500  0.0489  363 THR A CA  
2810 C C   . THR A 363 ? 1.3253 0.5188 0.8657 -0.2055 0.3502  0.0526  363 THR A C   
2811 O O   . THR A 363 ? 1.2979 0.5094 0.8831 -0.2009 0.3521  0.0413  363 THR A O   
2812 C CB  . THR A 363 ? 1.3167 0.4935 0.7964 -0.2098 0.3720  0.0441  363 THR A CB  
2813 O OG1 . THR A 363 ? 1.2875 0.4814 0.8100 -0.2046 0.3854  0.0313  363 THR A OG1 
2814 C CG2 . THR A 363 ? 1.3902 0.5541 0.8224 -0.2132 0.3725  0.0398  363 THR A CG2 
2815 N N   . SER A 364 ? 1.3170 0.4980 0.8455 -0.2080 0.3481  0.0686  364 SER A N   
2816 C CA  . SER A 364 ? 1.3025 0.4875 0.8706 -0.2050 0.3465  0.0741  364 SER A CA  
2817 C C   . SER A 364 ? 1.2871 0.4835 0.8954 -0.2028 0.3634  0.0639  364 SER A C   
2818 O O   . SER A 364 ? 1.2885 0.4926 0.9376 -0.1999 0.3615  0.0627  364 SER A O   
2819 C CB  . SER A 364 ? 1.3398 0.5084 0.8850 -0.2086 0.3436  0.0947  364 SER A CB  
2820 O OG  . SER A 364 ? 1.3709 0.5292 0.8816 -0.2137 0.3563  0.0989  364 SER A OG  
2821 N N   . ASP A 365 ? 1.2920 0.4897 0.8896 -0.2041 0.3799  0.0565  365 ASP A N   
2822 C CA  . ASP A 365 ? 1.2785 0.4892 0.9120 -0.2027 0.3966  0.0478  365 ASP A CA  
2823 C C   . ASP A 365 ? 1.2387 0.4717 0.9024 -0.1986 0.3988  0.0298  365 ASP A C   
2824 O O   . ASP A 365 ? 1.2820 0.5292 0.9744 -0.1978 0.4132  0.0219  365 ASP A O   
2825 C CB  . ASP A 365 ? 1.3095 0.5096 0.9161 -0.2061 0.4154  0.0519  365 ASP A CB  
2826 C CG  . ASP A 365 ? 1.4109 0.6040 0.9781 -0.2063 0.4204  0.0458  365 ASP A CG  
2827 O OD1 . ASP A 365 ? 1.3950 0.5865 0.9454 -0.2058 0.4063  0.0430  365 ASP A OD1 
2828 O OD2 . ASP A 365 ? 1.3858 0.5742 0.9384 -0.2071 0.4385  0.0439  365 ASP A OD2 
2829 N N   . GLY A 366 ? 1.2255 0.4637 0.8841 -0.1966 0.3845  0.0240  366 GLY A N   
2830 C CA  . GLY A 366 ? 1.2001 0.4618 0.8892 -0.1930 0.3843  0.0079  366 GLY A CA  
2831 C C   . GLY A 366 ? 1.2563 0.5180 0.9218 -0.1925 0.3922  0.0006  366 GLY A C   
2832 O O   . GLY A 366 ? 1.2375 0.5202 0.9321 -0.1894 0.3983  -0.0118 366 GLY A O   
2833 N N   . GLY A 367 ? 1.2308 0.4698 0.8449 -0.1955 0.3923  0.0077  367 GLY A N   
2834 C CA  . GLY A 367 ? 1.2846 0.5185 0.8721 -0.1950 0.4000  0.0008  367 GLY A CA  
2835 C C   . GLY A 367 ? 1.2178 0.4464 0.7760 -0.1964 0.3811  0.0005  367 GLY A C   
2836 O O   . GLY A 367 ? 1.2363 0.4716 0.7984 -0.1963 0.3605  0.0051  367 GLY A O   
2837 N N   . VAL A 368 ? 1.2284 0.4488 0.7584 -0.1963 0.3872  -0.0053 368 VAL A N   
2838 C CA  . VAL A 368 ? 1.3205 0.5388 0.8215 -0.1975 0.3692  -0.0071 368 VAL A CA  
2839 C C   . VAL A 368 ? 1.2792 0.4622 0.7175 -0.2056 0.3731  0.0014  368 VAL A C   
2840 O O   . VAL A 368 ? 1.3087 0.4766 0.7290 -0.2065 0.3911  0.0035  368 VAL A O   
2841 C CB  . VAL A 368 ? 1.2019 0.4377 0.7184 -0.1917 0.3707  -0.0209 368 VAL A CB  
2842 C CG1 . VAL A 368 ? 1.1504 0.4253 0.7277 -0.1848 0.3639  -0.0290 368 VAL A CG1 
2843 C CG2 . VAL A 368 ? 1.2237 0.4443 0.7269 -0.1902 0.3970  -0.0254 368 VAL A CG2 
2844 N N   . TYR A 369 ? 1.2867 0.4647 0.6942 -0.2100 0.3530  0.0049  369 TYR A N   
2845 C CA  . TYR A 369 ? 1.3825 0.5313 0.7293 -0.2184 0.3536  0.0110  369 TYR A CA  
2846 C C   . TYR A 369 ? 1.3779 0.5257 0.6984 -0.2224 0.3350  0.0079  369 TYR A C   
2847 O O   . TYR A 369 ? 1.4223 0.5953 0.7685 -0.2192 0.3146  0.0068  369 TYR A O   
2848 C CB  . TYR A 369 ? 1.3583 0.4996 0.6873 -0.2233 0.3467  0.0263  369 TYR A CB  
2849 C CG  . TYR A 369 ? 1.4054 0.5243 0.6895 -0.2281 0.3587  0.0294  369 TYR A CG  
2850 C CD1 . TYR A 369 ? 1.4193 0.5326 0.7110 -0.2246 0.3824  0.0255  369 TYR A CD1 
2851 C CD2 . TYR A 369 ? 1.4380 0.5433 0.6728 -0.2367 0.3460  0.0361  369 TYR A CD2 
2852 C CE1 . TYR A 369 ? 1.4616 0.5549 0.7127 -0.2290 0.3937  0.0278  369 TYR A CE1 
2853 C CE2 . TYR A 369 ? 1.4869 0.5728 0.6817 -0.2417 0.3566  0.0376  369 TYR A CE2 
2854 C CZ  . TYR A 369 ? 1.4937 0.5730 0.6966 -0.2376 0.3807  0.0333  369 TYR A CZ  
2855 O OH  . TYR A 369 ? 1.6173 0.6780 0.7809 -0.2426 0.3917  0.0345  369 TYR A OH  
2856 N N   . TRP A 370 ? 1.3685 0.4917 0.6399 -0.2281 0.3409  0.0050  370 TRP A N   
2857 C CA  . TRP A 370 ? 1.5345 0.6509 0.7721 -0.2347 0.3239  0.0032  370 TRP A CA  
2858 C C   . TRP A 370 ? 1.6129 0.7009 0.7928 -0.2419 0.3299  0.0022  370 TRP A C   
2859 O O   . TRP A 370 ? 1.5333 0.6072 0.7026 -0.2403 0.3496  0.0006  370 TRP A O   
2860 C CB  . TRP A 370 ? 1.3441 0.4761 0.6080 -0.2276 0.3225  -0.0105 370 TRP A CB  
2861 C CG  . TRP A 370 ? 1.3494 0.4721 0.6227 -0.2208 0.3489  -0.0210 370 TRP A CG  
2862 C CD1 . TRP A 370 ? 1.3922 0.4823 0.6227 -0.2241 0.3667  -0.0258 370 TRP A CD1 
2863 C CD2 . TRP A 370 ? 1.3113 0.4593 0.6407 -0.2094 0.3609  -0.0281 370 TRP A CD2 
2864 N NE1 . TRP A 370 ? 1.3827 0.4765 0.6401 -0.2141 0.3893  -0.0345 370 TRP A NE1 
2865 C CE2 . TRP A 370 ? 1.3328 0.4629 0.6510 -0.2056 0.3859  -0.0356 370 TRP A CE2 
2866 C CE3 . TRP A 370 ? 1.2625 0.4470 0.6499 -0.2023 0.3531  -0.0289 370 TRP A CE3 
2867 C CZ2 . TRP A 370 ? 1.3057 0.4555 0.6696 -0.1951 0.4027  -0.0424 370 TRP A CZ2 
2868 C CZ3 . TRP A 370 ? 1.2365 0.4396 0.6679 -0.1932 0.3696  -0.0367 370 TRP A CZ3 
2869 C CH2 . TRP A 370 ? 1.2575 0.4443 0.6774 -0.1897 0.3939  -0.0426 370 TRP A CH2 
2870 N N   . GLU A 371 ? 1.5719 0.6526 0.7149 -0.2505 0.3120  0.0028  371 GLU A N   
2871 C CA  . GLU A 371 ? 1.6337 0.6878 0.7215 -0.2590 0.3146  0.0002  371 GLU A CA  
2872 C C   . GLU A 371 ? 1.5906 0.6218 0.6661 -0.2551 0.3380  -0.0144 371 GLU A C   
2873 O O   . GLU A 371 ? 1.4922 0.5268 0.5871 -0.2498 0.3421  -0.0228 371 GLU A O   
2874 C CB  . GLU A 371 ? 1.6482 0.7025 0.7040 -0.2696 0.2887  0.0028  371 GLU A CB  
2875 C CG  . GLU A 371 ? 1.6925 0.7667 0.7503 -0.2744 0.2661  0.0188  371 GLU A CG  
2876 C CD  . GLU A 371 ? 1.7148 0.8166 0.8229 -0.2667 0.2585  0.0260  371 GLU A CD  
2877 O OE1 . GLU A 371 ? 1.6144 0.7222 0.7593 -0.2581 0.2706  0.0181  371 GLU A OE1 
2878 O OE2 . GLU A 371 ? 1.7498 0.8679 0.8622 -0.2691 0.2403  0.0396  371 GLU A OE2 
2879 N N   . GLY A 372 ? 1.5903 0.5989 0.6350 -0.2575 0.3537  -0.0168 372 GLY A N   
2880 C CA  . GLY A 372 ? 1.5786 0.5631 0.6095 -0.2530 0.3780  -0.0299 372 GLY A CA  
2881 C C   . GLY A 372 ? 1.5702 0.5644 0.6427 -0.2405 0.4023  -0.0326 372 GLY A C   
2882 O O   . GLY A 372 ? 1.6780 0.6548 0.7435 -0.2349 0.4240  -0.0427 372 GLY A O   
2883 N N   . ILE A 373 ? 1.6052 0.6266 0.7219 -0.2358 0.3994  -0.0238 373 ILE A N   
2884 C CA  . ILE A 373 ? 1.5919 0.6251 0.7503 -0.2252 0.4215  -0.0260 373 ILE A CA  
2885 C C   . ILE A 373 ? 1.5533 0.5678 0.6889 -0.2246 0.4433  -0.0271 373 ILE A C   
2886 O O   . ILE A 373 ? 1.5366 0.5558 0.6976 -0.2159 0.4652  -0.0311 373 ILE A O   
2887 C CB  . ILE A 373 ? 1.4615 0.5249 0.6692 -0.2223 0.4123  -0.0165 373 ILE A CB  
2888 C CG1 . ILE A 373 ? 1.4317 0.5128 0.6900 -0.2118 0.4316  -0.0213 373 ILE A CG1 
2889 C CG2 . ILE A 373 ? 1.4833 0.5444 0.6772 -0.2278 0.4079  -0.0040 373 ILE A CG2 
2890 C CD1 . ILE A 373 ? 1.5014 0.6119 0.8120 -0.2090 0.4223  -0.0152 373 ILE A CD1 
2891 N N   . ASP A 374 ? 1.6552 0.6511 0.7450 -0.2340 0.4371  -0.0231 374 ASP A N   
2892 C CA  . ASP A 374 ? 1.7454 0.7211 0.8072 -0.2348 0.4562  -0.0253 374 ASP A CA  
2893 C C   . ASP A 374 ? 1.7935 0.7851 0.8919 -0.2276 0.4736  -0.0198 374 ASP A C   
2894 O O   . ASP A 374 ? 1.8511 0.8371 0.9562 -0.2204 0.4968  -0.0264 374 ASP A O   
2895 C CB  . ASP A 374 ? 1.8649 0.8147 0.9019 -0.2316 0.4719  -0.0400 374 ASP A CB  
2896 C CG  . ASP A 374 ? 2.0693 0.9960 1.0719 -0.2339 0.4885  -0.0427 374 ASP A CG  
2897 O OD1 . ASP A 374 ? 2.1441 1.0760 1.1400 -0.2388 0.4874  -0.0329 374 ASP A OD1 
2898 O OD2 . ASP A 374 ? 2.2098 1.1136 1.1933 -0.2306 0.5024  -0.0540 374 ASP A OD2 
2899 N N   . GLU A 375 ? 1.7246 0.7366 0.8482 -0.2296 0.4618  -0.0072 375 GLU A N   
2900 C CA  . GLU A 375 ? 1.6349 0.6634 0.7973 -0.2239 0.4757  -0.0013 375 GLU A CA  
2901 C C   . GLU A 375 ? 1.6491 0.6873 0.8160 -0.2300 0.4622  0.0148  375 GLU A C   
2902 O O   . GLU A 375 ? 1.6299 0.6813 0.8138 -0.2317 0.4422  0.0213  375 GLU A O   
2903 C CB  . GLU A 375 ? 1.5976 0.6488 0.8141 -0.2148 0.4795  -0.0062 375 GLU A CB  
2904 C CG  . GLU A 375 ? 1.7119 0.7782 0.9674 -0.2081 0.4993  -0.0048 375 GLU A CG  
2905 C CD  . GLU A 375 ? 1.6541 0.7395 0.9545 -0.1989 0.5082  -0.0138 375 GLU A CD  
2906 O OE1 . GLU A 375 ? 1.6219 0.7058 0.9193 -0.1971 0.5014  -0.0215 375 GLU A OE1 
2907 O OE2 . GLU A 375 ? 1.7071 0.8105 1.0462 -0.1939 0.5216  -0.0125 375 GLU A OE2 
2908 N N   . PRO A 376 ? 1.7162 0.7484 0.8686 -0.2331 0.4725  0.0221  376 PRO A N   
2909 C CA  . PRO A 376 ? 1.7093 0.7506 0.8672 -0.2386 0.4606  0.0391  376 PRO A CA  
2910 C C   . PRO A 376 ? 1.6134 0.6768 0.8275 -0.2330 0.4601  0.0450  376 PRO A C   
2911 O O   . PRO A 376 ? 1.7003 0.7729 0.9476 -0.2260 0.4762  0.0383  376 PRO A O   
2912 C CB  . PRO A 376 ? 1.6584 0.6888 0.7895 -0.2426 0.4756  0.0439  376 PRO A CB  
2913 C CG  . PRO A 376 ? 1.6845 0.6952 0.7827 -0.2413 0.4897  0.0287  376 PRO A CG  
2914 C CD  . PRO A 376 ? 1.6518 0.6678 0.7785 -0.2322 0.4944  0.0159  376 PRO A CD  
2915 N N   . LEU A 377 ? 1.5955 0.6678 0.8208 -0.2363 0.4412  0.0579  377 LEU A N   
2916 C CA  . LEU A 377 ? 1.5720 0.6623 0.8486 -0.2322 0.4385  0.0644  377 LEU A CA  
2917 C C   . LEU A 377 ? 1.6201 0.7107 0.9012 -0.2354 0.4452  0.0790  377 LEU A C   
2918 O O   . LEU A 377 ? 1.6037 0.6836 0.8477 -0.2419 0.4445  0.0879  377 LEU A O   
2919 C CB  . LEU A 377 ? 1.5645 0.6638 0.8541 -0.2326 0.4142  0.0699  377 LEU A CB  
2920 C CG  . LEU A 377 ? 1.4899 0.5929 0.7813 -0.2297 0.4055  0.0570  377 LEU A CG  
2921 C CD1 . LEU A 377 ? 1.4653 0.5753 0.7582 -0.2318 0.3802  0.0647  377 LEU A CD1 
2922 C CD2 . LEU A 377 ? 1.5017 0.6196 0.8401 -0.2217 0.4171  0.0450  377 LEU A CD2 
2923 N N   . ALA A 378 ? 1.6059 0.7099 0.9338 -0.2313 0.4515  0.0813  378 ALA A N   
2924 C CA  . ALA A 378 ? 1.6094 0.7146 0.9470 -0.2344 0.4585  0.0951  378 ALA A CA  
2925 C C   . ALA A 378 ? 1.5626 0.6653 0.8911 -0.2394 0.4399  0.1131  378 ALA A C   
2926 O O   . ALA A 378 ? 1.5509 0.6541 0.8734 -0.2394 0.4214  0.1144  378 ALA A O   
2927 C CB  . ALA A 378 ? 1.5210 0.6416 0.9127 -0.2297 0.4678  0.0923  378 ALA A CB  
2928 N N   . PRO A 379 ? 1.5310 0.7429 0.7422 -0.3712 0.3604  0.0519  379 PRO A N   
2929 C CA  . PRO A 379 ? 1.5616 0.7632 0.7501 -0.3751 0.3347  0.0834  379 PRO A CA  
2930 C C   . PRO A 379 ? 1.5048 0.7388 0.7556 -0.3591 0.3256  0.0972  379 PRO A C   
2931 O O   . PRO A 379 ? 1.4660 0.7157 0.7664 -0.3481 0.3463  0.0833  379 PRO A O   
2932 C CB  . PRO A 379 ? 1.6281 0.7899 0.7775 -0.3842 0.3531  0.0842  379 PRO A CB  
2933 C CG  . PRO A 379 ? 1.6471 0.7906 0.7803 -0.3898 0.3842  0.0540  379 PRO A CG  
2934 C CD  . PRO A 379 ? 1.6120 0.7952 0.8072 -0.3764 0.3935  0.0343  379 PRO A CD  
2935 N N   . GLY A 380 ? 1.5036 0.7459 0.7524 -0.3583 0.2941  0.1247  380 GLY A N   
2936 C CA  . GLY A 380 ? 1.4579 0.7250 0.7630 -0.3431 0.2857  0.1400  380 GLY A CA  
2937 C C   . GLY A 380 ? 1.4342 0.7372 0.7912 -0.3305 0.2851  0.1274  380 GLY A C   
2938 O O   . GLY A 380 ? 1.4889 0.8092 0.8956 -0.3170 0.2856  0.1330  380 GLY A O   
2939 N N   . VAL A 381 ? 1.4398 0.7517 0.7856 -0.3346 0.2850  0.1102  381 VAL A N   
2940 C CA  . VAL A 381 ? 1.3091 0.6534 0.6992 -0.3234 0.2831  0.0989  381 VAL A CA  
2941 C C   . VAL A 381 ? 1.3106 0.6636 0.6899 -0.3261 0.2519  0.1205  381 VAL A C   
2942 O O   . VAL A 381 ? 1.3577 0.6963 0.6880 -0.3403 0.2378  0.1253  381 VAL A O   
2943 C CB  . VAL A 381 ? 1.3249 0.6751 0.7163 -0.3247 0.3036  0.0670  381 VAL A CB  
2944 C CG1 . VAL A 381 ? 1.3269 0.7088 0.7584 -0.3141 0.2985  0.0578  381 VAL A CG1 
2945 C CG2 . VAL A 381 ? 1.4036 0.7489 0.8165 -0.3213 0.3335  0.0477  381 VAL A CG2 
2946 N N   . THR A 382 ? 1.3701 0.7445 0.7951 -0.3132 0.2414  0.1335  382 THR A N   
2947 C CA  . THR A 382 ? 1.3436 0.7297 0.7711 -0.3138 0.2129  0.1557  382 THR A CA  
2948 C C   . THR A 382 ? 1.2103 0.6219 0.6662 -0.3064 0.2158  0.1380  382 THR A C   
2949 O O   . THR A 382 ? 1.2496 0.6724 0.7332 -0.2975 0.2380  0.1124  382 THR A O   
2950 C CB  . THR A 382 ? 1.2819 0.6710 0.7435 -0.3035 0.1999  0.1861  382 THR A CB  
2951 O OG1 . THR A 382 ? 1.2218 0.6193 0.7315 -0.2875 0.2223  0.1733  382 THR A OG1 
2952 C CG2 . THR A 382 ? 1.3195 0.6835 0.7471 -0.3127 0.1882  0.2110  382 THR A CG2 
2953 N N   . ILE A 383 ? 1.2659 0.6865 0.7156 -0.3108 0.1916  0.1532  383 ILE A N   
2954 C CA  . ILE A 383 ? 1.2636 0.7064 0.7343 -0.3057 0.1917  0.1392  383 ILE A CA  
2955 C C   . ILE A 383 ? 1.2537 0.7203 0.7711 -0.2919 0.1712  0.1611  383 ILE A C   
2956 O O   . ILE A 383 ? 1.3587 0.8235 0.8698 -0.2974 0.1446  0.1909  383 ILE A O   
2957 C CB  . ILE A 383 ? 1.3211 0.7579 0.7451 -0.3218 0.1821  0.1306  383 ILE A CB  
2958 C CG1 . ILE A 383 ? 1.3231 0.7392 0.7094 -0.3302 0.2039  0.1063  383 ILE A CG1 
2959 C CG2 . ILE A 383 ? 1.2577 0.7174 0.7057 -0.3158 0.1827  0.1175  383 ILE A CG2 
2960 C CD1 . ILE A 383 ? 1.3604 0.7621 0.6949 -0.3468 0.1976  0.0967  383 ILE A CD1 
2961 N N   . THR A 384 ? 1.1709 0.6637 0.7400 -0.2714 0.1817  0.1455  384 THR A N   
2962 C CA  . THR A 384 ? 1.2495 0.7703 0.8691 -0.2540 0.1662  0.1595  384 THR A CA  
2963 C C   . THR A 384 ? 1.2264 0.7670 0.8476 -0.2541 0.1599  0.1458  384 THR A C   
2964 O O   . THR A 384 ? 1.2230 0.7676 0.8435 -0.2507 0.1780  0.1177  384 THR A O   
2965 C CB  . THR A 384 ? 1.1395 0.6691 0.8096 -0.2318 0.1837  0.1521  384 THR A CB  
2966 O OG1 . THR A 384 ? 1.2962 0.8054 0.9649 -0.2323 0.1902  0.1655  384 THR A OG1 
2967 C CG2 . THR A 384 ? 1.1373 0.6913 0.8579 -0.2137 0.1725  0.1663  384 THR A CG2 
2968 N N   . SER A 385 ? 1.2487 0.8014 0.8740 -0.2583 0.1336  0.1669  385 SER A N   
2969 C CA  . SER A 385 ? 1.2795 0.8489 0.9049 -0.2602 0.1265  0.1562  385 SER A CA  
2970 C C   . SER A 385 ? 1.2208 0.8141 0.8976 -0.2365 0.1406  0.1409  385 SER A C   
2971 O O   . SER A 385 ? 1.1635 0.7590 0.8740 -0.2196 0.1543  0.1394  385 SER A O   
2972 C CB  . SER A 385 ? 1.3758 0.9545 1.0017 -0.2705 0.0931  0.1848  385 SER A CB  
2973 O OG  . SER A 385 ? 1.4007 0.9992 1.0857 -0.2535 0.0826  0.2099  385 SER A OG  
2974 N N   . TRP A 386 ? 1.1976 0.8050 0.8756 -0.2365 0.1377  0.1291  386 TRP A N   
2975 C CA  . TRP A 386 ? 1.2232 0.8500 0.9432 -0.2155 0.1494  0.1160  386 TRP A CA  
2976 C C   . TRP A 386 ? 1.2419 0.8859 1.0140 -0.2001 0.1398  0.1399  386 TRP A C   
2977 O O   . TRP A 386 ? 1.2954 0.9478 1.1023 -0.1807 0.1541  0.1316  386 TRP A O   
2978 C CB  . TRP A 386 ? 1.1984 0.8333 0.9043 -0.2200 0.1493  0.0988  386 TRP A CB  
2979 C CG  . TRP A 386 ? 1.2119 0.8586 0.9211 -0.2289 0.1254  0.1177  386 TRP A CG  
2980 C CD1 . TRP A 386 ? 1.2236 0.8592 0.8926 -0.2526 0.1058  0.1290  386 TRP A CD1 
2981 C CD2 . TRP A 386 ? 1.2438 0.9137 0.9986 -0.2160 0.1182  0.1280  386 TRP A CD2 
2982 N NE1 . TRP A 386 ? 1.2539 0.9070 0.9434 -0.2559 0.0839  0.1461  386 TRP A NE1 
2983 C CE2 . TRP A 386 ? 1.2763 0.9520 1.0219 -0.2329 0.0923  0.1460  386 TRP A CE2 
2984 C CE3 . TRP A 386 ? 1.1987 0.8821 0.9992 -0.1927 0.1322  0.1237  386 TRP A CE3 
2985 C CZ2 . TRP A 386 ? 1.2262 0.9249 1.0143 -0.2267 0.0802  0.1604  386 TRP A CZ2 
2986 C CZ3 . TRP A 386 ? 1.1791 0.8820 1.0178 -0.1857 0.1233  0.1375  386 TRP A CZ3 
2987 C CH2 . TRP A 386 ? 1.2163 0.9288 1.0525 -0.2023 0.0976  0.1560  386 TRP A CH2 
2988 N N   . LYS A 387 ? 1.2639 0.9113 1.0420 -0.2088 0.1163  0.1700  387 LYS A N   
2989 C CA  . LYS A 387 ? 1.2881 0.9519 1.1235 -0.1941 0.1081  0.1970  387 LYS A CA  
2990 C C   . LYS A 387 ? 1.3703 1.0227 1.2279 -0.1810 0.1216  0.2059  387 LYS A C   
2991 O O   . LYS A 387 ? 1.4382 1.1000 1.3444 -0.1687 0.1169  0.2313  387 LYS A O   
2992 C CB  . LYS A 387 ? 1.3169 0.9902 1.1553 -0.2093 0.0743  0.2287  387 LYS A CB  
2993 C CG  . LYS A 387 ? 1.3335 1.0213 1.1649 -0.2201 0.0594  0.2248  387 LYS A CG  
2994 C CD  . LYS A 387 ? 1.3820 1.0778 1.2157 -0.2381 0.0220  0.2577  387 LYS A CD  
2995 C CE  . LYS A 387 ? 1.4644 1.1741 1.2940 -0.2501 0.0068  0.2540  387 LYS A CE  
2996 N NZ  . LYS A 387 ? 1.4372 1.1732 1.3310 -0.2285 0.0188  0.2529  387 LYS A NZ  
2997 N N   . ASN A 388 ? 1.3576 0.9894 1.1838 -0.1835 0.1392  0.1860  388 ASN A N   
2998 C CA  . ASN A 388 ? 1.3099 0.9267 1.1514 -0.1735 0.1536  0.1916  388 ASN A CA  
2999 C C   . ASN A 388 ? 1.4168 1.0294 1.2665 -0.1793 0.1340  0.2278  388 ASN A C   
3000 O O   . ASN A 388 ? 1.4351 1.0525 1.3325 -0.1644 0.1348  0.2502  388 ASN A O   
3001 C CB  . ASN A 388 ? 1.2899 0.9114 1.1779 -0.1495 0.1738  0.1855  388 ASN A CB  
3002 C CG  . ASN A 388 ? 1.3503 0.9499 1.2404 -0.1415 0.1954  0.1774  388 ASN A CG  
3003 O OD1 . ASN A 388 ? 1.3380 0.9223 1.1928 -0.1522 0.2025  0.1609  388 ASN A OD1 
3004 N ND2 . ASN A 388 ? 1.4451 1.0412 1.3778 -0.1233 0.2077  0.1891  388 ASN A ND2 
3005 N N   . LYS A 389 ? 1.4347 1.0356 1.2355 -0.2018 0.1169  0.2341  389 LYS A N   
3006 C CA  . LYS A 389 ? 1.4702 1.0629 1.2664 -0.2113 0.0943  0.2688  389 LYS A CA  
3007 C C   . LYS A 389 ? 1.4790 1.0423 1.2053 -0.2341 0.0933  0.2618  389 LYS A C   
3008 O O   . LYS A 389 ? 1.4337 0.9893 1.1163 -0.2467 0.1010  0.2358  389 LYS A O   
3009 C CB  . LYS A 389 ? 1.4920 1.1062 1.3076 -0.2181 0.0606  0.2966  389 LYS A CB  
3010 C CG  . LYS A 389 ? 1.5032 1.1465 1.3929 -0.1961 0.0630  0.3067  389 LYS A CG  
3011 C CD  . LYS A 389 ? 1.5912 1.2578 1.5026 -0.2056 0.0284  0.3336  389 LYS A CD  
3012 C CE  . LYS A 389 ? 1.5685 1.2639 1.5551 -0.1839 0.0356  0.3407  389 LYS A CE  
3013 N NZ  . LYS A 389 ? 1.4756 1.1965 1.4883 -0.1944 0.0022  0.3652  389 LYS A NZ  
3014 N N   . GLU A 390 ? 1.6080 1.1527 1.3246 -0.2389 0.0859  0.2858  390 GLU A N   
3015 C CA  . GLU A 390 ? 1.6416 1.1537 1.2879 -0.2622 0.0838  0.2842  390 GLU A CA  
3016 C C   . GLU A 390 ? 1.6557 1.1647 1.2531 -0.2860 0.0575  0.2887  390 GLU A C   
3017 O O   . GLU A 390 ? 1.6997 1.2220 1.3117 -0.2910 0.0247  0.3179  390 GLU A O   
3018 C CB  . GLU A 390 ? 1.7222 1.2151 1.3686 -0.2630 0.0756  0.3155  390 GLU A CB  
3019 C CG  . GLU A 390 ? 1.7871 1.2735 1.4699 -0.2433 0.1051  0.3086  390 GLU A CG  
3020 C CD  . GLU A 390 ? 1.8310 1.2934 1.4738 -0.2505 0.1356  0.2760  390 GLU A CD  
3021 O OE1 . GLU A 390 ? 1.7332 1.1745 1.3137 -0.2724 0.1339  0.2680  390 GLU A OE1 
3022 O OE2 . GLU A 390 ? 1.9199 1.3829 1.5939 -0.2352 0.1619  0.2584  390 GLU A OE2 
3023 N N   . TRP A 391 ? 1.6025 1.0934 1.1441 -0.3013 0.0722  0.2601  391 TRP A N   
3024 C CA  . TRP A 391 ? 1.7113 1.1946 1.2018 -0.3242 0.0538  0.2572  391 TRP A CA  
3025 C C   . TRP A 391 ? 1.7685 1.2065 1.1748 -0.3504 0.0575  0.2544  391 TRP A C   
3026 O O   . TRP A 391 ? 1.6930 1.1169 1.0863 -0.3459 0.0876  0.2316  391 TRP A O   
3027 C CB  . TRP A 391 ? 1.6065 1.1069 1.1059 -0.3186 0.0709  0.2240  391 TRP A CB  
3028 C CG  . TRP A 391 ? 1.6881 1.1754 1.1310 -0.3426 0.0579  0.2169  391 TRP A CG  
3029 C CD1 . TRP A 391 ? 1.7018 1.2059 1.1517 -0.3501 0.0288  0.2300  391 TRP A CD1 
3030 C CD2 . TRP A 391 ? 1.7890 1.2406 1.1600 -0.3631 0.0758  0.1948  391 TRP A CD2 
3031 N NE1 . TRP A 391 ? 1.7740 1.2532 1.1563 -0.3750 0.0264  0.2164  391 TRP A NE1 
3032 C CE2 . TRP A 391 ? 1.8148 1.2621 1.1492 -0.3815 0.0561  0.1938  391 TRP A CE2 
3033 C CE3 . TRP A 391 ? 1.7809 1.2134 1.1290 -0.3609 0.1057  0.1711  391 TRP A CE3 
3034 C CZ2 . TRP A 391 ? 1.8631 1.2849 1.1371 -0.3965 0.0674  0.1684  391 TRP A CZ2 
3035 C CZ3 . TRP A 391 ? 1.8347 1.2449 1.1283 -0.3749 0.1166  0.1476  391 TRP A CZ3 
3036 C CH2 . TRP A 391 ? 1.8430 1.2462 1.0987 -0.3922 0.0985  0.1458  391 TRP A CH2 
3037 N N   . ARG A 392 ? 1.8900 1.3174 1.2533 -0.3702 0.0253  0.2714  392 ARG A N   
3038 C CA  . ARG A 392 ? 2.0992 1.4923 1.3881 -0.3892 0.0253  0.2615  392 ARG A CA  
3039 C C   . ARG A 392 ? 2.2034 1.5877 1.4433 -0.4091 0.0149  0.2455  392 ARG A C   
3040 O O   . ARG A 392 ? 2.1780 1.5827 1.4376 -0.4130 -0.0084 0.2565  392 ARG A O   
3041 C CB  . ARG A 392 ? 2.2633 1.6414 1.5326 -0.3979 -0.0049 0.2961  392 ARG A CB  
3042 C CG  . ARG A 392 ? 2.1956 1.5752 1.5056 -0.3796 0.0073  0.3121  392 ARG A CG  
3043 C CD  . ARG A 392 ? 2.2702 1.6283 1.5483 -0.3897 -0.0182 0.3416  392 ARG A CD  
3044 N NE  . ARG A 392 ? 2.3331 1.7048 1.6189 -0.3996 -0.0662 0.3753  392 ARG A NE  
3045 C CZ  . ARG A 392 ? 2.4203 1.7794 1.6857 -0.4091 -0.0982 0.4059  392 ARG A CZ  
3046 N NH1 . ARG A 392 ? 2.4384 1.7681 1.6702 -0.4100 -0.0861 0.4080  392 ARG A NH1 
3047 N NH2 . ARG A 392 ? 2.4346 1.8120 1.7165 -0.4181 -0.1441 0.4357  392 ARG A NH2 
3048 N N   . PRO A 393 ? 2.3221 1.6743 1.4997 -0.4222 0.0330  0.2195  393 PRO A N   
3049 C CA  . PRO A 393 ? 2.3757 1.7132 1.5037 -0.4415 0.0271  0.2015  393 PRO A CA  
3050 C C   . PRO A 393 ? 2.5325 1.8589 1.6216 -0.4653 -0.0194 0.2275  393 PRO A C   
3051 O O   . PRO A 393 ? 2.5829 1.8921 1.6250 -0.4853 -0.0284 0.2146  393 PRO A O   
3052 C CB  . PRO A 393 ? 2.4173 1.7178 1.4928 -0.4481 0.0603  0.1708  393 PRO A CB  
3053 C CG  . PRO A 393 ? 2.3686 1.6787 1.4866 -0.4266 0.0906  0.1652  393 PRO A CG  
3054 C CD  . PRO A 393 ? 2.3406 1.6697 1.4992 -0.4175 0.0661  0.2014  393 PRO A CD  
3055 N N   . GLN A 394 ? 2.6510 1.9863 1.7611 -0.4641 -0.0500 0.2643  394 GLN A N   
3056 C CA  . GLN A 394 ? 2.6953 2.0244 1.7773 -0.4864 -0.0994 0.2927  394 GLN A CA  
3057 C C   . GLN A 394 ? 2.6535 2.0234 1.7947 -0.4834 -0.1304 0.3156  394 GLN A C   
3058 O O   . GLN A 394 ? 2.7046 2.0729 1.8248 -0.5050 -0.1723 0.3343  394 GLN A O   
3059 C CB  . GLN A 394 ? 2.7686 2.0859 1.8442 -0.4875 -0.1201 0.3233  394 GLN A CB  
3060 C CG  . GLN A 394 ? 2.9347 2.2020 1.9312 -0.5020 -0.1038 0.3069  394 GLN A CG  
3061 C CD  . GLN A 394 ? 2.8497 2.1083 1.8526 -0.4844 -0.0500 0.2762  394 GLN A CD  
3062 O OE1 . GLN A 394 ? 2.7014 1.9914 1.7693 -0.4607 -0.0274 0.2705  394 GLN A OE1 
3063 N NE2 . GLN A 394 ? 2.9967 2.2116 1.9337 -0.4970 -0.0295 0.2563  394 GLN A NE2 
3064 N N   . ASP A 395 ? 2.5443 1.9494 1.7598 -0.4584 -0.1112 0.3145  395 ASP A N   
3065 C CA  . ASP A 395 ? 2.4846 1.9279 1.7620 -0.4539 -0.1351 0.3343  395 ASP A CA  
3066 C C   . ASP A 395 ? 2.4587 1.9012 1.7125 -0.4652 -0.1266 0.3071  395 ASP A C   
3067 O O   . ASP A 395 ? 2.4518 1.8712 1.6604 -0.4677 -0.0932 0.2703  395 ASP A O   
3068 C CB  . ASP A 395 ? 2.3423 1.8201 1.7098 -0.4217 -0.1153 0.3420  395 ASP A CB  
3069 C CG  . ASP A 395 ? 2.3662 1.8397 1.7560 -0.4093 -0.1158 0.3659  395 ASP A CG  
3070 O OD1 . ASP A 395 ? 2.4316 1.8823 1.7755 -0.4239 -0.1371 0.3802  395 ASP A OD1 
3071 O OD2 . ASP A 395 ? 2.1949 1.6926 1.6538 -0.3801 -0.0930 0.3638  395 ASP A OD2 
3072 N N   . GLU A 396 ? 2.4335 1.9030 1.7246 -0.4709 -0.1569 0.3263  396 GLU A N   
3073 C CA  . GLU A 396 ? 2.4133 1.8898 1.6978 -0.4761 -0.1477 0.2998  396 GLU A CA  
3074 C C   . GLU A 396 ? 2.2682 1.7792 1.6226 -0.4420 -0.1093 0.2741  396 GLU A C   
3075 O O   . GLU A 396 ? 2.2534 1.7620 1.5928 -0.4432 -0.0891 0.2448  396 GLU A O   
3076 C CB  . GLU A 396 ? 2.4907 1.9894 1.7979 -0.4918 -0.1941 0.3242  396 GLU A CB  
3077 C CG  . GLU A 396 ? 2.5249 2.0230 1.8129 -0.5028 -0.1872 0.2980  396 GLU A CG  
3078 C CD  . GLU A 396 ? 2.4119 1.9357 1.7320 -0.5178 -0.2327 0.3223  396 GLU A CD  
3079 O OE1 . GLU A 396 ? 2.3606 1.9147 1.7417 -0.5119 -0.2658 0.3594  396 GLU A OE1 
3080 O OE2 . GLU A 396 ? 2.3732 1.8869 1.6607 -0.5357 -0.2348 0.3049  396 GLU A OE2 
3081 N N   . GLU A 397 ? 2.1146 1.6542 1.5415 -0.4126 -0.0990 0.2846  397 GLU A N   
3082 C CA  . GLU A 397 ? 1.9282 1.4953 1.4155 -0.3810 -0.0636 0.2615  397 GLU A CA  
3083 C C   . GLU A 397 ? 1.8467 1.3862 1.2864 -0.3803 -0.0233 0.2245  397 GLU A C   
3084 O O   . GLU A 397 ? 1.8590 1.3742 1.2700 -0.3814 -0.0090 0.2230  397 GLU A O   
3085 C CB  . GLU A 397 ? 1.9138 1.5058 1.4752 -0.3534 -0.0597 0.2811  397 GLU A CB  
3086 C CG  . GLU A 397 ? 1.9330 1.5554 1.5562 -0.3502 -0.0958 0.3204  397 GLU A CG  
3087 C CD  . GLU A 397 ? 1.9657 1.6281 1.6657 -0.3291 -0.0894 0.3173  397 GLU A CD  
3088 O OE1 . GLU A 397 ? 1.8863 1.5531 1.5971 -0.3117 -0.0550 0.2867  397 GLU A OE1 
3089 O OE2 . GLU A 397 ? 1.9975 1.6863 1.7480 -0.3303 -0.1190 0.3466  397 GLU A OE2 
3090 N N   . PRO A 398 ? 1.7350 1.2776 1.1684 -0.3782 -0.0037 0.1955  398 PRO A N   
3091 C CA  . PRO A 398 ? 1.6623 1.1845 1.0660 -0.3739 0.0356  0.1622  398 PRO A CA  
3092 C C   . PRO A 398 ? 1.5875 1.1288 1.0471 -0.3446 0.0599  0.1551  398 PRO A C   
3093 O O   . PRO A 398 ? 1.5351 1.1094 1.0608 -0.3226 0.0569  0.1625  398 PRO A O   
3094 C CB  . PRO A 398 ? 1.6075 1.1358 1.0071 -0.3753 0.0457  0.1386  398 PRO A CB  
3095 C CG  . PRO A 398 ? 1.5937 1.1583 1.0495 -0.3672 0.0202  0.1567  398 PRO A CG  
3096 C CD  . PRO A 398 ? 1.7530 1.3179 1.2098 -0.3796 -0.0163 0.1931  398 PRO A CD  
3097 N N   . CYS A 399 ? 1.5926 1.1099 1.0238 -0.3455 0.0853  0.1404  399 CYS A N   
3098 C CA  . CYS A 399 ? 1.5461 1.0767 1.0244 -0.3214 0.1066  0.1339  399 CYS A CA  
3099 C C   . CYS A 399 ? 1.3345 0.8871 0.8515 -0.3015 0.1283  0.1077  399 CYS A C   
3100 O O   . CYS A 399 ? 1.2621 0.8333 0.8293 -0.2794 0.1378  0.1058  399 CYS A O   
3101 C CB  . CYS A 399 ? 1.5054 1.0039 0.9445 -0.3300 0.1269  0.1267  399 CYS A CB  
3102 S SG  . CYS A 399 ? 1.4593 0.9365 0.8603 -0.3375 0.1627  0.0892  399 CYS A SG  
3103 N N   . ALA A 400 ? 1.3432 0.8908 0.8350 -0.3096 0.1366  0.0878  400 ALA A N   
3104 C CA  . ALA A 400 ? 1.3051 0.8713 0.8289 -0.2922 0.1550  0.0643  400 ALA A CA  
3105 C C   . ALA A 400 ? 1.2632 0.8460 0.7974 -0.2929 0.1397  0.0670  400 ALA A C   
3106 O O   . ALA A 400 ? 1.3425 0.9098 0.8341 -0.3139 0.1285  0.0691  400 ALA A O   
3107 C CB  . ALA A 400 ? 1.3158 0.8622 0.8090 -0.2984 0.1828  0.0375  400 ALA A CB  
3108 N N   . HIS A 401 ? 1.2756 0.8862 0.8629 -0.2711 0.1401  0.0665  401 HIS A N   
3109 C CA  . HIS A 401 ? 1.1165 0.7437 0.7194 -0.2705 0.1274  0.0702  401 HIS A CA  
3110 C C   . HIS A 401 ? 1.1865 0.8011 0.7541 -0.2807 0.1394  0.0475  401 HIS A C   
3111 O O   . HIS A 401 ? 1.1939 0.8002 0.7534 -0.2751 0.1631  0.0254  401 HIS A O   
3112 C CB  . HIS A 401 ? 1.1099 0.7634 0.7720 -0.2443 0.1328  0.0705  401 HIS A CB  
3113 C CG  . HIS A 401 ? 1.1377 0.8081 0.8204 -0.2428 0.1219  0.0758  401 HIS A CG  
3114 N ND1 . HIS A 401 ? 1.0343 0.7063 0.7113 -0.2394 0.1338  0.0556  401 HIS A ND1 
3115 C CD2 . HIS A 401 ? 1.1000 0.7867 0.8122 -0.2446 0.1004  0.1000  401 HIS A CD2 
3116 C CE1 . HIS A 401 ? 1.0594 0.7464 0.7586 -0.2395 0.1213  0.0660  401 HIS A CE1 
3117 N NE2 . HIS A 401 ? 0.9952 0.6926 0.7182 -0.2429 0.1008  0.0930  401 HIS A NE2 
3118 N N   . PRO A 402 ? 1.1982 0.8109 0.7472 -0.2960 0.1237  0.0528  402 PRO A N   
3119 C CA  . PRO A 402 ? 1.0631 0.6591 0.5756 -0.3067 0.1372  0.0312  402 PRO A CA  
3120 C C   . PRO A 402 ? 1.1022 0.7103 0.6433 -0.2851 0.1613  0.0090  402 PRO A C   
3121 O O   . PRO A 402 ? 1.1640 0.7552 0.6808 -0.2881 0.1829  -0.0113 402 PRO A O   
3122 C CB  . PRO A 402 ? 1.1405 0.7408 0.6465 -0.3217 0.1128  0.0440  402 PRO A CB  
3123 C CG  . PRO A 402 ? 1.0546 0.6608 0.5683 -0.3303 0.0839  0.0735  402 PRO A CG  
3124 C CD  . PRO A 402 ? 1.1916 0.8154 0.7521 -0.3061 0.0923  0.0797  402 PRO A CD  
3125 N N   . ASN A 403 ? 1.0599 0.6947 0.6518 -0.2637 0.1590  0.0132  403 ASN A N   
3126 C CA  . ASN A 403 ? 1.1038 0.7480 0.7196 -0.2436 0.1783  -0.0058 403 ASN A CA  
3127 C C   . ASN A 403 ? 1.1180 0.7658 0.7548 -0.2271 0.1916  -0.0128 403 ASN A C   
3128 O O   . ASN A 403 ? 0.9807 0.6370 0.6398 -0.2097 0.2034  -0.0258 403 ASN A O   
3129 C CB  . ASN A 403 ? 1.1271 0.7922 0.7796 -0.2302 0.1712  0.0009  403 ASN A CB  
3130 C CG  . ASN A 403 ? 1.1450 0.8136 0.8089 -0.2141 0.1888  -0.0186 403 ASN A CG  
3131 O OD1 . ASN A 403 ? 1.0454 0.7012 0.6853 -0.2192 0.2019  -0.0355 403 ASN A OD1 
3132 N ND2 . ASN A 403 ? 1.1695 0.8532 0.8697 -0.1945 0.1903  -0.0153 403 ASN A ND2 
3133 N N   . SER A 404 ? 1.0831 0.7228 0.7115 -0.2332 0.1889  -0.0041 404 SER A N   
3134 C CA  . SER A 404 ? 1.0231 0.6636 0.6694 -0.2205 0.2018  -0.0117 404 SER A CA  
3135 C C   . SER A 404 ? 1.0332 0.6683 0.6740 -0.2173 0.2218  -0.0355 404 SER A C   
3136 O O   . SER A 404 ? 1.0373 0.6603 0.6507 -0.2293 0.2292  -0.0448 404 SER A O   
3137 C CB  . SER A 404 ? 1.0790 0.7059 0.7086 -0.2317 0.1986  -0.0003 404 SER A CB  
3138 O OG  . SER A 404 ? 1.1447 0.7487 0.7284 -0.2524 0.2045  -0.0059 404 SER A OG  
3139 N N   . ARG A 405 ? 0.9730 0.6158 0.6412 -0.2015 0.2305  -0.0447 405 ARG A N   
3140 C CA  . ARG A 405 ? 1.0126 0.6572 0.6890 -0.1944 0.2448  -0.0645 405 ARG A CA  
3141 C C   . ARG A 405 ? 0.9343 0.5767 0.6243 -0.1914 0.2550  -0.0727 405 ARG A C   
3142 O O   . ARG A 405 ? 0.9538 0.5943 0.6505 -0.1907 0.2513  -0.0644 405 ARG A O   
3143 C CB  . ARG A 405 ? 0.9463 0.6046 0.6457 -0.1767 0.2416  -0.0688 405 ARG A CB  
3144 C CG  . ARG A 405 ? 0.9316 0.5931 0.6228 -0.1790 0.2341  -0.0626 405 ARG A CG  
3145 C CD  . ARG A 405 ? 0.9547 0.6108 0.6323 -0.1831 0.2443  -0.0762 405 ARG A CD  
3146 N NE  . ARG A 405 ? 1.0093 0.6642 0.6729 -0.1905 0.2376  -0.0703 405 ARG A NE  
3147 C CZ  . ARG A 405 ? 0.9724 0.6214 0.6244 -0.1932 0.2457  -0.0803 405 ARG A CZ  
3148 N NH1 . ARG A 405 ? 0.9295 0.5750 0.5863 -0.1873 0.2611  -0.0954 405 ARG A NH1 
3149 N NH2 . ARG A 405 ? 1.0352 0.6816 0.6735 -0.2024 0.2382  -0.0741 405 ARG A NH2 
3150 N N   . PHE A 406 ? 0.8694 0.5121 0.5671 -0.1898 0.2681  -0.0886 406 PHE A N   
3151 C CA  . PHE A 406 ? 0.8537 0.5004 0.5765 -0.1841 0.2754  -0.0981 406 PHE A CA  
3152 C C   . PHE A 406 ? 0.8284 0.4878 0.5753 -0.1698 0.2744  -0.1092 406 PHE A C   
3153 O O   . PHE A 406 ? 0.9502 0.6115 0.6921 -0.1677 0.2765  -0.1130 406 PHE A O   
3154 C CB  . PHE A 406 ? 0.9610 0.5957 0.6767 -0.1974 0.2932  -0.1044 406 PHE A CB  
3155 C CG  . PHE A 406 ? 0.9752 0.6034 0.6805 -0.2032 0.3077  -0.1136 406 PHE A CG  
3156 C CD1 . PHE A 406 ? 0.9082 0.5470 0.6440 -0.1939 0.3163  -0.1258 406 PHE A CD1 
3157 C CD2 . PHE A 406 ? 0.9573 0.5662 0.6213 -0.2187 0.3128  -0.1093 406 PHE A CD2 
3158 C CE1 . PHE A 406 ? 0.8934 0.5244 0.6230 -0.1980 0.3328  -0.1335 406 PHE A CE1 
3159 C CE2 . PHE A 406 ? 1.0216 0.6189 0.6724 -0.2247 0.3296  -0.1188 406 PHE A CE2 
3160 C CZ  . PHE A 406 ? 0.9592 0.5677 0.6447 -0.2134 0.3413  -0.1309 406 PHE A CZ  
3161 N N   . CYS A 407 ? 0.7771 0.4430 0.5480 -0.1609 0.2702  -0.1139 407 CYS A N   
3162 C CA  . CYS A 407 ? 0.7954 0.4709 0.5860 -0.1479 0.2645  -0.1225 407 CYS A CA  
3163 C C   . CYS A 407 ? 0.7576 0.4383 0.5763 -0.1494 0.2685  -0.1319 407 CYS A C   
3164 O O   . CYS A 407 ? 0.7942 0.4731 0.6221 -0.1496 0.2635  -0.1322 407 CYS A O   
3165 C CB  . CYS A 407 ? 0.8524 0.5266 0.6403 -0.1364 0.2518  -0.1180 407 CYS A CB  
3166 S SG  . CYS A 407 ? 0.8461 0.5245 0.6469 -0.1220 0.2423  -0.1274 407 CYS A SG  
3167 N N   . THR A 408 ? 0.7711 0.4577 0.6061 -0.1507 0.2783  -0.1390 408 THR A N   
3168 C CA  . THR A 408 ? 0.7771 0.4707 0.6463 -0.1541 0.2847  -0.1460 408 THR A CA  
3169 C C   . THR A 408 ? 0.7870 0.4947 0.6879 -0.1441 0.2785  -0.1521 408 THR A C   
3170 O O   . THR A 408 ? 0.8240 0.5331 0.7188 -0.1376 0.2797  -0.1523 408 THR A O   
3171 C CB  . THR A 408 ? 0.8110 0.4964 0.6778 -0.1672 0.3080  -0.1470 408 THR A CB  
3172 O OG1 . THR A 408 ? 0.8775 0.5691 0.7810 -0.1714 0.3156  -0.1520 408 THR A OG1 
3173 C CG2 . THR A 408 ? 0.7605 0.4443 0.6249 -0.1662 0.3214  -0.1505 408 THR A CG2 
3174 N N   . PRO A 409 ? 0.7239 0.4419 0.6601 -0.1433 0.2706  -0.1563 409 PRO A N   
3175 C CA  . PRO A 409 ? 0.7355 0.4685 0.7068 -0.1347 0.2614  -0.1597 409 PRO A CA  
3176 C C   . PRO A 409 ? 0.8709 0.6096 0.8658 -0.1352 0.2822  -0.1612 409 PRO A C   
3177 O O   . PRO A 409 ? 0.7857 0.5201 0.7887 -0.1451 0.3046  -0.1625 409 PRO A O   
3178 C CB  . PRO A 409 ? 0.8051 0.5470 0.8111 -0.1390 0.2496  -0.1627 409 PRO A CB  
3179 C CG  . PRO A 409 ? 0.7472 0.4747 0.7242 -0.1455 0.2474  -0.1614 409 PRO A CG  
3180 C CD  . PRO A 409 ? 0.8149 0.5305 0.7600 -0.1506 0.2668  -0.1570 409 PRO A CD  
3181 N N   . ALA A 410 ? 0.7784 0.5236 0.7827 -0.1242 0.2768  -0.1607 410 ALA A N   
3182 C CA  . ALA A 410 ? 0.8508 0.5988 0.8790 -0.1229 0.2987  -0.1620 410 ALA A CA  
3183 C C   . ALA A 410 ? 0.8473 0.6108 0.9367 -0.1257 0.3075  -0.1634 410 ALA A C   
3184 O O   . ALA A 410 ? 0.8245 0.5838 0.9311 -0.1305 0.3366  -0.1653 410 ALA A O   
3185 C CB  . ALA A 410 ? 0.8066 0.5578 0.8347 -0.1094 0.2898  -0.1599 410 ALA A CB  
3186 N N   . SER A 411 ? 0.7771 0.5565 0.8997 -0.1238 0.2839  -0.1625 411 SER A N   
3187 C CA  . SER A 411 ? 0.8254 0.6241 1.0164 -0.1261 0.2886  -0.1622 411 SER A CA  
3188 C C   . SER A 411 ? 0.8446 0.6364 1.0448 -0.1396 0.3172  -0.1653 411 SER A C   
3189 O O   . SER A 411 ? 0.8259 0.6280 1.0805 -0.1415 0.3374  -0.1651 411 SER A O   
3190 C CB  . SER A 411 ? 0.7614 0.5751 0.9781 -0.1253 0.2534  -0.1607 411 SER A CB  
3191 O OG  . SER A 411 ? 0.8549 0.6564 1.0351 -0.1340 0.2437  -0.1638 411 SER A OG  
3192 N N   . GLN A 412 ? 0.8821 0.6555 1.0318 -0.1487 0.3206  -0.1670 412 GLN A N   
3193 C CA  . GLN A 412 ? 0.8684 0.6312 1.0196 -0.1622 0.3465  -0.1688 412 GLN A CA  
3194 C C   . GLN A 412 ? 0.9082 0.6530 1.0435 -0.1667 0.3832  -0.1703 412 GLN A C   
3195 O O   . GLN A 412 ? 0.9133 0.6474 1.0566 -0.1778 0.4100  -0.1720 412 GLN A O   
3196 C CB  . GLN A 412 ? 0.8025 0.5492 0.9033 -0.1700 0.3376  -0.1680 412 GLN A CB  
3197 C CG  . GLN A 412 ? 0.8190 0.5759 0.9343 -0.1695 0.3089  -0.1683 412 GLN A CG  
3198 C CD  . GLN A 412 ? 0.8072 0.5458 0.8715 -0.1742 0.3016  -0.1664 412 GLN A CD  
3199 O OE1 . GLN A 412 ? 0.9171 0.6563 0.9834 -0.1752 0.2825  -0.1673 412 GLN A OE1 
3200 N NE2 . GLN A 412 ? 0.7913 0.5118 0.8095 -0.1776 0.3166  -0.1630 412 GLN A NE2 
3201 N N   . CYS A 413 ? 0.8892 0.6267 0.9991 -0.1597 0.3866  -0.1702 413 CYS A N   
3202 C CA  . CYS A 413 ? 0.8774 0.5923 0.9663 -0.1657 0.4222  -0.1729 413 CYS A CA  
3203 C C   . CYS A 413 ? 0.9388 0.6607 1.0917 -0.1662 0.4510  -0.1748 413 CYS A C   
3204 O O   . CYS A 413 ? 0.9106 0.6591 1.1272 -0.1550 0.4406  -0.1724 413 CYS A O   
3205 C CB  . CYS A 413 ? 0.9600 0.6686 1.0218 -0.1570 0.4195  -0.1729 413 CYS A CB  
3206 S SG  . CYS A 413 ? 0.9963 0.6673 1.0109 -0.1681 0.4603  -0.1776 413 CYS A SG  
3207 N N   . PRO A 414 ? 0.9623 0.6600 1.1019 -0.1792 0.4875  -0.1780 414 PRO A N   
3208 C CA  . PRO A 414 ? 0.9477 0.6503 1.1528 -0.1787 0.5185  -0.1793 414 PRO A CA  
3209 C C   . PRO A 414 ? 0.9057 0.6040 1.1332 -0.1666 0.5333  -0.1797 414 PRO A C   
3210 O O   . PRO A 414 ? 0.8430 0.5565 1.1440 -0.1594 0.5478  -0.1777 414 PRO A O   
3211 C CB  . PRO A 414 ? 0.9337 0.5984 1.0906 -0.1879 0.5333  -0.1826 414 PRO A CB  
3212 C CG  . PRO A 414 ? 1.0551 0.6907 1.1217 -0.1947 0.5210  -0.1828 414 PRO A CG  
3213 C CD  . PRO A 414 ? 0.9660 0.6282 1.0287 -0.1925 0.4952  -0.1792 414 PRO A CD  
3214 N N   . ILE A 415 ? 0.9295 0.6070 1.0996 -0.1643 0.5284  -0.1808 415 ILE A N   
3215 C CA  . ILE A 415 ? 0.9028 0.5720 1.0892 -0.1541 0.5404  -0.1799 415 ILE A CA  
3216 C C   . ILE A 415 ? 0.9096 0.6068 1.1109 -0.1412 0.5225  -0.1779 415 ILE A C   
3217 O O   . ILE A 415 ? 0.9071 0.5910 1.0947 -0.1344 0.5254  -0.1766 415 ILE A O   
3218 C CB  . ILE A 415 ? 0.9414 0.5594 1.0539 -0.1636 0.5507  -0.1821 415 ILE A CB  
3219 C CG1 . ILE A 415 ? 1.0560 0.6606 1.0885 -0.1735 0.5270  -0.1818 415 ILE A CG1 
3220 C CG2 . ILE A 415 ? 0.9282 0.5152 1.0358 -0.1725 0.5749  -0.1858 415 ILE A CG2 
3221 C CD1 . ILE A 415 ? 1.0349 0.5939 0.9995 -0.1853 0.5322  -0.1827 415 ILE A CD1 
3222 N N   . ILE A 416 ? 0.8906 0.6176 1.1091 -0.1359 0.4845  -0.1740 416 ILE A N   
3223 C CA  . ILE A 416 ? 0.8739 0.6201 1.1005 -0.1206 0.4507  -0.1690 416 ILE A CA  
3224 C C   . ILE A 416 ? 0.8500 0.6131 1.1496 -0.1066 0.4610  -0.1641 416 ILE A C   
3225 O O   . ILE A 416 ? 0.8168 0.5989 1.1885 -0.1053 0.4702  -0.1608 416 ILE A O   
3226 C CB  . ILE A 416 ? 0.7640 0.5332 0.9964 -0.1188 0.4077  -0.1654 416 ILE A CB  
3227 C CG1 . ILE A 416 ? 0.7826 0.5594 0.9958 -0.1060 0.3746  -0.1614 416 ILE A CG1 
3228 C CG2 . ILE A 416 ? 0.7587 0.5564 1.0720 -0.1170 0.4009  -0.1614 416 ILE A CG2 
3229 C CD1 . ILE A 416 ? 0.7482 0.5009 0.8844 -0.1089 0.3748  -0.1642 416 ILE A CD1 
3230 N N   . ASP A 417 ? 0.8221 0.5788 1.1072 -0.0960 0.4600  -0.1626 417 ASP A N   
3231 C CA  . ASP A 417 ? 0.8688 0.6376 1.2215 -0.0818 0.4734  -0.1566 417 ASP A CA  
3232 C C   . ASP A 417 ? 0.8224 0.6312 1.2477 -0.0710 0.4372  -0.1460 417 ASP A C   
3233 O O   . ASP A 417 ? 0.8406 0.6612 1.2430 -0.0697 0.3956  -0.1436 417 ASP A O   
3234 C CB  . ASP A 417 ? 0.8276 0.5801 1.1458 -0.0723 0.4759  -0.1563 417 ASP A CB  
3235 C CG  . ASP A 417 ? 0.8314 0.5896 1.2164 -0.0579 0.4981  -0.1500 417 ASP A CG  
3236 O OD1 . ASP A 417 ? 0.7898 0.5275 1.1882 -0.0626 0.5429  -0.1542 417 ASP A OD1 
3237 O OD2 . ASP A 417 ? 0.8607 0.6414 1.2833 -0.0422 0.4703  -0.1398 417 ASP A OD2 
3238 N N   . PRO A 418 ? 0.8231 0.6517 1.3367 -0.0639 0.4517  -0.1389 418 PRO A N   
3239 C CA  . PRO A 418 ? 0.8423 0.7100 1.4287 -0.0556 0.4131  -0.1270 418 PRO A CA  
3240 C C   . PRO A 418 ? 0.8584 0.7358 1.4435 -0.0399 0.3786  -0.1177 418 PRO A C   
3241 O O   . PRO A 418 ? 0.9490 0.8560 1.6020 -0.0307 0.3508  -0.1050 418 PRO A O   
3242 C CB  . PRO A 418 ? 0.7319 0.6156 1.4165 -0.0522 0.4452  -0.1207 418 PRO A CB  
3243 C CG  . PRO A 418 ? 0.7428 0.5932 1.4047 -0.0507 0.4980  -0.1270 418 PRO A CG  
3244 C CD  . PRO A 418 ? 0.8067 0.6209 1.3584 -0.0643 0.5050  -0.1408 418 PRO A CD  
3245 N N   . ALA A 419 ? 0.8360 0.6879 1.3443 -0.0375 0.3791  -0.1228 419 ALA A N   
3246 C CA  . ALA A 419 ? 0.7975 0.6531 1.2940 -0.0233 0.3485  -0.1146 419 ALA A CA  
3247 C C   . ALA A 419 ? 0.8521 0.6849 1.2531 -0.0273 0.3328  -0.1219 419 ALA A C   
3248 O O   . ALA A 419 ? 0.9293 0.7549 1.3053 -0.0165 0.3190  -0.1174 419 ALA A O   
3249 C CB  . ALA A 419 ? 0.8555 0.7047 1.3861 -0.0091 0.3757  -0.1084 419 ALA A CB  
3250 N N   . TRP A 420 ? 0.8287 0.6498 1.1788 -0.0421 0.3356  -0.1319 420 TRP A N   
3251 C CA  . TRP A 420 ? 0.8800 0.6812 1.1476 -0.0458 0.3226  -0.1372 420 TRP A CA  
3252 C C   . TRP A 420 ? 0.7906 0.6007 1.0435 -0.0391 0.2780  -0.1313 420 TRP A C   
3253 O O   . TRP A 420 ? 0.8569 0.6507 1.0507 -0.0370 0.2681  -0.1329 420 TRP A O   
3254 C CB  . TRP A 420 ? 0.8990 0.6874 1.1234 -0.0627 0.3343  -0.1465 420 TRP A CB  
3255 C CG  . TRP A 420 ? 0.9161 0.7196 1.1524 -0.0695 0.3091  -0.1462 420 TRP A CG  
3256 C CD1 . TRP A 420 ? 0.8273 0.6498 1.1236 -0.0740 0.3105  -0.1447 420 TRP A CD1 
3257 C CD2 . TRP A 420 ? 0.8661 0.6644 1.0536 -0.0732 0.2812  -0.1478 420 TRP A CD2 
3258 N NE1 . TRP A 420 ? 0.8342 0.6630 1.1192 -0.0812 0.2835  -0.1459 420 TRP A NE1 
3259 C CE2 . TRP A 420 ? 0.8483 0.6611 1.0657 -0.0804 0.2663  -0.1480 420 TRP A CE2 
3260 C CE3 . TRP A 420 ? 0.8803 0.6622 1.0045 -0.0711 0.2694  -0.1488 420 TRP A CE3 
3261 C CZ2 . TRP A 420 ? 0.8754 0.6835 1.0574 -0.0856 0.2411  -0.1499 420 TRP A CZ2 
3262 C CZ3 . TRP A 420 ? 0.8976 0.6763 0.9906 -0.0751 0.2458  -0.1498 420 TRP A CZ3 
3263 C CH2 . TRP A 420 ? 0.8678 0.6579 0.9876 -0.0823 0.2324  -0.1507 420 TRP A CH2 
3264 N N   . GLU A 421 ? 0.8379 0.6711 1.1418 -0.0369 0.2515  -0.1246 421 GLU A N   
3265 C CA  . GLU A 421 ? 0.8352 0.6719 1.1229 -0.0319 0.2084  -0.1187 421 GLU A CA  
3266 C C   . GLU A 421 ? 0.8713 0.7218 1.2072 -0.0174 0.1907  -0.1054 421 GLU A C   
3267 O O   . GLU A 421 ? 0.9110 0.7641 1.2391 -0.0141 0.1521  -0.0986 421 GLU A O   
3268 C CB  . GLU A 421 ? 0.8119 0.6595 1.1094 -0.0433 0.1842  -0.1208 421 GLU A CB  
3269 C CG  . GLU A 421 ? 0.8993 0.7298 1.1394 -0.0557 0.1935  -0.1317 421 GLU A CG  
3270 C CD  . GLU A 421 ? 0.9198 0.7561 1.1629 -0.0664 0.1682  -0.1339 421 GLU A CD  
3271 O OE1 . GLU A 421 ? 0.8378 0.6962 1.1437 -0.0694 0.1564  -0.1296 421 GLU A OE1 
3272 O OE2 . GLU A 421 ? 0.9411 0.7593 1.1263 -0.0719 0.1608  -0.1396 421 GLU A OE2 
3273 N N   . SER A 422 ? 0.8761 0.7325 1.2594 -0.0092 0.2184  -0.1010 422 SER A N   
3274 C CA  . SER A 422 ? 0.9429 0.8118 1.3755 0.0062  0.2040  -0.0861 422 SER A CA  
3275 C C   . SER A 422 ? 0.9760 0.8234 1.3465 0.0157  0.1878  -0.0832 422 SER A C   
3276 O O   . SER A 422 ? 0.9856 0.8105 1.3086 0.0170  0.2143  -0.0903 422 SER A O   
3277 C CB  . SER A 422 ? 0.9031 0.7769 1.3955 0.0135  0.2451  -0.0831 422 SER A CB  
3278 O OG  . SER A 422 ? 0.9194 0.8103 1.4695 0.0046  0.2642  -0.0857 422 SER A OG  
3279 N N   . PRO A 423 ? 1.0216 0.8725 1.3878 0.0211  0.1452  -0.0728 423 PRO A N   
3280 C CA  . PRO A 423 ? 1.0624 0.8881 1.3621 0.0291  0.1317  -0.0705 423 PRO A CA  
3281 C C   . PRO A 423 ? 1.0754 0.8926 1.3865 0.0439  0.1543  -0.0638 423 PRO A C   
3282 O O   . PRO A 423 ? 1.1743 0.9672 1.4269 0.0495  0.1531  -0.0641 423 PRO A O   
3283 C CB  . PRO A 423 ? 1.0800 0.9109 1.3818 0.0304  0.0809  -0.0591 423 PRO A CB  
3284 C CG  . PRO A 423 ? 0.9990 0.8646 1.3944 0.0296  0.0704  -0.0493 423 PRO A CG  
3285 C CD  . PRO A 423 ? 0.9663 0.8425 1.3884 0.0194  0.1071  -0.0618 423 PRO A CD  
3286 N N   . GLU A 424 ? 1.0782 0.9123 1.4631 0.0503  0.1773  -0.0578 424 GLU A N   
3287 C CA  . GLU A 424 ? 1.0717 0.8951 1.4705 0.0647  0.2019  -0.0514 424 GLU A CA  
3288 C C   . GLU A 424 ? 1.0057 0.8069 1.3689 0.0591  0.2500  -0.0664 424 GLU A C   
3289 O O   . GLU A 424 ? 1.0118 0.7974 1.3739 0.0688  0.2735  -0.0639 424 GLU A O   
3290 C CB  . GLU A 424 ? 1.0709 0.9204 1.5707 0.0759  0.2056  -0.0358 424 GLU A CB  
3291 C CG  . GLU A 424 ? 1.1245 0.9814 1.6768 0.0715  0.2525  -0.0431 424 GLU A CG  
3292 C CD  . GLU A 424 ? 1.1465 1.0222 1.7204 0.0559  0.2484  -0.0507 424 GLU A CD  
3293 O OE1 . GLU A 424 ? 1.0990 0.9802 1.6410 0.0474  0.2103  -0.0523 424 GLU A OE1 
3294 O OE2 . GLU A 424 ? 1.1047 0.9866 1.7259 0.0519  0.2855  -0.0552 424 GLU A OE2 
3295 N N   . GLY A 425 ? 0.9892 0.7863 1.3213 0.0430  0.2639  -0.0812 425 GLY A N   
3296 C CA  . GLY A 425 ? 0.8610 0.6352 1.1547 0.0347  0.3052  -0.0948 425 GLY A CA  
3297 C C   . GLY A 425 ? 0.9240 0.7006 1.2741 0.0344  0.3461  -0.0965 425 GLY A C   
3298 O O   . GLY A 425 ? 0.9375 0.7368 1.3654 0.0419  0.3449  -0.0864 425 GLY A O   
3299 N N   . VAL A 426 ? 0.8612 0.6115 1.1704 0.0247  0.3837  -0.1092 426 VAL A N   
3300 C CA  . VAL A 426 ? 0.8374 0.5776 1.1817 0.0218  0.4302  -0.1139 426 VAL A CA  
3301 C C   . VAL A 426 ? 0.8872 0.5963 1.2032 0.0266  0.4593  -0.1167 426 VAL A C   
3302 O O   . VAL A 426 ? 0.8470 0.5356 1.0922 0.0203  0.4548  -0.1235 426 VAL A O   
3303 C CB  . VAL A 426 ? 0.7669 0.4964 1.0810 0.0014  0.4519  -0.1279 426 VAL A CB  
3304 C CG1 . VAL A 426 ? 0.7503 0.5101 1.1104 -0.0023 0.4321  -0.1244 426 VAL A CG1 
3305 C CG2 . VAL A 426 ? 0.7649 0.4740 0.9891 -0.0118 0.4425  -0.1379 426 VAL A CG2 
3306 N N   . PRO A 427 ? 0.8385 0.5427 1.2098 0.0375  0.4903  -0.1113 427 PRO A N   
3307 C CA  . PRO A 427 ? 0.8279 0.5040 1.1650 0.0370  0.5088  -0.1093 427 PRO A CA  
3308 C C   . PRO A 427 ? 0.8490 0.4961 1.1114 0.0086  0.5237  -0.1178 427 PRO A C   
3309 O O   . PRO A 427 ? 0.9088 0.5471 1.1800 -0.0052 0.5447  -0.1200 427 PRO A O   
3310 C CB  . PRO A 427 ? 0.8435 0.5275 1.2629 0.0508  0.5297  -0.0959 427 PRO A CB  
3311 C CG  . PRO A 427 ? 0.8344 0.5410 1.3154 0.0482  0.5368  -0.0959 427 PRO A CG  
3312 C CD  . PRO A 427 ? 0.8117 0.5400 1.2779 0.0463  0.5016  -0.1015 427 PRO A CD  
3313 N N   . ILE A 428 ? 0.5486 0.8449 0.8952 -0.0775 0.0252  -0.0283 428 ILE A N   
3314 C CA  . ILE A 428 ? 0.5433 0.8109 0.8658 -0.0718 0.0338  -0.0219 428 ILE A CA  
3315 C C   . ILE A 428 ? 0.5806 0.8585 0.8972 -0.0581 0.0345  -0.0122 428 ILE A C   
3316 O O   . ILE A 428 ? 0.6003 0.8871 0.9076 -0.0511 0.0185  -0.0064 428 ILE A O   
3317 C CB  . ILE A 428 ? 0.5148 0.7545 0.8096 -0.0723 0.0227  -0.0250 428 ILE A CB  
3318 C CG1 . ILE A 428 ? 0.6193 0.8476 0.9228 -0.0834 0.0268  -0.0377 428 ILE A CG1 
3319 C CG2 . ILE A 428 ? 0.4759 0.6918 0.7506 -0.0659 0.0287  -0.0189 428 ILE A CG2 
3320 C CD1 . ILE A 428 ? 0.5637 0.7783 0.8811 -0.0901 0.0479  -0.0376 428 ILE A CD1 
3321 N N   . GLU A 429 ? 0.5547 0.8261 0.8842 -0.0538 0.0571  -0.0143 429 GLU A N   
3322 C CA  . GLU A 429 ? 0.4542 0.7289 0.7854 -0.0384 0.0642  -0.0115 429 GLU A CA  
3323 C C   . GLU A 429 ? 0.5078 0.7455 0.8211 -0.0323 0.0742  -0.0101 429 GLU A C   
3324 O O   . GLU A 429 ? 0.5321 0.7643 0.8449 -0.0173 0.0836  -0.0068 429 GLU A O   
3325 C CB  . GLU A 429 ? 0.4162 0.7094 0.7753 -0.0341 0.0869  -0.0112 429 GLU A CB  
3326 C CG  . GLU A 429 ? 0.4974 0.8346 0.8817 -0.0385 0.0775  -0.0109 429 GLU A CG  
3327 C CD  . GLU A 429 ? 0.5182 0.8787 0.9327 -0.0329 0.0992  -0.0112 429 GLU A CD  
3328 O OE1 . GLU A 429 ? 0.5869 0.9270 0.9970 -0.0219 0.1211  -0.0104 429 GLU A OE1 
3329 O OE2 . GLU A 429 ? 0.5841 0.9822 1.0261 -0.0390 0.0957  -0.0109 429 GLU A OE2 
3330 N N   . GLY A 430 ? 0.4629 0.6742 0.7622 -0.0416 0.0738  -0.0109 430 GLY A N   
3331 C CA  . GLY A 430 ? 0.4472 0.6256 0.7309 -0.0363 0.0840  -0.0054 430 GLY A CA  
3332 C C   . GLY A 430 ? 0.4820 0.6435 0.7523 -0.0461 0.0692  -0.0079 430 GLY A C   
3333 O O   . GLY A 430 ? 0.5433 0.7077 0.8161 -0.0562 0.0633  -0.0132 430 GLY A O   
3334 N N   . ILE A 431 ? 0.3713 0.5069 0.6108 -0.0390 0.0591  -0.0029 431 ILE A N   
3335 C CA  . ILE A 431 ? 0.4269 0.5463 0.6525 -0.0450 0.0437  -0.0044 431 ILE A CA  
3336 C C   . ILE A 431 ? 0.4828 0.5496 0.6505 -0.0323 0.0467  0.0089  431 ILE A C   
3337 O O   . ILE A 431 ? 0.4983 0.5463 0.6260 -0.0191 0.0421  0.0140  431 ILE A O   
3338 C CB  . ILE A 431 ? 0.4792 0.6215 0.7036 -0.0473 0.0125  -0.0124 431 ILE A CB  
3339 C CG1 . ILE A 431 ? 0.4638 0.6276 0.6798 -0.0505 0.0048  -0.0146 431 ILE A CG1 
3340 C CG2 . ILE A 431 ? 0.4686 0.5935 0.6765 -0.0504 -0.0015 -0.0136 431 ILE A CG2 
3341 C CD1 . ILE A 431 ? 0.5805 0.7464 0.7650 -0.0496 -0.0167 -0.0087 431 ILE A CD1 
3342 N N   . ILE A 432 ? 0.5226 0.5650 0.6849 -0.0357 0.0538  0.0141  432 ILE A N   
3343 C CA  . ILE A 432 ? 0.5846 0.5788 0.6927 -0.0231 0.0582  0.0295  432 ILE A CA  
3344 C C   . ILE A 432 ? 0.5456 0.5300 0.6420 -0.0218 0.0347  0.0293  432 ILE A C   
3345 O O   . ILE A 432 ? 0.5961 0.5943 0.7296 -0.0321 0.0327  0.0218  432 ILE A O   
3346 C CB  . ILE A 432 ? 0.5314 0.5000 0.6404 -0.0248 0.0914  0.0417  432 ILE A CB  
3347 C CG1 . ILE A 432 ? 0.4573 0.4477 0.5941 -0.0293 0.1165  0.0388  432 ILE A CG1 
3348 C CG2 . ILE A 432 ? 0.5888 0.5084 0.6324 -0.0093 0.0954  0.0602  432 ILE A CG2 
3349 C CD1 . ILE A 432 ? 0.6170 0.5902 0.7678 -0.0366 0.1523  0.0489  432 ILE A CD1 
3350 N N   . PHE A 433 ? 0.5139 0.4766 0.5609 -0.0095 0.0171  0.0357  433 PHE A N   
3351 C CA  . PHE A 433 ? 0.5316 0.4844 0.5642 -0.0052 -0.0045 0.0381  433 PHE A CA  
3352 C C   . PHE A 433 ? 0.6569 0.5658 0.6389 0.0090  0.0015  0.0568  433 PHE A C   
3353 O O   . PHE A 433 ? 0.6858 0.5722 0.6306 0.0162  0.0165  0.0657  433 PHE A O   
3354 C CB  . PHE A 433 ? 0.5440 0.5137 0.5635 -0.0045 -0.0345 0.0293  433 PHE A CB  
3355 C CG  . PHE A 433 ? 0.5878 0.5995 0.6503 -0.0174 -0.0429 0.0141  433 PHE A CG  
3356 C CD1 . PHE A 433 ? 0.6442 0.6817 0.7511 -0.0283 -0.0442 0.0047  433 PHE A CD1 
3357 C CD2 . PHE A 433 ? 0.5514 0.5749 0.6070 -0.0179 -0.0498 0.0095  433 PHE A CD2 
3358 C CE1 . PHE A 433 ? 0.5678 0.6454 0.7079 -0.0401 -0.0528 -0.0087 433 PHE A CE1 
3359 C CE2 . PHE A 433 ? 0.5521 0.6134 0.6428 -0.0284 -0.0586 -0.0010 433 PHE A CE2 
3360 C CZ  . PHE A 433 ? 0.5020 0.5900 0.6279 -0.0387 -0.0581 -0.0097 433 PHE A CZ  
3361 N N   . GLY A 434 ? 0.6894 0.5873 0.6691 0.0144  -0.0105 0.0630  434 GLY A N   
3362 C CA  . GLY A 434 ? 0.6704 0.5288 0.6001 0.0299  -0.0094 0.0832  434 GLY A CA  
3363 C C   . GLY A 434 ? 0.6896 0.5417 0.6331 0.0365  -0.0215 0.0897  434 GLY A C   
3364 O O   . GLY A 434 ? 0.7000 0.5737 0.6948 0.0279  -0.0233 0.0778  434 GLY A O   
3365 N N   . GLY A 435 ? 0.7308 0.5536 0.6263 0.0532  -0.0301 0.1083  435 GLY A N   
3366 C CA  . GLY A 435 ? 0.7844 0.5959 0.6881 0.0650  -0.0407 0.1195  435 GLY A CA  
3367 C C   . GLY A 435 ? 0.8271 0.5969 0.6707 0.0838  -0.0385 0.1470  435 GLY A C   
3368 O O   . GLY A 435 ? 0.7988 0.5448 0.5993 0.0849  -0.0202 0.1575  435 GLY A O   
3369 N N   . ARG A 436 ? 0.7492 0.5118 0.5890 0.0998  -0.0576 0.1593  436 ARG A N   
3370 C CA  . ARG A 436 ? 0.8762 0.6215 0.6767 0.1113  -0.0589 0.1803  436 ARG A CA  
3371 C C   . ARG A 436 ? 0.9123 0.6907 0.6859 0.1133  -0.0880 0.1722  436 ARG A C   
3372 O O   . ARG A 436 ? 0.9418 0.7487 0.7362 0.1189  -0.1107 0.1691  436 ARG A O   
3373 C CB  . ARG A 436 ? 1.0307 0.7603 0.8594 0.1220  -0.0584 0.1952  436 ARG A CB  
3374 C CG  . ARG A 436 ? 0.9957 0.6877 0.8453 0.1163  -0.0229 0.2030  436 ARG A CG  
3375 C CD  . ARG A 436 ? 0.8871 0.5624 0.7706 0.1258  -0.0239 0.2106  436 ARG A CD  
3376 N NE  . ARG A 436 ? 1.0493 0.6936 0.9573 0.1151  0.0123  0.2132  436 ARG A NE  
3377 C CZ  . ARG A 436 ? 1.0090 0.6191 0.8919 0.1161  0.0313  0.2330  436 ARG A CZ  
3378 N NH1 . ARG A 436 ? 0.9360 0.5361 0.7681 0.1289  0.0182  0.2536  436 ARG A NH1 
3379 N NH2 . ARG A 436 ? 0.9947 0.5837 0.9069 0.1022  0.0644  0.2314  436 ARG A NH2 
3380 N N   . ARG A 437 ? 0.9460 0.7217 0.6767 0.1077  -0.0837 0.1669  437 ARG A N   
3381 C CA  . ARG A 437 ? 0.9022 0.7022 0.6050 0.1074  -0.1056 0.1580  437 ARG A CA  
3382 C C   . ARG A 437 ? 0.9931 0.7699 0.6452 0.1163  -0.1005 0.1772  437 ARG A C   
3383 O O   . ARG A 437 ? 0.9354 0.6863 0.5497 0.1149  -0.0791 0.1810  437 ARG A O   
3384 C CB  . ARG A 437 ? 0.8502 0.6617 0.5417 0.0952  -0.1062 0.1353  437 ARG A CB  
3385 C CG  . ARG A 437 ? 0.8284 0.6677 0.5677 0.0843  -0.1152 0.1153  437 ARG A CG  
3386 C CD  . ARG A 437 ? 0.8046 0.6801 0.5826 0.0848  -0.1364 0.1094  437 ARG A CD  
3387 N NE  . ARG A 437 ? 0.8619 0.7587 0.6227 0.0843  -0.1526 0.1047  437 ARG A NE  
3388 C CZ  . ARG A 437 ? 0.8124 0.7368 0.5837 0.0717  -0.1617 0.0845  437 ARG A CZ  
3389 N NH1 . ARG A 437 ? 0.6202 0.5548 0.4175 0.0590  -0.1563 0.0678  437 ARG A NH1 
3390 N NH2 . ARG A 437 ? 0.7007 0.6422 0.4572 0.0715  -0.1755 0.0826  437 ARG A NH2 
3391 N N   . PRO A 438 ? 0.9266 0.7129 0.5762 0.1261  -0.1183 0.1903  438 PRO A N   
3392 C CA  . PRO A 438 ? 1.0778 0.8422 0.6755 0.1348  -0.1157 0.2105  438 PRO A CA  
3393 C C   . PRO A 438 ? 1.1236 0.8925 0.6711 0.1301  -0.1197 0.1985  438 PRO A C   
3394 O O   . PRO A 438 ? 1.1750 0.9192 0.6721 0.1353  -0.1087 0.2125  438 PRO A O   
3395 C CB  . PRO A 438 ? 0.9916 0.7740 0.6061 0.1460  -0.1399 0.2246  438 PRO A CB  
3396 C CG  . PRO A 438 ? 0.8977 0.7228 0.5638 0.1404  -0.1579 0.2039  438 PRO A CG  
3397 C CD  . PRO A 438 ? 0.8555 0.6734 0.5502 0.1307  -0.1402 0.1888  438 PRO A CD  
3398 N N   . ALA A 439 ? 0.9959 0.7935 0.5554 0.1200  -0.1338 0.1729  439 ALA A N   
3399 C CA  . ALA A 439 ? 1.0460 0.8465 0.5614 0.1154  -0.1395 0.1596  439 ALA A CA  
3400 C C   . ALA A 439 ? 0.9781 0.7918 0.5135 0.1021  -0.1393 0.1315  439 ALA A C   
3401 O O   . ALA A 439 ? 0.9890 0.8204 0.5743 0.0958  -0.1420 0.1219  439 ALA A O   
3402 C CB  . ALA A 439 ? 1.0362 0.8635 0.5391 0.1183  -0.1675 0.1621  439 ALA A CB  
3403 N N   . GLY A 440 ? 1.0862 0.8895 0.5809 0.0984  -0.1356 0.1188  440 GLY A N   
3404 C CA  . GLY A 440 ? 0.9706 0.7821 0.4793 0.0866  -0.1367 0.0929  440 GLY A CA  
3405 C C   . GLY A 440 ? 1.0308 0.8224 0.5482 0.0839  -0.1138 0.0869  440 GLY A C   
3406 O O   . GLY A 440 ? 1.1081 0.8843 0.5997 0.0814  -0.1043 0.0736  440 GLY A O   
3407 N N   . VAL A 441 ? 1.0114 0.8028 0.5643 0.0848  -0.1043 0.0966  441 VAL A N   
3408 C CA  . VAL A 441 ? 1.0066 0.7877 0.5762 0.0805  -0.0857 0.0902  441 VAL A CA  
3409 C C   . VAL A 441 ? 1.0659 0.8122 0.5944 0.0877  -0.0538 0.1016  441 VAL A C   
3410 O O   . VAL A 441 ? 1.0369 0.7676 0.5513 0.0949  -0.0406 0.1224  441 VAL A O   
3411 C CB  . VAL A 441 ? 0.9374 0.7319 0.5592 0.0779  -0.0868 0.0960  441 VAL A CB  
3412 C CG1 . VAL A 441 ? 0.8547 0.6448 0.4953 0.0718  -0.0719 0.0883  441 VAL A CG1 
3413 C CG2 . VAL A 441 ? 0.8490 0.6810 0.5113 0.0720  -0.1138 0.0863  441 VAL A CG2 
3414 N N   . PRO A 442 ? 1.0860 0.8202 0.5977 0.0860  -0.0381 0.0893  442 PRO A N   
3415 C CA  . PRO A 442 ? 1.1080 0.8146 0.5862 0.0924  -0.0022 0.0990  442 PRO A CA  
3416 C C   . PRO A 442 ? 0.9752 0.6772 0.4871 0.0910  0.0253  0.1144  442 PRO A C   
3417 O O   . PRO A 442 ? 0.9143 0.6314 0.4720 0.0853  0.0167  0.1142  442 PRO A O   
3418 C CB  . PRO A 442 ? 1.1177 0.8181 0.5789 0.0914  0.0048  0.0784  442 PRO A CB  
3419 C CG  . PRO A 442 ? 0.9633 0.6861 0.4663 0.0826  -0.0195 0.0634  442 PRO A CG  
3420 C CD  . PRO A 442 ? 1.0059 0.7517 0.5322 0.0783  -0.0504 0.0665  442 PRO A CD  
3421 N N   . LEU A 443 ? 1.0978 0.7800 0.5898 0.0946  0.0606  0.1270  443 LEU A N   
3422 C CA  . LEU A 443 ? 1.0102 0.6892 0.5411 0.0898  0.0918  0.1422  443 LEU A CA  
3423 C C   . LEU A 443 ? 0.9050 0.6029 0.4868 0.0811  0.1011  0.1318  443 LEU A C   
3424 O O   . LEU A 443 ? 0.9764 0.6902 0.6201 0.0711  0.1100  0.1354  443 LEU A O   
3425 C CB  . LEU A 443 ? 0.9976 0.6587 0.5046 0.0921  0.1304  0.1528  443 LEU A CB  
3426 C CG  . LEU A 443 ? 0.9965 0.6606 0.5552 0.0825  0.1672  0.1635  443 LEU A CG  
3427 C CD1 . LEU A 443 ? 1.0163 0.6726 0.6000 0.0794  0.1620  0.1811  443 LEU A CD1 
3428 C CD2 . LEU A 443 ? 1.0814 0.7366 0.6236 0.0830  0.2059  0.1674  443 LEU A CD2 
3429 N N   . VAL A 444 ? 0.8762 0.5877 0.4576 0.0806  0.0948  0.1107  444 VAL A N   
3430 C CA  . VAL A 444 ? 0.9100 0.6577 0.5634 0.0701  0.0990  0.0944  444 VAL A CA  
3431 C C   . VAL A 444 ? 0.8979 0.6504 0.5368 0.0737  0.0872  0.0740  444 VAL A C   
3432 O O   . VAL A 444 ? 0.9835 0.7106 0.5638 0.0837  0.0966  0.0709  444 VAL A O   
3433 C CB  . VAL A 444 ? 0.7617 0.5183 0.4539 0.0646  0.1411  0.1008  444 VAL A CB  
3434 C CG1 . VAL A 444 ? 0.9152 0.6511 0.5587 0.0746  0.1715  0.1022  444 VAL A CG1 
3435 C CG2 . VAL A 444 ? 0.7459 0.5464 0.5176 0.0534  0.1405  0.0855  444 VAL A CG2 
3436 N N   . TYR A 445 ? 0.7862 0.5689 0.4762 0.0658  0.0673  0.0600  445 TYR A N   
3437 C CA  . TYR A 445 ? 0.8699 0.6564 0.5576 0.0686  0.0594  0.0424  445 TYR A CA  
3438 C C   . TYR A 445 ? 0.7374 0.5641 0.4993 0.0591  0.0531  0.0346  445 TYR A C   
3439 O O   . TYR A 445 ? 0.7391 0.5905 0.5472 0.0490  0.0483  0.0393  445 TYR A O   
3440 C CB  . TYR A 445 ? 0.8697 0.6364 0.5073 0.0707  0.0264  0.0334  445 TYR A CB  
3441 C CG  . TYR A 445 ? 0.8642 0.6484 0.5238 0.0614  -0.0078 0.0341  445 TYR A CG  
3442 C CD1 . TYR A 445 ? 0.8887 0.7009 0.5968 0.0515  -0.0262 0.0238  445 TYR A CD1 
3443 C CD2 . TYR A 445 ? 0.9383 0.7119 0.5693 0.0636  -0.0213 0.0459  445 TYR A CD2 
3444 C CE1 . TYR A 445 ? 0.8270 0.6577 0.5558 0.0427  -0.0546 0.0235  445 TYR A CE1 
3445 C CE2 . TYR A 445 ? 0.8388 0.6318 0.4942 0.0568  -0.0511 0.0455  445 TYR A CE2 
3446 C CZ  . TYR A 445 ? 0.9008 0.7229 0.6054 0.0457  -0.0665 0.0334  445 TYR A CZ  
3447 O OH  . TYR A 445 ? 0.8323 0.6770 0.5634 0.0384  -0.0926 0.0320  445 TYR A OH  
3448 N N   . GLU A 446 ? 0.7881 0.6201 0.5594 0.0634  0.0536  0.0225  446 GLU A N   
3449 C CA  . GLU A 446 ? 0.7998 0.6700 0.6361 0.0574  0.0487  0.0169  446 GLU A CA  
3450 C C   . GLU A 446 ? 0.8041 0.6741 0.6371 0.0540  0.0166  0.0076  446 GLU A C   
3451 O O   . GLU A 446 ? 0.8192 0.6573 0.6037 0.0596  0.0071  0.0005  446 GLU A O   
3452 C CB  . GLU A 446 ? 0.7298 0.6104 0.5894 0.0669  0.0773  0.0138  446 GLU A CB  
3453 C CG  . GLU A 446 ? 0.6997 0.6233 0.6258 0.0632  0.0710  0.0098  446 GLU A CG  
3454 C CD  . GLU A 446 ? 0.7703 0.7081 0.7232 0.0756  0.0982  0.0073  446 GLU A CD  
3455 O OE1 . GLU A 446 ? 0.7543 0.6791 0.6895 0.0822  0.1287  0.0102  446 GLU A OE1 
3456 O OE2 . GLU A 446 ? 0.7661 0.7291 0.7579 0.0795  0.0896  0.0034  446 GLU A OE2 
3457 N N   . ALA A 447 ? 0.7308 0.6361 0.6143 0.0433  0.0009  0.0070  447 ALA A N   
3458 C CA  . ALA A 447 ? 0.7168 0.6246 0.6018 0.0379  -0.0270 0.0006  447 ALA A CA  
3459 C C   . ALA A 447 ? 0.7364 0.6348 0.6222 0.0480  -0.0217 -0.0051 447 ALA A C   
3460 O O   . ALA A 447 ? 0.7161 0.6268 0.6268 0.0573  0.0005  -0.0038 447 ALA A O   
3461 C CB  . ALA A 447 ? 0.6036 0.5533 0.5399 0.0242  -0.0418 0.0021  447 ALA A CB  
3462 N N   . LEU A 448 ? 0.8109 0.6873 0.6721 0.0460  -0.0420 -0.0114 448 LEU A N   
3463 C CA  . LEU A 448 ? 0.7370 0.5953 0.5959 0.0563  -0.0384 -0.0167 448 LEU A CA  
3464 C C   . LEU A 448 ? 0.6681 0.5614 0.5810 0.0546  -0.0449 -0.0108 448 LEU A C   
3465 O O   . LEU A 448 ? 0.6987 0.5861 0.6237 0.0679  -0.0358 -0.0110 448 LEU A O   
3466 C CB  . LEU A 448 ? 0.6328 0.4499 0.4452 0.0525  -0.0572 -0.0264 448 LEU A CB  
3467 C CG  . LEU A 448 ? 0.8391 0.6250 0.5930 0.0531  -0.0568 -0.0329 448 LEU A CG  
3468 C CD1 . LEU A 448 ? 0.8376 0.5908 0.5519 0.0445  -0.0804 -0.0448 448 LEU A CD1 
3469 C CD2 . LEU A 448 ? 0.9091 0.6727 0.6360 0.0705  -0.0263 -0.0363 448 LEU A CD2 
3470 N N   . SER A 449 ? 0.6566 0.5864 0.6008 0.0399  -0.0602 -0.0056 449 SER A N   
3471 C CA  . SER A 449 ? 0.6745 0.6420 0.6652 0.0368  -0.0683 0.0006  449 SER A CA  
3472 C C   . SER A 449 ? 0.6293 0.6355 0.6458 0.0197  -0.0799 0.0026  449 SER A C   
3473 O O   . SER A 449 ? 0.5872 0.5858 0.5854 0.0114  -0.0844 -0.0002 449 SER A O   
3474 C CB  . SER A 449 ? 0.6231 0.5697 0.6031 0.0366  -0.0849 0.0019  449 SER A CB  
3475 O OG  . SER A 449 ? 0.6863 0.6181 0.6409 0.0207  -0.1046 -0.0015 449 SER A OG  
3476 N N   . TRP A 450 ? 0.5837 0.6322 0.6426 0.0156  -0.0851 0.0070  450 TRP A N   
3477 C CA  . TRP A 450 ? 0.5506 0.6360 0.6326 -0.0009 -0.0934 0.0058  450 TRP A CA  
3478 C C   . TRP A 450 ? 0.5439 0.6089 0.5907 -0.0104 -0.0909 0.0015  450 TRP A C   
3479 O O   . TRP A 450 ? 0.5618 0.6296 0.6041 -0.0151 -0.0836 -0.0028 450 TRP A O   
3480 C CB  . TRP A 450 ? 0.5477 0.6644 0.6458 -0.0021 -0.0845 0.0064  450 TRP A CB  
3481 C CG  . TRP A 450 ? 0.7107 0.8435 0.8033 -0.0097 -0.0704 -0.0067 450 TRP A CG  
3482 C CD1 . TRP A 450 ? 0.7211 0.8449 0.8041 -0.0148 -0.0732 -0.0085 450 TRP A CD1 
3483 C CD2 . TRP A 450 ? 0.7614 0.9062 0.8677 -0.0132 -0.0593 -0.0140 450 TRP A CD2 
3484 N NE1 . TRP A 450 ? 0.6992 0.8270 0.7918 -0.0190 -0.0680 -0.0152 450 TRP A NE1 
3485 C CE2 . TRP A 450 ? 0.7030 0.8399 0.8101 -0.0179 -0.0605 -0.0201 450 TRP A CE2 
3486 C CE3 . TRP A 450 ? 0.7086 0.8720 0.8401 -0.0153 -0.0539 -0.0091 450 TRP A CE3 
3487 C CZ2 . TRP A 450 ? 0.6785 0.8074 0.8075 -0.0210 -0.0586 -0.0239 450 TRP A CZ2 
3488 C CZ3 . TRP A 450 ? 0.6541 0.8254 0.7830 -0.0265 -0.0430 -0.0037 450 TRP A CZ3 
3489 C CH2 . TRP A 450 ? 0.7052 0.8438 0.8411 -0.0339 -0.0545 0.0086  450 TRP A CH2 
3490 N N   . GLN A 451 ? 0.5730 0.6198 0.6031 -0.0114 -0.0963 0.0034  451 GLN A N   
3491 C CA  . GLN A 451 ? 0.6069 0.6448 0.6205 -0.0179 -0.0910 -0.0005 451 GLN A CA  
3492 C C   . GLN A 451 ? 0.5801 0.5992 0.5749 -0.0179 -0.0933 -0.0037 451 GLN A C   
3493 O O   . GLN A 451 ? 0.6000 0.6270 0.5974 -0.0210 -0.0874 -0.0058 451 GLN A O   
3494 C CB  . GLN A 451 ? 0.6101 0.6255 0.6121 -0.0204 -0.1008 0.0031  451 GLN A CB  
3495 C CG  . GLN A 451 ? 0.5646 0.5975 0.5821 -0.0207 -0.1001 0.0086  451 GLN A CG  
3496 C CD  . GLN A 451 ? 0.6619 0.6990 0.6935 -0.0113 -0.1090 0.0159  451 GLN A CD  
3497 O OE1 . GLN A 451 ? 0.7307 0.7399 0.7540 -0.0014 -0.1225 0.0178  451 GLN A OE1 
3498 N NE2 . GLN A 451 ? 0.6363 0.7069 0.6873 -0.0090 -0.1016 0.0174  451 GLN A NE2 
3499 N N   . HIS A 452 ? 0.5929 0.5778 0.5618 -0.0117 -0.1066 -0.0043 452 HIS A N   
3500 C CA  . HIS A 452 ? 0.6226 0.5859 0.5622 -0.0093 -0.1084 -0.0077 452 HIS A CA  
3501 C C   . HIS A 452 ? 0.6369 0.6200 0.5913 -0.0094 -0.1031 -0.0054 452 HIS A C   
3502 O O   . HIS A 452 ? 0.5273 0.5097 0.4741 -0.0107 -0.1009 -0.0053 452 HIS A O   
3503 C CB  . HIS A 452 ? 0.6630 0.5787 0.5530 0.0035  -0.1157 -0.0125 452 HIS A CB  
3504 C CG  . HIS A 452 ? 0.6500 0.5400 0.4966 0.0075  -0.1148 -0.0155 452 HIS A CG  
3505 N ND1 . HIS A 452 ? 0.7500 0.6244 0.5770 0.0204  -0.0923 -0.0132 452 HIS A ND1 
3506 C CD2 . HIS A 452 ? 0.6697 0.5625 0.5141 0.0009  -0.1151 -0.0164 452 HIS A CD2 
3507 C CE1 . HIS A 452 ? 0.7228 0.5756 0.5066 0.0220  -0.0983 -0.0144 452 HIS A CE1 
3508 N NE2 . HIS A 452 ? 0.6232 0.4911 0.4243 0.0100  -0.1127 -0.0166 452 HIS A NE2 
3509 N N   . GLY A 453 ? 0.5144 0.5174 0.4959 -0.0077 -0.1026 -0.0031 453 GLY A N   
3510 C CA  . GLY A 453 ? 0.5975 0.6209 0.6034 -0.0106 -0.0915 -0.0016 453 GLY A CA  
3511 C C   . GLY A 453 ? 0.6223 0.6669 0.6419 -0.0184 -0.0850 -0.0050 453 GLY A C   
3512 O O   . GLY A 453 ? 0.4917 0.5281 0.5029 -0.0183 -0.0871 -0.0041 453 GLY A O   
3513 N N   . VAL A 454 ? 0.5565 0.6238 0.5893 -0.0202 -0.0731 -0.0098 454 VAL A N   
3514 C CA  . VAL A 454 ? 0.5209 0.5923 0.5596 -0.0240 -0.0705 -0.0118 454 VAL A CA  
3515 C C   . VAL A 454 ? 0.5028 0.5579 0.5256 -0.0237 -0.0765 -0.0099 454 VAL A C   
3516 O O   . VAL A 454 ? 0.5957 0.6550 0.6235 -0.0245 -0.0760 -0.0110 454 VAL A O   
3517 C CB  . VAL A 454 ? 0.4899 0.5681 0.5348 -0.0262 -0.0703 -0.0120 454 VAL A CB  
3518 C CG1 . VAL A 454 ? 0.4880 0.5705 0.5363 -0.0292 -0.0696 -0.0144 454 VAL A CG1 
3519 C CG2 . VAL A 454 ? 0.5202 0.6174 0.5824 -0.0252 -0.0661 -0.0154 454 VAL A CG2 
3520 N N   . PHE A 455 ? 0.5296 0.5669 0.5339 -0.0227 -0.0830 -0.0080 455 PHE A N   
3521 C CA  . PHE A 455 ? 0.6128 0.6374 0.6027 -0.0228 -0.0898 -0.0077 455 PHE A CA  
3522 C C   . PHE A 455 ? 0.5908 0.6121 0.5708 -0.0178 -0.0915 -0.0067 455 PHE A C   
3523 O O   . PHE A 455 ? 0.5954 0.6166 0.5736 -0.0173 -0.0962 -0.0061 455 PHE A O   
3524 C CB  . PHE A 455 ? 0.5393 0.5439 0.5091 -0.0233 -0.0969 -0.0082 455 PHE A CB  
3525 C CG  . PHE A 455 ? 0.5308 0.5235 0.4825 -0.0227 -0.1051 -0.0096 455 PHE A CG  
3526 C CD1 . PHE A 455 ? 0.4867 0.4871 0.4469 -0.0274 -0.1095 -0.0102 455 PHE A CD1 
3527 C CD2 . PHE A 455 ? 0.5140 0.4904 0.4381 -0.0170 -0.1084 -0.0107 455 PHE A CD2 
3528 C CE1 . PHE A 455 ? 0.5864 0.5817 0.5326 -0.0270 -0.1189 -0.0122 455 PHE A CE1 
3529 C CE2 . PHE A 455 ? 0.5799 0.5480 0.4855 -0.0162 -0.1171 -0.0123 455 PHE A CE2 
3530 C CZ  . PHE A 455 ? 0.4909 0.4701 0.4098 -0.0215 -0.1233 -0.0132 455 PHE A CZ  
3531 N N   . VAL A 456 ? 0.5653 0.5776 0.5359 -0.0141 -0.0930 -0.0042 456 VAL A N   
3532 C CA  . VAL A 456 ? 0.5937 0.5845 0.5423 -0.0085 -0.1023 0.0019  456 VAL A CA  
3533 C C   . VAL A 456 ? 0.5636 0.5716 0.5396 -0.0106 -0.1008 0.0033  456 VAL A C   
3534 O O   . VAL A 456 ? 0.5127 0.5139 0.4796 -0.0061 -0.1068 0.0072  456 VAL A O   
3535 C CB  . VAL A 456 ? 0.5851 0.5482 0.5056 -0.0016 -0.1048 0.0074  456 VAL A CB  
3536 C CG1 . VAL A 456 ? 0.6807 0.6280 0.5913 0.0062  -0.0887 0.0175  456 VAL A CG1 
3537 C CG2 . VAL A 456 ? 0.5529 0.4847 0.4268 0.0053  -0.1068 0.0045  456 VAL A CG2 
3538 N N   . GLY A 457 ? 0.5059 0.5365 0.5161 -0.0168 -0.0923 -0.0006 457 GLY A N   
3539 C CA  . GLY A 457 ? 0.5182 0.5645 0.5554 -0.0200 -0.0875 -0.0030 457 GLY A CA  
3540 C C   . GLY A 457 ? 0.5350 0.5908 0.5676 -0.0179 -0.0843 -0.0065 457 GLY A C   
3541 O O   . GLY A 457 ? 0.4587 0.5077 0.4944 -0.0144 -0.0934 -0.0025 457 GLY A O   
3542 N N   . ALA A 458 ? 0.5503 0.6096 0.5808 -0.0209 -0.0824 -0.0096 458 ALA A N   
3543 C CA  . ALA A 458 ? 0.4883 0.5526 0.5214 -0.0219 -0.0865 -0.0110 458 ALA A CA  
3544 C C   . ALA A 458 ? 0.4670 0.5214 0.4852 -0.0168 -0.0974 -0.0073 458 ALA A C   
3545 O O   . ALA A 458 ? 0.5005 0.5641 0.5261 -0.0162 -0.1021 -0.0082 458 ALA A O   
3546 C CB  . ALA A 458 ? 0.6091 0.6761 0.6409 -0.0262 -0.0853 -0.0130 458 ALA A CB  
3547 N N   . ALA A 459 ? 0.5117 0.5500 0.5070 -0.0124 -0.1018 -0.0034 459 ALA A N   
3548 C CA  . ALA A 459 ? 0.5500 0.5794 0.5242 -0.0067 -0.1126 0.0003  459 ALA A CA  
3549 C C   . ALA A 459 ? 0.5722 0.5908 0.5355 0.0032  -0.1191 0.0097  459 ALA A C   
3550 O O   . ALA A 459 ? 0.5630 0.5721 0.5036 0.0106  -0.1287 0.0156  459 ALA A O   
3551 C CB  . ALA A 459 ? 0.5377 0.5498 0.4846 -0.0067 -0.1157 -0.0004 459 ALA A CB  
3552 N N   . MET A 460 ? 0.4939 0.5060 0.4721 0.0037  -0.1190 0.0130  460 MET A N   
3553 C CA  . MET A 460 ? 0.5691 0.5552 0.5350 0.0157  -0.1295 0.0277  460 MET A CA  
3554 C C   . MET A 460 ? 0.5108 0.5036 0.4805 0.0245  -0.1370 0.0317  460 MET A C   
3555 O O   . MET A 460 ? 0.6689 0.6903 0.6678 0.0189  -0.1349 0.0219  460 MET A O   
3556 C CB  . MET A 460 ? 0.3687 0.3560 0.3710 0.0120  -0.1245 0.0294  460 MET A CB  
3557 C CG  . MET A 460 ? 0.5167 0.5037 0.5215 0.0033  -0.1060 0.0251  460 MET A CG  
3558 S SD  . MET A 460 ? 0.4749 0.4770 0.5346 -0.0072 -0.0812 0.0184  460 MET A SD  
3559 C CE  . MET A 460 ? 0.4922 0.4583 0.5461 0.0057  -0.0682 0.0342  460 MET A CE  
3560 N N   . ARG A 461 ? 0.4914 0.4570 0.4273 0.0396  -0.1422 0.0481  461 ARG A N   
3561 C CA  . ARG A 461 ? 0.6854 0.6557 0.6251 0.0517  -0.1502 0.0564  461 ARG A CA  
3562 C C   . ARG A 461 ? 0.7868 0.7154 0.7020 0.0696  -0.1454 0.0805  461 ARG A C   
3563 O O   . ARG A 461 ? 0.8435 0.7394 0.7242 0.0716  -0.1334 0.0907  461 ARG A O   
3564 C CB  . ARG A 461 ? 0.6336 0.6227 0.5546 0.0506  -0.1572 0.0528  461 ARG A CB  
3565 C CG  . ARG A 461 ? 0.6135 0.6370 0.5578 0.0342  -0.1537 0.0341  461 ARG A CG  
3566 C CD  . ARG A 461 ? 0.5809 0.6177 0.5064 0.0326  -0.1610 0.0324  461 ARG A CD  
3567 N NE  . ARG A 461 ? 0.5544 0.6042 0.4814 0.0435  -0.1739 0.0418  461 ARG A NE  
3568 C CZ  . ARG A 461 ? 0.7441 0.7999 0.6477 0.0467  -0.1857 0.0462  461 ARG A CZ  
3569 N NH1 . ARG A 461 ? 0.7938 0.8371 0.6676 0.0404  -0.1877 0.0401  461 ARG A NH1 
3570 N NH2 . ARG A 461 ? 0.7042 0.7768 0.6141 0.0575  -0.1982 0.0565  461 ARG A NH2 
3571 N N   . SER A 462 ? 0.7642 0.6916 0.6972 0.0830  -0.1491 0.0907  462 SER A N   
3572 C CA  . SER A 462 ? 0.8336 0.7168 0.7512 0.0994  -0.1361 0.1155  462 SER A CA  
3573 C C   . SER A 462 ? 0.8714 0.7625 0.8021 0.1162  -0.1443 0.1266  462 SER A C   
3574 O O   . SER A 462 ? 0.9141 0.8419 0.8796 0.1150  -0.1573 0.1127  462 SER A O   
3575 C CB  . SER A 462 ? 0.7568 0.6182 0.7103 0.0927  -0.1152 0.1142  462 SER A CB  
3576 O OG  . SER A 462 ? 0.8286 0.6456 0.7716 0.1043  -0.0932 0.1367  462 SER A OG  
3577 N N   . GLU A 463 ? 0.9173 0.7750 0.8215 0.1305  -0.1347 0.1529  463 GLU A N   
3578 C CA  . GLU A 463 ? 1.0707 0.9332 0.9873 0.1483  -0.1428 0.1686  463 GLU A CA  
3579 C C   . GLU A 463 ? 1.0624 0.9084 1.0263 0.1585  -0.1311 0.1685  463 GLU A C   
3580 O O   . GLU A 463 ? 1.0077 0.8252 0.9885 0.1509  -0.1128 0.1624  463 GLU A O   
3581 C CB  . GLU A 463 ? 1.0433 0.8753 0.9178 0.1561  -0.1398 0.1972  463 GLU A CB  
3582 C CG  . GLU A 463 ? 1.1189 0.8964 0.9759 0.1520  -0.1138 0.2105  463 GLU A CG  
3583 C CD  . GLU A 463 ? 1.2339 0.9787 1.0482 0.1605  -0.1112 0.2367  463 GLU A CD  
3584 O OE1 . GLU A 463 ? 1.2294 0.9943 1.0289 0.1700  -0.1329 0.2464  463 GLU A OE1 
3585 O OE2 . GLU A 463 ? 1.2653 0.9665 1.0607 0.1572  -0.0856 0.2474  463 GLU A OE2 
3586 N N   . ALA A 464 ? 1.1531 1.0167 1.1403 0.1749  -0.1412 0.1731  464 ALA A N   
3587 C CA  . ALA A 464 ? 1.3579 1.2057 1.3886 0.1862  -0.1310 0.1668  464 ALA A CA  
3588 C C   . ALA A 464 ? 1.4840 1.2619 1.4933 0.1973  -0.1055 0.1845  464 ALA A C   
3589 O O   . ALA A 464 ? 1.5065 1.2655 1.5147 0.1888  -0.1229 0.2100  464 ALA A O   
3590 C CB  . ALA A 464 ? 1.4413 1.3233 1.4960 0.2037  -0.1473 0.1677  464 ALA A CB  
3591 N N   . THR A 465 ? 1.6327 1.3870 1.6809 0.1819  -0.0889 0.1698  465 THR A N   
3592 C CA  . THR A 465 ? 1.7426 1.4411 1.7918 0.1772  -0.0631 0.1806  465 THR A CA  
3593 C C   . THR A 465 ? 1.8661 1.5580 1.9667 0.1856  -0.0534 0.1711  465 THR A C   
3594 O O   . THR A 465 ? 1.8481 1.5689 1.9668 0.2033  -0.0721 0.1651  465 THR A O   
3595 C CB  . THR A 465 ? 1.6241 1.3170 1.6827 0.1503  -0.0363 0.1734  465 THR A CB  
3596 O OG1 . THR A 465 ? 1.5618 1.2960 1.6781 0.1346  -0.0359 0.1454  465 THR A OG1 
3597 C CG2 . THR A 465 ? 1.5815 1.2756 1.5839 0.1453  -0.0434 0.1854  465 THR A CG2 
3598 N N   . ALA A 466 ? 1.8928 1.5507 2.0173 0.1720  -0.0229 0.1679  466 ALA A N   
3599 C CA  . ALA A 466 ? 1.9253 1.5703 2.0947 0.1778  -0.0112 0.1570  466 ALA A CA  
3600 C C   . ALA A 466 ? 1.8697 1.5317 2.0953 0.1510  0.0110  0.1255  466 ALA A C   
3601 O O   . ALA A 466 ? 1.7930 1.4241 2.0383 0.1396  0.0366  0.1199  466 ALA A O   
3602 C CB  . ALA A 466 ? 1.8808 1.4665 2.0275 0.1863  0.0031  0.1806  466 ALA A CB  
3603 N N   . ALA A 467 ? 1.6809 1.3940 1.9325 0.1392  -0.0007 0.1032  467 ALA A N   
3604 C CA  . ALA A 467 ? 1.4403 1.1775 1.7434 0.1131  0.0142  0.0690  467 ALA A CA  
3605 C C   . ALA A 467 ? 1.4064 1.1815 1.7563 0.1181  0.0037  0.0428  467 ALA A C   
3606 O O   . ALA A 467 ? 1.2235 0.9944 1.6104 0.1076  0.0217  0.0201  467 ALA A O   
3607 C CB  . ALA A 467 ? 1.2381 1.0049 1.5368 0.0925  0.0096  0.0600  467 ALA A CB  
3608 N N   . ALA A 468 ? 1.4941 1.3099 1.8415 0.1322  -0.0248 0.0437  468 ALA A N   
3609 C CA  . ALA A 468 ? 1.4423 1.2976 1.8298 0.1391  -0.0344 0.0216  468 ALA A CA  
3610 C C   . ALA A 468 ? 1.5537 1.3927 1.9293 0.1707  -0.0431 0.0425  468 ALA A C   
3611 O O   . ALA A 468 ? 1.5773 1.3629 1.9282 0.1835  -0.0314 0.0651  468 ALA A O   
3612 C CB  . ALA A 468 ? 1.3176 1.2366 1.7119 0.1304  -0.0590 0.0063  468 ALA A CB  
3613 N N   . GLU A 469 ? 1.5352 1.4211 1.9265 0.1827  -0.0632 0.0352  469 GLU A N   
3614 C CA  . GLU A 469 ? 1.5386 1.4187 1.9218 0.2142  -0.0735 0.0538  469 GLU A CA  
3615 C C   . GLU A 469 ? 1.5885 1.4881 1.9261 0.2277  -0.1005 0.0784  469 GLU A C   
3616 O O   . GLU A 469 ? 1.5087 1.4237 1.8432 0.2522  -0.1140 0.0902  469 GLU A O   
3617 C CB  . GLU A 469 ? 1.4537 1.3743 1.8858 0.2196  -0.0743 0.0298  469 GLU A CB  
3618 C CG  . GLU A 469 ? 1.3412 1.3310 1.7883 0.2019  -0.0905 0.0084  469 GLU A CG  
3619 C CD  . GLU A 469 ? 1.1961 1.2039 1.6775 0.1739  -0.0745 -0.0273 469 GLU A CD  
3620 O OE1 . GLU A 469 ? 1.1977 1.1665 1.6894 0.1642  -0.0520 -0.0354 469 GLU A OE1 
3621 O OE2 . GLU A 469 ? 1.1107 1.1719 1.6039 0.1597  -0.0830 -0.0471 469 GLU A OE2 
3622 N N   . HIS A 470 ? 1.6946 1.5955 1.9966 0.2120  -0.1074 0.0851  470 HIS A N   
3623 C CA  . HIS A 470 ? 1.7298 1.6507 1.9845 0.2200  -0.1305 0.1043  470 HIS A CA  
3624 C C   . HIS A 470 ? 1.7655 1.6351 1.9701 0.2448  -0.1279 0.1378  470 HIS A C   
3625 O O   . HIS A 470 ? 1.8126 1.6235 1.9997 0.2435  -0.1089 0.1472  470 HIS A O   
3626 C CB  . HIS A 470 ? 1.7013 1.6392 1.9325 0.1938  -0.1372 0.0970  470 HIS A CB  
3627 C CG  . HIS A 470 ? 1.6516 1.6336 1.9230 0.1688  -0.1383 0.0647  470 HIS A CG  
3628 N ND1 . HIS A 470 ? 1.6275 1.6654 1.9086 0.1611  -0.1534 0.0502  470 HIS A ND1 
3629 C CD2 . HIS A 470 ? 1.6233 1.6025 1.9246 0.1485  -0.1233 0.0444  470 HIS A CD2 
3630 C CE1 . HIS A 470 ? 1.5267 1.5907 1.8347 0.1377  -0.1471 0.0239  470 HIS A CE1 
3631 N NE2 . HIS A 470 ? 1.5286 1.5615 1.8517 0.1308  -0.1309 0.0190  470 HIS A NE2 
3632 N N   . LYS A 471 ? 1.6566 1.5506 1.8382 0.2650  -0.1461 0.1555  471 LYS A N   
3633 C CA  . LYS A 471 ? 1.6808 1.5344 1.8111 0.2913  -0.1458 0.1881  471 LYS A CA  
3634 C C   . LYS A 471 ? 1.7177 1.6167 1.8222 0.2819  -0.1621 0.2067  471 LYS A C   
3635 O O   . LYS A 471 ? 1.6239 1.5743 1.7391 0.2634  -0.1786 0.1903  471 LYS A O   
3636 C CB  . LYS A 471 ? 1.5520 1.3942 1.6987 0.3220  -0.1492 0.1946  471 LYS A CB  
3637 C CG  . LYS A 471 ? 1.4826 1.2789 1.6673 0.3242  -0.1322 0.1793  471 LYS A CG  
3638 C CD  . LYS A 471 ? 1.3740 1.1501 1.5691 0.3585  -0.1384 0.1885  471 LYS A CD  
3639 C CE  . LYS A 471 ? 1.2622 0.9973 1.5021 0.3540  -0.1142 0.1751  471 LYS A CE  
3640 N NZ  . LYS A 471 ? 1.2077 0.9166 1.4574 0.3880  -0.1203 0.1855  471 LYS A NZ  
3641 N N   . GLY A 472 ? 1.8052 1.6860 1.8884 0.2860  -0.1607 0.2419  472 GLY A N   
3642 C CA  . GLY A 472 ? 1.7808 1.6914 1.8453 0.2704  -0.1896 0.2579  472 GLY A CA  
3643 C C   . GLY A 472 ? 1.7442 1.6382 1.7664 0.2464  -0.1875 0.2532  472 GLY A C   
3644 O O   . GLY A 472 ? 1.6686 1.5404 1.6911 0.2362  -0.1666 0.2386  472 GLY A O   
3645 N N   . LYS A 473 ? 1.7772 1.6824 1.7574 0.2398  -0.2083 0.2647  473 LYS A N   
3646 C CA  . LYS A 473 ? 1.7514 1.6445 1.6822 0.2211  -0.2055 0.2598  473 LYS A CA  
3647 C C   . LYS A 473 ? 1.6254 1.5721 1.5521 0.2067  -0.2168 0.2310  473 LYS A C   
3648 O O   . LYS A 473 ? 1.6082 1.5810 1.5086 0.2022  -0.2357 0.2316  473 LYS A O   
3649 C CB  . LYS A 473 ? 1.9023 1.7650 1.7775 0.2233  -0.2151 0.2850  473 LYS A CB  
3650 C CG  . LYS A 473 ? 1.9309 1.7344 1.8039 0.2367  -0.2089 0.3116  473 LYS A CG  
3651 C CD  . LYS A 473 ? 1.9295 1.6834 1.8121 0.2286  -0.1807 0.3034  473 LYS A CD  
3652 C CE  . LYS A 473 ? 1.8449 1.5864 1.6799 0.2109  -0.1627 0.2952  473 LYS A CE  
3653 N NZ  . LYS A 473 ? 1.7160 1.4139 1.5617 0.2020  -0.1331 0.2871  473 LYS A NZ  
3654 N N   . VAL A 474 ? 1.4344 1.3939 1.3883 0.1970  -0.2062 0.2038  474 VAL A N   
3655 C CA  . VAL A 474 ? 1.1611 1.1643 1.1196 0.1779  -0.2161 0.1744  474 VAL A CA  
3656 C C   . VAL A 474 ? 1.0562 1.0429 1.0078 0.1592  -0.2012 0.1546  474 VAL A C   
3657 O O   . VAL A 474 ? 1.1099 1.0649 1.0746 0.1623  -0.1847 0.1557  474 VAL A O   
3658 C CB  . VAL A 474 ? 1.0926 1.1385 1.1015 0.1814  -0.2241 0.1594  474 VAL A CB  
3659 C CG1 . VAL A 474 ? 1.0031 1.0809 1.0255 0.1556  -0.2239 0.1280  474 VAL A CG1 
3660 C CG2 . VAL A 474 ? 1.0789 1.1564 1.0913 0.1939  -0.2442 0.1749  474 VAL A CG2 
3661 N N   . ILE A 475 ? 1.1833 0.6356 1.0293 0.0270  0.2113  0.1553  475 ILE A N   
3662 C CA  . ILE A 475 ? 1.0899 0.5306 0.9161 0.0192  0.2242  0.1390  475 ILE A CA  
3663 C C   . ILE A 475 ? 1.0949 0.5465 0.9480 0.0145  0.2291  0.1260  475 ILE A C   
3664 O O   . ILE A 475 ? 1.1068 0.5740 0.9725 0.0105  0.2168  0.1240  475 ILE A O   
3665 C CB  . ILE A 475 ? 1.1115 0.5469 0.8955 0.0123  0.2152  0.1338  475 ILE A CB  
3666 C CG1 . ILE A 475 ? 1.0893 0.5152 0.8430 0.0171  0.2126  0.1478  475 ILE A CG1 
3667 C CG2 . ILE A 475 ? 0.9999 0.4241 0.7698 0.0053  0.2283  0.1175  475 ILE A CG2 
3668 C CD1 . ILE A 475 ? 1.1372 0.5603 0.8473 0.0113  0.2028  0.1424  475 ILE A CD1 
3669 N N   . MET A 476 ? 1.0109 0.4554 0.8727 0.0144  0.2469  0.1175  476 MET A N   
3670 C CA  . MET A 476 ? 1.0318 0.4868 0.9166 0.0109  0.2544  0.1069  476 MET A CA  
3671 C C   . MET A 476 ? 0.9750 0.4195 0.8407 0.0051  0.2663  0.0948  476 MET A C   
3672 O O   . MET A 476 ? 0.9267 0.3560 0.7698 0.0054  0.2717  0.0939  476 MET A O   
3673 C CB  . MET A 476 ? 1.0893 0.5513 1.0107 0.0186  0.2642  0.1087  476 MET A CB  
3674 C CG  . MET A 476 ? 1.0470 0.4928 0.9667 0.0235  0.2784  0.1077  476 MET A CG  
3675 S SD  . MET A 476 ? 1.4174 0.8692 1.3828 0.0331  0.2894  0.1076  476 MET A SD  
3676 C CE  . MET A 476 ? 1.2553 0.7276 1.2383 0.0280  0.2957  0.0939  476 MET A CE  
3677 N N   . HIS A 477 ? 0.9116 0.3655 0.7882 0.0000  0.2704  0.0866  477 HIS A N   
3678 C CA  . HIS A 477 ? 0.8980 0.3445 0.7585 -0.0051 0.2797  0.0770  477 HIS A CA  
3679 C C   . HIS A 477 ? 0.9143 0.3572 0.7816 -0.0013 0.2948  0.0715  477 HIS A C   
3680 O O   . HIS A 477 ? 0.9688 0.4193 0.8602 0.0037  0.3008  0.0715  477 HIS A O   
3681 C CB  . HIS A 477 ? 0.9165 0.3744 0.7858 -0.0120 0.2787  0.0730  477 HIS A CB  
3682 C CG  . HIS A 477 ? 0.9111 0.3707 0.7751 -0.0179 0.2640  0.0750  477 HIS A CG  
3683 N ND1 . HIS A 477 ? 0.9811 0.4538 0.8635 -0.0176 0.2519  0.0809  477 HIS A ND1 
3684 C CD2 . HIS A 477 ? 0.9050 0.3551 0.7493 -0.0245 0.2588  0.0706  477 HIS A CD2 
3685 C CE1 . HIS A 477 ? 0.9545 0.4261 0.8274 -0.0246 0.2392  0.0790  477 HIS A CE1 
3686 N NE2 . HIS A 477 ? 0.9156 0.3724 0.7655 -0.0288 0.2438  0.0723  477 HIS A NE2 
3687 N N   . ASP A 478 ? 0.8880 0.3196 0.7356 -0.0035 0.3008  0.0657  478 ASP A N   
3688 C CA  . ASP A 478 ? 0.8936 0.3225 0.7458 -0.0016 0.3134  0.0581  478 ASP A CA  
3689 C C   . ASP A 478 ? 0.8772 0.3016 0.7106 -0.0064 0.3165  0.0513  478 ASP A C   
3690 O O   . ASP A 478 ? 0.8797 0.2935 0.7026 -0.0059 0.3203  0.0491  478 ASP A O   
3691 C CB  . ASP A 478 ? 0.9403 0.3573 0.7955 0.0037  0.3172  0.0620  478 ASP A CB  
3692 C CG  . ASP A 478 ? 0.8994 0.3155 0.7697 0.0057  0.3296  0.0525  478 ASP A CG  
3693 O OD1 . ASP A 478 ? 0.9166 0.3396 0.7845 0.0023  0.3347  0.0419  478 ASP A OD1 
3694 O OD2 . ASP A 478 ? 0.8937 0.3027 0.7786 0.0106  0.3336  0.0557  478 ASP A OD2 
3695 N N   . PRO A 479 ? 0.8716 0.3045 0.7031 -0.0108 0.3151  0.0492  479 PRO A N   
3696 C CA  . PRO A 479 ? 0.9053 0.3336 0.7205 -0.0144 0.3160  0.0456  479 PRO A CA  
3697 C C   . PRO A 479 ? 0.8661 0.2940 0.6803 -0.0130 0.3245  0.0379  479 PRO A C   
3698 O O   . PRO A 479 ? 0.8634 0.3005 0.6888 -0.0116 0.3309  0.0323  479 PRO A O   
3699 C CB  . PRO A 479 ? 0.8715 0.3109 0.6911 -0.0188 0.3146  0.0472  479 PRO A CB  
3700 C CG  . PRO A 479 ? 0.8642 0.3174 0.7040 -0.0171 0.3176  0.0482  479 PRO A CG  
3701 C CD  . PRO A 479 ? 0.9120 0.3596 0.7589 -0.0125 0.3136  0.0515  479 PRO A CD  
3702 N N   . PHE A 480 ? 0.8677 0.2862 0.6697 -0.0134 0.3246  0.0361  480 PHE A N   
3703 C CA  . PHE A 480 ? 0.8651 0.2845 0.6683 -0.0129 0.3307  0.0285  480 PHE A CA  
3704 C C   . PHE A 480 ? 0.8662 0.2854 0.6832 -0.0100 0.3361  0.0246  480 PHE A C   
3705 O O   . PHE A 480 ? 0.8662 0.2854 0.6889 -0.0107 0.3422  0.0160  480 PHE A O   
3706 C CB  . PHE A 480 ? 0.8615 0.2936 0.6641 -0.0149 0.3322  0.0236  480 PHE A CB  
3707 C CG  . PHE A 480 ? 0.9040 0.3359 0.6957 -0.0171 0.3273  0.0280  480 PHE A CG  
3708 C CD1 . PHE A 480 ? 0.9068 0.3377 0.6962 -0.0192 0.3225  0.0354  480 PHE A CD1 
3709 C CD2 . PHE A 480 ? 0.8725 0.3049 0.6598 -0.0170 0.3272  0.0248  480 PHE A CD2 
3710 C CE1 . PHE A 480 ? 0.9056 0.3334 0.6885 -0.0210 0.3186  0.0397  480 PHE A CE1 
3711 C CE2 . PHE A 480 ? 0.8707 0.3016 0.6516 -0.0177 0.3228  0.0300  480 PHE A CE2 
3712 C CZ  . PHE A 480 ? 0.9275 0.3548 0.7062 -0.0197 0.3190  0.0375  480 PHE A CZ  
3713 N N   . ALA A 481 ? 0.8696 0.2873 0.6938 -0.0070 0.3338  0.0309  481 ALA A N   
3714 C CA  . ALA A 481 ? 0.9411 0.3580 0.7831 -0.0035 0.3388  0.0295  481 ALA A CA  
3715 C C   . ALA A 481 ? 0.9088 0.3272 0.7653 -0.0034 0.3478  0.0195  481 ALA A C   
3716 O O   . ALA A 481 ? 0.8901 0.3075 0.7635 -0.0013 0.3537  0.0131  481 ALA A O   
3717 C CB  . ALA A 481 ? 0.8737 0.2901 0.7175 -0.0034 0.3409  0.0272  481 ALA A CB  
3718 N N   . MET A 482 ? 0.8905 0.3225 0.7424 -0.0053 0.3462  0.0169  482 MET A N   
3719 C CA  . MET A 482 ? 0.8684 0.3137 0.7286 -0.0054 0.3529  0.0052  482 MET A CA  
3720 C C   . MET A 482 ? 0.8686 0.3250 0.7415 -0.0032 0.3546  0.0079  482 MET A C   
3721 O O   . MET A 482 ? 0.8708 0.3409 0.7465 -0.0037 0.3612  -0.0009 482 MET A O   
3722 C CB  . MET A 482 ? 0.8665 0.3216 0.7095 -0.0098 0.3517  0.0002  482 MET A CB  
3723 C CG  . MET A 482 ? 0.9408 0.3914 0.7792 -0.0116 0.3520  -0.0078 482 MET A CG  
3724 S SD  . MET A 482 ? 0.9631 0.4269 0.8069 -0.0128 0.3587  -0.0277 482 MET A SD  
3725 C CE  . MET A 482 ? 0.9137 0.3977 0.7379 -0.0150 0.3566  -0.0255 482 MET A CE  
3726 N N   . ARG A 483 ? 0.8683 0.3209 0.7489 -0.0008 0.3490  0.0197  483 ARG A N   
3727 C CA  . ARG A 483 ? 0.8682 0.3338 0.7662 0.0013  0.3502  0.0227  483 ARG A CA  
3728 C C   . ARG A 483 ? 0.9401 0.4127 0.8596 0.0058  0.3618  0.0112  483 ARG A C   
3729 O O   . ARG A 483 ? 0.9846 0.4736 0.9108 0.0055  0.3680  0.0069  483 ARG A O   
3730 C CB  . ARG A 483 ? 0.8700 0.3308 0.7770 0.0042  0.3406  0.0363  483 ARG A CB  
3731 C CG  . ARG A 483 ? 0.9230 0.4001 0.8500 0.0052  0.3392  0.0409  483 ARG A CG  
3732 C CD  . ARG A 483 ? 0.9801 0.4552 0.9224 0.0098  0.3293  0.0529  483 ARG A CD  
3733 N NE  . ARG A 483 ? 1.0437 0.5120 1.0060 0.0180  0.3344  0.0527  483 ARG A NE  
3734 C CZ  . ARG A 483 ? 1.1662 0.6174 1.1215 0.0208  0.3321  0.0578  483 ARG A CZ  
3735 N NH1 . ARG A 483 ? 1.1483 0.5885 1.0753 0.0165  0.3253  0.0625  483 ARG A NH1 
3736 N NH2 . ARG A 483 ? 1.2552 0.6996 1.2337 0.0282  0.3381  0.0585  483 ARG A NH2 
3737 N N   . PRO A 484 ? 0.9462 0.4071 0.8782 0.0099  0.3664  0.0055  484 PRO A N   
3738 C CA  . PRO A 484 ? 0.9071 0.3730 0.8626 0.0145  0.3782  -0.0080 484 PRO A CA  
3739 C C   . PRO A 484 ? 0.8923 0.3661 0.8363 0.0107  0.3868  -0.0272 484 PRO A C   
3740 O O   . PRO A 484 ? 0.9140 0.3931 0.8747 0.0139  0.3976  -0.0421 484 PRO A O   
3741 C CB  . PRO A 484 ? 0.8936 0.3403 0.8675 0.0195  0.3791  -0.0055 484 PRO A CB  
3742 C CG  . PRO A 484 ? 0.9251 0.3604 0.8840 0.0182  0.3674  0.0124  484 PRO A CG  
3743 C CD  . PRO A 484 ? 0.9279 0.3697 0.8569 0.0110  0.3617  0.0126  484 PRO A CD  
3744 N N   . PHE A 485 ? 0.8870 0.3625 0.8036 0.0044  0.3820  -0.0281 485 PHE A N   
3745 C CA  . PHE A 485 ? 0.8943 0.3769 0.7991 0.0009  0.3871  -0.0459 485 PHE A CA  
3746 C C   . PHE A 485 ? 0.8984 0.3981 0.7772 -0.0039 0.3852  -0.0449 485 PHE A C   
3747 O O   . PHE A 485 ? 0.9026 0.4105 0.7673 -0.0069 0.3870  -0.0581 485 PHE A O   
3748 C CB  . PHE A 485 ? 0.8942 0.3623 0.7953 -0.0018 0.3831  -0.0500 485 PHE A CB  
3749 C CG  . PHE A 485 ? 0.9102 0.3589 0.8336 0.0021  0.3840  -0.0446 485 PHE A CG  
3750 C CD1 . PHE A 485 ? 0.9060 0.3492 0.8568 0.0065  0.3931  -0.0553 485 PHE A CD1 
3751 C CD2 . PHE A 485 ? 0.8894 0.3250 0.8064 0.0017  0.3766  -0.0285 485 PHE A CD2 
3752 C CE1 . PHE A 485 ? 0.9516 0.3759 0.9243 0.0105  0.3941  -0.0472 485 PHE A CE1 
3753 C CE2 . PHE A 485 ? 0.9200 0.3386 0.8545 0.0053  0.3780  -0.0208 485 PHE A CE2 
3754 C CZ  . PHE A 485 ? 0.9026 0.3214 0.8659 0.0094  0.3842  -0.0282 485 PHE A CZ  
3755 N N   . PHE A 486 ? 0.8875 0.3931 0.7605 -0.0049 0.3812  -0.0293 486 PHE A N   
3756 C CA  . PHE A 486 ? 0.9059 0.4259 0.7564 -0.0094 0.3801  -0.0253 486 PHE A CA  
3757 C C   . PHE A 486 ? 0.9050 0.4437 0.7506 -0.0094 0.3915  -0.0396 486 PHE A C   
3758 O O   . PHE A 486 ? 0.9100 0.4563 0.7732 -0.0060 0.4016  -0.0450 486 PHE A O   
3759 C CB  . PHE A 486 ? 0.9075 0.4302 0.7601 -0.0110 0.3760  -0.0074 486 PHE A CB  
3760 C CG  . PHE A 486 ? 0.8736 0.3805 0.7206 -0.0127 0.3639  0.0051  486 PHE A CG  
3761 C CD1 . PHE A 486 ? 0.8728 0.3731 0.7013 -0.0152 0.3578  0.0056  486 PHE A CD1 
3762 C CD2 . PHE A 486 ? 0.8979 0.3976 0.7588 -0.0114 0.3584  0.0152  486 PHE A CD2 
3763 C CE1 . PHE A 486 ? 0.8924 0.3781 0.7161 -0.0162 0.3487  0.0149  486 PHE A CE1 
3764 C CE2 . PHE A 486 ? 0.8633 0.3487 0.7158 -0.0130 0.3479  0.0241  486 PHE A CE2 
3765 C CZ  . PHE A 486 ? 0.8764 0.3543 0.7103 -0.0153 0.3442  0.0234  486 PHE A CZ  
3766 N N   . GLY A 487 ? 0.9144 0.4619 0.7360 -0.0129 0.3900  -0.0463 487 GLY A N   
3767 C CA  . GLY A 487 ? 0.9335 0.5008 0.7434 -0.0134 0.4001  -0.0606 487 GLY A CA  
3768 C C   . GLY A 487 ? 0.9509 0.5362 0.7479 -0.0153 0.4057  -0.0483 487 GLY A C   
3769 O O   . GLY A 487 ? 0.9590 0.5622 0.7483 -0.0150 0.4177  -0.0589 487 GLY A O   
3770 N N   . TYR A 488 ? 0.9469 0.5275 0.7420 -0.0177 0.3984  -0.0267 488 TYR A N   
3771 C CA  . TYR A 488 ? 0.9379 0.5337 0.7228 -0.0209 0.4033  -0.0121 488 TYR A CA  
3772 C C   . TYR A 488 ? 0.9220 0.5065 0.7214 -0.0229 0.3959  0.0079  488 TYR A C   
3773 O O   . TYR A 488 ? 0.9069 0.4735 0.7199 -0.0213 0.3870  0.0093  488 TYR A O   
3774 C CB  . TYR A 488 ? 0.9540 0.5610 0.7058 -0.0241 0.3999  -0.0085 488 TYR A CB  
3775 C CG  . TYR A 488 ? 0.9444 0.5369 0.6877 -0.0252 0.3841  -0.0003 488 TYR A CG  
3776 C CD1 . TYR A 488 ? 0.9577 0.5412 0.7013 -0.0236 0.3771  -0.0145 488 TYR A CD1 
3777 C CD2 . TYR A 488 ? 0.9413 0.5291 0.6799 -0.0278 0.3773  0.0212  488 TYR A CD2 
3778 C CE1 . TYR A 488 ? 1.0269 0.5990 0.7658 -0.0242 0.3643  -0.0074 488 TYR A CE1 
3779 C CE2 . TYR A 488 ? 0.9490 0.5236 0.6826 -0.0278 0.3643  0.0275  488 TYR A CE2 
3780 C CZ  . TYR A 488 ? 1.0362 0.6041 0.7699 -0.0257 0.3581  0.0133  488 TYR A CZ  
3781 O OH  . TYR A 488 ? 0.9859 0.5426 0.7177 -0.0253 0.3467  0.0194  488 TYR A OH  
3782 N N   . ASN A 489 ? 0.9469 0.5423 0.7428 -0.0268 0.3999  0.0232  489 ASN A N   
3783 C CA  . ASN A 489 ? 0.9180 0.5044 0.7287 -0.0303 0.3932  0.0409  489 ASN A CA  
3784 C C   . ASN A 489 ? 0.9253 0.4893 0.7328 -0.0304 0.3777  0.0446  489 ASN A C   
3785 O O   . ASN A 489 ? 0.9256 0.4850 0.7133 -0.0303 0.3718  0.0442  489 ASN A O   
3786 C CB  . ASN A 489 ? 0.9622 0.5607 0.7626 -0.0358 0.3982  0.0578  489 ASN A CB  
3787 C CG  . ASN A 489 ? 0.9239 0.5141 0.7442 -0.0408 0.3927  0.0743  489 ASN A CG  
3788 O OD1 . ASN A 489 ? 0.9711 0.5436 0.7888 -0.0426 0.3802  0.0814  489 ASN A OD1 
3789 N ND2 . ASN A 489 ? 0.9261 0.5298 0.7684 -0.0434 0.4023  0.0793  489 ASN A ND2 
3790 N N   . PHE A 490 ? 0.9176 0.4693 0.7450 -0.0302 0.3711  0.0479  490 PHE A N   
3791 C CA  . PHE A 490 ? 0.8834 0.4143 0.7069 -0.0298 0.3583  0.0494  490 PHE A CA  
3792 C C   . PHE A 490 ? 0.9165 0.4398 0.7307 -0.0344 0.3514  0.0627  490 PHE A C   
3793 O O   . PHE A 490 ? 0.9262 0.4366 0.7288 -0.0334 0.3440  0.0623  490 PHE A O   
3794 C CB  . PHE A 490 ? 0.9181 0.4398 0.7617 -0.0282 0.3529  0.0490  490 PHE A CB  
3795 C CG  . PHE A 490 ? 0.9467 0.4483 0.7839 -0.0283 0.3410  0.0513  490 PHE A CG  
3796 C CD1 . PHE A 490 ? 0.8687 0.3599 0.6915 -0.0257 0.3387  0.0449  490 PHE A CD1 
3797 C CD2 . PHE A 490 ? 0.8869 0.3814 0.7335 -0.0315 0.3325  0.0586  490 PHE A CD2 
3798 C CE1 . PHE A 490 ? 0.8770 0.3511 0.6939 -0.0256 0.3302  0.0466  490 PHE A CE1 
3799 C CE2 . PHE A 490 ? 0.9033 0.3800 0.7409 -0.0315 0.3229  0.0586  490 PHE A CE2 
3800 C CZ  . PHE A 490 ? 0.8654 0.3319 0.6878 -0.0282 0.3228  0.0530  490 PHE A CZ  
3801 N N   . GLY A 491 ? 0.9251 0.4559 0.7477 -0.0394 0.3545  0.0746  491 GLY A N   
3802 C CA  . GLY A 491 ? 0.8997 0.4225 0.7163 -0.0438 0.3495  0.0880  491 GLY A CA  
3803 C C   . GLY A 491 ? 0.9091 0.4345 0.7025 -0.0417 0.3497  0.0901  491 GLY A C   
3804 O O   . GLY A 491 ? 0.9207 0.4324 0.7075 -0.0411 0.3415  0.0945  491 GLY A O   
3805 N N   . LYS A 492 ? 0.9184 0.4627 0.6995 -0.0402 0.3588  0.0862  492 LYS A N   
3806 C CA  . LYS A 492 ? 0.9426 0.4931 0.7000 -0.0379 0.3569  0.0866  492 LYS A CA  
3807 C C   . LYS A 492 ? 0.9195 0.4595 0.6724 -0.0335 0.3486  0.0730  492 LYS A C   
3808 O O   . LYS A 492 ? 0.9606 0.5004 0.7002 -0.0317 0.3422  0.0752  492 LYS A O   
3809 C CB  . LYS A 492 ? 0.9456 0.5203 0.6883 -0.0376 0.3684  0.0821  492 LYS A CB  
3810 C CG  . LYS A 492 ? 0.9580 0.5461 0.7058 -0.0422 0.3799  0.0960  492 LYS A CG  
3811 C CD  . LYS A 492 ? 1.0247 0.6051 0.7721 -0.0462 0.3753  0.1192  492 LYS A CD  
3812 C CE  . LYS A 492 ? 1.0996 0.6902 0.8604 -0.0523 0.3870  0.1342  492 LYS A CE  
3813 N NZ  . LYS A 492 ? 1.0259 0.6028 0.7957 -0.0571 0.3818  0.1559  492 LYS A NZ  
3814 N N   . TYR A 493 ? 0.9107 0.4430 0.6764 -0.0315 0.3488  0.0602  493 TYR A N   
3815 C CA  . TYR A 493 ? 0.9154 0.4353 0.6805 -0.0282 0.3422  0.0496  493 TYR A CA  
3816 C C   . TYR A 493 ? 0.9220 0.4243 0.6884 -0.0285 0.3330  0.0585  493 TYR A C   
3817 O O   . TYR A 493 ? 0.9391 0.4388 0.6979 -0.0265 0.3277  0.0582  493 TYR A O   
3818 C CB  . TYR A 493 ? 0.8863 0.4004 0.6664 -0.0262 0.3453  0.0384  493 TYR A CB  
3819 C CG  . TYR A 493 ? 0.8786 0.3793 0.6608 -0.0234 0.3408  0.0290  493 TYR A CG  
3820 C CD1 . TYR A 493 ? 0.9061 0.4124 0.6856 -0.0217 0.3434  0.0152  493 TYR A CD1 
3821 C CD2 . TYR A 493 ? 0.9252 0.4083 0.7127 -0.0230 0.3349  0.0334  493 TYR A CD2 
3822 C CE1 . TYR A 493 ? 0.8755 0.3699 0.6607 -0.0200 0.3409  0.0078  493 TYR A CE1 
3823 C CE2 . TYR A 493 ? 0.9430 0.4149 0.7322 -0.0207 0.3331  0.0265  493 TYR A CE2 
3824 C CZ  . TYR A 493 ? 0.8703 0.3478 0.6600 -0.0194 0.3365  0.0146  493 TYR A CZ  
3825 O OH  . TYR A 493 ? 0.9067 0.3733 0.7015 -0.0180 0.3361  0.0088  493 TYR A OH  
3826 N N   . LEU A 494 ? 0.9028 0.3940 0.6806 -0.0309 0.3310  0.0655  494 LEU A N   
3827 C CA  . LEU A 494 ? 0.8883 0.3618 0.6677 -0.0314 0.3234  0.0716  494 LEU A CA  
3828 C C   . LEU A 494 ? 0.9523 0.4277 0.7241 -0.0313 0.3210  0.0827  494 LEU A C   
3829 O O   . LEU A 494 ? 0.9301 0.3959 0.6998 -0.0284 0.3156  0.0826  494 LEU A O   
3830 C CB  . LEU A 494 ? 0.9115 0.3764 0.7040 -0.0357 0.3214  0.0768  494 LEU A CB  
3831 C CG  . LEU A 494 ? 0.8791 0.3408 0.6797 -0.0349 0.3205  0.0682  494 LEU A CG  
3832 C CD1 . LEU A 494 ? 0.8810 0.3401 0.6960 -0.0399 0.3170  0.0735  494 LEU A CD1 
3833 C CD2 . LEU A 494 ? 0.9046 0.3514 0.6986 -0.0312 0.3161  0.0606  494 LEU A CD2 
3834 N N   . ALA A 495 ? 1.0195 0.5080 0.7882 -0.0341 0.3254  0.0937  495 ALA A N   
3835 C CA  . ALA A 495 ? 1.0340 0.5254 0.7948 -0.0335 0.3228  0.1078  495 ALA A CA  
3836 C C   . ALA A 495 ? 1.0613 0.5616 0.8086 -0.0284 0.3187  0.1017  495 ALA A C   
3837 O O   . ALA A 495 ? 1.0652 0.5603 0.8119 -0.0253 0.3120  0.1090  495 ALA A O   
3838 C CB  . ALA A 495 ? 0.9849 0.4919 0.7417 -0.0375 0.3303  0.1215  495 ALA A CB  
3839 N N   . HIS A 496 ? 0.9720 0.4861 0.7114 -0.0274 0.3224  0.0875  496 HIS A N   
3840 C CA  . HIS A 496 ? 0.9376 0.4614 0.6672 -0.0239 0.3175  0.0785  496 HIS A CA  
3841 C C   . HIS A 496 ? 1.0080 0.5159 0.7482 -0.0207 0.3107  0.0738  496 HIS A C   
3842 O O   . HIS A 496 ? 0.9542 0.4661 0.6924 -0.0175 0.3036  0.0768  496 HIS A O   
3843 C CB  . HIS A 496 ? 0.9751 0.5115 0.7001 -0.0243 0.3235  0.0602  496 HIS A CB  
3844 C CG  . HIS A 496 ? 1.0356 0.5864 0.7499 -0.0225 0.3187  0.0493  496 HIS A CG  
3845 N ND1 . HIS A 496 ? 0.9868 0.5527 0.6854 -0.0215 0.3122  0.0587  496 HIS A ND1 
3846 C CD2 . HIS A 496 ? 0.9316 0.4847 0.6503 -0.0220 0.3186  0.0299  496 HIS A CD2 
3847 C CE1 . HIS A 496 ? 0.9888 0.5673 0.6819 -0.0206 0.3071  0.0440  496 HIS A CE1 
3848 N NE2 . HIS A 496 ? 0.9625 0.5328 0.6688 -0.0214 0.3114  0.0259  496 HIS A NE2 
3849 N N   . TRP A 497 ? 0.9603 0.4516 0.7120 -0.0212 0.3127  0.0671  497 TRP A N   
3850 C CA  . TRP A 497 ? 0.9169 0.3935 0.6770 -0.0183 0.3089  0.0622  497 TRP A CA  
3851 C C   . TRP A 497 ? 1.0272 0.4932 0.7921 -0.0164 0.3038  0.0748  497 TRP A C   
3852 O O   . TRP A 497 ? 0.9728 0.4380 0.7421 -0.0123 0.2994  0.0744  497 TRP A O   
3853 C CB  . TRP A 497 ? 0.8836 0.3458 0.6506 -0.0195 0.3125  0.0545  497 TRP A CB  
3854 C CG  . TRP A 497 ? 0.9128 0.3791 0.6817 -0.0188 0.3162  0.0408  497 TRP A CG  
3855 C CD1 . TRP A 497 ? 0.8809 0.3585 0.6488 -0.0200 0.3210  0.0338  497 TRP A CD1 
3856 C CD2 . TRP A 497 ? 0.8712 0.3295 0.6459 -0.0168 0.3166  0.0325  497 TRP A CD2 
3857 N NE1 . TRP A 497 ? 0.9433 0.4185 0.7175 -0.0190 0.3237  0.0216  497 TRP A NE1 
3858 C CE2 . TRP A 497 ? 0.8681 0.3319 0.6463 -0.0175 0.3212  0.0216  497 TRP A CE2 
3859 C CE3 . TRP A 497 ? 0.8705 0.3174 0.6494 -0.0145 0.3149  0.0331  497 TRP A CE3 
3860 C CZ2 . TRP A 497 ? 0.8708 0.3286 0.6574 -0.0167 0.3238  0.0132  497 TRP A CZ2 
3861 C CZ3 . TRP A 497 ? 0.8838 0.3269 0.6692 -0.0135 0.3184  0.0244  497 TRP A CZ3 
3862 C CH2 . TRP A 497 ? 0.8635 0.3117 0.6530 -0.0150 0.3226  0.0155  497 TRP A CH2 
3863 N N   . LEU A 498 ? 1.0221 0.4797 0.7899 -0.0193 0.3047  0.0857  498 LEU A N   
3864 C CA  . LEU A 498 ? 0.9530 0.3974 0.7289 -0.0178 0.3007  0.0973  498 LEU A CA  
3865 C C   . LEU A 498 ? 1.0047 0.4612 0.7772 -0.0138 0.2958  0.1090  498 LEU A C   
3866 O O   . LEU A 498 ? 1.0451 0.4925 0.8276 -0.0092 0.2914  0.1146  498 LEU A O   
3867 C CB  . LEU A 498 ? 0.9227 0.3579 0.7046 -0.0232 0.3028  0.1070  498 LEU A CB  
3868 C CG  . LEU A 498 ? 0.9266 0.3509 0.7133 -0.0271 0.3047  0.0965  498 LEU A CG  
3869 C CD1 . LEU A 498 ? 0.9201 0.3423 0.7151 -0.0339 0.3063  0.1055  498 LEU A CD1 
3870 C CD2 . LEU A 498 ? 0.9122 0.3184 0.7044 -0.0245 0.3013  0.0875  498 LEU A CD2 
3871 N N   . SER A 499 ? 1.0129 0.4909 0.7714 -0.0149 0.2964  0.1124  499 SER A N   
3872 C CA  . SER A 499 ? 1.0598 0.5528 0.8112 -0.0111 0.2901  0.1247  499 SER A CA  
3873 C C   . SER A 499 ? 1.0463 0.5432 0.8040 -0.0053 0.2827  0.1167  499 SER A C   
3874 O O   . SER A 499 ? 1.1133 0.6176 0.8730 -0.0005 0.2749  0.1289  499 SER A O   
3875 C CB  . SER A 499 ? 1.0193 0.5368 0.7497 -0.0138 0.2927  0.1256  499 SER A CB  
3876 O OG  . SER A 499 ? 1.1265 0.6551 0.8510 -0.0142 0.2939  0.1048  499 SER A OG  
3877 N N   A MET A 500 ? 1.0623 0.5553 0.8256 -0.0055 0.2851  0.0978  500 MET A N   
3878 N N   B MET A 500 ? 1.0528 0.5460 0.8159 -0.0056 0.2852  0.0977  500 MET A N   
3879 C CA  A MET A 500 ? 1.0490 0.5473 0.8224 -0.0009 0.2796  0.0900  500 MET A CA  
3880 C CA  B MET A 500 ? 1.0820 0.5797 0.8555 -0.0010 0.2798  0.0896  500 MET A CA  
3881 C C   A MET A 500 ? 1.1323 0.6161 0.9235 0.0049  0.2762  0.0992  500 MET A C   
3882 C C   B MET A 500 ? 1.1184 0.6024 0.9093 0.0049  0.2762  0.0995  500 MET A C   
3883 O O   A MET A 500 ? 1.1684 0.6617 0.9703 0.0103  0.2693  0.1005  500 MET A O   
3884 O O   B MET A 500 ? 1.1391 0.6331 0.9401 0.0102  0.2690  0.1016  500 MET A O   
3885 C CB  A MET A 500 ? 1.0446 0.5386 0.8227 -0.0030 0.2852  0.0702  500 MET A CB  
3886 C CB  B MET A 500 ? 1.0473 0.5388 0.8262 -0.0030 0.2858  0.0703  500 MET A CB  
3887 C CG  A MET A 500 ? 1.0490 0.5557 0.8145 -0.0077 0.2891  0.0592  500 MET A CG  
3888 C CG  B MET A 500 ? 1.0516 0.5558 0.8189 -0.0076 0.2895  0.0584  500 MET A CG  
3889 S SD  A MET A 500 ? 1.1848 0.7221 0.9364 -0.0078 0.2810  0.0580  500 MET A SD  
3890 S SD  B MET A 500 ? 0.9719 0.4632 0.7480 -0.0099 0.2980  0.0409  500 MET A SD  
3891 C CE  A MET A 500 ? 1.0001 0.5448 0.7407 -0.0133 0.2898  0.0408  500 MET A CE  
3892 C CE  B MET A 500 ? 1.0270 0.5191 0.8208 -0.0064 0.2949  0.0342  500 MET A CE  
3893 N N   . ALA A 501 ? 1.0815 0.5432 0.8785 0.0040  0.2807  0.1046  501 ALA A N   
3894 C CA  . ALA A 501 ? 1.1103 0.5558 0.9257 0.0096  0.2788  0.1118  501 ALA A CA  
3895 C C   . ALA A 501 ? 1.2274 0.6799 1.0470 0.0141  0.2712  0.1332  501 ALA A C   
3896 O O   . ALA A 501 ? 1.1654 0.6060 1.0043 0.0204  0.2688  0.1405  501 ALA A O   
3897 C CB  . ALA A 501 ? 1.1140 0.5338 0.9337 0.0062  0.2851  0.1095  501 ALA A CB  
3898 N N   . HIS A 502 ? 1.2344 0.7059 1.0365 0.0115  0.2678  0.1438  502 HIS A N   
3899 C CA  . HIS A 502 ? 1.2566 0.7373 1.0582 0.0157  0.2602  0.1672  502 HIS A CA  
3900 C C   . HIS A 502 ? 1.3314 0.8385 1.1301 0.0212  0.2490  0.1684  502 HIS A C   
3901 O O   . HIS A 502 ? 1.4468 0.9631 1.2468 0.0266  0.2402  0.1891  502 HIS A O   
3902 C CB  . HIS A 502 ? 1.2924 0.7800 1.0740 0.0094  0.2640  0.1808  502 HIS A CB  
3903 C CG  . HIS A 502 ? 1.3040 0.7691 1.0919 0.0031  0.2734  0.1815  502 HIS A CG  
3904 N ND1 . HIS A 502 ? 1.3643 0.8354 1.1382 -0.0044 0.2803  0.1863  502 HIS A ND1 
3905 C CD2 . HIS A 502 ? 1.3079 0.7461 1.1159 0.0028  0.2767  0.1770  502 HIS A CD2 
3906 C CE1 . HIS A 502 ? 1.3815 0.8311 1.1688 -0.0093 0.2862  0.1853  502 HIS A CE1 
3907 N NE2 . HIS A 502 ? 1.3728 0.8018 1.1792 -0.0053 0.2837  0.1790  502 HIS A NE2 
3908 N N   . ARG A 503 ? 1.3295 0.8493 1.1258 0.0199  0.2483  0.1475  503 ARG A N   
3909 C CA  . ARG A 503 ? 1.4744 1.0220 1.2685 0.0234  0.2365  0.1459  503 ARG A CA  
3910 C C   . ARG A 503 ? 1.6196 1.1662 1.4423 0.0329  0.2281  0.1535  503 ARG A C   
3911 O O   . ARG A 503 ? 1.5491 1.0735 1.3943 0.0361  0.2345  0.1497  503 ARG A O   
3912 C CB  . ARG A 503 ? 1.4416 1.0003 1.2313 0.0184  0.2390  0.1201  503 ARG A CB  
3913 C CG  . ARG A 503 ? 1.3304 0.8901 1.0965 0.0102  0.2479  0.1105  503 ARG A CG  
3914 C CD  . ARG A 503 ? 1.4133 0.9825 1.1796 0.0060  0.2500  0.0857  503 ARG A CD  
3915 N NE  . ARG A 503 ? 1.5017 1.0998 1.2618 0.0063  0.2381  0.0803  503 ARG A NE  
3916 C CZ  . ARG A 503 ? 1.4508 1.0684 1.1860 0.0021  0.2363  0.0744  503 ARG A CZ  
3917 N NH1 . ARG A 503 ? 1.3824 0.9946 1.0988 -0.0023 0.2469  0.0738  503 ARG A NH1 
3918 N NH2 . ARG A 503 ? 1.4922 1.1368 1.2223 0.0022  0.2235  0.0677  503 ARG A NH2 
3919 N N   . PRO A 504 ? 1.8117 1.3837 1.6344 0.0380  0.2136  0.1638  504 PRO A N   
3920 C CA  . PRO A 504 ? 1.8323 1.4068 1.6869 0.0482  0.2046  0.1722  504 PRO A CA  
3921 C C   . PRO A 504 ? 1.8137 1.3912 1.6918 0.0487  0.2070  0.1490  504 PRO A C   
3922 O O   . PRO A 504 ? 1.8122 1.4070 1.6814 0.0427  0.2056  0.1310  504 PRO A O   
3923 C CB  . PRO A 504 ? 1.8845 1.4906 1.7276 0.0523  0.1866  0.1892  504 PRO A CB  
3924 C CG  . PRO A 504 ? 1.8826 1.4959 1.6853 0.0447  0.1893  0.1951  504 PRO A CG  
3925 C CD  . PRO A 504 ? 1.8460 1.4462 1.6388 0.0352  0.2044  0.1707  504 PRO A CD  
3926 N N   . ALA A 505 ? 1.5583 1.1185 1.4681 0.0557  0.2119  0.1494  505 ALA A N   
3927 C CA  . ALA A 505 ? 1.3697 0.9328 1.3059 0.0572  0.2163  0.1303  505 ALA A CA  
3928 C C   . ALA A 505 ? 1.3319 0.8896 1.2529 0.0468  0.2281  0.1074  505 ALA A C   
3929 O O   . ALA A 505 ? 1.3004 0.8722 1.2330 0.0442  0.2283  0.0915  505 ALA A O   
3930 C CB  . ALA A 505 ? 1.3122 0.9089 1.2675 0.0620  0.2001  0.1317  505 ALA A CB  
3931 N N   . ALA A 506 ? 1.3550 0.8923 1.2526 0.0409  0.2379  0.1068  506 ALA A N   
3932 C CA  . ALA A 506 ? 1.2792 0.8097 1.1625 0.0321  0.2487  0.0882  506 ALA A CA  
3933 C C   . ALA A 506 ? 1.2218 0.7339 1.1237 0.0334  0.2613  0.0760  506 ALA A C   
3934 O O   . ALA A 506 ? 1.2406 0.7297 1.1475 0.0368  0.2682  0.0803  506 ALA A O   
3935 C CB  . ALA A 506 ? 1.3150 0.8322 1.1709 0.0262  0.2541  0.0929  506 ALA A CB  
3936 N N   . LYS A 507 ? 1.2043 0.7264 1.1163 0.0304  0.2649  0.0605  507 LYS A N   
3937 C CA  . LYS A 507 ? 1.1176 0.6244 1.0434 0.0307  0.2789  0.0492  507 LYS A CA  
3938 C C   . LYS A 507 ? 1.0896 0.5794 0.9918 0.0232  0.2894  0.0412  507 LYS A C   
3939 O O   . LYS A 507 ? 1.0995 0.5943 0.9994 0.0174  0.2940  0.0300  507 LYS A O   
3940 C CB  . LYS A 507 ? 1.1161 0.6423 1.0678 0.0307  0.2787  0.0388  507 LYS A CB  
3941 C CG  . LYS A 507 ? 1.2034 0.7500 1.1828 0.0388  0.2666  0.0468  507 LYS A CG  
3942 C CD  . LYS A 507 ? 1.1834 0.7540 1.1896 0.0365  0.2643  0.0353  507 LYS A CD  
3943 C CE  . LYS A 507 ? 1.1802 0.7763 1.2144 0.0444  0.2485  0.0441  507 LYS A CE  
3944 N NZ  . LYS A 507 ? 1.2222 0.8461 1.2824 0.0402  0.2427  0.0320  507 LYS A NZ  
3945 N N   . LEU A 508 ? 1.1262 0.5959 1.0134 0.0232  0.2926  0.0476  508 LEU A N   
3946 C CA  . LEU A 508 ? 1.0797 0.5349 0.9458 0.0168  0.3003  0.0419  508 LEU A CA  
3947 C C   . LEU A 508 ? 1.0424 0.4868 0.9133 0.0159  0.3126  0.0306  508 LEU A C   
3948 O O   . LEU A 508 ? 1.0926 0.5271 0.9752 0.0209  0.3187  0.0291  508 LEU A O   
3949 C CB  . LEU A 508 ? 0.9600 0.3969 0.8141 0.0168  0.3001  0.0507  508 LEU A CB  
3950 C CG  . LEU A 508 ? 1.0662 0.5110 0.9155 0.0175  0.2901  0.0656  508 LEU A CG  
3951 C CD1 . LEU A 508 ? 0.9814 0.4051 0.8267 0.0170  0.2918  0.0736  508 LEU A CD1 
3952 C CD2 . LEU A 508 ? 1.0337 0.4953 0.8657 0.0117  0.2865  0.0652  508 LEU A CD2 
3953 N N   . PRO A 509 ? 0.9823 0.4281 0.8448 0.0102  0.3176  0.0229  509 PRO A N   
3954 C CA  . PRO A 509 ? 0.9936 0.4292 0.8584 0.0092  0.3302  0.0152  509 PRO A CA  
3955 C C   . PRO A 509 ? 1.0382 0.4518 0.8839 0.0088  0.3359  0.0160  509 PRO A C   
3956 O O   . PRO A 509 ? 0.9327 0.3397 0.7638 0.0070  0.3305  0.0208  509 PRO A O   
3957 C CB  . PRO A 509 ? 0.9006 0.3444 0.7639 0.0031  0.3319  0.0093  509 PRO A CB  
3958 C CG  . PRO A 509 ? 0.9175 0.3671 0.7666 0.0004  0.3228  0.0127  509 PRO A CG  
3959 C CD  . PRO A 509 ? 1.0150 0.4723 0.8669 0.0047  0.3129  0.0211  509 PRO A CD  
3960 N N   . LYS A 510 ? 0.9312 0.3351 0.7776 0.0102  0.3472  0.0108  510 LYS A N   
3961 C CA  . LYS A 510 ? 0.8998 0.2936 0.7265 0.0092  0.3495  0.0093  510 LYS A CA  
3962 C C   . LYS A 510 ? 0.8938 0.2899 0.7036 0.0037  0.3465  0.0107  510 LYS A C   
3963 O O   . LYS A 510 ? 0.8859 0.2886 0.7006 0.0008  0.3470  0.0109  510 LYS A O   
3964 C CB  . LYS A 510 ? 0.9109 0.2996 0.7385 0.0116  0.3625  0.0033  510 LYS A CB  
3965 C CG  . LYS A 510 ? 0.9868 0.3722 0.8314 0.0183  0.3662  0.0004  510 LYS A CG  
3966 C CD  . LYS A 510 ? 0.9614 0.3370 0.7963 0.0203  0.3788  -0.0070 510 LYS A CD  
3967 C CE  . LYS A 510 ? 0.9481 0.3193 0.7985 0.0272  0.3800  -0.0111 510 LYS A CE  
3968 N NZ  . LYS A 510 ? 1.0849 0.4524 0.9337 0.0272  0.3653  -0.0067 510 LYS A NZ  
3969 N N   . ILE A 511 ? 0.8999 0.2892 0.6918 0.0023  0.3435  0.0110  511 ILE A N   
3970 C CA  . ILE A 511 ? 0.8962 0.2867 0.6747 -0.0016 0.3395  0.0135  511 ILE A CA  
3971 C C   . ILE A 511 ? 0.9116 0.2900 0.6712 -0.0020 0.3448  0.0115  511 ILE A C   
3972 O O   . ILE A 511 ? 0.9255 0.2921 0.6750 -0.0013 0.3446  0.0082  511 ILE A O   
3973 C CB  . ILE A 511 ? 0.8917 0.2836 0.6673 -0.0037 0.3289  0.0176  511 ILE A CB  
3974 C CG1 . ILE A 511 ? 0.9058 0.3054 0.6930 -0.0038 0.3262  0.0211  511 ILE A CG1 
3975 C CG2 . ILE A 511 ? 0.8915 0.2827 0.6550 -0.0069 0.3255  0.0195  511 ILE A CG2 
3976 C CD1 . ILE A 511 ? 0.9494 0.3492 0.7335 -0.0060 0.3188  0.0274  511 ILE A CD1 
3977 N N   . PHE A 512 ? 0.9240 0.3026 0.6782 -0.0033 0.3502  0.0137  512 PHE A N   
3978 C CA  . PHE A 512 ? 0.9338 0.2969 0.6657 -0.0036 0.3568  0.0147  512 PHE A CA  
3979 C C   . PHE A 512 ? 0.9332 0.2961 0.6559 -0.0058 0.3499  0.0209  512 PHE A C   
3980 O O   . PHE A 512 ? 0.9172 0.2938 0.6544 -0.0066 0.3441  0.0233  512 PHE A O   
3981 C CB  . PHE A 512 ? 0.9430 0.3030 0.6769 -0.0024 0.3720  0.0152  512 PHE A CB  
3982 C CG  . PHE A 512 ? 0.9432 0.3051 0.6923 0.0002  0.3803  0.0093  512 PHE A CG  
3983 C CD1 . PHE A 512 ? 0.9650 0.3112 0.7012 0.0030  0.3897  0.0036  512 PHE A CD1 
3984 C CD2 . PHE A 512 ? 0.9249 0.3026 0.7019 0.0004  0.3793  0.0085  512 PHE A CD2 
3985 C CE1 . PHE A 512 ? 0.9654 0.3151 0.7205 0.0067  0.3979  -0.0021 512 PHE A CE1 
3986 C CE2 . PHE A 512 ? 0.9263 0.3059 0.7210 0.0035  0.3863  0.0040  512 PHE A CE2 
3987 C CZ  . PHE A 512 ? 0.9452 0.3123 0.7309 0.0071  0.3957  -0.0008 512 PHE A CZ  
3988 N N   . HIS A 513 ? 0.9564 0.3011 0.6539 -0.0065 0.3512  0.0232  513 HIS A N   
3989 C CA  . HIS A 513 ? 0.9619 0.3037 0.6500 -0.0078 0.3458  0.0315  513 HIS A CA  
3990 C C   . HIS A 513 ? 0.9862 0.3188 0.6538 -0.0066 0.3547  0.0376  513 HIS A C   
3991 O O   . HIS A 513 ? 1.0077 0.3341 0.6533 -0.0061 0.3577  0.0332  513 HIS A O   
3992 C CB  . HIS A 513 ? 0.9675 0.3048 0.6457 -0.0102 0.3332  0.0304  513 HIS A CB  
3993 C CG  . HIS A 513 ? 0.9664 0.3087 0.6453 -0.0108 0.3249  0.0391  513 HIS A CG  
3994 N ND1 . HIS A 513 ? 1.0178 0.3575 0.6765 -0.0103 0.3203  0.0447  513 HIS A ND1 
3995 C CD2 . HIS A 513 ? 0.9485 0.2998 0.6470 -0.0112 0.3204  0.0431  513 HIS A CD2 
3996 C CE1 . HIS A 513 ? 0.9814 0.3279 0.6505 -0.0099 0.3126  0.0528  513 HIS A CE1 
3997 N NE2 . HIS A 513 ? 0.9577 0.3106 0.6514 -0.0105 0.3137  0.0512  513 HIS A NE2 
3998 N N   . VAL A 514 ? 0.9840 0.3193 0.6599 -0.0059 0.3585  0.0473  514 VAL A N   
3999 C CA  . VAL A 514 ? 1.0079 0.3370 0.6670 -0.0047 0.3672  0.0572  514 VAL A CA  
4000 C C   . VAL A 514 ? 1.0172 0.3465 0.6681 -0.0036 0.3570  0.0690  514 VAL A C   
4001 O O   . VAL A 514 ? 1.0008 0.3353 0.6679 -0.0038 0.3470  0.0698  514 VAL A O   
4002 C CB  . VAL A 514 ? 0.9993 0.3369 0.6814 -0.0039 0.3792  0.0592  514 VAL A CB  
4003 C CG1 . VAL A 514 ? 0.9882 0.3301 0.6838 -0.0044 0.3870  0.0477  514 VAL A CG1 
4004 C CG2 . VAL A 514 ? 0.9754 0.3300 0.6881 -0.0031 0.3711  0.0605  514 VAL A CG2 
4005 N N   . ASN A 515 ? 1.0462 0.3712 0.6716 -0.0021 0.3597  0.0790  515 ASN A N   
4006 C CA  . ASN A 515 ? 1.0602 0.3862 0.6778 0.0001  0.3499  0.0936  515 ASN A CA  
4007 C C   . ASN A 515 ? 1.1089 0.4290 0.7140 0.0022  0.3622  0.1095  515 ASN A C   
4008 O O   . ASN A 515 ? 1.1620 0.4797 0.7336 0.0024  0.3663  0.1118  515 ASN A O   
4009 C CB  . ASN A 515 ? 1.0764 0.4056 0.6678 -0.0006 0.3337  0.0902  515 ASN A CB  
4010 C CG  . ASN A 515 ? 1.0931 0.4262 0.6775 0.0023  0.3215  0.1066  515 ASN A CG  
4011 O OD1 . ASN A 515 ? 1.1219 0.4550 0.7285 0.0053  0.3236  0.1194  515 ASN A OD1 
4012 N ND2 . ASN A 515 ? 1.1178 0.4545 0.6727 0.0016  0.3081  0.1057  515 ASN A ND2 
4013 N N   . TRP A 516 ? 1.0771 0.3963 0.7103 0.0036  0.3684  0.1195  516 TRP A N   
4014 C CA  . TRP A 516 ? 1.0994 0.4192 0.7298 0.0060  0.3772  0.1352  516 TRP A CA  
4015 C C   . TRP A 516 ? 1.1408 0.4534 0.7454 0.0094  0.3694  0.1568  516 TRP A C   
4016 O O   . TRP A 516 ? 1.2210 0.5332 0.8144 0.0116  0.3762  0.1730  516 TRP A O   
4017 C CB  . TRP A 516 ? 1.0756 0.4087 0.7537 0.0073  0.3797  0.1339  516 TRP A CB  
4018 C CG  . TRP A 516 ? 1.0463 0.3891 0.7523 0.0042  0.3864  0.1153  516 TRP A CG  
4019 C CD1 . TRP A 516 ? 1.0224 0.3772 0.7687 0.0036  0.3853  0.1075  516 TRP A CD1 
4020 C CD2 . TRP A 516 ? 1.0437 0.3846 0.7391 0.0014  0.3954  0.1030  516 TRP A CD2 
4021 N NE1 . TRP A 516 ? 1.0023 0.3637 0.7618 0.0002  0.3916  0.0922  516 TRP A NE1 
4022 C CE2 . TRP A 516 ? 1.0149 0.3684 0.7462 -0.0006 0.3978  0.0898  516 TRP A CE2 
4023 C CE3 . TRP A 516 ? 1.0842 0.4131 0.7429 0.0002  0.4024  0.1016  516 TRP A CE3 
4024 C CZ2 . TRP A 516 ? 1.0062 0.3617 0.7408 -0.0029 0.4056  0.0774  516 TRP A CZ2 
4025 C CZ3 . TRP A 516 ? 1.1054 0.4348 0.7691 -0.0018 0.4119  0.0879  516 TRP A CZ3 
4026 C CH2 . TRP A 516 ? 1.0264 0.3695 0.7293 -0.0030 0.4128  0.0769  516 TRP A CH2 
4027 N N   . PHE A 517 ? 1.1273 0.4449 0.7284 0.0107  0.3509  0.1553  517 PHE A N   
4028 C CA  . PHE A 517 ? 1.1530 0.4729 0.7487 0.0157  0.3383  0.1750  517 PHE A CA  
4029 C C   . PHE A 517 ? 1.1715 0.5000 0.7294 0.0158  0.3205  0.1742  517 PHE A C   
4030 O O   . PHE A 517 ? 1.1905 0.5258 0.7496 0.0196  0.3040  0.1862  517 PHE A O   
4031 C CB  . PHE A 517 ? 1.1806 0.5036 0.8187 0.0183  0.3306  0.1758  517 PHE A CB  
4032 C CG  . PHE A 517 ? 1.1866 0.5127 0.8668 0.0181  0.3420  0.1697  517 PHE A CG  
4033 C CD1 . PHE A 517 ? 1.1398 0.4689 0.8420 0.0221  0.3456  0.1840  517 PHE A CD1 
4034 C CD2 . PHE A 517 ? 1.1113 0.4459 0.8122 0.0142  0.3450  0.1469  517 PHE A CD2 
4035 C CE1 . PHE A 517 ? 1.0817 0.4199 0.8250 0.0212  0.3528  0.1739  517 PHE A CE1 
4036 C CE2 . PHE A 517 ? 1.1080 0.4538 0.8469 0.0138  0.3513  0.1379  517 PHE A CE2 
4037 C CZ  . PHE A 517 ? 1.0512 0.3978 0.8111 0.0169  0.3556  0.1504  517 PHE A CZ  
4038 N N   . ARG A 518 ? 1.1866 0.5153 0.7128 0.0119  0.3229  0.1594  518 ARG A N   
4039 C CA  . ARG A 518 ? 1.3045 0.6407 0.7926 0.0112  0.3061  0.1565  518 ARG A CA  
4040 C C   . ARG A 518 ? 1.4525 0.7895 0.9083 0.0156  0.3042  0.1804  518 ARG A C   
4041 O O   . ARG A 518 ? 1.3974 0.7267 0.8421 0.0169  0.3224  0.1928  518 ARG A O   
4042 C CB  . ARG A 518 ? 1.2912 0.6251 0.7533 0.0065  0.3117  0.1338  518 ARG A CB  
4043 C CG  . ARG A 518 ? 1.3182 0.6595 0.7461 0.0041  0.2926  0.1240  518 ARG A CG  
4044 C CD  . ARG A 518 ? 1.3175 0.6541 0.7287 -0.0005 0.2985  0.0981  518 ARG A CD  
4045 N NE  . ARG A 518 ? 1.3274 0.6701 0.7159 -0.0043 0.2784  0.0842  518 ARG A NE  
4046 C CZ  . ARG A 518 ? 1.3979 0.7361 0.7805 -0.0090 0.2779  0.0595  518 ARG A CZ  
4047 N NH1 . ARG A 518 ? 1.3387 0.6675 0.7357 -0.0094 0.2959  0.0472  518 ARG A NH1 
4048 N NH2 . ARG A 518 ? 1.3682 0.7120 0.7334 -0.0133 0.2582  0.0469  518 ARG A NH2 
4049 N N   . LYS A 519 ? 1.5115 0.8592 0.9536 0.0176  0.2817  0.1881  519 LYS A N   
4050 C CA  . LYS A 519 ? 1.6526 1.0041 1.0633 0.0225  0.2752  0.2133  519 LYS A CA  
4051 C C   . LYS A 519 ? 1.8991 1.2599 1.2567 0.0197  0.2608  0.2038  519 LYS A C   
4052 O O   . LYS A 519 ? 1.8478 1.2128 1.2016 0.0142  0.2514  0.1784  519 LYS A O   
4053 C CB  . LYS A 519 ? 1.6983 1.0567 1.1399 0.0289  0.2587  0.2341  519 LYS A CB  
4054 C CG  . LYS A 519 ? 1.5624 0.9105 1.0549 0.0324  0.2731  0.2445  519 LYS A CG  
4055 C CD  . LYS A 519 ? 1.5868 0.9407 1.1067 0.0405  0.2584  0.2676  519 LYS A CD  
4056 C CE  . LYS A 519 ? 1.5330 0.8736 1.1002 0.0444  0.2749  0.2788  519 LYS A CE  
4057 N NZ  . LYS A 519 ? 1.6796 1.0233 1.2726 0.0539  0.2630  0.3045  519 LYS A NZ  
4058 N N   . ASP A 520 ? 2.3344 1.6982 1.6505 0.0234  0.2593  0.2247  520 ASP A N   
4059 C CA  . ASP A 520 ? 2.4007 1.7752 1.6605 0.0212  0.2447  0.2177  520 ASP A CA  
4060 C C   . ASP A 520 ? 2.4370 1.8282 1.6958 0.0249  0.2136  0.2327  520 ASP A C   
4061 O O   . ASP A 520 ? 2.4091 1.8035 1.7154 0.0287  0.2040  0.2437  520 ASP A O   
4062 C CB  . ASP A 520 ? 2.4309 1.8007 1.6399 0.0226  0.2635  0.2305  520 ASP A CB  
4063 C CG  . ASP A 520 ? 2.4253 1.7915 1.6406 0.0299  0.2707  0.2694  520 ASP A CG  
4064 O OD1 . ASP A 520 ? 2.3981 1.7648 1.6583 0.0344  0.2607  0.2850  520 ASP A OD1 
4065 O OD2 . ASP A 520 ? 2.4494 1.8119 1.6262 0.0312  0.2877  0.2848  520 ASP A OD2 
4066 N N   . LYS A 521 ? 2.1467 1.5500 1.3513 0.0239  0.1974  0.2325  521 LYS A N   
4067 C CA  . LYS A 521 ? 2.0544 1.4771 1.2558 0.0271  0.1651  0.2460  521 LYS A CA  
4068 C C   . LYS A 521 ? 2.0360 1.4607 1.2440 0.0373  0.1629  0.2878  521 LYS A C   
4069 O O   . LYS A 521 ? 1.9667 1.4078 1.1853 0.0420  0.1362  0.3031  521 LYS A O   
4070 C CB  . LYS A 521 ? 1.9811 1.4173 1.1195 0.0224  0.1473  0.2314  521 LYS A CB  
4071 C CG  . LYS A 521 ? 1.9823 1.4159 1.1175 0.0122  0.1463  0.1892  521 LYS A CG  
4072 C CD  . LYS A 521 ? 1.8737 1.3205 0.9473 0.0072  0.1277  0.1725  521 LYS A CD  
4073 C CE  . LYS A 521 ? 1.8646 1.3064 0.9414 -0.0030 0.1264  0.1298  521 LYS A CE  
4074 N NZ  . LYS A 521 ? 2.0181 1.4712 1.0350 -0.0087 0.1091  0.1092  521 LYS A NZ  
4075 N N   . ASN A 522 ? 2.0294 1.4383 1.2353 0.0410  0.1899  0.3070  522 ASN A N   
4076 C CA  . ASN A 522 ? 1.9726 1.3793 1.1885 0.0506  0.1910  0.3482  522 ASN A CA  
4077 C C   . ASN A 522 ? 1.9430 1.3365 1.2303 0.0547  0.2032  0.3571  522 ASN A C   
4078 O O   . ASN A 522 ? 1.8534 1.2430 1.1608 0.0632  0.2036  0.3902  522 ASN A O   
4079 C CB  . ASN A 522 ? 2.0750 1.4728 1.2413 0.0518  0.2137  0.3676  522 ASN A CB  
4080 C CG  . ASN A 522 ? 2.0421 1.4527 1.1325 0.0478  0.2050  0.3569  522 ASN A CG  
4081 O OD1 . ASN A 522 ? 1.9969 1.4250 1.0696 0.0456  0.1765  0.3420  522 ASN A OD1 
4082 N ND2 . ASN A 522 ? 1.9366 1.3394 0.9824 0.0466  0.2300  0.3633  522 ASN A ND2 
4083 N N   . GLY A 523 ? 1.9903 1.3765 1.3158 0.0490  0.2131  0.3284  523 GLY A N   
4084 C CA  . GLY A 523 ? 1.8959 1.2691 1.2837 0.0517  0.2274  0.3328  523 GLY A CA  
4085 C C   . GLY A 523 ? 1.8994 1.2529 1.2915 0.0501  0.2596  0.3375  523 GLY A C   
4086 O O   . GLY A 523 ? 1.7639 1.1054 1.2039 0.0532  0.2719  0.3475  523 GLY A O   
4087 N N   . LYS A 524 ? 2.0160 1.3663 1.3614 0.0450  0.2741  0.3294  524 LYS A N   
4088 C CA  . LYS A 524 ? 1.9862 1.3205 1.3340 0.0427  0.3054  0.3341  524 LYS A CA  
4089 C C   . LYS A 524 ? 1.9233 1.2522 1.2906 0.0352  0.3193  0.2995  524 LYS A C   
4090 O O   . LYS A 524 ? 1.9031 1.2394 1.2457 0.0305  0.3121  0.2736  524 LYS A O   
4091 C CB  . LYS A 524 ? 2.0698 1.4054 1.3546 0.0425  0.3154  0.3487  524 LYS A CB  
4092 C CG  . LYS A 524 ? 2.1282 1.4496 1.4148 0.0394  0.3495  0.3544  524 LYS A CG  
4093 C CD  . LYS A 524 ? 2.1431 1.4720 1.3671 0.0390  0.3583  0.3661  524 LYS A CD  
4094 C CE  . LYS A 524 ? 2.0560 1.3904 1.3050 0.0346  0.3837  0.3621  524 LYS A CE  
4095 N NZ  . LYS A 524 ? 1.9574 1.3028 1.1480 0.0335  0.3933  0.3698  524 LYS A NZ  
4096 N N   . PHE A 525 ? 1.7123 1.0287 1.1252 0.0342  0.3385  0.2993  525 PHE A N   
4097 C CA  . PHE A 525 ? 1.5610 0.8734 0.9944 0.0278  0.3518  0.2697  525 PHE A CA  
4098 C C   . PHE A 525 ? 1.5295 0.8425 0.9191 0.0234  0.3665  0.2573  525 PHE A C   
4099 O O   . PHE A 525 ? 1.6610 0.9705 1.0226 0.0242  0.3820  0.2753  525 PHE A O   
4100 C CB  . PHE A 525 ? 1.3782 0.6852 0.8687 0.0272  0.3668  0.2709  525 PHE A CB  
4101 C CG  . PHE A 525 ? 1.4030 0.7106 0.9435 0.0296  0.3550  0.2667  525 PHE A CG  
4102 C CD1 . PHE A 525 ? 1.4198 0.7307 0.9601 0.0290  0.3390  0.2515  525 PHE A CD1 
4103 C CD2 . PHE A 525 ? 1.3199 0.6332 0.9134 0.0321  0.3570  0.2730  525 PHE A CD2 
4104 C CE1 . PHE A 525 ? 1.3115 0.6239 0.8971 0.0313  0.3306  0.2476  525 PHE A CE1 
4105 C CE2 . PHE A 525 ? 1.2660 0.5814 0.9039 0.0346  0.3476  0.2666  525 PHE A CE2 
4106 C CZ  . PHE A 525 ? 1.2993 0.6121 0.9314 0.0345  0.3363  0.2555  525 PHE A CZ  
4107 N N   . LEU A 526 ? 1.4952 0.8123 0.8801 0.0190  0.3627  0.2269  526 LEU A N   
4108 C CA  . LEU A 526 ? 1.4972 0.8148 0.8448 0.0156  0.3761  0.2103  526 LEU A CA  
4109 C C   . LEU A 526 ? 1.4402 0.7502 0.8141 0.0126  0.4029  0.2019  526 LEU A C   
4110 O O   . LEU A 526 ? 1.5458 0.8562 0.8951 0.0105  0.4174  0.1882  526 LEU A O   
4111 C CB  . LEU A 526 ? 1.4899 0.8139 0.8238 0.0126  0.3592  0.1813  526 LEU A CB  
4112 C CG  . LEU A 526 ? 1.6243 0.9588 0.9273 0.0137  0.3317  0.1835  526 LEU A CG  
4113 C CD1 . LEU A 526 ? 1.6386 0.9771 0.9475 0.0092  0.3161  0.1539  526 LEU A CD1 
4114 C CD2 . LEU A 526 ? 1.7690 1.1078 1.0099 0.0148  0.3343  0.1927  526 LEU A CD2 
4115 N N   . TRP A 527 ? 1.3923 0.6963 0.8167 0.0124  0.4098  0.2086  527 TRP A N   
4116 C CA  . TRP A 527 ? 1.3163 0.6240 0.7794 0.0098  0.4266  0.1947  527 TRP A CA  
4117 C C   . TRP A 527 ? 1.3426 0.6582 0.8550 0.0116  0.4284  0.2082  527 TRP A C   
4118 O O   . TRP A 527 ? 1.2569 0.5730 0.7990 0.0137  0.4150  0.2143  527 TRP A O   
4119 C CB  . TRP A 527 ? 1.2482 0.5520 0.7360 0.0067  0.4231  0.1707  527 TRP A CB  
4120 C CG  . TRP A 527 ? 1.2191 0.5289 0.7459 0.0045  0.4370  0.1553  527 TRP A CG  
4121 C CD1 . TRP A 527 ? 1.1793 0.4962 0.7592 0.0039  0.4338  0.1479  527 TRP A CD1 
4122 C CD2 . TRP A 527 ? 1.2312 0.5420 0.7464 0.0029  0.4559  0.1449  527 TRP A CD2 
4123 N NE1 . TRP A 527 ? 1.1648 0.4864 0.7659 0.0017  0.4484  0.1351  527 TRP A NE1 
4124 C CE2 . TRP A 527 ? 1.1958 0.5132 0.7605 0.0013  0.4626  0.1336  527 TRP A CE2 
4125 C CE3 . TRP A 527 ? 1.2706 0.5790 0.7385 0.0030  0.4678  0.1426  527 TRP A CE3 
4126 C CZ2 . TRP A 527 ? 1.1974 0.5178 0.7691 0.0000  0.4809  0.1227  527 TRP A CZ2 
4127 C CZ3 . TRP A 527 ? 1.3050 0.6173 0.7810 0.0022  0.4868  0.1298  527 TRP A CZ3 
4128 C CH2 . TRP A 527 ? 1.2344 0.5520 0.7634 0.0008  0.4934  0.1211  527 TRP A CH2 
4129 N N   . PRO A 528 ? 1.3330 0.6544 0.8562 0.0106  0.4452  0.2126  528 PRO A N   
4130 C CA  . PRO A 528 ? 1.2779 0.6048 0.8492 0.0110  0.4479  0.2244  528 PRO A CA  
4131 C C   . PRO A 528 ? 1.2612 0.5907 0.8860 0.0095  0.4425  0.2075  528 PRO A C   
4132 O O   . PRO A 528 ? 1.2933 0.6244 0.9514 0.0112  0.4345  0.2157  528 PRO A O   
4133 C CB  . PRO A 528 ? 1.2987 0.6306 0.8698 0.0086  0.4692  0.2271  528 PRO A CB  
4134 C CG  . PRO A 528 ? 1.3014 0.6319 0.8420 0.0069  0.4782  0.2078  528 PRO A CG  
4135 C CD  . PRO A 528 ? 1.3133 0.6367 0.8083 0.0087  0.4635  0.2061  528 PRO A CD  
4136 N N   . GLY A 529 ? 1.2506 0.5811 0.8841 0.0065  0.4466  0.1841  529 GLY A N   
4137 C CA  . GLY A 529 ? 1.2031 0.5386 0.8809 0.0050  0.4399  0.1677  529 GLY A CA  
4138 C C   . GLY A 529 ? 1.1445 0.4874 0.8689 0.0025  0.4499  0.1662  529 GLY A C   
4139 O O   . GLY A 529 ? 1.1638 0.5081 0.8898 0.0008  0.4654  0.1725  529 GLY A O   
4140 N N   . PHE A 530 ? 1.1206 0.4687 0.8833 0.0017  0.4412  0.1571  530 PHE A N   
4141 C CA  . PHE A 530 ? 1.1010 0.4559 0.9100 -0.0018 0.4488  0.1517  530 PHE A CA  
4142 C C   . PHE A 530 ? 1.1435 0.5025 0.9593 -0.0060 0.4643  0.1412  530 PHE A C   
4143 O O   . PHE A 530 ? 1.0801 0.4414 0.8889 -0.0071 0.4634  0.1251  530 PHE A O   
4144 C CB  . PHE A 530 ? 1.1266 0.4782 0.9502 -0.0007 0.4525  0.1728  530 PHE A CB  
4145 C CG  . PHE A 530 ? 1.1412 0.4889 0.9663 0.0040  0.4378  0.1837  530 PHE A CG  
4146 C CD1 . PHE A 530 ? 1.1107 0.4620 0.9713 0.0038  0.4294  0.1724  530 PHE A CD1 
4147 C CD2 . PHE A 530 ? 1.1601 0.5011 0.9506 0.0087  0.4325  0.2054  530 PHE A CD2 
4148 C CE1 . PHE A 530 ? 1.1075 0.4551 0.9728 0.0087  0.4173  0.1820  530 PHE A CE1 
4149 C CE2 . PHE A 530 ? 1.1637 0.5014 0.9591 0.0135  0.4188  0.2166  530 PHE A CE2 
4150 C CZ  . PHE A 530 ? 1.1366 0.4773 0.9712 0.0139  0.4117  0.2048  530 PHE A CZ  
4151 N N   . GLY A 531 ? 1.1178 0.4778 0.9497 -0.0083 0.4790  0.1511  531 GLY A N   
4152 C CA  . GLY A 531 ? 1.1174 0.4823 0.9606 -0.0122 0.4953  0.1424  531 GLY A CA  
4153 C C   . GLY A 531 ? 1.1637 0.5253 0.9665 -0.0103 0.5016  0.1386  531 GLY A C   
4154 O O   . GLY A 531 ? 1.1217 0.4876 0.9353 -0.0127 0.5116  0.1256  531 GLY A O   
4155 N N   . GLU A 532 ? 1.1514 0.5052 0.9087 -0.0062 0.4961  0.1496  532 GLU A N   
4156 C CA  . GLU A 532 ? 1.1667 0.5161 0.8827 -0.0048 0.5024  0.1443  532 GLU A CA  
4157 C C   . GLU A 532 ? 1.1379 0.4851 0.8502 -0.0047 0.4925  0.1249  532 GLU A C   
4158 O O   . GLU A 532 ? 1.1617 0.5057 0.8536 -0.0046 0.5006  0.1151  532 GLU A O   
4159 C CB  . GLU A 532 ? 1.2046 0.5472 0.8705 -0.0013 0.4988  0.1614  532 GLU A CB  
4160 C CG  . GLU A 532 ? 1.2397 0.5848 0.9036 -0.0011 0.5086  0.1840  532 GLU A CG  
4161 C CD  . GLU A 532 ? 1.2551 0.6063 0.9289 -0.0037 0.5312  0.1827  532 GLU A CD  
4162 O OE1 . GLU A 532 ? 1.2775 0.6318 0.9698 -0.0057 0.5391  0.1638  532 GLU A OE1 
4163 O OE2 . GLU A 532 ? 1.2905 0.6442 0.9548 -0.0038 0.5413  0.2016  532 GLU A OE2 
4164 N N   . ASN A 533 ? 1.1087 0.4581 0.8411 -0.0048 0.4758  0.1192  533 ASN A N   
4165 C CA  . ASN A 533 ? 1.0815 0.4309 0.8146 -0.0052 0.4662  0.1020  533 ASN A CA  
4166 C C   . ASN A 533 ? 1.0661 0.4214 0.8232 -0.0080 0.4773  0.0877  533 ASN A C   
4167 O O   . ASN A 533 ? 1.1324 0.4864 0.8861 -0.0080 0.4721  0.0752  533 ASN A O   
4168 C CB  . ASN A 533 ? 1.0539 0.4093 0.8100 -0.0051 0.4483  0.0985  533 ASN A CB  
4169 C CG  . ASN A 533 ? 1.0767 0.4260 0.8109 -0.0018 0.4363  0.1120  533 ASN A CG  
4170 O OD1 . ASN A 533 ? 1.0934 0.4329 0.7875 0.0000  0.4365  0.1202  533 ASN A OD1 
4171 N ND2 . ASN A 533 ? 1.0529 0.4076 0.8133 -0.0011 0.4262  0.1142  533 ASN A ND2 
4172 N N   . SER A 534 ? 1.0848 0.4466 0.8684 -0.0104 0.4921  0.0903  534 SER A N   
4173 C CA  . SER A 534 ? 1.0678 0.4354 0.8744 -0.0129 0.5047  0.0787  534 SER A CA  
4174 C C   . SER A 534 ? 1.0813 0.4408 0.8554 -0.0105 0.5163  0.0751  534 SER A C   
4175 O O   . SER A 534 ? 1.0884 0.4505 0.8776 -0.0113 0.5229  0.0636  534 SER A O   
4176 C CB  . SER A 534 ? 1.0700 0.4460 0.9114 -0.0165 0.5197  0.0840  534 SER A CB  
4177 O OG  . SER A 534 ? 1.1669 0.5383 0.9852 -0.0147 0.5313  0.0995  534 SER A OG  
4178 N N   . ARG A 535 ? 1.1123 0.4630 0.8425 -0.0077 0.5191  0.0844  535 ARG A N   
4179 C CA  . ARG A 535 ? 1.1753 0.5190 0.8706 -0.0056 0.5294  0.0777  535 ARG A CA  
4180 C C   . ARG A 535 ? 1.1460 0.4810 0.8289 -0.0052 0.5170  0.0662  535 ARG A C   
4181 O O   . ARG A 535 ? 1.1151 0.4529 0.7973 -0.0024 0.5202  0.0516  535 ARG A O   
4182 C CB  . ARG A 535 ? 1.1744 0.5131 0.8222 -0.0033 0.5332  0.0896  535 ARG A CB  
4183 C CG  . ARG A 535 ? 1.1964 0.5427 0.8537 -0.0039 0.5451  0.1047  535 ARG A CG  
4184 C CD  . ARG A 535 ? 1.3077 0.6500 0.9155 -0.0017 0.5438  0.1199  535 ARG A CD  
4185 N NE  . ARG A 535 ? 1.2592 0.6082 0.8780 -0.0025 0.5526  0.1386  535 ARG A NE  
4186 C CZ  . ARG A 535 ? 1.2913 0.6467 0.9005 -0.0025 0.5717  0.1436  535 ARG A CZ  
4187 N NH1 . ARG A 535 ? 1.3399 0.6970 0.9290 -0.0012 0.5844  0.1296  535 ARG A NH1 
4188 N NH2 . ARG A 535 ? 1.3663 0.7271 0.9877 -0.0039 0.5787  0.1630  535 ARG A NH2 
4189 N N   . VAL A 536 ? 1.1222 0.4540 0.8028 -0.0054 0.4961  0.0692  536 VAL A N   
4190 C CA  . VAL A 536 ? 1.0895 0.4194 0.7668 -0.0040 0.4783  0.0569  536 VAL A CA  
4191 C C   . VAL A 536 ? 1.0485 0.3878 0.7676 -0.0047 0.4753  0.0454  536 VAL A C   
4192 O O   . VAL A 536 ? 1.0752 0.4173 0.7967 -0.0018 0.4692  0.0326  536 VAL A O   
4193 C CB  . VAL A 536 ? 1.1057 0.4304 0.7717 -0.0045 0.4595  0.0647  536 VAL A CB  
4194 C CG1 . VAL A 536 ? 1.1006 0.4274 0.7707 -0.0035 0.4408  0.0521  536 VAL A CG1 
4195 C CG2 . VAL A 536 ? 1.1088 0.4266 0.7313 -0.0031 0.4591  0.0757  536 VAL A CG2 
4196 N N   . LEU A 537 ? 1.0598 0.4076 0.8142 -0.0078 0.4773  0.0489  537 LEU A N   
4197 C CA  . LEU A 537 ? 1.0054 0.3649 0.7982 -0.0090 0.4736  0.0383  537 LEU A CA  
4198 C C   . LEU A 537 ? 1.0116 0.3762 0.8161 -0.0068 0.4876  0.0305  537 LEU A C   
4199 O O   . LEU A 537 ? 0.9939 0.3673 0.8183 -0.0045 0.4797  0.0200  537 LEU A O   
4200 C CB  . LEU A 537 ? 1.0498 0.4249 0.8790 -0.0126 0.4715  0.0399  537 LEU A CB  
4201 C CG  . LEU A 537 ? 1.0367 0.4168 0.8668 -0.0132 0.4558  0.0439  537 LEU A CG  
4202 C CD1 . LEU A 537 ? 1.0550 0.4483 0.9264 -0.0179 0.4553  0.0403  537 LEU A CD1 
4203 C CD2 . LEU A 537 ? 0.9637 0.3441 0.7794 -0.0111 0.4368  0.0386  537 LEU A CD2 
4204 N N   . GLU A 538 ? 1.0374 0.4000 0.8315 -0.0066 0.5079  0.0356  538 GLU A N   
4205 C CA  . GLU A 538 ? 1.0448 0.4157 0.8518 -0.0031 0.5224  0.0267  538 GLU A CA  
4206 C C   . GLU A 538 ? 1.0445 0.4121 0.8348 0.0032  0.5128  0.0141  538 GLU A C   
4207 O O   . GLU A 538 ? 1.0316 0.4083 0.8493 0.0068  0.5113  0.0042  538 GLU A O   
4208 C CB  . GLU A 538 ? 1.0787 0.4470 0.8681 -0.0036 0.5472  0.0347  538 GLU A CB  
4209 C CG  . GLU A 538 ? 1.0906 0.4676 0.8915 0.0009  0.5652  0.0243  538 GLU A CG  
4210 C CD  . GLU A 538 ? 1.1586 0.5350 0.9416 0.0000  0.5925  0.0327  538 GLU A CD  
4211 O OE1 . GLU A 538 ? 1.1506 0.5173 0.8937 -0.0009 0.5908  0.0434  538 GLU A OE1 
4212 O OE2 . GLU A 538 ? 1.2439 0.6322 1.0548 0.0009  0.6122  0.0285  538 GLU A OE2 
4213 N N   . TRP A 539 ? 1.0602 0.4150 0.8080 0.0046  0.5054  0.0147  539 TRP A N   
4214 C CA  . TRP A 539 ? 1.0624 0.4114 0.7957 0.0094  0.4957  0.0021  539 TRP A CA  
4215 C C   . TRP A 539 ? 1.0650 0.4189 0.8254 0.0100  0.4767  -0.0022 539 TRP A C   
4216 O O   . TRP A 539 ? 1.0256 0.3818 0.8017 0.0148  0.4746  -0.0118 539 TRP A O   
4217 C CB  . TRP A 539 ? 1.0839 0.4199 0.7698 0.0088  0.4878  0.0037  539 TRP A CB  
4218 C CG  . TRP A 539 ? 1.0915 0.4196 0.7626 0.0125  0.4791  -0.0106 539 TRP A CG  
4219 C CD1 . TRP A 539 ? 1.1166 0.4405 0.7763 0.0168  0.4915  -0.0239 539 TRP A CD1 
4220 C CD2 . TRP A 539 ? 1.0765 0.3992 0.7449 0.0116  0.4574  -0.0137 539 TRP A CD2 
4221 N NE1 . TRP A 539 ? 1.1323 0.4469 0.7839 0.0186  0.4780  -0.0356 539 TRP A NE1 
4222 C CE2 . TRP A 539 ? 1.1048 0.4188 0.7619 0.0151  0.4571  -0.0286 539 TRP A CE2 
4223 C CE3 . TRP A 539 ? 1.0521 0.3765 0.7281 0.0082  0.4396  -0.0058 539 TRP A CE3 
4224 C CZ2 . TRP A 539 ? 1.1031 0.4094 0.7580 0.0143  0.4391  -0.0342 539 TRP A CZ2 
4225 C CZ3 . TRP A 539 ? 1.0582 0.3771 0.7304 0.0079  0.4228  -0.0110 539 TRP A CZ3 
4226 C CH2 . TRP A 539 ? 1.0994 0.4091 0.7621 0.0105  0.4224  -0.0243 539 TRP A CH2 
4227 N N   . MET A 540 ? 1.0227 0.3784 0.7890 0.0058  0.4632  0.0054  540 MET A N   
4228 C CA  . MET A 540 ? 0.9839 0.3461 0.7723 0.0059  0.4461  0.0024  540 MET A CA  
4229 C C   . MET A 540 ? 0.9709 0.3480 0.7992 0.0080  0.4501  -0.0024 540 MET A C   
4230 O O   . MET A 540 ? 0.9937 0.3749 0.8358 0.0119  0.4404  -0.0074 540 MET A O   
4231 C CB  . MET A 540 ? 0.9686 0.3324 0.7589 0.0009  0.4352  0.0100  540 MET A CB  
4232 C CG  . MET A 540 ? 0.9783 0.3304 0.7354 -0.0004 0.4278  0.0158  540 MET A CG  
4233 S SD  . MET A 540 ? 1.1205 0.4859 0.8903 -0.0043 0.4154  0.0227  540 MET A SD  
4234 C CE  . MET A 540 ? 1.0877 0.4397 0.8211 -0.0040 0.4068  0.0297  540 MET A CE  
4235 N N   . PHE A 541 ? 0.9726 0.3584 0.8220 0.0054  0.4640  0.0002  541 PHE A N   
4236 C CA  . PHE A 541 ? 0.9613 0.3643 0.8529 0.0068  0.4673  -0.0045 541 PHE A CA  
4237 C C   . PHE A 541 ? 1.0151 0.4190 0.9132 0.0147  0.4733  -0.0123 541 PHE A C   
4238 O O   . PHE A 541 ? 1.0140 0.4294 0.9409 0.0188  0.4648  -0.0161 541 PHE A O   
4239 C CB  . PHE A 541 ? 0.9827 0.3935 0.8956 0.0017  0.4843  -0.0004 541 PHE A CB  
4240 C CG  . PHE A 541 ? 1.0313 0.4631 0.9931 0.0004  0.4835  -0.0048 541 PHE A CG  
4241 C CD1 . PHE A 541 ? 0.9545 0.3979 0.9418 0.0062  0.4916  -0.0107 541 PHE A CD1 
4242 C CD2 . PHE A 541 ? 0.9367 0.3775 0.9209 -0.0067 0.4749  -0.0041 541 PHE A CD2 
4243 C CE1 . PHE A 541 ? 0.9591 0.4248 0.9944 0.0051  0.4892  -0.0143 541 PHE A CE1 
4244 C CE2 . PHE A 541 ? 0.9325 0.3947 0.9620 -0.0088 0.4723  -0.0096 541 PHE A CE2 
4245 C CZ  . PHE A 541 ? 1.0442 0.5200 1.0998 -0.0029 0.4787  -0.0139 541 PHE A CZ  
4246 N N   . GLY A 542 ? 0.9955 0.3875 0.8670 0.0175  0.4877  -0.0148 542 GLY A N   
4247 C CA  . GLY A 542 ? 1.0082 0.3988 0.8864 0.0256  0.4954  -0.0246 542 GLY A CA  
4248 C C   . GLY A 542 ? 1.0915 0.4730 0.9625 0.0299  0.4776  -0.0291 542 GLY A C   
4249 O O   . GLY A 542 ? 1.0635 0.4492 0.9602 0.0368  0.4761  -0.0345 542 GLY A O   
4250 N N   . ARG A 543 ? 1.0563 0.4256 0.8955 0.0260  0.4641  -0.0257 543 ARG A N   
4251 C CA  . ARG A 543 ? 1.0204 0.3812 0.8551 0.0285  0.4473  -0.0281 543 ARG A CA  
4252 C C   . ARG A 543 ? 0.9950 0.3702 0.8633 0.0299  0.4329  -0.0233 543 ARG A C   
4253 O O   . ARG A 543 ? 1.0220 0.3988 0.9027 0.0346  0.4229  -0.0243 543 ARG A O   
4254 C CB  . ARG A 543 ? 0.9977 0.3464 0.7965 0.0229  0.4359  -0.0243 543 ARG A CB  
4255 C CG  . ARG A 543 ? 1.0603 0.3948 0.8214 0.0223  0.4449  -0.0300 543 ARG A CG  
4256 C CD  . ARG A 543 ? 1.0542 0.3784 0.8134 0.0278  0.4481  -0.0431 543 ARG A CD  
4257 N NE  . ARG A 543 ? 1.0332 0.3584 0.7996 0.0268  0.4273  -0.0421 543 ARG A NE  
4258 C CZ  . ARG A 543 ? 1.1027 0.4301 0.8894 0.0313  0.4230  -0.0479 543 ARG A CZ  
4259 N NH1 . ARG A 543 ? 1.0746 0.4051 0.8785 0.0374  0.4367  -0.0559 543 ARG A NH1 
4260 N NH2 . ARG A 543 ? 1.1571 0.4834 0.9493 0.0299  0.4053  -0.0449 543 ARG A NH2 
4261 N N   . ILE A 544 ? 1.0538 0.4434 0.9377 0.0254  0.4299  -0.0175 544 ILE A N   
4262 C CA  . ILE A 544 ? 1.0796 0.4852 0.9920 0.0264  0.4155  -0.0141 544 ILE A CA  
4263 C C   . ILE A 544 ? 0.9366 0.3544 0.8860 0.0339  0.4205  -0.0174 544 ILE A C   
4264 O O   . ILE A 544 ? 0.9299 0.3563 0.8990 0.0384  0.4072  -0.0143 544 ILE A O   
4265 C CB  . ILE A 544 ? 0.9867 0.4053 0.9068 0.0190  0.4113  -0.0105 544 ILE A CB  
4266 C CG1 . ILE A 544 ? 0.9281 0.3367 0.8180 0.0135  0.4019  -0.0064 544 ILE A CG1 
4267 C CG2 . ILE A 544 ? 0.9254 0.3656 0.8786 0.0201  0.3991  -0.0098 544 ILE A CG2 
4268 C CD1 . ILE A 544 ? 0.9061 0.3246 0.8040 0.0066  0.3988  -0.0048 544 ILE A CD1 
4269 N N   . GLU A 545 ? 0.9485 0.3684 0.9088 0.0359  0.4398  -0.0226 545 GLU A N   
4270 C CA  . GLU A 545 ? 0.9893 0.4217 0.9885 0.0440  0.4467  -0.0264 545 GLU A CA  
4271 C C   . GLU A 545 ? 0.9836 0.4003 0.9786 0.0530  0.4508  -0.0324 545 GLU A C   
4272 O O   . GLU A 545 ? 0.9730 0.3984 1.0032 0.0617  0.4549  -0.0352 545 GLU A O   
4273 C CB  . GLU A 545 ? 1.0188 0.4620 1.0362 0.0421  0.4681  -0.0297 545 GLU A CB  
4274 C CG  . GLU A 545 ? 0.9430 0.4029 0.9770 0.0332  0.4649  -0.0251 545 GLU A CG  
4275 C CD  . GLU A 545 ? 1.0516 0.5252 1.1154 0.0316  0.4861  -0.0273 545 GLU A CD  
4276 O OE1 . GLU A 545 ? 1.1211 0.5845 1.1687 0.0331  0.5075  -0.0298 545 GLU A OE1 
4277 O OE2 . GLU A 545 ? 1.0919 0.5877 1.1954 0.0285  0.4815  -0.0268 545 GLU A OE2 
4278 N N   . GLY A 546 ? 1.0164 0.4112 0.9726 0.0512  0.4491  -0.0349 546 GLY A N   
4279 C CA  . GLY A 546 ? 1.0455 0.4322 0.9977 0.0566  0.4485  -0.0413 546 GLY A CA  
4280 C C   . GLY A 546 ? 1.1197 0.5030 1.0630 0.0586  0.4701  -0.0524 546 GLY A C   
4281 O O   . GLY A 546 ? 1.0331 0.4231 1.0054 0.0663  0.4796  -0.0585 546 GLY A O   
4282 N N   . GLU A 547 ? 1.1532 0.5261 1.0563 0.0521  0.4785  -0.0547 547 GLU A N   
4283 C CA  . GLU A 547 ? 1.1712 0.5389 1.0555 0.0531  0.4991  -0.0648 547 GLU A CA  
4284 C C   . GLU A 547 ? 1.2083 0.5578 1.0511 0.0505  0.4927  -0.0726 547 GLU A C   
4285 O O   . GLU A 547 ? 1.1375 0.4771 0.9538 0.0449  0.4790  -0.0676 547 GLU A O   
4286 C CB  . GLU A 547 ? 1.1442 0.5143 1.0146 0.0485  0.5173  -0.0606 547 GLU A CB  
4287 C CG  . GLU A 547 ? 1.1906 0.5798 1.1064 0.0508  0.5293  -0.0570 547 GLU A CG  
4288 C CD  . GLU A 547 ? 1.4764 0.8702 1.3816 0.0447  0.5478  -0.0511 547 GLU A CD  
4289 O OE1 . GLU A 547 ? 1.6029 0.9841 1.4628 0.0408  0.5543  -0.0502 547 GLU A OE1 
4290 O OE2 . GLU A 547 ? 1.5076 0.9205 1.4512 0.0429  0.5535  -0.0458 547 GLU A OE2 
4291 N N   . ASP A 548 ? 1.4153 0.7610 1.2549 0.0546  0.5025  -0.0860 548 ASP A N   
4292 C CA  . ASP A 548 ? 1.4486 0.7772 1.2526 0.0523  0.4965  -0.0974 548 ASP A CA  
4293 C C   . ASP A 548 ? 1.4495 0.7688 1.2025 0.0467  0.5068  -0.0991 548 ASP A C   
4294 O O   . ASP A 548 ? 1.4549 0.7706 1.1830 0.0474  0.5205  -0.1110 548 ASP A O   
4295 C CB  . ASP A 548 ? 1.4378 0.7657 1.2580 0.0588  0.5034  -0.1130 548 ASP A CB  
4296 C CG  . ASP A 548 ? 1.5346 0.8452 1.3327 0.0567  0.4910  -0.1254 548 ASP A CG  
4297 O OD1 . ASP A 548 ? 1.5781 0.8792 1.3557 0.0507  0.4748  -0.1198 548 ASP A OD1 
4298 O OD2 . ASP A 548 ? 1.5832 0.8899 1.3865 0.0610  0.4976  -0.1416 548 ASP A OD2 
4299 N N   . SER A 549 ? 1.2427 0.5589 0.9796 0.0415  0.4996  -0.0865 549 SER A N   
4300 C CA  . SER A 549 ? 1.2117 0.5193 0.9021 0.0371  0.5084  -0.0840 549 SER A CA  
4301 C C   . SER A 549 ? 1.1671 0.4583 0.8233 0.0323  0.4909  -0.0839 549 SER A C   
4302 O O   . SER A 549 ? 1.1778 0.4699 0.7999 0.0272  0.4897  -0.0759 549 SER A O   
4303 C CB  . SER A 549 ? 1.1904 0.5082 0.8923 0.0354  0.5187  -0.0688 549 SER A CB  
4304 O OG  . SER A 549 ? 1.2156 0.5396 0.9442 0.0327  0.4999  -0.0573 549 SER A OG  
4305 N N   . ALA A 550 ? 1.1754 0.4621 0.8462 0.0316  0.4716  -0.0875 550 ALA A N   
4306 C CA  . ALA A 550 ? 1.2329 0.5072 0.8815 0.0262  0.4532  -0.0855 550 ALA A CA  
4307 C C   . ALA A 550 ? 1.1936 0.4540 0.8202 0.0249  0.4477  -0.1035 550 ALA A C   
4308 O O   . ALA A 550 ? 1.1926 0.4554 0.8387 0.0283  0.4500  -0.1151 550 ALA A O   
4309 C CB  . ALA A 550 ? 1.1128 0.3948 0.7960 0.0246  0.4345  -0.0734 550 ALA A CB  
4310 N N   . LYS A 551 ? 1.2531 0.5072 0.8446 0.0186  0.4359  -0.1037 551 LYS A N   
4311 C CA  . LYS A 551 ? 1.2250 0.4645 0.7943 0.0154  0.4270  -0.1217 551 LYS A CA  
4312 C C   . LYS A 551 ? 1.2451 0.4815 0.8272 0.0093  0.4037  -0.1146 551 LYS A C   
4313 O O   . LYS A 551 ? 1.1790 0.4261 0.7602 0.0055  0.3933  -0.0969 551 LYS A O   
4314 C CB  . LYS A 551 ? 1.2628 0.5037 0.7799 0.0120  0.4300  -0.1274 551 LYS A CB  
4315 C CG  . LYS A 551 ? 1.4093 0.6372 0.9002 0.0076  0.4194  -0.1487 551 LYS A CG  
4316 C CD  . LYS A 551 ? 1.5516 0.7846 0.9872 0.0044  0.4201  -0.1519 551 LYS A CD  
4317 C CE  . LYS A 551 ? 1.4165 0.6623 0.8399 -0.0002 0.4053  -0.1278 551 LYS A CE  
4318 N NZ  . LYS A 551 ? 1.6535 0.9053 1.0227 -0.0025 0.4043  -0.1275 551 LYS A NZ  
4319 N N   . LEU A 552 ? 1.2123 0.4340 0.8088 0.0084  0.3967  -0.1284 552 LEU A N   
4320 C CA  . LEU A 552 ? 1.1940 0.4126 0.8061 0.0021  0.3765  -0.1216 552 LEU A CA  
4321 C C   . LEU A 552 ? 1.2223 0.4413 0.8010 -0.0064 0.3618  -0.1260 552 LEU A C   
4322 O O   . LEU A 552 ? 1.3262 0.5388 0.8733 -0.0079 0.3642  -0.1440 552 LEU A O   
4323 C CB  . LEU A 552 ? 1.1930 0.4105 0.8416 0.0026  0.3694  -0.1289 552 LEU A CB  
4324 C CG  . LEU A 552 ? 1.2136 0.4299 0.8832 -0.0039 0.3505  -0.1199 552 LEU A CG  
4325 C CD1 . LEU A 552 ? 1.1989 0.4314 0.8824 -0.0039 0.3458  -0.0955 552 LEU A CD1 
4326 C CD2 . LEU A 552 ? 1.2184 0.4347 0.9270 -0.0022 0.3451  -0.1242 552 LEU A CD2 
4327 N N   . THR A 553 ? 1.2299 0.4579 0.8160 -0.0118 0.3463  -0.1100 553 THR A N   
4328 C CA  . THR A 553 ? 1.2077 0.4401 0.7680 -0.0194 0.3303  -0.1109 553 THR A CA  
4329 C C   . THR A 553 ? 1.1770 0.4115 0.7641 -0.0258 0.3134  -0.1015 553 THR A C   
4330 O O   . THR A 553 ? 1.1717 0.4060 0.7920 -0.0237 0.3154  -0.0913 553 THR A O   
4331 C CB  . THR A 553 ? 1.2082 0.4558 0.7412 -0.0181 0.3324  -0.0967 553 THR A CB  
4332 O OG1 . THR A 553 ? 1.3688 0.6170 0.8613 -0.0218 0.3254  -0.1068 553 THR A OG1 
4333 C CG2 . THR A 553 ? 1.1637 0.4242 0.7144 -0.0204 0.3213  -0.0752 553 THR A CG2 
4334 N N   . PRO A 554 ? 1.1888 0.4270 0.7632 -0.0335 0.2967  -0.1043 554 PRO A N   
4335 C CA  . PRO A 554 ? 1.1678 0.4092 0.7710 -0.0402 0.2823  -0.0957 554 PRO A CA  
4336 C C   . PRO A 554 ? 1.2032 0.4602 0.8239 -0.0380 0.2822  -0.0719 554 PRO A C   
4337 O O   . PRO A 554 ? 1.2515 0.5109 0.9004 -0.0418 0.2757  -0.0634 554 PRO A O   
4338 C CB  . PRO A 554 ? 1.1962 0.4421 0.7791 -0.0484 0.2647  -0.1046 554 PRO A CB  
4339 C CG  . PRO A 554 ? 1.2342 0.4722 0.7796 -0.0468 0.2700  -0.1246 554 PRO A CG  
4340 C CD  . PRO A 554 ? 1.2269 0.4664 0.7613 -0.0370 0.2899  -0.1174 554 PRO A CD  
4341 N N   . ILE A 555 ? 1.1191 0.3862 0.7249 -0.0324 0.2900  -0.0613 555 ILE A N   
4342 C CA  . ILE A 555 ? 1.1301 0.4111 0.7525 -0.0304 0.2905  -0.0417 555 ILE A CA  
4343 C C   . ILE A 555 ? 1.0655 0.3466 0.7029 -0.0237 0.3053  -0.0358 555 ILE A C   
4344 O O   . ILE A 555 ? 1.0381 0.3298 0.6923 -0.0224 0.3060  -0.0223 555 ILE A O   
4345 C CB  . ILE A 555 ? 1.0875 0.3808 0.6891 -0.0298 0.2865  -0.0317 555 ILE A CB  
4346 C CG1 . ILE A 555 ? 1.1749 0.4654 0.7483 -0.0245 0.2993  -0.0343 555 ILE A CG1 
4347 C CG2 . ILE A 555 ? 1.1052 0.4028 0.6963 -0.0363 0.2687  -0.0355 555 ILE A CG2 
4348 C CD1 . ILE A 555 ? 1.1072 0.4086 0.6656 -0.0222 0.2991  -0.0192 555 ILE A CD1 
4349 N N   . GLY A 556 ? 1.0999 0.3709 0.7332 -0.0194 0.3169  -0.0465 556 GLY A N   
4350 C CA  . GLY A 556 ? 1.1101 0.3833 0.7603 -0.0129 0.3300  -0.0417 556 GLY A CA  
4351 C C   . GLY A 556 ? 1.1439 0.4114 0.7778 -0.0078 0.3448  -0.0525 556 GLY A C   
4352 O O   . GLY A 556 ? 1.1429 0.4031 0.7504 -0.0093 0.3454  -0.0650 556 GLY A O   
4353 N N   . TYR A 557 ? 1.1120 0.3845 0.7625 -0.0021 0.3571  -0.0480 557 TYR A N   
4354 C CA  . TYR A 557 ? 1.1206 0.3909 0.7608 0.0030  0.3741  -0.0562 557 TYR A CA  
4355 C C   . TYR A 557 ? 1.1101 0.3889 0.7254 0.0022  0.3801  -0.0483 557 TYR A C   
4356 O O   . TYR A 557 ? 1.1094 0.3985 0.7320 0.0007  0.3763  -0.0338 557 TYR A O   
4357 C CB  . TYR A 557 ? 1.0745 0.3493 0.7471 0.0093  0.3843  -0.0539 557 TYR A CB  
4358 C CG  . TYR A 557 ? 1.0688 0.3479 0.7705 0.0111  0.3765  -0.0581 557 TYR A CG  
4359 C CD1 . TYR A 557 ? 1.1484 0.4163 0.8468 0.0132  0.3811  -0.0744 557 TYR A CD1 
4360 C CD2 . TYR A 557 ? 1.0828 0.3777 0.8150 0.0112  0.3649  -0.0458 557 TYR A CD2 
4361 C CE1 . TYR A 557 ? 1.0933 0.3635 0.8220 0.0154  0.3740  -0.0770 557 TYR A CE1 
4362 C CE2 . TYR A 557 ? 1.0843 0.3806 0.8425 0.0137  0.3583  -0.0472 557 TYR A CE2 
4363 C CZ  . TYR A 557 ? 1.1173 0.4007 0.8758 0.0159  0.3628  -0.0621 557 TYR A CZ  
4364 O OH  . TYR A 557 ? 1.1448 0.4276 0.9324 0.0188  0.3565  -0.0625 557 TYR A OH  
4365 N N   . VAL A 558 ? 1.1308 0.4049 0.7166 0.0033  0.3900  -0.0579 558 VAL A N   
4366 C CA  . VAL A 558 ? 1.1436 0.4247 0.7042 0.0032  0.3985  -0.0486 558 VAL A CA  
4367 C C   . VAL A 558 ? 1.2232 0.5037 0.7790 0.0081  0.4211  -0.0562 558 VAL A C   
4368 O O   . VAL A 558 ? 1.1761 0.4491 0.7399 0.0116  0.4282  -0.0723 558 VAL A O   
4369 C CB  . VAL A 558 ? 1.1712 0.4505 0.6921 -0.0011 0.3872  -0.0493 558 VAL A CB  
4370 C CG1 . VAL A 558 ? 1.1505 0.4323 0.6821 -0.0058 0.3655  -0.0424 558 VAL A CG1 
4371 C CG2 . VAL A 558 ? 1.2190 0.4878 0.7138 -0.0011 0.3897  -0.0709 558 VAL A CG2 
4372 N N   . PRO A 559 ? 1.2151 0.5033 0.7607 0.0088  0.4340  -0.0446 559 PRO A N   
4373 C CA  . PRO A 559 ? 1.1881 0.4785 0.7340 0.0131  0.4581  -0.0501 559 PRO A CA  
4374 C C   . PRO A 559 ? 1.2325 0.5143 0.7430 0.0147  0.4660  -0.0689 559 PRO A C   
4375 O O   . PRO A 559 ? 1.2586 0.5362 0.7306 0.0113  0.4556  -0.0721 559 PRO A O   
4376 C CB  . PRO A 559 ? 1.1906 0.4896 0.7274 0.0115  0.4678  -0.0312 559 PRO A CB  
4377 C CG  . PRO A 559 ? 1.1614 0.4633 0.7099 0.0077  0.4491  -0.0162 559 PRO A CG  
4378 C CD  . PRO A 559 ? 1.2122 0.5073 0.7497 0.0056  0.4283  -0.0251 559 PRO A CD  
4379 N N   . LYS A 560 ? 1.2431 0.5233 0.7681 0.0201  0.4841  -0.0825 560 LYS A N   
4380 C CA  . LYS A 560 ? 1.3935 0.6661 0.8859 0.0224  0.4962  -0.1029 560 LYS A CA  
4381 C C   . LYS A 560 ? 1.5625 0.8412 1.0086 0.0208  0.5093  -0.0954 560 LYS A C   
4382 O O   . LYS A 560 ? 1.3617 0.6495 0.8076 0.0187  0.5119  -0.0735 560 LYS A O   
4383 C CB  . LYS A 560 ? 1.3687 0.6424 0.8938 0.0293  0.5143  -0.1165 560 LYS A CB  
4384 C CG  . LYS A 560 ? 1.3918 0.6618 0.9598 0.0311  0.4994  -0.1243 560 LYS A CG  
4385 C CD  . LYS A 560 ? 1.2720 0.5529 0.8751 0.0369  0.5116  -0.1338 560 LYS A CD  
4386 C CE  . LYS A 560 ? 1.3316 0.6111 0.9789 0.0396  0.4970  -0.1383 560 LYS A CE  
4387 N NZ  . LYS A 560 ? 1.2578 0.5473 0.9405 0.0467  0.5093  -0.1475 560 LYS A NZ  
4388 N N   . GLU A 561 ? 1.9459 1.2190 1.3521 0.0218  0.5181  -0.1143 561 GLU A N   
4389 C CA  . GLU A 561 ? 1.9832 1.2630 1.3427 0.0215  0.5350  -0.1085 561 GLU A CA  
4390 C C   . GLU A 561 ? 1.9594 1.2547 1.3517 0.0241  0.5557  -0.0945 561 GLU A C   
4391 O O   . GLU A 561 ? 1.9370 1.2375 1.3729 0.0279  0.5639  -0.1034 561 GLU A O   
4392 C CB  . GLU A 561 ? 2.0634 1.3422 1.3872 0.0218  0.5365  -0.1330 561 GLU A CB  
4393 C CG  . GLU A 561 ? 2.1852 1.4776 1.4660 0.0215  0.5512  -0.1263 561 GLU A CG  
4394 C CD  . GLU A 561 ? 2.2622 1.5579 1.5195 0.0232  0.5572  -0.1534 561 GLU A CD  
4395 O OE1 . GLU A 561 ? 2.2697 1.5573 1.5527 0.0249  0.5518  -0.1767 561 GLU A OE1 
4396 O OE2 . GLU A 561 ? 2.3413 1.6487 1.5559 0.0228  0.5672  -0.1509 561 GLU A OE2 
4397 N N   . ASP A 562 ? 1.5791 0.8825 0.9538 0.0216  0.5628  -0.0713 562 ASP A N   
4398 C CA  . ASP A 562 ? 1.5833 0.9012 0.9893 0.0225  0.5816  -0.0566 562 ASP A CA  
4399 C C   . ASP A 562 ? 1.5199 0.8397 0.9886 0.0237  0.5821  -0.0522 562 ASP A C   
4400 O O   . ASP A 562 ? 1.4139 0.7458 0.9196 0.0251  0.5975  -0.0480 562 ASP A O   
4401 C CB  . ASP A 562 ? 1.7443 1.0726 1.1459 0.0257  0.5996  -0.0705 562 ASP A CB  
4402 C CG  . ASP A 562 ? 1.8448 1.1778 1.1847 0.0241  0.6035  -0.0686 562 ASP A CG  
4403 O OD1 . ASP A 562 ? 1.7618 1.0994 1.0813 0.0212  0.6040  -0.0445 562 ASP A OD1 
4404 O OD2 . ASP A 562 ? 1.9283 1.2612 1.2411 0.0260  0.6053  -0.0911 562 ASP A OD2 
4405 N N   . ALA A 563 ? 1.5154 0.8248 0.9967 0.0232  0.5652  -0.0536 563 ALA A N   
4406 C CA  . ALA A 563 ? 1.3339 0.6487 0.8731 0.0238  0.5606  -0.0481 563 ALA A CA  
4407 C C   . ALA A 563 ? 1.2967 0.6192 0.8513 0.0190  0.5593  -0.0237 563 ALA A C   
4408 O O   . ALA A 563 ? 1.2901 0.6218 0.8904 0.0190  0.5660  -0.0184 563 ALA A O   
4409 C CB  . ALA A 563 ? 1.2772 0.5840 0.8323 0.0239  0.5346  -0.0567 563 ALA A CB  
4410 N N   . LEU A 564 ? 1.2605 0.5795 0.7800 0.0150  0.5503  -0.0093 564 LEU A N   
4411 C CA  . LEU A 564 ? 1.3347 0.6580 0.8687 0.0108  0.5495  0.0139  564 LEU A CA  
4412 C C   . LEU A 564 ? 1.3427 0.6726 0.8682 0.0100  0.5741  0.0264  564 LEU A C   
4413 O O   . LEU A 564 ? 1.3200 0.6504 0.8030 0.0110  0.5784  0.0269  564 LEU A O   
4414 C CB  . LEU A 564 ? 1.3056 0.6228 0.8121 0.0080  0.5271  0.0255  564 LEU A CB  
4415 C CG  . LEU A 564 ? 1.2974 0.6133 0.8326 0.0064  0.5026  0.0253  564 LEU A CG  
4416 C CD1 . LEU A 564 ? 1.3238 0.6365 0.8379 0.0040  0.4858  0.0411  564 LEU A CD1 
4417 C CD2 . LEU A 564 ? 1.2915 0.6146 0.8797 0.0053  0.5073  0.0289  564 LEU A CD2 
4418 N N   . ASN A 565 ? 1.3194 0.6585 0.8919 0.0081  0.5821  0.0355  565 ASN A N   
4419 C CA  . ASN A 565 ? 1.2742 0.6232 0.8523 0.0068  0.5961  0.0494  565 ASN A CA  
4420 C C   . ASN A 565 ? 1.2943 0.6397 0.8405 0.0048  0.5864  0.0700  565 ASN A C   
4421 O O   . ASN A 565 ? 1.2708 0.6146 0.8390 0.0022  0.5750  0.0828  565 ASN A O   
4422 C CB  . ASN A 565 ? 1.2435 0.6026 0.8827 0.0042  0.6039  0.0536  565 ASN A CB  
4423 C CG  . ASN A 565 ? 1.3517 0.7219 1.0027 0.0028  0.6216  0.0653  565 ASN A CG  
4424 O OD1 . ASN A 565 ? 1.3557 0.7255 0.9715 0.0027  0.6238  0.0785  565 ASN A OD1 
4425 N ND2 . ASN A 565 ? 1.3717 0.7532 1.0736 0.0014  0.6343  0.0614  565 ASN A ND2 
4426 N N   . LEU A 566 ? 1.3394 0.6849 0.8347 0.0065  0.5897  0.0726  566 LEU A N   
4427 C CA  . LEU A 566 ? 1.4164 0.7607 0.8778 0.0056  0.5806  0.0939  566 LEU A CA  
4428 C C   . LEU A 566 ? 1.5108 0.8665 0.9685 0.0053  0.5966  0.1106  566 LEU A C   
4429 O O   . LEU A 566 ? 1.5949 0.9519 1.0199 0.0053  0.5912  0.1298  566 LEU A O   
4430 C CB  . LEU A 566 ? 1.3958 0.7328 0.7961 0.0072  0.5694  0.0869  566 LEU A CB  
4431 C CG  . LEU A 566 ? 1.4443 0.7687 0.8423 0.0066  0.5513  0.0752  566 LEU A CG  
4432 C CD1 . LEU A 566 ? 1.5118 0.8299 0.8483 0.0075  0.5421  0.0654  566 LEU A CD1 
4433 C CD2 . LEU A 566 ? 1.3361 0.6570 0.7601 0.0045  0.5356  0.0935  566 LEU A CD2 
4434 N N   . LYS A 567 ? 1.4687 0.8337 0.9601 0.0049  0.6162  0.1051  567 LYS A N   
4435 C CA  . LYS A 567 ? 1.5273 0.9040 1.0165 0.0040  0.6337  0.1208  567 LYS A CA  
4436 C C   . LYS A 567 ? 1.4798 0.8569 0.9915 0.0011  0.6278  0.1466  567 LYS A C   
4437 O O   . LYS A 567 ? 1.3852 0.7581 0.9406 -0.0008 0.6182  0.1472  567 LYS A O   
4438 C CB  . LYS A 567 ? 1.6178 1.0047 1.1473 0.0037  0.6555  0.1091  567 LYS A CB  
4439 C CG  . LYS A 567 ? 1.7453 1.1330 1.2572 0.0076  0.6624  0.0834  567 LYS A CG  
4440 C CD  . LYS A 567 ? 1.8659 1.2666 1.4165 0.0081  0.6854  0.0746  567 LYS A CD  
4441 C CE  . LYS A 567 ? 1.9462 1.3484 1.4797 0.0129  0.6921  0.0489  567 LYS A CE  
4442 N NZ  . LYS A 567 ? 1.8942 1.3111 1.4652 0.0142  0.7153  0.0412  567 LYS A NZ  
4443 N N   . GLY A 568 ? 1.5441 0.9273 1.0261 0.0009  0.6336  0.1675  568 GLY A N   
4444 C CA  . GLY A 568 ? 1.4901 0.8725 0.9870 -0.0010 0.6263  0.1937  568 GLY A CA  
4445 C C   . GLY A 568 ? 1.6459 1.0203 1.1074 0.0010  0.6034  0.2055  568 GLY A C   
4446 O O   . GLY A 568 ? 1.6272 0.9998 1.1059 0.0003  0.5947  0.2267  568 GLY A O   
4447 N N   . LEU A 569 ? 1.6094 0.9789 1.0246 0.0035  0.5933  0.1920  569 LEU A N   
4448 C CA  . LEU A 569 ? 1.7398 1.1027 1.1180 0.0054  0.5714  0.2028  569 LEU A CA  
4449 C C   . LEU A 569 ? 1.8843 1.2523 1.1915 0.0072  0.5722  0.2024  569 LEU A C   
4450 O O   . LEU A 569 ? 1.9124 1.2876 1.1881 0.0078  0.5710  0.2260  569 LEU A O   
4451 C CB  . LEU A 569 ? 1.7587 1.1098 1.1515 0.0057  0.5539  0.1854  569 LEU A CB  
4452 C CG  . LEU A 569 ? 1.5605 0.9086 1.0204 0.0037  0.5517  0.1803  569 LEU A CG  
4453 C CD1 . LEU A 569 ? 1.4617 0.7999 0.9276 0.0038  0.5347  0.1641  569 LEU A CD1 
4454 C CD2 . LEU A 569 ? 1.5949 0.9453 1.0862 0.0031  0.5470  0.2045  569 LEU A CD2 
4455 N N   . GLY A 570 ? 2.0920 1.4572 1.3739 0.0080  0.5736  0.1751  570 GLY A N   
4456 C CA  . GLY A 570 ? 2.1020 1.4734 1.3178 0.0094  0.5756  0.1677  570 GLY A CA  
4457 C C   . GLY A 570 ? 2.2089 1.5765 1.3725 0.0105  0.5528  0.1770  570 GLY A C   
4458 O O   . GLY A 570 ? 2.1540 1.5197 1.2702 0.0111  0.5460  0.1572  570 GLY A O   
4459 N N   . ASP A 571 ? 2.3184 1.6852 1.4920 0.0110  0.5401  0.2061  571 ASP A N   
4460 C CA  . ASP A 571 ? 2.3072 1.6719 1.4357 0.0127  0.5172  0.2201  571 ASP A CA  
4461 C C   . ASP A 571 ? 2.2607 1.6102 1.4027 0.0127  0.4971  0.2091  571 ASP A C   
4462 O O   . ASP A 571 ? 2.2701 1.6166 1.3806 0.0142  0.4764  0.2209  571 ASP A O   
4463 C CB  . ASP A 571 ? 2.2928 1.6643 1.4294 0.0140  0.5126  0.2586  571 ASP A CB  
4464 C CG  . ASP A 571 ? 2.2807 1.6464 1.4919 0.0131  0.5156  0.2693  571 ASP A CG  
4465 O OD1 . ASP A 571 ? 2.2270 1.5876 1.4815 0.0111  0.5253  0.2480  571 ASP A OD1 
4466 O OD2 . ASP A 571 ? 2.2955 1.6625 1.5226 0.0144  0.5075  0.2981  571 ASP A OD2 
4467 N N   . VAL A 572 ? 2.0168 1.3575 1.2046 0.0109  0.5024  0.1881  572 VAL A N   
4468 C CA  . VAL A 572 ? 1.9219 1.2492 1.1250 0.0101  0.4852  0.1783  572 VAL A CA  
4469 C C   . VAL A 572 ? 1.8800 1.2028 1.0289 0.0094  0.4741  0.1562  572 VAL A C   
4470 O O   . VAL A 572 ? 1.9170 1.2406 1.0456 0.0087  0.4864  0.1312  572 VAL A O   
4471 C CB  . VAL A 572 ? 1.7055 1.0278 0.9708 0.0082  0.4939  0.1619  572 VAL A CB  
4472 C CG1 . VAL A 572 ? 1.7018 1.0140 0.9851 0.0070  0.4747  0.1520  572 VAL A CG1 
4473 C CG2 . VAL A 572 ? 1.8175 1.1463 1.1375 0.0082  0.5022  0.1796  572 VAL A CG2 
4474 N N   . ASN A 573 ? 1.8262 1.1520 0.9666 0.0101  0.4438  0.1609  573 ASN A N   
4475 C CA  . ASN A 573 ? 1.8610 1.1913 0.9711 0.0085  0.4221  0.1352  573 ASN A CA  
4476 C C   . ASN A 573 ? 1.7667 1.0916 0.9205 0.0060  0.4173  0.1057  573 ASN A C   
4477 O O   . ASN A 573 ? 1.7924 1.1166 0.9848 0.0053  0.3984  0.1062  573 ASN A O   
4478 C CB  . ASN A 573 ? 1.9019 1.2396 0.9967 0.0096  0.3904  0.1504  573 ASN A CB  
4479 C CG  . ASN A 573 ? 1.9540 1.2971 1.0260 0.0065  0.3656  0.1226  573 ASN A CG  
4480 O OD1 . ASN A 573 ? 1.9343 1.2751 0.9857 0.0040  0.3736  0.0937  573 ASN A OD1 
4481 N ND2 . ASN A 573 ? 2.0048 1.3552 1.0838 0.0066  0.3357  0.1307  573 ASN A ND2 
4482 N N   . VAL A 574 ? 1.7272 1.0486 0.8759 0.0052  0.4352  0.0806  574 VAL A N   
4483 C CA  . VAL A 574 ? 1.7393 1.0549 0.9308 0.0036  0.4324  0.0552  574 VAL A CA  
4484 C C   . VAL A 574 ? 1.7664 1.0822 0.9466 0.0008  0.4051  0.0344  574 VAL A C   
4485 O O   . VAL A 574 ? 1.6577 0.9695 0.8785 -0.0010 0.3939  0.0223  574 VAL A O   
4486 C CB  . VAL A 574 ? 1.7114 1.0233 0.9055 0.0048  0.4605  0.0363  574 VAL A CB  
4487 C CG1 . VAL A 574 ? 1.5966 0.9089 0.8250 0.0063  0.4848  0.0548  574 VAL A CG1 
4488 C CG2 . VAL A 574 ? 1.6916 1.0065 0.8227 0.0055  0.4709  0.0255  574 VAL A CG2 
4489 N N   . GLU A 575 ? 1.8647 1.1860 0.9904 -0.0003 0.3937  0.0302  575 GLU A N   
4490 C CA  . GLU A 575 ? 1.8606 1.1831 0.9763 -0.0043 0.3668  0.0092  575 GLU A CA  
4491 C C   . GLU A 575 ? 1.7958 1.1214 0.9524 -0.0059 0.3422  0.0213  575 GLU A C   
4492 O O   . GLU A 575 ? 1.6595 0.9804 0.8529 -0.0088 0.3327  0.0053  575 GLU A O   
4493 C CB  . GLU A 575 ? 1.9721 1.3033 1.0206 -0.0054 0.3563  0.0068  575 GLU A CB  
4494 C CG  . GLU A 575 ? 2.0622 1.3917 1.0641 -0.0041 0.3812  -0.0084 575 GLU A CG  
4495 C CD  . GLU A 575 ? 2.2285 1.5476 1.2400 -0.0062 0.3878  -0.0475 575 GLU A CD  
4496 O OE1 . GLU A 575 ? 2.0711 1.3836 1.1271 -0.0090 0.3736  -0.0602 575 GLU A OE1 
4497 O OE2 . GLU A 575 ? 2.2625 1.5798 1.2379 -0.0049 0.4083  -0.0651 575 GLU A OE2 
4498 N N   . GLU A 576 ? 1.8654 1.1992 1.0173 -0.0035 0.3326  0.0507  576 GLU A N   
4499 C CA  . GLU A 576 ? 1.8642 1.2027 1.0542 -0.0040 0.3101  0.0628  576 GLU A CA  
4500 C C   . GLU A 576 ? 1.8038 1.1356 1.0531 -0.0028 0.3211  0.0685  576 GLU A C   
4501 O O   . GLU A 576 ? 1.7306 1.0646 1.0171 -0.0042 0.3055  0.0683  576 GLU A O   
4502 C CB  . GLU A 576 ? 1.9518 1.3007 1.1211 -0.0004 0.2975  0.0932  576 GLU A CB  
4503 C CG  . GLU A 576 ? 2.0049 1.3612 1.2119 0.0000  0.2733  0.1054  576 GLU A CG  
4504 C CD  . GLU A 576 ? 2.1035 1.4704 1.2907 0.0049  0.2600  0.1362  576 GLU A CD  
4505 O OE1 . GLU A 576 ? 2.1550 1.5209 1.3063 0.0083  0.2738  0.1536  576 GLU A OE1 
4506 O OE2 . GLU A 576 ? 2.1128 1.4896 1.3218 0.0056  0.2361  0.1441  576 GLU A OE2 
4507 N N   . LEU A 577 ? 1.7423 1.0674 1.0014 -0.0005 0.3477  0.0730  577 LEU A N   
4508 C CA  . LEU A 577 ? 1.5678 0.8883 0.8811 0.0003  0.3572  0.0781  577 LEU A CA  
4509 C C   . LEU A 577 ? 1.4942 0.8103 0.8387 -0.0025 0.3545  0.0538  577 LEU A C   
4510 O O   . LEU A 577 ? 1.3595 0.6748 0.7482 -0.0026 0.3540  0.0567  577 LEU A O   
4511 C CB  . LEU A 577 ? 1.5309 0.8472 0.8475 0.0025  0.3855  0.0888  577 LEU A CB  
4512 C CG  . LEU A 577 ? 1.4452 0.7584 0.8159 0.0029  0.3958  0.0957  577 LEU A CG  
4513 C CD1 . LEU A 577 ? 1.4398 0.7554 0.8368 0.0038  0.3794  0.1129  577 LEU A CD1 
4514 C CD2 . LEU A 577 ? 1.4347 0.7455 0.8067 0.0040  0.4227  0.1081  577 LEU A CD2 
4515 N N   . PHE A 578 ? 1.5366 0.8495 0.8590 -0.0048 0.3530  0.0300  578 PHE A N   
4516 C CA  . PHE A 578 ? 1.4314 0.7385 0.7830 -0.0072 0.3496  0.0084  578 PHE A CA  
4517 C C   . PHE A 578 ? 1.4335 0.7410 0.7724 -0.0119 0.3272  -0.0082 578 PHE A C   
4518 O O   . PHE A 578 ? 1.4467 0.7476 0.8084 -0.0145 0.3241  -0.0260 578 PHE A O   
4519 C CB  . PHE A 578 ? 1.3654 0.6649 0.7166 -0.0053 0.3724  -0.0081 578 PHE A CB  
4520 C CG  . PHE A 578 ? 1.3446 0.6437 0.7340 -0.0025 0.3901  0.0011  578 PHE A CG  
4521 C CD1 . PHE A 578 ? 1.3089 0.6064 0.7431 -0.0029 0.3862  -0.0036 578 PHE A CD1 
4522 C CD2 . PHE A 578 ? 1.3402 0.6417 0.7210 0.0002  0.4105  0.0146  578 PHE A CD2 
4523 C CE1 . PHE A 578 ? 1.2678 0.5672 0.7363 -0.0008 0.4003  0.0034  578 PHE A CE1 
4524 C CE2 . PHE A 578 ? 1.3950 0.6975 0.8142 0.0017  0.4256  0.0213  578 PHE A CE2 
4525 C CZ  . PHE A 578 ? 1.3562 0.6582 0.8189 0.0012  0.4195  0.0149  578 PHE A CZ  
4526 N N   . GLY A 579 ? 1.4797 0.7950 0.7850 -0.0134 0.3110  -0.0022 579 GLY A N   
4527 C CA  . GLY A 579 ? 1.5036 0.8214 0.7981 -0.0190 0.2882  -0.0188 579 GLY A CA  
4528 C C   . GLY A 579 ? 1.4769 0.7943 0.8187 -0.0228 0.2745  -0.0229 579 GLY A C   
4529 O O   . GLY A 579 ? 1.4402 0.7647 0.8109 -0.0216 0.2680  -0.0044 579 GLY A O   
4530 N N   . ILE A 580 ? 1.4551 0.7638 0.8060 -0.0275 0.2715  -0.0471 580 ILE A N   
4531 C CA  . ILE A 580 ? 1.4128 0.7207 0.8063 -0.0322 0.2589  -0.0512 580 ILE A CA  
4532 C C   . ILE A 580 ? 1.3638 0.6772 0.7460 -0.0397 0.2345  -0.0637 580 ILE A C   
4533 O O   . ILE A 580 ? 1.5321 0.8359 0.9084 -0.0448 0.2315  -0.0880 580 ILE A O   
4534 C CB  . ILE A 580 ? 1.3399 0.6331 0.7603 -0.0321 0.2728  -0.0662 580 ILE A CB  
4535 C CG1 . ILE A 580 ? 1.3828 0.6745 0.8215 -0.0253 0.2937  -0.0527 580 ILE A CG1 
4536 C CG2 . ILE A 580 ? 1.3394 0.6312 0.7986 -0.0381 0.2593  -0.0705 580 ILE A CG2 
4537 C CD1 . ILE A 580 ? 1.3608 0.6410 0.8296 -0.0240 0.3055  -0.0637 580 ILE A CD1 
4538 N N   . SER A 581 ? 1.3640 0.6931 0.7461 -0.0405 0.2167  -0.0477 581 SER A N   
4539 C CA  . SER A 581 ? 1.3917 0.7303 0.7657 -0.0479 0.1910  -0.0578 581 SER A CA  
4540 C C   . SER A 581 ? 1.4315 0.7683 0.8526 -0.0551 0.1815  -0.0660 581 SER A C   
4541 O O   . SER A 581 ? 1.4894 0.8310 0.9492 -0.0535 0.1835  -0.0502 581 SER A O   
4542 C CB  . SER A 581 ? 1.4604 0.8185 0.8232 -0.0452 0.1748  -0.0354 581 SER A CB  
4543 O OG  . SER A 581 ? 1.5457 0.9165 0.9082 -0.0526 0.1477  -0.0444 581 SER A OG  
4544 N N   . LYS A 582 ? 1.5128 0.8426 0.9308 -0.0634 0.1721  -0.0913 582 LYS A N   
4545 C CA  . LYS A 582 ? 1.4840 0.8122 0.9472 -0.0716 0.1622  -0.0982 582 LYS A CA  
4546 C C   . LYS A 582 ? 1.4593 0.8095 0.9446 -0.0749 0.1412  -0.0828 582 LYS A C   
4547 O O   . LYS A 582 ? 1.4232 0.7772 0.9533 -0.0773 0.1405  -0.0738 582 LYS A O   
4548 C CB  . LYS A 582 ? 1.4984 0.8141 0.9536 -0.0807 0.1549  -0.1293 582 LYS A CB  
4549 C CG  . LYS A 582 ? 1.3703 0.6829 0.8733 -0.0908 0.1445  -0.1368 582 LYS A CG  
4550 C CD  . LYS A 582 ? 1.4513 0.7476 0.9479 -0.0996 0.1392  -0.1694 582 LYS A CD  
4551 C CE  . LYS A 582 ? 1.4239 0.7157 0.9716 -0.1107 0.1297  -0.1754 582 LYS A CE  
4552 N NZ  . LYS A 582 ? 1.4545 0.7278 0.9997 -0.1199 0.1249  -0.2087 582 LYS A NZ  
4553 N N   . GLU A 583 ? 1.5822 0.9483 1.0369 -0.0744 0.1244  -0.0787 583 GLU A N   
4554 C CA  . GLU A 583 ? 1.5918 0.9811 1.0695 -0.0763 0.1032  -0.0636 583 GLU A CA  
4555 C C   . GLU A 583 ? 1.5478 0.9435 1.0572 -0.0682 0.1142  -0.0366 583 GLU A C   
4556 O O   . GLU A 583 ? 1.5230 0.9321 1.0737 -0.0708 0.1051  -0.0275 583 GLU A O   
4557 C CB  . GLU A 583 ? 1.6844 1.0899 1.1191 -0.0749 0.0841  -0.0606 583 GLU A CB  
4558 C CG  . GLU A 583 ? 1.7859 1.1878 1.1840 -0.0834 0.0712  -0.0899 583 GLU A CG  
4559 C CD  . GLU A 583 ? 1.8312 1.2110 1.1898 -0.0802 0.0933  -0.1060 583 GLU A CD  
4560 O OE1 . GLU A 583 ? 1.7840 1.1549 1.1383 -0.0709 0.1166  -0.0909 583 GLU A OE1 
4561 O OE2 . GLU A 583 ? 1.8661 1.2379 1.2005 -0.0873 0.0878  -0.1348 583 GLU A OE2 
4562 N N   . PHE A 584 ? 1.4232 0.8098 0.9153 -0.0588 0.1345  -0.0248 584 PHE A N   
4563 C CA  . PHE A 584 ? 1.3219 0.7133 0.8430 -0.0514 0.1454  -0.0019 584 PHE A CA  
4564 C C   . PHE A 584 ? 1.2484 0.6318 0.8108 -0.0539 0.1579  -0.0051 584 PHE A C   
4565 O O   . PHE A 584 ? 1.2280 0.6217 0.8267 -0.0528 0.1573  0.0077  584 PHE A O   
4566 C CB  . PHE A 584 ? 1.3016 0.6855 0.7944 -0.0418 0.1631  0.0107  584 PHE A CB  
4567 C CG  . PHE A 584 ? 1.2260 0.6102 0.7496 -0.0351 0.1775  0.0292  584 PHE A CG  
4568 C CD1 . PHE A 584 ? 1.1739 0.5728 0.7173 -0.0305 0.1691  0.0488  584 PHE A CD1 
4569 C CD2 . PHE A 584 ? 1.2285 0.5988 0.7627 -0.0332 0.1989  0.0257  584 PHE A CD2 
4570 C CE1 . PHE A 584 ? 1.1822 0.5803 0.7542 -0.0246 0.1829  0.0626  584 PHE A CE1 
4571 C CE2 . PHE A 584 ? 1.1277 0.4991 0.6889 -0.0279 0.2110  0.0399  584 PHE A CE2 
4572 C CZ  . PHE A 584 ? 1.1205 0.5050 0.7000 -0.0238 0.2036  0.0572  584 PHE A CZ  
4573 N N   . TRP A 585 ? 1.2373 0.6027 0.7945 -0.0569 0.1697  -0.0216 585 TRP A N   
4574 C CA  . TRP A 585 ? 1.2499 0.6071 0.8422 -0.0580 0.1825  -0.0217 585 TRP A CA  
4575 C C   . TRP A 585 ? 1.2508 0.6127 0.8779 -0.0676 0.1705  -0.0280 585 TRP A C   
4576 O O   . TRP A 585 ? 1.1577 0.5189 0.8175 -0.0684 0.1789  -0.0218 585 TRP A O   
4577 C CB  . TRP A 585 ? 1.2447 0.5815 0.8224 -0.0561 0.1997  -0.0344 585 TRP A CB  
4578 C CG  . TRP A 585 ? 1.2803 0.6141 0.8378 -0.0468 0.2161  -0.0245 585 TRP A CG  
4579 C CD1 . TRP A 585 ? 1.2864 0.6183 0.8039 -0.0430 0.2194  -0.0259 585 TRP A CD1 
4580 C CD2 . TRP A 585 ? 1.2113 0.5448 0.7884 -0.0409 0.2316  -0.0113 585 TRP A CD2 
4581 N NE1 . TRP A 585 ? 1.2027 0.5324 0.7173 -0.0355 0.2369  -0.0136 585 TRP A NE1 
4582 C CE2 . TRP A 585 ? 1.1786 0.5093 0.7301 -0.0343 0.2437  -0.0057 585 TRP A CE2 
4583 C CE3 . TRP A 585 ? 1.1519 0.4882 0.7648 -0.0411 0.2364  -0.0043 585 TRP A CE3 
4584 C CZ2 . TRP A 585 ? 1.1977 0.5276 0.7619 -0.0285 0.2594  0.0054  585 TRP A CZ2 
4585 C CZ3 . TRP A 585 ? 1.2082 0.5445 0.8293 -0.0349 0.2511  0.0058  585 TRP A CZ3 
4586 C CH2 . TRP A 585 ? 1.1608 0.4938 0.7596 -0.0290 0.2620  0.0098  585 TRP A CH2 
4587 N N   . GLU A 586 ? 1.2634 0.6310 0.8844 -0.0755 0.1512  -0.0400 586 GLU A N   
4588 C CA  . GLU A 586 ? 1.2047 0.5799 0.8645 -0.0856 0.1391  -0.0439 586 GLU A CA  
4589 C C   . GLU A 586 ? 1.2003 0.5984 0.8908 -0.0836 0.1332  -0.0243 586 GLU A C   
4590 O O   . GLU A 586 ? 1.1456 0.5495 0.8760 -0.0890 0.1338  -0.0204 586 GLU A O   
4591 C CB  . GLU A 586 ? 1.3559 0.7324 1.0032 -0.0954 0.1187  -0.0640 586 GLU A CB  
4592 C CG  . GLU A 586 ? 1.3135 0.6658 0.9422 -0.0994 0.1252  -0.0879 586 GLU A CG  
4593 C CD  . GLU A 586 ? 1.5000 0.8529 1.1280 -0.1117 0.1046  -0.1108 586 GLU A CD  
4594 O OE1 . GLU A 586 ? 1.4809 0.8556 1.1139 -0.1162 0.0835  -0.1077 586 GLU A OE1 
4595 O OE2 . GLU A 586 ? 1.4490 0.7808 1.0738 -0.1169 0.1092  -0.1326 586 GLU A OE2 
4596 N N   . LYS A 587 ? 1.2728 0.6837 0.9466 -0.0756 0.1284  -0.0110 587 LYS A N   
4597 C CA  . LYS A 587 ? 1.1149 0.5457 0.8195 -0.0713 0.1258  0.0079  587 LYS A CA  
4598 C C   . LYS A 587 ? 1.1086 0.5337 0.8281 -0.0641 0.1482  0.0197  587 LYS A C   
4599 O O   . LYS A 587 ? 1.0997 0.5370 0.8553 -0.0639 0.1514  0.0292  587 LYS A O   
4600 C CB  . LYS A 587 ? 1.1392 0.5841 0.8230 -0.0645 0.1126  0.0192  587 LYS A CB  
4601 C CG  . LYS A 587 ? 1.2683 0.7288 0.9799 -0.0559 0.1155  0.0406  587 LYS A CG  
4602 C CD  . LYS A 587 ? 1.2852 0.7668 1.0451 -0.0612 0.1045  0.0434  587 LYS A CD  
4603 C CE  . LYS A 587 ? 1.2883 0.7860 1.0757 -0.0513 0.1072  0.0632  587 LYS A CE  
4604 N NZ  . LYS A 587 ? 1.3211 0.8423 1.1579 -0.0559 0.0973  0.0661  587 LYS A NZ  
4605 N N   . GLU A 588 ? 1.1256 0.5334 0.8181 -0.0585 0.1639  0.0181  588 GLU A N   
4606 C CA  . GLU A 588 ? 1.0928 0.4961 0.7977 -0.0521 0.1835  0.0274  588 GLU A CA  
4607 C C   . GLU A 588 ? 1.0811 0.4826 0.8167 -0.0577 0.1909  0.0245  588 GLU A C   
4608 O O   . GLU A 588 ? 1.0242 0.4342 0.7841 -0.0549 0.1994  0.0343  588 GLU A O   
4609 C CB  . GLU A 588 ? 1.0912 0.4773 0.7640 -0.0466 0.1977  0.0243  588 GLU A CB  
4610 C CG  . GLU A 588 ? 1.0830 0.4676 0.7646 -0.0391 0.2149  0.0351  588 GLU A CG  
4611 C CD  . GLU A 588 ? 1.0272 0.4239 0.7149 -0.0324 0.2123  0.0504  588 GLU A CD  
4612 O OE1 . GLU A 588 ? 1.0845 0.4870 0.7560 -0.0313 0.1994  0.0546  588 GLU A OE1 
4613 O OE2 . GLU A 588 ? 1.0038 0.4041 0.7127 -0.0282 0.2227  0.0581  588 GLU A OE2 
4614 N N   . VAL A 589 ? 1.1940 0.5838 0.9286 -0.0654 0.1883  0.0111  589 VAL A N   
4615 C CA  . VAL A 589 ? 1.1311 0.5178 0.8946 -0.0710 0.1952  0.0109  589 VAL A CA  
4616 C C   . VAL A 589 ? 1.1017 0.5084 0.9013 -0.0763 0.1876  0.0186  589 VAL A C   
4617 O O   . VAL A 589 ? 1.0981 0.5109 0.9220 -0.0764 0.1979  0.0273  589 VAL A O   
4618 C CB  . VAL A 589 ? 1.0958 0.4638 0.8539 -0.0781 0.1933  -0.0049 589 VAL A CB  
4619 C CG1 . VAL A 589 ? 1.0469 0.3963 0.7790 -0.0715 0.2065  -0.0106 589 VAL A CG1 
4620 C CG2 . VAL A 589 ? 1.1514 0.5217 0.8992 -0.0850 0.1743  -0.0179 589 VAL A CG2 
4621 N N   . GLU A 590 ? 1.1546 0.5735 0.9582 -0.0807 0.1694  0.0154  590 GLU A N   
4622 C CA  . GLU A 590 ? 1.1325 0.5735 0.9744 -0.0855 0.1617  0.0228  590 GLU A CA  
4623 C C   . GLU A 590 ? 1.1724 0.6277 1.0291 -0.0764 0.1726  0.0383  590 GLU A C   
4624 O O   . GLU A 590 ? 1.1497 0.6160 1.0381 -0.0787 0.1806  0.0450  590 GLU A O   
4625 C CB  . GLU A 590 ? 1.2181 0.6726 1.0592 -0.0897 0.1383  0.0176  590 GLU A CB  
4626 C CG  . GLU A 590 ? 1.2770 0.7575 1.1627 -0.0949 0.1284  0.0246  590 GLU A CG  
4627 C CD  . GLU A 590 ? 1.6072 1.0865 1.5250 -0.1085 0.1276  0.0176  590 GLU A CD  
4628 O OE1 . GLU A 590 ? 1.6882 1.1473 1.5917 -0.1155 0.1260  0.0036  590 GLU A OE1 
4629 O OE2 . GLU A 590 ? 1.5728 1.0708 1.5321 -0.1123 0.1297  0.0263  590 GLU A OE2 
4630 N N   . GLU A 591 ? 1.1377 0.5924 0.9721 -0.0662 0.1742  0.0437  591 GLU A N   
4631 C CA  . GLU A 591 ? 1.0450 0.5109 0.8948 -0.0573 0.1848  0.0562  591 GLU A CA  
4632 C C   . GLU A 591 ? 1.0170 0.4748 0.8701 -0.0556 0.2052  0.0573  591 GLU A C   
4633 O O   . GLU A 591 ? 1.0514 0.5221 0.9302 -0.0538 0.2143  0.0638  591 GLU A O   
4634 C CB  . GLU A 591 ? 1.0644 0.5278 0.8903 -0.0473 0.1826  0.0623  591 GLU A CB  
4635 C CG  . GLU A 591 ? 1.1485 0.6268 0.9766 -0.0466 0.1619  0.0667  591 GLU A CG  
4636 C CD  . GLU A 591 ? 1.2088 0.7114 1.0821 -0.0477 0.1556  0.0735  591 GLU A CD  
4637 O OE1 . GLU A 591 ? 1.1928 0.7019 1.0903 -0.0425 0.1699  0.0802  591 GLU A OE1 
4638 O OE2 . GLU A 591 ? 1.1328 0.6493 1.0187 -0.0540 0.1366  0.0710  591 GLU A OE2 
4639 N N   . ILE A 592 ? 0.9992 0.4372 0.8269 -0.0556 0.2126  0.0508  592 ILE A N   
4640 C CA  . ILE A 592 ? 1.0128 0.4449 0.8431 -0.0541 0.2294  0.0523  592 ILE A CA  
4641 C C   . ILE A 592 ? 1.0850 0.5235 0.9415 -0.0622 0.2318  0.0539  592 ILE A C   
4642 O O   . ILE A 592 ? 1.0449 0.4917 0.9152 -0.0608 0.2439  0.0601  592 ILE A O   
4643 C CB  . ILE A 592 ? 1.0220 0.4333 0.8234 -0.0522 0.2353  0.0454  592 ILE A CB  
4644 C CG1 . ILE A 592 ? 1.1120 0.5184 0.8890 -0.0446 0.2354  0.0459  592 ILE A CG1 
4645 C CG2 . ILE A 592 ? 0.9543 0.3619 0.7595 -0.0504 0.2500  0.0478  592 ILE A CG2 
4646 C CD1 . ILE A 592 ? 1.0088 0.3974 0.7607 -0.0420 0.2437  0.0396  592 ILE A CD1 
4647 N N   . ASP A 593 ? 1.0980 0.5332 0.9619 -0.0713 0.2208  0.0483  593 ASP A N   
4648 C CA  . ASP A 593 ? 1.0570 0.4977 0.9497 -0.0802 0.2233  0.0516  593 ASP A CA  
4649 C C   . ASP A 593 ? 1.0476 0.5135 0.9712 -0.0802 0.2256  0.0608  593 ASP A C   
4650 O O   . ASP A 593 ? 1.0462 0.5200 0.9842 -0.0803 0.2393  0.0684  593 ASP A O   
4651 C CB  . ASP A 593 ? 1.0424 0.4749 0.9415 -0.0907 0.2096  0.0422  593 ASP A CB  
4652 C CG  . ASP A 593 ? 1.1338 0.5694 1.0657 -0.1011 0.2131  0.0467  593 ASP A CG  
4653 O OD1 . ASP A 593 ? 1.1243 0.5507 1.0561 -0.1007 0.2265  0.0527  593 ASP A OD1 
4654 O OD2 . ASP A 593 ? 1.0842 0.5321 1.0431 -0.1099 0.2023  0.0453  593 ASP A OD2 
4655 N N   . LYS A 594 ? 1.0645 0.5445 0.9986 -0.0796 0.2125  0.0604  594 LYS A N   
4656 C CA  . LYS A 594 ? 1.0230 0.5283 0.9913 -0.0785 0.2146  0.0686  594 LYS A CA  
4657 C C   . LYS A 594 ? 1.0136 0.5241 0.9798 -0.0688 0.2324  0.0746  594 LYS A C   
4658 O O   . LYS A 594 ? 0.9927 0.5192 0.9841 -0.0695 0.2437  0.0803  594 LYS A O   
4659 C CB  . LYS A 594 ? 1.0088 0.5278 0.9858 -0.0765 0.1963  0.0683  594 LYS A CB  
4660 C CG  . LYS A 594 ? 1.0222 0.5413 1.0050 -0.0874 0.1766  0.0604  594 LYS A CG  
4661 C CD  . LYS A 594 ? 1.0823 0.6197 1.0748 -0.0848 0.1569  0.0620  594 LYS A CD  
4662 C CE  . LYS A 594 ? 1.0775 0.6074 1.0360 -0.0723 0.1551  0.0651  594 LYS A CE  
4663 N NZ  . LYS A 594 ? 1.0370 0.5851 1.0035 -0.0686 0.1348  0.0698  594 LYS A NZ  
4664 N N   . TYR A 595 ? 1.0023 0.4996 0.9390 -0.0600 0.2358  0.0725  595 TYR A N   
4665 C CA  . TYR A 595 ? 0.9665 0.4673 0.9014 -0.0515 0.2517  0.0754  595 TYR A CA  
4666 C C   . TYR A 595 ? 0.9965 0.4954 0.9295 -0.0547 0.2668  0.0763  595 TYR A C   
4667 O O   . TYR A 595 ? 0.9395 0.4534 0.8890 -0.0532 0.2791  0.0798  595 TYR A O   
4668 C CB  . TYR A 595 ? 0.9995 0.4851 0.9053 -0.0432 0.2518  0.0727  595 TYR A CB  
4669 C CG  . TYR A 595 ? 0.9611 0.4486 0.8667 -0.0352 0.2669  0.0732  595 TYR A CG  
4670 C CD1 . TYR A 595 ? 0.8817 0.3823 0.8085 -0.0283 0.2694  0.0765  595 TYR A CD1 
4671 C CD2 . TYR A 595 ? 0.9440 0.4207 0.8305 -0.0343 0.2779  0.0694  595 TYR A CD2 
4672 C CE1 . TYR A 595 ? 0.9453 0.4463 0.8737 -0.0215 0.2834  0.0741  595 TYR A CE1 
4673 C CE2 . TYR A 595 ? 0.8731 0.3524 0.7598 -0.0280 0.2903  0.0673  595 TYR A CE2 
4674 C CZ  . TYR A 595 ? 0.9430 0.4335 0.8503 -0.0220 0.2935  0.0687  595 TYR A CZ  
4675 O OH  . TYR A 595 ? 1.0139 0.5055 0.9230 -0.0162 0.3061  0.0638  595 TYR A OH  
4676 N N   . LEU A 596 ? 0.9902 0.4713 0.9031 -0.0587 0.2661  0.0736  596 LEU A N   
4677 C CA  . LEU A 596 ? 1.0602 0.5389 0.9687 -0.0607 0.2788  0.0768  596 LEU A CA  
4678 C C   . LEU A 596 ? 1.0532 0.5462 0.9888 -0.0687 0.2834  0.0843  596 LEU A C   
4679 O O   . LEU A 596 ? 1.0434 0.5458 0.9814 -0.0682 0.2971  0.0900  596 LEU A O   
4680 C CB  . LEU A 596 ? 1.0604 0.5168 0.9466 -0.0624 0.2757  0.0733  596 LEU A CB  
4681 C CG  . LEU A 596 ? 0.9926 0.4361 0.8521 -0.0546 0.2760  0.0671  596 LEU A CG  
4682 C CD1 . LEU A 596 ? 0.9218 0.3448 0.7649 -0.0564 0.2730  0.0628  596 LEU A CD1 
4683 C CD2 . LEU A 596 ? 0.9096 0.3601 0.7632 -0.0481 0.2885  0.0684  596 LEU A CD2 
4684 N N   . GLU A 597 ? 1.0480 0.5437 1.0041 -0.0766 0.2724  0.0844  597 GLU A N   
4685 C CA  . GLU A 597 ? 1.0629 0.5729 1.0497 -0.0855 0.2776  0.0924  597 GLU A CA  
4686 C C   . GLU A 597 ? 1.0251 0.5609 1.0331 -0.0815 0.2884  0.0968  597 GLU A C   
4687 O O   . GLU A 597 ? 1.0520 0.6003 1.0731 -0.0849 0.3025  0.1048  597 GLU A O   
4688 C CB  . GLU A 597 ? 1.1263 0.6353 1.1346 -0.0955 0.2619  0.0893  597 GLU A CB  
4689 C CG  . GLU A 597 ? 1.1943 0.7191 1.2407 -0.1060 0.2670  0.0978  597 GLU A CG  
4690 C CD  . GLU A 597 ? 1.2498 0.7765 1.3220 -0.1166 0.2495  0.0924  597 GLU A CD  
4691 O OE1 . GLU A 597 ? 1.2031 0.7183 1.2588 -0.1153 0.2330  0.0815  597 GLU A OE1 
4692 O OE2 . GLU A 597 ? 1.3094 0.8500 1.4183 -0.1265 0.2525  0.0988  597 GLU A OE2 
4693 N N   . ASP A 598 ? 1.0876 0.6315 1.0995 -0.0739 0.2829  0.0923  598 ASP A N   
4694 C CA  . ASP A 598 ? 1.0269 0.5948 1.0639 -0.0690 0.2931  0.0949  598 ASP A CA  
4695 C C   . ASP A 598 ? 1.0094 0.5780 1.0279 -0.0609 0.3106  0.0932  598 ASP A C   
4696 O O   . ASP A 598 ? 1.0540 0.6397 1.0855 -0.0612 0.3265  0.0965  598 ASP A O   
4697 C CB  . ASP A 598 ? 1.0314 0.6068 1.0827 -0.0629 0.2798  0.0922  598 ASP A CB  
4698 C CG  . ASP A 598 ? 1.1647 0.7614 1.2412 -0.0546 0.2913  0.0934  598 ASP A CG  
4699 O OD1 . ASP A 598 ? 1.2265 0.8441 1.3339 -0.0587 0.3011  0.0977  598 ASP A OD1 
4700 O OD2 . ASP A 598 ? 1.1504 0.7427 1.2179 -0.0441 0.2915  0.0901  598 ASP A OD2 
4701 N N   . GLN A 599 ? 0.9490 0.5003 0.9371 -0.0541 0.3084  0.0873  599 GLN A N   
4702 C CA  . GLN A 599 ? 0.9193 0.4728 0.8940 -0.0461 0.3223  0.0826  599 GLN A CA  
4703 C C   . GLN A 599 ? 0.9725 0.5226 0.9253 -0.0490 0.3332  0.0844  599 GLN A C   
4704 O O   . GLN A 599 ? 0.9899 0.5532 0.9417 -0.0464 0.3481  0.0829  599 GLN A O   
4705 C CB  . GLN A 599 ? 0.9083 0.4462 0.8648 -0.0382 0.3156  0.0761  599 GLN A CB  
4706 C CG  . GLN A 599 ? 0.9282 0.4712 0.9050 -0.0332 0.3059  0.0768  599 GLN A CG  
4707 C CD  . GLN A 599 ? 0.9339 0.4960 0.9391 -0.0267 0.3171  0.0756  599 GLN A CD  
4708 O OE1 . GLN A 599 ? 0.8609 0.4236 0.8598 -0.0214 0.3309  0.0692  599 GLN A OE1 
4709 N NE2 . GLN A 599 ? 0.9311 0.5097 0.9696 -0.0270 0.3111  0.0806  599 GLN A NE2 
4710 N N   . VAL A 600 ? 0.9306 0.4638 0.8656 -0.0538 0.3262  0.0873  600 VAL A N   
4711 C CA  . VAL A 600 ? 0.8817 0.4127 0.7979 -0.0559 0.3348  0.0918  600 VAL A CA  
4712 C C   . VAL A 600 ? 0.9806 0.5199 0.9127 -0.0650 0.3396  0.1040  600 VAL A C   
4713 O O   . VAL A 600 ? 0.9663 0.5134 0.8891 -0.0662 0.3512  0.1110  600 VAL A O   
4714 C CB  . VAL A 600 ? 0.9862 0.4947 0.8770 -0.0546 0.3266  0.0894  600 VAL A CB  
4715 C CG1 . VAL A 600 ? 0.9477 0.4571 0.8185 -0.0537 0.3349  0.0934  600 VAL A CG1 
4716 C CG2 . VAL A 600 ? 0.9797 0.4788 0.8600 -0.0473 0.3209  0.0790  600 VAL A CG2 
4717 N N   . ASN A 601 ? 0.9425 0.4808 0.8986 -0.0718 0.3306  0.1070  601 ASN A N   
4718 C CA  . ASN A 601 ? 1.0094 0.5586 0.9901 -0.0814 0.3362  0.1183  601 ASN A CA  
4719 C C   . ASN A 601 ? 0.9973 0.5385 0.9632 -0.0855 0.3434  0.1298  601 ASN A C   
4720 O O   . ASN A 601 ? 0.9995 0.5190 0.9518 -0.0866 0.3347  0.1301  601 ASN A O   
4721 C CB  . ASN A 601 ? 0.9670 0.5439 0.9700 -0.0801 0.3501  0.1201  601 ASN A CB  
4722 C CG  . ASN A 601 ? 1.0681 0.6592 1.1063 -0.0908 0.3545  0.1309  601 ASN A CG  
4723 O OD1 . ASN A 601 ? 1.1272 0.7064 1.1775 -0.0997 0.3442  0.1352  601 ASN A OD1 
4724 N ND2 . ASN A 601 ? 1.0036 0.6202 1.0604 -0.0902 0.3707  0.1344  601 ASN A ND2 
4725 N N   . ALA A 602 ? 0.9845 0.5438 0.9528 -0.0871 0.3598  0.1398  602 ALA A N   
4726 C CA  . ALA A 602 ? 0.9369 0.4921 0.8945 -0.0917 0.3673  0.1554  602 ALA A CA  
4727 C C   . ALA A 602 ? 0.9507 0.4994 0.8701 -0.0839 0.3690  0.1547  602 ALA A C   
4728 O O   . ALA A 602 ? 1.0651 0.6099 0.9729 -0.0861 0.3731  0.1692  602 ALA A O   
4729 C CB  . ALA A 602 ? 0.9485 0.5282 0.9229 -0.0971 0.3853  0.1683  602 ALA A CB  
4730 N N   . ASP A 603 ? 0.9870 0.5350 0.8888 -0.0751 0.3655  0.1395  603 ASP A N   
4731 C CA  . ASP A 603 ? 0.9986 0.5409 0.8680 -0.0684 0.3647  0.1365  603 ASP A CA  
4732 C C   . ASP A 603 ? 0.9481 0.4664 0.8090 -0.0652 0.3500  0.1288  603 ASP A C   
4733 O O   . ASP A 603 ? 0.9229 0.4360 0.7612 -0.0596 0.3477  0.1255  603 ASP A O   
4734 C CB  . ASP A 603 ? 0.9313 0.4906 0.7877 -0.0613 0.3733  0.1239  603 ASP A CB  
4735 C CG  . ASP A 603 ? 1.0095 0.5933 0.8632 -0.0632 0.3905  0.1311  603 ASP A CG  
4736 O OD1 . ASP A 603 ? 1.0292 0.6166 0.8652 -0.0652 0.3949  0.1446  603 ASP A OD1 
4737 O OD2 . ASP A 603 ? 0.9490 0.5491 0.8185 -0.0621 0.4000  0.1239  603 ASP A OD2 
4738 N N   . LEU A 604 ? 0.9167 0.4218 0.7952 -0.0688 0.3401  0.1253  604 LEU A N   
4739 C CA  . LEU A 604 ? 0.9418 0.4242 0.8117 -0.0663 0.3278  0.1178  604 LEU A CA  
4740 C C   . LEU A 604 ? 0.9380 0.4061 0.8001 -0.0675 0.3261  0.1280  604 LEU A C   
4741 O O   . LEU A 604 ? 1.0262 0.4926 0.9042 -0.0742 0.3265  0.1396  604 LEU A O   
4742 C CB  . LEU A 604 ? 0.9447 0.4184 0.8336 -0.0711 0.3177  0.1120  604 LEU A CB  
4743 C CG  . LEU A 604 ? 0.9733 0.4243 0.8513 -0.0690 0.3061  0.1025  604 LEU A CG  
4744 C CD1 . LEU A 604 ? 0.9268 0.3774 0.7853 -0.0600 0.3058  0.0921  604 LEU A CD1 
4745 C CD2 . LEU A 604 ? 0.9455 0.3900 0.8404 -0.0753 0.2953  0.0970  604 LEU A CD2 
4746 N N   . PRO A 605 ? 0.9577 0.4176 0.7999 -0.0607 0.3233  0.1243  605 PRO A N   
4747 C CA  . PRO A 605 ? 1.0028 0.4529 0.8432 -0.0597 0.3185  0.1333  605 PRO A CA  
4748 C C   . PRO A 605 ? 0.9369 0.3731 0.7952 -0.0629 0.3068  0.1286  605 PRO A C   
4749 O O   . PRO A 605 ? 1.0165 0.4447 0.8773 -0.0635 0.3010  0.1152  605 PRO A O   
4750 C CB  . PRO A 605 ? 1.0207 0.4651 0.8398 -0.0517 0.3177  0.1268  605 PRO A CB  
4751 C CG  . PRO A 605 ? 0.9191 0.3806 0.7287 -0.0486 0.3224  0.1161  605 PRO A CG  
4752 C CD  . PRO A 605 ? 0.9125 0.3764 0.7381 -0.0531 0.3229  0.1113  605 PRO A CD  
4753 N N   . TYR A 606 ? 0.9810 0.4136 0.8514 -0.0653 0.3037  0.1401  606 TYR A N   
4754 C CA  . TYR A 606 ? 1.0457 0.4631 0.9349 -0.0694 0.2938  0.1347  606 TYR A CA  
4755 C C   . TYR A 606 ? 0.9726 0.3752 0.8518 -0.0631 0.2866  0.1192  606 TYR A C   
4756 O O   . TYR A 606 ? 0.9826 0.3732 0.8681 -0.0663 0.2801  0.1065  606 TYR A O   
4757 C CB  . TYR A 606 ? 1.0205 0.4354 0.9262 -0.0724 0.2926  0.1510  606 TYR A CB  
4758 C CG  . TYR A 606 ? 1.1163 0.5119 1.0408 -0.0753 0.2829  0.1438  606 TYR A CG  
4759 C CD1 . TYR A 606 ? 1.1647 0.5537 1.1086 -0.0849 0.2787  0.1359  606 TYR A CD1 
4760 C CD2 . TYR A 606 ? 1.0591 0.4423 0.9834 -0.0685 0.2784  0.1441  606 TYR A CD2 
4761 C CE1 . TYR A 606 ? 1.1421 0.5115 1.1019 -0.0883 0.2704  0.1269  606 TYR A CE1 
4762 C CE2 . TYR A 606 ? 1.1214 0.4859 1.0634 -0.0709 0.2710  0.1356  606 TYR A CE2 
4763 C CZ  . TYR A 606 ? 1.1701 0.5272 1.1286 -0.0810 0.2671  0.1263  606 TYR A CZ  
4764 O OH  . TYR A 606 ? 1.1439 0.4805 1.1190 -0.0841 0.2602  0.1155  606 TYR A OH  
4765 N N   . GLU A 607 ? 0.9491 0.3522 0.8125 -0.0545 0.2882  0.1200  607 GLU A N   
4766 C CA  . GLU A 607 ? 0.9864 0.3776 0.8425 -0.0483 0.2835  0.1061  607 GLU A CA  
4767 C C   . GLU A 607 ? 1.0207 0.4102 0.8665 -0.0488 0.2825  0.0900  607 GLU A C   
4768 O O   . GLU A 607 ? 1.0106 0.3878 0.8540 -0.0474 0.2781  0.0774  607 GLU A O   
4769 C CB  . GLU A 607 ? 1.0076 0.4017 0.8511 -0.0398 0.2867  0.1108  607 GLU A CB  
4770 C CG  . GLU A 607 ? 1.0476 0.4393 0.9012 -0.0376 0.2856  0.1275  607 GLU A CG  
4771 C CD  . GLU A 607 ? 1.0610 0.4518 0.9048 -0.0288 0.2869  0.1313  607 GLU A CD  
4772 O OE1 . GLU A 607 ? 1.0705 0.4669 0.8973 -0.0261 0.2911  0.1250  607 GLU A OE1 
4773 O OE2 . GLU A 607 ? 1.3231 0.7065 1.1786 -0.0247 0.2836  0.1408  607 GLU A OE2 
4774 N N   . ILE A 608 ? 0.9647 0.3655 0.8041 -0.0504 0.2874  0.0909  608 ILE A N   
4775 C CA  . ILE A 608 ? 0.9761 0.3744 0.8086 -0.0511 0.2857  0.0789  608 ILE A CA  
4776 C C   . ILE A 608 ? 0.9518 0.3407 0.7973 -0.0593 0.2794  0.0752  608 ILE A C   
4777 O O   . ILE A 608 ? 1.0113 0.3882 0.8493 -0.0598 0.2746  0.0638  608 ILE A O   
4778 C CB  . ILE A 608 ? 0.9524 0.3639 0.7792 -0.0502 0.2931  0.0813  608 ILE A CB  
4779 C CG1 . ILE A 608 ? 0.9033 0.3200 0.7159 -0.0433 0.2991  0.0818  608 ILE A CG1 
4780 C CG2 . ILE A 608 ? 0.9281 0.3359 0.7513 -0.0505 0.2906  0.0722  608 ILE A CG2 
4781 C CD1 . ILE A 608 ? 0.8996 0.3085 0.7019 -0.0373 0.2960  0.0711  608 ILE A CD1 
4782 N N   . GLU A 609 ? 0.9361 0.3292 0.8008 -0.0665 0.2800  0.0852  609 GLU A N   
4783 C CA  . GLU A 609 ? 1.0139 0.3968 0.8955 -0.0760 0.2738  0.0812  609 GLU A CA  
4784 C C   . GLU A 609 ? 1.0067 0.3700 0.8896 -0.0765 0.2665  0.0714  609 GLU A C   
4785 O O   . GLU A 609 ? 0.9954 0.3439 0.8813 -0.0829 0.2603  0.0602  609 GLU A O   
4786 C CB  . GLU A 609 ? 1.0080 0.4012 0.9141 -0.0841 0.2774  0.0952  609 GLU A CB  
4787 C CG  . GLU A 609 ? 1.0393 0.4219 0.9692 -0.0958 0.2707  0.0913  609 GLU A CG  
4788 C CD  . GLU A 609 ? 1.1836 0.5783 1.1414 -0.1042 0.2755  0.1067  609 GLU A CD  
4789 O OE1 . GLU A 609 ? 1.1948 0.6070 1.1493 -0.1007 0.2853  0.1202  609 GLU A OE1 
4790 O OE2 . GLU A 609 ? 1.2168 0.6031 1.1995 -0.1147 0.2700  0.1047  609 GLU A OE2 
4791 N N   . ARG A 610 ? 0.9686 0.3301 0.8496 -0.0700 0.2677  0.0748  610 ARG A N   
4792 C CA  . ARG A 610 ? 0.9798 0.3228 0.8645 -0.0691 0.2627  0.0648  610 ARG A CA  
4793 C C   . ARG A 610 ? 1.0043 0.3369 0.8662 -0.0642 0.2619  0.0478  610 ARG A C   
4794 O O   . ARG A 610 ? 0.9989 0.3132 0.8597 -0.0676 0.2576  0.0336  610 ARG A O   
4795 C CB  . ARG A 610 ? 1.0645 0.4089 0.9567 -0.0626 0.2648  0.0754  610 ARG A CB  
4796 C CG  . ARG A 610 ? 1.0129 0.3385 0.9165 -0.0614 0.2607  0.0670  610 ARG A CG  
4797 C CD  . ARG A 610 ? 1.0052 0.3323 0.9219 -0.0557 0.2621  0.0823  610 ARG A CD  
4798 N NE  . ARG A 610 ? 0.9963 0.3345 0.8968 -0.0458 0.2668  0.0879  610 ARG A NE  
4799 C CZ  . ARG A 610 ? 1.0659 0.4068 0.9727 -0.0396 0.2682  0.1026  610 ARG A CZ  
4800 N NH1 . ARG A 610 ? 1.1957 0.5295 1.1244 -0.0414 0.2655  0.1149  610 ARG A NH1 
4801 N NH2 . ARG A 610 ? 0.9859 0.3357 0.8774 -0.0318 0.2720  0.1058  610 ARG A NH2 
4802 N N   . GLU A 611 ? 1.0476 0.3908 0.8910 -0.0566 0.2667  0.0487  611 GLU A N   
4803 C CA  . GLU A 611 ? 0.9672 0.3022 0.7886 -0.0525 0.2676  0.0353  611 GLU A CA  
4804 C C   . GLU A 611 ? 0.9783 0.3029 0.7912 -0.0596 0.2634  0.0273  611 GLU A C   
4805 O O   . GLU A 611 ? 1.0580 0.3638 0.8565 -0.0608 0.2614  0.0133  611 GLU A O   
4806 C CB  . GLU A 611 ? 0.9484 0.2980 0.7566 -0.0446 0.2736  0.0394  611 GLU A CB  
4807 C CG  . GLU A 611 ? 0.9419 0.2982 0.7556 -0.0377 0.2772  0.0457  611 GLU A CG  
4808 C CD  . GLU A 611 ? 1.0330 0.3756 0.8490 -0.0338 0.2772  0.0372  611 GLU A CD  
4809 O OE1 . GLU A 611 ? 0.9816 0.3107 0.7870 -0.0349 0.2768  0.0238  611 GLU A OE1 
4810 O OE2 . GLU A 611 ? 1.0773 0.4214 0.9053 -0.0293 0.2781  0.0440  611 GLU A OE2 
4811 N N   . LEU A 612 ? 0.9700 0.3052 0.7910 -0.0645 0.2627  0.0358  612 LEU A N   
4812 C CA  . LEU A 612 ? 0.9810 0.3184 0.8018 -0.0708 0.2536  0.0295  612 LEU A CA  
4813 C C   . LEU A 612 ? 1.0716 0.3935 0.9019 -0.0793 0.2452  0.0183  612 LEU A C   
4814 O O   . LEU A 612 ? 1.0653 0.3830 0.8820 -0.0813 0.2362  0.0046  612 LEU A O   
4815 C CB  . LEU A 612 ? 0.9634 0.3224 0.8023 -0.0743 0.2534  0.0411  612 LEU A CB  
4816 C CG  . LEU A 612 ? 0.9902 0.3598 0.8385 -0.0806 0.2414  0.0368  612 LEU A CG  
4817 C CD1 . LEU A 612 ? 1.0282 0.3975 0.8512 -0.0756 0.2346  0.0277  612 LEU A CD1 
4818 C CD2 . LEU A 612 ? 1.0721 0.4648 0.9415 -0.0821 0.2443  0.0487  612 LEU A CD2 
4819 N N   . ARG A 613 ? 1.0071 0.3200 0.8604 -0.0845 0.2479  0.0240  613 ARG A N   
4820 C CA  . ARG A 613 ? 1.0318 0.3268 0.8988 -0.0931 0.2408  0.0123  613 ARG A CA  
4821 C C   . ARG A 613 ? 1.0504 0.3247 0.8971 -0.0883 0.2412  -0.0054 613 ARG A C   
4822 O O   . ARG A 613 ? 1.0724 0.3383 0.9121 -0.0935 0.2320  -0.0233 613 ARG A O   
4823 C CB  . ARG A 613 ? 1.0636 0.3587 0.9622 -0.0973 0.2435  0.0245  613 ARG A CB  
4824 C CG  . ARG A 613 ? 1.0511 0.3625 0.9734 -0.1054 0.2445  0.0398  613 ARG A CG  
4825 C CD  . ARG A 613 ? 1.0978 0.4100 1.0520 -0.1109 0.2440  0.0498  613 ARG A CD  
4826 N NE  . ARG A 613 ? 1.0825 0.4131 1.0592 -0.1178 0.2479  0.0666  613 ARG A NE  
4827 C CZ  . ARG A 613 ? 1.1846 0.5171 1.1925 -0.1260 0.2477  0.0768  613 ARG A CZ  
4828 N NH1 . ARG A 613 ? 1.0757 0.3911 1.0979 -0.1283 0.2426  0.0718  613 ARG A NH1 
4829 N NH2 . ARG A 613 ? 1.1917 0.5434 1.2179 -0.1317 0.2538  0.0925  613 ARG A NH2 
4830 N N   . ALA A 614 ? 1.0408 0.3162 0.8797 -0.0776 0.2493  -0.0013 614 ALA A N   
4831 C CA  . ALA A 614 ? 1.1074 0.3672 0.9315 -0.0719 0.2517  -0.0174 614 ALA A CA  
4832 C C   . ALA A 614 ? 1.0858 0.3399 0.8756 -0.0709 0.2508  -0.0314 614 ALA A C   
4833 O O   . ALA A 614 ? 1.1679 0.4086 0.9450 -0.0727 0.2474  -0.0507 614 ALA A O   
4834 C CB  . ALA A 614 ? 1.0402 0.3127 0.8672 -0.0599 0.2588  -0.0084 614 ALA A CB  
4835 N N   . LEU A 615 ? 1.0567 0.3303 0.8328 -0.0669 0.2513  -0.0217 615 LEU A N   
4836 C CA  . LEU A 615 ? 1.0898 0.3693 0.8359 -0.0645 0.2476  -0.0305 615 LEU A CA  
4837 C C   . LEU A 615 ? 1.1668 0.4485 0.9098 -0.0736 0.2323  -0.0415 615 LEU A C   
4838 O O   . LEU A 615 ? 1.1748 0.4505 0.8924 -0.0738 0.2279  -0.0571 615 LEU A O   
4839 C CB  . LEU A 615 ? 1.1175 0.4162 0.8564 -0.0589 0.2509  -0.0160 615 LEU A CB  
4840 C CG  . LEU A 615 ? 1.0794 0.3861 0.7909 -0.0566 0.2461  -0.0194 615 LEU A CG  
4841 C CD1 . LEU A 615 ? 1.1273 0.4207 0.8113 -0.0521 0.2523  -0.0327 615 LEU A CD1 
4842 C CD2 . LEU A 615 ? 1.0170 0.3395 0.7285 -0.0509 0.2510  -0.0045 615 LEU A CD2 
4843 N N   . LYS A 616 ? 1.1569 0.4489 0.9254 -0.0816 0.2240  -0.0339 616 LYS A N   
4844 C CA  . LYS A 616 ? 1.1493 0.4455 0.9209 -0.0914 0.2076  -0.0449 616 LYS A CA  
4845 C C   . LYS A 616 ? 1.1780 0.4520 0.9468 -0.0969 0.2041  -0.0669 616 LYS A C   
4846 O O   . LYS A 616 ? 1.1927 0.4668 0.9440 -0.1017 0.1918  -0.0835 616 LYS A O   
4847 C CB  . LYS A 616 ? 1.1494 0.4598 0.9572 -0.0997 0.2020  -0.0330 616 LYS A CB  
4848 C CG  . LYS A 616 ? 1.2361 0.5527 1.0551 -0.1112 0.1838  -0.0444 616 LYS A CG  
4849 C CD  . LYS A 616 ? 1.4306 0.7612 1.2915 -0.1200 0.1810  -0.0320 616 LYS A CD  
4850 C CE  . LYS A 616 ? 1.6089 0.9437 1.4883 -0.1334 0.1627  -0.0456 616 LYS A CE  
4851 N NZ  . LYS A 616 ? 1.4902 0.8356 1.4163 -0.1435 0.1626  -0.0342 616 LYS A NZ  
4852 N N   . GLN A 617 ? 1.2027 0.4576 0.9884 -0.0959 0.2146  -0.0675 617 GLN A N   
4853 C CA  . GLN A 617 ? 1.1826 0.4134 0.9710 -0.1005 0.2132  -0.0893 617 GLN A CA  
4854 C C   . GLN A 617 ? 1.2121 0.4339 0.9620 -0.0931 0.2179  -0.1071 617 GLN A C   
4855 O O   . GLN A 617 ? 1.2146 0.4292 0.9479 -0.0983 0.2093  -0.1297 617 GLN A O   
4856 C CB  . GLN A 617 ? 1.1530 0.3656 0.9731 -0.0996 0.2240  -0.0818 617 GLN A CB  
4857 C CG  . GLN A 617 ? 1.2362 0.4215 1.0706 -0.1055 0.2225  -0.1033 617 GLN A CG  
4858 C CD  . GLN A 617 ? 1.2044 0.3900 1.0626 -0.1211 0.2077  -0.1117 617 GLN A CD  
4859 O OE1 . GLN A 617 ? 1.3685 0.5745 1.2414 -0.1272 0.2007  -0.0968 617 GLN A OE1 
4860 N NE2 . GLN A 617 ? 1.2433 0.4069 1.1076 -0.1278 0.2031  -0.1370 617 GLN A NE2 
4861 N N   . ARG A 618 ? 1.1698 0.3932 0.9049 -0.0813 0.2319  -0.0978 618 ARG A N   
4862 C CA  . ARG A 618 ? 1.1827 0.3987 0.8833 -0.0740 0.2395  -0.1129 618 ARG A CA  
4863 C C   . ARG A 618 ? 1.2007 0.4303 0.8651 -0.0763 0.2287  -0.1205 618 ARG A C   
4864 O O   . ARG A 618 ? 1.3219 0.5438 0.9559 -0.0749 0.2303  -0.1398 618 ARG A O   
4865 C CB  . ARG A 618 ? 1.1588 0.3784 0.8550 -0.0620 0.2557  -0.0989 618 ARG A CB  
4866 C CG  . ARG A 618 ? 1.1456 0.3533 0.8743 -0.0580 0.2655  -0.0908 618 ARG A CG  
4867 C CD  . ARG A 618 ? 1.1279 0.3401 0.8510 -0.0463 0.2800  -0.0814 618 ARG A CD  
4868 N NE  . ARG A 618 ? 1.1220 0.3559 0.8337 -0.0440 0.2796  -0.0649 618 ARG A NE  
4869 C CZ  . ARG A 618 ? 1.2058 0.4520 0.9360 -0.0435 0.2793  -0.0456 618 ARG A CZ  
4870 N NH1 . ARG A 618 ? 1.1603 0.4159 0.9225 -0.0442 0.2753  -0.0364 618 ARG A NH1 
4871 N NH2 . ARG A 618 ? 1.0994 0.3635 0.8188 -0.0414 0.2795  -0.0343 618 ARG A NH2 
4872 N N   . ILE A 619 ? 1.2022 0.4526 0.8693 -0.0793 0.2179  -0.1053 619 ILE A N   
4873 C CA  . ILE A 619 ? 1.2912 0.5562 0.9261 -0.0806 0.2057  -0.1089 619 ILE A CA  
4874 C C   . ILE A 619 ? 1.2937 0.5558 0.9264 -0.0920 0.1879  -0.1299 619 ILE A C   
4875 O O   . ILE A 619 ? 1.3306 0.5954 0.9268 -0.0928 0.1802  -0.1442 619 ILE A O   
4876 C CB  . ILE A 619 ? 1.2255 0.5136 0.8684 -0.0787 0.2004  -0.0853 619 ILE A CB  
4877 C CG1 . ILE A 619 ? 1.1770 0.4678 0.8149 -0.0677 0.2175  -0.0689 619 ILE A CG1 
4878 C CG2 . ILE A 619 ? 1.2537 0.5577 0.8704 -0.0809 0.1839  -0.0870 619 ILE A CG2 
4879 C CD1 . ILE A 619 ? 1.2042 0.5153 0.8502 -0.0649 0.2143  -0.0479 619 ILE A CD1 
4880 N N   . SER A 620 ? 1.2646 0.5220 0.9361 -0.1014 0.1809  -0.1321 620 SER A N   
4881 C CA  . SER A 620 ? 1.3092 0.5637 0.9848 -0.1138 0.1632  -0.1537 620 SER A CA  
4882 C C   . SER A 620 ? 1.3327 0.5629 0.9899 -0.1148 0.1680  -0.1830 620 SER A C   
4883 O O   . SER A 620 ? 1.3408 0.5690 0.9877 -0.1241 0.1530  -0.2063 620 SER A O   
4884 C CB  . SER A 620 ? 1.2654 0.5201 0.9925 -0.1244 0.1568  -0.1472 620 SER A CB  
4885 O OG  . SER A 620 ? 1.3360 0.5699 1.0898 -0.1223 0.1728  -0.1432 620 SER A OG  
4886 N N   . GLN A 621 ? 1.3321 0.5447 0.9863 -0.1053 0.1883  -0.1835 621 GLN A N   
4887 C CA  . GLN A 621 ? 1.3729 0.5623 1.0116 -0.1042 0.1963  -0.2115 621 GLN A CA  
4888 C C   . GLN A 621 ? 1.4557 0.6507 1.0392 -0.0973 0.2005  -0.2228 621 GLN A C   
4889 O O   . GLN A 621 ? 1.5150 0.6929 1.0802 -0.0953 0.2093  -0.2477 621 GLN A O   
4890 C CB  . GLN A 621 ? 1.4088 0.5778 1.0751 -0.0964 0.2164  -0.2062 621 GLN A CB  
4891 C CG  . GLN A 621 ? 1.3601 0.5206 1.0791 -0.1029 0.2140  -0.1946 621 GLN A CG  
4892 C CD  . GLN A 621 ? 1.4981 0.6447 1.2374 -0.1170 0.2005  -0.2174 621 GLN A CD  
4893 O OE1 . GLN A 621 ? 1.5248 0.6544 1.2490 -0.1190 0.2006  -0.2472 621 GLN A OE1 
4894 N NE2 . GLN A 621 ? 1.5220 0.6763 1.2971 -0.1274 0.1895  -0.2045 621 GLN A NE2 
4895 N N   . MET A 622 ? 1.4413 0.6595 0.9990 -0.0935 0.1956  -0.2049 622 MET A N   
4896 C CA  . MET A 622 ? 1.5024 0.7276 1.0064 -0.0875 0.1996  -0.2113 622 MET A CA  
4897 C C   . MET A 622 ? 1.5540 0.7816 1.0267 -0.0965 0.1815  -0.2378 622 MET A C   
4898 O O   . MET A 622 ? 1.5374 0.7715 1.0292 -0.1076 0.1606  -0.2429 622 MET A O   
4899 C CB  . MET A 622 ? 1.4442 0.6923 0.9344 -0.0812 0.1986  -0.1820 622 MET A CB  
4900 C CG  . MET A 622 ? 1.3235 0.5709 0.8390 -0.0723 0.2164  -0.1583 622 MET A CG  
4901 S SD  . MET A 622 ? 1.3738 0.6448 0.8739 -0.0652 0.2165  -0.1276 622 MET A SD  
4902 C CE  . MET A 622 ? 1.4277 0.7000 0.8662 -0.0600 0.2230  -0.1373 622 MET A CE  
4903 O OXT . MET A 622 ? 1.6838 0.9083 1.1113 -0.0933 0.1874  -0.2551 622 MET A OXT 
# 
