data_9LXL
# 
_entry.id   9LXL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9LXL         pdb_00009lxl 10.2210/pdb9lxl/pdb 
WWPDB D_1300056610 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9LXL 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kulminskaya_aa@pnpi.nrcki.ru 
_pdbx_contact_author.name_first         Anna 
_pdbx_contact_author.name_last          Kulminskaya 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3481-0007 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Korban, S.A.'        1 0000-0002-9475-7252 
'Borshchevskiy, V.I.' 2 0000-0003-4398-9712 
'Pospelov, V.A.'      3 ?                   
'Bobrov, K.S.'        4 0000-0003-2348-1014 
'Ivanova, D.N.'       5 ?                   
'Kulminskaya, A.A.'   6 0000-0002-3481-0007 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of GH29 family alpha-L-fucosidase from Fusarium proliferatum LE1' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Korban, S.A.'        1 0000-0002-9475-7252 
primary 'Borshchevskiy, V.I.' 2 0000-0003-4398-9712 
primary 'Pospelov, V.A.'      3 ?                   
primary 'Bobrov, K.S.'        4 0000-0003-2348-1014 
primary 'Ivanova, D.N.'       5 ?                   
primary 'Kulminskaya, A.A.'   6 0000-0002-3481-0007 
# 
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 alpha-L-fucosidase                       69097.578 1   3.2.1.51 ? ? ? 
2 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   3   ?        ? ? ? 
3 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 122.143   1   ?        ? ? ? 
4 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'          118.174   2   ?        ? ? ? 
5 non-polymer syn 'SODIUM ION'                             22.990    1   ?        ? ? ? 
6 non-polymer syn 'AZIDE ION'                              42.020    5   ?        ? ? ? 
7 non-polymer syn 'ACETATE ION'                            59.044    2   ?        ? ? ? 
8 water       nat water                                    18.015    234 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Alpha-L-fucosidase GH29' 
# 
_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       
;ETQASGPYEATWESTDKHIASPEWFRDAKFGVYWHWGAFTTPQYASEWYPRNMYEPGSDQRKHHTETYGPPEEWGYANFI
NGADDLKGNFVQFKPVLSSKGGEFDPEAIIKAVKASGAKFAGPVGEHHDGYSMWDSKVNEWNSVKRGPKLDLVKLWADLV
RKNGMKLVVAMHQAYNYNGFYEWAPKTNDTSLKKLLGQLSREESDQLWFDKHREMLDHVQPDIIWNDFSLDSPGYCADFD
GPCAVAEKKRLEFLAYYFNRAVEWNKEVVTTHKHFDVGFRDTSTVSDYERGGPANITRPYWLTDDAISASSWSYTVGIQY
YSSKAMVHSLLDRISKNGNMLLNISPTAVGVLPDEQLKVLQDIGDFLGRYGESVFSTRAWDIYGEGPNQVTGGSFTAPLQ
GNSSDIRFTRNKDANVLYATVLGWPDDKHVSIASLGSDALVDLKSLKSIELLGDKAGEYEQVSDWKQTKDALEISLPAKP
AESLAYVLKLTFDGGIPVPQPKIGASVFSATSATGRGVSLGLGDFSEEFLTEAGLKPDTIRFIRVSSGTKLTVYSTGDLS
GDSKELDAGEHKVEEGSVGSITISKAENLYFQSAAASFLEQKLISEEDLNSAVDHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ETQASGPYEATWESTDKHIASPEWFRDAKFGVYWHWGAFTTPQYASEWYPRNMYEPGSDQRKHHTETYGPPEEWGYANFI
NGADDLKGNFVQFKPVLSSKGGEFDPEAIIKAVKASGAKFAGPVGEHHDGYSMWDSKVNEWNSVKRGPKLDLVKLWADLV
RKNGMKLVVAMHQAYNYNGFYEWAPKTNDTSLKKLLGQLSREESDQLWFDKHREMLDHVQPDIIWNDFSLDSPGYCADFD
GPCAVAEKKRLEFLAYYFNRAVEWNKEVVTTHKHFDVGFRDTSTVSDYERGGPANITRPYWLTDDAISASSWSYTVGIQY
YSSKAMVHSLLDRISKNGNMLLNISPTAVGVLPDEQLKVLQDIGDFLGRYGESVFSTRAWDIYGEGPNQVTGGSFTAPLQ
GNSSDIRFTRNKDANVLYATVLGWPDDKHVSIASLGSDALVDLKSLKSIELLGDKAGEYEQVSDWKQTKDALEISLPAKP
AESLAYVLKLTFDGGIPVPQPKIGASVFSATSATGRGVSLGLGDFSEEFLTEAGLKPDTIRFIRVSSGTKLTVYSTGDLS
GDSKELDAGEHKVEEGSVGSITISKAENLYFQSAAASFLEQKLISEEDLNSAVDHHHHHH
;
_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 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
3 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL TRS 
4 '(4S)-2-METHYL-2,4-PENTANEDIOL'          MPD 
5 'SODIUM ION'                             NA  
6 'AZIDE ION'                              AZI 
7 'ACETATE ION'                            ACT 
8 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   THR n 
1 3   GLN n 
1 4   ALA n 
1 5   SER n 
1 6   GLY n 
1 7   PRO n 
1 8   TYR n 
1 9   GLU n 
1 10  ALA n 
1 11  THR n 
1 12  TRP n 
1 13  GLU n 
1 14  SER n 
1 15  THR n 
1 16  ASP n 
1 17  LYS n 
1 18  HIS n 
1 19  ILE n 
1 20  ALA n 
1 21  SER n 
1 22  PRO n 
1 23  GLU n 
1 24  TRP n 
1 25  PHE n 
1 26  ARG n 
1 27  ASP n 
1 28  ALA n 
1 29  LYS n 
1 30  PHE n 
1 31  GLY n 
1 32  VAL n 
1 33  TYR n 
1 34  TRP n 
1 35  HIS n 
1 36  TRP n 
1 37  GLY n 
1 38  ALA n 
1 39  PHE n 
1 40  THR n 
1 41  THR n 
1 42  PRO n 
1 43  GLN n 
1 44  TYR n 
1 45  ALA n 
1 46  SER n 
1 47  GLU n 
1 48  TRP n 
1 49  TYR n 
1 50  PRO n 
1 51  ARG n 
1 52  ASN n 
1 53  MET n 
1 54  TYR n 
1 55  GLU n 
1 56  PRO n 
1 57  GLY n 
1 58  SER n 
1 59  ASP n 
1 60  GLN n 
1 61  ARG n 
1 62  LYS n 
1 63  HIS n 
1 64  HIS n 
1 65  THR n 
1 66  GLU n 
1 67  THR n 
1 68  TYR n 
1 69  GLY n 
1 70  PRO n 
1 71  PRO n 
1 72  GLU n 
1 73  GLU n 
1 74  TRP n 
1 75  GLY n 
1 76  TYR n 
1 77  ALA n 
1 78  ASN n 
1 79  PHE n 
1 80  ILE n 
1 81  ASN n 
1 82  GLY n 
1 83  ALA n 
1 84  ASP n 
1 85  ASP n 
1 86  LEU n 
1 87  LYS n 
1 88  GLY n 
1 89  ASN n 
1 90  PHE n 
1 91  VAL n 
1 92  GLN n 
1 93  PHE n 
1 94  LYS n 
1 95  PRO n 
1 96  VAL n 
1 97  LEU n 
1 98  SER n 
1 99  SER n 
1 100 LYS n 
1 101 GLY n 
1 102 GLY n 
1 103 GLU n 
1 104 PHE n 
1 105 ASP n 
1 106 PRO n 
1 107 GLU n 
1 108 ALA n 
1 109 ILE n 
1 110 ILE n 
1 111 LYS n 
1 112 ALA n 
1 113 VAL n 
1 114 LYS n 
1 115 ALA n 
1 116 SER n 
1 117 GLY n 
1 118 ALA n 
1 119 LYS n 
1 120 PHE n 
1 121 ALA n 
1 122 GLY n 
1 123 PRO n 
1 124 VAL n 
1 125 GLY n 
1 126 GLU n 
1 127 HIS n 
1 128 HIS n 
1 129 ASP n 
1 130 GLY n 
1 131 TYR n 
1 132 SER n 
1 133 MET n 
1 134 TRP n 
1 135 ASP n 
1 136 SER n 
1 137 LYS n 
1 138 VAL n 
1 139 ASN n 
1 140 GLU n 
1 141 TRP n 
1 142 ASN n 
1 143 SER n 
1 144 VAL n 
1 145 LYS n 
1 146 ARG n 
1 147 GLY n 
1 148 PRO n 
1 149 LYS n 
1 150 LEU n 
1 151 ASP n 
1 152 LEU n 
1 153 VAL n 
1 154 LYS n 
1 155 LEU n 
1 156 TRP n 
1 157 ALA n 
1 158 ASP n 
1 159 LEU n 
1 160 VAL n 
1 161 ARG n 
1 162 LYS n 
1 163 ASN n 
1 164 GLY n 
1 165 MET n 
1 166 LYS n 
1 167 LEU n 
1 168 VAL n 
1 169 VAL n 
1 170 ALA n 
1 171 MET n 
1 172 HIS n 
1 173 GLN n 
1 174 ALA n 
1 175 TYR n 
1 176 ASN n 
1 177 TYR n 
1 178 ASN n 
1 179 GLY n 
1 180 PHE n 
1 181 TYR n 
1 182 GLU n 
1 183 TRP n 
1 184 ALA n 
1 185 PRO n 
1 186 LYS n 
1 187 THR n 
1 188 ASN n 
1 189 ASP n 
1 190 THR n 
1 191 SER n 
1 192 LEU n 
1 193 LYS n 
1 194 LYS n 
1 195 LEU n 
1 196 LEU n 
1 197 GLY n 
1 198 GLN n 
1 199 LEU n 
1 200 SER n 
1 201 ARG n 
1 202 GLU n 
1 203 GLU n 
1 204 SER n 
1 205 ASP n 
1 206 GLN n 
1 207 LEU n 
1 208 TRP n 
1 209 PHE n 
1 210 ASP n 
1 211 LYS n 
1 212 HIS n 
1 213 ARG n 
1 214 GLU n 
1 215 MET n 
1 216 LEU n 
1 217 ASP n 
1 218 HIS n 
1 219 VAL n 
1 220 GLN n 
1 221 PRO n 
1 222 ASP n 
1 223 ILE n 
1 224 ILE n 
1 225 TRP n 
1 226 ASN n 
1 227 ASP n 
1 228 PHE n 
1 229 SER n 
1 230 LEU n 
1 231 ASP n 
1 232 SER n 
1 233 PRO n 
1 234 GLY n 
1 235 TYR n 
1 236 CYS n 
1 237 ALA n 
1 238 ASP n 
1 239 PHE n 
1 240 ASP n 
1 241 GLY n 
1 242 PRO n 
1 243 CYS n 
1 244 ALA n 
1 245 VAL n 
1 246 ALA n 
1 247 GLU n 
1 248 LYS n 
1 249 LYS n 
1 250 ARG n 
1 251 LEU n 
1 252 GLU n 
1 253 PHE n 
1 254 LEU n 
1 255 ALA n 
1 256 TYR n 
1 257 TYR n 
1 258 PHE n 
1 259 ASN n 
1 260 ARG n 
1 261 ALA n 
1 262 VAL n 
1 263 GLU n 
1 264 TRP n 
1 265 ASN n 
1 266 LYS n 
1 267 GLU n 
1 268 VAL n 
1 269 VAL n 
1 270 THR n 
1 271 THR n 
1 272 HIS n 
1 273 LYS n 
1 274 HIS n 
1 275 PHE n 
1 276 ASP n 
1 277 VAL n 
1 278 GLY n 
1 279 PHE n 
1 280 ARG n 
1 281 ASP n 
1 282 THR n 
1 283 SER n 
1 284 THR n 
1 285 VAL n 
1 286 SER n 
1 287 ASP n 
1 288 TYR n 
1 289 GLU n 
1 290 ARG n 
1 291 GLY n 
1 292 GLY n 
1 293 PRO n 
1 294 ALA n 
1 295 ASN n 
1 296 ILE n 
1 297 THR n 
1 298 ARG n 
1 299 PRO n 
1 300 TYR n 
1 301 TRP n 
1 302 LEU n 
1 303 THR n 
1 304 ASP n 
1 305 ASP n 
1 306 ALA n 
1 307 ILE n 
1 308 SER n 
1 309 ALA n 
1 310 SER n 
1 311 SER n 
1 312 TRP n 
1 313 SER n 
1 314 TYR n 
1 315 THR n 
1 316 VAL n 
1 317 GLY n 
1 318 ILE n 
1 319 GLN n 
1 320 TYR n 
1 321 TYR n 
1 322 SER n 
1 323 SER n 
1 324 LYS n 
1 325 ALA n 
1 326 MET n 
1 327 VAL n 
1 328 HIS n 
1 329 SER n 
1 330 LEU n 
1 331 LEU n 
1 332 ASP n 
1 333 ARG n 
1 334 ILE n 
1 335 SER n 
1 336 LYS n 
1 337 ASN n 
1 338 GLY n 
1 339 ASN n 
1 340 MET n 
1 341 LEU n 
1 342 LEU n 
1 343 ASN n 
1 344 ILE n 
1 345 SER n 
1 346 PRO n 
1 347 THR n 
1 348 ALA n 
1 349 VAL n 
1 350 GLY n 
1 351 VAL n 
1 352 LEU n 
1 353 PRO n 
1 354 ASP n 
1 355 GLU n 
1 356 GLN n 
1 357 LEU n 
1 358 LYS n 
1 359 VAL n 
1 360 LEU n 
1 361 GLN n 
1 362 ASP n 
1 363 ILE n 
1 364 GLY n 
1 365 ASP n 
1 366 PHE n 
1 367 LEU n 
1 368 GLY n 
1 369 ARG n 
1 370 TYR n 
1 371 GLY n 
1 372 GLU n 
1 373 SER n 
1 374 VAL n 
1 375 PHE n 
1 376 SER n 
1 377 THR n 
1 378 ARG n 
1 379 ALA n 
1 380 TRP n 
1 381 ASP n 
1 382 ILE n 
1 383 TYR n 
1 384 GLY n 
1 385 GLU n 
1 386 GLY n 
1 387 PRO n 
1 388 ASN n 
1 389 GLN n 
1 390 VAL n 
1 391 THR n 
1 392 GLY n 
1 393 GLY n 
1 394 SER n 
1 395 PHE n 
1 396 THR n 
1 397 ALA n 
1 398 PRO n 
1 399 LEU n 
1 400 GLN n 
1 401 GLY n 
1 402 ASN n 
1 403 SER n 
1 404 SER n 
1 405 ASP n 
1 406 ILE n 
1 407 ARG n 
1 408 PHE n 
1 409 THR n 
1 410 ARG n 
1 411 ASN n 
1 412 LYS n 
1 413 ASP n 
1 414 ALA n 
1 415 ASN n 
1 416 VAL n 
1 417 LEU n 
1 418 TYR n 
1 419 ALA n 
1 420 THR n 
1 421 VAL n 
1 422 LEU n 
1 423 GLY n 
1 424 TRP n 
1 425 PRO n 
1 426 ASP n 
1 427 ASP n 
1 428 LYS n 
1 429 HIS n 
1 430 VAL n 
1 431 SER n 
1 432 ILE n 
1 433 ALA n 
1 434 SER n 
1 435 LEU n 
1 436 GLY n 
1 437 SER n 
1 438 ASP n 
1 439 ALA n 
1 440 LEU n 
1 441 VAL n 
1 442 ASP n 
1 443 LEU n 
1 444 LYS n 
1 445 SER n 
1 446 LEU n 
1 447 LYS n 
1 448 SER n 
1 449 ILE n 
1 450 GLU n 
1 451 LEU n 
1 452 LEU n 
1 453 GLY n 
1 454 ASP n 
1 455 LYS n 
1 456 ALA n 
1 457 GLY n 
1 458 GLU n 
1 459 TYR n 
1 460 GLU n 
1 461 GLN n 
1 462 VAL n 
1 463 SER n 
1 464 ASP n 
1 465 TRP n 
1 466 LYS n 
1 467 GLN n 
1 468 THR n 
1 469 LYS n 
1 470 ASP n 
1 471 ALA n 
1 472 LEU n 
1 473 GLU n 
1 474 ILE n 
1 475 SER n 
1 476 LEU n 
1 477 PRO n 
1 478 ALA n 
1 479 LYS n 
1 480 PRO n 
1 481 ALA n 
1 482 GLU n 
1 483 SER n 
1 484 LEU n 
1 485 ALA n 
1 486 TYR n 
1 487 VAL n 
1 488 LEU n 
1 489 LYS n 
1 490 LEU n 
1 491 THR n 
1 492 PHE n 
1 493 ASP n 
1 494 GLY n 
1 495 GLY n 
1 496 ILE n 
1 497 PRO n 
1 498 VAL n 
1 499 PRO n 
1 500 GLN n 
1 501 PRO n 
1 502 LYS n 
1 503 ILE n 
1 504 GLY n 
1 505 ALA n 
1 506 SER n 
1 507 VAL n 
1 508 PHE n 
1 509 SER n 
1 510 ALA n 
1 511 THR n 
1 512 SER n 
1 513 ALA n 
1 514 THR n 
1 515 GLY n 
1 516 ARG n 
1 517 GLY n 
1 518 VAL n 
1 519 SER n 
1 520 LEU n 
1 521 GLY n 
1 522 LEU n 
1 523 GLY n 
1 524 ASP n 
1 525 PHE n 
1 526 SER n 
1 527 GLU n 
1 528 GLU n 
1 529 PHE n 
1 530 LEU n 
1 531 THR n 
1 532 GLU n 
1 533 ALA n 
1 534 GLY n 
1 535 LEU n 
1 536 LYS n 
1 537 PRO n 
1 538 ASP n 
1 539 THR n 
1 540 ILE n 
1 541 ARG n 
1 542 PHE n 
1 543 ILE n 
1 544 ARG n 
1 545 VAL n 
1 546 SER n 
1 547 SER n 
1 548 GLY n 
1 549 THR n 
1 550 LYS n 
1 551 LEU n 
1 552 THR n 
1 553 VAL n 
1 554 TYR n 
1 555 SER n 
1 556 THR n 
1 557 GLY n 
1 558 ASP n 
1 559 LEU n 
1 560 SER n 
1 561 GLY n 
1 562 ASP n 
1 563 SER n 
1 564 LYS n 
1 565 GLU n 
1 566 LEU n 
1 567 ASP n 
1 568 ALA n 
1 569 GLY n 
1 570 GLU n 
1 571 HIS n 
1 572 LYS n 
1 573 VAL n 
1 574 GLU n 
1 575 GLU n 
1 576 GLY n 
1 577 SER n 
1 578 VAL n 
1 579 GLY n 
1 580 SER n 
1 581 ILE n 
1 582 THR n 
1 583 ILE n 
1 584 SER n 
1 585 LYS n 
1 586 ALA n 
1 587 GLU n 
1 588 ASN n 
1 589 LEU n 
1 590 TYR n 
1 591 PHE n 
1 592 GLN n 
1 593 SER n 
1 594 ALA n 
1 595 ALA n 
1 596 ALA n 
1 597 SER n 
1 598 PHE n 
1 599 LEU n 
1 600 GLU n 
1 601 GLN n 
1 602 LYS n 
1 603 LEU n 
1 604 ILE n 
1 605 SER n 
1 606 GLU n 
1 607 GLU n 
1 608 ASP n 
1 609 LEU n 
1 610 ASN n 
1 611 SER n 
1 612 ALA n 
1 613 VAL n 
1 614 ASP n 
1 615 HIS n 
1 616 HIS n 
1 617 HIS n 
1 618 HIS n 
1 619 HIS n 
1 620 HIS 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                   620 
_entity_src_gen.gene_src_common_name               'Bulb rot disease fungus, Fusarium proliferatum' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FPRO05_08134 
_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      'Gibberella intermedia' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     948311 
_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      'Komagataella pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_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 
ACT non-polymer                  . 'ACETATE ION'                            ? 'C2 H3 O2 -1'    59.044  
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 
AZI non-polymer                  . 'AZIDE ION'                              ? 'N3 -1'          42.020  
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
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 
MPD non-polymer                  . '(4S)-2-METHYL-2,4-PENTANEDIOL'          ? 'C6 H14 O2'      118.174 
NA  non-polymer                  . 'SODIUM ION'                             ? 'Na 1'           22.990  
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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 
TRS non-polymer                  . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 'TRIS BUFFER' 'C4 H12 N O3 1'  122.143 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   GLU 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   TYR 8   8   8   TYR TYR A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  TRP 12  12  12  TRP TRP A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  TRP 24  24  24  TRP TRP A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  ALA 28  28  28  ALA ALA 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  GLY 31  31  31  GLY GLY A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  TRP 34  34  34  TRP TRP A . n 
A 1 35  HIS 35  35  35  HIS HIS A . n 
A 1 36  TRP 36  36  36  TRP TRP A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  TRP 48  48  48  TRP TRP A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  MET 53  53  53  MET MET A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  TRP 74  74  74  TRP TRP A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 HIS 128 128 128 HIS HIS A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 MET 133 133 133 MET MET A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 TRP 141 141 141 TRP TRP A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ARG 146 146 146 ARG ARG 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 LYS 149 149 149 LYS LYS A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 TRP 156 156 156 TRP TRP A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 MET 171 171 171 MET MET A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 TYR 175 175 175 TYR TYR A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 PHE 180 180 180 PHE PHE A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 TRP 183 183 183 TRP TRP A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 GLN 198 198 198 GLN GLN A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 ARG 201 201 201 ARG ARG A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 HIS 212 212 212 HIS HIS A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 MET 215 215 215 MET MET A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 HIS 218 218 218 HIS HIS A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 PRO 221 221 221 PRO PRO A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 ILE 223 223 223 ILE ILE A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 TRP 225 225 225 TRP TRP A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 PHE 228 228 228 PHE PHE A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 PRO 233 233 233 PRO PRO 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 CYS 236 236 236 CYS CYS A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 ASP 240 240 240 ASP ASP A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 CYS 243 243 243 CYS CYS A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 VAL 245 245 245 VAL VAL A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 PHE 253 253 253 PHE PHE 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 TYR 256 256 256 TYR TYR A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 TRP 264 264 264 TRP TRP A . n 
A 1 265 ASN 265 265 265 ASN ASN A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 THR 270 270 270 THR THR A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 HIS 272 272 272 HIS HIS A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 HIS 274 274 274 HIS HIS A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 THR 282 282 282 THR THR A . n 
A 1 283 SER 283 283 283 SER SER A . n 
A 1 284 THR 284 284 284 THR THR A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 ASP 287 287 287 ASP ASP A . n 
A 1 288 TYR 288 288 288 TYR TYR A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 ARG 290 290 290 ARG ARG A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 ASN 295 295 295 ASN ASN A . n 
A 1 296 ILE 296 296 296 ILE ILE A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 TYR 300 300 300 TYR TYR A . n 
A 1 301 TRP 301 301 301 TRP TRP A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 ASP 305 305 305 ASP ASP A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 ILE 307 307 307 ILE ILE A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 TRP 312 312 312 TRP TRP A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 TYR 314 314 314 TYR TYR A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ILE 318 318 318 ILE ILE A . n 
A 1 319 GLN 319 319 319 GLN GLN A . n 
A 1 320 TYR 320 320 320 TYR TYR A . n 
A 1 321 TYR 321 321 321 TYR TYR A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 LYS 324 324 324 LYS LYS A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 MET 326 326 326 MET MET A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 HIS 328 328 328 HIS HIS A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 ILE 334 334 334 ILE ILE A . n 
A 1 335 SER 335 335 335 SER SER A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 ASN 339 339 339 ASN ASN A . n 
A 1 340 MET 340 340 340 MET MET A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 ASN 343 343 343 ASN ASN A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 PRO 353 353 353 PRO PRO A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 GLU 355 355 355 GLU GLU A . n 
A 1 356 GLN 356 356 356 GLN GLN A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 LYS 358 358 358 LYS LYS A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 GLN 361 361 361 GLN GLN A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ASP 365 365 365 ASP ASP A . n 
A 1 366 PHE 366 366 366 PHE PHE A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 TYR 370 370 370 TYR TYR A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 PHE 375 375 375 PHE PHE A . n 
A 1 376 SER 376 376 376 SER SER A . n 
A 1 377 THR 377 377 377 THR THR A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 ALA 379 379 379 ALA ALA A . n 
A 1 380 TRP 380 380 380 TRP TRP A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 ILE 382 382 382 ILE ILE A . n 
A 1 383 TYR 383 383 383 TYR TYR A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 PRO 387 387 387 PRO PRO A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 GLN 389 389 389 GLN GLN A . n 
A 1 390 VAL 390 390 390 VAL VAL A . n 
A 1 391 THR 391 391 391 THR THR A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 PHE 395 395 395 PHE PHE A . n 
A 1 396 THR 396 396 396 THR THR A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 PRO 398 398 398 PRO PRO A . n 
A 1 399 LEU 399 399 399 LEU LEU A . n 
A 1 400 GLN 400 400 400 GLN GLN A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 ASN 402 402 402 ASN ASN A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 ILE 406 406 406 ILE ILE A . n 
A 1 407 ARG 407 407 407 ARG ARG A . n 
A 1 408 PHE 408 408 408 PHE PHE A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 ARG 410 410 410 ARG ARG A . n 
A 1 411 ASN 411 411 411 ASN ASN A . n 
A 1 412 LYS 412 412 412 LYS LYS A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 ALA 414 414 414 ALA ALA A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 VAL 416 416 416 VAL VAL A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 TYR 418 418 418 TYR TYR A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 THR 420 420 420 THR THR A . n 
A 1 421 VAL 421 421 421 VAL VAL A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 GLY 423 423 423 GLY GLY A . n 
A 1 424 TRP 424 424 424 TRP TRP A . n 
A 1 425 PRO 425 425 425 PRO PRO A . n 
A 1 426 ASP 426 426 426 ASP ASP A . n 
A 1 427 ASP 427 427 427 ASP ASP A . n 
A 1 428 LYS 428 428 428 LYS LYS A . n 
A 1 429 HIS 429 429 429 HIS HIS A . n 
A 1 430 VAL 430 430 430 VAL VAL A . n 
A 1 431 SER 431 431 431 SER SER A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 SER 434 434 434 SER SER A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 GLY 436 436 436 GLY GLY A . n 
A 1 437 SER 437 437 437 SER SER A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 VAL 441 441 441 VAL VAL A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 LYS 444 444 444 LYS LYS A . n 
A 1 445 SER 445 445 445 SER SER A . n 
A 1 446 LEU 446 446 446 LEU LEU A . n 
A 1 447 LYS 447 447 447 LYS LYS A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 GLU 450 450 450 GLU GLU A . n 
A 1 451 LEU 451 451 451 LEU LEU A . n 
A 1 452 LEU 452 452 452 LEU LEU A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 ASP 454 454 454 ASP ASP A . n 
A 1 455 LYS 455 455 455 LYS LYS A . n 
A 1 456 ALA 456 456 456 ALA ALA A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 GLU 458 458 458 GLU GLU A . n 
A 1 459 TYR 459 459 459 TYR TYR A . n 
A 1 460 GLU 460 460 460 GLU GLU A . n 
A 1 461 GLN 461 461 461 GLN GLN A . n 
A 1 462 VAL 462 462 462 VAL VAL A . n 
A 1 463 SER 463 463 463 SER SER A . n 
A 1 464 ASP 464 464 464 ASP ASP A . n 
A 1 465 TRP 465 465 465 TRP TRP A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 GLN 467 467 467 GLN GLN A . n 
A 1 468 THR 468 468 468 THR THR A . n 
A 1 469 LYS 469 469 469 LYS LYS A . n 
A 1 470 ASP 470 470 470 ASP ASP A . n 
A 1 471 ALA 471 471 471 ALA ALA A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 GLU 473 473 473 GLU GLU A . n 
A 1 474 ILE 474 474 474 ILE ILE A . n 
A 1 475 SER 475 475 475 SER SER A . n 
A 1 476 LEU 476 476 476 LEU LEU A . n 
A 1 477 PRO 477 477 477 PRO PRO A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 LYS 479 479 479 LYS LYS A . n 
A 1 480 PRO 480 480 480 PRO PRO A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 GLU 482 482 482 GLU GLU A . n 
A 1 483 SER 483 483 483 SER SER A . n 
A 1 484 LEU 484 484 484 LEU LEU A . n 
A 1 485 ALA 485 485 485 ALA ALA A . n 
A 1 486 TYR 486 486 486 TYR TYR A . n 
A 1 487 VAL 487 487 487 VAL VAL A . n 
A 1 488 LEU 488 488 488 LEU LEU A . n 
A 1 489 LYS 489 489 489 LYS LYS A . n 
A 1 490 LEU 490 490 490 LEU LEU A . n 
A 1 491 THR 491 491 491 THR THR A . n 
A 1 492 PHE 492 492 492 PHE PHE A . n 
A 1 493 ASP 493 493 493 ASP ASP A . n 
A 1 494 GLY 494 494 494 GLY GLY A . n 
A 1 495 GLY 495 495 495 GLY GLY A . n 
A 1 496 ILE 496 496 496 ILE ILE A . n 
A 1 497 PRO 497 497 497 PRO PRO A . n 
A 1 498 VAL 498 498 498 VAL VAL A . n 
A 1 499 PRO 499 499 499 PRO PRO A . n 
A 1 500 GLN 500 500 500 GLN GLN A . n 
A 1 501 PRO 501 501 501 PRO PRO A . n 
A 1 502 LYS 502 502 502 LYS LYS A . n 
A 1 503 ILE 503 503 503 ILE ILE A . n 
A 1 504 GLY 504 504 504 GLY GLY A . n 
A 1 505 ALA 505 505 505 ALA ALA A . n 
A 1 506 SER 506 506 506 SER SER A . n 
A 1 507 VAL 507 507 507 VAL VAL A . n 
A 1 508 PHE 508 508 508 PHE PHE A . n 
A 1 509 SER 509 509 509 SER SER A . n 
A 1 510 ALA 510 510 510 ALA ALA A . n 
A 1 511 THR 511 511 511 THR THR A . n 
A 1 512 SER 512 512 512 SER SER A . n 
A 1 513 ALA 513 513 513 ALA ALA A . n 
A 1 514 THR 514 514 514 THR THR A . n 
A 1 515 GLY 515 515 515 GLY GLY A . n 
A 1 516 ARG 516 516 516 ARG ARG A . n 
A 1 517 GLY 517 517 517 GLY GLY A . n 
A 1 518 VAL 518 518 518 VAL VAL A . n 
A 1 519 SER 519 519 519 SER SER A . n 
A 1 520 LEU 520 520 520 LEU LEU A . n 
A 1 521 GLY 521 521 521 GLY GLY A . n 
A 1 522 LEU 522 522 522 LEU LEU A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 ASP 524 524 524 ASP ASP A . n 
A 1 525 PHE 525 525 525 PHE PHE A . n 
A 1 526 SER 526 526 526 SER SER A . n 
A 1 527 GLU 527 527 527 GLU GLU A . n 
A 1 528 GLU 528 528 528 GLU GLU A . n 
A 1 529 PHE 529 529 529 PHE PHE A . n 
A 1 530 LEU 530 530 530 LEU LEU A . n 
A 1 531 THR 531 531 531 THR THR A . n 
A 1 532 GLU 532 532 532 GLU GLU A . n 
A 1 533 ALA 533 533 533 ALA ALA A . n 
A 1 534 GLY 534 534 534 GLY GLY A . n 
A 1 535 LEU 535 535 535 LEU LEU A . n 
A 1 536 LYS 536 536 536 LYS LYS A . n 
A 1 537 PRO 537 537 537 PRO PRO A . n 
A 1 538 ASP 538 538 538 ASP ASP A . n 
A 1 539 THR 539 539 539 THR THR A . n 
A 1 540 ILE 540 540 540 ILE ILE A . n 
A 1 541 ARG 541 541 541 ARG ARG A . n 
A 1 542 PHE 542 542 542 PHE PHE A . n 
A 1 543 ILE 543 543 543 ILE ILE A . n 
A 1 544 ARG 544 544 544 ARG ARG A . n 
A 1 545 VAL 545 545 545 VAL VAL A . n 
A 1 546 SER 546 546 546 SER SER A . n 
A 1 547 SER 547 547 547 SER SER A . n 
A 1 548 GLY 548 548 548 GLY GLY A . n 
A 1 549 THR 549 549 549 THR THR A . n 
A 1 550 LYS 550 550 550 LYS LYS A . n 
A 1 551 LEU 551 551 551 LEU LEU A . n 
A 1 552 THR 552 552 552 THR THR A . n 
A 1 553 VAL 553 553 553 VAL VAL A . n 
A 1 554 TYR 554 554 554 TYR TYR A . n 
A 1 555 SER 555 555 555 SER SER A . n 
A 1 556 THR 556 556 556 THR THR A . n 
A 1 557 GLY 557 557 557 GLY GLY A . n 
A 1 558 ASP 558 558 558 ASP ASP A . n 
A 1 559 LEU 559 559 559 LEU LEU A . n 
A 1 560 SER 560 560 560 SER SER A . n 
A 1 561 GLY 561 561 561 GLY GLY A . n 
A 1 562 ASP 562 562 562 ASP ASP A . n 
A 1 563 SER 563 563 563 SER SER A . n 
A 1 564 LYS 564 564 564 LYS LYS A . n 
A 1 565 GLU 565 565 565 GLU GLU A . n 
A 1 566 LEU 566 566 566 LEU LEU A . n 
A 1 567 ASP 567 567 567 ASP ASP A . n 
A 1 568 ALA 568 568 568 ALA ALA A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 GLU 570 570 570 GLU GLU A . n 
A 1 571 HIS 571 571 571 HIS HIS A . n 
A 1 572 LYS 572 572 572 LYS LYS A . n 
A 1 573 VAL 573 573 573 VAL VAL A . n 
A 1 574 GLU 574 574 574 GLU GLU A . n 
A 1 575 GLU 575 575 575 GLU GLU A . n 
A 1 576 GLY 576 576 576 GLY GLY A . n 
A 1 577 SER 577 577 577 SER SER A . n 
A 1 578 VAL 578 578 578 VAL VAL A . n 
A 1 579 GLY 579 579 579 GLY GLY A . n 
A 1 580 SER 580 580 580 SER SER A . n 
A 1 581 ILE 581 581 581 ILE ILE A . n 
A 1 582 THR 582 582 582 THR THR A . n 
A 1 583 ILE 583 583 583 ILE ILE A . n 
A 1 584 SER 584 584 584 SER SER A . n 
A 1 585 LYS 585 585 585 LYS LYS A . n 
A 1 586 ALA 586 586 ?   ?   ?   A . n 
A 1 587 GLU 587 587 ?   ?   ?   A . n 
A 1 588 ASN 588 588 ?   ?   ?   A . n 
A 1 589 LEU 589 589 ?   ?   ?   A . n 
A 1 590 TYR 590 590 ?   ?   ?   A . n 
A 1 591 PHE 591 591 ?   ?   ?   A . n 
A 1 592 GLN 592 592 ?   ?   ?   A . n 
A 1 593 SER 593 593 ?   ?   ?   A . n 
A 1 594 ALA 594 594 ?   ?   ?   A . n 
A 1 595 ALA 595 595 ?   ?   ?   A . n 
A 1 596 ALA 596 596 ?   ?   ?   A . n 
A 1 597 SER 597 597 ?   ?   ?   A . n 
A 1 598 PHE 598 598 ?   ?   ?   A . n 
A 1 599 LEU 599 599 ?   ?   ?   A . n 
A 1 600 GLU 600 600 ?   ?   ?   A . n 
A 1 601 GLN 601 601 ?   ?   ?   A . n 
A 1 602 LYS 602 602 ?   ?   ?   A . n 
A 1 603 LEU 603 603 ?   ?   ?   A . n 
A 1 604 ILE 604 604 ?   ?   ?   A . n 
A 1 605 SER 605 605 ?   ?   ?   A . n 
A 1 606 GLU 606 606 ?   ?   ?   A . n 
A 1 607 GLU 607 607 ?   ?   ?   A . n 
A 1 608 ASP 608 608 ?   ?   ?   A . n 
A 1 609 LEU 609 609 ?   ?   ?   A . n 
A 1 610 ASN 610 610 ?   ?   ?   A . n 
A 1 611 SER 611 611 ?   ?   ?   A . n 
A 1 612 ALA 612 612 ?   ?   ?   A . n 
A 1 613 VAL 613 613 ?   ?   ?   A . n 
A 1 614 ASP 614 614 ?   ?   ?   A . n 
A 1 615 HIS 615 615 ?   ?   ?   A . n 
A 1 616 HIS 616 616 ?   ?   ?   A . n 
A 1 617 HIS 617 617 ?   ?   ?   A . n 
A 1 618 HIS 618 618 ?   ?   ?   A . n 
A 1 619 HIS 619 619 ?   ?   ?   A . n 
A 1 620 HIS 620 620 ?   ?   ?   A . n 
# 
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 NAG 1   701  601 NAG NAG A . 
C 2 NAG 1   702  602 NAG NAG A . 
D 3 TRS 1   703  603 TRS TRS A . 
E 4 MPD 1   704  604 MPD MPD A . 
F 4 MPD 1   705  605 MPD MPD A . 
G 2 NAG 1   706  606 NAG NAG A . 
H 5 NA  1   707  1   NA  NA  A . 
I 6 AZI 1   708  1   AZI AZI A . 
J 6 AZI 1   709  2   AZI AZI A . 
K 7 ACT 1   710  3   ACT ACT A . 
L 6 AZI 1   711  4   AZI AZI A . 
M 6 AZI 1   712  5   AZI AZI A . 
N 6 AZI 1   713  6   AZI AZI A . 
O 7 ACT 1   714  7   ACT ACT A . 
P 8 HOH 1   801  102 HOH HOH A . 
P 8 HOH 2   802  230 HOH HOH A . 
P 8 HOH 3   803  60  HOH HOH A . 
P 8 HOH 4   804  45  HOH HOH A . 
P 8 HOH 5   805  89  HOH HOH A . 
P 8 HOH 6   806  159 HOH HOH A . 
P 8 HOH 7   807  115 HOH HOH A . 
P 8 HOH 8   808  97  HOH HOH A . 
P 8 HOH 9   809  146 HOH HOH A . 
P 8 HOH 10  810  52  HOH HOH A . 
P 8 HOH 11  811  13  HOH HOH A . 
P 8 HOH 12  812  223 HOH HOH A . 
P 8 HOH 13  813  192 HOH HOH A . 
P 8 HOH 14  814  206 HOH HOH A . 
P 8 HOH 15  815  166 HOH HOH A . 
P 8 HOH 16  816  173 HOH HOH A . 
P 8 HOH 17  817  23  HOH HOH A . 
P 8 HOH 18  818  228 HOH HOH A . 
P 8 HOH 19  819  8   HOH HOH A . 
P 8 HOH 20  820  122 HOH HOH A . 
P 8 HOH 21  821  19  HOH HOH A . 
P 8 HOH 22  822  33  HOH HOH A . 
P 8 HOH 23  823  215 HOH HOH A . 
P 8 HOH 24  824  5   HOH HOH A . 
P 8 HOH 25  825  94  HOH HOH A . 
P 8 HOH 26  826  117 HOH HOH A . 
P 8 HOH 27  827  182 HOH HOH A . 
P 8 HOH 28  828  41  HOH HOH A . 
P 8 HOH 29  829  72  HOH HOH A . 
P 8 HOH 30  830  183 HOH HOH A . 
P 8 HOH 31  831  196 HOH HOH A . 
P 8 HOH 32  832  111 HOH HOH A . 
P 8 HOH 33  833  160 HOH HOH A . 
P 8 HOH 34  834  174 HOH HOH A . 
P 8 HOH 35  835  50  HOH HOH A . 
P 8 HOH 36  836  38  HOH HOH A . 
P 8 HOH 37  837  61  HOH HOH A . 
P 8 HOH 38  838  143 HOH HOH A . 
P 8 HOH 39  839  121 HOH HOH A . 
P 8 HOH 40  840  219 HOH HOH A . 
P 8 HOH 41  841  3   HOH HOH A . 
P 8 HOH 42  842  44  HOH HOH A . 
P 8 HOH 43  843  22  HOH HOH A . 
P 8 HOH 44  844  55  HOH HOH A . 
P 8 HOH 45  845  144 HOH HOH A . 
P 8 HOH 46  846  136 HOH HOH A . 
P 8 HOH 47  847  12  HOH HOH A . 
P 8 HOH 48  848  43  HOH HOH A . 
P 8 HOH 49  849  26  HOH HOH A . 
P 8 HOH 50  850  100 HOH HOH A . 
P 8 HOH 51  851  158 HOH HOH A . 
P 8 HOH 52  852  176 HOH HOH A . 
P 8 HOH 53  853  162 HOH HOH A . 
P 8 HOH 54  854  120 HOH HOH A . 
P 8 HOH 55  855  130 HOH HOH A . 
P 8 HOH 56  856  21  HOH HOH A . 
P 8 HOH 57  857  1   HOH HOH A . 
P 8 HOH 58  858  139 HOH HOH A . 
P 8 HOH 59  859  57  HOH HOH A . 
P 8 HOH 60  860  40  HOH HOH A . 
P 8 HOH 61  861  232 HOH HOH A . 
P 8 HOH 62  862  28  HOH HOH A . 
P 8 HOH 63  863  225 HOH HOH A . 
P 8 HOH 64  864  79  HOH HOH A . 
P 8 HOH 65  865  142 HOH HOH A . 
P 8 HOH 66  866  9   HOH HOH A . 
P 8 HOH 67  867  107 HOH HOH A . 
P 8 HOH 68  868  181 HOH HOH A . 
P 8 HOH 69  869  234 HOH HOH A . 
P 8 HOH 70  870  37  HOH HOH A . 
P 8 HOH 71  871  29  HOH HOH A . 
P 8 HOH 72  872  226 HOH HOH A . 
P 8 HOH 73  873  63  HOH HOH A . 
P 8 HOH 74  874  7   HOH HOH A . 
P 8 HOH 75  875  77  HOH HOH A . 
P 8 HOH 76  876  106 HOH HOH A . 
P 8 HOH 77  877  11  HOH HOH A . 
P 8 HOH 78  878  80  HOH HOH A . 
P 8 HOH 79  879  137 HOH HOH A . 
P 8 HOH 80  880  56  HOH HOH A . 
P 8 HOH 81  881  175 HOH HOH A . 
P 8 HOH 82  882  15  HOH HOH A . 
P 8 HOH 83  883  116 HOH HOH A . 
P 8 HOH 84  884  31  HOH HOH A . 
P 8 HOH 85  885  91  HOH HOH A . 
P 8 HOH 86  886  110 HOH HOH A . 
P 8 HOH 87  887  27  HOH HOH A . 
P 8 HOH 88  888  74  HOH HOH A . 
P 8 HOH 89  889  51  HOH HOH A . 
P 8 HOH 90  890  152 HOH HOH A . 
P 8 HOH 91  891  172 HOH HOH A . 
P 8 HOH 92  892  233 HOH HOH A . 
P 8 HOH 93  893  118 HOH HOH A . 
P 8 HOH 94  894  86  HOH HOH A . 
P 8 HOH 95  895  34  HOH HOH A . 
P 8 HOH 96  896  133 HOH HOH A . 
P 8 HOH 97  897  112 HOH HOH A . 
P 8 HOH 98  898  78  HOH HOH A . 
P 8 HOH 99  899  2   HOH HOH A . 
P 8 HOH 100 900  75  HOH HOH A . 
P 8 HOH 101 901  67  HOH HOH A . 
P 8 HOH 102 902  207 HOH HOH A . 
P 8 HOH 103 903  186 HOH HOH A . 
P 8 HOH 104 904  71  HOH HOH A . 
P 8 HOH 105 905  58  HOH HOH A . 
P 8 HOH 106 906  229 HOH HOH A . 
P 8 HOH 107 907  20  HOH HOH A . 
P 8 HOH 108 908  124 HOH HOH A . 
P 8 HOH 109 909  149 HOH HOH A . 
P 8 HOH 110 910  151 HOH HOH A . 
P 8 HOH 111 911  48  HOH HOH A . 
P 8 HOH 112 912  90  HOH HOH A . 
P 8 HOH 113 913  104 HOH HOH A . 
P 8 HOH 114 914  193 HOH HOH A . 
P 8 HOH 115 915  132 HOH HOH A . 
P 8 HOH 116 916  135 HOH HOH A . 
P 8 HOH 117 917  96  HOH HOH A . 
P 8 HOH 118 918  140 HOH HOH A . 
P 8 HOH 119 919  187 HOH HOH A . 
P 8 HOH 120 920  24  HOH HOH A . 
P 8 HOH 121 921  199 HOH HOH A . 
P 8 HOH 122 922  54  HOH HOH A . 
P 8 HOH 123 923  10  HOH HOH A . 
P 8 HOH 124 924  62  HOH HOH A . 
P 8 HOH 125 925  69  HOH HOH A . 
P 8 HOH 126 926  188 HOH HOH A . 
P 8 HOH 127 927  128 HOH HOH A . 
P 8 HOH 128 928  64  HOH HOH A . 
P 8 HOH 129 929  82  HOH HOH A . 
P 8 HOH 130 930  154 HOH HOH A . 
P 8 HOH 131 931  18  HOH HOH A . 
P 8 HOH 132 932  49  HOH HOH A . 
P 8 HOH 133 933  17  HOH HOH A . 
P 8 HOH 134 934  147 HOH HOH A . 
P 8 HOH 135 935  109 HOH HOH A . 
P 8 HOH 136 936  65  HOH HOH A . 
P 8 HOH 137 937  227 HOH HOH A . 
P 8 HOH 138 938  47  HOH HOH A . 
P 8 HOH 139 939  88  HOH HOH A . 
P 8 HOH 140 940  6   HOH HOH A . 
P 8 HOH 141 941  70  HOH HOH A . 
P 8 HOH 142 942  35  HOH HOH A . 
P 8 HOH 143 943  42  HOH HOH A . 
P 8 HOH 144 944  39  HOH HOH A . 
P 8 HOH 145 945  145 HOH HOH A . 
P 8 HOH 146 946  76  HOH HOH A . 
P 8 HOH 147 947  153 HOH HOH A . 
P 8 HOH 148 948  85  HOH HOH A . 
P 8 HOH 149 949  178 HOH HOH A . 
P 8 HOH 150 950  210 HOH HOH A . 
P 8 HOH 151 951  231 HOH HOH A . 
P 8 HOH 152 952  218 HOH HOH A . 
P 8 HOH 153 953  25  HOH HOH A . 
P 8 HOH 154 954  14  HOH HOH A . 
P 8 HOH 155 955  165 HOH HOH A . 
P 8 HOH 156 956  189 HOH HOH A . 
P 8 HOH 157 957  131 HOH HOH A . 
P 8 HOH 158 958  108 HOH HOH A . 
P 8 HOH 159 959  30  HOH HOH A . 
P 8 HOH 160 960  129 HOH HOH A . 
P 8 HOH 161 961  68  HOH HOH A . 
P 8 HOH 162 962  101 HOH HOH A . 
P 8 HOH 163 963  36  HOH HOH A . 
P 8 HOH 164 964  161 HOH HOH A . 
P 8 HOH 165 965  4   HOH HOH A . 
P 8 HOH 166 966  216 HOH HOH A . 
P 8 HOH 167 967  53  HOH HOH A . 
P 8 HOH 168 968  150 HOH HOH A . 
P 8 HOH 169 969  141 HOH HOH A . 
P 8 HOH 170 970  73  HOH HOH A . 
P 8 HOH 171 971  93  HOH HOH A . 
P 8 HOH 172 972  95  HOH HOH A . 
P 8 HOH 173 973  212 HOH HOH A . 
P 8 HOH 174 974  157 HOH HOH A . 
P 8 HOH 175 975  59  HOH HOH A . 
P 8 HOH 176 976  113 HOH HOH A . 
P 8 HOH 177 977  16  HOH HOH A . 
P 8 HOH 178 978  126 HOH HOH A . 
P 8 HOH 179 979  32  HOH HOH A . 
P 8 HOH 180 980  98  HOH HOH A . 
P 8 HOH 181 981  127 HOH HOH A . 
P 8 HOH 182 982  211 HOH HOH A . 
P 8 HOH 183 983  179 HOH HOH A . 
P 8 HOH 184 984  155 HOH HOH A . 
P 8 HOH 185 985  105 HOH HOH A . 
P 8 HOH 186 986  185 HOH HOH A . 
P 8 HOH 187 987  92  HOH HOH A . 
P 8 HOH 188 988  221 HOH HOH A . 
P 8 HOH 189 989  103 HOH HOH A . 
P 8 HOH 190 990  201 HOH HOH A . 
P 8 HOH 191 991  167 HOH HOH A . 
P 8 HOH 192 992  134 HOH HOH A . 
P 8 HOH 193 993  148 HOH HOH A . 
P 8 HOH 194 994  66  HOH HOH A . 
P 8 HOH 195 995  213 HOH HOH A . 
P 8 HOH 196 996  87  HOH HOH A . 
P 8 HOH 197 997  180 HOH HOH A . 
P 8 HOH 198 998  125 HOH HOH A . 
P 8 HOH 199 999  46  HOH HOH A . 
P 8 HOH 200 1000 205 HOH HOH A . 
P 8 HOH 201 1001 119 HOH HOH A . 
P 8 HOH 202 1002 83  HOH HOH A . 
P 8 HOH 203 1003 114 HOH HOH A . 
P 8 HOH 204 1004 171 HOH HOH A . 
P 8 HOH 205 1005 164 HOH HOH A . 
P 8 HOH 206 1006 224 HOH HOH A . 
P 8 HOH 207 1007 99  HOH HOH A . 
P 8 HOH 208 1008 123 HOH HOH A . 
P 8 HOH 209 1009 200 HOH HOH A . 
P 8 HOH 210 1010 163 HOH HOH A . 
P 8 HOH 211 1011 177 HOH HOH A . 
P 8 HOH 212 1012 84  HOH HOH A . 
P 8 HOH 213 1013 138 HOH HOH A . 
P 8 HOH 214 1014 202 HOH HOH A . 
P 8 HOH 215 1015 156 HOH HOH A . 
P 8 HOH 216 1016 203 HOH HOH A . 
P 8 HOH 217 1017 170 HOH HOH A . 
P 8 HOH 218 1018 168 HOH HOH A . 
P 8 HOH 219 1019 190 HOH HOH A . 
P 8 HOH 220 1020 209 HOH HOH A . 
P 8 HOH 221 1021 194 HOH HOH A . 
P 8 HOH 222 1022 169 HOH HOH A . 
P 8 HOH 223 1023 214 HOH HOH A . 
P 8 HOH 224 1024 217 HOH HOH A . 
P 8 HOH 225 1025 197 HOH HOH A . 
P 8 HOH 226 1026 222 HOH HOH A . 
P 8 HOH 227 1027 81  HOH HOH A . 
P 8 HOH 228 1028 184 HOH HOH A . 
P 8 HOH 229 1029 204 HOH HOH A . 
P 8 HOH 230 1030 191 HOH HOH A . 
P 8 HOH 231 1031 220 HOH HOH A . 
P 8 HOH 232 1032 208 HOH HOH A . 
P 8 HOH 233 1033 198 HOH HOH A . 
P 8 HOH 234 1034 195 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 62  ? CE  ? A LYS 62  CE  
2   1 Y 1 A LYS 62  ? NZ  ? A LYS 62  NZ  
3   1 Y 1 A LYS 87  ? CD  ? A LYS 87  CD  
4   1 Y 1 A LYS 87  ? CE  ? A LYS 87  CE  
5   1 Y 1 A LYS 87  ? NZ  ? A LYS 87  NZ  
6   1 Y 1 A LYS 94  ? NZ  ? A LYS 94  NZ  
7   1 Y 1 A LYS 100 ? CD  ? A LYS 100 CD  
8   1 Y 1 A LYS 100 ? CE  ? A LYS 100 CE  
9   1 Y 1 A LYS 100 ? NZ  ? A LYS 100 NZ  
10  1 Y 1 A LYS 137 ? CE  ? A LYS 137 CE  
11  1 Y 1 A LYS 137 ? NZ  ? A LYS 137 NZ  
12  1 Y 1 A GLU 202 ? CG  ? A GLU 202 CG  
13  1 Y 1 A GLU 202 ? CD  ? A GLU 202 CD  
14  1 Y 1 A GLU 202 ? OE1 ? A GLU 202 OE1 
15  1 Y 1 A GLU 202 ? OE2 ? A GLU 202 OE2 
16  1 Y 1 A LYS 248 ? CG  ? A LYS 248 CG  
17  1 Y 1 A LYS 248 ? CD  ? A LYS 248 CD  
18  1 Y 1 A LYS 248 ? CE  ? A LYS 248 CE  
19  1 Y 1 A LYS 248 ? NZ  ? A LYS 248 NZ  
20  1 Y 1 A SER 437 ? OG  ? A SER 437 OG  
21  1 Y 1 A LYS 444 ? CG  ? A LYS 444 CG  
22  1 Y 1 A LYS 444 ? CD  ? A LYS 444 CD  
23  1 Y 1 A LYS 444 ? CE  ? A LYS 444 CE  
24  1 Y 1 A LYS 444 ? NZ  ? A LYS 444 NZ  
25  1 Y 1 A LYS 455 ? CE  ? A LYS 455 CE  
26  1 Y 1 A LYS 455 ? NZ  ? A LYS 455 NZ  
27  1 Y 1 A LYS 466 ? CG  ? A LYS 466 CG  
28  1 Y 1 A LYS 466 ? CD  ? A LYS 466 CD  
29  1 Y 1 A LYS 466 ? CE  ? A LYS 466 CE  
30  1 Y 1 A LYS 466 ? NZ  ? A LYS 466 NZ  
31  1 Y 1 A LYS 469 ? CG  ? A LYS 469 CG  
32  1 Y 1 A LYS 469 ? CD  ? A LYS 469 CD  
33  1 Y 1 A LYS 469 ? CE  ? A LYS 469 CE  
34  1 Y 1 A LYS 469 ? NZ  ? A LYS 469 NZ  
35  1 Y 1 A LYS 502 ? CG  ? A LYS 502 CG  
36  1 Y 1 A LYS 502 ? CD  ? A LYS 502 CD  
37  1 Y 1 A LYS 502 ? CE  ? A LYS 502 CE  
38  1 Y 1 A LYS 502 ? NZ  ? A LYS 502 NZ  
39  1 Y 1 A ILE 503 ? CG1 ? A ILE 503 CG1 
40  1 Y 1 A ILE 503 ? CG2 ? A ILE 503 CG2 
41  1 Y 1 A ILE 503 ? CD1 ? A ILE 503 CD1 
42  1 Y 1 A THR 511 ? OG1 ? A THR 511 OG1 
43  1 Y 1 A THR 511 ? CG2 ? A THR 511 CG2 
44  1 Y 1 A GLU 527 ? CG  ? A GLU 527 CG  
45  1 Y 1 A GLU 527 ? CD  ? A GLU 527 CD  
46  1 Y 1 A GLU 527 ? OE1 ? A GLU 527 OE1 
47  1 Y 1 A GLU 527 ? OE2 ? A GLU 527 OE2 
48  1 Y 1 A LYS 536 ? CG  ? A LYS 536 CG  
49  1 Y 1 A LYS 536 ? CD  ? A LYS 536 CD  
50  1 Y 1 A LYS 536 ? CE  ? A LYS 536 CE  
51  1 Y 1 A LYS 536 ? NZ  ? A LYS 536 NZ  
52  1 Y 1 A LYS 550 ? CG  ? A LYS 550 CG  
53  1 Y 1 A LYS 550 ? CD  ? A LYS 550 CD  
54  1 Y 1 A LYS 550 ? CE  ? A LYS 550 CE  
55  1 Y 1 A LYS 550 ? NZ  ? A LYS 550 NZ  
56  1 Y 1 A THR 552 ? OG1 ? A THR 552 OG1 
57  1 Y 1 A THR 552 ? CG2 ? A THR 552 CG2 
58  1 Y 1 A SER 555 ? OG  ? A SER 555 OG  
59  1 Y 1 A THR 556 ? OG1 ? A THR 556 OG1 
60  1 Y 1 A THR 556 ? CG2 ? A THR 556 CG2 
61  1 Y 1 A ASP 558 ? CG  ? A ASP 558 CG  
62  1 Y 1 A ASP 558 ? OD1 ? A ASP 558 OD1 
63  1 Y 1 A ASP 558 ? OD2 ? A ASP 558 OD2 
64  1 Y 1 A LEU 559 ? CG  ? A LEU 559 CG  
65  1 Y 1 A LEU 559 ? CD1 ? A LEU 559 CD1 
66  1 Y 1 A LEU 559 ? CD2 ? A LEU 559 CD2 
67  1 Y 1 A ASP 562 ? CG  ? A ASP 562 CG  
68  1 Y 1 A ASP 562 ? OD1 ? A ASP 562 OD1 
69  1 Y 1 A ASP 562 ? OD2 ? A ASP 562 OD2 
70  1 Y 1 A LYS 564 ? CG  ? A LYS 564 CG  
71  1 Y 1 A LYS 564 ? CD  ? A LYS 564 CD  
72  1 Y 1 A LYS 564 ? CE  ? A LYS 564 CE  
73  1 Y 1 A LYS 564 ? NZ  ? A LYS 564 NZ  
74  1 Y 1 A GLU 565 ? CG  ? A GLU 565 CG  
75  1 Y 1 A GLU 565 ? CD  ? A GLU 565 CD  
76  1 Y 1 A GLU 565 ? OE1 ? A GLU 565 OE1 
77  1 Y 1 A GLU 565 ? OE2 ? A GLU 565 OE2 
78  1 Y 1 A LEU 566 ? CG  ? A LEU 566 CG  
79  1 Y 1 A LEU 566 ? CD1 ? A LEU 566 CD1 
80  1 Y 1 A LEU 566 ? CD2 ? A LEU 566 CD2 
81  1 Y 1 A ASP 567 ? CG  ? A ASP 567 CG  
82  1 Y 1 A ASP 567 ? OD1 ? A ASP 567 OD1 
83  1 Y 1 A ASP 567 ? OD2 ? A ASP 567 OD2 
84  1 Y 1 A LYS 572 ? CG  ? A LYS 572 CG  
85  1 Y 1 A LYS 572 ? CD  ? A LYS 572 CD  
86  1 Y 1 A LYS 572 ? CE  ? A LYS 572 CE  
87  1 Y 1 A LYS 572 ? NZ  ? A LYS 572 NZ  
88  1 Y 1 A VAL 573 ? CG1 ? A VAL 573 CG1 
89  1 Y 1 A VAL 573 ? CG2 ? A VAL 573 CG2 
90  1 Y 1 A GLU 574 ? CG  ? A GLU 574 CG  
91  1 Y 1 A GLU 574 ? CD  ? A GLU 574 CD  
92  1 Y 1 A GLU 574 ? OE1 ? A GLU 574 OE1 
93  1 Y 1 A GLU 574 ? OE2 ? A GLU 574 OE2 
94  1 Y 1 A SER 577 ? OG  ? A SER 577 OG  
95  1 Y 1 A VAL 578 ? CG1 ? A VAL 578 CG1 
96  1 Y 1 A VAL 578 ? CG2 ? A VAL 578 CG2 
97  1 Y 1 A SER 580 ? OG  ? A SER 580 OG  
98  1 Y 1 A ILE 581 ? CG1 ? A ILE 581 CG1 
99  1 Y 1 A ILE 581 ? CG2 ? A ILE 581 CG2 
100 1 Y 1 A ILE 581 ? CD1 ? A ILE 581 CD1 
101 1 Y 1 A SER 584 ? OG  ? A SER 584 OG  
102 1 Y 1 A LYS 585 ? CG  ? A LYS 585 CG  
103 1 Y 1 A LYS 585 ? CD  ? A LYS 585 CD  
104 1 Y 1 A LYS 585 ? CE  ? A LYS 585 CE  
105 1 Y 1 A LYS 585 ? NZ  ? A LYS 585 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? 'autoPROC 1.0.5' 1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487      2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487      3 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LXL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.757 
_cell.length_a_esd                 ? 
_cell.length_b                     76.757 
_cell.length_b_esd                 ? 
_cell.length_c                     225.338 
_cell.length_c_esd                 ? 
_cell.volume                       1327609.709 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9LXL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            'P 4abw 2nw' 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   9LXL 
_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             2.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.79 
_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              6.7 
_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    '0.1M Bis-Tris pH 6.7, 20% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 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         2023-12-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL17UM' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17UM 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          37.64 
_reflns.entry_id                                       9LXL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.191 
_reflns.d_resolution_low                               72.657 
_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                                     24244 
_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                           91.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                0.058 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.216 
_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                                    2.191 
_reflns_shell.d_res_low                                     2.441 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1212 
_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                               ? 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.589 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               56.81 
_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                                 9LXL 
_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                            2.191 
_refine.ls_d_res_low                             63.44 
_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                     24241 
_refine.ls_number_reflns_R_free                  1233 
_refine.ls_number_reflns_R_work                  23008 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    67.99 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2036 
_refine.ls_R_factor_R_free                       0.2339 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2020 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.36 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 25.9997 
_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                            0.2481 
_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.details                          ? 
_refine_hist.d_res_high                       2.191 
_refine_hist.d_res_low                        63.44 
_refine_hist.number_atoms_solvent             234 
_refine_hist.number_atoms_total               4803 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4479 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         90 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0101  ? 4724 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.4804  ? 6435 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0902  ? 685  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0123  ? 836  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.7278 ? 1653 ? f_dihedral_angle_d ? ? 
# 
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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 2.191 2.28  . . 3   139  3.71   . . . . 0.3347 . . . . . . . . . . . . . . . 0.2775 
'X-RAY DIFFRACTION' 2.28  2.38  . . 41  527  14.63  . . . . 0.3126 . . . . . . . . . . . . . . . 0.3638 
'X-RAY DIFFRACTION' 2.38  2.51  . . 64  1265 34.38  . . . . 0.3052 . . . . . . . . . . . . . . . 0.3518 
'X-RAY DIFFRACTION' 2.51  2.67  . . 132 2378 64.15  . . . . 0.2883 . . . . . . . . . . . . . . . 0.3080 
'X-RAY DIFFRACTION' 2.67  2.87  . . 180 3330 89.56  . . . . 0.2802 . . . . . . . . . . . . . . . 0.2745 
'X-RAY DIFFRACTION' 2.87  3.16  . . 200 3719 99.67  . . . . 0.2440 . . . . . . . . . . . . . . . 0.3035 
'X-RAY DIFFRACTION' 3.16  3.62  . . 191 3786 100.00 . . . . 0.2071 . . . . . . . . . . . . . . . 0.2414 
'X-RAY DIFFRACTION' 3.62  4.56  . . 207 3818 100.00 . . . . 0.1561 . . . . . . . . . . . . . . . 0.1980 
'X-RAY DIFFRACTION' 4.56  63.44 . . 215 4046 99.95  . . . . 0.1727 . . . . . . . . . . . . . . . 0.1919 
# 
_struct.entry_id                     9LXL 
_struct.title                        'Crystal structure of GH29 family alpha-L-fucosidase from Fusarium proliferatum LE1' 
_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        9LXL 
_struct_keywords.text            'alpha-L-fucosidase, GH29, Fusarium Proliferatum, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
K N N 7 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 7 ? 
P N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A365NIL9_GIBIN 
_struct_ref.pdbx_db_accession          A0A365NIL9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QASGPYEATWESTDKHIASPEWFRDAKFGVYWHWGAFTTPQYASEWYPRNMYEPGSDQRKHHTETYGPPEEWGYANFING
ADDLKGNFVQFKPVLSSKGGEFDPEAIIKAVKASGAKFAGPVGEHHDGYSMWDSKVNEWNSVKRGPKLDLVKLWADLVRK
NGMKLVVAMHQAYNYNGFYEWAPKTNDTSLKKLLGQLSREESDQLWFDKHREMLDHVQPDIIWNDFSLDSPGYCADFDGP
CAVAEKKRLEFLAYYFNRAVEWNKEVVTTHKHFDVGFRDTSTVSDYERGGPANITRPYWLTDDAISASSWSYTVGIQYYS
SKAMVHSLLDRISKNGNMLLNISPTAVGVLPDEQLKVLQDIGDFLGRYGESVFSTRAWDIYGEGPNQVTGGSFTAPLQGN
SSDIRFTRNKDANVLYATVLGWPDDKHVSIASLGSDALVDLKSLKSIELLGDKTGEYEQVSDWKQTKDALEISLPAQPAE
SLAYVLKLTFDGGIPVPQPKIGASVFSATSATGRGVSLGLGDFNEEFLTEAGLKPDTIRFIRVSSGTKLTVYSTGDLSGD
SKELDAGEHKVEEGSVGSITISKA
;
_struct_ref.pdbx_align_begin           25 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9LXL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 586 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A365NIL9 
_struct_ref_seq.db_align_beg                  25 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  608 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       3 
_struct_ref_seq.pdbx_auth_seq_align_end       586 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9LXL GLU A 1   ? UNP A0A365NIL9 ?   ?   'expression tag' 1   1  
1 9LXL THR A 2   ? UNP A0A365NIL9 ?   ?   'expression tag' 2   2  
1 9LXL ALA A 456 ? UNP A0A365NIL9 THR 478 variant          456 3  
1 9LXL LYS A 479 ? UNP A0A365NIL9 GLN 501 variant          479 4  
1 9LXL SER A 526 ? UNP A0A365NIL9 ASN 548 variant          526 5  
1 9LXL GLU A 587 ? UNP A0A365NIL9 ?   ?   'expression tag' 587 6  
1 9LXL ASN A 588 ? UNP A0A365NIL9 ?   ?   'expression tag' 588 7  
1 9LXL LEU A 589 ? UNP A0A365NIL9 ?   ?   'expression tag' 589 8  
1 9LXL TYR A 590 ? UNP A0A365NIL9 ?   ?   'expression tag' 590 9  
1 9LXL PHE A 591 ? UNP A0A365NIL9 ?   ?   'expression tag' 591 10 
1 9LXL GLN A 592 ? UNP A0A365NIL9 ?   ?   'expression tag' 592 11 
1 9LXL SER A 593 ? UNP A0A365NIL9 ?   ?   'expression tag' 593 12 
1 9LXL ALA A 594 ? UNP A0A365NIL9 ?   ?   'expression tag' 594 13 
1 9LXL ALA A 595 ? UNP A0A365NIL9 ?   ?   'expression tag' 595 14 
1 9LXL ALA A 596 ? UNP A0A365NIL9 ?   ?   'expression tag' 596 15 
1 9LXL SER A 597 ? UNP A0A365NIL9 ?   ?   'expression tag' 597 16 
1 9LXL PHE A 598 ? UNP A0A365NIL9 ?   ?   'expression tag' 598 17 
1 9LXL LEU A 599 ? UNP A0A365NIL9 ?   ?   'expression tag' 599 18 
1 9LXL GLU A 600 ? UNP A0A365NIL9 ?   ?   'expression tag' 600 19 
1 9LXL GLN A 601 ? UNP A0A365NIL9 ?   ?   'expression tag' 601 20 
1 9LXL LYS A 602 ? UNP A0A365NIL9 ?   ?   'expression tag' 602 21 
1 9LXL LEU A 603 ? UNP A0A365NIL9 ?   ?   'expression tag' 603 22 
1 9LXL ILE A 604 ? UNP A0A365NIL9 ?   ?   'expression tag' 604 23 
1 9LXL SER A 605 ? UNP A0A365NIL9 ?   ?   'expression tag' 605 24 
1 9LXL GLU A 606 ? UNP A0A365NIL9 ?   ?   'expression tag' 606 25 
1 9LXL GLU A 607 ? UNP A0A365NIL9 ?   ?   'expression tag' 607 26 
1 9LXL ASP A 608 ? UNP A0A365NIL9 ?   ?   'expression tag' 608 27 
1 9LXL LEU A 609 ? UNP A0A365NIL9 ?   ?   'expression tag' 609 28 
1 9LXL ASN A 610 ? UNP A0A365NIL9 ?   ?   'expression tag' 610 29 
1 9LXL SER A 611 ? UNP A0A365NIL9 ?   ?   'expression tag' 611 30 
1 9LXL ALA A 612 ? UNP A0A365NIL9 ?   ?   'expression tag' 612 31 
1 9LXL VAL A 613 ? UNP A0A365NIL9 ?   ?   'expression tag' 613 32 
1 9LXL ASP A 614 ? UNP A0A365NIL9 ?   ?   'expression tag' 614 33 
1 9LXL HIS A 615 ? UNP A0A365NIL9 ?   ?   'expression tag' 615 34 
1 9LXL HIS A 616 ? UNP A0A365NIL9 ?   ?   'expression tag' 616 35 
1 9LXL HIS A 617 ? UNP A0A365NIL9 ?   ?   'expression tag' 617 36 
1 9LXL HIS A 618 ? UNP A0A365NIL9 ?   ?   'expression tag' 618 37 
1 9LXL HIS A 619 ? UNP A0A365NIL9 ?   ?   'expression tag' 619 38 
1 9LXL HIS A 620 ? UNP A0A365NIL9 ?   ?   'expression tag' 620 39 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 750   ? 
1 MORE         1     ? 
1 'SSA (A^2)'  21810 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 THR A 11  ? ASP A 16  ? THR A 11  ASP A 16  1 ? 6  
HELX_P HELX_P2  AA2 PRO A 22  ? LYS A 29  ? PRO A 22  LYS A 29  1 ? 8  
HELX_P HELX_P3  AA3 GLY A 37  ? THR A 41  ? GLY A 37  THR A 41  5 ? 5  
HELX_P HELX_P4  AA4 TRP A 48  ? MET A 53  ? TRP A 48  MET A 53  1 ? 6  
HELX_P HELX_P5  AA5 SER A 58  ? TYR A 68  ? SER A 58  TYR A 68  1 ? 11 
HELX_P HELX_P6  AA6 GLY A 75  ? GLY A 82  ? GLY A 75  GLY A 82  1 ? 8  
HELX_P HELX_P7  AA7 LEU A 97  ? GLY A 101 ? LEU A 97  GLY A 101 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 105 ? SER A 116 ? ASP A 105 SER A 116 1 ? 12 
HELX_P HELX_P9  AA9 ASP A 151 ? ASN A 163 ? ASP A 151 ASN A 163 1 ? 13 
HELX_P HELX_P10 AB1 ALA A 174 ? ASN A 178 ? ALA A 174 ASN A 178 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 189 ? LEU A 196 ? ASP A 189 LEU A 196 1 ? 8  
HELX_P HELX_P12 AB3 SER A 200 ? GLN A 220 ? SER A 200 GLN A 220 1 ? 21 
HELX_P HELX_P13 AB4 ALA A 246 ? ASN A 265 ? ALA A 246 ASN A 265 1 ? 20 
HELX_P HELX_P14 AB5 SER A 322 ? LYS A 336 ? SER A 322 LYS A 336 1 ? 15 
HELX_P HELX_P15 AB6 PRO A 353 ? PHE A 375 ? PRO A 353 PHE A 375 1 ? 23 
HELX_P HELX_P16 AB7 ALA A 433 ? LEU A 440 ? ALA A 433 LEU A 440 5 ? 8  
HELX_P HELX_P17 AB8 ASP A 442 ? LYS A 444 ? ASP A 442 LYS A 444 5 ? 3  
HELX_P HELX_P18 AB9 SER A 526 ? GLY A 534 ? SER A 526 GLY A 534 1 ? 9  
HELX_P HELX_P19 AC1 LYS A 536 ? ILE A 540 ? LYS A 536 ILE A 540 5 ? 5  
# 
_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 
disulf1 disulf ?   ? A CYS 236 SG  ? ? ? 1_555 A CYS 243 SG ? ? A CYS 236 A CYS 243 1_555 ? ? ? ? ? ? ? 1.994 ? ?               
covale1 covale one ? A ASN 188 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 188 A NAG 701 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale2 covale one ? A ASN 295 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 295 A NAG 706 1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
covale3 covale one ? A ASN 402 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 402 A NAG 702 1_555 ? ? ? ? ? ? ? 1.430 ? N-Glycosylation 
metalc1 metalc ?   ? A ASP 16  O   ? ? ? 1_555 H NA  .   NA ? ? A ASP 16  A NA  707 1_555 ? ? ? ? ? ? ? 2.492 ? ?               
metalc2 metalc ?   ? A HIS 18  O   ? ? ? 1_555 H NA  .   NA ? ? A HIS 18  A NA  707 1_555 ? ? ? ? ? ? ? 2.733 ? ?               
metalc3 metalc ?   ? A THR 282 O   ? ? ? 1_555 H NA  .   NA ? ? A THR 282 A NA  707 1_555 ? ? ? ? ? ? ? 2.580 ? ?               
metalc4 metalc ?   ? H NA  .   NA  ? ? ? 1_555 P HOH .   O  ? ? A NA  707 A HOH 843 1_555 ? ? ? ? ? ? ? 2.979 ? ?               
metalc5 metalc ?   ? H NA  .   NA  ? ? ? 1_555 P HOH .   O  ? ? A NA  707 A HOH 963 1_555 ? ? ? ? ? ? ? 2.584 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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  O ? A ASP 16  ? A ASP 16  ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? A HIS 18  ? A HIS 18  ? 1_555 98.5  ? 
2  O ? A ASP 16  ? A ASP 16  ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? A THR 282 ? A THR 282 ? 1_555 95.7  ? 
3  O ? A HIS 18  ? A HIS 18  ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? A THR 282 ? A THR 282 ? 1_555 75.5  ? 
4  O ? A ASP 16  ? A ASP 16  ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? P HOH .   ? A HOH 843 ? 1_555 155.6 ? 
5  O ? A HIS 18  ? A HIS 18  ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? P HOH .   ? A HOH 843 ? 1_555 67.4  ? 
6  O ? A THR 282 ? A THR 282 ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? P HOH .   ? A HOH 843 ? 1_555 62.2  ? 
7  O ? A ASP 16  ? A ASP 16  ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? P HOH .   ? A HOH 963 ? 1_555 116.5 ? 
8  O ? A HIS 18  ? A HIS 18  ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? P HOH .   ? A HOH 963 ? 1_555 94.0  ? 
9  O ? A THR 282 ? A THR 282 ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? P HOH .   ? A HOH 963 ? 1_555 147.4 ? 
10 O ? P HOH .   ? A HOH 843 ? 1_555 NA ? H NA . ? A NA 707 ? 1_555 O ? P HOH .   ? A HOH 963 ? 1_555 85.2  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG B .   ? ASN A 188 ? NAG A 701 ? 1_555 ASN A 188 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG C .   ? ASN A 402 ? NAG A 702 ? 1_555 ASN A 402 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG G .   ? ASN A 295 ? NAG A 706 ? 1_555 ASN A 295 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 CYS A 236 ? CYS A 243 ? CYS A 236 ? 1_555 CYS A 243 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 3 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? 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 PHE A 30  ? TRP A 34  ? PHE A 30  TRP A 34  
AA1 2 PHE A 120 ? GLU A 126 ? PHE A 120 GLU A 126 
AA1 3 LYS A 166 ? MET A 171 ? LYS A 166 MET A 171 
AA1 4 ILE A 223 ? ASN A 226 ? ILE A 223 ASN A 226 
AA1 5 VAL A 269 ? LYS A 273 ? VAL A 269 LYS A 273 
AA1 6 VAL A 285 ? GLU A 289 ? VAL A 285 GLU A 289 
AA1 7 TRP A 301 ? ALA A 306 ? TRP A 301 ALA A 306 
AA1 8 GLY A 338 ? ILE A 344 ? GLY A 338 ILE A 344 
AA1 9 PHE A 30  ? TRP A 34  ? PHE A 30  TRP A 34  
AA2 1 ALA A 83  ? ASP A 84  ? ALA A 83  ASP A 84  
AA2 2 PHE A 90  ? VAL A 91  ? PHE A 90  VAL A 91  
AA3 1 GLY A 384 ? GLU A 385 ? GLY A 384 GLU A 385 
AA3 2 ILE A 406 ? ARG A 410 ? ILE A 406 ARG A 410 
AA3 3 VAL A 416 ? VAL A 421 ? VAL A 416 VAL A 421 
AA3 4 TYR A 486 ? PHE A 492 ? TYR A 486 PHE A 492 
AA3 5 LEU A 446 ? LEU A 452 ? LEU A 446 LEU A 452 
AA3 6 TYR A 459 ? GLN A 461 ? TYR A 459 GLN A 461 
AA4 1 HIS A 429 ? ILE A 432 ? HIS A 429 ILE A 432 
AA4 2 LEU A 472 ? SER A 475 ? LEU A 472 SER A 475 
AA4 3 ASP A 464 ? GLN A 467 ? ASP A 464 GLN A 467 
AA5 1 GLY A 517 ? LEU A 520 ? GLY A 517 LEU A 520 
AA5 2 ALA A 505 ? PHE A 508 ? ALA A 505 PHE A 508 
AA5 3 PHE A 542 ? VAL A 545 ? PHE A 542 VAL A 545 
AA5 4 GLY A 569 ? LYS A 572 ? GLY A 569 LYS A 572 
AA6 1 ASP A 524 ? PHE A 525 ? ASP A 524 PHE A 525 
AA6 2 SER A 580 ? SER A 584 ? SER A 580 SER A 584 
AA6 3 LYS A 550 ? TYR A 554 ? LYS A 550 TYR A 554 
AA6 4 SER A 563 ? LEU A 566 ? SER A 563 LEU A 566 
# 
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 VAL A 32  ? N VAL A 32  O PHE A 120 ? O PHE A 120 
AA1 2 3 N ALA A 121 ? N ALA A 121 O VAL A 168 ? O VAL A 168 
AA1 3 4 N MET A 171 ? N MET A 171 O TRP A 225 ? O TRP A 225 
AA1 4 5 N ILE A 224 ? N ILE A 224 O VAL A 269 ? O VAL A 269 
AA1 5 6 N HIS A 272 ? N HIS A 272 O ASP A 287 ? O ASP A 287 
AA1 6 7 N TYR A 288 ? N TYR A 288 O LEU A 302 ? O LEU A 302 
AA1 7 8 N THR A 303 ? N THR A 303 O LEU A 341 ? O LEU A 341 
AA1 8 9 O LEU A 342 ? O LEU A 342 N GLY A 31  ? N GLY A 31  
AA2 1 2 N ALA A 83  ? N ALA A 83  O VAL A 91  ? O VAL A 91  
AA3 1 2 N GLU A 385 ? N GLU A 385 O ILE A 406 ? O ILE A 406 
AA3 2 3 N THR A 409 ? N THR A 409 O TYR A 418 ? O TYR A 418 
AA3 3 4 N VAL A 421 ? N VAL A 421 O TYR A 486 ? O TYR A 486 
AA3 4 5 O THR A 491 ? O THR A 491 N SER A 448 ? N SER A 448 
AA3 5 6 N LEU A 451 ? N LEU A 451 O GLU A 460 ? O GLU A 460 
AA4 1 2 N ILE A 432 ? N ILE A 432 O LEU A 472 ? O LEU A 472 
AA4 2 3 O SER A 475 ? O SER A 475 N ASP A 464 ? N ASP A 464 
AA5 1 2 O LEU A 520 ? O LEU A 520 N ALA A 505 ? N ALA A 505 
AA5 2 3 N SER A 506 ? N SER A 506 O ARG A 544 ? O ARG A 544 
AA5 3 4 N ILE A 543 ? N ILE A 543 O HIS A 571 ? O HIS A 571 
AA6 1 2 N PHE A 525 ? N PHE A 525 O ILE A 581 ? O ILE A 581 
AA6 2 3 O THR A 582 ? O THR A 582 N THR A 552 ? N THR A 552 
AA6 3 4 N LEU A 551 ? N LEU A 551 O LEU A 566 ? O LEU A 566 
# 
_pdbx_entry_details.entry_id                   9LXL 
_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     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 O A HOH 835 ? ? O A HOH 982 ? ? 1.93 
2 1 O A HOH 851 ? ? O A HOH 961 ? ? 2.18 
# 
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 LYS A 29  ? ? 69.98   -57.21  
2 1 ALA A 45  ? ? 60.29   -118.20 
3 1 GLN A 220 ? ? 47.46   70.13   
4 1 ASP A 231 ? ? -156.25 65.59   
5 1 ALA A 237 ? ? 61.11   -128.69 
6 1 VAL A 374 ? ? -103.63 -62.15  
7 1 PRO A 480 ? ? -79.17  -163.91 
8 1 ASP A 567 ? ? -117.07 -161.13 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ARG 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    298 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    299 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            33.28 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -24.8380404831 30.1925764188 30.4498119878  0.826801663292 ? -0.0386336192122 ? -0.39109765309  ? 
0.207304160197 ? 0.0130946712045   ? 0.356163272029 ? 0.303565097811 ? -0.0502252102533 ? -0.0450866501676 ? 0.587971634907 ? 
0.0852828447564  ? 0.556089816641  ? -0.0251893178317  ? -0.0706710393227 ? 0.023952347741   ? 0.195201311758   ? 0.00214200146611 
? -0.171207377945  ? 0.111453942072   ? 0.094472755188   ? -0.187730917188  ? 
2 'X-RAY DIFFRACTION' ? refined -39.4245039889 29.5744218362 34.8420817646  0.996741231388 ? -0.0980180356504 ? -0.223251882691 ? 
0.252663357836 ? -0.0148214108867  ? 0.415631008397 ? 0.895222633486 ? -0.309598433741  ? -0.442830817752  ? 0.79300187419  ? 
0.92127041508    ? 2.59465492722   ? -0.133879496827   ? -0.0712693664769 ? 0.00217780755015 ? 0.53882868866    ? -0.0278848223276 
? 0.146708957537   ? 0.156465730278   ? -0.261927537383  ? 0.211541796954   ? 
3 'X-RAY DIFFRACTION' ? refined -27.2506678983 24.4803533622 39.2705215231  1.02784987058  ? -0.0940594165769 ? -0.410588307156 ? 
0.226436947291 ? -0.00932048111824 ? 0.371080596734 ? 0.013794723459 ? -0.0283115660395 ? 0.0519952996356  ? 0.204070955584 ? 
0.0732886035417  ? 0.289684786381  ? 0.00440731899124  ? -0.0526838523035 ? 0.0220083888068  ? 0.238891800166   ? -0.0370097655633 
? -0.081051540593  ? 0.0533194203415  ? -0.0199316988261 ? -0.0740127998349 ? 
4 'X-RAY DIFFRACTION' ? refined -14.5439598215 24.4429870155 31.0245404456  0.921293178604 ? -0.040329046362  ? -0.409897553468 ? 
0.142687467508 ? 0.00357734164201  ? 0.480837702359 ? 0.100982127218 ? -0.110498266044  ? -0.0354444548337 ? 0.22325368088  ? 
-0.0284729474348 ? 0.0763942635388 ? -0.00505074605708 ? -0.02813138351   ? 0.0321732536962  ? 0.0686027071277  ? 0.0307067864011  
? -0.0826505881619 ? -0.0200802410851 ? 0.016135019175   ? 0.0961497369645  ? 
5 'X-RAY DIFFRACTION' ? refined -26.2065608944 32.6386890862 12.0105939907  0.543993298415 ? 0.00202115524309 ? -0.346740716861 ? 
0.126104193869 ? 0.103027364202    ? 0.252971431662 ? 0.415943986444 ? -0.273351766246  ? 0.147337197823   ? 0.334895538487 ? 
-0.194363817764  ? 0.250890288229  ? 0.00683156549366  ? 0.0773846528791  ? 0.133787503459   ? 0.0844212014227  ? -0.0598385818751 
? -0.094348105044  ? 0.0341912733128  ? 0.0304780462836  ? 0.0207518427267  ? 
6 'X-RAY DIFFRACTION' ? refined -20.9517143443 27.9249696342 -10.3121398588 0.673211954912 ? 0.145605991445   ? -0.167968719256 ? 
0.540615294069 ? 0.0842811454277   ? 0.331333433968 ? 3.07550155928  ? -1.24848368206   ? -0.297710192574  ? 1.53395210071  ? 
-0.214042997404  ? 1.59378486298   ? 0.248484254067    ? 0.820119533026   ? 0.115725593026   ? -0.42896656133   ? -0.255996121993  
? -0.273620512233  ? 0.593463908038   ? 0.217976441827   ? 0.0076232405329  ? 
7 'X-RAY DIFFRACTION' ? refined -20.8896635141 27.9782761558 -6.54647814886 0.648431834785 ? 0.0107944215435  ? -0.212722142058 ? 
0.440140506991 ? 0.142342369634    ? 0.338242940155 ? 1.69653028773  ? 0.820391619698   ? -0.855418541051  ? 1.06412242785  ? 
0.512581725578   ? 2.8610053108    ? 0.152652008425    ? 0.545416475405   ? 0.0746206076674  ? -0.0748045109621 ? -0.229800281828  
? -0.292877385782  ? 0.23707439117    ? 0.046098392837   ? 0.0725736795752  ? 
8 'X-RAY DIFFRACTION' ? refined -0.59193859012 24.6524551614 3.07379570206  0.670555886307 ? 0.275813588606   ? -0.223246723355 ? 
0.717310439534 ? -0.017651201936   ? 0.957519309794 ? 6.70881083444  ? 1.08565788997    ? -0.995756090567  ? 1.87535859177  ? 
-2.80850848958   ? 7.84939075375   ? -0.136067487372   ? -0.31825205879   ? -0.829902878071  ? 0.300893488692   ? -0.0962741888087 
? -1.3989436696    ? 1.18111075754    ? 1.66192783884    ? 0.242657535182   ? 
9 'X-RAY DIFFRACTION' ? refined 6.86170408503  31.2686818318 3.37233802414  0.638688932486 ? 0.117123251709   ? -0.223767998272 ? 
1.5635918103   ? 0.145312016882    ? 1.10787383713  ? 4.6179859524   ? -1.10448110302   ? 0.490880973575   ? 4.78601568314  ? 
0.49949558936    ? 2.31219536706   ? 0.11982927997     ? -0.504674710081  ? -0.153799453506  ? 0.591789780492   ? -0.0732055600891 
? -1.37607740327   ? 0.244718292924   ? 1.46636884247    ? -0.0482357600826 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 3   ? A 65  A 67  ? ? 
;chain 'A' and (resid 3 through 67 )
;
2 'X-RAY DIFFRACTION' 2 A 66  A 68  ? A 131 A 133 ? ? 
;chain 'A' and (resid 68 through 133 )
;
3 'X-RAY DIFFRACTION' 3 A 132 A 134 ? A 217 A 219 ? ? 
;chain 'A' and (resid 134 through 219 )
;
4 'X-RAY DIFFRACTION' 4 A 218 A 220 ? A 282 A 284 ? ? 
;chain 'A' and (resid 220 through 284 )
;
5 'X-RAY DIFFRACTION' 5 A 283 A 285 ? A 408 A 410 ? ? 
;chain 'A' and (resid 285 through 410 )
;
6 'X-RAY DIFFRACTION' 6 A 409 A 411 ? A 473 A 475 ? ? 
;chain 'A' and (resid 411 through 475 )
;
7 'X-RAY DIFFRACTION' 7 A 474 A 476 ? A 502 A 504 ? ? 
;chain 'A' and (resid 476 through 504 )
;
8 'X-RAY DIFFRACTION' 8 A 503 A 505 ? A 539 A 541 ? ? 
;chain 'A' and (resid 505 through 541 )
;
9 'X-RAY DIFFRACTION' 9 A 540 A 542 ? A 583 A 585 ? ? 
;chain 'A' and (resid 542 through 585 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1034 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.84 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 GLU 1   ? A GLU 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A ALA 586 ? A ALA 586 
4  1 Y 1 A GLU 587 ? A GLU 587 
5  1 Y 1 A ASN 588 ? A ASN 588 
6  1 Y 1 A LEU 589 ? A LEU 589 
7  1 Y 1 A TYR 590 ? A TYR 590 
8  1 Y 1 A PHE 591 ? A PHE 591 
9  1 Y 1 A GLN 592 ? A GLN 592 
10 1 Y 1 A SER 593 ? A SER 593 
11 1 Y 1 A ALA 594 ? A ALA 594 
12 1 Y 1 A ALA 595 ? A ALA 595 
13 1 Y 1 A ALA 596 ? A ALA 596 
14 1 Y 1 A SER 597 ? A SER 597 
15 1 Y 1 A PHE 598 ? A PHE 598 
16 1 Y 1 A LEU 599 ? A LEU 599 
17 1 Y 1 A GLU 600 ? A GLU 600 
18 1 Y 1 A GLN 601 ? A GLN 601 
19 1 Y 1 A LYS 602 ? A LYS 602 
20 1 Y 1 A LEU 603 ? A LEU 603 
21 1 Y 1 A ILE 604 ? A ILE 604 
22 1 Y 1 A SER 605 ? A SER 605 
23 1 Y 1 A GLU 606 ? A GLU 606 
24 1 Y 1 A GLU 607 ? A GLU 607 
25 1 Y 1 A ASP 608 ? A ASP 608 
26 1 Y 1 A LEU 609 ? A LEU 609 
27 1 Y 1 A ASN 610 ? A ASN 610 
28 1 Y 1 A SER 611 ? A SER 611 
29 1 Y 1 A ALA 612 ? A ALA 612 
30 1 Y 1 A VAL 613 ? A VAL 613 
31 1 Y 1 A ASP 614 ? A ASP 614 
32 1 Y 1 A HIS 615 ? A HIS 615 
33 1 Y 1 A HIS 616 ? A HIS 616 
34 1 Y 1 A HIS 617 ? A HIS 617 
35 1 Y 1 A HIS 618 ? A HIS 618 
36 1 Y 1 A HIS 619 ? A HIS 619 
37 1 Y 1 A HIS 620 ? A HIS 620 
# 
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 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ARG N    N  N N 21  
ARG CA   C  N S 22  
ARG C    C  N N 23  
ARG O    O  N N 24  
ARG CB   C  N N 25  
ARG CG   C  N N 26  
ARG CD   C  N N 27  
ARG NE   N  N N 28  
ARG CZ   C  N N 29  
ARG NH1  N  N N 30  
ARG NH2  N  N N 31  
ARG OXT  O  N N 32  
ARG H    H  N N 33  
ARG H2   H  N N 34  
ARG HA   H  N N 35  
ARG HB2  H  N N 36  
ARG HB3  H  N N 37  
ARG HG2  H  N N 38  
ARG HG3  H  N N 39  
ARG HD2  H  N N 40  
ARG HD3  H  N N 41  
ARG HE   H  N N 42  
ARG HH11 H  N N 43  
ARG HH12 H  N N 44  
ARG HH21 H  N N 45  
ARG HH22 H  N N 46  
ARG HXT  H  N N 47  
ASN N    N  N N 48  
ASN CA   C  N S 49  
ASN C    C  N N 50  
ASN O    O  N N 51  
ASN CB   C  N N 52  
ASN CG   C  N N 53  
ASN OD1  O  N N 54  
ASN ND2  N  N N 55  
ASN OXT  O  N N 56  
ASN H    H  N N 57  
ASN H2   H  N N 58  
ASN HA   H  N N 59  
ASN HB2  H  N N 60  
ASN HB3  H  N N 61  
ASN HD21 H  N N 62  
ASN HD22 H  N N 63  
ASN HXT  H  N N 64  
ASP N    N  N N 65  
ASP CA   C  N S 66  
ASP C    C  N N 67  
ASP O    O  N N 68  
ASP CB   C  N N 69  
ASP CG   C  N N 70  
ASP OD1  O  N N 71  
ASP OD2  O  N N 72  
ASP OXT  O  N N 73  
ASP H    H  N N 74  
ASP H2   H  N N 75  
ASP HA   H  N N 76  
ASP HB2  H  N N 77  
ASP HB3  H  N N 78  
ASP HD2  H  N N 79  
ASP HXT  H  N N 80  
AZI N1   N  N N 81  
AZI N2   N  N N 82  
AZI N3   N  N N 83  
CYS N    N  N N 84  
CYS CA   C  N R 85  
CYS C    C  N N 86  
CYS O    O  N N 87  
CYS CB   C  N N 88  
CYS SG   S  N N 89  
CYS OXT  O  N N 90  
CYS H    H  N N 91  
CYS H2   H  N N 92  
CYS HA   H  N N 93  
CYS HB2  H  N N 94  
CYS HB3  H  N N 95  
CYS HG   H  N N 96  
CYS HXT  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
MPD C1   C  N N 260 
MPD C2   C  N N 261 
MPD O2   O  N N 262 
MPD CM   C  N N 263 
MPD C3   C  N N 264 
MPD C4   C  N S 265 
MPD O4   O  N N 266 
MPD C5   C  N N 267 
MPD H11  H  N N 268 
MPD H12  H  N N 269 
MPD H13  H  N N 270 
MPD HO2  H  N N 271 
MPD HM1  H  N N 272 
MPD HM2  H  N N 273 
MPD HM3  H  N N 274 
MPD H31  H  N N 275 
MPD H32  H  N N 276 
MPD H4   H  N N 277 
MPD HO4  H  N N 278 
MPD H51  H  N N 279 
MPD H52  H  N N 280 
MPD H53  H  N N 281 
NA  NA   NA N N 282 
NAG C1   C  N R 283 
NAG C2   C  N R 284 
NAG C3   C  N R 285 
NAG C4   C  N S 286 
NAG C5   C  N R 287 
NAG C6   C  N N 288 
NAG C7   C  N N 289 
NAG C8   C  N N 290 
NAG N2   N  N N 291 
NAG O1   O  N N 292 
NAG O3   O  N N 293 
NAG O4   O  N N 294 
NAG O5   O  N N 295 
NAG O6   O  N N 296 
NAG O7   O  N N 297 
NAG H1   H  N N 298 
NAG H2   H  N N 299 
NAG H3   H  N N 300 
NAG H4   H  N N 301 
NAG H5   H  N N 302 
NAG H61  H  N N 303 
NAG H62  H  N N 304 
NAG H81  H  N N 305 
NAG H82  H  N N 306 
NAG H83  H  N N 307 
NAG HN2  H  N N 308 
NAG HO1  H  N N 309 
NAG HO3  H  N N 310 
NAG HO4  H  N N 311 
NAG HO6  H  N N 312 
PHE N    N  N N 313 
PHE CA   C  N S 314 
PHE C    C  N N 315 
PHE O    O  N N 316 
PHE CB   C  N N 317 
PHE CG   C  Y N 318 
PHE CD1  C  Y N 319 
PHE CD2  C  Y N 320 
PHE CE1  C  Y N 321 
PHE CE2  C  Y N 322 
PHE CZ   C  Y N 323 
PHE OXT  O  N N 324 
PHE H    H  N N 325 
PHE H2   H  N N 326 
PHE HA   H  N N 327 
PHE HB2  H  N N 328 
PHE HB3  H  N N 329 
PHE HD1  H  N N 330 
PHE HD2  H  N N 331 
PHE HE1  H  N N 332 
PHE HE2  H  N N 333 
PHE HZ   H  N N 334 
PHE HXT  H  N N 335 
PRO N    N  N N 336 
PRO CA   C  N S 337 
PRO C    C  N N 338 
PRO O    O  N N 339 
PRO CB   C  N N 340 
PRO CG   C  N N 341 
PRO CD   C  N N 342 
PRO OXT  O  N N 343 
PRO H    H  N N 344 
PRO HA   H  N N 345 
PRO HB2  H  N N 346 
PRO HB3  H  N N 347 
PRO HG2  H  N N 348 
PRO HG3  H  N N 349 
PRO HD2  H  N N 350 
PRO HD3  H  N N 351 
PRO HXT  H  N N 352 
SER N    N  N N 353 
SER CA   C  N S 354 
SER C    C  N N 355 
SER O    O  N N 356 
SER CB   C  N N 357 
SER OG   O  N N 358 
SER OXT  O  N N 359 
SER H    H  N N 360 
SER H2   H  N N 361 
SER HA   H  N N 362 
SER HB2  H  N N 363 
SER HB3  H  N N 364 
SER HG   H  N N 365 
SER HXT  H  N N 366 
THR N    N  N N 367 
THR CA   C  N S 368 
THR C    C  N N 369 
THR O    O  N N 370 
THR CB   C  N R 371 
THR OG1  O  N N 372 
THR CG2  C  N N 373 
THR OXT  O  N N 374 
THR H    H  N N 375 
THR H2   H  N N 376 
THR HA   H  N N 377 
THR HB   H  N N 378 
THR HG1  H  N N 379 
THR HG21 H  N N 380 
THR HG22 H  N N 381 
THR HG23 H  N N 382 
THR HXT  H  N N 383 
TRP N    N  N N 384 
TRP CA   C  N S 385 
TRP C    C  N N 386 
TRP O    O  N N 387 
TRP CB   C  N N 388 
TRP CG   C  Y N 389 
TRP CD1  C  Y N 390 
TRP CD2  C  Y N 391 
TRP NE1  N  Y N 392 
TRP CE2  C  Y N 393 
TRP CE3  C  Y N 394 
TRP CZ2  C  Y N 395 
TRP CZ3  C  Y N 396 
TRP CH2  C  Y N 397 
TRP OXT  O  N N 398 
TRP H    H  N N 399 
TRP H2   H  N N 400 
TRP HA   H  N N 401 
TRP HB2  H  N N 402 
TRP HB3  H  N N 403 
TRP HD1  H  N N 404 
TRP HE1  H  N N 405 
TRP HE3  H  N N 406 
TRP HZ2  H  N N 407 
TRP HZ3  H  N N 408 
TRP HH2  H  N N 409 
TRP HXT  H  N N 410 
TRS C    C  N N 411 
TRS C1   C  N N 412 
TRS C2   C  N N 413 
TRS C3   C  N N 414 
TRS N    N  N N 415 
TRS O1   O  N N 416 
TRS O2   O  N N 417 
TRS O3   O  N N 418 
TRS H11  H  N N 419 
TRS H12  H  N N 420 
TRS H21  H  N N 421 
TRS H22  H  N N 422 
TRS H31  H  N N 423 
TRS H32  H  N N 424 
TRS HN1  H  N N 425 
TRS HN2  H  N N 426 
TRS HN3  H  N N 427 
TRS HO1  H  N N 428 
TRS HO2  H  N N 429 
TRS HO3  H  N N 430 
TYR N    N  N N 431 
TYR CA   C  N S 432 
TYR C    C  N N 433 
TYR O    O  N N 434 
TYR CB   C  N N 435 
TYR CG   C  Y N 436 
TYR CD1  C  Y N 437 
TYR CD2  C  Y N 438 
TYR CE1  C  Y N 439 
TYR CE2  C  Y N 440 
TYR CZ   C  Y N 441 
TYR OH   O  N N 442 
TYR OXT  O  N N 443 
TYR H    H  N N 444 
TYR H2   H  N N 445 
TYR HA   H  N N 446 
TYR HB2  H  N N 447 
TYR HB3  H  N N 448 
TYR HD1  H  N N 449 
TYR HD2  H  N N 450 
TYR HE1  H  N N 451 
TYR HE2  H  N N 452 
TYR HH   H  N N 453 
TYR HXT  H  N N 454 
VAL N    N  N N 455 
VAL CA   C  N S 456 
VAL C    C  N N 457 
VAL O    O  N N 458 
VAL CB   C  N N 459 
VAL CG1  C  N N 460 
VAL CG2  C  N N 461 
VAL OXT  O  N N 462 
VAL H    H  N N 463 
VAL H2   H  N N 464 
VAL HA   H  N N 465 
VAL HB   H  N N 466 
VAL HG11 H  N N 467 
VAL HG12 H  N N 468 
VAL HG13 H  N N 469 
VAL HG21 H  N N 470 
VAL HG22 H  N N 471 
VAL HG23 H  N N 472 
VAL HXT  H  N N 473 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
AZI N1  N2   doub N N 76  
AZI N2  N3   doub N N 77  
CYS N   CA   sing N N 78  
CYS N   H    sing N N 79  
CYS N   H2   sing N N 80  
CYS CA  C    sing N N 81  
CYS CA  CB   sing N N 82  
CYS CA  HA   sing N N 83  
CYS C   O    doub N N 84  
CYS C   OXT  sing N N 85  
CYS CB  SG   sing N N 86  
CYS CB  HB2  sing N N 87  
CYS CB  HB3  sing N N 88  
CYS SG  HG   sing N N 89  
CYS OXT HXT  sing N N 90  
GLN N   CA   sing N N 91  
GLN N   H    sing N N 92  
GLN N   H2   sing N N 93  
GLN CA  C    sing N N 94  
GLN CA  CB   sing N N 95  
GLN CA  HA   sing N N 96  
GLN C   O    doub N N 97  
GLN C   OXT  sing N N 98  
GLN CB  CG   sing N N 99  
GLN CB  HB2  sing N N 100 
GLN CB  HB3  sing N N 101 
GLN CG  CD   sing N N 102 
GLN CG  HG2  sing N N 103 
GLN CG  HG3  sing N N 104 
GLN CD  OE1  doub N N 105 
GLN CD  NE2  sing N N 106 
GLN NE2 HE21 sing N N 107 
GLN NE2 HE22 sing N N 108 
GLN OXT HXT  sing N N 109 
GLU N   CA   sing N N 110 
GLU N   H    sing N N 111 
GLU N   H2   sing N N 112 
GLU CA  C    sing N N 113 
GLU CA  CB   sing N N 114 
GLU CA  HA   sing N N 115 
GLU C   O    doub N N 116 
GLU C   OXT  sing N N 117 
GLU CB  CG   sing N N 118 
GLU CB  HB2  sing N N 119 
GLU CB  HB3  sing N N 120 
GLU CG  CD   sing N N 121 
GLU CG  HG2  sing N N 122 
GLU CG  HG3  sing N N 123 
GLU CD  OE1  doub N N 124 
GLU CD  OE2  sing N N 125 
GLU OE2 HE2  sing N N 126 
GLU OXT HXT  sing N N 127 
GLY N   CA   sing N N 128 
GLY N   H    sing N N 129 
GLY N   H2   sing N N 130 
GLY CA  C    sing N N 131 
GLY CA  HA2  sing N N 132 
GLY CA  HA3  sing N N 133 
GLY C   O    doub N N 134 
GLY C   OXT  sing N N 135 
GLY OXT HXT  sing N N 136 
HIS N   CA   sing N N 137 
HIS N   H    sing N N 138 
HIS N   H2   sing N N 139 
HIS CA  C    sing N N 140 
HIS CA  CB   sing N N 141 
HIS CA  HA   sing N N 142 
HIS C   O    doub N N 143 
HIS C   OXT  sing N N 144 
HIS CB  CG   sing N N 145 
HIS CB  HB2  sing N N 146 
HIS CB  HB3  sing N N 147 
HIS CG  ND1  sing Y N 148 
HIS CG  CD2  doub Y N 149 
HIS ND1 CE1  doub Y N 150 
HIS ND1 HD1  sing N N 151 
HIS CD2 NE2  sing Y N 152 
HIS CD2 HD2  sing N N 153 
HIS CE1 NE2  sing Y N 154 
HIS CE1 HE1  sing N N 155 
HIS NE2 HE2  sing N N 156 
HIS OXT HXT  sing N N 157 
HOH O   H1   sing N N 158 
HOH O   H2   sing N N 159 
ILE N   CA   sing N N 160 
ILE N   H    sing N N 161 
ILE N   H2   sing N N 162 
ILE CA  C    sing N N 163 
ILE CA  CB   sing N N 164 
ILE CA  HA   sing N N 165 
ILE C   O    doub N N 166 
ILE C   OXT  sing N N 167 
ILE CB  CG1  sing N N 168 
ILE CB  CG2  sing N N 169 
ILE CB  HB   sing N N 170 
ILE CG1 CD1  sing N N 171 
ILE CG1 HG12 sing N N 172 
ILE CG1 HG13 sing N N 173 
ILE CG2 HG21 sing N N 174 
ILE CG2 HG22 sing N N 175 
ILE CG2 HG23 sing N N 176 
ILE CD1 HD11 sing N N 177 
ILE CD1 HD12 sing N N 178 
ILE CD1 HD13 sing N N 179 
ILE OXT HXT  sing N N 180 
LEU N   CA   sing N N 181 
LEU N   H    sing N N 182 
LEU N   H2   sing N N 183 
LEU CA  C    sing N N 184 
LEU CA  CB   sing N N 185 
LEU CA  HA   sing N N 186 
LEU C   O    doub N N 187 
LEU C   OXT  sing N N 188 
LEU CB  CG   sing N N 189 
LEU CB  HB2  sing N N 190 
LEU CB  HB3  sing N N 191 
LEU CG  CD1  sing N N 192 
LEU CG  CD2  sing N N 193 
LEU CG  HG   sing N N 194 
LEU CD1 HD11 sing N N 195 
LEU CD1 HD12 sing N N 196 
LEU CD1 HD13 sing N N 197 
LEU CD2 HD21 sing N N 198 
LEU CD2 HD22 sing N N 199 
LEU CD2 HD23 sing N N 200 
LEU OXT HXT  sing N N 201 
LYS N   CA   sing N N 202 
LYS N   H    sing N N 203 
LYS N   H2   sing N N 204 
LYS CA  C    sing N N 205 
LYS CA  CB   sing N N 206 
LYS CA  HA   sing N N 207 
LYS C   O    doub N N 208 
LYS C   OXT  sing N N 209 
LYS CB  CG   sing N N 210 
LYS CB  HB2  sing N N 211 
LYS CB  HB3  sing N N 212 
LYS CG  CD   sing N N 213 
LYS CG  HG2  sing N N 214 
LYS CG  HG3  sing N N 215 
LYS CD  CE   sing N N 216 
LYS CD  HD2  sing N N 217 
LYS CD  HD3  sing N N 218 
LYS CE  NZ   sing N N 219 
LYS CE  HE2  sing N N 220 
LYS CE  HE3  sing N N 221 
LYS NZ  HZ1  sing N N 222 
LYS NZ  HZ2  sing N N 223 
LYS NZ  HZ3  sing N N 224 
LYS OXT HXT  sing N N 225 
MET N   CA   sing N N 226 
MET N   H    sing N N 227 
MET N   H2   sing N N 228 
MET CA  C    sing N N 229 
MET CA  CB   sing N N 230 
MET CA  HA   sing N N 231 
MET C   O    doub N N 232 
MET C   OXT  sing N N 233 
MET CB  CG   sing N N 234 
MET CB  HB2  sing N N 235 
MET CB  HB3  sing N N 236 
MET CG  SD   sing N N 237 
MET CG  HG2  sing N N 238 
MET CG  HG3  sing N N 239 
MET SD  CE   sing N N 240 
MET CE  HE1  sing N N 241 
MET CE  HE2  sing N N 242 
MET CE  HE3  sing N N 243 
MET OXT HXT  sing N N 244 
MPD C1  C2   sing N N 245 
MPD C1  H11  sing N N 246 
MPD C1  H12  sing N N 247 
MPD C1  H13  sing N N 248 
MPD C2  O2   sing N N 249 
MPD C2  CM   sing N N 250 
MPD C2  C3   sing N N 251 
MPD O2  HO2  sing N N 252 
MPD CM  HM1  sing N N 253 
MPD CM  HM2  sing N N 254 
MPD CM  HM3  sing N N 255 
MPD C3  C4   sing N N 256 
MPD C3  H31  sing N N 257 
MPD C3  H32  sing N N 258 
MPD C4  O4   sing N N 259 
MPD C4  C5   sing N N 260 
MPD C4  H4   sing N N 261 
MPD O4  HO4  sing N N 262 
MPD C5  H51  sing N N 263 
MPD C5  H52  sing N N 264 
MPD C5  H53  sing N N 265 
NAG C1  C2   sing N N 266 
NAG C1  O1   sing N N 267 
NAG C1  O5   sing N N 268 
NAG C1  H1   sing N N 269 
NAG C2  C3   sing N N 270 
NAG C2  N2   sing N N 271 
NAG C2  H2   sing N N 272 
NAG C3  C4   sing N N 273 
NAG C3  O3   sing N N 274 
NAG C3  H3   sing N N 275 
NAG C4  C5   sing N N 276 
NAG C4  O4   sing N N 277 
NAG C4  H4   sing N N 278 
NAG C5  C6   sing N N 279 
NAG C5  O5   sing N N 280 
NAG C5  H5   sing N N 281 
NAG C6  O6   sing N N 282 
NAG C6  H61  sing N N 283 
NAG C6  H62  sing N N 284 
NAG C7  C8   sing N N 285 
NAG C7  N2   sing N N 286 
NAG C7  O7   doub N N 287 
NAG C8  H81  sing N N 288 
NAG C8  H82  sing N N 289 
NAG C8  H83  sing N N 290 
NAG N2  HN2  sing N N 291 
NAG O1  HO1  sing N N 292 
NAG O3  HO3  sing N N 293 
NAG O4  HO4  sing N N 294 
NAG O6  HO6  sing N N 295 
PHE N   CA   sing N N 296 
PHE N   H    sing N N 297 
PHE N   H2   sing N N 298 
PHE CA  C    sing N N 299 
PHE CA  CB   sing N N 300 
PHE CA  HA   sing N N 301 
PHE C   O    doub N N 302 
PHE C   OXT  sing N N 303 
PHE CB  CG   sing N N 304 
PHE CB  HB2  sing N N 305 
PHE CB  HB3  sing N N 306 
PHE CG  CD1  doub Y N 307 
PHE CG  CD2  sing Y N 308 
PHE CD1 CE1  sing Y N 309 
PHE CD1 HD1  sing N N 310 
PHE CD2 CE2  doub Y N 311 
PHE CD2 HD2  sing N N 312 
PHE CE1 CZ   doub Y N 313 
PHE CE1 HE1  sing N N 314 
PHE CE2 CZ   sing Y N 315 
PHE CE2 HE2  sing N N 316 
PHE CZ  HZ   sing N N 317 
PHE OXT HXT  sing N N 318 
PRO N   CA   sing N N 319 
PRO N   CD   sing N N 320 
PRO N   H    sing N N 321 
PRO CA  C    sing N N 322 
PRO CA  CB   sing N N 323 
PRO CA  HA   sing N N 324 
PRO C   O    doub N N 325 
PRO C   OXT  sing N N 326 
PRO CB  CG   sing N N 327 
PRO CB  HB2  sing N N 328 
PRO CB  HB3  sing N N 329 
PRO CG  CD   sing N N 330 
PRO CG  HG2  sing N N 331 
PRO CG  HG3  sing N N 332 
PRO CD  HD2  sing N N 333 
PRO CD  HD3  sing N N 334 
PRO OXT HXT  sing N N 335 
SER N   CA   sing N N 336 
SER N   H    sing N N 337 
SER N   H2   sing N N 338 
SER CA  C    sing N N 339 
SER CA  CB   sing N N 340 
SER CA  HA   sing N N 341 
SER C   O    doub N N 342 
SER C   OXT  sing N N 343 
SER CB  OG   sing N N 344 
SER CB  HB2  sing N N 345 
SER CB  HB3  sing N N 346 
SER OG  HG   sing N N 347 
SER OXT HXT  sing N N 348 
THR N   CA   sing N N 349 
THR N   H    sing N N 350 
THR N   H2   sing N N 351 
THR CA  C    sing N N 352 
THR CA  CB   sing N N 353 
THR CA  HA   sing N N 354 
THR C   O    doub N N 355 
THR C   OXT  sing N N 356 
THR CB  OG1  sing N N 357 
THR CB  CG2  sing N N 358 
THR CB  HB   sing N N 359 
THR OG1 HG1  sing N N 360 
THR CG2 HG21 sing N N 361 
THR CG2 HG22 sing N N 362 
THR CG2 HG23 sing N N 363 
THR OXT HXT  sing N N 364 
TRP N   CA   sing N N 365 
TRP N   H    sing N N 366 
TRP N   H2   sing N N 367 
TRP CA  C    sing N N 368 
TRP CA  CB   sing N N 369 
TRP CA  HA   sing N N 370 
TRP C   O    doub N N 371 
TRP C   OXT  sing N N 372 
TRP CB  CG   sing N N 373 
TRP CB  HB2  sing N N 374 
TRP CB  HB3  sing N N 375 
TRP CG  CD1  doub Y N 376 
TRP CG  CD2  sing Y N 377 
TRP CD1 NE1  sing Y N 378 
TRP CD1 HD1  sing N N 379 
TRP CD2 CE2  doub Y N 380 
TRP CD2 CE3  sing Y N 381 
TRP NE1 CE2  sing Y N 382 
TRP NE1 HE1  sing N N 383 
TRP CE2 CZ2  sing Y N 384 
TRP CE3 CZ3  doub Y N 385 
TRP CE3 HE3  sing N N 386 
TRP CZ2 CH2  doub Y N 387 
TRP CZ2 HZ2  sing N N 388 
TRP CZ3 CH2  sing Y N 389 
TRP CZ3 HZ3  sing N N 390 
TRP CH2 HH2  sing N N 391 
TRP OXT HXT  sing N N 392 
TRS C   C1   sing N N 393 
TRS C   C2   sing N N 394 
TRS C   C3   sing N N 395 
TRS C   N    sing N N 396 
TRS C1  O1   sing N N 397 
TRS C1  H11  sing N N 398 
TRS C1  H12  sing N N 399 
TRS C2  O2   sing N N 400 
TRS C2  H21  sing N N 401 
TRS C2  H22  sing N N 402 
TRS C3  O3   sing N N 403 
TRS C3  H31  sing N N 404 
TRS C3  H32  sing N N 405 
TRS N   HN1  sing N N 406 
TRS N   HN2  sing N N 407 
TRS N   HN3  sing N N 408 
TRS O1  HO1  sing N N 409 
TRS O2  HO2  sing N N 410 
TRS O3  HO3  sing N N 411 
TYR N   CA   sing N N 412 
TYR N   H    sing N N 413 
TYR N   H2   sing N N 414 
TYR CA  C    sing N N 415 
TYR CA  CB   sing N N 416 
TYR CA  HA   sing N N 417 
TYR C   O    doub N N 418 
TYR C   OXT  sing N N 419 
TYR CB  CG   sing N N 420 
TYR CB  HB2  sing N N 421 
TYR CB  HB3  sing N N 422 
TYR CG  CD1  doub Y N 423 
TYR CG  CD2  sing Y N 424 
TYR CD1 CE1  sing Y N 425 
TYR CD1 HD1  sing N N 426 
TYR CD2 CE2  doub Y N 427 
TYR CD2 HD2  sing N N 428 
TYR CE1 CZ   doub Y N 429 
TYR CE1 HE1  sing N N 430 
TYR CE2 CZ   sing Y N 431 
TYR CE2 HE2  sing N N 432 
TYR CZ  OH   sing N N 433 
TYR OH  HH   sing N N 434 
TYR OXT HXT  sing N N 435 
VAL N   CA   sing N N 436 
VAL N   H    sing N N 437 
VAL N   H2   sing N N 438 
VAL CA  C    sing N N 439 
VAL CA  CB   sing N N 440 
VAL CA  HA   sing N N 441 
VAL C   O    doub N N 442 
VAL C   OXT  sing N N 443 
VAL CB  CG1  sing N N 444 
VAL CB  CG2  sing N N 445 
VAL CB  HB   sing N N 446 
VAL CG1 HG11 sing N N 447 
VAL CG1 HG12 sing N N 448 
VAL CG1 HG13 sing N N 449 
VAL CG2 HG21 sing N N 450 
VAL CG2 HG22 sing N N 451 
VAL CG2 HG23 sing N N 452 
VAL OXT HXT  sing N N 453 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Higher Education of the Russian Federation' 
_pdbx_audit_support.country                'Russian Federation' 
_pdbx_audit_support.grant_number           1023031500033-1-1.6.7;1.6.4;1.6.8 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_related_exp_data_set.data_reference       10.5281/zenodo.15005358 
_pdbx_related_exp_data_set.data_set_type        'diffraction image data' 
_pdbx_related_exp_data_set.details              ? 
_pdbx_related_exp_data_set.metadata_reference   ? 
_pdbx_related_exp_data_set.ordinal              1 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9LXL 
_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]   0.013028 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013028 
_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]   0.004438 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLN A 1 3   ? -12.92900 11.45300 40.57000  1.000 87.68642  ? 3    GLN A N   1 
ATOM   2    C  CA  . GLN A 1 3   ? -12.31700 11.01300 39.28900  1.000 83.96800  ? 3    GLN A CA  1 
ATOM   3    C  C   . GLN A 1 3   ? -13.19200 9.91400  38.66300  1.000 90.42980  ? 3    GLN A C   1 
ATOM   4    O  O   . GLN A 1 3   ? -13.94400 9.26500  39.40900  1.000 94.09545  ? 3    GLN A O   1 
ATOM   5    C  CB  . GLN A 1 3   ? -10.89400 10.54400 39.57200  1.000 83.62607  ? 3    GLN A CB  1 
ATOM   6    C  CG  . GLN A 1 3   ? -10.14100 11.48300 40.49900  1.000 83.49539  ? 3    GLN A CG  1 
ATOM   7    C  CD  . GLN A 1 3   ? -8.76700  10.97400 40.85300  1.000 86.74032  ? 3    GLN A CD  1 
ATOM   8    O  OE1 . GLN A 1 3   ? -8.31300  9.95200  40.34700  1.000 86.37383  ? 3    GLN A OE1 1 
ATOM   9    N  NE2 . GLN A 1 3   ? -8.09200  11.69300 41.73400  1.000 96.94848  ? 3    GLN A NE2 1 
ATOM   10   N  N   . ALA A 1 4   ? -13.08500 9.72400  37.34800  1.000 79.42915  ? 4    ALA A N   1 
ATOM   11   C  CA  . ALA A 1 4   ? -13.83000 8.66300  36.63900  1.000 65.08231  ? 4    ALA A CA  1 
ATOM   12   C  C   . ALA A 1 4   ? -12.83900 7.91300  35.76200  1.000 62.45631  ? 4    ALA A C   1 
ATOM   13   O  O   . ALA A 1 4   ? -11.92200 8.55300  35.22800  1.000 47.98982  ? 4    ALA A O   1 
ATOM   14   C  CB  . ALA A 1 4   ? -14.92800 9.27600  35.83300  1.000 61.87428  ? 4    ALA A CB  1 
ATOM   15   N  N   . SER A 1 5   ? -12.99800 6.58900  35.67000  1.000 65.53075  ? 5    SER A N   1 
ATOM   16   C  CA  . SER A 1 5   ? -11.99000 5.80400  34.91300  1.000 54.53753  ? 5    SER A CA  1 
ATOM   17   C  C   . SER A 1 5   ? -11.87300 6.35300  33.49000  1.000 54.69613  ? 5    SER A C   1 
ATOM   18   O  O   . SER A 1 5   ? -12.89800 6.55400  32.83700  1.000 51.42942  ? 5    SER A O   1 
ATOM   19   C  CB  . SER A 1 5   ? -12.23400 4.30900  34.95000  1.000 49.19079  ? 5    SER A CB  1 
ATOM   20   O  OG  . SER A 1 5   ? -11.22400 3.62700  34.22800  1.000 55.35499  ? 5    SER A OG  1 
ATOM   21   N  N   . GLY A 1 6   ? -10.65300 6.63300  33.08000  1.000 48.15221  ? 6    GLY A N   1 
ATOM   22   C  CA  . GLY A 1 6   ? -10.39800 7.13200  31.73500  1.000 47.65798  ? 6    GLY A CA  1 
ATOM   23   C  C   . GLY A 1 6   ? -8.92300  7.33000  31.53900  1.000 48.26668  ? 6    GLY A C   1 
ATOM   24   O  O   . GLY A 1 6   ? -8.16800  7.20600  32.50100  1.000 49.00938  ? 6    GLY A O   1 
ATOM   25   N  N   . PRO A 1 7   ? -8.49800  7.71000  30.33100  1.000 50.93415  ? 7    PRO A N   1 
ATOM   26   C  CA  . PRO A 1 7   ? -7.10400  7.97900  30.07400  1.000 52.43941  ? 7    PRO A CA  1 
ATOM   27   C  C   . PRO A 1 7   ? -6.71700  9.42600  30.41900  1.000 53.16923  ? 7    PRO A C   1 
ATOM   28   O  O   . PRO A 1 7   ? -5.67600  9.85100  30.00500  1.000 64.02311  ? 7    PRO A O   1 
ATOM   29   C  CB  . PRO A 1 7   ? -7.06000  7.74100  28.56200  1.000 48.26836  ? 7    PRO A CB  1 
ATOM   30   C  CG  . PRO A 1 7   ? -8.39200  8.22100  28.05800  1.000 47.24424  ? 7    PRO A CG  1 
ATOM   31   C  CD  . PRO A 1 7   ? -9.35800  7.85500  29.15900  1.000 47.26456  ? 7    PRO A CD  1 
ATOM   32   N  N   . TYR A 1 8   ? -7.57500  10.14400 31.13700  1.000 47.83931  ? 8    TYR A N   1 
ATOM   33   C  CA  . TYR A 1 8   ? -7.28200  11.58200 31.37500  1.000 57.89049  ? 8    TYR A CA  1 
ATOM   34   C  C   . TYR A 1 8   ? -7.03500  11.89900 32.84700  1.000 56.99792  ? 8    TYR A C   1 
ATOM   35   O  O   . TYR A 1 8   ? -7.87300  11.58300 33.69600  1.000 54.66501  ? 8    TYR A O   1 
ATOM   36   C  CB  . TYR A 1 8   ? -8.39300  12.48300 30.82400  1.000 57.75515  ? 8    TYR A CB  1 
ATOM   37   C  CG  . TYR A 1 8   ? -8.57100  12.43400 29.32900  1.000 54.50840  ? 8    TYR A CG  1 
ATOM   38   C  CD1 . TYR A 1 8   ? -7.64100  13.01100 28.48300  1.000 54.93436  ? 8    TYR A CD1 1 
ATOM   39   C  CD2 . TYR A 1 8   ? -9.67500  11.82600 28.75900  1.000 50.06252  ? 8    TYR A CD2 1 
ATOM   40   C  CE1 . TYR A 1 8   ? -7.79600  12.97000 27.10900  1.000 59.86525  ? 8    TYR A CE1 1 
ATOM   41   C  CE2 . TYR A 1 8   ? -9.84700  11.78000 27.38700  1.000 48.59200  ? 8    TYR A CE2 1 
ATOM   42   C  CZ  . TYR A 1 8   ? -8.90400  12.35500 26.55900  1.000 50.94327  ? 8    TYR A CZ  1 
ATOM   43   O  OH  . TYR A 1 8   ? -9.06200  12.31300 25.20800  1.000 54.68644  ? 8    TYR A OH  1 
ATOM   44   N  N   . GLU A 1 9   ? -5.88600  12.49300 33.12400  1.000 59.34030  ? 9    GLU A N   1 
ATOM   45   C  CA  . GLU A 1 9   ? -5.62500  12.98500 34.49800  1.000 59.18949  ? 9    GLU A CA  1 
ATOM   46   C  C   . GLU A 1 9   ? -5.90000  14.50000 34.48800  1.000 56.19883  ? 9    GLU A C   1 
ATOM   47   O  O   . GLU A 1 9   ? -5.84100  15.09400 33.40400  1.000 47.97689  ? 9    GLU A O   1 
ATOM   48   C  CB  . GLU A 1 9   ? -4.22400  12.60900 34.97200  1.000 62.75796  ? 9    GLU A CB  1 
ATOM   49   C  CG  . GLU A 1 9   ? -3.15600  12.63800 33.88600  1.000 79.08995  ? 9    GLU A CG  1 
ATOM   50   C  CD  . GLU A 1 9   ? -1.79400  12.27900 34.45000  1.000 90.99999  ? 9    GLU A CD  1 
ATOM   51   O  OE1 . GLU A 1 9   ? -1.65000  11.15000 34.95800  1.000 80.73582  ? 9    GLU A OE1 1 
ATOM   52   O  OE2 . GLU A 1 9   ? -0.88300  13.12900 34.39500  1.000 99.81817  ? 9    GLU A OE2 1 
ATOM   53   N  N   . ALA A 1 10  ? -6.09800  15.10500 35.66100  1.000 59.85833  ? 10   ALA A N   1 
ATOM   54   C  CA  . ALA A 1 10  ? -6.47400  16.53400 35.70300  1.000 49.90634  ? 10   ALA A CA  1 
ATOM   55   C  C   . ALA A 1 10  ? -5.22400  17.37800 35.53300  1.000 55.68653  ? 10   ALA A C   1 
ATOM   56   O  O   . ALA A 1 10  ? -4.88900  18.16500 36.42200  1.000 57.30520  ? 10   ALA A O   1 
ATOM   57   C  CB  . ALA A 1 10  ? -7.17400  16.84100 36.98500  1.000 47.98014  ? 10   ALA A CB  1 
ATOM   58   N  N   . THR A 1 11  ? -4.58300  17.22200 34.38600  1.000 52.58596  ? 11   THR A N   1 
ATOM   59   C  CA  . THR A 1 11  ? -3.43100  18.04800 34.04500  1.000 59.80510  ? 11   THR A CA  1 
ATOM   60   C  C   . THR A 1 11  ? -3.73300  18.63400 32.69600  1.000 58.64551  ? 11   THR A C   1 
ATOM   61   O  O   . THR A 1 11  ? -4.61100  18.10300 32.01200  1.000 57.96429  ? 11   THR A O   1 
ATOM   62   C  CB  . THR A 1 11  ? -2.16500  17.20600 33.99800  1.000 65.46890  ? 11   THR A CB  1 
ATOM   63   O  OG1 . THR A 1 11  ? -1.16600  18.08200 33.49200  1.000 84.39588  ? 11   THR A OG1 1 
ATOM   64   C  CG2 . THR A 1 11  ? -2.28200  16.01600 33.06900  1.000 65.00105  ? 11   THR A CG2 1 
ATOM   65   N  N   . TRP A 1 12  ? -3.00200  19.66100 32.29100  1.000 54.95373  ? 12   TRP A N   1 
ATOM   66   C  CA  . TRP A 1 12  ? -3.21000  20.24100 30.95100  1.000 49.44754  ? 12   TRP A CA  1 
ATOM   67   C  C   . TRP A 1 12  ? -2.74100  19.26600 29.88400  1.000 51.42130  ? 12   TRP A C   1 
ATOM   68   O  O   . TRP A 1 12  ? -3.44500  19.08600 28.89900  1.000 58.20842  ? 12   TRP A O   1 
ATOM   69   C  CB  . TRP A 1 12  ? -2.49500  21.59100 30.81900  1.000 54.45967  ? 12   TRP A CB  1 
ATOM   70   C  CG  . TRP A 1 12  ? -3.10600  22.67400 31.66500  1.000 62.52754  ? 12   TRP A CG  1 
ATOM   71   C  CD1 . TRP A 1 12  ? -2.62100  23.18000 32.83300  1.000 63.52074  ? 12   TRP A CD1 1 
ATOM   72   C  CD2 . TRP A 1 12  ? -4.36000  23.34700 31.42700  1.000 63.54829  ? 12   TRP A CD2 1 
ATOM   73   N  NE1 . TRP A 1 12  ? -3.46800  24.13500 33.32500  1.000 61.77549  ? 12   TRP A NE1 1 
ATOM   74   C  CE2 . TRP A 1 12  ? -4.54600  24.25400 32.49000  1.000 61.99084  ? 12   TRP A CE2 1 
ATOM   75   C  CE3 . TRP A 1 12  ? -5.33200  23.27400 30.42500  1.000 63.44796  ? 12   TRP A CE3 1 
ATOM   76   C  CZ2 . TRP A 1 12  ? -5.66300  25.07900 32.57500  1.000 61.57798  ? 12   TRP A CZ2 1 
ATOM   77   C  CZ3 . TRP A 1 12  ? -6.43900  24.08700 30.51600  1.000 59.58734  ? 12   TRP A CZ3 1 
ATOM   78   C  CH2 . TRP A 1 12  ? -6.60100  24.97300 31.57700  1.000 59.03142  ? 12   TRP A CH2 1 
ATOM   79   N  N   . GLU A 1 13  ? -1.59700  18.63600 30.08700  1.000 61.45776  ? 13   GLU A N   1 
ATOM   80   C  CA  . GLU A 1 13  ? -1.03100  17.77400 29.01100  1.000 63.75851  ? 13   GLU A CA  1 
ATOM   81   C  C   . GLU A 1 13  ? -1.92600  16.56200 28.72700  1.000 57.10403  ? 13   GLU A C   1 
ATOM   82   O  O   . GLU A 1 13  ? -2.01200  16.17400 27.56400  1.000 57.93792  ? 13   GLU A O   1 
ATOM   83   C  CB  . GLU A 1 13  ? 0.40100   17.36800 29.34500  1.000 69.89629  ? 13   GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 13  ? 1.09400   16.66200 28.19500  1.000 97.92271  ? 13   GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 13  ? 2.50100   16.17400 28.48400  1.000 108.99153 ? 13   GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 13  ? 3.05400   16.55800 29.53200  1.000 113.70503 ? 13   GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 13  ? 3.03600   15.40600 27.66100  1.000 110.10011 ? 13   GLU A OE2 1 
ATOM   88   N  N   . SER A 1 14  ? -2.59800  16.03000 29.73500  1.000 54.58668  ? 14   SER A N   1 
ATOM   89   C  CA  . SER A 1 14  ? -3.51800  14.89500 29.50700  1.000 60.95878  ? 14   SER A CA  1 
ATOM   90   C  C   . SER A 1 14  ? -4.78900  15.42700 28.85700  1.000 51.39925  ? 14   SER A C   1 
ATOM   91   O  O   . SER A 1 14  ? -5.24300  14.82800 27.88000  1.000 59.74910  ? 14   SER A O   1 
ATOM   92   C  CB  . SER A 1 14  ? -3.84000  14.17200 30.77900  1.000 56.38683  ? 14   SER A CB  1 
ATOM   93   O  OG  . SER A 1 14  ? -4.67500  13.04900 30.54800  1.000 67.35026  ? 14   SER A OG  1 
ATOM   94   N  N   . THR A 1 15  ? -5.31400  16.52100 29.38900  1.000 52.72783  ? 15   THR A N   1 
ATOM   95   C  CA  . THR A 1 15  ? -6.59900  17.04500 28.88300  1.000 50.44576  ? 15   THR A CA  1 
ATOM   96   C  C   . THR A 1 15  ? -6.41800  17.56400 27.47300  1.000 46.28487  ? 15   THR A C   1 
ATOM   97   O  O   . THR A 1 15  ? -7.36500  17.48000 26.70100  1.000 47.27147  ? 15   THR A O   1 
ATOM   98   C  CB  . THR A 1 15  ? -7.13600  18.10100 29.84700  1.000 47.23816  ? 15   THR A CB  1 
ATOM   99   O  OG1 . THR A 1 15  ? -6.09800  19.06500 29.97100  1.000 60.56917  ? 15   THR A OG1 1 
ATOM   100  C  CG2 . THR A 1 15  ? -7.51400  17.51100 31.19200  1.000 48.41820  ? 15   THR A CG2 1 
ATOM   101  N  N   . ASP A 1 16  ? -5.23100  18.03700 27.11700  1.000 46.20216  ? 16   ASP A N   1 
ATOM   102  C  CA  . ASP A 1 16  ? -4.97700  18.66400 25.79700  1.000 46.05118  ? 16   ASP A CA  1 
ATOM   103  C  C   . ASP A 1 16  ? -4.95800  17.63100 24.67000  1.000 56.42120  ? 16   ASP A C   1 
ATOM   104  O  O   . ASP A 1 16  ? -4.78300  18.03600 23.51800  1.000 59.51254  ? 16   ASP A O   1 
ATOM   105  C  CB  . ASP A 1 16  ? -3.65200  19.42500 25.78100  1.000 48.01079  ? 16   ASP A CB  1 
ATOM   106  C  CG  . ASP A 1 16  ? -3.66200  20.76500 26.48900  1.000 54.38526  ? 16   ASP A CG  1 
ATOM   107  O  OD1 . ASP A 1 16  ? -4.66200  21.07600 27.13800  1.000 51.79254  ? 16   ASP A OD1 1 
ATOM   108  O  OD2 . ASP A 1 16  ? -2.65900  21.48000 26.37700  1.000 61.43428  ? 16   ASP A OD2 1 
ATOM   109  N  N   . LYS A 1 17  ? -5.13800  16.35800 24.99100  1.000 51.26563  ? 17   LYS A N   1 
ATOM   110  C  CA  . LYS A 1 17  ? -5.05900  15.28900 23.96900  1.000 46.87842  ? 17   LYS A CA  1 
ATOM   111  C  C   . LYS A 1 17  ? -6.48500  15.01500 23.51800  1.000 45.15750  ? 17   LYS A C   1 
ATOM   112  O  O   . LYS A 1 17  ? -6.66700  14.38600 22.48300  1.000 51.47468  ? 17   LYS A O   1 
ATOM   113  C  CB  . LYS A 1 17  ? -4.36400  14.07000 24.57500  1.000 50.51316  ? 17   LYS A CB  1 
ATOM   114  C  CG  . LYS A 1 17  ? -2.88100  14.22900 24.86300  1.000 58.70621  ? 17   LYS A CG  1 
ATOM   115  C  CD  . LYS A 1 17  ? -2.37300  13.22000 25.86400  1.000 56.76682  ? 17   LYS A CD  1 
ATOM   116  C  CE  . LYS A 1 17  ? -1.02600  12.64600 25.48900  1.000 57.96425  ? 17   LYS A CE  1 
ATOM   117  N  NZ  . LYS A 1 17  ? -0.55700  11.66100 26.49100  1.000 70.00268  ? 17   LYS A NZ  1 
ATOM   118  N  N   . HIS A 1 18  ? -7.43700  15.51700 24.31500  1.000 46.24056  ? 18   HIS A N   1 
ATOM   119  C  CA  . HIS A 1 18  ? -8.86600  15.40900 23.94500  1.000 47.57016  ? 18   HIS A CA  1 
ATOM   120  C  C   . HIS A 1 18  ? -9.09000  16.09300 22.59500  1.000 54.65677  ? 18   HIS A C   1 
ATOM   121  O  O   . HIS A 1 18  ? -8.46500  17.15400 22.35500  1.000 43.34459  ? 18   HIS A O   1 
ATOM   122  C  CB  . HIS A 1 18  ? -9.72600  16.04300 25.03900  1.000 45.95418  ? 18   HIS A CB  1 
ATOM   123  C  CG  . HIS A 1 18  ? -11.16500 16.17000 24.66900  1.000 53.24598  ? 18   HIS A CG  1 
ATOM   124  N  ND1 . HIS A 1 18  ? -11.74000 17.38600 24.35200  1.000 56.74272  ? 18   HIS A ND1 1 
ATOM   125  C  CD2 . HIS A 1 18  ? -12.14400 15.24400 24.55400  1.000 45.62923  ? 18   HIS A CD2 1 
ATOM   126  C  CE1 . HIS A 1 18  ? -13.01400 17.20500 24.06300  1.000 54.23173  ? 18   HIS A CE1 1 
ATOM   127  N  NE2 . HIS A 1 18  ? -13.28800 15.89900 24.18100  1.000 48.85393  ? 18   HIS A NE2 1 
ATOM   128  N  N   . ILE A 1 19  ? -9.92600  15.50000 21.74400  1.000 49.69990  ? 19   ILE A N   1 
ATOM   129  C  CA  . ILE A 1 19  ? -10.28500 16.10000 20.43100  1.000 46.54131  ? 19   ILE A CA  1 
ATOM   130  C  C   . ILE A 1 19  ? -11.22000 17.28100 20.70600  1.000 44.82967  ? 19   ILE A C   1 
ATOM   131  O  O   . ILE A 1 19  ? -12.35000 17.04300 21.14300  1.000 44.62641  ? 19   ILE A O   1 
ATOM   132  C  CB  . ILE A 1 19  ? -10.90000 15.02800 19.51800  1.000 46.71179  ? 19   ILE A CB  1 
ATOM   133  C  CG1 . ILE A 1 19  ? -9.94500  13.86600 19.29600  1.000 49.65069  ? 19   ILE A CG1 1 
ATOM   134  C  CG2 . ILE A 1 19  ? -11.35100 15.64400 18.19400  1.000 44.29969  ? 19   ILE A CG2 1 
ATOM   135  C  CD1 . ILE A 1 19  ? -10.60600 12.64000 18.69800  1.000 53.72221  ? 19   ILE A CD1 1 
ATOM   136  N  N   . ALA A 1 20  ? -10.74100 18.49900 20.46600  1.000 41.61619  ? 20   ALA A N   1 
ATOM   137  C  CA  . ALA A 1 20  ? -11.52000 19.69000 20.79700  1.000 42.60369  ? 20   ALA A CA  1 
ATOM   138  C  C   . ALA A 1 20  ? -12.89000 19.65800 20.13300  1.000 41.89188  ? 20   ALA A C   1 
ATOM   139  O  O   . ALA A 1 20  ? -13.92100 19.80400 20.80000  1.000 43.67332  ? 20   ALA A O   1 
ATOM   140  C  CB  . ALA A 1 20  ? -10.75300 20.94600 20.38500  1.000 45.77404  ? 20   ALA A CB  1 
ATOM   141  N  N   . SER A 1 21  ? -12.86000 19.53500 18.80800  1.000 40.77475  ? 21   SER A N   1 
ATOM   142  C  CA  . SER A 1 21  ? -14.09500 19.54000 17.98200  1.000 51.41746  ? 21   SER A CA  1 
ATOM   143  C  C   . SER A 1 21  ? -14.14400 18.27200 17.11900  1.000 45.75622  ? 21   SER A C   1 
ATOM   144  O  O   . SER A 1 21  ? -13.42700 18.18600 16.12300  1.000 44.41536  ? 21   SER A O   1 
ATOM   145  C  CB  . SER A 1 21  ? -14.17100 20.79800 17.14100  1.000 47.88673  ? 21   SER A CB  1 
ATOM   146  O  OG  . SER A 1 21  ? -12.99900 20.95600 16.36300  1.000 62.61417  ? 21   SER A OG  1 
ATOM   147  N  N   . PRO A 1 22  ? -14.96800 17.28300 17.49800  1.000 45.07834  ? 22   PRO A N   1 
ATOM   148  C  CA  . PRO A 1 22  ? -15.05300 16.04900 16.73800  1.000 42.56313  ? 22   PRO A CA  1 
ATOM   149  C  C   . PRO A 1 22  ? -15.70000 16.24500 15.35000  1.000 47.31412  ? 22   PRO A C   1 
ATOM   150  O  O   . PRO A 1 22  ? -16.23900 17.29200 15.11900  1.000 52.60635  ? 22   PRO A O   1 
ATOM   151  C  CB  . PRO A 1 22  ? -15.92500 15.20100 17.66500  1.000 39.84219  ? 22   PRO A CB  1 
ATOM   152  C  CG  . PRO A 1 22  ? -16.78900 16.18900 18.38800  1.000 41.93202  ? 22   PRO A CG  1 
ATOM   153  C  CD  . PRO A 1 22  ? -15.83900 17.32700 18.66400  1.000 43.45309  ? 22   PRO A CD  1 
ATOM   154  N  N   . GLU A 1 23  ? -15.64100 15.23700 14.48000  1.000 43.57440  ? 23   GLU A N   1 
ATOM   155  C  CA  . GLU A 1 23  ? -16.20600 15.31500 13.10600  1.000 41.17179  ? 23   GLU A CA  1 
ATOM   156  C  C   . GLU A 1 23  ? -17.72700 15.53500 13.12400  1.000 42.01048  ? 23   GLU A C   1 
ATOM   157  O  O   . GLU A 1 23  ? -18.18200 16.33300 12.32200  1.000 45.53843  ? 23   GLU A O   1 
ATOM   158  C  CB  . GLU A 1 23  ? -15.80500 14.07400 12.31300  1.000 39.91571  ? 23   GLU A CB  1 
ATOM   159  C  CG  . GLU A 1 23  ? -16.15500 14.13300 10.83800  1.000 53.40389  ? 23   GLU A CG  1 
ATOM   160  C  CD  . GLU A 1 23  ? -15.80200 12.88000 10.05300  1.000 75.48969  ? 23   GLU A CD  1 
ATOM   161  O  OE1 . GLU A 1 23  ? -15.92300 11.77400 10.61600  1.000 65.03752  ? 23   GLU A OE1 1 
ATOM   162  O  OE2 . GLU A 1 23  ? -15.39700 13.01200 8.88500   1.000 67.76751  ? 23   GLU A OE2 1 
ATOM   163  N  N   . TRP A 1 24  ? -18.46800 14.89900 14.01500  1.000 39.80668  ? 24   TRP A N   1 
ATOM   164  C  CA  . TRP A 1 24  ? -19.91800 15.16600 14.04000  1.000 38.23898  ? 24   TRP A CA  1 
ATOM   165  C  C   . TRP A 1 24  ? -20.19100 16.65100 14.29600  1.000 41.76664  ? 24   TRP A C   1 
ATOM   166  O  O   . TRP A 1 24  ? -21.08300 17.19200 13.64600  1.000 45.94931  ? 24   TRP A O   1 
ATOM   167  C  CB  . TRP A 1 24  ? -20.63100 14.29100 15.06500  1.000 38.29943  ? 24   TRP A CB  1 
ATOM   168  C  CG  . TRP A 1 24  ? -20.31300 14.56300 16.50100  1.000 45.39569  ? 24   TRP A CG  1 
ATOM   169  C  CD1 . TRP A 1 24  ? -19.36200 13.95500 17.26500  1.000 42.30013  ? 24   TRP A CD1 1 
ATOM   170  C  CD2 . TRP A 1 24  ? -20.98000 15.50000 17.36200  1.000 51.07381  ? 24   TRP A CD2 1 
ATOM   171  N  NE1 . TRP A 1 24  ? -19.38600 14.45500 18.53700  1.000 44.28599  ? 24   TRP A NE1 1 
ATOM   172  C  CE2 . TRP A 1 24  ? -20.36500 15.40500 18.62700  1.000 48.18160  ? 24   TRP A CE2 1 
ATOM   173  C  CE3 . TRP A 1 24  ? -22.02500 16.41200 17.18600  1.000 38.00154  ? 24   TRP A CE3 1 
ATOM   174  C  CZ2 . TRP A 1 24  ? -20.76200 16.19000 19.70600  1.000 51.82070  ? 24   TRP A CZ2 1 
ATOM   175  C  CZ3 . TRP A 1 24  ? -22.42100 17.18300 18.25300  1.000 37.26683  ? 24   TRP A CZ3 1 
ATOM   176  C  CH2 . TRP A 1 24  ? -21.79600 17.07300 19.49400  1.000 54.74886  ? 24   TRP A CH2 1 
ATOM   177  N  N   . PHE A 1 25  ? -19.48300 17.25900 15.24600  1.000 37.90820  ? 25   PHE A N   1 
ATOM   178  C  CA  . PHE A 1 25  ? -19.69800 18.68400 15.59800  1.000 42.24006  ? 25   PHE A CA  1 
ATOM   179  C  C   . PHE A 1 25  ? -19.42500 19.51600 14.35700  1.000 39.77292  ? 25   PHE A C   1 
ATOM   180  O  O   . PHE A 1 25  ? -20.25500 20.35200 14.01300  1.000 41.59238  ? 25   PHE A O   1 
ATOM   181  C  CB  . PHE A 1 25  ? -18.79100 19.07900 16.76900  1.000 42.02771  ? 25   PHE A CB  1 
ATOM   182  C  CG  . PHE A 1 25  ? -18.94800 20.46600 17.33100  1.000 39.28402  ? 25   PHE A CG  1 
ATOM   183  C  CD1 . PHE A 1 25  ? -20.03600 20.79200 18.12100  1.000 37.17623  ? 25   PHE A CD1 1 
ATOM   184  C  CD2 . PHE A 1 25  ? -17.97000 21.42200 17.12700  1.000 39.34177  ? 25   PHE A CD2 1 
ATOM   185  C  CE1 . PHE A 1 25  ? -20.16400 22.06000 18.65900  1.000 36.95342  ? 25   PHE A CE1 1 
ATOM   186  C  CE2 . PHE A 1 25  ? -18.09800 22.68900 17.66900  1.000 40.46431  ? 25   PHE A CE2 1 
ATOM   187  C  CZ  . PHE A 1 25  ? -19.19500 23.00500 18.43100  1.000 37.09075  ? 25   PHE A CZ  1 
ATOM   188  N  N   . ARG A 1 26  ? -18.31500 19.22500 13.69900  1.000 38.80712  ? 26   ARG A N   1 
ATOM   189  C  CA  . ARG A 1 26  ? -17.95600 19.98700 12.48600  1.000 40.32157  ? 26   ARG A CA  1 
ATOM   190  C  C   . ARG A 1 26  ? -19.01800 19.78300 11.38600  1.000 41.02275  ? 26   ARG A C   1 
ATOM   191  O  O   . ARG A 1 26  ? -19.12000 20.64900 10.51900  1.000 50.57452  ? 26   ARG A O   1 
ATOM   192  C  CB  . ARG A 1 26  ? -16.54300 19.63300 12.03200  1.000 38.34259  ? 26   ARG A CB  1 
ATOM   193  C  CG  . ARG A 1 26  ? -15.45700 19.87600 13.06500  1.000 38.92153  ? 26   ARG A CG  1 
ATOM   194  C  CD  . ARG A 1 26  ? -14.09100 19.79000 12.41900  1.000 39.28806  ? 26   ARG A CD  1 
ATOM   195  N  NE  . ARG A 1 26  ? -13.04900 19.64600 13.42000  1.000 55.73383  ? 26   ARG A NE  1 
ATOM   196  C  CZ  . ARG A 1 26  ? -11.75100 19.73600 13.17500  1.000 55.67114  ? 26   ARG A CZ  1 
ATOM   197  N  NH1 . ARG A 1 26  ? -11.32400 19.98900 11.95100  1.000 61.72679  ? 26   ARG A NH1 1 
ATOM   198  N  NH2 . ARG A 1 26  ? -10.88400 19.58200 14.15600  1.000 53.21029  ? 26   ARG A NH2 1 
ATOM   199  N  N   . ASP A 1 27  ? -19.79600 18.70500 11.43800  1.000 39.19726  ? 27   ASP A N   1 
ATOM   200  C  CA  . ASP A 1 27  ? -20.81300 18.42600 10.39600  1.000 40.07633  ? 27   ASP A CA  1 
ATOM   201  C  C   . ASP A 1 27  ? -22.17400 18.97200 10.82700  1.000 43.80856  ? 27   ASP A C   1 
ATOM   202  O  O   . ASP A 1 27  ? -23.01300 19.17100 9.95200   1.000 41.96763  ? 27   ASP A O   1 
ATOM   203  C  CB  . ASP A 1 27  ? -20.89700 16.93300 10.07400  1.000 46.42723  ? 27   ASP A CB  1 
ATOM   204  C  CG  . ASP A 1 27  ? -19.61900 16.29700 9.56500   1.000 46.69287  ? 27   ASP A CG  1 
ATOM   205  O  OD1 . ASP A 1 27  ? -18.68400 17.03700 9.24700   1.000 51.69121  ? 27   ASP A OD1 1 
ATOM   206  O  OD2 . ASP A 1 27  ? -19.57700 15.06000 9.50300   1.000 40.04383  ? 27   ASP A OD2 1 
ATOM   207  N  N   . ALA A 1 28  ? -22.38200 19.19800 12.12000  1.000 40.89148  ? 28   ALA A N   1 
ATOM   208  C  CA  . ALA A 1 28  ? -23.70800 19.62600 12.61800  1.000 36.13232  ? 28   ALA A CA  1 
ATOM   209  C  C   . ALA A 1 28  ? -24.05100 21.05600 12.19800  1.000 38.71265  ? 28   ALA A C   1 
ATOM   210  O  O   . ALA A 1 28  ? -25.23000 21.29900 11.94200  1.000 39.85347  ? 28   ALA A O   1 
ATOM   211  C  CB  . ALA A 1 28  ? -23.75300 19.44800 14.10600  1.000 37.58127  ? 28   ALA A CB  1 
ATOM   212  N  N   . LYS A 1 29  ? -23.08100 21.96800 12.24700  1.000 43.00472  ? 29   LYS A N   1 
ATOM   213  C  CA  . LYS A 1 29  ? -23.26500 23.32800 11.74200  1.000 35.60017  ? 29   LYS A CA  1 
ATOM   214  C  C   . LYS A 1 29  ? -24.21200 24.17100 12.59200  1.000 39.29248  ? 29   LYS A C   1 
ATOM   215  O  O   . LYS A 1 29  ? -23.82500 25.24300 13.06800  1.000 37.77372  ? 29   LYS A O   1 
ATOM   216  C  CB  . LYS A 1 29  ? -23.75600 23.30500 10.29000  1.000 35.51505  ? 29   LYS A CB  1 
ATOM   217  C  CG  . LYS A 1 29  ? -22.77800 22.67400 9.31700   1.000 40.94769  ? 29   LYS A CG  1 
ATOM   218  C  CD  . LYS A 1 29  ? -21.38100 23.23700 9.51000   1.000 40.87627  ? 29   LYS A CD  1 
ATOM   219  C  CE  . LYS A 1 29  ? -20.42200 22.71200 8.45800   1.000 38.17106  ? 29   LYS A CE  1 
ATOM   220  N  NZ  . LYS A 1 29  ? -19.00600 23.01600 8.81000   1.000 41.80089  ? 29   LYS A NZ  1 
ATOM   221  N  N   . PHE A 1 30  ? -25.44800 23.71500 12.78600  1.000 36.72358  ? 30   PHE A N   1 
ATOM   222  C  CA  . PHE A 1 30  ? -26.48500 24.54300 13.38700  1.000 34.69674  ? 30   PHE A CA  1 
ATOM   223  C  C   . PHE A 1 30  ? -27.08800 23.86100 14.60700  1.000 40.32483  ? 30   PHE A C   1 
ATOM   224  O  O   . PHE A 1 30  ? -27.36000 22.65600 14.58700  1.000 39.06728  ? 30   PHE A O   1 
ATOM   225  C  CB  . PHE A 1 30  ? -27.58200 24.86100 12.36200  1.000 34.45049  ? 30   PHE A CB  1 
ATOM   226  C  CG  . PHE A 1 30  ? -28.72600 25.65200 12.92100  1.000 34.15654  ? 30   PHE A CG  1 
ATOM   227  C  CD1 . PHE A 1 30  ? -28.53300 26.94500 13.37700  1.000 40.37408  ? 30   PHE A CD1 1 
ATOM   228  C  CD2 . PHE A 1 30  ? -29.99600 25.10600 12.98100  1.000 34.04180  ? 30   PHE A CD2 1 
ATOM   229  C  CE1 . PHE A 1 30  ? -29.58600 27.67400 13.89100  1.000 33.80921  ? 30   PHE A CE1 1 
ATOM   230  C  CE2 . PHE A 1 30  ? -31.05300 25.83200 13.49200  1.000 33.81965  ? 30   PHE A CE2 1 
ATOM   231  C  CZ  . PHE A 1 30  ? -30.84700 27.11800 13.94700  1.000 33.70016  ? 30   PHE A CZ  1 
ATOM   232  N  N   . GLY A 1 31  ? -27.29900 24.64500 15.66300  1.000 39.64966  ? 31   GLY A N   1 
ATOM   233  C  CA  . GLY A 1 31  ? -27.90100 24.14200 16.88400  1.000 35.48410  ? 31   GLY A CA  1 
ATOM   234  C  C   . GLY A 1 31  ? -28.73500 25.21200 17.55600  1.000 40.36554  ? 31   GLY A C   1 
ATOM   235  O  O   . GLY A 1 31  ? -28.63000 26.40200 17.23900  1.000 39.94604  ? 31   GLY A O   1 
ATOM   236  N  N   . VAL A 1 32  ? -29.60100 24.76800 18.45600  1.000 35.96196  ? 32   VAL A N   1 
ATOM   237  C  CA  . VAL A 1 32  ? -30.52800 25.68700 19.16400  1.000 40.37244  ? 32   VAL A CA  1 
ATOM   238  C  C   . VAL A 1 32  ? -30.54900 25.36700 20.66300  1.000 40.40942  ? 32   VAL A C   1 
ATOM   239  O  O   . VAL A 1 32  ? -30.60800 24.18000 21.00400  1.000 44.36256  ? 32   VAL A O   1 
ATOM   240  C  CB  . VAL A 1 32  ? -31.95900 25.62400 18.59900  1.000 34.16074  ? 32   VAL A CB  1 
ATOM   241  C  CG1 . VAL A 1 32  ? -32.96600 26.38100 19.45000  1.000 37.46879  ? 32   VAL A CG1 1 
ATOM   242  C  CG2 . VAL A 1 32  ? -32.02800 26.03000 17.13600  1.000 33.79625  ? 32   VAL A CG2 1 
ATOM   243  N  N   . TYR A 1 33  ? -30.51000 26.40600 21.50300  1.000 40.56869  ? 33   TYR A N   1 
ATOM   244  C  CA  . TYR A 1 33  ? -30.65100 26.25600 22.97000  1.000 34.48733  ? 33   TYR A CA  1 
ATOM   245  C  C   . TYR A 1 33  ? -31.59500 27.35000 23.46200  1.000 39.26993  ? 33   TYR A C   1 
ATOM   246  O  O   . TYR A 1 33  ? -31.91700 28.24100 22.67400  1.000 43.00057  ? 33   TYR A O   1 
ATOM   247  C  CB  . TYR A 1 33  ? -29.29500 26.24800 23.67500  1.000 41.55527  ? 33   TYR A CB  1 
ATOM   248  C  CG  . TYR A 1 33  ? -28.57000 27.54700 23.91100  1.000 39.45097  ? 33   TYR A CG  1 
ATOM   249  C  CD1 . TYR A 1 33  ? -28.13200 28.34200 22.86900  1.000 40.64010  ? 33   TYR A CD1 1 
ATOM   250  C  CD2 . TYR A 1 33  ? -28.22400 27.92200 25.19700  1.000 45.19289  ? 33   TYR A CD2 1 
ATOM   251  C  CE1 . TYR A 1 33  ? -27.42500 29.50900 23.10200  1.000 41.58048  ? 33   TYR A CE1 1 
ATOM   252  C  CE2 . TYR A 1 33  ? -27.51300 29.08100 25.45000  1.000 43.46633  ? 33   TYR A CE2 1 
ATOM   253  C  CZ  . TYR A 1 33  ? -27.11300 29.88000 24.39800  1.000 53.26167  ? 33   TYR A CZ  1 
ATOM   254  O  OH  . TYR A 1 33  ? -26.41600 31.02400 24.65000  1.000 57.78282  ? 33   TYR A OH  1 
ATOM   255  N  N   . TRP A 1 34  ? -32.01700 27.27300 24.71500  1.000 40.00897  ? 34   TRP A N   1 
ATOM   256  C  CA  . TRP A 1 34  ? -33.01300 28.22500 25.25000  1.000 39.48652  ? 34   TRP A CA  1 
ATOM   257  C  C   . TRP A 1 34  ? -32.68000 28.72500 26.66400  1.000 40.20345  ? 34   TRP A C   1 
ATOM   258  O  O   . TRP A 1 34  ? -32.59400 27.90300 27.57800  1.000 44.64702  ? 34   TRP A O   1 
ATOM   259  C  CB  . TRP A 1 34  ? -34.40200 27.59200 25.20900  1.000 39.09735  ? 34   TRP A CB  1 
ATOM   260  C  CG  . TRP A 1 34  ? -34.50000 26.14500 25.57700  1.000 40.42969  ? 34   TRP A CG  1 
ATOM   261  C  CD1 . TRP A 1 34  ? -34.86600 25.62600 26.78400  1.000 44.54802  ? 34   TRP A CD1 1 
ATOM   262  C  CD2 . TRP A 1 34  ? -34.29500 25.02100 24.70600  1.000 43.62779  ? 34   TRP A CD2 1 
ATOM   263  N  NE1 . TRP A 1 34  ? -34.87900 24.26000 26.73200  1.000 46.37042  ? 34   TRP A NE1 1 
ATOM   264  C  CE2 . TRP A 1 34  ? -34.53000 23.85900 25.47100  1.000 51.48447  ? 34   TRP A CE2 1 
ATOM   265  C  CE3 . TRP A 1 34  ? -33.92900 24.88100 23.36400  1.000 38.36682  ? 34   TRP A CE3 1 
ATOM   266  C  CZ2 . TRP A 1 34  ? -34.40400 22.58000 24.93600  1.000 45.15449  ? 34   TRP A CZ2 1 
ATOM   267  C  CZ3 . TRP A 1 34  ? -33.80100 23.61600 22.83900  1.000 37.76127  ? 34   TRP A CZ3 1 
ATOM   268  C  CH2 . TRP A 1 34  ? -34.03800 22.48300 23.61400  1.000 35.66973  ? 34   TRP A CH2 1 
ATOM   269  N  N   . HIS A 1 35  ? -32.54700 30.04000 26.84200  1.000 42.02561  ? 35   HIS A N   1 
ATOM   270  C  CA  . HIS A 1 35  ? -32.38000 30.61100 28.19900  1.000 39.62023  ? 35   HIS A CA  1 
ATOM   271  C  C   . HIS A 1 35  ? -33.76900 30.65900 28.83200  1.000 45.35843  ? 35   HIS A C   1 
ATOM   272  O  O   . HIS A 1 35  ? -34.45700 31.66900 28.68500  1.000 42.13873  ? 35   HIS A O   1 
ATOM   273  C  CB  . HIS A 1 35  ? -31.70400 31.98100 28.14900  1.000 40.16247  ? 35   HIS A CB  1 
ATOM   274  C  CG  . HIS A 1 35  ? -30.22800 32.01300 27.99600  1.000 41.00731  ? 35   HIS A CG  1 
ATOM   275  N  ND1 . HIS A 1 35  ? -29.54700 31.51000 26.91300  1.000 43.97523  ? 35   HIS A ND1 1 
ATOM   276  C  CD2 . HIS A 1 35  ? -29.31100 32.55600 28.79000  1.000 35.59485  ? 35   HIS A CD2 1 
ATOM   277  C  CE1 . HIS A 1 35  ? -28.25500 31.73200 27.07700  1.000 48.25349  ? 35   HIS A CE1 1 
ATOM   278  N  NE2 . HIS A 1 35  ? -28.09100 32.36400 28.21000  1.000 49.48170  ? 35   HIS A NE2 1 
ATOM   279  N  N   . TRP A 1 36  ? -34.17000 29.57000 29.49200  1.000 43.48834  ? 36   TRP A N   1 
ATOM   280  C  CA  . TRP A 1 36  ? -35.48300 29.51500 30.17800  1.000 44.66699  ? 36   TRP A CA  1 
ATOM   281  C  C   . TRP A 1 36  ? -35.24900 29.07400 31.61800  1.000 43.64811  ? 36   TRP A C   1 
ATOM   282  O  O   . TRP A 1 36  ? -34.56000 28.07900 31.80800  1.000 48.74494  ? 36   TRP A O   1 
ATOM   283  C  CB  . TRP A 1 36  ? -36.45000 28.57600 29.45800  1.000 40.85592  ? 36   TRP A CB  1 
ATOM   284  C  CG  . TRP A 1 36  ? -37.85900 28.60100 29.95300  1.000 39.57091  ? 36   TRP A CG  1 
ATOM   285  C  CD1 . TRP A 1 36  ? -38.67900 29.68300 30.05500  1.000 41.19805  ? 36   TRP A CD1 1 
ATOM   286  C  CD2 . TRP A 1 36  ? -38.63000 27.47000 30.38900  1.000 40.79261  ? 36   TRP A CD2 1 
ATOM   287  N  NE1 . TRP A 1 36  ? -39.90100 29.30600 30.53900  1.000 51.35141  ? 36   TRP A NE1 1 
ATOM   288  C  CE2 . TRP A 1 36  ? -39.90200 27.95500 30.75000  1.000 43.13863  ? 36   TRP A CE2 1 
ATOM   289  C  CE3 . TRP A 1 36  ? -38.36900 26.10300 30.51200  1.000 39.81024  ? 36   TRP A CE3 1 
ATOM   290  C  CZ2 . TRP A 1 36  ? -40.90600 27.12000 31.22900  1.000 46.63873  ? 36   TRP A CZ2 1 
ATOM   291  C  CZ3 . TRP A 1 36  ? -39.36200 25.27900 30.98500  1.000 39.94657  ? 36   TRP A CZ3 1 
ATOM   292  C  CH2 . TRP A 1 36  ? -40.61100 25.78200 31.33600  1.000 46.79303  ? 36   TRP A CH2 1 
ATOM   293  N  N   . GLY A 1 37  ? -35.82400 29.78800 32.57400  1.000 44.37315  ? 37   GLY A N   1 
ATOM   294  C  CA  . GLY A 1 37  ? -35.60600 29.47000 33.98900  1.000 44.16661  ? 37   GLY A CA  1 
ATOM   295  C  C   . GLY A 1 37  ? -36.31300 30.44000 34.90100  1.000 44.93652  ? 37   GLY A C   1 
ATOM   296  O  O   . GLY A 1 37  ? -37.16000 31.20200 34.42400  1.000 44.02722  ? 37   GLY A O   1 
ATOM   297  N  N   . ALA A 1 38  ? -36.01400 30.36300 36.19000  1.000 42.18154  ? 38   ALA A N   1 
ATOM   298  C  CA  . ALA A 1 38  ? -36.62200 31.27600 37.17500  1.000 49.52944  ? 38   ALA A CA  1 
ATOM   299  C  C   . ALA A 1 38  ? -36.32400 32.73500 36.81500  1.000 43.82362  ? 38   ALA A C   1 
ATOM   300  O  O   . ALA A 1 38  ? -37.12000 33.60000 37.16900  1.000 47.75091  ? 38   ALA A O   1 
ATOM   301  C  CB  . ALA A 1 38  ? -36.09600 30.92300 38.53600  1.000 51.31369  ? 38   ALA A CB  1 
ATOM   302  N  N   . PHE A 1 39  ? -35.23300 32.98700 36.08900  1.000 39.74597  ? 39   PHE A N   1 
ATOM   303  C  CA  . PHE A 1 39  ? -34.84500 34.35500 35.64900  1.000 43.65045  ? 39   PHE A CA  1 
ATOM   304  C  C   . PHE A 1 39  ? -35.81700 34.92900 34.62900  1.000 40.06607  ? 39   PHE A C   1 
ATOM   305  O  O   . PHE A 1 39  ? -35.66500 36.10200 34.30200  1.000 47.82189  ? 39   PHE A O   1 
ATOM   306  C  CB  . PHE A 1 39  ? -33.47500 34.35600 34.97800  1.000 39.59124  ? 39   PHE A CB  1 
ATOM   307  C  CG  . PHE A 1 39  ? -33.18600 33.25400 33.97200  1.000 47.27671  ? 39   PHE A CG  1 
ATOM   308  C  CD1 . PHE A 1 39  ? -33.55500 33.39200 32.64100  1.000 47.31035  ? 39   PHE A CD1 1 
ATOM   309  C  CD2 . PHE A 1 39  ? -32.50300 32.10700 34.35000  1.000 46.01230  ? 39   PHE A CD2 1 
ATOM   310  C  CE1 . PHE A 1 39  ? -33.27600 32.39500 31.72500  1.000 50.01083  ? 39   PHE A CE1 1 
ATOM   311  C  CE2 . PHE A 1 39  ? -32.22600 31.11400 33.42800  1.000 56.21069  ? 39   PHE A CE2 1 
ATOM   312  C  CZ  . PHE A 1 39  ? -32.61200 31.26000 32.11900  1.000 50.87920  ? 39   PHE A CZ  1 
ATOM   313  N  N   . THR A 1 40  ? -36.77300 34.13500 34.15900  1.000 41.05508  ? 40   THR A N   1 
ATOM   314  C  CA  . THR A 1 40  ? -37.72000 34.55900 33.10500  1.000 39.28382  ? 40   THR A CA  1 
ATOM   315  C  C   . THR A 1 40  ? -39.00500 34.98200 33.78500  1.000 39.81221  ? 40   THR A C   1 
ATOM   316  O  O   . THR A 1 40  ? -39.78200 35.69500 33.16500  1.000 55.45095  ? 40   THR A O   1 
ATOM   317  C  CB  . THR A 1 40  ? -37.96700 33.41500 32.10600  1.000 42.56222  ? 40   THR A CB  1 
ATOM   318  O  OG1 . THR A 1 40  ? -36.71800 32.89800 31.64800  1.000 43.19857  ? 40   THR A OG1 1 
ATOM   319  C  CG2 . THR A 1 40  ? -38.80700 33.83000 30.91800  1.000 37.52693  ? 40   THR A CG2 1 
ATOM   320  N  N   . THR A 1 41  ? -39.17000 34.61800 35.04000  1.000 41.55212  ? 41   THR A N   1 
ATOM   321  C  CA  . THR A 1 41  ? -40.44000 34.86400 35.75900  1.000 40.87615  ? 41   THR A CA  1 
ATOM   322  C  C   . THR A 1 41  ? -40.83200 36.35100 35.72700  1.000 42.38993  ? 41   THR A C   1 
ATOM   323  O  O   . THR A 1 41  ? -42.00600 36.62900 35.47900  1.000 39.21904  ? 41   THR A O   1 
ATOM   324  C  CB  . THR A 1 41  ? -40.32300 34.26000 37.16800  1.000 49.45239  ? 41   THR A CB  1 
ATOM   325  O  OG1 . THR A 1 41  ? -39.55000 33.06300 37.10600  1.000 50.31947  ? 41   THR A OG1 1 
ATOM   326  C  CG2 . THR A 1 41  ? -41.66600 33.98500 37.80600  1.000 55.19582  ? 41   THR A CG2 1 
ATOM   327  N  N   . PRO A 1 42  ? -39.91800 37.30700 36.01200  1.000 47.74790  ? 42   PRO A N   1 
ATOM   328  C  CA  . PRO A 1 42  ? -40.26300 38.72500 36.03200  1.000 44.57541  ? 42   PRO A CA  1 
ATOM   329  C  C   . PRO A 1 42  ? -40.64300 39.19300 34.61800  1.000 57.26190  ? 42   PRO A C   1 
ATOM   330  O  O   . PRO A 1 42  ? -41.58700 39.92300 34.49000  1.000 60.85116  ? 42   PRO A O   1 
ATOM   331  C  CB  . PRO A 1 42  ? -38.97200 39.39900 36.50100  1.000 45.34456  ? 42   PRO A CB  1 
ATOM   332  C  CG  . PRO A 1 42  ? -38.18100 38.31000 37.16000  1.000 42.15228  ? 42   PRO A CG  1 
ATOM   333  C  CD  . PRO A 1 42  ? -38.50500 37.09300 36.33100  1.000 45.59530  ? 42   PRO A CD  1 
ATOM   334  N  N   . GLN A 1 43  ? -39.92700 38.72000 33.60000  1.000 50.96769  ? 43   GLN A N   1 
ATOM   335  C  CA  . GLN A 1 43  ? -40.22000 39.07000 32.18500  1.000 48.08920  ? 43   GLN A CA  1 
ATOM   336  C  C   . GLN A 1 43  ? -39.93400 40.56000 32.01500  1.000 52.67390  ? 43   GLN A C   1 
ATOM   337  O  O   . GLN A 1 43  ? -40.75300 41.25800 31.41200  1.000 53.54182  ? 43   GLN A O   1 
ATOM   338  C  CB  . GLN A 1 43  ? -41.62600 38.61700 31.78700  1.000 46.23896  ? 43   GLN A CB  1 
ATOM   339  C  CG  . GLN A 1 43  ? -41.72300 37.13700 31.45200  1.000 43.38328  ? 43   GLN A CG  1 
ATOM   340  C  CD  . GLN A 1 43  ? -43.10100 36.72900 30.99400  1.000 45.60136  ? 43   GLN A CD  1 
ATOM   341  O  OE1 . GLN A 1 43  ? -43.30300 35.64100 30.46900  1.000 47.63950  ? 43   GLN A OE1 1 
ATOM   342  N  NE2 . GLN A 1 43  ? -44.06400 37.61400 31.17400  1.000 50.85890  ? 43   GLN A NE2 1 
ATOM   343  N  N   . TYR A 1 44  ? -38.79200 41.00200 32.53500  1.000 49.10139  ? 44   TYR A N   1 
ATOM   344  C  CA  . TYR A 1 44  ? -38.39600 42.42400 32.41300  1.000 51.95953  ? 44   TYR A CA  1 
ATOM   345  C  C   . TYR A 1 44  ? -36.91500 42.49800 32.19100  1.000 47.19511  ? 44   TYR A C   1 
ATOM   346  O  O   . TYR A 1 44  ? -36.17000 41.65000 32.69600  1.000 42.57290  ? 44   TYR A O   1 
ATOM   347  C  CB  . TYR A 1 44  ? -38.84800 43.15700 33.67600  1.000 46.99952  ? 44   TYR A CB  1 
ATOM   348  C  CG  . TYR A 1 44  ? -38.76500 44.67400 33.67400  1.000 49.53407  ? 44   TYR A CG  1 
ATOM   349  C  CD1 . TYR A 1 44  ? -37.60800 45.33000 34.07100  1.000 47.16573  ? 44   TYR A CD1 1 
ATOM   350  C  CD2 . TYR A 1 44  ? -39.85800 45.44500 33.31000  1.000 58.61726  ? 44   TYR A CD2 1 
ATOM   351  C  CE1 . TYR A 1 44  ? -37.53600 46.71100 34.08100  1.000 54.83577  ? 44   TYR A CE1 1 
ATOM   352  C  CE2 . TYR A 1 44  ? -39.80100 46.82700 33.32000  1.000 56.31552  ? 44   TYR A CE2 1 
ATOM   353  C  CZ  . TYR A 1 44  ? -38.63600 47.46000 33.70800  1.000 59.65113  ? 44   TYR A CZ  1 
ATOM   354  O  OH  . TYR A 1 44  ? -38.58500 48.81900 33.71800  1.000 53.35075  ? 44   TYR A OH  1 
ATOM   355  N  N   . ALA A 1 45  ? -36.50100 43.47600 31.40000  1.000 42.70516  ? 45   ALA A N   1 
ATOM   356  C  CA  . ALA A 1 45  ? -35.06200 43.70400 31.18300  1.000 43.85795  ? 45   ALA A CA  1 
ATOM   357  C  C   . ALA A 1 45  ? -34.41100 42.47800 30.56700  1.000 45.31714  ? 45   ALA A C   1 
ATOM   358  O  O   . ALA A 1 45  ? -34.65100 42.22600 29.39100  1.000 59.39284  ? 45   ALA A O   1 
ATOM   359  C  CB  . ALA A 1 45  ? -34.37600 44.13600 32.45300  1.000 46.49121  ? 45   ALA A CB  1 
ATOM   360  N  N   . SER A 1 46  ? -33.45900 41.88800 31.27600  1.000 55.61744  ? 46   SER A N   1 
ATOM   361  C  CA  . SER A 1 46  ? -32.68300 40.76600 30.71100  1.000 45.48497  ? 46   SER A CA  1 
ATOM   362  C  C   . SER A 1 46  ? -32.71900 39.53000 31.61200  1.000 47.16779  ? 46   SER A C   1 
ATOM   363  O  O   . SER A 1 46  ? -33.45300 39.53200 32.60500  1.000 51.90709  ? 46   SER A O   1 
ATOM   364  C  CB  . SER A 1 46  ? -31.27400 41.21300 30.51800  1.000 46.72681  ? 46   SER A CB  1 
ATOM   365  O  OG  . SER A 1 46  ? -30.69700 41.61700 31.74900  1.000 53.96905  ? 46   SER A OG  1 
ATOM   366  N  N   . GLU A 1 47  ? -31.98300 38.50100 31.22100  1.000 47.45602  ? 47   GLU A N   1 
ATOM   367  C  CA  . GLU A 1 47  ? -31.83400 37.29200 32.06500  1.000 50.36443  ? 47   GLU A CA  1 
ATOM   368  C  C   . GLU A 1 47  ? -31.04600 37.69200 33.32000  1.000 50.54116  ? 47   GLU A C   1 
ATOM   369  O  O   . GLU A 1 47  ? -31.11400 36.94900 34.30200  1.000 50.90076  ? 47   GLU A O   1 
ATOM   370  C  CB  . GLU A 1 47  ? -31.11500 36.19300 31.29000  1.000 44.09047  ? 47   GLU A CB  1 
ATOM   371  C  CG  . GLU A 1 47  ? -29.70200 36.55500 30.84500  1.000 51.87855  ? 47   GLU A CG  1 
ATOM   372  C  CD  . GLU A 1 47  ? -29.60400 37.44500 29.62400  1.000 50.51843  ? 47   GLU A CD  1 
ATOM   373  O  OE1 . GLU A 1 47  ? -30.65200 37.84800 29.09200  1.000 50.68106  ? 47   GLU A OE1 1 
ATOM   374  O  OE2 . GLU A 1 47  ? -28.47100 37.73100 29.20600  1.000 50.59783  ? 47   GLU A OE2 1 
ATOM   375  N  N   . TRP A 1 48  ? -30.36000 38.83700 33.27200  1.000 44.44585  ? 48   TRP A N   1 
ATOM   376  C  CA  . TRP A 1 48  ? -29.55000 39.32700 34.41200  1.000 44.69938  ? 48   TRP A CA  1 
ATOM   377  C  C   . TRP A 1 48  ? -30.41000 40.12000 35.38600  1.000 41.70360  ? 48   TRP A C   1 
ATOM   378  O  O   . TRP A 1 48  ? -29.84100 40.84900 36.18800  1.000 51.02522  ? 48   TRP A O   1 
ATOM   379  C  CB  . TRP A 1 48  ? -28.36400 40.14400 33.90100  1.000 40.42704  ? 48   TRP A CB  1 
ATOM   380  C  CG  . TRP A 1 48  ? -27.19900 39.33000 33.41500  1.000 46.14206  ? 48   TRP A CG  1 
ATOM   381  C  CD1 . TRP A 1 48  ? -27.22600 38.10500 32.82100  1.000 47.57602  ? 48   TRP A CD1 1 
ATOM   382  C  CD2 . TRP A 1 48  ? -25.81000 39.70700 33.49800  1.000 48.20579  ? 48   TRP A CD2 1 
ATOM   383  N  NE1 . TRP A 1 48  ? -25.95500 37.69700 32.52100  1.000 53.86037  ? 48   TRP A NE1 1 
ATOM   384  C  CE2 . TRP A 1 48  ? -25.06600 38.65600 32.92700  1.000 47.58207  ? 48   TRP A CE2 1 
ATOM   385  C  CE3 . TRP A 1 48  ? -25.13100 40.82100 33.99500  1.000 43.23796  ? 48   TRP A CE3 1 
ATOM   386  C  CZ2 . TRP A 1 48  ? -23.67800 38.69300 32.84400  1.000 45.44260  ? 48   TRP A CZ2 1 
ATOM   387  C  CZ3 . TRP A 1 48  ? -23.76000 40.85500 33.91200  1.000 43.93216  ? 48   TRP A CZ3 1 
ATOM   388  C  CH2 . TRP A 1 48  ? -23.04500 39.80600 33.34300  1.000 42.96687  ? 48   TRP A CH2 1 
ATOM   389  N  N   . TYR A 1 49  ? -31.72600 39.97100 35.32600  1.000 41.92924  ? 49   TYR A N   1 
ATOM   390  C  CA  . TYR A 1 49  ? -32.60500 40.63100 36.32300  1.000 44.08147  ? 49   TYR A CA  1 
ATOM   391  C  C   . TYR A 1 49  ? -32.21000 40.17500 37.74100  1.000 48.85294  ? 49   TYR A C   1 
ATOM   392  O  O   . TYR A 1 49  ? -32.14700 41.02600 38.62300  1.000 50.35928  ? 49   TYR A O   1 
ATOM   393  C  CB  . TYR A 1 49  ? -34.08300 40.37500 36.03700  1.000 37.58032  ? 49   TYR A CB  1 
ATOM   394  C  CG  . TYR A 1 49  ? -35.14600 41.02900 36.90400  1.000 47.40418  ? 49   TYR A CG  1 
ATOM   395  C  CD1 . TYR A 1 49  ? -35.55200 40.44900 38.09700  1.000 50.29034  ? 49   TYR A CD1 1 
ATOM   396  C  CD2 . TYR A 1 49  ? -35.81500 42.16600 36.47800  1.000 45.15258  ? 49   TYR A CD2 1 
ATOM   397  C  CE1 . TYR A 1 49  ? -36.54200 41.02000 38.87500  1.000 51.38556  ? 49   TYR A CE1 1 
ATOM   398  C  CE2 . TYR A 1 49  ? -36.81200 42.74400 37.24300  1.000 50.23814  ? 49   TYR A CE2 1 
ATOM   399  C  CZ  . TYR A 1 49  ? -37.17700 42.16900 38.44500  1.000 49.24809  ? 49   TYR A CZ  1 
ATOM   400  O  OH  . TYR A 1 49  ? -38.15800 42.73100 39.20100  1.000 45.59778  ? 49   TYR A OH  1 
ATOM   401  N  N   . PRO A 1 50  ? -31.95900 38.87200 38.00800  1.000 51.97581  ? 50   PRO A N   1 
ATOM   402  C  CA  . PRO A 1 50  ? -31.51800 38.41500 39.32500  1.000 43.81711  ? 50   PRO A CA  1 
ATOM   403  C  C   . PRO A 1 50  ? -30.40600 39.31300 39.88500  1.000 45.43804  ? 50   PRO A C   1 
ATOM   404  O  O   . PRO A 1 50  ? -30.49700 39.66200 41.02200  1.000 42.88141  ? 50   PRO A O   1 
ATOM   405  C  CB  . PRO A 1 50  ? -31.01400 36.98600 39.06900  1.000 47.96232  ? 50   PRO A CB  1 
ATOM   406  C  CG  . PRO A 1 50  ? -31.06500 36.79300 37.57400  1.000 47.80696  ? 50   PRO A CG  1 
ATOM   407  C  CD  . PRO A 1 50  ? -32.13900 37.73900 37.09900  1.000 49.98521  ? 50   PRO A CD  1 
ATOM   408  N  N   . ARG A 1 51  ? -29.41400 39.63800 39.06700  1.000 38.26344  ? 51   ARG A N   1 
ATOM   409  C  CA  . ARG A 1 51  ? -28.32500 40.55200 39.47500  1.000 47.26610  ? 51   ARG A CA  1 
ATOM   410  C  C   . ARG A 1 51  ? -28.80700 42.00600 39.55200  1.000 42.85018  ? 51   ARG A C   1 
ATOM   411  O  O   . ARG A 1 51  ? -28.78200 42.55300 40.65300  1.000 49.76776  ? 51   ARG A O   1 
ATOM   412  C  CB  . ARG A 1 51  ? -27.18900 40.47600 38.46000  1.000 39.52161  ? 51   ARG A CB  1 
ATOM   413  C  CG  . ARG A 1 51  ? -26.25000 41.67100 38.47600  1.000 44.57032  ? 51   ARG A CG  1 
ATOM   414  C  CD  . ARG A 1 51  ? -25.15600 41.37500 37.48000  1.000 42.96934  ? 51   ARG A CD  1 
ATOM   415  N  NE  . ARG A 1 51  ? -24.18800 42.44200 37.31900  1.000 50.74033  ? 51   ARG A NE  1 
ATOM   416  C  CZ  . ARG A 1 51  ? -23.03400 42.50600 37.96100  1.000 47.95558  ? 51   ARG A CZ  1 
ATOM   417  N  NH1 . ARG A 1 51  ? -22.70400 41.55900 38.82000  1.000 48.84340  ? 51   ARG A NH1 1 
ATOM   418  N  NH2 . ARG A 1 51  ? -22.20600 43.50600 37.73100  1.000 46.48023  ? 51   ARG A NH2 1 
ATOM   419  N  N   . ASN A 1 52  ? -29.29400 42.57600 38.45200  1.000 44.24783  ? 52   ASN A N   1 
ATOM   420  C  CA  . ASN A 1 52  ? -29.66000 44.01300 38.36200  1.000 43.94813  ? 52   ASN A CA  1 
ATOM   421  C  C   . ASN A 1 52  ? -30.81700 44.37400 39.29700  1.000 50.00880  ? 52   ASN A C   1 
ATOM   422  O  O   . ASN A 1 52  ? -30.94000 45.55700 39.60200  1.000 60.22581  ? 52   ASN A O   1 
ATOM   423  C  CB  . ASN A 1 52  ? -29.85300 44.42800 36.90500  1.000 43.21892  ? 52   ASN A CB  1 
ATOM   424  C  CG  . ASN A 1 52  ? -28.63000 44.20900 36.05100  1.000 47.16030  ? 52   ASN A CG  1 
ATOM   425  O  OD1 . ASN A 1 52  ? -27.56200 44.75200 36.34800  1.000 58.95046  ? 52   ASN A OD1 1 
ATOM   426  N  ND2 . ASN A 1 52  ? -28.76800 43.45900 34.96900  1.000 41.23715  ? 52   ASN A ND2 1 
ATOM   427  N  N   . MET A 1 53  ? -31.62200 43.42900 39.75100  1.000 46.52987  ? 53   MET A N   1 
ATOM   428  C  CA  . MET A 1 53  ? -32.76300 43.82500 40.60800  1.000 51.56623  ? 53   MET A CA  1 
ATOM   429  C  C   . MET A 1 53  ? -32.24400 44.41600 41.93000  1.000 54.33126  ? 53   MET A C   1 
ATOM   430  O  O   . MET A 1 53  ? -33.03900 45.02900 42.65200  1.000 51.24861  ? 53   MET A O   1 
ATOM   431  C  CB  . MET A 1 53  ? -33.64600 42.62800 40.95600  1.000 44.68814  ? 53   MET A CB  1 
ATOM   432  C  CG  . MET A 1 53  ? -32.97500 41.60500 41.84700  1.000 50.34242  ? 53   MET A CG  1 
ATOM   433  S  SD  . MET A 1 53  ? -34.07100 40.28300 42.39400  1.000 52.82496  ? 53   MET A SD  1 
ATOM   434  C  CE  . MET A 1 53  ? -35.00200 41.07700 43.70500  1.000 58.10009  ? 53   MET A CE  1 
ATOM   435  N  N   . TYR A 1 54  ? -30.97300 44.19000 42.24100  1.000 53.92088  ? 54   TYR A N   1 
ATOM   436  C  CA  . TYR A 1 54  ? -30.38300 44.68100 43.51000  1.000 58.19506  ? 54   TYR A CA  1 
ATOM   437  C  C   . TYR A 1 54  ? -29.39900 45.80600 43.20500  1.000 52.49780  ? 54   TYR A C   1 
ATOM   438  O  O   . TYR A 1 54  ? -28.89400 46.42500 44.14600  1.000 61.15994  ? 54   TYR A O   1 
ATOM   439  C  CB  . TYR A 1 54  ? -29.65800 43.56800 44.27500  1.000 55.85435  ? 54   TYR A CB  1 
ATOM   440  C  CG  . TYR A 1 54  ? -30.43100 42.32800 44.69600  1.000 59.17698  ? 54   TYR A CG  1 
ATOM   441  C  CD1 . TYR A 1 54  ? -31.18100 42.32000 45.86300  1.000 57.47773  ? 54   TYR A CD1 1 
ATOM   442  C  CD2 . TYR A 1 54  ? -30.31400 41.13500 43.99500  1.000 55.82793  ? 54   TYR A CD2 1 
ATOM   443  C  CE1 . TYR A 1 54  ? -31.86500 41.18800 46.27100  1.000 65.76702  ? 54   TYR A CE1 1 
ATOM   444  C  CE2 . TYR A 1 54  ? -30.98200 39.99200 44.39800  1.000 47.76077  ? 54   TYR A CE2 1 
ATOM   445  C  CZ  . TYR A 1 54  ? -31.76100 40.02000 45.53900  1.000 58.07906  ? 54   TYR A CZ  1 
ATOM   446  O  OH  . TYR A 1 54  ? -32.42400 38.90300 45.94900  1.000 55.08600  ? 54   TYR A OH  1 
ATOM   447  N  N   . GLU A 1 55  ? -29.07600 46.02100 41.92600  1.000 48.58601  ? 55   GLU A N   1 
ATOM   448  C  CA  . GLU A 1 55  ? -28.14900 47.10300 41.49900  1.000 49.87492  ? 55   GLU A CA  1 
ATOM   449  C  C   . GLU A 1 55  ? -28.68100 48.42800 42.03100  1.000 56.00172  ? 55   GLU A C   1 
ATOM   450  O  O   . GLU A 1 55  ? -29.85100 48.74400 41.79500  1.000 59.04474  ? 55   GLU A O   1 
ATOM   451  C  CB  . GLU A 1 55  ? -28.03900 47.18400 39.97600  1.000 56.62905  ? 55   GLU A CB  1 
ATOM   452  C  CG  . GLU A 1 55  ? -26.85300 47.96200 39.42600  1.000 53.18838  ? 55   GLU A CG  1 
ATOM   453  C  CD  . GLU A 1 55  ? -26.73600 47.94400 37.90400  1.000 63.34139  ? 55   GLU A CD  1 
ATOM   454  O  OE1 . GLU A 1 55  ? -27.74100 47.63700 37.24100  1.000 67.91651  ? 55   GLU A OE1 1 
ATOM   455  O  OE2 . GLU A 1 55  ? -25.63500 48.21600 37.40000  1.000 61.69197  ? 55   GLU A OE2 1 
ATOM   456  N  N   . PRO A 1 56  ? -27.86400 49.19100 42.77700  1.000 65.96654  ? 56   PRO A N   1 
ATOM   457  C  CA  . PRO A 1 56  ? -28.29800 50.49100 43.31600  1.000 54.89168  ? 56   PRO A CA  1 
ATOM   458  C  C   . PRO A 1 56  ? -28.67000 51.45800 42.20300  1.000 51.92571  ? 56   PRO A C   1 
ATOM   459  O  O   . PRO A 1 56  ? -27.86200 51.76400 41.32400  1.000 57.19822  ? 56   PRO A O   1 
ATOM   460  C  CB  . PRO A 1 56  ? -27.07100 50.97500 44.09900  1.000 51.41258  ? 56   PRO A CB  1 
ATOM   461  C  CG  . PRO A 1 56  ? -26.27300 49.74000 44.37200  1.000 47.40032  ? 56   PRO A CG  1 
ATOM   462  C  CD  . PRO A 1 56  ? -26.49100 48.85400 43.18600  1.000 59.15930  ? 56   PRO A CD  1 
ATOM   463  N  N   . GLY A 1 57  ? -29.91100 51.93800 42.24600  1.000 51.17112  ? 57   GLY A N   1 
ATOM   464  C  CA  . GLY A 1 57  ? -30.37400 52.91600 41.28300  1.000 58.03820  ? 57   GLY A CA  1 
ATOM   465  C  C   . GLY A 1 57  ? -30.67000 52.38200 39.90100  1.000 57.91893  ? 57   GLY A C   1 
ATOM   466  O  O   . GLY A 1 57  ? -30.81300 53.17600 38.96600  1.000 59.62782  ? 57   GLY A O   1 
ATOM   467  N  N   . SER A 1 58  ? -30.87900 51.06400 39.79500  1.000 56.33810  ? 58   SER A N   1 
ATOM   468  C  CA  . SER A 1 58  ? -31.18100 50.40900 38.49800  1.000 47.68777  ? 58   SER A CA  1 
ATOM   469  C  C   . SER A 1 58  ? -32.66200 50.55900 38.16100  1.000 50.08515  ? 58   SER A C   1 
ATOM   470  O  O   . SER A 1 58  ? -33.46700 50.67400 39.09500  1.000 53.06921  ? 58   SER A O   1 
ATOM   471  C  CB  . SER A 1 58  ? -30.82800 48.94000 38.53900  1.000 50.35919  ? 58   SER A CB  1 
ATOM   472  O  OG  . SER A 1 58  ? -31.79900 48.20000 39.26200  1.000 47.04030  ? 58   SER A OG  1 
ATOM   473  N  N   . ASP A 1 59  ? -33.00100 50.52400 36.87500  1.000 39.29322  ? 59   ASP A N   1 
ATOM   474  C  CA  . ASP A 1 59  ? -34.43700 50.50900 36.48800  1.000 43.83689  ? 59   ASP A CA  1 
ATOM   475  C  C   . ASP A 1 59  ? -35.04300 49.19300 36.97400  1.000 47.48765  ? 59   ASP A C   1 
ATOM   476  O  O   . ASP A 1 59  ? -36.21900 49.18000 37.36700  1.000 50.15896  ? 59   ASP A O   1 
ATOM   477  C  CB  . ASP A 1 59  ? -34.62300 50.71600 34.99500  1.000 41.88834  ? 59   ASP A CB  1 
ATOM   478  C  CG  . ASP A 1 59  ? -36.02300 50.43900 34.47700  1.000 58.15092  ? 59   ASP A CG  1 
ATOM   479  O  OD1 . ASP A 1 59  ? -36.94500 51.17600 34.87000  1.000 58.22450  ? 59   ASP A OD1 1 
ATOM   480  O  OD2 . ASP A 1 59  ? -36.17600 49.47800 33.70100  1.000 59.16123  ? 59   ASP A OD2 1 
ATOM   481  N  N   . GLN A 1 60  ? -34.25400 48.12700 36.97100  1.000 44.78460  ? 60   GLN A N   1 
ATOM   482  C  CA  . GLN A 1 60  ? -34.75800 46.81500 37.44600  1.000 51.63337  ? 60   GLN A CA  1 
ATOM   483  C  C   . GLN A 1 60  ? -35.18000 46.95400 38.91900  1.000 55.88633  ? 60   GLN A C   1 
ATOM   484  O  O   . GLN A 1 60  ? -36.29500 46.52400 39.25800  1.000 50.69109  ? 60   GLN A O   1 
ATOM   485  C  CB  . GLN A 1 60  ? -33.70000 45.76100 37.12700  1.000 43.33744  ? 60   GLN A CB  1 
ATOM   486  C  CG  . GLN A 1 60  ? -33.40100 45.62600 35.64000  1.000 44.97203  ? 60   GLN A CG  1 
ATOM   487  C  CD  . GLN A 1 60  ? -32.20600 46.43800 35.19700  1.000 52.13380  ? 60   GLN A CD  1 
ATOM   488  O  OE1 . GLN A 1 60  ? -32.01500 47.58100 35.62000  1.000 56.20187  ? 60   GLN A OE1 1 
ATOM   489  N  NE2 . GLN A 1 60  ? -31.37200 45.84200 34.36000  1.000 47.86334  ? 60   GLN A NE2 1 
ATOM   490  N  N   . ARG A 1 61  ? -34.33000 47.57500 39.74000  1.000 53.30359  ? 61   ARG A N   1 
ATOM   491  C  CA  . ARG A 1 61  ? -34.65600 47.75600 41.17300  1.000 48.84175  ? 61   ARG A CA  1 
ATOM   492  C  C   . ARG A 1 61  ? -35.93100 48.58300 41.28300  1.000 53.76145  ? 61   ARG A C   1 
ATOM   493  O  O   . ARG A 1 61  ? -36.79800 48.24300 42.10700  1.000 48.64876  ? 61   ARG A O   1 
ATOM   494  C  CB  . ARG A 1 61  ? -33.50100 48.42600 41.91600  1.000 53.20426  ? 61   ARG A CB  1 
ATOM   495  C  CG  . ARG A 1 61  ? -33.79900 48.93000 43.32000  1.000 50.46691  ? 61   ARG A CG  1 
ATOM   496  C  CD  . ARG A 1 61  ? -32.59400 49.66800 43.87800  1.000 51.32443  ? 61   ARG A CD  1 
ATOM   497  N  NE  . ARG A 1 61  ? -31.52300 48.82200 44.41400  1.000 48.93920  ? 61   ARG A NE  1 
ATOM   498  C  CZ  . ARG A 1 61  ? -31.64100 48.04700 45.48200  1.000 61.17404  ? 61   ARG A CZ  1 
ATOM   499  N  NH1 . ARG A 1 61  ? -32.69700 48.14900 46.26600  1.000 61.74072  ? 61   ARG A NH1 1 
ATOM   500  N  NH2 . ARG A 1 61  ? -30.68000 47.20500 45.79500  1.000 51.40698  ? 61   ARG A NH2 1 
ATOM   501  N  N   . LYS A 1 62  ? -36.03200 49.62600 40.45600  1.000 52.13217  ? 62   LYS A N   1 
ATOM   502  C  CA  . LYS A 1 62  ? -37.25400 50.42300 40.51000  1.000 42.99731  ? 62   LYS A CA  1 
ATOM   503  C  C   . LYS A 1 62  ? -38.46700 49.58900 40.11700  1.000 52.65272  ? 62   LYS A C   1 
ATOM   504  O  O   . LYS A 1 62  ? -39.51400 49.64400 40.77400  1.000 56.70886  ? 62   LYS A O   1 
ATOM   505  C  CB  . LYS A 1 62  ? -37.12000 51.64600 39.60200  1.000 45.46243  ? 62   LYS A CB  1 
ATOM   506  C  CG  . LYS A 1 62  ? -38.38200 52.48700 39.49700  1.000 64.51194  ? 62   LYS A CG  1 
ATOM   507  C  CD  . LYS A 1 62  ? -38.19500 53.64500 38.53000  1.000 63.67933  ? 62   LYS A CD  1 
ATOM   508  N  N   . HIS A 1 63  ? -38.34000 48.80400 39.04200  1.000 60.54658  ? 63   HIS A N   1 
ATOM   509  C  CA  . HIS A 1 63  ? -39.44000 47.94500 38.61400  1.000 58.47400  ? 63   HIS A CA  1 
ATOM   510  C  C   . HIS A 1 63  ? -39.78500 46.91600 39.68300  1.000 53.50343  ? 63   HIS A C   1 
ATOM   511  O  O   . HIS A 1 63  ? -40.96400 46.67200 39.96200  1.000 59.78563  ? 63   HIS A O   1 
ATOM   512  C  CB  . HIS A 1 63  ? -39.08300 47.25100 37.29900  1.000 53.62511  ? 63   HIS A CB  1 
ATOM   513  C  CG  . HIS A 1 63  ? -40.07000 46.20700 36.87900  1.000 53.73678  ? 63   HIS A CG  1 
ATOM   514  N  ND1 . HIS A 1 63  ? -41.26100 46.51400 36.25600  1.000 60.49988  ? 63   HIS A ND1 1 
ATOM   515  C  CD2 . HIS A 1 63  ? -40.04600 44.85800 36.99600  1.000 55.73845  ? 63   HIS A CD2 1 
ATOM   516  C  CE1 . HIS A 1 63  ? -41.92600 45.40000 36.00600  1.000 58.21102  ? 63   HIS A CE1 1 
ATOM   517  N  NE2 . HIS A 1 63  ? -41.21100 44.38100 36.44600  1.000 56.87498  ? 63   HIS A NE2 1 
ATOM   518  N  N   . HIS A 1 64  ? -38.76600 46.30700 40.29600  1.000 49.43059  ? 64   HIS A N   1 
ATOM   519  C  CA  . HIS A 1 64  ? -39.01100 45.30900 41.33100  1.000 59.76845  ? 64   HIS A CA  1 
ATOM   520  C  C   . HIS A 1 64  ? -39.69700 45.92800 42.54100  1.000 59.66538  ? 64   HIS A C   1 
ATOM   521  O  O   . HIS A 1 64  ? -40.61100 45.32900 43.12100  1.000 53.00054  ? 64   HIS A O   1 
ATOM   522  C  CB  . HIS A 1 64  ? -37.69300 44.65200 41.74100  1.000 56.80361  ? 64   HIS A CB  1 
ATOM   523  C  CG  . HIS A 1 64  ? -37.86400 43.40900 42.55500  1.000 64.25451  ? 64   HIS A CG  1 
ATOM   524  N  ND1 . HIS A 1 64  ? -38.19100 42.19300 41.99500  1.000 63.17572  ? 64   HIS A ND1 1 
ATOM   525  C  CD2 . HIS A 1 64  ? -37.75600 43.19300 43.88800  1.000 65.16773  ? 64   HIS A CD2 1 
ATOM   526  C  CE1 . HIS A 1 64  ? -38.27600 41.28100 42.94600  1.000 60.40957  ? 64   HIS A CE1 1 
ATOM   527  N  NE2 . HIS A 1 64  ? -38.01700 41.86100 44.10400  1.000 61.64547  ? 64   HIS A NE2 1 
ATOM   528  N  N   . THR A 1 65  ? -39.27500 47.13300 42.93200  1.000 55.18816  ? 65   THR A N   1 
ATOM   529  C  CA  . THR A 1 65  ? -39.88100 47.79600 44.08100  1.000 49.34259  ? 65   THR A CA  1 
ATOM   530  C  C   . THR A 1 65  ? -41.32300 48.19100 43.79200  1.000 57.16007  ? 65   THR A C   1 
ATOM   531  O  O   . THR A 1 65  ? -42.19600 48.05200 44.65700  1.000 67.53016  ? 65   THR A O   1 
ATOM   532  C  CB  . THR A 1 65  ? -39.05300 49.02000 44.47500  1.000 53.55058  ? 65   THR A CB  1 
ATOM   533  O  OG1 . THR A 1 65  ? -37.72500 48.60800 44.82500  1.000 58.31859  ? 65   THR A OG1 1 
ATOM   534  C  CG2 . THR A 1 65  ? -39.68100 49.73600 45.66300  1.000 56.42565  ? 65   THR A CG2 1 
ATOM   535  N  N   . GLU A 1 66  ? -41.59700 48.67600 42.58100  1.000 58.72050  ? 66   GLU A N   1 
ATOM   536  C  CA  . GLU A 1 66  ? -42.95300 49.07400 42.22100  1.000 64.34360  ? 66   GLU A CA  1 
ATOM   537  C  C   . GLU A 1 66  ? -43.87400 47.88700 41.97100  1.000 61.95442  ? 66   GLU A C   1 
ATOM   538  O  O   . GLU A 1 66  ? -45.09600 48.04000 42.07300  1.000 52.11572  ? 66   GLU A O   1 
ATOM   539  C  CB  . GLU A 1 66  ? -42.92600 49.96900 40.98000  1.000 65.30179  ? 66   GLU A CB  1 
ATOM   540  C  CG  . GLU A 1 66  ? -42.22400 51.29900 41.18900  1.000 77.95319  ? 66   GLU A CG  1 
ATOM   541  C  CD  . GLU A 1 66  ? -42.09000 52.09000 39.90500  1.000 86.95743  ? 66   GLU A CD  1 
ATOM   542  O  OE1 . GLU A 1 66  ? -42.51200 51.57900 38.84500  1.000 73.37815  ? 66   GLU A OE1 1 
ATOM   543  O  OE2 . GLU A 1 66  ? -41.56300 53.22200 39.95300  1.000 92.70548  ? 66   GLU A OE2 1 
ATOM   544  N  N   . THR A 1 67  ? -43.32900 46.70100 41.70200  1.000 63.34104  ? 67   THR A N   1 
ATOM   545  C  CA  . THR A 1 67  ? -44.19100 45.53900 41.36100  1.000 56.77272  ? 67   THR A CA  1 
ATOM   546  C  C   . THR A 1 67  ? -44.28300 44.56100 42.51200  1.000 55.47792  ? 67   THR A C   1 
ATOM   547  O  O   . THR A 1 67  ? -45.41000 44.21000 42.88200  1.000 50.19422  ? 67   THR A O   1 
ATOM   548  C  CB  . THR A 1 67  ? -43.66700 44.88300 40.08700  1.000 57.55331  ? 67   THR A CB  1 
ATOM   549  O  OG1 . THR A 1 67  ? -43.32000 45.94200 39.20200  1.000 58.82918  ? 67   THR A OG1 1 
ATOM   550  C  CG2 . THR A 1 67  ? -44.69900 43.97800 39.44000  1.000 56.62493  ? 67   THR A CG2 1 
ATOM   551  N  N   . TYR A 1 68  ? -43.15400 44.15800 43.07900  1.000 56.02472  ? 68   TYR A N   1 
ATOM   552  C  CA  . TYR A 1 68  ? -43.18200 43.12300 44.14100  1.000 62.10576  ? 68   TYR A CA  1 
ATOM   553  C  C   . TYR A 1 68  ? -42.80000 43.69800 45.50900  1.000 62.47802  ? 68   TYR A C   1 
ATOM   554  O  O   . TYR A 1 68  ? -43.31600 43.19800 46.50900  1.000 60.34695  ? 68   TYR A O   1 
ATOM   555  C  CB  . TYR A 1 68  ? -42.24300 41.97900 43.75900  1.000 59.67090  ? 68   TYR A CB  1 
ATOM   556  C  CG  . TYR A 1 68  ? -42.28300 41.54100 42.31800  1.000 61.59393  ? 68   TYR A CG  1 
ATOM   557  C  CD1 . TYR A 1 68  ? -43.31600 40.75300 41.84100  1.000 57.12344  ? 68   TYR A CD1 1 
ATOM   558  C  CD2 . TYR A 1 68  ? -41.27400 41.89000 41.43900  1.000 59.82393  ? 68   TYR A CD2 1 
ATOM   559  C  CE1 . TYR A 1 68  ? -43.35200 40.33600 40.52200  1.000 58.47661  ? 68   TYR A CE1 1 
ATOM   560  C  CE2 . TYR A 1 68  ? -41.29500 41.48200 40.11700  1.000 55.17202  ? 68   TYR A CE2 1 
ATOM   561  C  CZ  . TYR A 1 68  ? -42.33800 40.70100 39.65800  1.000 61.84091  ? 68   TYR A CZ  1 
ATOM   562  O  OH  . TYR A 1 68  ? -42.36800 40.29300 38.35700  1.000 66.92171  ? 68   TYR A OH  1 
ATOM   563  N  N   . GLY A 1 69  ? -41.93000 44.71000 45.54700  1.000 66.31174  ? 69   GLY A N   1 
ATOM   564  C  CA  . GLY A 1 69  ? -41.46000 45.25500 46.79600  1.000 56.89912  ? 69   GLY A CA  1 
ATOM   565  C  C   . GLY A 1 69  ? -39.95900 45.45000 46.76900  1.000 60.17202  ? 69   GLY A C   1 
ATOM   566  O  O   . GLY A 1 69  ? -39.28600 45.09200 45.79800  1.000 63.43370  ? 69   GLY A O   1 
ATOM   567  N  N   . PRO A 1 70  ? -39.40500 46.03100 47.82900  1.000 66.08623  ? 70   PRO A N   1 
ATOM   568  C  CA  . PRO A 1 70  ? -37.95200 46.22000 47.89900  1.000 57.96116  ? 70   PRO A CA  1 
ATOM   569  C  C   . PRO A 1 70  ? -37.22900 44.88900 47.81100  1.000 63.09039  ? 70   PRO A C   1 
ATOM   570  O  O   . PRO A 1 70  ? -37.61900 43.91600 48.47400  1.000 64.67641  ? 70   PRO A O   1 
ATOM   571  C  CB  . PRO A 1 70  ? -37.74600 46.87800 49.27200  1.000 56.72704  ? 70   PRO A CB  1 
ATOM   572  C  CG  . PRO A 1 70  ? -39.05600 47.52100 49.58200  1.000 57.80867  ? 70   PRO A CG  1 
ATOM   573  C  CD  . PRO A 1 70  ? -40.09700 46.61500 48.99000  1.000 71.31198  ? 70   PRO A CD  1 
ATOM   574  N  N   . PRO A 1 71  ? -36.17700 44.80200 46.99300  1.000 63.75486  ? 71   PRO A N   1 
ATOM   575  C  CA  . PRO A 1 71  ? -35.44500 43.53000 46.87200  1.000 64.06110  ? 71   PRO A CA  1 
ATOM   576  C  C   . PRO A 1 71  ? -34.81800 43.06700 48.17400  1.000 65.30750  ? 71   PRO A C   1 
ATOM   577  O  O   . PRO A 1 71  ? -34.58900 41.86200 48.33900  1.000 59.81592  ? 71   PRO A O   1 
ATOM   578  C  CB  . PRO A 1 71  ? -34.37900 43.83700 45.81000  1.000 60.97017  ? 71   PRO A CB  1 
ATOM   579  C  CG  . PRO A 1 71  ? -34.24000 45.32800 45.82600  1.000 61.72345  ? 71   PRO A CG  1 
ATOM   580  C  CD  . PRO A 1 71  ? -35.60200 45.86000 46.14600  1.000 59.48271  ? 71   PRO A CD  1 
ATOM   581  N  N   . GLU A 1 72  ? -34.53600 43.98000 49.10500  1.000 62.62903  ? 72   GLU A N   1 
ATOM   582  C  CA  . GLU A 1 72  ? -34.06800 43.57600 50.42500  1.000 60.84087  ? 72   GLU A CA  1 
ATOM   583  C  C   . GLU A 1 72  ? -35.14900 42.84200 51.20900  1.000 60.32894  ? 72   GLU A C   1 
ATOM   584  O  O   . GLU A 1 72  ? -34.83100 42.13300 52.16900  1.000 61.84305  ? 72   GLU A O   1 
ATOM   585  C  CB  . GLU A 1 72  ? -33.58200 44.79500 51.21200  1.000 58.67895  ? 72   GLU A CB  1 
ATOM   586  C  CG  . GLU A 1 72  ? -32.34300 45.47200 50.63200  1.000 62.51761  ? 72   GLU A CG  1 
ATOM   587  C  CD  . GLU A 1 72  ? -32.64300 46.29600 49.39400  1.000 67.57329  ? 72   GLU A CD  1 
ATOM   588  O  OE1 . GLU A 1 72  ? -33.78900 46.77500 49.26000  1.000 72.12284  ? 72   GLU A OE1 1 
ATOM   589  O  OE2 . GLU A 1 72  ? -31.73400 46.45800 48.55300  1.000 76.94224  ? 72   GLU A OE2 1 
ATOM   590  N  N   . GLU A 1 73  ? -36.40700 43.06500 50.86100  1.000 63.07190  ? 73   GLU A N   1 
ATOM   591  C  CA  A GLU A 1 73  ? -37.51700 42.31400 51.50400  0.546 64.02874  ? 73   GLU A CA  1 
ATOM   592  C  CA  B GLU A 1 73  ? -37.52900 42.33300 51.49800  0.454 64.03955  ? 73   GLU A CA  1 
ATOM   593  C  C   . GLU A 1 73  ? -38.14300 41.20800 50.62100  1.000 65.64764  ? 73   GLU A C   1 
ATOM   594  O  O   . GLU A 1 73  ? -38.63500 40.12800 51.08100  1.000 69.10443  ? 73   GLU A O   1 
ATOM   595  C  CB  A GLU A 1 73  ? -38.63500 43.27200 51.90300  0.546 68.23842  ? 73   GLU A CB  1 
ATOM   596  C  CB  B GLU A 1 73  ? -38.56100 43.38300 51.90700  0.454 68.21113  ? 73   GLU A CB  1 
ATOM   597  C  CG  A GLU A 1 73  ? -38.15700 44.48000 52.68200  0.546 66.44518  ? 73   GLU A CG  1 
ATOM   598  C  CG  B GLU A 1 73  ? -39.78300 42.82400 52.60500  0.454 72.36134  ? 73   GLU A CG  1 
ATOM   599  C  CD  A GLU A 1 73  ? -39.27900 45.42300 53.07700  0.546 70.09032  ? 73   GLU A CD  1 
ATOM   600  C  CD  B GLU A 1 73  ? -40.74800 43.90300 53.06400  0.454 72.05445  ? 73   GLU A CD  1 
ATOM   601  O  OE1 A GLU A 1 73  ? -40.45400 45.03400 52.93200  0.546 70.23387  ? 73   GLU A OE1 1 
ATOM   602  O  OE1 B GLU A 1 73  ? -40.43900 45.09300 52.86000  0.454 70.21534  ? 73   GLU A OE1 1 
ATOM   603  O  OE2 A GLU A 1 73  ? -38.97300 46.54500 53.52300  0.546 72.33163  ? 73   GLU A OE2 1 
ATOM   604  O  OE2 B GLU A 1 73  ? -41.80400 43.55300 53.62500  0.454 76.99393  ? 73   GLU A OE2 1 
ATOM   605  N  N   . TRP A 1 74  ? -38.18700 41.48100 49.31500  1.000 62.19016  ? 74   TRP A N   1 
ATOM   606  C  CA  . TRP A 1 74  ? -38.78800 40.50000 48.37200  1.000 59.32120  ? 74   TRP A CA  1 
ATOM   607  C  C   . TRP A 1 74  ? -37.68200 40.12500 47.40300  1.000 66.19722  ? 74   TRP A C   1 
ATOM   608  O  O   . TRP A 1 74  ? -37.58500 40.77000 46.36500  1.000 69.28580  ? 74   TRP A O   1 
ATOM   609  C  CB  . TRP A 1 74  ? -39.98700 41.11900 47.65900  1.000 56.55906  ? 74   TRP A CB  1 
ATOM   610  C  CG  . TRP A 1 74  ? -40.99300 40.19300 47.04800  1.000 66.12362  ? 74   TRP A CG  1 
ATOM   611  C  CD1 . TRP A 1 74  ? -42.26800 39.97800 47.48400  1.000 57.70010  ? 74   TRP A CD1 1 
ATOM   612  C  CD2 . TRP A 1 74  ? -40.84000 39.39800 45.86000  1.000 60.59856  ? 74   TRP A CD2 1 
ATOM   613  N  NE1 . TRP A 1 74  ? -42.91000 39.09600 46.66200  1.000 53.04372  ? 74   TRP A NE1 1 
ATOM   614  C  CE2 . TRP A 1 74  ? -42.05900 38.72200 45.65800  1.000 58.52668  ? 74   TRP A CE2 1 
ATOM   615  C  CE3 . TRP A 1 74  ? -39.79500 39.18200 44.95700  1.000 64.72542  ? 74   TRP A CE3 1 
ATOM   616  C  CZ2 . TRP A 1 74  ? -42.25600 37.84700 44.59200  1.000 57.49008  ? 74   TRP A CZ2 1 
ATOM   617  C  CZ3 . TRP A 1 74  ? -39.99200 38.31900 43.90300  1.000 53.71397  ? 74   TRP A CZ3 1 
ATOM   618  C  CH2 . TRP A 1 74  ? -41.20600 37.66200 43.72700  1.000 50.06383  ? 74   TRP A CH2 1 
ATOM   619  N  N   . GLY A 1 75  ? -36.86400 39.13900 47.75800  1.000 61.30323  ? 75   GLY A N   1 
ATOM   620  C  CA  . GLY A 1 75  ? -35.70000 38.78600 46.93200  1.000 52.03711  ? 75   GLY A CA  1 
ATOM   621  C  C   . GLY A 1 75  ? -36.00000 37.76700 45.85500  1.000 58.81456  ? 75   GLY A C   1 
ATOM   622  O  O   . GLY A 1 75  ? -37.14700 37.32200 45.77000  1.000 59.56364  ? 75   GLY A O   1 
ATOM   623  N  N   . TYR A 1 76  ? -34.98200 37.39100 45.09300  1.000 49.77182  ? 76   TYR A N   1 
ATOM   624  C  CA  . TYR A 1 76  ? -35.14200 36.47400 43.96700  1.000 53.66088  ? 76   TYR A CA  1 
ATOM   625  C  C   . TYR A 1 76  ? -35.56400 35.08400 44.43400  1.000 53.14157  ? 76   TYR A C   1 
ATOM   626  O  O   . TYR A 1 76  ? -36.23200 34.34200 43.69400  1.000 59.88582  ? 76   TYR A O   1 
ATOM   627  C  CB  . TYR A 1 76  ? -33.82900 36.41900 43.18700  1.000 53.80778  ? 76   TYR A CB  1 
ATOM   628  C  CG  . TYR A 1 76  ? -33.85400 35.55800 41.95400  1.000 53.74011  ? 76   TYR A CG  1 
ATOM   629  C  CD1 . TYR A 1 76  ? -34.48500 35.98800 40.79700  1.000 46.49178  ? 76   TYR A CD1 1 
ATOM   630  C  CD2 . TYR A 1 76  ? -33.22400 34.32300 41.93900  1.000 52.67997  ? 76   TYR A CD2 1 
ATOM   631  C  CE1 . TYR A 1 76  ? -34.50400 35.20300 39.66200  1.000 50.85392  ? 76   TYR A CE1 1 
ATOM   632  C  CE2 . TYR A 1 76  ? -33.23500 33.53300 40.81100  1.000 54.84994  ? 76   TYR A CE2 1 
ATOM   633  C  CZ  . TYR A 1 76  ? -33.87400 33.97700 39.67400  1.000 52.07569  ? 76   TYR A CZ  1 
ATOM   634  O  OH  . TYR A 1 76  ? -33.88100 33.18700 38.55100  1.000 50.84118  ? 76   TYR A OH  1 
ATOM   635  N  N   . ALA A 1 77  ? -35.19400 34.72200 45.66400  1.000 50.20665  ? 77   ALA A N   1 
ATOM   636  C  CA  . ALA A 1 77  ? -35.68300 33.48700 46.25900  1.000 54.39954  ? 77   ALA A CA  1 
ATOM   637  C  C   . ALA A 1 77  ? -37.20200 33.45400 46.33700  1.000 58.60595  ? 77   ALA A C   1 
ATOM   638  O  O   . ALA A 1 77  ? -37.77700 32.37200 46.47500  1.000 68.03914  ? 77   ALA A O   1 
ATOM   639  C  CB  . ALA A 1 77  ? -35.08000 33.29900 47.65100  1.000 52.47593  ? 77   ALA A CB  1 
ATOM   640  N  N   . ASN A 1 78  ? -37.86600 34.61000 46.25100  1.000 56.07938  ? 78   ASN A N   1 
ATOM   641  C  CA  . ASN A 1 78  ? -39.32100 34.61100 46.14600  1.000 51.75555  ? 78   ASN A CA  1 
ATOM   642  C  C   . ASN A 1 78  ? -39.78100 34.24000 44.74200  1.000 58.37668  ? 78   ASN A C   1 
ATOM   643  O  O   . ASN A 1 78  ? -40.82400 33.59600 44.58700  1.000 59.81578  ? 78   ASN A O   1 
ATOM   644  C  CB  . ASN A 1 78  ? -39.88400 35.97400 46.54700  1.000 61.36586  ? 78   ASN A CB  1 
ATOM   645  C  CG  . ASN A 1 78  ? -39.84000 36.20300 48.04400  1.000 59.26263  ? 78   ASN A CG  1 
ATOM   646  O  OD1 . ASN A 1 78  ? -39.24400 35.42300 48.78600  1.000 72.40661  ? 78   ASN A OD1 1 
ATOM   647  N  ND2 . ASN A 1 78  ? -40.47200 37.28000 48.49500  1.000 67.92338  ? 78   ASN A ND2 1 
ATOM   648  N  N   . PHE A 1 79  ? -39.02900 34.63800 43.71200  1.000 53.41823  ? 79   PHE A N   1 
ATOM   649  C  CA  . PHE A 1 79  ? -39.30400 34.12900 42.37300  1.000 53.17207  ? 79   PHE A CA  1 
ATOM   650  C  C   . PHE A 1 79  ? -39.13400 32.61900 42.32700  1.000 56.66733  ? 79   PHE A C   1 
ATOM   651  O  O   . PHE A 1 79  ? -39.88600 31.92000 41.63700  1.000 57.89927  ? 79   PHE A O   1 
ATOM   652  C  CB  . PHE A 1 79  ? -38.38700 34.78800 41.34300  1.000 54.70500  ? 79   PHE A CB  1 
ATOM   653  C  CG  . PHE A 1 79  ? -38.73400 36.21400 41.04000  1.000 54.30125  ? 79   PHE A CG  1 
ATOM   654  C  CD1 . PHE A 1 79  ? -39.96000 36.53700 40.48300  1.000 51.32894  ? 79   PHE A CD1 1 
ATOM   655  C  CD2 . PHE A 1 79  ? -37.82700 37.22900 41.29100  1.000 47.42817  ? 79   PHE A CD2 1 
ATOM   656  C  CE1 . PHE A 1 79  ? -40.28100 37.85000 40.19800  1.000 59.38707  ? 79   PHE A CE1 1 
ATOM   657  C  CE2 . PHE A 1 79  ? -38.14100 38.54300 41.00600  1.000 52.44013  ? 79   PHE A CE2 1 
ATOM   658  C  CZ  . PHE A 1 79  ? -39.37000 38.85400 40.46000  1.000 62.03429  ? 79   PHE A CZ  1 
ATOM   659  N  N   . ILE A 1 80  ? -38.14800 32.09700 43.05700  1.000 65.17546  ? 80   ILE A N   1 
ATOM   660  C  CA  . ILE A 1 80  ? -37.92000 30.65400 43.02600  1.000 48.65688  ? 80   ILE A CA  1 
ATOM   661  C  C   . ILE A 1 80  ? -38.96500 29.90700 43.85400  1.000 52.54227  ? 80   ILE A C   1 
ATOM   662  O  O   . ILE A 1 80  ? -39.51400 28.89400 43.40800  1.000 55.80864  ? 80   ILE A O   1 
ATOM   663  C  CB  . ILE A 1 80  ? -36.48700 30.33200 43.48500  1.000 58.59392  ? 80   ILE A CB  1 
ATOM   664  C  CG1 . ILE A 1 80  ? -35.48700 30.75300 42.40500  1.000 47.75273  ? 80   ILE A CG1 1 
ATOM   665  C  CG2 . ILE A 1 80  ? -36.34400 28.84900 43.80400  1.000 59.01215  ? 80   ILE A CG2 1 
ATOM   666  C  CD1 . ILE A 1 80  ? -34.04600 30.47700 42.76300  1.000 47.99327  ? 80   ILE A CD1 1 
ATOM   667  N  N   . ASN A 1 81  ? -39.21800 30.36900 45.07600  1.000 64.40844  ? 81   ASN A N   1 
ATOM   668  C  CA  . ASN A 1 81  ? -40.06600 29.60100 46.03200  1.000 72.41977  ? 81   ASN A CA  1 
ATOM   669  C  C   . ASN A 1 81  ? -41.52700 30.03700 46.01600  1.000 67.50940  ? 81   ASN A C   1 
ATOM   670  O  O   . ASN A 1 81  ? -42.35300 29.30300 46.57200  1.000 69.88155  ? 81   ASN A O   1 
ATOM   671  C  CB  . ASN A 1 81  ? -39.48400 29.66100 47.45000  1.000 59.06707  ? 81   ASN A CB  1 
ATOM   672  C  CG  . ASN A 1 81  ? -38.14100 28.97900 47.57800  1.000 56.34629  ? 81   ASN A CG  1 
ATOM   673  O  OD1 . ASN A 1 81  ? -38.00300 27.80600 47.25100  1.000 66.89744  ? 81   ASN A OD1 1 
ATOM   674  N  ND2 . ASN A 1 81  ? -37.15500 29.69200 48.09200  1.000 55.69980  ? 81   ASN A ND2 1 
ATOM   675  N  N   . GLY A 1 82  ? -41.83900 31.18400 45.43600  1.000 58.92369  ? 82   GLY A N   1 
ATOM   676  C  CA  . GLY A 1 82  ? -43.26000 31.55400 45.31100  1.000 62.25345  ? 82   GLY A CA  1 
ATOM   677  C  C   . GLY A 1 82  ? -43.71000 32.59500 46.30800  1.000 60.31730  ? 82   GLY A C   1 
ATOM   678  O  O   . GLY A 1 82  ? -43.49200 32.38400 47.50100  1.000 68.58809  ? 82   GLY A O   1 
ATOM   679  N  N   . ALA A 1 83  ? -44.36300 33.65300 45.82900  1.000 59.26347  ? 83   ALA A N   1 
ATOM   680  C  CA  . ALA A 1 83  ? -44.79800 34.75400 46.71500  1.000 58.57306  ? 83   ALA A CA  1 
ATOM   681  C  C   . ALA A 1 83  ? -45.73200 35.71600 45.98200  1.000 63.81807  ? 83   ALA A C   1 
ATOM   682  O  O   . ALA A 1 83  ? -45.73100 35.71800 44.74900  1.000 65.72116  ? 83   ALA A O   1 
ATOM   683  C  CB  . ALA A 1 83  ? -43.58500 35.48100 47.21400  1.000 53.43220  ? 83   ALA A CB  1 
ATOM   684  N  N   . ASP A 1 84  ? -46.46800 36.52800 46.73400  1.000 63.00187  ? 84   ASP A N   1 
ATOM   685  C  CA  . ASP A 1 84  ? -47.37000 37.50000 46.13600  1.000 64.55131  ? 84   ASP A CA  1 
ATOM   686  C  C   . ASP A 1 84  ? -46.63500 38.79900 45.83300  1.000 64.84421  ? 84   ASP A C   1 
ATOM   687  O  O   . ASP A 1 84  ? -45.67100 39.16500 46.51200  1.000 62.59180  ? 84   ASP A O   1 
ATOM   688  C  CB  . ASP A 1 84  ? -48.55500 37.78300 47.06200  1.000 67.34099  ? 84   ASP A CB  1 
ATOM   689  C  CG  . ASP A 1 84  ? -49.47200 36.58800 47.22000  1.000 76.42124  ? 84   ASP A CG  1 
ATOM   690  O  OD1 . ASP A 1 84  ? -49.23200 35.55900 46.55500  1.000 85.67154  ? 84   ASP A OD1 1 
ATOM   691  O  OD2 . ASP A 1 84  ? -50.43400 36.67900 48.01100  1.000 78.54962  ? 84   ASP A OD2 1 
ATOM   692  N  N   . ASP A 1 85  ? -47.17600 39.50100 44.84000  1.000 70.64017  ? 85   ASP A N   1 
ATOM   693  C  CA  . ASP A 1 85  ? -46.64000 40.83000 44.48300  1.000 72.59388  ? 85   ASP A CA  1 
ATOM   694  C  C   . ASP A 1 85  ? -47.45900 41.85700 45.26600  1.000 67.59379  ? 85   ASP A C   1 
ATOM   695  O  O   . ASP A 1 85  ? -48.27200 41.44700 46.10300  1.000 69.40870  ? 85   ASP A O   1 
ATOM   696  C  CB  . ASP A 1 85  ? -46.67400 41.02100 42.97900  1.000 68.79785  ? 85   ASP A CB  1 
ATOM   697  C  CG  . ASP A 1 85  ? -48.03700 40.89100 42.31200  1.000 69.55261  ? 85   ASP A CG  1 
ATOM   698  O  OD1 . ASP A 1 85  ? -49.02800 40.66000 43.02900  1.000 74.08547  ? 85   ASP A OD1 1 
ATOM   699  O  OD2 . ASP A 1 85  ? -48.09300 41.02900 41.07600  1.000 60.87254  ? 85   ASP A OD2 1 
ATOM   700  N  N   . LEU A 1 86  ? -47.26900 43.13900 44.97900  1.000 68.08799  ? 86   LEU A N   1 
ATOM   701  C  CA  . LEU A 1 86  ? -47.97600 44.19800 45.73600  1.000 62.58269  ? 86   LEU A CA  1 
ATOM   702  C  C   . LEU A 1 86  ? -49.46500 44.16900 45.39100  1.000 74.17309  ? 86   LEU A C   1 
ATOM   703  O  O   . LEU A 1 86  ? -50.27900 44.49900 46.25900  1.000 84.16718  ? 86   LEU A O   1 
ATOM   704  C  CB  . LEU A 1 86  ? -47.31700 45.51900 45.37300  1.000 69.59040  ? 86   LEU A CB  1 
ATOM   705  C  CG  . LEU A 1 86  ? -45.86100 45.68000 45.81900  1.000 65.93734  ? 86   LEU A CG  1 
ATOM   706  C  CD1 . LEU A 1 86  ? -45.33000 47.05200 45.45900  1.000 61.68116  ? 86   LEU A CD1 1 
ATOM   707  C  CD2 . LEU A 1 86  ? -45.72000 45.42500 47.30600  1.000 62.60498  ? 86   LEU A CD2 1 
ATOM   708  N  N   . LYS A 1 87  ? -49.80200 43.75400 44.17100  1.000 85.61485  ? 87   LYS A N   1 
ATOM   709  C  CA  . LYS A 1 87  ? -51.22100 43.76500 43.73300  1.000 81.54078  ? 87   LYS A CA  1 
ATOM   710  C  C   . LYS A 1 87  ? -51.90100 42.51300 44.28600  1.000 77.29829  ? 87   LYS A C   1 
ATOM   711  O  O   . LYS A 1 87  ? -53.14000 42.48200 44.35000  1.000 72.54355  ? 87   LYS A O   1 
ATOM   712  C  CB  . LYS A 1 87  ? -51.30400 43.88800 42.21200  1.000 64.76752  ? 87   LYS A CB  1 
ATOM   713  C  CG  . LYS A 1 87  ? -50.70200 45.16600 41.65400  1.000 59.22454  ? 87   LYS A CG  1 
ATOM   714  N  N   . GLY A 1 88  ? -51.10000 41.53600 44.69100  1.000 74.52086  ? 88   GLY A N   1 
ATOM   715  C  CA  . GLY A 1 88  ? -51.69600 40.36800 45.30000  1.000 77.20294  ? 88   GLY A CA  1 
ATOM   716  C  C   . GLY A 1 88  ? -51.69000 39.11300 44.45300  1.000 86.25475  ? 88   GLY A C   1 
ATOM   717  O  O   . GLY A 1 88  ? -52.34200 38.13300 44.83200  1.000 92.88514  ? 88   GLY A O   1 
ATOM   718  N  N   . ASN A 1 89  ? -50.98100 39.10500 43.32700  1.000 84.49241  ? 89   ASN A N   1 
ATOM   719  C  CA  . ASN A 1 89  ? -50.92400 37.93900 42.45700  1.000 67.78227  ? 89   ASN A CA  1 
ATOM   720  C  C   . ASN A 1 89  ? -49.74500 37.05100 42.83500  1.000 72.72851  ? 89   ASN A C   1 
ATOM   721  O  O   . ASN A 1 89  ? -48.64800 37.54100 43.11700  1.000 77.80170  ? 89   ASN A O   1 
ATOM   722  C  CB  . ASN A 1 89  ? -50.80600 38.36200 40.99100  1.000 74.21809  ? 89   ASN A CB  1 
ATOM   723  C  CG  . ASN A 1 89  ? -51.86400 39.37000 40.58800  1.000 80.10244  ? 89   ASN A CG  1 
ATOM   724  O  OD1 . ASN A 1 89  ? -53.01400 39.01200 40.33000  1.000 100.12383 ? 89   ASN A OD1 1 
ATOM   725  N  ND2 . ASN A 1 89  ? -51.47800 40.63900 40.52500  1.000 78.78066  ? 89   ASN A ND2 1 
ATOM   726  N  N   . PHE A 1 90  ? -49.97900 35.74100 42.83200  1.000 76.74588  ? 90   PHE A N   1 
ATOM   727  C  CA  . PHE A 1 90  ? -48.92900 34.78400 43.16100  1.000 68.17275  ? 90   PHE A CA  1 
ATOM   728  C  C   . PHE A 1 90  ? -47.91200 34.72300 42.02800  1.000 65.05817  ? 90   PHE A C   1 
ATOM   729  O  O   . PHE A 1 90  ? -48.26700 34.43900 40.87900  1.000 74.10688  ? 90   PHE A O   1 
ATOM   730  C  CB  . PHE A 1 90  ? -49.53600 33.40800 43.42300  1.000 65.13848  ? 90   PHE A CB  1 
ATOM   731  C  CG  . PHE A 1 90  ? -48.55000 32.39400 43.92700  1.000 64.97808  ? 90   PHE A CG  1 
ATOM   732  C  CD1 . PHE A 1 90  ? -47.99900 32.51500 45.19200  1.000 56.45002  ? 90   PHE A CD1 1 
ATOM   733  C  CD2 . PHE A 1 90  ? -48.18400 31.31400 43.14300  1.000 67.97816  ? 90   PHE A CD2 1 
ATOM   734  C  CE1 . PHE A 1 90  ? -47.09300 31.58400 45.66100  1.000 64.86340  ? 90   PHE A CE1 1 
ATOM   735  C  CE2 . PHE A 1 90  ? -47.28000 30.37800 43.60600  1.000 63.45395  ? 90   PHE A CE2 1 
ATOM   736  C  CZ  . PHE A 1 90  ? -46.73300 30.51300 44.86700  1.000 58.68539  ? 90   PHE A CZ  1 
ATOM   737  N  N   . VAL A 1 91  ? -46.64400 34.91800 42.36400  1.000 60.42493  ? 91   VAL A N   1 
ATOM   738  C  CA  . VAL A 1 91  ? -45.58800 34.93900 41.31900  1.000 64.85291  ? 91   VAL A CA  1 
ATOM   739  C  C   . VAL A 1 91  ? -44.53900 33.87400 41.62800  1.000 66.57925  ? 91   VAL A C   1 
ATOM   740  O  O   . VAL A 1 91  ? -43.91800 33.96500 42.69200  1.000 67.34097  ? 91   VAL A O   1 
ATOM   741  C  CB  . VAL A 1 91  ? -44.94500 36.33300 41.19700  1.000 62.50050  ? 91   VAL A CB  1 
ATOM   742  C  CG1 . VAL A 1 91  ? -43.73000 36.33500 40.28700  1.000 60.86624  ? 91   VAL A CG1 1 
ATOM   743  C  CG2 . VAL A 1 91  ? -45.95100 37.38800 40.77200  1.000 62.92837  ? 91   VAL A CG2 1 
ATOM   744  N  N   . GLN A 1 92  ? -44.36600 32.89900 40.73300  1.000 60.52866  ? 92   GLN A N   1 
ATOM   745  C  CA  . GLN A 1 92  ? -43.30700 31.87300 40.89200  1.000 53.35398  ? 92   GLN A CA  1 
ATOM   746  C  C   . GLN A 1 92  ? -43.02600 31.22300 39.54000  1.000 58.33393  ? 92   GLN A C   1 
ATOM   747  O  O   . GLN A 1 92  ? -43.94200 31.16200 38.72500  1.000 62.51336  ? 92   GLN A O   1 
ATOM   748  C  CB  . GLN A 1 92  ? -43.76400 30.79700 41.87100  1.000 50.06970  ? 92   GLN A CB  1 
ATOM   749  C  CG  . GLN A 1 92  ? -42.69700 29.76700 42.20000  1.000 58.85210  ? 92   GLN A CG  1 
ATOM   750  C  CD  . GLN A 1 92  ? -43.18600 28.70200 43.15000  1.000 61.59881  ? 92   GLN A CD  1 
ATOM   751  O  OE1 . GLN A 1 92  ? -44.37800 28.56600 43.41100  1.000 52.16724  ? 92   GLN A OE1 1 
ATOM   752  N  NE2 . GLN A 1 92  ? -42.25600 27.92100 43.66800  1.000 58.19256  ? 92   GLN A NE2 1 
ATOM   753  N  N   . PHE A 1 93  ? -41.81300 30.72500 39.33700  1.000 55.94426  ? 93   PHE A N   1 
ATOM   754  C  CA  . PHE A 1 93  ? -41.52400 29.95400 38.11300  1.000 49.70585  ? 93   PHE A CA  1 
ATOM   755  C  C   . PHE A 1 93  ? -42.08000 28.55200 38.35300  1.000 60.67998  ? 93   PHE A C   1 
ATOM   756  O  O   . PHE A 1 93  ? -41.33700 27.68100 38.80400  1.000 61.24530  ? 93   PHE A O   1 
ATOM   757  C  CB  . PHE A 1 93  ? -40.02900 29.92900 37.83200  1.000 45.77947  ? 93   PHE A CB  1 
ATOM   758  C  CG  . PHE A 1 93  ? -39.61700 29.16200 36.60200  1.000 52.30244  ? 93   PHE A CG  1 
ATOM   759  C  CD1 . PHE A 1 93  ? -39.94400 29.61900 35.33700  1.000 50.62145  ? 93   PHE A CD1 1 
ATOM   760  C  CD2 . PHE A 1 93  ? -38.86900 28.00200 36.70800  1.000 50.77729  ? 93   PHE A CD2 1 
ATOM   761  C  CE1 . PHE A 1 93  ? -39.55700 28.91800 34.20600  1.000 46.07545  ? 93   PHE A CE1 1 
ATOM   762  C  CE2 . PHE A 1 93  ? -38.47800 27.30500 35.57700  1.000 50.61633  ? 93   PHE A CE2 1 
ATOM   763  C  CZ  . PHE A 1 93  ? -38.82200 27.76400 34.32800  1.000 43.64812  ? 93   PHE A CZ  1 
ATOM   764  N  N   . LYS A 1 94  ? -43.37200 28.37700 38.09400  1.000 59.99234  ? 94   LYS A N   1 
ATOM   765  C  CA  . LYS A 1 94  ? -44.01300 27.05300 38.24300  1.000 57.81489  ? 94   LYS A CA  1 
ATOM   766  C  C   . LYS A 1 94  ? -44.65200 26.70100 36.90500  1.000 58.84862  ? 94   LYS A C   1 
ATOM   767  O  O   . LYS A 1 94  ? -45.87200 26.82900 36.78500  1.000 69.45573  ? 94   LYS A O   1 
ATOM   768  C  CB  . LYS A 1 94  ? -45.07400 27.08700 39.34200  1.000 50.35637  ? 94   LYS A CB  1 
ATOM   769  C  CG  . LYS A 1 94  ? -45.51100 25.74100 39.89400  1.000 51.42830  ? 94   LYS A CG  1 
ATOM   770  C  CD  . LYS A 1 94  ? -46.48600 25.88800 41.03600  1.000 52.87703  ? 94   LYS A CD  1 
ATOM   771  C  CE  . LYS A 1 94  ? -46.86200 24.57200 41.67900  1.000 64.88818  ? 94   LYS A CE  1 
ATOM   772  N  N   . PRO A 1 95  ? -43.87000 26.31800 35.88600  1.000 54.64482  ? 95   PRO A N   1 
ATOM   773  C  CA  . PRO A 1 95  ? -44.45100 25.86300 34.62300  1.000 53.61810  ? 95   PRO A CA  1 
ATOM   774  C  C   . PRO A 1 95  ? -45.30000 24.58800 34.79300  1.000 55.46646  ? 95   PRO A C   1 
ATOM   775  O  O   . PRO A 1 95  ? -44.85500 23.71400 35.48100  1.000 57.31167  ? 95   PRO A O   1 
ATOM   776  C  CB  . PRO A 1 95  ? -43.19700 25.58900 33.79000  1.000 46.92457  ? 95   PRO A CB  1 
ATOM   777  C  CG  . PRO A 1 95  ? -42.08400 25.38200 34.77800  1.000 48.60242  ? 95   PRO A CG  1 
ATOM   778  C  CD  . PRO A 1 95  ? -42.41400 26.33200 35.90100  1.000 51.93149  ? 95   PRO A CD  1 
ATOM   779  N  N   . VAL A 1 96  ? -46.48400 24.51300 34.16800  1.000 57.02852  ? 96   VAL A N   1 
ATOM   780  C  CA  . VAL A 1 96  ? -47.34100 23.34000 34.28600  1.000 56.01525  ? 96   VAL A CA  1 
ATOM   781  C  C   . VAL A 1 96  ? -47.40400 22.65600 32.92900  1.000 63.15633  ? 96   VAL A C   1 
ATOM   782  O  O   . VAL A 1 96  ? -47.65700 23.31100 31.91000  1.000 66.80933  ? 96   VAL A O   1 
ATOM   783  C  CB  . VAL A 1 96  ? -48.74700 23.72100 34.77900  1.000 56.09049  ? 96   VAL A CB  1 
ATOM   784  C  CG1 . VAL A 1 96  ? -49.56400 22.47400 35.07600  1.000 53.33483  ? 96   VAL A CG1 1 
ATOM   785  C  CG2 . VAL A 1 96  ? -48.65500 24.61800 36.00600  1.000 57.06245  ? 96   VAL A CG2 1 
ATOM   786  N  N   . LEU A 1 97  ? -47.17400 21.34400 32.91600  1.000 65.11073  ? 97   LEU A N   1 
ATOM   787  C  CA  . LEU A 1 97  ? -47.22200 20.58500 31.67300  1.000 57.65533  ? 97   LEU A CA  1 
ATOM   788  C  C   . LEU A 1 97  ? -48.59300 20.70600 31.01900  1.000 61.79857  ? 97   LEU A C   1 
ATOM   789  O  O   . LEU A 1 97  ? -49.62800 20.65500 31.69000  1.000 60.89156  ? 97   LEU A O   1 
ATOM   790  C  CB  . LEU A 1 97  ? -46.89500 19.11300 31.93300  1.000 54.50563  ? 97   LEU A CB  1 
ATOM   791  C  CG  . LEU A 1 97  ? -45.45300 18.77300 32.31200  1.000 50.56408  ? 97   LEU A CG  1 
ATOM   792  C  CD1 . LEU A 1 97  ? -45.29500 17.27500 32.51900  1.000 51.74202  ? 97   LEU A CD1 1 
ATOM   793  C  CD2 . LEU A 1 97  ? -44.49600 19.26900 31.24500  1.000 52.68500  ? 97   LEU A CD2 1 
ATOM   794  N  N   . SER A 1 98  ? -48.59300 20.87600 29.69300  1.000 63.60092  ? 98   SER A N   1 
ATOM   795  C  CA  . SER A 1 98  ? -49.85100 20.99300 28.96400  1.000 62.06340  ? 98   SER A CA  1 
ATOM   796  C  C   . SER A 1 98  ? -50.67800 19.72100 29.07100  1.000 56.12994  ? 98   SER A C   1 
ATOM   797  O  O   . SER A 1 98  ? -51.91200 19.77500 29.02000  1.000 60.83447  ? 98   SER A O   1 
ATOM   798  C  CB  . SER A 1 98  ? -49.58100 21.33200 27.49800  1.000 62.55151  ? 98   SER A CB  1 
ATOM   799  O  OG  . SER A 1 98  ? -48.79600 20.32800 26.88000  1.000 54.92927  ? 98   SER A OG  1 
ATOM   800  N  N   . SER A 1 99  ? -50.02000 18.56900 29.22400  1.000 60.03238  ? 99   SER A N   1 
ATOM   801  C  CA  . SER A 1 99  ? -50.74200 17.32100 29.43800  1.000 69.89666  ? 99   SER A CA  1 
ATOM   802  C  C   . SER A 1 99  ? -51.45200 17.29400 30.78400  1.000 70.42349  ? 99   SER A C   1 
ATOM   803  O  O   . SER A 1 99  ? -52.36500 16.48200 30.97200  1.000 74.52989  ? 99   SER A O   1 
ATOM   804  C  CB  . SER A 1 99  ? -49.78500 16.13400 29.32800  1.000 61.53544  ? 99   SER A CB  1 
ATOM   805  O  OG  . SER A 1 99  ? -48.72200 16.24500 30.25800  1.000 54.25104  ? 99   SER A OG  1 
ATOM   806  N  N   . LYS A 1 100 ? -51.05500 18.15400 31.71900  1.000 63.75619  ? 100  LYS A N   1 
ATOM   807  C  CA  . LYS A 1 100 ? -51.72000 18.27600 33.00800  1.000 72.56727  ? 100  LYS A CA  1 
ATOM   808  C  C   . LYS A 1 100 ? -52.62000 19.50100 33.09400  1.000 79.63486  ? 100  LYS A C   1 
ATOM   809  O  O   . LYS A 1 100 ? -53.19200 19.75900 34.15700  1.000 74.63116  ? 100  LYS A O   1 
ATOM   810  C  CB  . LYS A 1 100 ? -50.68400 18.31800 34.13700  1.000 69.90696  ? 100  LYS A CB  1 
ATOM   811  C  CG  . LYS A 1 100 ? -49.88400 17.03400 34.29600  1.000 67.78149  ? 100  LYS A CG  1 
ATOM   812  N  N   . GLY A 1 101 ? -52.75700 20.25900 32.01000  1.000 78.11136  ? 101  GLY A N   1 
ATOM   813  C  CA  . GLY A 1 101 ? -53.62400 21.41800 31.97900  1.000 77.24239  ? 101  GLY A CA  1 
ATOM   814  C  C   . GLY A 1 101 ? -52.93100 22.76300 31.93200  1.000 75.73146  ? 101  GLY A C   1 
ATOM   815  O  O   . GLY A 1 101 ? -53.61200 23.79100 32.03100  1.000 80.65744  ? 101  GLY A O   1 
ATOM   816  N  N   . GLY A 1 102 ? -51.60700 22.79700 31.78100  1.000 64.17483  ? 102  GLY A N   1 
ATOM   817  C  CA  . GLY A 1 102 ? -50.86400 24.03600 31.75000  1.000 60.52826  ? 102  GLY A CA  1 
ATOM   818  C  C   . GLY A 1 102 ? -50.56000 24.50300 30.33700  1.000 64.79230  ? 102  GLY A C   1 
ATOM   819  O  O   . GLY A 1 102 ? -51.07500 23.98300 29.34500  1.000 64.51607  ? 102  GLY A O   1 
ATOM   820  N  N   . GLU A 1 103 ? -49.64000 25.47100 30.23900  1.000 60.52301  ? 103  GLU A N   1 
ATOM   821  C  CA  . GLU A 1 103 ? -49.27800 26.05400 28.92300  1.000 59.06036  ? 103  GLU A CA  1 
ATOM   822  C  C   . GLU A 1 103 ? -47.87300 25.60100 28.51700  1.000 59.94118  ? 103  GLU A C   1 
ATOM   823  O  O   . GLU A 1 103 ? -47.46200 25.89700 27.38900  1.000 51.69153  ? 103  GLU A O   1 
ATOM   824  C  CB  . GLU A 1 103 ? -49.31400 27.57600 29.00300  1.000 53.90249  ? 103  GLU A CB  1 
ATOM   825  C  CG  . GLU A 1 103 ? -50.60000 28.13600 29.59800  1.000 64.96009  ? 103  GLU A CG  1 
ATOM   826  C  CD  . GLU A 1 103 ? -50.52400 29.63600 29.81700  1.000 72.32861  ? 103  GLU A CD  1 
ATOM   827  O  OE1 . GLU A 1 103 ? -50.34800 30.37600 28.83000  1.000 70.85495  ? 103  GLU A OE1 1 
ATOM   828  O  OE2 . GLU A 1 103 ? -50.61500 30.05900 30.98500  1.000 72.14791  ? 103  GLU A OE2 1 
ATOM   829  N  N   . PHE A 1 104 ? -47.16200 24.92300 29.41300  1.000 61.71290  ? 104  PHE A N   1 
ATOM   830  C  CA  . PHE A 1 104 ? -45.83000 24.43000 29.08000  1.000 56.63565  ? 104  PHE A CA  1 
ATOM   831  C  C   . PHE A 1 104 ? -45.96800 23.15100 28.26200  1.000 58.74919  ? 104  PHE A C   1 
ATOM   832  O  O   . PHE A 1 104 ? -46.31600 22.09400 28.79800  1.000 57.48771  ? 104  PHE A O   1 
ATOM   833  C  CB  . PHE A 1 104 ? -45.01800 24.20300 30.35200  1.000 52.83019  ? 104  PHE A CB  1 
ATOM   834  C  CG  . PHE A 1 104 ? -43.67400 23.57900 30.11500  1.000 51.70669  ? 104  PHE A CG  1 
ATOM   835  C  CD1 . PHE A 1 104 ? -42.86000 24.02100 29.08600  1.000 52.49393  ? 104  PHE A CD1 1 
ATOM   836  C  CD2 . PHE A 1 104 ? -43.21700 22.55900 30.93400  1.000 51.92416  ? 104  PHE A CD2 1 
ATOM   837  C  CE1 . PHE A 1 104 ? -41.62300 23.44700 28.86800  1.000 49.82352  ? 104  PHE A CE1 1 
ATOM   838  C  CE2 . PHE A 1 104 ? -41.97900 21.98300 30.72300  1.000 45.27672  ? 104  PHE A CE2 1 
ATOM   839  C  CZ  . PHE A 1 104 ? -41.18200 22.42800 29.68900  1.000 44.06141  ? 104  PHE A CZ  1 
ATOM   840  N  N   . ASP A 1 105 ? -45.70000 23.25000 26.95800  1.000 59.45196  ? 105  ASP A N   1 
ATOM   841  C  CA  . ASP A 1 105 ? -45.78500 22.12800 26.02600  1.000 56.04741  ? 105  ASP A CA  1 
ATOM   842  C  C   . ASP A 1 105 ? -44.38600 21.87800 25.47400  1.000 54.41108  ? 105  ASP A C   1 
ATOM   843  O  O   . ASP A 1 105 ? -44.03800 22.36400 24.38700  1.000 59.73087  ? 105  ASP A O   1 
ATOM   844  C  CB  . ASP A 1 105 ? -46.78700 22.41200 24.90800  1.000 48.59143  ? 105  ASP A CB  1 
ATOM   845  C  CG  . ASP A 1 105 ? -47.09200 21.18700 24.06700  1.000 50.25827  ? 105  ASP A CG  1 
ATOM   846  O  OD1 . ASP A 1 105 ? -46.54000 20.10400 24.35800  1.000 63.28600  ? 105  ASP A OD1 1 
ATOM   847  O  OD2 . ASP A 1 105 ? -47.89000 21.30900 23.11500  1.000 58.13639  ? 105  ASP A OD2 1 
ATOM   848  N  N   . PRO A 1 106 ? -43.55400 21.12400 26.19700  1.000 49.63944  ? 106  PRO A N   1 
ATOM   849  C  CA  . PRO A 1 106 ? -42.18300 20.88800 25.71900  1.000 49.24827  ? 106  PRO A CA  1 
ATOM   850  C  C   . PRO A 1 106 ? -42.12800 20.10000 24.42400  1.000 54.28654  ? 106  PRO A C   1 
ATOM   851  O  O   . PRO A 1 106 ? -41.16500 20.24500 23.65900  1.000 56.98996  ? 106  PRO A O   1 
ATOM   852  C  CB  . PRO A 1 106 ? -41.53900 20.12100 26.88200  1.000 52.92940  ? 106  PRO A CB  1 
ATOM   853  C  CG  . PRO A 1 106 ? -42.68300 19.46500 27.57900  1.000 48.47963  ? 106  PRO A CG  1 
ATOM   854  C  CD  . PRO A 1 106 ? -43.83200 20.42300 27.46200  1.000 56.44044  ? 106  PRO A CD  1 
ATOM   855  N  N   . GLU A 1 107 ? -43.14200 19.27400 24.15200  1.000 55.79577  ? 107  GLU A N   1 
ATOM   856  C  CA  . GLU A 1 107 ? -43.17100 18.51900 22.90400  1.000 54.72782  ? 107  GLU A CA  1 
ATOM   857  C  C   . GLU A 1 107 ? -43.32200 19.44200 21.70100  1.000 48.62401  ? 107  GLU A C   1 
ATOM   858  O  O   . GLU A 1 107 ? -42.67200 19.23800 20.67100  1.000 50.74485  ? 107  GLU A O   1 
ATOM   859  C  CB  . GLU A 1 107 ? -44.29900 17.49000 22.94500  1.000 57.38249  ? 107  GLU A CB  1 
ATOM   860  C  CG  . GLU A 1 107 ? -44.03800 16.34400 23.90700  1.000 57.92855  ? 107  GLU A CG  1 
ATOM   861  C  CD  . GLU A 1 107 ? -45.24300 15.44800 24.08900  1.000 71.11697  ? 107  GLU A CD  1 
ATOM   862  O  OE1 . GLU A 1 107 ? -46.34900 15.97900 24.32300  1.000 72.61390  ? 107  GLU A OE1 1 
ATOM   863  O  OE2 . GLU A 1 107 ? -45.08600 14.21200 23.99700  1.000 79.53524  ? 107  GLU A OE2 1 
ATOM   864  N  N   . ALA A 1 108 ? -44.15800 20.47500 21.81700  1.000 45.82740  ? 108  ALA A N   1 
ATOM   865  C  CA  . ALA A 1 108 ? -44.29500 21.43100 20.72200  1.000 51.01461  ? 108  ALA A CA  1 
ATOM   866  C  C   . ALA A 1 108 ? -43.00400 22.21100 20.50700  1.000 55.05789  ? 108  ALA A C   1 
ATOM   867  O  O   . ALA A 1 108 ? -42.60200 22.46000 19.36300  1.000 67.15826  ? 108  ALA A O   1 
ATOM   868  C  CB  . ALA A 1 108 ? -45.46000 22.38100 20.99700  1.000 52.45766  ? 108  ALA A CB  1 
ATOM   869  N  N   . ILE A 1 109 ? -42.34000 22.60000 21.59800  1.000 56.69424  ? 109  ILE A N   1 
ATOM   870  C  CA  . ILE A 1 109 ? -41.08000 23.33000 21.48700  1.000 45.93928  ? 109  ILE A CA  1 
ATOM   871  C  C   . ILE A 1 109 ? -40.02500 22.47300 20.80200  1.000 49.42520  ? 109  ILE A C   1 
ATOM   872  O  O   . ILE A 1 109 ? -39.30500 22.94000 19.90900  1.000 44.83995  ? 109  ILE A O   1 
ATOM   873  C  CB  . ILE A 1 109 ? -40.61400 23.79900 22.87900  1.000 45.88176  ? 109  ILE A CB  1 
ATOM   874  C  CG1 . ILE A 1 109 ? -41.59500 24.82200 23.45600  1.000 47.06903  ? 109  ILE A CG1 1 
ATOM   875  C  CG2 . ILE A 1 109 ? -39.20600 24.37700 22.80900  1.000 42.78081  ? 109  ILE A CG2 1 
ATOM   876  C  CD1 . ILE A 1 109 ? -41.26200 25.26100 24.86300  1.000 53.15655  ? 109  ILE A CD1 1 
ATOM   877  N  N   . ILE A 1 110 ? -39.94100 21.19600 21.17300  1.000 48.07059  ? 110  ILE A N   1 
ATOM   878  C  CA  . ILE A 1 110 ? -38.89200 20.30700 20.59000  1.000 44.77112  ? 110  ILE A CA  1 
ATOM   879  C  C   . ILE A 1 110 ? -39.26600 19.98400 19.14100  1.000 48.02699  ? 110  ILE A C   1 
ATOM   880  O  O   . ILE A 1 110 ? -38.36000 19.79400 18.33000  1.000 50.22415  ? 110  ILE A O   1 
ATOM   881  C  CB  . ILE A 1 110 ? -38.67700 19.04100 21.43900  1.000 48.12051  ? 110  ILE A CB  1 
ATOM   882  C  CG1 . ILE A 1 110 ? -37.38000 18.32400 21.05900  1.000 53.13476  ? 110  ILE A CG1 1 
ATOM   883  C  CG2 . ILE A 1 110 ? -39.87100 18.11000 21.34500  1.000 62.57792  ? 110  ILE A CG2 1 
ATOM   884  C  CD1 . ILE A 1 110 ? -36.14900 19.17500 21.23100  1.000 51.15961  ? 110  ILE A CD1 1 
ATOM   885  N  N   . LYS A 1 111 ? -40.55800 19.96400 18.83600  1.000 44.11641  ? 111  LYS A N   1 
ATOM   886  C  CA  . LYS A 1 111 ? -40.94500 19.76300 17.41900  1.000 49.30502  ? 111  LYS A CA  1 
ATOM   887  C  C   . LYS A 1 111 ? -40.49400 20.97500 16.59800  1.000 46.48030  ? 111  LYS A C   1 
ATOM   888  O  O   . LYS A 1 111 ? -39.90900 20.77700 15.53600  1.000 44.33120  ? 111  LYS A O   1 
ATOM   889  C  CB  . LYS A 1 111 ? -42.45600 19.55100 17.31100  1.000 52.34088  ? 111  LYS A CB  1 
ATOM   890  C  CG  . LYS A 1 111 ? -43.07000 19.74100 15.93400  1.000 58.60406  ? 111  LYS A CG  1 
ATOM   891  C  CD  . LYS A 1 111 ? -44.54700 20.04800 16.02400  1.000 69.55375  ? 111  LYS A CD  1 
ATOM   892  C  CE  . LYS A 1 111 ? -44.82500 21.24300 16.91300  1.000 70.38195  ? 111  LYS A CE  1 
ATOM   893  N  NZ  . LYS A 1 111 ? -46.24400 21.30400 17.33400  1.000 66.13892  ? 111  LYS A NZ  1 
ATOM   894  N  N   . ALA A 1 112 ? -40.74400 22.18100 17.11000  1.000 45.12365  ? 112  ALA A N   1 
ATOM   895  C  CA  . ALA A 1 112 ? -40.30800 23.36700 16.37900  1.000 43.42968  ? 112  ALA A CA  1 
ATOM   896  C  C   . ALA A 1 112 ? -38.79400 23.38200 16.20600  1.000 41.33510  ? 112  ALA A C   1 
ATOM   897  O  O   . ALA A 1 112 ? -38.28500 23.71400 15.12700  1.000 40.08792  ? 112  ALA A O   1 
ATOM   898  C  CB  . ALA A 1 112 ? -40.78000 24.62900 17.09900  1.000 38.98997  ? 112  ALA A CB  1 
ATOM   899  N  N   . VAL A 1 113 ? -38.05700 23.01700 17.25900  1.000 41.15953  ? 113  VAL A N   1 
ATOM   900  C  CA  . VAL A 1 113 ? -36.59800 22.99400 17.17500  1.000 43.92671  ? 113  VAL A CA  1 
ATOM   901  C  C   . VAL A 1 113 ? -36.13900 21.97300 16.14000  1.000 44.27035  ? 113  VAL A C   1 
ATOM   902  O  O   . VAL A 1 113 ? -35.24500 22.24800 15.32900  1.000 43.15841  ? 113  VAL A O   1 
ATOM   903  C  CB  . VAL A 1 113 ? -35.98600 22.71600 18.56100  1.000 47.84552  ? 113  VAL A CB  1 
ATOM   904  C  CG1 . VAL A 1 113 ? -34.49200 22.44200 18.44200  1.000 37.31222  ? 113  VAL A CG1 1 
ATOM   905  C  CG2 . VAL A 1 113 ? -36.24000 23.88800 19.49600  1.000 42.40385  ? 113  VAL A CG2 1 
ATOM   906  N  N   . LYS A 1 114 ? -36.78600 20.80600 16.11800  1.000 45.85762  ? 114  LYS A N   1 
ATOM   907  C  CA  . LYS A 1 114 ? -36.44100 19.75400 15.12200  1.000 41.76526  ? 114  LYS A CA  1 
ATOM   908  C  C   . LYS A 1 114 ? -36.71100 20.31200 13.72800  1.000 41.64569  ? 114  LYS A C   1 
ATOM   909  O  O   . LYS A 1 114 ? -35.85000 20.18500 12.86000  1.000 42.73470  ? 114  LYS A O   1 
ATOM   910  C  CB  . LYS A 1 114 ? -37.25700 18.46800 15.30900  1.000 43.65250  ? 114  LYS A CB  1 
ATOM   911  C  CG  . LYS A 1 114 ? -36.96300 17.32500 14.35400  1.000 48.52043  ? 114  LYS A CG  1 
ATOM   912  C  CD  . LYS A 1 114 ? -35.55600 16.75800 14.46600  1.000 43.78142  ? 114  LYS A CD  1 
ATOM   913  C  CE  . LYS A 1 114 ? -35.33400 15.67500 13.46300  1.000 54.91484  ? 114  LYS A CE  1 
ATOM   914  N  NZ  . LYS A 1 114 ? -34.00500 15.07000 13.56100  1.000 59.39495  ? 114  LYS A NZ  1 
ATOM   915  N  N   . ALA A 1 115 ? -37.87100 20.93900 13.57000  1.000 47.03062  ? 115  ALA A N   1 
ATOM   916  C  CA  . ALA A 1 115 ? -38.23700 21.45400 12.25600  1.000 40.73511  ? 115  ALA A CA  1 
ATOM   917  C  C   . ALA A 1 115 ? -37.27800 22.54000 11.79000  1.000 42.69900  ? 115  ALA A C   1 
ATOM   918  O  O   . ALA A 1 115 ? -37.10100 22.73100 10.58100  1.000 43.21996  ? 115  ALA A O   1 
ATOM   919  C  CB  . ALA A 1 115 ? -39.66800 21.98700 12.28000  1.000 48.03978  ? 115  ALA A CB  1 
ATOM   920  N  N   . SER A 1 116 ? -36.65600 23.26200 12.72500  1.000 42.90444  ? 116  SER A N   1 
ATOM   921  C  CA  . SER A 1 116 ? -35.68300 24.28500 12.35500  1.000 49.79114  ? 116  SER A CA  1 
ATOM   922  C  C   . SER A 1 116 ? -34.43600 23.71000 11.69600  1.000 42.03681  ? 116  SER A C   1 
ATOM   923  O  O   . SER A 1 116 ? -33.65200 24.47400 11.12400  1.000 41.81008  ? 116  SER A O   1 
ATOM   924  C  CB  . SER A 1 116 ? -35.27600 25.09500 13.58700  1.000 41.04037  ? 116  SER A CB  1 
ATOM   925  O  OG  . SER A 1 116 ? -34.48200 24.31600 14.46400  1.000 36.44118  ? 116  SER A OG  1 
ATOM   926  N  N   . GLY A 1 117 ? -34.19600 22.41300 11.80400  1.000 37.48483  ? 117  GLY A N   1 
ATOM   927  C  CA  . GLY A 1 117 ? -33.02700 21.81900 11.13900  1.000 35.59432  ? 117  GLY A CA  1 
ATOM   928  C  C   . GLY A 1 117 ? -31.83900 21.68900 12.07600  1.000 47.60057  ? 117  GLY A C   1 
ATOM   929  O  O   . GLY A 1 117 ? -30.74400 21.33900 11.60800  1.000 48.84847  ? 117  GLY A O   1 
ATOM   930  N  N   . ALA A 1 118 ? -32.08000 21.92400 13.36200  1.000 39.02478  ? 118  ALA A N   1 
ATOM   931  C  CA  . ALA A 1 118 ? -31.02700 21.84200 14.39400  1.000 43.49765  ? 118  ALA A CA  1 
ATOM   932  C  C   . ALA A 1 118 ? -30.45100 20.42800 14.52700  1.000 43.61770  ? 118  ALA A C   1 
ATOM   933  O  O   . ALA A 1 118 ? -31.22900 19.48100 14.62800  1.000 37.34871  ? 118  ALA A O   1 
ATOM   934  C  CB  . ALA A 1 118 ? -31.60100 22.32500 15.69500  1.000 43.84554  ? 118  ALA A CB  1 
ATOM   935  N  N   . LYS A 1 119 ? -29.13100 20.33000 14.55300  1.000 38.98670  ? 119  LYS A N   1 
ATOM   936  C  CA  . LYS A 1 119 ? -28.42700 19.03900 14.69700  1.000 37.51128  ? 119  LYS A CA  1 
ATOM   937  C  C   . LYS A 1 119 ? -28.03200 18.83300 16.17000  1.000 49.51410  ? 119  LYS A C   1 
ATOM   938  O  O   . LYS A 1 119 ? -27.68500 17.69400 16.52300  1.000 42.41956  ? 119  LYS A O   1 
ATOM   939  C  CB  . LYS A 1 119 ? -27.26500 19.03600 13.70500  1.000 36.32204  ? 119  LYS A CB  1 
ATOM   940  C  CG  . LYS A 1 119 ? -27.68300 18.96200 12.24400  1.000 46.17283  ? 119  LYS A CG  1 
ATOM   941  C  CD  . LYS A 1 119 ? -28.46300 17.70200 11.92000  1.000 42.32634  ? 119  LYS A CD  1 
ATOM   942  C  CE  . LYS A 1 119 ? -28.89800 17.59000 10.47300  1.000 38.40603  ? 119  LYS A CE  1 
ATOM   943  N  NZ  . LYS A 1 119 ? -29.97600 18.54700 10.13800  1.000 45.89580  ? 119  LYS A NZ  1 
ATOM   944  N  N   . PHE A 1 120 ? -28.06600 19.89400 16.98200  1.000 45.73014  ? 120  PHE A N   1 
ATOM   945  C  CA  . PHE A 1 120 ? -27.80000 19.79500 18.43900  1.000 37.35000  ? 120  PHE A CA  1 
ATOM   946  C  C   . PHE A 1 120 ? -28.72700 20.76600 19.15400  1.000 38.90893  ? 120  PHE A C   1 
ATOM   947  O  O   . PHE A 1 120 ? -28.92700 21.86500 18.66700  1.000 41.98887  ? 120  PHE A O   1 
ATOM   948  C  CB  . PHE A 1 120 ? -26.32900 20.03700 18.76400  1.000 37.56720  ? 120  PHE A CB  1 
ATOM   949  C  CG  . PHE A 1 120 ? -25.72100 21.34200 18.32800  1.000 44.59917  ? 120  PHE A CG  1 
ATOM   950  C  CD1 . PHE A 1 120 ? -25.14300 21.47100 17.07800  1.000 37.02085  ? 120  PHE A CD1 1 
ATOM   951  C  CD2 . PHE A 1 120 ? -25.66500 22.42000 19.19400  1.000 41.00190  ? 120  PHE A CD2 1 
ATOM   952  C  CE1 . PHE A 1 120 ? -24.55500 22.66100 16.68900  1.000 40.62946  ? 120  PHE A CE1 1 
ATOM   953  C  CE2 . PHE A 1 120 ? -25.07600 23.60900 18.80300  1.000 43.93252  ? 120  PHE A CE2 1 
ATOM   954  C  CZ  . PHE A 1 120 ? -24.52200 23.72800 17.55200  1.000 44.73387  ? 120  PHE A CZ  1 
ATOM   955  N  N   . ALA A 1 121 ? -29.30800 20.32800 20.25000  1.000 41.68369  ? 121  ALA A N   1 
ATOM   956  C  CA  . ALA A 1 121 ? -30.23600 21.17500 21.00400  1.000 37.66272  ? 121  ALA A CA  1 
ATOM   957  C  C   . ALA A 1 121 ? -30.11100 20.88100 22.49000  1.000 40.06862  ? 121  ALA A C   1 
ATOM   958  O  O   . ALA A 1 121 ? -29.32000 20.02400 22.86400  1.000 40.89380  ? 121  ALA A O   1 
ATOM   959  C  CB  . ALA A 1 121 ? -31.62900 20.93300 20.53900  1.000 37.66031  ? 121  ALA A CB  1 
ATOM   960  N  N   . GLY A 1 122 ? -30.90300 21.57800 23.28400  1.000 40.51348  ? 122  GLY A N   1 
ATOM   961  C  CA  . GLY A 1 122 ? -30.88000 21.35400 24.72900  1.000 45.39956  ? 122  GLY A CA  1 
ATOM   962  C  C   . GLY A 1 122 ? -31.17400 22.59800 25.53100  1.000 49.74818  ? 122  GLY A C   1 
ATOM   963  O  O   . GLY A 1 122 ? -31.22600 23.68700 24.96100  1.000 45.51207  ? 122  GLY A O   1 
ATOM   964  N  N   . PRO A 1 123 ? -31.31700 22.47400 26.86300  1.000 49.92291  ? 123  PRO A N   1 
ATOM   965  C  CA  . PRO A 1 123 ? -31.69800 23.59800 27.67100  1.000 47.23635  ? 123  PRO A CA  1 
ATOM   966  C  C   . PRO A 1 123 ? -30.52700 24.27500 28.37000  1.000 49.66931  ? 123  PRO A C   1 
ATOM   967  O  O   . PRO A 1 123 ? -29.41000 23.83800 28.23200  1.000 49.67600  ? 123  PRO A O   1 
ATOM   968  C  CB  . PRO A 1 123 ? -32.48500 22.86700 28.75700  1.000 46.06671  ? 123  PRO A CB  1 
ATOM   969  C  CG  . PRO A 1 123 ? -31.67900 21.62200 29.01200  1.000 43.98139  ? 123  PRO A CG  1 
ATOM   970  C  CD  . PRO A 1 123 ? -31.09900 21.26500 27.66300  1.000 45.42598  ? 123  PRO A CD  1 
ATOM   971  N  N   . VAL A 1 124 ? -30.82300 25.37600 29.04600  1.000 45.89271  ? 124  VAL A N   1 
ATOM   972  C  CA  . VAL A 1 124 ? -29.77600 26.00000 29.89200  1.000 40.37779  ? 124  VAL A CA  1 
ATOM   973  C  C   . VAL A 1 124 ? -29.92900 25.24900 31.21500  1.000 41.63136  ? 124  VAL A C   1 
ATOM   974  O  O   . VAL A 1 124 ? -31.00200 25.33100 31.81500  1.000 46.93629  ? 124  VAL A O   1 
ATOM   975  C  CB  . VAL A 1 124 ? -29.89800 27.52400 30.08300  1.000 46.94769  ? 124  VAL A CB  1 
ATOM   976  C  CG1 . VAL A 1 124 ? -29.18900 28.00200 31.34300  1.000 46.43416  ? 124  VAL A CG1 1 
ATOM   977  C  CG2 . VAL A 1 124 ? -29.41500 28.29700 28.86400  1.000 47.20284  ? 124  VAL A CG2 1 
ATOM   978  N  N   . GLY A 1 125 ? -28.93000 24.46200 31.57100  1.000 41.88366  ? 125  GLY A N   1 
ATOM   979  C  CA  . GLY A 1 125 ? -29.06700 23.66700 32.78200  1.000 42.92880  ? 125  GLY A CA  1 
ATOM   980  C  C   . GLY A 1 125 ? -29.12100 24.52600 34.02900  1.000 51.05486  ? 125  GLY A C   1 
ATOM   981  O  O   . GLY A 1 125 ? -29.96600 24.32600 34.90500  1.000 49.45073  ? 125  GLY A O   1 
ATOM   982  N  N   . GLU A 1 126 ? -28.19100 25.48100 34.10400  1.000 56.31921  ? 126  GLU A N   1 
ATOM   983  C  CA  . GLU A 1 126 ? -28.14200 26.43200 35.23900  1.000 44.84194  ? 126  GLU A CA  1 
ATOM   984  C  C   . GLU A 1 126 ? -27.50500 27.74700 34.77900  1.000 44.51073  ? 126  GLU A C   1 
ATOM   985  O  O   . GLU A 1 126 ? -26.40800 27.71200 34.20700  1.000 45.78537  ? 126  GLU A O   1 
ATOM   986  C  CB  . GLU A 1 126 ? -27.32800 25.91700 36.42200  1.000 45.06842  ? 126  GLU A CB  1 
ATOM   987  C  CG  . GLU A 1 126 ? -27.45300 26.80200 37.65600  1.000 47.51539  ? 126  GLU A CG  1 
ATOM   988  C  CD  . GLU A 1 126 ? -26.80600 26.18900 38.87800  1.000 59.02257  ? 126  GLU A CD  1 
ATOM   989  O  OE1 . GLU A 1 126 ? -26.27900 25.07000 38.75000  1.000 65.19629  ? 126  GLU A OE1 1 
ATOM   990  O  OE2 . GLU A 1 126 ? -26.83300 26.82200 39.94600  1.000 57.46377  ? 126  GLU A OE2 1 
ATOM   991  N  N   . HIS A 1 127 ? -28.19100 28.85400 35.02800  1.000 44.16352  ? 127  HIS A N   1 
ATOM   992  C  CA  . HIS A 1 127 ? -27.63300 30.19600 34.71300  1.000 43.04893  ? 127  HIS A CA  1 
ATOM   993  C  C   . HIS A 1 127 ? -26.85500 30.71200 35.93400  1.000 44.04747  ? 127  HIS A C   1 
ATOM   994  O  O   . HIS A 1 127 ? -26.50000 29.90100 36.79300  1.000 49.66048  ? 127  HIS A O   1 
ATOM   995  C  CB  . HIS A 1 127 ? -28.73700 31.11800 34.18100  1.000 42.44209  ? 127  HIS A CB  1 
ATOM   996  C  CG  . HIS A 1 127 ? -28.23300 32.29500 33.42200  1.000 43.02676  ? 127  HIS A CG  1 
ATOM   997  N  ND1 . HIS A 1 127 ? -27.73700 32.18700 32.14400  1.000 42.74506  ? 127  HIS A ND1 1 
ATOM   998  C  CD2 . HIS A 1 127 ? -28.09800 33.57700 33.76400  1.000 44.15737  ? 127  HIS A CD2 1 
ATOM   999  C  CE1 . HIS A 1 127 ? -27.33900 33.37700 31.73200  1.000 50.09407  ? 127  HIS A CE1 1 
ATOM   1000 N  NE2 . HIS A 1 127 ? -27.55500 34.23500 32.69900  1.000 44.29362  ? 127  HIS A NE2 1 
ATOM   1001 N  N   . HIS A 1 128 ? -26.52200 31.99800 35.95500  1.000 44.27794  ? 128  HIS A N   1 
ATOM   1002 C  CA  . HIS A 1 128 ? -25.78400 32.64600 37.06800  1.000 45.22045  ? 128  HIS A CA  1 
ATOM   1003 C  C   . HIS A 1 128 ? -26.62400 32.74500 38.34500  1.000 45.78382  ? 128  HIS A C   1 
ATOM   1004 O  O   . HIS A 1 128 ? -26.05400 32.95700 39.40500  1.000 46.76757  ? 128  HIS A O   1 
ATOM   1005 C  CB  . HIS A 1 128 ? -25.38700 34.04100 36.58100  1.000 45.21450  ? 128  HIS A CB  1 
ATOM   1006 C  CG  . HIS A 1 128 ? -24.57700 34.14300 35.33700  1.000 44.80798  ? 128  HIS A CG  1 
ATOM   1007 N  ND1 . HIS A 1 128 ? -23.52500 33.32000 35.01100  1.000 50.99238  ? 128  HIS A ND1 1 
ATOM   1008 C  CD2 . HIS A 1 128 ? -24.64600 35.05300 34.36500  1.000 44.39511  ? 128  HIS A CD2 1 
ATOM   1009 C  CE1 . HIS A 1 128 ? -23.01000 33.71100 33.85700  1.000 51.20308  ? 128  HIS A CE1 1 
ATOM   1010 N  NE2 . HIS A 1 128 ? -23.67600 34.76300 33.45000  1.000 45.49623  ? 128  HIS A NE2 1 
ATOM   1011 N  N   . ASP A 1 129 ? -27.93100 32.58300 38.25200  1.000 45.28884  ? 129  ASP A N   1 
ATOM   1012 C  CA  . ASP A 1 129 ? -28.84500 32.77100 39.40500  1.000 47.25558  ? 129  ASP A CA  1 
ATOM   1013 C  C   . ASP A 1 129 ? -28.76300 31.64800 40.45300  1.000 56.86871  ? 129  ASP A C   1 
ATOM   1014 O  O   . ASP A 1 129 ? -29.42100 31.79600 41.48700  1.000 52.89300  ? 129  ASP A O   1 
ATOM   1015 C  CB  . ASP A 1 129 ? -30.26300 32.92600 38.88900  1.000 45.20678  ? 129  ASP A CB  1 
ATOM   1016 C  CG  . ASP A 1 129 ? -30.83200 31.72200 38.15700  1.000 44.62158  ? 129  ASP A CG  1 
ATOM   1017 O  OD1 . ASP A 1 129 ? -30.09800 31.14100 37.34700  1.000 54.06364  ? 129  ASP A OD1 1 
ATOM   1018 O  OD2 . ASP A 1 129 ? -32.01000 31.40600 38.38400  1.000 52.69651  ? 129  ASP A OD2 1 
ATOM   1019 N  N   . GLY A 1 130 ? -28.05700 30.54800 40.17100  1.000 49.51009  ? 130  GLY A N   1 
ATOM   1020 C  CA  . GLY A 1 130 ? -27.90300 29.45200 41.14800  1.000 57.89143  ? 130  GLY A CA  1 
ATOM   1021 C  C   . GLY A 1 130 ? -29.12800 28.56100 41.27500  1.000 59.33084  ? 130  GLY A C   1 
ATOM   1022 O  O   . GLY A 1 130 ? -29.33200 27.99400 42.35900  1.000 56.38257  ? 130  GLY A O   1 
ATOM   1023 N  N   . TYR A 1 131 ? -29.91700 28.44800 40.21200  1.000 50.44179  ? 131  TYR A N   1 
ATOM   1024 C  CA  . TYR A 1 131 ? -31.12300 27.58100 40.22600  1.000 51.78762  ? 131  TYR A CA  1 
ATOM   1025 C  C   . TYR A 1 131 ? -30.89000 26.38700 39.30900  1.000 55.23772  ? 131  TYR A C   1 
ATOM   1026 O  O   . TYR A 1 131 ? -31.11000 26.51200 38.10100  1.000 54.87778  ? 131  TYR A O   1 
ATOM   1027 C  CB  . TYR A 1 131 ? -32.35000 28.34600 39.75000  1.000 54.59088  ? 131  TYR A CB  1 
ATOM   1028 C  CG  . TYR A 1 131 ? -33.68600 27.66400 39.87300  1.000 53.17551  ? 131  TYR A CG  1 
ATOM   1029 C  CD1 . TYR A 1 131 ? -34.16000 27.21300 41.09100  1.000 47.51004  ? 131  TYR A CD1 1 
ATOM   1030 C  CD2 . TYR A 1 131 ? -34.50500 27.52400 38.76700  1.000 51.40075  ? 131  TYR A CD2 1 
ATOM   1031 C  CE1 . TYR A 1 131 ? -35.40400 26.61600 41.19900  1.000 52.96990  ? 131  TYR A CE1 1 
ATOM   1032 C  CE2 . TYR A 1 131 ? -35.74900 26.92800 38.85700  1.000 46.06218  ? 131  TYR A CE2 1 
ATOM   1033 C  CZ  . TYR A 1 131 ? -36.20000 26.47300 40.07900  1.000 51.63986  ? 131  TYR A CZ  1 
ATOM   1034 O  OH  . TYR A 1 131 ? -37.42700 25.89100 40.16800  1.000 62.96767  ? 131  TYR A OH  1 
ATOM   1035 N  N   . SER A 1 132 ? -30.45600 25.27100 39.88400  1.000 50.43589  ? 132  SER A N   1 
ATOM   1036 C  CA  . SER A 1 132 ? -30.20700 24.04500 39.09300  1.000 57.18856  ? 132  SER A CA  1 
ATOM   1037 C  C   . SER A 1 132 ? -31.54900 23.49900 38.59500  1.000 53.91039  ? 132  SER A C   1 
ATOM   1038 O  O   . SER A 1 132 ? -32.47100 23.39400 39.39300  1.000 52.00041  ? 132  SER A O   1 
ATOM   1039 C  CB  . SER A 1 132 ? -29.41900 23.06000 39.89700  1.000 53.35115  ? 132  SER A CB  1 
ATOM   1040 O  OG  . SER A 1 132 ? -28.04200 23.38800 39.89200  1.000 54.38788  ? 132  SER A OG  1 
ATOM   1041 N  N   . MET A 1 133 ? -31.66200 23.23500 37.29700  1.000 46.41248  ? 133  MET A N   1 
ATOM   1042 C  CA  . MET A 1 133 ? -32.97400 22.80100 36.74100  1.000 52.02761  ? 133  MET A CA  1 
ATOM   1043 C  C   . MET A 1 133 ? -33.01100 21.27400 36.57200  1.000 52.54812  ? 133  MET A C   1 
ATOM   1044 O  O   . MET A 1 133 ? -33.82900 20.79700 35.78400  1.000 52.48311  ? 133  MET A O   1 
ATOM   1045 C  CB  . MET A 1 133 ? -33.28300 23.54200 35.43900  1.000 44.64877  ? 133  MET A CB  1 
ATOM   1046 C  CG  . MET A 1 133 ? -34.29300 24.65900 35.62500  1.000 46.52377  ? 133  MET A CG  1 
ATOM   1047 S  SD  . MET A 1 133 ? -34.29100 25.88500 34.30000  1.000 47.12822  ? 133  MET A SD  1 
ATOM   1048 C  CE  . MET A 1 133 ? -32.56700 26.36300 34.28700  1.000 42.79895  ? 133  MET A CE  1 
ATOM   1049 N  N   . TRP A 1 134 ? -32.13600 20.56600 37.27900  1.000 50.68664  ? 134  TRP A N   1 
ATOM   1050 C  CA  . TRP A 1 134 ? -32.14400 19.08500 37.30200  1.000 56.19346  ? 134  TRP A CA  1 
ATOM   1051 C  C   . TRP A 1 134 ? -32.38100 18.65500 38.75100  1.000 56.22614  ? 134  TRP A C   1 
ATOM   1052 O  O   . TRP A 1 134 ? -32.49400 19.53700 39.60200  1.000 57.27270  ? 134  TRP A O   1 
ATOM   1053 C  CB  . TRP A 1 134 ? -30.83200 18.53500 36.75300  1.000 56.51025  ? 134  TRP A CB  1 
ATOM   1054 C  CG  . TRP A 1 134 ? -29.59600 18.90200 37.50900  1.000 57.29381  ? 134  TRP A CG  1 
ATOM   1055 C  CD1 . TRP A 1 134 ? -29.00200 18.18800 38.50600  1.000 53.11425  ? 134  TRP A CD1 1 
ATOM   1056 C  CD2 . TRP A 1 134 ? -28.76400 20.05300 37.29000  1.000 56.16959  ? 134  TRP A CD2 1 
ATOM   1057 N  NE1 . TRP A 1 134 ? -27.86600 18.82100 38.93100  1.000 52.80305  ? 134  TRP A NE1 1 
ATOM   1058 C  CE2 . TRP A 1 134 ? -27.69600 19.96900 38.20600  1.000 55.43348  ? 134  TRP A CE2 1 
ATOM   1059 C  CE3 . TRP A 1 134 ? -28.82200 21.14900 36.42400  1.000 55.56330  ? 134  TRP A CE3 1 
ATOM   1060 C  CZ2 . TRP A 1 134 ? -26.69800 20.93800 38.27500  1.000 58.24260  ? 134  TRP A CZ2 1 
ATOM   1061 C  CZ3 . TRP A 1 134 ? -27.83600 22.10500 36.49200  1.000 53.21025  ? 134  TRP A CZ3 1 
ATOM   1062 C  CH2 . TRP A 1 134 ? -26.78900 21.99900 37.40600  1.000 51.05973  ? 134  TRP A CH2 1 
ATOM   1063 N  N   . ASP A 1 135 ? -32.46500 17.35400 39.01400  1.000 53.75163  ? 135  ASP A N   1 
ATOM   1064 C  CA  . ASP A 1 135 ? -32.69800 16.85100 40.39300  1.000 56.83960  ? 135  ASP A CA  1 
ATOM   1065 C  C   . ASP A 1 135 ? -31.34300 16.80200 41.09800  1.000 64.25037  ? 135  ASP A C   1 
ATOM   1066 O  O   . ASP A 1 135 ? -30.71900 15.73200 41.10700  1.000 64.03324  ? 135  ASP A O   1 
ATOM   1067 C  CB  . ASP A 1 135 ? -33.42000 15.50700 40.40100  1.000 62.91910  ? 135  ASP A CB  1 
ATOM   1068 C  CG  . ASP A 1 135 ? -33.99700 15.10600 41.74400  1.000 78.26002  ? 135  ASP A CG  1 
ATOM   1069 O  OD1 . ASP A 1 135 ? -34.18600 15.99700 42.58700  1.000 80.08636  ? 135  ASP A OD1 1 
ATOM   1070 O  OD2 . ASP A 1 135 ? -34.25200 13.90400 41.93100  1.000 72.29338  ? 135  ASP A OD2 1 
ATOM   1071 N  N   . SER A 1 136 ? -30.89900 17.94400 41.62000  1.000 59.70097  ? 136  SER A N   1 
ATOM   1072 C  CA  . SER A 1 136 ? -29.57200 18.02800 42.27100  1.000 61.44848  ? 136  SER A CA  1 
ATOM   1073 C  C   . SER A 1 136 ? -29.67700 17.64200 43.74300  1.000 61.22760  ? 136  SER A C   1 
ATOM   1074 O  O   . SER A 1 136 ? -30.73300 17.85500 44.35300  1.000 63.39903  ? 136  SER A O   1 
ATOM   1075 C  CB  . SER A 1 136 ? -28.99600 19.40200 42.12700  1.000 52.61432  ? 136  SER A CB  1 
ATOM   1076 O  OG  . SER A 1 136 ? -27.75000 19.50300 42.79200  1.000 66.43175  ? 136  SER A OG  1 
ATOM   1077 N  N   . LYS A 1 137 ? -28.59800 17.10200 44.27400  1.000 55.45393  ? 137  LYS A N   1 
ATOM   1078 C  CA  . LYS A 1 137 ? -28.57900 16.80600 45.72100  1.000 71.70647  ? 137  LYS A CA  1 
ATOM   1079 C  C   . LYS A 1 137 ? -27.65300 17.84800 46.34400  1.000 67.30439  ? 137  LYS A C   1 
ATOM   1080 O  O   . LYS A 1 137 ? -27.87200 18.21800 47.50300  1.000 66.59404  ? 137  LYS A O   1 
ATOM   1081 C  CB  . LYS A 1 137 ? -28.09600 15.36800 45.92000  1.000 71.89295  ? 137  LYS A CB  1 
ATOM   1082 C  CG  . LYS A 1 137 ? -26.69300 15.07800 45.40700  1.000 65.38822  ? 137  LYS A CG  1 
ATOM   1083 C  CD  . LYS A 1 137 ? -26.32000 13.61700 45.46400  1.000 85.76734  ? 137  LYS A CD  1 
ATOM   1084 N  N   . VAL A 1 138 ? -26.69000 18.31700 45.56100  1.000 58.62751  ? 138  VAL A N   1 
ATOM   1085 C  CA  . VAL A 1 138 ? -25.70000 19.31100 46.03700  1.000 49.84990  ? 138  VAL A CA  1 
ATOM   1086 C  C   . VAL A 1 138 ? -26.35000 20.69800 46.13600  1.000 59.48247  ? 138  VAL A C   1 
ATOM   1087 O  O   . VAL A 1 138 ? -25.90700 21.47100 46.98200  1.000 68.36572  ? 138  VAL A O   1 
ATOM   1088 C  CB  . VAL A 1 138 ? -24.48700 19.29300 45.10000  1.000 49.51660  ? 138  VAL A CB  1 
ATOM   1089 C  CG1 . VAL A 1 138 ? -23.85500 17.91600 45.03400  1.000 58.97225  ? 138  VAL A CG1 1 
ATOM   1090 C  CG2 . VAL A 1 138 ? -24.84500 19.78400 43.70900  1.000 54.27891  ? 138  VAL A CG2 1 
ATOM   1091 N  N   . ASN A 1 139 ? -27.37400 20.98600 45.33300  1.000 53.26684  ? 139  ASN A N   1 
ATOM   1092 C  CA  . ASN A 1 139 ? -28.02200 22.29300 45.34700  1.000 57.07371  ? 139  ASN A CA  1 
ATOM   1093 C  C   . ASN A 1 139 ? -29.51300 22.08500 45.57600  1.000 49.12713  ? 139  ASN A C   1 
ATOM   1094 O  O   . ASN A 1 139 ? -30.21800 21.58500 44.69300  1.000 55.33267  ? 139  ASN A O   1 
ATOM   1095 C  CB  . ASN A 1 139 ? -27.76300 23.04900 44.04400  1.000 53.97234  ? 139  ASN A CB  1 
ATOM   1096 C  CG  . ASN A 1 139 ? -28.43200 24.41000 44.01300  1.000 53.91553  ? 139  ASN A CG  1 
ATOM   1097 O  OD1 . ASN A 1 139 ? -28.77100 24.97400 45.05500  1.000 52.48164  ? 139  ASN A OD1 1 
ATOM   1098 N  ND2 . ASN A 1 139 ? -28.62600 24.94600 42.81500  1.000 50.68809  ? 139  ASN A ND2 1 
ATOM   1099 N  N   . GLU A 1 140 ? -29.98900 22.46600 46.76300  1.000 54.87196  ? 140  GLU A N   1 
ATOM   1100 C  CA  . GLU A 1 140 ? -31.41100 22.38100 47.07100  1.000 54.11887  ? 140  GLU A CA  1 
ATOM   1101 C  C   . GLU A 1 140 ? -32.23700 23.41300 46.31800  1.000 50.95362  ? 140  GLU A C   1 
ATOM   1102 O  O   . GLU A 1 140 ? -33.46700 23.29400 46.28900  1.000 52.01487  ? 140  GLU A O   1 
ATOM   1103 C  CB  . GLU A 1 140 ? -31.63500 22.53600 48.57800  1.000 58.52317  ? 140  GLU A CB  1 
ATOM   1104 C  CG  . GLU A 1 140 ? -31.13100 23.84800 49.16900  1.000 54.98249  ? 140  GLU A CG  1 
ATOM   1105 C  CD  . GLU A 1 140 ? -29.64700 23.82400 49.49100  1.000 52.73812  ? 140  GLU A CD  1 
ATOM   1106 O  OE1 . GLU A 1 140 ? -28.95100 22.88600 49.04800  1.000 57.29697  ? 140  GLU A OE1 1 
ATOM   1107 O  OE2 . GLU A 1 140 ? -29.17400 24.74600 50.19000  1.000 51.38236  ? 140  GLU A OE2 1 
ATOM   1108 N  N   . TRP A 1 141 ? -31.60000 24.41700 45.71700  1.000 46.21340  ? 141  TRP A N   1 
ATOM   1109 C  CA  . TRP A 1 141 ? -32.30700 25.41100 44.90900  1.000 56.95876  ? 141  TRP A CA  1 
ATOM   1110 C  C   . TRP A 1 141 ? -32.45400 24.88300 43.48200  1.000 51.12178  ? 141  TRP A C   1 
ATOM   1111 O  O   . TRP A 1 141 ? -31.82400 25.35700 42.53600  1.000 58.27479  ? 141  TRP A O   1 
ATOM   1112 C  CB  . TRP A 1 141 ? -31.57200 26.74500 44.93500  1.000 54.59877  ? 141  TRP A CB  1 
ATOM   1113 C  CG  . TRP A 1 141 ? -31.47200 27.35800 46.29300  1.000 45.64629  ? 141  TRP A CG  1 
ATOM   1114 C  CD1 . TRP A 1 141 ? -30.47100 27.17900 47.20100  1.000 51.06585  ? 141  TRP A CD1 1 
ATOM   1115 C  CD2 . TRP A 1 141 ? -32.40800 28.25800 46.90000  1.000 54.92422  ? 141  TRP A CD2 1 
ATOM   1116 N  NE1 . TRP A 1 141 ? -30.72600 27.90900 48.33700  1.000 51.51735  ? 141  TRP A NE1 1 
ATOM   1117 C  CE2 . TRP A 1 141 ? -31.90900 28.58000 48.17700  1.000 51.99219  ? 141  TRP A CE2 1 
ATOM   1118 C  CE3 . TRP A 1 141 ? -33.62000 28.82100 46.48700  1.000 53.28781  ? 141  TRP A CE3 1 
ATOM   1119 C  CZ2 . TRP A 1 141 ? -32.57900 29.43900 49.04600  1.000 49.66443  ? 141  TRP A CZ2 1 
ATOM   1120 C  CZ3 . TRP A 1 141 ? -34.28400 29.67400 47.35200  1.000 54.82671  ? 141  TRP A CZ3 1 
ATOM   1121 C  CH2 . TRP A 1 141 ? -33.76200 29.97400 48.61600  1.000 45.62020  ? 141  TRP A CH2 1 
ATOM   1122 N  N   . ASN A 1 142 ? -33.30600 23.87100 43.33900  1.000 43.98284  ? 142  ASN A N   1 
ATOM   1123 C  CA  . ASN A 1 142 ? -33.51000 23.23000 42.05000  1.000 48.37313  ? 142  ASN A CA  1 
ATOM   1124 C  C   . ASN A 1 142 ? -34.99600 23.16200 41.72000  1.000 52.85403  ? 142  ASN A C   1 
ATOM   1125 O  O   . ASN A 1 142 ? -35.86200 23.44000 42.55500  1.000 52.27142  ? 142  ASN A O   1 
ATOM   1126 C  CB  . ASN A 1 142 ? -32.88500 21.82800 42.00800  1.000 51.64376  ? 142  ASN A CB  1 
ATOM   1127 C  CG  . ASN A 1 142 ? -33.50300 20.88500 43.01000  1.000 57.63618  ? 142  ASN A CG  1 
ATOM   1128 O  OD1 . ASN A 1 142 ? -34.59500 20.36000 42.79400  1.000 52.46131  ? 142  ASN A OD1 1 
ATOM   1129 N  ND2 . ASN A 1 142 ? -32.80400 20.65500 44.11300  1.000 59.95101  ? 142  ASN A ND2 1 
ATOM   1130 N  N   . SER A 1 143 ? -35.28000 22.78100 40.47200  1.000 48.35566  ? 143  SER A N   1 
ATOM   1131 C  CA  . SER A 1 143 ? -36.64100 22.78300 39.95200  1.000 59.69002  ? 143  SER A CA  1 
ATOM   1132 C  C   . SER A 1 143 ? -37.42600 21.52900 40.31100  1.000 56.53514  ? 143  SER A C   1 
ATOM   1133 O  O   . SER A 1 143 ? -38.62000 21.46100 40.00400  1.000 57.11056  ? 143  SER A O   1 
ATOM   1134 C  CB  . SER A 1 143 ? -36.61800 22.95100 38.43000  1.000 48.82714  ? 143  SER A CB  1 
ATOM   1135 O  OG  . SER A 1 143 ? -35.98700 21.84600 37.80700  1.000 48.93105  ? 143  SER A OG  1 
ATOM   1136 N  N   . VAL A 1 144 ? -36.79700 20.54100 40.93800  1.000 56.75229  ? 144  VAL A N   1 
ATOM   1137 C  CA  . VAL A 1 144 ? -37.51100 19.34300 41.36900  1.000 59.24100  ? 144  VAL A CA  1 
ATOM   1138 C  C   . VAL A 1 144 ? -38.08600 19.51900 42.76500  1.000 59.37506  ? 144  VAL A C   1 
ATOM   1139 O  O   . VAL A 1 144 ? -39.25700 19.21700 43.01100  1.000 56.28756  ? 144  VAL A O   1 
ATOM   1140 C  CB  . VAL A 1 144 ? -36.57900 18.11500 41.29300  1.000 66.92290  ? 144  VAL A CB  1 
ATOM   1141 C  CG1 . VAL A 1 144 ? -37.26700 16.88500 41.87000  1.000 53.78736  ? 144  VAL A CG1 1 
ATOM   1142 C  CG2 . VAL A 1 144 ? -36.16300 17.86600 39.85800  1.000 57.89779  ? 144  VAL A CG2 1 
ATOM   1143 N  N   . LYS A 1 145 ? -37.25600 20.04900 43.65800  1.000 60.64633  ? 145  LYS A N   1 
ATOM   1144 C  CA  . LYS A 1 145 ? -37.69700 20.25900 45.05500  1.000 57.77743  ? 145  LYS A CA  1 
ATOM   1145 C  C   . LYS A 1 145 ? -38.59300 21.49700 45.12600  1.000 60.37380  ? 145  LYS A C   1 
ATOM   1146 O  O   . LYS A 1 145 ? -39.41400 21.56500 46.04800  1.000 60.68103  ? 145  LYS A O   1 
ATOM   1147 C  CB  . LYS A 1 145 ? -36.42600 20.34500 45.89900  1.000 58.23758  ? 145  LYS A CB  1 
ATOM   1148 C  CG  . LYS A 1 145 ? -35.88000 19.00200 46.34300  1.000 66.98182  ? 145  LYS A CG  1 
ATOM   1149 C  CD  . LYS A 1 145 ? -34.43800 18.77700 45.92000  1.000 76.47668  ? 145  LYS A CD  1 
ATOM   1150 C  CE  . LYS A 1 145 ? -34.18100 17.34800 45.57600  1.000 82.02109  ? 145  LYS A CE  1 
ATOM   1151 N  NZ  . LYS A 1 145 ? -32.99400 17.20000 44.73400  1.000 64.89140  ? 145  LYS A NZ  1 
ATOM   1152 N  N   . ARG A 1 146 ? -38.47400 22.40900 44.15800  1.000 63.37919  ? 146  ARG A N   1 
ATOM   1153 C  CA  . ARG A 1 146 ? -39.24700 23.67700 44.24400  1.000 57.32050  ? 146  ARG A CA  1 
ATOM   1154 C  C   . ARG A 1 146 ? -39.93700 24.02800 42.92300  1.000 63.86195  ? 146  ARG A C   1 
ATOM   1155 O  O   . ARG A 1 146 ? -39.45200 23.59300 41.87500  1.000 64.50418  ? 146  ARG A O   1 
ATOM   1156 C  CB  . ARG A 1 146 ? -38.31400 24.81900 44.65400  1.000 56.61331  ? 146  ARG A CB  1 
ATOM   1157 C  CG  . ARG A 1 146 ? -37.22800 24.43800 45.64900  1.000 59.58918  ? 146  ARG A CG  1 
ATOM   1158 C  CD  . ARG A 1 146 ? -36.23000 25.56700 45.79800  1.000 59.27726  ? 146  ARG A CD  1 
ATOM   1159 N  NE  . ARG A 1 146 ? -35.10800 25.26400 46.67300  1.000 67.78753  ? 146  ARG A NE  1 
ATOM   1160 C  CZ  . ARG A 1 146 ? -35.00000 25.67200 47.93100  1.000 66.08096  ? 146  ARG A CZ  1 
ATOM   1161 N  NH1 . ARG A 1 146 ? -35.95900 26.39600 48.48000  1.000 58.49442  ? 146  ARG A NH1 1 
ATOM   1162 N  NH2 . ARG A 1 146 ? -33.93400 25.35000 48.63700  1.000 64.40709  ? 146  ARG A NH2 1 
ATOM   1163 N  N   . GLY A 1 147 ? -41.01700 24.81000 42.99200  1.000 62.47851  ? 147  GLY A N   1 
ATOM   1164 C  CA  . GLY A 1 147 ? -41.70200 25.26500 41.77500  1.000 51.83708  ? 147  GLY A CA  1 
ATOM   1165 C  C   . GLY A 1 147 ? -42.37700 24.18000 40.98000  1.000 60.98897  ? 147  GLY A C   1 
ATOM   1166 O  O   . GLY A 1 147 ? -43.34700 23.59800 41.48500  1.000 65.16540  ? 147  GLY A O   1 
ATOM   1167 N  N   . PRO A 1 148 ? -42.01200 23.99900 39.70300  1.000 59.19182  ? 148  PRO A N   1 
ATOM   1168 C  CA  . PRO A 1 148 ? -42.69400 23.03600 38.80400  1.000 59.39199  ? 148  PRO A CA  1 
ATOM   1169 C  C   . PRO A 1 148 ? -42.54300 21.59700 39.28700  1.000 59.93741  ? 148  PRO A C   1 
ATOM   1170 O  O   . PRO A 1 148 ? -43.31200 20.73500 38.82600  1.000 65.44345  ? 148  PRO A O   1 
ATOM   1171 C  CB  . PRO A 1 148 ? -41.98900 23.29700 37.49100  1.000 44.25554  ? 148  PRO A CB  1 
ATOM   1172 C  CG  . PRO A 1 148 ? -40.59000 23.68500 37.90300  1.000 53.75742  ? 148  PRO A CG  1 
ATOM   1173 C  CD  . PRO A 1 148 ? -40.84800 24.63300 39.01400  1.000 67.29221  ? 148  PRO A CD  1 
ATOM   1174 N  N   . LYS A 1 149 ? -41.55600 21.36700 40.14900  1.000 61.30138  ? 149  LYS A N   1 
ATOM   1175 C  CA  . LYS A 1 149 ? -41.28600 20.00400 40.64700  1.000 60.87063  ? 149  LYS A CA  1 
ATOM   1176 C  C   . LYS A 1 149 ? -41.19700 19.10300 39.41700  1.000 64.21506  ? 149  LYS A C   1 
ATOM   1177 O  O   . LYS A 1 149 ? -42.00400 18.16900 39.28800  1.000 61.96500  ? 149  LYS A O   1 
ATOM   1178 C  CB  . LYS A 1 149 ? -42.36300 19.60000 41.65300  1.000 65.06132  ? 149  LYS A CB  1 
ATOM   1179 C  CG  . LYS A 1 149 ? -42.39100 20.40200 42.94400  1.000 60.83939  ? 149  LYS A CG  1 
ATOM   1180 C  CD  . LYS A 1 149 ? -43.61000 20.10000 43.78000  1.000 56.68691  ? 149  LYS A CD  1 
ATOM   1181 C  CE  . LYS A 1 149 ? -43.49500 20.60500 45.20000  1.000 69.90009  ? 149  LYS A CE  1 
ATOM   1182 N  NZ  . LYS A 1 149 ? -44.72300 20.31500 45.97600  1.000 79.35676  ? 149  LYS A NZ  1 
ATOM   1183 N  N   . LEU A 1 150 ? -40.19500 19.33400 38.57200  1.000 61.11215  ? 150  LEU A N   1 
ATOM   1184 C  CA  A LEU A 1 150 ? -39.97000 18.57700 37.33400  0.865 60.46246  ? 150  LEU A CA  1 
ATOM   1185 C  CA  B LEU A 1 150 ? -40.01800 18.54500 37.32400  0.135 60.71192  ? 150  LEU A CA  1 
ATOM   1186 C  C   . LEU A 1 150 ? -38.54300 18.69800 36.88200  1.000 60.47391  ? 150  LEU A C   1 
ATOM   1187 O  O   . LEU A 1 150 ? -37.96300 19.82900 36.80800  1.000 53.84431  ? 150  LEU A O   1 
ATOM   1188 C  CB  A LEU A 1 150 ? -40.85900 19.13200 36.21900  0.865 58.90251  ? 150  LEU A CB  1 
ATOM   1189 C  CB  B LEU A 1 150 ? -40.96900 19.12600 36.27800  0.135 58.88687  ? 150  LEU A CB  1 
ATOM   1190 C  CG  A LEU A 1 150 ? -42.16100 18.38000 35.96500  0.865 63.23073  ? 150  LEU A CG  1 
ATOM   1191 C  CG  B LEU A 1 150 ? -41.05400 18.37600 34.95300  0.135 59.27384  ? 150  LEU A CG  1 
ATOM   1192 C  CD1 A LEU A 1 150 ? -43.14300 19.26300 35.22300  0.865 57.30828  ? 150  LEU A CD1 1 
ATOM   1193 C  CD1 B LEU A 1 150 ? -41.73400 17.03000 35.13700  0.135 61.13194  ? 150  LEU A CD1 1 
ATOM   1194 C  CD2 A LEU A 1 150 ? -41.90300 17.09800 35.18700  0.865 61.39017  ? 150  LEU A CD2 1 
ATOM   1195 C  CD2 B LEU A 1 150 ? -41.85300 19.19200 33.94900  0.135 57.04224  ? 150  LEU A CD2 1 
ATOM   1196 N  N   . ASP A 1 151 ? -37.87800 17.56900 36.62300  1.000 52.48917  ? 151  ASP A N   1 
ATOM   1197 C  CA  . ASP A 1 151 ? -36.43800 17.60100 36.24900  1.000 47.53555  ? 151  ASP A CA  1 
ATOM   1198 C  C   . ASP A 1 151 ? -36.36300 18.07800 34.79800  1.000 53.77247  ? 151  ASP A C   1 
ATOM   1199 O  O   . ASP A 1 151 ? -36.17200 17.23400 33.90400  1.000 48.73197  ? 151  ASP A O   1 
ATOM   1200 C  CB  . ASP A 1 151 ? -35.75000 16.26100 36.52000  1.000 48.18046  ? 151  ASP A CB  1 
ATOM   1201 C  CG  . ASP A 1 151 ? -34.24800 16.27700 36.30500  1.000 54.95817  ? 151  ASP A CG  1 
ATOM   1202 O  OD1 . ASP A 1 151 ? -33.77700 17.08400 35.48500  1.000 63.50119  ? 151  ASP A OD1 1 
ATOM   1203 O  OD2 . ASP A 1 151 ? -33.56200 15.50000 36.98800  1.000 50.65267  ? 151  ASP A OD2 1 
ATOM   1204 N  N   . LEU A 1 152 ? -36.50400 19.37900 34.58800  1.000 48.22655  ? 152  LEU A N   1 
ATOM   1205 C  CA  . LEU A 1 152 ? -36.53000 19.94700 33.22000  1.000 49.04917  ? 152  LEU A CA  1 
ATOM   1206 C  C   . LEU A 1 152 ? -35.31000 19.51100 32.40200  1.000 44.68085  ? 152  LEU A C   1 
ATOM   1207 O  O   . LEU A 1 152 ? -35.50300 19.20400 31.22600  1.000 45.39711  ? 152  LEU A O   1 
ATOM   1208 C  CB  . LEU A 1 152 ? -36.65000 21.45800 33.39800  1.000 41.14232  ? 152  LEU A CB  1 
ATOM   1209 C  CG  . LEU A 1 152 ? -37.90400 21.86100 34.16500  1.000 48.08689  ? 152  LEU A CG  1 
ATOM   1210 C  CD1 . LEU A 1 152 ? -37.84900 23.29700 34.63100  1.000 42.64846  ? 152  LEU A CD1 1 
ATOM   1211 C  CD2 . LEU A 1 152 ? -39.16400 21.56800 33.37100  1.000 45.63366  ? 152  LEU A CD2 1 
ATOM   1212 N  N   . VAL A 1 153 ? -34.11600 19.44800 32.98700  1.000 42.52855  ? 153  VAL A N   1 
ATOM   1213 C  CA  . VAL A 1 153 ? -32.97800 19.05000 32.16200  1.000 40.93315  ? 153  VAL A CA  1 
ATOM   1214 C  C   . VAL A 1 153 ? -33.17400 17.63500 31.63400  1.000 50.39037  ? 153  VAL A C   1 
ATOM   1215 O  O   . VAL A 1 153 ? -32.92100 17.35700 30.45600  1.000 50.00584  ? 153  VAL A O   1 
ATOM   1216 C  CB  . VAL A 1 153 ? -31.66400 19.19100 32.95300  1.000 41.15305  ? 153  VAL A CB  1 
ATOM   1217 C  CG1 . VAL A 1 153 ? -30.49300 18.64300 32.15000  1.000 41.01008  ? 153  VAL A CG1 1 
ATOM   1218 C  CG2 . VAL A 1 153 ? -31.41700 20.64600 33.31300  1.000 50.01345  ? 153  VAL A CG2 1 
ATOM   1219 N  N   . LYS A 1 154 ? -33.71400 16.73500 32.45500  1.000 47.53567  ? 154  LYS A N   1 
ATOM   1220 C  CA  . LYS A 1 154 ? -33.92500 15.33000 32.02200  1.000 48.21353  ? 154  LYS A CA  1 
ATOM   1221 C  C   . LYS A 1 154 ? -35.04900 15.32300 30.98800  1.000 49.62097  ? 154  LYS A C   1 
ATOM   1222 O  O   . LYS A 1 154 ? -34.93700 14.60800 29.99100  1.000 49.00262  ? 154  LYS A O   1 
ATOM   1223 C  CB  . LYS A 1 154 ? -34.31700 14.36400 33.14700  1.000 50.93184  ? 154  LYS A CB  1 
ATOM   1224 C  CG  . LYS A 1 154 ? -34.28400 12.88700 32.79800  1.000 54.88534  ? 154  LYS A CG  1 
ATOM   1225 C  CD  . LYS A 1 154 ? -32.88800 12.39000 32.45200  1.000 60.33938  ? 154  LYS A CD  1 
ATOM   1226 C  CE  . LYS A 1 154 ? -32.83600 10.90400 32.34500  1.000 66.44525  ? 154  LYS A CE  1 
ATOM   1227 N  NZ  . LYS A 1 154 ? -31.56800 10.45600 31.77000  1.000 71.52266  ? 154  LYS A NZ  1 
ATOM   1228 N  N   . LEU A 1 155 ? -36.06300 16.14000 31.23000  1.000 56.40034  ? 155  LEU A N   1 
ATOM   1229 C  CA  . LEU A 1 155 ? -37.16200 16.22800 30.27300  1.000 47.74964  ? 155  LEU A CA  1 
ATOM   1230 C  C   . LEU A 1 155 ? -36.65400 16.64600 28.89700  1.000 47.18810  ? 155  LEU A C   1 
ATOM   1231 O  O   . LEU A 1 155 ? -36.93900 15.99000 27.88400  1.000 58.29033  ? 155  LEU A O   1 
ATOM   1232 C  CB  . LEU A 1 155 ? -38.20600 17.22000 30.79100  1.000 45.46649  ? 155  LEU A CB  1 
ATOM   1233 C  CG  . LEU A 1 155 ? -39.63800 17.17800 30.25800  1.000 60.92727  ? 155  LEU A CG  1 
ATOM   1234 C  CD1 . LEU A 1 155 ? -40.36000 15.94600 30.77200  1.000 86.49851  ? 155  LEU A CD1 1 
ATOM   1235 C  CD2 . LEU A 1 155 ? -40.38600 18.44300 30.65300  1.000 50.00253  ? 155  LEU A CD2 1 
ATOM   1236 N  N   . TRP A 1 156 ? -35.88700 17.73900 28.84900  1.000 51.56332  ? 156  TRP A N   1 
ATOM   1237 C  CA  . TRP A 1 156 ? -35.36100 18.22100 27.57700  1.000 51.35037  ? 156  TRP A CA  1 
ATOM   1238 C  C   . TRP A 1 156 ? -34.40200 17.21400 26.95800  1.000 48.77404  ? 156  TRP A C   1 
ATOM   1239 O  O   . TRP A 1 156 ? -34.37200 17.05400 25.73600  1.000 52.21271  ? 156  TRP A O   1 
ATOM   1240 C  CB  . TRP A 1 156 ? -34.66200 19.56800 27.76100  1.000 48.82002  ? 156  TRP A CB  1 
ATOM   1241 C  CG  . TRP A 1 156 ? -35.57700 20.69600 28.12600  1.000 49.92371  ? 156  TRP A CG  1 
ATOM   1242 C  CD1 . TRP A 1 156 ? -35.49300 21.49100 29.23100  1.000 42.53367  ? 156  TRP A CD1 1 
ATOM   1243 C  CD2 . TRP A 1 156 ? -36.71100 21.16000 27.38300  1.000 41.11995  ? 156  TRP A CD2 1 
ATOM   1244 N  NE1 . TRP A 1 156 ? -36.50400 22.42000 29.22500  1.000 45.95520  ? 156  TRP A NE1 1 
ATOM   1245 C  CE2 . TRP A 1 156 ? -37.26600 22.23900 28.10000  1.000 44.22753  ? 156  TRP A CE2 1 
ATOM   1246 C  CE3 . TRP A 1 156 ? -37.31000 20.76900 26.18200  1.000 46.01782  ? 156  TRP A CE3 1 
ATOM   1247 C  CZ2 . TRP A 1 156 ? -38.39000 22.93000 27.65700  1.000 44.49051  ? 156  TRP A CZ2 1 
ATOM   1248 C  CZ3 . TRP A 1 156 ? -38.42700 21.45600 25.74500  1.000 43.87333  ? 156  TRP A CZ3 1 
ATOM   1249 C  CH2 . TRP A 1 156 ? -38.95500 22.52500 26.48000  1.000 44.96215  ? 156  TRP A CH2 1 
ATOM   1250 N  N   . ALA A 1 157 ? -33.61300 16.52300 27.78300  1.000 46.92948  ? 157  ALA A N   1 
ATOM   1251 C  CA  . ALA A 1 157 ? -32.68100 15.53100 27.25800  1.000 52.63463  ? 157  ALA A CA  1 
ATOM   1252 C  C   . ALA A 1 157 ? -33.42500 14.37500 26.60600  1.000 47.74358  ? 157  ALA A C   1 
ATOM   1253 O  O   . ALA A 1 157 ? -33.06900 13.92900 25.50800  1.000 47.50032  ? 157  ALA A O   1 
ATOM   1254 C  CB  . ALA A 1 157 ? -31.77100 15.02600 28.37700  1.000 50.04338  ? 157  ALA A CB  1 
ATOM   1255 N  N   . ASP A 1 158 ? -34.46800 13.87600 27.27300  1.000 48.46874  ? 158  ASP A N   1 
ATOM   1256 C  CA  . ASP A 1 158 ? -35.25400 12.78700 26.70600  1.000 48.88176  ? 158  ASP A CA  1 
ATOM   1257 C  C   . ASP A 1 158 ? -35.93800 13.21900 25.41700  1.000 52.61469  ? 158  ASP A C   1 
ATOM   1258 O  O   . ASP A 1 158 ? -35.97600 12.45800 24.44200  1.000 61.95189  ? 158  ASP A O   1 
ATOM   1259 C  CB  . ASP A 1 158 ? -36.28200 12.29400 27.72400  1.000 49.23023  ? 158  ASP A CB  1 
ATOM   1260 C  CG  . ASP A 1 158 ? -35.63700 11.73600 28.97600  1.000 60.64931  ? 158  ASP A CG  1 
ATOM   1261 O  OD1 . ASP A 1 158 ? -34.48900 11.25200 28.88800  1.000 51.43096  ? 158  ASP A OD1 1 
ATOM   1262 O  OD2 . ASP A 1 158 ? -36.27500 11.78200 30.04800  1.000 67.49382  ? 158  ASP A OD2 1 
ATOM   1263 N  N   . LEU A 1 159 ? -36.46900 14.44400 25.38200  1.000 54.62714  ? 159  LEU A N   1 
ATOM   1264 C  CA  . LEU A 1 159 ? -37.13800 14.90600 24.16900  1.000 47.49769  ? 159  LEU A CA  1 
ATOM   1265 C  C   . LEU A 1 159 ? -36.14700 15.12700 23.03100  1.000 52.41437  ? 159  LEU A C   1 
ATOM   1266 O  O   . LEU A 1 159 ? -36.46100 14.85100 21.86700  1.000 55.92802  ? 159  LEU A O   1 
ATOM   1267 C  CB  . LEU A 1 159 ? -37.92600 16.18100 24.45600  1.000 45.59081  ? 159  LEU A CB  1 
ATOM   1268 C  CG  . LEU A 1 159 ? -39.24200 15.95600 25.20000  1.000 49.02832  ? 159  LEU A CG  1 
ATOM   1269 C  CD1 . LEU A 1 159 ? -39.89400 17.28100 25.52500  1.000 53.71765  ? 159  LEU A CD1 1 
ATOM   1270 C  CD2 . LEU A 1 159 ? -40.17600 15.08300 24.37400  1.000 49.52090  ? 159  LEU A CD2 1 
ATOM   1271 N  N   . VAL A 1 160 ? -34.94600 15.62100 23.34400  1.000 53.06992  ? 160  VAL A N   1 
ATOM   1272 C  CA  . VAL A 1 160 ? -33.93900 15.84900 22.31300  1.000 48.19663  ? 160  VAL A CA  1 
ATOM   1273 C  C   . VAL A 1 160 ? -33.44700 14.52400 21.74600  1.000 46.68266  ? 160  VAL A C   1 
ATOM   1274 O  O   . VAL A 1 160 ? -33.29800 14.37300 20.52700  1.000 43.36423  ? 160  VAL A O   1 
ATOM   1275 C  CB  . VAL A 1 160 ? -32.78200 16.69500 22.87700  1.000 39.72167  ? 160  VAL A CB  1 
ATOM   1276 C  CG1 . VAL A 1 160 ? -31.57300 16.62500 21.96300  1.000 42.95240  ? 160  VAL A CG1 1 
ATOM   1277 C  CG2 . VAL A 1 160 ? -33.21500 18.13900 23.05200  1.000 43.95317  ? 160  VAL A CG2 1 
ATOM   1278 N  N   . ARG A 1 161 ? -33.17200 13.54500 22.59300  1.000 45.11011  ? 161  ARG A N   1 
ATOM   1279 C  CA  . ARG A 1 161 ? -32.74100 12.22200 22.07800  1.000 42.79856  ? 161  ARG A CA  1 
ATOM   1280 C  C   . ARG A 1 161 ? -33.87500 11.56800 21.27400  1.000 52.35668  ? 161  ARG A C   1 
ATOM   1281 O  O   . ARG A 1 161 ? -33.60200 11.06900 20.18500  1.000 51.44899  ? 161  ARG A O   1 
ATOM   1282 C  CB  . ARG A 1 161 ? -32.24700 11.32400 23.21300  1.000 52.92010  ? 161  ARG A CB  1 
ATOM   1283 C  CG  . ARG A 1 161 ? -30.75700 11.41000 23.50400  1.000 58.42019  ? 161  ARG A CG  1 
ATOM   1284 C  CD  . ARG A 1 161 ? -30.25300 12.75700 23.97200  1.000 63.24951  ? 161  ARG A CD  1 
ATOM   1285 N  NE  . ARG A 1 161 ? -28.82500 12.70100 24.24100  1.000 56.49099  ? 161  ARG A NE  1 
ATOM   1286 C  CZ  . ARG A 1 161 ? -28.29200 12.45800 25.42900  1.000 55.82298  ? 161  ARG A CZ  1 
ATOM   1287 N  NH1 . ARG A 1 161 ? -29.06900 12.25700 26.47800  1.000 50.81298  ? 161  ARG A NH1 1 
ATOM   1288 N  NH2 . ARG A 1 161 ? -26.98100 12.42600 25.56500  1.000 52.64665  ? 161  ARG A NH2 1 
ATOM   1289 N  N   . LYS A 1 162 ? -35.08900 11.58700 21.80500  1.000 47.89597  ? 162  LYS A N   1 
ATOM   1290 C  CA  . LYS A 1 162 ? -36.21300 10.94900 21.08900  1.000 46.94577  ? 162  LYS A CA  1 
ATOM   1291 C  C   . LYS A 1 162 ? -36.34700 11.53800 19.68500  1.000 54.90479  ? 162  LYS A C   1 
ATOM   1292 O  O   . LYS A 1 162 ? -36.68200 10.78800 18.75900  1.000 55.33741  ? 162  LYS A O   1 
ATOM   1293 C  CB  . LYS A 1 162 ? -37.51200 11.18200 21.85200  1.000 59.13599  ? 162  LYS A CB  1 
ATOM   1294 C  CG  . LYS A 1 162 ? -38.77400 10.83400 21.07700  1.000 71.74065  ? 162  LYS A CG  1 
ATOM   1295 C  CD  . LYS A 1 162 ? -40.03900 11.39400 21.68300  1.000 81.43495  ? 162  LYS A CD  1 
ATOM   1296 C  CE  . LYS A 1 162 ? -40.36300 10.80900 23.03900  1.000 83.22168  ? 162  LYS A CE  1 
ATOM   1297 N  NZ  . LYS A 1 162 ? -41.61800 11.37700 23.58300  1.000 103.94544 ? 162  LYS A NZ  1 
ATOM   1298 N  N   . ASN A 1 163 ? -36.11000 12.83900 19.54800  1.000 50.60930  ? 163  ASN A N   1 
ATOM   1299 C  CA  . ASN A 1 163 ? -36.23200 13.50300 18.25700  1.000 44.48756  ? 163  ASN A CA  1 
ATOM   1300 C  C   . ASN A 1 163 ? -34.94700 13.44000 17.44000  1.000 44.09059  ? 163  ASN A C   1 
ATOM   1301 O  O   . ASN A 1 163 ? -34.82000 14.16600 16.44900  1.000 47.75418  ? 163  ASN A O   1 
ATOM   1302 C  CB  . ASN A 1 163 ? -36.66400 14.95900 18.45200  1.000 43.09496  ? 163  ASN A CB  1 
ATOM   1303 C  CG  . ASN A 1 163 ? -38.12000 15.08300 18.86400  1.000 47.47766  ? 163  ASN A CG  1 
ATOM   1304 O  OD1 . ASN A 1 163 ? -38.97200 15.48300 18.07000  1.000 52.65493  ? 163  ASN A OD1 1 
ATOM   1305 N  ND2 . ASN A 1 163 ? -38.41300 14.73500 20.11100  1.000 47.61369  ? 163  ASN A ND2 1 
ATOM   1306 N  N   . GLY A 1 164 ? -34.00200 12.60500 17.82100  1.000 41.17867  ? 164  GLY A N   1 
ATOM   1307 C  CA  . GLY A 1 164 ? -32.82600 12.39300 16.96300  1.000 42.47590  ? 164  GLY A CA  1 
ATOM   1308 C  C   . GLY A 1 164 ? -31.86300 13.54500 16.88900  1.000 37.73757  ? 164  GLY A C   1 
ATOM   1309 O  O   . GLY A 1 164 ? -31.25900 13.74300 15.83300  1.000 40.87434  ? 164  GLY A O   1 
ATOM   1310 N  N   . MET A 1 165 ? -31.65500 14.21700 18.00600  1.000 38.32555  ? 165  MET A N   1 
ATOM   1311 C  CA  . MET A 1 165 ? -30.67200 15.32100 18.03000  1.000 43.69870  ? 165  MET A CA  1 
ATOM   1312 C  C   . MET A 1 165 ? -29.63100 15.16000 19.14300  1.000 43.36076  ? 165  MET A C   1 
ATOM   1313 O  O   . MET A 1 165 ? -29.94900 14.58100 20.18000  1.000 39.97364  ? 165  MET A O   1 
ATOM   1314 C  CB  . MET A 1 165 ? -31.38400 16.66100 18.21600  1.000 44.83048  ? 165  MET A CB  1 
ATOM   1315 C  CG  . MET A 1 165 ? -32.13200 17.14000 16.99100  1.000 48.43581  ? 165  MET A CG  1 
ATOM   1316 S  SD  . MET A 1 165 ? -33.03100 18.67900 17.26000  1.000 44.35124  ? 165  MET A SD  1 
ATOM   1317 C  CE  . MET A 1 165 ? -34.29300 18.18000 18.43300  1.000 39.46765  ? 165  MET A CE  1 
ATOM   1318 N  N   . LYS A 1 166 ? -28.43800 15.69400 18.90800  1.000 47.92231  ? 166  LYS A N   1 
ATOM   1319 C  CA  . LYS A 1 166 ? -27.39300 15.72100 19.95600  1.000 43.39524  ? 166  LYS A CA  1 
ATOM   1320 C  C   . LYS A 1 166 ? -27.83600 16.68700 21.06800  1.000 42.45131  ? 166  LYS A C   1 
ATOM   1321 O  O   . LYS A 1 166 ? -28.62200 17.59500 20.77300  1.000 38.49803  ? 166  LYS A O   1 
ATOM   1322 C  CB  . LYS A 1 166 ? -26.06400 16.05700 19.28600  1.000 41.16834  ? 166  LYS A CB  1 
ATOM   1323 C  CG  . LYS A 1 166 ? -25.43700 15.03200 18.36800  1.000 39.91030  ? 166  LYS A CG  1 
ATOM   1324 C  CD  . LYS A 1 166 ? -24.70100 13.93100 19.11500  1.000 38.61241  ? 166  LYS A CD  1 
ATOM   1325 C  CE  . LYS A 1 166 ? -23.90700 13.09300 18.17400  1.000 38.53854  ? 166  LYS A CE  1 
ATOM   1326 N  NZ  . LYS A 1 166 ? -23.11300 12.08900 18.87800  1.000 42.69967  ? 166  LYS A NZ  1 
ATOM   1327 N  N   . LEU A 1 167 ? -27.38400 16.46400 22.29900  1.000 40.90953  ? 167  LEU A N   1 
ATOM   1328 C  CA  . LEU A 1 167 ? -27.79700 17.22400 23.47200  1.000 39.14925  ? 167  LEU A CA  1 
ATOM   1329 C  C   . LEU A 1 167 ? -26.69000 18.18600 23.88200  1.000 44.18346  ? 167  LEU A C   1 
ATOM   1330 O  O   . LEU A 1 167 ? -25.55500 17.76500 24.13200  1.000 43.79106  ? 167  LEU A O   1 
ATOM   1331 C  CB  . LEU A 1 167 ? -28.14700 16.29900 24.63600  1.000 42.40994  ? 167  LEU A CB  1 
ATOM   1332 C  CG  . LEU A 1 167 ? -28.55600 17.03500 25.91200  1.000 40.23100  ? 167  LEU A CG  1 
ATOM   1333 C  CD1 . LEU A 1 167 ? -29.91300 17.70700 25.74100  1.000 39.52908  ? 167  LEU A CD1 1 
ATOM   1334 C  CD2 . LEU A 1 167 ? -28.55600 16.09500 27.10500  1.000 39.99533  ? 167  LEU A CD2 1 
ATOM   1335 N  N   . VAL A 1 168 ? -27.02500 19.47200 23.95300  1.000 40.27334  ? 168  VAL A N   1 
ATOM   1336 C  CA  . VAL A 1 168 ? -26.14800 20.49600 24.50800  1.000 39.36665  ? 168  VAL A CA  1 
ATOM   1337 C  C   . VAL A 1 168 ? -26.80100 21.04000 25.77000  1.000 39.58357  ? 168  VAL A C   1 
ATOM   1338 O  O   . VAL A 1 168 ? -28.02000 21.23600 25.81500  1.000 41.40162  ? 168  VAL A O   1 
ATOM   1339 C  CB  . VAL A 1 168 ? -25.86200 21.62700 23.49600  1.000 39.13819  ? 168  VAL A CB  1 
ATOM   1340 C  CG1 . VAL A 1 168 ? -27.15700 22.22300 22.96500  1.000 39.93968  ? 168  VAL A CG1 1 
ATOM   1341 C  CG2 . VAL A 1 168 ? -25.00600 22.71200 24.13000  1.000 41.72898  ? 168  VAL A CG2 1 
ATOM   1342 N  N   . VAL A 1 169 ? -25.99600 21.25300 26.80500  1.000 43.49080  ? 169  VAL A N   1 
ATOM   1343 C  CA  . VAL A 1 169 ? -26.46200 21.83600 28.05600  1.000 40.10506  ? 169  VAL A CA  1 
ATOM   1344 C  C   . VAL A 1 169 ? -25.60400 23.05700 28.34800  1.000 42.58783  ? 169  VAL A C   1 
ATOM   1345 O  O   . VAL A 1 169 ? -24.37100 22.95800 28.40400  1.000 44.87897  ? 169  VAL A O   1 
ATOM   1346 C  CB  . VAL A 1 169 ? -26.40400 20.83100 29.21600  1.000 47.52483  ? 169  VAL A CB  1 
ATOM   1347 C  CG1 . VAL A 1 169 ? -26.82800 21.50100 30.51400  1.000 40.66993  ? 169  VAL A CG1 1 
ATOM   1348 C  CG2 . VAL A 1 169 ? -27.29000 19.62700 28.91900  1.000 40.32774  ? 169  VAL A CG2 1 
ATOM   1349 N  N   . ALA A 1 170 ? -26.25300 24.20600 28.51800  1.000 42.63170  ? 170  ALA A N   1 
ATOM   1350 C  CA  . ALA A 1 170 ? -25.56400 25.45300 28.81000  1.000 44.18372  ? 170  ALA A CA  1 
ATOM   1351 C  C   . ALA A 1 170 ? -25.43700 25.62600 30.31600  1.000 44.82292  ? 170  ALA A C   1 
ATOM   1352 O  O   . ALA A 1 170 ? -26.42500 25.50400 31.04700  1.000 48.21409  ? 170  ALA A O   1 
ATOM   1353 C  CB  . ALA A 1 170 ? -26.30900 26.64100 28.20200  1.000 40.07039  ? 170  ALA A CB  1 
ATOM   1354 N  N   . MET A 1 171 ? -24.20100 25.84700 30.72800  1.000 48.66523  ? 171  MET A N   1 
ATOM   1355 C  CA  . MET A 1 171 ? -23.93200 26.06100 32.16600  1.000 47.42711  ? 171  MET A CA  1 
ATOM   1356 C  C   . MET A 1 171 ? -23.32700 27.45800 32.36300  1.000 45.90010  ? 171  MET A C   1 
ATOM   1357 O  O   . MET A 1 171 ? -22.34300 27.77200 31.69900  1.000 46.60194  ? 171  MET A O   1 
ATOM   1358 C  CB  . MET A 1 171 ? -22.99100 24.96300 32.66900  1.000 45.84108  ? 171  MET A CB  1 
ATOM   1359 C  CG  . MET A 1 171 ? -23.56700 23.56800 32.54400  1.000 50.42971  ? 171  MET A CG  1 
ATOM   1360 S  SD  . MET A 1 171 ? -24.98000 23.30200 33.62700  1.000 45.74282  ? 171  MET A SD  1 
ATOM   1361 C  CE  . MET A 1 171 ? -24.16100 23.27000 35.21800  1.000 49.59969  ? 171  MET A CE  1 
ATOM   1362 N  N   . HIS A 1 172 ? -23.93800 28.27400 33.20900  1.000 45.52159  ? 172  HIS A N   1 
ATOM   1363 C  CA  . HIS A 1 172 ? -23.42200 29.63700 33.50400  1.000 45.58731  ? 172  HIS A CA  1 
ATOM   1364 C  C   . HIS A 1 172 ? -23.34100 29.82000 35.02400  1.000 48.35600  ? 172  HIS A C   1 
ATOM   1365 O  O   . HIS A 1 172 ? -23.89700 30.78900 35.53100  1.000 50.85836  ? 172  HIS A O   1 
ATOM   1366 C  CB  . HIS A 1 172 ? -24.37100 30.68500 32.91900  1.000 41.32649  ? 172  HIS A CB  1 
ATOM   1367 C  CG  . HIS A 1 172 ? -25.08300 30.34300 31.65600  1.000 50.49756  ? 172  HIS A CG  1 
ATOM   1368 N  ND1 . HIS A 1 172 ? -24.71300 30.84100 30.42800  1.000 49.04645  ? 172  HIS A ND1 1 
ATOM   1369 C  CD2 . HIS A 1 172 ? -26.18800 29.62800 31.44100  1.000 53.69529  ? 172  HIS A CD2 1 
ATOM   1370 C  CE1 . HIS A 1 172 ? -25.55200 30.39800 29.50900  1.000 51.99466  ? 172  HIS A CE1 1 
ATOM   1371 N  NE2 . HIS A 1 172 ? -26.45300 29.66000 30.10200  1.000 49.62478  ? 172  HIS A NE2 1 
ATOM   1372 N  N   . GLN A 1 173 ? -22.65200 28.92800 35.73500  1.000 47.06265  ? 173  GLN A N   1 
ATOM   1373 C  CA  . GLN A 1 173 ? -22.65900 28.95700 37.22000  1.000 44.13143  ? 173  GLN A CA  1 
ATOM   1374 C  C   . GLN A 1 173 ? -21.29100 29.38200 37.74700  1.000 45.21838  ? 173  GLN A C   1 
ATOM   1375 O  O   . GLN A 1 173 ? -21.13000 29.46700 38.96200  1.000 54.07088  ? 173  GLN A O   1 
ATOM   1376 C  CB  . GLN A 1 173 ? -23.06400 27.57800 37.74100  1.000 53.19906  ? 173  GLN A CB  1 
ATOM   1377 C  CG  . GLN A 1 173 ? -21.95700 26.52500 37.77300  1.000 48.75249  ? 173  GLN A CG  1 
ATOM   1378 C  CD  . GLN A 1 173 ? -21.59500 25.94100 36.42500  1.000 53.82435  ? 173  GLN A CD  1 
ATOM   1379 O  OE1 . GLN A 1 173 ? -22.03700 26.40800 35.37200  1.000 53.22066  ? 173  GLN A OE1 1 
ATOM   1380 N  NE2 . GLN A 1 173 ? -20.76000 24.91400 36.44300  1.000 46.37876  ? 173  GLN A NE2 1 
ATOM   1381 N  N   . ALA A 1 174 ? -20.36300 29.66200 36.84800  1.000 53.28393  ? 174  ALA A N   1 
ATOM   1382 C  CA  . ALA A 1 174 ? -19.07000 30.16600 37.29900  1.000 42.94382  ? 174  ALA A CA  1 
ATOM   1383 C  C   . ALA A 1 174 ? -19.17100 31.59500 37.82100  1.000 44.12654  ? 174  ALA A C   1 
ATOM   1384 O  O   . ALA A 1 174 ? -18.55500 31.93100 38.83800  1.000 49.06494  ? 174  ALA A O   1 
ATOM   1385 C  CB  . ALA A 1 174 ? -18.05000 30.08700 36.16300  1.000 43.07677  ? 174  ALA A CB  1 
ATOM   1386 N  N   . TYR A 1 175 ? -19.93600 32.44700 37.13700  1.000 45.09939  ? 175  TYR A N   1 
ATOM   1387 C  CA  . TYR A 1 175 ? -20.09800 33.83800 37.54000  1.000 45.19503  ? 175  TYR A CA  1 
ATOM   1388 C  C   . TYR A 1 175 ? -21.05600 34.00800 38.71200  1.000 52.59902  ? 175  TYR A C   1 
ATOM   1389 O  O   . TYR A 1 175 ? -21.13200 35.10700 39.27400  1.000 49.52141  ? 175  TYR A O   1 
ATOM   1390 C  CB  . TYR A 1 175 ? -20.57500 34.66900 36.34200  1.000 42.60153  ? 175  TYR A CB  1 
ATOM   1391 C  CG  . TYR A 1 175 ? -20.66500 36.15600 36.60000  1.000 49.72859  ? 175  TYR A CG  1 
ATOM   1392 C  CD1 . TYR A 1 175 ? -19.59300 36.85400 37.13900  1.000 48.03953  ? 175  TYR A CD1 1 
ATOM   1393 C  CD2 . TYR A 1 175 ? -21.82000 36.86500 36.29400  1.000 48.22375  ? 175  TYR A CD2 1 
ATOM   1394 C  CE1 . TYR A 1 175 ? -19.67000 38.21400 37.37500  1.000 44.81252  ? 175  TYR A CE1 1 
ATOM   1395 C  CE2 . TYR A 1 175 ? -21.90500 38.22700 36.52300  1.000 47.02018  ? 175  TYR A CE2 1 
ATOM   1396 C  CZ  . TYR A 1 175 ? -20.82800 38.89600 37.06500  1.000 44.92130  ? 175  TYR A CZ  1 
ATOM   1397 O  OH  . TYR A 1 175 ? -20.90700 40.25200 37.29800  1.000 43.01589  ? 175  TYR A OH  1 
ATOM   1398 N  N   . ASN A 1 176 ? -21.77300 32.94900 39.10000  1.000 43.11318  ? 176  ASN A N   1 
ATOM   1399 C  CA  . ASN A 1 176 ? -22.69200 33.03400 40.23200  1.000 48.48244  ? 176  ASN A CA  1 
ATOM   1400 C  C   . ASN A 1 176 ? -21.99200 33.53700 41.48800  1.000 48.12995  ? 176  ASN A C   1 
ATOM   1401 O  O   . ASN A 1 176 ? -22.54000 34.36500 42.22500  1.000 46.18079  ? 176  ASN A O   1 
ATOM   1402 C  CB  . ASN A 1 176 ? -23.32900 31.66700 40.49300  1.000 49.93264  ? 176  ASN A CB  1 
ATOM   1403 C  CG  . ASN A 1 176 ? -24.05700 31.60500 41.82500  1.000 43.59411  ? 176  ASN A CG  1 
ATOM   1404 O  OD1 . ASN A 1 176 ? -23.47000 31.25500 42.85000  1.000 49.11185  ? 176  ASN A OD1 1 
ATOM   1405 N  ND2 . ASN A 1 176 ? -25.34200 31.94200 41.81500  1.000 43.49346  ? 176  ASN A ND2 1 
ATOM   1406 N  N   . TYR A 1 177 ? -20.77800 33.05200 41.75000  1.000 50.07196  ? 177  TYR A N   1 
ATOM   1407 C  CA  . TYR A 1 177 ? -20.03200 33.43200 42.94300  1.000 48.20097  ? 177  TYR A CA  1 
ATOM   1408 C  C   . TYR A 1 177 ? -18.84400 34.33200 42.62400  1.000 50.05244  ? 177  TYR A C   1 
ATOM   1409 O  O   . TYR A 1 177 ? -17.95400 34.49700 43.46500  1.000 52.25779  ? 177  TYR A O   1 
ATOM   1410 C  CB  . TYR A 1 177 ? -19.56900 32.18600 43.70000  1.000 53.14499  ? 177  TYR A CB  1 
ATOM   1411 C  CG  . TYR A 1 177 ? -18.65900 31.26900 42.90900  1.000 46.26522  ? 177  TYR A CG  1 
ATOM   1412 C  CD1 . TYR A 1 177 ? -19.18000 30.25100 42.12200  1.000 45.95570  ? 177  TYR A CD1 1 
ATOM   1413 C  CD2 . TYR A 1 177 ? -17.27800 31.41400 42.96300  1.000 46.21042  ? 177  TYR A CD2 1 
ATOM   1414 C  CE1 . TYR A 1 177 ? -18.35100 29.40900 41.40300  1.000 50.32889  ? 177  TYR A CE1 1 
ATOM   1415 C  CE2 . TYR A 1 177 ? -16.44300 30.57700 42.24900  1.000 50.36121  ? 177  TYR A CE2 1 
ATOM   1416 C  CZ  . TYR A 1 177 ? -16.98400 29.57700 41.47100  1.000 50.35592  ? 177  TYR A CZ  1 
ATOM   1417 O  OH  . TYR A 1 177 ? -16.15800 28.74000 40.75800  1.000 49.24746  ? 177  TYR A OH  1 
ATOM   1418 N  N   . ASN A 1 178 ? -18.80100 34.88800 41.40900  1.000 44.07881  ? 178  ASN A N   1 
ATOM   1419 C  CA  . ASN A 1 178 ? -17.69500 35.80000 41.00600  1.000 51.14711  ? 178  ASN A CA  1 
ATOM   1420 C  C   . ASN A 1 178 ? -18.19400 37.25000 40.78100  1.000 48.44423  ? 178  ASN A C   1 
ATOM   1421 O  O   . ASN A 1 178 ? -17.51200 37.98200 40.07900  1.000 44.01347  ? 178  ASN A O   1 
ATOM   1422 C  CB  . ASN A 1 178 ? -16.91000 35.25400 39.81700  1.000 43.94031  ? 178  ASN A CB  1 
ATOM   1423 C  CG  . ASN A 1 178 ? -15.84700 34.23800 40.17200  1.000 55.30837  ? 178  ASN A CG  1 
ATOM   1424 O  OD1 . ASN A 1 178 ? -14.73100 34.59900 40.53400  1.000 56.50961  ? 178  ASN A OD1 1 
ATOM   1425 N  ND2 . ASN A 1 178 ? -16.16900 32.96500 40.02600  1.000 45.65035  ? 178  ASN A ND2 1 
ATOM   1426 N  N   . GLY A 1 179 ? -19.30700 37.64500 41.39700  1.000 44.09487  ? 179  GLY A N   1 
ATOM   1427 C  CA  . GLY A 1 179 ? -19.82500 39.01800 41.30600  1.000 46.33042  ? 179  GLY A CA  1 
ATOM   1428 C  C   . GLY A 1 179 ? -21.23200 39.21600 40.77800  1.000 49.20490  ? 179  GLY A C   1 
ATOM   1429 O  O   . GLY A 1 179 ? -21.69900 40.35600 40.83300  1.000 53.34734  ? 179  GLY A O   1 
ATOM   1430 N  N   . PHE A 1 180 ? -21.92400 38.15900 40.37800  1.000 49.05996  ? 180  PHE A N   1 
ATOM   1431 C  CA  . PHE A 1 180 ? -23.27500 38.29500 39.78700  1.000 43.76870  ? 180  PHE A CA  1 
ATOM   1432 C  C   . PHE A 1 180 ? -24.19800 38.85700 40.83400  1.000 43.48828  ? 180  PHE A C   1 
ATOM   1433 O  O   . PHE A 1 180 ? -24.97800 39.74400 40.51100  1.000 48.54742  ? 180  PHE A O   1 
ATOM   1434 C  CB  . PHE A 1 180 ? -23.77200 36.96800 39.19400  1.000 43.04205  ? 180  PHE A CB  1 
ATOM   1435 C  CG  . PHE A 1 180 ? -25.14700 37.01100 38.54500  1.000 42.76575  ? 180  PHE A CG  1 
ATOM   1436 C  CD1 . PHE A 1 180 ? -25.29400 37.38200 37.21500  1.000 42.43967  ? 180  PHE A CD1 1 
ATOM   1437 C  CD2 . PHE A 1 180 ? -26.28200 36.64500 39.25300  1.000 42.84718  ? 180  PHE A CD2 1 
ATOM   1438 C  CE1 . PHE A 1 180 ? -26.54300 37.41500 36.62400  1.000 42.20399  ? 180  PHE A CE1 1 
ATOM   1439 C  CE2 . PHE A 1 180 ? -27.52900 36.67600 38.65400  1.000 43.49420  ? 180  PHE A CE2 1 
ATOM   1440 C  CZ  . PHE A 1 180 ? -27.65700 37.06200 37.34400  1.000 42.29503  ? 180  PHE A CZ  1 
ATOM   1441 N  N   . TYR A 1 181 ? -24.14400 38.32100 42.05000  1.000 47.30661  ? 181  TYR A N   1 
ATOM   1442 C  CA  . TYR A 1 181 ? -25.08100 38.78400 43.10600  1.000 51.16487  ? 181  TYR A CA  1 
ATOM   1443 C  C   . TYR A 1 181 ? -24.36400 39.77900 44.05200  1.000 58.29888  ? 181  TYR A C   1 
ATOM   1444 O  O   . TYR A 1 181 ? -24.73200 39.84100 45.23400  1.000 57.30854  ? 181  TYR A O   1 
ATOM   1445 C  CB  . TYR A 1 181 ? -25.59600 37.51900 43.78500  1.000 44.09965  ? 181  TYR A CB  1 
ATOM   1446 C  CG  . TYR A 1 181 ? -26.78500 36.78800 43.18000  1.000 49.49124  ? 181  TYR A CG  1 
ATOM   1447 C  CD1 . TYR A 1 181 ? -28.03000 37.39200 43.08700  1.000 53.36643  ? 181  TYR A CD1 1 
ATOM   1448 C  CD2 . TYR A 1 181 ? -26.67000 35.47200 42.75600  1.000 44.05466  ? 181  TYR A CD2 1 
ATOM   1449 C  CE1 . TYR A 1 181 ? -29.11900 36.71700 42.56500  1.000 47.09818  ? 181  TYR A CE1 1 
ATOM   1450 C  CE2 . TYR A 1 181 ? -27.75000 34.78500 42.23300  1.000 44.77943  ? 181  TYR A CE2 1 
ATOM   1451 C  CZ  . TYR A 1 181 ? -28.97700 35.41000 42.13800  1.000 50.80609  ? 181  TYR A CZ  1 
ATOM   1452 O  OH  . TYR A 1 181 ? -30.04900 34.74700 41.63000  1.000 50.60250  ? 181  TYR A OH  1 
ATOM   1453 N  N   . GLU A 1 182 ? -23.39900 40.54600 43.54600  1.000 46.74801  ? 182  GLU A N   1 
ATOM   1454 C  CA  . GLU A 1 182 ? -22.59500 41.47700 44.38500  1.000 44.66885  ? 182  GLU A CA  1 
ATOM   1455 C  C   . GLU A 1 182 ? -23.42700 42.58900 45.03600  1.000 44.82040  ? 182  GLU A C   1 
ATOM   1456 O  O   . GLU A 1 182 ? -22.93000 43.18400 45.99300  1.000 53.11630  ? 182  GLU A O   1 
ATOM   1457 C  CB  . GLU A 1 182 ? -21.49100 42.10700 43.54600  1.000 46.91966  ? 182  GLU A CB  1 
ATOM   1458 C  CG  . GLU A 1 182 ? -21.97300 43.17000 42.56600  1.000 48.67512  ? 182  GLU A CG  1 
ATOM   1459 C  CD  . GLU A 1 182 ? -20.88000 43.49800 41.57100  1.000 52.44960  ? 182  GLU A CD  1 
ATOM   1460 O  OE1 . GLU A 1 182 ? -19.78300 43.88900 42.00800  1.000 60.45796  ? 182  GLU A OE1 1 
ATOM   1461 O  OE2 . GLU A 1 182 ? -21.11600 43.35100 40.36000  1.000 53.58940  ? 182  GLU A OE2 1 
ATOM   1462 N  N   . TRP A 1 183 ? -24.63200 42.84400 44.55600  1.000 45.42996  ? 183  TRP A N   1 
ATOM   1463 C  CA  . TRP A 1 183 ? -25.45400 43.96300 45.07100  1.000 52.28361  ? 183  TRP A CA  1 
ATOM   1464 C  C   . TRP A 1 183 ? -26.60300 43.37700 45.86500  1.000 48.76814  ? 183  TRP A C   1 
ATOM   1465 O  O   . TRP A 1 183 ? -27.48400 44.12300 46.29200  1.000 53.48585  ? 183  TRP A O   1 
ATOM   1466 C  CB  . TRP A 1 183 ? -25.92700 44.87000 43.92600  1.000 49.76885  ? 183  TRP A CB  1 
ATOM   1467 C  CG  . TRP A 1 183 ? -24.80400 45.53500 43.19600  1.000 56.04263  ? 183  TRP A CG  1 
ATOM   1468 C  CD1 . TRP A 1 183 ? -23.80600 46.28600 43.74000  1.000 60.29962  ? 183  TRP A CD1 1 
ATOM   1469 C  CD2 . TRP A 1 183 ? -24.56100 45.51200 41.78000  1.000 57.36956  ? 183  TRP A CD2 1 
ATOM   1470 N  NE1 . TRP A 1 183 ? -22.95600 46.72500 42.76400  1.000 60.64333  ? 183  TRP A NE1 1 
ATOM   1471 C  CE2 . TRP A 1 183 ? -23.39300 46.26700 41.55200  1.000 57.65368  ? 183  TRP A CE2 1 
ATOM   1472 C  CE3 . TRP A 1 183 ? -25.20800 44.92800 40.68900  1.000 62.22530  ? 183  TRP A CE3 1 
ATOM   1473 C  CZ2 . TRP A 1 183 ? -22.86400 46.45500 40.27800  1.000 59.82655  ? 183  TRP A CZ2 1 
ATOM   1474 C  CZ3 . TRP A 1 183 ? -24.68500 45.11400 39.43000  1.000 68.76341  ? 183  TRP A CZ3 1 
ATOM   1475 C  CH2 . TRP A 1 183 ? -23.53100 45.86900 39.22900  1.000 58.30668  ? 183  TRP A CH2 1 
ATOM   1476 N  N   . ALA A 1 184 ? -26.57200 42.06900 46.03900  1.000 48.82404  ? 184  ALA A N   1 
ATOM   1477 C  CA  . ALA A 1 184 ? -27.59700 41.41600 46.87500  1.000 52.24417  ? 184  ALA A CA  1 
ATOM   1478 C  C   . ALA A 1 184 ? -27.17700 41.52700 48.34000  1.000 53.95470  ? 184  ALA A C   1 
ATOM   1479 O  O   . ALA A 1 184 ? -25.97600 41.57200 48.63300  1.000 45.54809  ? 184  ALA A O   1 
ATOM   1480 C  CB  . ALA A 1 184 ? -27.75500 39.98000 46.45800  1.000 52.31251  ? 184  ALA A CB  1 
ATOM   1481 N  N   . PRO A 1 185 ? -28.13300 41.59400 49.27700  1.000 46.39176  ? 185  PRO A N   1 
ATOM   1482 C  CA  . PRO A 1 185 ? -27.77800 41.74800 50.69200  1.000 51.39475  ? 185  PRO A CA  1 
ATOM   1483 C  C   . PRO A 1 185 ? -27.03400 40.53000 51.21700  1.000 60.55741  ? 185  PRO A C   1 
ATOM   1484 O  O   . PRO A 1 185 ? -27.41400 39.38500 50.95700  1.000 64.67474  ? 185  PRO A O   1 
ATOM   1485 C  CB  . PRO A 1 185 ? -29.13700 41.91200 51.38800  1.000 47.06663  ? 185  PRO A CB  1 
ATOM   1486 C  CG  . PRO A 1 185 ? -30.08900 42.30100 50.30600  1.000 53.95504  ? 185  PRO A CG  1 
ATOM   1487 C  CD  . PRO A 1 185 ? -29.59100 41.61300 49.07300  1.000 47.50503  ? 185  PRO A CD  1 
ATOM   1488 N  N   . LYS A 1 186 ? -26.02400 40.85000 52.03800  1.000 52.66523  ? 186  LYS A N   1 
ATOM   1489 C  CA  . LYS A 1 186 ? -25.27800 39.77200 52.71000  1.000 54.46416  ? 186  LYS A CA  1 
ATOM   1490 C  C   . LYS A 1 186 ? -26.28400 39.01600 53.55700  1.000 58.08935  ? 186  LYS A C   1 
ATOM   1491 O  O   . LYS A 1 186 ? -27.24600 39.63600 54.05500  1.000 50.23391  ? 186  LYS A O   1 
ATOM   1492 C  CB  . LYS A 1 186 ? -24.21900 40.33800 53.66100  1.000 57.34554  ? 186  LYS A CB  1 
ATOM   1493 C  CG  . LYS A 1 186 ? -22.89700 40.73500 53.01800  1.000 72.21125  ? 186  LYS A CG  1 
ATOM   1494 C  CD  . LYS A 1 186 ? -22.14700 39.56500 52.42400  1.000 71.74269  ? 186  LYS A CD  1 
ATOM   1495 C  CE  . LYS A 1 186 ? -20.72700 39.91300 52.03900  1.000 84.73759  ? 186  LYS A CE  1 
ATOM   1496 N  NZ  . LYS A 1 186 ? -20.67700 41.03800 51.07600  1.000 79.51273  ? 186  LYS A NZ  1 
ATOM   1497 N  N   . THR A 1 187 ? -26.09000 37.71700 53.67600  1.000 61.73260  ? 187  THR A N   1 
ATOM   1498 C  CA  . THR A 1 187 ? -26.94900 36.92500 54.58800  1.000 57.53299  ? 187  THR A CA  1 
ATOM   1499 C  C   . THR A 1 187 ? -26.08000 35.93700 55.35400  1.000 57.39412  ? 187  THR A C   1 
ATOM   1500 O  O   . THR A 1 187 ? -24.95600 35.67600 54.92000  1.000 54.35432  ? 187  THR A O   1 
ATOM   1501 C  CB  . THR A 1 187 ? -28.01900 36.12700 53.83500  1.000 49.87890  ? 187  THR A CB  1 
ATOM   1502 O  OG1 . THR A 1 187 ? -28.94600 35.59900 54.78300  1.000 54.08606  ? 187  THR A OG1 1 
ATOM   1503 C  CG2 . THR A 1 187 ? -27.44000 35.00400 53.00300  1.000 51.95643  ? 187  THR A CG2 1 
ATOM   1504 N  N   . ASN A 1 188 ? -26.61800 35.42000 56.44800  1.000 53.10440  ? 188  ASN A N   1 
ATOM   1505 C  CA  . ASN A 1 188 ? -25.89000 34.41100 57.24300  1.000 54.62955  ? 188  ASN A CA  1 
ATOM   1506 C  C   . ASN A 1 188 ? -26.46800 33.04300 56.85800  1.000 69.01183  ? 188  ASN A C   1 
ATOM   1507 O  O   . ASN A 1 188 ? -25.77600 32.04000 57.09800  1.000 64.70709  ? 188  ASN A O   1 
ATOM   1508 C  CB  . ASN A 1 188 ? -25.98500 34.73800 58.73600  1.000 60.68700  ? 188  ASN A CB  1 
ATOM   1509 C  CG  . ASN A 1 188 ? -25.34700 36.04600 59.14900  1.000 59.60426  ? 188  ASN A CG  1 
ATOM   1510 O  OD1 . ASN A 1 188 ? -24.47100 36.56300 58.46400  1.000 76.14679  ? 188  ASN A OD1 1 
ATOM   1511 N  ND2 . ASN A 1 188 ? -25.78100 36.58000 60.28000  1.000 77.88133  ? 188  ASN A ND2 1 
ATOM   1512 N  N   . ASP A 1 189 ? -27.66600 33.02300 56.24600  1.000 67.08108  ? 189  ASP A N   1 
ATOM   1513 C  CA  . ASP A 1 189 ? -28.33400 31.76000 55.81400  1.000 54.99691  ? 189  ASP A CA  1 
ATOM   1514 C  C   . ASP A 1 189 ? -27.43600 30.99500 54.85400  1.000 57.50762  ? 189  ASP A C   1 
ATOM   1515 O  O   . ASP A 1 189 ? -27.18500 31.49800 53.75600  1.000 62.24823  ? 189  ASP A O   1 
ATOM   1516 C  CB  . ASP A 1 189 ? -29.67400 32.01900 55.15600  1.000 50.58568  ? 189  ASP A CB  1 
ATOM   1517 C  CG  . ASP A 1 189 ? -30.43600 30.80000 54.65800  1.000 57.54815  ? 189  ASP A CG  1 
ATOM   1518 O  OD1 . ASP A 1 189 ? -29.90700 29.67900 54.78000  1.000 69.81287  ? 189  ASP A OD1 1 
ATOM   1519 O  OD2 . ASP A 1 189 ? -31.57000 30.98300 54.18200  1.000 63.44125  ? 189  ASP A OD2 1 
ATOM   1520 N  N   . THR A 1 190 ? -27.01700 29.80000 55.25600  1.000 60.09997  ? 190  THR A N   1 
ATOM   1521 C  CA  . THR A 1 190 ? -26.07300 29.02100 54.42300  1.000 64.93561  ? 190  THR A CA  1 
ATOM   1522 C  C   . THR A 1 190 ? -26.75600 28.55300 53.14700  1.000 56.14957  ? 190  THR A C   1 
ATOM   1523 O  O   . THR A 1 190 ? -26.05600 28.42500 52.13800  1.000 58.21708  ? 190  THR A O   1 
ATOM   1524 C  CB  . THR A 1 190 ? -25.47800 27.88400 55.25600  1.000 62.71602  ? 190  THR A CB  1 
ATOM   1525 O  OG1 . THR A 1 190 ? -24.86600 28.50900 56.37800  1.000 63.34750  ? 190  THR A OG1 1 
ATOM   1526 C  CG2 . THR A 1 190 ? -24.42800 27.08800 54.50500  1.000 65.73896  ? 190  THR A CG2 1 
ATOM   1527 N  N   . SER A 1 191 ? -28.06400 28.32500 53.17300  1.000 50.75531  ? 191  SER A N   1 
ATOM   1528 C  CA  . SER A 1 191 ? -28.78400 27.97100 51.91900  1.000 62.33509  ? 191  SER A CA  1 
ATOM   1529 C  C   . SER A 1 191 ? -28.79200 29.16900 50.95200  1.000 62.15561  ? 191  SER A C   1 
ATOM   1530 O  O   . SER A 1 191 ? -28.30600 29.01400 49.82600  1.000 56.60980  ? 191  SER A O   1 
ATOM   1531 C  CB  . SER A 1 191 ? -30.18000 27.48900 52.19500  1.000 52.59663  ? 191  SER A CB  1 
ATOM   1532 O  OG  . SER A 1 191 ? -30.77600 26.95400 51.02400  1.000 63.67663  ? 191  SER A OG  1 
ATOM   1533 N  N   . LEU A 1 192 ? -29.26400 30.33300 51.41100  1.000 55.42570  ? 192  LEU A N   1 
ATOM   1534 C  CA  . LEU A 1 192 ? -29.31000 31.54000 50.55000  1.000 50.62253  ? 192  LEU A CA  1 
ATOM   1535 C  C   . LEU A 1 192 ? -27.88100 31.91900 50.15400  1.000 54.93570  ? 192  LEU A C   1 
ATOM   1536 O  O   . LEU A 1 192 ? -27.69900 32.46100 49.06100  1.000 52.29347  ? 192  LEU A O   1 
ATOM   1537 C  CB  . LEU A 1 192 ? -30.03100 32.67200 51.25700  1.000 46.60176  ? 192  LEU A CB  1 
ATOM   1538 C  CG  . LEU A 1 192 ? -30.50600 33.82000 50.36800  1.000 57.57372  ? 192  LEU A CG  1 
ATOM   1539 C  CD1 . LEU A 1 192 ? -31.36300 33.23000 49.27000  1.000 49.99605  ? 192  LEU A CD1 1 
ATOM   1540 C  CD2 . LEU A 1 192 ? -31.33000 34.77400 51.20800  1.000 53.99148  ? 192  LEU A CD2 1 
ATOM   1541 N  N   . LYS A 1 193 ? -26.90700 31.58000 50.99200  1.000 52.43613  ? 193  LYS A N   1 
ATOM   1542 C  CA  . LYS A 1 193 ? -25.50900 31.84100 50.59000  1.000 56.66138  ? 193  LYS A CA  1 
ATOM   1543 C  C   . LYS A 1 193 ? -25.20800 30.97900 49.36800  1.000 56.29596  ? 193  LYS A C   1 
ATOM   1544 O  O   . LYS A 1 193 ? -24.53000 31.46200 48.44900  1.000 49.68495  ? 193  LYS A O   1 
ATOM   1545 C  CB  . LYS A 1 193 ? -24.51100 31.53800 51.70800  1.000 52.19800  ? 193  LYS A CB  1 
ATOM   1546 C  CG  . LYS A 1 193 ? -24.46900 32.50200 52.88000  1.000 55.78527  ? 193  LYS A CG  1 
ATOM   1547 C  CD  . LYS A 1 193 ? -23.22100 32.25200 53.71500  1.000 52.15682  ? 193  LYS A CD  1 
ATOM   1548 C  CE  . LYS A 1 193 ? -23.10200 33.14200 54.90100  1.000 55.94494  ? 193  LYS A CE  1 
ATOM   1549 N  NZ  . LYS A 1 193 ? -21.78500 32.99400 55.51800  1.000 76.33586  ? 193  LYS A NZ  1 
ATOM   1550 N  N   . LYS A 1 194 ? -25.72900 29.75100 49.35600  1.000 58.26449  ? 194  LYS A N   1 
ATOM   1551 C  CA  . LYS A 1 194 ? -25.51700 28.83100 48.21400  1.000 53.46600  ? 194  LYS A CA  1 
ATOM   1552 C  C   . LYS A 1 194 ? -26.20900 29.44800 46.99800  1.000 53.84617  ? 194  LYS A C   1 
ATOM   1553 O  O   . LYS A 1 194 ? -25.62500 29.46300 45.90800  1.000 44.60762  ? 194  LYS A O   1 
ATOM   1554 C  CB  . LYS A 1 194 ? -26.12400 27.45400 48.49700  1.000 45.36312  ? 194  LYS A CB  1 
ATOM   1555 C  CG  . LYS A 1 194 ? -26.05100 26.47300 47.34400  1.000 45.05405  ? 194  LYS A CG  1 
ATOM   1556 C  CD  . LYS A 1 194 ? -26.67100 25.12900 47.69300  1.000 55.25420  ? 194  LYS A CD  1 
ATOM   1557 C  CE  . LYS A 1 194 ? -25.94000 24.46000 48.80600  1.000 58.15110  ? 194  LYS A CE  1 
ATOM   1558 N  NZ  . LYS A 1 194 ? -26.55400 23.17600 49.14100  1.000 55.99897  ? 194  LYS A NZ  1 
ATOM   1559 N  N   . LEU A 1 195 ? -27.39700 29.97800 47.24100  1.000 54.27520  ? 195  LEU A N   1 
ATOM   1560 C  CA  . LEU A 1 195 ? -28.14700 30.53300 46.11600  1.000 47.60501  ? 195  LEU A CA  1 
ATOM   1561 C  C   . LEU A 1 195 ? -27.47700 31.78300 45.55600  1.000 49.39018  ? 195  LEU A C   1 
ATOM   1562 O  O   . LEU A 1 195 ? -27.45000 31.98600 44.33600  1.000 46.32842  ? 195  LEU A O   1 
ATOM   1563 C  CB  . LEU A 1 195 ? -29.58300 30.85300 46.53500  1.000 47.34785  ? 195  LEU A CB  1 
ATOM   1564 C  CG  . LEU A 1 195 ? -30.43200 31.56100 45.47000  1.000 44.24020  ? 195  LEU A CG  1 
ATOM   1565 C  CD1 . LEU A 1 195 ? -30.65000 30.66000 44.26300  1.000 46.19500  ? 195  LEU A CD1 1 
ATOM   1566 C  CD2 . LEU A 1 195 ? -31.76200 32.03900 46.03600  1.000 49.38722  ? 195  LEU A CD2 1 
ATOM   1567 N  N   . LEU A 1 196 ? -26.92800 32.63000 46.42900  1.000 45.49263  ? 196  LEU A N   1 
ATOM   1568 C  CA  . LEU A 1 196 ? -26.47200 33.96300 46.05100  1.000 49.44750  ? 196  LEU A CA  1 
ATOM   1569 C  C   . LEU A 1 196 ? -24.95200 34.06900 45.96800  1.000 46.14594  ? 196  LEU A C   1 
ATOM   1570 O  O   . LEU A 1 196 ? -24.41100 35.17900 46.00000  1.000 47.32461  ? 196  LEU A O   1 
ATOM   1571 C  CB  . LEU A 1 196 ? -27.03000 34.99700 47.03000  1.000 46.90800  ? 196  LEU A CB  1 
ATOM   1572 C  CG  . LEU A 1 196 ? -28.55500 35.03000 47.16100  1.000 44.80575  ? 196  LEU A CG  1 
ATOM   1573 C  CD1 . LEU A 1 196 ? -28.98000 36.12200 48.12500  1.000 48.40303  ? 196  LEU A CD1 1 
ATOM   1574 C  CD2 . LEU A 1 196 ? -29.20600 35.22600 45.80000  1.000 48.43004  ? 196  LEU A CD2 1 
ATOM   1575 N  N   . GLY A 1 197 ? -24.25400 32.94200 45.85700  1.000 47.94144  ? 197  GLY A N   1 
ATOM   1576 C  CA  . GLY A 1 197 ? -22.80900 32.96500 45.69100  1.000 47.05690  ? 197  GLY A CA  1 
ATOM   1577 C  C   . GLY A 1 197 ? -22.05300 33.57000 46.85300  1.000 55.71002  ? 197  GLY A C   1 
ATOM   1578 O  O   . GLY A 1 197 ? -21.00500 34.19100 46.64800  1.000 50.14760  ? 197  GLY A O   1 
ATOM   1579 N  N   . GLN A 1 198 ? -22.59100 33.44500 48.05900  1.000 53.84968  ? 198  GLN A N   1 
ATOM   1580 C  CA  . GLN A 1 198 ? -21.93000 33.99900 49.26600  1.000 50.51617  ? 198  GLN A CA  1 
ATOM   1581 C  C   . GLN A 1 198 ? -21.30000 32.86700 50.09300  1.000 62.79164  ? 198  GLN A C   1 
ATOM   1582 O  O   . GLN A 1 198 ? -21.25000 33.01600 51.31700  1.000 60.14382  ? 198  GLN A O   1 
ATOM   1583 C  CB  . GLN A 1 198 ? -22.93700 34.80200 50.08100  1.000 46.34585  ? 198  GLN A CB  1 
ATOM   1584 C  CG  . GLN A 1 198 ? -23.31200 36.14100 49.46900  1.000 49.77246  ? 198  GLN A CG  1 
ATOM   1585 C  CD  . GLN A 1 198 ? -24.39500 36.81000 50.27600  1.000 56.70851  ? 198  GLN A CD  1 
ATOM   1586 O  OE1 . GLN A 1 198 ? -24.52200 36.59300 51.47600  1.000 63.61953  ? 198  GLN A OE1 1 
ATOM   1587 N  NE2 . GLN A 1 198 ? -25.19700 37.62700 49.61600  1.000 59.81638  ? 198  GLN A NE2 1 
ATOM   1588 N  N   . LEU A 1 199 ? -20.86300 31.77400 49.46300  1.000 57.85330  ? 199  LEU A N   1 
ATOM   1589 C  CA  . LEU A 1 199 ? -20.14100 30.69900 50.17900  1.000 55.08455  ? 199  LEU A CA  1 
ATOM   1590 C  C   . LEU A 1 199 ? -18.64500 30.87000 49.94600  1.000 51.57999  ? 199  LEU A C   1 
ATOM   1591 O  O   . LEU A 1 199 ? -18.27500 31.65400 49.07300  1.000 54.72306  ? 199  LEU A O   1 
ATOM   1592 C  CB  . LEU A 1 199 ? -20.61400 29.33000 49.67700  1.000 48.90662  ? 199  LEU A CB  1 
ATOM   1593 C  CG  . LEU A 1 199 ? -22.06000 28.94900 49.97700  1.000 55.71722  ? 199  LEU A CG  1 
ATOM   1594 C  CD1 . LEU A 1 199 ? -22.42300 27.66200 49.25700  1.000 46.81895  ? 199  LEU A CD1 1 
ATOM   1595 C  CD2 . LEU A 1 199 ? -22.28100 28.79300 51.47000  1.000 49.72982  ? 199  LEU A CD2 1 
ATOM   1596 N  N   . SER A 1 200 ? -17.82800 30.21200 50.77400  1.000 46.85163  ? 200  SER A N   1 
ATOM   1597 C  CA  . SER A 1 200 ? -16.35300 30.27100 50.62000  1.000 48.21503  ? 200  SER A CA  1 
ATOM   1598 C  C   . SER A 1 200 ? -15.98500 29.93000 49.17400  1.000 54.00863  ? 200  SER A C   1 
ATOM   1599 O  O   . SER A 1 200 ? -16.70200 29.10400 48.57400  1.000 52.23544  ? 200  SER A O   1 
ATOM   1600 C  CB  . SER A 1 200 ? -15.68800 29.32400 51.59400  1.000 47.27714  ? 200  SER A CB  1 
ATOM   1601 O  OG  . SER A 1 200 ? -16.03600 27.97700 51.31200  1.000 58.85091  ? 200  SER A OG  1 
ATOM   1602 N  N   . ARG A 1 201 ? -14.93000 30.52000 48.70400  1.000 46.53810  ? 201  ARG A N   1 
ATOM   1603 C  CA  . ARG A 1 201 ? -14.49400 30.27500 47.34900  1.000 53.51538  ? 201  ARG A CA  1 
ATOM   1604 C  C   . ARG A 1 201 ? -14.34200 28.77400 47.17400  1.000 61.13011  ? 201  ARG A C   1 
ATOM   1605 O  O   . ARG A 1 201 ? -14.94100 28.24600 46.25600  1.000 55.72922  ? 201  ARG A O   1 
ATOM   1606 C  CB  . ARG A 1 201 ? -13.21300 31.04500 47.08700  1.000 51.74377  ? 201  ARG A CB  1 
ATOM   1607 C  CG  . ARG A 1 201 ? -12.71300 31.03200 45.65500  1.000 63.03104  ? 201  ARG A CG  1 
ATOM   1608 C  CD  . ARG A 1 201 ? -12.27600 32.42100 45.24100  1.000 51.30577  ? 201  ARG A CD  1 
ATOM   1609 N  NE  . ARG A 1 201 ? -13.40800 33.32800 45.25500  1.000 68.55763  ? 201  ARG A NE  1 
ATOM   1610 C  CZ  . ARG A 1 201 ? -14.09300 33.70100 44.18400  1.000 63.13796  ? 201  ARG A CZ  1 
ATOM   1611 N  NH1 . ARG A 1 201 ? -13.76700 33.24000 42.99400  1.000 59.16608  ? 201  ARG A NH1 1 
ATOM   1612 N  NH2 . ARG A 1 201 ? -15.11200 34.52300 44.30700  1.000 52.89596  ? 201  ARG A NH2 1 
ATOM   1613 N  N   . GLU A 1 202 ? -13.57800 28.12600 48.04900  1.000 60.21672  ? 202  GLU A N   1 
ATOM   1614 C  CA  . GLU A 1 202 ? -13.27900 26.67700 47.96400  1.000 49.68822  ? 202  GLU A CA  1 
ATOM   1615 C  C   . GLU A 1 202 ? -14.60100 25.92100 47.83400  1.000 50.37973  ? 202  GLU A C   1 
ATOM   1616 O  O   . GLU A 1 202 ? -14.71400 25.09200 46.94000  1.000 48.45962  ? 202  GLU A O   1 
ATOM   1617 C  CB  . GLU A 1 202 ? -12.46400 26.28200 49.19200  1.000 48.57966  ? 202  GLU A CB  1 
ATOM   1618 N  N   . GLU A 1 203 ? -15.55700 26.24700 48.68500  1.000 47.30771  ? 203  GLU A N   1 
ATOM   1619 C  CA  . GLU A 1 203 ? -16.89100 25.63300 48.60500  1.000 46.31945  ? 203  GLU A CA  1 
ATOM   1620 C  C   . GLU A 1 203 ? -17.54300 25.96200 47.26000  1.000 46.08364  ? 203  GLU A C   1 
ATOM   1621 O  O   . GLU A 1 203 ? -18.21000 25.07600 46.72300  1.000 56.76238  ? 203  GLU A O   1 
ATOM   1622 C  CB  . GLU A 1 203 ? -17.77200 26.14100 49.73800  1.000 46.84599  ? 203  GLU A CB  1 
ATOM   1623 C  CG  . GLU A 1 203 ? -17.59600 25.42200 51.05300  1.000 65.60645  ? 203  GLU A CG  1 
ATOM   1624 C  CD  . GLU A 1 203 ? -18.42300 26.05800 52.15500  1.000 78.94077  ? 203  GLU A CD  1 
ATOM   1625 O  OE1 . GLU A 1 203 ? -19.62900 25.76500 52.23100  1.000 76.19952  ? 203  GLU A OE1 1 
ATOM   1626 O  OE2 . GLU A 1 203 ? -17.86000 26.85800 52.92000  1.000 87.15794  ? 203  GLU A OE2 1 
ATOM   1627 N  N   . SER A 1 204 ? -17.37200 27.18400 46.74900  1.000 49.49947  ? 204  SER A N   1 
ATOM   1628 C  CA  . SER A 1 204 ? -18.05300 27.58200 45.52100  1.000 48.58408  ? 204  SER A CA  1 
ATOM   1629 C  C   . SER A 1 204 ? -17.45500 26.89100 44.30000  1.000 48.42411  ? 204  SER A C   1 
ATOM   1630 O  O   . SER A 1 204 ? -18.19000 26.45600 43.40600  1.000 53.38172  ? 204  SER A O   1 
ATOM   1631 C  CB  . SER A 1 204 ? -18.00600 29.10100 45.37100  1.000 54.99260  ? 204  SER A CB  1 
ATOM   1632 O  OG  . SER A 1 204 ? -18.84400 29.73200 46.32600  1.000 45.34984  ? 204  SER A OG  1 
ATOM   1633 N  N   . ASP A 1 205 ? -16.12500 26.77200 44.24100  1.000 45.16629  ? 205  ASP A N   1 
ATOM   1634 C  CA  . ASP A 1 205 ? -15.50600 26.00600 43.16300  1.000 52.50285  ? 205  ASP A CA  1 
ATOM   1635 C  C   . ASP A 1 205 ? -15.90800 24.53800 43.23500  1.000 49.66505  ? 205  ASP A C   1 
ATOM   1636 O  O   . ASP A 1 205 ? -16.18100 23.90200 42.20300  1.000 61.91893  ? 205  ASP A O   1 
ATOM   1637 C  CB  . ASP A 1 205 ? -13.98600 26.15200 43.22300  1.000 49.13504  ? 205  ASP A CB  1 
ATOM   1638 C  CG  . ASP A 1 205 ? -13.52000 27.54400 42.85500  1.000 49.31106  ? 205  ASP A CG  1 
ATOM   1639 O  OD1 . ASP A 1 205 ? -14.11000 28.14700 41.93300  1.000 54.86997  ? 205  ASP A OD1 1 
ATOM   1640 O  OD2 . ASP A 1 205 ? -12.56300 28.03600 43.48800  1.000 61.07939  ? 205  ASP A OD2 1 
ATOM   1641 N  N   . GLN A 1 206 ? -15.95200 23.98200 44.45000  1.000 54.57621  ? 206  GLN A N   1 
ATOM   1642 C  CA  . GLN A 1 206 ? -16.39700 22.60500 44.61000  1.000 50.43013  ? 206  GLN A CA  1 
ATOM   1643 C  C   . GLN A 1 206 ? -17.83400 22.43600 44.13800  1.000 50.76279  ? 206  GLN A C   1 
ATOM   1644 O  O   . GLN A 1 206 ? -18.17300 21.42700 43.51300  1.000 55.44393  ? 206  GLN A O   1 
ATOM   1645 C  CB  . GLN A 1 206 ? -16.25600 22.17000 46.06800  1.000 50.14035  ? 206  GLN A CB  1 
ATOM   1646 C  CG  . GLN A 1 206 ? -16.54500 20.69800 46.28800  1.000 45.89245  ? 206  GLN A CG  1 
ATOM   1647 C  CD  . GLN A 1 206 ? -15.63900 19.80800 45.46200  1.000 52.05164  ? 206  GLN A CD  1 
ATOM   1648 O  OE1 . GLN A 1 206 ? -14.42400 20.00700 45.42600  1.000 51.85120  ? 206  GLN A OE1 1 
ATOM   1649 N  NE2 . GLN A 1 206 ? -16.22600 18.82900 44.78400  1.000 45.60614  ? 206  GLN A NE2 1 
ATOM   1650 N  N   . LEU A 1 207 ? -18.69000 23.42400 44.41100  1.000 47.78003  ? 207  LEU A N   1 
ATOM   1651 C  CA  . LEU A 1 207 ? -20.08200 23.33100 43.98300  1.000 49.32915  ? 207  LEU A CA  1 
ATOM   1652 C  C   . LEU A 1 207 ? -20.20500 23.47100 42.47100  1.000 55.25810  ? 207  LEU A C   1 
ATOM   1653 O  O   . LEU A 1 207 ? -21.06300 22.83700 41.85400  1.000 63.73296  ? 207  LEU A O   1 
ATOM   1654 C  CB  . LEU A 1 207 ? -20.92100 24.39300 44.69500  1.000 44.77072  ? 207  LEU A CB  1 
ATOM   1655 C  CG  . LEU A 1 207 ? -22.43000 24.31400 44.46200  1.000 45.75568  ? 207  LEU A CG  1 
ATOM   1656 C  CD1 . LEU A 1 207 ? -22.94800 22.92000 44.77800  1.000 46.86698  ? 207  LEU A CD1 1 
ATOM   1657 C  CD2 . LEU A 1 207 ? -23.15700 25.35600 45.29500  1.000 48.12421  ? 207  LEU A CD2 1 
ATOM   1658 N  N   . TRP A 1 208 ? -19.36000 24.30100 41.86200  1.000 49.46595  ? 208  TRP A N   1 
ATOM   1659 C  CA  . TRP A 1 208 ? -19.27500 24.37400 40.40700  1.000 52.84095  ? 208  TRP A CA  1 
ATOM   1660 C  C   . TRP A 1 208 ? -18.99300 22.99700 39.81500  1.000 53.04519  ? 208  TRP A C   1 
ATOM   1661 O  O   . TRP A 1 208 ? -19.74400 22.48900 38.96500  1.000 52.49486  ? 208  TRP A O   1 
ATOM   1662 C  CB  . TRP A 1 208 ? -18.18200 25.38200 40.03300  1.000 51.54407  ? 208  TRP A CB  1 
ATOM   1663 C  CG  . TRP A 1 208 ? -17.88600 25.52500 38.57300  1.000 54.33101  ? 208  TRP A CG  1 
ATOM   1664 C  CD1 . TRP A 1 208 ? -18.46600 26.39800 37.70200  1.000 44.31805  ? 208  TRP A CD1 1 
ATOM   1665 C  CD2 . TRP A 1 208 ? -16.90400 24.80200 37.82100  1.000 58.69529  ? 208  TRP A CD2 1 
ATOM   1666 N  NE1 . TRP A 1 208 ? -17.92300 26.25100 36.44900  1.000 42.89631  ? 208  TRP A NE1 1 
ATOM   1667 C  CE2 . TRP A 1 208 ? -16.96000 25.27800 36.49600  1.000 56.74244  ? 208  TRP A CE2 1 
ATOM   1668 C  CE3 . TRP A 1 208 ? -15.98800 23.79400 38.13600  1.000 47.06778  ? 208  TRP A CE3 1 
ATOM   1669 C  CZ2 . TRP A 1 208 ? -16.13700 24.78000 35.48800  1.000 49.22120  ? 208  TRP A CZ2 1 
ATOM   1670 C  CZ3 . TRP A 1 208 ? -15.17400 23.30000 37.13400  1.000 45.03615  ? 208  TRP A CZ3 1 
ATOM   1671 C  CH2 . TRP A 1 208 ? -15.25300 23.79400 35.82700  1.000 49.03079  ? 208  TRP A CH2 1 
ATOM   1672 N  N   . PHE A 1 209 ? -17.91300 22.36800 40.28800  1.000 53.25267  ? 209  PHE A N   1 
ATOM   1673 C  CA  . PHE A 1 209 ? -17.56300 21.04100 39.79300  1.000 56.71003  ? 209  PHE A CA  1 
ATOM   1674 C  C   . PHE A 1 209 ? -18.66900 20.02600 40.07100  1.000 55.68551  ? 209  PHE A C   1 
ATOM   1675 O  O   . PHE A 1 209 ? -18.93800 19.14800 39.24300  1.000 55.53194  ? 209  PHE A O   1 
ATOM   1676 C  CB  . PHE A 1 209 ? -16.24900 20.56800 40.41200  1.000 56.47920  ? 209  PHE A CB  1 
ATOM   1677 C  CG  . PHE A 1 209 ? -15.88300 19.16300 40.02900  1.000 50.18246  ? 209  PHE A CG  1 
ATOM   1678 C  CD1 . PHE A 1 209 ? -15.16800 18.91300 38.87200  1.000 50.27800  ? 209  PHE A CD1 1 
ATOM   1679 C  CD2 . PHE A 1 209 ? -16.27100 18.09200 40.81600  1.000 56.83039  ? 209  PHE A CD2 1 
ATOM   1680 C  CE1 . PHE A 1 209 ? -14.84400 17.62700 38.51300  1.000 46.66670  ? 209  PHE A CE1 1 
ATOM   1681 C  CE2 . PHE A 1 209 ? -15.95200 16.80500 40.46000  1.000 51.82141  ? 209  PHE A CE2 1 
ATOM   1682 C  CZ  . PHE A 1 209 ? -15.23500 16.57200 39.30800  1.000 44.94679  ? 209  PHE A CZ  1 
ATOM   1683 N  N   . ASP A 1 210 ? -19.31000 20.11600 41.23900  1.000 49.23194  ? 210  ASP A N   1 
ATOM   1684 C  CA  . ASP A 1 210 ? -20.30300 19.11300 41.61000  1.000 56.59135  ? 210  ASP A CA  1 
ATOM   1685 C  C   . ASP A 1 210 ? -21.57600 19.25900 40.78800  1.000 52.15998  ? 210  ASP A C   1 
ATOM   1686 O  O   . ASP A 1 210 ? -22.20000 18.25800 40.42500  1.000 49.81510  ? 210  ASP A O   1 
ATOM   1687 C  CB  . ASP A 1 210 ? -20.61200 19.20200 43.10400  1.000 56.39282  ? 210  ASP A CB  1 
ATOM   1688 C  CG  . ASP A 1 210 ? -19.45000 18.74600 43.96700  1.000 58.75456  ? 210  ASP A CG  1 
ATOM   1689 O  OD1 . ASP A 1 210 ? -18.68900 17.85800 43.52700  1.000 61.41680  ? 210  ASP A OD1 1 
ATOM   1690 O  OD2 . ASP A 1 210 ? -19.29600 19.27600 45.08700  1.000 47.88881  ? 210  ASP A OD2 1 
ATOM   1691 N  N   . LYS A 1 211 ? -21.98400 20.49600 40.49500  1.000 55.14463  ? 211  LYS A N   1 
ATOM   1692 C  CA  . LYS A 1 211 ? -23.08800 20.71200 39.56800  1.000 60.70045  ? 211  LYS A CA  1 
ATOM   1693 C  C   . LYS A 1 211 ? -22.76400 20.11900 38.20500  1.000 55.19029  ? 211  LYS A C   1 
ATOM   1694 O  O   . LYS A 1 211 ? -23.59200 19.42100 37.60000  1.000 45.13233  ? 211  LYS A O   1 
ATOM   1695 C  CB  . LYS A 1 211 ? -23.38600 22.20800 39.44600  1.000 46.79556  ? 211  LYS A CB  1 
ATOM   1696 C  CG  . LYS A 1 211 ? -24.00300 22.83000 40.68600  1.000 44.67971  ? 211  LYS A CG  1 
ATOM   1697 C  CD  . LYS A 1 211 ? -24.00100 24.34900 40.58900  1.000 43.73874  ? 211  LYS A CD  1 
ATOM   1698 C  CE  . LYS A 1 211 ? -24.74400 24.98900 41.75200  1.000 43.59904  ? 211  LYS A CE  1 
ATOM   1699 N  NZ  . LYS A 1 211 ? -24.68400 26.47600 41.68800  1.000 46.52571  ? 211  LYS A NZ  1 
ATOM   1700 N  N   . HIS A 1 212 ? -21.58000 20.39600 37.68600  1.000 52.85685  ? 212  HIS A N   1 
ATOM   1701 C  CA  . HIS A 1 212 ? -21.20900 19.78100 36.39400  1.000 44.42266  ? 212  HIS A CA  1 
ATOM   1702 C  C   . HIS A 1 212 ? -21.34300 18.26100 36.49600  1.000 59.45040  ? 212  HIS A C   1 
ATOM   1703 O  O   . HIS A 1 212 ? -22.04300 17.67500 35.65400  1.000 59.01356  ? 212  HIS A O   1 
ATOM   1704 C  CB  . HIS A 1 212 ? -19.81600 20.22400 35.96700  1.000 45.59740  ? 212  HIS A CB  1 
ATOM   1705 C  CG  . HIS A 1 212 ? -19.82900 21.39200 35.04300  1.000 53.77047  ? 212  HIS A CG  1 
ATOM   1706 N  ND1 . HIS A 1 212 ? -18.71100 22.16500 34.81700  1.000 54.14527  ? 212  HIS A ND1 1 
ATOM   1707 C  CD2 . HIS A 1 212 ? -20.81500 21.91500 34.28700  1.000 42.10582  ? 212  HIS A CD2 1 
ATOM   1708 C  CE1 . HIS A 1 212 ? -19.00500 23.11100 33.95400  1.000 54.64994  ? 212  HIS A CE1 1 
ATOM   1709 N  NE2 . HIS A 1 212 ? -20.28900 22.97800 33.61500  1.000 57.55683  ? 212  HIS A NE2 1 
ATOM   1710 N  N   . ARG A 1 213 ? -20.69500 17.64900 37.48900  1.000 51.85247  ? 213  ARG A N   1 
ATOM   1711 C  CA  . ARG A 1 213 ? -20.71700 16.16500 37.59600  1.000 51.67048  ? 213  ARG A CA  1 
ATOM   1712 C  C   . ARG A 1 213 ? -22.15200 15.64900 37.67300  1.000 47.63111  ? 213  ARG A C   1 
ATOM   1713 O  O   . ARG A 1 213 ? -22.50700 14.76400 36.90400  1.000 49.97530  ? 213  ARG A O   1 
ATOM   1714 C  CB  . ARG A 1 213 ? -19.96500 15.68700 38.83900  1.000 55.31139  ? 213  ARG A CB  1 
ATOM   1715 C  CG  . ARG A 1 213 ? -20.24000 14.24000 39.21700  1.000 54.92754  ? 213  ARG A CG  1 
ATOM   1716 C  CD  . ARG A 1 213 ? -19.51900 13.81300 40.47900  1.000 51.37106  ? 213  ARG A CD  1 
ATOM   1717 N  NE  . ARG A 1 213 ? -19.77900 14.72800 41.57600  1.000 61.76986  ? 213  ARG A NE  1 
ATOM   1718 C  CZ  . ARG A 1 213 ? -20.89000 14.73100 42.29400  1.000 59.54961  ? 213  ARG A CZ  1 
ATOM   1719 N  NH1 . ARG A 1 213 ? -21.84900 13.86500 42.02400  1.000 45.75335  ? 213  ARG A NH1 1 
ATOM   1720 N  NH2 . ARG A 1 213 ? -21.04400 15.60500 43.27100  1.000 52.56451  ? 213  ARG A NH2 1 
ATOM   1721 N  N   . GLU A 1 214 ? -22.94000 16.18800 38.59500  1.000 43.29894  ? 214  GLU A N   1 
ATOM   1722 C  CA  . GLU A 1 214 ? -24.35000 15.75400 38.71900  1.000 45.59884  ? 214  GLU A CA  1 
ATOM   1723 C  C   . GLU A 1 214 ? -25.04300 15.81300 37.35600  1.000 50.44607  ? 214  GLU A C   1 
ATOM   1724 O  O   . GLU A 1 214 ? -25.63800 14.79500 36.96500  1.000 54.10257  ? 214  GLU A O   1 
ATOM   1725 C  CB  . GLU A 1 214 ? -25.12100 16.64800 39.68400  1.000 52.67471  ? 214  GLU A CB  1 
ATOM   1726 C  CG  . GLU A 1 214 ? -24.98600 16.27900 41.14200  1.000 53.68152  ? 214  GLU A CG  1 
ATOM   1727 C  CD  . GLU A 1 214 ? -25.90900 17.13800 41.98300  1.000 64.62945  ? 214  GLU A CD  1 
ATOM   1728 O  OE1 . GLU A 1 214 ? -26.42500 18.12700 41.43900  1.000 67.05117  ? 214  GLU A OE1 1 
ATOM   1729 O  OE2 . GLU A 1 214 ? -26.12400 16.80900 43.16100  1.000 64.65063  ? 214  GLU A OE2 1 
ATOM   1730 N  N   . MET A 1 215 ? -24.97500 16.95400 36.66400  1.000 44.12931  ? 215  MET A N   1 
ATOM   1731 C  CA  . MET A 1 215 ? -25.72900 17.08100 35.42100  1.000 47.65084  ? 215  MET A CA  1 
ATOM   1732 C  C   . MET A 1 215 ? -25.17900 16.16300 34.33200  1.000 49.40927  ? 215  MET A C   1 
ATOM   1733 O  O   . MET A 1 215 ? -25.95200 15.50100 33.62100  1.000 51.11198  ? 215  MET A O   1 
ATOM   1734 C  CB  . MET A 1 215 ? -25.73200 18.54100 34.96800  1.000 44.76672  ? 215  MET A CB  1 
ATOM   1735 C  CG  . MET A 1 215 ? -26.43200 18.79700 33.65100  1.000 55.25822  ? 215  MET A CG  1 
ATOM   1736 S  SD  . MET A 1 215 ? -25.26400 18.78400 32.28300  1.000 46.38356  ? 215  MET A SD  1 
ATOM   1737 C  CE  . MET A 1 215 ? -24.02000 19.89600 32.93100  1.000 51.53578  ? 215  MET A CE  1 
ATOM   1738 N  N   . LEU A 1 216 ? -23.86200 16.14300 34.14800  1.000 50.84760  ? 216  LEU A N   1 
ATOM   1739 C  CA  . LEU A 1 216 ? -23.25700 15.37200 33.03400  1.000 44.96291  ? 216  LEU A CA  1 
ATOM   1740 C  C   . LEU A 1 216 ? -23.46800 13.86100 33.23500  1.000 55.61183  ? 216  LEU A C   1 
ATOM   1741 O  O   . LEU A 1 216 ? -23.42600 13.13600 32.23700  1.000 51.68685  ? 216  LEU A O   1 
ATOM   1742 C  CB  . LEU A 1 216 ? -21.77100 15.71900 32.96400  1.000 41.96559  ? 216  LEU A CB  1 
ATOM   1743 C  CG  . LEU A 1 216 ? -20.85000 15.05500 33.98200  1.000 53.69158  ? 216  LEU A CG  1 
ATOM   1744 C  CD1 . LEU A 1 216 ? -20.36400 13.71300 33.42700  1.000 47.32773  ? 216  LEU A CD1 1 
ATOM   1745 C  CD2 . LEU A 1 216 ? -19.64500 15.94900 34.21800  1.000 54.20480  ? 216  LEU A CD2 1 
ATOM   1746 N  N   . ASP A 1 217 ? -23.65600 13.41300 34.47800  1.000 54.61753  ? 217  ASP A N   1 
ATOM   1747 C  CA  . ASP A 1 217 ? -23.90300 11.98400 34.77500  1.000 48.41142  ? 217  ASP A CA  1 
ATOM   1748 C  C   . ASP A 1 217 ? -25.40600 11.73200 34.67200  1.000 47.58989  ? 217  ASP A C   1 
ATOM   1749 O  O   . ASP A 1 217 ? -25.78400 10.59700 34.40700  1.000 62.84608  ? 217  ASP A O   1 
ATOM   1750 C  CB  . ASP A 1 217 ? -23.31000 11.59900 36.13800  1.000 47.61920  ? 217  ASP A CB  1 
ATOM   1751 C  CG  . ASP A 1 217 ? -21.79500 11.52800 36.18600  1.000 46.42972  ? 217  ASP A CG  1 
ATOM   1752 O  OD1 . ASP A 1 217 ? -21.17800 11.34800 35.13000  1.000 47.45048  ? 217  ASP A OD1 1 
ATOM   1753 O  OD2 . ASP A 1 217 ? -21.25000 11.64800 37.29000  1.000 44.80392  ? 217  ASP A OD2 1 
ATOM   1754 N  N   . HIS A 1 218 ? -26.21900 12.75900 34.87600  1.000 49.19178  ? 218  HIS A N   1 
ATOM   1755 C  CA  . HIS A 1 218 ? -27.69100 12.60200 34.84700  1.000 45.03877  ? 218  HIS A CA  1 
ATOM   1756 C  C   . HIS A 1 218 ? -28.18500 12.51500 33.40800  1.000 48.01803  ? 218  HIS A C   1 
ATOM   1757 O  O   . HIS A 1 218 ? -29.06900 11.70100 33.16500  1.000 47.30171  ? 218  HIS A O   1 
ATOM   1758 C  CB  . HIS A 1 218 ? -28.36800 13.76700 35.55500  1.000 42.29169  ? 218  HIS A CB  1 
ATOM   1759 C  CG  . HIS A 1 218 ? -29.83100 13.60500 35.76500  1.000 48.93283  ? 218  HIS A CG  1 
ATOM   1760 N  ND1 . HIS A 1 218 ? -30.36600 12.50500 36.39000  1.000 50.43487  ? 218  HIS A ND1 1 
ATOM   1761 C  CD2 . HIS A 1 218 ? -30.86600 14.41700 35.47300  1.000 44.21444  ? 218  HIS A CD2 1 
ATOM   1762 C  CE1 . HIS A 1 218 ? -31.67200 12.63200 36.45600  1.000 51.32070  ? 218  HIS A CE1 1 
ATOM   1763 N  NE2 . HIS A 1 218 ? -32.00100 13.79400 35.90000  1.000 49.17571  ? 218  HIS A NE2 1 
ATOM   1764 N  N   . VAL A 1 219 ? -27.64800 13.34400 32.50600  1.000 54.63913  ? 219  VAL A N   1 
ATOM   1765 C  CA  . VAL A 1 219 ? -28.19000 13.37000 31.15100  1.000 48.45571  ? 219  VAL A CA  1 
ATOM   1766 C  C   . VAL A 1 219 ? -27.16400 13.03000 30.08000  1.000 43.85358  ? 219  VAL A C   1 
ATOM   1767 O  O   . VAL A 1 219 ? -27.54100 12.88700 28.91200  1.000 42.35907  ? 219  VAL A O   1 
ATOM   1768 C  CB  . VAL A 1 219 ? -28.85600 14.72600 30.83600  1.000 52.12999  ? 219  VAL A CB  1 
ATOM   1769 C  CG1 . VAL A 1 219 ? -30.08400 14.92300 31.71300  1.000 41.13276  ? 219  VAL A CG1 1 
ATOM   1770 C  CG2 . VAL A 1 219 ? -27.86800 15.86500 31.01900  1.000 48.61561  ? 219  VAL A CG2 1 
ATOM   1771 N  N   . GLN A 1 220 ? -25.91200 12.85200 30.46100  1.000 42.82668  ? 220  GLN A N   1 
ATOM   1772 C  CA  . GLN A 1 220 ? -24.82200 12.52900 29.50600  1.000 50.30793  ? 220  GLN A CA  1 
ATOM   1773 C  C   . GLN A 1 220 ? -24.88400 13.47100 28.29400  1.000 54.33804  ? 220  GLN A C   1 
ATOM   1774 O  O   . GLN A 1 220 ? -25.15500 12.99100 27.18700  1.000 53.26707  ? 220  GLN A O   1 
ATOM   1775 C  CB  . GLN A 1 220 ? -24.81200 11.06400 29.05900  1.000 53.70326  ? 220  GLN A CB  1 
ATOM   1776 C  CG  . GLN A 1 220 ? -24.96300 10.05600 30.19200  1.000 56.63576  ? 220  GLN A CG  1 
ATOM   1777 C  CD  . GLN A 1 220 ? -26.39900 9.65600  30.44000  1.000 63.31255  ? 220  GLN A CD  1 
ATOM   1778 O  OE1 . GLN A 1 220 ? -27.24000 9.68100  29.53700  1.000 58.90570  ? 220  GLN A OE1 1 
ATOM   1779 N  NE2 . GLN A 1 220 ? -26.69700 9.28700  31.67700  1.000 67.93465  ? 220  GLN A NE2 1 
ATOM   1780 N  N   . PRO A 1 221 ? -24.56500 14.77500 28.43500  1.000 56.88885  ? 221  PRO A N   1 
ATOM   1781 C  CA  . PRO A 1 221 ? -24.68600 15.70000 27.30600  1.000 46.37568  ? 221  PRO A CA  1 
ATOM   1782 C  C   . PRO A 1 221 ? -23.55000 15.52300 26.31200  1.000 49.12705  ? 221  PRO A C   1 
ATOM   1783 O  O   . PRO A 1 221 ? -22.43500 15.13000 26.66200  1.000 41.04129  ? 221  PRO A O   1 
ATOM   1784 C  CB  . PRO A 1 221 ? -24.62900 17.07600 27.97500  1.000 43.69879  ? 221  PRO A CB  1 
ATOM   1785 C  CG  . PRO A 1 221 ? -23.78500 16.85100 29.17600  1.000 39.72708  ? 221  PRO A CG  1 
ATOM   1786 C  CD  . PRO A 1 221 ? -24.08800 15.45200 29.65200  1.000 44.27572  ? 221  PRO A CD  1 
ATOM   1787 N  N   . ASP A 1 222 ? -23.85600 15.82100 25.05000  1.000 47.73506  ? 222  ASP A N   1 
ATOM   1788 C  CA  . ASP A 1 222 ? -22.84400 15.76800 24.00300  1.000 44.19464  ? 222  ASP A CA  1 
ATOM   1789 C  C   . ASP A 1 222 ? -22.01400 17.04400 23.95100  1.000 46.08259  ? 222  ASP A C   1 
ATOM   1790 O  O   . ASP A 1 222 ? -20.86800 17.01400 23.48800  1.000 39.51583  ? 222  ASP A O   1 
ATOM   1791 C  CB  . ASP A 1 222 ? -23.50900 15.51000 22.65000  1.000 41.52883  ? 222  ASP A CB  1 
ATOM   1792 C  CG  . ASP A 1 222 ? -24.30000 14.21600 22.62800  1.000 40.64038  ? 222  ASP A CG  1 
ATOM   1793 O  OD1 . ASP A 1 222 ? -23.68400 13.13700 22.75900  1.000 41.33553  ? 222  ASP A OD1 1 
ATOM   1794 O  OD2 . ASP A 1 222 ? -25.54000 14.28000 22.50000  1.000 42.30765  ? 222  ASP A OD2 1 
ATOM   1795 N  N   . ILE A 1 223 ? -22.56900 18.16300 24.41300  1.000 46.75833  ? 223  ILE A N   1 
ATOM   1796 C  CA  . ILE A 1 223 ? -21.86400 19.43800 24.46400  1.000 39.55386  ? 223  ILE A CA  1 
ATOM   1797 C  C   . ILE A 1 223 ? -22.09600 20.06500 25.83200  1.000 41.00330  ? 223  ILE A C   1 
ATOM   1798 O  O   . ILE A 1 223 ? -23.23500 20.12400 26.30700  1.000 39.60768  ? 223  ILE A O   1 
ATOM   1799 C  CB  . ILE A 1 223 ? -22.32000 20.40300 23.35200  1.000 39.50177  ? 223  ILE A CB  1 
ATOM   1800 C  CG1 . ILE A 1 223 ? -22.12700 19.77600 21.97200  1.000 42.66330  ? 223  ILE A CG1 1 
ATOM   1801 C  CG2 . ILE A 1 223 ? -21.55300 21.71500 23.44100  1.000 39.56868  ? 223  ILE A CG2 1 
ATOM   1802 C  CD1 . ILE A 1 223 ? -22.62400 20.64400 20.83500  1.000 39.40296  ? 223  ILE A CD1 1 
ATOM   1803 N  N   . ILE A 1 224 ? -21.01800 20.52600 26.46100  1.000 46.60492  ? 224  ILE A N   1 
ATOM   1804 C  CA  . ILE A 1 224 ? -21.08300 21.30000 27.69600  1.000 41.41371  ? 224  ILE A CA  1 
ATOM   1805 C  C   . ILE A 1 224 ? -20.76300 22.74400 27.33800  1.000 43.28251  ? 224  ILE A C   1 
ATOM   1806 O  O   . ILE A 1 224 ? -19.60800 23.08200 27.04600  1.000 44.87890  ? 224  ILE A O   1 
ATOM   1807 C  CB  . ILE A 1 224 ? -20.11700 20.77000 28.76400  1.000 56.95669  ? 224  ILE A CB  1 
ATOM   1808 C  CG1 . ILE A 1 224 ? -20.61200 19.43700 29.31800  1.000 51.38107  ? 224  ILE A CG1 1 
ATOM   1809 C  CG2 . ILE A 1 224 ? -19.97200 21.77600 29.89800  1.000 46.10147  ? 224  ILE A CG2 1 
ATOM   1810 C  CD1 . ILE A 1 224 ? -21.77500 19.57200 30.25300  1.000 51.38566  ? 224  ILE A CD1 1 
ATOM   1811 N  N   . TRP A 1 225 ? -21.77900 23.60100 27.35400  1.000 41.69022  ? 225  TRP A N   1 
ATOM   1812 C  CA  . TRP A 1 225 ? -21.60200 25.00900 27.02800  1.000 47.76451  ? 225  TRP A CA  1 
ATOM   1813 C  C   . TRP A 1 225 ? -21.34600 25.78900 28.31200  1.000 44.64335  ? 225  TRP A C   1 
ATOM   1814 O  O   . TRP A 1 225 ? -22.20300 25.83100 29.20200  1.000 45.43317  ? 225  TRP A O   1 
ATOM   1815 C  CB  . TRP A 1 225 ? -22.82600 25.55200 26.29300  1.000 45.67872  ? 225  TRP A CB  1 
ATOM   1816 C  CG  . TRP A 1 225 ? -22.59400 26.88000 25.64100  1.000 41.67910  ? 225  TRP A CG  1 
ATOM   1817 C  CD1 . TRP A 1 225 ? -22.24700 27.10700 24.34000  1.000 42.43762  ? 225  TRP A CD1 1 
ATOM   1818 C  CD2 . TRP A 1 225 ? -22.68900 28.16700 26.26000  1.000 44.89043  ? 225  TRP A CD2 1 
ATOM   1819 N  NE1 . TRP A 1 225 ? -22.12200 28.45600 24.11200  1.000 42.01333  ? 225  TRP A NE1 1 
ATOM   1820 C  CE2 . TRP A 1 225 ? -22.38800 29.12800 25.27500  1.000 43.45481  ? 225  TRP A CE2 1 
ATOM   1821 C  CE3 . TRP A 1 225 ? -23.00000 28.59900 27.55200  1.000 43.33919  ? 225  TRP A CE3 1 
ATOM   1822 C  CZ2 . TRP A 1 225 ? -22.39000 30.49500 25.54300  1.000 44.29593  ? 225  TRP A CZ2 1 
ATOM   1823 C  CZ3 . TRP A 1 225 ? -22.99800 29.95400 27.81400  1.000 40.03654  ? 225  TRP A CZ3 1 
ATOM   1824 C  CH2 . TRP A 1 225 ? -22.69800 30.88600 26.81500  1.000 46.01883  ? 225  TRP A CH2 1 
ATOM   1825 N  N   . ASN A 1 226 ? -20.14500 26.32600 28.40200  1.000 41.11503  ? 226  ASN A N   1 
ATOM   1826 C  CA  . ASN A 1 226 ? -19.77000 27.10800 29.60500  1.000 48.13975  ? 226  ASN A CA  1 
ATOM   1827 C  C   . ASN A 1 226 ? -19.77100 28.61200 29.30600  1.000 51.02108  ? 226  ASN A C   1 
ATOM   1828 O  O   . ASN A 1 226 ? -19.15200 29.02200 28.31700  1.000 41.59122  ? 226  ASN A O   1 
ATOM   1829 C  CB  . ASN A 1 226 ? -18.42500 26.65500 30.16400  1.000 45.65325  ? 226  ASN A CB  1 
ATOM   1830 C  CG  . ASN A 1 226 ? -18.46700 25.25000 30.70500  1.000 53.34440  ? 226  ASN A CG  1 
ATOM   1831 O  OD1 . ASN A 1 226 ? -19.30000 24.94500 31.56300  1.000 54.18146  ? 226  ASN A OD1 1 
ATOM   1832 N  ND2 . ASN A 1 226 ? -17.59100 24.39000 30.21200  1.000 41.65428  ? 226  ASN A ND2 1 
ATOM   1833 N  N   . ASP A 1 227 ? -20.40400 29.38300 30.17900  1.000 47.09761  ? 227  ASP A N   1 
ATOM   1834 C  CA  . ASP A 1 227 ? -20.38700 30.86300 30.06900  1.000 45.58005  ? 227  ASP A CA  1 
ATOM   1835 C  C   . ASP A 1 227 ? -19.10400 31.39100 30.72200  1.000 49.78888  ? 227  ASP A C   1 
ATOM   1836 O  O   . ASP A 1 227 ? -18.18200 30.58400 30.92800  1.000 43.24355  ? 227  ASP A O   1 
ATOM   1837 C  CB  . ASP A 1 227 ? -21.65900 31.49100 30.60700  1.000 48.30582  ? 227  ASP A CB  1 
ATOM   1838 C  CG  . ASP A 1 227 ? -22.00800 32.86700 30.06200  1.000 45.78410  ? 227  ASP A CG  1 
ATOM   1839 O  OD1 . ASP A 1 227 ? -21.22900 33.39000 29.25000  1.000 49.13715  ? 227  ASP A OD1 1 
ATOM   1840 O  OD2 . ASP A 1 227 ? -23.06300 33.39100 30.45000  1.000 47.30428  ? 227  ASP A OD2 1 
ATOM   1841 N  N   . PHE A 1 228 ? -19.03000 32.68900 31.00900  1.000 41.84862  ? 228  PHE A N   1 
ATOM   1842 C  CA  . PHE A 1 228 ? -17.74700 33.30500 31.44300  1.000 40.91741  ? 228  PHE A CA  1 
ATOM   1843 C  C   . PHE A 1 228 ? -17.42900 33.08900 32.92000  1.000 43.58953  ? 228  PHE A C   1 
ATOM   1844 O  O   . PHE A 1 228 ? -18.22000 32.43200 33.59900  1.000 41.02919  ? 228  PHE A O   1 
ATOM   1845 C  CB  . PHE A 1 228 ? -17.82400 34.78700 31.04300  1.000 44.75671  ? 228  PHE A CB  1 
ATOM   1846 C  CG  . PHE A 1 228 ? -18.67200 35.69000 31.92300  1.000 41.04636  ? 228  PHE A CG  1 
ATOM   1847 C  CD1 . PHE A 1 228 ? -20.05500 35.68700 31.82200  1.000 41.33745  ? 228  PHE A CD1 1 
ATOM   1848 C  CD2 . PHE A 1 228 ? -18.07700 36.56800 32.81700  1.000 41.25662  ? 228  PHE A CD2 1 
ATOM   1849 C  CE1 . PHE A 1 228 ? -20.82000 36.51500 32.62100  1.000 47.90729  ? 228  PHE A CE1 1 
ATOM   1850 C  CE2 . PHE A 1 228 ? -18.84900 37.39400 33.61000  1.000 41.32945  ? 228  PHE A CE2 1 
ATOM   1851 C  CZ  . PHE A 1 228 ? -20.21400 37.36900 33.50700  1.000 46.17555  ? 228  PHE A CZ  1 
ATOM   1852 N  N   . SER A 1 229 ? -16.34300 33.71100 33.39100  1.000 46.89558  ? 229  SER A N   1 
ATOM   1853 C  CA  . SER A 1 229 ? -15.86100 33.60100 34.79900  1.000 46.80285  ? 229  SER A CA  1 
ATOM   1854 C  C   . SER A 1 229 ? -15.12300 32.28300 35.07600  1.000 48.45926  ? 229  SER A C   1 
ATOM   1855 O  O   . SER A 1 229 ? -15.10300 31.87800 36.23900  1.000 53.55514  ? 229  SER A O   1 
ATOM   1856 C  CB  . SER A 1 229 ? -16.92300 33.90900 35.82100  1.000 45.53145  ? 229  SER A CB  1 
ATOM   1857 O  OG  . SER A 1 229 ? -16.32200 34.29300 37.04400  1.000 57.49631  ? 229  SER A OG  1 
ATOM   1858 N  N   . LEU A 1 230 ? -14.58100 31.62900 34.05400  1.000 41.37560  ? 230  LEU A N   1 
ATOM   1859 C  CA  . LEU A 1 230 ? -13.72600 30.43700 34.28000  1.000 45.32588  ? 230  LEU A CA  1 
ATOM   1860 C  C   . LEU A 1 230 ? -12.32000 30.96600 34.58900  1.000 53.43146  ? 230  LEU A C   1 
ATOM   1861 O  O   . LEU A 1 230 ? -11.74900 30.51500 35.58600  1.000 49.92352  ? 230  LEU A O   1 
ATOM   1862 C  CB  . LEU A 1 230 ? -13.74200 29.49800 33.07500  1.000 46.19688  ? 230  LEU A CB  1 
ATOM   1863 C  CG  . LEU A 1 230 ? -15.11300 29.00100 32.61200  1.000 43.06419  ? 230  LEU A CG  1 
ATOM   1864 C  CD1 . LEU A 1 230 ? -14.93300 28.01700 31.48300  1.000 40.85233  ? 230  LEU A CD1 1 
ATOM   1865 C  CD2 . LEU A 1 230 ? -15.90600 28.37700 33.73700  1.000 50.51235  ? 230  LEU A CD2 1 
ATOM   1866 N  N   . ASP A 1 231 ? -11.76100 31.80700 33.72200  1.000 48.68119  ? 231  ASP A N   1 
ATOM   1867 C  CA  . ASP A 1 231 ? -10.48500 32.51600 33.98600  1.000 52.17553  ? 231  ASP A CA  1 
ATOM   1868 C  C   . ASP A 1 231 ? -10.55300 33.74700 33.08100  1.000 56.31308  ? 231  ASP A C   1 
ATOM   1869 O  O   . ASP A 1 231 ? -9.75400  33.84400 32.14300  1.000 49.47401  ? 231  ASP A O   1 
ATOM   1870 C  CB  . ASP A 1 231 ? -9.23600  31.66100 33.80600  1.000 52.49882  ? 231  ASP A CB  1 
ATOM   1871 C  CG  . ASP A 1 231 ? -7.96100  32.37300 34.22300  1.000 58.62369  ? 231  ASP A CG  1 
ATOM   1872 O  OD1 . ASP A 1 231 ? -8.06600  33.44600 34.83200  1.000 51.32916  ? 231  ASP A OD1 1 
ATOM   1873 O  OD2 . ASP A 1 231 ? -6.87400  31.84800 33.93000  1.000 62.20087  ? 231  ASP A OD2 1 
ATOM   1874 N  N   . SER A 1 232 ? -11.50000 34.63400 33.37300  1.000 50.71522  ? 232  SER A N   1 
ATOM   1875 C  CA  . SER A 1 232 ? -11.73200 35.82000 32.51500  1.000 43.56182  ? 232  SER A CA  1 
ATOM   1876 C  C   . SER A 1 232 ? -11.54400 37.11600 33.32900  1.000 54.33718  ? 232  SER A C   1 
ATOM   1877 O  O   . SER A 1 232 ? -12.56600 37.75700 33.64300  1.000 47.46838  ? 232  SER A O   1 
ATOM   1878 C  CB  . SER A 1 232 ? -13.10600 35.74400 31.90600  1.000 41.63208  ? 232  SER A CB  1 
ATOM   1879 O  OG  . SER A 1 232 ? -14.12700 35.70800 32.88900  1.000 51.65719  ? 232  SER A OG  1 
ATOM   1880 N  N   . PRO A 1 233 ? -10.32000 37.53100 33.72100  1.000 53.01650  ? 233  PRO A N   1 
ATOM   1881 C  CA  . PRO A 1 233 ? -10.16800 38.77100 34.50200  1.000 54.53951  ? 233  PRO A CA  1 
ATOM   1882 C  C   . PRO A 1 233 ? -10.62400 39.95600 33.66200  1.000 53.56795  ? 233  PRO A C   1 
ATOM   1883 O  O   . PRO A 1 233 ? -10.20000 40.08300 32.49700  1.000 56.95799  ? 233  PRO A O   1 
ATOM   1884 C  CB  . PRO A 1 233 ? -8.69500  38.79200 34.85400  1.000 54.74775  ? 233  PRO A CB  1 
ATOM   1885 C  CG  . PRO A 1 233 ? -8.02900  37.99100 33.76100  1.000 58.87992  ? 233  PRO A CG  1 
ATOM   1886 C  CD  . PRO A 1 233 ? -8.98100  36.87600 33.53900  1.000 58.54542  ? 233  PRO A CD  1 
ATOM   1887 N  N   . GLY A 1 234 ? -11.39600 40.84600 34.26800  1.000 53.03096  ? 234  GLY A N   1 
ATOM   1888 C  CA  . GLY A 1 234 ? -11.87900 42.04800 33.56100  1.000 57.04279  ? 234  GLY A CA  1 
ATOM   1889 C  C   . GLY A 1 234 ? -13.33100 42.00600 33.16100  1.000 47.31733  ? 234  GLY A C   1 
ATOM   1890 O  O   . GLY A 1 234 ? -13.81100 43.02300 32.64700  1.000 43.82445  ? 234  GLY A O   1 
ATOM   1891 N  N   . TYR A 1 235 ? -14.03300 40.92900 33.48200  1.000 44.80538  ? 235  TYR A N   1 
ATOM   1892 C  CA  . TYR A 1 235 ? -15.42900 40.79800 33.00500  1.000 45.34083  ? 235  TYR A CA  1 
ATOM   1893 C  C   . TYR A 1 235 ? -16.32900 40.61300 34.19000  1.000 47.57904  ? 235  TYR A C   1 
ATOM   1894 O  O   . TYR A 1 235 ? -17.52100 40.35800 34.00100  1.000 41.75357  ? 235  TYR A O   1 
ATOM   1895 C  CB  . TYR A 1 235 ? -15.48700 39.67300 31.97100  1.000 41.70266  ? 235  TYR A CB  1 
ATOM   1896 C  CG  . TYR A 1 235 ? -14.71700 39.87600 30.67500  1.000 43.48830  ? 235  TYR A CG  1 
ATOM   1897 C  CD1 . TYR A 1 235 ? -13.38000 39.51900 30.57300  1.000 47.61223  ? 235  TYR A CD1 1 
ATOM   1898 C  CD2 . TYR A 1 235 ? -15.34400 40.36800 29.53900  1.000 46.40760  ? 235  TYR A CD2 1 
ATOM   1899 C  CE1 . TYR A 1 235 ? -12.67900 39.68700 29.39200  1.000 47.67088  ? 235  TYR A CE1 1 
ATOM   1900 C  CE2 . TYR A 1 235 ? -14.65500 40.53800 28.35100  1.000 41.54739  ? 235  TYR A CE2 1 
ATOM   1901 C  CZ  . TYR A 1 235 ? -13.31900 40.19500 28.27700  1.000 45.44251  ? 235  TYR A CZ  1 
ATOM   1902 O  OH  . TYR A 1 235 ? -12.63200 40.35800 27.11300  1.000 43.85893  ? 235  TYR A OH  1 
ATOM   1903 N  N   . CYS A 1 236 ? -15.76100 40.76600 35.38600  1.000 43.55957  ? 236  CYS A N   1 
ATOM   1904 C  CA  . CYS A 1 236 ? -16.57300 40.62600 36.62200  1.000 47.06275  ? 236  CYS A CA  1 
ATOM   1905 C  C   . CYS A 1 236 ? -16.69500 41.97700 37.32200  1.000 47.25162  ? 236  CYS A C   1 
ATOM   1906 O  O   . CYS A 1 236 ? -16.87200 41.98600 38.53900  1.000 52.91337  ? 236  CYS A O   1 
ATOM   1907 C  CB  . CYS A 1 236 ? -16.02200 39.55100 37.55100  1.000 42.26973  ? 236  CYS A CB  1 
ATOM   1908 S  SG  . CYS A 1 236 ? -16.20200 37.87200 36.90600  1.000 50.88498  ? 236  CYS A SG  1 
ATOM   1909 N  N   . ALA A 1 237 ? -16.63900 43.06400 36.56000  1.000 51.18158  ? 237  ALA A N   1 
ATOM   1910 C  CA  . ALA A 1 237 ? -16.86400 44.40900 37.12900  1.000 49.20552  ? 237  ALA A CA  1 
ATOM   1911 C  C   . ALA A 1 237 ? -15.82500 44.73800 38.20200  1.000 48.45277  ? 237  ALA A C   1 
ATOM   1912 O  O   . ALA A 1 237 ? -14.63100 44.58100 37.93400  1.000 54.22958  ? 237  ALA A O   1 
ATOM   1913 C  CB  . ALA A 1 237 ? -18.25900 44.48300 37.67600  1.000 42.50823  ? 237  ALA A CB  1 
ATOM   1914 N  N   . ASP A 1 238 ? -16.29100 45.16100 39.36700  1.000 43.04063  ? 238  ASP A N   1 
ATOM   1915 C  CA  . ASP A 1 238 ? -15.36300 45.58000 40.44400  1.000 47.82439  ? 238  ASP A CA  1 
ATOM   1916 C  C   . ASP A 1 238 ? -15.64800 44.73200 41.68100  1.000 52.09136  ? 238  ASP A C   1 
ATOM   1917 O  O   . ASP A 1 238 ? -15.57600 45.27200 42.78700  1.000 55.76114  ? 238  ASP A O   1 
ATOM   1918 C  CB  . ASP A 1 238 ? -15.49400 47.07500 40.74000  1.000 43.55469  ? 238  ASP A CB  1 
ATOM   1919 C  CG  . ASP A 1 238 ? -15.31700 47.98300 39.54000  1.000 49.60209  ? 238  ASP A CG  1 
ATOM   1920 O  OD1 . ASP A 1 238 ? -14.27500 47.88100 38.87300  1.000 53.67915  ? 238  ASP A OD1 1 
ATOM   1921 O  OD2 . ASP A 1 238 ? -16.21900 48.79700 39.30200  1.000 43.90149  ? 238  ASP A OD2 1 
ATOM   1922 N  N   . PHE A 1 239 ? -16.00900 43.46700 41.48200  1.000 47.88581  ? 239  PHE A N   1 
ATOM   1923 C  CA  . PHE A 1 239 ? -16.24400 42.55100 42.62200  1.000 46.71054  ? 239  PHE A CA  1 
ATOM   1924 C  C   . PHE A 1 239 ? -14.88100 42.10700 43.13600  1.000 46.84145  ? 239  PHE A C   1 
ATOM   1925 O  O   . PHE A 1 239 ? -13.95900 41.94100 42.33600  1.000 54.21040  ? 239  PHE A O   1 
ATOM   1926 C  CB  . PHE A 1 239 ? -17.14800 41.39600 42.19900  1.000 46.46836  ? 239  PHE A CB  1 
ATOM   1927 C  CG  . PHE A 1 239 ? -17.38300 40.30500 43.20900  1.000 54.71371  ? 239  PHE A CG  1 
ATOM   1928 C  CD1 . PHE A 1 239 ? -18.42700 40.39000 44.11100  1.000 47.55914  ? 239  PHE A CD1 1 
ATOM   1929 C  CD2 . PHE A 1 239 ? -16.59000 39.17100 43.21800  1.000 50.95494  ? 239  PHE A CD2 1 
ATOM   1930 C  CE1 . PHE A 1 239 ? -18.65600 39.37400 45.02300  1.000 55.54946  ? 239  PHE A CE1 1 
ATOM   1931 C  CE2 . PHE A 1 239 ? -16.81900 38.15700 44.13100  1.000 50.33619  ? 239  PHE A CE2 1 
ATOM   1932 C  CZ  . PHE A 1 239 ? -17.85000 38.26100 45.03200  1.000 58.14106  ? 239  PHE A CZ  1 
ATOM   1933 N  N   . ASP A 1 240 ? -14.72700 41.97100 44.44800  1.000 44.14507  ? 240  ASP A N   1 
ATOM   1934 C  CA  . ASP A 1 240 ? -13.44000 41.43800 44.97500  1.000 52.11093  ? 240  ASP A CA  1 
ATOM   1935 C  C   . ASP A 1 240 ? -13.39800 39.94500 44.66300  1.000 58.47283  ? 240  ASP A C   1 
ATOM   1936 O  O   . ASP A 1 240 ? -13.78200 39.15400 45.53300  1.000 63.48708  ? 240  ASP A O   1 
ATOM   1937 C  CB  . ASP A 1 240 ? -13.22900 41.74400 46.46100  1.000 54.16981  ? 240  ASP A CB  1 
ATOM   1938 C  CG  . ASP A 1 240 ? -11.85200 41.36700 46.97100  1.000 61.51961  ? 240  ASP A CG  1 
ATOM   1939 O  OD1 . ASP A 1 240 ? -10.90100 41.40200 46.17600  1.000 64.41896  ? 240  ASP A OD1 1 
ATOM   1940 O  OD2 . ASP A 1 240 ? -11.74700 41.04100 48.16000  1.000 79.08124  ? 240  ASP A OD2 1 
ATOM   1941 N  N   . GLY A 1 241 ? -12.97900 39.60300 43.45200  1.000 53.38036  ? 241  GLY A N   1 
ATOM   1942 C  CA  . GLY A 1 241 ? -12.92800 38.20700 43.01700  1.000 46.72492  ? 241  GLY A CA  1 
ATOM   1943 C  C   . GLY A 1 241 ? -11.94600 38.06500 41.88500  1.000 51.19652  ? 241  GLY A C   1 
ATOM   1944 O  O   . GLY A 1 241 ? -11.55900 39.07900 41.30600  1.000 53.83936  ? 241  GLY A O   1 
ATOM   1945 N  N   . PRO A 1 242 ? -11.51200 36.83500 41.57000  1.000 51.06632  ? 242  PRO A N   1 
ATOM   1946 C  CA  . PRO A 1 242 ? -10.58000 36.61200 40.48500  1.000 44.52387  ? 242  PRO A CA  1 
ATOM   1947 C  C   . PRO A 1 242 ? -11.29100 36.47400 39.13000  1.000 51.85630  ? 242  PRO A C   1 
ATOM   1948 O  O   . PRO A 1 242 ? -10.61500 36.34700 38.14300  1.000 43.20915  ? 242  PRO A O   1 
ATOM   1949 C  CB  . PRO A 1 242 ? -9.98900  35.28100 40.95400  1.000 47.36508  ? 242  PRO A CB  1 
ATOM   1950 C  CG  . PRO A 1 242 ? -11.14900 34.54100 41.54500  1.000 48.52768  ? 242  PRO A CG  1 
ATOM   1951 C  CD  . PRO A 1 242 ? -11.91600 35.61800 42.27100  1.000 52.63107  ? 242  PRO A CD  1 
ATOM   1952 N  N   . CYS A 1 243 ? -12.62200 36.54300 39.13000  1.000 46.43032  ? 243  CYS A N   1 
ATOM   1953 C  CA  . CYS A 1 243 ? -13.37800 36.30700 37.90000  1.000 42.33706  ? 243  CYS A CA  1 
ATOM   1954 C  C   . CYS A 1 243 ? -12.98100 34.97500 37.27100  1.000 50.71972  ? 243  CYS A C   1 
ATOM   1955 O  O   . CYS A 1 243 ? -12.85400 34.85300 36.05100  1.000 43.29462  ? 243  CYS A O   1 
ATOM   1956 C  CB  . CYS A 1 243 ? -13.19300 37.45800 36.90700  1.000 45.30425  ? 243  CYS A CB  1 
ATOM   1957 S  SG  . CYS A 1 243 ? -14.57200 37.71100 35.76900  1.000 44.13194  ? 243  CYS A SG  1 
ATOM   1958 N  N   . ALA A 1 244 ? -12.77700 33.96500 38.11500  1.000 50.54666  ? 244  ALA A N   1 
ATOM   1959 C  CA  . ALA A 1 244 ? -12.23300 32.69900 37.65200  1.000 52.55467  ? 244  ALA A CA  1 
ATOM   1960 C  C   . ALA A 1 244 ? -12.68500 31.56800 38.56200  1.000 46.36738  ? 244  ALA A C   1 
ATOM   1961 O  O   . ALA A 1 244 ? -13.08900 31.78300 39.70800  1.000 49.99960  ? 244  ALA A O   1 
ATOM   1962 C  CB  . ALA A 1 244 ? -10.70100 32.73900 37.59200  1.000 42.32991  ? 244  ALA A CB  1 
ATOM   1963 N  N   . VAL A 1 245 ? -12.61500 30.35600 38.02600  1.000 53.24200  ? 245  VAL A N   1 
ATOM   1964 C  CA  . VAL A 1 245 ? -12.77100 29.13100 38.79600  1.000 46.17346  ? 245  VAL A CA  1 
ATOM   1965 C  C   . VAL A 1 245 ? -11.38000 28.58400 39.07000  1.000 45.44572  ? 245  VAL A C   1 
ATOM   1966 O  O   . VAL A 1 245 ? -10.45900 28.75200 38.26100  1.000 43.52820  ? 245  VAL A O   1 
ATOM   1967 C  CB  . VAL A 1 245 ? -13.65000 28.10400 38.04800  1.000 46.73734  ? 245  VAL A CB  1 
ATOM   1968 C  CG1 . VAL A 1 245 ? -13.84400 26.84100 38.87700  1.000 50.65476  ? 245  VAL A CG1 1 
ATOM   1969 C  CG2 . VAL A 1 245 ? -14.99100 28.71800 37.69700  1.000 41.56585  ? 245  VAL A CG2 1 
ATOM   1970 N  N   . ALA A 1 246 ? -11.21400 27.95100 40.23200  1.000 42.26433  ? 246  ALA A N   1 
ATOM   1971 C  CA  . ALA A 1 246 ? -9.93000  27.37000 40.60000  1.000 42.43179  ? 246  ALA A CA  1 
ATOM   1972 C  C   . ALA A 1 246 ? -9.42700  26.44000 39.50400  1.000 46.59839  ? 246  ALA A C   1 
ATOM   1973 O  O   . ALA A 1 246 ? -10.16400 25.57900 39.01400  1.000 47.82137  ? 246  ALA A O   1 
ATOM   1974 C  CB  . ALA A 1 246 ? -10.05600 26.61200 41.92300  1.000 51.30829  ? 246  ALA A CB  1 
ATOM   1975 N  N   . GLU A 1 247 ? -8.19700  26.66800 39.07100  1.000 42.39033  ? 247  GLU A N   1 
ATOM   1976 C  CA  . GLU A 1 247 ? -7.62300  25.87200 37.96800  1.000 42.26451  ? 247  GLU A CA  1 
ATOM   1977 C  C   . GLU A 1 247 ? -7.74500  24.37400 38.29100  1.000 57.52099  ? 247  GLU A C   1 
ATOM   1978 O  O   . GLU A 1 247 ? -8.13200  23.60800 37.39500  1.000 64.78310  ? 247  GLU A O   1 
ATOM   1979 C  CB  . GLU A 1 247 ? -6.17500  26.25200 37.68500  1.000 42.44858  ? 247  GLU A CB  1 
ATOM   1980 C  CG  . GLU A 1 247 ? -5.55600  25.50000 36.51400  1.000 55.44682  ? 247  GLU A CG  1 
ATOM   1981 C  CD  . GLU A 1 247 ? -4.09900  25.84900 36.28500  1.000 55.16150  ? 247  GLU A CD  1 
ATOM   1982 O  OE1 . GLU A 1 247 ? -3.80300  27.02900 36.04200  1.000 56.64037  ? 247  GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A 1 247 ? -3.25700  24.93900 36.34700  1.000 73.51231  ? 247  GLU A OE2 1 
ATOM   1984 N  N   . LYS A 1 248 ? -7.43100  23.97800 39.52100  1.000 55.29031  ? 248  LYS A N   1 
ATOM   1985 C  CA  . LYS A 1 248 ? -7.55400  22.57000 39.88100  1.000 58.58504  ? 248  LYS A CA  1 
ATOM   1986 C  C   . LYS A 1 248 ? -8.95300  22.05000 39.58100  1.000 48.84594  ? 248  LYS A C   1 
ATOM   1987 O  O   . LYS A 1 248 ? -9.11000  20.96100 39.01800  1.000 50.62937  ? 248  LYS A O   1 
ATOM   1988 C  CB  . LYS A 1 248 ? -7.21100  22.37400 41.35900  1.000 45.77336  ? 248  LYS A CB  1 
ATOM   1989 N  N   . LYS A 1 249 ? -9.98200  22.83000 39.91800  1.000 50.78975  ? 249  LYS A N   1 
ATOM   1990 C  CA  . LYS A 1 249 ? -11.35100 22.39000 39.66900  1.000 45.90073  ? 249  LYS A CA  1 
ATOM   1991 C  C   . LYS A 1 249 ? -11.66700 22.36000 38.17900  1.000 52.98288  ? 249  LYS A C   1 
ATOM   1992 O  O   . LYS A 1 249 ? -12.39000 21.47300 37.71500  1.000 56.01843  ? 249  LYS A O   1 
ATOM   1993 C  CB  . LYS A 1 249 ? -12.33600 23.28600 40.41800  1.000 52.46540  ? 249  LYS A CB  1 
ATOM   1994 C  CG  . LYS A 1 249 ? -12.31000 23.06900 41.92100  1.000 55.46496  ? 249  LYS A CG  1 
ATOM   1995 C  CD  . LYS A 1 249 ? -12.47700 21.59500 42.24800  1.000 49.60226  ? 249  LYS A CD  1 
ATOM   1996 C  CE  . LYS A 1 249 ? -12.03900 21.28800 43.66700  1.000 55.00835  ? 249  LYS A CE  1 
ATOM   1997 N  NZ  . LYS A 1 249 ? -12.06500 19.82300 43.93700  1.000 57.27294  ? 249  LYS A NZ  1 
ATOM   1998 N  N   . ARG A 1 250 ? -11.03600 23.22000 37.40200  1.000 50.14978  ? 250  ARG A N   1 
ATOM   1999 C  CA  . ARG A 1 250 ? -11.37100 23.26200 35.96800  1.000 47.24228  ? 250  ARG A CA  1 
ATOM   2000 C  C   . ARG A 1 250 ? -10.72600 22.02800 35.33100  1.000 52.34433  ? 250  ARG A C   1 
ATOM   2001 O  O   . ARG A 1 250 ? -11.40700 21.32200 34.57800  1.000 46.49721  ? 250  ARG A O   1 
ATOM   2002 C  CB  . ARG A 1 250 ? -10.92600 24.58800 35.33800  1.000 46.80673  ? 250  ARG A CB  1 
ATOM   2003 C  CG  . ARG A 1 250 ? -11.88100 25.74500 35.58500  1.000 45.63191  ? 250  ARG A CG  1 
ATOM   2004 C  CD  . ARG A 1 250 ? -11.36200 27.05700 35.02200  1.000 47.31235  ? 250  ARG A CD  1 
ATOM   2005 N  NE  . ARG A 1 250 ? -10.37300 27.68800 35.90000  1.000 50.77186  ? 250  ARG A NE  1 
ATOM   2006 C  CZ  . ARG A 1 250 ? -9.12000  27.93800 35.56700  1.000 42.37557  ? 250  ARG A CZ  1 
ATOM   2007 N  NH1 . ARG A 1 250 ? -8.62600  27.45500 34.44800  1.000 46.22412  ? 250  ARG A NH1 1 
ATOM   2008 N  NH2 . ARG A 1 250 ? -8.35800  28.65900 36.36400  1.000 42.38828  ? 250  ARG A NH2 1 
ATOM   2009 N  N   . LEU A 1 251 ? -9.45900  21.79300 35.64900  1.000 50.63796  ? 251  LEU A N   1 
ATOM   2010 C  CA  . LEU A 1 251 ? -8.76600  20.60500 35.09800  1.000 44.19863  ? 251  LEU A CA  1 
ATOM   2011 C  C   . LEU A 1 251 ? -9.46300  19.31300 35.58800  1.000 45.75109  ? 251  LEU A C   1 
ATOM   2012 O  O   . LEU A 1 251 ? -9.55700  18.37600 34.79700  1.000 51.66142  ? 251  LEU A O   1 
ATOM   2013 C  CB  . LEU A 1 251 ? -7.27900  20.65700 35.43000  1.000 42.99219  ? 251  LEU A CB  1 
ATOM   2014 C  CG  . LEU A 1 251 ? -6.44300  21.69100 34.67800  1.000 49.40871  ? 251  LEU A CG  1 
ATOM   2015 C  CD1 . LEU A 1 251 ? -5.04500  21.69300 35.25700  1.000 48.10008  ? 251  LEU A CD1 1 
ATOM   2016 C  CD2 . LEU A 1 251 ? -6.40200  21.27900 33.22500  1.000 51.50959  ? 251  LEU A CD2 1 
ATOM   2017 N  N   . GLU A 1 252 ? -9.98600  19.30700 36.80800  1.000 44.68047  ? 252  GLU A N   1 
ATOM   2018 C  CA  A GLU A 1 252 ? -10.71900 18.14700 37.30400  0.358 45.69387  ? 252  GLU A CA  1 
ATOM   2019 C  CA  B GLU A 1 252 ? -10.70400 18.13100 37.28200  0.642 45.80748  ? 252  GLU A CA  1 
ATOM   2020 C  C   . GLU A 1 252 ? -12.02100 17.95200 36.53700  1.000 46.46257  ? 252  GLU A C   1 
ATOM   2021 O  O   . GLU A 1 252 ? -12.40800 16.82100 36.22600  1.000 48.35416  ? 252  GLU A O   1 
ATOM   2022 C  CB  A GLU A 1 252 ? -10.98800 18.31400 38.80000  0.358 46.97003  ? 252  GLU A CB  1 
ATOM   2023 C  CB  B GLU A 1 252 ? -10.92600 18.22300 38.79200  0.642 47.06826  ? 252  GLU A CB  1 
ATOM   2024 C  CG  A GLU A 1 252 ? -11.54200 17.08500 39.49900  0.358 53.37822  ? 252  GLU A CG  1 
ATOM   2025 C  CG  B GLU A 1 252 ? -9.67900  17.88500 39.60200  0.642 50.06445  ? 252  GLU A CG  1 
ATOM   2026 C  CD  A GLU A 1 252 ? -11.83300 17.34300 40.96600  0.358 51.46919  ? 252  GLU A CD  1 
ATOM   2027 C  CD  B GLU A 1 252 ? -9.80200  18.25000 41.06700  0.642 52.02745  ? 252  GLU A CD  1 
ATOM   2028 O  OE1 A GLU A 1 252 ? -11.46600 18.42900 41.46600  0.358 53.28113  ? 252  GLU A OE1 1 
ATOM   2029 O  OE1 B GLU A 1 252 ? -10.89000 18.70000 41.48500  0.642 55.94315  ? 252  GLU A OE1 1 
ATOM   2030 O  OE2 A GLU A 1 252 ? -12.43100 16.46400 41.62100  0.358 49.02739  ? 252  GLU A OE2 1 
ATOM   2031 O  OE2 B GLU A 1 252 ? -8.80500  18.09000 41.80300  0.642 50.83580  ? 252  GLU A OE2 1 
ATOM   2032 N  N   . PHE A 1 253 ? -12.70800 19.05200 36.21700  1.000 50.53429  ? 253  PHE A N   1 
ATOM   2033 C  CA  . PHE A 1 253 ? -13.93200 18.96000 35.43000  1.000 43.24116  ? 253  PHE A CA  1 
ATOM   2034 C  C   . PHE A 1 253 ? -13.64400 18.44700 34.02500  1.000 44.45188  ? 253  PHE A C   1 
ATOM   2035 O  O   . PHE A 1 253 ? -14.36800 17.58800 33.50700  1.000 51.15265  ? 253  PHE A O   1 
ATOM   2036 C  CB  . PHE A 1 253 ? -14.62500 20.32100 35.36200  1.000 40.90362  ? 253  PHE A CB  1 
ATOM   2037 C  CG  . PHE A 1 253 ? -15.49800 20.49100 34.14800  1.000 48.70396  ? 253  PHE A CG  1 
ATOM   2038 C  CD1 . PHE A 1 253 ? -16.74900 19.89800 34.08800  1.000 47.13619  ? 253  PHE A CD1 1 
ATOM   2039 C  CD2 . PHE A 1 253 ? -15.06500 21.23700 33.06100  1.000 41.58864  ? 253  PHE A CD2 1 
ATOM   2040 C  CE1 . PHE A 1 253 ? -17.55300 20.04600 32.97000  1.000 43.25009  ? 253  PHE A CE1 1 
ATOM   2041 C  CE2 . PHE A 1 253 ? -15.86300 21.39000 31.94000  1.000 43.43413  ? 253  PHE A CE2 1 
ATOM   2042 C  CZ  . PHE A 1 253 ? -17.10900 20.79400 31.89600  1.000 48.24638  ? 253  PHE A CZ  1 
ATOM   2043 N  N   . LEU A 1 254 ? -12.60900 18.99000 33.38100  1.000 43.03775  ? 254  LEU A N   1 
ATOM   2044 C  CA  . LEU A 1 254 ? -12.25700 18.53300 32.03900  1.000 40.71161  ? 254  LEU A CA  1 
ATOM   2045 C  C   . LEU A 1 254 ? -11.94000 17.04200 32.04100  1.000 50.05183  ? 254  LEU A C   1 
ATOM   2046 O  O   . LEU A 1 254 ? -12.43400 16.28800 31.19200  1.000 48.64286  ? 254  LEU A O   1 
ATOM   2047 C  CB  . LEU A 1 254 ? -11.07500 19.33800 31.49700  1.000 44.31195  ? 254  LEU A CB  1 
ATOM   2048 C  CG  . LEU A 1 254 ? -11.35500 20.79800 31.13800  1.000 43.13367  ? 254  LEU A CG  1 
ATOM   2049 C  CD1 . LEU A 1 254 ? -10.12900 21.43000 30.50100  1.000 40.90387  ? 254  LEU A CD1 1 
ATOM   2050 C  CD2 . LEU A 1 254 ? -12.55700 20.89900 30.21400  1.000 46.00531  ? 254  LEU A CD2 1 
ATOM   2051 N  N   . ALA A 1 255 ? -11.12800 16.59700 33.00400  1.000 49.85420  ? 255  ALA A N   1 
ATOM   2052 C  CA  . ALA A 1 255 ? -10.77300 15.18400 33.08600  1.000 43.22600  ? 255  ALA A CA  1 
ATOM   2053 C  C   . ALA A 1 255 ? -11.99900 14.31600 33.34700  1.000 46.58881  ? 255  ALA A C   1 
ATOM   2054 O  O   . ALA A 1 255 ? -12.17100 13.26700 32.71200  1.000 42.32063  ? 255  ALA A O   1 
ATOM   2055 C  CB  . ALA A 1 255 ? -9.72200  14.97400 34.17500  1.000 42.88652  ? 255  ALA A CB  1 
ATOM   2056 N  N   . TYR A 1 256 ? -12.87200 14.74300 34.24300  1.000 43.27401  ? 256  TYR A N   1 
ATOM   2057 C  CA  . TYR A 1 256 ? -14.05500 13.92600 34.57300  1.000 40.67835  ? 256  TYR A CA  1 
ATOM   2058 C  C   . TYR A 1 256 ? -14.92300 13.80700 33.33700  1.000 47.00187  ? 256  TYR A C   1 
ATOM   2059 O  O   . TYR A 1 256 ? -15.33200 12.69300 32.99800  1.000 51.03797  ? 256  TYR A O   1 
ATOM   2060 C  CB  . TYR A 1 256 ? -14.84600 14.54400 35.71800  1.000 40.75267  ? 256  TYR A CB  1 
ATOM   2061 C  CG  . TYR A 1 256 ? -15.94100 13.69300 36.34300  1.000 51.25579  ? 256  TYR A CG  1 
ATOM   2062 C  CD1 . TYR A 1 256 ? -15.66500 12.84400 37.40500  1.000 56.46765  ? 256  TYR A CD1 1 
ATOM   2063 C  CD2 . TYR A 1 256 ? -17.25200 13.77000 35.89900  1.000 50.12143  ? 256  TYR A CD2 1 
ATOM   2064 C  CE1 . TYR A 1 256 ? -16.65500 12.07700 37.99200  1.000 53.85333  ? 256  TYR A CE1 1 
ATOM   2065 C  CE2 . TYR A 1 256 ? -18.25300 13.01100 36.48000  1.000 57.09669  ? 256  TYR A CE2 1 
ATOM   2066 C  CZ  . TYR A 1 256 ? -17.95200 12.15800 37.52500  1.000 54.73499  ? 256  TYR A CZ  1 
ATOM   2067 O  OH  . TYR A 1 256 ? -18.92900 11.40700 38.09900  1.000 47.83004  ? 256  TYR A OH  1 
ATOM   2068 N  N   . TYR A 1 257 ? -15.20800 14.93800 32.68300  1.000 54.96675  ? 257  TYR A N   1 
ATOM   2069 C  CA  . TYR A 1 257 ? -16.09800 14.90800 31.52900  1.000 50.42072  ? 257  TYR A CA  1 
ATOM   2070 C  C   . TYR A 1 257 ? -15.51800 14.05000 30.41300  1.000 45.62108  ? 257  TYR A C   1 
ATOM   2071 O  O   . TYR A 1 257 ? -16.23100 13.23700 29.81200  1.000 44.22771  ? 257  TYR A O   1 
ATOM   2072 C  CB  . TYR A 1 257 ? -16.36500 16.33200 31.04100  1.000 46.76084  ? 257  TYR A CB  1 
ATOM   2073 C  CG  . TYR A 1 257 ? -17.41900 16.43200 29.95900  1.000 56.84865  ? 257  TYR A CG  1 
ATOM   2074 C  CD1 . TYR A 1 257 ? -18.57900 15.67100 30.01900  1.000 44.51397  ? 257  TYR A CD1 1 
ATOM   2075 C  CD2 . TYR A 1 257 ? -17.26100 17.30300 28.88800  1.000 50.95345  ? 257  TYR A CD2 1 
ATOM   2076 C  CE1 . TYR A 1 257 ? -19.54500 15.76300 29.03400  1.000 43.69442  ? 257  TYR A CE1 1 
ATOM   2077 C  CE2 . TYR A 1 257 ? -18.22300 17.40300 27.90000  1.000 48.88551  ? 257  TYR A CE2 1 
ATOM   2078 C  CZ  . TYR A 1 257 ? -19.36100 16.62900 27.97700  1.000 50.74088  ? 257  TYR A CZ  1 
ATOM   2079 O  OH  . TYR A 1 257 ? -20.32100 16.72700 26.99700  1.000 47.64858  ? 257  TYR A OH  1 
ATOM   2080 N  N   . PHE A 1 258 ? -14.21700 14.18800 30.14300  1.000 42.63347  ? 258  PHE A N   1 
ATOM   2081 C  CA  . PHE A 1 258 ? -13.61400 13.41100 29.06600  1.000 44.12396  ? 258  PHE A CA  1 
ATOM   2082 C  C   . PHE A 1 258 ? -13.60000 11.92100 29.39400  1.000 49.58143  ? 258  PHE A C   1 
ATOM   2083 O  O   . PHE A 1 258 ? -13.83700 11.08200 28.51400  1.000 51.74168  ? 258  PHE A O   1 
ATOM   2084 C  CB  . PHE A 1 258 ? -12.20100 13.92200 28.78000  1.000 52.17936  ? 258  PHE A CB  1 
ATOM   2085 C  CG  . PHE A 1 258 ? -12.15100 15.35200 28.30400  1.000 58.19540  ? 258  PHE A CG  1 
ATOM   2086 C  CD1 . PHE A 1 258 ? -13.27400 15.96100 27.76500  1.000 55.94248  ? 258  PHE A CD1 1 
ATOM   2087 C  CD2 . PHE A 1 258 ? -10.97900 16.08800 28.39500  1.000 55.62818  ? 258  PHE A CD2 1 
ATOM   2088 C  CE1 . PHE A 1 258 ? -13.23100 17.27400 27.33000  1.000 42.86168  ? 258  PHE A CE1 1 
ATOM   2089 C  CE2 . PHE A 1 258 ? -10.93000 17.40200 27.96000  1.000 40.85050  ? 258  PHE A CE2 1 
ATOM   2090 C  CZ  . PHE A 1 258 ? -12.05800 17.99500 27.42600  1.000 44.75343  ? 258  PHE A CZ  1 
ATOM   2091 N  N   . ASN A 1 259 ? -13.37300 11.59500 30.65800  1.000 50.26123  ? 259  ASN A N   1 
ATOM   2092 C  CA  . ASN A 1 259 ? -13.28600 10.17700 31.07000  1.000 47.31340  ? 259  ASN A CA  1 
ATOM   2093 C  C   . ASN A 1 259 ? -14.69200 9.58400  31.00100  1.000 46.49646  ? 259  ASN A C   1 
ATOM   2094 O  O   . ASN A 1 259 ? -14.83400 8.49300  30.45700  1.000 50.86534  ? 259  ASN A O   1 
ATOM   2095 C  CB  . ASN A 1 259 ? -12.56700 10.03700 32.41900  1.000 48.78517  ? 259  ASN A CB  1 
ATOM   2096 C  CG  . ASN A 1 259 ? -11.08000 10.30100 32.33600  1.000 46.08301  ? 259  ASN A CG  1 
ATOM   2097 O  OD1 . ASN A 1 259 ? -10.47800 10.18000 31.27500  1.000 47.17239  ? 259  ASN A OD1 1 
ATOM   2098 N  ND2 . ASN A 1 259 ? -10.47400 10.64400 33.45800  1.000 42.41845  ? 259  ASN A ND2 1 
ATOM   2099 N  N   . ARG A 1 260 ? -15.68100 10.31000 31.49500  1.000 43.24267  ? 260  ARG A N   1 
ATOM   2100 C  CA  . ARG A 1 260 ? -17.06200 9.81800  31.40900  1.000 40.78882  ? 260  ARG A CA  1 
ATOM   2101 C  C   . ARG A 1 260 ? -17.41600 9.63300  29.91900  1.000 53.47816  ? 260  ARG A C   1 
ATOM   2102 O  O   . ARG A 1 260 ? -18.16300 8.69300  29.61800  1.000 53.08018  ? 260  ARG A O   1 
ATOM   2103 C  CB  . ARG A 1 260 ? -17.96500 10.75400 32.20400  1.000 43.81081  ? 260  ARG A CB  1 
ATOM   2104 C  CG  . ARG A 1 260 ? -17.93100 10.53200 33.70800  1.000 47.28352  ? 260  ARG A CG  1 
ATOM   2105 C  CD  . ARG A 1 260 ? -18.88700 9.42600  34.10000  1.000 53.81234  ? 260  ARG A CD  1 
ATOM   2106 N  NE  . ARG A 1 260 ? -19.14300 9.33800  35.52800  1.000 52.58537  ? 260  ARG A NE  1 
ATOM   2107 C  CZ  . ARG A 1 260 ? -18.52200 8.50500  36.35100  1.000 53.89908  ? 260  ARG A CZ  1 
ATOM   2108 N  NH1 . ARG A 1 260 ? -17.60000 7.68200  35.88500  1.000 59.12500  ? 260  ARG A NH1 1 
ATOM   2109 N  NH2 . ARG A 1 260 ? -18.82900 8.49100  37.63300  1.000 52.76490  ? 260  ARG A NH2 1 
ATOM   2110 N  N   . ALA A 1 261 ? -16.84700 10.44900 29.02000  1.000 55.01831  ? 261  ALA A N   1 
ATOM   2111 C  CA  . ALA A 1 261 ? -17.13800 10.34800 27.57200  1.000 50.44642  ? 261  ALA A CA  1 
ATOM   2112 C  C   . ALA A 1 261 ? -16.51500 9.06700  27.02200  1.000 49.11257  ? 261  ALA A C   1 
ATOM   2113 O  O   . ALA A 1 261 ? -17.15300 8.40900  26.19600  1.000 48.37519  ? 261  ALA A O   1 
ATOM   2114 C  CB  . ALA A 1 261 ? -16.62900 11.55400 26.83000  1.000 39.84702  ? 261  ALA A CB  1 
ATOM   2115 N  N   . VAL A 1 262 ? -15.33400 8.70100  27.51600  1.000 44.23557  ? 262  VAL A N   1 
ATOM   2116 C  CA  . VAL A 1 262 ? -14.64000 7.47700  27.03500  1.000 51.06339  ? 262  VAL A CA  1 
ATOM   2117 C  C   . VAL A 1 262 ? -15.40100 6.25400  27.56500  1.000 51.18193  ? 262  VAL A C   1 
ATOM   2118 O  O   . VAL A 1 262 ? -15.35900 5.22300  26.90700  1.000 46.99564  ? 262  VAL A O   1 
ATOM   2119 C  CB  . VAL A 1 262 ? -13.15000 7.45700  27.41000  1.000 47.38365  ? 262  VAL A CB  1 
ATOM   2120 C  CG1 . VAL A 1 262 ? -12.47800 6.15500  27.02400  1.000 51.17735  ? 262  VAL A CG1 1 
ATOM   2121 C  CG2 . VAL A 1 262 ? -12.39900 8.65100  26.85200  1.000 44.17918  ? 262  VAL A CG2 1 
ATOM   2122 N  N   . GLU A 1 263 ? -16.13800 6.40800  28.64500  1.000 52.20535  ? 263  GLU A N   1 
ATOM   2123 C  CA  . GLU A 1 263 ? -16.93800 5.29500  29.17800  1.000 46.45087  ? 263  GLU A CA  1 
ATOM   2124 C  C   . GLU A 1 263 ? -18.22600 5.18200  28.36700  1.000 44.86490  ? 263  GLU A C   1 
ATOM   2125 O  O   . GLU A 1 263 ? -18.69500 4.06200  28.18700  1.000 57.07562  ? 263  GLU A O   1 
ATOM   2126 C  CB  . GLU A 1 263 ? -17.24300 5.54800  30.65200  1.000 43.08058  ? 263  GLU A CB  1 
ATOM   2127 C  CG  . GLU A 1 263 ? -16.01100 5.76900  31.50200  1.000 40.21664  ? 263  GLU A CG  1 
ATOM   2128 C  CD  . GLU A 1 263 ? -16.33200 6.12500  32.94100  1.000 54.20260  ? 263  GLU A CD  1 
ATOM   2129 O  OE1 . GLU A 1 263 ? -17.52500 6.17000  33.28200  1.000 50.83888  ? 263  GLU A OE1 1 
ATOM   2130 O  OE2 . GLU A 1 263 ? -15.39000 6.36100  33.70800  1.000 46.87629  ? 263  GLU A OE2 1 
ATOM   2131 N  N   . TRP A 1 264 ? -18.77100 6.30800  27.90700  1.000 54.71197  ? 264  TRP A N   1 
ATOM   2132 C  CA  . TRP A 1 264 ? -20.05400 6.30400  27.15600  1.000 48.62133  ? 264  TRP A CA  1 
ATOM   2133 C  C   . TRP A 1 264 ? -19.79300 5.94700  25.70300  1.000 42.20845  ? 264  TRP A C   1 
ATOM   2134 O  O   . TRP A 1 264 ? -20.75400 5.66300  24.99700  1.000 40.88338  ? 264  TRP A O   1 
ATOM   2135 C  CB  . TRP A 1 264 ? -20.69900 7.69300  27.21100  1.000 55.03664  ? 264  TRP A CB  1 
ATOM   2136 C  CG  . TRP A 1 264 ? -20.95700 8.28500  28.56900  1.000 61.42479  ? 264  TRP A CG  1 
ATOM   2137 C  CD1 . TRP A 1 264 ? -21.23500 7.64600  29.74000  1.000 51.23130  ? 264  TRP A CD1 1 
ATOM   2138 C  CD2 . TRP A 1 264 ? -20.99000 9.69600  28.86600  1.000 58.59907  ? 264  TRP A CD2 1 
ATOM   2139 N  NE1 . TRP A 1 264 ? -21.42500 8.55700  30.74300  1.000 49.82690  ? 264  TRP A NE1 1 
ATOM   2140 C  CE2 . TRP A 1 264 ? -21.28400 9.82100  30.23800  1.000 50.59989  ? 264  TRP A CE2 1 
ATOM   2141 C  CE3 . TRP A 1 264 ? -20.79700 10.85500 28.10700  1.000 53.04612  ? 264  TRP A CE3 1 
ATOM   2142 C  CZ2 . TRP A 1 264 ? -21.38800 11.06000 30.86100  1.000 58.82389  ? 264  TRP A CZ2 1 
ATOM   2143 C  CZ3 . TRP A 1 264 ? -20.90200 12.07900 28.72500  1.000 54.77452  ? 264  TRP A CZ3 1 
ATOM   2144 C  CH2 . TRP A 1 264 ? -21.19700 12.17700 30.08200  1.000 55.67135  ? 264  TRP A CH2 1 
ATOM   2145 N  N   . ASN A 1 265 ? -18.53500 5.96800  25.29500  1.000 42.11142  ? 265  ASN A N   1 
ATOM   2146 C  CA  . ASN A 1 265 ? -18.17000 5.76800  23.86100  1.000 44.14085  ? 265  ASN A CA  1 
ATOM   2147 C  C   . ASN A 1 265 ? -18.78700 6.90700  23.03600  1.000 42.94109  ? 265  ASN A C   1 
ATOM   2148 O  O   . ASN A 1 265 ? -19.35900 6.61900  21.97600  1.000 47.96733  ? 265  ASN A O   1 
ATOM   2149 C  CB  . ASN A 1 265 ? -18.51300 4.39200  23.29600  1.000 49.87281  ? 265  ASN A CB  1 
ATOM   2150 C  CG  . ASN A 1 265 ? -17.76000 4.08900  22.02600  1.000 46.48766  ? 265  ASN A CG  1 
ATOM   2151 O  OD1 . ASN A 1 265 ? -16.72700 4.70600  21.75200  1.000 48.42025  ? 265  ASN A OD1 1 
ATOM   2152 N  ND2 . ASN A 1 265 ? -18.26200 3.15100  21.24000  1.000 45.08227  ? 265  ASN A ND2 1 
ATOM   2153 N  N   . LYS A 1 266 ? -18.67700 8.14500  23.51700  1.000 43.50903  ? 266  LYS A N   1 
ATOM   2154 C  CA  . LYS A 1 266 ? -19.23300 9.32200  22.79900  1.000 43.72716  ? 266  LYS A CA  1 
ATOM   2155 C  C   . LYS A 1 266 ? -18.17500 10.42800 22.70900  1.000 39.56801  ? 266  LYS A C   1 
ATOM   2156 O  O   . LYS A 1 266 ? -17.51800 10.68900 23.72000  1.000 53.35888  ? 266  LYS A O   1 
ATOM   2157 C  CB  . LYS A 1 266 ? -20.53000 9.76500  23.47200  1.000 39.51170  ? 266  LYS A CB  1 
ATOM   2158 C  CG  . LYS A 1 266 ? -21.75400 8.94200  23.14400  1.000 59.15674  ? 266  LYS A CG  1 
ATOM   2159 C  CD  . LYS A 1 266 ? -23.02900 9.66400  23.55100  1.000 58.27110  ? 266  LYS A CD  1 
ATOM   2160 C  CE  . LYS A 1 266 ? -22.88500 10.37200 24.85100  1.000 56.37862  ? 266  LYS A CE  1 
ATOM   2161 N  NZ  . LYS A 1 266 ? -24.20100 10.71900 25.38600  1.000 66.61302  ? 266  LYS A NZ  1 
ATOM   2162 N  N   . GLU A 1 267 ? -17.97700 10.98900 21.52300  1.000 47.11329  ? 267  GLU A N   1 
ATOM   2163 C  CA  . GLU A 1 267 ? -17.03100 12.11800 21.37400  1.000 40.60043  ? 267  GLU A CA  1 
ATOM   2164 C  C   . GLU A 1 267 ? -17.77900 13.36500 21.82100  1.000 43.23341  ? 267  GLU A C   1 
ATOM   2165 O  O   . GLU A 1 267 ? -18.77900 13.71300 21.19600  1.000 48.73257  ? 267  GLU A O   1 
ATOM   2166 C  CB  . GLU A 1 267 ? -16.48400 12.20400 19.96300  1.000 43.38376  ? 267  GLU A CB  1 
ATOM   2167 C  CG  . GLU A 1 267 ? -16.24100 10.86800 19.33500  1.000 50.11037  ? 267  GLU A CG  1 
ATOM   2168 C  CD  . GLU A 1 267 ? -16.06400 11.11100 17.85900  1.000 64.75262  ? 267  GLU A CD  1 
ATOM   2169 O  OE1 . GLU A 1 267 ? -17.08000 11.20000 17.15100  1.000 66.32453  ? 267  GLU A OE1 1 
ATOM   2170 O  OE2 . GLU A 1 267 ? -14.91000 11.24600 17.42200  1.000 62.03832  ? 267  GLU A OE2 1 
ATOM   2171 N  N   . VAL A 1 268 ? -17.31500 13.96900 22.90500  1.000 53.05955  ? 268  VAL A N   1 
ATOM   2172 C  CA  . VAL A 1 268 ? -18.07100 15.10700 23.50700  1.000 46.85645  ? 268  VAL A CA  1 
ATOM   2173 C  C   . VAL A 1 268 ? -17.34100 16.43700 23.28000  1.000 48.09424  ? 268  VAL A C   1 
ATOM   2174 O  O   . VAL A 1 268 ? -16.17000 16.41100 22.87500  1.000 40.78109  ? 268  VAL A O   1 
ATOM   2175 C  CB  . VAL A 1 268 ? -18.37000 14.87500 24.99700  1.000 41.38946  ? 268  VAL A CB  1 
ATOM   2176 C  CG1 . VAL A 1 268 ? -19.26000 13.66200 25.22100  1.000 44.59178  ? 268  VAL A CG1 1 
ATOM   2177 C  CG2 . VAL A 1 268 ? -17.09300 14.79600 25.81900  1.000 41.17375  ? 268  VAL A CG2 1 
ATOM   2178 N  N   . VAL A 1 269 ? -18.05500 17.54100 23.50000  1.000 40.98356  ? 269  VAL A N   1 
ATOM   2179 C  CA  . VAL A 1 269 ? -17.50200 18.87300 23.30500  1.000 43.11010  ? 269  VAL A CA  1 
ATOM   2180 C  C   . VAL A 1 269 ? -17.79000 19.70500 24.54500  1.000 39.79822  ? 269  VAL A C   1 
ATOM   2181 O  O   . VAL A 1 269 ? -18.87600 19.61800 25.12600  1.000 42.54816  ? 269  VAL A O   1 
ATOM   2182 C  CB  . VAL A 1 269 ? -18.09500 19.55400 22.05200  1.000 46.55907  ? 269  VAL A CB  1 
ATOM   2183 C  CG1 . VAL A 1 269 ? -17.47100 20.92600 21.83700  1.000 39.71296  ? 269  VAL A CG1 1 
ATOM   2184 C  CG2 . VAL A 1 269 ? -17.91400 18.68000 20.82500  1.000 39.59485  ? 269  VAL A CG2 1 
ATOM   2185 N  N   . THR A 1 270 ? -16.81300 20.50200 24.95900  1.000 39.88858  ? 270  THR A N   1 
ATOM   2186 C  CA  . THR A 1 270 ? -17.03400 21.56000 25.93000  1.000 42.51703  ? 270  THR A CA  1 
ATOM   2187 C  C   . THR A 1 270 ? -16.51200 22.85800 25.33100  1.000 40.01054  ? 270  THR A C   1 
ATOM   2188 O  O   . THR A 1 270 ? -15.61900 22.84700 24.47800  1.000 42.09882  ? 270  THR A O   1 
ATOM   2189 C  CB  . THR A 1 270 ? -16.36200 21.25600 27.28000  1.000 40.11046  ? 270  THR A CB  1 
ATOM   2190 O  OG1 . THR A 1 270 ? -16.81700 22.19200 28.26400  1.000 43.71644  ? 270  THR A OG1 1 
ATOM   2191 C  CG2 . THR A 1 270 ? -14.84700 21.33000 27.16300  1.000 46.91119  ? 270  THR A CG2 1 
ATOM   2192 N  N   . THR A 1 271 ? -17.10300 23.97500 25.74100  1.000 40.03335  ? 271  THR A N   1 
ATOM   2193 C  CA  . THR A 1 271 ? -16.82400 25.26300 25.12600  1.000 44.82691  ? 271  THR A CA  1 
ATOM   2194 C  C   . THR A 1 271 ? -16.38300 26.27100 26.17800  1.000 45.72985  ? 271  THR A C   1 
ATOM   2195 O  O   . THR A 1 271 ? -16.53100 26.06100 27.38500  1.000 43.99227  ? 271  THR A O   1 
ATOM   2196 C  CB  . THR A 1 271 ? -18.04900 25.79800 24.37000  1.000 43.97953  ? 271  THR A CB  1 
ATOM   2197 O  OG1 . THR A 1 271 ? -19.11200 26.04600 25.29600  1.000 39.94815  ? 271  THR A OG1 1 
ATOM   2198 C  CG2 . THR A 1 271 ? -18.52000 24.79200 23.32800  1.000 49.95477  ? 271  THR A CG2 1 
ATOM   2199 N  N   . HIS A 1 272 ? -15.77100 27.33700 25.65800  1.000 49.45152  ? 272  HIS A N   1 
ATOM   2200 C  CA  . HIS A 1 272 ? -15.34300 28.49100 26.48600  1.000 40.44286  ? 272  HIS A CA  1 
ATOM   2201 C  C   . HIS A 1 272 ? -15.45400 29.74200 25.60300  1.000 41.79190  ? 272  HIS A C   1 
ATOM   2202 O  O   . HIS A 1 272 ? -15.04700 29.70900 24.43700  1.000 40.53635  ? 272  HIS A O   1 
ATOM   2203 C  CB  . HIS A 1 272 ? -13.91100 28.30200 26.98000  1.000 40.60174  ? 272  HIS A CB  1 
ATOM   2204 C  CG  . HIS A 1 272 ? -12.83400 28.43000 25.97000  1.000 44.35517  ? 272  HIS A CG  1 
ATOM   2205 N  ND1 . HIS A 1 272 ? -12.13700 29.60300 25.80600  1.000 46.90618  ? 272  HIS A ND1 1 
ATOM   2206 C  CD2 . HIS A 1 272 ? -12.28400 27.55200 25.13700  1.000 47.82820  ? 272  HIS A CD2 1 
ATOM   2207 C  CE1 . HIS A 1 272 ? -11.21800 29.43400 24.87400  1.000 51.22500  ? 272  HIS A CE1 1 
ATOM   2208 N  NE2 . HIS A 1 272 ? -11.29300 28.19700 24.45200  1.000 46.45924  ? 272  HIS A NE2 1 
ATOM   2209 N  N   . LYS A 1 273 ? -15.93200 30.84400 26.17400  1.000 44.27692  ? 273  LYS A N   1 
ATOM   2210 C  CA  . LYS A 1 273 ? -15.94500 32.13300 25.44400  1.000 40.53966  ? 273  LYS A CA  1 
ATOM   2211 C  C   . LYS A 1 273 ? -14.50800 32.46300 25.03500  1.000 43.04057  ? 273  LYS A C   1 
ATOM   2212 O  O   . LYS A 1 273 ? -13.60400 32.20900 25.83100  1.000 41.63945  ? 273  LYS A O   1 
ATOM   2213 C  CB  . LYS A 1 273 ? -16.61800 33.18400 26.32200  1.000 40.60267  ? 273  LYS A CB  1 
ATOM   2214 C  CG  . LYS A 1 273 ? -18.09500 33.00200 26.57700  1.000 41.47087  ? 273  LYS A CG  1 
ATOM   2215 C  CD  . LYS A 1 273 ? -18.88500 33.21600 25.29700  1.000 41.87521  ? 273  LYS A CD  1 
ATOM   2216 C  CE  . LYS A 1 273 ? -20.33600 33.04400 25.53200  1.000 44.61347  ? 273  LYS A CE  1 
ATOM   2217 N  NZ  . LYS A 1 273 ? -20.78500 33.79100 26.70400  1.000 43.66810  ? 273  LYS A NZ  1 
ATOM   2218 N  N   . HIS A 1 274 ? -14.31600 32.98600 23.82800  1.000 45.74952  ? 274  HIS A N   1 
ATOM   2219 C  CA  . HIS A 1 274 ? -12.95800 33.27200 23.28800  1.000 50.88123  ? 274  HIS A CA  1 
ATOM   2220 C  C   . HIS A 1 274 ? -12.14500 34.14300 24.24300  1.000 48.85672  ? 274  HIS A C   1 
ATOM   2221 O  O   . HIS A 1 274 ? -10.92000 34.08600 24.17600  1.000 56.71638  ? 274  HIS A O   1 
ATOM   2222 C  CB  . HIS A 1 274 ? -13.06500 33.93900 21.91700  1.000 47.66346  ? 274  HIS A CB  1 
ATOM   2223 C  CG  . HIS A 1 274 ? -11.77500 34.10100 21.19400  1.000 61.36021  ? 274  HIS A CG  1 
ATOM   2224 N  ND1 . HIS A 1 274 ? -10.85000 33.08600 21.09700  1.000 75.97575  ? 274  HIS A ND1 1 
ATOM   2225 C  CD2 . HIS A 1 274 ? -11.26100 35.14900 20.51900  1.000 57.52732  ? 274  HIS A CD2 1 
ATOM   2226 C  CE1 . HIS A 1 274 ? -9.81600  33.50400 20.39900  1.000 79.28618  ? 274  HIS A CE1 1 
ATOM   2227 N  NE2 . HIS A 1 274 ? -10.04500 34.76600 20.03100  1.000 67.63710  ? 274  HIS A NE2 1 
ATOM   2228 N  N   . PHE A 1 275 ? -12.81800 34.93600 25.06700  1.000 51.76071  ? 275  PHE A N   1 
ATOM   2229 C  CA  . PHE A 1 275 ? -12.11600 35.82500 26.03100  1.000 58.35599  ? 275  PHE A CA  1 
ATOM   2230 C  C   . PHE A 1 275 ? -11.67400 34.98500 27.24400  1.000 55.08514  ? 275  PHE A C   1 
ATOM   2231 O  O   . PHE A 1 275 ? -10.50900 35.11000 27.62500  1.000 68.47637  ? 275  PHE A O   1 
ATOM   2232 C  CB  . PHE A 1 275 ? -12.97500 37.06100 26.32500  1.000 45.34070  ? 275  PHE A CB  1 
ATOM   2233 C  CG  . PHE A 1 275 ? -14.38500 36.89000 26.85800  1.000 44.24588  ? 275  PHE A CG  1 
ATOM   2234 C  CD1 . PHE A 1 275 ? -15.46000 36.78600 25.99100  1.000 42.81833  ? 275  PHE A CD1 1 
ATOM   2235 C  CD2 . PHE A 1 275 ? -14.63300 36.88800 28.22200  1.000 54.74868  ? 275  PHE A CD2 1 
ATOM   2236 C  CE1 . PHE A 1 275 ? -16.74300 36.65400 26.48200  1.000 51.12027  ? 275  PHE A CE1 1 
ATOM   2237 C  CE2 . PHE A 1 275 ? -15.92200 36.76000 28.70300  1.000 57.16147  ? 275  PHE A CE2 1 
ATOM   2238 C  CZ  . PHE A 1 275 ? -16.97300 36.64100 27.83200  1.000 45.72582  ? 275  PHE A CZ  1 
ATOM   2239 N  N   . ASP A 1 276 ? -12.55800 34.14500 27.78700  1.000 50.50104  ? 276  ASP A N   1 
ATOM   2240 C  CA  . ASP A 1 276 ? -12.20200 33.25100 28.92200  1.000 44.38126  ? 276  ASP A CA  1 
ATOM   2241 C  C   . ASP A 1 276 ? -11.05300 32.34200 28.51700  1.000 50.02386  ? 276  ASP A C   1 
ATOM   2242 O  O   . ASP A 1 276 ? -11.19400 31.62900 27.53600  1.000 53.62305  ? 276  ASP A O   1 
ATOM   2243 C  CB  . ASP A 1 276 ? -13.40800 32.48400 29.44400  1.000 43.27499  ? 276  ASP A CB  1 
ATOM   2244 C  CG  . ASP A 1 276 ? -13.40500 32.32700 30.94100  1.000 41.23957  ? 276  ASP A CG  1 
ATOM   2245 O  OD1 . ASP A 1 276 ? -12.31600 32.15100 31.48200  1.000 53.54661  ? 276  ASP A OD1 1 
ATOM   2246 O  OD2 . ASP A 1 276 ? -14.48800 32.38000 31.53200  1.000 49.46513  ? 276  ASP A OD2 1 
ATOM   2247 N  N   . VAL A 1 277 ? -9.94400  32.42800 29.24800  1.000 53.19301  ? 277  VAL A N   1 
ATOM   2248 C  CA  . VAL A 1 277 ? -8.74900  31.58400 28.96300  1.000 49.75340  ? 277  VAL A CA  1 
ATOM   2249 C  C   . VAL A 1 277 ? -8.75200  30.41900 29.96100  1.000 44.04994  ? 277  VAL A C   1 
ATOM   2250 O  O   . VAL A 1 277 ? -7.74300  29.72500 30.05800  1.000 47.23207  ? 277  VAL A O   1 
ATOM   2251 C  CB  . VAL A 1 277 ? -7.48300  32.45000 29.03800  1.000 41.81286  ? 277  VAL A CB  1 
ATOM   2252 C  CG1 . VAL A 1 277 ? -7.43100  33.47200 27.91200  1.000 41.81147  ? 277  VAL A CG1 1 
ATOM   2253 C  CG2 . VAL A 1 277 ? -7.32700  33.11700 30.39600  1.000 42.01258  ? 277  VAL A CG2 1 
ATOM   2254 N  N   . GLY A 1 278 ? -9.85700  30.24000 30.66800  1.000 43.36257  ? 278  GLY A N   1 
ATOM   2255 C  CA  . GLY A 1 278 ? -9.99500  29.11800 31.61000  1.000 42.01788  ? 278  GLY A CA  1 
ATOM   2256 C  C   . GLY A 1 278 ? -9.64600  27.79500 30.96500  1.000 49.16680  ? 278  GLY A C   1 
ATOM   2257 O  O   . GLY A 1 278 ? -8.98400  26.98300 31.61900  1.000 51.43660  ? 278  GLY A O   1 
ATOM   2258 N  N   . PHE A 1 279 ? -10.06500 27.59200 29.72100  1.000 41.18639  ? 279  PHE A N   1 
ATOM   2259 C  CA  . PHE A 1 279 ? -9.72100  26.35200 28.99200  1.000 45.32886  ? 279  PHE A CA  1 
ATOM   2260 C  C   . PHE A 1 279 ? -8.88400  26.72000 27.78300  1.000 46.16632  ? 279  PHE A C   1 
ATOM   2261 O  O   . PHE A 1 279 ? -8.93900  27.87800 27.37000  1.000 53.60666  ? 279  PHE A O   1 
ATOM   2262 C  CB  . PHE A 1 279 ? -10.98100 25.60900 28.54500  1.000 44.52548  ? 279  PHE A CB  1 
ATOM   2263 C  CG  . PHE A 1 279 ? -11.95400 25.19900 29.62000  1.000 46.97188  ? 279  PHE A CG  1 
ATOM   2264 C  CD1 . PHE A 1 279 ? -11.51600 24.78100 30.86400  1.000 40.95860  ? 279  PHE A CD1 1 
ATOM   2265 C  CD2 . PHE A 1 279 ? -13.31400 25.19400 29.36600  1.000 41.72662  ? 279  PHE A CD2 1 
ATOM   2266 C  CE1 . PHE A 1 279 ? -12.42200 24.40000 31.83900  1.000 42.44908  ? 279  PHE A CE1 1 
ATOM   2267 C  CE2 . PHE A 1 279 ? -14.21700 24.80400 30.34000  1.000 40.64587  ? 279  PHE A CE2 1 
ATOM   2268 C  CZ  . PHE A 1 279 ? -13.76900 24.41200 31.57600  1.000 40.77835  ? 279  PHE A CZ  1 
ATOM   2269 N  N   . ARG A 1 280 ? -8.17100  25.76200 27.19800  1.000 52.76631  ? 280  ARG A N   1 
ATOM   2270 C  CA  A ARG A 1 280 ? -7.47100  25.97700 25.91800  0.580 49.62807  ? 280  ARG A CA  1 
ATOM   2271 C  CA  B ARG A 1 280 ? -7.41300  26.02600 25.94200  0.420 49.75351  ? 280  ARG A CA  1 
ATOM   2272 C  C   . ARG A 1 280 ? -8.07200  25.36400 24.69200  1.000 47.72752  ? 280  ARG A C   1 
ATOM   2273 O  O   . ARG A 1 280 ? -9.02400  24.53200 24.79600  1.000 48.23711  ? 280  ARG A O   1 
ATOM   2274 C  CB  A ARG A 1 280 ? -6.04800  25.43900 26.09200  0.580 52.26987  ? 280  ARG A CB  1 
ATOM   2275 C  CB  B ARG A 1 280 ? -5.95200  25.62500 26.18400  0.420 52.10237  ? 280  ARG A CB  1 
ATOM   2276 C  CG  A ARG A 1 280 ? -5.40700  25.81000 27.42000  0.580 53.27047  ? 280  ARG A CG  1 
ATOM   2277 C  CG  B ARG A 1 280 ? -5.40900  26.11500 27.52300  0.420 53.31407  ? 280  ARG A CG  1 
ATOM   2278 C  CD  A ARG A 1 280 ? -4.03300  25.19300 27.60300  0.580 60.01194  ? 280  ARG A CD  1 
ATOM   2279 C  CD  B ARG A 1 280 ? -3.90700  26.03000 27.74300  0.420 59.68058  ? 280  ARG A CD  1 
ATOM   2280 N  NE  A ARG A 1 280 ? -3.53500  25.38000 28.95800  0.580 64.92785  ? 280  ARG A NE  1 
ATOM   2281 N  NE  B ARG A 1 280 ? -3.24400  24.74700 27.56300  0.420 59.82813  ? 280  ARG A NE  1 
ATOM   2282 C  CZ  A ARG A 1 280 ? -2.82200  26.42300 29.36500  0.580 58.78150  ? 280  ARG A CZ  1 
ATOM   2283 C  CZ  B ARG A 1 280 ? -1.92800  24.58500 27.61600  0.420 57.36695  ? 280  ARG A CZ  1 
ATOM   2284 N  NH1 A ARG A 1 280 ? -2.51500  27.38800 28.51600  0.580 62.85028  ? 280  ARG A NH1 1 
ATOM   2285 N  NH1 B ARG A 1 280 ? -1.14500  25.61900 27.86800  0.420 66.23784  ? 280  ARG A NH1 1 
ATOM   2286 N  NH2 A ARG A 1 280 ? -2.41900  26.49700 30.62100  0.580 50.45504  ? 280  ARG A NH2 1 
ATOM   2287 N  NH2 B ARG A 1 280 ? -1.39500  23.40300 27.36900  0.420 45.20371  ? 280  ARG A NH2 1 
ATOM   2288 N  N   . ASP A 1 281 ? -7.77500  25.89900 23.50400  1.000 50.13892  ? 281  ASP A N   1 
ATOM   2289 C  CA  . ASP A 1 281 ? -8.37800  25.39500 22.24200  1.000 43.27628  ? 281  ASP A CA  1 
ATOM   2290 C  C   . ASP A 1 281 ? -7.73400  24.05700 21.88100  1.000 53.39431  ? 281  ASP A C   1 
ATOM   2291 O  O   . ASP A 1 281 ? -8.02900  23.53500 20.79300  1.000 54.50570  ? 281  ASP A O   1 
ATOM   2292 C  CB  . ASP A 1 281 ? -8.25900  26.43500 21.12700  1.000 44.10697  ? 281  ASP A CB  1 
ATOM   2293 C  CG  . ASP A 1 281 ? -9.14200  27.64700 21.35200  1.000 52.99621  ? 281  ASP A CG  1 
ATOM   2294 O  OD1 . ASP A 1 281 ? -9.97900  27.59100 22.26800  1.000 45.56574  ? 281  ASP A OD1 1 
ATOM   2295 O  OD2 . ASP A 1 281 ? -8.98200  28.63500 20.61100  1.000 57.11168  ? 281  ASP A OD2 1 
ATOM   2296 N  N   . THR A 1 282 ? -6.87600  23.53800 22.75900  1.000 46.69461  ? 282  THR A N   1 
ATOM   2297 C  CA  . THR A 1 282 ? -6.29400  22.19700 22.50900  1.000 47.60765  ? 282  THR A CA  1 
ATOM   2298 C  C   . THR A 1 282 ? -7.39300  21.13900 22.64000  1.000 48.29814  ? 282  THR A C   1 
ATOM   2299 O  O   . THR A 1 282 ? -7.38300  20.18400 21.85400  1.000 48.20610  ? 282  THR A O   1 
ATOM   2300 C  CB  . THR A 1 282 ? -5.13400  21.95600 23.48200  1.000 42.58070  ? 282  THR A CB  1 
ATOM   2301 O  OG1 . THR A 1 282 ? -5.65800  22.08600 24.80300  1.000 50.54173  ? 282  THR A OG1 1 
ATOM   2302 C  CG2 . THR A 1 282 ? -3.98800  22.92200 23.28700  1.000 41.21253  ? 282  THR A CG2 1 
ATOM   2303 N  N   . SER A 1 283 ? -8.28300  21.30500 23.61500  1.000 45.35486  ? 283  SER A N   1 
ATOM   2304 C  CA  . SER A 1 283 ? -9.33900  20.30100 23.87800  1.000 43.53437  ? 283  SER A CA  1 
ATOM   2305 C  C   . SER A 1 283 ? -10.70500 20.97700 23.94900  1.000 46.42328  ? 283  SER A C   1 
ATOM   2306 O  O   . SER A 1 283 ? -11.71400 20.25700 24.01700  1.000 52.45863  ? 283  SER A O   1 
ATOM   2307 C  CB  . SER A 1 283 ? -9.04600  19.61100 25.17200  1.000 45.95941  ? 283  SER A CB  1 
ATOM   2308 O  OG  . SER A 1 283 ? -9.05100  20.53800 26.24600  1.000 43.86590  ? 283  SER A OG  1 
ATOM   2309 N  N   . THR A 1 284 ? -10.73800 22.30300 23.94800  1.000 44.79997  ? 284  THR A N   1 
ATOM   2310 C  CA  . THR A 1 284 ? -12.02800 23.01000 24.13200  1.000 40.33496  ? 284  THR A CA  1 
ATOM   2311 C  C   . THR A 1 284 ? -12.32400 23.89000 22.91300  1.000 41.78615  ? 284  THR A C   1 
ATOM   2312 O  O   . THR A 1 284 ? -11.39200 24.15200 22.14500  1.000 40.35362  ? 284  THR A O   1 
ATOM   2313 C  CB  . THR A 1 284 ? -12.00500 23.76400 25.46200  1.000 52.42801  ? 284  THR A CB  1 
ATOM   2314 O  OG1 . THR A 1 284 ? -11.65500 22.81800 26.46400  1.000 51.69244  ? 284  THR A OG1 1 
ATOM   2315 C  CG2 . THR A 1 284 ? -13.31400 24.44300 25.79900  1.000 60.36383  ? 284  THR A CG2 1 
ATOM   2316 N  N   . VAL A 1 285 ? -13.57700 24.30500 22.75100  1.000 39.85885  ? 285  VAL A N   1 
ATOM   2317 C  CA  . VAL A 1 285 ? -14.00300 25.08200 21.59200  1.000 48.56785  ? 285  VAL A CA  1 
ATOM   2318 C  C   . VAL A 1 285 ? -14.18500 26.54100 21.99200  1.000 42.11068  ? 285  VAL A C   1 
ATOM   2319 O  O   . VAL A 1 285 ? -14.90000 26.85000 22.95700  1.000 40.21998  ? 285  VAL A O   1 
ATOM   2320 C  CB  . VAL A 1 285 ? -15.29600 24.51200 20.98600  1.000 44.88238  ? 285  VAL A CB  1 
ATOM   2321 C  CG1 . VAL A 1 285 ? -15.83900 25.44800 19.91900  1.000 51.27238  ? 285  VAL A CG1 1 
ATOM   2322 C  CG2 . VAL A 1 285 ? -15.03200 23.13700 20.39600  1.000 43.56100  ? 285  VAL A CG2 1 
ATOM   2323 N  N   . SER A 1 286 ? -13.54500 27.43900 21.25300  1.000 42.44697  ? 286  SER A N   1 
ATOM   2324 C  CA  . SER A 1 286 ? -13.71400 28.90100 21.49100  1.000 50.16257  ? 286  SER A CA  1 
ATOM   2325 C  C   . SER A 1 286 ? -15.08400 29.38400 20.99100  1.000 40.86915  ? 286  SER A C   1 
ATOM   2326 O  O   . SER A 1 286 ? -15.36500 29.23400 19.80400  1.000 40.95308  ? 286  SER A O   1 
ATOM   2327 C  CB  . SER A 1 286 ? -12.58500 29.70400 20.89800  1.000 43.84722  ? 286  SER A CB  1 
ATOM   2328 O  OG  . SER A 1 286 ? -11.45100 29.72200 21.74600  1.000 51.82416  ? 286  SER A OG  1 
ATOM   2329 N  N   . ASP A 1 287 ? -15.87300 29.96900 21.87700  1.000 37.97771  ? 287  ASP A N   1 
ATOM   2330 C  CA  . ASP A 1 287 ? -17.22700 30.44000 21.51900  1.000 31.85623  ? 287  ASP A CA  1 
ATOM   2331 C  C   . ASP A 1 287 ? -17.23700 31.96200 21.36800  1.000 38.90907  ? 287  ASP A C   1 
ATOM   2332 O  O   . ASP A 1 287 ? -16.82200 32.64800 22.30900  1.000 45.96319  ? 287  ASP A O   1 
ATOM   2333 C  CB  . ASP A 1 287 ? -18.25000 30.01200 22.54600  1.000 32.28592  ? 287  ASP A CB  1 
ATOM   2334 C  CG  . ASP A 1 287 ? -19.67100 30.49500 22.32900  1.000 39.83100  ? 287  ASP A CG  1 
ATOM   2335 O  OD1 . ASP A 1 287 ? -19.87000 31.71700 22.29200  1.000 42.20917  ? 287  ASP A OD1 1 
ATOM   2336 O  OD2 . ASP A 1 287 ? -20.56300 29.63700 22.22700  1.000 51.28545  ? 287  ASP A OD2 1 
ATOM   2337 N  N   . TYR A 1 288 ? -17.70500 32.44500 20.22700  1.000 39.42902  ? 288  TYR A N   1 
ATOM   2338 C  CA  . TYR A 1 288 ? -17.85000 33.89900 19.98300  1.000 38.25587  ? 288  TYR A CA  1 
ATOM   2339 C  C   . TYR A 1 288 ? -19.31500 34.26100 20.24800  1.000 38.96800  ? 288  TYR A C   1 
ATOM   2340 O  O   . TYR A 1 288 ? -20.18600 33.63000 19.64700  1.000 37.38155  ? 288  TYR A O   1 
ATOM   2341 C  CB  . TYR A 1 288 ? -17.36800 34.20000 18.56800  1.000 36.58549  ? 288  TYR A CB  1 
ATOM   2342 C  CG  . TYR A 1 288 ? -15.90900 34.01100 18.25600  1.000 36.80923  ? 288  TYR A CG  1 
ATOM   2343 C  CD1 . TYR A 1 288 ? -15.41200 32.78100 17.86700  1.000 39.01615  ? 288  TYR A CD1 1 
ATOM   2344 C  CD2 . TYR A 1 288 ? -15.03700 35.08300 18.27400  1.000 49.51082  ? 288  TYR A CD2 1 
ATOM   2345 C  CE1 . TYR A 1 288 ? -14.07700 32.61300 17.54800  1.000 45.39929  ? 288  TYR A CE1 1 
ATOM   2346 C  CE2 . TYR A 1 288 ? -13.69900 34.93400 17.96100  1.000 51.64338  ? 288  TYR A CE2 1 
ATOM   2347 C  CZ  . TYR A 1 288 ? -13.21700 33.69300 17.59600  1.000 49.48359  ? 288  TYR A CZ  1 
ATOM   2348 O  OH  . TYR A 1 288 ? -11.90000 33.54400 17.28200  1.000 57.92757  ? 288  TYR A OH  1 
ATOM   2349 N  N   . GLU A 1 289 ? -19.53200 35.21900 21.13900  1.000 36.81320  ? 289  GLU A N   1 
ATOM   2350 C  CA  . GLU A 1 289 ? -20.91000 35.59600 21.51900  1.000 40.97756  ? 289  GLU A CA  1 
ATOM   2351 C  C   . GLU A 1 289 ? -21.43800 36.67600 20.57800  1.000 47.03031  ? 289  GLU A C   1 
ATOM   2352 O  O   . GLU A 1 289 ? -20.68500 37.59400 20.26100  1.000 47.57233  ? 289  GLU A O   1 
ATOM   2353 C  CB  . GLU A 1 289 ? -21.00700 36.09100 22.95700  1.000 41.04053  ? 289  GLU A CB  1 
ATOM   2354 C  CG  . GLU A 1 289 ? -22.42000 36.46400 23.39500  1.000 49.49015  ? 289  GLU A CG  1 
ATOM   2355 C  CD  . GLU A 1 289 ? -22.54200 36.82200 24.86400  1.000 44.64504  ? 289  GLU A CD  1 
ATOM   2356 O  OE1 . GLU A 1 289 ? -21.54100 36.65700 25.57400  1.000 47.46162  ? 289  GLU A OE1 1 
ATOM   2357 O  OE2 . GLU A 1 289 ? -23.61200 37.28500 25.29800  1.000 44.17578  ? 289  GLU A OE2 1 
ATOM   2358 N  N   . ARG A 1 290 ? -22.69200 36.53800 20.16600  1.000 42.55292  ? 290  ARG A N   1 
ATOM   2359 C  CA  . ARG A 1 290 ? -23.35000 37.56300 19.33100  1.000 35.81373  ? 290  ARG A CA  1 
ATOM   2360 C  C   . ARG A 1 290 ? -22.36600 38.05300 18.27000  1.000 44.10347  ? 290  ARG A C   1 
ATOM   2361 O  O   . ARG A 1 290 ? -22.21800 39.26100 18.12200  1.000 46.36489  ? 290  ARG A O   1 
ATOM   2362 C  CB  . ARG A 1 290 ? -23.94000 38.61500 20.26600  1.000 31.79771  ? 290  ARG A CB  1 
ATOM   2363 C  CG  . ARG A 1 290 ? -24.97700 38.08100 21.24000  1.000 40.16373  ? 290  ARG A CG  1 
ATOM   2364 C  CD  . ARG A 1 290 ? -25.67600 39.22500 21.93800  1.000 40.43458  ? 290  ARG A CD  1 
ATOM   2365 N  NE  . ARG A 1 290 ? -26.73300 38.82300 22.84700  1.000 38.59882  ? 290  ARG A NE  1 
ATOM   2366 C  CZ  . ARG A 1 290 ? -28.02000 38.80200 22.53400  1.000 42.58466  ? 290  ARG A CZ  1 
ATOM   2367 N  NH1 . ARG A 1 290 ? -28.40600 39.14600 21.32000  1.000 32.05357  ? 290  ARG A NH1 1 
ATOM   2368 N  NH2 . ARG A 1 290 ? -28.91400 38.42700 23.42900  1.000 43.82943  ? 290  ARG A NH2 1 
ATOM   2369 N  N   . GLY A 1 291 ? -21.74200 37.12700 17.55400  1.000 32.66012  ? 291  GLY A N   1 
ATOM   2370 C  CA  . GLY A 1 291 ? -20.84200 37.51500 16.46700  1.000 32.54156  ? 291  GLY A CA  1 
ATOM   2371 C  C   . GLY A 1 291 ? -19.91200 36.41400 16.03800  1.000 38.60444  ? 291  GLY A C   1 
ATOM   2372 O  O   . GLY A 1 291 ? -20.16500 35.26900 16.38200  1.000 42.23391  ? 291  GLY A O   1 
ATOM   2373 N  N   . GLY A 1 292 ? -18.88300 36.77300 15.28900  1.000 38.35239  ? 292  GLY A N   1 
ATOM   2374 C  CA  . GLY A 1 292 ? -17.90900 35.79100 14.82300  1.000 38.33202  ? 292  GLY A CA  1 
ATOM   2375 C  C   . GLY A 1 292 ? -16.74100 36.43000 14.12900  1.000 42.86620  ? 292  GLY A C   1 
ATOM   2376 O  O   . GLY A 1 292 ? -16.80300 37.61300 13.83000  1.000 43.48528  ? 292  GLY A O   1 
ATOM   2377 N  N   . PRO A 1 293 ? -15.66800 35.65500 13.89400  1.000 44.43534  ? 293  PRO A N   1 
ATOM   2378 C  CA  . PRO A 1 293 ? -14.51300 36.13900 13.17900  1.000 44.88337  ? 293  PRO A CA  1 
ATOM   2379 C  C   . PRO A 1 293 ? -14.85500 36.81400 11.84700  1.000 51.57852  ? 293  PRO A C   1 
ATOM   2380 O  O   . PRO A 1 293 ? -15.90200 36.56000 11.32000  1.000 55.50444  ? 293  PRO A O   1 
ATOM   2381 C  CB  . PRO A 1 293 ? -13.72200 34.85800 12.88700  1.000 42.99271  ? 293  PRO A CB  1 
ATOM   2382 C  CG  . PRO A 1 293 ? -14.65100 33.72100 13.19900  1.000 42.69789  ? 293  PRO A CG  1 
ATOM   2383 C  CD  . PRO A 1 293 ? -15.50300 34.26300 14.31700  1.000 39.86994  ? 293  PRO A CD  1 
ATOM   2384 N  N   . ALA A 1 294 ? -13.94000 37.62800 11.33900  1.000 41.18328  ? 294  ALA A N   1 
ATOM   2385 C  CA  . ALA A 1 294 ? -14.16200 38.34100 10.07300  1.000 46.19430  ? 294  ALA A CA  1 
ATOM   2386 C  C   . ALA A 1 294 ? -13.50300 37.56900 8.94000   1.000 50.24236  ? 294  ALA A C   1 
ATOM   2387 O  O   . ALA A 1 294 ? -13.89100 37.76900 7.79100   1.000 57.45404  ? 294  ALA A O   1 
ATOM   2388 C  CB  . ALA A 1 294 ? -13.58600 39.71900 10.19000  1.000 39.83784  ? 294  ALA A CB  1 
ATOM   2389 N  N   . ASN A 1 295 ? -12.50600 36.75900 9.26100   1.000 50.25552  ? 295  ASN A N   1 
ATOM   2390 C  CA  . ASN A 1 295 ? -11.88800 35.89900 8.22700   1.000 57.64821  ? 295  ASN A CA  1 
ATOM   2391 C  C   . ASN A 1 295 ? -12.01000 34.43800 8.66000   1.000 54.37917  ? 295  ASN A C   1 
ATOM   2392 O  O   . ASN A 1 295 ? -12.65800 34.17700 9.67300   1.000 53.31370  ? 295  ASN A O   1 
ATOM   2393 C  CB  . ASN A 1 295 ? -10.43200 36.27000 7.95300   1.000 67.41242  ? 295  ASN A CB  1 
ATOM   2394 C  CG  . ASN A 1 295 ? -10.20200 37.72400 7.60500   1.000 84.61489  ? 295  ASN A CG  1 
ATOM   2395 O  OD1 . ASN A 1 295 ? -10.42500 38.60500 8.43000   1.000 84.51631  ? 295  ASN A OD1 1 
ATOM   2396 N  ND2 . ASN A 1 295 ? -9.73800  37.98200 6.39100   1.000 97.31247  ? 295  ASN A ND2 1 
ATOM   2397 N  N   . ILE A 1 296 ? -11.39600 33.53700 7.90600   1.000 51.37928  ? 296  ILE A N   1 
ATOM   2398 C  CA  . ILE A 1 296 ? -11.42100 32.09200 8.25800   1.000 43.65834  ? 296  ILE A CA  1 
ATOM   2399 C  C   . ILE A 1 296 ? -10.55200 31.88700 9.50100   1.000 55.16882  ? 296  ILE A C   1 
ATOM   2400 O  O   . ILE A 1 296 ? -9.36000  32.20800 9.45300   1.000 54.68247  ? 296  ILE A O   1 
ATOM   2401 C  CB  . ILE A 1 296 ? -10.96100 31.24200 7.06800   1.000 43.34179  ? 296  ILE A CB  1 
ATOM   2402 C  CG1 . ILE A 1 296 ? -11.83700 31.50800 5.85300   1.000 44.85374  ? 296  ILE A CG1 1 
ATOM   2403 C  CG2 . ILE A 1 296 ? -10.93100 29.76000 7.43400   1.000 44.70922  ? 296  ILE A CG2 1 
ATOM   2404 C  CD1 . ILE A 1 296 ? -11.43800 30.72400 4.62200   1.000 44.58404  ? 296  ILE A CD1 1 
ATOM   2405 N  N   . THR A 1 297 ? -11.17800 31.39600 10.56100  1.000 55.12978  ? 297  THR A N   1 
ATOM   2406 C  CA  . THR A 1 297 ? -10.48700 31.20200 11.84700  1.000 43.16683  ? 297  THR A CA  1 
ATOM   2407 C  C   . THR A 1 297 ? -10.34500 29.71400 12.12700  1.000 49.01449  ? 297  THR A C   1 
ATOM   2408 O  O   . THR A 1 297 ? -11.36200 29.01400 12.17000  1.000 43.69612  ? 297  THR A O   1 
ATOM   2409 C  CB  . THR A 1 297 ? -11.24200 31.92600 12.96100  1.000 45.95247  ? 297  THR A CB  1 
ATOM   2410 O  OG1 . THR A 1 297 ? -11.09300 33.32200 12.71100  1.000 56.36013  ? 297  THR A OG1 1 
ATOM   2411 C  CG2 . THR A 1 297 ? -10.73100 31.59000 14.34300  1.000 46.75160  ? 297  THR A CG2 1 
ATOM   2412 N  N   . ARG A 1 298 ? -9.10500  29.28100 12.28400  1.000 50.89355  ? 298  ARG A N   1 
ATOM   2413 C  CA  . ARG A 1 298 ? -8.80900  27.87500 12.61100  1.000 54.76439  ? 298  ARG A CA  1 
ATOM   2414 C  C   . ARG A 1 298 ? -7.91600  27.88500 13.85800  1.000 58.77008  ? 298  ARG A C   1 
ATOM   2415 O  O   . ARG A 1 298 ? -6.89600  28.57900 13.84700  1.000 59.31472  ? 298  ARG A O   1 
ATOM   2416 C  CB  . ARG A 1 298 ? -8.08100  27.22700 11.43600  1.000 52.69166  ? 298  ARG A CB  1 
ATOM   2417 C  CG  . ARG A 1 298 ? -8.74300  27.38200 10.07800  1.000 54.95160  ? 298  ARG A CG  1 
ATOM   2418 C  CD  . ARG A 1 298 ? -7.87200  26.68900 9.04900   1.000 52.49098  ? 298  ARG A CD  1 
ATOM   2419 N  NE  . ARG A 1 298 ? -8.50700  26.57800 7.74900   1.000 51.79189  ? 298  ARG A NE  1 
ATOM   2420 C  CZ  . ARG A 1 298 ? -9.50600  25.75400 7.46900   1.000 56.96637  ? 298  ARG A CZ  1 
ATOM   2421 N  NH1 . ARG A 1 298 ? -9.99200  24.95600 8.40200   1.000 52.49183  ? 298  ARG A NH1 1 
ATOM   2422 N  NH2 . ARG A 1 298 ? -10.01800 25.73400 6.25500   1.000 64.60187  ? 298  ARG A NH2 1 
ATOM   2423 N  N   . PRO A 1 299 ? -8.25900  27.16400 14.93600  1.000 60.03146  ? 299  PRO A N   1 
ATOM   2424 C  CA  . PRO A 1 299 ? -8.95300  25.89900 14.82300  1.000 51.14147  ? 299  PRO A CA  1 
ATOM   2425 C  C   . PRO A 1 299 ? -10.47500 26.08600 14.79800  1.000 48.01099  ? 299  PRO A C   1 
ATOM   2426 O  O   . PRO A 1 299 ? -10.91600 27.19300 14.93000  1.000 51.83928  ? 299  PRO A O   1 
ATOM   2427 C  CB  . PRO A 1 299 ? -8.47800  25.20600 16.10600  1.000 44.61713  ? 299  PRO A CB  1 
ATOM   2428 C  CG  . PRO A 1 299 ? -8.41200  26.31700 17.11600  1.000 56.68464  ? 299  PRO A CG  1 
ATOM   2429 C  CD  . PRO A 1 299 ? -7.95200  27.52000 16.32100  1.000 68.70373  ? 299  PRO A CD  1 
ATOM   2430 N  N   . TYR A 1 300 ? -11.22200 24.99300 14.65500  1.000 42.32916  ? 300  TYR A N   1 
ATOM   2431 C  CA  . TYR A 1 300 ? -12.69700 25.07800 14.54400  1.000 39.26840  ? 300  TYR A CA  1 
ATOM   2432 C  C   . TYR A 1 300 ? -13.25900 25.84500 15.73200  1.000 41.16521  ? 300  TYR A C   1 
ATOM   2433 O  O   . TYR A 1 300 ? -12.71700 25.73000 16.81900  1.000 52.86154  ? 300  TYR A O   1 
ATOM   2434 C  CB  . TYR A 1 300 ? -13.31200 23.68900 14.37400  1.000 40.46938  ? 300  TYR A CB  1 
ATOM   2435 C  CG  . TYR A 1 300 ? -14.66100 23.62100 13.70800  1.000 35.85518  ? 300  TYR A CG  1 
ATOM   2436 C  CD1 . TYR A 1 300 ? -15.82800 23.71300 14.44400  1.000 38.53211  ? 300  TYR A CD1 1 
ATOM   2437 C  CD2 . TYR A 1 300 ? -14.77200 23.42800 12.34500  1.000 29.58873  ? 300  TYR A CD2 1 
ATOM   2438 C  CE1 . TYR A 1 300 ? -17.07100 23.64300 13.83900  1.000 33.58787  ? 300  TYR A CE1 1 
ATOM   2439 C  CE2 . TYR A 1 300 ? -16.00500 23.35400 11.72300  1.000 37.17467  ? 300  TYR A CE2 1 
ATOM   2440 C  CZ  . TYR A 1 300 ? -17.15900 23.46000 12.47200  1.000 33.89060  ? 300  TYR A CZ  1 
ATOM   2441 O  OH  . TYR A 1 300 ? -18.37400 23.39000 11.86200  1.000 34.96364  ? 300  TYR A OH  1 
ATOM   2442 N  N   . TRP A 1 301 ? -14.32600 26.59500 15.50600  1.000 42.58498  ? 301  TRP A N   1 
ATOM   2443 C  CA  . TRP A 1 301 ? -14.89100 27.45800 16.55400  1.000 40.50653  ? 301  TRP A CA  1 
ATOM   2444 C  C   . TRP A 1 301 ? -16.40400 27.41700 16.54200  1.000 36.71264  ? 301  TRP A C   1 
ATOM   2445 O  O   . TRP A 1 301 ? -16.98800 26.76500 15.68300  1.000 38.22528  ? 301  TRP A O   1 
ATOM   2446 C  CB  . TRP A 1 301 ? -14.39400 28.88800 16.33600  1.000 35.25557  ? 301  TRP A CB  1 
ATOM   2447 C  CG  . TRP A 1 301 ? -14.57600 29.42400 14.94300  1.000 40.44987  ? 301  TRP A CG  1 
ATOM   2448 C  CD1 . TRP A 1 301 ? -13.67600 29.38300 13.92300  1.000 41.48848  ? 301  TRP A CD1 1 
ATOM   2449 C  CD2 . TRP A 1 301 ? -15.74100 30.09500 14.42300  1.000 37.85688  ? 301  TRP A CD2 1 
ATOM   2450 N  NE1 . TRP A 1 301 ? -14.19400 29.98000 12.80800  1.000 35.32947  ? 301  TRP A NE1 1 
ATOM   2451 C  CE2 . TRP A 1 301 ? -15.45800 30.42400 13.08300  1.000 36.43510  ? 301  TRP A CE2 1 
ATOM   2452 C  CE3 . TRP A 1 301 ? -16.98400 30.44400 14.95600  1.000 34.70724  ? 301  TRP A CE3 1 
ATOM   2453 C  CZ2 . TRP A 1 301 ? -16.37700 31.08100 12.27200  1.000 28.82066  ? 301  TRP A CZ2 1 
ATOM   2454 C  CZ3 . TRP A 1 301 ? -17.89000 31.09400 14.15200  1.000 34.46372  ? 301  TRP A CZ3 1 
ATOM   2455 C  CH2 . TRP A 1 301 ? -17.58600 31.41200 12.83300  1.000 34.61405  ? 301  TRP A CH2 1 
ATOM   2456 N  N   . LEU A 1 302 ? -16.99800 28.10700 17.49800  1.000 39.21625  ? 302  LEU A N   1 
ATOM   2457 C  CA  . LEU A 1 302 ? -18.44400 28.13000 17.63300  1.000 30.99289  ? 302  LEU A CA  1 
ATOM   2458 C  C   . LEU A 1 302 ? -18.90700 29.56700 17.81300  1.000 41.24039  ? 302  LEU A C   1 
ATOM   2459 O  O   . LEU A 1 302 ? -18.17500 30.40700 18.34000  1.000 38.82530  ? 302  LEU A O   1 
ATOM   2460 C  CB  . LEU A 1 302 ? -18.90400 27.27200 18.82700  1.000 33.35317  ? 302  LEU A CB  1 
ATOM   2461 C  CG  . LEU A 1 302 ? -20.36400 27.34900 19.28300  1.000 31.83526  ? 302  LEU A CG  1 
ATOM   2462 C  CD1 . LEU A 1 302 ? -21.29700 26.79500 18.21800  1.000 33.59179  ? 302  LEU A CD1 1 
ATOM   2463 C  CD2 . LEU A 1 302 ? -20.56000 26.62700 20.60900  1.000 31.50154  ? 302  LEU A CD2 1 
ATOM   2464 N  N   . THR A 1 303 ? -20.15400 29.84200 17.42000  1.000 39.08513  ? 303  THR A N   1 
ATOM   2465 C  CA  . THR A 1 303 ? -20.79300 31.14500 17.66100  1.000 35.98163  ? 303  THR A CA  1 
ATOM   2466 C  C   . THR A 1 303 ? -22.06200 30.88700 18.41500  1.000 33.73757  ? 303  THR A C   1 
ATOM   2467 O  O   . THR A 1 303 ? -22.84300 30.04100 17.97500  1.000 33.73732  ? 303  THR A O   1 
ATOM   2468 C  CB  . THR A 1 303 ? -21.08600 31.93400 16.38400  1.000 34.69386  ? 303  THR A CB  1 
ATOM   2469 O  OG1 . THR A 1 303 ? -19.85100 32.45600 15.91600  1.000 47.87626  ? 303  THR A OG1 1 
ATOM   2470 C  CG2 . THR A 1 303 ? -22.03500 33.08900 16.63500  1.000 27.68628  ? 303  THR A CG2 1 
ATOM   2471 N  N   . ASP A 1 304 ? -22.24600 31.55800 19.53900  1.000 38.04182  ? 304  ASP A N   1 
ATOM   2472 C  CA  . ASP A 1 304 ? -23.54400 31.44900 20.23700  1.000 40.73314  ? 304  ASP A CA  1 
ATOM   2473 C  C   . ASP A 1 304 ? -24.25800 32.78400 20.00600  1.000 47.20977  ? 304  ASP A C   1 
ATOM   2474 O  O   . ASP A 1 304 ? -23.64800 33.83700 20.26000  1.000 42.75433  ? 304  ASP A O   1 
ATOM   2475 C  CB  . ASP A 1 304 ? -23.44500 31.07400 21.70500  1.000 38.35484  ? 304  ASP A CB  1 
ATOM   2476 C  CG  . ASP A 1 304 ? -23.19800 32.18700 22.71000  1.000 46.88580  ? 304  ASP A CG  1 
ATOM   2477 O  OD1 . ASP A 1 304 ? -22.17000 32.86800 22.60800  1.000 48.35537  ? 304  ASP A OD1 1 
ATOM   2478 O  OD2 . ASP A 1 304 ? -24.05900 32.35700 23.58700  1.000 41.41279  ? 304  ASP A OD2 1 
ATOM   2479 N  N   . ASP A 1 305 ? -25.46500 32.73300 19.45300  1.000 38.54679  ? 305  ASP A N   1 
ATOM   2480 C  CA  . ASP A 1 305 ? -26.22200 33.97300 19.19500  1.000 39.23281  ? 305  ASP A CA  1 
ATOM   2481 C  C   . ASP A 1 305 ? -27.61800 33.84800 19.78400  1.000 40.25304  ? 305  ASP A C   1 
ATOM   2482 O  O   . ASP A 1 305 ? -28.00400 32.74300 20.19300  1.000 31.73697  ? 305  ASP A O   1 
ATOM   2483 C  CB  . ASP A 1 305 ? -26.24300 34.32800 17.72100  1.000 47.50139  ? 305  ASP A CB  1 
ATOM   2484 C  CG  . ASP A 1 305 ? -26.32800 35.81500 17.40600  1.000 52.63822  ? 305  ASP A CG  1 
ATOM   2485 O  OD1 . ASP A 1 305 ? -27.27900 36.46300 17.86900  1.000 52.95514  ? 305  ASP A OD1 1 
ATOM   2486 O  OD2 . ASP A 1 305 ? -25.45200 36.30900 16.68100  1.000 58.74339  ? 305  ASP A OD2 1 
ATOM   2487 N  N   . ALA A 1 306 ? -28.32000 34.96800 19.84400  1.000 37.31753  ? 306  ALA A N   1 
ATOM   2488 C  CA  . ALA A 1 306 ? -29.67400 34.99500 20.36900  1.000 40.82122  ? 306  ALA A CA  1 
ATOM   2489 C  C   . ALA A 1 306 ? -30.64500 35.47800 19.30300  1.000 37.14482  ? 306  ALA A C   1 
ATOM   2490 O  O   . ALA A 1 306 ? -30.29500 36.28400 18.43600  1.000 42.08213  ? 306  ALA A O   1 
ATOM   2491 C  CB  . ALA A 1 306 ? -29.77300 35.89300 21.60500  1.000 31.00557  ? 306  ALA A CB  1 
ATOM   2492 N  N   . ILE A 1 307 ? -31.88100 34.97800 19.38500  1.000 37.50739  ? 307  ILE A N   1 
ATOM   2493 C  CA  . ILE A 1 307 ? -32.93400 35.40000 18.47000  1.000 37.24515  ? 307  ILE A CA  1 
ATOM   2494 C  C   . ILE A 1 307 ? -33.34300 36.84900 18.68500  1.000 39.97122  ? 307  ILE A C   1 
ATOM   2495 O  O   . ILE A 1 307 ? -34.10000 37.39800 17.87700  1.000 35.01213  ? 307  ILE A O   1 
ATOM   2496 C  CB  . ILE A 1 307 ? -34.15300 34.46300 18.60800  1.000 34.20611  ? 307  ILE A CB  1 
ATOM   2497 C  CG1 . ILE A 1 307 ? -34.99000 34.46400 17.32600  1.000 32.03853  ? 307  ILE A CG1 1 
ATOM   2498 C  CG2 . ILE A 1 307 ? -35.00000 34.85400 19.81200  1.000 40.60862  ? 307  ILE A CG2 1 
ATOM   2499 C  CD1 . ILE A 1 307 ? -36.10500 33.44400 17.32800  1.000 34.89201  ? 307  ILE A CD1 1 
ATOM   2500 N  N   . SER A 1 308 ? -32.88500 37.46100 19.78800  1.000 39.22011  ? 308  SER A N   1 
ATOM   2501 C  CA  . SER A 1 308 ? -33.17400 38.89000 20.09700  1.000 38.20266  ? 308  SER A CA  1 
ATOM   2502 C  C   . SER A 1 308 ? -31.87500 39.62700 20.40400  1.000 44.53635  ? 308  SER A C   1 
ATOM   2503 O  O   . SER A 1 308 ? -30.97800 39.02500 21.00500  1.000 36.55725  ? 308  SER A O   1 
ATOM   2504 C  CB  . SER A 1 308 ? -34.11800 39.08400 21.22900  1.000 36.90937  ? 308  SER A CB  1 
ATOM   2505 O  OG  . SER A 1 308 ? -34.12000 40.43100 21.66900  1.000 43.89571  ? 308  SER A OG  1 
ATOM   2506 N  N   . ALA A 1 309 ? -31.80300 40.91100 20.07300  1.000 45.67902  ? 309  ALA A N   1 
ATOM   2507 C  CA  . ALA A 1 309 ? -30.57100 41.70100 20.30900  1.000 44.72713  ? 309  ALA A CA  1 
ATOM   2508 C  C   . ALA A 1 309 ? -30.54300 42.22900 21.73700  1.000 42.49601  ? 309  ALA A C   1 
ATOM   2509 O  O   . ALA A 1 309 ? -29.49700 42.72100 22.16500  1.000 42.71420  ? 309  ALA A O   1 
ATOM   2510 C  CB  . ALA A 1 309 ? -30.51500 42.83300 19.33000  1.000 36.22279  ? 309  ALA A CB  1 
ATOM   2511 N  N   . SER A 1 310 ? -31.65100 42.08600 22.45300  1.000 45.47364  ? 310  SER A N   1 
ATOM   2512 C  CA  . SER A 1 310 ? -31.80100 42.67400 23.80100  1.000 44.16873  ? 310  SER A CA  1 
ATOM   2513 C  C   . SER A 1 310 ? -31.54500 41.65700 24.92300  1.000 47.62760  ? 310  SER A C   1 
ATOM   2514 O  O   . SER A 1 310 ? -30.70700 41.94700 25.77800  1.000 48.79698  ? 310  SER A O   1 
ATOM   2515 C  CB  . SER A 1 310 ? -33.17400 43.25500 23.91300  1.000 36.38524  ? 310  SER A CB  1 
ATOM   2516 O  OG  . SER A 1 310 ? -34.15400 42.25700 24.14000  1.000 64.98707  ? 310  SER A OG  1 
ATOM   2517 N  N   . SER A 1 311 ? -32.27100 40.54400 24.94000  1.000 43.74026  ? 311  SER A N   1 
ATOM   2518 C  CA  . SER A 1 311 ? -32.14800 39.55000 26.03200  1.000 41.24079  ? 311  SER A CA  1 
ATOM   2519 C  C   . SER A 1 311 ? -31.97600 38.14500 25.47100  1.000 47.27136  ? 311  SER A C   1 
ATOM   2520 O  O   . SER A 1 311 ? -32.20300 37.94400 24.27200  1.000 54.08863  ? 311  SER A O   1 
ATOM   2521 C  CB  . SER A 1 311 ? -33.33500 39.56000 26.92400  1.000 32.53636  ? 311  SER A CB  1 
ATOM   2522 O  OG  . SER A 1 311 ? -33.22200 38.58000 27.94000  1.000 53.23840  ? 311  SER A OG  1 
ATOM   2523 N  N   . TRP A 1 312 ? -31.56500 37.22700 26.32400  1.000 43.37034  ? 312  TRP A N   1 
ATOM   2524 C  CA  . TRP A 1 312 ? -31.48900 35.80600 25.93900  1.000 36.80859  ? 312  TRP A CA  1 
ATOM   2525 C  C   . TRP A 1 312 ? -32.74200 35.16800 26.52200  1.000 39.12642  ? 312  TRP A C   1 
ATOM   2526 O  O   . TRP A 1 312 ? -33.05400 34.04400 26.15200  1.000 45.39197  ? 312  TRP A O   1 
ATOM   2527 C  CB  . TRP A 1 312 ? -30.20000 35.20600 26.49000  1.000 38.96903  ? 312  TRP A CB  1 
ATOM   2528 C  CG  . TRP A 1 312 ? -28.93500 35.78000 25.93900  1.000 39.67143  ? 312  TRP A CG  1 
ATOM   2529 C  CD1 . TRP A 1 312 ? -28.33300 36.94600 26.30300  1.000 38.36396  ? 312  TRP A CD1 1 
ATOM   2530 C  CD2 . TRP A 1 312 ? -28.08800 35.18400 24.94400  1.000 42.94012  ? 312  TRP A CD2 1 
ATOM   2531 N  NE1 . TRP A 1 312 ? -27.18000 37.12500 25.59100  1.000 41.79724  ? 312  TRP A NE1 1 
ATOM   2532 C  CE2 . TRP A 1 312 ? -27.00300 36.06100 24.75000  1.000 43.72382  ? 312  TRP A CE2 1 
ATOM   2533 C  CE3 . TRP A 1 312 ? -28.14500 34.00600 24.19500  1.000 37.43623  ? 312  TRP A CE3 1 
ATOM   2534 C  CZ2 . TRP A 1 312 ? -25.98800 35.79300 23.83700  1.000 43.43599  ? 312  TRP A CZ2 1 
ATOM   2535 C  CZ3 . TRP A 1 312 ? -27.14100 33.74300 23.29300  1.000 35.71503  ? 312  TRP A CZ3 1 
ATOM   2536 C  CH2 . TRP A 1 312 ? -26.07900 34.62600 23.11700  1.000 41.99186  ? 312  TRP A CH2 1 
ATOM   2537 N  N   . SER A 1 313 ? -33.42700 35.89400 27.39800  1.000 43.70774  ? 313  SER A N   1 
ATOM   2538 C  CA  . SER A 1 313 ? -34.67400 35.39900 28.02400  1.000 46.96623  ? 313  SER A CA  1 
ATOM   2539 C  C   . SER A 1 313 ? -35.83500 36.28800 27.59200  1.000 39.96023  ? 313  SER A C   1 
ATOM   2540 O  O   . SER A 1 313 ? -35.57800 37.41100 27.17000  1.000 43.29748  ? 313  SER A O   1 
ATOM   2541 C  CB  . SER A 1 313 ? -34.56400 35.33500 29.52100  1.000 36.60838  ? 313  SER A CB  1 
ATOM   2542 O  OG  . SER A 1 313 ? -35.81000 35.02200 30.11000  1.000 44.38337  ? 313  SER A OG  1 
ATOM   2543 N  N   . TYR A 1 314 ? -37.06200 35.80600 27.75800  1.000 40.37477  ? 314  TYR A N   1 
ATOM   2544 C  CA  . TYR A 1 314 ? -38.23800 36.54600 27.24200  1.000 44.03824  ? 314  TYR A CA  1 
ATOM   2545 C  C   . TYR A 1 314 ? -38.59900 37.74000 28.12100  1.000 38.76442  ? 314  TYR A C   1 
ATOM   2546 O  O   . TYR A 1 314 ? -38.55800 37.62100 29.34100  1.000 45.20141  ? 314  TYR A O   1 
ATOM   2547 C  CB  . TYR A 1 314 ? -39.45100 35.63200 27.04300  1.000 35.93506  ? 314  TYR A CB  1 
ATOM   2548 C  CG  . TYR A 1 314 ? -40.74300 36.34800 26.75800  1.000 35.92456  ? 314  TYR A CG  1 
ATOM   2549 C  CD1 . TYR A 1 314 ? -41.05000 36.78800 25.48400  1.000 42.63378  ? 314  TYR A CD1 1 
ATOM   2550 C  CD2 . TYR A 1 314 ? -41.66100 36.58000 27.76300  1.000 38.40216  ? 314  TYR A CD2 1 
ATOM   2551 C  CE1 . TYR A 1 314 ? -42.23800 37.44300 25.21400  1.000 42.87945  ? 314  TYR A CE1 1 
ATOM   2552 C  CE2 . TYR A 1 314 ? -42.85300 37.23500 27.51200  1.000 42.79458  ? 314  TYR A CE2 1 
ATOM   2553 C  CZ  . TYR A 1 314 ? -43.14200 37.66900 26.23300  1.000 47.20927  ? 314  TYR A CZ  1 
ATOM   2554 O  OH  . TYR A 1 314 ? -44.31600 38.31100 25.98400  1.000 51.76359  ? 314  TYR A OH  1 
ATOM   2555 N  N   . THR A 1 315 ? -38.98700 38.84800 27.48600  1.000 38.01824  ? 315  THR A N   1 
ATOM   2556 C  CA  . THR A 1 315 ? -39.43200 40.07000 28.18800  1.000 47.95658  ? 315  THR A CA  1 
ATOM   2557 C  C   . THR A 1 315 ? -40.59600 40.66500 27.41500  1.000 44.75718  ? 315  THR A C   1 
ATOM   2558 O  O   . THR A 1 315 ? -40.53000 40.65600 26.18600  1.000 44.85403  ? 315  THR A O   1 
ATOM   2559 C  CB  . THR A 1 315 ? -38.27400 41.06000 28.28900  1.000 39.14474  ? 315  THR A CB  1 
ATOM   2560 O  OG1 . THR A 1 315 ? -37.98300 41.47200 26.96000  1.000 54.17995  ? 315  THR A OG1 1 
ATOM   2561 C  CG2 . THR A 1 315 ? -37.03100 40.46000 28.91900  1.000 39.21403  ? 315  THR A CG2 1 
ATOM   2562 N  N   . VAL A 1 316 ? -41.63000 41.16300 28.10000  1.000 51.43611  ? 316  VAL A N   1 
ATOM   2563 C  CA  . VAL A 1 316 ? -42.75100 41.85300 27.40000  1.000 51.79044  ? 316  VAL A CA  1 
ATOM   2564 C  C   . VAL A 1 316 ? -42.17300 42.93900 26.49300  1.000 50.91044  ? 316  VAL A C   1 
ATOM   2565 O  O   . VAL A 1 316 ? -41.43700 43.79300 26.99700  1.000 39.34471  ? 316  VAL A O   1 
ATOM   2566 C  CB  . VAL A 1 316 ? -43.78500 42.43800 28.37300  1.000 52.86248  ? 316  VAL A CB  1 
ATOM   2567 C  CG1 . VAL A 1 316 ? -44.89800 43.16400 27.64100  1.000 46.01326  ? 316  VAL A CG1 1 
ATOM   2568 C  CG2 . VAL A 1 316 ? -44.35200 41.37500 29.29900  1.000 45.88314  ? 316  VAL A CG2 1 
ATOM   2569 N  N   . GLY A 1 317 ? -42.47600 42.86100 25.19700  1.000 48.31123  ? 317  GLY A N   1 
ATOM   2570 C  CA  . GLY A 1 317 ? -42.01400 43.87000 24.23400  1.000 43.92227  ? 317  GLY A CA  1 
ATOM   2571 C  C   . GLY A 1 317 ? -40.73600 43.47700 23.55500  1.000 40.91327  ? 317  GLY A C   1 
ATOM   2572 O  O   . GLY A 1 317 ? -40.17800 44.29600 22.82800  1.000 54.53585  ? 317  GLY A O   1 
ATOM   2573 N  N   . ILE A 1 318 ? -40.30100 42.25200 23.78700  1.000 43.92281  ? 318  ILE A N   1 
ATOM   2574 C  CA  . ILE A 1 318 ? -39.06300 41.76300 23.13000  1.000 42.30061  ? 318  ILE A CA  1 
ATOM   2575 C  C   . ILE A 1 318 ? -39.27300 41.79400 21.62200  1.000 45.98479  ? 318  ILE A C   1 
ATOM   2576 O  O   . ILE A 1 318 ? -40.37200 41.48500 21.16400  1.000 38.48895  ? 318  ILE A O   1 
ATOM   2577 C  CB  . ILE A 1 318 ? -38.65800 40.35900 23.62900  1.000 40.15376  ? 318  ILE A CB  1 
ATOM   2578 C  CG1 . ILE A 1 318 ? -37.26300 39.96800 23.13600  1.000 41.15575  ? 318  ILE A CG1 1 
ATOM   2579 C  CG2 . ILE A 1 318 ? -39.70100 39.31700 23.27100  1.000 41.01385  ? 318  ILE A CG2 1 
ATOM   2580 C  CD1 . ILE A 1 318 ? -36.52500 39.04000 24.06700  1.000 39.44468  ? 318  ILE A CD1 1 
ATOM   2581 N  N   . GLN A 1 319 ? -38.24400 42.19200 20.90200  1.000 48.64805  ? 319  GLN A N   1 
ATOM   2582 C  CA  . GLN A 1 319 ? -38.32700 42.17900 19.43000  1.000 45.53722  ? 319  GLN A CA  1 
ATOM   2583 C  C   . GLN A 1 319 ? -37.27700 41.18800 18.95300  1.000 39.38039  ? 319  GLN A C   1 
ATOM   2584 O  O   . GLN A 1 319 ? -36.30500 40.97200 19.67100  1.000 37.79393  ? 319  GLN A O   1 
ATOM   2585 C  CB  . GLN A 1 319 ? -38.18800 43.59000 18.86600  1.000 43.98429  ? 319  GLN A CB  1 
ATOM   2586 C  CG  . GLN A 1 319 ? -39.26100 44.54400 19.35800  1.000 51.36245  ? 319  GLN A CG  1 
ATOM   2587 C  CD  . GLN A 1 319 ? -39.33600 45.77200 18.48800  1.000 63.70600  ? 319  GLN A CD  1 
ATOM   2588 O  OE1 . GLN A 1 319 ? -38.40300 46.09500 17.76000  1.000 60.08896  ? 319  GLN A OE1 1 
ATOM   2589 N  NE2 . GLN A 1 319 ? -40.45700 46.46600 18.55900  1.000 71.99341  ? 319  GLN A NE2 1 
ATOM   2590 N  N   . TYR A 1 320 ? -37.44800 40.66600 17.75300  1.000 42.93267  ? 320  TYR A N   1 
ATOM   2591 C  CA  . TYR A 1 320 ? -36.56100 39.57300 17.30800  1.000 39.21921  ? 320  TYR A CA  1 
ATOM   2592 C  C   . TYR A 1 320 ? -35.85200 39.91000 16.00900  1.000 34.41034  ? 320  TYR A C   1 
ATOM   2593 O  O   . TYR A 1 320 ? -36.30500 40.78200 15.27800  1.000 35.22761  ? 320  TYR A O   1 
ATOM   2594 C  CB  . TYR A 1 320 ? -37.40500 38.30700 17.15800  1.000 34.27471  ? 320  TYR A CB  1 
ATOM   2595 C  CG  . TYR A 1 320 ? -38.28900 37.95900 18.32500  1.000 33.86802  ? 320  TYR A CG  1 
ATOM   2596 C  CD1 . TYR A 1 320 ? -37.77100 37.39000 19.47400  1.000 38.91732  ? 320  TYR A CD1 1 
ATOM   2597 C  CD2 . TYR A 1 320 ? -39.65200 38.17900 18.27200  1.000 42.60578  ? 320  TYR A CD2 1 
ATOM   2598 C  CE1 . TYR A 1 320 ? -38.58300 37.06000 20.54500  1.000 36.65730  ? 320  TYR A CE1 1 
ATOM   2599 C  CE2 . TYR A 1 320 ? -40.47800 37.85400 19.33200  1.000 41.68292  ? 320  TYR A CE2 1 
ATOM   2600 C  CZ  . TYR A 1 320 ? -39.94300 37.28800 20.47100  1.000 41.24526  ? 320  TYR A CZ  1 
ATOM   2601 O  OH  . TYR A 1 320 ? -40.75800 36.97400 21.51500  1.000 45.01003  ? 320  TYR A OH  1 
ATOM   2602 N  N   . TYR A 1 321 ? -34.75700 39.21100 15.75700  1.000 34.48591  ? 321  TYR A N   1 
ATOM   2603 C  CA  . TYR A 1 321 ? -34.04700 39.37600 14.47500  1.000 34.89226  ? 321  TYR A CA  1 
ATOM   2604 C  C   . TYR A 1 321 ? -34.88000 38.77500 13.33300  1.000 44.51723  ? 321  TYR A C   1 
ATOM   2605 O  O   . TYR A 1 321 ? -35.90600 38.15100 13.59400  1.000 39.69693  ? 321  TYR A O   1 
ATOM   2606 C  CB  . TYR A 1 321 ? -32.68800 38.69200 14.53700  1.000 31.89882  ? 321  TYR A CB  1 
ATOM   2607 C  CG  . TYR A 1 321 ? -31.61200 39.36500 15.34800  1.000 46.78567  ? 321  TYR A CG  1 
ATOM   2608 C  CD1 . TYR A 1 321 ? -30.96500 40.49400 14.88000  1.000 37.94967  ? 321  TYR A CD1 1 
ATOM   2609 C  CD2 . TYR A 1 321 ? -31.20200 38.83900 16.56100  1.000 43.28926  ? 321  TYR A CD2 1 
ATOM   2610 C  CE1 . TYR A 1 321 ? -29.95900 41.09900 15.61100  1.000 43.83749  ? 321  TYR A CE1 1 
ATOM   2611 C  CE2 . TYR A 1 321 ? -30.19700 39.43300 17.30300  1.000 40.55265  ? 321  TYR A CE2 1 
ATOM   2612 C  CZ  . TYR A 1 321 ? -29.57300 40.56800 16.82600  1.000 42.53120  ? 321  TYR A CZ  1 
ATOM   2613 O  OH  . TYR A 1 321 ? -28.58300 41.16300 17.54900  1.000 47.00679  ? 321  TYR A OH  1 
ATOM   2614 N  N   . SER A 1 322 ? -34.43000 38.95700 12.09700  1.000 41.62547  ? 322  SER A N   1 
ATOM   2615 C  CA  . SER A 1 322 ? -35.15800 38.47100 10.91400  1.000 43.43827  ? 322  SER A CA  1 
ATOM   2616 C  C   . SER A 1 322 ? -34.63500 37.08500 10.54600  1.000 39.22333  ? 322  SER A C   1 
ATOM   2617 O  O   . SER A 1 322 ? -33.52100 36.73700 10.94900  1.000 32.97393  ? 322  SER A O   1 
ATOM   2618 C  CB  . SER A 1 322 ? -34.97800 39.43500 9.76700   1.000 33.68278  ? 322  SER A CB  1 
ATOM   2619 O  OG  . SER A 1 322 ? -33.68400 39.35800 9.19200   1.000 41.26949  ? 322  SER A OG  1 
ATOM   2620 N  N   . SER A 1 323 ? -35.42600 36.32600 9.80300   1.000 40.40025  ? 323  SER A N   1 
ATOM   2621 C  CA  . SER A 1 323 ? -34.98000 34.99700 9.33200   1.000 38.86123  ? 323  SER A CA  1 
ATOM   2622 C  C   . SER A 1 323 ? -33.75600 35.14800 8.42900   1.000 33.69567  ? 323  SER A C   1 
ATOM   2623 O  O   . SER A 1 323 ? -32.88400 34.29100 8.48600   1.000 42.76116  ? 323  SER A O   1 
ATOM   2624 C  CB  . SER A 1 323 ? -36.11500 34.30500 8.66000   1.000 42.75175  ? 323  SER A CB  1 
ATOM   2625 O  OG  . SER A 1 323 ? -37.27400 34.35600 9.46700   1.000 54.85596  ? 323  SER A OG  1 
ATOM   2626 N  N   . LYS A 1 324 ? -33.68400 36.23200 7.66100   1.000 38.78029  ? 324  LYS A N   1 
ATOM   2627 C  CA  . LYS A 1 324 ? -32.55300 36.44100 6.72200   1.000 43.45772  ? 324  LYS A CA  1 
ATOM   2628 C  C   . LYS A 1 324 ? -31.25500 36.64100 7.50000   1.000 41.76854  ? 324  LYS A C   1 
ATOM   2629 O  O   . LYS A 1 324 ? -30.23100 36.11100 7.08000   1.000 43.72337  ? 324  LYS A O   1 
ATOM   2630 C  CB  . LYS A 1 324 ? -32.79100 37.64600 5.81200   1.000 40.91518  ? 324  LYS A CB  1 
ATOM   2631 C  CG  . LYS A 1 324 ? -31.61100 38.02200 4.92800   1.000 43.04816  ? 324  LYS A CG  1 
ATOM   2632 C  CD  . LYS A 1 324 ? -31.72200 39.39600 4.31200   1.000 40.11978  ? 324  LYS A CD  1 
ATOM   2633 C  CE  . LYS A 1 324 ? -32.91200 39.54000 3.39100   1.000 50.81715  ? 324  LYS A CE  1 
ATOM   2634 N  NZ  . LYS A 1 324 ? -32.85400 38.56800 2.27500   1.000 62.33553  ? 324  LYS A NZ  1 
ATOM   2635 N  N   . ALA A 1 325 ? -31.31800 37.40500 8.57800   1.000 39.23167  ? 325  ALA A N   1 
ATOM   2636 C  CA  . ALA A 1 325 ? -30.10200 37.70800 9.35900   1.000 40.43887  ? 325  ALA A CA  1 
ATOM   2637 C  C   . ALA A 1 325 ? -29.53200 36.40400 9.90800   1.000 37.52769  ? 325  ALA A C   1 
ATOM   2638 O  O   . ALA A 1 325 ? -28.35600 36.14300 9.69500   1.000 40.08729  ? 325  ALA A O   1 
ATOM   2639 C  CB  . ALA A 1 325 ? -30.46400 38.66600 10.45500  1.000 40.34786  ? 325  ALA A CB  1 
ATOM   2640 N  N   . MET A 1 326 ? -30.39300 35.59600 10.50500  1.000 34.93154  ? 326  MET A N   1 
ATOM   2641 C  CA  . MET A 1 326 ? -29.97100 34.29700 11.06800  1.000 32.60867  ? 326  MET A CA  1 
ATOM   2642 C  C   . MET A 1 326 ? -29.41900 33.40500 9.95600   1.000 34.41877  ? 326  MET A C   1 
ATOM   2643 O  O   . MET A 1 326 ? -28.32200 32.87600 10.13600  1.000 35.56661  ? 326  MET A O   1 
ATOM   2644 C  CB  . MET A 1 326 ? -31.16000 33.64900 11.76800  1.000 31.35617  ? 326  MET A CB  1 
ATOM   2645 C  CG  . MET A 1 326 ? -31.77700 34.52200 12.84600  1.000 37.54834  ? 326  MET A CG  1 
ATOM   2646 S  SD  . MET A 1 326 ? -30.70200 34.87100 14.26600  1.000 38.48648  ? 326  MET A SD  1 
ATOM   2647 C  CE  . MET A 1 326 ? -29.69900 36.21500 13.64100  1.000 35.99097  ? 326  MET A CE  1 
ATOM   2648 N  N   . VAL A 1 327 ? -30.10700 33.31700 8.81800   1.000 35.57820  ? 327  VAL A N   1 
ATOM   2649 C  CA  . VAL A 1 327 ? -29.63500 32.39000 7.79200   1.000 33.01597  ? 327  VAL A CA  1 
ATOM   2650 C  C   . VAL A 1 327 ? -28.32800 32.88000 7.17800   1.000 36.64249  ? 327  VAL A C   1 
ATOM   2651 O  O   . VAL A 1 327 ? -27.38600 32.09800 6.98500   1.000 36.60166  ? 327  VAL A O   1 
ATOM   2652 C  CB  . VAL A 1 327 ? -30.72000 32.16800 6.72300   1.000 43.73372  ? 327  VAL A CB  1 
ATOM   2653 C  CG1 . VAL A 1 327 ? -30.14600 31.41100 5.53300   1.000 37.60204  ? 327  VAL A CG1 1 
ATOM   2654 C  CG2 . VAL A 1 327 ? -31.89100 31.40700 7.31800   1.000 40.97066  ? 327  VAL A CG2 1 
ATOM   2655 N  N   . HIS A 1 328 ? -28.25500 34.17600 6.90500   1.000 36.53476  ? 328  HIS A N   1 
ATOM   2656 C  CA  . HIS A 1 328 ? -27.03100 34.74200 6.29000   1.000 32.63095  ? 328  HIS A CA  1 
ATOM   2657 C  C   . HIS A 1 328 ? -25.86600 34.64300 7.28300   1.000 37.50154  ? 328  HIS A C   1 
ATOM   2658 O  O   . HIS A 1 328 ? -24.74100 34.35400 6.86300   1.000 44.77551  ? 328  HIS A O   1 
ATOM   2659 C  CB  . HIS A 1 328 ? -27.29900 36.15700 5.76900   1.000 34.22360  ? 328  HIS A CB  1 
ATOM   2660 C  CG  . HIS A 1 328 ? -28.16200 36.25100 4.55500   1.000 36.87994  ? 328  HIS A CG  1 
ATOM   2661 N  ND1 . HIS A 1 328 ? -28.05300 37.30200 3.67300   1.000 38.65131  ? 328  HIS A ND1 1 
ATOM   2662 C  CD2 . HIS A 1 328 ? -29.13900 35.47600 4.07900   1.000 34.72831  ? 328  HIS A CD2 1 
ATOM   2663 C  CE1 . HIS A 1 328 ? -28.93000 37.14600 2.69800   1.000 35.98196  ? 328  HIS A CE1 1 
ATOM   2664 N  NE2 . HIS A 1 328 ? -29.59800 36.04400 2.92400   1.000 30.40344  ? 328  HIS A NE2 1 
ATOM   2665 N  N   . SER A 1 329 ? -26.14000 34.86900 8.56200   1.000 33.01850  ? 329  SER A N   1 
ATOM   2666 C  CA  . SER A 1 329 ? -25.07400 34.79300 9.59300   1.000 38.27653  ? 329  SER A CA  1 
ATOM   2667 C  C   . SER A 1 329 ? -24.57500 33.33800 9.70300   1.000 33.07875  ? 329  SER A C   1 
ATOM   2668 O  O   . SER A 1 329 ? -23.36200 33.13800 9.70100   1.000 34.17081  ? 329  SER A O   1 
ATOM   2669 C  CB  . SER A 1 329 ? -25.55000 35.38900 10.88900  1.000 36.23741  ? 329  SER A CB  1 
ATOM   2670 O  OG  . SER A 1 329 ? -26.17200 36.64600 10.68200  1.000 38.53820  ? 329  SER A OG  1 
ATOM   2671 N  N   . LEU A 1 330 ? -25.48600 32.36600 9.68200   1.000 38.89767  ? 330  LEU A N   1 
ATOM   2672 C  CA  . LEU A 1 330 ? -25.10900 30.92800 9.70300   1.000 36.08733  ? 330  LEU A CA  1 
ATOM   2673 C  C   . LEU A 1 330 ? -24.20200 30.61500 8.51700   1.000 32.62312  ? 330  LEU A C   1 
ATOM   2674 O  O   . LEU A 1 330 ? -23.16900 29.98400 8.73100   1.000 39.21677  ? 330  LEU A O   1 
ATOM   2675 C  CB  . LEU A 1 330 ? -26.35500 30.05200 9.69100   1.000 25.61856  ? 330  LEU A CB  1 
ATOM   2676 C  CG  . LEU A 1 330 ? -26.12700 28.54800 9.51200   1.000 31.29596  ? 330  LEU A CG  1 
ATOM   2677 C  CD1 . LEU A 1 330 ? -25.22300 27.99700 10.59200  1.000 25.88210  ? 330  LEU A CD1 1 
ATOM   2678 C  CD2 . LEU A 1 330 ? -27.44400 27.79800 9.49200   1.000 28.78138  ? 330  LEU A CD2 1 
ATOM   2679 N  N   . LEU A 1 331 ? -24.53800 31.11700 7.33700   1.000 33.30424  ? 331  LEU A N   1 
ATOM   2680 C  CA  . LEU A 1 331 ? -23.73700 30.85300 6.11900   1.000 29.42492  ? 331  LEU A CA  1 
ATOM   2681 C  C   . LEU A 1 331 ? -22.33100 31.44600 6.25500   1.000 34.44909  ? 331  LEU A C   1 
ATOM   2682 O  O   . LEU A 1 331 ? -21.39300 30.82600 5.76200   1.000 46.25820  ? 331  LEU A O   1 
ATOM   2683 C  CB  . LEU A 1 331 ? -24.46900 31.38100 4.88900   1.000 33.66128  ? 331  LEU A CB  1 
ATOM   2684 C  CG  . LEU A 1 331 ? -25.79300 30.69600 4.53800   1.000 36.18784  ? 331  LEU A CG  1 
ATOM   2685 C  CD1 . LEU A 1 331 ? -26.45500 31.40400 3.37300   1.000 37.15511  ? 331  LEU A CD1 1 
ATOM   2686 C  CD2 . LEU A 1 331 ? -25.57700 29.23300 4.20800   1.000 29.37842  ? 331  LEU A CD2 1 
ATOM   2687 N  N   . ASP A 1 332 ? -22.18500 32.59900 6.89500   1.000 36.45778  ? 332  ASP A N   1 
ATOM   2688 C  CA  . ASP A 1 332 ? -20.85800 33.26600 7.00400   1.000 38.97131  ? 332  ASP A CA  1 
ATOM   2689 C  C   . ASP A 1 332 ? -20.01400 32.49800 8.02200   1.000 38.31342  ? 332  ASP A C   1 
ATOM   2690 O  O   . ASP A 1 332 ? -18.84600 32.27300 7.75100   1.000 40.98911  ? 332  ASP A O   1 
ATOM   2691 C  CB  . ASP A 1 332 ? -21.01300 34.75000 7.35600   1.000 38.39996  ? 332  ASP A CB  1 
ATOM   2692 C  CG  . ASP A 1 332 ? -19.71800 35.53100 7.45400   1.000 49.03084  ? 332  ASP A CG  1 
ATOM   2693 O  OD1 . ASP A 1 332 ? -19.00200 35.60800 6.44400   1.000 46.63980  ? 332  ASP A OD1 1 
ATOM   2694 O  OD2 . ASP A 1 332 ? -19.44700 36.06600 8.54000   1.000 46.24053  ? 332  ASP A OD2 1 
ATOM   2695 N  N   . ARG A 1 333 ? -20.62400 32.10700 9.13300   1.000 37.30299  ? 333  ARG A N   1 
ATOM   2696 C  CA  . ARG A 1 333 ? -19.92800 31.36200 10.21300  1.000 35.90650  ? 333  ARG A CA  1 
ATOM   2697 C  C   . ARG A 1 333 ? -19.40100 30.02100 9.68300   1.000 37.17205  ? 333  ARG A C   1 
ATOM   2698 O  O   . ARG A 1 333 ? -18.23600 29.71200 9.92400   1.000 41.44982  ? 333  ARG A O   1 
ATOM   2699 C  CB  . ARG A 1 333 ? -20.91900 31.20000 11.36200  1.000 35.04167  ? 333  ARG A CB  1 
ATOM   2700 C  CG  . ARG A 1 333 ? -21.67600 32.46500 11.73200  1.000 32.56895  ? 333  ARG A CG  1 
ATOM   2701 C  CD  . ARG A 1 333 ? -21.02100 33.40700 12.71500  1.000 40.51708  ? 333  ARG A CD  1 
ATOM   2702 N  NE  . ARG A 1 333 ? -21.77300 34.64300 12.87500  1.000 42.27404  ? 333  ARG A NE  1 
ATOM   2703 C  CZ  . ARG A 1 333 ? -22.94700 34.73600 13.49000  1.000 46.15779  ? 333  ARG A CZ  1 
ATOM   2704 N  NH1 . ARG A 1 333 ? -23.54600 33.65400 13.95200  1.000 47.35867  ? 333  ARG A NH1 1 
ATOM   2705 N  NH2 . ARG A 1 333 ? -23.54300 35.90700 13.60200  1.000 44.29396  ? 333  ARG A NH2 1 
ATOM   2706 N  N   . ILE A 1 334 ? -20.22200 29.28300 8.94100   1.000 34.83783  ? 334  ILE A N   1 
ATOM   2707 C  CA  . ILE A 1 334 ? -19.81900 27.94400 8.42600   1.000 31.24628  ? 334  ILE A CA  1 
ATOM   2708 C  C   . ILE A 1 334 ? -18.78800 28.14700 7.31300   1.000 33.89193  ? 334  ILE A C   1 
ATOM   2709 O  O   . ILE A 1 334 ? -17.90700 27.30100 7.16000   1.000 40.56316  ? 334  ILE A O   1 
ATOM   2710 C  CB  . ILE A 1 334 ? -21.05000 27.12800 7.99300   1.000 30.13436  ? 334  ILE A CB  1 
ATOM   2711 C  CG1 . ILE A 1 334 ? -21.72500 27.71400 6.75800   1.000 39.74381  ? 334  ILE A CG1 1 
ATOM   2712 C  CG2 . ILE A 1 334 ? -22.03100 26.96000 9.15000   1.000 32.44197  ? 334  ILE A CG2 1 
ATOM   2713 C  CD1 . ILE A 1 334 ? -22.88100 26.88200 6.24000   1.000 41.24741  ? 334  ILE A CD1 1 
ATOM   2714 N  N   . SER A 1 335 ? -18.88800 29.26200 6.60200   1.000 35.32308  ? 335  SER A N   1 
ATOM   2715 C  CA  . SER A 1 335 ? -17.87600 29.58900 5.56900   1.000 37.09112  ? 335  SER A CA  1 
ATOM   2716 C  C   . SER A 1 335 ? -16.52500 29.84500 6.24200   1.000 42.57844  ? 335  SER A C   1 
ATOM   2717 O  O   . SER A 1 335 ? -15.50400 29.58700 5.60500   1.000 40.92014  ? 335  SER A O   1 
ATOM   2718 C  CB  . SER A 1 335 ? -18.30800 30.79100 4.75400   1.000 36.15867  ? 335  SER A CB  1 
ATOM   2719 O  OG  . SER A 1 335 ? -18.11600 32.01500 5.44300   1.000 39.75253  ? 335  SER A OG  1 
ATOM   2720 N  N   . LYS A 1 336 ? -16.53000 30.27400 7.50600   1.000 36.51678  ? 336  LYS A N   1 
ATOM   2721 C  CA  . LYS A 1 336 ? -15.26700 30.62200 8.21100   1.000 36.26631  ? 336  LYS A CA  1 
ATOM   2722 C  C   . LYS A 1 336 ? -14.89900 29.55600 9.26500   1.000 43.41217  ? 336  LYS A C   1 
ATOM   2723 O  O   . LYS A 1 336 ? -14.36900 29.95700 10.29300  1.000 42.00998  ? 336  LYS A O   1 
ATOM   2724 C  CB  . LYS A 1 336 ? -15.39000 32.02700 8.80400   1.000 40.74290  ? 336  LYS A CB  1 
ATOM   2725 C  CG  . LYS A 1 336 ? -15.54900 33.16500 7.80900   1.000 39.57199  ? 336  LYS A CG  1 
ATOM   2726 C  CD  . LYS A 1 336 ? -16.11600 34.39600 8.46900   1.000 46.24727  ? 336  LYS A CD  1 
ATOM   2727 C  CE  . LYS A 1 336 ? -16.11100 35.62500 7.58900   1.000 47.82378  ? 336  LYS A CE  1 
ATOM   2728 N  NZ  . LYS A 1 336 ? -16.75300 36.76900 8.27300   1.000 45.31063  ? 336  LYS A NZ  1 
ATOM   2729 N  N   . ASN A 1 337 ? -15.15500 28.26100 9.02100   1.000 38.78185  ? 337  ASN A N   1 
ATOM   2730 C  CA  . ASN A 1 337 ? -14.75700 27.12500 9.91000   1.000 38.12663  ? 337  ASN A CA  1 
ATOM   2731 C  C   . ASN A 1 337 ? -15.37600 27.22000 11.29600  1.000 35.71634  ? 337  ASN A C   1 
ATOM   2732 O  O   . ASN A 1 337 ? -14.65300 27.02900 12.26400  1.000 34.37973  ? 337  ASN A O   1 
ATOM   2733 C  CB  . ASN A 1 337 ? -13.24300 26.96000 10.01000  1.000 44.51786  ? 337  ASN A CB  1 
ATOM   2734 C  CG  . ASN A 1 337 ? -12.81200 25.62600 10.56900  1.000 40.65917  ? 337  ASN A CG  1 
ATOM   2735 O  OD1 . ASN A 1 337 ? -13.29600 24.58300 10.14400  1.000 50.73516  ? 337  ASN A OD1 1 
ATOM   2736 N  ND2 . ASN A 1 337 ? -11.89200 25.65600 11.51600  1.000 48.83127  ? 337  ASN A ND2 1 
ATOM   2737 N  N   . GLY A 1 338 ? -16.67700 27.43500 11.35000  1.000 33.40003  ? 338  GLY A N   1 
ATOM   2738 C  CA  . GLY A 1 338 ? -17.37600 27.51300 12.62800  1.000 32.13349  ? 338  GLY A CA  1 
ATOM   2739 C  C   . GLY A 1 338 ? -18.79300 27.00200 12.56100  1.000 37.43121  ? 338  GLY A C   1 
ATOM   2740 O  O   . GLY A 1 338 ? -19.24600 26.67800 11.46900  1.000 33.78510  ? 338  GLY A O   1 
ATOM   2741 N  N   . ASN A 1 339 ? -19.45800 26.94800 13.70700  1.000 35.54708  ? 339  ASN A N   1 
ATOM   2742 C  CA  . ASN A 1 339 ? -20.86400 26.51100 13.78500  1.000 36.65313  ? 339  ASN A CA  1 
ATOM   2743 C  C   . ASN A 1 339 ? -21.68800 27.64500 14.38300  1.000 32.51390  ? 339  ASN A C   1 
ATOM   2744 O  O   . ASN A 1 339 ? -21.09600 28.64100 14.78000  1.000 34.50541  ? 339  ASN A O   1 
ATOM   2745 C  CB  . ASN A 1 339 ? -21.03900 25.27500 14.66900  1.000 32.86988  ? 339  ASN A CB  1 
ATOM   2746 C  CG  . ASN A 1 339 ? -20.52100 23.98900 14.07200  1.000 41.01866  ? 339  ASN A CG  1 
ATOM   2747 O  OD1 . ASN A 1 339 ? -20.33700 23.88600 12.86600  1.000 45.22375  ? 339  ASN A OD1 1 
ATOM   2748 N  ND2 . ASN A 1 339 ? -20.29700 22.99900 14.91700  1.000 35.22657  ? 339  ASN A ND2 1 
ATOM   2749 N  N   . MET A 1 340 ? -22.99600 27.46100 14.47900  1.000 31.51869  ? 340  MET A N   1 
ATOM   2750 C  CA  . MET A 1 340 ? -23.87400 28.48500 15.07900  1.000 34.58896  ? 340  MET A CA  1 
ATOM   2751 C  C   . MET A 1 340 ? -24.85800 27.87700 16.06400  1.000 38.44011  ? 340  MET A C   1 
ATOM   2752 O  O   . MET A 1 340 ? -25.57600 26.94200 15.69700  1.000 43.29242  ? 340  MET A O   1 
ATOM   2753 C  CB  . MET A 1 340 ? -24.64700 29.28200 14.02700  1.000 34.60914  ? 340  MET A CB  1 
ATOM   2754 C  CG  . MET A 1 340 ? -25.55600 30.34400 14.59700  1.000 37.93339  ? 340  MET A CG  1 
ATOM   2755 S  SD  . MET A 1 340 ? -26.21100 31.43400 13.31100  1.000 42.27109  ? 340  MET A SD  1 
ATOM   2756 C  CE  . MET A 1 340 ? -27.59700 32.16800 14.17300  1.000 43.49770  ? 340  MET A CE  1 
ATOM   2757 N  N   . LEU A 1 341 ? -24.89600 28.43900 17.26200  1.000 36.44404  ? 341  LEU A N   1 
ATOM   2758 C  CA  . LEU A 1 341 ? -25.82900 27.99400 18.29000  1.000 34.58733  ? 341  LEU A CA  1 
ATOM   2759 C  C   . LEU A 1 341 ? -26.78700 29.14600 18.56400  1.000 39.78520  ? 341  LEU A C   1 
ATOM   2760 O  O   . LEU A 1 341 ? -26.40600 30.14300 19.18800  1.000 39.36788  ? 341  LEU A O   1 
ATOM   2761 C  CB  . LEU A 1 341 ? -25.08600 27.56500 19.55400  1.000 34.19524  ? 341  LEU A CB  1 
ATOM   2762 C  CG  . LEU A 1 341 ? -25.94500 27.19300 20.76200  1.000 34.85131  ? 341  LEU A CG  1 
ATOM   2763 C  CD1 . LEU A 1 341 ? -26.89600 26.05500 20.42700  1.000 36.33862  ? 341  LEU A CD1 1 
ATOM   2764 C  CD2 . LEU A 1 341 ? -25.06400 26.83100 21.94800  1.000 41.88881  ? 341  LEU A CD2 1 
ATOM   2765 N  N   . LEU A 1 342 ? -28.02300 29.01600 18.09000  1.000 32.29767  ? 342  LEU A N   1 
ATOM   2766 C  CA  A LEU A 1 342 ? -29.01800 30.07100 18.22400  0.502 35.67250  ? 342  LEU A CA  1 
ATOM   2767 C  CA  B LEU A 1 342 ? -29.01800 30.07100 18.22400  0.498 35.68178  ? 342  LEU A CA  1 
ATOM   2768 C  C   . LEU A 1 342 ? -29.82800 29.87400 19.49800  1.000 40.16867  ? 342  LEU A C   1 
ATOM   2769 O  O   . LEU A 1 342 ? -30.24600 28.75400 19.81000  1.000 42.23194  ? 342  LEU A O   1 
ATOM   2770 C  CB  A LEU A 1 342 ? -29.94500 30.09400 17.00800  0.502 34.06019  ? 342  LEU A CB  1 
ATOM   2771 C  CB  B LEU A 1 342 ? -29.94500 30.09400 17.00800  0.498 34.07608  ? 342  LEU A CB  1 
ATOM   2772 C  CG  A LEU A 1 342 ? -31.02800 31.17500 17.01600  0.502 36.96313  ? 342  LEU A CG  1 
ATOM   2773 C  CG  B LEU A 1 342 ? -31.03000 31.17300 17.01700  0.498 35.76473  ? 342  LEU A CG  1 
ATOM   2774 C  CD1 A LEU A 1 342 ? -30.40100 32.55900 17.06600  0.502 34.84767  ? 342  LEU A CD1 1 
ATOM   2775 C  CD1 B LEU A 1 342 ? -30.40400 32.55800 17.06700  0.498 34.54010  ? 342  LEU A CD1 1 
ATOM   2776 C  CD2 A LEU A 1 342 ? -31.94500 31.03600 15.81000  0.502 34.43654  ? 342  LEU A CD2 1 
ATOM   2777 C  CD2 B LEU A 1 342 ? -31.94700 31.03300 15.81100  0.498 34.79129  ? 342  LEU A CD2 1 
ATOM   2778 N  N   . ASN A 1 343 ? -30.04700 30.96200 20.22800  1.000 41.78280  ? 343  ASN A N   1 
ATOM   2779 C  CA  . ASN A 1 343 ? -30.82500 30.94000 21.45800  1.000 38.40547  ? 343  ASN A CA  1 
ATOM   2780 C  C   . ASN A 1 343 ? -32.24200 31.42400 21.18200  1.000 36.19145  ? 343  ASN A C   1 
ATOM   2781 O  O   . ASN A 1 343 ? -32.43700 32.43800 20.50400  1.000 38.48147  ? 343  ASN A O   1 
ATOM   2782 C  CB  . ASN A 1 343 ? -30.16900 31.80800 22.53200  1.000 32.13884  ? 343  ASN A CB  1 
ATOM   2783 C  CG  . ASN A 1 343 ? -31.04100 31.97700 23.76000  1.000 33.60262  ? 343  ASN A CG  1 
ATOM   2784 O  OD1 . ASN A 1 343 ? -31.03100 31.14300 24.66500  1.000 42.27283  ? 343  ASN A OD1 1 
ATOM   2785 N  ND2 . ASN A 1 343 ? -31.80000 33.06700 23.79800  1.000 35.26331  ? 343  ASN A ND2 1 
ATOM   2786 N  N   . ILE A 1 344 ? -33.22500 30.69300 21.70100  1.000 32.79329  ? 344  ILE A N   1 
ATOM   2787 C  CA  . ILE A 1 344 ? -34.61800 31.11000 21.65500  1.000 37.14928  ? 344  ILE A CA  1 
ATOM   2788 C  C   . ILE A 1 344 ? -35.07100 31.41200 23.07700  1.000 34.09451  ? 344  ILE A C   1 
ATOM   2789 O  O   . ILE A 1 344 ? -34.43900 31.01300 24.06000  1.000 34.51556  ? 344  ILE A O   1 
ATOM   2790 C  CB  . ILE A 1 344 ? -35.53000 30.05800 20.98900  1.000 45.83903  ? 344  ILE A CB  1 
ATOM   2791 C  CG1 . ILE A 1 344 ? -35.43800 28.72000 21.72200  1.000 46.11216  ? 344  ILE A CG1 1 
ATOM   2792 C  CG2 . ILE A 1 344 ? -35.16400 29.88900 19.52100  1.000 36.00931  ? 344  ILE A CG2 1 
ATOM   2793 C  CD1 . ILE A 1 344 ? -36.27100 27.62300 21.09400  1.000 36.51227  ? 344  ILE A CD1 1 
ATOM   2794 N  N   . SER A 1 345 ? -36.18700 32.13100 23.18400  1.000 36.28447  ? 345  SER A N   1 
ATOM   2795 C  CA  . SER A 1 345 ? -36.63300 32.70400 24.45400  1.000 35.15192  ? 345  SER A CA  1 
ATOM   2796 C  C   . SER A 1 345 ? -38.08700 32.34000 24.71800  1.000 36.84881  ? 345  SER A C   1 
ATOM   2797 O  O   . SER A 1 345 ? -39.00300 33.08300 24.34100  1.000 42.00063  ? 345  SER A O   1 
ATOM   2798 C  CB  . SER A 1 345 ? -36.44800 34.22000 24.45400  1.000 36.02753  ? 345  SER A CB  1 
ATOM   2799 O  OG  . SER A 1 345 ? -35.14600 34.57100 24.01900  1.000 39.61312  ? 345  SER A OG  1 
ATOM   2800 N  N   . PRO A 1 346 ? -38.33800 31.20800 25.37000  1.000 36.45401  ? 346  PRO A N   1 
ATOM   2801 C  CA  . PRO A 1 346 ? -39.71300 30.87800 25.75900  1.000 37.08269  ? 346  PRO A CA  1 
ATOM   2802 C  C   . PRO A 1 346 ? -40.19600 31.78400 26.87800  1.000 37.87312  ? 346  PRO A C   1 
ATOM   2803 O  O   . PRO A 1 346 ? -39.41100 32.29100 27.68400  1.000 41.36214  ? 346  PRO A O   1 
ATOM   2804 C  CB  . PRO A 1 346 ? -39.61500 29.42200 26.23200  1.000 30.02348  ? 346  PRO A CB  1 
ATOM   2805 C  CG  . PRO A 1 346 ? -38.29000 28.92500 25.73500  1.000 27.27375  ? 346  PRO A CG  1 
ATOM   2806 C  CD  . PRO A 1 346 ? -37.39900 30.12400 25.69800  1.000 39.61359  ? 346  PRO A CD  1 
ATOM   2807 N  N   . THR A 1 347 ? -41.51400 31.92500 26.95900  1.000 41.23516  ? 347  THR A N   1 
ATOM   2808 C  CA  . THR A 1 347 ? -42.14400 32.73100 28.00800  1.000 39.78035  ? 347  THR A CA  1 
ATOM   2809 C  C   . THR A 1 347 ? -42.01800 32.02200 29.32500  1.000 47.34192  ? 347  THR A C   1 
ATOM   2810 O  O   . THR A 1 347 ? -41.73000 30.82000 29.32400  1.000 43.78164  ? 347  THR A O   1 
ATOM   2811 C  CB  . THR A 1 347 ? -43.61600 32.93500 27.66900  1.000 39.31989  ? 347  THR A CB  1 
ATOM   2812 O  OG1 . THR A 1 347 ? -44.19100 31.63700 27.61200  1.000 52.87141  ? 347  THR A OG1 1 
ATOM   2813 C  CG2 . THR A 1 347 ? -43.80700 33.66000 26.34900  1.000 47.95690  ? 347  THR A CG2 1 
ATOM   2814 N  N   . ALA A 1 348 ? -42.28600 32.74400 30.41000  1.000 48.74421  ? 348  ALA A N   1 
ATOM   2815 C  CA  . ALA A 1 348 ? -42.12700 32.16400 31.73800  1.000 51.78123  ? 348  ALA A CA  1 
ATOM   2816 C  C   . ALA A 1 348 ? -43.01000 30.93400 31.92100  1.000 42.39698  ? 348  ALA A C   1 
ATOM   2817 O  O   . ALA A 1 348 ? -42.64500 30.01500 32.67000  1.000 51.45390  ? 348  ALA A O   1 
ATOM   2818 C  CB  . ALA A 1 348 ? -42.43100 33.21900 32.80200  1.000 45.93045  ? 348  ALA A CB  1 
ATOM   2819 N  N   . VAL A 1 349 ? -44.13000 30.89000 31.20200  1.000 46.25510  ? 349  VAL A N   1 
ATOM   2820 C  CA  . VAL A 1 349 ? -45.08800 29.74900 31.28200  1.000 50.69091  ? 349  VAL A CA  1 
ATOM   2821 C  C   . VAL A 1 349 ? -44.71300 28.63900 30.28200  1.000 51.48642  ? 349  VAL A C   1 
ATOM   2822 O  O   . VAL A 1 349 ? -45.46500 27.66200 30.20300  1.000 45.95861  ? 349  VAL A O   1 
ATOM   2823 C  CB  . VAL A 1 349 ? -46.51600 30.26500 31.04700  1.000 43.27662  ? 349  VAL A CB  1 
ATOM   2824 C  CG1 . VAL A 1 349 ? -46.98200 31.18400 32.16600  1.000 40.36699  ? 349  VAL A CG1 1 
ATOM   2825 C  CG2 . VAL A 1 349 ? -46.68000 30.90700 29.68000  1.000 41.11398  ? 349  VAL A CG2 1 
ATOM   2826 N  N   . GLY A 1 350 ? -43.61500 28.78900 29.54300  1.000 48.96172  ? 350  GLY A N   1 
ATOM   2827 C  CA  . GLY A 1 350 ? -43.15000 27.74800 28.65600  1.000 54.09652  ? 350  GLY A CA  1 
ATOM   2828 C  C   . GLY A 1 350 ? -43.73200 27.77000 27.26300  1.000 50.50614  ? 350  GLY A C   1 
ATOM   2829 O  O   . GLY A 1 350 ? -43.79900 26.71700 26.62100  1.000 41.21980  ? 350  GLY A O   1 
ATOM   2830 N  N   . VAL A 1 351 ? -44.11600 28.94900 26.77900  1.000 46.85503  ? 351  VAL A N   1 
ATOM   2831 C  CA  . VAL A 1 351 ? -44.69300 29.08400 25.41400  1.000 42.28524  ? 351  VAL A CA  1 
ATOM   2832 C  C   . VAL A 1 351 ? -43.66900 29.77800 24.51200  1.000 47.94255  ? 351  VAL A C   1 
ATOM   2833 O  O   . VAL A 1 351 ? -43.08900 30.77000 24.95400  1.000 46.10363  ? 351  VAL A O   1 
ATOM   2834 C  CB  . VAL A 1 351 ? -46.03700 29.82500 25.42900  1.000 44.43884  ? 351  VAL A CB  1 
ATOM   2835 C  CG1 . VAL A 1 351 ? -46.51500 30.17000 24.02600  1.000 48.62641  ? 351  VAL A CG1 1 
ATOM   2836 C  CG2 . VAL A 1 351 ? -47.10400 29.05900 26.19500  1.000 49.08124  ? 351  VAL A CG2 1 
ATOM   2837 N  N   . LEU A 1 352 ? -43.44800 29.24000 23.31300  1.000 50.34863  ? 352  LEU A N   1 
ATOM   2838 C  CA  . LEU A 1 352 ? -42.54100 29.89100 22.33600  1.000 47.95026  ? 352  LEU A CA  1 
ATOM   2839 C  C   . LEU A 1 352 ? -43.39300 30.83800 21.47700  1.000 45.48843  ? 352  LEU A C   1 
ATOM   2840 O  O   . LEU A 1 352 ? -44.30700 30.36000 20.78800  1.000 41.80870  ? 352  LEU A O   1 
ATOM   2841 C  CB  . LEU A 1 352 ? -41.78200 28.85900 21.51300  1.000 40.71248  ? 352  LEU A CB  1 
ATOM   2842 C  CG  . LEU A 1 352 ? -40.42300 29.29300 20.96700  1.000 55.84787  ? 352  LEU A CG  1 
ATOM   2843 C  CD1 . LEU A 1 352 ? -39.54600 29.73000 22.12400  1.000 45.60740  ? 352  LEU A CD1 1 
ATOM   2844 C  CD2 . LEU A 1 352 ? -39.80300 28.10600 20.26100  1.000 50.56805  ? 352  LEU A CD2 1 
ATOM   2845 N  N   . PRO A 1 353 ? -43.16100 32.16500 21.54400  1.000 49.05801  ? 353  PRO A N   1 
ATOM   2846 C  CA  . PRO A 1 353 ? -43.96900 33.18400 20.79800  1.000 39.10250  ? 353  PRO A CA  1 
ATOM   2847 C  C   . PRO A 1 353 ? -43.97300 32.92600 19.29300  1.000 42.96021  ? 353  PRO A C   1 
ATOM   2848 O  O   . PRO A 1 353 ? -42.99500 32.36900 18.76100  1.000 40.90239  ? 353  PRO A O   1 
ATOM   2849 C  CB  . PRO A 1 353 ? -43.33000 34.49400 21.23900  1.000 44.58665  ? 353  PRO A CB  1 
ATOM   2850 C  CG  . PRO A 1 353 ? -42.70500 34.17700 22.57700  1.000 43.71713  ? 353  PRO A CG  1 
ATOM   2851 C  CD  . PRO A 1 353 ? -42.11400 32.83400 22.37000  1.000 35.55972  ? 353  PRO A CD  1 
ATOM   2852 N  N   . ASP A 1 354 ? -45.02800 33.35400 18.60200  1.000 47.38214  ? 354  ASP A N   1 
ATOM   2853 C  CA  . ASP A 1 354 ? -45.20700 33.04800 17.14800  1.000 49.74218  ? 354  ASP A CA  1 
ATOM   2854 C  C   . ASP A 1 354 ? -44.08100 33.60800 16.27400  1.000 41.01379  ? 354  ASP A C   1 
ATOM   2855 O  O   . ASP A 1 354 ? -43.77300 32.98200 15.25600  1.000 44.11212  ? 354  ASP A O   1 
ATOM   2856 C  CB  . ASP A 1 354 ? -46.59300 33.45700 16.68100  1.000 53.82668  ? 354  ASP A CB  1 
ATOM   2857 C  CG  . ASP A 1 354 ? -47.72600 32.57900 17.18500  1.000 64.93926  ? 354  ASP A CG  1 
ATOM   2858 O  OD1 . ASP A 1 354 ? -47.43000 31.59000 17.88300  1.000 50.09416  ? 354  ASP A OD1 1 
ATOM   2859 O  OD2 . ASP A 1 354 ? -48.89200 32.90500 16.89200  1.000 67.24563  ? 354  ASP A OD2 1 
ATOM   2860 N  N   . GLU A 1 355 ? -43.48600 34.73000 16.65500  1.000 37.88745  ? 355  GLU A N   1 
ATOM   2861 C  CA  . GLU A 1 355 ? -42.44500 35.30300 15.77000  1.000 38.11514  ? 355  GLU A CA  1 
ATOM   2862 C  C   . GLU A 1 355 ? -41.18500 34.43500 15.86000  1.000 42.33042  ? 355  GLU A C   1 
ATOM   2863 O  O   . GLU A 1 355 ? -40.50600 34.30000 14.84400  1.000 49.18232  ? 355  GLU A O   1 
ATOM   2864 C  CB  . GLU A 1 355 ? -42.21300 36.76900 16.12000  1.000 47.37371  ? 355  GLU A CB  1 
ATOM   2865 C  CG  . GLU A 1 355 ? -43.48700 37.59900 16.22300  1.000 51.71961  ? 355  GLU A CG  1 
ATOM   2866 C  CD  . GLU A 1 355 ? -43.20700 39.00800 16.70700  1.000 61.41722  ? 355  GLU A CD  1 
ATOM   2867 O  OE1 . GLU A 1 355 ? -42.37200 39.68700 16.07900  1.000 64.07258  ? 355  GLU A OE1 1 
ATOM   2868 O  OE2 . GLU A 1 355 ? -43.81600 39.42400 17.71100  1.000 61.29744  ? 355  GLU A OE2 1 
ATOM   2869 N  N   . GLN A 1 356 ? -40.88100 33.89400 17.03800  1.000 39.42247  ? 356  GLN A N   1 
ATOM   2870 C  CA  . GLN A 1 356 ? -39.76900 32.95800 17.16400  1.000 40.87063  ? 356  GLN A CA  1 
ATOM   2871 C  C   . GLN A 1 356 ? -40.05000 31.66900 16.40300  1.000 40.68839  ? 356  GLN A C   1 
ATOM   2872 O  O   . GLN A 1 356 ? -39.14900 31.10300 15.77100  1.000 39.59235  ? 356  GLN A O   1 
ATOM   2873 C  CB  . GLN A 1 356 ? -39.49400 32.66100 18.63800  1.000 41.66075  ? 356  GLN A CB  1 
ATOM   2874 C  CG  . GLN A 1 356 ? -39.44800 33.89500 19.52000  1.000 37.06830  ? 356  GLN A CG  1 
ATOM   2875 C  CD  . GLN A 1 356 ? -38.84700 33.61500 20.88400  1.000 40.00740  ? 356  GLN A CD  1 
ATOM   2876 O  OE1 . GLN A 1 356 ? -37.97500 32.75700 21.02600  1.000 42.39253  ? 356  GLN A OE1 1 
ATOM   2877 N  NE2 . GLN A 1 356 ? -39.31000 34.33900 21.89600  1.000 42.27511  ? 356  GLN A NE2 1 
ATOM   2878 N  N   . LEU A 1 357 ? -41.30400 31.23300 16.44200  1.000 45.00167  ? 357  LEU A N   1 
ATOM   2879 C  CA  . LEU A 1 357 ? -41.72100 30.02600 15.68100  1.000 47.86702  ? 357  LEU A CA  1 
ATOM   2880 C  C   . LEU A 1 357 ? -41.53100 30.27000 14.17300  1.000 40.32450  ? 357  LEU A C   1 
ATOM   2881 O  O   . LEU A 1 357 ? -41.01600 29.37800 13.49400  1.000 37.18522  ? 357  LEU A O   1 
ATOM   2882 C  CB  . LEU A 1 357 ? -43.16300 29.70300 16.06200  1.000 43.56503  ? 357  LEU A CB  1 
ATOM   2883 C  CG  . LEU A 1 357 ? -43.39200 29.17100 17.47700  1.000 47.83976  ? 357  LEU A CG  1 
ATOM   2884 C  CD1 . LEU A 1 357 ? -44.87100 28.94900 17.71000  1.000 39.87772  ? 357  LEU A CD1 1 
ATOM   2885 C  CD2 . LEU A 1 357 ? -42.62700 27.88000 17.67300  1.000 34.98154  ? 357  LEU A CD2 1 
ATOM   2886 N  N   . LYS A 1 358 ? -41.83900 31.46800 13.68300  1.000 39.65377  ? 358  LYS A N   1 
ATOM   2887 C  CA  . LYS A 1 358 ? -41.63500 31.77600 12.24800  1.000 43.78799  ? 358  LYS A CA  1 
ATOM   2888 C  C   . LYS A 1 358 ? -40.14300 31.81300 11.89900  1.000 42.24512  ? 358  LYS A C   1 
ATOM   2889 O  O   . LYS A 1 358 ? -39.77000 31.26200 10.86600  1.000 46.79792  ? 358  LYS A O   1 
ATOM   2890 C  CB  . LYS A 1 358 ? -42.34500 33.07800 11.86800  1.000 47.44673  ? 358  LYS A CB  1 
ATOM   2891 C  CG  . LYS A 1 358 ? -42.27600 33.46500 10.39800  1.000 56.72121  ? 358  LYS A CG  1 
ATOM   2892 C  CD  . LYS A 1 358 ? -42.71300 32.36100 9.46500   1.000 64.05770  ? 358  LYS A CD  1 
ATOM   2893 C  CE  . LYS A 1 358 ? -43.19600 32.86900 8.12400   1.000 59.06377  ? 358  LYS A CE  1 
ATOM   2894 N  NZ  . LYS A 1 358 ? -42.25300 33.84700 7.53300   1.000 66.03627  ? 358  LYS A NZ  1 
ATOM   2895 N  N   . VAL A 1 359 ? -39.32000 32.40900 12.75300  1.000 39.70474  ? 359  VAL A N   1 
ATOM   2896 C  CA  . VAL A 1 359 ? -37.85500 32.43000 12.45900  1.000 38.38255  ? 359  VAL A CA  1 
ATOM   2897 C  C   . VAL A 1 359 ? -37.39200 30.97000 12.37300  1.000 43.51056  ? 359  VAL A C   1 
ATOM   2898 O  O   . VAL A 1 359 ? -36.68500 30.62800 11.42500  1.000 38.07823  ? 359  VAL A O   1 
ATOM   2899 C  CB  . VAL A 1 359 ? -37.01500 33.19200 13.50200  1.000 40.31260  ? 359  VAL A CB  1 
ATOM   2900 C  CG1 . VAL A 1 359 ? -35.52100 32.97900 13.31200  1.000 31.35887  ? 359  VAL A CG1 1 
ATOM   2901 C  CG2 . VAL A 1 359 ? -37.35300 34.67700 13.52500  1.000 39.99148  ? 359  VAL A CG2 1 
ATOM   2902 N  N   . LEU A 1 360 ? -37.77700 30.17000 13.36700  1.000 42.68925  ? 360  LEU A N   1 
ATOM   2903 C  CA  . LEU A 1 360 ? -37.32900 28.78200 13.35200  1.000 31.29928  ? 360  LEU A CA  1 
ATOM   2904 C  C   . LEU A 1 360 ? -37.82300 28.05500 12.10900  1.000 41.28870  ? 360  LEU A C   1 
ATOM   2905 O  O   . LEU A 1 360 ? -37.08500 27.26200 11.51400  1.000 41.00731  ? 360  LEU A O   1 
ATOM   2906 C  CB  . LEU A 1 360 ? -37.79700 28.06100 14.61700  1.000 40.56327  ? 360  LEU A CB  1 
ATOM   2907 C  CG  . LEU A 1 360 ? -37.08600 28.41800 15.92400  1.000 38.79367  ? 360  LEU A CG  1 
ATOM   2908 C  CD1 . LEU A 1 360 ? -37.71300 27.68000 17.09800  1.000 37.79298  ? 360  LEU A CD1 1 
ATOM   2909 C  CD2 . LEU A 1 360 ? -35.59900 28.10900 15.82800  1.000 33.21518  ? 360  LEU A CD2 1 
ATOM   2910 N  N   . GLN A 1 361 ? -39.04600 28.32300 11.66100  1.000 43.69720  ? 361  GLN A N   1 
ATOM   2911 C  CA  . GLN A 1 361 ? -39.60100 27.58100 10.49700  1.000 40.07681  ? 361  GLN A CA  1 
ATOM   2912 C  C   . GLN A 1 361 ? -38.96800 28.08500 9.20000   1.000 44.58007  ? 361  GLN A C   1 
ATOM   2913 O  O   . GLN A 1 361 ? -38.79700 27.28100 8.29100   1.000 44.16793  ? 361  GLN A O   1 
ATOM   2914 C  CB  . GLN A 1 361 ? -41.11600 27.69300 10.42000  1.000 39.27280  ? 361  GLN A CB  1 
ATOM   2915 C  CG  . GLN A 1 361 ? -41.73900 26.67400 9.48100   1.000 46.75208  ? 361  GLN A CG  1 
ATOM   2916 C  CD  . GLN A 1 361 ? -41.39200 25.26100 9.88000   1.000 58.14615  ? 361  GLN A CD  1 
ATOM   2917 O  OE1 . GLN A 1 361 ? -41.79200 24.77700 10.93500  1.000 51.37940  ? 361  GLN A OE1 1 
ATOM   2918 N  NE2 . GLN A 1 361 ? -40.64000 24.58600 9.02900   1.000 46.87904  ? 361  GLN A NE2 1 
ATOM   2919 N  N   . ASP A 1 362 ? -38.61400 29.36700 9.14700   1.000 44.23964  ? 362  ASP A N   1 
ATOM   2920 C  CA  . ASP A 1 362 ? -37.91200 29.87800 7.93900   1.000 40.86733  ? 362  ASP A CA  1 
ATOM   2921 C  C   . ASP A 1 362 ? -36.52600 29.24000 7.88000   1.000 38.28991  ? 362  ASP A C   1 
ATOM   2922 O  O   . ASP A 1 362 ? -36.13200 28.79800 6.79900   1.000 46.49152  ? 362  ASP A O   1 
ATOM   2923 C  CB  . ASP A 1 362 ? -37.91600 31.39900 7.88100   1.000 40.66042  ? 362  ASP A CB  1 
ATOM   2924 C  CG  . ASP A 1 362 ? -39.28000 32.05400 7.73500   1.000 42.62513  ? 362  ASP A CG  1 
ATOM   2925 O  OD1 . ASP A 1 362 ? -40.16900 31.42900 7.13200   1.000 57.75483  ? 362  ASP A OD1 1 
ATOM   2926 O  OD2 . ASP A 1 362 ? -39.44100 33.17900 8.23200   1.000 42.51424  ? 362  ASP A OD2 1 
ATOM   2927 N  N   . ILE A 1 363 ? -35.82000 29.20200 9.00300   1.000 37.63658  ? 363  ILE A N   1 
ATOM   2928 C  CA  . ILE A 1 363 ? -34.52800 28.52200 9.05600   1.000 39.55681  ? 363  ILE A CA  1 
ATOM   2929 C  C   . ILE A 1 363 ? -34.68200 27.06100 8.65100   1.000 38.92022  ? 363  ILE A C   1 
ATOM   2930 O  O   . ILE A 1 363 ? -33.85200 26.51200 7.91600   1.000 35.58849  ? 363  ILE A O   1 
ATOM   2931 C  CB  . ILE A 1 363 ? -33.91100 28.65700 10.46100  1.000 36.49723  ? 363  ILE A CB  1 
ATOM   2932 C  CG1 . ILE A 1 363 ? -33.58900 30.12100 10.76700  1.000 40.16572  ? 363  ILE A CG1 1 
ATOM   2933 C  CG2 . ILE A 1 363 ? -32.66700 27.79400 10.58600  1.000 31.61694  ? 363  ILE A CG2 1 
ATOM   2934 C  CD1 . ILE A 1 363 ? -33.04800 30.34200 12.16100  1.000 32.45612  ? 363  ILE A CD1 1 
ATOM   2935 N  N   . GLY A 1 364 ? -35.75300 26.41500 9.11600   1.000 44.92216  ? 364  GLY A N   1 
ATOM   2936 C  CA  . GLY A 1 364 ? -35.96700 25.01900 8.78100   1.000 41.05878  ? 364  GLY A CA  1 
ATOM   2937 C  C   . GLY A 1 364 ? -36.27800 24.80700 7.31400   1.000 41.90049  ? 364  GLY A C   1 
ATOM   2938 O  O   . GLY A 1 364 ? -35.85100 23.81600 6.72200   1.000 42.22666  ? 364  GLY A O   1 
ATOM   2939 N  N   . ASP A 1 365 ? -37.03600 25.72400 6.71100   1.000 40.58197  ? 365  ASP A N   1 
ATOM   2940 C  CA  . ASP A 1 365 ? -37.26000 25.66800 5.27100   1.000 41.15450  ? 365  ASP A CA  1 
ATOM   2941 C  C   . ASP A 1 365 ? -35.93700 25.71500 4.52100   1.000 38.93990  ? 365  ASP A C   1 
ATOM   2942 O  O   . ASP A 1 365 ? -35.63900 24.83400 3.70000   1.000 56.12311  ? 365  ASP A O   1 
ATOM   2943 C  CB  . ASP A 1 365 ? -38.16800 26.81800 4.83300   1.000 36.17117  ? 365  ASP A CB  1 
ATOM   2944 C  CG  . ASP A 1 365 ? -39.58900 26.67000 5.34200   1.000 46.19232  ? 365  ASP A CG  1 
ATOM   2945 O  OD1 . ASP A 1 365 ? -39.91500 25.60300 5.90200   1.000 47.76440  ? 365  ASP A OD1 1 
ATOM   2946 O  OD2 . ASP A 1 365 ? -40.38100 27.62300 5.18300   1.000 37.73066  ? 365  ASP A OD2 1 
ATOM   2947 N  N   . PHE A 1 366 ? -35.09700 26.68900 4.81500   1.000 40.29545  ? 366  PHE A N   1 
ATOM   2948 C  CA  . PHE A 1 366 ? -33.80800 26.81900 4.09300   1.000 41.10568  ? 366  PHE A CA  1 
ATOM   2949 C  C   . PHE A 1 366 ? -32.95600 25.56800 4.31200   1.000 41.61629  ? 366  PHE A C   1 
ATOM   2950 O  O   . PHE A 1 366 ? -32.35100 25.09000 3.34900   1.000 39.84294  ? 366  PHE A O   1 
ATOM   2951 C  CB  . PHE A 1 366 ? -33.02100 28.07900 4.47200   1.000 30.26107  ? 366  PHE A CB  1 
ATOM   2952 C  CG  . PHE A 1 366 ? -31.67600 28.23200 3.78100   1.000 37.35350  ? 366  PHE A CG  1 
ATOM   2953 C  CD1 . PHE A 1 366 ? -31.57300 28.89100 2.56400   1.000 34.39919  ? 366  PHE A CD1 1 
ATOM   2954 C  CD2 . PHE A 1 366 ? -30.51800 27.72000 4.35000   1.000 35.83825  ? 366  PHE A CD2 1 
ATOM   2955 C  CE1 . PHE A 1 366 ? -30.34900 29.02600 1.93500   1.000 38.52001  ? 366  PHE A CE1 1 
ATOM   2956 C  CE2 . PHE A 1 366 ? -29.29700 27.85900 3.71500   1.000 38.74534  ? 366  PHE A CE2 1 
ATOM   2957 C  CZ  . PHE A 1 366 ? -29.21500 28.51100 2.51100   1.000 40.05308  ? 366  PHE A CZ  1 
ATOM   2958 N  N   . LEU A 1 367 ? -32.90800 25.04900 5.54000   1.000 39.37254  ? 367  LEU A N   1 
ATOM   2959 C  CA  . LEU A 1 367 ? -31.96200 23.92000 5.77800   1.000 39.38330  ? 367  LEU A CA  1 
ATOM   2960 C  C   . LEU A 1 367 ? -32.49200 22.59900 5.17500   1.000 41.83879  ? 367  LEU A C   1 
ATOM   2961 O  O   . LEU A 1 367 ? -31.69800 21.86700 4.59100   1.000 37.34996  ? 367  LEU A O   1 
ATOM   2962 C  CB  . LEU A 1 367 ? -31.63100 23.82000 7.26700   1.000 39.17270  ? 367  LEU A CB  1 
ATOM   2963 C  CG  . LEU A 1 367 ? -30.72900 24.91400 7.84000   1.000 35.80239  ? 367  LEU A CG  1 
ATOM   2964 C  CD1 . LEU A 1 367 ? -30.61400 24.73700 9.33600   1.000 31.53550  ? 367  LEU A CD1 1 
ATOM   2965 C  CD2 . LEU A 1 367 ? -29.36400 24.82900 7.19600   1.000 35.21615  ? 367  LEU A CD2 1 
ATOM   2966 N  N   . GLY A 1 368 ? -33.79200 22.35600 5.27600   1.000 39.76314  ? 368  GLY A N   1 
ATOM   2967 C  CA  . GLY A 1 368 ? -34.40200 21.15800 4.68000   1.000 43.60609  ? 368  GLY A CA  1 
ATOM   2968 C  C   . GLY A 1 368 ? -34.25200 21.15400 3.17400   1.000 48.18720  ? 368  GLY A C   1 
ATOM   2969 O  O   . GLY A 1 368 ? -34.21700 20.06300 2.59400   1.000 48.45992  ? 368  GLY A O   1 
ATOM   2970 N  N   . ARG A 1 369 ? -34.10200 22.33200 2.57500   1.000 40.42705  ? 369  ARG A N   1 
ATOM   2971 C  CA  . ARG A 1 369 ? -33.96400 22.44200 1.10700   1.000 39.07193  ? 369  ARG A CA  1 
ATOM   2972 C  C   . ARG A 1 369 ? -32.49300 22.42900 0.69900   1.000 45.89595  ? 369  ARG A C   1 
ATOM   2973 O  O   . ARG A 1 369 ? -32.19400 21.84300 -0.34600  1.000 43.46304  ? 369  ARG A O   1 
ATOM   2974 C  CB  . ARG A 1 369 ? -34.67400 23.71200 0.62600   1.000 33.00093  ? 369  ARG A CB  1 
ATOM   2975 C  CG  . ARG A 1 369 ? -34.64500 24.03300 -0.85900  1.000 45.56897  ? 369  ARG A CG  1 
ATOM   2976 C  CD  . ARG A 1 369 ? -35.49900 25.26000 -1.12600  1.000 40.01130  ? 369  ARG A CD  1 
ATOM   2977 N  NE  . ARG A 1 369 ? -35.39500 25.71200 -2.51500  1.000 40.88900  ? 369  ARG A NE  1 
ATOM   2978 C  CZ  . ARG A 1 369 ? -36.01800 26.76800 -3.00500  1.000 42.15003  ? 369  ARG A CZ  1 
ATOM   2979 N  NH1 . ARG A 1 369 ? -36.86600 27.44200 -2.25600  1.000 43.10322  ? 369  ARG A NH1 1 
ATOM   2980 N  NH2 . ARG A 1 369 ? -35.77900 27.15100 -4.24100  1.000 50.89184  ? 369  ARG A NH2 1 
ATOM   2981 N  N   . TYR A 1 370 ? -31.60900 23.05000 1.48300   1.000 36.38258  ? 370  TYR A N   1 
ATOM   2982 C  CA  . TYR A 1 370 ? -30.21500 23.11900 0.97100   1.000 36.90840  ? 370  TYR A CA  1 
ATOM   2983 C  C   . TYR A 1 370 ? -29.18300 22.49200 1.93700   1.000 34.19703  ? 370  TYR A C   1 
ATOM   2984 O  O   . TYR A 1 370 ? -28.01100 22.84400 1.82600   1.000 39.30324  ? 370  TYR A O   1 
ATOM   2985 C  CB  . TYR A 1 370 ? -29.87500 24.56600 0.61100   1.000 33.91514  ? 370  TYR A CB  1 
ATOM   2986 C  CG  . TYR A 1 370 ? -30.78800 25.32200 -0.34300  1.000 43.17748  ? 370  TYR A CG  1 
ATOM   2987 C  CD1 . TYR A 1 370 ? -30.63800 25.19600 -1.71500  1.000 49.52241  ? 370  TYR A CD1 1 
ATOM   2988 C  CD2 . TYR A 1 370 ? -31.71500 26.24600 0.12200   1.000 39.69180  ? 370  TYR A CD2 1 
ATOM   2989 C  CE1 . TYR A 1 370 ? -31.43200 25.90500 -2.59700  1.000 46.51439  ? 370  TYR A CE1 1 
ATOM   2990 C  CE2 . TYR A 1 370 ? -32.50800 26.97300 -0.75000  1.000 42.79320  ? 370  TYR A CE2 1 
ATOM   2991 C  CZ  . TYR A 1 370 ? -32.36600 26.80100 -2.11400  1.000 45.59888  ? 370  TYR A CZ  1 
ATOM   2992 O  OH  . TYR A 1 370 ? -33.13200 27.49500 -3.00100  1.000 43.54406  ? 370  TYR A OH  1 
ATOM   2993 N  N   . GLY A 1 371 ? -29.58400 21.58400 2.81800   1.000 35.15929  ? 371  GLY A N   1 
ATOM   2994 C  CA  . GLY A 1 371 ? -28.67500 20.92300 3.77600   1.000 33.14908  ? 371  GLY A CA  1 
ATOM   2995 C  C   . GLY A 1 371 ? -27.40300 20.39400 3.16500   1.000 33.38535  ? 371  GLY A C   1 
ATOM   2996 O  O   . GLY A 1 371 ? -26.37000 20.45000 3.82300   1.000 41.14856  ? 371  GLY A O   1 
ATOM   2997 N  N   . GLU A 1 372 ? -27.48000 19.87300 1.95700   1.000 39.26611  ? 372  GLU A N   1 
ATOM   2998 C  CA  . GLU A 1 372 ? -26.29500 19.31600 1.26900   1.000 44.03374  ? 372  GLU A CA  1 
ATOM   2999 C  C   . GLU A 1 372 ? -25.17100 20.35000 1.27000   1.000 38.23908  ? 372  GLU A C   1 
ATOM   3000 O  O   . GLU A 1 372 ? -24.00600 19.95900 1.36200   1.000 38.86266  ? 372  GLU A O   1 
ATOM   3001 C  CB  . GLU A 1 372 ? -26.71800 18.94100 -0.14400  1.000 40.59684  ? 372  GLU A CB  1 
ATOM   3002 C  CG  . GLU A 1 372 ? -25.56200 18.55900 -1.05900  1.000 50.55391  ? 372  GLU A CG  1 
ATOM   3003 C  CD  . GLU A 1 372 ? -26.02000 18.39100 -2.49300  1.000 54.58293  ? 372  GLU A CD  1 
ATOM   3004 O  OE1 . GLU A 1 372 ? -27.21900 18.59200 -2.76500  1.000 40.15343  ? 372  GLU A OE1 1 
ATOM   3005 O  OE2 . GLU A 1 372 ? -25.17200 18.05100 -3.33200  1.000 56.29957  ? 372  GLU A OE2 1 
ATOM   3006 N  N   . SER A 1 373 ? -25.52500 21.63200 1.20900   1.000 33.77395  ? 373  SER A N   1 
ATOM   3007 C  CA  . SER A 1 373 ? -24.52700 22.73000 1.10900   1.000 43.22478  ? 373  SER A CA  1 
ATOM   3008 C  C   . SER A 1 373 ? -23.95100 23.09600 2.47600   1.000 47.93381  ? 373  SER A C   1 
ATOM   3009 O  O   . SER A 1 373 ? -22.83600 23.61400 2.50800   1.000 49.10825  ? 373  SER A O   1 
ATOM   3010 C  CB  . SER A 1 373 ? -25.15600 23.93500 0.47100   1.000 31.55433  ? 373  SER A CB  1 
ATOM   3011 O  OG  . SER A 1 373 ? -26.22000 24.44200 1.25200   1.000 48.91668  ? 373  SER A OG  1 
ATOM   3012 N  N   . VAL A 1 374 ? -24.69800 22.84600 3.54300   1.000 43.40391  ? 374  VAL A N   1 
ATOM   3013 C  CA  . VAL A 1 374 ? -24.27100 23.25200 4.90900   1.000 40.26162  ? 374  VAL A CA  1 
ATOM   3014 C  C   . VAL A 1 374 ? -23.76000 22.03500 5.68300   1.000 39.12231  ? 374  VAL A C   1 
ATOM   3015 O  O   . VAL A 1 374 ? -22.57200 22.00600 5.98300   1.000 46.90034  ? 374  VAL A O   1 
ATOM   3016 C  CB  . VAL A 1 374 ? -25.46100 23.91200 5.62400   1.000 34.30888  ? 374  VAL A CB  1 
ATOM   3017 C  CG1 . VAL A 1 374 ? -25.19100 24.15900 7.09500   1.000 43.61664  ? 374  VAL A CG1 1 
ATOM   3018 C  CG2 . VAL A 1 374 ? -25.91200 25.18000 4.92200   1.000 37.17570  ? 374  VAL A CG2 1 
ATOM   3019 N  N   . PHE A 1 375 ? -24.60900 21.04300 5.91700   1.000 37.92610  ? 375  PHE A N   1 
ATOM   3020 C  CA  . PHE A 1 375 ? -24.24200 19.89100 6.77800   1.000 33.03052  ? 375  PHE A CA  1 
ATOM   3021 C  C   . PHE A 1 375 ? -23.17000 19.00100 6.15300   1.000 35.04347  ? 375  PHE A C   1 
ATOM   3022 O  O   . PHE A 1 375 ? -23.21400 18.76800 4.95200   1.000 42.47389  ? 375  PHE A O   1 
ATOM   3023 C  CB  . PHE A 1 375 ? -25.49100 19.09800 7.14200   1.000 32.36302  ? 375  PHE A CB  1 
ATOM   3024 C  CG  . PHE A 1 375 ? -26.61600 19.87600 7.76700   1.000 33.74204  ? 375  PHE A CG  1 
ATOM   3025 C  CD1 . PHE A 1 375 ? -26.48500 20.42600 9.02900   1.000 33.30414  ? 375  PHE A CD1 1 
ATOM   3026 C  CD2 . PHE A 1 375 ? -27.82300 20.02300 7.10700   1.000 31.02780  ? 375  PHE A CD2 1 
ATOM   3027 C  CE1 . PHE A 1 375 ? -27.53100 21.12300 9.60700   1.000 40.75037  ? 375  PHE A CE1 1 
ATOM   3028 C  CE2 . PHE A 1 375 ? -28.86700 20.72200 7.68600   1.000 36.51194  ? 375  PHE A CE2 1 
ATOM   3029 C  CZ  . PHE A 1 375 ? -28.72000 21.27100 8.93600   1.000 38.51267  ? 375  PHE A CZ  1 
ATOM   3030 N  N   . SER A 1 376 ? -22.23400 18.52500 6.97000   1.000 39.51647  ? 376  SER A N   1 
ATOM   3031 C  CA  . SER A 1 376 ? -21.13200 17.62400 6.52700   1.000 42.07283  ? 376  SER A CA  1 
ATOM   3032 C  C   . SER A 1 376 ? -20.21600 18.32500 5.52400   1.000 40.98800  ? 376  SER A C   1 
ATOM   3033 O  O   . SER A 1 376 ? -19.42700 17.63900 4.88100   1.000 44.78484  ? 376  SER A O   1 
ATOM   3034 C  CB  . SER A 1 376 ? -21.64600 16.28700 6.06400   1.000 31.74079  ? 376  SER A CB  1 
ATOM   3035 O  OG  . SER A 1 376 ? -22.33800 15.62600 7.10600   1.000 36.76992  ? 376  SER A OG  1 
ATOM   3036 N  N   . THR A 1 377 ? -20.29700 19.64600 5.43900   1.000 35.53087  ? 377  THR A N   1 
ATOM   3037 C  CA  . THR A 1 377 ? -19.39200 20.40800 4.59400   1.000 39.05742  ? 377  THR A CA  1 
ATOM   3038 C  C   . THR A 1 377 ? -18.28500 21.02200 5.44100   1.000 41.21283  ? 377  THR A C   1 
ATOM   3039 O  O   . THR A 1 377 ? -18.38200 21.10900 6.66700   1.000 38.23040  ? 377  THR A O   1 
ATOM   3040 C  CB  . THR A 1 377 ? -20.13900 21.51000 3.83300   1.000 40.44744  ? 377  THR A CB  1 
ATOM   3041 O  OG1 . THR A 1 377 ? -20.65800 22.47000 4.76100   1.000 42.40419  ? 377  THR A OG1 1 
ATOM   3042 C  CG2 . THR A 1 377 ? -21.28600 20.92200 3.02400   1.000 36.19432  ? 377  THR A CG2 1 
ATOM   3043 N  N   . ARG A 1 378 ? -17.21800 21.44300 4.77000   1.000 41.18239  ? 378  ARG A N   1 
ATOM   3044 C  CA  . ARG A 1 378 ? -16.09900 22.10300 5.42100   1.000 34.98611  ? 378  ARG A CA  1 
ATOM   3045 C  C   . ARG A 1 378 ? -15.88200 23.47600 4.80400   1.000 43.56499  ? 378  ARG A C   1 
ATOM   3046 O  O   . ARG A 1 378 ? -16.33700 23.76300 3.69400   1.000 48.49695  ? 378  ARG A O   1 
ATOM   3047 C  CB  . ARG A 1 378 ? -14.81200 21.27400 5.30900   1.000 36.07641  ? 378  ARG A CB  1 
ATOM   3048 C  CG  . ARG A 1 378 ? -14.83000 19.98500 6.11000   1.000 37.90501  ? 378  ARG A CG  1 
ATOM   3049 C  CD  . ARG A 1 378 ? -14.95400 20.26300 7.60100   1.000 39.02045  ? 378  ARG A CD  1 
ATOM   3050 N  NE  . ARG A 1 378 ? -15.00600 19.03300 8.38200   1.000 41.92598  ? 378  ARG A NE  1 
ATOM   3051 C  CZ  . ARG A 1 378 ? -16.11700 18.35900 8.64500   1.000 42.31819  ? 378  ARG A CZ  1 
ATOM   3052 N  NH1 . ARG A 1 378 ? -17.29500 18.76800 8.20000   1.000 38.05712  ? 378  ARG A NH1 1 
ATOM   3053 N  NH2 . ARG A 1 378 ? -16.04600 17.24800 9.37200   1.000 42.33520  ? 378  ARG A NH2 1 
ATOM   3054 N  N   . ALA A 1 379 ? -15.17700 24.32700 5.54300   1.000 48.00268  ? 379  ALA A N   1 
ATOM   3055 C  CA  . ALA A 1 379 ? -14.86000 25.65300 5.03900   1.000 41.50885  ? 379  ALA A CA  1 
ATOM   3056 C  C   . ALA A 1 379 ? -13.81200 25.56500 3.93800   1.000 44.93398  ? 379  ALA A C   1 
ATOM   3057 O  O   . ALA A 1 379 ? -12.84900 24.79900 4.03200   1.000 63.69752  ? 379  ALA A O   1 
ATOM   3058 C  CB  . ALA A 1 379 ? -14.35900 26.55000 6.16900   1.000 32.62875  ? 379  ALA A CB  1 
ATOM   3059 N  N   . TRP A 1 380 ? -13.96800 26.38300 2.90800   1.000 47.13278  ? 380  TRP A N   1 
ATOM   3060 C  CA  . TRP A 1 380 ? -12.94200 26.42900 1.84700   1.000 45.88970  ? 380  TRP A CA  1 
ATOM   3061 C  C   . TRP A 1 380 ? -11.79000 27.30000 2.33800   1.000 48.93377  ? 380  TRP A C   1 
ATOM   3062 O  O   . TRP A 1 380 ? -11.81400 27.74200 3.48800   1.000 50.23696  ? 380  TRP A O   1 
ATOM   3063 C  CB  . TRP A 1 380 ? -13.56600 26.97400 0.56000   1.000 51.64624  ? 380  TRP A CB  1 
ATOM   3064 C  CG  . TRP A 1 380 ? -12.81400 26.70700 -0.71500  1.000 53.99501  ? 380  TRP A CG  1 
ATOM   3065 C  CD1 . TRP A 1 380 ? -12.02400 25.63800 -1.00900  1.000 61.15036  ? 380  TRP A CD1 1 
ATOM   3066 C  CD2 . TRP A 1 380 ? -12.81000 27.54300 -1.89100  1.000 61.39281  ? 380  TRP A CD2 1 
ATOM   3067 N  NE1 . TRP A 1 380 ? -11.51800 25.75500 -2.27600  1.000 56.92617  ? 380  TRP A NE1 1 
ATOM   3068 C  CE2 . TRP A 1 380 ? -11.98500 26.90900 -2.84200  1.000 59.68006  ? 380  TRP A CE2 1 
ATOM   3069 C  CE3 . TRP A 1 380 ? -13.41900 28.75500 -2.22800  1.000 50.59407  ? 380  TRP A CE3 1 
ATOM   3070 C  CZ2 . TRP A 1 380 ? -11.75400 27.45200 -4.10300  1.000 61.90391  ? 380  TRP A CZ2 1 
ATOM   3071 C  CZ3 . TRP A 1 380 ? -13.19200 29.28700 -3.47500  1.000 51.42077  ? 380  TRP A CZ3 1 
ATOM   3072 C  CH2 . TRP A 1 380 ? -12.37100 28.64500 -4.39700  1.000 54.32742  ? 380  TRP A CH2 1 
ATOM   3073 N  N   . ASP A 1 381 ? -10.81800 27.54500 1.47700   1.000 44.07355  ? 381  ASP A N   1 
ATOM   3074 C  CA  . ASP A 1 381 ? -9.68000  28.42200 1.83800   1.000 53.39484  ? 381  ASP A CA  1 
ATOM   3075 C  C   . ASP A 1 381 ? -10.08800 29.89100 1.64700   1.000 51.64402  ? 381  ASP A C   1 
ATOM   3076 O  O   . ASP A 1 381 ? -9.37300  30.75700 2.17300   1.000 53.80294  ? 381  ASP A O   1 
ATOM   3077 C  CB  . ASP A 1 381 ? -8.44100  27.95400 1.09500   1.000 62.75890  ? 381  ASP A CB  1 
ATOM   3078 C  CG  . ASP A 1 381 ? -7.89300  26.60500 1.52500   1.000 68.71629  ? 381  ASP A CG  1 
ATOM   3079 O  OD1 . ASP A 1 381 ? -8.43900  26.02400 2.48200   1.000 68.43932  ? 381  ASP A OD1 1 
ATOM   3080 O  OD2 . ASP A 1 381 ? -6.94800  26.13600 0.87200   1.000 76.66192  ? 381  ASP A OD2 1 
ATOM   3081 N  N   . ILE A 1 382 ? -11.18500 30.16200 0.93000   1.000 51.25341  ? 382  ILE A N   1 
ATOM   3082 C  CA  . ILE A 1 382 ? -11.69600 31.51800 0.75800   1.000 45.73105  ? 382  ILE A CA  1 
ATOM   3083 C  C   . ILE A 1 382 ? -13.15800 31.50300 1.18200   1.000 39.28357  ? 382  ILE A C   1 
ATOM   3084 O  O   . ILE A 1 382 ? -13.96300 30.75600 0.61100   1.000 46.66464  ? 382  ILE A O   1 
ATOM   3085 C  CB  . ILE A 1 382 ? -11.54500 32.00500 -0.69200  1.000 42.04143  ? 382  ILE A CB  1 
ATOM   3086 C  CG1 . ILE A 1 382 ? -10.09300 31.85900 -1.15000  1.000 47.43838  ? 382  ILE A CG1 1 
ATOM   3087 C  CG2 . ILE A 1 382 ? -11.99900 33.44700 -0.81900  1.000 44.01737  ? 382  ILE A CG2 1 
ATOM   3088 C  CD1 . ILE A 1 382 ? -9.86700  32.19900 -2.60300  1.000 53.45651  ? 382  ILE A CD1 1 
ATOM   3089 N  N   . TYR A 1 383 ? -13.50400 32.31900 2.18200   1.000 47.67445  ? 383  TYR A N   1 
ATOM   3090 C  CA  . TYR A 1 383 ? -14.82100 32.17600 2.79500   1.000 44.92875  ? 383  TYR A CA  1 
ATOM   3091 C  C   . TYR A 1 383 ? -15.93100 32.70900 1.89900   1.000 44.96943  ? 383  TYR A C   1 
ATOM   3092 O  O   . TYR A 1 383 ? -17.05000 32.18200 1.92400   1.000 45.18942  ? 383  TYR A O   1 
ATOM   3093 C  CB  . TYR A 1 383 ? -14.85000 32.85300 4.17100   1.000 45.39903  ? 383  TYR A CB  1 
ATOM   3094 C  CG  . TYR A 1 383 ? -14.99700 34.36200 4.18100   1.000 44.98493  ? 383  TYR A CG  1 
ATOM   3095 C  CD1 . TYR A 1 383 ? -16.25200 34.96100 4.15200   1.000 41.92364  ? 383  TYR A CD1 1 
ATOM   3096 C  CD2 . TYR A 1 383 ? -13.88300 35.18700 4.26000   1.000 47.60525  ? 383  TYR A CD2 1 
ATOM   3097 C  CE1 . TYR A 1 383 ? -16.38900 36.33400 4.17200   1.000 45.87578  ? 383  TYR A CE1 1 
ATOM   3098 C  CE2 . TYR A 1 383 ? -14.01100 36.56200 4.28500   1.000 52.04581  ? 383  TYR A CE2 1 
ATOM   3099 C  CZ  . TYR A 1 383 ? -15.26700 37.13000 4.24100   1.000 49.23628  ? 383  TYR A CZ  1 
ATOM   3100 O  OH  . TYR A 1 383 ? -15.40100 38.49900 4.26600   1.000 63.04233  ? 383  TYR A OH  1 
ATOM   3101 N  N   . GLY A 1 384 ? -15.59100 33.70200 1.09300   1.000 44.90992  ? 384  GLY A N   1 
ATOM   3102 C  CA  . GLY A 1 384 ? -16.63100 34.31200 0.25900   1.000 43.50531  ? 384  GLY A CA  1 
ATOM   3103 C  C   . GLY A 1 384 ? -16.17000 35.46900 -0.59000  1.000 40.81435  ? 384  GLY A C   1 
ATOM   3104 O  O   . GLY A 1 384 ? -14.98100 35.79700 -0.56800  1.000 41.19657  ? 384  GLY A O   1 
ATOM   3105 N  N   . GLU A 1 385 ? -17.10700 36.04000 -1.33400  1.000 45.45448  ? 385  GLU A N   1 
ATOM   3106 C  CA  . GLU A 1 385 ? -16.83100 37.19500 -2.21100  1.000 46.41364  ? 385  GLU A CA  1 
ATOM   3107 C  C   . GLU A 1 385 ? -18.04800 38.10700 -2.07300  1.000 44.23231  ? 385  GLU A C   1 
ATOM   3108 O  O   . GLU A 1 385 ? -19.13100 37.59700 -1.78000  1.000 47.20828  ? 385  GLU A O   1 
ATOM   3109 C  CB  . GLU A 1 385 ? -16.61200 36.71800 -3.64100  1.000 40.01731  ? 385  GLU A CB  1 
ATOM   3110 C  CG  . GLU A 1 385 ? -15.37900 35.87200 -3.85500  1.000 45.50629  ? 385  GLU A CG  1 
ATOM   3111 C  CD  . GLU A 1 385 ? -15.24800 35.43500 -5.30000  1.000 55.54672  ? 385  GLU A CD  1 
ATOM   3112 O  OE1 . GLU A 1 385 ? -16.09600 35.84500 -6.10800  1.000 57.20008  ? 385  GLU A OE1 1 
ATOM   3113 O  OE2 . GLU A 1 385 ? -14.30500 34.69500 -5.61200  1.000 66.94284  ? 385  GLU A OE2 1 
ATOM   3114 N  N   . GLY A 1 386 ? -17.86700 39.41200 -2.20900  1.000 43.99877  ? 386  GLY A N   1 
ATOM   3115 C  CA  . GLY A 1 386 ? -18.99900 40.32100 -1.99600  1.000 45.27291  ? 386  GLY A CA  1 
ATOM   3116 C  C   . GLY A 1 386 ? -18.68600 41.56600 -1.20000  1.000 37.87674  ? 386  GLY A C   1 
ATOM   3117 O  O   . GLY A 1 386 ? -17.69000 41.59400 -0.48900  1.000 47.23644  ? 386  GLY A O   1 
ATOM   3118 N  N   . PRO A 1 387 ? -19.54500 42.59400 -1.29100  1.000 43.62150  ? 387  PRO A N   1 
ATOM   3119 C  CA  . PRO A 1 387 ? -19.35000 43.83400 -0.55000  1.000 45.82484  ? 387  PRO A CA  1 
ATOM   3120 C  C   . PRO A 1 387 ? -19.75400 43.77200 0.92500   1.000 47.84739  ? 387  PRO A C   1 
ATOM   3121 O  O   . PRO A 1 387 ? -19.20500 44.50900 1.70700   1.000 48.97695  ? 387  PRO A O   1 
ATOM   3122 C  CB  . PRO A 1 387 ? -20.36900 44.73800 -1.25500  1.000 52.05691  ? 387  PRO A CB  1 
ATOM   3123 C  CG  . PRO A 1 387 ? -21.47900 43.81800 -1.67100  1.000 45.04031  ? 387  PRO A CG  1 
ATOM   3124 C  CD  . PRO A 1 387 ? -20.73700 42.59300 -2.13900  1.000 40.98297  ? 387  PRO A CD  1 
ATOM   3125 N  N   . ASN A 1 388 ? -20.69600 42.90500 1.25400   1.000 39.56679  ? 388  ASN A N   1 
ATOM   3126 C  CA  . ASN A 1 388 ? -21.23200 42.81800 2.63200   1.000 40.94881  ? 388  ASN A CA  1 
ATOM   3127 C  C   . ASN A 1 388 ? -20.40900 41.83700 3.47500   1.000 48.64416  ? 388  ASN A C   1 
ATOM   3128 O  O   . ASN A 1 388 ? -20.43500 40.63500 3.19300   1.000 44.47286  ? 388  ASN A O   1 
ATOM   3129 C  CB  . ASN A 1 388 ? -22.72700 42.54600 2.60400   1.000 39.83955  ? 388  ASN A CB  1 
ATOM   3130 C  CG  . ASN A 1 388 ? -23.51900 43.64700 1.94400   1.000 44.58953  ? 388  ASN A CG  1 
ATOM   3131 O  OD1 . ASN A 1 388 ? -23.80900 44.66800 2.57300   1.000 48.81672  ? 388  ASN A OD1 1 
ATOM   3132 N  ND2 . ASN A 1 388 ? -23.89900 43.44900 0.69200   1.000 48.94979  ? 388  ASN A ND2 1 
ATOM   3133 N  N   . GLN A 1 389 ? -19.71900 42.36100 4.48000   1.000 47.01283  ? 389  GLN A N   1 
ATOM   3134 C  CA  . GLN A 1 389 ? -18.91100 41.54600 5.37400   1.000 46.49122  ? 389  GLN A CA  1 
ATOM   3135 C  C   . GLN A 1 389 ? -19.16500 41.98100 6.81000   1.000 42.00128  ? 389  GLN A C   1 
ATOM   3136 O  O   . GLN A 1 389 ? -19.38400 43.16400 7.08300   1.000 52.00544  ? 389  GLN A O   1 
ATOM   3137 C  CB  . GLN A 1 389 ? -17.41000 41.67900 5.06400   1.000 53.71788  ? 389  GLN A CB  1 
ATOM   3138 C  CG  . GLN A 1 389 ? -17.05700 41.56200 3.59100   1.000 55.55055  ? 389  GLN A CG  1 
ATOM   3139 C  CD  . GLN A 1 389 ? -15.65800 42.06300 3.28200   1.000 77.20395  ? 389  GLN A CD  1 
ATOM   3140 O  OE1 . GLN A 1 389 ? -14.86700 42.31300 4.18900   1.000 86.75312  ? 389  GLN A OE1 1 
ATOM   3141 N  NE2 . GLN A 1 389 ? -15.34900 42.21500 1.99800   1.000 79.29393  ? 389  GLN A NE2 1 
ATOM   3142 N  N   . VAL A 1 390 ? -19.02200 41.04400 7.73000   1.000 42.84996  ? 390  VAL A N   1 
ATOM   3143 C  CA  . VAL A 1 390 ? -19.23900 41.34000 9.17000   1.000 44.81421  ? 390  VAL A CA  1 
ATOM   3144 C  C   . VAL A 1 390 ? -18.01400 42.07600 9.73300   1.000 46.95968  ? 390  VAL A C   1 
ATOM   3145 O  O   . VAL A 1 390 ? -16.92200 41.90300 9.19000   1.000 42.03502  ? 390  VAL A O   1 
ATOM   3146 C  CB  . VAL A 1 390 ? -19.58100 40.04400 9.92900   1.000 40.08400  ? 390  VAL A CB  1 
ATOM   3147 C  CG1 . VAL A 1 390 ? -20.89300 39.44600 9.45700   1.000 40.17467  ? 390  VAL A CG1 1 
ATOM   3148 C  CG2 . VAL A 1 390 ? -18.46000 39.02500 9.82800   1.000 51.37384  ? 390  VAL A CG2 1 
ATOM   3149 N  N   . THR A 1 391 ? -18.21000 42.87000 10.78200  1.000 48.52691  ? 391  THR A N   1 
ATOM   3150 C  CA  . THR A 1 391 ? -17.12500 43.70200 11.37500  1.000 52.49657  ? 391  THR A CA  1 
ATOM   3151 C  C   . THR A 1 391 ? -15.99700 42.81500 11.89700  1.000 44.52707  ? 391  THR A C   1 
ATOM   3152 O  O   . THR A 1 391 ? -14.84500 43.08200 11.55500  1.000 44.14502  ? 391  THR A O   1 
ATOM   3153 C  CB  . THR A 1 391 ? -17.71300 44.64000 12.43300  1.000 45.28126  ? 391  THR A CB  1 
ATOM   3154 O  OG1 . THR A 1 391 ? -18.56500 43.86500 13.27100  1.000 66.29595  ? 391  THR A OG1 1 
ATOM   3155 C  CG2 . THR A 1 391 ? -18.50700 45.77400 11.82800  1.000 40.89909  ? 391  THR A CG2 1 
ATOM   3156 N  N   . GLY A 1 392 ? -16.34300 41.78100 12.65300  1.000 44.85650  ? 392  GLY A N   1 
ATOM   3157 C  CA  . GLY A 1 392 ? -15.33300 40.84000 13.15500  1.000 45.33044  ? 392  GLY A CA  1 
ATOM   3158 C  C   . GLY A 1 392 ? -15.34400 40.78200 14.66300  1.000 48.38473  ? 392  GLY A C   1 
ATOM   3159 O  O   . GLY A 1 392 ? -15.27700 41.84100 15.29500  1.000 58.50591  ? 392  GLY A O   1 
ATOM   3160 N  N   . GLY A 1 393 ? -15.42900 39.58300 15.21900  1.000 42.22452  ? 393  GLY A N   1 
ATOM   3161 C  CA  . GLY A 1 393 ? -15.36400 39.45200 16.67500  1.000 45.70049  ? 393  GLY A CA  1 
ATOM   3162 C  C   . GLY A 1 393 ? -16.71000 39.24300 17.30000  1.000 42.73846  ? 393  GLY A C   1 
ATOM   3163 O  O   . GLY A 1 393 ? -17.70000 39.14300 16.57500  1.000 52.22907  ? 393  GLY A O   1 
ATOM   3164 N  N   . SER A 1 394 ? -16.73100 39.17700 18.61700  1.000 43.09462  ? 394  SER A N   1 
ATOM   3165 C  CA  . SER A 1 394 ? -17.99800 38.99500 19.34000  1.000 41.98281  ? 394  SER A CA  1 
ATOM   3166 C  C   . SER A 1 394 ? -18.74800 40.32800 19.42700  1.000 41.82480  ? 394  SER A C   1 
ATOM   3167 O  O   . SER A 1 394 ? -18.12300 41.37700 19.21400  1.000 42.64355  ? 394  SER A O   1 
ATOM   3168 C  CB  . SER A 1 394 ? -17.72900 38.40700 20.70000  1.000 46.75558  ? 394  SER A CB  1 
ATOM   3169 O  OG  . SER A 1 394 ? -17.01400 37.18500 20.60700  1.000 51.82743  ? 394  SER A OG  1 
ATOM   3170 N  N   . PHE A 1 395 ? -20.03100 40.27300 19.74800  1.000 39.02431  ? 395  PHE A N   1 
ATOM   3171 C  CA  . PHE A 1 395 ? -20.87400 41.48900 19.85000  1.000 45.23789  ? 395  PHE A CA  1 
ATOM   3172 C  C   . PHE A 1 395 ? -20.81500 42.29100 18.53600  1.000 46.66033  ? 395  PHE A C   1 
ATOM   3173 O  O   . PHE A 1 395 ? -20.67700 43.51500 18.58300  1.000 48.11547  ? 395  PHE A O   1 
ATOM   3174 C  CB  . PHE A 1 395 ? -20.44100 42.16500 21.14900  1.000 47.66551  ? 395  PHE A CB  1 
ATOM   3175 C  CG  . PHE A 1 395 ? -20.62400 41.33400 22.40800  1.000 38.76433  ? 395  PHE A CG  1 
ATOM   3176 C  CD1 . PHE A 1 395 ? -21.84700 41.29400 23.05900  1.000 43.80732  ? 395  PHE A CD1 1 
ATOM   3177 C  CD2 . PHE A 1 395 ? -19.56200 40.62600 22.95200  1.000 38.34814  ? 395  PHE A CD2 1 
ATOM   3178 C  CE1 . PHE A 1 395 ? -22.01100 40.54600 24.20900  1.000 46.52801  ? 395  PHE A CE1 1 
ATOM   3179 C  CE2 . PHE A 1 395 ? -19.73200 39.88300 24.10400  1.000 46.07210  ? 395  PHE A CE2 1 
ATOM   3180 C  CZ  . PHE A 1 395 ? -20.95400 39.84500 24.72600  1.000 45.91490  ? 395  PHE A CZ  1 
ATOM   3181 N  N   . THR A 1 396 ? -20.90200 41.60300 17.40000  1.000 46.77530  ? 396  THR A N   1 
ATOM   3182 C  CA  . THR A 1 396 ? -20.92900 42.27300 16.09200  1.000 41.30637  ? 396  THR A CA  1 
ATOM   3183 C  C   . THR A 1 396 ? -22.30700 42.09000 15.47600  1.000 48.81648  ? 396  THR A C   1 
ATOM   3184 O  O   . THR A 1 396 ? -23.09200 41.29700 16.00500  1.000 48.14741  ? 396  THR A O   1 
ATOM   3185 C  CB  . THR A 1 396 ? -19.80000 41.73700 15.22300  1.000 36.92087  ? 396  THR A CB  1 
ATOM   3186 O  OG1 . THR A 1 396 ? -19.94400 40.32400 15.18100  1.000 51.75061  ? 396  THR A OG1 1 
ATOM   3187 C  CG2 . THR A 1 396 ? -18.43800 42.09500 15.78500  1.000 46.36299  ? 396  THR A CG2 1 
ATOM   3188 N  N   . ALA A 1 397 ? -22.61600 42.84800 14.42300  1.000 54.12909  ? 397  ALA A N   1 
ATOM   3189 C  CA  . ALA A 1 397 ? -23.96500 42.78800 13.81600  1.000 52.51792  ? 397  ALA A CA  1 
ATOM   3190 C  C   . ALA A 1 397 ? -24.15900 41.52000 12.98300  1.000 43.55654  ? 397  ALA A C   1 
ATOM   3191 O  O   . ALA A 1 397 ? -23.23800 41.10500 12.26700  1.000 39.67720  ? 397  ALA A O   1 
ATOM   3192 C  CB  . ALA A 1 397 ? -24.22900 44.03400 13.01000  1.000 41.61377  ? 397  ALA A CB  1 
ATOM   3193 N  N   . PRO A 1 398 ? -25.34700 40.90200 13.03200  1.000 40.77963  ? 398  PRO A N   1 
ATOM   3194 C  CA  . PRO A 1 398 ? -25.66400 39.73300 12.16500  1.000 38.73846  ? 398  PRO A CA  1 
ATOM   3195 C  C   . PRO A 1 398 ? -25.51400 40.11200 10.69600  1.000 42.29490  ? 398  PRO A C   1 
ATOM   3196 O  O   . PRO A 1 398 ? -25.89500 41.23600 10.31800  1.000 47.81732  ? 398  PRO A O   1 
ATOM   3197 C  CB  . PRO A 1 398 ? -27.07700 39.38200 12.56200  1.000 32.50114  ? 398  PRO A CB  1 
ATOM   3198 C  CG  . PRO A 1 398 ? -27.23700 39.94000 13.95400  1.000 48.97059  ? 398  PRO A CG  1 
ATOM   3199 C  CD  . PRO A 1 398 ? -26.48900 41.22100 13.93800  1.000 41.30746  ? 398  PRO A CD  1 
ATOM   3200 N  N   . LEU A 1 399 ? -24.95500 39.21700 9.88800   1.000 44.30115  ? 399  LEU A N   1 
ATOM   3201 C  CA  . LEU A 1 399 ? -24.79800 39.47900 8.43300   1.000 40.90420  ? 399  LEU A CA  1 
ATOM   3202 C  C   . LEU A 1 399 ? -26.15200 39.53100 7.73200   1.000 38.94923  ? 399  LEU A C   1 
ATOM   3203 O  O   . LEU A 1 399 ? -27.01200 38.69800 8.02100   1.000 40.48947  ? 399  LEU A O   1 
ATOM   3204 C  CB  . LEU A 1 399 ? -23.92500 38.46400 7.70200   1.000 29.35918  ? 399  LEU A CB  1 
ATOM   3205 C  CG  . LEU A 1 399 ? -23.72000 38.68700 6.20300   1.000 31.47115  ? 399  LEU A CG  1 
ATOM   3206 C  CD1 . LEU A 1 399 ? -22.97700 39.97800 5.93100   1.000 35.91109  ? 399  LEU A CD1 1 
ATOM   3207 C  CD2 . LEU A 1 399 ? -22.99300 37.51200 5.58600   1.000 26.33518  ? 399  LEU A CD2 1 
ATOM   3208 N  N   . GLN A 1 400 ? -26.33300 40.51000 6.87000   1.000 41.57746  ? 400  GLN A N   1 
ATOM   3209 C  CA  . GLN A 1 400 ? -27.53900 40.58600 6.02100   1.000 38.25159  ? 400  GLN A CA  1 
ATOM   3210 C  C   . GLN A 1 400 ? -26.95200 40.96900 4.67100   1.000 45.13930  ? 400  GLN A C   1 
ATOM   3211 O  O   . GLN A 1 400 ? -26.50900 42.10800 4.53200   1.000 51.71822  ? 400  GLN A O   1 
ATOM   3212 C  CB  . GLN A 1 400 ? -28.58000 41.53900 6.59400   1.000 36.29819  ? 400  GLN A CB  1 
ATOM   3213 C  CG  . GLN A 1 400 ? -29.29300 41.01400 7.82400   1.000 47.90312  ? 400  GLN A CG  1 
ATOM   3214 C  CD  . GLN A 1 400 ? -30.52100 41.83200 8.12000   1.000 40.97846  ? 400  GLN A CD  1 
ATOM   3215 O  OE1 . GLN A 1 400 ? -31.34300 42.08300 7.24600   1.000 44.78098  ? 400  GLN A OE1 1 
ATOM   3216 N  NE2 . GLN A 1 400 ? -30.65000 42.25800 9.36400   1.000 41.65637  ? 400  GLN A NE2 1 
ATOM   3217 N  N   . GLY A 1 401 ? -26.82900 40.00500 3.77200   1.000 38.06159  ? 401  GLY A N   1 
ATOM   3218 C  CA  . GLY A 1 401 ? -26.20100 40.25500 2.47200   1.000 36.93208  ? 401  GLY A CA  1 
ATOM   3219 C  C   . GLY A 1 401 ? -27.20800 40.33600 1.34400   1.000 44.74147  ? 401  GLY A C   1 
ATOM   3220 O  O   . GLY A 1 401 ? -28.38800 40.54000 1.62300   1.000 40.75302  ? 401  GLY A O   1 
ATOM   3221 N  N   . ASN A 1 402 ? -26.72800 40.18200 0.11700   1.000 39.21924  ? 402  ASN A N   1 
ATOM   3222 C  CA  . ASN A 1 402 ? -27.60800 40.29700 -1.06500  1.000 40.27968  ? 402  ASN A CA  1 
ATOM   3223 C  C   . ASN A 1 402 ? -27.02800 39.49900 -2.23200  1.000 39.32552  ? 402  ASN A C   1 
ATOM   3224 O  O   . ASN A 1 402 ? -26.04400 38.79400 -2.01300  1.000 39.70209  ? 402  ASN A O   1 
ATOM   3225 C  CB  . ASN A 1 402 ? -27.88100 41.76800 -1.39600  1.000 34.97961  ? 402  ASN A CB  1 
ATOM   3226 C  CG  . ASN A 1 402 ? -26.68400 42.56800 -1.85700  1.000 40.48758  ? 402  ASN A CG  1 
ATOM   3227 O  OD1 . ASN A 1 402 ? -25.70600 42.02300 -2.35200  1.000 42.93614  ? 402  ASN A OD1 1 
ATOM   3228 N  ND2 . ASN A 1 402 ? -26.77800 43.87600 -1.70100  1.000 47.13298  ? 402  ASN A ND2 1 
ATOM   3229 N  N   . SER A 1 403 ? -27.60300 39.65300 -3.42300  1.000 42.65154  ? 403  SER A N   1 
ATOM   3230 C  CA  . SER A 1 403 ? -27.20300 38.90300 -4.64000  1.000 39.93223  ? 403  SER A CA  1 
ATOM   3231 C  C   . SER A 1 403 ? -25.72700 39.09800 -5.00300  1.000 44.08421  ? 403  SER A C   1 
ATOM   3232 O  O   . SER A 1 403 ? -25.20600 38.30100 -5.78700  1.000 38.96190  ? 403  SER A O   1 
ATOM   3233 C  CB  . SER A 1 403 ? -28.08600 39.32300 -5.77400  1.000 37.73585  ? 403  SER A CB  1 
ATOM   3234 O  OG  . SER A 1 403 ? -27.93400 40.70300 -6.05300  1.000 45.11539  ? 403  SER A OG  1 
ATOM   3235 N  N   . SER A 1 404 ? -25.09000 40.13200 -4.47300  1.000 34.62487  ? 404  SER A N   1 
ATOM   3236 C  CA  . SER A 1 404 ? -23.68200 40.32600 -4.78600  1.000 35.43876  ? 404  SER A CA  1 
ATOM   3237 C  C   . SER A 1 404 ? -22.76500 39.56900 -3.83800  1.000 46.72943  ? 404  SER A C   1 
ATOM   3238 O  O   . SER A 1 404 ? -21.54700 39.56800 -4.04300  1.000 42.89976  ? 404  SER A O   1 
ATOM   3239 C  CB  . SER A 1 404 ? -23.33500 41.82000 -4.76300  1.000 43.62889  ? 404  SER A CB  1 
ATOM   3240 O  OG  . SER A 1 404 ? -24.00100 42.51600 -5.80400  1.000 58.84170  ? 404  SER A OG  1 
ATOM   3241 N  N   . ASP A 1 405 ? -23.35800 38.92800 -2.83500  1.000 41.03857  ? 405  ASP A N   1 
ATOM   3242 C  CA  . ASP A 1 405 ? -22.56900 38.22700 -1.79400  1.000 35.72612  ? 405  ASP A CA  1 
ATOM   3243 C  C   . ASP A 1 405 ? -22.57500 36.71300 -2.01300  1.000 40.07854  ? 405  ASP A C   1 
ATOM   3244 O  O   . ASP A 1 405 ? -23.64500 36.14900 -2.27500  1.000 34.83045  ? 405  ASP A O   1 
ATOM   3245 C  CB  . ASP A 1 405 ? -23.06200 38.60300 -0.41500  1.000 35.23925  ? 405  ASP A CB  1 
ATOM   3246 C  CG  . ASP A 1 405 ? -22.94100 40.07100 -0.04000  1.000 42.42808  ? 405  ASP A CG  1 
ATOM   3247 O  OD1 . ASP A 1 405 ? -21.81600 40.59400 -0.09100  1.000 46.61451  ? 405  ASP A OD1 1 
ATOM   3248 O  OD2 . ASP A 1 405 ? -23.96500 40.65600 0.34600   1.000 41.56233  ? 405  ASP A OD2 1 
ATOM   3249 N  N   . ILE A 1 406 ? -21.39600 36.11100 -1.96700  1.000 42.04514  ? 406  ILE A N   1 
ATOM   3250 C  CA  . ILE A 1 406 ? -21.25300 34.64100 -2.12400  1.000 37.09382  ? 406  ILE A CA  1 
ATOM   3251 C  C   . ILE A 1 406 ? -20.60300 34.06900 -0.86300  1.000 46.73201  ? 406  ILE A C   1 
ATOM   3252 O  O   . ILE A 1 406 ? -19.69100 34.70600 -0.32500  1.000 39.28476  ? 406  ILE A O   1 
ATOM   3253 C  CB  . ILE A 1 406 ? -20.42500 34.30100 -3.37100  1.000 44.10128  ? 406  ILE A CB  1 
ATOM   3254 C  CG1 . ILE A 1 406 ? -20.96500 35.00100 -4.62000  1.000 42.45982  ? 406  ILE A CG1 1 
ATOM   3255 C  CG2 . ILE A 1 406 ? -20.33300 32.79600 -3.56000  1.000 44.31435  ? 406  ILE A CG2 1 
ATOM   3256 C  CD1 . ILE A 1 406 ? -20.11600 34.80200 -5.84600  1.000 47.56074  ? 406  ILE A CD1 1 
ATOM   3257 N  N   . ARG A 1 407 ? -21.07700 32.90700 -0.42200  1.000 46.67962  ? 407  ARG A N   1 
ATOM   3258 C  CA  . ARG A 1 407 ? -20.47600 32.21700 0.74200   1.000 39.80217  ? 407  ARG A CA  1 
ATOM   3259 C  C   . ARG A 1 407 ? -20.10700 30.79700 0.29900   1.000 39.52450  ? 407  ARG A C   1 
ATOM   3260 O  O   . ARG A 1 407 ? -20.97000 30.08700 -0.21800  1.000 35.46719  ? 407  ARG A O   1 
ATOM   3261 C  CB  . ARG A 1 407 ? -21.40400 32.32500 1.94800   1.000 35.27793  ? 407  ARG A CB  1 
ATOM   3262 C  CG  . ARG A 1 407 ? -21.42500 33.69900 2.59700   1.000 34.22360  ? 407  ARG A CG  1 
ATOM   3263 C  CD  . ARG A 1 407 ? -20.04700 34.17500 3.00400   1.000 37.82336  ? 407  ARG A CD  1 
ATOM   3264 N  NE  . ARG A 1 407 ? -20.14100 35.43200 3.72600   1.000 50.51320  ? 407  ARG A NE  1 
ATOM   3265 C  CZ  . ARG A 1 407 ? -20.07600 36.63200 3.16800   1.000 44.39251  ? 407  ARG A CZ  1 
ATOM   3266 N  NH1 . ARG A 1 407 ? -19.90500 36.74900 1.86400   1.000 41.19699  ? 407  ARG A NH1 1 
ATOM   3267 N  NH2 . ARG A 1 407 ? -20.18200 37.71100 3.91700   1.000 44.96982  ? 407  ARG A NH2 1 
ATOM   3268 N  N   . PHE A 1 408 ? -18.85500 30.41800 0.51200   1.000 41.09315  ? 408  PHE A N   1 
ATOM   3269 C  CA  . PHE A 1 408 ? -18.36800 29.12600 -0.01400  1.000 36.86356  ? 408  PHE A CA  1 
ATOM   3270 C  C   . PHE A 1 408 ? -18.29400 28.01900 1.04300   1.000 46.36560  ? 408  PHE A C   1 
ATOM   3271 O  O   . PHE A 1 408 ? -17.96200 28.31500 2.19700   1.000 43.93262  ? 408  PHE A O   1 
ATOM   3272 C  CB  . PHE A 1 408 ? -16.99400 29.32300 -0.64600  1.000 38.25575  ? 408  PHE A CB  1 
ATOM   3273 C  CG  . PHE A 1 408 ? -16.90900 30.24300 -1.83300  1.000 46.83242  ? 408  PHE A CG  1 
ATOM   3274 C  CD1 . PHE A 1 408 ? -17.51700 29.91400 -3.03100  1.000 46.31470  ? 408  PHE A CD1 1 
ATOM   3275 C  CD2 . PHE A 1 408 ? -16.17300 31.41200 -1.76600  1.000 44.57206  ? 408  PHE A CD2 1 
ATOM   3276 C  CE1 . PHE A 1 408 ? -17.41600 30.75500 -4.12700  1.000 53.56870  ? 408  PHE A CE1 1 
ATOM   3277 C  CE2 . PHE A 1 408 ? -16.07300 32.25000 -2.86300  1.000 45.92027  ? 408  PHE A CE2 1 
ATOM   3278 C  CZ  . PHE A 1 408 ? -16.69500 31.92000 -4.04100  1.000 48.63895  ? 408  PHE A CZ  1 
ATOM   3279 N  N   . THR A 1 409 ? -18.63400 26.79700 0.62900   1.000 44.36309  ? 409  THR A N   1 
ATOM   3280 C  CA  . THR A 1 409 ? -18.50600 25.58500 1.47800   1.000 46.98825  ? 409  THR A CA  1 
ATOM   3281 C  C   . THR A 1 409 ? -18.01500 24.47700 0.53700   1.000 43.71771  ? 409  THR A C   1 
ATOM   3282 O  O   . THR A 1 409 ? -18.15800 24.65600 -0.67300  1.000 47.86709  ? 409  THR A O   1 
ATOM   3283 C  CB  . THR A 1 409 ? -19.80200 25.22200 2.21200   1.000 35.27973  ? 409  THR A CB  1 
ATOM   3284 O  OG1 . THR A 1 409 ? -20.77200 24.78000 1.26400   1.000 49.29784  ? 409  THR A OG1 1 
ATOM   3285 C  CG2 . THR A 1 409 ? -20.35000 26.36000 3.04400   1.000 43.55774  ? 409  THR A CG2 1 
ATOM   3286 N  N   . ARG A 1 410 ? -17.40900 23.41300 1.06400   1.000 44.83754  ? 410  ARG A N   1 
ATOM   3287 C  CA  . ARG A 1 410 ? -16.92200 22.31600 0.24100   1.000 40.72009  ? 410  ARG A CA  1 
ATOM   3288 C  C   . ARG A 1 410 ? -17.19600 20.99800 0.94600   1.000 42.96074  ? 410  ARG A C   1 
ATOM   3289 O  O   . ARG A 1 410 ? -17.31700 20.93900 2.17200   1.000 45.28863  ? 410  ARG A O   1 
ATOM   3290 C  CB  . ARG A 1 410 ? -15.42400 22.45100 -0.06000  1.000 51.40967  ? 410  ARG A CB  1 
ATOM   3291 C  CG  . ARG A 1 410 ? -14.53000 22.35200 1.16600   1.000 48.92610  ? 410  ARG A CG  1 
ATOM   3292 C  CD  . ARG A 1 410 ? -13.07600 22.15700 0.76800   1.000 59.06688  ? 410  ARG A CD  1 
ATOM   3293 N  NE  . ARG A 1 410 ? -12.18400 22.15300 1.92200   1.000 61.71449  ? 410  ARG A NE  1 
ATOM   3294 C  CZ  . ARG A 1 410 ? -11.89400 21.07900 2.64300   1.000 53.74828  ? 410  ARG A CZ  1 
ATOM   3295 N  NH1 . ARG A 1 410 ? -12.42100 19.89700 2.36800   1.000 48.93682  ? 410  ARG A NH1 1 
ATOM   3296 N  NH2 . ARG A 1 410 ? -11.05300 21.19300 3.66700   1.000 45.76458  ? 410  ARG A NH2 1 
ATOM   3297 N  N   . ASN A 1 411 ? -17.29100 19.93400 0.15200   1.000 48.96512  ? 411  ASN A N   1 
ATOM   3298 C  CA  . ASN A 1 411 ? -17.42400 18.60500 0.72200   1.000 50.99307  ? 411  ASN A CA  1 
ATOM   3299 C  C   . ASN A 1 411 ? -16.08400 18.14800 1.29700   1.000 52.02385  ? 411  ASN A C   1 
ATOM   3300 O  O   . ASN A 1 411 ? -15.03900 18.77000 1.08800   1.000 53.70374  ? 411  ASN A O   1 
ATOM   3301 C  CB  . ASN A 1 411 ? -17.93700 17.61700 -0.32700  1.000 57.98207  ? 411  ASN A CB  1 
ATOM   3302 C  CG  . ASN A 1 411 ? -16.97700 17.44200 -1.48800  1.000 48.35856  ? 411  ASN A CG  1 
ATOM   3303 O  OD1 . ASN A 1 411 ? -16.14500 18.30800 -1.76000  1.000 55.74078  ? 411  ASN A OD1 1 
ATOM   3304 N  ND2 . ASN A 1 411 ? -17.09500 16.31700 -2.18500  1.000 50.01988  ? 411  ASN A ND2 1 
ATOM   3305 N  N   . LYS A 1 412 ? -16.12400 17.04000 2.04100   1.000 51.06269  ? 412  LYS A N   1 
ATOM   3306 C  CA  . LYS A 1 412 ? -14.91500 16.55600 2.70100   1.000 54.58861  ? 412  LYS A CA  1 
ATOM   3307 C  C   . LYS A 1 412 ? -13.87300 16.07500 1.70000   1.000 60.25429  ? 412  LYS A C   1 
ATOM   3308 O  O   . LYS A 1 412 ? -12.67000 16.21600 1.94700   1.000 66.77547  ? 412  LYS A O   1 
ATOM   3309 C  CB  . LYS A 1 412 ? -15.26600 15.44200 3.68500   1.000 53.77643  ? 412  LYS A CB  1 
ATOM   3310 C  CG  . LYS A 1 412 ? -16.17900 15.89000 4.81000   1.000 52.23876  ? 412  LYS A CG  1 
ATOM   3311 C  CD  . LYS A 1 412 ? -16.54300 14.73400 5.72000   1.000 45.73988  ? 412  LYS A CD  1 
ATOM   3312 C  CE  . LYS A 1 412 ? -17.51300 15.17900 6.79800   1.000 48.06396  ? 412  LYS A CE  1 
ATOM   3313 N  NZ  . LYS A 1 412 ? -17.90100 14.06100 7.69800   1.000 45.43661  ? 412  LYS A NZ  1 
ATOM   3314 N  N   . ASP A 1 413 ? -14.30500 15.51400 0.56900   1.000 57.76205  ? 413  ASP A N   1 
ATOM   3315 C  CA  . ASP A 1 413 ? -13.36700 15.07400 -0.45700  1.000 56.61644  ? 413  ASP A CA  1 
ATOM   3316 C  C   . ASP A 1 413 ? -12.74600 16.23100 -1.22800  1.000 59.94899  ? 413  ASP A C   1 
ATOM   3317 O  O   . ASP A 1 413 ? -11.84300 15.99400 -2.04000  1.000 68.82652  ? 413  ASP A O   1 
ATOM   3318 C  CB  . ASP A 1 413 ? -14.06400 14.12000 -1.42800  1.000 58.33118  ? 413  ASP A CB  1 
ATOM   3319 C  CG  . ASP A 1 413 ? -14.52100 12.83900 -0.75900  1.000 68.39030  ? 413  ASP A CG  1 
ATOM   3320 O  OD1 . ASP A 1 413 ? -13.93400 12.46600 0.28000   1.000 75.40779  ? 413  ASP A OD1 1 
ATOM   3321 O  OD2 . ASP A 1 413 ? -15.46300 12.20100 -1.27500  1.000 68.93186  ? 413  ASP A OD2 1 
ATOM   3322 N  N   . ALA A 1 414 ? -13.21000 17.46200 -0.99800  1.000 57.57832  ? 414  ALA A N   1 
ATOM   3323 C  CA  . ALA A 1 414 ? -12.66600 18.66700 -1.63100  1.000 61.00877  ? 414  ALA A CA  1 
ATOM   3324 C  C   . ALA A 1 414 ? -12.76700 18.62000 -3.15400  1.000 58.87203  ? 414  ALA A C   1 
ATOM   3325 O  O   . ALA A 1 414 ? -11.88400 19.11200 -3.85800  1.000 60.92295  ? 414  ALA A O   1 
ATOM   3326 C  CB  . ALA A 1 414 ? -11.21900 18.92100 -1.19800  1.000 56.79660  ? 414  ALA A CB  1 
ATOM   3327 N  N   . ASN A 1 415 ? -13.84600 18.03800 -3.68400  1.000 61.23839  ? 415  ASN A N   1 
ATOM   3328 C  CA  . ASN A 1 415 ? -14.08400 18.04800 -5.12300  1.000 60.75385  ? 415  ASN A CA  1 
ATOM   3329 C  C   . ASN A 1 415 ? -15.45700 18.60400 -5.48300  1.000 59.82703  ? 415  ASN A C   1 
ATOM   3330 O  O   . ASN A 1 415 ? -15.87400 18.49000 -6.64300  1.000 67.21926  ? 415  ASN A O   1 
ATOM   3331 C  CB  . ASN A 1 415 ? -13.91000 16.64300 -5.71400  1.000 62.46988  ? 415  ASN A CB  1 
ATOM   3332 C  CG  . ASN A 1 415 ? -14.70200 15.59000 -4.96800  1.000 60.95344  ? 415  ASN A CG  1 
ATOM   3333 O  OD1 . ASN A 1 415 ? -15.85700 15.80200 -4.60100  1.000 61.11566  ? 415  ASN A OD1 1 
ATOM   3334 N  ND2 . ASN A 1 415 ? -14.07700 14.44200 -4.73800  1.000 82.19617  ? 415  ASN A ND2 1 
ATOM   3335 N  N   . VAL A 1 416 ? -16.16800 19.19200 -4.52400  1.000 46.98116  ? 416  VAL A N   1 
ATOM   3336 C  CA  . VAL A 1 416 ? -17.44500 19.85700 -4.75600  1.000 45.21299  ? 416  VAL A CA  1 
ATOM   3337 C  C   . VAL A 1 416 ? -17.41200 21.19100 -4.02500  1.000 52.30407  ? 416  VAL A C   1 
ATOM   3338 O  O   . VAL A 1 416 ? -17.01800 21.25000 -2.85500  1.000 44.22733  ? 416  VAL A O   1 
ATOM   3339 C  CB  . VAL A 1 416 ? -18.63800 19.00500 -4.27800  1.000 51.55935  ? 416  VAL A CB  1 
ATOM   3340 C  CG1 . VAL A 1 416 ? -19.93200 19.79600 -4.38000  1.000 44.32010  ? 416  VAL A CG1 1 
ATOM   3341 C  CG2 . VAL A 1 416 ? -18.73600 17.71700 -5.08300  1.000 48.66126  ? 416  VAL A CG2 1 
ATOM   3342 N  N   . LEU A 1 417 ? -17.81100 22.25700 -4.71300  1.000 55.04738  ? 417  LEU A N   1 
ATOM   3343 C  CA  . LEU A 1 417 ? -17.80100 23.60600 -4.15800  1.000 41.73700  ? 417  LEU A CA  1 
ATOM   3344 C  C   . LEU A 1 417 ? -19.21900 24.15500 -4.16600  1.000 44.59325  ? 417  LEU A C   1 
ATOM   3345 O  O   . LEU A 1 417 ? -19.83700 24.26800 -5.22800  1.000 46.12413  ? 417  LEU A O   1 
ATOM   3346 C  CB  . LEU A 1 417 ? -16.86900 24.52000 -4.95600  1.000 41.10682  ? 417  LEU A CB  1 
ATOM   3347 C  CG  . LEU A 1 417 ? -16.71600 25.95100 -4.43700  1.000 47.43205  ? 417  LEU A CG  1 
ATOM   3348 C  CD1 . LEU A 1 417 ? -16.00500 25.95900 -3.09300  1.000 42.52562  ? 417  LEU A CD1 1 
ATOM   3349 C  CD2 . LEU A 1 417 ? -15.97900 26.81600 -5.44500  1.000 48.18301  ? 417  LEU A CD2 1 
ATOM   3350 N  N   . TYR A 1 418 ? -19.73700 24.49300 -2.99000  1.000 41.66400  ? 418  TYR A N   1 
ATOM   3351 C  CA  . TYR A 1 418 ? -21.05300 25.10100 -2.86400  1.000 45.90177  ? 418  TYR A CA  1 
ATOM   3352 C  C   . TYR A 1 418 ? -20.88500 26.60400 -2.69200  1.000 43.16331  ? 418  TYR A C   1 
ATOM   3353 O  O   . TYR A 1 418 ? -20.32600 27.06000 -1.68800  1.000 51.15218  ? 418  TYR A O   1 
ATOM   3354 C  CB  . TYR A 1 418 ? -21.82700 24.51100 -1.68600  1.000 37.61979  ? 418  TYR A CB  1 
ATOM   3355 C  CG  . TYR A 1 418 ? -22.03500 23.02200 -1.78100  1.000 47.38917  ? 418  TYR A CG  1 
ATOM   3356 C  CD1 . TYR A 1 418 ? -23.01300 22.49000 -2.60900  1.000 40.70680  ? 418  TYR A CD1 1 
ATOM   3357 C  CD2 . TYR A 1 418 ? -21.25500 22.14600 -1.03900  1.000 47.55598  ? 418  TYR A CD2 1 
ATOM   3358 C  CE1 . TYR A 1 418 ? -23.20700 21.12500 -2.69800  1.000 45.13111  ? 418  TYR A CE1 1 
ATOM   3359 C  CE2 . TYR A 1 418 ? -21.44200 20.78300 -1.12000  1.000 46.92369  ? 418  TYR A CE2 1 
ATOM   3360 C  CZ  . TYR A 1 418 ? -22.41700 20.27700 -1.95000  1.000 47.68601  ? 418  TYR A CZ  1 
ATOM   3361 O  OH  . TYR A 1 418 ? -22.60000 18.91500 -2.03100  1.000 50.82803  ? 418  TYR A OH  1 
ATOM   3362 N  N   . ALA A 1 419 ? -21.36100 27.36100 -3.67400  1.000 40.38274  ? 419  ALA A N   1 
ATOM   3363 C  CA  . ALA A 1 419 ? -21.34700 28.81900 -3.64300  1.000 42.71837  ? 419  ALA A CA  1 
ATOM   3364 C  C   . ALA A 1 419 ? -22.78000 29.28800 -3.43200  1.000 40.61161  ? 419  ALA A C   1 
ATOM   3365 O  O   . ALA A 1 419 ? -23.62900 29.12700 -4.31500  1.000 40.65622  ? 419  ALA A O   1 
ATOM   3366 C  CB  . ALA A 1 419 ? -20.76000 29.39100 -4.93100  1.000 42.15790  ? 419  ALA A CB  1 
ATOM   3367 N  N   . THR A 1 420 ? -23.01500 29.90100 -2.28700  1.000 37.88350  ? 420  THR A N   1 
ATOM   3368 C  CA  . THR A 1 420 ? -24.37200 30.35300 -1.96700  1.000 40.53320  ? 420  THR A CA  1 
ATOM   3369 C  C   . THR A 1 420 ? -24.46600 31.85600 -2.14300  1.000 37.51966  ? 420  THR A C   1 
ATOM   3370 O  O   . THR A 1 420 ? -23.65900 32.58200 -1.55600  1.000 38.52075  ? 420  THR A O   1 
ATOM   3371 C  CB  . THR A 1 420 ? -24.78100 29.86300 -0.57800  1.000 42.71713  ? 420  THR A CB  1 
ATOM   3372 O  OG1 . THR A 1 420 ? -24.66100 28.44700 -0.62900  1.000 38.87105  ? 420  THR A OG1 1 
ATOM   3373 C  CG2 . THR A 1 420 ? -26.19600 30.27100 -0.21400  1.000 35.79356  ? 420  THR A CG2 1 
ATOM   3374 N  N   . VAL A 1 421 ? -25.40600 32.28800 -2.98200  1.000 41.95690  ? 421  VAL A N   1 
ATOM   3375 C  CA  . VAL A 1 421 ? -25.62300 33.73700 -3.21900  1.000 40.98496  ? 421  VAL A CA  1 
ATOM   3376 C  C   . VAL A 1 421 ? -26.67000 34.18200 -2.20000  1.000 46.15076  ? 421  VAL A C   1 
ATOM   3377 O  O   . VAL A 1 421 ? -27.65300 33.46000 -2.03900  1.000 43.37354  ? 421  VAL A O   1 
ATOM   3378 C  CB  . VAL A 1 421 ? -26.00600 34.01500 -4.67900  1.000 38.48434  ? 421  VAL A CB  1 
ATOM   3379 C  CG1 . VAL A 1 421 ? -26.12600 35.50500 -4.94600  1.000 43.94410  ? 421  VAL A CG1 1 
ATOM   3380 C  CG2 . VAL A 1 421 ? -25.00100 33.39600 -5.63800  1.000 38.62949  ? 421  VAL A CG2 1 
ATOM   3381 N  N   . LEU A 1 422 ? -26.47500 35.35000 -1.59300  1.000 43.18082  ? 422  LEU A N   1 
ATOM   3382 C  CA  . LEU A 1 422 ? -27.35600 35.83100 -0.49600  1.000 43.18929  ? 422  LEU A CA  1 
ATOM   3383 C  C   . LEU A 1 422 ? -28.59100 36.51000 -1.07000  1.000 40.84910  ? 422  LEU A C   1 
ATOM   3384 O  O   . LEU A 1 422 ? -29.30600 37.17900 -0.32100  1.000 39.79226  ? 422  LEU A O   1 
ATOM   3385 C  CB  . LEU A 1 422 ? -26.53900 36.75800 0.40200   1.000 43.10976  ? 422  LEU A CB  1 
ATOM   3386 C  CG  . LEU A 1 422 ? -25.35400 36.09800 1.10500   1.000 40.85625  ? 422  LEU A CG  1 
ATOM   3387 C  CD1 . LEU A 1 422 ? -24.84700 36.96100 2.24800   1.000 37.67189  ? 422  LEU A CD1 1 
ATOM   3388 C  CD2 . LEU A 1 422 ? -25.72600 34.71500 1.60900   1.000 28.75715  ? 422  LEU A CD2 1 
ATOM   3389 N  N   . GLY A 1 423 ? -28.79200 36.35200 -2.36500  1.000 43.35634  ? 423  GLY A N   1 
ATOM   3390 C  CA  . GLY A 1 423 ? -30.02100 36.84200 -2.98700  1.000 41.98668  ? 423  GLY A CA  1 
ATOM   3391 C  C   . GLY A 1 423 ? -30.09100 36.36200 -4.40700  1.000 46.83691  ? 423  GLY A C   1 
ATOM   3392 O  O   . GLY A 1 423 ? -29.17300 35.66500 -4.84400  1.000 50.53941  ? 423  GLY A O   1 
ATOM   3393 N  N   . TRP A 1 424 ? -31.16300 36.69600 -5.09100  1.000 42.77748  ? 424  TRP A N   1 
ATOM   3394 C  CA  . TRP A 1 424 ? -31.26900 36.37400 -6.50500  1.000 40.60788  ? 424  TRP A CA  1 
ATOM   3395 C  C   . TRP A 1 424 ? -30.80200 37.55800 -7.33300  1.000 47.23109  ? 424  TRP A C   1 
ATOM   3396 O  O   . TRP A 1 424 ? -31.38300 38.64900 -7.21700  1.000 46.81864  ? 424  TRP A O   1 
ATOM   3397 C  CB  . TRP A 1 424 ? -32.69600 36.00000 -6.88200  1.000 40.35401  ? 424  TRP A CB  1 
ATOM   3398 C  CG  . TRP A 1 424 ? -32.78300 35.49500 -8.28500  1.000 47.74526  ? 424  TRP A CG  1 
ATOM   3399 C  CD1 . TRP A 1 424 ? -33.24200 36.17200 -9.37600  1.000 43.33861  ? 424  TRP A CD1 1 
ATOM   3400 C  CD2 . TRP A 1 424 ? -32.36800 34.20700 -8.75800  1.000 50.02362  ? 424  TRP A CD2 1 
ATOM   3401 N  NE1 . TRP A 1 424 ? -33.15200 35.38300 -10.49600 1.000 43.95960  ? 424  TRP A NE1 1 
ATOM   3402 C  CE2 . TRP A 1 424 ? -32.61700 34.17100 -10.14400 1.000 44.36734  ? 424  TRP A CE2 1 
ATOM   3403 C  CE3 . TRP A 1 424 ? -31.81600 33.07900 -8.14200  1.000 50.30580  ? 424  TRP A CE3 1 
ATOM   3404 C  CZ2 . TRP A 1 424 ? -32.33200 33.05300 -10.92600 1.000 48.61380  ? 424  TRP A CZ2 1 
ATOM   3405 C  CZ3 . TRP A 1 424 ? -31.53500 31.96800 -8.92000  1.000 43.24576  ? 424  TRP A CZ3 1 
ATOM   3406 C  CH2 . TRP A 1 424 ? -31.79500 31.96300 -10.29700 1.000 48.06573  ? 424  TRP A CH2 1 
ATOM   3407 N  N   . PRO A 1 425 ? -29.77000 37.40500 -8.16200  1.000 45.95692  ? 425  PRO A N   1 
ATOM   3408 C  CA  . PRO A 1 425 ? -29.33100 38.52400 -9.00700  1.000 42.74473  ? 425  PRO A CA  1 
ATOM   3409 C  C   . PRO A 1 425 ? -30.36100 38.82300 -10.08700 1.000 49.03602  ? 425  PRO A C   1 
ATOM   3410 O  O   . PRO A 1 425 ? -30.82800 37.92100 -10.78600 1.000 42.87319  ? 425  PRO A O   1 
ATOM   3411 C  CB  . PRO A 1 425 ? -28.01000 38.02500 -9.60300  1.000 46.52662  ? 425  PRO A CB  1 
ATOM   3412 C  CG  . PRO A 1 425 ? -28.12000 36.53400 -9.56000  1.000 47.54389  ? 425  PRO A CG  1 
ATOM   3413 C  CD  . PRO A 1 425 ? -28.92600 36.20900 -8.33500  1.000 36.31596  ? 425  PRO A CD  1 
ATOM   3414 N  N   . ASP A 1 426 ? -30.71200 40.10400 -10.22000 1.000 51.62852  ? 426  ASP A N   1 
ATOM   3415 C  CA  . ASP A 1 426 ? -31.73400 40.49600 -11.18300 1.000 45.51811  ? 426  ASP A CA  1 
ATOM   3416 C  C   . ASP A 1 426 ? -31.30300 40.24400 -12.62100 1.000 51.79129  ? 426  ASP A C   1 
ATOM   3417 O  O   . ASP A 1 426 ? -32.16200 40.12500 -13.50300 1.000 47.48568  ? 426  ASP A O   1 
ATOM   3418 C  CB  . ASP A 1 426 ? -32.09600 41.96800 -10.99500 1.000 40.62698  ? 426  ASP A CB  1 
ATOM   3419 C  CG  . ASP A 1 426 ? -32.91000 42.21100 -9.74400  1.000 48.91593  ? 426  ASP A CG  1 
ATOM   3420 O  OD1 . ASP A 1 426 ? -33.33400 41.22400 -9.10600  1.000 52.90747  ? 426  ASP A OD1 1 
ATOM   3421 O  OD2 . ASP A 1 426 ? -33.12700 43.39000 -9.39700  1.000 42.53893  ? 426  ASP A OD2 1 
ATOM   3422 N  N   . ASP A 1 427 ? -30.00200 40.16100 -12.88300 1.000 56.47655  ? 427  ASP A N   1 
ATOM   3423 C  CA  . ASP A 1 427 ? -29.50300 39.82100 -14.20700 1.000 53.48879  ? 427  ASP A CA  1 
ATOM   3424 C  C   . ASP A 1 427 ? -29.23400 38.32900 -14.36400 1.000 48.77067  ? 427  ASP A C   1 
ATOM   3425 O  O   . ASP A 1 427 ? -28.72500 37.91100 -15.41000 1.000 55.60913  ? 427  ASP A O   1 
ATOM   3426 C  CB  . ASP A 1 427 ? -28.23800 40.62600 -14.51900 1.000 45.34358  ? 427  ASP A CB  1 
ATOM   3427 C  CG  . ASP A 1 427 ? -27.15000 40.43500 -13.48100 1.000 56.79247  ? 427  ASP A CG  1 
ATOM   3428 O  OD1 . ASP A 1 427 ? -27.37900 39.70500 -12.49200 1.000 59.39547  ? 427  ASP A OD1 1 
ATOM   3429 O  OD2 . ASP A 1 427 ? -26.05900 41.01900 -13.65300 1.000 64.07240  ? 427  ASP A OD2 1 
ATOM   3430 N  N   . LYS A 1 428 ? -29.56700 37.52600 -13.35200 1.000 56.03718  ? 428  LYS A N   1 
ATOM   3431 C  CA  . LYS A 1 428 ? -29.39700 36.07400 -13.38900 1.000 50.22013  ? 428  LYS A CA  1 
ATOM   3432 C  C   . LYS A 1 428 ? -27.95000 35.70300 -13.70300 1.000 53.11448  ? 428  LYS A C   1 
ATOM   3433 O  O   . LYS A 1 428 ? -27.66600 34.83400 -14.53000 1.000 56.20201  ? 428  LYS A O   1 
ATOM   3434 C  CB  . LYS A 1 428 ? -30.36400 35.43700 -14.38900 1.000 50.25828  ? 428  LYS A CB  1 
ATOM   3435 C  CG  . LYS A 1 428 ? -31.83000 35.70100 -14.07600 1.000 53.58342  ? 428  LYS A CG  1 
ATOM   3436 C  CD  . LYS A 1 428 ? -32.74800 35.31500 -15.23400 1.000 49.53477  ? 428  LYS A CD  1 
ATOM   3437 C  CE  . LYS A 1 428 ? -32.86500 33.80700 -15.39000 1.000 53.25290  ? 428  LYS A CE  1 
ATOM   3438 N  NZ  . LYS A 1 428 ? -33.91400 33.43100 -16.37700 1.000 55.34230  ? 428  LYS A NZ  1 
ATOM   3439 N  N   . HIS A 1 429 ? -27.05000 36.43100 -13.06100 1.000 51.54950  ? 429  HIS A N   1 
ATOM   3440 C  CA  . HIS A 1 429 ? -25.61300 36.18600 -13.28800 1.000 57.74870  ? 429  HIS A CA  1 
ATOM   3441 C  C   . HIS A 1 429 ? -24.87500 36.08900 -11.95100 1.000 54.04557  ? 429  HIS A C   1 
ATOM   3442 O  O   . HIS A 1 429 ? -25.25400 36.79500 -11.02000 1.000 55.11600  ? 429  HIS A O   1 
ATOM   3443 C  CB  . HIS A 1 429 ? -25.02400 37.27000 -14.19000 1.000 50.22110  ? 429  HIS A CB  1 
ATOM   3444 C  CG  . HIS A 1 429 ? -23.69700 36.91800 -14.76400 1.000 63.83212  ? 429  HIS A CG  1 
ATOM   3445 N  ND1 . HIS A 1 429 ? -23.57500 36.18600 -15.92300 1.000 66.87887  ? 429  HIS A ND1 1 
ATOM   3446 C  CD2 . HIS A 1 429 ? -22.44400 37.19400 -14.35400 1.000 58.38318  ? 429  HIS A CD2 1 
ATOM   3447 C  CE1 . HIS A 1 429 ? -22.30200 36.02000 -16.20000 1.000 66.61650  ? 429  HIS A CE1 1 
ATOM   3448 N  NE2 . HIS A 1 429 ? -21.59000 36.62900 -15.25600 1.000 67.08361  ? 429  HIS A NE2 1 
ATOM   3449 N  N   . VAL A 1 430 ? -23.85700 35.24600 -11.89300 1.000 55.25453  ? 430  VAL A N   1 
ATOM   3450 C  CA  . VAL A 1 430 ? -23.01600 35.05600 -10.71700 1.000 50.22427  ? 430  VAL A CA  1 
ATOM   3451 C  C   . VAL A 1 430 ? -21.56100 35.05400 -11.16500 1.000 54.88325  ? 430  VAL A C   1 
ATOM   3452 O  O   . VAL A 1 430 ? -21.19100 34.31800 -12.08500 1.000 57.15724  ? 430  VAL A O   1 
ATOM   3453 C  CB  . VAL A 1 430 ? -23.35300 33.74800 -9.97400  1.000 57.42185  ? 430  VAL A CB  1 
ATOM   3454 C  CG1 . VAL A 1 430 ? -22.41400 33.54800 -8.79400  1.000 45.75984  ? 430  VAL A CG1 1 
ATOM   3455 C  CG2 . VAL A 1 430 ? -24.80300 33.75300 -9.51600  1.000 43.19515  ? 430  VAL A CG2 1 
ATOM   3456 N  N   . SER A 1 431 ? -20.73700 35.87200 -10.51500 1.000 52.88050  ? 431  SER A N   1 
ATOM   3457 C  CA  . SER A 1 431 ? -19.32100 35.98000 -10.84200 1.000 55.57883  ? 431  SER A CA  1 
ATOM   3458 C  C   . SER A 1 431 ? -18.50300 35.49600 -9.65500  1.000 51.79063  ? 431  SER A C   1 
ATOM   3459 O  O   . SER A 1 431 ? -18.62900 36.03400 -8.54900  1.000 54.57372  ? 431  SER A O   1 
ATOM   3460 C  CB  . SER A 1 431 ? -18.94700 37.42000 -11.20600 1.000 56.42386  ? 431  SER A CB  1 
ATOM   3461 O  OG  . SER A 1 431 ? -19.67200 37.86900 -12.33800 1.000 56.35338  ? 431  SER A OG  1 
ATOM   3462 N  N   . ILE A 1 432 ? -17.67100 34.48600 -9.88100  1.000 47.57370  ? 432  ILE A N   1 
ATOM   3463 C  CA  . ILE A 1 432 ? -16.79600 33.93700 -8.85100  1.000 51.57464  ? 432  ILE A CA  1 
ATOM   3464 C  C   . ILE A 1 432 ? -15.38000 34.38700 -9.18900  1.000 55.01897  ? 432  ILE A C   1 
ATOM   3465 O  O   . ILE A 1 432 ? -14.71600 33.79800 -10.04900 1.000 55.13425  ? 432  ILE A O   1 
ATOM   3466 C  CB  . ILE A 1 432 ? -16.90400 32.41200 -8.76100  1.000 51.25258  ? 432  ILE A CB  1 
ATOM   3467 C  CG1 . ILE A 1 432 ? -18.33900 32.00600 -8.41600  1.000 51.95203  ? 432  ILE A CG1 1 
ATOM   3468 C  CG2 . ILE A 1 432 ? -15.93100 31.86800 -7.72400  1.000 48.91392  ? 432  ILE A CG2 1 
ATOM   3469 C  CD1 . ILE A 1 432 ? -18.56000 30.51200 -8.38200  1.000 43.23088  ? 432  ILE A CD1 1 
ATOM   3470 N  N   . ALA A 1 433 ? -14.91100 35.43700 -8.50900  1.000 57.13930  ? 433  ALA A N   1 
ATOM   3471 C  CA  . ALA A 1 433 ? -13.62800 36.03500 -8.86700  1.000 51.40149  ? 433  ALA A CA  1 
ATOM   3472 C  C   . ALA A 1 433 ? -12.46900 35.08800 -8.58300  1.000 56.34907  ? 433  ALA A C   1 
ATOM   3473 O  O   . ALA A 1 433 ? -11.48600 35.05300 -9.33300  1.000 60.74155  ? 433  ALA A O   1 
ATOM   3474 C  CB  . ALA A 1 433 ? -13.43800 37.35300 -8.11800  1.000 43.89356  ? 433  ALA A CB  1 
ATOM   3475 N  N   . SER A 1 434 ? -12.56900 34.30800 -7.51700  1.000 59.51683  ? 434  SER A N   1 
ATOM   3476 C  CA  . SER A 1 434 ? -11.49900 33.39200 -7.13900  1.000 56.47462  ? 434  SER A CA  1 
ATOM   3477 C  C   . SER A 1 434 ? -11.37800 32.17800 -8.07100  1.000 58.47729  ? 434  SER A C   1 
ATOM   3478 O  O   . SER A 1 434 ? -10.54800 31.30600 -7.79000  1.000 68.50755  ? 434  SER A O   1 
ATOM   3479 C  CB  . SER A 1 434 ? -11.70300 32.92500 -5.69600  1.000 54.39158  ? 434  SER A CB  1 
ATOM   3480 O  OG  . SER A 1 434 ? -13.02500 32.46700 -5.49300  1.000 67.41578  ? 434  SER A OG  1 
ATOM   3481 N  N   . LEU A 1 435 ? -12.23800 32.04000 -9.07600  1.000 60.60989  ? 435  LEU A N   1 
ATOM   3482 C  CA  . LEU A 1 435 ? -12.08500 30.91100 -10.03200 1.000 56.86467  ? 435  LEU A CA  1 
ATOM   3483 C  C   . LEU A 1 435 ? -11.81300 31.47700 -11.41900 1.000 64.35748  ? 435  LEU A C   1 
ATOM   3484 O  O   . LEU A 1 435 ? -12.07100 30.78200 -12.40600 1.000 67.35699  ? 435  LEU A O   1 
ATOM   3485 C  CB  . LEU A 1 435 ? -13.32200 30.01900 -10.00800 1.000 51.71790  ? 435  LEU A CB  1 
ATOM   3486 C  CG  . LEU A 1 435 ? -13.51200 29.20600 -8.73100  1.000 57.57754  ? 435  LEU A CG  1 
ATOM   3487 C  CD1 . LEU A 1 435 ? -14.63800 28.20100 -8.89500  1.000 42.92678  ? 435  LEU A CD1 1 
ATOM   3488 C  CD2 . LEU A 1 435 ? -12.22000 28.50000 -8.35300  1.000 57.99468  ? 435  LEU A CD2 1 
ATOM   3489 N  N   . GLY A 1 436 ? -11.28600 32.69400 -11.46100 1.000 74.29255  ? 436  GLY A N   1 
ATOM   3490 C  CA  . GLY A 1 436 ? -10.91800 33.32400 -12.73800 1.000 78.51667  ? 436  GLY A CA  1 
ATOM   3491 C  C   . GLY A 1 436 ? -9.53700  32.91100 -13.19200 1.000 80.18308  ? 436  GLY A C   1 
ATOM   3492 O  O   . GLY A 1 436 ? -8.88000  32.16100 -12.46600 1.000 79.65442  ? 436  GLY A O   1 
ATOM   3493 N  N   . SER A 1 437 ? -9.13000  33.36600 -14.37200 1.000 81.66022  ? 437  SER A N   1 
ATOM   3494 C  CA  . SER A 1 437 ? -7.81100  33.00100 -14.92900 1.000 74.86406  ? 437  SER A CA  1 
ATOM   3495 C  C   . SER A 1 437 ? -6.73500  33.73700 -14.14500 1.000 79.94860  ? 437  SER A C   1 
ATOM   3496 O  O   . SER A 1 437 ? -5.65300  33.16900 -13.95900 1.000 79.12479  ? 437  SER A O   1 
ATOM   3497 C  CB  . SER A 1 437 ? -7.75000  33.34900 -16.38000 1.000 59.33210  ? 437  SER A CB  1 
ATOM   3498 N  N   . ASP A 1 438 ? -7.02800  34.96400 -13.72200 1.000 78.89402  ? 438  ASP A N   1 
ATOM   3499 C  CA  . ASP A 1 438 ? -6.05000  35.65900 -12.89400 1.000 77.30436  ? 438  ASP A CA  1 
ATOM   3500 C  C   . ASP A 1 438 ? -5.76700  34.92000 -11.59300 1.000 74.18340  ? 438  ASP A C   1 
ATOM   3501 O  O   . ASP A 1 438 ? -4.72900  35.16500 -10.97000 1.000 71.84121  ? 438  ASP A O   1 
ATOM   3502 C  CB  . ASP A 1 438 ? -6.52500  37.08100 -12.59300 1.000 76.90547  ? 438  ASP A CB  1 
ATOM   3503 C  CG  . ASP A 1 438 ? -6.64700  37.93200 -13.84200 1.000 92.04129  ? 438  ASP A CG  1 
ATOM   3504 O  OD1 . ASP A 1 438 ? -6.25000  37.45800 -14.92700 1.000 102.09065 ? 438  ASP A OD1 1 
ATOM   3505 O  OD2 . ASP A 1 438 ? -7.14600  39.07300 -13.74100 1.000 95.90901  ? 438  ASP A OD2 1 
ATOM   3506 N  N   . ALA A 1 439 ? -6.66000  34.02800 -11.17100 1.000 76.48595  ? 439  ALA A N   1 
ATOM   3507 C  CA  . ALA A 1 439 ? -6.44500  33.21700 -9.98100  1.000 63.96893  ? 439  ALA A CA  1 
ATOM   3508 C  C   . ALA A 1 439 ? -5.59000  31.98700 -10.25300 1.000 76.17564  ? 439  ALA A C   1 
ATOM   3509 O  O   . ALA A 1 439 ? -5.44500  31.14600 -9.35800  1.000 79.00324  ? 439  ALA A O   1 
ATOM   3510 C  CB  . ALA A 1 439 ? -7.78700  32.79200 -9.38200  1.000 64.93071  ? 439  ALA A CB  1 
ATOM   3511 N  N   . LEU A 1 440 ? -5.05800  31.87000 -11.47400 1.000 70.45983  ? 440  LEU A N   1 
ATOM   3512 C  CA  . LEU A 1 440 ? -4.18600  30.72400 -11.85900 1.000 77.49825  ? 440  LEU A CA  1 
ATOM   3513 C  C   . LEU A 1 440 ? -4.96400  29.43200 -11.65000 1.000 73.23608  ? 440  LEU A C   1 
ATOM   3514 O  O   . LEU A 1 440 ? -4.36200  28.45200 -11.18800 1.000 79.86085  ? 440  LEU A O   1 
ATOM   3515 C  CB  . LEU A 1 440 ? -2.89300  30.76200 -11.04100 1.000 82.78808  ? 440  LEU A CB  1 
ATOM   3516 C  CG  . LEU A 1 440 ? -2.13900  32.08800 -11.08900 1.000 79.30107  ? 440  LEU A CG  1 
ATOM   3517 C  CD1 . LEU A 1 440 ? -0.90300  32.04400 -10.20800 1.000 85.26883  ? 440  LEU A CD1 1 
ATOM   3518 C  CD2 . LEU A 1 440 ? -1.76200  32.44300 -12.51700 1.000 73.62526  ? 440  LEU A CD2 1 
ATOM   3519 N  N   . VAL A 1 441 ? -6.23600  29.43300 -12.01200 1.000 66.42421  ? 441  VAL A N   1 
ATOM   3520 C  CA  . VAL A 1 441 ? -7.12700  28.28900 -11.86300 1.000 69.27042  ? 441  VAL A CA  1 
ATOM   3521 C  C   . VAL A 1 441 ? -7.46400  27.75200 -13.24600 1.000 78.10725  ? 441  VAL A C   1 
ATOM   3522 O  O   . VAL A 1 441 ? -7.92000  28.50300 -14.11700 1.000 74.12111  ? 441  VAL A O   1 
ATOM   3523 C  CB  . VAL A 1 441 ? -8.40600  28.67300 -11.09800 1.000 70.00270  ? 441  VAL A CB  1 
ATOM   3524 C  CG1 . VAL A 1 441 ? -9.47700  27.61100 -11.28100 1.000 73.23570  ? 441  VAL A CG1 1 
ATOM   3525 C  CG2 . VAL A 1 441 ? -8.10000  28.87400 -9.62700  1.000 66.84159  ? 441  VAL A CG2 1 
ATOM   3526 N  N   . ASP A 1 442 ? -7.33600  26.43600 -13.42400 1.000 68.65615  ? 442  ASP A N   1 
ATOM   3527 C  CA  . ASP A 1 442 ? -7.74600  25.80300 -14.70200 1.000 66.32526  ? 442  ASP A CA  1 
ATOM   3528 C  C   . ASP A 1 442 ? -9.02900  25.01100 -14.44600 1.000 79.99891  ? 442  ASP A C   1 
ATOM   3529 O  O   . ASP A 1 442 ? -8.98700  24.09400 -13.61600 1.000 72.86435  ? 442  ASP A O   1 
ATOM   3530 C  CB  . ASP A 1 442 ? -6.63000  24.94200 -15.28100 1.000 71.66300  ? 442  ASP A CB  1 
ATOM   3531 C  CG  . ASP A 1 442 ? -7.00200  24.20100 -16.55300 1.000 90.28950  ? 442  ASP A CG  1 
ATOM   3532 O  OD1 . ASP A 1 442 ? -8.14200  24.36500 -17.02200 1.000 88.45279  ? 442  ASP A OD1 1 
ATOM   3533 O  OD2 . ASP A 1 442 ? -6.14000  23.46200 -17.06600 1.000 92.47195  ? 442  ASP A OD2 1 
ATOM   3534 N  N   . LEU A 1 443 ? -10.11600 25.33700 -15.15300 1.000 73.33393  ? 443  LEU A N   1 
ATOM   3535 C  CA  . LEU A 1 443 ? -11.42200 24.69200 -14.87200 1.000 69.40076  ? 443  LEU A CA  1 
ATOM   3536 C  C   . LEU A 1 443 ? -11.65500 23.53400 -15.83500 1.000 73.94103  ? 443  LEU A C   1 
ATOM   3537 O  O   . LEU A 1 443 ? -12.80300 23.11600 -15.98600 1.000 80.91591  ? 443  LEU A O   1 
ATOM   3538 C  CB  . LEU A 1 443 ? -12.52000 25.74800 -14.97600 1.000 64.61351  ? 443  LEU A CB  1 
ATOM   3539 C  CG  . LEU A 1 443 ? -12.44300 26.87800 -13.95200 1.000 70.35734  ? 443  LEU A CG  1 
ATOM   3540 C  CD1 . LEU A 1 443 ? -13.46300 27.96100 -14.26300 1.000 68.15675  ? 443  LEU A CD1 1 
ATOM   3541 C  CD2 . LEU A 1 443 ? -12.64500 26.34500 -12.54500 1.000 61.37648  ? 443  LEU A CD2 1 
ATOM   3542 N  N   . LYS A 1 444 ? -10.58900 23.02600 -16.43400 1.000 76.81576  ? 444  LYS A N   1 
ATOM   3543 C  CA  . LYS A 1 444 ? -10.72000 21.84800 -17.31700 1.000 75.61365  ? 444  LYS A CA  1 
ATOM   3544 C  C   . LYS A 1 444 ? -11.37800 20.73400 -16.52700 1.000 71.63798  ? 444  LYS A C   1 
ATOM   3545 O  O   . LYS A 1 444 ? -12.14500 19.96400 -17.12100 1.000 76.77861  ? 444  LYS A O   1 
ATOM   3546 C  CB  . LYS A 1 444 ? -9.34200  21.38200 -17.77300 1.000 70.89617  ? 444  LYS A CB  1 
ATOM   3547 N  N   . SER A 1 445 ? -11.06900 20.65800 -15.23600 1.000 75.36712  ? 445  SER A N   1 
ATOM   3548 C  CA  . SER A 1 445 ? -11.59800 19.56200 -14.43800 1.000 80.38509  ? 445  SER A CA  1 
ATOM   3549 C  C   . SER A 1 445 ? -13.01500 19.81500 -13.93900 1.000 74.77681  ? 445  SER A C   1 
ATOM   3550 O  O   . SER A 1 445 ? -13.58500 18.94500 -13.27300 1.000 69.11557  ? 445  SER A O   1 
ATOM   3551 C  CB  . SER A 1 445 ? -10.67400 19.29200 -13.24700 1.000 66.26472  ? 445  SER A CB  1 
ATOM   3552 O  OG  . SER A 1 445 ? -10.56500 20.43300 -12.41500 1.000 70.62671  ? 445  SER A OG  1 
ATOM   3553 N  N   . LEU A 1 446 ? -13.58300 20.96400 -14.30700 1.000 64.44678  ? 446  LEU A N   1 
ATOM   3554 C  CA  . LEU A 1 446 ? -14.95700 21.31400 -13.87300 1.000 61.45374  ? 446  LEU A CA  1 
ATOM   3555 C  C   . LEU A 1 446 ? -15.94200 20.50100 -14.70000 1.000 66.55217  ? 446  LEU A C   1 
ATOM   3556 O  O   . LEU A 1 446 ? -16.02500 20.73100 -15.90900 1.000 79.83042  ? 446  LEU A O   1 
ATOM   3557 C  CB  . LEU A 1 446 ? -15.22000 22.81200 -13.99100 1.000 68.41859  ? 446  LEU A CB  1 
ATOM   3558 C  CG  . LEU A 1 446 ? -16.59200 23.30600 -13.52100 1.000 66.05786  ? 446  LEU A CG  1 
ATOM   3559 C  CD1 . LEU A 1 446 ? -17.02900 22.64600 -12.22700 1.000 64.15830  ? 446  LEU A CD1 1 
ATOM   3560 C  CD2 . LEU A 1 446 ? -16.56200 24.81200 -13.35800 1.000 58.75342  ? 446  LEU A CD2 1 
ATOM   3561 N  N   . LYS A 1 447 ? -16.67900 19.60700 -14.06200 1.000 64.41393  ? 447  LYS A N   1 
ATOM   3562 C  CA  . LYS A 1 447 ? -17.56400 18.70100 -14.83000 1.000 69.96414  ? 447  LYS A CA  1 
ATOM   3563 C  C   . LYS A 1 447 ? -19.00900 19.19400 -14.80500 1.000 66.38193  ? 447  LYS A C   1 
ATOM   3564 O  O   . LYS A 1 447 ? -19.76100 18.81500 -15.71000 1.000 65.55895  ? 447  LYS A O   1 
ATOM   3565 C  CB  . LYS A 1 447 ? -17.48000 17.28700 -14.26100 1.000 64.18648  ? 447  LYS A CB  1 
ATOM   3566 C  CG  . LYS A 1 447 ? -16.15100 16.58100 -14.48700 1.000 74.22841  ? 447  LYS A CG  1 
ATOM   3567 C  CD  . LYS A 1 447 ? -15.38200 17.12800 -15.67000 1.000 86.75923  ? 447  LYS A CD  1 
ATOM   3568 C  CE  . LYS A 1 447 ? -15.54700 16.30100 -16.92700 1.000 67.32705  ? 447  LYS A CE  1 
ATOM   3569 N  NZ  . LYS A 1 447 ? -14.85600 16.92000 -18.08200 1.000 63.58731  ? 447  LYS A NZ  1 
ATOM   3570 N  N   . SER A 1 448 ? -19.38400 19.98200 -13.80100 1.000 63.07372  ? 448  SER A N   1 
ATOM   3571 C  CA  . SER A 1 448 ? -20.81000 20.37500 -13.72500 1.000 55.91137  ? 448  SER A CA  1 
ATOM   3572 C  C   . SER A 1 448 ? -21.08900 21.51500 -12.75900 1.000 56.12260  ? 448  SER A C   1 
ATOM   3573 O  O   . SER A 1 448 ? -20.56200 21.49000 -11.64700 1.000 65.72498  ? 448  SER A O   1 
ATOM   3574 C  CB  . SER A 1 448 ? -21.67600 19.20600 -13.37000 1.000 62.02352  ? 448  SER A CB  1 
ATOM   3575 O  OG  . SER A 1 448 ? -21.71500 19.00800 -11.96800 1.000 73.98772  ? 448  SER A OG  1 
ATOM   3576 N  N   . ILE A 1 449 ? -21.87200 22.48800 -13.20500 1.000 60.29110  ? 449  ILE A N   1 
ATOM   3577 C  CA  . ILE A 1 449 ? -22.37600 23.53700 -12.32800 1.000 55.38809  ? 449  ILE A CA  1 
ATOM   3578 C  C   . ILE A 1 449 ? -23.89300 23.43500 -12.31900 1.000 61.41725  ? 449  ILE A C   1 
ATOM   3579 O  O   . ILE A 1 449 ? -24.52500 23.45200 -13.38100 1.000 68.25008  ? 449  ILE A O   1 
ATOM   3580 C  CB  . ILE A 1 449 ? -21.93700 24.94300 -12.78000 1.000 49.82607  ? 449  ILE A CB  1 
ATOM   3581 C  CG1 . ILE A 1 449 ? -20.41300 25.04100 -12.86000 1.000 60.59017  ? 449  ILE A CG1 1 
ATOM   3582 C  CG2 . ILE A 1 449 ? -22.48800 25.99200 -11.83400 1.000 49.95855  ? 449  ILE A CG2 1 
ATOM   3583 C  CD1 . ILE A 1 449 ? -19.92900 26.39800 -13.31500 1.000 52.06989  ? 449  ILE A CD1 1 
ATOM   3584 N  N   . GLU A 1 450 ? -24.47500 23.32300 -11.12800 1.000 63.43949  ? 450  GLU A N   1 
ATOM   3585 C  CA  . GLU A 1 450 ? -25.90900 23.13800 -10.97100 1.000 54.38607  ? 450  GLU A CA  1 
ATOM   3586 C  C   . GLU A 1 450 ? -26.46000 24.17600 -10.00400 1.000 50.51352  ? 450  GLU A C   1 
ATOM   3587 O  O   . GLU A 1 450 ? -25.73100 24.73700 -9.18500  1.000 51.95429  ? 450  GLU A O   1 
ATOM   3588 C  CB  . GLU A 1 450 ? -26.24000 21.73000 -10.45100 1.000 54.11084  ? 450  GLU A CB  1 
ATOM   3589 C  CG  . GLU A 1 450 ? -25.80200 20.59900 -11.36500 1.000 61.65568  ? 450  GLU A CG  1 
ATOM   3590 C  CD  . GLU A 1 450 ? -25.81500 19.25200 -10.66800 1.000 53.55507  ? 450  GLU A CD  1 
ATOM   3591 O  OE1 . GLU A 1 450 ? -25.16700 19.12300 -9.60900  1.000 51.39698  ? 450  GLU A OE1 1 
ATOM   3592 O  OE2 . GLU A 1 450 ? -26.47700 18.32400 -11.17600 1.000 59.05599  ? 450  GLU A OE2 1 
ATOM   3593 N  N   . LEU A 1 451 ? -27.77200 24.37500 -10.07200 1.000 53.09902  ? 451  LEU A N   1 
ATOM   3594 C  CA  . LEU A 1 451 ? -28.46100 25.26700 -9.11700  1.000 49.68806  ? 451  LEU A CA  1 
ATOM   3595 C  C   . LEU A 1 451 ? -29.44900 24.37900 -8.37000  1.000 51.24273  ? 451  LEU A C   1 
ATOM   3596 O  O   . LEU A 1 451 ? -30.23300 23.67800 -9.02300  1.000 46.46513  ? 451  LEU A O   1 
ATOM   3597 C  CB  . LEU A 1 451 ? -29.19100 26.45500 -9.73500  1.000 50.98122  ? 451  LEU A CB  1 
ATOM   3598 C  CG  . LEU A 1 451 ? -30.00500 27.31500 -8.76900  1.000 47.95829  ? 451  LEU A CG  1 
ATOM   3599 C  CD1 . LEU A 1 451 ? -29.08200 28.28600 -8.06700  1.000 42.98864  ? 451  LEU A CD1 1 
ATOM   3600 C  CD2 . LEU A 1 451 ? -31.07300 28.05600 -9.54300  1.000 50.28166  ? 451  LEU A CD2 1 
ATOM   3601 N  N   . LEU A 1 452 ? -29.42100 24.45400 -7.04900  1.000 42.20359  ? 452  LEU A N   1 
ATOM   3602 C  CA  . LEU A 1 452 ? -30.30800 23.59800 -6.23500  1.000 44.88370  ? 452  LEU A CA  1 
ATOM   3603 C  C   . LEU A 1 452 ? -31.73900 24.10700 -6.37900  1.000 42.01224  ? 452  LEU A C   1 
ATOM   3604 O  O   . LEU A 1 452 ? -31.93400 25.32300 -6.36600  1.000 42.69076  ? 452  LEU A O   1 
ATOM   3605 C  CB  . LEU A 1 452 ? -29.84400 23.48800 -4.78500  1.000 38.46567  ? 452  LEU A CB  1 
ATOM   3606 C  CG  . LEU A 1 452 ? -28.64000 22.57700 -4.51900  1.000 41.88569  ? 452  LEU A CG  1 
ATOM   3607 C  CD1 . LEU A 1 452 ? -27.36200 22.98700 -5.21700  1.000 40.78394  ? 452  LEU A CD1 1 
ATOM   3608 C  CD2 . LEU A 1 452 ? -28.41000 22.41500 -3.03200  1.000 37.94694  ? 452  LEU A CD2 1 
ATOM   3609 N  N   . GLY A 1 453 ? -32.69000 23.19000 -6.46400  1.000 43.56086  ? 453  GLY A N   1 
ATOM   3610 C  CA  . GLY A 1 453 ? -34.07400 23.58200 -6.75000  1.000 45.89902  ? 453  GLY A CA  1 
ATOM   3611 C  C   . GLY A 1 453 ? -34.98000 23.70600 -5.56200  1.000 50.30673  ? 453  GLY A C   1 
ATOM   3612 O  O   . GLY A 1 453 ? -34.49500 24.05600 -4.47900  1.000 50.94449  ? 453  GLY A O   1 
ATOM   3613 N  N   . ASP A 1 454 ? -36.25700 23.41900 -5.76400  1.000 43.20805  ? 454  ASP A N   1 
ATOM   3614 C  CA  . ASP A 1 454 ? -37.26800 23.64900 -4.70900  1.000 49.08440  ? 454  ASP A CA  1 
ATOM   3615 C  C   . ASP A 1 454 ? -37.19900 22.59200 -3.60600  1.000 48.71700  ? 454  ASP A C   1 
ATOM   3616 O  O   . ASP A 1 454 ? -37.60600 22.89300 -2.47700  1.000 50.45123  ? 454  ASP A O   1 
ATOM   3617 C  CB  . ASP A 1 454 ? -38.64200 23.70700 -5.35100  1.000 57.50901  ? 454  ASP A CB  1 
ATOM   3618 C  CG  . ASP A 1 454 ? -38.81200 24.70000 -6.48900  1.000 58.92410  ? 454  ASP A CG  1 
ATOM   3619 O  OD1 . ASP A 1 454 ? -37.82700 25.38300 -6.82300  1.000 63.42535  ? 454  ASP A OD1 1 
ATOM   3620 O  OD2 . ASP A 1 454 ? -39.93200 24.77800 -7.02600  1.000 50.98801  ? 454  ASP A OD2 1 
ATOM   3621 N  N   . LYS A 1 455 ? -36.76100 21.38800 -3.94600  1.000 52.59736  ? 455  LYS A N   1 
ATOM   3622 C  CA  . LYS A 1 455 ? -36.66900 20.30300 -2.94600  1.000 48.08935  ? 455  LYS A CA  1 
ATOM   3623 C  C   . LYS A 1 455 ? -35.28900 19.66000 -3.03400  1.000 49.70815  ? 455  LYS A C   1 
ATOM   3624 O  O   . LYS A 1 455 ? -34.65200 19.73200 -4.08700  1.000 50.55416  ? 455  LYS A O   1 
ATOM   3625 C  CB  . LYS A 1 455 ? -37.76500 19.24900 -3.11200  1.000 58.17961  ? 455  LYS A CB  1 
ATOM   3626 C  CG  . LYS A 1 455 ? -39.19200 19.73200 -2.91900  1.000 67.12744  ? 455  LYS A CG  1 
ATOM   3627 C  CD  . LYS A 1 455 ? -40.22000 18.61800 -3.07400  1.000 53.40704  ? 455  LYS A CD  1 
ATOM   3628 N  N   . ALA A 1 456 ? -34.85700 19.07000 -1.93100  1.000 55.23592  ? 456  ALA A N   1 
ATOM   3629 C  CA  . ALA A 1 456 ? -33.53000 18.42300 -1.87700  1.000 49.20660  ? 456  ALA A CA  1 
ATOM   3630 C  C   . ALA A 1 456 ? -33.41600 17.31900 -2.92600  1.000 56.26911  ? 456  ALA A C   1 
ATOM   3631 O  O   . ALA A 1 456 ? -34.33500 16.50400 -3.04800  1.000 58.12320  ? 456  ALA A O   1 
ATOM   3632 C  CB  . ALA A 1 456 ? -33.32100 17.90100 -0.48800  1.000 43.70814  ? 456  ALA A CB  1 
ATOM   3633 N  N   . GLY A 1 457 ? -32.31300 17.31200 -3.65500  1.000 53.72755  ? 457  GLY A N   1 
ATOM   3634 C  CA  . GLY A 1 457 ? -32.07800 16.33300 -4.72500  1.000 45.66929  ? 457  GLY A CA  1 
ATOM   3635 C  C   . GLY A 1 457 ? -32.58300 16.82600 -6.06100  1.000 50.50071  ? 457  GLY A C   1 
ATOM   3636 O  O   . GLY A 1 457 ? -32.23700 16.20300 -7.06700  1.000 62.43427  ? 457  GLY A O   1 
ATOM   3637 N  N   . GLU A 1 458 ? -33.35500 17.90800 -6.08400  1.000 50.76940  ? 458  GLU A N   1 
ATOM   3638 C  CA  . GLU A 1 458 ? -33.76900 18.52400 -7.36800  1.000 47.75159  ? 458  GLU A CA  1 
ATOM   3639 C  C   . GLU A 1 458 ? -32.68300 19.52400 -7.78500  1.000 48.82385  ? 458  GLU A C   1 
ATOM   3640 O  O   . GLU A 1 458 ? -32.46000 20.48600 -7.04400  1.000 49.46362  ? 458  GLU A O   1 
ATOM   3641 C  CB  . GLU A 1 458 ? -35.13200 19.20300 -7.27600  1.000 46.85614  ? 458  GLU A CB  1 
ATOM   3642 C  CG  . GLU A 1 458 ? -36.26900 18.27100 -6.87500  1.000 63.97407  ? 458  GLU A CG  1 
ATOM   3643 C  CD  . GLU A 1 458 ? -37.60900 18.97700 -6.79800  1.000 65.22780  ? 458  GLU A CD  1 
ATOM   3644 O  OE1 . GLU A 1 458 ? -37.64100 20.19600 -7.05300  1.000 55.42597  ? 458  GLU A OE1 1 
ATOM   3645 O  OE2 . GLU A 1 458 ? -38.61700 18.31200 -6.49300  1.000 69.69282  ? 458  GLU A OE2 1 
ATOM   3646 N  N   . TYR A 1 459 ? -32.00200 19.26900 -8.89500  1.000 52.02740  ? 459  TYR A N   1 
ATOM   3647 C  CA  . TYR A 1 459 ? -30.99600 20.21700 -9.42800  1.000 53.22991  ? 459  TYR A CA  1 
ATOM   3648 C  C   . TYR A 1 459 ? -31.39200 20.68200 -10.84300 1.000 60.82230  ? 459  TYR A C   1 
ATOM   3649 O  O   . TYR A 1 459 ? -32.15500 19.97900 -11.52700 1.000 52.44584  ? 459  TYR A O   1 
ATOM   3650 C  CB  . TYR A 1 459 ? -29.62600 19.54600 -9.47900  1.000 48.45259  ? 459  TYR A CB  1 
ATOM   3651 C  CG  . TYR A 1 459 ? -29.11100 18.88600 -8.21000  1.000 53.23618  ? 459  TYR A CG  1 
ATOM   3652 C  CD1 . TYR A 1 459 ? -28.37300 19.59900 -7.27500  1.000 45.35439  ? 459  TYR A CD1 1 
ATOM   3653 C  CD2 . TYR A 1 459 ? -29.33700 17.53900 -7.97100  1.000 52.35596  ? 459  TYR A CD2 1 
ATOM   3654 C  CE1 . TYR A 1 459 ? -27.89300 18.99200 -6.12800  1.000 49.47774  ? 459  TYR A CE1 1 
ATOM   3655 C  CE2 . TYR A 1 459 ? -28.86400 16.92100 -6.82800  1.000 51.64047  ? 459  TYR A CE2 1 
ATOM   3656 C  CZ  . TYR A 1 459 ? -28.14200 17.65000 -5.90500  1.000 49.72202  ? 459  TYR A CZ  1 
ATOM   3657 O  OH  . TYR A 1 459 ? -27.68500 17.02200 -4.78900  1.000 58.89490  ? 459  TYR A OH  1 
ATOM   3658 N  N   . GLU A 1 460 ? -30.91700 21.85500 -11.25000 1.000 58.53326  ? 460  GLU A N   1 
ATOM   3659 C  CA  . GLU A 1 460 ? -31.13100 22.31200 -12.64000 1.000 59.49159  ? 460  GLU A CA  1 
ATOM   3660 C  C   . GLU A 1 460 ? -29.78700 22.76500 -13.18100 1.000 57.20810  ? 460  GLU A C   1 
ATOM   3661 O  O   . GLU A 1 460 ? -29.16700 23.63500 -12.57000 1.000 52.75197  ? 460  GLU A O   1 
ATOM   3662 C  CB  . GLU A 1 460 ? -32.14600 23.44100 -12.77400 1.000 67.96711  ? 460  GLU A CB  1 
ATOM   3663 C  CG  . GLU A 1 460 ? -32.12800 24.06500 -14.15900 1.000 76.36210  ? 460  GLU A CG  1 
ATOM   3664 C  CD  . GLU A 1 460 ? -33.46300 24.55500 -14.69000 1.000 76.60126  ? 460  GLU A CD  1 
ATOM   3665 O  OE1 . GLU A 1 460 ? -34.39300 24.71200 -13.88500 1.000 89.03229  ? 460  GLU A OE1 1 
ATOM   3666 O  OE2 . GLU A 1 460 ? -33.56700 24.76700 -15.91200 1.000 72.50739  ? 460  GLU A OE2 1 
ATOM   3667 N  N   . GLN A 1 461 ? -29.39300 22.18600 -14.31100 1.000 77.08641  ? 461  GLN A N   1 
ATOM   3668 C  CA  . GLN A 1 461 ? -28.10400 22.51500 -14.89700 1.000 71.51484  ? 461  GLN A CA  1 
ATOM   3669 C  C   . GLN A 1 461 ? -28.01300 24.00800 -15.18900 1.000 69.03370  ? 461  GLN A C   1 
ATOM   3670 O  O   . GLN A 1 461 ? -29.00100 24.65800 -15.53700 1.000 68.06404  ? 461  GLN A O   1 
ATOM   3671 C  CB  . GLN A 1 461 ? -27.88700 21.71600 -16.18200 1.000 79.53631  ? 461  GLN A CB  1 
ATOM   3672 C  CG  . GLN A 1 461 ? -27.29900 20.33600 -15.96000 1.000 88.66645  ? 461  GLN A CG  1 
ATOM   3673 C  CD  . GLN A 1 461 ? -25.86000 20.39000 -15.48700 1.000 94.16437  ? 461  GLN A CD  1 
ATOM   3674 O  OE1 . GLN A 1 461 ? -25.13900 21.35000 -15.76100 1.000 89.23612  ? 461  GLN A OE1 1 
ATOM   3675 N  NE2 . GLN A 1 461 ? -25.43400 19.35700 -14.77000 1.000 97.41473  ? 461  GLN A NE2 1 
ATOM   3676 N  N   . VAL A 1 462 ? -26.80600 24.55200 -15.03400 1.000 64.81630  ? 462  VAL A N   1 
ATOM   3677 C  CA  . VAL A 1 462 ? -26.58900 25.96000 -15.32900 1.000 64.93650  ? 462  VAL A CA  1 
ATOM   3678 C  C   . VAL A 1 462 ? -26.73300 26.19100 -16.83000 1.000 78.34858  ? 462  VAL A C   1 
ATOM   3679 O  O   . VAL A 1 462 ? -26.44200 25.31100 -17.65200 1.000 84.07032  ? 462  VAL A O   1 
ATOM   3680 C  CB  . VAL A 1 462 ? -25.21000 26.41300 -14.81300 1.000 68.55772  ? 462  VAL A CB  1 
ATOM   3681 C  CG1 . VAL A 1 462 ? -24.08900 25.79200 -15.63700 1.000 75.69420  ? 462  VAL A CG1 1 
ATOM   3682 C  CG2 . VAL A 1 462 ? -25.11200 27.92300 -14.81200 1.000 68.67415  ? 462  VAL A CG2 1 
ATOM   3683 N  N   . SER A 1 463 ? -27.21500 27.38100 -17.19300 1.000 70.95686  ? 463  SER A N   1 
ATOM   3684 C  CA  . SER A 1 463 ? -27.43700 27.68900 -18.60300 1.000 76.63925  ? 463  SER A CA  1 
ATOM   3685 C  C   . SER A 1 463 ? -26.12000 27.74500 -19.36700 1.000 76.02763  ? 463  SER A C   1 
ATOM   3686 O  O   . SER A 1 463 ? -25.97900 27.12500 -20.42800 1.000 77.26678  ? 463  SER A O   1 
ATOM   3687 C  CB  . SER A 1 463 ? -28.19500 29.01000 -18.74000 1.000 66.18460  ? 463  SER A CB  1 
ATOM   3688 O  OG  . SER A 1 463 ? -29.45800 28.94300 -18.10100 1.000 73.01265  ? 463  SER A OG  1 
ATOM   3689 N  N   . ASP A 1 464 ? -25.14200 28.47300 -18.83700 1.000 75.26305  ? 464  ASP A N   1 
ATOM   3690 C  CA  . ASP A 1 464 ? -23.86700 28.67800 -19.50800 1.000 71.83939  ? 464  ASP A CA  1 
ATOM   3691 C  C   . ASP A 1 464 ? -22.87600 29.24000 -18.50000 1.000 74.41997  ? 464  ASP A C   1 
ATOM   3692 O  O   . ASP A 1 464 ? -23.27000 29.87800 -17.52000 1.000 67.35883  ? 464  ASP A O   1 
ATOM   3693 C  CB  . ASP A 1 464 ? -24.02000 29.62700 -20.70600 1.000 81.31991  ? 464  ASP A CB  1 
ATOM   3694 C  CG  . ASP A 1 464 ? -22.69200 30.00800 -21.32700 1.000 95.48413  ? 464  ASP A CG  1 
ATOM   3695 O  OD1 . ASP A 1 464 ? -21.99800 29.11100 -21.84900 1.000 101.91314 ? 464  ASP A OD1 1 
ATOM   3696 O  OD2 . ASP A 1 464 ? -22.34400 31.20600 -21.29300 1.000 97.57550  ? 464  ASP A OD2 1 
ATOM   3697 N  N   . TRP A 1 465 ? -21.59400 28.97400 -18.73200 1.000 75.13067  ? 465  TRP A N   1 
ATOM   3698 C  CA  . TRP A 1 465 ? -20.54700 29.57900 -17.92400 1.000 74.91645  ? 465  TRP A CA  1 
ATOM   3699 C  C   . TRP A 1 465 ? -19.28800 29.72000 -18.76200 1.000 68.21502  ? 465  TRP A C   1 
ATOM   3700 O  O   . TRP A 1 465 ? -19.10300 29.03300 -19.77000 1.000 64.10513  ? 465  TRP A O   1 
ATOM   3701 C  CB  . TRP A 1 465 ? -20.26400 28.77600 -16.64600 1.000 66.41508  ? 465  TRP A CB  1 
ATOM   3702 C  CG  . TRP A 1 465 ? -19.86200 27.34900 -16.86600 1.000 71.78664  ? 465  TRP A CG  1 
ATOM   3703 C  CD1 . TRP A 1 465 ? -20.69000 26.26800 -16.93200 1.000 72.88336  ? 465  TRP A CD1 1 
ATOM   3704 C  CD2 . TRP A 1 465 ? -18.52900 26.84300 -17.02200 1.000 74.07637  ? 465  TRP A CD2 1 
ATOM   3705 N  NE1 . TRP A 1 465 ? -19.95900 25.12200 -17.13000 1.000 71.56945  ? 465  TRP A NE1 1 
ATOM   3706 C  CE2 . TRP A 1 465 ? -18.63000 25.44800 -17.18900 1.000 68.94940  ? 465  TRP A CE2 1 
ATOM   3707 C  CE3 . TRP A 1 465 ? -17.26300 27.43400 -17.04400 1.000 71.76519  ? 465  TRP A CE3 1 
ATOM   3708 C  CZ2 . TRP A 1 465 ? -17.51300 24.63600 -17.37500 1.000 70.60517  ? 465  TRP A CZ2 1 
ATOM   3709 C  CZ3 . TRP A 1 465 ? -16.15500 26.62600 -17.22800 1.000 64.16348  ? 465  TRP A CZ3 1 
ATOM   3710 C  CH2 . TRP A 1 465 ? -16.28800 25.24200 -17.39100 1.000 69.94027  ? 465  TRP A CH2 1 
ATOM   3711 N  N   . LYS A 1 466 ? -18.42300 30.63400 -18.33000 1.000 70.75922  ? 466  LYS A N   1 
ATOM   3712 C  CA  . LYS A 1 466 ? -17.19400 30.91400 -19.05800 1.000 67.25851  ? 466  LYS A CA  1 
ATOM   3713 C  C   . LYS A 1 466 ? -16.16700 31.49700 -18.10100 1.000 60.59467  ? 466  LYS A C   1 
ATOM   3714 O  O   . LYS A 1 466 ? -16.49500 32.34600 -17.27000 1.000 67.77942  ? 466  LYS A O   1 
ATOM   3715 C  CB  . LYS A 1 466 ? -17.44700 31.87800 -20.22300 1.000 60.10587  ? 466  LYS A CB  1 
ATOM   3716 N  N   . GLN A 1 467 ? -14.92500 31.04000 -18.22600 1.000 64.24104  ? 467  GLN A N   1 
ATOM   3717 C  CA  . GLN A 1 467 ? -13.83600 31.54400 -17.39700 1.000 68.66245  ? 467  GLN A CA  1 
ATOM   3718 C  C   . GLN A 1 467 ? -13.21600 32.75200 -18.08600 1.000 69.95767  ? 467  GLN A C   1 
ATOM   3719 O  O   . GLN A 1 467 ? -12.58700 32.62100 -19.14100 1.000 75.48463  ? 467  GLN A O   1 
ATOM   3720 C  CB  . GLN A 1 467 ? -12.78700 30.46600 -17.14400 1.000 63.64130  ? 467  GLN A CB  1 
ATOM   3721 C  CG  . GLN A 1 467 ? -11.64000 30.94400 -16.26200 1.000 65.83888  ? 467  GLN A CG  1 
ATOM   3722 C  CD  . GLN A 1 467 ? -10.63700 29.85300 -15.95100 1.000 71.06501  ? 467  GLN A CD  1 
ATOM   3723 O  OE1 . GLN A 1 467 ? -10.26500 29.06800 -16.82200 1.000 75.00717  ? 467  GLN A OE1 1 
ATOM   3724 N  NE2 . GLN A 1 467 ? -10.19300 29.79800 -14.70000 1.000 64.72887  ? 467  GLN A NE2 1 
ATOM   3725 N  N   . THR A 1 468 ? -13.40100 33.92700 -17.49500 1.000 69.07082  ? 468  THR A N   1 
ATOM   3726 C  CA  . THR A 1 468 ? -12.70900 35.12800 -17.92200 1.000 73.51322  ? 468  THR A CA  1 
ATOM   3727 C  C   . THR A 1 468 ? -11.48300 35.33600 -17.03700 1.000 76.84602  ? 468  THR A C   1 
ATOM   3728 O  O   . THR A 1 468 ? -11.21200 34.56500 -16.11300 1.000 67.21576  ? 468  THR A O   1 
ATOM   3729 C  CB  . THR A 1 468 ? -13.64100 36.34000 -17.87300 1.000 71.39642  ? 468  THR A CB  1 
ATOM   3730 O  OG1 . THR A 1 468 ? -14.01300 36.60500 -16.51500 1.000 73.95396  ? 468  THR A OG1 1 
ATOM   3731 C  CG2 . THR A 1 468 ? -14.89400 36.07900 -18.69200 1.000 55.95654  ? 468  THR A CG2 1 
ATOM   3732 N  N   . LYS A 1 469 ? -10.68000 36.33700 -17.35700 1.000 77.91256  ? 469  LYS A N   1 
ATOM   3733 C  CA  . LYS A 1 469 ? -9.44800  36.52300 -16.56300 1.000 81.38661  ? 469  LYS A CA  1 
ATOM   3734 C  C   . LYS A 1 469 ? -9.85500  37.04000 -15.18200 1.000 81.81521  ? 469  LYS A C   1 
ATOM   3735 O  O   . LYS A 1 469 ? -9.32400  36.54200 -14.17800 1.000 79.18629  ? 469  LYS A O   1 
ATOM   3736 C  CB  . LYS A 1 469 ? -8.50000  37.49600 -17.26500 1.000 70.43130  ? 469  LYS A CB  1 
ATOM   3737 N  N   . ASP A 1 470 ? -10.80600 37.96400 -15.15200 1.000 87.15129  ? 470  ASP A N   1 
ATOM   3738 C  CA  . ASP A 1 470 ? -11.21000 38.60600 -13.87900 1.000 89.87011  ? 470  ASP A CA  1 
ATOM   3739 C  C   . ASP A 1 470 ? -12.02000 37.64200 -13.00800 1.000 89.47796  ? 470  ASP A C   1 
ATOM   3740 O  O   . ASP A 1 470 ? -11.99000 37.80400 -11.77900 1.000 87.80730  ? 470  ASP A O   1 
ATOM   3741 C  CB  . ASP A 1 470 ? -12.00600 39.87900 -14.17200 1.000 91.27075  ? 470  ASP A CB  1 
ATOM   3742 C  CG  . ASP A 1 470 ? -11.16600 41.14100 -14.17300 1.000 98.30971  ? 470  ASP A CG  1 
ATOM   3743 O  OD1 . ASP A 1 470 ? -9.95000  41.03400 -13.93900 1.000 98.77248  ? 470  ASP A OD1 1 
ATOM   3744 O  OD2 . ASP A 1 470 ? -11.73900 42.22000 -14.40600 1.000 97.87894  ? 470  ASP A OD2 1 
ATOM   3745 N  N   . ALA A 1 471 ? -12.74000 36.70200 -13.61300 1.000 77.76274  ? 471  ALA A N   1 
ATOM   3746 C  CA  . ALA A 1 471 ? -13.60800 35.83500 -12.79400 1.000 60.70987  ? 471  ALA A CA  1 
ATOM   3747 C  C   . ALA A 1 471 ? -14.28000 34.74300 -13.61200 1.000 66.80042  ? 471  ALA A C   1 
ATOM   3748 O  O   . ALA A 1 471 ? -14.18700 34.76100 -14.84300 1.000 74.91953  ? 471  ALA A O   1 
ATOM   3749 C  CB  . ALA A 1 471 ? -14.65900 36.68100 -12.13400 1.000 56.28672  ? 471  ALA A CB  1 
ATOM   3750 N  N   . LEU A 1 472 ? -14.90200 33.79200 -12.92600 1.000 61.57839  ? 472  LEU A N   1 
ATOM   3751 C  CA  . LEU A 1 472 ? -15.70000 32.77800 -13.60100 1.000 57.80577  ? 472  LEU A CA  1 
ATOM   3752 C  C   . LEU A 1 472 ? -17.13900 33.27300 -13.66300 1.000 62.56383  ? 472  LEU A C   1 
ATOM   3753 O  O   . LEU A 1 472 ? -17.77200 33.48400 -12.62100 1.000 63.58602  ? 472  LEU A O   1 
ATOM   3754 C  CB  . LEU A 1 472 ? -15.61500 31.44100 -12.86500 1.000 57.90132  ? 472  LEU A CB  1 
ATOM   3755 C  CG  . LEU A 1 472 ? -16.69300 30.39700 -13.17400 1.000 57.86431  ? 472  LEU A CG  1 
ATOM   3756 C  CD1 . LEU A 1 472 ? -16.65100 29.97900 -14.63500 1.000 64.98154  ? 472  LEU A CD1 1 
ATOM   3757 C  CD2 . LEU A 1 472 ? -16.55000 29.18600 -12.26200 1.000 45.88864  ? 472  LEU A CD2 1 
ATOM   3758 N  N   . GLU A 1 473 ? -17.64300 33.48600 -14.87700 1.000 62.97894  ? 473  GLU A N   1 
ATOM   3759 C  CA  . GLU A 1 473 ? -18.98000 34.01500 -15.08300 1.000 63.45915  ? 473  GLU A CA  1 
ATOM   3760 C  C   . GLU A 1 473 ? -19.96800 32.87500 -15.28400 1.000 62.99673  ? 473  GLU A C   1 
ATOM   3761 O  O   . GLU A 1 473 ? -19.69100 31.91800 -16.01500 1.000 63.02569  ? 473  GLU A O   1 
ATOM   3762 C  CB  . GLU A 1 473 ? -19.00000 34.95200 -16.29100 1.000 62.29919  ? 473  GLU A CB  1 
ATOM   3763 C  CG  . GLU A 1 473 ? -17.89300 35.99600 -16.28000 1.000 57.43163  ? 473  GLU A CG  1 
ATOM   3764 C  CD  . GLU A 1 473 ? -17.98600 36.94200 -15.09800 1.000 69.06312  ? 473  GLU A CD  1 
ATOM   3765 O  OE1 . GLU A 1 473 ? -19.10000 37.13300 -14.56700 1.000 71.33058  ? 473  GLU A OE1 1 
ATOM   3766 O  OE2 . GLU A 1 473 ? -16.94100 37.49700 -14.70000 1.000 66.85632  ? 473  GLU A OE2 1 
ATOM   3767 N  N   . ILE A 1 474 ? -21.13000 32.99600 -14.64300 1.000 59.58310  ? 474  ILE A N   1 
ATOM   3768 C  CA  . ILE A 1 474 ? -22.14200 31.94900 -14.59900 1.000 59.22669  ? 474  ILE A CA  1 
ATOM   3769 C  C   . ILE A 1 474 ? -23.49400 32.58600 -14.88700 1.000 55.01462  ? 474  ILE A C   1 
ATOM   3770 O  O   . ILE A 1 474 ? -23.88100 33.55100 -14.22100 1.000 54.61579  ? 474  ILE A O   1 
ATOM   3771 C  CB  . ILE A 1 474 ? -22.15700 31.24900 -13.22500 1.000 54.75554  ? 474  ILE A CB  1 
ATOM   3772 C  CG1 . ILE A 1 474 ? -20.90400 30.38900 -13.03700 1.000 59.81649  ? 474  ILE A CG1 1 
ATOM   3773 C  CG2 . ILE A 1 474 ? -23.42200 30.43400 -13.04300 1.000 54.17454  ? 474  ILE A CG2 1 
ATOM   3774 C  CD1 . ILE A 1 474 ? -20.77100 29.79700 -11.64600 1.000 49.16882  ? 474  ILE A CD1 1 
ATOM   3775 N  N   . SER A 1 475 ? -24.20700 32.05600 -15.87800 1.000 52.78372  ? 475  SER A N   1 
ATOM   3776 C  CA  A SER A 1 475 ? -25.54000 32.52900 -16.23200 0.687 56.81030  ? 475  SER A CA  1 
ATOM   3777 C  CA  B SER A 1 475 ? -25.54000 32.52900 -16.23300 0.313 56.73424  ? 475  SER A CA  1 
ATOM   3778 C  C   . SER A 1 475 ? -26.56300 31.59600 -15.59200 1.000 53.94683  ? 475  SER A C   1 
ATOM   3779 O  O   . SER A 1 475 ? -26.68900 30.43400 -15.99200 1.000 57.56898  ? 475  SER A O   1 
ATOM   3780 C  CB  A SER A 1 475 ? -25.71300 32.58500 -17.74800 0.687 54.89151  ? 475  SER A CB  1 
ATOM   3781 C  CB  B SER A 1 475 ? -25.71200 32.58300 -17.75000 0.313 54.93313  ? 475  SER A CB  1 
ATOM   3782 O  OG  A SER A 1 475 ? -25.48500 31.31600 -18.33400 0.687 62.59487  ? 475  SER A OG  1 
ATOM   3783 O  OG  B SER A 1 475 ? -26.98200 33.10200 -18.10300 0.313 59.07843  ? 475  SER A OG  1 
ATOM   3784 N  N   . LEU A 1 476 ? -27.39300 32.17900 -14.76100 1.000 49.31596  ? 476  LEU A N   1 
ATOM   3785 C  CA  . LEU A 1 476 ? -28.22800 31.33400 -13.89600 1.000 49.54307  ? 476  LEU A CA  1 
ATOM   3786 C  C   . LEU A 1 476 ? -29.43800 30.83500 -14.67500 1.000 53.37706  ? 476  LEU A C   1 
ATOM   3787 O  O   . LEU A 1 476 ? -29.87900 31.51000 -15.61200 1.000 54.81523  ? 476  LEU A O   1 
ATOM   3788 C  CB  . LEU A 1 476 ? -28.65200 32.13000 -12.67000 1.000 54.12858  ? 476  LEU A CB  1 
ATOM   3789 C  CG  . LEU A 1 476 ? -27.58100 32.36000 -11.60200 1.000 49.38459  ? 476  LEU A CG  1 
ATOM   3790 C  CD1 . LEU A 1 476 ? -28.24600 33.02900 -10.41900 1.000 41.22426  ? 476  LEU A CD1 1 
ATOM   3791 C  CD2 . LEU A 1 476 ? -26.98100 31.03100 -11.19200 1.000 56.19087  ? 476  LEU A CD2 1 
ATOM   3792 N  N   . PRO A 1 477 ? -29.99200 29.67500 -14.31000 1.000 63.63837  ? 477  PRO A N   1 
ATOM   3793 C  CA  . PRO A 1 477 ? -31.23600 29.17100 -14.90900 1.000 49.32611  ? 477  PRO A CA  1 
ATOM   3794 C  C   . PRO A 1 477 ? -32.40600 29.90800 -14.28900 1.000 53.29099  ? 477  PRO A C   1 
ATOM   3795 O  O   . PRO A 1 477 ? -32.19600 30.83800 -13.48800 1.000 52.16313  ? 477  PRO A O   1 
ATOM   3796 C  CB  . PRO A 1 477 ? -31.22300 27.69700 -14.56700 1.000 54.53239  ? 477  PRO A CB  1 
ATOM   3797 C  CG  . PRO A 1 477 ? -30.48100 27.63100 -13.25500 1.000 54.79573  ? 477  PRO A CG  1 
ATOM   3798 C  CD  . PRO A 1 477 ? -29.43500 28.68800 -13.33400 1.000 58.88058  ? 477  PRO A CD  1 
ATOM   3799 N  N   . ALA A 1 478 ? -33.62600 29.51200 -14.61100 1.000 50.70041  ? 478  ALA A N   1 
ATOM   3800 C  CA  . ALA A 1 478 ? -34.81000 30.23800 -14.10700 1.000 55.29299  ? 478  ALA A CA  1 
ATOM   3801 C  C   . ALA A 1 478 ? -34.89200 30.19100 -12.57600 1.000 58.36122  ? 478  ALA A C   1 
ATOM   3802 O  O   . ALA A 1 478 ? -34.63200 29.12500 -12.00200 1.000 54.11117  ? 478  ALA A O   1 
ATOM   3803 C  CB  . ALA A 1 478 ? -36.04600 29.66100 -14.73100 1.000 54.36435  ? 478  ALA A CB  1 
ATOM   3804 N  N   . LYS A 1 479 ? -35.31600 31.29500 -11.96100 1.000 52.22244  ? 479  LYS A N   1 
ATOM   3805 C  CA  . LYS A 1 479 ? -35.32700 31.36000 -10.48600 1.000 47.34185  ? 479  LYS A CA  1 
ATOM   3806 C  C   . LYS A 1 479 ? -36.18500 30.23100 -9.95300  1.000 52.91783  ? 479  LYS A C   1 
ATOM   3807 O  O   . LYS A 1 479 ? -37.32400 30.07500 -10.40100 1.000 62.45058  ? 479  LYS A O   1 
ATOM   3808 C  CB  . LYS A 1 479 ? -35.84600 32.68400 -9.92600  1.000 43.96897  ? 479  LYS A CB  1 
ATOM   3809 C  CG  . LYS A 1 479 ? -35.78300 32.76600 -8.40600  1.000 55.96582  ? 479  LYS A CG  1 
ATOM   3810 C  CD  . LYS A 1 479 ? -35.87000 34.15400 -7.81800  1.000 48.97671  ? 479  LYS A CD  1 
ATOM   3811 C  CE  . LYS A 1 479 ? -37.23200 34.79500 -7.92800  1.000 58.58184  ? 479  LYS A CE  1 
ATOM   3812 N  NZ  . LYS A 1 479 ? -37.23100 36.14600 -7.32200  1.000 63.34524  ? 479  LYS A NZ  1 
ATOM   3813 N  N   . PRO A 1 480 ? -35.67300 29.47900 -8.97100  1.000 49.38256  ? 480  PRO A N   1 
ATOM   3814 C  CA  . PRO A 1 480 ? -36.44100 28.42400 -8.37700  1.000 48.99499  ? 480  PRO A CA  1 
ATOM   3815 C  C   . PRO A 1 480 ? -37.40800 29.06000 -7.38300  1.000 49.85042  ? 480  PRO A C   1 
ATOM   3816 O  O   . PRO A 1 480 ? -37.64500 30.23100 -7.46600  1.000 49.84220  ? 480  PRO A O   1 
ATOM   3817 C  CB  . PRO A 1 480 ? -35.34500 27.61600 -7.68900  1.000 47.85274  ? 480  PRO A CB  1 
ATOM   3818 C  CG  . PRO A 1 480 ? -34.32200 28.63700 -7.28200  1.000 45.17707  ? 480  PRO A CG  1 
ATOM   3819 C  CD  . PRO A 1 480 ? -34.32200 29.61600 -8.43100  1.000 54.70074  ? 480  PRO A CD  1 
ATOM   3820 N  N   . ALA A 1 481 ? -37.96500 28.24600 -6.50500  1.000 52.15288  ? 481  ALA A N   1 
ATOM   3821 C  CA  . ALA A 1 481 ? -38.90400 28.74400 -5.48700  1.000 41.39571  ? 481  ALA A CA  1 
ATOM   3822 C  C   . ALA A 1 481 ? -38.19500 29.77600 -4.62700  1.000 44.33154  ? 481  ALA A C   1 
ATOM   3823 O  O   . ALA A 1 481 ? -36.97500 29.70200 -4.50100  1.000 56.59905  ? 481  ALA A O   1 
ATOM   3824 C  CB  . ALA A 1 481 ? -39.39400 27.59500 -4.66600  1.000 41.06961  ? 481  ALA A CB  1 
ATOM   3825 N  N   . GLU A 1 482 ? -38.94900 30.71900 -4.09000  1.000 43.39586  ? 482  GLU A N   1 
ATOM   3826 C  CA  . GLU A 1 482 ? -38.32800 31.81500 -3.31800  1.000 41.68137  ? 482  GLU A CA  1 
ATOM   3827 C  C   . GLU A 1 482 ? -37.58900 31.24500 -2.11100  1.000 50.57577  ? 482  GLU A C   1 
ATOM   3828 O  O   . GLU A 1 482 ? -38.10200 30.30800 -1.49500  1.000 43.96371  ? 482  GLU A O   1 
ATOM   3829 C  CB  . GLU A 1 482 ? -39.38300 32.81200 -2.86200  1.000 40.98383  ? 482  GLU A CB  1 
ATOM   3830 C  CG  . GLU A 1 482 ? -38.81300 34.16200 -2.48400  1.000 59.93421  ? 482  GLU A CG  1 
ATOM   3831 C  CD  . GLU A 1 482 ? -38.27400 34.95100 -3.66400  1.000 71.93953  ? 482  GLU A CD  1 
ATOM   3832 O  OE1 . GLU A 1 482 ? -38.63400 34.62000 -4.80600  1.000 65.51968  ? 482  GLU A OE1 1 
ATOM   3833 O  OE2 . GLU A 1 482 ? -37.48800 35.88700 -3.43600  1.000 81.34873  ? 482  GLU A OE2 1 
ATOM   3834 N  N   . SER A 1 483 ? -36.44100 31.83000 -1.78800  1.000 54.55201  ? 483  SER A N   1 
ATOM   3835 C  CA  . SER A 1 483 ? -35.66400 31.41800 -0.62900  1.000 46.75377  ? 483  SER A CA  1 
ATOM   3836 C  C   . SER A 1 483 ? -34.72300 32.54900 -0.24200  1.000 39.51309  ? 483  SER A C   1 
ATOM   3837 O  O   . SER A 1 483 ? -34.42200 33.43400 -1.04700  1.000 51.01467  ? 483  SER A O   1 
ATOM   3838 C  CB  . SER A 1 483 ? -34.88400 30.12700 -0.90800  1.000 43.93433  ? 483  SER A CB  1 
ATOM   3839 O  OG  . SER A 1 483 ? -34.11200 30.24000 -2.09000  1.000 50.85929  ? 483  SER A OG  1 
ATOM   3840 N  N   . LEU A 1 484 ? -34.26300 32.53700 1.01300   1.000 39.63584  ? 484  LEU A N   1 
ATOM   3841 C  CA  . LEU A 1 484 ? -33.39000 33.61700 1.55100   1.000 42.89115  ? 484  LEU A CA  1 
ATOM   3842 C  C   . LEU A 1 484 ? -32.01600 33.57800 0.87400   1.000 39.53619  ? 484  LEU A C   1 
ATOM   3843 O  O   . LEU A 1 484 ? -31.31100 34.58300 0.94400   1.000 38.35044  ? 484  LEU A O   1 
ATOM   3844 C  CB  . LEU A 1 484 ? -33.30300 33.47900 3.07000   1.000 34.68878  ? 484  LEU A CB  1 
ATOM   3845 C  CG  . LEU A 1 484 ? -34.61700 33.61200 3.84200   1.000 43.70828  ? 484  LEU A CG  1 
ATOM   3846 C  CD1 . LEU A 1 484 ? -34.41200 33.18700 5.28200   1.000 38.42940  ? 484  LEU A CD1 1 
ATOM   3847 C  CD2 . LEU A 1 484 ? -35.10200 35.04600 3.78000   1.000 35.43768  ? 484  LEU A CD2 1 
ATOM   3848 N  N   . ALA A 1 485 ? -31.67300 32.46300 0.23800   1.000 40.10284  ? 485  ALA A N   1 
ATOM   3849 C  CA  . ALA A 1 485 ? -30.41500 32.38200 -0.53100  1.000 36.11289  ? 485  ALA A CA  1 
ATOM   3850 C  C   . ALA A 1 485 ? -30.51200 31.27000 -1.57000  1.000 40.22453  ? 485  ALA A C   1 
ATOM   3851 O  O   . ALA A 1 485 ? -31.42100 30.43700 -1.46000  1.000 41.69728  ? 485  ALA A O   1 
ATOM   3852 C  CB  . ALA A 1 485 ? -29.23500 32.19600 0.38400   1.000 39.08607  ? 485  ALA A CB  1 
ATOM   3853 N  N   . TYR A 1 486 ? -29.59100 31.27900 -2.51700  1.000 38.97473  ? 486  TYR A N   1 
ATOM   3854 C  CA  . TYR A 1 486 ? -29.65500 30.33200 -3.65000  1.000 41.67436  ? 486  TYR A CA  1 
ATOM   3855 C  C   . TYR A 1 486 ? -28.29600 29.65600 -3.73700  1.000 41.96657  ? 486  TYR A C   1 
ATOM   3856 O  O   . TYR A 1 486 ? -27.28600 30.35000 -3.63900  1.000 42.68236  ? 486  TYR A O   1 
ATOM   3857 C  CB  . TYR A 1 486 ? -30.15100 31.07200 -4.90100  1.000 37.03552  ? 486  TYR A CB  1 
ATOM   3858 C  CG  . TYR A 1 486 ? -31.49900 31.72600 -4.72700  1.000 44.55770  ? 486  TYR A CG  1 
ATOM   3859 C  CD1 . TYR A 1 486 ? -31.61000 33.01600 -4.24100  1.000 46.79997  ? 486  TYR A CD1 1 
ATOM   3860 C  CD2 . TYR A 1 486 ? -32.67000 31.04800 -5.02100  1.000 46.02212  ? 486  TYR A CD2 1 
ATOM   3861 C  CE1 . TYR A 1 486 ? -32.84200 33.62000 -4.06300  1.000 46.46181  ? 486  TYR A CE1 1 
ATOM   3862 C  CE2 . TYR A 1 486 ? -33.91100 31.63600 -4.85000  1.000 42.52243  ? 486  TYR A CE2 1 
ATOM   3863 C  CZ  . TYR A 1 486 ? -33.99800 32.92800 -4.36900  1.000 47.49349  ? 486  TYR A CZ  1 
ATOM   3864 O  OH  . TYR A 1 486 ? -35.21300 33.51900 -4.19300  1.000 39.91320  ? 486  TYR A OH  1 
ATOM   3865 N  N   . VAL A 1 487 ? -28.29000 28.34300 -3.93600  1.000 39.83993  ? 487  VAL A N   1 
ATOM   3866 C  CA  . VAL A 1 487 ? -27.01200 27.59600 -3.84400  1.000 39.81016  ? 487  VAL A CA  1 
ATOM   3867 C  C   . VAL A 1 487 ? -26.57700 27.03100 -5.19300  1.000 41.80502  ? 487  VAL A C   1 
ATOM   3868 O  O   . VAL A 1 487 ? -27.38800 26.37600 -5.85300  1.000 40.46965  ? 487  VAL A O   1 
ATOM   3869 C  CB  . VAL A 1 487 ? -27.11800 26.49400 -2.76400  1.000 39.82925  ? 487  VAL A CB  1 
ATOM   3870 C  CG1 . VAL A 1 487 ? -25.83500 25.69400 -2.62500  1.000 49.35063  ? 487  VAL A CG1 1 
ATOM   3871 C  CG2 . VAL A 1 487 ? -27.55400 27.05000 -1.42100  1.000 39.39749  ? 487  VAL A CG2 1 
ATOM   3872 N  N   . LEU A 1 488 ? -25.32700 27.27800 -5.54900  1.000 39.86868  ? 488  LEU A N   1 
ATOM   3873 C  CA  . LEU A 1 488 ? -24.75000 26.68400 -6.76700  1.000 43.76039  ? 488  LEU A CA  1 
ATOM   3874 C  C   . LEU A 1 488 ? -23.82100 25.55400 -6.33300  1.000 48.40523  ? 488  LEU A C   1 
ATOM   3875 O  O   . LEU A 1 488 ? -23.03800 25.76900 -5.40300  1.000 45.68160  ? 488  LEU A O   1 
ATOM   3876 C  CB  . LEU A 1 488 ? -23.97100 27.74700 -7.54300  1.000 37.54867  ? 488  LEU A CB  1 
ATOM   3877 C  CG  . LEU A 1 488 ? -24.79200 28.69200 -8.41400  1.000 42.83964  ? 488  LEU A CG  1 
ATOM   3878 C  CD1 . LEU A 1 488 ? -23.95100 29.87900 -8.85000  1.000 38.38148  ? 488  LEU A CD1 1 
ATOM   3879 C  CD2 . LEU A 1 488 ? -25.34600 27.96000 -9.62400  1.000 41.33052  ? 488  LEU A CD2 1 
ATOM   3880 N  N   . LYS A 1 489 ? -23.91600 24.40300 -6.98300  1.000 50.43376  ? 489  LYS A N   1 
ATOM   3881 C  CA  . LYS A 1 489 ? -23.06300 23.25600 -6.69900  1.000 44.44013  ? 489  LYS A CA  1 
ATOM   3882 C  C   . LYS A 1 489 ? -22.14900 23.02700 -7.89400  1.000 51.02242  ? 489  LYS A C   1 
ATOM   3883 O  O   . LYS A 1 489 ? -22.62200 22.71000 -8.99000  1.000 45.75349  ? 489  LYS A O   1 
ATOM   3884 C  CB  . LYS A 1 489 ? -23.90200 22.01300 -6.40900  1.000 50.18048  ? 489  LYS A CB  1 
ATOM   3885 C  CG  . LYS A 1 489 ? -23.09500 20.73800 -6.27000  1.000 50.49634  ? 489  LYS A CG  1 
ATOM   3886 C  CD  . LYS A 1 489 ? -23.99700 19.54300 -6.01200  1.000 47.48813  ? 489  LYS A CD  1 
ATOM   3887 C  CE  . LYS A 1 489 ? -23.19700 18.25800 -5.91400  1.000 51.65209  ? 489  LYS A CE  1 
ATOM   3888 N  NZ  . LYS A 1 489 ? -24.07300 17.08800 -5.64400  1.000 49.29748  ? 489  LYS A NZ  1 
ATOM   3889 N  N   . LEU A 1 490 ? -20.84900 23.20700 -7.68500  1.000 51.02192  ? 490  LEU A N   1 
ATOM   3890 C  CA  . LEU A 1 490 ? -19.84100 23.01900 -8.71900  1.000 51.46021  ? 490  LEU A CA  1 
ATOM   3891 C  C   . LEU A 1 490 ? -19.14500 21.69200 -8.44300  1.000 50.70529  ? 490  LEU A C   1 
ATOM   3892 O  O   . LEU A 1 490 ? -18.37000 21.57800 -7.48800  1.000 52.68531  ? 490  LEU A O   1 
ATOM   3893 C  CB  . LEU A 1 490 ? -18.83800 24.17300 -8.72900  1.000 43.85724  ? 490  LEU A CB  1 
ATOM   3894 C  CG  . LEU A 1 490 ? -19.27700 25.59900 -9.08700  1.000 47.23891  ? 490  LEU A CG  1 
ATOM   3895 C  CD1 . LEU A 1 490 ? -20.10700 26.24500 -7.98600  1.000 39.76599  ? 490  LEU A CD1 1 
ATOM   3896 C  CD2 . LEU A 1 490 ? -18.06000 26.45700 -9.40000  1.000 48.92604  ? 490  LEU A CD2 1 
ATOM   3897 N  N   . THR A 1 491 ? -19.43900 20.69000 -9.26400  1.000 54.77952  ? 491  THR A N   1 
ATOM   3898 C  CA  . THR A 1 491 ? -18.82000 19.37900 -9.14100  1.000 51.96118  ? 491  THR A CA  1 
ATOM   3899 C  C   . THR A 1 491 ? -17.58800 19.33100 -10.03500 1.000 51.97028  ? 491  THR A C   1 
ATOM   3900 O  O   . THR A 1 491 ? -17.70000 19.45700 -11.26300 1.000 61.73735  ? 491  THR A O   1 
ATOM   3901 C  CB  . THR A 1 491 ? -19.80300 18.27000 -9.51600  1.000 51.96706  ? 491  THR A CB  1 
ATOM   3902 O  OG1 . THR A 1 491 ? -20.98100 18.38400 -8.70900  1.000 61.83499  ? 491  THR A OG1 1 
ATOM   3903 C  CG2 . THR A 1 491 ? -19.17200 16.90300 -9.29100  1.000 52.62562  ? 491  THR A CG2 1 
ATOM   3904 N  N   . PHE A 1 492 ? -16.42300 19.15800 -9.41400  1.000 58.23944  ? 492  PHE A N   1 
ATOM   3905 C  CA  . PHE A 1 492 ? -15.14000 19.06000 -10.09200 1.000 61.94624  ? 492  PHE A CA  1 
ATOM   3906 C  C   . PHE A 1 492 ? -14.70200 17.60300 -10.19600 1.000 71.39323  ? 492  PHE A C   1 
ATOM   3907 O  O   . PHE A 1 492 ? -15.28000 16.70300 -9.58100  1.000 71.83440  ? 492  PHE A O   1 
ATOM   3908 C  CB  . PHE A 1 492 ? -14.07000 19.86900 -9.35100  1.000 53.30218  ? 492  PHE A CB  1 
ATOM   3909 C  CG  . PHE A 1 492 ? -14.19800 21.35600 -9.51800  1.000 58.15277  ? 492  PHE A CG  1 
ATOM   3910 C  CD1 . PHE A 1 492 ? -13.55600 22.00500 -10.56000 1.000 68.24171  ? 492  PHE A CD1 1 
ATOM   3911 C  CD2 . PHE A 1 492 ? -14.94300 22.10700 -8.62400  1.000 56.29594  ? 492  PHE A CD2 1 
ATOM   3912 C  CE1 . PHE A 1 492 ? -13.66500 23.37400 -10.71700 1.000 62.25836  ? 492  PHE A CE1 1 
ATOM   3913 C  CE2 . PHE A 1 492 ? -15.05500 23.47900 -8.77500  1.000 66.56476  ? 492  PHE A CE2 1 
ATOM   3914 C  CZ  . PHE A 1 492 ? -14.41500 24.11200 -9.82300  1.000 63.20447  ? 492  PHE A CZ  1 
ATOM   3915 N  N   . ASP A 1 493 ? -13.69000 17.35800 -11.01400 1.000 80.52233  ? 493  ASP A N   1 
ATOM   3916 C  CA  . ASP A 1 493 ? -13.14400 15.98800 -11.12300 1.000 81.85381  ? 493  ASP A CA  1 
ATOM   3917 C  C   . ASP A 1 493 ? -11.67500 16.07800 -10.75700 1.000 87.99880  ? 493  ASP A C   1 
ATOM   3918 O  O   . ASP A 1 493 ? -10.93000 16.76300 -11.46900 1.000 84.00327  ? 493  ASP A O   1 
ATOM   3919 C  CB  . ASP A 1 493 ? -13.28500 15.41300 -12.52800 1.000 84.57165  ? 493  ASP A CB  1 
ATOM   3920 C  CG  . ASP A 1 493 ? -13.03000 13.92000 -12.61100 1.000 92.83574  ? 493  ASP A CG  1 
ATOM   3921 O  OD1 . ASP A 1 493 ? -12.62200 13.34000 -11.59100 1.000 104.34615 ? 493  ASP A OD1 1 
ATOM   3922 O  OD2 . ASP A 1 493 ? -13.25400 13.35300 -13.69400 1.000 77.78403  ? 493  ASP A OD2 1 
ATOM   3923 N  N   . GLY A 1 494 ? -11.27900 15.40500 -9.68500  1.000 122.05708 ? 494  GLY A N   1 
ATOM   3924 C  CA  . GLY A 1 494 ? -9.88300  15.54600 -9.25100  1.000 122.33392 ? 494  GLY A CA  1 
ATOM   3925 C  C   . GLY A 1 494 ? -9.70500  16.67300 -8.26300  1.000 117.49286 ? 494  GLY A C   1 
ATOM   3926 O  O   . GLY A 1 494 ? -8.58800  17.21000 -8.17700  1.000 120.75390 ? 494  GLY A O   1 
ATOM   3927 N  N   . GLY A 1 495 ? -10.77400 17.07200 -7.58900  1.000 77.51874  ? 495  GLY A N   1 
ATOM   3928 C  CA  . GLY A 1 495 ? -10.58200 18.07000 -6.53000  1.000 79.05202  ? 495  GLY A CA  1 
ATOM   3929 C  C   . GLY A 1 495 ? -10.74800 19.49500 -6.99600  1.000 70.65059  ? 495  GLY A C   1 
ATOM   3930 O  O   . GLY A 1 495 ? -10.66700 19.74500 -8.20200  1.000 66.89852  ? 495  GLY A O   1 
ATOM   3931 N  N   . ILE A 1 496 ? -10.94500 20.39100 -6.04100  1.000 64.17550  ? 496  ILE A N   1 
ATOM   3932 C  CA  . ILE A 1 496 ? -11.20500 21.81200 -6.39200  1.000 57.06840  ? 496  ILE A CA  1 
ATOM   3933 C  C   . ILE A 1 496 ? -9.85100  22.48200 -6.65300  1.000 57.94483  ? 496  ILE A C   1 
ATOM   3934 O  O   . ILE A 1 496 ? -8.94300  22.30200 -5.83400  1.000 67.00222  ? 496  ILE A O   1 
ATOM   3935 C  CB  . ILE A 1 496 ? -11.97300 22.50100 -5.25500  1.000 57.42554  ? 496  ILE A CB  1 
ATOM   3936 C  CG1 . ILE A 1 496 ? -13.28500 21.79000 -4.94900  1.000 60.66230  ? 496  ILE A CG1 1 
ATOM   3937 C  CG2 . ILE A 1 496 ? -12.19500 23.98200 -5.55900  1.000 58.34721  ? 496  ILE A CG2 1 
ATOM   3938 C  CD1 . ILE A 1 496 ? -14.03100 22.36700 -3.76300  1.000 51.10880  ? 496  ILE A CD1 1 
ATOM   3939 N  N   . PRO A 1 497 ? -9.67900  23.23100 -7.75900  1.000 55.84066  ? 497  PRO A N   1 
ATOM   3940 C  CA  . PRO A 1 497 ? -8.41300  23.92100 -8.03100  1.000 61.31009  ? 497  PRO A CA  1 
ATOM   3941 C  C   . PRO A 1 497 ? -8.04600  24.86100 -6.89600  1.000 62.25808  ? 497  PRO A C   1 
ATOM   3942 O  O   . PRO A 1 497 ? -8.90900  25.37800 -6.18000  1.000 66.59328  ? 497  PRO A O   1 
ATOM   3943 C  CB  . PRO A 1 497 ? -8.69900  24.69500 -9.32400  1.000 58.30290  ? 497  PRO A CB  1 
ATOM   3944 C  CG  . PRO A 1 497 ? -9.82800  23.96500 -9.96000  1.000 59.99764  ? 497  PRO A CG  1 
ATOM   3945 C  CD  . PRO A 1 497 ? -10.66400 23.44200 -8.83500  1.000 59.27488  ? 497  PRO A CD  1 
ATOM   3946 N  N   . VAL A 1 498 ? -6.74400  25.07800 -6.73400  1.000 62.45652  ? 498  VAL A N   1 
ATOM   3947 C  CA  . VAL A 1 498 ? -6.20700  25.90900 -5.66600  1.000 61.42199  ? 498  VAL A CA  1 
ATOM   3948 C  C   . VAL A 1 498 ? -6.04900  27.32900 -6.21300  1.000 68.81785  ? 498  VAL A C   1 
ATOM   3949 O  O   . VAL A 1 498 ? -5.13300  27.56000 -7.02300  1.000 81.31937  ? 498  VAL A O   1 
ATOM   3950 C  CB  . VAL A 1 498 ? -4.87600  25.36400 -5.14100  1.000 59.02585  ? 498  VAL A CB  1 
ATOM   3951 C  CG1 . VAL A 1 498 ? -4.46000  26.09600 -3.87300  1.000 66.99812  ? 498  VAL A CG1 1 
ATOM   3952 C  CG2 . VAL A 1 498 ? -4.98100  23.86700 -4.89400  1.000 77.54550  ? 498  VAL A CG2 1 
ATOM   3953 N  N   . PRO A 1 499 ? -6.88000  28.28000 -5.81000  1.000 64.01822  ? 499  PRO A N   1 
ATOM   3954 C  CA  . PRO A 1 499 ? -6.77200  29.63700 -6.35000  1.000 67.99149  ? 499  PRO A CA  1 
ATOM   3955 C  C   . PRO A 1 499 ? -5.61900  30.41700 -5.73900  1.000 68.04669  ? 499  PRO A C   1 
ATOM   3956 O  O   . PRO A 1 499 ? -5.21200  30.19300 -4.59700  1.000 59.05150  ? 499  PRO A O   1 
ATOM   3957 C  CB  . PRO A 1 499 ? -8.11800  30.26800 -5.97900  1.000 63.10994  ? 499  PRO A CB  1 
ATOM   3958 C  CG  . PRO A 1 499 ? -8.52300  29.55000 -4.73800  1.000 70.75720  ? 499  PRO A CG  1 
ATOM   3959 C  CD  . PRO A 1 499 ? -8.02000  28.14000 -4.88700  1.000 60.83141  ? 499  PRO A CD  1 
ATOM   3960 N  N   . GLN A 1 500 ? -5.09300  31.35000 -6.53300  1.000 75.45198  ? 500  GLN A N   1 
ATOM   3961 C  CA  . GLN A 1 500 ? -4.02300  32.23000 -6.09100  1.000 76.67272  ? 500  GLN A CA  1 
ATOM   3962 C  C   . GLN A 1 500 ? -4.62100  33.57000 -5.69300  1.000 76.65206  ? 500  GLN A C   1 
ATOM   3963 O  O   . GLN A 1 500 ? -5.16800  34.27200 -6.55800  1.000 74.70642  ? 500  GLN A O   1 
ATOM   3964 C  CB  . GLN A 1 500 ? -2.98800  32.41500 -7.19800  1.000 72.64482  ? 500  GLN A CB  1 
ATOM   3965 C  CG  . GLN A 1 500 ? -1.81000  33.29300 -6.81000  1.000 78.90869  ? 500  GLN A CG  1 
ATOM   3966 C  CD  . GLN A 1 500 ? -0.85700  32.60500 -5.85300  1.000 74.48659  ? 500  GLN A CD  1 
ATOM   3967 O  OE1 . GLN A 1 500 ? -0.77000  31.37700 -5.82000  1.000 67.50312  ? 500  GLN A OE1 1 
ATOM   3968 N  NE2 . GLN A 1 500 ? -0.13600  33.39400 -5.06600  1.000 78.87426  ? 500  GLN A NE2 1 
ATOM   3969 N  N   . PRO A 1 501 ? -4.55500  33.96500 -4.42400  1.000 70.03894  ? 501  PRO A N   1 
ATOM   3970 C  CA  . PRO A 1 501 ? -5.14300  35.24700 -4.02100  1.000 82.03517  ? 501  PRO A CA  1 
ATOM   3971 C  C   . PRO A 1 501 ? -4.41900  36.42100 -4.66000  1.000 84.36580  ? 501  PRO A C   1 
ATOM   3972 O  O   . PRO A 1 501 ? -3.23000  36.35100 -4.97900  1.000 92.50904  ? 501  PRO A O   1 
ATOM   3973 C  CB  . PRO A 1 501 ? -4.97300  35.25700 -2.49600  1.000 77.50461  ? 501  PRO A CB  1 
ATOM   3974 C  CG  . PRO A 1 501 ? -4.73100  33.82600 -2.11800  1.000 64.51052  ? 501  PRO A CG  1 
ATOM   3975 C  CD  . PRO A 1 501 ? -4.00600  33.22200 -3.27900  1.000 65.00634  ? 501  PRO A CD  1 
ATOM   3976 N  N   . LYS A 1 502 ? -5.12400  37.53700 -4.81500  1.000 82.32913  ? 502  LYS A N   1 
ATOM   3977 C  CA  . LYS A 1 502 ? -4.47200  38.75600 -5.36500  1.000 83.95959  ? 502  LYS A CA  1 
ATOM   3978 C  C   . LYS A 1 502 ? -3.39900  39.20800 -4.37900  1.000 84.06849  ? 502  LYS A C   1 
ATOM   3979 O  O   . LYS A 1 502 ? -2.28800  39.51400 -4.81800  1.000 83.16196  ? 502  LYS A O   1 
ATOM   3980 C  CB  . LYS A 1 502 ? -5.51600  39.84800 -5.60200  1.000 70.56806  ? 502  LYS A CB  1 
ATOM   3981 N  N   . ILE A 1 503 ? -3.72900  39.21500 -3.08900  1.000 88.99416  ? 503  ILE A N   1 
ATOM   3982 C  CA  . ILE A 1 503 ? -2.75000  39.61000 -2.03400  1.000 88.39784  ? 503  ILE A CA  1 
ATOM   3983 C  C   . ILE A 1 503 ? -2.63100  38.46400 -1.03000  1.000 86.99657  ? 503  ILE A C   1 
ATOM   3984 O  O   . ILE A 1 503 ? -3.39500  38.44900 -0.05600  1.000 87.18149  ? 503  ILE A O   1 
ATOM   3985 C  CB  . ILE A 1 503 ? -3.18000  40.92200 -1.35700  1.000 91.28133  ? 503  ILE A CB  1 
ATOM   3986 N  N   . GLY A 1 504 ? -1.70200  37.54700 -1.27400  1.000 86.71570  ? 504  GLY A N   1 
ATOM   3987 C  CA  . GLY A 1 504 ? -1.53200  36.37500 -0.40200  1.000 86.12925  ? 504  GLY A CA  1 
ATOM   3988 C  C   . GLY A 1 504 ? -0.62800  35.37000 -1.06700  1.000 85.72703  ? 504  GLY A C   1 
ATOM   3989 O  O   . GLY A 1 504 ? 0.26200   35.79300 -1.81600  1.000 89.06024  ? 504  GLY A O   1 
ATOM   3990 N  N   . ALA A 1 505 ? -0.84000  34.08600 -0.78900  1.000 86.70610  ? 505  ALA A N   1 
ATOM   3991 C  CA  . ALA A 1 505 ? -0.05100  33.05700 -1.49200  1.000 78.85358  ? 505  ALA A CA  1 
ATOM   3992 C  C   . ALA A 1 505 ? -0.73000  31.69400 -1.43600  1.000 74.22946  ? 505  ALA A C   1 
ATOM   3993 O  O   . ALA A 1 505 ? -1.78100  31.56600 -0.79300  1.000 68.74101  ? 505  ALA A O   1 
ATOM   3994 C  CB  . ALA A 1 505 ? 1.32500   32.98600 -0.90500  1.000 81.02518  ? 505  ALA A CB  1 
ATOM   3995 N  N   . SER A 1 506 ? -0.12000  30.71700 -2.09500  1.000 76.33452  ? 506  SER A N   1 
ATOM   3996 C  CA  . SER A 1 506 ? -0.67700  29.37100 -2.14900  1.000 78.77185  ? 506  SER A CA  1 
ATOM   3997 C  C   . SER A 1 506 ? 0.44600   28.36100 -1.97100  1.000 86.22586  ? 506  SER A C   1 
ATOM   3998 O  O   . SER A 1 506 ? 1.48500   28.46000 -2.63000  1.000 89.87251  ? 506  SER A O   1 
ATOM   3999 C  CB  . SER A 1 506 ? -1.41200  29.12600 -3.47200  1.000 77.45591  ? 506  SER A CB  1 
ATOM   4000 O  OG  . SER A 1 506 ? -0.54000  29.27700 -4.57900  1.000 85.24751  ? 506  SER A OG  1 
ATOM   4001 N  N   . VAL A 1 507 ? 0.20200   27.37500 -1.10800  1.000 84.85866  ? 507  VAL A N   1 
ATOM   4002 C  CA  . VAL A 1 507 ? 1.22700   26.34400 -0.80300  1.000 80.95836  ? 507  VAL A CA  1 
ATOM   4003 C  C   . VAL A 1 507 ? 0.72200   24.99800 -1.30800  1.000 77.41544  ? 507  VAL A C   1 
ATOM   4004 O  O   . VAL A 1 507 ? -0.49300  24.79300 -1.31200  1.000 84.18999  ? 507  VAL A O   1 
ATOM   4005 C  CB  . VAL A 1 507 ? 1.49400   26.29800 0.70700   1.000 83.40073  ? 507  VAL A CB  1 
ATOM   4006 C  CG1 . VAL A 1 507 ? 2.09600   27.60000 1.20800   1.000 76.88202  ? 507  VAL A CG1 1 
ATOM   4007 C  CG2 . VAL A 1 507 ? 0.24100   25.94900 1.49200   1.000 75.33279  ? 507  VAL A CG2 1 
ATOM   4008 N  N   . PHE A 1 508 ? 1.63700   24.11500 -1.71300  1.000 82.76423  ? 508  PHE A N   1 
ATOM   4009 C  CA  . PHE A 1 508 ? 1.24100   22.80400 -2.28700  1.000 89.62521  ? 508  PHE A CA  1 
ATOM   4010 C  C   . PHE A 1 508 ? 2.20700   21.71300 -1.81500  1.000 99.11922  ? 508  PHE A C   1 
ATOM   4011 O  O   . PHE A 1 508 ? 3.41900   21.98300 -1.73100  1.000 95.77722  ? 508  PHE A O   1 
ATOM   4012 C  CB  . PHE A 1 508 ? 1.26900   22.86900 -3.81500  1.000 89.62163  ? 508  PHE A CB  1 
ATOM   4013 C  CG  . PHE A 1 508 ? 0.52500   24.02900 -4.42400  1.000 94.16425  ? 508  PHE A CG  1 
ATOM   4014 C  CD1 . PHE A 1 508 ? 1.13700   25.26400 -4.57000  1.000 96.03621  ? 508  PHE A CD1 1 
ATOM   4015 C  CD2 . PHE A 1 508 ? -0.77800  23.88400 -4.86900  1.000 88.74598  ? 508  PHE A CD2 1 
ATOM   4016 C  CE1 . PHE A 1 508 ? 0.45800   26.33100 -5.13500  1.000 89.94748  ? 508  PHE A CE1 1 
ATOM   4017 C  CE2 . PHE A 1 508 ? -1.45500  24.95100 -5.43700  1.000 85.54782  ? 508  PHE A CE2 1 
ATOM   4018 C  CZ  . PHE A 1 508 ? -0.83700  26.17200 -5.56800  1.000 86.86960  ? 508  PHE A CZ  1 
ATOM   4019 N  N   . SER A 1 509 ? 1.68600   20.51600 -1.53000  1.000 95.98105  ? 509  SER A N   1 
ATOM   4020 C  CA  . SER A 1 509 ? 2.54800   19.37700 -1.12200  1.000 90.64672  ? 509  SER A CA  1 
ATOM   4021 C  C   . SER A 1 509 ? 3.08300   18.68900 -2.37600  1.000 105.11507 ? 509  SER A C   1 
ATOM   4022 O  O   . SER A 1 509 ? 2.77800   17.49900 -2.56900  1.000 111.55291 ? 509  SER A O   1 
ATOM   4023 C  CB  . SER A 1 509 ? 1.78100   18.41000 -0.26700  1.000 87.16864  ? 509  SER A CB  1 
ATOM   4024 O  OG  . SER A 1 509 ? 2.58500   17.29500 0.08400   1.000 114.08141 ? 509  SER A OG  1 
ATOM   4025 N  N   . ALA A 1 510 ? 3.85800   19.41000 -3.18600  1.000 102.80084 ? 510  ALA A N   1 
ATOM   4026 C  CA  . ALA A 1 510 ? 4.35300   18.84200 -4.46000  1.000 106.90207 ? 510  ALA A CA  1 
ATOM   4027 C  C   . ALA A 1 510 ? 5.48300   19.72200 -4.99100  1.000 112.34646 ? 510  ALA A C   1 
ATOM   4028 O  O   . ALA A 1 510 ? 5.67900   20.82100 -4.44000  1.000 108.05554 ? 510  ALA A O   1 
ATOM   4029 C  CB  . ALA A 1 510 ? 3.22400   18.73700 -5.45100  1.000 97.68651  ? 510  ALA A CB  1 
ATOM   4030 N  N   . THR A 1 511 ? 6.19900   19.25500 -6.01700  1.000 114.98219 ? 511  THR A N   1 
ATOM   4031 C  CA  . THR A 1 511 ? 7.37200   20.03900 -6.48700  1.000 109.61760 ? 511  THR A CA  1 
ATOM   4032 C  C   . THR A 1 511 ? 6.88700   21.22200 -7.32000  1.000 113.48293 ? 511  THR A C   1 
ATOM   4033 O  O   . THR A 1 511 ? 7.71300   22.08900 -7.64800  1.000 112.35503 ? 511  THR A O   1 
ATOM   4034 C  CB  . THR A 1 511 ? 8.36700   19.15100 -7.24000  1.000 110.26741 ? 511  THR A CB  1 
ATOM   4035 N  N   . SER A 1 512 ? 5.60600   21.22300 -7.67200  1.000 111.52247 ? 512  SER A N   1 
ATOM   4036 C  CA  . SER A 1 512 ? 5.06600   22.31400 -8.51800  1.000 101.29659 ? 512  SER A CA  1 
ATOM   4037 C  C   . SER A 1 512 ? 3.71800   22.77600 -7.97000  1.000 95.07978  ? 512  SER A C   1 
ATOM   4038 O  O   . SER A 1 512 ? 3.27300   22.22300 -6.95600  1.000 95.20028  ? 512  SER A O   1 
ATOM   4039 C  CB  . SER A 1 512 ? 4.93800   21.85700 -9.93600  1.000 95.40127  ? 512  SER A CB  1 
ATOM   4040 O  OG  . SER A 1 512 ? 4.09900   20.71800 -10.02100 1.000 106.79045 ? 512  SER A OG  1 
ATOM   4041 N  N   . ALA A 1 513 ? 3.09900   23.74100 -8.64300  1.000 94.03463  ? 513  ALA A N   1 
ATOM   4042 C  CA  . ALA A 1 513 ? 1.75800   24.19800 -8.23800  1.000 94.32747  ? 513  ALA A CA  1 
ATOM   4043 C  C   . ALA A 1 513 ? 0.76000   23.20300 -8.79900  1.000 98.45428  ? 513  ALA A C   1 
ATOM   4044 O  O   . ALA A 1 513 ? -0.04200  23.59400 -9.65400  1.000 99.81747  ? 513  ALA A O   1 
ATOM   4045 C  CB  . ALA A 1 513 ? 1.50200   25.56100 -8.80100  1.000 92.22870  ? 513  ALA A CB  1 
ATOM   4046 N  N   . THR A 1 514 ? 0.84300   21.96000 -8.33700  1.000 99.65411  ? 514  THR A N   1 
ATOM   4047 C  CA  . THR A 1 514 ? -0.09200  20.91700 -8.80300  1.000 88.97358  ? 514  THR A CA  1 
ATOM   4048 C  C   . THR A 1 514 ? -0.49900  20.07800 -7.59800  1.000 95.61522  ? 514  THR A C   1 
ATOM   4049 O  O   . THR A 1 514 ? 0.26300   20.03500 -6.62600  1.000 103.42435 ? 514  THR A O   1 
ATOM   4050 C  CB  . THR A 1 514 ? 0.54300   20.08300 -9.91700  1.000 88.41936  ? 514  THR A CB  1 
ATOM   4051 O  OG1 . THR A 1 514 ? 0.94000   20.97200 -10.96000 1.000 96.01770  ? 514  THR A OG1 1 
ATOM   4052 C  CG2 . THR A 1 514 ? -0.39300  19.03200 -10.46900 1.000 84.68480  ? 514  THR A CG2 1 
ATOM   4053 N  N   . GLY A 1 515 ? -1.67900  19.47500 -7.65500  1.000 100.75121 ? 515  GLY A N   1 
ATOM   4054 C  CA  . GLY A 1 515 ? -2.12000  18.58900 -6.56400  1.000 108.47997 ? 515  GLY A CA  1 
ATOM   4055 C  C   . GLY A 1 515 ? -2.68500  19.34800 -5.38400  1.000 102.65707 ? 515  GLY A C   1 
ATOM   4056 O  O   . GLY A 1 515 ? -2.92100  20.55900 -5.51600  1.000 103.60466 ? 515  GLY A O   1 
ATOM   4057 N  N   . ARG A 1 516 ? -2.84000  18.66300 -4.25400  1.000 99.13352  ? 516  ARG A N   1 
ATOM   4058 C  CA  . ARG A 1 516 ? -3.42800  19.29800 -3.05400  1.000 103.90570 ? 516  ARG A CA  1 
ATOM   4059 C  C   . ARG A 1 516 ? -2.65700  20.57400 -2.72400  1.000 98.73259  ? 516  ARG A C   1 
ATOM   4060 O  O   . ARG A 1 516 ? -1.42300  20.57200 -2.84600  1.000 98.35116  ? 516  ARG A O   1 
ATOM   4061 C  CB  . ARG A 1 516 ? -3.37500  18.33700 -1.86700  1.000 97.00607  ? 516  ARG A CB  1 
ATOM   4062 C  CG  . ARG A 1 516 ? -3.94900  18.90900 -0.58000  1.000 105.25603 ? 516  ARG A CG  1 
ATOM   4063 C  CD  . ARG A 1 516 ? -5.41500  19.25700 -0.72900  1.000 106.86614 ? 516  ARG A CD  1 
ATOM   4064 N  NE  . ARG A 1 516 ? -5.96400  19.84200 0.48400   1.000 100.26473 ? 516  ARG A NE  1 
ATOM   4065 C  CZ  . ARG A 1 516 ? -7.23100  20.20200 0.62700   1.000 88.27082  ? 516  ARG A CZ  1 
ATOM   4066 N  NH1 . ARG A 1 516 ? -8.08000  20.02900 -0.36900  1.000 84.48273  ? 516  ARG A NH1 1 
ATOM   4067 N  NH2 . ARG A 1 516 ? -7.64500  20.72600 1.76500   1.000 82.98793  ? 516  ARG A NH2 1 
ATOM   4068 N  N   . GLY A 1 517 ? -3.38100  21.62600 -2.35700  1.000 81.41202  ? 517  GLY A N   1 
ATOM   4069 C  CA  . GLY A 1 517 ? -2.74800  22.90200 -2.00600  1.000 79.67980  ? 517  GLY A CA  1 
ATOM   4070 C  C   . GLY A 1 517 ? -3.63500  23.68100 -1.06800  1.000 80.54504  ? 517  GLY A C   1 
ATOM   4071 O  O   . GLY A 1 517 ? -4.80900  23.30400 -0.91800  1.000 80.86842  ? 517  GLY A O   1 
ATOM   4072 N  N   . VAL A 1 518 ? -3.08500  24.69900 -0.41800  1.000 75.09899  ? 518  VAL A N   1 
ATOM   4073 C  CA  . VAL A 1 518 ? -3.92200  25.56500 0.45200   1.000 66.59186  ? 518  VAL A CA  1 
ATOM   4074 C  C   . VAL A 1 518 ? -3.69300  27.00900 0.01900   1.000 66.04396  ? 518  VAL A C   1 
ATOM   4075 O  O   . VAL A 1 518 ? -2.53500  27.38500 -0.17100  1.000 73.03190  ? 518  VAL A O   1 
ATOM   4076 C  CB  . VAL A 1 518 ? -3.63600  25.34000 1.94500   1.000 66.45250  ? 518  VAL A CB  1 
ATOM   4077 C  CG1 . VAL A 1 518 ? -4.38200  26.33800 2.81500   1.000 62.29486  ? 518  VAL A CG1 1 
ATOM   4078 C  CG2 . VAL A 1 518 ? -3.96700  23.91900 2.36700   1.000 71.75241  ? 518  VAL A CG2 1 
ATOM   4079 N  N   . SER A 1 519 ? -4.77400  27.75400 -0.18300  1.000 62.02054  ? 519  SER A N   1 
ATOM   4080 C  CA  . SER A 1 519 ? -4.68200  29.17500 -0.58600  1.000 64.90143  ? 519  SER A CA  1 
ATOM   4081 C  C   . SER A 1 519 ? -4.74500  30.03900 0.67500   1.000 68.21446  ? 519  SER A C   1 
ATOM   4082 O  O   . SER A 1 519 ? -5.67000  29.84300 1.47700   1.000 68.75543  ? 519  SER A O   1 
ATOM   4083 C  CB  . SER A 1 519 ? -5.77800  29.50800 -1.54700  1.000 58.51532  ? 519  SER A CB  1 
ATOM   4084 O  OG  . SER A 1 519 ? -5.82200  28.58900 -2.62500  1.000 58.23541  ? 519  SER A OG  1 
ATOM   4085 N  N   . LEU A 1 520 ? -3.76600  30.92500 0.84400   1.000 64.04389  ? 520  LEU A N   1 
ATOM   4086 C  CA  . LEU A 1 520 ? -3.69600  31.70700 2.09800   1.000 68.06016  ? 520  LEU A CA  1 
ATOM   4087 C  C   . LEU A 1 520 ? -3.60300  33.20800 1.81100   1.000 70.05463  ? 520  LEU A C   1 
ATOM   4088 O  O   . LEU A 1 520 ? -2.78500  33.60600 0.97700   1.000 76.61913  ? 520  LEU A O   1 
ATOM   4089 C  CB  . LEU A 1 520 ? -2.48700  31.21100 2.88600   1.000 71.76866  ? 520  LEU A CB  1 
ATOM   4090 C  CG  . LEU A 1 520 ? -2.47800  29.73000 3.26500   1.000 62.12681  ? 520  LEU A CG  1 
ATOM   4091 C  CD1 . LEU A 1 520 ? -1.11200  29.38300 3.81600   1.000 62.05461  ? 520  LEU A CD1 1 
ATOM   4092 C  CD2 . LEU A 1 520 ? -3.54100  29.49700 4.31400   1.000 69.94720  ? 520  LEU A CD2 1 
ATOM   4093 N  N   . GLY A 1 521 ? -4.45000  33.99400 2.46000   1.000 72.34622  ? 521  GLY A N   1 
ATOM   4094 C  CA  . GLY A 1 521 ? -4.41400  35.46100 2.34100   1.000 71.26375  ? 521  GLY A CA  1 
ATOM   4095 C  C   . GLY A 1 521 ? -3.65300  36.05900 3.50000   1.000 78.73477  ? 521  GLY A C   1 
ATOM   4096 O  O   . GLY A 1 521 ? -2.82200  35.35300 4.08200   1.000 79.67524  ? 521  GLY A O   1 
ATOM   4097 N  N   . LEU A 1 522 ? -3.85900  37.35000 3.75700   1.000 80.65263  ? 522  LEU A N   1 
ATOM   4098 C  CA  . LEU A 1 522 ? -3.09700  38.06700 4.81200   1.000 85.71935  ? 522  LEU A CA  1 
ATOM   4099 C  C   . LEU A 1 522 ? -3.43300  37.48600 6.18300   1.000 80.96066  ? 522  LEU A C   1 
ATOM   4100 O  O   . LEU A 1 522 ? -4.61500  37.45500 6.53900   1.000 87.35679  ? 522  LEU A O   1 
ATOM   4101 C  CB  . LEU A 1 522 ? -3.39100  39.56800 4.77700   1.000 87.18906  ? 522  LEU A CB  1 
ATOM   4102 C  CG  . LEU A 1 522 ? -2.95600  40.35600 3.53800   1.000 88.92052  ? 522  LEU A CG  1 
ATOM   4103 C  CD1 . LEU A 1 522 ? -3.43400  41.79000 3.57200   1.000 72.10276  ? 522  LEU A CD1 1 
ATOM   4104 C  CD2 . LEU A 1 522 ? -1.47500  40.28900 3.24000   1.000 90.31976  ? 522  LEU A CD2 1 
ATOM   4105 N  N   . GLY A 1 523 ? -2.42000  37.01700 6.90000   1.000 86.95203  ? 523  GLY A N   1 
ATOM   4106 C  CA  . GLY A 1 523 ? -2.65100  36.54000 8.27000   1.000 87.62647  ? 523  GLY A CA  1 
ATOM   4107 C  C   . GLY A 1 523 ? -1.48900  35.73600 8.79400   1.000 87.36891  ? 523  GLY A C   1 
ATOM   4108 O  O   . GLY A 1 523 ? -0.41700  35.75600 8.16200   1.000 86.14639  ? 523  GLY A O   1 
ATOM   4109 N  N   . ASP A 1 524 ? -1.68900  35.08300 9.93500   1.000 90.39035  ? 524  ASP A N   1 
ATOM   4110 C  CA  . ASP A 1 524 ? -0.66300  34.15900 10.47000  1.000 85.94623  ? 524  ASP A CA  1 
ATOM   4111 C  C   . ASP A 1 524 ? -1.28000  32.76100 10.43600  1.000 80.48577  ? 524  ASP A C   1 
ATOM   4112 O  O   . ASP A 1 524 ? -2.42200  32.60800 10.90700  1.000 75.24197  ? 524  ASP A O   1 
ATOM   4113 C  CB  . ASP A 1 524 ? -0.19900  34.58200 11.85300  1.000 96.37819  ? 524  ASP A CB  1 
ATOM   4114 C  CG  . ASP A 1 524 ? 0.36200   35.99000 11.97400  1.000 99.39389  ? 524  ASP A CG  1 
ATOM   4115 O  OD1 . ASP A 1 524 ? 1.36000   36.28700 11.28800  1.000 100.42507 ? 524  ASP A OD1 1 
ATOM   4116 O  OD2 . ASP A 1 524 ? -0.19700  36.77000 12.76900  1.000 103.71524 ? 524  ASP A OD2 1 
ATOM   4117 N  N   . PHE A 1 525 ? -0.55300  31.80500 9.87100   1.000 81.83207  ? 525  PHE A N   1 
ATOM   4118 C  CA  . PHE A 1 525 ? -1.11100  30.44300 9.72400   1.000 77.19550  ? 525  PHE A CA  1 
ATOM   4119 C  C   . PHE A 1 525 ? -0.23000  29.45100 10.48600  1.000 74.88038  ? 525  PHE A C   1 
ATOM   4120 O  O   . PHE A 1 525 ? 0.83900   29.08600 9.98400   1.000 68.65873  ? 525  PHE A O   1 
ATOM   4121 C  CB  . PHE A 1 525 ? -1.31800  30.14800 8.23600   1.000 72.72805  ? 525  PHE A CB  1 
ATOM   4122 C  CG  . PHE A 1 525 ? -1.98300  31.27500 7.49200   1.000 69.92674  ? 525  PHE A CG  1 
ATOM   4123 C  CD1 . PHE A 1 525 ? -3.33600  31.51800 7.64700   1.000 72.19759  ? 525  PHE A CD1 1 
ATOM   4124 C  CD2 . PHE A 1 525 ? -1.25200  32.10900 6.66500   1.000 76.38144  ? 525  PHE A CD2 1 
ATOM   4125 C  CE1 . PHE A 1 525 ? -3.94900  32.56000 6.97400   1.000 75.68951  ? 525  PHE A CE1 1 
ATOM   4126 C  CE2 . PHE A 1 525 ? -1.86700  33.15300 5.99500   1.000 79.65274  ? 525  PHE A CE2 1 
ATOM   4127 C  CZ  . PHE A 1 525 ? -3.21300  33.37500 6.15000   1.000 77.90154  ? 525  PHE A CZ  1 
ATOM   4128 N  N   . SER A 1 526 ? -0.68800  29.05000 11.67100  1.000 81.35314  ? 526  SER A N   1 
ATOM   4129 C  CA  . SER A 1 526 ? 0.03200   28.05600 12.50100  1.000 74.79100  ? 526  SER A CA  1 
ATOM   4130 C  C   . SER A 1 526 ? -0.02200  26.69500 11.82000  1.000 84.33001  ? 526  SER A C   1 
ATOM   4131 O  O   . SER A 1 526 ? -0.77700  26.54400 10.85300  1.000 84.04794  ? 526  SER A O   1 
ATOM   4132 C  CB  . SER A 1 526 ? -0.61100  27.96900 13.83900  1.000 80.50576  ? 526  SER A CB  1 
ATOM   4133 O  OG  . SER A 1 526 ? -1.61500  26.96800 13.84200  1.000 80.03618  ? 526  SER A OG  1 
ATOM   4134 N  N   . GLU A 1 527 ? 0.73100   25.73300 12.34100  1.000 86.58534  ? 527  GLU A N   1 
ATOM   4135 C  CA  . GLU A 1 527 ? 0.70000   24.36900 11.77000  1.000 84.47679  ? 527  GLU A CA  1 
ATOM   4136 C  C   . GLU A 1 527 ? -0.69300  23.80900 12.00700  1.000 76.09990  ? 527  GLU A C   1 
ATOM   4137 O  O   . GLU A 1 527 ? -1.19400  23.07900 11.15100  1.000 78.76874  ? 527  GLU A O   1 
ATOM   4138 C  CB  . GLU A 1 527 ? 1.75300   23.48700 12.43500  1.000 86.04348  ? 527  GLU A CB  1 
ATOM   4139 N  N   . GLU A 1 528 ? -1.28300  24.15800 13.13700  1.000 73.11654  ? 528  GLU A N   1 
ATOM   4140 C  CA  . GLU A 1 528 ? -2.66800  23.71500 13.37100  1.000 71.43591  ? 528  GLU A CA  1 
ATOM   4141 C  C   . GLU A 1 528 ? -3.51000  24.23900 12.21000  1.000 67.70242  ? 528  GLU A C   1 
ATOM   4142 O  O   . GLU A 1 528 ? -4.33800  23.48200 11.69100  1.000 63.57655  ? 528  GLU A O   1 
ATOM   4143 C  CB  . GLU A 1 528 ? -3.18400  24.23400 14.70700  1.000 75.10897  ? 528  GLU A CB  1 
ATOM   4144 C  CG  . GLU A 1 528 ? -4.49200  23.59500 15.12800  1.000 72.02551  ? 528  GLU A CG  1 
ATOM   4145 C  CD  . GLU A 1 528 ? -4.93400  23.94200 16.53700  1.000 83.81498  ? 528  GLU A CD  1 
ATOM   4146 O  OE1 . GLU A 1 528 ? -4.51200  24.99800 17.04100  1.000 83.39664  ? 528  GLU A OE1 1 
ATOM   4147 O  OE2 . GLU A 1 528 ? -5.69500  23.15200 17.12500  1.000 83.93195  ? 528  GLU A OE2 1 
ATOM   4148 N  N   . PHE A 1 529 ? -3.27400  25.48900 11.81600  1.000 72.82827  ? 529  PHE A N   1 
ATOM   4149 C  CA  . PHE A 1 529 ? -4.14000  26.06800 10.75600  1.000 68.17532  ? 529  PHE A CA  1 
ATOM   4150 C  C   . PHE A 1 529 ? -3.91200  25.28300 9.48400   1.000 67.36521  ? 529  PHE A C   1 
ATOM   4151 O  O   . PHE A 1 529 ? -4.85900  24.77700 8.87300   1.000 64.63690  ? 529  PHE A O   1 
ATOM   4152 C  CB  . PHE A 1 529 ? -3.83400  27.55400 10.55900  1.000 65.35921  ? 529  PHE A CB  1 
ATOM   4153 C  CG  . PHE A 1 529 ? -4.72600  28.31100 9.58500   1.000 55.89851  ? 529  PHE A CG  1 
ATOM   4154 C  CD1 . PHE A 1 529 ? -4.65300  28.08300 8.21700   1.000 59.77758  ? 529  PHE A CD1 1 
ATOM   4155 C  CD2 . PHE A 1 529 ? -5.61800  29.27200 10.04100  1.000 61.23322  ? 529  PHE A CD2 1 
ATOM   4156 C  CE1 . PHE A 1 529 ? -5.46500  28.77800 7.34000   1.000 62.51719  ? 529  PHE A CE1 1 
ATOM   4157 C  CE2 . PHE A 1 529 ? -6.42500  29.96900 9.15700   1.000 52.79299  ? 529  PHE A CE2 1 
ATOM   4158 C  CZ  . PHE A 1 529 ? -6.34600  29.72000 7.81100   1.000 61.77189  ? 529  PHE A CZ  1 
ATOM   4159 N  N   . LEU A 1 530 ? -2.65200  25.16500 9.10400   1.000 70.12005  ? 530  LEU A N   1 
ATOM   4160 C  CA  . LEU A 1 530 ? -2.36900  24.49800 7.83800   1.000 75.06111  ? 530  LEU A CA  1 
ATOM   4161 C  C   . LEU A 1 530 ? -2.81600  23.04300 7.86700   1.000 75.28180  ? 530  LEU A C   1 
ATOM   4162 O  O   . LEU A 1 530 ? -3.30600  22.51600 6.86100   1.000 72.68999  ? 530  LEU A O   1 
ATOM   4163 C  CB  . LEU A 1 530 ? -0.87900  24.60100 7.51500   1.000 73.29653  ? 530  LEU A CB  1 
ATOM   4164 C  CG  . LEU A 1 530 ? -0.33800  26.02600 7.39300   1.000 68.07068  ? 530  LEU A CG  1 
ATOM   4165 C  CD1 . LEU A 1 530 ? 1.15200   26.01300 7.10000   1.000 70.32962  ? 530  LEU A CD1 1 
ATOM   4166 C  CD2 . LEU A 1 530 ? -1.09400  26.79400 6.32000   1.000 60.30588  ? 530  LEU A CD2 1 
ATOM   4167 N  N   . THR A 1 531 ? -2.66500  22.37800 9.01500   1.000 73.40494  ? 531  THR A N   1 
ATOM   4168 C  CA  . THR A 1 531 ? -3.08900  20.98700 9.12300   1.000 72.51940  ? 531  THR A CA  1 
ATOM   4169 C  C   . THR A 1 531 ? -4.60300  20.86100 9.02000   1.000 74.05245  ? 531  THR A C   1 
ATOM   4170 O  O   . THR A 1 531 ? -5.11000  19.96400 8.33600   1.000 73.33727  ? 531  THR A O   1 
ATOM   4171 C  CB  . THR A 1 531 ? -2.58600  20.38300 10.43500  1.000 75.79727  ? 531  THR A CB  1 
ATOM   4172 O  OG1 . THR A 1 531 ? -1.15500  20.46700 10.48400  1.000 76.43662  ? 531  THR A OG1 1 
ATOM   4173 C  CG2 . THR A 1 531 ? -3.00300  18.92500 10.54500  1.000 75.44797  ? 531  THR A CG2 1 
ATOM   4174 N  N   . GLU A 1 532 ? -5.34700  21.75100 9.68400   1.000 69.87360  ? 532  GLU A N   1 
ATOM   4175 C  CA  . GLU A 1 532 ? -6.79900  21.72100 9.56000   1.000 70.71011  ? 532  GLU A CA  1 
ATOM   4176 C  C   . GLU A 1 532 ? -7.25700  22.12300 8.16600   1.000 68.65929  ? 532  GLU A C   1 
ATOM   4177 O  O   . GLU A 1 532 ? -8.35000  21.72900 7.74600   1.000 60.64709  ? 532  GLU A O   1 
ATOM   4178 C  CB  . GLU A 1 532 ? -7.44300  22.63200 10.60500  1.000 60.89770  ? 532  GLU A CB  1 
ATOM   4179 C  CG  . GLU A 1 532 ? -8.89000  22.27900 10.91300  1.000 61.59705  ? 532  GLU A CG  1 
ATOM   4180 C  CD  . GLU A 1 532 ? -9.55800  23.28500 11.82500  1.000 55.31877  ? 532  GLU A CD  1 
ATOM   4181 O  OE1 . GLU A 1 532 ? -9.58200  24.48100 11.47300  1.000 57.19985  ? 532  GLU A OE1 1 
ATOM   4182 O  OE2 . GLU A 1 532 ? -10.05500 22.88100 12.89600  1.000 57.31717  ? 532  GLU A OE2 1 
ATOM   4183 N  N   . ALA A 1 533 ? -6.44500  22.89600 7.44000   1.000 73.05489  ? 533  ALA A N   1 
ATOM   4184 C  CA  . ALA A 1 533 ? -6.77300  23.23000 6.06100   1.000 69.00790  ? 533  ALA A CA  1 
ATOM   4185 C  C   . ALA A 1 533 ? -6.65100  22.03000 5.13200   1.000 72.01346  ? 533  ALA A C   1 
ATOM   4186 O  O   . ALA A 1 533 ? -7.24400  22.03900 4.04900   1.000 66.06425  ? 533  ALA A O   1 
ATOM   4187 C  CB  . ALA A 1 533 ? -5.87800  24.36600 5.56400   1.000 68.55977  ? 533  ALA A CB  1 
ATOM   4188 N  N   . GLY A 1 534 ? -5.89600  21.00700 5.52700   1.000 78.70602  ? 534  GLY A N   1 
ATOM   4189 C  CA  . GLY A 1 534 ? -5.76800  19.80400 4.72800   1.000 82.87289  ? 534  GLY A CA  1 
ATOM   4190 C  C   . GLY A 1 534 ? -4.36200  19.55300 4.22600   1.000 83.44111  ? 534  GLY A C   1 
ATOM   4191 O  O   . GLY A 1 534 ? -4.15800  18.74600 3.31400   1.000 76.61211  ? 534  GLY A O   1 
ATOM   4192 N  N   . LEU A 1 535 ? -3.38200  20.28400 4.76200   1.000 75.70442  ? 535  LEU A N   1 
ATOM   4193 C  CA  . LEU A 1 535 ? -1.97200  20.11400 4.33500   1.000 70.86468  ? 535  LEU A CA  1 
ATOM   4194 C  C   . LEU A 1 535 ? -1.04800  20.34400 5.52400   1.000 88.74326  ? 535  LEU A C   1 
ATOM   4195 O  O   . LEU A 1 535 ? -0.80400  21.51400 5.85400   1.000 81.99768  ? 535  LEU A O   1 
ATOM   4196 C  CB  . LEU A 1 535 ? -1.63700  21.10100 3.22300   1.000 66.90353  ? 535  LEU A CB  1 
ATOM   4197 C  CG  . LEU A 1 535 ? -0.59900  20.63100 2.20800   1.000 83.29507  ? 535  LEU A CG  1 
ATOM   4198 C  CD1 . LEU A 1 535 ? -1.22800  19.69300 1.19200   1.000 95.79509  ? 535  LEU A CD1 1 
ATOM   4199 C  CD2 . LEU A 1 535 ? 0.04600   21.81300 1.50500   1.000 82.67867  ? 535  LEU A CD2 1 
ATOM   4200 N  N   . LYS A 1 536 ? -0.54400  19.26300 6.12700   1.000 91.70820  ? 536  LYS A N   1 
ATOM   4201 C  CA  . LYS A 1 536 ? 0.40100   19.39100 7.22600   1.000 89.94435  ? 536  LYS A CA  1 
ATOM   4202 C  C   . LYS A 1 536 ? 1.63400   20.16000 6.75600   1.000 100.86520 ? 536  LYS A C   1 
ATOM   4203 O  O   . LYS A 1 536 ? 2.14500   19.90400 5.65800   1.000 96.59841  ? 536  LYS A O   1 
ATOM   4204 C  CB  . LYS A 1 536 ? 0.80300   18.01200 7.75100   1.000 86.25033  ? 536  LYS A CB  1 
ATOM   4205 N  N   . PRO A 1 537 ? 2.13800   21.10500 7.55400   1.000 100.79997 ? 537  PRO A N   1 
ATOM   4206 C  CA  . PRO A 1 537 ? 3.22600   21.97300 7.06800   1.000 95.72697  ? 537  PRO A CA  1 
ATOM   4207 C  C   . PRO A 1 537 ? 4.52500   21.23900 6.78000   1.000 112.37603 ? 537  PRO A C   1 
ATOM   4208 O  O   . PRO A 1 537 ? 5.33900   21.74600 5.99900   1.000 107.80822 ? 537  PRO A O   1 
ATOM   4209 C  CB  . PRO A 1 537 ? 3.39600   22.99000 8.20500   1.000 100.05767 ? 537  PRO A CB  1 
ATOM   4210 C  CG  . PRO A 1 537 ? 2.87000   22.29300 9.41800   1.000 107.70076 ? 537  PRO A CG  1 
ATOM   4211 C  CD  . PRO A 1 537 ? 1.74000   21.43100 8.93400   1.000 93.88801  ? 537  PRO A CD  1 
ATOM   4212 N  N   . ASP A 1 538 ? 4.74900   20.07000 7.37500   1.000 127.62891 ? 538  ASP A N   1 
ATOM   4213 C  CA  . ASP A 1 538 ? 5.96500   19.30900 7.11800   1.000 130.83610 ? 538  ASP A CA  1 
ATOM   4214 C  C   . ASP A 1 538 ? 5.89800   18.50000 5.82600   1.000 128.94527 ? 538  ASP A C   1 
ATOM   4215 O  O   . ASP A 1 538 ? 6.82100   17.72600 5.55000   1.000 134.95326 ? 538  ASP A O   1 
ATOM   4216 C  CB  . ASP A 1 538 ? 6.27200   18.38400 8.30000   1.000 136.13444 ? 538  ASP A CB  1 
ATOM   4217 C  CG  . ASP A 1 538 ? 5.09700   17.50600 8.67400   1.000 133.53422 ? 538  ASP A CG  1 
ATOM   4218 O  OD1 . ASP A 1 538 ? 4.00300   17.69500 8.10300   1.000 132.36703 ? 538  ASP A OD1 1 
ATOM   4219 O  OD2 . ASP A 1 538 ? 5.26800   16.62400 9.54100   1.000 136.61197 ? 538  ASP A OD2 1 
ATOM   4220 N  N   . THR A 1 539 ? 4.83500   18.65700 5.03700   1.000 114.66503 ? 539  THR A N   1 
ATOM   4221 C  CA  . THR A 1 539 ? 4.71900   18.00900 3.73700   1.000 109.71071 ? 539  THR A CA  1 
ATOM   4222 C  C   . THR A 1 539 ? 4.62800   19.01500 2.59700   1.000 102.57685 ? 539  THR A C   1 
ATOM   4223 O  O   . THR A 1 539 ? 4.35000   18.62200 1.45700   1.000 108.89876 ? 539  THR A O   1 
ATOM   4224 C  CB  . THR A 1 539 ? 3.50500   17.07400 3.70500   1.000 103.21083 ? 539  THR A CB  1 
ATOM   4225 O  OG1 . THR A 1 539 ? 2.32700   17.80000 4.07600   1.000 99.26986  ? 539  THR A OG1 1 
ATOM   4226 C  CG2 . THR A 1 539 ? 3.70000   15.91100 4.66400   1.000 101.83911 ? 539  THR A CG2 1 
ATOM   4227 N  N   . ILE A 1 540 ? 4.85000   20.29600 2.87100   1.000 98.81522  ? 540  ILE A N   1 
ATOM   4228 C  CA  . ILE A 1 540 ? 4.79000   21.32700 1.84200   1.000 100.96601 ? 540  ILE A CA  1 
ATOM   4229 C  C   . ILE A 1 540 ? 6.12200   21.38100 1.10900   1.000 109.24484 ? 540  ILE A C   1 
ATOM   4230 O  O   . ILE A 1 540 ? 7.19100   21.28500 1.72400   1.000 106.32471 ? 540  ILE A O   1 
ATOM   4231 C  CB  . ILE A 1 540 ? 4.43900   22.69000 2.46600   1.000 95.93367  ? 540  ILE A CB  1 
ATOM   4232 C  CG1 . ILE A 1 540 ? 3.10500   22.61000 3.21000   1.000 94.76048  ? 540  ILE A CG1 1 
ATOM   4233 C  CG2 . ILE A 1 540 ? 4.39200   23.77800 1.40300   1.000 91.90261  ? 540  ILE A CG2 1 
ATOM   4234 C  CD1 . ILE A 1 540 ? 2.66000   23.92500 3.80900   1.000 77.35181  ? 540  ILE A CD1 1 
ATOM   4235 N  N   . ARG A 1 541 ? 6.06600   21.53100 -0.21500  1.000 116.86689 ? 541  ARG A N   1 
ATOM   4236 C  CA  . ARG A 1 541 ? 7.28300   21.64000 -1.00600  1.000 121.55694 ? 541  ARG A CA  1 
ATOM   4237 C  C   . ARG A 1 541 ? 7.25300   22.75300 -2.04500  1.000 121.68523 ? 541  ARG A C   1 
ATOM   4238 O  O   . ARG A 1 541 ? 8.26000   22.94500 -2.73300  1.000 119.61600 ? 541  ARG A O   1 
ATOM   4239 C  CB  . ARG A 1 541 ? 7.59700   20.30400 -1.70300  1.000 118.26450 ? 541  ARG A CB  1 
ATOM   4240 C  CG  . ARG A 1 541 ? 7.99400   19.19000 -0.74400  1.000 118.73788 ? 541  ARG A CG  1 
ATOM   4241 C  CD  . ARG A 1 541 ? 8.13000   17.84900 -1.44700  1.000 124.26103 ? 541  ARG A CD  1 
ATOM   4242 N  NE  . ARG A 1 541 ? 6.86200   17.38700 -2.00000  1.000 126.36053 ? 541  ARG A NE  1 
ATOM   4243 C  CZ  . ARG A 1 541 ? 6.70500   16.24800 -2.66100  1.000 130.32874 ? 541  ARG A CZ  1 
ATOM   4244 N  NH1 . ARG A 1 541 ? 7.72000   15.42500 -2.87200  1.000 133.02166 ? 541  ARG A NH1 1 
ATOM   4245 N  NH2 . ARG A 1 541 ? 5.50100   15.92700 -3.12400  1.000 132.49605 ? 541  ARG A NH2 1 
ATOM   4246 N  N   . PHE A 1 542 ? 6.15400   23.49300 -2.18300  1.000 115.96864 ? 542  PHE A N   1 
ATOM   4247 C  CA  . PHE A 1 542 ? 6.09600   24.59000 -3.14000  1.000 112.20036 ? 542  PHE A CA  1 
ATOM   4248 C  C   . PHE A 1 542 ? 5.28200   25.73500 -2.55600  1.000 109.90666 ? 542  PHE A C   1 
ATOM   4249 O  O   . PHE A 1 542 ? 4.27100   25.50400 -1.89000  1.000 109.58669 ? 542  PHE A O   1 
ATOM   4250 C  CB  . PHE A 1 542 ? 5.48500   24.13200 -4.47000  1.000 111.43665 ? 542  PHE A CB  1 
ATOM   4251 C  CG  . PHE A 1 542 ? 5.71300   25.08900 -5.60300  1.000 114.50314 ? 542  PHE A CG  1 
ATOM   4252 C  CD1 . PHE A 1 542 ? 6.89300   25.05400 -6.32600  1.000 113.71205 ? 542  PHE A CD1 1 
ATOM   4253 C  CD2 . PHE A 1 542 ? 4.74800   26.01900 -5.94900  1.000 117.93567 ? 542  PHE A CD2 1 
ATOM   4254 C  CE1 . PHE A 1 542 ? 7.10800   25.93000 -7.37100  1.000 114.20094 ? 542  PHE A CE1 1 
ATOM   4255 C  CE2 . PHE A 1 542 ? 4.95700   26.89900 -6.99400  1.000 119.38466 ? 542  PHE A CE2 1 
ATOM   4256 C  CZ  . PHE A 1 542 ? 6.13900   26.85300 -7.70700  1.000 116.25965 ? 542  PHE A CZ  1 
ATOM   4257 N  N   . ILE A 1 543 ? 5.76500   26.96700 -2.74600  1.000 100.40567 ? 543  ILE A N   1 
ATOM   4258 C  CA  . ILE A 1 543 ? 5.00500   28.16000 -2.27500  1.000 104.14627 ? 543  ILE A CA  1 
ATOM   4259 C  C   . ILE A 1 543 ? 4.96900   29.18500 -3.41300  1.000 104.52496 ? 543  ILE A C   1 
ATOM   4260 O  O   . ILE A 1 543 ? 6.04400   29.53600 -3.92200  1.000 107.03150 ? 543  ILE A O   1 
ATOM   4261 C  CB  . ILE A 1 543 ? 5.62300   28.76700 -1.00900  1.000 98.50495  ? 543  ILE A CB  1 
ATOM   4262 C  CG1 . ILE A 1 543 ? 5.79900   27.72500 0.09400   1.000 93.20079  ? 543  ILE A CG1 1 
ATOM   4263 C  CG2 . ILE A 1 543 ? 4.80800   29.96700 -0.53000  1.000 79.72838  ? 543  ILE A CG2 1 
ATOM   4264 C  CD1 . ILE A 1 543 ? 6.44900   28.26700 1.35300   1.000 85.89154  ? 543  ILE A CD1 1 
ATOM   4265 N  N   . ARG A 1 544 ? 3.77200   29.62900 -3.79300  1.000 100.86492 ? 544  ARG A N   1 
ATOM   4266 C  CA  . ARG A 1 544 ? 3.64100   30.60100 -4.90500  1.000 102.27924 ? 544  ARG A CA  1 
ATOM   4267 C  C   . ARG A 1 544 ? 3.12900   31.89700 -4.30200  1.000 101.19097 ? 544  ARG A C   1 
ATOM   4268 O  O   . ARG A 1 544 ? 2.10400   31.85000 -3.60900  1.000 97.50901  ? 544  ARG A O   1 
ATOM   4269 C  CB  . ARG A 1 544 ? 2.70700   30.09000 -6.00400  1.000 101.28076 ? 544  ARG A CB  1 
ATOM   4270 C  CG  . ARG A 1 544 ? 2.44000   31.06300 -7.14100  1.000 100.86860 ? 544  ARG A CG  1 
ATOM   4271 C  CD  . ARG A 1 544 ? 1.76200   30.32700 -8.28200  1.000 96.22334  ? 544  ARG A CD  1 
ATOM   4272 N  NE  . ARG A 1 544 ? 0.56300   29.60300 -7.84900  1.000 90.95180  ? 544  ARG A NE  1 
ATOM   4273 C  CZ  . ARG A 1 544 ? -0.17400  28.85600 -8.65600  1.000 89.83805  ? 544  ARG A CZ  1 
ATOM   4274 N  NH1 . ARG A 1 544 ? 0.20900   28.66600 -9.90300  1.000 91.19913  ? 544  ARG A NH1 1 
ATOM   4275 N  NH2 . ARG A 1 544 ? -1.28400  28.29500 -8.21500  1.000 90.46722  ? 544  ARG A NH2 1 
ATOM   4276 N  N   . VAL A 1 545 ? 3.80800   33.00400 -4.58000  1.000 100.22836 ? 545  VAL A N   1 
ATOM   4277 C  CA  . VAL A 1 545 ? 3.42600   34.25800 -3.88200  1.000 98.95256  ? 545  VAL A CA  1 
ATOM   4278 C  C   . VAL A 1 545 ? 2.78800   35.24400 -4.85300  1.000 95.96201  ? 545  VAL A C   1 
ATOM   4279 O  O   . VAL A 1 545 ? 3.25400   35.34800 -5.99700  1.000 98.57102  ? 545  VAL A O   1 
ATOM   4280 C  CB  . VAL A 1 545 ? 4.67800   34.84800 -3.21700  1.000 104.53223 ? 545  VAL A CB  1 
ATOM   4281 C  CG1 . VAL A 1 545 ? 4.39400   36.18900 -2.56400  1.000 107.25545 ? 545  VAL A CG1 1 
ATOM   4282 C  CG2 . VAL A 1 545 ? 5.26700   33.88200 -2.19700  1.000 105.62664 ? 545  VAL A CG2 1 
ATOM   4283 N  N   . SER A 1 546 ? 1.74900   35.92600 -4.39200  1.000 94.30680  ? 546  SER A N   1 
ATOM   4284 C  CA  . SER A 1 546 ? 1.13900   36.97400 -5.23900  1.000 91.69396  ? 546  SER A CA  1 
ATOM   4285 C  C   . SER A 1 546 ? 1.94900   38.26600 -5.10800  1.000 105.71153 ? 546  SER A C   1 
ATOM   4286 O  O   . SER A 1 546 ? 2.89300   38.29100 -4.30600  1.000 113.74265 ? 546  SER A O   1 
ATOM   4287 C  CB  . SER A 1 546 ? -0.29700  37.17500 -4.86700  1.000 95.80668  ? 546  SER A CB  1 
ATOM   4288 O  OG  . SER A 1 546 ? -0.99100  35.94200 -4.97300  1.000 85.57486  ? 546  SER A OG  1 
ATOM   4289 N  N   . SER A 1 547 ? 1.58200   39.27300 -5.89400  1.000 106.97763 ? 547  SER A N   1 
ATOM   4290 C  CA  . SER A 1 547 ? 2.33600   40.54900 -5.94300  1.000 107.20589 ? 547  SER A CA  1 
ATOM   4291 C  C   . SER A 1 547 ? 2.58600   41.15100 -4.56500  1.000 118.50514 ? 547  SER A C   1 
ATOM   4292 O  O   . SER A 1 547 ? 1.64800   41.18400 -3.75500  1.000 117.41948 ? 547  SER A O   1 
ATOM   4293 C  CB  . SER A 1 547 ? 1.60400   41.53600 -6.81100  1.000 101.84751 ? 547  SER A CB  1 
ATOM   4294 O  OG  . SER A 1 547 ? 0.31700   41.81400 -6.28600  1.000 102.03664 ? 547  SER A OG  1 
ATOM   4295 N  N   . GLY A 1 548 ? 3.81800   41.58900 -4.31400  1.000 131.26502 ? 548  GLY A N   1 
ATOM   4296 C  CA  . GLY A 1 548 ? 4.12800   42.31900 -3.06800  1.000 135.42765 ? 548  GLY A CA  1 
ATOM   4297 C  C   . GLY A 1 548 ? 3.55300   41.68200 -1.82300  1.000 133.76994 ? 548  GLY A C   1 
ATOM   4298 O  O   . GLY A 1 548 ? 3.19800   42.43000 -0.89300  1.000 133.80478 ? 548  GLY A O   1 
ATOM   4299 N  N   . THR A 1 549 ? 3.50500   40.35900 -1.77800  1.000 121.65923 ? 549  THR A N   1 
ATOM   4300 C  CA  . THR A 1 549 ? 3.03500   39.69600 -0.54300  1.000 122.93037 ? 549  THR A CA  1 
ATOM   4301 C  C   . THR A 1 549 ? 4.23100   38.97700 0.08800   1.000 122.20423 ? 549  THR A C   1 
ATOM   4302 O  O   . THR A 1 549 ? 4.56100   37.88200 -0.38300  1.000 119.79610 ? 549  THR A O   1 
ATOM   4303 C  CB  . THR A 1 549 ? 1.82000   38.81600 -0.86600  1.000 111.56587 ? 549  THR A CB  1 
ATOM   4304 O  OG1 . THR A 1 549 ? 2.13500   37.99100 -1.98600  1.000 110.95294 ? 549  THR A OG1 1 
ATOM   4305 C  CG2 . THR A 1 549 ? 0.58200   39.62700 -1.17300  1.000 104.99706 ? 549  THR A CG2 1 
ATOM   4306 N  N   . LYS A 1 550 ? 4.85700   39.56900 1.11000   1.000 119.34850 ? 550  LYS A N   1 
ATOM   4307 C  CA  . LYS A 1 550 ? 6.05400   38.94700 1.66300   1.000 121.51915 ? 550  LYS A CA  1 
ATOM   4308 C  C   . LYS A 1 550 ? 5.65800   37.84700 2.63800   1.000 119.29430 ? 550  LYS A C   1 
ATOM   4309 O  O   . LYS A 1 550 ? 4.79400   38.05300 3.50000   1.000 117.67509 ? 550  LYS A O   1 
ATOM   4310 C  CB  . LYS A 1 550 ? 6.93500   39.98400 2.36000   1.000 123.49055 ? 550  LYS A CB  1 
ATOM   4311 N  N   . LEU A 1 551 ? 6.29300   36.68500 2.51000   1.000 118.11799 ? 551  LEU A N   1 
ATOM   4312 C  CA  . LEU A 1 551 ? 5.97400   35.53500 3.34100   1.000 121.27933 ? 551  LEU A CA  1 
ATOM   4313 C  C   . LEU A 1 551 ? 7.12700   35.27100 4.30000   1.000 126.99401 ? 551  LEU A C   1 
ATOM   4314 O  O   . LEU A 1 551 ? 8.29500   35.29900 3.90200   1.000 131.41852 ? 551  LEU A O   1 
ATOM   4315 C  CB  . LEU A 1 551 ? 5.68700   34.30200 2.48000   1.000 118.66965 ? 551  LEU A CB  1 
ATOM   4316 C  CG  . LEU A 1 551 ? 4.71700   33.26200 3.05400   1.000 115.95547 ? 551  LEU A CG  1 
ATOM   4317 C  CD1 . LEU A 1 551 ? 4.12600   32.42300 1.93600   1.000 106.99052 ? 551  LEU A CD1 1 
ATOM   4318 C  CD2 . LEU A 1 551 ? 5.39400   32.37000 4.08300   1.000 123.63244 ? 551  LEU A CD2 1 
ATOM   4319 N  N   . THR A 1 552 ? 6.79300   35.04100 5.56300   1.000 119.61361 ? 552  THR A N   1 
ATOM   4320 C  CA  . THR A 1 552 ? 7.75700   34.67100 6.59000   1.000 110.43797 ? 552  THR A CA  1 
ATOM   4321 C  C   . THR A 1 552 ? 7.52400   33.21000 6.94500   1.000 111.49752 ? 552  THR A C   1 
ATOM   4322 O  O   . THR A 1 552 ? 6.42500   32.84300 7.37800   1.000 114.35422 ? 552  THR A O   1 
ATOM   4323 C  CB  . THR A 1 552 ? 7.62300   35.56000 7.82800   1.000 105.52165 ? 552  THR A CB  1 
ATOM   4324 N  N   . VAL A 1 553 ? 8.54600   32.38400 6.73900   1.000 107.69407 ? 553  VAL A N   1 
ATOM   4325 C  CA  . VAL A 1 553 ? 8.46500   30.94500 6.95400   1.000 115.57257 ? 553  VAL A CA  1 
ATOM   4326 C  C   . VAL A 1 553 ? 9.14500   30.61300 8.27400   1.000 121.15325 ? 553  VAL A C   1 
ATOM   4327 O  O   . VAL A 1 553 ? 10.25800  31.08300 8.54700   1.000 133.14707 ? 553  VAL A O   1 
ATOM   4328 C  CB  . VAL A 1 553 ? 9.11500   30.17100 5.79400   1.000 112.62144 ? 553  VAL A CB  1 
ATOM   4329 C  CG1 . VAL A 1 553 ? 8.84100   28.68000 5.92800   1.000 114.05982 ? 553  VAL A CG1 1 
ATOM   4330 C  CG2 . VAL A 1 553 ? 8.61600   30.70000 4.45800   1.000 97.58675  ? 553  VAL A CG2 1 
ATOM   4331 N  N   . TYR A 1 554 ? 8.51000   29.72200 9.04000   1.000 115.83334 ? 554  TYR A N   1 
ATOM   4332 C  CA  . TYR A 1 554 ? 9.04200   29.30800 10.35600  1.000 121.98526 ? 554  TYR A CA  1 
ATOM   4333 C  C   . TYR A 1 554 ? 8.99200   27.78900 10.44700  1.000 121.76783 ? 554  TYR A C   1 
ATOM   4334 O  O   . TYR A 1 554 ? 8.14000   27.19400 9.77500   1.000 123.85566 ? 554  TYR A O   1 
ATOM   4335 C  CB  . TYR A 1 554 ? 8.14700   29.82900 11.47600  1.000 126.30303 ? 554  TYR A CB  1 
ATOM   4336 C  CG  . TYR A 1 554 ? 8.04000   31.32800 11.59800  1.000 131.58777 ? 554  TYR A CG  1 
ATOM   4337 C  CD1 . TYR A 1 554 ? 7.40800   32.08500 10.62700  1.000 125.82058 ? 554  TYR A CD1 1 
ATOM   4338 C  CD2 . TYR A 1 554 ? 8.52900   31.98600 12.71200  1.000 133.58545 ? 554  TYR A CD2 1 
ATOM   4339 C  CE1 . TYR A 1 554 ? 7.29700   33.46000 10.74200  1.000 124.57549 ? 554  TYR A CE1 1 
ATOM   4340 C  CE2 . TYR A 1 554 ? 8.42100   33.35800 12.84700  1.000 131.08392 ? 554  TYR A CE2 1 
ATOM   4341 C  CZ  . TYR A 1 554 ? 7.80400   34.09900 11.85700  1.000 127.85405 ? 554  TYR A CZ  1 
ATOM   4342 O  OH  . TYR A 1 554 ? 7.69400   35.45300 11.98400  1.000 126.27300 ? 554  TYR A OH  1 
ATOM   4343 N  N   . SER A 1 555 ? 9.82700   27.17800 11.28800  1.000 122.15731 ? 555  SER A N   1 
ATOM   4344 C  CA  . SER A 1 555 ? 9.73800   25.71000 11.49800  1.000 113.90993 ? 555  SER A CA  1 
ATOM   4345 C  C   . SER A 1 555 ? 8.87100   25.49900 12.72100  1.000 123.92517 ? 555  SER A C   1 
ATOM   4346 O  O   . SER A 1 555 ? 8.45200   24.35800 12.96600  1.000 118.95608 ? 555  SER A O   1 
ATOM   4347 C  CB  . SER A 1 555 ? 11.07800  25.09900 11.70200  1.000 116.81182 ? 555  SER A CB  1 
ATOM   4348 N  N   . THR A 1 556 ? 8.64800   26.58000 13.45900  1.000 134.97831 ? 556  THR A N   1 
ATOM   4349 C  CA  . THR A 1 556 ? 7.75600   26.51000 14.63600  1.000 137.06098 ? 556  THR A CA  1 
ATOM   4350 C  C   . THR A 1 556 ? 6.31500   26.34100 14.17300  1.000 134.94963 ? 556  THR A C   1 
ATOM   4351 O  O   . THR A 1 556 ? 5.93100   26.99500 13.19100  1.000 129.96901 ? 556  THR A O   1 
ATOM   4352 C  CB  . THR A 1 556 ? 7.83800   27.78500 15.48200  1.000 136.22474 ? 556  THR A CB  1 
ATOM   4353 N  N   . GLY A 1 557 ? 5.54900   25.51500 14.88100  1.000 138.20560 ? 557  GLY A N   1 
ATOM   4354 C  CA  . GLY A 1 557 ? 4.12100   25.38300 14.56600  1.000 130.07731 ? 557  GLY A CA  1 
ATOM   4355 C  C   . GLY A 1 557 ? 3.41000   26.55400 15.19300  1.000 131.18111 ? 557  GLY A C   1 
ATOM   4356 O  O   . GLY A 1 557 ? 2.17200   26.53800 15.21500  1.000 125.44513 ? 557  GLY A O   1 
ATOM   4357 N  N   . ASP A 1 558 ? 4.18000   27.47900 15.77200  1.000 133.29861 ? 558  ASP A N   1 
ATOM   4358 C  CA  . ASP A 1 558 ? 3.59700   28.68200 16.41500  1.000 130.23745 ? 558  ASP A CA  1 
ATOM   4359 C  C   . ASP A 1 558 ? 4.38600   29.92100 15.99800  1.000 128.15008 ? 558  ASP A C   1 
ATOM   4360 O  O   . ASP A 1 558 ? 4.32800   30.92100 16.72500  1.000 133.24404 ? 558  ASP A O   1 
ATOM   4361 C  CB  . ASP A 1 558 ? 3.58200   28.54600 17.93300  1.000 116.64284 ? 558  ASP A CB  1 
ATOM   4362 N  N   . LEU A 1 559 ? 5.08700   29.85500 14.87200  1.000 125.70009 ? 559  LEU A N   1 
ATOM   4363 C  CA  . LEU A 1 559 ? 5.80800   31.05100 14.37900  1.000 126.09050 ? 559  LEU A CA  1 
ATOM   4364 C  C   . LEU A 1 559 ? 6.71400   31.58200 15.49000  1.000 138.66435 ? 559  LEU A C   1 
ATOM   4365 O  O   . LEU A 1 559 ? 6.46600   32.70500 15.97200  1.000 134.37738 ? 559  LEU A O   1 
ATOM   4366 C  CB  . LEU A 1 559 ? 4.79100   32.11000 13.95500  1.000 115.04967 ? 559  LEU A CB  1 
ATOM   4367 N  N   . SER A 1 560 ? 7.70500   30.78500 15.89700  1.000 134.36990 ? 560  SER A N   1 
ATOM   4368 C  CA  . SER A 1 560 ? 8.60600   31.19500 17.00200  1.000 134.24033 ? 560  SER A CA  1 
ATOM   4369 C  C   . SER A 1 560 ? 10.01600  30.65200 16.78600  1.000 146.29159 ? 560  SER A C   1 
ATOM   4370 O  O   . SER A 1 560 ? 10.17000  29.42100 16.77500  1.000 147.95458 ? 560  SER A O   1 
ATOM   4371 C  CB  . SER A 1 560 ? 8.06000   30.73400 18.32100  1.000 132.63499 ? 560  SER A CB  1 
ATOM   4372 O  OG  . SER A 1 560 ? 6.80400   31.34100 18.58200  1.000 133.37951 ? 560  SER A OG  1 
ATOM   4373 N  N   . GLY A 1 561 ? 11.00200  31.53800 16.63000  1.000 157.96306 ? 561  GLY A N   1 
ATOM   4374 C  CA  . GLY A 1 561 ? 12.40600  31.11000 16.52900  1.000 151.44011 ? 561  GLY A CA  1 
ATOM   4375 C  C   . GLY A 1 561 ? 13.03600  31.51100 15.22400  1.000 151.63407 ? 561  GLY A C   1 
ATOM   4376 O  O   . GLY A 1 561 ? 12.44900  32.34800 14.51200  1.000 147.02695 ? 561  GLY A O   1 
ATOM   4377 N  N   . ASP A 1 562 ? 14.16600  30.89300 14.88700  1.000 143.99847 ? 562  ASP A N   1 
ATOM   4378 C  CA  . ASP A 1 562 ? 14.86400  31.37400 13.67200  1.000 137.10660 ? 562  ASP A CA  1 
ATOM   4379 C  C   . ASP A 1 562 ? 13.86100  31.23400 12.53000  1.000 140.68588 ? 562  ASP A C   1 
ATOM   4380 O  O   . ASP A 1 562 ? 13.24300  30.15600 12.39900  1.000 139.09134 ? 562  ASP A O   1 
ATOM   4381 C  CB  . ASP A 1 562 ? 16.17000  30.62900 13.44600  1.000 133.62137 ? 562  ASP A CB  1 
ATOM   4382 N  N   . SER A 1 563 ? 13.71400  32.28000 11.71100  1.000 139.96847 ? 563  SER A N   1 
ATOM   4383 C  CA  . SER A 1 563 ? 12.70400  32.25000 10.62000  1.000 132.51132 ? 563  SER A CA  1 
ATOM   4384 C  C   . SER A 1 563 ? 13.27200  32.84100 9.32600   1.000 135.82530 ? 563  SER A C   1 
ATOM   4385 O  O   . SER A 1 563 ? 13.69300  34.01300 9.35300   1.000 130.44491 ? 563  SER A O   1 
ATOM   4386 C  CB  . SER A 1 563 ? 11.44800  32.97300 11.03300  1.000 124.70250 ? 563  SER A CB  1 
ATOM   4387 O  OG  . SER A 1 563 ? 11.72700  34.32700 11.35200  1.000 119.72602 ? 563  SER A OG  1 
ATOM   4388 N  N   . LYS A 1 564 ? 13.27600  32.06100 8.24100   1.000 138.71593 ? 564  LYS A N   1 
ATOM   4389 C  CA  . LYS A 1 564 ? 13.72300  32.57400 6.91600   1.000 135.61848 ? 564  LYS A CA  1 
ATOM   4390 C  C   . LYS A 1 564 ? 12.55300  33.31900 6.26300   1.000 127.79244 ? 564  LYS A C   1 
ATOM   4391 O  O   . LYS A 1 564 ? 11.45200  33.29500 6.84400   1.000 128.08221 ? 564  LYS A O   1 
ATOM   4392 C  CB  . LYS A 1 564 ? 14.21200  31.42400 6.03100   1.000 128.87684 ? 564  LYS A CB  1 
ATOM   4393 N  N   . GLU A 1 565 ? 12.78100  33.96300 5.11300   1.000 111.50240 ? 565  GLU A N   1 
ATOM   4394 C  CA  . GLU A 1 565 ? 11.70400  34.76800 4.47400   1.000 108.66186 ? 565  GLU A CA  1 
ATOM   4395 C  C   . GLU A 1 565 ? 11.75600  34.65200 2.94700   1.000 102.61536 ? 565  GLU A C   1 
ATOM   4396 O  O   . GLU A 1 565 ? 12.85100  34.39500 2.41600   1.000 116.06595 ? 565  GLU A O   1 
ATOM   4397 C  CB  . GLU A 1 565 ? 11.81700  36.23100 4.90600   1.000 103.04562 ? 565  GLU A CB  1 
ATOM   4398 N  N   . LEU A 1 566 ? 10.61500  34.83300 2.27500   1.000 100.97177 ? 566  LEU A N   1 
ATOM   4399 C  CA  . LEU A 1 566 ? 10.53400  34.79200 0.82400   1.000 110.74152 ? 566  LEU A CA  1 
ATOM   4400 C  C   . LEU A 1 566 ? 9.69500   35.96000 0.32500   1.000 114.54803 ? 566  LEU A C   1 
ATOM   4401 O  O   . LEU A 1 566 ? 8.81600   36.46500 1.03300   1.000 113.11889 ? 566  LEU A O   1 
ATOM   4402 C  CB  . LEU A 1 566 ? 9.93300   33.46500 0.33400   1.000 93.29552  ? 566  LEU A CB  1 
ATOM   4403 N  N   . ASP A 1 567 ? 9.86800   36.30900 -0.94800  1.000 113.90554 ? 567  ASP A N   1 
ATOM   4404 C  CA  . ASP A 1 567 ? 9.07800   37.43100 -1.52100  1.000 116.18912 ? 567  ASP A CA  1 
ATOM   4405 C  C   . ASP A 1 567 ? 8.18600   36.90800 -2.64700  1.000 125.72446 ? 567  ASP A C   1 
ATOM   4406 O  O   . ASP A 1 567 ? 7.90700   35.69800 -2.66800  1.000 130.59253 ? 567  ASP A O   1 
ATOM   4407 C  CB  . ASP A 1 567 ? 9.97600   38.57200 -1.96500  1.000 106.77671 ? 567  ASP A CB  1 
ATOM   4408 N  N   . ALA A 1 568 ? 7.71700   37.80700 -3.50600  1.000 126.60656 ? 568  ALA A N   1 
ATOM   4409 C  CA  . ALA A 1 568 ? 6.80900   37.40100 -4.59600  1.000 121.69822 ? 568  ALA A CA  1 
ATOM   4410 C  C   . ALA A 1 568 ? 7.54100   36.41800 -5.50200  1.000 119.39255 ? 568  ALA A C   1 
ATOM   4411 O  O   . ALA A 1 568 ? 8.77300   36.32200 -5.39500  1.000 118.46025 ? 568  ALA A O   1 
ATOM   4412 C  CB  . ALA A 1 568 ? 6.35000   38.61800 -5.35200  1.000 116.10546 ? 568  ALA A CB  1 
ATOM   4413 N  N   . GLY A 1 569 ? 6.80300   35.72500 -6.35800  1.000 108.39722 ? 569  GLY A N   1 
ATOM   4414 C  CA  . GLY A 1 569 ? 7.42400   34.75200 -7.26400  1.000 110.07078 ? 569  GLY A CA  1 
ATOM   4415 C  C   . GLY A 1 569 ? 7.30900   33.35100 -6.72400  1.000 112.74799 ? 569  GLY A C   1 
ATOM   4416 O  O   . GLY A 1 569 ? 6.99400   33.20700 -5.54100  1.000 118.15332 ? 569  GLY A O   1 
ATOM   4417 N  N   . GLU A 1 570 ? 7.56700   32.35600 -7.57000  1.000 113.35196 ? 570  GLU A N   1 
ATOM   4418 C  CA  . GLU A 1 570 ? 7.45000   30.94100 -7.15000  1.000 114.50688 ? 570  GLU A CA  1 
ATOM   4419 C  C   . GLU A 1 570 ? 8.62800   30.59400 -6.25700  1.000 117.37003 ? 570  GLU A C   1 
ATOM   4420 O  O   . GLU A 1 570 ? 9.65500   31.27400 -6.36400  1.000 127.67752 ? 570  GLU A O   1 
ATOM   4421 C  CB  . GLU A 1 570 ? 7.49000   30.01800 -8.36600  1.000 123.58571 ? 570  GLU A CB  1 
ATOM   4422 C  CG  . GLU A 1 570 ? 6.25800   30.08900 -9.24700  1.000 124.82402 ? 570  GLU A CG  1 
ATOM   4423 C  CD  . GLU A 1 570 ? 6.23500   29.03300 -10.34000 1.000 124.75155 ? 570  GLU A CD  1 
ATOM   4424 O  OE1 . GLU A 1 570 ? 7.13700   28.17500 -10.34600 1.000 128.11145 ? 570  GLU A OE1 1 
ATOM   4425 O  OE2 . GLU A 1 570 ? 5.31800   29.07100 -11.18200 1.000 121.08487 ? 570  GLU A OE2 1 
ATOM   4426 N  N   . HIS A 1 571 ? 8.48400   29.57300 -5.41800  1.000 115.97609 ? 571  HIS A N   1 
ATOM   4427 C  CA  . HIS A 1 571 ? 9.63700   29.10900 -4.60200  1.000 115.53873 ? 571  HIS A CA  1 
ATOM   4428 C  C   . HIS A 1 571 ? 9.48500   27.61500 -4.29600  1.000 112.68440 ? 571  HIS A C   1 
ATOM   4429 O  O   . HIS A 1 571 ? 8.33400   27.13500 -4.24900  1.000 118.11507 ? 571  HIS A O   1 
ATOM   4430 C  CB  . HIS A 1 571 ? 9.75700   29.92600 -3.31100  1.000 109.49423 ? 571  HIS A CB  1 
ATOM   4431 C  CG  . HIS A 1 571 ? 9.67500   31.40600 -3.47200  1.000 114.80041 ? 571  HIS A CG  1 
ATOM   4432 N  ND1 . HIS A 1 571 ? 10.75000  32.19600 -3.81100  1.000 121.86864 ? 571  HIS A ND1 1 
ATOM   4433 C  CD2 . HIS A 1 571 ? 8.63100   32.23100 -3.36800  1.000 118.04374 ? 571  HIS A CD2 1 
ATOM   4434 C  CE1 . HIS A 1 571 ? 10.35700  33.45900 -3.89100  1.000 117.18634 ? 571  HIS A CE1 1 
ATOM   4435 N  NE2 . HIS A 1 571 ? 9.07200   33.50200 -3.62500  1.000 116.02577 ? 571  HIS A NE2 1 
ATOM   4436 N  N   . LYS A 1 572 ? 10.59900  26.90100 -4.09900  1.000 112.85925 ? 572  LYS A N   1 
ATOM   4437 C  CA  . LYS A 1 572 ? 10.57700  25.48400 -3.75700  1.000 109.59631 ? 572  LYS A CA  1 
ATOM   4438 C  C   . LYS A 1 572 ? 11.26200  25.30200 -2.41000  1.000 115.75601 ? 572  LYS A C   1 
ATOM   4439 O  O   . LYS A 1 572 ? 12.44300  25.63400 -2.26200  1.000 117.74440 ? 572  LYS A O   1 
ATOM   4440 C  CB  . LYS A 1 572 ? 11.26800  24.64800 -4.83400  1.000 100.99876 ? 572  LYS A CB  1 
ATOM   4441 N  N   . VAL A 1 573 ? 10.52400  24.78400 -1.43600  1.000 117.78256 ? 573  VAL A N   1 
ATOM   4442 C  CA  . VAL A 1 573 ? 11.03200  24.60100 -0.08300  1.000 115.87284 ? 573  VAL A CA  1 
ATOM   4443 C  C   . VAL A 1 573 ? 11.33400  23.12800 0.13700   1.000 117.78449 ? 573  VAL A C   1 
ATOM   4444 O  O   . VAL A 1 573 ? 10.67200  22.24400 -0.41800  1.000 113.32722 ? 573  VAL A O   1 
ATOM   4445 C  CB  . VAL A 1 573 ? 10.03200  25.12500 0.96900   1.000 104.17213 ? 573  VAL A CB  1 
ATOM   4446 N  N   . GLU A 1 574 ? 12.34900  22.86100 0.95400   1.000 115.04729 ? 574  GLU A N   1 
ATOM   4447 C  CA  . GLU A 1 574 ? 12.68400  21.48800 1.30100   1.000 119.98073 ? 574  GLU A CA  1 
ATOM   4448 C  C   . GLU A 1 574 ? 11.58500  20.88300 2.16400   1.000 116.48504 ? 574  GLU A C   1 
ATOM   4449 O  O   . GLU A 1 574 ? 10.99700  21.56000 3.01200   1.000 119.04179 ? 574  GLU A O   1 
ATOM   4450 C  CB  . GLU A 1 574 ? 14.02200  21.43500 2.03800   1.000 116.54119 ? 574  GLU A CB  1 
ATOM   4451 N  N   . GLU A 1 575 ? 11.30500  19.60200 1.93700   1.000 112.97022 ? 575  GLU A N   1 
ATOM   4452 C  CA  . GLU A 1 575 ? 10.22400  18.92900 2.64700   1.000 121.38117 ? 575  GLU A CA  1 
ATOM   4453 C  C   . GLU A 1 575 ? 10.50900  18.89500 4.14200   1.000 130.57115 ? 575  GLU A C   1 
ATOM   4454 O  O   . GLU A 1 575 ? 11.47300  18.26600 4.58700   1.000 135.07313 ? 575  GLU A O   1 
ATOM   4455 C  CB  . GLU A 1 575 ? 10.04000  17.51300 2.10400   1.000 113.29490 ? 575  GLU A CB  1 
ATOM   4456 C  CG  . GLU A 1 575 ? 8.83600   16.78500 2.68200   1.000 126.44505 ? 575  GLU A CG  1 
ATOM   4457 C  CD  . GLU A 1 575 ? 8.61600   15.42500 2.04900   1.000 132.19033 ? 575  GLU A CD  1 
ATOM   4458 O  OE1 . GLU A 1 575 ? 9.57700   14.87500 1.47400   1.000 127.56652 ? 575  GLU A OE1 1 
ATOM   4459 O  OE2 . GLU A 1 575 ? 7.48100   14.90900 2.12200   1.000 128.01822 ? 575  GLU A OE2 1 
ATOM   4460 N  N   . GLY A 1 576 ? 9.66300   19.57200 4.91600   1.000 130.81035 ? 576  GLY A N   1 
ATOM   4461 C  CA  . GLY A 1 576 ? 9.83100   19.66900 6.35000   1.000 125.11580 ? 576  GLY A CA  1 
ATOM   4462 C  C   . GLY A 1 576 ? 10.39000  20.98400 6.84300   1.000 117.26004 ? 576  GLY A C   1 
ATOM   4463 O  O   . GLY A 1 576 ? 10.50300  21.17000 8.06100   1.000 119.34543 ? 576  GLY A O   1 
ATOM   4464 N  N   . SER A 1 577 ? 10.74100  21.90300 5.94100   1.000 108.96480 ? 577  SER A N   1 
ATOM   4465 C  CA  . SER A 1 577 ? 11.30600  23.18100 6.36000   1.000 109.57988 ? 577  SER A CA  1 
ATOM   4466 C  C   . SER A 1 577 ? 10.23200  24.17300 6.78700   1.000 112.48895 ? 577  SER A C   1 
ATOM   4467 O  O   . SER A 1 577 ? 10.50500  25.06000 7.60300   1.000 117.83335 ? 577  SER A O   1 
ATOM   4468 C  CB  . SER A 1 577 ? 12.14800  23.77800 5.23200   1.000 109.84157 ? 577  SER A CB  1 
ATOM   4469 N  N   . VAL A 1 578 ? 8.99700   23.94800 6.33600   1.000 111.18062 ? 578  VAL A N   1 
ATOM   4470 C  CA  . VAL A 1 578 ? 7.89600   24.90200 6.66300   1.000 111.09343 ? 578  VAL A CA  1 
ATOM   4471 C  C   . VAL A 1 578 ? 7.10600   24.39900 7.87100   1.000 112.72908 ? 578  VAL A C   1 
ATOM   4472 O  O   . VAL A 1 578 ? 6.68500   23.22700 7.86100   1.000 106.72872 ? 578  VAL A O   1 
ATOM   4473 C  CB  . VAL A 1 578 ? 6.97300   25.13800 5.45300   1.000 94.25458  ? 578  VAL A CB  1 
ATOM   4474 N  N   . GLY A 1 579 ? 6.93100   25.26000 8.87400   1.000 112.90172 ? 579  GLY A N   1 
ATOM   4475 C  CA  . GLY A 1 579 ? 6.10300   24.90700 10.03800  1.000 110.27405 ? 579  GLY A CA  1 
ATOM   4476 C  C   . GLY A 1 579 ? 5.10200   26.01100 10.30800  1.000 109.61745 ? 579  GLY A C   1 
ATOM   4477 O  O   . GLY A 1 579 ? 4.18000   25.79400 11.10600  1.000 110.86724 ? 579  GLY A O   1 
ATOM   4478 N  N   . SER A 1 580 ? 5.27500   27.15200 9.64500   1.000 104.74667 ? 580  SER A N   1 
ATOM   4479 C  CA  . SER A 1 580 ? 4.33300   28.28300 9.82400   1.000 99.18328  ? 580  SER A CA  1 
ATOM   4480 C  C   . SER A 1 580 ? 4.50400   29.29100 8.68900   1.000 97.96985  ? 580  SER A C   1 
ATOM   4481 O  O   . SER A 1 580 ? 5.57500   29.29700 8.07300   1.000 100.85517 ? 580  SER A O   1 
ATOM   4482 C  CB  . SER A 1 580 ? 4.52700   28.92700 11.16400  1.000 109.43053 ? 580  SER A CB  1 
ATOM   4483 N  N   . ILE A 1 581 ? 3.47000   30.09600 8.42400   1.000 86.68868  ? 581  ILE A N   1 
ATOM   4484 C  CA  . ILE A 1 581 ? 3.54700   31.05300 7.32600   1.000 92.94665  ? 581  ILE A CA  1 
ATOM   4485 C  C   . ILE A 1 581 ? 2.86200   32.34700 7.74400   1.000 98.99410  ? 581  ILE A C   1 
ATOM   4486 O  O   . ILE A 1 581 ? 1.70100   32.33200 8.17000   1.000 96.37525  ? 581  ILE A O   1 
ATOM   4487 C  CB  . ILE A 1 581 ? 2.91000   30.49600 6.03900   1.000 81.38109  ? 581  ILE A CB  1 
ATOM   4488 N  N   . THR A 1 582 ? 3.57300   33.46300 7.60800   1.000 104.17264 ? 582  THR A N   1 
ATOM   4489 C  CA  . THR A 1 582 ? 3.03500   34.78700 7.90600   1.000 95.24921  ? 582  THR A CA  1 
ATOM   4490 C  C   . THR A 1 582 ? 3.01800   35.60900 6.62600   1.000 99.22676  ? 582  THR A C   1 
ATOM   4491 O  O   . THR A 1 582 ? 4.05600   35.76900 5.97800   1.000 103.97135 ? 582  THR A O   1 
ATOM   4492 C  CB  . THR A 1 582 ? 3.86500   35.49000 8.98300   1.000 93.70758  ? 582  THR A CB  1 
ATOM   4493 O  OG1 . THR A 1 582 ? 3.57700   34.91500 10.26400  1.000 99.28148  ? 582  THR A OG1 1 
ATOM   4494 C  CG2 . THR A 1 582 ? 3.55700   36.98100 9.01300   1.000 88.08801  ? 582  THR A CG2 1 
ATOM   4495 N  N   . ILE A 1 583 ? 1.84800   36.12900 6.26300   1.000 95.76633  ? 583  ILE A N   1 
ATOM   4496 C  CA  . ILE A 1 583 ? 1.68400   36.93800 5.06100   1.000 99.61602  ? 583  ILE A CA  1 
ATOM   4497 C  C   . ILE A 1 583 ? 1.66600   38.40500 5.46500   1.000 107.95083 ? 583  ILE A C   1 
ATOM   4498 O  O   . ILE A 1 583 ? 0.95400   38.78900 6.40200   1.000 104.95521 ? 583  ILE A O   1 
ATOM   4499 C  CB  . ILE A 1 583 ? 0.39800   36.55600 4.30800   1.000 89.82135  ? 583  ILE A CB  1 
ATOM   4500 C  CG1 . ILE A 1 583 ? 0.45200   35.09000 3.87200   1.000 87.18678  ? 583  ILE A CG1 1 
ATOM   4501 C  CG2 . ILE A 1 583 ? 0.18500   37.46700 3.10800   1.000 95.65170  ? 583  ILE A CG2 1 
ATOM   4502 C  CD1 . ILE A 1 583 ? 1.43400   34.82000 2.76000   1.000 93.45803  ? 583  ILE A CD1 1 
ATOM   4503 N  N   . SER A 1 584 ? 2.44700   39.22900 4.76700   1.000 112.19481 ? 584  SER A N   1 
ATOM   4504 C  CA  . SER A 1 584 ? 2.52400   40.64800 5.07700   1.000 113.06268 ? 584  SER A CA  1 
ATOM   4505 C  C   . SER A 1 584 ? 2.57800   41.45200 3.78600   1.000 117.05374 ? 584  SER A C   1 
ATOM   4506 O  O   . SER A 1 584 ? 2.84500   40.91700 2.70600   1.000 115.27553 ? 584  SER A O   1 
ATOM   4507 C  CB  . SER A 1 584 ? 3.74200   40.96700 5.95400   1.000 97.28214  ? 584  SER A CB  1 
ATOM   4508 N  N   . LYS A 1 585 ? 2.31600   42.75200 3.91700   1.000 120.11219 ? 585  LYS A N   1 
ATOM   4509 C  CA  . LYS A 1 585 ? 2.34800   43.68900 2.79500   1.000 106.72921 ? 585  LYS A CA  1 
ATOM   4510 C  C   . LYS A 1 585 ? 1.41700   43.25600 1.66700   1.000 100.89356 ? 585  LYS A C   1 
ATOM   4511 O  O   . LYS A 1 585 ? 0.42200   43.92300 1.38300   1.000 94.29576  ? 585  LYS A O   1 
ATOM   4512 C  CB  . LYS A 1 585 ? 3.77600   43.84800 2.26500   1.000 97.62188  ? 585  LYS A CB  1 
HETATM 4513 C  C1  . NAG B 2 .   ? -25.29000 37.81900 60.83300  1.000 80.91889  ? 701  NAG A C1  1 
HETATM 4514 C  C2  . NAG B 2 .   ? -26.32500 38.59200 61.65200  1.000 78.51416  ? 701  NAG A C2  1 
HETATM 4515 C  C3  . NAG B 2 .   ? -25.74200 39.92500 62.11200  1.000 79.55834  ? 701  NAG A C3  1 
HETATM 4516 C  C4  . NAG B 2 .   ? -24.43400 39.70300 62.85700  1.000 77.12627  ? 701  NAG A C4  1 
HETATM 4517 C  C5  . NAG B 2 .   ? -23.46900 38.89100 61.99700  1.000 77.29158  ? 701  NAG A C5  1 
HETATM 4518 C  C6  . NAG B 2 .   ? -22.19300 38.53200 62.72100  1.000 66.01889  ? 701  NAG A C6  1 
HETATM 4519 C  C7  . NAG B 2 .   ? -28.60100 37.98800 60.96000  1.000 81.41006  ? 701  NAG A C7  1 
HETATM 4520 C  C8  . NAG B 2 .   ? -29.77600 38.35900 60.10600  1.000 69.31030  ? 701  NAG A C8  1 
HETATM 4521 N  N2  . NAG B 2 .   ? -27.54400 38.80400 60.89000  1.000 76.90838  ? 701  NAG A N2  1 
HETATM 4522 O  O3  . NAG B 2 .   ? -26.68000 40.58600 62.95500  1.000 87.57703  ? 701  NAG A O3  1 
HETATM 4523 O  O4  . NAG B 2 .   ? -23.83800 40.95500 63.17700  1.000 92.61902  ? 701  NAG A O4  1 
HETATM 4524 O  O5  . NAG B 2 .   ? -24.08500 37.65400 61.60500  1.000 76.17197  ? 701  NAG A O5  1 
HETATM 4525 O  O6  . NAG B 2 .   ? -22.44700 37.67800 63.82800  1.000 56.12386  ? 701  NAG A O6  1 
HETATM 4526 O  O7  . NAG B 2 .   ? -28.60800 36.99300 61.67700  1.000 76.04993  ? 701  NAG A O7  1 
HETATM 4527 C  C1  . NAG C 2 .   ? -25.77800 44.82200 -2.08800  1.000 47.61198  ? 702  NAG A C1  1 
HETATM 4528 C  C2  . NAG C 2 .   ? -26.36200 45.81100 -3.10300  1.000 47.81524  ? 702  NAG A C2  1 
HETATM 4529 C  C3  . NAG C 2 .   ? -25.32600 46.86800 -3.47700  1.000 50.45210  ? 702  NAG A C3  1 
HETATM 4530 C  C4  . NAG C 2 .   ? -24.76500 47.52900 -2.22600  1.000 56.64986  ? 702  NAG A C4  1 
HETATM 4531 C  C5  . NAG C 2 .   ? -24.23100 46.46500 -1.27300  1.000 53.07161  ? 702  NAG A C5  1 
HETATM 4532 C  C6  . NAG C 2 .   ? -23.72800 47.03000 0.03600   1.000 49.43952  ? 702  NAG A C6  1 
HETATM 4533 C  C7  . NAG C 2 .   ? -28.09200 44.67400 -4.43000  1.000 50.53536  ? 702  NAG A C7  1 
HETATM 4534 C  C8  . NAG C 2 .   ? -28.40400 43.98400 -5.72300  1.000 53.45843  ? 702  NAG A C8  1 
HETATM 4535 N  N2  . NAG C 2 .   ? -26.83800 45.11900 -4.29100  1.000 47.04188  ? 702  NAG A N2  1 
HETATM 4536 O  O3  . NAG C 2 .   ? -25.93200 47.84500 -4.31500  1.000 63.82767  ? 702  NAG A O3  1 
HETATM 4537 O  O4  . NAG C 2 .   ? -23.71200 48.42000 -2.57500  1.000 64.61281  ? 702  NAG A O4  1 
HETATM 4538 O  O5  . NAG C 2 .   ? -25.27600 45.53600 -0.95300  1.000 52.56751  ? 702  NAG A O5  1 
HETATM 4539 O  O6  . NAG C 2 .   ? -24.79200 47.52600 0.83700   1.000 72.20919  ? 702  NAG A O6  1 
HETATM 4540 O  O7  . NAG C 2 .   ? -28.93700 44.82300 -3.55200  1.000 58.02827  ? 702  NAG A O7  1 
HETATM 4541 C  C   . TRS D 3 .   ? -21.62900 38.95300 28.56400  0.869 61.79445  ? 703  TRS A C   1 
HETATM 4542 C  C1  . TRS D 3 .   ? -22.01300 39.53800 29.91700  0.869 52.48504  ? 703  TRS A C1  1 
HETATM 4543 C  C2  . TRS D 3 .   ? -21.15000 37.51200 28.71500  0.869 57.19468  ? 703  TRS A C2  1 
HETATM 4544 C  C3  . TRS D 3 .   ? -20.53900 39.80800 27.92800  0.869 54.39142  ? 703  TRS A C3  1 
HETATM 4545 N  N   . TRS D 3 .   ? -22.83900 38.95600 27.67300  0.869 42.31244  ? 703  TRS A N   1 
HETATM 4546 O  O1  . TRS D 3 .   ? -20.88900 39.62600 30.77600  0.869 58.26431  ? 703  TRS A O1  1 
HETATM 4547 O  O2  . TRS D 3 .   ? -19.82500 37.44400 29.21400  0.869 51.79568  ? 703  TRS A O2  1 
HETATM 4548 O  O3  . TRS D 3 .   ? -19.40400 39.91000 28.77000  0.869 57.84563  ? 703  TRS A O3  1 
HETATM 4549 C  C1  . MPD E 4 .   ? -25.74000 42.11500 26.31800  1.000 56.44953  ? 704  MPD A C1  1 
HETATM 4550 C  C2  . MPD E 4 .   ? -26.26600 40.69900 26.17300  1.000 51.65685  ? 704  MPD A C2  1 
HETATM 4551 O  O2  . MPD E 4 .   ? -25.35700 40.00200 25.31200  1.000 50.16267  ? 704  MPD A O2  1 
HETATM 4552 C  CM  . MPD E 4 .   ? -27.63600 40.69700 25.51900  1.000 48.08804  ? 704  MPD A CM  1 
HETATM 4553 C  C3  . MPD E 4 .   ? -26.28000 39.96300 27.51500  1.000 48.71962  ? 704  MPD A C3  1 
HETATM 4554 C  C4  . MPD E 4 .   ? -27.05100 40.69300 28.57700  1.000 54.28140  ? 704  MPD A C4  1 
HETATM 4555 O  O4  . MPD E 4 .   ? -28.40900 40.28100 28.54300  1.000 42.57546  ? 704  MPD A O4  1 
HETATM 4556 C  C5  . MPD E 4 .   ? -26.50100 40.47600 29.95400  1.000 50.91162  ? 704  MPD A C5  1 
HETATM 4557 C  C1  . MPD F 4 .   ? -27.09400 3.95500  26.81300  1.000 64.74179  ? 705  MPD A C1  1 
HETATM 4558 C  C2  . MPD F 4 .   ? -27.37900 5.40900  27.14500  1.000 69.40970  ? 705  MPD A C2  1 
HETATM 4559 O  O2  . MPD F 4 .   ? -28.14500 5.43000  28.35700  1.000 81.82678  ? 705  MPD A O2  1 
HETATM 4560 C  CM  . MPD F 4 .   ? -28.22100 6.06000  26.06200  1.000 63.66594  ? 705  MPD A CM  1 
HETATM 4561 C  C3  . MPD F 4 .   ? -26.08400 6.18600  27.39100  1.000 53.72762  ? 705  MPD A C3  1 
HETATM 4562 C  C4  . MPD F 4 .   ? -25.07500 5.86900  26.32800  1.000 60.21130  ? 705  MPD A C4  1 
HETATM 4563 O  O4  . MPD F 4 .   ? -25.27100 6.74500  25.22700  1.000 77.60779  ? 705  MPD A O4  1 
HETATM 4564 C  C5  . MPD F 4 .   ? -23.66000 5.98200  26.80300  1.000 54.70045  ? 705  MPD A C5  1 
HETATM 4565 C  C1  . NAG G 2 .   ? -9.47800  39.33700 5.96600   1.000 115.42401 ? 706  NAG A C1  1 
HETATM 4566 C  C2  . NAG G 2 .   ? -8.32100  40.11300 6.58100   1.000 112.02408 ? 706  NAG A C2  1 
HETATM 4567 C  C3  . NAG G 2 .   ? -8.71200  41.58400 6.56300   1.000 110.16081 ? 706  NAG A C3  1 
HETATM 4568 C  C4  . NAG G 2 .   ? -9.14000  41.96400 5.15200   1.000 119.76514 ? 706  NAG A C4  1 
HETATM 4569 C  C5  . NAG G 2 .   ? -10.27800 41.06800 4.67400   1.000 119.67700 ? 706  NAG A C5  1 
HETATM 4570 C  C6  . NAG G 2 .   ? -10.79700 41.45200 3.29300   1.000 103.91061 ? 706  NAG A C6  1 
HETATM 4571 C  C7  . NAG G 2 .   ? -7.39000  40.21300 8.87700   1.000 101.73846 ? 706  NAG A C7  1 
HETATM 4572 C  C8  . NAG G 2 .   ? -8.23700  40.89600 9.90500   1.000 93.60966  ? 706  NAG A C8  1 
HETATM 4573 N  N2  . NAG G 2 .   ? -8.05100  39.58700 7.90900   1.000 107.75056 ? 706  NAG A N2  1 
HETATM 4574 O  O3  . NAG G 2 .   ? -7.62200  42.41900 6.95700   1.000 109.37252 ? 706  NAG A O3  1 
HETATM 4575 O  O4  . NAG G 2 .   ? -9.55700  43.33000 5.13900   1.000 131.98198 ? 706  NAG A O4  1 
HETATM 4576 O  O5  . NAG G 2 .   ? -9.79100  39.73200 4.64000   1.000 124.07738 ? 706  NAG A O5  1 
HETATM 4577 O  O6  . NAG G 2 .   ? -11.48200 42.70800 3.35900   1.000 97.37338  ? 706  NAG A O6  1 
HETATM 4578 O  O7  . NAG G 2 .   ? -6.17300  40.21400 8.94300   1.000 99.17968  ? 706  NAG A O7  1 
HETATM 4579 NA NA  . NA  H 5 .   ? -6.06300  18.01800 21.38000  1.000 46.89905  ? 707  NA  A NA  1 
HETATM 4580 N  N1  . AZI I 6 .   ? -35.63000 18.22300 8.93600   1.000 67.61051  ? 708  AZI A N1  1 
HETATM 4581 N  N2  . AZI I 6 .   ? -34.79400 18.85500 8.43000   1.000 75.71768  ? 708  AZI A N2  1 
HETATM 4582 N  N3  . AZI I 6 .   ? -33.95700 19.48600 7.92300   1.000 56.34559  ? 708  AZI A N3  1 
HETATM 4583 N  N1  . AZI J 6 .   ? -37.14600 45.71100 22.76600  1.000 69.00770  ? 709  AZI A N1  1 
HETATM 4584 N  N2  . AZI J 6 .   ? -36.60400 44.71700 22.49900  1.000 76.62067  ? 709  AZI A N2  1 
HETATM 4585 N  N3  . AZI J 6 .   ? -36.06000 43.72400 22.23200  1.000 53.11011  ? 709  AZI A N3  1 
HETATM 4586 C  C   . ACT K 7 .   ? -28.23000 45.17400 3.92900   1.000 69.79384  ? 710  ACT A C   1 
HETATM 4587 O  O   . ACT K 7 .   ? -29.43000 45.04500 4.20500   1.000 60.95713  ? 710  ACT A O   1 
HETATM 4588 O  OXT . ACT K 7 .   ? -27.78600 45.17600 2.78000   1.000 58.37104  ? 710  ACT A OXT 1 
HETATM 4589 C  CH3 . ACT K 7 .   ? -27.24100 45.34300 5.07900   1.000 64.05568  ? 710  ACT A CH3 1 
HETATM 4590 N  N1  . AZI L 6 .   ? -20.10300 45.15400 45.59700  1.000 62.21770  ? 711  AZI A N1  1 
HETATM 4591 N  N2  . AZI L 6 .   ? -19.18200 45.38600 44.92800  1.000 72.51308  ? 711  AZI A N2  1 
HETATM 4592 N  N3  . AZI L 6 .   ? -18.26100 45.61700 44.25700  1.000 64.65813  ? 711  AZI A N3  1 
HETATM 4593 N  N1  . AZI M 6 .   ? -26.92600 44.22800 32.64100  1.000 65.34924  ? 712  AZI A N1  1 
HETATM 4594 N  N2  . AZI M 6 .   ? -25.79900 44.18000 32.51800  1.000 71.66060  ? 712  AZI A N2  1 
HETATM 4595 N  N3  . AZI M 6 .   ? -24.67200 44.13500 32.41500  1.000 56.48182  ? 712  AZI A N3  1 
HETATM 4596 N  N1  . AZI N 6 .   ? 0.82500   19.70600 31.56400  1.000 63.94292  ? 713  AZI A N1  1 
HETATM 4597 N  N2  . AZI N 6 .   ? 0.21600   20.17200 32.39600  1.000 80.06765  ? 713  AZI A N2  1 
HETATM 4598 N  N3  . AZI N 6 .   ? -0.37500  20.64500 33.23800  1.000 75.36093  ? 713  AZI A N3  1 
HETATM 4599 C  C   . ACT O 7 .   ? -45.78300 29.55000 12.41500  1.000 76.24783  ? 714  ACT A C   1 
HETATM 4600 O  O   . ACT O 7 .   ? -45.89400 29.97300 11.25300  1.000 84.76082  ? 714  ACT A O   1 
HETATM 4601 O  OXT . ACT O 7 .   ? -45.03100 28.61600 12.74200  1.000 67.24472  ? 714  ACT A OXT 1 
HETATM 4602 C  CH3 . ACT O 7 .   ? -46.62100 30.22100 13.50400  1.000 48.63582  ? 714  ACT A CH3 1 
HETATM 4603 O  O   . HOH P 8 .   ? -6.80700  21.06800 27.87100  1.000 43.66405  ? 801  HOH A O   1 
HETATM 4604 O  O   . HOH P 8 .   ? -19.26400 36.89600 25.21700  1.000 55.13479  ? 802  HOH A O   1 
HETATM 4605 O  O   . HOH P 8 .   ? -25.84400 29.76700 39.03400  1.000 44.51689  ? 803  HOH A O   1 
HETATM 4606 O  O   . HOH P 8 .   ? -14.00700 15.35200 20.92000  1.000 45.36923  ? 804  HOH A O   1 
HETATM 4607 O  O   . HOH P 8 .   ? -20.46100 32.00700 34.33200  1.000 46.85137  ? 805  HOH A O   1 
HETATM 4608 O  O   . HOH P 8 .   ? -31.29900 50.61100 35.19000  1.000 49.84153  ? 806  HOH A O   1 
HETATM 4609 O  O   . HOH P 8 .   ? -19.09900 41.34900 39.18500  1.000 49.42718  ? 807  HOH A O   1 
HETATM 4610 O  O   . HOH P 8 .   ? -6.97400  28.88600 33.43500  1.000 47.63878  ? 808  HOH A O   1 
HETATM 4611 O  O   . HOH P 8 .   ? -23.83700 14.53200 43.23300  1.000 50.85842  ? 809  HOH A O   1 
HETATM 4612 O  O   . HOH P 8 .   ? -42.49200 40.38000 21.64200  1.000 43.68988  ? 810  HOH A O   1 
HETATM 4613 O  O   . HOH P 8 .   ? -21.72500 13.00300 21.30300  1.000 37.42144  ? 811  HOH A O   1 
HETATM 4614 O  O   . HOH P 8 .   ? -26.59000 12.07800 22.71500  1.000 55.61135  ? 812  HOH A O   1 
HETATM 4615 O  O   . HOH P 8 .   ? -20.51700 4.15300  29.83400  1.000 58.73854  ? 813  HOH A O   1 
HETATM 4616 O  O   . HOH P 8 .   ? -35.57500 19.30800 0.41100   1.000 50.84250  ? 814  HOH A O   1 
HETATM 4617 O  O   . HOH P 8 .   ? -18.68900 29.17900 52.96500  1.000 54.56883  ? 815  HOH A O   1 
HETATM 4618 O  O   . HOH P 8 .   ? -21.15200 30.49300 46.76600  1.000 50.93612  ? 816  HOH A O   1 
HETATM 4619 O  O   . HOH P 8 .   ? -18.79600 16.47600 2.78500   1.000 38.00793  ? 817  HOH A O   1 
HETATM 4620 O  O   . HOH P 8 .   ? -42.33400 41.82400 36.39400  1.000 56.85307  ? 818  HOH A O   1 
HETATM 4621 O  O   . HOH P 8 .   ? -17.81600 25.14100 9.33400   1.000 34.99362  ? 819  HOH A O   1 
HETATM 4622 O  O   . HOH P 8 .   ? -22.69000 20.02700 -9.91400  1.000 53.34763  ? 820  HOH A O   1 
HETATM 4623 O  O   . HOH P 8 .   ? -36.62000 32.66500 27.94300  1.000 36.68024  ? 821  HOH A O   1 
HETATM 4624 O  O   . HOH P 8 .   ? -33.60500 19.09700 12.89300  1.000 39.50370  ? 822  HOH A O   1 
HETATM 4625 O  O   . HOH P 8 .   ? -36.57900 37.18000 31.10100  1.000 44.26457  ? 823  HOH A O   1 
HETATM 4626 O  O   . HOH P 8 .   ? -11.77300 26.93100 18.79600  1.000 39.18339  ? 824  HOH A O   1 
HETATM 4627 O  O   . HOH P 8 .   ? -16.32500 30.73700 29.25100  1.000 45.76859  ? 825  HOH A O   1 
HETATM 4628 O  O   . HOH P 8 .   ? -46.73200 30.82400 20.31700  1.000 48.18800  ? 826  HOH A O   1 
HETATM 4629 O  O   . HOH P 8 .   ? -14.40900 4.76700  36.68200  1.000 52.76508  ? 827  HOH A O   1 
HETATM 4630 O  O   . HOH P 8 .   ? -44.63300 39.30400 37.86900  1.000 42.70847  ? 828  HOH A O   1 
HETATM 4631 O  O   . HOH P 8 .   ? -9.41100  35.04800 13.48700  1.000 50.63977  ? 829  HOH A O   1 
HETATM 4632 O  O   . HOH P 8 .   ? -18.47200 34.23300 46.36600  1.000 55.95487  ? 830  HOH A O   1 
HETATM 4633 O  O   . HOH P 8 .   ? -46.39700 38.30300 27.45700  1.000 47.53050  ? 831  HOH A O   1 
HETATM 4634 O  O   . HOH P 8 .   ? -6.96600  30.09900 3.65900   1.000 50.78093  ? 832  HOH A O   1 
HETATM 4635 O  O   . HOH P 8 .   ? -15.39200 9.27500  23.72800  1.000 46.83996  ? 833  HOH A O   1 
HETATM 4636 O  O   . HOH P 8 .   ? -9.08900  24.54800 -3.76900  1.000 51.30500  ? 834  HOH A O   1 
HETATM 4637 O  O   . HOH P 8 .   ? -15.06800 13.07900 23.74500  1.000 48.16399  ? 835  HOH A O   1 
HETATM 4638 O  O   . HOH P 8 .   ? -10.77000 19.19100 17.36600  1.000 38.61318  ? 836  HOH A O   1 
HETATM 4639 O  O   . HOH P 8 .   ? -33.48100 38.53200 -15.02100 1.000 46.28503  ? 837  HOH A O   1 
HETATM 4640 O  O   . HOH P 8 .   ? -38.89600 44.15000 26.93000  1.000 47.48134  ? 838  HOH A O   1 
HETATM 4641 O  O   . HOH P 8 .   ? -24.61900 37.39200 28.66200  1.000 46.16568  ? 839  HOH A O   1 
HETATM 4642 O  O   . HOH P 8 .   ? -8.26200  27.12600 4.99900   1.000 55.02354  ? 840  HOH A O   1 
HETATM 4643 O  O   . HOH P 8 .   ? -24.60200 38.27700 15.26500  1.000 33.08205  ? 841  HOH A O   1 
HETATM 4644 O  O   . HOH P 8 .   ? -39.19400 27.55100 41.02500  1.000 45.10076  ? 842  HOH A O   1 
HETATM 4645 O  O   . HOH P 8 .   ? -8.33600  18.68200 19.57300  1.000 38.05190  ? 843  HOH A O   1 
HETATM 4646 O  O   . HOH P 8 .   ? -44.88500 25.30300 24.76700  1.000 43.59826  ? 844  HOH A O   1 
HETATM 4647 O  O   . HOH P 8 .   ? -19.28500 46.01100 40.63900  1.000 51.41481  ? 845  HOH A O   1 
HETATM 4648 O  O   . HOH P 8 .   ? -31.88900 38.06200 -0.06200  1.000 50.27795  ? 846  HOH A O   1 
HETATM 4649 O  O   . HOH P 8 .   ? -22.51800 29.42100 44.39500  1.000 37.25760  ? 847  HOH A O   1 
HETATM 4650 O  O   . HOH P 8 .   ? -10.42600 24.53400 19.77800  1.000 46.23652  ? 848  HOH A O   1 
HETATM 4651 O  O   . HOH P 8 .   ? -29.77100 18.80800 -2.31400  1.000 37.47073  ? 849  HOH A O   1 
HETATM 4652 O  O   . HOH P 8 .   ? -35.88200 38.77000 33.13800  1.000 46.68175  ? 850  HOH A O   1 
HETATM 4653 O  O   . HOH P 8 .   ? -41.37500 16.25300 17.41900  1.000 52.68302  ? 851  HOH A O   1 
HETATM 4654 O  O   . HOH P 8 .   ? -8.14600  35.70300 37.60100  1.000 57.81408  ? 852  HOH A O   1 
HETATM 4655 O  O   . HOH P 8 .   ? -33.38200 27.13700 51.17200  1.000 54.85894  ? 853  HOH A O   1 
HETATM 4656 O  O   . HOH P 8 .   ? -21.73500 5.58100  22.57200  1.000 46.00484  ? 854  HOH A O   1 
HETATM 4657 O  O   . HOH P 8 .   ? -39.20600 36.09300 9.83400   1.000 50.59897  ? 855  HOH A O   1 
HETATM 4658 O  O   . HOH P 8 .   ? -22.34900 27.64700 0.33900   1.000 38.09086  ? 856  HOH A O   1 
HETATM 4659 O  O   . HOH P 8 .   ? -38.50100 38.26500 13.17400  1.000 30.04858  ? 857  HOH A O   1 
HETATM 4660 O  O   . HOH P 8 .   ? -35.10100 49.22000 46.38400  1.000 50.31248  ? 858  HOH A O   1 
HETATM 4661 O  O   . HOH P 8 .   ? -13.26900 11.45200 25.96800  1.000 44.13957  ? 859  HOH A O   1 
HETATM 4662 O  O   . HOH P 8 .   ? -15.44200 28.57900 2.99100   1.000 41.13832  ? 860  HOH A O   1 
HETATM 4663 O  O   . HOH P 8 .   ? -29.49600 42.83900 27.96100  1.000 49.09832  ? 861  HOH A O   1 
HETATM 4664 O  O   . HOH P 8 .   ? -30.93000 41.06400 1.02500   1.000 39.12410  ? 862  HOH A O   1 
HETATM 4665 O  O   . HOH P 8 .   ? -26.00800 27.16400 1.28600   1.000 44.03370  ? 863  HOH A O   1 
HETATM 4666 O  O   . HOH P 8 .   ? -33.23800 37.79800 -3.81600  1.000 41.54158  ? 864  HOH A O   1 
HETATM 4667 O  O   . HOH P 8 .   ? -24.85700 40.82200 17.95600  1.000 50.18852  ? 865  HOH A O   1 
HETATM 4668 O  O   . HOH P 8 .   ? -30.80700 28.83900 36.18600  1.000 38.35983  ? 866  HOH A O   1 
HETATM 4669 O  O   . HOH P 8 .   ? -31.92700 42.73600 33.85500  1.000 44.03778  ? 867  HOH A O   1 
HETATM 4670 O  O   . HOH P 8 .   ? -31.80800 11.23200 29.07500  1.000 56.40017  ? 868  HOH A O   1 
HETATM 4671 O  O   . HOH P 8 .   ? -2.70800  11.26400 30.01000  1.000 55.73163  ? 869  HOH A O   1 
HETATM 4672 O  O   . HOH P 8 .   ? -11.55000 11.49200 24.46300  1.000 40.08012  ? 870  HOH A O   1 
HETATM 4673 O  O   . HOH P 8 .   ? -14.83700 37.69600 40.50900  1.000 41.40514  ? 871  HOH A O   1 
HETATM 4674 O  O   . HOH P 8 .   ? -17.99000 38.37800 6.45500   1.000 49.48232  ? 872  HOH A O   1 
HETATM 4675 O  O   . HOH P 8 .   ? -19.51300 23.02200 47.95400  1.000 43.81644  ? 873  HOH A O   1 
HETATM 4676 O  O   . HOH P 8 .   ? -33.37600 29.72500 36.48500  1.000 35.53399  ? 874  HOH A O   1 
HETATM 4677 O  O   . HOH P 8 .   ? -21.20000 48.55500 43.81700  1.000 47.47014  ? 875  HOH A O   1 
HETATM 4678 O  O   . HOH P 8 .   ? -40.64200 18.86600 13.68900  1.000 46.75397  ? 876  HOH A O   1 
HETATM 4679 O  O   . HOH P 8 .   ? -33.03600 35.85900 22.67200  1.000 33.87463  ? 877  HOH A O   1 
HETATM 4680 O  O   . HOH P 8 .   ? -8.54600  21.17300 14.44800  1.000 48.56852  ? 878  HOH A O   1 
HETATM 4681 O  O   . HOH P 8 .   ? -33.61200 52.16700 41.40900  1.000 48.26167  ? 879  HOH A O   1 
HETATM 4682 O  O   . HOH P 8 .   ? -19.31300 39.29700 0.98500   1.000 45.20473  ? 880  HOH A O   1 
HETATM 4683 O  O   . HOH P 8 .   ? -16.07800 7.48800  39.50700  1.000 52.12967  ? 881  HOH A O   1 
HETATM 4684 O  O   . HOH P 8 .   ? -14.47000 19.97400 23.55600  1.000 37.78686  ? 882  HOH A O   1 
HETATM 4685 O  O   . HOH P 8 .   ? -38.22200 44.94600 29.76700  1.000 43.85283  ? 883  HOH A O   1 
HETATM 4686 O  O   . HOH P 8 .   ? -18.77300 28.81100 25.48700  1.000 42.55875  ? 884  HOH A O   1 
HETATM 4687 O  O   . HOH P 8 .   ? -25.60600 16.84800 -7.96600  1.000 46.58132  ? 885  HOH A O   1 
HETATM 4688 O  O   . HOH P 8 .   ? -39.69000 41.12500 16.14400  1.000 45.54963  ? 886  HOH A O   1 
HETATM 4689 O  O   . HOH P 8 .   ? -23.45700 33.92200 25.83200  1.000 36.86321  ? 887  HOH A O   1 
HETATM 4690 O  O   . HOH P 8 .   ? -29.06500 11.93300 20.46400  1.000 44.45701  ? 888  HOH A O   1 
HETATM 4691 O  O   . HOH P 8 .   ? -26.46700 35.83800 29.75100  1.000 40.04858  ? 889  HOH A O   1 
HETATM 4692 O  O   . HOH P 8 .   ? -34.98000 35.48900 -17.97300 1.000 50.90431  ? 890  HOH A O   1 
HETATM 4693 O  O   . HOH P 8 .   ? -29.09600 49.09800 35.25200  1.000 52.05748  ? 891  HOH A O   1 
HETATM 4694 O  O   . HOH P 8 .   ? -33.84100 43.37800 26.94000  1.000 61.96870  ? 892  HOH A O   1 
HETATM 4695 O  O   . HOH P 8 .   ? -10.64900 37.40600 11.29800  1.000 48.37721  ? 893  HOH A O   1 
HETATM 4696 O  O   . HOH P 8 .   ? -19.33200 26.55600 34.01200  1.000 47.71501  ? 894  HOH A O   1 
HETATM 4697 O  O   . HOH P 8 .   ? -19.44000 29.45800 33.21100  1.000 39.20424  ? 895  HOH A O   1 
HETATM 4698 O  O   . HOH P 8 .   ? -16.89600 14.33500 0.65800   1.000 52.28607  ? 896  HOH A O   1 
HETATM 4699 O  O   . HOH P 8 .   ? -39.43600 15.20200 36.30200  1.000 52.24274  ? 897  HOH A O   1 
HETATM 4700 O  O   . HOH P 8 .   ? -9.11600  8.03600  35.13900  1.000 43.82051  ? 898  HOH A O   1 
HETATM 4701 O  O   . HOH P 8 .   ? -31.15300 27.73600 -5.05000  1.000 33.36811  ? 899  HOH A O   1 
HETATM 4702 O  O   . HOH P 8 .   ? -21.54400 36.91600 43.04400  1.000 47.41709  ? 900  HOH A O   1 
HETATM 4703 O  O   . HOH P 8 .   ? -26.90400 39.26900 18.87800  1.000 42.53273  ? 901  HOH A O   1 
HETATM 4704 O  O   . HOH P 8 .   ? -39.74000 25.35300 13.28400  1.000 46.22573  ? 902  HOH A O   1 
HETATM 4705 O  O   . HOH P 8 .   ? -34.99700 25.65500 -11.24800 1.000 62.94612  ? 903  HOH A O   1 
HETATM 4706 O  O   . HOH P 8 .   ? -30.29000 19.76100 0.15500   1.000 41.71282  ? 904  HOH A O   1 
HETATM 4707 O  O   . HOH P 8 .   ? -45.39100 33.68900 30.67400  1.000 44.93304  ? 905  HOH A O   1 
HETATM 4708 O  O   . HOH P 8 .   ? -4.75700  29.02000 29.25200  1.000 56.63008  ? 906  HOH A O   1 
HETATM 4709 O  O   . HOH P 8 .   ? -11.35800 22.88300 17.71600  1.000 40.36859  ? 907  HOH A O   1 
HETATM 4710 O  O   . HOH P 8 .   ? -22.84400 37.54800 46.42700  1.000 42.30453  ? 908  HOH A O   1 
HETATM 4711 O  O   . HOH P 8 .   ? -22.29800 35.37400 62.11800  1.000 51.66610  ? 909  HOH A O   1 
HETATM 4712 O  O   . HOH P 8 .   ? -42.83700 43.12600 32.12900  1.000 59.04412  ? 910  HOH A O   1 
HETATM 4713 O  O   . HOH P 8 .   ? -33.44200 25.93900 30.13400  1.000 42.45249  ? 911  HOH A O   1 
HETATM 4714 O  O   . HOH P 8 .   ? -13.68100 13.00300 15.48200  1.000 53.40220  ? 912  HOH A O   1 
HETATM 4715 O  O   . HOH P 8 .   ? -7.08600  21.32500 18.88800  1.000 46.38751  ? 913  HOH A O   1 
HETATM 4716 O  O   . HOH P 8 .   ? -7.416    7.242    39.791    1.000 54.91660  ? 914  HOH A O   1 
HETATM 4717 O  O   . HOH P 8 .   ? -21.83400 38.71500 13.15300  1.000 48.22018  ? 915  HOH A O   1 
HETATM 4718 O  O   . HOH P 8 .   ? -26.59400 35.89600 -17.37800 1.000 49.84963  ? 916  HOH A O   1 
HETATM 4719 O  O   . HOH P 8 .   ? -32.00500 40.97600 -5.55300  1.000 50.13175  ? 917  HOH A O   1 
HETATM 4720 O  O   . HOH P 8 .   ? -31.74700 19.08800 5.52300   1.000 53.40960  ? 918  HOH A O   1 
HETATM 4721 O  O   . HOH P 8 .   ? -49.61300 32.09600 26.56700  1.000 59.63033  ? 919  HOH A O   1 
HETATM 4722 O  O   . HOH P 8 .   ? -18.74100 24.22400 6.14100   1.000 38.15470  ? 920  HOH A O   1 
HETATM 4723 O  O   . HOH P 8 .   ? -18.26800 27.85500 -22.33500 1.000 61.13652  ? 921  HOH A O   1 
HETATM 4724 O  O   . HOH P 8 .   ? -44.26300 40.56300 24.08200  1.000 42.68062  ? 922  HOH A O   1 
HETATM 4725 O  O   . HOH P 8 .   ? -36.85800 30.45700 4.47100   1.000 35.79036  ? 923  HOH A O   1 
HETATM 4726 O  O   . HOH P 8 .   ? -13.32700 40.52100 39.43100  1.000 44.08159  ? 924  HOH A O   1 
HETATM 4727 O  O   . HOH P 8 .   ? -8.60800  22.91300 27.94800  1.000 47.69719  ? 925  HOH A O   1 
HETATM 4728 O  O   . HOH P 8 .   ? -29.86500 8.39800  30.00900  1.000 54.16702  ? 926  HOH A O   1 
HETATM 4729 O  O   . HOH P 8 .   ? -24.24200 22.05100 50.61100  1.000 51.13265  ? 927  HOH A O   1 
HETATM 4730 O  O   . HOH P 8 .   ? -30.39600 41.64500 -7.40700  1.000 43.22803  ? 928  HOH A O   1 
HETATM 4731 O  O   . HOH P 8 .   ? -35.90300 41.83700 12.53400  1.000 47.29959  ? 929  HOH A O   1 
HETATM 4732 O  O   . HOH P 8 .   ? -52.38500 23.43800 26.73000  1.000 52.23718  ? 930  HOH A O   1 
HETATM 4733 O  O   . HOH P 8 .   ? -22.53900 17.48800 2.13900   1.000 35.57657  ? 931  HOH A O   1 
HETATM 4734 O  O   . HOH P 8 .   ? -20.28200 12.99300 6.24700   1.000 43.19283  ? 932  HOH A O   1 
HETATM 4735 O  O   . HOH P 8 .   ? -15.77200 24.20300 8.51800   1.000 36.78513  ? 933  HOH A O   1 
HETATM 4736 O  O   . HOH P 8 .   ? -39.14700 21.61800 8.67400   1.000 51.26194  ? 934  HOH A O   1 
HETATM 4737 O  O   . HOH P 8 .   ? -21.14200 20.88600 46.84100  1.000 47.83169  ? 935  HOH A O   1 
HETATM 4738 O  O   . HOH P 8 .   ? -32.38800 17.53700 11.63600  1.000 44.25900  ? 936  HOH A O   1 
HETATM 4739 O  O   . HOH P 8 .   ? -44.63700 35.15000 35.42100  1.000 51.33859  ? 937  HOH A O   1 
HETATM 4740 O  O   . HOH P 8 .   ? -26.51400 41.68700 42.45100  1.000 42.68914  ? 938  HOH A O   1 
HETATM 4741 O  O   . HOH P 8 .   ? -2.13000  9.09100  26.19200  1.000 45.61029  ? 939  HOH A O   1 
HETATM 4742 O  O   . HOH P 8 .   ? -14.20900 37.04500 21.75600  1.000 32.43596  ? 940  HOH A O   1 
HETATM 4743 O  O   . HOH P 8 .   ? -25.61100 34.13800 27.96500  1.000 41.21652  ? 941  HOH A O   1 
HETATM 4744 O  O   . HOH P 8 .   ? -25.33500 11.15000 21.11900  1.000 40.79532  ? 942  HOH A O   1 
HETATM 4745 O  O   . HOH P 8 .   ? -36.38000 37.53900 6.88500   1.000 43.39717  ? 943  HOH A O   1 
HETATM 4746 O  O   . HOH P 8 .   ? -32.91800 41.64900 11.81100  1.000 41.96452  ? 944  HOH A O   1 
HETATM 4747 O  O   . HOH P 8 .   ? -31.40700 20.24700 -4.13400  1.000 52.58528  ? 945  HOH A O   1 
HETATM 4748 O  O   . HOH P 8 .   ? -41.08300 44.98200 29.84400  1.000 46.99311  ? 946  HOH A O   1 
HETATM 4749 O  O   . HOH P 8 .   ? -41.08400 49.83700 32.17500  1.000 48.51624  ? 947  HOH A O   1 
HETATM 4750 O  O   . HOH P 8 .   ? -30.28300 34.36500 35.81700  1.000 49.35057  ? 948  HOH A O   1 
HETATM 4751 O  O   . HOH P 8 .   ? -28.86200 46.72900 32.74800  1.000 50.88865  ? 949  HOH A O   1 
HETATM 4752 O  O   . HOH P 8 .   ? -15.12200 40.62200 -3.05700  1.000 43.83597  ? 950  HOH A O   1 
HETATM 4753 O  O   . HOH P 8 .   ? -23.59600 36.46100 30.71000  1.000 50.81693  ? 951  HOH A O   1 
HETATM 4754 O  O   . HOH P 8 .   ? -35.98000 22.18700 -8.80200  1.000 52.75001  ? 952  HOH A O   1 
HETATM 4755 O  O   . HOH P 8 .   ? -40.13400 36.39100 12.54400  1.000 41.15577  ? 953  HOH A O   1 
HETATM 4756 O  O   . HOH P 8 .   ? -20.61600 10.45400 19.84100  1.000 34.06448  ? 954  HOH A O   1 
HETATM 4757 O  O   . HOH P 8 .   ? -18.93500 17.08000 -18.18900 1.000 53.84595  ? 955  HOH A O   1 
HETATM 4758 O  O   . HOH P 8 .   ? -8.98900  22.82400 -1.49800  1.000 59.36134  ? 956  HOH A O   1 
HETATM 4759 O  O   . HOH P 8 .   ? -13.32100 32.46400 50.61200  1.000 50.27494  ? 957  HOH A O   1 
HETATM 4760 O  O   . HOH P 8 .   ? -13.29300 16.01500 10.36200  1.000 45.56116  ? 958  HOH A O   1 
HETATM 4761 O  O   . HOH P 8 .   ? -36.00700 53.96400 36.08100  1.000 43.15481  ? 959  HOH A O   1 
HETATM 4762 O  O   . HOH P 8 .   ? -22.01300 13.82700 11.13600  1.000 46.46724  ? 960  HOH A O   1 
HETATM 4763 O  O   . HOH P 8 .   ? -42.77000 16.47700 19.07800  1.000 45.48748  ? 961  HOH A O   1 
HETATM 4764 O  O   . HOH P 8 .   ? -47.79100 26.89200 32.42500  1.000 46.76327  ? 962  HOH A O   1 
HETATM 4765 O  O   . HOH P 8 .   ? -5.73600  15.95600 19.85700  1.000 39.19415  ? 963  HOH A O   1 
HETATM 4766 O  O   . HOH P 8 .   ? -21.152   45.688   13.772    1.000 46.63570  ? 964  HOH A O   1 
HETATM 4767 O  O   . HOH P 8 .   ? -34.88800 24.23800 31.31600  1.000 33.73678  ? 965  HOH A O   1 
HETATM 4768 O  O   . HOH P 8 .   ? -23.84900 15.76600 12.83600  1.000 45.75426  ? 966  HOH A O   1 
HETATM 4769 O  O   . HOH P 8 .   ? -23.62400 26.71500 2.17700   1.000 41.22066  ? 967  HOH A O   1 
HETATM 4770 O  O   . HOH P 8 .   ? -47.20400 32.64500 27.09500  1.000 53.28508  ? 968  HOH A O   1 
HETATM 4771 O  O   . HOH P 8 .   ? -20.69000 5.81000  32.81600  1.000 51.95054  ? 969  HOH A O   1 
HETATM 4772 O  O   . HOH P 8 .   ? -16.542   7.689    20.555    1.000 43.40710  ? 970  HOH A O   1 
HETATM 4773 O  O   . HOH P 8 .   ? -18.53800 34.71300 11.41000  1.000 43.63340  ? 971  HOH A O   1 
HETATM 4774 O  O   . HOH P 8 .   ? -11.07700 12.51200 22.08900  1.000 51.35786  ? 972  HOH A O   1 
HETATM 4775 O  O   . HOH P 8 .   ? -9.763    44.073   -16.164   1.000 58.67120  ? 973  HOH A O   1 
HETATM 4776 O  O   . HOH P 8 .   ? -44.95900 40.18000 32.92100  1.000 52.21499  ? 974  HOH A O   1 
HETATM 4777 O  O   . HOH P 8 .   ? -45.15800 26.71200 22.21300  1.000 40.83685  ? 975  HOH A O   1 
HETATM 4778 O  O   . HOH P 8 .   ? -23.42300 12.15800 39.64800  1.000 46.56109  ? 976  HOH A O   1 
HETATM 4779 O  O   . HOH P 8 .   ? -35.42900 29.87900 2.50600   1.000 43.17333  ? 977  HOH A O   1 
HETATM 4780 O  O   . HOH P 8 .   ? -13.48100 26.80500 52.97200  1.000 47.99239  ? 978  HOH A O   1 
HETATM 4781 O  O   . HOH P 8 .   ? -30.26100 56.40600 39.14200  1.000 42.47591  ? 979  HOH A O   1 
HETATM 4782 O  O   . HOH P 8 .   ? -38.15500 18.02400 11.03600  1.000 46.74939  ? 980  HOH A O   1 
HETATM 4783 O  O   . HOH P 8 .   ? -34.80800 36.92600 -12.91400 1.000 46.51744  ? 981  HOH A O   1 
HETATM 4784 O  O   . HOH P 8 .   ? -13.79200 13.19200 22.29900  1.000 51.34900  ? 982  HOH A O   1 
HETATM 4785 O  O   . HOH P 8 .   ? -47.43100 32.47600 38.29600  1.000 53.75818  ? 983  HOH A O   1 
HETATM 4786 O  O   . HOH P 8 .   ? -26.48600 25.10100 52.17800  1.000 55.42812  ? 984  HOH A O   1 
HETATM 4787 O  O   . HOH P 8 .   ? -27.16800 15.03200 14.53700  1.000 49.20115  ? 985  HOH A O   1 
HETATM 4788 O  O   . HOH P 8 .   ? -24.21700 41.10900 -16.46500 1.000 58.96743  ? 986  HOH A O   1 
HETATM 4789 O  O   . HOH P 8 .   ? -17.39500 42.98500 46.49100  1.000 43.61805  ? 987  HOH A O   1 
HETATM 4790 O  O   . HOH P 8 .   ? -38.90200 25.54000 -10.16600 1.000 50.76656  ? 988  HOH A O   1 
HETATM 4791 O  O   . HOH P 8 .   ? -27.50200 16.98000 3.77300   1.000 49.07615  ? 989  HOH A O   1 
HETATM 4792 O  O   . HOH P 8 .   ? -4.28500  30.20400 32.34300  1.000 57.88158  ? 990  HOH A O   1 
HETATM 4793 O  O   . HOH P 8 .   ? -33.80600 47.83100 31.74000  1.000 50.36780  ? 991  HOH A O   1 
HETATM 4794 O  O   . HOH P 8 .   ? -20.10100 46.00000 4.73300   1.000 49.72639  ? 992  HOH A O   1 
HETATM 4795 O  O   . HOH P 8 .   ? -19.23100 33.00900 57.90400  1.000 54.28839  ? 993  HOH A O   1 
HETATM 4796 O  O   . HOH P 8 .   ? -9.39700  21.57900 16.64800  1.000 44.36031  ? 994  HOH A O   1 
HETATM 4797 O  O   . HOH P 8 .   ? -10.86600 29.08400 50.09100  1.000 56.45439  ? 995  HOH A O   1 
HETATM 4798 O  O   . HOH P 8 .   ? -26.40200 43.76300 16.48100  1.000 46.76719  ? 996  HOH A O   1 
HETATM 4799 O  O   . HOH P 8 .   ? -11.66700 16.41400 12.64400  1.000 52.27285  ? 997  HOH A O   1 
HETATM 4800 O  O   . HOH P 8 .   ? -43.49800 29.40200 8.49600   1.000 54.98793  ? 998  HOH A O   1 
HETATM 4801 O  O   . HOH P 8 .   ? -22.79100 43.11500 9.11300   1.000 44.43892  ? 999  HOH A O   1 
HETATM 4802 O  O   . HOH P 8 .   ? -7.42700  35.54200 23.97900  1.000 52.47390  ? 1000 HOH A O   1 
HETATM 4803 O  O   . HOH P 8 .   ? -8.36800  17.61100 12.01300  1.000 46.56614  ? 1001 HOH A O   1 
HETATM 4804 O  O   . HOH P 8 .   ? -46.46600 37.42200 22.96000  1.000 44.03836  ? 1002 HOH A O   1 
HETATM 4805 O  O   . HOH P 8 .   ? -29.97000 22.32400 53.05800  1.000 49.87658  ? 1003 HOH A O   1 
HETATM 4806 O  O   . HOH P 8 .   ? -35.71800 21.46600 -12.29700 1.000 55.09208  ? 1004 HOH A O   1 
HETATM 4807 O  O   . HOH P 8 .   ? -21.03100 29.18400 55.56400  1.000 54.42105  ? 1005 HOH A O   1 
HETATM 4808 O  O   . HOH P 8 .   ? -34.56000 7.62800  17.77900  1.000 56.87868  ? 1006 HOH A O   1 
HETATM 4809 O  O   . HOH P 8 .   ? -35.85900 38.19800 -11.05500 1.000 45.03154  ? 1007 HOH A O   1 
HETATM 4810 O  O   . HOH P 8 .   ? -16.84400 35.22100 50.07300  1.000 50.13848  ? 1008 HOH A O   1 
HETATM 4811 O  O   . HOH P 8 .   ? -18.86400 25.61900 -21.83300 1.000 60.08367  ? 1009 HOH A O   1 
HETATM 4812 O  O   . HOH P 8 .   ? -40.56000 14.28500 27.97100  1.000 52.05405  ? 1010 HOH A O   1 
HETATM 4813 O  O   . HOH P 8 .   ? -28.95500 12.17200 40.33300  1.000 55.94907  ? 1011 HOH A O   1 
HETATM 4814 O  O   . HOH P 8 .   ? -8.28900  31.70700 17.13500  1.000 44.99548  ? 1012 HOH A O   1 
HETATM 4815 O  O   . HOH P 8 .   ? -22.15700 40.22300 -17.14900 1.000 57.23707  ? 1013 HOH A O   1 
HETATM 4816 O  O   . HOH P 8 .   ? -10.20400 35.83600 45.85500  1.000 52.75679  ? 1014 HOH A O   1 
HETATM 4817 O  O   . HOH P 8 .   ? -18.34500 35.49800 55.92000  1.000 60.19613  ? 1015 HOH A O   1 
HETATM 4818 O  O   . HOH P 8 .   ? -29.04600 14.29700 -1.78200  1.000 53.62072  ? 1016 HOH A O   1 
HETATM 4819 O  O   . HOH P 8 .   ? -16.08800 41.59200 24.90100  1.000 47.18759  ? 1017 HOH A O   1 
HETATM 4820 O  O   . HOH P 8 .   ? -18.61900 36.98500 48.92300  1.000 54.64240  ? 1018 HOH A O   1 
HETATM 4821 O  O   . HOH P 8 .   ? -24.795   5.430    32.190    1.000 53.89854  ? 1019 HOH A O   1 
HETATM 4822 O  O   . HOH P 8 .   ? -11.50900 8.82200  0.78200   1.000 53.63322  ? 1020 HOH A O   1 
HETATM 4823 O  O   . HOH P 8 .   ? -32.414   43.691   -16.258   1.000 53.29618  ? 1021 HOH A O   1 
HETATM 4824 O  O   . HOH P 8 .   ? -13.42800 41.18700 22.70400  1.000 49.20859  ? 1022 HOH A O   1 
HETATM 4825 O  O   . HOH P 8 .   ? -10.44800 24.25300 44.98700  1.000 47.13695  ? 1023 HOH A O   1 
HETATM 4826 O  O   . HOH P 8 .   ? -44.97400 42.57600 32.86200  1.000 65.26600  ? 1024 HOH A O   1 
HETATM 4827 O  O   . HOH P 8 .   ? -48.043   37.577   16.920    1.000 58.28531  ? 1025 HOH A O   1 
HETATM 4828 O  O   . HOH P 8 .   ? -38.74100 26.26000 -12.94800 1.000 52.69167  ? 1026 HOH A O   1 
HETATM 4829 O  O   . HOH P 8 .   ? -24.94300 14.42200 14.44900  1.000 47.51503  ? 1027 HOH A O   1 
HETATM 4830 O  O   . HOH P 8 .   ? -14.07300 35.73300 49.31500  1.000 54.32469  ? 1028 HOH A O   1 
HETATM 4831 O  O   . HOH P 8 .   ? -43.98100 14.90000 28.58600  1.000 54.36151  ? 1029 HOH A O   1 
HETATM 4832 O  O   . HOH P 8 .   ? -46.97300 34.58900 23.73100  1.000 60.03859  ? 1030 HOH A O   1 
HETATM 4833 O  O   . HOH P 8 .   ? -33.97900 46.83500 54.40000  1.000 49.41747  ? 1031 HOH A O   1 
HETATM 4834 O  O   . HOH P 8 .   ? -39.12300 33.74200 2.12900   1.000 58.99674  ? 1032 HOH A O   1 
HETATM 4835 O  O   . HOH P 8 .   ? -47.77000 39.15900 20.92700  1.000 62.85458  ? 1033 HOH A O   1 
HETATM 4836 O  O   . HOH P 8 .   ? -49.13100 35.24300 24.77600  1.000 57.84395  ? 1034 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   . GLN A 3   ? 1.48235 0.83899 1.01034 0.03479  -0.36803 0.00620  3   GLN A N   
2    C CA  . GLN A 3   ? 1.42991 0.79322 0.96727 0.03773  -0.36817 0.00631  3   GLN A CA  
3    C C   . GLN A 3   ? 1.51862 0.87248 1.04482 0.03609  -0.36269 0.00636  3   GLN A C   
4    O O   . GLN A 3   ? 1.57413 0.91608 1.08499 0.03475  -0.36053 0.00674  3   GLN A O   
5    C CB  . GLN A 3   ? 1.42228 0.79011 0.96502 0.04595  -0.37496 0.00745  3   GLN A CB  
6    C CG  . GLN A 3   ? 1.41596 0.79067 0.96581 0.04745  -0.38084 0.00738  3   GLN A CG  
7    C CD  . GLN A 3   ? 1.45399 0.83313 1.00862 0.05573  -0.38797 0.00846  3   GLN A CD  
8    O OE1 . GLN A 3   ? 1.45010 0.82774 1.00397 0.06082  -0.38849 0.00941  3   GLN A OE1 
9    N NE2 . GLN A 3   ? 1.57972 0.96444 1.13944 0.05732  -0.39366 0.00833  3   GLN A NE2 
10   N N   . ALA A 4   ? 1.37521 0.73415 0.90858 0.03618  -0.36063 0.00605  4   ALA A N   
11   C CA  . ALA A 4   ? 1.19946 0.55032 0.72305 0.03493  -0.35575 0.00605  4   ALA A CA  
12   C C   . ALA A 4   ? 1.16285 0.51759 0.69262 0.04141  -0.35769 0.00695  4   ALA A C   
13   O O   . ALA A 4   ? 0.97082 0.33712 0.51545 0.04392  -0.36081 0.00694  4   ALA A O   
14   C CB  . ALA A 4   ? 1.15775 0.51032 0.68287 0.02749  -0.35034 0.00458  4   ALA A CB  
15   N N   . SER A 5   ? 1.20882 0.55377 0.72728 0.04428  -0.35598 0.00789  5   SER A N   
16   C CA  . SER A 5   ? 1.06690 0.41450 0.59078 0.05153  -0.35790 0.00902  5   SER A CA  
17   C C   . SER A 5   ? 1.06139 0.41895 0.59787 0.04988  -0.35601 0.00816  5   SER A C   
18   O O   . SER A 5   ? 1.02153 0.37758 0.55497 0.04358  -0.35101 0.00698  5   SER A O   
19   C CB  . SER A 5   ? 1.00819 0.34300 0.51783 0.05467  -0.35570 0.01024  5   SER A CB  
20   O OG  . SER A 5   ? 1.08329 0.42084 0.59911 0.06211  -0.35752 0.01136  5   SER A OG  
21   N N   . GLY A 6   ? 0.97053 0.33822 0.52081 0.05541  -0.36021 0.00878  6   GLY A N   
22   C CA  . GLY A 6   ? 0.95708 0.33418 0.51953 0.05476  -0.35885 0.00833  6   GLY A CA  
23   C C   . GLY A 6   ? 0.95647 0.34403 0.53341 0.06201  -0.36449 0.00938  6   GLY A C   
24   O O   . GLY A 6   ? 0.96526 0.35361 0.54326 0.06679  -0.36965 0.01020  6   GLY A O   
25   N N   . PRO A 7   ? 0.98351 0.37970 0.57206 0.06277  -0.36389 0.00938  7   PRO A N   
26   C CA  . PRO A 7   ? 0.99381 0.40111 0.59754 0.06940  -0.36929 0.01039  7   PRO A CA  
27   C C   . PRO A 7   ? 0.99482 0.41399 0.61138 0.06627  -0.37318 0.00981  7   PRO A C   
28   O O   . PRO A 7   ? 1.12390 0.55396 0.75473 0.07017  -0.37718 0.01044  7   PRO A O   
29   C CB  . PRO A 7   ? 0.93883 0.34815 0.54699 0.07041  -0.36563 0.01061  7   PRO A CB  
30   C CG  . PRO A 7   ? 0.92908 0.33503 0.53095 0.06133  -0.35969 0.00918  7   PRO A CG  
31   C CD  . PRO A 7   ? 0.93783 0.33314 0.52486 0.05744  -0.35804 0.00849  7   PRO A CD  
32   N N   . TYR A 8   ? 0.92991 0.34653 0.54124 0.05933  -0.37176 0.00867  8   TYR A N   
33   C CA  . TYR A 8   ? 1.04964 0.47693 0.67300 0.05580  -0.37475 0.00810  8   TYR A CA  
34   C C   . TYR A 8   ? 1.03920 0.46593 0.66053 0.05635  -0.37931 0.00796  8   TYR A C   
35   O O   . TYR A 8   ? 1.01759 0.43402 0.62541 0.05368  -0.37711 0.00756  8   TYR A O   
36   C CB  . TYR A 8   ? 1.04820 0.47544 0.67079 0.04711  -0.36937 0.00690  8   TYR A CB  
37   C CG  . TYR A 8   ? 1.00496 0.43473 0.63138 0.04605  -0.36547 0.00699  8   TYR A CG  
38   C CD1 . TYR A 8   ? 1.00163 0.44271 0.64292 0.04841  -0.36810 0.00773  8   TYR A CD1 
39   C CD2 . TYR A 8   ? 0.95540 0.37630 0.57044 0.04259  -0.35932 0.00634  8   TYR A CD2 
40   C CE1 . TYR A 8   ? 1.06261 0.50537 0.70663 0.04767  -0.36447 0.00800  8   TYR A CE1 
41   C CE2 . TYR A 8   ? 0.93520 0.35810 0.55298 0.04169  -0.35582 0.00639  8   TYR A CE2 
42   C CZ  . TYR A 8   ? 0.95672 0.39021 0.58868 0.04434  -0.35827 0.00730  8   TYR A CZ  
43   O OH  . TYR A 8   ? 1.00303 0.43785 0.63696 0.04370  -0.35475 0.00753  8   TYR A OH  
44   N N   . GLU A 9   ? 1.06080 0.49853 0.69534 0.05990  -0.38572 0.00833  9   GLU A N   
45   C CA  . GLU A 9   ? 1.05889 0.49740 0.69265 0.05987  -0.39041 0.00801  9   GLU A CA  
46   C C   . GLU A 9   ? 1.01587 0.46153 0.65790 0.05309  -0.39003 0.00702  9   GLU A C   
47   O O   . GLU A 9   ? 0.90604 0.35894 0.55792 0.05072  -0.38833 0.00695  9   GLU A O   
48   C CB  . GLU A 9   ? 1.09918 0.54450 0.74084 0.06821  -0.39814 0.00891  9   GLU A CB  
49   C CG  . GLU A 9   ? 1.29666 0.75397 0.95443 0.07293  -0.40095 0.00958  9   GLU A CG  
50   C CD  . GLU A 9   ? 1.44228 0.90692 1.10839 0.08135  -0.40895 0.01033  9   GLU A CD  
51   O OE1 . GLU A 9   ? 1.31804 0.77480 0.97475 0.08701  -0.40991 0.01120  9   GLU A OE1 
52   O OE2 . GLU A 9   ? 1.54409 1.02240 1.22614 0.08221  -0.41436 0.01003  9   GLU A OE2 
53   N N   . ALA A 10  ? 1.06399 0.50788 0.70248 0.05066  -0.39195 0.00644  10  ALA A N   
54   C CA  . ALA A 10  ? 0.93416 0.38313 0.57892 0.04411  -0.39086 0.00561  10  ALA A CA  
55   C C   . ALA A 10  ? 0.99657 0.46025 0.65901 0.04618  -0.39729 0.00565  10  ALA A C   
56   O O   . ALA A 10  ? 1.01457 0.48219 0.68058 0.04523  -0.40134 0.00514  10  ALA A O   
57   C CB  . ALA A 10  ? 0.91601 0.35704 0.54997 0.04104  -0.39018 0.00508  10  ALA A CB  
58   N N   . THR A 11  ? 0.95114 0.42265 0.62423 0.04876  -0.39805 0.00622  11  THR A N   
59   C CA  . THR A 11  ? 1.03158 0.51796 0.72278 0.05017  -0.40382 0.00627  11  THR A CA  
60   C C   . THR A 11  ? 1.01309 0.50383 0.71134 0.04604  -0.39969 0.00650  11  THR A C   
61   O O   . THR A 11  ? 1.01009 0.49281 0.69948 0.04425  -0.39338 0.00671  11  THR A O   
62   C CB  . THR A 11  ? 1.09872 0.59147 0.79732 0.05882  -0.40992 0.00703  11  THR A CB  
63   O OG1 . THR A 11  ? 1.32717 0.83507 1.04442 0.05914  -0.41480 0.00695  11  THR A OG1 
64   C CG2 . THR A 11  ? 1.09608 0.58364 0.79002 0.06292  -0.40630 0.00806  11  THR A CG2 
65   N N   . TRP A 12  ? 0.95702 0.46021 0.67076 0.04468  -0.40333 0.00647  12  TRP A N   
66   C CA  . TRP A 12  ? 0.88346 0.39110 0.60422 0.04100  -0.39983 0.00696  12  TRP A CA  
67   C C   . TRP A 12  ? 0.90699 0.41617 0.63061 0.04651  -0.39944 0.00807  12  TRP A C   
68   O O   . TRP A 12  ? 0.99613 0.50058 0.71494 0.04418  -0.39361 0.00850  12  TRP A O   
69   C CB  . TRP A 12  ? 0.93730 0.45789 0.67403 0.03806  -0.40426 0.00674  12  TRP A CB  
70   C CG  . TRP A 12  ? 1.04138 0.55953 0.77484 0.03193  -0.40320 0.00583  12  TRP A CG  
71   C CD1 . TRP A 12  ? 1.05182 0.57349 0.78819 0.03215  -0.40842 0.00493  12  TRP A CD1 
72   C CD2 . TRP A 12  ? 1.05920 0.57023 0.78512 0.02510  -0.39625 0.00580  12  TRP A CD2 
73   N NE1 . TRP A 12  ? 1.03301 0.55004 0.76414 0.02607  -0.40509 0.00445  12  TRP A NE1 
74   C CE2 . TRP A 12  ? 1.03994 0.55053 0.76490 0.02183  -0.39760 0.00505  12  TRP A CE2 
75   C CE3 . TRP A 12  ? 1.06181 0.56705 0.78188 0.02172  -0.38917 0.00634  12  TRP A CE3 
76   C CZ2 . TRP A 12  ? 1.03876 0.54337 0.75755 0.01577  -0.39197 0.00506  12  TRP A CZ2 
77   C CZ3 . TRP A 12  ? 1.01667 0.51643 0.73095 0.01553  -0.38383 0.00620  12  TRP A CZ3 
78   C CH2 . TRP A 12  ? 1.00989 0.50932 0.72371 0.01281  -0.38513 0.00570  12  TRP A CH2 
79   N N   . GLU A 13  ? 1.02959 0.54496 0.76057 0.05396  -0.40541 0.00853  13  GLU A N   
80   C CA  . GLU A 13  ? 1.05629 0.57419 0.79205 0.06009  -0.40526 0.00983  13  GLU A CA  
81   C C   . GLU A 13  ? 0.98225 0.48599 0.70146 0.06144  -0.39877 0.01017  13  GLU A C   
82   O O   . GLU A 13  ? 0.99296 0.49574 0.71268 0.06277  -0.39528 0.01105  13  GLU A O   
83   C CB  . GLU A 13  ? 1.12646 0.65461 0.87467 0.06837  -0.41320 0.01023  13  GLU A CB  
84   C CG  . GLU A 13  ? 1.47727 1.00986 1.23349 0.07507  -0.41337 0.01167  13  GLU A CG  
85   C CD  . GLU A 13  ? 1.60959 1.15265 1.37894 0.08419  -0.42098 0.01206  13  GLU A CD  
86   O OE1 . GLU A 13  ? 1.66541 1.21477 1.44010 0.08467  -0.42707 0.01108  13  GLU A OE1 
87   O OE2 . GLU A 13  ? 1.62139 1.16624 1.39568 0.09104  -0.42069 0.01329  13  GLU A OE2 
88   N N   . SER A 14  ? 0.95869 0.45173 0.66363 0.06071  -0.39712 0.00949  14  SER A N   
89   C CA  . SER A 14  ? 1.04929 0.52871 0.73816 0.06112  -0.39097 0.00960  14  SER A CA  
90   C C   . SER A 14  ? 0.93215 0.40633 0.61446 0.05297  -0.38385 0.00892  14  SER A C   
91   O O   . SER A 14  ? 1.04120 0.51053 0.71846 0.05310  -0.37905 0.00925  14  SER A O   
92   C CB  . SER A 14  ? 0.99898 0.46867 0.67480 0.06269  -0.39163 0.00922  14  SER A CB  
93   O OG  . SER A 14  ? 1.14704 0.60401 0.80795 0.06305  -0.38608 0.00934  14  SER A OG  
94   N N   . THR A 15  ? 0.94848 0.42377 0.63117 0.04647  -0.38335 0.00801  15  THR A N   
95   C CA  . THR A 15  ? 0.92354 0.39352 0.59965 0.03885  -0.37655 0.00732  15  THR A CA  
96   C C   . THR A 15  ? 0.86543 0.34234 0.55084 0.03744  -0.37494 0.00801  15  THR A C   
97   O O   . THR A 15  ? 0.88198 0.35349 0.56062 0.03361  -0.36899 0.00773  15  THR A O   
98   C CB  . THR A 15  ? 0.88352 0.35291 0.55841 0.03319  -0.37653 0.00644  15  THR A CB  
99   O OG1 . THR A 15  ? 1.04345 0.52479 0.73312 0.03396  -0.38235 0.00676  15  THR A OG1 
100  C CG2 . THR A 15  ? 0.90550 0.36580 0.56837 0.03420  -0.37705 0.00588  15  THR A CG2 
101  N N   . ASP A 16  ? 0.85553 0.34406 0.55588 0.04064  -0.38023 0.00892  16  ASP A N   
102  C CA  . ASP A 16  ? 0.84795 0.34373 0.55806 0.03916  -0.37931 0.00989  16  ASP A CA  
103  C C   . ASP A 16  ? 0.98171 0.47376 0.68828 0.04339  -0.37609 0.01085  16  ASP A C   
104  O O   . ASP A 16  ? 1.01717 0.51382 0.73022 0.04268  -0.37486 0.01189  16  ASP A O   
105  C CB  . ASP A 16  ? 0.86215 0.37198 0.59007 0.04159  -0.38650 0.01062  16  ASP A CB  
106  C CG  . ASP A 16  ? 0.93905 0.45433 0.67301 0.03599  -0.38904 0.00981  16  ASP A CG  
107  O OD1 . ASP A 16  ? 0.91203 0.41972 0.63613 0.03104  -0.38540 0.00883  16  ASP A OD1 
108  O OD2 . ASP A 16  ? 1.01938 0.54658 0.76826 0.03677  -0.39467 0.01019  16  ASP A OD2 
109  N N   . LYS A 17  ? 0.92276 0.40618 0.61892 0.04764  -0.37467 0.01063  17  LYS A N   
110  C CA  . LYS A 17  ? 0.86993 0.34891 0.56232 0.05244  -0.37158 0.01154  17  LYS A CA  
111  C C   . LYS A 17  ? 0.85643 0.32487 0.53448 0.04672  -0.36406 0.01052  17  LYS A C   
112  O O   . LYS A 17  ? 0.93902 0.40355 0.61323 0.04845  -0.36024 0.01102  17  LYS A O   
113  C CB  . LYS A 17  ? 0.91780 0.39369 0.60778 0.06070  -0.37468 0.01195  17  LYS A CB  
114  C CG  . LYS A 17  ? 1.01251 0.49999 0.71806 0.06747  -0.38233 0.01293  17  LYS A CG  
115  C CD  . LYS A 17  ? 0.99048 0.47441 0.69199 0.07421  -0.38589 0.01295  17  LYS A CD  
116  C CE  . LYS A 17  ? 0.99918 0.49050 0.71269 0.08405  -0.39047 0.01431  17  LYS A CE  
117  N NZ  . LYS A 17  ? 1.15447 0.64193 0.86339 0.09076  -0.39396 0.01440  17  LYS A NZ  
118  N N   . HIS A 18  ? 0.87379 0.33823 0.54491 0.04025  -0.36227 0.00908  18  HIS A N   
119  C CA  . HIS A 18  ? 0.89754 0.35343 0.55649 0.03407  -0.35553 0.00786  18  HIS A CA  
120  C C   . HIS A 18  ? 0.98429 0.44437 0.64805 0.03080  -0.35245 0.00835  18  HIS A C   
121  O O   . HIS A 18  ? 0.83386 0.30328 0.50975 0.02991  -0.35538 0.00924  18  HIS A O   
122  C CB  . HIS A 18  ? 0.87986 0.33250 0.53369 0.02812  -0.35468 0.00650  18  HIS A CB  
123  C CG  . HIS A 18  ? 0.97757 0.42367 0.62187 0.02146  -0.34838 0.00523  18  HIS A CG  
124  N ND1 . HIS A 18  ? 1.01927 0.46893 0.66777 0.01539  -0.34619 0.00492  18  HIS A ND1 
125  C CD2 . HIS A 18  ? 0.88864 0.32521 0.51984 0.01998  -0.34402 0.00423  18  HIS A CD2 
126  C CE1 . HIS A 18  ? 0.99292 0.43585 0.63179 0.01072  -0.34082 0.00374  18  HIS A CE1 
127  N NE2 . HIS A 18  ? 0.93098 0.36608 0.55917 0.01318  -0.33956 0.00319  18  HIS A NE2 
128  N N   . ILE A 19  ? 0.92686 0.38026 0.58125 0.02912  -0.34701 0.00784  19  ILE A N   
129  C CA  . ILE A 19  ? 0.88522 0.34124 0.54189 0.02571  -0.34351 0.00825  19  ILE A CA  
130  C C   . ILE A 19  ? 0.86319 0.32045 0.51969 0.01777  -0.34159 0.00715  19  ILE A C   
131  O O   . ILE A 19  ? 0.86632 0.31659 0.51269 0.01371  -0.33822 0.00550  19  ILE A O   
132  C CB  . ILE A 19  ? 0.89366 0.34166 0.53951 0.02663  -0.33852 0.00785  19  ILE A CB  
133  C CG1 . ILE A 19  ? 0.93149 0.37724 0.57778 0.03511  -0.34008 0.00906  19  ILE A CG1 
134  C CG2 . ILE A 19  ? 0.86213 0.31215 0.50891 0.02293  -0.33478 0.00819  19  ILE A CG2 
135  C CD1 . ILE A 19  ? 0.99068 0.42633 0.62419 0.03616  -0.33525 0.00837  19  ILE A CD1 
136  N N   . ALA A 20  ? 0.81599 0.28164 0.48360 0.01592  -0.34376 0.00818  20  ALA A N   
137  C CA  . ALA A 20  ? 0.82781 0.29452 0.49641 0.00912  -0.34211 0.00746  20  ALA A CA  
138  C C   . ALA A 20  ? 0.82392 0.28470 0.48308 0.00403  -0.33586 0.00627  20  ALA A C   
139  O O   . ALA A 20  ? 0.85028 0.30594 0.50317 -0.00010 -0.33322 0.00491  20  ALA A O   
140  C CB  . ALA A 20  ? 0.86041 0.33675 0.54204 0.00811  -0.34515 0.00907  20  ALA A CB  
141  N N   . SER A 21  ? 0.80948 0.27136 0.46842 0.00454  -0.33372 0.00701  21  SER A N   
142  C CA  . SER A 21  ? 0.94848 0.40596 0.59918 -0.00006 -0.32819 0.00591  21  SER A CA  
143  C C   . SER A 21  ? 0.88108 0.33373 0.52373 0.00338  -0.32599 0.00578  21  SER A C   
144  O O   . SER A 21  ? 0.86192 0.31728 0.50838 0.00677  -0.32622 0.00748  21  SER A O   
145  C CB  . SER A 21  ? 0.89983 0.36274 0.55690 -0.00366 -0.32711 0.00702  21  SER A CB  
146  O OG  . SER A 21  ? 1.08176 0.55051 0.74678 0.00022  -0.32980 0.00929  21  SER A OG  
147  N N   . PRO A 22  ? 0.87881 0.32372 0.51024 0.00270  -0.32378 0.00401  22  PRO A N   
148  C CA  . PRO A 22  ? 0.85160 0.29099 0.47462 0.00589  -0.32158 0.00393  22  PRO A CA  
149  C C   . PRO A 22  ? 0.91308 0.35223 0.53242 0.00309  -0.31760 0.00385  22  PRO A C   
150  O O   . PRO A 22  ? 0.97798 0.42065 0.60017 -0.00179 -0.31650 0.00354  22  PRO A O   
151  C CB  . PRO A 22  ? 0.82335 0.25502 0.43546 0.00420  -0.32058 0.00204  22  PRO A CB  
152  C CG  . PRO A 22  ? 0.84881 0.28206 0.46235 -0.00192 -0.31964 0.00101  22  PRO A CG  
153  C CD  . PRO A 22  ? 0.86138 0.30196 0.48768 -0.00107 -0.32320 0.00231  22  PRO A CD  
154  N N   . GLU A 23  ? 0.86947 0.30384 0.48232 0.00640  -0.31541 0.00418  23  GLU A N   
155  C CA  . GLU A 23  ? 0.84094 0.27422 0.44919 0.00439  -0.31161 0.00422  23  GLU A CA  
156  C C   . GLU A 23  ? 0.85490 0.28637 0.45494 -0.00253 -0.30925 0.00204  23  GLU A C   
157  O O   . GLU A 23  ? 0.89721 0.33334 0.49970 -0.00555 -0.30646 0.00279  23  GLU A O   
158  C CB  . GLU A 23  ? 0.82916 0.25591 0.43155 0.00987  -0.30957 0.00485  23  GLU A CB  
159  C CG  . GLU A 23  ? 1.00197 0.42690 0.60023 0.00893  -0.30572 0.00519  23  GLU A CG  
160  C CD  . GLU A 23  ? 1.28658 0.70330 0.87839 0.01428  -0.30305 0.00539  23  GLU A CD  
161  O OE1 . GLU A 23  ? 1.15842 0.56904 0.74366 0.01640  -0.30311 0.00448  23  GLU A OE1 
162  O OE2 . GLU A 23  ? 1.18871 0.60436 0.78178 0.01638  -0.30067 0.00644  23  GLU A OE2 
163  N N   . TRP A 24  ? 0.82919 0.25896 0.42433 -0.00372 -0.30732 0.00160  24  TRP A N   
164  C CA  . TRP A 24  ? 0.80703 0.24349 0.40239 -0.00830 -0.30018 0.00294  24  TRP A CA  
165  C C   . TRP A 24  ? 0.84449 0.29124 0.45121 -0.01165 -0.29810 0.00421  24  TRP A C   
166  O O   . TRP A 24  ? 0.89504 0.34732 0.50350 -0.01467 -0.29324 0.00518  24  TRP A O   
167  C CB  . TRP A 24  ? 0.81087 0.24428 0.40005 -0.00893 -0.29839 0.00282  24  TRP A CB  
168  C CG  . TRP A 24  ? 0.89915 0.33325 0.49242 -0.00870 -0.30084 0.00267  24  TRP A CG  
169  C CD1 . TRP A 24  ? 0.86342 0.29013 0.45366 -0.00501 -0.30658 0.00143  24  TRP A CD1 
170  C CD2 . TRP A 24  ? 0.96624 0.40786 0.56647 -0.01209 -0.29777 0.00374  24  TRP A CD2 
171  N NE1 . TRP A 24  ? 0.88625 0.31551 0.48091 -0.00605 -0.30732 0.00175  24  TRP A NE1 
172  C CE2 . TRP A 24  ? 0.93064 0.36879 0.53126 -0.01035 -0.30187 0.00319  24  TRP A CE2 
173  C CE3 . TRP A 24  ? 0.79604 0.24603 0.40181 -0.01606 -0.29222 0.00506  24  TRP A CE3 
174  C CZ2 . TRP A 24  ? 0.97354 0.41614 0.57928 -0.01256 -0.30040 0.00403  24  TRP A CZ2 
175  C CZ3 . TRP A 24  ? 0.78357 0.23766 0.39474 -0.01798 -0.29071 0.00591  24  TRP A CZ3 
176  C CH2 . TRP A 24  ? 1.00630 0.45675 0.61715 -0.01631 -0.29469 0.00544  24  TRP A CH2 
177  N N   . PHE A 25  ? 0.79275 0.24123 0.40636 -0.01099 -0.30180 0.00419  25  PHE A N   
178  C CA  . PHE A 25  ? 0.84136 0.29840 0.46516 -0.01392 -0.30013 0.00553  25  PHE A CA  
179  C C   . PHE A 25  ? 0.80770 0.26800 0.43549 -0.01475 -0.30007 0.00624  25  PHE A C   
180  O O   . PHE A 25  ? 0.82751 0.29391 0.45890 -0.01784 -0.29539 0.00748  25  PHE A O   
181  C CB  . PHE A 25  ? 0.83700 0.29357 0.46629 -0.01248 -0.30542 0.00529  25  PHE A CB  
182  C CG  . PHE A 25  ? 0.79675 0.26056 0.43531 -0.01506 -0.30434 0.00671  25  PHE A CG  
183  C CD1 . PHE A 25  ? 0.76875 0.23605 0.40773 -0.01756 -0.29939 0.00767  25  PHE A CD1 
184  C CD2 . PHE A 25  ? 0.79410 0.26024 0.44047 -0.01476 -0.30884 0.00718  25  PHE A CD2 
185  C CE1 . PHE A 25  ? 0.76158 0.23444 0.40804 -0.01940 -0.29867 0.00906  25  PHE A CE1 
186  C CE2 . PHE A 25  ? 0.80381 0.27580 0.45786 -0.01704 -0.30812 0.00859  25  PHE A CE2 
187  C CZ  . PHE A 25  ? 0.76010 0.23530 0.41387 -0.01916 -0.30296 0.00948  25  PHE A CZ  
188  N N   . ARG A 26  ? 0.79773 0.25284 0.42392 -0.01177 -0.30532 0.00547  26  ARG A N   
189  C CA  . ARG A 26  ? 0.81560 0.27219 0.44425 -0.01246 -0.30595 0.00624  26  ARG A CA  
190  C C   . ARG A 26  ? 0.82633 0.28351 0.44883 -0.01432 -0.29996 0.00664  26  ARG A C   
191  O O   . ARG A 26  ? 0.94551 0.40571 0.57038 -0.01615 -0.29861 0.00766  26  ARG A O   
192  C CB  . ARG A 26  ? 0.79156 0.24411 0.42117 -0.00778 -0.31146 0.00646  26  ARG A CB  
193  C CG  . ARG A 26  ? 0.79432 0.25088 0.43365 -0.00483 -0.31597 0.00756  26  ARG A CG  
194  C CD  . ARG A 26  ? 0.79554 0.25520 0.44203 0.00087  -0.31795 0.01044  26  ARG A CD  
195  N NE  . ARG A 26  ? 1.00017 0.46291 0.65455 0.00493  -0.32280 0.01116  26  ARG A NE  
196  C CZ  . ARG A 26  ? 0.99479 0.46182 0.65863 0.00997  -0.32600 0.01368  26  ARG A CZ  
197  N NH1 . ARG A 26  ? 1.07040 0.53814 0.73680 0.01150  -0.32432 0.01595  26  ARG A NH1 
198  N NH2 . ARG A 26  ? 0.96017 0.43054 0.63104 0.01359  -0.33091 0.01398  26  ARG A NH2 
199  N N   . ASP A 27  ? 0.80681 0.26095 0.42156 -0.01402 -0.29678 0.00596  27  ASP A N   
200  C CA  . ASP A 27  ? 0.81994 0.27416 0.42862 -0.01569 -0.29174 0.00630  27  ASP A CA  
201  C C   . ASP A 27  ? 0.86323 0.32510 0.47619 -0.01958 -0.28588 0.00721  27  ASP A C   
202  O O   . ASP A 27  ? 0.83988 0.30350 0.45120 -0.02151 -0.28197 0.00773  27  ASP A O   
203  C CB  . ASP A 27  ? 0.90709 0.35264 0.50430 -0.01320 -0.29199 0.00525  27  ASP A CB  
204  C CG  . ASP A 27  ? 0.91558 0.35127 0.50727 -0.00872 -0.29755 0.00399  27  ASP A CG  
205  O OD1 . ASP A 27  ? 0.97724 0.41304 0.57375 -0.00774 -0.30130 0.00408  27  ASP A OD1 
206  O OD2 . ASP A 27  ? 0.83727 0.26466 0.41955 -0.00615 -0.29832 0.00291  27  ASP A OD2 
207  N N   . ALA A 28  ? 0.82363 0.28846 0.44159 -0.02042 -0.28543 0.00746  28  ALA A N   
208  C CA  . ALA A 28  ? 0.76073 0.22987 0.38226 -0.02334 -0.27975 0.00901  28  ALA A CA  
209  C C   . ALA A 28  ? 0.78891 0.26396 0.41803 -0.02500 -0.27746 0.01147  28  ALA A C   
210  O O   . ALA A 28  ? 0.80253 0.28013 0.43159 -0.02628 -0.27311 0.01402  28  ALA A O   
211  C CB  . ALA A 28  ? 0.77861 0.24779 0.40151 -0.02320 -0.28047 0.00897  28  ALA A CB  
212  N N   . LYS A 29  ? 0.84053 0.31813 0.47532 -0.02476 -0.28110 0.01122  29  LYS A N   
213  C CA  . LYS A 29  ? 0.74312 0.22585 0.38367 -0.02645 -0.27983 0.01302  29  LYS A CA  
214  C C   . LYS A 29  ? 0.78626 0.27481 0.43187 -0.02806 -0.27664 0.01500  29  LYS A C   
215  O O   . LYS A 29  ? 0.76369 0.25600 0.41554 -0.02873 -0.27826 0.01558  29  LYS A O   
216  C CB  . LYS A 29  ? 0.74399 0.22528 0.38014 -0.02706 -0.27737 0.01357  29  LYS A CB  
217  C CG  . LYS A 29  ? 0.81674 0.29223 0.44686 -0.02552 -0.28095 0.01152  29  LYS A CG  
218  C CD  . LYS A 29  ? 0.81449 0.28996 0.44867 -0.02451 -0.28689 0.01116  29  LYS A CD  
219  C CE  . LYS A 29  ? 0.78473 0.25335 0.41224 -0.02228 -0.29092 0.01037  29  LYS A CE  
220  N NZ  . LYS A 29  ? 0.82998 0.29650 0.46177 -0.02053 -0.29763 0.01041  29  LYS A NZ  
221  N N   . PHE A 30  ? 0.75459 0.24367 0.39707 -0.02868 -0.27262 0.01607  30  PHE A N   
222  C CA  . PHE A 30  ? 0.72596 0.22042 0.37193 -0.03027 -0.26980 0.01766  30  PHE A CA  
223  C C   . PHE A 30  ? 0.79848 0.29170 0.44198 -0.03024 -0.26861 0.01782  30  PHE A C   
224  O O   . PHE A 30  ? 0.78612 0.27485 0.42341 -0.02967 -0.26793 0.01759  30  PHE A O   
225  C CB  . PHE A 30  ? 0.72265 0.21930 0.36702 -0.03161 -0.26659 0.01881  30  PHE A CB  
226  C CG  . PHE A 30  ? 0.71637 0.21781 0.36361 -0.03313 -0.26411 0.01993  30  PHE A CG  
227  C CD1 . PHE A 30  ? 0.79168 0.29732 0.44504 -0.03370 -0.26478 0.02027  30  PHE A CD1 
228  C CD2 . PHE A 30  ? 0.71632 0.21745 0.35966 -0.03404 -0.26152 0.02060  30  PHE A CD2 
229  C CE1 . PHE A 30  ? 0.70667 0.21593 0.36199 -0.03481 -0.26277 0.02106  30  PHE A CE1 
230  C CE2 . PHE A 30  ? 0.71152 0.21635 0.35713 -0.03536 -0.25977 0.02137  30  PHE A CE2 
231  C CZ  . PHE A 30  ? 0.70671 0.21553 0.35821 -0.03558 -0.26032 0.02153  30  PHE A CZ  
232  N N   . GLY A 31  ? 0.78749 0.28399 0.43503 -0.03091 -0.26851 0.01831  31  GLY A N   
233  C CA  . GLY A 31  ? 0.73624 0.23112 0.38087 -0.03114 -0.26750 0.01853  31  GLY A CA  
234  C C   . GLY A 31  ? 0.79546 0.29487 0.44338 -0.03250 -0.26579 0.01960  31  GLY A C   
235  O O   . GLY A 31  ? 0.78695 0.29064 0.44017 -0.03298 -0.26600 0.01996  31  GLY A O   
236  N N   . VAL A 32  ? 0.74157 0.23932 0.38550 -0.03318 -0.26422 0.02008  32  VAL A N   
237  C CA  . VAL A 32  ? 0.79581 0.29675 0.44141 -0.03444 -0.26266 0.02092  32  VAL A CA  
238  C C   . VAL A 32  ? 0.79860 0.29593 0.44084 -0.03433 -0.26344 0.02072  32  VAL A C   
239  O O   . VAL A 32  ? 0.85241 0.34461 0.48856 -0.03417 -0.26344 0.02052  32  VAL A O   
240  C CB  . VAL A 32  ? 0.71750 0.21989 0.36056 -0.03603 -0.25973 0.02189  32  VAL A CB  
241  C CG1 . VAL A 32  ? 0.75877 0.26284 0.40204 -0.03720 -0.25858 0.02249  32  VAL A CG1 
242  C CG2 . VAL A 32  ? 0.71101 0.21635 0.35674 -0.03621 -0.25911 0.02200  32  VAL A CG2 
243  N N   . TYR A 33  ? 0.79893 0.29819 0.44431 -0.03444 -0.26420 0.02078  33  TYR A N   
244  C CA  . TYR A 33  ? 0.72454 0.21990 0.36592 -0.03450 -0.26493 0.02064  33  TYR A CA  
245  C C   . TYR A 33  ? 0.78383 0.28195 0.42630 -0.03557 -0.26353 0.02136  33  TYR A C   
246  O O   . TYR A 33  ? 0.82790 0.33091 0.47501 -0.03596 -0.26256 0.02174  33  TYR A O   
247  C CB  . TYR A 33  ? 0.81452 0.30710 0.45730 -0.03296 -0.26878 0.01950  33  TYR A CB  
248  C CG  . TYR A 33  ? 0.78465 0.28044 0.43386 -0.03250 -0.27121 0.01937  33  TYR A CG  
249  C CD1 . TYR A 33  ? 0.79597 0.29657 0.45160 -0.03250 -0.27165 0.01959  33  TYR A CD1 
250  C CD2 . TYR A 33  ? 0.85870 0.35164 0.50678 -0.03206 -0.27359 0.01902  33  TYR A CD2 
251  C CE1 . TYR A 33  ? 0.80537 0.30814 0.46636 -0.03230 -0.27428 0.01965  33  TYR A CE1 
252  C CE2 . TYR A 33  ? 0.83431 0.32942 0.48779 -0.03170 -0.27634 0.01900  33  TYR A CE2 
253  C CZ  . TYR A 33  ? 0.95450 0.45461 0.61459 -0.03190 -0.27669 0.01938  33  TYR A CZ  
254  O OH  . TYR A 33  ? 1.00960 0.51129 0.67459 -0.03180 -0.27965 0.01954  33  TYR A OH  
255  N N   . TRP A 34  ? 0.79609 0.29038 0.43369 -0.03598 -0.26365 0.02142  34  TRP A N   
256  C CA  . TRP A 34  ? 0.78920 0.28481 0.42629 -0.03696 -0.26248 0.02196  34  TRP A CA  
257  C C   . TRP A 34  ? 0.80017 0.29228 0.43509 -0.03646 -0.26449 0.02155  34  TRP A C   
258  O O   . TRP A 34  ? 0.86064 0.34670 0.48904 -0.03646 -0.26523 0.02130  34  TRP A O   
259  C CB  . TRP A 34  ? 0.78698 0.28059 0.41795 -0.03870 -0.25999 0.02274  34  TRP A CB  
260  C CG  . TRP A 34  ? 0.80844 0.29598 0.43172 -0.03927 -0.25971 0.02289  34  TRP A CG  
261  C CD1 . TRP A 34  ? 0.86544 0.34649 0.48070 -0.04004 -0.25990 0.02303  34  TRP A CD1 
262  C CD2 . TRP A 34  ? 0.84978 0.33632 0.47155 -0.03923 -0.25922 0.02298  34  TRP A CD2 
263  N NE1 . TRP A 34  ? 0.89228 0.36834 0.50124 -0.04054 -0.25957 0.02324  34  TRP A NE1 
264  C CE2 . TRP A 34  ? 0.95466 0.43401 0.56751 -0.03997 -0.25920 0.02320  34  TRP A CE2 
265  C CE3 . TRP A 34  ? 0.78045 0.27067 0.40665 -0.03865 -0.25893 0.02287  34  TRP A CE3 
266  C CZ2 . TRP A 34  ? 0.87706 0.35300 0.48560 -0.04004 -0.25896 0.02334  34  TRP A CZ2 
267  C CZ3 . TRP A 34  ? 0.77536 0.26218 0.39722 -0.03863 -0.25873 0.02293  34  TRP A CZ3 
268  C CH2 . TRP A 34  ? 0.75405 0.23393 0.36731 -0.03927 -0.25877 0.02318  34  TRP A CH2 
269  N N   . HIS A 35  ? 0.82077 0.31585 0.46016 -0.03611 -0.26546 0.02148  35  HIS A N   
270  C CA  . HIS A 35  ? 0.79258 0.28379 0.42902 -0.03572 -0.26743 0.02114  35  HIS A CA  
271  C C   . HIS A 35  ? 0.86844 0.35676 0.49821 -0.03700 -0.26541 0.02159  35  HIS A C   
272  O O   . HIS A 35  ? 0.82612 0.31713 0.45782 -0.03733 -0.26465 0.02179  35  HIS A O   
273  C CB  . HIS A 35  ? 0.79613 0.29077 0.43909 -0.03496 -0.26956 0.02096  35  HIS A CB  
274  C CG  . HIS A 35  ? 0.80508 0.30019 0.45282 -0.03386 -0.27292 0.02048  35  HIS A CG  
275  N ND1 . HIS A 35  ? 0.84035 0.33818 0.49233 -0.03355 -0.27316 0.02040  35  HIS A ND1 
276  C CD2 . HIS A 35  ? 0.73698 0.22974 0.38572 -0.03306 -0.27666 0.02004  35  HIS A CD2 
277  C CE1 . HIS A 35  ? 0.89362 0.39068 0.54911 -0.03262 -0.27709 0.01992  35  HIS A CE1 
278  N NE2 . HIS A 35  ? 0.91073 0.40483 0.56452 -0.03234 -0.27937 0.01973  35  HIS A NE2 
279  N N   . TRP A 36  ? 0.84949 0.33180 0.47107 -0.03777 -0.26480 0.02172  36  TRP A N   
280  C CA  . TRP A 36  ? 0.86845 0.34654 0.48216 -0.03934 -0.26327 0.02221  36  TRP A CA  
281  C C   . TRP A 36  ? 0.86127 0.33090 0.46626 -0.03929 -0.26484 0.02186  36  TRP A C   
282  O O   . TRP A 36  ? 0.92792 0.39394 0.53023 -0.03885 -0.26579 0.02158  36  TRP A O   
283  C CB  . TRP A 36  ? 0.82124 0.29931 0.43179 -0.04108 -0.26080 0.02300  36  TRP A CB  
284  C CG  . TRP A 36  ? 0.80872 0.28292 0.41187 -0.04308 -0.25955 0.02357  36  TRP A CG  
285  C CD1 . TRP A 36  ? 0.82863 0.30421 0.43249 -0.04340 -0.25942 0.02353  36  TRP A CD1 
286  C CD2 . TRP A 36  ? 0.82975 0.29725 0.42293 -0.04522 -0.25853 0.02426  36  TRP A CD2 
287  N NE1 . TRP A 36  ? 0.96200 0.43208 0.55704 -0.04560 -0.25859 0.02406  36  TRP A NE1 
288  C CE2 . TRP A 36  ? 0.86192 0.32699 0.45016 -0.04697 -0.25795 0.02461  36  TRP A CE2 
289  C CE3 . TRP A 36  ? 0.82089 0.28351 0.40821 -0.04591 -0.25827 0.02458  36  TRP A CE3 
290  C CZ2 . TRP A 36  ? 0.91221 0.37012 0.48973 -0.04975 -0.25711 0.02537  36  TRP A CZ2 
291  C CZ3 . TRP A 36  ? 0.82848 0.28413 0.40519 -0.04858 -0.25726 0.02541  36  TRP A CZ3 
292  C CH2 . TRP A 36  ? 0.91758 0.37092 0.48941 -0.05066 -0.25667 0.02584  36  TRP A CH2 
293  N N   . GLY A 37  ? 0.87334 0.33924 0.47339 -0.03965 -0.26526 0.02179  37  GLY A N   
294  C CA  . GLY A 37  ? 0.87683 0.33373 0.46757 -0.03956 -0.26698 0.02141  37  GLY A CA  
295  C C   . GLY A 37  ? 0.88956 0.34271 0.47511 -0.03990 -0.26738 0.02129  37  GLY A C   
296  O O   . GLY A 37  ? 0.87587 0.33288 0.46408 -0.04045 -0.26603 0.02154  37  GLY A O   
297  N N   . ALA A 38  ? 0.86020 0.30503 0.43748 -0.03954 -0.26936 0.02082  38  ALA A N   
298  C CA  . ALA A 38  ? 0.95719 0.39682 0.52788 -0.03968 -0.27009 0.02055  38  ALA A CA  
299  C C   . ALA A 38  ? 0.87987 0.32579 0.45944 -0.03823 -0.27137 0.02011  38  ALA A C   
300  O O   . ALA A 38  ? 0.93133 0.37539 0.50760 -0.03846 -0.27116 0.01996  38  ALA A O   
301  C CB  . ALA A 38  ? 0.98642 0.41597 0.54729 -0.03918 -0.27255 0.02001  38  ALA A CB  
302  N N   . PHE A 39  ? 0.82249 0.27516 0.41252 -0.03690 -0.27273 0.01990  39  PHE A N   
303  C CA  . PHE A 39  ? 0.86712 0.32565 0.46575 -0.03577 -0.27407 0.01962  39  PHE A CA  
304  C C   . PHE A 39  ? 0.81802 0.28286 0.42145 -0.03640 -0.27146 0.02001  39  PHE A C   
305  O O   . PHE A 39  ? 0.91310 0.38174 0.52217 -0.03559 -0.27242 0.01978  39  PHE A O   
306  C CB  . PHE A 39  ? 0.81075 0.27463 0.41890 -0.03468 -0.27604 0.01948  39  PHE A CB  
307  C CG  . PHE A 39  ? 0.90529 0.37333 0.51768 -0.03502 -0.27440 0.01984  39  PHE A CG  
308  C CD1 . PHE A 39  ? 0.90082 0.37647 0.52029 -0.03548 -0.27194 0.02034  39  PHE A CD1 
309  C CD2 . PHE A 39  ? 0.89191 0.35558 0.50076 -0.03469 -0.27570 0.01955  39  PHE A CD2 
310  C CE1 . PHE A 39  ? 0.93300 0.41166 0.55553 -0.03570 -0.27066 0.02059  39  PHE A CE1 
311  C CE2 . PHE A 39  ? 1.01896 0.48572 0.63107 -0.03483 -0.27444 0.01973  39  PHE A CE2 
312  C CZ  . PHE A 39  ? 0.94670 0.42092 0.56556 -0.03536 -0.27188 0.02027  39  PHE A CZ  
313  N N   . THR A 40  ? 0.83131 0.29653 0.43207 -0.03784 -0.26866 0.02057  40  THR A N   
314  C CA  . THR A 40  ? 0.80554 0.27635 0.41072 -0.03844 -0.26663 0.02090  40  THR A CA  
315  C C   . THR A 40  ? 0.81684 0.28212 0.41373 -0.03926 -0.26628 0.02074  40  THR A C   
316  O O   . THR A 40  ? 1.01288 0.48132 0.61268 -0.03926 -0.26572 0.02065  40  THR A O   
317  C CB  . THR A 40  ? 0.84527 0.31943 0.45247 -0.03961 -0.26439 0.02159  40  THR A CB  
318  O OG1 . THR A 40  ? 0.85038 0.32772 0.46325 -0.03873 -0.26506 0.02157  40  THR A OG1 
319  C CG2 . THR A 40  ? 0.77786 0.25778 0.39021 -0.04007 -0.26288 0.02186  40  THR A CG2 
320  N N   . THR A 41  ? 0.84525 0.30182 0.43171 -0.03980 -0.26697 0.02059  41  THR A N   
321  C CA  . THR A 41  ? 0.84243 0.29192 0.41875 -0.04092 -0.26663 0.02046  41  THR A CA  
322  C C   . THR A 41  ? 0.86038 0.31111 0.43913 -0.03955 -0.26787 0.01968  41  THR A C   
323  O O   . THR A 41  ? 0.82148 0.27115 0.39751 -0.04030 -0.26722 0.01960  41  THR A O   
324  C CB  . THR A 41  ? 0.95866 0.39764 0.52267 -0.04156 -0.26740 0.02037  41  THR A CB  
325  O OG1 . THR A 41  ? 0.96952 0.40848 0.53391 -0.04193 -0.26705 0.02084  41  THR A OG1 
326  C CG2 . THR A 41  ? 1.03847 0.46887 0.58986 -0.04369 -0.26635 0.02058  41  THR A CG2 
327  N N   . PRO A 42  ? 0.92647 0.37841 0.50933 -0.03765 -0.27001 0.01905  42  PRO A N   
328  C CA  . PRO A 42  ? 0.88580 0.33788 0.46998 -0.03629 -0.27141 0.01826  42  PRO A CA  
329  C C   . PRO A 42  ? 1.04038 0.50104 0.63428 -0.03603 -0.27034 0.01841  42  PRO A C   
330  O O   . PRO A 42  ? 1.08685 0.54624 0.67898 -0.03564 -0.27063 0.01788  42  PRO A O   
331  C CB  . PRO A 42  ? 0.89445 0.34656 0.48187 -0.03476 -0.27407 0.01785  42  PRO A CB  
332  C CG  . PRO A 42  ? 0.85647 0.30497 0.44015 -0.03528 -0.27450 0.01817  42  PRO A CG  
333  C CD  . PRO A 42  ? 0.89796 0.35047 0.48398 -0.03674 -0.27169 0.01902  42  PRO A CD  
334  N N   . GLN A 43  ? 0.95509 0.42336 0.55809 -0.03620 -0.26931 0.01905  43  GLN A N   
335  C CA  . GLN A 43  ? 0.91318 0.38913 0.52486 -0.03604 -0.26824 0.01926  43  GLN A CA  
336  C C   . GLN A 43  ? 0.96911 0.44695 0.58530 -0.03439 -0.27008 0.01862  43  GLN A C   
337  O O   . GLN A 43  ? 0.97908 0.45839 0.59688 -0.03390 -0.27006 0.01826  43  GLN A O   
338  C CB  . GLN A 43  ? 0.89138 0.36614 0.49934 -0.03729 -0.26684 0.01942  43  GLN A CB  
339  C CG  . GLN A 43  ? 0.85547 0.33082 0.46208 -0.03914 -0.26492 0.02033  43  GLN A CG  
340  C CD  . GLN A 43  ? 0.88521 0.35915 0.48829 -0.04072 -0.26413 0.02060  43  GLN A CD  
341  O OE1 . GLN A 43  ? 0.91074 0.38578 0.51356 -0.04234 -0.26276 0.02138  43  GLN A OE1 
342  N NE2 . GLN A 43  ? 0.95269 0.42588 0.55383 -0.04032 -0.26475 0.01931  43  GLN A NE2 
343  N N   . TYR A 44  ? 0.92355 0.40075 0.54133 -0.03361 -0.27198 0.01849  44  TYR A N   
344  C CA  . TYR A 44  ? 0.95812 0.43642 0.57969 -0.03233 -0.27412 0.01802  44  TYR A CA  
345  C C   . TYR A 44  ? 0.89446 0.37621 0.52252 -0.03226 -0.27557 0.01849  44  TYR A C   
346  O O   . TYR A 44  ? 0.83684 0.31709 0.46365 -0.03266 -0.27602 0.01874  44  TYR A O   
347  C CB  . TYR A 44  ? 0.90100 0.37105 0.51372 -0.03147 -0.27614 0.01708  44  TYR A CB  
348  C CG  . TYR A 44  ? 0.93294 0.40210 0.54703 -0.03008 -0.27852 0.01640  44  TYR A CG  
349  C CD1 . TYR A 44  ? 0.90258 0.37086 0.51864 -0.02965 -0.28128 0.01640  44  TYR A CD1 
350  C CD2 . TYR A 44  ? 1.04870 0.51703 0.66146 -0.02919 -0.27847 0.01569  44  TYR A CD2 
351  C CE1 . TYR A 44  ? 1.00009 0.46679 0.61663 -0.02858 -0.28369 0.01583  44  TYR A CE1 
352  C CE2 . TYR A 44  ? 1.01995 0.48663 0.63315 -0.02779 -0.28084 0.01497  44  TYR A CE2 
353  C CZ  . TYR A 44  ? 1.06190 0.52774 0.67683 -0.02759 -0.28334 0.01510  44  TYR A CZ  
354  O OH  . TYR A 44  ? 0.98295 0.44649 0.59765 -0.02641 -0.28589 0.01445  44  TYR A OH  
355  N N   . ALA A 45  ? 0.83404 0.31992 0.46864 -0.03182 -0.27655 0.01861  45  ALA A N   
356  C CA  . ALA A 45  ? 0.84584 0.33425 0.48631 -0.03197 -0.27867 0.01910  45  ALA A CA  
357  C C   . ALA A 45  ? 0.86154 0.35407 0.50623 -0.03276 -0.27723 0.01978  45  ALA A C   
358  O O   . ALA A 45  ? 1.03655 0.53426 0.68584 -0.03317 -0.27509 0.02021  45  ALA A O   
359  C CB  . ALA A 45  ? 0.88265 0.36499 0.51882 -0.03151 -0.28214 0.01868  45  ALA A CB  
360  N N   . SER A 46  ? 0.99322 0.48321 0.63678 -0.03280 -0.27907 0.01981  46  SER A N   
361  C CA  . SER A 46  ? 0.86252 0.35568 0.51002 -0.03327 -0.27845 0.02028  46  SER A CA  
362  C C   . SER A 46  ? 0.88747 0.37598 0.52872 -0.03331 -0.27811 0.02002  46  SER A C   
363  O O   . SER A 46  ? 0.95187 0.43488 0.58548 -0.03322 -0.27795 0.01960  46  SER A O   
364  C CB  . SER A 46  ? 0.87593 0.37042 0.52906 -0.03322 -0.28189 0.02056  46  SER A CB  
365  O OG  . SER A 46  ? 0.97079 0.45954 0.62025 -0.03275 -0.28563 0.02013  46  SER A OG  
366  N N   . GLU A 47  ? 0.88970 0.37986 0.53355 -0.03347 -0.27806 0.02025  47  GLU A N   
367  C CA  . GLU A 47  ? 0.93028 0.41530 0.56804 -0.03341 -0.27834 0.01996  47  GLU A CA  
368  C C   . GLU A 47  ? 0.93571 0.41465 0.56997 -0.03267 -0.28256 0.01943  47  GLU A C   
369  O O   . GLU A 47  ? 0.94483 0.41749 0.57167 -0.03252 -0.28317 0.01906  47  GLU A O   
370  C CB  . GLU A 47  ? 0.84859 0.33641 0.49023 -0.03346 -0.27796 0.02015  47  GLU A CB  
371  C CG  . GLU A 47  ? 0.94400 0.43433 0.59282 -0.03295 -0.28138 0.02015  47  GLU A CG  
372  C CD  . GLU A 47  ? 0.92214 0.41886 0.57847 -0.03336 -0.28074 0.02071  47  GLU A CD  
373  O OE1 . GLU A 47  ? 0.92330 0.42274 0.57960 -0.03381 -0.27769 0.02098  47  GLU A OE1 
374  O OE2 . GLU A 47  ? 0.92077 0.41914 0.58258 -0.03325 -0.28366 0.02088  47  GLU A OE2 
375  N N   . TRP A 48  ? 0.85658 0.33676 0.49541 -0.03233 -0.28554 0.01943  48  TRP A N   
376  C CA  . TRP A 48  ? 0.86277 0.33695 0.49865 -0.03168 -0.29031 0.01894  48  TRP A CA  
377  C C   . TRP A 48  ? 0.82913 0.29790 0.45752 -0.03147 -0.29041 0.01850  48  TRP A C   
378  O O   . TRP A 48  ? 0.94940 0.41356 0.57577 -0.03097 -0.29443 0.01812  48  TRP A O   
379  C CB  . TRP A 48  ? 0.80495 0.28223 0.44886 -0.03169 -0.29408 0.01924  48  TRP A CB  
380  C CG  . TRP A 48  ? 0.87499 0.35413 0.52407 -0.03156 -0.29617 0.01935  48  TRP A CG  
381  C CD1 . TRP A 48  ? 0.89212 0.37351 0.54204 -0.03156 -0.29372 0.01938  48  TRP A CD1 
382  C CD2 . TRP A 48  ? 0.89987 0.37805 0.55368 -0.03140 -0.30180 0.01937  48  TRP A CD2 
383  N NE1 . TRP A 48  ? 0.96998 0.45181 0.62466 -0.03119 -0.29734 0.01929  48  TRP A NE1 
384  C CE2 . TRP A 48  ? 0.89018 0.37016 0.54756 -0.03113 -0.30246 0.01932  48  TRP A CE2 
385  C CE3 . TRP A 48  ? 0.83740 0.31291 0.49254 -0.03149 -0.30673 0.01941  48  TRP A CE3 
386  C CZ2 . TRP A 48  ? 0.86161 0.34089 0.52411 -0.03090 -0.30804 0.01928  48  TRP A CZ2 
387  C CZ3 . TRP A 48  ? 0.84464 0.31956 0.50501 -0.03149 -0.31227 0.01951  48  TRP A CZ3 
388  C CH2 . TRP A 48  ? 0.83050 0.30736 0.49468 -0.03116 -0.31299 0.01944  48  TRP A CH2 
389  N N   . TYR A 49  ? 0.83349 0.30215 0.45748 -0.03184 -0.28655 0.01851  49  TYR A N   
390  C CA  . TYR A 49  ? 0.86578 0.32797 0.48115 -0.03154 -0.28681 0.01794  49  TYR A CA  
391  C C   . TYR A 49  ? 0.93229 0.38526 0.53864 -0.03110 -0.28963 0.01739  49  TYR A C   
392  O O   . TYR A 49  ? 0.95496 0.40211 0.55636 -0.03050 -0.29246 0.01682  49  TYR A O   
393  C CB  . TYR A 49  ? 0.78452 0.24729 0.39607 -0.03213 -0.28265 0.01803  49  TYR A CB  
394  C CG  . TYR A 49  ? 0.91421 0.37031 0.51662 -0.03185 -0.28266 0.01739  49  TYR A CG  
395  C CD1 . TYR A 49  ? 0.95746 0.40474 0.54860 -0.03204 -0.28288 0.01704  49  TYR A CD1 
396  C CD2 . TYR A 49  ? 0.88445 0.34245 0.48870 -0.03138 -0.28236 0.01710  49  TYR A CD2 
397  C CE1 . TYR A 49  ? 0.97678 0.41708 0.55855 -0.03181 -0.28293 0.01640  49  TYR A CE1 
398  C CE2 . TYR A 49  ? 0.95407 0.40531 0.54944 -0.03092 -0.28260 0.01634  49  TYR A CE2 
399  C CZ  . TYR A 49  ? 0.94830 0.39061 0.53229 -0.03117 -0.28285 0.01599  49  TYR A CZ  
400  O OH  . TYR A 49  ? 0.90673 0.34375 0.48203 -0.03085 -0.28251 0.01462  49  TYR A OH  
401  N N   . PRO A 50  ? 0.97369 0.42429 0.57687 -0.03132 -0.28917 0.01746  50  PRO A N   
402  C CA  . PRO A 50  ? 0.87651 0.31767 0.47068 -0.03079 -0.29225 0.01689  50  PRO A CA  
403  C C   . PRO A 50  ? 0.89744 0.33569 0.49330 -0.02981 -0.29777 0.01640  50  PRO A C   
404  O O   . PRO A 50  ? 0.87078 0.30063 0.45789 -0.02931 -0.30018 0.01580  50  PRO A O   
405  C CB  . PRO A 50  ? 0.92852 0.37029 0.52354 -0.03095 -0.29170 0.01708  50  PRO A CB  
406  C CG  . PRO A 50  ? 0.91971 0.37168 0.52505 -0.03152 -0.28864 0.01774  50  PRO A CG  
407  C CD  . PRO A 50  ? 0.94557 0.40128 0.55236 -0.03205 -0.28585 0.01802  50  PRO A CD  
408  N N   . ARG A 51  ? 0.80094 0.24557 0.40732 -0.02971 -0.29977 0.01670  51  ARG A N   
409  C CA  . ARG A 51  ? 0.91489 0.35714 0.52386 -0.02913 -0.30551 0.01641  51  ARG A CA  
410  C C   . ARG A 51  ? 0.85921 0.30114 0.46776 -0.02921 -0.30593 0.01634  51  ARG A C   
411  O O   . ARG A 51  ? 0.95204 0.38589 0.55302 -0.02863 -0.30914 0.01567  51  ARG A O   
412  C CB  . ARG A 51  ? 0.81072 0.25987 0.43105 -0.02933 -0.30744 0.01690  51  ARG A CB  
413  C CG  . ARG A 51  ? 0.87301 0.32206 0.49840 -0.02937 -0.31267 0.01698  51  ARG A CG  
414  C CD  . ARG A 51  ? 0.84732 0.30239 0.48294 -0.02972 -0.31453 0.01753  51  ARG A CD  
415  N NE  . ARG A 51  ? 0.94360 0.39914 0.58516 -0.03019 -0.31975 0.01787  51  ARG A NE  
416  C CZ  . ARG A 51  ? 0.90871 0.36177 0.55161 -0.02991 -0.32577 0.01701  51  ARG A CZ  
417  N NH1 . ARG A 51  ? 0.92297 0.37186 0.56100 -0.02881 -0.32757 0.01588  51  ARG A NH1 
418  N NH2 . ARG A 51  ? 0.88601 0.34387 0.53616 -0.03097 -0.32929 0.01660  51  ARG A NH2 
419  N N   . ASN A 52  ? 0.87215 0.32166 0.48741 -0.02980 -0.30285 0.01690  52  ASN A N   
420  C CA  . ASN A 52  ? 0.86818 0.31770 0.48395 -0.02977 -0.30364 0.01680  52  ASN A CA  
421  C C   . ASN A 52  ? 0.95094 0.39333 0.55584 -0.02919 -0.30246 0.01601  52  ASN A C   
422  O O   . ASN A 52  ? 1.08200 0.52144 0.68487 -0.02881 -0.30457 0.01553  52  ASN A O   
423  C CB  . ASN A 52  ? 0.85272 0.31153 0.47786 -0.03043 -0.30086 0.01756  52  ASN A CB  
424  C CG  . ASN A 52  ? 0.89760 0.36196 0.53232 -0.03105 -0.30277 0.01831  52  ASN A CG  
425  O OD1 . ASN A 52  ? 1.04693 0.50899 0.68392 -0.03117 -0.30786 0.01837  52  ASN A OD1 
426  N ND2 . ASN A 52  ? 0.81850 0.28967 0.45866 -0.03151 -0.29916 0.01889  52  ASN A ND2 
427  N N   . MET A 53  ? 0.91039 0.34953 0.50801 -0.02921 -0.29948 0.01581  53  MET A N   
428  C CA  . MET A 53  ? 0.98028 0.41205 0.56694 -0.02878 -0.29850 0.01505  53  MET A CA  
429  C C   . MET A 53  ? 1.01885 0.44595 0.59954 -0.02828 -0.30186 0.01297  53  MET A C   
430  O O   . MET A 53  ? 0.98323 0.40741 0.55657 -0.02799 -0.30079 0.01122  53  MET A O   
431  C CB  . MET A 53  ? 0.89683 0.32533 0.47579 -0.02931 -0.29500 0.01513  53  MET A CB  
432  C CG  . MET A 53  ? 0.97252 0.39474 0.54552 -0.02929 -0.29694 0.01504  53  MET A CG  
433  S SD  . MET A 53  ? 1.00983 0.42599 0.57129 -0.03024 -0.29314 0.01518  53  MET A SD  
434  C CE  . MET A 53  ? 1.08251 0.49323 0.63180 -0.03004 -0.29236 0.01283  53  MET A CE  
435  N N   . TYR A 54  ? 1.01299 0.43935 0.59641 -0.02817 -0.30584 0.01293  54  TYR A N   
436  C CA  . TYR A 54  ? 1.07043 0.49246 0.64825 -0.02774 -0.30960 0.01083  54  TYR A CA  
437  C C   . TYR A 54  ? 0.99404 0.42037 0.58027 -0.02798 -0.31352 0.01034  54  TYR A C   
438  O O   . TYR A 54  ? 1.10576 0.52946 0.68858 -0.02783 -0.31695 0.00839  54  TYR A O   
439  C CB  . TYR A 54  ? 1.04383 0.46118 0.61720 -0.02742 -0.31193 0.01067  54  TYR A CB  
440  C CG  . TYR A 54  ? 1.09092 0.50261 0.65492 -0.02746 -0.30881 0.01113  54  TYR A CG  
441  C CD1 . TYR A 54  ? 1.07589 0.48082 0.62719 -0.02730 -0.30767 0.00965  54  TYR A CD1 
442  C CD2 . TYR A 54  ? 1.04726 0.45960 0.61435 -0.02777 -0.30742 0.01286  54  TYR A CD2 
443  C CE1 . TYR A 54  ? 1.18589 0.58509 0.72787 -0.02768 -0.30494 0.01011  54  TYR A CE1 
444  C CE2 . TYR A 54  ? 0.95007 0.35654 0.50808 -0.02812 -0.30484 0.01324  54  TYR A CE2 
445  C CZ  . TYR A 54  ? 1.08716 0.48704 0.63254 -0.02817 -0.30360 0.01196  54  TYR A CZ  
446  O OH  . TYR A 54  ? 1.05460 0.44817 0.59025 -0.02883 -0.30108 0.01239  54  TYR A OH  
447  N N   . GLU A 55  ? 0.93894 0.37150 0.53561 -0.02851 -0.31328 0.01203  55  GLU A N   
448  C CA  . GLU A 55  ? 0.95104 0.38793 0.55605 -0.02919 -0.31688 0.01177  55  GLU A CA  
449  C C   . GLU A 55  ? 1.03072 0.46573 0.63136 -0.02915 -0.31715 0.00984  55  GLU A C   
450  O O   . GLU A 55  ? 1.07059 0.50505 0.66779 -0.02871 -0.31354 0.00984  55  GLU A O   
451  C CB  . GLU A 55  ? 1.03124 0.47430 0.64610 -0.02982 -0.31554 0.01399  55  GLU A CB  
452  C CG  . GLU A 55  ? 0.98301 0.43069 0.60721 -0.03094 -0.31953 0.01412  55  GLU A CG  
453  C CD  . GLU A 55  ? 1.10689 0.56005 0.73974 -0.03161 -0.31814 0.01643  55  GLU A CD  
454  O OE1 . GLU A 55  ? 1.16518 0.61871 0.79664 -0.03110 -0.31398 0.01773  55  GLU A OE1 
455  O OE2 . GLU A 55  ? 1.08209 0.53911 0.72281 -0.03273 -0.32137 0.01677  55  GLU A OE2 
456  N N   . PRO A 56  ? 1.15740 0.59123 0.75779 -0.02958 -0.32151 0.00790  56  PRO A N   
457  C CA  . PRO A 56  ? 1.01945 0.45082 0.61536 -0.02963 -0.32210 0.00566  56  PRO A CA  
458  C C   . PRO A 56  ? 0.97857 0.41386 0.58050 -0.03013 -0.32072 0.00651  56  PRO A C   
459  O O   . PRO A 56  ? 1.04065 0.48074 0.65188 -0.03129 -0.32266 0.00773  56  PRO A O   
460  C CB  . PRO A 56  ? 0.97523 0.40588 0.57233 -0.03046 -0.32769 0.00370  56  PRO A CB  
461  C CG  . PRO A 56  ? 0.92403 0.35477 0.52220 -0.03019 -0.32959 0.00445  56  PRO A CG  
462  C CD  . PRO A 56  ? 1.06970 0.50431 0.67377 -0.03006 -0.32636 0.00735  56  PRO A CD  
463  N N   . GLY A 57  ? 0.97169 0.40470 0.56788 -0.02924 -0.31747 0.00571  57  GLY A N   
464  C CA  . GLY A 57  ? 1.05640 0.49204 0.65675 -0.02937 -0.31638 0.00615  57  GLY A CA  
465  C C   . GLY A 57  ? 1.05101 0.49163 0.65801 -0.02934 -0.31371 0.00911  57  GLY A C   
466  O O   . GLY A 57  ? 1.07027 0.51347 0.68184 -0.02962 -0.31361 0.00984  57  GLY A O   
467  N N   . SER A 58  ? 1.03100 0.47222 0.63738 -0.02897 -0.31137 0.01060  58  SER A N   
468  C CA  . SER A 58  ? 0.91805 0.36368 0.53019 -0.02900 -0.30865 0.01326  58  SER A CA  
469  C C   . SER A 58  ? 0.94980 0.39514 0.55807 -0.02801 -0.30471 0.01301  58  SER A C   
470  O O   . SER A 58  ? 0.99167 0.43299 0.59173 -0.02726 -0.30341 0.01092  58  SER A O   
471  C CB  . SER A 58  ? 0.95166 0.39746 0.56430 -0.02913 -0.30780 0.01456  58  SER A CB  
472  O OG  . SER A 58  ? 0.91371 0.35573 0.51789 -0.02846 -0.30482 0.01377  58  SER A OG  
473  N N   . ASP A 59  ? 0.80994 0.25932 0.42370 -0.02802 -0.30300 0.01490  59  ASP A N   
474  C CA  . ASP A 59  ? 0.86838 0.31810 0.47912 -0.02707 -0.29939 0.01456  59  ASP A CA  
475  C C   . ASP A 59  ? 0.91665 0.36509 0.52257 -0.02710 -0.29637 0.01449  59  ASP A C   
476  O O   . ASP A 59  ? 0.95302 0.39982 0.55297 -0.02651 -0.29388 0.01290  59  ASP A O   
477  C CB  . ASP A 59  ? 0.83811 0.29600 0.45746 -0.02749 -0.29719 0.01539  59  ASP A CB  
478  C CG  . ASP A 59  ? 1.04389 0.50376 0.66182 -0.02675 -0.29338 0.01492  59  ASP A CG  
479  O OD1 . ASP A 59  ? 1.04875 0.50321 0.66031 -0.02535 -0.29405 0.01376  59  ASP A OD1 
480  O OD2 . ASP A 59  ? 1.05296 0.51913 0.67577 -0.02752 -0.29014 0.01564  59  ASP A OD2 
481  N N   . GLN A 60  ? 0.88039 0.33160 0.48962 -0.02807 -0.29596 0.01529  60  GLN A N   
482  C CA  . GLN A 60  ? 0.96943 0.41887 0.57354 -0.02835 -0.29329 0.01527  60  GLN A CA  
483  C C   . GLN A 60  ? 1.02983 0.47099 0.62261 -0.02777 -0.29421 0.01353  60  GLN A C   
484  O O   . GLN A 60  ? 0.96668 0.40622 0.55312 -0.02780 -0.29118 0.01259  60  GLN A O   
485  C CB  . GLN A 60  ? 0.86083 0.31480 0.47100 -0.02928 -0.29321 0.01617  60  GLN A CB  
486  C CG  . GLN A 60  ? 0.87459 0.33841 0.49573 -0.03000 -0.29121 0.01710  60  GLN A CG  
487  C CD  . GLN A 60  ? 0.96207 0.42848 0.59030 -0.03031 -0.29466 0.01759  60  GLN A CD  
488  O OE1 . GLN A 60  ? 1.01559 0.47800 0.64182 -0.02993 -0.29789 0.01721  60  GLN A OE1 
489  N NE2 . GLN A 60  ? 0.90343 0.37578 0.53938 -0.03110 -0.29435 0.01844  60  GLN A NE2 
490  N N   . ARG A 61  ? 0.99857 0.43694 0.58979 -0.02759 -0.29766 0.01236  61  ARG A N   
491  C CA  . ARG A 61  ? 0.94751 0.37988 0.52837 -0.02720 -0.29802 0.00987  61  ARG A CA  
492  C C   . ARG A 61  ? 1.01163 0.44326 0.58780 -0.02650 -0.29577 0.00785  61  ARG A C   
493  O O   . ARG A 61  ? 0.95124 0.37897 0.51823 -0.02639 -0.29359 0.00620  61  ARG A O   
494  C CB  . ARG A 61  ? 1.00351 0.43361 0.58441 -0.02718 -0.30253 0.00874  61  ARG A CB  
495  C CG  . ARG A 61  ? 0.97442 0.39829 0.54480 -0.02668 -0.30338 0.00580  61  ARG A CG  
496  C CD  . ARG A 61  ? 0.98513 0.40779 0.55717 -0.02689 -0.30824 0.00466  61  ARG A CD  
497  N NE  . ARG A 61  ? 0.95546 0.37655 0.52745 -0.02722 -0.31110 0.00518  61  ARG A NE  
498  C CZ  . ARG A 61  ? 1.11544 0.53087 0.67802 -0.02690 -0.31100 0.00432  61  ARG A CZ  
499  N NH1 . ARG A 61  ? 1.12783 0.53832 0.67971 -0.02643 -0.30848 0.00258  61  ARG A NH1 
500  N NH2 . ARG A 61  ? 0.99183 0.40618 0.55523 -0.02700 -0.31365 0.00499  61  ARG A NH2 
501  N N   . LYS A 62  ? 0.98793 0.42290 0.56995 -0.02604 -0.29639 0.00789  62  LYS A N   
502  C CA  . LYS A 62  ? 0.87394 0.30799 0.45177 -0.02507 -0.29453 0.00567  62  LYS A CA  
503  C C   . LYS A 62  ? 0.99618 0.43213 0.57225 -0.02520 -0.29047 0.00587  62  LYS A C   
504  O O   . LYS A 62  ? 1.05106 0.48425 0.61937 -0.02482 -0.28839 0.00343  62  LYS A O   
505  C CB  . LYS A 62  ? 0.90209 0.33883 0.48644 -0.02450 -0.29622 0.00587  62  LYS A CB  
506  C CG  . LYS A 62  ? 1.14482 0.58060 0.72573 -0.02315 -0.29463 0.00352  62  LYS A CG  
507  C CD  . LYS A 62  ? 1.13162 0.56929 0.71862 -0.02256 -0.29663 0.00403  62  LYS A CD  
508  N N   . HIS A 63  ? 1.09227 0.53290 0.67533 -0.02589 -0.28934 0.00854  63  HIS A N   
509  C CA  . HIS A 63  ? 1.06563 0.50851 0.64761 -0.02639 -0.28571 0.00871  63  HIS A CA  
510  C C   . HIS A 63  ? 1.00709 0.44577 0.58003 -0.02733 -0.28392 0.00790  63  HIS A C   
511  O O   . HIS A 63  ? 1.08876 0.52682 0.65600 -0.02766 -0.28118 0.00617  63  HIS A O   
512  C CB  . HIS A 63  ? 0.99956 0.44760 0.59035 -0.02708 -0.28514 0.01169  63  HIS A CB  
513  C CG  . HIS A 63  ? 1.00051 0.45087 0.59037 -0.02803 -0.28171 0.01198  63  HIS A CG  
514  N ND1 . HIS A 63  ? 1.08473 0.53832 0.67566 -0.02771 -0.27986 0.01080  63  HIS A ND1 
515  C CD2 . HIS A 63  ? 1.02678 0.47649 0.61454 -0.02941 -0.28005 0.01316  63  HIS A CD2 
516  C CE1 . HIS A 63  ? 1.05546 0.51092 0.64537 -0.02908 -0.27718 0.01118  63  HIS A CE1 
517  N NE2 . HIS A 63  ? 1.04014 0.49303 0.62782 -0.03017 -0.27716 0.01271  63  HIS A NE2 
518  N N   . HIS A 64  ? 0.95718 0.39263 0.52832 -0.02784 -0.28562 0.00897  64  HIS A N   
519  C CA  . HIS A 64  ? 1.09307 0.52327 0.65459 -0.02871 -0.28430 0.00843  64  HIS A CA  
520  C C   . HIS A 64  ? 1.09705 0.52201 0.64795 -0.02822 -0.28382 0.00524  64  HIS A C   
521  O O   . HIS A 64  ? 1.01653 0.43847 0.55879 -0.02906 -0.28112 0.00405  64  HIS A O   
522  C CB  . HIS A 64  ? 1.05639 0.48361 0.61828 -0.02895 -0.28700 0.00995  64  HIS A CB  
523  C CG  . HIS A 64  ? 1.15567 0.57726 0.70845 -0.02993 -0.28573 0.01013  64  HIS A CG  
524  N ND1 . HIS A 64  ? 1.14146 0.56402 0.69491 -0.03116 -0.28340 0.01187  64  HIS A ND1 
525  C CD2 . HIS A 64  ? 1.17326 0.58752 0.71529 -0.02992 -0.28659 0.00878  64  HIS A CD2 
526  C CE1 . HIS A 64  ? 1.11205 0.52780 0.65544 -0.03195 -0.28289 0.01169  64  HIS A CE1 
527  N NE2 . HIS A 64  ? 1.13183 0.54240 0.66802 -0.03116 -0.28478 0.00985  64  HIS A NE2 
528  N N   . THR A 65  ? 1.04082 0.46433 0.59174 -0.02701 -0.28640 0.00366  65  THR A N   
529  C CA  . THR A 65  ? 0.97209 0.39011 0.51258 -0.02637 -0.28605 0.00029  65  THR A CA  
530  C C   . THR A 65  ? 1.07122 0.49099 0.60961 -0.02603 -0.28291 -0.00191 65  THR A C   
531  O O   . THR A 65  ? 1.20742 0.62291 0.73550 -0.02625 -0.28071 -0.00443 65  THR A O   
532  C CB  . THR A 65  ? 1.02564 0.44179 0.56725 -0.02528 -0.28978 -0.00097 65  THR A CB  
533  O OG1 . THR A 65  ? 1.08598 0.50060 0.62926 -0.02572 -0.29298 0.00060  65  THR A OG1 
534  C CG2 . THR A 65  ? 1.06791 0.47782 0.59819 -0.02449 -0.28937 -0.00478 65  THR A CG2 
535  N N   . GLU A 66  ? 1.08587 0.51166 0.63357 -0.02547 -0.28274 -0.00119 66  GLU A N   
536  C CA  . GLU A 66  ? 1.15674 0.58457 0.70346 -0.02492 -0.28029 -0.00353 66  GLU A CA  
537  C C   . GLU A 66  ? 1.12631 0.55645 0.67123 -0.02656 -0.27681 -0.00317 66  GLU A C   
538  O O   . GLU A 66  ? 1.00298 0.43337 0.54382 -0.02651 -0.27453 -0.00600 66  GLU A O   
539  C CB  . GLU A 66  ? 1.16383 0.59669 0.72066 -0.02368 -0.28168 -0.00279 66  GLU A CB  
540  C CG  . GLU A 66  ? 1.32460 0.75483 0.88243 -0.02225 -0.28498 -0.00370 66  GLU A CG  
541  C CD  . GLU A 66  ? 1.43409 0.86854 1.00136 -0.02131 -0.28655 -0.00238 66  GLU A CD  
542  O OE1 . GLU A 66  ? 1.25845 0.69796 0.83162 -0.02163 -0.28514 -0.00071 66  GLU A OE1 
543  O OE2 . GLU A 66  ? 1.50725 0.93958 1.07556 -0.02037 -0.28928 -0.00306 66  GLU A OE2 
544  N N   . THR A 67  ? 1.14268 0.57404 0.68995 -0.02811 -0.27643 -0.00010 67  THR A N   
545  C CA  . THR A 67  ? 1.05916 0.49283 0.60511 -0.03004 -0.27325 0.00039  67  THR A CA  
546  C C   . THR A 67  ? 1.04873 0.47596 0.58321 -0.03168 -0.27180 0.00009  67  THR A C   
547  O O   . THR A 67  ? 0.98460 0.41063 0.51193 -0.03298 -0.26893 -0.00204 67  THR A O   
548  C CB  . THR A 67  ? 1.06364 0.50302 0.62010 -0.03066 -0.27355 0.00387  67  THR A CB  
549  O OG1 . THR A 67  ? 1.07548 0.51883 0.64093 -0.02895 -0.27555 0.00429  67  THR A OG1 
550  C CG2 . THR A 67  ? 1.05024 0.49366 0.60759 -0.03247 -0.27057 0.00394  67  THR A CG2 
551  N N   . TYR A 68  ? 1.21253 0.38518 0.53097 0.00001  -0.22615 -0.06380 68  TYR A N   
552  C CA  . TYR A 68  ? 1.29409 0.46577 0.59989 -0.00578 -0.22105 -0.06503 68  TYR A CA  
553  C C   . TYR A 68  ? 1.31000 0.46730 0.59658 -0.00278 -0.22139 -0.06828 68  TYR A C   
554  O O   . TYR A 68  ? 1.29123 0.44166 0.56002 -0.00260 -0.21517 -0.07323 68  TYR A O   
555  C CB  . TYR A 68  ? 1.25529 0.43961 0.57232 -0.01649 -0.22343 -0.05562 68  TYR A CB  
556  C CG  . TYR A 68  ? 1.26696 0.46733 0.60599 -0.02021 -0.22508 -0.05094 68  TYR A CG  
557  C CD1 . TYR A 68  ? 1.20707 0.41370 0.54966 -0.02239 -0.21898 -0.05480 68  TYR A CD1 
558  C CD2 . TYR A 68  ? 1.23583 0.44599 0.59122 -0.02256 -0.23230 -0.04378 68  TYR A CD2 
559  C CE1 . TYR A 68  ? 1.21247 0.43430 0.57507 -0.02588 -0.22093 -0.05126 68  TYR A CE1 
560  C CE2 . TYR A 68  ? 1.16556 0.39067 0.54006 -0.02566 -0.23381 -0.03960 68  TYR A CE2 
561  C CZ  . TYR A 68  ? 1.24683 0.47755 0.62529 -0.02687 -0.22853 -0.04307 68  TYR A CZ  
562  O OH  . TYR A 68  ? 1.30001 0.54565 0.69706 -0.02991 -0.23043 -0.03971 68  TYR A OH  
563  N N   . GLY A 69  ? 1.35929 0.51208 0.64818 -0.00139 -0.22775 -0.06628 69  GLY A N   
564  C CA  . GLY A 69  ? 1.24964 0.39030 0.52196 0.00032  -0.22893 -0.06995 69  GLY A CA  
565  C C   . GLY A 69  ? 1.28706 0.43244 0.56676 -0.00661 -0.23665 -0.06461 69  GLY A C   
566  O O   . GLY A 69  ? 1.31810 0.47685 0.61525 -0.01271 -0.24053 -0.05782 69  GLY A O   
567  N N   . PRO A 70  ? 1.36959 0.50519 0.63620 -0.00581 -0.23890 -0.06885 70  PRO A N   
568  C CA  . PRO A 70  ? 1.26281 0.40381 0.53564 -0.01277 -0.24617 -0.06649 70  PRO A CA  
569  C C   . PRO A 70  ? 1.32207 0.47544 0.59964 -0.01836 -0.24937 -0.06025 70  PRO A C   
570  O O   . PRO A 70  ? 1.34800 0.49755 0.61186 -0.01657 -0.24627 -0.05989 70  PRO A O   
571  C CB  . PRO A 70  ? 1.25790 0.38552 0.51195 -0.00972 -0.24671 -0.07434 70  PRO A CB  
572  C CG  . PRO A 70  ? 1.28005 0.39412 0.52229 -0.00054 -0.24016 -0.08044 70  PRO A CG  
573  C CD  . PRO A 70  ? 1.44790 0.56784 0.69379 0.00176  -0.23477 -0.07751 70  PRO A CD  
574  N N   . PRO A 71  ? 1.32024 0.48695 0.61520 -0.02492 -0.25502 -0.05553 71  PRO A N   
575  C CA  . PRO A 71  ? 1.31914 0.49680 0.61808 -0.02858 -0.25870 -0.04999 71  PRO A CA  
576  C C   . PRO A 71  ? 1.34335 0.51417 0.62386 -0.02659 -0.26214 -0.05304 71  PRO A C   
577  O O   . PRO A 71  ? 1.27554 0.44748 0.54971 -0.02606 -0.26325 -0.04892 71  PRO A O   
578  C CB  . PRO A 71  ? 1.26769 0.46046 0.58845 -0.03538 -0.26409 -0.04684 71  PRO A CB  
579  C CG  . PRO A 71  ? 1.27922 0.46493 0.60105 -0.03665 -0.26402 -0.05229 71  PRO A CG  
580  C CD  . PRO A 71  ? 1.25988 0.43059 0.56961 -0.02919 -0.25767 -0.05552 71  PRO A CD  
581  N N   . GLU A 72  ? 1.31563 0.47818 0.58581 -0.02490 -0.26384 -0.06048 72  GLU A N   
582  C CA  . GLU A 72  ? 1.30191 0.45766 0.55210 -0.02130 -0.26685 -0.06450 72  GLU A CA  
583  C C   . GLU A 72  ? 1.30807 0.44931 0.53484 -0.01521 -0.25997 -0.06395 72  GLU A C   
584  O O   . GLU A 72  ? 1.33604 0.47041 0.54330 -0.01153 -0.26160 -0.06455 72  GLU A O   
585  C CB  . GLU A 72  ? 1.27744 0.42913 0.52296 -0.02156 -0.26958 -0.07394 72  GLU A CB  
586  C CG  . GLU A 72  ? 1.31491 0.48035 0.58013 -0.02967 -0.27562 -0.07664 72  GLU A CG  
587  C CD  . GLU A 72  ? 1.37246 0.53969 0.65533 -0.03467 -0.27236 -0.07389 72  GLU A CD  
588  O OE1 . GLU A 72  ? 1.43579 0.59121 0.71334 -0.03027 -0.26626 -0.07349 72  GLU A OE1 
589  O OE2 . GLU A 72  ? 1.48067 0.66110 0.78169 -0.04236 -0.27572 -0.07262 72  GLU A OE2 
590  N N   . GLU A 73  ? 1.34446 0.48058 0.57141 -0.01373 -0.25198 -0.06403 73  GLU A N   
591  C CA  A GLU A 73  ? 1.36776 0.49164 0.57340 -0.00997 -0.24329 -0.06455 73  GLU A CA  
592  C CA  B GLU A 73  ? 1.36784 0.49173 0.57364 -0.00995 -0.24324 -0.06463 73  GLU A CA  
593  C C   . GLU A 73  ? 1.38452 0.51299 0.59679 -0.01361 -0.23776 -0.05811 73  GLU A C   
594  O O   . GLU A 73  ? 1.43777 0.55661 0.63128 -0.01387 -0.23138 -0.05637 73  GLU A O   
595  C CB  A GLU A 73  ? 1.42656 0.54151 0.62467 -0.00507 -0.23655 -0.07219 73  GLU A CB  
596  C CB  B GLU A 73  ? 1.42585 0.54104 0.62482 -0.00502 -0.23723 -0.07251 73  GLU A CB  
597  C CG  A GLU A 73  ? 1.40756 0.51693 0.60012 -0.00195 -0.24076 -0.07944 73  GLU A CG  
598  C CG  B GLU A 73  ? 1.48936 0.59347 0.66658 -0.00155 -0.22678 -0.07580 73  GLU A CG  
599  C CD  A GLU A 73  ? 1.46019 0.55915 0.64377 0.00456  -0.23413 -0.08738 73  GLU A CD  
600  C CD  B GLU A 73  ? 1.49039 0.58707 0.66028 0.00510  -0.22143 -0.08513 73  GLU A CD  
601  O OE1 A GLU A 73  ? 1.46448 0.56107 0.64302 0.00736  -0.22588 -0.08839 73  GLU A OE1 
602  O OE1 B GLU A 73  ? 1.46358 0.56062 0.64366 0.00729  -0.22617 -0.08830 73  GLU A OE1 
603  O OE2 A GLU A 73  ? 1.49114 0.58459 0.67255 0.00678  -0.23693 -0.09352 73  GLU A OE2 
604  O OE2 B GLU A 73  ? 1.56098 0.65084 0.71360 0.00798  -0.21190 -0.08972 73  GLU A OE2 
605  N N   . TRP A 74  ? 1.32755 0.46988 0.56551 -0.01705 -0.23905 -0.05496 74  TRP A N   
606  C CA  . TRP A 74  ? 1.28547 0.43516 0.53331 -0.02112 -0.23392 -0.04996 74  TRP A CA  
607  C C   . TRP A 74  ? 1.36072 0.52571 0.62876 -0.02568 -0.24170 -0.04286 74  TRP A C   
608  O O   . TRP A 74  ? 1.38837 0.56585 0.67832 -0.02741 -0.24411 -0.04169 74  TRP A O   
609  C CB  . TRP A 74  ? 1.24542 0.39891 0.50466 -0.01948 -0.22796 -0.05393 74  TRP A CB  
610  C CG  . TRP A 74  ? 1.36383 0.52163 0.62693 -0.02302 -0.21972 -0.05340 74  TRP A CG  
611  C CD1 . TRP A 74  ? 1.26429 0.41444 0.51361 -0.02193 -0.20948 -0.06042 74  TRP A CD1 
612  C CD2 . TRP A 74  ? 1.28254 0.45481 0.56512 -0.02899 -0.22034 -0.04711 74  TRP A CD2 
613  N NE1 . TRP A 74  ? 1.19929 0.35789 0.45823 -0.02797 -0.20355 -0.05950 74  TRP A NE1 
614  C CE2 . TRP A 74  ? 1.25742 0.42922 0.53710 -0.03206 -0.21022 -0.05094 74  TRP A CE2 
615  C CE3 . TRP A 74  ? 1.32371 0.51015 0.62541 -0.03243 -0.22797 -0.03969 74  TRP A CE3 
616  C CZ2 . TRP A 74  ? 1.23468 0.41906 0.53062 -0.03867 -0.20781 -0.04728 74  TRP A CZ2 
617  C CZ3 . TRP A 74  ? 1.17485 0.37395 0.49208 -0.03768 -0.22573 -0.03554 74  TRP A CZ3 
618  C CH2 . TRP A 74  ? 1.12990 0.32765 0.44465 -0.04083 -0.21590 -0.03910 74  TRP A CH2 
619  N N   . GLY A 75  ? 1.30279 0.46518 0.56128 -0.02655 -0.24552 -0.03874 75  GLY A N   
620  C CA  . GLY A 75  ? 1.17461 0.35166 0.45090 -0.02966 -0.25366 -0.03338 75  GLY A CA  
621  C C   . GLY A 75  ? 1.25319 0.43969 0.54180 -0.03389 -0.25041 -0.02734 75  GLY A C   
622  O O   . GLY A 75  ? 1.26592 0.44760 0.54962 -0.03538 -0.24119 -0.02785 75  GLY A O   
623  N N   . TYR A 76  ? 1.12910 0.32896 0.43304 -0.03609 -0.25735 -0.02286 76  TYR A N   
624  C CA  . TYR A 76  ? 1.16968 0.38121 0.48798 -0.04014 -0.25513 -0.01747 76  TYR A CA  
625  C C   . TYR A 76  ? 1.17543 0.37166 0.47204 -0.04018 -0.24935 -0.01493 76  TYR A C   
626  O O   . TYR A 76  ? 1.25649 0.45814 0.56076 -0.04473 -0.24258 -0.01262 76  TYR A O   
627  C CB  . TYR A 76  ? 1.16006 0.38763 0.49676 -0.04160 -0.26433 -0.01426 76  TYR A CB  
628  C CG  . TYR A 76  ? 1.14886 0.39073 0.50229 -0.04537 -0.26313 -0.00914 76  TYR A CG  
629  C CD1 . TYR A 76  ? 1.04437 0.30207 0.42004 -0.04914 -0.25934 -0.00853 76  TYR A CD1 
630  C CD2 . TYR A 76  ? 1.13924 0.37745 0.48491 -0.04417 -0.26623 -0.00539 76  TYR A CD2 
631  C CE1 . TYR A 76  ? 1.08952 0.36159 0.48111 -0.05256 -0.25821 -0.00461 76  TYR A CE1 
632  C CE2 . TYR A 76  ? 1.15730 0.40869 0.51806 -0.04760 -0.26498 -0.00141 76  TYR A CE2 
633  C CZ  . TYR A 76  ? 1.10802 0.37776 0.49286 -0.05225 -0.26076 -0.00119 76  TYR A CZ  
634  O OH  . TYR A 76  ? 1.08253 0.36634 0.48286 -0.05559 -0.25943 0.00206  76  TYR A OH  
635  N N   . ALA A 77  ? 1.15464 0.33026 0.42272 -0.03533 -0.25122 -0.01576 77  ALA A N   
636  C CA  . ALA A 77  ? 1.22450 0.37821 0.46423 -0.03524 -0.24388 -0.01354 77  ALA A CA  
637  C C   . ALA A 77  ? 1.28116 0.42915 0.51645 -0.04038 -0.22977 -0.01658 77  ALA A C   
638  O O   . ALA A 77  ? 1.41090 0.54467 0.62960 -0.04429 -0.22020 -0.01468 77  ALA A O   
639  C CB  . ALA A 77  ? 1.21893 0.34913 0.42578 -0.02742 -0.24817 -0.01466 77  ALA A CB  
640  N N   . ASN A 78  ? 1.24157 0.39882 0.49038 -0.04050 -0.22765 -0.02195 78  ASN A N   
641  C CA  . ASN A 78  ? 1.18731 0.34272 0.43645 -0.04493 -0.21503 -0.02647 78  ASN A CA  
642  C C   . ASN A 78  ? 1.25544 0.43040 0.53220 -0.05127 -0.21162 -0.02473 78  ASN A C   
643  O O   . ASN A 78  ? 1.27581 0.44732 0.54960 -0.05761 -0.20014 -0.02726 78  ASN A O   
644  C CB  . ASN A 78  ? 1.30813 0.46434 0.55915 -0.04050 -0.21485 -0.03386 78  ASN A CB  
645  C CG  . ASN A 78  ? 1.29874 0.43408 0.51889 -0.03543 -0.21383 -0.03759 78  ASN A CG  
646  O OD1 . ASN A 78  ? 1.47811 0.59802 0.67499 -0.03412 -0.21516 -0.03413 78  ASN A OD1 
647  N ND2 . ASN A 78  ? 1.40970 0.54340 0.62769 -0.03135 -0.21172 -0.04501 78  ASN A ND2 
648  N N   . PHE A 79  ? 1.17705 0.37257 0.48003 -0.05043 -0.22079 -0.02129 79  PHE A N   
649  C CA  . PHE A 79  ? 1.15975 0.37364 0.48691 -0.05588 -0.21851 -0.01892 79  PHE A CA  
650  C C   . PHE A 79  ? 1.20945 0.41678 0.52686 -0.06083 -0.21377 -0.01440 79  PHE A C   
651  O O   . PHE A 79  ? 1.21983 0.43334 0.54673 -0.06777 -0.20537 -0.01498 79  PHE A O   
652  C CB  . PHE A 79  ? 1.16369 0.39841 0.51644 -0.05402 -0.22905 -0.01563 79  PHE A CB  
653  C CG  . PHE A 79  ? 1.15267 0.39332 0.51721 -0.05050 -0.23149 -0.01957 79  PHE A CG  
654  C CD1 . PHE A 79  ? 1.11094 0.35527 0.48406 -0.05082 -0.22558 -0.02418 79  PHE A CD1 
655  C CD2 . PHE A 79  ? 1.06530 0.30601 0.43074 -0.04678 -0.23974 -0.01943 79  PHE A CD2 
656  C CE1 . PHE A 79  ? 1.21060 0.45570 0.59014 -0.04543 -0.22847 -0.02782 79  PHE A CE1 
657  C CE2 . PHE A 79  ? 1.12593 0.36778 0.49878 -0.04356 -0.24110 -0.02280 79  PHE A CE2 
658  C CZ  . PHE A 79  ? 1.24521 0.48792 0.62389 -0.04188 -0.23575 -0.02654 79  PHE A CZ  
659  N N   . ILE A 80  ? 1.32883 0.52194 0.62560 -0.05700 -0.21922 -0.01054 80  ILE A N   
660  C CA  . ILE A 80  ? 1.12774 0.31017 0.41083 -0.05986 -0.21519 -0.00605 80  ILE A CA  
661  C C   . ILE A 80  ? 1.19430 0.35192 0.45014 -0.06502 -0.20014 -0.00781 80  ILE A C   
662  O O   . ILE A 80  ? 1.23610 0.39177 0.49261 -0.07290 -0.18964 -0.00656 80  ILE A O   
663  C CB  . ILE A 80  ? 1.26221 0.43498 0.52911 -0.05212 -0.22751 -0.00216 80  ILE A CB  
664  C CG1 . ILE A 80  ? 1.10629 0.30517 0.40293 -0.05056 -0.23945 -0.00028 80  ILE A CG1 
665  C CG2 . ILE A 80  ? 1.28370 0.43468 0.52381 -0.05234 -0.22244 0.00160  80  ILE A CG2 
666  C CD1 . ILE A 80  ? 1.11604 0.30721 0.40028 -0.04297 -0.25245 0.00218  80  ILE A CD1 
667  N N   . ASN A 81  ? 1.35977 0.49726 0.59020 -0.06140 -0.19815 -0.01098 81  ASN A N   
668  C CA  . ASN A 81  ? 1.48212 0.59040 0.67910 -0.06630 -0.18321 -0.01223 81  ASN A CA  
669  C C   . ASN A 81  ? 1.41644 0.52872 0.61989 -0.07417 -0.17043 -0.02052 81  ASN A C   
670  O O   . ASN A 81  ? 1.46108 0.55286 0.64124 -0.08217 -0.15518 -0.02264 81  ASN A O   
671  C CB  . ASN A 81  ? 1.33535 0.41512 0.49381 -0.05750 -0.18745 -0.01135 81  ASN A CB  
672  C CG  . ASN A 81  ? 1.30952 0.37880 0.45259 -0.04946 -0.19881 -0.00484 81  ASN A CG  
673  O OD1 . ASN A 81  ? 1.44878 0.50950 0.58352 -0.05210 -0.19403 -0.00002 81  ASN A OD1 
674  N ND2 . ASN A 81  ? 1.30296 0.37234 0.44104 -0.03929 -0.21345 -0.00567 81  ASN A ND2 
675  N N   . GLY A 82  ? 1.29086 0.42643 0.52155 -0.07191 -0.17587 -0.02585 82  GLY A N   
676  C CA  . GLY A 82  ? 1.32794 0.47162 0.56578 -0.07780 -0.16445 -0.03535 82  GLY A CA  
677  C C   . GLY A 82  ? 1.30763 0.44967 0.53448 -0.07053 -0.16298 -0.04142 82  GLY A C   
678  O O   . GLY A 82  ? 1.43003 0.54978 0.62622 -0.06797 -0.16014 -0.04021 82  GLY A O   
679  N N   . ALA A 83  ? 1.27924 0.44367 0.52883 -0.06650 -0.16425 -0.04789 83  ALA A N   
680  C CA  . ALA A 83  ? 1.27419 0.43706 0.51426 -0.05796 -0.16362 -0.05460 83  ALA A CA  
681  C C   . ALA A 83  ? 1.32255 0.51281 0.58943 -0.05318 -0.16236 -0.06173 83  ALA A C   
682  O O   . ALA A 83  ? 1.33254 0.53995 0.62462 -0.05469 -0.16671 -0.06035 83  ALA A O   
683  C CB  . ALA A 83  ? 1.22072 0.36302 0.44645 -0.04993 -0.17957 -0.05303 83  ALA A CB  
684  N N   . ASP A 84  ? 1.31353 0.50696 0.57329 -0.04608 -0.15723 -0.06920 84  ASP A N   
685  C CA  . ASP A 84  ? 1.31785 0.53563 0.59918 -0.03805 -0.15647 -0.07658 84  ASP A CA  
686  C C   . ASP A 84  ? 1.32465 0.53062 0.60851 -0.02716 -0.17250 -0.07637 84  ASP A C   
687  O O   . ASP A 84  ? 1.31093 0.49142 0.57586 -0.02501 -0.18146 -0.07439 84  ASP A O   
688  C CB  . ASP A 84  ? 1.35259 0.58086 0.62520 -0.03434 -0.14290 -0.08584 84  ASP A CB  
689  C CG  . ASP A 84  ? 1.46167 0.70660 0.73539 -0.04696 -0.12454 -0.08804 84  ASP A CG  
690  O OD1 . ASP A 84  ? 1.57530 0.82275 0.85708 -0.05814 -0.12241 -0.08253 84  ASP A OD1 
691  O OD2 . ASP A 84  ? 1.48781 0.74297 0.75375 -0.04637 -0.11160 -0.09591 84  ASP A OD2 
692  N N   . ASP A 85  ? 1.38420 0.60955 0.69026 -0.02020 -0.17492 -0.07944 85  ASP A N   
693  C CA  . ASP A 85  ? 1.41307 0.62514 0.72003 -0.00964 -0.18792 -0.07976 85  ASP A CA  
694  C C   . ASP A 85  ? 1.35367 0.56444 0.65015 0.00295  -0.18357 -0.08891 85  ASP A C   
695  O O   . ASP A 85  ? 1.37603 0.59647 0.66471 0.00192  -0.17148 -0.09416 85  ASP A O   
696  C CB  . ASP A 85  ? 1.35127 0.57960 0.68313 -0.00772 -0.19345 -0.07676 85  ASP A CB  
697  C CG  . ASP A 85  ? 1.34217 0.60597 0.69454 -0.00315 -0.18403 -0.08234 85  ASP A CG  
698  O OD1 . ASP A 85  ? 1.39596 0.67419 0.74476 -0.00226 -0.17204 -0.08957 85  ASP A OD1 
699  O OD2 . ASP A 85  ? 1.22094 0.49934 0.59260 -0.00045 -0.18872 -0.08007 85  ASP A OD2 
700  N N   . LEU A 86  ? 1.36440 0.56282 0.65981 0.01425  -0.19232 -0.09096 86  LEU A N   
701  C CA  . LEU A 86  ? 1.30068 0.49361 0.58356 0.02803  -0.18916 -0.10004 86  LEU A CA  
702  C C   . LEU A 86  ? 1.43055 0.65844 0.72924 0.03662  -0.17845 -0.10713 86  LEU A C   
703  O O   . LEU A 86  ? 1.55839 0.79206 0.84752 0.04426  -0.17050 -0.11574 86  LEU A O   
704  C CB  . LEU A 86  ? 1.40019 0.56705 0.67688 0.03675  -0.20112 -0.09964 86  LEU A CB  
705  C CG  . LEU A 86  ? 1.36881 0.50567 0.63084 0.02799  -0.21111 -0.09529 86  LEU A CG  
706  C CD1 . LEU A 86  ? 1.31764 0.44318 0.58278 0.03513  -0.21776 -0.09248 86  LEU A CD1 
707  C CD2 . LEU A 86  ? 1.33568 0.46489 0.57814 0.02527  -0.20670 -0.09840 86  LEU A CD2 
708  N N   . LYS A 87  ? 1.55915 0.81218 0.88164 0.03522  -0.17820 -0.10448 87  LYS A N   
709  C CA  . LYS A 87  ? 1.48868 0.78066 0.82885 0.04440  -0.16915 -0.11284 87  LYS A CA  
710  C C   . LYS A 87  ? 1.42528 0.74209 0.76961 0.03098  -0.15428 -0.11669 87  LYS A C   
711  O O   . LYS A 87  ? 1.35052 0.70067 0.70514 0.03642  -0.14380 -0.12672 87  LYS A O   
712  C CB  . LYS A 87  ? 1.26305 0.57236 0.62546 0.04933  -0.17540 -0.10940 87  LYS A CB  
713  C CG  . LYS A 87  ? 1.20452 0.48625 0.55950 0.06253  -0.18822 -0.10549 87  LYS A CG  
714  N N   . GLY A 88  ? 1.39884 0.69888 0.73373 0.01437  -0.15318 -0.10942 88  GLY A N   
715  C CA  . GLY A 88  ? 1.42836 0.74382 0.76118 0.00092  -0.13786 -0.11234 88  GLY A CA  
716  C C   . GLY A 88  ? 1.53146 0.86429 0.88153 -0.01439 -0.13324 -0.10797 88  GLY A C   
717  O O   . GLY A 88  ? 1.61042 0.95842 0.96038 -0.02664 -0.11839 -0.11166 88  GLY A O   
718  N N   . ASN A 89  ? 1.50550 0.83560 0.86922 -0.01490 -0.14462 -0.10068 89  ASN A N   
719  C CA  . ASN A 89  ? 1.28320 0.62882 0.66340 -0.02877 -0.14118 -0.09683 89  ASN A CA  
720  C C   . ASN A 89  ? 1.36208 0.67603 0.72524 -0.04143 -0.14413 -0.08659 89  ASN A C   
721  O O   . ASN A 89  ? 1.44096 0.72529 0.78986 -0.03726 -0.15627 -0.08032 89  ASN A O   
722  C CB  . ASN A 89  ? 1.35151 0.71310 0.75534 -0.02186 -0.15166 -0.09466 89  ASN A CB  
723  C CG  . ASN A 89  ? 1.41242 0.80159 0.82952 -0.00481 -0.15139 -0.10400 89  ASN A CG  
724  O OD1 . ASN A 89  ? 1.64767 1.07527 1.08130 -0.00554 -0.14094 -0.11337 89  ASN A OD1 
725  N ND2 . ASN A 89  ? 1.40485 0.77455 0.81391 0.01091  -0.16273 -0.10217 89  ASN A ND2 
726  N N   . PHE A 90  ? 1.41047 0.73105 0.77446 -0.05672 -0.13277 -0.08570 90  PHE A N   
727  C CA  . PHE A 90  ? 1.31789 0.60849 0.66387 -0.06714 -0.13467 -0.07611 90  PHE A CA  
728  C C   . PHE A 90  ? 1.27540 0.56167 0.63484 -0.06706 -0.14904 -0.06825 90  PHE A C   
729  O O   . PHE A 90  ? 1.37361 0.68473 0.75738 -0.07027 -0.14849 -0.06948 90  PHE A O   
730  C CB  . PHE A 90  ? 1.27940 0.57520 0.62036 -0.08344 -0.11701 -0.07764 90  PHE A CB  
731  C CG  . PHE A 90  ? 1.29744 0.55804 0.61339 -0.09184 -0.11726 -0.06795 90  PHE A CG  
732  C CD1 . PHE A 90  ? 1.21049 0.43970 0.49464 -0.08782 -0.11863 -0.06442 90  PHE A CD1 
733  C CD2 . PHE A 90  ? 1.33371 0.59263 0.65652 -0.10244 -0.11626 -0.06285 90  PHE A CD2 
734  C CE1 . PHE A 90  ? 1.33613 0.53332 0.59507 -0.09275 -0.11959 -0.05564 90  PHE A CE1 
735  C CE2 . PHE A 90  ? 1.29611 0.52124 0.59362 -0.10762 -0.11680 -0.05405 90  PHE A CE2 
736  C CZ  . PHE A 90  ? 1.25675 0.45117 0.52186 -0.10207 -0.11869 -0.05028 90  PHE A CZ  
737  N N   . VAL A 91  ? 1.23194 0.48859 0.57534 -0.06422 -0.16132 -0.06091 91  VAL A N   
738  C CA  . VAL A 91  ? 1.28506 0.53824 0.64081 -0.06414 -0.17542 -0.05405 91  VAL A CA  
739  C C   . VAL A 91  ? 1.32022 0.55015 0.65934 -0.07173 -0.17801 -0.04641 91  VAL A C   
740  O O   . VAL A 91  ? 1.34637 0.55171 0.66057 -0.06884 -0.18121 -0.04453 91  VAL A O   
741  C CB  . VAL A 91  ? 1.25839 0.50187 0.61448 -0.05278 -0.18982 -0.05367 91  VAL A CB  
742  C CG1 . VAL A 91  ? 1.23613 0.47469 0.60182 -0.05436 -0.20321 -0.04645 91  VAL A CG1 
743  C CG2 . VAL A 91  ? 1.25227 0.51583 0.62289 -0.04264 -0.18810 -0.06043 91  VAL A CG2 
744  N N   . GLN A 92  ? 1.23681 0.47471 0.58830 -0.07997 -0.17679 -0.04277 92  GLN A N   
745  C CA  . GLN A 92  ? 1.15540 0.37692 0.49489 -0.08400 -0.17945 -0.03413 92  GLN A CA  
746  C C   . GLN A 92  ? 1.20345 0.44493 0.56804 -0.08880 -0.18160 -0.03001 92  GLN A C   
747  O O   . GLN A 92  ? 1.24650 0.50236 0.62637 -0.09458 -0.17703 -0.03668 92  GLN A O   
748  C CB  . GLN A 92  ? 1.13056 0.32995 0.44190 -0.09214 -0.16548 -0.03501 92  GLN A CB  
749  C CG  . GLN A 92  ? 1.25191 0.43622 0.54798 -0.09191 -0.16708 -0.02482 92  GLN A CG  
750  C CD  . GLN A 92  ? 1.30710 0.46301 0.57037 -0.09995 -0.15205 -0.02499 92  GLN A CD  
751  O OE1 . GLN A 92  ? 1.18681 0.34724 0.44807 -0.10807 -0.13692 -0.03149 92  GLN A OE1 
752  N NE2 . GLN A 92  ? 1.27731 0.41452 0.51922 -0.09609 -0.15423 -0.01645 92  GLN A NE2 
753  N N   . PHE A 93  ? 1.17165 0.41517 0.53881 -0.08619 -0.18838 -0.02080 93  PHE A N   
754  C CA  . PHE A 93  ? 1.07985 0.34091 0.46784 -0.09081 -0.18922 -0.01732 93  PHE A CA  
755  C C   . PHE A 93  ? 1.22791 0.47592 0.60173 -0.10150 -0.17531 -0.01813 93  PHE A C   
756  O O   . PHE A 93  ? 1.24549 0.47914 0.60241 -0.10047 -0.17468 -0.01190 93  PHE A O   
757  C CB  . PHE A 93  ? 1.02598 0.29391 0.41952 -0.08396 -0.20133 -0.00932 93  PHE A CB  
758  C CG  . PHE A 93  ? 1.09612 0.38166 0.50947 -0.08730 -0.20300 -0.00604 93  PHE A CG  
759  C CD1 . PHE A 93  ? 1.05812 0.36644 0.49883 -0.08880 -0.20566 -0.00799 93  PHE A CD1 
760  C CD2 . PHE A 93  ? 1.08315 0.36070 0.48545 -0.08769 -0.20267 -0.00137 93  PHE A CD2 
761  C CE1 . PHE A 93  ? 0.98940 0.31374 0.44752 -0.09170 -0.20719 -0.00537 93  PHE A CE1 
762  C CE2 . PHE A 93  ? 1.07004 0.36326 0.48989 -0.09008 -0.20429 0.00087  93  PHE A CE2 
763  C CZ  . PHE A 93  ? 0.96417 0.28158 0.41268 -0.09250 -0.20630 -0.00109 93  PHE A CZ  
764  N N   . LYS A 94  ? 1.21656 0.46823 0.59464 -0.11164 -0.16431 -0.02692 94  LYS A N   
765  C CA  . LYS A 94  ? 1.19695 0.43708 0.56267 -0.12541 -0.14834 -0.02921 94  LYS A CA  
766  C C   . LYS A 94  ? 1.19272 0.45778 0.58548 -0.13494 -0.14520 -0.03538 94  LYS A C   
767  O O   . LYS A 94  ? 1.31482 0.60363 0.72055 -0.14101 -0.13396 -0.04424 94  LYS A O   
768  C CB  . LYS A 94  ? 1.11318 0.34155 0.45858 -0.13131 -0.13379 -0.03600 94  LYS A CB  
769  C CG  . LYS A 94  ? 1.14135 0.34883 0.46387 -0.14487 -0.11551 -0.03575 94  LYS A CG  
770  C CD  . LYS A 94  ? 1.16620 0.37071 0.47218 -0.14885 -0.10010 -0.04100 94  LYS A CD  
771  C CE  . LYS A 94  ? 1.33678 0.51428 0.61440 -0.16320 -0.08066 -0.03990 94  LYS A CE  
772  N N   . PRO A 95  ? 1.12793 0.40834 0.53998 -0.13221 -0.15251 -0.02921 95  PRO A N   
773  C CA  . PRO A 95  ? 1.09935 0.40263 0.53526 -0.14174 -0.14913 -0.03530 95  PRO A CA  
774  C C   . PRO A 95  ? 1.12935 0.42352 0.55460 -0.15928 -0.13040 -0.04125 95  PRO A C   
775  O O   . PRO A 95  ? 1.16774 0.43850 0.57135 -0.16057 -0.12343 -0.03446 95  PRO A O   
776  C CB  . PRO A 95  ? 1.00609 0.32024 0.45659 -0.13380 -0.15993 -0.02558 95  PRO A CB  
777  C CG  . PRO A 95  ? 1.04226 0.33460 0.46980 -0.12473 -0.16393 -0.01601 95  PRO A CG  
778  C CD  . PRO A 95  ? 1.09461 0.37299 0.50556 -0.12033 -0.16453 -0.01820 95  PRO A CD  
779  N N   . VAL A 96  ? 1.13121 0.45739 0.57822 -0.16900 -0.12046 -0.05205 96  VAL A N   
780  C CA  . VAL A 96  ? 1.12049 0.44578 0.56206 -0.18738 -0.10035 -0.05885 96  VAL A CA  
781  C C   . VAL A 96  ? 1.19607 0.54254 0.66105 -0.19576 -0.10040 -0.06292 96  VAL A C   
782  O O   . VAL A 96  ? 1.21948 0.60396 0.71501 -0.19020 -0.10882 -0.06743 96  VAL A O   
783  C CB  . VAL A 96  ? 1.10994 0.46214 0.55910 -0.19337 -0.08578 -0.07030 96  VAL A CB  
784  C CG1 . VAL A 96  ? 1.08072 0.42658 0.51918 -0.21507 -0.06293 -0.07745 96  VAL A CG1 
785  C CG2 . VAL A 96  ? 1.13409 0.47018 0.56384 -0.18200 -0.08860 -0.06675 96  VAL A CG2 
786  N N   . LEU A 97  ? 1.23500 0.55522 0.68369 -0.20838 -0.09090 -0.06135 97  LEU A N   
787  C CA  . LEU A 97  ? 1.12595 0.46758 0.59711 -0.21605 -0.08908 -0.06506 97  LEU A CA  
788  C C   . LEU A 97  ? 1.15402 0.54095 0.65309 -0.22829 -0.07929 -0.08110 97  LEU A C   
789  O O   . LEU A 97  ? 1.14065 0.53676 0.63619 -0.23825 -0.06349 -0.08957 97  LEU A O   
790  C CB  . LEU A 97  ? 1.10007 0.41730 0.55360 -0.22327 -0.07536 -0.05922 97  LEU A CB  
791  C CG  . LEU A 97  ? 1.06430 0.35653 0.50038 -0.20594 -0.08467 -0.04297 97  LEU A CG  
792  C CD1 . LEU A 97  ? 1.09429 0.36170 0.50997 -0.21339 -0.07032 -0.03972 97  LEU A CD1 
793  C CD2 . LEU A 97  ? 1.07524 0.39035 0.53620 -0.19154 -0.10390 -0.03790 97  LEU A CD2 
794  N N   . SER A 98  ? 1.15516 0.57678 0.68460 -0.22567 -0.08837 -0.08517 98  SER A N   
795  C CA  . SER A 98  ? 1.10795 0.58191 0.66826 -0.23366 -0.08049 -0.10055 98  SER A CA  
796  C C   . SER A 98  ? 1.03468 0.50770 0.59030 -0.25842 -0.05819 -0.11172 98  SER A C   
797  O O   . SER A 98  ? 1.07561 0.58725 0.64857 -0.26850 -0.04581 -0.12643 98  SER A O   
798  C CB  . SER A 98  ? 1.09319 0.60043 0.68306 -0.22533 -0.09508 -0.10169 98  SER A CB  
799  O OG  . SER A 98  ? 1.00533 0.49165 0.59008 -0.23211 -0.09691 -0.09749 98  SER A OG  
800  N N   . SER A 99  ? 1.10682 0.53595 0.63819 -0.26848 -0.05235 -0.10570 99  SER A N   
801  C CA  . SER A 99  ? 1.23927 0.65709 0.75939 -0.29356 -0.02928 -0.11531 99  SER A CA  
802  C C   . SER A 99  ? 1.25880 0.66064 0.75633 -0.30272 -0.01186 -0.11792 99  SER A C   
803  O O   . SER A 99  ? 1.31089 0.71607 0.80483 -0.32564 0.00988  -0.12961 99  SER A O   
804  C CB  . SER A 99  ? 1.14872 0.53458 0.65477 -0.29036 -0.02655 -0.10235 99  SER A CB  
805  O OG  . SER A 99  ? 1.07902 0.42519 0.55708 -0.27300 -0.03388 -0.08474 99  SER A OG  
806  N N   . LYS A 100 ? 1.18527 0.57008 0.66709 -0.28644 -0.02021 -0.10802 100 LYS A N   
807  C CA  . LYS A 100 ? 1.30767 0.68065 0.76891 -0.29259 -0.00521 -0.11034 100 LYS A CA  
808  C C   . LYS A 100 ? 1.37158 0.79529 0.85889 -0.28401 -0.00790 -0.11967 100 LYS A C   
809  O O   . LYS A 100 ? 1.31443 0.73380 0.78742 -0.28678 0.00312  -0.12230 100 LYS A O   
810  C CB  . LYS A 100 ? 1.30661 0.62217 0.72736 -0.28050 -0.01109 -0.09365 100 LYS A CB  
811  C CG  . LYS A 100 ? 1.30389 0.57433 0.69717 -0.28368 -0.00512 -0.08253 100 LYS A CG  
812  N N   . GLY A 101 ? 1.32480 0.79512 0.84796 -0.27262 -0.02210 -0.12465 101 GLY A N   
813  C CA  . GLY A 101 ? 1.28943 0.80847 0.83696 -0.26189 -0.02551 -0.13398 101 GLY A CA  
814  C C   . GLY A 101 ? 1.26889 0.78811 0.82045 -0.23498 -0.04782 -0.12366 101 GLY A C   
815  O O   . GLY A 101 ? 1.31517 0.86789 0.88156 -0.22351 -0.05081 -0.13023 101 GLY A O   
816  N N   . GLY A 102 ? 1.13892 0.62216 0.67727 -0.22464 -0.06315 -0.10856 102 GLY A N   
817  C CA  . GLY A 102 ? 1.09349 0.57286 0.63344 -0.20185 -0.08325 -0.09896 102 GLY A CA  
818  C C   . GLY A 102 ? 1.12860 0.63683 0.69638 -0.19167 -0.09885 -0.09858 102 GLY A C   
819  O O   . GLY A 102 ? 1.10728 0.64694 0.69710 -0.20038 -0.09478 -0.10752 102 GLY A O   
820  N N   . GLU A 103 ? 1.07983 0.57499 0.64477 -0.17367 -0.11690 -0.08788 103 GLU A N   
821  C CA  . GLU A 103 ? 1.04572 0.56458 0.63372 -0.16253 -0.13222 -0.08594 103 GLU A CA  
822  C C   . GLU A 103 ? 1.07004 0.55844 0.64900 -0.16211 -0.14322 -0.07406 103 GLU A C   
823  O O   . GLU A 103 ? 0.95447 0.45908 0.55049 -0.15558 -0.15471 -0.07181 103 GLU A O   
824  C CB  . GLU A 103 ? 0.97603 0.50409 0.56792 -0.14274 -0.14385 -0.08359 103 GLU A CB  
825  C CG  . GLU A 103 ? 1.10596 0.65976 0.70247 -0.13950 -0.13424 -0.09463 103 GLU A CG  
826  C CD  . GLU A 103 ? 1.20048 0.75326 0.79442 -0.11873 -0.14569 -0.09110 103 GLU A CD  
827  O OE1 . GLU A 103 ? 1.17206 0.74030 0.77981 -0.10590 -0.15783 -0.08893 103 GLU A OE1 
828  O OE2 . GLU A 103 ? 1.21057 0.74426 0.78646 -0.11544 -0.14213 -0.09029 103 GLU A OE2 
829  N N   . PHE A 104 ? 1.11544 0.56195 0.66741 -0.16774 -0.13990 -0.06694 104 PHE A N   
830  C CA  . PHE A 104 ? 1.06323 0.48281 0.60586 -0.16624 -0.15012 -0.05693 104 PHE A CA  
831  C C   . PHE A 104 ? 1.08515 0.51113 0.63592 -0.18018 -0.14244 -0.06151 104 PHE A C   
832  O O   . PHE A 104 ? 1.07991 0.48863 0.61573 -0.19360 -0.12743 -0.06444 104 PHE A O   
833  C CB  . PHE A 104 ? 1.03844 0.41787 0.55100 -0.16258 -0.14921 -0.04717 104 PHE A CB  
834  C CG  . PHE A 104 ? 1.02655 0.39940 0.53866 -0.15482 -0.15441 -0.03484 104 PHE A CG  
835  C CD1 . PHE A 104 ? 1.02364 0.41528 0.55561 -0.14546 -0.16782 -0.02993 104 PHE A CD1 
836  C CD2 . PHE A 104 ? 1.04558 0.39271 0.53460 -0.15649 -0.14609 -0.02896 104 PHE A CD2 
837  C CE1 . PHE A 104 ? 0.99166 0.37928 0.52213 -0.13886 -0.17283 -0.02082 104 PHE A CE1 
838  C CE2 . PHE A 104 ? 0.96418 0.30600 0.45013 -0.14816 -0.15237 -0.01983 104 PHE A CE2 
839  C CZ  . PHE A 104 ? 0.93447 0.29774 0.44192 -0.13974 -0.16582 -0.01640 104 PHE A CZ  
840  N N   . ASP A 105 ? 1.07838 0.52859 0.65193 -0.17700 -0.15191 -0.06210 105 ASP A N   
841  C CA  . ASP A 105 ? 1.02690 0.48970 0.61295 -0.18785 -0.14575 -0.06655 105 ASP A CA  
842  C C   . ASP A 105 ? 1.00566 0.46490 0.59682 -0.17597 -0.15502 -0.05353 105 ASP A C   
843  O O   . ASP A 105 ? 1.05934 0.54045 0.66971 -0.16923 -0.16648 -0.05253 105 ASP A O   
844  C CB  . ASP A 105 ? 0.90620 0.41749 0.52256 -0.19069 -0.14515 -0.07853 105 ASP A CB  
845  C CG  . ASP A 105 ? 0.91968 0.44325 0.54665 -0.20612 -0.13640 -0.08697 105 ASP A CG  
846  O OD1 . ASP A 105 ? 1.09902 0.59432 0.71124 -0.21263 -0.12898 -0.08209 105 ASP A OD1 
847  O OD2 . ASP A 105 ? 0.99595 0.56364 0.64932 -0.20816 -0.13529 -0.09746 105 ASP A OD2 
848  N N   . PRO A 106 ? 0.96037 0.39294 0.53276 -0.17291 -0.15065 -0.04410 106 PRO A N   
849  C CA  . PRO A 106 ? 0.95496 0.38614 0.53011 -0.16147 -0.16032 -0.03368 106 PRO A CA  
850  C C   . PRO A 106 ? 1.00629 0.45632 0.60003 -0.16659 -0.15923 -0.03765 106 PRO A C   
851  O O   . PRO A 106 ? 1.03371 0.49379 0.63787 -0.15737 -0.16996 -0.03182 106 PRO A O   
852  C CB  . PRO A 106 ? 1.02227 0.42024 0.56856 -0.15858 -0.15469 -0.02621 106 PRO A CB  
853  C CG  . PRO A 106 ? 0.97529 0.35899 0.50772 -0.17329 -0.13728 -0.03359 106 PRO A CG  
854  C CD  . PRO A 106 ? 1.06534 0.46818 0.61096 -0.17971 -0.13691 -0.04342 106 PRO A CD  
855  N N   . GLU A 107 ? 1.02189 0.47803 0.62006 -0.18198 -0.14602 -0.04836 107 GLU A N   
856  C CA  . GLU A 107 ? 0.99568 0.47148 0.61225 -0.18773 -0.14442 -0.05387 107 GLU A CA  
857  C C   . GLU A 107 ? 0.89796 0.40880 0.54073 -0.18346 -0.15684 -0.05786 107 GLU A C   
858  O O   . GLU A 107 ? 0.91578 0.44030 0.57199 -0.17867 -0.16351 -0.05551 107 GLU A O   
859  C CB  . GLU A 107 ? 1.02943 0.50583 0.64501 -0.20690 -0.12639 -0.06612 107 GLU A CB  
860  C CG  . GLU A 107 ? 1.05787 0.49720 0.64595 -0.21098 -0.11315 -0.06120 107 GLU A CG  
861  C CD  . GLU A 107 ? 1.22639 0.66445 0.81128 -0.23182 -0.09313 -0.07340 107 GLU A CD  
862  O OE1 . GLU A 107 ? 1.23812 0.69180 0.82908 -0.24247 -0.08759 -0.08373 107 GLU A OE1 
863  O OE2 . GLU A 107 ? 1.34151 0.76341 0.91705 -0.23794 -0.08263 -0.07344 107 GLU A OE2 
864  N N   . ALA A 108 ? 0.85619 0.38083 0.50422 -0.18422 -0.16059 -0.06396 108 ALA A N   
865  C CA  . ALA A 108 ? 0.90499 0.46007 0.57327 -0.17775 -0.17383 -0.06692 108 ALA A CA  
866  C C   . ALA A 108 ? 0.95822 0.50718 0.62654 -0.16113 -0.18771 -0.05288 108 ALA A C   
867  O O   . ALA A 108 ? 1.09960 0.66848 0.78362 -0.15585 -0.19636 -0.05139 108 ALA A O   
868  C CB  . ALA A 108 ? 0.91763 0.48772 0.58780 -0.17922 -0.17524 -0.07644 108 ALA A CB  
869  N N   . ILE A 109 ? 0.99358 0.51650 0.64404 -0.15355 -0.18942 -0.04314 109 ILE A N   
870  C CA  . ILE A 109 ? 0.85908 0.37749 0.50892 -0.13994 -0.20132 -0.03117 109 ILE A CA  
871  C C   . ILE A 109 ? 0.90065 0.42167 0.55562 -0.13787 -0.20279 -0.02606 109 ILE A C   
872  O O   . ILE A 109 ? 0.83410 0.36877 0.50085 -0.13115 -0.21217 -0.02160 109 ILE A O   
873  C CB  . ILE A 109 ? 0.87399 0.36638 0.50293 -0.13373 -0.20198 -0.02394 109 ILE A CB  
874  C CG1 . ILE A 109 ? 0.89125 0.38159 0.51557 -0.13382 -0.20243 -0.02916 109 ILE A CG1 
875  C CG2 . ILE A 109 ? 0.83603 0.32549 0.46396 -0.12214 -0.21303 -0.01318 109 ILE A CG2 
876  C CD1 . ILE A 109 ? 0.98363 0.44905 0.58702 -0.12859 -0.20192 -0.02360 109 ILE A CD1 
877  N N   . ILE A 110 ? 0.89156 0.39848 0.53643 -0.14381 -0.19323 -0.02723 110 ILE A N   
878  C CA  . ILE A 110 ? 0.84978 0.35546 0.49586 -0.14064 -0.19532 -0.02312 110 ILE A CA  
879  C C   . ILE A 110 ? 0.87440 0.40733 0.54308 -0.14593 -0.19517 -0.03018 110 ILE A C   
880  O O   . ILE A 110 ? 0.89690 0.43807 0.57332 -0.14056 -0.20158 -0.02647 110 ILE A O   
881  C CB  . ILE A 110 ? 0.90878 0.38664 0.53293 -0.14385 -0.18581 -0.02218 110 ILE A CB  
882  C CG1 . ILE A 110 ? 0.97601 0.44729 0.59557 -0.13650 -0.19174 -0.01679 110 ILE A CG1 
883  C CG2 . ILE A 110 ? 1.09154 0.56923 0.71690 -0.15869 -0.17077 -0.03246 110 ILE A CG2 
884  C CD1 . ILE A 110 ? 0.95165 0.42327 0.56892 -0.12381 -0.20591 -0.00820 110 ILE A CD1 
885  N N   . LYS A 111 ? 0.81639 0.36472 0.49511 -0.15615 -0.18867 -0.04101 111 LYS A N   
886  C CA  . LYS A 111 ? 0.86442 0.44350 0.56544 -0.16041 -0.19014 -0.04897 111 LYS A CA  
887  C C   . LYS A 111 ? 0.81815 0.41618 0.53171 -0.14963 -0.20415 -0.04379 111 LYS A C   
888  O O   . LYS A 111 ? 0.78199 0.39495 0.50743 -0.14652 -0.20869 -0.04241 111 LYS A O   
889  C CB  . LYS A 111 ? 0.89459 0.49054 0.60359 -0.17398 -0.18135 -0.06370 111 LYS A CB  
890  C CG  . LYS A 111 ? 0.95313 0.58802 0.68554 -0.17661 -0.18597 -0.07364 111 LYS A CG  
891  C CD  . LYS A 111 ? 1.08278 0.73869 0.82126 -0.18638 -0.18227 -0.08796 111 LYS A CD  
892  C CE  . LYS A 111 ? 1.10064 0.74595 0.82761 -0.17974 -0.18830 -0.08443 111 LYS A CE  
893  N NZ  . LYS A 111 ? 1.03913 0.70371 0.77014 -0.18853 -0.17872 -0.09785 111 LYS A NZ  
894  N N   . ALA A 112 ? 0.80365 0.39835 0.51249 -0.14417 -0.21010 -0.04093 112 ALA A N   
895  C CA  . ALA A 112 ? 0.77535 0.38254 0.49224 -0.13410 -0.22240 -0.03531 112 ALA A CA  
896  C C   . ALA A 112 ? 0.75252 0.35077 0.46726 -0.12637 -0.22770 -0.02388 112 ALA A C   
897  O O   . ALA A 112 ? 0.72758 0.34172 0.45386 -0.12212 -0.23405 -0.02119 112 ALA A O   
898  C CB  . ALA A 112 ? 0.72517 0.32341 0.43286 -0.12915 -0.22738 -0.03413 112 ALA A CB  
899  N N   . VAL A 113 ? 0.76346 0.33773 0.46268 -0.12447 -0.22538 -0.01786 113 VAL A N   
900  C CA  . VAL A 113 ? 0.80143 0.36970 0.49789 -0.11738 -0.23139 -0.00908 113 VAL A CA  
901  C C   . VAL A 113 ? 0.79818 0.37884 0.50505 -0.11925 -0.23032 -0.01135 113 VAL A C   
902  O O   . VAL A 113 ? 0.77754 0.36907 0.49322 -0.11449 -0.23670 -0.00724 113 VAL A O   
903  C CB  . VAL A 113 ? 0.86671 0.40875 0.54245 -0.11447 -0.23026 -0.00427 113 VAL A CB  
904  C CG1 . VAL A 113 ? 0.73550 0.27383 0.40837 -0.10804 -0.23695 0.00183  113 VAL A CG1 
905  C CG2 . VAL A 113 ? 0.80431 0.33603 0.47081 -0.11118 -0.23285 -0.00143 113 VAL A CG2 
906  N N   . LYS A 114 ? 0.81903 0.39825 0.52510 -0.12710 -0.22140 -0.01877 114 LYS A N   
907  C CA  . LYS A 114 ? 0.76072 0.35038 0.47579 -0.12954 -0.21957 -0.02248 114 LYS A CA  
908  C C   . LYS A 114 ? 0.74171 0.36249 0.47815 -0.12924 -0.22401 -0.02562 114 LYS A C   
909  O O   . LYS A 114 ? 0.74938 0.38052 0.49382 -0.12515 -0.22860 -0.02299 114 LYS A O   
910  C CB  . LYS A 114 ? 0.78867 0.37078 0.49915 -0.14004 -0.20752 -0.03145 114 LYS A CB  
911  C CG  . LYS A 114 ? 0.84557 0.43488 0.56311 -0.14318 -0.20470 -0.03644 114 LYS A CG  
912  C CD  . LYS A 114 ? 0.79519 0.36726 0.50104 -0.13498 -0.21015 -0.02957 114 LYS A CD  
913  C CE  . LYS A 114 ? 0.93149 0.51070 0.64432 -0.13791 -0.20771 -0.03553 114 LYS A CE  
914  N NZ  . LYS A 114 ? 0.99832 0.56004 0.69838 -0.12955 -0.21391 -0.03046 114 LYS A NZ  
915  N N   . ALA A 115 ? 0.80284 0.43765 0.54646 -0.13284 -0.22317 -0.03138 115 ALA A N   
916  C CA  . ALA A 115 ? 0.70719 0.37215 0.46841 -0.13153 -0.22809 -0.03513 115 ALA A CA  
917  C C   . ALA A 115 ? 0.73069 0.39796 0.49371 -0.12179 -0.23768 -0.02501 115 ALA A C   
918  O O   . ALA A 115 ? 0.72606 0.41469 0.50141 -0.11935 -0.24135 -0.02548 115 ALA A O   
919  C CB  . ALA A 115 ? 0.79338 0.47291 0.55900 -0.13551 -0.22752 -0.04398 115 ALA A CB  
920  N N   . SER A 116 ? 0.74470 0.39043 0.49504 -0.11689 -0.24106 -0.01640 116 SER A N   
921  C CA  . SER A 116 ? 0.83189 0.47714 0.58280 -0.11001 -0.24850 -0.00759 116 SER A CA  
922  C C   . SER A 116 ? 0.72976 0.38074 0.48670 -0.10832 -0.24938 -0.00444 116 SER A C   
923  O O   . SER A 116 ? 0.72401 0.37994 0.48465 -0.10477 -0.25402 0.00099  116 SER A O   
924  C CB  . SER A 116 ? 0.73407 0.35536 0.46992 -0.10660 -0.25102 -0.00085 116 SER A CB  
925  O OG  . SER A 116 ? 0.68426 0.28976 0.41058 -0.10634 -0.24870 0.00160  116 SER A OG  
926  N N   . GLY A 117 ? 0.67338 0.32144 0.42943 -0.11099 -0.24502 -0.00801 117 GLY A N   
927  C CA  . GLY A 117 ? 0.64561 0.29983 0.40699 -0.10856 -0.24676 -0.00650 117 GLY A CA  
928  C C   . GLY A 117 ? 0.80841 0.44278 0.55741 -0.10424 -0.24985 -0.00096 117 GLY A C   
929  O O   . GLY A 117 ? 0.82115 0.46073 0.57414 -0.10129 -0.25262 -0.00002 117 GLY A O   
930  N N   . ALA A 118 ? 0.71160 0.32533 0.44583 -0.10375 -0.24949 0.00139  118 ALA A N   
931  C CA  . ALA A 118 ? 0.77931 0.37394 0.49947 -0.09897 -0.25342 0.00580  118 ALA A CA  
932  C C   . ALA A 118 ? 0.78720 0.37120 0.49887 -0.09746 -0.25338 0.00303  118 ALA A C   
933  O O   . ALA A 118 ? 0.71229 0.28869 0.41810 -0.10177 -0.24740 -0.00167 118 ALA A O   
934  C CB  . ALA A 118 ? 0.79486 0.37094 0.50013 -0.09909 -0.25225 0.00772  118 ALA A CB  
935  N N   . LYS A 119 ? 0.72959 0.31195 0.43978 -0.09181 -0.25959 0.00503  119 LYS A N   
936  C CA  . LYS A 119 ? 0.71911 0.28808 0.41807 -0.08794 -0.26223 0.00224  119 LYS A CA  
937  C C   . LYS A 119 ? 0.88906 0.42890 0.56335 -0.08279 -0.26618 0.00465  119 LYS A C   
938  O O   . LYS A 119 ? 0.81181 0.33136 0.46858 -0.07893 -0.26820 0.00242  119 LYS A O   
939  C CB  . LYS A 119 ? 0.69238 0.28128 0.40641 -0.08439 -0.26672 0.00088  119 LYS A CB  
940  C CG  . LYS A 119 ? 0.80194 0.41665 0.53577 -0.08887 -0.26260 -0.00233 119 LYS A CG  
941  C CD  . LYS A 119 ? 0.75687 0.36516 0.48618 -0.09257 -0.25790 -0.00803 119 LYS A CD  
942  C CE  . LYS A 119 ? 0.69158 0.32707 0.44061 -0.09689 -0.25415 -0.01259 119 LYS A CE  
943  N NZ  . LYS A 119 ? 0.77774 0.42835 0.53774 -0.10187 -0.25017 -0.01184 119 LYS A NZ  
944  N N   . PHE A 120 ? 0.84345 0.37966 0.51443 -0.08213 -0.26762 0.00868  120 PHE A N   
945  C CA  . PHE A 120 ? 0.75444 0.26372 0.40097 -0.07732 -0.27118 0.01065  120 PHE A CA  
946  C C   . PHE A 120 ? 0.77606 0.28265 0.41965 -0.08119 -0.26702 0.01327  120 PHE A C   
947  O O   . PHE A 120 ? 0.80368 0.32799 0.46372 -0.08393 -0.26626 0.01486  120 PHE A O   
948  C CB  . PHE A 120 ? 0.75773 0.26633 0.40332 -0.06956 -0.28020 0.01073  120 PHE A CB  
949  C CG  . PHE A 120 ? 0.83149 0.36450 0.49858 -0.07130 -0.28117 0.01164  120 PHE A CG  
950  C CD1 . PHE A 120 ? 0.71947 0.27890 0.40826 -0.07290 -0.28064 0.00945  120 PHE A CD1 
951  C CD2 . PHE A 120 ? 0.78873 0.31718 0.45197 -0.07163 -0.28220 0.01408  120 PHE A CD2 
952  C CE1 . PHE A 120 ? 0.75310 0.33289 0.45775 -0.07577 -0.28038 0.00999  120 PHE A CE1 
953  C CE2 . PHE A 120 ? 0.81381 0.36187 0.49355 -0.07450 -0.28232 0.01429  120 PHE A CE2 
954  C CZ  . PHE A 120 ? 0.80905 0.38209 0.50854 -0.07696 -0.28120 0.01238  120 PHE A CZ  
955  N N   . ALA A 121 ? 0.82619 0.30991 0.44769 -0.08134 -0.26371 0.01311  121 ALA A N   
956  C CA  . ALA A 121 ? 0.77761 0.25820 0.39520 -0.08475 -0.25904 0.01427  121 ALA A CA  
957  C C   . ALA A 121 ? 0.82687 0.27961 0.41594 -0.08072 -0.26007 0.01522  121 ALA A C   
958  O O   . ALA A 121 ? 0.84897 0.28422 0.42059 -0.07475 -0.26506 0.01509  121 ALA A O   
959  C CB  . ALA A 121 ? 0.77229 0.26040 0.39823 -0.09302 -0.24838 0.01051  121 ALA A CB  
960  N N   . GLY A 122 ? 0.83600 0.28397 0.41936 -0.08330 -0.25562 0.01561  122 GLY A N   
961  C CA  . GLY A 122 ? 0.91599 0.33775 0.47123 -0.07985 -0.25541 0.01613  122 GLY A CA  
962  C C   . GLY A 122 ? 0.97168 0.39338 0.52514 -0.07961 -0.25633 0.01748  122 GLY A C   
963  O O   . GLY A 122 ? 0.90531 0.34567 0.47826 -0.08105 -0.25848 0.01851  122 GLY A O   
964  N N   . PRO A 123 ? 0.98996 0.38880 0.51808 -0.07722 -0.25484 0.01738  123 PRO A N   
965  C CA  . PRO A 123 ? 0.95759 0.35463 0.48254 -0.07727 -0.25471 0.01778  123 PRO A CA  
966  C C   . PRO A 123 ? 0.99361 0.38406 0.50954 -0.06985 -0.26650 0.01990  123 PRO A C   
967  O O   . PRO A 123 ? 0.99597 0.38281 0.50868 -0.06426 -0.27496 0.02091  123 PRO A O   
968  C CB  . PRO A 123 ? 0.95925 0.33206 0.45902 -0.07914 -0.24503 0.01602  123 PRO A CB  
969  C CG  . PRO A 123 ? 0.94645 0.29985 0.42479 -0.07377 -0.24823 0.01646  123 PRO A CG  
970  C CD  . PRO A 123 ? 0.95185 0.32332 0.45081 -0.07368 -0.25308 0.01670  123 PRO A CD  
971  N N   . VAL A 124 ? 0.94668 0.33608 0.46096 -0.07008 -0.26648 0.01989  124 VAL A N   
972  C CA  . VAL A 124 ? 0.88340 0.26327 0.38751 -0.06381 -0.27609 0.02092  124 VAL A CA  
973  C C   . VAL A 124 ? 0.92012 0.27137 0.39031 -0.05966 -0.27522 0.01992  124 VAL A C   
974  O O   . VAL A 124 ? 0.99318 0.33654 0.45364 -0.06334 -0.26622 0.01836  124 VAL A O   
975  C CB  . VAL A 124 ? 0.96021 0.34872 0.47487 -0.06560 -0.27669 0.02075  124 VAL A CB  
976  C CG1 . VAL A 124 ? 0.96477 0.33692 0.46259 -0.06036 -0.28278 0.01996  124 VAL A CG1 
977  C CG2 . VAL A 124 ? 0.94650 0.35822 0.48877 -0.06852 -0.27886 0.02178  124 VAL A CG2 
978  N N   . GLY A 125 ? 0.93460 0.26945 0.38733 -0.05190 -0.28328 0.02049  125 GLY A N   
979  C CA  . GLY A 125 ? 0.97015 0.27510 0.38584 -0.04694 -0.28214 0.01902  125 GLY A CA  
980  C C   . GLY A 125 ? 1.08083 0.37474 0.48428 -0.04425 -0.28277 0.01794  125 GLY A C   
981  O O   . GLY A 125 ? 1.07524 0.35041 0.45325 -0.04592 -0.27630 0.01715  125 GLY A O   
982  N N   . GLU A 126 ? 1.13881 0.44167 0.55939 -0.04072 -0.29015 0.01746  126 GLU A N   
983  C CA  . GLU A 126 ? 1.00053 0.29251 0.41076 -0.03835 -0.29235 0.01620  126 GLU A CA  
984  C C   . GLU A 126 ? 0.97935 0.29366 0.41820 -0.04146 -0.29686 0.01473  126 GLU A C   
985  O O   . GLU A 126 ? 0.98408 0.31389 0.44166 -0.03985 -0.30181 0.01154  126 GLU A O   
986  C CB  . GLU A 126 ? 1.01935 0.28666 0.40638 -0.02755 -0.29688 0.01189  126 GLU A CB  
987  C CG  . GLU A 126 ? 1.06014 0.31331 0.43192 -0.02536 -0.29848 0.01043  126 GLU A CG  
988  C CD  . GLU A 126 ? 1.22475 0.44984 0.56799 -0.01350 -0.30262 0.00537  126 GLU A CD  
989  O OE1 . GLU A 126 ? 1.30911 0.52483 0.64322 -0.00648 -0.30413 0.00262  126 GLU A OE1 
990  O OE2 . GLU A 126 ? 1.21187 0.42893 0.54255 -0.01059 -0.30355 0.00269  126 GLU A OE2 
991  N N   . HIS A 127 ? 0.97159 0.29190 0.41452 -0.04639 -0.29302 0.01450  127 HIS A N   
992  C CA  . HIS A 127 ? 0.94308 0.28350 0.40908 -0.05027 -0.29516 0.01159  127 HIS A CA  
993  C C   . HIS A 127 ? 0.96216 0.29423 0.41722 -0.04568 -0.30031 0.00594  127 HIS A C   
994  O O   . HIS A 127 ? 1.04592 0.36038 0.48057 -0.03786 -0.30358 0.00404  127 HIS A O   
995  C CB  . HIS A 127 ? 0.92839 0.27915 0.40507 -0.05697 -0.28850 0.01328  127 HIS A CB  
996  C CG  . HIS A 127 ? 0.92186 0.29171 0.42126 -0.06193 -0.28967 0.01203  127 HIS A CG  
997  N ND1 . HIS A 127 ? 0.90479 0.29365 0.42568 -0.06536 -0.29027 0.01345  127 HIS A ND1 
998  C CD2 . HIS A 127 ? 0.93519 0.30602 0.43658 -0.06447 -0.29002 0.00916  127 HIS A CD2 
999  C CE1 . HIS A 127 ? 0.98991 0.38978 0.52365 -0.07029 -0.29055 0.01180  127 HIS A CE1 
1000 N NE2 . HIS A 127 ? 0.92417 0.31273 0.44606 -0.06998 -0.29041 0.00914  127 HIS A NE2 
1001 N N   . HIS A 128 ? 0.95631 0.30170 0.42435 -0.05021 -0.30103 0.00239  128 HIS A N   
1002 C CA  . HIS A 128 ? 0.97134 0.31498 0.43185 -0.04758 -0.30549 -0.00473 128 HIS A CA  
1003 C C   . HIS A 128 ? 0.99585 0.31433 0.42939 -0.04350 -0.30337 -0.00451 128 HIS A C   
1004 O O   . HIS A 128 ? 1.01371 0.32744 0.43580 -0.03888 -0.30744 -0.01039 128 HIS A O   
1005 C CB  . HIS A 128 ? 0.95835 0.32094 0.43866 -0.05617 -0.30493 -0.00810 128 HIS A CB  
1006 C CG  . HIS A 128 ? 0.93654 0.32398 0.44198 -0.06197 -0.30570 -0.00891 128 HIS A CG  
1007 N ND1 . HIS A 128 ? 1.00663 0.40960 0.52125 -0.05889 -0.31010 -0.01236 128 HIS A ND1 
1008 C CD2 . HIS A 128 ? 0.92190 0.32125 0.44366 -0.07054 -0.30234 -0.00752 128 HIS A CD2 
1009 C CE1 . HIS A 128 ? 0.99460 0.41943 0.53146 -0.06637 -0.30886 -0.01290 128 HIS A CE1 
1010 N NE2 . HIS A 128 ? 0.92229 0.34361 0.46274 -0.07367 -0.30415 -0.00962 128 HIS A NE2 
1011 N N   . ASP A 129 ? 0.99687 0.30309 0.42081 -0.04514 -0.29680 0.00091  129 ASP A N   
1012 C CA  . ASP A 129 ? 1.03721 0.32198 0.43631 -0.04264 -0.29294 0.00038  129 ASP A CA  
1013 C C   . ASP A 129 ? 1.17757 0.43683 0.54634 -0.03444 -0.29441 0.00056  129 ASP A C   
1014 O O   . ASP A 129 ? 1.14110 0.38155 0.48704 -0.03221 -0.29102 -0.00040 129 ASP A O   
1015 C CB  . ASP A 129 ? 1.00984 0.29624 0.41157 -0.04758 -0.28407 0.00351  129 ASP A CB  
1016 C CG  . ASP A 129 ? 1.00192 0.28976 0.40374 -0.04919 -0.27948 0.00762  129 ASP A CG  
1017 O OD1 . ASP A 129 ? 1.11393 0.41211 0.52813 -0.04911 -0.28357 0.00971  129 ASP A OD1 
1018 O OD2 . ASP A 129 ? 1.11033 0.39028 0.50162 -0.05125 -0.27085 0.00746  129 ASP A OD2 
1019 N N   . GLY A 130 ? 1.08599 0.34252 0.45265 -0.02973 -0.29832 0.00153  130 GLY A N   
1020 C CA  . GLY A 130 ? 1.21226 0.44035 0.54700 -0.02024 -0.29945 0.00104  130 GLY A CA  
1021 C C   . GLY A 130 ? 1.24808 0.45048 0.55575 -0.02198 -0.29115 0.00757  130 GLY A C   
1022 O O   . GLY A 130 ? 1.22958 0.40605 0.50665 -0.01617 -0.28780 0.00599  130 GLY A O   
1023 N N   . TYR A 131 ? 1.12496 0.34434 0.44726 -0.03068 -0.28532 0.01123  131 TYR A N   
1024 C CA  . TYR A 131 ? 1.15171 0.36132 0.45467 -0.03576 -0.27426 0.01239  131 TYR A CA  
1025 C C   . TYR A 131 ? 1.19113 0.40756 0.50010 -0.03687 -0.27274 0.01301  131 TYR A C   
1026 O O   . TYR A 131 ? 1.16922 0.40948 0.50640 -0.04338 -0.27121 0.01423  131 TYR A O   
1027 C CB  . TYR A 131 ? 1.17328 0.40189 0.49903 -0.04552 -0.26346 0.01041  131 TYR A CB  
1028 C CG  . TYR A 131 ? 1.16139 0.38110 0.47794 -0.05211 -0.24774 0.00956  131 TYR A CG  
1029 C CD1 . TYR A 131 ? 1.11083 0.30131 0.39302 -0.05050 -0.24070 0.00894  131 TYR A CD1 
1030 C CD2 . TYR A 131 ? 1.12332 0.36312 0.46655 -0.06034 -0.23896 0.00935  131 TYR A CD2 
1031 C CE1 . TYR A 131 ? 1.18504 0.36656 0.46101 -0.05828 -0.22405 0.00853  131 TYR A CE1 
1032 C CE2 . TYR A 131 ? 1.06013 0.29188 0.39815 -0.06762 -0.22364 0.00825  131 TYR A CE2 
1033 C CZ  . TYR A 131 ? 1.15156 0.35411 0.45640 -0.06733 -0.21557 0.00795  131 TYR A CZ  
1034 O OH  . TYR A 131 ? 1.29979 0.49334 0.59935 -0.07642 -0.19912 0.00665  131 TYR A OH  
1035 N N   . SER A 132 ? 1.14484 0.34151 0.42998 -0.03001 -0.27163 0.01071  132 SER A N   
1036 C CA  . SER A 132 ? 1.23027 0.42755 0.51509 -0.03001 -0.27034 0.01029  132 SER A CA  
1037 C C   . SER A 132 ? 1.18928 0.38566 0.47340 -0.04139 -0.25563 0.01271  132 SER A C   
1038 O O   . SER A 132 ? 1.17617 0.35605 0.44356 -0.04483 -0.24330 0.01289  132 SER A O   
1039 C CB  . SER A 132 ? 1.19929 0.37114 0.45666 -0.01851 -0.27223 0.00519  132 SER A CB  
1040 O OG  . SER A 132 ? 1.20461 0.38031 0.48158 -0.00859 -0.28320 0.00112  132 SER A OG  
1041 N N   . MET A 133 ? 1.07691 0.29622 0.39033 -0.04720 -0.25319 0.01402  133 MET A N   
1042 C CA  . MET A 133 ? 1.14080 0.36725 0.46876 -0.05855 -0.23552 0.01483  133 MET A CA  
1043 C C   . MET A 133 ? 1.15829 0.36789 0.47041 -0.05897 -0.22683 0.01564  133 MET A C   
1044 O O   . MET A 133 ? 1.14854 0.36798 0.47760 -0.06852 -0.21508 0.01585  133 MET A O   
1045 C CB  . MET A 133 ? 1.02197 0.28312 0.39136 -0.06520 -0.23640 0.01474  133 MET A CB  
1046 C CG  . MET A 133 ? 1.03819 0.30895 0.42055 -0.07069 -0.23059 0.01318  133 MET A CG  
1047 S SD  . MET A 133 ? 1.01982 0.32701 0.44383 -0.07328 -0.23671 0.01275  133 MET A SD  
1048 C CE  . MET A 133 ? 0.96355 0.27486 0.38776 -0.06430 -0.25483 0.01503  133 MET A CE  
1049 N N   . TRP A 134 ? 1.03334 0.38125 0.51127 -0.06329 -0.29802 0.03017  134 TRP A N   
1050 C CA  . TRP A 134 ? 1.10486 0.45075 0.57948 -0.06447 -0.29716 0.03071  134 TRP A CA  
1051 C C   . TRP A 134 ? 1.11210 0.44873 0.57550 -0.06620 -0.29740 0.03102  134 TRP A C   
1052 O O   . TRP A 134 ? 1.12801 0.46072 0.58737 -0.06625 -0.29824 0.03078  134 TRP A O   
1053 C CB  . TRP A 134 ? 1.10459 0.45524 0.58730 -0.06291 -0.29889 0.03093  134 TRP A CB  
1054 C CG  . TRP A 134 ? 1.11452 0.46358 0.59880 -0.06177 -0.30197 0.03096  134 TRP A CG  
1055 C CD1 . TRP A 134 ? 1.06520 0.40859 0.54431 -0.06218 -0.30349 0.03128  134 TRP A CD1 
1056 C CD2 . TRP A 134 ? 1.09646 0.44962 0.58811 -0.06006 -0.30404 0.03064  134 TRP A CD2 
1057 N NE1 . TRP A 134 ? 1.05993 0.40359 0.54275 -0.06078 -0.30646 0.03115  134 TRP A NE1 
1058 C CE2 . TRP A 134 ? 1.08873 0.43830 0.57918 -0.05957 -0.30684 0.03080  134 TRP A CE2 
1059 C CE3 . TRP A 134 ? 1.08441 0.44355 0.58319 -0.05894 -0.30385 0.03024  134 TRP A CE3 
1060 C CZ2 . TRP A 134 ? 1.12164 0.47348 0.61784 -0.05817 -0.30947 0.03061  134 TRP A CZ2 
1061 C CZ3 . TRP A 134 ? 1.05204 0.41338 0.55633 -0.05760 -0.30633 0.03009  134 TRP A CZ3 
1062 C CH2 . TRP A 134 ? 1.02642 0.38416 0.52945 -0.05729 -0.30912 0.03029  134 TRP A CH2 
1063 N N   . ASP A 135 ? 1.08366 0.41671 0.54195 -0.06757 -0.29665 0.03153  135 ASP A N   
1064 C CA  . ASP A 135 ? 1.12964 0.45339 0.57661 -0.06937 -0.29674 0.03186  135 ASP A CA  
1065 C C   . ASP A 135 ? 1.22348 0.54565 0.67209 -0.06795 -0.29980 0.03196  135 ASP A C   
1066 O O   . ASP A 135 ? 1.22091 0.54237 0.66969 -0.06783 -0.30048 0.03230  135 ASP A O   
1067 C CB  . ASP A 135 ? 1.21020 0.53019 0.65025 -0.07163 -0.29456 0.03236  135 ASP A CB  
1068 C CG  . ASP A 135 ? 1.41214 0.72214 0.83925 -0.07402 -0.29392 0.03267  135 ASP A CG  
1069 O OD1 . ASP A 135 ? 1.43806 0.74404 0.86081 -0.07418 -0.29453 0.03239  135 ASP A OD1 
1070 O OD2 . ASP A 135 ? 1.33979 0.64593 0.76110 -0.07574 -0.29278 0.03317  135 ASP A OD2 
1071 N N   . SER A 136 ? 1.16552 0.48727 0.61557 -0.06684 -0.30168 0.03162  136 SER A N   
1072 C CA  . SER A 136 ? 1.18741 0.50781 0.63954 -0.06542 -0.30491 0.03165  136 SER A CA  
1073 C C   . SER A 136 ? 1.19154 0.50231 0.63252 -0.06675 -0.30548 0.03187  136 SER A C   
1074 O O   . SER A 136 ? 1.22368 0.52914 0.65606 -0.06849 -0.30374 0.03186  136 SER A O   
1075 C CB  . SER A 136 ? 1.07196 0.39629 0.53085 -0.06371 -0.30678 0.03122  136 SER A CB  
1076 O OG  . SER A 136 ? 1.24704 0.56960 0.70747 -0.06254 -0.31001 0.03125  136 SER A OG  
1077 N N   . LYS A 137 ? 1.11914 0.42760 0.56026 -0.06591 -0.30791 0.03202  137 LYS A N   
1078 C CA  . LYS A 137 ? 1.33158 0.63066 0.76228 -0.06692 -0.30881 0.03219  137 LYS A CA  
1079 C C   . LYS A 137 ? 1.27509 0.57364 0.70853 -0.06531 -0.31198 0.03186  137 LYS A C   
1080 O O   . LYS A 137 ? 1.27108 0.56267 0.69652 -0.06601 -0.31252 0.03182  137 LYS A O   
1081 C CB  . LYS A 137 ? 1.33595 0.63188 0.76377 -0.06719 -0.30928 0.03255  137 LYS A CB  
1082 C CG  . LYS A 137 ? 1.24896 0.54956 0.68593 -0.06492 -0.31208 0.03240  137 LYS A CG  
1083 C CD  . LYS A 137 ? 1.50894 0.80666 0.94317 -0.06509 -0.31229 0.03266  137 LYS A CD  
1084 N N   . VAL A 138 ? 1.15923 0.46485 0.60350 -0.06335 -0.31390 0.03165  138 VAL A N   
1085 C CA  . VAL A 138 ? 1.04679 0.35254 0.49473 -0.06184 -0.31716 0.03136  138 VAL A CA  
1086 C C   . VAL A 138 ? 1.16872 0.47511 0.61624 -0.06198 -0.31646 0.03107  138 VAL A C   
1087 O O   . VAL A 138 ? 1.28300 0.58599 0.72860 -0.06147 -0.31862 0.03090  138 VAL A O   
1088 C CB  . VAL A 138 ? 1.03636 0.34929 0.49575 -0.05997 -0.31930 0.03125  138 VAL A CB  
1089 C CG1 . VAL A 138 ? 1.15655 0.46827 0.61586 -0.05969 -0.32011 0.03142  138 VAL A CG1 
1090 C CG2 . VAL A 138 ? 1.09096 0.41252 0.55888 -0.05955 -0.31752 0.03114  138 VAL A CG2 
1091 N N   . ASN A 139 ? 1.08832 0.39844 0.53713 -0.06262 -0.31363 0.03097  139 ASN A N   
1092 C CA  . ASN A 139 ? 1.13643 0.44717 0.58494 -0.06257 -0.31295 0.03058  139 ASN A CA  
1093 C C   . ASN A 139 ? 1.04018 0.34663 0.47979 -0.06451 -0.30975 0.03056  139 ASN A C   
1094 O O   . ASN A 139 ? 1.11715 0.42698 0.55826 -0.06520 -0.30732 0.03063  139 ASN A O   
1095 C CB  . ASN A 139 ? 1.09036 0.41026 0.55008 -0.06118 -0.31296 0.03033  139 ASN A CB  
1096 C CG  . ASN A 139 ? 1.08954 0.41001 0.54899 -0.06097 -0.31232 0.02986  139 ASN A CG  
1097 O OD1 . ASN A 139 ? 1.07588 0.39015 0.52804 -0.06144 -0.31275 0.02968  139 ASN A OD1 
1098 N ND2 . ASN A 139 ? 1.04367 0.37136 0.51088 -0.06019 -0.31132 0.02962  139 ASN A ND2 
1099 N N   . GLU A 140 ? 1.11867 0.41741 0.54880 -0.06543 -0.30980 0.03045  140 GLU A N   
1100 C CA  . GLU A 140 ? 1.11387 0.40766 0.53474 -0.06740 -0.30692 0.03036  140 GLU A CA  
1101 C C   . GLU A 140 ? 1.07135 0.36924 0.49542 -0.06704 -0.30543 0.02982  140 GLU A C   
1102 O O   . GLU A 140 ? 1.08781 0.38289 0.50563 -0.06862 -0.30288 0.02969  140 GLU A O   
1103 C CB  . GLU A 140 ? 1.17666 0.46068 0.58627 -0.06842 -0.30751 0.03034  140 GLU A CB  
1104 C CG  . GLU A 140 ? 1.13178 0.41476 0.54254 -0.06695 -0.30988 0.02991  140 GLU A CG  
1105 C CD  . GLU A 140 ? 1.10132 0.38532 0.51717 -0.06539 -0.31335 0.03009  140 GLU A CD  
1106 O OE1 . GLU A 140 ? 1.15655 0.44354 0.57693 -0.06507 -0.31399 0.03045  140 GLU A OE1 
1107 O OE2 . GLU A 140 ? 1.08518 0.36677 0.50035 -0.06448 -0.31554 0.02983  140 GLU A OE2 
1108 N N   . TRP A 141 ? 1.00618 0.31026 0.43946 -0.06506 -0.30702 0.02949  141 TRP A N   
1109 C CA  . TRP A 141 ? 1.13956 0.44796 0.57665 -0.06443 -0.30578 0.02893  141 TRP A CA  
1110 C C   . TRP A 141 ? 1.06045 0.37658 0.50536 -0.06418 -0.30421 0.02902  141 TRP A C   
1111 O O   . TRP A 141 ? 1.14523 0.46874 0.60020 -0.06258 -0.30508 0.02889  141 TRP A O   
1112 C CB  . TRP A 141 ? 1.10689 0.41792 0.54969 -0.06255 -0.30814 0.02854  141 TRP A CB  
1113 C CG  . TRP A 141 ? 0.99852 0.30206 0.43377 -0.06267 -0.30970 0.02839  141 TRP A CG  
1114 C CD1 . TRP A 141 ? 1.06884 0.36886 0.50257 -0.06241 -0.31224 0.02870  141 TRP A CD1 
1115 C CD2 . TRP A 141 ? 1.12017 0.41854 0.54816 -0.06298 -0.30893 0.02782  141 TRP A CD2 
1116 N NE1 . TRP A 141 ? 1.07945 0.37252 0.50546 -0.06257 -0.31304 0.02841  141 TRP A NE1 
1117 C CE2 . TRP A 141 ? 1.08708 0.37899 0.50939 -0.06291 -0.31101 0.02786  141 TRP A CE2 
1118 C CE3 . TRP A 141 ? 1.09906 0.39962 0.52601 -0.06329 -0.30613 0.02653  141 TRP A CE3 
1119 C CZ2 . TRP A 141 ? 1.06242 0.34790 0.47671 -0.06308 -0.31090 0.02734  141 TRP A CZ2 
1120 C CZ3 . TRP A 141 ? 1.12113 0.41938 0.54266 -0.06355 -0.30488 0.02467  141 TRP A CZ3 
1121 C CH2 . TRP A 141 ? 1.00947 0.29960 0.42429 -0.06343 -0.30741 0.02532  141 TRP A CH2 
1122 N N   . ASN A 142 ? 0.97243 0.28648 0.41224 -0.06593 -0.30183 0.02927  142 ASN A N   
1123 C CA  . ASN A 142 ? 1.02375 0.34433 0.46989 -0.06590 -0.30023 0.02940  142 ASN A CA  
1124 C C   . ASN A 142 ? 1.08272 0.40180 0.52369 -0.06742 -0.29730 0.02907  142 ASN A C   
1125 O O   . ASN A 142 ? 1.07823 0.39510 0.51275 -0.06889 -0.29506 0.02733  142 ASN A O   
1126 C CB  . ASN A 142 ? 1.06496 0.38565 0.51162 -0.06645 -0.30043 0.03007  142 ASN A CB  
1127 C CG  . ASN A 142 ? 1.14760 0.45977 0.58255 -0.06880 -0.29925 0.03047  142 ASN A CG  
1128 O OD1 . ASN A 142 ? 1.08442 0.39466 0.51421 -0.07063 -0.29672 0.03055  142 ASN A OD1 
1129 N ND2 . ASN A 142 ? 1.18021 0.48698 0.61067 -0.06886 -0.30110 0.03072  142 ASN A ND2 
1130 N N   . SER A 143 ? 1.02140 0.34715 0.46875 -0.06722 -0.29573 0.02892  143 SER A N   
1131 C CA  . SER A 143 ? 1.16277 0.49435 0.61083 -0.06858 -0.29132 0.02652  143 SER A CA  
1132 C C   . SER A 143 ? 1.12636 0.45470 0.56701 -0.07137 -0.28868 0.02627  143 SER A C   
1133 O O   . SER A 143 ? 1.13232 0.46497 0.57265 -0.07291 -0.28487 0.02406  143 SER A O   
1134 C CB  . SER A 143 ? 1.01897 0.35907 0.47716 -0.06710 -0.29082 0.02639  143 SER A CB  
1135 O OG  . SER A 143 ? 1.01985 0.35932 0.47999 -0.06693 -0.29215 0.02853  143 SER A OG  
1136 N N   . VAL A 144 ? 1.13360 0.45444 0.56829 -0.07211 -0.29060 0.02839  144 VAL A N   
1137 C CA  . VAL A 144 ? 1.16919 0.48591 0.59579 -0.07497 -0.28819 0.02831  144 VAL A CA  
1138 C C   . VAL A 144 ? 1.17628 0.48676 0.59294 -0.07690 -0.28690 0.02712  144 VAL A C   
1139 O O   . VAL A 144 ? 1.13862 0.44963 0.55042 -0.07946 -0.28314 0.02521  144 VAL A O   
1140 C CB  . VAL A 144 ? 1.26890 0.58025 0.69362 -0.07477 -0.29083 0.03119  144 VAL A CB  
1141 C CG1 . VAL A 144 ? 1.10760 0.41336 0.52271 -0.07786 -0.28856 0.03128  144 VAL A CG1 
1142 C CG2 . VAL A 144 ? 1.14778 0.46834 0.58373 -0.07316 -0.29075 0.03119  144 VAL A CG2 
1143 N N   . LYS A 145 ? 1.19521 0.49997 0.60911 -0.07567 -0.29005 0.02814  145 LYS A N   
1144 C CA  . LYS A 145 ? 1.16441 0.46242 0.56844 -0.07727 -0.28921 0.02718  145 LYS A CA  
1145 C C   . LYS A 145 ? 1.19498 0.49816 0.60079 -0.07719 -0.28674 0.02422  145 LYS A C   
1146 O O   . LYS A 145 ? 1.20262 0.50241 0.60057 -0.07917 -0.28441 0.02256  145 LYS A O   
1147 C CB  . LYS A 145 ? 1.17388 0.46399 0.57489 -0.07577 -0.29373 0.02940  145 LYS A CB  
1148 C CG  . LYS A 145 ? 1.28890 0.57204 0.68406 -0.07676 -0.29504 0.03133  145 LYS A CG  
1149 C CD  . LYS A 145 ? 1.40379 0.69292 0.80906 -0.07435 -0.29756 0.03151  145 LYS A CD  
1150 C CE  . LYS A 145 ? 1.47376 0.76344 0.87923 -0.07514 -0.29694 0.03210  145 LYS A CE  
1151 N NZ  . LYS A 145 ? 1.25038 0.54779 0.66741 -0.07273 -0.29884 0.03212  145 LYS A NZ  
1152 N N   . ARG A 146 ? 1.22717 0.53820 0.64276 -0.07504 -0.28711 0.02350  146 ARG A N   
1153 C CA  . ARG A 146 ? 1.14839 0.46385 0.56568 -0.07455 -0.28519 0.02070  146 ARG A CA  
1154 C C   . ARG A 146 ? 1.22497 0.55050 0.65100 -0.07394 -0.28274 0.01890  146 ARG A C   
1155 O O   . ARG A 146 ? 1.22963 0.55891 0.66233 -0.07297 -0.28371 0.02032  146 ARG A O   
1156 C CB  . ARG A 146 ? 1.13939 0.45284 0.55882 -0.07209 -0.28875 0.02146  146 ARG A CB  
1157 C CG  . ARG A 146 ? 1.18207 0.48628 0.59577 -0.07187 -0.29245 0.02395  146 ARG A CG  
1158 C CD  . ARG A 146 ? 1.17694 0.48056 0.59477 -0.06932 -0.29615 0.02475  146 ARG A CD  
1159 N NE  . ARG A 146 ? 1.28897 0.58423 0.70242 -0.06884 -0.30006 0.02704  146 ARG A NE  
1160 C CZ  . ARG A 146 ? 1.27213 0.56041 0.67823 -0.06907 -0.30120 0.02688  146 ARG A CZ  
1161 N NH1 . ARG A 146 ? 1.17729 0.46589 0.57934 -0.06980 -0.29864 0.02452  146 ARG A NH1 
1162 N NH2 . ARG A 146 ? 1.25427 0.53560 0.65730 -0.06850 -0.30482 0.02883  146 ARG A NH2 
1163 N N   . GLY A 147 ? 1.20618 0.53569 0.63202 -0.07435 -0.27979 0.01580  147 GLY A N   
1164 C CA  . GLY A 147 ? 1.06552 0.40445 0.49960 -0.07351 -0.27759 0.01381  147 GLY A CA  
1165 C C   . GLY A 147 ? 1.17967 0.52247 0.61516 -0.07533 -0.27485 0.01337  147 GLY A C   
1166 O O   . GLY A 147 ? 1.23519 0.57655 0.66425 -0.07807 -0.27178 0.01173  147 GLY A O   
1167 N N   . PRO A 148 ? 1.15222 0.50058 0.59622 -0.07391 -0.27554 0.01437  148 PRO A N   
1168 C CA  . PRO A 148 ? 1.15250 0.50535 0.59878 -0.07543 -0.27290 0.01380  148 PRO A CA  
1169 C C   . PRO A 148 ? 1.16383 0.51045 0.60307 -0.07786 -0.27285 0.01566  148 PRO A C   
1170 O O   . PRO A 148 ? 1.23295 0.58201 0.67159 -0.07989 -0.27012 0.01482  148 PRO A O   
1171 C CB  . PRO A 148 ? 0.95556 0.31397 0.41198 -0.07279 -0.27476 0.01513  148 PRO A CB  
1172 C CG  . PRO A 148 ? 1.07735 0.43095 0.53423 -0.07081 -0.27910 0.01781  148 PRO A CG  
1173 C CD  . PRO A 148 ? 1.25153 0.60188 0.70339 -0.07086 -0.27905 0.01633  148 PRO A CD  
1174 N N   . LYS A 149 ? 1.18535 0.52418 0.61965 -0.07754 -0.27592 0.01810  149 LYS A N   
1175 C CA  . LYS A 149 ? 1.18459 0.51648 0.61173 -0.07956 -0.27637 0.02014  149 LYS A CA  
1176 C C   . LYS A 149 ? 1.22373 0.55980 0.65635 -0.07948 -0.27604 0.02125  149 LYS A C   
1177 O O   . LYS A 149 ? 1.19633 0.53258 0.62548 -0.08206 -0.27323 0.02054  149 LYS A O   
1178 C CB  . LYS A 149 ? 1.24228 0.57020 0.65956 -0.08293 -0.27310 0.01828  149 LYS A CB  
1179 C CG  . LYS A 149 ? 1.19266 0.51541 0.60355 -0.08300 -0.27360 0.01739  149 LYS A CG  
1180 C CD  . LYS A 149 ? 1.14381 0.46415 0.54588 -0.08638 -0.26978 0.01500  149 LYS A CD  
1181 C CE  . LYS A 149 ? 1.31640 0.62937 0.71011 -0.08671 -0.27061 0.01476  149 LYS A CE  
1182 N NZ  . LYS A 149 ? 1.43972 0.75064 0.82483 -0.09013 -0.26664 0.01224  149 LYS A NZ  
1183 N N   . LEU A 150 ? 1.18090 0.51969 0.62139 -0.07670 -0.27896 0.02305  150 LEU A N   
1184 C CA  A LEU A 150 ? 1.16934 0.51219 0.61576 -0.07611 -0.27910 0.02426  150 LEU A CA  
1185 C CA  B LEU A 150 ? 1.17251 0.51545 0.61882 -0.07621 -0.27894 0.02420  150 LEU A CA  
1186 C C   . LEU A 150 ? 1.16789 0.51002 0.61982 -0.07324 -0.28332 0.02690  150 LEU A C   
1187 O O   . LEU A 150 ? 1.08158 0.42575 0.53851 -0.07098 -0.28532 0.02686  150 LEU A O   
1188 C CB  A LEU A 150 ? 1.14387 0.49627 0.59789 -0.07567 -0.27631 0.02184  150 LEU A CB  
1189 C CB  B LEU A 150 ? 1.14387 0.49623 0.59734 -0.07591 -0.27599 0.02161  150 LEU A CB  
1190 C CG  A LEU A 150 ? 1.19866 0.55371 0.65011 -0.07853 -0.27217 0.01986  150 LEU A CG  
1191 C CG  B LEU A 150 ? 1.14513 0.50255 0.60446 -0.07566 -0.27522 0.02219  150 LEU A CG  
1192 C CD1 A LEU A 150 ? 1.11867 0.48239 0.57640 -0.07803 -0.26945 0.01672  150 LEU A CD1 
1193 C CD1 B LEU A 150 ? 1.17180 0.52631 0.62462 -0.07880 -0.27289 0.02221  150 LEU A CD1 
1194 C CD2 A LEU A 150 ? 1.17505 0.52993 0.62757 -0.07905 -0.27242 0.02178  150 LEU A CD2 
1195 C CD2 B LEU A 150 ? 1.11123 0.47780 0.57831 -0.07474 -0.27291 0.01962  150 LEU A CD2 
1196 N N   . ASP A 151 ? 1.06822 0.40698 0.51915 -0.07323 -0.28502 0.02927  151 ASP A N   
1197 C CA  . ASP A 151 ? 1.00267 0.34304 0.46042 -0.07062 -0.28841 0.03079  151 ASP A CA  
1198 C C   . ASP A 151 ? 1.07510 0.42441 0.54360 -0.06867 -0.28812 0.03035  151 ASP A C   
1199 O O   . ASP A 151 ? 1.00830 0.36186 0.48143 -0.06844 -0.28745 0.03061  151 ASP A O   
1200 C CB  . ASP A 151 ? 1.01198 0.35053 0.46813 -0.07123 -0.28883 0.03148  151 ASP A CB  
1201 C CG  . ASP A 151 ? 1.09342 0.43658 0.55816 -0.06880 -0.29126 0.03152  151 ASP A CG  
1202 O OD1 . ASP A 151 ? 1.19626 0.54621 0.67029 -0.06674 -0.29206 0.03111  151 ASP A OD1 
1203 O OD2 . ASP A 151 ? 1.04113 0.38064 0.50280 -0.06905 -0.29240 0.03194  151 ASP A OD2 
1204 N N   . LEU A 152 ? 1.00289 0.35462 0.47488 -0.06730 -0.28861 0.02970  152 LEU A N   
1205 C CA  . LEU A 152 ? 1.00744 0.36719 0.48901 -0.06547 -0.28823 0.02920  152 LEU A CA  
1206 C C   . LEU A 152 ? 0.94662 0.31311 0.43793 -0.06376 -0.28928 0.02945  152 LEU A C   
1207 O O   . LEU A 152 ? 0.95203 0.32394 0.44891 -0.06319 -0.28816 0.02935  152 LEU A O   
1208 C CB  . LEU A 152 ? 0.90546 0.26786 0.38989 -0.06426 -0.28835 0.02769  152 LEU A CB  
1209 C CG  . LEU A 152 ? 0.99525 0.35756 0.47428 -0.06613 -0.28511 0.02500  152 LEU A CG  
1210 C CD1 . LEU A 152 ? 0.92580 0.28872 0.40593 -0.06489 -0.28584 0.02377  152 LEU A CD1 
1211 C CD2 . LEU A 152 ? 0.96147 0.32987 0.44253 -0.06731 -0.28116 0.02282  152 LEU A CD2 
1212 N N   . VAL A 153 ? 0.91898 0.28490 0.41201 -0.06299 -0.29139 0.02975  153 VAL A N   
1213 C CA  . VAL A 153 ? 0.89368 0.26578 0.39582 -0.06138 -0.29244 0.02992  153 VAL A CA  
1214 C C   . VAL A 153 ? 1.01350 0.38619 0.51492 -0.06225 -0.29104 0.03035  153 VAL A C   
1215 O O   . VAL A 153 ? 1.00409 0.38301 0.51289 -0.06116 -0.29056 0.03027  153 VAL A O   
1216 C CB  . VAL A 153 ? 0.89655 0.26712 0.39996 -0.06053 -0.29519 0.03014  153 VAL A CB  
1217 C CG1 . VAL A 153 ? 0.89007 0.26615 0.40197 -0.05906 -0.29636 0.03032  153 VAL A CG1 
1218 C CG2 . VAL A 153 ? 1.00808 0.37891 0.51330 -0.05955 -0.29663 0.02973  153 VAL A CG2 
1219 N N   . LYS A 154 ? 0.98265 0.34870 0.47479 -0.06433 -0.29020 0.03078  154 LYS A N   
1220 C CA  . LYS A 154 ? 0.99183 0.35770 0.48236 -0.06537 -0.28887 0.03123  154 LYS A CA  
1221 C C   . LYS A 154 ? 1.00820 0.37723 0.49994 -0.06594 -0.28654 0.03099  154 LYS A C   
1222 O O   . LYS A 154 ? 0.99733 0.37073 0.49382 -0.06545 -0.28579 0.03110  154 LYS A O   
1223 C CB  . LYS A 154 ? 1.03273 0.39021 0.51224 -0.06775 -0.28836 0.03179  154 LYS A CB  
1224 C CG  . LYS A 154 ? 1.08349 0.44042 0.56148 -0.06861 -0.28745 0.03230  154 LYS A CG  
1225 C CD  . LYS A 154 ? 1.14900 0.50959 0.63403 -0.06653 -0.28937 0.03238  154 LYS A CD  
1226 C CE  . LYS A 154 ? 1.22812 0.58655 0.70995 -0.06743 -0.28870 0.03286  154 LYS A CE  
1227 N NZ  . LYS A 154 ? 1.28840 0.65117 0.77796 -0.06519 -0.29040 0.03279  154 LYS A NZ  
1228 N N   . LEU A 155 ? 1.09621 0.46292 0.58383 -0.06680 -0.28561 0.03062  155 LEU A N   
1229 C CA  . LEU A 155 ? 0.98544 0.35478 0.47404 -0.06725 -0.28364 0.03029  155 LEU A CA  
1230 C C   . LEU A 155 ? 0.97153 0.34976 0.47164 -0.06476 -0.28387 0.02987  155 LEU A C   
1231 O O   . LEU A 155 ? 1.10985 0.49173 0.61318 -0.06472 -0.28262 0.02991  155 LEU A O   
1232 C CB  . LEU A 155 ? 0.95831 0.32629 0.44292 -0.06822 -0.28221 0.02887  155 LEU A CB  
1233 C CG  . LEU A 155 ? 1.15185 0.52560 0.63751 -0.06987 -0.27796 0.02619  155 LEU A CG  
1234 C CD1 . LEU A 155 ? 1.47971 0.84942 0.95742 -0.07304 -0.27580 0.02605  155 LEU A CD1 
1235 C CD2 . LEU A 155 ? 1.01219 0.38912 0.49856 -0.06992 -0.27618 0.02343  155 LEU A CD2 
1236 N N   . TRP A 156 ? 1.02381 0.40539 0.52997 -0.06275 -0.28548 0.02947  156 TRP A N   
1237 C CA  . TRP A 156 ? 1.01487 0.40456 0.53164 -0.06050 -0.28573 0.02908  156 TRP A CA  
1238 C C   . TRP A 156 ? 0.97915 0.37266 0.50138 -0.05974 -0.28614 0.02949  156 TRP A C   
1239 O O   . TRP A 156 ? 1.01857 0.41790 0.54738 -0.05867 -0.28536 0.02929  156 TRP A O   
1240 C CB  . TRP A 156 ? 0.98063 0.37235 0.50196 -0.05882 -0.28749 0.02867  156 TRP A CB  
1241 C CG  . TRP A 156 ? 0.99677 0.38586 0.51425 -0.05901 -0.28712 0.02808  156 TRP A CG  
1242 C CD1 . TRP A 156 ? 0.90622 0.29070 0.41917 -0.05922 -0.28834 0.02797  156 TRP A CD1 
1243 C CD2 . TRP A 156 ? 0.88470 0.27533 0.40234 -0.05888 -0.28555 0.02746  156 TRP A CD2 
1244 N NE1 . TRP A 156 ? 0.95072 0.33417 0.46120 -0.05922 -0.28744 0.02713  156 TRP A NE1 
1245 C CE2 . TRP A 156 ? 0.92530 0.31490 0.44025 -0.05911 -0.28493 0.02592  156 TRP A CE2 
1246 C CE3 . TRP A 156 ? 0.94410 0.33902 0.46535 -0.05862 -0.28391 0.02718  156 TRP A CE3 
1247 C CZ2 . TRP A 156 ? 0.92596 0.32109 0.44339 -0.05914 -0.28192 0.02318  156 TRP A CZ2 
1248 C CZ3 . TRP A 156 ? 0.91424 0.31469 0.43805 -0.05871 -0.28093 0.02447  156 TRP A CZ3 
1249 C CH2 . TRP A 156 ? 0.92863 0.32916 0.45056 -0.05893 -0.27998 0.02246  156 TRP A CH2 
1250 N N   . ALA A 157 ? 0.95789 0.34794 0.47728 -0.06018 -0.28742 0.03001  157 ALA A N   
1251 C CA  . ALA A 157 ? 1.02765 0.42061 0.55162 -0.05935 -0.28800 0.03033  157 ALA A CA  
1252 C C   . ALA A 157 ? 0.96632 0.35948 0.48824 -0.06042 -0.28595 0.03056  157 ALA A C   
1253 O O   . ALA A 157 ? 0.95930 0.35778 0.48771 -0.05926 -0.28560 0.03050  157 ALA A O   
1254 C CB  . ALA A 157 ? 0.99766 0.38584 0.51792 -0.05962 -0.28992 0.03076  157 ALA A CB  
1255 N N   . ASP A 158 ? 0.98062 0.36774 0.49323 -0.06276 -0.28460 0.03085  158 ASP A N   
1256 C CA  . ASP A 158 ? 0.98692 0.37360 0.49676 -0.06413 -0.28265 0.03112  158 ASP A CA  
1257 C C   . ASP A 158 ? 1.03045 0.42284 0.54583 -0.06336 -0.28124 0.03062  158 ASP A C   
1258 O O   . ASP A 158 ? 1.14639 0.54227 0.66522 -0.06302 -0.28032 0.03069  158 ASP A O   
1259 C CB  . ASP A 158 ? 0.99792 0.37650 0.49610 -0.06712 -0.28150 0.03153  158 ASP A CB  
1260 C CG  . ASP A 158 ? 1.14659 0.51909 0.63871 -0.06793 -0.28277 0.03203  158 ASP A CG  
1261 O OD1 . ASP A 158 ? 1.02779 0.40218 0.52417 -0.06646 -0.28423 0.03217  158 ASP A OD1 
1262 O OD2 . ASP A 158 ? 1.23866 0.60425 0.72155 -0.07003 -0.28237 0.03224  158 ASP A OD2 
1263 N N   . LEU A 159 ? 1.05535 0.44862 0.57160 -0.06295 -0.28113 0.03006  159 LEU A N   
1264 C CA  . LEU A 159 ? 0.96168 0.36004 0.48298 -0.06205 -0.27992 0.02950  159 LEU A CA  
1265 C C   . LEU A 159 ? 1.01769 0.42391 0.54990 -0.05945 -0.28060 0.02922  159 LEU A C   
1266 O O   . LEU A 159 ? 1.05925 0.46990 0.59586 -0.05880 -0.27946 0.02900  159 LEU A O   
1267 C CB  . LEU A 159 ? 0.93875 0.33559 0.45790 -0.06208 -0.27983 0.02889  159 LEU A CB  
1268 C CG  . LEU A 159 ? 0.98678 0.37896 0.49711 -0.06487 -0.27775 0.02811  159 LEU A CG  
1269 C CD1 . LEU A 159 ? 1.04446 0.44012 0.55644 -0.06476 -0.27620 0.02554  159 LEU A CD1 
1270 C CD2 . LEU A 159 ? 0.99168 0.38724 0.50264 -0.06623 -0.27495 0.02718  159 LEU A CD2 
1271 N N   . VAL A 160 ? 1.02405 0.43185 0.56051 -0.05804 -0.28249 0.02923  160 VAL A N   
1272 C CA  . VAL A 160 ? 0.95670 0.37147 0.50307 -0.05580 -0.28325 0.02901  160 VAL A CA  
1273 C C   . VAL A 160 ? 0.93630 0.35276 0.48467 -0.05564 -0.28297 0.02939  160 VAL A C   
1274 O O   . VAL A 160 ? 0.89026 0.31228 0.44510 -0.05438 -0.28233 0.02915  160 VAL A O   
1275 C CB  . VAL A 160 ? 0.84813 0.26337 0.39774 -0.05467 -0.28553 0.02898  160 VAL A CB  
1276 C CG1 . VAL A 160 ? 0.88404 0.30525 0.44270 -0.05279 -0.28657 0.02894  160 VAL A CG1 
1277 C CG2 . VAL A 160 ? 0.90160 0.31697 0.45146 -0.05427 -0.28571 0.02846  160 VAL A CG2 
1278 N N   . ARG A 161 ? 0.91987 0.33145 0.46266 -0.05681 -0.28347 0.02995  161 ARG A N   
1279 C CA  . ARG A 161 ? 0.88985 0.30245 0.43386 -0.05662 -0.28322 0.03028  161 ARG A CA  
1280 C C   . ARG A 161 ? 1.01122 0.42461 0.55349 -0.05760 -0.28092 0.03028  161 ARG A C   
1281 O O   . ARG A 161 ? 0.99637 0.41436 0.54409 -0.05645 -0.28044 0.03016  161 ARG A O   
1282 C CB  . ARG A 161 ? 1.02217 0.42870 0.55985 -0.05766 -0.28431 0.03083  161 ARG A CB  
1283 C CG  . ARG A 161 ? 1.09007 0.49751 0.63212 -0.05604 -0.28681 0.03082  161 ARG A CG  
1284 C CD  . ARG A 161 ? 1.15006 0.55827 0.69486 -0.05523 -0.28843 0.03055  161 ARG A CD  
1285 N NE  . ARG A 161 ? 1.06308 0.47166 0.61166 -0.05390 -0.29096 0.03057  161 ARG A NE  
1286 C CZ  . ARG A 161 ? 1.05805 0.46117 0.60181 -0.05439 -0.29267 0.03082  161 ARG A CZ  
1287 N NH1 . ARG A 161 ? 0.99971 0.39652 0.53443 -0.05624 -0.29200 0.03112  161 ARG A NH1 
1288 N NH2 . ARG A 161 ? 1.01627 0.41998 0.56408 -0.05306 -0.29513 0.03074  161 ARG A NH2 
1289 N N   . LYS A 162 ? 0.95876 0.36755 0.49351 -0.05969 -0.27965 0.03039  162 LYS A N   
1290 C CA  . LYS A 162 ? 0.94744 0.35636 0.47993 -0.06089 -0.27761 0.03042  162 LYS A CA  
1291 C C   . LYS A 162 ? 1.04305 0.45913 0.58395 -0.05900 -0.27696 0.02978  162 LYS A C   
1292 O O   . LYS A 162 ? 1.04720 0.46560 0.58977 -0.05898 -0.27579 0.02979  162 LYS A O   
1293 C CB  . LYS A 162 ? 1.10676 0.50978 0.63035 -0.06338 -0.27656 0.03049  162 LYS A CB  
1294 C CG  . LYS A 162 ? 1.26694 0.67025 0.78862 -0.06461 -0.27465 0.03038  162 LYS A CG  
1295 C CD  . LYS A 162 ? 1.39386 0.79218 0.90813 -0.06667 -0.27387 0.03024  162 LYS A CD  
1296 C CE  . LYS A 162 ? 1.42284 0.81286 0.92635 -0.06955 -0.27375 0.03090  162 LYS A CE  
1297 N NZ  . LYS A 162 ? 1.68557 1.07730 1.18658 -0.07186 -0.27063 0.02820  162 LYS A NZ  
1298 N N   . ASN A 163 ? 0.98603 0.40518 0.53170 -0.05751 -0.27769 0.02923  163 ASN A N   
1299 C CA  . ASN A 163 ? 0.90379 0.32940 0.45713 -0.05568 -0.27712 0.02857  163 ASN A CA  
1300 C C   . ASN A 163 ? 0.89389 0.32537 0.45598 -0.05347 -0.27804 0.02848  163 ASN A C   
1301 O O   . ASN A 163 ? 0.93620 0.37311 0.50513 -0.05178 -0.27787 0.02793  163 ASN A O   
1302 C CB  . ASN A 163 ? 0.88592 0.31172 0.43978 -0.05516 -0.27740 0.02797  163 ASN A CB  
1303 C CG  . ASN A 163 ? 0.94553 0.36657 0.49184 -0.05702 -0.27625 0.02782  163 ASN A CG  
1304 O OD1 . ASN A 163 ? 1.00989 0.43300 0.55776 -0.05659 -0.27527 0.02724  163 ASN A OD1 
1305 N ND2 . ASN A 163 ? 0.95233 0.36665 0.49013 -0.05914 -0.27643 0.02831  163 ASN A ND2 
1306 N N   . GLY A 164 ? 0.85751 0.28777 0.41932 -0.05345 -0.27906 0.02897  164 GLY A N   
1307 C CA  . GLY A 164 ? 0.86957 0.30506 0.43926 -0.05147 -0.27991 0.02887  164 GLY A CA  
1308 C C   . GLY A 164 ? 0.80636 0.24520 0.38229 -0.04987 -0.28152 0.02856  164 GLY A C   
1309 O O   . GLY A 164 ? 0.84182 0.28613 0.42508 -0.04822 -0.28167 0.02826  164 GLY A O   
1310 N N   . MET A 165 ? 0.81602 0.25135 0.38883 -0.05044 -0.28279 0.02868  165 MET A N   
1311 C CA  . MET A 165 ? 0.88135 0.31932 0.45968 -0.04911 -0.28458 0.02847  165 MET A CA  
1312 C C   . MET A 165 ? 0.87895 0.31325 0.45532 -0.04934 -0.28684 0.02887  165 MET A C   
1313 O O   . MET A 165 ? 0.84035 0.26899 0.40948 -0.05076 -0.28690 0.02924  165 MET A O   
1314 C CB  . MET A 165 ? 0.89597 0.33383 0.47355 -0.04921 -0.28423 0.02805  165 MET A CB  
1315 C CG  . MET A 165 ? 0.93878 0.38122 0.52033 -0.04836 -0.28259 0.02747  165 MET A CG  
1316 S SD  . MET A 165 ? 0.88795 0.32941 0.46779 -0.04835 -0.28229 0.02687  165 MET A SD  
1317 C CE  . MET A 165 ? 0.83221 0.26617 0.40121 -0.05065 -0.28138 0.02709  165 MET A CE  
1318 N N   . LYS A 166 ? 0.93366 0.37095 0.51622 -0.04802 -0.28870 0.02878  166 LYS A N   
1319 C CA  . LYS A 166 ? 0.87789 0.31176 0.45918 -0.04809 -0.29121 0.02907  166 LYS A CA  
1320 C C   . LYS A 166 ? 0.86888 0.29878 0.44529 -0.04903 -0.29170 0.02909  166 LYS A C   
1321 O O   . LYS A 166 ? 0.81817 0.24962 0.39496 -0.04906 -0.29055 0.02876  166 LYS A O   
1322 C CB  . LYS A 166 ? 0.84553 0.28374 0.43494 -0.04655 -0.29308 0.02894  166 LYS A CB  
1323 C CG  . LYS A 166 ? 0.82725 0.26831 0.42085 -0.04557 -0.29309 0.02890  166 LYS A CG  
1324 C CD  . LYS A 166 ? 0.81332 0.25001 0.40377 -0.04574 -0.29466 0.02914  166 LYS A CD  
1325 C CE  . LYS A 166 ? 0.80975 0.24933 0.40521 -0.04449 -0.29510 0.02894  166 LYS A CE  
1326 N NZ  . LYS A 166 ? 0.86486 0.29997 0.45757 -0.04444 -0.29690 0.02899  166 LYS A NZ  
1327 N N   . LEU A 167 ? 0.85269 0.27734 0.42434 -0.04972 -0.29334 0.02940  167 LEU A N   
1328 C CA  . LEU A 167 ? 0.83386 0.25383 0.39980 -0.05071 -0.29385 0.02945  167 LEU A CA  
1329 C C   . LEU A 167 ? 0.89625 0.31666 0.46586 -0.04991 -0.29650 0.02942  167 LEU A C   
1330 O O   . LEU A 167 ? 0.89084 0.31060 0.46242 -0.04940 -0.29861 0.02959  167 LEU A O   
1331 C CB  . LEU A 167 ? 0.88044 0.29349 0.43746 -0.05221 -0.29379 0.02984  167 LEU A CB  
1332 C CG  . LEU A 167 ? 0.85684 0.26445 0.40730 -0.05328 -0.29436 0.02989  167 LEU A CG  
1333 C CD1 . LEU A 167 ? 0.84893 0.25646 0.39653 -0.05402 -0.29226 0.02958  167 LEU A CD1 
1334 C CD2 . LEU A 167 ? 0.85893 0.25955 0.40116 -0.05458 -0.29488 0.03032  167 LEU A CD2 
1335 N N   . VAL A 168 ? 0.84621 0.26744 0.41655 -0.04981 -0.29649 0.02915  168 VAL A N   
1336 C CA  . VAL A 168 ? 0.83425 0.25488 0.40662 -0.04939 -0.29895 0.02917  168 VAL A CA  
1337 C C   . VAL A 168 ? 0.84147 0.25630 0.40622 -0.05047 -0.29906 0.02917  168 VAL A C   
1338 O O   . VAL A 168 ? 0.86640 0.27983 0.42685 -0.05115 -0.29704 0.02894  168 VAL A O   
1339 C CB  . VAL A 168 ? 0.82692 0.25333 0.40682 -0.04830 -0.29912 0.02886  168 VAL A CB  
1340 C CG1 . VAL A 168 ? 0.83693 0.26487 0.41573 -0.04836 -0.29666 0.02842  168 VAL A CG1 
1341 C CG2 . VAL A 168 ? 0.85965 0.28490 0.44096 -0.04811 -0.30172 0.02894  168 VAL A CG2 
1342 N N   . VAL A 169 ? 0.89286 0.30394 0.45565 -0.05062 -0.30149 0.02939  169 VAL A N   
1343 C CA  . VAL A 169 ? 0.85426 0.25960 0.40995 -0.05152 -0.30193 0.02939  169 VAL A CA  
1344 C C   . VAL A 169 ? 0.88435 0.29029 0.44350 -0.05087 -0.30437 0.02933  169 VAL A C   
1345 O O   . VAL A 169 ? 0.91178 0.31850 0.47492 -0.05031 -0.30680 0.02954  169 VAL A O   
1346 C CB  . VAL A 169 ? 0.95288 0.35173 0.50112 -0.05254 -0.30254 0.02974  169 VAL A CB  
1347 C CG1 . VAL A 169 ? 0.87054 0.26330 0.41143 -0.05342 -0.30313 0.02972  169 VAL A CG1 
1348 C CG2 . VAL A 169 ? 0.86331 0.26127 0.40768 -0.05341 -0.30010 0.02987  169 VAL A CG2 
1349 N N   . ALA A 170 ? 0.88564 0.29099 0.44317 -0.05094 -0.30384 0.02901  170 ALA A N   
1350 C CA  . ALA A 170 ? 0.90437 0.30991 0.46450 -0.05045 -0.30602 0.02896  170 ALA A CA  
1351 C C   . ALA A 170 ? 0.91708 0.31577 0.47022 -0.05118 -0.30766 0.02911  170 ALA A C   
1352 O O   . ALA A 170 ? 0.96413 0.35813 0.50966 -0.05205 -0.30633 0.02899  170 ALA A O   
1353 C CB  . ALA A 170 ? 0.85082 0.25901 0.41266 -0.04999 -0.30470 0.02847  170 ALA A CB  
1354 N N   . MET A 171 ? 0.96506 0.36315 0.52085 -0.05086 -0.31061 0.02938  171 MET A N   
1355 C CA  . MET A 171 ? 0.95361 0.34518 0.50323 -0.05142 -0.31258 0.02952  171 MET A CA  
1356 C C   . MET A 171 ? 0.93320 0.32518 0.48562 -0.05101 -0.31476 0.02946  171 MET A C   
1357 O O   . MET A 171 ? 0.93829 0.33440 0.49797 -0.05040 -0.31643 0.02962  171 MET A O   
1358 C CB  . MET A 171 ? 0.93453 0.32367 0.48355 -0.05148 -0.31450 0.02986  171 MET A CB  
1359 C CG  . MET A 171 ? 0.99415 0.38223 0.53971 -0.05197 -0.31246 0.02995  171 MET A CG  
1360 S SD  . MET A 171 ? 0.94098 0.32206 0.47498 -0.05342 -0.31031 0.02991  171 MET A SD  
1361 C CE  . MET A 171 ? 0.99418 0.36792 0.52247 -0.05372 -0.31344 0.03012  171 MET A CE  
1362 N N   . HIS A 172 ? 0.93175 0.31946 0.47840 -0.05139 -0.31468 0.02925  172 HIS A N   
1363 C CA  . HIS A 172 ? 0.93216 0.31946 0.48049 -0.05108 -0.31679 0.02920  172 HIS A CA  
1364 C C   . HIS A 172 ? 0.97217 0.35215 0.51299 -0.05164 -0.31849 0.02926  172 HIS A C   
1365 O O   . HIS A 172 ? 1.00609 0.38329 0.54300 -0.05171 -0.31833 0.02896  172 HIS A O   
1366 C CB  . HIS A 172 ? 0.87734 0.26680 0.42608 -0.05074 -0.31486 0.02870  172 HIS A CB  
1367 C CG  . HIS A 172 ? 0.99057 0.38522 0.54290 -0.05037 -0.31209 0.02844  172 HIS A CG  
1368 N ND1 . HIS A 172 ? 0.96751 0.36836 0.52767 -0.04962 -0.31199 0.02840  172 HIS A ND1 
1369 C CD2 . HIS A 172 ? 1.03238 0.42662 0.58117 -0.05069 -0.30936 0.02820  172 HIS A CD2 
1370 C CE1 . HIS A 172 ? 1.00334 0.40748 0.56474 -0.04937 -0.30929 0.02810  172 HIS A CE1 
1371 N NE2 . HIS A 172 ? 0.97687 0.37711 0.53153 -0.05003 -0.30771 0.02798  172 HIS A NE2 
1372 N N   . GLN A 173 ? 0.95757 0.33429 0.49630 -0.05192 -0.32018 0.02958  173 GLN A N   
1373 C CA  . GLN A 173 ? 0.92564 0.29483 0.45632 -0.05248 -0.32159 0.02962  173 GLN A CA  
1374 C C   . GLN A 173 ? 0.93893 0.30681 0.47235 -0.05216 -0.32551 0.02988  173 GLN A C   
1375 O O   . GLN A 173 ? 1.05508 0.41685 0.58252 -0.05248 -0.32713 0.02991  173 GLN A O   
1376 C CB  . GLN A 173 ? 1.04380 0.40910 0.56843 -0.05315 -0.32041 0.02974  173 GLN A CB  
1377 C CG  . GLN A 173 ? 0.98655 0.35194 0.51388 -0.05287 -0.32242 0.03006  173 GLN A CG  
1378 C CD  . GLN A 173 ? 1.04584 0.41803 0.58121 -0.05228 -0.32168 0.03013  173 GLN A CD  
1379 O OE1 . GLN A 173 ? 1.03484 0.41240 0.57490 -0.05200 -0.31989 0.02999  173 GLN A OE1 
1380 N NE2 . GLN A 173 ? 0.95115 0.32295 0.48809 -0.05200 -0.32317 0.03030  173 GLN A NE2 
1381 N N   . ALA A 174 ? 1.03643 0.40969 0.57843 -0.05160 -0.32700 0.03005  174 ALA A N   
1382 C CA  . ALA A 174 ? 0.90494 0.27696 0.44976 -0.05142 -0.33093 0.03031  174 ALA A CA  
1383 C C   . ALA A 174 ? 0.92129 0.29113 0.46419 -0.05155 -0.33200 0.03023  174 ALA A C   
1384 O O   . ALA A 174 ? 0.98636 0.35152 0.52637 -0.05170 -0.33481 0.03034  174 ALA A O   
1385 C CB  . ALA A 174 ? 0.90140 0.27954 0.45578 -0.05094 -0.33232 0.03055  174 ALA A CB  
1386 N N   . TYR A 175 ? 0.93208 0.30506 0.47642 -0.05142 -0.32990 0.02999  175 TYR A N   
1387 C CA  . TYR A 175 ? 0.93457 0.30558 0.47706 -0.05144 -0.33073 0.02983  175 TYR A CA  
1388 C C   . TYR A 175 ? 1.03376 0.39815 0.56661 -0.05174 -0.32972 0.02947  175 TYR A C   
1389 O O   . TYR A 175 ? 0.99666 0.35813 0.52679 -0.05172 -0.33078 0.02931  175 TYR A O   
1390 C CB  . TYR A 175 ? 0.89826 0.27479 0.44561 -0.05106 -0.32888 0.02962  175 TYR A CB  
1391 C CG  . TYR A 175 ? 0.98942 0.36440 0.53564 -0.05097 -0.32986 0.02945  175 TYR A CG  
1392 C CD1 . TYR A 175 ? 0.96827 0.34124 0.51577 -0.05122 -0.33342 0.02984  175 TYR A CD1 
1393 C CD2 . TYR A 175 ? 0.97106 0.34638 0.51484 -0.05062 -0.32734 0.02887  175 TYR A CD2 
1394 C CE1 . TYR A 175 ? 0.92839 0.29970 0.47459 -0.05118 -0.33436 0.02971  175 TYR A CE1 
1395 C CE2 . TYR A 175 ? 0.95682 0.33043 0.49930 -0.05043 -0.32826 0.02866  175 TYR A CE2 
1396 C CZ  . TYR A 175 ? 0.93052 0.30213 0.47415 -0.05075 -0.33173 0.02911  175 TYR A CZ  
1397 O OH  . TYR A 175 ? 0.90756 0.27722 0.44962 -0.05061 -0.33270 0.02892  175 TYR A OH  
1398 N N   . ASN A 176 ? 0.91636 0.27803 0.44372 -0.05208 -0.32777 0.02935  176 ASN A N   
1399 C CA  . ASN A 176 ? 0.98987 0.34475 0.50750 -0.05252 -0.32680 0.02903  176 ASN A CA  
1400 C C   . ASN A 176 ? 0.98867 0.33771 0.50234 -0.05264 -0.32997 0.02916  176 ASN A C   
1401 O O   . ASN A 176 ? 0.96736 0.31200 0.47529 -0.05269 -0.32993 0.02884  176 ASN A O   
1402 C CB  . ASN A 176 ? 1.01074 0.36322 0.52325 -0.05312 -0.32476 0.02907  176 ASN A CB  
1403 C CG  . ASN A 176 ? 0.93670 0.28113 0.43855 -0.05379 -0.32434 0.02887  176 ASN A CG  
1404 O OD1 . ASN A 176 ? 1.00959 0.34898 0.50745 -0.05404 -0.32642 0.02909  176 ASN A OD1 
1405 N ND2 . ASN A 176 ? 0.93755 0.28046 0.43454 -0.05405 -0.32172 0.02842  176 ASN A ND2 
1406 N N   . TYR A 177 ? 1.01243 0.36112 0.52896 -0.05260 -0.33286 0.02958  177 TYR A N   
1407 C CA  . TYR A 177 ? 0.99181 0.33483 0.50477 -0.05267 -0.33616 0.02970  177 TYR A CA  
1408 C C   . TYR A 177 ? 1.01200 0.35780 0.53197 -0.05238 -0.33944 0.02999  177 TYR A C   
1409 O O   . TYR A 177 ? 1.04163 0.38355 0.56038 -0.05241 -0.34279 0.03018  177 TYR A O   
1410 C CB  . TYR A 177 ? 1.05700 0.39591 0.56635 -0.05287 -0.33737 0.02988  177 TYR A CB  
1411 C CG  . TYR A 177 ? 0.96595 0.30943 0.48248 -0.05256 -0.33840 0.03017  177 TYR A CG  
1412 C CD1 . TYR A 177 ? 0.96043 0.30729 0.47839 -0.05261 -0.33563 0.03016  177 TYR A CD1 
1413 C CD2 . TYR A 177 ? 0.96336 0.30743 0.48500 -0.05221 -0.34226 0.03042  177 TYR A CD2 
1414 C CE1 . TYR A 177 ? 1.01241 0.36317 0.53668 -0.05221 -0.33660 0.03035  177 TYR A CE1 
1415 C CE2 . TYR A 177 ? 1.01256 0.36041 0.54052 -0.05184 -0.34335 0.03059  177 TYR A CE2 
1416 C CZ  . TYR A 177 ? 1.01097 0.36215 0.54018 -0.05179 -0.34047 0.03053  177 TYR A CZ  
1417 O OH  . TYR A 177 ? 0.99372 0.34844 0.52902 -0.05133 -0.34156 0.03063  177 TYR A OH  
1418 N N   . ASN A 178 ? 0.93178 0.28405 0.45896 -0.05215 -0.33862 0.03005  178 ASN A N   
1419 C CA  . ASN A 178 ? 1.01813 0.37317 0.55205 -0.05209 -0.34166 0.03041  178 ASN A CA  
1420 C C   . ASN A 178 ? 0.98372 0.33943 0.51751 -0.05203 -0.34102 0.03020  178 ASN A C   
1421 O O   . ASN A 178 ? 0.92425 0.28370 0.46436 -0.05208 -0.34254 0.03051  178 ASN A O   
1422 C CB  . ASN A 178 ? 0.92173 0.28322 0.46458 -0.05195 -0.34215 0.03075  178 ASN A CB  
1423 C CG  . ASN A 178 ? 1.06569 0.42576 0.61001 -0.05191 -0.34486 0.03101  178 ASN A CG  
1424 O OD1 . ASN A 178 ? 1.08062 0.43923 0.62726 -0.05202 -0.34865 0.03131  178 ASN A OD1 
1425 N ND2 . ASN A 178 ? 0.94363 0.30411 0.48677 -0.05173 -0.34306 0.03088  178 ASN A ND2 
1426 N N   . GLY A 179 ? 0.93240 0.28412 0.45889 -0.05196 -0.33907 0.02970  179 GLY A N   
1427 C CA  . GLY A 179 ? 0.96123 0.31258 0.48654 -0.05173 -0.33859 0.02937  179 GLY A CA  
1428 C C   . GLY A 179 ? 0.99798 0.35071 0.52087 -0.05132 -0.33477 0.02873  179 GLY A C   
1429 O O   . GLY A 179 ? 1.05153 0.40298 0.57244 -0.05099 -0.33452 0.02834  179 GLY A O   
1430 N N   . PHE A 180 ? 0.99576 0.35026 0.51803 -0.05133 -0.33202 0.02856  180 PHE A N   
1431 C CA  . PHE A 180 ? 0.92888 0.28490 0.44923 -0.05094 -0.32848 0.02792  180 PHE A CA  
1432 C C   . PHE A 180 ? 0.93061 0.27993 0.44181 -0.05087 -0.32787 0.02734  180 PHE A C   
1433 O O   . PHE A 180 ? 0.99498 0.34455 0.50504 -0.05029 -0.32654 0.02675  180 PHE A O   
1434 C CB  . PHE A 180 ? 0.91840 0.27729 0.43971 -0.05113 -0.32592 0.02794  180 PHE A CB  
1435 C CG  . PHE A 180 ? 0.91496 0.27543 0.43451 -0.05079 -0.32244 0.02730  180 PHE A CG  
1436 C CD1 . PHE A 180 ? 0.90648 0.27332 0.43271 -0.05018 -0.32115 0.02712  180 PHE A CD1 
1437 C CD2 . PHE A 180 ? 0.92052 0.27588 0.43159 -0.05111 -0.32055 0.02686  180 PHE A CD2 
1438 C CE1 . PHE A 180 ? 0.90364 0.27170 0.42822 -0.04977 -0.31818 0.02647  180 PHE A CE1 
1439 C CE2 . PHE A 180 ? 0.92887 0.28542 0.43830 -0.05082 -0.31762 0.02624  180 PHE A CE2 
1440 C CZ  . PHE A 180 ? 0.90928 0.27220 0.42555 -0.05009 -0.31649 0.02602  180 PHE A CZ  
1441 N N   . TYR A 181 ? 0.98323 0.32645 0.48775 -0.05138 -0.32879 0.02745  181 TYR A N   
1442 C CA  . TYR A 181 ? 1.03765 0.37382 0.53256 -0.05137 -0.32810 0.02688  181 TYR A CA  
1443 C C   . TYR A 181 ? 1.13025 0.46196 0.62289 -0.05124 -0.33127 0.02697  181 TYR A C   
1444 O O   . TYR A 181 ? 1.12281 0.44754 0.60711 -0.05143 -0.33165 0.02673  181 TYR A O   
1445 C CB  . TYR A 181 ? 0.95172 0.28379 0.44008 -0.05213 -0.32674 0.02694  181 TYR A CB  
1446 C CG  . TYR A 181 ? 1.02007 0.35372 0.50666 -0.05237 -0.32319 0.02662  181 TYR A CG  
1447 C CD1 . TYR A 181 ? 1.07119 0.40313 0.55336 -0.05203 -0.32106 0.02586  181 TYR A CD1 
1448 C CD2 . TYR A 181 ? 0.94961 0.28588 0.43839 -0.05294 -0.32212 0.02704  181 TYR A CD2 
1449 C CE1 . TYR A 181 ? 0.99211 0.32506 0.47234 -0.05235 -0.31805 0.02557  181 TYR A CE1 
1450 C CE2 . TYR A 181 ? 0.95907 0.29643 0.44591 -0.05332 -0.31902 0.02680  181 TYR A CE2 
1451 C CZ  . TYR A 181 ? 1.03738 0.37307 0.51995 -0.05308 -0.31701 0.02607  181 TYR A CZ  
1452 O OH  . TYR A 181 ? 1.03525 0.37170 0.51572 -0.05353 -0.31414 0.02582  181 TYR A OH  
1453 N N   . GLU A 182 ? 0.98046 0.31580 0.47995 -0.05101 -0.33348 0.02731  182 GLU A N   
1454 C CA  . GLU A 182 ? 0.95594 0.28732 0.45395 -0.05103 -0.33683 0.02750  182 GLU A CA  
1455 C C   . GLU A 182 ? 0.96192 0.28811 0.45294 -0.05052 -0.33641 0.02680  182 GLU A C   
1456 O O   . GLU A 182 ? 1.06980 0.39107 0.55731 -0.05059 -0.33896 0.02689  182 GLU A O   
1457 C CB  . GLU A 182 ? 0.97972 0.31637 0.48665 -0.05107 -0.33903 0.02804  182 GLU A CB  
1458 C CG  . GLU A 182 ? 0.99958 0.34004 0.50981 -0.05050 -0.33768 0.02767  182 GLU A CG  
1459 C CD  . GLU A 182 ? 1.04233 0.38868 0.56183 -0.05078 -0.33947 0.02833  182 GLU A CD  
1460 O OE1 . GLU A 182 ? 1.14373 0.48854 0.66486 -0.05128 -0.34289 0.02890  182 GLU A OE1 
1461 O OE2 . GLU A 182 ? 1.05297 0.40525 0.57794 -0.05055 -0.33755 0.02829  182 GLU A OE2 
1462 N N   . TRP A 183 ? 0.97010 0.29705 0.45899 -0.04996 -0.33346 0.02609  183 TRP A N   
1463 C CA  . TRP A 183 ? 1.06063 0.38279 0.54312 -0.04923 -0.33307 0.02529  183 TRP A CA  
1464 C C   . TRP A 183 ? 1.02112 0.33755 0.49430 -0.04931 -0.33097 0.02473  183 TRP A C   
1465 O O   . TRP A 183 ? 1.08445 0.39644 0.55133 -0.04865 -0.33018 0.02395  183 TRP A O   
1466 C CB  . TRP A 183 ? 1.02579 0.35256 0.51264 -0.04835 -0.33171 0.02480  183 TRP A CB  
1467 C CG  . TRP A 183 ? 1.10088 0.43249 0.59600 -0.04845 -0.33386 0.02540  183 TRP A CG  
1468 C CD1 . TRP A 183 ? 1.15534 0.48472 0.65104 -0.04877 -0.33714 0.02587  183 TRP A CD1 
1469 C CD2 . TRP A 183 ? 1.11228 0.45150 0.61600 -0.04836 -0.33297 0.02564  183 TRP A CD2 
1470 N NE1 . TRP A 183 ? 1.15509 0.49005 0.65904 -0.04900 -0.33839 0.02642  183 TRP A NE1 
1471 C CE2 . TRP A 183 ? 1.11352 0.45457 0.62248 -0.04873 -0.33584 0.02628  183 TRP A CE2 
1472 C CE3 . TRP A 183 ? 1.17084 0.51528 0.67816 -0.04804 -0.33011 0.02538  183 TRP A CE3 
1473 C CZ2 . TRP A 183 ? 1.13601 0.48375 0.65338 -0.04883 -0.33586 0.02669  183 TRP A CZ2 
1474 C CZ3 . TRP A 183 ? 1.24857 0.59976 0.76436 -0.04800 -0.33010 0.02573  183 TRP A CZ3 
1475 C CH2 . TRP A 183 ? 1.11400 0.46675 0.63464 -0.04841 -0.33290 0.02638  183 TRP A CH2 
1476 N N   . ALA A 184 ? 1.02216 0.33851 0.49442 -0.05013 -0.33017 0.02513  184 ALA A N   
1477 C CA  . ALA A 184 ? 1.07070 0.38092 0.53342 -0.05055 -0.32832 0.02474  184 ALA A CA  
1478 C C   . ALA A 184 ? 1.09728 0.39986 0.55290 -0.05087 -0.33060 0.02488  184 ALA A C   
1479 O O   . ALA A 184 ? 0.98952 0.29249 0.44861 -0.05106 -0.33346 0.02549  184 ALA A O   
1480 C CB  . ALA A 184 ? 1.07019 0.38309 0.53436 -0.05139 -0.32651 0.02514  184 ALA A CB  
1481 N N   . PRO A 185 ? 1.00728 0.30259 0.45281 -0.05093 -0.32951 0.02431  185 PRO A N   
1482 C CA  . PRO A 185 ? 1.07564 0.36325 0.51387 -0.05116 -0.33163 0.02439  185 PRO A CA  
1483 C C   . PRO A 185 ? 1.19226 0.47859 0.63006 -0.05215 -0.33271 0.02515  185 PRO A C   
1484 O O   . PRO A 185 ? 1.24426 0.53169 0.68140 -0.05291 -0.33074 0.02536  185 PRO A O   
1485 C CB  . PRO A 185 ? 1.02674 0.30734 0.45423 -0.05110 -0.32955 0.02358  185 PRO A CB  
1486 C CG  . PRO A 185 ? 1.11164 0.39657 0.54183 -0.05043 -0.32704 0.02291  185 PRO A CG  
1487 C CD  . PRO A 185 ? 1.02377 0.31729 0.46391 -0.05073 -0.32643 0.02352  185 PRO A CD  
1488 N N   . LYS A 186 ? 1.09355 0.37670 0.53080 -0.05208 -0.33595 0.02548  186 LYS A N   
1489 C CA  . LYS A 186 ? 1.11767 0.39829 0.55343 -0.05281 -0.33745 0.02609  186 LYS A CA  
1490 C C   . LYS A 186 ? 1.16942 0.44316 0.59455 -0.05353 -0.33530 0.02583  186 LYS A C   
1491 O O   . LYS A 186 ? 1.07407 0.34283 0.49177 -0.05334 -0.33404 0.02519  186 LYS A O   
1492 C CB  . LYS A 186 ? 1.15591 0.43239 0.59057 -0.05254 -0.34131 0.02631  186 LYS A CB  
1493 C CG  . LYS A 186 ? 1.33886 0.62115 0.78369 -0.05226 -0.34422 0.02684  186 LYS A CG  
1494 C CD  . LYS A 186 ? 1.32916 0.61627 0.78047 -0.05267 -0.34463 0.02744  186 LYS A CD  
1495 C CE  . LYS A 186 ? 1.48954 0.78064 0.94947 -0.05250 -0.34814 0.02797  186 LYS A CE  
1496 N NZ  . LYS A 186 ? 1.41938 0.71589 0.88585 -0.05214 -0.34809 0.02792  186 LYS A NZ  
1497 N N   . THR A 187 ? 1.21597 0.48934 0.64025 -0.05436 -0.33484 0.02630  187 THR A N   
1498 C CA  . THR A 187 ? 1.16888 0.43484 0.58227 -0.05532 -0.33303 0.02618  187 THR A CA  
1499 C C   . THR A 187 ? 1.16895 0.43147 0.58030 -0.05582 -0.33499 0.02674  187 THR A C   
1500 O O   . THR A 187 ? 1.12622 0.39342 0.54557 -0.05546 -0.33714 0.02719  187 THR A O   
1501 C CB  . THR A 187 ? 1.07137 0.33982 0.48397 -0.05613 -0.32931 0.02610  187 THR A CB  
1502 O OG1 . THR A 187 ? 1.13125 0.39157 0.53220 -0.05720 -0.32759 0.02593  187 THR A OG1 
1503 C CG2 . THR A 187 ? 1.09321 0.36779 0.51311 -0.05652 -0.32906 0.02672  187 THR A CG2 
1504 N N   . ASN A 188 ? 1.12094 0.37523 0.52156 -0.05662 -0.33425 0.02666  188 ASN A N   
1505 C CA  . ASN A 188 ? 1.14273 0.39280 0.54014 -0.05708 -0.33595 0.02713  188 ASN A CA  
1506 C C   . ASN A 188 ? 1.32527 0.57608 0.72079 -0.05828 -0.33315 0.02743  188 ASN A C   
1507 O O   . ASN A 188 ? 1.27096 0.52085 0.66676 -0.05854 -0.33433 0.02787  188 ASN A O   
1508 C CB  . ASN A 188 ? 1.22630 0.46647 0.61307 -0.05716 -0.33727 0.02690  188 ASN A CB  
1509 C CG  . ASN A 188 ? 1.21234 0.45149 0.60086 -0.05600 -0.34027 0.02664  188 ASN A CG  
1510 O OD1 . ASN A 188 ? 1.41655 0.66197 0.81471 -0.05521 -0.34230 0.02680  188 ASN A OD1 
1511 N ND2 . ASN A 188 ? 1.44976 0.68072 0.82866 -0.05597 -0.34059 0.02626  188 ASN A ND2 
1512 N N   . ASP A 189 ? 1.30081 0.55327 0.69470 -0.05894 -0.32971 0.02718  189 ASP A N   
1513 C CA  . ASP A 189 ? 1.14821 0.40138 0.54004 -0.06028 -0.32680 0.02747  189 ASP A CA  
1514 C C   . ASP A 189 ? 1.17410 0.43486 0.57607 -0.05992 -0.32760 0.02797  189 ASP A C   
1515 O O   . ASP A 189 ? 1.22829 0.49697 0.63989 -0.05907 -0.32766 0.02790  189 ASP A O   
1516 C CB  . ASP A 189 ? 1.09240 0.34714 0.48249 -0.06086 -0.32338 0.02706  189 ASP A CB  
1517 C CG  . ASP A 189 ? 1.18106 0.43655 0.56896 -0.06241 -0.32033 0.02736  189 ASP A CG  
1518 O OD1 . ASP A 189 ? 1.33652 0.59158 0.72448 -0.06301 -0.32075 0.02791  189 ASP A OD1 
1519 O OD2 . ASP A 189 ? 1.25626 0.51228 0.64194 -0.06300 -0.31764 0.02700  189 ASP A OD2 
1520 N N   . THR A 190 ? 1.20873 0.46675 0.60805 -0.06056 -0.32806 0.02841  190 THR A N   
1521 C CA  . THR A 190 ? 1.26475 0.52926 0.67325 -0.06005 -0.32915 0.02883  190 THR A CA  
1522 C C   . THR A 190 ? 1.14966 0.42079 0.56298 -0.06055 -0.32609 0.02891  190 THR A C   
1523 O O   . THR A 190 ? 1.16996 0.44865 0.59337 -0.05973 -0.32686 0.02908  190 THR A O   
1524 C CB  . THR A 190 ? 1.24013 0.49913 0.64367 -0.06044 -0.33057 0.02918  190 THR A CB  
1525 O OG1 . THR A 190 ? 1.25134 0.50459 0.65099 -0.05980 -0.33354 0.02902  190 THR A OG1 
1526 C CG2 . THR A 190 ? 1.27355 0.53831 0.68592 -0.05972 -0.33210 0.02950  190 THR A CG2 
1527 N N   . SER A 191 ? 1.08459 0.35290 0.49098 -0.06187 -0.32283 0.02877  191 SER A N   
1528 C CA  . SER A 191 ? 1.22761 0.50223 0.63861 -0.06234 -0.31995 0.02879  191 SER A CA  
1529 C C   . SER A 191 ? 1.22008 0.50183 0.63971 -0.06105 -0.32005 0.02838  191 SER A C   
1530 O O   . SER A 191 ? 1.14396 0.43360 0.57336 -0.06034 -0.32014 0.02854  191 SER A O   
1531 C CB  . SER A 191 ? 1.10924 0.37871 0.51048 -0.06418 -0.31664 0.02872  191 SER A CB  
1532 O OG  . SER A 191 ? 1.24623 0.52143 0.65175 -0.06473 -0.31412 0.02881  191 SER A OG  
1533 N N   . LEU A 192 ? 1.13709 0.41580 0.55304 -0.06068 -0.32019 0.02786  192 LEU A N   
1534 C CA  . LEU A 192 ? 1.07178 0.35653 0.49511 -0.05941 -0.32032 0.02742  192 LEU A CA  
1535 C C   . LEU A 192 ? 1.12124 0.41148 0.55458 -0.05810 -0.32341 0.02768  192 LEU A C   
1536 O O   . LEU A 192 ? 1.08244 0.37995 0.52453 -0.05726 -0.32329 0.02757  192 LEU A O   
1537 C CB  . LEU A 192 ? 1.02496 0.30428 0.44141 -0.05918 -0.32018 0.02677  192 LEU A CB  
1538 C CG  . LEU A 192 ? 1.16059 0.44481 0.58213 -0.05810 -0.31940 0.02617  192 LEU A CG  
1539 C CD1 . LEU A 192 ? 1.06224 0.35109 0.48629 -0.05865 -0.31640 0.02610  192 LEU A CD1 
1540 C CD2 . LEU A 192 ? 1.12044 0.39777 0.53322 -0.05793 -0.31910 0.02547  192 LEU A CD2 
1541 N N   . LYS A 193 ? 1.09126 0.37795 0.52313 -0.05803 -0.32606 0.02802  193 LYS A N   
1542 C CA  . LYS A 193 ? 1.13994 0.43164 0.58129 -0.05695 -0.32915 0.02830  193 LYS A CA  
1543 C C   . LYS A 193 ? 1.13008 0.42922 0.57969 -0.05690 -0.32819 0.02863  193 LYS A C   
1544 O O   . LYS A 193 ? 1.04090 0.34684 0.50006 -0.05604 -0.32929 0.02869  193 LYS A O   
1545 C CB  . LYS A 193 ? 1.08633 0.37253 0.52442 -0.05683 -0.33235 0.02855  193 LYS A CB  
1546 C CG  . LYS A 193 ? 1.13612 0.41564 0.56783 -0.05658 -0.33419 0.02827  193 LYS A CG  
1547 C CD  . LYS A 193 ? 1.09141 0.36741 0.52289 -0.05618 -0.33794 0.02853  193 LYS A CD  
1548 C CE  . LYS A 193 ? 1.14377 0.41295 0.56893 -0.05591 -0.33999 0.02828  193 LYS A CE  
1549 N NZ  . LYS A 193 ? 1.40222 0.66920 0.82899 -0.05536 -0.34397 0.02851  193 LYS A NZ  
1550 N N   . LYS A 194 ? 1.15685 0.45445 0.60249 -0.05787 -0.32614 0.02884  194 LYS A N   
1551 C CA  . LYS A 194 ? 1.09152 0.39570 0.54424 -0.05784 -0.32504 0.02913  194 LYS A CA  
1552 C C   . LYS A 194 ? 1.09223 0.40306 0.55061 -0.05755 -0.32280 0.02885  194 LYS A C   
1553 O O   . LYS A 194 ? 0.96960 0.28776 0.43752 -0.05680 -0.32318 0.02897  194 LYS A O   
1554 C CB  . LYS A 194 ? 0.99242 0.29279 0.43838 -0.05913 -0.32299 0.02939  194 LYS A CB  
1555 C CG  . LYS A 194 ? 0.98435 0.29092 0.43658 -0.05917 -0.32156 0.02966  194 LYS A CG  
1556 C CD  . LYS A 194 ? 1.11753 0.41962 0.56226 -0.06060 -0.31958 0.02995  194 LYS A CD  
1557 C CE  . LYS A 194 ? 1.15815 0.45378 0.59755 -0.06071 -0.32181 0.03018  194 LYS A CE  
1558 N NZ  . LYS A 194 ? 1.13500 0.42597 0.56673 -0.06219 -0.31983 0.03049  194 LYS A NZ  
1559 N N   . LEU A 195 ? 1.10077 0.40850 0.55295 -0.05807 -0.32071 0.02843  195 LEU A N   
1560 C CA  . LEU A 195 ? 1.01287 0.32626 0.46964 -0.05771 -0.31856 0.02806  195 LEU A CA  
1561 C C   . LEU A 195 ? 1.03110 0.34953 0.49597 -0.05634 -0.32035 0.02785  195 LEU A C   
1562 O O   . LEU A 195 ? 0.98728 0.31287 0.46012 -0.05574 -0.31951 0.02779  195 LEU A O   
1563 C CB  . LEU A 195 ? 1.01429 0.32260 0.46212 -0.05850 -0.31614 0.02756  195 LEU A CB  
1564 C CG  . LEU A 195 ? 0.97203 0.28522 0.42368 -0.05793 -0.31415 0.02701  195 LEU A CG  
1565 C CD1 . LEU A 195 ? 0.99284 0.31225 0.45011 -0.05822 -0.31217 0.02724  195 LEU A CD1 
1566 C CD2 . LEU A 195 ? 1.04240 0.34949 0.48460 -0.05850 -0.31238 0.02639  195 LEU A CD2 
1567 N N   . LEU A 196 ? 0.98372 0.29832 0.44647 -0.05590 -0.32285 0.02777  196 LEU A N   
1568 C CA  . LEU A 196 ? 1.03080 0.34872 0.49926 -0.05483 -0.32442 0.02753  196 LEU A CA  
1569 C C   . LEU A 196 ? 0.98564 0.30642 0.46128 -0.05430 -0.32777 0.02801  196 LEU A C   
1570 O O   . LEU A 196 ? 0.99931 0.32085 0.47796 -0.05367 -0.32979 0.02793  196 LEU A O   
1571 C CB  . LEU A 196 ? 1.00334 0.31482 0.46414 -0.05469 -0.32482 0.02702  196 LEU A CB  
1572 C CG  . LEU A 196 ? 0.98046 0.28838 0.43358 -0.05515 -0.32176 0.02644  196 LEU A CG  
1573 C CD1 . LEU A 196 ? 1.03056 0.33205 0.47648 -0.05479 -0.32251 0.02588  196 LEU A CD1 
1574 C CD2 . LEU A 196 ? 1.02219 0.33679 0.48114 -0.05470 -0.31947 0.02611  196 LEU A CD2 
1575 N N   . GLY A 197 ? 1.00708 0.32918 0.48530 -0.05455 -0.32851 0.02849  197 GLY A N   
1576 C CA  . GLY A 197 ? 0.99258 0.31748 0.47789 -0.05404 -0.33177 0.02889  197 GLY A CA  
1577 C C   . GLY A 197 ? 1.10514 0.42449 0.58710 -0.05389 -0.33513 0.02895  197 GLY A C   
1578 O O   . GLY A 197 ? 1.03184 0.35366 0.51989 -0.05342 -0.33795 0.02915  197 GLY A O   
1579 N N   . GLN A 198 ? 1.08739 0.39909 0.55956 -0.05434 -0.33491 0.02877  198 GLN A N   
1580 C CA  . GLN A 198 ? 1.04859 0.35421 0.51658 -0.05417 -0.33810 0.02878  198 GLN A CA  
1581 C C   . GLN A 198 ? 1.20684 0.50783 0.67113 -0.05443 -0.33980 0.02905  198 GLN A C   
1582 O O   . GLN A 198 ? 1.17819 0.47195 0.63505 -0.05456 -0.34125 0.02895  198 GLN A O   
1583 C CB  . GLN A 198 ? 1.00062 0.30038 0.45993 -0.05434 -0.33693 0.02830  198 GLN A CB  
1584 C CG  . GLN A 198 ? 1.04177 0.34489 0.50446 -0.05379 -0.33635 0.02794  198 GLN A CG  
1585 C CD  . GLN A 198 ? 1.13481 0.43165 0.58821 -0.05386 -0.33500 0.02737  198 GLN A CD  
1586 O OE1 . GLN A 198 ? 1.22762 0.51704 0.67260 -0.05422 -0.33568 0.02731  198 GLN A OE1 
1587 N NE2 . GLN A 198 ? 1.17287 0.47238 0.62750 -0.05345 -0.33312 0.02689  198 GLN A NE2 
1588 N N   . LEU A 199 ? 1.14155 0.44620 0.61041 -0.05444 -0.33961 0.02934  199 LEU A N   
1589 C CA  . LEU A 199 ? 1.10883 0.40927 0.57486 -0.05446 -0.34159 0.02953  199 LEU A CA  
1590 C C   . LEU A 199 ? 1.06086 0.36414 0.53480 -0.05368 -0.34556 0.02972  199 LEU A C   
1591 O O   . LEU A 199 ? 1.09605 0.40527 0.57790 -0.05333 -0.34614 0.02980  199 LEU A O   
1592 C CB  . LEU A 199 ? 1.03031 0.33226 0.49566 -0.05494 -0.33898 0.02967  199 LEU A CB  
1593 C CG  . LEU A 199 ? 1.12069 0.41895 0.57736 -0.05600 -0.33524 0.02955  199 LEU A CG  
1594 C CD1 . LEU A 199 ? 1.00669 0.30775 0.46446 -0.05649 -0.33284 0.02976  199 LEU A CD1 
1595 C CD2 . LEU A 199 ? 1.05171 0.34040 0.49740 -0.05653 -0.33600 0.02948  199 LEU A CD2 
1596 N N   . SER A 200 ? 1.00349 0.30196 0.47470 -0.05344 -0.34835 0.02977  200 SER A N   
1597 C CA  . SER A 200 ? 1.01776 0.31816 0.49604 -0.05269 -0.35253 0.02989  200 SER A CA  
1598 C C   . SER A 200 ? 1.08497 0.39385 0.57326 -0.05241 -0.35185 0.03005  200 SER A C   
1599 O O   . SER A 200 ? 1.06179 0.37313 0.54979 -0.05268 -0.34862 0.03006  200 SER A O   
1600 C CB  . SER A 200 ? 1.00957 0.30368 0.48307 -0.05239 -0.35506 0.02980  200 SER A CB  
1601 O OG  . SER A 200 ? 1.15664 0.45095 0.62847 -0.05254 -0.35295 0.02981  200 SER A OG  
1602 N N   . ARG A 201 ? 0.98654 0.29908 0.48261 -0.05197 -0.35483 0.03018  201 ARG A N   
1603 C CA  . ARG A 201 ? 1.06916 0.38944 0.57475 -0.05170 -0.35450 0.03034  201 ARG A CA  
1604 C C   . ARG A 201 ? 1.16576 0.48587 0.67104 -0.05140 -0.35396 0.03024  201 ARG A C   
1605 O O   . ARG A 201 ? 1.09502 0.41970 0.60274 -0.05153 -0.35084 0.03028  201 ARG A O   
1606 C CB  . ARG A 201 ? 1.04348 0.36611 0.55643 -0.05139 -0.35859 0.03053  201 ARG A CB  
1607 C CG  . ARG A 201 ? 1.18037 0.51104 0.70348 -0.05121 -0.35851 0.03073  201 ARG A CG  
1608 C CD  . ARG A 201 ? 1.02906 0.36280 0.55752 -0.05149 -0.36018 0.03103  201 ARG A CD  
1609 N NE  . ARG A 201 ? 1.24869 0.58256 0.77363 -0.05190 -0.35717 0.03098  201 ARG A NE  
1610 C CZ  . ARG A 201 ? 1.17689 0.51649 0.70557 -0.05203 -0.35409 0.03101  201 ARG A CZ  
1611 N NH1 . ARG A 201 ? 1.12203 0.46788 0.65813 -0.05185 -0.35346 0.03116  201 ARG A NH1 
1612 N NH2 . ARG A 201 ? 1.04874 0.38756 0.57350 -0.05226 -0.35169 0.03084  201 ARG A NH2 
1613 N N   . GLU A 202 ? 1.15707 0.47176 0.65913 -0.05098 -0.35698 0.03008  202 GLU A N   
1614 C CA  . GLU A 202 ? 1.02424 0.33796 0.52573 -0.05053 -0.35710 0.02991  202 GLU A CA  
1615 C C   . GLU A 202 ? 1.03499 0.34829 0.53092 -0.05119 -0.35244 0.02995  202 GLU A C   
1616 O O   . GLU A 202 ? 1.00809 0.32553 0.50762 -0.05105 -0.35070 0.02996  202 GLU A O   
1617 C CB  . GLU A 202 ? 1.01437 0.32059 0.51085 -0.05001 -0.36093 0.02964  202 GLU A CB  
1618 N N   . GLU A 203 ? 1.00055 0.30890 0.48802 -0.05192 -0.35062 0.02997  203 GLU A N   
1619 C CA  . GLU A 203 ? 0.99029 0.29776 0.47188 -0.05279 -0.34624 0.03004  203 GLU A CA  
1620 C C   . GLU A 203 ? 0.98254 0.29797 0.47046 -0.05301 -0.34311 0.03016  203 GLU A C   
1621 O O   . GLU A 203 ? 1.11751 0.43465 0.60456 -0.05340 -0.34020 0.03022  203 GLU A O   
1622 C CB  . GLU A 203 ? 1.00248 0.30325 0.47421 -0.05357 -0.34514 0.03001  203 GLU A CB  
1623 C CG  . GLU A 203 ? 1.24601 0.53802 0.70871 -0.05368 -0.34664 0.02992  203 GLU A CG  
1624 C CD  . GLU A 203 ? 1.42026 0.70566 0.87346 -0.05443 -0.34571 0.02986  203 GLU A CD  
1625 O OE1 . GLU A 203 ? 1.38822 0.67178 0.83523 -0.05547 -0.34217 0.02993  203 GLU A OE1 
1626 O OE2 . GLU A 203 ? 1.52588 0.80789 0.97784 -0.05400 -0.34859 0.02974  203 GLU A OE2 
1627 N N   . SER A 204 ? 1.02242 0.34221 0.51612 -0.05280 -0.34370 0.03018  204 SER A N   
1628 C CA  . SER A 204 ? 1.00670 0.33352 0.50575 -0.05296 -0.34071 0.03023  204 SER A CA  
1629 C C   . SER A 204 ? 0.99961 0.33301 0.50727 -0.05241 -0.34073 0.03032  204 SER A C   
1630 O O   . SER A 204 ? 1.06042 0.39799 0.56985 -0.05263 -0.33754 0.03034  204 SER A O   
1631 C CB  . SER A 204 ? 1.08609 0.41506 0.58832 -0.05285 -0.34151 0.03020  204 SER A CB  
1632 O OG  . SER A 204 ? 0.96855 0.29199 0.46254 -0.05335 -0.34057 0.03003  204 SER A OG  
1633 N N   . ASP A 205 ? 0.95632 0.29052 0.46927 -0.05169 -0.34439 0.03033  205 ASP A N   
1634 C CA  . ASP A 205 ? 1.04495 0.38453 0.56538 -0.05111 -0.34465 0.03034  205 ASP A CA  
1635 C C   . ASP A 205 ? 1.01117 0.34858 0.52729 -0.05117 -0.34284 0.03025  205 ASP A C   
1636 O O   . ASP A 205 ? 1.16345 0.50571 0.68348 -0.05107 -0.34065 0.03027  205 ASP A O   
1637 C CB  . ASP A 205 ? 1.00040 0.34012 0.52639 -0.05037 -0.34932 0.03029  205 ASP A CB  
1638 C CG  . ASP A 205 ? 0.99954 0.34269 0.53136 -0.05044 -0.35102 0.03050  205 ASP A CG  
1639 O OD1 . ASP A 205 ? 1.06689 0.41543 0.60249 -0.05070 -0.34850 0.03064  205 ASP A OD1 
1640 O OD2 . ASP A 205 ? 1.14936 0.48960 0.68178 -0.05025 -0.35495 0.03051  205 ASP A OD2 
1641 N N   . GLN A 206 ? 1.07865 0.40855 0.58645 -0.05137 -0.34375 0.03016  206 GLN A N   
1642 C CA  . GLN A 206 ? 1.02885 0.35583 0.53143 -0.05160 -0.34198 0.03012  206 GLN A CA  
1643 C C   . GLN A 206 ? 1.03347 0.36231 0.53298 -0.05260 -0.33730 0.03031  206 GLN A C   
1644 O O   . GLN A 206 ? 1.09195 0.42273 0.59193 -0.05272 -0.33525 0.03036  206 GLN A O   
1645 C CB  . GLN A 206 ? 1.03125 0.34924 0.52462 -0.05175 -0.34373 0.03001  206 GLN A CB  
1646 C CG  . GLN A 206 ? 0.98055 0.29482 0.46833 -0.05196 -0.34244 0.02998  206 GLN A CG  
1647 C CD  . GLN A 206 ? 1.05513 0.37299 0.54961 -0.05089 -0.34389 0.02973  206 GLN A CD  
1648 O OE1 . GLN A 206 ? 1.05055 0.36920 0.55036 -0.04981 -0.34765 0.02943  206 GLN A OE1 
1649 N NE2 . GLN A 206 ? 0.97292 0.29282 0.46708 -0.05120 -0.34101 0.02982  206 GLN A NE2 
1650 N N   . LEU A 207 ? 0.99697 0.32513 0.49332 -0.05331 -0.33568 0.03037  207 LEU A N   
1651 C CA  . LEU A 207 ? 1.01715 0.34673 0.51040 -0.05427 -0.33147 0.03046  207 LEU A CA  
1652 C C   . LEU A 207 ? 1.08639 0.42463 0.58854 -0.05388 -0.32973 0.03047  207 LEU A C   
1653 O O   . LEU A 207 ? 1.19333 0.53360 0.69462 -0.05441 -0.32662 0.03053  207 LEU A O   
1654 C CB  . LEU A 207 ? 0.96252 0.28864 0.44992 -0.05496 -0.33051 0.03038  207 LEU A CB  
1655 C CG  . LEU A 207 ? 0.97668 0.30265 0.45918 -0.05607 -0.32643 0.03037  207 LEU A CG  
1656 C CD1 . LEU A 207 ? 0.99437 0.31625 0.47012 -0.05702 -0.32469 0.03057  207 LEU A CD1 
1657 C CD2 . LEU A 207 ? 1.01031 0.33181 0.48638 -0.05661 -0.32598 0.03017  207 LEU A CD2 
1658 N N   . TRP A 208 ? 1.00859 0.35176 0.51912 -0.05303 -0.33175 0.03042  208 TRP A N   
1659 C CA  . TRP A 208 ? 1.04567 0.39693 0.56512 -0.05254 -0.33055 0.03043  208 TRP A CA  
1660 C C   . TRP A 208 ? 1.04696 0.39997 0.56855 -0.05222 -0.33003 0.03045  208 TRP A C   
1661 O O   . TRP A 208 ? 1.03843 0.39498 0.56115 -0.05246 -0.32700 0.03048  208 TRP A O   
1662 C CB  . TRP A 208 ? 1.02541 0.38031 0.55272 -0.05179 -0.33355 0.03043  208 TRP A CB  
1663 C CG  . TRP A 208 ? 1.05489 0.41776 0.59167 -0.05126 -0.33291 0.03047  208 TRP A CG  
1664 C CD1 . TRP A 208 ? 0.92511 0.29303 0.46574 -0.05130 -0.33091 0.03045  208 TRP A CD1 
1665 C CD2 . TRP A 208 ? 1.10677 0.47316 0.65022 -0.05052 -0.33443 0.03046  208 TRP A CD2 
1666 N NE1 . TRP A 208 ? 0.90210 0.27650 0.45126 -0.05072 -0.33098 0.03050  208 TRP A NE1 
1667 C CE2 . TRP A 208 ? 1.07710 0.45070 0.62816 -0.05025 -0.33312 0.03051  208 TRP A CE2 
1668 C CE3 . TRP A 208 ? 0.96033 0.32421 0.50382 -0.05001 -0.33684 0.03036  208 TRP A CE3 
1669 C CZ2 . TRP A 208 ? 0.97774 0.35608 0.53636 -0.04957 -0.33409 0.03049  208 TRP A CZ2 
1670 C CZ3 . TRP A 208 ? 0.93052 0.29907 0.48158 -0.04925 -0.33788 0.03027  208 TRP A CZ3 
1671 C CH2 . TRP A 208 ? 0.97624 0.35195 0.53475 -0.04907 -0.33648 0.03036  208 TRP A CH2 
1672 N N   . PHE A 209 ? 1.05046 0.40060 0.57230 -0.05162 -0.33311 0.03038  209 PHE A N   
1673 C CA  . PHE A 209 ? 1.09337 0.44447 0.61688 -0.05116 -0.33297 0.03029  209 PHE A CA  
1674 C C   . PHE A 209 ? 1.08416 0.43180 0.59984 -0.05209 -0.32981 0.03042  209 PHE A C   
1675 O O   . PHE A 209 ? 1.08055 0.43121 0.59820 -0.05203 -0.32789 0.03044  209 PHE A O   
1676 C CB  . PHE A 209 ? 1.09155 0.43894 0.61546 -0.05030 -0.33709 0.03005  209 PHE A CB  
1677 C CG  . PHE A 209 ? 1.01163 0.35889 0.53619 -0.04971 -0.33717 0.02983  209 PHE A CG  
1678 C CD1 . PHE A 209 ? 1.00799 0.36111 0.54124 -0.04878 -0.33794 0.02962  209 PHE A CD1 
1679 C CD2 . PHE A 209 ? 1.10070 0.44172 0.61688 -0.05012 -0.33644 0.02981  209 PHE A CD2 
1680 C CE1 . PHE A 209 ? 0.96224 0.31501 0.49587 -0.04816 -0.33803 0.02932  209 PHE A CE1 
1681 C CE2 . PHE A 209 ? 1.03730 0.37792 0.55376 -0.04956 -0.33651 0.02956  209 PHE A CE2 
1682 C CZ  . PHE A 209 ? 0.94534 0.29185 0.47058 -0.04851 -0.33733 0.02927  209 PHE A CZ  
1683 N N   . ASP A 210 ? 1.00769 0.34871 0.51419 -0.05303 -0.32929 0.03053  210 ASP A N   
1684 C CA  . ASP A 210 ? 1.10507 0.44183 0.60331 -0.05415 -0.32659 0.03071  210 ASP A CA  
1685 C C   . ASP A 210 ? 1.04754 0.38830 0.54601 -0.05503 -0.32263 0.03085  210 ASP A C   
1686 O O   . ASP A 210 ? 1.01870 0.35939 0.51465 -0.05568 -0.32030 0.03100  210 ASP A O   
1687 C CB  . ASP A 210 ? 1.10881 0.43699 0.59687 -0.05500 -0.32725 0.03077  210 ASP A CB  
1688 C CG  . ASP A 210 ? 1.14098 0.46411 0.62732 -0.05417 -0.33098 0.03059  210 ASP A CG  
1689 O OD1 . ASP A 210 ? 1.17302 0.49751 0.66303 -0.05329 -0.33225 0.03043  210 ASP A OD1 
1690 O OD2 . ASP A 210 ? 1.00693 0.32453 0.48810 -0.05433 -0.33273 0.03055  210 ASP A OD2 
1691 N N   . LYS A 211 ? 1.08336 0.42732 0.58457 -0.05507 -0.32192 0.03076  211 LYS A N   
1692 C CA  . LYS A 211 ? 1.15171 0.50016 0.65448 -0.05561 -0.31852 0.03076  211 LYS A CA  
1693 C C   . LYS A 211 ? 1.07689 0.43227 0.58782 -0.05483 -0.31777 0.03076  211 LYS A C   
1694 O O   . LYS A 211 ? 0.94938 0.30631 0.45914 -0.05545 -0.31498 0.03085  211 LYS A O   
1695 C CB  . LYS A 211 ? 0.97401 0.32481 0.47920 -0.05542 -0.31844 0.03055  211 LYS A CB  
1696 C CG  . LYS A 211 ? 0.95238 0.29643 0.44881 -0.05629 -0.31844 0.03048  211 LYS A CG  
1697 C CD  . LYS A 211 ? 0.93864 0.28491 0.43832 -0.05576 -0.31915 0.03022  211 LYS A CD  
1698 C CE  . LYS A 211 ? 0.94211 0.28167 0.43279 -0.05657 -0.31885 0.03006  211 LYS A CE  
1699 N NZ  . LYS A 211 ? 0.97758 0.31893 0.47126 -0.05593 -0.31976 0.02977  211 LYS A NZ  
1700 N N   . HIS A 212 ? 1.04325 0.40272 0.56235 -0.05355 -0.32024 0.03064  212 HIS A N   
1701 C CA  . HIS A 212 ? 0.93183 0.29753 0.45850 -0.05276 -0.31966 0.03060  212 HIS A CA  
1702 C C   . HIS A 212 ? 1.12454 0.48732 0.64699 -0.05308 -0.31878 0.03070  212 HIS A C   
1703 O O   . HIS A 212 ? 1.11769 0.48355 0.64101 -0.05339 -0.31608 0.03077  212 HIS A O   
1704 C CB  . HIS A 212 ? 0.94268 0.31200 0.47782 -0.05147 -0.32288 0.03045  212 HIS A CB  
1705 C CG  . HIS A 212 ? 1.04169 0.41732 0.58402 -0.05109 -0.32245 0.03040  212 HIS A CG  
1706 N ND1 . HIS A 212 ? 1.04338 0.42156 0.59233 -0.05033 -0.32539 0.03036  212 HIS A ND1 
1707 C CD2 . HIS A 212 ? 0.89217 0.27177 0.43589 -0.05139 -0.31955 0.03037  212 HIS A CD2 
1708 C CE1 . HIS A 212 ? 1.04633 0.42979 0.60033 -0.05021 -0.32420 0.03035  212 HIS A CE1 
1709 N NE2 . HIS A 212 ? 1.08384 0.46826 0.63480 -0.05075 -0.32065 0.03031  212 HIS A NE2 
1710 N N   . ARG A 213 ? 1.03182 0.38865 0.54969 -0.05299 -0.32105 0.03069  213 ARG A N   
1711 C CA  . ARG A 213 ? 1.03196 0.38557 0.54571 -0.05318 -0.32049 0.03074  213 ARG A CA  
1712 C C   . ARG A 213 ? 0.98396 0.33535 0.49046 -0.05480 -0.31681 0.03107  213 ARG A C   
1713 O O   . ARG A 213 ? 1.01256 0.36623 0.52004 -0.05495 -0.31491 0.03116  213 ARG A O   
1714 C CB  . ARG A 213 ? 1.08238 0.42865 0.59055 -0.05297 -0.32340 0.03063  213 ARG A CB  
1715 C CG  . ARG A 213 ? 1.08155 0.42269 0.58276 -0.05353 -0.32248 0.03074  213 ARG A CG  
1716 C CD  . ARG A 213 ? 1.04106 0.37450 0.53631 -0.05325 -0.32542 0.03056  213 ARG A CD  
1717 N NE  . ARG A 213 ? 1.17600 0.50503 0.66594 -0.05396 -0.32611 0.03069  213 ARG A NE  
1718 C CZ  . ARG A 213 ? 1.15242 0.47671 0.63349 -0.05560 -0.32383 0.03105  213 ARG A CZ  
1719 N NH1 . ARG A 213 ? 0.97949 0.30289 0.45604 -0.05684 -0.32073 0.03137  213 ARG A NH1 
1720 N NH2 . ARG A 213 ? 1.06678 0.38706 0.54337 -0.05607 -0.32469 0.03108  213 ARG A NH2 
1721 N N   . GLU A 214 ? 0.93308 0.27980 0.43228 -0.05603 -0.31596 0.03123  214 GLU A N   
1722 C CA  . GLU A 214 ? 0.96561 0.30962 0.45731 -0.05783 -0.31256 0.03152  214 GLU A CA  
1723 C C   . GLU A 214 ? 1.02281 0.37383 0.52007 -0.05786 -0.30987 0.03149  214 GLU A C   
1724 O O   . GLU A 214 ? 1.07009 0.42080 0.56476 -0.05869 -0.30779 0.03171  214 GLU A O   
1725 C CB  . GLU A 214 ? 1.05908 0.39846 0.54386 -0.05899 -0.31199 0.03154  214 GLU A CB  
1726 C CG  . GLU A 214 ? 1.07793 0.40844 0.55328 -0.05975 -0.31333 0.03168  214 GLU A CG  
1727 C CD  . GLU A 214 ? 1.22046 0.54652 0.68864 -0.06102 -0.31229 0.03167  214 GLU A CD  
1728 O OE1 . GLU A 214 ? 1.24855 0.57878 0.72031 -0.06091 -0.31117 0.03147  214 GLU A OE1 
1729 O OE2 . GLU A 214 ? 1.22644 0.54469 0.68530 -0.06207 -0.31256 0.03183  214 GLU A OE2 
1730 N N   . MET A 215 ? 0.93850 0.29535 0.44286 -0.05703 -0.30995 0.03124  215 MET A N   
1731 C CA  . MET A 215 ? 0.97953 0.34251 0.48847 -0.05706 -0.30734 0.03116  215 MET A CA  
1732 C C   . MET A 215 ? 0.99805 0.36588 0.51340 -0.05611 -0.30722 0.03117  215 MET A C   
1733 O O   . MET A 215 ? 1.01916 0.38886 0.53401 -0.05672 -0.30472 0.03128  215 MET A O   
1734 C CB  . MET A 215 ? 0.93953 0.30714 0.45427 -0.05630 -0.30762 0.03085  215 MET A CB  
1735 C CG  . MET A 215 ? 1.06847 0.44258 0.58851 -0.05607 -0.30521 0.03067  215 MET A CG  
1736 S SD  . MET A 215 ? 0.94926 0.33162 0.48149 -0.05419 -0.30645 0.03053  215 MET A SD  
1737 C CE  . MET A 215 ? 1.01363 0.39532 0.54918 -0.05326 -0.31013 0.03044  215 MET A CE  
1738 N N   . LEU A 216 ? 1.01352 0.38345 0.53501 -0.05463 -0.30993 0.03102  216 LEU A N   
1739 C CA  . LEU A 216 ? 0.93508 0.30991 0.46339 -0.05352 -0.31000 0.03091  216 LEU A CA  
1740 C C   . LEU A 216 ? 1.07314 0.44399 0.59587 -0.05413 -0.30912 0.03110  216 LEU A C   
1741 O O   . LEU A 216 ? 1.02084 0.39549 0.54753 -0.05361 -0.30808 0.03105  216 LEU A O   
1742 C CB  . LEU A 216 ? 0.89426 0.27094 0.42931 -0.05198 -0.31348 0.03063  216 LEU A CB  
1743 C CG  . LEU A 216 ? 1.04604 0.41670 0.57730 -0.05166 -0.31636 0.03055  216 LEU A CG  
1744 C CD1 . LEU A 216 ? 0.96476 0.33584 0.49764 -0.05093 -0.31655 0.03037  216 LEU A CD1 
1745 C CD2 . LEU A 216 ? 1.05051 0.42204 0.58698 -0.05060 -0.31991 0.03029  216 LEU A CD2 
1746 N N   . ASP A 217 ? 1.06605 0.42935 0.57981 -0.05517 -0.30959 0.03131  217 ASP A N   
1747 C CA  . ASP A 217 ? 0.99118 0.34976 0.49848 -0.05595 -0.30874 0.03155  217 ASP A CA  
1748 C C   . ASP A 217 ? 0.98318 0.34057 0.48445 -0.05792 -0.30521 0.03193  217 ASP A C   
1749 O O   . ASP A 217 ? 1.17789 0.53393 0.67605 -0.05860 -0.30374 0.03216  217 ASP A O   
1750 C CB  . ASP A 217 ? 0.98601 0.33677 0.48653 -0.05609 -0.31112 0.03156  217 ASP A CB  
1751 C CG  . ASP A 217 ? 0.96899 0.32020 0.47493 -0.05417 -0.31478 0.03108  217 ASP A CG  
1752 O OD1 . ASP A 217 ? 0.97739 0.33416 0.49136 -0.05285 -0.31529 0.03077  217 ASP A OD1 
1753 O OD2 . ASP A 217 ? 0.95161 0.29730 0.45344 -0.05405 -0.31717 0.03098  217 ASP A OD2 
1754 N N   . HIS A 218 ? 1.00396 0.36159 0.50352 -0.05880 -0.30402 0.03194  218 HIS A N   
1755 C CA  . HIS A 218 ? 0.95405 0.30988 0.44733 -0.06082 -0.30085 0.03220  218 HIS A CA  
1756 C C   . HIS A 218 ? 0.98734 0.35019 0.48694 -0.06048 -0.29876 0.03210  218 HIS A C   
1757 O O   . HIS A 218 ? 0.98021 0.34163 0.47541 -0.06191 -0.29651 0.03238  218 HIS A O   
1758 C CB  . HIS A 218 ? 0.92144 0.27477 0.41068 -0.06171 -0.30049 0.03210  218 HIS A CB  
1759 C CG  . HIS A 218 ? 1.00939 0.35916 0.49067 -0.06399 -0.29765 0.03230  218 HIS A CG  
1760 N ND1 . HIS A 218 ? 1.03362 0.37696 0.50572 -0.06592 -0.29650 0.03275  218 HIS A ND1 
1761 C CD2 . HIS A 218 ? 0.94935 0.30056 0.43003 -0.06473 -0.29586 0.03209  218 HIS A CD2 
1762 C CE1 . HIS A 218 ? 1.04757 0.38861 0.51378 -0.06792 -0.29407 0.03283  218 HIS A CE1 
1763 N NE2 . HIS A 218 ? 1.01711 0.36287 0.48847 -0.06715 -0.29370 0.03239  218 HIS A NE2 
1764 N N   . VAL A 219 ? 1.06564 0.43551 0.57488 -0.05876 -0.29950 0.03173  219 VAL A N   
1765 C CA  . VAL A 219 ? 0.98326 0.35962 0.49821 -0.05842 -0.29745 0.03158  219 VAL A CA  
1766 C C   . VAL A 219 ? 0.91988 0.30228 0.44408 -0.05650 -0.29848 0.03139  219 VAL A C   
1767 O O   . VAL A 219 ? 0.89765 0.28528 0.42652 -0.05613 -0.29681 0.03128  219 VAL A O   
1768 C CB  . VAL A 219 ? 1.02793 0.40744 0.54533 -0.05838 -0.29653 0.03126  219 VAL A CB  
1769 C CG1 . VAL A 219 ? 0.89383 0.26738 0.40165 -0.06043 -0.29500 0.03137  219 VAL A CG1 
1770 C CG2 . VAL A 219 ? 0.98086 0.36251 0.50380 -0.05690 -0.29901 0.03098  219 VAL A CG2 
1771 N N   . GLN A 220 ? 0.85164 0.29724 0.47833 -0.02658 -0.32576 0.01549  220 GLN A N   
1772 C CA  . GLN A 220 ? 0.94485 0.39237 0.57426 -0.02654 -0.32599 0.01565  220 GLN A CA  
1773 C C   . GLN A 220 ? 0.99496 0.44389 0.62575 -0.02683 -0.32545 0.01590  220 GLN A C   
1774 O O   . GLN A 220 ? 0.98043 0.43075 0.61273 -0.02724 -0.32511 0.01617  220 GLN A O   
1775 C CB  . GLN A 220 ? 0.98714 0.43551 0.61783 -0.02680 -0.32612 0.01582  220 GLN A CB  
1776 C CG  . GLN A 220 ? 1.02538 0.47210 0.65443 -0.02662 -0.32661 0.01560  220 GLN A CG  
1777 C CD  . GLN A 220 ? 1.11078 0.55646 0.73835 -0.02714 -0.32632 0.01573  220 GLN A CD  
1778 O OE1 . GLN A 220 ? 1.05431 0.50100 0.68284 -0.02773 -0.32586 0.01608  220 GLN A OE1 
1779 N NE2 . GLN A 220 ? 1.17092 0.61429 0.79600 -0.02690 -0.32671 0.01544  220 GLN A NE2 
1780 N N   . PRO A 221 ? 1.02761 0.47605 0.65786 -0.02658 -0.32549 0.01579  221 PRO A N   
1781 C CA  . PRO A 221 ? 0.89382 0.34324 0.52501 -0.02687 -0.32501 0.01600  221 PRO A CA  
1782 C C   . PRO A 221 ? 0.92747 0.37820 0.56094 -0.02680 -0.32536 0.01611  221 PRO A C   
1783 O O   . PRO A 221 ? 0.82482 0.27547 0.45910 -0.02643 -0.32616 0.01599  221 PRO A O   
1784 C CB  . PRO A 221 ? 0.86091 0.30894 0.49051 -0.02657 -0.32514 0.01580  221 PRO A CB  
1785 C CG  . PRO A 221 ? 0.81126 0.25806 0.44013 -0.02596 -0.32605 0.01550  221 PRO A CG  
1786 C CD  . PRO A 221 ? 0.86901 0.31570 0.49757 -0.02599 -0.32608 0.01545  221 PRO A CD  
1787 N N   . ASP A 222 ? 0.90922 0.36093 0.54356 -0.02715 -0.32484 0.01631  222 ASP A N   
1788 C CA  . ASP A 222 ? 0.86350 0.31608 0.49961 -0.02709 -0.32516 0.01638  222 ASP A CA  
1789 C C   . ASP A 222 ? 0.88760 0.33955 0.52378 -0.02688 -0.32566 0.01631  222 ASP A C   
1790 O O   . ASP A 222 ? 0.80392 0.25606 0.44145 -0.02673 -0.32636 0.01630  222 ASP A O   
1791 C CB  . ASP A 222 ? 0.82924 0.28277 0.46590 -0.02747 -0.32451 0.01657  222 ASP A CB  
1792 C CG  . ASP A 222 ? 0.81777 0.27181 0.45457 -0.02771 -0.32427 0.01667  222 ASP A CG  
1793 O OD1 . ASP A 222 ? 0.82620 0.28053 0.46384 -0.02757 -0.32472 0.01665  222 ASP A OD1 
1794 O OD2 . ASP A 222 ? 0.83914 0.29314 0.47521 -0.02804 -0.32376 0.01678  222 ASP A OD2 
1795 N N   . ILE A 223 ? 0.89696 0.34798 0.53166 -0.02689 -0.32541 0.01625  223 ILE A N   
1796 C CA  . ILE A 223 ? 0.80606 0.25618 0.44063 -0.02672 -0.32600 0.01618  223 ILE A CA  
1797 C C   . ILE A 223 ? 0.82551 0.27414 0.45829 -0.02641 -0.32627 0.01598  223 ILE A C   
1798 O O   . ILE A 223 ? 0.80856 0.25671 0.43964 -0.02653 -0.32555 0.01594  223 ILE A O   
1799 C CB  . ILE A 223 ? 0.80548 0.25564 0.43976 -0.02703 -0.32542 0.01629  223 ILE A CB  
1800 C CG1 . ILE A 223 ? 0.84471 0.29598 0.48032 -0.02723 -0.32519 0.01642  223 ILE A CG1 
1801 C CG2 . ILE A 223 ? 0.80679 0.25576 0.44088 -0.02688 -0.32620 0.01623  223 ILE A CG2 
1802 C CD1 . ILE A 223 ? 0.80368 0.25476 0.43869 -0.02747 -0.32463 0.01648  223 ILE A CD1 
1803 N N   . ILE A 224 ? 0.89667 0.34436 0.52974 -0.02600 -0.32745 0.01583  224 ILE A N   
1804 C CA  . ILE A 224 ? 0.83214 0.27803 0.46335 -0.02559 -0.32795 0.01558  224 ILE A CA  
1805 C C   . ILE A 224 ? 0.85616 0.30116 0.48721 -0.02564 -0.32839 0.01561  224 ILE A C   
1806 O O   . ILE A 224 ? 0.87592 0.32076 0.50852 -0.02554 -0.32955 0.01563  224 ILE A O   
1807 C CB  . ILE A 224 ? 1.02917 0.47428 0.66064 -0.02500 -0.32921 0.01535  224 ILE A CB  
1808 C CG1 . ILE A 224 ? 0.95864 0.40409 0.58952 -0.02493 -0.32874 0.01527  224 ILE A CG1 
1809 C CG2 . ILE A 224 ? 0.89304 0.33597 0.52263 -0.02448 -0.33004 0.01506  224 ILE A CG2 
1810 C CD1 . ILE A 224 ? 0.96010 0.40419 0.58813 -0.02483 -0.32809 0.01507  224 ILE A CD1 
1811 N N   . TRP A 225 ? 0.83687 0.28113 0.46603 -0.02581 -0.32757 0.01560  225 TRP A N   
1812 C CA  . TRP A 225 ? 0.91433 0.35752 0.54298 -0.02588 -0.32792 0.01561  225 TRP A CA  
1813 C C   . TRP A 225 ? 0.87609 0.31712 0.50303 -0.02535 -0.32889 0.01532  225 TRP A C   
1814 O O   . TRP A 225 ? 0.88722 0.32720 0.51183 -0.02514 -0.32837 0.01513  225 TRP A O   
1815 C CB  . TRP A 225 ? 0.88826 0.33163 0.51569 -0.02632 -0.32659 0.01573  225 TRP A CB  
1816 C CG  . TRP A 225 ? 0.83800 0.28046 0.46516 -0.02648 -0.32689 0.01579  225 TRP A CG  
1817 C CD1 . TRP A 225 ? 0.84698 0.29008 0.47538 -0.02681 -0.32685 0.01597  225 TRP A CD1 
1818 C CD2 . TRP A 225 ? 0.87998 0.32040 0.50525 -0.02629 -0.32733 0.01564  225 TRP A CD2 
1819 N NE1 . TRP A 225 ? 0.84243 0.28402 0.46987 -0.02687 -0.32726 0.01596  225 TRP A NE1 
1820 C CE2 . TRP A 225 ? 0.86183 0.30182 0.48744 -0.02657 -0.32757 0.01576  225 TRP A CE2 
1821 C CE3 . TRP A 225 ? 0.86165 0.30031 0.48474 -0.02587 -0.32761 0.01537  225 TRP A CE3 
1822 C CZ2 . TRP A 225 ? 0.87370 0.31165 0.49769 -0.02650 -0.32809 0.01567  225 TRP A CZ2 
1823 C CZ3 . TRP A 225 ? 0.82104 0.25768 0.44249 -0.02575 -0.32812 0.01526  225 TRP A CZ3 
1824 C CH2 . TRP A 225 ? 0.89672 0.33308 0.51871 -0.02609 -0.32836 0.01542  225 TRP A CH2 
1825 N N   . ASN A 226 ? 0.83129 0.27152 0.45938 -0.02512 -0.33042 0.01528  226 ASN A N   
1826 C CA  . ASN A 226 ? 0.92153 0.35945 0.54810 -0.02453 -0.33167 0.01497  226 ASN A CA  
1827 C C   . ASN A 226 ? 0.95881 0.39525 0.58452 -0.02469 -0.33210 0.01499  226 ASN A C   
1828 O O   . ASN A 226 ? 0.83864 0.27553 0.46611 -0.02507 -0.33260 0.01521  226 ASN A O   
1829 C CB  . ASN A 226 ? 0.88958 0.32716 0.51787 -0.02406 -0.33349 0.01484  226 ASN A CB  
1830 C CG  . ASN A 226 ? 0.98663 0.42510 0.61511 -0.02378 -0.33317 0.01475  226 ASN A CG  
1831 O OD1 . ASN A 226 ? 0.99827 0.43597 0.62440 -0.02349 -0.33246 0.01453  226 ASN A OD1 
1832 N ND2 . ASN A 226 ? 0.83725 0.27711 0.46831 -0.02387 -0.33375 0.01488  226 ASN A ND2 
1833 N N   . ASP A 227 ? 0.91071 0.34517 0.53361 -0.02435 -0.33201 0.01474  227 ASP A N   
1834 C CA  . ASP A 227 ? 0.89250 0.32511 0.51422 -0.02441 -0.33259 0.01471  227 ASP A CA  
1835 C C   . ASP A 227 ? 0.94613 0.37697 0.56865 -0.02393 -0.33493 0.01452  227 ASP A C   
1836 O O   . ASP A 227 ? 0.86230 0.29387 0.48689 -0.02370 -0.33598 0.01450  227 ASP A O   
1837 C CB  . ASP A 227 ? 0.92867 0.35979 0.54694 -0.02430 -0.33147 0.01452  227 ASP A CB  
1838 C CG  . ASP A 227 ? 0.89757 0.32741 0.51461 -0.02460 -0.33134 0.01460  227 ASP A CG  
1839 O OD1 . ASP A 227 ? 0.93940 0.36937 0.55822 -0.02492 -0.33220 0.01479  227 ASP A OD1 
1840 O OD2 . ASP A 227 ? 0.91820 0.34676 0.53238 -0.02452 -0.33041 0.01445  227 ASP A OD2 
1841 N N   . PHE A 228 ? 0.84683 0.27537 0.46786 -0.02380 -0.33585 0.01437  228 PHE A N   
1842 C CA  . PHE A 228 ? 0.83522 0.26199 0.45746 -0.02345 -0.33842 0.01422  228 PHE A CA  
1843 C C   . PHE A 228 ? 0.87013 0.29507 0.49100 -0.02250 -0.33967 0.01377  228 PHE A C   
1844 O O   . PHE A 228 ? 0.83837 0.26338 0.45717 -0.02213 -0.33843 0.01359  228 PHE A O   
1845 C CB  . PHE A 228 ? 0.88481 0.30973 0.50601 -0.02375 -0.33896 0.01426  228 PHE A CB  
1846 C CG  . PHE A 228 ? 0.83993 0.26233 0.45731 -0.02331 -0.33864 0.01394  228 PHE A CG  
1847 C CD1 . PHE A 228 ? 0.84434 0.26710 0.45919 -0.02347 -0.33640 0.01396  228 PHE A CD1 
1848 C CD2 . PHE A 228 ? 0.84393 0.26340 0.46023 -0.02274 -0.34073 0.01360  228 PHE A CD2 
1849 C CE1 . PHE A 228 ? 0.92961 0.34985 0.54080 -0.02306 -0.33615 0.01365  228 PHE A CE1 
1850 C CE2 . PHE A 228 ? 0.84697 0.26388 0.45948 -0.02228 -0.34046 0.01328  228 PHE A CE2 
1851 C CZ  . PHE A 228 ? 0.90909 0.32637 0.51900 -0.02245 -0.33812 0.01330  228 PHE A CZ  
1852 N N   . SER A 229 ? 0.91234 0.33536 0.53412 -0.02212 -0.34219 0.01358  229 SER A N   
1853 C CA  . SER A 229 ? 0.91231 0.33312 0.53286 -0.02108 -0.34388 0.01308  229 SER A CA  
1854 C C   . SER A 229 ? 0.93210 0.35431 0.55483 -0.02075 -0.34449 0.01305  229 SER A C   
1855 O O   . SER A 229 ? 0.99772 0.41847 0.61866 -0.01985 -0.34506 0.01263  229 SER A O   
1856 C CB  . SER A 229 ? 0.89838 0.31710 0.51450 -0.02044 -0.34290 0.01270  229 SER A CB  
1857 O OG  . SER A 229 ? 1.05141 0.46710 0.66609 -0.01943 -0.34508 0.01218  229 SER A OG  
1858 N N   . LEU A 230 ? 0.84041 0.26515 0.46653 -0.02140 -0.34434 0.01344  230 LEU A N   
1859 C CA  . LEU A 230 ? 0.88930 0.31517 0.51771 -0.02109 -0.34523 0.01340  230 LEU A CA  
1860 C C   . LEU A 230 ? 0.99176 0.41595 0.62243 -0.02075 -0.34844 0.01322  230 LEU A C   
1861 O O   . LEU A 230 ? 0.94776 0.37076 0.57835 -0.01991 -0.34993 0.01285  230 LEU A O   
1862 C CB  . LEU A 230 ? 0.89847 0.32748 0.52932 -0.02187 -0.34380 0.01384  230 LEU A CB  
1863 C CG  . LEU A 230 ? 0.85880 0.28953 0.48792 -0.02230 -0.34088 0.01404  230 LEU A CG  
1864 C CD1 . LEU A 230 ? 0.82901 0.26250 0.46070 -0.02292 -0.33995 0.01441  230 LEU A CD1 
1865 C CD2 . LEU A 230 ? 0.95432 0.38435 0.58057 -0.02165 -0.33994 0.01372  230 LEU A CD2 
1866 N N   . ASP A 231 ? 0.93093 0.35504 0.56369 -0.02141 -0.34955 0.01346  231 ASP A N   
1867 C CA  . ASP A 231 ? 0.97511 0.39726 0.61007 -0.02120 -0.35290 0.01328  231 ASP A CA  
1868 C C   . ASP A 231 ? 1.02760 0.44914 0.66290 -0.02199 -0.35314 0.01355  231 ASP A C   
1869 O O   . ASP A 231 ? 0.93954 0.36201 0.57824 -0.02268 -0.35399 0.01378  231 ASP A O   
1870 C CB  . ASP A 231 ? 0.97758 0.40080 0.61634 -0.02117 -0.35468 0.01334  231 ASP A CB  
1871 C CG  . ASP A 231 ? 1.05512 0.47611 0.69620 -0.02087 -0.35842 0.01308  231 ASP A CG  
1872 O OD1 . ASP A 231 ? 0.96415 0.38258 0.60354 -0.02052 -0.35965 0.01278  231 ASP A OD1 
1873 O OD2 . ASP A 231 ? 1.09900 0.52074 0.74361 -0.02098 -0.36018 0.01315  231 ASP A OD2 
1874 N N   . SER A 232 ? 0.95831 0.37835 0.59029 -0.02191 -0.35211 0.01343  232 SER A N   
1875 C CA  . SER A 232 ? 0.86776 0.28739 0.50000 -0.02270 -0.35153 0.01355  232 SER A CA  
1876 C C   . SER A 232 ? 1.00514 0.42217 0.63725 -0.02241 -0.35225 0.01281  232 SER A C   
1877 O O   . SER A 232 ? 0.92006 0.33548 0.54804 -0.02219 -0.35141 0.01283  232 SER A O   
1878 C CB  . SER A 232 ? 0.84393 0.26469 0.47320 -0.02309 -0.34875 0.01392  232 SER A CB  
1879 O OG  . SER A 232 ? 0.97243 0.39226 0.59805 -0.02245 -0.34737 0.01360  232 SER A OG  
1880 N N   . PRO A 233 ? 0.98723 0.40361 0.62354 -0.02237 -0.35382 0.01210  233 PRO A N   
1881 C CA  . PRO A 233 ? 1.00744 0.42122 0.64359 -0.02210 -0.35456 0.01128  233 PRO A CA  
1882 C C   . PRO A 233 ? 0.99440 0.40882 0.63212 -0.02314 -0.35161 0.01096  233 PRO A C   
1883 O O   . PRO A 233 ? 1.03490 0.45179 0.67746 -0.02425 -0.34964 0.01090  233 PRO A O   
1884 C CB  . PRO A 233 ? 1.00836 0.42206 0.64975 -0.02208 -0.35670 0.01053  233 PRO A CB  
1885 C CG  . PRO A 233 ? 1.05800 0.47500 0.70417 -0.02294 -0.35577 0.01083  233 PRO A CG  
1886 C CD  . PRO A 233 ? 1.05504 0.47288 0.69655 -0.02255 -0.35521 0.01189  233 PRO A CD  
1887 N N   . GLY A 234 ? 0.98971 0.40168 0.62355 -0.02274 -0.35136 0.01072  234 GLY A N   
1888 C CA  . GLY A 234 ? 1.04009 0.45225 0.67503 -0.02362 -0.34859 0.01041  234 GLY A CA  
1889 C C   . GLY A 234 ? 0.91848 0.33080 0.54856 -0.02363 -0.34654 0.01110  234 GLY A C   
1890 O O   . GLY A 234 ? 0.87419 0.28632 0.50462 -0.02422 -0.34430 0.01087  234 GLY A O   
1891 N N   . TYR A 235 ? 0.88817 0.30051 0.51373 -0.02295 -0.34736 0.01184  235 TYR A N   
1892 C CA  . TYR A 235 ? 0.89614 0.30899 0.51762 -0.02311 -0.34537 0.01242  235 TYR A CA  
1893 C C   . TYR A 235 ? 0.92761 0.33768 0.54249 -0.02202 -0.34676 0.01257  235 TYR A C   
1894 O O   . TYR A 235 ? 0.85488 0.26530 0.46627 -0.02206 -0.34525 0.01292  235 TYR A O   
1895 C CB  . TYR A 235 ? 0.84848 0.26448 0.47155 -0.02364 -0.34445 0.01308  235 TYR A CB  
1896 C CG  . TYR A 235 ? 0.86823 0.28678 0.49735 -0.02471 -0.34268 0.01294  235 TYR A CG  
1897 C CD1 . TYR A 235 ? 0.91848 0.33808 0.55248 -0.02490 -0.34385 0.01268  235 TYR A CD1 
1898 C CD2 . TYR A 235 ? 0.90456 0.32436 0.53436 -0.02547 -0.33985 0.01308  235 TYR A CD2 
1899 C CE1 . TYR A 235 ? 0.91672 0.33843 0.55613 -0.02587 -0.34214 0.01253  235 TYR A CE1 
1900 C CE2 . TYR A 235 ? 0.84064 0.26240 0.47558 -0.02634 -0.33817 0.01297  235 TYR A CE2 
1901 C CZ  . TYR A 235 ? 0.88805 0.31076 0.52780 -0.02656 -0.33926 0.01269  235 TYR A CZ  
1902 O OH  . TYR A 235 ? 0.86576 0.29017 0.51051 -0.02741 -0.33750 0.01255  235 TYR A OH  
1903 N N   . CYS A 236 ? 0.87802 0.28541 0.49164 -0.02108 -0.34927 0.01215  236 CYS A N   
1904 C CA  . CYS A 236 ? 0.92482 0.32993 0.53342 -0.02002 -0.34918 0.01184  236 CYS A CA  
1905 C C   . CYS A 236 ? 0.92966 0.33069 0.53500 -0.01949 -0.35062 0.01141  236 CYS A C   
1906 O O   . CYS A 236 ? 1.00321 0.40176 0.60550 -0.01842 -0.35120 0.01086  236 CYS A O   
1907 C CB  . CYS A 236 ? 0.86383 0.26914 0.47309 -0.01916 -0.35008 0.01153  236 CYS A CB  
1908 S SG  . CYS A 236 ? 0.97059 0.38036 0.58245 -0.01964 -0.34787 0.01195  236 CYS A SG  
1909 N N   . ALA A 237 ? 0.97815 0.37992 0.58660 -0.02042 -0.34871 0.01107  237 ALA A N   
1910 C CA  . ALA A 237 ? 0.95469 0.35345 0.56145 -0.02016 -0.34844 0.01033  237 ALA A CA  
1911 C C   . ALA A 237 ? 0.94576 0.34189 0.55333 -0.01933 -0.35129 0.00955  237 ALA A C   
1912 O O   . ALA A 237 ? 1.01654 0.41425 0.62968 -0.01977 -0.35220 0.00924  237 ALA A O   
1913 C CB  . ALA A 237 ? 0.87295 0.26944 0.47273 -0.01949 -0.34788 0.01057  237 ALA A CB  
1914 N N   . ASP A 238 ? 0.88037 0.27252 0.48246 -0.01816 -0.35263 0.00920  238 ASP A N   
1915 C CA  . ASP A 238 ? 0.94187 0.33098 0.54427 -0.01724 -0.35545 0.00832  238 ASP A CA  
1916 C C   . ASP A 238 ? 0.99907 0.38506 0.59510 -0.01554 -0.35813 0.00865  238 ASP A C   
1917 O O   . ASP A 238 ? 1.04807 0.42999 0.64062 -0.01436 -0.35999 0.00800  238 ASP A O   
1918 C CB  . ASP A 238 ? 0.88878 0.27532 0.49078 -0.01731 -0.35474 0.00736  238 ASP A CB  
1919 C CG  . ASP A 238 ? 0.96258 0.35175 0.57033 -0.01894 -0.35186 0.00704  238 ASP A CG  
1920 O OD1 . ASP A 238 ? 1.01109 0.40296 0.62551 -0.01988 -0.35181 0.00679  238 ASP A OD1 
1921 O OD2 . ASP A 238 ? 0.89145 0.27974 0.49687 -0.01921 -0.34969 0.00701  238 ASP A OD2 
1922 N N   . PHE A 239 ? 0.94497 0.33359 0.54088 -0.01559 -0.35685 0.00921  239 PHE A N   
1923 C CA  . PHE A 239 ? 0.93123 0.31899 0.52457 -0.01438 -0.35644 0.00873  239 PHE A CA  
1924 C C   . PHE A 239 ? 0.93209 0.31928 0.52839 -0.01372 -0.35953 0.00842  239 PHE A C   
1925 O O   . PHE A 239 ? 1.02304 0.41245 0.62426 -0.01453 -0.36077 0.00882  239 PHE A O   
1926 C CB  . PHE A 239 ? 0.92698 0.31829 0.52032 -0.01487 -0.35307 0.00913  239 PHE A CB  
1927 C CG  . PHE A 239 ? 1.03227 0.42316 0.62344 -0.01382 -0.35249 0.00874  239 PHE A CG  
1928 C CD1 . PHE A 239 ? 0.94434 0.33264 0.53005 -0.01296 -0.35118 0.00827  239 PHE A CD1 
1929 C CD2 . PHE A 239 ? 0.98287 0.37586 0.57732 -0.01373 -0.35317 0.00884  239 PHE A CD2 
1930 C CE1 . PHE A 239 ? 1.04648 0.43417 0.62997 -0.01200 -0.35067 0.00789  239 PHE A CE1 
1931 C CE2 . PHE A 239 ? 0.97594 0.36839 0.56822 -0.01277 -0.35263 0.00847  239 PHE A CE2 
1932 C CZ  . PHE A 239 ? 1.07752 0.46728 0.66429 -0.01191 -0.35140 0.00799  239 PHE A CZ  
1933 N N   . ASP A 240 ? 0.90004 0.28399 0.49328 -0.01223 -0.36095 0.00769  240 ASP A N   
1934 C CA  . ASP A 240 ? 1.00018 0.38356 0.59624 -0.01150 -0.36394 0.00735  240 ASP A CA  
1935 C C   . ASP A 240 ? 1.07867 0.46588 0.67716 -0.01180 -0.36223 0.00774  240 ASP A C   
1936 O O   . ASP A 240 ? 1.14343 0.52979 0.73900 -0.01080 -0.36138 0.00738  240 ASP A O   
1937 C CB  . ASP A 240 ? 1.02924 0.40772 0.62124 -0.00970 -0.36622 0.00640  240 ASP A CB  
1938 C CG  . ASP A 240 ? 1.12163 0.49913 0.71670 -0.00892 -0.36975 0.00598  240 ASP A CG  
1939 O OD1 . ASP A 240 ? 1.15587 0.53545 0.75630 -0.00984 -0.37139 0.00635  240 ASP A OD1 
1940 O OD2 . ASP A 240 ? 1.34608 0.72060 0.93804 -0.00736 -0.37088 0.00526  240 ASP A OD2 
1941 N N   . GLY A 241 ? 1.01127 0.40231 0.61463 -0.01313 -0.36173 0.00843  241 GLY A N   
1942 C CA  . GLY A 241 ? 0.92489 0.31968 0.53077 -0.01354 -0.36009 0.00884  241 GLY A CA  
1943 C C   . GLY A 241 ? 0.97864 0.37630 0.59030 -0.01465 -0.36117 0.00938  241 GLY A C   
1944 O O   . GLY A 241 ? 1.01175 0.40880 0.62510 -0.01530 -0.36256 0.00953  241 GLY A O   
1945 N N   . PRO A 242 ? 0.97505 0.37558 0.58966 -0.01487 -0.36069 0.00965  242 PRO A N   
1946 C CA  . PRO A 242 ? 0.88953 0.29272 0.50945 -0.01588 -0.36165 0.01015  242 PRO A CA  
1947 C C   . PRO A 242 ? 0.98089 0.38749 0.60192 -0.01725 -0.35871 0.01087  242 PRO A C   
1948 O O   . PRO A 242 ? 0.86938 0.27801 0.49436 -0.01811 -0.35929 0.01130  242 PRO A O   
1949 C CB  . PRO A 242 ? 0.92467 0.32892 0.54607 -0.01525 -0.36214 0.01000  242 PRO A CB  
1950 C CG  . PRO A 242 ? 0.94071 0.34514 0.55799 -0.01472 -0.35934 0.00987  242 PRO A CG  
1951 C CD  . PRO A 242 ? 0.99535 0.39640 0.60800 -0.01411 -0.35926 0.00945  242 PRO A CD  
1952 N N   . CYS A 243 ? 0.91329 0.32014 0.53071 -0.01735 -0.35584 0.01095  243 CYS A N   
1953 C CA  . CYS A 243 ? 0.86013 0.27012 0.47836 -0.01851 -0.35303 0.01157  243 CYS A CA  
1954 C C   . CYS A 243 ? 0.96406 0.37745 0.58560 -0.01894 -0.35224 0.01193  243 CYS A C   
1955 O O   . CYS A 243 ? 0.86832 0.28413 0.49255 -0.01994 -0.35147 0.01244  243 CYS A O   
1956 C CB  . CYS A 243 ? 0.89729 0.30710 0.51697 -0.01944 -0.35364 0.01189  243 CYS A CB  
1957 S SG  . CYS A 243 ? 0.88230 0.29410 0.50041 -0.02046 -0.35014 0.01240  243 CYS A SG  
1958 N N   . ALA A 244 ? 0.96203 0.37537 0.58314 -0.01813 -0.35249 0.01164  244 ALA A N   
1959 C CA  . ALA A 244 ? 0.98549 0.40160 0.60975 -0.01840 -0.35221 0.01191  244 ALA A CA  
1960 C C   . ALA A 244 ? 0.90787 0.32398 0.52990 -0.01760 -0.35113 0.01162  244 ALA A C   
1961 O O   . ALA A 244 ? 0.95597 0.36941 0.57437 -0.01663 -0.35141 0.01112  244 ALA A O   
1962 C CB  . ALA A 244 ? 0.85482 0.27053 0.48300 -0.01831 -0.35539 0.01184  244 ALA A CB  
1963 N N   . VAL A 245 ? 0.99332 0.41226 0.61738 -0.01800 -0.34996 0.01192  245 VAL A N   
1964 C CA  . VAL A 245 ? 0.90417 0.32326 0.52695 -0.01731 -0.34938 0.01168  245 VAL A CA  
1965 C C   . VAL A 245 ? 0.89404 0.31293 0.51977 -0.01682 -0.35190 0.01152  245 VAL A C   
1966 O O   . VAL A 245 ? 0.86809 0.28815 0.49764 -0.01741 -0.35322 0.01181  245 VAL A O   
1967 C CB  . VAL A 245 ? 0.91023 0.33239 0.53319 -0.01807 -0.34651 0.01208  245 VAL A CB  
1968 C CG1 . VAL A 245 ? 0.96040 0.38244 0.58181 -0.01738 -0.34601 0.01180  245 VAL A CG1 
1969 C CG2 . VAL A 245 ? 0.84552 0.26784 0.46595 -0.01860 -0.34428 0.01223  245 VAL A CG2 
1970 N N   . ALA A 246 ? 0.85495 0.27211 0.47879 -0.01569 -0.35270 0.01104  246 ALA A N   
1971 C CA  . ALA A 246 ? 0.85637 0.27310 0.48274 -0.01509 -0.35516 0.01082  246 ALA A CA  
1972 C C   . ALA A 246 ? 0.90668 0.32680 0.53705 -0.01599 -0.35459 0.01133  246 ALA A C   
1973 O O   . ALA A 246 ? 0.92155 0.34394 0.55150 -0.01653 -0.35212 0.01163  246 ALA A O   
1974 C CB  . ALA A 246 ? 0.97056 0.38518 0.59374 -0.01378 -0.35547 0.01025  246 ALA A CB  
1975 N N   . GLU A 247 ? 0.85201 0.27236 0.48626 -0.01621 -0.35695 0.01141  247 GLU A N   
1976 C CA  . GLU A 247 ? 0.84816 0.27146 0.48624 -0.01706 -0.35664 0.01188  247 GLU A CA  
1977 C C   . GLU A 247 ? 1.04120 0.46563 0.67870 -0.01668 -0.35553 0.01182  247 GLU A C   
1978 O O   . GLU A 247 ? 1.13197 0.55908 0.77041 -0.01746 -0.35350 0.01223  247 GLU A O   
1979 C CB  . GLU A 247 ? 0.84928 0.27210 0.49147 -0.01714 -0.35983 0.01186  247 GLU A CB  
1980 C CG  . GLU A 247 ? 1.01173 0.43730 0.65769 -0.01800 -0.35962 0.01232  247 GLU A CG  
1981 C CD  . GLU A 247 ? 1.00695 0.43185 0.65708 -0.01808 -0.36302 0.01227  247 GLU A CD  
1982 O OE1 . GLU A 247 ? 1.02572 0.44945 0.67691 -0.01841 -0.36456 0.01230  247 GLU A OE1 
1983 O OE2 . GLU A 247 ? 1.23843 0.66390 0.89080 -0.01782 -0.36423 0.01220  247 GLU A OE2 
1984 N N   . LYS A 248 ? 1.01422 0.43649 0.65007 -0.01548 -0.35689 0.01128  248 LYS A N   
1985 C CA  . LYS A 248 ? 1.05598 0.47900 0.69098 -0.01508 -0.35594 0.01118  248 LYS A CA  
1986 C C   . LYS A 248 ? 0.93296 0.35757 0.56539 -0.01563 -0.35259 0.01143  248 LYS A C   
1987 O O   . LYS A 248 ? 0.95446 0.38132 0.58791 -0.01612 -0.35119 0.01169  248 LYS A O   
1988 C CB  . LYS A 248 ? 0.89559 0.31543 0.52815 -0.01357 -0.35775 0.01049  248 LYS A CB  
1989 N N   . LYS A 249 ? 0.95907 0.38247 0.58824 -0.01557 -0.35139 0.01132  249 LYS A N   
1990 C CA  . LYS A 249 ? 0.89751 0.32221 0.52430 -0.01610 -0.34843 0.01150  249 LYS A CA  
1991 C C   . LYS A 249 ? 0.98528 0.41318 0.61464 -0.01745 -0.34674 0.01214  249 LYS A C   
1992 O O   . LYS A 249 ? 1.02319 0.45298 0.65228 -0.01798 -0.34472 0.01237  249 LYS A O   
1993 C CB  . LYS A 249 ? 0.98282 0.40517 0.60545 -0.01567 -0.34777 0.01119  249 LYS A CB  
1994 C CG  . LYS A 249 ? 1.02312 0.44216 0.64214 -0.01426 -0.34889 0.01050  249 LYS A CG  
1995 C CD  . LYS A 249 ? 0.94892 0.36860 0.56714 -0.01403 -0.34806 0.01036  249 LYS A CD  
1996 C CE  . LYS A 249 ? 1.01944 0.43577 0.63485 -0.01250 -0.34982 0.00964  249 LYS A CE  
1997 N NZ  . LYS A 249 ? 1.04811 0.46501 0.66298 -0.01230 -0.34925 0.00948  249 LYS A NZ  
1998 N N   . ARG A 250 ? 0.94834 0.37675 0.58037 -0.01797 -0.34776 0.01241  250 ARG A N   
1999 C CA  . ARG A 250 ? 0.90997 0.34104 0.54397 -0.01916 -0.34617 0.01297  250 ARG A CA  
2000 C C   . ARG A 250 ? 0.97295 0.40614 0.60976 -0.01946 -0.34617 0.01318  250 ARG A C   
2001 O O   . ARG A 250 ? 0.89818 0.33344 0.53506 -0.02009 -0.34413 0.01348  250 ARG A O   
2002 C CB  . ARG A 250 ? 0.90408 0.33470 0.53967 -0.01962 -0.34730 0.01314  250 ARG A CB  
2003 C CG  . ARG A 250 ? 0.89064 0.31983 0.52333 -0.01964 -0.34645 0.01306  250 ARG A CG  
2004 C CD  . ARG A 250 ? 0.91168 0.34010 0.54587 -0.02006 -0.34784 0.01320  250 ARG A CD  
2005 N NE  . ARG A 250 ? 0.95621 0.38203 0.59086 -0.01930 -0.35080 0.01280  250 ARG A NE  
2006 C CZ  . ARG A 250 ? 0.84881 0.27442 0.48685 -0.01943 -0.35324 0.01285  250 ARG A CZ  
2007 N NH1 . ARG A 250 ? 0.89578 0.32361 0.53692 -0.02020 -0.35306 0.01325  250 ARG A NH1 
2008 N NH2 . ARG A 250 ? 0.84975 0.27277 0.48804 -0.01877 -0.35601 0.01246  250 ARG A NH2 
2009 N N   . LEU A 251 ? 0.95086 0.38333 0.58982 -0.01898 -0.34852 0.01301  251 LEU A N   
2010 C CA  . LEU A 251 ? 0.86786 0.30209 0.50940 -0.01919 -0.34871 0.01317  251 LEU A CA  
2011 C C   . LEU A 251 ? 0.88804 0.32279 0.52750 -0.01890 -0.34711 0.01304  251 LEU A C   
2012 O O   . LEU A 251 ? 0.96181 0.39859 0.60250 -0.01945 -0.34594 0.01331  251 LEU A O   
2013 C CB  . LEU A 251 ? 0.85207 0.28516 0.49627 -0.01869 -0.35176 0.01297  251 LEU A CB  
2014 C CG  . LEU A 251 ? 0.93240 0.36537 0.57954 -0.01921 -0.35352 0.01316  251 LEU A CG  
2015 C CD1 . LEU A 251 ? 0.91552 0.34698 0.56508 -0.01856 -0.35682 0.01285  251 LEU A CD1 
2016 C CD2 . LEU A 251 ? 0.95748 0.39289 0.60676 -0.02022 -0.35230 0.01365  251 LEU A CD2 
2017 N N   . GLU A 252 ? 0.87622 0.30900 0.51243 -0.01810 -0.34706 0.01262  252 GLU A N   
2018 C CA  A GLU A 252 ? 0.88977 0.32270 0.52369 -0.01787 -0.34562 0.01246  252 GLU A CA  
2019 C CA  B GLU A 252 ? 0.89116 0.32415 0.52516 -0.01788 -0.34562 0.01247  252 GLU A CA  
2020 C C   . GLU A 252 ? 0.89922 0.33398 0.53216 -0.01877 -0.34292 0.01280  252 GLU A C   
2021 O O   . GLU A 252 ? 0.92271 0.35884 0.55569 -0.01910 -0.34170 0.01291  252 GLU A O   
2022 C CB  A GLU A 252 ? 0.90815 0.33808 0.53841 -0.01674 -0.34633 0.01187  252 GLU A CB  
2023 C CB  B GLU A 252 ? 0.90932 0.33932 0.53974 -0.01673 -0.34638 0.01187  252 GLU A CB  
2024 C CG  A GLU A 252 ? 0.99033 0.41975 0.61805 -0.01634 -0.34541 0.01156  252 GLU A CG  
2025 C CG  B GLU A 252 ? 0.94755 0.37586 0.57880 -0.01570 -0.34895 0.01147  252 GLU A CG  
2026 C CD  A GLU A 252 ? 0.96865 0.39469 0.59226 -0.01516 -0.34615 0.01090  252 GLU A CD  
2027 C CD  B GLU A 252 ? 0.97479 0.39965 0.60236 -0.01442 -0.35007 0.01082  252 GLU A CD  
2028 O OE1 A GLU A 252 ? 0.99246 0.41653 0.61546 -0.01455 -0.34761 0.01069  252 GLU A OE1 
2029 O OE1 B GLU A 252 ? 1.02590 0.44964 0.65005 -0.01435 -0.34873 0.01067  252 GLU A OE1 
2030 O OE2 A GLU A 252 ? 0.93897 0.36407 0.55977 -0.01482 -0.34536 0.01056  252 GLU A OE2 
2031 O OE2 B GLU A 252 ? 0.96016 0.38322 0.58815 -0.01344 -0.35237 0.01044  252 GLU A OE2 
2032 N N   . PHE A 253 ? 0.95112 0.38578 0.58317 -0.01918 -0.34209 0.01295  253 PHE A N   
2033 C CA  . PHE A 253 ? 0.85844 0.29476 0.48977 -0.02003 -0.33973 0.01328  253 PHE A CA  
2034 C C   . PHE A 253 ? 0.87185 0.31082 0.50630 -0.02088 -0.33909 0.01374  253 PHE A C   
2035 O O   . PHE A 253 ? 0.95627 0.39673 0.59057 -0.02137 -0.33750 0.01393  253 PHE A O   
2036 C CB  . PHE A 253 ? 0.82962 0.26510 0.45944 -0.02024 -0.33919 0.01332  253 PHE A CB  
2037 C CG  . PHE A 253 ? 0.92753 0.36503 0.55796 -0.02123 -0.33729 0.01376  253 PHE A CG  
2038 C CD1 . PHE A 253 ? 0.90803 0.34620 0.53673 -0.02159 -0.33541 0.01381  253 PHE A CD1 
2039 C CD2 . PHE A 253 ? 0.83633 0.27484 0.46901 -0.02180 -0.33753 0.01409  253 PHE A CD2 
2040 C CE1 . PHE A 253 ? 0.85803 0.29793 0.48735 -0.02243 -0.33385 0.01418  253 PHE A CE1 
2041 C CE2 . PHE A 253 ? 0.85905 0.29919 0.49206 -0.02261 -0.33586 0.01444  253 PHE A CE2 
2042 C CZ  . PHE A 253 ? 0.92030 0.36117 0.55168 -0.02290 -0.33404 0.01449  253 PHE A CZ  
2043 N N   . LEU A 254 ? 0.85292 0.29225 0.49006 -0.02105 -0.34042 0.01392  254 LEU A N   
2044 C CA  . LEU A 254 ? 0.82187 0.26332 0.46167 -0.02177 -0.33998 0.01430  254 LEU A CA  
2045 C C   . LEU A 254 ? 0.93958 0.38196 0.58020 -0.02165 -0.33989 0.01426  254 LEU A C   
2046 O O   . LEU A 254 ? 0.92103 0.36509 0.56208 -0.02220 -0.33846 0.01451  254 LEU A O   
2047 C CB  . LEU A 254 ? 0.86669 0.30786 0.50910 -0.02189 -0.34182 0.01440  254 LEU A CB  
2048 C CG  . LEU A 254 ? 0.85213 0.29262 0.49413 -0.02223 -0.34182 0.01452  254 LEU A CG  
2049 C CD1 . LEU A 254 ? 0.82305 0.26324 0.46787 -0.02245 -0.34380 0.01463  254 LEU A CD1 
2050 C CD2 . LEU A 254 ? 0.88840 0.33027 0.52932 -0.02293 -0.33947 0.01480  254 LEU A CD2 
2051 N N   . ALA A 255 ? 0.93746 0.37860 0.57818 -0.02090 -0.34151 0.01394  255 ALA A N   
2052 C CA  . ALA A 255 ? 0.85311 0.29485 0.49443 -0.02073 -0.34158 0.01386  255 ALA A CA  
2053 C C   . ALA A 255 ? 0.89638 0.33849 0.53530 -0.02086 -0.33969 0.01382  255 ALA A C   
2054 O O   . ALA A 255 ? 0.84161 0.28512 0.48126 -0.02126 -0.33880 0.01399  255 ALA A O   
2055 C CB  . ALA A 255 ? 0.84932 0.28931 0.49086 -0.01979 -0.34380 0.01346  255 ALA A CB  
2056 N N   . TYR A 256 ? 0.85584 0.29654 0.49184 -0.02055 -0.33913 0.01358  256 TYR A N   
2057 C CA  . TYR A 256 ? 0.82377 0.26444 0.45738 -0.02070 -0.33757 0.01350  256 TYR A CA  
2058 C C   . TYR A 256 ? 0.90289 0.34565 0.53733 -0.02167 -0.33578 0.01394  256 TYR A C   
2059 O O   . TYR A 256 ? 0.95365 0.39736 0.58820 -0.02201 -0.33494 0.01404  256 TYR A O   
2060 C CB  . TYR A 256 ? 0.82660 0.26508 0.45674 -0.02021 -0.33738 0.01313  256 TYR A CB  
2061 C CG  . TYR A 256 ? 0.96087 0.39850 0.58812 -0.02021 -0.33626 0.01289  256 TYR A CG  
2062 C CD1 . TYR A 256 ? 1.02806 0.46392 0.65354 -0.01948 -0.33709 0.01241  256 TYR A CD1 
2063 C CD2 . TYR A 256 ? 0.94663 0.38495 0.57281 -0.02093 -0.33455 0.01311  256 TYR A CD2 
2064 C CE1 . TYR A 256 ? 0.99628 0.43097 0.61893 -0.01951 -0.33621 0.01215  256 TYR A CE1 
2065 C CE2 . TYR A 256 ? 1.03619 0.47344 0.65979 -0.02098 -0.33375 0.01290  256 TYR A CE2 
2066 C CZ  . TYR A 256 ? 1.00751 0.44288 0.62929 -0.02030 -0.33458 0.01241  256 TYR A CZ  
2067 O OH  . TYR A 256 ? 0.92144 0.35538 0.54050 -0.02038 -0.33391 0.01217  256 TYR A OH  
2068 N N   . TYR A 257 ? 1.00344 0.44671 0.63834 -0.02208 -0.33531 0.01418  257 TYR A N   
2069 C CA  . TYR A 257 ? 0.94512 0.39012 0.58052 -0.02291 -0.33368 0.01456  257 TYR A CA  
2070 C C   . TYR A 257 ? 0.88291 0.32966 0.52083 -0.02329 -0.33364 0.01482  257 TYR A C   
2071 O O   . TYR A 257 ? 0.86489 0.31275 0.50281 -0.02375 -0.33249 0.01499  257 TYR A O   
2072 C CB  . TYR A 257 ? 0.89879 0.34375 0.53416 -0.02319 -0.33340 0.01471  257 TYR A CB  
2073 C CG  . TYR A 257 ? 1.02608 0.47245 0.66147 -0.02395 -0.33175 0.01503  257 TYR A CG  
2074 C CD1 . TYR A 257 ? 0.87017 0.31691 0.50425 -0.02424 -0.33050 0.01507  257 TYR A CD1 
2075 C CD2 . TYR A 257 ? 0.95076 0.39785 0.58738 -0.02435 -0.33159 0.01527  257 TYR A CD2 
2076 C CE1 . TYR A 257 ? 0.85936 0.30727 0.49356 -0.02488 -0.32921 0.01535  257 TYR A CE1 
2077 C CE2 . TYR A 257 ? 0.92426 0.37244 0.56073 -0.02494 -0.33020 0.01552  257 TYR A CE2 
2078 C CZ  . TYR A 257 ? 0.94798 0.39661 0.58333 -0.02519 -0.32904 0.01556  257 TYR A CZ  
2079 O OH  . TYR A 257 ? 0.90850 0.35811 0.54381 -0.02574 -0.32785 0.01579  257 TYR A OH  
2080 N N   . PHE A 258 ? 0.84435 0.29115 0.48437 -0.02309 -0.33505 0.01482  258 PHE A N   
2081 C CA  . PHE A 258 ? 0.86205 0.31022 0.50424 -0.02341 -0.33511 0.01502  258 PHE A CA  
2082 C C   . PHE A 258 ? 0.93118 0.37954 0.57315 -0.02324 -0.33502 0.01491  258 PHE A C   
2083 O O   . PHE A 258 ? 0.95792 0.40746 0.60057 -0.02365 -0.33423 0.01509  258 PHE A O   
2084 C CB  . PHE A 258 ? 0.96345 0.41129 0.60785 -0.02323 -0.33687 0.01502  258 PHE A CB  
2085 C CG  . PHE A 258 ? 1.03962 0.48717 0.68438 -0.02349 -0.33709 0.01515  258 PHE A CG  
2086 C CD1 . PHE A 258 ? 1.01133 0.45938 0.65485 -0.02395 -0.33552 0.01532  258 PHE A CD1 
2087 C CD2 . PHE A 258 ? 1.00687 0.45351 0.65324 -0.02328 -0.33901 0.01509  258 PHE A CD2 
2088 C CE1 . PHE A 258 ? 0.84576 0.29336 0.48942 -0.02418 -0.33575 0.01542  258 PHE A CE1 
2089 C CE2 . PHE A 258 ? 0.81979 0.26593 0.46641 -0.02355 -0.33934 0.01520  258 PHE A CE2 
2090 C CZ  . PHE A 258 ? 0.86955 0.31616 0.51471 -0.02399 -0.33765 0.01537  258 PHE A CZ  
2091 N N   . ASN A 259 ? 0.94064 0.38763 0.58142 -0.02262 -0.33584 0.01458  259 ASN A N   
2092 C CA  . ASN A 259 ? 0.90350 0.35033 0.54387 -0.02241 -0.33594 0.01442  259 ASN A CA  
2093 C C   . ASN A 259 ? 0.89362 0.34080 0.53223 -0.02286 -0.33430 0.01451  259 ASN A C   
2094 O O   . ASN A 259 ? 0.94850 0.39650 0.58766 -0.02316 -0.33384 0.01463  259 ASN A O   
2095 C CB  . ASN A 259 ? 0.92306 0.36804 0.56252 -0.02154 -0.33748 0.01398  259 ASN A CB  
2096 C CG  . ASN A 259 ? 0.88813 0.33290 0.52992 -0.02116 -0.33937 0.01392  259 ASN A CG  
2097 O OD1 . ASN A 259 ? 0.90075 0.34674 0.54485 -0.02155 -0.33957 0.01417  259 ASN A OD1 
2098 N ND2 . ASN A 259 ? 0.84253 0.28553 0.48365 -0.02036 -0.34091 0.01355  259 ASN A ND2 
2099 N N   . ARG A 260 ? 0.85331 0.29978 0.48994 -0.02292 -0.33356 0.01446  260 ARG A N   
2100 C CA  . ARG A 260 ? 0.82267 0.26934 0.45778 -0.02342 -0.33218 0.01457  260 ARG A CA  
2101 C C   . ARG A 260 ? 0.98214 0.43078 0.61901 -0.02414 -0.33122 0.01499  260 ARG A C   
2102 O O   . ARG A 260 ? 0.97706 0.42613 0.61362 -0.02453 -0.33053 0.01512  260 ARG A O   
2103 C CB  . ARG A 260 ? 0.86221 0.30753 0.49486 -0.02331 -0.33174 0.01440  260 ARG A CB  
2104 C CG  . ARG A 260 ? 0.90785 0.35080 0.53791 -0.02260 -0.33249 0.01390  260 ARG A CG  
2105 C CD  . ARG A 260 ? 0.99141 0.43359 0.61963 -0.02283 -0.33186 0.01381  260 ARG A CD  
2106 N NE  . ARG A 260 ? 0.97787 0.41731 0.60283 -0.02220 -0.33236 0.01328  260 ARG A NE  
2107 C CZ  . ARG A 260 ? 0.99532 0.43330 0.61930 -0.02158 -0.33333 0.01288  260 ARG A CZ  
2108 N NH1 . ARG A 260 ? 1.06038 0.49952 0.68659 -0.02155 -0.33391 0.01299  260 ARG A NH1 
2109 N NH2 . ARG A 260 ? 0.98304 0.41817 0.60361 -0.02095 -0.33375 0.01233  260 ARG A NH2 
2110 N N   . ALA A 261 ? 1.00077 0.45033 0.63934 -0.02428 -0.33136 0.01518  261 ALA A N   
2111 C CA  . ALA A 261 ? 0.94191 0.39301 0.58181 -0.02485 -0.33054 0.01550  261 ALA A CA  
2112 C C   . ALA A 261 ? 0.92437 0.37609 0.56559 -0.02486 -0.33089 0.01554  261 ALA A C   
2113 O O   . ALA A 261 ? 0.91470 0.36724 0.55610 -0.02527 -0.33010 0.01572  261 ALA A O   
2114 C CB  . ALA A 261 ? 0.80719 0.25863 0.44818 -0.02493 -0.33075 0.01561  261 ALA A CB  
2115 N N   . VAL A 262 ? 0.86254 0.31370 0.50452 -0.02438 -0.33213 0.01534  262 VAL A N   
2116 C CA  . VAL A 262 ? 0.94850 0.40004 0.59164 -0.02434 -0.33259 0.01534  262 VAL A CA  
2117 C C   . VAL A 262 ? 0.95057 0.40174 0.59237 -0.02440 -0.33213 0.01527  262 VAL A C   
2118 O O   . VAL A 262 ? 0.89719 0.34885 0.53958 -0.02459 -0.33200 0.01536  262 VAL A O   
2119 C CB  . VAL A 262 ? 0.90167 0.35260 0.54610 -0.02382 -0.33421 0.01514  262 VAL A CB  
2120 C CG1 . VAL A 262 ? 0.94935 0.40045 0.59470 -0.02374 -0.33470 0.01509  262 VAL A CG1 
2121 C CG2 . VAL A 262 ? 0.86056 0.31163 0.50642 -0.02384 -0.33487 0.01522  262 VAL A CG2 
2122 N N   . GLU A 263 ? 0.96450 0.41467 0.60440 -0.02429 -0.33191 0.01512  263 GLU A N   
2123 C CA  . GLU A 263 ? 0.89235 0.34182 0.53075 -0.02441 -0.33158 0.01506  263 GLU A CA  
2124 C C   . GLU A 263 ? 0.87204 0.32236 0.51026 -0.02511 -0.33040 0.01538  263 GLU A C   
2125 O O   . GLU A 263 ? 1.02679 0.47704 0.66479 -0.02537 -0.33025 0.01547  263 GLU A O   
2126 C CB  . GLU A 263 ? 0.85105 0.29869 0.48713 -0.02399 -0.33191 0.01472  263 GLU A CB  
2127 C CG  . GLU A 263 ? 0.81511 0.26170 0.45124 -0.02321 -0.33325 0.01436  263 GLU A CG  
2128 C CD  . GLU A 263 ? 0.99385 0.43831 0.62729 -0.02268 -0.33361 0.01394  263 GLU A CD  
2129 O OE1 . GLU A 263 ? 0.95216 0.39589 0.58360 -0.02296 -0.33278 0.01394  263 GLU A OE1 
2130 O OE2 . GLU A 263 ? 0.90150 0.34484 0.53474 -0.02195 -0.33484 0.01360  263 GLU A OE2 
2131 N N   . TRP A 264 ? 0.99652 0.44746 0.63482 -0.02537 -0.32972 0.01555  264 TRP A N   
2132 C CA  . TRP A 264 ? 0.91922 0.37085 0.55732 -0.02599 -0.32872 0.01584  264 TRP A CA  
2133 C C   . TRP A 264 ? 0.83698 0.28994 0.47681 -0.02624 -0.32852 0.01606  264 TRP A C   
2134 O O   . TRP A 264 ? 0.82003 0.27348 0.45987 -0.02668 -0.32793 0.01628  264 TRP A O   
2135 C CB  . TRP A 264 ? 1.00072 0.45233 0.63809 -0.02612 -0.32814 0.01589  264 TRP A CB  
2136 C CG  . TRP A 264 ? 1.08280 0.53288 0.71818 -0.02582 -0.32832 0.01562  264 TRP A CG  
2137 C CD1 . TRP A 264 ? 0.95484 0.40333 0.58839 -0.02560 -0.32866 0.01538  264 TRP A CD1 
2138 C CD2 . TRP A 264 ? 1.04738 0.49705 0.68207 -0.02565 -0.32820 0.01554  264 TRP A CD2 
2139 N NE1 . TRP A 264 ? 0.93816 0.38522 0.56982 -0.02526 -0.32876 0.01512  264 TRP A NE1 
2140 C CE2 . TRP A 264 ? 0.94747 0.39526 0.57984 -0.02529 -0.32849 0.01523  264 TRP A CE2 
2141 C CE3 . TRP A 264 ? 0.97649 0.42694 0.61209 -0.02575 -0.32795 0.01568  264 TRP A CE3 
2142 C CZ2 . TRP A 264 ? 1.05244 0.49918 0.68342 -0.02501 -0.32853 0.01505  264 TRP A CZ2 
2143 C CZ3 . TRP A 264 ? 0.99911 0.44860 0.63348 -0.02553 -0.32800 0.01554  264 TRP A CZ3 
2144 C CH2 . TRP A 264 ? 1.01182 0.45951 0.64393 -0.02515 -0.32828 0.01523  264 TRP A CH2 
2145 N N   . ASN A 265 ? 0.83521 0.28849 0.47634 -0.02592 -0.32913 0.01597  265 ASN A N   
2146 C CA  . ASN A 265 ? 0.86017 0.31436 0.50262 -0.02606 -0.32901 0.01611  265 ASN A CA  
2147 C C   . ASN A 265 ? 0.84479 0.29955 0.48722 -0.02634 -0.32826 0.01626  265 ASN A C   
2148 O O   . ASN A 265 ? 0.90822 0.36349 0.55082 -0.02661 -0.32776 0.01640  265 ASN A O   
2149 C CB  . ASN A 265 ? 0.93268 0.38700 0.57525 -0.02626 -0.32894 0.01620  265 ASN A CB  
2150 C CG  . ASN A 265 ? 0.88932 0.34404 0.53296 -0.02617 -0.32915 0.01620  265 ASN A CG  
2151 O OD1 . ASN A 265 ? 0.91354 0.36826 0.55795 -0.02592 -0.32960 0.01610  265 ASN A OD1 
2152 N ND2 . ASN A 265 ? 0.87150 0.32633 0.51510 -0.02637 -0.32895 0.01629  265 ASN A ND2 
2153 N N   . LYS A 266 ? 0.85218 0.30668 0.49428 -0.02623 -0.32827 0.01621  266 LYS A N   
2154 C CA  . LYS A 266 ? 0.85489 0.30974 0.49680 -0.02648 -0.32761 0.01633  266 LYS A CA  
2155 C C   . LYS A 266 ? 0.80210 0.25666 0.44465 -0.02623 -0.32822 0.01624  266 LYS A C   
2156 O O   . LYS A 266 ? 0.97698 0.43089 0.61952 -0.02591 -0.32897 0.01610  266 LYS A O   
2157 C CB  . LYS A 266 ? 0.80207 0.25663 0.44256 -0.02672 -0.32693 0.01638  266 LYS A CB  
2158 C CG  . LYS A 266 ? 1.05092 0.50577 0.69100 -0.02713 -0.32637 0.01655  266 LYS A CG  
2159 C CD  . LYS A 266 ? 1.04024 0.49475 0.67905 -0.02743 -0.32577 0.01662  266 LYS A CD  
2160 C CE  . LYS A 266 ? 1.01702 0.47051 0.65460 -0.02717 -0.32596 0.01644  266 LYS A CE  
2161 N NZ  . LYS A 266 ? 1.14738 0.60019 0.78342 -0.02747 -0.32548 0.01648  266 LYS A NZ  
2162 N N   . GLU A 267 ? 0.89743 0.35222 0.54044 -0.02635 -0.32806 0.01631  267 GLU A N   
2163 C CA  . GLU A 267 ? 0.81493 0.26920 0.45850 -0.02621 -0.32876 0.01625  267 GLU A CA  
2164 C C   . GLU A 267 ? 0.84875 0.30269 0.49123 -0.02634 -0.32827 0.01629  267 GLU A C   
2165 O O   . GLU A 267 ? 0.91856 0.37279 0.56026 -0.02662 -0.32733 0.01638  267 GLU A O   
2166 C CB  . GLU A 267 ? 0.85000 0.30424 0.49415 -0.02627 -0.32890 0.01626  267 GLU A CB  
2167 C CG  . GLU A 267 ? 0.93495 0.38948 0.57954 -0.02621 -0.32896 0.01623  267 GLU A CG  
2168 C CD  . GLU A 267 ? 1.12057 0.57476 0.76497 -0.02626 -0.32883 0.01620  267 GLU A CD  
2169 O OE1 . GLU A 267 ? 1.14072 0.59513 0.78418 -0.02643 -0.32792 0.01625  267 GLU A OE1 
2170 O OE2 . GLU A 267 ? 1.08620 0.53970 0.73127 -0.02610 -0.32976 0.01611  267 GLU A OE2 
2171 N N   . VAL A 268 ? 0.97349 0.42670 0.61584 -0.02608 -0.32899 0.01618  268 VAL A N   
2172 C CA  . VAL A 268 ? 0.89558 0.34820 0.53655 -0.02614 -0.32856 0.01617  268 VAL A CA  
2173 C C   . VAL A 268 ? 0.91139 0.36324 0.55273 -0.02609 -0.32931 0.01616  268 VAL A C   
2174 O O   . VAL A 268 ? 0.81836 0.27003 0.46111 -0.02598 -0.33037 0.01614  268 VAL A O   
2175 C CB  . VAL A 268 ? 0.82694 0.27888 0.46679 -0.02586 -0.32874 0.01602  268 VAL A CB  
2176 C CG1 . VAL A 268 ? 0.86756 0.31996 0.50676 -0.02601 -0.32802 0.01605  268 VAL A CG1 
2177 C CG2 . VAL A 268 ? 0.82421 0.27537 0.46483 -0.02536 -0.33019 0.01583  268 VAL A CG2 
2178 N N   . VAL A 269 ? 0.82195 0.27324 0.46199 -0.02620 -0.32883 0.01617  269 VAL A N   
2179 C CA  . VAL A 269 ? 0.84917 0.29951 0.48930 -0.02620 -0.32954 0.01616  269 VAL A CA  
2180 C C   . VAL A 269 ? 0.80807 0.25725 0.44683 -0.02596 -0.32981 0.01603  269 VAL A C   
2181 O O   . VAL A 269 ? 0.84345 0.29258 0.48061 -0.02598 -0.32887 0.01599  269 VAL A O   
2182 C CB  . VAL A 269 ? 0.89299 0.34346 0.53259 -0.02658 -0.32868 0.01629  269 VAL A CB  
2183 C CG1 . VAL A 269 ? 0.80670 0.25592 0.44630 -0.02661 -0.32955 0.01628  269 VAL A CG1 
2184 C CG2 . VAL A 269 ? 0.80421 0.25553 0.44469 -0.02672 -0.32838 0.01635  269 VAL A CG2 
2185 N N   . THR A 270 ? 0.80941 0.25745 0.44872 -0.02573 -0.33122 0.01594  270 THR A N   
2186 C CA  . THR A 270 ? 0.84368 0.29026 0.48152 -0.02549 -0.33162 0.01580  270 THR A CA  
2187 C C   . THR A 270 ? 0.81211 0.25775 0.45036 -0.02568 -0.33242 0.01587  270 THR A C   
2188 O O   . THR A 270 ? 0.83793 0.28375 0.47789 -0.02585 -0.33322 0.01597  270 THR A O   
2189 C CB  . THR A 270 ? 0.81354 0.25913 0.45135 -0.02488 -0.33291 0.01555  270 THR A CB  
2190 O OG1 . THR A 270 ? 0.86044 0.30441 0.49618 -0.02459 -0.33306 0.01536  270 THR A OG1 
2191 C CG2 . THR A 270 ? 0.89906 0.34424 0.53912 -0.02471 -0.33484 0.01553  270 THR A CG2 
2192 N N   . THR A 271 ? 0.81338 0.25783 0.44988 -0.02567 -0.33221 0.01580  271 THR A N   
2193 C CA  . THR A 271 ? 0.87446 0.31784 0.51092 -0.02591 -0.33278 0.01588  271 THR A CA  
2194 C C   . THR A 271 ? 0.88679 0.32819 0.52255 -0.02555 -0.33422 0.01569  271 THR A C   
2195 O O   . THR A 271 ? 0.86535 0.30609 0.50007 -0.02507 -0.33447 0.01547  271 THR A O   
2196 C CB  . THR A 271 ? 0.86420 0.30782 0.49901 -0.02630 -0.33113 0.01599  271 THR A CB  
2197 O OG1 . THR A 271 ? 0.81405 0.25713 0.44667 -0.02613 -0.33028 0.01585  271 THR A OG1 
2198 C CG2 . THR A 271 ? 0.93908 0.38446 0.57451 -0.02659 -0.32987 0.01613  271 THR A CG2 
2199 N N   . HIS A 272 ? 0.93411 0.37437 0.57045 -0.02577 -0.33534 0.01576  272 HIS A N   
2200 C CA  . HIS A 272 ? 0.82096 0.25903 0.45665 -0.02550 -0.33692 0.01559  272 HIS A CA  
2201 C C   . HIS A 272 ? 0.83858 0.27560 0.47373 -0.02596 -0.33700 0.01573  272 HIS A C   
2202 O O   . HIS A 272 ? 0.82209 0.25960 0.45851 -0.02638 -0.33709 0.01593  272 HIS A O   
2203 C CB  . HIS A 272 ? 0.82244 0.25983 0.46041 -0.02518 -0.33932 0.01549  272 HIS A CB  
2204 C CG  . HIS A 272 ? 0.86914 0.30656 0.50959 -0.02558 -0.34067 0.01568  272 HIS A CG  
2205 N ND1 . HIS A 272 ? 0.90184 0.33743 0.54295 -0.02577 -0.34252 0.01570  272 HIS A ND1 
2206 C CD2 . HIS A 272 ? 0.91205 0.35079 0.55441 -0.02581 -0.34068 0.01583  272 HIS A CD2 
2207 C CE1 . HIS A 272 ? 0.95572 0.39152 0.59908 -0.02613 -0.34359 0.01588  272 HIS A CE1 
2208 N NE2 . HIS A 272 ? 0.89451 0.33219 0.53855 -0.02614 -0.34245 0.01595  272 HIS A NE2 
2209 N N   . LYS A 273 ? 0.87131 0.30659 0.50442 -0.02584 -0.33712 0.01560  273 LYS A N   
2210 C CA  . LYS A 273 ? 0.82468 0.25852 0.45712 -0.02625 -0.33749 0.01571  273 LYS A CA  
2211 C C   . LYS A 273 ? 0.85581 0.28875 0.49079 -0.02643 -0.33983 0.01580  273 LYS A C   
2212 O O   . LYS A 273 ? 0.83773 0.27019 0.47420 -0.02607 -0.34165 0.01566  273 LYS A O   
2213 C CB  . LYS A 273 ? 0.82702 0.25891 0.45679 -0.02599 -0.33745 0.01551  273 LYS A CB  
2214 C CG  . LYS A 273 ? 0.83868 0.27117 0.46586 -0.02591 -0.33519 0.01545  273 LYS A CG  
2215 C CD  . LYS A 273 ? 0.84374 0.27704 0.47029 -0.02646 -0.33358 0.01567  273 LYS A CD  
2216 C CE  . LYS A 273 ? 0.87900 0.31282 0.50329 -0.02642 -0.33159 0.01561  273 LYS A CE  
2217 N NZ  . LYS A 273 ? 0.86851 0.30035 0.49034 -0.02602 -0.33183 0.01535  273 LYS A NZ  
2218 N N   . HIS A 274 ? 0.88890 0.32273 0.52664 -0.02705 -0.33770 0.01563  274 HIS A N   
2219 C CA  . HIS A 274 ? 0.95191 0.38631 0.59504 -0.02746 -0.33724 0.01526  274 HIS A CA  
2220 C C   . HIS A 274 ? 0.92596 0.35904 0.57133 -0.02737 -0.33840 0.01479  274 HIS A C   
2221 O O   . HIS A 274 ? 1.02391 0.45739 0.67366 -0.02758 -0.33895 0.01447  274 HIS A O   
2222 C CB  . HIS A 274 ? 0.91034 0.34527 0.55539 -0.02807 -0.33448 0.01514  274 HIS A CB  
2223 C CG  . HIS A 274 ? 1.08183 0.51734 0.73224 -0.02853 -0.33365 0.01480  274 HIS A CG  
2224 N ND1 . HIS A 274 ? 1.26583 0.70232 0.91858 -0.02848 -0.33474 0.01483  274 HIS A ND1 
2225 C CD2 . HIS A 274 ? 1.03221 0.46737 0.68620 -0.02906 -0.33172 0.01444  274 HIS A CD2 
2226 C CE1 . HIS A 274 ? 1.30606 0.74278 0.96367 -0.02898 -0.33354 0.01448  274 HIS A CE1 
2227 N NE2 . HIS A 274 ? 1.15850 0.59440 0.81700 -0.02934 -0.33164 0.01425  274 HIS A NE2 
2228 N N   . PHE A 275 ? 0.96423 0.39569 0.60675 -0.02708 -0.33872 0.01470  275 PHE A N   
2229 C CA  . PHE A 275 ? 1.04771 0.47758 0.69197 -0.02693 -0.33995 0.01416  275 PHE A CA  
2230 C C   . PHE A 275 ? 1.00697 0.43609 0.64992 -0.02613 -0.34298 0.01425  275 PHE A C   
2231 O O   . PHE A 275 ? 1.17542 0.60429 0.82208 -0.02612 -0.34432 0.01381  275 PHE A O   
2232 C CB  . PHE A 275 ? 0.88423 0.31248 0.52603 -0.02693 -0.33888 0.01396  275 PHE A CB  
2233 C CG  . PHE A 275 ? 0.87270 0.29999 0.50846 -0.02641 -0.33906 0.01437  275 PHE A CG  
2234 C CD1 . PHE A 275 ? 0.85506 0.28321 0.48863 -0.02669 -0.33715 0.01472  275 PHE A CD1 
2235 C CD2 . PHE A 275 ? 1.00753 0.43283 0.63985 -0.02562 -0.34112 0.01433  275 PHE A CD2 
2236 C CE1 . PHE A 275 ? 0.96220 0.38947 0.59067 -0.02631 -0.33729 0.01499  275 PHE A CE1 
2237 C CE2 . PHE A 275 ? 1.04023 0.46449 0.66715 -0.02520 -0.34112 0.01463  275 PHE A CE2 
2238 C CZ  . PHE A 275 ? 0.89560 0.32096 0.52081 -0.02560 -0.33919 0.01494  275 PHE A CZ  
2239 N N   . ASP A 276 ? 0.95067 0.37941 0.58873 -0.02550 -0.34398 0.01477  276 ASP A N   
2240 C CA  . ASP A 276 ? 0.87400 0.30186 0.51043 -0.02464 -0.34668 0.01491  276 ASP A CA  
2241 C C   . ASP A 276 ? 0.94368 0.37302 0.58398 -0.02478 -0.34760 0.01495  276 ASP A C   
2242 O O   . ASP A 276 ? 0.98841 0.41961 0.62941 -0.02520 -0.34637 0.01525  276 ASP A O   
2243 C CB  . ASP A 276 ? 0.86041 0.28948 0.49436 -0.02430 -0.34416 0.01480  276 ASP A CB  
2244 C CG  . ASP A 276 ? 0.83560 0.26325 0.46806 -0.02341 -0.34496 0.01438  276 ASP A CG  
2245 O OD1 . ASP A 276 ? 0.99113 0.41798 0.62542 -0.02300 -0.34723 0.01421  276 ASP A OD1 
2246 O OD2 . ASP A 276 ? 0.94094 0.36815 0.57036 -0.02311 -0.34340 0.01422  276 ASP A OD2 
2247 N N   . VAL A 277 ? 0.98323 0.41170 0.62616 -0.02443 -0.34962 0.01456  277 VAL A N   
2248 C CA  . VAL A 277 ? 0.93787 0.36764 0.58489 -0.02454 -0.35062 0.01450  277 VAL A CA  
2249 C C   . VAL A 277 ? 0.86638 0.29593 0.51138 -0.02362 -0.35202 0.01463  277 VAL A C   
2250 O O   . VAL A 277 ? 0.90569 0.33562 0.55329 -0.02344 -0.35363 0.01459  277 VAL A O   
2251 C CB  . VAL A 277 ? 0.83551 0.26502 0.48817 -0.02493 -0.35112 0.01370  277 VAL A CB  
2252 C CG1 . VAL A 277 ? 0.83398 0.26451 0.49016 -0.02602 -0.34830 0.01333  277 VAL A CG1 
2253 C CG2 . VAL A 277 ? 0.83935 0.26631 0.49062 -0.02418 -0.35334 0.01329  277 VAL A CG2 
2254 N N   . GLY A 278 ? 0.85872 0.28830 0.50057 -0.02320 -0.35008 0.01446  278 GLY A N   
2255 C CA  . GLY A 278 ? 0.84177 0.27188 0.48283 -0.02248 -0.34958 0.01421  278 GLY A CA  
2256 C C   . GLY A 278 ? 0.93083 0.36330 0.57399 -0.02273 -0.34888 0.01442  278 GLY A C   
2257 O O   . GLY A 278 ? 0.95924 0.39167 0.60345 -0.02217 -0.35002 0.01422  278 GLY A O   
2258 N N   . PHE A 279 ? 0.82902 0.26326 0.47262 -0.02348 -0.34716 0.01479  279 PHE A N   
2259 C CA  . PHE A 279 ? 0.88017 0.31647 0.52565 -0.02373 -0.34654 0.01498  279 PHE A CA  
2260 C C   . PHE A 279 ? 0.88991 0.32633 0.53787 -0.02437 -0.34767 0.01525  279 PHE A C   
2261 O O   . PHE A 279 ? 0.98463 0.41991 0.63227 -0.02474 -0.34814 0.01535  279 PHE A O   
2262 C CB  . PHE A 279 ? 0.86999 0.30815 0.51363 -0.02398 -0.34354 0.01513  279 PHE A CB  
2263 C CG  . PHE A 279 ? 0.90190 0.33992 0.54289 -0.02346 -0.34223 0.01490  279 PHE A CG  
2264 C CD1 . PHE A 279 ? 0.82621 0.26316 0.46688 -0.02268 -0.34346 0.01457  279 PHE A CD1 
2265 C CD2 . PHE A 279 ? 0.83596 0.27475 0.47471 -0.02374 -0.33985 0.01500  279 PHE A CD2 
2266 C CE1 . PHE A 279 ? 0.84616 0.28265 0.48406 -0.02219 -0.34231 0.01433  279 PHE A CE1 
2267 C CE2 . PHE A 279 ? 0.82321 0.26167 0.45948 -0.02331 -0.33878 0.01478  279 PHE A CE2 
2268 C CZ  . PHE A 279 ? 0.82548 0.26271 0.46120 -0.02254 -0.33998 0.01445  279 PHE A CZ  
2269 N N   . ARG A 280 ? 0.97238 0.40998 0.62252 -0.02451 -0.34805 0.01537  280 ARG A N   
2270 C CA  A ARG A 280 ? 0.93195 0.36962 0.58407 -0.02514 -0.34885 0.01563  280 ARG A CA  
2271 C CA  B ARG A 280 ? 0.93354 0.37111 0.58576 -0.02514 -0.34901 0.01563  280 ARG A CA  
2272 C C   . ARG A 280 ? 0.90758 0.34684 0.55901 -0.02560 -0.34663 0.01586  280 ARG A C   
2273 O O   . ARG A 280 ? 0.91408 0.35480 0.56391 -0.02546 -0.34440 0.01584  280 ARG A O   
2274 C CB  A ARG A 280 ? 0.96446 0.40183 0.61973 -0.02495 -0.35142 0.01556  280 ARG A CB  
2275 C CB  B ARG A 280 ? 0.96233 0.39945 0.61787 -0.02495 -0.35169 0.01552  280 ARG A CB  
2276 C CG  A ARG A 280 ? 0.97737 0.41320 0.63347 -0.02432 -0.35380 0.01525  280 ARG A CG  
2277 C CG  B ARG A 280 ? 0.97810 0.41350 0.63409 -0.02432 -0.35409 0.01523  280 ARG A CG  
2278 C CD  A ARG A 280 ? 1.06152 0.49737 0.72129 -0.02413 -0.35596 0.01506  280 ARG A CD  
2279 C CD  B ARG A 280 ? 1.05704 0.49243 0.71812 -0.02432 -0.35581 0.01475  280 ARG A CD  
2280 N NE  A ARG A 280 ? 1.12432 0.55849 0.78415 -0.02333 -0.35849 0.01478  280 ARG A NE  
2281 N NE  B ARG A 280 ? 1.05824 0.49445 0.72051 -0.02412 -0.35678 0.01492  280 ARG A NE  
2282 C CZ  A ARG A 280 ? 1.04579 0.47894 0.70870 -0.02342 -0.35963 0.01422  280 ARG A CZ  
2283 C CZ  B ARG A 280 ? 1.02538 0.46183 0.69247 -0.02420 -0.35805 0.01447  280 ARG A CZ  
2284 N NH1 A ARG A 280 ? 1.09561 0.52975 0.76266 -0.02445 -0.35761 0.01373  280 ARG A NH1 
2285 N NH1 B ARG A 280 ? 1.13650 0.57246 0.80779 -0.02451 -0.35858 0.01381  280 ARG A NH1 
2286 N NH2 A ARG A 280 ? 0.94125 0.37243 0.60339 -0.02250 -0.36245 0.01404  280 ARG A NH2 
2287 N NH2 B ARG A 280 ? 0.87080 0.30799 0.53875 -0.02405 -0.35870 0.01463  280 ARG A NH2 
2288 N N   . ASP A 281 ? 0.93748 0.37689 0.59068 -0.02623 -0.34579 0.01585  281 ASP A N   
2289 C CA  . ASP A 281 ? 0.85056 0.29106 0.50268 -0.02657 -0.34379 0.01603  281 ASP A CA  
2290 C C   . ASP A 281 ? 0.97806 0.41939 0.63129 -0.02645 -0.34443 0.01612  281 ASP A C   
2291 O O   . ASP A 281 ? 0.99204 0.43414 0.64479 -0.02668 -0.34294 0.01619  281 ASP A O   
2292 C CB  . ASP A 281 ? 0.86013 0.30086 0.51488 -0.02724 -0.34127 0.01571  281 ASP A CB  
2293 C CG  . ASP A 281 ? 0.97363 0.41354 0.62644 -0.02735 -0.34036 0.01568  281 ASP A CG  
2294 O OD1 . ASP A 281 ? 0.88102 0.32026 0.53002 -0.02693 -0.34152 0.01595  281 ASP A OD1 
2295 O OD2 . ASP A 281 ? 1.02503 0.46483 0.68013 -0.02785 -0.33843 0.01540  281 ASP A OD2 
2296 N N   . THR A 282 ? 0.89287 0.33388 0.54744 -0.02604 -0.34661 0.01607  282 THR A N   
2297 C CA  . THR A 282 ? 0.90373 0.34565 0.55949 -0.02589 -0.34692 0.01608  282 THR A CA  
2298 C C   . THR A 282 ? 0.91251 0.35617 0.56642 -0.02570 -0.34435 0.01603  282 THR A C   
2299 O O   . THR A 282 ? 0.91103 0.35556 0.56502 -0.02580 -0.34352 0.01608  282 THR A O   
2300 C CB  . THR A 282 ? 0.83948 0.28077 0.49763 -0.02549 -0.34947 0.01592  282 THR A CB  
2301 O OG1 . THR A 282 ? 0.94072 0.38194 0.59770 -0.02499 -0.34919 0.01572  282 THR A OG1 
2302 C CG2 . THR A 282 ? 0.82049 0.26160 0.48379 -0.02593 -0.34946 0.01543  282 THR A CG2 
2303 N N   . SER A 283 ? 0.87569 0.31962 0.52797 -0.02543 -0.34331 0.01593  283 SER A N   
2304 C CA  . SER A 283 ? 0.85269 0.29807 0.50334 -0.02527 -0.34114 0.01588  283 SER A CA  
2305 C C   . SER A 283 ? 0.89004 0.33556 0.53828 -0.02542 -0.33930 0.01592  283 SER A C   
2306 O O   . SER A 283 ? 0.96656 0.41320 0.61343 -0.02540 -0.33748 0.01592  283 SER A O   
2307 C CB  . SER A 283 ? 0.88333 0.32866 0.53426 -0.02469 -0.34189 0.01567  283 SER A CB  
2308 O OG  . SER A 283 ? 0.85746 0.30148 0.50776 -0.02436 -0.34285 0.01551  283 SER A OG  
2309 N N   . THR A 284 ? 0.87004 0.31434 0.51781 -0.02557 -0.33987 0.01595  284 THR A N   
2310 C CA  . THR A 284 ? 0.81432 0.25854 0.45968 -0.02567 -0.33826 0.01596  284 THR A CA  
2311 C C   . THR A 284 ? 0.83303 0.27685 0.47780 -0.02618 -0.33770 0.01613  284 THR A C   
2312 O O   . THR A 284 ? 0.81464 0.25779 0.46083 -0.02640 -0.33898 0.01621  284 THR A O   
2313 C CB  . THR A 284 ? 0.96821 0.41104 0.61278 -0.02526 -0.33925 0.01576  284 THR A CB  
2314 O OG1 . THR A 284 ? 0.95867 0.40172 0.60369 -0.02474 -0.33982 0.01558  284 THR A OG1 
2315 C CG2 . THR A 284 ? 1.06970 0.51222 0.71163 -0.02530 -0.33770 0.01573  284 THR A CG2 
2316 N N   . VAL A 285 ? 0.68512 0.33827 0.49106 -0.02774 -0.23250 0.01840  285 VAL A N   
2317 C CA  . VAL A 285 ? 0.79220 0.45057 0.60259 -0.02822 -0.23169 0.02002  285 VAL A CA  
2318 C C   . VAL A 285 ? 0.70938 0.36715 0.52349 -0.02961 -0.23396 0.02002  285 VAL A C   
2319 O O   . VAL A 285 ? 0.68642 0.34338 0.49838 -0.02869 -0.23236 0.01869  285 VAL A O   
2320 C CB  . VAL A 285 ? 0.74696 0.40496 0.55340 -0.02763 -0.22842 0.01886  285 VAL A CB  
2321 C CG1 . VAL A 285 ? 0.82454 0.48806 0.63551 -0.02794 -0.22745 0.02050  285 VAL A CG1 
2322 C CG2 . VAL A 285 ? 0.73041 0.39041 0.53430 -0.02593 -0.22618 0.01933  285 VAL A CG2 
2323 N N   . SER A 286 ? 0.70932 0.37286 0.53062 -0.03031 -0.23543 0.02281  286 SER A N   
2324 C CA  . SER A 286 ? 0.80589 0.46866 0.63140 -0.03191 -0.23815 0.02293  286 SER A CA  
2325 C C   . SER A 286 ? 0.68830 0.35177 0.51278 -0.03196 -0.23592 0.02215  286 SER A C   
2326 O O   . SER A 286 ? 0.68680 0.35604 0.51319 -0.03136 -0.23349 0.02396  286 SER A O   
2327 C CB  . SER A 286 ? 0.72057 0.39042 0.55500 -0.03249 -0.24017 0.02673  286 SER A CB  
2328 O OG  . SER A 286 ? 0.82186 0.48933 0.65789 -0.03303 -0.24353 0.02693  286 SER A OG  
2329 N N   . ASP A 287 ? 0.65234 0.31529 0.47536 -0.03104 -0.23454 0.02079  287 ASP A N   
2330 C CA  . ASP A 287 ? 0.57459 0.23909 0.39671 -0.03067 -0.23196 0.02024  287 ASP A CA  
2331 C C   . ASP A 287 ? 0.66139 0.32774 0.48924 -0.03177 -0.23433 0.02128  287 ASP A C   
2332 O O   . ASP A 287 ? 0.75068 0.41569 0.58002 -0.03156 -0.23637 0.02091  287 ASP A O   
2333 C CB  . ASP A 287 ? 0.58276 0.24510 0.39886 -0.02882 -0.22881 0.01810  287 ASP A CB  
2334 C CG  . ASP A 287 ? 0.67831 0.34184 0.49324 -0.02838 -0.22637 0.01752  287 ASP A CG  
2335 O OD1 . ASP A 287 ? 0.70689 0.37156 0.52531 -0.02884 -0.22775 0.01792  287 ASP A OD1 
2336 O OD2 . ASP A 287 ? 0.82493 0.48811 0.63558 -0.02760 -0.22332 0.01671  287 ASP A OD2 
2337 N N   . TYR A 288 ? 0.66611 0.33513 0.49688 -0.03280 -0.23424 0.02250  288 TYR A N   
2338 C CA  . TYR A 288 ? 0.64873 0.31972 0.48510 -0.03390 -0.23638 0.02361  288 TYR A CA  
2339 C C   . TYR A 288 ? 0.65887 0.32981 0.49192 -0.03263 -0.23335 0.02202  288 TYR A C   
2340 O O   . TYR A 288 ? 0.63965 0.31122 0.46946 -0.03217 -0.23043 0.02160  288 TYR A O   
2341 C CB  . TYR A 288 ? 0.62378 0.29999 0.46631 -0.03518 -0.23743 0.02682  288 TYR A CB  
2342 C CG  . TYR A 288 ? 0.62304 0.30446 0.47109 -0.03507 -0.23854 0.03004  288 TYR A CG  
2343 C CD1 . TYR A 288 ? 0.65076 0.33495 0.49673 -0.03354 -0.23607 0.03098  288 TYR A CD1 
2344 C CD2 . TYR A 288 ? 0.78039 0.46452 0.63628 -0.03636 -0.24205 0.03251  288 TYR A CD2 
2345 C CE1 . TYR A 288 ? 0.72808 0.41766 0.57923 -0.03308 -0.23685 0.03430  288 TYR A CE1 
2346 C CE2 . TYR A 288 ? 0.80365 0.49325 0.66532 -0.03617 -0.24297 0.03603  288 TYR A CE2 
2347 C CZ  . TYR A 288 ? 0.77615 0.46867 0.63533 -0.03440 -0.24021 0.03699  288 TYR A CZ  
2348 O OH  . TYR A 288 ? 0.87928 0.57756 0.74414 -0.03387 -0.24092 0.04073  288 TYR A OH  
2349 N N   . GLU A 289 ? 0.63171 0.30157 0.46546 -0.03201 -0.23436 0.02118  289 GLU A N   
2350 C CA  . GLU A 289 ? 0.68585 0.35505 0.51607 -0.03062 -0.23186 0.01963  289 GLU A CA  
2351 C C   . GLU A 289 ? 0.76005 0.43206 0.59483 -0.03178 -0.23270 0.02089  289 GLU A C   
2352 O O   . GLU A 289 ? 0.76436 0.43776 0.60540 -0.03325 -0.23617 0.02250  289 GLU A O   
2353 C CB  . GLU A 289 ? 0.68863 0.35445 0.51627 -0.02898 -0.23261 0.01786  289 GLU A CB  
2354 C CG  . GLU A 289 ? 0.79744 0.46198 0.62098 -0.02741 -0.23039 0.01633  289 GLU A CG  
2355 C CD  . GLU A 289 ? 0.73884 0.39900 0.55847 -0.02537 -0.23125 0.01442  289 GLU A CD  
2356 O OE1 . GLU A 289 ? 0.77519 0.43325 0.59489 -0.02509 -0.23327 0.01416  289 GLU A OE1 
2357 O OE2 . GLU A 289 ? 0.73451 0.39304 0.55092 -0.02397 -0.23021 0.01322  289 GLU A OE2 
2358 N N   . ARG A 290 ? 0.70407 0.37680 0.53595 -0.03119 -0.22978 0.02030  290 ARG A N   
2359 C CA  . ARG A 290 ? 0.61672 0.29179 0.45225 -0.03208 -0.23037 0.02132  290 ARG A CA  
2360 C C   . ARG A 290 ? 0.71848 0.39618 0.56107 -0.03435 -0.23368 0.02395  290 ARG A C   
2361 O O   . ARG A 290 ? 0.74499 0.42384 0.59283 -0.03532 -0.23639 0.02506  290 ARG A O   
2362 C CB  . ARG A 290 ? 0.56665 0.24000 0.40152 -0.03089 -0.23101 0.02001  290 ARG A CB  
2363 C CG  . ARG A 290 ? 0.67601 0.34643 0.50360 -0.02870 -0.22798 0.01774  290 ARG A CG  
2364 C CD  . ARG A 290 ? 0.68028 0.34888 0.50718 -0.02748 -0.22891 0.01661  290 ARG A CD  
2365 N NE  . ARG A 290 ? 0.66040 0.32585 0.48034 -0.02538 -0.22650 0.01469  290 ARG A NE  
2366 C CZ  . ARG A 290 ? 0.71159 0.37745 0.52898 -0.02495 -0.22425 0.01440  290 ARG A CZ  
2367 N NH1 . ARG A 290 ? 0.57584 0.24513 0.39692 -0.02638 -0.22397 0.01577  290 ARG A NH1 
2368 N NH2 . ARG A 290 ? 0.73054 0.39315 0.54163 -0.02312 -0.22255 0.01286  290 ARG A NH2 
2369 N N   . GLY A 291 ? 0.57332 0.25167 0.41594 -0.03514 -0.23364 0.02500  291 GLY A N   
2370 C CA  . GLY A 291 ? 0.56708 0.25206 0.41728 -0.03590 -0.23472 0.02884  291 GLY A CA  
2371 C C   . GLY A 291 ? 0.64257 0.33123 0.49299 -0.03496 -0.23308 0.03059  291 GLY A C   
2372 O O   . GLY A 291 ? 0.69191 0.37690 0.53589 -0.03420 -0.23131 0.02839  291 GLY A O   
2373 N N   . GLY A 292 ? 0.63446 0.33043 0.49233 -0.03484 -0.23359 0.03470  292 GLY A N   
2374 C CA  . GLY A 292 ? 0.63251 0.33284 0.49109 -0.03352 -0.23202 0.03688  292 GLY A CA  
2375 C C   . GLY A 292 ? 0.68417 0.39256 0.55199 -0.03338 -0.23306 0.04193  292 GLY A C   
2376 O O   . GLY A 292 ? 0.68899 0.40031 0.56295 -0.03427 -0.23453 0.04400  292 GLY A O   
2377 N N   . PRO A 293 ? 0.70241 0.41445 0.57148 -0.03216 -0.23233 0.04412  293 PRO A N   
2378 C CA  . PRO A 293 ? 0.70228 0.42282 0.58027 -0.03153 -0.23275 0.04960  293 PRO A CA  
2379 C C   . PRO A 293 ? 0.78241 0.51157 0.66577 -0.03011 -0.23020 0.05380  293 PRO A C   
2380 O O   . PRO A 293 ? 0.83351 0.56283 0.71257 -0.02902 -0.22737 0.05248  293 PRO A O   
2381 C CB  . PRO A 293 ? 0.67815 0.40162 0.55375 -0.02928 -0.23051 0.05083  293 PRO A CB  
2382 C CG  . PRO A 293 ? 0.67981 0.39709 0.54542 -0.02863 -0.22839 0.04616  293 PRO A CG  
2383 C CD  . PRO A 293 ? 0.64818 0.35642 0.51028 -0.03116 -0.23100 0.04168  293 PRO A CD  
2384 N N   . ALA A 294 ? 0.64527 0.38145 0.53805 -0.03003 -0.23125 0.05899  294 ALA A N   
2385 C CA  . ALA A 294 ? 0.70389 0.44874 0.60254 -0.02842 -0.22880 0.06371  294 ALA A CA  
2386 C C   . ALA A 294 ? 0.75182 0.50560 0.65155 -0.02458 -0.22476 0.06825  294 ALA A C   
2387 O O   . ALA A 294 ? 0.84036 0.60090 0.74173 -0.02216 -0.22149 0.07140  294 ALA A O   
2388 C CB  . ALA A 294 ? 0.61929 0.36642 0.52795 -0.03045 -0.23230 0.06703  294 ALA A CB  
2389 N N   . ASN A 295 ? 0.75220 0.50613 0.65115 -0.02382 -0.22508 0.06875  295 ASN A N   
2390 C CA  . ASN A 295 ? 0.84322 0.60522 0.74194 -0.01959 -0.22110 0.07271  295 ASN A CA  
2391 C C   . ASN A 295 ? 0.80674 0.56343 0.69599 -0.01866 -0.22001 0.06838  295 ASN A C   
2392 O O   . ASN A 295 ? 0.79833 0.54567 0.68168 -0.02122 -0.22195 0.06276  295 ASN A O   
2393 C CB  . ASN A 295 ? 0.96135 0.73081 0.86920 -0.01856 -0.22180 0.07891  295 ASN A CB  
2394 C CG  . ASN A 295 ? 1.17413 0.94846 1.09239 -0.01980 -0.22333 0.08351  295 ASN A CG  
2395 O OD1 . ASN A 295 ? 1.17383 0.94251 1.09490 -0.02365 -0.22742 0.08128  295 ASN A OD1 
2396 N ND2 . ASN A 295 ? 1.32958 1.11429 1.25356 -0.01631 -0.22012 0.09006  295 ASN A ND2 
2397 N N   . ILE A 296 ? 0.76720 0.52979 0.65519 -0.01485 -0.21697 0.07117  296 ILE A N   
2398 C CA  . ILE A 296 ? 0.67385 0.43172 0.55325 -0.01371 -0.21597 0.06741  296 ILE A CA  
2399 C C   . ILE A 296 ? 0.82124 0.57379 0.70114 -0.01609 -0.21947 0.06575  296 ILE A C   
2400 O O   . ILE A 296 ? 0.81105 0.56886 0.69777 -0.01556 -0.22047 0.07013  296 ILE A O   
2401 C CB  . ILE A 296 ? 0.66758 0.43353 0.54568 -0.00858 -0.21195 0.07108  296 ILE A CB  
2402 C CG1 . ILE A 296 ? 0.68521 0.45628 0.56275 -0.00611 -0.20877 0.07270  296 ILE A CG1 
2403 C CG2 . ILE A 296 ? 0.68938 0.45028 0.55909 -0.00745 -0.21127 0.06729  296 ILE A CG2 
2404 C CD1 . ILE A 296 ? 0.67966 0.45887 0.55546 -0.00049 -0.20483 0.07635  296 ILE A CD1 
2405 N N   . THR A 297 ? 0.82638 0.56894 0.69936 -0.01851 -0.22117 0.05980  297 THR A N   
2406 C CA  . THR A 297 ? 0.67715 0.41348 0.54952 -0.02080 -0.22466 0.05757  297 THR A CA  
2407 C C   . THR A 297 ? 0.75494 0.48771 0.61968 -0.01918 -0.22326 0.05492  297 THR A C   
2408 O O   . THR A 297 ? 0.69175 0.41946 0.54904 -0.01899 -0.22170 0.05099  297 THR A O   
2409 C CB  . THR A 297 ? 0.71594 0.44334 0.58670 -0.02463 -0.22803 0.05316  297 THR A CB  
2410 O OG1 . THR A 297 ? 0.84366 0.57498 0.72279 -0.02603 -0.22987 0.05628  297 THR A OG1 
2411 C CG2 . THR A 297 ? 0.72956 0.44919 0.59760 -0.02659 -0.23138 0.04998  297 THR A CG2 
2412 N N   . ARG A 298 ? 0.77698 0.51264 0.64410 -0.01804 -0.22388 0.05736  298 ARG A N   
2413 C CA  . ARG A 298 ? 0.82932 0.56171 0.68977 -0.01646 -0.22290 0.05516  298 ARG A CA  
2414 C C   . ARG A 298 ? 0.88114 0.60896 0.74289 -0.01862 -0.22660 0.05418  298 ARG A C   
2415 O O   . ARG A 298 ? 0.88377 0.61658 0.75334 -0.01896 -0.22841 0.05821  298 ARG A O   
2416 C CB  . ARG A 298 ? 0.79954 0.54114 0.66136 -0.01195 -0.21956 0.05970  298 ARG A CB  
2417 C CG  . ARG A 298 ? 0.82599 0.57391 0.68801 -0.00921 -0.21606 0.06190  298 ARG A CG  
2418 C CD  . ARG A 298 ? 0.79161 0.54832 0.65449 -0.00423 -0.21301 0.06647  298 ARG A CD  
2419 N NE  . ARG A 298 ? 0.78150 0.54364 0.64272 -0.00083 -0.20947 0.06809  298 ARG A NE  
2420 C CZ  . ARG A 298 ? 0.85107 0.60888 0.70452 0.00004  -0.20792 0.06415  298 ARG A CZ  
2421 N NH1 . ARG A 298 ? 0.79987 0.54792 0.64666 -0.00221 -0.20936 0.05858  298 ARG A NH1 
2422 N NH2 . ARG A 298 ? 0.94628 0.70952 0.79877 0.00327  -0.20501 0.06596  298 ARG A NH2 
2423 N N   . PRO A 299 ? 0.90257 0.62113 0.75722 -0.02003 -0.22787 0.04921  299 PRO A N   
2424 C CA  . PRO A 299 ? 0.79411 0.50881 0.64022 -0.01844 -0.22526 0.04597  299 PRO A CA  
2425 C C   . PRO A 299 ? 0.75764 0.46731 0.59924 -0.01972 -0.22431 0.04238  299 PRO A C   
2426 O O   . PRO A 299 ? 0.80520 0.51435 0.65011 -0.02173 -0.22573 0.04236  299 PRO A O   
2427 C CB  . PRO A 299 ? 0.71525 0.42270 0.55730 -0.01956 -0.22750 0.04307  299 PRO A CB  
2428 C CG  . PRO A 299 ? 0.86845 0.57153 0.71378 -0.02286 -0.23143 0.04200  299 PRO A CG  
2429 C CD  . PRO A 299 ? 1.01481 0.72617 0.86945 -0.02299 -0.23196 0.04671  299 PRO A CD  
2430 N N   . TYR A 300 ? 0.68933 0.39529 0.52370 -0.01853 -0.22211 0.03954  300 TYR A N   
2431 C CA  . TYR A 300 ? 0.65333 0.35508 0.48361 -0.01948 -0.22093 0.03652  300 TYR A CA  
2432 C C   . TYR A 300 ? 0.68002 0.37450 0.50957 -0.02272 -0.22359 0.03358  300 TYR A C   
2433 O O   . TYR A 300 ? 0.83010 0.51981 0.65858 -0.02389 -0.22593 0.03221  300 TYR A O   
2434 C CB  . TYR A 300 ? 0.67230 0.37022 0.49513 -0.01795 -0.21877 0.03387  300 TYR A CB  
2435 C CG  . TYR A 300 ? 0.61514 0.31216 0.43504 -0.01771 -0.21673 0.03238  300 TYR A CG  
2436 C CD1 . TYR A 300 ? 0.65275 0.34246 0.46883 -0.01993 -0.21725 0.02886  300 TYR A CD1 
2437 C CD2 . TYR A 300 ? 0.53329 0.23687 0.35407 -0.01497 -0.21425 0.03463  300 TYR A CD2 
2438 C CE1 . TYR A 300 ? 0.59111 0.28019 0.40488 -0.01976 -0.21547 0.02771  300 TYR A CE1 
2439 C CE2 . TYR A 300 ? 0.63055 0.33322 0.44870 -0.01472 -0.21261 0.03326  300 TYR A CE2 
2440 C CZ  . TYR A 300 ? 0.59247 0.28789 0.40732 -0.01727 -0.21328 0.02981  300 TYR A CZ  
2441 O OH  . TYR A 300 ? 0.60700 0.30177 0.41968 -0.01707 -0.21175 0.02871  300 TYR A OH  
2442 N N   . TRP A 301 ? 0.69812 0.39190 0.52801 -0.02381 -0.22317 0.03272  301 TRP A N   
2443 C CA  . TRP A 301 ? 0.67407 0.36152 0.50347 -0.02643 -0.22564 0.03024  301 TRP A CA  
2444 C C   . TRP A 301 ? 0.62891 0.31228 0.45372 -0.02691 -0.22405 0.02752  301 TRP A C   
2445 O O   . TRP A 301 ? 0.64808 0.33366 0.47065 -0.02546 -0.22131 0.02764  301 TRP A O   
2446 C CB  . TRP A 301 ? 0.60334 0.29550 0.44071 -0.02756 -0.22775 0.03310  301 TRP A CB  
2447 C CG  . TRP A 301 ? 0.66462 0.36539 0.50690 -0.02630 -0.22562 0.03661  301 TRP A CG  
2448 C CD1 . TRP A 301 ? 0.67311 0.38278 0.52048 -0.02424 -0.22429 0.04108  301 TRP A CD1 
2449 C CD2 . TRP A 301 ? 0.63145 0.33297 0.47396 -0.02671 -0.22442 0.03620  301 TRP A CD2 
2450 N NE1 . TRP A 301 ? 0.59198 0.30780 0.44258 -0.02323 -0.22231 0.04351  301 TRP A NE1 
2451 C CE2 . TRP A 301 ? 0.60855 0.31950 0.45632 -0.02484 -0.22243 0.04051  301 TRP A CE2 
2452 C CE3 . TRP A 301 ? 0.59484 0.29027 0.43361 -0.02820 -0.22471 0.03288  301 TRP A CE3 
2453 C CZ2 . TRP A 301 ? 0.51050 0.22472 0.35983 -0.02457 -0.22086 0.04140  301 TRP A CZ2 
2454 C CZ3 . TRP A 301 ? 0.59006 0.28884 0.43056 -0.02803 -0.22320 0.03376  301 TRP A CZ3 
2455 C CH2 . TRP A 301 ? 0.58717 0.29511 0.43289 -0.02633 -0.22139 0.03788  301 TRP A CH2 
2456 N N   . LEU A 302 ? 0.66304 0.34051 0.48649 -0.02873 -0.22592 0.02522  302 LEU A N   
2457 C CA  . LEU A 302 ? 0.56165 0.23507 0.38086 -0.02916 -0.22456 0.02282  302 LEU A CA  
2458 C C   . LEU A 302 ? 0.69039 0.36360 0.51296 -0.03056 -0.22625 0.02287  302 LEU A C   
2459 O O   . LEU A 302 ? 0.65876 0.33142 0.48501 -0.03158 -0.22925 0.02345  302 LEU A O   
2460 C CB  . LEU A 302 ? 0.59669 0.26180 0.40878 -0.02934 -0.22461 0.01951  302 LEU A CB  
2461 C CG  . LEU A 302 ? 0.57830 0.24372 0.38758 -0.02851 -0.22139 0.01826  302 LEU A CG  
2462 C CD1 . LEU A 302 ? 0.60086 0.26713 0.40835 -0.02830 -0.21932 0.01818  302 LEU A CD1 
2463 C CD2 . LEU A 302 ? 0.57640 0.23933 0.38119 -0.02731 -0.21981 0.01679  302 LEU A CD2 
2464 N N   . THR A 303 ? 0.66354 0.33676 0.48475 -0.03060 -0.22456 0.02215  303 THR A N   
2465 C CA  . THR A 303 ? 0.62388 0.29604 0.44721 -0.03173 -0.22598 0.02175  303 THR A CA  
2466 C C   . THR A 303 ? 0.59734 0.26848 0.41606 -0.03038 -0.22268 0.01990  303 THR A C   
2467 O O   . THR A 303 ? 0.59852 0.26953 0.41382 -0.02980 -0.22020 0.01933  303 THR A O   
2468 C CB  . THR A 303 ? 0.60323 0.28296 0.43202 -0.03149 -0.22477 0.02449  303 THR A CB  
2469 O OG1 . THR A 303 ? 0.76600 0.45155 0.60153 -0.03152 -0.22623 0.02769  303 THR A OG1 
2470 C CG2 . THR A 303 ? 0.51485 0.19272 0.34439 -0.03245 -0.22571 0.02356  303 THR A CG2 
2471 N N   . ASP A 304 ? 0.65226 0.32241 0.47074 -0.02981 -0.22289 0.01905  304 ASP A N   
2472 C CA  . ASP A 304 ? 0.68815 0.35719 0.50233 -0.02854 -0.22013 0.01756  304 ASP A CA  
2473 C C   . ASP A 304 ? 0.76873 0.43927 0.58575 -0.02889 -0.22071 0.01789  304 ASP A C   
2474 O O   . ASP A 304 ? 0.71095 0.38171 0.53181 -0.02937 -0.22338 0.01839  304 ASP A O   
2475 C CB  . ASP A 304 ? 0.66046 0.32627 0.47058 -0.02720 -0.21974 0.01612  304 ASP A CB  
2476 C CG  . ASP A 304 ? 0.76866 0.43289 0.57989 -0.02666 -0.22182 0.01558  304 ASP A CG  
2477 O OD1 . ASP A 304 ? 0.78555 0.45044 0.60129 -0.02753 -0.22477 0.01646  304 ASP A OD1 
2478 O OD2 . ASP A 304 ? 0.70134 0.36338 0.50878 -0.02533 -0.22072 0.01432  304 ASP A OD2 
2479 N N   . ASP A 305 ? 0.65913 0.33073 0.47474 -0.02877 -0.21858 0.01777  305 ASP A N   
2480 C CA  . ASP A 305 ? 0.66657 0.33949 0.48461 -0.02904 -0.21908 0.01807  305 ASP A CA  
2481 C C   . ASP A 305 ? 0.68145 0.35300 0.49498 -0.02783 -0.21663 0.01681  305 ASP A C   
2482 O O   . ASP A 305 ? 0.57557 0.24561 0.38467 -0.02712 -0.21458 0.01603  305 ASP A O   
2483 C CB  . ASP A 305 ? 0.76901 0.44478 0.59104 -0.03044 -0.21988 0.01969  305 ASP A CB  
2484 C CG  . ASP A 305 ? 0.83194 0.50928 0.65880 -0.03127 -0.22208 0.02065  305 ASP A CG  
2485 O OD1 . ASP A 305 ? 0.83653 0.51335 0.66217 -0.03053 -0.22132 0.01982  305 ASP A OD1 
2486 O OD2 . ASP A 305 ? 0.90707 0.58598 0.73892 -0.03271 -0.22477 0.02234  305 ASP A OD2 
2487 N N   . ALA A 306 ? 0.64376 0.31562 0.45851 -0.02768 -0.21717 0.01673  306 ALA A N   
2488 C CA  . ALA A 306 ? 0.69001 0.36035 0.50066 -0.02658 -0.21533 0.01571  306 ALA A CA  
2489 C C   . ALA A 306 ? 0.64202 0.31475 0.45456 -0.02733 -0.21469 0.01652  306 ALA A C   
2490 O O   . ALA A 306 ? 0.70219 0.37722 0.51951 -0.02842 -0.21634 0.01768  306 ALA A O   
2491 C CB  . ALA A 306 ? 0.56723 0.23461 0.37623 -0.02519 -0.21670 0.01452  306 ALA A CB  
2492 N N   . ILE A 307 ? 0.64811 0.32011 0.45690 -0.02682 -0.21255 0.01604  307 ILE A N   
2493 C CA  . ILE A 307 ? 0.64376 0.31761 0.45378 -0.02741 -0.21193 0.01670  307 ILE A CA  
2494 C C   . ILE A 307 ? 0.67780 0.35142 0.48951 -0.02705 -0.21346 0.01658  307 ILE A C   
2495 O O   . ILE A 307 ? 0.61385 0.28913 0.42733 -0.02763 -0.21344 0.01728  307 ILE A O   
2496 C CB  . ILE A 307 ? 0.60709 0.27990 0.41269 -0.02706 -0.20961 0.01630  307 ILE A CB  
2497 C CG1 . ILE A 307 ? 0.57824 0.25348 0.38560 -0.02804 -0.20893 0.01728  307 ILE A CG1 
2498 C CG2 . ILE A 307 ? 0.69060 0.36025 0.49210 -0.02572 -0.20951 0.01522  307 ILE A CG2 
2499 C CD1 . ILE A 307 ? 0.61584 0.29030 0.41960 -0.02804 -0.20704 0.01716  307 ILE A CD1 
2500 N N   . SER A 308 ? 0.66937 0.34057 0.48025 -0.02597 -0.21493 0.01562  308 SER A N   
2501 C CA  . SER A 308 ? 0.65629 0.32663 0.46861 -0.02534 -0.21685 0.01527  308 SER A CA  
2502 C C   . SER A 308 ? 0.73526 0.40550 0.55142 -0.02553 -0.21968 0.01538  308 SER A C   
2503 O O   . SER A 308 ? 0.63497 0.30395 0.45009 -0.02525 -0.21994 0.01496  308 SER A O   
2504 C CB  . SER A 308 ? 0.64305 0.30949 0.44985 -0.02341 -0.21644 0.01374  308 SER A CB  
2505 O OG  . SER A 308 ? 0.73205 0.39619 0.53960 -0.02253 -0.21925 0.01312  308 SER A OG  
2506 N N   . ALA A 309 ? 0.74799 0.41921 0.56839 -0.02597 -0.22198 0.01592  309 ALA A N   
2507 C CA  . ALA A 309 ? 0.73443 0.40563 0.55936 -0.02645 -0.22527 0.01629  309 ALA A CA  
2508 C C   . ALA A 309 ? 0.70934 0.37500 0.53032 -0.02445 -0.22743 0.01438  309 ALA A C   
2509 O O   . ALA A 309 ? 0.71161 0.37607 0.53527 -0.02459 -0.23045 0.01436  309 ALA A O   
2510 C CB  . ALA A 309 ? 0.62379 0.29759 0.45492 -0.02797 -0.22761 0.01788  309 ALA A CB  
2511 N N   . SER A 310 ? 0.75038 0.41245 0.56496 -0.02258 -0.22616 0.01286  310 SER A N   
2512 C CA  . SER A 310 ? 0.73758 0.39337 0.54726 -0.02020 -0.22852 0.01086  310 SER A CA  
2513 C C   . SER A 310 ? 0.78455 0.43676 0.58832 -0.01865 -0.22742 0.00957  310 SER A C   
2514 O O   . SER A 310 ? 0.80068 0.44955 0.60383 -0.01767 -0.23002 0.00865  310 SER A O   
2515 C CB  . SER A 310 ? 0.64112 0.29435 0.44700 -0.01890 -0.22846 0.01005  310 SER A CB  
2516 O OG  . SER A 310 ? 1.00564 0.65783 0.80574 -0.01812 -0.22530 0.00963  310 SER A OG  
2517 N N   . SER A 311 ? 0.73662 0.38913 0.53618 -0.01843 -0.22406 0.00952  311 SER A N   
2518 C CA  . SER A 311 ? 0.70826 0.35698 0.50173 -0.01694 -0.22313 0.00840  311 SER A CA  
2519 C C   . SER A 311 ? 0.78305 0.43571 0.57733 -0.01841 -0.21981 0.00948  311 SER A C   
2520 O O   . SER A 311 ? 0.86636 0.52402 0.66474 -0.02019 -0.21807 0.01085  311 SER A O   
2521 C CB  . SER A 311 ? 0.60247 0.24563 0.38814 -0.01467 -0.22305 0.00699  311 SER A CB  
2522 O OG  . SER A 311 ? 0.86792 0.50727 0.64763 -0.01331 -0.22235 0.00611  311 SER A OG  
2523 N N   . TRP A 312 ? 0.73582 0.38591 0.52614 -0.01753 -0.21926 0.00880  312 TRP A N   
2524 C CA  . TRP A 312 ? 0.65212 0.30452 0.44192 -0.01866 -0.21658 0.00957  312 TRP A CA  
2525 C C   . TRP A 312 ? 0.68472 0.33400 0.46791 -0.01756 -0.21494 0.00897  312 TRP A C   
2526 O O   . TRP A 312 ? 0.76402 0.41454 0.54613 -0.01855 -0.21297 0.00964  312 TRP A O   
2527 C CB  . TRP A 312 ? 0.67991 0.33110 0.46964 -0.01855 -0.21751 0.00935  312 TRP A CB  
2528 C CG  . TRP A 312 ? 0.68573 0.33969 0.48191 -0.01981 -0.21952 0.01014  312 TRP A CG  
2529 C CD1 . TRP A 312 ? 0.66862 0.32156 0.46748 -0.01932 -0.22242 0.00976  312 TRP A CD1 
2530 C CD2 . TRP A 312 ? 0.72437 0.38217 0.52499 -0.02175 -0.21917 0.01153  312 TRP A CD2 
2531 N NE1 . TRP A 312 ? 0.70898 0.36510 0.51403 -0.02109 -0.22396 0.01102  312 TRP A NE1 
2532 C CE2 . TRP A 312 ? 0.73211 0.39110 0.53809 -0.02251 -0.22202 0.01211  312 TRP A CE2 
2533 C CE3 . TRP A 312 ? 0.65400 0.31398 0.45443 -0.02283 -0.21702 0.01233  312 TRP A CE3 
2534 C CZ2 . TRP A 312 ? 0.72576 0.38795 0.53666 -0.02434 -0.22280 0.01359  312 TRP A CZ2 
2535 C CZ3 . TRP A 312 ? 0.62974 0.29263 0.43464 -0.02436 -0.21770 0.01354  312 TRP A CZ3 
2536 C CH2 . TRP A 312 ? 0.70720 0.37114 0.51716 -0.02512 -0.22058 0.01422  312 TRP A CH2 
2537 N N   . SER A 313 ? 0.74607 0.39023 0.52439 -0.01558 -0.21655 0.00775  313 SER A N   
2538 C CA  . SER A 313 ? 0.79117 0.43107 0.56227 -0.01439 -0.21577 0.00723  313 SER A CA  
2539 C C   . SER A 313 ? 0.70261 0.34224 0.47346 -0.01423 -0.21617 0.00730  313 SER A C   
2540 O O   . SER A 313 ? 0.74302 0.38411 0.51798 -0.01434 -0.21768 0.00728  313 SER A O   
2541 C CB  . SER A 313 ? 0.66495 0.29748 0.42852 -0.01175 -0.21763 0.00562  313 SER A CB  
2542 O OG  . SER A 313 ? 0.76751 0.39520 0.52366 -0.01046 -0.21744 0.00516  313 SER A OG  
2543 N N   . TYR A 314 ? 0.71029 0.34759 0.47618 -0.01395 -0.21523 0.00742  314 TYR A N   
2544 C CA  . TYR A 314 ? 0.75672 0.39405 0.52249 -0.01403 -0.21549 0.00771  314 TYR A CA  
2545 C C   . TYR A 314 ? 0.69368 0.32467 0.45452 -0.01124 -0.21840 0.00606  314 TYR A C   
2546 O O   . TYR A 314 ? 0.77970 0.40421 0.53353 -0.00881 -0.21982 0.00466  314 TYR A O   
2547 C CB  . TYR A 314 ? 0.65531 0.29227 0.41779 -0.01495 -0.21387 0.00860  314 TYR A CB  
2548 C CG  . TYR A 314 ? 0.65548 0.29265 0.41684 -0.01435 -0.21396 0.00914  314 TYR A CG  
2549 C CD1 . TYR A 314 ? 0.73664 0.37908 0.50417 -0.01620 -0.21322 0.01025  314 TYR A CD1 
2550 C CD2 . TYR A 314 ? 0.68980 0.32461 0.44470 -0.01123 -0.21383 0.00923  314 TYR A CD2 
2551 C CE1 . TYR A 314 ? 0.73886 0.38397 0.50640 -0.01520 -0.21247 0.01137  314 TYR A CE1 
2552 C CE2 . TYR A 314 ? 0.74457 0.38213 0.49929 -0.01006 -0.21302 0.01042  314 TYR A CE2 
2553 C CZ  . TYR A 314 ? 0.79664 0.43927 0.55783 -0.01216 -0.21239 0.01146  314 TYR A CZ  
2554 O OH  . TYR A 314 ? 0.85340 0.49885 0.61454 -0.01096 -0.21160 0.01276  314 TYR A OH  
2555 N N   . THR A 315 ? 0.68265 0.31516 0.44671 -0.01142 -0.21938 0.00620  315 THR A N   
2556 C CA  . THR A 315 ? 0.81201 0.43851 0.57160 -0.00866 -0.22235 0.00458  315 THR A CA  
2557 C C   . THR A 315 ? 0.77077 0.39850 0.53131 -0.00926 -0.22224 0.00526  315 THR A C   
2558 O O   . THR A 315 ? 0.76736 0.40180 0.53509 -0.01191 -0.22073 0.00686  315 THR A O   
2559 C CB  . THR A 315 ? 0.69883 0.32574 0.46276 -0.00816 -0.22475 0.00384  315 THR A CB  
2560 O OG1 . THR A 315 ? 0.88393 0.51795 0.65670 -0.01087 -0.22402 0.00543  315 THR A OG1 
2561 C CG2 . THR A 315 ? 0.69982 0.32623 0.46391 -0.00796 -0.22494 0.00343  315 THR A CG2 
2562 N N   . VAL A 316 ? 0.85950 0.48177 0.61307 -0.00652 -0.22349 0.00433  316 VAL A N   
2563 C CA  . VAL A 316 ? 0.86172 0.48856 0.61753 -0.00623 -0.22235 0.00582  316 VAL A CA  
2564 C C   . VAL A 316 ? 0.84829 0.47546 0.61062 -0.00825 -0.22500 0.00522  316 VAL A C   
2565 O O   . VAL A 316 ? 0.70275 0.32693 0.46523 -0.00677 -0.22771 0.00378  316 VAL A O   
2566 C CB  . VAL A 316 ? 0.87898 0.50231 0.62725 -0.00181 -0.22277 0.00539  316 VAL A CB  
2567 C CG1 . VAL A 316 ? 0.78979 0.41787 0.54064 -0.00148 -0.22167 0.00705  316 VAL A CG1 
2568 C CG2 . VAL A 316 ? 0.79255 0.41636 0.53444 0.00037  -0.22012 0.00647  316 VAL A CG2 
2569 N N   . GLY A 317 ? 0.81051 0.44540 0.57970 -0.01082 -0.22279 0.00739  317 GLY A N   
2570 C CA  . GLY A 317 ? 0.75167 0.38928 0.52790 -0.01254 -0.22453 0.00769  317 GLY A CA  
2571 C C   . GLY A 317 ? 0.70901 0.35285 0.49266 -0.01485 -0.22331 0.00886  317 GLY A C   
2572 O O   . GLY A 317 ? 0.87829 0.52552 0.66830 -0.01601 -0.22455 0.00956  317 GLY A O   
2573 N N   . ILE A 318 ? 0.74710 0.39207 0.52970 -0.01546 -0.22118 0.00912  318 ILE A N   
2574 C CA  . ILE A 318 ? 0.72253 0.37311 0.51159 -0.01749 -0.21998 0.01021  318 ILE A CA  
2575 C C   . ILE A 318 ? 0.76501 0.42183 0.56038 -0.01990 -0.21863 0.01207  318 ILE A C   
2576 O O   . ILE A 318 ? 0.67035 0.32777 0.46428 -0.02040 -0.21732 0.01267  318 ILE A O   
2577 C CB  . ILE A 318 ? 0.69631 0.34671 0.48264 -0.01759 -0.21791 0.01013  318 ILE A CB  
2578 C CG1 . ILE A 318 ? 0.70556 0.36050 0.49767 -0.01912 -0.21731 0.01092  318 ILE A CG1 
2579 C CG2 . ILE A 318 ? 0.70768 0.35907 0.49159 -0.01849 -0.21544 0.01095  318 ILE A CG2 
2580 C CD1 . ILE A 318 ? 0.68571 0.33842 0.47459 -0.01835 -0.21682 0.01017  318 ILE A CD1 
2581 N N   . GLN A 319 ? 0.79523 0.45605 0.59713 -0.02128 -0.21935 0.01297  319 GLN A N   
2582 C CA  . GLN A 319 ? 0.75207 0.41847 0.55966 -0.02343 -0.21829 0.01479  319 GLN A CA  
2583 C C   . GLN A 319 ? 0.67186 0.34197 0.48245 -0.02473 -0.21667 0.01561  319 GLN A C   
2584 O O   . GLN A 319 ? 0.65235 0.32116 0.46249 -0.02421 -0.21730 0.01496  319 GLN A O   
2585 C CB  . GLN A 319 ? 0.73048 0.39788 0.54285 -0.02393 -0.22100 0.01540  319 GLN A CB  
2586 C CG  . GLN A 319 ? 0.82649 0.48971 0.63534 -0.02238 -0.22274 0.01441  319 GLN A CG  
2587 C CD  . GLN A 319 ? 0.98040 0.64557 0.79457 -0.02335 -0.22496 0.01547  319 GLN A CD  
2588 O OE1 . GLN A 319 ? 0.93131 0.60008 0.75172 -0.02496 -0.22600 0.01678  319 GLN A OE1 
2589 N NE2 . GLN A 319 ? 1.08670 0.75010 0.89862 -0.02217 -0.22557 0.01523  319 GLN A NE2 
2590 N N   . TYR A 320 ? 0.71468 0.38857 0.52800 -0.02628 -0.21523 0.01697  320 TYR A N   
2591 C CA  . TYR A 320 ? 0.66671 0.34232 0.48112 -0.02729 -0.21429 0.01757  320 TYR A CA  
2592 C C   . TYR A 320 ? 0.60277 0.28176 0.42290 -0.02896 -0.21556 0.01919  320 TYR A C   
2593 O O   . TYR A 320 ? 0.61087 0.29316 0.43446 -0.02906 -0.21574 0.02049  320 TYR A O   
2594 C CB  . TYR A 320 ? 0.60540 0.28079 0.41609 -0.02740 -0.21181 0.01753  320 TYR A CB  
2595 C CG  . TYR A 320 ? 0.60333 0.27522 0.40828 -0.02602 -0.21085 0.01634  320 TYR A CG  
2596 C CD1 . TYR A 320 ? 0.66938 0.33849 0.47082 -0.02497 -0.21064 0.01529  320 TYR A CD1 
2597 C CD2 . TYR A 320 ? 0.71501 0.38603 0.51778 -0.02581 -0.21041 0.01640  320 TYR A CD2 
2598 C CE1 . TYR A 320 ? 0.64394 0.30926 0.43961 -0.02368 -0.21011 0.01434  320 TYR A CE1 
2599 C CE2 . TYR A 320 ? 0.70625 0.37401 0.50350 -0.02447 -0.20978 0.01565  320 TYR A CE2 
2600 C CZ  . TYR A 320 ? 0.70329 0.36730 0.49653 -0.02354 -0.21000 0.01449  320 TYR A CZ  
2601 O OH  . TYR A 320 ? 0.75481 0.41383 0.54154 -0.02236 -0.21029 0.01372  320 TYR A OH  
2602 N N   . TYR A 321 ? 0.60298 0.28287 0.42445 -0.02961 -0.21566 0.01964  321 TYR A N   
2603 C CA  . TYR A 321 ? 0.60463 0.28952 0.43159 -0.03052 -0.21602 0.02187  321 TYR A CA  
2604 C C   . TYR A 321 ? 0.72470 0.41473 0.55203 -0.03000 -0.21285 0.02340  321 TYR A C   
2605 O O   . TYR A 321 ? 0.66562 0.35384 0.48885 -0.02962 -0.21121 0.02239  321 TYR A O   
2606 C CB  . TYR A 321 ? 0.56673 0.25092 0.39436 -0.03111 -0.21698 0.02195  321 TYR A CB  
2607 C CG  . TYR A 321 ? 0.75541 0.43726 0.58497 -0.03150 -0.21999 0.02146  321 TYR A CG  
2608 C CD1 . TYR A 321 ? 0.64059 0.32506 0.47626 -0.03235 -0.22252 0.02317  321 TYR A CD1 
2609 C CD2 . TYR A 321 ? 0.71298 0.39252 0.53930 -0.03035 -0.21935 0.02006  321 TYR A CD2 
2610 C CE1 . TYR A 321 ? 0.71500 0.39761 0.55301 -0.03276 -0.22551 0.02289  321 TYR A CE1 
2611 C CE2 . TYR A 321 ? 0.67793 0.35649 0.50640 -0.03024 -0.22168 0.01989  321 TYR A CE2 
2612 C CZ  . TYR A 321 ? 0.70046 0.38061 0.53492 -0.03146 -0.22480 0.02129  321 TYR A CZ  
2613 O OH  . TYR A 321 ? 0.75662 0.43577 0.59366 -0.03147 -0.22745 0.02121  321 TYR A OH  
2614 N N   . SER A 322 ? 0.68430 0.38075 0.51652 -0.02982 -0.21211 0.02596  322 SER A N   
2615 C CA  . SER A 322 ? 0.70539 0.40693 0.53814 -0.02901 -0.20937 0.02751  322 SER A CA  
2616 C C   . SER A 322 ? 0.65272 0.35429 0.48330 -0.02873 -0.20820 0.02736  322 SER A C   
2617 O O   . SER A 322 ? 0.57426 0.27389 0.40471 -0.02910 -0.20942 0.02693  322 SER A O   
2618 C CB  . SER A 322 ? 0.57745 0.28607 0.41627 -0.02842 -0.20908 0.03057  322 SER A CB  
2619 O OG  . SER A 322 ? 0.67111 0.38337 0.51358 -0.02821 -0.20951 0.03253  322 SER A OG  
2620 N N   . SER A 323 ? 0.66749 0.37110 0.49643 -0.02803 -0.20608 0.02770  323 SER A N   
2621 C CA  . SER A 323 ? 0.64868 0.35237 0.47550 -0.02747 -0.20509 0.02756  323 SER A CA  
2622 C C   . SER A 323 ? 0.58016 0.28919 0.41093 -0.02648 -0.20511 0.02987  323 SER A C   
2623 O O   . SER A 323 ? 0.69584 0.40370 0.52519 -0.02618 -0.20526 0.02951  323 SER A O   
2624 C CB  . SER A 323 ? 0.69823 0.40313 0.52302 -0.02686 -0.20329 0.02757  323 SER A CB  
2625 O OG  . SER A 323 ? 0.85364 0.55488 0.67576 -0.02767 -0.20323 0.02616  323 SER A OG  
2626 N N   . LYS A 324 ? 0.64095 0.35585 0.47668 -0.02584 -0.20494 0.03241  324 LYS A N   
2627 C CA  . LYS A 324 ? 0.69662 0.41788 0.53669 -0.02451 -0.20465 0.03543  324 LYS A CA  
2628 C C   . LYS A 324 ? 0.67534 0.39454 0.51713 -0.02548 -0.20676 0.03538  324 LYS A C   
2629 O O   . LYS A 324 ? 0.69889 0.42077 0.54162 -0.02446 -0.20647 0.03677  324 LYS A O   
2630 C CB  . LYS A 324 ? 0.66037 0.38843 0.50580 -0.02363 -0.20405 0.03856  324 LYS A CB  
2631 C CG  . LYS A 324 ? 0.68327 0.41844 0.53392 -0.02211 -0.20374 0.04238  324 LYS A CG  
2632 C CD  . LYS A 324 ? 0.64220 0.38323 0.49894 -0.02164 -0.20367 0.04566  324 LYS A CD  
2633 C CE  . LYS A 324 ? 0.77664 0.52133 0.63285 -0.02025 -0.20160 0.04651  324 LYS A CE  
2634 N NZ  . LYS A 324 ? 0.92177 0.67080 0.77590 -0.01767 -0.19935 0.04769  324 LYS A NZ  
2635 N N   . ALA A 325 ? 0.64458 0.35932 0.48672 -0.02717 -0.20890 0.03390  325 ALA A N   
2636 C CA  . ALA A 325 ? 0.65996 0.37247 0.50406 -0.02820 -0.21143 0.03380  325 ALA A CA  
2637 C C   . ALA A 325 ? 0.62603 0.33425 0.46561 -0.02826 -0.21144 0.03186  325 ALA A C   
2638 O O   . ALA A 325 ? 0.65692 0.36753 0.49868 -0.02783 -0.21190 0.03337  325 ALA A O   
2639 C CB  . ALA A 325 ? 0.66053 0.36800 0.50451 -0.02968 -0.21384 0.03196  325 ALA A CB  
2640 N N   . MET A 326 ? 0.59693 0.29965 0.43067 -0.02857 -0.21072 0.02903  326 MET A N   
2641 C CA  . MET A 326 ? 0.57056 0.26873 0.39969 -0.02861 -0.21064 0.02714  326 MET A CA  
2642 C C   . MET A 326 ? 0.59177 0.29465 0.42134 -0.02697 -0.20894 0.02885  326 MET A C   
2643 O O   . MET A 326 ? 0.60644 0.30897 0.43596 -0.02671 -0.20959 0.02906  326 MET A O   
2644 C CB  . MET A 326 ? 0.55848 0.25095 0.38196 -0.02906 -0.20988 0.02450  326 MET A CB  
2645 C CG  . MET A 326 ? 0.63868 0.32688 0.46111 -0.03001 -0.21128 0.02298  326 MET A CG  
2646 S SD  . MET A 326 ? 0.65276 0.33515 0.47440 -0.03091 -0.21440 0.02137  326 MET A SD  
2647 C CE  . MET A 326 ? 0.61674 0.30470 0.44605 -0.03122 -0.21632 0.02400  326 MET A CE  
2648 N N   . VAL A 327 ? 0.60472 0.31222 0.43487 -0.02564 -0.20694 0.03020  327 VAL A N   
2649 C CA  . VAL A 327 ? 0.57119 0.28256 0.40072 -0.02359 -0.20540 0.03151  327 VAL A CA  
2650 C C   . VAL A 327 ? 0.61328 0.33112 0.44785 -0.02233 -0.20559 0.03479  327 VAL A C   
2651 O O   . VAL A 327 ? 0.61268 0.33156 0.44646 -0.02109 -0.20536 0.03537  327 VAL A O   
2652 C CB  . VAL A 327 ? 0.70621 0.42070 0.53477 -0.02222 -0.20344 0.03206  327 VAL A CB  
2653 C CG1 . VAL A 327 ? 0.62698 0.34644 0.45528 -0.01947 -0.20202 0.03379  327 VAL A CG1 
2654 C CG2 . VAL A 327 ? 0.67499 0.38316 0.49855 -0.02335 -0.20328 0.02914  327 VAL A CG2 
2655 N N   . HIS A 328 ? 0.60866 0.33089 0.44860 -0.02258 -0.20606 0.03714  328 HIS A N   
2656 C CA  . HIS A 328 ? 0.55496 0.28415 0.40072 -0.02134 -0.20620 0.04105  328 HIS A CA  
2657 C C   . HIS A 328 ? 0.61750 0.34334 0.46404 -0.02267 -0.20846 0.04045  328 HIS A C   
2658 O O   . HIS A 328 ? 0.70742 0.43758 0.55626 -0.02120 -0.20817 0.04292  328 HIS A O   
2659 C CB  . HIS A 328 ? 0.57141 0.30586 0.42307 -0.02138 -0.20625 0.04391  328 HIS A CB  
2660 C CG  . HIS A 328 ? 0.60322 0.34302 0.45503 -0.01934 -0.20379 0.04558  328 HIS A CG  
2661 N ND1 . HIS A 328 ? 0.62120 0.36848 0.47889 -0.01809 -0.20303 0.04963  328 HIS A ND1 
2662 C CD2 . HIS A 328 ? 0.57784 0.31668 0.42499 -0.01832 -0.20211 0.04396  328 HIS A CD2 
2663 C CE1 . HIS A 328 ? 0.58672 0.33750 0.44293 -0.01621 -0.20085 0.05031  328 HIS A CE1 
2664 N NE2 . HIS A 328 ? 0.51988 0.26555 0.36976 -0.01639 -0.20040 0.04682  328 HIS A NE2 
2665 N N   . SER A 329 ? 0.56384 0.28236 0.40835 -0.02510 -0.21061 0.03737  329 SER A N   
2666 C CA  . SER A 329 ? 0.63159 0.34627 0.47647 -0.02639 -0.21309 0.03650  329 SER A CA  
2667 C C   . SER A 329 ? 0.56804 0.28051 0.40829 -0.02539 -0.21220 0.03524  329 SER A C   
2668 O O   . SER A 329 ? 0.58035 0.29510 0.42288 -0.02485 -0.21291 0.03692  329 SER A O   
2669 C CB  . SER A 329 ? 0.60876 0.31616 0.45193 -0.02866 -0.21553 0.03351  329 SER A CB  
2670 O OG  . SER A 329 ? 0.63603 0.34542 0.48282 -0.02923 -0.21610 0.03448  329 SER A OG  
2671 N N   . LEU A 330 ? 0.64487 0.35374 0.47933 -0.02498 -0.21062 0.03281  330 LEU A N   
2672 C CA  . LEU A 330 ? 0.61155 0.31814 0.44147 -0.02388 -0.20977 0.03159  330 LEU A CA  
2673 C C   . LEU A 330 ? 0.56426 0.27847 0.39681 -0.02120 -0.20834 0.03490  330 LEU A C   
2674 O O   . LEU A 330 ? 0.64796 0.36205 0.48004 -0.02052 -0.20880 0.03525  330 LEU A O   
2675 C CB  . LEU A 330 ? 0.48225 0.18456 0.30658 -0.02383 -0.20838 0.02902  330 LEU A CB  
2676 C CG  . LEU A 330 ? 0.55639 0.25656 0.37615 -0.02249 -0.20746 0.02790  330 LEU A CG  
2677 C CD1 . LEU A 330 ? 0.49005 0.18544 0.30791 -0.02332 -0.20899 0.02652  330 LEU A CD1 
2678 C CD2 . LEU A 330 ? 0.52747 0.22347 0.34262 -0.02274 -0.20646 0.02569  330 LEU A CD2 
2679 N N   . LEU A 331 ? 0.56967 0.29063 0.40511 -0.01954 -0.20669 0.03752  331 LEU A N   
2680 C CA  . LEU A 331 ? 0.51710 0.24614 0.35478 -0.01625 -0.20496 0.04113  331 LEU A CA  
2681 C C   . LEU A 331 ? 0.57735 0.31081 0.42076 -0.01610 -0.20609 0.04441  331 LEU A C   
2682 O O   . LEU A 331 ? 0.72548 0.46299 0.56913 -0.01366 -0.20516 0.04648  331 LEU A O   
2683 C CB  . LEU A 331 ? 0.56804 0.30334 0.40760 -0.01441 -0.20300 0.04339  331 LEU A CB  
2684 C CG  . LEU A 331 ? 0.60288 0.33495 0.43715 -0.01404 -0.20181 0.04071  331 LEU A CG  
2685 C CD1 . LEU A 331 ? 0.61206 0.35076 0.44891 -0.01231 -0.20017 0.04323  331 LEU A CD1 
2686 C CD2 . LEU A 331 ? 0.51895 0.24931 0.34799 -0.01196 -0.20098 0.03936  331 LEU A CD2 
2687 N N   . ASP A 332 ? 0.60151 0.33423 0.44948 -0.01848 -0.20815 0.04497  332 ASP A N   
2688 C CA  . ASP A 332 ? 0.62971 0.36681 0.48421 -0.01856 -0.20961 0.04848  332 ASP A CA  
2689 C C   . ASP A 332 ? 0.62397 0.35583 0.47593 -0.01956 -0.21137 0.04645  332 ASP A C   
2690 O O   . ASP A 332 ? 0.65536 0.39182 0.51022 -0.01802 -0.21124 0.04939  332 ASP A O   
2691 C CB  . ASP A 332 ? 0.62045 0.35785 0.48072 -0.02086 -0.21171 0.04955  332 ASP A CB  
2692 C CG  . ASP A 332 ? 0.75109 0.49284 0.61902 -0.02126 -0.21360 0.05339  332 ASP A CG  
2693 O OD1 . ASP A 332 ? 0.71648 0.46677 0.58885 -0.01863 -0.21180 0.05819  332 ASP A OD1 
2694 O OD2 . ASP A 332 ? 0.71699 0.45354 0.58641 -0.02403 -0.21691 0.05170  332 ASP A OD2 
2695 N N   . ARG A 333 ? 0.61594 0.33878 0.46262 -0.02179 -0.21276 0.04184  333 ARG A N   
2696 C CA  . ARG A 333 ? 0.60124 0.31821 0.44484 -0.02278 -0.21448 0.03956  333 ARG A CA  
2697 C C   . ARG A 333 ? 0.61777 0.33660 0.45800 -0.02017 -0.21254 0.04001  333 ARG A C   
2698 O O   . ARG A 333 ? 0.67098 0.39116 0.51277 -0.01962 -0.21339 0.04139  333 ARG A O   
2699 C CB  . ARG A 333 ? 0.59528 0.30279 0.43335 -0.02503 -0.21564 0.03488  333 ARG A CB  
2700 C CG  . ARG A 333 ? 0.56378 0.26959 0.40410 -0.02692 -0.21706 0.03424  333 ARG A CG  
2701 C CD  . ARG A 333 ? 0.66420 0.36728 0.50798 -0.02893 -0.22059 0.03409  333 ARG A CD  
2702 N NE  . ARG A 333 ? 0.68596 0.38819 0.53207 -0.03025 -0.22182 0.03376  333 ARG A NE  
2703 C CZ  . ARG A 333 ? 0.73865 0.43500 0.58014 -0.03104 -0.22179 0.03058  333 ARG A CZ  
2704 N NH1 . ARG A 333 ? 0.75786 0.44902 0.59253 -0.03073 -0.22043 0.02773  333 ARG A NH1 
2705 N NH2 . ARG A 333 ? 0.71433 0.41039 0.55824 -0.03196 -0.22302 0.03054  333 ARG A NH2 
2706 N N   . ILE A 334 ? 0.58951 0.30864 0.42553 -0.01847 -0.21017 0.03905  334 ILE A N   
2707 C CA  . ILE A 334 ? 0.54505 0.26508 0.37709 -0.01578 -0.20854 0.03902  334 ILE A CA  
2708 C C   . ILE A 334 ? 0.57365 0.30364 0.41045 -0.01256 -0.20713 0.04397  334 ILE A C   
2709 O O   . ILE A 334 ? 0.65805 0.38964 0.49352 -0.01045 -0.20661 0.04489  334 ILE A O   
2710 C CB  . ILE A 334 ? 0.53398 0.25073 0.36025 -0.01504 -0.20693 0.03638  334 ILE A CB  
2711 C CG1 . ILE A 334 ? 0.65287 0.37589 0.48133 -0.01337 -0.20509 0.03855  334 ILE A CG1 
2712 C CG2 . ILE A 334 ? 0.56765 0.27517 0.38982 -0.01804 -0.20816 0.03221  334 ILE A CG2 
2713 C CD1 . ILE A 334 ? 0.67464 0.39481 0.49776 -0.01245 -0.20375 0.03621  334 ILE A CD1 
2714 N N   . SER A 335 ? 0.58776 0.32428 0.43008 -0.01208 -0.20651 0.04729  335 SER A N   
2715 C CA  . SER A 335 ? 0.60493 0.35172 0.45264 -0.00880 -0.20500 0.05286  335 SER A CA  
2716 C C   . SER A 335 ? 0.67251 0.42046 0.52482 -0.00965 -0.20691 0.05497  335 SER A C   
2717 O O   . SER A 335 ? 0.64834 0.40325 0.50319 -0.00653 -0.20560 0.05895  335 SER A O   
2718 C CB  . SER A 335 ? 0.58923 0.34240 0.44224 -0.00830 -0.20403 0.05613  335 SER A CB  
2719 O OG  . SER A 335 ? 0.63307 0.38541 0.49194 -0.01142 -0.20644 0.05699  335 SER A OG  
2720 N N   . LYS A 336 ? 0.59779 0.33896 0.45071 -0.01349 -0.20993 0.05231  336 LYS A N   
2721 C CA  . LYS A 336 ? 0.59279 0.33461 0.45056 -0.01467 -0.21234 0.05419  336 LYS A CA  
2722 C C   . LYS A 336 ? 0.68757 0.42201 0.53989 -0.01564 -0.21374 0.05053  336 LYS A C   
2723 O O   . LYS A 336 ? 0.67035 0.40105 0.52479 -0.01814 -0.21670 0.04973  336 LYS A O   
2724 C CB  . LYS A 336 ? 0.64809 0.38846 0.51149 -0.01795 -0.21516 0.05450  336 LYS A CB  
2725 C CG  . LYS A 336 ? 0.62843 0.37660 0.49853 -0.01704 -0.21407 0.05886  336 LYS A CG  
2726 C CD  . LYS A 336 ? 0.71326 0.45745 0.58647 -0.02051 -0.21687 0.05742  336 LYS A CD  
2727 C CE  . LYS A 336 ? 0.72807 0.47990 0.60912 -0.01990 -0.21631 0.06217  336 LYS A CE  
2728 N NZ  . LYS A 336 ? 0.69708 0.44414 0.58038 -0.02323 -0.21922 0.06019  336 LYS A NZ  
2729 N N   . ASN A 337 ? 0.63185 0.36416 0.47752 -0.01367 -0.21186 0.04846  337 ASN A N   
2730 C CA  . ASN A 337 ? 0.62744 0.35334 0.46786 -0.01406 -0.21282 0.04542  337 ASN A CA  
2731 C C   . ASN A 337 ? 0.60137 0.31731 0.43838 -0.01771 -0.21527 0.04081  337 ASN A C   
2732 O O   . ASN A 337 ? 0.58574 0.29802 0.42252 -0.01892 -0.21737 0.03989  337 ASN A O   
2733 C CB  . ASN A 337 ? 0.70566 0.43594 0.54988 -0.01275 -0.21355 0.04869  337 ASN A CB  
2734 C CG  . ASN A 337 ? 0.66025 0.38582 0.49879 -0.01197 -0.21367 0.04630  337 ASN A CG  
2735 O OD1 . ASN A 337 ? 0.79039 0.51421 0.62311 -0.01008 -0.21180 0.04447  337 ASN A OD1 
2736 N ND2 . ASN A 337 ? 0.76388 0.48729 0.60419 -0.01339 -0.21606 0.04636  337 ASN A ND2 
2737 N N   . GLY A 338 ? 0.57433 0.28629 0.40843 -0.01900 -0.21481 0.03817  338 GLY A N   
2738 C CA  . GLY A 338 ? 0.56258 0.26539 0.39295 -0.02187 -0.21669 0.03407  338 GLY A CA  
2739 C C   . GLY A 338 ? 0.63309 0.33129 0.45783 -0.02207 -0.21512 0.03103  338 GLY A C   
2740 O O   . GLY A 338 ? 0.58581 0.28795 0.40992 -0.02017 -0.21285 0.03203  338 GLY A O   
2741 N N   . ASN A 339 ? 0.61317 0.30341 0.43404 -0.02412 -0.21635 0.02766  339 ASN A N   
2742 C CA  . ASN A 339 ? 0.63037 0.31599 0.44629 -0.02454 -0.21502 0.02503  339 ASN A CA  
2743 C C   . ASN A 339 ? 0.57850 0.26143 0.39546 -0.02651 -0.21616 0.02398  339 ASN A C   
2744 O O   . ASN A 339 ? 0.60208 0.28592 0.42305 -0.02751 -0.21821 0.02492  339 ASN A O   
2745 C CB  . ASN A 339 ? 0.58697 0.26533 0.39661 -0.02476 -0.21509 0.02218  339 ASN A CB  
2746 C CG  . ASN A 339 ? 0.69051 0.37022 0.49779 -0.02270 -0.21382 0.02256  339 ASN A CG  
2747 O OD1 . ASN A 339 ? 0.74115 0.42686 0.55029 -0.02073 -0.21236 0.02459  339 ASN A OD1 
2748 N ND2 . ASN A 339 ? 0.62047 0.29456 0.42342 -0.02289 -0.21439 0.02066  339 ASN A ND2 
2749 N N   . MET A 340 ? 0.56821 0.24774 0.38161 -0.02695 -0.21502 0.02211  340 MET A N   
2750 C CA  . MET A 340 ? 0.60790 0.28472 0.42161 -0.02844 -0.21590 0.02103  340 MET A CA  
2751 C C   . MET A 340 ? 0.66044 0.33146 0.46865 -0.02872 -0.21501 0.01851  340 MET A C   
2752 O O   . MET A 340 ? 0.72314 0.39353 0.52824 -0.02813 -0.21315 0.01793  340 MET A O   
2753 C CB  . MET A 340 ? 0.60530 0.28741 0.42228 -0.02815 -0.21461 0.02261  340 MET A CB  
2754 C CG  . MET A 340 ? 0.64812 0.32776 0.46542 -0.02942 -0.21547 0.02160  340 MET A CG  
2755 S SD  . MET A 340 ? 0.69894 0.38586 0.52130 -0.02900 -0.21427 0.02405  340 MET A SD  
2756 C CE  . MET A 340 ? 0.71697 0.39888 0.53687 -0.03016 -0.21474 0.02188  340 MET A CE  
2757 N N   . LEU A 341 ? 0.63520 0.30590 0.44360 -0.02857 -0.21494 0.01800  341 LEU A N   
2758 C CA  . LEU A 341 ? 0.61342 0.28279 0.41796 -0.02770 -0.21264 0.01679  341 LEU A CA  
2759 C C   . LEU A 341 ? 0.67855 0.34887 0.48423 -0.02778 -0.21232 0.01672  341 LEU A C   
2760 O O   . LEU A 341 ? 0.67267 0.34283 0.48030 -0.02780 -0.21385 0.01672  341 LEU A O   
2761 C CB  . LEU A 341 ? 0.60994 0.27696 0.41237 -0.02706 -0.21307 0.01604  341 LEU A CB  
2762 C CG  . LEU A 341 ? 0.62039 0.28528 0.41852 -0.02613 -0.21134 0.01492  341 LEU A CG  
2763 C CD1 . LEU A 341 ? 0.64037 0.30499 0.43534 -0.02600 -0.20912 0.01469  341 LEU A CD1 
2764 C CD2 . LEU A 341 ? 0.71111 0.37330 0.50718 -0.02545 -0.21229 0.01428  341 LEU A CD2 
2765 N N   . LEU A 342 ? 0.58387 0.25496 0.38834 -0.02779 -0.21058 0.01667  342 LEU A N   
2766 C CA  A LEU A 342 ? 0.62606 0.29794 0.43139 -0.02783 -0.21032 0.01666  342 LEU A CA  
2767 C CA  B LEU A 342 ? 0.62618 0.29806 0.43150 -0.02783 -0.21032 0.01666  342 LEU A CA  
2768 C C   . LEU A 342 ? 0.68516 0.35471 0.48636 -0.02689 -0.20904 0.01559  342 LEU A C   
2769 O O   . LEU A 342 ? 0.71294 0.38111 0.51058 -0.02658 -0.20756 0.01517  342 LEU A O   
2770 C CB  A LEU A 342 ? 0.60473 0.27845 0.41095 -0.02838 -0.20949 0.01730  342 LEU A CB  
2771 C CB  B LEU A 342 ? 0.60493 0.27865 0.41116 -0.02838 -0.20949 0.01730  342 LEU A CB  
2772 C CG  A LEU A 342 ? 0.64088 0.31548 0.44806 -0.02849 -0.20931 0.01740  342 LEU A CG  
2773 C CG  B LEU A 342 ? 0.62571 0.30031 0.43288 -0.02849 -0.20930 0.01740  342 LEU A CG  
2774 C CD1 A LEU A 342 ? 0.61246 0.28798 0.42362 -0.02885 -0.21153 0.01789  342 LEU A CD1 
2775 C CD1 B LEU A 342 ? 0.60857 0.28408 0.41972 -0.02885 -0.21153 0.01789  342 LEU A CD1 
2776 C CD2 A LEU A 342 ? 0.60820 0.28433 0.41590 -0.02902 -0.20853 0.01802  342 LEU A CD2 
2777 C CD2 B LEU A 342 ? 0.61270 0.28883 0.42039 -0.02902 -0.20852 0.01802  342 LEU A CD2 
2778 N N   . ASN A 343 ? 0.70578 0.37451 0.50726 -0.02640 -0.20991 0.01520  343 ASN A N   
2779 C CA  . ASN A 343 ? 0.66548 0.33123 0.46252 -0.02527 -0.20924 0.01418  343 ASN A CA  
2780 C C   . ASN A 343 ? 0.63751 0.30376 0.43384 -0.02531 -0.20834 0.01429  343 ASN A C   
2781 O O   . ASN A 343 ? 0.66471 0.33297 0.46444 -0.02578 -0.20908 0.01481  343 ASN A O   
2782 C CB  . ASN A 343 ? 0.58693 0.25043 0.38378 -0.02429 -0.21115 0.01342  343 ASN A CB  
2783 C CG  . ASN A 343 ? 0.60846 0.26814 0.40015 -0.02279 -0.21092 0.01230  343 ASN A CG  
2784 O OD1 . ASN A 343 ? 0.72079 0.37742 0.50797 -0.02198 -0.21047 0.01164  343 ASN A OD1 
2785 N ND2 . ASN A 343 ? 0.62946 0.28891 0.42147 -0.02233 -0.21146 0.01208  343 ASN A ND2 
2786 N N   . ILE A 344 ? 0.59659 0.26087 0.38854 -0.02493 -0.20699 0.01393  344 ILE A N   
2787 C CA  . ILE A 344 ? 0.65236 0.31631 0.44283 -0.02488 -0.20642 0.01402  344 ILE A CA  
2788 C C   . ILE A 344 ? 0.61678 0.27637 0.40228 -0.02337 -0.20701 0.01298  344 ILE A C   
2789 O O   . ILE A 344 ? 0.62403 0.28076 0.40664 -0.02245 -0.20751 0.01225  344 ILE A O   
2790 C CB  . ILE A 344 ? 0.76241 0.42737 0.55189 -0.02585 -0.20488 0.01469  344 ILE A CB  
2791 C CG1 . ILE A 344 ? 0.76800 0.43053 0.55352 -0.02569 -0.20422 0.01440  344 ILE A CG1 
2792 C CG2 . ILE A 344 ? 0.63526 0.30385 0.42907 -0.02694 -0.20463 0.01555  344 ILE A CG2 
2793 C CD1 . ILE A 344 ? 0.64637 0.30972 0.43121 -0.02675 -0.20311 0.01511  344 ILE A CD1 
2794 N N   . SER A 345 ? 0.64531 0.30394 0.42939 -0.02295 -0.20716 0.01289  345 SER A N   
2795 C CA  . SER A 345 ? 0.63419 0.28812 0.41331 -0.02112 -0.20823 0.01179  345 SER A CA  
2796 C C   . SER A 345 ? 0.65795 0.30958 0.43255 -0.02104 -0.20763 0.01199  345 SER A C   
2797 O O   . SER A 345 ? 0.72293 0.37493 0.49797 -0.02109 -0.20789 0.01224  345 SER A O   
2798 C CB  . SER A 345 ? 0.64443 0.29850 0.42595 -0.02026 -0.20983 0.01128  345 SER A CB  
2799 O OG  . SER A 345 ? 0.68727 0.34398 0.47387 -0.02085 -0.21069 0.01150  345 SER A OG  
2800 N N   . PRO A 346 ? 0.65538 0.30425 0.42545 -0.02103 -0.20715 0.01200  346 PRO A N   
2801 C CA  . PRO A 346 ? 0.66585 0.31205 0.43107 -0.02090 -0.20710 0.01249  346 PRO A CA  
2802 C C   . PRO A 346 ? 0.67882 0.32134 0.43885 -0.01809 -0.20821 0.01190  346 PRO A C   
2803 O O   . PRO A 346 ? 0.72565 0.36301 0.48291 -0.01667 -0.21023 0.01016  346 PRO A O   
2804 C CB  . PRO A 346 ? 0.57750 0.22322 0.34005 -0.02130 -0.20608 0.01307  346 PRO A CB  
2805 C CG  . PRO A 346 ? 0.54088 0.18823 0.30716 -0.02231 -0.20597 0.01270  346 PRO A CG  
2806 C CD  . PRO A 346 ? 0.69577 0.34422 0.46514 -0.02127 -0.20677 0.01192  346 PRO A CD  
2807 N N   . THR A 347 ? 0.72113 0.36616 0.47946 -0.01709 -0.20698 0.01346  347 THR A N   
2808 C CA  . THR A 347 ? 0.70556 0.34763 0.45828 -0.01387 -0.20771 0.01324  347 THR A CA  
2809 C C   . THR A 347 ? 0.80461 0.44334 0.55082 -0.01181 -0.20762 0.01319  347 THR A C   
2810 O O   . THR A 347 ? 0.75903 0.39891 0.50556 -0.01322 -0.20659 0.01391  347 THR A O   
2811 C CB  . THR A 347 ? 0.69808 0.34478 0.45112 -0.01336 -0.20606 0.01548  347 THR A CB  
2812 O OG1 . THR A 347 ? 0.86860 0.51878 0.62149 -0.01449 -0.20410 0.01764  347 THR A OG1 
2813 C CG2 . THR A 347 ? 0.80413 0.45449 0.56352 -0.01518 -0.20607 0.01569  347 THR A CG2 
2814 N N   . ALA A 348 ? 0.82569 0.46049 0.56588 -0.00831 -0.20867 0.01248  348 ALA A N   
2815 C CA  . ALA A 348 ? 0.86755 0.49902 0.60088 -0.00573 -0.20867 0.01242  348 ALA A CA  
2816 C C   . ALA A 348 ? 0.74761 0.38376 0.47952 -0.00598 -0.20598 0.01549  348 ALA A C   
2817 O O   . ALA A 348 ? 0.86386 0.49874 0.59241 -0.00539 -0.20558 0.01587  348 ALA A O   
2818 C CB  . ALA A 348 ? 0.79725 0.42400 0.52389 -0.00137 -0.21022 0.01126  348 ALA A CB  
2819 N N   . VAL A 349 ? 0.79368 0.43525 0.52855 -0.00704 -0.20431 0.01781  349 VAL A N   
2820 C CA  . VAL A 349 ? 0.84846 0.49477 0.58280 -0.00758 -0.20207 0.02124  349 VAL A CA  
2821 C C   . VAL A 349 ? 0.85577 0.50466 0.59581 -0.01172 -0.20161 0.02162  349 VAL A C   
2822 O O   . VAL A 349 ? 0.78444 0.43687 0.52491 -0.01273 -0.20028 0.02435  349 VAL A O   
2823 C CB  . VAL A 349 ? 0.75302 0.40366 0.48763 -0.00646 -0.20079 0.02379  349 VAL A CB  
2824 C CG1 . VAL A 349 ? 0.71927 0.36744 0.44705 -0.00172 -0.20100 0.02383  349 VAL A CG1 
2825 C CG2 . VAL A 349 ? 0.72252 0.37579 0.46383 -0.00898 -0.20111 0.02321  349 VAL A CG2 
2826 N N   . GLY A 350 ? 0.82299 0.47014 0.56719 -0.01386 -0.20280 0.01917  350 GLY A N   
2827 C CA  . GLY A 350 ? 0.88593 0.53484 0.63465 -0.01715 -0.20249 0.01926  350 GLY A CA  
2828 C C   . GLY A 350 ? 0.83698 0.49037 0.59165 -0.01963 -0.20189 0.02019  350 GLY A C   
2829 O O   . GLY A 350 ? 0.71785 0.37320 0.47512 -0.02192 -0.20146 0.02107  350 GLY A O   
2830 N N   . VAL A 351 ? 0.78962 0.44431 0.54635 -0.01910 -0.20209 0.01990  351 VAL A N   
2831 C CA  . VAL A 351 ? 0.72834 0.38755 0.49076 -0.02117 -0.20153 0.02084  351 VAL A CA  
2832 C C   . VAL A 351 ? 0.79864 0.45738 0.56558 -0.02227 -0.20240 0.01881  351 VAL A C   
2833 O O   . VAL A 351 ? 0.77674 0.43248 0.54250 -0.02085 -0.20358 0.01722  351 VAL A O   
2834 C CB  . VAL A 351 ? 0.75478 0.41698 0.51671 -0.01982 -0.20085 0.02271  351 VAL A CB  
2835 C CG1 . VAL A 351 ? 0.80443 0.47092 0.57224 -0.02166 -0.20051 0.02337  351 VAL A CG1 
2836 C CG2 . VAL A 351 ? 0.81425 0.47808 0.57253 -0.01886 -0.19979 0.02553  351 VAL A CG2 
2837 N N   . LEU A 352 ? 0.82661 0.48809 0.59832 -0.02455 -0.20199 0.01901  352 LEU A N   
2838 C CA  . LEU A 352 ? 0.79439 0.45670 0.57080 -0.02541 -0.20249 0.01776  352 LEU A CA  
2839 C C   . LEU A 352 ? 0.76077 0.42704 0.54055 -0.02542 -0.20209 0.01877  352 LEU A C   
2840 O O   . LEU A 352 ? 0.71240 0.38220 0.49394 -0.02639 -0.20115 0.02037  352 LEU A O   
2841 C CB  . LEU A 352 ? 0.70201 0.36418 0.48070 -0.02735 -0.20269 0.01743  352 LEU A CB  
2842 C CG  . LEU A 352 ? 0.89272 0.55475 0.67449 -0.02753 -0.20348 0.01633  352 LEU A CG  
2843 C CD1 . LEU A 352 ? 0.76476 0.42397 0.54414 -0.02594 -0.20416 0.01518  352 LEU A CD1 
2844 C CD2 . LEU A 352 ? 0.82455 0.48858 0.60823 -0.02843 -0.20269 0.01671  352 LEU A CD2 
2845 N N   . PRO A 353 ? 0.80598 0.47149 0.58652 -0.02435 -0.20303 0.01795  353 PRO A N   
2846 C CA  . PRO A 353 ? 0.67766 0.34682 0.46123 -0.02412 -0.20277 0.01894  353 PRO A CA  
2847 C C   . PRO A 353 ? 0.72302 0.39711 0.51216 -0.02584 -0.20181 0.01987  353 PRO A C   
2848 O O   . PRO A 353 ? 0.69662 0.37002 0.48746 -0.02704 -0.20222 0.01919  353 PRO A O   
2849 C CB  . PRO A 353 ? 0.74830 0.41433 0.53146 -0.02286 -0.20459 0.01742  353 PRO A CB  
2850 C CG  . PRO A 353 ? 0.74098 0.40122 0.51885 -0.02168 -0.20568 0.01594  353 PRO A CG  
2851 C CD  . PRO A 353 ? 0.63731 0.29799 0.41580 -0.02323 -0.20481 0.01600  353 PRO A CD  
2852 N N   . ASP A 354 ? 0.77695 0.45506 0.56830 -0.02584 -0.20108 0.02138  354 ASP A N   
2853 C CA  . ASP A 354 ? 0.80364 0.48658 0.59975 -0.02713 -0.20014 0.02246  354 ASP A CA  
2854 C C   . ASP A 354 ? 0.69175 0.37514 0.49145 -0.02762 -0.20102 0.02176  354 ASP A C   
2855 O O   . ASP A 354 ? 0.72974 0.41471 0.53161 -0.02861 -0.20087 0.02212  354 ASP A O   
2856 C CB  . ASP A 354 ? 0.85368 0.54042 0.65106 -0.02688 -0.19948 0.02430  354 ASP A CB  
2857 C CG  . ASP A 354 ? 0.99538 0.68208 0.78993 -0.02712 -0.19909 0.02568  354 ASP A CG  
2858 O OD1 . ASP A 354 ? 0.80937 0.49307 0.60091 -0.02754 -0.19929 0.02522  354 ASP A OD1 
2859 O OD2 . ASP A 354 ? 1.02322 0.71308 0.81873 -0.02685 -0.19868 0.02741  354 ASP A OD2 
2860 N N   . GLU A 355 ? 0.65250 0.33440 0.45265 -0.02685 -0.20217 0.02090  355 GLU A N   
2861 C CA  . GLU A 355 ? 0.65363 0.33677 0.45780 -0.02742 -0.20320 0.02080  355 GLU A CA  
2862 C C   . GLU A 355 ? 0.70834 0.38837 0.51165 -0.02826 -0.20406 0.01975  355 GLU A C   
2863 O O   . GLU A 355 ? 0.79329 0.47569 0.59973 -0.02884 -0.20415 0.02031  355 GLU A O   
2864 C CB  . GLU A 355 ? 0.77065 0.45325 0.57609 -0.02655 -0.20455 0.02040  355 GLU A CB  
2865 C CG  . GLU A 355 ? 0.82486 0.50992 0.63032 -0.02533 -0.20370 0.02132  355 GLU A CG  
2866 C CD  . GLU A 355 ? 0.94845 0.63101 0.75412 -0.02440 -0.20587 0.02053  355 GLU A CD  
2867 O OE1 . GLU A 355 ? 0.98002 0.66442 0.79003 -0.02495 -0.20686 0.02076  355 GLU A OE1 
2868 O OE2 . GLU A 355 ? 0.94966 0.62832 0.75104 -0.02302 -0.20680 0.01979  355 GLU A OE2 
2869 N N   . GLN A 356 ? 0.67451 0.34973 0.47363 -0.02805 -0.20461 0.01845  356 GLN A N   
2870 C CA  . GLN A 356 ? 0.69384 0.36693 0.49213 -0.02858 -0.20497 0.01772  356 GLN A CA  
2871 C C   . GLN A 356 ? 0.69125 0.36534 0.48938 -0.02952 -0.20400 0.01831  356 GLN A C   
2872 O O   . GLN A 356 ? 0.67642 0.35172 0.47618 -0.02975 -0.20388 0.01842  356 GLN A O   
2873 C CB  . GLN A 356 ? 0.70634 0.37606 0.50052 -0.02749 -0.20496 0.01672  356 GLN A CB  
2874 C CG  . GLN A 356 ? 0.64922 0.31685 0.44236 -0.02619 -0.20618 0.01590  356 GLN A CG  
2875 C CD  . GLN A 356 ? 0.68890 0.35299 0.47820 -0.02488 -0.20652 0.01479  356 GLN A CD  
2876 O OE1 . GLN A 356 ? 0.71910 0.38330 0.50833 -0.02506 -0.20608 0.01469  356 GLN A OE1 
2877 N NE2 . GLN A 356 ? 0.72002 0.38052 0.50572 -0.02338 -0.20749 0.01390  356 GLN A NE2 
2878 N N   . LEU A 357 ? 0.74592 0.42121 0.54273 -0.02958 -0.20285 0.01910  357 LEU A N   
2879 C CA  . LEU A 357 ? 0.78170 0.45830 0.57873 -0.03041 -0.20209 0.01982  357 LEU A CA  
2880 C C   . LEU A 357 ? 0.68346 0.36411 0.48457 -0.03049 -0.20185 0.02065  357 LEU A C   
2881 O O   . LEU A 357 ? 0.64373 0.32411 0.44503 -0.03077 -0.20196 0.02053  357 LEU A O   
2882 C CB  . LEU A 357 ? 0.72727 0.40521 0.52280 -0.03045 -0.20111 0.02090  357 LEU A CB  
2883 C CG  . LEU A 357 ? 0.78394 0.45866 0.57509 -0.03014 -0.20107 0.02057  357 LEU A CG  
2884 C CD1 . LEU A 357 ? 0.68234 0.35995 0.47289 -0.03005 -0.19998 0.02230  357 LEU A CD1 
2885 C CD2 . LEU A 357 ? 0.62294 0.29413 0.41207 -0.03096 -0.20167 0.01974  357 LEU A CD2 
2886 N N   . LYS A 358 ? 0.67276 0.35703 0.47687 -0.02996 -0.20162 0.02147  358 LYS A N   
2887 C CA  . LYS A 358 ? 0.72233 0.41111 0.53030 -0.02969 -0.20128 0.02256  358 LYS A CA  
2888 C C   . LYS A 358 ? 0.70243 0.39093 0.51177 -0.02950 -0.20210 0.02219  358 LYS A C   
2889 O O   . LYS A 358 ? 0.75897 0.44965 0.56948 -0.02914 -0.20175 0.02277  358 LYS A O   
2890 C CB  . LYS A 358 ? 0.76631 0.45923 0.57722 -0.02912 -0.20084 0.02375  358 LYS A CB  
2891 C CG  . LYS A 358 ? 0.88066 0.57897 0.69551 -0.02856 -0.20031 0.02524  358 LYS A CG  
2892 C CD  . LYS A 358 ? 0.97326 0.67296 0.78768 -0.02853 -0.19964 0.02572  358 LYS A CD  
2893 C CE  . LYS A 358 ? 0.90697 0.61251 0.72468 -0.02761 -0.19886 0.02742  358 LYS A CE  
2894 N NZ  . LYS A 358 ? 0.99301 0.70201 0.81406 -0.02674 -0.19897 0.02836  358 LYS A NZ  
2895 N N   . VAL A 359 ? 0.67121 0.35714 0.48025 -0.02958 -0.20325 0.02133  359 VAL A N   
2896 C CA  . VAL A 359 ? 0.65383 0.33995 0.46458 -0.02949 -0.20419 0.02128  359 VAL A CA  
2897 C C   . VAL A 359 ? 0.72043 0.40419 0.52859 -0.02960 -0.20398 0.02061  359 VAL A C   
2898 O O   . VAL A 359 ? 0.65020 0.33659 0.46001 -0.02901 -0.20378 0.02135  359 VAL A O   
2899 C CB  . VAL A 359 ? 0.67937 0.36232 0.49000 -0.02972 -0.20594 0.02031  359 VAL A CB  
2900 C CG1 . VAL A 359 ? 0.56546 0.24843 0.37760 -0.02978 -0.20700 0.02039  359 VAL A CG1 
2901 C CG2 . VAL A 359 ? 0.67367 0.35870 0.48712 -0.02949 -0.20656 0.02093  359 VAL A CG2 
2902 N N   . LEU A 360 ? 0.71291 0.39203 0.51705 -0.03012 -0.20405 0.01940  360 LEU A N   
2903 C CA  . LEU A 360 ? 0.57016 0.24711 0.37197 -0.03016 -0.20389 0.01883  360 LEU A CA  
2904 C C   . LEU A 360 ? 0.69574 0.37492 0.49813 -0.02991 -0.20321 0.01957  360 LEU A C   
2905 O O   . LEU A 360 ? 0.69233 0.37140 0.49436 -0.02935 -0.20333 0.01945  360 LEU A O   
2906 C CB  . LEU A 360 ? 0.68917 0.36431 0.48774 -0.03006 -0.20288 0.01835  360 LEU A CB  
2907 C CG  . LEU A 360 ? 0.66758 0.34141 0.46499 -0.02942 -0.20296 0.01769  360 LEU A CG  
2908 C CD1 . LEU A 360 ? 0.65701 0.32843 0.45052 -0.02933 -0.20228 0.01734  360 LEU A CD1 
2909 C CD2 . LEU A 360 ? 0.59663 0.27045 0.39495 -0.02903 -0.20347 0.01740  360 LEU A CD2 
2910 N N   . GLN A 361 ? 0.72505 0.40681 0.52844 -0.02999 -0.20243 0.02043  361 GLN A N   
2911 C CA  . GLN A 361 ? 0.67838 0.36221 0.48215 -0.02957 -0.20194 0.02110  361 GLN A CA  
2912 C C   . GLN A 361 ? 0.73276 0.42149 0.53959 -0.02814 -0.20157 0.02216  361 GLN A C   
2913 O O   . GLN A 361 ? 0.72748 0.41695 0.53375 -0.02718 -0.20150 0.02228  361 GLN A O   
2914 C CB  . GLN A 361 ? 0.66759 0.35293 0.47167 -0.03010 -0.20140 0.02189  361 GLN A CB  
2915 C CG  . GLN A 361 ? 0.76231 0.44810 0.56596 -0.02996 -0.20147 0.02224  361 GLN A CG  
2916 C CD  . GLN A 361 ? 0.90933 0.59018 0.70978 -0.03050 -0.20232 0.02114  361 GLN A CD  
2917 O OE1 . GLN A 361 ? 0.82540 0.50304 0.62374 -0.03168 -0.20264 0.02076  361 GLN A OE1 
2918 N NE2 . GLN A 361 ? 0.76691 0.44740 0.56688 -0.02940 -0.20270 0.02075  361 GLN A NE2 
2919 N N   . ASP A 362 ? 0.72637 0.41832 0.53621 -0.02784 -0.20147 0.02298  362 ASP A N   
2920 C CA  . ASP A 362 ? 0.68075 0.37821 0.49381 -0.02633 -0.20107 0.02448  362 ASP A CA  
2921 C C   . ASP A 362 ? 0.64871 0.34516 0.46097 -0.02562 -0.20156 0.02414  362 ASP A C   
2922 O O   . ASP A 362 ? 0.75142 0.45102 0.56403 -0.02394 -0.20106 0.02498  362 ASP A O   
2923 C CB  . ASP A 362 ? 0.67555 0.37691 0.49245 -0.02630 -0.20102 0.02578  362 ASP A CB  
2924 C CG  . ASP A 362 ? 0.69942 0.40278 0.51736 -0.02654 -0.20037 0.02642  362 ASP A CG  
2925 O OD1 . ASP A 362 ? 0.89109 0.59530 0.70803 -0.02625 -0.19972 0.02661  362 ASP A OD1 
2926 O OD2 . ASP A 362 ? 0.69721 0.40118 0.51695 -0.02696 -0.20069 0.02672  362 ASP A OD2 
2927 N N   . ILE A 363 ? 0.64219 0.33459 0.45324 -0.02661 -0.20251 0.02301  363 ILE A N   
2928 C CA  . ILE A 363 ? 0.66724 0.35840 0.47734 -0.02601 -0.20305 0.02266  363 ILE A CA  
2929 C C   . ILE A 363 ? 0.66109 0.34990 0.46780 -0.02532 -0.20279 0.02183  363 ILE A C   
2930 O O   . ILE A 363 ? 0.61833 0.30899 0.42488 -0.02370 -0.20265 0.02229  363 ILE A O   
2931 C CB  . ILE A 363 ? 0.63049 0.31691 0.43933 -0.02730 -0.20431 0.02136  363 ILE A CB  
2932 C CG1 . ILE A 363 ? 0.67503 0.36363 0.48746 -0.02774 -0.20508 0.02217  363 ILE A CG1 
2933 C CG2 . ILE A 363 ? 0.56972 0.25443 0.37716 -0.02675 -0.20488 0.02091  363 ILE A CG2 
2934 C CD1 . ILE A 363 ? 0.57955 0.26315 0.39049 -0.02880 -0.20665 0.02074  363 ILE A CD1 
2935 N N   . GLY A 364 ? 0.73931 0.42420 0.54333 -0.02641 -0.20283 0.02076  364 GLY A N   
2936 C CA  . GLY A 364 ? 0.69235 0.37438 0.49332 -0.02599 -0.20301 0.01996  364 GLY A CA  
2937 C C   . GLY A 364 ? 0.70142 0.38741 0.50319 -0.02417 -0.20247 0.02087  364 GLY A C   
2938 O O   . GLY A 364 ? 0.70655 0.39156 0.50632 -0.02276 -0.20277 0.02043  364 GLY A O   
2939 N N   . ASP A 365 ? 0.68235 0.37279 0.48678 -0.02396 -0.20176 0.02211  365 ASP A N   
2940 C CA  . ASP A 365 ? 0.68779 0.38281 0.49308 -0.02185 -0.20123 0.02316  365 ASP A CA  
2941 C C   . ASP A 365 ? 0.65818 0.35710 0.46426 -0.01945 -0.20086 0.02408  365 ASP A C   
2942 O O   . ASP A 365 ? 0.87640 0.57563 0.68040 -0.01737 -0.20096 0.02387  365 ASP A O   
2943 C CB  . ASP A 365 ? 0.62206 0.32181 0.43047 -0.02198 -0.20046 0.02458  365 ASP A CB  
2944 C CG  . ASP A 365 ? 0.75014 0.44719 0.55777 -0.02381 -0.20071 0.02407  365 ASP A CG  
2945 O OD1 . ASP A 365 ? 0.77273 0.46460 0.57751 -0.02489 -0.20151 0.02283  365 ASP A OD1 
2946 O OD2 . ASP A 365 ? 0.64103 0.34148 0.45109 -0.02412 -0.20012 0.02514  365 ASP A OD2 
2947 N N   . PHE A 366 ? 0.67340 0.37527 0.48237 -0.01957 -0.20058 0.02518  366 PHE A N   
2948 C CA  . PHE A 366 ? 0.68153 0.38832 0.49198 -0.01721 -0.20014 0.02675  366 PHE A CA  
2949 C C   . PHE A 366 ? 0.69043 0.39338 0.49742 -0.01641 -0.20075 0.02545  366 PHE A C   
2950 O O   . PHE A 366 ? 0.66713 0.37340 0.47332 -0.01358 -0.20030 0.02628  366 PHE A O   
2951 C CB  . PHE A 366 ? 0.54158 0.25190 0.35630 -0.01782 -0.20013 0.02841  366 PHE A CB  
2952 C CG  . PHE A 366 ? 0.62876 0.34484 0.44566 -0.01543 -0.19967 0.03066  366 PHE A CG  
2953 C CD1 . PHE A 366 ? 0.58767 0.31174 0.40761 -0.01301 -0.19845 0.03353  366 PHE A CD1 
2954 C CD2 . PHE A 366 ? 0.61057 0.32453 0.42659 -0.01543 -0.20036 0.03024  366 PHE A CD2 
2955 C CE1 . PHE A 366 ? 0.63712 0.36720 0.45926 -0.01053 -0.19781 0.03617  366 PHE A CE1 
2956 C CE2 . PHE A 366 ? 0.64465 0.36453 0.46297 -0.01308 -0.19984 0.03274  366 PHE A CE2 
2957 C CZ  . PHE A 366 ? 0.65745 0.38551 0.47888 -0.01058 -0.19850 0.03584  366 PHE A CZ  
2958 N N   . LEU A 367 ? 0.66493 0.36129 0.46976 -0.01856 -0.20171 0.02356  367 LEU A N   
2959 C CA  . LEU A 367 ? 0.66717 0.36020 0.46901 -0.01771 -0.20231 0.02252  367 LEU A CA  
2960 C C   . LEU A 367 ? 0.70063 0.39052 0.49854 -0.01646 -0.20264 0.02124  367 LEU A C   
2961 O O   . LEU A 367 ? 0.64411 0.33478 0.44024 -0.01407 -0.20269 0.02125  367 LEU A O   
2962 C CB  . LEU A 367 ? 0.66669 0.35418 0.46752 -0.02012 -0.20326 0.02114  367 LEU A CB  
2963 C CG  . LEU A 367 ? 0.62206 0.31199 0.42627 -0.02083 -0.20353 0.02219  367 LEU A CG  
2964 C CD1 . LEU A 367 ? 0.57072 0.25443 0.37306 -0.02303 -0.20464 0.02048  367 LEU A CD1 
2965 C CD2 . LEU A 367 ? 0.61263 0.30714 0.41829 -0.01857 -0.20331 0.02378  367 LEU A CD2 
2966 N N   . GLY A 368 ? 0.67571 0.36256 0.47255 -0.01788 -0.20297 0.02037  368 GLY A N   
2967 C CA  . GLY A 368 ? 0.72654 0.41017 0.52012 -0.01690 -0.20373 0.01927  368 GLY A CA  
2968 C C   . GLY A 368 ? 0.78278 0.47172 0.57639 -0.01348 -0.20323 0.02024  368 GLY A C   
2969 O O   . GLY A 368 ? 0.78814 0.47463 0.57848 -0.01164 -0.20408 0.01920  368 GLY A O   
2970 N N   . ARG A 369 ? 0.68098 0.37703 0.47804 -0.01244 -0.20198 0.02223  369 ARG A N   
2971 C CA  . ARG A 369 ? 0.66168 0.36402 0.45886 -0.00880 -0.20126 0.02358  369 ARG A CA  
2972 C C   . ARG A 369 ? 0.74657 0.45333 0.54394 -0.00595 -0.20054 0.02491  369 ARG A C   
2973 O O   . ARG A 369 ? 0.71569 0.42496 0.51075 -0.00240 -0.20042 0.02514  369 ARG A O   
2974 C CB  . ARG A 369 ? 0.58157 0.28980 0.38252 -0.00903 -0.20022 0.02543  369 ARG A CB  
2975 C CG  . ARG A 369 ? 0.73803 0.45378 0.53960 -0.00532 -0.19927 0.02727  369 ARG A CG  
2976 C CD  . ARG A 369 ? 0.66484 0.38526 0.47015 -0.00620 -0.19843 0.02891  369 ARG A CD  
2977 N NE  . ARG A 369 ? 0.67290 0.40149 0.47921 -0.00252 -0.19731 0.03117  369 ARG A NE  
2978 C CZ  . ARG A 369 ? 0.68599 0.42001 0.49551 -0.00238 -0.19640 0.03306  369 ARG A CZ  
2979 N NH1 . ARG A 369 ? 0.69803 0.42987 0.50982 -0.00566 -0.19658 0.03272  369 ARG A NH1 
2980 N NH2 . ARG A 369 ? 0.79381 0.53571 0.60415 0.00129  -0.19526 0.03543  369 ARG A NH2 
2981 N N   . TYR A 370 ? 0.62484 0.33271 0.42482 -0.00726 -0.20018 0.02586  370 TYR A N   
2982 C CA  . TYR A 370 ? 0.62930 0.34283 0.43022 -0.00427 -0.19938 0.02787  370 TYR A CA  
2983 C C   . TYR A 370 ? 0.59685 0.30608 0.39640 -0.00515 -0.20016 0.02685  370 TYR A C   
2984 O O   . TYR A 370 ? 0.65915 0.37328 0.46091 -0.00365 -0.19955 0.02895  370 TYR A O   
2985 C CB  . TYR A 370 ? 0.58685 0.30859 0.39319 -0.00383 -0.19812 0.03117  370 TYR A CB  
2986 C CG  . TYR A 370 ? 0.70179 0.42876 0.51000 -0.00279 -0.19720 0.03266  370 TYR A CG  
2987 C CD1 . TYR A 370 ? 0.78023 0.51372 0.58768 0.00142  -0.19615 0.03448  370 TYR A CD1 
2988 C CD2 . TYR A 370 ? 0.65701 0.38319 0.46791 -0.00569 -0.19730 0.03258  370 TYR A CD2 
2989 C CE1 . TYR A 370 ? 0.73982 0.47853 0.54898 0.00257  -0.19529 0.03602  370 TYR A CE1 
2990 C CE2 . TYR A 370 ? 0.69393 0.42526 0.50675 -0.00465 -0.19642 0.03414  370 TYR A CE2 
2991 C CZ  . TYR A 370 ? 0.72764 0.46526 0.53965 -0.00057 -0.19542 0.03587  370 TYR A CZ  
2992 O OH  . TYR A 370 ? 0.69926 0.44224 0.51298 0.00070  -0.19456 0.03751  370 TYR A OH  
2993 N N   . GLY A 371 ? 0.61293 0.31380 0.40917 -0.00731 -0.20143 0.02406  371 GLY A N   
2994 C CA  . GLY A 371 ? 0.58951 0.28591 0.38410 -0.00815 -0.20224 0.02296  371 GLY A CA  
2995 C C   . GLY A 371 ? 0.59165 0.29165 0.38519 -0.00463 -0.20184 0.02408  371 GLY A C   
2996 O O   . GLY A 371 ? 0.68956 0.38972 0.48418 -0.00506 -0.20203 0.02464  371 GLY A O   
2997 N N   . GLU A 372 ? 0.66595 0.36874 0.45725 -0.00107 -0.20141 0.02440  372 GLU A N   
2998 C CA  . GLU A 372 ? 0.72550 0.43231 0.51527 0.00303  -0.20088 0.02565  372 GLU A CA  
2999 C C   . GLU A 372 ? 0.64779 0.36258 0.44254 0.00377  -0.19965 0.02919  372 GLU A C   
3000 O O   . GLU A 372 ? 0.65522 0.37172 0.44967 0.00554  -0.19951 0.03020  372 GLU A O   
3001 C CB  . GLU A 372 ? 0.68172 0.39184 0.46894 0.00698  -0.20044 0.02588  372 GLU A CB  
3002 C CG  . GLU A 372 ? 0.80622 0.52252 0.59207 0.01205  -0.19949 0.02784  372 GLU A CG  
3003 C CD  . GLU A 372 ? 0.85659 0.57721 0.64010 0.01623  -0.19899 0.02834  372 GLU A CD  
3004 O OE1 . GLU A 372 ? 0.67453 0.39331 0.45781 0.01495  -0.19948 0.02716  372 GLU A OE1 
3005 O OE2 . GLU A 372 ? 0.87710 0.60309 0.65894 0.02092  -0.19815 0.03000  372 GLU A OE2 
3006 N N   . SER A 373 ? 0.58817 0.30749 0.38760 0.00233  -0.19894 0.03112  373 SER A N   
3007 C CA  . SER A 373 ? 0.70329 0.43071 0.50834 0.00304  -0.19793 0.03503  373 SER A CA  
3008 C C   . SER A 373 ? 0.76333 0.48713 0.57081 -0.00052 -0.19911 0.03456  373 SER A C   
3009 O O   . SER A 373 ? 0.77514 0.50429 0.58646 0.00035  -0.19878 0.03750  373 SER A O   
3010 C CB  . SER A 373 ? 0.55217 0.28554 0.36122 0.00304  -0.19691 0.03730  373 SER A CB  
3011 O OG  . SER A 373 ? 0.77358 0.50164 0.58339 -0.00106 -0.19783 0.03520  373 SER A OG  
3012 N N   . VAL A 374 ? 0.70947 0.42480 0.51488 -0.00418 -0.20046 0.03124  374 VAL A N   
3013 C CA  . VAL A 374 ? 0.67035 0.38180 0.47761 -0.00755 -0.20177 0.03050  374 VAL A CA  
3014 C C   . VAL A 374 ? 0.65947 0.36447 0.46253 -0.00785 -0.20278 0.02820  374 VAL A C   
3015 O O   . VAL A 374 ? 0.75684 0.46381 0.56135 -0.00719 -0.20309 0.02951  374 VAL A O   
3016 C CB  . VAL A 374 ? 0.59622 0.30328 0.40408 -0.01108 -0.20242 0.02877  374 VAL A CB  
3017 C CG1 . VAL A 374 ? 0.71576 0.41745 0.52402 -0.01427 -0.20396 0.02732  374 VAL A CG1 
3018 C CG2 . VAL A 374 ? 0.62893 0.34235 0.44122 -0.01087 -0.20154 0.03113  374 VAL A CG2 
3019 N N   . PHE A 375 ? 0.64823 0.34627 0.44651 -0.00858 -0.20329 0.02523  375 PHE A N   
3020 C CA  . PHE A 375 ? 0.58986 0.28100 0.38415 -0.00926 -0.20438 0.02297  375 PHE A CA  
3021 C C   . PHE A 375 ? 0.61521 0.30875 0.40754 -0.00569 -0.20406 0.02377  375 PHE A C   
3022 O O   . PHE A 375 ? 0.70821 0.40594 0.49967 -0.00246 -0.20312 0.02477  375 PHE A O   
3023 C CB  . PHE A 375 ? 0.58528 0.26881 0.37556 -0.01096 -0.20504 0.02013  375 PHE A CB  
3024 C CG  . PHE A 375 ? 0.60300 0.28427 0.39476 -0.01412 -0.20521 0.01948  375 PHE A CG  
3025 C CD1 . PHE A 375 ? 0.59796 0.27652 0.39092 -0.01682 -0.20594 0.01900  375 PHE A CD1 
3026 C CD2 . PHE A 375 ? 0.56851 0.25025 0.36015 -0.01417 -0.20474 0.01931  375 PHE A CD2 
3027 C CE1 . PHE A 375 ? 0.69262 0.36922 0.48649 -0.01927 -0.20605 0.01843  375 PHE A CE1 
3028 C CE2 . PHE A 375 ? 0.63811 0.31813 0.43105 -0.01684 -0.20481 0.01889  375 PHE A CE2 
3029 C CZ  . PHE A 375 ? 0.66395 0.34146 0.45790 -0.01928 -0.20539 0.01846  375 PHE A CZ  
3030 N N   . SER A 376 ? 0.67298 0.36399 0.46447 -0.00609 -0.20487 0.02336  376 SER A N   
3031 C CA  . SER A 376 ? 0.70539 0.39833 0.49485 -0.00269 -0.20465 0.02410  376 SER A CA  
3032 C C   . SER A 376 ? 0.68690 0.39012 0.48033 0.00057  -0.20323 0.02805  376 SER A C   
3033 O O   . SER A 376 ? 0.73454 0.44084 0.52624 0.00424  -0.20262 0.02916  376 SER A O   
3034 C CB  . SER A 376 ? 0.57809 0.26602 0.36190 -0.00093 -0.20497 0.02176  376 SER A CB  
3035 O OG  . SER A 376 ? 0.64580 0.32469 0.42660 -0.00399 -0.20632 0.01881  376 SER A OG  
3036 N N   . THR A 377 ? 0.61432 0.32271 0.41298 -0.00065 -0.20275 0.03029  377 THR A N   
3037 C CA  . THR A 377 ? 0.65401 0.37260 0.45739 0.00217  -0.20141 0.03472  377 THR A CA  
3038 C C   . THR A 377 ? 0.67915 0.39968 0.48707 0.00060  -0.20227 0.03667  377 THR A C   
3039 O O   . THR A 377 ? 0.64355 0.35776 0.45127 -0.00298 -0.20393 0.03445  377 THR A O   
3040 C CB  . THR A 377 ? 0.66870 0.39257 0.47555 0.00218  -0.20037 0.03654  377 THR A CB  
3041 O OG1 . THR A 377 ? 0.69352 0.41426 0.50339 -0.00212 -0.20149 0.03564  377 THR A OG1 
3042 C CG2 . THR A 377 ? 0.61704 0.33870 0.41948 0.00356  -0.19982 0.03450  377 THR A CG2 
3043 N N   . ARG A 378 ? 0.67437 0.40393 0.48644 0.00354  -0.20116 0.04109  378 ARG A N   
3044 C CA  . ARG A 378 ? 0.59310 0.32572 0.41049 0.00239  -0.20206 0.04371  378 ARG A CA  
3045 C C   . ARG A 378 ? 0.69645 0.43785 0.52097 0.00289  -0.20121 0.04824  378 ARG A C   
3046 O O   . ARG A 378 ? 0.75689 0.50379 0.58198 0.00536  -0.19940 0.05014  378 ARG A O   
3047 C CB  . ARG A 378 ? 0.60618 0.34178 0.42279 0.00555  -0.20165 0.04559  378 ARG A CB  
3048 C CG  . ARG A 378 ? 0.63437 0.36109 0.44475 0.00471  -0.20285 0.04143  378 ARG A CG  
3049 C CD  . ARG A 378 ? 0.65084 0.37009 0.46168 -0.00007 -0.20518 0.03873  378 ARG A CD  
3050 N NE  . ARG A 378 ? 0.69237 0.40330 0.49733 -0.00077 -0.20619 0.03506  378 ARG A NE  
3051 C CZ  . ARG A 378 ? 0.70167 0.40485 0.50139 -0.00216 -0.20650 0.03115  378 ARG A CZ  
3052 N NH1 . ARG A 378 ? 0.64804 0.35052 0.44744 -0.00303 -0.20593 0.03019  378 ARG A NH1 
3053 N NH2 . ARG A 378 ? 0.70581 0.40197 0.50077 -0.00264 -0.20744 0.02841  378 ARG A NH2 
3054 N N   . ALA A 379 ? 0.75042 0.49297 0.58049 0.00056  -0.20271 0.05002  379 ALA A N   
3055 C CA  . ALA A 379 ? 0.66296 0.41358 0.50060 0.00084  -0.20224 0.05467  379 ALA A CA  
3056 C C   . ALA A 379 ? 0.70175 0.46302 0.54251 0.00586  -0.19995 0.06032  379 ALA A C   
3057 O O   . ALA A 379 ? 0.93935 0.70184 0.77902 0.00794  -0.19976 0.06136  379 ALA A O   
3058 C CB  . ALA A 379 ? 0.54958 0.29781 0.39236 -0.00308 -0.20498 0.05488  379 ALA A CB  
3059 N N   . TRP A 380 ? 0.72553 0.49489 0.57041 0.00804  -0.19811 0.06437  380 TRP A N   
3060 C CA  . TRP A 380 ? 0.70483 0.48541 0.55336 0.01327  -0.19561 0.07068  380 TRP A CA  
3061 C C   . TRP A 380 ? 0.73921 0.52400 0.59605 0.01205  -0.19679 0.07499  380 TRP A C   
3062 O O   . TRP A 380 ? 0.75723 0.53557 0.61598 0.00725  -0.19976 0.07242  380 TRP A O   
3063 C CB  . TRP A 380 ? 0.77495 0.56273 0.62464 0.01635  -0.19308 0.07364  380 TRP A CB  
3064 C CG  . TRP A 380 ? 0.80075 0.59950 0.65132 0.02292  -0.18987 0.07934  380 TRP A CG  
3065 C CD1 . TRP A 380 ? 0.89174 0.69284 0.73886 0.02693  -0.18872 0.08035  380 TRP A CD1 
3066 C CD2 . TRP A 380 ? 0.88948 0.69864 0.74453 0.02663  -0.18723 0.08508  380 TRP A CD2 
3067 N NE1 . TRP A 380 ? 0.83379 0.64628 0.68287 0.03302  -0.18553 0.08642  380 TRP A NE1 
3068 C CE2 . TRP A 380 ? 0.86532 0.68302 0.71922 0.03304  -0.18447 0.08950  380 TRP A CE2 
3069 C CE3 . TRP A 380 ? 0.75012 0.56229 0.60993 0.02538  -0.18688 0.08705  380 TRP A CE3 
3070 C CZ2 . TRP A 380 ? 0.88850 0.71780 0.74576 0.03838  -0.18125 0.09597  380 TRP A CZ2 
3071 C CZ3 . TRP A 380 ? 0.75574 0.57904 0.61897 0.03046  -0.18377 0.09330  380 TRP A CZ3 
3072 C CH2 . TRP A 380 ? 0.79014 0.62200 0.65206 0.03697  -0.18092 0.09779  380 TRP A CH2 
3073 N N   . ASP A 381 ? 0.67251 0.46789 0.53419 0.01649  -0.19457 0.08154  381 ASP A N   
3074 C CA  . ASP A 381 ? 0.78600 0.58616 0.65660 0.01562  -0.19565 0.08643  381 ASP A CA  
3075 C C   . ASP A 381 ? 0.76055 0.56353 0.63816 0.01350  -0.19614 0.08893  381 ASP A C   
3076 O O   . ASP A 381 ? 0.78494 0.58917 0.67015 0.01114  -0.19814 0.09165  381 ASP A O   
3077 C CB  . ASP A 381 ? 0.90078 0.71048 0.77330 0.02142  -0.19303 0.09236  381 ASP A CB  
3078 C CG  . ASP A 381 ? 0.97940 0.78544 0.84607 0.02270  -0.19332 0.08984  381 ASP A CG  
3079 O OD1 . ASP A 381 ? 0.98119 0.77675 0.84245 0.01879  -0.19572 0.08338  381 ASP A OD1 
3080 O OD2 . ASP A 381 ? 1.07718 0.89104 0.94458 0.02792  -0.19097 0.09454  381 ASP A OD2 
3081 N N   . ILE A 382 ? 0.75610 0.55987 0.63143 0.01425  -0.19459 0.08804  382 ILE A N   
3082 C CA  . ILE A 382 ? 0.68350 0.48923 0.56483 0.01217  -0.19508 0.08992  382 ILE A CA  
3083 C C   . ILE A 382 ? 0.60662 0.40350 0.48248 0.00849  -0.19641 0.08347  382 ILE A C   
3084 O O   . ILE A 382 ? 0.70274 0.49850 0.57181 0.01054  -0.19465 0.08094  382 ILE A O   
3085 C CB  . ILE A 382 ? 0.63171 0.44904 0.51663 0.01759  -0.19133 0.09656  382 ILE A CB  
3086 C CG1 . ILE A 382 ? 0.69557 0.52191 0.58496 0.02214  -0.18949 0.10316  382 ILE A CG1 
3087 C CG2 . ILE A 382 ? 0.65384 0.47301 0.54561 0.01528  -0.19202 0.09876  382 ILE A CG2 
3088 C CD1 . ILE A 382 ? 0.76700 0.60519 0.65892 0.02859  -0.18531 0.11007  382 ILE A CD1 
3089 N N   . TYR A 383 ? 0.71403 0.50459 0.59280 0.00321  -0.19962 0.08086  383 TYR A N   
3090 C CA  . TYR A 383 ? 0.68433 0.46550 0.55726 -0.00029 -0.20104 0.07442  383 TYR A CA  
3091 C C   . TYR A 383 ? 0.68399 0.46806 0.55658 0.00080  -0.19915 0.07495  383 TYR A C   
3092 O O   . TYR A 383 ? 0.69076 0.46939 0.55684 0.00009  -0.19885 0.07041  383 TYR A O   
3093 C CB  . TYR A 383 ? 0.69203 0.46549 0.56744 -0.00572 -0.20505 0.07139  383 TYR A CB  
3094 C CG  . TYR A 383 ? 0.68346 0.45920 0.56656 -0.00791 -0.20650 0.07391  383 TYR A CG  
3095 C CD1 . TYR A 383 ? 0.64616 0.41882 0.52793 -0.00969 -0.20667 0.07147  383 TYR A CD1 
3096 C CD2 . TYR A 383 ? 0.71210 0.49270 0.60398 -0.00831 -0.20792 0.07871  383 TYR A CD2 
3097 C CE1 . TYR A 383 ? 0.69330 0.46775 0.58202 -0.01162 -0.20814 0.07368  383 TYR A CE1 
3098 C CE2 . TYR A 383 ? 0.76538 0.54753 0.66459 -0.01045 -0.20959 0.08094  383 TYR A CE2 
3099 C CZ  . TYR A 383 ? 0.73144 0.51044 0.62888 -0.01206 -0.20969 0.07833  383 TYR A CZ  
3100 O OH  . TYR A 383 ? 0.90342 0.68378 0.80812 -0.01411 -0.21147 0.08050  383 TYR A OH  
3101 N N   . GLY A 384 ? 0.67798 0.47074 0.55765 0.00273  -0.19782 0.08073  384 GLY A N   
3102 C CA  . GLY A 384 ? 0.65913 0.45489 0.53898 0.00373  -0.19612 0.08153  384 GLY A CA  
3103 C C   . GLY A 384 ? 0.61900 0.42446 0.50730 0.00593  -0.19465 0.08843  384 GLY A C   
3104 O O   . GLY A 384 ? 0.62018 0.43044 0.51467 0.00684  -0.19487 0.09301  384 GLY A O   
3105 N N   . GLU A 385 ? 0.67678 0.48501 0.56527 0.00691  -0.19312 0.08925  385 GLU A N   
3106 C CA  . GLU A 385 ? 0.68330 0.50061 0.57960 0.00919  -0.19146 0.09587  385 GLU A CA  
3107 C C   . GLU A 385 ? 0.65656 0.47029 0.55378 0.00606  -0.19258 0.09358  385 GLU A C   
3108 O O   . GLU A 385 ? 0.69869 0.50587 0.58914 0.00438  -0.19309 0.08801  385 GLU A O   
3109 C CB  . GLU A 385 ? 0.59967 0.42679 0.49402 0.01601  -0.18714 0.10048  385 GLU A CB  
3110 C CG  . GLU A 385 ? 0.66791 0.49955 0.56157 0.01983  -0.18573 0.10340  385 GLU A CG  
3111 C CD  . GLU A 385 ? 0.79264 0.63418 0.68371 0.02715  -0.18142 0.10793  385 GLU A CD  
3112 O OE1 . GLU A 385 ? 0.81276 0.65758 0.70300 0.02895  -0.17971 0.10885  385 GLU A OE1 
3113 O OE2 . GLU A 385 ? 0.93589 0.78198 0.82565 0.03121  -0.17980 0.11058  385 GLU A OE2 
3114 N N   . GLY A 386 ? 0.64961 0.46701 0.55514 0.00510  -0.19318 0.09767  386 GLY A N   
3115 C CA  . GLY A 386 ? 0.66664 0.48028 0.57324 0.00199  -0.19452 0.09542  386 GLY A CA  
3116 C C   . GLY A 386 ? 0.57114 0.38213 0.48587 -0.00229 -0.19802 0.09635  386 GLY A C   
3117 O O   . GLY A 386 ? 0.68902 0.49833 0.60742 -0.00414 -0.20037 0.09693  386 GLY A O   
3118 N N   . PRO A 387 ? 0.64318 0.45350 0.56073 -0.00392 -0.19865 0.09632  387 PRO A N   
3119 C CA  . PRO A 387 ? 0.66953 0.47688 0.59473 -0.00799 -0.20234 0.09690  387 PRO A CA  
3120 C C   . PRO A 387 ? 0.70007 0.49620 0.62172 -0.01299 -0.20659 0.09009  387 PRO A C   
3121 O O   . PRO A 387 ? 0.71344 0.50663 0.64083 -0.01612 -0.21026 0.09030  387 PRO A O   
3122 C CB  . PRO A 387 ? 0.74689 0.55707 0.67397 -0.00727 -0.20093 0.09842  387 PRO A CB  
3123 C CG  . PRO A 387 ? 0.66167 0.47046 0.57920 -0.00535 -0.19837 0.09463  387 PRO A CG  
3124 C CD  . PRO A 387 ? 0.61039 0.42290 0.52388 -0.00173 -0.19596 0.09579  387 PRO A CD  
3125 N N   . ASN A 388 ? 0.60024 0.39047 0.51265 -0.01340 -0.20606 0.08441  388 ASN A N   
3126 C CA  . ASN A 388 ? 0.62282 0.40229 0.53076 -0.01754 -0.20958 0.07789  388 ASN A CA  
3127 C C   . ASN A 388 ? 0.72297 0.49787 0.62742 -0.01848 -0.21110 0.07530  388 ASN A C   
3128 O O   . ASN A 388 ? 0.67216 0.44724 0.57037 -0.01638 -0.20880 0.07391  388 ASN A O   
3129 C CB  . ASN A 388 ? 0.61252 0.38788 0.51332 -0.01769 -0.20835 0.07357  388 ASN A CB  
3130 C CG  . ASN A 388 ? 0.67011 0.44921 0.57488 -0.01724 -0.20749 0.07593  388 ASN A CG  
3131 O OD1 . ASN A 388 ? 0.72372 0.49920 0.63189 -0.01994 -0.21031 0.07497  388 ASN A OD1 
3132 N ND2 . ASN A 388 ? 0.72325 0.50934 0.62728 -0.01369 -0.20374 0.07886  388 ASN A ND2 
3133 N N   . GLN A 389 ? 0.70235 0.47311 0.61081 -0.02152 -0.21509 0.07461  389 GLN A N   
3134 C CA  . GLN A 389 ? 0.69823 0.46433 0.60389 -0.02265 -0.21696 0.07220  389 GLN A CA  
3135 C C   . GLN A 389 ? 0.64514 0.40143 0.54928 -0.02662 -0.22150 0.06727  389 GLN A C   
3136 O O   . GLN A 389 ? 0.77062 0.52569 0.67966 -0.02856 -0.22410 0.06769  389 GLN A O   
3137 C CB  . GLN A 389 ? 0.78503 0.55767 0.69833 -0.02156 -0.21729 0.07772  389 GLN A CB  
3138 C CG  . GLN A 389 ? 0.80355 0.58708 0.72004 -0.01712 -0.21292 0.08386  389 GLN A CG  
3139 C CD  . GLN A 389 ? 1.07226 0.86279 0.99835 -0.01624 -0.21345 0.09027  389 GLN A CD  
3140 O OE1 . GLN A 389 ? 1.19308 0.98012 1.12302 -0.01905 -0.21721 0.08982  389 GLN A OE1 
3141 N NE2 . GLN A 389 ? 1.09411 0.89458 1.02411 -0.01216 -0.20972 0.09642  389 GLN A NE2 
3142 N N   . VAL A 390 ? 0.66029 0.40982 0.55800 -0.02756 -0.22262 0.06297  390 VAL A N   
3143 C CA  . VAL A 390 ? 0.68936 0.42905 0.58433 -0.03077 -0.22683 0.05805  390 VAL A CA  
3144 C C   . VAL A 390 ? 0.71396 0.45371 0.61658 -0.03266 -0.23103 0.06021  390 VAL A C   
3145 O O   . VAL A 390 ? 0.64765 0.39388 0.55561 -0.03145 -0.23027 0.06469  390 VAL A O   
3146 C CB  . VAL A 390 ? 0.63513 0.36760 0.52028 -0.03078 -0.22618 0.05292  390 VAL A CB  
3147 C CG1 . VAL A 390 ? 0.63881 0.37044 0.51721 -0.02942 -0.22272 0.05065  390 VAL A CG1 
3148 C CG2 . VAL A 390 ? 0.77744 0.51233 0.66220 -0.02946 -0.22530 0.05442  390 VAL A CG2 
3149 N N   . THR A 391 ? 0.73601 0.46873 0.63906 -0.03533 -0.23537 0.05718  391 THR A N   
3150 C CA  . THR A 391 ? 0.78398 0.51589 0.69476 -0.03748 -0.24024 0.05889  391 THR A CA  
3151 C C   . THR A 391 ? 0.68381 0.41445 0.59357 -0.03754 -0.24123 0.05872  391 THR A C   
3152 O O   . THR A 391 ? 0.67435 0.41068 0.59228 -0.03756 -0.24224 0.06340  391 THR A O   
3153 C CB  . THR A 391 ? 0.69577 0.41932 0.60540 -0.03987 -0.24476 0.05478  391 THR A CB  
3154 O OG1 . THR A 391 ? 0.96831 0.68359 0.86704 -0.03973 -0.24413 0.04889  391 THR A OG1 
3155 C CG2 . THR A 391 ? 0.63787 0.36435 0.55176 -0.03993 -0.24453 0.05647  391 THR A CG2 
3156 N N   . GLY A 392 ? 0.69343 0.41722 0.59370 -0.03739 -0.24068 0.05385  392 GLY A N   
3157 C CA  . GLY A 392 ? 0.70051 0.42285 0.59899 -0.03722 -0.24132 0.05348  392 GLY A CA  
3158 C C   . GLY A 392 ? 0.74447 0.45614 0.63779 -0.03918 -0.24539 0.04824  392 GLY A C   
3159 O O   . GLY A 392 ? 0.87273 0.58059 0.76965 -0.04118 -0.24980 0.04737  392 GLY A O   
3160 N N   . GLY A 393 ? 0.67080 0.37766 0.55589 -0.03842 -0.24401 0.04491  393 GLY A N   
3161 C CA  . GLY A 393 ? 0.71996 0.41668 0.59977 -0.03977 -0.24758 0.04027  393 GLY A CA  
3162 C C   . GLY A 393 ? 0.68804 0.37707 0.55876 -0.03953 -0.24654 0.03529  393 GLY A C   
3163 O O   . GLY A 393 ? 0.80802 0.49978 0.67666 -0.03852 -0.24306 0.03541  393 GLY A O   
3164 N N   . SER A 394 ? 0.69738 0.37712 0.56290 -0.04021 -0.24945 0.03128  394 SER A N   
3165 C CA  . SER A 394 ? 0.68677 0.36373 0.54465 -0.03794 -0.24582 0.02792  394 SER A CA  
3166 C C   . SER A 394 ? 0.68370 0.36128 0.54418 -0.03784 -0.24665 0.02772  394 SER A C   
3167 O O   . SER A 394 ? 0.69107 0.37012 0.55907 -0.03953 -0.25063 0.02971  394 SER A O   
3168 C CB  . SER A 394 ? 0.75014 0.42353 0.60283 -0.03607 -0.24499 0.02559  394 SER A CB  
3169 O OG  . SER A 394 ? 0.81532 0.48808 0.66580 -0.03619 -0.24443 0.02584  394 SER A OG  
3170 N N   . PHE A 395 ? 0.65055 0.32695 0.50524 -0.03597 -0.24323 0.02552  395 PHE A N   
3171 C CA  . PHE A 395 ? 0.72872 0.40526 0.58486 -0.03556 -0.24378 0.02505  395 PHE A CA  
3172 C C   . PHE A 395 ? 0.74305 0.42330 0.60653 -0.03792 -0.24597 0.02795  395 PHE A C   
3173 O O   . PHE A 395 ? 0.75944 0.44031 0.62842 -0.03870 -0.24910 0.02886  395 PHE A O   
3174 C CB  . PHE A 395 ? 0.76043 0.43390 0.61674 -0.03443 -0.24624 0.02363  395 PHE A CB  
3175 C CG  . PHE A 395 ? 0.65168 0.32109 0.50009 -0.03197 -0.24404 0.02089  395 PHE A CG  
3176 C CD1 . PHE A 395 ? 0.71876 0.38533 0.56039 -0.02973 -0.24150 0.01857  395 PHE A CD1 
3177 C CD2 . PHE A 395 ? 0.64708 0.31503 0.49494 -0.03198 -0.24506 0.02085  395 PHE A CD2 
3178 C CE1 . PHE A 395 ? 0.75688 0.41947 0.59150 -0.02757 -0.23989 0.01642  395 PHE A CE1 
3179 C CE2 . PHE A 395 ? 0.74856 0.41264 0.58933 -0.02976 -0.24327 0.01853  395 PHE A CE2 
3180 C CZ  . PHE A 395 ? 0.74963 0.41106 0.58386 -0.02758 -0.24072 0.01640  395 PHE A CZ  
3181 N N   . THR A 396 ? 0.74379 0.42616 0.60730 -0.03898 -0.24463 0.02941  396 THR A N   
3182 C CA  . THR A 396 ? 0.66950 0.35961 0.54034 -0.03945 -0.24399 0.03340  396 THR A CA  
3183 C C   . THR A 396 ? 0.76542 0.45715 0.63224 -0.03819 -0.23994 0.03276  396 THR A C   
3184 O O   . THR A 396 ? 0.76138 0.44790 0.62010 -0.03745 -0.23810 0.02941  396 THR A O   
3185 C CB  . THR A 396 ? 0.60953 0.30749 0.48581 -0.03902 -0.24247 0.03771  396 THR A CB  
3186 O OG1 . THR A 396 ? 0.79988 0.49699 0.66941 -0.03767 -0.23903 0.03628  396 THR A OG1 
3187 C CG2 . THR A 396 ? 0.72757 0.42467 0.60935 -0.04046 -0.24684 0.03895  396 THR A CG2 
3188 N N   . ALA A 397 ? 0.82847 0.52712 0.70107 -0.03792 -0.23871 0.03604  397 ALA A N   
3189 C CA  . ALA A 397 ? 0.80861 0.50893 0.67790 -0.03675 -0.23516 0.03556  397 ALA A CA  
3190 C C   . ALA A 397 ? 0.69483 0.39927 0.56085 -0.03514 -0.23054 0.03649  397 ALA A C   
3191 O O   . ALA A 397 ? 0.64249 0.35280 0.51226 -0.03447 -0.22941 0.03969  397 ALA A O   
3192 C CB  . ALA A 397 ? 0.66626 0.37222 0.54265 -0.03684 -0.23552 0.03873  397 ALA A CB  
3193 N N   . PRO A 398 ? 0.66282 0.36449 0.52212 -0.03434 -0.22788 0.03395  398 PRO A N   
3194 C CA  . PRO A 398 ? 0.63674 0.34211 0.49303 -0.03277 -0.22377 0.03470  398 PRO A CA  
3195 C C   . PRO A 398 ? 0.67656 0.39153 0.53892 -0.03149 -0.22164 0.03925  398 PRO A C   
3196 O O   . PRO A 398 ? 0.74403 0.46193 0.61088 -0.03170 -0.22219 0.04097  398 PRO A O   
3197 C CB  . PRO A 398 ? 0.56160 0.26212 0.41118 -0.03254 -0.22221 0.03146  398 PRO A CB  
3198 C CG  . PRO A 398 ? 0.77371 0.46632 0.62063 -0.03367 -0.22537 0.02832  398 PRO A CG  
3199 C CD  . PRO A 398 ? 0.67362 0.36832 0.52755 -0.03464 -0.22865 0.03026  398 PRO A CD  
3200 N N   . LEU A 399 ? 0.70030 0.42014 0.56280 -0.02991 -0.21926 0.04131  399 LEU A N   
3201 C CA  . LEU A 399 ? 0.65241 0.38178 0.51998 -0.02793 -0.21677 0.04594  399 LEU A CA  
3202 C C   . LEU A 399 ? 0.62790 0.35890 0.49309 -0.02689 -0.21419 0.04557  399 LEU A C   
3203 O O   . LEU A 399 ? 0.65113 0.37755 0.50973 -0.02686 -0.21300 0.04227  399 LEU A O   
3204 C CB  . LEU A 399 ? 0.50461 0.23887 0.37203 -0.02579 -0.21466 0.04821  399 LEU A CB  
3205 C CG  . LEU A 399 ? 0.52648 0.27079 0.39848 -0.02301 -0.21186 0.05323  399 LEU A CG  
3206 C CD1 . LEU A 399 ? 0.57787 0.32762 0.45897 -0.02337 -0.21334 0.05770  399 LEU A CD1 
3207 C CD2 . LEU A 399 ? 0.46093 0.20889 0.33080 -0.02040 -0.20967 0.05465  399 LEU A CD2 
3208 N N   . GLN A 400 ? 0.65724 0.39452 0.52799 -0.02611 -0.21348 0.04902  400 GLN A N   
3209 C CA  . GLN A 400 ? 0.61465 0.35485 0.48388 -0.02476 -0.21084 0.04940  400 GLN A CA  
3210 C C   . GLN A 400 ? 0.69656 0.44670 0.57183 -0.02234 -0.20888 0.05490  400 GLN A C   
3211 O O   . GLN A 400 ? 0.77642 0.53002 0.65862 -0.02279 -0.21018 0.05803  400 GLN A O   
3212 C CB  . GLN A 400 ? 0.59127 0.32755 0.46035 -0.02634 -0.21225 0.04745  400 GLN A CB  
3213 C CG  . GLN A 400 ? 0.74362 0.47076 0.60573 -0.02785 -0.21335 0.04236  400 GLN A CG  
3214 C CD  . GLN A 400 ? 0.65698 0.38176 0.51825 -0.02843 -0.21372 0.04093  400 GLN A CD  
3215 O OE1 . GLN A 400 ? 0.70339 0.43250 0.56558 -0.02729 -0.21163 0.04246  400 GLN A OE1 
3216 N NE2 . GLN A 400 ? 0.66852 0.38641 0.52782 -0.02995 -0.21643 0.03803  400 GLN A NE2 
3217 N N   . GLY A 401 ? 0.60635 0.36069 0.47912 -0.01971 -0.20608 0.05613  401 GLY A N   
3218 C CA  . GLY A 401 ? 0.58710 0.35129 0.46485 -0.01663 -0.20386 0.06163  401 GLY A CA  
3219 C C   . GLY A 401 ? 0.68477 0.45377 0.56143 -0.01427 -0.20106 0.06298  401 GLY A C   
3220 O O   . GLY A 401 ? 0.63648 0.40152 0.51043 -0.01561 -0.20131 0.06016  401 GLY A O   
3221 N N   . ASN A 402 ? 0.61132 0.38883 0.49000 -0.01060 -0.19847 0.06736  402 ASN A N   
3222 C CA  . ASN A 402 ? 0.62319 0.40621 0.50105 -0.00783 -0.19579 0.06915  402 ASN A CA  
3223 C C   . ASN A 402 ? 0.60918 0.39946 0.48556 -0.00326 -0.19299 0.07226  402 ASN A C   
3224 O O   . ASN A 402 ? 0.61434 0.40437 0.48979 -0.00260 -0.19320 0.07242  402 ASN A O   
3225 C CB  . ASN A 402 ? 0.55241 0.33962 0.43703 -0.00810 -0.19589 0.07260  402 ASN A CB  
3226 C CG  . ASN A 402 ? 0.61708 0.41150 0.50976 -0.00664 -0.19562 0.07856  402 ASN A CG  
3227 O OD1 . ASN A 402 ? 0.64629 0.44552 0.53957 -0.00398 -0.19423 0.08142  402 ASN A OD1 
3228 N ND2 . ASN A 402 ? 0.69884 0.49407 0.59792 -0.00824 -0.19696 0.08061  402 ASN A ND2 
3229 N N   . SER A 403 ? 0.64921 0.44593 0.52543 0.00000  -0.19052 0.07480  403 SER A N   
3230 C CA  . SER A 403 ? 0.61310 0.41714 0.48701 0.00509  -0.18774 0.07769  403 SER A CA  
3231 C C   . SER A 403 ? 0.66166 0.47273 0.54061 0.00776  -0.18674 0.08310  403 SER A C   
3232 O O   . SER A 403 ? 0.59600 0.41212 0.47225 0.01197  -0.18472 0.08502  403 SER A O   
3233 C CB  . SER A 403 ? 0.58329 0.39327 0.45723 0.00793  -0.18562 0.07989  403 SER A CB  
3234 O OG  . SER A 403 ? 0.67252 0.48775 0.55391 0.00809  -0.18519 0.08449  403 SER A OG  
3235 N N   . SER A 404 ? 0.53933 0.35082 0.42544 0.00556  -0.18817 0.08561  404 SER A N   
3236 C CA  . SER A 404 ? 0.54564 0.36373 0.43713 0.00797  -0.18731 0.09104  404 SER A CA  
3237 C C   . SER A 404 ? 0.69080 0.50387 0.58084 0.00608  -0.18921 0.08871  404 SER A C   
3238 O O   . SER A 404 ? 0.63925 0.45749 0.53325 0.00815  -0.18855 0.09299  404 SER A O   
3239 C CB  . SER A 404 ? 0.64510 0.46662 0.54598 0.00674  -0.18807 0.09556  404 SER A CB  
3240 O OG  . SER A 404 ? 0.83507 0.66284 0.73781 0.00946  -0.18576 0.09892  404 SER A OG  
3241 N N   . ASP A 405 ? 0.62384 0.42719 0.50825 0.00246  -0.19140 0.08225  405 ASP A N   
3242 C CA  . ASP A 405 ? 0.55910 0.35657 0.44176 0.00026  -0.19350 0.07949  405 ASP A CA  
3243 C C   . ASP A 405 ? 0.61744 0.41317 0.49220 0.00252  -0.19226 0.07674  405 ASP A C   
3244 O O   . ASP A 405 ? 0.55391 0.34671 0.42278 0.00284  -0.19157 0.07337  405 ASP A O   
3245 C CB  . ASP A 405 ? 0.55632 0.34405 0.43856 -0.00513 -0.19697 0.07462  405 ASP A CB  
3246 C CG  . ASP A 405 ? 0.64458 0.43288 0.53462 -0.00767 -0.19898 0.07685  405 ASP A CG  
3247 O OD1 . ASP A 405 ? 0.69390 0.48660 0.59064 -0.00727 -0.19956 0.08115  405 ASP A OD1 
3248 O OD2 . ASP A 405 ? 0.63528 0.41925 0.52465 -0.01006 -0.20015 0.07418  405 ASP A OD2 
3249 N N   . ILE A 406 ? 0.64151 0.43940 0.51661 0.00423  -0.19201 0.07851  406 ILE A N   
3250 C CA  . ILE A 406 ? 0.58185 0.37786 0.44968 0.00648  -0.19110 0.07600  406 ILE A CA  
3251 C C   . ILE A 406 ? 0.70687 0.49549 0.57324 0.00338  -0.19360 0.07272  406 ILE A C   
3252 O O   . ILE A 406 ? 0.61023 0.39993 0.48248 0.00184  -0.19505 0.07510  406 ILE A O   
3253 C CB  . ILE A 406 ? 0.66690 0.47324 0.53550 0.01254  -0.18801 0.08144  406 ILE A CB  
3254 C CG1 . ILE A 406 ? 0.64266 0.45722 0.51340 0.01597  -0.18547 0.08547  406 ILE A CG1 
3255 C CG2 . ILE A 406 ? 0.67294 0.47701 0.53380 0.01497  -0.18734 0.07860  406 ILE A CG2 
3256 C CD1 . ILE A 406 ? 0.70320 0.52880 0.57510 0.02247  -0.18223 0.09158  406 ILE A CD1 
3257 N N   . ARG A 407 ? 0.71115 0.49243 0.57004 0.00254  -0.19418 0.06754  407 ARG A N   
3258 C CA  . ARG A 407 ? 0.62717 0.40136 0.48377 0.00008  -0.19630 0.06437  407 ARG A CA  
3259 C C   . ARG A 407 ? 0.62553 0.40000 0.47622 0.00347  -0.19493 0.06350  407 ARG A C   
3260 O O   . ARG A 407 ? 0.57664 0.34924 0.42171 0.00487  -0.19394 0.06103  407 ARG A O   
3261 C CB  . ARG A 407 ? 0.57419 0.33812 0.42809 -0.00477 -0.19876 0.05892  407 ARG A CB  
3262 C CG  . ARG A 407 ? 0.55905 0.32222 0.41906 -0.00808 -0.20078 0.05982  407 ARG A CG  
3263 C CD  . ARG A 407 ? 0.60167 0.36768 0.46776 -0.00856 -0.20225 0.06305  407 ARG A CD  
3264 N NE  . ARG A 407 ? 0.76139 0.52513 0.63275 -0.01205 -0.20484 0.06310  407 ARG A NE  
3265 C CZ  . ARG A 407 ? 0.67953 0.44932 0.55786 -0.01172 -0.20463 0.06726  407 ARG A CZ  
3266 N NH1 . ARG A 407 ? 0.63516 0.41411 0.51602 -0.00782 -0.20163 0.07202  407 ARG A NH1 
3267 N NH2 . ARG A 407 ? 0.68649 0.45305 0.56912 -0.01505 -0.20747 0.06669  407 ARG A NH2 
3268 N N   . PHE A 408 ? 0.64419 0.42080 0.49635 0.00473  -0.19509 0.06552  408 PHE A N   
3269 C CA  . PHE A 408 ? 0.59183 0.36993 0.43889 0.00864  -0.19365 0.06545  408 PHE A CA  
3270 C C   . PHE A 408 ? 0.71723 0.48574 0.55871 0.00636  -0.19551 0.06037  408 PHE A C   
3271 O O   . PHE A 408 ? 0.68740 0.45094 0.53089 0.00265  -0.19776 0.05890  408 PHE A O   
3272 C CB  . PHE A 408 ? 0.60447 0.39257 0.45650 0.01265  -0.19201 0.07176  408 PHE A CB  
3273 C CG  . PHE A 408 ? 0.70779 0.50662 0.56501 0.01619  -0.18955 0.07774  408 PHE A CG  
3274 C CD1 . PHE A 408 ? 0.70092 0.50434 0.55449 0.02032  -0.18715 0.07858  408 PHE A CD1 
3275 C CD2 . PHE A 408 ? 0.67443 0.47886 0.54025 0.01564  -0.18969 0.08275  408 PHE A CD2 
3276 C CE1 . PHE A 408 ? 0.78784 0.60152 0.64601 0.02399  -0.18469 0.08443  408 PHE A CE1 
3277 C CE2 . PHE A 408 ? 0.68655 0.50092 0.55729 0.01919  -0.18722 0.08867  408 PHE A CE2 
3278 C CZ  . PHE A 408 ? 0.72070 0.53988 0.58747 0.02350  -0.18458 0.08958  408 PHE A CZ  
3279 N N   . THR A 409 ? 0.69502 0.46093 0.52965 0.00866  -0.19471 0.05779  409 THR A N   
3280 C CA  . THR A 409 ? 0.73301 0.49036 0.56197 0.00735  -0.19614 0.05342  409 THR A CA  
3281 C C   . THR A 409 ? 0.69175 0.45281 0.51651 0.01250  -0.19448 0.05448  409 THR A C   
3282 O O   . THR A 409 ? 0.74175 0.51011 0.56687 0.01633  -0.19249 0.05735  409 THR A O   
3283 C CB  . THR A 409 ? 0.58975 0.33675 0.41396 0.00361  -0.19761 0.04776  409 THR A CB  
3284 O OG1 . THR A 409 ? 0.76853 0.51581 0.58875 0.00574  -0.19642 0.04658  409 THR A OG1 
3285 C CG2 . THR A 409 ? 0.69432 0.43835 0.52232 -0.00081 -0.19905 0.04694  409 THR A CG2 
3286 N N   . ARG A 410 ? 0.70866 0.46528 0.52968 0.01284  -0.19528 0.05251  410 ARG A N   
3287 C CA  . ARG A 410 ? 0.65705 0.41645 0.47367 0.01778  -0.19399 0.05319  410 ARG A CA  
3288 C C   . ARG A 410 ? 0.69116 0.44018 0.50097 0.01642  -0.19560 0.04787  410 ARG A C   
3289 O O   . ARG A 410 ? 0.72325 0.46469 0.53281 0.01215  -0.19746 0.04494  410 ARG A O   
3290 C CB  . ARG A 410 ? 0.78808 0.55639 0.60886 0.02125  -0.19272 0.05858  410 ARG A CB  
3291 C CG  . ARG A 410 ? 0.75720 0.52176 0.58000 0.01844  -0.19446 0.05810  410 ARG A CG  
3292 C CD  . ARG A 410 ? 0.88191 0.65485 0.70751 0.02267  -0.19309 0.06318  410 ARG A CD  
3293 N NE  . ARG A 410 ? 0.91557 0.68554 0.74377 0.01997  -0.19489 0.06309  410 ARG A NE  
3294 C CZ  . ARG A 410 ? 0.81852 0.58168 0.64199 0.01931  -0.19616 0.05971  410 ARG A CZ  
3295 N NH1 . ARG A 410 ? 0.76181 0.51980 0.57776 0.02097  -0.19599 0.05599  410 ARG A NH1 
3296 N NH2 . ARG A 410 ? 0.71704 0.47834 0.54346 0.01696  -0.19782 0.06009  410 ARG A NH2 
3297 N N   . ASN A 411 ? 0.86259 0.50219 0.49567 0.17775  -0.19703 0.03016  411 ASN A N   
3298 C CA  . ASN A 411 ? 0.90839 0.50927 0.51985 0.18434  -0.19712 0.02723  411 ASN A CA  
3299 C C   . ASN A 411 ? 0.91581 0.52614 0.53472 0.20340  -0.19154 0.02964  411 ASN A C   
3300 O O   . ASN A 411 ? 0.91985 0.56326 0.55739 0.21268  -0.18883 0.03237  411 ASN A O   
3301 C CB  . ASN A 411 ? 1.02247 0.58146 0.59912 0.18851  -0.19970 0.01882  411 ASN A CB  
3302 C CG  . ASN A 411 ? 0.89948 0.46878 0.46915 0.20491  -0.19297 0.01282  411 ASN A CG  
3303 O OD1 . ASN A 411 ? 0.97437 0.58120 0.56232 0.21172  -0.18980 0.01858  411 ASN A OD1 
3304 N ND2 . ASN A 411 ? 0.93999 0.47611 0.48443 0.21152  -0.19036 0.00094  411 ASN A ND2 
3305 N N   . LYS A 412 ? 0.91739 0.49936 0.52339 0.20920  -0.18954 0.02980  412 LYS A N   
3306 C CA  . LYS A 412 ? 0.95612 0.54869 0.56931 0.22696  -0.18422 0.03307  412 LYS A CA  
3307 C C   . LYS A 412 ? 1.03319 0.62129 0.63491 0.24839  -0.18020 0.02943  412 LYS A C   
3308 O O   . LYS A 412 ? 1.10116 0.71715 0.71885 0.26226  -0.17651 0.03274  412 LYS A O   
3309 C CB  . LYS A 412 ? 0.95947 0.52268 0.56111 0.22855  -0.18142 0.03624  412 LYS A CB  
3310 C CG  . LYS A 412 ? 0.93271 0.50566 0.54646 0.21141  -0.18350 0.04165  412 LYS A CG  
3311 C CD  . LYS A 412 ? 0.86370 0.40816 0.46605 0.21442  -0.17896 0.04769  412 LYS A CD  
3312 C CE  . LYS A 412 ? 0.88609 0.44141 0.49872 0.19916  -0.18002 0.05405  412 LYS A CE  
3313 N NZ  . LYS A 412 ? 0.86432 0.39425 0.46782 0.20260  -0.17403 0.06313  412 LYS A NZ  
3314 N N   . ASP A 413 ? 1.02213 0.57637 0.59620 0.25260  -0.18127 0.02210  413 ASP A N   
3315 C CA  . ASP A 413 ? 1.01361 0.56372 0.57384 0.27552  -0.17666 0.01749  413 ASP A CA  
3316 C C   . ASP A 413 ? 1.03443 0.63041 0.61295 0.27785  -0.17487 0.02055  413 ASP A C   
3317 O O   . ASP A 413 ? 1.14459 0.75103 0.71947 0.29533  -0.16713 0.01776  413 ASP A O   
3318 C CB  . ASP A 413 ? 1.05965 0.56685 0.58982 0.27456  -0.17536 0.00376  413 ASP A CB  
3319 C CG  . ASP A 413 ? 1.20974 0.66550 0.72328 0.27637  -0.17582 0.00177  413 ASP A CG  
3320 O OD1 . ASP A 413 ? 1.29348 0.75414 0.81753 0.28377  -0.17173 0.01028  413 ASP A OD1 
3321 O OD2 . ASP A 413 ? 1.23386 0.65437 0.73087 0.26532  -0.17725 -0.00975 413 ASP A OD2 
3322 N N   . ALA A 414 ? 0.98693 0.61259 0.58819 0.25939  -0.17944 0.02617  414 ALA A N   
3323 C CA  . ALA A 414 ? 1.00718 0.67795 0.63293 0.25871  -0.17660 0.03171  414 ALA A CA  
3324 C C   . ALA A 414 ? 0.98450 0.65754 0.59483 0.26144  -0.16924 0.02567  414 ALA A C   
3325 O O   . ALA A 414 ? 0.99514 0.70066 0.61899 0.27221  -0.16143 0.03044  414 ALA A O   
3326 C CB  . ALA A 414 ? 0.93323 0.63838 0.58640 0.27387  -0.17206 0.03818  414 ALA A CB  
3327 N N   . ASN A 415 ? 1.03436 0.67529 0.61714 0.25215  -0.17164 0.01520  415 ASN A N   
3328 C CA  . ASN A 415 ? 1.03245 0.67798 0.59794 0.25412  -0.16676 0.00770  415 ASN A CA  
3329 C C   . ASN A 415 ? 1.02245 0.66675 0.58396 0.23155  -0.17316 0.00507  415 ASN A C   
3330 O O   . ASN A 415 ? 1.12267 0.76668 0.66468 0.23209  -0.17150 -0.00345 415 ASN A O   
3331 C CB  . ASN A 415 ? 1.07741 0.68674 0.60943 0.27018  -0.16333 -0.00738 415 ASN A CB  
3332 C CG  . ASN A 415 ? 1.08011 0.63972 0.59612 0.26230  -0.17029 -0.01574 415 ASN A CG  
3333 O OD1 . ASN A 415 ? 1.08558 0.63350 0.60304 0.24098  -0.17800 -0.01626 415 ASN A OD1 
3334 N ND2 . ASN A 415 ? 1.36346 0.89378 0.86584 0.28016  -0.16662 -0.02103 415 ASN A ND2 
3335 N N   . VAL A 416 ? 0.85374 0.49903 0.43231 0.21322  -0.18060 0.01170  416 VAL A N   
3336 C CA  . VAL A 416 ? 0.82948 0.47881 0.40959 0.19197  -0.18649 0.01166  416 VAL A CA  
3337 C C   . VAL A 416 ? 0.89717 0.57835 0.51179 0.18153  -0.18844 0.02565  416 VAL A C   
3338 O O   . VAL A 416 ? 0.78980 0.47085 0.41979 0.18258  -0.19123 0.03063  416 VAL A O   
3339 C CB  . VAL A 416 ? 0.92936 0.53782 0.49184 0.17821  -0.19447 0.00239  416 VAL A CB  
3340 C CG1 . VAL A 416 ? 0.83219 0.45029 0.40149 0.15625  -0.20081 0.00433  416 VAL A CG1 
3341 C CG2 . VAL A 416 ? 0.91421 0.48930 0.44540 0.18682  -0.19347 -0.01423 416 VAL A CG2 
3342 N N   . LEU A 417 ? 0.91872 0.62740 0.54543 0.17270  -0.18711 0.03159  417 LEU A N   
3343 C CA  . LEU A 417 ? 0.72849 0.46690 0.39042 0.16264  -0.18831 0.04393  417 LEU A CA  
3344 C C   . LEU A 417 ? 0.76564 0.50146 0.42724 0.14272  -0.19465 0.04432  417 LEU A C   
3345 O O   . LEU A 417 ? 0.78796 0.52837 0.43619 0.13943  -0.19338 0.04251  417 LEU A O   
3346 C CB  . LEU A 417 ? 0.70012 0.47719 0.38456 0.17158  -0.17863 0.05462  417 LEU A CB  
3347 C CG  . LEU A 417 ? 0.75593 0.56350 0.48278 0.16187  -0.17893 0.06697  417 LEU A CG  
3348 C CD1 . LEU A 417 ? 0.68638 0.49493 0.43446 0.16426  -0.18398 0.06650  417 LEU A CD1 
3349 C CD2 . LEU A 417 ? 0.74623 0.58967 0.49483 0.16908  -0.16743 0.07941  417 LEU A CD2 
3350 N N   . TYR A 418 ? 0.72239 0.45713 0.40353 0.12848  -0.19778 0.04516  418 TYR A N   
3351 C CA  . TYR A 418 ? 0.77190 0.51053 0.46163 0.10880  -0.20013 0.04574  418 TYR A CA  
3352 C C   . TYR A 418 ? 0.71318 0.48659 0.44024 0.10253  -0.19677 0.05630  418 TYR A C   
3353 O O   . TYR A 418 ? 0.80264 0.58669 0.55422 0.10252  -0.19678 0.05842  418 TYR A O   
3354 C CB  . TYR A 418 ? 0.67577 0.39132 0.36228 0.09835  -0.20406 0.04024  418 TYR A CB  
3355 C CG  . TYR A 418 ? 0.82483 0.49998 0.47577 0.10412  -0.20899 0.03166  418 TYR A CG  
3356 C CD1 . TYR A 418 ? 0.75563 0.41050 0.38054 0.09789  -0.21523 0.02504  418 TYR A CD1 
3357 C CD2 . TYR A 418 ? 0.83567 0.49219 0.47905 0.11629  -0.20837 0.03005  418 TYR A CD2 
3358 C CE1 . TYR A 418 ? 0.83388 0.45018 0.43071 0.10149  -0.21891 0.01517  418 TYR A CE1 
3359 C CE2 . TYR A 418 ? 0.85261 0.46689 0.46339 0.12284  -0.21311 0.02369  418 TYR A CE2 
3360 C CZ  . TYR A 418 ? 0.87500 0.47024 0.46661 0.11365  -0.21642 0.01488  418 TYR A CZ  
3361 O OH  . TYR A 418 ? 0.93483 0.49134 0.50506 0.11642  -0.21660 0.00493  418 TYR A OH  
3362 N N   . ALA A 419 ? 0.67120 0.46154 0.40162 0.09833  -0.19473 0.06270  419 ALA A N   
3363 C CA  . ALA A 419 ? 0.67990 0.49873 0.44447 0.09239  -0.19216 0.07441  419 ALA A CA  
3364 C C   . ALA A 419 ? 0.65145 0.47058 0.42102 0.07523  -0.19358 0.07326  419 ALA A C   
3365 O O   . ALA A 419 ? 0.65810 0.47622 0.41043 0.07144  -0.19368 0.07249  419 ALA A O   
3366 C CB  . ALA A 419 ? 0.66516 0.50501 0.43164 0.10347  -0.18705 0.08663  419 ALA A CB  
3367 N N   . THR A 420 ? 0.60772 0.43071 0.40097 0.06656  -0.19482 0.07276  420 THR A N   
3368 C CA  . THR A 420 ? 0.63923 0.46274 0.43811 0.05208  -0.19537 0.07156  420 THR A CA  
3369 C C   . THR A 420 ? 0.58315 0.43037 0.41206 0.04842  -0.19310 0.08234  420 THR A C   
3370 O O   . THR A 420 ? 0.58408 0.44089 0.43864 0.05134  -0.19418 0.08560  420 THR A O   
3371 C CB  . THR A 420 ? 0.67250 0.48024 0.47031 0.04619  -0.19800 0.06288  420 THR A CB  
3372 O OG1 . THR A 420 ? 0.64148 0.42461 0.41083 0.05104  -0.20010 0.05584  420 THR A OG1 
3373 C CG2 . THR A 420 ? 0.58290 0.39124 0.38585 0.03285  -0.19810 0.06222  420 THR A CG2 
3374 N N   . VAL A 421 ? 0.63729 0.49340 0.46349 0.04308  -0.19090 0.08780  421 VAL A N   
3375 C CA  . VAL A 421 ? 0.60881 0.48520 0.46324 0.04011  -0.18809 0.10002  421 VAL A CA  
3376 C C   . VAL A 421 ? 0.67174 0.54426 0.53752 0.02842  -0.19002 0.09441  421 VAL A C   
3377 O O   . VAL A 421 ? 0.64634 0.50797 0.49369 0.02198  -0.19120 0.08668  421 VAL A O   
3378 C CB  . VAL A 421 ? 0.57525 0.46652 0.42046 0.04375  -0.18375 0.11099  421 VAL A CB  
3379 C CG1 . VAL A 421 ? 0.62769 0.53813 0.50385 0.04262  -0.17949 0.12659  421 VAL A CG1 
3380 C CG2 . VAL A 421 ? 0.58243 0.47586 0.40945 0.05732  -0.18197 0.11494  421 VAL A CG2 
3381 N N   . LEU A 422 ? 0.62106 0.50220 0.51742 0.02623  -0.19090 0.09884  422 LEU A N   
3382 C CA  . LEU A 422 ? 0.61891 0.49623 0.52586 0.01744  -0.19348 0.09270  422 LEU A CA  
3383 C C   . LEU A 422 ? 0.58502 0.47137 0.49569 0.01130  -0.19034 0.09964  422 LEU A C   
3384 O O   . LEU A 422 ? 0.56708 0.45376 0.49108 0.00547  -0.19191 0.09783  422 LEU A O   
3385 C CB  . LEU A 422 ? 0.60614 0.48770 0.54413 0.01903  -0.19825 0.09212  422 LEU A CB  
3386 C CG  . LEU A 422 ? 0.58034 0.45608 0.51594 0.02602  -0.20250 0.08388  422 LEU A CG  
3387 C CD1 . LEU A 422 ? 0.52871 0.40886 0.49379 0.02613  -0.21003 0.07817  422 LEU A CD1 
3388 C CD2 . LEU A 422 ? 0.44333 0.30296 0.34635 0.02602  -0.20167 0.07360  422 LEU A CD2 
3389 N N   . GLY A 423 ? 0.61797 0.51283 0.51654 0.01430  -0.18638 0.10740  423 GLY A N   
3390 C CA  . GLY A 423 ? 0.59725 0.50272 0.49533 0.01006  -0.18370 0.11333  423 GLY A CA  
3391 C C   . GLY A 423 ? 0.66255 0.57736 0.53968 0.01605  -0.18099 0.11870  423 GLY A C   
3392 O O   . GLY A 423 ? 0.71529 0.62659 0.57839 0.02329  -0.18112 0.11768  423 GLY A O   
3393 N N   . TRP A 424 ? 0.60821 0.53534 0.48180 0.01425  -0.17931 0.12354  424 TRP A N   
3394 C CA  . TRP A 424 ? 0.58296 0.52366 0.43629 0.02199  -0.17750 0.12892  424 TRP A CA  
3395 C C   . TRP A 424 ? 0.65517 0.61436 0.52503 0.03153  -0.17000 0.14811  424 TRP A C   
3396 O O   . TRP A 424 ? 0.64016 0.60716 0.53158 0.02881  -0.16680 0.15674  424 TRP A O   
3397 C CB  . TRP A 424 ? 0.58265 0.52903 0.42159 0.01630  -0.18093 0.12311  424 TRP A CB  
3398 C CG  . TRP A 424 ? 0.67979 0.64048 0.49383 0.02488  -0.18170 0.12450  424 TRP A CG  
3399 C CD1 . TRP A 424 ? 0.61704 0.60103 0.42861 0.03335  -0.17830 0.13566  424 TRP A CD1 
3400 C CD2 . TRP A 424 ? 0.72082 0.67299 0.50686 0.02749  -0.18668 0.11358  424 TRP A CD2 
3401 N NE1 . TRP A 424 ? 0.63098 0.62536 0.41393 0.04158  -0.18117 0.13192  424 TRP A NE1 
3402 C CE2 . TRP A 424 ? 0.64780 0.62252 0.41544 0.03702  -0.18662 0.11791  424 TRP A CE2 
3403 C CE3 . TRP A 424 ? 0.73717 0.66354 0.51069 0.02382  -0.19137 0.10019  424 TRP A CE3 
3404 C CZ2 . TRP A 424 ? 0.71220 0.68500 0.44990 0.04132  -0.19184 0.10764  424 TRP A CZ2 
3405 C CZ3 . TRP A 424 ? 0.65975 0.57978 0.40362 0.02878  -0.19615 0.09052  424 TRP A CZ3 
3406 C CH2 . TRP A 424 ? 0.71909 0.66193 0.44526 0.03686  -0.19668 0.09317  424 TRP A CH2 
3407 N N   . PRO A 425 ? 0.63958 0.60525 0.50132 0.04302  -0.16635 0.15642  425 PRO A N   
3408 C CA  . PRO A 425 ? 0.58752 0.56999 0.46659 0.05207  -0.15720 0.17723  425 PRO A CA  
3409 C C   . PRO A 425 ? 0.66703 0.66500 0.53112 0.05674  -0.15486 0.18309  425 PRO A C   
3410 O O   . PRO A 425 ? 0.59922 0.60045 0.42931 0.06133  -0.15976 0.17414  425 PRO A O   
3411 C CB  . PRO A 425 ? 0.63813 0.62289 0.50677 0.06355  -0.15433 0.18290  425 PRO A CB  
3412 C CG  . PRO A 425 ? 0.66679 0.64039 0.49927 0.06363  -0.16269 0.16458  425 PRO A CG  
3413 C CD  . PRO A 425 ? 0.52838 0.48514 0.36632 0.04833  -0.16960 0.14808  425 PRO A CD  
3414 N N   . ASP A 426 ? 0.68734 0.69559 0.57872 0.05563  -0.14784 0.19769  426 ASP A N   
3415 C CA  . ASP A 426 ? 0.60859 0.63190 0.48899 0.05972  -0.14588 0.20392  426 ASP A CA  
3416 C C   . ASP A 426 ? 0.69091 0.72865 0.54827 0.07240  -0.14162 0.21247  426 ASP A C   
3417 O O   . ASP A 426 ? 0.63982 0.68857 0.47585 0.07608  -0.14449 0.21141  426 ASP A O   
3418 C CB  . ASP A 426 ? 0.53119 0.56299 0.44946 0.05652  -0.13756 0.21960  426 ASP A CB  
3419 C CG  . ASP A 426 ? 0.63472 0.65515 0.56871 0.04443  -0.14354 0.20951  426 ASP A CG  
3420 O OD1 . ASP A 426 ? 0.69529 0.70451 0.61044 0.03797  -0.15287 0.19136  426 ASP A OD1 
3421 O OD2 . ASP A 426 ? 0.54205 0.56547 0.50877 0.04140  -0.13813 0.22015  426 ASP A OD2 
3422 N N   . ASP A 427 ? 0.74746 0.78814 0.61025 0.07907  -0.13468 0.22102  427 ASP A N   
3423 C CA  . ASP A 427 ? 0.71120 0.76909 0.55204 0.09170  -0.12879 0.22848  427 ASP A CA  
3424 C C   . ASP A 427 ? 0.66890 0.71489 0.46928 0.09405  -0.14012 0.21002  427 ASP A C   
3425 O O   . ASP A 427 ? 0.75708 0.81827 0.53755 0.10522  -0.13500 0.21342  427 ASP A O   
3426 C CB  . ASP A 427 ? 0.59189 0.66599 0.46497 0.09980  -0.11107 0.25090  427 ASP A CB  
3427 C CG  . ASP A 427 ? 0.73476 0.79421 0.62889 0.09578  -0.11207 0.24823  427 ASP A CG  
3428 O OD1 . ASP A 427 ? 0.77909 0.81592 0.66175 0.08726  -0.12592 0.22929  427 ASP A OD1 
3429 O OD2 . ASP A 427 ? 0.81265 0.88486 0.73695 0.10152  -0.09846 0.26565  427 ASP A OD2 
3430 N N   . LYS A 428 ? 0.77301 0.79435 0.56180 0.08529  -0.15348 0.19058  428 LYS A N   
3431 C CA  . LYS A 428 ? 0.71669 0.72249 0.46896 0.08498  -0.16583 0.17242  428 LYS A CA  
3432 C C   . LYS A 428 ? 0.75091 0.76399 0.50321 0.09386  -0.15808 0.17936  428 LYS A C   
3433 O O   . LYS A 428 ? 0.79650 0.81813 0.52079 0.10186  -0.15763 0.17241  428 LYS A O   
3434 C CB  . LYS A 428 ? 0.72378 0.73949 0.44631 0.08068  -0.17510 0.16430  428 LYS A CB  
3435 C CG  . LYS A 428 ? 0.76704 0.77883 0.49005 0.07832  -0.17942 0.15311  428 LYS A CG  
3436 C CD  . LYS A 428 ? 0.71856 0.74481 0.41872 0.07168  -0.18949 0.15050  428 LYS A CD  
3437 C CE  . LYS A 428 ? 0.76220 0.81210 0.44906 0.06050  -0.19478 0.13642  428 LYS A CE  
3438 N NZ  . LYS A 428 ? 0.79347 0.85359 0.45570 0.05826  -0.20533 0.12666  428 LYS A NZ  
3439 N N   . HIS A 429 ? 0.71991 0.73303 0.50570 0.09636  -0.14886 0.19139  429 HIS A N   
3440 C CA  . HIS A 429 ? 0.79409 0.81549 0.58461 0.10849  -0.13920 0.19886  429 HIS A CA  
3441 C C   . HIS A 429 ? 0.74536 0.74950 0.55862 0.10328  -0.14349 0.19544  429 HIS A C   
3442 O O   . HIS A 429 ? 0.75185 0.74838 0.59392 0.09169  -0.14615 0.19608  429 HIS A O   
3443 C CB  . HIS A 429 ? 0.68060 0.73126 0.49631 0.11925  -0.11973 0.22334  429 HIS A CB  
3444 C CG  . HIS A 429 ? 0.84929 0.91411 0.66193 0.13545  -0.10779 0.23110  429 HIS A CG  
3445 N ND1 . HIS A 429 ? 0.89616 0.97378 0.67116 0.14992  -0.10385 0.22647  429 HIS A ND1 
3446 C CD2 . HIS A 429 ? 0.76831 0.83823 0.61176 0.14038  -0.09867 0.24262  429 HIS A CD2 
3447 C CE1 . HIS A 429 ? 0.88714 0.97653 0.66746 0.16432  -0.09176 0.23520  429 HIS A CE1 
3448 N NE2 . HIS A 429 ? 0.88004 0.96553 0.70330 0.15837  -0.08845 0.24596  429 HIS A NE2 
3449 N N   . VAL A 430 ? 0.76635 0.76614 0.56692 0.11322  -0.14275 0.19003  430 VAL A N   
3450 C CA  . VAL A 430 ? 0.70081 0.68375 0.52373 0.10808  -0.14522 0.18168  430 VAL A CA  
3451 C C   . VAL A 430 ? 0.75007 0.74890 0.58634 0.12259  -0.13151 0.19116  430 VAL A C   
3452 O O   . VAL A 430 ? 0.78713 0.79258 0.59201 0.13735  -0.12649 0.18887  430 VAL A O   
3453 C CB  . VAL A 430 ? 0.81306 0.76419 0.60452 0.10231  -0.15945 0.15601  430 VAL A CB  
3454 C CG1 . VAL A 430 ? 0.66282 0.60011 0.47573 0.09994  -0.16132 0.14871  430 VAL A CG1 
3455 C CG2 . VAL A 430 ? 0.63792 0.57922 0.42408 0.08635  -0.16864 0.14679  430 VAL A CG2 
3456 N N   . SER A 431 ? 0.70644 0.71246 0.59032 0.11872  -0.12572 0.20081  431 SER A N   
3457 C CA  . SER A 431 ? 0.72713 0.75137 0.63324 0.13069  -0.11230 0.21146  431 SER A CA  
3458 C C   . SER A 431 ? 0.67943 0.68826 0.60012 0.12699  -0.11959 0.19602  431 SER A C   
3459 O O   . SER A 431 ? 0.70762 0.70765 0.65828 0.11376  -0.12751 0.19116  431 SER A O   
3460 C CB  . SER A 431 ? 0.71208 0.76297 0.66880 0.13007  -0.09776 0.23838  431 SER A CB  
3461 O OG  . SER A 431 ? 0.71051 0.77818 0.65248 0.13625  -0.08988 0.25541  431 SER A OG  
3462 N N   . ILE A 432 ? 0.63406 0.64076 0.53277 0.14010  -0.11711 0.18797  432 ILE A N   
3463 C CA  . ILE A 432 ? 0.68481 0.68022 0.59457 0.14040  -0.12308 0.17482  432 ILE A CA  
3464 C C   . ILE A 432 ? 0.70641 0.73032 0.65374 0.15078  -0.10868 0.18971  432 ILE A C   
3465 O O   . ILE A 432 ? 0.71043 0.74562 0.63880 0.16753  -0.09845 0.19364  432 ILE A O   
3466 C CB  . ILE A 432 ? 0.70608 0.67559 0.56569 0.14786  -0.13114 0.15450  432 ILE A CB  
3467 C CG1 . ILE A 432 ? 0.73419 0.67693 0.56282 0.13561  -0.14474 0.14123  432 ILE A CG1 
3468 C CG2 . ILE A 432 ? 0.67529 0.63610 0.54712 0.15098  -0.13599 0.14393  432 ILE A CG2 
3469 C CD1 . ILE A 432 ? 0.64879 0.56309 0.43070 0.14120  -0.15225 0.12179  432 ILE A CD1 
3470 N N   . ALA A 433 ? 0.71069 0.74711 0.71323 0.14099  -0.10784 0.19738  433 ALA A N   
3471 C CA  . ALA A 433 ? 0.61275 0.67963 0.66065 0.14809  -0.09324 0.21424  433 ALA A CA  
3472 C C   . ALA A 433 ? 0.67649 0.74569 0.71883 0.16055  -0.09346 0.20433  433 ALA A C   
3473 O O   . ALA A 433 ? 0.71991 0.81368 0.77432 0.17428  -0.07857 0.21753  433 ALA A O   
3474 C CB  . ALA A 433 ? 0.49315 0.56988 0.60472 0.13273  -0.09467 0.22096  433 ALA A CB  
3475 N N   . SER A 434 ? 0.73073 0.77591 0.75473 0.15739  -0.10924 0.18266  434 SER A N   
3476 C CA  . SER A 434 ? 0.69364 0.73967 0.71248 0.16999  -0.11063 0.17308  434 SER A CA  
3477 C C   . SER A 434 ? 0.73887 0.77735 0.70565 0.18874  -0.10377 0.16986  434 SER A C   
3478 O O   . SER A 434 ? 0.86994 0.90574 0.82730 0.20115  -0.10466 0.16133  434 SER A O   
3479 C CB  . SER A 434 ? 0.67712 0.69958 0.68994 0.16251  -0.12922 0.15259  434 SER A CB  
3480 O OG  . SER A 434 ? 0.86641 0.85789 0.83719 0.15488  -0.13918 0.14181  434 SER A OG  
3481 N N   . LEU A 435 ? 0.77981 0.81253 0.71056 0.19133  -0.09910 0.17360  435 LEU A N   
3482 C CA  . LEU A 435 ? 0.75060 0.77772 0.63228 0.21056  -0.09276 0.16823  435 LEU A CA  
3483 C C   . LEU A 435 ? 0.83329 0.89260 0.71940 0.22222  -0.07407 0.18942  435 LEU A C   
3484 O O   . LEU A 435 ? 0.88728 0.94382 0.72816 0.23626  -0.06941 0.18577  435 LEU A O   
3485 C CB  . LEU A 435 ? 0.71508 0.70628 0.54368 0.20606  -0.10546 0.14960  435 LEU A CB  
3486 C CG  . LEU A 435 ? 0.80421 0.76228 0.62119 0.19924  -0.12117 0.13001  435 LEU A CG  
3487 C CD1 . LEU A 435 ? 0.64730 0.57094 0.41278 0.19677  -0.13074 0.11308  435 LEU A CD1 
3488 C CD2 . LEU A 435 ? 0.80672 0.76734 0.62947 0.21442  -0.11825 0.12567  435 LEU A CD2 
3489 N N   . GLY A 436 ? 0.93111 1.02018 0.87149 0.21704  -0.06373 0.21059  436 GLY A N   
3490 C CA  . GLY A 436 ? 0.96938 1.09287 0.92102 0.22907  -0.04309 0.23579  436 GLY A CA  
3491 C C   . GLY A 436 ? 0.97930 1.12716 0.94014 0.24919  -0.02842 0.24325  436 GLY A C   
3492 O O   . GLY A 436 ? 0.97642 1.11352 0.93656 0.25295  -0.03558 0.22808  436 GLY A O   
3493 N N   . SER A 437 ? 0.98471 1.16560 0.95241 0.26327  -0.00787 0.26696  437 SER A N   
3494 C CA  . SER A 437 ? 0.88641 1.09537 0.86271 0.28486  0.00906  0.27694  437 SER A CA  
3495 C C   . SER A 437 ? 0.91958 1.14954 0.96856 0.27554  0.01283  0.28788  437 SER A C   
3496 O O   . SER A 437 ? 0.90224 1.14337 0.96077 0.28771  0.01665  0.28419  437 SER A O   
3497 C CB  . SER A 437 ? 0.68333 0.92378 0.64723 0.30259  0.03061  0.30106  437 SER A CB  
3498 N N   . ASP A 438 ? 0.88745 1.12322 0.98695 0.25518  0.01158  0.30025  438 ASP A N   
3499 C CA  . ASP A 438 ? 0.83742 1.09121 1.00858 0.24417  0.01194  0.30610  438 ASP A CA  
3500 C C   . ASP A 438 ? 0.80618 1.03812 0.97434 0.23869  -0.00874 0.27802  438 ASP A C   
3501 O O   . ASP A 438 ? 0.75326 1.00428 0.97210 0.23616  -0.00903 0.27888  438 ASP A O   
3502 C CB  . ASP A 438 ? 0.81342 1.07095 1.03769 0.22217  0.01175  0.31997  438 ASP A CB  
3503 C CG  . ASP A 438 ? 0.99176 1.27553 1.22986 0.22852  0.03485  0.35309  438 ASP A CG  
3504 O OD1 . ASP A 438 ? 1.12171 1.42572 1.33155 0.25072  0.05177  0.36607  438 ASP A OD1 
3505 O OD2 . ASP A 438 ? 1.02782 1.31214 1.30414 0.21269  0.03655  0.36655  438 ASP A OD2 
3506 N N   . ALA A 439 ? 0.86672 1.06090 0.97850 0.23719  -0.02578 0.25409  439 ALA A N   
3507 C CA  . ALA A 439 ? 0.71888 0.89104 0.82061 0.23511  -0.04406 0.22937  439 ALA A CA  
3508 C C   . ALA A 439 ? 0.88286 1.05718 0.95429 0.25837  -0.03924 0.22211  439 ALA A C   
3509 O O   . ALA A 439 ? 0.93127 1.08477 0.98573 0.26042  -0.05328 0.20242  439 ALA A O   
3510 C CB  . ALA A 439 ? 0.75967 0.89004 0.81736 0.22327  -0.06285 0.20921  439 ALA A CB  
3511 N N   . LEU A 440 ? 0.80512 1.00401 0.86803 0.27714  -0.01914 0.23829  440 LEU A N   
3512 C CA  . LEU A 440 ? 0.90215 1.10587 0.93655 0.30245  -0.01187 0.23257  440 LEU A CA  
3513 C C   . LEU A 440 ? 0.88586 1.04461 0.85217 0.30781  -0.02615 0.20659  440 LEU A C   
3514 O O   . LEU A 440 ? 0.97833 1.12611 0.92991 0.32018  -0.03094 0.19300  440 LEU A O   
3515 C CB  . LEU A 440 ? 0.94485 1.17094 1.02978 0.30465  -0.01303 0.23298  440 LEU A CB  
3516 C CG  . LEU A 440 ? 0.86069 1.12955 1.02283 0.29492  -0.00138 0.25652  440 LEU A CG  
3517 C CD1 . LEU A 440 ? 0.91246 1.20355 1.12382 0.29642  -0.00602 0.25276  440 LEU A CD1 
3518 C CD2 . LEU A 440 ? 0.77635 1.07824 0.94284 0.31001  0.02499  0.28323  440 LEU A CD2 
3519 N N   . VAL A 441 ? 0.82006 0.95507 0.74869 0.29945  -0.03191 0.20100  441 VAL A N   
3520 C CA  . VAL A 441 ? 0.89084 0.98219 0.75893 0.30099  -0.04561 0.17689  441 VAL A CA  
3521 C C   . VAL A 441 ? 1.01941 1.11102 0.83730 0.31874  -0.03525 0.17641  441 VAL A C   
3522 O O   . VAL A 441 ? 0.96224 1.07310 0.78092 0.31717  -0.02626 0.19148  441 VAL A O   
3523 C CB  . VAL A 441 ? 0.91018 0.97399 0.77561 0.27600  -0.06287 0.16799  441 VAL A CB  
3524 C CG1 . VAL A 441 ? 0.98505 1.00874 0.78883 0.27699  -0.07343 0.14737  441 VAL A CG1 
3525 C CG2 . VAL A 441 ? 0.86051 0.91748 0.76169 0.26270  -0.07611 0.16129  441 VAL A CG2 
3526 N N   . ASP A 442 ? 0.92300 0.99083 0.69479 0.33557  -0.03787 0.15757  442 ASP A N   
3527 C CA  . ASP A 442 ? 0.91281 0.97647 0.63078 0.35298  -0.03128 0.15074  442 ASP A CA  
3528 C C   . ASP A 442 ? 1.11692 1.13352 0.78915 0.34207  -0.04973 0.12563  442 ASP A C   
3529 O O   . ASP A 442 ? 1.04188 1.02475 0.70187 0.34103  -0.06075 0.10781  442 ASP A O   
3530 C CB  . ASP A 442 ? 0.98262 1.05706 0.68318 0.38247  -0.01835 0.14791  442 ASP A CB  
3531 C CG  . ASP A 442 ? 1.23987 1.30869 0.88203 0.40281  -0.01290 0.13647  442 ASP A CG  
3532 O OD1 . ASP A 442 ? 1.22890 1.28758 0.84432 0.39361  -0.01979 0.13093  442 ASP A OD1 
3533 O OD2 . ASP A 442 ? 1.27117 1.34722 0.89512 0.42870  -0.00220 0.13227  442 ASP A OD2 
3534 N N   . LEU A 443 ? 1.04046 1.05640 0.68949 0.33512  -0.05243 0.12526  443 LEU A N   
3535 C CA  . LEU A 443 ? 1.01661 0.99078 0.62952 0.32112  -0.07079 0.10247  443 LEU A CA  
3536 C C   . LEU A 443 ? 1.09875 1.05578 0.65489 0.33980  -0.07128 0.08149  443 LEU A C   
3537 O O   . LEU A 443 ? 1.20600 1.13744 0.73100 0.33007  -0.08421 0.06429  443 LEU A O   
3538 C CB  . LEU A 443 ? 0.94869 0.93280 0.57353 0.30111  -0.07558 0.11306  443 LEU A CB  
3539 C CG  . LEU A 443 ? 0.99952 0.99439 0.67935 0.28081  -0.07758 0.12952  443 LEU A CG  
3540 C CD1 . LEU A 443 ? 0.96362 0.97190 0.65413 0.26557  -0.07902 0.14224  443 LEU A CD1 
3541 C CD2 . LEU A 443 ? 0.89578 0.85495 0.58129 0.26647  -0.09335 0.11382  443 LEU A CD2 
3542 N N   . LYS A 444 ? 1.13417 1.10518 0.67930 0.36580  -0.05803 0.08182  444 LYS A N   
3543 C CA  . LYS A 444 ? 1.14342 1.09581 0.63375 0.38604  -0.05877 0.05834  444 LYS A CA  
3544 C C   . LYS A 444 ? 1.11882 1.01587 0.58723 0.37479  -0.07687 0.03091  444 LYS A C   
3545 O O   . LYS A 444 ? 1.20602 1.07920 0.63202 0.37773  -0.08528 0.00802  444 LYS A O   
3546 C CB  . LYS A 444 ? 1.07849 1.04928 0.56596 0.41571  -0.04219 0.06198  444 LYS A CB  
3547 N N   . SER A 445 ? 1.16230 1.04126 0.66004 0.36299  -0.08243 0.03353  445 SER A N   
3548 C CA  . SER A 445 ? 1.24948 1.07616 0.72863 0.35447  -0.09705 0.01108  445 SER A CA  
3549 C C   . SER A 445 ? 1.18569 0.99077 0.66472 0.32606  -0.11291 0.00536  445 SER A C   
3550 O O   . SER A 445 ? 1.13287 0.89462 0.59859 0.31660  -0.12474 -0.01147 445 SER A O   
3551 C CB  . SER A 445 ? 1.06458 0.88179 0.57139 0.35677  -0.09631 0.01658  445 SER A CB  
3552 O OG  . SER A 445 ? 1.09652 0.93765 0.64933 0.33967  -0.09729 0.03670  445 SER A OG  
3553 N N   . LEU A 446 ? 1.04000 0.87518 0.53351 0.31396  -0.11208 0.01994  446 LEU A N   
3554 C CA  . LEU A 446 ? 1.00642 0.82634 0.50220 0.28752  -0.12632 0.01642  446 LEU A CA  
3555 C C   . LEU A 446 ? 1.09308 0.89096 0.54464 0.28823  -0.13542 -0.00723 446 LEU A C   
3556 O O   . LEU A 446 ? 1.25955 1.08295 0.69069 0.30055  -0.13003 -0.00717 446 LEU A O   
3557 C CB  . LEU A 446 ? 1.07121 0.92988 0.59850 0.27586  -0.12201 0.04008  446 LEU A CB  
3558 C CG  . LEU A 446 ? 1.04271 0.89065 0.57653 0.24985  -0.13528 0.03920  446 LEU A CG  
3559 C CD1 . LEU A 446 ? 1.03116 0.83818 0.56838 0.23420  -0.14811 0.02690  446 LEU A CD1 
3560 C CD2 . LEU A 446 ? 0.92477 0.80802 0.49956 0.23991  -0.12924 0.06476  446 LEU A CD2 
3561 N N   . LYS A 447 ? 1.08493 0.83863 0.52388 0.27534  -0.14884 -0.02627 447 LYS A N   
3562 C CA  . LYS A 447 ? 1.17646 0.90588 0.57597 0.27572  -0.15877 -0.05268 447 LYS A CA  
3563 C C   . LYS A 447 ? 1.12999 0.86025 0.53197 0.25143  -0.17151 -0.05433 447 LYS A C   
3564 O O   . LYS A 447 ? 1.13000 0.85795 0.50299 0.25243  -0.17906 -0.07229 447 LYS A O   
3565 C CB  . LYS A 447 ? 1.12550 0.80313 0.51016 0.27775  -0.16476 -0.07405 447 LYS A CB  
3566 C CG  . LYS A 447 ? 1.25786 0.93088 0.63160 0.30533  -0.15322 -0.07789 447 LYS A CG  
3567 C CD  . LYS A 447 ? 1.40466 1.12292 0.76888 0.32836  -0.13966 -0.06920 447 LYS A CD  
3568 C CE  . LYS A 447 ? 1.17605 0.88671 0.49536 0.34655  -0.14099 -0.09472 447 LYS A CE  
3569 N NZ  . LYS A 447 ? 1.11569 0.87544 0.42490 0.36989  -0.12654 -0.08310 447 LYS A NZ  
3570 N N   . SER A 448 ? 1.07578 0.80988 0.51086 0.23130  -0.17443 -0.03775 448 SER A N   
3571 C CA  . SER A 448 ? 0.98458 0.71762 0.42217 0.20849  -0.18670 -0.04010 448 SER A CA  
3572 C C   . SER A 448 ? 0.96955 0.71742 0.44543 0.19052  -0.18672 -0.01806 448 SER A C   
3573 O O   . SER A 448 ? 1.08830 0.82319 0.58576 0.18703  -0.18485 -0.01095 448 SER A O   
3574 C CB  . SER A 448 ? 1.08261 0.77030 0.50370 0.19613  -0.20015 -0.06403 448 SER A CB  
3575 O OG  . SER A 448 ? 1.23567 0.89643 0.67910 0.18252  -0.20272 -0.05841 448 SER A OG  
3576 N N   . ILE A 449 ? 1.01070 0.78639 0.49370 0.18138  -0.18878 -0.00808 449 ILE A N   
3577 C CA  . ILE A 449 ? 0.93378 0.71988 0.45083 0.16282  -0.19083 0.00918  449 ILE A CA  
3578 C C   . ILE A 449 ? 1.01634 0.79195 0.52529 0.14381  -0.20451 -0.00078 449 ILE A C   
3579 O O   . ILE A 449 ? 1.10315 0.89501 0.59504 0.14553  -0.20696 -0.00762 449 ILE A O   
3580 C CB  . ILE A 449 ? 0.84067 0.67099 0.38150 0.16854  -0.17942 0.03403  449 ILE A CB  
3581 C CG1 . ILE A 449 ? 0.96841 0.81290 0.52085 0.18724  -0.16519 0.04442  449 ILE A CG1 
3582 C CG2 . ILE A 449 ? 0.82830 0.66521 0.40469 0.14947  -0.18240 0.04886  449 ILE A CG2 
3583 C CD1 . ILE A 449 ? 0.83691 0.72392 0.41758 0.19242  -0.15239 0.07028  449 ILE A CD1 
3584 N N   . GLU A 450 ? 1.04423 0.79672 0.56945 0.12566  -0.21171 -0.00142 450 GLU A N   
3585 C CA  . GLU A 450 ? 0.93271 0.67521 0.45850 0.10560  -0.22231 -0.01045 450 GLU A CA  
3586 C C   . GLU A 450 ? 0.86643 0.62261 0.43024 0.08841  -0.22012 0.00614  450 GLU A C   
3587 O O   . GLU A 450 ? 0.87598 0.63614 0.46191 0.09025  -0.21414 0.01928  450 GLU A O   
3588 C CB  . GLU A 450 ? 0.95097 0.64667 0.45833 0.09960  -0.23228 -0.03067 450 GLU A CB  
3589 C CG  . GLU A 450 ? 1.06278 0.74169 0.53817 0.11465  -0.23283 -0.05162 450 GLU A CG  
3590 C CD  . GLU A 450 ? 0.97869 0.60921 0.44695 0.11054  -0.23707 -0.06734 450 GLU A CD  
3591 O OE1 . GLU A 450 ? 0.95179 0.56670 0.43436 0.11217  -0.23156 -0.05780 450 GLU A OE1 
3592 O OE2 . GLU A 450 ? 1.06195 0.67042 0.51148 0.10597  -0.24607 -0.08922 450 GLU A OE2 
3593 N N   . LEU A 451 ? 0.89410 0.65735 0.46607 0.07206  -0.22528 0.00349  451 LEU A N   
3594 C CA  . LEU A 451 ? 0.83613 0.60987 0.44192 0.05600  -0.22335 0.01629  451 LEU A CA  
3595 C C   . LEU A 451 ? 0.86751 0.60999 0.46949 0.04040  -0.23319 0.00458  451 LEU A C   
3596 O O   . LEU A 451 ? 0.81519 0.55008 0.40020 0.03535  -0.24132 -0.00974 451 LEU A O   
3597 C CB  . LEU A 451 ? 0.83346 0.64654 0.45706 0.05129  -0.21916 0.02797  451 LEU A CB  
3598 C CG  . LEU A 451 ? 0.78156 0.60316 0.43748 0.03617  -0.21729 0.03811  451 LEU A CG  
3599 C CD1 . LEU A 451 ? 0.70658 0.53842 0.38838 0.04065  -0.20835 0.05318  451 LEU A CD1 
3600 C CD2 . LEU A 451 ? 0.79817 0.65094 0.46137 0.03129  -0.21716 0.04323  451 LEU A CD2 
3601 N N   . LEU A 452 ? 0.75220 0.47994 0.37140 0.03317  -0.23218 0.01101  452 LEU A N   
3602 C CA  . LEU A 452 ? 0.79793 0.49437 0.41308 0.01917  -0.24095 0.00363  452 LEU A CA  
3603 C C   . LEU A 452 ? 0.74980 0.46560 0.38088 0.00347  -0.24318 0.00557  452 LEU A C   
3604 O O   . LEU A 452 ? 0.73979 0.48788 0.39438 0.00225  -0.23563 0.01786  452 LEU A O   
3605 C CB  . LEU A 452 ? 0.71957 0.39689 0.34507 0.01876  -0.23875 0.01097  452 LEU A CB  
3606 C CG  . LEU A 452 ? 0.77965 0.42784 0.38398 0.03339  -0.24005 0.00640  452 LEU A CG  
3607 C CD1 . LEU A 452 ? 0.75990 0.42745 0.36226 0.05130  -0.23254 0.00911  452 LEU A CD1 
3608 C CD2 . LEU A 452 ? 0.73161 0.36352 0.34669 0.03217  -0.23844 0.01403  452 LEU A CD2 
3609 N N   . GLY A 453 ? 0.77989 0.47526 0.39997 -0.00807 -0.25340 -0.00640 453 GLY A N   
3610 C CA  . GLY A 453 ? 0.79751 0.51432 0.43212 -0.02191 -0.25638 -0.00603 453 GLY A CA  
3611 C C   . GLY A 453 ? 0.84950 0.55881 0.50312 -0.03698 -0.25768 0.00215  453 GLY A C   
3612 O O   . GLY A 453 ? 0.85640 0.55914 0.52011 -0.03471 -0.25202 0.01292  453 GLY A O   
3613 N N   . ASP A 454 ? 0.75670 0.46935 0.41566 -0.05124 -0.26485 -0.00332 454 ASP A N   
3614 C CA  . ASP A 454 ? 0.82484 0.53679 0.50336 -0.06572 -0.26569 0.00640  454 ASP A CA  
3615 C C   . ASP A 454 ? 0.83750 0.50635 0.50718 -0.07328 -0.27190 0.00533  454 ASP A C   
3616 O O   . ASP A 454 ? 0.85591 0.52279 0.53821 -0.07983 -0.27026 0.01761  454 ASP A O   
3617 C CB  . ASP A 454 ? 0.92081 0.65445 0.60982 -0.07784 -0.27132 0.00146  454 ASP A CB  
3618 C CG  . ASP A 454 ? 0.92261 0.69922 0.61702 -0.06971 -0.26688 0.00286  454 ASP A CG  
3619 O OD1 . ASP A 454 ? 0.97640 0.76597 0.66751 -0.05519 -0.25866 0.00866  454 ASP A OD1 
3620 O OD2 . ASP A 454 ? 0.81234 0.61004 0.51493 -0.07786 -0.27194 -0.00122 454 ASP A OD2 
3621 N N   . LYS A 455 ? 0.90484 0.54037 0.55325 -0.07220 -0.27878 -0.00947 455 LYS A N   
3622 C CA  . LYS A 455 ? 0.86332 0.45619 0.50767 -0.07794 -0.27997 -0.01011 455 LYS A CA  
3623 C C   . LYS A 455 ? 0.89829 0.46644 0.52396 -0.06066 -0.27472 -0.01596 455 LYS A C   
3624 O O   . LYS A 455 ? 0.91163 0.48799 0.52121 -0.04951 -0.27671 -0.02630 455 LYS A O   
3625 C CB  . LYS A 455 ? 0.99546 0.56813 0.64697 -0.09648 -0.28708 -0.02201 455 LYS A CB  
3626 C CG  . LYS A 455 ? 1.09366 0.68965 0.76723 -0.11473 -0.29190 -0.01564 455 LYS A CG  
3627 C CD  . LYS A 455 ? 0.92199 0.49879 0.60845 -0.13354 -0.29779 -0.02758 455 LYS A CD  
3628 N N   . ALA A 456 ? 0.97660 0.51766 0.60445 -0.05727 -0.26758 -0.00806 456 ALA A N   
3629 C CA  . ALA A 456 ? 0.91350 0.43078 0.52535 -0.03958 -0.26193 -0.01170 456 ALA A CA  
3630 C C   . ALA A 456 ? 1.01675 0.50871 0.61251 -0.03851 -0.26677 -0.03323 456 ALA A C   
3631 O O   . ALA A 456 ? 1.04523 0.51662 0.64656 -0.05380 -0.27205 -0.04290 456 ALA A O   
3632 C CB  . ALA A 456 ? 0.84992 0.34304 0.46775 -0.03752 -0.25439 0.00127  456 ALA A CB  
3633 N N   . GLY A 457 ? 0.98966 0.48415 0.56759 -0.02066 -0.26489 -0.04089 457 GLY A N   
3634 C CA  . GLY A 457 ? 0.90107 0.37408 0.46007 -0.01555 -0.26925 -0.06341 457 GLY A CA  
3635 C C   . GLY A 457 ? 0.95522 0.45770 0.50587 -0.01837 -0.27823 -0.07654 457 GLY A C   
3636 O O   . GLY A 457 ? 1.11617 0.60895 0.64710 -0.00965 -0.28184 -0.09609 457 GLY A O   
3637 N N   . GLU A 458 ? 0.94233 0.48050 0.50617 -0.02825 -0.28154 -0.06630 458 GLU A N   
3638 C CA  . GLU A 458 ? 0.89279 0.46886 0.45270 -0.02693 -0.28599 -0.07369 458 GLU A CA  
3639 C C   . GLU A 458 ? 0.89850 0.50485 0.45173 -0.00734 -0.27737 -0.06245 458 GLU A C   
3640 O O   . GLU A 458 ? 0.89552 0.51891 0.46496 -0.00658 -0.27083 -0.04277 458 GLU A O   
3641 C CB  . GLU A 458 ? 0.86271 0.46905 0.44856 -0.04422 -0.28783 -0.06554 458 GLU A CB  
3642 C CG  . GLU A 458 ? 1.08333 0.66544 0.68196 -0.06482 -0.29515 -0.07446 458 GLU A CG  
3643 C CD  . GLU A 458 ? 1.07958 0.69508 0.70370 -0.08029 -0.29687 -0.06590 458 GLU A CD  
3644 O OE1 . GLU A 458 ? 0.93992 0.59503 0.57098 -0.07416 -0.29176 -0.05343 458 GLU A OE1 
3645 O OE2 . GLU A 458 ? 1.13540 0.73779 0.77482 -0.09796 -0.30206 -0.07129 458 GLU A OE2 
3646 N N   . TYR A 459 ? 0.94400 0.55633 0.47648 0.00833  -0.27628 -0.07467 459 TYR A N   
3647 C CA  . TYR A 459 ? 0.94972 0.59438 0.47840 0.02684  -0.26675 -0.06296 459 TYR A CA  
3648 C C   . TYR A 459 ? 1.03389 0.71850 0.55858 0.03156  -0.26606 -0.06828 459 TYR A C   
3649 O O   . TYR A 459 ? 0.93161 0.61278 0.44831 0.02538  -0.27410 -0.08714 459 TYR A O   
3650 C CB  . TYR A 459 ? 0.90612 0.52520 0.40966 0.04636  -0.26421 -0.06954 459 TYR A CB  
3651 C CG  . TYR A 459 ? 0.97562 0.55909 0.48802 0.04569  -0.25927 -0.06490 459 TYR A CG  
3652 C CD1 . TYR A 459 ? 0.86668 0.46029 0.39629 0.05094  -0.25065 -0.04491 459 TYR A CD1 
3653 C CD2 . TYR A 459 ? 0.98149 0.52193 0.48587 0.04094  -0.26309 -0.08074 459 TYR A CD2 
3654 C CE1 . TYR A 459 ? 0.92644 0.49132 0.46217 0.05269  -0.24651 -0.04038 459 TYR A CE1 
3655 C CE2 . TYR A 459 ? 0.98045 0.48943 0.49222 0.04246  -0.25736 -0.07407 459 TYR A CE2 
3656 C CZ  . TYR A 459 ? 0.94684 0.46963 0.47275 0.04911  -0.24928 -0.05362 459 TYR A CZ  
3657 O OH  . TYR A 459 ? 1.07074 0.56537 0.60163 0.05256  -0.24434 -0.04705 459 TYR A OH  
3658 N N   . GLU A 460 ? 0.98950 0.71249 0.52201 0.04176  -0.25656 -0.05149 460 GLU A N   
3659 C CA  . GLU A 460 ? 0.99143 0.75353 0.51545 0.05014  -0.25483 -0.05388 460 GLU A CA  
3660 C C   . GLU A 460 ? 0.96112 0.73911 0.47342 0.07238  -0.24420 -0.04412 460 GLU A C   
3661 O O   . GLU A 460 ? 0.89524 0.68291 0.42619 0.07500  -0.23551 -0.02387 460 GLU A O   
3662 C CB  . GLU A 460 ? 1.07778 0.87872 0.62594 0.03949  -0.25313 -0.03978 460 GLU A CB  
3663 C CG  . GLU A 460 ? 1.17313 1.01703 0.71125 0.05194  -0.24921 -0.03627 460 GLU A CG  
3664 C CD  . GLU A 460 ? 1.16159 1.03832 0.71059 0.04145  -0.25398 -0.03557 460 GLU A CD  
3665 O OE1 . GLU A 460 ? 1.31333 1.18521 0.88428 0.02470  -0.25772 -0.03268 460 GLU A OE1 
3666 O OE2 . GLU A 460 ? 1.10409 1.01208 0.63878 0.05101  -0.25373 -0.03749 460 GLU A OE2 
3667 N N   . GLN A 461 ? 1.22078 1.00310 0.70506 0.08776  -0.24467 -0.05881 461 GLN A N   
3668 C CA  . GLN A 461 ? 1.14927 0.94748 0.62049 0.11096  -0.23353 -0.04982 461 GLN A CA  
3669 C C   . GLN A 461 ? 1.09587 0.93877 0.58832 0.11366  -0.22286 -0.02280 461 GLN A C   
3670 O O   . GLN A 461 ? 1.07070 0.94004 0.57538 0.10354  -0.22477 -0.01682 461 GLN A O   
3671 C CB  . GLN A 461 ? 1.26059 1.06265 0.69877 0.12727  -0.23506 -0.07053 461 GLN A CB  
3672 C CG  . GLN A 461 ? 1.39902 1.15601 0.81389 0.13510  -0.23969 -0.09316 461 GLN A CG  
3673 C CD  . GLN A 461 ? 1.47390 1.22009 0.88383 0.15273  -0.22976 -0.08167 461 GLN A CD  
3674 O OE1 . GLN A 461 ? 1.39784 1.17695 0.81578 0.16494  -0.21785 -0.06038 461 GLN A OE1 
3675 N NE2 . GLN A 461 ? 1.53407 1.23459 0.93266 0.15426  -0.23420 -0.09481 461 GLN A NE2 
3676 N N   . VAL A 462 ? 1.03768 0.88873 0.53632 0.12767  -0.21137 -0.00577 462 VAL A N   
3677 C CA  . VAL A 462 ? 1.01851 0.90893 0.53985 0.13122  -0.20005 0.02105  462 VAL A CA  
3678 C C   . VAL A 462 ? 1.18282 1.10797 0.68610 0.14436  -0.19540 0.02207  462 VAL A C   
3679 O O   . VAL A 462 ? 1.26699 1.18820 0.73910 0.15845  -0.19661 0.00438  462 VAL A O   
3680 C CB  . VAL A 462 ? 1.05949 0.95018 0.59521 0.14302  -0.18896 0.03813  462 VAL A CB  
3681 C CG1 . VAL A 462 ? 1.15834 1.05157 0.66613 0.16802  -0.18166 0.03236  462 VAL A CG1 
3682 C CG2 . VAL A 462 ? 1.03874 0.96266 0.60791 0.14094  -0.17887 0.06645  462 VAL A CG2 
3683 N N   . SER A 463 ? 1.07145 1.03017 0.59442 0.14016  -0.19009 0.04256  463 SER A N   
3684 C CA  . SER A 463 ? 1.13722 1.12995 0.64477 0.15207  -0.18541 0.04612  463 SER A CA  
3685 C C   . SER A 463 ? 1.12857 1.13679 0.62335 0.17761  -0.17055 0.05496  463 SER A C   
3686 O O   . SER A 463 ? 1.15112 1.16884 0.61583 0.19319  -0.16968 0.04144  463 SER A O   
3687 C CB  . SER A 463 ? 0.98681 1.00767 0.52023 0.14261  -0.18221 0.06893  463 SER A CB  
3688 O OG  . SER A 463 ? 1.07263 1.08414 0.61738 0.12069  -0.19499 0.06091  463 SER A OG  
3689 N N   . ASP A 464 ? 1.10934 1.12183 0.62848 0.18260  -0.15847 0.07718  464 ASP A N   
3690 C CA  . ASP A 464 ? 1.06052 1.09343 0.57562 0.20636  -0.14157 0.09073  464 ASP A CA  
3691 C C   . ASP A 464 ? 1.08440 1.11116 0.63206 0.20542  -0.13337 0.10949  464 ASP A C   
3692 O O   . ASP A 464 ? 0.98793 1.00555 0.56585 0.18739  -0.13800 0.11833  464 ASP A O   
3693 C CB  . ASP A 464 ? 1.16536 1.23985 0.68458 0.21667  -0.12917 0.11032  464 ASP A CB  
3694 C CG  . ASP A 464 ? 1.33475 1.43474 0.85847 0.24024  -0.10839 0.12993  464 ASP A CG  
3695 O OD1 . ASP A 464 ? 1.42641 1.52499 0.92084 0.25896  -0.10521 0.11643  464 ASP A OD1 
3696 O OD2 . ASP A 464 ? 1.34250 1.46403 0.90089 0.24025  -0.09461 0.15896  464 ASP A OD2 
3697 N N   . TRP A 465 ? 1.09331 1.12596 0.63536 0.22543  -0.12162 0.11442  465 TRP A N   
3698 C CA  . TRP A 465 ? 1.07820 1.11286 0.65543 0.22687  -0.11223 0.13448  465 TRP A CA  
3699 C C   . TRP A 465 ? 0.98383 1.04760 0.56043 0.25199  -0.09267 0.15019  465 TRP A C   
3700 O O   . TRP A 465 ? 0.94071 1.01329 0.48170 0.27018  -0.08869 0.13914  465 TRP A O   
3701 C CB  . TRP A 465 ? 0.98384 0.97925 0.56037 0.21955  -0.12415 0.11841  465 TRP A CB  
3702 C CG  . TRP A 465 ? 1.07324 1.04529 0.60904 0.23355  -0.12896 0.09360  465 TRP A CG  
3703 C CD1 . TRP A 465 ? 1.10798 1.05124 0.61001 0.22778  -0.14371 0.06522  465 TRP A CD1 
3704 C CD2 . TRP A 465 ? 1.10223 1.07680 0.63553 0.25269  -0.11723 0.09349  465 TRP A CD2 
3705 N NE1 . TRP A 465 ? 1.10692 1.03167 0.58072 0.24432  -0.14298 0.04748  465 TRP A NE1 
3706 C CE2 . TRP A 465 ? 1.06093 1.00531 0.55353 0.25990  -0.12625 0.06438  465 TRP A CE2 
3707 C CE3 . TRP A 465 ? 1.05427 1.05432 0.61815 0.26439  -0.09978 0.11521  465 TRP A CE3 
3708 C CZ2 . TRP A 465 ? 1.08836 1.02671 0.56761 0.27986  -0.11809 0.05655  465 TRP A CZ2 
3709 C CZ3 . TRP A 465 ? 0.96313 0.96018 0.51461 0.28369  -0.09185 0.10798  465 TRP A CZ3 
3710 C CH2 . TRP A 465 ? 1.06102 1.02712 0.56928 0.29201  -0.10086 0.07894  465 TRP A CH2 
3711 N N   . LYS A 466 ? 0.99643 1.07643 0.61566 0.25285  -0.08015 0.17610  466 LYS A N   
3712 C CA  . LYS A 466 ? 0.93825 1.05028 0.56699 0.27506  -0.05913 0.19629  466 LYS A CA  
3713 C C   . LYS A 466 ? 0.83584 0.95028 0.51620 0.26988  -0.05189 0.21333  466 LYS A C   
3714 O O   . LYS A 466 ? 0.91524 1.02441 0.63566 0.24987  -0.05610 0.22223  466 LYS A O   
3715 C CB  . LYS A 466 ? 0.83193 0.98218 0.46964 0.28114  -0.04354 0.21799  466 LYS A CB  
3716 N N   . GLN A 467 ? 0.87808 1.00082 0.56196 0.28591  -0.04064 0.21447  467 GLN A N   
3717 C CA  . GLN A 467 ? 0.91366 1.04291 0.65230 0.28012  -0.03282 0.22728  467 GLN A CA  
3718 C C   . GLN A 467 ? 0.90231 1.07482 0.68094 0.28799  -0.01058 0.26319  467 GLN A C   
3719 O O   . GLN A 467 ? 0.96791 1.16867 0.73149 0.31127  0.00629  0.27573  467 GLN A O   
3720 C CB  . GLN A 467 ? 0.85744 0.97618 0.58445 0.29355  -0.03163 0.21194  467 GLN A CB  
3721 C CG  . GLN A 467 ? 0.86281 0.99143 0.64733 0.28801  -0.02543 0.22334  467 GLN A CG  
3722 C CD  . GLN A 467 ? 0.93622 1.05469 0.70923 0.30197  -0.02535 0.20814  467 GLN A CD  
3723 O OE1 . GLN A 467 ? 0.99672 1.12106 0.73215 0.32466  -0.01740 0.20271  467 GLN A OE1 
3724 N NE2 . GLN A 467 ? 0.85026 0.95427 0.65487 0.28991  -0.03440 0.20081  467 GLN A NE2 
3725 N N   . THR A 468 ? 0.87225 1.04972 0.70240 0.26929  -0.00984 0.28005  468 THR A N   
3726 C CA  . THR A 468 ? 0.89918 1.11318 0.78081 0.27284  0.01137  0.31492  468 THR A CA  
3727 C C   . THR A 468 ? 0.92173 1.13958 0.85849 0.26650  0.01532  0.31788  468 THR A C   
3728 O O   . THR A 468 ? 0.80967 1.00317 0.74105 0.26088  0.00141  0.29373  468 THR A O   
3729 C CB  . THR A 468 ? 0.86237 1.07964 0.77073 0.25714  0.01070  0.33216  468 THR A CB  
3730 O OG1 . THR A 468 ? 0.89446 1.08324 0.83221 0.23215  -0.00640 0.31745  468 THR A OG1 
3731 C CG2 . THR A 468 ? 0.68578 0.89945 0.54087 0.26090  0.00468  0.32369  468 THR A CG2 
3732 N N   . LYS A 469 ? 0.90635 1.15714 0.89683 0.26904  0.03509  0.34824  469 LYS A N   
3733 C CA  . LYS A 469 ? 0.92894 1.18801 0.97537 0.26349  0.03847  0.35024  469 LYS A CA  
3734 C C   . LYS A 469 ? 0.93046 1.16418 1.01397 0.23621  0.01978  0.33662  469 LYS A C   
3735 O O   . LYS A 469 ? 0.89796 1.11793 0.99283 0.23029  0.00766  0.31694  469 LYS A O   
3736 C CB  . LYS A 469 ? 0.75795 1.05977 0.85835 0.27159  0.06501  0.38716  469 LYS A CB  
3737 N N   . ASP A 470 ? 0.99523 1.22336 1.09276 0.22218  0.01725  0.34608  470 ASP A N   
3738 C CA  . ASP A 470 ? 1.02389 1.23071 1.16006 0.19732  0.00121  0.33483  470 ASP A CA  
3739 C C   . ASP A 470 ? 1.04713 1.21595 1.13667 0.18946  -0.02324 0.30092  470 ASP A C   
3740 O O   . ASP A 470 ? 1.02259 1.17499 1.13870 0.17377  -0.03759 0.28565  470 ASP A O   
3741 C CB  . ASP A 470 ? 1.03062 1.24265 1.19460 0.18696  0.00738  0.35621  470 ASP A CB  
3742 C CG  . ASP A 470 ? 1.08530 1.32215 1.32788 0.18065  0.02378  0.38294  470 ASP A CG  
3743 O OD1 . ASP A 470 ? 1.07432 1.32699 1.35160 0.18352  0.02976  0.38437  470 ASP A OD1 
3744 O OD2 . ASP A 470 ? 1.06940 1.30959 1.33996 0.17289  0.03050  0.40230  470 ASP A OD2 
3745 N N   . ALA A 471 ? 0.92478 1.08087 0.94897 0.19988  -0.02784 0.28966  471 ALA A N   
3746 C CA  . ALA A 471 ? 0.73450 0.85348 0.71872 0.19054  -0.05000 0.25986  471 ALA A CA  
3747 C C   . ALA A 471 ? 0.83837 0.94593 0.75381 0.20336  -0.05349 0.24745  471 ALA A C   
3748 O O   . ALA A 471 ? 0.94013 1.07013 0.83634 0.21972  -0.03961 0.26186  471 ALA A O   
3749 C CB  . ALA A 471 ? 0.67676 0.78187 0.68001 0.17022  -0.06055 0.25912  471 ALA A CB  
3750 N N   . LEU A 472 ? 0.79506 0.86912 0.67551 0.19675  -0.07149 0.22091  472 LEU A N   
3751 C CA  . LEU A 472 ? 0.77282 0.83161 0.59193 0.20481  -0.07792 0.20555  472 LEU A CA  
3752 C C   . LEU A 472 ? 0.83889 0.89031 0.64795 0.19108  -0.08688 0.20588  472 LEU A C   
3753 O O   . LEU A 472 ? 0.85404 0.88507 0.67687 0.17281  -0.09979 0.19701  472 LEU A O   
3754 C CB  . LEU A 472 ? 0.79517 0.82046 0.58436 0.20506  -0.09136 0.17805  472 LEU A CB  
3755 C CG  . LEU A 472 ? 0.82221 0.82069 0.55568 0.20495  -0.10377 0.15652  472 LEU A CG  
3756 C CD1 . LEU A 472 ? 0.91960 0.93479 0.61461 0.22524  -0.09462 0.15799  472 LEU A CD1 
3757 C CD2 . LEU A 472 ? 0.68867 0.65150 0.40339 0.20310  -0.11567 0.13284  472 LEU A CD2 
3758 N N   . GLU A 473 ? 0.84549 0.91625 0.63117 0.20119  -0.07969 0.21689  473 GLU A N   
3759 C CA  . GLU A 473 ? 0.85456 0.92492 0.63168 0.19094  -0.08678 0.22012  473 GLU A CA  
3760 C C   . GLU A 473 ? 0.87443 0.92225 0.59691 0.19033  -0.10249 0.19424  473 GLU A C   
3761 O O   . GLU A 473 ? 0.88776 0.93512 0.57181 0.20549  -0.10114 0.18198  473 GLU A O   
3762 C CB  . GLU A 473 ? 0.82472 0.93041 0.61196 0.20035  -0.06951 0.24537  473 GLU A CB  
3763 C CG  . GLU A 473 ? 0.73669 0.86763 0.57782 0.20470  -0.05112 0.27431  473 GLU A CG  
3764 C CD  . GLU A 473 ? 0.86976 0.99048 0.76384 0.18473  -0.05631 0.28063  473 GLU A CD  
3765 O OE1 . GLU A 473 ? 0.90594 1.00858 0.79572 0.16942  -0.06977 0.27083  473 GLU A OE1 
3766 O OE2 . GLU A 473 ? 0.82241 0.95318 0.76464 0.18301  -0.04673 0.29221  473 GLU A OE2 
3767 N N   . ILE A 474 ? 0.83713 0.86643 0.56033 0.17127  -0.11663 0.18452  474 ILE A N   
3768 C CA  . ILE A 474 ? 0.85387 0.85850 0.53797 0.16362  -0.13240 0.15827  474 ILE A CA  
3769 C C   . ILE A 474 ? 0.79644 0.80957 0.48430 0.14975  -0.13720 0.16143  474 ILE A C   
3770 O O   . ILE A 474 ? 0.78011 0.79409 0.50095 0.13703  -0.13822 0.17323  474 ILE A O   
3771 C CB  . ILE A 474 ? 0.80906 0.77715 0.49426 0.15194  -0.14580 0.14039  474 ILE A CB  
3772 C CG1 . ILE A 474 ? 0.87878 0.83619 0.55779 0.16410  -0.14108 0.13160  474 ILE A CG1 
3773 C CG2 . ILE A 474 ? 0.81810 0.76300 0.47728 0.13803  -0.16054 0.11819  474 ILE A CG2 
3774 C CD1 . ILE A 474 ? 0.75181 0.67701 0.43937 0.15285  -0.15101 0.11700  474 ILE A CD1 
3775 N N   . SER A 475 ? 0.77688 0.79679 0.43187 0.15314  -0.14050 0.15014  475 SER A N   
3776 C CA  A SER A 475 ? 0.82465 0.85396 0.47992 0.14132  -0.14642 0.15104  475 SER A CA  
3777 C CA  B SER A 475 ? 0.82368 0.85302 0.47894 0.14133  -0.14641 0.15104  475 SER A CA  
3778 C C   . SER A 475 ? 0.80207 0.80630 0.44136 0.12522  -0.16375 0.12680  475 SER A C   
3779 O O   . SER A 475 ? 0.86256 0.85561 0.46919 0.12951  -0.17025 0.10508  475 SER A O   
3780 C CB  A SER A 475 ? 0.79850 0.85555 0.43157 0.15558  -0.13907 0.15415  475 SER A CB  
3781 C CB  B SER A 475 ? 0.79905 0.85611 0.43205 0.15562  -0.13907 0.15413  475 SER A CB  
3782 O OG  A SER A 475 ? 0.91135 0.96195 0.50503 0.16684  -0.14320 0.13229  475 SER A OG  
3783 O OG  B SER A 475 ? 0.84746 0.91478 0.48246 0.14554  -0.14482 0.15610  475 SER A OG  
3784 N N   . LEU A 476 ? 0.73611 0.74118 0.39649 0.06722  -0.17893 0.17116  476 LEU A N   
3785 C CA  . LEU A 476 ? 0.73750 0.74551 0.39940 0.05549  -0.18393 0.15446  476 LEU A CA  
3786 C C   . LEU A 476 ? 0.78369 0.81781 0.42659 0.05776  -0.18857 0.14221  476 LEU A C   
3787 O O   . LEU A 476 ? 0.80485 0.83938 0.43851 0.06375  -0.19332 0.14937  476 LEU A O   
3788 C CB  . LEU A 476 ? 0.79490 0.78618 0.47556 0.05370  -0.18522 0.15732  476 LEU A CB  
3789 C CG  . LEU A 476 ? 0.74175 0.69811 0.43653 0.04687  -0.18288 0.16057  476 LEU A CG  
3790 C CD1 . LEU A 476 ? 0.63932 0.58035 0.34666 0.04308  -0.18528 0.15933  476 LEU A CD1 
3791 C CD2 . LEU A 476 ? 0.83645 0.77633 0.52222 0.03546  -0.18559 0.14626  476 LEU A CD2 
3792 N N   . PRO A 477 ? 0.91453 0.95457 0.54887 0.04422  -0.19102 0.12291  477 PRO A N   
3793 C CA  . PRO A 477 ? 0.73316 0.79190 0.34910 0.04271  -0.19601 0.10706  477 PRO A CA  
3794 C C   . PRO A 477 ? 0.77782 0.84204 0.40495 0.04587  -0.20180 0.10679  477 PRO A C   
3795 O O   . PRO A 477 ? 0.75888 0.81623 0.40685 0.05168  -0.19988 0.11993  477 PRO A O   
3796 C CB  . PRO A 477 ? 0.80350 0.86066 0.40783 0.02555  -0.19331 0.08628  477 PRO A CB  
3797 C CG  . PRO A 477 ? 0.81500 0.83484 0.43215 0.01700  -0.19315 0.08840  477 PRO A CG  
3798 C CD  . PRO A 477 ? 0.86486 0.87460 0.49773 0.02864  -0.19128 0.11083  477 PRO A CD  
3799 N N   . ALA A 478 ? 0.74262 0.82317 0.36060 0.03751  -0.20735 0.09370  478 ALA A N   
3800 C CA  . ALA A 478 ? 0.79235 0.88523 0.42331 0.03925  -0.21360 0.09476  478 ALA A CA  
3801 C C   . ALA A 478 ? 0.83050 0.91404 0.47292 0.03727  -0.21173 0.08625  478 ALA A C   
3802 O O   . ALA A 478 ? 0.78035 0.85675 0.41888 0.02104  -0.20676 0.07129  478 ALA A O   
3803 C CB  . ALA A 478 ? 0.77102 0.89849 0.39609 0.03022  -0.21499 0.08052  478 ALA A CB  
3804 N N   . LYS A 479 ? 0.74735 0.83089 0.40598 0.04549  -0.21529 0.09735  479 LYS A N   
3805 C CA  . LYS A 479 ? 0.68596 0.75394 0.35888 0.03236  -0.21385 0.09389  479 LYS A CA  
3806 C C   . LYS A 479 ? 0.75792 0.83194 0.42077 0.01428  -0.21481 0.06682  479 LYS A C   
3807 O O   . LYS A 479 ? 0.87174 0.97288 0.52822 0.01701  -0.21940 0.05508  479 LYS A O   
3808 C CB  . LYS A 479 ? 0.63802 0.70524 0.32735 0.04263  -0.21843 0.10762  479 LYS A CB  
3809 C CG  . LYS A 479 ? 0.80010 0.83047 0.49588 0.02792  -0.22028 0.10088  479 LYS A CG  
3810 C CD  . LYS A 479 ? 0.71199 0.72580 0.42310 0.03835  -0.22330 0.11740  479 LYS A CD  
3811 C CE  . LYS A 479 ? 0.82060 0.86743 0.53782 0.04967  -0.23138 0.11865  479 LYS A CE  
3812 N NZ  . LYS A 479 ? 0.88158 0.90665 0.61860 0.06158  -0.22848 0.13308  479 LYS A NZ  
3813 N N   . PRO A 480 ? 0.72610 0.76447 0.38574 -0.00342 -0.21146 0.05583  480 PRO A N   
3814 C CA  . PRO A 480 ? 0.72412 0.76214 0.37533 -0.02106 -0.20910 0.03053  480 PRO A CA  
3815 C C   . PRO A 480 ? 0.73023 0.77178 0.39208 -0.02516 -0.21345 0.02545  480 PRO A C   
3816 O O   . PRO A 480 ? 0.72251 0.77601 0.39526 -0.01179 -0.21959 0.04086  480 PRO A O   
3817 C CB  . PRO A 480 ? 0.72731 0.71879 0.37209 -0.03340 -0.20454 0.02716  480 PRO A CB  
3818 C CG  . PRO A 480 ? 0.69842 0.66290 0.35521 -0.02471 -0.20758 0.04850  480 PRO A CG  
3819 C CD  . PRO A 480 ? 0.80633 0.80188 0.47017 -0.00509 -0.20926 0.06700  480 PRO A CD  
3820 N N   . ALA A 481 ? 0.76398 0.79515 0.42244 -0.04295 -0.20920 0.00393  481 ALA A N   
3821 C CA  . ALA A 481 ? 0.62349 0.65795 0.29141 -0.04968 -0.21189 -0.00449 481 ALA A CA  
3822 C C   . ALA A 481 ? 0.66967 0.66875 0.34597 -0.04750 -0.21689 0.01247  481 ALA A C   
3823 O O   . ALA A 481 ? 0.83727 0.80190 0.51134 -0.04720 -0.21529 0.02344  481 ALA A O   
3824 C CB  . ALA A 481 ? 0.62483 0.64673 0.28890 -0.06919 -0.20283 -0.02884 481 ALA A CB  
3825 N N   . GLU A 482 ? 0.65166 0.65989 0.33730 -0.04509 -0.22347 0.01392  482 GLU A N   
3826 C CA  . GLU A 482 ? 0.63940 0.61198 0.33232 -0.04143 -0.22926 0.03017  482 GLU A CA  
3827 C C   . GLU A 482 ? 0.76875 0.69529 0.45761 -0.06073 -0.22339 0.02185  482 GLU A C   
3828 O O   . GLU A 482 ? 0.68634 0.61224 0.37184 -0.07738 -0.21571 0.00115  482 GLU A O   
3829 C CB  . GLU A 482 ? 0.61801 0.60980 0.32939 -0.03498 -0.23066 0.02814  482 GLU A CB  
3830 C CG  . GLU A 482 ? 0.85909 0.82612 0.59201 -0.02091 -0.22620 0.04744  482 GLU A CG  
3831 C CD  . GLU A 482 ? 1.00538 0.98224 0.74575 0.00452  -0.22596 0.07332  482 GLU A CD  
3832 O OE1 . GLU A 482 ? 0.91423 0.92782 0.64739 0.01453  -0.23004 0.07609  482 GLU A OE1 
3833 O OE2 . GLU A 482 ? 1.13058 1.07816 0.88214 0.01250  -0.22119 0.09023  482 GLU A OE2 
3834 N N   . SER A 483 ? 0.82984 0.72155 0.52133 -0.05723 -0.22562 0.03874  483 SER A N   
3835 C CA  . SER A 483 ? 0.74566 0.59637 0.43441 -0.07383 -0.22192 0.03404  483 SER A CA  
3836 C C   . SER A 483 ? 0.66031 0.48379 0.35722 -0.06816 -0.22594 0.05344  483 SER A C   
3837 O O   . SER A 483 ? 0.79769 0.63249 0.50814 -0.04895 -0.22346 0.07116  483 SER A O   
3838 C CB  . SER A 483 ? 0.71641 0.55627 0.39662 -0.07821 -0.21501 0.02984  483 SER A CB  
3839 O OG  . SER A 483 ? 0.80076 0.65042 0.48124 -0.06210 -0.21592 0.04468  483 SER A OG  
3840 N N   . LEU A 484 ? 0.67322 0.46379 0.36896 -0.08458 -0.22554 0.04914  484 LEU A N   
3841 C CA  . LEU A 484 ? 0.71657 0.48441 0.42869 -0.08218 -0.22150 0.06358  484 LEU A CA  
3842 C C   . LEU A 484 ? 0.67706 0.43643 0.38870 -0.07246 -0.22221 0.08118  484 LEU A C   
3843 O O   . LEU A 484 ? 0.66077 0.40952 0.38685 -0.06675 -0.21763 0.09553  484 LEU A O   
3844 C CB  . LEU A 484 ? 0.62365 0.36297 0.33140 -0.10521 -0.22170 0.05224  484 LEU A CB  
3845 C CG  . LEU A 484 ? 0.73472 0.48162 0.44438 -0.11697 -0.21928 0.03375  484 LEU A CG  
3846 C CD1 . LEU A 484 ? 0.67845 0.39925 0.38244 -0.13990 -0.21546 0.02314  484 LEU A CD1 
3847 C CD2 . LEU A 484 ? 0.61829 0.37533 0.35285 -0.10367 -0.21160 0.04027  484 LEU A CD2 
3848 N N   . ALA A 485 ? 0.68515 0.45202 0.38656 -0.07071 -0.22228 0.07724  485 ALA A N   
3849 C CA  . ALA A 485 ? 0.63175 0.39992 0.34045 -0.05953 -0.21752 0.08987  485 ALA A CA  
3850 C C   . ALA A 485 ? 0.68024 0.46823 0.37987 -0.05324 -0.21488 0.08305  485 ALA A C   
3851 O O   . ALA A 485 ? 0.70068 0.49513 0.38850 -0.06124 -0.21543 0.06722  485 ALA A O   
3852 C CB  . ALA A 485 ? 0.67724 0.41878 0.38907 -0.07003 -0.21729 0.09161  485 ALA A CB  
3853 N N   . TYR A 486 ? 0.65950 0.45674 0.36462 -0.04088 -0.21074 0.09383  486 TYR A N   
3854 C CA  . TYR A 486 ? 0.69071 0.50761 0.38512 -0.03423 -0.20862 0.08900  486 TYR A CA  
3855 C C   . TYR A 486 ? 0.69951 0.50192 0.39310 -0.03335 -0.20667 0.09193  486 TYR A C   
3856 O O   . TYR A 486 ? 0.70560 0.50268 0.41346 -0.02883 -0.20429 0.10423  486 TYR A O   
3857 C CB  . TYR A 486 ? 0.61934 0.46947 0.31837 -0.01840 -0.20659 0.09907  486 TYR A CB  
3858 C CG  . TYR A 486 ? 0.70907 0.57436 0.40957 -0.01744 -0.21044 0.09657  486 TYR A CG  
3859 C CD1 . TYR A 486 ? 0.73624 0.59261 0.44933 -0.01312 -0.21164 0.10831  486 TYR A CD1 
3860 C CD2 . TYR A 486 ? 0.72345 0.61235 0.41283 -0.02127 -0.21261 0.08160  486 TYR A CD2 
3861 C CE1 . TYR A 486 ? 0.72729 0.59662 0.44142 -0.01029 -0.21687 0.10665  486 TYR A CE1 
3862 C CE2 . TYR A 486 ? 0.67186 0.57965 0.36415 -0.01967 -0.21705 0.07831  486 TYR A CE2 
3863 C CZ  . TYR A 486 ? 0.73425 0.63167 0.43861 -0.01311 -0.22034 0.09145  486 TYR A CZ  
3864 O OH  . TYR A 486 ? 0.63123 0.54670 0.33859 -0.00952 -0.22636 0.08877  486 TYR A OH  
3865 N N   . VAL A 487 ? 0.68000 0.47694 0.35679 -0.03748 -0.20726 0.08051  487 VAL A N   
3866 C CA  . VAL A 487 ? 0.68685 0.46514 0.36061 -0.03624 -0.20752 0.08260  487 VAL A CA  
3867 C C   . VAL A 487 ? 0.71012 0.50385 0.37443 -0.02530 -0.20516 0.08469  487 VAL A C   
3868 O O   . VAL A 487 ? 0.69493 0.50027 0.34246 -0.02691 -0.20449 0.07446  487 VAL A O   
3869 C CB  . VAL A 487 ? 0.70238 0.44966 0.36129 -0.05001 -0.21093 0.06972  487 VAL A CB  
3870 C CG1 . VAL A 487 ? 0.83122 0.55829 0.48559 -0.04634 -0.21302 0.07279  487 VAL A CG1 
3871 C CG2 . VAL A 487 ? 0.69944 0.43197 0.36551 -0.06269 -0.21315 0.06745  487 VAL A CG2 
3872 N N   . LEU A 488 ? 0.68182 0.47672 0.35629 -0.01608 -0.20349 0.09650  488 LEU A N   
3873 C CA  . LEU A 488 ? 0.73129 0.53691 0.39449 -0.00638 -0.20189 0.09861  488 LEU A CA  
3874 C C   . LEU A 488 ? 0.80291 0.58102 0.45525 -0.00681 -0.20557 0.09421  488 LEU A C   
3875 O O   . LEU A 488 ? 0.76810 0.53248 0.43511 -0.00815 -0.20734 0.09935  488 LEU A O   
3876 C CB  . LEU A 488 ? 0.63977 0.46665 0.32026 0.00485  -0.19716 0.11552  488 LEU A CB  
3877 C CG  . LEU A 488 ? 0.69608 0.55145 0.38018 0.01038  -0.19337 0.12228  488 LEU A CG  
3878 C CD1 . LEU A 488 ? 0.63024 0.49643 0.33165 0.01891  -0.18788 0.14019  488 LEU A CD1 
3879 C CD2 . LEU A 488 ? 0.67759 0.55247 0.34032 0.01338  -0.19331 0.11569  488 LEU A CD2 
3880 N N   . LYS A 489 ? 0.83999 0.61033 0.46594 -0.00555 -0.20665 0.08472  489 LYS A N   
3881 C CA  . LYS A 489 ? 0.77962 0.51945 0.38945 -0.00253 -0.21067 0.08103  489 LYS A CA  
3882 C C   . LYS A 489 ? 0.85823 0.61241 0.46798 0.01120  -0.20552 0.08532  489 LYS A C   
3883 O O   . LYS A 489 ? 0.79004 0.56130 0.38709 0.01204  -0.19893 0.07765  489 LYS A O   
3884 C CB  . LYS A 489 ? 0.87214 0.58486 0.44963 -0.01329 -0.21225 0.06312  489 LYS A CB  
3885 C CG  . LYS A 489 ? 0.89125 0.57257 0.45481 -0.00786 -0.21071 0.05721  489 LYS A CG  
3886 C CD  . LYS A 489 ? 0.87369 0.52600 0.40464 -0.02084 -0.20858 0.03828  489 LYS A CD  
3887 C CE  . LYS A 489 ? 0.94287 0.55973 0.45994 -0.01343 -0.20472 0.03276  489 LYS A CE  
3888 N NZ  . LYS A 489 ? 0.93623 0.51893 0.41792 -0.02794 -0.20105 0.01419  489 LYS A NZ  
3889 N N   . LEU A 490 ? 0.85229 0.60537 0.48093 0.02082  -0.20586 0.09586  490 LEU A N   
3890 C CA  . LEU A 490 ? 0.84921 0.61987 0.48618 0.03381  -0.19776 0.09863  490 LEU A CA  
3891 C C   . LEU A 490 ? 0.85090 0.59546 0.48021 0.04077  -0.19640 0.08971  490 LEU A C   
3892 O O   . LEU A 490 ? 0.87741 0.60632 0.51807 0.04455  -0.20262 0.09564  490 LEU A O   
3893 C CB  . LEU A 490 ? 0.73664 0.52824 0.40150 0.03966  -0.19782 0.11592  490 LEU A CB  
3894 C CG  . LEU A 490 ? 0.76862 0.58330 0.44295 0.03586  -0.19705 0.12809  490 LEU A CG  
3895 C CD1 . LEU A 490 ? 0.67493 0.47997 0.35603 0.02463  -0.20121 0.12843  490 LEU A CD1 
3896 C CD2 . LEU A 490 ? 0.77579 0.61001 0.47317 0.04210  -0.19281 0.14235  490 LEU A CD2 
3897 N N   . THR A 491 ? 0.91091 0.65038 0.52008 0.04239  -0.18812 0.07548  491 THR A N   
3898 C CA  . THR A 491 ? 0.88786 0.59911 0.48733 0.05077  -0.18428 0.06605  491 THR A CA  
3899 C C   . THR A 491 ? 0.87488 0.60774 0.49201 0.06688  -0.17568 0.06953  491 THR A C   
3900 O O   . THR A 491 ? 0.99117 0.74955 0.60502 0.06764  -0.16608 0.06542  491 THR A O   
3901 C CB  . THR A 491 ? 0.90627 0.59607 0.47217 0.04190  -0.17775 0.04647  491 THR A CB  
3902 O OG1 . THR A 491 ? 1.04126 0.71621 0.59198 0.02526  -0.18519 0.04244  491 THR A OG1 
3903 C CG2 . THR A 491 ? 0.93125 0.58332 0.48496 0.05117  -0.17293 0.03730  491 THR A CG2 
3904 N N   . PHE A 492 ? 0.95054 0.67594 0.58635 0.07920  -0.17926 0.07692  492 PHE A N   
3905 C CA  . PHE A 492 ? 0.98362 0.73019 0.63986 0.09555  -0.17162 0.07963  492 PHE A CA  
3906 C C   . PHE A 492 ? 1.11674 0.83467 0.76121 0.10833  -0.16485 0.06702  492 PHE A C   
3907 O O   . PHE A 492 ? 1.14364 0.82113 0.76461 0.10458  -0.16743 0.05865  492 PHE A O   
3908 C CB  . PHE A 492 ? 0.85793 0.62145 0.54585 0.10158  -0.17979 0.09595  492 PHE A CB  
3909 C CG  . PHE A 492 ? 0.90399 0.69876 0.60679 0.09183  -0.18165 0.10844  492 PHE A CG  
3910 C CD1 . PHE A 492 ? 1.01453 0.84557 0.73278 0.09604  -0.17251 0.11327  492 PHE A CD1 
3911 C CD2 . PHE A 492 ? 0.88427 0.67006 0.58466 0.07823  -0.19149 0.11520  492 PHE A CD2 
3912 C CE1 . PHE A 492 ? 0.92735 0.78176 0.65642 0.08717  -0.17314 0.12571  492 PHE A CE1 
3913 C CE2 . PHE A 492 ? 1.00205 0.81186 0.71524 0.07043  -0.19175 0.12677  492 PHE A CE2 
3914 C CZ  . PHE A 492 ? 0.94413 0.78656 0.67079 0.07509  -0.18259 0.13262  492 PHE A CZ  
3915 N N   . ASP A 493 ? 1.22078 0.95836 0.88034 0.12321  -0.15475 0.06491  493 ASP A N   
3916 C CA  . ASP A 493 ? 1.24948 0.95930 0.90129 0.13891  -0.14685 0.05327  493 ASP A CA  
3917 C C   . ASP A 493 ? 1.31045 1.03710 0.99600 0.15862  -0.14997 0.06363  493 ASP A C   
3918 O O   . ASP A 493 ? 1.23775 1.00673 0.94726 0.16314  -0.14431 0.06818  493 ASP A O   
3919 C CB  . ASP A 493 ? 1.28602 1.00370 0.92362 0.13995  -0.12903 0.03692  493 ASP A CB  
3920 C CG  . ASP A 493 ? 1.40934 1.08744 1.03056 0.15255  -0.11898 0.02170  493 ASP A CG  
3921 O OD1 . ASP A 493 ? 1.56518 1.21097 1.18852 0.16381  -0.12652 0.02614  493 ASP A OD1 
3922 O OD2 . ASP A 493 ? 1.22387 0.90269 0.82888 0.15066  -0.10338 0.00567  493 ASP A OD2 
3923 N N   . GLY A 494 ? 1.75175 1.44765 1.43821 0.16948  -0.15874 0.06736  494 GLY A N   
3924 C CA  . GLY A 494 ? 1.73631 1.45455 1.45728 0.18841  -0.16395 0.07841  494 GLY A CA  
3925 C C   . GLY A 494 ? 1.66180 1.40041 1.40199 0.17904  -0.17961 0.09547  494 GLY A C   
3926 O O   . GLY A 494 ? 1.67988 1.45543 1.45279 0.18832  -0.18210 0.10466  494 GLY A O   
3927 N N   . GLY A 495 ? 1.16852 0.88716 0.88968 0.15965  -0.18853 0.09833  495 GLY A N   
3928 C CA  . GLY A 495 ? 1.17749 0.91059 0.91553 0.15038  -0.20287 0.11337  495 GLY A CA  
3929 C C   . GLY A 495 ? 1.05382 0.82480 0.80578 0.13581  -0.20061 0.11975  495 GLY A C   
3930 O O   . GLY A 495 ? 0.99699 0.79217 0.75267 0.13724  -0.18835 0.11523  495 GLY A O   
3931 N N   . ILE A 496 ? 0.96865 0.74276 0.72697 0.12215  -0.21169 0.13019  496 ILE A N   
3932 C CA  . ILE A 496 ? 0.86564 0.66846 0.63424 0.10732  -0.20913 0.13711  496 ILE A CA  
3933 C C   . ILE A 496 ? 0.85153 0.69671 0.65340 0.11414  -0.20608 0.14548  496 ILE A C   
3934 O O   . ILE A 496 ? 0.95820 0.81003 0.77755 0.12139  -0.21421 0.15098  496 ILE A O   
3935 C CB  . ILE A 496 ? 0.87787 0.66464 0.63940 0.08926  -0.22021 0.14313  496 ILE A CB  
3936 C CG1 . ILE A 496 ? 0.94282 0.69008 0.67199 0.08142  -0.22289 0.13347  496 ILE A CG1 
3937 C CG2 . ILE A 496 ? 0.87756 0.68936 0.65001 0.07580  -0.21672 0.15103  496 ILE A CG2 
3938 C CD1 . ILE A 496 ? 0.82971 0.56041 0.55178 0.06376  -0.23329 0.13757  496 ILE A CD1 
3939 N N   . PRO A 497 ? 0.81205 0.68732 0.62232 0.11149  -0.19474 0.14666  497 PRO A N   
3940 C CA  . PRO A 497 ? 0.85750 0.77407 0.69793 0.11470  -0.19030 0.15364  497 PRO A CA  
3941 C C   . PRO A 497 ? 0.86109 0.78673 0.71771 0.10266  -0.20027 0.16492  497 PRO A C   
3942 O O   . PRO A 497 ? 0.92709 0.83175 0.77140 0.08806  -0.20714 0.16859  497 PRO A O   
3943 C CB  . PRO A 497 ? 0.81416 0.75075 0.65033 0.10771  -0.17712 0.15406  497 PRO A CB  
3944 C CG  . PRO A 497 ? 0.85362 0.76544 0.66058 0.10889  -0.17319 0.14379  497 PRO A CG  
3945 C CD  . PRO A 497 ? 0.86279 0.73626 0.65313 0.10479  -0.18535 0.14147  497 PRO A CD  
3946 N N   . VAL A 498 ? 0.84291 0.80232 0.72784 0.10810  -0.20034 0.16926  498 VAL A N   
3947 C CA  . VAL A 498 ? 0.81904 0.79325 0.72147 0.09611  -0.20905 0.17858  498 VAL A CA  
3948 C C   . VAL A 498 ? 0.90154 0.90039 0.81283 0.07970  -0.19896 0.18470  498 VAL A C   
3949 O O   . VAL A 498 ? 1.04237 1.07622 0.97117 0.08397  -0.18877 0.18437  498 VAL A O   
3950 C CB  . VAL A 498 ? 0.77096 0.77221 0.69955 0.11024  -0.21541 0.17981  498 VAL A CB  
3951 C CG1 . VAL A 498 ? 0.86334 0.87685 0.80543 0.09578  -0.22682 0.18845  498 VAL A CG1 
3952 C CG2 . VAL A 498 ? 1.01818 0.99226 0.93594 0.13109  -0.22184 0.17389  498 VAL A CG2 
3953 N N   . PRO A 499 ? 0.85054 0.83171 0.75015 0.06134  -0.20040 0.19003  499 PRO A N   
3954 C CA  . PRO A 499 ? 0.89362 0.89140 0.79834 0.04649  -0.18955 0.19681  499 PRO A CA  
3955 C C   . PRO A 499 ? 0.87574 0.90415 0.80558 0.03542  -0.18984 0.20226  499 PRO A C   
3956 O O   . PRO A 499 ? 0.75751 0.78869 0.69748 0.03331  -0.20143 0.20286  499 PRO A O   
3957 C CB  . PRO A 499 ? 0.85023 0.81395 0.73371 0.03324  -0.19202 0.19987  499 PRO A CB  
3958 C CG  . PRO A 499 ? 0.95746 0.89667 0.83433 0.03362  -0.20661 0.19638  499 PRO A CG  
3959 C CD  . PRO A 499 ? 0.82982 0.77238 0.70912 0.05360  -0.21071 0.18946  499 PRO A CD  
3960 N N   . GLN A 500 ? 0.95869 1.01119 0.89696 0.02696  -0.17650 0.20624  500 GLN A N   
3961 C CA  . GLN A 500 ? 0.95655 1.03993 0.91674 0.01227  -0.17353 0.21039  500 GLN A CA  
3962 C C   . GLN A 500 ? 0.96677 1.02919 0.91646 -0.01063 -0.16943 0.21759  500 GLN A C   
3963 O O   . GLN A 500 ? 0.95096 1.00101 0.88654 -0.01538 -0.15803 0.22211  500 GLN A O   
3964 C CB  . GLN A 500 ? 0.88715 1.01032 0.86271 0.01525  -0.15958 0.20917  500 GLN A CB  
3965 C CG  . GLN A 500 ? 0.94633 1.10665 0.94518 -0.00159 -0.15499 0.21170  500 GLN A CG  
3966 C CD  . GLN A 500 ? 0.87204 1.06230 0.89581 0.00577  -0.16767 0.20780  500 GLN A CD  
3967 O OE1 . GLN A 500 ? 0.78180 0.97329 0.80972 0.02837  -0.17612 0.20289  500 GLN A OE1 
3968 N NE2 . GLN A 500 ? 0.91430 1.12865 0.95390 -0.01337 -0.16882 0.21015  500 GLN A NE2 
3969 N N   . PRO A 501 ? 0.88313 0.94001 0.83802 -0.02485 -0.17781 0.21903  501 PRO A N   
3970 C CA  . PRO A 501 ? 1.04632 1.07977 0.99088 -0.04668 -0.17216 0.22452  501 PRO A CA  
3971 C C   . PRO A 501 ? 1.06677 1.12002 1.01872 -0.06182 -0.15554 0.22943  501 PRO A C   
3972 O O   . PRO A 501 ? 1.15013 1.24349 1.12130 -0.06191 -0.15098 0.22752  501 PRO A O   
3973 C CB  . PRO A 501 ? 0.98720 1.01880 0.93882 -0.05892 -0.18469 0.22276  501 PRO A CB  
3974 C CG  . PRO A 501 ? 0.81788 0.85814 0.77508 -0.03944 -0.19962 0.21792  501 PRO A CG  
3975 C CD  . PRO A 501 ? 0.81081 0.88003 0.77910 -0.02105 -0.19308 0.21581  501 PRO A CD  
3976 N N   . LYS A 502 ? 1.05563 1.08033 0.99217 -0.07536 -0.14577 0.23573  502 LYS A N   
3977 C CA  . LYS A 502 ? 1.07163 1.10757 1.01089 -0.09268 -0.12833 0.24143  502 LYS A CA  
3978 C C   . LYS A 502 ? 1.05775 1.11991 1.01656 -0.11311 -0.12884 0.23807  502 LYS A C   
3979 O O   . LYS A 502 ? 1.02965 1.12750 1.00262 -0.12099 -0.11933 0.23734  502 LYS A O   
3980 C CB  . LYS A 502 ? 0.92348 0.91707 0.84071 -0.10136 -0.11854 0.24985  502 LYS A CB  
3981 N N   . ILE A 503 ? 1.12494 1.17242 1.08402 -0.12222 -0.13970 0.23526  503 ILE A N   
3982 C CA  . ILE A 503 ? 1.10242 1.17728 1.07902 -0.14350 -0.14199 0.23134  503 ILE A CA  
3983 C C   . ILE A 503 ? 1.07685 1.16523 1.06339 -0.13272 -0.16291 0.22613  503 ILE A C   
3984 O O   . ILE A 503 ? 1.09235 1.15194 1.06822 -0.13872 -0.17191 0.22502  503 ILE A O   
3985 C CB  . ILE A 503 ? 1.15322 1.19668 1.11838 -0.17064 -0.13263 0.23323  503 ILE A CB  
3986 N N   . GLY A 504 ? 1.05302 1.18307 1.05871 -0.11701 -0.16967 0.22324  504 GLY A N   
3987 C CA  . GLY A 504 ? 1.03880 1.18071 1.05301 -0.10284 -0.18970 0.22017  504 GLY A CA  
3988 C C   . GLY A 504 ? 1.01396 1.19589 1.04739 -0.07914 -0.19278 0.21780  504 GLY A C   
3989 O O   . GLY A 504 ? 1.03934 1.25673 1.08781 -0.08321 -0.18046 0.21686  504 GLY A O   
3990 N N   . ALA A 505 ? 0.84922 1.14044 1.30478 0.00528  -0.17189 -0.05188 505 ALA A N   
3991 C CA  . ALA A 505 ? 0.71894 1.06747 1.20967 0.03600  -0.16239 -0.05089 505 ALA A CA  
3992 C C   . ALA A 505 ? 0.69595 0.98842 1.13601 0.07029  -0.15267 -0.05746 505 ALA A C   
3993 O O   . ALA A 505 ? 0.67021 0.89032 1.05132 0.06697  -0.15698 -0.05903 505 ALA A O   
3994 C CB  . ALA A 505 ? 0.70723 1.12451 1.24685 0.04399  -0.18896 -0.04704 505 ALA A CB  
3995 N N   . SER A 506 ? 0.70426 1.02937 1.16673 0.10196  -0.13878 -0.06092 506 SER A N   
3996 C CA  . SER A 506 ? 0.77192 1.03450 1.18655 0.13260  -0.12693 -0.06936 506 SER A CA  
3997 C C   . SER A 506 ? 0.84551 1.13831 1.29237 0.17867  -0.13169 -0.06911 506 SER A C   
3998 O O   . SER A 506 ? 0.84490 1.21919 1.35065 0.19128  -0.12215 -0.06775 506 SER A O   
3999 C CB  . SER A 506 ? 0.76704 1.01690 1.15904 0.12349  -0.09142 -0.07871 506 SER A CB  
4000 O OG  . SER A 506 ? 0.82058 1.15178 1.26666 0.12856  -0.07160 -0.08176 506 SER A OG  
4001 N N   . VAL A 507 ? 0.86195 1.09147 1.27082 0.20565  -0.14429 -0.06674 507 VAL A N   
4002 C CA  . VAL A 507 ? 0.79583 1.04564 1.23457 0.25725  -0.14892 -0.05980 507 VAL A CA  
4003 C C   . VAL A 507 ? 0.79400 0.95978 1.18765 0.28778  -0.12295 -0.07297 507 VAL A C   
4004 O O   . VAL A 507 ? 0.92816 1.01288 1.25780 0.26489  -0.11755 -0.08027 507 VAL A O   
4005 C CB  . VAL A 507 ? 0.82741 1.07743 1.26401 0.26478  -0.18758 -0.04010 507 VAL A CB  
4006 C CG1 . VAL A 507 ? 0.70428 1.03536 1.18153 0.23029  -0.21386 -0.03227 507 VAL A CG1 
4007 C CG2 . VAL A 507 ? 0.78312 0.93473 1.14445 0.25262  -0.19768 -0.03897 507 VAL A CG2 
4008 N N   . PHE A 508 ? 0.84469 1.02974 1.27023 0.33766  -0.10656 -0.07539 508 PHE A N   
4009 C CA  . PHE A 508 ? 0.97758 1.07047 1.35730 0.36749  -0.07727 -0.09412 508 PHE A CA  
4010 C C   . PHE A 508 ? 1.09103 1.17638 1.49866 0.43449  -0.07745 -0.08078 508 PHE A C   
4011 O O   . PHE A 508 ? 0.99054 1.17879 1.46977 0.46315  -0.08326 -0.06499 508 PHE A O   
4012 C CB  . PHE A 508 ? 0.96773 1.08649 1.35100 0.36060  -0.03816 -0.12223 508 PHE A CB  
4013 C CG  . PHE A 508 ? 1.01707 1.17012 1.39061 0.30054  -0.03499 -0.12743 508 PHE A CG  
4014 C CD1 . PHE A 508 ? 0.98479 1.24469 1.41946 0.27928  -0.04441 -0.11443 508 PHE A CD1 
4015 C CD2 . PHE A 508 ? 0.99512 1.07659 1.30023 0.26443  -0.02216 -0.14150 508 PHE A CD2 
4016 C CE1 . PHE A 508 ? 0.90121 1.18657 1.32981 0.22812  -0.03941 -0.11414 508 PHE A CE1 
4017 C CE2 . PHE A 508 ? 0.94272 1.06358 1.24412 0.21460  -0.01762 -0.13920 508 PHE A CE2 
4018 C CZ  . PHE A 508 ? 0.90623 1.12451 1.26991 0.19905  -0.02526 -0.12497 508 PHE A CZ  
4019 N N   . SER A 509 ? 1.10770 1.07703 1.46211 0.45827  -0.07067 -0.08338 509 SER A N   
4020 C CA  . SER A 509 ? 1.03984 0.98580 1.41852 0.52899  -0.06591 -0.06725 509 SER A CA  
4021 C C   . SER A 509 ? 1.22402 1.15803 1.61185 0.57062  -0.01941 -0.09723 509 SER A C   
4022 O O   . SER A 509 ? 1.36072 1.17672 1.70105 0.59623  0.00394  -0.11095 509 SER A O   
4023 C CB  . SER A 509 ? 1.05731 0.87857 1.37613 0.53566  -0.07808 -0.05369 509 SER A CB  
4024 O OG  . SER A 509 ? 1.39881 1.19447 1.74129 0.59208  -0.06613 -0.03098 509 SER A OG  
4025 N N   . ALA A 510 ? 1.13677 1.18802 1.58117 0.57196  -0.00501 -0.10594 510 ALA A N   
4026 C CA  . ALA A 510 ? 1.18608 1.23939 1.63633 0.60958  0.04267  -0.13828 510 ALA A CA  
4027 C C   . ALA A 510 ? 1.17281 1.38973 1.70612 0.61290  0.04817  -0.12726 510 ALA A C   
4028 O O   . ALA A 510 ? 1.07217 1.38440 1.64905 0.58136  0.01336  -0.10272 510 ALA A O   
4029 C CB  . ALA A 510 ? 1.12228 1.09348 1.49589 0.56261  0.06808  -0.18089 510 ALA A CB  
4030 N N   . THR A 511 ? 1.19113 1.43529 1.74238 0.64239  0.09020  -0.14412 511 THR A N   
4031 C CA  . THR A 511 ? 1.04278 1.44661 1.67558 0.64258  0.09410  -0.12618 511 THR A CA  
4032 C C   . THR A 511 ? 1.06676 1.54410 1.70097 0.58972  0.09526  -0.14439 511 THR A C   
4033 O O   . THR A 511 ? 0.98759 1.59580 1.68559 0.57169  0.09149  -0.12408 511 THR A O   
4034 C CB  . THR A 511 ? 1.03897 1.45515 1.69554 0.69307  0.13569  -0.13561 511 THR A CB  
4035 N N   . SER A 512 ? 1.09510 1.48380 1.65844 0.55403  0.10061  -0.17673 512 SER A N   
4036 C CA  . SER A 512 ? 0.94793 1.39462 1.50626 0.48731  0.10451  -0.18580 512 SER A CA  
4037 C C   . SER A 512 ? 0.91620 1.28017 1.41623 0.42486  0.07786  -0.18222 512 SER A C   
4038 O O   . SER A 512 ? 0.96105 1.23029 1.42584 0.43395  0.05699  -0.17426 512 SER A O   
4039 C CB  . SER A 512 ? 0.88573 1.32792 1.41117 0.49336  0.15206  -0.22611 512 SER A CB  
4040 O OG  . SER A 512 ? 1.10918 1.40057 1.54780 0.50189  0.16976  -0.25974 512 SER A OG  
4041 N N   . ALA A 513 ? 0.89212 1.29653 1.38423 0.36660  0.08068  -0.18458 513 ALA A N   
4042 C CA  . ALA A 513 ? 0.93783 1.27150 1.37468 0.31100  0.06139  -0.17974 513 ALA A CA  
4043 C C   . ALA A 513 ? 1.05444 1.28038 1.40599 0.30406  0.08604  -0.21214 513 ALA A C   
4044 O O   . ALA A 513 ? 1.07898 1.31555 1.39808 0.25873  0.10073  -0.22238 513 ALA A O   
4045 C CB  . ALA A 513 ? 0.87411 1.29211 1.33805 0.25774  0.05911  -0.16569 513 ALA A CB  
4046 N N   . THR A 514 ? 1.11313 1.24201 1.43127 0.34643  0.09016  -0.22501 514 THR A N   
4047 C CA  . THR A 514 ? 1.04676 1.05672 1.27712 0.33566  0.11203  -0.25791 514 THR A CA  
4048 C C   . THR A 514 ? 1.18346 1.07408 1.37540 0.35240  0.08967  -0.24624 514 THR A C   
4049 O O   . THR A 514 ? 1.26090 1.16863 1.50012 0.39247  0.06818  -0.22005 514 THR A O   
4050 C CB  . THR A 514 ? 1.04345 1.05089 1.26519 0.37393  0.15618  -0.29744 514 THR A CB  
4051 O OG1 . THR A 514 ? 1.08251 1.21968 1.34604 0.35548  0.17332  -0.30064 514 THR A OG1 
4052 C CG2 . THR A 514 ? 1.07058 0.95168 1.19537 0.35477  0.17976  -0.33752 514 THR A CG2 
4053 N N   . GLY A 515 ? 1.31140 1.09537 1.42133 0.31778  0.09273  -0.26089 515 GLY A N   
4054 C CA  . GLY A 515 ? 1.46249 1.12815 1.53110 0.33030  0.07322  -0.24770 515 GLY A CA  
4055 C C   . GLY A 515 ? 1.38006 1.06407 1.45637 0.30170  0.03212  -0.20815 515 GLY A C   
4056 O O   . GLY A 515 ? 1.35447 1.12565 1.45639 0.26559  0.02216  -0.19618 515 GLY A O   
4057 N N   . ARG A 516 ? 1.36831 0.97354 1.42478 0.32075  0.01045  -0.18742 516 ARG A N   
4058 C CA  . ARG A 516 ? 1.42521 1.04334 1.47940 0.29486  -0.02768 -0.15196 516 ARG A CA  
4059 C C   . ARG A 516 ? 1.29364 1.03566 1.42209 0.29885  -0.04580 -0.13409 516 ARG A C   
4060 O O   . ARG A 516 ? 1.24851 1.05033 1.43806 0.34169  -0.04078 -0.13367 516 ARG A O   
4061 C CB  . ARG A 516 ? 1.37089 0.90687 1.40803 0.32687  -0.04786 -0.12802 516 ARG A CB  
4062 C CG  . ARG A 516 ? 1.47244 1.02469 1.50212 0.30329  -0.08603 -0.09296 516 ARG A CG  
4063 C CD  . ARG A 516 ? 1.52235 1.04789 1.49019 0.24133  -0.08750 -0.09428 516 ARG A CD  
4064 N NE  . ARG A 516 ? 1.43488 0.98077 1.39395 0.22312  -0.11979 -0.06326 516 ARG A NE  
4065 C CZ  . ARG A 516 ? 1.30286 0.83757 1.21346 0.17652  -0.12497 -0.05458 516 ARG A CZ  
4066 N NH1 . ARG A 516 ? 1.27767 0.78613 1.14615 0.13959  -0.10273 -0.07132 516 ARG A NH1 
4067 N NH2 . ARG A 516 ? 1.23124 0.78756 1.13436 0.16716  -0.15159 -0.02854 516 ARG A NH2 
4068 N N   . GLY A 517 ? 1.06460 0.84268 1.18601 0.25445  -0.06420 -0.11998 517 GLY A N   
4069 C CA  . GLY A 517 ? 0.98837 0.86801 1.17108 0.24899  -0.08225 -0.10559 517 GLY A CA  
4070 C C   . GLY A 517 ? 1.01017 0.88373 1.16645 0.21364  -0.10800 -0.08673 517 GLY A C   
4071 O O   . GLY A 517 ? 1.05734 0.86407 1.15122 0.19032  -0.10712 -0.08411 517 GLY A O   
4072 N N   . VAL A 518 ? 0.90457 0.84487 1.10398 0.20949  -0.13012 -0.07422 518 VAL A N   
4073 C CA  . VAL A 518 ? 0.80842 0.74206 0.97971 0.17713  -0.15054 -0.06161 518 VAL A CA  
4074 C C   . VAL A 518 ? 0.76460 0.76828 0.97649 0.14988  -0.14738 -0.06449 518 VAL A C   
4075 O O   . VAL A 518 ? 0.81086 0.88126 1.08275 0.16075  -0.15111 -0.06593 518 VAL A O   
4076 C CB  . VAL A 518 ? 0.81168 0.73582 0.97739 0.19421  -0.18441 -0.04399 518 VAL A CB  
4077 C CG1 . VAL A 518 ? 0.76810 0.69331 0.90552 0.16316  -0.20224 -0.03706 518 VAL A CG1 
4078 C CG2 . VAL A 518 ? 0.91821 0.76575 1.04230 0.21874  -0.18669 -0.03445 518 VAL A CG2 
4079 N N   . SER A 519 ? 0.72835 0.71837 0.90978 0.11630  -0.13882 -0.06199 519 SER A N   
4080 C CA  . SER A 519 ? 0.73585 0.77779 0.95232 0.08979  -0.13348 -0.06054 519 SER A CA  
4081 C C   . SER A 519 ? 0.78271 0.81765 0.99149 0.07928  -0.15953 -0.05489 519 SER A C   
4082 O O   . SER A 519 ? 0.82406 0.80935 0.97898 0.07722  -0.16762 -0.04906 519 SER A O   
4083 C CB  . SER A 519 ? 0.66531 0.70090 0.85711 0.06431  -0.10683 -0.05687 519 SER A CB  
4084 O OG  . SER A 519 ? 0.66483 0.69965 0.84820 0.06965  -0.08408 -0.06671 519 SER A OG  
4085 N N   . LEU A 520 ? 0.69644 0.78187 0.95507 0.07104  -0.17217 -0.05741 520 LEU A N   
4086 C CA  . LEU A 520 ? 0.75464 0.83064 1.00069 0.05806  -0.19866 -0.05882 520 LEU A CA  
4087 C C   . LEU A 520 ? 0.76516 0.85900 1.03760 0.02580  -0.19312 -0.06183 520 LEU A C   
4088 O O   . LEU A 520 ? 0.81114 0.95974 1.14029 0.01670  -0.18583 -0.06038 520 LEU A O   
4089 C CB  . LEU A 520 ? 0.77915 0.89437 1.05337 0.07616  -0.22781 -0.05819 520 LEU A CB  
4090 C CG  . LEU A 520 ? 0.67196 0.76379 0.92479 0.11269  -0.23412 -0.05006 520 LEU A CG  
4091 C CD1 . LEU A 520 ? 0.63486 0.78863 0.93431 0.13336  -0.25878 -0.04248 520 LEU A CD1 
4092 C CD2 . LEU A 520 ? 0.81422 0.84482 0.99864 0.11032  -0.24577 -0.04522 520 LEU A CD2 
4093 N N   . GLY A 521 ? 0.82374 0.87019 1.05490 0.01066  -0.19401 -0.06439 521 GLY A N   
4094 C CA  . GLY A 521 ? 0.80567 0.84751 1.05452 -0.01839 -0.18822 -0.06808 521 GLY A CA  
4095 C C   . GLY A 521 ? 0.90057 0.94275 1.14824 -0.03478 -0.21923 -0.08415 521 GLY A C   
4096 O O   . GLY A 521 ? 0.89663 0.97558 1.15509 -0.02447 -0.24496 -0.08657 521 GLY A O   
4097 N N   . LEU A 522 ? 0.94015 0.94580 1.17848 -0.06105 -0.21588 -0.09377 522 LEU A N   
4098 C CA  . LEU A 522 ? 1.00742 1.00961 1.23992 -0.08772 -0.24526 -0.11488 522 LEU A CA  
4099 C C   . LEU A 522 ? 0.97550 0.95452 1.14611 -0.07341 -0.26737 -0.12670 522 LEU A C   
4100 O O   . LEU A 522 ? 1.09370 1.01710 1.20836 -0.05841 -0.25263 -0.12745 522 LEU A O   
4101 C CB  . LEU A 522 ? 1.04761 0.99266 1.27252 -0.11811 -0.23172 -0.12601 522 LEU A CB  
4102 C CG  . LEU A 522 ? 1.04057 1.00880 1.32920 -0.14067 -0.21354 -0.11093 522 LEU A CG  
4103 C CD1 . LEU A 522 ? 0.85860 0.74930 1.13168 -0.16452 -0.19629 -0.11816 522 LEU A CD1 
4104 C CD2 . LEU A 522 ? 1.00824 1.06129 1.36220 -0.16349 -0.23629 -0.10767 522 LEU A CD2 
4105 N N   . GLY A 523 ? 1.02955 1.06115 1.21307 -0.07702 -0.30122 -0.13067 523 GLY A N   
4106 C CA  . GLY A 523 ? 1.06102 1.08140 1.18699 -0.06782 -0.32540 -0.13895 523 GLY A CA  
4107 C C   . GLY A 523 ? 1.02119 1.12110 1.17733 -0.06208 -0.35980 -0.12906 523 GLY A C   
4108 O O   . GLY A 523 ? 0.96183 1.12688 1.18446 -0.07022 -0.36588 -0.12035 523 GLY A O   
4109 N N   . ASP A 524 ? 1.07392 1.17626 1.18423 -0.04806 -0.38132 -0.12674 524 ASP A N   
4110 C CA  . ASP A 524 ? 0.98094 1.16383 1.12079 -0.03362 -0.41304 -0.10739 524 ASP A CA  
4111 C C   . ASP A 524 ? 0.92351 1.08762 1.04696 0.01319  -0.40418 -0.08157 524 ASP A C   
4112 O O   . ASP A 524 ? 0.89770 1.00272 0.95843 0.02065  -0.39560 -0.08369 524 ASP A O   
4113 C CB  . ASP A 524 ? 1.11364 1.32892 1.21937 -0.06222 -0.45008 -0.12145 524 ASP A CB  
4114 C CG  . ASP A 524 ? 1.14926 1.36813 1.25912 -0.11713 -0.46021 -0.15215 524 ASP A CG  
4115 O OD1 . ASP A 524 ? 1.12112 1.39676 1.29782 -0.13504 -0.46479 -0.14573 524 ASP A OD1 
4116 O OD2 . ASP A 524 ? 1.24414 1.40826 1.28831 -0.14223 -0.46285 -0.18240 524 ASP A OD2 
4117 N N   . PHE A 525 ? 0.90697 1.11768 1.08460 0.04295  -0.40420 -0.05805 525 PHE A N   
4118 C CA  . PHE A 525 ? 0.86466 1.04167 1.02675 0.08560  -0.39268 -0.03516 525 PHE A CA  
4119 C C   . PHE A 525 ? 0.80794 1.04494 0.99224 0.11383  -0.42125 -0.00708 525 PHE A C   
4120 O O   . PHE A 525 ? 0.68705 0.98557 0.93610 0.13280  -0.42297 0.00651  525 PHE A O   
4121 C CB  . PHE A 525 ? 0.80606 0.95787 0.99941 0.10036  -0.35671 -0.03512 525 PHE A CB  
4122 C CG  . PHE A 525 ? 0.78529 0.90176 0.96985 0.07007  -0.33203 -0.05580 525 PHE A CG  
4123 C CD1 . PHE A 525 ? 0.85707 0.90522 0.98089 0.06262  -0.31667 -0.06144 525 PHE A CD1 
4124 C CD2 . PHE A 525 ? 0.83494 0.99284 1.07437 0.04982  -0.32412 -0.06448 525 PHE A CD2 
4125 C CE1 . PHE A 525 ? 0.91218 0.93168 1.03200 0.04024  -0.29233 -0.07400 525 PHE A CE1 
4126 C CE2 . PHE A 525 ? 0.88954 1.01349 1.12340 0.02374  -0.30100 -0.07717 525 PHE A CE2 
4127 C CZ  . PHE A 525 ? 0.91040 0.96422 1.08529 0.02121  -0.28456 -0.08127 525 PHE A CZ  
4128 N N   . SER A 526 ? 0.91113 1.13625 1.04367 0.11805  -0.44173 0.00450  526 SER A N   
4129 C CA  . SER A 526 ? 0.80357 1.08531 0.95284 0.14727  -0.46964 0.03963  526 SER A CA  
4130 C C   . SER A 526 ? 0.92909 1.17431 1.10076 0.19663  -0.44959 0.06602  526 SER A C   
4131 O O   . SER A 526 ? 0.95382 1.12712 1.11249 0.20013  -0.41730 0.05305  526 SER A O   
4132 C CB  . SER A 526 ? 0.90216 1.17326 0.98343 0.13496  -0.48206 0.04714  526 SER A CB  
4133 O OG  . SER A 526 ? 0.93254 1.13280 0.97566 0.15995  -0.46489 0.06657  526 SER A OG  
4134 N N   . GLU A 527 ? 0.93387 1.22450 1.13147 0.22824  -0.45782 0.10286  527 GLU A N   
4135 C CA  . GLU A 527 ? 0.91851 1.15940 1.13182 0.27708  -0.43536 0.12736  527 GLU A CA  
4136 C C   . GLU A 527 ? 0.86951 1.01032 1.01163 0.27354  -0.42406 0.13004  527 GLU A C   
4137 O O   . GLU A 527 ? 0.93158 0.99474 1.06653 0.29359  -0.40032 0.12827  527 GLU A O   
4138 C CB  . GLU A 527 ? 0.90217 1.21234 1.15476 0.31128  -0.44366 0.17256  527 GLU A CB  
4139 N N   . GLU A 528 ? 0.84655 0.99507 0.93648 0.24581  -0.43898 0.13336  528 GLU A N   
4140 C CA  . GLU A 528 ? 0.87455 0.94162 0.89806 0.23714  -0.42589 0.13752  528 GLU A CA  
4141 C C   . GLU A 528 ? 0.85492 0.85596 0.86150 0.22335  -0.40713 0.10502  528 GLU A C   
4142 O O   . GLU A 528 ? 0.83669 0.76286 0.81607 0.23048  -0.38790 0.11162  528 GLU A O   
4143 C CB  . GLU A 528 ? 0.92760 1.02653 0.89967 0.20766  -0.44011 0.13929  528 GLU A CB  
4144 C CG  . GLU A 528 ? 0.92768 0.96774 0.84122 0.20234  -0.42548 0.15501  528 GLU A CG  
4145 C CD  . GLU A 528 ? 1.07683 1.16261 0.94515 0.18083  -0.43556 0.16167  528 GLU A CD  
4146 O OE1 . GLU A 528 ? 1.05459 1.19500 0.91910 0.15994  -0.45114 0.13876  528 GLU A OE1 
4147 O OE2 . GLU A 528 ? 1.09473 1.16297 0.93133 0.18371  -0.42704 0.18841  528 GLU A OE2 
4148 N N   . PHE A 529 ? 0.90376 0.93602 0.92736 0.20026  -0.41005 0.07308  529 PHE A N   
4149 C CA  . PHE A 529 ? 0.86716 0.84816 0.87503 0.17946  -0.37721 0.04647  529 PHE A CA  
4150 C C   . PHE A 529 ? 0.85569 0.80580 0.89808 0.20193  -0.35097 0.04742  529 PHE A C   
4151 O O   . PHE A 529 ? 0.85392 0.73855 0.86343 0.19937  -0.32840 0.04726  529 PHE A O   
4152 C CB  . PHE A 529 ? 0.81306 0.83151 0.83879 0.14815  -0.37599 0.01549  529 PHE A CB  
4153 C CG  . PHE A 529 ? 0.71210 0.68800 0.72379 0.12694  -0.34378 -0.00575 529 PHE A CG  
4154 C CD1 . PHE A 529 ? 0.75408 0.71718 0.80002 0.13324  -0.31630 -0.01013 529 PHE A CD1 
4155 C CD2 . PHE A 529 ? 0.80254 0.75694 0.76710 0.10271  -0.33968 -0.01992 529 PHE A CD2 
4156 C CE1 . PHE A 529 ? 0.80109 0.73798 0.83630 0.11315  -0.28829 -0.02315 529 PHE A CE1 
4157 C CE2 . PHE A 529 ? 0.70873 0.63137 0.66579 0.08804  -0.30926 -0.03184 529 PHE A CE2 
4158 C CZ  . PHE A 529 ? 0.81179 0.72973 0.80552 0.09184  -0.28503 -0.03109 529 PHE A CZ  
4159 N N   . LEU A 530 ? 0.85190 0.85416 0.95818 0.22286  -0.35386 0.04856  530 LEU A N   
4160 C CA  . LEU A 530 ? 0.91220 0.88942 1.05036 0.24627  -0.32488 0.04334  530 LEU A CA  
4161 C C   . LEU A 530 ? 0.95066 0.85113 1.05857 0.27528  -0.31699 0.06335  530 LEU A C   
4162 O O   . LEU A 530 ? 0.94335 0.78229 1.03625 0.27711  -0.28811 0.05118  530 LEU A O   
4163 C CB  . LEU A 530 ? 0.83686 0.89638 1.05169 0.26907  -0.32920 0.04543  530 LEU A CB  
4164 C CG  . LEU A 530 ? 0.73428 0.86864 0.98346 0.23447  -0.33726 0.02693  530 LEU A CG  
4165 C CD1 . LEU A 530 ? 0.70558 0.93364 1.03299 0.25639  -0.34313 0.03612  530 LEU A CD1 
4166 C CD2 . LEU A 530 ? 0.65175 0.75190 0.88770 0.20397  -0.30810 0.00039  530 LEU A CD2 
4167 N N   . THR A 531 ? 0.93042 0.83227 1.02636 0.29487  -0.34269 0.09494  531 THR A N   
4168 C CA  . THR A 531 ? 0.95637 0.77624 1.02280 0.32052  -0.33672 0.11888  531 THR A CA  
4169 C C   . THR A 531 ? 1.02579 0.76740 1.02046 0.28642  -0.32547 0.11387  531 THR A C   
4170 O O   . THR A 531 ? 1.05238 0.71173 1.02237 0.29034  -0.30389 0.11229  531 THR A O   
4171 C CB  . THR A 531 ? 0.98261 0.84204 1.05530 0.33579  -0.35358 0.15883  531 THR A CB  
4172 O OG1 . THR A 531 ? 0.93914 0.88405 1.08106 0.36520  -0.36032 0.16905  531 THR A OG1 
4173 C CG2 . THR A 531 ? 1.01485 0.79025 1.06159 0.35487  -0.33774 0.18580  531 THR A CG2 
4174 N N   . GLU A 532 ? 0.97636 0.74367 0.93485 0.25181  -0.33865 0.11090  532 GLU A N   
4175 C CA  . GLU A 532 ? 1.02667 0.73804 0.92195 0.22019  -0.32642 0.10997  532 GLU A CA  
4176 C C   . GLU A 532 ? 1.00769 0.69714 0.90392 0.19938  -0.29367 0.07992  532 GLU A C   
4177 O O   . GLU A 532 ? 0.93927 0.57526 0.78979 0.17763  -0.27841 0.08230  532 GLU A O   
4178 C CB  . GLU A 532 ? 0.90063 0.65335 0.75985 0.19426  -0.34241 0.11277  532 GLU A CB  
4179 C CG  . GLU A 532 ? 0.94238 0.65783 0.74020 0.16774  -0.32957 0.12712  532 GLU A CG  
4180 C CD  . GLU A 532 ? 0.85647 0.62052 0.62487 0.14448  -0.33028 0.12216  532 GLU A CD  
4181 O OE1 . GLU A 532 ? 0.87249 0.65628 0.64457 0.13511  -0.32839 0.09706  532 GLU A OE1 
4182 O OE2 . GLU A 532 ? 0.88425 0.66621 0.62733 0.13772  -0.33085 0.14334  532 GLU A OE2 
4183 N N   . ALA A 533 ? 1.03014 0.76780 0.97782 0.20244  -0.28362 0.05519  533 ALA A N   
4184 C CA  . ALA A 533 ? 0.98038 0.70744 0.93417 0.18484  -0.25234 0.03066  533 ALA A CA  
4185 C C   . ALA A 533 ? 1.03878 0.70641 0.99099 0.20132  -0.23099 0.02547  533 ALA A C   
4186 O O   . ALA A 533 ? 0.97669 0.62169 0.91176 0.17961  -0.20526 0.00848  533 ALA A O   
4187 C CB  . ALA A 533 ? 0.93147 0.73025 0.94324 0.18269  -0.24843 0.01024  533 ALA A CB  
4188 N N   . GLY A 534 ? 1.12681 0.76882 1.09484 0.23954  -0.23989 0.03989  534 GLY A N   
4189 C CA  . GLY A 534 ? 1.20690 0.77490 1.16699 0.25974  -0.21738 0.03242  534 GLY A CA  
4190 C C   . GLY A 534 ? 1.18226 0.78194 1.20617 0.30590  -0.20681 0.02264  534 GLY A C   
4191 O O   . GLY A 534 ? 1.11464 0.66013 1.13614 0.32457  -0.17982 0.00529  534 GLY A O   
4192 N N   . LEU A 535 ? 1.03450 0.72725 1.11467 0.32236  -0.22611 0.03154  535 LEU A N   
4193 C CA  . LEU A 535 ? 0.93215 0.67888 1.08151 0.36761  -0.21762 0.02876  535 LEU A CA  
4194 C C   . LEU A 535 ? 1.11740 0.94389 1.31055 0.39056  -0.25188 0.05994  535 LEU A C   
4195 O O   . LEU A 535 ? 0.99689 0.90614 1.21250 0.36341  -0.26997 0.05631  535 LEU A O   
4196 C CB  . LEU A 535 ? 0.84781 0.66090 1.03331 0.34880  -0.19800 -0.00092 535 LEU A CB  
4197 C CG  . LEU A 535 ? 1.03131 0.86782 1.26570 0.39034  -0.17018 -0.01502 535 LEU A CG  
4198 C CD1 . LEU A 535 ? 1.23898 0.97535 1.42545 0.39268  -0.13491 -0.04030 535 LEU A CD1 
4199 C CD2 . LEU A 535 ? 0.96973 0.91257 1.25912 0.37326  -0.16400 -0.02948 535 LEU A CD2 
4200 N N   . LYS A 536 ? 1.15943 0.96177 1.36329 0.43668  -0.25910 0.09058  536 LYS A N   
4201 C CA  . LYS A 536 ? 1.09149 0.98791 1.33807 0.45129  -0.28383 0.12612  536 LYS A CA  
4202 C C   . LYS A 536 ? 1.16634 1.17798 1.48811 0.46389  -0.28473 0.11786  536 LYS A C   
4203 O O   . LYS A 536 ? 1.10126 1.11314 1.45590 0.49062  -0.25480 0.10056  536 LYS A O   
4204 C CB  . LYS A 536 ? 1.05415 0.91458 1.30839 0.49188  -0.27327 0.16542  536 LYS A CB  
4205 N N   . PRO A 537 ? 1.12267 1.23674 1.47053 0.44114  -0.31701 0.12911  537 PRO A N   
4206 C CA  . PRO A 537 ? 0.99741 1.22543 1.41435 0.43883  -0.31982 0.12027  537 PRO A CA  
4207 C C   . PRO A 537 ? 1.16590 1.45382 1.65005 0.48878  -0.30154 0.14696  537 PRO A C   
4208 O O   . PRO A 537 ? 1.06349 1.42914 1.60358 0.49197  -0.29059 0.13635  537 PRO A O   
4209 C CB  . PRO A 537 ? 1.02608 1.33432 1.44133 0.39636  -0.36055 0.12942  537 PRO A CB  
4210 C CG  . PRO A 537 ? 1.15346 1.41953 1.51915 0.39936  -0.37542 0.15886  537 PRO A CG  
4211 C CD  . PRO A 537 ? 1.04083 1.17401 1.35248 0.41136  -0.35076 0.14892  537 PRO A CD  
4212 N N   . ASP A 538 ? 1.36914 1.62416 1.85602 0.52494  -0.29778 0.18339  538 ASP A N   
4213 C CA  . ASP A 538 ? 1.37224 1.66819 1.93075 0.57174  -0.28470 0.20483  538 ASP A CA  
4214 C C   . ASP A 538 ? 1.37610 1.59046 1.93277 0.60924  -0.23621 0.17901  538 ASP A C   
4215 O O   . ASP A 538 ? 1.43188 1.65959 2.03613 0.65378  -0.22106 0.18842  538 ASP A O   
4216 C CB  . ASP A 538 ? 1.44043 1.72587 2.00619 0.59373  -0.30933 0.24578  538 ASP A CB  
4217 C CG  . ASP A 538 ? 1.47161 1.62975 1.97234 0.59431  -0.29962 0.25644  538 ASP A CG  
4218 O OD1 . ASP A 538 ? 1.50465 1.58321 1.94149 0.57383  -0.27840 0.22659  538 ASP A OD1 
4219 O OD2 . ASP A 538 ? 1.51747 1.65147 2.02169 0.61417  -0.31828 0.28819  538 ASP A OD2 
4220 N N   . THR A 539 ? 1.24402 1.37212 1.74060 0.59068  -0.21479 0.14050  539 THR A N   
4221 C CA  . THR A 539 ? 1.20984 1.26302 1.69565 0.61580  -0.16936 0.10743  539 THR A CA  
4222 C C   . THR A 539 ? 1.10257 1.20059 1.59429 0.59255  -0.15612 0.06625  539 THR A C   
4223 O O   . THR A 539 ? 1.21006 1.24739 1.68020 0.60303  -0.11924 0.03189  539 THR A O   
4224 C CB  . THR A 539 ? 1.20653 1.10286 1.61216 0.61031  -0.15467 0.09523  539 THR A CB  
4225 O OG1 . THR A 539 ? 1.18691 1.05247 1.53242 0.55918  -0.17995 0.08297  539 THR A OG1 
4226 C CG2 . THR A 539 ? 1.20250 1.05235 1.61457 0.63815  -0.16122 0.13701  539 THR A CG2 
4227 N N   . ILE A 540 ? 1.01046 1.21288 1.53119 0.55710  -0.18542 0.06775  540 ILE A N   
4228 C CA  . ILE A 540 ? 1.01416 1.26931 1.55278 0.52908  -0.17624 0.03349  540 ILE A CA  
4229 C C   . ILE A 540 ? 1.05874 1.42044 1.67163 0.55547  -0.15325 0.04077  540 ILE A C   
4230 O O   . ILE A 540 ? 0.97671 1.41938 1.64377 0.57152  -0.16734 0.07577  540 ILE A O   
4231 C CB  . ILE A 540 ? 0.93580 1.24109 1.46816 0.46176  -0.21045 0.03450  540 ILE A CB  
4232 C CG1 . ILE A 540 ? 0.98234 1.18295 1.43518 0.42906  -0.22551 0.03159  540 ILE A CG1 
4233 C CG2 . ILE A 540 ? 0.86302 1.21596 1.41290 0.41894  -0.19380 0.00842  540 ILE A CG2 
4234 C CD1 . ILE A 540 ? 0.75627 0.98932 1.19343 0.36806  -0.25296 0.02734  540 ILE A CD1 
4235 N N   . ARG A 541 ? 1.15251 1.51848 1.76942 0.55624  -0.11905 0.00781  541 ARG A N   
4236 C CA  . ARG A 541 ? 1.15477 1.62474 1.83910 0.57537  -0.09532 0.01316  541 ARG A CA  
4237 C C   . ARG A 541 ? 1.12395 1.66971 1.82982 0.53650  -0.08472 -0.00977 541 ARG A C   
4238 O O   . ARG A 541 ? 1.04850 1.68721 1.80916 0.54419  -0.06645 -0.00328 541 ARG A O   
4239 C CB  . ARG A 541 ? 1.13794 1.54139 1.81417 0.63151  -0.05115 0.00129  541 ARG A CB  
4240 C CG  . ARG A 541 ? 1.15861 1.51306 1.83983 0.67304  -0.05977 0.03144  541 ARG A CG  
4241 C CD  . ARG A 541 ? 1.26490 1.52789 1.92856 0.72330  -0.01599 0.01147  541 ARG A CD  
4242 N NE  . ARG A 541 ? 1.36606 1.48903 1.94603 0.70987  0.00701  -0.02705 541 ARG A NE  
4243 C CZ  . ARG A 541 ? 1.46340 1.48030 2.00820 0.73864  0.04510  -0.05488 541 ARG A CZ  
4244 N NH1 . ARG A 541 ? 1.47889 1.50953 2.06579 0.78986  0.06624  -0.05012 541 ARG A NH1 
4245 N NH2 . ARG A 541 ? 1.55922 1.45312 2.02191 0.71265  0.06064  -0.09062 541 ARG A NH2 
4246 N N   . PHE A 542 ? 1.01955 1.82686 1.55987 0.34538  -0.13409 0.13722  542 PHE A N   
4247 C CA  . PHE A 542 ? 0.96777 1.79480 1.50054 0.32465  -0.10665 0.12412  542 PHE A CA  
4248 C C   . PHE A 542 ? 0.96253 1.76291 1.45051 0.28397  -0.10909 0.12904  542 PHE A C   
4249 O O   . PHE A 542 ? 0.99083 1.73494 1.43802 0.27673  -0.12015 0.13471  542 PHE A O   
4250 C CB  . PHE A 542 ? 0.97524 1.76868 1.49017 0.34410  -0.08262 0.10530  542 PHE A CB  
4251 C CG  . PHE A 542 ? 1.00451 1.82882 1.51727 0.33258  -0.05262 0.09449  542 PHE A CG  
4252 C CD1 . PHE A 542 ? 0.95723 1.84656 1.51675 0.34973  -0.03486 0.08932  542 PHE A CD1 
4253 C CD2 . PHE A 542 ? 1.07581 1.86430 1.54091 0.30559  -0.04094 0.09106  542 PHE A CD2 
4254 C CE1 . PHE A 542 ? 0.95594 1.87282 1.51035 0.33894  -0.00370 0.08361  542 PHE A CE1 
4255 C CE2 . PHE A 542 ? 1.08787 1.90096 1.54725 0.29582  -0.01344 0.08542  542 PHE A CE2 
4256 C CZ  . PHE A 542 ? 1.01292 1.88964 1.51478 0.31196  0.00640  0.08301  542 PHE A CZ  
4257 N N   . ILE A 543 ? 0.82394 1.66647 1.32454 0.25737  -0.09868 0.12751  543 ILE A N   
4258 C CA  . ILE A 543 ? 0.89302 1.70970 1.35436 0.21867  -0.09975 0.12879  543 ILE A CA  
4259 C C   . ILE A 543 ? 0.89437 1.72280 1.35430 0.20201  -0.07084 0.12041  543 ILE A C   
4260 O O   . ILE A 543 ? 0.89106 1.77918 1.39646 0.20225  -0.05835 0.12094  543 ILE A O   
4261 C CB  . ILE A 543 ? 0.80519 1.65604 1.28151 0.19736  -0.12508 0.13800  543 ILE A CB  
4262 C CG1 . ILE A 543 ? 0.74054 1.58464 1.21602 0.21755  -0.15464 0.15011  543 ILE A CG1 
4263 C CG2 . ILE A 543 ? 0.59105 1.41172 1.02655 0.16003  -0.12585 0.13527  543 ILE A CG2 
4264 C CD1 . ILE A 543 ? 0.63306 1.51250 1.11792 0.20052  -0.18414 0.15749  543 ILE A CD1 
4265 N N   . ARG A 544 ? 0.88240 1.65609 1.29392 0.18886  -0.06039 0.11442  544 ARG A N   
4266 C CA  . ARG A 544 ? 0.90247 1.67918 1.30450 0.17476  -0.03411 0.10948  544 ARG A CA  
4267 C C   . ARG A 544 ? 0.90122 1.66025 1.28332 0.13606  -0.03963 0.11212  544 ARG A C   
4268 O O   . ARG A 544 ? 0.88316 1.59278 1.22896 0.12824  -0.05280 0.10992  544 ARG A O   
4269 C CB  . ARG A 544 ? 0.91831 1.64739 1.28251 0.19484  -0.01906 0.09805  544 ARG A CB  
4270 C CG  . ARG A 544 ? 0.92231 1.64594 1.26429 0.18287  0.00544  0.09533  544 ARG A CG  
4271 C CD  . ARG A 544 ? 0.88647 1.57404 1.19554 0.21171  0.01633  0.08128  544 ARG A CD  
4272 N NE  . ARG A 544 ? 0.84905 1.47554 1.13116 0.21918  -0.00220 0.07240  544 ARG A NE  
4273 C CZ  . ARG A 544 ? 0.85606 1.44369 1.11369 0.24328  -0.00065 0.05672  544 ARG A CZ  
4274 N NH1 . ARG A 544 ? 0.87035 1.47434 1.12046 0.26575  0.01746  0.04705  544 ARG A NH1 
4275 N NH2 . ARG A 544 ? 0.88728 1.42096 1.12910 0.24510  -0.01682 0.04992  544 ARG A NH2 
4276 N N   . VAL A 545 ? 0.86761 1.66496 1.27565 0.11310  -0.02821 0.11629  545 VAL A N   
4277 C CA  . VAL A 545 ? 0.86036 1.64227 1.25711 0.07587  -0.03731 0.11670  545 VAL A CA  
4278 C C   . VAL A 545 ? 0.84060 1.59308 1.21245 0.06007  -0.01527 0.11610  545 VAL A C   
4279 O O   . VAL A 545 ? 0.86231 1.63710 1.24584 0.06821  0.00922  0.12077  545 VAL A O   
4280 C CB  . VAL A 545 ? 0.89180 1.73617 1.34378 0.05717  -0.04871 0.12153  545 VAL A CB  
4281 C CG1 . VAL A 545 ? 0.93268 1.76352 1.37902 0.01893  -0.05841 0.11831  545 VAL A CG1 
4282 C CG2 . VAL A 545 ? 0.89017 1.76101 1.36215 0.07474  -0.07565 0.12308  545 VAL A CG2 
4283 N N   . SER A 546 ? 0.84742 1.55119 1.18462 0.03994  -0.02353 0.11105  546 SER A N   
4284 C CA  . SER A 546 ? 0.83151 1.50507 1.14738 0.02377  -0.00642 0.11196  546 SER A CA  
4285 C C   . SER A 546 ? 0.98503 1.69235 1.33917 -0.00850 -0.00235 0.11928  546 SER A C   
4286 O O   . SER A 546 ? 1.05762 1.81053 1.45355 -0.01764 -0.01586 0.12004  546 SER A O   
4287 C CB  . SER A 546 ? 0.91979 1.52938 1.19105 0.01746  -0.01605 0.10234  546 SER A CB  
4288 O OG  . SER A 546 ? 0.80794 1.38921 1.05430 0.04551  -0.01992 0.09605  546 SER A OG  
4289 N N   . SER A 547 ? 1.01290 1.69702 1.35475 -0.02405 0.01419  0.12480  547 SER A N   
4290 C CA  . SER A 547 ? 0.99304 1.70430 1.37599 -0.05607 0.02202  0.13449  547 SER A CA  
4291 C C   . SER A 547 ? 1.12366 1.84511 1.53389 -0.08292 -0.00438 0.12480  547 SER A C   
4292 O O   . SER A 547 ? 1.13551 1.81460 1.51129 -0.08631 -0.02290 0.11147  547 SER A O   
4293 C CB  . SER A 547 ? 0.94953 1.61607 1.30413 -0.06837 0.03808  0.14189  547 SER A CB  
4294 O OG  . SER A 547 ? 0.98516 1.59169 1.30008 -0.07379 0.02141  0.12863  547 SER A OG  
4295 N N   . GLY A 548 ? 1.24602 2.02401 1.71744 -0.10041 -0.00587 0.12997  548 GLY A N   
4296 C CA  . GLY A 548 ? 1.28542 2.07459 1.78562 -0.12840 -0.03333 0.11796  548 GLY A CA  
4297 C C   . GLY A 548 ? 1.28342 2.05206 1.74717 -0.11814 -0.06288 0.10161  548 GLY A C   
4298 O O   . GLY A 548 ? 1.29380 2.04110 1.74907 -0.13962 -0.08268 0.08741  548 GLY A O   
4299 N N   . THR A 549 ? 1.13431 1.90967 1.57852 -0.08646 -0.06544 0.10363  549 THR A N   
4300 C CA  . THR A 549 ? 1.16758 1.92549 1.57772 -0.07649 -0.09199 0.09312  549 THR A CA  
4301 C C   . THR A 549 ? 1.12502 1.94329 1.57490 -0.06489 -0.11137 0.09600  549 THR A C   
4302 O O   . THR A 549 ? 1.08576 1.92287 1.54308 -0.03624 -0.10370 0.10486  549 THR A O   
4303 C CB  . THR A 549 ? 1.06000 1.76494 1.41406 -0.05198 -0.08267 0.09337  549 THR A CB  
4304 O OG1 . THR A 549 ? 1.04362 1.76420 1.40789 -0.02655 -0.06312 0.10352  549 THR A OG1 
4305 C CG2 . THR A 549 ? 1.00859 1.65470 1.32612 -0.06572 -0.07272 0.08657  549 THR A CG2 
4306 N N   . LYS A 550 ? 1.07060 1.91765 1.54645 -0.08492 -0.13774 0.08699  550 LYS A N   
4307 C CA  . LYS A 550 ? 1.06282 1.97154 1.58282 -0.07348 -0.15942 0.08969  550 LYS A CA  
4308 C C   . LYS A 550 ? 1.05660 1.94710 1.52894 -0.04873 -0.18193 0.08993  550 LYS A C   
4309 O O   . LYS A 550 ? 1.06848 1.91604 1.48660 -0.05579 -0.19469 0.08106  550 LYS A O   
4310 C CB  . LYS A 550 ? 1.05707 2.00704 1.62796 -0.10364 -0.18308 0.07839  550 LYS A CB  
4311 N N   . LEU A 551 ? 1.02398 1.94662 1.51735 -0.01922 -0.18545 0.10092  551 LEU A N   
4312 C CA  . LEU A 551 ? 1.08410 1.98779 1.53617 0.00690  -0.20475 0.10673  551 LEU A CA  
4313 C C   . LEU A 551 ? 1.12605 2.08568 1.61346 0.01283  -0.24100 0.10751  551 LEU A C   
4314 O O   . LEU A 551 ? 1.13780 2.15930 1.69621 0.01477  -0.24296 0.10919  551 LEU A O   
4315 C CB  . LEU A 551 ? 1.05909 1.94581 1.50401 0.04001  -0.18393 0.11837  551 LEU A CB  
4316 C CG  . LEU A 551 ? 1.06242 1.89558 1.44777 0.06107  -0.19021 0.12523  551 LEU A CG  
4317 C CD1 . LEU A 551 ? 0.96206 1.76371 1.33938 0.08400  -0.16351 0.12942  551 LEU A CD1 
4318 C CD2 . LEU A 551 ? 1.14978 2.00800 1.53969 0.08154  -0.22165 0.13552  551 LEU A CD2 
4319 N N   . THR A 552 ? 1.05586 1.99510 1.49381 0.01591  -0.26944 0.10632  552 THR A N   
4320 C CA  . THR A 552 ? 0.91856 1.90292 1.37466 0.02644  -0.30956 0.10836  552 THR A CA  
4321 C C   . THR A 552 ? 0.95082 1.91375 1.37183 0.06302  -0.31692 0.12768  552 THR A C   
4322 O O   . THR A 552 ? 1.03019 1.93402 1.38073 0.06803  -0.31093 0.13358  552 THR A O   
4323 C CB  . THR A 552 ? 0.87032 1.84852 1.29050 0.00329  -0.33981 0.09219  552 THR A CB  
4324 N N   . VAL A 553 ? 0.86884 1.87923 1.34381 0.08834  -0.32821 0.13797  553 VAL A N   
4325 C CA  . VAL A 553 ? 0.98110 1.97343 1.43670 0.12557  -0.33537 0.15775  553 VAL A CA  
4326 C C   . VAL A 553 ? 1.04592 2.06501 1.49234 0.13750  -0.38251 0.16504  553 VAL A C   
4327 O O   . VAL A 553 ? 1.15815 2.24076 1.66008 0.13093  -0.40907 0.15600  553 VAL A O   
4328 C CB  . VAL A 553 ? 0.91149 1.93498 1.43263 0.15083  -0.31601 0.16329  553 VAL A CB  
4329 C CG1 . VAL A 553 ? 0.94819 1.93870 1.44687 0.18881  -0.32004 0.18213  553 VAL A CG1 
4330 C CG2 . VAL A 553 ? 0.72295 1.73061 1.25430 0.13681  -0.27238 0.15366  553 VAL A CG2 
4331 N N   . TYR A 554 ? 1.01613 1.98808 1.39693 0.15737  -0.39282 0.18331  554 TYR A N   
4332 C CA  . TYR A 554 ? 1.09734 2.08529 1.45225 0.17278  -0.43853 0.19512  554 TYR A CA  
4333 C C   . TYR A 554 ? 1.10660 2.06942 1.45060 0.21211  -0.44242 0.22370  554 TYR A C   
4334 O O   . TYR A 554 ? 1.15490 2.06793 1.48313 0.22010  -0.40901 0.23190  554 TYR A O   
4335 C CB  . TYR A 554 ? 1.19774 2.14117 1.46003 0.15539  -0.44770 0.19272  554 TYR A CB  
4336 C CG  . TYR A 554 ? 1.26155 2.21702 1.52117 0.11719  -0.44761 0.16327  554 TYR A CG  
4337 C CD1 . TYR A 554 ? 1.19025 2.12569 1.46468 0.09300  -0.40908 0.14821  554 TYR A CD1 
4338 C CD2 . TYR A 554 ? 1.28482 2.26730 1.52352 0.10630  -0.48807 0.14993  554 TYR A CD2 
4339 C CE1 . TYR A 554 ? 1.17235 2.11377 1.44718 0.05858  -0.40958 0.12231  554 TYR A CE1 
4340 C CE2 . TYR A 554 ? 1.25075 2.24015 1.48969 0.07151  -0.48971 0.12036  554 TYR A CE2 
4341 C CZ  . TYR A 554 ? 1.21031 2.17803 1.46953 0.04728  -0.44958 0.10739  554 TYR A CZ  
4342 O OH  . TYR A 554 ? 1.18817 2.15841 1.45122 0.01355  -0.45170 0.07927  554 TYR A OH  
4343 N N   . SER A 555 ? 1.09970 2.09170 1.45003 0.23617  -0.48406 0.23847  555 SER A N   
4344 C CA  . SER A 555 ? 1.01111 1.97099 1.34596 0.27457  -0.49071 0.26945  555 SER A CA  
4345 C C   . SER A 555 ? 1.19125 2.09418 1.42316 0.27423  -0.50179 0.28937  555 SER A C   
4346 O O   . SER A 555 ? 1.15402 2.01081 1.35496 0.29957  -0.49943 0.31878  555 SER A O   
4347 C CB  . SER A 555 ? 1.01028 2.02126 1.40678 0.30250  -0.52669 0.27572  555 SER A CB  
4348 N N   . THR A 556 ? 1.34590 2.25328 1.52938 0.24657  -0.51301 0.27324  556 THR A N   
4349 C CA  . THR A 556 ? 1.42528 2.27985 1.50257 0.24398  -0.51804 0.28913  556 THR A CA  
4350 C C   . THR A 556 ? 1.43519 2.21988 1.47240 0.23301  -0.46854 0.29467  556 THR A C   
4351 O O   . THR A 556 ? 1.36101 2.14468 1.43254 0.21141  -0.43707 0.27145  556 THR A O   
4352 C CB  . THR A 556 ? 1.42117 2.29771 1.45704 0.21688  -0.54019 0.26367  556 THR A CB  
4353 N N   . GLY A 557 ? 1.51813 2.24718 1.48586 0.24704  -0.46283 0.32537  557 GLY A N   
4354 C CA  . GLY A 557 ? 1.44913 2.11304 1.38017 0.23461  -0.41723 0.33020  557 GLY A CA  
4355 C C   . GLY A 557 ? 1.48798 2.14081 1.35549 0.20423  -0.40832 0.30971  557 GLY A C   
4356 O O   . GLY A 557 ? 1.44678 2.04732 1.27224 0.19300  -0.37365 0.31406  557 GLY A O   
4357 N N   . ASP A 558 ? 1.50110 2.20138 1.36226 0.19337  -0.44120 0.28845  558 ASP A N   
4358 C CA  . ASP A 558 ? 1.48449 2.17708 1.28687 0.16520  -0.43710 0.26302  558 ASP A CA  
4359 C C   . ASP A 558 ? 1.42058 2.16790 1.28063 0.14248  -0.45381 0.22394  558 ASP A C   
4360 O O   . ASP A 558 ? 1.49593 2.25158 1.31516 0.12374  -0.46830 0.20011  558 ASP A O   
4361 C CB  . ASP A 558 ? 1.34691 2.03012 1.05487 0.17559  -0.46430 0.27839  558 ASP A CB  
4362 N N   . LEU A 559 ? 1.34733 2.12954 1.29916 0.14417  -0.45043 0.21744  559 LEU A N   
4363 C CA  . LEU A 559 ? 1.31432 2.14725 1.32929 0.11959  -0.46012 0.18342  559 LEU A CA  
4364 C C   . LEU A 559 ? 1.46380 2.34109 1.46372 0.11738  -0.51105 0.17026  559 LEU A C   
4365 O O   . LEU A 559 ? 1.41993 2.29606 1.38974 0.09198  -0.51733 0.14241  559 LEU A O   
4366 C CB  . LEU A 559 ? 1.19087 1.99084 1.18966 0.08800  -0.42552 0.15928  559 LEU A CB  
4367 N N   . SER A 560 ? 1.39082 2.30398 1.41064 0.14467  -0.54815 0.18838  560 SER A N   
4368 C CA  . SER A 560 ? 1.37960 2.33692 1.38400 0.14660  -0.60369 0.17629  560 SER A CA  
4369 C C   . SER A 560 ? 1.48550 2.49769 1.57522 0.16702  -0.63615 0.18212  560 SER A C   
4370 O O   . SER A 560 ? 1.51257 2.50728 1.60175 0.19847  -0.63700 0.21297  560 SER A O   
4371 C CB  . SER A 560 ? 1.41061 2.32841 1.30050 0.16273  -0.62029 0.19561  560 SER A CB  
4372 O OG  . SER A 560 ? 1.46240 2.32748 1.27793 0.14165  -0.58735 0.18422  560 SER A OG  
4373 N N   . GLY A 561 ? 1.59165 2.65488 1.75535 0.14807  -0.65783 0.15148  561 GLY A N   
4374 C CA  . GLY A 561 ? 1.46618 2.57311 1.71474 0.16442  -0.68757 0.15187  561 GLY A CA  
4375 C C   . GLY A 561 ? 1.41180 2.57122 1.77838 0.15068  -0.66528 0.13809  561 GLY A C   
4376 O O   . GLY A 561 ? 1.34779 2.51097 1.72760 0.12291  -0.63322 0.12396  561 GLY A O   
4377 N N   . ASP A 562 ? 1.27513 2.47200 1.72416 0.17052  -0.67902 0.14389  562 ASP A N   
4378 C CA  . ASP A 562 ? 1.13099 2.38305 1.69539 0.15556  -0.65565 0.12903  562 ASP A CA  
4379 C C   . ASP A 562 ? 1.18612 2.41727 1.74203 0.15208  -0.60018 0.14013  562 ASP A C   
4380 O O   . ASP A 562 ? 1.19336 2.38541 1.70607 0.17926  -0.58455 0.16570  562 ASP A O   
4381 C CB  . ASP A 562 ? 1.04308 2.33739 1.69653 0.18073  -0.67401 0.13448  562 ASP A CB  
4382 N N   . SER A 563 ? 1.15504 2.40918 1.75394 0.11967  -0.57217 0.12238  563 SER A N   
4383 C CA  . SER A 563 ? 1.07709 2.29756 1.66018 0.11368  -0.51872 0.13025  563 SER A CA  
4384 C C   . SER A 563 ? 1.07229 2.33746 1.75099 0.09624  -0.48603 0.11966  563 SER A C   
4385 O O   . SER A 563 ? 0.97890 2.27724 1.70017 0.06342  -0.49335 0.09923  563 SER A O   
4386 C CB  . SER A 563 ? 1.03032 2.18447 1.52334 0.08882  -0.50503 0.12077  563 SER A CB  
4387 O OG  . SER A 563 ? 0.95239 2.13083 1.46583 0.05325  -0.52073 0.09328  563 SER A OG  
4388 N N   . LYS A 564 ? 1.09885 2.36319 1.80854 0.11756  -0.45080 0.13294  564 LYS A N   
4389 C CA  . LYS A 564 ? 1.02076 2.32270 1.80942 0.10339  -0.41185 0.12600  564 LYS A CA  
4390 C C   . LYS A 564 ? 0.95909 2.20034 1.69610 0.07720  -0.37085 0.12060  564 LYS A C   
4391 O O   . LYS A 564 ? 1.01413 2.18945 1.66296 0.07415  -0.37347 0.12184  564 LYS A O   
4392 C CB  . LYS A 564 ? 0.91107 2.23740 1.74826 0.14019  -0.39155 0.13929  564 LYS A CB  
4393 N N   . GLU A 565 ? 0.72773 1.99110 1.51776 0.05964  -0.33414 0.11599  565 GLU A N   
4394 C CA  . GLU A 565 ? 0.72608 1.93278 1.46980 0.03440  -0.29840 0.11144  565 GLU A CA  
4395 C C   . GLU A 565 ? 0.63570 1.85030 1.41291 0.04074  -0.24995 0.11820  565 GLU A C   
4396 O O   . GLU A 565 ? 0.75789 2.03812 1.61397 0.05172  -0.24283 0.12146  565 GLU A O   
4397 C CB  . GLU A 565 ? 0.64644 1.86258 1.40624 -0.00811 -0.31095 0.09470  565 GLU A CB  
4398 N N   . LEU A 566 ? 0.65525 1.80700 1.37422 0.03540  -0.21837 0.11946  566 LEU A N   
4399 C CA  . LEU A 566 ? 0.77406 1.92527 1.50835 0.04153  -0.17348 0.12480  566 LEU A CA  
4400 C C   . LEU A 566 ? 0.84793 1.95511 1.54927 0.00974  -0.15009 0.12091  566 LEU A C   
4401 O O   . LEU A 566 ? 0.86431 1.92181 1.51188 -0.00746 -0.16441 0.11374  566 LEU A O   
4402 C CB  . LEU A 566 ? 0.57951 1.69315 1.27214 0.08020  -0.15998 0.13134  566 LEU A CB  
4403 N N   . ASP A 567 ? 0.82731 1.94706 1.55352 0.00590  -0.11165 0.12661  567 ASP A N   
4404 C CA  . ASP A 567 ? 0.88134 1.95676 1.57656 -0.02236 -0.08888 0.12629  567 ASP A CA  
4405 C C   . ASP A 567 ? 1.03565 2.06385 1.67745 -0.00063 -0.05707 0.13138  567 ASP A C   
4406 O O   . ASP A 567 ? 1.11103 2.12447 1.72642 0.03263  -0.06065 0.13085  567 ASP A O   
4407 C CB  . ASP A 567 ? 0.72249 1.84633 1.48821 -0.05330 -0.07370 0.13045  567 ASP A CB  
4408 N N   . ALA A 568 ? 1.06122 2.06273 1.68652 -0.01903 -0.03024 0.13562  568 ALA A N   
4409 C CA  . ALA A 568 ? 1.03347 1.98756 1.60295 0.00115  -0.00388 0.13843  568 ALA A CA  
4410 C C   . ALA A 568 ? 0.98194 1.97810 1.57634 0.03442  0.01804  0.14321  568 ALA A C   
4411 O O   . ALA A 568 ? 0.92462 1.98936 1.58697 0.03538  0.01872  0.14700  568 ALA A O   
4412 C CB  . ALA A 568 ? 0.97753 1.90295 1.53099 -0.02441 0.01882  0.14501  568 ALA A CB  
4413 N N   . GLY A 569 ? 0.87239 1.82975 1.41645 0.06125  0.03423  0.14068  569 GLY A N   
4414 C CA  . GLY A 569 ? 0.87631 1.86850 1.43737 0.09644  0.05567  0.14072  569 GLY A CA  
4415 C C   . GLY A 569 ? 0.91533 1.89844 1.47013 0.12957  0.03330  0.13128  569 GLY A C   
4416 O O   . GLY A 569 ? 0.99266 1.95639 1.54023 0.12190  0.00158  0.12911  569 GLY A O   
4417 N N   . GLU A 570 ? 0.91826 1.91390 1.47470 0.16596  0.05010  0.12606  570 GLU A N   
4418 C CA  . GLU A 570 ? 0.93843 1.92004 1.49227 0.20043  0.02974  0.11738  570 GLU A CA  
4419 C C   . GLU A 570 ? 0.93161 1.97464 1.55328 0.20480  0.00966  0.12216  570 GLU A C   
4420 O O   . GLU A 570 ? 1.02240 2.12869 1.70007 0.18946  0.02090  0.12846  570 GLU A O   
4421 C CB  . GLU A 570 ? 1.05740 2.03828 1.60001 0.23935  0.05349  0.10676  570 GLU A CB  
4422 C CG  . GLU A 570 ? 1.11853 2.03421 1.59001 0.24371  0.06590  0.09810  570 GLU A CG  
4423 C CD  . GLU A 570 ? 1.12507 2.03438 1.58054 0.28603  0.08216  0.08204  570 GLU A CD  
4424 O OE1 . GLU A 570 ? 1.13829 2.09029 1.63907 0.31338  0.08354  0.07730  570 GLU A OE1 
4425 O OE2 . GLU A 570 ? 1.11336 1.97518 1.51213 0.29289  0.09162  0.07248  570 GLU A OE2 
4426 N N   . HIS A 571 ? 0.92083 1.94569 1.54004 0.22506  -0.01941 0.12042  571 HIS A N   
4427 C CA  . HIS A 571 ? 0.87436 1.95786 1.55773 0.23594  -0.04233 0.12537  571 HIS A CA  
4428 C C   . HIS A 571 ? 0.84849 1.90675 1.52625 0.27534  -0.06086 0.12300  571 HIS A C   
4429 O O   . HIS A 571 ? 0.96002 1.94761 1.58021 0.28171  -0.06566 0.12017  571 HIS A O   
4430 C CB  . HIS A 571 ? 0.79231 1.88513 1.48285 0.20253  -0.07273 0.13257  571 HIS A CB  
4431 C CG  . HIS A 571 ? 0.85767 1.95719 1.54704 0.16110  -0.05960 0.13369  571 HIS A CG  
4432 N ND1 . HIS A 571 ? 0.90264 2.07006 1.65775 0.14377  -0.04533 0.13667  571 HIS A ND1 
4433 C CD2 . HIS A 571 ? 0.93517 1.98017 1.56978 0.13406  -0.05767 0.13248  571 HIS A CD2 
4434 C CE1 . HIS A 571 ? 0.85467 2.00456 1.59332 0.10658  -0.03625 0.13835  571 HIS A CE1 
4435 N NE2 . HIS A 571 ? 0.88932 1.96501 1.55412 0.10129  -0.04424 0.13506  571 HIS A NE2 
4436 N N   . LYS A 572 ? 0.81140 1.92483 1.55191 0.30095  -0.07123 0.12439  572 LYS A N   
4437 C CA  . LYS A 572 ? 0.77621 1.86757 1.52038 0.33943  -0.09125 0.12443  572 LYS A CA  
4438 C C   . LYS A 572 ? 0.83270 1.95441 1.61109 0.33913  -0.13151 0.13754  572 LYS A C   
4439 O O   . LYS A 572 ? 0.81048 2.00708 1.65619 0.33695  -0.13683 0.13889  572 LYS A O   
4440 C CB  . LYS A 572 ? 0.64159 1.76714 1.42876 0.37886  -0.06798 0.11206  572 LYS A CB  
4441 N N   . VAL A 573 ? 0.89249 1.95748 1.62523 0.34142  -0.15967 0.14769  573 VAL A N   
4442 C CA  . VAL A 573 ? 0.85730 1.94085 1.60449 0.34208  -0.20085 0.16234  573 VAL A CA  
4443 C C   . VAL A 573 ? 0.87766 1.95099 1.64663 0.38637  -0.21912 0.16974  573 VAL A C   
4444 O O   . VAL A 573 ? 0.84604 1.86727 1.59261 0.40911  -0.20617 0.16579  573 VAL A O   
4445 C CB  . VAL A 573 ? 0.75111 1.78009 1.42686 0.31271  -0.21911 0.17180  573 VAL A CB  
4446 N N   . GLU A 574 ? 0.81083 1.93341 1.62703 0.39937  -0.25187 0.17981  574 GLU A N   
4447 C CA  . GLU A 574 ? 0.87631 1.97395 1.70847 0.43684  -0.27295 0.18758  574 GLU A CA  
4448 C C   . GLU A 574 ? 0.87945 1.90332 1.64313 0.44206  -0.29277 0.20857  574 GLU A C   
4449 O O   . GLU A 574 ? 0.93724 1.93913 1.64668 0.41309  -0.30524 0.21875  574 GLU A O   
4450 C CB  . GLU A 574 ? 0.79790 1.94457 1.68556 0.44065  -0.30460 0.19000  574 GLU A CB  
4451 N N   . GLU A 575 ? 0.85229 1.82514 1.61492 0.47421  -0.29235 0.21183  575 GLU A N   
4452 C CA  . GLU A 575 ? 1.00334 1.90128 1.70732 0.48010  -0.30546 0.23392  575 GLU A CA  
4453 C C   . GLU A 575 ? 1.12924 2.02367 1.80820 0.47463  -0.34532 0.25952  575 GLU A C   
4454 O O   . GLU A 575 ? 1.16969 2.07802 1.88446 0.49416  -0.37083 0.26454  575 GLU A O   
4455 C CB  . GLU A 575 ? 0.91218 1.75842 1.63409 0.51603  -0.29986 0.23086  575 GLU A CB  
4456 C CG  . GLU A 575 ? 1.12438 1.88713 1.79283 0.52015  -0.30675 0.25347  575 GLU A CG  
4457 C CD  . GLU A 575 ? 1.20619 1.91644 1.90000 0.55385  -0.30079 0.24671  575 GLU A CD  
4458 O OE1 . GLU A 575 ? 1.12017 1.85567 1.87110 0.57674  -0.30090 0.22904  575 GLU A OE1 
4459 O OE2 . GLU A 575 ? 1.18893 1.82773 1.84745 0.55328  -0.29498 0.25626  575 GLU A OE2 
4460 N N   . GLY A 576 ? 1.16434 2.03027 1.77559 0.44508  -0.34943 0.27163  576 GLY A N   
4461 C CA  . GLY A 576 ? 1.10434 1.97092 1.67858 0.44007  -0.38628 0.29598  576 GLY A CA  
4462 C C   . GLY A 576 ? 0.98507 1.91129 1.55900 0.40985  -0.40063 0.28563  576 GLY A C   
4463 O O   . GLY A 576 ? 1.02524 1.95015 1.55919 0.40319  -0.43249 0.30096  576 GLY A O   
4464 N N   . SER A 577 ? 0.85048 1.82431 1.46538 0.39046  -0.37781 0.25927  577 SER A N   
4465 C CA  . SER A 577 ? 0.83593 1.86621 1.46140 0.35975  -0.39140 0.24778  577 SER A CA  
4466 C C   . SER A 577 ? 0.91235 1.89989 1.46183 0.32051  -0.38100 0.24345  577 SER A C   
4467 O O   . SER A 577 ? 0.97625 1.99042 1.51046 0.29770  -0.40388 0.23941  577 SER A O   
4468 C CB  . SER A 577 ? 0.78989 1.88854 1.49504 0.35361  -0.36885 0.22485  577 SER A CB  
4469 N N   . VAL A 578 ? 0.93451 1.85368 1.43617 0.31530  -0.35059 0.24410  578 VAL A N   
4470 C CA  . VAL A 578 ? 0.96974 1.84745 1.40386 0.27906  -0.33696 0.23788  578 VAL A CA  
4471 C C   . VAL A 578 ? 1.03424 1.85532 1.39363 0.28236  -0.35281 0.26085  578 VAL A C   
4472 O O   . VAL A 578 ? 0.97683 1.75304 1.32534 0.30732  -0.34926 0.27936  578 VAL A O   
4473 C CB  . VAL A 578 ? 0.77071 1.61197 1.19856 0.26756  -0.29447 0.22271  578 VAL A CB  
4474 N N   . GLY A 579 ? 1.05194 1.87518 1.36263 0.25826  -0.36897 0.25935  579 GLY A N   
4475 C CA  . GLY A 579 ? 1.06351 1.83320 1.29320 0.25868  -0.37818 0.28088  579 GLY A CA  
4476 C C   . GLY A 579 ? 1.08323 1.82486 1.25686 0.22316  -0.36011 0.26574  579 GLY A C   
4477 O O   . GLY A 579 ? 1.13877 1.83034 1.24334 0.22002  -0.35548 0.28069  579 GLY A O   
4478 N N   . SER A 580 ? 1.00081 1.77320 1.20589 0.19783  -0.34833 0.23794  580 SER A N   
4479 C CA  . SER A 580 ? 0.95466 1.70011 1.11374 0.16432  -0.33119 0.22050  580 SER A CA  
4480 C C   . SER A 580 ? 0.91386 1.68528 1.12327 0.14250  -0.31091 0.19477  580 SER A C   
4481 O O   . SER A 580 ? 0.91067 1.73486 1.18651 0.14959  -0.31736 0.18990  580 SER A O   
4482 C CB  . SER A 580 ? 1.09644 1.85490 1.20651 0.15191  -0.36092 0.21755  580 SER A CB  
4483 N N   . ILE A 581 ? 0.79304 1.52810 0.97263 0.11792  -0.28610 0.18057  581 ILE A N   
4484 C CA  . ILE A 581 ? 0.85284 1.60478 1.07393 0.09780  -0.26562 0.16033  581 ILE A CA  
4485 C C   . ILE A 581 ? 0.94804 1.68026 1.13302 0.06523  -0.26124 0.14187  581 ILE A C   
4486 O O   . ILE A 581 ? 0.95045 1.63143 1.07994 0.06031  -0.24923 0.14271  581 ILE A O   
4487 C CB  . ILE A 581 ? 0.71179 1.43245 0.94787 0.10937  -0.23281 0.16197  581 ILE A CB  
4488 N N   . THR A 582 ? 0.98790 1.76064 1.20955 0.04304  -0.26979 0.12472  582 THR A N   
4489 C CA  . THR A 582 ? 0.88813 1.64402 1.08689 0.01160  -0.26688 0.10387  582 THR A CA  
4490 C C   . THR A 582 ? 0.92222 1.68220 1.16575 -0.00582 -0.24148 0.09363  582 THR A C   
4491 O O   . THR A 582 ? 0.94540 1.75389 1.25115 -0.00700 -0.24253 0.09424  582 THR A O   
4492 C CB  . THR A 582 ? 0.85480 1.64971 1.05595 -0.00213 -0.30335 0.09088  582 THR A CB  
4493 O OG1 . THR A 582 ? 0.95301 1.73019 1.08904 0.01128  -0.32403 0.09900  582 THR A OG1 
4494 C CG2 . THR A 582 ? 0.78649 1.57235 0.98810 -0.03621 -0.29993 0.06507  582 THR A CG2 
4495 N N   . ILE A 583 ? 0.90514 1.61539 1.11815 -0.01855 -0.21813 0.08558  583 ILE A N   
4496 C CA  . ILE A 583 ? 0.94530 1.65010 1.18955 -0.03404 -0.19412 0.07851  583 ILE A CA  
4497 C C   . ILE A 583 ? 1.05000 1.75427 1.29737 -0.06659 -0.20206 0.05866  583 ILE A C   
4498 O O   . ILE A 583 ? 1.03759 1.71169 1.23854 -0.07572 -0.21045 0.04648  583 ILE A O   
4499 C CB  . ILE A 583 ? 0.84983 1.49921 1.06377 -0.02477 -0.16635 0.08186  583 ILE A CB  
4500 C CG1 . ILE A 583 ? 0.81586 1.46398 1.03286 0.00740  -0.16035 0.09850  583 ILE A CG1 
4501 C CG2 . ILE A 583 ? 0.91899 1.55920 1.15613 -0.03994 -0.14451 0.07565  583 ILE A CG2 
4502 C CD1 . ILE A 583 ? 0.86383 1.55330 1.13385 0.01900  -0.15162 0.10445  583 ILE A CD1 
4503 N N   . SER A 584 ? 1.07420 1.81110 1.37759 -0.08403 -0.19812 0.05513  584 SER A N   
4504 C CA  . SER A 584 ? 1.08066 1.81669 1.39852 -0.11629 -0.20660 0.03631  584 SER A CA  
4505 C C   . SER A 584 ? 1.11866 1.85172 1.47713 -0.13205 -0.18085 0.04009  584 SER A C   
4506 O O   . SER A 584 ? 1.08411 1.83087 1.46496 -0.11783 -0.15980 0.05657  584 SER A O   
4507 C CB  . SER A 584 ? 0.85040 1.64090 1.20498 -0.12704 -0.24072 0.02685  584 SER A CB  
4508 N N   . LYS A 585 ? 1.16188 1.87484 1.52700 -0.16059 -0.18269 0.02460  585 LYS A N   
4509 C CA  . LYS A 585 ? 0.98314 1.68757 1.38452 -0.17916 -0.16018 0.02999  585 LYS A CA  
4510 C C   . LYS A 585 ? 0.93283 1.59715 1.30352 -0.16187 -0.12983 0.04398  585 LYS A C   
4511 O O   . LYS A 585 ? 0.87429 1.48845 1.22007 -0.17063 -0.11926 0.03813  585 LYS A O   
4512 C CB  . LYS A 585 ? 0.82161 1.58932 1.29825 -0.18808 -0.15862 0.04130  585 LYS A CB  
# 
