data_8YYG
# 
_entry.id   8YYG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YYG         pdb_00008yyg 10.2210/pdb8yyg/pdb 
WWPDB D_1300046614 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        8YYG 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_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              bgopal@iisc.ac.in 
_pdbx_contact_author.name_first         Balasubramanian 
_pdbx_contact_author.name_last          Gopal 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9097-5052 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Singh, A.K.'    1 0000-0002-4415-5827 
'Chinnasamy, K.' 2 0000-0002-0300-5005 
'Gopal, B.'      3 0000-0001-9097-5052 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108152 
_citation.page_last                 108152 
_citation.title                     'A physicochemical rationale for the varied catalytic efficiency in RNase J paralogues.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.108152 
_citation.pdbx_database_id_PubMed   39742998 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Singh, A.K.'    1 ? 
primary 'Chinnasamy, K.' 2 ? 
primary 'Pahelkar, N.R.' 3 ? 
primary 'Gopal, B.'      4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribonuclease J 2'   64312.258 1   3.1.-.- H78A ? ? 
2 non-polymer syn 'MANGANESE (II) ION' 54.938    1   ?       ?    ? ? 
3 water       nat water                18.015    237 ?       ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'RNase J2' 
# 
_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       
;MGSSHHHHHHSQDPMSLIKKKNKDIRIIPLGGVGEIAKNMYIVEVDDEMFMLDAGLMFPEDEMLGVDIVIPDIQYVIENK
ERLKGIFLTHGAEHAIGAVSYVLEQIDAPVYGSKLTIALVKEAMKARNIKKKVRYYTVNHDSIMRFKNVNVSFFNTTHSI
PDSLGVCIHTSYGSIVYTGEFKFDQSLHGHYAPDLKRMAEIGDEGVFALISDSTEAEKPGYNTPENIIEHHMYDAFAKVK
GRLIVSCYASNFVRIQQVLNIASQLNRKVSFLGRSLESSFNIARKMGYFDIPKDLLIPINEVENYPKNEVIIIATGMQGE
PVEALSQMARKKHKIMNIEEGDSIFLAITASANMEVIIADTLNELVRAGAHIIPNNKKIHASSHGCMEELKMMLNIMKPE
YFVPVQGEFKMQIAHAKLAAETGVAPEKIFLVEKGDVISYNGKDMILNEKVQSGNILIDGIGVGDVGNIVLRDRHLLAED
GIFIAVVTLDPKNRRIAAGPEIQSRGFVYVRESEELLKEAEEKVRKIVEEGLQEKRIEWSEIKQNMRDQISKLLFESTKR
RPMIIPVISEI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSQDPMSLIKKKNKDIRIIPLGGVGEIAKNMYIVEVDDEMFMLDAGLMFPEDEMLGVDIVIPDIQYVIENK
ERLKGIFLTHGAEHAIGAVSYVLEQIDAPVYGSKLTIALVKEAMKARNIKKKVRYYTVNHDSIMRFKNVNVSFFNTTHSI
PDSLGVCIHTSYGSIVYTGEFKFDQSLHGHYAPDLKRMAEIGDEGVFALISDSTEAEKPGYNTPENIIEHHMYDAFAKVK
GRLIVSCYASNFVRIQQVLNIASQLNRKVSFLGRSLESSFNIARKMGYFDIPKDLLIPINEVENYPKNEVIIIATGMQGE
PVEALSQMARKKHKIMNIEEGDSIFLAITASANMEVIIADTLNELVRAGAHIIPNNKKIHASSHGCMEELKMMLNIMKPE
YFVPVQGEFKMQIAHAKLAAETGVAPEKIFLVEKGDVISYNGKDMILNEKVQSGNILIDGIGVGDVGNIVLRDRHLLAED
GIFIAVVTLDPKNRRIAAGPEIQSRGFVYVRESEELLKEAEEKVRKIVEEGLQEKRIEWSEIKQNMRDQISKLLFESTKR
RPMIIPVISEI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION' MN  
3 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  GLN n 
1 13  ASP n 
1 14  PRO n 
1 15  MET n 
1 16  SER n 
1 17  LEU n 
1 18  ILE n 
1 19  LYS n 
1 20  LYS n 
1 21  LYS n 
1 22  ASN n 
1 23  LYS n 
1 24  ASP n 
1 25  ILE n 
1 26  ARG n 
1 27  ILE n 
1 28  ILE n 
1 29  PRO n 
1 30  LEU n 
1 31  GLY n 
1 32  GLY n 
1 33  VAL n 
1 34  GLY n 
1 35  GLU n 
1 36  ILE n 
1 37  ALA n 
1 38  LYS n 
1 39  ASN n 
1 40  MET n 
1 41  TYR n 
1 42  ILE n 
1 43  VAL n 
1 44  GLU n 
1 45  VAL n 
1 46  ASP n 
1 47  ASP n 
1 48  GLU n 
1 49  MET n 
1 50  PHE n 
1 51  MET n 
1 52  LEU n 
1 53  ASP n 
1 54  ALA n 
1 55  GLY n 
1 56  LEU n 
1 57  MET n 
1 58  PHE n 
1 59  PRO n 
1 60  GLU n 
1 61  ASP n 
1 62  GLU n 
1 63  MET n 
1 64  LEU n 
1 65  GLY n 
1 66  VAL n 
1 67  ASP n 
1 68  ILE n 
1 69  VAL n 
1 70  ILE n 
1 71  PRO n 
1 72  ASP n 
1 73  ILE n 
1 74  GLN n 
1 75  TYR n 
1 76  VAL n 
1 77  ILE n 
1 78  GLU n 
1 79  ASN n 
1 80  LYS n 
1 81  GLU n 
1 82  ARG n 
1 83  LEU n 
1 84  LYS n 
1 85  GLY n 
1 86  ILE n 
1 87  PHE n 
1 88  LEU n 
1 89  THR n 
1 90  HIS n 
1 91  GLY n 
1 92  ALA n 
1 93  GLU n 
1 94  HIS n 
1 95  ALA n 
1 96  ILE n 
1 97  GLY n 
1 98  ALA n 
1 99  VAL n 
1 100 SER n 
1 101 TYR n 
1 102 VAL n 
1 103 LEU n 
1 104 GLU n 
1 105 GLN n 
1 106 ILE n 
1 107 ASP n 
1 108 ALA n 
1 109 PRO n 
1 110 VAL n 
1 111 TYR n 
1 112 GLY n 
1 113 SER n 
1 114 LYS n 
1 115 LEU n 
1 116 THR n 
1 117 ILE n 
1 118 ALA n 
1 119 LEU n 
1 120 VAL n 
1 121 LYS n 
1 122 GLU n 
1 123 ALA n 
1 124 MET n 
1 125 LYS n 
1 126 ALA n 
1 127 ARG n 
1 128 ASN n 
1 129 ILE n 
1 130 LYS n 
1 131 LYS n 
1 132 LYS n 
1 133 VAL n 
1 134 ARG n 
1 135 TYR n 
1 136 TYR n 
1 137 THR n 
1 138 VAL n 
1 139 ASN n 
1 140 HIS n 
1 141 ASP n 
1 142 SER n 
1 143 ILE n 
1 144 MET n 
1 145 ARG n 
1 146 PHE n 
1 147 LYS n 
1 148 ASN n 
1 149 VAL n 
1 150 ASN n 
1 151 VAL n 
1 152 SER n 
1 153 PHE n 
1 154 PHE n 
1 155 ASN n 
1 156 THR n 
1 157 THR n 
1 158 HIS n 
1 159 SER n 
1 160 ILE n 
1 161 PRO n 
1 162 ASP n 
1 163 SER n 
1 164 LEU n 
1 165 GLY n 
1 166 VAL n 
1 167 CYS n 
1 168 ILE n 
1 169 HIS n 
1 170 THR n 
1 171 SER n 
1 172 TYR n 
1 173 GLY n 
1 174 SER n 
1 175 ILE n 
1 176 VAL n 
1 177 TYR n 
1 178 THR n 
1 179 GLY n 
1 180 GLU n 
1 181 PHE n 
1 182 LYS n 
1 183 PHE n 
1 184 ASP n 
1 185 GLN n 
1 186 SER n 
1 187 LEU n 
1 188 HIS n 
1 189 GLY n 
1 190 HIS n 
1 191 TYR n 
1 192 ALA n 
1 193 PRO n 
1 194 ASP n 
1 195 LEU n 
1 196 LYS n 
1 197 ARG n 
1 198 MET n 
1 199 ALA n 
1 200 GLU n 
1 201 ILE n 
1 202 GLY n 
1 203 ASP n 
1 204 GLU n 
1 205 GLY n 
1 206 VAL n 
1 207 PHE n 
1 208 ALA n 
1 209 LEU n 
1 210 ILE n 
1 211 SER n 
1 212 ASP n 
1 213 SER n 
1 214 THR n 
1 215 GLU n 
1 216 ALA n 
1 217 GLU n 
1 218 LYS n 
1 219 PRO n 
1 220 GLY n 
1 221 TYR n 
1 222 ASN n 
1 223 THR n 
1 224 PRO n 
1 225 GLU n 
1 226 ASN n 
1 227 ILE n 
1 228 ILE n 
1 229 GLU n 
1 230 HIS n 
1 231 HIS n 
1 232 MET n 
1 233 TYR n 
1 234 ASP n 
1 235 ALA n 
1 236 PHE n 
1 237 ALA n 
1 238 LYS n 
1 239 VAL n 
1 240 LYS n 
1 241 GLY n 
1 242 ARG n 
1 243 LEU n 
1 244 ILE n 
1 245 VAL n 
1 246 SER n 
1 247 CYS n 
1 248 TYR n 
1 249 ALA n 
1 250 SER n 
1 251 ASN n 
1 252 PHE n 
1 253 VAL n 
1 254 ARG n 
1 255 ILE n 
1 256 GLN n 
1 257 GLN n 
1 258 VAL n 
1 259 LEU n 
1 260 ASN n 
1 261 ILE n 
1 262 ALA n 
1 263 SER n 
1 264 GLN n 
1 265 LEU n 
1 266 ASN n 
1 267 ARG n 
1 268 LYS n 
1 269 VAL n 
1 270 SER n 
1 271 PHE n 
1 272 LEU n 
1 273 GLY n 
1 274 ARG n 
1 275 SER n 
1 276 LEU n 
1 277 GLU n 
1 278 SER n 
1 279 SER n 
1 280 PHE n 
1 281 ASN n 
1 282 ILE n 
1 283 ALA n 
1 284 ARG n 
1 285 LYS n 
1 286 MET n 
1 287 GLY n 
1 288 TYR n 
1 289 PHE n 
1 290 ASP n 
1 291 ILE n 
1 292 PRO n 
1 293 LYS n 
1 294 ASP n 
1 295 LEU n 
1 296 LEU n 
1 297 ILE n 
1 298 PRO n 
1 299 ILE n 
1 300 ASN n 
1 301 GLU n 
1 302 VAL n 
1 303 GLU n 
1 304 ASN n 
1 305 TYR n 
1 306 PRO n 
1 307 LYS n 
1 308 ASN n 
1 309 GLU n 
1 310 VAL n 
1 311 ILE n 
1 312 ILE n 
1 313 ILE n 
1 314 ALA n 
1 315 THR n 
1 316 GLY n 
1 317 MET n 
1 318 GLN n 
1 319 GLY n 
1 320 GLU n 
1 321 PRO n 
1 322 VAL n 
1 323 GLU n 
1 324 ALA n 
1 325 LEU n 
1 326 SER n 
1 327 GLN n 
1 328 MET n 
1 329 ALA n 
1 330 ARG n 
1 331 LYS n 
1 332 LYS n 
1 333 HIS n 
1 334 LYS n 
1 335 ILE n 
1 336 MET n 
1 337 ASN n 
1 338 ILE n 
1 339 GLU n 
1 340 GLU n 
1 341 GLY n 
1 342 ASP n 
1 343 SER n 
1 344 ILE n 
1 345 PHE n 
1 346 LEU n 
1 347 ALA n 
1 348 ILE n 
1 349 THR n 
1 350 ALA n 
1 351 SER n 
1 352 ALA n 
1 353 ASN n 
1 354 MET n 
1 355 GLU n 
1 356 VAL n 
1 357 ILE n 
1 358 ILE n 
1 359 ALA n 
1 360 ASP n 
1 361 THR n 
1 362 LEU n 
1 363 ASN n 
1 364 GLU n 
1 365 LEU n 
1 366 VAL n 
1 367 ARG n 
1 368 ALA n 
1 369 GLY n 
1 370 ALA n 
1 371 HIS n 
1 372 ILE n 
1 373 ILE n 
1 374 PRO n 
1 375 ASN n 
1 376 ASN n 
1 377 LYS n 
1 378 LYS n 
1 379 ILE n 
1 380 HIS n 
1 381 ALA n 
1 382 SER n 
1 383 SER n 
1 384 HIS n 
1 385 GLY n 
1 386 CYS n 
1 387 MET n 
1 388 GLU n 
1 389 GLU n 
1 390 LEU n 
1 391 LYS n 
1 392 MET n 
1 393 MET n 
1 394 LEU n 
1 395 ASN n 
1 396 ILE n 
1 397 MET n 
1 398 LYS n 
1 399 PRO n 
1 400 GLU n 
1 401 TYR n 
1 402 PHE n 
1 403 VAL n 
1 404 PRO n 
1 405 VAL n 
1 406 GLN n 
1 407 GLY n 
1 408 GLU n 
1 409 PHE n 
1 410 LYS n 
1 411 MET n 
1 412 GLN n 
1 413 ILE n 
1 414 ALA n 
1 415 HIS n 
1 416 ALA n 
1 417 LYS n 
1 418 LEU n 
1 419 ALA n 
1 420 ALA n 
1 421 GLU n 
1 422 THR n 
1 423 GLY n 
1 424 VAL n 
1 425 ALA n 
1 426 PRO n 
1 427 GLU n 
1 428 LYS n 
1 429 ILE n 
1 430 PHE n 
1 431 LEU n 
1 432 VAL n 
1 433 GLU n 
1 434 LYS n 
1 435 GLY n 
1 436 ASP n 
1 437 VAL n 
1 438 ILE n 
1 439 SER n 
1 440 TYR n 
1 441 ASN n 
1 442 GLY n 
1 443 LYS n 
1 444 ASP n 
1 445 MET n 
1 446 ILE n 
1 447 LEU n 
1 448 ASN n 
1 449 GLU n 
1 450 LYS n 
1 451 VAL n 
1 452 GLN n 
1 453 SER n 
1 454 GLY n 
1 455 ASN n 
1 456 ILE n 
1 457 LEU n 
1 458 ILE n 
1 459 ASP n 
1 460 GLY n 
1 461 ILE n 
1 462 GLY n 
1 463 VAL n 
1 464 GLY n 
1 465 ASP n 
1 466 VAL n 
1 467 GLY n 
1 468 ASN n 
1 469 ILE n 
1 470 VAL n 
1 471 LEU n 
1 472 ARG n 
1 473 ASP n 
1 474 ARG n 
1 475 HIS n 
1 476 LEU n 
1 477 LEU n 
1 478 ALA n 
1 479 GLU n 
1 480 ASP n 
1 481 GLY n 
1 482 ILE n 
1 483 PHE n 
1 484 ILE n 
1 485 ALA n 
1 486 VAL n 
1 487 VAL n 
1 488 THR n 
1 489 LEU n 
1 490 ASP n 
1 491 PRO n 
1 492 LYS n 
1 493 ASN n 
1 494 ARG n 
1 495 ARG n 
1 496 ILE n 
1 497 ALA n 
1 498 ALA n 
1 499 GLY n 
1 500 PRO n 
1 501 GLU n 
1 502 ILE n 
1 503 GLN n 
1 504 SER n 
1 505 ARG n 
1 506 GLY n 
1 507 PHE n 
1 508 VAL n 
1 509 TYR n 
1 510 VAL n 
1 511 ARG n 
1 512 GLU n 
1 513 SER n 
1 514 GLU n 
1 515 GLU n 
1 516 LEU n 
1 517 LEU n 
1 518 LYS n 
1 519 GLU n 
1 520 ALA n 
1 521 GLU n 
1 522 GLU n 
1 523 LYS n 
1 524 VAL n 
1 525 ARG n 
1 526 LYS n 
1 527 ILE n 
1 528 VAL n 
1 529 GLU n 
1 530 GLU n 
1 531 GLY n 
1 532 LEU n 
1 533 GLN n 
1 534 GLU n 
1 535 LYS n 
1 536 ARG n 
1 537 ILE n 
1 538 GLU n 
1 539 TRP n 
1 540 SER n 
1 541 GLU n 
1 542 ILE n 
1 543 LYS n 
1 544 GLN n 
1 545 ASN n 
1 546 MET n 
1 547 ARG n 
1 548 ASP n 
1 549 GLN n 
1 550 ILE n 
1 551 SER n 
1 552 LYS n 
1 553 LEU n 
1 554 LEU n 
1 555 PHE n 
1 556 GLU n 
1 557 SER n 
1 558 THR n 
1 559 LYS n 
1 560 ARG n 
1 561 ARG n 
1 562 PRO n 
1 563 MET n 
1 564 ILE n 
1 565 ILE n 
1 566 PRO n 
1 567 VAL n 
1 568 ILE n 
1 569 SER n 
1 570 GLU n 
1 571 ILE 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                   571 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rnj2, SERP0842' 
_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      'Staphylococcus aureus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1280 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE              ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE             ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE           ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'      ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'  149.211 
MN  non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'           54.938  
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE               ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -13 ?   ?   ?   A . n 
A 1 2   GLY 2   -12 ?   ?   ?   A . n 
A 1 3   SER 3   -11 ?   ?   ?   A . n 
A 1 4   SER 4   -10 ?   ?   ?   A . n 
A 1 5   HIS 5   -9  ?   ?   ?   A . n 
A 1 6   HIS 6   -8  ?   ?   ?   A . n 
A 1 7   HIS 7   -7  ?   ?   ?   A . n 
A 1 8   HIS 8   -6  ?   ?   ?   A . n 
A 1 9   HIS 9   -5  ?   ?   ?   A . n 
A 1 10  HIS 10  -4  ?   ?   ?   A . n 
A 1 11  SER 11  -3  ?   ?   ?   A . n 
A 1 12  GLN 12  -2  ?   ?   ?   A . n 
A 1 13  ASP 13  -1  ?   ?   ?   A . n 
A 1 14  PRO 14  0   ?   ?   ?   A . n 
A 1 15  MET 15  1   ?   ?   ?   A . n 
A 1 16  SER 16  2   ?   ?   ?   A . n 
A 1 17  LEU 17  3   ?   ?   ?   A . n 
A 1 18  ILE 18  4   4   ILE ILE A . n 
A 1 19  LYS 19  5   5   LYS LYS A . n 
A 1 20  LYS 20  6   6   LYS LYS A . n 
A 1 21  LYS 21  7   7   LYS LYS A . n 
A 1 22  ASN 22  8   8   ASN ASN A . n 
A 1 23  LYS 23  9   9   LYS LYS A . n 
A 1 24  ASP 24  10  10  ASP ASP A . n 
A 1 25  ILE 25  11  11  ILE ILE A . n 
A 1 26  ARG 26  12  12  ARG ARG A . n 
A 1 27  ILE 27  13  13  ILE ILE A . n 
A 1 28  ILE 28  14  14  ILE ILE A . n 
A 1 29  PRO 29  15  15  PRO PRO A . n 
A 1 30  LEU 30  16  16  LEU LEU A . n 
A 1 31  GLY 31  17  17  GLY GLY A . n 
A 1 32  GLY 32  18  18  GLY GLY A . n 
A 1 33  VAL 33  19  19  VAL VAL A . n 
A 1 34  GLY 34  20  20  GLY GLY A . n 
A 1 35  GLU 35  21  21  GLU GLU A . n 
A 1 36  ILE 36  22  22  ILE ILE A . n 
A 1 37  ALA 37  23  23  ALA ALA A . n 
A 1 38  LYS 38  24  24  LYS LYS A . n 
A 1 39  ASN 39  25  25  ASN ASN A . n 
A 1 40  MET 40  26  26  MET MET A . n 
A 1 41  TYR 41  27  27  TYR TYR A . n 
A 1 42  ILE 42  28  28  ILE ILE A . n 
A 1 43  VAL 43  29  29  VAL VAL A . n 
A 1 44  GLU 44  30  30  GLU GLU A . n 
A 1 45  VAL 45  31  31  VAL VAL A . n 
A 1 46  ASP 46  32  32  ASP ASP A . n 
A 1 47  ASP 47  33  33  ASP ASP A . n 
A 1 48  GLU 48  34  34  GLU GLU A . n 
A 1 49  MET 49  35  35  MET MET A . n 
A 1 50  PHE 50  36  36  PHE PHE A . n 
A 1 51  MET 51  37  37  MET MET A . n 
A 1 52  LEU 52  38  38  LEU LEU A . n 
A 1 53  ASP 53  39  39  ASP ASP A . n 
A 1 54  ALA 54  40  40  ALA ALA A . n 
A 1 55  GLY 55  41  41  GLY GLY A . n 
A 1 56  LEU 56  42  42  LEU LEU A . n 
A 1 57  MET 57  43  43  MET MET A . n 
A 1 58  PHE 58  44  44  PHE PHE A . n 
A 1 59  PRO 59  45  45  PRO PRO A . n 
A 1 60  GLU 60  46  46  GLU GLU A . n 
A 1 61  ASP 61  47  47  ASP ASP A . n 
A 1 62  GLU 62  48  ?   ?   ?   A . n 
A 1 63  MET 63  49  49  MET MET A . n 
A 1 64  LEU 64  50  50  LEU LEU A . n 
A 1 65  GLY 65  51  51  GLY GLY A . n 
A 1 66  VAL 66  52  52  VAL VAL A . n 
A 1 67  ASP 67  53  53  ASP ASP A . n 
A 1 68  ILE 68  54  54  ILE ILE A . n 
A 1 69  VAL 69  55  55  VAL VAL A . n 
A 1 70  ILE 70  56  56  ILE ILE A . n 
A 1 71  PRO 71  57  57  PRO PRO A . n 
A 1 72  ASP 72  58  58  ASP ASP A . n 
A 1 73  ILE 73  59  59  ILE ILE A . n 
A 1 74  GLN 74  60  60  GLN GLN A . n 
A 1 75  TYR 75  61  61  TYR TYR A . n 
A 1 76  VAL 76  62  62  VAL VAL A . n 
A 1 77  ILE 77  63  63  ILE ILE A . n 
A 1 78  GLU 78  64  64  GLU GLU A . n 
A 1 79  ASN 79  65  65  ASN ASN A . n 
A 1 80  LYS 80  66  66  LYS LYS A . n 
A 1 81  GLU 81  67  67  GLU GLU A . n 
A 1 82  ARG 82  68  68  ARG ARG A . n 
A 1 83  LEU 83  69  69  LEU LEU A . n 
A 1 84  LYS 84  70  70  LYS LYS A . n 
A 1 85  GLY 85  71  71  GLY GLY A . n 
A 1 86  ILE 86  72  72  ILE ILE A . n 
A 1 87  PHE 87  73  73  PHE PHE A . n 
A 1 88  LEU 88  74  74  LEU LEU A . n 
A 1 89  THR 89  75  75  THR THR A . n 
A 1 90  HIS 90  76  76  HIS HIS A . n 
A 1 91  GLY 91  77  77  GLY GLY A . n 
A 1 92  ALA 92  78  78  ALA ALA A . n 
A 1 93  GLU 93  79  79  GLU GLU A . n 
A 1 94  HIS 94  80  80  HIS HIS A . n 
A 1 95  ALA 95  81  81  ALA ALA A . n 
A 1 96  ILE 96  82  82  ILE ILE A . n 
A 1 97  GLY 97  83  83  GLY GLY A . n 
A 1 98  ALA 98  84  84  ALA ALA A . n 
A 1 99  VAL 99  85  85  VAL VAL A . n 
A 1 100 SER 100 86  86  SER SER A . n 
A 1 101 TYR 101 87  87  TYR TYR A . n 
A 1 102 VAL 102 88  88  VAL VAL A . n 
A 1 103 LEU 103 89  89  LEU LEU A . n 
A 1 104 GLU 104 90  90  GLU GLU A . n 
A 1 105 GLN 105 91  91  GLN GLN A . n 
A 1 106 ILE 106 92  92  ILE ILE A . n 
A 1 107 ASP 107 93  93  ASP ASP A . n 
A 1 108 ALA 108 94  94  ALA ALA A . n 
A 1 109 PRO 109 95  95  PRO PRO A . n 
A 1 110 VAL 110 96  96  VAL VAL A . n 
A 1 111 TYR 111 97  97  TYR TYR A . n 
A 1 112 GLY 112 98  98  GLY GLY A . n 
A 1 113 SER 113 99  99  SER SER A . n 
A 1 114 LYS 114 100 100 LYS LYS A . n 
A 1 115 LEU 115 101 101 LEU LEU A . n 
A 1 116 THR 116 102 102 THR THR A . n 
A 1 117 ILE 117 103 103 ILE ILE A . n 
A 1 118 ALA 118 104 104 ALA ALA A . n 
A 1 119 LEU 119 105 105 LEU LEU A . n 
A 1 120 VAL 120 106 106 VAL VAL A . n 
A 1 121 LYS 121 107 107 LYS LYS A . n 
A 1 122 GLU 122 108 108 GLU GLU A . n 
A 1 123 ALA 123 109 109 ALA ALA A . n 
A 1 124 MET 124 110 110 MET MET A . n 
A 1 125 LYS 125 111 111 LYS LYS A . n 
A 1 126 ALA 126 112 112 ALA ALA A . n 
A 1 127 ARG 127 113 113 ARG ARG A . n 
A 1 128 ASN 128 114 114 ASN ASN A . n 
A 1 129 ILE 129 115 115 ILE ILE A . n 
A 1 130 LYS 130 116 116 LYS LYS A . n 
A 1 131 LYS 131 117 117 LYS LYS A . n 
A 1 132 LYS 132 118 118 LYS LYS A . n 
A 1 133 VAL 133 119 119 VAL VAL A . n 
A 1 134 ARG 134 120 120 ARG ARG A . n 
A 1 135 TYR 135 121 121 TYR TYR A . n 
A 1 136 TYR 136 122 122 TYR TYR A . n 
A 1 137 THR 137 123 123 THR THR A . n 
A 1 138 VAL 138 124 124 VAL VAL A . n 
A 1 139 ASN 139 125 125 ASN ASN A . n 
A 1 140 HIS 140 126 126 HIS HIS A . n 
A 1 141 ASP 141 127 127 ASP ASP A . n 
A 1 142 SER 142 128 128 SER SER A . n 
A 1 143 ILE 143 129 129 ILE ILE A . n 
A 1 144 MET 144 130 130 MET MET A . n 
A 1 145 ARG 145 131 131 ARG ARG A . n 
A 1 146 PHE 146 132 132 PHE PHE A . n 
A 1 147 LYS 147 133 133 LYS LYS A . n 
A 1 148 ASN 148 134 134 ASN ASN A . n 
A 1 149 VAL 149 135 135 VAL VAL A . n 
A 1 150 ASN 150 136 136 ASN ASN A . n 
A 1 151 VAL 151 137 137 VAL VAL A . n 
A 1 152 SER 152 138 138 SER SER A . n 
A 1 153 PHE 153 139 139 PHE PHE A . n 
A 1 154 PHE 154 140 140 PHE PHE A . n 
A 1 155 ASN 155 141 141 ASN ASN A . n 
A 1 156 THR 156 142 142 THR THR A . n 
A 1 157 THR 157 143 143 THR THR A . n 
A 1 158 HIS 158 144 144 HIS HIS A . n 
A 1 159 SER 159 145 145 SER SER A . n 
A 1 160 ILE 160 146 146 ILE ILE A . n 
A 1 161 PRO 161 147 147 PRO PRO A . n 
A 1 162 ASP 162 148 148 ASP ASP A . n 
A 1 163 SER 163 149 149 SER SER A . n 
A 1 164 LEU 164 150 150 LEU LEU A . n 
A 1 165 GLY 165 151 151 GLY GLY A . n 
A 1 166 VAL 166 152 152 VAL VAL A . n 
A 1 167 CYS 167 153 153 CYS CYS A . n 
A 1 168 ILE 168 154 154 ILE ILE A . n 
A 1 169 HIS 169 155 155 HIS HIS A . n 
A 1 170 THR 170 156 156 THR THR A . n 
A 1 171 SER 171 157 157 SER SER A . n 
A 1 172 TYR 172 158 158 TYR TYR A . n 
A 1 173 GLY 173 159 159 GLY GLY A . n 
A 1 174 SER 174 160 160 SER SER A . n 
A 1 175 ILE 175 161 161 ILE ILE A . n 
A 1 176 VAL 176 162 162 VAL VAL A . n 
A 1 177 TYR 177 163 163 TYR TYR A . n 
A 1 178 THR 178 164 164 THR THR A . n 
A 1 179 GLY 179 165 165 GLY GLY A . n 
A 1 180 GLU 180 166 166 GLU GLU A . n 
A 1 181 PHE 181 167 167 PHE PHE A . n 
A 1 182 LYS 182 168 168 LYS LYS A . n 
A 1 183 PHE 183 169 169 PHE PHE A . n 
A 1 184 ASP 184 170 170 ASP ASP A . n 
A 1 185 GLN 185 171 171 GLN GLN A . n 
A 1 186 SER 186 172 172 SER SER A . n 
A 1 187 LEU 187 173 173 LEU LEU A . n 
A 1 188 HIS 188 174 174 HIS HIS A . n 
A 1 189 GLY 189 175 175 GLY GLY A . n 
A 1 190 HIS 190 176 176 HIS HIS A . n 
A 1 191 TYR 191 177 177 TYR TYR A . n 
A 1 192 ALA 192 178 178 ALA ALA A . n 
A 1 193 PRO 193 179 179 PRO PRO A . n 
A 1 194 ASP 194 180 180 ASP ASP A . n 
A 1 195 LEU 195 181 181 LEU LEU A . n 
A 1 196 LYS 196 182 182 LYS LYS A . n 
A 1 197 ARG 197 183 183 ARG ARG A . n 
A 1 198 MET 198 184 184 MET MET A . n 
A 1 199 ALA 199 185 185 ALA ALA A . n 
A 1 200 GLU 200 186 186 GLU GLU A . n 
A 1 201 ILE 201 187 187 ILE ILE A . n 
A 1 202 GLY 202 188 188 GLY GLY A . n 
A 1 203 ASP 203 189 189 ASP ASP A . n 
A 1 204 GLU 204 190 190 GLU GLU A . n 
A 1 205 GLY 205 191 191 GLY GLY A . n 
A 1 206 VAL 206 192 192 VAL VAL A . n 
A 1 207 PHE 207 193 193 PHE PHE A . n 
A 1 208 ALA 208 194 194 ALA ALA A . n 
A 1 209 LEU 209 195 195 LEU LEU A . n 
A 1 210 ILE 210 196 196 ILE ILE A . n 
A 1 211 SER 211 197 197 SER SER A . n 
A 1 212 ASP 212 198 198 ASP ASP A . n 
A 1 213 SER 213 199 199 SER SER A . n 
A 1 214 THR 214 200 200 THR THR A . n 
A 1 215 GLU 215 201 201 GLU GLU A . n 
A 1 216 ALA 216 202 202 ALA ALA A . n 
A 1 217 GLU 217 203 203 GLU GLU A . n 
A 1 218 LYS 218 204 204 LYS LYS A . n 
A 1 219 PRO 219 205 205 PRO PRO A . n 
A 1 220 GLY 220 206 206 GLY GLY A . n 
A 1 221 TYR 221 207 207 TYR TYR A . n 
A 1 222 ASN 222 208 208 ASN ASN A . n 
A 1 223 THR 223 209 209 THR THR A . n 
A 1 224 PRO 224 210 210 PRO PRO A . n 
A 1 225 GLU 225 211 211 GLU GLU A . n 
A 1 226 ASN 226 212 212 ASN ASN A . n 
A 1 227 ILE 227 213 213 ILE ILE A . n 
A 1 228 ILE 228 214 214 ILE ILE A . n 
A 1 229 GLU 229 215 215 GLU GLU A . n 
A 1 230 HIS 230 216 216 HIS HIS A . n 
A 1 231 HIS 231 217 217 HIS HIS A . n 
A 1 232 MET 232 218 218 MET MET A . n 
A 1 233 TYR 233 219 219 TYR TYR A . n 
A 1 234 ASP 234 220 220 ASP ASP A . n 
A 1 235 ALA 235 221 221 ALA ALA A . n 
A 1 236 PHE 236 222 222 PHE PHE A . n 
A 1 237 ALA 237 223 223 ALA ALA A . n 
A 1 238 LYS 238 224 224 LYS LYS A . n 
A 1 239 VAL 239 225 225 VAL VAL A . n 
A 1 240 LYS 240 226 226 LYS LYS A . n 
A 1 241 GLY 241 227 227 GLY GLY A . n 
A 1 242 ARG 242 228 228 ARG ARG A . n 
A 1 243 LEU 243 229 229 LEU LEU A . n 
A 1 244 ILE 244 230 230 ILE ILE A . n 
A 1 245 VAL 245 231 231 VAL VAL A . n 
A 1 246 SER 246 232 232 SER SER A . n 
A 1 247 CYS 247 233 233 CYS CYS A . n 
A 1 248 TYR 248 234 234 TYR TYR A . n 
A 1 249 ALA 249 235 235 ALA ALA A . n 
A 1 250 SER 250 236 236 SER SER A . n 
A 1 251 ASN 251 237 237 ASN ASN A . n 
A 1 252 PHE 252 238 238 PHE PHE A . n 
A 1 253 VAL 253 239 239 VAL VAL A . n 
A 1 254 ARG 254 240 240 ARG ARG A . n 
A 1 255 ILE 255 241 241 ILE ILE A . n 
A 1 256 GLN 256 242 242 GLN GLN A . n 
A 1 257 GLN 257 243 243 GLN GLN A . n 
A 1 258 VAL 258 244 244 VAL VAL A . n 
A 1 259 LEU 259 245 245 LEU LEU A . n 
A 1 260 ASN 260 246 246 ASN ASN A . n 
A 1 261 ILE 261 247 247 ILE ILE A . n 
A 1 262 ALA 262 248 248 ALA ALA A . n 
A 1 263 SER 263 249 249 SER SER A . n 
A 1 264 GLN 264 250 250 GLN GLN A . n 
A 1 265 LEU 265 251 251 LEU LEU A . n 
A 1 266 ASN 266 252 252 ASN ASN A . n 
A 1 267 ARG 267 253 253 ARG ARG A . n 
A 1 268 LYS 268 254 254 LYS LYS A . n 
A 1 269 VAL 269 255 255 VAL VAL A . n 
A 1 270 SER 270 256 256 SER SER A . n 
A 1 271 PHE 271 257 257 PHE PHE A . n 
A 1 272 LEU 272 258 258 LEU LEU A . n 
A 1 273 GLY 273 259 259 GLY GLY A . n 
A 1 274 ARG 274 260 260 ARG ARG A . n 
A 1 275 SER 275 261 ?   ?   ?   A . n 
A 1 276 LEU 276 262 ?   ?   ?   A . n 
A 1 277 GLU 277 263 263 GLU GLU A . n 
A 1 278 SER 278 264 264 SER SER A . n 
A 1 279 SER 279 265 265 SER SER A . n 
A 1 280 PHE 280 266 266 PHE PHE A . n 
A 1 281 ASN 281 267 267 ASN ASN A . n 
A 1 282 ILE 282 268 268 ILE ILE A . n 
A 1 283 ALA 283 269 269 ALA ALA A . n 
A 1 284 ARG 284 270 270 ARG ARG A . n 
A 1 285 LYS 285 271 271 LYS LYS A . n 
A 1 286 MET 286 272 272 MET MET A . n 
A 1 287 GLY 287 273 273 GLY GLY A . n 
A 1 288 TYR 288 274 274 TYR TYR A . n 
A 1 289 PHE 289 275 275 PHE PHE A . n 
A 1 290 ASP 290 276 276 ASP ASP A . n 
A 1 291 ILE 291 277 277 ILE ILE A . n 
A 1 292 PRO 292 278 278 PRO PRO A . n 
A 1 293 LYS 293 279 279 LYS LYS A . n 
A 1 294 ASP 294 280 280 ASP ASP A . n 
A 1 295 LEU 295 281 281 LEU LEU A . n 
A 1 296 LEU 296 282 282 LEU LEU A . n 
A 1 297 ILE 297 283 283 ILE ILE A . n 
A 1 298 PRO 298 284 284 PRO PRO A . n 
A 1 299 ILE 299 285 285 ILE ILE A . n 
A 1 300 ASN 300 286 286 ASN ASN A . n 
A 1 301 GLU 301 287 287 GLU GLU A . n 
A 1 302 VAL 302 288 288 VAL VAL A . n 
A 1 303 GLU 303 289 289 GLU GLU A . n 
A 1 304 ASN 304 290 290 ASN ASN A . n 
A 1 305 TYR 305 291 291 TYR TYR A . n 
A 1 306 PRO 306 292 292 PRO PRO A . n 
A 1 307 LYS 307 293 293 LYS LYS A . n 
A 1 308 ASN 308 294 294 ASN ASN A . n 
A 1 309 GLU 309 295 295 GLU GLU A . n 
A 1 310 VAL 310 296 296 VAL VAL A . n 
A 1 311 ILE 311 297 297 ILE ILE A . n 
A 1 312 ILE 312 298 298 ILE ILE A . n 
A 1 313 ILE 313 299 299 ILE ILE A . n 
A 1 314 ALA 314 300 300 ALA ALA A . n 
A 1 315 THR 315 301 301 THR THR A . n 
A 1 316 GLY 316 302 302 GLY GLY A . n 
A 1 317 MET 317 303 303 MET MET A . n 
A 1 318 GLN 318 304 304 GLN GLN A . n 
A 1 319 GLY 319 305 305 GLY GLY A . n 
A 1 320 GLU 320 306 306 GLU GLU A . n 
A 1 321 PRO 321 307 307 PRO PRO A . n 
A 1 322 VAL 322 308 308 VAL VAL A . n 
A 1 323 GLU 323 309 309 GLU GLU A . n 
A 1 324 ALA 324 310 310 ALA ALA A . n 
A 1 325 LEU 325 311 311 LEU LEU A . n 
A 1 326 SER 326 312 312 SER SER A . n 
A 1 327 GLN 327 313 313 GLN GLN A . n 
A 1 328 MET 328 314 314 MET MET A . n 
A 1 329 ALA 329 315 315 ALA ALA A . n 
A 1 330 ARG 330 316 316 ARG ARG A . n 
A 1 331 LYS 331 317 317 LYS LYS A . n 
A 1 332 LYS 332 318 318 LYS LYS A . n 
A 1 333 HIS 333 319 319 HIS HIS A . n 
A 1 334 LYS 334 320 320 LYS LYS A . n 
A 1 335 ILE 335 321 321 ILE ILE A . n 
A 1 336 MET 336 322 322 MET MET A . n 
A 1 337 ASN 337 323 323 ASN ASN A . n 
A 1 338 ILE 338 324 324 ILE ILE A . n 
A 1 339 GLU 339 325 325 GLU GLU A . n 
A 1 340 GLU 340 326 326 GLU GLU A . n 
A 1 341 GLY 341 327 327 GLY GLY A . n 
A 1 342 ASP 342 328 328 ASP ASP A . n 
A 1 343 SER 343 329 329 SER SER A . n 
A 1 344 ILE 344 330 330 ILE ILE A . n 
A 1 345 PHE 345 331 331 PHE PHE A . n 
A 1 346 LEU 346 332 332 LEU LEU A . n 
A 1 347 ALA 347 333 333 ALA ALA A . n 
A 1 348 ILE 348 334 334 ILE ILE A . n 
A 1 349 THR 349 335 335 THR THR A . n 
A 1 350 ALA 350 336 336 ALA ALA A . n 
A 1 351 SER 351 337 337 SER SER A . n 
A 1 352 ALA 352 338 338 ALA ALA A . n 
A 1 353 ASN 353 339 339 ASN ASN A . n 
A 1 354 MET 354 340 340 MET MET A . n 
A 1 355 GLU 355 341 341 GLU GLU A . n 
A 1 356 VAL 356 342 342 VAL VAL A . n 
A 1 357 ILE 357 343 343 ILE ILE A . n 
A 1 358 ILE 358 344 344 ILE ILE A . n 
A 1 359 ALA 359 345 345 ALA ALA A . n 
A 1 360 ASP 360 346 346 ASP ASP A . n 
A 1 361 THR 361 347 347 THR THR A . n 
A 1 362 LEU 362 348 348 LEU LEU A . n 
A 1 363 ASN 363 349 349 ASN ASN A . n 
A 1 364 GLU 364 350 350 GLU GLU A . n 
A 1 365 LEU 365 351 351 LEU LEU A . n 
A 1 366 VAL 366 352 352 VAL VAL A . n 
A 1 367 ARG 367 353 353 ARG ARG A . n 
A 1 368 ALA 368 354 354 ALA ALA A . n 
A 1 369 GLY 369 355 355 GLY GLY A . n 
A 1 370 ALA 370 356 356 ALA ALA A . n 
A 1 371 HIS 371 357 357 HIS HIS A . n 
A 1 372 ILE 372 358 358 ILE ILE A . n 
A 1 373 ILE 373 359 359 ILE ILE A . n 
A 1 374 PRO 374 360 360 PRO PRO A . n 
A 1 375 ASN 375 361 361 ASN ASN A . n 
A 1 376 ASN 376 362 362 ASN ASN A . n 
A 1 377 LYS 377 363 363 LYS LYS A . n 
A 1 378 LYS 378 364 364 LYS LYS A . n 
A 1 379 ILE 379 365 365 ILE ILE A . n 
A 1 380 HIS 380 366 366 HIS HIS A . n 
A 1 381 ALA 381 367 367 ALA ALA A . n 
A 1 382 SER 382 368 368 SER SER A . n 
A 1 383 SER 383 369 369 SER SER A . n 
A 1 384 HIS 384 370 370 HIS HIS A . n 
A 1 385 GLY 385 371 371 GLY GLY A . n 
A 1 386 CYS 386 372 372 CYS CYS A . n 
A 1 387 MET 387 373 373 MET MET A . n 
A 1 388 GLU 388 374 374 GLU GLU A . n 
A 1 389 GLU 389 375 375 GLU GLU A . n 
A 1 390 LEU 390 376 376 LEU LEU A . n 
A 1 391 LYS 391 377 377 LYS LYS A . n 
A 1 392 MET 392 378 378 MET MET A . n 
A 1 393 MET 393 379 379 MET MET A . n 
A 1 394 LEU 394 380 380 LEU LEU A . n 
A 1 395 ASN 395 381 381 ASN ASN A . n 
A 1 396 ILE 396 382 382 ILE ILE A . n 
A 1 397 MET 397 383 383 MET MET A . n 
A 1 398 LYS 398 384 384 LYS LYS A . n 
A 1 399 PRO 399 385 385 PRO PRO A . n 
A 1 400 GLU 400 386 386 GLU GLU A . n 
A 1 401 TYR 401 387 387 TYR TYR A . n 
A 1 402 PHE 402 388 388 PHE PHE A . n 
A 1 403 VAL 403 389 389 VAL VAL A . n 
A 1 404 PRO 404 390 390 PRO PRO A . n 
A 1 405 VAL 405 391 391 VAL VAL A . n 
A 1 406 GLN 406 392 392 GLN GLN A . n 
A 1 407 GLY 407 393 393 GLY GLY A . n 
A 1 408 GLU 408 394 394 GLU GLU A . n 
A 1 409 PHE 409 395 395 PHE PHE A . n 
A 1 410 LYS 410 396 396 LYS LYS A . n 
A 1 411 MET 411 397 397 MET MET A . n 
A 1 412 GLN 412 398 398 GLN GLN A . n 
A 1 413 ILE 413 399 399 ILE ILE A . n 
A 1 414 ALA 414 400 400 ALA ALA A . n 
A 1 415 HIS 415 401 401 HIS HIS A . n 
A 1 416 ALA 416 402 402 ALA ALA A . n 
A 1 417 LYS 417 403 403 LYS LYS A . n 
A 1 418 LEU 418 404 404 LEU LEU A . n 
A 1 419 ALA 419 405 405 ALA ALA A . n 
A 1 420 ALA 420 406 406 ALA ALA A . n 
A 1 421 GLU 421 407 407 GLU GLU A . n 
A 1 422 THR 422 408 408 THR THR A . n 
A 1 423 GLY 423 409 409 GLY GLY A . n 
A 1 424 VAL 424 410 410 VAL VAL A . n 
A 1 425 ALA 425 411 411 ALA ALA A . n 
A 1 426 PRO 426 412 412 PRO PRO A . n 
A 1 427 GLU 427 413 413 GLU GLU A . n 
A 1 428 LYS 428 414 414 LYS LYS A . n 
A 1 429 ILE 429 415 415 ILE ILE A . n 
A 1 430 PHE 430 416 416 PHE PHE A . n 
A 1 431 LEU 431 417 417 LEU LEU A . n 
A 1 432 VAL 432 418 418 VAL VAL A . n 
A 1 433 GLU 433 419 419 GLU GLU A . n 
A 1 434 LYS 434 420 420 LYS LYS A . n 
A 1 435 GLY 435 421 421 GLY GLY A . n 
A 1 436 ASP 436 422 422 ASP ASP A . n 
A 1 437 VAL 437 423 423 VAL VAL A . n 
A 1 438 ILE 438 424 424 ILE ILE A . n 
A 1 439 SER 439 425 425 SER SER A . n 
A 1 440 TYR 440 426 426 TYR TYR A . n 
A 1 441 ASN 441 427 427 ASN ASN A . n 
A 1 442 GLY 442 428 428 GLY GLY A . n 
A 1 443 LYS 443 429 429 LYS LYS A . n 
A 1 444 ASP 444 430 430 ASP ASP A . n 
A 1 445 MET 445 431 431 MET MET A . n 
A 1 446 ILE 446 432 432 ILE ILE A . n 
A 1 447 LEU 447 433 433 LEU LEU A . n 
A 1 448 ASN 448 434 434 ASN ASN A . n 
A 1 449 GLU 449 435 435 GLU GLU A . n 
A 1 450 LYS 450 436 436 LYS LYS A . n 
A 1 451 VAL 451 437 437 VAL VAL A . n 
A 1 452 GLN 452 438 438 GLN GLN A . n 
A 1 453 SER 453 439 439 SER SER A . n 
A 1 454 GLY 454 440 440 GLY GLY A . n 
A 1 455 ASN 455 441 441 ASN ASN A . n 
A 1 456 ILE 456 442 442 ILE ILE A . n 
A 1 457 LEU 457 443 443 LEU LEU A . n 
A 1 458 ILE 458 444 444 ILE ILE A . n 
A 1 459 ASP 459 445 445 ASP ASP A . n 
A 1 460 GLY 460 446 446 GLY GLY A . n 
A 1 461 ILE 461 447 ?   ?   ?   A . n 
A 1 462 GLY 462 448 ?   ?   ?   A . n 
A 1 463 VAL 463 449 ?   ?   ?   A . n 
A 1 464 GLY 464 450 ?   ?   ?   A . n 
A 1 465 ASP 465 451 ?   ?   ?   A . n 
A 1 466 VAL 466 452 ?   ?   ?   A . n 
A 1 467 GLY 467 453 ?   ?   ?   A . n 
A 1 468 ASN 468 454 ?   ?   ?   A . n 
A 1 469 ILE 469 455 ?   ?   ?   A . n 
A 1 470 VAL 470 456 ?   ?   ?   A . n 
A 1 471 LEU 471 457 ?   ?   ?   A . n 
A 1 472 ARG 472 458 ?   ?   ?   A . n 
A 1 473 ASP 473 459 ?   ?   ?   A . n 
A 1 474 ARG 474 460 ?   ?   ?   A . n 
A 1 475 HIS 475 461 ?   ?   ?   A . n 
A 1 476 LEU 476 462 ?   ?   ?   A . n 
A 1 477 LEU 477 463 ?   ?   ?   A . n 
A 1 478 ALA 478 464 ?   ?   ?   A . n 
A 1 479 GLU 479 465 ?   ?   ?   A . n 
A 1 480 ASP 480 466 ?   ?   ?   A . n 
A 1 481 GLY 481 467 ?   ?   ?   A . n 
A 1 482 ILE 482 468 ?   ?   ?   A . n 
A 1 483 PHE 483 469 ?   ?   ?   A . n 
A 1 484 ILE 484 470 ?   ?   ?   A . n 
A 1 485 ALA 485 471 ?   ?   ?   A . n 
A 1 486 VAL 486 472 ?   ?   ?   A . n 
A 1 487 VAL 487 473 ?   ?   ?   A . n 
A 1 488 THR 488 474 ?   ?   ?   A . n 
A 1 489 LEU 489 475 ?   ?   ?   A . n 
A 1 490 ASP 490 476 ?   ?   ?   A . n 
A 1 491 PRO 491 477 ?   ?   ?   A . n 
A 1 492 LYS 492 478 ?   ?   ?   A . n 
A 1 493 ASN 493 479 ?   ?   ?   A . n 
A 1 494 ARG 494 480 ?   ?   ?   A . n 
A 1 495 ARG 495 481 ?   ?   ?   A . n 
A 1 496 ILE 496 482 ?   ?   ?   A . n 
A 1 497 ALA 497 483 ?   ?   ?   A . n 
A 1 498 ALA 498 484 ?   ?   ?   A . n 
A 1 499 GLY 499 485 ?   ?   ?   A . n 
A 1 500 PRO 500 486 ?   ?   ?   A . n 
A 1 501 GLU 501 487 ?   ?   ?   A . n 
A 1 502 ILE 502 488 ?   ?   ?   A . n 
A 1 503 GLN 503 489 ?   ?   ?   A . n 
A 1 504 SER 504 490 ?   ?   ?   A . n 
A 1 505 ARG 505 491 ?   ?   ?   A . n 
A 1 506 GLY 506 492 ?   ?   ?   A . n 
A 1 507 PHE 507 493 ?   ?   ?   A . n 
A 1 508 VAL 508 494 ?   ?   ?   A . n 
A 1 509 TYR 509 495 ?   ?   ?   A . n 
A 1 510 VAL 510 496 ?   ?   ?   A . n 
A 1 511 ARG 511 497 ?   ?   ?   A . n 
A 1 512 GLU 512 498 ?   ?   ?   A . n 
A 1 513 SER 513 499 ?   ?   ?   A . n 
A 1 514 GLU 514 500 ?   ?   ?   A . n 
A 1 515 GLU 515 501 ?   ?   ?   A . n 
A 1 516 LEU 516 502 ?   ?   ?   A . n 
A 1 517 LEU 517 503 ?   ?   ?   A . n 
A 1 518 LYS 518 504 ?   ?   ?   A . n 
A 1 519 GLU 519 505 ?   ?   ?   A . n 
A 1 520 ALA 520 506 ?   ?   ?   A . n 
A 1 521 GLU 521 507 ?   ?   ?   A . n 
A 1 522 GLU 522 508 ?   ?   ?   A . n 
A 1 523 LYS 523 509 ?   ?   ?   A . n 
A 1 524 VAL 524 510 ?   ?   ?   A . n 
A 1 525 ARG 525 511 ?   ?   ?   A . n 
A 1 526 LYS 526 512 ?   ?   ?   A . n 
A 1 527 ILE 527 513 ?   ?   ?   A . n 
A 1 528 VAL 528 514 ?   ?   ?   A . n 
A 1 529 GLU 529 515 ?   ?   ?   A . n 
A 1 530 GLU 530 516 ?   ?   ?   A . n 
A 1 531 GLY 531 517 ?   ?   ?   A . n 
A 1 532 LEU 532 518 ?   ?   ?   A . n 
A 1 533 GLN 533 519 ?   ?   ?   A . n 
A 1 534 GLU 534 520 ?   ?   ?   A . n 
A 1 535 LYS 535 521 ?   ?   ?   A . n 
A 1 536 ARG 536 522 ?   ?   ?   A . n 
A 1 537 ILE 537 523 ?   ?   ?   A . n 
A 1 538 GLU 538 524 ?   ?   ?   A . n 
A 1 539 TRP 539 525 ?   ?   ?   A . n 
A 1 540 SER 540 526 ?   ?   ?   A . n 
A 1 541 GLU 541 527 ?   ?   ?   A . n 
A 1 542 ILE 542 528 ?   ?   ?   A . n 
A 1 543 LYS 543 529 ?   ?   ?   A . n 
A 1 544 GLN 544 530 ?   ?   ?   A . n 
A 1 545 ASN 545 531 ?   ?   ?   A . n 
A 1 546 MET 546 532 ?   ?   ?   A . n 
A 1 547 ARG 547 533 ?   ?   ?   A . n 
A 1 548 ASP 548 534 ?   ?   ?   A . n 
A 1 549 GLN 549 535 ?   ?   ?   A . n 
A 1 550 ILE 550 536 ?   ?   ?   A . n 
A 1 551 SER 551 537 ?   ?   ?   A . n 
A 1 552 LYS 552 538 ?   ?   ?   A . n 
A 1 553 LEU 553 539 ?   ?   ?   A . n 
A 1 554 LEU 554 540 ?   ?   ?   A . n 
A 1 555 PHE 555 541 ?   ?   ?   A . n 
A 1 556 GLU 556 542 ?   ?   ?   A . n 
A 1 557 SER 557 543 ?   ?   ?   A . n 
A 1 558 THR 558 544 ?   ?   ?   A . n 
A 1 559 LYS 559 545 ?   ?   ?   A . n 
A 1 560 ARG 560 546 ?   ?   ?   A . n 
A 1 561 ARG 561 547 ?   ?   ?   A . n 
A 1 562 PRO 562 548 ?   ?   ?   A . n 
A 1 563 MET 563 549 ?   ?   ?   A . n 
A 1 564 ILE 564 550 ?   ?   ?   A . n 
A 1 565 ILE 565 551 ?   ?   ?   A . n 
A 1 566 PRO 566 552 ?   ?   ?   A . n 
A 1 567 VAL 567 553 ?   ?   ?   A . n 
A 1 568 ILE 568 554 ?   ?   ?   A . n 
A 1 569 SER 569 555 ?   ?   ?   A . n 
A 1 570 GLU 570 556 ?   ?   ?   A . n 
A 1 571 ILE 571 557 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MN  1   601 1   MN  MN  A . 
C 3 HOH 1   701 103 HOH HOH A . 
C 3 HOH 2   702 221 HOH HOH A . 
C 3 HOH 3   703 167 HOH HOH A . 
C 3 HOH 4   704 156 HOH HOH A . 
C 3 HOH 5   705 242 HOH HOH A . 
C 3 HOH 6   706 189 HOH HOH A . 
C 3 HOH 7   707 108 HOH HOH A . 
C 3 HOH 8   708 132 HOH HOH A . 
C 3 HOH 9   709 42  HOH HOH A . 
C 3 HOH 10  710 165 HOH HOH A . 
C 3 HOH 11  711 67  HOH HOH A . 
C 3 HOH 12  712 188 HOH HOH A . 
C 3 HOH 13  713 34  HOH HOH A . 
C 3 HOH 14  714 143 HOH HOH A . 
C 3 HOH 15  715 69  HOH HOH A . 
C 3 HOH 16  716 235 HOH HOH A . 
C 3 HOH 17  717 136 HOH HOH A . 
C 3 HOH 18  718 227 HOH HOH A . 
C 3 HOH 19  719 78  HOH HOH A . 
C 3 HOH 20  720 10  HOH HOH A . 
C 3 HOH 21  721 199 HOH HOH A . 
C 3 HOH 22  722 211 HOH HOH A . 
C 3 HOH 23  723 112 HOH HOH A . 
C 3 HOH 24  724 86  HOH HOH A . 
C 3 HOH 25  725 236 HOH HOH A . 
C 3 HOH 26  726 127 HOH HOH A . 
C 3 HOH 27  727 88  HOH HOH A . 
C 3 HOH 28  728 99  HOH HOH A . 
C 3 HOH 29  729 19  HOH HOH A . 
C 3 HOH 30  730 121 HOH HOH A . 
C 3 HOH 31  731 7   HOH HOH A . 
C 3 HOH 32  732 135 HOH HOH A . 
C 3 HOH 33  733 215 HOH HOH A . 
C 3 HOH 34  734 98  HOH HOH A . 
C 3 HOH 35  735 116 HOH HOH A . 
C 3 HOH 36  736 15  HOH HOH A . 
C 3 HOH 37  737 120 HOH HOH A . 
C 3 HOH 38  738 125 HOH HOH A . 
C 3 HOH 39  739 96  HOH HOH A . 
C 3 HOH 40  740 22  HOH HOH A . 
C 3 HOH 41  741 240 HOH HOH A . 
C 3 HOH 42  742 45  HOH HOH A . 
C 3 HOH 43  743 223 HOH HOH A . 
C 3 HOH 44  744 191 HOH HOH A . 
C 3 HOH 45  745 59  HOH HOH A . 
C 3 HOH 46  746 97  HOH HOH A . 
C 3 HOH 47  747 60  HOH HOH A . 
C 3 HOH 48  748 12  HOH HOH A . 
C 3 HOH 49  749 177 HOH HOH A . 
C 3 HOH 50  750 131 HOH HOH A . 
C 3 HOH 51  751 90  HOH HOH A . 
C 3 HOH 52  752 168 HOH HOH A . 
C 3 HOH 53  753 33  HOH HOH A . 
C 3 HOH 54  754 213 HOH HOH A . 
C 3 HOH 55  755 160 HOH HOH A . 
C 3 HOH 56  756 124 HOH HOH A . 
C 3 HOH 57  757 35  HOH HOH A . 
C 3 HOH 58  758 63  HOH HOH A . 
C 3 HOH 59  759 21  HOH HOH A . 
C 3 HOH 60  760 232 HOH HOH A . 
C 3 HOH 61  761 114 HOH HOH A . 
C 3 HOH 62  762 54  HOH HOH A . 
C 3 HOH 63  763 148 HOH HOH A . 
C 3 HOH 64  764 138 HOH HOH A . 
C 3 HOH 65  765 80  HOH HOH A . 
C 3 HOH 66  766 106 HOH HOH A . 
C 3 HOH 67  767 17  HOH HOH A . 
C 3 HOH 68  768 205 HOH HOH A . 
C 3 HOH 69  769 122 HOH HOH A . 
C 3 HOH 70  770 158 HOH HOH A . 
C 3 HOH 71  771 104 HOH HOH A . 
C 3 HOH 72  772 110 HOH HOH A . 
C 3 HOH 73  773 24  HOH HOH A . 
C 3 HOH 74  774 39  HOH HOH A . 
C 3 HOH 75  775 27  HOH HOH A . 
C 3 HOH 76  776 91  HOH HOH A . 
C 3 HOH 77  777 83  HOH HOH A . 
C 3 HOH 78  778 144 HOH HOH A . 
C 3 HOH 79  779 2   HOH HOH A . 
C 3 HOH 80  780 40  HOH HOH A . 
C 3 HOH 81  781 208 HOH HOH A . 
C 3 HOH 82  782 13  HOH HOH A . 
C 3 HOH 83  783 57  HOH HOH A . 
C 3 HOH 84  784 155 HOH HOH A . 
C 3 HOH 85  785 146 HOH HOH A . 
C 3 HOH 86  786 46  HOH HOH A . 
C 3 HOH 87  787 20  HOH HOH A . 
C 3 HOH 88  788 62  HOH HOH A . 
C 3 HOH 89  789 130 HOH HOH A . 
C 3 HOH 90  790 29  HOH HOH A . 
C 3 HOH 91  791 71  HOH HOH A . 
C 3 HOH 92  792 8   HOH HOH A . 
C 3 HOH 93  793 61  HOH HOH A . 
C 3 HOH 94  794 66  HOH HOH A . 
C 3 HOH 95  795 147 HOH HOH A . 
C 3 HOH 96  796 3   HOH HOH A . 
C 3 HOH 97  797 18  HOH HOH A . 
C 3 HOH 98  798 251 HOH HOH A . 
C 3 HOH 99  799 44  HOH HOH A . 
C 3 HOH 100 800 6   HOH HOH A . 
C 3 HOH 101 801 239 HOH HOH A . 
C 3 HOH 102 802 107 HOH HOH A . 
C 3 HOH 103 803 198 HOH HOH A . 
C 3 HOH 104 804 241 HOH HOH A . 
C 3 HOH 105 805 94  HOH HOH A . 
C 3 HOH 106 806 170 HOH HOH A . 
C 3 HOH 107 807 95  HOH HOH A . 
C 3 HOH 108 808 181 HOH HOH A . 
C 3 HOH 109 809 128 HOH HOH A . 
C 3 HOH 110 810 47  HOH HOH A . 
C 3 HOH 111 811 172 HOH HOH A . 
C 3 HOH 112 812 233 HOH HOH A . 
C 3 HOH 113 813 118 HOH HOH A . 
C 3 HOH 114 814 85  HOH HOH A . 
C 3 HOH 115 815 65  HOH HOH A . 
C 3 HOH 116 816 82  HOH HOH A . 
C 3 HOH 117 817 209 HOH HOH A . 
C 3 HOH 118 818 180 HOH HOH A . 
C 3 HOH 119 819 184 HOH HOH A . 
C 3 HOH 120 820 101 HOH HOH A . 
C 3 HOH 121 821 212 HOH HOH A . 
C 3 HOH 122 822 55  HOH HOH A . 
C 3 HOH 123 823 137 HOH HOH A . 
C 3 HOH 124 824 244 HOH HOH A . 
C 3 HOH 125 825 119 HOH HOH A . 
C 3 HOH 126 826 218 HOH HOH A . 
C 3 HOH 127 827 133 HOH HOH A . 
C 3 HOH 128 828 32  HOH HOH A . 
C 3 HOH 129 829 41  HOH HOH A . 
C 3 HOH 130 830 238 HOH HOH A . 
C 3 HOH 131 831 187 HOH HOH A . 
C 3 HOH 132 832 93  HOH HOH A . 
C 3 HOH 133 833 81  HOH HOH A . 
C 3 HOH 134 834 72  HOH HOH A . 
C 3 HOH 135 835 30  HOH HOH A . 
C 3 HOH 136 836 140 HOH HOH A . 
C 3 HOH 137 837 92  HOH HOH A . 
C 3 HOH 138 838 245 HOH HOH A . 
C 3 HOH 139 839 16  HOH HOH A . 
C 3 HOH 140 840 164 HOH HOH A . 
C 3 HOH 141 841 87  HOH HOH A . 
C 3 HOH 142 842 64  HOH HOH A . 
C 3 HOH 143 843 179 HOH HOH A . 
C 3 HOH 144 844 117 HOH HOH A . 
C 3 HOH 145 845 194 HOH HOH A . 
C 3 HOH 146 846 230 HOH HOH A . 
C 3 HOH 147 847 228 HOH HOH A . 
C 3 HOH 148 848 202 HOH HOH A . 
C 3 HOH 149 849 37  HOH HOH A . 
C 3 HOH 150 850 150 HOH HOH A . 
C 3 HOH 151 851 31  HOH HOH A . 
C 3 HOH 152 852 115 HOH HOH A . 
C 3 HOH 153 853 224 HOH HOH A . 
C 3 HOH 154 854 5   HOH HOH A . 
C 3 HOH 155 855 178 HOH HOH A . 
C 3 HOH 156 856 74  HOH HOH A . 
C 3 HOH 157 857 231 HOH HOH A . 
C 3 HOH 158 858 77  HOH HOH A . 
C 3 HOH 159 859 48  HOH HOH A . 
C 3 HOH 160 860 196 HOH HOH A . 
C 3 HOH 161 861 153 HOH HOH A . 
C 3 HOH 162 862 26  HOH HOH A . 
C 3 HOH 163 863 102 HOH HOH A . 
C 3 HOH 164 864 159 HOH HOH A . 
C 3 HOH 165 865 217 HOH HOH A . 
C 3 HOH 166 866 25  HOH HOH A . 
C 3 HOH 167 867 11  HOH HOH A . 
C 3 HOH 168 868 76  HOH HOH A . 
C 3 HOH 169 869 185 HOH HOH A . 
C 3 HOH 170 870 58  HOH HOH A . 
C 3 HOH 171 871 247 HOH HOH A . 
C 3 HOH 172 872 28  HOH HOH A . 
C 3 HOH 173 873 166 HOH HOH A . 
C 3 HOH 174 874 123 HOH HOH A . 
C 3 HOH 175 875 79  HOH HOH A . 
C 3 HOH 176 876 207 HOH HOH A . 
C 3 HOH 177 877 234 HOH HOH A . 
C 3 HOH 178 878 248 HOH HOH A . 
C 3 HOH 179 879 171 HOH HOH A . 
C 3 HOH 180 880 222 HOH HOH A . 
C 3 HOH 181 881 56  HOH HOH A . 
C 3 HOH 182 882 246 HOH HOH A . 
C 3 HOH 183 883 111 HOH HOH A . 
C 3 HOH 184 884 84  HOH HOH A . 
C 3 HOH 185 885 243 HOH HOH A . 
C 3 HOH 186 886 113 HOH HOH A . 
C 3 HOH 187 887 43  HOH HOH A . 
C 3 HOH 188 888 14  HOH HOH A . 
C 3 HOH 189 889 23  HOH HOH A . 
C 3 HOH 190 890 249 HOH HOH A . 
C 3 HOH 191 891 139 HOH HOH A . 
C 3 HOH 192 892 154 HOH HOH A . 
C 3 HOH 193 893 169 HOH HOH A . 
C 3 HOH 194 894 220 HOH HOH A . 
C 3 HOH 195 895 192 HOH HOH A . 
C 3 HOH 196 896 203 HOH HOH A . 
C 3 HOH 197 897 193 HOH HOH A . 
C 3 HOH 198 898 195 HOH HOH A . 
C 3 HOH 199 899 105 HOH HOH A . 
C 3 HOH 200 900 182 HOH HOH A . 
C 3 HOH 201 901 197 HOH HOH A . 
C 3 HOH 202 902 216 HOH HOH A . 
C 3 HOH 203 903 201 HOH HOH A . 
C 3 HOH 204 904 142 HOH HOH A . 
C 3 HOH 205 905 36  HOH HOH A . 
C 3 HOH 206 906 174 HOH HOH A . 
C 3 HOH 207 907 109 HOH HOH A . 
C 3 HOH 208 908 204 HOH HOH A . 
C 3 HOH 209 909 190 HOH HOH A . 
C 3 HOH 210 910 75  HOH HOH A . 
C 3 HOH 211 911 175 HOH HOH A . 
C 3 HOH 212 912 210 HOH HOH A . 
C 3 HOH 213 913 229 HOH HOH A . 
C 3 HOH 214 914 126 HOH HOH A . 
C 3 HOH 215 915 100 HOH HOH A . 
C 3 HOH 216 916 157 HOH HOH A . 
C 3 HOH 217 917 68  HOH HOH A . 
C 3 HOH 218 918 206 HOH HOH A . 
C 3 HOH 219 919 141 HOH HOH A . 
C 3 HOH 220 920 89  HOH HOH A . 
C 3 HOH 221 921 161 HOH HOH A . 
C 3 HOH 222 922 225 HOH HOH A . 
C 3 HOH 223 923 250 HOH HOH A . 
C 3 HOH 224 924 186 HOH HOH A . 
C 3 HOH 225 925 183 HOH HOH A . 
C 3 HOH 226 926 176 HOH HOH A . 
C 3 HOH 227 927 237 HOH HOH A . 
C 3 HOH 228 928 129 HOH HOH A . 
C 3 HOH 229 929 214 HOH HOH A . 
C 3 HOH 230 930 173 HOH HOH A . 
C 3 HOH 231 931 219 HOH HOH A . 
C 3 HOH 232 932 73  HOH HOH A . 
C 3 HOH 233 933 152 HOH HOH A . 
C 3 HOH 234 934 151 HOH HOH A . 
C 3 HOH 235 935 200 HOH HOH A . 
C 3 HOH 236 936 149 HOH HOH A . 
C 3 HOH 237 937 226 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 5   ? CG  ? A LYS 19  CG  
2  1 Y 1 A LYS 5   ? CD  ? A LYS 19  CD  
3  1 Y 1 A LYS 5   ? CE  ? A LYS 19  CE  
4  1 Y 1 A LYS 5   ? NZ  ? A LYS 19  NZ  
5  1 Y 1 A LYS 6   ? CG  ? A LYS 20  CG  
6  1 Y 1 A LYS 6   ? CD  ? A LYS 20  CD  
7  1 Y 1 A LYS 6   ? CE  ? A LYS 20  CE  
8  1 Y 1 A LYS 6   ? NZ  ? A LYS 20  NZ  
9  1 Y 1 A LYS 7   ? CG  ? A LYS 21  CG  
10 1 Y 1 A LYS 7   ? CD  ? A LYS 21  CD  
11 1 Y 1 A LYS 7   ? CE  ? A LYS 21  CE  
12 1 Y 1 A LYS 7   ? NZ  ? A LYS 21  NZ  
13 1 Y 1 A LYS 9   ? NZ  ? A LYS 23  NZ  
14 1 Y 1 A GLU 46  ? CB  ? A GLU 60  CB  
15 1 Y 1 A GLU 46  ? CG  ? A GLU 60  CG  
16 1 Y 1 A GLU 46  ? CD  ? A GLU 60  CD  
17 1 Y 1 A GLU 46  ? OE1 ? A GLU 60  OE1 
18 1 Y 1 A GLU 46  ? OE2 ? A GLU 60  OE2 
19 1 Y 1 A ASP 47  ? CB  ? A ASP 61  CB  
20 1 Y 1 A ASP 47  ? CG  ? A ASP 61  CG  
21 1 Y 1 A ASP 47  ? OD1 ? A ASP 61  OD1 
22 1 Y 1 A ASP 47  ? OD2 ? A ASP 61  OD2 
23 1 Y 1 A LEU 50  ? CG  ? A LEU 64  CG  
24 1 Y 1 A LEU 50  ? CD1 ? A LEU 64  CD1 
25 1 Y 1 A LEU 50  ? CD2 ? A LEU 64  CD2 
26 1 Y 1 A ASP 93  ? CG  ? A ASP 107 CG  
27 1 Y 1 A ASP 93  ? OD1 ? A ASP 107 OD1 
28 1 Y 1 A ASP 93  ? OD2 ? A ASP 107 OD2 
29 1 Y 1 A LYS 111 ? CG  ? A LYS 125 CG  
30 1 Y 1 A LYS 111 ? CD  ? A LYS 125 CD  
31 1 Y 1 A LYS 111 ? CE  ? A LYS 125 CE  
32 1 Y 1 A LYS 111 ? NZ  ? A LYS 125 NZ  
33 1 Y 1 A LYS 116 ? CG  ? A LYS 130 CG  
34 1 Y 1 A LYS 116 ? CD  ? A LYS 130 CD  
35 1 Y 1 A LYS 116 ? CE  ? A LYS 130 CE  
36 1 Y 1 A LYS 116 ? NZ  ? A LYS 130 NZ  
37 1 Y 1 A LYS 117 ? CG  ? A LYS 131 CG  
38 1 Y 1 A LYS 117 ? CD  ? A LYS 131 CD  
39 1 Y 1 A LYS 117 ? CE  ? A LYS 131 CE  
40 1 Y 1 A LYS 117 ? NZ  ? A LYS 131 NZ  
41 1 Y 1 A LYS 118 ? CG  ? A LYS 132 CG  
42 1 Y 1 A LYS 118 ? CD  ? A LYS 132 CD  
43 1 Y 1 A LYS 118 ? CE  ? A LYS 132 CE  
44 1 Y 1 A LYS 118 ? NZ  ? A LYS 132 NZ  
45 1 Y 1 A ARG 260 ? CG  ? A ARG 274 CG  
46 1 Y 1 A ARG 260 ? CD  ? A ARG 274 CD  
47 1 Y 1 A ARG 260 ? NE  ? A ARG 274 NE  
48 1 Y 1 A ARG 260 ? CZ  ? A ARG 274 CZ  
49 1 Y 1 A ARG 260 ? NH1 ? A ARG 274 NH1 
50 1 Y 1 A ARG 260 ? NH2 ? A ARG 274 NH2 
51 1 Y 1 A SER 264 ? OG  ? A SER 278 OG  
52 1 Y 1 A SER 265 ? OG  ? A SER 279 OG  
53 1 Y 1 A ARG 270 ? CG  ? A ARG 284 CG  
54 1 Y 1 A ARG 270 ? CD  ? A ARG 284 CD  
55 1 Y 1 A ARG 270 ? NE  ? A ARG 284 NE  
56 1 Y 1 A ARG 270 ? CZ  ? A ARG 284 CZ  
57 1 Y 1 A ARG 270 ? NH1 ? A ARG 284 NH1 
58 1 Y 1 A ARG 270 ? NH2 ? A ARG 284 NH2 
59 1 Y 1 A LYS 271 ? CG  ? A LYS 285 CG  
60 1 Y 1 A LYS 271 ? CD  ? A LYS 285 CD  
61 1 Y 1 A LYS 271 ? CE  ? A LYS 285 CE  
62 1 Y 1 A LYS 271 ? NZ  ? A LYS 285 NZ  
63 1 Y 1 A LYS 279 ? CG  ? A LYS 293 CG  
64 1 Y 1 A LYS 279 ? CD  ? A LYS 293 CD  
65 1 Y 1 A LYS 279 ? CE  ? A LYS 293 CE  
66 1 Y 1 A LYS 279 ? NZ  ? A LYS 293 NZ  
67 1 Y 1 A ASP 280 ? CG  ? A ASP 294 CG  
68 1 Y 1 A ASP 280 ? OD1 ? A ASP 294 OD1 
69 1 Y 1 A ASP 280 ? OD2 ? A ASP 294 OD2 
70 1 Y 1 A MET 303 ? CG  ? A MET 317 CG  
71 1 Y 1 A MET 303 ? SD  ? A MET 317 SD  
72 1 Y 1 A MET 303 ? CE  ? A MET 317 CE  
73 1 Y 1 A GLN 304 ? CG  ? A GLN 318 CG  
74 1 Y 1 A GLN 304 ? CD  ? A GLN 318 CD  
75 1 Y 1 A GLN 304 ? OE1 ? A GLN 318 OE1 
76 1 Y 1 A GLN 304 ? NE2 ? A GLN 318 NE2 
77 1 Y 1 A LYS 318 ? CE  ? A LYS 332 CE  
78 1 Y 1 A LYS 318 ? NZ  ? A LYS 332 NZ  
79 1 Y 1 A LYS 320 ? CG  ? A LYS 334 CG  
80 1 Y 1 A LYS 320 ? CD  ? A LYS 334 CD  
81 1 Y 1 A LYS 320 ? CE  ? A LYS 334 CE  
82 1 Y 1 A LYS 320 ? NZ  ? A LYS 334 NZ  
83 1 Y 1 A THR 335 ? OG1 ? A THR 349 OG1 
84 1 Y 1 A THR 335 ? CG2 ? A THR 349 CG2 
85 1 Y 1 A LYS 364 ? CG  ? A LYS 378 CG  
86 1 Y 1 A LYS 364 ? CD  ? A LYS 378 CD  
87 1 Y 1 A LYS 364 ? CE  ? A LYS 378 CE  
88 1 Y 1 A LYS 364 ? NZ  ? A LYS 378 NZ  
89 1 Y 1 A GLN 392 ? OE1 ? A GLN 406 OE1 
90 1 Y 1 A LYS 429 ? CE  ? A LYS 443 CE  
91 1 Y 1 A LYS 429 ? NZ  ? A LYS 443 NZ  
92 1 Y 1 A ASP 445 ? CG  ? A ASP 459 CG  
93 1 Y 1 A ASP 445 ? OD1 ? A ASP 459 OD1 
94 1 Y 1 A ASP 445 ? OD2 ? A ASP 459 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0350 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YYG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.830 
_cell.length_a_esd                 ? 
_cell.length_b                     72.280 
_cell.length_b_esd                 ? 
_cell.length_c                     105.610 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8YYG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8YYG 
_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             1.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          27.06 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_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    '100mM tri-sodium citrate dihydrate pH 5.6, 20% PEG 4000, 20% Isopropanol, 40% Formamide' 
_exptl_crystal_grow.pdbx_pH_range   5.6-6.0 
_exptl_crystal_grow.temp            293 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YYG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.25 
_reflns.d_resolution_low                               44.7 
_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                                     112367 
_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                           93.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.10 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.25 
_reflns_shell.d_res_low                                     1.32 
_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                             17472 
_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                                  0.630 
_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]                            -0.12 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.10 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.22 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.234 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.967 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8YYG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.25 
_refine.ls_d_res_low                             44.7 
_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                     106592 
_refine.ls_number_reflns_R_free                  5586 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.93 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16734 
_refine.ls_R_factor_R_free                       0.19720 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16576 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.048 
_refine.pdbx_overall_ESU_R_Free                  0.047 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             1.734 
_refine.overall_SU_ML                            0.033 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.25 
_refine_hist.d_res_low                        44.7 
_refine_hist.number_atoms_solvent             237 
_refine_hist.number_atoms_total               3595 
_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        3357 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_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' ? 0.018  0.012  3448  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3191  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.667  1.626  4665  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.574  1.549  7417  ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.284  5.000  447   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.324  10.000 11    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.826 10.000 588   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.200  534   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  3898  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  644   ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.882  1.945  1770  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.862  1.943  1769  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.251  2.912  2211  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.250  2.914  2212  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.812  2.270  1678  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.811  2.271  1679  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.984  3.263  2451  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.067  38.622 14761 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.049  38.248 14602 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 13.851 3.000  6639  ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.250 
_refine_ls_shell.d_res_low                        1.282 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             429 
_refine_ls_shell.number_reflns_R_work             8377 
_refine_ls_shell.percent_reflns_obs               99.85 
_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                  0.316 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_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                  0.329 
# 
_struct.entry_id                     8YYG 
_struct.title                        'RNase J2 mutant H78A' 
_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        8YYG 
_struct_keywords.text            'Ribonuclease, RNase J2, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING PROTEIN' 
# 
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 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RNJ2_STAEQ 
_struct_ref.pdbx_db_accession          Q5HPR6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSLIKKKNKDIRIIPLGGVGEIAKNMYIVEVDDEMFMLDAGLMFPEDEMLGVDIVIPDIQYVIENKERLKGIFLTHGHEH
AIGAVSYVLEQIDAPVYGSKLTIALVKEAMKARNIKKKVRYYTVNHDSIMRFKNVNVSFFNTTHSIPDSLGVCIHTSYGS
IVYTGEFKFDQSLHGHYAPDLKRMAEIGDEGVFALISDSTEAEKPGYNTPENIIEHHMYDAFAKVKGRLIVSCYASNFVR
IQQVLNIASQLNRKVSFLGRSLESSFNIARKMGYFDIPKDLLIPINEVENYPKNEVIIIATGMQGEPVEALSQMARKKHK
IMNIEEGDSIFLAITASANMEVIIADTLNELVRAGAHIIPNNKKIHASSHGCMEELKMMLNIMKPEYFVPVQGEFKMQIA
HAKLAAETGVAPEKIFLVEKGDVISYNGKDMILNEKVQSGNILIDGIGVGDVGNIVLRDRHLLAEDGIFIAVVTLDPKNR
RIAAGPEIQSRGFVYVRESEELLKEAEEKVRKIVEEGLQEKRIEWSEIKQNMRDQISKLLFESTKRRPMIIPVISEI
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YYG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 15 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 571 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q5HPR6 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  557 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       557 
# 
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 8YYG MET A 1  ? UNP Q5HPR6 ?   ?  'initiating methionine' -13 1  
1 8YYG GLY A 2  ? UNP Q5HPR6 ?   ?  'expression tag'        -12 2  
1 8YYG SER A 3  ? UNP Q5HPR6 ?   ?  'expression tag'        -11 3  
1 8YYG SER A 4  ? UNP Q5HPR6 ?   ?  'expression tag'        -10 4  
1 8YYG HIS A 5  ? UNP Q5HPR6 ?   ?  'expression tag'        -9  5  
1 8YYG HIS A 6  ? UNP Q5HPR6 ?   ?  'expression tag'        -8  6  
1 8YYG HIS A 7  ? UNP Q5HPR6 ?   ?  'expression tag'        -7  7  
1 8YYG HIS A 8  ? UNP Q5HPR6 ?   ?  'expression tag'        -6  8  
1 8YYG HIS A 9  ? UNP Q5HPR6 ?   ?  'expression tag'        -5  9  
1 8YYG HIS A 10 ? UNP Q5HPR6 ?   ?  'expression tag'        -4  10 
1 8YYG SER A 11 ? UNP Q5HPR6 ?   ?  'expression tag'        -3  11 
1 8YYG GLN A 12 ? UNP Q5HPR6 ?   ?  'expression tag'        -2  12 
1 8YYG ASP A 13 ? UNP Q5HPR6 ?   ?  'expression tag'        -1  13 
1 8YYG PRO A 14 ? UNP Q5HPR6 ?   ?  'expression tag'        0   14 
1 8YYG ALA A 92 ? UNP Q5HPR6 HIS 78 'engineered mutation'   78  15 
# 
_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)' 130   ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  17970 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 ILE A 73  ? ASN A 79  ? ILE A 59  ASN A 65  1 ? 7  
HELX_P HELX_P2  AA2 ALA A 92  ? GLY A 97  ? ALA A 78  GLY A 83  1 ? 6  
HELX_P HELX_P3  AA3 ALA A 98  ? ILE A 106 ? ALA A 84  ILE A 92  1 ? 9  
HELX_P HELX_P4  AA4 SER A 113 ? ARG A 127 ? SER A 99  ARG A 113 1 ? 15 
HELX_P HELX_P5  AA5 HIS A 188 ? ALA A 192 ? HIS A 174 ALA A 178 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 194 ? GLY A 205 ? ASP A 180 GLY A 191 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 224 ? LYS A 238 ? PRO A 210 LYS A 224 1 ? 15 
HELX_P HELX_P8  AA8 ASN A 251 ? LEU A 265 ? ASN A 237 LEU A 251 1 ? 15 
HELX_P HELX_P9  AA9 SER A 278 ? MET A 286 ? SER A 264 MET A 272 1 ? 9  
HELX_P HELX_P10 AB1 PRO A 298 ? TYR A 305 ? PRO A 284 TYR A 291 5 ? 8  
HELX_P HELX_P11 AB2 PRO A 306 ? ASN A 308 ? PRO A 292 ASN A 294 5 ? 3  
HELX_P HELX_P12 AB3 GLU A 320 ? ARG A 330 ? GLU A 306 ARG A 316 1 ? 11 
HELX_P HELX_P13 AB4 MET A 354 ? ALA A 368 ? MET A 340 ALA A 354 1 ? 15 
HELX_P HELX_P14 AB5 CYS A 386 ? LYS A 398 ? CYS A 372 LYS A 384 1 ? 13 
HELX_P HELX_P15 AB6 GLU A 408 ? GLY A 423 ? GLU A 394 GLY A 409 1 ? 16 
HELX_P HELX_P16 AB7 ALA A 425 ? ILE A 429 ? ALA A 411 ILE A 415 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 
metalc1 metalc ? ? A HIS 90  NE2 ? ? ? 1_555 B MN  . MN ? ? A HIS 76  A MN  601 1_555 ? ? ? ? ? ? ? 2.532 ? ? 
metalc2 metalc ? ? A HIS 158 NE2 ? ? ? 1_555 B MN  . MN ? ? A HIS 144 A MN  601 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc3 metalc ? ? A GLU 180 OE1 ? ? ? 1_555 B MN  . MN ? ? A GLU 166 A MN  601 1_555 ? ? ? ? ? ? ? 1.915 ? ? 
metalc4 metalc ? ? B MN  .   MN  ? ? ? 1_555 C HOH . O  ? ? A MN  601 A HOH 871 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc5 metalc ? ? B MN  .   MN  ? ? ? 1_555 C HOH . O  ? ? A MN  601 A HOH 878 1_555 ? ? ? ? ? ? ? 2.212 ? ? 
metalc6 metalc ? ? B MN  .   MN  ? ? ? 1_555 C HOH . O  ? ? A MN  601 A HOH 882 1_555 ? ? ? ? ? ? ? 2.192 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 90  ? A HIS 76  ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 NE2 ? A HIS 158 ? A HIS 144 ? 1_555 92.0  ? 
2  NE2 ? A HIS 90  ? A HIS 76  ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 OE1 ? A GLU 180 ? A GLU 166 ? 1_555 80.7  ? 
3  NE2 ? A HIS 158 ? A HIS 144 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 OE1 ? A GLU 180 ? A GLU 166 ? 1_555 103.6 ? 
4  NE2 ? A HIS 90  ? A HIS 76  ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 871 ? 1_555 169.8 ? 
5  NE2 ? A HIS 158 ? A HIS 144 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 871 ? 1_555 89.4  ? 
6  OE1 ? A GLU 180 ? A GLU 166 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 871 ? 1_555 89.1  ? 
7  NE2 ? A HIS 90  ? A HIS 76  ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 878 ? 1_555 127.1 ? 
8  NE2 ? A HIS 158 ? A HIS 144 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 878 ? 1_555 88.9  ? 
9  OE1 ? A GLU 180 ? A GLU 166 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 878 ? 1_555 149.6 ? 
10 O   ? C HOH .   ? A HOH 871 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 878 ? 1_555 63.0  ? 
11 NE2 ? A HIS 90  ? A HIS 76  ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 882 ? 1_555 107.5 ? 
12 NE2 ? A HIS 158 ? A HIS 144 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 882 ? 1_555 153.7 ? 
13 OE1 ? A GLU 180 ? A GLU 166 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 882 ? 1_555 96.9  ? 
14 O   ? C HOH .   ? A HOH 871 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 882 ? 1_555 74.4  ? 
15 O   ? C HOH .   ? A HOH 878 ? 1_555 MN ? B MN . ? A MN 601 ? 1_555 O   ? C HOH .   ? A HOH 882 ? 1_555 65.4  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 5 ? 
# 
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 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? 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 TYR A 135 ? THR A 137 ? TYR A 121 THR A 123 
AA1 2 VAL A 110 ? GLY A 112 ? VAL A 96  GLY A 98  
AA1 3 LEU A 83  ? PHE A 87  ? LEU A 69  PHE A 73  
AA1 4 GLU A 48  ? LEU A 52  ? GLU A 34  LEU A 38  
AA1 5 MET A 40  ? VAL A 45  ? MET A 26  VAL A 31  
AA1 6 ILE A 25  ? GLY A 31  ? ILE A 11  GLY A 17  
AA1 7 ASP A 436 ? TYR A 440 ? ASP A 422 TYR A 426 
AA1 8 MET A 445 ? LYS A 450 ? MET A 431 LYS A 436 
AA2 1 ILE A 68  ? PRO A 71  ? ILE A 54  PRO A 57  
AA2 2 ASN A 455 ? ILE A 458 ? ASN A 441 ILE A 444 
AA3 1 ILE A 143 ? ARG A 145 ? ILE A 129 ARG A 131 
AA3 2 ASN A 150 ? THR A 156 ? ASN A 136 THR A 142 
AA3 3 SER A 163 ? THR A 170 ? SER A 149 THR A 156 
AA3 4 GLY A 173 ? TYR A 177 ? GLY A 159 TYR A 163 
AA3 5 VAL A 206 ? ASP A 212 ? VAL A 192 ASP A 198 
AA3 6 TYR A 401 ? VAL A 405 ? TYR A 387 VAL A 391 
AA4 1 LYS A 268 ? GLY A 273 ? LYS A 254 GLY A 259 
AA4 2 VAL A 310 ? GLY A 316 ? VAL A 296 GLY A 302 
AA4 3 LEU A 243 ? CYS A 247 ? LEU A 229 CYS A 233 
AA4 4 SER A 343 ? ALA A 347 ? SER A 329 ALA A 333 
AA4 5 HIS A 371 ? ILE A 372 ? HIS A 357 ILE A 358 
# 
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 O TYR A 136 ? O TYR A 122 N VAL A 110 ? N VAL A 96  
AA1 2 3 O TYR A 111 ? O TYR A 97  N ILE A 86  ? N ILE A 72  
AA1 3 4 O LYS A 84  ? O LYS A 70  N MET A 49  ? N MET A 35  
AA1 4 5 O LEU A 52  ? O LEU A 38  N TYR A 41  ? N TYR A 27  
AA1 5 6 O ILE A 42  ? O ILE A 28  N ILE A 28  ? N ILE A 14  
AA1 6 7 N ILE A 27  ? N ILE A 13  O ILE A 438 ? O ILE A 424 
AA1 7 8 N SER A 439 ? N SER A 425 O ILE A 446 ? O ILE A 432 
AA2 1 2 N ILE A 68  ? N ILE A 54  O ILE A 458 ? O ILE A 444 
AA3 1 2 N MET A 144 ? N MET A 130 O VAL A 151 ? O VAL A 137 
AA3 2 3 N ASN A 150 ? N ASN A 136 O HIS A 169 ? O HIS A 155 
AA3 3 4 N ILE A 168 ? N ILE A 154 O ILE A 175 ? O ILE A 161 
AA3 4 5 N VAL A 176 ? N VAL A 162 O ILE A 210 ? O ILE A 196 
AA3 5 6 N LEU A 209 ? N LEU A 195 O VAL A 403 ? O VAL A 389 
AA4 1 2 N LEU A 272 ? N LEU A 258 O ILE A 313 ? O ILE A 299 
AA4 2 3 O ILE A 312 ? O ILE A 298 N VAL A 245 ? N VAL A 231 
AA4 3 4 N SER A 246 ? N SER A 232 O ALA A 347 ? O ALA A 333 
AA4 4 5 N ILE A 344 ? N ILE A 330 O HIS A 371 ? O HIS A 357 
# 
_pdbx_entry_details.entry_id                   8YYG 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 824 ? ? O A HOH 871 ? ? 2.09 
2 1 O A HOH 838 ? ? O A HOH 882 ? ? 2.11 
3 1 O A HOH 848 ? ? O A HOH 903 ? ? 2.13 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CE1 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             76 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            NE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             76 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.163 
_pdbx_validate_rmsd_bond.bond_target_value         1.317 
_pdbx_validate_rmsd_bond.bond_deviation            -0.154 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A HIS 76  ? ? CG A HIS 76  ? ? CD2 A HIS 76  ? ? 140.69 131.40 9.29  1.20 N 
2 1 NE A ARG 240 ? ? CZ A ARG 240 ? ? NH2 A ARG 240 ? ? 116.68 120.30 -3.62 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 23  ? ? -106.41 -161.72 
2 1 MET A 26  ? ? -164.63 113.86  
3 1 ASP A 32  ? ? 46.29   -124.28 
4 1 ASP A 39  ? ? 67.51   161.19  
5 1 ALA A 40  ? ? -158.99 71.19   
6 1 ALA A 333 ? ? -104.97 63.81   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 113 ? ? 0.077 'SIDE CHAIN' 
2 1 ARG A 131 ? ? 0.081 'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 935 ? 6.31 . 
2 1 O ? A HOH 936 ? 6.98 . 
3 1 O ? A HOH 937 ? 8.22 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -13 ? A MET 1   
2   1 Y 1 A GLY -12 ? A GLY 2   
3   1 Y 1 A SER -11 ? A SER 3   
4   1 Y 1 A SER -10 ? A SER 4   
5   1 Y 1 A HIS -9  ? A HIS 5   
6   1 Y 1 A HIS -8  ? A HIS 6   
7   1 Y 1 A HIS -7  ? A HIS 7   
8   1 Y 1 A HIS -6  ? A HIS 8   
9   1 Y 1 A HIS -5  ? A HIS 9   
10  1 Y 1 A HIS -4  ? A HIS 10  
11  1 Y 1 A SER -3  ? A SER 11  
12  1 Y 1 A GLN -2  ? A GLN 12  
13  1 Y 1 A ASP -1  ? A ASP 13  
14  1 Y 1 A PRO 0   ? A PRO 14  
15  1 Y 1 A MET 1   ? A MET 15  
16  1 Y 1 A SER 2   ? A SER 16  
17  1 Y 1 A LEU 3   ? A LEU 17  
18  1 Y 1 A GLU 48  ? A GLU 62  
19  1 Y 1 A SER 261 ? A SER 275 
20  1 Y 1 A LEU 262 ? A LEU 276 
21  1 Y 1 A ILE 447 ? A ILE 461 
22  1 Y 1 A GLY 448 ? A GLY 462 
23  1 Y 1 A VAL 449 ? A VAL 463 
24  1 Y 1 A GLY 450 ? A GLY 464 
25  1 Y 1 A ASP 451 ? A ASP 465 
26  1 Y 1 A VAL 452 ? A VAL 466 
27  1 Y 1 A GLY 453 ? A GLY 467 
28  1 Y 1 A ASN 454 ? A ASN 468 
29  1 Y 1 A ILE 455 ? A ILE 469 
30  1 Y 1 A VAL 456 ? A VAL 470 
31  1 Y 1 A LEU 457 ? A LEU 471 
32  1 Y 1 A ARG 458 ? A ARG 472 
33  1 Y 1 A ASP 459 ? A ASP 473 
34  1 Y 1 A ARG 460 ? A ARG 474 
35  1 Y 1 A HIS 461 ? A HIS 475 
36  1 Y 1 A LEU 462 ? A LEU 476 
37  1 Y 1 A LEU 463 ? A LEU 477 
38  1 Y 1 A ALA 464 ? A ALA 478 
39  1 Y 1 A GLU 465 ? A GLU 479 
40  1 Y 1 A ASP 466 ? A ASP 480 
41  1 Y 1 A GLY 467 ? A GLY 481 
42  1 Y 1 A ILE 468 ? A ILE 482 
43  1 Y 1 A PHE 469 ? A PHE 483 
44  1 Y 1 A ILE 470 ? A ILE 484 
45  1 Y 1 A ALA 471 ? A ALA 485 
46  1 Y 1 A VAL 472 ? A VAL 486 
47  1 Y 1 A VAL 473 ? A VAL 487 
48  1 Y 1 A THR 474 ? A THR 488 
49  1 Y 1 A LEU 475 ? A LEU 489 
50  1 Y 1 A ASP 476 ? A ASP 490 
51  1 Y 1 A PRO 477 ? A PRO 491 
52  1 Y 1 A LYS 478 ? A LYS 492 
53  1 Y 1 A ASN 479 ? A ASN 493 
54  1 Y 1 A ARG 480 ? A ARG 494 
55  1 Y 1 A ARG 481 ? A ARG 495 
56  1 Y 1 A ILE 482 ? A ILE 496 
57  1 Y 1 A ALA 483 ? A ALA 497 
58  1 Y 1 A ALA 484 ? A ALA 498 
59  1 Y 1 A GLY 485 ? A GLY 499 
60  1 Y 1 A PRO 486 ? A PRO 500 
61  1 Y 1 A GLU 487 ? A GLU 501 
62  1 Y 1 A ILE 488 ? A ILE 502 
63  1 Y 1 A GLN 489 ? A GLN 503 
64  1 Y 1 A SER 490 ? A SER 504 
65  1 Y 1 A ARG 491 ? A ARG 505 
66  1 Y 1 A GLY 492 ? A GLY 506 
67  1 Y 1 A PHE 493 ? A PHE 507 
68  1 Y 1 A VAL 494 ? A VAL 508 
69  1 Y 1 A TYR 495 ? A TYR 509 
70  1 Y 1 A VAL 496 ? A VAL 510 
71  1 Y 1 A ARG 497 ? A ARG 511 
72  1 Y 1 A GLU 498 ? A GLU 512 
73  1 Y 1 A SER 499 ? A SER 513 
74  1 Y 1 A GLU 500 ? A GLU 514 
75  1 Y 1 A GLU 501 ? A GLU 515 
76  1 Y 1 A LEU 502 ? A LEU 516 
77  1 Y 1 A LEU 503 ? A LEU 517 
78  1 Y 1 A LYS 504 ? A LYS 518 
79  1 Y 1 A GLU 505 ? A GLU 519 
80  1 Y 1 A ALA 506 ? A ALA 520 
81  1 Y 1 A GLU 507 ? A GLU 521 
82  1 Y 1 A GLU 508 ? A GLU 522 
83  1 Y 1 A LYS 509 ? A LYS 523 
84  1 Y 1 A VAL 510 ? A VAL 524 
85  1 Y 1 A ARG 511 ? A ARG 525 
86  1 Y 1 A LYS 512 ? A LYS 526 
87  1 Y 1 A ILE 513 ? A ILE 527 
88  1 Y 1 A VAL 514 ? A VAL 528 
89  1 Y 1 A GLU 515 ? A GLU 529 
90  1 Y 1 A GLU 516 ? A GLU 530 
91  1 Y 1 A GLY 517 ? A GLY 531 
92  1 Y 1 A LEU 518 ? A LEU 532 
93  1 Y 1 A GLN 519 ? A GLN 533 
94  1 Y 1 A GLU 520 ? A GLU 534 
95  1 Y 1 A LYS 521 ? A LYS 535 
96  1 Y 1 A ARG 522 ? A ARG 536 
97  1 Y 1 A ILE 523 ? A ILE 537 
98  1 Y 1 A GLU 524 ? A GLU 538 
99  1 Y 1 A TRP 525 ? A TRP 539 
100 1 Y 1 A SER 526 ? A SER 540 
101 1 Y 1 A GLU 527 ? A GLU 541 
102 1 Y 1 A ILE 528 ? A ILE 542 
103 1 Y 1 A LYS 529 ? A LYS 543 
104 1 Y 1 A GLN 530 ? A GLN 544 
105 1 Y 1 A ASN 531 ? A ASN 545 
106 1 Y 1 A MET 532 ? A MET 546 
107 1 Y 1 A ARG 533 ? A ARG 547 
108 1 Y 1 A ASP 534 ? A ASP 548 
109 1 Y 1 A GLN 535 ? A GLN 549 
110 1 Y 1 A ILE 536 ? A ILE 550 
111 1 Y 1 A SER 537 ? A SER 551 
112 1 Y 1 A LYS 538 ? A LYS 552 
113 1 Y 1 A LEU 539 ? A LEU 553 
114 1 Y 1 A LEU 540 ? A LEU 554 
115 1 Y 1 A PHE 541 ? A PHE 555 
116 1 Y 1 A GLU 542 ? A GLU 556 
117 1 Y 1 A SER 543 ? A SER 557 
118 1 Y 1 A THR 544 ? A THR 558 
119 1 Y 1 A LYS 545 ? A LYS 559 
120 1 Y 1 A ARG 546 ? A ARG 560 
121 1 Y 1 A ARG 547 ? A ARG 561 
122 1 Y 1 A PRO 548 ? A PRO 562 
123 1 Y 1 A MET 549 ? A MET 563 
124 1 Y 1 A ILE 550 ? A ILE 564 
125 1 Y 1 A ILE 551 ? A ILE 565 
126 1 Y 1 A PRO 552 ? A PRO 566 
127 1 Y 1 A VAL 553 ? A VAL 567 
128 1 Y 1 A ILE 554 ? A ILE 568 
129 1 Y 1 A SER 555 ? A SER 569 
130 1 Y 1 A GLU 556 ? A GLU 570 
131 1 Y 1 A ILE 557 ? A ILE 571 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
MN  MN   MN N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Science and Engineering Research Board (SERB)'   India FA/DSTO-17-0001.03 1 
'Department of Science & Technology (DST, India)' India SP/DSTO-16-1668.03 2 
'Science and Engineering Research Board (SERB)'   India SP/SERB-23-0307.26 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6K6W 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YYG 
_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]   0.017596 
_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]   0.013835 
_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]   0.009469 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MN 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ILE A 1 18  ? 12.572  27.278  29.231  1.00 34.20  ? 4   ILE A N   1 
ATOM   2    C  CA  . ILE A 1 18  ? 11.238  26.710  28.861  1.00 32.65  ? 4   ILE A CA  1 
ATOM   3    C  C   . ILE A 1 18  ? 11.407  25.966  27.531  1.00 30.46  ? 4   ILE A C   1 
ATOM   4    O  O   . ILE A 1 18  ? 11.688  26.585  26.508  1.00 39.37  ? 4   ILE A O   1 
ATOM   5    C  CB  . ILE A 1 18  ? 10.134  27.793  28.731  1.00 37.24  ? 4   ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 18  ? 10.006  28.706  29.955  1.00 37.33  ? 4   ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 18  ? 8.785   27.161  28.366  1.00 34.64  ? 4   ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 18  ? 9.098   29.900  29.725  1.00 36.84  ? 4   ILE A CD1 1 
ATOM   9    N  N   . LYS A 1 19  ? 11.262  24.637  27.548  1.00 30.09  ? 5   LYS A N   1 
ATOM   10   C  CA  . LYS A 1 19  ? 11.262  23.842  26.331  1.00 29.84  ? 5   LYS A CA  1 
ATOM   11   C  C   . LYS A 1 19  ? 9.813   23.712  25.850  1.00 39.39  ? 5   LYS A C   1 
ATOM   12   O  O   . LYS A 1 19  ? 8.882   23.668  26.659  1.00 35.41  ? 5   LYS A O   1 
ATOM   13   C  CB  . LYS A 1 19  ? 11.881  22.462  26.592  1.00 36.37  ? 5   LYS A CB  1 
ATOM   14   N  N   . LYS A 1 20  ? 9.631   23.660  24.524  1.00 36.79  ? 6   LYS A N   1 
ATOM   15   C  CA  . LYS A 1 20  ? 8.326   23.437  23.923  1.00 33.77  ? 6   LYS A CA  1 
ATOM   16   C  C   . LYS A 1 20  ? 7.885   22.019  24.273  1.00 29.82  ? 6   LYS A C   1 
ATOM   17   O  O   . LYS A 1 20  ? 8.682   21.088  24.184  1.00 35.74  ? 6   LYS A O   1 
ATOM   18   C  CB  . LYS A 1 20  ? 8.385   23.653  22.406  1.00 33.95  ? 6   LYS A CB  1 
ATOM   19   N  N   . LYS A 1 21  ? 6.649   21.887  24.761  1.00 27.84  ? 7   LYS A N   1 
ATOM   20   C  CA  . LYS A 1 21  ? 6.056   20.608  25.094  1.00 23.26  ? 7   LYS A CA  1 
ATOM   21   C  C   . LYS A 1 21  ? 4.713   20.468  24.393  1.00 22.89  ? 7   LYS A C   1 
ATOM   22   O  O   . LYS A 1 21  ? 3.942   21.416  24.273  1.00 26.75  ? 7   LYS A O   1 
ATOM   23   C  CB  . LYS A 1 21  ? 5.790   20.489  26.585  1.00 27.41  ? 7   LYS A CB  1 
ATOM   24   N  N   . ASN A 1 22  ? 4.377   19.239  23.996  1.00 18.28  ? 8   ASN A N   1 
ATOM   25   C  CA  . ASN A 1 22  ? 3.080   18.975  23.377  1.00 19.78  ? 8   ASN A CA  1 
ATOM   26   C  C   . ASN A 1 22  ? 1.980   18.814  24.430  1.00 19.05  ? 8   ASN A C   1 
ATOM   27   O  O   . ASN A 1 22  ? 2.202   18.296  25.532  1.00 23.24  ? 8   ASN A O   1 
ATOM   28   C  CB  . ASN A 1 22  ? 3.185   17.733  22.493  1.00 18.49  ? 8   ASN A CB  1 
ATOM   29   C  CG  . ASN A 1 22  ? 4.334   17.819  21.515  1.00 17.11  ? 8   ASN A CG  1 
ATOM   30   O  OD1 . ASN A 1 22  ? 5.167   16.901  21.430  1.00 20.38  ? 8   ASN A OD1 1 
ATOM   31   N  ND2 . ASN A 1 22  ? 4.420   18.897  20.762  1.00 18.92  ? 8   ASN A ND2 1 
ATOM   32   N  N   . LYS A 1 23  ? 0.754   19.147  24.034  1.00 18.95  ? 9   LYS A N   1 
ATOM   33   C  CA  . LYS A 1 23  ? -0.367  19.035  24.935  1.00 18.49  ? 9   LYS A CA  1 
ATOM   34   C  C   . LYS A 1 23  ? -1.430  18.074  24.406  1.00 16.09  ? 9   LYS A C   1 
ATOM   35   O  O   . LYS A 1 23  ? -1.858  17.180  25.103  1.00 18.49  ? 9   LYS A O   1 
ATOM   36   C  CB  . LYS A 1 23  ? -0.955  20.417  25.223  1.00 22.86  ? 9   LYS A CB  1 
ATOM   37   C  CG  . LYS A 1 23  ? -2.183  20.385  26.134  1.00 24.18  ? 9   LYS A CG  1 
ATOM   38   C  CD  . LYS A 1 23  ? -2.443  21.701  26.848  1.00 39.03  ? 9   LYS A CD  1 
ATOM   39   C  CE  . LYS A 1 23  ? -2.258  22.908  25.951  1.00 39.80  ? 9   LYS A CE  1 
ATOM   40   N  N   . ASP A 1 24  ? -1.935  18.329  23.199  1.00 18.55  ? 10  ASP A N   1 
ATOM   41   C  CA  . ASP A 1 24  ? -3.109  17.652  22.689  1.00 16.30  ? 10  ASP A CA  1 
ATOM   42   C  C   . ASP A 1 24  ? -2.737  16.865  21.434  1.00 16.11  ? 10  ASP A C   1 
ATOM   43   O  O   . ASP A 1 24  ? -2.038  17.370  20.543  1.00 17.73  ? 10  ASP A O   1 
ATOM   44   C  CB  . ASP A 1 24  ? -4.221  18.649  22.363  1.00 17.91  ? 10  ASP A CB  1 
ATOM   45   C  CG  . ASP A 1 24  ? -4.702  19.428  23.579  1.00 21.83  ? 10  ASP A CG  1 
ATOM   46   O  OD1 . ASP A 1 24  ? -5.075  18.780  24.550  1.00 24.06  ? 10  ASP A OD1 1 
ATOM   47   O  OD2 . ASP A 1 24  ? -4.762  20.673  23.508  1.00 30.42  ? 10  ASP A OD2 1 
ATOM   48   N  N   . ILE A 1 25  ? -3.198  15.620  21.388  1.00 14.69  ? 11  ILE A N   1 
ATOM   49   C  CA  . ILE A 1 25  ? -2.996  14.752  20.236  1.00 14.47  ? 11  ILE A CA  1 
ATOM   50   C  C   . ILE A 1 25  ? -4.367  14.345  19.696  1.00 12.99  ? 11  ILE A C   1 
ATOM   51   O  O   . ILE A 1 25  ? -5.238  14.017  20.502  1.00 14.28  ? 11  ILE A O   1 
ATOM   52   C  CB  . ILE A 1 25  ? -2.221  13.489  20.648  1.00 14.93  ? 11  ILE A CB  1 
ATOM   53   C  CG1 . ILE A 1 25  ? -0.981  13.844  21.452  1.00 21.66  ? 11  ILE A CG1 1 
ATOM   54   C  CG2 . ILE A 1 25  ? -2.020  12.572  19.430  1.00 15.88  ? 11  ILE A CG2 1 
ATOM   55   C  CD1 . ILE A 1 25  ? 0.004   14.629  20.724  1.00 21.41  ? 11  ILE A CD1 1 
ATOM   56   N  N   . ARG A 1 26  ? -4.506  14.279  18.367  1.00 12.33  ? 12  ARG A N   1 
ATOM   57   C  CA  . ARG A 1 26  ? -5.660  13.651  17.729  1.00 12.11  ? 12  ARG A CA  1 
ATOM   58   C  C   . ARG A 1 26  ? -5.200  12.644  16.683  1.00 10.66  ? 12  ARG A C   1 
ATOM   59   O  O   . ARG A 1 26  ? -4.253  12.919  15.965  1.00 11.37  ? 12  ARG A O   1 
ATOM   60   C  CB  . ARG A 1 26  ? -6.563  14.702  17.052  1.00 13.58  ? 12  ARG A CB  1 
ATOM   61   C  CG  . ARG A 1 26  ? -7.210  15.666  18.054  1.00 15.93  ? 12  ARG A CG  1 
ATOM   62   C  CD  . ARG A 1 26  ? -7.605  17.003  17.466  1.00 17.20  ? 12  ARG A CD  1 
ATOM   63   N  NE  . ARG A 1 26  ? -8.646  16.904  16.440  1.00 15.53  ? 12  ARG A NE  1 
ATOM   64   C  CZ  . ARG A 1 26  ? -9.961  16.945  16.684  1.00 14.57  ? 12  ARG A CZ  1 
ATOM   65   N  NH1 . ARG A 1 26  ? -10.424 16.943  17.930  1.00 17.31  ? 12  ARG A NH1 1 
ATOM   66   N  NH2 . ARG A 1 26  ? -10.778 16.995  15.646  1.00 16.28  ? 12  ARG A NH2 1 
ATOM   67   N  N   . ILE A 1 27  ? -5.841  11.490  16.626  1.00 11.01  ? 13  ILE A N   1 
ATOM   68   C  CA  . ILE A 1 27  ? -5.636  10.503  15.573  1.00 10.62  ? 13  ILE A CA  1 
ATOM   69   C  C   . ILE A 1 27  ? -7.000  10.206  14.944  1.00 9.88   ? 13  ILE A C   1 
ATOM   70   O  O   . ILE A 1 27  ? -7.931  9.808   15.658  1.00 11.05  ? 13  ILE A O   1 
ATOM   71   C  CB  . ILE A 1 27  ? -4.990  9.214   16.146  1.00 11.59  ? 13  ILE A CB  1 
ATOM   72   C  CG1 . ILE A 1 27  ? -3.635  9.533   16.804  1.00 13.96  ? 13  ILE A CG1 1 
ATOM   73   C  CG2 . ILE A 1 27  ? -4.892  8.144   15.062  1.00 12.88  ? 13  ILE A CG2 1 
ATOM   74   C  CD1 . ILE A 1 27  ? -3.117  8.413   17.660  1.00 13.49  ? 13  ILE A CD1 1 
ATOM   75   N  N   . ILE A 1 28  ? -7.092  10.410  13.649  1.00 9.26   ? 14  ILE A N   1 
ATOM   76   C  CA  . ILE A 1 28  ? -8.358  10.322  12.936  1.00 10.04  ? 14  ILE A CA  1 
ATOM   77   C  C   . ILE A 1 28  ? -8.195  9.533   11.640  1.00 9.42   ? 14  ILE A C   1 
ATOM   78   O  O   . ILE A 1 28  ? -7.573  9.995   10.679  1.00 10.21  ? 14  ILE A O   1 
ATOM   79   C  CB  . ILE A 1 28  ? -8.842  11.747  12.582  1.00 11.13  ? 14  ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 28  ? -8.931  12.668  13.810  1.00 10.77  ? 14  ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 28  ? -10.180 11.639  11.851  1.00 12.45  ? 14  ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 28  ? -9.239  14.138  13.499  1.00 14.08  ? 14  ILE A CD1 1 
ATOM   83   N  N   . PRO A 1 29  ? -8.778  8.332   11.568  1.00 9.58   ? 15  PRO A N   1 
ATOM   84   C  CA  . PRO A 1 29  ? -8.747  7.619   10.293  1.00 9.92   ? 15  PRO A CA  1 
ATOM   85   C  C   . PRO A 1 29  ? -9.762  8.203   9.310   1.00 10.09  ? 15  PRO A C   1 
ATOM   86   O  O   . PRO A 1 29  ? -10.961 8.290   9.656   1.00 11.89  ? 15  PRO A O   1 
ATOM   87   C  CB  . PRO A 1 29  ? -9.150  6.186   10.712  1.00 11.19  ? 15  PRO A CB  1 
ATOM   88   C  CG  . PRO A 1 29  ? -10.058 6.383   11.889  1.00 13.98  ? 15  PRO A CG  1 
ATOM   89   C  CD  . PRO A 1 29  ? -9.448  7.571   12.626  1.00 12.32  ? 15  PRO A CD  1 
ATOM   90   N  N   . LEU A 1 30  ? -9.347  8.554   8.108   1.00 9.31   ? 16  LEU A N   1 
ATOM   91   C  CA  . LEU A 1 30  ? -10.266 8.958   7.063   1.00 9.34   ? 16  LEU A CA  1 
ATOM   92   C  C   . LEU A 1 30  ? -10.464 7.897   6.015   1.00 9.96   ? 16  LEU A C   1 
ATOM   93   O  O   . LEU A 1 30  ? -11.364 8.011   5.195   1.00 11.10  ? 16  LEU A O   1 
ATOM   94   C  CB  . LEU A 1 30  ? -9.830  10.298  6.461   1.00 11.36  ? 16  LEU A CB  1 
ATOM   95   C  CG  . LEU A 1 30  ? -9.940  11.516  7.403   1.00 10.31  ? 16  LEU A CG  1 
ATOM   96   C  CD1 . LEU A 1 30  ? -9.479  12.748  6.624   1.00 11.92  ? 16  LEU A CD1 1 
ATOM   97   C  CD2 . LEU A 1 30  ? -11.349 11.709  7.928   1.00 11.46  ? 16  LEU A CD2 1 
ATOM   98   N  N   . GLY A 1 31  ? -9.639  6.855   6.024   1.00 9.70   ? 17  GLY A N   1 
ATOM   99   C  CA  . GLY A 1 31  ? -9.764  5.700   5.135   1.00 10.56  ? 17  GLY A CA  1 
ATOM   100  C  C   . GLY A 1 31  ? -8.865  4.607   5.674   1.00 9.94   ? 17  GLY A C   1 
ATOM   101  O  O   . GLY A 1 31  ? -7.901  4.866   6.402   1.00 10.45  ? 17  GLY A O   1 
ATOM   102  N  N   . GLY A 1 32  ? -9.254  3.355   5.429   1.00 10.10  ? 18  GLY A N   1 
ATOM   103  C  CA  . GLY A 1 32  ? -8.409  2.213   5.753   1.00 9.24   ? 18  GLY A CA  1 
ATOM   104  C  C   . GLY A 1 32  ? -8.903  1.456   6.972   1.00 10.59  ? 18  GLY A C   1 
ATOM   105  O  O   . GLY A 1 32  ? -8.250  0.493   7.378   1.00 11.16  ? 18  GLY A O   1 
ATOM   106  N  N   . VAL A 1 33  ? -10.046 1.816   7.533   1.00 10.34  ? 19  VAL A N   1 
ATOM   107  C  CA  . VAL A 1 33  ? -10.688 1.060   8.598   1.00 11.98  ? 19  VAL A CA  1 
ATOM   108  C  C   . VAL A 1 33  ? -12.104 0.747   8.147   1.00 12.89  ? 19  VAL A C   1 
ATOM   109  O  O   . VAL A 1 33  ? -12.731 1.513   7.449   1.00 13.95  ? 19  VAL A O   1 
ATOM   110  C  CB  . VAL A 1 33  ? -10.633 1.760   9.959   1.00 12.35  ? 19  VAL A CB  1 
ATOM   111  C  CG1 . VAL A 1 33  ? -9.218  1.959   10.425  1.00 12.68  ? 19  VAL A CG1 1 
ATOM   112  C  CG2 . VAL A 1 33  ? -11.325 3.115   9.913   1.00 13.33  ? 19  VAL A CG2 1 
ATOM   113  N  N   . GLY A 1 34  ? -12.550 -0.472  8.446   1.00 13.67  ? 20  GLY A N   1 
ATOM   114  C  CA  . GLY A 1 34  ? -13.785 -1.004  7.926   1.00 15.12  ? 20  GLY A CA  1 
ATOM   115  C  C   . GLY A 1 34  ? -13.667 -1.388  6.468   1.00 15.83  ? 20  GLY A C   1 
ATOM   116  O  O   . GLY A 1 34  ? -14.676 -1.619  5.795   1.00 20.90  ? 20  GLY A O   1 
ATOM   117  N  N   . GLU A 1 35  ? -12.412 -1.585  6.044   1.00 13.42  ? 21  GLU A N   1 
ATOM   118  C  CA  . GLU A 1 35  ? -12.035 -1.889  4.640   1.00 14.73  ? 21  GLU A CA  1 
ATOM   119  C  C   . GLU A 1 35  ? -10.510 -2.144  4.630   1.00 13.05  ? 21  GLU A C   1 
ATOM   120  O  O   . GLU A 1 35  ? -9.902  -1.867  5.633   1.00 14.49  ? 21  GLU A O   1 
ATOM   121  C  CB  . GLU A 1 35  ? -12.427 -0.681  3.783   1.00 16.76  ? 21  GLU A CB  1 
ATOM   122  C  CG  . GLU A 1 35  ? -11.602 0.566   4.098   1.00 14.09  ? 21  GLU A CG  1 
ATOM   123  C  CD  . GLU A 1 35  ? -12.254 1.924   3.884   1.00 14.91  ? 21  GLU A CD  1 
ATOM   124  O  OE1 . GLU A 1 35  ? -11.528 2.928   3.903   1.00 14.30  ? 21  GLU A OE1 1 
ATOM   125  O  OE2 . GLU A 1 35  ? -13.481 1.975   3.689   1.00 18.42  ? 21  GLU A OE2 1 
ATOM   126  N  N   . ILE A 1 36  ? -9.878  -2.623  3.536   1.00 20.67  ? 22  ILE A N   1 
ATOM   127  C  CA  . ILE A 1 36  ? -8.391  -2.870  3.640   1.00 21.89  ? 22  ILE A CA  1 
ATOM   128  C  C   . ILE A 1 36  ? -7.501  -1.930  2.809   1.00 24.48  ? 22  ILE A C   1 
ATOM   129  O  O   . ILE A 1 36  ? -6.256  -1.963  3.030   1.00 35.16  ? 22  ILE A O   1 
ATOM   130  C  CB  . ILE A 1 36  ? -8.004  -4.321  3.293   1.00 30.00  ? 22  ILE A CB  1 
ATOM   131  C  CG1 . ILE A 1 36  ? -8.676  -4.769  1.997   1.00 30.00  ? 22  ILE A CG1 1 
ATOM   132  C  CG2 . ILE A 1 36  ? -8.290  -5.263  4.446   1.00 30.00  ? 22  ILE A CG2 1 
ATOM   133  C  CD1 . ILE A 1 36  ? -7.856  -4.476  0.774   1.00 30.00  ? 22  ILE A CD1 1 
ATOM   134  N  N   . ALA A 1 37  ? -8.084  -1.182  1.902   1.00 14.86  ? 23  ALA A N   1 
ATOM   135  C  CA  . ALA A 1 37  ? -7.316  -0.254  1.052   1.00 13.98  ? 23  ALA A CA  1 
ATOM   136  C  C   . ALA A 1 37  ? -7.571  1.192   1.515   1.00 14.55  ? 23  ALA A C   1 
ATOM   137  O  O   . ALA A 1 37  ? -7.985  1.356   2.653   1.00 16.74  ? 23  ALA A O   1 
ATOM   138  C  CB  . ALA A 1 37  ? -7.749  -0.473  -0.378  1.00 19.68  ? 23  ALA A CB  1 
ATOM   139  N  N   . LYS A 1 38  ? -7.280  2.188   0.673   1.00 12.23  ? 24  LYS A N   1 
ATOM   140  C  CA  . LYS A 1 38  ? -7.592  3.595   0.939   1.00 12.04  ? 24  LYS A CA  1 
ATOM   141  C  C   . LYS A 1 38  ? -7.065  4.066   2.285   1.00 10.79  ? 24  LYS A C   1 
ATOM   142  O  O   . LYS A 1 38  ? -7.766  4.729   3.055   1.00 13.88  ? 24  LYS A O   1 
ATOM   143  C  CB  . LYS A 1 38  ? -9.108  3.704   0.884   1.00 21.39  ? 24  LYS A CB  1 
ATOM   144  C  CG  . LYS A 1 38  ? -9.666  5.082   0.988   1.00 19.08  ? 24  LYS A CG  1 
ATOM   145  C  CD  . LYS A 1 38  ? -11.050 5.146   0.241   1.00 21.07  ? 24  LYS A CD  1 
ATOM   146  C  CE  . LYS A 1 38  ? -12.203 4.251   0.690   1.00 17.72  ? 24  LYS A CE  1 
ATOM   147  N  NZ  . LYS A 1 38  ? -12.731 4.558   2.072   1.00 17.55  ? 24  LYS A NZ  1 
ATOM   148  N  N   . ASN A 1 39  ? -5.821  3.775   2.591   1.00 10.97  ? 25  ASN A N   1 
ATOM   149  C  CA  . ASN A 1 39  ? -5.266  4.231   3.859   1.00 9.55   ? 25  ASN A CA  1 
ATOM   150  C  C   . ASN A 1 39  ? -5.172  5.758   3.866   1.00 9.31   ? 25  ASN A C   1 
ATOM   151  O  O   . ASN A 1 39  ? -4.604  6.350   2.956   1.00 9.29   ? 25  ASN A O   1 
ATOM   152  C  CB  . ASN A 1 39  ? -3.838  3.700   4.082   1.00 11.35  ? 25  ASN A CB  1 
ATOM   153  C  CG  . ASN A 1 39  ? -3.743  2.233   4.421   1.00 13.60  ? 25  ASN A CG  1 
ATOM   154  O  OD1 . ASN A 1 39  ? -4.336  1.729   5.382   1.00 16.91  ? 25  ASN A OD1 1 
ATOM   155  N  ND2 . ASN A 1 39  ? -3.064  1.530   3.538   1.00 18.17  ? 25  ASN A ND2 1 
ATOM   156  N  N   . MET A 1 40  ? -5.604  6.346   4.958   1.00 7.76   ? 26  MET A N   1 
ATOM   157  C  CA  . MET A 1 40  ? -5.387  7.774   5.146   1.00 7.89   ? 26  MET A CA  1 
ATOM   158  C  C   . MET A 1 40  ? -5.642  8.047   6.626   1.00 9.06   ? 26  MET A C   1 
ATOM   159  O  O   . MET A 1 40  ? -6.797  7.950   7.088   1.00 9.27   ? 26  MET A O   1 
ATOM   160  C  CB  . MET A 1 40  ? -6.330  8.660   4.341   1.00 8.20   ? 26  MET A CB  1 
ATOM   161  C  CG  . MET A 1 40  ? -6.014  10.123  4.488   1.00 8.99   ? 26  MET A CG  1 
ATOM   162  S  SD  . MET A 1 40  ? -7.153  11.229  3.634   1.00 10.91  ? 26  MET A SD  1 
ATOM   163  C  CE  . MET A 1 40  ? -6.509  11.038  1.970   1.00 12.31  ? 26  MET A CE  1 
ATOM   164  N  N   . TYR A 1 41  ? -4.600  8.435   7.370   1.00 8.44   ? 27  TYR A N   1 
ATOM   165  C  CA  . TYR A 1 41  ? -4.693  8.635   8.795   1.00 8.74   ? 27  TYR A CA  1 
ATOM   166  C  C   . TYR A 1 41  ? -4.209  10.038  9.107   1.00 9.58   ? 27  TYR A C   1 
ATOM   167  O  O   . TYR A 1 41  ? -3.082  10.415  8.789   1.00 10.89  ? 27  TYR A O   1 
ATOM   168  C  CB  . TYR A 1 41  ? -3.890  7.573   9.570   1.00 9.56   ? 27  TYR A CB  1 
ATOM   169  C  CG  . TYR A 1 41  ? -4.259  6.176   9.130   1.00 9.63   ? 27  TYR A CG  1 
ATOM   170  C  CD1 . TYR A 1 41  ? -5.482  5.633   9.459   1.00 9.37   ? 27  TYR A CD1 1 
ATOM   171  C  CD2 . TYR A 1 41  ? -3.480  5.472   8.233   1.00 10.23  ? 27  TYR A CD2 1 
ATOM   172  C  CE1 . TYR A 1 41  ? -5.891  4.408   9.003   1.00 10.10  ? 27  TYR A CE1 1 
ATOM   173  C  CE2 . TYR A 1 41  ? -3.880  4.244   7.745   1.00 10.30  ? 27  TYR A CE2 1 
ATOM   174  C  CZ  . TYR A 1 41  ? -5.103  3.737   8.098   1.00 9.76   ? 27  TYR A CZ  1 
ATOM   175  O  OH  . TYR A 1 41  ? -5.532  2.526   7.598   1.00 10.79  ? 27  TYR A OH  1 
ATOM   176  N  N   . ILE A 1 42  ? -5.021  10.815  9.804   1.00 9.51   ? 28  ILE A N   1 
ATOM   177  C  CA  . ILE A 1 42  ? -4.667  12.169  10.148  1.00 9.39   ? 28  ILE A CA  1 
ATOM   178  C  C   . ILE A 1 42  ? -4.162  12.144  11.571  1.00 9.78   ? 28  ILE A C   1 
ATOM   179  O  O   . ILE A 1 42  ? -4.819  11.631  12.471  1.00 10.79  ? 28  ILE A O   1 
ATOM   180  C  CB  . ILE A 1 42  ? -5.867  13.121  9.993   1.00 10.23  ? 28  ILE A CB  1 
ATOM   181  C  CG1 . ILE A 1 42  ? -6.466  13.068  8.599   1.00 11.68  ? 28  ILE A CG1 1 
ATOM   182  C  CG2 . ILE A 1 42  ? -5.486  14.544  10.350  1.00 12.14  ? 28  ILE A CG2 1 
ATOM   183  C  CD1 . ILE A 1 42  ? -5.517  13.302  7.459   1.00 13.83  ? 28  ILE A CD1 1 
ATOM   184  N  N   . VAL A 1 43  ? -2.994  12.745  11.789  1.00 9.57   ? 29  VAL A N   1 
ATOM   185  C  CA  . VAL A 1 43  ? -2.474  12.914  13.142  1.00 9.99   ? 29  VAL A CA  1 
ATOM   186  C  C   . VAL A 1 43  ? -2.301  14.399  13.385  1.00 11.06  ? 29  VAL A C   1 
ATOM   187  O  O   . VAL A 1 43  ? -1.687  15.089  12.570  1.00 12.62  ? 29  VAL A O   1 
ATOM   188  C  CB  . VAL A 1 43  ? -1.157  12.152  13.359  1.00 11.93  ? 29  VAL A CB  1 
ATOM   189  C  CG1 . VAL A 1 43  ? -0.606  12.454  14.744  1.00 13.91  ? 29  VAL A CG1 1 
ATOM   190  C  CG2 . VAL A 1 43  ? -1.339  10.664  13.126  1.00 12.24  ? 29  VAL A CG2 1 
ATOM   191  N  N   . GLU A 1 44  ? -2.800  14.876  14.532  1.00 11.50  ? 30  GLU A N   1 
ATOM   192  C  CA  . GLU A 1 44  ? -2.589  16.267  14.887  1.00 11.76  ? 30  GLU A CA  1 
ATOM   193  C  C   . GLU A 1 44  ? -1.867  16.267  16.238  1.00 12.22  ? 30  GLU A C   1 
ATOM   194  O  O   . GLU A 1 44  ? -2.204  15.546  17.171  1.00 12.36  ? 30  GLU A O   1 
ATOM   195  C  CB  . GLU A 1 44  ? -3.909  17.031  15.036  1.00 13.06  ? 30  GLU A CB  1 
ATOM   196  C  CG  . GLU A 1 44  ? -4.790  17.043  13.805  1.00 13.93  ? 30  GLU A CG  1 
ATOM   197  C  CD  . GLU A 1 44  ? -6.109  17.772  14.018  1.00 15.44  ? 30  GLU A CD  1 
ATOM   198  O  OE1 . GLU A 1 44  ? -6.061  19.010  14.290  1.00 17.58  ? 30  GLU A OE1 1 
ATOM   199  O  OE2 . GLU A 1 44  ? -7.148  17.145  13.848  1.00 15.10  ? 30  GLU A OE2 1 
ATOM   200  N  N   . VAL A 1 45  ? -0.877  17.149  16.307  1.00 12.29  ? 31  VAL A N   1 
ATOM   201  C  CA  . VAL A 1 45  ? -0.150  17.407  17.541  1.00 12.61  ? 31  VAL A CA  1 
ATOM   202  C  C   . VAL A 1 45  ? -0.203  18.930  17.753  1.00 14.75  ? 31  VAL A C   1 
ATOM   203  O  O   . VAL A 1 45  ? 0.362   19.678  16.954  1.00 14.30  ? 31  VAL A O   1 
ATOM   204  C  CB  . VAL A 1 45  ? 1.292   16.894  17.480  1.00 14.35  ? 31  VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 45  ? 1.973   17.172  18.824  1.00 15.80  ? 31  VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 45  ? 1.390   15.413  17.141  1.00 13.68  ? 31  VAL A CG2 1 
ATOM   207  N  N   . ASP A 1 46  ? -1.006  19.348  18.726  1.00 15.91  ? 32  ASP A N   1 
ATOM   208  C  CA  . ASP A 1 46  ? -1.417  20.750  18.884  1.00 15.23  ? 32  ASP A CA  1 
ATOM   209  C  C   . ASP A 1 46  ? -1.848  21.299  17.524  1.00 16.31  ? 32  ASP A C   1 
ATOM   210  O  O   . ASP A 1 46  ? -2.703  20.717  16.873  1.00 16.86  ? 32  ASP A O   1 
ATOM   211  C  CB  . ASP A 1 46  ? -0.335  21.504  19.652  1.00 20.81  ? 32  ASP A CB  1 
ATOM   212  C  CG  . ASP A 1 46  ? -0.197  20.871  21.025  1.00 24.77  ? 32  ASP A CG  1 
ATOM   213  O  OD1 . ASP A 1 46  ? -1.250  20.684  21.692  1.00 26.25  ? 32  ASP A OD1 1 
ATOM   214  O  OD2 . ASP A 1 46  ? 0.911   20.552  21.387  1.00 29.71  ? 32  ASP A OD2 1 
ATOM   215  N  N   . ASP A 1 47  ? -1.242  22.399  17.073  1.00 16.07  ? 33  ASP A N   1 
ATOM   216  C  CA  . ASP A 1 47  ? -1.739  23.107  15.909  1.00 16.31  ? 33  ASP A CA  1 
ATOM   217  C  C   . ASP A 1 47  ? -1.040  22.662  14.623  1.00 15.94  ? 33  ASP A C   1 
ATOM   218  O  O   . ASP A 1 47  ? -1.168  23.343  13.601  1.00 17.90  ? 33  ASP A O   1 
ATOM   219  C  CB  . ASP A 1 47  ? -1.597  24.625  16.027  1.00 18.40  ? 33  ASP A CB  1 
ATOM   220  C  CG  . ASP A 1 47  ? -0.195  25.156  16.264  1.00 24.95  ? 33  ASP A CG  1 
ATOM   221  O  OD1 . ASP A 1 47  ? 0.726   24.356  16.579  1.00 29.44  ? 33  ASP A OD1 1 
ATOM   222  O  OD2 . ASP A 1 47  ? -0.031  26.381  16.164  1.00 31.55  ? 33  ASP A OD2 1 
ATOM   223  N  N   . GLU A 1 48  ? -0.416  21.460  14.634  1.00 15.00  ? 34  GLU A N   1 
ATOM   224  C  CA  . GLU A 1 48  ? 0.107   20.874  13.416  1.00 14.24  ? 34  GLU A CA  1 
ATOM   225  C  C   . GLU A 1 48  ? -0.614  19.579  13.060  1.00 13.07  ? 34  GLU A C   1 
ATOM   226  O  O   . GLU A 1 48  ? -0.819  18.701  13.904  1.00 15.27  ? 34  GLU A O   1 
ATOM   227  C  CB  . GLU A 1 48  ? 1.609   20.622  13.552  1.00 15.76  ? 34  GLU A CB  1 
ATOM   228  C  CG  . GLU A 1 48  ? 2.404   21.925  13.580  1.00 19.14  ? 34  GLU A CG  1 
ATOM   229  C  CD  . GLU A 1 48  ? 3.920   21.775  13.607  1.00 23.82  ? 34  GLU A CD  1 
ATOM   230  O  OE1 . GLU A 1 48  ? 4.622   22.466  12.830  1.00 25.87  ? 34  GLU A OE1 1 
ATOM   231  O  OE2 . GLU A 1 48  ? 4.388   20.961  14.377  1.00 22.97  ? 34  GLU A OE2 1 
ATOM   232  N  N   . MET A 1 49  ? -0.926  19.448  11.767  1.00 12.97  ? 35  MET A N   1 
ATOM   233  C  CA  . MET A 1 49  ? -1.649  18.306  11.248  1.00 12.82  ? 35  MET A CA  1 
ATOM   234  C  C   . MET A 1 49  ? -0.777  17.616  10.195  1.00 11.38  ? 35  MET A C   1 
ATOM   235  O  O   . MET A 1 49  ? -0.158  18.284  9.350   1.00 13.28  ? 35  MET A O   1 
ATOM   236  C  CB  . MET A 1 49  ? -2.973  18.811  10.647  1.00 14.45  ? 35  MET A CB  1 
ATOM   237  C  CG  . MET A 1 49  ? -3.821  17.715  10.024  1.00 12.54  ? 35  MET A CG  1 
ATOM   238  S  SD  . MET A 1 49  ? -5.348  18.238  9.248   1.00 17.36  ? 35  MET A SD  1 
ATOM   239  C  CE  . MET A 1 49  ? -6.294  18.824  10.624  1.00 21.39  ? 35  MET A CE  1 
ATOM   240  N  N   . PHE A 1 50  ? -0.810  16.267  10.211  1.00 10.86  ? 36  PHE A N   1 
ATOM   241  C  CA  . PHE A 1 50  ? -0.028  15.434  9.284   1.00 11.68  ? 36  PHE A CA  1 
ATOM   242  C  C   . PHE A 1 50  ? -0.991  14.427  8.637   1.00 10.37  ? 36  PHE A C   1 
ATOM   243  O  O   . PHE A 1 50  ? -1.798  13.825  9.355   1.00 12.76  ? 36  PHE A O   1 
ATOM   244  C  CB  . PHE A 1 50  ? 1.067   14.707  10.086  1.00 12.18  ? 36  PHE A CB  1 
ATOM   245  C  CG  . PHE A 1 50  ? 1.955   15.665  10.835  1.00 14.08  ? 36  PHE A CG  1 
ATOM   246  C  CD1 . PHE A 1 50  ? 3.009   16.329  10.197  1.00 17.76  ? 36  PHE A CD1 1 
ATOM   247  C  CD2 . PHE A 1 50  ? 1.629   16.030  12.132  1.00 15.74  ? 36  PHE A CD2 1 
ATOM   248  C  CE1 . PHE A 1 50  ? 3.782   17.272  10.877  1.00 17.52  ? 36  PHE A CE1 1 
ATOM   249  C  CE2 . PHE A 1 50  ? 2.387   16.983  12.817  1.00 17.20  ? 36  PHE A CE2 1 
ATOM   250  C  CZ  . PHE A 1 50  ? 3.456   17.594  12.172  1.00 18.06  ? 36  PHE A CZ  1 
ATOM   251  N  N   . MET A 1 51  ? -0.860  14.194  7.361   1.00 8.81   ? 37  MET A N   1 
ATOM   252  C  CA  . MET A 1 51  ? -1.617  13.173  6.676   1.00 9.69   ? 37  MET A CA  1 
ATOM   253  C  C   . MET A 1 51  ? -0.706  11.988  6.392   1.00 9.45   ? 37  MET A C   1 
ATOM   254  O  O   . MET A 1 51  ? 0.305   12.153  5.705   1.00 10.44  ? 37  MET A O   1 
ATOM   255  C  CB  . MET A 1 51  ? -2.191  13.709  5.351   1.00 10.22  ? 37  MET A CB  1 
ATOM   256  C  CG  . MET A 1 51  ? -2.990  12.674  4.583   1.00 9.70   ? 37  MET A CG  1 
ATOM   257  S  SD  . MET A 1 51  ? -3.577  13.356  2.982   1.00 11.52  ? 37  MET A SD  1 
ATOM   258  C  CE  . MET A 1 51  ? -4.916  14.435  3.515   1.00 11.94  ? 37  MET A CE  1 
ATOM   259  N  N   . LEU A 1 52  ? -1.075  10.810  6.912   1.00 8.37   ? 38  LEU A N   1 
ATOM   260  C  CA  . LEU A 1 52  ? -0.271  9.617   6.779   1.00 8.94   ? 38  LEU A CA  1 
ATOM   261  C  C   . LEU A 1 52  ? -0.960  8.700   5.791   1.00 9.34   ? 38  LEU A C   1 
ATOM   262  O  O   . LEU A 1 52  ? -2.044  8.128   6.067   1.00 9.70   ? 38  LEU A O   1 
ATOM   263  C  CB  . LEU A 1 52  ? -0.073  8.901   8.101   1.00 9.91   ? 38  LEU A CB  1 
ATOM   264  C  CG  . LEU A 1 52  ? 0.475   9.743   9.230   1.00 11.05  ? 38  LEU A CG  1 
ATOM   265  C  CD1 . LEU A 1 52  ? 0.690   8.924   10.482  1.00 12.87  ? 38  LEU A CD1 1 
ATOM   266  C  CD2 . LEU A 1 52  ? 1.741   10.501  8.876   1.00 14.01  ? 38  LEU A CD2 1 
ATOM   267  N  N   . ASP A 1 53  ? -0.350  8.618   4.598   1.00 9.65   ? 39  ASP A N   1 
ATOM   268  C  CA  . ASP A 1 53  ? -0.900  7.952   3.430   1.00 8.87   ? 39  ASP A CA  1 
ATOM   269  C  C   . ASP A 1 53  ? -2.136  8.648   2.853   1.00 8.70   ? 39  ASP A C   1 
ATOM   270  O  O   . ASP A 1 53  ? -2.795  9.450   3.509   1.00 9.74   ? 39  ASP A O   1 
ATOM   271  C  CB  . ASP A 1 53  ? -1.101  6.429   3.655   1.00 9.55   ? 39  ASP A CB  1 
ATOM   272  C  CG  . ASP A 1 53  ? 0.237   5.682   3.558   1.00 9.94   ? 39  ASP A CG  1 
ATOM   273  O  OD1 . ASP A 1 53  ? 0.300   4.541   4.042   1.00 12.84  ? 39  ASP A OD1 1 
ATOM   274  O  OD2 . ASP A 1 53  ? 1.226   6.222   2.998   1.00 12.01  ? 39  ASP A OD2 1 
ATOM   275  N  N   . ALA A 1 54  ? -2.401  8.295   1.591   1.00 8.95   ? 40  ALA A N   1 
ATOM   276  C  CA  . ALA A 1 54  ? -3.519  8.835   0.849   1.00 9.58   ? 40  ALA A CA  1 
ATOM   277  C  C   . ALA A 1 54  ? -3.850  7.906   -0.286  1.00 8.60   ? 40  ALA A C   1 
ATOM   278  O  O   . ALA A 1 54  ? -3.631  8.167   -1.437  1.00 10.18  ? 40  ALA A O   1 
ATOM   279  C  CB  . ALA A 1 54  ? -3.209  10.249  0.346   1.00 11.40  ? 40  ALA A CB  1 
ATOM   280  N  N   . GLY A 1 55  ? -4.419  6.737   0.110   1.00 9.34   ? 41  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 55  ? -4.703  5.664   -0.811  1.00 10.27  ? 41  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 55  ? -6.052  5.734   -1.509  1.00 11.01  ? 41  GLY A C   1 
ATOM   283  O  O   . GLY A 1 55  ? -6.924  6.528   -1.153  1.00 11.35  ? 41  GLY A O   1 
ATOM   284  N  N   . LEU A 1 56  ? -6.194  4.846   -2.504  1.00 10.98  ? 42  LEU A N   1 
ATOM   285  C  CA  . LEU A 1 56  ? -7.495  4.620   -3.126  1.00 11.47  ? 42  LEU A CA  1 
ATOM   286  C  C   . LEU A 1 56  ? -7.926  3.188   -2.800  1.00 12.11  ? 42  LEU A C   1 
ATOM   287  O  O   . LEU A 1 56  ? -7.178  2.387   -2.241  1.00 12.87  ? 42  LEU A O   1 
ATOM   288  C  CB  . LEU A 1 56  ? -7.471  4.838   -4.657  1.00 14.01  ? 42  LEU A CB  1 
ATOM   289  C  CG  . LEU A 1 56  ? -6.543  3.908   -5.463  1.00 14.20  ? 42  LEU A CG  1 
ATOM   290  C  CD1 . LEU A 1 56  ? -7.085  2.494   -5.601  1.00 16.75  ? 42  LEU A CD1 1 
ATOM   291  C  CD2 . LEU A 1 56  ? -6.323  4.458   -6.867  1.00 19.34  ? 42  LEU A CD2 1 
ATOM   292  N  N   . MET A 1 57  ? -9.198  2.936   -3.139  1.00 13.48  ? 43  MET A N   1 
ATOM   293  C  CA  . MET A 1 57  ? -9.738  1.596   -3.071  1.00 13.38  ? 43  MET A CA  1 
ATOM   294  C  C   . MET A 1 57  ? -10.465 1.362   -4.396  1.00 16.93  ? 43  MET A C   1 
ATOM   295  O  O   . MET A 1 57  ? -11.056 2.261   -4.972  1.00 17.25  ? 43  MET A O   1 
ATOM   296  C  CB  . MET A 1 57  ? -10.723 1.515   -1.909  1.00 16.72  ? 43  MET A CB  1 
ATOM   297  C  CG  . MET A 1 57  ? -11.454 0.196   -1.747  1.00 17.31  ? 43  MET A CG  1 
ATOM   298  S  SD  . MET A 1 57  ? -12.632 0.341   -0.345  1.00 20.89  ? 43  MET A SD  1 
ATOM   299  C  CE  . MET A 1 57  ? -14.021 1.096   -1.162  1.00 23.24  ? 43  MET A CE  1 
ATOM   300  N  N   . PHE A 1 58  ? -10.407 0.123   -4.884  1.00 17.95  ? 44  PHE A N   1 
ATOM   301  C  CA  . PHE A 1 58  ? -11.155 -0.210  -6.079  1.00 22.38  ? 44  PHE A CA  1 
ATOM   302  C  C   . PHE A 1 58  ? -12.602 -0.487  -5.691  1.00 20.77  ? 44  PHE A C   1 
ATOM   303  O  O   . PHE A 1 58  ? -12.920 -0.881  -4.564  1.00 25.19  ? 44  PHE A O   1 
ATOM   304  C  CB  . PHE A 1 58  ? -10.458 -1.329  -6.864  1.00 22.24  ? 44  PHE A CB  1 
ATOM   305  C  CG  . PHE A 1 58  ? -9.125  -0.880  -7.420  1.00 24.97  ? 44  PHE A CG  1 
ATOM   306  C  CD1 . PHE A 1 58  ? -9.072  0.110   -8.395  1.00 23.69  ? 44  PHE A CD1 1 
ATOM   307  C  CD2 . PHE A 1 58  ? -7.927  -1.379  -6.918  1.00 25.14  ? 44  PHE A CD2 1 
ATOM   308  C  CE1 . PHE A 1 58  ? -7.857  0.557   -8.895  1.00 28.88  ? 44  PHE A CE1 1 
ATOM   309  C  CE2 . PHE A 1 58  ? -6.713  -0.928  -7.419  1.00 24.87  ? 44  PHE A CE2 1 
ATOM   310  C  CZ  . PHE A 1 58  ? -6.692  0.013   -8.424  1.00 21.61  ? 44  PHE A CZ  1 
ATOM   311  N  N   . PRO A 1 59  ? -13.554 -0.185  -6.592  1.00 27.20  ? 45  PRO A N   1 
ATOM   312  C  CA  . PRO A 1 59  ? -14.974 -0.249  -6.260  1.00 29.72  ? 45  PRO A CA  1 
ATOM   313  C  C   . PRO A 1 59  ? -15.499 -1.615  -5.820  1.00 35.86  ? 45  PRO A C   1 
ATOM   314  O  O   . PRO A 1 59  ? -15.023 -2.644  -6.287  1.00 38.49  ? 45  PRO A O   1 
ATOM   315  C  CB  . PRO A 1 59  ? -15.625 0.101   -7.605  1.00 40.41  ? 45  PRO A CB  1 
ATOM   316  C  CG  . PRO A 1 59  ? -14.612 0.939   -8.325  1.00 39.19  ? 45  PRO A CG  1 
ATOM   317  C  CD  . PRO A 1 59  ? -13.309 0.265   -7.971  1.00 37.13  ? 45  PRO A CD  1 
ATOM   318  N  N   . GLU A 1 60  ? -16.479 -1.610  -4.906  1.00 33.18  ? 46  GLU A N   1 
ATOM   319  C  CA  . GLU A 1 60  ? -17.163 -2.829  -4.508  1.00 41.53  ? 46  GLU A CA  1 
ATOM   320  C  C   . GLU A 1 60  ? -18.248 -3.113  -5.544  1.00 49.40  ? 46  GLU A C   1 
ATOM   321  O  O   . GLU A 1 60  ? -18.633 -2.205  -6.271  1.00 43.34  ? 46  GLU A O   1 
ATOM   322  N  N   . ASP A 1 61  ? -18.740 -4.360  -5.600  1.00 48.08  ? 47  ASP A N   1 
ATOM   323  C  CA  . ASP A 1 61  ? -19.693 -4.767  -6.626  1.00 41.02  ? 47  ASP A CA  1 
ATOM   324  C  C   . ASP A 1 61  ? -21.006 -3.986  -6.483  1.00 37.24  ? 47  ASP A C   1 
ATOM   325  O  O   . ASP A 1 61  ? -21.494 -3.884  -5.331  1.00 50.85  ? 47  ASP A O   1 
ATOM   326  N  N   . MET A 1 63  ? -21.055 -1.317  -6.480  1.00 66.84  ? 49  MET A N   1 
ATOM   327  C  CA  . MET A 1 63  ? -20.990 0.026   -7.121  1.00 64.25  ? 49  MET A CA  1 
ATOM   328  C  C   . MET A 1 63  ? -21.170 -0.122  -8.633  1.00 60.31  ? 49  MET A C   1 
ATOM   329  O  O   . MET A 1 63  ? -20.814 -1.162  -9.196  1.00 68.65  ? 49  MET A O   1 
ATOM   330  C  CB  . MET A 1 63  ? -19.640 0.703   -6.845  1.00 47.92  ? 49  MET A CB  1 
ATOM   331  C  CG  . MET A 1 63  ? -19.572 1.505   -5.542  1.00 53.06  ? 49  MET A CG  1 
ATOM   332  S  SD  . MET A 1 63  ? -17.862 1.638   -4.900  1.00 59.90  ? 49  MET A SD  1 
ATOM   333  C  CE  . MET A 1 63  ? -18.137 2.274   -3.244  1.00 39.81  ? 49  MET A CE  1 
ATOM   334  N  N   . LEU A 1 64  ? -21.696 0.937   -9.268  1.00 75.66  ? 50  LEU A N   1 
ATOM   335  C  CA  . LEU A 1 64  ? -21.928 0.970   -10.709 1.00 78.89  ? 50  LEU A CA  1 
ATOM   336  C  C   . LEU A 1 64  ? -21.371 2.257   -11.328 1.00 64.13  ? 50  LEU A C   1 
ATOM   337  O  O   . LEU A 1 64  ? -21.536 3.334   -10.770 1.00 84.74  ? 50  LEU A O   1 
ATOM   338  C  CB  . LEU A 1 64  ? -23.428 0.855   -10.981 1.00 75.32  ? 50  LEU A CB  1 
ATOM   339  N  N   . GLY A 1 65  ? -20.754 2.089   -12.522 1.00 91.72  ? 51  GLY A N   1 
ATOM   340  C  CA  . GLY A 1 65  ? -19.914 3.102   -13.172 1.00 80.11  ? 51  GLY A CA  1 
ATOM   341  C  C   . GLY A 1 65  ? -18.889 3.854   -12.289 1.00 77.13  ? 51  GLY A C   1 
ATOM   342  O  O   . GLY A 1 65  ? -18.688 5.057   -12.485 1.00 79.84  ? 51  GLY A O   1 
ATOM   343  N  N   . VAL A 1 66  ? -18.149 3.151   -11.409 1.00 49.94  ? 52  VAL A N   1 
ATOM   344  C  CA  . VAL A 1 66  ? -17.104 3.742   -10.581 1.00 37.09  ? 52  VAL A CA  1 
ATOM   345  C  C   . VAL A 1 66  ? -15.773 3.105   -10.977 1.00 29.39  ? 52  VAL A C   1 
ATOM   346  O  O   . VAL A 1 66  ? -15.696 1.890   -11.151 1.00 32.07  ? 52  VAL A O   1 
ATOM   347  C  CB  . VAL A 1 66  ? -17.432 3.531   -9.089  1.00 34.66  ? 52  VAL A CB  1 
ATOM   348  C  CG1 . VAL A 1 66  ? -16.360 4.099   -8.164  1.00 32.21  ? 52  VAL A CG1 1 
ATOM   349  C  CG2 . VAL A 1 66  ? -18.796 4.116   -8.713  1.00 35.77  ? 52  VAL A CG2 1 
ATOM   350  N  N   . ASP A 1 67  ? -14.726 3.927   -11.125 1.00 28.41  ? 53  ASP A N   1 
ATOM   351  C  CA  . ASP A 1 67  ? -13.386 3.420   -11.394 1.00 29.48  ? 53  ASP A CA  1 
ATOM   352  C  C   . ASP A 1 67  ? -12.615 3.228   -10.084 1.00 23.41  ? 53  ASP A C   1 
ATOM   353  O  O   . ASP A 1 67  ? -12.012 2.178   -9.888  1.00 27.19  ? 53  ASP A O   1 
ATOM   354  C  CB  . ASP A 1 67  ? -12.640 4.336   -12.367 1.00 33.45  ? 53  ASP A CB  1 
ATOM   355  C  CG  . ASP A 1 67  ? -13.176 4.256   -13.785 1.00 40.16  ? 53  ASP A CG  1 
ATOM   356  O  OD1 . ASP A 1 67  ? -13.048 5.258   -14.511 1.00 52.78  ? 53  ASP A OD1 1 
ATOM   357  O  OD2 . ASP A 1 67  ? -13.699 3.184   -14.142 1.00 59.15  ? 53  ASP A OD2 1 
ATOM   358  N  N   . ILE A 1 68  ? -12.571 4.275   -9.239  1.00 23.51  ? 54  ILE A N   1 
ATOM   359  C  CA  . ILE A 1 68  ? -11.855 4.244   -7.964  1.00 18.44  ? 54  ILE A CA  1 
ATOM   360  C  C   . ILE A 1 68  ? -12.667 5.014   -6.924  1.00 17.93  ? 54  ILE A C   1 
ATOM   361  O  O   . ILE A 1 68  ? -13.574 5.792   -7.232  1.00 19.35  ? 54  ILE A O   1 
ATOM   362  C  CB  . ILE A 1 68  ? -10.409 4.802   -8.074  1.00 19.26  ? 54  ILE A CB  1 
ATOM   363  C  CG1 . ILE A 1 68  ? -10.367 6.322   -8.269  1.00 19.67  ? 54  ILE A CG1 1 
ATOM   364  C  CG2 . ILE A 1 68  ? -9.577  4.089   -9.139  1.00 20.62  ? 54  ILE A CG2 1 
ATOM   365  C  CD1 . ILE A 1 68  ? -8.997  6.935   -8.054  1.00 19.56  ? 54  ILE A CD1 1 
ATOM   366  N  N   . VAL A 1 69  ? -12.325 4.743   -5.662  1.00 16.70  ? 55  VAL A N   1 
ATOM   367  C  CA  . VAL A 1 69  ? -12.907 5.388   -4.512  1.00 15.94  ? 55  VAL A CA  1 
ATOM   368  C  C   . VAL A 1 69  ? -11.765 6.011   -3.712  1.00 13.73  ? 55  VAL A C   1 
ATOM   369  O  O   . VAL A 1 69  ? -10.737 5.361   -3.502  1.00 14.67  ? 55  VAL A O   1 
ATOM   370  C  CB  . VAL A 1 69  ? -13.643 4.348   -3.643  1.00 16.96  ? 55  VAL A CB  1 
ATOM   371  C  CG1 . VAL A 1 69  ? -14.279 5.021   -2.449  1.00 15.76  ? 55  VAL A CG1 1 
ATOM   372  C  CG2 . VAL A 1 69  ? -14.637 3.504   -4.434  1.00 21.35  ? 55  VAL A CG2 1 
ATOM   373  N  N   . ILE A 1 70  ? -11.954 7.261   -3.290  1.00 12.88  ? 56  ILE A N   1 
ATOM   374  C  CA  . ILE A 1 70  ? -10.952 7.937   -2.482  1.00 12.20  ? 56  ILE A CA  1 
ATOM   375  C  C   . ILE A 1 70  ? -11.583 8.480   -1.217  1.00 11.25  ? 56  ILE A C   1 
ATOM   376  O  O   . ILE A 1 70  ? -12.813 8.616   -1.135  1.00 12.81  ? 56  ILE A O   1 
ATOM   377  C  CB  . ILE A 1 70  ? -10.230 9.044   -3.264  1.00 13.94  ? 56  ILE A CB  1 
ATOM   378  C  CG1 . ILE A 1 70  ? -11.161 10.208  -3.613  1.00 16.30  ? 56  ILE A CG1 1 
ATOM   379  C  CG2 . ILE A 1 70  ? -9.530  8.450   -4.473  1.00 15.02  ? 56  ILE A CG2 1 
ATOM   380  C  CD1 . ILE A 1 70  ? -10.455 11.335  -4.356  1.00 18.93  ? 56  ILE A CD1 1 
ATOM   381  N  N   . PRO A 1 71  ? -10.774 8.847   -0.211  1.00 10.42  ? 57  PRO A N   1 
ATOM   382  C  CA  . PRO A 1 71  ? -11.365 9.400   0.992   1.00 10.97  ? 57  PRO A CA  1 
ATOM   383  C  C   . PRO A 1 71  ? -11.965 10.784  0.821   1.00 11.29  ? 57  PRO A C   1 
ATOM   384  O  O   . PRO A 1 71  ? -11.448 11.577  0.052   1.00 13.29  ? 57  PRO A O   1 
ATOM   385  C  CB  . PRO A 1 71  ? -10.173 9.495   1.978   1.00 11.87  ? 57  PRO A CB  1 
ATOM   386  C  CG  . PRO A 1 71  ? -9.231  8.419   1.468   1.00 12.17  ? 57  PRO A CG  1 
ATOM   387  C  CD  . PRO A 1 71  ? -9.336  8.565   -0.043  1.00 11.47  ? 57  PRO A CD  1 
ATOM   388  N  N   . ASP A 1 72  ? -13.049 11.063  1.552   1.00 10.58  ? 58  ASP A N   1 
ATOM   389  C  CA  . ASP A 1 72  ? -13.519 12.425  1.745   1.00 11.30  ? 58  ASP A CA  1 
ATOM   390  C  C   . ASP A 1 72  ? -12.543 13.116  2.682   1.00 10.72  ? 58  ASP A C   1 
ATOM   391  O  O   . ASP A 1 72  ? -12.382 12.707  3.830   1.00 11.53  ? 58  ASP A O   1 
ATOM   392  C  CB  . ASP A 1 72  ? -14.921 12.330  2.320   1.00 12.60  ? 58  ASP A CB  1 
ATOM   393  C  CG  . ASP A 1 72  ? -15.601 13.646  2.529   1.00 13.30  ? 58  ASP A CG  1 
ATOM   394  O  OD1 . ASP A 1 72  ? -14.940 14.666  2.426   1.00 14.40  ? 58  ASP A OD1 1 
ATOM   395  O  OD2 . ASP A 1 72  ? -16.824 13.630  2.736   1.00 16.34  ? 58  ASP A OD2 1 
ATOM   396  N  N   . ILE A 1 73  ? -11.966 14.214  2.204   1.00 10.94  ? 59  ILE A N   1 
ATOM   397  C  CA  . ILE A 1 73  ? -11.030 14.995  2.975   1.00 11.17  ? 59  ILE A CA  1 
ATOM   398  C  C   . ILE A 1 73  ? -11.569 16.353  3.433   1.00 10.53  ? 59  ILE A C   1 
ATOM   399  O  O   . ILE A 1 73  ? -10.793 17.230  3.812   1.00 11.12  ? 59  ILE A O   1 
ATOM   400  C  CB  . ILE A 1 73  ? -9.705  15.163  2.225   1.00 11.33  ? 59  ILE A CB  1 
ATOM   401  C  CG1 . ILE A 1 73  ? -9.842  15.957  0.930   1.00 13.04  ? 59  ILE A CG1 1 
ATOM   402  C  CG2 . ILE A 1 73  ? -9.072  13.777  2.007   1.00 13.22  ? 59  ILE A CG2 1 
ATOM   403  C  CD1 . ILE A 1 73  ? -8.524  16.480  0.389   1.00 16.15  ? 59  ILE A CD1 1 
ATOM   404  N  N   . GLN A 1 74  ? -12.890 16.498  3.517   1.00 10.97  ? 60  GLN A N   1 
ATOM   405  C  CA  . GLN A 1 74  ? -13.476 17.754  3.949   1.00 11.18  ? 60  GLN A CA  1 
ATOM   406  C  C   . GLN A 1 74  ? -12.882 18.197  5.288   1.00 11.30  ? 60  GLN A C   1 
ATOM   407  O  O   . GLN A 1 74  ? -12.666 19.403  5.519   1.00 11.96  ? 60  GLN A O   1 
ATOM   408  C  CB  . GLN A 1 74  ? -15.001 17.588  4.029   1.00 12.00  ? 60  GLN A CB  1 
ATOM   409  C  CG  . GLN A 1 74  ? -15.719 18.804  4.606   1.00 11.83  ? 60  GLN A CG  1 
ATOM   410  C  CD  . GLN A 1 74  ? -15.582 20.085  3.785   1.00 10.95  ? 60  GLN A CD  1 
ATOM   411  O  OE1 . GLN A 1 74  ? -15.150 20.071  2.635   1.00 11.37  ? 60  GLN A OE1 1 
ATOM   412  N  NE2 . GLN A 1 74  ? -16.045 21.191  4.362   1.00 13.40  ? 60  GLN A NE2 1 
ATOM   413  N  N   . TYR A 1 75  ? -12.695 17.271  6.237   1.00 11.36  ? 61  TYR A N   1 
ATOM   414  C  CA  . TYR A 1 75  ? -12.139 17.702  7.510   1.00 11.83  ? 61  TYR A CA  1 
ATOM   415  C  C   . TYR A 1 75  ? -10.775 18.368  7.348   1.00 12.77  ? 61  TYR A C   1 
ATOM   416  O  O   . TYR A 1 75  ? -10.474 19.372  8.020   1.00 12.88  ? 61  TYR A O   1 
ATOM   417  C  CB  . TYR A 1 75  ? -12.047 16.527  8.498   1.00 12.59  ? 61  TYR A CB  1 
ATOM   418  C  CG  . TYR A 1 75  ? -11.353 16.907  9.773   1.00 11.86  ? 61  TYR A CG  1 
ATOM   419  C  CD1 . TYR A 1 75  ? -11.985 17.673  10.722  1.00 15.54  ? 61  TYR A CD1 1 
ATOM   420  C  CD2 . TYR A 1 75  ? -10.042 16.507  10.004  1.00 12.06  ? 61  TYR A CD2 1 
ATOM   421  C  CE1 . TYR A 1 75  ? -11.320 18.082  11.861  1.00 13.89  ? 61  TYR A CE1 1 
ATOM   422  C  CE2 . TYR A 1 75  ? -9.378  16.877  11.168  1.00 13.15  ? 61  TYR A CE2 1 
ATOM   423  C  CZ  . TYR A 1 75  ? -10.010 17.675  12.096  1.00 13.38  ? 61  TYR A CZ  1 
ATOM   424  O  OH  . TYR A 1 75  ? -9.427  18.093  13.267  1.00 15.42  ? 61  TYR A OH  1 
ATOM   425  N  N   . VAL A 1 76  ? -9.966  17.806  6.470   1.00 10.72  ? 62  VAL A N   1 
ATOM   426  C  CA  . VAL A 1 76  ? -8.644  18.376  6.250   1.00 11.49  ? 62  VAL A CA  1 
ATOM   427  C  C   . VAL A 1 76  ? -8.811  19.757  5.576   1.00 12.89  ? 62  VAL A C   1 
ATOM   428  O  O   . VAL A 1 76  ? -8.101  20.700  5.938   1.00 12.89  ? 62  VAL A O   1 
ATOM   429  C  CB  . VAL A 1 76  ? -7.774  17.435  5.410   1.00 11.73  ? 62  VAL A CB  1 
ATOM   430  C  CG1 . VAL A 1 76  ? -6.404  18.012  5.131   1.00 12.43  ? 62  VAL A CG1 1 
ATOM   431  C  CG2 . VAL A 1 76  ? -7.657  16.061  6.020   1.00 13.60  ? 62  VAL A CG2 1 
ATOM   432  N  N   . ILE A 1 77  ? -9.684  19.866  4.574   1.00 11.57  ? 63  ILE A N   1 
ATOM   433  C  CA  . ILE A 1 77  ? -9.901  21.136  3.899   1.00 12.22  ? 63  ILE A CA  1 
ATOM   434  C  C   . ILE A 1 77  ? -10.335 22.210  4.893   1.00 12.41  ? 63  ILE A C   1 
ATOM   435  O  O   . ILE A 1 77  ? -9.841  23.332  4.823   1.00 13.92  ? 63  ILE A O   1 
ATOM   436  C  CB  . ILE A 1 77  ? -10.923 20.942  2.784   1.00 12.60  ? 63  ILE A CB  1 
ATOM   437  C  CG1 . ILE A 1 77  ? -10.341 20.043  1.700   1.00 14.47  ? 63  ILE A CG1 1 
ATOM   438  C  CG2 . ILE A 1 77  ? -11.365 22.303  2.225   1.00 15.28  ? 63  ILE A CG2 1 
ATOM   439  C  CD1 . ILE A 1 77  ? -11.320 19.650  0.651   1.00 20.33  ? 63  ILE A CD1 1 
ATOM   440  N  N   . GLU A 1 78  ? -11.239 21.875  5.817   1.00 13.24  ? 64  GLU A N   1 
ATOM   441  C  CA  . GLU A 1 78  ? -11.709 22.828  6.815   1.00 13.60  ? 64  GLU A CA  1 
ATOM   442  C  C   . GLU A 1 78  ? -10.584 23.362  7.688   1.00 15.06  ? 64  GLU A C   1 
ATOM   443  O  O   . GLU A 1 78  ? -10.751 24.426  8.305   1.00 16.10  ? 64  GLU A O   1 
ATOM   444  C  CB  . GLU A 1 78  ? -12.773 22.192  7.707   1.00 14.98  ? 64  GLU A CB  1 
ATOM   445  C  CG  . GLU A 1 78  ? -14.091 21.986  6.998   1.00 16.08  ? 64  GLU A CG  1 
ATOM   446  C  CD  . GLU A 1 78  ? -15.153 21.239  7.768   1.00 21.11  ? 64  GLU A CD  1 
ATOM   447  O  OE1 . GLU A 1 78  ? -14.837 20.842  8.935   1.00 30.48  ? 64  GLU A OE1 1 
ATOM   448  O  OE2 . GLU A 1 78  ? -16.282 21.023  7.193   1.00 17.76  ? 64  GLU A OE2 1 
ATOM   449  N  N   . ASN A 1 79  ? -9.490  22.596  7.800   1.00 13.80  ? 65  ASN A N   1 
ATOM   450  C  CA  . ASN A 1 79  ? -8.398  22.883  8.715   1.00 14.13  ? 65  ASN A CA  1 
ATOM   451  C  C   . ASN A 1 79  ? -7.081  22.974  7.951   1.00 13.29  ? 65  ASN A C   1 
ATOM   452  O  O   . ASN A 1 79  ? -6.015  22.797  8.567   1.00 15.09  ? 65  ASN A O   1 
ATOM   453  C  CB  . ASN A 1 79  ? -8.341  21.785  9.784   1.00 14.60  ? 65  ASN A CB  1 
ATOM   454  C  CG  . ASN A 1 79  ? -9.592  21.827  10.623  1.00 16.13  ? 65  ASN A CG  1 
ATOM   455  O  OD1 . ASN A 1 79  ? -9.709  22.725  11.455  1.00 18.17  ? 65  ASN A OD1 1 
ATOM   456  N  ND2 . ASN A 1 79  ? -10.537 20.918  10.404  1.00 16.20  ? 65  ASN A ND2 1 
ATOM   457  N  N   . LYS A 1 80  ? -7.127  23.315  6.655   1.00 13.66  ? 66  LYS A N   1 
ATOM   458  C  CA  . LYS A 1 80  ? -6.009  23.080  5.759   1.00 15.04  ? 66  LYS A CA  1 
ATOM   459  C  C   . LYS A 1 80  ? -4.787  23.939  6.077   1.00 15.09  ? 66  LYS A C   1 
ATOM   460  O  O   . LYS A 1 80  ? -3.667  23.550  5.751   1.00 16.34  ? 66  LYS A O   1 
ATOM   461  C  CB  . LYS A 1 80  ? -6.378  23.231  4.288   1.00 16.72  ? 66  LYS A CB  1 
ATOM   462  C  CG  . LYS A 1 80  ? -6.763  24.642  3.866   1.00 17.54  ? 66  LYS A CG  1 
ATOM   463  C  CD  . LYS A 1 80  ? -7.266  24.700  2.448   1.00 22.78  ? 66  LYS A CD  1 
ATOM   464  C  CE  . LYS A 1 80  ? -7.371  26.101  1.910   1.00 28.13  ? 66  LYS A CE  1 
ATOM   465  N  NZ  . LYS A 1 80  ? -7.833  26.052  0.509   1.00 29.24  ? 66  LYS A NZ  1 
ATOM   466  N  N   . GLU A 1 81  ? -5.004  25.062  6.756   1.00 15.72  ? 67  GLU A N   1 
ATOM   467  C  CA  . GLU A 1 81  ? -3.884  25.919  7.106   1.00 17.57  ? 67  GLU A CA  1 
ATOM   468  C  C   . GLU A 1 81  ? -2.941  25.246  8.095   1.00 17.80  ? 67  GLU A C   1 
ATOM   469  O  O   . GLU A 1 81  ? -1.789  25.682  8.187   1.00 20.45  ? 67  GLU A O   1 
ATOM   470  C  CB  . GLU A 1 81  ? -4.383  27.257  7.658   1.00 22.55  ? 67  GLU A CB  1 
ATOM   471  C  CG  . GLU A 1 81  ? -5.254  27.151  8.911   1.00 26.29  ? 67  GLU A CG  1 
ATOM   472  C  CD  . GLU A 1 81  ? -6.748  26.760  8.881   1.00 33.67  ? 67  GLU A CD  1 
ATOM   473  O  OE1 . GLU A 1 81  ? -7.341  26.293  7.844   1.00 24.57  ? 67  GLU A OE1 1 
ATOM   474  O  OE2 . GLU A 1 81  ? -7.377  26.945  9.949   1.00 37.73  ? 67  GLU A OE2 1 
ATOM   475  N  N   . ARG A 1 82  ? -3.421  24.192  8.784   1.00 14.67  ? 68  ARG A N   1 
ATOM   476  C  CA  . ARG A 1 82  ? -2.592  23.479  9.748   1.00 15.40  ? 68  ARG A CA  1 
ATOM   477  C  C   . ARG A 1 82  ? -1.890  22.260  9.132   1.00 13.86  ? 68  ARG A C   1 
ATOM   478  O  O   . ARG A 1 82  ? -1.068  21.655  9.823   1.00 14.58  ? 68  ARG A O   1 
ATOM   479  C  CB  . ARG A 1 82  ? -3.424  23.059  10.969  1.00 15.78  ? 68  ARG A CB  1 
ATOM   480  C  CG  . ARG A 1 82  ? -4.047  24.258  11.670  1.00 17.43  ? 68  ARG A CG  1 
ATOM   481  C  CD  . ARG A 1 82  ? -4.399  23.966  13.109  1.00 18.57  ? 68  ARG A CD  1 
ATOM   482  N  NE  . ARG A 1 82  ? -5.243  22.781  13.295  1.00 18.24  ? 68  ARG A NE  1 
ATOM   483  C  CZ  . ARG A 1 82  ? -6.541  22.687  13.026  1.00 17.11  ? 68  ARG A CZ  1 
ATOM   484  N  NH1 . ARG A 1 82  ? -7.215  23.735  12.591  1.00 19.60  ? 68  ARG A NH1 1 
ATOM   485  N  NH2 . ARG A 1 82  ? -7.164  21.522  13.174  1.00 18.19  ? 68  ARG A NH2 1 
ATOM   486  N  N   . LEU A 1 83  ? -2.178  21.893  7.873   1.00 13.91  ? 69  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 83  ? -1.590  20.690  7.291   1.00 13.58  ? 69  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 83  ? -0.141  20.972  6.927   1.00 15.57  ? 69  LEU A C   1 
ATOM   489  O  O   . LEU A 1 83  ? 0.145   21.822  6.071   1.00 18.33  ? 69  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 83  ? -2.383  20.259  6.057   1.00 14.05  ? 69  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 83  ? -1.879  18.990  5.378   1.00 14.34  ? 69  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 83  ? -2.023  17.770  6.283   1.00 15.05  ? 69  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 83  ? -2.595  18.772  4.040   1.00 15.26  ? 69  LEU A CD2 1 
ATOM   494  N  N   . LYS A 1 84  ? 0.769   20.197  7.536   1.00 13.43  ? 70  LYS A N   1 
ATOM   495  C  CA  . LYS A 1 84  ? 2.204   20.432  7.371   1.00 14.43  ? 70  LYS A CA  1 
ATOM   496  C  C   . LYS A 1 84  ? 2.813   19.482  6.358   1.00 15.36  ? 70  LYS A C   1 
ATOM   497  O  O   . LYS A 1 84  ? 3.904   19.725  5.844   1.00 17.43  ? 70  LYS A O   1 
ATOM   498  C  CB  . LYS A 1 84  ? 2.911   20.381  8.732   1.00 21.46  ? 70  LYS A CB  1 
ATOM   499  C  CG  . LYS A 1 84  ? 2.349   21.363  9.749   1.00 24.83  ? 70  LYS A CG  1 
ATOM   500  C  CD  . LYS A 1 84  ? 2.291   22.803  9.226   1.00 29.44  ? 70  LYS A CD  1 
ATOM   501  C  CE  . LYS A 1 84  ? 1.651   23.801  10.177  1.00 40.21  ? 70  LYS A CE  1 
ATOM   502  N  NZ  . LYS A 1 84  ? 1.069   24.960  9.450   1.00 44.24  ? 70  LYS A NZ  1 
ATOM   503  N  N   . GLY A 1 85  ? 2.141   18.369  6.049   1.00 14.37  ? 71  GLY A N   1 
ATOM   504  C  CA  . GLY A 1 85  ? 2.673   17.444  5.070   1.00 16.17  ? 71  GLY A CA  1 
ATOM   505  C  C   . GLY A 1 85  ? 1.827   16.196  4.869   1.00 12.56  ? 71  GLY A C   1 
ATOM   506  O  O   . GLY A 1 85  ? 0.983   15.878  5.721   1.00 12.71  ? 71  GLY A O   1 
ATOM   507  N  N   . ILE A 1 86  ? 2.091   15.562  3.725   1.00 13.64  ? 72  ILE A N   1 
ATOM   508  C  CA  . ILE A 1 86  ? 1.533   14.272  3.354   1.00 11.79  ? 72  ILE A CA  1 
ATOM   509  C  C   . ILE A 1 86  ? 2.706   13.304  3.319   1.00 11.85  ? 72  ILE A C   1 
ATOM   510  O  O   . ILE A 1 86  ? 3.719   13.554  2.638   1.00 14.08  ? 72  ILE A O   1 
ATOM   511  C  CB  . ILE A 1 86  ? 0.871   14.355  1.976   1.00 14.70  ? 72  ILE A CB  1 
ATOM   512  C  CG1 . ILE A 1 86  ? -0.248  15.404  1.911   1.00 16.27  ? 72  ILE A CG1 1 
ATOM   513  C  CG2 . ILE A 1 86  ? 0.384   13.005  1.530   1.00 13.89  ? 72  ILE A CG2 1 
ATOM   514  C  CD1 . ILE A 1 86  ? -0.656  15.708  0.504   1.00 23.97  ? 72  ILE A CD1 1 
ATOM   515  N  N   . PHE A 1 87  ? 2.642   12.268  4.158   1.00 10.39  ? 73  PHE A N   1 
ATOM   516  C  CA  . PHE A 1 87  ? 3.747   11.323  4.333   1.00 10.12  ? 73  PHE A CA  1 
ATOM   517  C  C   . PHE A 1 87  ? 3.343   9.982   3.788   1.00 9.12   ? 73  PHE A C   1 
ATOM   518  O  O   . PHE A 1 87  ? 2.304   9.431   4.206   1.00 10.56  ? 73  PHE A O   1 
ATOM   519  C  CB  . PHE A 1 87  ? 4.064   11.184  5.817   1.00 11.97  ? 73  PHE A CB  1 
ATOM   520  C  CG  . PHE A 1 87  ? 4.453   12.498  6.417   1.00 13.90  ? 73  PHE A CG  1 
ATOM   521  C  CD1 . PHE A 1 87  ? 3.496   13.483  6.661   1.00 15.75  ? 73  PHE A CD1 1 
ATOM   522  C  CD2 . PHE A 1 87  ? 5.786   12.804  6.616   1.00 14.05  ? 73  PHE A CD2 1 
ATOM   523  C  CE1 . PHE A 1 87  ? 3.857   14.727  7.150   1.00 17.95  ? 73  PHE A CE1 1 
ATOM   524  C  CE2 . PHE A 1 87  ? 6.145   14.041  7.147   1.00 15.99  ? 73  PHE A CE2 1 
ATOM   525  C  CZ  . PHE A 1 87  ? 5.193   14.999  7.378   1.00 18.15  ? 73  PHE A CZ  1 
ATOM   526  N  N   . LEU A 1 88  ? 4.037   9.512   2.765   1.00 9.13   ? 74  LEU A N   1 
ATOM   527  C  CA  . LEU A 1 88  ? 3.642   8.331   2.024   1.00 10.10  ? 74  LEU A CA  1 
ATOM   528  C  C   . LEU A 1 88  ? 4.582   7.167   2.300   1.00 10.08  ? 74  LEU A C   1 
ATOM   529  O  O   . LEU A 1 88  ? 5.793   7.316   2.097   1.00 11.58  ? 74  LEU A O   1 
ATOM   530  C  CB  . LEU A 1 88  ? 3.640   8.690   0.538   1.00 9.82   ? 74  LEU A CB  1 
ATOM   531  C  CG  . LEU A 1 88  ? 2.735   9.840   0.137   1.00 10.36  ? 74  LEU A CG  1 
ATOM   532  C  CD1 . LEU A 1 88  ? 2.929   10.152  -1.333  1.00 11.84  ? 74  LEU A CD1 1 
ATOM   533  C  CD2 . LEU A 1 88  ? 1.290   9.522   0.488   1.00 11.84  ? 74  LEU A CD2 1 
ATOM   534  N  N   . THR A 1 89  ? 4.040   6.024   2.700   1.00 9.56   ? 75  THR A N   1 
ATOM   535  C  CA  . THR A 1 89  ? 4.846   4.905   3.155   1.00 9.93   ? 75  THR A CA  1 
ATOM   536  C  C   . THR A 1 89  ? 5.439   4.093   2.016   1.00 9.28   ? 75  THR A C   1 
ATOM   537  O  O   . THR A 1 89  ? 6.546   3.563   2.163   1.00 10.94  ? 75  THR A O   1 
ATOM   538  C  CB  . THR A 1 89  ? 4.018   4.006   4.095   1.00 9.82   ? 75  THR A CB  1 
ATOM   539  O  OG1 . THR A 1 89  ? 2.854   3.540   3.418   1.00 10.33  ? 75  THR A OG1 1 
ATOM   540  C  CG2 . THR A 1 89  ? 3.637   4.706   5.382   1.00 11.09  ? 75  THR A CG2 1 
ATOM   541  N  N   . HIS A 1 90  ? 4.734   3.961   0.921   1.00 9.52   ? 76  HIS A N   1 
ATOM   542  C  CA  . HIS A 1 90  ? 5.217   3.155   -0.167  1.00 10.30  ? 76  HIS A CA  1 
ATOM   543  C  C   . HIS A 1 90  ? 4.424   3.486   -1.401  1.00 10.39  ? 76  HIS A C   1 
ATOM   544  O  O   . HIS A 1 90  ? 3.387   4.128   -1.278  1.00 13.79  ? 76  HIS A O   1 
ATOM   545  C  CB  . HIS A 1 90  ? 5.062   1.654   0.189   1.00 13.51  ? 76  HIS A CB  1 
ATOM   546  C  CG  . HIS A 1 90  ? 3.642   1.091   0.318   1.00 13.30  ? 76  HIS A CG  1 
ATOM   547  N  ND1 . HIS A 1 90  ? 3.224   0.088   -0.527  1.00 21.72  ? 76  HIS A ND1 1 
ATOM   548  C  CD2 . HIS A 1 90  ? 2.536   1.124   1.179   1.00 15.18  ? 76  HIS A CD2 1 
ATOM   549  C  CE1 . HIS A 1 90  ? 2.003   -0.342  -0.294  1.00 22.91  ? 76  HIS A CE1 1 
ATOM   550  N  NE2 . HIS A 1 90  ? 1.630   0.071   0.727   1.00 20.81  ? 76  HIS A NE2 1 
ATOM   551  N  N   . GLY A 1 91  ? 4.864   3.003   -2.556  1.00 11.04  ? 77  GLY A N   1 
ATOM   552  C  CA  . GLY A 1 91  ? 4.384   3.495   -3.835  1.00 13.98  ? 77  GLY A CA  1 
ATOM   553  C  C   . GLY A 1 91  ? 3.152   2.816   -4.388  1.00 18.55  ? 77  GLY A C   1 
ATOM   554  O  O   . GLY A 1 91  ? 2.852   3.084   -5.552  1.00 21.48  ? 77  GLY A O   1 
ATOM   555  N  N   . ALA A 1 92  ? 2.472   1.986   -3.611  1.00 15.13  ? 78  ALA A N   1 
ATOM   556  C  CA  . ALA A 1 92  ? 1.294   1.270   -4.080  1.00 14.58  ? 78  ALA A CA  1 
ATOM   557  C  C   . ALA A 1 92  ? 0.008   2.067   -3.940  1.00 13.02  ? 78  ALA A C   1 
ATOM   558  O  O   . ALA A 1 92  ? -0.095  2.991   -3.146  1.00 12.06  ? 78  ALA A O   1 
ATOM   559  C  CB  . ALA A 1 92  ? 1.177   0.008   -3.313  1.00 18.54  ? 78  ALA A CB  1 
ATOM   560  N  N   . GLU A 1 93  ? -1.017  1.620   -4.647  1.00 14.59  ? 79  GLU A N   1 
ATOM   561  C  CA  . GLU A 1 93  ? -2.276  2.348   -4.724  1.00 15.54  ? 79  GLU A CA  1 
ATOM   562  C  C   . GLU A 1 93  ? -2.964  2.490   -3.376  1.00 12.81  ? 79  GLU A C   1 
ATOM   563  O  O   . GLU A 1 93  ? -3.591  3.511   -3.139  1.00 12.80  ? 79  GLU A O   1 
ATOM   564  C  CB  . GLU A 1 93  ? -3.234  1.673   -5.713  1.00 22.78  ? 79  GLU A CB  1 
ATOM   565  C  CG  . GLU A 1 93  ? -2.794  1.767   -7.159  1.00 27.97  ? 79  GLU A CG  1 
ATOM   566  C  CD  . GLU A 1 93  ? -2.692  3.142   -7.821  1.00 44.22  ? 79  GLU A CD  1 
ATOM   567  O  OE1 . GLU A 1 93  ? -1.940  4.046   -7.327  1.00 43.93  ? 79  GLU A OE1 1 
ATOM   568  O  OE2 . GLU A 1 93  ? -3.316  3.298   -8.894  1.00 59.95  ? 79  GLU A OE2 1 
ATOM   569  N  N   . HIS A 1 94  ? -2.784  1.520   -2.457  1.00 13.13  ? 80  HIS A N   1 
ATOM   570  C  CA  . HIS A 1 94  ? -3.334  1.656   -1.129  1.00 13.63  ? 80  HIS A CA  1 
ATOM   571  C  C   . HIS A 1 94  ? -2.766  2.784   -0.334  1.00 12.77  ? 80  HIS A C   1 
ATOM   572  O  O   . HIS A 1 94  ? -3.361  3.124   0.683   1.00 13.41  ? 80  HIS A O   1 
ATOM   573  C  CB  . HIS A 1 94  ? -2.979  0.470   -0.228  1.00 19.39  ? 80  HIS A CB  1 
ATOM   574  C  CG  . HIS A 1 94  ? -3.711  -0.786  -0.455  1.00 17.15  ? 80  HIS A CG  1 
ATOM   575  N  ND1 . HIS A 1 94  ? -4.536  -1.119  -1.495  1.00 18.36  ? 80  HIS A ND1 1 
ATOM   576  C  CD2 . HIS A 1 94  ? -3.677  -1.822  0.431   0.83 16.03  ? 80  HIS A CD2 1 
ATOM   577  C  CE1 . HIS A 1 94  ? -4.968  -2.362  -1.279  1.00 17.51  ? 80  HIS A CE1 1 
ATOM   578  N  NE2 . HIS A 1 94  ? -4.432  -2.821  -0.109  0.79 21.87  ? 80  HIS A NE2 1 
ATOM   579  N  N   . ALA A 1 95  ? -1.597  3.280   -0.710  1.00 11.60  ? 81  ALA A N   1 
ATOM   580  C  CA  . ALA A 1 95  ? -0.917  4.376   -0.047  1.00 11.99  ? 81  ALA A CA  1 
ATOM   581  C  C   . ALA A 1 95  ? -0.920  5.664   -0.859  1.00 9.87   ? 81  ALA A C   1 
ATOM   582  O  O   . ALA A 1 95  ? -0.909  6.713   -0.248  1.00 11.57  ? 81  ALA A O   1 
ATOM   583  C  CB  . ALA A 1 95  ? 0.499   3.975   0.323   1.00 14.35  ? 81  ALA A CB  1 
ATOM   584  N  N   . ILE A 1 96  ? -0.911  5.632   -2.197  1.00 10.59  ? 82  ILE A N   1 
ATOM   585  C  CA  . ILE A 1 96  ? -0.735  6.859   -2.943  1.00 10.82  ? 82  ILE A CA  1 
ATOM   586  C  C   . ILE A 1 96  ? -1.820  7.116   -3.965  1.00 10.82  ? 82  ILE A C   1 
ATOM   587  O  O   . ILE A 1 96  ? -1.786  8.171   -4.590  1.00 11.86  ? 82  ILE A O   1 
ATOM   588  C  CB  . ILE A 1 96  ? 0.638   6.874   -3.644  1.00 12.20  ? 82  ILE A CB  1 
ATOM   589  C  CG1 . ILE A 1 96  ? 0.735   5.906   -4.832  1.00 13.32  ? 82  ILE A CG1 1 
ATOM   590  C  CG2 . ILE A 1 96  ? 1.796   6.682   -2.677  1.00 14.65  ? 82  ILE A CG2 1 
ATOM   591  C  CD1 . ILE A 1 96  ? 1.877   6.219   -5.748  1.00 16.57  ? 82  ILE A CD1 1 
ATOM   592  N  N   . GLY A 1 97  ? -2.795  6.237   -4.110  1.00 11.28  ? 83  GLY A N   1 
ATOM   593  C  CA  . GLY A 1 97  ? -3.764  6.404   -5.173  1.00 13.25  ? 83  GLY A CA  1 
ATOM   594  C  C   . GLY A 1 97  ? -4.641  7.658   -5.120  1.00 12.33  ? 83  GLY A C   1 
ATOM   595  O  O   . GLY A 1 97  ? -5.155  8.050   -6.160  1.00 15.39  ? 83  GLY A O   1 
ATOM   596  N  N   . ALA A 1 98  ? -4.802  8.284   -3.971  1.00 11.76  ? 84  ALA A N   1 
ATOM   597  C  CA  . ALA A 1 98  ? -5.614  9.484   -3.865  1.00 11.96  ? 84  ALA A CA  1 
ATOM   598  C  C   . ALA A 1 98  ? -4.759  10.742  -3.901  1.00 11.78  ? 84  ALA A C   1 
ATOM   599  O  O   . ALA A 1 98  ? -5.305  11.841  -3.823  1.00 13.12  ? 84  ALA A O   1 
ATOM   600  C  CB  . ALA A 1 98  ? -6.441  9.453   -2.595  1.00 12.43  ? 84  ALA A CB  1 
ATOM   601  N  N   . VAL A 1 99  ? -3.424  10.636  -3.954  1.00 12.12  ? 85  VAL A N   1 
ATOM   602  C  CA  . VAL A 1 99  ? -2.580  11.807  -3.721  1.00 12.43  ? 85  VAL A CA  1 
ATOM   603  C  C   . VAL A 1 99  ? -2.899  12.936  -4.703  1.00 11.47  ? 85  VAL A C   1 
ATOM   604  O  O   . VAL A 1 99  ? -2.971  14.107  -4.345  1.00 12.87  ? 85  VAL A O   1 
ATOM   605  C  CB  . VAL A 1 99  ? -1.081  11.448  -3.751  1.00 14.44  ? 85  VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 99  ? -0.202  12.701  -3.845  1.00 15.39  ? 85  VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 99  ? -0.756  10.608  -2.550  1.00 14.73  ? 85  VAL A CG2 1 
ATOM   608  N  N   . SER A 1 100 ? -3.008  12.589  -5.977  1.00 13.77  ? 86  SER A N   1 
ATOM   609  C  CA  . SER A 1 100 ? -3.265  13.590  -7.005  1.00 14.30  ? 86  SER A CA  1 
ATOM   610  C  C   . SER A 1 100 ? -4.568  14.366  -6.743  1.00 15.39  ? 86  SER A C   1 
ATOM   611  O  O   . SER A 1 100 ? -4.654  15.605  -6.879  1.00 17.74  ? 86  SER A O   1 
ATOM   612  C  CB  . SER A 1 100 ? -3.241  12.977  -8.396  1.00 16.96  ? 86  SER A CB  1 
ATOM   613  O  OG  . SER A 1 100 ? -4.326  12.099  -8.632  1.00 18.05  ? 86  SER A OG  1 
ATOM   614  N  N   . TYR A 1 101 ? -5.610  13.671  -6.285  1.00 14.12  ? 87  TYR A N   1 
ATOM   615  C  CA  . TYR A 1 101 ? -6.883  14.271  -5.924  1.00 14.17  ? 87  TYR A CA  1 
ATOM   616  C  C   . TYR A 1 101 ? -6.780  15.163  -4.689  1.00 13.68  ? 87  TYR A C   1 
ATOM   617  O  O   . TYR A 1 101 ? -7.380  16.241  -4.635  1.00 16.27  ? 87  TYR A O   1 
ATOM   618  C  CB  . TYR A 1 101 ? -7.920  13.167  -5.670  1.00 15.11  ? 87  TYR A CB  1 
ATOM   619  C  CG  . TYR A 1 101 ? -8.141  12.341  -6.906  1.00 14.00  ? 87  TYR A CG  1 
ATOM   620  C  CD1 . TYR A 1 101 ? -9.096  12.713  -7.844  1.00 16.99  ? 87  TYR A CD1 1 
ATOM   621  C  CD2 . TYR A 1 101 ? -7.398  11.196  -7.169  1.00 14.78  ? 87  TYR A CD2 1 
ATOM   622  C  CE1 . TYR A 1 101 ? -9.278  11.995  -9.013  1.00 18.07  ? 87  TYR A CE1 1 
ATOM   623  C  CE2 . TYR A 1 101 ? -7.546  10.491  -8.349  1.00 16.80  ? 87  TYR A CE2 1 
ATOM   624  C  CZ  . TYR A 1 101 ? -8.509  10.879  -9.271  1.00 18.57  ? 87  TYR A CZ  1 
ATOM   625  O  OH  . TYR A 1 101 ? -8.681  10.179  -10.448 1.00 21.50  ? 87  TYR A OH  1 
ATOM   626  N  N   . VAL A 1 102 ? -5.974  14.772  -3.689  1.00 13.47  ? 88  VAL A N   1 
ATOM   627  C  CA  . VAL A 1 102 ? -5.771  15.586  -2.507  1.00 13.58  ? 88  VAL A CA  1 
ATOM   628  C  C   . VAL A 1 102 ? -5.097  16.896  -2.914  1.00 14.24  ? 88  VAL A C   1 
ATOM   629  O  O   . VAL A 1 102 ? -5.482  17.968  -2.443  1.00 15.35  ? 88  VAL A O   1 
ATOM   630  C  CB  . VAL A 1 102 ? -4.902  14.835  -1.479  1.00 12.94  ? 88  VAL A CB  1 
ATOM   631  C  CG1 . VAL A 1 102 ? -4.464  15.722  -0.328  1.00 13.69  ? 88  VAL A CG1 1 
ATOM   632  C  CG2 . VAL A 1 102 ? -5.675  13.631  -0.947  1.00 13.98  ? 88  VAL A CG2 1 
ATOM   633  N  N   . LEU A 1 103 ? -4.047  16.755  -3.736  1.00 12.61  ? 89  LEU A N   1 
ATOM   634  C  CA  . LEU A 1 103 ? -3.271  17.919  -4.138  1.00 15.50  ? 89  LEU A CA  1 
ATOM   635  C  C   . LEU A 1 103 ? -4.099  18.924  -4.945  1.00 16.27  ? 89  LEU A C   1 
ATOM   636  O  O   . LEU A 1 103 ? -3.727  20.084  -5.025  1.00 18.30  ? 89  LEU A O   1 
ATOM   637  C  CB  . LEU A 1 103 ? -2.026  17.473  -4.908  1.00 14.82  ? 89  LEU A CB  1 
ATOM   638  C  CG  . LEU A 1 103 ? -0.970  16.844  -3.998  1.00 16.51  ? 89  LEU A CG  1 
ATOM   639  C  CD1 . LEU A 1 103 ? 0.167   16.215  -4.808  1.00 19.80  ? 89  LEU A CD1 1 
ATOM   640  C  CD2 . LEU A 1 103 ? -0.412  17.881  -3.016  1.00 18.48  ? 89  LEU A CD2 1 
ATOM   641  N  N   . GLU A 1 104 ? -5.179  18.497  -5.593  1.00 16.08  ? 90  GLU A N   1 
ATOM   642  C  CA  . GLU A 1 104 ? -6.065  19.439  -6.270  1.00 19.45  ? 90  GLU A CA  1 
ATOM   643  C  C   . GLU A 1 104 ? -6.790  20.358  -5.290  1.00 17.95  ? 90  GLU A C   1 
ATOM   644  O  O   . GLU A 1 104 ? -7.233  21.447  -5.682  1.00 24.94  ? 90  GLU A O   1 
ATOM   645  C  CB  . GLU A 1 104 ? -7.087  18.668  -7.106  1.00 20.46  ? 90  GLU A CB  1 
ATOM   646  C  CG  . GLU A 1 104 ? -6.480  17.939  -8.319  1.00 30.21  ? 90  GLU A CG  1 
ATOM   647  C  CD  . GLU A 1 104 ? -7.457  17.255  -9.278  1.00 41.70  ? 90  GLU A CD  1 
ATOM   648  O  OE1 . GLU A 1 104 ? -7.893  16.098  -9.016  1.00 29.95  ? 90  GLU A OE1 1 
ATOM   649  O  OE2 . GLU A 1 104 ? -7.813  17.880  -10.290 1.00 39.45  ? 90  GLU A OE2 1 
ATOM   650  N  N   . GLN A 1 105 ? -7.014  19.905  -4.056  1.00 18.56  ? 91  GLN A N   1 
ATOM   651  C  CA  . GLN A 1 105 ? -7.810  20.598  -3.054  1.00 21.49  ? 91  GLN A CA  1 
ATOM   652  C  C   . GLN A 1 105 ? -6.952  21.373  -2.061  1.00 20.03  ? 91  GLN A C   1 
ATOM   653  O  O   . GLN A 1 105 ? -7.400  22.390  -1.542  1.00 22.66  ? 91  GLN A O   1 
ATOM   654  C  CB  . GLN A 1 105 ? -8.656  19.601  -2.272  1.00 19.05  ? 91  GLN A CB  1 
ATOM   655  C  CG  . GLN A 1 105 ? -9.570  18.761  -3.147  1.00 24.84  ? 91  GLN A CG  1 
ATOM   656  C  CD  . GLN A 1 105 ? -10.973 19.265  -2.977  1.00 40.35  ? 91  GLN A CD  1 
ATOM   657  O  OE1 . GLN A 1 105 ? -11.861 18.524  -2.563  1.00 69.71  ? 91  GLN A OE1 1 
ATOM   658  N  NE2 . GLN A 1 105 ? -11.151 20.561  -3.181  1.00 30.26  ? 91  GLN A NE2 1 
ATOM   659  N  N   . ILE A 1 106 ? -5.734  20.898  -1.772  1.00 19.72  ? 92  ILE A N   1 
ATOM   660  C  CA  . ILE A 1 106 ? -4.874  21.471  -0.755  1.00 21.72  ? 92  ILE A CA  1 
ATOM   661  C  C   . ILE A 1 106 ? -3.434  21.402  -1.256  1.00 20.53  ? 92  ILE A C   1 
ATOM   662  O  O   . ILE A 1 106 ? -3.050  20.477  -1.941  1.00 24.92  ? 92  ILE A O   1 
ATOM   663  C  CB  . ILE A 1 106 ? -5.007  20.742  0.597   1.00 24.94  ? 92  ILE A CB  1 
ATOM   664  C  CG1 . ILE A 1 106 ? -6.447  20.673  1.106   1.00 28.91  ? 92  ILE A CG1 1 
ATOM   665  C  CG2 . ILE A 1 106 ? -4.069  21.369  1.626   1.00 37.60  ? 92  ILE A CG2 1 
ATOM   666  C  CD1 . ILE A 1 106 ? -6.620  19.787  2.312   1.00 36.25  ? 92  ILE A CD1 1 
ATOM   667  N  N   . ASP A 1 107 ? -2.634  22.398  -0.888  1.00 30.97  ? 93  ASP A N   1 
ATOM   668  C  CA  . ASP A 1 107 ? -1.201  22.446  -1.156  1.00 31.92  ? 93  ASP A CA  1 
ATOM   669  C  C   . ASP A 1 107 ? -0.443  22.102  0.127   1.00 66.99  ? 93  ASP A C   1 
ATOM   670  O  O   . ASP A 1 107 ? -0.526  22.823  1.123   1.00 74.03  ? 93  ASP A O   1 
ATOM   671  C  CB  . ASP A 1 107 ? -0.815  23.828  -1.695  1.00 41.52  ? 93  ASP A CB  1 
ATOM   672  N  N   . ALA A 1 108 ? 0.288   20.974  0.095   1.00 21.51  ? 94  ALA A N   1 
ATOM   673  C  CA  . ALA A 1 108 ? 1.141   20.601  1.204   1.00 19.11  ? 94  ALA A CA  1 
ATOM   674  C  C   . ALA A 1 108 ? 2.332   19.835  0.605   1.00 16.87  ? 94  ALA A C   1 
ATOM   675  O  O   . ALA A 1 108 ? 2.193   19.219  -0.466  1.00 19.88  ? 94  ALA A O   1 
ATOM   676  C  CB  . ALA A 1 108 ? 0.374   19.767  2.193   1.00 25.85  ? 94  ALA A CB  1 
ATOM   677  N  N   . PRO A 1 109 ? 3.489   19.846  1.290   1.00 18.13  ? 95  PRO A N   1 
ATOM   678  C  CA  . PRO A 1 109 ? 4.604   19.017  0.830   1.00 17.90  ? 95  PRO A CA  1 
ATOM   679  C  C   . PRO A 1 109 ? 4.280   17.536  0.909   1.00 14.90  ? 95  PRO A C   1 
ATOM   680  O  O   . PRO A 1 109 ? 3.507   17.088  1.778   1.00 15.37  ? 95  PRO A O   1 
ATOM   681  C  CB  . PRO A 1 109 ? 5.746   19.394  1.791   1.00 25.13  ? 95  PRO A CB  1 
ATOM   682  C  CG  . PRO A 1 109 ? 5.305   20.651  2.511   1.00 27.83  ? 95  PRO A CG  1 
ATOM   683  C  CD  . PRO A 1 109 ? 3.798   20.543  2.543   1.00 22.41  ? 95  PRO A CD  1 
ATOM   684  N  N   . VAL A 1 110 ? 4.901   16.800  -0.004  1.00 13.62  ? 96  VAL A N   1 
ATOM   685  C  CA  . VAL A 1 110 ? 4.711   15.364  -0.138  1.00 12.13  ? 96  VAL A CA  1 
ATOM   686  C  C   . VAL A 1 110 ? 6.045   14.685  0.152   1.00 12.21  ? 96  VAL A C   1 
ATOM   687  O  O   . VAL A 1 110 ? 7.021   14.852  -0.595  1.00 12.95  ? 96  VAL A O   1 
ATOM   688  C  CB  . VAL A 1 110 ? 4.234   14.959  -1.547  1.00 12.76  ? 96  VAL A CB  1 
ATOM   689  C  CG1 . VAL A 1 110 ? 4.164   13.456  -1.717  1.00 14.67  ? 96  VAL A CG1 1 
ATOM   690  C  CG2 . VAL A 1 110 ? 2.909   15.617  -1.890  1.00 15.84  ? 96  VAL A CG2 1 
ATOM   691  N  N   . TYR A 1 111 ? 6.117   13.947  1.261   1.00 11.31  ? 97  TYR A N   1 
ATOM   692  C  CA  . TYR A 1 111 ? 7.308   13.244  1.703   1.00 10.95  ? 97  TYR A CA  1 
ATOM   693  C  C   . TYR A 1 111 ? 7.177   11.763  1.350   1.00 10.29  ? 97  TYR A C   1 
ATOM   694  O  O   . TYR A 1 111 ? 6.157   11.106  1.644   1.00 12.34  ? 97  TYR A O   1 
ATOM   695  C  CB  . TYR A 1 111 ? 7.423   13.371  3.226   1.00 12.54  ? 97  TYR A CB  1 
ATOM   696  C  CG  . TYR A 1 111 ? 7.564   14.809  3.662   1.00 11.92  ? 97  TYR A CG  1 
ATOM   697  C  CD1 . TYR A 1 111 ? 8.806   15.401  3.845   1.00 12.82  ? 97  TYR A CD1 1 
ATOM   698  C  CD2 . TYR A 1 111 ? 6.465   15.579  3.972   1.00 13.52  ? 97  TYR A CD2 1 
ATOM   699  C  CE1 . TYR A 1 111 ? 8.939   16.709  4.282   1.00 14.56  ? 97  TYR A CE1 1 
ATOM   700  C  CE2 . TYR A 1 111 ? 6.580   16.908  4.363   1.00 15.46  ? 97  TYR A CE2 1 
ATOM   701  C  CZ  . TYR A 1 111 ? 7.826   17.465  4.564   1.00 13.91  ? 97  TYR A CZ  1 
ATOM   702  O  OH  . TYR A 1 111 ? 7.951   18.785  4.967   1.00 17.39  ? 97  TYR A OH  1 
ATOM   703  N  N   . GLY A 1 112 ? 8.251   11.164  0.822   1.00 11.07  ? 98  GLY A N   1 
ATOM   704  C  CA  . GLY A 1 112 ? 8.236   9.735   0.547   1.00 10.87  ? 98  GLY A CA  1 
ATOM   705  C  C   . GLY A 1 112 ? 9.600   9.295   0.048   1.00 11.22  ? 98  GLY A C   1 
ATOM   706  O  O   . GLY A 1 112 ? 10.493  10.146  -0.129  1.00 11.85  ? 98  GLY A O   1 
ATOM   707  N  N   . SER A 1 113 ? 9.807   7.993   -0.011  1.00 11.23  ? 99  SER A N   1 
ATOM   708  C  CA  . SER A 1 113 ? 11.071  7.457   -0.490  1.00 11.69  ? 99  SER A CA  1 
ATOM   709  C  C   . SER A 1 113 ? 11.299  7.848   -1.935  1.00 12.23  ? 99  SER A C   1 
ATOM   710  O  O   . SER A 1 113 ? 10.374  8.263   -2.652  1.00 12.09  ? 99  SER A O   1 
ATOM   711  C  CB  . SER A 1 113 ? 11.099  5.959   -0.378  1.00 12.79  ? 99  SER A CB  1 
ATOM   712  O  OG  . SER A 1 113 ? 10.218  5.411   -1.335  1.00 13.69  ? 99  SER A OG  1 
ATOM   713  N  N   . LYS A 1 114 ? 12.545  7.618   -2.408  1.00 13.47  ? 100 LYS A N   1 
ATOM   714  C  CA  . LYS A 1 114 ? 12.806  7.981   -3.798  1.00 15.63  ? 100 LYS A CA  1 
ATOM   715  C  C   . LYS A 1 114 ? 11.885  7.280   -4.780  1.00 15.51  ? 100 LYS A C   1 
ATOM   716  O  O   . LYS A 1 114 ? 11.458  7.861   -5.774  1.00 15.29  ? 100 LYS A O   1 
ATOM   717  C  CB  . LYS A 1 114 ? 14.255  7.796   -4.226  1.00 22.65  ? 100 LYS A CB  1 
ATOM   718  C  CG  . LYS A 1 114 ? 14.865  6.426   -4.058  1.00 23.22  ? 100 LYS A CG  1 
ATOM   719  C  CD  . LYS A 1 114 ? 16.297  6.413   -4.621  1.00 23.12  ? 100 LYS A CD  1 
ATOM   720  C  CE  . LYS A 1 114 ? 16.402  6.702   -6.107  1.00 37.41  ? 100 LYS A CE  1 
ATOM   721  N  NZ  . LYS A 1 114 ? 17.786  6.537   -6.625  1.00 52.73  ? 100 LYS A NZ  1 
ATOM   722  N  N   . LEU A 1 115 ? 11.589  5.989   -4.561  1.00 14.05  ? 101 LEU A N   1 
ATOM   723  C  CA  . LEU A 1 115 ? 10.661  5.318   -5.467  1.00 13.89  ? 101 LEU A CA  1 
ATOM   724  C  C   . LEU A 1 115 ? 9.227   5.864   -5.354  1.00 12.44  ? 101 LEU A C   1 
ATOM   725  O  O   . LEU A 1 115 ? 8.556   6.055   -6.374  1.00 13.88  ? 101 LEU A O   1 
ATOM   726  C  CB  . LEU A 1 115 ? 10.755  3.804   -5.239  1.00 14.30  ? 101 LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 115 ? 9.739   2.973   -6.048  1.00 15.64  ? 101 LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 115 ? 9.883   3.171   -7.569  1.00 17.11  ? 101 LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 115 ? 9.900   1.499   -5.719  1.00 16.63  ? 101 LEU A CD2 1 
ATOM   730  N  N   . THR A 1 116 ? 8.778   6.060   -4.112  1.00 13.13  ? 102 THR A N   1 
ATOM   731  C  CA  . THR A 1 116 ? 7.440   6.562   -3.891  1.00 12.49  ? 102 THR A CA  1 
ATOM   732  C  C   . THR A 1 116 ? 7.245   7.889   -4.632  1.00 13.51  ? 102 THR A C   1 
ATOM   733  O  O   . THR A 1 116 ? 6.239   8.137   -5.308  1.00 13.93  ? 102 THR A O   1 
ATOM   734  C  CB  . THR A 1 116 ? 7.151   6.724   -2.411  1.00 13.16  ? 102 THR A CB  1 
ATOM   735  O  OG1 . THR A 1 116 ? 7.247   5.392   -1.869  1.00 13.62  ? 102 THR A OG1 1 
ATOM   736  C  CG2 . THR A 1 116 ? 5.778   7.316   -2.157  1.00 15.30  ? 102 THR A CG2 1 
ATOM   737  N  N   . ILE A 1 117 ? 8.235   8.815   -4.498  1.00 13.14  ? 103 ILE A N   1 
ATOM   738  C  CA  . ILE A 1 117 ? 8.113   10.123  -5.141  1.00 15.09  ? 103 ILE A CA  1 
ATOM   739  C  C   . ILE A 1 117 ? 8.051   9.966   -6.663  1.00 16.05  ? 103 ILE A C   1 
ATOM   740  O  O   . ILE A 1 117 ? 7.283   10.644  -7.349  1.00 15.96  ? 103 ILE A O   1 
ATOM   741  C  CB  . ILE A 1 117 ? 9.278   11.049  -4.720  1.00 16.60  ? 103 ILE A CB  1 
ATOM   742  C  CG1 . ILE A 1 117 ? 9.215   11.372  -3.220  1.00 17.28  ? 103 ILE A CG1 1 
ATOM   743  C  CG2 . ILE A 1 117 ? 9.356   12.293  -5.608  1.00 16.73  ? 103 ILE A CG2 1 
ATOM   744  C  CD1 . ILE A 1 117 ? 7.984   12.122  -2.769  1.00 17.64  ? 103 ILE A CD1 1 
ATOM   745  N  N   . ALA A 1 118 ? 8.889   9.091   -7.223  1.00 15.74  ? 104 ALA A N   1 
ATOM   746  C  CA  . ALA A 1 118 ? 8.877   8.917   -8.669  1.00 17.04  ? 104 ALA A CA  1 
ATOM   747  C  C   . ALA A 1 118 ? 7.497   8.433   -9.131  1.00 17.31  ? 104 ALA A C   1 
ATOM   748  O  O   . ALA A 1 118 ? 6.999   8.836   -10.176 1.00 17.77  ? 104 ALA A O   1 
ATOM   749  C  CB  . ALA A 1 118 ? 9.978   7.969   -9.121  1.00 18.16  ? 104 ALA A CB  1 
ATOM   750  N  N   . LEU A 1 119 ? 6.886   7.539   -8.359  1.00 15.71  ? 105 LEU A N   1 
ATOM   751  C  CA  . LEU A 1 119 ? 5.596   6.993   -8.758  1.00 15.52  ? 105 LEU A CA  1 
ATOM   752  C  C   . LEU A 1 119 ? 4.484   8.027   -8.613  1.00 14.70  ? 105 LEU A C   1 
ATOM   753  O  O   . LEU A 1 119 ? 3.568   8.088   -9.451  1.00 17.35  ? 105 LEU A O   1 
ATOM   754  C  CB  . LEU A 1 119 ? 5.313   5.720   -7.959  1.00 16.77  ? 105 LEU A CB  1 
ATOM   755  C  CG  . LEU A 1 119 ? 6.262   4.582   -8.311  1.00 15.98  ? 105 LEU A CG  1 
ATOM   756  C  CD1 . LEU A 1 119 ? 6.103   3.436   -7.339  1.00 18.49  ? 105 LEU A CD1 1 
ATOM   757  C  CD2 . LEU A 1 119 ? 6.056   4.122   -9.745  1.00 21.34  ? 105 LEU A CD2 1 
ATOM   758  N  N   . VAL A 1 120 ? 4.558   8.901   -7.598  1.00 14.54  ? 106 VAL A N   1 
ATOM   759  C  CA  . VAL A 1 120 ? 3.577   9.954   -7.515  1.00 14.79  ? 106 VAL A CA  1 
ATOM   760  C  C   . VAL A 1 120 ? 3.690   10.892  -8.711  1.00 17.96  ? 106 VAL A C   1 
ATOM   761  O  O   . VAL A 1 120 ? 2.696   11.306  -9.297  1.00 17.42  ? 106 VAL A O   1 
ATOM   762  C  CB  . VAL A 1 120 ? 3.673   10.702  -6.191  1.00 13.86  ? 106 VAL A CB  1 
ATOM   763  C  CG1 . VAL A 1 120 ? 2.752   11.904  -6.247  1.00 16.02  ? 106 VAL A CG1 1 
ATOM   764  C  CG2 . VAL A 1 120 ? 3.385   9.797   -4.998  1.00 13.75  ? 106 VAL A CG2 1 
ATOM   765  N  N   . LYS A 1 121 ? 4.924   11.233  -9.098  1.00 16.00  ? 107 LYS A N   1 
ATOM   766  C  CA  . LYS A 1 121 ? 5.076   12.068  -10.294 1.00 17.74  ? 107 LYS A CA  1 
ATOM   767  C  C   . LYS A 1 121 ? 4.458   11.458  -11.545 1.00 21.25  ? 107 LYS A C   1 
ATOM   768  O  O   . LYS A 1 121 ? 3.854   12.182  -12.361 1.00 21.79  ? 107 LYS A O   1 
ATOM   769  C  CB  . LYS A 1 121 ? 6.550   12.291  -10.564 1.00 19.77  ? 107 LYS A CB  1 
ATOM   770  C  CG  . LYS A 1 121 ? 7.166   13.248  -9.583  1.00 18.92  ? 107 LYS A CG  1 
ATOM   771  C  CD  . LYS A 1 121 ? 8.579   13.516  -9.940  1.00 25.19  ? 107 LYS A CD  1 
ATOM   772  C  CE  . LYS A 1 121 ? 9.332   14.317  -8.913  1.00 25.31  ? 107 LYS A CE  1 
ATOM   773  N  NZ  . LYS A 1 121 ? 10.747  14.315  -9.321  1.00 31.08  ? 107 LYS A NZ  1 
ATOM   774  N  N   . GLU A 1 122 ? 4.616   10.152  -11.710 1.00 22.55  ? 108 GLU A N   1 
ATOM   775  C  CA  . GLU A 1 122 ? 4.035   9.471   -12.859 1.00 26.52  ? 108 GLU A CA  1 
ATOM   776  C  C   . GLU A 1 122 ? 2.508   9.584   -12.800 1.00 26.01  ? 108 GLU A C   1 
ATOM   777  O  O   . GLU A 1 122 ? 1.875   9.803   -13.846 1.00 27.33  ? 108 GLU A O   1 
ATOM   778  C  CB  . GLU A 1 122 ? 4.514   8.014   -12.922 1.00 26.11  ? 108 GLU A CB  1 
ATOM   779  C  CG  . GLU A 1 122 ? 3.977   7.246   -14.119 1.00 38.26  ? 108 GLU A CG  1 
ATOM   780  C  CD  . GLU A 1 122 ? 4.176   7.952   -15.452 1.00 61.37  ? 108 GLU A CD  1 
ATOM   781  O  OE1 . GLU A 1 122 ? 5.299   8.445   -15.676 1.00 52.02  ? 108 GLU A OE1 1 
ATOM   782  O  OE2 . GLU A 1 122 ? 3.205   8.021   -16.254 1.00 58.94  ? 108 GLU A OE2 1 
ATOM   783  N  N   . ALA A 1 123 ? 1.920   9.495   -11.583 1.00 22.79  ? 109 ALA A N   1 
ATOM   784  C  CA  . ALA A 1 123 ? 0.467   9.595   -11.426 1.00 21.80  ? 109 ALA A CA  1 
ATOM   785  C  C   . ALA A 1 123 ? -0.028  10.987  -11.802 1.00 22.47  ? 109 ALA A C   1 
ATOM   786  O  O   . ALA A 1 123 ? -1.059  11.145  -12.428 1.00 22.88  ? 109 ALA A O   1 
ATOM   787  C  CB  . ALA A 1 123 ? 0.046   9.233   -10.018 1.00 21.07  ? 109 ALA A CB  1 
ATOM   788  N  N   . MET A 1 124 ? 0.724   12.007  -11.410 1.00 21.17  ? 110 MET A N   1 
ATOM   789  C  CA  . MET A 1 124 ? 0.359   13.374  -11.749 1.00 22.23  ? 110 MET A CA  1 
ATOM   790  C  C   . MET A 1 124 ? 0.430   13.557  -13.268 1.00 25.20  ? 110 MET A C   1 
ATOM   791  O  O   . MET A 1 124 ? -0.451  14.193  -13.847 1.00 24.91  ? 110 MET A O   1 
ATOM   792  C  CB  . MET A 1 124 ? 1.299   14.356  -11.044 1.00 20.01  ? 110 MET A CB  1 
ATOM   793  C  CG  . MET A 1 124 ? 1.208   14.300  -9.517  1.00 20.08  ? 110 MET A CG  1 
ATOM   794  S  SD  . MET A 1 124 ? -0.355  14.842  -8.831  1.00 22.57  ? 110 MET A SD  1 
ATOM   795  C  CE  . MET A 1 124 ? -0.194  16.620  -8.779  1.00 31.08  ? 110 MET A CE  1 
ATOM   796  N  N   . LYS A 1 125 ? 1.470   12.994  -13.901 1.00 24.62  ? 111 LYS A N   1 
ATOM   797  C  CA  . LYS A 1 125 ? 1.675   13.108  -15.343 1.00 30.32  ? 111 LYS A CA  1 
ATOM   798  C  C   . LYS A 1 125 ? 0.536   12.421  -16.105 1.00 36.68  ? 111 LYS A C   1 
ATOM   799  O  O   . LYS A 1 125 ? 0.030   12.956  -17.098 1.00 32.93  ? 111 LYS A O   1 
ATOM   800  C  CB  . LYS A 1 125 ? 3.065   12.556  -15.689 1.00 32.85  ? 111 LYS A CB  1 
ATOM   801  N  N   . ALA A 1 126 ? 0.098   11.255  -15.606 1.00 31.05  ? 112 ALA A N   1 
ATOM   802  C  CA  . ALA A 1 126 ? -0.978  10.494  -16.226 1.00 32.33  ? 112 ALA A CA  1 
ATOM   803  C  C   . ALA A 1 126 ? -2.299  11.266  -16.225 1.00 30.77  ? 112 ALA A C   1 
ATOM   804  O  O   . ALA A 1 126 ? -3.114  11.045  -17.117 1.00 35.65  ? 112 ALA A O   1 
ATOM   805  C  CB  . ALA A 1 126 ? -1.126  9.140   -15.575 1.00 31.54  ? 112 ALA A CB  1 
ATOM   806  N  N   . ARG A 1 127 ? -2.502  12.161  -15.247 1.00 26.83  ? 113 ARG A N   1 
ATOM   807  C  CA  . ARG A 1 127 ? -3.720  12.951  -15.175 1.00 24.89  ? 113 ARG A CA  1 
ATOM   808  C  C   . ARG A 1 127 ? -3.487  14.352  -15.726 1.00 28.20  ? 113 ARG A C   1 
ATOM   809  O  O   . ARG A 1 127 ? -4.363  15.207  -15.626 1.00 30.79  ? 113 ARG A O   1 
ATOM   810  C  CB  . ARG A 1 127 ? -4.217  13.052  -13.731 1.00 25.60  ? 113 ARG A CB  1 
ATOM   811  C  CG  . ARG A 1 127 ? -4.588  11.708  -13.136 1.00 28.16  ? 113 ARG A CG  1 
ATOM   812  C  CD  . ARG A 1 127 ? -5.211  11.842  -11.750 1.00 27.57  ? 113 ARG A CD  1 
ATOM   813  N  NE  . ARG A 1 127 ? -6.474  12.555  -11.806 1.00 26.07  ? 113 ARG A NE  1 
ATOM   814  C  CZ  . ARG A 1 127 ? -6.883  13.534  -11.008 1.00 25.84  ? 113 ARG A CZ  1 
ATOM   815  N  NH1 . ARG A 1 127 ? -6.355  13.725  -9.812  1.00 22.27  ? 113 ARG A NH1 1 
ATOM   816  N  NH2 . ARG A 1 127 ? -7.916  14.273  -11.379 1.00 27.89  ? 113 ARG A NH2 1 
ATOM   817  N  N   . ASN A 1 128 ? -2.281  14.583  -16.257 1.00 27.04  ? 114 ASN A N   1 
ATOM   818  C  CA  . ASN A 1 128 ? -1.938  15.853  -16.884 1.00 32.49  ? 114 ASN A CA  1 
ATOM   819  C  C   . ASN A 1 128 ? -2.099  17.010  -15.895 1.00 31.68  ? 114 ASN A C   1 
ATOM   820  O  O   . ASN A 1 128 ? -2.608  18.076  -16.232 1.00 34.07  ? 114 ASN A O   1 
ATOM   821  C  CB  . ASN A 1 128 ? -2.768  16.128  -18.137 1.00 33.69  ? 114 ASN A CB  1 
ATOM   822  C  CG  . ASN A 1 128 ? -2.277  17.352  -18.870 1.00 50.46  ? 114 ASN A CG  1 
ATOM   823  O  OD1 . ASN A 1 128 ? -3.033  17.977  -19.606 1.00 43.65  ? 114 ASN A OD1 1 
ATOM   824  N  ND2 . ASN A 1 128 ? -1.031  17.733  -18.620 1.00 52.24  ? 114 ASN A ND2 1 
ATOM   825  N  N   . ILE A 1 129 ? -1.649  16.801  -14.661 1.00 31.87  ? 115 ILE A N   1 
ATOM   826  C  CA  . ILE A 1 129 ? -1.666  17.848  -13.657 1.00 29.69  ? 115 ILE A CA  1 
ATOM   827  C  C   . ILE A 1 129 ? -0.291  18.492  -13.678 1.00 29.71  ? 115 ILE A C   1 
ATOM   828  O  O   . ILE A 1 129 ? 0.709   17.804  -13.454 1.00 34.49  ? 115 ILE A O   1 
ATOM   829  C  CB  . ILE A 1 129 ? -2.069  17.282  -12.277 1.00 32.04  ? 115 ILE A CB  1 
ATOM   830  C  CG1 . ILE A 1 129 ? -3.477  16.686  -12.354 1.00 35.55  ? 115 ILE A CG1 1 
ATOM   831  C  CG2 . ILE A 1 129 ? -1.961  18.337  -11.182 1.00 39.39  ? 115 ILE A CG2 1 
ATOM   832  C  CD1 . ILE A 1 129 ? -3.879  15.910  -11.147 1.00 38.27  ? 115 ILE A CD1 1 
ATOM   833  N  N   . LYS A 1 130 ? -0.271  19.792  -14.002 1.00 39.95  ? 116 LYS A N   1 
ATOM   834  C  CA  . LYS A 1 130 ? 0.973   20.522  -14.184 1.00 42.00  ? 116 LYS A CA  1 
ATOM   835  C  C   . LYS A 1 130 ? 1.227   21.447  -12.991 1.00 32.01  ? 116 LYS A C   1 
ATOM   836  O  O   . LYS A 1 130 ? 2.279   22.084  -12.954 1.00 46.05  ? 116 LYS A O   1 
ATOM   837  C  CB  . LYS A 1 130 ? 0.972   21.289  -15.519 1.00 38.91  ? 116 LYS A CB  1 
ATOM   838  N  N   . LYS A 1 131 ? 0.286   21.525  -12.031 1.00 40.09  ? 117 LYS A N   1 
ATOM   839  C  CA  . LYS A 1 131 ? 0.447   22.332  -10.828 1.00 33.81  ? 117 LYS A CA  1 
ATOM   840  C  C   . LYS A 1 131 ? 1.777   21.974  -10.146 1.00 40.33  ? 117 LYS A C   1 
ATOM   841  O  O   . LYS A 1 131 ? 2.210   20.816  -10.184 1.00 32.43  ? 117 LYS A O   1 
ATOM   842  C  CB  . LYS A 1 131 ? -0.739  22.120  -9.876  1.00 46.62  ? 117 LYS A CB  1 
ATOM   843  N  N   . LYS A 1 132 ? 2.445   22.984  -9.555  1.00 37.30  ? 118 LYS A N   1 
ATOM   844  C  CA  . LYS A 1 132 ? 3.698   22.771  -8.850  1.00 34.57  ? 118 LYS A CA  1 
ATOM   845  C  C   . LYS A 1 132 ? 3.393   21.935  -7.608  1.00 28.13  ? 118 LYS A C   1 
ATOM   846  O  O   . LYS A 1 132 ? 2.451   22.272  -6.907  1.00 36.31  ? 118 LYS A O   1 
ATOM   847  C  CB  . LYS A 1 132 ? 4.358   24.103  -8.469  1.00 30.99  ? 118 LYS A CB  1 
ATOM   848  N  N   . VAL A 1 133 ? 4.211   20.900  -7.359  1.00 25.23  ? 119 VAL A N   1 
ATOM   849  C  CA  . VAL A 1 133 ? 4.141   20.073  -6.161  1.00 23.05  ? 119 VAL A CA  1 
ATOM   850  C  C   . VAL A 1 133 ? 5.492   20.165  -5.452  1.00 18.53  ? 119 VAL A C   1 
ATOM   851  O  O   . VAL A 1 133 ? 6.533   20.065  -6.110  1.00 22.39  ? 119 VAL A O   1 
ATOM   852  C  CB  . VAL A 1 133 ? 3.816   18.603  -6.476  1.00 22.61  ? 119 VAL A CB  1 
ATOM   853  C  CG1 . VAL A 1 133 ? 3.761   17.753  -5.216  1.00 21.51  ? 119 VAL A CG1 1 
ATOM   854  C  CG2 . VAL A 1 133 ? 2.515   18.491  -7.243  1.00 31.32  ? 119 VAL A CG2 1 
ATOM   855  N  N   . ARG A 1 134 ? 5.497   20.321  -4.134  1.00 16.01  ? 120 ARG A N   1 
ATOM   856  C  CA  . ARG A 1 134 ? 6.701   20.264  -3.323  1.00 15.59  ? 120 ARG A CA  1 
ATOM   857  C  C   . ARG A 1 134 ? 6.979   18.845  -2.835  1.00 14.71  ? 120 ARG A C   1 
ATOM   858  O  O   . ARG A 1 134 ? 6.610   18.479  -1.708  1.00 20.78  ? 120 ARG A O   1 
ATOM   859  C  CB  . ARG A 1 134 ? 6.596   21.184  -2.120  1.00 18.33  ? 120 ARG A CB  1 
ATOM   860  C  CG  . ARG A 1 134 ? 6.531   22.644  -2.512  1.00 22.43  ? 120 ARG A CG  1 
ATOM   861  C  CD  . ARG A 1 134 ? 6.344   23.512  -1.271  1.00 25.86  ? 120 ARG A CD  1 
ATOM   862  N  NE  . ARG A 1 134 ? 4.935   23.509  -0.855  1.00 24.83  ? 120 ARG A NE  1 
ATOM   863  C  CZ  . ARG A 1 134 ? 4.462   23.781  0.366   1.00 28.99  ? 120 ARG A CZ  1 
ATOM   864  N  NH1 . ARG A 1 134 ? 5.269   24.007  1.386   1.00 29.86  ? 120 ARG A NH1 1 
ATOM   865  N  NH2 . ARG A 1 134 ? 3.154   23.784  0.570   1.00 34.57  ? 120 ARG A NH2 1 
ATOM   866  N  N   . TYR A 1 135 ? 7.710   18.078  -3.627  1.00 11.89  ? 121 TYR A N   1 
ATOM   867  C  CA  . TYR A 1 135 ? 8.152   16.756  -3.221  1.00 11.78  ? 121 TYR A CA  1 
ATOM   868  C  C   . TYR A 1 135 ? 9.353   16.883  -2.309  1.00 11.31  ? 121 TYR A C   1 
ATOM   869  O  O   . TYR A 1 135 ? 10.244  17.733  -2.564  1.00 12.39  ? 121 TYR A O   1 
ATOM   870  C  CB  . TYR A 1 135 ? 8.556   15.961  -4.448  1.00 13.49  ? 121 TYR A CB  1 
ATOM   871  C  CG  . TYR A 1 135 ? 7.440   15.727  -5.410  1.00 12.92  ? 121 TYR A CG  1 
ATOM   872  C  CD1 . TYR A 1 135 ? 6.395   14.872  -5.099  1.00 17.03  ? 121 TYR A CD1 1 
ATOM   873  C  CD2 . TYR A 1 135 ? 7.381   16.374  -6.622  1.00 15.26  ? 121 TYR A CD2 1 
ATOM   874  C  CE1 . TYR A 1 135 ? 5.370   14.645  -5.999  1.00 16.61  ? 121 TYR A CE1 1 
ATOM   875  C  CE2 . TYR A 1 135 ? 6.340   16.193  -7.522  1.00 17.22  ? 121 TYR A CE2 1 
ATOM   876  C  CZ  . TYR A 1 135 ? 5.324   15.308  -7.213  1.00 17.22  ? 121 TYR A CZ  1 
ATOM   877  O  OH  . TYR A 1 135 ? 4.270   15.061  -8.099  1.00 20.65  ? 121 TYR A OH  1 
ATOM   878  N  N   . TYR A 1 136 ? 9.476   15.988  -1.339  1.00 10.99  ? 122 TYR A N   1 
ATOM   879  C  CA  . TYR A 1 136 ? 10.635  15.895  -0.468  1.00 12.13  ? 122 TYR A CA  1 
ATOM   880  C  C   . TYR A 1 136 ? 10.966  14.423  -0.313  1.00 12.58  ? 122 TYR A C   1 
ATOM   881  O  O   . TYR A 1 136 ? 10.250  13.674  0.379   1.00 13.49  ? 122 TYR A O   1 
ATOM   882  C  CB  . TYR A 1 136 ? 10.450  16.569  0.904   1.00 15.72  ? 122 TYR A CB  1 
ATOM   883  C  CG  . TYR A 1 136 ? 10.309  18.069  0.755   1.00 25.26  ? 122 TYR A CG  1 
ATOM   884  C  CD1 . TYR A 1 136 ? 11.304  18.793  0.060   1.00 48.18  ? 122 TYR A CD1 1 
ATOM   885  C  CD2 . TYR A 1 136 ? 9.106   18.718  0.964   1.00 22.74  ? 122 TYR A CD2 1 
ATOM   886  C  CE1 . TYR A 1 136 ? 11.133  20.098  -0.350  1.00 28.17  ? 122 TYR A CE1 1 
ATOM   887  C  CE2 . TYR A 1 136 ? 8.937   20.055  0.616   1.00 25.92  ? 122 TYR A CE2 1 
ATOM   888  C  CZ  . TYR A 1 136 ? 9.951   20.743  -0.038  1.00 25.92  ? 122 TYR A CZ  1 
ATOM   889  O  OH  . TYR A 1 136 ? 9.755   22.053  -0.363  1.00 26.04  ? 122 TYR A OH  1 
ATOM   890  N  N   . THR A 1 137 ? 12.037  13.983  -0.976  1.00 11.90  ? 123 THR A N   1 
ATOM   891  C  CA  . THR A 1 137 ? 12.499  12.622  -0.808  1.00 11.93  ? 123 THR A CA  1 
ATOM   892  C  C   . THR A 1 137 ? 13.096  12.459  0.589   1.00 14.15  ? 123 THR A C   1 
ATOM   893  O  O   . THR A 1 137 ? 13.981  13.223  1.008   1.00 15.48  ? 123 THR A O   1 
ATOM   894  C  CB  . THR A 1 137 ? 13.520  12.279  -1.902  1.00 13.81  ? 123 THR A CB  1 
ATOM   895  O  OG1 . THR A 1 137 ? 12.880  12.390  -3.159  1.00 14.46  ? 123 THR A OG1 1 
ATOM   896  C  CG2 . THR A 1 137 ? 14.066  10.888  -1.709  1.00 16.37  ? 123 THR A CG2 1 
ATOM   897  N  N   . VAL A 1 138 ? 12.712  11.370  1.238   1.00 12.28  ? 124 VAL A N   1 
ATOM   898  C  CA  . VAL A 1 138 ? 13.192  10.975  2.543   1.00 12.93  ? 124 VAL A CA  1 
ATOM   899  C  C   . VAL A 1 138 ? 13.703  9.535   2.484   1.00 12.27  ? 124 VAL A C   1 
ATOM   900  O  O   . VAL A 1 138 ? 13.396  8.792   1.576   1.00 13.69  ? 124 VAL A O   1 
ATOM   901  C  CB  . VAL A 1 138 ? 12.147  11.155  3.659   1.00 12.65  ? 124 VAL A CB  1 
ATOM   902  C  CG1 . VAL A 1 138 ? 11.768  12.609  3.799   1.00 14.31  ? 124 VAL A CG1 1 
ATOM   903  C  CG2 . VAL A 1 138 ? 10.932  10.268  3.481   1.00 13.27  ? 124 VAL A CG2 1 
ATOM   904  N  N   . ASN A 1 139 ? 14.617  9.231   3.407   1.00 14.25  ? 125 ASN A N   1 
ATOM   905  C  CA  . ASN A 1 139 ? 15.016  7.855   3.657   1.00 14.48  ? 125 ASN A CA  1 
ATOM   906  C  C   . ASN A 1 139 ? 15.073  7.643   5.163   1.00 14.37  ? 125 ASN A C   1 
ATOM   907  O  O   . ASN A 1 139 ? 14.723  8.509   5.969   1.00 14.62  ? 125 ASN A O   1 
ATOM   908  C  CB  . ASN A 1 139 ? 16.322  7.546   2.896   1.00 15.01  ? 125 ASN A CB  1 
ATOM   909  C  CG  . ASN A 1 139 ? 17.462  8.434   3.305   1.00 15.73  ? 125 ASN A CG  1 
ATOM   910  O  OD1 . ASN A 1 139 ? 17.593  8.817   4.464   1.00 16.47  ? 125 ASN A OD1 1 
ATOM   911  N  ND2 . ASN A 1 139 ? 18.256  8.822   2.319   1.00 20.98  ? 125 ASN A ND2 1 
ATOM   912  N  N   . HIS A 1 140 ? 15.600  6.477   5.570   1.00 14.26  ? 126 HIS A N   1 
ATOM   913  C  CA  . HIS A 1 140 ? 15.634  6.150   6.975   1.00 14.15  ? 126 HIS A CA  1 
ATOM   914  C  C   . HIS A 1 140 ? 16.604  6.974   7.806   1.00 14.47  ? 126 HIS A C   1 
ATOM   915  O  O   . HIS A 1 140 ? 16.534  6.901   9.013   1.00 18.20  ? 126 HIS A O   1 
ATOM   916  C  CB  . HIS A 1 140 ? 15.879  4.671   7.186   1.00 15.35  ? 126 HIS A CB  1 
ATOM   917  C  CG  . HIS A 1 140 ? 17.220  4.161   6.747   1.00 16.99  ? 126 HIS A CG  1 
ATOM   918  N  ND1 . HIS A 1 140 ? 17.598  2.857   6.972   1.00 21.03  ? 126 HIS A ND1 1 
ATOM   919  C  CD2 . HIS A 1 140 ? 18.290  4.775   6.161   1.00 19.54  ? 126 HIS A CD2 1 
ATOM   920  C  CE1 . HIS A 1 140 ? 18.854  2.671   6.543   1.00 22.35  ? 126 HIS A CE1 1 
ATOM   921  N  NE2 . HIS A 1 140 ? 19.286  3.840   6.007   1.00 23.37  ? 126 HIS A NE2 1 
ATOM   922  N  N   . ASP A 1 141 ? 17.398  7.861   7.184   1.00 15.57  ? 127 ASP A N   1 
ATOM   923  C  CA  . ASP A 1 141 ? 18.227  8.781   7.922   1.00 17.76  ? 127 ASP A CA  1 
ATOM   924  C  C   . ASP A 1 141 ? 17.641  10.177  7.981   1.00 17.47  ? 127 ASP A C   1 
ATOM   925  O  O   . ASP A 1 141 ? 18.171  11.012  8.685   1.00 19.76  ? 127 ASP A O   1 
ATOM   926  C  CB  . ASP A 1 141 ? 19.615  8.829   7.299   1.00 19.00  ? 127 ASP A CB  1 
ATOM   927  C  CG  . ASP A 1 141 ? 20.424  7.558   7.556   1.00 24.06  ? 127 ASP A CG  1 
ATOM   928  O  OD1 . ASP A 1 141 ? 20.158  6.877   8.565   1.00 25.20  ? 127 ASP A OD1 1 
ATOM   929  O  OD2 . ASP A 1 141 ? 21.303  7.248   6.732   1.00 30.81  ? 127 ASP A OD2 1 
ATOM   930  N  N   . SER A 1 142 ? 16.495  10.407  7.312   1.00 15.82  ? 128 SER A N   1 
ATOM   931  C  CA  . SER A 1 142 ? 15.888  11.729  7.295   1.00 15.40  ? 128 SER A CA  1 
ATOM   932  C  C   . SER A 1 142 ? 15.208  12.016  8.632   1.00 15.22  ? 128 SER A C   1 
ATOM   933  O  O   . SER A 1 142 ? 14.464  11.181  9.144   1.00 15.37  ? 128 SER A O   1 
ATOM   934  C  CB  . SER A 1 142 ? 14.888  11.853  6.183   1.00 14.21  ? 128 SER A CB  1 
ATOM   935  O  OG  . SER A 1 142 ? 15.456  11.544  4.925   1.00 16.32  ? 128 SER A OG  1 
ATOM   936  N  N   . ILE A 1 143 ? 15.336  13.255  9.118   1.00 16.52  ? 129 ILE A N   1 
ATOM   937  C  CA  . ILE A 1 143 ? 14.532  13.752  10.215  1.00 16.61  ? 129 ILE A CA  1 
ATOM   938  C  C   . ILE A 1 143 ? 13.931  15.088  9.780   1.00 16.12  ? 129 ILE A C   1 
ATOM   939  O  O   . ILE A 1 143 ? 14.646  16.076  9.538   1.00 19.09  ? 129 ILE A O   1 
ATOM   940  C  CB  . ILE A 1 143 ? 15.356  13.878  11.515  1.00 19.82  ? 129 ILE A CB  1 
ATOM   941  C  CG1 . ILE A 1 143 ? 15.931  12.528  11.964  1.00 22.84  ? 129 ILE A CG1 1 
ATOM   942  C  CG2 . ILE A 1 143 ? 14.525  14.535  12.613  1.00 20.44  ? 129 ILE A CG2 1 
ATOM   943  C  CD1 . ILE A 1 143 ? 16.947  12.628  13.090  1.00 28.65  ? 129 ILE A CD1 1 
ATOM   944  N  N   . MET A 1 144 ? 12.606  15.122  9.664   1.00 16.41  ? 130 MET A N   1 
ATOM   945  C  CA  . MET A 1 144 ? 11.919  16.338  9.262   1.00 16.73  ? 130 MET A CA  1 
ATOM   946  C  C   . MET A 1 144 ? 11.477  17.082  10.509  1.00 17.78  ? 130 MET A C   1 
ATOM   947  O  O   . MET A 1 144 ? 10.790  16.524  11.359  1.00 19.39  ? 130 MET A O   1 
ATOM   948  C  CB  . MET A 1 144 ? 10.719  15.960  8.376   1.00 17.38  ? 130 MET A CB  1 
ATOM   949  C  CG  . MET A 1 144 ? 11.136  15.255  7.085   1.00 20.08  ? 130 MET A CG  1 
ATOM   950  S  SD  . MET A 1 144 ? 12.068  16.305  5.910   1.00 24.57  ? 130 MET A SD  1 
ATOM   951  C  CE  . MET A 1 144 ? 13.710  15.666  6.191   1.00 26.80  ? 130 MET A CE  1 
ATOM   952  N  N   . ARG A 1 145 ? 11.917  18.349  10.653  1.00 18.15  ? 131 ARG A N   1 
ATOM   953  C  CA  . ARG A 1 145 ? 11.629  19.111  11.855  1.00 19.32  ? 131 ARG A CA  1 
ATOM   954  C  C   . ARG A 1 145 ? 10.514  20.117  11.588  1.00 23.07  ? 131 ARG A C   1 
ATOM   955  O  O   . ARG A 1 145 ? 10.539  20.833  10.600  1.00 24.96  ? 131 ARG A O   1 
ATOM   956  C  CB  . ARG A 1 145 ? 12.906  19.789  12.353  1.00 21.61  ? 131 ARG A CB  1 
ATOM   957  C  CG  . ARG A 1 145 ? 14.067  18.814  12.523  1.00 25.57  ? 131 ARG A CG  1 
ATOM   958  C  CD  . ARG A 1 145 ? 15.325  19.451  13.064  1.00 26.90  ? 131 ARG A CD  1 
ATOM   959  N  NE  . ARG A 1 145 ? 16.318  18.446  13.449  1.00 31.36  ? 131 ARG A NE  1 
ATOM   960  C  CZ  . ARG A 1 145 ? 17.048  17.712  12.623  1.00 43.62  ? 131 ARG A CZ  1 
ATOM   961  N  NH1 . ARG A 1 145 ? 17.223  18.082  11.365  1.00 51.29  ? 131 ARG A NH1 1 
ATOM   962  N  NH2 . ARG A 1 145 ? 17.656  16.635  13.096  1.00 48.83  ? 131 ARG A NH2 1 
ATOM   963  N  N   . PHE A 1 146 ? 9.527   20.106  12.477  1.00 18.49  ? 132 PHE A N   1 
ATOM   964  C  CA  . PHE A 1 146 ? 8.381   20.994  12.431  1.00 18.29  ? 132 PHE A CA  1 
ATOM   965  C  C   . PHE A 1 146 ? 8.373   21.785  13.737  1.00 22.09  ? 132 PHE A C   1 
ATOM   966  O  O   . PHE A 1 146 ? 9.204   21.589  14.615  1.00 25.16  ? 132 PHE A O   1 
ATOM   967  C  CB  . PHE A 1 146 ? 7.106   20.162  12.182  1.00 17.62  ? 132 PHE A CB  1 
ATOM   968  C  CG  . PHE A 1 146 ? 7.126   19.405  10.882  1.00 17.09  ? 132 PHE A CG  1 
ATOM   969  C  CD1 . PHE A 1 146 ? 6.683   19.990  9.699   1.00 20.20  ? 132 PHE A CD1 1 
ATOM   970  C  CD2 . PHE A 1 146 ? 7.522   18.086  10.832  1.00 15.55  ? 132 PHE A CD2 1 
ATOM   971  C  CE1 . PHE A 1 146 ? 6.722   19.311  8.498   1.00 20.57  ? 132 PHE A CE1 1 
ATOM   972  C  CE2 . PHE A 1 146 ? 7.611   17.431  9.618   1.00 15.70  ? 132 PHE A CE2 1 
ATOM   973  C  CZ  . PHE A 1 146 ? 7.198   18.032  8.462   1.00 18.09  ? 132 PHE A CZ  1 
ATOM   974  N  N   . LYS A 1 147 ? 7.388   22.639  13.920  1.00 19.36  ? 133 LYS A N   1 
ATOM   975  C  CA  . LYS A 1 147 ? 7.348   23.430  15.148  1.00 20.64  ? 133 LYS A CA  1 
ATOM   976  C  C   . LYS A 1 147 ? 7.142   22.561  16.398  1.00 21.60  ? 133 LYS A C   1 
ATOM   977  O  O   . LYS A 1 147 ? 7.676   22.843  17.473  1.00 25.82  ? 133 LYS A O   1 
ATOM   978  C  CB  . LYS A 1 147 ? 6.215   24.454  15.006  1.00 25.24  ? 133 LYS A CB  1 
ATOM   979  C  CG  . LYS A 1 147 ? 6.219   25.585  16.018  1.00 32.01  ? 133 LYS A CG  1 
ATOM   980  C  CD  . LYS A 1 147 ? 5.245   26.709  15.660  1.00 39.67  ? 133 LYS A CD  1 
ATOM   981  C  CE  . LYS A 1 147 ? 3.806   26.254  15.489  1.00 53.09  ? 133 LYS A CE  1 
ATOM   982  N  NZ  . LYS A 1 147 ? 3.228   25.774  16.767  1.00 56.03  ? 133 LYS A NZ  1 
ATOM   983  N  N   . ASN A 1 148 ? 6.242   21.572  16.312  1.00 19.37  ? 134 ASN A N   1 
ATOM   984  C  CA  . ASN A 1 148 ? 5.771   20.856  17.496  1.00 20.08  ? 134 ASN A CA  1 
ATOM   985  C  C   . ASN A 1 148 ? 6.452   19.498  17.657  1.00 19.55  ? 134 ASN A C   1 
ATOM   986  O  O   . ASN A 1 148 ? 6.367   18.924  18.725  1.00 22.03  ? 134 ASN A O   1 
ATOM   987  C  CB  . ASN A 1 148 ? 4.246   20.689  17.452  1.00 20.39  ? 134 ASN A CB  1 
ATOM   988  C  CG  . ASN A 1 148 ? 3.491   22.001  17.424  1.00 19.19  ? 134 ASN A CG  1 
ATOM   989  O  OD1 . ASN A 1 148 ? 4.036   23.058  17.729  1.00 24.72  ? 134 ASN A OD1 1 
ATOM   990  N  ND2 . ASN A 1 148 ? 2.233   21.965  17.028  1.00 24.74  ? 134 ASN A ND2 1 
ATOM   991  N  N   . VAL A 1 149 ? 6.951   18.940  16.550  1.00 18.66  ? 135 VAL A N   1 
ATOM   992  C  CA  . VAL A 1 149 ? 7.400   17.566  16.494  1.00 15.49  ? 135 VAL A CA  1 
ATOM   993  C  C   . VAL A 1 149 ? 8.519   17.475  15.465  1.00 16.25  ? 135 VAL A C   1 
ATOM   994  O  O   . VAL A 1 149 ? 8.666   18.320  14.593  1.00 16.91  ? 135 VAL A O   1 
ATOM   995  C  CB  . VAL A 1 149 ? 6.258   16.615  16.069  1.00 18.08  ? 135 VAL A CB  1 
ATOM   996  C  CG1 . VAL A 1 149 ? 5.109   16.685  17.055  1.00 20.47  ? 135 VAL A CG1 1 
ATOM   997  C  CG2 . VAL A 1 149 ? 5.783   16.953  14.673  1.00 17.75  ? 135 VAL A CG2 1 
ATOM   998  N  N   . ASN A 1 150 ? 9.214   16.339  15.564  1.00 15.94  ? 136 ASN A N   1 
ATOM   999  C  CA  . ASN A 1 150 ? 10.109  15.851  14.524  1.00 16.02  ? 136 ASN A CA  1 
ATOM   1000 C  C   . ASN A 1 150 ? 9.509   14.564  13.977  1.00 14.05  ? 136 ASN A C   1 
ATOM   1001 O  O   . ASN A 1 150 ? 8.865   13.852  14.731  1.00 15.94  ? 136 ASN A O   1 
ATOM   1002 C  CB  . ASN A 1 150 ? 11.502  15.543  15.063  1.00 19.26  ? 136 ASN A CB  1 
ATOM   1003 C  CG  . ASN A 1 150 ? 12.197  16.762  15.603  1.00 22.74  ? 136 ASN A CG  1 
ATOM   1004 O  OD1 . ASN A 1 150 ? 12.065  17.845  15.032  1.00 22.72  ? 136 ASN A OD1 1 
ATOM   1005 N  ND2 . ASN A 1 150 ? 12.951  16.572  16.673  1.00 30.64  ? 136 ASN A ND2 1 
ATOM   1006 N  N   . VAL A 1 151 ? 9.766   14.305  12.695  1.00 13.73  ? 137 VAL A N   1 
ATOM   1007 C  CA  . VAL A 1 151 ? 9.280   13.087  12.053  1.00 12.52  ? 137 VAL A CA  1 
ATOM   1008 C  C   . VAL A 1 151 ? 10.470  12.341  11.454  1.00 13.18  ? 137 VAL A C   1 
ATOM   1009 O  O   . VAL A 1 151 ? 11.232  12.902  10.674  1.00 14.48  ? 137 VAL A O   1 
ATOM   1010 C  CB  . VAL A 1 151 ? 8.232   13.392  10.973  1.00 12.89  ? 137 VAL A CB  1 
ATOM   1011 C  CG1 . VAL A 1 151 ? 7.714   12.095  10.370  1.00 14.45  ? 137 VAL A CG1 1 
ATOM   1012 C  CG2 . VAL A 1 151 ? 7.112   14.274  11.464  1.00 14.91  ? 137 VAL A CG2 1 
ATOM   1013 N  N   . SER A 1 152 ? 10.605  11.065  11.834  1.00 13.25  ? 138 SER A N   1 
ATOM   1014 C  CA  . SER A 1 152 ? 11.663  10.205  11.344  1.00 12.90  ? 138 SER A CA  1 
ATOM   1015 C  C   . SER A 1 152 ? 10.998  8.988   10.675  1.00 13.17  ? 138 SER A C   1 
ATOM   1016 O  O   . SER A 1 152 ? 9.763   8.842   10.659  1.00 12.07  ? 138 SER A O   1 
ATOM   1017 C  CB  . SER A 1 152 ? 12.593  9.796   12.456  1.00 14.04  ? 138 SER A CB  1 
ATOM   1018 O  OG  . SER A 1 152 ? 12.005  8.945   13.421  1.00 15.97  ? 138 SER A OG  1 
ATOM   1019 N  N   . PHE A 1 153 ? 11.815  8.127   10.056  1.00 12.60  ? 139 PHE A N   1 
ATOM   1020 C  CA  . PHE A 1 153 ? 11.382  7.065   9.159   1.00 12.33  ? 139 PHE A CA  1 
ATOM   1021 C  C   . PHE A 1 153 ? 12.251  5.845   9.371   1.00 12.76  ? 139 PHE A C   1 
ATOM   1022 O  O   . PHE A 1 153 ? 13.387  5.936   9.852   1.00 14.89  ? 139 PHE A O   1 
ATOM   1023 C  CB  . PHE A 1 153 ? 11.490  7.493   7.689   1.00 13.62  ? 139 PHE A CB  1 
ATOM   1024 C  CG  . PHE A 1 153 ? 10.776  8.783   7.409   1.00 12.50  ? 139 PHE A CG  1 
ATOM   1025 C  CD1 . PHE A 1 153 ? 9.434   8.824   7.062   1.00 12.34  ? 139 PHE A CD1 1 
ATOM   1026 C  CD2 . PHE A 1 153 ? 11.432  9.998   7.508   1.00 13.11  ? 139 PHE A CD2 1 
ATOM   1027 C  CE1 . PHE A 1 153 ? 8.791   10.027  6.844   1.00 13.24  ? 139 PHE A CE1 1 
ATOM   1028 C  CE2 . PHE A 1 153 ? 10.758  11.204  7.374   1.00 13.58  ? 139 PHE A CE2 1 
ATOM   1029 C  CZ  . PHE A 1 153 ? 9.439   11.219  7.022   1.00 13.98  ? 139 PHE A CZ  1 
ATOM   1030 N  N   . PHE A 1 154 ? 11.719  4.670   9.080   1.00 12.12  ? 140 PHE A N   1 
ATOM   1031 C  CA  . PHE A 1 154 ? 12.469  3.432   9.211   1.00 11.46  ? 140 PHE A CA  1 
ATOM   1032 C  C   . PHE A 1 154 ? 12.037  2.526   8.063   1.00 11.53  ? 140 PHE A C   1 
ATOM   1033 O  O   . PHE A 1 154 ? 10.876  2.453   7.701   1.00 11.26  ? 140 PHE A O   1 
ATOM   1034 C  CB  . PHE A 1 154 ? 12.273  2.813   10.578  1.00 13.62  ? 140 PHE A CB  1 
ATOM   1035 C  CG  . PHE A 1 154 ? 10.850  2.553   10.981  1.00 12.99  ? 140 PHE A CG  1 
ATOM   1036 C  CD1 . PHE A 1 154 ? 10.121  3.553   11.617  1.00 12.53  ? 140 PHE A CD1 1 
ATOM   1037 C  CD2 . PHE A 1 154 ? 10.244  1.344   10.729  1.00 12.25  ? 140 PHE A CD2 1 
ATOM   1038 C  CE1 . PHE A 1 154 ? 8.808   3.344   11.993  1.00 13.59  ? 140 PHE A CE1 1 
ATOM   1039 C  CE2 . PHE A 1 154 ? 8.925   1.135   11.108  1.00 11.73  ? 140 PHE A CE2 1 
ATOM   1040 C  CZ  . PHE A 1 154 ? 8.240   2.112   11.800  1.00 12.68  ? 140 PHE A CZ  1 
ATOM   1041 N  N   . ASN A 1 155 ? 12.975  1.731   7.537   1.00 11.73  ? 141 ASN A N   1 
ATOM   1042 C  CA  . ASN A 1 155 ? 12.611  0.796   6.491   1.00 11.83  ? 141 ASN A CA  1 
ATOM   1043 C  C   . ASN A 1 155 ? 11.766  -0.356  7.029   1.00 12.03  ? 141 ASN A C   1 
ATOM   1044 O  O   . ASN A 1 155 ? 12.036  -0.927  8.085   1.00 12.40  ? 141 ASN A O   1 
ATOM   1045 C  CB  . ASN A 1 155 ? 13.828  0.164   5.815   1.00 13.89  ? 141 ASN A CB  1 
ATOM   1046 C  CG  . ASN A 1 155 ? 14.888  1.077   5.227   1.00 21.07  ? 141 ASN A CG  1 
ATOM   1047 O  OD1 . ASN A 1 155 ? 14.674  2.219   4.936   1.00 17.76  ? 141 ASN A OD1 1 
ATOM   1048 N  ND2 . ASN A 1 155 ? 16.100  0.587   5.062   1.00 28.95  ? 141 ASN A ND2 1 
ATOM   1049 N  N   . THR A 1 156 ? 10.768  -0.708  6.225   1.00 11.82  ? 142 THR A N   1 
ATOM   1050 C  CA  . THR A 1 156 ? 9.917   -1.863  6.425   1.00 12.02  ? 142 THR A CA  1 
ATOM   1051 C  C   . THR A 1 156 ? 10.045  -2.819  5.229   1.00 12.44  ? 142 THR A C   1 
ATOM   1052 O  O   . THR A 1 156 ? 10.514  -2.452  4.159   1.00 13.64  ? 142 THR A O   1 
ATOM   1053 C  CB  . THR A 1 156 ? 8.439   -1.433  6.596   1.00 11.98  ? 142 THR A CB  1 
ATOM   1054 O  OG1 . THR A 1 156 ? 8.099   -0.692  5.422   1.00 12.09  ? 142 THR A OG1 1 
ATOM   1055 C  CG2 . THR A 1 156 ? 8.234   -0.647  7.866   1.00 12.14  ? 142 THR A CG2 1 
ATOM   1056 N  N   . THR A 1 157 ? 9.579   -4.027  5.458   1.00 13.45  ? 143 THR A N   1 
ATOM   1057 C  CA  . THR A 1 157 ? 9.482   -5.049  4.421   1.00 13.36  ? 143 THR A CA  1 
ATOM   1058 C  C   . THR A 1 157 ? 8.050   -5.125  3.888   1.00 13.01  ? 143 THR A C   1 
ATOM   1059 O  O   . THR A 1 157 ? 7.124   -5.384  4.644   1.00 12.41  ? 143 THR A O   1 
ATOM   1060 C  CB  . THR A 1 157 ? 9.919   -6.421  4.957   1.00 14.21  ? 143 THR A CB  1 
ATOM   1061 O  OG1 . THR A 1 157 ? 11.251  -6.337  5.489   1.00 14.97  ? 143 THR A OG1 1 
ATOM   1062 C  CG2 . THR A 1 157 ? 9.869   -7.480  3.870   1.00 13.88  ? 143 THR A CG2 1 
ATOM   1063 N  N   . HIS A 1 158 ? 7.899   -4.993  2.571   1.00 13.84  ? 144 HIS A N   1 
ATOM   1064 C  CA  . HIS A 1 158 ? 6.611   -5.126  1.919   1.00 12.83  ? 144 HIS A CA  1 
ATOM   1065 C  C   . HIS A 1 158 ? 6.903   -5.691  0.523   1.00 14.76  ? 144 HIS A C   1 
ATOM   1066 O  O   . HIS A 1 158 ? 8.028   -6.042  0.202   1.00 18.12  ? 144 HIS A O   1 
ATOM   1067 C  CB  . HIS A 1 158 ? 5.857   -3.766  1.935   1.00 15.97  ? 144 HIS A CB  1 
ATOM   1068 C  CG  . HIS A 1 158 ? 4.380   -3.776  1.602   1.00 14.42  ? 144 HIS A CG  1 
ATOM   1069 N  ND1 . HIS A 1 158 ? 3.446   -4.670  2.065   1.00 16.48  ? 144 HIS A ND1 1 
ATOM   1070 C  CD2 . HIS A 1 158 ? 3.659   -2.947  0.755   1.00 22.73  ? 144 HIS A CD2 1 
ATOM   1071 C  CE1 . HIS A 1 158 ? 2.245   -4.367  1.524   1.00 21.70  ? 144 HIS A CE1 1 
ATOM   1072 N  NE2 . HIS A 1 158 ? 2.305   -3.218  0.787   1.00 20.20  ? 144 HIS A NE2 1 
ATOM   1073 N  N   . SER A 1 159 ? 5.922   -5.644  -0.373  1.00 14.86  ? 145 SER A N   1 
ATOM   1074 C  CA  . SER A 1 159 ? 6.040   -6.245  -1.696  1.00 16.39  ? 145 SER A CA  1 
ATOM   1075 C  C   . SER A 1 159 ? 6.609   -5.258  -2.708  1.00 14.82  ? 145 SER A C   1 
ATOM   1076 O  O   . SER A 1 159 ? 6.881   -5.623  -3.849  1.00 17.66  ? 145 SER A O   1 
ATOM   1077 C  CB  . SER A 1 159 ? 4.686   -6.718  -2.148  1.00 17.39  ? 145 SER A CB  1 
ATOM   1078 O  OG  . SER A 1 159 ? 3.707   -5.676  -2.037  1.00 24.79  ? 145 SER A OG  1 
ATOM   1079 N  N   . ILE A 1 160 ? 6.779   -4.008  -2.291  1.00 14.45  ? 146 ILE A N   1 
ATOM   1080 C  CA  . ILE A 1 160 ? 7.445   -2.965  -3.066  1.00 14.71  ? 146 ILE A CA  1 
ATOM   1081 C  C   . ILE A 1 160 ? 8.619   -2.500  -2.227  1.00 15.03  ? 146 ILE A C   1 
ATOM   1082 O  O   . ILE A 1 160 ? 8.517   -2.424  -0.989  1.00 16.25  ? 146 ILE A O   1 
ATOM   1083 C  CB  . ILE A 1 160 ? 6.480   -1.813  -3.488  1.00 15.86  ? 146 ILE A CB  1 
ATOM   1084 C  CG1 . ILE A 1 160 ? 6.999   -0.917  -4.620  1.00 16.67  ? 146 ILE A CG1 1 
ATOM   1085 C  CG2 . ILE A 1 160 ? 6.079   -0.990  -2.269  1.00 16.74  ? 146 ILE A CG2 1 
ATOM   1086 C  CD1 . ILE A 1 160 ? 6.000   0.080   -5.163  1.00 17.90  ? 146 ILE A CD1 1 
ATOM   1087 N  N   . PRO A 1 161 ? 9.802   -2.301  -2.852  1.00 17.38  ? 147 PRO A N   1 
ATOM   1088 C  CA  . PRO A 1 161 ? 10.952  -1.801  -2.110  1.00 18.98  ? 147 PRO A CA  1 
ATOM   1089 C  C   . PRO A 1 161 ? 10.776  -0.322  -1.743  1.00 12.79  ? 147 PRO A C   1 
ATOM   1090 O  O   . PRO A 1 161 ? 9.828   0.384   -2.099  1.00 17.92  ? 147 PRO A O   1 
ATOM   1091 C  CB  . PRO A 1 161 ? 12.126  -2.087  -3.059  1.00 21.18  ? 147 PRO A CB  1 
ATOM   1092 C  CG  . PRO A 1 161 ? 11.522  -2.005  -4.410  1.00 18.19  ? 147 PRO A CG  1 
ATOM   1093 C  CD  . PRO A 1 161 ? 10.107  -2.529  -4.275  1.00 16.94  ? 147 PRO A CD  1 
ATOM   1094 N  N   . ASP A 1 162 ? 11.656  0.067   -0.844  1.00 18.04  ? 148 ASP A N   1 
ATOM   1095 C  CA  . ASP A 1 162 ? 11.776  1.458   -0.377  1.00 18.89  ? 148 ASP A CA  1 
ATOM   1096 C  C   . ASP A 1 162 ? 10.515  1.861   0.392   1.00 17.22  ? 148 ASP A C   1 
ATOM   1097 O  O   . ASP A 1 162 ? 9.921   2.928   0.090   1.00 16.19  ? 148 ASP A O   1 
ATOM   1098 C  CB  . ASP A 1 162 ? 12.051  2.465   -1.521  1.00 24.68  ? 148 ASP A CB  1 
ATOM   1099 C  CG  . ASP A 1 162 ? 13.477  2.604   -2.019  1.00 65.11  ? 148 ASP A CG  1 
ATOM   1100 O  OD1 . ASP A 1 162 ? 14.350  1.752   -1.634  1.00 41.03  ? 148 ASP A OD1 1 
ATOM   1101 O  OD2 . ASP A 1 162 ? 13.722  3.630   -2.760  1.00 78.93  ? 148 ASP A OD2 1 
ATOM   1102 N  N   . SER A 1 163 ? 9.976   0.888   1.167   1.00 14.15  ? 149 SER A N   1 
ATOM   1103 C  CA  . SER A 1 163 ? 8.838   1.171   2.044   1.00 11.91  ? 149 SER A CA  1 
ATOM   1104 C  C   . SER A 1 163 ? 9.356   1.681   3.377   1.00 11.41  ? 149 SER A C   1 
ATOM   1105 O  O   . SER A 1 163 ? 10.382  1.219   3.898   1.00 12.01  ? 149 SER A O   1 
ATOM   1106 C  CB  . SER A 1 163 ? 7.897   0.015   2.167   1.00 13.09  ? 149 SER A CB  1 
ATOM   1107 O  OG  . SER A 1 163 ? 8.547   -1.121  2.634   1.00 14.81  ? 149 SER A OG  1 
ATOM   1108 N  N   . LEU A 1 164 ? 8.624   2.653   3.914   1.00 11.83  ? 150 LEU A N   1 
ATOM   1109 C  CA  . LEU A 1 164 ? 9.009   3.307   5.154   1.00 10.52  ? 150 LEU A CA  1 
ATOM   1110 C  C   . LEU A 1 164 ? 7.861   3.340   6.149   1.00 11.01  ? 150 LEU A C   1 
ATOM   1111 O  O   . LEU A 1 164 ? 6.734   3.541   5.765   1.00 13.06  ? 150 LEU A O   1 
ATOM   1112 C  CB  . LEU A 1 164 ? 9.436   4.739   4.894   1.00 10.68  ? 150 LEU A CB  1 
ATOM   1113 C  CG  . LEU A 1 164 ? 10.699  4.960   4.060   1.00 11.81  ? 150 LEU A CG  1 
ATOM   1114 C  CD1 . LEU A 1 164 ? 10.817  6.422   3.686   1.00 13.71  ? 150 LEU A CD1 1 
ATOM   1115 C  CD2 . LEU A 1 164 ? 11.941  4.480   4.828   1.00 11.83  ? 150 LEU A CD2 1 
ATOM   1116 N  N   . GLY A 1 165 ? 8.147   3.088   7.419   1.00 10.20  ? 151 GLY A N   1 
ATOM   1117 C  CA  . GLY A 1 165 ? 7.286   3.479   8.498   1.00 9.62   ? 151 GLY A CA  1 
ATOM   1118 C  C   . GLY A 1 165 ? 7.609   4.909   8.924   1.00 9.85   ? 151 GLY A C   1 
ATOM   1119 O  O   . GLY A 1 165 ? 8.675   5.453   8.616   1.00 11.28  ? 151 GLY A O   1 
ATOM   1120 N  N   . VAL A 1 166 ? 6.630   5.523   9.580   1.00 10.36  ? 152 VAL A N   1 
ATOM   1121 C  CA  . VAL A 1 166 ? 6.705   6.915   9.976   1.00 10.48  ? 152 VAL A CA  1 
ATOM   1122 C  C   . VAL A 1 166 ? 6.669   6.986   11.496  1.00 11.37  ? 152 VAL A C   1 
ATOM   1123 O  O   . VAL A 1 166 ? 5.826   6.349   12.141  1.00 12.73  ? 152 VAL A O   1 
ATOM   1124 C  CB  . VAL A 1 166 ? 5.554   7.723   9.373   1.00 10.54  ? 152 VAL A CB  1 
ATOM   1125 C  CG1 . VAL A 1 166 ? 5.676   9.187   9.758   1.00 13.17  ? 152 VAL A CG1 1 
ATOM   1126 C  CG2 . VAL A 1 166 ? 5.507   7.553   7.862   1.00 12.08  ? 152 VAL A CG2 1 
ATOM   1127 N  N   . CYS A 1 167 ? 7.545   7.832   12.085  1.00 12.09  ? 153 CYS A N   1 
ATOM   1128 C  CA  . CYS A 1 167 ? 7.648   7.961   13.538  1.00 12.50  ? 153 CYS A CA  1 
ATOM   1129 C  C   . CYS A 1 167 ? 7.540   9.444   13.868  1.00 13.74  ? 153 CYS A C   1 
ATOM   1130 O  O   . CYS A 1 167 ? 8.455   10.204  13.538  1.00 13.57  ? 153 CYS A O   1 
ATOM   1131 C  CB  . CYS A 1 167 ? 8.985   7.395   14.024  1.00 14.46  ? 153 CYS A CB  1 
ATOM   1132 S  SG  . CYS A 1 167 ? 9.207   7.442   15.815  1.00 16.35  ? 153 CYS A SG  1 
ATOM   1133 N  N   . ILE A 1 168 ? 6.406   9.863   14.446  1.00 11.79  ? 154 ILE A N   1 
ATOM   1134 C  CA  . ILE A 1 168 ? 6.209   11.247  14.866  1.00 13.53  ? 154 ILE A CA  1 
ATOM   1135 C  C   . ILE A 1 168 ? 6.608   11.348  16.334  1.00 12.31  ? 154 ILE A C   1 
ATOM   1136 O  O   . ILE A 1 168 ? 6.004   10.749  17.200  1.00 13.51  ? 154 ILE A O   1 
ATOM   1137 C  CB  . ILE A 1 168 ? 4.751   11.702  14.657  1.00 11.33  ? 154 ILE A CB  1 
ATOM   1138 C  CG1 . ILE A 1 168 ? 4.383   11.545  13.190  1.00 12.87  ? 154 ILE A CG1 1 
ATOM   1139 C  CG2 . ILE A 1 168 ? 4.597   13.134  15.135  1.00 14.63  ? 154 ILE A CG2 1 
ATOM   1140 C  CD1 . ILE A 1 168 ? 2.920   11.752  12.901  1.00 13.97  ? 154 ILE A CD1 1 
ATOM   1141 N  N   . HIS A 1 169 ? 7.636   12.137  16.618  1.00 13.77  ? 155 HIS A N   1 
ATOM   1142 C  CA  . HIS A 1 169 ? 8.152   12.239  17.971  1.00 13.35  ? 155 HIS A CA  1 
ATOM   1143 C  C   . HIS A 1 169 ? 7.438   13.350  18.738  1.00 13.82  ? 155 HIS A C   1 
ATOM   1144 O  O   . HIS A 1 169 ? 7.404   14.471  18.267  1.00 17.07  ? 155 HIS A O   1 
ATOM   1145 C  CB  . HIS A 1 169 ? 9.648   12.529  17.946  1.00 15.55  ? 155 HIS A CB  1 
ATOM   1146 C  CG  . HIS A 1 169 ? 10.464  11.498  17.233  1.00 15.76  ? 155 HIS A CG  1 
ATOM   1147 N  ND1 . HIS A 1 169 ? 11.080  10.457  17.895  1.00 21.00  ? 155 HIS A ND1 1 
ATOM   1148 C  CD2 . HIS A 1 169 ? 10.703  11.304  15.896  1.00 17.74  ? 155 HIS A CD2 1 
ATOM   1149 C  CE1 . HIS A 1 169 ? 11.743  9.703   17.010  1.00 19.72  ? 155 HIS A CE1 1 
ATOM   1150 N  NE2 . HIS A 1 169 ? 11.474  10.179  15.754  1.00 17.63  ? 155 HIS A NE2 1 
ATOM   1151 N  N   . THR A 1 170 ? 6.820   13.019  19.868  1.00 13.92  ? 156 THR A N   1 
ATOM   1152 C  CA  . THR A 1 170 ? 6.109   13.954  20.719  1.00 15.67  ? 156 THR A CA  1 
ATOM   1153 C  C   . THR A 1 170 ? 6.683   13.856  22.130  1.00 16.31  ? 156 THR A C   1 
ATOM   1154 O  O   . THR A 1 170 ? 7.369   12.893  22.484  1.00 16.39  ? 156 THR A O   1 
ATOM   1155 C  CB  . THR A 1 170 ? 4.596   13.709  20.760  1.00 15.40  ? 156 THR A CB  1 
ATOM   1156 O  OG1 . THR A 1 170 ? 4.228   12.752  21.755  1.00 15.61  ? 156 THR A OG1 1 
ATOM   1157 C  CG2 . THR A 1 170 ? 4.018   13.315  19.423  1.00 14.90  ? 156 THR A CG2 1 
ATOM   1158 N  N   . SER A 1 171 ? 6.285   14.820  22.964  1.00 17.71  ? 157 SER A N   1 
ATOM   1159 C  CA  . SER A 1 171 ? 6.789   14.821  24.325  1.00 17.32  ? 157 SER A CA  1 
ATOM   1160 C  C   . SER A 1 171 ? 6.107   13.723  25.152  1.00 17.81  ? 157 SER A C   1 
ATOM   1161 O  O   . SER A 1 171 ? 6.533   13.472  26.268  1.00 19.80  ? 157 SER A O   1 
ATOM   1162 C  CB  . SER A 1 171 ? 6.700   16.190  24.963  1.00 22.06  ? 157 SER A CB  1 
ATOM   1163 O  OG  . SER A 1 171 ? 5.388   16.665  24.961  1.00 24.07  ? 157 SER A OG  1 
ATOM   1164 N  N   . TYR A 1 172 ? 5.072   13.039  24.610  1.00 16.14  ? 158 TYR A N   1 
ATOM   1165 C  CA  . TYR A 1 172 ? 4.447   11.912  25.268  1.00 15.39  ? 158 TYR A CA  1 
ATOM   1166 C  C   . TYR A 1 172 ? 5.088   10.583  24.864  1.00 16.61  ? 158 TYR A C   1 
ATOM   1167 O  O   . TYR A 1 172 ? 4.646   9.538   25.318  1.00 18.18  ? 158 TYR A O   1 
ATOM   1168 C  CB  . TYR A 1 172 ? 2.956   11.883  24.959  1.00 16.31  ? 158 TYR A CB  1 
ATOM   1169 C  CG  . TYR A 1 172 ? 2.153   13.061  25.441  1.00 16.21  ? 158 TYR A CG  1 
ATOM   1170 C  CD1 . TYR A 1 172 ? 2.168   13.441  26.782  1.00 16.69  ? 158 TYR A CD1 1 
ATOM   1171 C  CD2 . TYR A 1 172 ? 1.419   13.836  24.565  1.00 18.07  ? 158 TYR A CD2 1 
ATOM   1172 C  CE1 . TYR A 1 172 ? 1.386   14.482  27.227  1.00 16.74  ? 158 TYR A CE1 1 
ATOM   1173 C  CE2 . TYR A 1 172 ? 0.621   14.883  25.009  1.00 17.59  ? 158 TYR A CE2 1 
ATOM   1174 C  CZ  . TYR A 1 172 ? 0.632   15.234  26.346  1.00 17.13  ? 158 TYR A CZ  1 
ATOM   1175 O  OH  . TYR A 1 172 ? -0.181  16.214  26.858  1.00 17.57  ? 158 TYR A OH  1 
ATOM   1176 N  N   . GLY A 1 173 ? 6.002   10.632  23.873  1.00 16.30  ? 159 GLY A N   1 
ATOM   1177 C  CA  . GLY A 1 173 ? 6.498   9.451   23.184  1.00 15.73  ? 159 GLY A CA  1 
ATOM   1178 C  C   . GLY A 1 173 ? 6.116   9.485   21.709  1.00 14.55  ? 159 GLY A C   1 
ATOM   1179 O  O   . GLY A 1 173 ? 5.404   10.370  21.235  1.00 16.42  ? 159 GLY A O   1 
ATOM   1180 N  N   . SER A 1 174 ? 6.521   8.467   20.978  1.00 14.81  ? 160 SER A N   1 
ATOM   1181 C  CA  A SER A 1 174 ? 6.364   8.439   19.532  0.50 13.82  ? 160 SER A CA  1 
ATOM   1182 C  CA  B SER A 1 174 ? 6.331   8.534   19.537  0.50 13.69  ? 160 SER A CA  1 
ATOM   1183 C  C   . SER A 1 174 ? 4.966   7.974   19.147  1.00 11.27  ? 160 SER A C   1 
ATOM   1184 O  O   . SER A 1 174 ? 4.426   7.093   19.783  1.00 13.51  ? 160 SER A O   1 
ATOM   1185 C  CB  A SER A 1 174 ? 7.427   7.541   18.925  0.50 13.65  ? 160 SER A CB  1 
ATOM   1186 C  CB  B SER A 1 174 ? 7.466   7.862   18.806  0.50 14.60  ? 160 SER A CB  1 
ATOM   1187 O  OG  A SER A 1 174 ? 8.705   8.127   19.102  0.50 16.18  ? 160 SER A OG  1 
ATOM   1188 O  OG  B SER A 1 174 ? 7.538   6.508   19.184  0.50 13.14  ? 160 SER A OG  1 
ATOM   1189 N  N   . ILE A 1 175 ? 4.502   8.479   18.010  1.00 11.06  ? 161 ILE A N   1 
ATOM   1190 C  CA  . ILE A 1 175 ? 3.359   7.951   17.295  1.00 11.02  ? 161 ILE A CA  1 
ATOM   1191 C  C   . ILE A 1 175 ? 3.917   7.287   16.056  1.00 10.89  ? 161 ILE A C   1 
ATOM   1192 O  O   . ILE A 1 175 ? 4.481   7.959   15.198  1.00 11.73  ? 161 ILE A O   1 
ATOM   1193 C  CB  . ILE A 1 175 ? 2.369   9.068   16.952  1.00 11.98  ? 161 ILE A CB  1 
ATOM   1194 C  CG1 . ILE A 1 175 ? 1.896   9.793   18.210  1.00 13.18  ? 161 ILE A CG1 1 
ATOM   1195 C  CG2 . ILE A 1 175 ? 1.179   8.539   16.163  1.00 12.40  ? 161 ILE A CG2 1 
ATOM   1196 C  CD1 . ILE A 1 175 ? 1.179   11.109  17.915  1.00 15.14  ? 161 ILE A CD1 1 
ATOM   1197 N  N   . VAL A 1 176 ? 3.770   5.947   15.997  1.00 10.67  ? 162 VAL A N   1 
ATOM   1198 C  CA  . VAL A 1 176 ? 4.366   5.157   14.936  1.00 12.30  ? 162 VAL A CA  1 
ATOM   1199 C  C   . VAL A 1 176 ? 3.286   4.621   14.025  1.00 9.85   ? 162 VAL A C   1 
ATOM   1200 O  O   . VAL A 1 176 ? 2.356   3.965   14.507  1.00 11.31  ? 162 VAL A O   1 
ATOM   1201 C  CB  . VAL A 1 176 ? 5.196   4.011   15.548  1.00 11.35  ? 162 VAL A CB  1 
ATOM   1202 C  CG1 . VAL A 1 176 ? 5.701   3.037   14.490  1.00 12.55  ? 162 VAL A CG1 1 
ATOM   1203 C  CG2 . VAL A 1 176 ? 6.354   4.567   16.360  1.00 13.21  ? 162 VAL A CG2 1 
ATOM   1204 N  N   . TYR A 1 177 ? 3.463   4.872   12.741  1.00 9.66   ? 163 TYR A N   1 
ATOM   1205 C  CA  . TYR A 1 177 ? 2.608   4.303   11.718  1.00 10.13  ? 163 TYR A CA  1 
ATOM   1206 C  C   . TYR A 1 177 ? 3.420   3.346   10.867  1.00 9.28   ? 163 TYR A C   1 
ATOM   1207 O  O   . TYR A 1 177 ? 4.406   3.727   10.269  1.00 10.77  ? 163 TYR A O   1 
ATOM   1208 C  CB  . TYR A 1 177 ? 1.997   5.422   10.880  1.00 10.61  ? 163 TYR A CB  1 
ATOM   1209 C  CG  . TYR A 1 177 ? 1.257   4.929   9.668   1.00 9.28   ? 163 TYR A CG  1 
ATOM   1210 C  CD1 . TYR A 1 177 ? 0.281   3.929   9.740   1.00 11.09  ? 163 TYR A CD1 1 
ATOM   1211 C  CD2 . TYR A 1 177 ? 1.472   5.449   8.400   1.00 10.31  ? 163 TYR A CD2 1 
ATOM   1212 C  CE1 . TYR A 1 177 ? -0.423  3.473   8.611   1.00 11.34  ? 163 TYR A CE1 1 
ATOM   1213 C  CE2 . TYR A 1 177 ? 0.777   5.044   7.290   1.00 10.65  ? 163 TYR A CE2 1 
ATOM   1214 C  CZ  . TYR A 1 177 ? -0.172  4.055   7.372   1.00 10.51  ? 163 TYR A CZ  1 
ATOM   1215 O  OH  . TYR A 1 177 ? -0.847  3.655   6.306   1.00 12.50  ? 163 TYR A OH  1 
ATOM   1216 N  N   . THR A 1 178 ? 3.005   2.074   10.843  1.00 10.28  ? 164 THR A N   1 
ATOM   1217 C  CA  . THR A 1 178 ? 3.774   1.051   10.189  1.00 11.21  ? 164 THR A CA  1 
ATOM   1218 C  C   . THR A 1 178 ? 3.688   1.061   8.684   1.00 11.43  ? 164 THR A C   1 
ATOM   1219 O  O   . THR A 1 178 ? 4.543   0.482   8.017   1.00 11.95  ? 164 THR A O   1 
ATOM   1220 C  CB  . THR A 1 178 ? 3.332   -0.351  10.631  1.00 11.41  ? 164 THR A CB  1 
ATOM   1221 O  OG1 . THR A 1 178 ? 1.945   -0.565  10.288  1.00 10.87  ? 164 THR A OG1 1 
ATOM   1222 C  CG2 . THR A 1 178 ? 3.472   -0.544  12.119  1.00 12.25  ? 164 THR A CG2 1 
ATOM   1223 N  N   . GLY A 1 179 ? 2.647   1.667   8.132   1.00 10.51  ? 165 GLY A N   1 
ATOM   1224 C  CA  . GLY A 1 179 ? 2.220   1.368   6.787   1.00 12.40  ? 165 GLY A CA  1 
ATOM   1225 C  C   . GLY A 1 179 ? 1.958   -0.122  6.632   1.00 11.71  ? 165 GLY A C   1 
ATOM   1226 O  O   . GLY A 1 179 ? 1.570   -0.787  7.581   1.00 13.48  ? 165 GLY A O   1 
ATOM   1227 N  N   . GLU A 1 180 ? 1.991   -0.626  5.424   1.00 11.14  ? 166 GLU A N   1 
ATOM   1228 C  CA  . GLU A 1 180 ? 1.792   -2.045  5.182   1.00 11.49  ? 166 GLU A CA  1 
ATOM   1229 C  C   . GLU A 1 180 ? 3.124   -2.774  5.240   1.00 10.70  ? 166 GLU A C   1 
ATOM   1230 O  O   . GLU A 1 180 ? 4.114   -2.336  4.657   1.00 12.19  ? 166 GLU A O   1 
ATOM   1231 C  CB  . GLU A 1 180 ? 1.107   -2.218  3.843   1.00 13.21  ? 166 GLU A CB  1 
ATOM   1232 C  CG  . GLU A 1 180 ? -0.221  -1.501  3.870   1.00 18.65  ? 166 GLU A CG  1 
ATOM   1233 C  CD  . GLU A 1 180 ? -1.010  -1.481  2.601   0.67 15.27  ? 166 GLU A CD  1 
ATOM   1234 O  OE1 . GLU A 1 180 ? -0.458  -1.825  1.479   0.89 17.50  ? 166 GLU A OE1 1 
ATOM   1235 O  OE2 . GLU A 1 180 ? -2.273  -1.250  2.813   1.00 18.35  ? 166 GLU A OE2 1 
ATOM   1236 N  N   . PHE A 1 181 ? 3.174   -3.867  5.988   1.00 11.21  ? 167 PHE A N   1 
ATOM   1237 C  CA  . PHE A 1 181 ? 4.431   -4.526  6.233   1.00 10.58  ? 167 PHE A CA  1 
ATOM   1238 C  C   . PHE A 1 181 ? 4.218   -5.983  6.571   1.00 11.07  ? 167 PHE A C   1 
ATOM   1239 O  O   . PHE A 1 181 ? 3.117   -6.388  6.955   1.00 11.90  ? 167 PHE A O   1 
ATOM   1240 C  CB  . PHE A 1 181 ? 5.183   -3.902  7.434   1.00 11.88  ? 167 PHE A CB  1 
ATOM   1241 C  CG  . PHE A 1 181 ? 4.630   -4.260  8.799   1.00 10.17  ? 167 PHE A CG  1 
ATOM   1242 C  CD1 . PHE A 1 181 ? 3.543   -3.579  9.266   1.00 10.64  ? 167 PHE A CD1 1 
ATOM   1243 C  CD2 . PHE A 1 181 ? 5.112   -5.334  9.540   1.00 11.88  ? 167 PHE A CD2 1 
ATOM   1244 C  CE1 . PHE A 1 181 ? 2.990   -3.911  10.469  1.00 11.03  ? 167 PHE A CE1 1 
ATOM   1245 C  CE2 . PHE A 1 181 ? 4.541   -5.678  10.756  1.00 12.03  ? 167 PHE A CE2 1 
ATOM   1246 C  CZ  . PHE A 1 181 ? 3.450   -4.982  11.198  1.00 11.74  ? 167 PHE A CZ  1 
ATOM   1247 N  N   . LYS A 1 182 ? 5.322   -6.709  6.431   1.00 11.82  ? 168 LYS A N   1 
ATOM   1248 C  CA  . LYS A 1 182 ? 5.444   -8.088  6.892   1.00 12.27  ? 168 LYS A CA  1 
ATOM   1249 C  C   . LYS A 1 182 ? 6.881   -8.257  7.338   1.00 12.57  ? 168 LYS A C   1 
ATOM   1250 O  O   . LYS A 1 182 ? 7.671   -7.336  7.330   1.00 13.18  ? 168 LYS A O   1 
ATOM   1251 C  CB  . LYS A 1 182 ? 5.031   -9.072  5.809   1.00 14.56  ? 168 LYS A CB  1 
ATOM   1252 C  CG  . LYS A 1 182 ? 5.924   -9.166  4.603   1.00 16.05  ? 168 LYS A CG  1 
ATOM   1253 C  CD  . LYS A 1 182 ? 5.448   -10.368 3.797   1.00 19.22  ? 168 LYS A CD  1 
ATOM   1254 C  CE  . LYS A 1 182 ? 6.080   -10.506 2.438   1.00 20.00  ? 168 LYS A CE  1 
ATOM   1255 N  NZ  . LYS A 1 182 ? 5.471   -11.670 1.736   1.00 19.12  ? 168 LYS A NZ  1 
ATOM   1256 N  N   . PHE A 1 183 ? 7.218   -9.472  7.792   1.00 13.37  ? 169 PHE A N   1 
ATOM   1257 C  CA  . PHE A 1 183 ? 8.603   -9.788  8.096   1.00 12.49  ? 169 PHE A CA  1 
ATOM   1258 C  C   . PHE A 1 183 ? 8.934   -11.102 7.393   1.00 14.92  ? 169 PHE A C   1 
ATOM   1259 O  O   . PHE A 1 183 ? 8.219   -12.086 7.565   1.00 17.70  ? 169 PHE A O   1 
ATOM   1260 C  CB  . PHE A 1 183 ? 8.879   -9.926  9.592   1.00 13.98  ? 169 PHE A CB  1 
ATOM   1261 C  CG  . PHE A 1 183 ? 8.848   -8.621  10.358  1.00 13.13  ? 169 PHE A CG  1 
ATOM   1262 C  CD1 . PHE A 1 183 ? 9.799   -7.649  10.130  1.00 13.97  ? 169 PHE A CD1 1 
ATOM   1263 C  CD2 . PHE A 1 183 ? 7.840   -8.338  11.267  1.00 14.65  ? 169 PHE A CD2 1 
ATOM   1264 C  CE1 . PHE A 1 183 ? 9.783   -6.447  10.818  1.00 14.73  ? 169 PHE A CE1 1 
ATOM   1265 C  CE2 . PHE A 1 183 ? 7.829   -7.144  11.975  1.00 15.51  ? 169 PHE A CE2 1 
ATOM   1266 C  CZ  . PHE A 1 183 ? 8.812   -6.205  11.768  1.00 15.70  ? 169 PHE A CZ  1 
ATOM   1267 N  N   . ASP A 1 184 ? 10.027  -11.100 6.626   1.00 15.47  ? 170 ASP A N   1 
ATOM   1268 C  CA  . ASP A 1 184 ? 10.435  -12.271 5.860   1.00 15.45  ? 170 ASP A CA  1 
ATOM   1269 C  C   . ASP A 1 184 ? 11.934  -12.178 5.579   1.00 17.14  ? 170 ASP A C   1 
ATOM   1270 O  O   . ASP A 1 184 ? 12.374  -11.347 4.797   1.00 17.88  ? 170 ASP A O   1 
ATOM   1271 C  CB  . ASP A 1 184 ? 9.669   -12.279 4.545   1.00 16.61  ? 170 ASP A CB  1 
ATOM   1272 C  CG  . ASP A 1 184 ? 10.006  -13.419 3.599   1.00 18.33  ? 170 ASP A CG  1 
ATOM   1273 O  OD1 . ASP A 1 184 ? 11.033  -14.169 3.835   1.00 21.46  ? 170 ASP A OD1 1 
ATOM   1274 O  OD2 . ASP A 1 184 ? 9.292   -13.561 2.599   1.00 18.46  ? 170 ASP A OD2 1 
ATOM   1275 N  N   . GLN A 1 185 ? 12.717  -13.043 6.240   1.00 15.85  ? 171 GLN A N   1 
ATOM   1276 C  CA  . GLN A 1 185 ? 14.171  -12.997 6.169   1.00 17.25  ? 171 GLN A CA  1 
ATOM   1277 C  C   . GLN A 1 185 ? 14.704  -13.382 4.784   1.00 19.74  ? 171 GLN A C   1 
ATOM   1278 O  O   . GLN A 1 185 ? 15.901  -13.241 4.540   1.00 24.95  ? 171 GLN A O   1 
ATOM   1279 C  CB  . GLN A 1 185 ? 14.737  -13.923 7.253   1.00 18.52  ? 171 GLN A CB  1 
ATOM   1280 C  CG  . GLN A 1 185 ? 14.532  -13.346 8.649   1.00 24.32  ? 171 GLN A CG  1 
ATOM   1281 C  CD  . GLN A 1 185 ? 15.018  -14.229 9.772   1.00 21.76  ? 171 GLN A CD  1 
ATOM   1282 O  OE1 . GLN A 1 185 ? 14.232  -14.687 10.624  1.00 24.92  ? 171 GLN A OE1 1 
ATOM   1283 N  NE2 . GLN A 1 185 ? 16.325  -14.446 9.792   1.00 23.31  ? 171 GLN A NE2 1 
ATOM   1284 N  N   . SER A 1 186 ? 13.867  -13.892 3.885   1.00 18.56  ? 172 SER A N   1 
ATOM   1285 C  CA  . SER A 1 186 ? 14.331  -14.191 2.546   1.00 20.84  ? 172 SER A CA  1 
ATOM   1286 C  C   . SER A 1 186 ? 14.296  -12.971 1.616   1.00 20.69  ? 172 SER A C   1 
ATOM   1287 O  O   . SER A 1 186 ? 14.736  -13.083 0.467   1.00 29.44  ? 172 SER A O   1 
ATOM   1288 C  CB  . SER A 1 186 ? 13.547  -15.344 2.006   1.00 21.94  ? 172 SER A CB  1 
ATOM   1289 O  OG  . SER A 1 186 ? 12.261  -14.960 1.524   1.00 22.18  ? 172 SER A OG  1 
ATOM   1290 N  N   . LEU A 1 187 ? 13.759  -11.828 2.060   1.00 21.58  ? 173 LEU A N   1 
ATOM   1291 C  CA  . LEU A 1 187 ? 13.804  -10.592 1.284   1.00 22.45  ? 173 LEU A CA  1 
ATOM   1292 C  C   . LEU A 1 187 ? 14.956  -9.721  1.784   1.00 22.32  ? 173 LEU A C   1 
ATOM   1293 O  O   . LEU A 1 187 ? 15.113  -9.569  2.994   1.00 27.76  ? 173 LEU A O   1 
ATOM   1294 C  CB  . LEU A 1 187 ? 12.453  -9.878  1.453   1.00 19.53  ? 173 LEU A CB  1 
ATOM   1295 C  CG  . LEU A 1 187 ? 11.277  -10.542 0.731   1.00 18.10  ? 173 LEU A CG  1 
ATOM   1296 C  CD1 . LEU A 1 187 ? 9.959   -9.831  1.001   1.00 19.62  ? 173 LEU A CD1 1 
ATOM   1297 C  CD2 . LEU A 1 187 ? 11.546  -10.596 -0.760  1.00 21.53  ? 173 LEU A CD2 1 
ATOM   1298 N  N   . HIS A 1 188 ? 15.739  -9.126  0.863   1.00 25.34  ? 174 HIS A N   1 
ATOM   1299 C  CA  . HIS A 1 188 ? 16.960  -8.403  1.211   1.00 26.57  ? 174 HIS A CA  1 
ATOM   1300 C  C   . HIS A 1 188 ? 17.010  -7.058  0.487   1.00 25.59  ? 174 HIS A C   1 
ATOM   1301 O  O   . HIS A 1 188 ? 16.061  -6.642  -0.184  1.00 23.50  ? 174 HIS A O   1 
ATOM   1302 C  CB  . HIS A 1 188 ? 18.209  -9.237  0.841   1.00 38.69  ? 174 HIS A CB  1 
ATOM   1303 C  CG  . HIS A 1 188 ? 18.179  -10.675 1.271   1.00 36.41  ? 174 HIS A CG  1 
ATOM   1304 N  ND1 . HIS A 1 188 ? 18.029  -11.736 0.403   1.00 42.04  ? 174 HIS A ND1 1 
ATOM   1305 C  CD2 . HIS A 1 188 ? 18.229  -11.197 2.533   1.00 49.25  ? 174 HIS A CD2 1 
ATOM   1306 C  CE1 . HIS A 1 188 ? 18.002  -12.871 1.101   1.00 48.59  ? 174 HIS A CE1 1 
ATOM   1307 N  NE2 . HIS A 1 188 ? 18.116  -12.557 2.426   1.00 40.89  ? 174 HIS A NE2 1 
ATOM   1308 N  N   . GLY A 1 189 ? 18.155  -6.363  0.584   1.00 29.13  ? 175 GLY A N   1 
ATOM   1309 C  CA  . GLY A 1 189 ? 18.362  -5.129  -0.155  1.00 28.21  ? 175 GLY A CA  1 
ATOM   1310 C  C   . GLY A 1 189 ? 17.339  -4.074  0.233   1.00 22.02  ? 175 GLY A C   1 
ATOM   1311 O  O   . GLY A 1 189 ? 17.205  -3.722  1.409   1.00 26.02  ? 175 GLY A O   1 
ATOM   1312 N  N   . HIS A 1 190 ? 16.622  -3.546  -0.763  1.00 22.35  ? 176 HIS A N   1 
ATOM   1313 C  CA  . HIS A 1 190 ? 15.728  -2.432  -0.530  1.00 23.42  ? 176 HIS A CA  1 
ATOM   1314 C  C   . HIS A 1 190 ? 14.425  -2.942  0.102   1.00 18.50  ? 176 HIS A C   1 
ATOM   1315 O  O   . HIS A 1 190 ? 13.497  -2.138  0.241   1.00 21.46  ? 176 HIS A O   1 
ATOM   1316 C  CB  . HIS A 1 190 ? 15.519  -1.645  -1.829  1.00 21.83  ? 176 HIS A CB  1 
ATOM   1317 C  CG  . HIS A 1 190 ? 16.709  -0.850  -2.284  1.00 35.64  ? 176 HIS A CG  1 
ATOM   1318 N  ND1 . HIS A 1 190 ? 17.927  -1.409  -2.601  1.00 48.40  ? 176 HIS A ND1 1 
ATOM   1319 C  CD2 . HIS A 1 190 ? 16.838  0.499   -2.454  1.00 47.35  ? 176 HIS A CD2 1 
ATOM   1320 C  CE1 . HIS A 1 190 ? 18.775  -0.450  -2.988  1.00 53.03  ? 176 HIS A CE1 1 
ATOM   1321 N  NE2 . HIS A 1 190 ? 18.114  0.751   -2.873  1.00 70.27  ? 176 HIS A NE2 1 
ATOM   1322 N  N   . TYR A 1 191 ? 14.366  -4.260  0.396   1.00 17.19  ? 177 TYR A N   1 
ATOM   1323 C  CA  . TYR A 1 191 ? 13.233  -4.844  1.135   1.00 16.75  ? 177 TYR A CA  1 
ATOM   1324 C  C   . TYR A 1 191 ? 13.551  -5.121  2.610   1.00 17.20  ? 177 TYR A C   1 
ATOM   1325 O  O   . TYR A 1 191 ? 12.669  -5.502  3.370   1.00 17.53  ? 177 TYR A O   1 
ATOM   1326 C  CB  . TYR A 1 191 ? 12.794  -6.195  0.555   1.00 18.68  ? 177 TYR A CB  1 
ATOM   1327 C  CG  . TYR A 1 191 ? 12.280  -6.121  -0.863  1.00 17.77  ? 177 TYR A CG  1 
ATOM   1328 C  CD1 . TYR A 1 191 ? 10.981  -5.721  -1.098  1.00 16.53  ? 177 TYR A CD1 1 
ATOM   1329 C  CD2 . TYR A 1 191 ? 13.079  -6.414  -1.956  1.00 20.72  ? 177 TYR A CD2 1 
ATOM   1330 C  CE1 . TYR A 1 191 ? 10.491  -5.623  -2.389  1.00 18.97  ? 177 TYR A CE1 1 
ATOM   1331 C  CE2 . TYR A 1 191 ? 12.604  -6.326  -3.256  1.00 23.06  ? 177 TYR A CE2 1 
ATOM   1332 C  CZ  . TYR A 1 191 ? 11.299  -5.913  -3.478  1.00 24.39  ? 177 TYR A CZ  1 
ATOM   1333 O  OH  . TYR A 1 191 ? 10.780  -5.848  -4.774  1.00 29.18  ? 177 TYR A OH  1 
ATOM   1334 N  N   . ALA A 1 192 ? 14.819  -4.983  3.023   1.00 18.40  ? 178 ALA A N   1 
ATOM   1335 C  CA  . ALA A 1 192 ? 15.237  -5.362  4.371   1.00 18.16  ? 178 ALA A CA  1 
ATOM   1336 C  C   . ALA A 1 192 ? 14.694  -4.386  5.412   1.00 15.45  ? 178 ALA A C   1 
ATOM   1337 O  O   . ALA A 1 192 ? 14.640  -3.179  5.179   1.00 18.66  ? 178 ALA A O   1 
ATOM   1338 C  CB  . ALA A 1 192 ? 16.750  -5.418  4.492   1.00 22.67  ? 178 ALA A CB  1 
ATOM   1339 N  N   . PRO A 1 193 ? 14.215  -4.888  6.571   1.00 14.94  ? 179 PRO A N   1 
ATOM   1340 C  CA  . PRO A 1 193 ? 13.608  -4.017  7.582   1.00 15.10  ? 179 PRO A CA  1 
ATOM   1341 C  C   . PRO A 1 193 ? 14.682  -3.456  8.502   1.00 15.49  ? 179 PRO A C   1 
ATOM   1342 O  O   . PRO A 1 193 ? 15.739  -4.074  8.692   1.00 17.79  ? 179 PRO A O   1 
ATOM   1343 C  CB  . PRO A 1 193 ? 12.681  -4.970  8.346   1.00 16.07  ? 179 PRO A CB  1 
ATOM   1344 C  CG  . PRO A 1 193 ? 13.421  -6.288  8.311   1.00 16.49  ? 179 PRO A CG  1 
ATOM   1345 C  CD  . PRO A 1 193 ? 14.114  -6.305  6.957   1.00 16.73  ? 179 PRO A CD  1 
ATOM   1346 N  N   . ASP A 1 194 ? 14.445  -2.268  9.047   1.00 14.93  ? 180 ASP A N   1 
ATOM   1347 C  CA  . ASP A 1 194 ? 15.344  -1.630  10.009  1.00 13.80  ? 180 ASP A CA  1 
ATOM   1348 C  C   . ASP A 1 194 ? 15.037  -2.124  11.415  1.00 14.93  ? 180 ASP A C   1 
ATOM   1349 O  O   . ASP A 1 194 ? 14.526  -1.373  12.217  1.00 16.20  ? 180 ASP A O   1 
ATOM   1350 C  CB  . ASP A 1 194 ? 15.218  -0.116  9.874   1.00 14.66  ? 180 ASP A CB  1 
ATOM   1351 C  CG  . ASP A 1 194 ? 15.981  0.437   8.695   1.00 16.92  ? 180 ASP A CG  1 
ATOM   1352 O  OD1 . ASP A 1 194 ? 16.898  -0.266  8.158   1.00 20.81  ? 180 ASP A OD1 1 
ATOM   1353 O  OD2 . ASP A 1 194 ? 15.703  1.598   8.355   1.00 16.78  ? 180 ASP A OD2 1 
ATOM   1354 N  N   . LEU A 1 195 ? 15.412  -3.371  11.736  1.00 16.41  ? 181 LEU A N   1 
ATOM   1355 C  CA  . LEU A 1 195 ? 15.091  -3.944  13.043  1.00 15.89  ? 181 LEU A CA  1 
ATOM   1356 C  C   . LEU A 1 195 ? 15.745  -3.205  14.203  1.00 17.45  ? 181 LEU A C   1 
ATOM   1357 O  O   . LEU A 1 195 ? 15.139  -3.066  15.262  1.00 16.59  ? 181 LEU A O   1 
ATOM   1358 C  CB  . LEU A 1 195 ? 15.425  -5.439  13.086  1.00 16.61  ? 181 LEU A CB  1 
ATOM   1359 C  CG  . LEU A 1 195 ? 14.668  -6.332  12.113  1.00 22.20  ? 181 LEU A CG  1 
ATOM   1360 C  CD1 . LEU A 1 195 ? 15.152  -7.768  12.242  1.00 25.59  ? 181 LEU A CD1 1 
ATOM   1361 C  CD2 . LEU A 1 195 ? 13.186  -6.270  12.384  1.00 21.99  ? 181 LEU A CD2 1 
ATOM   1362 N  N   . LYS A 1 196 ? 16.998  -2.806  14.021  1.00 17.81  ? 182 LYS A N   1 
ATOM   1363 C  CA  . LYS A 1 196 ? 17.703  -2.106  15.085  1.00 20.70  ? 182 LYS A CA  1 
ATOM   1364 C  C   . LYS A 1 196 ? 17.072  -0.730  15.309  1.00 19.29  ? 182 LYS A C   1 
ATOM   1365 O  O   . LYS A 1 196 ? 16.897  -0.339  16.455  1.00 19.10  ? 182 LYS A O   1 
ATOM   1366 C  CB  . LYS A 1 196 ? 19.180  -1.977  14.730  1.00 21.31  ? 182 LYS A CB  1 
ATOM   1367 C  CG  . LYS A 1 196 ? 20.097  -1.530  15.852  1.00 38.90  ? 182 LYS A CG  1 
ATOM   1368 C  CD  . LYS A 1 196 ? 21.582  -1.674  15.512  1.00 38.32  ? 182 LYS A CD  1 
ATOM   1369 C  CE  . LYS A 1 196 ? 22.492  -1.509  16.711  1.00 52.43  ? 182 LYS A CE  1 
ATOM   1370 N  NZ  . LYS A 1 196 ? 22.227  -0.239  17.431  1.00 61.98  ? 182 LYS A NZ  1 
ATOM   1371 N  N   . ARG A 1 197 ? 16.773  0.018   14.234  1.00 18.17  ? 183 ARG A N   1 
ATOM   1372 C  CA  . ARG A 1 197 ? 16.127  1.315   14.390  1.00 19.79  ? 183 ARG A CA  1 
ATOM   1373 C  C   . ARG A 1 197 ? 14.762  1.135   15.040  1.00 16.89  ? 183 ARG A C   1 
ATOM   1374 O  O   . ARG A 1 197 ? 14.405  1.943   15.900  1.00 16.50  ? 183 ARG A O   1 
ATOM   1375 C  CB  . ARG A 1 197 ? 15.968  2.040   13.055  1.00 22.29  ? 183 ARG A CB  1 
ATOM   1376 C  CG  . ARG A 1 197 ? 17.282  2.544   12.493  1.00 27.34  ? 183 ARG A CG  1 
ATOM   1377 C  CD  . ARG A 1 197 ? 17.178  3.051   11.080  1.00 37.97  ? 183 ARG A CD  1 
ATOM   1378 N  NE  . ARG A 1 197 ? 18.528  3.131   10.528  1.00 45.31  ? 183 ARG A NE  1 
ATOM   1379 C  CZ  . ARG A 1 197 ? 19.094  4.253   10.142  1.00 37.51  ? 183 ARG A CZ  1 
ATOM   1380 N  NH1 . ARG A 1 197 ? 18.466  5.393   10.339  1.00 36.68  ? 183 ARG A NH1 1 
ATOM   1381 N  NH2 . ARG A 1 197 ? 20.274  4.227   9.555   1.00 36.07  ? 183 ARG A NH2 1 
ATOM   1382 N  N   . MET A 1 198 ? 14.033  0.067   14.703  1.00 15.42  ? 184 MET A N   1 
ATOM   1383 C  CA  . MET A 1 198 ? 12.725  -0.135  15.280  1.00 15.32  ? 184 MET A CA  1 
ATOM   1384 C  C   . MET A 1 198 ? 12.859  -0.398  16.780  1.00 15.16  ? 184 MET A C   1 
ATOM   1385 O  O   . MET A 1 198 ? 12.082  0.068   17.602  1.00 15.65  ? 184 MET A O   1 
ATOM   1386 C  CB  . MET A 1 198 ? 12.024  -1.290  14.582  1.00 14.75  ? 184 MET A CB  1 
ATOM   1387 C  CG  . MET A 1 198 ? 11.525  -0.973  13.170  1.00 15.11  ? 184 MET A CG  1 
ATOM   1388 S  SD  . MET A 1 198 ? 10.701  -2.486  12.562  1.00 26.44  ? 184 MET A SD  1 
ATOM   1389 C  CE  . MET A 1 198 ? 10.808  -2.381  10.797  1.00 23.42  ? 184 MET A CE  1 
ATOM   1390 N  N   . ALA A 1 199 ? 13.860  -1.205  17.170  1.00 16.48  ? 185 ALA A N   1 
ATOM   1391 C  CA  . ALA A 1 199 ? 14.096  -1.507  18.571  1.00 16.43  ? 185 ALA A CA  1 
ATOM   1392 C  C   . ALA A 1 199 ? 14.428  -0.233  19.356  1.00 15.50  ? 185 ALA A C   1 
ATOM   1393 O  O   . ALA A 1 199 ? 13.986  -0.064  20.480  1.00 17.52  ? 185 ALA A O   1 
ATOM   1394 C  CB  . ALA A 1 199 ? 15.207  -2.523  18.691  1.00 19.52  ? 185 ALA A CB  1 
ATOM   1395 N  N   . GLU A 1 200 ? 15.225  0.652   18.772  1.00 16.63  ? 186 GLU A N   1 
ATOM   1396 C  CA  . GLU A 1 200 ? 15.539  1.937   19.367  1.00 18.19  ? 186 GLU A CA  1 
ATOM   1397 C  C   . GLU A 1 200 ? 14.278  2.771   19.568  1.00 17.16  ? 186 GLU A C   1 
ATOM   1398 O  O   . GLU A 1 200 ? 14.113  3.334   20.626  1.00 18.44  ? 186 GLU A O   1 
ATOM   1399 C  CB  . GLU A 1 200 ? 16.555  2.690   18.512  1.00 19.26  ? 186 GLU A CB  1 
ATOM   1400 C  CG  . GLU A 1 200 ? 17.952  2.101   18.585  1.00 28.00  ? 186 GLU A CG  1 
ATOM   1401 C  CD  . GLU A 1 200 ? 18.922  2.529   17.494  1.00 38.69  ? 186 GLU A CD  1 
ATOM   1402 O  OE1 . GLU A 1 200 ? 20.098  2.092   17.575  1.00 49.66  ? 186 GLU A OE1 1 
ATOM   1403 O  OE2 . GLU A 1 200 ? 18.514  3.262   16.539  1.00 34.42  ? 186 GLU A OE2 1 
ATOM   1404 N  N   . ILE A 1 201 ? 13.374  2.811   18.572  1.00 15.53  ? 187 ILE A N   1 
ATOM   1405 C  CA  . ILE A 1 201 ? 12.132  3.569   18.723  1.00 14.86  ? 187 ILE A CA  1 
ATOM   1406 C  C   . ILE A 1 201 ? 11.316  2.995   19.892  1.00 14.63  ? 187 ILE A C   1 
ATOM   1407 O  O   . ILE A 1 201 ? 10.802  3.751   20.732  1.00 16.01  ? 187 ILE A O   1 
ATOM   1408 C  CB  . ILE A 1 201 ? 11.339  3.490   17.392  1.00 14.75  ? 187 ILE A CB  1 
ATOM   1409 C  CG1 . ILE A 1 201 ? 12.047  4.280   16.278  1.00 16.35  ? 187 ILE A CG1 1 
ATOM   1410 C  CG2 . ILE A 1 201 ? 9.886   3.947   17.563  1.00 14.96  ? 187 ILE A CG2 1 
ATOM   1411 C  CD1 . ILE A 1 201 ? 11.512  4.042   14.869  1.00 17.88  ? 187 ILE A CD1 1 
ATOM   1412 N  N   . GLY A 1 202 ? 11.192  1.664   19.952  1.00 14.95  ? 188 GLY A N   1 
ATOM   1413 C  CA  . GLY A 1 202 ? 10.495  0.986   21.024  1.00 16.42  ? 188 GLY A CA  1 
ATOM   1414 C  C   . GLY A 1 202 ? 11.093  1.299   22.397  1.00 16.88  ? 188 GLY A C   1 
ATOM   1415 O  O   . GLY A 1 202 ? 10.366  1.509   23.367  1.00 17.64  ? 188 GLY A O   1 
ATOM   1416 N  N   . ASP A 1 203 ? 12.427  1.233   22.492  1.00 17.72  ? 189 ASP A N   1 
ATOM   1417 C  CA  . ASP A 1 203 ? 13.124  1.478   23.745  1.00 19.51  ? 189 ASP A CA  1 
ATOM   1418 C  C   . ASP A 1 203 ? 12.970  2.927   24.205  1.00 18.14  ? 189 ASP A C   1 
ATOM   1419 O  O   . ASP A 1 203 ? 12.902  3.220   25.406  1.00 21.84  ? 189 ASP A O   1 
ATOM   1420 C  CB  . ASP A 1 203 ? 14.605  1.134   23.593  1.00 21.43  ? 189 ASP A CB  1 
ATOM   1421 C  CG  . ASP A 1 203 ? 14.903  -0.353  23.546  1.00 23.06  ? 189 ASP A CG  1 
ATOM   1422 O  OD1 . ASP A 1 203 ? 13.990  -1.162  23.805  1.00 28.25  ? 189 ASP A OD1 1 
ATOM   1423 O  OD2 . ASP A 1 203 ? 16.055  -0.694  23.234  1.00 32.92  ? 189 ASP A OD2 1 
ATOM   1424 N  N   . GLU A 1 204 ? 12.919  3.855   23.266  1.00 18.94  ? 190 GLU A N   1 
ATOM   1425 C  CA  . GLU A 1 204 ? 12.807  5.262   23.601  1.00 19.92  ? 190 GLU A CA  1 
ATOM   1426 C  C   . GLU A 1 204 ? 11.405  5.607   24.093  1.00 18.32  ? 190 GLU A C   1 
ATOM   1427 O  O   . GLU A 1 204 ? 11.246  6.537   24.879  1.00 23.10  ? 190 GLU A O   1 
ATOM   1428 C  CB  . GLU A 1 204 ? 13.222  6.182   22.462  1.00 21.63  ? 190 GLU A CB  1 
ATOM   1429 C  CG  . GLU A 1 204 ? 14.700  6.167   22.167  1.00 26.19  ? 190 GLU A CG  1 
ATOM   1430 C  CD  . GLU A 1 204 ? 15.170  7.028   21.001  1.00 38.00  ? 190 GLU A CD  1 
ATOM   1431 O  OE1 . GLU A 1 204 ? 16.380  6.987   20.699  1.00 44.65  ? 190 GLU A OE1 1 
ATOM   1432 O  OE2 . GLU A 1 204 ? 14.343  7.759   20.398  1.00 49.23  ? 190 GLU A OE2 1 
ATOM   1433 N  N   . GLY A 1 205 ? 10.399  4.853   23.656  1.00 16.89  ? 191 GLY A N   1 
ATOM   1434 C  CA  . GLY A 1 205 ? 9.050   5.021   24.147  1.00 17.12  ? 191 GLY A CA  1 
ATOM   1435 C  C   . GLY A 1 205 ? 8.063   5.384   23.046  1.00 15.24  ? 191 GLY A C   1 
ATOM   1436 O  O   . GLY A 1 205 ? 8.120   6.507   22.544  1.00 16.29  ? 191 GLY A O   1 
ATOM   1437 N  N   . VAL A 1 206 ? 7.159   4.430   22.786  1.00 13.91  ? 192 VAL A N   1 
ATOM   1438 C  CA  . VAL A 1 206 ? 6.103   4.617   21.808  1.00 13.22  ? 192 VAL A CA  1 
ATOM   1439 C  C   . VAL A 1 206 ? 4.829   4.870   22.608  1.00 12.39  ? 192 VAL A C   1 
ATOM   1440 O  O   . VAL A 1 206 ? 4.345   4.019   23.336  1.00 14.40  ? 192 VAL A O   1 
ATOM   1441 C  CB  . VAL A 1 206 ? 6.031   3.375   20.904  1.00 13.85  ? 192 VAL A CB  1 
ATOM   1442 C  CG1 . VAL A 1 206 ? 4.816   3.472   19.997  1.00 13.39  ? 192 VAL A CG1 1 
ATOM   1443 C  CG2 . VAL A 1 206 ? 7.303   3.201   20.094  1.00 13.52  ? 192 VAL A CG2 1 
ATOM   1444 N  N   . PHE A 1 207 ? 4.280   6.044   22.339  1.00 13.32  ? 193 PHE A N   1 
ATOM   1445 C  CA  . PHE A 1 207 ? 2.980   6.442   22.871  1.00 12.90  ? 193 PHE A CA  1 
ATOM   1446 C  C   . PHE A 1 207 ? 1.835   5.729   22.153  1.00 11.64  ? 193 PHE A C   1 
ATOM   1447 O  O   . PHE A 1 207 ? 0.929   5.262   22.819  1.00 13.95  ? 193 PHE A O   1 
ATOM   1448 C  CB  . PHE A 1 207 ? 2.879   7.966   22.747  1.00 14.42  ? 193 PHE A CB  1 
ATOM   1449 C  CG  . PHE A 1 207 ? 1.514   8.516   23.024  1.00 15.84  ? 193 PHE A CG  1 
ATOM   1450 C  CD1 . PHE A 1 207 ? 1.038   8.556   24.320  1.00 20.08  ? 193 PHE A CD1 1 
ATOM   1451 C  CD2 . PHE A 1 207 ? 0.708   8.927   21.975  1.00 20.26  ? 193 PHE A CD2 1 
ATOM   1452 C  CE1 . PHE A 1 207 ? -0.229  9.064   24.570  1.00 22.45  ? 193 PHE A CE1 1 
ATOM   1453 C  CE2 . PHE A 1 207 ? -0.587  9.364   22.215  1.00 22.55  ? 193 PHE A CE2 1 
ATOM   1454 C  CZ  . PHE A 1 207 ? -1.022  9.441   23.509  1.00 22.93  ? 193 PHE A CZ  1 
ATOM   1455 N  N   . ALA A 1 208 ? 1.861   5.656   20.804  1.00 11.90  ? 194 ALA A N   1 
ATOM   1456 C  CA  . ALA A 1 208 ? 0.781   5.001   20.069  1.00 12.38  ? 194 ALA A CA  1 
ATOM   1457 C  C   . ALA A 1 208 ? 1.357   4.311   18.850  1.00 11.12  ? 194 ALA A C   1 
ATOM   1458 O  O   . ALA A 1 208 ? 2.165   4.910   18.150  1.00 12.83  ? 194 ALA A O   1 
ATOM   1459 C  CB  . ALA A 1 208 ? -0.345  5.943   19.650  1.00 12.01  ? 194 ALA A CB  1 
ATOM   1460 N  N   . LEU A 1 209 ? 0.920   3.078   18.634  1.00 10.67  ? 195 LEU A N   1 
ATOM   1461 C  CA  . LEU A 1 209 ? 1.259   2.354   17.424  1.00 10.56  ? 195 LEU A CA  1 
ATOM   1462 C  C   . LEU A 1 209 ? -0.005  2.214   16.590  1.00 9.61   ? 195 LEU A C   1 
ATOM   1463 O  O   . LEU A 1 209 ? -1.017  1.749   17.112  1.00 11.08  ? 195 LEU A O   1 
ATOM   1464 C  CB  . LEU A 1 209 ? 1.816   0.986   17.823  1.00 12.26  ? 195 LEU A CB  1 
ATOM   1465 C  CG  . LEU A 1 209 ? 2.150   0.071   16.639  1.00 11.38  ? 195 LEU A CG  1 
ATOM   1466 C  CD1 . LEU A 1 209 ? 3.282   0.611   15.773  1.00 11.47  ? 195 LEU A CD1 1 
ATOM   1467 C  CD2 . LEU A 1 209 ? 2.488   -1.350  17.145  1.00 12.85  ? 195 LEU A CD2 1 
ATOM   1468 N  N   . ILE A 1 210 ? 0.131   2.536   15.303  1.00 10.12  ? 196 ILE A N   1 
ATOM   1469 C  CA  . ILE A 1 210 ? -0.926  2.420   14.301  1.00 10.17  ? 196 ILE A CA  1 
ATOM   1470 C  C   . ILE A 1 210 ? -0.416  1.394   13.292  1.00 9.94   ? 196 ILE A C   1 
ATOM   1471 O  O   . ILE A 1 210 ? 0.564   1.660   12.599  1.00 9.88   ? 196 ILE A O   1 
ATOM   1472 C  CB  . ILE A 1 210 ? -1.164  3.808   13.653  1.00 11.15  ? 196 ILE A CB  1 
ATOM   1473 C  CG1 . ILE A 1 210 ? -1.466  4.892   14.686  1.00 11.82  ? 196 ILE A CG1 1 
ATOM   1474 C  CG2 . ILE A 1 210 ? -2.228  3.710   12.574  1.00 10.88  ? 196 ILE A CG2 1 
ATOM   1475 C  CD1 . ILE A 1 210 ? -1.381  6.305   14.125  1.00 11.79  ? 196 ILE A CD1 1 
ATOM   1476 N  N   . SER A 1 211 ? -1.046  0.201   13.255  1.00 9.20   ? 197 SER A N   1 
ATOM   1477 C  CA  . SER A 1 211 ? -0.457  -0.953  12.582  1.00 10.40  ? 197 SER A CA  1 
ATOM   1478 C  C   . SER A 1 211 ? -1.450  -1.688  11.690  1.00 9.85   ? 197 SER A C   1 
ATOM   1479 O  O   . SER A 1 211 ? -2.633  -1.722  11.966  1.00 10.67  ? 197 SER A O   1 
ATOM   1480 C  CB  . SER A 1 211 ? 0.161   -1.878  13.612  1.00 10.26  ? 197 SER A CB  1 
ATOM   1481 O  OG  . SER A 1 211 ? 0.854   -2.920  12.948  1.00 10.92  ? 197 SER A OG  1 
ATOM   1482 N  N   . ASP A 1 212 ? -0.943  -2.309  10.612  1.00 10.28  ? 198 ASP A N   1 
ATOM   1483 C  CA  . ASP A 1 212 ? -1.642  -3.007  9.543   1.00 10.30  ? 198 ASP A CA  1 
ATOM   1484 C  C   . ASP A 1 212 ? -2.286  -4.316  10.002  1.00 9.48   ? 198 ASP A C   1 
ATOM   1485 O  O   . ASP A 1 212 ? -1.606  -5.258  10.419  1.00 11.93  ? 198 ASP A O   1 
ATOM   1486 C  CB  . ASP A 1 212 ? -0.598  -3.291  8.498   1.00 10.93  ? 198 ASP A CB  1 
ATOM   1487 C  CG  . ASP A 1 212 ? -1.081  -3.995  7.242   1.00 12.10  ? 198 ASP A CG  1 
ATOM   1488 O  OD1 . ASP A 1 212 ? -2.281  -4.280  7.105   1.00 11.90  ? 198 ASP A OD1 1 
ATOM   1489 O  OD2 . ASP A 1 212 ? -0.198  -4.294  6.369   1.00 11.71  ? 198 ASP A OD2 1 
ATOM   1490 N  N   . SER A 1 213 ? -3.607  -4.403  9.846   1.00 9.76   ? 199 SER A N   1 
ATOM   1491 C  CA  . SER A 1 213 ? -4.379  -5.541  10.382  1.00 9.72   ? 199 SER A CA  1 
ATOM   1492 C  C   . SER A 1 213 ? -4.796  -6.552  9.324   1.00 10.81  ? 199 SER A C   1 
ATOM   1493 O  O   . SER A 1 213 ? -5.530  -7.501  9.626   1.00 11.30  ? 199 SER A O   1 
ATOM   1494 C  CB  . SER A 1 213 ? -5.629  -5.027  11.029  1.00 10.26  ? 199 SER A CB  1 
ATOM   1495 O  OG  . SER A 1 213 ? -5.378  -4.049  12.062  1.00 9.91   ? 199 SER A OG  1 
ATOM   1496 N  N   . THR A 1 214 ? -4.424  -6.322  8.080   1.00 10.05  ? 200 THR A N   1 
ATOM   1497 C  CA  . THR A 1 214 ? -4.928  -7.097  6.969   1.00 11.53  ? 200 THR A CA  1 
ATOM   1498 C  C   . THR A 1 214 ? -4.946  -8.612  7.209   1.00 12.00  ? 200 THR A C   1 
ATOM   1499 O  O   . THR A 1 214 ? -5.963  -9.245  6.883   1.00 14.27  ? 200 THR A O   1 
ATOM   1500 C  CB  . THR A 1 214 ? -4.111  -6.865  5.692   1.00 13.02  ? 200 THR A CB  1 
ATOM   1501 O  OG1 . THR A 1 214 ? -4.077  -5.468  5.403   1.00 13.67  ? 200 THR A OG1 1 
ATOM   1502 C  CG2 . THR A 1 214 ? -4.701  -7.537  4.467   1.00 14.61  ? 200 THR A CG2 1 
ATOM   1503 N  N   . GLU A 1 215 ? -3.839  -9.173  7.687   1.00 11.74  ? 201 GLU A N   1 
ATOM   1504 C  CA  . GLU A 1 215 ? -3.720  -10.617 7.898   1.00 11.74  ? 201 GLU A CA  1 
ATOM   1505 C  C   . GLU A 1 215 ? -3.727  -10.985 9.372   1.00 11.94  ? 201 GLU A C   1 
ATOM   1506 O  O   . GLU A 1 215 ? -3.252  -12.063 9.751   1.00 13.39  ? 201 GLU A O   1 
ATOM   1507 C  CB  . GLU A 1 215 ? -2.492  -11.139 7.188   1.00 12.92  ? 201 GLU A CB  1 
ATOM   1508 C  CG  . GLU A 1 215 ? -2.578  -11.054 5.684   1.00 14.98  ? 201 GLU A CG  1 
ATOM   1509 C  CD  . GLU A 1 215 ? -3.582  -11.928 4.991   1.00 21.90  ? 201 GLU A CD  1 
ATOM   1510 O  OE1 . GLU A 1 215 ? -3.956  -11.549 3.884   1.00 29.92  ? 201 GLU A OE1 1 
ATOM   1511 O  OE2 . GLU A 1 215 ? -3.976  -12.950 5.552   1.00 26.07  ? 201 GLU A OE2 1 
ATOM   1512 N  N   . ALA A 1 216 ? -4.275  -10.148 10.234  1.00 12.42  ? 202 ALA A N   1 
ATOM   1513 C  CA  . ALA A 1 216 ? -4.312  -10.400 11.667  1.00 12.77  ? 202 ALA A CA  1 
ATOM   1514 C  C   . ALA A 1 216 ? -5.143  -11.643 12.053  1.00 13.27  ? 202 ALA A C   1 
ATOM   1515 O  O   . ALA A 1 216 ? -4.919  -12.156 13.156  1.00 15.28  ? 202 ALA A O   1 
ATOM   1516 C  CB  . ALA A 1 216 ? -4.803  -9.183  12.404  1.00 12.12  ? 202 ALA A CB  1 
ATOM   1517 N  N   . GLU A 1 217 ? -6.021  -12.128 11.178  1.00 15.05  ? 203 GLU A N   1 
ATOM   1518 C  CA  . GLU A 1 217 ? -6.777  -13.337 11.467  1.00 16.01  ? 203 GLU A CA  1 
ATOM   1519 C  C   . GLU A 1 217 ? -5.950  -14.608 11.215  1.00 17.34  ? 203 GLU A C   1 
ATOM   1520 O  O   . GLU A 1 217 ? -6.425  -15.714 11.543  1.00 20.49  ? 203 GLU A O   1 
ATOM   1521 C  CB  . GLU A 1 217 ? -8.060  -13.357 10.654  1.00 16.84  ? 203 GLU A CB  1 
ATOM   1522 C  CG  . GLU A 1 217 ? -8.979  -12.172 10.872  1.00 18.66  ? 203 GLU A CG  1 
ATOM   1523 C  CD  . GLU A 1 217 ? -10.072 -12.031 9.824   1.00 20.90  ? 203 GLU A CD  1 
ATOM   1524 O  OE1 . GLU A 1 217 ? -9.748  -11.671 8.641   1.00 21.22  ? 203 GLU A OE1 1 
ATOM   1525 O  OE2 . GLU A 1 217 ? -11.236 -12.425 10.138  1.00 26.17  ? 203 GLU A OE2 1 
ATOM   1526 N  N   . LYS A 1 218 ? -4.807  -14.512 10.525  1.00 16.92  ? 204 LYS A N   1 
ATOM   1527 C  CA  . LYS A 1 218 ? -4.123  -15.683 10.017  1.00 17.72  ? 204 LYS A CA  1 
ATOM   1528 C  C   . LYS A 1 218 ? -3.029  -16.076 10.991  1.00 17.37  ? 204 LYS A C   1 
ATOM   1529 O  O   . LYS A 1 218 ? -2.042  -15.367 11.170  1.00 16.11  ? 204 LYS A O   1 
ATOM   1530 C  CB  . LYS A 1 218 ? -3.520  -15.423 8.634   1.00 16.79  ? 204 LYS A CB  1 
ATOM   1531 C  CG  . LYS A 1 218 ? -2.759  -16.622 8.080   1.00 22.40  ? 204 LYS A CG  1 
ATOM   1532 C  CD  . LYS A 1 218 ? -3.676  -17.830 7.763   1.00 27.72  ? 204 LYS A CD  1 
ATOM   1533 C  CE  . LYS A 1 218 ? -2.958  -19.113 7.390   1.00 32.39  ? 204 LYS A CE  1 
ATOM   1534 N  NZ  . LYS A 1 218 ? -2.403  -19.767 8.605   1.00 43.06  ? 204 LYS A NZ  1 
ATOM   1535 N  N   . PRO A 1 219 ? -3.105  -17.285 11.608  1.00 18.48  ? 205 PRO A N   1 
ATOM   1536 C  CA  . PRO A 1 219 ? -2.027  -17.740 12.488  1.00 18.87  ? 205 PRO A CA  1 
ATOM   1537 C  C   . PRO A 1 219 ? -0.686  -17.920 11.766  1.00 16.01  ? 205 PRO A C   1 
ATOM   1538 O  O   . PRO A 1 219 ? -0.636  -18.112 10.553  1.00 18.78  ? 205 PRO A O   1 
ATOM   1539 C  CB  . PRO A 1 219 ? -2.535  -19.098 13.017  1.00 19.59  ? 205 PRO A CB  1 
ATOM   1540 C  CG  . PRO A 1 219 ? -4.024  -19.005 12.893  1.00 23.84  ? 205 PRO A CG  1 
ATOM   1541 C  CD  . PRO A 1 219 ? -4.269  -18.186 11.636  1.00 20.25  ? 205 PRO A CD  1 
ATOM   1542 N  N   . GLY A 1 220 ? 0.394   -17.803 12.542  1.00 17.07  ? 206 GLY A N   1 
ATOM   1543 C  CA  . GLY A 1 220 ? 1.756   -18.041 12.104  1.00 15.36  ? 206 GLY A CA  1 
ATOM   1544 C  C   . GLY A 1 220 ? 2.389   -16.857 11.371  1.00 15.35  ? 206 GLY A C   1 
ATOM   1545 O  O   . GLY A 1 220 ? 2.168   -15.701 11.702  1.00 14.82  ? 206 GLY A O   1 
ATOM   1546 N  N   . TYR A 1 221 ? 3.160   -17.205 10.329  1.00 16.18  ? 207 TYR A N   1 
ATOM   1547 C  CA  . TYR A 1 221 ? 3.919   -16.303 9.491   1.00 15.16  ? 207 TYR A CA  1 
ATOM   1548 C  C   . TYR A 1 221 ? 3.443   -16.481 8.055   1.00 17.16  ? 207 TYR A C   1 
ATOM   1549 O  O   . TYR A 1 221 ? 3.104   -17.581 7.644   1.00 17.41  ? 207 TYR A O   1 
ATOM   1550 C  CB  . TYR A 1 221 ? 5.418   -16.597 9.533   1.00 15.82  ? 207 TYR A CB  1 
ATOM   1551 C  CG  . TYR A 1 221 ? 6.097   -16.375 10.850  1.00 15.91  ? 207 TYR A CG  1 
ATOM   1552 C  CD1 . TYR A 1 221 ? 6.032   -17.333 11.854  1.00 17.34  ? 207 TYR A CD1 1 
ATOM   1553 C  CD2 . TYR A 1 221 ? 6.801   -15.217 11.118  1.00 16.99  ? 207 TYR A CD2 1 
ATOM   1554 C  CE1 . TYR A 1 221 ? 6.663   -17.152 13.074  1.00 17.64  ? 207 TYR A CE1 1 
ATOM   1555 C  CE2 . TYR A 1 221 ? 7.414   -15.016 12.332  1.00 17.99  ? 207 TYR A CE2 1 
ATOM   1556 C  CZ  . TYR A 1 221 ? 7.389   -16.007 13.295  1.00 18.13  ? 207 TYR A CZ  1 
ATOM   1557 O  OH  . TYR A 1 221 ? 8.013   -15.832 14.490  1.00 22.59  ? 207 TYR A OH  1 
ATOM   1558 N  N   . ASN A 1 222 ? 3.579   -15.444 7.241   1.00 16.25  ? 208 ASN A N   1 
ATOM   1559 C  CA  . ASN A 1 222 ? 3.499   -15.598 5.797   1.00 17.65  ? 208 ASN A CA  1 
ATOM   1560 C  C   . ASN A 1 222 ? 4.499   -16.651 5.340   1.00 18.51  ? 208 ASN A C   1 
ATOM   1561 O  O   . ASN A 1 222 ? 5.585   -16.712 5.881   1.00 17.27  ? 208 ASN A O   1 
ATOM   1562 C  CB  . ASN A 1 222 ? 3.857   -14.298 5.087   1.00 17.44  ? 208 ASN A CB  1 
ATOM   1563 C  CG  . ASN A 1 222 ? 2.718   -13.299 5.087   1.00 16.61  ? 208 ASN A CG  1 
ATOM   1564 O  OD1 . ASN A 1 222 ? 2.835   -12.228 5.691   1.00 20.84  ? 208 ASN A OD1 1 
ATOM   1565 N  ND2 . ASN A 1 222 ? 1.590   -13.695 4.523   1.00 18.17  ? 208 ASN A ND2 1 
ATOM   1566 N  N   . THR A 1 223 ? 4.164   -17.398 4.289   1.00 17.90  ? 209 THR A N   1 
ATOM   1567 C  CA  . THR A 1 223 ? 5.158   -18.258 3.663   1.00 19.53  ? 209 THR A CA  1 
ATOM   1568 C  C   . THR A 1 223 ? 6.300   -17.380 3.148   1.00 19.43  ? 209 THR A C   1 
ATOM   1569 O  O   . THR A 1 223 ? 6.061   -16.365 2.480   1.00 17.59  ? 209 THR A O   1 
ATOM   1570 C  CB  . THR A 1 223 ? 4.574   -19.089 2.527   1.00 20.02  ? 209 THR A CB  1 
ATOM   1571 O  OG1 . THR A 1 223 ? 3.474   -19.818 3.082   1.00 21.28  ? 209 THR A OG1 1 
ATOM   1572 C  CG2 . THR A 1 223 ? 5.635   -19.979 1.913   1.00 20.97  ? 209 THR A CG2 1 
ATOM   1573 N  N   . PRO A 1 224 ? 7.574   -17.709 3.448   1.00 16.49  ? 210 PRO A N   1 
ATOM   1574 C  CA  . PRO A 1 224 ? 8.713   -16.939 2.965   1.00 17.31  ? 210 PRO A CA  1 
ATOM   1575 C  C   . PRO A 1 224 ? 8.690   -16.888 1.445   1.00 17.56  ? 210 PRO A C   1 
ATOM   1576 O  O   . PRO A 1 224 ? 8.366   -17.868 0.815   1.00 17.22  ? 210 PRO A O   1 
ATOM   1577 C  CB  . PRO A 1 224 ? 9.914   -17.760 3.436   1.00 21.54  ? 210 PRO A CB  1 
ATOM   1578 C  CG  . PRO A 1 224 ? 9.417   -18.380 4.692   1.00 20.92  ? 210 PRO A CG  1 
ATOM   1579 C  CD  . PRO A 1 224 ? 8.002   -18.785 4.377   1.00 20.53  ? 210 PRO A CD  1 
ATOM   1580 N  N   . GLU A 1 225 ? 9.133   -15.779 0.873   1.00 16.42  ? 211 GLU A N   1 
ATOM   1581 C  CA  . GLU A 1 225 ? 9.064   -15.581 -0.562  1.00 16.09  ? 211 GLU A CA  1 
ATOM   1582 C  C   . GLU A 1 225 ? 9.949   -16.558 -1.328  1.00 16.80  ? 211 GLU A C   1 
ATOM   1583 O  O   . GLU A 1 225 ? 9.618   -16.895 -2.448  1.00 16.80  ? 211 GLU A O   1 
ATOM   1584 C  CB  . GLU A 1 225 ? 9.404   -14.141 -0.906  1.00 18.26  ? 211 GLU A CB  1 
ATOM   1585 C  CG  . GLU A 1 225 ? 8.324   -13.166 -0.504  1.00 17.64  ? 211 GLU A CG  1 
ATOM   1586 C  CD  . GLU A 1 225 ? 7.021   -13.194 -1.277  1.00 18.53  ? 211 GLU A CD  1 
ATOM   1587 O  OE1 . GLU A 1 225 ? 6.891   -13.984 -2.187  1.00 18.27  ? 211 GLU A OE1 1 
ATOM   1588 O  OE2 . GLU A 1 225 ? 6.112   -12.399 -0.902  1.00 21.06  ? 211 GLU A OE2 1 
ATOM   1589 N  N   . ASN A 1 226 ? 11.058  -17.044 -0.746  1.00 17.54  ? 212 ASN A N   1 
ATOM   1590 C  CA  . ASN A 1 226 ? 11.876  -18.034 -1.468  1.00 18.85  ? 212 ASN A CA  1 
ATOM   1591 C  C   . ASN A 1 226 ? 11.087  -19.325 -1.711  1.00 18.66  ? 212 ASN A C   1 
ATOM   1592 O  O   . ASN A 1 226 ? 11.278  -19.984 -2.741  1.00 20.82  ? 212 ASN A O   1 
ATOM   1593 C  CB  . ASN A 1 226 ? 13.211  -18.343 -0.776  1.00 18.81  ? 212 ASN A CB  1 
ATOM   1594 C  CG  . ASN A 1 226 ? 13.091  -18.927 0.624   1.00 21.64  ? 212 ASN A CG  1 
ATOM   1595 O  OD1 . ASN A 1 226 ? 12.334  -18.415 1.446   1.00 22.92  ? 212 ASN A OD1 1 
ATOM   1596 N  ND2 . ASN A 1 226 ? 13.744  -20.052 0.884   1.00 23.36  ? 212 ASN A ND2 1 
ATOM   1597 N  N   . ILE A 1 227 ? 10.299  -19.753 -0.726  1.00 19.11  ? 213 ILE A N   1 
ATOM   1598 C  CA  . ILE A 1 227 ? 9.461   -20.931 -0.777  1.00 19.98  ? 213 ILE A CA  1 
ATOM   1599 C  C   . ILE A 1 227 ? 8.324   -20.678 -1.757  1.00 19.27  ? 213 ILE A C   1 
ATOM   1600 O  O   . ILE A 1 227 ? 7.995   -21.535 -2.565  1.00 18.68  ? 213 ILE A O   1 
ATOM   1601 C  CB  . ILE A 1 227 ? 9.027   -21.319 0.650   1.00 18.96  ? 213 ILE A CB  1 
ATOM   1602 C  CG1 . ILE A 1 227 ? 10.267  -21.638 1.514   1.00 21.70  ? 213 ILE A CG1 1 
ATOM   1603 C  CG2 . ILE A 1 227 ? 7.945   -22.399 0.624   1.00 19.55  ? 213 ILE A CG2 1 
ATOM   1604 C  CD1 . ILE A 1 227 ? 9.953   -22.009 2.932   1.00 25.15  ? 213 ILE A CD1 1 
ATOM   1605 N  N   . ILE A 1 228 ? 7.753   -19.479 -1.736  1.00 17.53  ? 214 ILE A N   1 
ATOM   1606 C  CA  . ILE A 1 228 ? 6.744   -19.132 -2.739  1.00 16.25  ? 214 ILE A CA  1 
ATOM   1607 C  C   . ILE A 1 228 ? 7.313   -19.256 -4.155  1.00 15.98  ? 214 ILE A C   1 
ATOM   1608 O  O   . ILE A 1 228 ? 6.648   -19.832 -5.024  1.00 15.79  ? 214 ILE A O   1 
ATOM   1609 C  CB  . ILE A 1 228 ? 6.122   -17.747 -2.461  1.00 16.43  ? 214 ILE A CB  1 
ATOM   1610 C  CG1 . ILE A 1 228 ? 5.242   -17.812 -1.194  1.00 18.13  ? 214 ILE A CG1 1 
ATOM   1611 C  CG2 . ILE A 1 228 ? 5.367   -17.187 -3.679  1.00 16.14  ? 214 ILE A CG2 1 
ATOM   1612 C  CD1 . ILE A 1 228 ? 4.603   -16.510 -0.802  1.00 27.59  ? 214 ILE A CD1 1 
ATOM   1613 N  N   . GLU A 1 229 ? 8.514   -18.699 -4.357  1.00 14.97  ? 215 GLU A N   1 
ATOM   1614 C  CA  . GLU A 1 229 ? 9.097   -18.703 -5.693  1.00 16.65  ? 215 GLU A CA  1 
ATOM   1615 C  C   . GLU A 1 229 ? 9.324   -20.143 -6.171  1.00 18.17  ? 215 GLU A C   1 
ATOM   1616 O  O   . GLU A 1 229 ? 9.116   -20.455 -7.343  1.00 17.06  ? 215 GLU A O   1 
ATOM   1617 C  CB  . GLU A 1 229 ? 10.393  -17.898 -5.730  1.00 19.05  ? 215 GLU A CB  1 
ATOM   1618 C  CG  . GLU A 1 229 ? 11.001  -17.818 -7.119  1.00 18.45  ? 215 GLU A CG  1 
ATOM   1619 C  CD  . GLU A 1 229 ? 12.194  -16.877 -7.195  1.00 24.64  ? 215 GLU A CD  1 
ATOM   1620 O  OE1 . GLU A 1 229 ? 12.513  -16.264 -6.164  1.00 29.96  ? 215 GLU A OE1 1 
ATOM   1621 O  OE2 . GLU A 1 229 ? 12.805  -16.755 -8.259  1.00 26.69  ? 215 GLU A OE2 1 
ATOM   1622 N  N   . HIS A 1 230 ? 9.818   -21.003 -5.277  1.00 17.88  ? 216 HIS A N   1 
ATOM   1623 C  CA  . HIS A 1 230 ? 10.051  -22.417 -5.562  1.00 18.62  ? 216 HIS A CA  1 
ATOM   1624 C  C   . HIS A 1 230 ? 8.741   -23.131 -5.935  1.00 18.59  ? 216 HIS A C   1 
ATOM   1625 O  O   . HIS A 1 230 ? 8.686   -23.910 -6.903  1.00 19.54  ? 216 HIS A O   1 
ATOM   1626 C  CB  . HIS A 1 230 ? 10.799  -23.033 -4.371  1.00 21.12  ? 216 HIS A CB  1 
ATOM   1627 C  CG  . HIS A 1 230 ? 12.240  -22.583 -4.288  1.00 27.72  ? 216 HIS A CG  1 
ATOM   1628 N  ND1 . HIS A 1 230 ? 13.060  -22.776 -3.191  1.00 34.71  ? 216 HIS A ND1 1 
ATOM   1629 C  CD2 . HIS A 1 230 ? 12.995  -21.882 -5.202  1.00 34.68  ? 216 HIS A CD2 1 
ATOM   1630 C  CE1 . HIS A 1 230 ? 14.262  -22.251 -3.434  1.00 40.80  ? 216 HIS A CE1 1 
ATOM   1631 N  NE2 . HIS A 1 230 ? 14.240  -21.672 -4.668  1.00 39.18  ? 216 HIS A NE2 1 
ATOM   1632 N  N   . HIS A 1 231 ? 7.650   -22.827 -5.230  1.00 16.93  ? 217 HIS A N   1 
ATOM   1633 C  CA  . HIS A 1 231 ? 6.357   -23.412 -5.541  1.00 17.54  ? 217 HIS A CA  1 
ATOM   1634 C  C   . HIS A 1 231 ? 5.782   -22.862 -6.850  1.00 18.35  ? 217 HIS A C   1 
ATOM   1635 O  O   . HIS A 1 231 ? 5.154   -23.629 -7.594  1.00 18.77  ? 217 HIS A O   1 
ATOM   1636 C  CB  . HIS A 1 231 ? 5.375   -23.268 -4.359  1.00 23.44  ? 217 HIS A CB  1 
ATOM   1637 C  CG  . HIS A 1 231 ? 5.645   -24.248 -3.241  1.00 27.19  ? 217 HIS A CG  1 
ATOM   1638 N  ND1 . HIS A 1 231 ? 5.093   -25.506 -3.164  1.00 33.68  ? 217 HIS A ND1 1 
ATOM   1639 C  CD2 . HIS A 1 231 ? 6.497   -24.133 -2.183  1.00 29.31  ? 217 HIS A CD2 1 
ATOM   1640 C  CE1 . HIS A 1 231 ? 5.538   -26.120 -2.073  1.00 38.66  ? 217 HIS A CE1 1 
ATOM   1641 N  NE2 . HIS A 1 231 ? 6.408   -25.280 -1.445  1.00 35.51  ? 217 HIS A NE2 1 
ATOM   1642 N  N   . MET A 1 232 ? 6.024   -21.583 -7.147  1.00 16.81  ? 218 MET A N   1 
ATOM   1643 C  CA  . MET A 1 232 ? 5.595   -21.015 -8.421  1.00 16.25  ? 218 MET A CA  1 
ATOM   1644 C  C   . MET A 1 232 ? 6.311   -21.716 -9.567  1.00 15.41  ? 218 MET A C   1 
ATOM   1645 O  O   . MET A 1 232 ? 5.711   -22.033 -10.588 1.00 16.03  ? 218 MET A O   1 
ATOM   1646 C  CB  . MET A 1 232 ? 5.883   -19.512 -8.462  1.00 16.07  ? 218 MET A CB  1 
ATOM   1647 C  CG  . MET A 1 232 ? 4.957   -18.708 -7.584  1.00 18.92  ? 218 MET A CG  1 
ATOM   1648 S  SD  . MET A 1 232 ? 5.504   -16.996 -7.340  1.00 17.51  ? 218 MET A SD  1 
ATOM   1649 C  CE  . MET A 1 232 ? 5.366   -16.336 -8.988  1.00 17.60  ? 218 MET A CE  1 
ATOM   1650 N  N   . TYR A 1 233 ? 7.625   -21.937 -9.379  1.00 16.02  ? 219 TYR A N   1 
ATOM   1651 C  CA  . TYR A 1 233 ? 8.376   -22.664 -10.396 1.00 16.09  ? 219 TYR A CA  1 
ATOM   1652 C  C   . TYR A 1 233 ? 7.713   -24.002 -10.713 1.00 16.85  ? 219 TYR A C   1 
ATOM   1653 O  O   . TYR A 1 233 ? 7.522   -24.319 -11.895 1.00 17.74  ? 219 TYR A O   1 
ATOM   1654 C  CB  . TYR A 1 233 ? 9.857   -22.866 -10.023 1.00 16.50  ? 219 TYR A CB  1 
ATOM   1655 C  CG  . TYR A 1 233 ? 10.567  -23.706 -11.039 1.00 16.19  ? 219 TYR A CG  1 
ATOM   1656 C  CD1 . TYR A 1 233 ? 10.496  -25.083 -10.978 1.00 15.48  ? 219 TYR A CD1 1 
ATOM   1657 C  CD2 . TYR A 1 233 ? 11.300  -23.137 -12.055 1.00 17.22  ? 219 TYR A CD2 1 
ATOM   1658 C  CE1 . TYR A 1 233 ? 11.105  -25.876 -11.935 1.00 16.76  ? 219 TYR A CE1 1 
ATOM   1659 C  CE2 . TYR A 1 233 ? 11.912  -23.916 -13.021 1.00 16.60  ? 219 TYR A CE2 1 
ATOM   1660 C  CZ  . TYR A 1 233 ? 11.823  -25.296 -12.965 1.00 16.29  ? 219 TYR A CZ  1 
ATOM   1661 O  OH  . TYR A 1 233 ? 12.397  -26.123 -13.922 1.00 18.79  ? 219 TYR A OH  1 
ATOM   1662 N  N   . ASP A 1 234 ? 7.415   -24.781 -9.667  1.00 16.32  ? 220 ASP A N   1 
ATOM   1663 C  CA  . ASP A 1 234 ? 6.848   -26.106 -9.847  1.00 18.47  ? 220 ASP A CA  1 
ATOM   1664 C  C   . ASP A 1 234 ? 5.531   -25.998 -10.603 1.00 18.75  ? 220 ASP A C   1 
ATOM   1665 O  O   . ASP A 1 234 ? 5.266   -26.793 -11.508 1.00 20.28  ? 220 ASP A O   1 
ATOM   1666 C  CB  . ASP A 1 234 ? 6.671   -26.855 -8.519  1.00 20.79  ? 220 ASP A CB  1 
ATOM   1667 C  CG  . ASP A 1 234 ? 7.959   -27.313 -7.860  1.00 26.62  ? 220 ASP A CG  1 
ATOM   1668 O  OD1 . ASP A 1 234 ? 9.016   -27.259 -8.513  1.00 26.56  ? 220 ASP A OD1 1 
ATOM   1669 O  OD2 . ASP A 1 234 ? 7.891   -27.663 -6.687  1.00 30.70  ? 220 ASP A OD2 1 
ATOM   1670 N  N   . ALA A 1 235 ? 4.685   -25.043 -10.178 1.00 18.74  ? 221 ALA A N   1 
ATOM   1671 C  CA  . ALA A 1 235 ? 3.383   -24.877 -10.808 1.00 19.13  ? 221 ALA A CA  1 
ATOM   1672 C  C   . ALA A 1 235 ? 3.545   -24.486 -12.279 1.00 17.30  ? 221 ALA A C   1 
ATOM   1673 O  O   . ALA A 1 235 ? 2.858   -25.023 -13.158 1.00 19.91  ? 221 ALA A O   1 
ATOM   1674 C  CB  . ALA A 1 235 ? 2.592   -23.826 -10.076 1.00 19.98  ? 221 ALA A CB  1 
ATOM   1675 N  N   . PHE A 1 236 ? 4.429   -23.535 -12.545 1.00 16.46  ? 222 PHE A N   1 
ATOM   1676 C  CA  . PHE A 1 236 ? 4.572   -22.970 -13.879 1.00 16.56  ? 222 PHE A CA  1 
ATOM   1677 C  C   . PHE A 1 236 ? 5.170   -24.008 -14.825 1.00 17.68  ? 222 PHE A C   1 
ATOM   1678 O  O   . PHE A 1 236 ? 4.829   -24.049 -15.996 1.00 18.47  ? 222 PHE A O   1 
ATOM   1679 C  CB  . PHE A 1 236 ? 5.391   -21.683 -13.913 1.00 14.90  ? 222 PHE A CB  1 
ATOM   1680 C  CG  . PHE A 1 236 ? 4.779   -20.444 -13.274 1.00 15.75  ? 222 PHE A CG  1 
ATOM   1681 C  CD1 . PHE A 1 236 ? 3.625   -20.467 -12.501 1.00 17.64  ? 222 PHE A CD1 1 
ATOM   1682 C  CD2 . PHE A 1 236 ? 5.452   -19.241 -13.403 1.00 17.36  ? 222 PHE A CD2 1 
ATOM   1683 C  CE1 . PHE A 1 236 ? 3.164   -19.281 -11.915 1.00 18.05  ? 222 PHE A CE1 1 
ATOM   1684 C  CE2 . PHE A 1 236 ? 4.982   -18.071 -12.827 1.00 19.89  ? 222 PHE A CE2 1 
ATOM   1685 C  CZ  . PHE A 1 236 ? 3.864   -18.123 -12.051 1.00 18.60  ? 222 PHE A CZ  1 
ATOM   1686 N  N   . ALA A 1 237 ? 6.063   -24.856 -14.285 1.00 17.37  ? 223 ALA A N   1 
ATOM   1687 C  CA  . ALA A 1 237 ? 6.693   -25.914 -15.058 1.00 21.70  ? 223 ALA A CA  1 
ATOM   1688 C  C   . ALA A 1 237 ? 5.653   -26.887 -15.638 1.00 19.59  ? 223 ALA A C   1 
ATOM   1689 O  O   . ALA A 1 237 ? 5.958   -27.515 -16.653 1.00 22.70  ? 223 ALA A O   1 
ATOM   1690 C  CB  . ALA A 1 237 ? 7.746   -26.632 -14.212 1.00 20.36  ? 223 ALA A CB  1 
ATOM   1691 N  N   . LYS A 1 238 ? 4.495   -27.082 -14.985 1.00 20.71  ? 224 LYS A N   1 
ATOM   1692 C  CA  . LYS A 1 238 ? 3.432   -27.989 -15.405 1.00 21.34  ? 224 LYS A CA  1 
ATOM   1693 C  C   . LYS A 1 238 ? 2.511   -27.379 -16.465 1.00 24.00  ? 224 LYS A C   1 
ATOM   1694 O  O   . LYS A 1 238 ? 1.700   -28.102 -17.046 1.00 26.22  ? 224 LYS A O   1 
ATOM   1695 C  CB  . LYS A 1 238 ? 2.505   -28.409 -14.254 1.00 26.38  ? 224 LYS A CB  1 
ATOM   1696 C  CG  . LYS A 1 238 ? 3.145   -29.154 -13.090 1.00 32.93  ? 224 LYS A CG  1 
ATOM   1697 C  CD  . LYS A 1 238 ? 2.164   -29.351 -11.955 1.00 37.26  ? 224 LYS A CD  1 
ATOM   1698 C  CE  . LYS A 1 238 ? 2.750   -29.990 -10.717 1.00 50.74  ? 224 LYS A CE  1 
ATOM   1699 N  NZ  . LYS A 1 238 ? 2.801   -31.466 -10.837 1.00 71.38  ? 224 LYS A NZ  1 
ATOM   1700 N  N   . VAL A 1 239 ? 2.589   -26.064 -16.710 1.00 18.59  ? 225 VAL A N   1 
ATOM   1701 C  CA  . VAL A 1 239 ? 1.688   -25.379 -17.623 1.00 21.04  ? 225 VAL A CA  1 
ATOM   1702 C  C   . VAL A 1 239 ? 2.037   -25.761 -19.059 1.00 19.48  ? 225 VAL A C   1 
ATOM   1703 O  O   . VAL A 1 239 ? 3.169   -25.543 -19.520 1.00 21.86  ? 225 VAL A O   1 
ATOM   1704 C  CB  . VAL A 1 239 ? 1.777   -23.856 -17.412 1.00 18.48  ? 225 VAL A CB  1 
ATOM   1705 C  CG1 . VAL A 1 239 ? 0.984   -23.150 -18.488 1.00 20.55  ? 225 VAL A CG1 1 
ATOM   1706 C  CG2 . VAL A 1 239 ? 1.233   -23.469 -16.060 1.00 20.48  ? 225 VAL A CG2 1 
ATOM   1707 N  N   . LYS A 1 240 ? 1.060   -26.293 -19.817 1.00 23.96  ? 226 LYS A N   1 
ATOM   1708 C  CA  . LYS A 1 240 ? 1.350   -26.766 -21.173 1.00 28.06  ? 226 LYS A CA  1 
ATOM   1709 C  C   . LYS A 1 240 ? 1.118   -25.698 -22.241 1.00 21.34  ? 226 LYS A C   1 
ATOM   1710 O  O   . LYS A 1 240 ? 1.697   -25.811 -23.340 1.00 23.94  ? 226 LYS A O   1 
ATOM   1711 C  CB  . LYS A 1 240 ? 0.522   -27.991 -21.543 1.00 30.61  ? 226 LYS A CB  1 
ATOM   1712 C  CG  . LYS A 1 240 ? 0.808   -29.191 -20.659 1.00 30.79  ? 226 LYS A CG  1 
ATOM   1713 C  CD  . LYS A 1 240 ? -0.216  -30.290 -20.784 1.00 48.60  ? 226 LYS A CD  1 
ATOM   1714 C  CE  . LYS A 1 240 ? 0.056   -31.448 -19.846 1.00 58.39  ? 226 LYS A CE  1 
ATOM   1715 N  NZ  . LYS A 1 240 ? -0.870  -32.574 -20.106 1.00 73.22  ? 226 LYS A NZ  1 
ATOM   1716 N  N   . GLY A 1 241 ? 0.278   -24.689 -21.950 1.00 20.93  ? 227 GLY A N   1 
ATOM   1717 C  CA  . GLY A 1 241 ? 0.030   -23.623 -22.904 1.00 21.04  ? 227 GLY A CA  1 
ATOM   1718 C  C   . GLY A 1 241 ? 0.485   -22.281 -22.359 1.00 20.06  ? 227 GLY A C   1 
ATOM   1719 O  O   . GLY A 1 241 ? 1.530   -22.167 -21.724 1.00 20.25  ? 227 GLY A O   1 
ATOM   1720 N  N   . ARG A 1 242 ? -0.267  -21.232 -22.687 1.00 19.59  ? 228 ARG A N   1 
ATOM   1721 C  CA  . ARG A 1 242 ? 0.059   -19.895 -22.223 1.00 19.29  ? 228 ARG A CA  1 
ATOM   1722 C  C   . ARG A 1 242 ? -0.208  -19.805 -20.718 1.00 15.74  ? 228 ARG A C   1 
ATOM   1723 O  O   . ARG A 1 242 ? -1.059  -20.503 -20.204 1.00 16.21  ? 228 ARG A O   1 
ATOM   1724 C  CB  . ARG A 1 242 ? -0.799  -18.844 -22.915 1.00 18.55  ? 228 ARG A CB  1 
ATOM   1725 C  CG  . ARG A 1 242 ? -0.717  -18.846 -24.423 1.00 22.86  ? 228 ARG A CG  1 
ATOM   1726 C  CD  . ARG A 1 242 ? -1.278  -17.572 -25.016 1.00 21.51  ? 228 ARG A CD  1 
ATOM   1727 N  NE  . ARG A 1 242 ? -2.644  -17.310 -24.590 1.00 24.72  ? 228 ARG A NE  1 
ATOM   1728 C  CZ  . ARG A 1 242 ? -3.314  -16.234 -24.958 1.00 25.40  ? 228 ARG A CZ  1 
ATOM   1729 N  NH1 . ARG A 1 242 ? -2.742  -15.366 -25.780 1.00 25.55  ? 228 ARG A NH1 1 
ATOM   1730 N  NH2 . ARG A 1 242 ? -4.524  -16.007 -24.468 1.00 23.30  ? 228 ARG A NH2 1 
ATOM   1731 N  N   . LEU A 1 243 ? 0.526   -18.907 -20.048 1.00 15.76  ? 229 LEU A N   1 
ATOM   1732 C  CA  . LEU A 1 243 ? 0.299   -18.597 -18.645 1.00 16.27  ? 229 LEU A CA  1 
ATOM   1733 C  C   . LEU A 1 243 ? -0.051  -17.124 -18.559 1.00 14.59  ? 229 LEU A C   1 
ATOM   1734 O  O   . LEU A 1 243 ? 0.718   -16.300 -19.034 1.00 15.56  ? 229 LEU A O   1 
ATOM   1735 C  CB  . LEU A 1 243 ? 1.576   -18.902 -17.853 1.00 16.09  ? 229 LEU A CB  1 
ATOM   1736 C  CG  . LEU A 1 243 ? 1.490   -18.552 -16.377 1.00 17.98  ? 229 LEU A CG  1 
ATOM   1737 C  CD1 . LEU A 1 243 ? 0.382   -19.330 -15.715 1.00 17.53  ? 229 LEU A CD1 1 
ATOM   1738 C  CD2 . LEU A 1 243 ? 2.806   -18.804 -15.668 1.00 21.12  ? 229 LEU A CD2 1 
ATOM   1739 N  N   . ILE A 1 244 ? -1.093  -16.849 -17.767 1.00 14.91  ? 230 ILE A N   1 
ATOM   1740 C  CA  . ILE A 1 244 ? -1.447  -15.484 -17.434 1.00 16.30  ? 230 ILE A CA  1 
ATOM   1741 C  C   . ILE A 1 244 ? -1.297  -15.355 -15.930 1.00 14.93  ? 230 ILE A C   1 
ATOM   1742 O  O   . ILE A 1 244 ? -1.916  -16.096 -15.185 1.00 15.85  ? 230 ILE A O   1 
ATOM   1743 C  CB  . ILE A 1 244 ? -2.885  -15.148 -17.859 1.00 16.54  ? 230 ILE A CB  1 
ATOM   1744 C  CG1 . ILE A 1 244 ? -2.999  -15.252 -19.375 1.00 22.24  ? 230 ILE A CG1 1 
ATOM   1745 C  CG2 . ILE A 1 244 ? -3.264  -13.741 -17.387 1.00 18.73  ? 230 ILE A CG2 1 
ATOM   1746 C  CD1 . ILE A 1 244 ? -3.251  -16.608 -19.883 1.00 32.85  ? 230 ILE A CD1 1 
ATOM   1747 N  N   . VAL A 1 245 ? -0.479  -14.390 -15.517 1.00 14.52  ? 231 VAL A N   1 
ATOM   1748 C  CA  . VAL A 1 245 ? -0.331  -14.090 -14.107 1.00 15.90  ? 231 VAL A CA  1 
ATOM   1749 C  C   . VAL A 1 245 ? -1.099  -12.798 -13.826 1.00 15.10  ? 231 VAL A C   1 
ATOM   1750 O  O   . VAL A 1 245 ? -0.787  -11.772 -14.420 1.00 16.91  ? 231 VAL A O   1 
ATOM   1751 C  CB  . VAL A 1 245 ? 1.149   -13.936 -13.745 1.00 16.14  ? 231 VAL A CB  1 
ATOM   1752 C  CG1 . VAL A 1 245 ? 1.295   -13.499 -12.290 1.00 17.20  ? 231 VAL A CG1 1 
ATOM   1753 C  CG2 . VAL A 1 245 ? 1.942   -15.195 -14.020 1.00 16.98  ? 231 VAL A CG2 1 
ATOM   1754 N  N   . SER A 1 246 ? -1.949  -12.836 -12.802 1.00 14.93  ? 232 SER A N   1 
ATOM   1755 C  CA  . SER A 1 246 ? -2.756  -11.700 -12.411 1.00 16.45  ? 232 SER A CA  1 
ATOM   1756 C  C   . SER A 1 246 ? -2.207  -11.220 -11.079 1.00 16.30  ? 232 SER A C   1 
ATOM   1757 O  O   . SER A 1 246 ? -2.244  -11.966 -10.107 1.00 18.50  ? 232 SER A O   1 
ATOM   1758 C  CB  . SER A 1 246 ? -4.227  -12.144 -12.276 1.00 18.37  ? 232 SER A CB  1 
ATOM   1759 O  OG  . SER A 1 246 ? -5.058  -11.141 -11.781 1.00 23.20  ? 232 SER A OG  1 
ATOM   1760 N  N   . CYS A 1 247 ? -1.698  -9.977  -11.024 1.00 17.61  ? 233 CYS A N   1 
ATOM   1761 C  CA  . CYS A 1 247 ? -1.185  -9.426  -9.773  1.00 18.67  ? 233 CYS A CA  1 
ATOM   1762 C  C   . CYS A 1 247 ? -1.172  -7.907  -9.862  1.00 19.99  ? 233 CYS A C   1 
ATOM   1763 O  O   . CYS A 1 247 ? -1.406  -7.346  -10.918 1.00 21.16  ? 233 CYS A O   1 
ATOM   1764 C  CB  . CYS A 1 247 ? 0.228   -9.911  -9.452  1.00 19.97  ? 233 CYS A CB  1 
ATOM   1765 S  SG  . CYS A 1 247 ? 1.531   -9.358  -10.586 1.00 22.20  ? 233 CYS A SG  1 
ATOM   1766 N  N   . TYR A 1 248 ? -0.900  -7.264  -8.723  1.00 19.33  ? 234 TYR A N   1 
ATOM   1767 C  CA  . TYR A 1 248 ? -0.754  -5.816  -8.692  1.00 19.56  ? 234 TYR A CA  1 
ATOM   1768 C  C   . TYR A 1 248 ? 0.567   -5.394  -9.332  1.00 21.72  ? 234 TYR A C   1 
ATOM   1769 O  O   . TYR A 1 248 ? 1.603   -6.033  -9.145  1.00 19.52  ? 234 TYR A O   1 
ATOM   1770 C  CB  . TYR A 1 248 ? -0.840  -5.305  -7.252  1.00 21.91  ? 234 TYR A CB  1 
ATOM   1771 C  CG  . TYR A 1 248 ? -2.248  -5.258  -6.738  1.00 26.70  ? 234 TYR A CG  1 
ATOM   1772 C  CD1 . TYR A 1 248 ? -2.980  -4.096  -6.913  1.00 37.68  ? 234 TYR A CD1 1 
ATOM   1773 C  CD2 . TYR A 1 248 ? -2.829  -6.303  -6.042  1.00 43.49  ? 234 TYR A CD2 1 
ATOM   1774 C  CE1 . TYR A 1 248 ? -4.278  -3.980  -6.460  1.00 52.50  ? 234 TYR A CE1 1 
ATOM   1775 C  CE2 . TYR A 1 248 ? -4.131  -6.200  -5.569  1.00 46.63  ? 234 TYR A CE2 1 
ATOM   1776 C  CZ  . TYR A 1 248 ? -4.849  -5.036  -5.788  1.00 61.06  ? 234 TYR A CZ  1 
ATOM   1777 O  OH  . TYR A 1 248 ? -6.123  -4.865  -5.363  1.00 61.11  ? 234 TYR A OH  1 
ATOM   1778 N  N   . ALA A 1 249 ? 0.539   -4.265  -10.062 1.00 20.64  ? 235 ALA A N   1 
ATOM   1779 C  CA  . ALA A 1 249 ? 1.748   -3.687  -10.635 1.00 21.32  ? 235 ALA A CA  1 
ATOM   1780 C  C   . ALA A 1 249 ? 2.750   -3.310  -9.551  1.00 20.97  ? 235 ALA A C   1 
ATOM   1781 O  O   . ALA A 1 249 ? 3.955   -3.280  -9.816  1.00 24.30  ? 235 ALA A O   1 
ATOM   1782 C  CB  . ALA A 1 249 ? 1.376   -2.494  -11.471 1.00 26.12  ? 235 ALA A CB  1 
ATOM   1783 N  N   . SER A 1 250 ? 2.254   -3.074  -8.324  1.00 19.77  ? 236 SER A N   1 
ATOM   1784 C  CA  . SER A 1 250 ? 3.121   -2.731  -7.215  1.00 18.66  ? 236 SER A CA  1 
ATOM   1785 C  C   . SER A 1 250 ? 3.699   -3.949  -6.509  1.00 19.34  ? 236 SER A C   1 
ATOM   1786 O  O   . SER A 1 250 ? 4.511   -3.763  -5.594  1.00 18.70  ? 236 SER A O   1 
ATOM   1787 C  CB  . SER A 1 250 ? 2.393   -1.885  -6.199  1.00 22.02  ? 236 SER A CB  1 
ATOM   1788 O  OG  . SER A 1 250 ? 1.169   -2.516  -5.824  1.00 23.99  ? 236 SER A OG  1 
ATOM   1789 N  N   . ASN A 1 251 ? 3.324   -5.181  -6.909  1.00 16.86  ? 237 ASN A N   1 
ATOM   1790 C  CA  . ASN A 1 251 ? 3.899   -6.355  -6.294  1.00 16.71  ? 237 ASN A CA  1 
ATOM   1791 C  C   . ASN A 1 251 ? 5.207   -6.684  -7.016  1.00 13.75  ? 237 ASN A C   1 
ATOM   1792 O  O   . ASN A 1 251 ? 5.300   -7.616  -7.837  1.00 14.92  ? 237 ASN A O   1 
ATOM   1793 C  CB  . ASN A 1 251 ? 2.900   -7.515  -6.286  1.00 16.40  ? 237 ASN A CB  1 
ATOM   1794 C  CG  . ASN A 1 251 ? 3.357   -8.660  -5.406  1.00 16.44  ? 237 ASN A CG  1 
ATOM   1795 O  OD1 . ASN A 1 251 ? 4.518   -8.785  -5.040  1.00 17.42  ? 237 ASN A OD1 1 
ATOM   1796 N  ND2 . ASN A 1 251 ? 2.443   -9.570  -5.095  1.00 21.54  ? 237 ASN A ND2 1 
ATOM   1797 N  N   . PHE A 1 252 ? 6.252   -5.922  -6.716  1.00 13.66  ? 238 PHE A N   1 
ATOM   1798 C  CA  . PHE A 1 252 ? 7.506   -6.043  -7.425  1.00 14.68  ? 238 PHE A CA  1 
ATOM   1799 C  C   . PHE A 1 252 ? 8.128   -7.405  -7.085  1.00 14.03  ? 238 PHE A C   1 
ATOM   1800 O  O   . PHE A 1 252 ? 8.812   -8.014  -7.910  1.00 16.28  ? 238 PHE A O   1 
ATOM   1801 C  CB  . PHE A 1 252 ? 8.490   -4.941  -7.025  1.00 16.78  ? 238 PHE A CB  1 
ATOM   1802 C  CG  . PHE A 1 252 ? 8.242   -3.570  -7.589  1.00 15.77  ? 238 PHE A CG  1 
ATOM   1803 C  CD1 . PHE A 1 252 ? 7.045   -3.211  -8.185  1.00 18.96  ? 238 PHE A CD1 1 
ATOM   1804 C  CD2 . PHE A 1 252 ? 9.273   -2.642  -7.566  1.00 17.87  ? 238 PHE A CD2 1 
ATOM   1805 C  CE1 . PHE A 1 252 ? 6.852   -1.919  -8.662  1.00 19.79  ? 238 PHE A CE1 1 
ATOM   1806 C  CE2 . PHE A 1 252 ? 9.082   -1.356  -8.054  1.00 19.66  ? 238 PHE A CE2 1 
ATOM   1807 C  CZ  . PHE A 1 252 ? 7.893   -1.010  -8.648  1.00 19.10  ? 238 PHE A CZ  1 
ATOM   1808 N  N   . VAL A 1 253 ? 7.907   -7.901  -5.867  1.00 14.10  ? 239 VAL A N   1 
ATOM   1809 C  CA  . VAL A 1 253 ? 8.431   -9.217  -5.501  1.00 14.96  ? 239 VAL A CA  1 
ATOM   1810 C  C   . VAL A 1 253 ? 7.898   -10.283 -6.448  1.00 16.09  ? 239 VAL A C   1 
ATOM   1811 O  O   . VAL A 1 253 ? 8.652   -11.107 -6.958  1.00 15.81  ? 239 VAL A O   1 
ATOM   1812 C  CB  . VAL A 1 253 ? 8.065   -9.576  -4.047  1.00 17.07  ? 239 VAL A CB  1 
ATOM   1813 C  CG1 . VAL A 1 253 ? 8.302   -11.030 -3.715  1.00 19.72  ? 239 VAL A CG1 1 
ATOM   1814 C  CG2 . VAL A 1 253 ? 8.818   -8.671  -3.073  1.00 18.78  ? 239 VAL A CG2 1 
ATOM   1815 N  N   . ARG A 1 254 ? 6.590   -10.303 -6.639  1.00 14.94  ? 240 ARG A N   1 
ATOM   1816 C  CA  . ARG A 1 254 ? 5.976   -11.310 -7.507  1.00 15.89  ? 240 ARG A CA  1 
ATOM   1817 C  C   . ARG A 1 254 ? 6.446   -11.146 -8.951  1.00 14.75  ? 240 ARG A C   1 
ATOM   1818 O  O   . ARG A 1 254 ? 6.712   -12.137 -9.676  1.00 15.67  ? 240 ARG A O   1 
ATOM   1819 C  CB  . ARG A 1 254 ? 4.460   -11.234 -7.346  1.00 15.49  ? 240 ARG A CB  1 
ATOM   1820 C  CG  . ARG A 1 254 ? 3.735   -12.469 -7.852  1.00 20.28  ? 240 ARG A CG  1 
ATOM   1821 C  CD  . ARG A 1 254 ? 3.824   -13.684 -6.938  1.00 19.72  ? 240 ARG A CD  1 
ATOM   1822 N  NE  . ARG A 1 254 ? 3.186   -13.644 -5.635  1.00 20.48  ? 240 ARG A NE  1 
ATOM   1823 C  CZ  . ARG A 1 254 ? 3.769   -13.635 -4.433  1.00 18.93  ? 240 ARG A CZ  1 
ATOM   1824 N  NH1 . ARG A 1 254 ? 5.083   -13.572 -4.263  1.00 18.30  ? 240 ARG A NH1 1 
ATOM   1825 N  NH2 . ARG A 1 254 ? 2.964   -13.613 -3.382  1.00 27.92  ? 240 ARG A NH2 1 
ATOM   1826 N  N   . ILE A 1 255 ? 6.513   -9.900  -9.414  1.00 13.95  ? 241 ILE A N   1 
ATOM   1827 C  CA  . ILE A 1 255 ? 6.959   -9.663  -10.776 1.00 15.40  ? 241 ILE A CA  1 
ATOM   1828 C  C   . ILE A 1 255 ? 8.372   -10.227 -10.959 1.00 14.75  ? 241 ILE A C   1 
ATOM   1829 O  O   . ILE A 1 255 ? 8.657   -10.919 -11.967 1.00 15.94  ? 241 ILE A O   1 
ATOM   1830 C  CB  . ILE A 1 255 ? 6.822   -8.178  -11.154 1.00 14.79  ? 241 ILE A CB  1 
ATOM   1831 C  CG1 . ILE A 1 255 ? 5.348   -7.764  -11.221 1.00 16.37  ? 241 ILE A CG1 1 
ATOM   1832 C  CG2 . ILE A 1 255 ? 7.561   -7.850  -12.443 1.00 18.06  ? 241 ILE A CG2 1 
ATOM   1833 C  CD1 . ILE A 1 255 ? 5.176   -6.264  -11.206 1.00 21.62  ? 241 ILE A CD1 1 
ATOM   1834 N  N   . GLN A 1 256 ? 9.276   -9.932  -10.028 1.00 14.71  ? 242 GLN A N   1 
ATOM   1835 C  CA  . GLN A 1 256 ? 10.636  -10.445 -10.102 1.00 16.11  ? 242 GLN A CA  1 
ATOM   1836 C  C   . GLN A 1 256 ? 10.651  -11.968 -10.143 1.00 15.26  ? 242 GLN A C   1 
ATOM   1837 O  O   . GLN A 1 256 ? 11.437  -12.558 -10.905 1.00 16.21  ? 242 GLN A O   1 
ATOM   1838 C  CB  . GLN A 1 256 ? 11.491  -9.914  -8.957  1.00 17.26  ? 242 GLN A CB  1 
ATOM   1839 C  CG  . GLN A 1 256 ? 12.942  -10.365 -9.026  1.00 19.00  ? 242 GLN A CG  1 
ATOM   1840 C  CD  . GLN A 1 256 ? 13.684  -9.760  -10.196 1.00 19.93  ? 242 GLN A CD  1 
ATOM   1841 O  OE1 . GLN A 1 256 ? 13.889  -8.551  -10.252 1.00 23.84  ? 242 GLN A OE1 1 
ATOM   1842 N  NE2 . GLN A 1 256 ? 14.084  -10.596 -11.150 1.00 24.65  ? 242 GLN A NE2 1 
ATOM   1843 N  N   . GLN A 1 257 ? 9.824   -12.607 -9.340  1.00 15.00  ? 243 GLN A N   1 
ATOM   1844 C  CA  . GLN A 1 257 ? 9.749   -14.040 -9.336  1.00 13.63  ? 243 GLN A CA  1 
ATOM   1845 C  C   . GLN A 1 257 ? 9.336   -14.550 -10.716 1.00 14.53  ? 243 GLN A C   1 
ATOM   1846 O  O   . GLN A 1 257 ? 9.896   -15.546 -11.221 1.00 16.56  ? 243 GLN A O   1 
ATOM   1847 C  CB  . GLN A 1 257 ? 8.801   -14.546 -8.251  1.00 15.20  ? 243 GLN A CB  1 
ATOM   1848 C  CG  . GLN A 1 257 ? 9.299   -14.289 -6.834  1.00 16.81  ? 243 GLN A CG  1 
ATOM   1849 C  CD  . GLN A 1 257 ? 8.216   -14.408 -5.795  1.00 17.15  ? 243 GLN A CD  1 
ATOM   1850 O  OE1 . GLN A 1 257 ? 7.038   -14.267 -6.122  1.00 16.49  ? 243 GLN A OE1 1 
ATOM   1851 N  NE2 . GLN A 1 257 ? 8.614   -14.721 -4.575  1.00 18.08  ? 243 GLN A NE2 1 
ATOM   1852 N  N   . VAL A 1 258 ? 8.311   -13.932 -11.320 1.00 14.61  ? 244 VAL A N   1 
ATOM   1853 C  CA  . VAL A 1 258 ? 7.848   -14.357 -12.632 1.00 15.34  ? 244 VAL A CA  1 
ATOM   1854 C  C   . VAL A 1 258 ? 8.960   -14.220 -13.664 1.00 15.24  ? 244 VAL A C   1 
ATOM   1855 O  O   . VAL A 1 258 ? 9.169   -15.136 -14.503 1.00 16.34  ? 244 VAL A O   1 
ATOM   1856 C  CB  . VAL A 1 258 ? 6.577   -13.609 -13.069 1.00 15.48  ? 244 VAL A CB  1 
ATOM   1857 C  CG1 . VAL A 1 258 ? 6.208   -13.934 -14.512 1.00 16.79  ? 244 VAL A CG1 1 
ATOM   1858 C  CG2 . VAL A 1 258 ? 5.400   -13.906 -12.153 1.00 16.83  ? 244 VAL A CG2 1 
ATOM   1859 N  N   . LEU A 1 259 ? 9.726   -13.133 -13.594 1.00 15.04  ? 245 LEU A N   1 
ATOM   1860 C  CA  . LEU A 1 259 ? 10.828  -12.917 -14.518 1.00 16.49  ? 245 LEU A CA  1 
ATOM   1861 C  C   . LEU A 1 259 ? 11.878  -14.014 -14.349 1.00 16.95  ? 245 LEU A C   1 
ATOM   1862 O  O   . LEU A 1 259 ? 12.364  -14.580 -15.336 1.00 18.97  ? 245 LEU A O   1 
ATOM   1863 C  CB  . LEU A 1 259 ? 11.511  -11.555 -14.325 1.00 18.09  ? 245 LEU A CB  1 
ATOM   1864 C  CG  . LEU A 1 259 ? 10.633  -10.322 -14.551 1.00 20.95  ? 245 LEU A CG  1 
ATOM   1865 C  CD1 . LEU A 1 259 ? 11.378  -9.057  -14.165 1.00 23.54  ? 245 LEU A CD1 1 
ATOM   1866 C  CD2 . LEU A 1 259 ? 10.195  -10.202 -15.995 1.00 25.08  ? 245 LEU A CD2 1 
ATOM   1867 N  N   . ASN A 1 260 ? 12.249  -14.300 -13.101 1.00 17.06  ? 246 ASN A N   1 
ATOM   1868 C  CA  . ASN A 1 260 ? 13.237  -15.336 -12.838 1.00 16.54  ? 246 ASN A CA  1 
ATOM   1869 C  C   . ASN A 1 260 ? 12.790  -16.669 -13.435 1.00 15.17  ? 246 ASN A C   1 
ATOM   1870 O  O   . ASN A 1 260 ? 13.561  -17.394 -14.064 1.00 17.99  ? 246 ASN A O   1 
ATOM   1871 C  CB  . ASN A 1 260 ? 13.429  -15.525 -11.333 1.00 18.35  ? 246 ASN A CB  1 
ATOM   1872 C  CG  . ASN A 1 260 ? 14.055  -14.347 -10.626 1.00 19.64  ? 246 ASN A CG  1 
ATOM   1873 O  OD1 . ASN A 1 260 ? 14.637  -13.458 -11.239 1.00 20.31  ? 246 ASN A OD1 1 
ATOM   1874 N  ND2 . ASN A 1 260 ? 14.031  -14.404 -9.305  1.00 22.86  ? 246 ASN A ND2 1 
ATOM   1875 N  N   . ILE A 1 261 ? 11.562  -17.050 -13.147 1.00 14.80  ? 247 ILE A N   1 
ATOM   1876 C  CA  . ILE A 1 261 ? 11.028  -18.340 -13.521 1.00 15.98  ? 247 ILE A CA  1 
ATOM   1877 C  C   . ILE A 1 261 ? 10.925  -18.412 -15.047 1.00 17.12  ? 247 ILE A C   1 
ATOM   1878 O  O   . ILE A 1 261 ? 11.217  -19.469 -15.617 1.00 16.98  ? 247 ILE A O   1 
ATOM   1879 C  CB  . ILE A 1 261 ? 9.703   -18.645 -12.808 1.00 15.64  ? 247 ILE A CB  1 
ATOM   1880 C  CG1 . ILE A 1 261 ? 9.946   -18.829 -11.316 1.00 16.15  ? 247 ILE A CG1 1 
ATOM   1881 C  CG2 . ILE A 1 261 ? 9.036   -19.869 -13.380 1.00 16.13  ? 247 ILE A CG2 1 
ATOM   1882 C  CD1 . ILE A 1 261 ? 8.684   -18.682 -10.469 1.00 18.74  ? 247 ILE A CD1 1 
ATOM   1883 N  N   . ALA A 1 262 ? 10.415  -17.349 -15.703 1.00 15.33  ? 248 ALA A N   1 
ATOM   1884 C  CA  . ALA A 1 262 ? 10.304  -17.322 -17.131 1.00 17.39  ? 248 ALA A CA  1 
ATOM   1885 C  C   . ALA A 1 262 ? 11.668  -17.645 -17.730 1.00 16.97  ? 248 ALA A C   1 
ATOM   1886 O  O   . ALA A 1 262 ? 11.764  -18.436 -18.670 1.00 17.59  ? 248 ALA A O   1 
ATOM   1887 C  CB  . ALA A 1 262 ? 9.833   -15.989 -17.581 1.00 16.10  ? 248 ALA A CB  1 
ATOM   1888 N  N   . SER A 1 263 ? 12.715  -16.989 -17.239 1.00 18.21  ? 249 SER A N   1 
ATOM   1889 C  CA  . SER A 1 263 ? 14.046  -17.184 -17.781 1.00 21.00  ? 249 SER A CA  1 
ATOM   1890 C  C   . SER A 1 263 ? 14.433  -18.662 -17.658 1.00 19.47  ? 249 SER A C   1 
ATOM   1891 O  O   . SER A 1 263 ? 14.998  -19.207 -18.601 1.00 23.19  ? 249 SER A O   1 
ATOM   1892 C  CB  . SER A 1 263 ? 15.034  -16.276 -17.106 1.00 27.70  ? 249 SER A CB  1 
ATOM   1893 O  OG  . SER A 1 263 ? 16.293  -16.313 -17.746 1.00 36.27  ? 249 SER A OG  1 
ATOM   1894 N  N   . GLN A 1 264 ? 14.111  -19.315 -16.517 1.00 17.88  ? 250 GLN A N   1 
ATOM   1895 C  CA  . GLN A 1 264 ? 14.461  -20.713 -16.292 1.00 20.65  ? 250 GLN A CA  1 
ATOM   1896 C  C   . GLN A 1 264 ? 13.657  -21.688 -17.150 1.00 19.73  ? 250 GLN A C   1 
ATOM   1897 O  O   . GLN A 1 264 ? 14.127  -22.806 -17.429 1.00 21.42  ? 250 GLN A O   1 
ATOM   1898 C  CB  . GLN A 1 264 ? 14.274  -21.055 -14.812 1.00 20.34  ? 250 GLN A CB  1 
ATOM   1899 C  CG  . GLN A 1 264 ? 15.204  -20.263 -13.912 1.00 28.26  ? 250 GLN A CG  1 
ATOM   1900 C  CD  . GLN A 1 264 ? 14.773  -20.217 -12.465 1.00 28.70  ? 250 GLN A CD  1 
ATOM   1901 O  OE1 . GLN A 1 264 ? 14.330  -21.197 -11.883 1.00 34.57  ? 250 GLN A OE1 1 
ATOM   1902 N  NE2 . GLN A 1 264 ? 14.940  -19.060 -11.851 1.00 39.48  ? 250 GLN A NE2 1 
ATOM   1903 N  N   . LEU A 1 265 ? 12.451  -21.280 -17.583 1.00 18.49  ? 251 LEU A N   1 
ATOM   1904 C  CA  . LEU A 1 265 ? 11.558  -22.151 -18.336 1.00 18.05  ? 251 LEU A CA  1 
ATOM   1905 C  C   . LEU A 1 265 ? 11.595  -21.797 -19.827 1.00 20.95  ? 251 LEU A C   1 
ATOM   1906 O  O   . LEU A 1 265 ? 10.786  -22.332 -20.577 1.00 26.46  ? 251 LEU A O   1 
ATOM   1907 C  CB  . LEU A 1 265 ? 10.119  -22.051 -17.805 1.00 17.90  ? 251 LEU A CB  1 
ATOM   1908 C  CG  . LEU A 1 265 ? 9.900   -22.582 -16.396 1.00 21.25  ? 251 LEU A CG  1 
ATOM   1909 C  CD1 . LEU A 1 265 ? 8.459   -22.346 -15.986 1.00 21.53  ? 251 LEU A CD1 1 
ATOM   1910 C  CD2 . LEU A 1 265 ? 10.258  -24.047 -16.314 1.00 18.79  ? 251 LEU A CD2 1 
ATOM   1911 N  N   . ASN A 1 266 ? 12.527  -20.920 -20.247 1.00 20.34  ? 252 ASN A N   1 
ATOM   1912 C  CA  . ASN A 1 266 ? 12.590  -20.441 -21.626 1.00 20.77  ? 252 ASN A CA  1 
ATOM   1913 C  C   . ASN A 1 266 ? 11.222  -19.930 -22.091 1.00 22.98  ? 252 ASN A C   1 
ATOM   1914 O  O   . ASN A 1 266 ? 10.811  -20.145 -23.237 1.00 26.47  ? 252 ASN A O   1 
ATOM   1915 C  CB  . ASN A 1 266 ? 13.253  -21.464 -22.555 1.00 26.88  ? 252 ASN A CB  1 
ATOM   1916 C  CG  . ASN A 1 266 ? 14.746  -21.649 -22.315 1.00 21.80  ? 252 ASN A CG  1 
ATOM   1917 O  OD1 . ASN A 1 266 ? 15.508  -20.692 -22.154 1.00 32.68  ? 252 ASN A OD1 1 
ATOM   1918 N  ND2 . ASN A 1 266 ? 15.207  -22.885 -22.317 1.00 29.29  ? 252 ASN A ND2 1 
ATOM   1919 N  N   . ARG A 1 267 ? 10.596  -19.113 -21.239 1.00 23.01  ? 253 ARG A N   1 
ATOM   1920 C  CA  . ARG A 1 267 ? 9.422   -18.356 -21.617 1.00 21.47  ? 253 ARG A CA  1 
ATOM   1921 C  C   . ARG A 1 267 ? 9.787   -16.874 -21.676 1.00 20.38  ? 253 ARG A C   1 
ATOM   1922 O  O   . ARG A 1 267 ? 10.629  -16.379 -20.933 1.00 22.22  ? 253 ARG A O   1 
ATOM   1923 C  CB  . ARG A 1 267 ? 8.246   -18.593 -20.664 1.00 21.32  ? 253 ARG A CB  1 
ATOM   1924 C  CG  . ARG A 1 267 ? 7.607   -19.972 -20.681 1.00 19.94  ? 253 ARG A CG  1 
ATOM   1925 C  CD  . ARG A 1 267 ? 6.377   -20.045 -19.777 1.00 22.25  ? 253 ARG A CD  1 
ATOM   1926 N  NE  . ARG A 1 267 ? 5.678   -21.325 -19.754 1.00 22.47  ? 253 ARG A NE  1 
ATOM   1927 C  CZ  . ARG A 1 267 ? 4.503   -21.616 -20.339 1.00 19.97  ? 253 ARG A CZ  1 
ATOM   1928 N  NH1 . ARG A 1 267 ? 3.752   -20.676 -20.898 1.00 20.58  ? 253 ARG A NH1 1 
ATOM   1929 N  NH2 . ARG A 1 267 ? 4.047   -22.853 -20.294 1.00 22.12  ? 253 ARG A NH2 1 
ATOM   1930 N  N   . LYS A 1 268 ? 9.140   -16.173 -22.619 1.00 19.95  ? 254 LYS A N   1 
ATOM   1931 C  CA  . LYS A 1 268 ? 9.149   -14.729 -22.673 1.00 20.20  ? 254 LYS A CA  1 
ATOM   1932 C  C   . LYS A 1 268 ? 8.087   -14.206 -21.702 1.00 18.91  ? 254 LYS A C   1 
ATOM   1933 O  O   . LYS A 1 268 ? 7.099   -14.899 -21.431 1.00 21.17  ? 254 LYS A O   1 
ATOM   1934 C  CB  . LYS A 1 268 ? 8.892   -14.227 -24.095 1.00 21.98  ? 254 LYS A CB  1 
ATOM   1935 C  CG  . LYS A 1 268 ? 9.850   -14.745 -25.155 1.00 24.86  ? 254 LYS A CG  1 
ATOM   1936 C  CD  . LYS A 1 268 ? 11.261  -14.296 -24.955 1.00 25.01  ? 254 LYS A CD  1 
ATOM   1937 C  CE  . LYS A 1 268 ? 12.136  -14.477 -26.176 1.00 31.96  ? 254 LYS A CE  1 
ATOM   1938 N  NZ  . LYS A 1 268 ? 13.490  -13.949 -25.914 1.00 41.71  ? 254 LYS A NZ  1 
ATOM   1939 N  N   . VAL A 1 269 ? 8.269   -12.932 -21.365 1.00 19.58  ? 255 VAL A N   1 
ATOM   1940 C  CA  . VAL A 1 269 ? 7.329   -12.230 -20.493 1.00 19.33  ? 255 VAL A CA  1 
ATOM   1941 C  C   . VAL A 1 269 ? 6.813   -11.006 -21.234 1.00 20.00  ? 255 VAL A C   1 
ATOM   1942 O  O   . VAL A 1 269 ? 7.607   -10.239 -21.779 1.00 20.29  ? 255 VAL A O   1 
ATOM   1943 C  CB  . VAL A 1 269 ? 7.947   -11.848 -19.134 1.00 18.47  ? 255 VAL A CB  1 
ATOM   1944 C  CG1 . VAL A 1 269 ? 6.998   -11.013 -18.296 1.00 19.08  ? 255 VAL A CG1 1 
ATOM   1945 C  CG2 . VAL A 1 269 ? 8.369   -13.100 -18.367 1.00 19.97  ? 255 VAL A CG2 1 
ATOM   1946 N  N   . SER A 1 270 ? 5.492   -10.781 -21.156 1.00 19.09  ? 256 SER A N   1 
ATOM   1947 C  CA  . SER A 1 270 ? 4.934   -9.549  -21.675 1.00 20.51  ? 256 SER A CA  1 
ATOM   1948 C  C   . SER A 1 270 ? 3.958   -8.962  -20.669 1.00 17.10  ? 256 SER A C   1 
ATOM   1949 O  O   . SER A 1 270 ? 3.197   -9.696  -20.071 1.00 20.32  ? 256 SER A O   1 
ATOM   1950 C  CB  . SER A 1 270 ? 4.282   -9.838  -22.980 1.00 27.98  ? 256 SER A CB  1 
ATOM   1951 O  OG  . SER A 1 270 ? 4.063   -8.614  -23.651 1.00 24.86  ? 256 SER A OG  1 
ATOM   1952 N  N   . PHE A 1 271 ? 3.969   -7.629  -20.567 1.00 19.32  ? 257 PHE A N   1 
ATOM   1953 C  CA  . PHE A 1 271 ? 3.071   -6.903  -19.696 1.00 19.71  ? 257 PHE A CA  1 
ATOM   1954 C  C   . PHE A 1 271 ? 1.813   -6.461  -20.437 1.00 19.55  ? 257 PHE A C   1 
ATOM   1955 O  O   . PHE A 1 271 ? 1.877   -5.883  -21.518 1.00 21.88  ? 257 PHE A O   1 
ATOM   1956 C  CB  . PHE A 1 271 ? 3.817   -5.699  -19.146 1.00 22.62  ? 257 PHE A CB  1 
ATOM   1957 C  CG  . PHE A 1 271 ? 4.866   -6.082  -18.142 1.00 26.71  ? 257 PHE A CG  1 
ATOM   1958 C  CD1 . PHE A 1 271 ? 6.209   -6.153  -18.465 1.00 36.55  ? 257 PHE A CD1 1 
ATOM   1959 C  CD2 . PHE A 1 271 ? 4.492   -6.289  -16.815 1.00 34.86  ? 257 PHE A CD2 1 
ATOM   1960 C  CE1 . PHE A 1 271 ? 7.152   -6.474  -17.493 1.00 33.29  ? 257 PHE A CE1 1 
ATOM   1961 C  CE2 . PHE A 1 271 ? 5.439   -6.601  -15.854 1.00 38.29  ? 257 PHE A CE2 1 
ATOM   1962 C  CZ  . PHE A 1 271 ? 6.765   -6.690  -16.200 1.00 38.38  ? 257 PHE A CZ  1 
ATOM   1963 N  N   . LEU A 1 272 ? 0.672   -6.767  -19.820 1.00 20.88  ? 258 LEU A N   1 
ATOM   1964 C  CA  . LEU A 1 272 ? -0.625  -6.231  -20.195 1.00 25.24  ? 258 LEU A CA  1 
ATOM   1965 C  C   . LEU A 1 272 ? -1.121  -5.287  -19.091 1.00 25.81  ? 258 LEU A C   1 
ATOM   1966 O  O   . LEU A 1 272 ? -1.439  -5.716  -17.973 1.00 29.34  ? 258 LEU A O   1 
ATOM   1967 C  CB  . LEU A 1 272 ? -1.576  -7.408  -20.367 1.00 21.07  ? 258 LEU A CB  1 
ATOM   1968 C  CG  . LEU A 1 272 ? -2.931  -7.076  -20.972 1.00 22.20  ? 258 LEU A CG  1 
ATOM   1969 C  CD1 . LEU A 1 272 ? -2.772  -6.545  -22.385 1.00 29.47  ? 258 LEU A CD1 1 
ATOM   1970 C  CD2 . LEU A 1 272 ? -3.813  -8.315  -20.954 1.00 29.95  ? 258 LEU A CD2 1 
ATOM   1971 N  N   . GLY A 1 273 ? -1.140  -3.988  -19.389 1.00 30.11  ? 259 GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 273 ? -1.557  -2.976  -18.426 1.00 34.49  ? 259 GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 273 ? -0.759  -1.684  -18.584 1.00 47.89  ? 259 GLY A C   1 
ATOM   1974 O  O   . GLY A 1 273 ? 0.271   -1.665  -19.257 1.00 67.56  ? 259 GLY A O   1 
ATOM   1975 N  N   . ARG A 1 274 ? -1.250  -0.616  -17.940 1.00 52.22  ? 260 ARG A N   1 
ATOM   1976 C  CA  . ARG A 1 274 ? -0.825  0.758   -18.199 1.00 42.03  ? 260 ARG A CA  1 
ATOM   1977 C  C   . ARG A 1 274 ? 0.699   0.903   -18.078 1.00 39.81  ? 260 ARG A C   1 
ATOM   1978 O  O   . ARG A 1 274 ? 1.139   1.397   -17.019 1.00 40.53  ? 260 ARG A O   1 
ATOM   1979 C  CB  . ARG A 1 274 ? -1.525  1.721   -17.233 1.00 51.49  ? 260 ARG A CB  1 
ATOM   1980 N  N   . GLU A 1 277 ? 4.767   -1.382  -18.617 1.00 89.16  ? 263 GLU A N   1 
ATOM   1981 C  CA  . GLU A 1 277 ? 4.176   -0.721  -17.420 1.00 129.03 ? 263 GLU A CA  1 
ATOM   1982 C  C   . GLU A 1 277 ? 4.906   0.593   -17.160 1.00 114.62 ? 263 GLU A C   1 
ATOM   1983 O  O   . GLU A 1 277 ? 6.111   0.690   -17.428 1.00 37.56  ? 263 GLU A O   1 
ATOM   1984 C  CB  . GLU A 1 277 ? 4.378   -1.592  -16.185 1.00 82.17  ? 263 GLU A CB  1 
ATOM   1985 C  CG  . GLU A 1 277 ? 3.141   -1.758  -15.317 1.00 99.21  ? 263 GLU A CG  1 
ATOM   1986 C  CD  . GLU A 1 277 ? 2.503   -3.130  -15.454 1.00 78.97  ? 263 GLU A CD  1 
ATOM   1987 O  OE1 . GLU A 1 277 ? 3.205   -4.147  -15.204 1.00 87.56  ? 263 GLU A OE1 1 
ATOM   1988 O  OE2 . GLU A 1 277 ? 1.309   -3.186  -15.815 1.00 92.12  ? 263 GLU A OE2 1 
ATOM   1989 N  N   . SER A 1 278 ? 4.151   1.582   -16.658 1.00 94.37  ? 264 SER A N   1 
ATOM   1990 C  CA  . SER A 1 278 ? 4.704   2.811   -16.115 1.00 75.36  ? 264 SER A CA  1 
ATOM   1991 C  C   . SER A 1 278 ? 5.569   2.494   -14.890 1.00 46.75  ? 264 SER A C   1 
ATOM   1992 O  O   . SER A 1 278 ? 6.748   2.845   -14.862 1.00 32.37  ? 264 SER A O   1 
ATOM   1993 C  CB  . SER A 1 278 ? 3.593   3.789   -15.807 1.00 42.36  ? 264 SER A CB  1 
ATOM   1994 N  N   . SER A 1 279 ? 4.994   1.797   -13.896 1.00 35.68  ? 265 SER A N   1 
ATOM   1995 C  CA  . SER A 1 279 ? 5.702   1.454   -12.664 1.00 31.78  ? 265 SER A CA  1 
ATOM   1996 C  C   . SER A 1 279 ? 6.988   0.692   -12.983 1.00 26.54  ? 265 SER A C   1 
ATOM   1997 O  O   . SER A 1 279 ? 8.023   0.955   -12.400 1.00 28.39  ? 265 SER A O   1 
ATOM   1998 C  CB  . SER A 1 279 ? 4.822   0.664   -11.699 1.00 29.89  ? 265 SER A CB  1 
ATOM   1999 N  N   . PHE A 1 280 ? 6.949   -0.233  -13.939 1.00 28.31  ? 266 PHE A N   1 
ATOM   2000 C  CA  . PHE A 1 280 ? 8.117   -1.060  -14.193 1.00 25.69  ? 266 PHE A CA  1 
ATOM   2001 C  C   . PHE A 1 280 ? 9.228   -0.246  -14.838 1.00 31.90  ? 266 PHE A C   1 
ATOM   2002 O  O   . PHE A 1 280 ? 10.405  -0.428  -14.523 1.00 29.36  ? 266 PHE A O   1 
ATOM   2003 C  CB  . PHE A 1 280 ? 7.765   -2.211  -15.141 1.00 27.55  ? 266 PHE A CB  1 
ATOM   2004 C  CG  . PHE A 1 280 ? 8.857   -3.235  -15.279 1.00 32.09  ? 266 PHE A CG  1 
ATOM   2005 C  CD1 . PHE A 1 280 ? 9.699   -3.240  -16.383 1.00 29.13  ? 266 PHE A CD1 1 
ATOM   2006 C  CD2 . PHE A 1 280 ? 8.995   -4.221  -14.314 1.00 26.61  ? 266 PHE A CD2 1 
ATOM   2007 C  CE1 . PHE A 1 280 ? 10.684  -4.209  -16.498 1.00 30.64  ? 266 PHE A CE1 1 
ATOM   2008 C  CE2 . PHE A 1 280 ? 9.991   -5.175  -14.421 1.00 30.86  ? 266 PHE A CE2 1 
ATOM   2009 C  CZ  . PHE A 1 280 ? 10.828  -5.170  -15.511 1.00 27.27  ? 266 PHE A CZ  1 
ATOM   2010 N  N   . ASN A 1 281 ? 8.829   0.618   -15.780 1.00 32.73  ? 267 ASN A N   1 
ATOM   2011 C  CA  . ASN A 1 281 ? 9.776   1.417   -16.537 1.00 31.94  ? 267 ASN A CA  1 
ATOM   2012 C  C   . ASN A 1 281 ? 10.525  2.328   -15.563 1.00 28.40  ? 267 ASN A C   1 
ATOM   2013 O  O   . ASN A 1 281 ? 11.759  2.393   -15.585 1.00 31.22  ? 267 ASN A O   1 
ATOM   2014 C  CB  . ASN A 1 281 ? 9.064   2.156   -17.680 1.00 39.26  ? 267 ASN A CB  1 
ATOM   2015 C  CG  . ASN A 1 281 ? 9.824   2.097   -18.990 1.00 59.63  ? 267 ASN A CG  1 
ATOM   2016 O  OD1 . ASN A 1 281 ? 10.964  1.638   -19.036 1.00 77.52  ? 267 ASN A OD1 1 
ATOM   2017 N  ND2 . ASN A 1 281 ? 9.194   2.539   -20.068 1.00 67.53  ? 267 ASN A ND2 1 
ATOM   2018 N  N   . ILE A 1 282 ? 9.772   2.965   -14.651 1.00 30.85  ? 268 ILE A N   1 
ATOM   2019 C  CA  . ILE A 1 282 ? 10.360  3.854   -13.666 1.00 35.78  ? 268 ILE A CA  1 
ATOM   2020 C  C   . ILE A 1 282 ? 11.278  3.058   -12.744 1.00 22.86  ? 268 ILE A C   1 
ATOM   2021 O  O   . ILE A 1 282 ? 12.375  3.499   -12.447 1.00 26.69  ? 268 ILE A O   1 
ATOM   2022 C  CB  . ILE A 1 282 ? 9.267   4.632   -12.902 1.00 32.39  ? 268 ILE A CB  1 
ATOM   2023 C  CG1 . ILE A 1 282 ? 8.695   5.771   -13.754 1.00 33.62  ? 268 ILE A CG1 1 
ATOM   2024 C  CG2 . ILE A 1 282 ? 9.781   5.157   -11.572 1.00 39.54  ? 268 ILE A CG2 1 
ATOM   2025 C  CD1 . ILE A 1 282 ? 7.249   5.609   -14.124 1.00 47.11  ? 268 ILE A CD1 1 
ATOM   2026 N  N   . ALA A 1 283 ? 10.804  1.918   -12.214 1.00 21.97  ? 269 ALA A N   1 
ATOM   2027 C  CA  . ALA A 1 283 ? 11.607  1.151   -11.285 1.00 25.65  ? 269 ALA A CA  1 
ATOM   2028 C  C   . ALA A 1 283 ? 12.856  0.572   -11.967 1.00 22.43  ? 269 ALA A C   1 
ATOM   2029 O  O   . ALA A 1 283 ? 13.882  0.475   -11.315 1.00 26.37  ? 269 ALA A O   1 
ATOM   2030 C  CB  . ALA A 1 283 ? 10.752  0.099   -10.624 1.00 24.66  ? 269 ALA A CB  1 
ATOM   2031 N  N   . ARG A 1 284 ? 12.744  0.095   -13.215 1.00 29.51  ? 270 ARG A N   1 
ATOM   2032 C  CA  . ARG A 1 284 ? 13.884  -0.466  -13.939 1.00 30.84  ? 270 ARG A CA  1 
ATOM   2033 C  C   . ARG A 1 284 ? 14.983  0.592   -14.081 1.00 31.50  ? 270 ARG A C   1 
ATOM   2034 O  O   . ARG A 1 284 ? 16.146  0.306   -13.782 1.00 33.04  ? 270 ARG A O   1 
ATOM   2035 C  CB  . ARG A 1 284 ? 13.443  -0.998  -15.308 1.00 39.45  ? 270 ARG A CB  1 
ATOM   2036 N  N   . LYS A 1 285 ? 14.595  1.826   -14.469 1.00 33.02  ? 271 LYS A N   1 
ATOM   2037 C  CA  . LYS A 1 285 ? 15.539  2.910   -14.710 1.00 40.44  ? 271 LYS A CA  1 
ATOM   2038 C  C   . LYS A 1 285 ? 16.238  3.301   -13.408 1.00 34.11  ? 271 LYS A C   1 
ATOM   2039 O  O   . LYS A 1 285 ? 17.364  3.788   -13.429 1.00 46.49  ? 271 LYS A O   1 
ATOM   2040 C  CB  . LYS A 1 285 ? 14.825  4.120   -15.325 1.00 41.87  ? 271 LYS A CB  1 
ATOM   2041 N  N   . MET A 1 286 ? 15.561  3.097   -12.264 1.00 31.03  ? 272 MET A N   1 
ATOM   2042 C  CA  . MET A 1 286 ? 16.152  3.421   -10.984 1.00 30.88  ? 272 MET A CA  1 
ATOM   2043 C  C   . MET A 1 286 ? 16.909  2.221   -10.424 1.00 29.59  ? 272 MET A C   1 
ATOM   2044 O  O   . MET A 1 286 ? 17.517  2.317   -9.369  1.00 37.43  ? 272 MET A O   1 
ATOM   2045 C  CB  . MET A 1 286 ? 15.043  3.889   -10.029 1.00 32.45  ? 272 MET A CB  1 
ATOM   2046 C  CG  . MET A 1 286 ? 14.255  5.094   -10.575 1.00 32.74  ? 272 MET A CG  1 
ATOM   2047 S  SD  . MET A 1 286 ? 12.974  5.762   -9.464  1.00 37.41  ? 272 MET A SD  1 
ATOM   2048 C  CE  . MET A 1 286 ? 13.675  5.098   -7.964  1.00 22.62  ? 272 MET A CE  1 
ATOM   2049 N  N   . GLY A 1 287 ? 16.877  1.085   -11.137 1.00 29.46  ? 273 GLY A N   1 
ATOM   2050 C  CA  . GLY A 1 287 ? 17.725  -0.053  -10.832 1.00 29.93  ? 273 GLY A CA  1 
ATOM   2051 C  C   . GLY A 1 287 ? 17.066  -1.127  -9.967  1.00 31.94  ? 273 GLY A C   1 
ATOM   2052 O  O   . GLY A 1 287 ? 17.786  -1.951  -9.434  1.00 29.61  ? 273 GLY A O   1 
ATOM   2053 N  N   . TYR A 1 288 ? 15.722  -1.152  -9.834  1.00 27.98  ? 274 TYR A N   1 
ATOM   2054 C  CA  . TYR A 1 288 ? 15.083  -2.053  -8.873  1.00 30.82  ? 274 TYR A CA  1 
ATOM   2055 C  C   . TYR A 1 288 ? 14.858  -3.482  -9.386  1.00 29.55  ? 274 TYR A C   1 
ATOM   2056 O  O   . TYR A 1 288 ? 14.449  -4.341  -8.609  1.00 30.92  ? 274 TYR A O   1 
ATOM   2057 C  CB  . TYR A 1 288 ? 13.743  -1.494  -8.398  1.00 22.00  ? 274 TYR A CB  1 
ATOM   2058 C  CG  . TYR A 1 288 ? 13.881  -0.386  -7.388  1.00 27.03  ? 274 TYR A CG  1 
ATOM   2059 C  CD1 . TYR A 1 288 ? 14.293  -0.647  -6.082  1.00 30.65  ? 274 TYR A CD1 1 
ATOM   2060 C  CD2 . TYR A 1 288 ? 13.686  0.926   -7.767  1.00 29.76  ? 274 TYR A CD2 1 
ATOM   2061 C  CE1 . TYR A 1 288 ? 14.434  0.372   -5.158  1.00 34.46  ? 274 TYR A CE1 1 
ATOM   2062 C  CE2 . TYR A 1 288 ? 13.824  1.958   -6.850  1.00 30.21  ? 274 TYR A CE2 1 
ATOM   2063 C  CZ  . TYR A 1 288 ? 14.229  1.678   -5.564  1.00 33.50  ? 274 TYR A CZ  1 
ATOM   2064 O  OH  . TYR A 1 288 ? 14.329  2.761   -4.726  1.00 58.17  ? 274 TYR A OH  1 
ATOM   2065 N  N   . PHE A 1 289 ? 15.064  -3.766  -10.672 1.00 30.15  ? 275 PHE A N   1 
ATOM   2066 C  CA  . PHE A 1 289 ? 14.771  -5.113  -11.162 1.00 25.45  ? 275 PHE A CA  1 
ATOM   2067 C  C   . PHE A 1 289 ? 15.985  -5.805  -11.774 1.00 35.37  ? 275 PHE A C   1 
ATOM   2068 O  O   . PHE A 1 289 ? 16.794  -5.143  -12.425 1.00 32.02  ? 275 PHE A O   1 
ATOM   2069 C  CB  . PHE A 1 289 ? 13.688  -5.053  -12.229 1.00 24.43  ? 275 PHE A CB  1 
ATOM   2070 C  CG  . PHE A 1 289 ? 12.309  -4.954  -11.648 1.00 21.58  ? 275 PHE A CG  1 
ATOM   2071 C  CD1 . PHE A 1 289 ? 11.666  -6.086  -11.173 1.00 22.91  ? 275 PHE A CD1 1 
ATOM   2072 C  CD2 . PHE A 1 289 ? 11.671  -3.725  -11.534 1.00 22.44  ? 275 PHE A CD2 1 
ATOM   2073 C  CE1 . PHE A 1 289 ? 10.404  -5.990  -10.610 1.00 23.66  ? 275 PHE A CE1 1 
ATOM   2074 C  CE2 . PHE A 1 289 ? 10.415  -3.647  -10.961 1.00 23.44  ? 275 PHE A CE2 1 
ATOM   2075 C  CZ  . PHE A 1 289 ? 9.771   -4.788  -10.574 1.00 20.44  ? 275 PHE A CZ  1 
ATOM   2076 N  N   . ASP A 1 290 ? 16.026  -7.150  -11.650 1.00 29.27  ? 276 ASP A N   1 
ATOM   2077 C  CA  . ASP A 1 290 ? 17.050  -7.966  -12.293 1.00 37.79  ? 276 ASP A CA  1 
ATOM   2078 C  C   . ASP A 1 290 ? 16.423  -8.625  -13.528 1.00 33.34  ? 276 ASP A C   1 
ATOM   2079 O  O   . ASP A 1 290 ? 15.695  -9.595  -13.394 1.00 32.81  ? 276 ASP A O   1 
ATOM   2080 C  CB  . ASP A 1 290 ? 17.618  -8.988  -11.290 1.00 42.31  ? 276 ASP A CB  1 
ATOM   2081 C  CG  . ASP A 1 290 ? 18.734  -9.863  -11.828 1.00 54.54  ? 276 ASP A CG  1 
ATOM   2082 O  OD1 . ASP A 1 290 ? 19.904  -9.439  -11.743 1.00 81.19  ? 276 ASP A OD1 1 
ATOM   2083 O  OD2 . ASP A 1 290 ? 18.420  -10.955 -12.335 1.00 76.44  ? 276 ASP A OD2 1 
ATOM   2084 N  N   . ILE A 1 291 ? 16.709  -8.111  -14.735 1.00 33.64  ? 277 ILE A N   1 
ATOM   2085 C  CA  . ILE A 1 291 ? 15.984  -8.521  -15.933 1.00 33.85  ? 277 ILE A CA  1 
ATOM   2086 C  C   . ILE A 1 291 ? 16.956  -9.127  -16.933 1.00 40.99  ? 277 ILE A C   1 
ATOM   2087 O  O   . ILE A 1 291 ? 17.813  -8.413  -17.445 1.00 40.06  ? 277 ILE A O   1 
ATOM   2088 C  CB  . ILE A 1 291 ? 15.250  -7.342  -16.605 1.00 42.14  ? 277 ILE A CB  1 
ATOM   2089 C  CG1 . ILE A 1 291 ? 14.397  -6.544  -15.623 1.00 49.10  ? 277 ILE A CG1 1 
ATOM   2090 C  CG2 . ILE A 1 291 ? 14.440  -7.814  -17.808 1.00 42.63  ? 277 ILE A CG2 1 
ATOM   2091 C  CD1 . ILE A 1 291 ? 14.162  -5.126  -16.078 1.00 56.49  ? 277 ILE A CD1 1 
ATOM   2092 N  N   . PRO A 1 292 ? 16.835  -10.434 -17.264 1.00 41.42  ? 278 PRO A N   1 
ATOM   2093 C  CA  . PRO A 1 292 ? 17.567  -11.012 -18.397 1.00 46.25  ? 278 PRO A CA  1 
ATOM   2094 C  C   . PRO A 1 292 ? 17.335  -10.245 -19.702 1.00 50.74  ? 278 PRO A C   1 
ATOM   2095 O  O   . PRO A 1 292 ? 16.238  -9.752  -19.945 1.00 57.84  ? 278 PRO A O   1 
ATOM   2096 C  CB  . PRO A 1 292 ? 17.008  -12.441 -18.496 1.00 49.95  ? 278 PRO A CB  1 
ATOM   2097 C  CG  . PRO A 1 292 ? 16.492  -12.758 -17.105 1.00 54.01  ? 278 PRO A CG  1 
ATOM   2098 C  CD  . PRO A 1 292 ? 16.054  -11.432 -16.516 1.00 47.55  ? 278 PRO A CD  1 
ATOM   2099 N  N   . LYS A 1 293 ? 18.380  -10.125 -20.534 1.00 48.36  ? 279 LYS A N   1 
ATOM   2100 C  CA  . LYS A 1 293 ? 18.242  -9.567  -21.874 1.00 48.98  ? 279 LYS A CA  1 
ATOM   2101 C  C   . LYS A 1 293 ? 17.376  -10.515 -22.706 1.00 42.48  ? 279 LYS A C   1 
ATOM   2102 O  O   . LYS A 1 293 ? 17.430  -11.731 -22.517 1.00 47.09  ? 279 LYS A O   1 
ATOM   2103 C  CB  . LYS A 1 293 ? 19.621  -9.339  -22.515 1.00 48.99  ? 279 LYS A CB  1 
ATOM   2104 N  N   . ASP A 1 294 ? 16.545  -9.942  -23.593 1.00 37.70  ? 280 ASP A N   1 
ATOM   2105 C  CA  . ASP A 1 294 ? 15.690  -10.698 -24.500 1.00 36.33  ? 280 ASP A CA  1 
ATOM   2106 C  C   . ASP A 1 294 ? 14.527  -11.375 -23.763 1.00 33.29  ? 280 ASP A C   1 
ATOM   2107 O  O   . ASP A 1 294 ? 13.824  -12.172 -24.377 1.00 37.00  ? 280 ASP A O   1 
ATOM   2108 C  CB  . ASP A 1 294 ? 16.492  -11.727 -25.312 1.00 40.95  ? 280 ASP A CB  1 
ATOM   2109 N  N   . LEU A 1 295 ? 14.266  -11.048 -22.487 1.00 29.95  ? 281 LEU A N   1 
ATOM   2110 C  CA  . LEU A 1 295 ? 13.196  -11.729 -21.761 1.00 24.67  ? 281 LEU A CA  1 
ATOM   2111 C  C   . LEU A 1 295 ? 11.838  -11.095 -22.079 1.00 21.21  ? 281 LEU A C   1 
ATOM   2112 O  O   . LEU A 1 295 ? 10.848  -11.799 -22.338 1.00 23.86  ? 281 LEU A O   1 
ATOM   2113 C  CB  . LEU A 1 295 ? 13.490  -11.688 -20.257 1.00 28.77  ? 281 LEU A CB  1 
ATOM   2114 C  CG  . LEU A 1 295 ? 12.438  -12.366 -19.377 1.00 28.72  ? 281 LEU A CG  1 
ATOM   2115 C  CD1 . LEU A 1 295 ? 12.266  -13.823 -19.736 1.00 24.33  ? 281 LEU A CD1 1 
ATOM   2116 C  CD2 . LEU A 1 295 ? 12.799  -12.247 -17.917 1.00 31.49  ? 281 LEU A CD2 1 
ATOM   2117 N  N   . LEU A 1 296 ? 11.832  -9.747  -22.070 1.00 22.81  ? 282 LEU A N   1 
ATOM   2118 C  CA  . LEU A 1 296 ? 10.603  -8.978  -22.230 1.00 25.56  ? 282 LEU A CA  1 
ATOM   2119 C  C   . LEU A 1 296 ? 10.303  -8.834  -23.716 1.00 31.50  ? 282 LEU A C   1 
ATOM   2120 O  O   . LEU A 1 296 ? 11.215  -8.605  -24.509 1.00 34.41  ? 282 LEU A O   1 
ATOM   2121 C  CB  . LEU A 1 296 ? 10.774  -7.593  -21.605 1.00 30.31  ? 282 LEU A CB  1 
ATOM   2122 C  CG  . LEU A 1 296 ? 10.868  -7.571  -20.092 1.00 28.29  ? 282 LEU A CG  1 
ATOM   2123 C  CD1 . LEU A 1 296 ? 10.756  -6.142  -19.593 1.00 34.56  ? 282 LEU A CD1 1 
ATOM   2124 C  CD2 . LEU A 1 296 ? 9.781   -8.432  -19.467 1.00 32.38  ? 282 LEU A CD2 1 
ATOM   2125 N  N   . ILE A 1 297 ? 9.017   -8.946  -24.058 1.00 24.77  ? 283 ILE A N   1 
ATOM   2126 C  CA  . ILE A 1 297 ? 8.523   -8.728  -25.401 1.00 29.39  ? 283 ILE A CA  1 
ATOM   2127 C  C   . ILE A 1 297 ? 7.309   -7.805  -25.309 1.00 31.71  ? 283 ILE A C   1 
ATOM   2128 O  O   . ILE A 1 297 ? 6.618   -7.806  -24.293 1.00 26.19  ? 283 ILE A O   1 
ATOM   2129 C  CB  . ILE A 1 297 ? 8.204   -10.061 -26.113 1.00 26.88  ? 283 ILE A CB  1 
ATOM   2130 C  CG1 . ILE A 1 297 ? 7.123   -10.873 -25.400 1.00 36.15  ? 283 ILE A CG1 1 
ATOM   2131 C  CG2 . ILE A 1 297 ? 9.480   -10.868 -26.325 1.00 32.02  ? 283 ILE A CG2 1 
ATOM   2132 C  CD1 . ILE A 1 297 ? 6.586   -12.016 -26.211 1.00 29.38  ? 283 ILE A CD1 1 
ATOM   2133 N  N   . PRO A 1 298 ? 7.053   -6.960  -26.337 1.00 36.16  ? 284 PRO A N   1 
ATOM   2134 C  CA  . PRO A 1 298 ? 5.796   -6.228  -26.465 1.00 49.05  ? 284 PRO A CA  1 
ATOM   2135 C  C   . PRO A 1 298 ? 4.624   -7.185  -26.632 1.00 61.55  ? 284 PRO A C   1 
ATOM   2136 O  O   . PRO A 1 298 ? 4.724   -8.250  -27.243 1.00 44.98  ? 284 PRO A O   1 
ATOM   2137 C  CB  . PRO A 1 298 ? 5.942   -5.358  -27.729 1.00 66.92  ? 284 PRO A CB  1 
ATOM   2138 C  CG  . PRO A 1 298 ? 7.398   -5.443  -28.120 1.00 47.45  ? 284 PRO A CG  1 
ATOM   2139 C  CD  . PRO A 1 298 ? 7.977   -6.670  -27.444 1.00 35.42  ? 284 PRO A CD  1 
ATOM   2140 N  N   . ILE A 1 299 ? 3.468   -6.741  -26.145 1.00 50.71  ? 285 ILE A N   1 
ATOM   2141 C  CA  . ILE A 1 299 ? 2.281   -7.572  -26.081 1.00 42.73  ? 285 ILE A CA  1 
ATOM   2142 C  C   . ILE A 1 299 ? 1.752   -7.924  -27.476 1.00 37.16  ? 285 ILE A C   1 
ATOM   2143 O  O   . ILE A 1 299 ? 1.120   -8.968  -27.639 1.00 33.03  ? 285 ILE A O   1 
ATOM   2144 C  CB  . ILE A 1 299 ? 1.220   -6.887  -25.191 1.00 45.68  ? 285 ILE A CB  1 
ATOM   2145 C  CG1 . ILE A 1 299 ? 0.051   -7.828  -24.901 1.00 36.25  ? 285 ILE A CG1 1 
ATOM   2146 C  CG2 . ILE A 1 299 ? 0.749   -5.548  -25.759 1.00 41.88  ? 285 ILE A CG2 1 
ATOM   2147 C  CD1 . ILE A 1 299 ? 0.370   -8.946  -23.966 1.00 43.67  ? 285 ILE A CD1 1 
ATOM   2148 N  N   . ASN A 1 300 ? 1.990   -7.076  -28.492 1.00 55.22  ? 286 ASN A N   1 
ATOM   2149 C  CA  . ASN A 1 300 ? 1.508   -7.378  -29.838 1.00 55.72  ? 286 ASN A CA  1 
ATOM   2150 C  C   . ASN A 1 300 ? 2.318   -8.512  -30.483 1.00 54.69  ? 286 ASN A C   1 
ATOM   2151 O  O   . ASN A 1 300 ? 1.823   -9.140  -31.419 1.00 51.75  ? 286 ASN A O   1 
ATOM   2152 C  CB  . ASN A 1 300 ? 1.440   -6.144  -30.751 1.00 45.87  ? 286 ASN A CB  1 
ATOM   2153 C  CG  . ASN A 1 300 ? 2.771   -5.439  -30.907 1.00 38.43  ? 286 ASN A CG  1 
ATOM   2154 O  OD1 . ASN A 1 300 ? 3.809   -6.078  -31.063 1.00 66.83  ? 286 ASN A OD1 1 
ATOM   2155 N  ND2 . ASN A 1 300 ? 2.755   -4.118  -30.836 1.00 72.62  ? 286 ASN A ND2 1 
ATOM   2156 N  N   . GLU A 1 301 ? 3.529   -8.774  -29.958 1.00 65.29  ? 287 GLU A N   1 
ATOM   2157 C  CA  . GLU A 1 301 ? 4.405   -9.857  -30.409 1.00 77.86  ? 287 GLU A CA  1 
ATOM   2158 C  C   . GLU A 1 301 ? 4.044   -11.235 -29.835 1.00 60.11  ? 287 GLU A C   1 
ATOM   2159 O  O   . GLU A 1 301 ? 4.634   -12.222 -30.261 1.00 50.90  ? 287 GLU A O   1 
ATOM   2160 C  CB  . GLU A 1 301 ? 5.841   -9.589  -29.969 1.00 67.27  ? 287 GLU A CB  1 
ATOM   2161 C  CG  . GLU A 1 301 ? 6.485   -8.351  -30.575 1.00 71.91  ? 287 GLU A CG  1 
ATOM   2162 C  CD  . GLU A 1 301 ? 7.085   -8.539  -31.953 1.00 77.24  ? 287 GLU A CD  1 
ATOM   2163 O  OE1 . GLU A 1 301 ? 6.795   -9.562  -32.605 1.00 89.74  ? 287 GLU A OE1 1 
ATOM   2164 O  OE2 . GLU A 1 301 ? 7.876   -7.677  -32.353 1.00 92.98  ? 287 GLU A OE2 1 
ATOM   2165 N  N   . VAL A 1 302 ? 3.136   -11.342 -28.860 1.00 46.22  ? 288 VAL A N   1 
ATOM   2166 C  CA  . VAL A 1 302 ? 2.922   -12.588 -28.132 1.00 30.53  ? 288 VAL A CA  1 
ATOM   2167 C  C   . VAL A 1 302 ? 2.368   -13.681 -29.046 1.00 34.16  ? 288 VAL A C   1 
ATOM   2168 O  O   . VAL A 1 302 ? 2.782   -14.830 -28.944 1.00 34.71  ? 288 VAL A O   1 
ATOM   2169 C  CB  . VAL A 1 302 ? 2.007   -12.361 -26.911 1.00 29.18  ? 288 VAL A CB  1 
ATOM   2170 C  CG1 . VAL A 1 302 ? 1.366   -13.642 -26.400 1.00 32.52  ? 288 VAL A CG1 1 
ATOM   2171 C  CG2 . VAL A 1 302 ? 2.766   -11.657 -25.798 1.00 32.12  ? 288 VAL A CG2 1 
ATOM   2172 N  N   . GLU A 1 303 ? 1.444   -13.347 -29.952 1.00 33.15  ? 289 GLU A N   1 
ATOM   2173 C  CA  . GLU A 1 303 ? 0.810   -14.374 -30.773 1.00 32.47  ? 289 GLU A CA  1 
ATOM   2174 C  C   . GLU A 1 303 ? 1.798   -14.984 -31.781 1.00 42.90  ? 289 GLU A C   1 
ATOM   2175 O  O   . GLU A 1 303 ? 1.490   -16.010 -32.380 1.00 42.54  ? 289 GLU A O   1 
ATOM   2176 C  CB  . GLU A 1 303 ? -0.450  -13.829 -31.445 1.00 36.97  ? 289 GLU A CB  1 
ATOM   2177 C  CG  . GLU A 1 303 ? -0.171  -12.856 -32.574 1.00 39.15  ? 289 GLU A CG  1 
ATOM   2178 C  CD  . GLU A 1 303 ? -1.352  -12.577 -33.491 1.00 36.23  ? 289 GLU A CD  1 
ATOM   2179 O  OE1 . GLU A 1 303 ? -1.114  -12.005 -34.546 1.00 50.23  ? 289 GLU A OE1 1 
ATOM   2180 O  OE2 . GLU A 1 303 ? -2.510  -12.921 -33.143 1.00 50.25  ? 289 GLU A OE2 1 
ATOM   2181 N  N   . ASN A 1 304 ? 3.000   -14.398 -31.925 1.00 45.04  ? 290 ASN A N   1 
ATOM   2182 C  CA  . ASN A 1 304 ? 4.050   -14.925 -32.791 1.00 47.34  ? 290 ASN A CA  1 
ATOM   2183 C  C   . ASN A 1 304 ? 4.822   -16.084 -32.157 1.00 49.74  ? 290 ASN A C   1 
ATOM   2184 O  O   . ASN A 1 304 ? 5.591   -16.763 -32.832 1.00 43.50  ? 290 ASN A O   1 
ATOM   2185 C  CB  . ASN A 1 304 ? 5.029   -13.816 -33.174 1.00 38.61  ? 290 ASN A CB  1 
ATOM   2186 C  CG  . ASN A 1 304 ? 4.327   -12.767 -33.997 1.00 39.65  ? 290 ASN A CG  1 
ATOM   2187 O  OD1 . ASN A 1 304 ? 3.339   -13.080 -34.658 1.00 46.65  ? 290 ASN A OD1 1 
ATOM   2188 N  ND2 . ASN A 1 304 ? 4.806   -11.539 -33.935 1.00 44.41  ? 290 ASN A ND2 1 
ATOM   2189 N  N   . TYR A 1 305 ? 4.646   -16.322 -30.859 1.00 44.81  ? 291 TYR A N   1 
ATOM   2190 C  CA  . TYR A 1 305 ? 5.377   -17.400 -30.220 1.00 28.97  ? 291 TYR A CA  1 
ATOM   2191 C  C   . TYR A 1 305 ? 4.475   -18.607 -30.045 1.00 28.01  ? 291 TYR A C   1 
ATOM   2192 O  O   . TYR A 1 305 ? 3.265   -18.476 -29.951 1.00 34.13  ? 291 TYR A O   1 
ATOM   2193 C  CB  . TYR A 1 305 ? 5.930   -16.948 -28.865 1.00 27.93  ? 291 TYR A CB  1 
ATOM   2194 C  CG  . TYR A 1 305 ? 7.088   -15.993 -28.953 1.00 27.77  ? 291 TYR A CG  1 
ATOM   2195 C  CD1 . TYR A 1 305 ? 6.887   -14.658 -29.282 1.00 30.68  ? 291 TYR A CD1 1 
ATOM   2196 C  CD2 . TYR A 1 305 ? 8.384   -16.429 -28.739 1.00 32.16  ? 291 TYR A CD2 1 
ATOM   2197 C  CE1 . TYR A 1 305 ? 7.946   -13.767 -29.362 1.00 32.10  ? 291 TYR A CE1 1 
ATOM   2198 C  CE2 . TYR A 1 305 ? 9.455   -15.559 -28.847 1.00 34.44  ? 291 TYR A CE2 1 
ATOM   2199 C  CZ  . TYR A 1 305 ? 9.238   -14.231 -29.182 1.00 40.17  ? 291 TYR A CZ  1 
ATOM   2200 O  OH  . TYR A 1 305 ? 10.300  -13.366 -29.267 1.00 36.79  ? 291 TYR A OH  1 
ATOM   2201 N  N   . PRO A 1 306 ? 5.045   -19.811 -29.829 1.00 24.05  ? 292 PRO A N   1 
ATOM   2202 C  CA  . PRO A 1 306 ? 4.249   -20.931 -29.338 1.00 23.76  ? 292 PRO A CA  1 
ATOM   2203 C  C   . PRO A 1 306 ? 3.619   -20.553 -27.990 1.00 20.89  ? 292 PRO A C   1 
ATOM   2204 O  O   . PRO A 1 306 ? 4.207   -19.815 -27.188 1.00 23.40  ? 292 PRO A O   1 
ATOM   2205 C  CB  . PRO A 1 306 ? 5.274   -22.062 -29.173 1.00 29.13  ? 292 PRO A CB  1 
ATOM   2206 C  CG  . PRO A 1 306 ? 6.423   -21.669 -30.099 1.00 31.62  ? 292 PRO A CG  1 
ATOM   2207 C  CD  . PRO A 1 306 ? 6.468   -20.155 -30.037 1.00 30.12  ? 292 PRO A CD  1 
ATOM   2208 N  N   . LYS A 1 307 ? 2.468   -21.140 -27.699 1.00 22.85  ? 293 LYS A N   1 
ATOM   2209 C  CA  . LYS A 1 307 ? 1.726   -20.765 -26.503 1.00 20.25  ? 293 LYS A CA  1 
ATOM   2210 C  C   . LYS A 1 307 ? 2.536   -21.073 -25.246 1.00 23.23  ? 293 LYS A C   1 
ATOM   2211 O  O   . LYS A 1 307 ? 2.460   -20.323 -24.274 1.00 22.68  ? 293 LYS A O   1 
ATOM   2212 C  CB  . LYS A 1 307 ? 0.392   -21.513 -26.461 1.00 23.28  ? 293 LYS A CB  1 
ATOM   2213 C  CG  . LYS A 1 307 ? -0.563  -21.163 -27.596 1.00 27.05  ? 293 LYS A CG  1 
ATOM   2214 C  CD  . LYS A 1 307 ? -1.762  -22.070 -27.682 1.00 35.19  ? 293 LYS A CD  1 
ATOM   2215 C  CE  . LYS A 1 307 ? -1.438  -23.528 -27.959 1.00 57.87  ? 293 LYS A CE  1 
ATOM   2216 N  NZ  . LYS A 1 307 ? -0.805  -23.742 -29.289 1.00 73.29  ? 293 LYS A NZ  1 
ATOM   2217 N  N   . ASN A 1 308 ? 3.329   -22.160 -25.288 1.00 22.42  ? 294 ASN A N   1 
ATOM   2218 C  CA  . ASN A 1 308 ? 4.080   -22.620 -24.125 1.00 24.08  ? 294 ASN A CA  1 
ATOM   2219 C  C   . ASN A 1 308 ? 5.386   -21.843 -23.922 1.00 22.12  ? 294 ASN A C   1 
ATOM   2220 O  O   . ASN A 1 308 ? 6.134   -22.174 -22.995 1.00 23.79  ? 294 ASN A O   1 
ATOM   2221 C  CB  . ASN A 1 308 ? 4.283   -24.133 -24.168 1.00 24.42  ? 294 ASN A CB  1 
ATOM   2222 C  CG  . ASN A 1 308 ? 5.256   -24.628 -25.225 1.00 30.13  ? 294 ASN A CG  1 
ATOM   2223 O  OD1 . ASN A 1 308 ? 5.930   -23.851 -25.908 1.00 28.25  ? 294 ASN A OD1 1 
ATOM   2224 N  ND2 . ASN A 1 308 ? 5.356   -25.944 -25.347 1.00 36.53  ? 294 ASN A ND2 1 
ATOM   2225 N  N   . GLU A 1 309 ? 5.605   -20.747 -24.667 1.00 19.44  ? 295 GLU A N   1 
ATOM   2226 C  CA  . GLU A 1 309 ? 6.774   -19.885 -24.546 1.00 22.70  ? 295 GLU A CA  1 
ATOM   2227 C  C   . GLU A 1 309 ? 6.410   -18.482 -24.082 1.00 18.57  ? 295 GLU A C   1 
ATOM   2228 O  O   . GLU A 1 309 ? 7.267   -17.597 -24.163 1.00 21.03  ? 295 GLU A O   1 
ATOM   2229 C  CB  . GLU A 1 309 ? 7.541   -19.773 -25.854 1.00 24.88  ? 295 GLU A CB  1 
ATOM   2230 C  CG  . GLU A 1 309 ? 8.266   -21.063 -26.158 1.00 32.86  ? 295 GLU A CG  1 
ATOM   2231 C  CD  . GLU A 1 309 ? 9.021   -21.023 -27.470 1.00 39.33  ? 295 GLU A CD  1 
ATOM   2232 O  OE1 . GLU A 1 309 ? 9.533   -19.936 -27.814 1.00 37.64  ? 295 GLU A OE1 1 
ATOM   2233 O  OE2 . GLU A 1 309 ? 9.100   -22.078 -28.133 1.00 59.34  ? 295 GLU A OE2 1 
ATOM   2234 N  N   . VAL A 1 310 ? 5.190   -18.312 -23.510 1.00 21.47  ? 296 VAL A N   1 
ATOM   2235 C  CA  . VAL A 1 310 ? 4.812   -16.970 -23.089 1.00 23.89  ? 296 VAL A CA  1 
ATOM   2236 C  C   . VAL A 1 310 ? 4.191   -16.995 -21.692 1.00 18.01  ? 296 VAL A C   1 
ATOM   2237 O  O   . VAL A 1 310 ? 3.391   -17.876 -21.366 1.00 19.64  ? 296 VAL A O   1 
ATOM   2238 C  CB  . VAL A 1 310 ? 3.898   -16.285 -24.126 1.00 24.13  ? 296 VAL A CB  1 
ATOM   2239 C  CG1 . VAL A 1 310 ? 4.574   -16.140 -25.494 1.00 27.38  ? 296 VAL A CG1 1 
ATOM   2240 C  CG2 . VAL A 1 310 ? 2.565   -17.016 -24.260 1.00 31.07  ? 296 VAL A CG2 1 
ATOM   2241 N  N   . ILE A 1 311 ? 4.547   -15.949 -20.939 1.00 20.69  ? 297 ILE A N   1 
ATOM   2242 C  CA  . ILE A 1 311 ? 3.845   -15.548 -19.728 1.00 17.07  ? 297 ILE A CA  1 
ATOM   2243 C  C   . ILE A 1 311 ? 3.387   -14.107 -19.918 1.00 18.87  ? 297 ILE A C   1 
ATOM   2244 O  O   . ILE A 1 311 ? 4.220   -13.257 -20.165 1.00 21.13  ? 297 ILE A O   1 
ATOM   2245 C  CB  . ILE A 1 311 ? 4.748   -15.644 -18.478 1.00 18.42  ? 297 ILE A CB  1 
ATOM   2246 C  CG1 . ILE A 1 311 ? 5.408   -17.011 -18.358 1.00 19.26  ? 297 ILE A CG1 1 
ATOM   2247 C  CG2 . ILE A 1 311 ? 3.931   -15.283 -17.252 1.00 18.71  ? 297 ILE A CG2 1 
ATOM   2248 C  CD1 . ILE A 1 311 ? 6.227   -17.177 -17.078 1.00 22.41  ? 297 ILE A CD1 1 
ATOM   2249 N  N   . ILE A 1 312 ? 2.098   -13.864 -19.680 1.00 17.88  ? 298 ILE A N   1 
ATOM   2250 C  CA  . ILE A 1 312 ? 1.564   -12.508 -19.674 1.00 18.62  ? 298 ILE A CA  1 
ATOM   2251 C  C   . ILE A 1 312 ? 1.299   -12.108 -18.233 1.00 18.10  ? 298 ILE A C   1 
ATOM   2252 O  O   . ILE A 1 312 ? 0.603   -12.839 -17.534 1.00 19.08  ? 298 ILE A O   1 
ATOM   2253 C  CB  . ILE A 1 312 ? 0.274   -12.481 -20.505 1.00 19.67  ? 298 ILE A CB  1 
ATOM   2254 C  CG1 . ILE A 1 312 ? 0.628   -12.865 -21.945 1.00 23.52  ? 298 ILE A CG1 1 
ATOM   2255 C  CG2 . ILE A 1 312 ? -0.455  -11.149 -20.439 1.00 19.70  ? 298 ILE A CG2 1 
ATOM   2256 C  CD1 . ILE A 1 312 ? -0.379  -13.773 -22.573 1.00 40.82  ? 298 ILE A CD1 1 
ATOM   2257 N  N   . ILE A 1 313 ? 1.844   -10.953 -17.848 1.00 16.51  ? 299 ILE A N   1 
ATOM   2258 C  CA  . ILE A 1 313 ? 1.519   -10.393 -16.546 1.00 15.63  ? 299 ILE A CA  1 
ATOM   2259 C  C   . ILE A 1 313 ? 0.461   -9.316  -16.758 1.00 16.23  ? 299 ILE A C   1 
ATOM   2260 O  O   . ILE A 1 313 ? 0.725   -8.317  -17.446 1.00 17.67  ? 299 ILE A O   1 
ATOM   2261 C  CB  . ILE A 1 313 ? 2.766   -9.821  -15.845 1.00 18.22  ? 299 ILE A CB  1 
ATOM   2262 C  CG1 . ILE A 1 313 ? 3.843   -10.895 -15.683 1.00 17.92  ? 299 ILE A CG1 1 
ATOM   2263 C  CG2 . ILE A 1 313 ? 2.372   -9.200  -14.497 1.00 18.74  ? 299 ILE A CG2 1 
ATOM   2264 C  CD1 . ILE A 1 313 ? 5.168   -10.381 -15.161 1.00 20.31  ? 299 ILE A CD1 1 
ATOM   2265 N  N   . ALA A 1 314 ? -0.731  -9.563  -16.217 1.00 17.22  ? 300 ALA A N   1 
ATOM   2266 C  CA  . ALA A 1 314 ? -1.910  -8.714  -16.436 1.00 18.32  ? 300 ALA A CA  1 
ATOM   2267 C  C   . ALA A 1 314 ? -2.243  -7.967  -15.141 1.00 18.05  ? 300 ALA A C   1 
ATOM   2268 O  O   . ALA A 1 314 ? -2.704  -8.564  -14.167 1.00 19.43  ? 300 ALA A O   1 
ATOM   2269 C  CB  . ALA A 1 314 ? -3.068  -9.584  -16.891 1.00 20.94  ? 300 ALA A CB  1 
ATOM   2270 N  N   . THR A 1 315 ? -1.959  -6.660  -15.109 1.00 20.63  ? 301 THR A N   1 
ATOM   2271 C  CA  . THR A 1 315 ? -2.057  -5.913  -13.854 1.00 19.83  ? 301 THR A CA  1 
ATOM   2272 C  C   . THR A 1 315 ? -3.181  -4.885  -13.854 1.00 26.08  ? 301 THR A C   1 
ATOM   2273 O  O   . THR A 1 315 ? -3.399  -4.237  -12.803 1.00 25.27  ? 301 THR A O   1 
ATOM   2274 C  CB  . THR A 1 315 ? -0.772  -5.191  -13.487 1.00 23.83  ? 301 THR A CB  1 
ATOM   2275 O  OG1 . THR A 1 315 ? -0.533  -4.227  -14.515 1.00 25.70  ? 301 THR A OG1 1 
ATOM   2276 C  CG2 . THR A 1 315 ? 0.412   -6.127  -13.386 1.00 28.62  ? 301 THR A CG2 1 
ATOM   2277 N  N   . GLY A 1 316 ? -3.930  -4.742  -14.965 1.00 26.89  ? 302 GLY A N   1 
ATOM   2278 C  CA  . GLY A 1 316 ? -5.033  -3.779  -14.962 1.00 25.28  ? 302 GLY A CA  1 
ATOM   2279 C  C   . GLY A 1 316 ? -4.665  -2.427  -15.582 1.00 35.13  ? 302 GLY A C   1 
ATOM   2280 O  O   . GLY A 1 316 ? -3.593  -1.893  -15.301 1.00 33.36  ? 302 GLY A O   1 
ATOM   2281 N  N   . MET A 1 317 ? -5.573  -1.873  -16.407 1.00 38.98  ? 303 MET A N   1 
ATOM   2282 C  CA  . MET A 1 317 ? -5.386  -0.573  -17.037 1.00 46.88  ? 303 MET A CA  1 
ATOM   2283 C  C   . MET A 1 317 ? -5.244  0.496   -15.955 1.00 39.25  ? 303 MET A C   1 
ATOM   2284 O  O   . MET A 1 317 ? -4.331  1.318   -16.002 1.00 53.02  ? 303 MET A O   1 
ATOM   2285 C  CB  . MET A 1 317 ? -6.565  -0.225  -17.957 1.00 49.79  ? 303 MET A CB  1 
ATOM   2286 N  N   . GLN A 1 318 ? -6.141  0.442   -14.960 1.00 37.27  ? 304 GLN A N   1 
ATOM   2287 C  CA  . GLN A 1 318 ? -6.153  1.381   -13.847 1.00 42.64  ? 304 GLN A CA  1 
ATOM   2288 C  C   . GLN A 1 318 ? -5.296  0.879   -12.683 1.00 36.50  ? 304 GLN A C   1 
ATOM   2289 O  O   . GLN A 1 318 ? -5.122  1.602   -11.721 1.00 46.41  ? 304 GLN A O   1 
ATOM   2290 C  CB  . GLN A 1 318 ? -7.586  1.596   -13.350 1.00 41.50  ? 304 GLN A CB  1 
ATOM   2291 N  N   . GLY A 1 319 ? -4.802  -0.371  -12.723 1.00 31.94  ? 305 GLY A N   1 
ATOM   2292 C  CA  . GLY A 1 319 ? -4.046  -0.927  -11.610 1.00 28.43  ? 305 GLY A CA  1 
ATOM   2293 C  C   . GLY A 1 319 ? -4.817  -2.008  -10.836 1.00 25.48  ? 305 GLY A C   1 
ATOM   2294 O  O   . GLY A 1 319 ? -4.279  -2.549  -9.865  1.00 27.48  ? 305 GLY A O   1 
ATOM   2295 N  N   . GLU A 1 320 ? -6.062  -2.310  -11.263 1.00 24.32  ? 306 GLU A N   1 
ATOM   2296 C  CA  . GLU A 1 320 ? -6.934  -3.327  -10.675 1.00 23.09  ? 306 GLU A CA  1 
ATOM   2297 C  C   . GLU A 1 320 ? -6.902  -4.610  -11.499 1.00 25.78  ? 306 GLU A C   1 
ATOM   2298 O  O   . GLU A 1 320 ? -7.582  -4.701  -12.533 1.00 24.14  ? 306 GLU A O   1 
ATOM   2299 C  CB  . GLU A 1 320 ? -8.363  -2.763  -10.629 1.00 30.21  ? 306 GLU A CB  1 
ATOM   2300 C  CG  . GLU A 1 320 ? -9.261  -3.478  -9.614  1.00 43.40  ? 306 GLU A CG  1 
ATOM   2301 C  CD  . GLU A 1 320 ? -9.491  -4.972  -9.792  1.00 45.46  ? 306 GLU A CD  1 
ATOM   2302 O  OE1 . GLU A 1 320 ? -10.480 -5.322  -10.462 1.00 39.79  ? 306 GLU A OE1 1 
ATOM   2303 O  OE2 . GLU A 1 320 ? -8.721  -5.789  -9.220  1.00 33.11  ? 306 GLU A OE2 1 
ATOM   2304 N  N   . PRO A 1 321 ? -6.131  -5.641  -11.075 1.00 24.31  ? 307 PRO A N   1 
ATOM   2305 C  CA  . PRO A 1 321 ? -5.904  -6.799  -11.936 1.00 19.97  ? 307 PRO A CA  1 
ATOM   2306 C  C   . PRO A 1 321 ? -7.152  -7.646  -12.195 1.00 17.79  ? 307 PRO A C   1 
ATOM   2307 O  O   . PRO A 1 321 ? -7.263  -8.179  -13.299 1.00 18.15  ? 307 PRO A O   1 
ATOM   2308 C  CB  . PRO A 1 321 ? -4.799  -7.644  -11.262 1.00 19.56  ? 307 PRO A CB  1 
ATOM   2309 C  CG  . PRO A 1 321 ? -4.694  -7.112  -9.871  1.00 27.22  ? 307 PRO A CG  1 
ATOM   2310 C  CD  . PRO A 1 321 ? -5.491  -5.825  -9.774  1.00 21.52  ? 307 PRO A CD  1 
ATOM   2311 N  N   . VAL A 1 322 ? -8.051  -7.799  -11.202 1.00 19.34  ? 308 VAL A N   1 
ATOM   2312 C  CA  . VAL A 1 322 ? -9.146  -8.748  -11.412 1.00 18.07  ? 308 VAL A CA  1 
ATOM   2313 C  C   . VAL A 1 322 ? -10.117 -8.254  -12.495 1.00 19.21  ? 308 VAL A C   1 
ATOM   2314 O  O   . VAL A 1 322 ? -10.603 -9.059  -13.301 1.00 19.67  ? 308 VAL A O   1 
ATOM   2315 C  CB  . VAL A 1 322 ? -9.865  -9.097  -10.095 1.00 21.00  ? 308 VAL A CB  1 
ATOM   2316 C  CG1 . VAL A 1 322 ? -10.905 -10.170 -10.335 1.00 23.71  ? 308 VAL A CG1 1 
ATOM   2317 C  CG2 . VAL A 1 322 ? -8.909  -9.554  -9.004  1.00 24.94  ? 308 VAL A CG2 1 
ATOM   2318 N  N   . GLU A 1 323 ? -10.297 -6.927  -12.606 1.00 20.56  ? 309 GLU A N   1 
ATOM   2319 C  CA  . GLU A 1 323 ? -11.152 -6.363  -13.642 1.00 23.60  ? 309 GLU A CA  1 
ATOM   2320 C  C   . GLU A 1 323 ? -10.583 -6.733  -15.010 1.00 20.95  ? 309 GLU A C   1 
ATOM   2321 O  O   . GLU A 1 323 ? -11.340 -7.069  -15.903 1.00 20.16  ? 309 GLU A O   1 
ATOM   2322 C  CB  . GLU A 1 323 ? -11.248 -4.844  -13.489 1.00 47.82  ? 309 GLU A CB  1 
ATOM   2323 C  CG  . GLU A 1 323 ? -11.923 -4.119  -14.647 1.00 61.18  ? 309 GLU A CG  1 
ATOM   2324 C  CD  . GLU A 1 323 ? -13.359 -4.527  -14.923 1.00 69.60  ? 309 GLU A CD  1 
ATOM   2325 O  OE1 . GLU A 1 323 ? -14.083 -4.839  -13.946 1.00 87.97  ? 309 GLU A OE1 1 
ATOM   2326 O  OE2 . GLU A 1 323 ? -13.758 -4.510  -16.112 1.00 80.84  ? 309 GLU A OE2 1 
ATOM   2327 N  N   . ALA A 1 324 ? -9.261  -6.613  -15.155 1.00 20.38  ? 310 ALA A N   1 
ATOM   2328 C  CA  . ALA A 1 324 ? -8.655  -6.925  -16.439 1.00 17.12  ? 310 ALA A CA  1 
ATOM   2329 C  C   . ALA A 1 324 ? -8.797  -8.421  -16.744 1.00 16.82  ? 310 ALA A C   1 
ATOM   2330 O  O   . ALA A 1 324 ? -9.138  -8.798  -17.862 1.00 16.66  ? 310 ALA A O   1 
ATOM   2331 C  CB  . ALA A 1 324 ? -7.200  -6.516  -16.453 1.00 18.39  ? 310 ALA A CB  1 
ATOM   2332 N  N   . LEU A 1 325 ? -8.610  -9.276  -15.741 1.00 15.14  ? 311 LEU A N   1 
ATOM   2333 C  CA  . LEU A 1 325 ? -8.768  -10.717 -15.923 1.00 13.90  ? 311 LEU A CA  1 
ATOM   2334 C  C   . LEU A 1 325 ? -10.214 -11.066 -16.274 1.00 15.56  ? 311 LEU A C   1 
ATOM   2335 O  O   . LEU A 1 325 ? -10.447 -11.932 -17.116 1.00 15.36  ? 311 LEU A O   1 
ATOM   2336 C  CB  . LEU A 1 325 ? -8.310  -11.413 -14.654 1.00 14.74  ? 311 LEU A CB  1 
ATOM   2337 C  CG  . LEU A 1 325 ? -8.249  -12.909 -14.701 1.00 15.14  ? 311 LEU A CG  1 
ATOM   2338 C  CD1 . LEU A 1 325 ? -7.265  -13.373 -15.759 1.00 18.87  ? 311 LEU A CD1 1 
ATOM   2339 C  CD2 . LEU A 1 325 ? -7.824  -13.415 -13.338 1.00 17.61  ? 311 LEU A CD2 1 
ATOM   2340 N  N   . SER A 1 326 ? -11.185 -10.390 -15.638 1.00 15.10  ? 312 SER A N   1 
ATOM   2341 C  CA  . SER A 1 326 ? -12.582 -10.565 -15.993 1.00 17.22  ? 312 SER A CA  1 
ATOM   2342 C  C   . SER A 1 326 ? -12.851 -10.205 -17.450 1.00 16.91  ? 312 SER A C   1 
ATOM   2343 O  O   . SER A 1 326 ? -13.520 -10.958 -18.136 1.00 16.96  ? 312 SER A O   1 
ATOM   2344 C  CB  . SER A 1 326 ? -13.478 -9.796  -15.083 1.00 19.96  ? 312 SER A CB  1 
ATOM   2345 O  OG  . SER A 1 326 ? -14.813 -9.987  -15.548 1.00 23.04  ? 312 SER A OG  1 
ATOM   2346 N  N   . GLN A 1 327 ? -12.307 -9.079  -17.898 1.00 15.39  ? 313 GLN A N   1 
ATOM   2347 C  CA  . GLN A 1 327 ? -12.442 -8.711  -19.294 1.00 15.10  ? 313 GLN A CA  1 
ATOM   2348 C  C   . GLN A 1 327 ? -11.860 -9.804  -20.187 1.00 15.39  ? 313 GLN A C   1 
ATOM   2349 O  O   . GLN A 1 327 ? -12.472 -10.214 -21.182 1.00 16.16  ? 313 GLN A O   1 
ATOM   2350 C  CB  . GLN A 1 327 ? -11.729 -7.385  -19.569 1.00 16.79  ? 313 GLN A CB  1 
ATOM   2351 C  CG  . GLN A 1 327 ? -12.461 -6.178  -19.004 1.00 20.85  ? 313 GLN A CG  1 
ATOM   2352 C  CD  . GLN A 1 327 ? -11.642 -4.912  -19.113 1.00 35.13  ? 313 GLN A CD  1 
ATOM   2353 O  OE1 . GLN A 1 327 ? -10.735 -4.805  -19.932 1.00 45.34  ? 313 GLN A OE1 1 
ATOM   2354 N  NE2 . GLN A 1 327 ? -11.951 -3.944  -18.267 1.00 48.54  ? 313 GLN A NE2 1 
ATOM   2355 N  N   . MET A 1 328 ? -10.641 -10.255 -19.873 1.00 13.83  ? 314 MET A N   1 
ATOM   2356 C  CA  . MET A 1 328 ? -10.037 -11.276 -20.699 1.00 13.66  ? 314 MET A CA  1 
ATOM   2357 C  C   . MET A 1 328 ? -10.881 -12.546 -20.756 1.00 13.63  ? 314 MET A C   1 
ATOM   2358 O  O   . MET A 1 328 ? -10.977 -13.200 -21.811 1.00 14.89  ? 314 MET A O   1 
ATOM   2359 C  CB  . MET A 1 328 ? -8.633  -11.623 -20.197 1.00 14.56  ? 314 MET A CB  1 
ATOM   2360 C  CG  . MET A 1 328 ? -7.641  -10.508 -20.279 1.00 16.51  ? 314 MET A CG  1 
ATOM   2361 S  SD  . MET A 1 328 ? -6.033  -10.981 -19.514 1.00 21.82  ? 314 MET A SD  1 
ATOM   2362 C  CE  . MET A 1 328 ? -5.247  -11.766 -20.922 1.00 26.38  ? 314 MET A CE  1 
ATOM   2363 N  N   . ALA A 1 329 ? -11.401 -12.950 -19.590 1.00 13.74  ? 315 ALA A N   1 
ATOM   2364 C  CA  . ALA A 1 329 ? -12.179 -14.167 -19.470 1.00 14.24  ? 315 ALA A CA  1 
ATOM   2365 C  C   . ALA A 1 329 ? -13.433 -14.116 -20.341 1.00 16.60  ? 315 ALA A C   1 
ATOM   2366 O  O   . ALA A 1 329 ? -13.852 -15.146 -20.869 1.00 18.21  ? 315 ALA A O   1 
ATOM   2367 C  CB  . ALA A 1 329 ? -12.522 -14.410 -18.043 1.00 15.86  ? 315 ALA A CB  1 
ATOM   2368 N  N   . ARG A 1 330 ? -14.086 -12.946 -20.376 1.00 17.08  ? 316 ARG A N   1 
ATOM   2369 C  CA  . ARG A 1 330 ? -15.331 -12.726 -21.096 1.00 16.99  ? 316 ARG A CA  1 
ATOM   2370 C  C   . ARG A 1 330 ? -15.054 -12.330 -22.553 1.00 18.61  ? 316 ARG A C   1 
ATOM   2371 O  O   . ARG A 1 330 ? -15.980 -12.116 -23.327 1.00 20.33  ? 316 ARG A O   1 
ATOM   2372 C  CB  . ARG A 1 330 ? -16.164 -11.622 -20.423 1.00 19.52  ? 316 ARG A CB  1 
ATOM   2373 C  CG  . ARG A 1 330 ? -16.688 -11.929 -19.022 1.00 23.64  ? 316 ARG A CG  1 
ATOM   2374 C  CD  . ARG A 1 330 ? -16.905 -10.692 -18.145 1.00 25.98  ? 316 ARG A CD  1 
ATOM   2375 N  NE  . ARG A 1 330 ? -17.460 -9.496  -18.746 1.00 48.31  ? 316 ARG A NE  1 
ATOM   2376 C  CZ  . ARG A 1 330 ? -16.919 -8.288  -18.634 1.00 55.45  ? 316 ARG A CZ  1 
ATOM   2377 N  NH1 . ARG A 1 330 ? -15.784 -8.123  -17.975 1.00 44.23  ? 316 ARG A NH1 1 
ATOM   2378 N  NH2 . ARG A 1 330 ? -17.526 -7.241  -19.163 1.00 76.44  ? 316 ARG A NH2 1 
ATOM   2379 N  N   . LYS A 1 331 ? -13.774 -12.252 -22.929 1.00 17.48  ? 317 LYS A N   1 
ATOM   2380 C  CA  . LYS A 1 331 ? -13.341 -11.980 -24.292 1.00 17.20  ? 317 LYS A CA  1 
ATOM   2381 C  C   . LYS A 1 331 ? -13.728 -10.555 -24.697 1.00 16.32  ? 317 LYS A C   1 
ATOM   2382 O  O   . LYS A 1 331 ? -13.980 -10.294 -25.879 1.00 18.81  ? 317 LYS A O   1 
ATOM   2383 C  CB  . LYS A 1 331 ? -13.854 -13.041 -25.280 1.00 19.38  ? 317 LYS A CB  1 
ATOM   2384 C  CG  . LYS A 1 331 ? -13.346 -14.453 -24.958 1.00 23.57  ? 317 LYS A CG  1 
ATOM   2385 C  CD  . LYS A 1 331 ? -13.801 -15.543 -25.919 1.00 28.92  ? 317 LYS A CD  1 
ATOM   2386 C  CE  . LYS A 1 331 ? -13.254 -16.907 -25.556 1.00 29.26  ? 317 LYS A CE  1 
ATOM   2387 N  NZ  . LYS A 1 331 ? -13.742 -17.329 -24.235 1.00 44.23  ? 317 LYS A NZ  1 
ATOM   2388 N  N   . LYS A 1 332 ? -13.630 -9.635  -23.733 1.00 17.44  ? 318 LYS A N   1 
ATOM   2389 C  CA  . LYS A 1 332 ? -14.040 -8.254  -23.836 1.00 17.68  ? 318 LYS A CA  1 
ATOM   2390 C  C   . LYS A 1 332 ? -12.836 -7.323  -23.788 1.00 20.01  ? 318 LYS A C   1 
ATOM   2391 O  O   . LYS A 1 332 ? -12.967 -6.116  -23.943 1.00 25.98  ? 318 LYS A O   1 
ATOM   2392 C  CB  . LYS A 1 332 ? -15.046 -7.876  -22.740 1.00 22.48  ? 318 LYS A CB  1 
ATOM   2393 C  CG  . LYS A 1 332 ? -16.427 -8.492  -22.903 1.00 26.79  ? 318 LYS A CG  1 
ATOM   2394 C  CD  . LYS A 1 332 ? -17.467 -7.921  -21.948 1.00 37.79  ? 318 LYS A CD  1 
ATOM   2395 N  N   . HIS A 1 333 ? -11.648 -7.869  -23.523 1.00 18.35  ? 319 HIS A N   1 
ATOM   2396 C  CA  . HIS A 1 333 ? -10.470 -7.048  -23.429 1.00 18.49  ? 319 HIS A CA  1 
ATOM   2397 C  C   . HIS A 1 333 ? -10.099 -6.516  -24.822 1.00 21.17  ? 319 HIS A C   1 
ATOM   2398 O  O   . HIS A 1 333 ? -10.224 -7.221  -25.825 1.00 23.17  ? 319 HIS A O   1 
ATOM   2399 C  CB  . HIS A 1 333 ? -9.334  -7.850  -22.809 1.00 16.45  ? 319 HIS A CB  1 
ATOM   2400 C  CG  . HIS A 1 333 ? -8.217  -7.014  -22.292 1.00 18.17  ? 319 HIS A CG  1 
ATOM   2401 N  ND1 . HIS A 1 333 ? -7.237  -6.453  -23.058 1.00 19.90  ? 319 HIS A ND1 1 
ATOM   2402 C  CD2 . HIS A 1 333 ? -7.976  -6.634  -21.008 1.00 18.48  ? 319 HIS A CD2 1 
ATOM   2403 C  CE1 . HIS A 1 333 ? -6.436  -5.723  -22.280 1.00 22.86  ? 319 HIS A CE1 1 
ATOM   2404 N  NE2 . HIS A 1 333 ? -6.870  -5.823  -21.007 1.00 23.83  ? 319 HIS A NE2 1 
ATOM   2405 N  N   . LYS A 1 334 ? -9.632  -5.271  -24.835 1.00 24.14  ? 320 LYS A N   1 
ATOM   2406 C  CA  . LYS A 1 334 ? -9.288  -4.543  -26.042 1.00 26.70  ? 320 LYS A CA  1 
ATOM   2407 C  C   . LYS A 1 334 ? -8.065  -5.127  -26.731 1.00 25.21  ? 320 LYS A C   1 
ATOM   2408 O  O   . LYS A 1 334 ? -7.919  -5.001  -27.945 1.00 31.40  ? 320 LYS A O   1 
ATOM   2409 C  CB  . LYS A 1 334 ? -9.041  -3.056  -25.724 1.00 29.42  ? 320 LYS A CB  1 
ATOM   2410 N  N   . ILE A 1 335 ? -7.155  -5.716  -25.954 1.00 23.28  ? 321 ILE A N   1 
ATOM   2411 C  CA  . ILE A 1 335 ? -5.810  -6.042  -26.426 1.00 25.89  ? 321 ILE A CA  1 
ATOM   2412 C  C   . ILE A 1 335 ? -5.612  -7.556  -26.548 1.00 24.07  ? 321 ILE A C   1 
ATOM   2413 O  O   . ILE A 1 335 ? -5.130  -8.026  -27.574 1.00 26.22  ? 321 ILE A O   1 
ATOM   2414 C  CB  . ILE A 1 335 ? -4.743  -5.402  -25.508 1.00 25.49  ? 321 ILE A CB  1 
ATOM   2415 C  CG1 . ILE A 1 335 ? -4.945  -3.896  -25.324 1.00 31.44  ? 321 ILE A CG1 1 
ATOM   2416 C  CG2 . ILE A 1 335 ? -3.335  -5.703  -26.003 1.00 30.06  ? 321 ILE A CG2 1 
ATOM   2417 C  CD1 . ILE A 1 335 ? -3.909  -3.240  -24.443 1.00 39.85  ? 321 ILE A CD1 1 
ATOM   2418 N  N   A MET A 1 336 ? -5.969  -8.312  -25.498 0.58 20.38  ? 322 MET A N   1 
ATOM   2419 N  N   B MET A 1 336 ? -5.948  -8.307  -25.490 0.42 21.08  ? 322 MET A N   1 
ATOM   2420 C  CA  A MET A 1 336 ? -5.712  -9.737  -25.466 0.58 16.99  ? 322 MET A CA  1 
ATOM   2421 C  CA  B MET A 1 336 ? -5.699  -9.735  -25.465 0.42 19.05  ? 322 MET A CA  1 
ATOM   2422 C  C   A MET A 1 336 ? -6.746  -10.410 -24.569 0.58 15.94  ? 322 MET A C   1 
ATOM   2423 C  C   B MET A 1 336 ? -6.752  -10.398 -24.580 0.42 17.29  ? 322 MET A C   1 
ATOM   2424 O  O   A MET A 1 336 ? -7.002  -9.931  -23.454 0.58 18.47  ? 322 MET A O   1 
ATOM   2425 O  O   B MET A 1 336 ? -7.034  -9.897  -23.485 0.42 20.07  ? 322 MET A O   1 
ATOM   2426 C  CB  A MET A 1 336 ? -4.307  -9.984  -24.901 0.58 19.42  ? 322 MET A CB  1 
ATOM   2427 C  CB  B MET A 1 336 ? -4.303  -9.998  -24.886 0.42 23.46  ? 322 MET A CB  1 
ATOM   2428 C  CG  A MET A 1 336 ? -3.958  -11.449 -24.709 0.58 18.05  ? 322 MET A CG  1 
ATOM   2429 C  CG  B MET A 1 336 ? -3.695  -11.321 -25.299 0.42 31.77  ? 322 MET A CG  1 
ATOM   2430 S  SD  A MET A 1 336 ? -3.930  -12.346 -26.278 0.58 27.58  ? 322 MET A SD  1 
ATOM   2431 S  SD  B MET A 1 336 ? -2.354  -11.858 -24.195 0.42 29.80  ? 322 MET A SD  1 
ATOM   2432 C  CE  A MET A 1 336 ? -2.283  -11.952 -26.867 0.58 34.35  ? 322 MET A CE  1 
ATOM   2433 C  CE  B MET A 1 336 ? -3.289  -13.099 -23.303 0.42 36.76  ? 322 MET A CE  1 
ATOM   2434 N  N   . ASN A 1 337 ? -7.317  -11.507 -25.067 1.00 17.70  ? 323 ASN A N   1 
ATOM   2435 C  CA  . ASN A 1 337 ? -8.313  -12.280 -24.349 1.00 16.09  ? 323 ASN A CA  1 
ATOM   2436 C  C   . ASN A 1 337 ? -7.826  -13.697 -24.035 1.00 16.92  ? 323 ASN A C   1 
ATOM   2437 O  O   . ASN A 1 337 ? -6.899  -14.212 -24.642 1.00 19.19  ? 323 ASN A O   1 
ATOM   2438 C  CB  . ASN A 1 337 ? -9.597  -12.332 -25.167 1.00 16.73  ? 323 ASN A CB  1 
ATOM   2439 C  CG  . ASN A 1 337 ? -10.211 -10.963 -25.197 1.00 17.29  ? 323 ASN A CG  1 
ATOM   2440 O  OD1 . ASN A 1 337 ? -10.497 -10.415 -24.150 1.00 17.71  ? 323 ASN A OD1 1 
ATOM   2441 N  ND2 . ASN A 1 337 ? -10.419 -10.444 -26.387 1.00 23.23  ? 323 ASN A ND2 1 
ATOM   2442 N  N   . ILE A 1 338 ? -8.521  -14.335 -23.084 1.00 15.66  ? 324 ILE A N   1 
ATOM   2443 C  CA  . ILE A 1 338 ? -8.273  -15.714 -22.708 1.00 16.69  ? 324 ILE A CA  1 
ATOM   2444 C  C   . ILE A 1 338 ? -8.762  -16.618 -23.825 1.00 17.88  ? 324 ILE A C   1 
ATOM   2445 O  O   . ILE A 1 338 ? -9.752  -16.352 -24.506 1.00 22.89  ? 324 ILE A O   1 
ATOM   2446 C  CB  . ILE A 1 338 ? -9.044  -16.064 -21.409 1.00 18.19  ? 324 ILE A CB  1 
ATOM   2447 C  CG1 . ILE A 1 338 ? -8.668  -15.230 -20.197 1.00 26.69  ? 324 ILE A CG1 1 
ATOM   2448 C  CG2 . ILE A 1 338 ? -8.983  -17.537 -21.059 1.00 21.18  ? 324 ILE A CG2 1 
ATOM   2449 C  CD1 . ILE A 1 338 ? -7.238  -15.265 -19.919 1.00 28.30  ? 324 ILE A CD1 1 
ATOM   2450 N  N   . GLU A 1 339 ? -8.033  -17.714 -23.994 1.00 17.37  ? 325 GLU A N   1 
ATOM   2451 C  CA  . GLU A 1 339 ? -8.422  -18.792 -24.891 1.00 19.01  ? 325 GLU A CA  1 
ATOM   2452 C  C   . GLU A 1 339 ? -8.423  -20.110 -24.121 1.00 22.51  ? 325 GLU A C   1 
ATOM   2453 O  O   . GLU A 1 339 ? -7.739  -20.286 -23.106 1.00 19.05  ? 325 GLU A O   1 
ATOM   2454 C  CB  . GLU A 1 339 ? -7.542  -18.804 -26.138 1.00 30.12  ? 325 GLU A CB  1 
ATOM   2455 C  CG  . GLU A 1 339 ? -6.062  -18.886 -25.887 1.00 36.78  ? 325 GLU A CG  1 
ATOM   2456 C  CD  . GLU A 1 339 ? -5.226  -18.899 -27.158 1.00 50.09  ? 325 GLU A CD  1 
ATOM   2457 O  OE1 . GLU A 1 339 ? -5.448  -18.019 -28.026 1.00 43.70  ? 325 GLU A OE1 1 
ATOM   2458 O  OE2 . GLU A 1 339 ? -4.344  -19.790 -27.274 0.40 40.22  ? 325 GLU A OE2 1 
ATOM   2459 N  N   . GLU A 1 340 ? -9.220  -21.060 -24.608 1.00 20.87  ? 326 GLU A N   1 
ATOM   2460 C  CA  . GLU A 1 340 ? -9.277  -22.394 -24.050 1.00 20.27  ? 326 GLU A CA  1 
ATOM   2461 C  C   . GLU A 1 340 ? -7.865  -22.960 -23.938 1.00 22.42  ? 326 GLU A C   1 
ATOM   2462 O  O   . GLU A 1 340 ? -7.052  -22.823 -24.866 1.00 22.28  ? 326 GLU A O   1 
ATOM   2463 C  CB  . GLU A 1 340 ? -10.144 -23.280 -24.942 1.00 23.98  ? 326 GLU A CB  1 
ATOM   2464 C  CG  . GLU A 1 340 ? -10.444 -24.658 -24.378 1.00 30.79  ? 326 GLU A CG  1 
ATOM   2465 C  CD  . GLU A 1 340 ? -11.375 -25.494 -25.232 1.00 41.76  ? 326 GLU A CD  1 
ATOM   2466 O  OE1 . GLU A 1 340 ? -11.421 -26.722 -25.006 1.00 51.06  ? 326 GLU A OE1 1 
ATOM   2467 O  OE2 . GLU A 1 340 ? -12.064 -24.916 -26.099 1.00 49.02  ? 326 GLU A OE2 1 
ATOM   2468 N  N   . GLY A 1 341 ? -7.592  -23.538 -22.760 1.00 20.54  ? 327 GLY A N   1 
ATOM   2469 C  CA  . GLY A 1 341 ? -6.303  -24.143 -22.488 1.00 21.19  ? 327 GLY A CA  1 
ATOM   2470 C  C   . GLY A 1 341 ? -5.309  -23.208 -21.808 1.00 17.23  ? 327 GLY A C   1 
ATOM   2471 O  O   . GLY A 1 341 ? -4.332  -23.677 -21.273 1.00 19.51  ? 327 GLY A O   1 
ATOM   2472 N  N   . ASP A 1 342 ? -5.564  -21.896 -21.785 1.00 16.77  ? 328 ASP A N   1 
ATOM   2473 C  CA  . ASP A 1 342 ? -4.738  -20.994 -20.992 1.00 16.33  ? 328 ASP A CA  1 
ATOM   2474 C  C   . ASP A 1 342 ? -4.790  -21.381 -19.517 1.00 15.92  ? 328 ASP A C   1 
ATOM   2475 O  O   . ASP A 1 342 ? -5.785  -21.894 -19.029 1.00 18.13  ? 328 ASP A O   1 
ATOM   2476 C  CB  . ASP A 1 342 ? -5.255  -19.573 -21.059 1.00 17.64  ? 328 ASP A CB  1 
ATOM   2477 C  CG  . ASP A 1 342 ? -4.984  -18.829 -22.334 1.00 20.89  ? 328 ASP A CG  1 
ATOM   2478 O  OD1 . ASP A 1 342 ? -4.118  -19.294 -23.137 1.00 20.33  ? 328 ASP A OD1 1 
ATOM   2479 O  OD2 . ASP A 1 342 ? -5.568  -17.710 -22.461 1.00 19.83  ? 328 ASP A OD2 1 
ATOM   2480 N  N   . SER A 1 343 ? -3.670  -21.116 -18.811 1.00 17.07  ? 329 SER A N   1 
ATOM   2481 C  CA  . SER A 1 343 ? -3.564  -21.329 -17.375 1.00 16.16  ? 329 SER A CA  1 
ATOM   2482 C  C   . SER A 1 343 ? -3.419  -19.967 -16.701 1.00 13.89  ? 329 SER A C   1 
ATOM   2483 O  O   . SER A 1 343 ? -2.789  -19.089 -17.240 1.00 16.76  ? 329 SER A O   1 
ATOM   2484 C  CB  . SER A 1 343 ? -2.394  -22.214 -17.045 1.00 18.29  ? 329 SER A CB  1 
ATOM   2485 O  OG  . SER A 1 343 ? -2.544  -23.503 -17.635 1.00 18.76  ? 329 SER A OG  1 
ATOM   2486 N  N   . ILE A 1 344 ? -3.991  -19.879 -15.497 1.00 16.49  ? 330 ILE A N   1 
ATOM   2487 C  CA  . ILE A 1 344 ? -4.132  -18.624 -14.755 1.00 15.78  ? 330 ILE A CA  1 
ATOM   2488 C  C   . ILE A 1 344 ? -3.506  -18.788 -13.378 1.00 15.51  ? 330 ILE A C   1 
ATOM   2489 O  O   . ILE A 1 344 ? -3.929  -19.693 -12.647 1.00 17.07  ? 330 ILE A O   1 
ATOM   2490 C  CB  . ILE A 1 344 ? -5.613  -18.234 -14.591 1.00 17.09  ? 330 ILE A CB  1 
ATOM   2491 C  CG1 . ILE A 1 344 ? -6.394  -18.392 -15.902 1.00 23.59  ? 330 ILE A CG1 1 
ATOM   2492 C  CG2 . ILE A 1 344 ? -5.752  -16.867 -13.970 1.00 20.71  ? 330 ILE A CG2 1 
ATOM   2493 C  CD1 . ILE A 1 344 ? -5.909  -17.495 -16.984 1.00 22.58  ? 330 ILE A CD1 1 
ATOM   2494 N  N   . PHE A 1 345 ? -2.585  -17.859 -13.058 1.00 15.49  ? 331 PHE A N   1 
ATOM   2495 C  CA  . PHE A 1 345 ? -2.057  -17.788 -11.702 1.00 16.29  ? 331 PHE A CA  1 
ATOM   2496 C  C   . PHE A 1 345 ? -2.579  -16.508 -11.064 1.00 14.25  ? 331 PHE A C   1 
ATOM   2497 O  O   . PHE A 1 345 ? -2.212  -15.423 -11.480 1.00 15.49  ? 331 PHE A O   1 
ATOM   2498 C  CB  . PHE A 1 345 ? -0.527  -17.845 -11.744 1.00 16.96  ? 331 PHE A CB  1 
ATOM   2499 C  CG  . PHE A 1 345 ? 0.077   -17.947 -10.372 1.00 21.28  ? 331 PHE A CG  1 
ATOM   2500 C  CD1 . PHE A 1 345 ? 0.051   -19.162 -9.701  1.00 24.97  ? 331 PHE A CD1 1 
ATOM   2501 C  CD2 . PHE A 1 345 ? 0.734   -16.883 -9.801  1.00 21.07  ? 331 PHE A CD2 1 
ATOM   2502 C  CE1 . PHE A 1 345 ? 0.602   -19.280 -8.439  1.00 30.63  ? 331 PHE A CE1 1 
ATOM   2503 C  CE2 . PHE A 1 345 ? 1.277   -17.007 -8.527  1.00 25.36  ? 331 PHE A CE2 1 
ATOM   2504 C  CZ  . PHE A 1 345 ? 1.198   -18.198 -7.862  1.00 24.51  ? 331 PHE A CZ  1 
ATOM   2505 N  N   . LEU A 1 346 ? -3.458  -16.617 -10.065 1.00 18.15  ? 332 LEU A N   1 
ATOM   2506 C  CA  . LEU A 1 346 ? -4.047  -15.433 -9.465  1.00 20.17  ? 332 LEU A CA  1 
ATOM   2507 C  C   . LEU A 1 346 ? -3.280  -15.081 -8.192  1.00 24.95  ? 332 LEU A C   1 
ATOM   2508 O  O   . LEU A 1 346 ? -3.410  -15.735 -7.161  1.00 29.62  ? 332 LEU A O   1 
ATOM   2509 C  CB  . LEU A 1 346 ? -5.549  -15.682 -9.280  1.00 25.10  ? 332 LEU A CB  1 
ATOM   2510 C  CG  . LEU A 1 346 ? -6.408  -14.529 -8.763  1.00 29.86  ? 332 LEU A CG  1 
ATOM   2511 C  CD1 . LEU A 1 346 ? -6.214  -13.252 -9.576  1.00 34.87  ? 332 LEU A CD1 1 
ATOM   2512 C  CD2 . LEU A 1 346 ? -7.874  -14.937 -8.770  1.00 45.27  ? 332 LEU A CD2 1 
ATOM   2513 N  N   . ALA A 1 347 ? -2.427  -14.058 -8.311  1.00 27.88  ? 333 ALA A N   1 
ATOM   2514 C  CA  . ALA A 1 347 ? -1.532  -13.642 -7.246  1.00 34.12  ? 333 ALA A CA  1 
ATOM   2515 C  C   . ALA A 1 347 ? -2.078  -12.358 -6.626  1.00 32.44  ? 333 ALA A C   1 
ATOM   2516 O  O   . ALA A 1 347 ? -1.468  -11.287 -6.730  1.00 38.32  ? 333 ALA A O   1 
ATOM   2517 C  CB  . ALA A 1 347 ? -0.125  -13.468 -7.785  1.00 31.46  ? 333 ALA A CB  1 
ATOM   2518 N  N   . ILE A 1 348 ? -3.265  -12.474 -6.024  1.00 35.84  ? 334 ILE A N   1 
ATOM   2519 C  CA  . ILE A 1 348 ? -3.905  -11.360 -5.341  1.00 35.90  ? 334 ILE A CA  1 
ATOM   2520 C  C   . ILE A 1 348 ? -4.438  -11.869 -4.011  1.00 44.00  ? 334 ILE A C   1 
ATOM   2521 O  O   . ILE A 1 348 ? -4.758  -13.051 -3.900  1.00 49.72  ? 334 ILE A O   1 
ATOM   2522 C  CB  . ILE A 1 348 ? -5.056  -10.745 -6.166  1.00 41.17  ? 334 ILE A CB  1 
ATOM   2523 C  CG1 . ILE A 1 348 ? -6.168  -11.769 -6.399  1.00 45.64  ? 334 ILE A CG1 1 
ATOM   2524 C  CG2 . ILE A 1 348 ? -4.563  -10.133 -7.474  1.00 44.52  ? 334 ILE A CG2 1 
ATOM   2525 C  CD1 . ILE A 1 348 ? -7.522  -11.160 -6.618  1.00 57.01  ? 334 ILE A CD1 1 
ATOM   2526 N  N   . THR A 1 349 ? -4.593  -10.937 -3.056  1.00 43.37  ? 335 THR A N   1 
ATOM   2527 C  CA  . THR A 1 349 ? -5.121  -11.205 -1.724  1.00 45.74  ? 335 THR A CA  1 
ATOM   2528 C  C   . THR A 1 349 ? -6.546  -10.648 -1.625  1.00 55.00  ? 335 THR A C   1 
ATOM   2529 O  O   . THR A 1 349 ? -6.732  -9.435  -1.531  1.00 40.82  ? 335 THR A O   1 
ATOM   2530 C  CB  . THR A 1 349 ? -4.187  -10.616 -0.654  1.00 40.21  ? 335 THR A CB  1 
ATOM   2531 N  N   . ALA A 1 350 ? -7.547  -11.543 -1.636  1.00 66.11  ? 336 ALA A N   1 
ATOM   2532 C  CA  . ALA A 1 350 ? -8.956  -11.168 -1.675  1.00 60.62  ? 336 ALA A CA  1 
ATOM   2533 C  C   . ALA A 1 350 ? -9.358  -10.335 -0.455  1.00 56.94  ? 336 ALA A C   1 
ATOM   2534 O  O   . ALA A 1 350 ? -8.891  -10.577 0.652   1.00 66.20  ? 336 ALA A O   1 
ATOM   2535 C  CB  . ALA A 1 350 ? -9.817  -12.409 -1.777  1.00 50.73  ? 336 ALA A CB  1 
ATOM   2536 N  N   . SER A 1 351 ? -10.242 -9.355  -0.685  1.00 51.32  ? 337 SER A N   1 
ATOM   2537 C  CA  . SER A 1 351 ? -10.925 -8.615  0.364   1.00 41.73  ? 337 SER A CA  1 
ATOM   2538 C  C   . SER A 1 351 ? -12.433 -8.781  0.221   1.00 43.20  ? 337 SER A C   1 
ATOM   2539 O  O   . SER A 1 351 ? -12.912 -9.163  -0.842  1.00 46.19  ? 337 SER A O   1 
ATOM   2540 C  CB  . SER A 1 351 ? -10.597 -7.154  0.265   1.00 39.18  ? 337 SER A CB  1 
ATOM   2541 O  OG  . SER A 1 351 ? -11.342 -6.562  -0.791  1.00 35.25  ? 337 SER A OG  1 
ATOM   2542 N  N   . ALA A 1 352 ? -13.171 -8.349  1.250   1.00 28.78  ? 338 ALA A N   1 
ATOM   2543 C  CA  . ALA A 1 352 ? -14.629 -8.374  1.222   1.00 39.52  ? 338 ALA A CA  1 
ATOM   2544 C  C   . ALA A 1 352 ? -15.153 -7.574  0.033   1.00 32.94  ? 338 ALA A C   1 
ATOM   2545 O  O   . ALA A 1 352 ? -16.135 -7.958  -0.599  1.00 34.64  ? 338 ALA A O   1 
ATOM   2546 C  CB  . ALA A 1 352 ? -15.204 -7.833  2.514   1.00 46.51  ? 338 ALA A CB  1 
ATOM   2547 N  N   . ASN A 1 353 ? -14.495 -6.442  -0.217  1.00 31.01  ? 339 ASN A N   1 
ATOM   2548 C  CA  . ASN A 1 353 ? -14.804 -5.537  -1.316  1.00 38.63  ? 339 ASN A CA  1 
ATOM   2549 C  C   . ASN A 1 353 ? -14.748 -6.255  -2.667  1.00 38.13  ? 339 ASN A C   1 
ATOM   2550 O  O   . ASN A 1 353 ? -15.472 -5.874  -3.589  1.00 39.94  ? 339 ASN A O   1 
ATOM   2551 C  CB  . ASN A 1 353 ? -13.823 -4.353  -1.280  1.00 40.51  ? 339 ASN A CB  1 
ATOM   2552 C  CG  . ASN A 1 353 ? -14.130 -3.256  -2.271  1.00 51.92  ? 339 ASN A CG  1 
ATOM   2553 O  OD1 . ASN A 1 353 ? -15.169 -2.598  -2.190  1.00 53.69  ? 339 ASN A OD1 1 
ATOM   2554 N  ND2 . ASN A 1 353 ? -13.193 -3.023  -3.175  1.00 38.40  ? 339 ASN A ND2 1 
ATOM   2555 N  N   . MET A 1 354 ? -13.880 -7.274  -2.774  1.00 28.01  ? 340 MET A N   1 
ATOM   2556 C  CA  . MET A 1 354 ? -13.466 -7.885  -4.038  1.00 30.48  ? 340 MET A CA  1 
ATOM   2557 C  C   . MET A 1 354 ? -14.021 -9.308  -4.199  1.00 29.65  ? 340 MET A C   1 
ATOM   2558 O  O   . MET A 1 354 ? -13.836 -9.936  -5.244  1.00 26.84  ? 340 MET A O   1 
ATOM   2559 C  CB  . MET A 1 354 ? -11.935 -8.011  -4.100  1.00 34.79  ? 340 MET A CB  1 
ATOM   2560 C  CG  . MET A 1 354 ? -11.151 -6.697  -4.046  1.00 33.37  ? 340 MET A CG  1 
ATOM   2561 S  SD  . MET A 1 354 ? -11.347 -5.608  -5.478  1.00 37.42  ? 340 MET A SD  1 
ATOM   2562 C  CE  . MET A 1 354 ? -10.966 -6.681  -6.858  1.00 45.34  ? 340 MET A CE  1 
ATOM   2563 N  N   . GLU A 1 355 ? -14.623 -9.895  -3.160  1.00 26.88  ? 341 GLU A N   1 
ATOM   2564 C  CA  . GLU A 1 355 ? -14.838 -11.342 -3.199  1.00 25.11  ? 341 GLU A CA  1 
ATOM   2565 C  C   . GLU A 1 355 ? -15.856 -11.710 -4.288  1.00 22.80  ? 341 GLU A C   1 
ATOM   2566 O  O   . GLU A 1 355 ? -15.766 -12.796 -4.886  1.00 22.12  ? 341 GLU A O   1 
ATOM   2567 C  CB  . GLU A 1 355 ? -15.179 -11.872 -1.805  1.00 29.55  ? 341 GLU A CB  1 
ATOM   2568 C  CG  . GLU A 1 355 ? -16.408 -11.233 -1.211  1.00 28.47  ? 341 GLU A CG  1 
ATOM   2569 C  CD  . GLU A 1 355 ? -16.663 -11.577 0.253   1.00 46.00  ? 341 GLU A CD  1 
ATOM   2570 O  OE1 . GLU A 1 355 ? -17.718 -11.164 0.732   1.00 30.83  ? 341 GLU A OE1 1 
ATOM   2571 O  OE2 . GLU A 1 355 ? -15.803 -12.241 0.918   1.00 32.28  ? 341 GLU A OE2 1 
ATOM   2572 N  N   . VAL A 1 356 ? -16.782 -10.807 -4.629  1.00 22.90  ? 342 VAL A N   1 
ATOM   2573 C  CA  . VAL A 1 356 ? -17.780 -11.077 -5.664  1.00 24.37  ? 342 VAL A CA  1 
ATOM   2574 C  C   . VAL A 1 356 ? -17.140 -11.071 -7.049  1.00 25.90  ? 342 VAL A C   1 
ATOM   2575 O  O   . VAL A 1 356 ? -17.339 -12.011 -7.831  1.00 21.59  ? 342 VAL A O   1 
ATOM   2576 C  CB  . VAL A 1 356 ? -18.963 -10.094 -5.608  1.00 24.67  ? 342 VAL A CB  1 
ATOM   2577 C  CG1 . VAL A 1 356 ? -19.908 -10.260 -6.799  1.00 27.78  ? 342 VAL A CG1 1 
ATOM   2578 C  CG2 . VAL A 1 356 ? -19.720 -10.231 -4.295  1.00 29.54  ? 342 VAL A CG2 1 
ATOM   2579 N  N   . ILE A 1 357 ? -16.357 -10.028 -7.359  1.00 24.23  ? 343 ILE A N   1 
ATOM   2580 C  CA  . ILE A 1 357 ? -15.721 -9.994  -8.660  1.00 21.82  ? 343 ILE A CA  1 
ATOM   2581 C  C   . ILE A 1 357 ? -14.762 -11.173 -8.796  1.00 17.24  ? 343 ILE A C   1 
ATOM   2582 O  O   . ILE A 1 357 ? -14.675 -11.747 -9.875  1.00 18.52  ? 343 ILE A O   1 
ATOM   2583 C  CB  . ILE A 1 357 ? -15.052 -8.644  -8.995  1.00 23.22  ? 343 ILE A CB  1 
ATOM   2584 C  CG1 . ILE A 1 357 ? -14.665 -8.600  -10.477 1.00 26.31  ? 343 ILE A CG1 1 
ATOM   2585 C  CG2 . ILE A 1 357 ? -13.854 -8.340  -8.099  1.00 27.50  ? 343 ILE A CG2 1 
ATOM   2586 C  CD1 . ILE A 1 357 ? -14.146 -7.246  -10.914 1.00 32.25  ? 343 ILE A CD1 1 
ATOM   2587 N  N   . ILE A 1 358 ? -14.023 -11.549 -7.751  1.00 19.44  ? 344 ILE A N   1 
ATOM   2588 C  CA  . ILE A 1 358 ? -13.122 -12.685 -7.854  1.00 18.16  ? 344 ILE A CA  1 
ATOM   2589 C  C   . ILE A 1 358 ? -13.920 -13.959 -8.196  1.00 18.39  ? 344 ILE A C   1 
ATOM   2590 O  O   . ILE A 1 358 ? -13.527 -14.712 -9.089  1.00 17.63  ? 344 ILE A O   1 
ATOM   2591 C  CB  . ILE A 1 358 ? -12.290 -12.827 -6.561  1.00 23.58  ? 344 ILE A CB  1 
ATOM   2592 C  CG1 . ILE A 1 358 ? -11.227 -11.721 -6.459  1.00 27.66  ? 344 ILE A CG1 1 
ATOM   2593 C  CG2 . ILE A 1 358 ? -11.666 -14.210 -6.460  1.00 20.66  ? 344 ILE A CG2 1 
ATOM   2594 C  CD1 . ILE A 1 358 ? -10.556 -11.641 -5.123  1.00 38.91  ? 344 ILE A CD1 1 
ATOM   2595 N  N   . ALA A 1 359 ? -15.027 -14.207 -7.474  1.00 17.42  ? 345 ALA A N   1 
ATOM   2596 C  CA  . ALA A 1 359 ? -15.828 -15.407 -7.674  1.00 17.59  ? 345 ALA A CA  1 
ATOM   2597 C  C   . ALA A 1 359 ? -16.376 -15.461 -9.081  1.00 16.22  ? 345 ALA A C   1 
ATOM   2598 O  O   . ALA A 1 359 ? -16.290 -16.476 -9.758  1.00 17.24  ? 345 ALA A O   1 
ATOM   2599 C  CB  . ALA A 1 359 ? -16.964 -15.419 -6.685  1.00 20.49  ? 345 ALA A CB  1 
ATOM   2600 N  N   . ASP A 1 360 ? -16.915 -14.331 -9.532  1.00 16.23  ? 346 ASP A N   1 
ATOM   2601 C  CA  . ASP A 1 360 ? -17.454 -14.254 -10.865 1.00 17.15  ? 346 ASP A CA  1 
ATOM   2602 C  C   . ASP A 1 360 ? -16.370 -14.530 -11.914 1.00 15.93  ? 346 ASP A C   1 
ATOM   2603 O  O   . ASP A 1 360 ? -16.611 -15.204 -12.914 1.00 15.96  ? 346 ASP A O   1 
ATOM   2604 C  CB  . ASP A 1 360 ? -18.066 -12.879 -11.143 1.00 18.56  ? 346 ASP A CB  1 
ATOM   2605 C  CG  . ASP A 1 360 ? -19.326 -12.558 -10.356 1.00 26.49  ? 346 ASP A CG  1 
ATOM   2606 O  OD1 . ASP A 1 360 ? -19.878 -13.485 -9.745  1.00 25.23  ? 346 ASP A OD1 1 
ATOM   2607 O  OD2 . ASP A 1 360 ? -19.747 -11.368 -10.342 1.00 29.46  ? 346 ASP A OD2 1 
ATOM   2608 N  N   . THR A 1 361 ? -15.177 -13.965 -11.701 1.00 14.90  ? 347 THR A N   1 
ATOM   2609 C  CA  . THR A 1 361 ? -14.083 -14.094 -12.659 1.00 14.92  ? 347 THR A CA  1 
ATOM   2610 C  C   . THR A 1 361 ? -13.634 -15.549 -12.755 1.00 14.21  ? 347 THR A C   1 
ATOM   2611 O  O   . THR A 1 361 ? -13.358 -16.055 -13.847 1.00 16.26  ? 347 THR A O   1 
ATOM   2612 C  CB  . THR A 1 361 ? -12.985 -13.093 -12.314 1.00 16.50  ? 347 THR A CB  1 
ATOM   2613 O  OG1 . THR A 1 361 ? -13.517 -11.762 -12.340 1.00 18.16  ? 347 THR A OG1 1 
ATOM   2614 C  CG2 . THR A 1 361 ? -11.845 -13.219 -13.292 1.00 17.86  ? 347 THR A CG2 1 
ATOM   2615 N  N   . LEU A 1 362 ? -13.476 -16.185 -11.596 1.00 15.93  ? 348 LEU A N   1 
ATOM   2616 C  CA  . LEU A 1 362 ? -13.127 -17.609 -11.582 1.00 16.72  ? 348 LEU A CA  1 
ATOM   2617 C  C   . LEU A 1 362 ? -14.144 -18.447 -12.372 1.00 16.20  ? 348 LEU A C   1 
ATOM   2618 O  O   . LEU A 1 362 ? -13.757 -19.334 -13.146 1.00 16.59  ? 348 LEU A O   1 
ATOM   2619 C  CB  . LEU A 1 362 ? -13.007 -18.070 -10.131 1.00 18.84  ? 348 LEU A CB  1 
ATOM   2620 C  CG  . LEU A 1 362 ? -11.811 -17.521 -9.338  1.00 24.54  ? 348 LEU A CG  1 
ATOM   2621 C  CD1 . LEU A 1 362 ? -11.852 -18.014 -7.892  1.00 26.76  ? 348 LEU A CD1 1 
ATOM   2622 C  CD2 . LEU A 1 362 ? -10.482 -17.919 -9.962  1.00 28.96  ? 348 LEU A CD2 1 
ATOM   2623 N  N   . ASN A 1 363 ? -15.437 -18.160 -12.209 1.00 14.24  ? 349 ASN A N   1 
ATOM   2624 C  CA  . ASN A 1 363 ? -16.453 -18.914 -12.924 1.00 16.15  ? 349 ASN A CA  1 
ATOM   2625 C  C   . ASN A 1 363 ? -16.335 -18.654 -14.422 1.00 16.39  ? 349 ASN A C   1 
ATOM   2626 O  O   . ASN A 1 363 ? -16.437 -19.584 -15.199 1.00 17.69  ? 349 ASN A O   1 
ATOM   2627 C  CB  . ASN A 1 363 ? -17.843 -18.506 -12.452 1.00 15.67  ? 349 ASN A CB  1 
ATOM   2628 C  CG  . ASN A 1 363 ? -18.199 -19.069 -11.102 1.00 16.56  ? 349 ASN A CG  1 
ATOM   2629 O  OD1 . ASN A 1 363 ? -17.686 -20.135 -10.756 1.00 20.63  ? 349 ASN A OD1 1 
ATOM   2630 N  ND2 . ASN A 1 363 ? -19.101 -18.402 -10.405 1.00 18.41  ? 349 ASN A ND2 1 
ATOM   2631 N  N   . GLU A 1 364 ? -16.109 -17.391 -14.803 1.00 15.96  ? 350 GLU A N   1 
ATOM   2632 C  CA  . GLU A 1 364 ? -15.944 -17.007 -16.201 1.00 16.81  ? 350 GLU A CA  1 
ATOM   2633 C  C   . GLU A 1 364 ? -14.742 -17.738 -16.818 1.00 15.13  ? 350 GLU A C   1 
ATOM   2634 O  O   . GLU A 1 364 ? -14.800 -18.209 -17.950 1.00 17.18  ? 350 GLU A O   1 
ATOM   2635 C  CB  . GLU A 1 364 ? -15.755 -15.481 -16.334 1.00 19.96  ? 350 GLU A CB  1 
ATOM   2636 C  CG  . GLU A 1 364 ? -16.938 -14.577 -15.901 1.00 20.34  ? 350 GLU A CG  1 
ATOM   2637 C  CD  . GLU A 1 364 ? -16.632 -13.117 -15.510 1.00 23.75  ? 350 GLU A CD  1 
ATOM   2638 O  OE1 . GLU A 1 364 ? -15.451 -12.660 -15.639 1.00 25.20  ? 350 GLU A OE1 1 
ATOM   2639 O  OE2 . GLU A 1 364 ? -17.605 -12.397 -15.088 1.00 25.04  ? 350 GLU A OE2 1 
ATOM   2640 N  N   . LEU A 1 365 ? -13.615 -17.834 -16.087 1.00 15.15  ? 351 LEU A N   1 
ATOM   2641 C  CA  . LEU A 1 365 ? -12.428 -18.503 -16.602 1.00 14.99  ? 351 LEU A CA  1 
ATOM   2642 C  C   . LEU A 1 365 ? -12.697 -19.991 -16.823 1.00 17.82  ? 351 LEU A C   1 
ATOM   2643 O  O   . LEU A 1 365 ? -12.284 -20.550 -17.842 1.00 19.04  ? 351 LEU A O   1 
ATOM   2644 C  CB  . LEU A 1 365 ? -11.257 -18.287 -15.625 1.00 16.26  ? 351 LEU A CB  1 
ATOM   2645 C  CG  . LEU A 1 365 ? -10.687 -16.866 -15.591 1.00 16.41  ? 351 LEU A CG  1 
ATOM   2646 C  CD1 . LEU A 1 365 ? -9.868  -16.630 -14.320 1.00 19.14  ? 351 LEU A CD1 1 
ATOM   2647 C  CD2 . LEU A 1 365 ? -9.864  -16.605 -16.837 1.00 18.35  ? 351 LEU A CD2 1 
ATOM   2648 N  N   . VAL A 1 366 ? -13.395 -20.624 -15.881 1.00 17.61  ? 352 VAL A N   1 
ATOM   2649 C  CA  . VAL A 1 366 ? -13.672 -22.038 -16.036 1.00 19.22  ? 352 VAL A CA  1 
ATOM   2650 C  C   . VAL A 1 366 ? -14.606 -22.247 -17.235 1.00 19.42  ? 352 VAL A C   1 
ATOM   2651 O  O   . VAL A 1 366 ? -14.329 -23.131 -18.036 1.00 20.97  ? 352 VAL A O   1 
ATOM   2652 C  CB  . VAL A 1 366 ? -14.203 -22.646 -14.728 1.00 19.10  ? 352 VAL A CB  1 
ATOM   2653 C  CG1 . VAL A 1 366 ? -14.750 -24.041 -14.981 1.00 25.46  ? 352 VAL A CG1 1 
ATOM   2654 C  CG2 . VAL A 1 366 ? -13.110 -22.667 -13.675 1.00 20.25  ? 352 VAL A CG2 1 
ATOM   2655 N  N   . ARG A 1 367 ? -15.640 -21.408 -17.375 1.00 18.49  ? 353 ARG A N   1 
ATOM   2656 C  CA  . ARG A 1 367 ? -16.519 -21.467 -18.549 1.00 19.07  ? 353 ARG A CA  1 
ATOM   2657 C  C   . ARG A 1 367 ? -15.734 -21.318 -19.860 1.00 22.56  ? 353 ARG A C   1 
ATOM   2658 O  O   . ARG A 1 367 ? -16.064 -21.985 -20.830 1.00 25.17  ? 353 ARG A O   1 
ATOM   2659 C  CB  . ARG A 1 367 ? -17.571 -20.349 -18.527 1.00 22.51  ? 353 ARG A CB  1 
ATOM   2660 C  CG  . ARG A 1 367 ? -18.624 -20.432 -17.433 1.00 31.72  ? 353 ARG A CG  1 
ATOM   2661 C  CD  . ARG A 1 367 ? -19.979 -19.822 -17.793 1.00 41.47  ? 353 ARG A CD  1 
ATOM   2662 N  NE  . ARG A 1 367 ? -20.022 -18.367 -17.972 1.00 41.09  ? 353 ARG A NE  1 
ATOM   2663 C  CZ  . ARG A 1 367 ? -19.850 -17.438 -17.023 1.00 35.57  ? 353 ARG A CZ  1 
ATOM   2664 N  NH1 . ARG A 1 367 ? -19.807 -17.755 -15.742 1.00 29.89  ? 353 ARG A NH1 1 
ATOM   2665 N  NH2 . ARG A 1 367 ? -19.707 -16.165 -17.366 1.00 33.78  ? 353 ARG A NH2 1 
ATOM   2666 N  N   . ALA A 1 368 ? -14.694 -20.453 -19.877 1.00 18.88  ? 354 ALA A N   1 
ATOM   2667 C  CA  . ALA A 1 368 ? -13.869 -20.200 -21.060 1.00 21.23  ? 354 ALA A CA  1 
ATOM   2668 C  C   . ALA A 1 368 ? -12.887 -21.347 -21.363 1.00 21.34  ? 354 ALA A C   1 
ATOM   2669 O  O   . ALA A 1 368 ? -12.186 -21.325 -22.369 1.00 24.08  ? 354 ALA A O   1 
ATOM   2670 C  CB  . ALA A 1 368 ? -13.142 -18.872 -20.937 1.00 22.34  ? 354 ALA A CB  1 
ATOM   2671 N  N   . GLY A 1 369 ? -12.857 -22.391 -20.547 1.00 20.36  ? 355 GLY A N   1 
ATOM   2672 C  CA  . GLY A 1 369 ? -11.916 -23.472 -20.779 1.00 20.21  ? 355 GLY A CA  1 
ATOM   2673 C  C   . GLY A 1 369 ? -10.501 -23.181 -20.271 1.00 20.57  ? 355 GLY A C   1 
ATOM   2674 O  O   . GLY A 1 369 ? -9.566  -23.841 -20.690 1.00 22.17  ? 355 GLY A O   1 
ATOM   2675 N  N   . ALA A 1 370 ? -10.316 -22.207 -19.376 1.00 17.74  ? 356 ALA A N   1 
ATOM   2676 C  CA  . ALA A 1 370 ? -9.016  -21.928 -18.783 1.00 17.58  ? 356 ALA A CA  1 
ATOM   2677 C  C   . ALA A 1 370 ? -8.839  -22.769 -17.525 1.00 16.99  ? 356 ALA A C   1 
ATOM   2678 O  O   . ALA A 1 370 ? -9.811  -23.269 -16.972 1.00 21.39  ? 356 ALA A O   1 
ATOM   2679 C  CB  . ALA A 1 370 ? -8.875  -20.469 -18.442 1.00 18.34  ? 356 ALA A CB  1 
ATOM   2680 N  N   . HIS A 1 371 ? -7.570  -22.952 -17.165 1.00 20.60  ? 357 HIS A N   1 
ATOM   2681 C  CA  . HIS A 1 371 ? -7.161  -23.742 -16.015 1.00 20.34  ? 357 HIS A CA  1 
ATOM   2682 C  C   . HIS A 1 371 ? -6.619  -22.820 -14.936 1.00 18.24  ? 357 HIS A C   1 
ATOM   2683 O  O   . HIS A 1 371 ? -5.623  -22.147 -15.132 1.00 22.51  ? 357 HIS A O   1 
ATOM   2684 C  CB  . HIS A 1 371 ? -6.110  -24.789 -16.407 1.00 23.06  ? 357 HIS A CB  1 
ATOM   2685 C  CG  . HIS A 1 371 ? -6.581  -25.703 -17.489 1.00 29.61  ? 357 HIS A CG  1 
ATOM   2686 N  ND1 . HIS A 1 371 ? -7.562  -26.644 -17.293 1.00 33.30  ? 357 HIS A ND1 1 
ATOM   2687 C  CD2 . HIS A 1 371 ? -6.234  -25.741 -18.804 1.00 37.07  ? 357 HIS A CD2 1 
ATOM   2688 C  CE1 . HIS A 1 371 ? -7.806  -27.262 -18.445 1.00 39.89  ? 357 HIS A CE1 1 
ATOM   2689 N  NE2 . HIS A 1 371 ? -6.980  -26.725 -19.397 1.00 43.60  ? 357 HIS A NE2 1 
ATOM   2690 N  N   . ILE A 1 372 ? -7.246  -22.862 -13.776 1.00 21.62  ? 358 ILE A N   1 
ATOM   2691 C  CA  . ILE A 1 372 ? -6.824  -22.033 -12.669 1.00 19.59  ? 358 ILE A CA  1 
ATOM   2692 C  C   . ILE A 1 372 ? -5.838  -22.852 -11.856 1.00 18.49  ? 358 ILE A C   1 
ATOM   2693 O  O   . ILE A 1 372 ? -6.183  -23.947 -11.397 1.00 22.31  ? 358 ILE A O   1 
ATOM   2694 C  CB  . ILE A 1 372 ? -8.038  -21.595 -11.840 1.00 21.96  ? 358 ILE A CB  1 
ATOM   2695 C  CG1 . ILE A 1 372 ? -9.054  -20.878 -12.758 1.00 26.98  ? 358 ILE A CG1 1 
ATOM   2696 C  CG2 . ILE A 1 372 ? -7.571  -20.778 -10.643 1.00 22.27  ? 358 ILE A CG2 1 
ATOM   2697 C  CD1 . ILE A 1 372 ? -10.453 -20.889 -12.245 1.00 35.08  ? 358 ILE A CD1 1 
ATOM   2698 N  N   . ILE A 1 373 ? -4.618  -22.340 -11.723 1.00 17.04  ? 359 ILE A N   1 
ATOM   2699 C  CA  . ILE A 1 373 ? -3.630  -23.013 -10.888 1.00 19.87  ? 359 ILE A CA  1 
ATOM   2700 C  C   . ILE A 1 373 ? -4.115  -22.954 -9.436  1.00 20.40  ? 359 ILE A C   1 
ATOM   2701 O  O   . ILE A 1 373 ? -4.444  -21.910 -8.899  1.00 21.32  ? 359 ILE A O   1 
ATOM   2702 C  CB  . ILE A 1 373 ? -2.274  -22.344 -11.101 1.00 20.65  ? 359 ILE A CB  1 
ATOM   2703 C  CG1 . ILE A 1 373 ? -1.809  -22.584 -12.537 1.00 19.39  ? 359 ILE A CG1 1 
ATOM   2704 C  CG2 . ILE A 1 373 ? -1.224  -22.814 -10.092 1.00 19.76  ? 359 ILE A CG2 1 
ATOM   2705 C  CD1 . ILE A 1 373 ? -0.535  -21.879 -12.892 1.00 20.43  ? 359 ILE A CD1 1 
ATOM   2706 N  N   . PRO A 1 374 ? -4.220  -24.119 -8.765  1.00 26.86  ? 360 PRO A N   1 
ATOM   2707 C  CA  . PRO A 1 374 ? -4.789  -24.156 -7.423  1.00 29.84  ? 360 PRO A CA  1 
ATOM   2708 C  C   . PRO A 1 374 ? -3.881  -23.475 -6.408  1.00 31.87  ? 360 PRO A C   1 
ATOM   2709 O  O   . PRO A 1 374 ? -2.679  -23.395 -6.620  1.00 27.51  ? 360 PRO A O   1 
ATOM   2710 C  CB  . PRO A 1 374 ? -4.939  -25.664 -7.157  1.00 34.83  ? 360 PRO A CB  1 
ATOM   2711 C  CG  . PRO A 1 374 ? -3.929  -26.335 -8.064  1.00 33.10  ? 360 PRO A CG  1 
ATOM   2712 C  CD  . PRO A 1 374 ? -3.848  -25.444 -9.285  1.00 28.65  ? 360 PRO A CD  1 
ATOM   2713 N  N   . ASN A 1 375 ? -4.483  -22.935 -5.342  1.00 39.84  ? 361 ASN A N   1 
ATOM   2714 C  CA  . ASN A 1 375 ? -3.741  -22.586 -4.136  1.00 36.59  ? 361 ASN A CA  1 
ATOM   2715 C  C   . ASN A 1 375 ? -3.160  -23.856 -3.515  1.00 34.38  ? 361 ASN A C   1 
ATOM   2716 O  O   . ASN A 1 375 ? -3.818  -24.887 -3.438  1.00 43.11  ? 361 ASN A O   1 
ATOM   2717 C  CB  . ASN A 1 375 ? -4.593  -21.804 -3.132  1.00 40.91  ? 361 ASN A CB  1 
ATOM   2718 C  CG  . ASN A 1 375 ? -4.747  -20.347 -3.518  1.00 51.63  ? 361 ASN A CG  1 
ATOM   2719 O  OD1 . ASN A 1 375 ? -4.953  -20.024 -4.685  1.00 64.06  ? 361 ASN A OD1 1 
ATOM   2720 N  ND2 . ASN A 1 375 ? -4.624  -19.459 -2.550  1.00 47.88  ? 361 ASN A ND2 1 
ATOM   2721 N  N   . ASN A 1 376 ? -1.886  -23.771 -3.135  1.00 32.82  ? 362 ASN A N   1 
ATOM   2722 C  CA  . ASN A 1 376 ? -1.240  -24.773 -2.304  1.00 30.68  ? 362 ASN A CA  1 
ATOM   2723 C  C   . ASN A 1 376 ? -1.709  -24.552 -0.865  1.00 35.31  ? 362 ASN A C   1 
ATOM   2724 O  O   . ASN A 1 376 ? -1.544  -23.463 -0.335  1.00 33.27  ? 362 ASN A O   1 
ATOM   2725 C  CB  . ASN A 1 376 ? 0.280   -24.686 -2.442  1.00 32.35  ? 362 ASN A CB  1 
ATOM   2726 C  CG  . ASN A 1 376 ? 1.009   -25.770 -1.673  1.00 37.48  ? 362 ASN A CG  1 
ATOM   2727 O  OD1 . ASN A 1 376 ? 0.619   -26.118 -0.558  1.00 39.61  ? 362 ASN A OD1 1 
ATOM   2728 N  ND2 . ASN A 1 376 ? 2.073   -26.302 -2.258  1.00 47.51  ? 362 ASN A ND2 1 
ATOM   2729 N  N   . LYS A 1 377 ? -2.287  -25.580 -0.227  1.00 36.71  ? 363 LYS A N   1 
ATOM   2730 C  CA  . LYS A 1 377 ? -2.807  -25.454 1.128   1.00 40.31  ? 363 LYS A CA  1 
ATOM   2731 C  C   . LYS A 1 377 ? -1.671  -25.128 2.112   1.00 43.46  ? 363 LYS A C   1 
ATOM   2732 O  O   . LYS A 1 377 ? -1.913  -24.470 3.128   1.00 44.21  ? 363 LYS A O   1 
ATOM   2733 C  CB  . LYS A 1 377 ? -3.622  -26.704 1.474   1.00 46.10  ? 363 LYS A CB  1 
ATOM   2734 C  CG  . LYS A 1 377 ? -4.069  -26.829 2.923   1.00 54.33  ? 363 LYS A CG  1 
ATOM   2735 C  CD  . LYS A 1 377 ? -3.118  -27.654 3.765   1.00 69.60  ? 363 LYS A CD  1 
ATOM   2736 C  CE  . LYS A 1 377 ? -3.096  -27.259 5.225   1.00 53.00  ? 363 LYS A CE  1 
ATOM   2737 N  NZ  . LYS A 1 377 ? -2.038  -28.001 5.947   1.00 53.50  ? 363 LYS A NZ  1 
ATOM   2738 N  N   . LYS A 1 378 ? -0.430  -25.530 1.785   1.00 36.78  ? 364 LYS A N   1 
ATOM   2739 C  CA  . LYS A 1 378 ? 0.740   -25.312 2.632   1.00 37.47  ? 364 LYS A CA  1 
ATOM   2740 C  C   . LYS A 1 378 ? 1.314   -23.898 2.475   1.00 32.35  ? 364 LYS A C   1 
ATOM   2741 O  O   . LYS A 1 378 ? 2.223   -23.528 3.216   1.00 38.36  ? 364 LYS A O   1 
ATOM   2742 C  CB  . LYS A 1 378 ? 1.851   -26.317 2.293   1.00 44.81  ? 364 LYS A CB  1 
ATOM   2743 N  N   . ILE A 1 379 ? 0.797   -23.107 1.521   1.00 33.28  ? 365 ILE A N   1 
ATOM   2744 C  CA  . ILE A 1 379 ? 1.292   -21.759 1.266   1.00 34.33  ? 365 ILE A CA  1 
ATOM   2745 C  C   . ILE A 1 379 ? 0.266   -20.729 1.730   1.00 34.97  ? 365 ILE A C   1 
ATOM   2746 O  O   . ILE A 1 379 ? -0.911  -20.827 1.399   1.00 31.37  ? 365 ILE A O   1 
ATOM   2747 C  CB  . ILE A 1 379 ? 1.612   -21.560 -0.232  1.00 31.82  ? 365 ILE A CB  1 
ATOM   2748 C  CG1 . ILE A 1 379 ? 2.717   -22.509 -0.695  1.00 42.03  ? 365 ILE A CG1 1 
ATOM   2749 C  CG2 . ILE A 1 379 ? 1.944   -20.106 -0.545  1.00 39.08  ? 365 ILE A CG2 1 
ATOM   2750 C  CD1 . ILE A 1 379 ? 3.164   -22.266 -2.119  1.00 44.80  ? 365 ILE A CD1 1 
ATOM   2751 N  N   . HIS A 1 380 ? 0.762   -19.702 2.436   1.00 25.85  ? 366 HIS A N   1 
ATOM   2752 C  CA  . HIS A 1 380 ? 0.018   -18.488 2.705   1.00 25.86  ? 366 HIS A CA  1 
ATOM   2753 C  C   . HIS A 1 380 ? 0.828   -17.328 2.147   1.00 24.07  ? 366 HIS A C   1 
ATOM   2754 O  O   . HIS A 1 380 ? 1.883   -16.988 2.692   1.00 22.35  ? 366 HIS A O   1 
ATOM   2755 C  CB  . HIS A 1 380 ? -0.273  -18.292 4.200   1.00 29.51  ? 366 HIS A CB  1 
ATOM   2756 C  CG  . HIS A 1 380 ? -1.242  -17.167 4.417   1.00 35.67  ? 366 HIS A CG  1 
ATOM   2757 N  ND1 . HIS A 1 380 ? -0.884  -15.832 4.494   1.00 33.90  ? 366 HIS A ND1 1 
ATOM   2758 C  CD2 . HIS A 1 380 ? -2.604  -17.227 4.496   1.00 30.26  ? 366 HIS A CD2 1 
ATOM   2759 C  CE1 . HIS A 1 380 ? -1.983  -15.105 4.666   1.00 30.13  ? 366 HIS A CE1 1 
ATOM   2760 N  NE2 . HIS A 1 380 ? -3.066  -15.950 4.669   1.00 40.53  ? 366 HIS A NE2 1 
ATOM   2761 N  N   . ALA A 1 381 ? 0.345   -16.783 1.014   1.00 22.29  ? 367 ALA A N   1 
ATOM   2762 C  CA  . ALA A 1 381 ? 1.038   -15.718 0.305   1.00 20.62  ? 367 ALA A CA  1 
ATOM   2763 C  C   . ALA A 1 381 ? 0.307   -14.401 0.557   1.00 20.15  ? 367 ALA A C   1 
ATOM   2764 O  O   . ALA A 1 381 ? -0.846  -14.255 0.169   1.00 26.71  ? 367 ALA A O   1 
ATOM   2765 C  CB  . ALA A 1 381 ? 1.093   -16.012 -1.166  1.00 23.21  ? 367 ALA A CB  1 
ATOM   2766 N  N   . SER A 1 382 ? 0.945   -13.459 1.243   1.00 18.46  ? 368 SER A N   1 
ATOM   2767 C  CA  . SER A 1 382 ? 0.408   -12.115 1.337   1.00 17.05  ? 368 SER A CA  1 
ATOM   2768 C  C   . SER A 1 382 ? 1.574   -11.136 1.507   1.00 16.97  ? 368 SER A C   1 
ATOM   2769 O  O   . SER A 1 382 ? 2.685   -11.513 1.904   1.00 18.34  ? 368 SER A O   1 
ATOM   2770 C  CB  . SER A 1 382 ? -0.594  -12.046 2.467   1.00 19.60  ? 368 SER A CB  1 
ATOM   2771 O  OG  . SER A 1 382 ? -0.008  -11.576 3.645   1.00 24.10  ? 368 SER A OG  1 
ATOM   2772 N  N   . SER A 1 383 ? 1.266   -9.841  1.366   1.00 15.56  ? 369 SER A N   1 
ATOM   2773 C  CA  . SER A 1 383 ? 2.228   -8.778  1.594   1.00 17.31  ? 369 SER A CA  1 
ATOM   2774 C  C   . SER A 1 383 ? 2.103   -8.161  3.001   1.00 14.95  ? 369 SER A C   1 
ATOM   2775 O  O   . SER A 1 383 ? 2.831   -7.204  3.302   1.00 17.36  ? 369 SER A O   1 
ATOM   2776 C  CB  . SER A 1 383 ? 2.110   -7.730  0.507   1.00 20.39  ? 369 SER A CB  1 
ATOM   2777 O  OG  . SER A 1 383 ? 0.854   -7.161  0.611   1.00 28.38  ? 369 SER A OG  1 
ATOM   2778 N  N   . HIS A 1 384 ? 1.238   -8.724  3.855   1.00 13.63  ? 370 HIS A N   1 
ATOM   2779 C  CA  . HIS A 1 384 ? 0.907   -8.175  5.160   1.00 13.46  ? 370 HIS A CA  1 
ATOM   2780 C  C   . HIS A 1 384 ? 1.177   -9.203  6.244   1.00 12.48  ? 370 HIS A C   1 
ATOM   2781 O  O   . HIS A 1 384 ? 0.822   -10.365 6.051   1.00 14.14  ? 370 HIS A O   1 
ATOM   2782 C  CB  . HIS A 1 384 ? -0.567  -7.789  5.190   1.00 12.81  ? 370 HIS A CB  1 
ATOM   2783 C  CG  . HIS A 1 384 ? -0.950  -6.879  4.070   1.00 12.81  ? 370 HIS A CG  1 
ATOM   2784 N  ND1 . HIS A 1 384 ? -0.933  -5.501  4.176   1.00 13.33  ? 370 HIS A ND1 1 
ATOM   2785 C  CD2 . HIS A 1 384 ? -1.356  -7.212  2.827   1.00 14.73  ? 370 HIS A CD2 1 
ATOM   2786 C  CE1 . HIS A 1 384 ? -1.250  -5.022  2.969   1.00 14.20  ? 370 HIS A CE1 1 
ATOM   2787 N  NE2 . HIS A 1 384 ? -1.586  -6.044  2.157   1.00 15.82  ? 370 HIS A NE2 1 
ATOM   2788 N  N   . GLY A 1 385 ? 1.731   -8.754  7.364   1.00 12.36  ? 371 GLY A N   1 
ATOM   2789 C  CA  . GLY A 1 385 ? 2.113   -9.697  8.406   1.00 13.49  ? 371 GLY A CA  1 
ATOM   2790 C  C   . GLY A 1 385 ? 0.924   -10.479 8.950   1.00 12.47  ? 371 GLY A C   1 
ATOM   2791 O  O   . GLY A 1 385 ? -0.141  -9.954  9.227   1.00 12.10  ? 371 GLY A O   1 
ATOM   2792 N  N   . CYS A 1 386 ? 1.141   -11.799 9.086   1.00 12.23  ? 372 CYS A N   1 
ATOM   2793 C  CA  . CYS A 1 386 ? 0.226   -12.675 9.800   1.00 13.27  ? 372 CYS A CA  1 
ATOM   2794 C  C   . CYS A 1 386 ? 0.459   -12.509 11.307  1.00 11.98  ? 372 CYS A C   1 
ATOM   2795 O  O   . CYS A 1 386 ? 1.280   -11.695 11.741  1.00 11.69  ? 372 CYS A O   1 
ATOM   2796 C  CB  . CYS A 1 386 ? 0.450   -14.121 9.359   1.00 14.95  ? 372 CYS A CB  1 
ATOM   2797 S  SG  . CYS A 1 386 ? 0.015   -14.385 7.615   1.00 16.45  ? 372 CYS A SG  1 
ATOM   2798 N  N   . MET A 1 387 ? -0.253  -13.312 12.115  1.00 13.62  ? 373 MET A N   1 
ATOM   2799 C  CA  . MET A 1 387 ? -0.228  -13.037 13.536  1.00 13.01  ? 373 MET A CA  1 
ATOM   2800 C  C   . MET A 1 387 ? 1.168   -12.864 14.133  1.00 13.20  ? 373 MET A C   1 
ATOM   2801 O  O   . MET A 1 387 ? 1.389   -12.001 14.989  1.00 13.06  ? 373 MET A O   1 
ATOM   2802 C  CB  . MET A 1 387 ? -0.944  -14.135 14.317  1.00 15.72  ? 373 MET A CB  1 
ATOM   2803 C  CG  . MET A 1 387 ? -2.459  -14.121 14.184  1.00 14.72  ? 373 MET A CG  1 
ATOM   2804 S  SD  . MET A 1 387 ? -3.221  -15.414 15.213  1.00 19.52  ? 373 MET A SD  1 
ATOM   2805 C  CE  . MET A 1 387 ? -4.866  -15.456 14.508  1.00 23.46  ? 373 MET A CE  1 
ATOM   2806 N  N   . GLU A 1 388 ? 2.082   -13.814 13.833  1.00 13.82  ? 374 GLU A N   1 
ATOM   2807 C  CA  . GLU A 1 388 ? 3.361   -13.733 14.496  1.00 13.92  ? 374 GLU A CA  1 
ATOM   2808 C  C   . GLU A 1 388 ? 4.167   -12.523 14.048  1.00 13.92  ? 374 GLU A C   1 
ATOM   2809 O  O   . GLU A 1 388 ? 4.945   -11.998 14.851  1.00 13.99  ? 374 GLU A O   1 
ATOM   2810 C  CB  . GLU A 1 388 ? 4.170   -14.999 14.252  1.00 14.94  ? 374 GLU A CB  1 
ATOM   2811 C  CG  . GLU A 1 388 ? 3.571   -16.242 14.887  1.00 17.79  ? 374 GLU A CG  1 
ATOM   2812 C  CD  . GLU A 1 388 ? 3.350   -16.148 16.382  1.00 19.61  ? 374 GLU A CD  1 
ATOM   2813 O  OE1 . GLU A 1 388 ? 4.269   -15.700 17.091  1.00 22.47  ? 374 GLU A OE1 1 
ATOM   2814 O  OE2 . GLU A 1 388 ? 2.277   -16.578 16.809  1.00 27.61  ? 374 GLU A OE2 1 
ATOM   2815 N  N   . GLU A 1 389 ? 3.981   -12.079 12.799  1.00 13.06  ? 375 GLU A N   1 
ATOM   2816 C  CA  . GLU A 1 389 ? 4.682   -10.893 12.349  1.00 12.22  ? 375 GLU A CA  1 
ATOM   2817 C  C   . GLU A 1 389 ? 4.128   -9.619  12.977  1.00 12.06  ? 375 GLU A C   1 
ATOM   2818 O  O   . GLU A 1 389 ? 4.887   -8.710  13.307  1.00 11.69  ? 375 GLU A O   1 
ATOM   2819 C  CB  . GLU A 1 389 ? 4.525   -10.832 10.840  1.00 12.32  ? 375 GLU A CB  1 
ATOM   2820 C  CG  . GLU A 1 389 ? 5.274   -11.923 10.094  1.00 14.23  ? 375 GLU A CG  1 
ATOM   2821 C  CD  . GLU A 1 389 ? 4.651   -12.235 8.756   1.00 15.07  ? 375 GLU A CD  1 
ATOM   2822 O  OE1 . GLU A 1 389 ? 5.096   -11.588 7.753   1.00 16.43  ? 375 GLU A OE1 1 
ATOM   2823 O  OE2 . GLU A 1 389 ? 3.711   -13.057 8.710   1.00 16.05  ? 375 GLU A OE2 1 
ATOM   2824 N  N   . LEU A 1 390 ? 2.811   -9.590  13.193  1.00 11.67  ? 376 LEU A N   1 
ATOM   2825 C  CA  . LEU A 1 390 ? 2.203   -8.451  13.869  1.00 11.98  ? 376 LEU A CA  1 
ATOM   2826 C  C   . LEU A 1 390 ? 2.640   -8.417  15.320  1.00 11.59  ? 376 LEU A C   1 
ATOM   2827 O  O   . LEU A 1 390 ? 2.887   -7.364  15.877  1.00 11.43  ? 376 LEU A O   1 
ATOM   2828 C  CB  . LEU A 1 390 ? 0.694   -8.497  13.710  1.00 11.38  ? 376 LEU A CB  1 
ATOM   2829 C  CG  . LEU A 1 390 ? 0.198   -8.451  12.282  1.00 11.38  ? 376 LEU A CG  1 
ATOM   2830 C  CD1 . LEU A 1 390 ? -1.302  -8.431  12.244  1.00 12.19  ? 376 LEU A CD1 1 
ATOM   2831 C  CD2 . LEU A 1 390 ? 0.758   -7.273  11.490  1.00 10.99  ? 376 LEU A CD2 1 
ATOM   2832 N  N   . LYS A 1 391 ? 2.713   -9.603  15.955  1.00 13.41  ? 377 LYS A N   1 
ATOM   2833 C  CA  . LYS A 1 391 ? 3.238   -9.672  17.307  1.00 12.15  ? 377 LYS A CA  1 
ATOM   2834 C  C   . LYS A 1 391 ? 4.688   -9.239  17.422  1.00 13.10  ? 377 LYS A C   1 
ATOM   2835 O  O   . LYS A 1 391 ? 5.112   -8.588  18.402  1.00 13.64  ? 377 LYS A O   1 
ATOM   2836 C  CB  . LYS A 1 391 ? 3.057   -11.060 17.934  1.00 14.89  ? 377 LYS A CB  1 
ATOM   2837 C  CG  . LYS A 1 391 ? 1.592   -11.361 18.242  1.00 15.61  ? 377 LYS A CG  1 
ATOM   2838 C  CD  . LYS A 1 391 ? 1.308   -12.611 19.028  1.00 25.44  ? 377 LYS A CD  1 
ATOM   2839 C  CE  . LYS A 1 391 ? 1.898   -13.831 18.379  1.00 29.76  ? 377 LYS A CE  1 
ATOM   2840 N  NZ  . LYS A 1 391 ? 1.580   -15.074 19.127  1.00 31.24  ? 377 LYS A NZ  1 
ATOM   2841 N  N   . MET A 1 392 ? 5.486   -9.587  16.408  1.00 13.15  ? 378 MET A N   1 
ATOM   2842 C  CA  . MET A 1 392 ? 6.870   -9.149  16.412  1.00 12.71  ? 378 MET A CA  1 
ATOM   2843 C  C   . MET A 1 392 ? 6.921   -7.609  16.428  1.00 11.94  ? 378 MET A C   1 
ATOM   2844 O  O   . MET A 1 392 ? 7.683   -7.018  17.156  1.00 13.53  ? 378 MET A O   1 
ATOM   2845 C  CB  . MET A 1 392 ? 7.579   -9.732  15.189  1.00 15.29  ? 378 MET A CB  1 
ATOM   2846 C  CG  . MET A 1 392 ? 8.963   -9.294  14.979  1.00 17.07  ? 378 MET A CG  1 
ATOM   2847 S  SD  . MET A 1 392 ? 9.750   -10.302 13.670  1.00 20.55  ? 378 MET A SD  1 
ATOM   2848 C  CE  . MET A 1 392 ? 11.144  -9.241  13.304  1.00 22.29  ? 378 MET A CE  1 
ATOM   2849 N  N   . MET A 1 393 ? 6.115   -6.949  15.589  1.00 11.66  ? 379 MET A N   1 
ATOM   2850 C  CA  . MET A 1 393 ? 6.098   -5.488  15.584  1.00 11.68  ? 379 MET A CA  1 
ATOM   2851 C  C   . MET A 1 393 ? 5.616   -4.925  16.940  1.00 11.45  ? 379 MET A C   1 
ATOM   2852 O  O   . MET A 1 393 ? 6.236   -3.992  17.438  1.00 12.48  ? 379 MET A O   1 
ATOM   2853 C  CB  . MET A 1 393 ? 5.251   -4.978  14.402  1.00 12.30  ? 379 MET A CB  1 
ATOM   2854 C  CG  . MET A 1 393 ? 5.073   -3.463  14.370  1.00 12.54  ? 379 MET A CG  1 
ATOM   2855 S  SD  . MET A 1 393 ? 6.631   -2.631  13.856  1.00 14.50  ? 379 MET A SD  1 
ATOM   2856 C  CE  . MET A 1 393 ? 6.632   -2.989  12.101  1.00 14.29  ? 379 MET A CE  1 
ATOM   2857 N  N   . LEU A 1 394 ? 4.571   -5.527  17.502  1.00 10.61  ? 380 LEU A N   1 
ATOM   2858 C  CA  . LEU A 1 394 ? 4.091   -5.112  18.812  1.00 12.43  ? 380 LEU A CA  1 
ATOM   2859 C  C   . LEU A 1 394 ? 5.156   -5.266  19.907  1.00 13.39  ? 380 LEU A C   1 
ATOM   2860 O  O   . LEU A 1 394 ? 5.273   -4.420  20.802  1.00 15.31  ? 380 LEU A O   1 
ATOM   2861 C  CB  . LEU A 1 394 ? 2.816   -5.900  19.157  1.00 12.33  ? 380 LEU A CB  1 
ATOM   2862 C  CG  . LEU A 1 394 ? 1.552   -5.314  18.513  1.00 12.67  ? 380 LEU A CG  1 
ATOM   2863 C  CD1 . LEU A 1 394 ? 0.498   -6.386  18.262  1.00 13.41  ? 380 LEU A CD1 1 
ATOM   2864 C  CD2 . LEU A 1 394 ? 0.988   -4.203  19.388  1.00 12.87  ? 380 LEU A CD2 1 
ATOM   2865 N  N   . ASN A 1 395 ? 5.904   -6.388  19.873  1.00 12.82  ? 381 ASN A N   1 
ATOM   2866 C  CA  . ASN A 1 395 ? 6.915   -6.638  20.905  1.00 13.65  ? 381 ASN A CA  1 
ATOM   2867 C  C   . ASN A 1 395 ? 8.141   -5.747  20.750  1.00 14.23  ? 381 ASN A C   1 
ATOM   2868 O  O   . ASN A 1 395 ? 8.775   -5.409  21.764  1.00 17.93  ? 381 ASN A O   1 
ATOM   2869 C  CB  . ASN A 1 395 ? 7.300   -8.107  20.944  1.00 16.63  ? 381 ASN A CB  1 
ATOM   2870 C  CG  . ASN A 1 395 ? 6.232   -8.963  21.574  1.00 17.62  ? 381 ASN A CG  1 
ATOM   2871 O  OD1 . ASN A 1 395 ? 5.603   -8.518  22.530  1.00 21.11  ? 381 ASN A OD1 1 
ATOM   2872 N  ND2 . ASN A 1 395 ? 6.119   -10.199 21.119  1.00 21.41  ? 381 ASN A ND2 1 
ATOM   2873 N  N   . ILE A 1 396 ? 8.471   -5.326  19.515  1.00 13.35  ? 382 ILE A N   1 
ATOM   2874 C  CA  . ILE A 1 396 ? 9.573   -4.403  19.311  1.00 13.34  ? 382 ILE A CA  1 
ATOM   2875 C  C   . ILE A 1 396 ? 9.160   -3.002  19.758  1.00 14.21  ? 382 ILE A C   1 
ATOM   2876 O  O   . ILE A 1 396 ? 9.950   -2.253  20.318  1.00 15.92  ? 382 ILE A O   1 
ATOM   2877 C  CB  . ILE A 1 396 ? 9.979   -4.418  17.831  1.00 15.68  ? 382 ILE A CB  1 
ATOM   2878 C  CG1 . ILE A 1 396 ? 10.518  -5.772  17.372  1.00 19.57  ? 382 ILE A CG1 1 
ATOM   2879 C  CG2 . ILE A 1 396 ? 10.979  -3.307  17.573  1.00 20.84  ? 382 ILE A CG2 1 
ATOM   2880 C  CD1 . ILE A 1 396 ? 10.682  -5.896  15.864  1.00 20.93  ? 382 ILE A CD1 1 
ATOM   2881 N  N   . MET A 1 397 ? 7.931   -2.595  19.440  1.00 13.29  ? 383 MET A N   1 
ATOM   2882 C  CA  . MET A 1 397 ? 7.494   -1.220  19.669  1.00 13.29  ? 383 MET A CA  1 
ATOM   2883 C  C   . MET A 1 397 ? 7.041   -0.976  21.101  1.00 13.67  ? 383 MET A C   1 
ATOM   2884 O  O   . MET A 1 397 ? 7.119   0.163   21.556  1.00 14.80  ? 383 MET A O   1 
ATOM   2885 C  CB  . MET A 1 397 ? 6.386   -0.896  18.659  1.00 12.44  ? 383 MET A CB  1 
ATOM   2886 C  CG  . MET A 1 397 ? 6.870   -0.770  17.215  1.00 12.60  ? 383 MET A CG  1 
ATOM   2887 S  SD  . MET A 1 397 ? 7.916   0.691   17.025  1.00 15.53  ? 383 MET A SD  1 
ATOM   2888 C  CE  . MET A 1 397 ? 8.607   0.388   15.402  1.00 16.71  ? 383 MET A CE  1 
ATOM   2889 N  N   . LYS A 1 398 ? 6.429   -1.985  21.725  1.00 14.47  ? 384 LYS A N   1 
ATOM   2890 C  CA  . LYS A 1 398 ? 5.964   -1.879  23.113  1.00 15.56  ? 384 LYS A CA  1 
ATOM   2891 C  C   . LYS A 1 398 ? 5.131   -0.603  23.313  1.00 15.79  ? 384 LYS A C   1 
ATOM   2892 O  O   . LYS A 1 398 ? 5.388   0.224   24.199  1.00 15.83  ? 384 LYS A O   1 
ATOM   2893 C  CB  . LYS A 1 398 ? 7.110   -1.917  24.142  1.00 17.98  ? 384 LYS A CB  1 
ATOM   2894 C  CG  . LYS A 1 398 ? 7.884   -3.220  24.128  1.00 20.78  ? 384 LYS A CG  1 
ATOM   2895 C  CD  . LYS A 1 398 ? 9.224   -3.118  24.826  1.00 23.60  ? 384 LYS A CD  1 
ATOM   2896 C  CE  . LYS A 1 398 ? 10.229  -2.220  24.140  1.00 27.37  ? 384 LYS A CE  1 
ATOM   2897 N  NZ  . LYS A 1 398 ? 11.614  -2.481  24.591  1.00 35.44  ? 384 LYS A NZ  1 
ATOM   2898 N  N   . PRO A 1 399 ? 4.052   -0.411  22.511  1.00 14.28  ? 385 PRO A N   1 
ATOM   2899 C  CA  . PRO A 1 399 ? 3.340   0.854   22.593  1.00 13.69  ? 385 PRO A CA  1 
ATOM   2900 C  C   . PRO A 1 399 ? 2.498   0.935   23.868  1.00 13.64  ? 385 PRO A C   1 
ATOM   2901 O  O   . PRO A 1 399 ? 1.958   -0.052  24.323  1.00 15.47  ? 385 PRO A O   1 
ATOM   2902 C  CB  . PRO A 1 399 ? 2.459   0.784   21.339  1.00 12.97  ? 385 PRO A CB  1 
ATOM   2903 C  CG  . PRO A 1 399 ? 2.206   -0.679  21.162  1.00 13.79  ? 385 PRO A CG  1 
ATOM   2904 C  CD  . PRO A 1 399 ? 3.501   -1.352  21.528  1.00 13.46  ? 385 PRO A CD  1 
ATOM   2905 N  N   . GLU A 1 400 ? 2.259   2.160   24.297  1.00 14.33  ? 386 GLU A N   1 
ATOM   2906 C  CA  . GLU A 1 400 ? 1.323   2.381   25.383  1.00 14.02  ? 386 GLU A CA  1 
ATOM   2907 C  C   . GLU A 1 400 ? -0.125  2.218   24.927  1.00 12.66  ? 386 GLU A C   1 
ATOM   2908 O  O   . GLU A 1 400 ? -0.908  1.480   25.507  1.00 14.57  ? 386 GLU A O   1 
ATOM   2909 C  CB  . GLU A 1 400 ? 1.559   3.756   25.969  1.00 15.83  ? 386 GLU A CB  1 
ATOM   2910 C  CG  . GLU A 1 400 ? 0.704   4.000   27.210  1.00 19.10  ? 386 GLU A CG  1 
ATOM   2911 C  CD  . GLU A 1 400 ? 0.834   5.354   27.879  1.00 19.02  ? 386 GLU A CD  1 
ATOM   2912 O  OE1 . GLU A 1 400 ? 1.583   6.230   27.388  1.00 22.08  ? 386 GLU A OE1 1 
ATOM   2913 O  OE2 . GLU A 1 400 ? 0.125   5.520   28.900  1.00 22.24  ? 386 GLU A OE2 1 
ATOM   2914 N  N   . TYR A 1 401 ? -0.472  2.843   23.797  1.00 12.27  ? 387 TYR A N   1 
ATOM   2915 C  CA  . TYR A 1 401 ? -1.782  2.807   23.156  1.00 12.31  ? 387 TYR A CA  1 
ATOM   2916 C  C   . TYR A 1 401 ? -1.660  2.172   21.764  1.00 11.51  ? 387 TYR A C   1 
ATOM   2917 O  O   . TYR A 1 401 ? -0.607  2.259   21.120  1.00 12.15  ? 387 TYR A O   1 
ATOM   2918 C  CB  . TYR A 1 401 ? -2.327  4.227   22.972  1.00 12.89  ? 387 TYR A CB  1 
ATOM   2919 C  CG  . TYR A 1 401 ? -2.670  4.881   24.283  1.00 13.16  ? 387 TYR A CG  1 
ATOM   2920 C  CD1 . TYR A 1 401 ? -3.883  4.658   24.887  1.00 14.69  ? 387 TYR A CD1 1 
ATOM   2921 C  CD2 . TYR A 1 401 ? -1.745  5.676   24.947  1.00 13.08  ? 387 TYR A CD2 1 
ATOM   2922 C  CE1 . TYR A 1 401 ? -4.220  5.217   26.114  1.00 15.70  ? 387 TYR A CE1 1 
ATOM   2923 C  CE2 . TYR A 1 401 ? -2.073  6.284   26.158  1.00 16.06  ? 387 TYR A CE2 1 
ATOM   2924 C  CZ  . TYR A 1 401 ? -3.293  6.011   26.761  1.00 14.92  ? 387 TYR A CZ  1 
ATOM   2925 O  OH  . TYR A 1 401 ? -3.659  6.596   27.965  1.00 18.38  ? 387 TYR A OH  1 
ATOM   2926 N  N   . PHE A 1 402 ? -2.717  1.491   21.351  1.00 10.92  ? 388 PHE A N   1 
ATOM   2927 C  CA  . PHE A 1 402 ? -2.688  0.750   20.112  1.00 10.71  ? 388 PHE A CA  1 
ATOM   2928 C  C   . PHE A 1 402 ? -3.961  1.021   19.314  1.00 11.61  ? 388 PHE A C   1 
ATOM   2929 O  O   . PHE A 1 402 ? -5.064  0.941   19.836  1.00 11.94  ? 388 PHE A O   1 
ATOM   2930 C  CB  . PHE A 1 402 ? -2.480  -0.744  20.388  1.00 11.62  ? 388 PHE A CB  1 
ATOM   2931 C  CG  . PHE A 1 402 ? -2.437  -1.597  19.149  1.00 11.92  ? 388 PHE A CG  1 
ATOM   2932 C  CD1 . PHE A 1 402 ? -1.434  -1.401  18.218  1.00 12.89  ? 388 PHE A CD1 1 
ATOM   2933 C  CD2 . PHE A 1 402 ? -3.368  -2.559  18.916  1.00 11.75  ? 388 PHE A CD2 1 
ATOM   2934 C  CE1 . PHE A 1 402 ? -1.408  -2.122  17.048  1.00 12.05  ? 388 PHE A CE1 1 
ATOM   2935 C  CE2 . PHE A 1 402 ? -3.321  -3.301  17.730  1.00 12.02  ? 388 PHE A CE2 1 
ATOM   2936 C  CZ  . PHE A 1 402 ? -2.330  -3.074  16.816  1.00 11.73  ? 388 PHE A CZ  1 
ATOM   2937 N  N   . VAL A 1 403 ? -3.737  1.282   18.022  1.00 10.86  ? 389 VAL A N   1 
ATOM   2938 C  CA  . VAL A 1 403 ? -4.787  1.601   17.076  1.00 9.97   ? 389 VAL A CA  1 
ATOM   2939 C  C   . VAL A 1 403 ? -4.613  0.707   15.859  1.00 10.76  ? 389 VAL A C   1 
ATOM   2940 O  O   . VAL A 1 403 ? -3.843  1.030   14.947  1.00 10.32  ? 389 VAL A O   1 
ATOM   2941 C  CB  . VAL A 1 403 ? -4.763  3.090   16.679  1.00 10.96  ? 389 VAL A CB  1 
ATOM   2942 C  CG1 . VAL A 1 403 ? -6.004  3.391   15.817  1.00 12.80  ? 389 VAL A CG1 1 
ATOM   2943 C  CG2 . VAL A 1 403 ? -4.730  4.010   17.897  1.00 13.79  ? 389 VAL A CG2 1 
ATOM   2944 N  N   . PRO A 1 404 ? -5.325  -0.443  15.792  1.00 9.49   ? 390 PRO A N   1 
ATOM   2945 C  CA  . PRO A 1 404 ? -5.222  -1.291  14.607  1.00 8.92   ? 390 PRO A CA  1 
ATOM   2946 C  C   . PRO A 1 404 ? -5.967  -0.669  13.442  1.00 9.74   ? 390 PRO A C   1 
ATOM   2947 O  O   . PRO A 1 404 ? -7.129  -0.316  13.585  1.00 10.60  ? 390 PRO A O   1 
ATOM   2948 C  CB  . PRO A 1 404 ? -5.843  -2.607  15.069  1.00 11.23  ? 390 PRO A CB  1 
ATOM   2949 C  CG  . PRO A 1 404 ? -6.773  -2.243  16.197  1.00 12.12  ? 390 PRO A CG  1 
ATOM   2950 C  CD  . PRO A 1 404 ? -6.111  -1.071  16.879  1.00 11.31  ? 390 PRO A CD  1 
ATOM   2951 N  N   . VAL A 1 405 ? -5.289  -0.622  12.295  1.00 9.75   ? 391 VAL A N   1 
ATOM   2952 C  CA  . VAL A 1 405 ? -5.866  -0.039  11.090  1.00 9.65   ? 391 VAL A CA  1 
ATOM   2953 C  C   . VAL A 1 405 ? -5.649  -0.970  9.927   1.00 9.39   ? 391 VAL A C   1 
ATOM   2954 O  O   . VAL A 1 405 ? -5.250  -2.122  10.124  1.00 10.48  ? 391 VAL A O   1 
ATOM   2955 C  CB  . VAL A 1 405 ? -5.358  1.399   10.844  1.00 9.17   ? 391 VAL A CB  1 
ATOM   2956 C  CG1 . VAL A 1 405 ? -5.642  2.331   12.018  1.00 10.37  ? 391 VAL A CG1 1 
ATOM   2957 C  CG2 . VAL A 1 405 ? -3.886  1.390   10.474  1.00 9.57   ? 391 VAL A CG2 1 
ATOM   2958 N  N   . GLN A 1 406 ? -5.997  -0.541  8.735   1.00 9.57   ? 392 GLN A N   1 
ATOM   2959 C  CA  A GLN A 1 406 ? -5.926  -1.344  7.525   0.50 10.56  ? 392 GLN A CA  1 
ATOM   2960 C  CA  B GLN A 1 406 ? -5.903  -1.350  7.525   0.50 10.59  ? 392 GLN A CA  1 
ATOM   2961 C  C   . GLN A 1 406 ? -6.603  -2.691  7.720   1.00 11.90  ? 392 GLN A C   1 
ATOM   2962 O  O   . GLN A 1 406 ? -6.016  -3.804  7.703   1.00 12.11  ? 392 GLN A O   1 
ATOM   2963 C  CB  A GLN A 1 406 ? -4.528  -1.493  6.957   0.50 10.80  ? 392 GLN A CB  1 
ATOM   2964 C  CB  B GLN A 1 406 ? -4.470  -1.509  7.042   0.50 11.19  ? 392 GLN A CB  1 
ATOM   2965 C  CG  A GLN A 1 406 ? -4.614  -2.041  5.536   0.50 12.35  ? 392 GLN A CG  1 
ATOM   2966 C  CG  B GLN A 1 406 ? -4.381  -2.036  5.611   0.50 13.97  ? 392 GLN A CG  1 
ATOM   2967 C  CD  A GLN A 1 406 ? -3.343  -1.867  4.751   0.50 16.93  ? 392 GLN A CD  1 
ATOM   2968 C  CD  B GLN A 1 406 ? -4.510  -0.940  4.582   0.50 28.77  ? 392 GLN A CD  1 
ATOM   2969 N  NE2 A GLN A 1 406 ? -2.372  -1.202  5.343   0.50 19.80  ? 392 GLN A NE2 1 
ATOM   2970 N  NE2 B GLN A 1 406 ? -5.652  -0.268  4.541   0.50 13.44  ? 392 GLN A NE2 1 
ATOM   2971 N  N   . GLY A 1 407 ? -7.914  -2.611  7.865   1.00 11.44  ? 393 GLY A N   1 
ATOM   2972 C  CA  . GLY A 1 407 ? -8.706  -3.826  7.964   1.00 13.86  ? 393 GLY A CA  1 
ATOM   2973 C  C   . GLY A 1 407 ? -10.184 -3.540  8.154   1.00 14.16  ? 393 GLY A C   1 
ATOM   2974 O  O   . GLY A 1 407 ? -10.588 -2.511  8.654   1.00 12.87  ? 393 GLY A O   1 
ATOM   2975 N  N   . GLU A 1 408 ? -10.942 -4.563  7.777   1.00 14.25  ? 394 GLU A N   1 
ATOM   2976 C  CA  . GLU A 1 408 ? -12.320 -4.666  8.174   1.00 14.70  ? 394 GLU A CA  1 
ATOM   2977 C  C   . GLU A 1 408 ? -12.349 -4.748  9.690   1.00 13.77  ? 394 GLU A C   1 
ATOM   2978 O  O   . GLU A 1 408 ? -11.347 -5.101  10.337  1.00 13.31  ? 394 GLU A O   1 
ATOM   2979 C  CB  . GLU A 1 408 ? -12.958 -5.916  7.581   1.00 16.67  ? 394 GLU A CB  1 
ATOM   2980 C  CG  . GLU A 1 408 ? -13.031 -5.922  6.071   1.00 21.66  ? 394 GLU A CG  1 
ATOM   2981 C  CD  . GLU A 1 408 ? -13.808 -7.181  5.671   1.00 29.78  ? 394 GLU A CD  1 
ATOM   2982 O  OE1 . GLU A 1 408 ? -15.049 -7.157  5.764   1.00 53.11  ? 394 GLU A OE1 1 
ATOM   2983 O  OE2 . GLU A 1 408 ? -13.179 -8.227  5.460   1.00 36.22  ? 394 GLU A OE2 1 
ATOM   2984 N  N   . PHE A 1 409 ? -13.521 -4.527  10.272  1.00 15.10  ? 395 PHE A N   1 
ATOM   2985 C  CA  . PHE A 1 409 ? -13.636 -4.516  11.714  1.00 14.58  ? 395 PHE A CA  1 
ATOM   2986 C  C   . PHE A 1 409 ? -13.154 -5.836  12.337  1.00 15.47  ? 395 PHE A C   1 
ATOM   2987 O  O   . PHE A 1 409 ? -12.420 -5.859  13.338  1.00 14.89  ? 395 PHE A O   1 
ATOM   2988 C  CB  . PHE A 1 409 ? -15.041 -4.146  12.167  1.00 18.32  ? 395 PHE A CB  1 
ATOM   2989 C  CG  . PHE A 1 409 ? -15.083 -3.603  13.571  1.00 21.56  ? 395 PHE A CG  1 
ATOM   2990 C  CD1 . PHE A 1 409 ? -14.532 -2.359  13.866  1.00 26.87  ? 395 PHE A CD1 1 
ATOM   2991 C  CD2 . PHE A 1 409 ? -15.679 -4.316  14.596  1.00 25.94  ? 395 PHE A CD2 1 
ATOM   2992 C  CE1 . PHE A 1 409 ? -14.591 -1.837  15.147  1.00 34.85  ? 395 PHE A CE1 1 
ATOM   2993 C  CE2 . PHE A 1 409 ? -15.750 -3.793  15.881  1.00 26.10  ? 395 PHE A CE2 1 
ATOM   2994 C  CZ  . PHE A 1 409 ? -15.185 -2.564  16.151  1.00 27.30  ? 395 PHE A CZ  1 
ATOM   2995 N  N   . LYS A 1 410 ? -13.537 -6.964  11.736  1.00 14.81  ? 396 LYS A N   1 
ATOM   2996 C  CA  . LYS A 1 410 ? -13.068 -8.246  12.239  1.00 16.37  ? 396 LYS A CA  1 
ATOM   2997 C  C   . LYS A 1 410 ? -11.548 -8.414  12.250  1.00 14.45  ? 396 LYS A C   1 
ATOM   2998 O  O   . LYS A 1 410 ? -11.012 -9.068  13.138  1.00 14.18  ? 396 LYS A O   1 
ATOM   2999 C  CB  . LYS A 1 410 ? -13.719 -9.365  11.431  1.00 16.48  ? 396 LYS A CB  1 
ATOM   3000 C  CG  . LYS A 1 410 ? -13.249 -9.546  10.004  1.00 20.99  ? 396 LYS A CG  1 
ATOM   3001 C  CD  . LYS A 1 410 ? -14.167 -10.467 9.215   1.00 26.04  ? 396 LYS A CD  1 
ATOM   3002 C  CE  . LYS A 1 410 ? -13.550 -10.810 7.882   1.00 31.58  ? 396 LYS A CE  1 
ATOM   3003 N  NZ  . LYS A 1 410 ? -14.439 -11.684 7.077   1.00 42.00  ? 396 LYS A NZ  1 
ATOM   3004 N  N   . MET A 1 411 ? -10.850 -7.808  11.280  1.00 13.15  ? 397 MET A N   1 
ATOM   3005 C  CA  . MET A 1 411 ? -9.394  -7.823  11.260  1.00 12.56  ? 397 MET A CA  1 
ATOM   3006 C  C   . MET A 1 411 ? -8.842  -6.932  12.368  1.00 11.15  ? 397 MET A C   1 
ATOM   3007 O  O   . MET A 1 411 ? -7.829  -7.251  13.029  1.00 11.21  ? 397 MET A O   1 
ATOM   3008 C  CB  . MET A 1 411 ? -8.891  -7.358  9.886   1.00 11.93  ? 397 MET A CB  1 
ATOM   3009 C  CG  . MET A 1 411 ? -9.310  -8.271  8.761   1.00 14.57  ? 397 MET A CG  1 
ATOM   3010 S  SD  . MET A 1 411 ? -9.083  -7.443  7.163   1.00 16.79  ? 397 MET A SD  1 
ATOM   3011 C  CE  . MET A 1 411 ? -9.736  -8.698  6.073   1.00 20.44  ? 397 MET A CE  1 
ATOM   3012 N  N   . GLN A 1 412 ? -9.458  -5.754  12.523  1.00 11.71  ? 398 GLN A N   1 
ATOM   3013 C  CA  . GLN A 1 412 ? -9.015  -4.879  13.599  1.00 11.02  ? 398 GLN A CA  1 
ATOM   3014 C  C   . GLN A 1 412 ? -9.169  -5.532  14.984  1.00 13.02  ? 398 GLN A C   1 
ATOM   3015 O  O   . GLN A 1 412 ? -8.271  -5.427  15.818  1.00 12.02  ? 398 GLN A O   1 
ATOM   3016 C  CB  . GLN A 1 412 ? -9.805  -3.571  13.610  1.00 11.24  ? 398 GLN A CB  1 
ATOM   3017 C  CG  . GLN A 1 412 ? -9.630  -2.730  12.330  1.00 13.20  ? 398 GLN A CG  1 
ATOM   3018 C  CD  . GLN A 1 412 ? -10.552 -1.539  12.358  1.00 12.71  ? 398 GLN A CD  1 
ATOM   3019 O  OE1 . GLN A 1 412 ? -10.260 -0.481  12.940  1.00 15.58  ? 398 GLN A OE1 1 
ATOM   3020 N  NE2 . GLN A 1 412 ? -11.628 -1.674  11.662  1.00 14.24  ? 398 GLN A NE2 1 
ATOM   3021 N  N   . ILE A 1 413 ? -10.281 -6.280  15.183  1.00 12.36  ? 399 ILE A N   1 
ATOM   3022 C  CA  . ILE A 1 413 ? -10.480 -7.023  16.422  1.00 12.46  ? 399 ILE A CA  1 
ATOM   3023 C  C   . ILE A 1 413 ? -9.413  -8.108  16.573  1.00 12.76  ? 399 ILE A C   1 
ATOM   3024 O  O   . ILE A 1 413 ? -8.838  -8.257  17.641  1.00 12.71  ? 399 ILE A O   1 
ATOM   3025 C  CB  . ILE A 1 413 ? -11.886 -7.661  16.495  1.00 14.92  ? 399 ILE A CB  1 
ATOM   3026 C  CG1 . ILE A 1 413 ? -12.974 -6.592  16.614  1.00 17.91  ? 399 ILE A CG1 1 
ATOM   3027 C  CG2 . ILE A 1 413 ? -11.970 -8.698  17.627  1.00 18.20  ? 399 ILE A CG2 1 
ATOM   3028 C  CD1 . ILE A 1 413 ? -14.360 -7.100  16.290  1.00 20.41  ? 399 ILE A CD1 1 
ATOM   3029 N  N   . ALA A 1 414 ? -9.120  -8.836  15.493  1.00 12.46  ? 400 ALA A N   1 
ATOM   3030 C  CA  . ALA A 1 414 ? -8.079  -9.877  15.608  1.00 13.08  ? 400 ALA A CA  1 
ATOM   3031 C  C   . ALA A 1 414 ? -6.753  -9.251  16.003  1.00 13.38  ? 400 ALA A C   1 
ATOM   3032 O  O   . ALA A 1 414 ? -6.033  -9.780  16.857  1.00 13.39  ? 400 ALA A O   1 
ATOM   3033 C  CB  . ALA A 1 414 ? -7.964  -10.596 14.288  1.00 14.78  ? 400 ALA A CB  1 
ATOM   3034 N  N   . HIS A 1 415 ? -6.475  -8.046  15.461  1.00 11.94  ? 401 HIS A N   1 
ATOM   3035 C  CA  . HIS A 1 415 ? -5.201  -7.418  15.745  1.00 10.82  ? 401 HIS A CA  1 
ATOM   3036 C  C   . HIS A 1 415 ? -5.137  -6.908  17.183  1.00 11.12  ? 401 HIS A C   1 
ATOM   3037 O  O   . HIS A 1 415 ? -4.130  -6.992  17.892  1.00 12.55  ? 401 HIS A O   1 
ATOM   3038 C  CB  . HIS A 1 415 ? -4.939  -6.288  14.751  1.00 10.00  ? 401 HIS A CB  1 
ATOM   3039 C  CG  . HIS A 1 415 ? -3.522  -5.859  14.604  1.00 10.82  ? 401 HIS A CG  1 
ATOM   3040 N  ND1 . HIS A 1 415 ? -3.182  -4.998  13.591  1.00 10.58  ? 401 HIS A ND1 1 
ATOM   3041 C  CD2 . HIS A 1 415 ? -2.362  -6.197  15.248  1.00 9.95   ? 401 HIS A CD2 1 
ATOM   3042 C  CE1 . HIS A 1 415 ? -1.862  -4.813  13.651  1.00 10.39  ? 401 HIS A CE1 1 
ATOM   3043 N  NE2 . HIS A 1 415 ? -1.320  -5.543  14.644  1.00 10.60  ? 401 HIS A NE2 1 
ATOM   3044 N  N   . ALA A 1 416 ? -6.257  -6.376  17.664  1.00 13.00  ? 402 ALA A N   1 
ATOM   3045 C  CA  . ALA A 1 416 ? -6.404  -5.936  19.027  1.00 12.64  ? 402 ALA A CA  1 
ATOM   3046 C  C   . ALA A 1 416 ? -6.128  -7.100  19.987  1.00 13.04  ? 402 ALA A C   1 
ATOM   3047 O  O   . ALA A 1 416 ? -5.472  -6.914  21.027  1.00 13.97  ? 402 ALA A O   1 
ATOM   3048 C  CB  . ALA A 1 416 ? -7.796  -5.391  19.235  1.00 13.94  ? 402 ALA A CB  1 
ATOM   3049 N  N   . LYS A 1 417 ? -6.648  -8.297  19.695  1.00 14.40  ? 403 LYS A N   1 
ATOM   3050 C  CA  . LYS A 1 417 ? -6.382  -9.493  20.516  1.00 14.67  ? 403 LYS A CA  1 
ATOM   3051 C  C   . LYS A 1 417 ? -4.884  -9.797  20.571  1.00 14.83  ? 403 LYS A C   1 
ATOM   3052 O  O   . LYS A 1 417 ? -4.358  -10.106 21.654  1.00 16.87  ? 403 LYS A O   1 
ATOM   3053 C  CB  . LYS A 1 417 ? -7.147  -10.722 20.044  1.00 16.28  ? 403 LYS A CB  1 
ATOM   3054 C  CG  . LYS A 1 417 ? -8.652  -10.613 20.223  1.00 18.20  ? 403 LYS A CG  1 
ATOM   3055 C  CD  . LYS A 1 417 ? -9.537  -11.644 19.467  1.00 21.37  ? 403 LYS A CD  1 
ATOM   3056 C  CE  . LYS A 1 417 ? -11.016 -11.436 19.774  1.00 23.36  ? 403 LYS A CE  1 
ATOM   3057 N  NZ  . LYS A 1 417 ? -11.919 -12.317 18.974  1.00 23.85  ? 403 LYS A NZ  1 
ATOM   3058 N  N   . LEU A 1 418 ? -4.187  -9.676  19.429  1.00 14.56  ? 404 LEU A N   1 
ATOM   3059 C  CA  . LEU A 1 418 ? -2.741  -9.842  19.436  1.00 14.71  ? 404 LEU A CA  1 
ATOM   3060 C  C   . LEU A 1 418 ? -2.066  -8.823  20.345  1.00 13.80  ? 404 LEU A C   1 
ATOM   3061 O  O   . LEU A 1 418 ? -1.130  -9.137  21.096  1.00 14.77  ? 404 LEU A O   1 
ATOM   3062 C  CB  . LEU A 1 418 ? -2.185  -9.726  18.005  1.00 12.49  ? 404 LEU A CB  1 
ATOM   3063 C  CG  . LEU A 1 418 ? -2.721  -10.734 16.999  1.00 14.68  ? 404 LEU A CG  1 
ATOM   3064 C  CD1 . LEU A 1 418 ? -2.225  -10.443 15.594  1.00 15.84  ? 404 LEU A CD1 1 
ATOM   3065 C  CD2 . LEU A 1 418 ? -2.394  -12.149 17.387  1.00 16.05  ? 404 LEU A CD2 1 
ATOM   3066 N  N   . ALA A 1 419 ? -2.500  -7.550  20.253  1.00 13.41  ? 405 ALA A N   1 
ATOM   3067 C  CA  . ALA A 1 419 ? -1.892  -6.532  21.084  1.00 13.19  ? 405 ALA A CA  1 
ATOM   3068 C  C   . ALA A 1 419 ? -2.040  -6.862  22.571  1.00 15.15  ? 405 ALA A C   1 
ATOM   3069 O  O   . ALA A 1 419 ? -1.099  -6.733  23.338  1.00 15.23  ? 405 ALA A O   1 
ATOM   3070 C  CB  . ALA A 1 419 ? -2.458  -5.168  20.772  1.00 13.80  ? 405 ALA A CB  1 
ATOM   3071 N  N   . ALA A 1 420 ? -3.247  -7.259  22.961  1.00 14.68  ? 406 ALA A N   1 
ATOM   3072 C  CA  . ALA A 1 420 ? -3.493  -7.642  24.351  1.00 15.17  ? 406 ALA A CA  1 
ATOM   3073 C  C   . ALA A 1 420 ? -2.598  -8.835  24.753  1.00 17.80  ? 406 ALA A C   1 
ATOM   3074 O  O   . ALA A 1 420 ? -2.035  -8.852  25.862  1.00 18.75  ? 406 ALA A O   1 
ATOM   3075 C  CB  . ALA A 1 420 ? -4.952  -7.934  24.557  1.00 18.82  ? 406 ALA A CB  1 
ATOM   3076 N  N   . GLU A 1 421 ? -2.416  -9.817  23.854  1.00 16.75  ? 407 GLU A N   1 
ATOM   3077 C  CA  . GLU A 1 421 ? -1.542  -10.955 24.144  1.00 16.93  ? 407 GLU A CA  1 
ATOM   3078 C  C   . GLU A 1 421 ? -0.112  -10.468 24.418  1.00 18.82  ? 407 GLU A C   1 
ATOM   3079 O  O   . GLU A 1 421 ? 0.599   -11.045 25.250  1.00 21.67  ? 407 GLU A O   1 
ATOM   3080 C  CB  . GLU A 1 421 ? -1.639  -11.915 22.945  1.00 19.92  ? 407 GLU A CB  1 
ATOM   3081 C  CG  . GLU A 1 421 ? -0.758  -13.143 22.945  1.00 28.97  ? 407 GLU A CG  1 
ATOM   3082 C  CD  . GLU A 1 421 ? -1.002  -14.048 21.740  1.00 33.67  ? 407 GLU A CD  1 
ATOM   3083 O  OE1 . GLU A 1 421 ? -1.958  -13.795 20.943  1.00 35.40  ? 407 GLU A OE1 1 
ATOM   3084 O  OE2 . GLU A 1 421 ? -0.228  -15.007 21.581  1.00 39.16  ? 407 GLU A OE2 1 
ATOM   3085 N  N   . THR A 1 422 ? 0.366   -9.451  23.679  1.00 16.75  ? 408 THR A N   1 
ATOM   3086 C  CA  . THR A 1 422 ? 1.723   -8.973  23.857  1.00 15.37  ? 408 THR A CA  1 
ATOM   3087 C  C   . THR A 1 422 ? 1.885   -8.100  25.098  1.00 17.88  ? 408 THR A C   1 
ATOM   3088 O  O   . THR A 1 422 ? 2.992   -7.680  25.422  1.00 21.13  ? 408 THR A O   1 
ATOM   3089 C  CB  . THR A 1 422 ? 2.288   -8.239  22.635  1.00 15.71  ? 408 THR A CB  1 
ATOM   3090 O  OG1 . THR A 1 422 ? 1.613   -6.996  22.472  1.00 16.07  ? 408 THR A OG1 1 
ATOM   3091 C  CG2 . THR A 1 422 ? 2.242   -9.085  21.381  1.00 16.27  ? 408 THR A CG2 1 
ATOM   3092 N  N   . GLY A 1 423 ? 0.782   -7.708  25.731  1.00 16.97  ? 409 GLY A N   1 
ATOM   3093 C  CA  . GLY A 1 423 ? 0.908   -6.923  26.949  1.00 18.80  ? 409 GLY A CA  1 
ATOM   3094 C  C   . GLY A 1 423 ? 0.361   -5.497  26.862  1.00 17.19  ? 409 GLY A C   1 
ATOM   3095 O  O   . GLY A 1 423 ? 0.511   -4.735  27.821  1.00 21.66  ? 409 GLY A O   1 
ATOM   3096 N  N   . VAL A 1 424 ? -0.228  -5.078  25.726  1.00 17.37  ? 410 VAL A N   1 
ATOM   3097 C  CA  . VAL A 1 424 ? -0.831  -3.757  25.688  1.00 16.86  ? 410 VAL A CA  1 
ATOM   3098 C  C   . VAL A 1 424 ? -2.053  -3.783  26.611  1.00 17.68  ? 410 VAL A C   1 
ATOM   3099 O  O   . VAL A 1 424 ? -2.869  -4.690  26.534  1.00 18.43  ? 410 VAL A O   1 
ATOM   3100 C  CB  . VAL A 1 424 ? -1.215  -3.316  24.264  1.00 14.89  ? 410 VAL A CB  1 
ATOM   3101 C  CG1 . VAL A 1 424 ? -1.862  -1.930  24.274  1.00 15.70  ? 410 VAL A CG1 1 
ATOM   3102 C  CG2 . VAL A 1 424 ? -0.014  -3.366  23.321  1.00 15.26  ? 410 VAL A CG2 1 
ATOM   3103 N  N   . ALA A 1 425 ? -2.209  -2.739  27.454  1.00 18.89  ? 411 ALA A N   1 
ATOM   3104 C  CA  . ALA A 1 425 ? -3.380  -2.667  28.308  1.00 19.76  ? 411 ALA A CA  1 
ATOM   3105 C  C   . ALA A 1 425 ? -4.642  -2.683  27.448  1.00 19.18  ? 411 ALA A C   1 
ATOM   3106 O  O   . ALA A 1 425 ? -4.764  -1.859  26.538  1.00 17.89  ? 411 ALA A O   1 
ATOM   3107 C  CB  . ALA A 1 425 ? -3.318  -1.423  29.178  1.00 21.19  ? 411 ALA A CB  1 
ATOM   3108 N  N   . PRO A 1 426 ? -5.637  -3.572  27.691  1.00 20.08  ? 412 PRO A N   1 
ATOM   3109 C  CA  . PRO A 1 426 ? -6.837  -3.624  26.848  1.00 21.06  ? 412 PRO A CA  1 
ATOM   3110 C  C   . PRO A 1 426 ? -7.631  -2.312  26.756  1.00 17.67  ? 412 PRO A C   1 
ATOM   3111 O  O   . PRO A 1 426 ? -8.189  -1.994  25.708  1.00 19.35  ? 412 PRO A O   1 
ATOM   3112 C  CB  . PRO A 1 426 ? -7.695  -4.747  27.427  1.00 25.95  ? 412 PRO A CB  1 
ATOM   3113 C  CG  . PRO A 1 426 ? -7.104  -5.012  28.790  1.00 37.07  ? 412 PRO A CG  1 
ATOM   3114 C  CD  . PRO A 1 426 ? -5.649  -4.616  28.734  1.00 25.97  ? 412 PRO A CD  1 
ATOM   3115 N  N   . GLU A 1 427 ? -7.671  -1.552  27.861  1.00 21.39  ? 413 GLU A N   1 
ATOM   3116 C  CA  . GLU A 1 427 ? -8.357  -0.264  27.853  1.00 19.08  ? 413 GLU A CA  1 
ATOM   3117 C  C   . GLU A 1 427 ? -7.596  0.777   27.017  1.00 18.05  ? 413 GLU A C   1 
ATOM   3118 O  O   . GLU A 1 427 ? -8.099  1.883   26.840  1.00 19.83  ? 413 GLU A O   1 
ATOM   3119 C  CB  . GLU A 1 427 ? -8.577  0.206   29.304  1.00 22.66  ? 413 GLU A CB  1 
ATOM   3120 C  CG  . GLU A 1 427 ? -7.348  0.729   30.020  1.00 33.80  ? 413 GLU A CG  1 
ATOM   3121 C  CD  . GLU A 1 427 ? -6.421  -0.280  30.688  1.00 46.63  ? 413 GLU A CD  1 
ATOM   3122 O  OE1 . GLU A 1 427 ? -6.667  -1.539  30.616  1.00 36.40  ? 413 GLU A OE1 1 
ATOM   3123 O  OE2 . GLU A 1 427 ? -5.449  0.204   31.325  1.00 45.36  ? 413 GLU A OE2 1 
ATOM   3124 N  N   . LYS A 1 428 ? -6.342  0.494   26.623  1.00 16.19  ? 414 LYS A N   1 
ATOM   3125 C  CA  . LYS A 1 428 ? -5.554  1.395   25.777  1.00 15.09  ? 414 LYS A CA  1 
ATOM   3126 C  C   . LYS A 1 428 ? -5.545  0.968   24.294  1.00 12.69  ? 414 LYS A C   1 
ATOM   3127 O  O   . LYS A 1 428 ? -4.764  1.510   23.519  1.00 13.95  ? 414 LYS A O   1 
ATOM   3128 C  CB  . LYS A 1 428 ? -4.149  1.516   26.360  1.00 14.96  ? 414 LYS A CB  1 
ATOM   3129 C  CG  . LYS A 1 428 ? -4.136  2.136   27.751  1.00 17.06  ? 414 LYS A CG  1 
ATOM   3130 C  CD  . LYS A 1 428 ? -2.776  2.540   28.253  1.00 15.99  ? 414 LYS A CD  1 
ATOM   3131 C  CE  . LYS A 1 428 ? -2.842  3.128   29.628  1.00 19.57  ? 414 LYS A CE  1 
ATOM   3132 N  NZ  . LYS A 1 428 ? -1.506  3.453   30.137  1.00 24.20  ? 414 LYS A NZ  1 
ATOM   3133 N  N   . ILE A 1 429 ? -6.388  0.042   23.934  1.00 13.58  ? 415 ILE A N   1 
ATOM   3134 C  CA  . ILE A 1 429 ? -6.586  -0.383  22.571  1.00 12.55  ? 415 ILE A CA  1 
ATOM   3135 C  C   . ILE A 1 429 ? -7.853  0.252   22.048  1.00 13.00  ? 415 ILE A C   1 
ATOM   3136 O  O   . ILE A 1 429 ? -8.924  0.083   22.616  1.00 15.57  ? 415 ILE A O   1 
ATOM   3137 C  CB  . ILE A 1 429 ? -6.640  -1.915  22.427  1.00 15.50  ? 415 ILE A CB  1 
ATOM   3138 C  CG1 . ILE A 1 429 ? -5.378  -2.563  23.002  1.00 15.19  ? 415 ILE A CG1 1 
ATOM   3139 C  CG2 . ILE A 1 429 ? -6.904  -2.331  20.978  1.00 14.97  ? 415 ILE A CG2 1 
ATOM   3140 C  CD1 . ILE A 1 429 ? -5.494  -4.095  23.122  1.00 18.17  ? 415 ILE A CD1 1 
ATOM   3141 N  N   . PHE A 1 430 ? -7.737  0.979   20.928  1.00 13.62  ? 416 PHE A N   1 
ATOM   3142 C  CA  . PHE A 1 430 ? -8.877  1.707   20.381  1.00 13.39  ? 416 PHE A CA  1 
ATOM   3143 C  C   . PHE A 1 430 ? -9.262  1.114   19.027  1.00 14.60  ? 416 PHE A C   1 
ATOM   3144 O  O   . PHE A 1 430 ? -8.429  1.087   18.124  1.00 15.93  ? 416 PHE A O   1 
ATOM   3145 C  CB  . PHE A 1 430 ? -8.559  3.209   20.297  1.00 16.49  ? 416 PHE A CB  1 
ATOM   3146 C  CG  . PHE A 1 430 ? -8.623  3.900   21.630  1.00 14.47  ? 416 PHE A CG  1 
ATOM   3147 C  CD1 . PHE A 1 430 ? -7.604  3.769   22.561  1.00 17.00  ? 416 PHE A CD1 1 
ATOM   3148 C  CD2 . PHE A 1 430 ? -9.750  4.624   21.973  1.00 16.17  ? 416 PHE A CD2 1 
ATOM   3149 C  CE1 . PHE A 1 430 ? -7.703  4.360   23.814  1.00 16.18  ? 416 PHE A CE1 1 
ATOM   3150 C  CE2 . PHE A 1 430 ? -9.885  5.172   23.241  1.00 19.42  ? 416 PHE A CE2 1 
ATOM   3151 C  CZ  . PHE A 1 430 ? -8.853  5.057   24.160  1.00 17.71  ? 416 PHE A CZ  1 
ATOM   3152 N  N   . LEU A 1 431 ? -10.509 0.673   18.901  1.00 13.87  ? 417 LEU A N   1 
ATOM   3153 C  CA  . LEU A 1 431 ? -11.099 0.124   17.696  1.00 13.84  ? 417 LEU A CA  1 
ATOM   3154 C  C   . LEU A 1 431 ? -11.937 1.213   17.054  1.00 13.94  ? 417 LEU A C   1 
ATOM   3155 O  O   . LEU A 1 431 ? -12.976 1.568   17.607  1.00 18.93  ? 417 LEU A O   1 
ATOM   3156 C  CB  . LEU A 1 431 ? -12.018 -1.050  18.055  1.00 17.64  ? 417 LEU A CB  1 
ATOM   3157 C  CG  . LEU A 1 431 ? -11.313 -2.322  18.514  1.00 17.93  ? 417 LEU A CG  1 
ATOM   3158 C  CD1 . LEU A 1 431 ? -12.352 -3.338  19.002  1.00 25.13  ? 417 LEU A CD1 1 
ATOM   3159 C  CD2 . LEU A 1 431 ? -10.473 -2.948  17.427  1.00 22.47  ? 417 LEU A CD2 1 
ATOM   3160 N  N   . VAL A 1 432 ? -11.471 1.732   15.922  1.00 12.95  ? 418 VAL A N   1 
ATOM   3161 C  CA  . VAL A 1 432 ? -12.045 2.950   15.356  1.00 14.07  ? 418 VAL A CA  1 
ATOM   3162 C  C   . VAL A 1 432 ? -12.713 2.665   14.001  1.00 12.54  ? 418 VAL A C   1 
ATOM   3163 O  O   . VAL A 1 432 ? -12.319 1.757   13.256  1.00 14.68  ? 418 VAL A O   1 
ATOM   3164 C  CB  . VAL A 1 432 ? -10.966 4.049   15.187  1.00 16.83  ? 418 VAL A CB  1 
ATOM   3165 C  CG1 . VAL A 1 432 ? -10.512 4.586   16.540  1.00 26.18  ? 418 VAL A CG1 1 
ATOM   3166 C  CG2 . VAL A 1 432 ? -9.804  3.572   14.317  1.00 18.26  ? 418 VAL A CG2 1 
ATOM   3167 N  N   . GLU A 1 433 ? -13.698 3.517   13.647  1.00 11.94  ? 419 GLU A N   1 
ATOM   3168 C  CA  . GLU A 1 433 ? -14.321 3.609   12.348  1.00 12.82  ? 419 GLU A CA  1 
ATOM   3169 C  C   . GLU A 1 433 ? -13.877 4.920   11.679  1.00 11.83  ? 419 GLU A C   1 
ATOM   3170 O  O   . GLU A 1 433 ? -13.372 5.820   12.324  1.00 11.86  ? 419 GLU A O   1 
ATOM   3171 C  CB  . GLU A 1 433 ? -15.851 3.578   12.442  1.00 17.93  ? 419 GLU A CB  1 
ATOM   3172 C  CG  . GLU A 1 433 ? -16.402 2.271   12.934  1.00 22.18  ? 419 GLU A CG  1 
ATOM   3173 C  CD  . GLU A 1 433 ? -17.904 2.305   13.141  1.00 36.71  ? 419 GLU A CD  1 
ATOM   3174 O  OE1 . GLU A 1 433 ? -18.331 2.811   14.178  1.00 38.28  ? 419 GLU A OE1 1 
ATOM   3175 O  OE2 . GLU A 1 433 ? -18.630 1.834   12.256  1.00 51.91  ? 419 GLU A OE2 1 
ATOM   3176 N  N   . LYS A 1 434 ? -14.099 5.007   10.388  1.00 11.74  ? 420 LYS A N   1 
ATOM   3177 C  CA  . LYS A 1 434 ? -13.783 6.217   9.657   1.00 11.13  ? 420 LYS A CA  1 
ATOM   3178 C  C   . LYS A 1 434 ? -14.469 7.421   10.290  1.00 11.56  ? 420 LYS A C   1 
ATOM   3179 O  O   . LYS A 1 434 ? -15.646 7.362   10.671  1.00 12.48  ? 420 LYS A O   1 
ATOM   3180 C  CB  . LYS A 1 434 ? -14.164 6.127   8.184   1.00 12.87  ? 420 LYS A CB  1 
ATOM   3181 C  CG  . LYS A 1 434 ? -13.306 5.181   7.376   1.00 12.76  ? 420 LYS A CG  1 
ATOM   3182 C  CD  . LYS A 1 434 ? -13.723 5.107   5.912   1.00 14.61  ? 420 LYS A CD  1 
ATOM   3183 C  CE  . LYS A 1 434 ? -15.058 4.447   5.651   1.00 18.55  ? 420 LYS A CE  1 
ATOM   3184 N  NZ  . LYS A 1 434 ? -15.040 2.997   5.892   1.00 20.09  ? 420 LYS A NZ  1 
ATOM   3185 N  N   . GLY A 1 435 ? -13.703 8.512   10.490  1.00 10.85  ? 421 GLY A N   1 
ATOM   3186 C  CA  . GLY A 1 435 ? -14.207 9.727   11.065  1.00 11.16  ? 421 GLY A CA  1 
ATOM   3187 C  C   . GLY A 1 435 ? -14.097 9.803   12.581  1.00 10.66  ? 421 GLY A C   1 
ATOM   3188 O  O   . GLY A 1 435 ? -14.341 10.867  13.117  1.00 12.31  ? 421 GLY A O   1 
ATOM   3189 N  N   . ASP A 1 436 ? -13.790 8.697   13.276  1.00 10.65  ? 422 ASP A N   1 
ATOM   3190 C  CA  . ASP A 1 436 ? -13.651 8.759   14.711  1.00 11.35  ? 422 ASP A CA  1 
ATOM   3191 C  C   . ASP A 1 436 ? -12.421 9.584   15.053  1.00 11.74  ? 422 ASP A C   1 
ATOM   3192 O  O   . ASP A 1 436 ? -11.405 9.538   14.357  1.00 12.63  ? 422 ASP A O   1 
ATOM   3193 C  CB  . ASP A 1 436 ? -13.467 7.355   15.300  1.00 13.52  ? 422 ASP A CB  1 
ATOM   3194 C  CG  . ASP A 1 436 ? -14.739 6.547   15.431  1.00 16.40  ? 422 ASP A CG  1 
ATOM   3195 O  OD1 . ASP A 1 436 ? -15.827 7.139   15.426  1.00 18.17  ? 422 ASP A OD1 1 
ATOM   3196 O  OD2 . ASP A 1 436 ? -14.634 5.333   15.565  1.00 16.74  ? 422 ASP A OD2 1 
ATOM   3197 N  N   . VAL A 1 437 ? -12.500 10.303  16.174  1.00 11.47  ? 423 VAL A N   1 
ATOM   3198 C  CA  . VAL A 1 437 ? -11.387 11.082  16.678  1.00 11.09  ? 423 VAL A CA  1 
ATOM   3199 C  C   . VAL A 1 437 ? -10.925 10.465  17.986  1.00 10.98  ? 423 VAL A C   1 
ATOM   3200 O  O   . VAL A 1 437 ? -11.643 10.501  18.985  1.00 13.19  ? 423 VAL A O   1 
ATOM   3201 C  CB  . VAL A 1 437 ? -11.778 12.561  16.884  1.00 12.50  ? 423 VAL A CB  1 
ATOM   3202 C  CG1 . VAL A 1 437 ? -10.585 13.373  17.384  1.00 13.89  ? 423 VAL A CG1 1 
ATOM   3203 C  CG2 . VAL A 1 437 ? -12.352 13.181  15.619  1.00 13.00  ? 423 VAL A CG2 1 
ATOM   3204 N  N   . ILE A 1 438 ? -9.727  9.854   17.970  1.00 10.95  ? 424 ILE A N   1 
ATOM   3205 C  CA  . ILE A 1 438 ? -9.064  9.495   19.207  1.00 11.46  ? 424 ILE A CA  1 
ATOM   3206 C  C   . ILE A 1 438 ? -8.287  10.703  19.687  1.00 12.04  ? 424 ILE A C   1 
ATOM   3207 O  O   . ILE A 1 438 ? -7.558  11.290  18.901  1.00 14.22  ? 424 ILE A O   1 
ATOM   3208 C  CB  . ILE A 1 438 ? -8.106  8.325   18.923  1.00 13.91  ? 424 ILE A CB  1 
ATOM   3209 C  CG1 . ILE A 1 438 ? -8.798  7.110   18.300  1.00 15.20  ? 424 ILE A CG1 1 
ATOM   3210 C  CG2 . ILE A 1 438 ? -7.365  7.968   20.200  1.00 18.88  ? 424 ILE A CG2 1 
ATOM   3211 C  CD1 . ILE A 1 438 ? -7.785  6.112   17.803  1.00 20.42  ? 424 ILE A CD1 1 
ATOM   3212 N  N   . SER A 1 439 ? -8.460  11.111  20.948  1.00 12.83  ? 425 SER A N   1 
ATOM   3213 C  CA  A SER A 1 439 ? -7.827  12.335  21.432  0.50 13.54  ? 425 SER A CA  1 
ATOM   3214 C  CA  B SER A 1 439 ? -7.708  12.279  21.376  0.50 13.28  ? 425 SER A CA  1 
ATOM   3215 C  C   . SER A 1 439 ? -7.115  12.077  22.762  1.00 12.14  ? 425 SER A C   1 
ATOM   3216 O  O   . SER A 1 439 ? -7.640  11.326  23.581  1.00 14.87  ? 425 SER A O   1 
ATOM   3217 C  CB  A SER A 1 439 ? -8.863  13.450  21.538  0.50 15.13  ? 425 SER A CB  1 
ATOM   3218 C  CB  B SER A 1 439 ? -8.522  13.542  21.270  0.50 13.81  ? 425 SER A CB  1 
ATOM   3219 O  OG  A SER A 1 439 ? -8.302  14.657  22.044  0.50 20.13  ? 425 SER A OG  1 
ATOM   3220 O  OG  B SER A 1 439 ? -9.640  13.486  22.135  0.50 14.43  ? 425 SER A OG  1 
ATOM   3221 N  N   . TYR A 1 440 ? -5.987  12.767  22.984  1.00 12.94  ? 426 TYR A N   1 
ATOM   3222 C  CA  . TYR A 1 440 ? -5.261  12.711  24.232  1.00 13.50  ? 426 TYR A CA  1 
ATOM   3223 C  C   . TYR A 1 440 ? -4.933  14.131  24.672  1.00 14.89  ? 426 TYR A C   1 
ATOM   3224 O  O   . TYR A 1 440 ? -4.568  14.974  23.862  1.00 16.90  ? 426 TYR A O   1 
ATOM   3225 C  CB  . TYR A 1 440 ? -3.966  11.927  24.043  1.00 14.76  ? 426 TYR A CB  1 
ATOM   3226 C  CG  . TYR A 1 440 ? -3.201  11.601  25.285  1.00 16.74  ? 426 TYR A CG  1 
ATOM   3227 C  CD1 . TYR A 1 440 ? -3.750  10.737  26.202  1.00 16.88  ? 426 TYR A CD1 1 
ATOM   3228 C  CD2 . TYR A 1 440 ? -1.930  12.084  25.520  1.00 17.41  ? 426 TYR A CD2 1 
ATOM   3229 C  CE1 . TYR A 1 440 ? -3.063  10.358  27.334  1.00 16.75  ? 426 TYR A CE1 1 
ATOM   3230 C  CE2 . TYR A 1 440 ? -1.232  11.729  26.666  1.00 17.86  ? 426 TYR A CE2 1 
ATOM   3231 C  CZ  . TYR A 1 440 ? -1.788  10.851  27.565  1.00 19.16  ? 426 TYR A CZ  1 
ATOM   3232 O  OH  . TYR A 1 440 ? -1.057  10.509  28.673  1.00 22.79  ? 426 TYR A OH  1 
ATOM   3233 N  N   . ASN A 1 441 ? -5.017  14.351  26.000  1.00 15.15  ? 427 ASN A N   1 
ATOM   3234 C  CA  . ASN A 1 441 ? -4.779  15.666  26.581  1.00 16.96  ? 427 ASN A CA  1 
ATOM   3235 C  C   . ASN A 1 441 ? -3.700  15.623  27.662  1.00 20.10  ? 427 ASN A C   1 
ATOM   3236 O  O   . ASN A 1 441 ? -3.565  16.586  28.433  1.00 21.45  ? 427 ASN A O   1 
ATOM   3237 C  CB  . ASN A 1 441 ? -6.058  16.210  27.213  1.00 17.03  ? 427 ASN A CB  1 
ATOM   3238 C  CG  . ASN A 1 441 ? -6.523  15.375  28.399  1.00 16.86  ? 427 ASN A CG  1 
ATOM   3239 O  OD1 . ASN A 1 441 ? -6.029  14.275  28.677  1.00 16.85  ? 427 ASN A OD1 1 
ATOM   3240 N  ND2 . ASN A 1 441 ? -7.502  15.897  29.126  1.00 18.67  ? 427 ASN A ND2 1 
ATOM   3241 N  N   . GLY A 1 442 ? -2.975  14.495  27.745  1.00 18.82  ? 428 GLY A N   1 
ATOM   3242 C  CA  . GLY A 1 442 ? -1.924  14.326  28.728  1.00 20.89  ? 428 GLY A CA  1 
ATOM   3243 C  C   . GLY A 1 442 ? -2.402  13.614  29.985  1.00 22.09  ? 428 GLY A C   1 
ATOM   3244 O  O   . GLY A 1 442 ? -1.594  13.297  30.860  1.00 25.50  ? 428 GLY A O   1 
ATOM   3245 N  N   . LYS A 1 443 ? -3.714  13.385  30.065  1.00 20.92  ? 429 LYS A N   1 
ATOM   3246 C  CA  . LYS A 1 443 ? -4.379  12.775  31.214  1.00 24.78  ? 429 LYS A CA  1 
ATOM   3247 C  C   . LYS A 1 443 ? -5.142  11.522  30.745  1.00 25.13  ? 429 LYS A C   1 
ATOM   3248 O  O   . LYS A 1 443 ? -4.998  10.454  31.306  1.00 27.15  ? 429 LYS A O   1 
ATOM   3249 C  CB  . LYS A 1 443 ? -5.330  13.769  31.918  1.00 26.04  ? 429 LYS A CB  1 
ATOM   3250 C  CG  . LYS A 1 443 ? -4.724  15.122  32.307  1.00 28.33  ? 429 LYS A CG  1 
ATOM   3251 C  CD  . LYS A 1 443 ? -5.604  16.069  33.101  1.00 33.10  ? 429 LYS A CD  1 
ATOM   3252 N  N   . ASP A 1 444 ? -5.942  11.627  29.681  1.00 18.93  ? 430 ASP A N   1 
ATOM   3253 C  CA  . ASP A 1 444 ? -6.847  10.566  29.273  1.00 17.73  ? 430 ASP A CA  1 
ATOM   3254 C  C   . ASP A 1 444 ? -6.893  10.470  27.748  1.00 16.90  ? 430 ASP A C   1 
ATOM   3255 O  O   . ASP A 1 444 ? -6.918  11.496  27.099  1.00 16.19  ? 430 ASP A O   1 
ATOM   3256 C  CB  . ASP A 1 444 ? -8.255  10.872  29.803  1.00 19.52  ? 430 ASP A CB  1 
ATOM   3257 C  CG  . ASP A 1 444 ? -8.401  10.706  31.305  1.00 23.06  ? 430 ASP A CG  1 
ATOM   3258 O  OD1 . ASP A 1 444 ? -8.334  9.559   31.727  1.00 28.88  ? 430 ASP A OD1 1 
ATOM   3259 O  OD2 . ASP A 1 444 ? -8.605  11.714  31.978  1.00 24.25  ? 430 ASP A OD2 1 
ATOM   3260 N  N   . MET A 1 445 ? -6.946  9.252   27.242  1.00 16.59  ? 431 MET A N   1 
ATOM   3261 C  CA  A MET A 1 445 ? -7.184  8.977   25.838  0.56 17.12  ? 431 MET A CA  1 
ATOM   3262 C  CA  B MET A 1 445 ? -7.177  9.001   25.824  0.44 14.82  ? 431 MET A CA  1 
ATOM   3263 C  C   . MET A 1 445 ? -8.664  8.667   25.674  1.00 15.47  ? 431 MET A C   1 
ATOM   3264 O  O   . MET A 1 445 ? -9.190  7.802   26.372  1.00 16.39  ? 431 MET A O   1 
ATOM   3265 C  CB  A MET A 1 445 ? -6.370  7.761   25.398  0.56 17.95  ? 431 MET A CB  1 
ATOM   3266 C  CB  B MET A 1 445 ? -6.288  7.878   25.252  0.44 14.41  ? 431 MET A CB  1 
ATOM   3267 C  CG  A MET A 1 445 ? -5.111  8.129   24.667  0.56 34.65  ? 431 MET A CG  1 
ATOM   3268 C  CG  B MET A 1 445 ? -6.542  7.622   23.744  0.44 9.72   ? 431 MET A CG  1 
ATOM   3269 S  SD  A MET A 1 445 ? -5.384  8.826   23.029  0.56 15.71  ? 431 MET A SD  1 
ATOM   3270 S  SD  B MET A 1 445 ? -5.385  6.614   22.681  0.44 19.63  ? 431 MET A SD  1 
ATOM   3271 C  CE  A MET A 1 445 ? -4.358  7.643   22.146  0.56 21.12  ? 431 MET A CE  1 
ATOM   3272 C  CE  B MET A 1 445 ? -3.929  7.650   22.827  0.44 15.83  ? 431 MET A CE  1 
ATOM   3273 N  N   . ILE A 1 446 ? -9.339  9.410   24.783  1.00 13.45  ? 432 ILE A N   1 
ATOM   3274 C  CA  . ILE A 1 446 ? -10.773 9.316   24.647  1.00 14.51  ? 432 ILE A CA  1 
ATOM   3275 C  C   . ILE A 1 446 ? -11.128 9.131   23.177  1.00 14.04  ? 432 ILE A C   1 
ATOM   3276 O  O   . ILE A 1 446 ? -10.346 9.423   22.251  1.00 13.22  ? 432 ILE A O   1 
ATOM   3277 C  CB  . ILE A 1 446 ? -11.449 10.584  25.227  1.00 15.68  ? 432 ILE A CB  1 
ATOM   3278 C  CG1 . ILE A 1 446 ? -11.166 11.837  24.394  1.00 14.78  ? 432 ILE A CG1 1 
ATOM   3279 C  CG2 . ILE A 1 446 ? -11.056 10.778  26.691  1.00 17.56  ? 432 ILE A CG2 1 
ATOM   3280 C  CD1 . ILE A 1 446 ? -11.885 13.070  24.890  1.00 17.00  ? 432 ILE A CD1 1 
ATOM   3281 N  N   . LEU A 1 447 ? -12.374 8.713   22.993  1.00 14.48  ? 433 LEU A N   1 
ATOM   3282 C  CA  . LEU A 1 447 ? -12.998 8.617   21.674  1.00 14.76  ? 433 LEU A CA  1 
ATOM   3283 C  C   . LEU A 1 447 ? -14.385 9.231   21.780  1.00 13.94  ? 433 LEU A C   1 
ATOM   3284 O  O   . LEU A 1 447 ? -15.361 8.518   21.984  1.00 18.41  ? 433 LEU A O   1 
ATOM   3285 C  CB  . LEU A 1 447 ? -13.000 7.126   21.297  1.00 16.96  ? 433 LEU A CB  1 
ATOM   3286 C  CG  . LEU A 1 447 ? -13.630 6.747   19.969  1.00 24.78  ? 433 LEU A CG  1 
ATOM   3287 C  CD1 . LEU A 1 447 ? -12.985 7.514   18.864  1.00 28.79  ? 433 LEU A CD1 1 
ATOM   3288 C  CD2 . LEU A 1 447 ? -13.461 5.267   19.681  1.00 30.54  ? 433 LEU A CD2 1 
ATOM   3289 N  N   . ASN A 1 448 ? -14.441 10.566  21.642  1.00 14.48  ? 434 ASN A N   1 
ATOM   3290 C  CA  . ASN A 1 448 ? -15.630 11.331  21.989  1.00 15.93  ? 434 ASN A CA  1 
ATOM   3291 C  C   . ASN A 1 448 ? -16.077 12.315  20.916  1.00 17.58  ? 434 ASN A C   1 
ATOM   3292 O  O   . ASN A 1 448 ? -16.835 13.234  21.209  1.00 23.02  ? 434 ASN A O   1 
ATOM   3293 C  CB  . ASN A 1 448 ? -15.305 12.100  23.261  1.00 17.80  ? 434 ASN A CB  1 
ATOM   3294 C  CG  . ASN A 1 448 ? -16.522 12.753  23.906  1.00 18.37  ? 434 ASN A CG  1 
ATOM   3295 O  OD1 . ASN A 1 448 ? -17.559 12.118  24.053  1.00 22.10  ? 434 ASN A OD1 1 
ATOM   3296 N  ND2 . ASN A 1 448 ? -16.396 14.026  24.226  1.00 22.02  ? 434 ASN A ND2 1 
ATOM   3297 N  N   . GLU A 1 449 ? -15.558 12.194  19.696  1.00 15.44  ? 435 GLU A N   1 
ATOM   3298 C  CA  . GLU A 1 449 ? -15.887 13.120  18.639  1.00 15.27  ? 435 GLU A CA  1 
ATOM   3299 C  C   . GLU A 1 449 ? -15.804 12.347  17.329  1.00 14.15  ? 435 GLU A C   1 
ATOM   3300 O  O   . GLU A 1 449 ? -15.074 11.335  17.229  1.00 14.01  ? 435 GLU A O   1 
ATOM   3301 C  CB  . GLU A 1 449 ? -14.860 14.265  18.692  1.00 18.24  ? 435 GLU A CB  1 
ATOM   3302 C  CG  . GLU A 1 449 ? -15.001 15.364  17.612  1.00 19.46  ? 435 GLU A CG  1 
ATOM   3303 C  CD  . GLU A 1 449 ? -13.849 16.363  17.578  1.00 21.25  ? 435 GLU A CD  1 
ATOM   3304 O  OE1 . GLU A 1 449 ? -13.094 16.381  18.553  1.00 22.23  ? 435 GLU A OE1 1 
ATOM   3305 O  OE2 . GLU A 1 449 ? -13.650 17.067  16.523  1.00 24.14  ? 435 GLU A OE2 1 
ATOM   3306 N  N   . LYS A 1 450 ? -16.594 12.772  16.359  1.00 15.19  ? 436 LYS A N   1 
ATOM   3307 C  CA  . LYS A 1 450 ? -16.513 12.322  14.983  1.00 15.37  ? 436 LYS A CA  1 
ATOM   3308 C  C   . LYS A 1 450 ? -16.372 13.537  14.080  1.00 14.88  ? 436 LYS A C   1 
ATOM   3309 O  O   . LYS A 1 450 ? -16.952 14.599  14.360  1.00 18.58  ? 436 LYS A O   1 
ATOM   3310 C  CB  . LYS A 1 450 ? -17.750 11.509  14.611  1.00 18.23  ? 436 LYS A CB  1 
ATOM   3311 C  CG  . LYS A 1 450 ? -17.848 10.115  15.225  1.00 24.74  ? 436 LYS A CG  1 
ATOM   3312 C  CD  . LYS A 1 450 ? -18.874 9.153   14.594  1.00 39.91  ? 436 LYS A CD  1 
ATOM   3313 C  CE  . LYS A 1 450 ? -18.646 8.834   13.115  1.00 41.79  ? 436 LYS A CE  1 
ATOM   3314 N  NZ  . LYS A 1 450 ? -17.383 8.090   12.827  1.00 27.00  ? 436 LYS A NZ  1 
ATOM   3315 N  N   . VAL A 1 451 ? -15.637 13.380  12.981  1.00 12.49  ? 437 VAL A N   1 
ATOM   3316 C  CA  . VAL A 1 451 ? -15.546 14.351  11.899  1.00 13.62  ? 437 VAL A CA  1 
ATOM   3317 C  C   . VAL A 1 451 ? -16.135 13.745  10.632  1.00 12.77  ? 437 VAL A C   1 
ATOM   3318 O  O   . VAL A 1 451 ? -16.365 12.537  10.529  1.00 13.59  ? 437 VAL A O   1 
ATOM   3319 C  CB  . VAL A 1 451 ? -14.116 14.864  11.672  1.00 14.05  ? 437 VAL A CB  1 
ATOM   3320 C  CG1 . VAL A 1 451 ? -13.524 15.443  12.940  1.00 18.03  ? 437 VAL A CG1 1 
ATOM   3321 C  CG2 . VAL A 1 451 ? -13.215 13.746  11.148  1.00 14.03  ? 437 VAL A CG2 1 
ATOM   3322 N  N   . GLN A 1 452 ? -16.356 14.588  9.614   1.00 12.63  ? 438 GLN A N   1 
ATOM   3323 C  CA  . GLN A 1 452 ? -16.899 14.099  8.367   1.00 12.61  ? 438 GLN A CA  1 
ATOM   3324 C  C   . GLN A 1 452 ? -15.924 13.066  7.783   1.00 10.97  ? 438 GLN A C   1 
ATOM   3325 O  O   . GLN A 1 452 ? -14.724 13.298  7.781   1.00 12.93  ? 438 GLN A O   1 
ATOM   3326 C  CB  . GLN A 1 452 ? -17.111 15.266  7.395   1.00 12.69  ? 438 GLN A CB  1 
ATOM   3327 C  CG  . GLN A 1 452 ? -17.752 14.829  6.109   1.00 12.93  ? 438 GLN A CG  1 
ATOM   3328 C  CD  . GLN A 1 452 ? -18.157 16.043  5.290   1.00 12.45  ? 438 GLN A CD  1 
ATOM   3329 O  OE1 . GLN A 1 452 ? -18.630 17.069  5.830   1.00 14.42  ? 438 GLN A OE1 1 
ATOM   3330 N  NE2 . GLN A 1 452 ? -17.980 15.957  3.985   1.00 12.19  ? 438 GLN A NE2 1 
ATOM   3331 N  N   . SER A 1 453 ? -16.466 11.997  7.184   1.00 11.73  ? 439 SER A N   1 
ATOM   3332 C  CA  . SER A 1 453 ? -15.647 11.005  6.504   1.00 13.24  ? 439 SER A CA  1 
ATOM   3333 C  C   . SER A 1 453 ? -16.540 10.277  5.512   1.00 11.63  ? 439 SER A C   1 
ATOM   3334 O  O   . SER A 1 453 ? -17.773 10.365  5.641   1.00 15.16  ? 439 SER A O   1 
ATOM   3335 C  CB  . SER A 1 453 ? -15.010 10.029  7.472   1.00 12.35  ? 439 SER A CB  1 
ATOM   3336 O  OG  . SER A 1 453 ? -16.008 9.169   7.999   1.00 14.50  ? 439 SER A OG  1 
ATOM   3337 N  N   . GLY A 1 454 ? -15.959 9.568   4.574   1.00 12.06  ? 440 GLY A N   1 
ATOM   3338 C  CA  . GLY A 1 454 ? -16.735 8.793   3.659   1.00 15.20  ? 440 GLY A CA  1 
ATOM   3339 C  C   . GLY A 1 454 ? -15.974 8.489   2.389   1.00 12.69  ? 440 GLY A C   1 
ATOM   3340 O  O   . GLY A 1 454 ? -14.773 8.688   2.305   1.00 12.68  ? 440 GLY A O   1 
ATOM   3341 N  N   . ASN A 1 455 ? -16.719 7.971   1.422   1.00 14.70  ? 441 ASN A N   1 
ATOM   3342 C  CA  . ASN A 1 455 ? -16.206 7.450   0.182   1.00 14.60  ? 441 ASN A CA  1 
ATOM   3343 C  C   . ASN A 1 455 ? -16.582 8.431   -0.920  1.00 15.84  ? 441 ASN A C   1 
ATOM   3344 O  O   . ASN A 1 455 ? -17.761 8.628   -1.153  1.00 20.54  ? 441 ASN A O   1 
ATOM   3345 C  CB  . ASN A 1 455 ? -16.793 6.042   -0.042  1.00 17.48  ? 441 ASN A CB  1 
ATOM   3346 C  CG  . ASN A 1 455 ? -16.213 4.968   0.859   1.00 17.94  ? 441 ASN A CG  1 
ATOM   3347 O  OD1 . ASN A 1 455 ? -15.289 5.210   1.638   1.00 20.58  ? 441 ASN A OD1 1 
ATOM   3348 N  ND2 . ASN A 1 455 ? -16.640 3.727   0.713   1.00 22.21  ? 441 ASN A ND2 1 
ATOM   3349 N  N   . ILE A 1 456 ? -15.593 8.954   -1.627  1.00 16.55  ? 442 ILE A N   1 
ATOM   3350 C  CA  . ILE A 1 456 ? -15.774 9.760   -2.817  1.00 16.80  ? 442 ILE A CA  1 
ATOM   3351 C  C   . ILE A 1 456 ? -15.592 8.858   -4.035  1.00 16.62  ? 442 ILE A C   1 
ATOM   3352 O  O   . ILE A 1 456 ? -14.538 8.262   -4.226  1.00 16.20  ? 442 ILE A O   1 
ATOM   3353 C  CB  . ILE A 1 456 ? -14.771 10.931  -2.854  1.00 18.67  ? 442 ILE A CB  1 
ATOM   3354 C  CG1 . ILE A 1 456 ? -14.843 11.762  -1.570  1.00 22.12  ? 442 ILE A CG1 1 
ATOM   3355 C  CG2 . ILE A 1 456 ? -14.942 11.777  -4.110  1.00 22.98  ? 442 ILE A CG2 1 
ATOM   3356 C  CD1 . ILE A 1 456 ? -16.185 12.396  -1.366  1.00 20.72  ? 442 ILE A CD1 1 
ATOM   3357 N  N   . LEU A 1 457 ? -16.622 8.780   -4.879  1.00 17.84  ? 443 LEU A N   1 
ATOM   3358 C  CA  . LEU A 1 457 ? -16.632 7.904   -6.043  1.00 20.38  ? 443 LEU A CA  1 
ATOM   3359 C  C   . LEU A 1 457 ? -16.099 8.635   -7.285  1.00 20.77  ? 443 LEU A C   1 
ATOM   3360 O  O   . LEU A 1 457 ? -16.590 9.707   -7.632  1.00 26.63  ? 443 LEU A O   1 
ATOM   3361 C  CB  . LEU A 1 457 ? -18.073 7.416   -6.248  1.00 21.80  ? 443 LEU A CB  1 
ATOM   3362 C  CG  . LEU A 1 457 ? -18.769 6.810   -5.032  1.00 26.92  ? 443 LEU A CG  1 
ATOM   3363 C  CD1 . LEU A 1 457 ? -20.157 6.300   -5.420  1.00 33.82  ? 443 LEU A CD1 1 
ATOM   3364 C  CD2 . LEU A 1 457 ? -17.972 5.673   -4.412  1.00 30.90  ? 443 LEU A CD2 1 
ATOM   3365 N  N   . ILE A 1 458 ? -15.085 8.030   -7.954  1.00 20.93  ? 444 ILE A N   1 
ATOM   3366 C  CA  . ILE A 1 458 ? -14.402 8.613   -9.107  1.00 25.11  ? 444 ILE A CA  1 
ATOM   3367 C  C   . ILE A 1 458 ? -14.602 7.727   -10.353 1.00 22.78  ? 444 ILE A C   1 
ATOM   3368 O  O   . ILE A 1 458 ? -14.330 6.531   -10.336 1.00 25.82  ? 444 ILE A O   1 
ATOM   3369 C  CB  . ILE A 1 458 ? -12.901 8.797   -8.808  1.00 22.37  ? 444 ILE A CB  1 
ATOM   3370 C  CG1 . ILE A 1 458 ? -12.625 9.543   -7.496  1.00 24.39  ? 444 ILE A CG1 1 
ATOM   3371 C  CG2 . ILE A 1 458 ? -12.190 9.461   -9.982  1.00 24.10  ? 444 ILE A CG2 1 
ATOM   3372 C  CD1 . ILE A 1 458 ? -12.886 11.015  -7.522  1.00 22.39  ? 444 ILE A CD1 1 
ATOM   3373 N  N   . ASP A 1 459 ? -15.048 8.340   -11.456 1.00 31.36  ? 445 ASP A N   1 
ATOM   3374 C  CA  . ASP A 1 459 ? -15.107 7.680   -12.759 1.00 42.84  ? 445 ASP A CA  1 
ATOM   3375 C  C   . ASP A 1 459 ? -14.372 8.510   -13.799 1.00 60.45  ? 445 ASP A C   1 
ATOM   3376 O  O   . ASP A 1 459 ? -14.076 9.680   -13.559 1.00 56.35  ? 445 ASP A O   1 
ATOM   3377 C  CB  . ASP A 1 459 ? -16.531 7.499   -13.282 1.00 32.72  ? 445 ASP A CB  1 
ATOM   3378 N  N   . GLY A 1 460 ? -14.212 7.887   -14.980 1.00 45.23  ? 446 GLY A N   1 
ATOM   3379 C  CA  . GLY A 1 460 ? -13.419 8.385   -16.095 1.00 36.12  ? 446 GLY A CA  1 
ATOM   3380 C  C   . GLY A 1 460 ? -13.304 9.897   -16.108 1.00 45.98  ? 446 GLY A C   1 
ATOM   3381 O  O   . GLY A 1 460 ? -12.696 10.389  -17.090 1.00 61.58  ? 446 GLY A O   1 
HETATM 3382 MN MN  . MN  B 2 .   ? 0.673   -2.147  -0.033  0.41 11.19  ? 601 MN  A MN  1 
HETATM 3383 O  O   . HOH C 3 .   ? 12.683  7.227   18.806  1.00 33.35  ? 701 HOH A O   1 
HETATM 3384 O  O   . HOH C 3 .   ? -2.154  -3.238  -10.643 1.00 32.62  ? 702 HOH A O   1 
HETATM 3385 O  O   . HOH C 3 .   ? 14.471  4.941   -0.880  1.00 29.71  ? 703 HOH A O   1 
HETATM 3386 O  O   . HOH C 3 .   ? -8.807  14.862  24.418  1.00 24.29  ? 704 HOH A O   1 
HETATM 3387 O  O   . HOH C 3 .   ? 13.612  -7.146  -8.198  1.00 32.71  ? 705 HOH A O   1 
HETATM 3388 O  O   . HOH C 3 .   ? -3.291  5.796   -9.185  1.00 38.17  ? 706 HOH A O   1 
HETATM 3389 O  O   . HOH C 3 .   ? -9.765  26.172  10.133  1.00 33.89  ? 707 HOH A O   1 
HETATM 3390 O  O   . HOH C 3 .   ? -12.006 -13.209 12.417  1.00 30.33  ? 708 HOH A O   1 
HETATM 3391 O  O   . HOH C 3 .   ? 3.731   -13.300 -0.764  1.00 26.32  ? 709 HOH A O   1 
HETATM 3392 O  O   . HOH C 3 .   ? -1.287  -1.696  -14.221 1.00 27.54  ? 710 HOH A O   1 
HETATM 3393 O  O   . HOH C 3 .   ? 14.199  -9.262  5.372   1.00 26.02  ? 711 HOH A O   1 
HETATM 3394 O  O   . HOH C 3 .   ? -3.751  9.678   -9.331  1.00 27.37  ? 712 HOH A O   1 
HETATM 3395 O  O   . HOH C 3 .   ? 10.310  6.371   20.140  1.00 19.90  ? 713 HOH A O   1 
HETATM 3396 O  O   . HOH C 3 .   ? -8.961  14.143  31.064  1.00 21.51  ? 714 HOH A O   1 
HETATM 3397 O  O   . HOH C 3 .   ? 17.552  -11.782 5.972   1.00 35.71  ? 715 HOH A O   1 
HETATM 3398 O  O   . HOH C 3 .   ? -12.885 22.528  -3.359  1.00 26.55  ? 716 HOH A O   1 
HETATM 3399 O  O   . HOH C 3 .   ? -1.665  7.631   29.333  1.00 24.99  ? 717 HOH A O   1 
HETATM 3400 O  O   . HOH C 3 .   ? -6.487  26.644  12.406  1.00 29.05  ? 718 HOH A O   1 
HETATM 3401 O  O   . HOH C 3 .   ? -2.369  -25.855 -16.450 1.00 37.97  ? 719 HOH A O   1 
HETATM 3402 O  O   . HOH C 3 .   ? -0.448  -8.929  -6.121  1.00 23.66  ? 720 HOH A O   1 
HETATM 3403 O  O   . HOH C 3 .   ? 5.262   -9.856  24.797  1.00 35.00  ? 721 HOH A O   1 
HETATM 3404 O  O   . HOH C 3 .   ? 11.449  20.276  15.911  1.00 28.68  ? 722 HOH A O   1 
HETATM 3405 O  O   . HOH C 3 .   ? -17.635 10.284  9.904   1.00 21.16  ? 723 HOH A O   1 
HETATM 3406 O  O   . HOH C 3 .   ? -5.196  -9.606  -14.182 1.00 20.91  ? 724 HOH A O   1 
HETATM 3407 O  O   . HOH C 3 .   ? 5.233   22.026  6.050   1.00 30.24  ? 725 HOH A O   1 
HETATM 3408 O  O   . HOH C 3 .   ? -7.978  -15.947 13.700  1.00 45.91  ? 726 HOH A O   1 
HETATM 3409 O  O   . HOH C 3 .   ? 15.686  4.316   3.629   1.00 17.14  ? 727 HOH A O   1 
HETATM 3410 O  O   . HOH C 3 .   ? 14.793  8.746   10.190  1.00 16.53  ? 728 HOH A O   1 
HETATM 3411 O  O   . HOH C 3 .   ? -12.647 7.053   3.026   1.00 13.42  ? 729 HOH A O   1 
HETATM 3412 O  O   . HOH C 3 .   ? -6.169  -13.455 6.995   1.00 27.18  ? 730 HOH A O   1 
HETATM 3413 O  O   . HOH C 3 .   ? 5.748   0.759   5.646   1.00 15.30  ? 731 HOH A O   1 
HETATM 3414 O  O   . HOH C 3 .   ? -8.776  0.680   15.445  1.00 16.19  ? 732 HOH A O   1 
HETATM 3415 O  O   . HOH C 3 .   ? 14.112  -25.007 -15.652 1.00 21.22  ? 733 HOH A O   1 
HETATM 3416 O  O   . HOH C 3 .   ? 10.173  19.608  6.227   1.00 35.82  ? 734 HOH A O   1 
HETATM 3417 O  O   . HOH C 3 .   ? -15.659 1.312   2.268   1.00 24.61  ? 735 HOH A O   1 
HETATM 3418 O  O   . HOH C 3 .   ? 7.779   6.021   0.828   1.00 13.28  ? 736 HOH A O   1 
HETATM 3419 O  O   . HOH C 3 .   ? 6.111   -6.154  -22.231 1.00 30.82  ? 737 HOH A O   1 
HETATM 3420 O  O   . HOH C 3 .   ? 0.233   -17.641 15.414  1.00 23.86  ? 738 HOH A O   1 
HETATM 3421 O  O   . HOH C 3 .   ? 4.169   16.605  -10.306 1.00 24.95  ? 739 HOH A O   1 
HETATM 3422 O  O   . HOH C 3 .   ? -20.513 -15.983 -10.537 1.00 25.03  ? 740 HOH A O   1 
HETATM 3423 O  O   . HOH C 3 .   ? 5.061   -26.569 -21.145 1.00 36.21  ? 741 HOH A O   1 
HETATM 3424 O  O   . HOH C 3 .   ? -2.837  -21.554 -23.870 1.00 26.35  ? 742 HOH A O   1 
HETATM 3425 O  O   . HOH C 3 .   ? -4.089  -5.882  -17.479 1.00 36.77  ? 743 HOH A O   1 
HETATM 3426 O  O   . HOH C 3 .   ? 12.420  -4.886  -6.701  1.00 43.20  ? 744 HOH A O   1 
HETATM 3427 O  O   . HOH C 3 .   ? -17.546 18.722  7.854   1.00 17.57  ? 745 HOH A O   1 
HETATM 3428 O  O   . HOH C 3 .   ? 7.898   19.625  -8.407  1.00 28.21  ? 746 HOH A O   1 
HETATM 3429 O  O   . HOH C 3 .   ? -5.085  7.431   -8.796  1.00 22.40  ? 747 HOH A O   1 
HETATM 3430 O  O   . HOH C 3 .   ? 6.643   -13.763 3.139   1.00 19.98  ? 748 HOH A O   1 
HETATM 3431 O  O   . HOH C 3 .   ? -9.717  16.702  20.539  1.00 26.47  ? 749 HOH A O   1 
HETATM 3432 O  O   . HOH C 3 .   ? -12.034 -11.283 14.328  1.00 21.60  ? 750 HOH A O   1 
HETATM 3433 O  O   . HOH C 3 .   ? 14.533  7.191   -0.298  1.00 23.53  ? 751 HOH A O   1 
HETATM 3434 O  O   . HOH C 3 .   ? 1.218   -6.532  -2.703  1.00 42.51  ? 752 HOH A O   1 
HETATM 3435 O  O   . HOH C 3 .   ? 7.741   1.844   23.979  1.00 16.34  ? 753 HOH A O   1 
HETATM 3436 O  O   . HOH C 3 .   ? -18.633 11.600  2.719   1.00 26.82  ? 754 HOH A O   1 
HETATM 3437 O  O   . HOH C 3 .   ? -9.946  -15.597 -27.112 1.00 25.67  ? 755 HOH A O   1 
HETATM 3438 O  O   . HOH C 3 .   ? 0.680   -18.724 8.115   1.00 31.66  ? 756 HOH A O   1 
HETATM 3439 O  O   . HOH C 3 .   ? 13.079  6.531   12.756  1.00 29.31  ? 757 HOH A O   1 
HETATM 3440 O  O   . HOH C 3 .   ? -0.710  6.233   -8.389  1.00 31.31  ? 758 HOH A O   1 
HETATM 3441 O  O   . HOH C 3 .   ? -12.981 14.467  6.043   1.00 13.96  ? 759 HOH A O   1 
HETATM 3442 O  O   . HOH C 3 .   ? 13.156  -16.745 -21.895 1.00 30.75  ? 760 HOH A O   1 
HETATM 3443 O  O   . HOH C 3 .   ? -17.746 5.941   9.662   1.00 26.81  ? 761 HOH A O   1 
HETATM 3444 O  O   . HOH C 3 .   ? -12.199 12.324  20.941  1.00 17.43  ? 762 HOH A O   1 
HETATM 3445 O  O   . HOH C 3 .   ? -13.345 21.120  11.212  1.00 27.95  ? 763 HOH A O   1 
HETATM 3446 O  O   . HOH C 3 .   ? -7.589  4.414   27.760  1.00 38.28  ? 764 HOH A O   1 
HETATM 3447 O  O   . HOH C 3 .   ? -12.851 -19.978 -24.665 1.00 30.81  ? 765 HOH A O   1 
HETATM 3448 O  O   . HOH C 3 .   ? -2.710  -7.091  27.855  1.00 24.01  ? 766 HOH A O   1 
HETATM 3449 O  O   . HOH C 3 .   ? 9.936   -3.247  1.216   1.00 16.68  ? 767 HOH A O   1 
HETATM 3450 O  O   . HOH C 3 .   ? 5.573   -27.386 -5.235  1.00 38.57  ? 768 HOH A O   1 
HETATM 3451 O  O   . HOH C 3 .   ? 4.096   -21.442 5.212   1.00 27.41  ? 769 HOH A O   1 
HETATM 3452 O  O   . HOH C 3 .   ? -15.845 17.257  14.876  1.00 30.34  ? 770 HOH A O   1 
HETATM 3453 O  O   . HOH C 3 .   ? 12.419  -2.545  21.498  1.00 24.97  ? 771 HOH A O   1 
HETATM 3454 O  O   . HOH C 3 .   ? -3.818  20.610  14.277  1.00 18.52  ? 772 HOH A O   1 
HETATM 3455 O  O   . HOH C 3 .   ? -7.026  -11.252 8.529   1.00 17.32  ? 773 HOH A O   1 
HETATM 3456 O  O   . HOH C 3 .   ? -1.544  -7.673  8.565   1.00 12.46  ? 774 HOH A O   1 
HETATM 3457 O  O   . HOH C 3 .   ? -13.790 0.048   11.554  1.00 22.74  ? 775 HOH A O   1 
HETATM 3458 O  O   . HOH C 3 .   ? 14.504  11.196  -5.060  1.00 19.03  ? 776 HOH A O   1 
HETATM 3459 O  O   . HOH C 3 .   ? -0.394  -0.464  27.416  1.00 19.68  ? 777 HOH A O   1 
HETATM 3460 O  O   . HOH C 3 .   ? -5.971  19.879  26.933  1.00 33.37  ? 778 HOH A O   1 
HETATM 3461 O  O   . HOH C 3 .   ? -0.976  -0.823  -6.298  1.00 23.47  ? 779 HOH A O   1 
HETATM 3462 O  O   . HOH C 3 .   ? 1.375   -4.926  14.884  1.00 12.09  ? 780 HOH A O   1 
HETATM 3463 O  O   . HOH C 3 .   ? 4.467   16.369  27.563  1.00 34.84  ? 781 HOH A O   1 
HETATM 3464 O  O   . HOH C 3 .   ? 13.284  -18.791 4.030   1.00 24.22  ? 782 HOH A O   1 
HETATM 3465 O  O   . HOH C 3 .   ? -12.435 15.064  20.914  1.00 24.16  ? 783 HOH A O   1 
HETATM 3466 O  O   . HOH C 3 .   ? -8.584  13.685  26.676  1.00 18.91  ? 784 HOH A O   1 
HETATM 3467 O  O   . HOH C 3 .   ? -7.669  20.229  16.207  1.00 31.44  ? 785 HOH A O   1 
HETATM 3468 O  O   . HOH C 3 .   ? -1.740  -23.238 -20.287 1.00 20.09  ? 786 HOH A O   1 
HETATM 3469 O  O   . HOH C 3 .   ? -13.117 10.118  4.704   1.00 11.21  ? 787 HOH A O   1 
HETATM 3470 O  O   . HOH C 3 .   ? -2.876  9.072   -12.032 1.00 27.55  ? 788 HOH A O   1 
HETATM 3471 O  O   . HOH C 3 .   ? -10.682 -12.180 16.482  1.00 22.37  ? 789 HOH A O   1 
HETATM 3472 O  O   . HOH C 3 .   ? -17.498 7.133   6.817   1.00 22.49  ? 790 HOH A O   1 
HETATM 3473 O  O   . HOH C 3 .   ? -3.661  -19.236 -8.887  1.00 29.24  ? 791 HOH A O   1 
HETATM 3474 O  O   . HOH C 3 .   ? 8.655   -4.852  8.125   1.00 14.68  ? 792 HOH A O   1 
HETATM 3475 O  O   . HOH C 3 .   ? -6.901  8.120   -11.055 1.00 29.45  ? 793 HOH A O   1 
HETATM 3476 O  O   . HOH C 3 .   ? 11.693  -8.807  6.708   1.00 18.44  ? 794 HOH A O   1 
HETATM 3477 O  O   . HOH C 3 .   ? -9.964  20.685  14.151  1.00 25.59  ? 795 HOH A O   1 
HETATM 3478 O  O   . HOH C 3 .   ? -4.509  -4.636  2.771   1.00 20.09  ? 796 HOH A O   1 
HETATM 3479 O  O   . HOH C 3 .   ? 11.979  -0.930  2.327   1.00 18.90  ? 797 HOH A O   1 
HETATM 3480 O  O   . HOH C 3 .   ? -5.824  -11.752 23.379  1.00 32.06  ? 798 HOH A O   1 
HETATM 3481 O  O   . HOH C 3 .   ? 11.499  -14.627 -4.132  1.00 25.83  ? 799 HOH A O   1 
HETATM 3482 O  O   . HOH C 3 .   ? 4.244   0.206   3.490   1.00 16.66  ? 800 HOH A O   1 
HETATM 3483 O  O   . HOH C 3 .   ? -14.283 18.434  0.533   1.00 29.48  ? 801 HOH A O   1 
HETATM 3484 O  O   . HOH C 3 .   ? -9.462  27.182  6.242   1.00 30.14  ? 802 HOH A O   1 
HETATM 3485 O  O   . HOH C 3 .   ? 8.405   -6.566  24.290  1.00 32.85  ? 803 HOH A O   1 
HETATM 3486 O  O   . HOH C 3 .   ? -1.486  21.714  -4.594  1.00 33.35  ? 804 HOH A O   1 
HETATM 3487 O  O   . HOH C 3 .   ? 8.602   9.716   -12.306 1.00 29.92  ? 805 HOH A O   1 
HETATM 3488 O  O   . HOH C 3 .   ? 6.498   -29.302 -11.769 1.00 31.45  ? 806 HOH A O   1 
HETATM 3489 O  O   . HOH C 3 .   ? 4.589   14.868  -12.723 1.00 26.68  ? 807 HOH A O   1 
HETATM 3490 O  O   . HOH C 3 .   ? 4.817   -19.777 7.283   1.00 23.63  ? 808 HOH A O   1 
HETATM 3491 O  O   . HOH C 3 .   ? -5.960  -12.561 16.450  1.00 33.32  ? 809 HOH A O   1 
HETATM 3492 O  O   . HOH C 3 .   ? -6.236  -1.798  -3.633  1.00 39.92  ? 810 HOH A O   1 
HETATM 3493 O  O   . HOH C 3 .   ? 6.094   -23.923 -18.511 1.00 23.79  ? 811 HOH A O   1 
HETATM 3494 O  O   . HOH C 3 .   ? -19.588 -15.668 -13.860 1.00 33.22  ? 812 HOH A O   1 
HETATM 3495 O  O   . HOH C 3 .   ? -14.359 -8.079  -27.582 1.00 21.69  ? 813 HOH A O   1 
HETATM 3496 O  O   . HOH C 3 .   ? 2.877   20.501  -2.901  1.00 21.99  ? 814 HOH A O   1 
HETATM 3497 O  O   . HOH C 3 .   ? -0.285  8.711   -6.940  1.00 25.62  ? 815 HOH A O   1 
HETATM 3498 O  O   . HOH C 3 .   ? 3.528   -5.028  23.211  1.00 23.79  ? 816 HOH A O   1 
HETATM 3499 O  O   . HOH C 3 .   ? 7.911   17.466  20.941  1.00 30.19  ? 817 HOH A O   1 
HETATM 3500 O  O   . HOH C 3 .   ? -7.012  -10.315 4.464   1.00 35.28  ? 818 HOH A O   1 
HETATM 3501 O  O   . HOH C 3 .   ? 15.415  -9.882  -1.864  1.00 33.36  ? 819 HOH A O   1 
HETATM 3502 O  O   . HOH C 3 .   ? 10.053  8.562   22.145  1.00 26.30  ? 820 HOH A O   1 
HETATM 3503 O  O   . HOH C 3 .   ? -19.473 10.365  0.322   1.00 30.52  ? 821 HOH A O   1 
HETATM 3504 O  O   . HOH C 3 .   ? -7.140  16.938  23.833  1.00 29.34  ? 822 HOH A O   1 
HETATM 3505 O  O   . HOH C 3 .   ? -6.386  6.884   28.783  1.00 27.26  ? 823 HOH A O   1 
HETATM 3506 O  O   . HOH C 3 .   ? -2.127  -5.386  -0.584  1.00 33.20  ? 824 HOH A O   1 
HETATM 3507 O  O   . HOH C 3 .   ? -9.638  -3.667  -22.329 1.00 30.28  ? 825 HOH A O   1 
HETATM 3508 O  O   . HOH C 3 .   ? -0.697  -15.750 -27.760 1.00 42.42  ? 826 HOH A O   1 
HETATM 3509 O  O   . HOH C 3 .   ? -14.425 -11.196 19.820  1.00 31.09  ? 827 HOH A O   1 
HETATM 3510 O  O   . HOH C 3 .   ? 2.987   -2.619  25.103  1.00 28.18  ? 828 HOH A O   1 
HETATM 3511 O  O   . HOH C 3 .   ? -0.212  1.833   3.221   1.00 31.23  ? 829 HOH A O   1 
HETATM 3512 O  O   . HOH C 3 .   ? -16.129 -16.698 -20.041 1.00 30.40  ? 830 HOH A O   1 
HETATM 3513 O  O   . HOH C 3 .   ? -11.183 -3.041  0.994   1.00 30.44  ? 831 HOH A O   1 
HETATM 3514 O  O   . HOH C 3 .   ? 11.529  11.569  -8.883  1.00 27.42  ? 832 HOH A O   1 
HETATM 3515 O  O   . HOH C 3 .   ? -18.060 -21.846 -14.415 1.00 30.99  ? 833 HOH A O   1 
HETATM 3516 O  O   . HOH C 3 .   ? 0.222   -25.840 -12.282 1.00 30.00  ? 834 HOH A O   1 
HETATM 3517 O  O   . HOH C 3 .   ? -15.745 -3.763  8.582   1.00 20.48  ? 835 HOH A O   1 
HETATM 3518 O  O   . HOH C 3 .   ? -12.234 1.159   21.177  1.00 26.67  ? 836 HOH A O   1 
HETATM 3519 O  O   . HOH C 3 .   ? 12.876  10.082  -6.983  1.00 21.36  ? 837 HOH A O   1 
HETATM 3520 O  O   . HOH C 3 .   ? -1.988  -1.154  -3.248  1.00 20.94  ? 838 HOH A O   1 
HETATM 3521 O  O   . HOH C 3 .   ? 7.737   2.615   -2.630  1.00 16.55  ? 839 HOH A O   1 
HETATM 3522 O  O   . HOH C 3 .   ? -17.281 -8.128  -3.349  1.00 38.34  ? 840 HOH A O   1 
HETATM 3523 O  O   . HOH C 3 .   ? -5.531  -4.222  -18.989 1.00 27.33  ? 841 HOH A O   1 
HETATM 3524 O  O   . HOH C 3 .   ? -2.456  9.986   -7.139  1.00 23.87  ? 842 HOH A O   1 
HETATM 3525 O  O   . HOH C 3 .   ? -2.159  -17.741 -0.103  1.00 35.76  ? 843 HOH A O   1 
HETATM 3526 O  O   . HOH C 3 .   ? -18.965 10.453  -4.484  1.00 28.09  ? 844 HOH A O   1 
HETATM 3527 O  O   . HOH C 3 .   ? 17.289  14.835  7.634   1.00 30.18  ? 845 HOH A O   1 
HETATM 3528 O  O   . HOH C 3 .   ? 10.193  23.307  29.916  1.00 29.74  ? 846 HOH A O   1 
HETATM 3529 O  O   . HOH C 3 .   ? 13.889  19.286  8.712   1.00 29.78  ? 847 HOH A O   1 
HETATM 3530 O  O   . HOH C 3 .   ? 4.185   6.684   26.129  1.00 30.80  ? 848 HOH A O   1 
HETATM 3531 O  O   . HOH C 3 .   ? -10.329 24.655  -0.131  1.00 26.42  ? 849 HOH A O   1 
HETATM 3532 O  O   . HOH C 3 .   ? 14.278  -5.518  16.620  1.00 28.93  ? 850 HOH A O   1 
HETATM 3533 O  O   . HOH C 3 .   ? -15.768 -7.017  9.833   1.00 20.14  ? 851 HOH A O   1 
HETATM 3534 O  O   . HOH C 3 .   ? -19.506 7.334   2.098   1.00 27.30  ? 852 HOH A O   1 
HETATM 3535 O  O   . HOH C 3 .   ? 18.832  11.466  4.773   1.00 26.61  ? 853 HOH A O   1 
HETATM 3536 O  O   . HOH C 3 .   ? -1.373  -9.330  0.172   1.00 25.32  ? 854 HOH A O   1 
HETATM 3537 O  O   . HOH C 3 .   ? 4.690   -10.338 -2.544  1.00 32.74  ? 855 HOH A O   1 
HETATM 3538 O  O   . HOH C 3 .   ? -0.443  -25.176 -7.335  1.00 31.68  ? 856 HOH A O   1 
HETATM 3539 O  O   . HOH C 3 .   ? 11.365  -24.999 -7.471  1.00 30.29  ? 857 HOH A O   1 
HETATM 3540 O  O   . HOH C 3 .   ? -1.688  -26.786 -18.865 1.00 28.92  ? 858 HOH A O   1 
HETATM 3541 O  O   . HOH C 3 .   ? -8.898  -2.010  -3.510  1.00 26.16  ? 859 HOH A O   1 
HETATM 3542 O  O   . HOH C 3 .   ? 18.448  -1.402  18.731  1.00 35.26  ? 860 HOH A O   1 
HETATM 3543 O  O   . HOH C 3 .   ? 9.686   -8.654  18.585  1.00 28.91  ? 861 HOH A O   1 
HETATM 3544 O  O   . HOH C 3 .   ? -11.444 13.902  -1.775  1.00 25.83  ? 862 HOH A O   1 
HETATM 3545 O  O   . HOH C 3 .   ? 8.938   10.610  20.696  1.00 24.36  ? 863 HOH A O   1 
HETATM 3546 O  O   . HOH C 3 .   ? -18.694 14.636  17.307  1.00 25.49  ? 864 HOH A O   1 
HETATM 3547 O  O   . HOH C 3 .   ? 17.032  -21.176 -19.654 1.00 30.24  ? 865 HOH A O   1 
HETATM 3548 O  O   . HOH C 3 .   ? -13.295 15.568  -0.079  1.00 21.93  ? 866 HOH A O   1 
HETATM 3549 O  O   . HOH C 3 .   ? 3.816   -14.604 1.652   1.00 25.21  ? 867 HOH A O   1 
HETATM 3550 O  O   . HOH C 3 .   ? 3.542   -26.001 -6.818  1.00 30.35  ? 868 HOH A O   1 
HETATM 3551 O  O   . HOH C 3 .   ? 16.697  -4.965  -3.384  1.00 33.32  ? 869 HOH A O   1 
HETATM 3552 O  O   . HOH C 3 .   ? -15.728 17.509  9.739   1.00 19.53  ? 870 HOH A O   1 
HETATM 3553 O  O   . HOH C 3 .   ? -0.443  -4.167  -0.391  1.00 28.78  ? 871 HOH A O   1 
HETATM 3554 O  O   . HOH C 3 .   ? -15.377 2.754   8.878   1.00 19.27  ? 872 HOH A O   1 
HETATM 3555 O  O   . HOH C 3 .   ? -6.971  -11.880 -28.028 1.00 35.49  ? 873 HOH A O   1 
HETATM 3556 O  O   . HOH C 3 .   ? 3.627   -20.165 10.025  1.00 26.05  ? 874 HOH A O   1 
HETATM 3557 O  O   . HOH C 3 .   ? -11.155 -20.332 -26.802 1.00 29.05  ? 875 HOH A O   1 
HETATM 3558 O  O   . HOH C 3 .   ? 6.298   -13.353 17.180  1.00 29.08  ? 876 HOH A O   1 
HETATM 3559 O  O   . HOH C 3 .   ? -8.517  18.464  27.901  1.00 32.48  ? 877 HOH A O   1 
HETATM 3560 O  O   . HOH C 3 .   ? 1.031   -3.162  -1.965  1.00 35.36  ? 878 HOH A O   1 
HETATM 3561 O  O   . HOH C 3 .   ? 2.954   -24.362 -27.347 1.00 31.36  ? 879 HOH A O   1 
HETATM 3562 O  O   . HOH C 3 .   ? 18.114  -0.771  11.598  1.00 22.92  ? 880 HOH A O   1 
HETATM 3563 O  O   . HOH C 3 .   ? -14.029 15.682  23.177  1.00 27.67  ? 881 HOH A O   1 
HETATM 3564 O  O   . HOH C 3 .   ? -0.825  -1.726  -1.577  1.00 31.53  ? 882 HOH A O   1 
HETATM 3565 O  O   . HOH C 3 .   ? 12.488  14.376  18.793  1.00 40.79  ? 883 HOH A O   1 
HETATM 3566 O  O   . HOH C 3 .   ? -0.179  0.659   29.917  1.00 30.22  ? 884 HOH A O   1 
HETATM 3567 O  O   . HOH C 3 .   ? 14.332  -7.896  -21.549 1.00 42.41  ? 885 HOH A O   1 
HETATM 3568 O  O   . HOH C 3 .   ? -19.472 11.908  7.970   1.00 26.63  ? 886 HOH A O   1 
HETATM 3569 O  O   . HOH C 3 .   ? 13.055  -14.502 -1.746  1.00 32.30  ? 887 HOH A O   1 
HETATM 3570 O  O   . HOH C 3 .   ? 13.910  -21.427 3.686   1.00 26.21  ? 888 HOH A O   1 
HETATM 3571 O  O   . HOH C 3 .   ? -20.381 -14.353 -6.780  1.00 32.41  ? 889 HOH A O   1 
HETATM 3572 O  O   . HOH C 3 .   ? 5.022   24.330  25.932  1.00 37.14  ? 890 HOH A O   1 
HETATM 3573 O  O   . HOH C 3 .   ? -10.806 1.959   24.426  1.00 39.01  ? 891 HOH A O   1 
HETATM 3574 O  O   . HOH C 3 .   ? 5.528   -13.404 20.773  1.00 34.95  ? 892 HOH A O   1 
HETATM 3575 O  O   . HOH C 3 .   ? 2.098   -10.746 -1.711  1.00 36.30  ? 893 HOH A O   1 
HETATM 3576 O  O   . HOH C 3 .   ? -8.200  -3.707  -18.066 1.00 66.23  ? 894 HOH A O   1 
HETATM 3577 O  O   . HOH C 3 .   ? 16.343  -7.813  -3.329  1.00 33.25  ? 895 HOH A O   1 
HETATM 3578 O  O   . HOH C 3 .   ? 2.289   -24.178 -5.674  1.00 50.75  ? 896 HOH A O   1 
HETATM 3579 O  O   . HOH C 3 .   ? 15.011  -4.056  -5.158  1.00 47.20  ? 897 HOH A O   1 
HETATM 3580 O  O   . HOH C 3 .   ? 15.063  9.671   15.041  1.00 36.59  ? 898 HOH A O   1 
HETATM 3581 O  O   . HOH C 3 .   ? 3.709   -12.219 22.771  1.00 23.62  ? 899 HOH A O   1 
HETATM 3582 O  O   . HOH C 3 .   ? 7.380   -19.159 7.763   1.00 21.42  ? 900 HOH A O   1 
HETATM 3583 O  O   . HOH C 3 .   ? 11.285  -7.648  20.504  1.00 35.70  ? 901 HOH A O   1 
HETATM 3584 O  O   . HOH C 3 .   ? 12.874  -26.158 -17.878 1.00 33.75  ? 902 HOH A O   1 
HETATM 3585 O  O   . HOH C 3 .   ? 6.251   6.337   25.772  1.00 35.65  ? 903 HOH A O   1 
HETATM 3586 O  O   . HOH C 3 .   ? -10.543 13.946  28.846  1.00 20.23  ? 904 HOH A O   1 
HETATM 3587 O  O   . HOH C 3 .   ? -11.156 26.630  1.848   1.00 28.21  ? 905 HOH A O   1 
HETATM 3588 O  O   . HOH C 3 .   ? -7.422  -19.329 -7.279  1.00 44.74  ? 906 HOH A O   1 
HETATM 3589 O  O   . HOH C 3 .   ? -4.019  23.048  19.372  1.00 40.79  ? 907 HOH A O   1 
HETATM 3590 O  O   . HOH C 3 .   ? 2.623   -21.586 -5.744  1.00 60.01  ? 908 HOH A O   1 
HETATM 3591 O  O   . HOH C 3 .   ? 0.458   6.332   -12.871 1.00 34.46  ? 909 HOH A O   1 
HETATM 3592 O  O   . HOH C 3 .   ? 2.535   -27.692 -8.668  1.00 34.87  ? 910 HOH A O   1 
HETATM 3593 O  O   . HOH C 3 .   ? 18.118  4.021   2.443   1.00 34.58  ? 911 HOH A O   1 
HETATM 3594 O  O   . HOH C 3 .   ? 10.246  18.430  18.673  1.00 39.70  ? 912 HOH A O   1 
HETATM 3595 O  O   . HOH C 3 .   ? 16.217  21.490  9.836   1.00 41.17  ? 913 HOH A O   1 
HETATM 3596 O  O   . HOH C 3 .   ? -5.069  -14.288 18.606  1.00 34.14  ? 914 HOH A O   1 
HETATM 3597 O  O   . HOH C 3 .   ? 16.433  8.863   12.472  1.00 31.50  ? 915 HOH A O   1 
HETATM 3598 O  O   . HOH C 3 .   ? -15.496 18.664  12.203  1.00 31.18  ? 916 HOH A O   1 
HETATM 3599 O  O   . HOH C 3 .   ? 12.878  -10.018 9.196   1.00 28.01  ? 917 HOH A O   1 
HETATM 3600 O  O   . HOH C 3 .   ? 5.324   -19.561 16.501  1.00 43.40  ? 918 HOH A O   1 
HETATM 3601 O  O   . HOH C 3 .   ? -11.451 16.392  28.191  1.00 32.14  ? 919 HOH A O   1 
HETATM 3602 O  O   . HOH C 3 .   ? 13.749  4.396   1.584   1.00 22.04  ? 920 HOH A O   1 
HETATM 3603 O  O   . HOH C 3 .   ? -10.995 -18.019 -28.043 1.00 36.58  ? 921 HOH A O   1 
HETATM 3604 O  O   . HOH C 3 .   ? 15.604  9.714   -8.171  1.00 28.74  ? 922 HOH A O   1 
HETATM 3605 O  O   . HOH C 3 .   ? -10.333 15.548  33.010  1.00 38.63  ? 923 HOH A O   1 
HETATM 3606 O  O   . HOH C 3 .   ? 17.241  10.338  -4.587  1.00 19.34  ? 924 HOH A O   1 
HETATM 3607 O  O   . HOH C 3 .   ? 6.677   -22.278 4.876   1.00 36.54  ? 925 HOH A O   1 
HETATM 3608 O  O   . HOH C 3 .   ? -8.296  19.962  20.548  1.00 46.76  ? 926 HOH A O   1 
HETATM 3609 O  O   . HOH C 3 .   ? 6.243   23.014  8.029   1.00 40.69  ? 927 HOH A O   1 
HETATM 3610 O  O   . HOH C 3 .   ? -8.271  -13.798 15.932  1.00 24.76  ? 928 HOH A O   1 
HETATM 3611 O  O   . HOH C 3 .   ? -20.212 12.677  -1.399  1.00 39.80  ? 929 HOH A O   1 
HETATM 3612 O  O   . HOH C 3 .   ? 1.926   -18.169 -4.230  1.00 37.57  ? 930 HOH A O   1 
HETATM 3613 O  O   . HOH C 3 .   ? 20.193  -11.491 9.434   1.00 39.73  ? 931 HOH A O   1 
HETATM 3614 O  O   . HOH C 3 .   ? 0.073   -26.648 -9.428  1.00 33.39  ? 932 HOH A O   1 
HETATM 3615 O  O   . HOH C 3 .   ? 11.996  -9.583  17.072  1.00 32.76  ? 933 HOH A O   1 
HETATM 3616 O  O   . HOH C 3 .   ? 13.737  -8.177  15.946  1.00 29.43  ? 934 HOH A O   1 
HETATM 3617 O  O   . HOH C 3 .   ? 16.184  -9.286  15.186  1.00 34.15  ? 935 HOH A O   1 
HETATM 3618 O  O   . HOH C 3 .   ? -15.283 -5.810  20.035  1.00 47.13  ? 936 HOH A O   1 
HETATM 3619 O  O   . HOH C 3 .   ? 16.498  -11.245 17.732  1.00 27.46  ? 937 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   . ILE A 18  ? 0.5699 0.3780 0.3514 -0.1398 0.1937  -0.0615 4   ILE A N   
2    C  CA  . ILE A 18  ? 0.4151 0.3658 0.4594 -0.1675 -0.0408 -0.0420 4   ILE A CA  
3    C  C   . ILE A 18  ? 0.5413 0.3357 0.2800 -0.0310 0.0568  -0.0003 4   ILE A C   
4    O  O   . ILE A 18  ? 0.5035 0.6348 0.3573 -0.0454 0.0517  0.1041  4   ILE A O   
5    C  CB  . ILE A 18  ? 0.4482 0.5211 0.4454 -0.0753 0.0302  -0.0366 4   ILE A CB  
6    C  CG1 . ILE A 18  ? 0.4010 0.4976 0.5196 -0.0262 0.0111  -0.0655 4   ILE A CG1 
7    C  CG2 . ILE A 18  ? 0.4101 0.5170 0.3888 -0.1495 -0.0353 0.0291  4   ILE A CG2 
8    C  CD1 . ILE A 18  ? 0.4368 0.5192 0.4434 -0.0088 0.0847  -0.0210 4   ILE A CD1 
9    N  N   . LYS A 19  ? 0.3827 0.4309 0.3295 -0.0507 -0.0735 -0.0463 5   LYS A N   
10   C  CA  . LYS A 19  ? 0.2684 0.5229 0.3426 -0.0595 -0.0255 -0.0228 5   LYS A CA  
11   C  C   . LYS A 19  ? 0.4250 0.7190 0.3527 -0.0412 0.0126  0.0400  5   LYS A C   
12   O  O   . LYS A 19  ? 0.3047 0.6164 0.4241 -0.1186 0.0342  -0.0524 5   LYS A O   
13   C  CB  . LYS A 19  ? 0.3934 0.4775 0.5109 0.0441  -0.1047 0.0461  5   LYS A CB  
14   N  N   . LYS A 20  ? 0.3020 0.6781 0.4175 0.0573  0.0113  -0.0151 6   LYS A N   
15   C  CA  . LYS A 20  ? 0.3818 0.5814 0.3199 -0.0073 -0.0344 0.0202  6   LYS A CA  
16   C  C   . LYS A 20  ? 0.4511 0.3516 0.3301 0.0791  -0.0866 -0.0460 6   LYS A C   
17   O  O   . LYS A 20  ? 0.5134 0.4281 0.4165 0.0771  -0.0401 -0.1171 6   LYS A O   
18   C  CB  . LYS A 20  ? 0.3922 0.5203 0.3773 -0.0412 -0.0828 0.0255  6   LYS A CB  
19   N  N   . LYS A 21  ? 0.3078 0.3373 0.4126 -0.0243 -0.1092 0.0029  7   LYS A N   
20   C  CA  . LYS A 21  ? 0.2761 0.2294 0.3782 -0.0302 -0.0424 -0.1286 7   LYS A CA  
21   C  C   . LYS A 21  ? 0.2501 0.2132 0.4062 -0.0383 -0.0902 -0.0561 7   LYS A C   
22   O  O   . LYS A 21  ? 0.3541 0.2398 0.4225 0.0179  -0.1246 -0.0937 7   LYS A O   
23   C  CB  . LYS A 21  ? 0.3226 0.4071 0.3117 -0.0660 -0.0214 0.0137  7   LYS A CB  
24   N  N   . ASN A 22  ? 0.2291 0.2055 0.2600 -0.0133 -0.0238 -0.0787 8   ASN A N   
25   C  CA  . ASN A 22  ? 0.2318 0.2446 0.2748 -0.0232 -0.0719 -0.0529 8   ASN A CA  
26   C  C   . ASN A 22  ? 0.3003 0.1812 0.2420 0.0028  -0.0494 -0.0613 8   ASN A C   
27   O  O   . ASN A 22  ? 0.3019 0.3006 0.2804 -0.0081 -0.0713 -0.0354 8   ASN A O   
28   C  CB  . ASN A 22  ? 0.2692 0.1891 0.2441 -0.0408 -0.0677 -0.0762 8   ASN A CB  
29   C  CG  . ASN A 22  ? 0.2114 0.2282 0.2102 -0.0153 -0.0571 -0.0324 8   ASN A CG  
30   O  OD1 . ASN A 22  ? 0.3096 0.2415 0.2230 0.0610  -0.0480 -0.0463 8   ASN A OD1 
31   N  ND2 . ASN A 22  ? 0.2645 0.2164 0.2378 0.0119  -0.0794 -0.0357 8   ASN A ND2 
32   N  N   . LYS A 23  ? 0.2447 0.2458 0.2294 -0.0149 -0.0348 -0.0281 9   LYS A N   
33   C  CA  . LYS A 23  ? 0.1917 0.2322 0.2785 0.0099  -0.0375 -0.0418 9   LYS A CA  
34   C  C   . LYS A 23  ? 0.2047 0.1985 0.2079 -0.0239 0.0167  -0.0169 9   LYS A C   
35   O  O   . LYS A 23  ? 0.2285 0.2522 0.2218 0.0000  -0.0253 -0.0060 9   LYS A O   
36   C  CB  . LYS A 23  ? 0.3749 0.2551 0.2386 -0.0228 -0.0139 -0.1046 9   LYS A CB  
37   C  CG  . LYS A 23  ? 0.2654 0.2808 0.3723 0.0756  -0.0266 -0.0090 9   LYS A CG  
38   C  CD  . LYS A 23  ? 0.5213 0.4335 0.5282 0.0892  -0.0131 -0.1264 9   LYS A CD  
39   C  CE  . LYS A 23  ? 0.6335 0.3718 0.5069 0.0725  0.0386  -0.1377 9   LYS A CE  
40   N  N   . ASP A 24  ? 0.2485 0.2277 0.2286 -0.0037 -0.0165 -0.0679 10  ASP A N   
41   C  CA  . ASP A 24  ? 0.2271 0.1958 0.1962 -0.0115 0.0021  -0.0509 10  ASP A CA  
42   C  C   . ASP A 24  ? 0.2270 0.1950 0.1900 0.0030  0.0157  -0.0205 10  ASP A C   
43   O  O   . ASP A 24  ? 0.2803 0.1970 0.1960 -0.0246 0.0138  -0.0513 10  ASP A O   
44   C  CB  . ASP A 24  ? 0.2070 0.2628 0.2104 0.0022  -0.0136 -0.0319 10  ASP A CB  
45   C  CG  . ASP A 24  ? 0.3157 0.2406 0.2731 0.0308  0.0134  -0.0419 10  ASP A CG  
46   O  OD1 . ASP A 24  ? 0.2858 0.3230 0.3053 0.0565  0.0232  -0.0219 10  ASP A OD1 
47   O  OD2 . ASP A 24  ? 0.5363 0.3381 0.2814 0.0245  -0.0052 -0.0675 10  ASP A OD2 
48   N  N   . ILE A 25  ? 0.1865 0.2113 0.1603 0.0037  -0.0039 -0.0289 11  ILE A N   
49   C  CA  . ILE A 25  ? 0.1977 0.1889 0.1630 0.0098  0.0015  -0.0604 11  ILE A CA  
50   C  C   . ILE A 25  ? 0.1589 0.1671 0.1675 0.0047  -0.0057 -0.0169 11  ILE A C   
51   O  O   . ILE A 25  ? 0.1689 0.2100 0.1635 -0.0211 0.0056  -0.0378 11  ILE A O   
52   C  CB  . ILE A 25  ? 0.1775 0.2359 0.1539 -0.0198 -0.0385 -0.0267 11  ILE A CB  
53   C  CG1 . ILE A 25  ? 0.2486 0.2519 0.3222 0.0517  -0.0479 -0.0208 11  ILE A CG1 
54   C  CG2 . ILE A 25  ? 0.1841 0.2231 0.1961 0.0109  0.0266  -0.0416 11  ILE A CG2 
55   C  CD1 . ILE A 25  ? 0.1876 0.3251 0.3008 0.0362  -0.0079 0.0494  11  ILE A CD1 
56   N  N   . ARG A 26  ? 0.1497 0.1711 0.1477 -0.0160 -0.0024 -0.0164 12  ARG A N   
57   C  CA  . ARG A 26  ? 0.1202 0.1580 0.1818 0.0090  -0.0015 -0.0205 12  ARG A CA  
58   C  C   . ARG A 26  ? 0.1157 0.1548 0.1344 0.0074  -0.0001 -0.0149 12  ARG A C   
59   O  O   . ARG A 26  ? 0.1333 0.1545 0.1441 -0.0023 -0.0032 -0.0073 12  ARG A O   
60   C  CB  . ARG A 26  ? 0.1516 0.1661 0.1983 0.0287  0.0034  -0.0160 12  ARG A CB  
61   C  CG  . ARG A 26  ? 0.2064 0.1891 0.2095 0.0644  -0.0291 -0.0174 12  ARG A CG  
62   C  CD  . ARG A 26  ? 0.2444 0.1672 0.2418 0.0381  -0.0193 -0.0522 12  ARG A CD  
63   N  NE  . ARG A 26  ? 0.2124 0.1539 0.2237 0.0181  0.0046  -0.0284 12  ARG A NE  
64   C  CZ  . ARG A 26  ? 0.2108 0.1472 0.1953 0.0249  0.0013  -0.0144 12  ARG A CZ  
65   N  NH1 . ARG A 26  ? 0.2700 0.1558 0.2318 0.0317  0.0023  -0.0252 12  ARG A NH1 
66   N  NH2 . ARG A 26  ? 0.1963 0.1799 0.2422 0.0404  -0.0004 -0.0204 12  ARG A NH2 
67   N  N   . ILE A 27  ? 0.1428 0.1392 0.1363 0.0027  0.0141  -0.0145 13  ILE A N   
68   C  CA  . ILE A 27  ? 0.1195 0.1412 0.1428 0.0078  0.0116  -0.0158 13  ILE A CA  
69   C  C   . ILE A 27  ? 0.1213 0.1295 0.1244 0.0196  -0.0008 0.0128  13  ILE A C   
70   O  O   . ILE A 27  ? 0.1322 0.1591 0.1285 0.0031  0.0108  -0.0095 13  ILE A O   
71   C  CB  . ILE A 27  ? 0.1360 0.1564 0.1479 0.0051  0.0102  -0.0098 13  ILE A CB  
72   C  CG1 . ILE A 27  ? 0.1766 0.1826 0.1712 0.0306  0.0076  -0.0044 13  ILE A CG1 
73   C  CG2 . ILE A 27  ? 0.1434 0.1593 0.1864 0.0190  -0.0054 0.0034  13  ILE A CG2 
74   C  CD1 . ILE A 27  ? 0.1525 0.1862 0.1738 0.0224  -0.0012 -0.0098 13  ILE A CD1 
75   N  N   . ILE A 28  ? 0.0978 0.1373 0.1166 0.0071  0.0092  -0.0101 14  ILE A N   
76   C  CA  . ILE A 28  ? 0.1087 0.1457 0.1269 -0.0012 0.0098  0.0084  14  ILE A CA  
77   C  C   . ILE A 28  ? 0.0965 0.1455 0.1157 -0.0014 -0.0011 -0.0121 14  ILE A C   
78   O  O   . ILE A 28  ? 0.1202 0.1303 0.1373 -0.0084 0.0085  0.0008  14  ILE A O   
79   C  CB  . ILE A 28  ? 0.1246 0.1488 0.1493 0.0058  0.0178  0.0126  14  ILE A CB  
80   C  CG1 . ILE A 28  ? 0.1361 0.1351 0.1377 0.0307  0.0184  -0.0074 14  ILE A CG1 
81   C  CG2 . ILE A 28  ? 0.1399 0.1620 0.1710 -0.0051 0.0127  0.0186  14  ILE A CG2 
82   C  CD1 . ILE A 28  ? 0.1983 0.1476 0.1888 0.0265  0.0063  -0.0257 14  ILE A CD1 
83   N  N   . PRO A 29  ? 0.1177 0.1219 0.1244 0.0121  0.0088  0.0168  15  PRO A N   
84   C  CA  . PRO A 29  ? 0.1203 0.1107 0.1458 0.0093  -0.0076 -0.0021 15  PRO A CA  
85   C  C   . PRO A 29  ? 0.1048 0.1358 0.1429 0.0151  0.0107  0.0000  15  PRO A C   
86   O  O   . PRO A 29  ? 0.1084 0.1736 0.1695 0.0103  0.0137  0.0339  15  PRO A O   
87   C  CB  . PRO A 29  ? 0.1479 0.1320 0.1451 0.0057  0.0033  0.0128  15  PRO A CB  
88   C  CG  . PRO A 29  ? 0.1597 0.1735 0.1976 0.0326  0.0029  0.0039  15  PRO A CG  
89   C  CD  . PRO A 29  ? 0.1562 0.1374 0.1742 -0.0075 0.0425  0.0053  15  PRO A CD  
90   N  N   . LEU A 30  ? 0.1132 0.1116 0.1286 0.0025  0.0016  0.0000  16  LEU A N   
91   C  CA  . LEU A 30  ? 0.0832 0.1241 0.1474 -0.0008 0.0067  0.0202  16  LEU A CA  
92   C  C   . LEU A 30  ? 0.1176 0.1219 0.1388 0.0016  0.0047  0.0021  16  LEU A C   
93   O  O   . LEU A 30  ? 0.1432 0.1218 0.1568 0.0264  -0.0150 -0.0022 16  LEU A O   
94   C  CB  . LEU A 30  ? 0.1096 0.1493 0.1727 0.0154  -0.0168 0.0172  16  LEU A CB  
95   C  CG  . LEU A 30  ? 0.1140 0.1173 0.1603 0.0052  -0.0130 0.0068  16  LEU A CG  
96   C  CD1 . LEU A 30  ? 0.1125 0.1339 0.2064 0.0193  -0.0183 0.0172  16  LEU A CD1 
97   C  CD2 . LEU A 30  ? 0.1406 0.1202 0.1744 0.0204  0.0057  -0.0118 16  LEU A CD2 
98   N  N   . GLY A 31  ? 0.1053 0.1202 0.1430 0.0047  -0.0001 0.0010  17  GLY A N   
99   C  CA  . GLY A 31  ? 0.1244 0.1151 0.1616 0.0015  -0.0028 0.0216  17  GLY A CA  
100  C  C   . GLY A 31  ? 0.1212 0.1167 0.1398 -0.0033 0.0051  0.0149  17  GLY A C   
101  O  O   . GLY A 31  ? 0.1197 0.1126 0.1648 0.0082  -0.0062 0.0251  17  GLY A O   
102  N  N   . GLY A 32  ? 0.1095 0.1127 0.1613 -0.0010 -0.0039 0.0137  18  GLY A N   
103  C  CA  . GLY A 32  ? 0.1220 0.1030 0.1262 0.0261  0.0035  0.0154  18  GLY A CA  
104  C  C   . GLY A 32  ? 0.1194 0.1320 0.1508 0.0072  0.0049  0.0073  18  GLY A C   
105  O  O   . GLY A 32  ? 0.1323 0.1245 0.1669 0.0102  -0.0101 0.0238  18  GLY A O   
106  N  N   . VAL A 33  ? 0.1332 0.1103 0.1492 0.0007  0.0045  0.0239  19  VAL A N   
107  C  CA  . VAL A 33  ? 0.1389 0.1287 0.1873 0.0065  0.0031  0.0264  19  VAL A CA  
108  C  C   . VAL A 33  ? 0.1477 0.1494 0.1923 -0.0096 0.0114  0.0245  19  VAL A C   
109  O  O   . VAL A 33  ? 0.1369 0.1362 0.2566 -0.0032 -0.0038 0.0003  19  VAL A O   
110  C  CB  . VAL A 33  ? 0.1470 0.1623 0.1598 0.0148  0.0210  0.0260  19  VAL A CB  
111  C  CG1 . VAL A 33  ? 0.1368 0.1823 0.1625 -0.0014 0.0119  0.0144  19  VAL A CG1 
112  C  CG2 . VAL A 33  ? 0.1572 0.1657 0.1834 0.0184  0.0236  0.0001  19  VAL A CG2 
113  N  N   . GLY A 34  ? 0.1477 0.1432 0.2286 0.0058  0.0188  0.0167  20  GLY A N   
114  C  CA  . GLY A 34  ? 0.1519 0.1556 0.2667 -0.0201 0.0117  0.0041  20  GLY A CA  
115  C  C   . GLY A 34  ? 0.1992 0.1237 0.2783 -0.0285 -0.0183 0.0361  20  GLY A C   
116  O  O   . GLY A 34  ? 0.1908 0.2500 0.3532 -0.0714 -0.0724 0.0589  20  GLY A O   
117  N  N   . GLU A 35  ? 0.1727 0.1231 0.2141 -0.0311 -0.0004 0.0138  21  GLU A N   
118  C  CA  . GLU A 35  ? 0.2282 0.1234 0.2081 -0.0518 -0.0126 0.0070  21  GLU A CA  
119  C  C   . GLU A 35  ? 0.2104 0.1132 0.1720 -0.0205 0.0334  -0.0063 21  GLU A C   
120  O  O   . GLU A 35  ? 0.1774 0.1668 0.2063 -0.0059 0.0005  -0.0118 21  GLU A O   
121  C  CB  . GLU A 35  ? 0.2354 0.1627 0.2387 -0.0596 -0.0481 0.0101  21  GLU A CB  
122  C  CG  . GLU A 35  ? 0.1824 0.1563 0.1966 -0.0475 -0.0142 0.0108  21  GLU A CG  
123  C  CD  . GLU A 35  ? 0.1765 0.1911 0.1987 -0.0210 -0.0029 -0.0102 21  GLU A CD  
124  O  OE1 . GLU A 35  ? 0.1687 0.1600 0.2146 -0.0093 -0.0445 -0.0049 21  GLU A OE1 
125  O  OE2 . GLU A 35  ? 0.1542 0.2697 0.2757 -0.0044 -0.0335 -0.0094 21  GLU A OE2 
126  N  N   . ILE A 36  ? 0.4465 0.0950 0.2436 -0.0227 0.0139  0.0008  22  ILE A N   
127  C  CA  . ILE A 36  ? 0.3446 0.2275 0.2593 -0.0220 0.0349  -0.0171 22  ILE A CA  
128  C  C   . ILE A 36  ? 0.1573 0.4210 0.3518 0.0574  -0.0876 -0.0257 22  ILE A C   
129  O  O   . ILE A 36  ? 0.2433 0.3663 0.7263 0.0159  0.1657  -0.2357 22  ILE A O   
134  N  N   . ALA A 37  ? 0.2374 0.1135 0.2134 -0.0160 -0.0446 0.0144  23  ALA A N   
135  C  CA  . ALA A 37  ? 0.2389 0.1178 0.1743 -0.0353 -0.0116 -0.0103 23  ALA A CA  
136  C  C   . ALA A 37  ? 0.2279 0.1368 0.1880 -0.0483 0.0327  -0.0285 23  ALA A C   
137  O  O   . ALA A 37  ? 0.3004 0.1490 0.1864 -0.0998 0.0474  -0.0286 23  ALA A O   
138  C  CB  . ALA A 37  ? 0.3570 0.1675 0.2231 -0.0032 -0.0185 -0.0133 23  ALA A CB  
139  N  N   . LYS A 38  ? 0.1929 0.1158 0.1560 -0.0226 0.0241  -0.0065 24  LYS A N   
140  C  CA  . LYS A 38  ? 0.1607 0.1131 0.1835 -0.0159 0.0117  -0.0180 24  LYS A CA  
141  C  C   . LYS A 38  ? 0.1531 0.1017 0.1551 -0.0286 0.0201  -0.0068 24  LYS A C   
142  O  O   . LYS A 38  ? 0.1343 0.1713 0.2216 -0.0402 0.0153  -0.0602 24  LYS A O   
143  C  CB  . LYS A 38  ? 0.3404 0.2181 0.2542 0.0428  -0.0577 -0.1091 24  LYS A CB  
144  C  CG  . LYS A 38  ? 0.2719 0.1862 0.2668 -0.0316 -0.0798 0.0621  24  LYS A CG  
145  C  CD  . LYS A 38  ? 0.2834 0.2818 0.2351 0.0815  -0.0476 -0.0117 24  LYS A CD  
146  C  CE  . LYS A 38  ? 0.3552 0.1552 0.1627 0.0805  -0.0847 -0.0018 24  LYS A CE  
147  N  NZ  . LYS A 38  ? 0.2689 0.2203 0.1777 0.0589  -0.0771 0.0031  24  LYS A NZ  
148  N  N   . ASN A 39  ? 0.1479 0.1039 0.1648 -0.0106 0.0157  -0.0076 25  ASN A N   
149  C  CA  . ASN A 39  ? 0.1219 0.0985 0.1425 -0.0052 0.0147  0.0241  25  ASN A CA  
150  C  C   . ASN A 39  ? 0.1221 0.0939 0.1377 -0.0149 0.0133  0.0123  25  ASN A C   
151  O  O   . ASN A 39  ? 0.1190 0.0944 0.1394 -0.0085 0.0103  0.0148  25  ASN A O   
152  C  CB  . ASN A 39  ? 0.1626 0.0970 0.1714 0.0247  0.0146  0.0299  25  ASN A CB  
153  C  CG  . ASN A 39  ? 0.1741 0.1447 0.1980 0.0105  0.0556  -0.0077 25  ASN A CG  
154  O  OD1 . ASN A 39  ? 0.3033 0.1492 0.1900 0.0401  0.0384  0.0303  25  ASN A OD1 
155  N  ND2 . ASN A 39  ? 0.2881 0.1640 0.2380 0.0260  0.0615  -0.0248 25  ASN A ND2 
156  N  N   . MET A 40  ? 0.1038 0.0773 0.1134 0.0000  0.0094  0.0094  26  MET A N   
157  C  CA  . MET A 40  ? 0.0852 0.0800 0.1345 0.0030  -0.0152 0.0066  26  MET A CA  
158  C  C   . MET A 40  ? 0.1179 0.0829 0.1431 0.0162  0.0033  0.0156  26  MET A C   
159  O  O   . MET A 40  ? 0.1026 0.1159 0.1338 0.0044  0.0075  0.0045  26  MET A O   
160  C  CB  . MET A 40  ? 0.0999 0.0912 0.1203 -0.0040 -0.0112 0.0033  26  MET A CB  
161  C  CG  . MET A 40  ? 0.0885 0.0932 0.1596 0.0029  -0.0228 0.0134  26  MET A CG  
162  S  SD  . MET A 40  ? 0.1277 0.1126 0.1739 0.0141  0.0015  0.0278  26  MET A SD  
163  C  CE  . MET A 40  ? 0.1353 0.1182 0.2141 0.0207  -0.0029 0.0387  26  MET A CE  
164  N  N   . TYR A 41  ? 0.0998 0.0958 0.1251 -0.0047 0.0006  0.0070  27  TYR A N   
165  C  CA  . TYR A 41  ? 0.0823 0.1185 0.1311 0.0022  0.0080  0.0050  27  TYR A CA  
166  C  C   . TYR A 41  ? 0.1017 0.1201 0.1421 0.0096  0.0202  -0.0001 27  TYR A C   
167  O  O   . TYR A 41  ? 0.1247 0.1183 0.1705 -0.0049 0.0349  -0.0203 27  TYR A O   
168  C  CB  . TYR A 41  ? 0.1026 0.1225 0.1380 0.0204  -0.0110 0.0255  27  TYR A CB  
169  C  CG  . TYR A 41  ? 0.1050 0.1169 0.1437 0.0115  -0.0035 0.0187  27  TYR A CG  
170  C  CD1 . TYR A 41  ? 0.1118 0.1065 0.1376 0.0155  0.0053  -0.0015 27  TYR A CD1 
171  C  CD2 . TYR A 41  ? 0.1383 0.1228 0.1273 -0.0255 0.0107  0.0120  27  TYR A CD2 
172  C  CE1 . TYR A 41  ? 0.1283 0.1047 0.1507 -0.0038 -0.0027 0.0050  27  TYR A CE1 
173  C  CE2 . TYR A 41  ? 0.1404 0.1267 0.1242 0.0133  0.0148  0.0008  27  TYR A CE2 
174  C  CZ  . TYR A 41  ? 0.1152 0.1173 0.1382 0.0035  -0.0022 0.0157  27  TYR A CZ  
175  O  OH  . TYR A 41  ? 0.1397 0.1135 0.1567 0.0088  -0.0201 0.0215  27  TYR A OH  
176  N  N   . ILE A 42  ? 0.1053 0.1124 0.1433 -0.0068 0.0075  0.0089  28  ILE A N   
177  C  CA  . ILE A 42  ? 0.0974 0.1138 0.1454 0.0004  0.0299  0.0021  28  ILE A CA  
178  C  C   . ILE A 42  ? 0.1188 0.1172 0.1354 0.0050  0.0210  -0.0074 28  ILE A C   
179  O  O   . ILE A 42  ? 0.1276 0.1535 0.1287 -0.0088 0.0078  -0.0018 28  ILE A O   
180  C  CB  . ILE A 42  ? 0.1099 0.1419 0.1366 0.0134  0.0193  0.0092  28  ILE A CB  
181  C  CG1 . ILE A 42  ? 0.1177 0.1411 0.1847 0.0300  -0.0050 0.0267  28  ILE A CG1 
182  C  CG2 . ILE A 42  ? 0.1252 0.1525 0.1834 0.0325  0.0002  0.0094  28  ILE A CG2 
183  C  CD1 . ILE A 42  ? 0.1128 0.2110 0.2016 0.0318  0.0016  0.0206  28  ILE A CD1 
184  N  N   . VAL A 43  ? 0.1240 0.1210 0.1185 -0.0077 0.0007  -0.0177 29  VAL A N   
185  C  CA  . VAL A 43  ? 0.1178 0.1295 0.1322 -0.0071 0.0124  -0.0094 29  VAL A CA  
186  C  C   . VAL A 43  ? 0.1264 0.1543 0.1396 -0.0109 -0.0052 -0.0030 29  VAL A C   
187  O  O   . VAL A 43  ? 0.1634 0.1530 0.1630 -0.0261 0.0161  -0.0173 29  VAL A O   
188  C  CB  . VAL A 43  ? 0.1384 0.1618 0.1529 -0.0018 -0.0070 -0.0027 29  VAL A CB  
189  C  CG1 . VAL A 43  ? 0.1403 0.2028 0.1852 0.0002  -0.0453 -0.0045 29  VAL A CG1 
190  C  CG2 . VAL A 43  ? 0.1425 0.1587 0.1638 0.0276  0.0013  -0.0140 29  VAL A CG2 
191  N  N   . GLU A 44  ? 0.1463 0.1293 0.1611 -0.0082 -0.0044 0.0028  30  GLU A N   
192  C  CA  . GLU A 44  ? 0.1463 0.1479 0.1527 -0.0097 -0.0046 0.0088  30  GLU A CA  
193  C  C   . GLU A 44  ? 0.1454 0.1467 0.1720 -0.0035 -0.0069 -0.0039 30  GLU A C   
194  O  O   . GLU A 44  ? 0.1463 0.1696 0.1534 -0.0100 -0.0145 -0.0100 30  GLU A O   
195  C  CB  . GLU A 44  ? 0.1747 0.1416 0.1799 0.0241  -0.0183 -0.0080 30  GLU A CB  
196  C  CG  . GLU A 44  ? 0.1825 0.1649 0.1815 0.0020  0.0091  0.0006  30  GLU A CG  
197  C  CD  . GLU A 44  ? 0.2069 0.1726 0.2072 -0.0306 0.0016  -0.0108 30  GLU A CD  
198  O  OE1 . GLU A 44  ? 0.2105 0.1904 0.2669 0.0262  -0.0153 -0.0065 30  GLU A OE1 
199  O  OE2 . GLU A 44  ? 0.1639 0.1860 0.2237 0.0136  -0.0179 -0.0012 30  GLU A OE2 
200  N  N   . VAL A 45  ? 0.1518 0.1571 0.1577 -0.0243 -0.0144 -0.0091 31  VAL A N   
201  C  CA  . VAL A 45  ? 0.1617 0.1415 0.1756 0.0200  -0.0212 -0.0347 31  VAL A CA  
202  C  C   . VAL A 45  ? 0.2036 0.1791 0.1774 -0.0194 -0.0279 -0.0163 31  VAL A C   
203  O  O   . VAL A 45  ? 0.1726 0.1674 0.2030 -0.0222 -0.0134 -0.0321 31  VAL A O   
204  C  CB  . VAL A 45  ? 0.1427 0.2079 0.1946 0.0144  -0.0419 -0.0467 31  VAL A CB  
205  C  CG1 . VAL A 45  ? 0.1474 0.2437 0.2089 -0.0112 -0.0219 -0.0296 31  VAL A CG1 
206  C  CG2 . VAL A 45  ? 0.1340 0.2090 0.1766 0.0116  -0.0136 -0.0125 31  VAL A CG2 
207  N  N   . ASP A 46  ? 0.2284 0.1602 0.2157 0.0081  -0.0213 -0.0299 32  ASP A N   
208  C  CA  . ASP A 46  ? 0.2070 0.1521 0.2194 -0.0086 -0.0186 -0.0403 32  ASP A CA  
209  C  C   . ASP A 46  ? 0.1916 0.2013 0.2268 0.0169  0.0112  -0.0156 32  ASP A C   
210  O  O   . ASP A 46  ? 0.1942 0.1948 0.2513 0.0110  -0.0192 -0.0371 32  ASP A O   
211  C  CB  . ASP A 46  ? 0.2983 0.2439 0.2484 -0.0583 -0.0182 -0.0555 32  ASP A CB  
212  C  CG  . ASP A 46  ? 0.3243 0.2870 0.3296 -0.0864 -0.0380 -0.1328 32  ASP A CG  
213  O  OD1 . ASP A 46  ? 0.4289 0.2941 0.2742 -0.1069 -0.0371 -0.0269 32  ASP A OD1 
214  O  OD2 . ASP A 46  ? 0.4967 0.3462 0.2860 0.0156  -0.1302 -0.0250 32  ASP A OD2 
215  N  N   . ASP A 47  ? 0.2347 0.1781 0.1979 0.0011  0.0000  -0.0434 33  ASP A N   
216  C  CA  . ASP A 47  ? 0.2289 0.1626 0.2280 -0.0219 -0.0204 0.0044  33  ASP A CA  
217  C  C   . ASP A 47  ? 0.2085 0.1946 0.2024 -0.0032 -0.0171 -0.0134 33  ASP A C   
218  O  O   . ASP A 47  ? 0.2260 0.1734 0.2806 -0.0110 -0.0030 -0.0052 33  ASP A O   
219  C  CB  . ASP A 47  ? 0.2608 0.1544 0.2837 0.0216  -0.0174 -0.0404 33  ASP A CB  
220  C  CG  . ASP A 47  ? 0.3208 0.2211 0.4061 0.0129  -0.0153 -0.0471 33  ASP A CG  
221  O  OD1 . ASP A 47  ? 0.3387 0.2207 0.5590 -0.0904 -0.0486 -0.0546 33  ASP A OD1 
222  O  OD2 . ASP A 47  ? 0.4904 0.1905 0.5177 -0.0156 -0.0035 -0.0312 33  ASP A OD2 
223  N  N   . GLU A 48  ? 0.1991 0.1563 0.2144 0.0031  -0.0163 -0.0175 34  GLU A N   
224  C  CA  . GLU A 48  ? 0.1974 0.1473 0.1962 -0.0044 -0.0317 -0.0150 34  GLU A CA  
225  C  C   . GLU A 48  ? 0.1560 0.1568 0.1837 -0.0022 -0.0085 0.0187  34  GLU A C   
226  O  O   . GLU A 48  ? 0.2129 0.1774 0.1899 -0.0298 -0.0223 -0.0174 34  GLU A O   
227  C  CB  . GLU A 48  ? 0.2130 0.1545 0.2311 -0.0143 0.0257  -0.0423 34  GLU A CB  
228  C  CG  . GLU A 48  ? 0.2215 0.2180 0.2878 -0.0051 0.0187  -0.0708 34  GLU A CG  
229  C  CD  . GLU A 48  ? 0.2810 0.3053 0.3189 -0.0020 0.0095  -0.0010 34  GLU A CD  
230  O  OE1 . GLU A 48  ? 0.2469 0.3327 0.4031 -0.0417 -0.0001 -0.0164 34  GLU A OE1 
231  O  OE2 . GLU A 48  ? 0.2346 0.3290 0.3089 -0.0328 0.0238  -0.0029 34  GLU A OE2 
232  N  N   . MET A 49  ? 0.1711 0.1382 0.1834 -0.0111 -0.0080 -0.0051 35  MET A N   
233  C  CA  . MET A 49  ? 0.1674 0.1422 0.1773 -0.0204 -0.0096 -0.0113 35  MET A CA  
234  C  C   . MET A 49  ? 0.1472 0.1465 0.1386 -0.0123 -0.0137 -0.0084 35  MET A C   
235  O  O   . MET A 49  ? 0.1557 0.1417 0.2071 0.0039  0.0051  0.0092  35  MET A O   
236  C  CB  . MET A 49  ? 0.1638 0.1545 0.2306 -0.0203 -0.0140 0.0070  35  MET A CB  
237  C  CG  . MET A 49  ? 0.1188 0.1620 0.1956 0.0178  -0.0085 0.0053  35  MET A CG  
238  S  SD  . MET A 49  ? 0.1985 0.1732 0.2876 0.0071  -0.0521 0.0132  35  MET A SD  
239  C  CE  . MET A 49  ? 0.2796 0.2598 0.2731 -0.0129 -0.0950 0.0776  35  MET A CE  
240  N  N   . PHE A 50  ? 0.1265 0.1260 0.1600 -0.0098 -0.0098 -0.0100 36  PHE A N   
241  C  CA  . PHE A 50  ? 0.1506 0.1322 0.1610 -0.0193 0.0028  -0.0065 36  PHE A CA  
242  C  C   . PHE A 50  ? 0.1234 0.1321 0.1383 -0.0110 0.0078  -0.0019 36  PHE A C   
243  O  O   . PHE A 50  ? 0.1499 0.1817 0.1531 -0.0396 0.0147  -0.0132 36  PHE A O   
244  C  CB  . PHE A 50  ? 0.1380 0.1438 0.1808 -0.0148 -0.0052 -0.0265 36  PHE A CB  
245  C  CG  . PHE A 50  ? 0.1211 0.1819 0.2318 0.0026  -0.0129 -0.0003 36  PHE A CG  
246  C  CD1 . PHE A 50  ? 0.1455 0.2478 0.2812 -0.0069 -0.0037 -0.0628 36  PHE A CD1 
247  C  CD2 . PHE A 50  ? 0.1589 0.1903 0.2487 -0.0379 -0.0419 -0.0351 36  PHE A CD2 
248  C  CE1 . PHE A 50  ? 0.1520 0.2247 0.2889 -0.0372 -0.0244 -0.0478 36  PHE A CE1 
249  C  CE2 . PHE A 50  ? 0.2355 0.2062 0.2117 -0.0031 -0.0459 0.0077  36  PHE A CE2 
250  C  CZ  . PHE A 50  ? 0.2182 0.1686 0.2992 -0.0127 -0.0394 0.0155  36  PHE A CZ  
251  N  N   . MET A 51  ? 0.1043 0.0960 0.1343 -0.0134 0.0047  0.0022  37  MET A N   
252  C  CA  . MET A 51  ? 0.1067 0.1014 0.1599 -0.0026 -0.0062 -0.0068 37  MET A CA  
253  C  C   . MET A 51  ? 0.1063 0.1019 0.1506 -0.0071 0.0150  0.0032  37  MET A C   
254  O  O   . MET A 51  ? 0.1148 0.1033 0.1784 0.0139  0.0232  0.0118  37  MET A O   
255  C  CB  . MET A 51  ? 0.1126 0.1221 0.1536 -0.0038 0.0085  0.0017  37  MET A CB  
256  C  CG  . MET A 51  ? 0.1100 0.1223 0.1359 -0.0081 0.0096  -0.0111 37  MET A CG  
257  S  SD  . MET A 51  ? 0.1297 0.1457 0.1623 0.0089  -0.0031 0.0121  37  MET A SD  
258  C  CE  . MET A 51  ? 0.1395 0.1308 0.1830 0.0132  -0.0017 0.0308  37  MET A CE  
259  N  N   . LEU A 52  ? 0.0889 0.0980 0.1311 0.0019  0.0074  0.0004  38  LEU A N   
260  C  CA  . LEU A 52  ? 0.0954 0.1046 0.1395 0.0096  0.0034  -0.0034 38  LEU A CA  
261  C  C   . LEU A 52  ? 0.1308 0.0891 0.1347 0.0139  -0.0035 0.0061  38  LEU A C   
262  O  O   . LEU A 52  ? 0.1115 0.1208 0.1362 -0.0040 0.0009  0.0057  38  LEU A O   
263  C  CB  . LEU A 52  ? 0.0975 0.1319 0.1469 0.0133  0.0002  -0.0076 38  LEU A CB  
264  C  CG  . LEU A 52  ? 0.1263 0.1507 0.1425 0.0058  -0.0050 -0.0007 38  LEU A CG  
265  C  CD1 . LEU A 52  ? 0.1880 0.1428 0.1580 0.0105  -0.0127 0.0193  38  LEU A CD1 
266  C  CD2 . LEU A 52  ? 0.1647 0.2047 0.1629 -0.0038 -0.0160 -0.0087 38  LEU A CD2 
267  N  N   . ASP A 53  ? 0.1157 0.1045 0.1465 -0.0044 0.0020  0.0093  39  ASP A N   
268  C  CA  . ASP A 53  ? 0.1022 0.0991 0.1354 -0.0029 0.0100  0.0007  39  ASP A CA  
269  C  C   . ASP A 53  ? 0.1086 0.0931 0.1288 -0.0144 -0.0029 0.0070  39  ASP A C   
270  O  O   . ASP A 53  ? 0.1252 0.1110 0.1337 -0.0028 0.0012  -0.0007 39  ASP A O   
271  C  CB  . ASP A 53  ? 0.1007 0.1114 0.1508 -0.0008 -0.0169 0.0103  39  ASP A CB  
272  C  CG  . ASP A 53  ? 0.1297 0.1122 0.1357 -0.0065 -0.0023 0.0046  39  ASP A CG  
273  O  OD1 . ASP A 53  ? 0.1840 0.1357 0.1680 0.0175  -0.0060 0.0187  39  ASP A OD1 
274  O  OD2 . ASP A 53  ? 0.1133 0.1482 0.1945 0.0073  -0.0042 0.0083  39  ASP A OD2 
275  N  N   . ALA A 54  ? 0.1034 0.1034 0.1331 0.0153  -0.0094 0.0005  40  ALA A N   
276  C  CA  . ALA A 54  ? 0.1163 0.0978 0.1497 0.0102  -0.0078 0.0139  40  ALA A CA  
277  C  C   . ALA A 54  ? 0.0904 0.1200 0.1163 0.0050  -0.0010 0.0199  40  ALA A C   
278  O  O   . ALA A 54  ? 0.1313 0.1311 0.1242 0.0067  0.0016  0.0099  40  ALA A O   
279  C  CB  . ALA A 54  ? 0.1383 0.1331 0.1616 0.0023  0.0086  0.0214  40  ALA A CB  
280  N  N   . GLY A 55  ? 0.1097 0.1189 0.1260 0.0026  0.0037  0.0088  41  GLY A N   
281  C  CA  . GLY A 55  ? 0.1154 0.1217 0.1530 0.0073  -0.0010 -0.0101 41  GLY A CA  
282  C  C   . GLY A 55  ? 0.1518 0.1264 0.1398 -0.0002 0.0014  0.0063  41  GLY A C   
283  O  O   . GLY A 55  ? 0.1251 0.1318 0.1743 -0.0151 -0.0024 -0.0023 41  GLY A O   
284  N  N   . LEU A 56  ? 0.1342 0.1456 0.1372 0.0038  0.0014  -0.0124 42  LEU A N   
285  C  CA  . LEU A 56  ? 0.1279 0.1556 0.1521 -0.0031 -0.0012 0.0009  42  LEU A CA  
286  C  C   . LEU A 56  ? 0.1279 0.1741 0.1579 -0.0114 -0.0049 0.0044  42  LEU A C   
287  O  O   . LEU A 56  ? 0.1637 0.1500 0.1750 -0.0284 0.0003  -0.0083 42  LEU A O   
288  C  CB  . LEU A 56  ? 0.1585 0.2031 0.1707 -0.0296 -0.0337 -0.0029 42  LEU A CB  
289  C  CG  . LEU A 56  ? 0.1853 0.2018 0.1523 -0.0502 -0.0191 0.0161  42  LEU A CG  
290  C  CD1 . LEU A 56  ? 0.2310 0.2190 0.1862 -0.0156 0.0004  -0.0455 42  LEU A CD1 
291  C  CD2 . LEU A 56  ? 0.2059 0.3110 0.2178 -0.0712 -0.0359 0.0156  42  LEU A CD2 
292  N  N   . MET A 57  ? 0.1597 0.1572 0.1953 -0.0068 -0.0009 -0.0120 43  MET A N   
293  C  CA  . MET A 57  ? 0.1812 0.1689 0.1582 -0.0155 -0.0020 -0.0029 43  MET A CA  
294  C  C   . MET A 57  ? 0.2166 0.1912 0.2352 -0.0067 -0.0064 0.0077  43  MET A C   
295  O  O   . MET A 57  ? 0.2339 0.2099 0.2113 -0.0158 -0.0387 -0.0414 43  MET A O   
296  C  CB  . MET A 57  ? 0.2508 0.1892 0.1950 -0.0643 -0.0052 -0.0447 43  MET A CB  
297  C  CG  . MET A 57  ? 0.2296 0.2281 0.1999 -0.0286 0.0233  -0.0157 43  MET A CG  
298  S  SD  . MET A 57  ? 0.2265 0.2763 0.2909 -0.0240 0.0196  0.0223  43  MET A SD  
299  C  CE  . MET A 57  ? 0.2788 0.2571 0.3471 -0.0697 0.0165  0.0499  43  MET A CE  
300  N  N   . PHE A 58  ? 0.2372 0.1994 0.2451 -0.0227 0.0084  -0.0534 44  PHE A N   
301  C  CA  . PHE A 58  ? 0.3236 0.3127 0.2138 -0.0337 0.0278  -0.0488 44  PHE A CA  
302  C  C   . PHE A 58  ? 0.2955 0.2764 0.2170 -0.0484 0.0209  -0.0391 44  PHE A C   
303  O  O   . PHE A 58  ? 0.3370 0.3076 0.3122 -0.1207 -0.0412 0.0078  44  PHE A O   
304  C  CB  . PHE A 58  ? 0.3130 0.2802 0.2518 -0.0464 0.0176  -0.1027 44  PHE A CB  
305  C  CG  . PHE A 58  ? 0.3602 0.3061 0.2823 -0.0149 0.0128  -0.1221 44  PHE A CG  
306  C  CD1 . PHE A 58  ? 0.3262 0.3119 0.2617 -0.0742 0.0102  -0.1346 44  PHE A CD1 
307  C  CD2 . PHE A 58  ? 0.3338 0.3400 0.2812 -0.0240 0.0745  -0.0599 44  PHE A CD2 
308  C  CE1 . PHE A 58  ? 0.4148 0.3725 0.3097 -0.0049 0.0462  -0.1729 44  PHE A CE1 
309  C  CE2 . PHE A 58  ? 0.3560 0.2687 0.3201 -0.0622 0.0289  -0.0782 44  PHE A CE2 
310  C  CZ  . PHE A 58  ? 0.3092 0.2690 0.2428 -0.0554 0.0200  -0.0857 44  PHE A CZ  
311  N  N   . PRO A 59  ? 0.2644 0.3470 0.4220 -0.1368 -0.0639 -0.0254 45  PRO A N   
312  C  CA  . PRO A 59  ? 0.3072 0.3834 0.4384 -0.2055 -0.0070 -0.0710 45  PRO A CA  
313  C  C   . PRO A 59  ? 0.3930 0.4162 0.5533 -0.0606 0.0900  0.0354  45  PRO A C   
314  O  O   . PRO A 59  ? 0.4708 0.3693 0.6221 -0.1300 -0.0766 -0.0906 45  PRO A O   
315  C  CB  . PRO A 59  ? 0.4068 0.6231 0.5052 -0.0708 -0.1133 -0.0024 45  PRO A CB  
316  C  CG  . PRO A 59  ? 0.3741 0.6039 0.5111 -0.0539 -0.1044 0.0410  45  PRO A CG  
317  C  CD  . PRO A 59  ? 0.4558 0.5424 0.4122 -0.1143 -0.1097 0.0347  45  PRO A CD  
318  N  N   . GLU A 60  ? 0.2733 0.5084 0.4790 -0.0785 0.0296  0.0422  46  GLU A N   
319  C  CA  . GLU A 60  ? 0.5205 0.4598 0.5973 -0.1274 0.1702  0.1018  46  GLU A CA  
320  C  C   . GLU A 60  ? 0.6770 0.4550 0.7448 -0.1332 0.0059  0.0807  46  GLU A C   
321  O  O   . GLU A 60  ? 0.5261 0.5256 0.5951 -0.0670 -0.0462 0.0363  46  GLU A O   
322  N  N   . ASP A 61  ? 0.4912 0.5136 0.8217 -0.0620 0.0979  0.0664  47  ASP A N   
323  C  CA  . ASP A 61  ? 0.4770 0.4148 0.6665 -0.1735 0.0047  -0.0028 47  ASP A CA  
324  C  C   . ASP A 61  ? 0.3853 0.4692 0.5603 -0.1367 0.0283  -0.0152 47  ASP A C   
325  O  O   . ASP A 61  ? 0.6295 0.7069 0.5953 -0.0514 0.1450  -0.0977 47  ASP A O   
326  N  N   . MET A 63  ? 0.9709 0.6535 0.9152 -0.0490 -0.1450 -0.0637 49  MET A N   
327  C  CA  . MET A 63  ? 0.8762 0.6259 0.9391 -0.0972 -0.0502 -0.2017 49  MET A CA  
328  C  C   . MET A 63  ? 0.9783 0.5717 0.7414 -0.0995 0.0653  -0.4916 49  MET A C   
329  O  O   . MET A 63  ? 0.8712 0.8539 0.8831 -0.0977 -0.2278 -0.3088 49  MET A O   
330  C  CB  . MET A 63  ? 0.3608 0.5896 0.8702 -0.2098 -0.0453 -0.0981 49  MET A CB  
331  C  CG  . MET A 63  ? 0.5612 0.7182 0.7365 -0.3610 -0.1571 -0.4141 49  MET A CG  
332  S  SD  . MET A 63  ? 0.8173 0.4844 0.9743 -0.2370 -0.0258 -0.1388 49  MET A SD  
333  C  CE  . MET A 63  ? 0.5836 0.3520 0.5768 -0.1404 0.1178  -0.0563 49  MET A CE  
334  N  N   . LEU A 64  ? 1.1143 1.0725 0.6878 0.2999  0.1663  -0.4110 50  LEU A N   
335  C  CA  . LEU A 64  ? 1.4295 0.9215 0.6463 0.3431  0.4593  -0.4211 50  LEU A CA  
336  C  C   . LEU A 64  ? 0.6849 0.9459 0.8057 0.1696  0.1125  -0.7797 50  LEU A C   
337  O  O   . LEU A 64  ? 1.7969 0.9085 0.5142 0.3388  0.5255  0.3471  50  LEU A O   
338  C  CB  . LEU A 64  ? 1.0968 1.2028 0.5619 0.4285  0.3977  -0.4379 50  LEU A CB  
339  N  N   . GLY A 65  ? 1.2012 0.9879 1.2956 -0.0222 -0.0618 -0.7619 51  GLY A N   
340  C  CA  . GLY A 65  ? 0.9025 0.8634 1.2776 -0.1910 -0.2948 -0.7315 51  GLY A CA  
341  C  C   . GLY A 65  ? 1.1450 0.5739 1.2115 0.5515  0.0672  0.1371  51  GLY A C   
342  O  O   . GLY A 65  ? 0.8966 0.8776 1.2593 0.4248  -0.0629 -0.0578 51  GLY A O   
343  N  N   . VAL A 66  ? 0.7613 0.2954 0.8405 -0.0675 0.2542  -0.1834 52  VAL A N   
344  C  CA  . VAL A 66  ? 0.4758 0.4950 0.4384 -0.0135 0.0136  -0.1255 52  VAL A CA  
345  C  C   . VAL A 66  ? 0.3912 0.3148 0.4104 -0.0349 -0.1070 -0.0266 52  VAL A C   
346  O  O   . VAL A 66  ? 0.3577 0.5013 0.3594 -0.0860 -0.1431 -0.0791 52  VAL A O   
347  C  CB  . VAL A 66  ? 0.2951 0.5471 0.4746 -0.0884 -0.0508 -0.0952 52  VAL A CB  
348  C  CG1 . VAL A 66  ? 0.3626 0.4792 0.3819 -0.0668 -0.1594 -0.1446 52  VAL A CG1 
349  C  CG2 . VAL A 66  ? 0.3890 0.5166 0.4535 -0.0809 -0.0441 -0.1641 52  VAL A CG2 
350  N  N   . ASP A 67  ? 0.3093 0.5196 0.2503 -0.0558 -0.0934 -0.0628 53  ASP A N   
351  C  CA  . ASP A 67  ? 0.3713 0.4177 0.3310 -0.0057 -0.0681 -0.0632 53  ASP A CA  
352  C  C   . ASP A 67  ? 0.2959 0.3287 0.2647 -0.0219 -0.0662 -0.0063 53  ASP A C   
353  O  O   . ASP A 67  ? 0.3912 0.3637 0.2782 -0.0598 -0.0230 -0.0817 53  ASP A O   
354  C  CB  . ASP A 67  ? 0.5397 0.5776 0.1536 -0.0609 -0.0947 -0.0124 53  ASP A CB  
355  C  CG  . ASP A 67  ? 0.6281 0.4296 0.4682 -0.0857 0.0212  -0.1166 53  ASP A CG  
356  O  OD1 . ASP A 67  ? 0.9042 0.7322 0.3687 0.0492  -0.0470 0.0827  53  ASP A OD1 
357  O  OD2 . ASP A 67  ? 0.8780 0.8480 0.5212 -0.1103 -0.0509 0.0345  53  ASP A OD2 
358  N  N   . ILE A 68  ? 0.2718 0.3464 0.2748 -0.0545 -0.0274 -0.0128 54  ILE A N   
359  C  CA  . ILE A 68  ? 0.2103 0.2944 0.1960 -0.0249 -0.0649 -0.0204 54  ILE A CA  
360  C  C   . ILE A 68  ? 0.1962 0.2429 0.2421 -0.0095 -0.0273 -0.0160 54  ILE A C   
361  O  O   . ILE A 68  ? 0.2380 0.2974 0.1996 -0.0335 -0.0746 -0.0102 54  ILE A O   
362  C  CB  . ILE A 68  ? 0.2303 0.3087 0.1928 -0.0098 -0.0664 -0.0029 54  ILE A CB  
363  C  CG1 . ILE A 68  ? 0.2258 0.3225 0.1988 -0.0066 -0.0190 -0.0183 54  ILE A CG1 
364  C  CG2 . ILE A 68  ? 0.2341 0.3324 0.2168 -0.0236 -0.0411 0.0035  54  ILE A CG2 
365  C  CD1 . ILE A 68  ? 0.2120 0.2946 0.2366 -0.0207 0.0036  0.0034  54  ILE A CD1 
366  N  N   . VAL A 69  ? 0.2147 0.2084 0.2110 -0.0505 -0.0449 -0.0061 55  VAL A N   
367  C  CA  . VAL A 69  ? 0.1540 0.2330 0.2186 -0.0465 -0.0426 0.0081  55  VAL A CA  
368  C  C   . VAL A 69  ? 0.1432 0.2020 0.1765 -0.0206 -0.0102 0.0118  55  VAL A C   
369  O  O   . VAL A 69  ? 0.1729 0.1890 0.1952 -0.0147 -0.0231 -0.0125 55  VAL A O   
370  C  CB  . VAL A 69  ? 0.1622 0.2562 0.2257 -0.0372 -0.0643 0.0151  55  VAL A CB  
371  C  CG1 . VAL A 69  ? 0.1570 0.2247 0.2168 -0.0248 -0.0301 0.0264  55  VAL A CG1 
372  C  CG2 . VAL A 69  ? 0.2441 0.3046 0.2623 -0.0535 -0.0509 -0.0320 55  VAL A CG2 
373  N  N   . ILE A 70  ? 0.1431 0.1859 0.1602 -0.0086 -0.0154 -0.0049 56  ILE A N   
374  C  CA  . ILE A 70  ? 0.1226 0.1585 0.1824 -0.0131 -0.0177 0.0119  56  ILE A CA  
375  C  C   . ILE A 70  ? 0.1393 0.1400 0.1482 -0.0129 -0.0153 0.0129  56  ILE A C   
376  O  O   . ILE A 70  ? 0.1192 0.1794 0.1880 -0.0064 -0.0185 0.0132  56  ILE A O   
377  C  CB  . ILE A 70  ? 0.1560 0.1914 0.1821 -0.0260 -0.0054 0.0000  56  ILE A CB  
378  C  CG1 . ILE A 70  ? 0.2118 0.2156 0.1919 -0.0235 -0.0096 0.0151  56  ILE A CG1 
379  C  CG2 . ILE A 70  ? 0.1813 0.2185 0.1708 -0.0171 -0.0382 0.0024  56  ILE A CG2 
380  C  CD1 . ILE A 70  ? 0.2656 0.2405 0.2131 -0.0405 -0.0083 0.0453  56  ILE A CD1 
381  N  N   . PRO A 71  ? 0.1211 0.1239 0.1506 -0.0074 -0.0099 0.0093  57  PRO A N   
382  C  CA  . PRO A 71  ? 0.1248 0.1333 0.1584 -0.0048 -0.0172 0.0089  57  PRO A CA  
383  C  C   . PRO A 71  ? 0.1237 0.1416 0.1636 -0.0176 -0.0200 0.0218  57  PRO A C   
384  O  O   . PRO A 71  ? 0.1620 0.1617 0.1810 -0.0053 -0.0044 0.0276  57  PRO A O   
385  C  CB  . PRO A 71  ? 0.1487 0.1423 0.1597 -0.0021 -0.0111 -0.0025 57  PRO A CB  
386  C  CG  . PRO A 71  ? 0.1455 0.1547 0.1620 0.0160  -0.0342 0.0013  57  PRO A CG  
387  C  CD  . PRO A 71  ? 0.1094 0.1806 0.1458 0.0223  -0.0113 -0.0033 57  PRO A CD  
388  N  N   . ASP A 72  ? 0.1314 0.1128 0.1578 0.0014  -0.0161 0.0176  58  ASP A N   
389  C  CA  . ASP A 72  ? 0.1364 0.1324 0.1603 0.0181  -0.0185 0.0322  58  ASP A CA  
390  C  C   . ASP A 72  ? 0.1180 0.1346 0.1543 0.0119  -0.0079 0.0101  58  ASP A C   
391  O  O   . ASP A 72  ? 0.1535 0.1270 0.1575 -0.0053 -0.0198 0.0198  58  ASP A O   
392  C  CB  . ASP A 72  ? 0.1567 0.1389 0.1829 0.0161  -0.0268 0.0267  58  ASP A CB  
393  C  CG  . ASP A 72  ? 0.1198 0.1584 0.2270 0.0126  -0.0214 0.0375  58  ASP A CG  
394  O  OD1 . ASP A 72  ? 0.1445 0.1628 0.2397 0.0053  -0.0404 0.0127  58  ASP A OD1 
395  O  OD2 . ASP A 72  ? 0.1677 0.1516 0.3013 0.0233  0.0040  0.0249  58  ASP A OD2 
396  N  N   . ILE A 73  ? 0.1052 0.1301 0.1803 0.0109  -0.0179 0.0133  59  ILE A N   
397  C  CA  . ILE A 73  ? 0.1228 0.1206 0.1810 0.0147  -0.0135 0.0299  59  ILE A CA  
398  C  C   . ILE A 73  ? 0.1207 0.1149 0.1644 0.0204  -0.0310 0.0122  59  ILE A C   
399  O  O   . ILE A 73  ? 0.1137 0.1147 0.1939 0.0120  -0.0195 0.0096  59  ILE A O   
400  C  CB  . ILE A 73  ? 0.1130 0.1194 0.1978 0.0124  -0.0070 0.0158  59  ILE A CB  
401  C  CG1 . ILE A 73  ? 0.1377 0.1483 0.2091 0.0137  0.0158  0.0341  59  ILE A CG1 
402  C  CG2 . ILE A 73  ? 0.1172 0.1326 0.2523 0.0076  -0.0109 0.0070  59  ILE A CG2 
403  C  CD1 . ILE A 73  ? 0.2018 0.1541 0.2575 0.0312  0.0265  0.0303  59  ILE A CD1 
404  N  N   . GLN A 74  ? 0.1211 0.1194 0.1761 0.0075  -0.0090 0.0240  60  GLN A N   
405  C  CA  . GLN A 74  ? 0.1337 0.1019 0.1892 0.0125  -0.0081 0.0118  60  GLN A CA  
406  C  C   . GLN A 74  ? 0.1113 0.1306 0.1873 0.0232  -0.0233 0.0090  60  GLN A C   
407  O  O   . GLN A 74  ? 0.1277 0.1176 0.2090 0.0151  -0.0212 0.0141  60  GLN A O   
408  C  CB  . GLN A 74  ? 0.1283 0.1456 0.1819 0.0103  -0.0254 0.0328  60  GLN A CB  
409  C  CG  . GLN A 74  ? 0.1011 0.1597 0.1886 0.0292  -0.0006 0.0305  60  GLN A CG  
410  C  CD  . GLN A 74  ? 0.1217 0.1373 0.1568 0.0261  -0.0150 -0.0008 60  GLN A CD  
411  O  OE1 . GLN A 74  ? 0.1195 0.1312 0.1812 0.0394  -0.0301 0.0178  60  GLN A OE1 
412  N  NE2 . GLN A 74  ? 0.1650 0.1616 0.1825 0.0399  -0.0122 -0.0157 60  GLN A NE2 
413  N  N   . TYR A 75  ? 0.1244 0.1276 0.1794 0.0153  -0.0298 0.0253  61  TYR A N   
414  C  CA  . TYR A 75  ? 0.1171 0.1260 0.2060 0.0232  0.0007  0.0335  61  TYR A CA  
415  C  C   . TYR A 75  ? 0.1450 0.1343 0.2056 0.0117  -0.0025 0.0360  61  TYR A C   
416  O  O   . TYR A 75  ? 0.1299 0.1523 0.2069 0.0102  -0.0173 0.0090  61  TYR A O   
417  C  CB  . TYR A 75  ? 0.1426 0.1293 0.2062 0.0140  -0.0343 0.0342  61  TYR A CB  
418  C  CG  . TYR A 75  ? 0.1335 0.1520 0.1651 0.0053  -0.0200 0.0252  61  TYR A CG  
419  C  CD1 . TYR A 75  ? 0.1759 0.1840 0.2302 0.0005  -0.0235 0.0280  61  TYR A CD1 
420  C  CD2 . TYR A 75  ? 0.1400 0.1477 0.1706 0.0238  -0.0096 0.0047  61  TYR A CD2 
421  C  CE1 . TYR A 75  ? 0.1542 0.1717 0.2018 0.0095  0.0058  0.0089  61  TYR A CE1 
422  C  CE2 . TYR A 75  ? 0.1744 0.1519 0.1732 0.0215  -0.0200 0.0167  61  TYR A CE2 
423  C  CZ  . TYR A 75  ? 0.1447 0.1728 0.1908 0.0007  -0.0124 0.0044  61  TYR A CZ  
424  O  OH  . TYR A 75  ? 0.1828 0.2006 0.2025 0.0072  -0.0231 -0.0005 61  TYR A OH  
425  N  N   . VAL A 76  ? 0.1235 0.1127 0.1709 0.0058  -0.0135 0.0227  62  VAL A N   
426  C  CA  . VAL A 76  ? 0.1199 0.1177 0.1987 0.0103  -0.0394 -0.0016 62  VAL A CA  
427  C  C   . VAL A 76  ? 0.1484 0.1093 0.2320 0.0175  -0.0196 0.0006  62  VAL A C   
428  O  O   . VAL A 76  ? 0.1366 0.1309 0.2222 0.0090  -0.0198 0.0121  62  VAL A O   
429  C  CB  . VAL A 76  ? 0.1220 0.1083 0.2151 0.0032  -0.0133 0.0126  62  VAL A CB  
430  C  CG1 . VAL A 76  ? 0.1453 0.1435 0.1833 0.0083  0.0026  -0.0077 62  VAL A CG1 
431  C  CG2 . VAL A 76  ? 0.1525 0.1432 0.2210 0.0308  0.0170  0.0361  62  VAL A CG2 
432  N  N   . ILE A 77  ? 0.1352 0.1149 0.1893 0.0167  -0.0170 0.0184  63  ILE A N   
433  C  CA  . ILE A 77  ? 0.1229 0.1339 0.2074 0.0036  -0.0068 0.0219  63  ILE A CA  
434  C  C   . ILE A 77  ? 0.1354 0.1359 0.1999 0.0221  -0.0297 0.0225  63  ILE A C   
435  O  O   . ILE A 77  ? 0.1738 0.1148 0.2401 0.0122  -0.0077 0.0334  63  ILE A O   
436  C  CB  . ILE A 77  ? 0.1307 0.1356 0.2125 0.0068  -0.0100 0.0342  63  ILE A CB  
437  C  CG1 . ILE A 77  ? 0.1522 0.1675 0.2300 0.0278  -0.0133 0.0528  63  ILE A CG1 
438  C  CG2 . ILE A 77  ? 0.1652 0.1645 0.2507 0.0381  -0.0004 0.0305  63  ILE A CG2 
439  C  CD1 . ILE A 77  ? 0.2531 0.2297 0.2897 -0.0120 0.0104  0.0497  63  ILE A CD1 
440  N  N   . GLU A 78  ? 0.1801 0.1222 0.2005 0.0359  -0.0163 0.0212  64  GLU A N   
441  C  CA  . GLU A 78  ? 0.1709 0.1270 0.2187 0.0433  -0.0174 0.0094  64  GLU A CA  
442  C  C   . GLU A 78  ? 0.1922 0.1606 0.2194 0.0142  -0.0185 -0.0062 64  GLU A C   
443  O  O   . GLU A 78  ? 0.1911 0.1642 0.2561 0.0431  -0.0136 -0.0279 64  GLU A O   
444  C  CB  . GLU A 78  ? 0.1812 0.1615 0.2263 0.0083  0.0085  -0.0136 64  GLU A CB  
445  C  CG  . GLU A 78  ? 0.1889 0.1823 0.2397 0.0191  0.0000  0.0164  64  GLU A CG  
446  C  CD  . GLU A 78  ? 0.2473 0.2849 0.2697 -0.0105 -0.0340 0.0547  64  GLU A CD  
447  O  OE1 . GLU A 78  ? 0.3000 0.5444 0.3134 -0.0806 -0.0769 0.0901  64  GLU A OE1 
448  O  OE2 . GLU A 78  ? 0.1796 0.2623 0.2327 0.0106  -0.0015 0.0176  64  GLU A OE2 
449  N  N   . ASN A 79  ? 0.1671 0.1189 0.2380 0.0199  -0.0328 0.0106  65  ASN A N   
450  C  CA  . ASN A 79  ? 0.2056 0.1364 0.1947 0.0119  -0.0198 -0.0149 65  ASN A CA  
451  C  C   . ASN A 79  ? 0.1829 0.1144 0.2074 -0.0076 -0.0183 -0.0098 65  ASN A C   
452  O  O   . ASN A 79  ? 0.1780 0.1457 0.2494 -0.0050 -0.0287 0.0045  65  ASN A O   
453  C  CB  . ASN A 79  ? 0.1979 0.1429 0.2138 0.0228  -0.0123 -0.0059 65  ASN A CB  
454  C  CG  . ASN A 79  ? 0.2123 0.1978 0.2025 0.0227  -0.0085 -0.0166 65  ASN A CG  
455  O  OD1 . ASN A 79  ? 0.2063 0.2272 0.2568 -0.0083 -0.0201 -0.0468 65  ASN A OD1 
456  N  ND2 . ASN A 79  ? 0.1850 0.1831 0.2474 -0.0077 -0.0117 0.0224  65  ASN A ND2 
457  N  N   . LYS A 80  ? 0.1719 0.1358 0.2110 0.0089  -0.0002 0.0142  66  LYS A N   
458  C  CA  . LYS A 80  ? 0.1807 0.1378 0.2526 -0.0276 -0.0029 0.0239  66  LYS A CA  
459  C  C   . LYS A 80  ? 0.1663 0.1503 0.2564 -0.0042 -0.0076 0.0127  66  LYS A C   
460  O  O   . LYS A 80  ? 0.1738 0.1614 0.2853 -0.0038 -0.0042 0.0191  66  LYS A O   
461  C  CB  . LYS A 80  ? 0.1905 0.1914 0.2534 -0.0377 0.0287  0.0106  66  LYS A CB  
462  C  CG  . LYS A 80  ? 0.2005 0.1835 0.2823 -0.0090 0.0051  0.0141  66  LYS A CG  
463  C  CD  . LYS A 80  ? 0.2868 0.2346 0.3439 -0.0428 -0.0251 0.0367  66  LYS A CD  
464  C  CE  . LYS A 80  ? 0.3652 0.3456 0.3577 -0.0064 -0.1204 0.0225  66  LYS A CE  
465  N  NZ  . LYS A 80  ? 0.4085 0.3687 0.3336 -0.0461 -0.0327 0.0571  66  LYS A NZ  
466  N  N   . GLU A 81  ? 0.1648 0.1471 0.2852 -0.0143 -0.0260 -0.0026 67  GLU A N   
467  C  CA  . GLU A 81  ? 0.2035 0.1591 0.3047 -0.0322 -0.0165 0.0342  67  GLU A CA  
468  C  C   . GLU A 81  ? 0.1721 0.1991 0.3049 -0.0222 -0.0358 0.0335  67  GLU A C   
469  O  O   . GLU A 81  ? 0.2220 0.2170 0.3378 -0.0056 -0.0613 0.0248  67  GLU A O   
470  C  CB  . GLU A 81  ? 0.3130 0.1131 0.4306 -0.0339 -0.0606 0.0017  67  GLU A CB  
471  C  CG  . GLU A 81  ? 0.3918 0.1973 0.4097 0.0520  -0.0448 -0.0098 67  GLU A CG  
472  C  CD  . GLU A 81  ? 0.4036 0.4663 0.4094 0.0145  -0.0373 -0.0539 67  GLU A CD  
473  O  OE1 . GLU A 81  ? 0.3145 0.2171 0.4020 0.0684  -0.0240 -0.0448 67  GLU A OE1 
474  O  OE2 . GLU A 81  ? 0.5254 0.4597 0.4482 -0.0404 0.1010  -0.0809 67  GLU A OE2 
475  N  N   . ARG A 82  ? 0.1724 0.1446 0.2401 0.0033  -0.0315 -0.0032 68  ARG A N   
476  C  CA  . ARG A 82  ? 0.1792 0.1800 0.2258 0.0000  -0.0351 -0.0162 68  ARG A CA  
477  C  C   . ARG A 82  ? 0.1702 0.1505 0.2058 -0.0243 0.0106  0.0119  68  ARG A C   
478  O  O   . ARG A 82  ? 0.1701 0.1426 0.2409 -0.0095 -0.0162 0.0037  68  ARG A O   
479  C  CB  . ARG A 82  ? 0.2222 0.1484 0.2286 0.0182  -0.0346 -0.0099 68  ARG A CB  
480  C  CG  . ARG A 82  ? 0.2336 0.1609 0.2675 0.0157  -0.0020 -0.0369 68  ARG A CG  
481  C  CD  . ARG A 82  ? 0.2213 0.2018 0.2822 0.0089  0.0117  -0.0452 68  ARG A CD  
482  N  NE  . ARG A 82  ? 0.2158 0.2210 0.2560 0.0103  -0.0194 -0.0345 68  ARG A NE  
483  C  CZ  . ARG A 82  ? 0.2244 0.1712 0.2544 0.0096  -0.0207 -0.0286 68  ARG A CZ  
484  N  NH1 . ARG A 82  ? 0.2394 0.2180 0.2871 0.0288  -0.0250 -0.0362 68  ARG A NH1 
485  N  NH2 . ARG A 82  ? 0.2239 0.2146 0.2526 0.0192  0.0170  -0.0525 68  ARG A NH2 
486  N  N   . LEU A 83  ? 0.1770 0.1381 0.2132 0.0202  -0.0041 0.0038  69  LEU A N   
487  C  CA  . LEU A 83  ? 0.1689 0.1267 0.2202 0.0182  0.0010  -0.0027 69  LEU A CA  
488  C  C   . LEU A 83  ? 0.1827 0.1699 0.2389 -0.0230 -0.0043 0.0202  69  LEU A C   
489  O  O   . LEU A 83  ? 0.2167 0.1923 0.2874 -0.0254 -0.0042 0.0406  69  LEU A O   
490  C  CB  . LEU A 83  ? 0.1797 0.1552 0.1988 0.0016  0.0117  0.0184  69  LEU A CB  
491  C  CG  . LEU A 83  ? 0.1607 0.1811 0.2028 0.0032  0.0223  0.0089  69  LEU A CG  
492  C  CD1 . LEU A 83  ? 0.1798 0.1678 0.2242 0.0070  -0.0198 0.0112  69  LEU A CD1 
493  C  CD2 . LEU A 83  ? 0.1736 0.1829 0.2230 0.0047  0.0051  0.0171  69  LEU A CD2 
494  N  N   . LYS A 84  ? 0.1501 0.1469 0.2129 -0.0099 -0.0033 0.0213  70  LYS A N   
495  C  CA  . LYS A 84  ? 0.1450 0.1832 0.2200 -0.0241 0.0025  0.0127  70  LYS A CA  
496  C  C   . LYS A 84  ? 0.1546 0.1444 0.2845 -0.0020 0.0208  -0.0151 70  LYS A C   
497  O  O   . LYS A 84  ? 0.1940 0.1862 0.2819 -0.0281 0.0335  0.0167  70  LYS A O   
498  C  CB  . LYS A 84  ? 0.1651 0.3271 0.3231 -0.0326 -0.0083 0.0038  70  LYS A CB  
499  C  CG  . LYS A 84  ? 0.2087 0.4112 0.3236 -0.0452 0.0090  -0.0405 70  LYS A CG  
500  C  CD  . LYS A 84  ? 0.4154 0.3193 0.3839 -0.0307 0.0040  -0.0308 70  LYS A CD  
501  C  CE  . LYS A 84  ? 0.5582 0.3113 0.6583 0.0667  -0.0412 0.0985  70  LYS A CE  
502  N  NZ  . LYS A 84  ? 0.5740 0.5483 0.5584 -0.0956 0.0082  0.1683  70  LYS A NZ  
503  N  N   . GLY A 85  ? 0.1737 0.1222 0.2498 0.0017  0.0211  -0.0020 71  GLY A N   
504  C  CA  . GLY A 85  ? 0.1985 0.1189 0.2967 -0.0327 0.0608  0.0263  71  GLY A CA  
505  C  C   . GLY A 85  ? 0.1758 0.0930 0.2082 -0.0204 0.0416  0.0241  71  GLY A C   
506  O  O   . GLY A 85  ? 0.1549 0.1136 0.2143 0.0101  0.0462  0.0264  71  GLY A O   
507  N  N   . ILE A 86  ? 0.1758 0.1227 0.2195 -0.0281 0.0435  0.0225  72  ILE A N   
508  C  CA  . ILE A 86  ? 0.1422 0.1087 0.1970 0.0050  0.0416  0.0070  72  ILE A CA  
509  C  C   . ILE A 86  ? 0.1453 0.1130 0.1919 0.0175  0.0437  0.0132  72  ILE A C   
510  O  O   . ILE A 86  ? 0.1510 0.1555 0.2284 -0.0048 0.0722  0.0384  72  ILE A O   
511  C  CB  . ILE A 86  ? 0.1310 0.1976 0.2296 -0.0045 0.0554  0.0217  72  ILE A CB  
512  C  CG1 . ILE A 86  ? 0.1524 0.1965 0.2692 0.0196  0.0402  0.0680  72  ILE A CG1 
513  C  CG2 . ILE A 86  ? 0.1476 0.1892 0.1910 0.0455  0.0088  0.0089  72  ILE A CG2 
514  C  CD1 . ILE A 86  ? 0.1725 0.3662 0.3719 0.0622  0.0692  0.0938  72  ILE A CD1 
515  N  N   . PHE A 87  ? 0.1291 0.0938 0.1717 -0.0053 0.0346  0.0285  73  PHE A N   
516  C  CA  . PHE A 87  ? 0.1213 0.1161 0.1469 0.0005  0.0202  -0.0058 73  PHE A CA  
517  C  C   . PHE A 87  ? 0.0975 0.1058 0.1430 -0.0106 0.0030  0.0149  73  PHE A C   
518  O  O   . PHE A 87  ? 0.1045 0.1301 0.1664 -0.0049 0.0204  0.0131  73  PHE A O   
519  C  CB  . PHE A 87  ? 0.1387 0.1329 0.1830 -0.0100 0.0170  -0.0072 73  PHE A CB  
520  C  CG  . PHE A 87  ? 0.1506 0.1644 0.2131 -0.0199 0.0122  -0.0144 73  PHE A CG  
521  C  CD1 . PHE A 87  ? 0.2094 0.1614 0.2276 -0.0099 0.0352  -0.0391 73  PHE A CD1 
522  C  CD2 . PHE A 87  ? 0.1411 0.1614 0.2313 -0.0322 0.0103  0.0011  73  PHE A CD2 
523  C  CE1 . PHE A 87  ? 0.1839 0.2422 0.2558 -0.0256 0.0153  -0.0673 73  PHE A CE1 
524  C  CE2 . PHE A 87  ? 0.1546 0.2121 0.2405 -0.0365 -0.0055 -0.0049 73  PHE A CE2 
525  C  CZ  . PHE A 87  ? 0.1951 0.2124 0.2821 -0.0514 0.0130  -0.0776 73  PHE A CZ  
526  N  N   . LEU A 88  ? 0.1111 0.1019 0.1338 -0.0259 0.0141  0.0036  74  LEU A N   
527  C  CA  . LEU A 88  ? 0.1150 0.1334 0.1352 -0.0033 0.0053  -0.0119 74  LEU A CA  
528  C  C   . LEU A 88  ? 0.1126 0.1166 0.1538 -0.0051 0.0202  0.0083  74  LEU A C   
529  O  O   . LEU A 88  ? 0.1152 0.1369 0.1878 -0.0136 0.0062  0.0005  74  LEU A O   
530  C  CB  . LEU A 88  ? 0.1140 0.1131 0.1457 -0.0253 0.0044  -0.0142 74  LEU A CB  
531  C  CG  . LEU A 88  ? 0.1245 0.1254 0.1438 -0.0106 0.0048  -0.0118 74  LEU A CG  
532  C  CD1 . LEU A 88  ? 0.1253 0.1680 0.1565 0.0181  -0.0140 0.0236  74  LEU A CD1 
533  C  CD2 . LEU A 88  ? 0.1427 0.1454 0.1618 -0.0190 -0.0062 0.0321  74  LEU A CD2 
534  N  N   . THR A 89  ? 0.1027 0.1033 0.1571 0.0039  0.0115  0.0150  75  THR A N   
535  C  CA  . THR A 89  ? 0.1090 0.1163 0.1520 0.0019  0.0143  0.0025  75  THR A CA  
536  C  C   . THR A 89  ? 0.1119 0.0989 0.1415 -0.0148 0.0195  0.0151  75  THR A C   
537  O  O   . THR A 89  ? 0.1221 0.1449 0.1487 0.0201  0.0000  0.0064  75  THR A O   
538  C  CB  . THR A 89  ? 0.1172 0.1291 0.1268 0.0092  -0.0012 0.0292  75  THR A CB  
539  O  OG1 . THR A 89  ? 0.1219 0.1193 0.1509 -0.0018 0.0017  -0.0024 75  THR A OG1 
540  C  CG2 . THR A 89  ? 0.1038 0.1695 0.1480 0.0234  0.0024  0.0246  75  THR A CG2 
541  N  N   . HIS A 90  ? 0.1221 0.1029 0.1365 0.0203  -0.0061 0.0123  76  HIS A N   
542  C  CA  . HIS A 90  ? 0.1359 0.1181 0.1371 -0.0156 -0.0102 0.0156  76  HIS A CA  
543  C  C   . HIS A 90  ? 0.1301 0.1478 0.1165 -0.0051 0.0223  -0.0048 76  HIS A C   
544  O  O   . HIS A 90  ? 0.1528 0.2115 0.1596 0.0410  0.0073  0.0002  76  HIS A O   
545  C  CB  . HIS A 90  ? 0.2038 0.1225 0.1868 0.0304  0.0037  -0.0066 76  HIS A CB  
546  C  CG  . HIS A 90  ? 0.2019 0.1389 0.1642 -0.0456 0.0099  0.0107  76  HIS A CG  
547  N  ND1 . HIS A 90  ? 0.1906 0.2814 0.3532 -0.0187 0.0352  0.0404  76  HIS A ND1 
548  C  CD2 . HIS A 90  ? 0.2683 0.2000 0.1082 0.0961  0.0421  0.0575  76  HIS A CD2 
549  C  CE1 . HIS A 90  ? 0.3138 0.3104 0.2462 0.0329  0.0105  -0.0113 76  HIS A CE1 
550  N  NE2 . HIS A 90  ? 0.2046 0.2719 0.3140 -0.0811 0.0037  0.1383  76  HIS A NE2 
551  N  N   . GLY A 91  ? 0.1521 0.1546 0.1126 -0.0010 0.0106  -0.0081 77  GLY A N   
552  C  CA  . GLY A 91  ? 0.1817 0.1958 0.1535 0.0276  0.0197  -0.0053 77  GLY A CA  
553  C  C   . GLY A 91  ? 0.2653 0.2474 0.1918 0.0671  0.0158  0.0048  77  GLY A C   
554  O  O   . GLY A 91  ? 0.2497 0.3865 0.1800 -0.0053 0.0023  -0.0151 77  GLY A O   
555  N  N   . ALA A 92  ? 0.1779 0.2169 0.1799 -0.0070 0.0022  -0.0713 78  ALA A N   
556  C  CA  . ALA A 92  ? 0.1738 0.2008 0.1794 0.0120  -0.0335 -0.0565 78  ALA A CA  
557  C  C   . ALA A 92  ? 0.1497 0.1682 0.1766 0.0117  0.0040  -0.0192 78  ALA A C   
558  O  O   . ALA A 92  ? 0.1763 0.1386 0.1432 0.0096  0.0155  -0.0110 78  ALA A O   
559  C  CB  . ALA A 92  ? 0.1553 0.1998 0.3493 -0.0141 -0.0449 -0.0135 78  ALA A CB  
560  N  N   . GLU A 93  ? 0.1828 0.2015 0.1698 0.0209  -0.0024 -0.0399 79  GLU A N   
561  C  CA  . GLU A 93  ? 0.1687 0.2449 0.1769 0.0099  -0.0088 -0.0046 79  GLU A CA  
562  C  C   . GLU A 93  ? 0.1634 0.1586 0.1645 0.0045  0.0273  0.0054  79  GLU A C   
563  O  O   . GLU A 93  ? 0.1546 0.1333 0.1982 -0.0017 0.0108  0.0024  79  GLU A O   
564  C  CB  . GLU A 93  ? 0.2015 0.4099 0.2539 0.0367  -0.0271 -0.0568 79  GLU A CB  
565  C  CG  . GLU A 93  ? 0.3302 0.4820 0.2504 0.1166  -0.0682 -0.0267 79  GLU A CG  
566  C  CD  . GLU A 93  ? 0.5864 0.7070 0.3866 -0.0381 -0.0496 -0.0161 79  GLU A CD  
567  O  OE1 . GLU A 93  ? 0.6325 0.5087 0.5278 -0.0188 -0.0156 -0.0120 79  GLU A OE1 
568  O  OE2 . GLU A 93  ? 0.6409 1.0863 0.5504 -0.0566 -0.0882 0.0611  79  GLU A OE2 
569  N  N   . HIS A 94  ? 0.1816 0.1397 0.1776 0.0325  0.0294  -0.0013 80  HIS A N   
570  C  CA  . HIS A 94  ? 0.1727 0.1538 0.1912 0.0136  0.0451  0.0503  80  HIS A CA  
571  C  C   . HIS A 94  ? 0.1800 0.1469 0.1582 0.0301  0.0138  0.0236  80  HIS A C   
572  O  O   . HIS A 94  ? 0.1751 0.1805 0.1539 0.0319  0.0264  0.0071  80  HIS A O   
573  C  CB  . HIS A 94  ? 0.3053 0.2116 0.2198 0.0033  0.0689  0.0404  80  HIS A CB  
574  C  CG  . HIS A 94  ? 0.1715 0.2727 0.2074 -0.0342 0.0162  -0.0135 80  HIS A CG  
575  N  ND1 . HIS A 94  ? 0.2363 0.2425 0.2187 -0.0566 -0.0122 -0.0312 80  HIS A ND1 
576  C  CD2 . HIS A 94  ? 0.1933 0.1869 0.2286 0.0039  -0.0430 0.0706  80  HIS A CD2 
577  C  CE1 . HIS A 94  ? 0.2689 0.1693 0.2272 -0.0607 0.0388  0.0079  80  HIS A CE1 
578  N  NE2 . HIS A 94  ? 0.2508 0.2222 0.3577 -0.0388 0.0253  -0.0632 80  HIS A NE2 
579  N  N   . ALA A 95  ? 0.1472 0.1444 0.1490 0.0252  0.0170  0.0064  81  ALA A N   
580  C  CA  . ALA A 95  ? 0.1329 0.1767 0.1458 0.0101  0.0139  0.0087  81  ALA A CA  
581  C  C   . ALA A 95  ? 0.1089 0.1314 0.1344 0.0097  0.0070  0.0013  81  ALA A C   
582  O  O   . ALA A 95  ? 0.1446 0.1463 0.1486 -0.0038 0.0166  -0.0090 81  ALA A O   
583  C  CB  . ALA A 95  ? 0.1899 0.2090 0.1464 0.0610  -0.0008 -0.0265 81  ALA A CB  
584  N  N   . ILE A 96  ? 0.1378 0.1403 0.1239 0.0149  0.0107  -0.0108 82  ILE A N   
585  C  CA  . ILE A 96  ? 0.1361 0.1315 0.1435 -0.0103 -0.0005 -0.0077 82  ILE A CA  
586  C  C   . ILE A 96  ? 0.1354 0.1432 0.1326 0.0056  -0.0001 0.0045  82  ILE A C   
587  O  O   . ILE A 96  ? 0.1530 0.1513 0.1461 0.0032  0.0148  0.0150  82  ILE A O   
588  C  CB  . ILE A 96  ? 0.1465 0.1585 0.1583 -0.0122 0.0061  0.0115  82  ILE A CB  
589  C  CG1 . ILE A 96  ? 0.1648 0.1834 0.1576 -0.0224 0.0424  -0.0176 82  ILE A CG1 
590  C  CG2 . ILE A 96  ? 0.1721 0.1394 0.2450 -0.0070 -0.0202 0.0095  82  ILE A CG2 
591  C  CD1 . ILE A 96  ? 0.2143 0.1662 0.2491 0.0025  0.0687  -0.0142 82  ILE A CD1 
592  N  N   . GLY A 97  ? 0.1582 0.1418 0.1287 -0.0017 -0.0004 0.0180  83  GLY A N   
593  C  CA  . GLY A 97  ? 0.1816 0.1838 0.1380 -0.0123 -0.0130 -0.0009 83  GLY A CA  
594  C  C   . GLY A 97  ? 0.1394 0.1724 0.1565 -0.0089 -0.0209 0.0210  83  GLY A C   
595  O  O   . GLY A 97  ? 0.2109 0.2301 0.1437 0.0247  -0.0359 0.0175  83  GLY A O   
596  N  N   . ALA A 98  ? 0.1358 0.1379 0.1730 0.0026  0.0017  0.0302  84  ALA A N   
597  C  CA  . ALA A 98  ? 0.1734 0.1378 0.1429 0.0142  0.0031  0.0063  84  ALA A CA  
598  C  C   . ALA A 98  ? 0.1750 0.1539 0.1185 0.0016  0.0159  0.0151  84  ALA A C   
599  O  O   . ALA A 98  ? 0.1480 0.1460 0.2045 0.0106  -0.0020 0.0201  84  ALA A O   
600  C  CB  . ALA A 98  ? 0.1383 0.1594 0.1746 0.0078  -0.0017 0.0185  84  ALA A CB  
601  N  N   . VAL A 99  ? 0.1616 0.1401 0.1586 0.0028  -0.0130 0.0160  85  VAL A N   
602  C  CA  . VAL A 99  ? 0.1434 0.1508 0.1781 -0.0022 0.0031  0.0260  85  VAL A CA  
603  C  C   . VAL A 99  ? 0.1192 0.1443 0.1721 0.0100  -0.0015 0.0123  85  VAL A C   
604  O  O   . VAL A 99  ? 0.1347 0.1585 0.1954 -0.0028 -0.0019 0.0080  85  VAL A O   
605  C  CB  . VAL A 99  ? 0.1645 0.1602 0.2240 -0.0263 -0.0208 0.0305  85  VAL A CB  
606  C  CG1 . VAL A 99  ? 0.1718 0.1867 0.2263 0.0121  0.0270  0.0126  85  VAL A CG1 
607  C  CG2 . VAL A 99  ? 0.1711 0.1903 0.1983 -0.0180 -0.0147 0.0089  85  VAL A CG2 
608  N  N   . SER A 100 ? 0.1675 0.1739 0.1816 -0.0185 0.0063  0.0276  86  SER A N   
609  C  CA  . SER A 100 ? 0.1596 0.1938 0.1898 -0.0356 -0.0047 0.0584  86  SER A CA  
610  C  C   . SER A 100 ? 0.1874 0.1844 0.2127 -0.0022 -0.0035 0.0559  86  SER A C   
611  O  O   . SER A 100 ? 0.2278 0.1775 0.2684 0.0040  -0.0031 0.0717  86  SER A O   
612  C  CB  . SER A 100 ? 0.2222 0.2315 0.1903 -0.0589 0.0062  0.0378  86  SER A CB  
613  O  OG  . SER A 100 ? 0.2167 0.2500 0.2190 -0.0497 -0.0288 0.0272  86  SER A OG  
614  N  N   . TYR A 101 ? 0.1731 0.1660 0.1971 -0.0184 -0.0059 0.0556  87  TYR A N   
615  C  CA  . TYR A 101 ? 0.1615 0.1586 0.2183 -0.0179 -0.0226 0.0433  87  TYR A CA  
616  C  C   . TYR A 101 ? 0.1522 0.1549 0.2127 -0.0291 -0.0132 -0.0080 87  TYR A C   
617  O  O   . TYR A 101 ? 0.2109 0.1546 0.2526 0.0356  -0.0130 0.0182  87  TYR A O   
618  C  CB  . TYR A 101 ? 0.1736 0.1876 0.2129 -0.0122 0.0094  0.0456  87  TYR A CB  
619  C  CG  . TYR A 101 ? 0.1471 0.1988 0.1858 -0.0259 -0.0106 0.0080  87  TYR A CG  
620  C  CD1 . TYR A 101 ? 0.1758 0.2554 0.2144 -0.0132 -0.0029 0.0115  87  TYR A CD1 
621  C  CD2 . TYR A 101 ? 0.1756 0.1889 0.1968 -0.0299 -0.0468 0.0143  87  TYR A CD2 
622  C  CE1 . TYR A 101 ? 0.2501 0.2287 0.2075 0.0315  -0.0259 0.0128  87  TYR A CE1 
623  C  CE2 . TYR A 101 ? 0.2072 0.2106 0.2204 -0.0192 -0.0330 0.0083  87  TYR A CE2 
624  C  CZ  . TYR A 101 ? 0.2479 0.2348 0.2225 -0.0036 -0.0025 0.0029  87  TYR A CZ  
625  O  OH  . TYR A 101 ? 0.3212 0.2543 0.2412 -0.0552 -0.0364 0.0095  87  TYR A OH  
626  N  N   . VAL A 102 ? 0.1617 0.1514 0.1986 -0.0009 -0.0080 0.0452  88  VAL A N   
627  C  CA  . VAL A 102 ? 0.1367 0.1637 0.2156 0.0146  -0.0073 0.0449  88  VAL A CA  
628  C  C   . VAL A 102 ? 0.1581 0.1580 0.2249 0.0082  -0.0011 0.0111  88  VAL A C   
629  O  O   . VAL A 102 ? 0.1785 0.1624 0.2421 0.0229  0.0134  0.0241  88  VAL A O   
630  C  CB  . VAL A 102 ? 0.1165 0.1601 0.2151 0.0181  0.0158  0.0352  88  VAL A CB  
631  C  CG1 . VAL A 102 ? 0.1608 0.1668 0.1923 -0.0124 0.0158  0.0512  88  VAL A CG1 
632  C  CG2 . VAL A 102 ? 0.1596 0.1790 0.1926 -0.0084 0.0005  0.0321  88  VAL A CG2 
633  N  N   . LEU A 103 ? 0.1667 0.1260 0.1862 0.0055  0.0052  0.0458  89  LEU A N   
634  C  CA  . LEU A 103 ? 0.1921 0.1523 0.2442 -0.0182 -0.0114 0.0247  89  LEU A CA  
635  C  C   . LEU A 103 ? 0.2012 0.1451 0.2718 -0.0205 -0.0306 0.0264  89  LEU A C   
636  O  O   . LEU A 103 ? 0.2440 0.1488 0.3023 -0.0236 -0.0113 0.0593  89  LEU A O   
637  C  CB  . LEU A 103 ? 0.1755 0.1594 0.2279 -0.0572 -0.0087 0.0546  89  LEU A CB  
638  C  CG  . LEU A 103 ? 0.1796 0.1876 0.2601 -0.0169 0.0203  0.0436  89  LEU A CG  
639  C  CD1 . LEU A 103 ? 0.2387 0.1811 0.3325 -0.0493 0.0290  0.0334  89  LEU A CD1 
640  C  CD2 . LEU A 103 ? 0.2180 0.2201 0.2640 0.0201  -0.0155 0.0313  89  LEU A CD2 
641  N  N   . GLU A 104 ? 0.2179 0.1437 0.2491 -0.0309 -0.0393 0.0584  90  GLU A N   
642  C  CA  . GLU A 104 ? 0.2488 0.1884 0.3016 -0.0092 -0.0461 0.0751  90  GLU A CA  
643  C  C   . GLU A 104 ? 0.2260 0.2134 0.2424 0.0010  -0.0342 0.0273  90  GLU A C   
644  O  O   . GLU A 104 ? 0.4066 0.1732 0.3676 0.0599  -0.0690 0.0566  90  GLU A O   
645  C  CB  . GLU A 104 ? 0.2949 0.2022 0.2803 0.0109  -0.0887 0.0800  90  GLU A CB  
646  C  CG  . GLU A 104 ? 0.4266 0.2780 0.4432 0.0033  -0.0636 0.1090  90  GLU A CG  
647  C  CD  . GLU A 104 ? 0.5664 0.4708 0.5469 0.0735  -0.1649 0.0894  90  GLU A CD  
648  O  OE1 . GLU A 104 ? 0.3681 0.4023 0.3672 -0.0222 -0.0833 0.1105  90  GLU A OE1 
649  O  OE2 . GLU A 104 ? 0.6258 0.4738 0.3992 0.0958  -0.0978 0.1626  90  GLU A OE2 
650  N  N   . GLN A 105 ? 0.2205 0.2000 0.2844 -0.0037 -0.0321 0.0335  91  GLN A N   
651  C  CA  . GLN A 105 ? 0.2948 0.1950 0.3266 0.0697  -0.0229 0.0321  91  GLN A CA  
652  C  C   . GLN A 105 ? 0.2062 0.2174 0.3373 0.0724  -0.0311 -0.0178 91  GLN A C   
653  O  O   . GLN A 105 ? 0.2648 0.2282 0.3677 0.0480  -0.0303 -0.0415 91  GLN A O   
654  C  CB  . GLN A 105 ? 0.2043 0.2377 0.2816 0.0301  -0.0313 0.0063  91  GLN A CB  
655  C  CG  . GLN A 105 ? 0.2671 0.3314 0.3453 -0.0143 -0.0446 0.0067  91  GLN A CG  
656  C  CD  . GLN A 105 ? 0.3916 0.5219 0.6195 0.0098  -0.1238 -0.0796 91  GLN A CD  
657  O  OE1 . GLN A 105 ? 1.1124 0.7009 0.8351 -0.5116 0.1328  -0.0111 91  GLN A OE1 
658  N  NE2 . GLN A 105 ? 0.4156 0.3470 0.3869 0.0293  -0.0025 0.0384  91  GLN A NE2 
659  N  N   . ILE A 106 ? 0.2420 0.1809 0.3260 0.0481  -0.0244 -0.0200 92  ILE A N   
660  C  CA  . ILE A 106 ? 0.3028 0.1854 0.3371 0.0349  -0.0652 0.0153  92  ILE A CA  
661  C  C   . ILE A 106 ? 0.2456 0.1718 0.3625 0.0386  -0.0054 0.0260  92  ILE A C   
662  O  O   . ILE A 106 ? 0.2989 0.2847 0.3631 -0.0331 0.0554  -0.0639 92  ILE A O   
663  C  CB  . ILE A 106 ? 0.3345 0.2300 0.3829 0.0160  -0.0652 -0.0151 92  ILE A CB  
664  C  CG1 . ILE A 106 ? 0.4473 0.2877 0.3634 -0.1024 -0.0318 -0.0170 92  ILE A CG1 
665  C  CG2 . ILE A 106 ? 0.5004 0.4526 0.4755 0.0574  -0.0590 0.0382  92  ILE A CG2 
666  C  CD1 . ILE A 106 ? 0.5430 0.4904 0.3437 -0.0650 -0.0343 0.0954  92  ILE A CD1 
667  N  N   . ASP A 107 ? 0.2574 0.2712 0.6479 0.0305  0.0036  -0.0550 93  ASP A N   
668  C  CA  . ASP A 107 ? 0.2283 0.4217 0.5625 0.0041  -0.0450 -0.1311 93  ASP A CA  
669  C  C   . ASP A 107 ? 0.6557 1.3930 0.4965 -0.1260 0.2262  0.4638  93  ASP A C   
670  O  O   . ASP A 107 ? 1.7381 0.3434 0.7310 0.3609  0.3017  0.2713  93  ASP A O   
671  C  CB  . ASP A 107 ? 0.6573 0.2656 0.6544 -0.0257 0.1408  -0.0400 93  ASP A CB  
672  N  N   . ALA A 108 ? 0.3110 0.1615 0.3447 0.0119  0.0640  0.0411  94  ALA A N   
673  C  CA  . ALA A 108 ? 0.2976 0.1403 0.2882 0.0137  0.1217  0.0101  94  ALA A CA  
674  C  C   . ALA A 108 ? 0.2300 0.1537 0.2573 -0.0058 0.0443  0.0388  94  ALA A C   
675  O  O   . ALA A 108 ? 0.2707 0.1502 0.3345 -0.0082 0.0841  0.0607  94  ALA A O   
676  C  CB  . ALA A 108 ? 0.2979 0.2137 0.4704 0.0682  0.1777  0.0801  94  ALA A CB  
677  N  N   . PRO A 109 ? 0.2714 0.1277 0.2897 -0.0222 0.0948  0.0520  95  PRO A N   
678  C  CA  . PRO A 109 ? 0.2954 0.1162 0.2685 0.0489  0.0937  0.0235  95  PRO A CA  
679  C  C   . PRO A 109 ? 0.2464 0.1015 0.2180 -0.0073 0.0466  0.0942  95  PRO A C   
680  O  O   . PRO A 109 ? 0.2084 0.1264 0.2490 0.0093  0.0962  0.0519  95  PRO A O   
681  C  CB  . PRO A 109 ? 0.3701 0.1508 0.4338 -0.0409 0.0928  0.0222  95  PRO A CB  
682  C  CG  . PRO A 109 ? 0.4547 0.1993 0.4032 0.0146  0.0512  -0.0125 95  PRO A CG  
683  C  CD  . PRO A 109 ? 0.3084 0.1874 0.3555 -0.0393 0.0861  0.0536  95  PRO A CD  
684  N  N   . VAL A 110 ? 0.1879 0.1134 0.2161 -0.0240 0.0789  0.0430  96  VAL A N   
685  C  CA  . VAL A 110 ? 0.1437 0.1053 0.2119 -0.0178 0.0360  0.0458  96  VAL A CA  
686  C  C   . VAL A 110 ? 0.1208 0.1426 0.2003 0.0095  0.0268  0.0141  96  VAL A C   
687  O  O   . VAL A 110 ? 0.1376 0.1513 0.2029 -0.0258 0.0455  0.0224  96  VAL A O   
688  C  CB  . VAL A 110 ? 0.1322 0.1326 0.2198 -0.0048 0.0213  0.0341  96  VAL A CB  
689  C  CG1 . VAL A 110 ? 0.1249 0.1697 0.2627 -0.0013 -0.0187 0.0273  96  VAL A CG1 
690  C  CG2 . VAL A 110 ? 0.1710 0.1902 0.2405 0.0183  0.0118  0.0470  96  VAL A CG2 
691  N  N   . TYR A 111 ? 0.1317 0.1261 0.1717 -0.0031 0.0271  0.0277  97  TYR A N   
692  C  CA  . TYR A 111 ? 0.1117 0.1245 0.1796 -0.0251 0.0296  0.0302  97  TYR A CA  
693  C  C   . TYR A 111 ? 0.1096 0.1022 0.1791 -0.0172 0.0124  0.0075  97  TYR A C   
694  O  O   . TYR A 111 ? 0.1064 0.1357 0.2265 -0.0182 0.0311  0.0225  97  TYR A O   
695  C  CB  . TYR A 111 ? 0.1113 0.1494 0.2157 -0.0096 0.0220  0.0176  97  TYR A CB  
696  C  CG  . TYR A 111 ? 0.1391 0.1379 0.1758 -0.0024 0.0256  -0.0049 97  TYR A CG  
697  C  CD1 . TYR A 111 ? 0.1499 0.1445 0.1925 -0.0221 0.0153  -0.0084 97  TYR A CD1 
698  C  CD2 . TYR A 111 ? 0.1413 0.1253 0.2468 -0.0257 0.0297  -0.0045 97  TYR A CD2 
699  C  CE1 . TYR A 111 ? 0.1399 0.1849 0.2282 -0.0228 0.0069  -0.0116 97  TYR A CE1 
700  C  CE2 . TYR A 111 ? 0.1505 0.1531 0.2835 -0.0057 0.0442  -0.0038 97  TYR A CE2 
701  C  CZ  . TYR A 111 ? 0.1871 0.1203 0.2208 -0.0282 0.0136  -0.0148 97  TYR A CZ  
702  O  OH  . TYR A 111 ? 0.2319 0.1709 0.2578 -0.0101 0.0201  -0.0254 97  TYR A OH  
703  N  N   . GLY A 112 ? 0.1158 0.1115 0.1930 -0.0177 0.0120  0.0006  98  GLY A N   
704  C  CA  . GLY A 112 ? 0.1023 0.1148 0.1957 0.0064  0.0139  0.0033  98  GLY A CA  
705  C  C   . GLY A 112 ? 0.1275 0.1194 0.1795 0.0104  0.0029  -0.0180 98  GLY A C   
706  O  O   . GLY A 112 ? 0.1240 0.1370 0.1890 -0.0137 0.0152  0.0035  98  GLY A O   
707  N  N   . SER A 113 ? 0.1108 0.1257 0.1899 -0.0090 0.0314  0.0101  99  SER A N   
708  C  CA  . SER A 113 ? 0.0956 0.1371 0.2113 0.0155  0.0152  -0.0092 99  SER A CA  
709  C  C   . SER A 113 ? 0.1313 0.1249 0.2082 -0.0148 0.0077  -0.0071 99  SER A C   
710  O  O   . SER A 113 ? 0.1465 0.1306 0.1822 -0.0205 0.0264  0.0182  99  SER A O   
711  C  CB  . SER A 113 ? 0.1338 0.1303 0.2217 0.0052  0.0182  0.0019  99  SER A CB  
712  O  OG  . SER A 113 ? 0.1658 0.1377 0.2166 -0.0045 0.0286  -0.0080 99  SER A OG  
713  N  N   . LYS A 114 ? 0.1282 0.1651 0.2183 -0.0085 0.0268  -0.0134 100 LYS A N   
714  C  CA  . LYS A 114 ? 0.1667 0.1913 0.2356 -0.0246 0.0122  -0.0208 100 LYS A CA  
715  C  C   . LYS A 114 ? 0.1733 0.2229 0.1931 -0.0092 0.0643  -0.0309 100 LYS A C   
716  O  O   . LYS A 114 ? 0.1642 0.1769 0.2398 -0.0327 0.0553  -0.0075 100 LYS A O   
717  C  CB  . LYS A 114 ? 0.1413 0.3179 0.4013 -0.0602 0.0185  -0.0362 100 LYS A CB  
718  C  CG  . LYS A 114 ? 0.2682 0.2631 0.3507 -0.0664 0.0283  0.0321  100 LYS A CG  
719  C  CD  . LYS A 114 ? 0.1703 0.3245 0.3836 0.0089  0.0431  0.0139  100 LYS A CD  
720  C  CE  . LYS A 114 ? 0.3186 0.4038 0.6987 -0.0002 -0.0134 0.0568  100 LYS A CE  
721  N  NZ  . LYS A 114 ? 0.4569 0.7215 0.8248 -0.1465 -0.0220 -0.0575 100 LYS A NZ  
722  N  N   . LEU A 115 ? 0.1700 0.1633 0.2004 -0.0051 0.0404  0.0002  101 LEU A N   
723  C  CA  . LEU A 115 ? 0.1689 0.1643 0.1944 -0.0054 0.0313  0.0012  101 LEU A CA  
724  C  C   . LEU A 115 ? 0.1597 0.1514 0.1613 -0.0215 0.0115  -0.0076 101 LEU A C   
725  O  O   . LEU A 115 ? 0.1494 0.1842 0.1936 -0.0158 0.0329  -0.0168 101 LEU A O   
726  C  CB  . LEU A 115 ? 0.1820 0.1654 0.1958 -0.0055 0.0280  -0.0173 101 LEU A CB  
727  C  CG  . LEU A 115 ? 0.1847 0.2266 0.1829 -0.0046 0.0555  -0.0331 101 LEU A CG  
728  C  CD1 . LEU A 115 ? 0.2143 0.1965 0.2390 -0.0271 0.0251  -0.0058 101 LEU A CD1 
729  C  CD2 . LEU A 115 ? 0.2464 0.1744 0.2110 -0.0216 0.0406  -0.0320 101 LEU A CD2 
730  N  N   . THR A 116 ? 0.1474 0.1453 0.2061 -0.0298 0.0114  -0.0165 102 THR A N   
731  C  CA  . THR A 116 ? 0.1303 0.1439 0.2003 -0.0120 0.0164  0.0054  102 THR A CA  
732  C  C   . THR A 116 ? 0.1259 0.1698 0.2175 -0.0063 0.0227  0.0145  102 THR A C   
733  O  O   . THR A 116 ? 0.1680 0.1643 0.1970 -0.0284 0.0197  -0.0055 102 THR A O   
734  C  CB  . THR A 116 ? 0.1227 0.1824 0.1947 -0.0122 0.0208  0.0029  102 THR A CB  
735  O  OG1 . THR A 116 ? 0.1691 0.1496 0.1985 -0.0291 0.0575  -0.0134 102 THR A OG1 
736  C  CG2 . THR A 116 ? 0.1447 0.2013 0.2353 -0.0136 0.0088  -0.0408 102 THR A CG2 
737  N  N   . ILE A 117 ? 0.1325 0.1516 0.2150 -0.0269 0.0176  0.0090  103 ILE A N   
738  C  CA  . ILE A 117 ? 0.1579 0.1769 0.2385 -0.0023 0.0035  0.0131  103 ILE A CA  
739  C  C   . ILE A 117 ? 0.1624 0.1829 0.2644 -0.0628 0.0198  0.0173  103 ILE A C   
740  O  O   . ILE A 117 ? 0.1736 0.2110 0.2215 -0.0338 0.0268  0.0136  103 ILE A O   
741  C  CB  . ILE A 117 ? 0.1763 0.1837 0.2707 -0.0021 0.0205  0.0327  103 ILE A CB  
742  C  CG1 . ILE A 117 ? 0.2006 0.1424 0.3135 -0.0222 -0.0198 0.0200  103 ILE A CG1 
743  C  CG2 . ILE A 117 ? 0.1881 0.1507 0.2966 -0.0119 0.0235  0.0183  103 ILE A CG2 
744  C  CD1 . ILE A 117 ? 0.2224 0.1931 0.2547 -0.0152 -0.0186 0.0000  103 ILE A CD1 
745  N  N   . ALA A 118 ? 0.1724 0.1828 0.2427 -0.0149 0.0192  -0.0097 104 ALA A N   
746  C  CA  . ALA A 118 ? 0.1953 0.1800 0.2720 -0.0235 0.0123  0.0126  104 ALA A CA  
747  C  C   . ALA A 118 ? 0.1802 0.2161 0.2613 -0.0042 0.0192  0.0152  104 ALA A C   
748  O  O   . ALA A 118 ? 0.2204 0.2424 0.2122 -0.0129 0.0583  0.0198  104 ALA A O   
749  C  CB  . ALA A 118 ? 0.2046 0.2271 0.2580 0.0190  0.0485  0.0117  104 ALA A CB  
750  N  N   . LEU A 119 ? 0.1975 0.1984 0.2009 -0.0143 0.0319  0.0151  105 LEU A N   
751  C  CA  . LEU A 119 ? 0.2074 0.1918 0.1902 -0.0139 0.0179  -0.0137 105 LEU A CA  
752  C  C   . LEU A 119 ? 0.1789 0.2050 0.1745 -0.0118 0.0253  0.0204  105 LEU A C   
753  O  O   . LEU A 119 ? 0.2115 0.2627 0.1850 -0.0147 0.0023  -0.0057 105 LEU A O   
754  C  CB  . LEU A 119 ? 0.2418 0.2136 0.1818 -0.0253 0.0246  -0.0088 105 LEU A CB  
755  C  CG  . LEU A 119 ? 0.2406 0.1877 0.1788 -0.0352 0.0111  -0.0017 105 LEU A CG  
756  C  CD1 . LEU A 119 ? 0.2400 0.2224 0.2398 -0.0384 0.0259  -0.0089 105 LEU A CD1 
757  C  CD2 . LEU A 119 ? 0.3323 0.2437 0.2346 0.0094  0.0187  -0.0521 105 LEU A CD2 
758  N  N   . VAL A 120 ? 0.1739 0.1860 0.1923 -0.0238 0.0155  0.0074  106 VAL A N   
759  C  CA  . VAL A 120 ? 0.1777 0.2039 0.1800 -0.0140 0.0145  0.0382  106 VAL A CA  
760  C  C   . VAL A 120 ? 0.1759 0.2545 0.2518 -0.0103 0.0457  0.0239  106 VAL A C   
761  O  O   . VAL A 120 ? 0.2190 0.2467 0.1959 -0.0133 0.0383  0.0242  106 VAL A O   
762  C  CB  . VAL A 120 ? 0.1319 0.1914 0.2031 -0.0255 0.0290  0.0051  106 VAL A CB  
763  C  CG1 . VAL A 120 ? 0.1929 0.1855 0.2301 -0.0246 0.0209  -0.0007 106 VAL A CG1 
764  C  CG2 . VAL A 120 ? 0.1721 0.1684 0.1819 -0.0293 -0.0001 0.0167  106 VAL A CG2 
765  N  N   . LYS A 121 ? 0.1714 0.2354 0.2009 -0.0113 0.0253  0.0329  107 LYS A N   
766  C  CA  . LYS A 121 ? 0.1940 0.2335 0.2465 -0.0359 0.0365  0.0336  107 LYS A CA  
767  C  C   . LYS A 121 ? 0.2500 0.3382 0.2191 -0.0393 0.1003  0.0429  107 LYS A C   
768  O  O   . LYS A 121 ? 0.2795 0.3273 0.2210 -0.0128 0.0384  0.0457  107 LYS A O   
769  C  CB  . LYS A 121 ? 0.2087 0.2680 0.2745 -0.0597 0.0611  0.0301  107 LYS A CB  
770  C  CG  . LYS A 121 ? 0.2007 0.2574 0.2607 -0.0361 0.0001  0.0243  107 LYS A CG  
771  C  CD  . LYS A 121 ? 0.2287 0.3809 0.3476 -0.0602 0.0352  -0.0190 107 LYS A CD  
772  C  CE  . LYS A 121 ? 0.2765 0.2584 0.4268 -0.1437 0.0503  -0.0360 107 LYS A CE  
773  N  NZ  . LYS A 121 ? 0.2689 0.4678 0.4440 -0.1017 0.0754  -0.1139 107 LYS A NZ  
774  N  N   . GLU A 122 ? 0.2769 0.3494 0.2304 0.0097  0.0294  0.0316  108 GLU A N   
775  C  CA  . GLU A 122 ? 0.3170 0.4365 0.2538 -0.0325 0.0183  0.0302  108 GLU A CA  
776  C  C   . GLU A 122 ? 0.2627 0.4467 0.2787 0.0029  0.0280  0.0139  108 GLU A C   
777  O  O   . GLU A 122 ? 0.3677 0.4486 0.2220 -0.0329 0.0001  0.0046  108 GLU A O   
778  C  CB  . GLU A 122 ? 0.3561 0.4489 0.1871 -0.0263 -0.0087 -0.0276 108 GLU A CB  
779  C  CG  . GLU A 122 ? 0.6618 0.5172 0.2747 0.0004  0.0465  -0.0522 108 GLU A CG  
780  C  CD  . GLU A 122 ? 0.9179 0.8865 0.5272 -0.1178 0.1326  0.0024  108 GLU A CD  
781  O  OE1 . GLU A 122 ? 0.5797 1.0451 0.3514 -0.1466 0.3836  0.0176  108 GLU A OE1 
782  O  OE2 . GLU A 122 ? 0.8814 0.9604 0.3973 -0.1271 0.0333  0.0061  108 GLU A OE2 
783  N  N   . ALA A 123 ? 0.2606 0.3451 0.2601 -0.0453 0.0187  0.0231  109 ALA A N   
784  C  CA  . ALA A 123 ? 0.3019 0.2941 0.2321 -0.0344 -0.0052 -0.0362 109 ALA A CA  
785  C  C   . ALA A 123 ? 0.2915 0.3481 0.2140 -0.0038 0.0484  -0.0099 109 ALA A C   
786  O  O   . ALA A 123 ? 0.2832 0.3420 0.2440 -0.0179 -0.0428 0.0401  109 ALA A O   
787  C  CB  . ALA A 123 ? 0.2350 0.3088 0.2568 -0.0412 0.0230  0.0466  109 ALA A CB  
788  N  N   . MET A 124 ? 0.2606 0.3089 0.2348 -0.0397 -0.0137 0.0441  110 MET A N   
789  C  CA  . MET A 124 ? 0.2432 0.3563 0.2448 -0.0193 0.0183  0.0159  110 MET A CA  
790  C  C   . MET A 124 ? 0.2703 0.4218 0.2653 -0.0085 0.0323  0.0600  110 MET A C   
791  O  O   . MET A 124 ? 0.2951 0.3934 0.2578 -0.0199 0.0125  0.0871  110 MET A O   
792  C  CB  . MET A 124 ? 0.2511 0.2667 0.2423 -0.0398 -0.0084 0.0523  110 MET A CB  
793  C  CG  . MET A 124 ? 0.2090 0.3080 0.2456 -0.0437 -0.0106 0.0032  110 MET A CG  
794  S  SD  . MET A 124 ? 0.2249 0.3235 0.3091 -0.0574 0.0080  0.0019  110 MET A SD  
795  C  CE  . MET A 124 ? 0.4887 0.4204 0.2718 0.0632  -0.0480 0.1266  110 MET A CE  
796  N  N   . LYS A 125 ? 0.3529 0.4130 0.1695 0.0339  0.0307  0.1086  111 LYS A N   
797  C  CA  . LYS A 125 ? 0.4142 0.5179 0.2199 0.0365  0.0781  0.0923  111 LYS A CA  
798  C  C   . LYS A 125 ? 0.5394 0.5825 0.2718 -0.0213 0.0080  0.1904  111 LYS A C   
799  O  O   . LYS A 125 ? 0.3845 0.5213 0.3452 -0.0305 -0.0599 0.0667  111 LYS A O   
800  C  CB  . LYS A 125 ? 0.3771 0.6666 0.2043 0.0668  0.0412  0.0418  111 LYS A CB  
801  N  N   . ALA A 126 ? 0.3792 0.5025 0.2979 -0.0206 0.0253  0.0259  112 ALA A N   
802  C  CA  . ALA A 126 ? 0.4544 0.5949 0.1790 -0.0235 0.0212  -0.0128 112 ALA A CA  
803  C  C   . ALA A 126 ? 0.4426 0.3928 0.3335 0.0319  -0.0255 -0.0461 112 ALA A C   
804  O  O   . ALA A 126 ? 0.5059 0.5959 0.2527 0.0323  -0.1179 -0.0072 112 ALA A O   
805  C  CB  . ALA A 126 ? 0.4760 0.5506 0.1715 -0.0320 -0.0454 -0.0057 112 ALA A CB  
806  N  N   . ARG A 127 ? 0.3673 0.3792 0.2729 -0.0081 0.0057  0.0306  113 ARG A N   
807  C  CA  . ARG A 127 ? 0.3192 0.3187 0.3075 0.0121  0.0274  0.0369  113 ARG A CA  
808  C  C   . ARG A 127 ? 0.3290 0.4345 0.3077 -0.0055 -0.0017 0.0170  113 ARG A C   
809  O  O   . ARG A 127 ? 0.3407 0.4393 0.3898 0.0031  -0.0389 0.0691  113 ARG A O   
810  C  CB  . ARG A 127 ? 0.2788 0.3986 0.2950 -0.0293 0.0196  0.0095  113 ARG A CB  
811  C  CG  . ARG A 127 ? 0.3592 0.4395 0.2712 -0.0056 0.0048  0.0457  113 ARG A CG  
812  C  CD  . ARG A 127 ? 0.3230 0.4404 0.2839 -0.0213 -0.0136 0.0443  113 ARG A CD  
813  N  NE  . ARG A 127 ? 0.3354 0.4225 0.2327 -0.0152 -0.0715 -0.0065 113 ARG A NE  
814  C  CZ  . ARG A 127 ? 0.2551 0.3725 0.3541 -0.0146 -0.0094 0.0688  113 ARG A CZ  
815  N  NH1 . ARG A 127 ? 0.2626 0.3138 0.2694 -0.0636 -0.0424 0.0338  113 ARG A NH1 
816  N  NH2 . ARG A 127 ? 0.2835 0.4809 0.2951 0.0092  -0.0305 0.1449  113 ARG A NH2 
817  N  N   . ASN A 128 ? 0.3348 0.4129 0.2797 -0.0495 -0.0195 0.0798  114 ASN A N   
818  C  CA  . ASN A 128 ? 0.4074 0.4599 0.3670 -0.0809 -0.0284 0.1789  114 ASN A CA  
819  C  C   . ASN A 128 ? 0.4234 0.3622 0.4181 -0.0174 -0.0361 0.1039  114 ASN A C   
820  O  O   . ASN A 128 ? 0.4725 0.4084 0.4134 -0.0166 -0.1598 0.1445  114 ASN A O   
821  C  CB  . ASN A 128 ? 0.4897 0.4270 0.3632 -0.0610 -0.0498 0.0310  114 ASN A CB  
822  C  CG  . ASN A 128 ? 0.5413 0.7305 0.6454 -0.0984 -0.1568 -0.0039 114 ASN A CG  
823  O  OD1 . ASN A 128 ? 0.5224 0.6117 0.5244 0.1407  -0.0629 0.1217  114 ASN A OD1 
824  N  ND2 . ASN A 128 ? 0.5160 0.7964 0.6725 0.0025  -0.2184 -0.1380 114 ASN A ND2 
825  N  N   . ILE A 129 ? 0.3500 0.4412 0.4194 -0.0452 -0.0687 0.1035  115 ILE A N   
826  C  CA  . ILE A 129 ? 0.3671 0.3791 0.3819 -0.0439 -0.0697 0.1259  115 ILE A CA  
827  C  C   . ILE A 129 ? 0.3278 0.3270 0.4737 -0.0310 -0.0444 0.1500  115 ILE A C   
828  O  O   . ILE A 129 ? 0.3995 0.5045 0.4063 -0.0937 -0.0643 0.1500  115 ILE A O   
829  C  CB  . ILE A 129 ? 0.3261 0.4663 0.4249 -0.0985 -0.0687 0.0724  115 ILE A CB  
830  C  CG1 . ILE A 129 ? 0.3164 0.5169 0.5173 -0.0906 -0.0497 0.0038  115 ILE A CG1 
831  C  CG2 . ILE A 129 ? 0.4823 0.5437 0.4707 0.0673  -0.0864 0.1946  115 ILE A CG2 
832  C  CD1 . ILE A 129 ? 0.5060 0.4699 0.4780 -0.1350 -0.0065 0.0994  115 ILE A CD1 
833  N  N   . LYS A 130 ? 0.4453 0.5466 0.5261 -0.1254 -0.1564 0.1563  116 LYS A N   
834  C  CA  . LYS A 130 ? 0.5509 0.5485 0.4962 -0.2036 -0.0116 0.2233  116 LYS A CA  
835  C  C   . LYS A 130 ? 0.5084 0.4243 0.2832 -0.1189 -0.1320 0.0702  116 LYS A C   
836  O  O   . LYS A 130 ? 0.5942 0.5653 0.5901 -0.3081 -0.1213 0.2773  116 LYS A O   
837  C  CB  . LYS A 130 ? 0.5282 0.4207 0.5292 -0.0873 -0.0598 0.1976  116 LYS A CB  
838  N  N   . LYS A 131 ? 0.4210 0.5182 0.5839 -0.0793 -0.1360 0.1282  117 LYS A N   
839  C  CA  . LYS A 131 ? 0.3925 0.3495 0.5423 -0.1170 -0.0905 0.1626  117 LYS A CA  
840  C  C   . LYS A 131 ? 0.5451 0.4561 0.5309 -0.0194 -0.1320 0.0679  117 LYS A C   
841  O  O   . LYS A 131 ? 0.4670 0.3628 0.4023 0.0093  -0.0249 0.0727  117 LYS A O   
842  C  CB  . LYS A 131 ? 0.3550 0.7483 0.6680 0.0525  -0.0207 0.0492  117 LYS A CB  
843  N  N   . LYS A 132 ? 0.4745 0.3758 0.5666 0.0338  0.0040  0.1938  118 LYS A N   
844  C  CA  . LYS A 132 ? 0.4620 0.3635 0.4877 -0.1568 0.0152  0.2117  118 LYS A CA  
845  C  C   . LYS A 132 ? 0.4011 0.2981 0.3697 0.0314  0.0284  0.1441  118 LYS A C   
846  O  O   . LYS A 132 ? 0.4459 0.4350 0.4985 -0.0489 0.0459  0.2737  118 LYS A O   
847  C  CB  . LYS A 132 ? 0.3745 0.3355 0.4675 -0.0511 0.0539  0.1005  118 LYS A CB  
848  N  N   . VAL A 133 ? 0.2240 0.3307 0.4036 -0.0620 0.0484  0.0925  119 VAL A N   
849  C  CA  . VAL A 133 ? 0.2486 0.3146 0.3123 -0.0513 0.0376  0.0490  119 VAL A CA  
850  C  C   . VAL A 133 ? 0.1993 0.2108 0.2939 -0.0522 -0.0028 0.0263  119 VAL A C   
851  O  O   . VAL A 133 ? 0.2031 0.3244 0.3232 -0.0293 0.0652  0.0055  119 VAL A O   
852  C  CB  . VAL A 133 ? 0.2186 0.3418 0.2987 -0.0155 0.0216  0.0215  119 VAL A CB  
853  C  CG1 . VAL A 133 ? 0.2003 0.2902 0.3266 -0.0423 -0.0074 0.0154  119 VAL A CG1 
854  C  CG2 . VAL A 133 ? 0.3405 0.4419 0.4074 -0.0496 -0.0275 0.1410  119 VAL A CG2 
855  N  N   . ARG A 134 ? 0.1833 0.1603 0.2644 -0.0107 0.0380  0.0346  120 ARG A N   
856  C  CA  . ARG A 134 ? 0.1776 0.1479 0.2666 -0.0370 0.0299  0.0410  120 ARG A CA  
857  C  C   . ARG A 134 ? 0.1936 0.1319 0.2334 -0.0150 0.0571  0.0458  120 ARG A C   
858  O  O   . ARG A 134 ? 0.3112 0.1599 0.3183 0.0127  0.1666  0.0502  120 ARG A O   
859  C  CB  . ARG A 134 ? 0.2277 0.1579 0.3106 -0.0161 0.0183  0.0541  120 ARG A CB  
860  C  CG  . ARG A 134 ? 0.2557 0.2026 0.3938 -0.0161 0.0122  0.0720  120 ARG A CG  
861  C  CD  . ARG A 134 ? 0.3629 0.2318 0.3876 -0.0113 -0.0148 0.0254  120 ARG A CD  
862  N  NE  . ARG A 134 ? 0.3149 0.2416 0.3866 0.0280  0.0334  0.0141  120 ARG A NE  
863  C  CZ  . ARG A 134 ? 0.3360 0.3590 0.4063 0.0181  0.0632  0.0846  120 ARG A CZ  
864  N  NH1 . ARG A 134 ? 0.4158 0.2962 0.4222 0.0189  0.0346  -0.0299 120 ARG A NH1 
865  N  NH2 . ARG A 134 ? 0.4105 0.3785 0.5244 0.0120  0.0742  0.0652  120 ARG A NH2 
866  N  N   . TYR A 135 ? 0.1266 0.1301 0.1948 -0.0259 0.0214  0.0391  121 TYR A N   
867  C  CA  . TYR A 135 ? 0.1331 0.1102 0.2042 -0.0296 0.0221  0.0470  121 TYR A CA  
868  C  C   . TYR A 135 ? 0.1295 0.1253 0.1750 -0.0090 -0.0021 0.0108  121 TYR A C   
869  O  O   . TYR A 135 ? 0.1254 0.1493 0.1957 -0.0380 0.0178  0.0499  121 TYR A O   
870  C  CB  . TYR A 135 ? 0.1684 0.1338 0.2101 -0.0088 0.0293  0.0216  121 TYR A CB  
871  C  CG  . TYR A 135 ? 0.1532 0.1560 0.1814 -0.0417 0.0156  0.0332  121 TYR A CG  
872  C  CD1 . TYR A 135 ? 0.2082 0.1826 0.2562 -0.0302 0.0069  0.0530  121 TYR A CD1 
873  C  CD2 . TYR A 135 ? 0.1542 0.2209 0.2046 -0.0557 -0.0142 0.0377  121 TYR A CD2 
874  C  CE1 . TYR A 135 ? 0.2044 0.1829 0.2436 -0.0409 0.0024  0.0479  121 TYR A CE1 
875  C  CE2 . TYR A 135 ? 0.1848 0.2601 0.2094 -0.0678 0.0305  0.0665  121 TYR A CE2 
876  C  CZ  . TYR A 135 ? 0.1965 0.2455 0.2121 -0.0526 -0.0299 -0.0010 121 TYR A CZ  
877  O  OH  . TYR A 135 ? 0.2182 0.3298 0.2363 -0.0871 -0.0192 0.0371  121 TYR A OH  
878  N  N   . TYR A 136 ? 0.1003 0.1329 0.1843 -0.0245 0.0162  0.0305  122 TYR A N   
879  C  CA  . TYR A 136 ? 0.1340 0.1373 0.1896 -0.0117 0.0281  0.0052  122 TYR A CA  
880  C  C   . TYR A 136 ? 0.1496 0.1379 0.1901 -0.0247 0.0007  0.0051  122 TYR A C   
881  O  O   . TYR A 136 ? 0.1225 0.1752 0.2146 -0.0126 0.0352  0.0452  122 TYR A O   
882  C  CB  . TYR A 136 ? 0.1329 0.2373 0.2268 -0.0398 0.0267  -0.0067 122 TYR A CB  
883  C  CG  . TYR A 136 ? 0.3337 0.4793 0.1464 -0.0226 0.0109  -0.0260 122 TYR A CG  
884  C  CD1 . TYR A 136 ? 0.8010 0.5968 0.4327 0.0845  0.2021  0.2344  122 TYR A CD1 
885  C  CD2 . TYR A 136 ? 0.2991 0.2541 0.3107 -0.0132 0.0261  -0.0400 122 TYR A CD2 
886  C  CE1 . TYR A 136 ? 0.4113 0.2611 0.3979 -0.1175 -0.0374 0.0113  122 TYR A CE1 
887  C  CE2 . TYR A 136 ? 0.2699 0.2496 0.4653 0.0110  0.0473  0.0243  122 TYR A CE2 
888  C  CZ  . TYR A 136 ? 0.2419 0.2642 0.4786 -0.0312 -0.0013 0.0787  122 TYR A CZ  
889  O  OH  . TYR A 136 ? 0.2683 0.3002 0.4207 -0.0055 -0.0267 0.0689  122 TYR A OH  
890  N  N   . THR A 137 ? 0.1347 0.1261 0.1913 -0.0185 0.0293  0.0171  123 THR A N   
891  C  CA  . THR A 137 ? 0.1291 0.1422 0.1818 -0.0255 0.0216  0.0250  123 THR A CA  
892  C  C   . THR A 137 ? 0.1273 0.1713 0.2387 -0.0180 0.0118  0.0229  123 THR A C   
893  O  O   . THR A 137 ? 0.1388 0.1823 0.2669 -0.0322 -0.0225 0.0242  123 THR A O   
894  C  CB  . THR A 137 ? 0.1570 0.1393 0.2284 -0.0359 0.0351  0.0060  123 THR A CB  
895  O  OG1 . THR A 137 ? 0.1766 0.1630 0.2097 -0.0355 0.0509  0.0173  123 THR A OG1 
896  C  CG2 . THR A 137 ? 0.1717 0.1766 0.2735 0.0015  0.0300  -0.0125 123 THR A CG2 
897  N  N   . VAL A 138 ? 0.1098 0.1336 0.2231 -0.0182 -0.0025 0.0305  124 VAL A N   
898  C  CA  . VAL A 138 ? 0.1267 0.1374 0.2271 -0.0004 0.0176  0.0306  124 VAL A CA  
899  C  C   . VAL A 138 ? 0.1381 0.1502 0.1777 -0.0068 0.0197  0.0124  124 VAL A C   
900  O  O   . VAL A 138 ? 0.1336 0.1823 0.2043 0.0271  0.0026  -0.0019 124 VAL A O   
901  C  CB  . VAL A 138 ? 0.1379 0.1512 0.1913 0.0117  -0.0046 0.0254  124 VAL A CB  
902  C  CG1 . VAL A 138 ? 0.1708 0.1553 0.2176 0.0100  0.0074  0.0201  124 VAL A CG1 
903  C  CG2 . VAL A 138 ? 0.1367 0.1740 0.1935 -0.0051 -0.0086 0.0186  124 VAL A CG2 
904  N  N   . ASN A 139 ? 0.1355 0.1760 0.2297 0.0046  0.0173  0.0253  125 ASN A N   
905  C  CA  . ASN A 139 ? 0.1496 0.1644 0.2361 0.0396  0.0416  0.0008  125 ASN A CA  
906  C  C   . ASN A 139 ? 0.1341 0.1893 0.2226 -0.0016 0.0326  0.0104  125 ASN A C   
907  O  O   . ASN A 139 ? 0.1309 0.1891 0.2353 0.0140  0.0063  0.0166  125 ASN A O   
908  C  CB  . ASN A 139 ? 0.1706 0.1975 0.2020 0.0293  0.0007  0.0168  125 ASN A CB  
909  C  CG  . ASN A 139 ? 0.1540 0.2097 0.2339 0.0441  0.0352  0.0142  125 ASN A CG  
910  O  OD1 . ASN A 139 ? 0.1354 0.2365 0.2536 -0.0005 0.0267  0.0272  125 ASN A OD1 
911  N  ND2 . ASN A 139 ? 0.2408 0.2708 0.2854 -0.0299 0.1028  0.0360  125 ASN A ND2 
912  N  N   . HIS A 140 ? 0.1358 0.2057 0.2001 0.0435  0.0362  0.0200  126 HIS A N   
913  C  CA  . HIS A 140 ? 0.1428 0.2015 0.1931 0.0156  0.0292  0.0120  126 HIS A CA  
914  C  C   . HIS A 140 ? 0.1470 0.2142 0.1883 0.0098  -0.0002 0.0343  126 HIS A C   
915  O  O   . HIS A 140 ? 0.2176 0.2753 0.1986 0.0142  0.0331  0.0282  126 HIS A O   
916  C  CB  . HIS A 140 ? 0.1657 0.1968 0.2205 0.0100  0.0257  0.0157  126 HIS A CB  
917  C  CG  . HIS A 140 ? 0.1733 0.2022 0.2700 0.0263  0.0110  0.0310  126 HIS A CG  
918  N  ND1 . HIS A 140 ? 0.2582 0.2279 0.3128 0.0715  0.0110  -0.0016 126 HIS A ND1 
919  C  CD2 . HIS A 140 ? 0.1947 0.2049 0.3427 0.0923  0.0223  0.0180  126 HIS A CD2 
920  C  CE1 . HIS A 140 ? 0.1185 0.2911 0.4394 0.0613  0.0295  0.0235  126 HIS A CE1 
921  N  NE2 . HIS A 140 ? 0.1794 0.3001 0.4082 0.0687  0.0453  0.0263  126 HIS A NE2 
922  N  N   . ASP A 141 ? 0.1631 0.1963 0.2321 0.0178  0.0286  0.0338  127 ASP A N   
923  C  CA  . ASP A 141 ? 0.1840 0.2224 0.2681 0.0039  -0.0189 0.0317  127 ASP A CA  
924  C  C   . ASP A 141 ? 0.1811 0.2345 0.2479 -0.0077 -0.0049 -0.0084 127 ASP A C   
925  O  O   . ASP A 141 ? 0.1819 0.2623 0.3066 0.0113  -0.0399 -0.0047 127 ASP A O   
926  C  CB  . ASP A 141 ? 0.1673 0.2560 0.2985 0.0291  0.0150  0.0188  127 ASP A CB  
927  C  CG  . ASP A 141 ? 0.2570 0.3331 0.3240 -0.0033 0.0306  0.0233  127 ASP A CG  
928  O  OD1 . ASP A 141 ? 0.1800 0.3680 0.4094 0.0478  0.0002  0.0358  127 ASP A OD1 
929  O  OD2 . ASP A 141 ? 0.2941 0.4361 0.4401 0.0994  0.0626  0.0218  127 ASP A OD2 
930  N  N   . SER A 142 ? 0.1458 0.2072 0.2480 0.0023  -0.0175 0.0126  128 SER A N   
931  C  CA  . SER A 142 ? 0.1478 0.1864 0.2507 -0.0194 0.0026  0.0317  128 SER A CA  
932  C  C   . SER A 142 ? 0.1566 0.2029 0.2187 0.0048  -0.0154 0.0040  128 SER A C   
933  O  O   . SER A 142 ? 0.1473 0.2012 0.2354 -0.0118 0.0088  0.0056  128 SER A O   
934  C  CB  . SER A 142 ? 0.1493 0.1844 0.2060 -0.0025 -0.0151 0.0200  128 SER A CB  
935  O  OG  . SER A 142 ? 0.1571 0.2204 0.2424 -0.0027 0.0000  0.0069  128 SER A OG  
936  N  N   . ILE A 143 ? 0.1365 0.2308 0.2604 -0.0164 0.0064  -0.0256 129 ILE A N   
937  C  CA  . ILE A 143 ? 0.1476 0.2265 0.2567 -0.0309 -0.0299 -0.0037 129 ILE A CA  
938  C  C   . ILE A 143 ? 0.1775 0.1586 0.2763 0.0002  -0.0193 -0.0297 129 ILE A C   
939  O  O   . ILE A 143 ? 0.1853 0.2058 0.3340 -0.0474 0.0021  -0.0333 129 ILE A O   
940  C  CB  . ILE A 143 ? 0.2181 0.2716 0.2632 -0.0065 -0.0092 -0.0330 129 ILE A CB  
941  C  CG1 . ILE A 143 ? 0.2238 0.3405 0.3035 -0.0185 -0.0683 -0.0299 129 ILE A CG1 
942  C  CG2 . ILE A 143 ? 0.2367 0.2745 0.2653 -0.0261 -0.0414 -0.0786 129 ILE A CG2 
943  C  CD1 . ILE A 143 ? 0.3107 0.3920 0.3858 0.0198  -0.0847 -0.0212 129 ILE A CD1 
944  N  N   . MET A 144 ? 0.1508 0.1892 0.2832 -0.0324 0.0172  0.0053  130 MET A N   
945  C  CA  . MET A 144 ? 0.1636 0.1779 0.2939 -0.0241 -0.0215 0.0108  130 MET A CA  
946  C  C   . MET A 144 ? 0.2031 0.1799 0.2922 -0.0172 0.0160  0.0264  130 MET A C   
947  O  O   . MET A 144 ? 0.2341 0.1890 0.3134 -0.0440 0.0317  0.0021  130 MET A O   
948  C  CB  . MET A 144 ? 0.1893 0.1930 0.2780 -0.0018 -0.0194 0.0377  130 MET A CB  
949  C  CG  . MET A 144 ? 0.2101 0.2212 0.3313 -0.0205 -0.0348 0.0507  130 MET A CG  
950  S  SD  . MET A 144 ? 0.2221 0.3133 0.3980 -0.0141 -0.0236 0.0162  130 MET A SD  
951  C  CE  . MET A 144 ? 0.3314 0.2590 0.4277 0.0321  -0.0729 0.0631  130 MET A CE  
952  N  N   . ARG A 145 ? 0.2353 0.1784 0.2758 -0.0625 -0.0041 -0.0264 131 ARG A N   
953  C  CA  . ARG A 145 ? 0.1443 0.1973 0.3922 -0.0708 0.0130  -0.0084 131 ARG A CA  
954  C  C   . ARG A 145 ? 0.2882 0.1952 0.3933 -0.0372 -0.0179 0.0075  131 ARG A C   
955  O  O   . ARG A 145 ? 0.2780 0.2556 0.4145 -0.0088 0.0855  0.0291  131 ARG A O   
956  C  CB  . ARG A 145 ? 0.2136 0.2376 0.3695 -0.0411 0.0249  -0.0559 131 ARG A CB  
957  C  CG  . ARG A 145 ? 0.2173 0.3357 0.4183 -0.0383 -0.0278 -0.0606 131 ARG A CG  
958  C  CD  . ARG A 145 ? 0.2614 0.3478 0.4128 -0.0535 -0.0073 -0.0979 131 ARG A CD  
959  N  NE  . ARG A 145 ? 0.3698 0.4637 0.3578 0.0229  -0.0697 -0.0916 131 ARG A NE  
960  C  CZ  . ARG A 145 ? 0.6369 0.4741 0.5461 0.0920  -0.1301 -0.1008 131 ARG A CZ  
961  N  NH1 . ARG A 145 ? 0.6540 0.8077 0.4870 0.0644  -0.0610 -0.0581 131 ARG A NH1 
962  N  NH2 . ARG A 145 ? 0.5833 0.6249 0.6471 0.0924  -0.1899 -0.1436 131 ARG A NH2 
963  N  N   . PHE A 146 ? 0.1693 0.1805 0.3524 -0.0465 -0.0142 -0.0301 132 PHE A N   
964  C  CA  . PHE A 146 ? 0.1792 0.1745 0.3408 -0.0216 0.0073  -0.0396 132 PHE A CA  
965  C  C   . PHE A 146 ? 0.2482 0.2077 0.3834 0.0134  -0.0109 -0.0651 132 PHE A C   
966  O  O   . PHE A 146 ? 0.2171 0.3098 0.4287 -0.0253 -0.0493 -0.1269 132 PHE A O   
967  C  CB  . PHE A 146 ? 0.1509 0.1949 0.3233 -0.0383 0.0083  -0.0158 132 PHE A CB  
968  C  CG  . PHE A 146 ? 0.1635 0.2050 0.2808 -0.0333 0.0225  0.0165  132 PHE A CG  
969  C  CD1 . PHE A 146 ? 0.2340 0.2019 0.3315 -0.0428 -0.0110 -0.0113 132 PHE A CD1 
970  C  CD2 . PHE A 146 ? 0.1624 0.1710 0.2572 -0.0227 -0.0059 0.0227  132 PHE A CD2 
971  C  CE1 . PHE A 146 ? 0.2337 0.2465 0.3012 -0.0381 -0.0404 0.0241  132 PHE A CE1 
972  C  CE2 . PHE A 146 ? 0.1614 0.1878 0.2471 -0.0529 -0.0045 -0.0065 132 PHE A CE2 
973  C  CZ  . PHE A 146 ? 0.1925 0.2001 0.2947 -0.0440 -0.0085 -0.0286 132 PHE A CZ  
974  N  N   . LYS A 147 ? 0.2176 0.1921 0.3258 -0.0313 0.0245  -0.0307 133 LYS A N   
975  C  CA  . LYS A 147 ? 0.2304 0.2060 0.3478 -0.0310 -0.0126 -0.0762 133 LYS A CA  
976  C  C   . LYS A 147 ? 0.2394 0.2770 0.3040 0.0265  -0.0399 -0.0960 133 LYS A C   
977  O  O   . LYS A 147 ? 0.2951 0.3033 0.3825 -0.0209 -0.0302 -0.0849 133 LYS A O   
978  C  CB  . LYS A 147 ? 0.3036 0.2179 0.4373 0.0151  0.0146  -0.0691 133 LYS A CB  
979  C  CG  . LYS A 147 ? 0.3226 0.3318 0.5618 0.0416  -0.0562 -0.1596 133 LYS A CG  
980  C  CD  . LYS A 147 ? 0.4119 0.4349 0.6604 0.1395  0.0681  -0.0352 133 LYS A CD  
981  C  CE  . LYS A 147 ? 0.6144 0.6140 0.7885 0.1196  0.1000  -0.0680 133 LYS A CE  
982  N  NZ  . LYS A 147 ? 0.5072 0.7441 0.8775 0.0382  -0.0014 0.0533  133 LYS A NZ  
983  N  N   . ASN A 148 ? 0.1934 0.2176 0.3249 -0.0289 -0.0237 -0.0329 134 ASN A N   
984  C  CA  . ASN A 148 ? 0.2369 0.2244 0.3015 0.0213  0.0003  -0.0493 134 ASN A CA  
985  C  C   . ASN A 148 ? 0.2676 0.2273 0.2478 0.0306  0.0168  -0.0108 134 ASN A C   
986  O  O   . ASN A 148 ? 0.2826 0.2799 0.2742 0.0611  0.0025  -0.0355 134 ASN A O   
987  C  CB  . ASN A 148 ? 0.2750 0.2205 0.2790 0.0138  -0.0126 -0.0704 134 ASN A CB  
988  C  CG  . ASN A 148 ? 0.2629 0.1946 0.2714 0.0036  -0.0144 -0.0110 134 ASN A CG  
989  O  OD1 . ASN A 148 ? 0.2609 0.2588 0.4192 -0.0232 -0.0077 -0.0721 134 ASN A OD1 
990  N  ND2 . ASN A 148 ? 0.2196 0.3904 0.3296 -0.0762 -0.0561 -0.0582 134 ASN A ND2 
991  N  N   . VAL A 149 ? 0.1857 0.2756 0.2478 0.0311  -0.0425 -0.0353 135 VAL A N   
992  C  CA  . VAL A 149 ? 0.1863 0.2011 0.2011 -0.0119 -0.0154 -0.0401 135 VAL A CA  
993  C  C   . VAL A 149 ? 0.1697 0.2193 0.2284 -0.0357 -0.0418 -0.0179 135 VAL A C   
994  O  O   . VAL A 149 ? 0.1644 0.1987 0.2794 -0.0051 0.0061  -0.0665 135 VAL A O   
995  C  CB  . VAL A 149 ? 0.2128 0.2294 0.2446 -0.0211 0.0068  -0.0261 135 VAL A CB  
996  C  CG1 . VAL A 149 ? 0.2203 0.2708 0.2863 -0.0113 0.0069  -0.0077 135 VAL A CG1 
997  C  CG2 . VAL A 149 ? 0.1844 0.1927 0.2969 -0.0357 -0.0355 0.0155  135 VAL A CG2 
998  N  N   . ASN A 150 ? 0.1702 0.2001 0.2353 0.0044  -0.0299 -0.0420 136 ASN A N   
999  C  CA  . ASN A 150 ? 0.1586 0.2020 0.2481 -0.0214 0.0032  -0.0461 136 ASN A CA  
1000 C  C   . ASN A 150 ? 0.1695 0.1551 0.2091 -0.0092 -0.0102 -0.0051 136 ASN A C   
1001 O  O   . ASN A 150 ? 0.2122 0.1732 0.2201 -0.0190 0.0033  -0.0332 136 ASN A O   
1002 C  CB  . ASN A 150 ? 0.1878 0.2241 0.3196 -0.0212 -0.0377 -0.0715 136 ASN A CB  
1003 C  CG  . ASN A 150 ? 0.1901 0.3309 0.3428 0.0069  -0.0631 -0.0313 136 ASN A CG  
1004 O  OD1 . ASN A 150 ? 0.2189 0.3004 0.3439 -0.0598 -0.0313 -0.0588 136 ASN A OD1 
1005 N  ND2 . ASN A 150 ? 0.2514 0.3751 0.5377 -0.0799 -0.1033 -0.0343 136 ASN A ND2 
1006 N  N   . VAL A 151 ? 0.1513 0.1635 0.2069 -0.0410 -0.0007 -0.0074 137 VAL A N   
1007 C  CA  . VAL A 151 ? 0.1451 0.1325 0.1981 -0.0144 0.0133  -0.0229 137 VAL A CA  
1008 C  C   . VAL A 151 ? 0.1558 0.1530 0.1917 0.0034  0.0054  -0.0149 137 VAL A C   
1009 O  O   . VAL A 151 ? 0.1624 0.1621 0.2256 -0.0170 0.0042  -0.0035 137 VAL A O   
1010 C  CB  . VAL A 151 ? 0.1458 0.1297 0.2143 -0.0210 0.0010  -0.0094 137 VAL A CB  
1011 C  CG1 . VAL A 151 ? 0.1516 0.1637 0.2336 -0.0360 -0.0405 -0.0271 137 VAL A CG1 
1012 C  CG2 . VAL A 151 ? 0.1500 0.1497 0.2667 -0.0200 -0.0157 -0.0217 137 VAL A CG2 
1013 N  N   . SER A 152 ? 0.1347 0.1584 0.2102 -0.0137 -0.0001 -0.0108 138 SER A N   
1014 C  CA  . SER A 152 ? 0.1416 0.1598 0.1886 -0.0123 -0.0052 -0.0321 138 SER A CA  
1015 C  C   . SER A 152 ? 0.1501 0.1628 0.1873 -0.0050 -0.0110 -0.0318 138 SER A C   
1016 O  O   . SER A 152 ? 0.1309 0.1381 0.1895 -0.0116 0.0102  -0.0152 138 SER A O   
1017 C  CB  . SER A 152 ? 0.1541 0.1726 0.2063 0.0038  0.0013  -0.0231 138 SER A CB  
1018 O  OG  . SER A 152 ? 0.1771 0.2088 0.2209 0.0194  -0.0140 -0.0052 138 SER A OG  
1019 N  N   . PHE A 153 ? 0.1163 0.1616 0.2006 -0.0019 0.0204  -0.0217 139 PHE A N   
1020 C  CA  . PHE A 153 ? 0.1327 0.1519 0.1835 0.0117  0.0055  -0.0243 139 PHE A CA  
1021 C  C   . PHE A 153 ? 0.1343 0.1621 0.1883 0.0037  0.0029  -0.0167 139 PHE A C   
1022 O  O   . PHE A 153 ? 0.1256 0.1887 0.2513 0.0068  -0.0239 -0.0260 139 PHE A O   
1023 C  CB  . PHE A 153 ? 0.1324 0.1642 0.2205 -0.0115 0.0248  -0.0209 139 PHE A CB  
1024 C  CG  . PHE A 153 ? 0.1297 0.1571 0.1879 0.0075  0.0249  -0.0048 139 PHE A CG  
1025 C  CD1 . PHE A 153 ? 0.1161 0.1443 0.2083 0.0109  0.0010  -0.0083 139 PHE A CD1 
1026 C  CD2 . PHE A 153 ? 0.1496 0.1723 0.1760 -0.0149 0.0166  -0.0040 139 PHE A CD2 
1027 C  CE1 . PHE A 153 ? 0.1389 0.1518 0.2120 -0.0123 -0.0270 0.0195  139 PHE A CE1 
1028 C  CE2 . PHE A 153 ? 0.1724 0.1604 0.1831 -0.0246 0.0064  -0.0030 139 PHE A CE2 
1029 C  CZ  . PHE A 153 ? 0.1569 0.1414 0.2328 0.0041  0.0179  0.0124  139 PHE A CZ  
1030 N  N   . PHE A 154 ? 0.1168 0.1504 0.1933 0.0078  0.0011  -0.0095 140 PHE A N   
1031 C  CA  . PHE A 154 ? 0.0948 0.1705 0.1700 0.0234  -0.0039 -0.0078 140 PHE A CA  
1032 C  C   . PHE A 154 ? 0.1201 0.1651 0.1526 0.0031  -0.0179 -0.0272 140 PHE A C   
1033 O  O   . PHE A 154 ? 0.1044 0.1679 0.1555 0.0136  -0.0076 -0.0010 140 PHE A O   
1034 C  CB  . PHE A 154 ? 0.1581 0.2032 0.1560 0.0211  -0.0114 -0.0116 140 PHE A CB  
1035 C  CG  . PHE A 154 ? 0.1613 0.1635 0.1686 0.0176  -0.0203 -0.0090 140 PHE A CG  
1036 C  CD1 . PHE A 154 ? 0.1478 0.1666 0.1616 -0.0048 0.0148  -0.0055 140 PHE A CD1 
1037 C  CD2 . PHE A 154 ? 0.1651 0.1664 0.1339 0.0281  0.0025  -0.0113 140 PHE A CD2 
1038 C  CE1 . PHE A 154 ? 0.1739 0.1820 0.1604 0.0138  -0.0006 0.0015  140 PHE A CE1 
1039 C  CE2 . PHE A 154 ? 0.1802 0.1398 0.1254 0.0054  -0.0141 -0.0063 140 PHE A CE2 
1040 C  CZ  . PHE A 154 ? 0.1656 0.1729 0.1432 -0.0021 0.0272  -0.0309 140 PHE A CZ  
1041 N  N   . ASN A 155 ? 0.1117 0.1461 0.1877 0.0216  0.0004  -0.0147 141 ASN A N   
1042 C  CA  . ASN A 155 ? 0.1268 0.1456 0.1768 0.0175  -0.0077 0.0085  141 ASN A CA  
1043 C  C   . ASN A 155 ? 0.1484 0.1555 0.1531 0.0073  0.0014  -0.0151 141 ASN A C   
1044 O  O   . ASN A 155 ? 0.1369 0.1701 0.1641 0.0102  -0.0036 0.0182  141 ASN A O   
1045 C  CB  . ASN A 155 ? 0.1482 0.1771 0.2023 0.0067  0.0408  -0.0005 141 ASN A CB  
1046 C  CG  . ASN A 155 ? 0.2836 0.2378 0.2792 0.0271  0.0657  -0.0434 141 ASN A CG  
1047 O  OD1 . ASN A 155 ? 0.2006 0.2473 0.2266 0.0436  0.0241  0.0323  141 ASN A OD1 
1048 N  ND2 . ASN A 155 ? 0.2679 0.3878 0.4440 0.1030  0.1086  0.0533  141 ASN A ND2 
1049 N  N   . THR A 156 ? 0.1493 0.1587 0.1411 0.0182  -0.0090 -0.0016 142 THR A N   
1050 C  CA  . THR A 156 ? 0.1411 0.1588 0.1568 0.0173  -0.0073 -0.0029 142 THR A CA  
1051 C  C   . THR A 156 ? 0.1712 0.1615 0.1397 0.0141  0.0077  0.0000  142 THR A C   
1052 O  O   . THR A 156 ? 0.1959 0.1615 0.1609 0.0033  0.0247  0.0025  142 THR A O   
1053 C  CB  . THR A 156 ? 0.1257 0.1647 0.1647 0.0257  0.0014  -0.0077 142 THR A CB  
1054 O  OG1 . THR A 156 ? 0.1362 0.1828 0.1401 0.0162  0.0027  0.0065  142 THR A OG1 
1055 C  CG2 . THR A 156 ? 0.1666 0.1426 0.1519 0.0262  -0.0088 0.0129  142 THR A CG2 
1056 N  N   . THR A 157 ? 0.1738 0.1712 0.1660 -0.0116 0.0244  -0.0071 143 THR A N   
1057 C  CA  . THR A 157 ? 0.1599 0.1622 0.1853 0.0023  0.0101  -0.0087 143 THR A CA  
1058 C  C   . THR A 157 ? 0.1636 0.1628 0.1679 -0.0120 -0.0061 -0.0099 143 THR A C   
1059 O  O   . THR A 157 ? 0.1580 0.1544 0.1589 0.0003  -0.0003 -0.0016 143 THR A O   
1060 C  CB  . THR A 157 ? 0.1370 0.1702 0.2325 0.0125  0.0150  -0.0161 143 THR A CB  
1061 O  OG1 . THR A 157 ? 0.1660 0.2055 0.1970 0.0134  0.0036  -0.0274 143 THR A OG1 
1062 C  CG2 . THR A 157 ? 0.1959 0.1659 0.1653 0.0214  0.0087  -0.0222 143 THR A CG2 
1063 N  N   . HIS A 158 ? 0.1737 0.1917 0.1603 -0.0107 0.0347  0.0018  144 HIS A N   
1064 C  CA  . HIS A 158 ? 0.1917 0.1560 0.1397 0.0099  -0.0022 -0.0129 144 HIS A CA  
1065 C  C   . HIS A 158 ? 0.1813 0.1902 0.1890 0.0016  0.0064  0.0012  144 HIS A C   
1066 O  O   . HIS A 158 ? 0.2450 0.2505 0.1929 0.0166  0.0124  -0.0319 144 HIS A O   
1067 C  CB  . HIS A 158 ? 0.2411 0.1659 0.1996 -0.0033 -0.0143 -0.0088 144 HIS A CB  
1068 C  CG  . HIS A 158 ? 0.2083 0.1860 0.1534 -0.0332 -0.0324 -0.0384 144 HIS A CG  
1069 N  ND1 . HIS A 158 ? 0.2076 0.2040 0.2143 0.0026  -0.0103 -0.0163 144 HIS A ND1 
1070 C  CD2 . HIS A 158 ? 0.2452 0.2589 0.3592 0.0372  -0.0451 0.1094  144 HIS A CD2 
1071 C  CE1 . HIS A 158 ? 0.2613 0.2247 0.3384 -0.0168 -0.0769 0.0199  144 HIS A CE1 
1072 N  NE2 . HIS A 158 ? 0.2695 0.2661 0.2319 -0.0092 -0.0112 0.0574  144 HIS A NE2 
1073 N  N   . SER A 159 ? 0.2033 0.2207 0.1403 -0.0099 0.0129  -0.0142 145 SER A N   
1074 C  CA  . SER A 159 ? 0.2448 0.2250 0.1528 -0.0075 0.0354  -0.0017 145 SER A CA  
1075 C  C   . SER A 159 ? 0.2341 0.1680 0.1606 0.0034  0.0560  -0.0018 145 SER A C   
1076 O  O   . SER A 159 ? 0.3193 0.1822 0.1692 -0.0101 0.0481  -0.0140 145 SER A O   
1077 C  CB  . SER A 159 ? 0.2558 0.2558 0.1488 -0.0592 -0.0073 0.0034  145 SER A CB  
1078 O  OG  . SER A 159 ? 0.2714 0.3853 0.2849 -0.0451 -0.0577 0.0136  145 SER A OG  
1079 N  N   . ILE A 160 ? 0.2127 0.1636 0.1724 -0.0156 0.0353  -0.0158 146 ILE A N   
1080 C  CA  . ILE A 160 ? 0.1881 0.1811 0.1897 0.0049  0.0433  -0.0184 146 ILE A CA  
1081 C  C   . ILE A 160 ? 0.1945 0.1708 0.2056 0.0230  0.0115  -0.0108 146 ILE A C   
1082 O  O   . ILE A 160 ? 0.2356 0.1949 0.1866 -0.0290 0.0370  -0.0094 146 ILE A O   
1083 C  CB  . ILE A 160 ? 0.2347 0.1725 0.1951 -0.0260 0.0501  -0.0019 146 ILE A CB  
1084 C  CG1 . ILE A 160 ? 0.2384 0.1749 0.2199 0.0075  0.0320  0.0040  146 ILE A CG1 
1085 C  CG2 . ILE A 160 ? 0.2452 0.2048 0.1860 -0.0022 0.0297  -0.0077 146 ILE A CG2 
1086 C  CD1 . ILE A 160 ? 0.2696 0.1879 0.2226 0.0079  0.0573  -0.0083 146 ILE A CD1 
1087 N  N   . PRO A 161 ? 0.2310 0.2341 0.1952 -0.0340 0.0409  -0.0667 147 PRO A N   
1088 C  CA  . PRO A 161 ? 0.2029 0.2939 0.2243 -0.0185 0.0498  -0.0102 147 PRO A CA  
1089 C  C   . PRO A 161 ? 0.1485 0.1707 0.1667 -0.0097 0.0253  -0.0157 147 PRO A C   
1090 O  O   . PRO A 161 ? 0.2732 0.2189 0.1887 -0.0279 0.0521  -0.0083 147 PRO A O   
1091 C  CB  . PRO A 161 ? 0.2326 0.3607 0.2114 -0.0233 0.0231  -0.0064 147 PRO A CB  
1092 C  CG  . PRO A 161 ? 0.2083 0.2762 0.2065 -0.0077 0.0390  0.0030  147 PRO A CG  
1093 C  CD  . PRO A 161 ? 0.1973 0.2551 0.1910 -0.0307 0.0380  -0.0167 147 PRO A CD  
1094 N  N   . ASP A 162 ? 0.1568 0.2983 0.2304 -0.0288 0.0745  -0.0356 148 ASP A N   
1095 C  CA  . ASP A 162 ? 0.2964 0.1882 0.2330 -0.0597 0.0186  -0.0782 148 ASP A CA  
1096 C  C   . ASP A 162 ? 0.2252 0.1634 0.2657 0.0642  0.1170  0.0478  148 ASP A C   
1097 O  O   . ASP A 162 ? 0.1993 0.1931 0.2226 -0.0392 0.0021  0.0268  148 ASP A O   
1098 C  CB  . ASP A 162 ? 0.3276 0.2623 0.3475 -0.0710 0.0402  0.0390  148 ASP A CB  
1099 C  CG  . ASP A 162 ? 0.5667 1.1447 0.7626 -0.3169 -0.0513 -0.1823 148 ASP A CG  
1100 O  OD1 . ASP A 162 ? 0.5240 0.5469 0.4880 -0.0793 -0.0270 -0.0275 148 ASP A OD1 
1101 O  OD2 . ASP A 162 ? 1.4932 0.8757 0.6298 -0.0577 0.2034  0.1698  148 ASP A OD2 
1102 N  N   . SER A 163 ? 0.1873 0.1893 0.1610 -0.0248 0.0201  -0.0284 149 SER A N   
1103 C  CA  . SER A 163 ? 0.1478 0.1619 0.1427 0.0133  0.0097  -0.0045 149 SER A CA  
1104 C  C   . SER A 163 ? 0.1461 0.1470 0.1404 -0.0100 -0.0035 0.0008  149 SER A C   
1105 O  O   . SER A 163 ? 0.1501 0.1524 0.1538 0.0147  0.0037  -0.0047 149 SER A O   
1106 C  CB  . SER A 163 ? 0.1691 0.1558 0.1724 0.0012  -0.0060 0.0113  149 SER A CB  
1107 O  OG  . SER A 163 ? 0.1743 0.2031 0.1851 0.0122  0.0055  -0.0090 149 SER A OG  
1108 N  N   . LEU A 164 ? 0.1330 0.1611 0.1553 0.0200  -0.0050 0.0142  150 LEU A N   
1109 C  CA  . LEU A 164 ? 0.1187 0.1365 0.1445 0.0172  0.0063  0.0186  150 LEU A CA  
1110 C  C   . LEU A 164 ? 0.0973 0.1848 0.1360 -0.0025 0.0045  -0.0138 150 LEU A C   
1111 O  O   . LEU A 164 ? 0.1224 0.2085 0.1652 0.0073  -0.0103 -0.0036 150 LEU A O   
1112 C  CB  . LEU A 164 ? 0.1162 0.1387 0.1506 0.0065  0.0013  -0.0044 150 LEU A CB  
1113 C  CG  . LEU A 164 ? 0.1378 0.1235 0.1872 -0.0027 0.0055  0.0207  150 LEU A CG  
1114 C  CD1 . LEU A 164 ? 0.1456 0.1716 0.2035 -0.0122 0.0118  0.0204  150 LEU A CD1 
1115 C  CD2 . LEU A 164 ? 0.1113 0.1515 0.1865 0.0176  0.0297  0.0185  150 LEU A CD2 
1116 N  N   . GLY A 165 ? 0.1206 0.1351 0.1317 0.0090  0.0056  -0.0078 151 GLY A N   
1117 C  CA  . GLY A 165 ? 0.1092 0.1385 0.1177 0.0105  0.0131  0.0202  151 GLY A CA  
1118 C  C   . GLY A 165 ? 0.1038 0.1379 0.1325 0.0036  0.0122  0.0170  151 GLY A C   
1119 O  O   . GLY A 165 ? 0.1202 0.1400 0.1681 -0.0045 0.0012  -0.0068 151 GLY A O   
1120 N  N   . VAL A 166 ? 0.1155 0.1162 0.1619 0.0020  0.0117  -0.0013 152 VAL A N   
1121 C  CA  . VAL A 166 ? 0.1093 0.1299 0.1590 -0.0143 -0.0011 -0.0007 152 VAL A CA  
1122 C  C   . VAL A 166 ? 0.1200 0.1486 0.1634 0.0073  0.0062  -0.0140 152 VAL A C   
1123 O  O   . VAL A 166 ? 0.1565 0.1708 0.1560 -0.0123 0.0176  -0.0182 152 VAL A O   
1124 C  CB  . VAL A 166 ? 0.1132 0.1241 0.1631 0.0020  -0.0013 -0.0006 152 VAL A CB  
1125 C  CG1 . VAL A 166 ? 0.1415 0.1523 0.2064 -0.0008 -0.0249 0.0001  152 VAL A CG1 
1126 C  CG2 . VAL A 166 ? 0.1521 0.1307 0.1760 -0.0376 -0.0020 0.0310  152 VAL A CG2 
1127 N  N   . CYS A 167 ? 0.1448 0.1528 0.1618 -0.0115 0.0029  -0.0106 153 CYS A N   
1128 C  CA  . CYS A 167 ? 0.1296 0.1573 0.1878 0.0209  -0.0251 0.0026  153 CYS A CA  
1129 C  C   . CYS A 167 ? 0.1783 0.1577 0.1857 -0.0317 0.0120  -0.0146 153 CYS A C   
1130 O  O   . CYS A 167 ? 0.1462 0.1681 0.2010 -0.0197 0.0119  -0.0207 153 CYS A O   
1131 C  CB  . CYS A 167 ? 0.1168 0.2566 0.1758 -0.0137 -0.0445 -0.0065 153 CYS A CB  
1132 S  SG  . CYS A 167 ? 0.1857 0.2154 0.2201 0.0078  -0.0262 -0.0097 153 CYS A SG  
1133 N  N   . ILE A 168 ? 0.1321 0.1299 0.1857 -0.0064 -0.0098 -0.0283 154 ILE A N   
1134 C  CA  . ILE A 168 ? 0.1621 0.1507 0.2012 -0.0066 -0.0031 0.0127  154 ILE A CA  
1135 C  C   . ILE A 168 ? 0.1351 0.1418 0.1906 -0.0083 -0.0129 -0.0198 154 ILE A C   
1136 O  O   . ILE A 168 ? 0.1749 0.1539 0.1842 -0.0264 -0.0117 -0.0242 154 ILE A O   
1137 C  CB  . ILE A 168 ? 0.1138 0.1480 0.1687 0.0067  0.0085  -0.0097 154 ILE A CB  
1138 C  CG1 . ILE A 168 ? 0.1334 0.1676 0.1880 -0.0186 -0.0138 0.0211  154 ILE A CG1 
1139 C  CG2 . ILE A 168 ? 0.1683 0.1641 0.2233 0.0054  -0.0130 -0.0295 154 ILE A CG2 
1140 C  CD1 . ILE A 168 ? 0.1775 0.1681 0.1851 -0.0036 -0.0262 -0.0249 154 ILE A CD1 
1141 N  N   . HIS A 169 ? 0.1538 0.1880 0.1812 -0.0040 -0.0183 -0.0202 155 HIS A N   
1142 C  CA  . HIS A 169 ? 0.1624 0.1769 0.1676 0.0010  -0.0273 -0.0291 155 HIS A CA  
1143 C  C   . HIS A 169 ? 0.1738 0.1759 0.1752 -0.0123 0.0096  -0.0150 155 HIS A C   
1144 O  O   . HIS A 169 ? 0.2316 0.1949 0.2221 0.0071  -0.0130 -0.0216 155 HIS A O   
1145 C  CB  . HIS A 169 ? 0.1546 0.2206 0.2155 -0.0114 -0.0139 -0.0336 155 HIS A CB  
1146 C  CG  . HIS A 169 ? 0.1697 0.2230 0.2060 0.0213  -0.0350 -0.0305 155 HIS A CG  
1147 N  ND1 . HIS A 169 ? 0.2837 0.2791 0.2350 0.0586  -0.0154 -0.0269 155 HIS A ND1 
1148 C  CD2 . HIS A 169 ? 0.1788 0.2249 0.2703 0.0088  -0.0147 -0.0028 155 HIS A CD2 
1149 C  CE1 . HIS A 169 ? 0.2483 0.2452 0.2558 0.0632  0.0027  -0.0199 155 HIS A CE1 
1150 N  NE2 . HIS A 169 ? 0.1864 0.2429 0.2402 0.0082  -0.0043 -0.0048 155 HIS A NE2 
1151 N  N   . THR A 170 ? 0.1908 0.1601 0.1780 -0.0137 -0.0166 -0.0297 156 THR A N   
1152 C  CA  . THR A 170 ? 0.1988 0.1857 0.2108 0.0263  -0.0255 -0.0582 156 THR A CA  
1153 C  C   . THR A 170 ? 0.2082 0.1940 0.2175 0.0266  -0.0504 -0.0460 156 THR A C   
1154 O  O   . THR A 170 ? 0.2079 0.2138 0.2007 0.0003  -0.0339 -0.0369 156 THR A O   
1155 C  CB  . THR A 170 ? 0.1729 0.1962 0.2159 0.0263  -0.0111 -0.0594 156 THR A CB  
1156 O  OG1 . THR A 170 ? 0.1804 0.2189 0.1936 0.0097  -0.0106 -0.0415 156 THR A OG1 
1157 C  CG2 . THR A 170 ? 0.2021 0.1756 0.1884 0.0118  -0.0175 -0.0124 156 THR A CG2 
1158 N  N   . SER A 171 ? 0.2064 0.2454 0.2208 0.0345  -0.0274 -0.0469 157 SER A N   
1159 C  CA  . SER A 171 ? 0.1963 0.2554 0.2061 0.0493  -0.0412 -0.0706 157 SER A CA  
1160 C  C   . SER A 171 ? 0.2116 0.2456 0.2193 -0.0005 -0.0234 -0.0359 157 SER A C   
1161 O  O   . SER A 171 ? 0.2719 0.2789 0.2013 0.0126  -0.0699 -0.0228 157 SER A O   
1162 C  CB  . SER A 171 ? 0.2979 0.3217 0.2183 0.0612  -0.0125 -0.0721 157 SER A CB  
1163 O  OG  . SER A 171 ? 0.3445 0.3032 0.2668 0.0458  -0.0693 -0.1222 157 SER A OG  
1164 N  N   . TYR A 172 ? 0.2037 0.2188 0.1907 0.0244  -0.0106 -0.0404 158 TYR A N   
1165 C  CA  . TYR A 172 ? 0.1794 0.2348 0.1705 0.0197  -0.0396 -0.0495 158 TYR A CA  
1166 C  C   . TYR A 172 ? 0.1862 0.2365 0.2084 -0.0091 -0.0589 -0.0094 158 TYR A C   
1167 O  O   . TYR A 172 ? 0.2762 0.2540 0.1605 0.0175  -0.0149 -0.0224 158 TYR A O   
1168 C  CB  . TYR A 172 ? 0.1966 0.2520 0.1708 0.0157  -0.0244 -0.0519 158 TYR A CB  
1169 C  CG  . TYR A 172 ? 0.1975 0.2320 0.1864 0.0055  0.0058  -0.0384 158 TYR A CG  
1170 C  CD1 . TYR A 172 ? 0.2198 0.2246 0.1895 0.0277  -0.0433 -0.0257 158 TYR A CD1 
1171 C  CD2 . TYR A 172 ? 0.2227 0.2311 0.2328 0.0133  -0.0410 -0.0180 158 TYR A CD2 
1172 C  CE1 . TYR A 172 ? 0.2041 0.2433 0.1887 0.0192  -0.0197 -0.0567 158 TYR A CE1 
1173 C  CE2 . TYR A 172 ? 0.2121 0.2513 0.2048 -0.0089 -0.0487 -0.0065 158 TYR A CE2 
1174 C  CZ  . TYR A 172 ? 0.2061 0.2321 0.2125 0.0186  -0.0163 -0.0739 158 TYR A CZ  
1175 O  OH  . TYR A 172 ? 0.2045 0.2591 0.2038 0.0210  -0.0179 -0.0600 158 TYR A OH  
1176 N  N   . GLY A 173 ? 0.1941 0.2058 0.2193 0.0087  -0.0551 -0.0332 159 GLY A N   
1177 C  CA  . GLY A 173 ? 0.1823 0.2419 0.1734 0.0354  -0.0264 -0.0257 159 GLY A CA  
1178 C  C   . GLY A 173 ? 0.1859 0.1847 0.1822 0.0335  -0.0549 -0.0106 159 GLY A C   
1179 O  O   . GLY A 173 ? 0.2134 0.2035 0.2067 0.0484  -0.0451 -0.0250 159 GLY A O   
1180 N  N   . SER A 174 ? 0.1786 0.1891 0.1949 0.0148  -0.0191 -0.0367 160 SER A N   
1181 C  CA  A SER A 174 ? 0.1475 0.1851 0.1925 0.0162  -0.0278 -0.0497 160 SER A CA  
1182 C  CA  B SER A 174 ? 0.1414 0.1858 0.1929 0.0220  -0.0274 -0.0510 160 SER A CA  
1183 C  C   . SER A 174 ? 0.1317 0.1574 0.1390 0.0147  0.0067  -0.0270 160 SER A C   
1184 O  O   . SER A 174 ? 0.1757 0.1760 0.1612 0.0153  -0.0404 -0.0007 160 SER A O   
1185 C  CB  A SER A 174 ? 0.1401 0.2075 0.1709 0.0167  -0.0256 -0.0172 160 SER A CB  
1186 C  CB  B SER A 174 ? 0.1309 0.2407 0.1831 0.0156  -0.0226 -0.0158 160 SER A CB  
1187 O  OG  A SER A 174 ? 0.1799 0.2373 0.1975 0.0017  -0.0077 -0.0542 160 SER A OG  
1188 O  OG  B SER A 174 ? 0.1414 0.1771 0.1807 0.0053  -0.0182 -0.0159 160 SER A OG  
1189 N  N   . ILE A 175 ? 0.1332 0.1479 0.1388 0.0005  0.0001  -0.0072 161 ILE A N   
1190 C  CA  . ILE A 175 ? 0.1296 0.1495 0.1394 0.0029  -0.0076 -0.0190 161 ILE A CA  
1191 C  C   . ILE A 175 ? 0.1290 0.1480 0.1367 0.0042  -0.0016 0.0062  161 ILE A C   
1192 O  O   . ILE A 175 ? 0.1532 0.1435 0.1488 0.0071  -0.0140 -0.0086 161 ILE A O   
1193 C  CB  . ILE A 175 ? 0.1451 0.1692 0.1409 0.0187  -0.0260 -0.0025 161 ILE A CB  
1194 C  CG1 . ILE A 175 ? 0.1603 0.1845 0.1560 0.0525  -0.0311 -0.0051 161 ILE A CG1 
1195 C  CG2 . ILE A 175 ? 0.1481 0.1588 0.1641 0.0246  -0.0263 -0.0077 161 ILE A CG2 
1196 C  CD1 . ILE A 175 ? 0.1897 0.2029 0.1826 0.0184  -0.0281 -0.0185 161 ILE A CD1 
1197 N  N   . VAL A 176 ? 0.1188 0.1501 0.1364 0.0015  0.0080  -0.0132 162 VAL A N   
1198 C  CA  . VAL A 176 ? 0.1693 0.1441 0.1539 -0.0063 -0.0016 0.0004  162 VAL A CA  
1199 C  C   . VAL A 176 ? 0.1200 0.1261 0.1280 0.0067  -0.0062 -0.0139 162 VAL A C   
1200 O  O   . VAL A 176 ? 0.1435 0.1590 0.1271 -0.0004 0.0087  0.0142  162 VAL A O   
1201 C  CB  . VAL A 176 ? 0.1216 0.1524 0.1571 0.0161  -0.0064 0.0042  162 VAL A CB  
1202 C  CG1 . VAL A 176 ? 0.1406 0.1529 0.1834 0.0295  0.0204  0.0093  162 VAL A CG1 
1203 C  CG2 . VAL A 176 ? 0.1721 0.1551 0.1747 0.0202  -0.0045 -0.0207 162 VAL A CG2 
1204 N  N   . TYR A 177 ? 0.1026 0.1222 0.1423 -0.0023 -0.0004 0.0010  163 TYR A N   
1205 C  CA  . TYR A 177 ? 0.1208 0.1188 0.1450 -0.0008 0.0065  0.0016  163 TYR A CA  
1206 C  C   . TYR A 177 ? 0.1221 0.1246 0.1058 0.0054  0.0111  0.0080  163 TYR A C   
1207 O  O   . TYR A 177 ? 0.1259 0.1226 0.1604 -0.0126 0.0145  0.0044  163 TYR A O   
1208 C  CB  . TYR A 177 ? 0.1193 0.1219 0.1618 0.0028  0.0225  0.0189  163 TYR A CB  
1209 C  CG  . TYR A 177 ? 0.0999 0.1139 0.1386 0.0226  -0.0001 0.0135  163 TYR A CG  
1210 C  CD1 . TYR A 177 ? 0.1223 0.1583 0.1407 0.0044  -0.0038 0.0120  163 TYR A CD1 
1211 C  CD2 . TYR A 177 ? 0.1269 0.1295 0.1353 0.0087  0.0011  0.0022  163 TYR A CD2 
1212 C  CE1 . TYR A 177 ? 0.1120 0.1549 0.1639 -0.0060 0.0061  0.0081  163 TYR A CE1 
1213 C  CE2 . TYR A 177 ? 0.1340 0.1344 0.1359 0.0287  0.0150  0.0016  163 TYR A CE2 
1214 C  CZ  . TYR A 177 ? 0.1185 0.1475 0.1331 0.0146  -0.0204 0.0115  163 TYR A CZ  
1215 O  OH  . TYR A 177 ? 0.1392 0.1757 0.1599 0.0021  -0.0095 0.0163  163 TYR A OH  
1216 N  N   . THR A 178 ? 0.1070 0.1217 0.1616 0.0082  0.0136  -0.0074 164 THR A N   
1217 C  CA  . THR A 178 ? 0.1223 0.1235 0.1801 0.0201  0.0128  0.0021  164 THR A CA  
1218 C  C   . THR A 178 ? 0.1312 0.1321 0.1708 0.0066  0.0153  -0.0062 164 THR A C   
1219 O  O   . THR A 178 ? 0.1381 0.1474 0.1683 0.0103  0.0318  0.0108  164 THR A O   
1220 C  CB  . THR A 178 ? 0.1521 0.1290 0.1523 0.0213  0.0115  0.0068  164 THR A CB  
1221 O  OG1 . THR A 178 ? 0.1268 0.1296 0.1563 0.0130  0.0085  0.0212  164 THR A OG1 
1222 C  CG2 . THR A 178 ? 0.1436 0.1405 0.1812 0.0129  0.0085  0.0019  164 THR A CG2 
1223 N  N   . GLY A 179 ? 0.1348 0.1159 0.1484 0.0267  0.0022  0.0033  165 GLY A N   
1224 C  CA  . GLY A 179 ? 0.1662 0.1416 0.1633 0.0264  0.0231  0.0228  165 GLY A CA  
1225 C  C   . GLY A 179 ? 0.1493 0.1485 0.1471 0.0016  0.0137  0.0210  165 GLY A C   
1226 O  O   . GLY A 179 ? 0.1716 0.1726 0.1679 -0.0084 0.0160  0.0174  165 GLY A O   
1227 N  N   . GLU A 180 ? 0.1451 0.1205 0.1577 -0.0061 -0.0004 0.0184  166 GLU A N   
1228 C  CA  . GLU A 180 ? 0.1513 0.1386 0.1466 -0.0003 0.0183  0.0187  166 GLU A CA  
1229 C  C   . GLU A 180 ? 0.1298 0.1342 0.1423 0.0182  0.0063  0.0169  166 GLU A C   
1230 O  O   . GLU A 180 ? 0.1436 0.1470 0.1722 0.0076  0.0243  0.0153  166 GLU A O   
1231 C  CB  . GLU A 180 ? 0.1625 0.1309 0.2085 -0.0163 -0.0005 0.0238  166 GLU A CB  
1232 C  CG  . GLU A 180 ? 0.2274 0.1734 0.3076 -0.0038 -0.0374 0.0682  166 GLU A CG  
1233 C  CD  . GLU A 180 ? 0.2081 0.1074 0.2646 0.0174  -0.0461 0.0338  166 GLU A CD  
1234 O  OE1 . GLU A 180 ? 0.2343 0.2739 0.1567 0.0117  -0.0335 -0.0128 166 GLU A OE1 
1235 O  OE2 . GLU A 180 ? 0.2353 0.2151 0.2467 0.0108  0.0170  -0.0004 166 GLU A OE2 
1236 N  N   . PHE A 181 ? 0.1240 0.1319 0.1700 0.0032  0.0037  0.0081  167 PHE A N   
1237 C  CA  . PHE A 181 ? 0.1383 0.1276 0.1359 0.0012  0.0067  0.0106  167 PHE A CA  
1238 C  C   . PHE A 181 ? 0.1487 0.1362 0.1357 0.0107  0.0078  -0.0023 167 PHE A C   
1239 O  O   . PHE A 181 ? 0.1515 0.1366 0.1639 0.0024  -0.0019 0.0174  167 PHE A O   
1240 C  CB  . PHE A 181 ? 0.1753 0.1176 0.1585 0.0225  -0.0009 0.0080  167 PHE A CB  
1241 C  CG  . PHE A 181 ? 0.1256 0.1329 0.1276 0.0124  -0.0032 0.0009  167 PHE A CG  
1242 C  CD1 . PHE A 181 ? 0.1489 0.1170 0.1383 0.0203  -0.0014 0.0191  167 PHE A CD1 
1243 C  CD2 . PHE A 181 ? 0.1710 0.1402 0.1398 0.0634  -0.0061 0.0120  167 PHE A CD2 
1244 C  CE1 . PHE A 181 ? 0.1562 0.1365 0.1263 0.0406  0.0175  0.0051  167 PHE A CE1 
1245 C  CE2 . PHE A 181 ? 0.1693 0.1537 0.1338 0.0203  -0.0081 -0.0007 167 PHE A CE2 
1246 C  CZ  . PHE A 181 ? 0.1629 0.1455 0.1375 0.0001  0.0162  0.0177  167 PHE A CZ  
1247 N  N   . LYS A 182 ? 0.1620 0.1373 0.1495 0.0045  0.0068  0.0101  168 LYS A N   
1248 C  CA  . LYS A 182 ? 0.1652 0.1386 0.1625 -0.0271 0.0021  0.0177  168 LYS A CA  
1249 C  C   . LYS A 182 ? 0.1671 0.1508 0.1596 0.0161  0.0028  0.0164  168 LYS A C   
1250 O  O   . LYS A 182 ? 0.1790 0.1561 0.1657 0.0211  0.0055  0.0189  168 LYS A O   
1251 C  CB  . LYS A 182 ? 0.1705 0.1684 0.2141 -0.0025 0.0027  0.0238  168 LYS A CB  
1252 C  CG  . LYS A 182 ? 0.2513 0.1695 0.1890 0.0302  0.0065  -0.0144 168 LYS A CG  
1253 C  CD  . LYS A 182 ? 0.2647 0.2239 0.2416 0.0255  0.0283  -0.0289 168 LYS A CD  
1254 C  CE  . LYS A 182 ? 0.2986 0.1726 0.2884 0.0544  0.0094  -0.0001 168 LYS A CE  
1255 N  NZ  . LYS A 182 ? 0.2686 0.2122 0.2457 0.0618  -0.0019 -0.0150 168 LYS A NZ  
1256 N  N   . PHE A 183 ? 0.1947 0.1518 0.1613 0.0173  0.0187  0.0135  169 PHE A N   
1257 C  CA  . PHE A 183 ? 0.1798 0.1541 0.1404 0.0375  0.0141  -0.0113 169 PHE A CA  
1258 C  C   . PHE A 183 ? 0.2024 0.1651 0.1991 0.0166  -0.0006 0.0151  169 PHE A C   
1259 O  O   . PHE A 183 ? 0.2418 0.1956 0.2350 0.0389  0.0279  -0.0280 169 PHE A O   
1260 C  CB  . PHE A 183 ? 0.1831 0.1742 0.1737 0.0451  -0.0107 0.0309  169 PHE A CB  
1261 C  CG  . PHE A 183 ? 0.1846 0.1500 0.1641 0.0210  -0.0057 0.0091  169 PHE A CG  
1262 C  CD1 . PHE A 183 ? 0.1784 0.1976 0.1547 0.0120  -0.0021 0.0063  169 PHE A CD1 
1263 C  CD2 . PHE A 183 ? 0.1569 0.1941 0.2057 0.0032  0.0024  -0.0112 169 PHE A CD2 
1264 C  CE1 . PHE A 183 ? 0.1845 0.1865 0.1885 -0.0013 -0.0152 0.0005  169 PHE A CE1 
1265 C  CE2 . PHE A 183 ? 0.1801 0.1966 0.2123 0.0620  -0.0019 -0.0027 169 PHE A CE2 
1266 C  CZ  . PHE A 183 ? 0.2191 0.1717 0.2056 0.0449  -0.0004 -0.0364 169 PHE A CZ  
1267 N  N   . ASP A 184 ? 0.2256 0.1588 0.2032 0.0414  0.0064  0.0064  170 ASP A N   
1268 C  CA  . ASP A 184 ? 0.2362 0.1533 0.1973 0.0487  0.0183  0.0104  170 ASP A CA  
1269 C  C   . ASP A 184 ? 0.2380 0.1823 0.2307 0.0278  0.0046  0.0097  170 ASP A C   
1270 O  O   . ASP A 184 ? 0.2029 0.2152 0.2612 0.0681  0.0094  0.0149  170 ASP A O   
1271 C  CB  . ASP A 184 ? 0.2072 0.2274 0.1963 0.0709  -0.0180 -0.0131 170 ASP A CB  
1272 C  CG  . ASP A 184 ? 0.2195 0.2401 0.2368 0.0891  -0.0375 -0.0356 170 ASP A CG  
1273 O  OD1 . ASP A 184 ? 0.2361 0.3118 0.2673 0.1030  -0.0220 -0.0454 170 ASP A OD1 
1274 O  OD2 . ASP A 184 ? 0.2270 0.2705 0.2037 0.0632  -0.0133 -0.0457 170 ASP A OD2 
1275 N  N   . GLN A 185 ? 0.2036 0.1880 0.2106 0.0351  -0.0159 0.0112  171 GLN A N   
1276 C  CA  . GLN A 185 ? 0.2215 0.2450 0.1889 0.0114  -0.0288 -0.0046 171 GLN A CA  
1277 C  C   . GLN A 185 ? 0.2678 0.2008 0.2813 0.0017  -0.0274 -0.0404 171 GLN A C   
1278 O  O   . GLN A 185 ? 0.2206 0.4139 0.3131 0.0314  0.0339  -0.0226 171 GLN A O   
1279 C  CB  . GLN A 185 ? 0.2397 0.2483 0.2156 0.0303  -0.0177 -0.0022 171 GLN A CB  
1280 C  CG  . GLN A 185 ? 0.2746 0.3400 0.3093 0.0580  0.0214  -0.0138 171 GLN A CG  
1281 C  CD  . GLN A 185 ? 0.2303 0.2601 0.3363 -0.0162 0.0516  0.0727  171 GLN A CD  
1282 O  OE1 . GLN A 185 ? 0.3209 0.3681 0.2578 0.0449  0.0462  0.0203  171 GLN A OE1 
1283 N  NE2 . GLN A 185 ? 0.2667 0.3111 0.3076 0.0028  -0.0349 0.0584  171 GLN A NE2 
1284 N  N   . SER A 186 ? 0.2314 0.2445 0.2293 0.0840  0.0135  -0.0172 172 SER A N   
1285 C  CA  . SER A 186 ? 0.2133 0.3107 0.2676 0.0974  0.0574  -0.0262 172 SER A CA  
1286 C  C   . SER A 186 ? 0.2726 0.2775 0.2360 0.0858  0.0200  -0.0428 172 SER A C   
1287 O  O   . SER A 186 ? 0.4482 0.4263 0.2437 0.1539  0.0540  -0.0156 172 SER A O   
1288 C  CB  . SER A 186 ? 0.2560 0.2967 0.2806 0.1190  -0.0184 -0.0505 172 SER A CB  
1289 O  OG  . SER A 186 ? 0.2513 0.3037 0.2876 0.1308  -0.0284 -0.0256 172 SER A OG  
1290 N  N   . LEU A 187 ? 0.2476 0.2936 0.2785 0.0657  0.0291  -0.0196 173 LEU A N   
1291 C  CA  . LEU A 187 ? 0.2650 0.3651 0.2226 0.0791  0.0368  -0.0067 173 LEU A CA  
1292 C  C   . LEU A 187 ? 0.2373 0.3453 0.2654 0.0407  -0.0136 0.0132  173 LEU A C   
1293 O  O   . LEU A 187 ? 0.2663 0.5067 0.2816 -0.0404 -0.0261 0.0062  173 LEU A O   
1294 C  CB  . LEU A 187 ? 0.2063 0.2686 0.2668 0.0291  0.0074  0.0316  173 LEU A CB  
1295 C  CG  . LEU A 187 ? 0.2316 0.2451 0.2108 0.0408  -0.0199 0.0023  173 LEU A CG  
1296 C  CD1 . LEU A 187 ? 0.2469 0.2386 0.2598 0.0726  -0.0333 -0.0055 173 LEU A CD1 
1297 C  CD2 . LEU A 187 ? 0.2169 0.3172 0.2839 0.0545  0.0383  -0.0028 173 LEU A CD2 
1298 N  N   . HIS A 188 ? 0.2502 0.3964 0.3160 0.0087  -0.0068 -0.0180 174 HIS A N   
1299 C  CA  . HIS A 188 ? 0.1825 0.3849 0.4420 0.0074  0.0136  -0.0147 174 HIS A CA  
1300 C  C   . HIS A 188 ? 0.1847 0.3868 0.4005 0.0212  0.0151  -0.0139 174 HIS A C   
1301 O  O   . HIS A 188 ? 0.2187 0.3994 0.2748 -0.0111 0.0330  0.0095  174 HIS A O   
1302 C  CB  . HIS A 188 ? 0.3332 0.5400 0.5966 0.0301  0.0196  0.0443  174 HIS A CB  
1303 C  CG  . HIS A 188 ? 0.2818 0.5403 0.5613 0.1642  0.0082  0.0190  174 HIS A CG  
1304 N  ND1 . HIS A 188 ? 0.4383 0.6444 0.5145 0.1580  0.0012  0.0679  174 HIS A ND1 
1305 C  CD2 . HIS A 188 ? 0.4306 0.7513 0.6892 0.1263  0.0384  0.0781  174 HIS A CD2 
1306 C  CE1 . HIS A 188 ? 0.4514 0.6940 0.7008 0.0281  0.0828  0.1507  174 HIS A CE1 
1307 N  NE2 . HIS A 188 ? 0.3836 0.6053 0.5647 0.0991  0.0116  0.1369  174 HIS A NE2 
1308 N  N   . GLY A 189 ? 0.2029 0.4692 0.4346 -0.0666 -0.0229 0.0220  175 GLY A N   
1309 C  CA  . GLY A 189 ? 0.1803 0.3620 0.5294 0.0320  -0.0176 -0.0339 175 GLY A CA  
1310 C  C   . GLY A 189 ? 0.1703 0.3456 0.3207 0.0105  0.0527  0.0526  175 GLY A C   
1311 O  O   . GLY A 189 ? 0.2379 0.4976 0.2531 -0.0551 0.0191  -0.0060 175 GLY A O   
1312 N  N   . HIS A 190 ? 0.2383 0.3193 0.2915 -0.0420 0.0348  -0.0152 176 HIS A N   
1313 C  CA  . HIS A 190 ? 0.2462 0.3122 0.3313 -0.0385 0.0283  -0.0174 176 HIS A CA  
1314 C  C   . HIS A 190 ? 0.1354 0.2599 0.3076 -0.0214 0.0081  0.0120  176 HIS A C   
1315 O  O   . HIS A 190 ? 0.2182 0.2940 0.3029 -0.0535 0.0903  -0.0245 176 HIS A O   
1316 C  CB  . HIS A 190 ? 0.1940 0.3784 0.2570 -0.0484 0.0690  0.0047  176 HIS A CB  
1317 C  CG  . HIS A 190 ? 0.3243 0.5361 0.4935 0.0081  -0.0117 -0.0263 176 HIS A CG  
1318 N  ND1 . HIS A 190 ? 0.5013 0.4610 0.8765 0.1699  -0.1166 -0.2626 176 HIS A ND1 
1319 C  CD2 . HIS A 190 ? 0.9263 0.2574 0.6154 0.2863  -0.2909 -0.3066 176 HIS A CD2 
1320 C  CE1 . HIS A 190 ? 0.9168 0.3215 0.7764 0.2239  -0.0103 -0.3337 176 HIS A CE1 
1321 N  NE2 . HIS A 190 ? 0.2030 1.2134 1.2533 0.0852  -0.0148 -0.2037 176 HIS A NE2 
1322 N  N   . TYR A 191 ? 0.2018 0.2591 0.1920 -0.0087 0.0496  -0.0432 177 TYR A N   
1323 C  CA  . TYR A 191 ? 0.1567 0.2461 0.2334 0.0042  0.0506  0.0004  177 TYR A CA  
1324 C  C   . TYR A 191 ? 0.1858 0.2530 0.2144 0.0044  0.0113  0.0063  177 TYR A C   
1325 O  O   . TYR A 191 ? 0.1948 0.2568 0.2143 0.0018  0.0211  0.0034  177 TYR A O   
1326 C  CB  . TYR A 191 ? 0.1792 0.3034 0.2271 0.0069  0.0597  -0.0024 177 TYR A CB  
1327 C  CG  . TYR A 191 ? 0.2297 0.2526 0.1925 -0.0007 0.0255  -0.0472 177 TYR A CG  
1328 C  CD1 . TYR A 191 ? 0.1979 0.2271 0.2028 0.0065  0.0170  -0.0251 177 TYR A CD1 
1329 C  CD2 . TYR A 191 ? 0.1954 0.4060 0.1858 -0.0282 -0.0011 -0.0326 177 TYR A CD2 
1330 C  CE1 . TYR A 191 ? 0.2703 0.2109 0.2394 -0.0032 -0.0127 -0.0118 177 TYR A CE1 
1331 C  CE2 . TYR A 191 ? 0.2911 0.4340 0.1509 0.0073  0.0507  -0.0552 177 TYR A CE2 
1332 C  CZ  . TYR A 191 ? 0.3497 0.3242 0.2528 0.0081  -0.0368 -0.0699 177 TYR A CZ  
1333 O  OH  . TYR A 191 ? 0.4277 0.3909 0.2900 -0.0213 -0.1140 -0.0450 177 TYR A OH  
1334 N  N   . ALA A 192 ? 0.1686 0.3002 0.2303 -0.0052 0.0059  -0.0628 178 ALA A N   
1335 C  CA  . ALA A 192 ? 0.1701 0.2980 0.2216 0.0262  0.0327  -0.0515 178 ALA A CA  
1336 C  C   . ALA A 192 ? 0.1841 0.2050 0.1979 0.0331  -0.0154 -0.0265 178 ALA A C   
1337 O  O   . ALA A 192 ? 0.2164 0.2722 0.2200 0.0164  -0.0053 -0.0004 178 ALA A O   
1338 C  CB  . ALA A 192 ? 0.1930 0.3973 0.2710 -0.0016 0.0159  -0.0411 178 ALA A CB  
1339 N  N   . PRO A 193 ? 0.1875 0.2153 0.1646 0.0179  -0.0131 -0.0222 179 PRO A N   
1340 C  CA  . PRO A 193 ? 0.1878 0.2114 0.1745 0.0148  -0.0058 -0.0358 179 PRO A CA  
1341 C  C   . PRO A 193 ? 0.1807 0.1972 0.2104 0.0102  -0.0231 0.0019  179 PRO A C   
1342 O  O   . PRO A 193 ? 0.1756 0.2425 0.2576 0.0416  -0.0236 -0.0369 179 PRO A O   
1343 C  CB  . PRO A 193 ? 0.1912 0.2018 0.2173 0.0202  -0.0056 0.0002  179 PRO A CB  
1344 C  CG  . PRO A 193 ? 0.2020 0.1928 0.2317 -0.0113 -0.0506 -0.0335 179 PRO A CG  
1345 C  CD  . PRO A 193 ? 0.2021 0.2164 0.2169 0.0018  -0.0153 -0.0377 179 PRO A CD  
1346 N  N   . ASP A 194 ? 0.1812 0.1932 0.1927 0.0024  -0.0145 -0.0365 180 ASP A N   
1347 C  CA  . ASP A 194 ? 0.1432 0.1902 0.1907 0.0253  -0.0136 -0.0157 180 ASP A CA  
1348 C  C   . ASP A 194 ? 0.1768 0.1907 0.1996 0.0256  -0.0228 -0.0134 180 ASP A C   
1349 O  O   . ASP A 194 ? 0.1957 0.2325 0.1872 0.0207  -0.0272 -0.0117 180 ASP A O   
1350 C  CB  . ASP A 194 ? 0.1876 0.1849 0.1843 0.0324  -0.0261 0.0028  180 ASP A CB  
1351 C  CG  . ASP A 194 ? 0.1790 0.2093 0.2545 0.0165  -0.0250 0.0000  180 ASP A CG  
1352 O  OD1 . ASP A 194 ? 0.2029 0.3082 0.2794 0.0301  0.0329  0.0225  180 ASP A OD1 
1353 O  OD2 . ASP A 194 ? 0.1506 0.1873 0.2994 0.0134  -0.0437 0.0269  180 ASP A OD2 
1354 N  N   . LEU A 195 ? 0.2123 0.2207 0.1904 0.0309  -0.0194 -0.0095 181 LEU A N   
1355 C  CA  . LEU A 195 ? 0.2042 0.2232 0.1762 0.0490  -0.0323 -0.0046 181 LEU A CA  
1356 C  C   . LEU A 195 ? 0.2043 0.2684 0.1901 0.0490  -0.0208 0.0212  181 LEU A C   
1357 O  O   . LEU A 195 ? 0.2037 0.2377 0.1887 0.0431  -0.0267 -0.0045 181 LEU A O   
1358 C  CB  . LEU A 195 ? 0.2357 0.2345 0.1609 0.0421  -0.0610 0.0093  181 LEU A CB  
1359 C  CG  . LEU A 195 ? 0.3629 0.2892 0.1914 0.0514  -0.0642 0.0264  181 LEU A CG  
1360 C  CD1 . LEU A 195 ? 0.3377 0.2825 0.3521 0.0493  -0.0160 -0.0720 181 LEU A CD1 
1361 C  CD2 . LEU A 195 ? 0.2677 0.2863 0.2813 0.0512  -0.0205 -0.0173 181 LEU A CD2 
1362 N  N   . LYS A 196 ? 0.1989 0.2838 0.1937 0.0558  -0.0202 -0.0331 182 LYS A N   
1363 C  CA  . LYS A 196 ? 0.2350 0.3272 0.2242 0.0333  -0.0393 -0.0337 182 LYS A CA  
1364 C  C   . LYS A 196 ? 0.1764 0.3043 0.2520 0.0355  -0.0086 -0.0257 182 LYS A C   
1365 O  O   . LYS A 196 ? 0.1960 0.3095 0.2201 0.0400  -0.0397 -0.0399 182 LYS A O   
1366 C  CB  . LYS A 196 ? 0.1941 0.3765 0.2388 0.0305  -0.0376 -0.0472 182 LYS A CB  
1367 C  CG  . LYS A 196 ? 0.3834 0.6449 0.4495 0.0096  -0.0205 -0.0870 182 LYS A CG  
1368 C  CD  . LYS A 196 ? 0.2578 0.6911 0.5070 -0.0360 -0.0538 -0.0019 182 LYS A CD  
1369 C  CE  . LYS A 196 ? 0.6918 0.8229 0.4771 -0.0604 -0.1226 0.0043  182 LYS A CE  
1370 N  NZ  . LYS A 196 ? 1.0745 0.7687 0.5117 -0.1098 -0.1979 0.1419  182 LYS A NZ  
1371 N  N   . ARG A 197 ? 0.1888 0.2676 0.2338 0.0121  -0.0029 -0.0316 183 ARG A N   
1372 C  CA  . ARG A 197 ? 0.2464 0.3041 0.2013 -0.0139 -0.0654 -0.0374 183 ARG A CA  
1373 C  C   . ARG A 197 ? 0.1784 0.2359 0.2274 -0.0062 -0.0295 -0.0227 183 ARG A C   
1374 O  O   . ARG A 197 ? 0.1869 0.2427 0.1973 0.0290  -0.0150 -0.0510 183 ARG A O   
1375 C  CB  . ARG A 197 ? 0.2953 0.2938 0.2576 0.0209  -0.0019 -0.0459 183 ARG A CB  
1376 C  CG  . ARG A 197 ? 0.3623 0.3744 0.3017 -0.0458 0.0267  0.0005  183 ARG A CG  
1377 C  CD  . ARG A 197 ? 0.4409 0.5291 0.4727 -0.1400 0.0786  -0.0688 183 ARG A CD  
1378 N  NE  . ARG A 197 ? 0.5053 0.6217 0.5944 -0.2386 -0.0706 -0.0155 183 ARG A NE  
1379 C  CZ  . ARG A 197 ? 0.5054 0.4771 0.4426 -0.0769 0.0122  0.0379  183 ARG A CZ  
1380 N  NH1 . ARG A 197 ? 0.4198 0.5561 0.4177 0.0855  -0.0358 0.0079  183 ARG A NH1 
1381 N  NH2 . ARG A 197 ? 0.3391 0.4845 0.5467 -0.0873 0.1157  0.0287  183 ARG A NH2 
1382 N  N   . MET A 198 ? 0.1908 0.2086 0.1864 0.0108  -0.0144 -0.0190 184 MET A N   
1383 C  CA  . MET A 198 ? 0.1869 0.1844 0.2108 0.0294  0.0058  -0.0182 184 MET A CA  
1384 C  C   . MET A 198 ? 0.1595 0.2229 0.1936 0.0312  -0.0066 -0.0276 184 MET A C   
1385 O  O   . MET A 198 ? 0.1810 0.2406 0.1729 0.0395  -0.0179 -0.0242 184 MET A O   
1386 C  CB  . MET A 198 ? 0.1583 0.2130 0.1889 0.0092  -0.0159 0.0108  184 MET A CB  
1387 C  CG  . MET A 198 ? 0.1594 0.1988 0.2159 0.0176  -0.0214 -0.0432 184 MET A CG  
1388 S  SD  . MET A 198 ? 0.3670 0.4136 0.2237 -0.1279 -0.0689 -0.0091 184 MET A SD  
1389 C  CE  . MET A 198 ? 0.3585 0.2436 0.2875 0.0569  0.1463  0.0266  184 MET A CE  
1390 N  N   . ALA A 199 ? 0.1785 0.2502 0.1973 0.0509  -0.0275 0.0008  185 ALA A N   
1391 C  CA  . ALA A 199 ? 0.1978 0.2347 0.1914 0.0588  -0.0351 -0.0110 185 ALA A CA  
1392 C  C   . ALA A 199 ? 0.1361 0.2449 0.2077 0.0544  -0.0561 0.0220  185 ALA A C   
1393 O  O   . ALA A 199 ? 0.2010 0.2957 0.1688 0.0382  -0.0340 -0.0128 185 ALA A O   
1394 C  CB  . ALA A 199 ? 0.3155 0.2556 0.1704 0.0726  -0.0370 -0.0221 185 ALA A CB  
1395 N  N   . GLU A 200 ? 0.1546 0.2740 0.2033 0.0531  -0.0527 0.0013  186 GLU A N   
1396 C  CA  . GLU A 200 ? 0.1977 0.2527 0.2406 0.0149  -0.0464 -0.0169 186 GLU A CA  
1397 C  C   . GLU A 200 ? 0.1908 0.2529 0.2080 0.0498  -0.0351 -0.0223 186 GLU A C   
1398 O  O   . GLU A 200 ? 0.1711 0.3070 0.2224 0.0500  -0.0579 -0.0193 186 GLU A O   
1399 C  CB  . GLU A 200 ? 0.1750 0.2778 0.2789 0.0370  -0.0403 -0.0427 186 GLU A CB  
1400 C  CG  . GLU A 200 ? 0.2834 0.4096 0.3708 -0.0128 -0.0516 -0.0528 186 GLU A CG  
1401 C  CD  . GLU A 200 ? 0.3791 0.6272 0.4634 0.0179  0.0309  0.0704  186 GLU A CD  
1402 O  OE1 . GLU A 200 ? 0.3707 0.7009 0.8150 0.0473  0.0291  -0.1250 186 GLU A OE1 
1403 O  OE2 . GLU A 200 ? 0.3339 0.5344 0.4393 -0.0902 -0.0610 0.0376  186 GLU A OE2 
1404 N  N   . ILE A 201 ? 0.1756 0.2428 0.1716 0.0336  -0.0378 -0.0413 187 ILE A N   
1405 C  CA  . ILE A 201 ? 0.1672 0.1859 0.2113 0.0349  -0.0445 -0.0140 187 ILE A CA  
1406 C  C   . ILE A 201 ? 0.1560 0.2172 0.1825 0.0285  -0.0465 -0.0074 187 ILE A C   
1407 O  O   . ILE A 201 ? 0.1888 0.2285 0.1907 0.0352  -0.0275 -0.0249 187 ILE A O   
1408 C  CB  . ILE A 201 ? 0.1652 0.2230 0.1723 0.0224  -0.0170 -0.0244 187 ILE A CB  
1409 C  CG1 . ILE A 201 ? 0.1522 0.2210 0.2479 0.0265  -0.0088 -0.0043 187 ILE A CG1 
1410 C  CG2 . ILE A 201 ? 0.1576 0.2036 0.2073 0.0051  -0.0131 -0.0319 187 ILE A CG2 
1411 C  CD1 . ILE A 201 ? 0.2207 0.2625 0.1959 0.0120  -0.0219 0.0314  187 ILE A CD1 
1412 N  N   . GLY A 202 ? 0.1664 0.2211 0.1804 0.0352  -0.0321 0.0033  188 GLY A N   
1413 C  CA  . GLY A 202 ? 0.1897 0.2430 0.1912 0.0363  -0.0094 -0.0313 188 GLY A CA  
1414 C  C   . GLY A 202 ? 0.1817 0.2672 0.1925 0.0616  -0.0215 0.0265  188 GLY A C   
1415 O  O   . GLY A 202 ? 0.2094 0.2680 0.1926 0.0655  -0.0428 0.0090  188 GLY A O   
1416 N  N   . ASP A 203 ? 0.2085 0.2858 0.1788 0.0646  -0.0328 -0.0254 189 ASP A N   
1417 C  CA  . ASP A 203 ? 0.2252 0.3621 0.1538 0.0225  -0.0679 -0.0167 189 ASP A CA  
1418 C  C   . ASP A 203 ? 0.2369 0.2927 0.1595 0.0422  -0.0481 -0.0295 189 ASP A C   
1419 O  O   . ASP A 203 ? 0.2783 0.3543 0.1969 0.0762  -0.0659 -0.0276 189 ASP A O   
1420 C  CB  . ASP A 203 ? 0.2322 0.3726 0.2093 0.0599  -0.0965 -0.0322 189 ASP A CB  
1421 C  CG  . ASP A 203 ? 0.2341 0.3694 0.2724 0.0139  -0.0608 0.0201  189 ASP A CG  
1422 O  OD1 . ASP A 203 ? 0.3338 0.3584 0.3809 0.1337  -0.0121 0.0330  189 ASP A OD1 
1423 O  OD2 . ASP A 203 ? 0.2498 0.5874 0.4134 0.1801  -0.0873 0.0341  189 ASP A OD2 
1424 N  N   . GLU A 204 ? 0.2349 0.2874 0.1974 0.0404  -0.0610 -0.0286 190 GLU A N   
1425 C  CA  . GLU A 204 ? 0.2314 0.2836 0.2415 0.0044  -0.0797 -0.0553 190 GLU A CA  
1426 C  C   . GLU A 204 ? 0.2121 0.2308 0.2532 -0.0003 0.0097  -0.0638 190 GLU A C   
1427 O  O   . GLU A 204 ? 0.3010 0.2695 0.3069 -0.0158 -0.0035 -0.0980 190 GLU A O   
1428 C  CB  . GLU A 204 ? 0.2355 0.2774 0.3088 0.0702  -0.0584 -0.0376 190 GLU A CB  
1429 C  CG  . GLU A 204 ? 0.2752 0.3841 0.3358 0.0091  -0.0520 0.0052  190 GLU A CG  
1430 C  CD  . GLU A 204 ? 0.3833 0.5383 0.5221 0.0269  -0.1118 0.1362  190 GLU A CD  
1431 O  OE1 . GLU A 204 ? 0.4153 0.5695 0.7118 -0.0335 0.0664  0.0512  190 GLU A OE1 
1432 O  OE2 . GLU A 204 ? 0.5036 0.8252 0.5416 -0.0842 -0.0500 0.3866  190 GLU A OE2 
1433 N  N   . GLY A 205 ? 0.2026 0.2557 0.1834 0.0048  -0.0585 -0.0533 191 GLY A N   
1434 C  CA  . GLY A 205 ? 0.2170 0.2442 0.1891 0.0393  -0.0390 -0.0249 191 GLY A CA  
1435 C  C   . GLY A 205 ? 0.1756 0.2091 0.1943 0.0311  -0.0324 -0.0066 191 GLY A C   
1436 O  O   . GLY A 205 ? 0.1908 0.2012 0.2266 -0.0013 -0.0461 -0.0097 191 GLY A O   
1437 N  N   . VAL A 206 ? 0.1750 0.1801 0.1731 0.0326  -0.0274 -0.0093 192 VAL A N   
1438 C  CA  . VAL A 206 ? 0.1729 0.1856 0.1435 0.0185  -0.0357 -0.0047 192 VAL A CA  
1439 C  C   . VAL A 206 ? 0.1584 0.1655 0.1469 0.0116  0.0014  0.0013  192 VAL A C   
1440 O  O   . VAL A 206 ? 0.1925 0.1880 0.1666 0.0269  -0.0039 -0.0093 192 VAL A O   
1441 C  CB  . VAL A 206 ? 0.1594 0.1817 0.1852 0.0077  -0.0038 -0.0412 192 VAL A CB  
1442 C  CG1 . VAL A 206 ? 0.1643 0.1979 0.1466 0.0459  0.0015  -0.0272 192 VAL A CG1 
1443 C  CG2 . VAL A 206 ? 0.1557 0.1961 0.1617 0.0198  -0.0212 -0.0304 192 VAL A CG2 
1444 N  N   . PHE A 207 ? 0.1510 0.1779 0.1770 0.0052  -0.0137 -0.0171 193 PHE A N   
1445 C  CA  . PHE A 207 ? 0.1488 0.1781 0.1631 0.0236  -0.0009 -0.0094 193 PHE A CA  
1446 C  C   . PHE A 207 ? 0.1304 0.1621 0.1498 0.0256  -0.0053 -0.0100 193 PHE A C   
1447 O  O   . PHE A 207 ? 0.1947 0.2001 0.1351 0.0038  0.0098  -0.0140 193 PHE A O   
1448 C  CB  . PHE A 207 ? 0.1834 0.1899 0.1745 0.0107  -0.0207 -0.0177 193 PHE A CB  
1449 C  CG  . PHE A 207 ? 0.2386 0.1843 0.1789 -0.0011 -0.0104 -0.0370 193 PHE A CG  
1450 C  CD1 . PHE A 207 ? 0.2466 0.2608 0.2552 0.0470  0.0043  0.0079  193 PHE A CD1 
1451 C  CD2 . PHE A 207 ? 0.2285 0.2479 0.2931 0.0641  0.0253  -0.0350 193 PHE A CD2 
1452 C  CE1 . PHE A 207 ? 0.2612 0.2566 0.3351 0.0577  0.0986  -0.0466 193 PHE A CE1 
1453 C  CE2 . PHE A 207 ? 0.2429 0.3049 0.3088 0.0863  -0.0191 -0.0024 193 PHE A CE2 
1454 C  CZ  . PHE A 207 ? 0.2271 0.2865 0.3575 0.0977  0.0846  -0.0443 193 PHE A CZ  
1455 N  N   . ALA A 208 ? 0.1780 0.1521 0.1219 0.0128  -0.0003 -0.0079 194 ALA A N   
1456 C  CA  . ALA A 208 ? 0.1686 0.1683 0.1334 0.0053  -0.0093 -0.0121 194 ALA A CA  
1457 C  C   . ALA A 208 ? 0.1303 0.1721 0.1200 0.0054  -0.0069 -0.0154 194 ALA A C   
1458 O  O   . ALA A 208 ? 0.1566 0.1698 0.1610 0.0119  0.0003  0.0056  194 ALA A O   
1459 C  CB  . ALA A 208 ? 0.1597 0.1552 0.1411 0.0244  0.0072  -0.0249 194 ALA A CB  
1460 N  N   . LEU A 209 ? 0.1350 0.1538 0.1164 0.0099  0.0168  -0.0130 195 LEU A N   
1461 C  CA  . LEU A 209 ? 0.1239 0.1524 0.1249 0.0155  -0.0073 0.0051  195 LEU A CA  
1462 C  C   . LEU A 209 ? 0.1215 0.1129 0.1307 0.0107  0.0004  0.0073  195 LEU A C   
1463 O  O   . LEU A 209 ? 0.1306 0.1622 0.1279 -0.0043 0.0125  0.0070  195 LEU A O   
1464 C  CB  . LEU A 209 ? 0.1529 0.1524 0.1604 0.0258  0.0089  0.0125  195 LEU A CB  
1465 C  CG  . LEU A 209 ? 0.1517 0.1256 0.1549 0.0319  0.0004  0.0228  195 LEU A CG  
1466 C  CD1 . LEU A 209 ? 0.1455 0.1540 0.1360 0.0208  -0.0087 0.0172  195 LEU A CD1 
1467 C  CD2 . LEU A 209 ? 0.1564 0.1722 0.1595 0.0217  0.0175  0.0208  195 LEU A CD2 
1468 N  N   . ILE A 210 ? 0.1381 0.1314 0.1146 0.0112  -0.0001 0.0011  196 ILE A N   
1469 C  CA  . ILE A 210 ? 0.1107 0.1270 0.1484 0.0082  0.0001  0.0115  196 ILE A CA  
1470 C  C   . ILE A 210 ? 0.1156 0.1240 0.1378 0.0055  0.0158  0.0100  196 ILE A C   
1471 O  O   . ILE A 210 ? 0.1267 0.1129 0.1356 0.0008  0.0091  0.0001  196 ILE A O   
1472 C  CB  . ILE A 210 ? 0.1265 0.1356 0.1615 0.0001  -0.0074 -0.0028 196 ILE A CB  
1473 C  CG1 . ILE A 210 ? 0.1423 0.1370 0.1697 0.0217  0.0403  0.0160  196 ILE A CG1 
1474 C  CG2 . ILE A 210 ? 0.1437 0.1356 0.1339 -0.0007 0.0036  0.0316  196 ILE A CG2 
1475 C  CD1 . ILE A 210 ? 0.1465 0.1300 0.1712 0.0112  -0.0037 -0.0142 196 ILE A CD1 
1476 N  N   . SER A 211 ? 0.1090 0.1062 0.1343 -0.0028 0.0071  0.0015  197 SER A N   
1477 C  CA  . SER A 211 ? 0.1357 0.1257 0.1336 0.0121  0.0060  0.0093  197 SER A CA  
1478 C  C   . SER A 211 ? 0.1251 0.1125 0.1366 0.0036  0.0101  0.0011  197 SER A C   
1479 O  O   . SER A 211 ? 0.1170 0.1341 0.1541 0.0012  0.0096  0.0025  197 SER A O   
1480 C  CB  . SER A 211 ? 0.1210 0.1210 0.1478 0.0358  0.0091  0.0060  197 SER A CB  
1481 O  OG  . SER A 211 ? 0.1443 0.1329 0.1374 0.0135  0.0068  -0.0055 197 SER A OG  
1482 N  N   . ASP A 212 ? 0.1171 0.1248 0.1485 -0.0141 0.0191  -0.0035 198 ASP A N   
1483 C  CA  . ASP A 212 ? 0.1156 0.1116 0.1641 -0.0235 0.0115  -0.0048 198 ASP A CA  
1484 C  C   . ASP A 212 ? 0.1286 0.1160 0.1154 0.0068  -0.0044 0.0134  198 ASP A C   
1485 O  O   . ASP A 212 ? 0.1428 0.1416 0.1689 0.0161  0.0206  0.0299  198 ASP A O   
1486 C  CB  . ASP A 212 ? 0.1284 0.1269 0.1597 -0.0113 -0.0027 -0.0002 198 ASP A CB  
1487 C  CG  . ASP A 212 ? 0.1680 0.1352 0.1565 -0.0007 0.0074  0.0163  198 ASP A CG  
1488 O  OD1 . ASP A 212 ? 0.1639 0.1230 0.1651 0.0108  0.0120  0.0097  198 ASP A OD1 
1489 O  OD2 . ASP A 212 ? 0.1735 0.1259 0.1453 0.0005  0.0235  0.0037  198 ASP A OD2 
1490 N  N   . SER A 213 ? 0.1264 0.1093 0.1351 -0.0078 -0.0034 0.0112  199 SER A N   
1491 C  CA  . SER A 213 ? 0.1403 0.1113 0.1177 -0.0157 0.0113  0.0223  199 SER A CA  
1492 C  C   . SER A 213 ? 0.1461 0.1138 0.1507 -0.0008 0.0052  0.0049  199 SER A C   
1493 O  O   . SER A 213 ? 0.1561 0.1052 0.1680 -0.0148 0.0143  0.0112  199 SER A O   
1494 C  CB  . SER A 213 ? 0.1223 0.1018 0.1657 -0.0139 0.0284  0.0296  199 SER A CB  
1495 O  OG  . SER A 213 ? 0.1324 0.1060 0.1382 0.0089  0.0071  0.0136  199 SER A OG  
1496 N  N   . THR A 214 ? 0.1472 0.0985 0.1359 0.0034  0.0038  0.0000  200 THR A N   
1497 C  CA  . THR A 214 ? 0.1681 0.1215 0.1485 0.0164  -0.0051 0.0066  200 THR A CA  
1498 C  C   . THR A 214 ? 0.1661 0.1165 0.1733 -0.0015 -0.0012 -0.0080 200 THR A C   
1499 O  O   . THR A 214 ? 0.1821 0.1447 0.2153 -0.0016 -0.0247 0.0103  200 THR A O   
1500 C  CB  . THR A 214 ? 0.2103 0.0903 0.1941 0.0147  -0.0006 -0.0166 200 THR A CB  
1501 O  OG1 . THR A 214 ? 0.2284 0.1235 0.1672 -0.0014 -0.0042 0.0156  200 THR A OG1 
1502 C  CG2 . THR A 214 ? 0.2597 0.1146 0.1808 -0.0408 -0.0116 0.0094  200 THR A CG2 
1503 N  N   . GLU A 215 ? 0.1640 0.0908 0.1911 -0.0122 0.0130  0.0071  201 GLU A N   
1504 C  CA  . GLU A 215 ? 0.1836 0.0843 0.1781 -0.0077 0.0076  -0.0024 201 GLU A CA  
1505 C  C   . GLU A 215 ? 0.1546 0.1410 0.1581 0.0138  0.0145  -0.0014 201 GLU A C   
1506 O  O   . GLU A 215 ? 0.1969 0.1276 0.1839 0.0139  0.0056  0.0139  201 GLU A O   
1507 C  CB  . GLU A 215 ? 0.1965 0.1259 0.1681 -0.0051 0.0141  -0.0031 201 GLU A CB  
1508 C  CG  . GLU A 215 ? 0.2130 0.1309 0.2252 0.0078  0.0127  -0.0004 201 GLU A CG  
1509 C  CD  . GLU A 215 ? 0.3330 0.2523 0.2467 0.0301  0.0089  -0.0439 201 GLU A CD  
1510 O  OE1 . GLU A 215 ? 0.5162 0.3039 0.3165 -0.0807 -0.1047 -0.0464 201 GLU A OE1 
1511 O  OE2 . GLU A 215 ? 0.3953 0.2437 0.3513 -0.0763 -0.0037 -0.0033 201 GLU A OE2 
1512 N  N   . ALA A 216 ? 0.1842 0.1177 0.1700 -0.0009 0.0152  -0.0127 202 ALA A N   
1513 C  CA  . ALA A 216 ? 0.1566 0.1293 0.1992 -0.0011 0.0068  -0.0124 202 ALA A CA  
1514 C  C   . ALA A 216 ? 0.1969 0.1331 0.1740 -0.0093 0.0084  0.0001  202 ALA A C   
1515 O  O   . ALA A 216 ? 0.2242 0.1490 0.2071 -0.0153 0.0070  0.0244  202 ALA A O   
1516 C  CB  . ALA A 216 ? 0.1866 0.1194 0.1544 0.0030  0.0477  0.0152  202 ALA A CB  
1517 N  N   . GLU A 217 ? 0.2323 0.1213 0.2183 -0.0300 0.0318  0.0239  203 GLU A N   
1518 C  CA  . GLU A 217 ? 0.2630 0.1422 0.2030 -0.0454 0.0553  0.0318  203 GLU A CA  
1519 C  C   . GLU A 217 ? 0.2011 0.1510 0.3064 -0.0152 0.0075  0.0223  203 GLU A C   
1520 O  O   . GLU A 217 ? 0.2776 0.1281 0.3728 -0.0457 0.0298  0.0364  203 GLU A O   
1521 C  CB  . GLU A 217 ? 0.2352 0.1244 0.2801 -0.0309 0.0172  0.0125  203 GLU A CB  
1522 C  CG  . GLU A 217 ? 0.2465 0.1730 0.2892 -0.0231 0.0144  0.0093  203 GLU A CG  
1523 C  CD  . GLU A 217 ? 0.3027 0.2568 0.2343 -0.0363 0.0272  -0.0044 203 GLU A CD  
1524 O  OE1 . GLU A 217 ? 0.2948 0.2117 0.2996 -0.0510 0.0309  0.0356  203 GLU A OE1 
1525 O  OE2 . GLU A 217 ? 0.2788 0.3629 0.3524 -0.0478 0.0314  0.0682  203 GLU A OE2 
1526 N  N   . LYS A 218 ? 0.2703 0.1029 0.2697 0.0105  0.0343  0.0000  204 LYS A N   
1527 C  CA  . LYS A 218 ? 0.2449 0.1400 0.2884 -0.0169 0.0073  -0.0057 204 LYS A CA  
1528 C  C   . LYS A 218 ? 0.2467 0.1256 0.2874 -0.0099 0.0020  0.0148  204 LYS A C   
1529 O  O   . LYS A 218 ? 0.2404 0.1441 0.2275 -0.0134 -0.0049 0.0133  204 LYS A O   
1530 C  CB  . LYS A 218 ? 0.2528 0.1396 0.2456 0.0107  0.0145  -0.0151 204 LYS A CB  
1531 C  CG  . LYS A 218 ? 0.3825 0.1948 0.2736 0.0140  0.0063  0.0067  204 LYS A CG  
1532 C  CD  . LYS A 218 ? 0.3022 0.2769 0.4739 0.0004  -0.0172 0.0252  204 LYS A CD  
1533 C  CE  . LYS A 218 ? 0.4381 0.3884 0.4038 0.0447  0.0698  -0.1064 204 LYS A CE  
1534 N  NZ  . LYS A 218 ? 0.6727 0.3962 0.5669 0.0320  0.0699  -0.1087 204 LYS A NZ  
1535 N  N   . PRO A 219 ? 0.2717 0.1400 0.2901 -0.0038 0.0138  0.0374  205 PRO A N   
1536 C  CA  . PRO A 219 ? 0.2591 0.1721 0.2856 -0.0002 0.0077  0.0258  205 PRO A CA  
1537 C  C   . PRO A 219 ? 0.2548 0.1067 0.2467 0.0223  0.0157  0.0429  205 PRO A C   
1538 O  O   . PRO A 219 ? 0.3074 0.1641 0.2418 0.0274  0.0132  0.0206  205 PRO A O   
1539 C  CB  . PRO A 219 ? 0.3413 0.1364 0.2665 0.0043  0.0422  0.0735  205 PRO A CB  
1540 C  CG  . PRO A 219 ? 0.3396 0.2043 0.3618 -0.0158 -0.0154 0.0149  205 PRO A CG  
1541 C  CD  . PRO A 219 ? 0.2973 0.1138 0.3583 -0.0210 0.0448  0.0529  205 PRO A CD  
1542 N  N   . GLY A 220 ? 0.2801 0.1546 0.2137 0.0043  0.0223  0.0382  206 GLY A N   
1543 C  CA  . GLY A 220 ? 0.2509 0.1561 0.1765 0.0065  0.0094  0.0265  206 GLY A CA  
1544 C  C   . GLY A 220 ? 0.2574 0.1629 0.1628 0.0229  0.0144  0.0191  206 GLY A C   
1545 O  O   . GLY A 220 ? 0.2480 0.1337 0.1812 0.0459  0.0022  0.0233  206 GLY A O   
1546 N  N   . TYR A 221 ? 0.2664 0.1240 0.2243 0.0203  0.0453  0.0159  207 TYR A N   
1547 C  CA  . TYR A 221 ? 0.2299 0.1460 0.2000 0.0032  -0.0035 0.0199  207 TYR A CA  
1548 C  C   . TYR A 221 ? 0.2734 0.1566 0.2218 0.0206  -0.0095 -0.0125 207 TYR A C   
1549 O  O   . TYR A 221 ? 0.2861 0.1747 0.2006 0.0138  -0.0079 -0.0020 207 TYR A O   
1550 C  CB  . TYR A 221 ? 0.2287 0.1627 0.2095 0.0470  0.0156  0.0198  207 TYR A CB  
1551 C  CG  . TYR A 221 ? 0.2056 0.1700 0.2288 0.0538  -0.0024 0.0259  207 TYR A CG  
1552 C  CD1 . TYR A 221 ? 0.2407 0.1823 0.2357 0.0515  -0.0116 0.0277  207 TYR A CD1 
1553 C  CD2 . TYR A 221 ? 0.2181 0.2168 0.2106 0.0655  0.0240  -0.0117 207 TYR A CD2 
1554 C  CE1 . TYR A 221 ? 0.2300 0.2356 0.2045 0.0692  0.0123  0.0282  207 TYR A CE1 
1555 C  CE2 . TYR A 221 ? 0.2838 0.1868 0.2130 0.0566  0.0063  0.0056  207 TYR A CE2 
1556 C  CZ  . TYR A 221 ? 0.2370 0.2568 0.1950 0.0862  0.0205  -0.0055 207 TYR A CZ  
1557 O  OH  . TYR A 221 ? 0.3256 0.3243 0.2083 0.1103  -0.0156 -0.0452 207 TYR A OH  
1558 N  N   . ASN A 222 ? 0.2754 0.1414 0.2006 0.0368  0.0309  0.0137  208 ASN A N   
1559 C  CA  . ASN A 222 ? 0.2692 0.1911 0.2101 0.0536  0.0050  0.0312  208 ASN A CA  
1560 C  C   . ASN A 222 ? 0.3033 0.1828 0.2172 -0.0015 -0.0217 0.0087  208 ASN A C   
1561 O  O   . ASN A 222 ? 0.2604 0.1952 0.2005 0.0441  0.0032  -0.0156 208 ASN A O   
1562 C  CB  . ASN A 222 ? 0.2458 0.1704 0.2462 0.0463  0.0049  0.0244  208 ASN A CB  
1563 C  CG  . ASN A 222 ? 0.2543 0.1963 0.1804 0.0389  -0.0049 0.0086  208 ASN A CG  
1564 O  OD1 . ASN A 222 ? 0.3399 0.1964 0.2555 0.0133  0.0090  -0.0043 208 ASN A OD1 
1565 N  ND2 . ASN A 222 ? 0.2916 0.1954 0.2033 0.0053  -0.0184 0.0337  208 ASN A ND2 
1566 N  N   . THR A 223 ? 0.2645 0.2326 0.1829 0.0145  -0.0179 -0.0001 209 THR A N   
1567 C  CA  . THR A 223 ? 0.3171 0.2064 0.2184 0.0487  -0.0222 0.0514  209 THR A CA  
1568 C  C   . THR A 223 ? 0.2832 0.2515 0.2034 0.0459  0.0141  -0.0278 209 THR A C   
1569 O  O   . THR A 223 ? 0.3036 0.1673 0.1975 0.0634  -0.0280 0.0201  209 THR A O   
1570 C  CB  . THR A 223 ? 0.3137 0.2134 0.2335 0.0327  -0.0031 0.0198  209 THR A CB  
1571 O  OG1 . THR A 223 ? 0.3610 0.2068 0.2407 -0.0005 0.0035  -0.0140 209 THR A OG1 
1572 C  CG2 . THR A 223 ? 0.3532 0.2122 0.2314 0.0265  0.0081  0.0148  209 THR A CG2 
1573 N  N   . PRO A 224 ? 0.2496 0.2225 0.1544 0.0471  -0.0032 0.0054  210 PRO A N   
1574 C  CA  . PRO A 224 ? 0.2416 0.2383 0.1776 0.0569  -0.0173 0.0057  210 PRO A CA  
1575 C  C   . PRO A 224 ? 0.2614 0.1963 0.2095 0.0318  -0.0397 -0.0353 210 PRO A C   
1576 O  O   . PRO A 224 ? 0.3185 0.2242 0.1114 0.0917  0.0041  -0.0358 210 PRO A O   
1577 C  CB  . PRO A 224 ? 0.3028 0.2966 0.2188 0.0968  0.0002  -0.0048 210 PRO A CB  
1578 C  CG  . PRO A 224 ? 0.2672 0.2671 0.2604 0.0778  0.0222  0.0101  210 PRO A CG  
1579 C  CD  . PRO A 224 ? 0.3665 0.2220 0.1915 0.0306  -0.0167 0.0542  210 PRO A CD  
1580 N  N   . GLU A 225 ? 0.2643 0.1803 0.1793 0.0478  -0.0060 -0.0279 211 GLU A N   
1581 C  CA  . GLU A 225 ? 0.2697 0.1864 0.1553 0.0522  0.0053  -0.0154 211 GLU A CA  
1582 C  C   . GLU A 225 ? 0.2401 0.2231 0.1748 0.0613  0.0033  0.0185  211 GLU A C   
1583 O  O   . GLU A 225 ? 0.2827 0.1959 0.1594 0.0701  -0.0013 -0.0262 211 GLU A O   
1584 C  CB  . GLU A 225 ? 0.2895 0.2360 0.1682 0.0745  0.0115  -0.0092 211 GLU A CB  
1585 C  CG  . GLU A 225 ? 0.2627 0.2181 0.1895 0.0818  -0.0108 -0.0467 211 GLU A CG  
1586 C  CD  . GLU A 225 ? 0.2976 0.2105 0.1957 0.0512  0.0058  -0.0239 211 GLU A CD  
1587 O  OE1 . GLU A 225 ? 0.2573 0.2366 0.2000 0.0350  -0.0329 0.0210  211 GLU A OE1 
1588 O  OE2 . GLU A 225 ? 0.3155 0.2612 0.2232 0.0878  0.0486  -0.0010 211 GLU A OE2 
1589 N  N   . ASN A 226 ? 0.2660 0.2254 0.1748 0.0695  0.0021  -0.0166 212 ASN A N   
1590 C  CA  . ASN A 226 ? 0.2628 0.2487 0.2044 0.1110  -0.0156 -0.0556 212 ASN A CA  
1591 C  C   . ASN A 226 ? 0.2384 0.2232 0.2474 0.1323  -0.0017 0.0095  212 ASN A C   
1592 O  O   . ASN A 226 ? 0.3322 0.2536 0.2051 0.1395  -0.0099 -0.0656 212 ASN A O   
1593 C  CB  . ASN A 226 ? 0.2416 0.2598 0.2132 0.0663  0.0138  -0.0566 212 ASN A CB  
1594 C  CG  . ASN A 226 ? 0.2620 0.3191 0.2409 0.0922  -0.0424 -0.0322 212 ASN A CG  
1595 O  OD1 . ASN A 226 ? 0.3169 0.2989 0.2550 0.1225  -0.0250 0.0408  212 ASN A OD1 
1596 N  ND2 . ASN A 226 ? 0.3418 0.2644 0.2812 0.1143  -0.0318 -0.0145 212 ASN A ND2 
1597 N  N   . ILE A 227 ? 0.2966 0.2281 0.2011 0.1030  0.0017  0.0117  213 ILE A N   
1598 C  CA  . ILE A 227 ? 0.3272 0.2707 0.1611 0.0823  -0.0155 -0.0138 213 ILE A CA  
1599 C  C   . ILE A 227 ? 0.2999 0.1907 0.2414 0.0620  -0.0428 -0.0246 213 ILE A C   
1600 O  O   . ILE A 227 ? 0.3042 0.1986 0.2068 0.0941  -0.0425 -0.0088 213 ILE A O   
1601 C  CB  . ILE A 227 ? 0.3137 0.1820 0.2246 0.1009  -0.0095 -0.0318 213 ILE A CB  
1602 C  CG1 . ILE A 227 ? 0.3697 0.2343 0.2202 0.1165  -0.0665 -0.0195 213 ILE A CG1 
1603 C  CG2 . ILE A 227 ? 0.3327 0.1967 0.2132 0.0673  -0.0095 -0.0023 213 ILE A CG2 
1604 C  CD1 . ILE A 227 ? 0.4657 0.2328 0.2568 0.1370  -0.0741 0.0091  213 ILE A CD1 
1605 N  N   . ILE A 228 ? 0.2859 0.1908 0.1892 0.0794  -0.0143 -0.0176 214 ILE A N   
1606 C  CA  . ILE A 228 ? 0.2551 0.1746 0.1876 0.0796  0.0283  -0.0079 214 ILE A CA  
1607 C  C   . ILE A 228 ? 0.2281 0.1559 0.2229 0.0618  0.0173  -0.0034 214 ILE A C   
1608 O  O   . ILE A 228 ? 0.2029 0.1900 0.2067 0.0758  0.0038  -0.0055 214 ILE A O   
1609 C  CB  . ILE A 228 ? 0.2711 0.1973 0.1559 0.0606  0.0337  0.0110  214 ILE A CB  
1610 C  CG1 . ILE A 228 ? 0.3234 0.2165 0.1488 0.1049  0.0301  0.0231  214 ILE A CG1 
1611 C  CG2 . ILE A 228 ? 0.2484 0.1854 0.1793 0.0597  0.0452  0.0026  214 ILE A CG2 
1612 C  CD1 . ILE A 228 ? 0.3552 0.3238 0.3691 0.0466  -0.0113 -0.0459 214 ILE A CD1 
1613 N  N   . GLU A 229 ? 0.2244 0.1650 0.1792 0.0576  0.0001  0.0031  215 GLU A N   
1614 C  CA  . GLU A 229 ? 0.2551 0.2018 0.1756 0.0778  0.0182  0.0194  215 GLU A CA  
1615 C  C   . GLU A 229 ? 0.3105 0.1906 0.1892 0.0868  -0.0340 0.0101  215 GLU A C   
1616 O  O   . GLU A 229 ? 0.2307 0.2327 0.1845 0.0757  -0.0173 -0.0370 215 GLU A O   
1617 C  CB  . GLU A 229 ? 0.2793 0.2659 0.1784 0.0849  -0.0090 -0.0009 215 GLU A CB  
1618 C  CG  . GLU A 229 ? 0.2464 0.2293 0.2251 0.0634  0.0177  0.0254  215 GLU A CG  
1619 C  CD  . GLU A 229 ? 0.2746 0.3617 0.2998 0.0501  -0.0068 -0.0322 215 GLU A CD  
1620 O  OE1 . GLU A 229 ? 0.3376 0.4917 0.3088 0.0591  -0.0333 -0.0679 215 GLU A OE1 
1621 O  OE2 . GLU A 229 ? 0.3395 0.3936 0.2810 0.0376  -0.0059 -0.0155 215 GLU A OE2 
1622 N  N   . HIS A 230 ? 0.2753 0.2075 0.1963 0.0671  -0.0105 -0.0275 216 HIS A N   
1623 C  CA  . HIS A 230 ? 0.2934 0.1938 0.2200 0.1112  0.0026  -0.0559 216 HIS A CA  
1624 C  C   . HIS A 230 ? 0.2446 0.2026 0.2588 0.0699  -0.0166 -0.0047 216 HIS A C   
1625 O  O   . HIS A 230 ? 0.2915 0.2235 0.2274 0.0810  -0.0242 -0.0344 216 HIS A O   
1626 C  CB  . HIS A 230 ? 0.3441 0.1643 0.2938 0.1049  -0.0219 -0.0236 216 HIS A CB  
1627 C  CG  . HIS A 230 ? 0.3887 0.2989 0.3654 0.0203  -0.0320 0.0084  216 HIS A CG  
1628 N  ND1 . HIS A 230 ? 0.4388 0.4176 0.4624 0.0635  -0.1199 0.0014  216 HIS A ND1 
1629 C  CD2 . HIS A 230 ? 0.2763 0.5423 0.4988 0.0546  -0.1283 0.1607  216 HIS A CD2 
1630 C  CE1 . HIS A 230 ? 0.5359 0.5302 0.4841 -0.0569 -0.1993 0.0272  216 HIS A CE1 
1631 N  NE2 . HIS A 230 ? 0.4606 0.5040 0.5240 -0.0604 -0.1663 0.0332  216 HIS A NE2 
1632 N  N   . HIS A 231 ? 0.2454 0.2269 0.1709 0.0429  -0.0069 0.0000  217 HIS A N   
1633 C  CA  . HIS A 231 ? 0.2845 0.1878 0.1940 0.0755  0.0307  -0.0309 217 HIS A CA  
1634 C  C   . HIS A 231 ? 0.2444 0.2095 0.2432 0.0607  -0.0018 0.0070  217 HIS A C   
1635 O  O   . HIS A 231 ? 0.2474 0.2073 0.2582 0.0461  -0.0247 0.0030  217 HIS A O   
1636 C  CB  . HIS A 231 ? 0.3642 0.2817 0.2446 0.0803  -0.0616 0.0112  217 HIS A CB  
1637 C  CG  . HIS A 231 ? 0.4313 0.2813 0.3204 -0.0103 -0.0725 0.0651  217 HIS A CG  
1638 N  ND1 . HIS A 231 ? 0.5515 0.3653 0.3628 -0.0229 -0.0294 0.1115  217 HIS A ND1 
1639 C  CD2 . HIS A 231 ? 0.6024 0.2702 0.2411 -0.0534 -0.0681 0.0474  217 HIS A CD2 
1640 C  CE1 . HIS A 231 ? 0.5866 0.2967 0.5856 0.0052  -0.0702 -0.0254 217 HIS A CE1 
1641 N  NE2 . HIS A 231 ? 0.6345 0.3650 0.3494 -0.0023 -0.0601 0.0781  217 HIS A NE2 
1642 N  N   . MET A 232 ? 0.2560 0.2125 0.1703 0.0496  -0.0191 -0.0283 218 MET A N   
1643 C  CA  . MET A 232 ? 0.2339 0.2160 0.1676 0.0335  -0.0041 -0.0191 218 MET A CA  
1644 C  C   . MET A 232 ? 0.1801 0.2454 0.1598 0.0369  -0.0274 -0.0221 218 MET A C   
1645 O  O   . MET A 232 ? 0.2103 0.1846 0.2139 0.0885  -0.0383 -0.0262 218 MET A O   
1646 C  CB  . MET A 232 ? 0.2196 0.1949 0.1958 0.0504  0.0021  -0.0268 218 MET A CB  
1647 C  CG  . MET A 232 ? 0.2894 0.2429 0.1864 0.0712  0.0393  0.0311  218 MET A CG  
1648 S  SD  . MET A 232 ? 0.2520 0.2128 0.2004 0.0672  -0.0123 -0.0075 218 MET A SD  
1649 C  CE  . MET A 232 ? 0.2619 0.2515 0.1552 0.0737  -0.0167 -0.0028 218 MET A CE  
1650 N  N   . TYR A 233 ? 0.1967 0.2293 0.1825 0.0536  -0.0389 -0.0353 219 TYR A N   
1651 C  CA  . TYR A 233 ? 0.2054 0.2152 0.1907 0.0361  -0.0138 -0.0124 219 TYR A CA  
1652 C  C   . TYR A 233 ? 0.1879 0.2269 0.2254 0.0650  0.0069  -0.0030 219 TYR A C   
1653 O  O   . TYR A 233 ? 0.2343 0.2179 0.2219 0.0848  -0.0271 -0.0251 219 TYR A O   
1654 C  CB  . TYR A 233 ? 0.2143 0.2541 0.1585 0.0454  -0.0183 -0.0252 219 TYR A CB  
1655 C  CG  . TYR A 233 ? 0.1883 0.2068 0.2199 0.0581  -0.0228 -0.0284 219 TYR A CG  
1656 C  CD1 . TYR A 233 ? 0.1648 0.2217 0.2016 0.0343  -0.0296 0.0207  219 TYR A CD1 
1657 C  CD2 . TYR A 233 ? 0.2188 0.2171 0.2181 0.0499  -0.0125 -0.0049 219 TYR A CD2 
1658 C  CE1 . TYR A 233 ? 0.1838 0.2278 0.2252 0.0653  -0.0275 0.0063  219 TYR A CE1 
1659 C  CE2 . TYR A 233 ? 0.1962 0.2214 0.2130 0.0434  -0.0025 -0.0010 219 TYR A CE2 
1660 C  CZ  . TYR A 233 ? 0.1768 0.2412 0.2008 0.0660  -0.0350 -0.0103 219 TYR A CZ  
1661 O  OH  . TYR A 233 ? 0.2175 0.2267 0.2695 0.0654  0.0068  -0.0364 219 TYR A OH  
1662 N  N   . ASP A 234 ? 0.2109 0.2075 0.2015 0.0589  -0.0233 -0.0188 220 ASP A N   
1663 C  CA  . ASP A 234 ? 0.2568 0.2077 0.2370 0.0394  -0.0362 -0.0020 220 ASP A CA  
1664 C  C   . ASP A 234 ? 0.2636 0.2137 0.2349 0.0563  -0.0475 -0.0170 220 ASP A C   
1665 O  O   . ASP A 234 ? 0.2557 0.2380 0.2768 0.0944  -0.0739 -0.0340 220 ASP A O   
1666 C  CB  . ASP A 234 ? 0.2254 0.2730 0.2915 0.0199  -0.0516 -0.0158 220 ASP A CB  
1667 C  CG  . ASP A 234 ? 0.2902 0.3767 0.3446 0.0977  0.0258  0.0489  220 ASP A CG  
1668 O  OD1 . ASP A 234 ? 0.2702 0.3622 0.3765 0.1017  -0.0369 0.0749  220 ASP A OD1 
1669 O  OD2 . ASP A 234 ? 0.4192 0.4292 0.3178 0.0729  -0.0901 0.0690  220 ASP A OD2 
1670 N  N   . ALA A 235 ? 0.2614 0.2142 0.2363 0.0497  -0.0500 -0.0289 221 ALA A N   
1671 C  CA  . ALA A 235 ? 0.2218 0.2464 0.2586 0.0578  -0.0067 -0.0062 221 ALA A CA  
1672 C  C   . ALA A 235 ? 0.1938 0.2373 0.2261 0.0636  -0.0107 -0.0135 221 ALA A C   
1673 O  O   . ALA A 235 ? 0.2423 0.2409 0.2734 0.0351  -0.0755 -0.0127 221 ALA A O   
1674 C  CB  . ALA A 235 ? 0.2604 0.2611 0.2375 0.0750  -0.0300 -0.0232 221 ALA A CB  
1675 N  N   . PHE A 236 ? 0.1937 0.2168 0.2148 0.0616  -0.0347 -0.0068 222 PHE A N   
1676 C  CA  . PHE A 236 ? 0.2310 0.2167 0.1815 0.0523  -0.0329 -0.0173 222 PHE A CA  
1677 C  C   . PHE A 236 ? 0.2346 0.2332 0.2039 0.0855  -0.0446 -0.0291 222 PHE A C   
1678 O  O   . PHE A 236 ? 0.2593 0.2385 0.2037 0.0881  -0.0366 -0.0369 222 PHE A O   
1679 C  CB  . PHE A 236 ? 0.1782 0.2019 0.1860 0.0619  -0.0211 -0.0172 222 PHE A CB  
1680 C  CG  . PHE A 236 ? 0.1860 0.2167 0.1955 0.0662  -0.0194 0.0139  222 PHE A CG  
1681 C  CD1 . PHE A 236 ? 0.2562 0.1977 0.2162 0.1105  -0.0271 -0.0017 222 PHE A CD1 
1682 C  CD2 . PHE A 236 ? 0.2223 0.2154 0.2217 0.0612  -0.0095 -0.0022 222 PHE A CD2 
1683 C  CE1 . PHE A 236 ? 0.2809 0.2271 0.1777 0.0976  -0.0084 0.0089  222 PHE A CE1 
1684 C  CE2 . PHE A 236 ? 0.2750 0.2186 0.2620 0.0339  -0.0624 -0.0182 222 PHE A CE2 
1685 C  CZ  . PHE A 236 ? 0.2737 0.2233 0.2096 0.0923  -0.0318 -0.0546 222 PHE A CZ  
1686 N  N   . ALA A 237 ? 0.2102 0.2151 0.2344 0.0874  -0.0718 -0.0442 223 ALA A N   
1687 C  CA  . ALA A 237 ? 0.2722 0.2667 0.2855 0.1073  -0.0137 -0.0442 223 ALA A CA  
1688 C  C   . ALA A 237 ? 0.2322 0.2666 0.2454 0.1080  -0.0229 -0.0200 223 ALA A C   
1689 O  O   . ALA A 237 ? 0.3207 0.2751 0.2667 0.1018  -0.0286 -0.0734 223 ALA A O   
1690 C  CB  . ALA A 237 ? 0.2588 0.2463 0.2683 0.1268  -0.0417 -0.0351 223 ALA A CB  
1691 N  N   . LYS A 238 ? 0.3000 0.1914 0.2955 0.0813  -0.0388 -0.0314 224 LYS A N   
1692 C  CA  . LYS A 238 ? 0.3235 0.1913 0.2960 0.0293  -0.0326 -0.0391 224 LYS A CA  
1693 C  C   . LYS A 238 ? 0.3662 0.2396 0.3059 -0.0047 -0.1026 -0.0262 224 LYS A C   
1694 O  O   . LYS A 238 ? 0.3275 0.2766 0.3921 0.0058  -0.0678 -0.0467 224 LYS A O   
1695 C  CB  . LYS A 238 ? 0.4511 0.2218 0.3290 0.0329  -0.0784 0.0051  224 LYS A CB  
1696 C  CG  . LYS A 238 ? 0.4680 0.3714 0.4115 0.0796  -0.0570 -0.0108 224 LYS A CG  
1697 C  CD  . LYS A 238 ? 0.5695 0.4221 0.4239 -0.0234 0.0145  0.0922  224 LYS A CD  
1698 C  CE  . LYS A 238 ? 0.6241 0.5756 0.7279 0.0873  -0.0819 0.0808  224 LYS A CE  
1699 N  NZ  . LYS A 238 ? 0.8778 0.9758 0.8583 0.0420  -0.0764 0.1014  224 LYS A NZ  
1700 N  N   . VAL A 239 ? 0.2734 0.2225 0.2103 0.0512  -0.0617 -0.0245 225 VAL A N   
1701 C  CA  . VAL A 239 ? 0.3259 0.2253 0.2479 0.0277  -0.0897 -0.0415 225 VAL A CA  
1702 C  C   . VAL A 239 ? 0.2642 0.2393 0.2363 0.0320  -0.0651 0.0101  225 VAL A C   
1703 O  O   . VAL A 239 ? 0.3178 0.2474 0.2651 0.0737  0.0111  -0.0488 225 VAL A O   
1704 C  CB  . VAL A 239 ? 0.3027 0.1760 0.2234 0.0346  -0.0491 -0.0230 225 VAL A CB  
1705 C  CG1 . VAL A 239 ? 0.3187 0.2084 0.2534 0.0616  -0.0716 -0.0408 225 VAL A CG1 
1706 C  CG2 . VAL A 239 ? 0.2722 0.2550 0.2508 0.0946  -0.0901 -0.0514 225 VAL A CG2 
1707 N  N   . LYS A 240 ? 0.3371 0.2733 0.2999 0.0817  -0.0522 -0.0490 226 LYS A N   
1708 C  CA  . LYS A 240 ? 0.4846 0.2568 0.3247 0.1081  -0.0197 -0.1074 226 LYS A CA  
1709 C  C   . LYS A 240 ? 0.3680 0.2450 0.1977 0.0696  -0.0444 -0.0917 226 LYS A C   
1710 O  O   . LYS A 240 ? 0.4050 0.2870 0.2173 0.0889  -0.0318 -0.0821 226 LYS A O   
1711 C  CB  . LYS A 240 ? 0.4961 0.2701 0.3966 0.0570  -0.0506 -0.1219 226 LYS A CB  
1712 C  CG  . LYS A 240 ? 0.5545 0.2604 0.3546 0.0163  -0.0507 -0.0734 226 LYS A CG  
1713 C  CD  . LYS A 240 ? 0.8982 0.3640 0.5844 -0.0953 -0.1549 0.0113  226 LYS A CD  
1714 C  CE  . LYS A 240 ? 1.1973 0.3739 0.6471 -0.1104 -0.0723 -0.1743 226 LYS A CE  
1715 N  NZ  . LYS A 240 ? 1.2501 0.6195 0.9123 -0.2245 -0.0744 -0.0016 226 LYS A NZ  
1716 N  N   . GLY A 241 ? 0.3325 0.2349 0.2277 0.0595  -0.0089 -0.0440 227 GLY A N   
1717 C  CA  . GLY A 241 ? 0.3182 0.2623 0.2189 0.0528  -0.0432 -0.0532 227 GLY A CA  
1718 C  C   . GLY A 241 ? 0.2759 0.2814 0.2047 0.0751  -0.0378 -0.1035 227 GLY A C   
1719 O  O   . GLY A 241 ? 0.2712 0.2666 0.2313 0.0891  -0.0424 -0.0754 227 GLY A O   
1720 N  N   . ARG A 242 ? 0.2744 0.2653 0.2047 0.0846  -0.0342 -0.0713 228 ARG A N   
1721 C  CA  . ARG A 242 ? 0.2579 0.2707 0.2040 0.0846  -0.0365 -0.0075 228 ARG A CA  
1722 C  C   . ARG A 242 ? 0.2060 0.2053 0.1866 0.0558  0.0043  -0.0191 228 ARG A C   
1723 O  O   . ARG A 242 ? 0.2236 0.2221 0.1702 0.0365  -0.0252 -0.0285 228 ARG A O   
1724 C  CB  . ARG A 242 ? 0.2628 0.2569 0.1851 0.0660  -0.0161 -0.0310 228 ARG A CB  
1725 C  CG  . ARG A 242 ? 0.3590 0.3225 0.1869 0.0885  0.0662  -0.0266 228 ARG A CG  
1726 C  CD  . ARG A 242 ? 0.2727 0.2831 0.2613 0.0537  0.0309  0.0015  228 ARG A CD  
1727 N  NE  . ARG A 242 ? 0.3900 0.2460 0.3030 0.0830  0.0240  0.0349  228 ARG A NE  
1728 C  CZ  . ARG A 242 ? 0.3098 0.3643 0.2910 0.0805  -0.0012 -0.0321 228 ARG A CZ  
1729 N  NH1 . ARG A 242 ? 0.3604 0.3220 0.2881 0.0153  -0.0004 0.0288  228 ARG A NH1 
1730 N  NH2 . ARG A 242 ? 0.2650 0.3262 0.2938 0.0252  0.0230  0.0684  228 ARG A NH2 
1731 N  N   . LEU A 243 ? 0.1968 0.2293 0.1724 0.0352  0.0112  -0.0115 229 LEU A N   
1732 C  CA  . LEU A 243 ? 0.2296 0.2072 0.1813 0.0657  -0.0196 -0.0126 229 LEU A CA  
1733 C  C   . LEU A 243 ? 0.1894 0.2042 0.1607 0.0351  -0.0363 -0.0111 229 LEU A C   
1734 O  O   . LEU A 243 ? 0.2181 0.2051 0.1676 0.0480  -0.0141 -0.0239 229 LEU A O   
1735 C  CB  . LEU A 243 ? 0.2061 0.2021 0.2030 0.0661  -0.0041 -0.0095 229 LEU A CB  
1736 C  CG  . LEU A 243 ? 0.2535 0.2185 0.2111 0.0756  -0.0426 -0.0130 229 LEU A CG  
1737 C  CD1 . LEU A 243 ? 0.2586 0.2008 0.2066 0.0615  -0.0205 -0.0222 229 LEU A CD1 
1738 C  CD2 . LEU A 243 ? 0.2720 0.2718 0.2584 0.0310  -0.0357 0.0479  229 LEU A CD2 
1739 N  N   . ILE A 244 ? 0.2181 0.1900 0.1583 0.0195  -0.0140 -0.0077 230 ILE A N   
1740 C  CA  . ILE A 244 ? 0.2337 0.2025 0.1830 0.0340  -0.0207 -0.0092 230 ILE A CA  
1741 C  C   . ILE A 244 ? 0.1828 0.1987 0.1858 0.0493  -0.0294 0.0093  230 ILE A C   
1742 O  O   . ILE A 244 ? 0.2068 0.1969 0.1984 0.0318  -0.0122 -0.0170 230 ILE A O   
1743 C  CB  . ILE A 244 ? 0.2342 0.2198 0.1744 0.0304  -0.0107 0.0033  230 ILE A CB  
1744 C  CG1 . ILE A 244 ? 0.2475 0.3135 0.2840 0.0712  -0.0647 -0.0177 230 ILE A CG1 
1745 C  CG2 . ILE A 244 ? 0.2531 0.2262 0.2322 0.0588  -0.0273 -0.0293 230 ILE A CG2 
1746 C  CD1 . ILE A 244 ? 0.4254 0.4665 0.3561 0.0031  -0.0802 -0.0646 230 ILE A CD1 
1747 N  N   . VAL A 245 ? 0.2172 0.1822 0.1523 0.0319  -0.0010 -0.0171 231 VAL A N   
1748 C  CA  . VAL A 245 ? 0.2322 0.1918 0.1799 0.0211  -0.0022 -0.0015 231 VAL A CA  
1749 C  C   . VAL A 245 ? 0.2007 0.1882 0.1846 0.0076  -0.0030 0.0020  231 VAL A C   
1750 O  O   . VAL A 245 ? 0.2593 0.2004 0.1826 0.0215  0.0285  -0.0182 231 VAL A O   
1751 C  CB  . VAL A 245 ? 0.2242 0.2137 0.1750 0.0074  0.0016  -0.0071 231 VAL A CB  
1752 C  CG1 . VAL A 245 ? 0.2152 0.2712 0.1669 0.0436  -0.0086 -0.0011 231 VAL A CG1 
1753 C  CG2 . VAL A 245 ? 0.2244 0.2331 0.1874 0.0314  0.0024  -0.0150 231 VAL A CG2 
1754 N  N   . SER A 246 ? 0.2108 0.1525 0.2038 0.0162  0.0184  -0.0047 232 SER A N   
1755 C  CA  . SER A 246 ? 0.2182 0.2128 0.1938 0.0183  0.0262  -0.0307 232 SER A CA  
1756 C  C   . SER A 246 ? 0.2169 0.1750 0.2272 0.0303  -0.0043 -0.0139 232 SER A C   
1757 O  O   . SER A 246 ? 0.2782 0.2096 0.2148 -0.0085 -0.0187 -0.0264 232 SER A O   
1758 C  CB  . SER A 246 ? 0.2232 0.2081 0.2665 0.0489  0.0361  -0.0545 232 SER A CB  
1759 O  OG  . SER A 246 ? 0.2890 0.2795 0.3129 0.0429  -0.0050 -0.0238 232 SER A OG  
1760 N  N   . CYS A 247 ? 0.2457 0.1868 0.2366 -0.0020 0.0012  -0.0236 233 CYS A N   
1761 C  CA  . CYS A 247 ? 0.2289 0.1964 0.2839 -0.0001 -0.0321 -0.0116 233 CYS A CA  
1762 C  C   . CYS A 247 ? 0.2585 0.2178 0.2831 -0.0176 -0.0126 -0.0490 233 CYS A C   
1763 O  O   . CYS A 247 ? 0.2535 0.2273 0.3229 0.0026  -0.0408 -0.0360 233 CYS A O   
1764 C  CB  . CYS A 247 ? 0.2718 0.2386 0.2482 0.0121  -0.0139 -0.0597 233 CYS A CB  
1765 S  SG  . CYS A 247 ? 0.2680 0.2529 0.3225 0.0184  0.0341  -0.0405 233 CYS A SG  
1766 N  N   . TYR A 248 ? 0.2486 0.2335 0.2521 0.0124  -0.0246 -0.0291 234 TYR A N   
1767 C  CA  . TYR A 248 ? 0.2766 0.1993 0.2674 0.0313  -0.0297 -0.0193 234 TYR A CA  
1768 C  C   . TYR A 248 ? 0.2948 0.2061 0.3242 -0.0311 -0.0349 -0.0319 234 TYR A C   
1769 O  O   . TYR A 248 ? 0.2563 0.1937 0.2913 0.0072  -0.0322 -0.0671 234 TYR A O   
1770 C  CB  . TYR A 248 ? 0.2907 0.2367 0.3051 -0.0195 -0.0287 -0.0460 234 TYR A CB  
1771 C  CG  . TYR A 248 ? 0.4397 0.2650 0.3095 0.0173  0.0855  -0.0682 234 TYR A CG  
1772 C  CD1 . TYR A 248 ? 0.4868 0.3935 0.5513 0.0676  -0.0237 0.0998  234 TYR A CD1 
1773 C  CD2 . TYR A 248 ? 0.4183 0.5176 0.7163 -0.0001 0.1664  -0.0255 234 TYR A CD2 
1774 C  CE1 . TYR A 248 ? 0.8102 0.6236 0.5609 0.0987  0.0695  -0.0025 234 TYR A CE1 
1775 C  CE2 . TYR A 248 ? 0.5806 0.4357 0.7551 0.0367  0.2128  -0.0738 234 TYR A CE2 
1776 C  CZ  . TYR A 248 ? 0.7416 0.7497 0.8285 0.1492  0.1562  0.2220  234 TYR A CZ  
1777 O  OH  . TYR A 248 ? 0.8298 0.5719 0.9200 0.1564  -0.0390 -0.1513 234 TYR A OH  
1778 N  N   . ALA A 249 ? 0.2531 0.2723 0.2588 0.0240  0.0156  -0.0297 235 ALA A N   
1779 C  CA  . ALA A 249 ? 0.2941 0.2085 0.3074 0.0380  0.0167  -0.0238 235 ALA A CA  
1780 C  C   . ALA A 249 ? 0.2894 0.2516 0.2558 -0.0132 0.0177  -0.0472 235 ALA A C   
1781 O  O   . ALA A 249 ? 0.2714 0.2818 0.3702 0.0181  0.0425  -0.0764 235 ALA A O   
1782 C  CB  . ALA A 249 ? 0.3546 0.2902 0.3477 0.0221  -0.0097 -0.0042 235 ALA A CB  
1783 N  N   . SER A 250 ? 0.2419 0.2218 0.2873 0.0701  0.0097  -0.0504 236 SER A N   
1784 C  CA  . SER A 250 ? 0.2166 0.2189 0.2732 0.0518  -0.0111 -0.0676 236 SER A CA  
1785 C  C   . SER A 250 ? 0.2181 0.2416 0.2751 0.0101  -0.0063 -0.0433 236 SER A C   
1786 O  O   . SER A 250 ? 0.2435 0.2224 0.2446 0.0112  0.0056  -0.0989 236 SER A O   
1787 C  CB  . SER A 250 ? 0.2051 0.2549 0.3765 0.0307  0.0466  -0.1202 236 SER A CB  
1788 O  OG  . SER A 250 ? 0.2822 0.2423 0.3870 0.0132  0.0691  -0.1386 236 SER A OG  
1789 N  N   . ASN A 251 ? 0.2201 0.1889 0.2315 -0.0110 0.0267  -0.0504 237 ASN A N   
1790 C  CA  . ASN A 251 ? 0.1893 0.2345 0.2109 -0.0023 0.0396  -0.0434 237 ASN A CA  
1791 C  C   . ASN A 251 ? 0.1674 0.1747 0.1801 0.0082  0.0080  -0.0177 237 ASN A C   
1792 O  O   . ASN A 251 ? 0.2090 0.1756 0.1821 0.0083  -0.0137 -0.0352 237 ASN A O   
1793 C  CB  . ASN A 251 ? 0.1960 0.2113 0.2155 0.0102  0.0590  -0.0647 237 ASN A CB  
1794 C  CG  . ASN A 251 ? 0.2175 0.1916 0.2153 0.0072  0.0433  -0.0455 237 ASN A CG  
1795 O  OD1 . ASN A 251 ? 0.2378 0.2138 0.2103 -0.0103 0.0198  -0.0543 237 ASN A OD1 
1796 N  ND2 . ASN A 251 ? 0.2548 0.2460 0.3175 -0.0689 0.0873  -0.0300 237 ASN A ND2 
1797 N  N   . PHE A 252 ? 0.1827 0.1636 0.1726 0.0079  0.0293  -0.0389 238 PHE A N   
1798 C  CA  . PHE A 252 ? 0.1733 0.2114 0.1728 -0.0122 0.0291  -0.0176 238 PHE A CA  
1799 C  C   . PHE A 252 ? 0.1912 0.1888 0.1531 -0.0056 -0.0087 -0.0043 238 PHE A C   
1800 O  O   . PHE A 252 ? 0.2202 0.2200 0.1781 0.0274  0.0172  -0.0183 238 PHE A O   
1801 C  CB  . PHE A 252 ? 0.1934 0.2302 0.2138 -0.0030 0.0091  -0.0268 238 PHE A CB  
1802 C  CG  . PHE A 252 ? 0.2247 0.1829 0.1913 -0.0107 0.0123  -0.0465 238 PHE A CG  
1803 C  CD1 . PHE A 252 ? 0.2686 0.2019 0.2497 -0.0107 0.0041  0.0000  238 PHE A CD1 
1804 C  CD2 . PHE A 252 ? 0.2531 0.2443 0.1816 -0.0031 0.0698  -0.0291 238 PHE A CD2 
1805 C  CE1 . PHE A 252 ? 0.2612 0.2079 0.2826 0.0190  0.0477  0.0072  238 PHE A CE1 
1806 C  CE2 . PHE A 252 ? 0.3218 0.2011 0.2239 -0.0507 0.0582  -0.0444 238 PHE A CE2 
1807 C  CZ  . PHE A 252 ? 0.2583 0.2215 0.2456 0.0176  0.0577  -0.0247 238 PHE A CZ  
1808 N  N   . VAL A 253 ? 0.2079 0.1750 0.1526 -0.0057 0.0066  -0.0189 239 VAL A N   
1809 C  CA  . VAL A 253 ? 0.2160 0.2054 0.1469 -0.0018 -0.0077 0.0000  239 VAL A CA  
1810 C  C   . VAL A 253 ? 0.2036 0.2067 0.2008 0.0064  0.0152  -0.0142 239 VAL A C   
1811 O  O   . VAL A 253 ? 0.2172 0.1996 0.1838 0.0229  0.0026  -0.0262 239 VAL A O   
1812 C  CB  . VAL A 253 ? 0.2652 0.2223 0.1611 -0.0188 0.0039  0.0040  239 VAL A CB  
1813 C  CG1 . VAL A 253 ? 0.3096 0.2744 0.1653 -0.0399 -0.0159 -0.0159 239 VAL A CG1 
1814 C  CG2 . VAL A 253 ? 0.2539 0.2589 0.2005 -0.0040 -0.0018 -0.0139 239 VAL A CG2 
1815 N  N   . ARG A 254 ? 0.2157 0.1633 0.1885 0.0011  -0.0128 -0.0396 240 ARG A N   
1816 C  CA  . ARG A 254 ? 0.2222 0.1772 0.2042 0.0330  -0.0205 -0.0138 240 ARG A CA  
1817 C  C   . ARG A 254 ? 0.2104 0.1677 0.1822 0.0218  0.0134  -0.0057 240 ARG A C   
1818 O  O   . ARG A 254 ? 0.2350 0.1710 0.1892 0.0532  0.0029  -0.0239 240 ARG A O   
1819 C  CB  . ARG A 254 ? 0.2022 0.1711 0.2149 0.0153  -0.0042 -0.0148 240 ARG A CB  
1820 C  CG  . ARG A 254 ? 0.2700 0.2504 0.2502 0.0443  -0.0095 -0.0247 240 ARG A CG  
1821 C  CD  . ARG A 254 ? 0.2598 0.2059 0.2833 -0.0260 -0.0350 0.0035  240 ARG A CD  
1822 N  NE  . ARG A 254 ? 0.2478 0.2412 0.2891 0.0594  -0.0040 0.0101  240 ARG A NE  
1823 C  CZ  . ARG A 254 ? 0.2449 0.2383 0.2361 -0.0180 0.0247  -0.0165 240 ARG A CZ  
1824 N  NH1 . ARG A 254 ? 0.2525 0.2007 0.2420 0.0171  0.0294  0.0181  240 ARG A NH1 
1825 N  NH2 . ARG A 254 ? 0.3317 0.4145 0.3147 0.0017  0.0260  -0.1172 240 ARG A NH2 
1826 N  N   . ILE A 255 ? 0.1945 0.1878 0.1475 0.0164  -0.0024 -0.0282 241 ILE A N   
1827 C  CA  . ILE A 255 ? 0.2264 0.1834 0.1752 -0.0021 -0.0055 0.0032  241 ILE A CA  
1828 C  C   . ILE A 255 ? 0.1872 0.2258 0.1473 0.0341  -0.0036 -0.0181 241 ILE A C   
1829 O  O   . ILE A 255 ? 0.2445 0.2092 0.1518 0.0598  -0.0069 -0.0110 241 ILE A O   
1830 C  CB  . ILE A 255 ? 0.2173 0.2186 0.1258 0.0347  0.0004  -0.0124 241 ILE A CB  
1831 C  CG1 . ILE A 255 ? 0.2242 0.2296 0.1682 0.0777  0.0115  -0.0276 241 ILE A CG1 
1832 C  CG2 . ILE A 255 ? 0.2582 0.2405 0.1874 0.0355  0.0142  -0.0133 241 ILE A CG2 
1833 C  CD1 . ILE A 255 ? 0.3313 0.2847 0.2053 0.0880  0.0268  0.0041  241 ILE A CD1 
1834 N  N   . GLN A 256 ? 0.2004 0.1960 0.1624 0.0329  -0.0047 0.0030  242 GLN A N   
1835 C  CA  . GLN A 256 ? 0.1952 0.2416 0.1750 0.0133  0.0082  -0.0044 242 GLN A CA  
1836 C  C   . GLN A 256 ? 0.1749 0.2070 0.1978 0.0267  -0.0111 -0.0015 242 GLN A C   
1837 O  O   . GLN A 256 ? 0.1941 0.2529 0.1685 0.0630  0.0092  -0.0117 242 GLN A O   
1838 C  CB  . GLN A 256 ? 0.2072 0.2572 0.1913 0.0156  0.0118  -0.0186 242 GLN A CB  
1839 C  CG  . GLN A 256 ? 0.2260 0.3043 0.1914 0.0198  -0.0320 -0.0011 242 GLN A CG  
1840 C  CD  . GLN A 256 ? 0.2110 0.2766 0.2695 0.0165  -0.0045 -0.0210 242 GLN A CD  
1841 O  OE1 . GLN A 256 ? 0.2476 0.3162 0.3418 0.0299  0.1031  -0.0209 242 GLN A OE1 
1842 N  NE2 . GLN A 256 ? 0.2727 0.3760 0.2877 0.0456  0.0449  -0.0644 242 GLN A NE2 
1843 N  N   . GLN A 257 ? 0.2064 0.1835 0.1799 0.0231  -0.0092 -0.0322 243 GLN A N   
1844 C  CA  . GLN A 257 ? 0.1733 0.1831 0.1614 0.0329  -0.0104 -0.0125 243 GLN A CA  
1845 C  C   . GLN A 257 ? 0.1916 0.2157 0.1447 0.0572  0.0039  -0.0068 243 GLN A C   
1846 O  O   . GLN A 257 ? 0.2446 0.2103 0.1743 0.0767  0.0094  -0.0088 243 GLN A O   
1847 C  CB  . GLN A 257 ? 0.2034 0.2010 0.1731 0.0413  0.0110  -0.0025 243 GLN A CB  
1848 C  CG  . GLN A 257 ? 0.2012 0.2521 0.1852 0.0646  -0.0086 -0.0110 243 GLN A CG  
1849 C  CD  . GLN A 257 ? 0.2384 0.2272 0.1859 0.0706  -0.0073 -0.0214 243 GLN A CD  
1850 O  OE1 . GLN A 257 ? 0.2076 0.2525 0.1664 0.0398  0.0141  -0.0065 243 GLN A OE1 
1851 N  NE2 . GLN A 257 ? 0.3035 0.2196 0.1639 0.0662  0.0074  -0.0065 243 GLN A NE2 
1852 N  N   . VAL A 258 ? 0.1814 0.2098 0.1639 0.0525  -0.0014 -0.0102 244 VAL A N   
1853 C  CA  . VAL A 258 ? 0.1863 0.2097 0.1867 0.0290  -0.0003 -0.0115 244 VAL A CA  
1854 C  C   . VAL A 258 ? 0.1936 0.2108 0.1745 0.0528  -0.0073 -0.0072 244 VAL A C   
1855 O  O   . VAL A 258 ? 0.2451 0.2035 0.1720 0.0841  -0.0177 -0.0412 244 VAL A O   
1856 C  CB  . VAL A 258 ? 0.2054 0.2138 0.1688 0.0520  -0.0362 -0.0058 244 VAL A CB  
1857 C  CG1 . VAL A 258 ? 0.2248 0.2333 0.1799 0.0625  -0.0297 -0.0175 244 VAL A CG1 
1858 C  CG2 . VAL A 258 ? 0.2267 0.2140 0.1986 0.0443  -0.0211 -0.0552 244 VAL A CG2 
1859 N  N   . LEU A 259 ? 0.2074 0.2049 0.1591 0.0581  -0.0036 -0.0220 245 LEU A N   
1860 C  CA  . LEU A 259 ? 0.2063 0.2313 0.1887 0.0616  -0.0248 0.0169  245 LEU A CA  
1861 C  C   . LEU A 259 ? 0.2407 0.2314 0.1717 0.0658  -0.0148 0.0062  245 LEU A C   
1862 O  O   . LEU A 259 ? 0.2691 0.2585 0.1930 0.0961  -0.0051 -0.0120 245 LEU A O   
1863 C  CB  . LEU A 259 ? 0.2501 0.2584 0.1786 0.0553  -0.0054 0.0068  245 LEU A CB  
1864 C  CG  . LEU A 259 ? 0.3347 0.2601 0.2011 0.0581  0.0530  -0.0071 245 LEU A CG  
1865 C  CD1 . LEU A 259 ? 0.3577 0.2801 0.2564 0.0328  0.0256  -0.0250 245 LEU A CD1 
1866 C  CD2 . LEU A 259 ? 0.3902 0.2346 0.3281 0.0934  -0.0451 -0.0046 245 LEU A CD2 
1867 N  N   . ASN A 260 ? 0.2169 0.2424 0.1888 0.0577  0.0017  -0.0138 246 ASN A N   
1868 C  CA  . ASN A 260 ? 0.1884 0.2336 0.2064 0.0638  0.0341  0.0087  246 ASN A CA  
1869 C  C   . ASN A 260 ? 0.1894 0.1961 0.1909 0.0372  -0.0058 -0.0301 246 ASN A C   
1870 O  O   . ASN A 260 ? 0.2081 0.2320 0.2431 0.0968  0.0292  -0.0129 246 ASN A O   
1871 C  CB  . ASN A 260 ? 0.2260 0.2769 0.1944 0.0727  0.0089  -0.0065 246 ASN A CB  
1872 C  CG  . ASN A 260 ? 0.1947 0.2769 0.2743 0.0974  -0.0226 0.0395  246 ASN A CG  
1873 O  OD1 . ASN A 260 ? 0.2420 0.2543 0.2751 0.0181  -0.0049 -0.0349 246 ASN A OD1 
1874 N  ND2 . ASN A 260 ? 0.2847 0.3855 0.1981 0.0934  -0.0207 -0.0228 246 ASN A ND2 
1875 N  N   . ILE A 261 ? 0.2084 0.1952 0.1585 0.0353  0.0150  0.0013  247 ILE A N   
1876 C  CA  . ILE A 261 ? 0.2143 0.2088 0.1839 0.0525  -0.0144 0.0017  247 ILE A CA  
1877 C  C   . ILE A 261 ? 0.2602 0.2107 0.1794 0.0786  -0.0013 0.0086  247 ILE A C   
1878 O  O   . ILE A 261 ? 0.2670 0.1997 0.1782 0.0818  0.0056  -0.0108 247 ILE A O   
1879 C  CB  . ILE A 261 ? 0.2171 0.1837 0.1933 0.0573  -0.0279 -0.0063 247 ILE A CB  
1880 C  CG1 . ILE A 261 ? 0.2179 0.2222 0.1733 0.0694  0.0128  -0.0100 247 ILE A CG1 
1881 C  CG2 . ILE A 261 ? 0.2265 0.2230 0.1632 0.0529  0.0107  -0.0089 247 ILE A CG2 
1882 C  CD1 . ILE A 261 ? 0.2640 0.2274 0.2205 0.0375  0.0004  -0.0476 247 ILE A CD1 
1883 N  N   . ALA A 262 ? 0.2544 0.1928 0.1350 0.0836  0.0153  -0.0034 248 ALA A N   
1884 C  CA  . ALA A 262 ? 0.2729 0.2112 0.1766 0.0855  -0.0025 -0.0145 248 ALA A CA  
1885 C  C   . ALA A 262 ? 0.2231 0.2287 0.1930 0.0373  0.0162  -0.0072 248 ALA A C   
1886 O  O   . ALA A 262 ? 0.2639 0.2324 0.1719 0.0867  -0.0089 -0.0209 248 ALA A O   
1887 C  CB  . ALA A 262 ? 0.2459 0.1991 0.1665 0.0735  0.0100  -0.0108 248 ALA A CB  
1888 N  N   . SER A 263 ? 0.2426 0.2406 0.2085 0.0658  0.0349  -0.0323 249 SER A N   
1889 C  CA  . SER A 263 ? 0.2742 0.3062 0.2176 0.0214  0.0694  0.0198  249 SER A CA  
1890 C  C   . SER A 263 ? 0.2624 0.2503 0.2271 0.0832  0.0199  -0.0014 249 SER A C   
1891 O  O   . SER A 263 ? 0.3271 0.3147 0.2394 0.1185  0.0327  -0.0250 249 SER A O   
1892 C  CB  . SER A 263 ? 0.2133 0.3400 0.4990 0.0702  0.0684  -0.0002 249 SER A CB  
1893 O  OG  . SER A 263 ? 0.3639 0.5418 0.4723 -0.0152 0.0290  0.0182  249 SER A OG  
1894 N  N   . GLN A 264 ? 0.2332 0.2221 0.2238 0.0928  -0.0096 -0.0280 250 GLN A N   
1895 C  CA  . GLN A 264 ? 0.2381 0.2522 0.2941 0.1277  -0.0265 0.0021  250 GLN A CA  
1896 C  C   . GLN A 264 ? 0.2274 0.2268 0.2954 0.0711  0.0000  -0.0166 250 GLN A C   
1897 O  O   . GLN A 264 ? 0.3031 0.2471 0.2637 0.1185  -0.0131 -0.0564 250 GLN A O   
1898 C  CB  . GLN A 264 ? 0.2764 0.2601 0.2363 0.1143  -0.0616 0.0272  250 GLN A CB  
1899 C  CG  . GLN A 264 ? 0.3260 0.3424 0.4051 0.1006  -0.0765 0.0622  250 GLN A CG  
1900 C  CD  . GLN A 264 ? 0.2569 0.4470 0.3865 0.0280  0.0273  -0.0318 250 GLN A CD  
1901 O  OE1 . GLN A 264 ? 0.5150 0.4151 0.3833 -0.1407 0.0814  -0.1378 250 GLN A OE1 
1902 N  NE2 . GLN A 264 ? 0.5549 0.4815 0.4635 0.2025  0.0026  -0.0447 250 GLN A NE2 
1903 N  N   . LEU A 265 ? 0.2517 0.2205 0.2303 0.0955  -0.0220 -0.0072 251 LEU A N   
1904 C  CA  . LEU A 265 ? 0.2551 0.2266 0.2038 0.0822  0.0012  0.0009  251 LEU A CA  
1905 C  C   . LEU A 265 ? 0.3023 0.1750 0.3187 0.1045  -0.0006 0.0028  251 LEU A C   
1906 O  O   . LEU A 265 ? 0.4356 0.2979 0.2718 0.0778  -0.0511 -0.0322 251 LEU A O   
1907 C  CB  . LEU A 265 ? 0.2692 0.1730 0.2379 0.0478  -0.0222 -0.0452 251 LEU A CB  
1908 C  CG  . LEU A 265 ? 0.2706 0.3037 0.2330 0.0477  -0.0159 -0.0445 251 LEU A CG  
1909 C  CD1 . LEU A 265 ? 0.2507 0.3120 0.2551 0.0492  0.0014  -0.0723 251 LEU A CD1 
1910 C  CD2 . LEU A 265 ? 0.2568 0.2676 0.1894 0.0163  -0.0475 -0.0101 251 LEU A CD2 
1911 N  N   . ASN A 266 ? 0.2957 0.2774 0.1995 0.0916  0.0282  -0.0069 252 ASN A N   
1912 C  CA  . ASN A 266 ? 0.3164 0.2803 0.1923 0.1075  0.0358  -0.0183 252 ASN A CA  
1913 C  C   . ASN A 266 ? 0.3998 0.2814 0.1917 0.1069  -0.0309 0.0096  252 ASN A C   
1914 O  O   . ASN A 266 ? 0.4463 0.3759 0.1834 0.1460  -0.0159 -0.0849 252 ASN A O   
1915 C  CB  . ASN A 266 ? 0.3933 0.3334 0.2945 0.1200  0.0165  -0.0597 252 ASN A CB  
1916 C  CG  . ASN A 266 ? 0.3726 0.2416 0.2139 0.0364  0.0676  0.0014  252 ASN A CG  
1917 O  OD1 . ASN A 266 ? 0.3933 0.3612 0.4870 0.1031  0.0027  -0.0029 252 ASN A OD1 
1918 N  ND2 . ASN A 266 ? 0.4199 0.2744 0.4185 0.0872  0.0465  0.0543  252 ASN A ND2 
1919 N  N   . ARG A 267 ? 0.3482 0.3391 0.1866 0.1116  -0.0084 -0.0566 253 ARG A N   
1920 C  CA  . ARG A 267 ? 0.2910 0.3471 0.1777 0.0525  -0.0299 0.0211  253 ARG A CA  
1921 C  C   . ARG A 267 ? 0.2871 0.2917 0.1953 0.0265  0.0001  -0.0010 253 ARG A C   
1922 O  O   . ARG A 267 ? 0.3437 0.2635 0.2369 0.0835  -0.0037 -0.0266 253 ARG A O   
1923 C  CB  . ARG A 267 ? 0.3155 0.2923 0.2023 0.0879  -0.0152 0.0200  253 ARG A CB  
1924 C  CG  . ARG A 267 ? 0.2898 0.2886 0.1789 0.0297  -0.0334 -0.0043 253 ARG A CG  
1925 C  CD  . ARG A 267 ? 0.2839 0.2958 0.2657 0.0150  -0.0598 0.0159  253 ARG A CD  
1926 N  NE  . ARG A 267 ? 0.2573 0.2826 0.3137 0.0681  -0.0474 -0.0231 253 ARG A NE  
1927 C  CZ  . ARG A 267 ? 0.2383 0.2583 0.2619 0.0263  0.0005  -0.0197 253 ARG A CZ  
1928 N  NH1 . ARG A 267 ? 0.2830 0.2361 0.2625 0.1228  -0.0382 -0.0252 253 ARG A NH1 
1929 N  NH2 . ARG A 267 ? 0.2916 0.3170 0.2317 0.0620  -0.0466 -0.0587 253 ARG A NH2 
1930 N  N   . LYS A 268 ? 0.3038 0.2826 0.1715 0.1087  0.0000  -0.0210 254 LYS A N   
1931 C  CA  . LYS A 268 ? 0.3073 0.3118 0.1481 0.0647  0.0496  0.0149  254 LYS A CA  
1932 C  C   . LYS A 268 ? 0.2614 0.2576 0.1993 0.0261  0.0436  -0.0473 254 LYS A C   
1933 O  O   . LYS A 268 ? 0.3296 0.2483 0.2264 0.1013  0.0396  -0.0175 254 LYS A O   
1934 C  CB  . LYS A 268 ? 0.2901 0.3382 0.2069 0.0613  0.0597  0.0433  254 LYS A CB  
1935 C  CG  . LYS A 268 ? 0.3505 0.4088 0.1852 0.0537  0.0657  -0.0089 254 LYS A CG  
1936 C  CD  . LYS A 268 ? 0.3605 0.3403 0.2493 0.0307  0.0876  -0.0526 254 LYS A CD  
1937 C  CE  . LYS A 268 ? 0.3846 0.5431 0.2867 0.0316  0.0756  -0.1603 254 LYS A CE  
1938 N  NZ  . LYS A 268 ? 0.4903 0.6672 0.4270 0.0304  0.1373  -0.0583 254 LYS A NZ  
1939 N  N   . VAL A 269 ? 0.2721 0.2815 0.1903 0.0475  0.0629  0.0152  255 VAL A N   
1940 C  CA  . VAL A 269 ? 0.2612 0.2482 0.2251 0.0879  0.0490  0.0153  255 VAL A CA  
1941 C  C   . VAL A 269 ? 0.2294 0.2677 0.2626 0.0787  0.0125  0.0337  255 VAL A C   
1942 O  O   . VAL A 269 ? 0.2757 0.2468 0.2484 0.0658  0.0202  0.0438  255 VAL A O   
1943 C  CB  . VAL A 269 ? 0.2405 0.2307 0.2303 0.1153  0.0212  0.0281  255 VAL A CB  
1944 C  CG1 . VAL A 269 ? 0.2635 0.2178 0.2435 0.0884  0.0240  -0.0073 255 VAL A CG1 
1945 C  CG2 . VAL A 269 ? 0.3251 0.2261 0.2076 0.0747  0.0504  0.0138  255 VAL A CG2 
1946 N  N   . SER A 270 ? 0.2817 0.2501 0.1935 0.0774  0.0471  0.0511  256 SER A N   
1947 C  CA  . SER A 270 ? 0.3035 0.2557 0.2199 0.1077  0.0677  0.0495  256 SER A CA  
1948 C  C   . SER A 270 ? 0.2215 0.1924 0.2358 0.0471  0.0306  0.0255  256 SER A C   
1949 O  O   . SER A 270 ? 0.2832 0.2274 0.2615 0.0601  0.0458  0.0356  256 SER A O   
1950 C  CB  . SER A 270 ? 0.4224 0.3581 0.2823 0.1527  0.0654  -0.0067 256 SER A CB  
1951 O  OG  . SER A 270 ? 0.3679 0.3250 0.2513 0.1237  0.0112  0.0622  256 SER A OG  
1952 N  N   . PHE A 271 ? 0.2975 0.2318 0.2047 0.0551  0.0264  0.0421  257 PHE A N   
1953 C  CA  . PHE A 271 ? 0.2639 0.2439 0.2410 0.0607  0.0415  0.0838  257 PHE A CA  
1954 C  C   . PHE A 271 ? 0.2762 0.2199 0.2465 0.0652  -0.0011 0.0346  257 PHE A C   
1955 O  O   . PHE A 271 ? 0.3014 0.2961 0.2336 0.0592  -0.0019 0.0715  257 PHE A O   
1956 C  CB  . PHE A 271 ? 0.3422 0.2896 0.2276 0.0227  0.0238  0.0306  257 PHE A CB  
1957 C  CG  . PHE A 271 ? 0.3650 0.3991 0.2505 -0.0603 -0.0464 -0.0172 257 PHE A CG  
1958 C  CD1 . PHE A 271 ? 0.4891 0.6698 0.2296 0.0139  -0.0784 0.0253  257 PHE A CD1 
1959 C  CD2 . PHE A 271 ? 0.5455 0.4304 0.3486 0.0781  -0.1321 0.0741  257 PHE A CD2 
1960 C  CE1 . PHE A 271 ? 0.4000 0.6065 0.2583 0.0131  -0.0506 0.1397  257 PHE A CE1 
1961 C  CE2 . PHE A 271 ? 0.5040 0.4898 0.4608 0.0372  -0.0415 0.0856  257 PHE A CE2 
1962 C  CZ  . PHE A 271 ? 0.4018 0.5872 0.4692 0.1504  -0.0071 0.0566  257 PHE A CZ  
1963 N  N   . LEU A 272 ? 0.2593 0.2266 0.3072 0.0278  0.0162  0.0841  258 LEU A N   
1964 C  CA  . LEU A 272 ? 0.2790 0.3027 0.3770 -0.0154 0.0365  0.0986  258 LEU A CA  
1965 C  C   . LEU A 272 ? 0.2778 0.3678 0.3351 0.0318  -0.0090 0.0470  258 LEU A C   
1966 O  O   . LEU A 272 ? 0.3686 0.3412 0.4047 0.0934  0.1086  0.0645  258 LEU A O   
1967 C  CB  . LEU A 272 ? 0.2788 0.2857 0.2359 0.0384  -0.0197 0.0068  258 LEU A CB  
1968 C  CG  . LEU A 272 ? 0.3015 0.2936 0.2481 0.0442  -0.0006 0.0360  258 LEU A CG  
1969 C  CD1 . LEU A 272 ? 0.3719 0.3829 0.3647 0.0384  -0.0494 0.0326  258 LEU A CD1 
1970 C  CD2 . LEU A 272 ? 0.3920 0.3039 0.4419 0.0481  -0.0870 0.0354  258 LEU A CD2 
1971 N  N   . GLY A 273 ? 0.4073 0.3622 0.3742 0.0067  -0.0881 0.0438  259 GLY A N   
1972 C  CA  . GLY A 273 ? 0.2655 0.4577 0.5871 -0.0387 0.0301  -0.0334 259 GLY A CA  
1973 C  C   . GLY A 273 ? 0.5751 0.5920 0.6526 -0.1455 0.1410  -0.0447 259 GLY A C   
1974 O  O   . GLY A 273 ? 0.7117 0.5967 1.2585 -0.3598 0.0932  -0.2192 259 GLY A O   
1975 N  N   . ARG A 274 ? 0.3811 0.9463 0.6566 -0.1816 -0.1023 -0.3459 260 ARG A N   
1976 C  CA  . ARG A 274 ? 0.4034 0.6501 0.5435 -0.2490 -0.1913 -0.1130 260 ARG A CA  
1977 C  C   . ARG A 274 ? 0.4149 0.4567 0.6407 -0.1611 -0.2018 -0.3751 260 ARG A C   
1978 O  O   . ARG A 274 ? 0.5715 0.6763 0.2921 -0.0979 0.0820  -0.0208 260 ARG A O   
1979 C  CB  . ARG A 274 ? 0.4537 0.9247 0.5781 -0.3828 0.1648  -0.1981 260 ARG A CB  
1980 N  N   . GLU A 277 ? 0.3276 1.7182 1.3420 0.3955  -0.3646 -0.0379 263 GLU A N   
1981 C  CA  . GLU A 277 ? 1.0206 1.5638 2.3178 0.6524  -0.1742 -0.1123 263 GLU A CA  
1982 C  C   . GLU A 277 ? 0.4436 1.9820 1.9292 -0.1382 -0.5949 -0.1010 263 GLU A C   
1983 O  O   . GLU A 277 ? 0.8243 0.1125 0.4901 -0.0432 -0.0847 -0.2176 263 GLU A O   
1984 C  CB  . GLU A 277 ? 1.1096 0.6462 1.3659 0.3537  0.1198  0.0073  263 GLU A CB  
1985 C  CG  . GLU A 277 ? 1.3223 1.0439 1.4033 0.5266  -0.4042 0.1193  263 GLU A CG  
1986 C  CD  . GLU A 277 ? 0.4000 1.9085 0.6921 -0.2377 -0.3416 0.2303  263 GLU A CD  
1987 O  OE1 . GLU A 277 ? 1.4823 0.9707 0.8739 -0.1310 -0.1317 -0.4881 263 GLU A OE1 
1988 O  OE2 . GLU A 277 ? 1.9847 1.1570 0.3583 0.1798  0.3839  -0.3493 263 GLU A OE2 
1989 N  N   . SER A 278 ? 0.7983 1.1864 1.6006 0.5413  -0.5636 -0.0170 264 SER A N   
1990 C  CA  . SER A 278 ? 0.7865 1.0539 1.0226 0.0756  -0.2288 0.0466  264 SER A CA  
1991 C  C   . SER A 278 ? 0.4964 0.5586 0.7210 0.1236  -0.0246 0.0667  264 SER A C   
1992 O  O   . SER A 278 ? 0.4129 0.3870 0.4298 0.0576  -0.0072 -0.0836 264 SER A O   
1993 C  CB  . SER A 278 ? 0.4261 0.5988 0.5844 -0.1099 -0.1333 -0.0792 264 SER A CB  
1994 N  N   . SER A 279 ? 0.5169 0.3836 0.4549 -0.0028 -0.0409 0.0350  265 SER A N   
1995 C  CA  . SER A 279 ? 0.4425 0.2523 0.5127 -0.0388 -0.0031 0.0016  265 SER A CA  
1996 C  C   . SER A 279 ? 0.3763 0.2944 0.3375 0.0255  0.0157  -0.0434 265 SER A C   
1997 O  O   . SER A 279 ? 0.3665 0.3283 0.3836 -0.0591 -0.0407 -0.0028 265 SER A O   
1998 C  CB  . SER A 279 ? 0.3308 0.4432 0.3614 0.0627  0.0137  0.0875  265 SER A CB  
1999 N  N   . PHE A 280 ? 0.3641 0.2914 0.4200 0.0430  -0.0630 -0.0586 266 PHE A N   
2000 C  CA  . PHE A 280 ? 0.3765 0.2670 0.3324 0.0002  0.0104  -0.0262 266 PHE A CA  
2001 C  C   . PHE A 280 ? 0.4861 0.2831 0.4429 0.0073  -0.0884 -0.1882 266 PHE A C   
2002 O  O   . PHE A 280 ? 0.4366 0.2923 0.3863 0.0129  0.0828  -0.0371 266 PHE A O   
2003 C  CB  . PHE A 280 ? 0.3899 0.2995 0.3573 0.0450  -0.0164 -0.0046 266 PHE A CB  
2004 C  CG  . PHE A 280 ? 0.5240 0.3663 0.3287 -0.0022 -0.0523 -0.0828 266 PHE A CG  
2005 C  CD1 . PHE A 280 ? 0.3548 0.2990 0.4530 0.0283  0.0402  -0.0375 266 PHE A CD1 
2006 C  CD2 . PHE A 280 ? 0.3451 0.3515 0.3144 -0.0260 -0.0183 -0.0158 266 PHE A CD2 
2007 C  CE1 . PHE A 280 ? 0.4848 0.3612 0.3179 0.0042  0.0013  0.0258  266 PHE A CE1 
2008 C  CE2 . PHE A 280 ? 0.4430 0.3668 0.3626 0.0067  0.0291  0.0176  266 PHE A CE2 
2009 C  CZ  . PHE A 280 ? 0.4523 0.3491 0.2347 0.0626  0.0517  0.0064  266 PHE A CZ  
2010 N  N   . ASN A 281 ? 0.5021 0.3836 0.3575 -0.0338 -0.0537 -0.0034 267 ASN A N   
2011 C  CA  . ASN A 281 ? 0.4697 0.4391 0.3046 -0.0594 -0.0308 -0.0086 267 ASN A CA  
2012 C  C   . ASN A 281 ? 0.3818 0.4251 0.2720 -0.0155 0.0797  0.0064  267 ASN A C   
2013 O  O   . ASN A 281 ? 0.5204 0.3319 0.3338 -0.0545 0.0839  -0.0052 267 ASN A O   
2014 C  CB  . ASN A 281 ? 0.5827 0.5621 0.3466 0.0217  -0.0262 0.0938  267 ASN A CB  
2015 C  CG  . ASN A 281 ? 0.7600 0.9987 0.5068 0.1188  -0.0071 0.0276  267 ASN A CG  
2016 O  OD1 . ASN A 281 ? 0.9603 1.3355 0.6493 0.2415  -0.0662 0.0459  267 ASN A OD1 
2017 N  ND2 . ASN A 281 ? 0.7828 1.1892 0.5935 0.0474  0.0122  -0.2300 267 ASN A ND2 
2018 N  N   . ILE A 282 ? 0.4831 0.3851 0.3037 -0.0571 0.0693  0.0505  268 ILE A N   
2019 C  CA  . ILE A 282 ? 0.5511 0.3852 0.4232 -0.0565 0.0401  -0.0014 268 ILE A CA  
2020 C  C   . ILE A 282 ? 0.2839 0.2596 0.3250 -0.0424 0.0376  -0.0021 268 ILE A C   
2021 O  O   . ILE A 282 ? 0.3204 0.3192 0.3745 -0.0492 0.0492  -0.0370 268 ILE A O   
2022 C  CB  . ILE A 282 ? 0.4589 0.4217 0.3500 0.1157  0.0044  -0.0798 268 ILE A CB  
2023 C  CG1 . ILE A 282 ? 0.5016 0.3567 0.4188 0.0192  0.0322  0.0504  268 ILE A CG1 
2024 C  CG2 . ILE A 282 ? 0.5216 0.6394 0.3413 -0.0301 0.1271  -0.0771 268 ILE A CG2 
2025 C  CD1 . ILE A 282 ? 0.4890 0.5286 0.7723 -0.0073 0.1145  0.1014  268 ILE A CD1 
2026 N  N   . ALA A 283 ? 0.3107 0.2555 0.2686 -0.0386 0.0558  -0.0272 269 ALA A N   
2027 C  CA  . ALA A 283 ? 0.2656 0.3495 0.3593 -0.0586 0.0858  -0.0174 269 ALA A CA  
2028 C  C   . ALA A 283 ? 0.2830 0.3214 0.2478 -0.0140 0.0927  0.0189  269 ALA A C   
2029 O  O   . ALA A 283 ? 0.3299 0.3718 0.3000 -0.0153 0.0736  -0.0533 269 ALA A O   
2030 C  CB  . ALA A 283 ? 0.2047 0.3794 0.3525 -0.0617 0.0383  0.0118  269 ALA A CB  
2031 N  N   . ARG A 284 ? 0.4057 0.3957 0.3195 -0.0590 0.0960  -0.0333 270 ARG A N   
2032 C  CA  . ARG A 284 ? 0.3969 0.3902 0.3843 0.0084  0.0303  -0.0595 270 ARG A CA  
2033 C  C   . ARG A 284 ? 0.3957 0.4470 0.3542 0.0237  0.0966  0.0161  270 ARG A C   
2034 O  O   . ARG A 284 ? 0.4232 0.4447 0.3873 0.0001  0.1420  -0.0953 270 ARG A O   
2035 C  CB  . ARG A 284 ? 0.5217 0.5484 0.4287 0.0226  -0.0735 -0.1560 270 ARG A CB  
2036 N  N   . LYS A 285 ? 0.4620 0.4143 0.3781 -0.0308 0.1608  -0.0221 271 LYS A N   
2037 C  CA  . LYS A 285 ? 0.5408 0.4616 0.5340 -0.0094 0.1540  -0.0890 271 LYS A CA  
2038 C  C   . LYS A 285 ? 0.3089 0.4833 0.5034 -0.0893 0.2622  -0.0053 271 LYS A C   
2039 O  O   . LYS A 285 ? 0.5392 0.4245 0.8026 -0.0265 0.1207  -0.1098 271 LYS A O   
2040 C  CB  . LYS A 285 ? 0.5239 0.3688 0.6980 0.0078  0.1725  0.0033  271 LYS A CB  
2041 N  N   . MET A 286 ? 0.3489 0.3869 0.4431 -0.0277 0.1793  -0.0759 272 MET A N   
2042 C  CA  . MET A 286 ? 0.2804 0.4164 0.4764 0.0111  0.1780  -0.0402 272 MET A CA  
2043 C  C   . MET A 286 ? 0.3484 0.4320 0.3439 -0.0143 0.0629  -0.1144 272 MET A C   
2044 O  O   . MET A 286 ? 0.3763 0.5283 0.5176 -0.0254 0.0680  -0.2461 272 MET A O   
2045 C  CB  . MET A 286 ? 0.3234 0.4558 0.4535 0.0292  0.1067  -0.1816 272 MET A CB  
2046 C  CG  . MET A 286 ? 0.3667 0.4453 0.4317 -0.0382 0.1510  0.0000  272 MET A CG  
2047 S  SD  . MET A 286 ? 0.3886 0.4647 0.5681 0.0614  0.1602  0.0192  272 MET A SD  
2048 C  CE  . MET A 286 ? 0.1954 0.3637 0.3003 -0.0223 0.1229  -0.0060 272 MET A CE  
2049 N  N   . GLY A 287 ? 0.2615 0.4006 0.4569 0.0169  0.0835  -0.0427 273 GLY A N   
2050 C  CA  . GLY A 287 ? 0.3392 0.3709 0.4268 0.0382  0.1295  -0.0833 273 GLY A CA  
2051 C  C   . GLY A 287 ? 0.3056 0.4944 0.4134 0.0820  0.0872  0.0448  273 GLY A C   
2052 O  O   . GLY A 287 ? 0.2969 0.4280 0.4000 0.0158  0.0036  -0.0422 273 GLY A O   
2053 N  N   . TYR A 288 ? 0.2591 0.4005 0.4033 0.0419  0.0433  -0.0562 274 TYR A N   
2054 C  CA  . TYR A 288 ? 0.3402 0.3858 0.4449 0.0218  0.1058  -0.0790 274 TYR A CA  
2055 C  C   . TYR A 288 ? 0.3448 0.3834 0.3944 0.0079  0.1122  -0.0272 274 TYR A C   
2056 O  O   . TYR A 288 ? 0.4329 0.3876 0.3541 0.0760  0.0587  -0.0503 274 TYR A O   
2057 C  CB  . TYR A 288 ? 0.2313 0.3234 0.2808 -0.0111 0.0506  -0.0757 274 TYR A CB  
2058 C  CG  . TYR A 288 ? 0.2531 0.3561 0.4178 -0.0452 0.0456  -0.0680 274 TYR A CG  
2059 C  CD1 . TYR A 288 ? 0.2440 0.4907 0.4298 -0.2246 0.1221  -0.1170 274 TYR A CD1 
2060 C  CD2 . TYR A 288 ? 0.2831 0.4439 0.4035 -0.0448 0.0350  -0.1163 274 TYR A CD2 
2061 C  CE1 . TYR A 288 ? 0.5495 0.4697 0.2901 -0.2630 0.0180  -0.1166 274 TYR A CE1 
2062 C  CE2 . TYR A 288 ? 0.3175 0.3769 0.4534 -0.0188 0.0248  -0.1999 274 TYR A CE2 
2063 C  CZ  . TYR A 288 ? 0.6488 0.3800 0.2438 -0.1093 -0.0430 -0.1403 274 TYR A CZ  
2064 O  OH  . TYR A 288 ? 0.6145 0.7317 0.8639 -0.0953 -0.1031 0.0791  274 TYR A OH  
2065 N  N   . PHE A 289 ? 0.3516 0.4104 0.3834 0.0691  0.0219  -0.0882 275 PHE A N   
2066 C  CA  . PHE A 289 ? 0.2403 0.3774 0.3492 0.0273  0.0757  -0.0172 275 PHE A CA  
2067 C  C   . PHE A 289 ? 0.4214 0.3895 0.5330 0.0668  0.0797  -0.0292 275 PHE A C   
2068 O  O   . PHE A 289 ? 0.2328 0.4815 0.5021 0.0027  0.1701  0.0557  275 PHE A O   
2069 C  CB  . PHE A 289 ? 0.2766 0.3787 0.2727 0.0168  0.0630  -0.0543 275 PHE A CB  
2070 C  CG  . PHE A 289 ? 0.2923 0.3126 0.2147 -0.0020 0.0758  -0.0318 275 PHE A CG  
2071 C  CD1 . PHE A 289 ? 0.2912 0.2797 0.2994 0.0221  0.0339  -0.0553 275 PHE A CD1 
2072 C  CD2 . PHE A 289 ? 0.2813 0.3110 0.2602 -0.0051 0.0678  -0.0418 275 PHE A CD2 
2073 C  CE1 . PHE A 289 ? 0.3529 0.2890 0.2568 -0.0124 0.0131  0.0229  275 PHE A CE1 
2074 C  CE2 . PHE A 289 ? 0.2968 0.2862 0.3075 0.0402  0.0629  0.0050  275 PHE A CE2 
2075 C  CZ  . PHE A 289 ? 0.2360 0.3010 0.2394 0.0154  0.0398  -0.0214 275 PHE A CZ  
2076 N  N   . ASP A 290 ? 0.2999 0.4030 0.4091 0.0617  0.1595  -0.0021 276 ASP A N   
2077 C  CA  . ASP A 290 ? 0.4477 0.4939 0.4939 0.0282  0.1641  -0.0253 276 ASP A CA  
2078 C  C   . ASP A 290 ? 0.4038 0.4889 0.3740 -0.0009 0.0915  -0.0328 276 ASP A C   
2079 O  O   . ASP A 290 ? 0.4321 0.4225 0.3919 -0.0099 0.1518  -0.0329 276 ASP A O   
2080 C  CB  . ASP A 290 ? 0.3454 0.5603 0.7019 0.1222  0.1725  0.0886  276 ASP A CB  
2081 C  CG  . ASP A 290 ? 0.4797 0.5461 1.0462 -0.1136 0.1096  0.0547  276 ASP A CG  
2082 O  OD1 . ASP A 290 ? 0.9080 1.0029 1.1738 0.0829  0.4643  -0.0348 276 ASP A OD1 
2083 O  OD2 . ASP A 290 ? 0.8857 0.7783 1.2401 -0.1883 0.1223  0.1409  276 ASP A OD2 
2084 N  N   . ILE A 291 ? 0.4267 0.4793 0.3722 0.0568  0.1561  0.0076  277 ILE A N   
2085 C  CA  . ILE A 291 ? 0.4717 0.4345 0.3797 0.0536  0.0844  -0.0459 277 ILE A CA  
2086 C  C   . ILE A 291 ? 0.4718 0.4940 0.5916 0.1172  0.2078  -0.1777 277 ILE A C   
2087 O  O   . ILE A 291 ? 0.3483 0.6805 0.4933 -0.0362 0.2031  -0.0653 277 ILE A O   
2088 C  CB  . ILE A 291 ? 0.4313 0.6725 0.4972 0.2003  0.0489  0.0124  277 ILE A CB  
2089 C  CG1 . ILE A 291 ? 0.5909 0.7623 0.5122 0.2186  0.1954  -0.1006 277 ILE A CG1 
2090 C  CG2 . ILE A 291 ? 0.4482 0.7992 0.3720 0.0857  0.1829  -0.0050 277 ILE A CG2 
2091 C  CD1 . ILE A 291 ? 0.8215 0.8375 0.4874 0.2509  0.1516  -0.0105 277 ILE A CD1 
2092 N  N   . PRO A 292 ? 0.5332 0.5854 0.4549 0.1626  0.1085  -0.1499 278 PRO A N   
2093 C  CA  . PRO A 292 ? 0.4987 0.7630 0.4955 0.1966  -0.0301 -0.1883 278 PRO A CA  
2094 C  C   . PRO A 292 ? 0.5159 1.0554 0.3563 0.1044  0.1129  -0.1174 278 PRO A C   
2095 O  O   . PRO A 292 ? 0.4813 1.0537 0.6625 0.1656  0.1568  -0.2620 278 PRO A O   
2096 C  CB  . PRO A 292 ? 0.5562 0.7701 0.5715 0.2255  -0.1410 -0.1404 278 PRO A CB  
2097 C  CG  . PRO A 292 ? 0.6653 0.6474 0.7393 0.2430  -0.0758 -0.0973 278 PRO A CG  
2098 C  CD  . PRO A 292 ? 0.5186 0.6646 0.6234 0.1105  -0.0417 -0.1548 278 PRO A CD  
2099 N  N   . LYS A 293 ? 0.4327 0.9419 0.4628 0.2083  -0.0210 -0.2049 279 LYS A N   
2100 C  CA  . LYS A 293 ? 0.3258 1.1275 0.4073 0.0507  0.2369  -0.1121 279 LYS A CA  
2101 C  C   . LYS A 293 ? 0.3106 0.7426 0.5607 0.0362  0.1050  -0.0338 279 LYS A C   
2102 O  O   . LYS A 293 ? 0.4075 0.8298 0.5519 0.1494  0.1034  0.0712  279 LYS A O   
2103 C  CB  . LYS A 293 ? 0.4607 1.0121 0.3884 -0.1028 0.1505  -0.0305 279 LYS A CB  
2104 N  N   . ASP A 294 ? 0.4000 0.6517 0.3808 0.0168  0.1148  -0.0264 280 ASP A N   
2105 C  CA  . ASP A 294 ? 0.4591 0.5016 0.4195 -0.0052 0.0465  0.0676  280 ASP A CA  
2106 C  C   . ASP A 294 ? 0.3736 0.5086 0.3825 -0.0778 -0.1037 -0.0624 280 ASP A C   
2107 O  O   . ASP A 294 ? 0.5038 0.4171 0.4848 0.0170  -0.0091 -0.0193 280 ASP A O   
2108 C  CB  . ASP A 294 ? 0.5988 0.4682 0.4889 0.0355  0.0799  -0.0054 280 ASP A CB  
2109 N  N   . LEU A 295 ? 0.3399 0.3939 0.4040 0.0464  0.0405  0.0035  281 LEU A N   
2110 C  CA  . LEU A 295 ? 0.2487 0.3789 0.3094 0.0802  0.0338  0.0038  281 LEU A CA  
2111 C  C   . LEU A 295 ? 0.2771 0.2684 0.2602 0.0296  0.0139  0.0210  281 LEU A C   
2112 O  O   . LEU A 295 ? 0.3170 0.3379 0.2517 0.0791  0.0822  0.0021  281 LEU A O   
2113 C  CB  . LEU A 295 ? 0.3320 0.4207 0.3402 0.1088  0.0187  0.0420  281 LEU A CB  
2114 C  CG  . LEU A 295 ? 0.3703 0.3612 0.3596 0.0418  0.0609  0.0212  281 LEU A CG  
2115 C  CD1 . LEU A 295 ? 0.3621 0.3862 0.1760 0.0438  0.0674  -0.0154 281 LEU A CD1 
2116 C  CD2 . LEU A 295 ? 0.3981 0.4678 0.3306 0.0433  0.0901  -0.0061 281 LEU A CD2 
2117 N  N   . LEU A 296 ? 0.2695 0.3335 0.2633 0.0728  0.0675  0.0685  282 LEU A N   
2118 C  CA  . LEU A 296 ? 0.3197 0.3961 0.2550 0.0791  0.0544  0.0122  282 LEU A CA  
2119 C  C   . LEU A 296 ? 0.4238 0.4474 0.3254 0.0758  0.0164  0.0645  282 LEU A C   
2120 O  O   . LEU A 296 ? 0.4336 0.5056 0.3680 0.1077  0.0990  0.1573  282 LEU A O   
2121 C  CB  . LEU A 296 ? 0.3837 0.3952 0.3727 0.0678  0.0456  0.0303  282 LEU A CB  
2122 C  CG  . LEU A 296 ? 0.3847 0.3555 0.3346 0.0344  0.0933  -0.0275 282 LEU A CG  
2123 C  CD1 . LEU A 296 ? 0.4232 0.4499 0.4398 -0.0961 0.1321  -0.0074 282 LEU A CD1 
2124 C  CD2 . LEU A 296 ? 0.4148 0.4301 0.3852 -0.0619 0.1230  0.0150  282 LEU A CD2 
2125 N  N   . ILE A 297 ? 0.3180 0.3866 0.2365 0.0996  0.0692  0.0396  283 ILE A N   
2126 C  CA  . ILE A 297 ? 0.3941 0.4559 0.2664 0.1352  0.0494  0.0945  283 ILE A CA  
2127 C  C   . ILE A 297 ? 0.3630 0.4811 0.3606 0.1525  0.1277  0.1417  283 ILE A C   
2128 O  O   . ILE A 297 ? 0.3571 0.3631 0.2748 0.1192  0.0616  0.0847  283 ILE A O   
2129 C  CB  . ILE A 297 ? 0.3105 0.4430 0.2678 0.1222  -0.0063 0.0956  283 ILE A CB  
2130 C  CG1 . ILE A 297 ? 0.4676 0.4294 0.4763 0.2057  0.0341  0.0214  283 ILE A CG1 
2131 C  CG2 . ILE A 297 ? 0.4175 0.4389 0.3601 0.1562  0.1438  0.1055  283 ILE A CG2 
2132 C  CD1 . ILE A 297 ? 0.3318 0.4978 0.2864 0.1562  0.0349  0.0279  283 ILE A CD1 
2133 N  N   . PRO A 298 ? 0.4625 0.5479 0.3634 0.0637  0.0922  0.0986  284 PRO A N   
2134 C  CA  . PRO A 298 ? 0.6793 0.7703 0.4137 0.2226  -0.1336 0.4686  284 PRO A CA  
2135 C  C   . PRO A 298 ? 1.2383 0.7150 0.3851 -0.1253 -0.4915 0.4066  284 PRO A C   
2136 O  O   . PRO A 298 ? 0.7007 0.6997 0.3084 0.2238  -0.1344 0.1889  284 PRO A O   
2137 C  CB  . PRO A 298 ? 0.7805 0.9750 0.7871 0.0298  -0.0898 0.3995  284 PRO A CB  
2138 C  CG  . PRO A 298 ? 0.6148 0.5868 0.6012 -0.0140 0.0190  -0.0743 284 PRO A CG  
2139 C  CD  . PRO A 298 ? 0.4437 0.5648 0.3371 0.1993  0.0706  0.1623  284 PRO A CD  
2140 N  N   . ILE A 299 ? 1.0436 0.5029 0.3803 0.3156  -0.0582 0.3676  285 ILE A N   
2141 C  CA  . ILE A 299 ? 0.7268 0.2876 0.6091 0.1733  0.0515  0.0245  285 ILE A CA  
2142 C  C   . ILE A 299 ? 0.4233 0.4192 0.5694 0.1501  0.1397  0.0070  285 ILE A C   
2143 O  O   . ILE A 299 ? 0.4545 0.5099 0.2905 0.1498  -0.0237 0.1385  285 ILE A O   
2144 C  CB  . ILE A 299 ? 0.6333 0.6102 0.4918 0.0996  -0.0535 0.1075  285 ILE A CB  
2145 C  CG1 . ILE A 299 ? 0.4390 0.4744 0.4640 0.1412  -0.0187 -0.0243 285 ILE A CG1 
2146 C  CG2 . ILE A 299 ? 0.5323 0.5411 0.5177 0.0928  -0.0797 0.1104  285 ILE A CG2 
2147 C  CD1 . ILE A 299 ? 0.5661 0.6463 0.4467 0.0461  0.0823  0.0321  285 ILE A CD1 
2148 N  N   . ASN A 300 ? 0.7064 0.5614 0.8302 0.1297  0.0920  0.0574  286 ASN A N   
2149 C  CA  . ASN A 300 ? 0.7570 0.4336 0.9264 0.2401  0.0351  0.1181  286 ASN A CA  
2150 C  C   . ASN A 300 ? 0.6370 0.7571 0.6839 0.1276  0.0982  -0.0821 286 ASN A C   
2151 O  O   . ASN A 300 ? 0.6001 0.6906 0.6754 0.0286  0.1944  -0.1147 286 ASN A O   
2152 C  CB  . ASN A 300 ? 0.9008 0.3818 0.4601 0.0865  -0.0597 0.0999  286 ASN A CB  
2153 C  CG  . ASN A 300 ? 0.6424 0.4106 0.4069 0.0968  -0.0399 0.0405  286 ASN A CG  
2154 O  OD1 . ASN A 300 ? 1.0321 0.6889 0.8181 0.1776  -0.0444 -0.0136 286 ASN A OD1 
2155 N  ND2 . ASN A 300 ? 1.2285 0.8263 0.7043 0.2614  0.2081  0.0868  286 ASN A ND2 
2156 N  N   . GLU A 301 ? 0.9572 0.9741 0.5494 0.1174  0.3463  0.2985  287 GLU A N   
2157 C  CA  . GLU A 301 ? 1.1507 1.3531 0.4545 -0.2511 -0.4096 -0.1481 287 GLU A CA  
2158 C  C   . GLU A 301 ? 0.6113 0.8229 0.8495 0.0231  -0.0561 0.0607  287 GLU A C   
2159 O  O   . GLU A 301 ? 0.7168 0.6487 0.5685 0.0004  0.1500  -0.0390 287 GLU A O   
2160 C  CB  . GLU A 301 ? 0.5866 0.9866 0.9825 0.0689  0.0276  0.0695  287 GLU A CB  
2161 C  CG  . GLU A 301 ? 0.7025 1.0440 0.9856 0.0680  -0.0799 0.0010  287 GLU A CG  
2162 C  CD  . GLU A 301 ? 0.9216 0.9005 1.1126 -0.0517 -0.1260 0.0055  287 GLU A CD  
2163 O  OE1 . GLU A 301 ? 1.0229 1.3550 1.0318 -0.2674 -0.2949 0.1442  287 GLU A OE1 
2164 O  OE2 . GLU A 301 ? 1.1490 1.0018 1.3817 -0.2778 -0.2024 0.0588  287 GLU A OE2 
2165 N  N   . VAL A 302 ? 0.7030 0.7048 0.3483 -0.1107 -0.0813 0.1860  288 VAL A N   
2166 C  CA  . VAL A 302 ? 0.4095 0.3600 0.3903 0.2137  -0.0106 0.0468  288 VAL A CA  
2167 C  C   . VAL A 302 ? 0.4627 0.4610 0.3739 0.1339  0.0423  0.1071  288 VAL A C   
2168 O  O   . VAL A 302 ? 0.5138 0.5509 0.2538 0.1232  0.0171  0.0424  288 VAL A O   
2169 C  CB  . VAL A 302 ? 0.4311 0.3398 0.3378 0.1559  0.0899  0.0126  288 VAL A CB  
2170 C  CG1 . VAL A 302 ? 0.2789 0.5029 0.4535 0.1599  0.0897  0.0426  288 VAL A CG1 
2171 C  CG2 . VAL A 302 ? 0.5215 0.4825 0.2161 0.0646  0.1099  0.1079  288 VAL A CG2 
2172 N  N   . GLU A 303 ? 0.4191 0.5347 0.3054 0.1191  -0.0241 0.0733  289 GLU A N   
2173 C  CA  . GLU A 303 ? 0.3986 0.5302 0.3048 0.0751  -0.0264 0.0754  289 GLU A CA  
2174 C  C   . GLU A 303 ? 0.5293 0.6959 0.4045 0.0589  -0.0693 0.0605  289 GLU A C   
2175 O  O   . GLU A 303 ? 0.5970 0.6412 0.3778 0.1403  0.0613  0.0883  289 GLU A O   
2176 C  CB  . GLU A 303 ? 0.5675 0.5230 0.3140 0.1536  -0.0595 0.0152  289 GLU A CB  
2177 C  CG  . GLU A 303 ? 0.5868 0.5785 0.3220 0.0750  0.0246  0.0919  289 GLU A CG  
2178 C  CD  . GLU A 303 ? 0.4549 0.5713 0.3503 0.0576  0.0228  0.0948  289 GLU A CD  
2179 O  OE1 . GLU A 303 ? 0.5107 0.7447 0.6528 0.0353  0.0389  0.1654  289 GLU A OE1 
2180 O  OE2 . GLU A 303 ? 0.4449 0.8092 0.6550 0.2050  -0.0980 0.0926  289 GLU A OE2 
2181 N  N   . ASN A 304 ? 0.5800 0.6853 0.4458 0.1000  0.1243  0.1730  290 ASN A N   
2182 C  CA  . ASN A 304 ? 0.6976 0.6730 0.4279 0.1150  0.0531  0.0778  290 ASN A CA  
2183 C  C   . ASN A 304 ? 0.6709 0.5944 0.6246 0.2057  -0.0023 -0.1032 290 ASN A C   
2184 O  O   . ASN A 304 ? 0.5528 0.5390 0.5610 0.1970  -0.2106 0.1375  290 ASN A O   
2185 C  CB  . ASN A 304 ? 0.5851 0.5749 0.3070 0.1016  0.0677  0.0577  290 ASN A CB  
2186 C  CG  . ASN A 304 ? 0.5057 0.6208 0.3799 0.0173  0.0386  0.1321  290 ASN A CG  
2187 O  OD1 . ASN A 304 ? 0.6726 0.6615 0.4384 0.1393  0.0172  0.0026  290 ASN A OD1 
2188 N  ND2 . ASN A 304 ? 0.7227 0.6787 0.2859 -0.0649 0.0206  0.0302  290 ASN A ND2 
2189 N  N   . TYR A 305 ? 0.6542 0.6016 0.4465 0.1655  -0.0859 0.0769  291 TYR A N   
2190 C  CA  . TYR A 305 ? 0.4263 0.4302 0.2440 0.1097  0.0700  -0.0264 291 TYR A CA  
2191 C  C   . TYR A 305 ? 0.3900 0.5087 0.1655 0.1022  -0.0471 -0.0714 291 TYR A C   
2192 O  O   . TYR A 305 ? 0.3960 0.6707 0.2300 0.0747  -0.0264 0.0189  291 TYR A O   
2193 C  CB  . TYR A 305 ? 0.3814 0.4675 0.2123 0.0978  0.0331  0.0134  291 TYR A CB  
2194 C  CG  . TYR A 305 ? 0.3791 0.3801 0.2958 0.0822  0.0456  0.0159  291 TYR A CG  
2195 C  CD1 . TYR A 305 ? 0.4045 0.5013 0.2598 0.0723  0.0974  0.0030  291 TYR A CD1 
2196 C  CD2 . TYR A 305 ? 0.4378 0.5004 0.2836 0.0563  0.0357  0.0215  291 TYR A CD2 
2197 C  CE1 . TYR A 305 ? 0.4449 0.4627 0.3118 0.0435  -0.0642 -0.0076 291 TYR A CE1 
2198 C  CE2 . TYR A 305 ? 0.4796 0.4808 0.3481 0.0785  0.1092  -0.0241 291 TYR A CE2 
2199 C  CZ  . TYR A 305 ? 0.5623 0.6020 0.3619 0.0245  0.0422  -0.0935 291 TYR A CZ  
2200 O  OH  . TYR A 305 ? 0.4328 0.6383 0.3265 -0.0489 0.0999  -0.0805 291 TYR A OH  
2201 N  N   . PRO A 306 ? 0.3196 0.4104 0.1836 0.0672  0.0299  -0.0519 292 PRO A N   
2202 C  CA  . PRO A 306 ? 0.3294 0.3816 0.1917 0.0280  -0.0133 -0.0841 292 PRO A CA  
2203 C  C   . PRO A 306 ? 0.2873 0.3017 0.2047 -0.0067 0.0547  -0.0800 292 PRO A C   
2204 O  O   . PRO A 306 ? 0.2752 0.3685 0.2453 0.0550  0.0134  -0.0914 292 PRO A O   
2205 C  CB  . PRO A 306 ? 0.3342 0.4253 0.3471 0.0628  0.0067  -0.1179 292 PRO A CB  
2206 C  CG  . PRO A 306 ? 0.3514 0.4515 0.3984 0.0790  0.0571  -0.0571 292 PRO A CG  
2207 C  CD  . PRO A 306 ? 0.2744 0.5394 0.3304 0.0811  -0.0028 -0.0576 292 PRO A CD  
2208 N  N   . LYS A 307 ? 0.3043 0.3361 0.2277 0.0894  -0.0110 -0.0496 293 LYS A N   
2209 C  CA  . LYS A 307 ? 0.2808 0.3090 0.1793 0.1041  0.0078  -0.0198 293 LYS A CA  
2210 C  C   . LYS A 307 ? 0.3217 0.3378 0.2229 0.1246  -0.0722 -0.0850 293 LYS A C   
2211 O  O   . LYS A 307 ? 0.3053 0.3783 0.1781 0.0786  0.0108  -0.0834 293 LYS A O   
2212 C  CB  . LYS A 307 ? 0.3510 0.3360 0.1975 0.0735  -0.0031 -0.0613 293 LYS A CB  
2213 C  CG  . LYS A 307 ? 0.3998 0.4247 0.2032 0.0592  -0.0390 -0.0026 293 LYS A CG  
2214 C  CD  . LYS A 307 ? 0.4558 0.5429 0.3381 0.0378  0.0521  -0.0854 293 LYS A CD  
2215 C  CE  . LYS A 307 ? 0.7887 0.8610 0.5488 0.1373  0.0189  -0.0380 293 LYS A CE  
2216 N  NZ  . LYS A 307 ? 1.1071 0.8546 0.8230 0.1853  -0.1057 -0.2061 293 LYS A NZ  
2217 N  N   . ASN A 308 ? 0.3255 0.3356 0.1904 0.0861  -0.0195 -0.0830 294 ASN A N   
2218 C  CA  . ASN A 308 ? 0.3635 0.3300 0.2215 0.0981  -0.0052 -0.0624 294 ASN A CA  
2219 C  C   . ASN A 308 ? 0.3182 0.2520 0.2700 0.1326  0.0423  -0.0916 294 ASN A C   
2220 O  O   . ASN A 308 ? 0.3369 0.3523 0.2145 0.1061  -0.0423 -0.0595 294 ASN A O   
2221 C  CB  . ASN A 308 ? 0.3307 0.3597 0.2373 0.0231  -0.0200 -0.0427 294 ASN A CB  
2222 C  CG  . ASN A 308 ? 0.3758 0.3749 0.3940 0.0893  0.0511  -0.0777 294 ASN A CG  
2223 O  OD1 . ASN A 308 ? 0.4169 0.3025 0.3537 0.0724  0.0871  -0.0659 294 ASN A OD1 
2224 N  ND2 . ASN A 308 ? 0.4598 0.4273 0.5007 0.1122  0.0375  -0.2127 294 ASN A ND2 
2225 N  N   . GLU A 309 ? 0.2338 0.3127 0.1921 0.0813  -0.0014 -0.0530 295 GLU A N   
2226 C  CA  . GLU A 309 ? 0.3163 0.3170 0.2291 0.0657  0.0147  -0.0617 295 GLU A CA  
2227 C  C   . GLU A 309 ? 0.2704 0.2727 0.1625 0.0154  -0.0015 -0.0154 295 GLU A C   
2228 O  O   . GLU A 309 ? 0.3412 0.2699 0.1876 0.0824  -0.0462 -0.0126 295 GLU A O   
2229 C  CB  . GLU A 309 ? 0.3225 0.3197 0.3028 0.0650  -0.0362 -0.0092 295 GLU A CB  
2230 C  CG  . GLU A 309 ? 0.4042 0.4459 0.3984 0.1253  0.1305  -0.0380 295 GLU A CG  
2231 C  CD  . GLU A 309 ? 0.4521 0.6120 0.4302 -0.0182 0.1495  0.0036  295 GLU A CD  
2232 O  OE1 . GLU A 309 ? 0.5175 0.4304 0.4820 0.0604  0.0984  -0.1363 295 GLU A OE1 
2233 O  OE2 . GLU A 309 ? 0.5589 0.8604 0.8352 0.1496  0.4302  -0.2153 295 GLU A OE2 
2234 N  N   . VAL A 310 ? 0.3205 0.3120 0.1831 0.1282  0.0199  -0.0233 296 VAL A N   
2235 C  CA  . VAL A 310 ? 0.3976 0.3044 0.2054 0.1173  -0.0291 0.0265  296 VAL A CA  
2236 C  C   . VAL A 310 ? 0.2738 0.2303 0.1803 0.0449  -0.0087 0.0272  296 VAL A C   
2237 O  O   . VAL A 310 ? 0.2793 0.2720 0.1949 0.1040  -0.0021 -0.0389 296 VAL A O   
2238 C  CB  . VAL A 310 ? 0.3735 0.3121 0.2310 0.1800  0.0244  -0.0187 296 VAL A CB  
2239 C  CG1 . VAL A 310 ? 0.4561 0.3783 0.2059 0.1968  0.0361  0.0428  296 VAL A CG1 
2240 C  CG2 . VAL A 310 ? 0.4445 0.4254 0.3106 0.0481  0.0517  0.0590  296 VAL A CG2 
2241 N  N   . ILE A 311 ? 0.2823 0.2509 0.2526 0.0644  0.0474  0.0041  297 ILE A N   
2242 C  CA  . ILE A 311 ? 0.2529 0.2157 0.1798 0.0611  0.0323  0.0061  297 ILE A CA  
2243 C  C   . ILE A 311 ? 0.2805 0.2285 0.2077 0.0477  0.0012  0.0041  297 ILE A C   
2244 O  O   . ILE A 311 ? 0.2808 0.2359 0.2860 0.0723  0.0534  -0.0229 297 ILE A O   
2245 C  CB  . ILE A 311 ? 0.2568 0.2322 0.2108 0.0428  0.0138  -0.0011 297 ILE A CB  
2246 C  CG1 . ILE A 311 ? 0.2762 0.2677 0.1877 0.0465  0.0280  -0.0283 297 ILE A CG1 
2247 C  CG2 . ILE A 311 ? 0.2654 0.2736 0.1717 0.0606  -0.0028 -0.0340 297 ILE A CG2 
2248 C  CD1 . ILE A 311 ? 0.3138 0.3146 0.2227 0.0541  0.0301  -0.0429 297 ILE A CD1 
2249 N  N   . ILE A 312 ? 0.2836 0.2355 0.1599 0.0522  0.0207  -0.0040 298 ILE A N   
2250 C  CA  . ILE A 312 ? 0.3366 0.2070 0.1638 0.0575  0.0013  0.0169  298 ILE A CA  
2251 C  C   . ILE A 312 ? 0.2545 0.2373 0.1958 0.0186  0.0326  -0.0147 298 ILE A C   
2252 O  O   . ILE A 312 ? 0.2922 0.2323 0.2001 0.0234  0.0487  -0.0407 298 ILE A O   
2253 C  CB  . ILE A 312 ? 0.3441 0.2419 0.1612 0.0427  0.0184  -0.0248 298 ILE A CB  
2254 C  CG1 . ILE A 312 ? 0.3866 0.2562 0.2509 0.1079  -0.0326 -0.0194 298 ILE A CG1 
2255 C  CG2 . ILE A 312 ? 0.3322 0.2257 0.1903 0.0461  0.0139  0.0063  298 ILE A CG2 
2256 C  CD1 . ILE A 312 ? 0.6954 0.5694 0.2858 -0.0811 0.1324  0.0355  298 ILE A CD1 
2257 N  N   . ILE A 313 ? 0.2448 0.2094 0.1729 0.0562  0.0165  0.0131  299 ILE A N   
2258 C  CA  . ILE A 313 ? 0.2348 0.1931 0.1660 0.0383  0.0325  -0.0012 299 ILE A CA  
2259 C  C   . ILE A 313 ? 0.2455 0.1652 0.2059 0.0470  0.0199  0.0119  299 ILE A C   
2260 O  O   . ILE A 313 ? 0.2650 0.1967 0.2094 0.0518  0.0273  0.0269  299 ILE A O   
2261 C  CB  . ILE A 313 ? 0.2594 0.2145 0.2183 0.0531  0.0436  0.0226  299 ILE A CB  
2262 C  CG1 . ILE A 313 ? 0.2319 0.2201 0.2288 0.0481  0.0188  0.0225  299 ILE A CG1 
2263 C  CG2 . ILE A 313 ? 0.2606 0.2330 0.2183 0.0644  0.0131  -0.0011 299 ILE A CG2 
2264 C  CD1 . ILE A 313 ? 0.2659 0.2886 0.2168 0.0796  0.0210  0.0548  299 ILE A CD1 
2265 N  N   . ALA A 314 ? 0.2429 0.1988 0.2123 0.0458  -0.0062 0.0059  300 ALA A N   
2266 C  CA  . ALA A 314 ? 0.2348 0.2461 0.2152 0.0553  0.0186  0.0046  300 ALA A CA  
2267 C  C   . ALA A 314 ? 0.2570 0.2290 0.1996 -0.0025 0.0421  -0.0142 300 ALA A C   
2268 O  O   . ALA A 314 ? 0.2806 0.2095 0.2479 0.0130  0.0335  -0.0191 300 ALA A O   
2269 C  CB  . ALA A 314 ? 0.3129 0.2612 0.2215 0.0711  -0.0067 -0.0135 300 ALA A CB  
2270 N  N   . THR A 315 ? 0.3329 0.2094 0.2414 -0.0154 0.0390  0.0021  301 THR A N   
2271 C  CA  . THR A 315 ? 0.2637 0.2530 0.2366 -0.0381 0.0055  0.0038  301 THR A CA  
2272 C  C   . THR A 315 ? 0.2735 0.3428 0.3745 0.0043  0.0267  0.0176  301 THR A C   
2273 O  O   . THR A 315 ? 0.3195 0.2998 0.3408 0.0119  0.0610  -0.0289 301 THR A O   
2274 C  CB  . THR A 315 ? 0.3190 0.2572 0.3290 0.0176  0.0499  -0.0239 301 THR A CB  
2275 O  OG1 . THR A 315 ? 0.3321 0.2997 0.3445 -0.0189 0.0505  0.0599  301 THR A OG1 
2276 C  CG2 . THR A 315 ? 0.3801 0.2647 0.4423 0.0442  0.0231  -0.0155 301 THR A CG2 
2277 N  N   . GLY A 316 ? 0.3123 0.2930 0.4164 -0.0221 -0.0148 -0.0384 302 GLY A N   
2278 C  CA  . GLY A 316 ? 0.2544 0.2769 0.4291 0.0158  0.0271  -0.0624 302 GLY A CA  
2279 C  C   . GLY A 316 ? 0.4822 0.3590 0.4933 0.0408  -0.1256 0.0210  302 GLY A C   
2280 O  O   . GLY A 316 ? 0.5016 0.2817 0.4840 0.0441  -0.0690 0.0259  302 GLY A O   
2281 N  N   . MET A 317 ? 0.5411 0.4241 0.5156 -0.0399 0.0080  -0.0134 303 MET A N   
2282 C  CA  . MET A 317 ? 0.5734 0.5459 0.6619 0.1160  -0.1222 0.0274  303 MET A CA  
2283 C  C   . MET A 317 ? 0.5533 0.3002 0.6376 0.0733  0.0017  0.0449  303 MET A C   
2284 O  O   . MET A 317 ? 0.6964 0.5447 0.7731 -0.0374 -0.0517 0.0285  303 MET A O   
2285 C  CB  . MET A 317 ? 0.5086 0.7532 0.6299 0.0882  -0.1549 -0.0275 303 MET A CB  
2286 N  N   . GLN A 318 ? 0.6344 0.2974 0.4842 0.0195  0.0115  0.0258  304 GLN A N   
2287 C  CA  . GLN A 318 ? 0.7933 0.2814 0.5455 -0.0318 -0.0338 -0.0070 304 GLN A CA  
2288 C  C   . GLN A 318 ? 0.4319 0.3225 0.6321 -0.0602 -0.1044 -0.0284 304 GLN A C   
2289 O  O   . GLN A 318 ? 0.8692 0.4264 0.4676 -0.1232 0.0117  -0.1680 304 GLN A O   
2290 C  CB  . GLN A 318 ? 0.7241 0.5082 0.3443 -0.0139 -0.1264 -0.0919 304 GLN A CB  
2291 N  N   . GLY A 319 ? 0.5111 0.3080 0.3943 0.0456  0.0044  -0.0026 305 GLY A N   
2292 C  CA  . GLY A 319 ? 0.4638 0.2725 0.3438 0.0219  0.0037  -0.0341 305 GLY A CA  
2293 C  C   . GLY A 319 ? 0.2599 0.4508 0.2575 0.0191  0.0472  0.0109  305 GLY A C   
2294 O  O   . GLY A 319 ? 0.4144 0.3184 0.3110 -0.0828 -0.0487 0.0521  305 GLY A O   
2295 N  N   . GLU A 320 ? 0.3940 0.2193 0.3106 -0.0505 0.0234  -0.0266 306 GLU A N   
2296 C  CA  . GLU A 320 ? 0.3534 0.2258 0.2979 -0.0636 0.0683  -0.0497 306 GLU A CA  
2297 C  C   . GLU A 320 ? 0.3612 0.3029 0.3153 -0.0777 -0.0553 -0.0664 306 GLU A C   
2298 O  O   . GLU A 320 ? 0.3603 0.2506 0.3061 0.0658  0.0191  -0.0691 306 GLU A O   
2299 C  CB  . GLU A 320 ? 0.3240 0.3436 0.4800 0.0230  0.0362  -0.1849 306 GLU A CB  
2300 C  CG  . GLU A 320 ? 0.4286 0.5271 0.6931 0.0045  0.0832  -0.2127 306 GLU A CG  
2301 C  CD  . GLU A 320 ? 0.5065 0.5235 0.6970 0.1331  0.0097  -0.2617 306 GLU A CD  
2302 O  OE1 . GLU A 320 ? 0.5031 0.5836 0.4251 0.1132  -0.0588 -0.1778 306 GLU A OE1 
2303 O  OE2 . GLU A 320 ? 0.4809 0.4406 0.3362 -0.1014 0.1307  -0.1074 306 GLU A OE2 
2304 N  N   . PRO A 321 ? 0.3148 0.2920 0.3168 -0.0241 -0.0180 -0.0559 307 PRO A N   
2305 C  CA  . PRO A 321 ? 0.2718 0.2457 0.2412 0.0000  0.0083  -0.0725 307 PRO A CA  
2306 C  C   . PRO A 321 ? 0.1750 0.2823 0.2185 -0.0127 0.0162  0.0029  307 PRO A C   
2307 O  O   . PRO A 321 ? 0.2347 0.2500 0.2048 -0.0005 -0.0075 -0.0291 307 PRO A O   
2308 C  CB  . PRO A 321 ? 0.2201 0.2492 0.2739 -0.0272 -0.0396 -0.0267 307 PRO A CB  
2309 C  CG  . PRO A 321 ? 0.3959 0.4046 0.2335 0.0462  -0.0261 0.0066  307 PRO A CG  
2310 C  CD  . PRO A 321 ? 0.2649 0.2820 0.2706 -0.0022 -0.0028 -0.0390 307 PRO A CD  
2311 N  N   . VAL A 322 ? 0.2443 0.2909 0.1996 -0.0555 0.0375  -0.0671 308 VAL A N   
2312 C  CA  . VAL A 322 ? 0.2434 0.2308 0.2124 -0.0397 0.0400  -0.0491 308 VAL A CA  
2313 C  C   . VAL A 322 ? 0.2850 0.1948 0.2500 -0.0365 0.0416  -0.0131 308 VAL A C   
2314 O  O   . VAL A 322 ? 0.2558 0.2712 0.2202 -0.0377 -0.0007 -0.0218 308 VAL A O   
2315 C  CB  . VAL A 322 ? 0.3089 0.2646 0.2242 -0.0860 -0.0149 -0.0033 308 VAL A CB  
2316 C  CG1 . VAL A 322 ? 0.3152 0.3895 0.1960 -0.1172 -0.0061 -0.0033 308 VAL A CG1 
2317 C  CG2 . VAL A 322 ? 0.3541 0.3156 0.2777 -0.0567 0.0163  0.0214  308 VAL A CG2 
2318 N  N   . GLU A 323 ? 0.2886 0.2504 0.2421 0.0071  -0.0190 -0.0365 309 GLU A N   
2319 C  CA  . GLU A 323 ? 0.3356 0.3317 0.2292 0.0412  0.0319  -0.0166 309 GLU A CA  
2320 C  C   . GLU A 323 ? 0.3322 0.2310 0.2326 0.0550  0.0011  0.0048  309 GLU A C   
2321 O  O   . GLU A 323 ? 0.3043 0.2086 0.2530 0.0351  0.0013  -0.0078 309 GLU A O   
2322 C  CB  . GLU A 323 ? 0.6376 0.5593 0.6200 0.0040  -0.0549 -0.0234 309 GLU A CB  
2323 C  CG  . GLU A 323 ? 0.9006 0.5718 0.8522 0.2081  -0.0771 -0.1239 309 GLU A CG  
2324 C  CD  . GLU A 323 ? 0.6205 0.8635 1.1603 0.3988  0.0996  -0.1045 309 GLU A CD  
2325 O  OE1 . GLU A 323 ? 1.2789 1.4114 0.6519 0.1139  0.1670  -0.1696 309 GLU A OE1 
2326 O  OE2 . GLU A 323 ? 0.7768 1.3336 0.9608 0.4421  0.1683  -0.5235 309 GLU A OE2 
2327 N  N   . ALA A 324 ? 0.3118 0.2040 0.2584 -0.0276 0.0129  -0.0267 310 ALA A N   
2328 C  CA  . ALA A 324 ? 0.2826 0.1820 0.1858 0.0047  0.0066  -0.0237 310 ALA A CA  
2329 C  C   . ALA A 324 ? 0.2202 0.1751 0.2435 0.0156  -0.0014 0.0187  310 ALA A C   
2330 O  O   . ALA A 324 ? 0.2500 0.2055 0.1773 -0.0152 0.0020  -0.0047 310 ALA A O   
2331 C  CB  . ALA A 324 ? 0.2690 0.2338 0.1959 -0.0441 0.0043  -0.0147 310 ALA A CB  
2332 N  N   . LEU A 325 ? 0.2196 0.1840 0.1714 -0.0072 -0.0084 -0.0046 311 LEU A N   
2333 C  CA  . LEU A 325 ? 0.1808 0.1695 0.1777 0.0104  -0.0009 0.0029  311 LEU A CA  
2334 C  C   . LEU A 325 ? 0.1965 0.2112 0.1833 0.0194  -0.0219 0.0180  311 LEU A C   
2335 O  O   . LEU A 325 ? 0.2184 0.1990 0.1663 0.0271  -0.0300 -0.0048 311 LEU A O   
2336 C  CB  . LEU A 325 ? 0.2181 0.1987 0.1431 -0.0043 -0.0023 0.0096  311 LEU A CB  
2337 C  CG  . LEU A 325 ? 0.2305 0.1924 0.1524 -0.0232 -0.0210 -0.0078 311 LEU A CG  
2338 C  CD1 . LEU A 325 ? 0.2946 0.1999 0.2223 -0.0005 0.0050  -0.0027 311 LEU A CD1 
2339 C  CD2 . LEU A 325 ? 0.2300 0.2594 0.1796 -0.0167 -0.0318 0.0029  311 LEU A CD2 
2340 N  N   . SER A 326 ? 0.1931 0.1985 0.1819 0.0109  -0.0115 -0.0033 312 SER A N   
2341 C  CA  . SER A 326 ? 0.2338 0.2467 0.1739 0.0064  -0.0092 0.0159  312 SER A CA  
2342 C  C   . SER A 326 ? 0.2115 0.2161 0.2148 0.0224  -0.0056 0.0212  312 SER A C   
2343 O  O   . SER A 326 ? 0.2135 0.2145 0.2160 0.0133  -0.0097 0.0207  312 SER A O   
2344 C  CB  . SER A 326 ? 0.2309 0.3451 0.1823 0.0138  -0.0064 0.0023  312 SER A CB  
2345 O  OG  . SER A 326 ? 0.2183 0.3749 0.2821 0.0433  0.0017  0.0181  312 SER A OG  
2346 N  N   . GLN A 327 ? 0.1961 0.1991 0.1891 0.0258  0.0053  -0.0007 313 GLN A N   
2347 C  CA  . GLN A 327 ? 0.1980 0.2011 0.1744 0.0427  -0.0204 0.0141  313 GLN A CA  
2348 C  C   . GLN A 327 ? 0.2137 0.1891 0.1818 0.0196  0.0000  0.0275  313 GLN A C   
2349 O  O   . GLN A 327 ? 0.2226 0.2088 0.1824 0.0408  -0.0172 0.0152  313 GLN A O   
2350 C  CB  . GLN A 327 ? 0.2253 0.2044 0.2079 0.0369  -0.0040 0.0240  313 GLN A CB  
2351 C  CG  . GLN A 327 ? 0.2354 0.2450 0.3118 0.0618  -0.0015 0.0394  313 GLN A CG  
2352 C  CD  . GLN A 327 ? 0.4893 0.3932 0.4521 0.0368  0.1424  0.0291  313 GLN A CD  
2353 O  OE1 . GLN A 327 ? 0.5468 0.5347 0.6409 0.0313  0.0952  -0.0309 313 GLN A OE1 
2354 N  NE2 . GLN A 327 ? 0.7151 0.3777 0.7514 0.0699  0.1455  -0.0038 313 GLN A NE2 
2355 N  N   . MET A 328 ? 0.1766 0.1823 0.1663 0.0201  -0.0292 0.0093  314 MET A N   
2356 C  CA  . MET A 328 ? 0.1917 0.1937 0.1335 0.0152  -0.0341 0.0144  314 MET A CA  
2357 C  C   . MET A 328 ? 0.1913 0.1802 0.1463 0.0239  -0.0286 0.0185  314 MET A C   
2358 O  O   . MET A 328 ? 0.2007 0.2120 0.1529 0.0325  -0.0410 -0.0061 314 MET A O   
2359 C  CB  . MET A 328 ? 0.2147 0.2095 0.1290 0.0057  -0.0352 -0.0035 314 MET A CB  
2360 C  CG  . MET A 328 ? 0.2112 0.2377 0.1783 0.0266  -0.0309 -0.0020 314 MET A CG  
2361 S  SD  . MET A 328 ? 0.2467 0.3409 0.2413 -0.0184 -0.0537 0.0494  314 MET A SD  
2362 C  CE  . MET A 328 ? 0.3500 0.3560 0.2962 -0.0086 -0.0564 0.1163  314 MET A CE  
2363 N  N   . ALA A 329 ? 0.1882 0.1869 0.1470 0.0191  -0.0201 0.0119  315 ALA A N   
2364 C  CA  . ALA A 329 ? 0.1825 0.1867 0.1718 0.0219  -0.0297 0.0114  315 ALA A CA  
2365 C  C   . ALA A 329 ? 0.2193 0.1915 0.2197 0.0091  -0.0205 -0.0018 315 ALA A C   
2366 O  O   . ALA A 329 ? 0.2261 0.2316 0.2341 0.0021  -0.0436 0.0130  315 ALA A O   
2367 C  CB  . ALA A 329 ? 0.1971 0.2162 0.1893 -0.0134 -0.0136 0.0441  315 ALA A CB  
2368 N  N   . ARG A 330 ? 0.2147 0.2289 0.2052 0.0298  -0.0228 0.0298  316 ARG A N   
2369 C  CA  . ARG A 330 ? 0.1810 0.2669 0.1975 0.0024  -0.0542 0.0205  316 ARG A CA  
2370 C  C   . ARG A 330 ? 0.2263 0.2804 0.2003 0.0012  -0.0036 0.0144  316 ARG A C   
2371 O  O   . ARG A 330 ? 0.2198 0.3342 0.2182 0.0272  -0.0735 0.0070  316 ARG A O   
2372 C  CB  . ARG A 330 ? 0.2000 0.3342 0.2072 0.0526  -0.0247 0.0485  316 ARG A CB  
2373 C  CG  . ARG A 330 ? 0.2653 0.4467 0.1861 0.0379  -0.0618 0.0602  316 ARG A CG  
2374 C  CD  . ARG A 330 ? 0.2884 0.4606 0.2380 0.1181  0.0514  0.0848  316 ARG A CD  
2375 N  NE  . ARG A 330 ? 0.6880 0.6262 0.5212 0.0959  0.1397  -0.1339 316 ARG A NE  
2376 C  CZ  . ARG A 330 ? 0.7072 0.6395 0.7600 0.2732  0.0897  -0.1226 316 ARG A CZ  
2377 N  NH1 . ARG A 330 ? 0.5010 0.6497 0.5297 0.2421  -0.1233 -0.0086 316 ARG A NH1 
2378 N  NH2 . ARG A 330 ? 0.9007 1.0756 0.9278 0.1561  -0.2033 0.0613  316 ARG A NH2 
2379 N  N   . LYS A 331 ? 0.2236 0.2503 0.1900 0.0372  -0.0337 0.0377  317 LYS A N   
2380 C  CA  . LYS A 331 ? 0.2079 0.2692 0.1763 0.0059  -0.0366 0.0135  317 LYS A CA  
2381 C  C   . LYS A 331 ? 0.2139 0.2269 0.1793 0.0356  -0.0531 0.0132  317 LYS A C   
2382 O  O   . LYS A 331 ? 0.2119 0.3131 0.1894 0.0243  -0.0662 0.0405  317 LYS A O   
2383 C  CB  . LYS A 331 ? 0.2434 0.2728 0.2200 0.0268  -0.0240 -0.0515 317 LYS A CB  
2384 C  CG  . LYS A 331 ? 0.3818 0.2515 0.2620 -0.0646 -0.0319 -0.0236 317 LYS A CG  
2385 C  CD  . LYS A 331 ? 0.4286 0.3457 0.3246 0.0067  -0.1491 0.0330  317 LYS A CD  
2386 C  CE  . LYS A 331 ? 0.4040 0.2908 0.4166 0.0319  -0.0045 0.0203  317 LYS A CE  
2387 N  NZ  . LYS A 331 ? 0.6094 0.5035 0.5675 0.0555  -0.0603 0.0492  317 LYS A NZ  
2388 N  N   . LYS A 332 ? 0.2456 0.2089 0.2081 0.0586  -0.0328 0.0403  318 LYS A N   
2389 C  CA  . LYS A 332 ? 0.2660 0.2291 0.1767 0.0668  -0.0058 0.0241  318 LYS A CA  
2390 C  C   . LYS A 332 ? 0.2731 0.2288 0.2581 0.0662  -0.0217 0.0444  318 LYS A C   
2391 O  O   . LYS A 332 ? 0.3432 0.2502 0.3936 0.0970  0.0209  0.0871  318 LYS A O   
2392 C  CB  . LYS A 332 ? 0.2547 0.2607 0.3384 0.0847  -0.0105 0.0354  318 LYS A CB  
2393 C  CG  . LYS A 332 ? 0.3637 0.3507 0.3033 0.0633  -0.0173 -0.0316 318 LYS A CG  
2394 C  CD  . LYS A 332 ? 0.4583 0.4725 0.5048 0.0336  0.1083  -0.0594 318 LYS A CD  
2395 N  N   . HIS A 333 ? 0.2220 0.2478 0.2274 0.0633  -0.0054 0.0334  319 HIS A N   
2396 C  CA  . HIS A 333 ? 0.2753 0.2137 0.2135 0.0717  0.0146  0.0339  319 HIS A CA  
2397 C  C   . HIS A 333 ? 0.2765 0.2574 0.2704 0.0299  -0.0384 0.0334  319 HIS A C   
2398 O  O   . HIS A 333 ? 0.3288 0.3142 0.2371 0.0551  0.0011  0.0628  319 HIS A O   
2399 C  CB  . HIS A 333 ? 0.2229 0.1833 0.2186 0.0512  0.0039  0.0361  319 HIS A CB  
2400 C  CG  . HIS A 333 ? 0.2505 0.1823 0.2574 0.0172  0.0206  0.0046  319 HIS A CG  
2401 N  ND1 . HIS A 333 ? 0.2794 0.2197 0.2570 0.0217  -0.0179 0.0376  319 HIS A ND1 
2402 C  CD2 . HIS A 333 ? 0.2402 0.2159 0.2458 0.0349  0.0196  0.0120  319 HIS A CD2 
2403 C  CE1 . HIS A 333 ? 0.2960 0.2419 0.3306 -0.0010 0.0216  0.0036  319 HIS A CE1 
2404 N  NE2 . HIS A 333 ? 0.2743 0.2713 0.3598 -0.0045 0.0144  0.0031  319 HIS A NE2 
2405 N  N   . LYS A 334 ? 0.3273 0.2787 0.3111 0.0066  0.0035  0.0898  320 LYS A N   
2406 C  CA  . LYS A 334 ? 0.4031 0.2808 0.3305 0.0085  0.0331  0.1722  320 LYS A CA  
2407 C  C   . LYS A 334 ? 0.3092 0.3663 0.2820 0.0175  0.0262  0.1086  320 LYS A C   
2408 O  O   . LYS A 334 ? 0.4478 0.4741 0.2709 0.0720  0.0221  0.0881  320 LYS A O   
2409 C  CB  . LYS A 334 ? 0.4163 0.3033 0.3980 -0.0023 0.1099  0.1138  320 LYS A CB  
2410 N  N   . ILE A 335 ? 0.2839 0.2820 0.3185 0.0306  0.0446  0.1324  321 ILE A N   
2411 C  CA  . ILE A 335 ? 0.3269 0.3402 0.3165 0.0559  0.0316  0.0674  321 ILE A CA  
2412 C  C   . ILE A 335 ? 0.3281 0.3829 0.2034 0.0179  -0.0015 0.0225  321 ILE A C   
2413 O  O   . ILE A 335 ? 0.3899 0.3989 0.2075 0.0900  0.0514  0.0639  321 ILE A O   
2414 C  CB  . ILE A 335 ? 0.3822 0.2949 0.2914 -0.0399 0.0782  0.0822  321 ILE A CB  
2415 C  CG1 . ILE A 335 ? 0.4517 0.3528 0.3898 -0.0859 0.0112  0.0785  321 ILE A CG1 
2416 C  CG2 . ILE A 335 ? 0.3568 0.3708 0.4142 0.0281  0.0503  0.0875  321 ILE A CG2 
2417 C  CD1 . ILE A 335 ? 0.6287 0.3375 0.5477 -0.1355 0.0091  0.0434  321 ILE A CD1 
2418 N  N   A MET A 336 ? 0.2770 0.2758 0.2214 0.0439  0.0397  0.0553  322 MET A N   
2419 N  N   B MET A 336 ? 0.2827 0.3023 0.2159 0.0653  0.0429  0.0756  322 MET A N   
2420 C  CA  A MET A 336 ? 0.2033 0.2652 0.1772 0.0291  -0.0002 0.0084  322 MET A CA  
2421 C  CA  B MET A 336 ? 0.2232 0.2980 0.2026 0.0497  0.0007  0.0223  322 MET A CA  
2422 C  C   A MET A 336 ? 0.2009 0.1912 0.2133 0.0344  -0.0061 0.0202  322 MET A C   
2423 C  C   B MET A 336 ? 0.2153 0.2167 0.2248 0.0546  -0.0097 0.0302  322 MET A C   
2424 O  O   A MET A 336 ? 0.2649 0.2349 0.2018 0.0323  -0.0008 0.0032  322 MET A O   
2425 O  O   B MET A 336 ? 0.2961 0.2619 0.2043 0.0465  -0.0040 0.0076  322 MET A O   
2426 C  CB  A MET A 336 ? 0.2132 0.2768 0.2477 0.0345  0.0371  0.0056  322 MET A CB  
2427 C  CB  B MET A 336 ? 0.2377 0.3241 0.3296 0.0616  0.0364  0.0202  322 MET A CB  
2428 C  CG  A MET A 336 ? 0.2124 0.2832 0.1901 0.0361  0.0034  0.0062  322 MET A CG  
2429 C  CG  B MET A 336 ? 0.3676 0.4197 0.4198 0.0246  -0.0011 -0.0010 322 MET A CG  
2430 S  SD  A MET A 336 ? 0.3737 0.3367 0.3374 0.0919  0.0054  0.0419  322 MET A SD  
2431 S  SD  B MET A 336 ? 0.2301 0.4426 0.4595 0.0628  -0.0228 0.0335  322 MET A SD  
2432 C  CE  A MET A 336 ? 0.3405 0.4403 0.5240 0.1219  0.0731  0.0306  322 MET A CE  
2433 C  CE  B MET A 336 ? 0.4600 0.4667 0.4700 0.0567  0.0100  0.0520  322 MET A CE  
2434 N  N   . ASN A 337 ? 0.2253 0.2489 0.1982 0.0323  -0.0030 0.0287  323 ASN A N   
2435 C  CA  . ASN A 337 ? 0.2180 0.2055 0.1879 0.0399  -0.0123 0.0342  323 ASN A CA  
2436 C  C   . ASN A 337 ? 0.2205 0.2365 0.1856 0.0329  -0.0002 0.0010  323 ASN A C   
2437 O  O   . ASN A 337 ? 0.2581 0.2659 0.2050 0.0944  -0.0029 0.0127  323 ASN A O   
2438 C  CB  . ASN A 337 ? 0.2285 0.2224 0.1846 0.0654  -0.0044 0.0043  323 ASN A CB  
2439 C  CG  . ASN A 337 ? 0.2081 0.2389 0.2098 0.0263  0.0259  0.0096  323 ASN A CG  
2440 O  OD1 . ASN A 337 ? 0.2263 0.2386 0.2080 0.0707  -0.0292 0.0002  323 ASN A OD1 
2441 N  ND2 . ASN A 337 ? 0.3852 0.2802 0.2171 0.0657  0.0017  0.0438  323 ASN A ND2 
2442 N  N   . ILE A 338 ? 0.2308 0.1986 0.1656 0.0443  0.0033  0.0160  324 ILE A N   
2443 C  CA  . ILE A 338 ? 0.2378 0.1881 0.2082 0.0601  0.0081  0.0157  324 ILE A CA  
2444 C  C   . ILE A 338 ? 0.2307 0.2268 0.2219 0.0570  0.0040  -0.0212 324 ILE A C   
2445 O  O   . ILE A 338 ? 0.2686 0.2999 0.3010 0.0721  -0.0753 0.0113  324 ILE A O   
2446 C  CB  . ILE A 338 ? 0.2873 0.1918 0.2118 0.0510  0.0186  0.0165  324 ILE A CB  
2447 C  CG1 . ILE A 338 ? 0.4093 0.2193 0.3854 0.0209  -0.0244 0.0455  324 ILE A CG1 
2448 C  CG2 . ILE A 338 ? 0.2820 0.2772 0.2454 0.0707  0.0174  0.0264  324 ILE A CG2 
2449 C  CD1 . ILE A 338 ? 0.2418 0.3600 0.4734 0.0132  -0.1625 0.0093  324 ILE A CD1 
2450 N  N   . GLU A 339 ? 0.2659 0.2166 0.1774 0.0504  -0.0459 -0.0171 325 GLU A N   
2451 C  CA  . GLU A 339 ? 0.2313 0.2517 0.2393 0.0381  -0.0546 -0.0353 325 GLU A CA  
2452 C  C   . GLU A 339 ? 0.2940 0.2552 0.3061 0.0536  -0.0284 -0.0187 325 GLU A C   
2453 O  O   . GLU A 339 ? 0.2914 0.2399 0.1925 0.0456  -0.0703 -0.0223 325 GLU A O   
2454 C  CB  . GLU A 339 ? 0.4691 0.4157 0.2593 0.0365  0.0088  -0.0459 325 GLU A CB  
2455 C  CG  . GLU A 339 ? 0.6247 0.4605 0.3121 0.0362  -0.0176 -0.0695 325 GLU A CG  
2456 C  CD  . GLU A 339 ? 0.8063 0.6164 0.4805 0.0555  0.0746  -0.0398 325 GLU A CD  
2457 O  OE1 . GLU A 339 ? 0.5800 0.7008 0.3794 0.0980  -0.0135 -0.0768 325 GLU A OE1 
2458 O  OE2 . GLU A 339 ? 0.5130 0.5233 0.4917 0.2408  -0.0559 0.0787  325 GLU A OE2 
2459 N  N   . GLU A 340 ? 0.2863 0.2712 0.2352 0.0152  -0.0728 -0.0304 326 GLU A N   
2460 C  CA  . GLU A 340 ? 0.2854 0.2950 0.1897 0.0182  -0.0607 -0.0363 326 GLU A CA  
2461 C  C   . GLU A 340 ? 0.3351 0.2538 0.2629 -0.0188 -0.0032 -0.0689 326 GLU A C   
2462 O  O   . GLU A 340 ? 0.3046 0.3056 0.2361 0.0427  -0.0287 -0.0712 326 GLU A O   
2463 C  CB  . GLU A 340 ? 0.2962 0.2895 0.3254 -0.0108 -0.1162 -0.0367 326 GLU A CB  
2464 C  CG  . GLU A 340 ? 0.4806 0.2986 0.3904 -0.0668 -0.0868 -0.0597 326 GLU A CG  
2465 C  CD  . GLU A 340 ? 0.5874 0.3861 0.6129 -0.0443 -0.0973 0.0146  326 GLU A CD  
2466 O  OE1 . GLU A 340 ? 0.6968 0.5090 0.7340 0.0068  -0.1626 -0.0687 326 GLU A OE1 
2467 O  OE2 . GLU A 340 ? 0.7316 0.5897 0.5411 0.0806  -0.0721 -0.2562 326 GLU A OE2 
2468 N  N   . GLY A 341 ? 0.3002 0.2307 0.2495 0.0217  -0.0325 -0.0593 327 GLY A N   
2469 C  CA  . GLY A 341 ? 0.2877 0.2015 0.3157 0.0288  -0.0692 -0.0719 327 GLY A CA  
2470 C  C   . GLY A 341 ? 0.2374 0.1950 0.2221 0.0262  -0.0306 -0.0450 327 GLY A C   
2471 O  O   . GLY A 341 ? 0.2424 0.2268 0.2719 0.0456  -0.0727 -0.0261 327 GLY A O   
2472 N  N   . ASP A 342 ? 0.2262 0.1818 0.2290 0.0435  -0.0445 -0.0294 328 ASP A N   
2473 C  CA  . ASP A 342 ? 0.2269 0.1602 0.2333 0.0477  -0.0213 -0.0112 328 ASP A CA  
2474 C  C   . ASP A 342 ? 0.1919 0.1892 0.2237 0.0372  -0.0123 -0.0200 328 ASP A C   
2475 O  O   . ASP A 342 ? 0.2300 0.2425 0.2161 0.0246  -0.0497 0.0084  328 ASP A O   
2476 C  CB  . ASP A 342 ? 0.2249 0.2422 0.2031 0.0258  -0.0276 -0.0403 328 ASP A CB  
2477 C  CG  . ASP A 342 ? 0.2571 0.2817 0.2549 0.0341  -0.0666 -0.0183 328 ASP A CG  
2478 O  OD1 . ASP A 342 ? 0.2433 0.2638 0.2650 0.0363  -0.0076 0.0103  328 ASP A OD1 
2479 O  OD2 . ASP A 342 ? 0.2749 0.2395 0.2388 0.0712  -0.0178 0.0301  328 ASP A OD2 
2480 N  N   . SER A 343 ? 0.2188 0.2056 0.2240 0.0624  -0.0319 -0.0291 329 SER A N   
2481 C  CA  . SER A 343 ? 0.2169 0.1961 0.2007 0.0623  -0.0616 -0.0431 329 SER A CA  
2482 C  C   . SER A 343 ? 0.1684 0.1636 0.1957 0.0290  -0.0161 -0.0137 329 SER A C   
2483 O  O   . SER A 343 ? 0.2141 0.2122 0.2103 0.0167  -0.0130 -0.0330 329 SER A O   
2484 C  CB  . SER A 343 ? 0.2584 0.2364 0.2000 0.0684  -0.0398 -0.0454 329 SER A CB  
2485 O  OG  . SER A 343 ? 0.2625 0.1782 0.2720 0.0499  -0.0448 -0.0425 329 SER A OG  
2486 N  N   . ILE A 344 ? 0.2185 0.2030 0.2050 0.0513  -0.0302 -0.0247 330 ILE A N   
2487 C  CA  . ILE A 344 ? 0.2130 0.1874 0.1991 0.0479  -0.0400 -0.0393 330 ILE A CA  
2488 C  C   . ILE A 344 ? 0.2113 0.1945 0.1834 0.0087  -0.0092 -0.0164 330 ILE A C   
2489 O  O   . ILE A 344 ? 0.2188 0.2075 0.2221 0.0106  -0.0422 -0.0128 330 ILE A O   
2490 C  CB  . ILE A 344 ? 0.2255 0.2202 0.2033 0.0561  -0.0602 -0.0125 330 ILE A CB  
2491 C  CG1 . ILE A 344 ? 0.2328 0.3327 0.3307 0.1348  -0.0117 -0.0156 330 ILE A CG1 
2492 C  CG2 . ILE A 344 ? 0.2763 0.2473 0.2631 0.0639  -0.0499 0.0193  330 ILE A CG2 
2493 C  CD1 . ILE A 344 ? 0.2268 0.3156 0.3155 0.0755  -0.0315 0.0949  330 ILE A CD1 
2494 N  N   . PHE A 345 ? 0.2136 0.1881 0.1865 0.0235  -0.0098 -0.0111 331 PHE A N   
2495 C  CA  . PHE A 345 ? 0.2385 0.2017 0.1787 0.0102  -0.0152 0.0022  331 PHE A CA  
2496 C  C   . PHE A 345 ? 0.1776 0.1993 0.1644 -0.0135 -0.0161 -0.0076 331 PHE A C   
2497 O  O   . PHE A 345 ? 0.2110 0.1889 0.1883 -0.0048 -0.0027 0.0002  331 PHE A O   
2498 C  CB  . PHE A 345 ? 0.2307 0.2565 0.1571 -0.0015 -0.0435 -0.0021 331 PHE A CB  
2499 C  CG  . PHE A 345 ? 0.2245 0.3123 0.2714 0.0516  -0.0283 -0.0040 331 PHE A CG  
2500 C  CD1 . PHE A 345 ? 0.3112 0.4277 0.2095 0.0045  -0.0981 0.0311  331 PHE A CD1 
2501 C  CD2 . PHE A 345 ? 0.2906 0.3078 0.2021 0.0740  -0.0091 -0.0305 331 PHE A CD2 
2502 C  CE1 . PHE A 345 ? 0.3725 0.4995 0.2918 0.0033  -0.0145 0.0619  331 PHE A CE1 
2503 C  CE2 . PHE A 345 ? 0.3493 0.3851 0.2291 0.0571  -0.0322 -0.0266 331 PHE A CE2 
2504 C  CZ  . PHE A 345 ? 0.2830 0.4284 0.2199 0.0116  -0.0728 -0.0187 331 PHE A CZ  
2505 N  N   . LEU A 346 ? 0.2554 0.2306 0.2035 -0.0029 0.0089  -0.0200 332 LEU A N   
2506 C  CA  . LEU A 346 ? 0.3028 0.2543 0.2089 -0.0031 0.0186  -0.0532 332 LEU A CA  
2507 C  C   . LEU A 346 ? 0.3493 0.3149 0.2836 0.0332  0.0064  0.0019  332 LEU A C   
2508 O  O   . LEU A 346 ? 0.5011 0.3496 0.2744 -0.0128 0.0711  0.0684  332 LEU A O   
2509 C  CB  . LEU A 346 ? 0.3263 0.3422 0.2851 -0.0015 0.0654  -0.0780 332 LEU A CB  
2510 C  CG  . LEU A 346 ? 0.3461 0.4309 0.3576 -0.0200 0.0631  -0.1042 332 LEU A CG  
2511 C  CD1 . LEU A 346 ? 0.3937 0.5965 0.3344 0.0870  0.0210  -0.1292 332 LEU A CD1 
2512 C  CD2 . LEU A 346 ? 0.3921 0.7338 0.5941 -0.1278 0.0035  -0.1044 332 LEU A CD2 
2513 N  N   . ALA A 347 ? 0.3818 0.4395 0.2379 -0.0068 -0.0995 0.0336  333 ALA A N   
2514 C  CA  . ALA A 347 ? 0.4903 0.4957 0.3103 -0.0508 -0.0826 0.0226  333 ALA A CA  
2515 C  C   . ALA A 347 ? 0.3842 0.4869 0.3612 0.0259  -0.0901 -0.0348 333 ALA A C   
2516 O  O   . ALA A 347 ? 0.5187 0.5214 0.4157 -0.0463 0.0051  0.0315  333 ALA A O   
2517 C  CB  . ALA A 347 ? 0.4675 0.4505 0.2771 0.0504  -0.1398 0.1016  333 ALA A CB  
2518 N  N   . ILE A 348 ? 0.5321 0.4747 0.3548 -0.0029 0.0279  -0.0445 334 ILE A N   
2519 C  CA  . ILE A 348 ? 0.5955 0.4492 0.3191 0.0177  0.0026  -0.0389 334 ILE A CA  
2520 C  C   . ILE A 348 ? 0.5032 0.5904 0.5783 0.0631  0.2009  0.1316  334 ILE A C   
2521 O  O   . ILE A 348 ? 0.6445 0.5849 0.6596 -0.0401 0.0548  0.2742  334 ILE A O   
2522 C  CB  . ILE A 348 ? 0.4673 0.5518 0.5451 0.1068  -0.0240 0.1001  334 ILE A CB  
2523 C  CG1 . ILE A 348 ? 0.3809 0.6953 0.6577 -0.0675 0.0088  0.1975  334 ILE A CG1 
2524 C  CG2 . ILE A 348 ? 0.6538 0.4973 0.5401 0.1472  0.0079  0.0145  334 ILE A CG2 
2525 C  CD1 . ILE A 348 ? 0.6192 0.6754 0.8713 -0.1232 0.0603  0.3067  334 ILE A CD1 
2526 N  N   . THR A 349 ? 0.5742 0.5377 0.5360 -0.0909 -0.0852 -0.0567 335 THR A N   
2527 C  CA  . THR A 349 ? 0.3571 0.5570 0.8236 0.0033  -0.2503 0.3303  335 THR A CA  
2528 C  C   . THR A 349 ? 0.4320 0.3559 1.3016 -0.2287 -0.2402 0.1551  335 THR A C   
2529 O  O   . THR A 349 ? 0.3790 0.5141 0.6575 -0.0260 -0.0427 -0.0030 335 THR A O   
2530 C  CB  . THR A 349 ? 0.3524 0.7233 0.4520 -0.3598 -0.2486 0.1592  335 THR A CB  
2531 N  N   . ALA A 350 ? 0.7783 0.4355 1.2979 -0.1671 -0.0517 0.0416  336 ALA A N   
2532 C  CA  . ALA A 350 ? 0.7600 0.5927 0.9504 -0.0413 -0.2069 0.0476  336 ALA A CA  
2533 C  C   . ALA A 350 ? 0.6809 0.8313 0.6510 0.0378  -0.1767 -0.0442 336 ALA A C   
2534 O  O   . ALA A 350 ? 0.7962 0.9937 0.7255 0.0728  -0.2388 0.1871  336 ALA A O   
2535 C  CB  . ALA A 350 ? 0.6678 0.5516 0.7080 -0.1774 -0.0792 0.0733  336 ALA A CB  
2536 N  N   . SER A 351 ? 0.6913 0.4585 0.7998 -0.0573 -0.2628 -0.0979 337 SER A N   
2537 C  CA  . SER A 351 ? 0.5120 0.4248 0.6485 -0.0175 -0.1749 -0.0298 337 SER A CA  
2538 C  C   . SER A 351 ? 0.6391 0.4300 0.5723 -0.0002 0.0654  0.1192  337 SER A C   
2539 O  O   . SER A 351 ? 0.7030 0.3937 0.6580 0.0724  -0.0409 0.0459  337 SER A O   
2540 C  CB  . SER A 351 ? 0.5336 0.3704 0.5845 -0.0431 -0.2136 0.0286  337 SER A CB  
2541 O  OG  . SER A 351 ? 0.5563 0.2766 0.5062 -0.0899 -0.1324 0.0400  337 SER A OG  
2542 N  N   . ALA A 352 ? 0.4502 0.3675 0.2756 -0.1669 -0.0890 0.0125  338 ALA A N   
2543 C  CA  . ALA A 352 ? 0.4956 0.5805 0.4254 -0.2260 -0.0999 -0.0055 338 ALA A CA  
2544 C  C   . ALA A 352 ? 0.4300 0.5133 0.3080 -0.1491 -0.0667 0.0052  338 ALA A C   
2545 O  O   . ALA A 352 ? 0.4084 0.6254 0.2824 -0.1075 0.0365  -0.0724 338 ALA A O   
2546 C  CB  . ALA A 352 ? 0.6179 0.6705 0.4788 -0.2028 -0.0446 -0.0646 338 ALA A CB  
2547 N  N   . ASN A 353 ? 0.5868 0.3077 0.2836 -0.0950 0.0085  -0.0257 339 ASN A N   
2548 C  CA  . ASN A 353 ? 0.6271 0.4370 0.4035 -0.0973 -0.0104 0.0663  339 ASN A CA  
2549 C  C   . ASN A 353 ? 0.6579 0.4512 0.3393 -0.0394 -0.1067 0.0481  339 ASN A C   
2550 O  O   . ASN A 353 ? 0.8175 0.3886 0.3115 -0.1057 -0.2499 0.0635  339 ASN A O   
2551 C  CB  . ASN A 353 ? 0.6203 0.5407 0.3781 -0.0001 -0.0516 0.0049  339 ASN A CB  
2552 C  CG  . ASN A 353 ? 0.8981 0.5856 0.4888 -0.1689 0.1155  -0.1162 339 ASN A CG  
2553 O  OD1 . ASN A 353 ? 0.7839 0.5949 0.6610 -0.0305 -0.0562 0.1614  339 ASN A OD1 
2554 N  ND2 . ASN A 353 ? 0.8217 0.3381 0.2992 -0.1394 0.0863  -0.0308 339 ASN A ND2 
2555 N  N   . MET A 354 ? 0.4990 0.2839 0.2813 -0.0508 0.0219  -0.0107 340 MET A N   
2556 C  CA  . MET A 354 ? 0.5361 0.3031 0.3187 -0.0989 -0.0356 -0.0887 340 MET A CA  
2557 C  C   . MET A 354 ? 0.5075 0.2381 0.3808 -0.0513 0.1117  0.0366  340 MET A C   
2558 O  O   . MET A 354 ? 0.4580 0.2663 0.2953 -0.1490 0.0463  -0.0436 340 MET A O   
2559 C  CB  . MET A 354 ? 0.5366 0.3804 0.4048 -0.1812 -0.0329 -0.0404 340 MET A CB  
2560 C  CG  . MET A 354 ? 0.5385 0.4492 0.2800 -0.1334 0.0160  -0.0243 340 MET A CG  
2561 S  SD  . MET A 354 ? 0.5475 0.4635 0.4104 -0.1357 0.0251  0.0157  340 MET A SD  
2562 C  CE  . MET A 354 ? 0.6571 0.5448 0.5205 -0.0896 0.0436  -0.2050 340 MET A CE  
2563 N  N   . GLU A 355 ? 0.4935 0.3003 0.2272 -0.1438 0.0922  -0.0124 341 GLU A N   
2564 C  CA  . GLU A 355 ? 0.4744 0.1953 0.2842 -0.0938 0.0933  0.0006  341 GLU A CA  
2565 C  C   . GLU A 355 ? 0.3612 0.2473 0.2574 -0.0692 0.0558  0.0600  341 GLU A C   
2566 O  O   . GLU A 355 ? 0.4060 0.1636 0.2708 -0.0691 0.0434  -0.0068 341 GLU A O   
2567 C  CB  . GLU A 355 ? 0.4389 0.3205 0.3633 -0.1682 0.0766  -0.0128 341 GLU A CB  
2568 C  CG  . GLU A 355 ? 0.4291 0.2892 0.3635 -0.1326 0.0471  0.0290  341 GLU A CG  
2569 C  CD  . GLU A 355 ? 0.6468 0.6680 0.4330 -0.1212 -0.0003 0.0084  341 GLU A CD  
2570 O  OE1 . GLU A 355 ? 0.4369 0.3924 0.3418 -0.0900 0.0168  -0.0514 341 GLU A OE1 
2571 O  OE2 . GLU A 355 ? 0.5032 0.4177 0.3054 -0.0653 0.0399  -0.0241 341 GLU A OE2 
2572 N  N   . VAL A 356 ? 0.3443 0.2347 0.2910 -0.0743 0.0526  -0.0196 342 VAL A N   
2573 C  CA  . VAL A 356 ? 0.3810 0.2787 0.2662 -0.0677 0.0646  0.0487  342 VAL A CA  
2574 C  C   . VAL A 356 ? 0.4441 0.2491 0.2905 -0.0669 0.0632  -0.0119 342 VAL A C   
2575 O  O   . VAL A 356 ? 0.3518 0.2184 0.2498 -0.0665 0.0285  -0.0023 342 VAL A O   
2576 C  CB  . VAL A 356 ? 0.3667 0.2594 0.3112 -0.0282 0.0904  -0.0065 342 VAL A CB  
2577 C  CG1 . VAL A 356 ? 0.4389 0.2656 0.3508 0.0149  0.0911  0.0505  342 VAL A CG1 
2578 C  CG2 . VAL A 356 ? 0.4459 0.3713 0.3052 -0.0181 0.1101  0.0734  342 VAL A CG2 
2579 N  N   . ILE A 357 ? 0.4497 0.1822 0.2886 -0.0571 0.0723  0.0087  343 ILE A N   
2580 C  CA  . ILE A 357 ? 0.3950 0.2017 0.2323 -0.0423 0.0462  0.0457  343 ILE A CA  
2581 C  C   . ILE A 357 ? 0.2448 0.1854 0.2247 -0.0618 0.0327  0.0093  343 ILE A C   
2582 O  O   . ILE A 357 ? 0.3140 0.1841 0.2054 -0.0482 0.0329  0.0087  343 ILE A O   
2583 C  CB  . ILE A 357 ? 0.3806 0.2058 0.2956 -0.0246 0.0290  0.0031  343 ILE A CB  
2584 C  CG1 . ILE A 357 ? 0.4878 0.1769 0.3350 -0.0352 0.0476  0.0427  343 ILE A CG1 
2585 C  CG2 . ILE A 357 ? 0.4254 0.2931 0.3264 -0.1185 0.0877  0.0148  343 ILE A CG2 
2586 C  CD1 . ILE A 357 ? 0.6048 0.2565 0.3640 -0.0289 0.0878  0.0146  343 ILE A CD1 
2587 N  N   . ILE A 358 ? 0.2955 0.1860 0.2572 -0.0884 -0.0071 -0.0082 344 ILE A N   
2588 C  CA  . ILE A 358 ? 0.2611 0.2048 0.2240 -0.0804 0.0017  0.0109  344 ILE A CA  
2589 C  C   . ILE A 358 ? 0.2468 0.2094 0.2423 -0.0335 0.0276  0.0181  344 ILE A C   
2590 O  O   . ILE A 358 ? 0.2474 0.2003 0.2221 -0.0446 -0.0015 0.0041  344 ILE A O   
2591 C  CB  . ILE A 358 ? 0.3064 0.2608 0.3286 -0.0969 -0.0544 0.0162  344 ILE A CB  
2592 C  CG1 . ILE A 358 ? 0.3713 0.3526 0.3268 -0.1596 -0.0081 0.0122  344 ILE A CG1 
2593 C  CG2 . ILE A 358 ? 0.2345 0.3422 0.2083 -0.0418 -0.0456 0.0066  344 ILE A CG2 
2594 C  CD1 . ILE A 358 ? 0.5577 0.5034 0.4172 -0.1593 0.0481  0.0723  344 ILE A CD1 
2595 N  N   . ALA A 359 ? 0.2610 0.1935 0.2071 -0.0592 -0.0101 -0.0169 345 ALA A N   
2596 C  CA  . ALA A 359 ? 0.2796 0.1172 0.2715 -0.0616 0.0008  0.0119  345 ALA A CA  
2597 C  C   . ALA A 359 ? 0.2227 0.1532 0.2402 -0.0242 0.0255  0.0225  345 ALA A C   
2598 O  O   . ALA A 359 ? 0.2523 0.1622 0.2405 -0.0438 -0.0037 0.0088  345 ALA A O   
2599 C  CB  . ALA A 359 ? 0.3273 0.1954 0.2558 -0.0724 0.0300  0.0297  345 ALA A CB  
2600 N  N   . ASP A 360 ? 0.2342 0.1664 0.2161 -0.0220 0.0260  0.0082  346 ASP A N   
2601 C  CA  . ASP A 360 ? 0.2529 0.1867 0.2120 -0.0198 0.0060  0.0040  346 ASP A CA  
2602 C  C   . ASP A 360 ? 0.2106 0.1795 0.2150 0.0010  -0.0070 0.0202  346 ASP A C   
2603 O  O   . ASP A 360 ? 0.1951 0.1904 0.2209 -0.0143 0.0115  0.0133  346 ASP A O   
2604 C  CB  . ASP A 360 ? 0.2772 0.1633 0.2645 -0.0109 0.0050  0.0209  346 ASP A CB  
2605 C  CG  . ASP A 360 ? 0.3192 0.2798 0.4072 -0.0168 0.0503  0.0435  346 ASP A CG  
2606 O  OD1 . ASP A 360 ? 0.2978 0.2978 0.3629 -0.0516 0.0379  0.0336  346 ASP A OD1 
2607 O  OD2 . ASP A 360 ? 0.4838 0.3030 0.3326 0.0468  0.0640  0.0000  346 ASP A OD2 
2608 N  N   . THR A 361 ? 0.2034 0.1554 0.2072 -0.0412 0.0070  0.0183  347 THR A N   
2609 C  CA  . THR A 361 ? 0.1776 0.1748 0.2142 -0.0172 -0.0188 0.0192  347 THR A CA  
2610 C  C   . THR A 361 ? 0.1489 0.1884 0.2026 -0.0098 0.0031  0.0087  347 THR A C   
2611 O  O   . THR A 361 ? 0.1970 0.1902 0.2304 -0.0132 0.0113  0.0162  347 THR A O   
2612 C  CB  . THR A 361 ? 0.2124 0.1835 0.2308 -0.0088 -0.0115 0.0276  347 THR A CB  
2613 O  OG1 . THR A 361 ? 0.2642 0.1911 0.2344 -0.0409 0.0091  0.0292  347 THR A OG1 
2614 C  CG2 . THR A 361 ? 0.2068 0.2294 0.2422 -0.0372 -0.0080 0.0005  347 THR A CG2 
2615 N  N   . LEU A 362 ? 0.2299 0.1810 0.1942 -0.0078 -0.0228 -0.0026 348 LEU A N   
2616 C  CA  . LEU A 362 ? 0.2194 0.1888 0.2271 -0.0046 -0.0152 -0.0208 348 LEU A CA  
2617 C  C   . LEU A 362 ? 0.2235 0.2005 0.1914 -0.0014 -0.0273 0.0172  348 LEU A C   
2618 O  O   . LEU A 362 ? 0.2192 0.1914 0.2197 0.0087  -0.0286 0.0086  348 LEU A O   
2619 C  CB  . LEU A 362 ? 0.2885 0.2077 0.2193 0.0033  -0.0692 -0.0052 348 LEU A CB  
2620 C  CG  . LEU A 362 ? 0.3694 0.2574 0.3054 -0.0355 -0.1216 -0.0339 348 LEU A CG  
2621 C  CD1 . LEU A 362 ? 0.4099 0.2977 0.3091 0.0056  -0.1391 -0.0033 348 LEU A CD1 
2622 C  CD2 . LEU A 362 ? 0.4340 0.3440 0.3222 -0.0038 -0.1516 -0.0377 348 LEU A CD2 
2623 N  N   . ASN A 363 ? 0.2265 0.1382 0.1761 -0.0366 -0.0258 0.0077  349 ASN A N   
2624 C  CA  . ASN A 363 ? 0.2189 0.1829 0.2116 -0.0256 -0.0488 -0.0203 349 ASN A CA  
2625 C  C   . ASN A 363 ? 0.1946 0.2168 0.2110 -0.0015 -0.0031 -0.0036 349 ASN A C   
2626 O  O   . ASN A 363 ? 0.2350 0.2343 0.2027 -0.0346 -0.0056 0.0038  349 ASN A O   
2627 C  CB  . ASN A 363 ? 0.2224 0.1932 0.1797 -0.0265 0.0117  0.0013  349 ASN A CB  
2628 C  CG  . ASN A 363 ? 0.2455 0.1682 0.2151 -0.0241 -0.0092 -0.0067 349 ASN A CG  
2629 O  OD1 . ASN A 363 ? 0.3360 0.2162 0.2317 0.0019  0.0248  0.0197  349 ASN A OD1 
2630 N  ND2 . ASN A 363 ? 0.2627 0.2085 0.2282 -0.0976 0.0326  -0.0149 349 ASN A ND2 
2631 N  N   . GLU A 364 ? 0.2186 0.2101 0.1775 0.0000  -0.0279 0.0113  350 GLU A N   
2632 C  CA  . GLU A 364 ? 0.1818 0.2466 0.2103 -0.0228 -0.0337 -0.0110 350 GLU A CA  
2633 C  C   . GLU A 364 ? 0.2121 0.1864 0.1763 0.0102  -0.0110 0.0117  350 GLU A C   
2634 O  O   . GLU A 364 ? 0.1983 0.2623 0.1921 0.0101  -0.0248 -0.0061 350 GLU A O   
2635 C  CB  . GLU A 364 ? 0.2793 0.2830 0.1961 0.0232  0.0060  0.0431  350 GLU A CB  
2636 C  CG  . GLU A 364 ? 0.3101 0.2583 0.2044 0.0186  -0.0100 0.0056  350 GLU A CG  
2637 C  CD  . GLU A 364 ? 0.2905 0.3251 0.2866 0.0134  0.0287  0.0481  350 GLU A CD  
2638 O  OE1 . GLU A 364 ? 0.3591 0.3296 0.2685 0.0136  -0.0038 0.0377  350 GLU A OE1 
2639 O  OE2 . GLU A 364 ? 0.3594 0.3401 0.2519 0.0810  0.0533  0.0164  350 GLU A OE2 
2640 N  N   . LEU A 365 ? 0.1930 0.1768 0.2056 0.0000  -0.0194 0.0027  351 LEU A N   
2641 C  CA  . LEU A 365 ? 0.2159 0.1819 0.1714 -0.0074 -0.0120 0.0164  351 LEU A CA  
2642 C  C   . LEU A 365 ? 0.1938 0.2559 0.2274 0.0062  -0.0080 0.0063  351 LEU A C   
2643 O  O   . LEU A 365 ? 0.2583 0.2466 0.2183 0.0019  -0.0308 -0.0170 351 LEU A O   
2644 C  CB  . LEU A 365 ? 0.1999 0.2237 0.1942 -0.0329 -0.0218 -0.0078 351 LEU A CB  
2645 C  CG  . LEU A 365 ? 0.1985 0.2578 0.1669 0.0022  -0.0131 -0.0241 351 LEU A CG  
2646 C  CD1 . LEU A 365 ? 0.2090 0.2527 0.2654 -0.0022 -0.0509 -0.0031 351 LEU A CD1 
2647 C  CD2 . LEU A 365 ? 0.1774 0.2281 0.2913 0.0213  0.0038  0.0089  351 LEU A CD2 
2648 N  N   . VAL A 366 ? 0.2737 0.1802 0.2151 -0.0230 -0.0167 -0.0103 352 VAL A N   
2649 C  CA  . VAL A 366 ? 0.2776 0.2329 0.2198 -0.0026 -0.0188 0.0006  352 VAL A CA  
2650 C  C   . VAL A 366 ? 0.2842 0.2378 0.2156 -0.0148 0.0027  -0.0034 352 VAL A C   
2651 O  O   . VAL A 366 ? 0.2961 0.2472 0.2534 -0.0286 -0.0106 -0.0362 352 VAL A O   
2652 C  CB  . VAL A 366 ? 0.3309 0.1793 0.2155 -0.0267 -0.0167 -0.0171 352 VAL A CB  
2653 C  CG1 . VAL A 366 ? 0.4490 0.2650 0.2534 -0.0359 0.0104  -0.0281 352 VAL A CG1 
2654 C  CG2 . VAL A 366 ? 0.3622 0.2105 0.1967 0.0326  -0.0415 -0.0049 352 VAL A CG2 
2655 N  N   . ARG A 367 ? 0.2480 0.2567 0.1977 -0.0503 -0.0302 0.0043  353 ARG A N   
2656 C  CA  . ARG A 367 ? 0.2428 0.2714 0.2101 -0.0141 -0.0346 -0.0449 353 ARG A CA  
2657 C  C   . ARG A 367 ? 0.3184 0.3614 0.1773 -0.0260 -0.0361 -0.0553 353 ARG A C   
2658 O  O   . ARG A 367 ? 0.2923 0.4144 0.2495 -0.0558 -0.0545 -0.0705 353 ARG A O   
2659 C  CB  . ARG A 367 ? 0.2313 0.3545 0.2695 0.0186  -0.0697 -0.0805 353 ARG A CB  
2660 C  CG  . ARG A 367 ? 0.4028 0.3145 0.4879 -0.0044 -0.0436 0.0177  353 ARG A CG  
2661 C  CD  . ARG A 367 ? 0.4364 0.4521 0.6870 -0.0882 -0.1488 0.0298  353 ARG A CD  
2662 N  NE  . ARG A 367 ? 0.4807 0.4838 0.5964 -0.1457 -0.0184 0.0401  353 ARG A NE  
2663 C  CZ  . ARG A 367 ? 0.4818 0.3618 0.5080 -0.0528 0.0710  0.0338  353 ARG A CZ  
2664 N  NH1 . ARG A 367 ? 0.4064 0.3516 0.3777 -0.0463 0.0710  0.0680  353 ARG A NH1 
2665 N  NH2 . ARG A 367 ? 0.4977 0.3610 0.4245 0.0285  -0.0934 0.0183  353 ARG A NH2 
2666 N  N   . ALA A 368 ? 0.2203 0.2808 0.2160 0.0050  -0.0120 -0.0231 354 ALA A N   
2667 C  CA  . ALA A 368 ? 0.2415 0.3304 0.2346 0.0199  -0.0197 -0.0278 354 ALA A CA  
2668 C  C   . ALA A 368 ? 0.3020 0.2832 0.2255 -0.0072 -0.0071 -0.0368 354 ALA A C   
2669 O  O   . ALA A 368 ? 0.3293 0.3771 0.2085 0.0553  -0.0078 0.0119  354 ALA A O   
2670 C  CB  . ALA A 368 ? 0.3173 0.3312 0.2003 0.0490  0.0155  0.0334  354 ALA A CB  
2671 N  N   . GLY A 369 ? 0.2536 0.2721 0.2477 0.0257  -0.0169 -0.0471 355 GLY A N   
2672 C  CA  . GLY A 369 ? 0.2872 0.2363 0.2444 -0.0285 -0.0390 -0.0429 355 GLY A CA  
2673 C  C   . GLY A 369 ? 0.2613 0.2807 0.2393 -0.0146 0.0079  0.0291  355 GLY A C   
2674 O  O   . GLY A 369 ? 0.2826 0.2700 0.2896 0.0418  -0.0422 -0.0436 355 GLY A O   
2675 N  N   . ALA A 370 ? 0.2033 0.2179 0.2526 0.0178  -0.0332 -0.0117 356 ALA A N   
2676 C  CA  . ALA A 370 ? 0.1903 0.2329 0.2446 0.0033  -0.0216 0.0015  356 ALA A CA  
2677 C  C   . ALA A 370 ? 0.2314 0.2093 0.2048 -0.0098 -0.0221 -0.0236 356 ALA A C   
2678 O  O   . ALA A 370 ? 0.2598 0.3035 0.2495 -0.0134 -0.0417 -0.0003 356 ALA A O   
2679 C  CB  . ALA A 370 ? 0.2561 0.1826 0.2580 -0.0014 -0.0077 0.0370  356 ALA A CB  
2680 N  N   . HIS A 371 ? 0.2566 0.2404 0.2853 -0.0188 -0.0421 0.0210  357 HIS A N   
2681 C  CA  . HIS A 371 ? 0.2849 0.2377 0.2502 0.0138  -0.0371 0.0280  357 HIS A CA  
2682 C  C   . HIS A 371 ? 0.2879 0.1800 0.2248 0.0186  -0.0313 -0.0031 357 HIS A C   
2683 O  O   . HIS A 371 ? 0.3379 0.3085 0.2088 -0.0027 -0.0369 -0.0291 357 HIS A O   
2684 C  CB  . HIS A 371 ? 0.3879 0.2064 0.2816 0.0470  -0.0879 -0.0412 357 HIS A CB  
2685 C  CG  . HIS A 371 ? 0.4399 0.3100 0.3750 0.0554  -0.0522 -0.0674 357 HIS A CG  
2686 N  ND1 . HIS A 371 ? 0.4629 0.3943 0.4080 -0.0336 -0.1067 -0.0979 357 HIS A ND1 
2687 C  CD2 . HIS A 371 ? 0.5593 0.3847 0.4645 0.0574  0.0068  -0.0970 357 HIS A CD2 
2688 C  CE1 . HIS A 371 ? 0.7557 0.3267 0.4329 -0.1301 -0.0165 -0.1476 357 HIS A CE1 
2689 N  NE2 . HIS A 371 ? 0.7554 0.3477 0.5532 -0.1279 -0.0285 -0.1657 357 HIS A NE2 
2690 N  N   . ILE A 372 ? 0.3135 0.2277 0.2800 0.0316  -0.0555 0.0104  358 ILE A N   
2691 C  CA  . ILE A 372 ? 0.2558 0.2375 0.2509 0.0387  -0.0665 0.0142  358 ILE A CA  
2692 C  C   . ILE A 372 ? 0.2295 0.2185 0.2546 0.0283  -0.0029 0.0302  358 ILE A C   
2693 O  O   . ILE A 372 ? 0.2894 0.2536 0.3046 0.0171  -0.0827 0.0464  358 ILE A O   
2694 C  CB  . ILE A 372 ? 0.2735 0.3111 0.2496 -0.0164 -0.0792 0.0243  358 ILE A CB  
2695 C  CG1 . ILE A 372 ? 0.2353 0.4423 0.3474 0.0125  -0.1000 -0.1083 358 ILE A CG1 
2696 C  CG2 . ILE A 372 ? 0.2357 0.3476 0.2626 0.0514  -0.0587 -0.0083 358 ILE A CG2 
2697 C  CD1 . ILE A 372 ? 0.5038 0.4221 0.4067 0.0358  -0.0986 0.0012  358 ILE A CD1 
2698 N  N   . ILE A 373 ? 0.2533 0.1724 0.2214 0.0457  -0.0293 0.0211  359 ILE A N   
2699 C  CA  . ILE A 373 ? 0.2866 0.2188 0.2493 0.0600  -0.0705 -0.0074 359 ILE A CA  
2700 C  C   . ILE A 373 ? 0.2566 0.2391 0.2793 0.0085  -0.0582 -0.0121 359 ILE A C   
2701 O  O   . ILE A 373 ? 0.2819 0.3192 0.2088 0.0332  -0.0620 0.0106  359 ILE A O   
2702 C  CB  . ILE A 373 ? 0.2518 0.2278 0.3048 0.0865  -0.0439 0.0422  359 ILE A CB  
2703 C  CG1 . ILE A 373 ? 0.2657 0.2415 0.2295 0.0527  -0.0217 0.0129  359 ILE A CG1 
2704 C  CG2 . ILE A 373 ? 0.2447 0.2487 0.2574 0.0741  -0.0664 0.0306  359 ILE A CG2 
2705 C  CD1 . ILE A 373 ? 0.2642 0.2700 0.2420 0.0401  0.0073  0.0021  359 ILE A CD1 
2706 N  N   . PRO A 374 ? 0.3551 0.3347 0.3308 -0.0210 -0.0457 0.0812  360 PRO A N   
2707 C  CA  . PRO A 374 ? 0.4519 0.3893 0.2925 -0.0285 -0.0297 0.0940  360 PRO A CA  
2708 C  C   . PRO A 374 ? 0.4054 0.5764 0.2290 0.0148  -0.0444 0.0682  360 PRO A C   
2709 O  O   . PRO A 374 ? 0.3383 0.4514 0.2553 -0.0149 -0.0359 0.0561  360 PRO A O   
2710 C  CB  . PRO A 374 ? 0.5313 0.3789 0.4131 -0.1082 -0.0422 0.0731  360 PRO A CB  
2711 C  CG  . PRO A 374 ? 0.4484 0.3614 0.4476 -0.0704 -0.0381 0.1713  360 PRO A CG  
2712 C  CD  . PRO A 374 ? 0.3741 0.3660 0.3483 -0.0083 -0.1197 0.0561  360 PRO A CD  
2713 N  N   . ASN A 375 ? 0.4588 0.7068 0.3478 0.0955  0.0464  0.0583  361 ASN A N   
2714 C  CA  . ASN A 375 ? 0.5284 0.4814 0.3802 -0.0097 -0.0076 -0.0604 361 ASN A CA  
2715 C  C   . ASN A 375 ? 0.4956 0.4235 0.3872 -0.0770 -0.0327 0.0825  361 ASN A C   
2716 O  O   . ASN A 375 ? 0.5825 0.4541 0.6014 -0.1526 -0.1401 0.2177  361 ASN A O   
2717 C  CB  . ASN A 375 ? 0.7094 0.4105 0.4343 -0.0139 0.0530  -0.0810 361 ASN A CB  
2718 C  CG  . ASN A 375 ? 0.8769 0.6584 0.4264 -0.0882 0.0007  -0.1638 361 ASN A CG  
2719 O  OD1 . ASN A 375 ? 1.1039 0.7145 0.6154 -0.0678 0.0222  0.0187  361 ASN A OD1 
2720 N  ND2 . ASN A 375 ? 0.6390 0.5337 0.6466 -0.1506 0.1202  -0.2330 361 ASN A ND2 
2721 N  N   . ASN A 376 ? 0.5293 0.3235 0.3942 0.0039  -0.0608 0.0315  362 ASN A N   
2722 C  CA  . ASN A 376 ? 0.4371 0.2987 0.4299 -0.0363 -0.1103 -0.0358 362 ASN A CA  
2723 C  C   . ASN A 376 ? 0.5223 0.3360 0.4830 -0.0342 -0.0716 0.0069  362 ASN A C   
2724 O  O   . ASN A 376 ? 0.5818 0.3102 0.3721 -0.0111 -0.0439 -0.0010 362 ASN A O   
2725 C  CB  . ASN A 376 ? 0.4197 0.3545 0.4549 -0.0442 0.0353  -0.0936 362 ASN A CB  
2726 C  CG  . ASN A 376 ? 0.5021 0.3473 0.5743 -0.0165 0.0074  -0.1094 362 ASN A CG  
2727 O  OD1 . ASN A 376 ? 0.6533 0.3247 0.5267 0.0214  0.0074  0.0439  362 ASN A OD1 
2728 N  ND2 . ASN A 376 ? 0.6391 0.5288 0.6373 0.0178  0.1838  -0.2940 362 ASN A ND2 
2729 N  N   . LYS A 377 ? 0.5774 0.4052 0.4120 -0.0131 -0.0778 0.0134  363 LYS A N   
2730 C  CA  . LYS A 377 ? 0.5234 0.4592 0.5486 -0.0951 -0.1097 0.0711  363 LYS A CA  
2731 C  C   . LYS A 377 ? 0.7263 0.4289 0.4960 -0.0537 -0.0914 0.0239  363 LYS A C   
2732 O  O   . LYS A 377 ? 0.7354 0.4221 0.5220 -0.0345 -0.0507 0.1174  363 LYS A O   
2733 C  CB  . LYS A 377 ? 0.5965 0.6489 0.5060 -0.2849 -0.0809 0.0770  363 LYS A CB  
2734 C  CG  . LYS A 377 ? 0.6297 0.9135 0.5211 -0.0513 -0.1090 0.2539  363 LYS A CG  
2735 C  CD  . LYS A 377 ? 0.9017 0.9307 0.8121 0.0569  -0.1000 0.2574  363 LYS A CD  
2736 C  CE  . LYS A 377 ? 0.5971 0.8762 0.5404 0.2036  -0.1085 0.2033  363 LYS A CE  
2737 N  NZ  . LYS A 377 ? 0.5780 0.8651 0.5894 0.0336  -0.1199 0.1024  363 LYS A NZ  
2738 N  N   . LYS A 378 ? 0.5871 0.3193 0.4910 -0.0456 -0.0798 0.0740  364 LYS A N   
2739 C  CA  . LYS A 378 ? 0.5025 0.3711 0.5499 -0.0268 -0.1371 -0.0247 364 LYS A CA  
2740 C  C   . LYS A 378 ? 0.5098 0.3070 0.4120 0.0112  -0.1507 -0.0542 364 LYS A C   
2741 O  O   . LYS A 378 ? 0.5515 0.3835 0.5221 0.0180  -0.1816 -0.0004 364 LYS A O   
2742 C  CB  . LYS A 378 ? 0.6317 0.5855 0.4851 0.1267  -0.2230 -0.0078 364 LYS A CB  
2743 N  N   . ILE A 379 ? 0.5258 0.2796 0.4590 0.0397  0.0267  -0.0234 365 ILE A N   
2744 C  CA  . ILE A 379 ? 0.5235 0.2387 0.5420 -0.0088 0.0570  -0.1185 365 ILE A CA  
2745 C  C   . ILE A 379 ? 0.4709 0.3410 0.5166 0.0035  -0.0284 -0.0960 365 ILE A C   
2746 O  O   . ILE A 379 ? 0.4359 0.2212 0.5346 0.0128  0.0501  -0.0616 365 ILE A O   
2747 C  CB  . ILE A 379 ? 0.4532 0.2310 0.5247 -0.0572 0.0383  -0.0709 365 ILE A CB  
2748 C  CG1 . ILE A 379 ? 0.6738 0.2817 0.6414 0.0326  0.0773  -0.2628 365 ILE A CG1 
2749 C  CG2 . ILE A 379 ? 0.4595 0.4047 0.6205 0.0356  -0.0111 -0.0708 365 ILE A CG2 
2750 C  CD1 . ILE A 379 ? 0.7554 0.2928 0.6540 -0.0533 0.0428  0.0040  365 ILE A CD1 
2751 N  N   . HIS A 380 ? 0.4007 0.1922 0.3892 0.0444  -0.0015 -0.0373 366 HIS A N   
2752 C  CA  . HIS A 380 ? 0.3586 0.3062 0.3176 0.0069  -0.0046 -0.0255 366 HIS A CA  
2753 C  C   . HIS A 380 ? 0.4223 0.2262 0.2660 0.0066  -0.0302 -0.0164 366 HIS A C   
2754 O  O   . HIS A 380 ? 0.3639 0.2060 0.2791 0.0047  -0.0340 0.0079  366 HIS A O   
2755 C  CB  . HIS A 380 ? 0.5474 0.3349 0.2387 0.0519  -0.0354 -0.0267 366 HIS A CB  
2756 C  CG  . HIS A 380 ? 0.5675 0.3242 0.4633 0.0275  0.0731  -0.0993 366 HIS A CG  
2757 N  ND1 . HIS A 380 ? 0.4774 0.4000 0.4103 0.0869  -0.0311 -0.1496 366 HIS A ND1 
2758 C  CD2 . HIS A 380 ? 0.3294 0.2907 0.5293 -0.0033 -0.0065 -0.0337 366 HIS A CD2 
2759 C  CE1 . HIS A 380 ? 0.5293 0.2962 0.3193 0.0237  -0.1542 -0.0676 366 HIS A CE1 
2760 N  NE2 . HIS A 380 ? 0.5817 0.3504 0.6077 0.1064  0.0238  -0.0326 366 HIS A NE2 
2761 N  N   . ALA A 381 ? 0.3724 0.2489 0.2254 0.0101  -0.0408 -0.0104 367 ALA A N   
2762 C  CA  . ALA A 381 ? 0.3326 0.1718 0.2787 0.0171  -0.0104 0.0116  367 ALA A CA  
2763 C  C   . ALA A 381 ? 0.2787 0.2193 0.2676 0.0344  -0.0346 -0.0255 367 ALA A C   
2764 O  O   . ALA A 381 ? 0.3640 0.2896 0.3610 0.0414  -0.0515 0.0210  367 ALA A O   
2765 C  CB  . ALA A 381 ? 0.3712 0.2652 0.2453 0.0548  0.0233  -0.0310 367 ALA A CB  
2766 N  N   . SER A 382 ? 0.2776 0.2013 0.2225 0.0120  -0.0105 0.0311  368 SER A N   
2767 C  CA  . SER A 382 ? 0.2239 0.2373 0.1863 0.0204  -0.0290 0.0256  368 SER A CA  
2768 C  C   . SER A 382 ? 0.2175 0.2345 0.1926 0.0263  0.0165  -0.0010 368 SER A C   
2769 O  O   . SER A 382 ? 0.2372 0.2122 0.2473 0.0000  0.0207  0.0019  368 SER A O   
2770 C  CB  . SER A 382 ? 0.2798 0.2167 0.2480 0.0209  -0.0143 0.0282  368 SER A CB  
2771 O  OG  . SER A 382 ? 0.3129 0.3361 0.2667 -0.0221 0.0165  0.0320  368 SER A OG  
2772 N  N   . SER A 383 ? 0.2266 0.1888 0.1756 0.0017  -0.0005 0.0110  369 SER A N   
2773 C  CA  . SER A 383 ? 0.2791 0.1769 0.2017 -0.0059 0.0179  0.0185  369 SER A CA  
2774 C  C   . SER A 383 ? 0.2160 0.1757 0.1761 -0.0122 0.0030  0.0091  369 SER A C   
2775 O  O   . SER A 383 ? 0.2397 0.2247 0.1953 -0.0534 0.0207  0.0208  369 SER A O   
2776 C  CB  . SER A 383 ? 0.2955 0.2528 0.2264 -0.0246 -0.0271 0.0595  369 SER A CB  
2777 O  OG  . SER A 383 ? 0.4200 0.3463 0.3119 0.0190  -0.0410 0.0744  369 SER A OG  
2778 N  N   . HIS A 384 ? 0.2031 0.1328 0.1818 0.0047  0.0121  0.0146  370 HIS A N   
2779 C  CA  . HIS A 384 ? 0.1946 0.1444 0.1722 0.0164  -0.0124 0.0243  370 HIS A CA  
2780 C  C   . HIS A 384 ? 0.1917 0.1272 0.1551 -0.0010 -0.0042 0.0217  370 HIS A C   
2781 O  O   . HIS A 384 ? 0.2376 0.1114 0.1882 -0.0087 -0.0181 0.0186  370 HIS A O   
2782 C  CB  . HIS A 384 ? 0.1830 0.1393 0.1643 0.0206  0.0265  0.0210  370 HIS A CB  
2783 C  CG  . HIS A 384 ? 0.1985 0.1413 0.1469 0.0160  -0.0212 0.0019  370 HIS A CG  
2784 N  ND1 . HIS A 384 ? 0.2183 0.1335 0.1546 0.0234  -0.0194 0.0215  370 HIS A ND1 
2785 C  CD2 . HIS A 384 ? 0.2258 0.1398 0.1938 0.0571  -0.0217 0.0065  370 HIS A CD2 
2786 C  CE1 . HIS A 384 ? 0.2225 0.1478 0.1690 0.0292  -0.0310 0.0231  370 HIS A CE1 
2787 N  NE2 . HIS A 384 ? 0.2322 0.1724 0.1964 0.0292  0.0016  0.0116  370 HIS A NE2 
2788 N  N   . GLY A 385 ? 0.1784 0.1211 0.1700 -0.0003 -0.0009 0.0231  371 GLY A N   
2789 C  CA  . GLY A 385 ? 0.1830 0.1304 0.1990 0.0325  -0.0060 0.0257  371 GLY A CA  
2790 C  C   . GLY A 385 ? 0.1582 0.1421 0.1732 -0.0062 -0.0160 0.0004  371 GLY A C   
2791 O  O   . GLY A 385 ? 0.1754 0.1149 0.1693 -0.0038 0.0099  0.0210  371 GLY A O   
2792 N  N   . CYS A 386 ? 0.1738 0.1209 0.1698 0.0401  0.0304  0.0145  372 CYS A N   
2793 C  CA  . CYS A 386 ? 0.1813 0.1140 0.2087 0.0104  0.0078  0.0095  372 CYS A CA  
2794 C  C   . CYS A 386 ? 0.1621 0.1194 0.1737 0.0102  0.0038  0.0289  372 CYS A C   
2795 O  O   . CYS A 386 ? 0.1751 0.1161 0.1528 0.0198  0.0099  0.0187  372 CYS A O   
2796 C  CB  . CYS A 386 ? 0.2444 0.1100 0.2136 -0.0024 0.0362  0.0061  372 CYS A CB  
2797 S  SG  . CYS A 386 ? 0.2552 0.1563 0.2132 0.0131  -0.0050 0.0085  372 CYS A SG  
2798 N  N   . MET A 387 ? 0.2078 0.1082 0.2015 0.0052  0.0099  0.0195  373 MET A N   
2799 C  CA  . MET A 387 ? 0.2041 0.1089 0.1812 0.0156  0.0377  0.0250  373 MET A CA  
2800 C  C   . MET A 387 ? 0.2099 0.1403 0.1513 0.0266  -0.0008 -0.0028 373 MET A C   
2801 O  O   . MET A 387 ? 0.1971 0.1396 0.1593 0.0237  0.0231  0.0119  373 MET A O   
2802 C  CB  . MET A 387 ? 0.2288 0.1613 0.2070 0.0059  0.0244  0.0357  373 MET A CB  
2803 C  CG  . MET A 387 ? 0.2385 0.1155 0.2050 -0.0203 0.0206  0.0392  373 MET A CG  
2804 S  SD  . MET A 387 ? 0.2899 0.1903 0.2612 -0.0228 0.0531  0.0445  373 MET A SD  
2805 C  CE  . MET A 387 ? 0.3567 0.1953 0.3392 -0.0662 0.0436  0.0656  373 MET A CE  
2806 N  N   . GLU A 388 ? 0.2118 0.1116 0.2016 0.0336  0.0146  0.0131  374 GLU A N   
2807 C  CA  . GLU A 388 ? 0.2293 0.1351 0.1644 0.0347  0.0093  0.0133  374 GLU A CA  
2808 C  C   . GLU A 388 ? 0.1974 0.1490 0.1822 0.0465  -0.0109 -0.0207 374 GLU A C   
2809 O  O   . GLU A 388 ? 0.2166 0.1297 0.1852 0.0324  -0.0004 0.0203  374 GLU A O   
2810 C  CB  . GLU A 388 ? 0.2270 0.1466 0.1942 0.0275  0.0006  0.0195  374 GLU A CB  
2811 C  CG  . GLU A 388 ? 0.3216 0.1566 0.1974 0.0346  0.0197  0.0268  374 GLU A CG  
2812 C  CD  . GLU A 388 ? 0.2807 0.2166 0.2475 0.0128  -0.0077 0.0605  374 GLU A CD  
2813 O  OE1 . GLU A 388 ? 0.3528 0.2190 0.2818 0.0113  -0.0186 0.0672  374 GLU A OE1 
2814 O  OE2 . GLU A 388 ? 0.3836 0.3982 0.2669 -0.0376 0.0582  0.0780  374 GLU A OE2 
2815 N  N   . GLU A 389 ? 0.2047 0.1267 0.1646 0.0278  0.0149  0.0034  375 GLU A N   
2816 C  CA  . GLU A 389 ? 0.1590 0.1367 0.1686 0.0192  0.0078  0.0040  375 GLU A CA  
2817 C  C   . GLU A 389 ? 0.1772 0.1361 0.1446 0.0140  -0.0030 0.0271  375 GLU A C   
2818 O  O   . GLU A 389 ? 0.1499 0.1405 0.1538 0.0336  0.0088  0.0139  375 GLU A O   
2819 C  CB  . GLU A 389 ? 0.1605 0.1336 0.1739 0.0381  -0.0007 -0.0040 375 GLU A CB  
2820 C  CG  . GLU A 389 ? 0.2079 0.1539 0.1788 0.0178  -0.0111 0.0096  375 GLU A CG  
2821 C  CD  . GLU A 389 ? 0.1925 0.1796 0.2002 0.0450  0.0321  -0.0167 375 GLU A CD  
2822 O  OE1 . GLU A 389 ? 0.2328 0.1927 0.1986 0.0283  0.0186  0.0260  375 GLU A OE1 
2823 O  OE2 . GLU A 389 ? 0.2438 0.1811 0.1848 0.0280  0.0168  0.0107  375 GLU A OE2 
2824 N  N   . LEU A 390 ? 0.1788 0.1143 0.1500 0.0208  0.0087  0.0097  376 LEU A N   
2825 C  CA  . LEU A 390 ? 0.1848 0.1124 0.1577 0.0310  -0.0067 -0.0052 376 LEU A CA  
2826 C  C   . LEU A 390 ? 0.1440 0.1255 0.1707 0.0286  0.0012  -0.0027 376 LEU A C   
2827 O  O   . LEU A 390 ? 0.1641 0.1319 0.1381 0.0307  -0.0045 0.0025  376 LEU A O   
2828 C  CB  . LEU A 390 ? 0.1460 0.1179 0.1683 0.0291  0.0171  0.0119  376 LEU A CB  
2829 C  CG  . LEU A 390 ? 0.1548 0.1361 0.1411 0.0250  0.0129  0.0116  376 LEU A CG  
2830 C  CD1 . LEU A 390 ? 0.1775 0.1269 0.1586 -0.0095 0.0040  0.0158  376 LEU A CD1 
2831 C  CD2 . LEU A 390 ? 0.1431 0.1370 0.1371 -0.0140 0.0129  0.0071  376 LEU A CD2 
2832 N  N   . LYS A 391 ? 0.1937 0.1511 0.1646 0.0467  0.0124  -0.0058 377 LYS A N   
2833 C  CA  . LYS A 391 ? 0.2009 0.1328 0.1280 0.0319  0.0100  -0.0119 377 LYS A CA  
2834 C  C   . LYS A 391 ? 0.2228 0.1308 0.1442 0.0263  -0.0055 0.0298  377 LYS A C   
2835 O  O   . LYS A 391 ? 0.2110 0.1484 0.1586 0.0361  -0.0172 0.0058  377 LYS A O   
2836 C  CB  . LYS A 391 ? 0.2612 0.1657 0.1387 0.0454  0.0129  0.0322  377 LYS A CB  
2837 C  CG  . LYS A 391 ? 0.2654 0.1606 0.1669 0.0277  0.0165  0.0439  377 LYS A CG  
2838 C  CD  . LYS A 391 ? 0.3216 0.2381 0.4067 0.0378  0.0113  0.0544  377 LYS A CD  
2839 C  CE  . LYS A 391 ? 0.4279 0.2515 0.4511 -0.0097 0.1098  0.0909  377 LYS A CE  
2840 N  NZ  . LYS A 391 ? 0.5004 0.2393 0.4470 0.0137  0.0254  0.0894  377 LYS A NZ  
2841 N  N   . MET A 392 ? 0.1999 0.1377 0.1621 0.0435  -0.0021 0.0078  378 MET A N   
2842 C  CA  . MET A 392 ? 0.1882 0.1410 0.1537 0.0516  -0.0025 0.0017  378 MET A CA  
2843 C  C   . MET A 392 ? 0.1649 0.1439 0.1448 0.0030  -0.0089 -0.0053 378 MET A C   
2844 O  O   . MET A 392 ? 0.1745 0.1678 0.1715 0.0363  -0.0163 0.0007  378 MET A O   
2845 C  CB  . MET A 392 ? 0.2113 0.1637 0.2057 0.0395  0.0089  0.0277  378 MET A CB  
2846 C  CG  . MET A 392 ? 0.2637 0.1886 0.1961 0.0492  0.0209  0.0107  378 MET A CG  
2847 S  SD  . MET A 392 ? 0.2907 0.2267 0.2632 0.0807  0.0264  0.0248  378 MET A SD  
2848 C  CE  . MET A 392 ? 0.2716 0.2636 0.3118 0.0690  -0.0024 0.0396  378 MET A CE  
2849 N  N   . MET A 393 ? 0.1653 0.1314 0.1460 0.0271  -0.0115 0.0262  379 MET A N   
2850 C  CA  . MET A 393 ? 0.1546 0.1692 0.1198 0.0174  -0.0092 -0.0043 379 MET A CA  
2851 C  C   . MET A 393 ? 0.1560 0.1227 0.1562 0.0387  -0.0201 0.0215  379 MET A C   
2852 O  O   . MET A 393 ? 0.1632 0.1691 0.1418 0.0210  -0.0177 0.0158  379 MET A O   
2853 C  CB  . MET A 393 ? 0.1745 0.1507 0.1421 0.0146  -0.0100 0.0120  379 MET A CB  
2854 C  CG  . MET A 393 ? 0.1597 0.1613 0.1552 0.0263  -0.0120 -0.0100 379 MET A CG  
2855 S  SD  . MET A 393 ? 0.1925 0.1809 0.1774 0.0023  -0.0057 0.0042  379 MET A SD  
2856 C  CE  . MET A 393 ? 0.1598 0.1793 0.2038 0.0108  0.0129  0.0162  379 MET A CE  
2857 N  N   . LEU A 394 ? 0.1661 0.1212 0.1156 0.0241  -0.0159 0.0201  380 LEU A N   
2858 C  CA  . LEU A 394 ? 0.1747 0.1461 0.1514 0.0206  0.0011  -0.0125 380 LEU A CA  
2859 C  C   . LEU A 394 ? 0.1828 0.1507 0.1750 0.0301  -0.0063 0.0082  380 LEU A C   
2860 O  O   . LEU A 394 ? 0.2286 0.1847 0.1681 0.0397  -0.0087 0.0115  380 LEU A O   
2861 C  CB  . LEU A 394 ? 0.1879 0.1576 0.1229 0.0297  -0.0124 0.0179  380 LEU A CB  
2862 C  CG  . LEU A 394 ? 0.1785 0.1722 0.1305 0.0411  0.0063  0.0206  380 LEU A CG  
2863 C  CD1 . LEU A 394 ? 0.1821 0.1746 0.1528 0.0255  0.0444  0.0051  380 LEU A CD1 
2864 C  CD2 . LEU A 394 ? 0.1813 0.1490 0.1586 0.0176  0.0022  0.0215  380 LEU A CD2 
2865 N  N   . ASN A 395 ? 0.1768 0.1842 0.1258 0.0230  -0.0067 0.0001  381 ASN A N   
2866 C  CA  . ASN A 395 ? 0.1721 0.1857 0.1605 0.0457  -0.0108 0.0093  381 ASN A CA  
2867 C  C   . ASN A 395 ? 0.1766 0.1703 0.1934 0.0683  -0.0104 -0.0004 381 ASN A C   
2868 O  O   . ASN A 395 ? 0.2452 0.2618 0.1742 0.0352  -0.0336 -0.0014 381 ASN A O   
2869 C  CB  . ASN A 395 ? 0.2273 0.2102 0.1940 0.0879  -0.0218 0.0284  381 ASN A CB  
2870 C  CG  . ASN A 395 ? 0.2210 0.2268 0.2214 0.0457  -0.0352 0.0169  381 ASN A CG  
2871 O  OD1 . ASN A 395 ? 0.2758 0.2529 0.2734 0.0430  -0.0150 0.0820  381 ASN A OD1 
2872 N  ND2 . ASN A 395 ? 0.3264 0.2274 0.2594 0.0299  -0.0768 0.0769  381 ASN A ND2 
2873 N  N   . ILE A 396 ? 0.1619 0.1781 0.1670 0.0605  -0.0032 0.0448  382 ILE A N   
2874 C  CA  . ILE A 396 ? 0.1812 0.1700 0.1555 0.0398  -0.0352 0.0067  382 ILE A CA  
2875 C  C   . ILE A 396 ? 0.1479 0.1936 0.1983 0.0311  -0.0040 0.0000  382 ILE A C   
2876 O  O   . ILE A 396 ? 0.1938 0.1992 0.2116 0.0468  -0.0432 -0.0023 382 ILE A O   
2877 C  CB  . ILE A 396 ? 0.2098 0.1932 0.1926 0.0403  0.0004  0.0008  382 ILE A CB  
2878 C  CG1 . ILE A 396 ? 0.2389 0.2182 0.2864 0.0116  -0.0207 -0.0214 382 ILE A CG1 
2879 C  CG2 . ILE A 396 ? 0.2384 0.2933 0.2602 0.0428  0.0576  -0.0052 382 ILE A CG2 
2880 C  CD1 . ILE A 396 ? 0.2696 0.2203 0.3050 0.0274  -0.0213 -0.0003 382 ILE A CD1 
2881 N  N   . MET A 397 ? 0.1627 0.1761 0.1661 0.0323  -0.0143 -0.0039 383 MET A N   
2882 C  CA  . MET A 397 ? 0.1849 0.1762 0.1438 0.0450  -0.0276 0.0036  383 MET A CA  
2883 C  C   . MET A 397 ? 0.1407 0.2006 0.1782 0.0291  -0.0416 -0.0001 383 MET A C   
2884 O  O   . MET A 397 ? 0.1947 0.1890 0.1784 0.0451  -0.0137 -0.0113 383 MET A O   
2885 C  CB  . MET A 397 ? 0.1814 0.1565 0.1345 0.0401  -0.0258 0.0036  383 MET A CB  
2886 C  CG  . MET A 397 ? 0.1687 0.1913 0.1185 0.0252  -0.0214 -0.0128 383 MET A CG  
2887 S  SD  . MET A 397 ? 0.2189 0.2022 0.1686 0.0206  -0.0144 -0.0013 383 MET A SD  
2888 C  CE  . MET A 397 ? 0.2161 0.1927 0.2259 0.0105  0.0418  0.0085  383 MET A CE  
2889 N  N   . LYS A 398 ? 0.2083 0.1841 0.1571 0.0318  -0.0018 0.0005  384 LYS A N   
2890 C  CA  . LYS A 398 ? 0.2263 0.2187 0.1461 0.0391  -0.0097 -0.0186 384 LYS A CA  
2891 C  C   . LYS A 398 ? 0.2241 0.2171 0.1586 0.0517  0.0124  -0.0387 384 LYS A C   
2892 O  O   . LYS A 398 ? 0.2084 0.2344 0.1587 0.0408  -0.0084 0.0010  384 LYS A O   
2893 C  CB  . LYS A 398 ? 0.2463 0.2541 0.1828 0.0781  -0.0293 0.0126  384 LYS A CB  
2894 C  CG  . LYS A 398 ? 0.2621 0.3570 0.1704 0.0579  -0.0040 0.0462  384 LYS A CG  
2895 C  CD  . LYS A 398 ? 0.2676 0.3830 0.2459 0.0818  -0.0730 0.0161  384 LYS A CD  
2896 C  CE  . LYS A 398 ? 0.2681 0.4289 0.3427 0.1161  -0.0726 0.0673  384 LYS A CE  
2897 N  NZ  . LYS A 398 ? 0.3859 0.6009 0.3598 0.0588  0.0326  0.0340  384 LYS A NZ  
2898 N  N   . PRO A 399 ? 0.1893 0.2030 0.1501 0.0287  -0.0045 -0.0041 385 PRO A N   
2899 C  CA  . PRO A 399 ? 0.1838 0.1976 0.1385 0.0134  0.0143  -0.0080 385 PRO A CA  
2900 C  C   . PRO A 399 ? 0.1609 0.1954 0.1620 0.0142  -0.0123 -0.0025 385 PRO A C   
2901 O  O   . PRO A 399 ? 0.2096 0.2218 0.1561 0.0228  0.0163  -0.0063 385 PRO A O   
2902 C  CB  . PRO A 399 ? 0.1715 0.1998 0.1214 0.0165  0.0208  0.0037  385 PRO A CB  
2903 C  CG  . PRO A 399 ? 0.1746 0.2057 0.1434 0.0041  -0.0160 -0.0091 385 PRO A CG  
2904 C  CD  . PRO A 399 ? 0.1773 0.1819 0.1519 0.0259  0.0061  0.0132  385 PRO A CD  
2905 N  N   . GLU A 400 ? 0.2086 0.1934 0.1423 0.0208  -0.0012 0.0137  386 GLU A N   
2906 C  CA  . GLU A 400 ? 0.1854 0.2303 0.1167 0.0010  -0.0070 0.0000  386 GLU A CA  
2907 C  C   . GLU A 400 ? 0.1429 0.1836 0.1545 0.0235  -0.0015 -0.0013 386 GLU A C   
2908 O  O   . GLU A 400 ? 0.2030 0.1947 0.1559 0.0062  -0.0069 0.0249  386 GLU A O   
2909 C  CB  . GLU A 400 ? 0.2221 0.2287 0.1505 0.0076  -0.0210 -0.0102 386 GLU A CB  
2910 C  CG  . GLU A 400 ? 0.2540 0.2600 0.2115 0.0680  -0.0094 -0.0171 386 GLU A CG  
2911 C  CD  . GLU A 400 ? 0.2457 0.3098 0.1670 0.0108  0.0285  0.0041  386 GLU A CD  
2912 O  OE1 . GLU A 400 ? 0.3186 0.2866 0.2338 0.0184  -0.0015 -0.0662 386 GLU A OE1 
2913 O  OE2 . GLU A 400 ? 0.2982 0.3628 0.1839 0.0354  0.0189  -0.0306 386 GLU A OE2 
2914 N  N   . TYR A 401 ? 0.1759 0.1785 0.1115 0.0222  -0.0162 0.0040  387 TYR A N   
2915 C  CA  . TYR A 401 ? 0.1478 0.1792 0.1404 0.0248  -0.0025 0.0055  387 TYR A CA  
2916 C  C   . TYR A 401 ? 0.1434 0.1678 0.1260 0.0146  0.0033  0.0271  387 TYR A C   
2917 O  O   . TYR A 401 ? 0.1516 0.1641 0.1456 0.0062  0.0076  -0.0031 387 TYR A O   
2918 C  CB  . TYR A 401 ? 0.1907 0.1786 0.1201 0.0288  0.0108  -0.0100 387 TYR A CB  
2919 C  CG  . TYR A 401 ? 0.1705 0.1810 0.1485 0.0275  0.0094  -0.0157 387 TYR A CG  
2920 C  CD1 . TYR A 401 ? 0.1958 0.1791 0.1830 0.0340  -0.0023 -0.0020 387 TYR A CD1 
2921 C  CD2 . TYR A 401 ? 0.1841 0.1898 0.1231 0.0179  0.0141  -0.0100 387 TYR A CD2 
2922 C  CE1 . TYR A 401 ? 0.2094 0.2211 0.1657 0.0413  0.0249  -0.0244 387 TYR A CE1 
2923 C  CE2 . TYR A 401 ? 0.2050 0.2203 0.1849 0.0254  -0.0163 -0.0236 387 TYR A CE2 
2924 C  CZ  . TYR A 401 ? 0.2046 0.2187 0.1434 0.0133  0.0134  -0.0209 387 TYR A CZ  
2925 O  OH  . TYR A 401 ? 0.2798 0.2672 0.1512 0.0702  0.0325  -0.0120 387 TYR A OH  
2926 N  N   . PHE A 402 ? 0.1326 0.1524 0.1298 0.0160  0.0060  -0.0024 388 PHE A N   
2927 C  CA  . PHE A 402 ? 0.1406 0.1544 0.1119 0.0265  -0.0057 0.0170  388 PHE A CA  
2928 C  C   . PHE A 402 ? 0.1242 0.1550 0.1619 -0.0010 -0.0001 0.0131  388 PHE A C   
2929 O  O   . PHE A 402 ? 0.1440 0.1734 0.1363 0.0093  0.0056  0.0084  388 PHE A O   
2930 C  CB  . PHE A 402 ? 0.1396 0.1611 0.1408 0.0160  -0.0106 0.0058  388 PHE A CB  
2931 C  CG  . PHE A 402 ? 0.1430 0.1444 0.1653 0.0178  -0.0009 0.0019  388 PHE A CG  
2932 C  CD1 . PHE A 402 ? 0.1751 0.1608 0.1537 -0.0009 -0.0098 -0.0029 388 PHE A CD1 
2933 C  CD2 . PHE A 402 ? 0.1796 0.1377 0.1288 0.0080  0.0119  0.0234  388 PHE A CD2 
2934 C  CE1 . PHE A 402 ? 0.1570 0.1537 0.1468 0.0106  0.0182  -0.0098 388 PHE A CE1 
2935 C  CE2 . PHE A 402 ? 0.1656 0.1218 0.1692 0.0052  0.0084  -0.0042 388 PHE A CE2 
2936 C  CZ  . PHE A 402 ? 0.1616 0.1299 0.1542 0.0157  -0.0032 0.0133  388 PHE A CZ  
2937 N  N   . VAL A 403 ? 0.1290 0.1529 0.1306 0.0247  -0.0021 -0.0077 389 VAL A N   
2938 C  CA  . VAL A 403 ? 0.1117 0.1198 0.1473 -0.0061 -0.0001 0.0283  389 VAL A CA  
2939 C  C   . VAL A 403 ? 0.1256 0.1537 0.1293 0.0020  -0.0012 0.0016  389 VAL A C   
2940 O  O   . VAL A 403 ? 0.1204 0.1345 0.1370 -0.0105 0.0054  0.0026  389 VAL A O   
2941 C  CB  . VAL A 403 ? 0.1413 0.1239 0.1511 0.0083  -0.0157 0.0154  389 VAL A CB  
2942 C  CG1 . VAL A 403 ? 0.1639 0.1473 0.1749 0.0174  0.0085  -0.0144 389 VAL A CG1 
2943 C  CG2 . VAL A 403 ? 0.1931 0.1388 0.1920 0.0101  -0.0260 0.0082  389 VAL A CG2 
2944 N  N   . PRO A 404 ? 0.1275 0.1128 0.1200 0.0083  0.0104  0.0099  390 PRO A N   
2945 C  CA  . PRO A 404 ? 0.1091 0.1033 0.1265 0.0081  0.0148  0.0139  390 PRO A CA  
2946 C  C   . PRO A 404 ? 0.1244 0.0964 0.1489 0.0023  0.0031  0.0058  390 PRO A C   
2947 O  O   . PRO A 404 ? 0.1200 0.1392 0.1435 0.0170  -0.0010 0.0156  390 PRO A O   
2948 C  CB  . PRO A 404 ? 0.1691 0.1225 0.1351 0.0115  -0.0009 0.0371  390 PRO A CB  
2949 C  CG  . PRO A 404 ? 0.1582 0.1589 0.1433 0.0030  0.0274  0.0307  390 PRO A CG  
2950 C  CD  . PRO A 404 ? 0.1600 0.1439 0.1255 0.0223  0.0174  0.0181  390 PRO A CD  
2951 N  N   . VAL A 405 ? 0.1326 0.1011 0.1367 0.0204  -0.0007 0.0043  391 VAL A N   
2952 C  CA  . VAL A 405 ? 0.1213 0.1112 0.1339 0.0066  0.0114  0.0110  391 VAL A CA  
2953 C  C   . VAL A 405 ? 0.1085 0.1195 0.1286 -0.0063 -0.0132 -0.0005 391 VAL A C   
2954 O  O   . VAL A 405 ? 0.1589 0.0937 0.1455 0.0179  0.0004  0.0189  391 VAL A O   
2955 C  CB  . VAL A 405 ? 0.1249 0.1091 0.1143 0.0010  0.0017  0.0136  391 VAL A CB  
2956 C  CG1 . VAL A 405 ? 0.1354 0.1297 0.1286 0.0053  0.0020  0.0275  391 VAL A CG1 
2957 C  CG2 . VAL A 405 ? 0.1368 0.1085 0.1182 -0.0083 -0.0043 0.0032  391 VAL A CG2 
2958 N  N   . GLN A 406 ? 0.1396 0.1074 0.1165 0.0108  -0.0179 0.0037  392 GLN A N   
2959 C  CA  A GLN A 406 ? 0.1406 0.1198 0.1407 0.0000  -0.0197 0.0038  392 GLN A CA  
2960 C  CA  B GLN A 406 ? 0.1426 0.1196 0.1399 0.0025  -0.0231 0.0045  392 GLN A CA  
2961 C  C   . GLN A 406 ? 0.1702 0.1294 0.1523 0.0030  0.0040  0.0198  392 GLN A C   
2962 O  O   . GLN A 406 ? 0.1715 0.1097 0.1786 0.0130  0.0000  0.0048  392 GLN A O   
2963 C  CB  A GLN A 406 ? 0.1419 0.1404 0.1279 -0.0125 -0.0047 -0.0012 392 GLN A CB  
2964 C  CB  B GLN A 406 ? 0.1456 0.1515 0.1281 -0.0180 -0.0045 -0.0058 392 GLN A CB  
2965 C  CG  A GLN A 406 ? 0.1525 0.1256 0.1908 0.0080  0.0144  0.0070  392 GLN A CG  
2966 C  CG  B GLN A 406 ? 0.1764 0.1522 0.2019 0.0572  -0.0275 0.0161  392 GLN A CG  
2967 C  CD  A GLN A 406 ? 0.2171 0.1278 0.2981 0.1199  0.0896  0.0108  392 GLN A CD  
2968 C  CD  B GLN A 406 ? 0.4698 0.3550 0.2680 0.1196  0.0730  -0.0195 392 GLN A CD  
2969 N  NE2 A GLN A 406 ? 0.1896 0.2986 0.2639 0.0065  0.0251  0.0789  392 GLN A NE2 
2970 N  NE2 B GLN A 406 ? 0.2430 0.0664 0.2012 0.0268  -0.0013 0.0185  392 GLN A NE2 
2971 N  N   . GLY A 407 ? 0.1477 0.0903 0.1965 -0.0074 -0.0126 0.0104  393 GLY A N   
2972 C  CA  . GLY A 407 ? 0.1642 0.1290 0.2334 -0.0220 -0.0167 -0.0081 393 GLY A CA  
2973 C  C   . GLY A 407 ? 0.1781 0.1543 0.2056 -0.0246 -0.0072 -0.0023 393 GLY A C   
2974 O  O   . GLY A 407 ? 0.1450 0.1409 0.2031 -0.0197 -0.0170 0.0156  393 GLY A O   
2975 N  N   . GLU A 408 ? 0.1810 0.1445 0.2158 -0.0315 -0.0256 0.0140  394 GLU A N   
2976 C  CA  . GLU A 408 ? 0.1622 0.1615 0.2349 -0.0218 -0.0243 0.0070  394 GLU A CA  
2977 C  C   . GLU A 408 ? 0.1610 0.1365 0.2255 -0.0302 -0.0032 0.0089  394 GLU A C   
2978 O  O   . GLU A 408 ? 0.1698 0.1297 0.2060 -0.0203 -0.0188 0.0179  394 GLU A O   
2979 C  CB  . GLU A 408 ? 0.1858 0.2055 0.2419 -0.0747 -0.0066 -0.0125 394 GLU A CB  
2980 C  CG  . GLU A 408 ? 0.2482 0.2831 0.2915 -0.0632 -0.0513 0.0021  394 GLU A CG  
2981 C  CD  . GLU A 408 ? 0.3585 0.3911 0.3818 0.0114  -0.1161 -0.0963 394 GLU A CD  
2982 O  OE1 . GLU A 408 ? 0.5612 0.6254 0.8312 0.0085  -0.1688 -0.3480 394 GLU A OE1 
2983 O  OE2 . GLU A 408 ? 0.5324 0.4424 0.4012 -0.1842 0.0368  -0.0337 394 GLU A OE2 
2984 N  N   . PHE A 409 ? 0.1651 0.1726 0.2359 -0.0092 0.0003  0.0157  395 PHE A N   
2985 C  CA  . PHE A 409 ? 0.1296 0.1878 0.2364 -0.0254 0.0042  0.0022  395 PHE A CA  
2986 C  C   . PHE A 409 ? 0.1449 0.2285 0.2142 -0.0063 0.0287  0.0218  395 PHE A C   
2987 O  O   . PHE A 409 ? 0.1540 0.2189 0.1928 -0.0250 0.0230  0.0126  395 PHE A O   
2988 C  CB  . PHE A 409 ? 0.1669 0.2498 0.2791 0.0126  -0.0071 0.0054  395 PHE A CB  
2989 C  CG  . PHE A 409 ? 0.1878 0.2784 0.3529 0.0078  0.0204  0.0014  395 PHE A CG  
2990 C  CD1 . PHE A 409 ? 0.2734 0.4318 0.3157 -0.0054 0.0157  -0.0304 395 PHE A CD1 
2991 C  CD2 . PHE A 409 ? 0.3477 0.3005 0.3373 -0.0590 0.0005  0.0094  395 PHE A CD2 
2992 C  CE1 . PHE A 409 ? 0.4949 0.5173 0.3117 -0.0069 -0.0101 -0.0728 395 PHE A CE1 
2993 C  CE2 . PHE A 409 ? 0.2994 0.3654 0.3266 -0.0107 0.0332  0.0053  395 PHE A CE2 
2994 C  CZ  . PHE A 409 ? 0.4405 0.3833 0.2132 -0.0754 0.0031  0.0321  395 PHE A CZ  
2995 N  N   . LYS A 410 ? 0.1525 0.1875 0.2228 -0.0236 -0.0019 0.0229  396 LYS A N   
2996 C  CA  . LYS A 410 ? 0.1516 0.2064 0.2636 -0.0216 0.0237  0.0199  396 LYS A CA  
2997 C  C   . LYS A 410 ? 0.1899 0.1510 0.2080 -0.0108 0.0184  0.0108  396 LYS A C   
2998 O  O   . LYS A 410 ? 0.1770 0.1535 0.2081 -0.0303 0.0107  0.0323  396 LYS A O   
2999 C  CB  . LYS A 410 ? 0.2150 0.1549 0.2561 -0.0303 -0.0081 0.0076  396 LYS A CB  
3000 C  CG  . LYS A 410 ? 0.2599 0.2122 0.3253 -0.0712 -0.0053 -0.0565 396 LYS A CG  
3001 C  CD  . LYS A 410 ? 0.3771 0.2361 0.3762 -0.1254 -0.0490 -0.0694 396 LYS A CD  
3002 C  CE  . LYS A 410 ? 0.4752 0.3704 0.3543 -0.0559 -0.0965 -0.1064 396 LYS A CE  
3003 N  NZ  . LYS A 410 ? 0.5270 0.3887 0.6801 -0.1890 -0.2131 -0.0527 396 LYS A NZ  
3004 N  N   . MET A 411 ? 0.1695 0.1401 0.1899 -0.0208 0.0109  0.0237  397 MET A N   
3005 C  CA  . MET A 411 ? 0.1464 0.1400 0.1906 -0.0267 0.0085  0.0048  397 MET A CA  
3006 C  C   . MET A 411 ? 0.1440 0.1251 0.1544 -0.0163 0.0017  0.0152  397 MET A C   
3007 O  O   . MET A 411 ? 0.1334 0.1248 0.1678 -0.0165 0.0047  0.0257  397 MET A O   
3008 C  CB  . MET A 411 ? 0.1703 0.1288 0.1539 -0.0173 0.0201  -0.0039 397 MET A CB  
3009 C  CG  . MET A 411 ? 0.2241 0.1455 0.1837 -0.0253 0.0133  0.0013  397 MET A CG  
3010 S  SD  . MET A 411 ? 0.2336 0.1773 0.2268 -0.0114 0.0000  0.0027  397 MET A SD  
3011 C  CE  . MET A 411 ? 0.2823 0.2533 0.2407 -0.0101 -0.0567 -0.0714 397 MET A CE  
3012 N  N   . GLN A 412 ? 0.1409 0.1309 0.1730 0.0140  0.0102  0.0062  398 GLN A N   
3013 C  CA  . GLN A 412 ? 0.1387 0.1392 0.1405 0.0090  0.0149  0.0289  398 GLN A CA  
3014 C  C   . GLN A 412 ? 0.1574 0.1351 0.2020 -0.0019 0.0151  0.0065  398 GLN A C   
3015 O  O   . GLN A 412 ? 0.1624 0.1218 0.1725 0.0037  0.0075  0.0197  398 GLN A O   
3016 C  CB  . GLN A 412 ? 0.1264 0.1364 0.1640 -0.0217 0.0005  0.0183  398 GLN A CB  
3017 C  CG  . GLN A 412 ? 0.1625 0.1476 0.1915 0.0020  0.0146  0.0136  398 GLN A CG  
3018 C  CD  . GLN A 412 ? 0.1548 0.1359 0.1920 -0.0179 -0.0079 0.0024  398 GLN A CD  
3019 O  OE1 . GLN A 412 ? 0.2290 0.1404 0.2226 0.0035  -0.0101 -0.0090 398 GLN A OE1 
3020 N  NE2 . GLN A 412 ? 0.1781 0.1099 0.2528 0.0057  -0.0265 -0.0402 398 GLN A NE2 
3021 N  N   . ILE A 413 ? 0.1515 0.1371 0.1808 -0.0254 0.0274  0.0324  399 ILE A N   
3022 C  CA  . ILE A 413 ? 0.1534 0.1455 0.1742 0.0109  0.0120  0.0001  399 ILE A CA  
3023 C  C   . ILE A 413 ? 0.1661 0.1227 0.1959 -0.0177 0.0203  0.0363  399 ILE A C   
3024 O  O   . ILE A 413 ? 0.1714 0.1408 0.1705 -0.0079 0.0267  0.0238  399 ILE A O   
3025 C  CB  . ILE A 413 ? 0.1565 0.2002 0.2102 0.0122  0.0293  0.0268  399 ILE A CB  
3026 C  CG1 . ILE A 413 ? 0.1841 0.2158 0.2806 -0.0221 0.0195  0.0177  399 ILE A CG1 
3027 C  CG2 . ILE A 413 ? 0.2066 0.2343 0.2503 -0.0054 0.0295  0.0730  399 ILE A CG2 
3028 C  CD1 . ILE A 413 ? 0.1772 0.2746 0.3237 -0.0135 0.0426  0.0450  399 ILE A CD1 
3029 N  N   . ALA A 414 ? 0.1562 0.1255 0.1914 -0.0200 0.0033  0.0204  400 ALA A N   
3030 C  CA  . ALA A 414 ? 0.1694 0.1444 0.1829 -0.0076 -0.0052 0.0506  400 ALA A CA  
3031 C  C   . ALA A 414 ? 0.1761 0.1385 0.1934 0.0112  -0.0089 0.0403  400 ALA A C   
3032 O  O   . ALA A 414 ? 0.1773 0.1502 0.1811 -0.0037 0.0235  0.0421  400 ALA A O   
3033 C  CB  . ALA A 414 ? 0.2056 0.1517 0.2040 -0.0024 0.0472  0.0278  400 ALA A CB  
3034 N  N   . HIS A 415 ? 0.1628 0.1236 0.1673 0.0094  0.0210  0.0355  401 HIS A N   
3035 C  CA  . HIS A 415 ? 0.1486 0.1345 0.1276 0.0155  0.0018  0.0213  401 HIS A CA  
3036 C  C   . HIS A 415 ? 0.1453 0.1152 0.1619 -0.0099 0.0096  0.0214  401 HIS A C   
3037 O  O   . HIS A 415 ? 0.1608 0.1633 0.1527 0.0074  0.0183  0.0282  401 HIS A O   
3038 C  CB  . HIS A 415 ? 0.1313 0.1128 0.1357 0.0309  0.0046  0.0289  401 HIS A CB  
3039 C  CG  . HIS A 415 ? 0.1445 0.1294 0.1372 0.0034  0.0082  0.0179  401 HIS A CG  
3040 N  ND1 . HIS A 415 ? 0.1477 0.1112 0.1429 0.0010  0.0252  0.0197  401 HIS A ND1 
3041 C  CD2 . HIS A 415 ? 0.1342 0.1181 0.1257 0.0069  0.0044  0.0109  401 HIS A CD2 
3042 C  CE1 . HIS A 415 ? 0.1451 0.1041 0.1456 0.0123  0.0191  0.0214  401 HIS A CE1 
3043 N  NE2 . HIS A 415 ? 0.1253 0.1169 0.1603 0.0079  0.0127  0.0171  401 HIS A NE2 
3044 N  N   . ALA A 416 ? 0.1837 0.1446 0.1655 0.0037  0.0400  0.0221  402 ALA A N   
3045 C  CA  . ALA A 416 ? 0.1644 0.1687 0.1471 0.0123  0.0126  0.0117  402 ALA A CA  
3046 C  C   . ALA A 416 ? 0.1674 0.1772 0.1509 0.0066  0.0263  0.0085  402 ALA A C   
3047 O  O   . ALA A 416 ? 0.2016 0.1759 0.1533 0.0160  0.0058  0.0248  402 ALA A O   
3048 C  CB  . ALA A 416 ? 0.1787 0.1711 0.1799 -0.0209 0.0280  -0.0087 402 ALA A CB  
3049 N  N   . LYS A 417 ? 0.2044 0.1685 0.1741 -0.0062 0.0115  0.0324  403 LYS A N   
3050 C  CA  . LYS A 417 ? 0.2025 0.1920 0.1629 0.0182  0.0195  0.0315  403 LYS A CA  
3051 C  C   . LYS A 417 ? 0.2105 0.1496 0.2034 -0.0048 0.0099  0.0031  403 LYS A C   
3052 O  O   . LYS A 417 ? 0.2279 0.2234 0.1895 0.0273  0.0161  0.0529  403 LYS A O   
3053 C  CB  . LYS A 417 ? 0.2459 0.2002 0.1723 -0.0032 -0.0104 0.0566  403 LYS A CB  
3054 C  CG  . LYS A 417 ? 0.2796 0.2226 0.1891 -0.0474 0.0136  0.0217  403 LYS A CG  
3055 C  CD  . LYS A 417 ? 0.3171 0.2780 0.2166 -0.0843 -0.0098 0.0370  403 LYS A CD  
3056 C  CE  . LYS A 417 ? 0.2738 0.2853 0.3284 -0.1076 -0.0002 0.0330  403 LYS A CE  
3057 N  NZ  . LYS A 417 ? 0.3165 0.2997 0.2898 -0.0657 0.0276  0.0357  403 LYS A NZ  
3058 N  N   . LEU A 418 ? 0.2047 0.1572 0.1910 0.0201  0.0292  0.0406  404 LEU A N   
3059 C  CA  . LEU A 418 ? 0.2099 0.1776 0.1713 0.0144  0.0007  0.0666  404 LEU A CA  
3060 C  C   . LEU A 418 ? 0.1763 0.1874 0.1603 0.0156  0.0124  0.0331  404 LEU A C   
3061 O  O   . LEU A 418 ? 0.1965 0.1766 0.1880 0.0481  0.0078  0.0380  404 LEU A O   
3062 C  CB  . LEU A 418 ? 0.1806 0.1384 0.1554 0.0408  0.0310  0.0380  404 LEU A CB  
3063 C  CG  . LEU A 418 ? 0.1969 0.1726 0.1881 0.0420  0.0205  0.0333  404 LEU A CG  
3064 C  CD1 . LEU A 418 ? 0.2224 0.1555 0.2236 0.0358  0.0358  0.0378  404 LEU A CD1 
3065 C  CD2 . LEU A 418 ? 0.2621 0.1802 0.1675 0.0320  0.0023  0.0300  404 LEU A CD2 
3066 N  N   . ALA A 419 ? 0.2141 0.1471 0.1482 0.0327  0.0262  0.0355  405 ALA A N   
3067 C  CA  . ALA A 419 ? 0.1619 0.1862 0.1528 0.0171  0.0110  0.0595  405 ALA A CA  
3068 C  C   . ALA A 419 ? 0.1834 0.2179 0.1743 0.0219  -0.0096 0.0379  405 ALA A C   
3069 O  O   . ALA A 419 ? 0.2252 0.2012 0.1523 0.0334  0.0039  0.0375  405 ALA A O   
3070 C  CB  . ALA A 419 ? 0.1949 0.1793 0.1501 0.0275  0.0048  0.0401  405 ALA A CB  
3071 N  N   . ALA A 420 ? 0.2026 0.2190 0.1359 0.0200  -0.0014 0.0382  406 ALA A N   
3072 C  CA  . ALA A 420 ? 0.2144 0.2228 0.1391 0.0047  0.0183  0.0507  406 ALA A CA  
3073 C  C   . ALA A 420 ? 0.2923 0.2168 0.1672 0.0048  0.0223  0.0374  406 ALA A C   
3074 O  O   . ALA A 420 ? 0.2781 0.2627 0.1714 0.0538  0.0039  0.0434  406 ALA A O   
3075 C  CB  . ALA A 420 ? 0.2822 0.2722 0.1603 0.0061  0.0476  0.0512  406 ALA A CB  
3076 N  N   . GLU A 421 ? 0.2367 0.2300 0.1698 0.0153  -0.0001 0.0616  407 GLU A N   
3077 C  CA  . GLU A 421 ? 0.2631 0.1902 0.1899 0.0314  0.0155  0.0829  407 GLU A CA  
3078 C  C   . GLU A 421 ? 0.2590 0.2539 0.2021 0.0499  0.0233  0.0658  407 GLU A C   
3079 O  O   . GLU A 421 ? 0.2767 0.2721 0.2743 0.0437  -0.0124 0.1096  407 GLU A O   
3080 C  CB  . GLU A 421 ? 0.2842 0.2125 0.2602 0.0587  0.0178  0.0464  407 GLU A CB  
3081 C  CG  . GLU A 421 ? 0.4056 0.3338 0.3613 -0.0534 0.0316  0.0266  407 GLU A CG  
3082 C  CD  . GLU A 421 ? 0.4417 0.3561 0.4814 0.1275  -0.0539 -0.0146 407 GLU A CD  
3083 O  OE1 . GLU A 421 ? 0.5058 0.2997 0.5395 0.0021  0.0293  -0.0672 407 GLU A OE1 
3084 O  OE2 . GLU A 421 ? 0.6030 0.4346 0.4502 0.1084  0.0680  0.0215  407 GLU A OE2 
3085 N  N   . THR A 422 ? 0.2623 0.2078 0.1660 0.0039  0.0314  0.0412  408 THR A N   
3086 C  CA  . THR A 422 ? 0.2327 0.1863 0.1650 0.0244  0.0118  0.0431  408 THR A CA  
3087 C  C   . THR A 422 ? 0.2457 0.2377 0.1956 0.0386  0.0065  0.0320  408 THR A C   
3088 O  O   . THR A 422 ? 0.2745 0.3353 0.1929 0.0370  -0.0124 0.0129  408 THR A O   
3089 C  CB  . THR A 422 ? 0.2136 0.1874 0.1959 0.0412  -0.0058 0.0336  408 THR A CB  
3090 O  OG1 . THR A 422 ? 0.2305 0.1978 0.1822 0.0317  0.0138  0.0333  408 THR A OG1 
3091 C  CG2 . THR A 422 ? 0.2704 0.1934 0.1541 0.0650  -0.0352 0.0302  408 THR A CG2 
3092 N  N   . GLY A 423 ? 0.2263 0.2313 0.1871 0.0407  -0.0235 0.0375  409 GLY A N   
3093 C  CA  . GLY A 423 ? 0.2659 0.2628 0.1856 0.0485  -0.0498 0.0242  409 GLY A CA  
3094 C  C   . GLY A 423 ? 0.2173 0.2506 0.1853 0.0460  -0.0020 0.0111  409 GLY A C   
3095 O  O   . GLY A 423 ? 0.3595 0.2796 0.1837 0.0857  -0.0368 -0.0059 409 GLY A O   
3096 N  N   . VAL A 424 ? 0.2663 0.2389 0.1548 0.0372  -0.0300 0.0380  410 VAL A N   
3097 C  CA  . VAL A 424 ? 0.2600 0.2344 0.1462 0.0296  -0.0065 0.0539  410 VAL A CA  
3098 C  C   . VAL A 424 ? 0.2447 0.2222 0.2048 0.0191  -0.0055 0.0242  410 VAL A C   
3099 O  O   . VAL A 424 ? 0.2703 0.2539 0.1758 0.0294  0.0232  0.0131  410 VAL A O   
3100 C  CB  . VAL A 424 ? 0.2178 0.2248 0.1228 0.0389  -0.0012 0.0114  410 VAL A CB  
3101 C  CG1 . VAL A 424 ? 0.2469 0.2169 0.1326 0.0537  0.0213  0.0202  410 VAL A CG1 
3102 C  CG2 . VAL A 424 ? 0.1926 0.2105 0.1765 0.0377  0.0165  0.0057  410 VAL A CG2 
3103 N  N   . ALA A 425 ? 0.2746 0.2606 0.1825 0.0641  -0.0034 0.0407  411 ALA A N   
3104 C  CA  . ALA A 425 ? 0.2719 0.2846 0.1943 0.0345  0.0063  0.0535  411 ALA A CA  
3105 C  C   . ALA A 425 ? 0.2669 0.2551 0.2065 0.0680  0.0372  -0.0103 411 ALA A C   
3106 O  O   . ALA A 425 ? 0.2845 0.2305 0.1647 0.0323  0.0586  0.0449  411 ALA A O   
3107 C  CB  . ALA A 425 ? 0.3251 0.2864 0.1934 0.0570  0.0137  0.0083  411 ALA A CB  
3108 N  N   . PRO A 426 ? 0.2776 0.2362 0.2489 0.0099  0.0451  0.0519  412 PRO A N   
3109 C  CA  . PRO A 426 ? 0.2411 0.2952 0.2635 -0.0064 0.0679  0.0007  412 PRO A CA  
3110 C  C   . PRO A 426 ? 0.2310 0.2601 0.1800 0.0299  0.0221  0.0047  412 PRO A C   
3111 O  O   . PRO A 426 ? 0.2296 0.2840 0.2214 -0.0189 0.0160  0.0077  412 PRO A O   
3112 C  CB  . PRO A 426 ? 0.3591 0.3172 0.3094 0.0073  0.0649  0.0468  412 PRO A CB  
3113 C  CG  . PRO A 426 ? 0.5537 0.4117 0.4428 0.0174  0.0181  0.1601  412 PRO A CG  
3114 C  CD  . PRO A 426 ? 0.3622 0.3173 0.3072 0.0710  0.0150  0.0943  412 PRO A CD  
3115 N  N   . GLU A 427 ? 0.2971 0.2728 0.2428 0.0249  0.0856  0.0303  413 GLU A N   
3116 C  CA  . GLU A 427 ? 0.2774 0.2595 0.1880 0.0396  0.0507  0.0366  413 GLU A CA  
3117 C  C   . GLU A 427 ? 0.2451 0.2526 0.1880 0.0357  0.0443  0.0290  413 GLU A C   
3118 O  O   . GLU A 427 ? 0.2696 0.2546 0.2292 0.0558  0.0473  0.0304  413 GLU A O   
3119 C  CB  . GLU A 427 ? 0.2713 0.3678 0.2216 0.0608  0.1426  0.0330  413 GLU A CB  
3120 C  CG  . GLU A 427 ? 0.4536 0.5914 0.2389 0.0107  0.1438  0.0360  413 GLU A CG  
3121 C  CD  . GLU A 427 ? 0.6088 0.6789 0.4837 0.0446  0.0371  0.0307  413 GLU A CD  
3122 O  OE1 . GLU A 427 ? 0.4726 0.6347 0.2757 0.0564  0.0518  0.0128  413 GLU A OE1 
3123 O  OE2 . GLU A 427 ? 0.5170 0.7721 0.4342 0.1171  0.0318  -0.0216 413 GLU A OE2 
3124 N  N   . LYS A 428 ? 0.2172 0.2382 0.1597 0.0421  0.0394  0.0121  414 LYS A N   
3125 C  CA  . LYS A 428 ? 0.2227 0.1944 0.1560 0.0233  0.0062  -0.0064 414 LYS A CA  
3126 C  C   . LYS A 428 ? 0.1863 0.1684 0.1274 0.0106  -0.0004 -0.0127 414 LYS A C   
3127 O  O   . LYS A 428 ? 0.1773 0.1931 0.1594 0.0155  0.0203  -0.0167 414 LYS A O   
3128 C  CB  . LYS A 428 ? 0.2178 0.2206 0.1298 0.0103  0.0132  -0.0076 414 LYS A CB  
3129 C  CG  . LYS A 428 ? 0.2337 0.2698 0.1446 0.0351  0.0110  -0.0103 414 LYS A CG  
3130 C  CD  . LYS A 428 ? 0.2180 0.2651 0.1241 0.0322  -0.0048 -0.0065 414 LYS A CD  
3131 C  CE  . LYS A 428 ? 0.2465 0.3026 0.1943 -0.0160 0.0189  -0.0227 414 LYS A CE  
3132 N  NZ  . LYS A 428 ? 0.3298 0.3629 0.2265 -0.0187 -0.0242 -0.0580 414 LYS A NZ  
3133 N  N   . ILE A 429 ? 0.2064 0.1874 0.1222 0.0059  0.0243  0.0314  415 ILE A N   
3134 C  CA  . ILE A 429 ? 0.1772 0.1860 0.1136 0.0115  0.0309  0.0100  415 ILE A CA  
3135 C  C   . ILE A 429 ? 0.1389 0.1875 0.1673 -0.0028 0.0123  -0.0098 415 ILE A C   
3136 O  O   . ILE A 429 ? 0.1877 0.2328 0.1708 0.0015  0.0353  0.0327  415 ILE A O   
3137 C  CB  . ILE A 429 ? 0.2301 0.1923 0.1665 0.0144  0.0401  -0.0070 415 ILE A CB  
3138 C  CG1 . ILE A 429 ? 0.2274 0.1905 0.1590 0.0186  0.0505  0.0302  415 ILE A CG1 
3139 C  CG2 . ILE A 429 ? 0.2052 0.1709 0.1927 -0.0161 0.0329  -0.0005 415 ILE A CG2 
3140 C  CD1 . ILE A 429 ? 0.3076 0.2252 0.1574 0.0310  0.0526  0.0317  415 ILE A CD1 
3141 N  N   . PHE A 430 ? 0.1631 0.1866 0.1676 0.0311  0.0186  0.0190  416 PHE A N   
3142 C  CA  . PHE A 430 ? 0.1524 0.1943 0.1619 0.0141  0.0026  0.0060  416 PHE A CA  
3143 C  C   . PHE A 430 ? 0.1834 0.1769 0.1942 0.0159  -0.0026 0.0050  416 PHE A C   
3144 O  O   . PHE A 430 ? 0.1708 0.2602 0.1740 0.0123  0.0246  -0.0187 416 PHE A O   
3145 C  CB  . PHE A 430 ? 0.1991 0.2425 0.1850 0.0458  0.0219  0.0051  416 PHE A CB  
3146 C  CG  . PHE A 430 ? 0.2003 0.1656 0.1836 0.0158  0.0174  0.0170  416 PHE A CG  
3147 C  CD1 . PHE A 430 ? 0.2386 0.1894 0.2179 0.0129  -0.0238 -0.0103 416 PHE A CD1 
3148 C  CD2 . PHE A 430 ? 0.2039 0.2098 0.2004 0.0281  -0.0176 -0.0053 416 PHE A CD2 
3149 C  CE1 . PHE A 430 ? 0.2007 0.2004 0.2135 0.0267  -0.0396 -0.0218 416 PHE A CE1 
3150 C  CE2 . PHE A 430 ? 0.2699 0.2597 0.2083 0.0438  0.0075  -0.0585 416 PHE A CE2 
3151 C  CZ  . PHE A 430 ? 0.2211 0.2432 0.2086 0.0060  -0.0415 -0.0496 416 PHE A CZ  
3152 N  N   . LEU A 431 ? 0.1888 0.1726 0.1652 -0.0111 0.0135  0.0138  417 LEU A N   
3153 C  CA  . LEU A 431 ? 0.1632 0.1821 0.1805 0.0149  0.0211  0.0278  417 LEU A CA  
3154 C  C   . LEU A 431 ? 0.1399 0.1977 0.1917 0.0373  0.0070  0.0160  417 LEU A C   
3155 O  O   . LEU A 431 ? 0.1949 0.2895 0.2348 0.0581  0.0451  0.0464  417 LEU A O   
3156 C  CB  . LEU A 431 ? 0.2288 0.2152 0.2261 -0.0231 0.0081  0.0384  417 LEU A CB  
3157 C  CG  . LEU A 431 ? 0.2681 0.1888 0.2243 -0.0093 0.0086  0.0522  417 LEU A CG  
3158 C  CD1 . LEU A 431 ? 0.3853 0.2446 0.3249 -0.0273 0.0624  0.0345  417 LEU A CD1 
3159 C  CD2 . LEU A 431 ? 0.2522 0.2531 0.3483 0.0141  0.1137  0.0754  417 LEU A CD2 
3160 N  N   . VAL A 432 ? 0.1782 0.1679 0.1459 0.0288  0.0118  0.0060  418 VAL A N   
3161 C  CA  . VAL A 432 ? 0.1758 0.1742 0.1845 0.0293  0.0194  0.0215  418 VAL A CA  
3162 C  C   . VAL A 432 ? 0.1580 0.1558 0.1626 -0.0108 0.0170  0.0190  418 VAL A C   
3163 O  O   . VAL A 432 ? 0.1782 0.1750 0.2045 0.0184  -0.0210 0.0048  418 VAL A O   
3164 C  CB  . VAL A 432 ? 0.2500 0.1866 0.2025 0.0231  -0.0481 0.0067  418 VAL A CB  
3165 C  CG1 . VAL A 432 ? 0.4113 0.2445 0.3386 -0.0141 -0.1248 0.0113  418 VAL A CG1 
3166 C  CG2 . VAL A 432 ? 0.2037 0.2321 0.2580 -0.0350 -0.0511 0.0302  418 VAL A CG2 
3167 N  N   . GLU A 433 ? 0.1480 0.1467 0.1588 0.0052  0.0208  0.0144  419 GLU A N   
3168 C  CA  . GLU A 433 ? 0.1394 0.1540 0.1935 -0.0029 0.0150  0.0185  419 GLU A CA  
3169 C  C   . GLU A 433 ? 0.1409 0.1297 0.1789 0.0051  0.0049  -0.0029 419 GLU A C   
3170 O  O   . GLU A 433 ? 0.1451 0.1423 0.1630 0.0014  0.0009  0.0020  419 GLU A O   
3171 C  CB  . GLU A 433 ? 0.1910 0.2347 0.2553 -0.0528 -0.0161 0.0546  419 GLU A CB  
3172 C  CG  . GLU A 433 ? 0.2658 0.2751 0.3015 -0.0033 0.0839  -0.0199 419 GLU A CG  
3173 C  CD  . GLU A 433 ? 0.3183 0.6257 0.4505 -0.0756 0.0626  -0.0676 419 GLU A CD  
3174 O  OE1 . GLU A 433 ? 0.3020 0.6113 0.5409 0.0024  0.0448  -0.0976 419 GLU A OE1 
3175 O  OE2 . GLU A 433 ? 0.4727 0.9051 0.5942 0.0120  -0.1169 -0.0372 419 GLU A OE2 
3176 N  N   . LYS A 434 ? 0.1338 0.1392 0.1727 0.0192  -0.0001 -0.0009 420 LYS A N   
3177 C  CA  . LYS A 434 ? 0.1173 0.1476 0.1578 -0.0010 0.0027  0.0188  420 LYS A CA  
3178 C  C   . LYS A 434 ? 0.1201 0.1379 0.1810 -0.0018 0.0143  0.0060  420 LYS A C   
3179 O  O   . LYS A 434 ? 0.1125 0.1728 0.1886 0.0153  0.0065  0.0109  420 LYS A O   
3180 C  CB  . LYS A 434 ? 0.1432 0.1604 0.1853 0.0106  -0.0003 -0.0019 420 LYS A CB  
3181 C  CG  . LYS A 434 ? 0.1598 0.1587 0.1664 0.0101  -0.0009 -0.0027 420 LYS A CG  
3182 C  CD  . LYS A 434 ? 0.1681 0.1865 0.2003 0.0159  -0.0025 -0.0061 420 LYS A CD  
3183 C  CE  . LYS A 434 ? 0.2001 0.2973 0.2072 0.0457  -0.0083 -0.0158 420 LYS A CE  
3184 N  NZ  . LYS A 434 ? 0.1911 0.3491 0.2228 -0.0308 -0.0174 -0.0528 420 LYS A NZ  
3185 N  N   . GLY A 435 ? 0.1275 0.1430 0.1417 0.0166  0.0110  -0.0032 421 GLY A N   
3186 C  CA  . GLY A 435 ? 0.1292 0.1212 0.1736 0.0312  0.0094  0.0080  421 GLY A CA  
3187 C  C   . GLY A 435 ? 0.1149 0.1333 0.1567 0.0123  0.0004  0.0056  421 GLY A C   
3188 O  O   . GLY A 435 ? 0.1606 0.1270 0.1802 0.0243  0.0051  0.0091  421 GLY A O   
3189 N  N   . ASP A 436 ? 0.1183 0.1340 0.1521 0.0124  0.0138  0.0122  422 ASP A N   
3190 C  CA  . ASP A 436 ? 0.1290 0.1380 0.1642 0.0169  -0.0009 -0.0098 422 ASP A CA  
3191 C  C   . ASP A 436 ? 0.1258 0.1627 0.1575 0.0124  -0.0048 0.0064  422 ASP A C   
3192 O  O   . ASP A 436 ? 0.1236 0.1877 0.1683 0.0110  0.0226  -0.0194 422 ASP A O   
3193 C  CB  . ASP A 436 ? 0.1677 0.1538 0.1921 0.0235  0.0140  0.0144  422 ASP A CB  
3194 C  CG  . ASP A 436 ? 0.1950 0.1830 0.2450 0.0285  0.0379  0.0205  422 ASP A CG  
3195 O  OD1 . ASP A 436 ? 0.1853 0.2297 0.2751 0.0038  0.0262  0.0319  422 ASP A OD1 
3196 O  OD2 . ASP A 436 ? 0.2481 0.1895 0.1981 0.0029  0.0436  0.0176  422 ASP A OD2 
3197 N  N   . VAL A 437 ? 0.1409 0.1575 0.1373 0.0140  0.0039  -0.0066 423 VAL A N   
3198 C  CA  . VAL A 437 ? 0.1285 0.1477 0.1448 0.0190  0.0035  -0.0135 423 VAL A CA  
3199 C  C   . VAL A 437 ? 0.1239 0.1550 0.1380 0.0073  0.0098  0.0023  423 VAL A C   
3200 O  O   . VAL A 437 ? 0.1489 0.1968 0.1554 0.0223  0.0200  -0.0093 423 VAL A O   
3201 C  CB  . VAL A 437 ? 0.1458 0.1634 0.1656 0.0199  0.0229  -0.0097 423 VAL A CB  
3202 C  CG1 . VAL A 437 ? 0.1918 0.1559 0.1800 0.0052  0.0085  -0.0017 423 VAL A CG1 
3203 C  CG2 . VAL A 437 ? 0.1792 0.1498 0.1647 0.0162  0.0070  -0.0054 423 VAL A CG2 
3204 N  N   . ILE A 438 ? 0.1416 0.1450 0.1294 0.0251  0.0120  -0.0101 424 ILE A N   
3205 C  CA  . ILE A 438 ? 0.1353 0.1687 0.1313 0.0072  0.0147  -0.0196 424 ILE A CA  
3206 C  C   . ILE A 438 ? 0.1576 0.1568 0.1430 0.0037  0.0220  -0.0081 424 ILE A C   
3207 O  O   . ILE A 438 ? 0.1907 0.1970 0.1523 -0.0197 0.0325  -0.0062 424 ILE A O   
3208 C  CB  . ILE A 438 ? 0.1701 0.1716 0.1866 0.0128  -0.0141 0.0040  424 ILE A CB  
3209 C  CG1 . ILE A 438 ? 0.1848 0.1731 0.2197 0.0258  0.0106  -0.0303 424 ILE A CG1 
3210 C  CG2 . ILE A 438 ? 0.2103 0.2616 0.2453 0.0913  0.0007  -0.0007 424 ILE A CG2 
3211 C  CD1 . ILE A 438 ? 0.2550 0.1750 0.3457 0.0331  0.0237  -0.0184 424 ILE A CD1 
3212 N  N   . SER A 439 ? 0.1511 0.1911 0.1450 0.0183  0.0102  -0.0072 425 SER A N   
3213 C  CA  A SER A 439 ? 0.1665 0.2039 0.1439 0.0129  0.0187  -0.0065 425 SER A CA  
3214 C  CA  B SER A 439 ? 0.1612 0.2000 0.1431 0.0230  0.0292  -0.0105 425 SER A CA  
3215 C  C   . SER A 439 ? 0.1505 0.1594 0.1510 0.0243  0.0096  -0.0210 425 SER A C   
3216 O  O   . SER A 439 ? 0.1656 0.2191 0.1803 -0.0051 -0.0041 0.0037  425 SER A O   
3217 C  CB  A SER A 439 ? 0.1910 0.1782 0.2056 -0.0147 -0.0254 -0.0171 425 SER A CB  
3218 C  CB  B SER A 439 ? 0.2275 0.1641 0.1330 0.0211  0.0094  -0.0282 425 SER A CB  
3219 O  OG  A SER A 439 ? 0.2651 0.2091 0.2904 -0.0043 -0.0338 -0.0435 425 SER A OG  
3220 O  OG  B SER A 439 ? 0.1798 0.1810 0.1872 0.0577  0.0332  -0.0084 425 SER A OG  
3221 N  N   . TYR A 440 ? 0.1757 0.1925 0.1232 0.0108  0.0059  -0.0087 426 TYR A N   
3222 C  CA  . TYR A 440 ? 0.1914 0.2020 0.1196 0.0218  0.0078  -0.0068 426 TYR A CA  
3223 C  C   . TYR A 440 ? 0.1756 0.2402 0.1498 -0.0092 -0.0077 -0.0208 426 TYR A C   
3224 O  O   . TYR A 440 ? 0.2426 0.2328 0.1666 -0.0202 0.0018  -0.0516 426 TYR A O   
3225 C  CB  . TYR A 440 ? 0.1776 0.2400 0.1430 0.0315  -0.0020 -0.0282 426 TYR A CB  
3226 C  CG  . TYR A 440 ? 0.1992 0.2426 0.1940 0.0410  -0.0146 -0.0484 426 TYR A CG  
3227 C  CD1 . TYR A 440 ? 0.2057 0.2504 0.1850 0.0110  -0.0168 -0.0088 426 TYR A CD1 
3228 C  CD2 . TYR A 440 ? 0.2054 0.2559 0.2001 0.0232  0.0083  -0.0326 426 TYR A CD2 
3229 C  CE1 . TYR A 440 ? 0.1954 0.2525 0.1883 -0.0017 -0.0222 0.0161  426 TYR A CE1 
3230 C  CE2 . TYR A 440 ? 0.1585 0.2860 0.2341 0.0040  -0.0080 0.0123  426 TYR A CE2 
3231 C  CZ  . TYR A 440 ? 0.2274 0.3064 0.1939 0.0047  -0.0535 -0.0340 426 TYR A CZ  
3232 O  OH  . TYR A 440 ? 0.2437 0.3905 0.2317 0.0489  -0.0561 -0.0023 426 TYR A OH  
3233 N  N   . ASN A 441 ? 0.2325 0.2073 0.1355 0.0076  -0.0011 -0.0197 427 ASN A N   
3234 C  CA  . ASN A 441 ? 0.2054 0.2294 0.2095 -0.0070 -0.0144 -0.0142 427 ASN A CA  
3235 C  C   . ASN A 441 ? 0.2456 0.2829 0.2350 -0.0111 -0.0204 -0.0438 427 ASN A C   
3236 O  O   . ASN A 441 ? 0.2800 0.3009 0.2338 0.0188  -0.0265 -0.0776 427 ASN A O   
3237 C  CB  . ASN A 441 ? 0.2216 0.2193 0.2060 0.0225  -0.0279 -0.0661 427 ASN A CB  
3238 C  CG  . ASN A 441 ? 0.2166 0.2292 0.1947 0.0004  0.0001  -0.0353 427 ASN A CG  
3239 O  OD1 . ASN A 441 ? 0.2024 0.2793 0.1583 0.0087  0.0072  -0.0338 427 ASN A OD1 
3240 N  ND2 . ASN A 441 ? 0.2317 0.2727 0.2050 0.0039  0.0208  -0.0751 427 ASN A ND2 
3241 N  N   . GLY A 442 ? 0.2711 0.2877 0.1563 0.0028  -0.0378 -0.0516 428 GLY A N   
3242 C  CA  . GLY A 442 ? 0.2173 0.3356 0.2407 -0.0413 -0.0222 -0.0414 428 GLY A CA  
3243 C  C   . GLY A 442 ? 0.2861 0.3077 0.2454 -0.0162 -0.0593 0.0011  428 GLY A C   
3244 O  O   . GLY A 442 ? 0.3093 0.4421 0.2172 0.0359  -0.0550 -0.0015 428 GLY A O   
3245 N  N   . LYS A 443 ? 0.2266 0.3880 0.1802 -0.0004 -0.0072 -0.0232 429 LYS A N   
3246 C  CA  . LYS A 443 ? 0.3185 0.3494 0.2734 -0.0091 -0.0534 0.0390  429 LYS A CA  
3247 C  C   . LYS A 443 ? 0.3238 0.3162 0.3146 0.0620  -0.0434 -0.0296 429 LYS A C   
3248 O  O   . LYS A 443 ? 0.3253 0.3857 0.3203 0.0099  -0.1042 0.0192  429 LYS A O   
3249 C  CB  . LYS A 443 ? 0.2907 0.4438 0.2546 -0.0808 -0.0112 0.0096  429 LYS A CB  
3250 C  CG  . LYS A 443 ? 0.3012 0.4706 0.3046 -0.0262 -0.0169 -0.0563 429 LYS A CG  
3251 C  CD  . LYS A 443 ? 0.3406 0.4936 0.4232 -0.0758 0.0801  0.0042  429 LYS A CD  
3252 N  N   . ASP A 444 ? 0.2595 0.2949 0.1648 -0.0130 -0.0195 -0.0091 430 ASP A N   
3253 C  CA  . ASP A 444 ? 0.2234 0.2734 0.1768 0.0047  0.0109  0.0090  430 ASP A CA  
3254 C  C   . ASP A 444 ? 0.1638 0.2659 0.2122 0.0028  0.0051  0.0109  430 ASP A C   
3255 O  O   . ASP A 444 ? 0.2019 0.2298 0.1832 0.0102  0.0170  -0.0137 430 ASP A O   
3256 C  CB  . ASP A 444 ? 0.2462 0.2973 0.1979 0.0134  0.0375  0.0298  430 ASP A CB  
3257 C  CG  . ASP A 444 ? 0.3144 0.3126 0.2493 0.0081  -0.0516 -0.0324 430 ASP A CG  
3258 O  OD1 . ASP A 444 ? 0.4231 0.4826 0.1915 -0.0212 0.0335  0.0545  430 ASP A OD1 
3259 O  OD2 . ASP A 444 ? 0.2925 0.3681 0.2609 0.0835  -0.0001 -0.0421 430 ASP A OD2 
3260 N  N   . MET A 445 ? 0.1965 0.2590 0.1746 0.0254  -0.0003 0.0215  431 MET A N   
3261 C  CA  A MET A 445 ? 0.2232 0.2362 0.1909 0.0149  -0.0044 -0.0218 431 MET A CA  
3262 C  CA  B MET A 445 ? 0.1788 0.2067 0.1776 0.0109  0.0044  -0.0192 431 MET A CA  
3263 C  C   . MET A 445 ? 0.1862 0.2116 0.1900 0.0057  0.0213  -0.0225 431 MET A C   
3264 O  O   . MET A 445 ? 0.2003 0.2438 0.1785 0.0060  -0.0093 0.0021  431 MET A O   
3265 C  CB  A MET A 445 ? 0.2715 0.2016 0.2088 0.0402  0.0174  0.0176  431 MET A CB  
3266 C  CB  B MET A 445 ? 0.1526 0.1696 0.2252 0.0315  0.0141  0.0100  431 MET A CB  
3267 C  CG  A MET A 445 ? 0.4537 0.3470 0.5157 0.0421  0.0040  -0.0115 431 MET A CG  
3268 C  CG  B MET A 445 ? 0.1037 0.1354 0.1300 0.0302  0.0556  -0.0148 431 MET A CG  
3269 S  SD  A MET A 445 ? 0.1982 0.2024 0.1963 0.0270  0.0211  -0.0126 431 MET A SD  
3270 S  SD  B MET A 445 ? 0.2376 0.2739 0.2343 0.0610  0.0426  0.0019  431 MET A SD  
3271 C  CE  A MET A 445 ? 0.1787 0.2791 0.3446 0.0781  -0.0415 -0.0129 431 MET A CE  
3272 C  CE  B MET A 445 ? 0.2087 0.2512 0.1416 0.0584  0.0551  0.0866  431 MET A CE  
3273 N  N   . ILE A 446 ? 0.1670 0.2097 0.1341 0.0134  0.0054  -0.0152 432 ILE A N   
3274 C  CA  . ILE A 446 ? 0.1817 0.2155 0.1542 0.0038  0.0063  -0.0161 432 ILE A CA  
3275 C  C   . ILE A 446 ? 0.1963 0.1868 0.1504 0.0027  0.0141  -0.0065 432 ILE A C   
3276 O  O   . ILE A 446 ? 0.1865 0.1933 0.1222 0.0190  0.0191  -0.0089 432 ILE A O   
3277 C  CB  . ILE A 446 ? 0.1816 0.2307 0.1833 0.0193  0.0207  -0.0239 432 ILE A CB  
3278 C  CG1 . ILE A 446 ? 0.1651 0.1899 0.2066 0.0120  0.0119  -0.0210 432 ILE A CG1 
3279 C  CG2 . ILE A 446 ? 0.2286 0.2565 0.1821 0.0433  0.0289  -0.0100 432 ILE A CG2 
3280 C  CD1 . ILE A 446 ? 0.2034 0.2190 0.2235 0.0215  0.0540  -0.0407 432 ILE A CD1 
3281 N  N   . LEU A 447 ? 0.1830 0.2273 0.1399 0.0168  0.0150  -0.0023 433 LEU A N   
3282 C  CA  . LEU A 447 ? 0.1781 0.1983 0.1841 0.0132  0.0061  0.0090  433 LEU A CA  
3283 C  C   . LEU A 447 ? 0.1785 0.2039 0.1473 0.0036  0.0073  0.0025  433 LEU A C   
3284 O  O   . LEU A 447 ? 0.2077 0.2541 0.2375 0.0145  0.0304  -0.0262 433 LEU A O   
3285 C  CB  . LEU A 447 ? 0.2019 0.2615 0.1808 0.0038  0.0278  -0.0142 433 LEU A CB  
3286 C  CG  . LEU A 447 ? 0.3194 0.2949 0.3272 0.0284  -0.0425 -0.0481 433 LEU A CG  
3287 C  CD1 . LEU A 447 ? 0.4388 0.4025 0.2523 -0.0704 0.0676  -0.0833 433 LEU A CD1 
3288 C  CD2 . LEU A 447 ? 0.4817 0.3296 0.3490 -0.0349 0.0091  -0.1415 433 LEU A CD2 
3289 N  N   . ASN A 448 ? 0.1590 0.2335 0.1576 0.0155  0.0155  0.0053  434 ASN A N   
3290 C  CA  . ASN A 448 ? 0.1628 0.2354 0.2070 0.0477  0.0312  0.0119  434 ASN A CA  
3291 C  C   . ASN A 448 ? 0.2480 0.2474 0.1725 0.0890  0.0309  -0.0086 434 ASN A C   
3292 O  O   . ASN A 448 ? 0.2911 0.3449 0.2383 0.1504  0.0685  -0.0025 434 ASN A O   
3293 C  CB  . ASN A 448 ? 0.2072 0.2892 0.1798 0.0625  0.0343  -0.0115 434 ASN A CB  
3294 C  CG  . ASN A 448 ? 0.2263 0.2675 0.2039 0.0191  0.0043  -0.0360 434 ASN A CG  
3295 O  OD1 . ASN A 448 ? 0.2772 0.3200 0.2424 0.0785  0.0457  -0.0008 434 ASN A OD1 
3296 N  ND2 . ASN A 448 ? 0.3243 0.3050 0.2074 0.0638  0.0420  -0.0451 434 ASN A ND2 
3297 N  N   . GLU A 449 ? 0.1830 0.2068 0.1969 0.0796  0.0355  0.0027  435 GLU A N   
3298 C  CA  . GLU A 449 ? 0.1897 0.2153 0.1752 0.0564  0.0022  0.0072  435 GLU A CA  
3299 C  C   . GLU A 449 ? 0.1761 0.2100 0.1513 0.0485  0.0067  -0.0050 435 GLU A C   
3300 O  O   . GLU A 449 ? 0.1439 0.1870 0.2011 0.0329  0.0299  0.0049  435 GLU A O   
3301 C  CB  . GLU A 449 ? 0.2160 0.2142 0.2626 0.0752  0.0140  -0.0156 435 GLU A CB  
3302 C  CG  . GLU A 449 ? 0.2229 0.2577 0.2585 0.0217  0.0439  -0.0087 435 GLU A CG  
3303 C  CD  . GLU A 449 ? 0.2765 0.2595 0.2713 0.0345  0.0009  -0.0257 435 GLU A CD  
3304 O  OE1 . GLU A 449 ? 0.3059 0.2681 0.2705 0.0055  0.0493  -0.0164 435 GLU A OE1 
3305 O  OE2 . GLU A 449 ? 0.2704 0.2946 0.3520 0.0607  0.0287  -0.0140 435 GLU A OE2 
3306 N  N   . LYS A 450 ? 0.1648 0.2251 0.1873 0.0521  0.0280  -0.0151 436 LYS A N   
3307 C  CA  . LYS A 450 ? 0.1913 0.2163 0.1761 0.0259  -0.0078 0.0158  436 LYS A CA  
3308 C  C   . LYS A 450 ? 0.2025 0.1472 0.2154 0.0513  0.0077  0.0357  436 LYS A C   
3309 O  O   . LYS A 450 ? 0.2707 0.2030 0.2321 0.0932  0.0345  -0.0001 436 LYS A O   
3310 C  CB  . LYS A 450 ? 0.2296 0.2859 0.1769 0.0051  -0.0050 0.0150  436 LYS A CB  
3311 C  CG  . LYS A 450 ? 0.2545 0.4137 0.2718 -0.0198 -0.0052 0.0240  436 LYS A CG  
3312 C  CD  . LYS A 450 ? 0.4103 0.6657 0.4403 -0.1062 -0.0157 0.0859  436 LYS A CD  
3313 C  CE  . LYS A 450 ? 0.3408 0.6685 0.5783 -0.0533 0.0518  -0.0406 436 LYS A CE  
3314 N  NZ  . LYS A 450 ? 0.3450 0.3916 0.2890 -0.0135 0.0813  -0.0182 436 LYS A NZ  
3315 N  N   . VAL A 451 ? 0.1499 0.1479 0.1766 0.0399  0.0160  0.0152  437 VAL A N   
3316 C  CA  . VAL A 451 ? 0.1778 0.1476 0.1919 0.0487  0.0074  0.0098  437 VAL A CA  
3317 C  C   . VAL A 451 ? 0.1223 0.1836 0.1791 0.0323  -0.0022 0.0065  437 VAL A C   
3318 O  O   . VAL A 451 ? 0.1391 0.1636 0.2137 0.0168  -0.0087 0.0171  437 VAL A O   
3319 C  CB  . VAL A 451 ? 0.1841 0.1577 0.1920 0.0132  -0.0320 0.0319  437 VAL A CB  
3320 C  CG1 . VAL A 451 ? 0.2714 0.1825 0.2311 -0.0239 -0.0364 0.0141  437 VAL A CG1 
3321 C  CG2 . VAL A 451 ? 0.1373 0.1698 0.2257 0.0119  -0.0092 0.0455  437 VAL A CG2 
3322 N  N   . GLN A 452 ? 0.1584 0.1304 0.1909 0.0441  -0.0028 0.0075  438 GLN A N   
3323 C  CA  . GLN A 452 ? 0.1312 0.1385 0.2094 0.0434  -0.0097 0.0165  438 GLN A CA  
3324 C  C   . GLN A 452 ? 0.1110 0.1447 0.1611 0.0315  -0.0377 0.0228  438 GLN A C   
3325 O  O   . GLN A 452 ? 0.1244 0.1604 0.2062 0.0092  -0.0142 0.0189  438 GLN A O   
3326 C  CB  . GLN A 452 ? 0.1460 0.1391 0.1970 0.0604  -0.0145 0.0446  438 GLN A CB  
3327 C  CG  . GLN A 452 ? 0.1600 0.1241 0.2070 0.0276  -0.0221 0.0306  438 GLN A CG  
3328 C  CD  . GLN A 452 ? 0.1290 0.1364 0.2077 0.0222  -0.0128 0.0040  438 GLN A CD  
3329 O  OE1 . GLN A 452 ? 0.1734 0.1734 0.2009 0.0650  -0.0107 0.0277  438 GLN A OE1 
3330 N  NE2 . GLN A 452 ? 0.1104 0.1467 0.2059 0.0298  -0.0328 0.0160  438 GLN A NE2 
3331 N  N   . SER A 453 ? 0.1161 0.1401 0.1896 0.0241  -0.0159 0.0055  439 SER A N   
3332 C  CA  . SER A 453 ? 0.1642 0.1279 0.2107 0.0438  -0.0225 0.0008  439 SER A CA  
3333 C  C   . SER A 453 ? 0.1136 0.1640 0.1642 0.0115  0.0153  0.0128  439 SER A C   
3334 O  O   . SER A 453 ? 0.1430 0.2090 0.2238 0.0038  -0.0105 0.0122  439 SER A O   
3335 C  CB  . SER A 453 ? 0.1238 0.1459 0.1991 0.0232  0.0220  0.0393  439 SER A CB  
3336 O  OG  . SER A 453 ? 0.1713 0.1843 0.1950 0.0183  -0.0035 0.0420  439 SER A OG  
3337 N  N   . GLY A 454 ? 0.1368 0.1535 0.1679 0.0057  -0.0041 -0.0103 440 GLY A N   
3338 C  CA  . GLY A 454 ? 0.1542 0.2057 0.2174 0.0242  -0.0106 -0.0061 440 GLY A CA  
3339 C  C   . GLY A 454 ? 0.1549 0.1407 0.1866 -0.0066 0.0009  -0.0031 440 GLY A C   
3340 O  O   . GLY A 454 ? 0.1250 0.1469 0.2097 0.0094  -0.0079 0.0106  440 GLY A O   
3341 N  N   . ASN A 455 ? 0.1476 0.2118 0.1989 -0.0136 0.0013  -0.0230 441 ASN A N   
3342 C  CA  . ASN A 455 ? 0.1295 0.2214 0.2037 -0.0151 -0.0190 -0.0027 441 ASN A CA  
3343 C  C   . ASN A 455 ? 0.1340 0.2520 0.2156 0.0124  -0.0206 -0.0021 441 ASN A C   
3344 O  O   . ASN A 455 ? 0.1580 0.3728 0.2495 0.0434  -0.0349 0.0361  441 ASN A O   
3345 C  CB  . ASN A 455 ? 0.1518 0.2681 0.2443 -0.0378 0.0276  -0.0402 441 ASN A CB  
3346 C  CG  . ASN A 455 ? 0.2162 0.1950 0.2702 -0.0208 0.0135  -0.0203 441 ASN A CG  
3347 O  OD1 . ASN A 455 ? 0.2176 0.2550 0.3094 -0.0083 -0.0252 0.0377  441 ASN A OD1 
3348 N  ND2 . ASN A 455 ? 0.2550 0.3156 0.2733 -0.0451 -0.0628 -0.0243 441 ASN A ND2 
3349 N  N   . ILE A 456 ? 0.1572 0.2326 0.2387 -0.0105 -0.0533 0.0069  442 ILE A N   
3350 C  CA  . ILE A 456 ? 0.1276 0.2635 0.2468 -0.0221 -0.0287 0.0155  442 ILE A CA  
3351 C  C   . ILE A 456 ? 0.1799 0.2453 0.2062 0.0138  -0.0425 0.0015  442 ILE A C   
3352 O  O   . ILE A 456 ? 0.1720 0.2322 0.2111 0.0209  -0.0539 -0.0136 442 ILE A O   
3353 C  CB  . ILE A 456 ? 0.2017 0.2597 0.2478 -0.0027 -0.0578 0.0073  442 ILE A CB  
3354 C  CG1 . ILE A 456 ? 0.2322 0.3198 0.2882 0.0491  -0.0454 0.0143  442 ILE A CG1 
3355 C  CG2 . ILE A 456 ? 0.3310 0.2740 0.2680 0.0254  0.0089  0.0345  442 ILE A CG2 
3356 C  CD1 . ILE A 456 ? 0.2670 0.2940 0.2261 0.0613  -0.0146 -0.0173 442 ILE A CD1 
3357 N  N   . LEU A 457 ? 0.1781 0.2643 0.2354 -0.0137 -0.0705 0.0093  443 LEU A N   
3358 C  CA  . LEU A 457 ? 0.2043 0.3410 0.2287 -0.0200 -0.0761 -0.0156 443 LEU A CA  
3359 C  C   . LEU A 457 ? 0.2077 0.3396 0.2417 0.0235  -0.0696 0.0067  443 LEU A C   
3360 O  O   . LEU A 457 ? 0.3035 0.4099 0.2982 0.0476  -0.0781 0.0588  443 LEU A O   
3361 C  CB  . LEU A 457 ? 0.1617 0.3921 0.2744 -0.0091 -0.0847 -0.0389 443 LEU A CB  
3362 C  CG  . LEU A 457 ? 0.2356 0.3883 0.3988 -0.0022 -0.0564 0.0459  443 LEU A CG  
3363 C  CD1 . LEU A 457 ? 0.2239 0.6660 0.3948 -0.1653 -0.0922 0.0182  443 LEU A CD1 
3364 C  CD2 . LEU A 457 ? 0.2782 0.5139 0.3818 -0.0721 -0.0287 0.0022  443 LEU A CD2 
3365 N  N   . ILE A 458 ? 0.1909 0.3863 0.2181 0.0340  -0.0736 0.0315  444 ILE A N   
3366 C  CA  . ILE A 458 ? 0.2352 0.4303 0.2884 0.0384  0.0060  0.0148  444 ILE A CA  
3367 C  C   . ILE A 458 ? 0.3319 0.3279 0.2056 0.0005  -0.0452 0.0019  444 ILE A C   
3368 O  O   . ILE A 458 ? 0.3485 0.3979 0.2343 -0.0086 -0.0833 -0.0245 444 ILE A O   
3369 C  CB  . ILE A 458 ? 0.2664 0.3544 0.2292 0.0079  -0.0365 0.0336  444 ILE A CB  
3370 C  CG1 . ILE A 458 ? 0.3141 0.3641 0.2482 0.0394  -0.0510 -0.0007 444 ILE A CG1 
3371 C  CG2 . ILE A 458 ? 0.3022 0.3916 0.2218 0.0014  -0.0196 0.0021  444 ILE A CG2 
3372 C  CD1 . ILE A 458 ? 0.2924 0.3595 0.1989 0.0246  0.0384  -0.0183 444 ILE A CD1 
3373 N  N   . ASP A 459 ? 0.4320 0.4912 0.2681 -0.0006 -0.0768 0.0432  445 ASP A N   
3374 C  CA  . ASP A 459 ? 0.5279 0.7020 0.3977 -0.0060 -0.1159 0.0050  445 ASP A CA  
3375 C  C   . ASP A 459 ? 0.7911 0.8757 0.6299 -0.0557 0.0969  0.0273  445 ASP A C   
3376 O  O   . ASP A 459 ? 0.9481 0.8712 0.3217 -0.2162 -0.0243 -0.0358 445 ASP A O   
3377 C  CB  . ASP A 459 ? 0.2947 0.5119 0.4365 0.0727  -0.0890 -0.0819 445 ASP A CB  
3378 N  N   . GLY A 460 ? 0.7005 0.3751 0.6429 0.1341  -0.0039 -0.1059 446 GLY A N   
3379 C  CA  . GLY A 460 ? 0.5550 0.4489 0.3684 0.0387  -0.1099 -0.0352 446 GLY A CA  
3380 C  C   . GLY A 460 ? 0.5540 0.5707 0.6220 -0.0186 -0.0660 0.1522  446 GLY A C   
3381 O  O   . GLY A 460 ? 0.6399 1.0138 0.6859 0.3208  -0.0404 -0.0082 446 GLY A O   
3382 MN MN  . MN  B .   ? 0.1606 0.1040 0.1605 0.0025  -0.0033 0.0168  601 MN  A MN  
3383 O  O   . HOH C .   ? 0.4847 0.4497 0.3324 -0.0928 -0.0434 -0.0511 701 HOH A O   
3384 O  O   . HOH C .   ? 0.3425 0.3616 0.5352 0.0801  -0.0039 -0.1047 702 HOH A O   
3385 O  O   . HOH C .   ? 0.3499 0.4428 0.3361 0.0260  0.0763  0.0107  703 HOH A O   
3386 O  O   . HOH C .   ? 0.2888 0.3373 0.2967 -0.0027 0.0288  -0.0553 704 HOH A O   
3387 O  O   . HOH C .   ? 0.4269 0.4293 0.3863 -0.0732 0.0734  -0.0886 705 HOH A O   
3388 O  O   . HOH C .   ? 0.6101 0.4306 0.4094 0.0721  -0.0340 0.0023  706 HOH A O   
3389 O  O   . HOH C .   ? 0.5111 0.2582 0.5181 0.0217  0.0019  -0.1157 707 HOH A O   
3390 O  O   . HOH C .   ? 0.4722 0.2537 0.4264 -0.0348 0.0555  -0.0165 708 HOH A O   
3391 O  O   . HOH C .   ? 0.3351 0.3793 0.2856 0.0397  -0.0125 -0.0474 709 HOH A O   
3392 O  O   . HOH C .   ? 0.3511 0.2577 0.4375 0.0287  0.0048  -0.0058 710 HOH A O   
3393 O  O   . HOH C .   ? 0.3261 0.2884 0.3739 0.0152  0.0788  -0.0674 711 HOH A O   
3394 O  O   . HOH C .   ? 0.3711 0.3997 0.2688 -0.0782 -0.0217 0.0387  712 HOH A O   
3395 O  O   . HOH C .   ? 0.2216 0.2623 0.2719 0.0446  -0.0617 -0.0399 713 HOH A O   
3396 O  O   . HOH C .   ? 0.2480 0.3581 0.2110 0.0240  0.0105  -0.0784 714 HOH A O   
3397 O  O   . HOH C .   ? 0.3267 0.4598 0.5703 0.0397  -0.0448 0.0832  715 HOH A O   
3398 O  O   . HOH C .   ? 0.3406 0.3299 0.3382 0.0085  0.0196  0.0431  716 HOH A O   
3399 O  O   . HOH C .   ? 0.3761 0.3552 0.2182 0.0376  -0.0117 -0.0540 717 HOH A O   
3400 O  O   . HOH C .   ? 0.4260 0.2207 0.4569 0.0573  0.0100  -0.0234 718 HOH A O   
3401 O  O   . HOH C .   ? 0.5673 0.3732 0.5021 0.1142  -0.0832 -0.0013 719 HOH A O   
3402 O  O   . HOH C .   ? 0.2330 0.2907 0.3752 -0.0170 0.0026  -0.0885 720 HOH A O   
3403 O  O   . HOH C .   ? 0.3541 0.5992 0.3764 0.0669  -0.0722 0.1376  721 HOH A O   
3404 O  O   . HOH C .   ? 0.3705 0.3451 0.3738 -0.0818 -0.0208 -0.0470 722 HOH A O   
3405 O  O   . HOH C .   ? 0.2641 0.2391 0.3005 -0.0122 0.0340  -0.0051 723 HOH A O   
3406 O  O   . HOH C .   ? 0.2548 0.2595 0.2798 -0.0011 -0.0092 -0.0838 724 HOH A O   
3407 O  O   . HOH C .   ? 0.3526 0.3606 0.4356 -0.0771 0.0709  0.0231  725 HOH A O   
3408 O  O   . HOH C .   ? 0.5032 0.6604 0.5807 0.0375  -0.0606 -0.0420 726 HOH A O   
3409 O  O   . HOH C .   ? 0.2221 0.2016 0.2274 0.0254  0.0458  0.0178  727 HOH A O   
3410 O  O   . HOH C .   ? 0.1356 0.2312 0.2613 -0.0111 -0.0036 -0.0155 728 HOH A O   
3411 O  O   . HOH C .   ? 0.1762 0.1582 0.1754 0.0217  -0.0124 -0.0081 729 HOH A O   
3412 O  O   . HOH C .   ? 0.4551 0.2499 0.3274 0.0081  0.0367  0.0121  730 HOH A O   
3413 O  O   . HOH C .   ? 0.1462 0.2411 0.1940 0.0255  0.0127  0.0250  731 HOH A O   
3414 O  O   . HOH C .   ? 0.1578 0.2915 0.1658 0.0343  0.0329  -0.0081 732 HOH A O   
3415 O  O   . HOH C .   ? 0.2454 0.2477 0.3130 0.0913  -0.0043 -0.0062 733 HOH A O   
3416 O  O   . HOH C .   ? 0.3070 0.3228 0.7312 -0.0728 -0.0419 -0.0184 734 HOH A O   
3417 O  O   . HOH C .   ? 0.2702 0.3699 0.2949 -0.0693 -0.0878 0.0216  735 HOH A O   
3418 O  O   . HOH C .   ? 0.1262 0.1589 0.2196 -0.0285 0.0372  -0.0082 736 HOH A O   
3419 O  O   . HOH C .   ? 0.4750 0.4221 0.2738 0.0626  0.0643  0.1181  737 HOH A O   
3420 O  O   . HOH C .   ? 0.4059 0.2675 0.2331 0.0099  0.0478  0.0729  738 HOH A O   
3421 O  O   . HOH C .   ? 0.2698 0.4019 0.2762 -0.0833 -0.0583 0.1026  739 HOH A O   
3422 O  O   . HOH C .   ? 0.2900 0.2774 0.3833 -0.0765 0.0300  0.0190  740 HOH A O   
3423 O  O   . HOH C .   ? 0.4551 0.4576 0.4631 0.0944  0.0281  -0.1455 741 HOH A O   
3424 O  O   . HOH C .   ? 0.3276 0.3826 0.2907 0.0986  -0.0577 -0.0551 742 HOH A O   
3425 O  O   . HOH C .   ? 0.4701 0.4953 0.4314 0.1084  0.1102  0.1548  743 HOH A O   
3426 O  O   . HOH C .   ? 0.5267 0.5696 0.5450 0.1642  0.0136  0.0396  744 HOH A O   
3427 O  O   . HOH C .   ? 0.2262 0.1814 0.2597 0.0593  0.0021  0.0162  745 HOH A O   
3428 O  O   . HOH C .   ? 0.3513 0.3878 0.3325 -0.1146 0.0131  0.0748  746 HOH A O   
3429 O  O   . HOH C .   ? 0.3510 0.2966 0.2032 0.0257  -0.0350 0.0340  747 HOH A O   
3430 O  O   . HOH C .   ? 0.2891 0.1962 0.2736 0.0433  -0.0087 -0.0435 748 HOH A O   
3431 O  O   . HOH C .   ? 0.3832 0.3075 0.3148 0.1277  0.0048  0.0005  749 HOH A O   
3432 O  O   . HOH C .   ? 0.2432 0.2409 0.3364 -0.0657 0.0411  0.0938  750 HOH A O   
3433 O  O   . HOH C .   ? 0.1452 0.3380 0.4106 0.0557  -0.0189 -0.1115 751 HOH A O   
3434 O  O   . HOH C .   ? 0.5309 0.3682 0.7159 0.0162  -0.1170 0.0741  752 HOH A O   
3435 O  O   . HOH C .   ? 0.2109 0.2303 0.1797 0.0406  -0.0111 0.0152  753 HOH A O   
3436 O  O   . HOH C .   ? 0.2149 0.3154 0.4884 -0.0421 -0.0520 0.1142  754 HOH A O   
3437 O  O   . HOH C .   ? 0.3554 0.3696 0.2504 0.1687  -0.0289 -0.0003 755 HOH A O   
3438 O  O   . HOH C .   ? 0.4649 0.3576 0.3804 -0.0707 0.0965  -0.0474 756 HOH A O   
3439 O  O   . HOH C .   ? 0.4129 0.2502 0.4505 0.0508  -0.0063 -0.0371 757 HOH A O   
3440 O  O   . HOH C .   ? 0.5472 0.3256 0.3166 -0.0192 -0.0103 0.0427  758 HOH A O   
3441 O  O   . HOH C .   ? 0.1884 0.1292 0.2128 -0.0026 0.0137  0.0298  759 HOH A O   
3442 O  O   . HOH C .   ? 0.3677 0.4277 0.3729 0.1026  0.1194  -0.0059 760 HOH A O   
3443 O  O   . HOH C .   ? 0.2248 0.3832 0.4108 -0.0359 -0.0285 0.0001  761 HOH A O   
3444 O  O   . HOH C .   ? 0.2342 0.2445 0.1833 0.0281  0.0136  -0.0034 762 HOH A O   
3445 O  O   . HOH C .   ? 0.2560 0.4134 0.3923 0.0142  0.0780  -0.0694 763 HOH A O   
3446 O  O   . HOH C .   ? 0.3226 0.4929 0.6388 -0.0203 0.0228  -0.0876 764 HOH A O   
3447 O  O   . HOH C .   ? 0.4556 0.4400 0.2750 0.0610  0.0293  0.0734  765 HOH A O   
3448 O  O   . HOH C .   ? 0.3518 0.3217 0.2388 0.0169  0.0455  0.0812  766 HOH A O   
3449 O  O   . HOH C .   ? 0.2123 0.2399 0.1813 -0.0316 0.0265  -0.0198 767 HOH A O   
3450 O  O   . HOH C .   ? 0.5293 0.4677 0.4683 0.0375  -0.0690 0.0616  768 HOH A O   
3451 O  O   . HOH C .   ? 0.5182 0.2231 0.2998 -0.0306 0.0231  0.0155  769 HOH A O   
3452 O  O   . HOH C .   ? 0.4479 0.2844 0.4205 0.0749  -0.0560 0.0011  770 HOH A O   
3453 O  O   . HOH C .   ? 0.2651 0.4409 0.2426 0.0937  -0.0622 0.0395  771 HOH A O   
3454 O  O   . HOH C .   ? 0.2075 0.1932 0.3028 0.0328  -0.0435 -0.0124 772 HOH A O   
3455 O  O   . HOH C .   ? 0.2548 0.1694 0.2338 -0.0350 0.0008  0.0225  773 HOH A O   
3456 O  O   . HOH C .   ? 0.1766 0.1093 0.1874 0.0016  -0.0054 0.0190  774 HOH A O   
3457 O  O   . HOH C .   ? 0.2584 0.2243 0.3813 0.0104  0.0084  -0.0208 775 HOH A O   
3458 O  O   . HOH C .   ? 0.2280 0.2118 0.2832 -0.0632 0.0549  0.0286  776 HOH A O   
3459 O  O   . HOH C .   ? 0.3016 0.2604 0.1855 0.0378  -0.0076 0.0448  777 HOH A O   
3460 O  O   . HOH C .   ? 0.5907 0.3591 0.3181 0.0167  0.0425  -0.0767 778 HOH A O   
3461 O  O   . HOH C .   ? 0.2464 0.3449 0.3002 -0.0111 -0.0087 -0.1265 779 HOH A O   
3462 O  O   . HOH C .   ? 0.1583 0.1412 0.1596 0.0206  0.0093  0.0324  780 HOH A O   
3463 O  O   . HOH C .   ? 0.4342 0.5295 0.3600 -0.1158 -0.0225 -0.0844 781 HOH A O   
3464 O  O   . HOH C .   ? 0.3726 0.2892 0.2583 0.0714  -0.0461 -0.0129 782 HOH A O   
3465 O  O   . HOH C .   ? 0.3131 0.2873 0.3174 0.0183  -0.0037 -0.0466 783 HOH A O   
3466 O  O   . HOH C .   ? 0.2268 0.2553 0.2363 -0.0025 0.0086  -0.0363 784 HOH A O   
3467 O  O   . HOH C .   ? 0.5823 0.3125 0.2997 0.0733  0.0521  -0.0264 785 HOH A O   
3468 O  O   . HOH C .   ? 0.2493 0.2576 0.2561 0.0739  -0.0521 -0.0477 786 HOH A O   
3469 O  O   . HOH C .   ? 0.1227 0.1304 0.1728 0.0213  -0.0095 0.0140  787 HOH A O   
3470 O  O   . HOH C .   ? 0.3739 0.3689 0.3037 -0.0608 -0.0007 -0.0064 788 HOH A O   
3471 O  O   . HOH C .   ? 0.3512 0.2367 0.2621 -0.0890 0.0073  0.0633  789 HOH A O   
3472 O  O   . HOH C .   ? 0.2489 0.2500 0.3556 -0.0367 -0.0192 0.0429  790 HOH A O   
3473 O  O   . HOH C .   ? 0.4619 0.3673 0.2816 -0.0517 0.0479  0.0668  791 HOH A O   
3474 O  O   . HOH C .   ? 0.2031 0.2018 0.1527 0.0570  -0.0130 0.0105  792 HOH A O   
3475 O  O   . HOH C .   ? 0.4101 0.4138 0.2950 -0.0057 -0.0359 0.0114  793 HOH A O   
3476 O  O   . HOH C .   ? 0.2209 0.2447 0.2349 0.0181  -0.0277 -0.0112 794 HOH A O   
3477 O  O   . HOH C .   ? 0.3444 0.3086 0.3192 -0.0036 -0.0124 -0.0544 795 HOH A O   
3478 O  O   . HOH C .   ? 0.2870 0.2036 0.2724 0.0016  -0.0152 -0.0006 796 HOH A O   
3479 O  O   . HOH C .   ? 0.2146 0.2105 0.2927 -0.0020 0.0477  0.0187  797 HOH A O   
3480 O  O   . HOH C .   ? 0.4803 0.4313 0.3061 0.0151  0.0235  0.1166  798 HOH A O   
3481 O  O   . HOH C .   ? 0.3111 0.3674 0.3029 0.0520  -0.0237 -0.0355 799 HOH A O   
3482 O  O   . HOH C .   ? 0.1914 0.2395 0.2021 -0.0344 0.0014  0.0381  800 HOH A O   
3483 O  O   . HOH C .   ? 0.4379 0.2885 0.3936 0.0183  -0.0490 -0.0453 801 HOH A O   
3484 O  O   . HOH C .   ? 0.3399 0.3808 0.4244 0.0965  0.0013  -0.0381 802 HOH A O   
3485 O  O   . HOH C .   ? 0.6518 0.3892 0.2071 0.0416  -0.0287 0.0815  803 HOH A O   
3486 O  O   . HOH C .   ? 0.4210 0.3465 0.4996 -0.1441 0.0208  0.0334  804 HOH A O   
3487 O  O   . HOH C .   ? 0.3719 0.4291 0.3356 -0.0646 0.1299  0.0677  805 HOH A O   
3488 O  O   . HOH C .   ? 0.5047 0.2581 0.4321 0.1198  -0.0547 0.0000  806 HOH A O   
3489 O  O   . HOH C .   ? 0.3080 0.3998 0.3058 -0.0699 0.0276  0.1231  807 HOH A O   
3490 O  O   . HOH C .   ? 0.3998 0.1771 0.3208 0.0639  0.0266  -0.0101 808 HOH A O   
3491 O  O   . HOH C .   ? 0.4046 0.3235 0.5377 0.0121  -0.1310 -0.0218 809 HOH A O   
3492 O  O   . HOH C .   ? 0.3794 0.5204 0.6167 0.0832  -0.0336 0.1088  810 HOH A O   
3493 O  O   . HOH C .   ? 0.3160 0.3008 0.2871 0.0714  -0.0718 -0.0144 811 HOH A O   
3494 O  O   . HOH C .   ? 0.5404 0.2982 0.4236 -0.0109 -0.0334 0.0019  812 HOH A O   
3495 O  O   . HOH C .   ? 0.3053 0.3389 0.1796 -0.0628 -0.0709 0.0099  813 HOH A O   
3496 O  O   . HOH C .   ? 0.2306 0.2869 0.3180 0.0185  0.0826  0.0420  814 HOH A O   
3497 O  O   . HOH C .   ? 0.3888 0.2814 0.3030 0.0377  0.0706  0.0266  815 HOH A O   
3498 O  O   . HOH C .   ? 0.3357 0.3087 0.2594 0.0401  0.0057  -0.0322 816 HOH A O   
3499 O  O   . HOH C .   ? 0.2793 0.4254 0.4425 -0.0580 -0.0216 0.0740  817 HOH A O   
3500 O  O   . HOH C .   ? 0.5650 0.4454 0.3299 -0.2367 0.0254  0.0299  818 HOH A O   
3501 O  O   . HOH C .   ? 0.4183 0.5537 0.2952 0.0689  -0.0234 0.0290  819 HOH A O   
3502 O  O   . HOH C .   ? 0.2999 0.3479 0.3514 0.0315  -0.0593 -0.0243 820 HOH A O   
3503 O  O   . HOH C .   ? 0.2867 0.4298 0.4429 -0.0232 0.0385  -0.0406 821 HOH A O   
3504 O  O   . HOH C .   ? 0.3347 0.4468 0.3330 -0.0408 -0.0144 0.0196  822 HOH A O   
3505 O  O   . HOH C .   ? 0.3789 0.3757 0.2809 -0.0095 0.0261  0.0202  823 HOH A O   
3506 O  O   . HOH C .   ? 0.4830 0.4026 0.3756 0.0326  -0.0637 0.0351  824 HOH A O   
3507 O  O   . HOH C .   ? 0.4421 0.2395 0.4686 0.0392  -0.0384 -0.0064 825 HOH A O   
3508 O  O   . HOH C .   ? 0.5715 0.5794 0.4605 0.0813  0.2460  0.1513  826 HOH A O   
3509 O  O   . HOH C .   ? 0.4082 0.4092 0.3638 -0.1043 0.0160  -0.0660 827 HOH A O   
3510 O  O   . HOH C .   ? 0.3540 0.3670 0.3496 0.0459  -0.0618 0.0046  828 HOH A O   
3511 O  O   . HOH C .   ? 0.4822 0.3393 0.3650 -0.0905 0.1404  -0.0880 829 HOH A O   
3512 O  O   . HOH C .   ? 0.3911 0.4708 0.2932 0.0295  -0.0463 0.0267  830 HOH A O   
3513 O  O   . HOH C .   ? 0.5013 0.2612 0.3940 -0.0367 -0.0155 -0.0632 831 HOH A O   
3514 O  O   . HOH C .   ? 0.3071 0.3092 0.4254 -0.0164 0.0086  0.1050  832 HOH A O   
3515 O  O   . HOH C .   ? 0.4741 0.3370 0.3663 -0.1447 0.0205  0.0452  833 HOH A O   
3516 O  O   . HOH C .   ? 0.3572 0.2854 0.4972 0.0573  -0.0349 -0.0039 834 HOH A O   
3517 O  O   . HOH C .   ? 0.2168 0.2439 0.3172 -0.0425 -0.0181 0.0665  835 HOH A O   
3518 O  O   . HOH C .   ? 0.2772 0.4957 0.2403 -0.0510 0.0903  -0.0745 836 HOH A O   
3519 O  O   . HOH C .   ? 0.2749 0.2156 0.3210 -0.0609 0.0645  0.0438  837 HOH A O   
3520 O  O   . HOH C .   ? 0.2638 0.2419 0.2898 -0.0019 0.0881  -0.0942 838 HOH A O   
3521 O  O   . HOH C .   ? 0.1517 0.2311 0.2461 -0.0175 0.0334  -0.0642 839 HOH A O   
3522 O  O   . HOH C .   ? 0.6754 0.3195 0.4618 0.0098  0.1281  -0.0557 840 HOH A O   
3523 O  O   . HOH C .   ? 0.3382 0.3616 0.3385 0.0266  -0.0368 -0.0706 841 HOH A O   
3524 O  O   . HOH C .   ? 0.3819 0.2347 0.2903 0.0246  0.0687  0.0077  842 HOH A O   
3525 O  O   . HOH C .   ? 0.4434 0.3595 0.5558 -0.1042 -0.2061 0.0086  843 HOH A O   
3526 O  O   . HOH C .   ? 0.2484 0.3766 0.4424 0.0050  -0.1217 0.0463  844 HOH A O   
3527 O  O   . HOH C .   ? 0.3181 0.2714 0.5569 -0.0776 0.1856  -0.0517 845 HOH A O   
3528 O  O   . HOH C .   ? 0.5581 0.3383 0.2333 0.0653  -0.0772 -0.0477 846 HOH A O   
3529 O  O   . HOH C .   ? 0.3703 0.3204 0.4407 -0.0626 0.0223  0.0037  847 HOH A O   
3530 O  O   . HOH C .   ? 0.4507 0.4572 0.2622 -0.0269 -0.0533 -0.0706 848 HOH A O   
3531 O  O   . HOH C .   ? 0.3614 0.2708 0.3717 0.0733  0.1045  0.1390  849 HOH A O   
3532 O  O   . HOH C .   ? 0.4510 0.3632 0.2850 0.0503  0.0045  -0.0051 850 HOH A O   
3533 O  O   . HOH C .   ? 0.2067 0.2449 0.3134 -0.0574 -0.0199 0.0200  851 HOH A O   
3534 O  O   . HOH C .   ? 0.1663 0.4411 0.4297 -0.0451 0.0302  -0.0889 852 HOH A O   
3535 O  O   . HOH C .   ? 0.2715 0.3451 0.3945 -0.0255 0.0044  0.0789  853 HOH A O   
3536 O  O   . HOH C .   ? 0.4172 0.2929 0.2517 0.0383  -0.0327 -0.0427 854 HOH A O   
3537 O  O   . HOH C .   ? 0.5133 0.2816 0.4489 0.0476  0.0058  0.0287  855 HOH A O   
3538 O  O   . HOH C .   ? 0.4502 0.3626 0.3907 0.0350  0.0073  0.0212  856 HOH A O   
3539 O  O   . HOH C .   ? 0.3426 0.4745 0.3337 0.1793  -0.0063 0.0114  857 HOH A O   
3540 O  O   . HOH C .   ? 0.3488 0.3283 0.4217 0.0254  -0.0844 -0.0219 858 HOH A O   
3541 O  O   . HOH C .   ? 0.4397 0.2798 0.2744 -0.0567 0.0289  -0.0733 859 HOH A O   
3542 O  O   . HOH C .   ? 0.3456 0.5505 0.4436 0.0824  -0.1044 0.0276  860 HOH A O   
3543 O  O   . HOH C .   ? 0.3215 0.4026 0.3741 0.0744  -0.0364 0.0338  861 HOH A O   
3544 O  O   . HOH C .   ? 0.4072 0.2402 0.3337 -0.0758 -0.0020 0.0539  862 HOH A O   
3545 O  O   . HOH C .   ? 0.3033 0.3286 0.2936 -0.0129 -0.0860 -0.0003 863 HOH A O   
3546 O  O   . HOH C .   ? 0.2769 0.3885 0.3031 0.1238  0.0405  -0.0239 864 HOH A O   
3547 O  O   . HOH C .   ? 0.4113 0.3318 0.4059 0.0344  -0.0139 0.0892  865 HOH A O   
3548 O  O   . HOH C .   ? 0.2610 0.2935 0.2786 -0.0053 -0.0424 0.0665  866 HOH A O   
3549 O  O   . HOH C .   ? 0.3277 0.3218 0.3083 0.0175  0.0206  -0.0004 867 HOH A O   
3550 O  O   . HOH C .   ? 0.3883 0.4420 0.3228 0.0441  0.0253  0.0478  868 HOH A O   
3551 O  O   . HOH C .   ? 0.4671 0.5187 0.2802 -0.0535 0.1216  -0.0734 869 HOH A O   
3552 O  O   . HOH C .   ? 0.2469 0.1785 0.3163 0.0415  -0.0417 0.0025  870 HOH A O   
3553 O  O   . HOH C .   ? 0.3859 0.3148 0.3926 -0.0943 0.0130  -0.0050 871 HOH A O   
3554 O  O   . HOH C .   ? 0.2634 0.2134 0.2552 -0.0303 0.0101  -0.0543 872 HOH A O   
3555 O  O   . HOH C .   ? 0.5893 0.6021 0.1569 -0.0782 0.0483  -0.0366 873 HOH A O   
3556 O  O   . HOH C .   ? 0.4299 0.1947 0.3651 0.0751  0.0918  0.0004  874 HOH A O   
3557 O  O   . HOH C .   ? 0.3465 0.3861 0.3709 -0.0259 -0.1283 -0.0090 875 HOH A O   
3558 O  O   . HOH C .   ? 0.4626 0.2709 0.3712 0.1080  -0.0595 -0.0096 876 HOH A O   
3559 O  O   . HOH C .   ? 0.4750 0.4585 0.3002 0.1647  0.0359  -0.0511 877 HOH A O   
3560 O  O   . HOH C .   ? 0.5539 0.4625 0.3269 0.1312  0.0460  -0.1044 878 HOH A O   
3561 O  O   . HOH C .   ? 0.3704 0.5245 0.2966 0.0937  -0.0141 -0.0966 879 HOH A O   
3562 O  O   . HOH C .   ? 0.2125 0.4089 0.2494 0.0172  -0.0673 -0.0553 880 HOH A O   
3563 O  O   . HOH C .   ? 0.3886 0.3019 0.3606 0.1106  0.0676  -0.0215 881 HOH A O   
3564 O  O   . HOH C .   ? 0.2877 0.6031 0.3071 -0.0366 0.0694  -0.0632 882 HOH A O   
3565 O  O   . HOH C .   ? 0.3108 0.6329 0.6059 -0.2181 -0.0399 0.1361  883 HOH A O   
3566 O  O   . HOH C .   ? 0.4113 0.5021 0.2347 0.0923  -0.0765 -0.0088 884 HOH A O   
3567 O  O   . HOH C .   ? 0.4926 0.4999 0.6188 -0.0462 0.2470  0.0413  885 HOH A O   
3568 O  O   . HOH C .   ? 0.1715 0.3576 0.4825 -0.0130 0.0360  0.0114  886 HOH A O   
3569 O  O   . HOH C .   ? 0.3623 0.4873 0.3776 0.0243  -0.0278 0.0487  887 HOH A O   
3570 O  O   . HOH C .   ? 0.4475 0.2541 0.2941 0.0640  0.0264  -0.0062 888 HOH A O   
3571 O  O   . HOH C .   ? 0.5170 0.3422 0.3721 -0.0850 0.0888  0.0289  889 HOH A O   
3572 O  O   . HOH C .   ? 0.4882 0.3011 0.6217 0.0344  -0.0671 -0.0987 890 HOH A O   
3573 O  O   . HOH C .   ? 0.6019 0.3907 0.4894 -0.0843 0.2251  -0.0484 891 HOH A O   
3574 O  O   . HOH C .   ? 0.5707 0.3107 0.4463 0.0245  0.0388  -0.0146 892 HOH A O   
3575 O  O   . HOH C .   ? 0.5529 0.4868 0.3392 0.1352  0.0161  -0.1289 893 HOH A O   
3576 O  O   . HOH C .   ? 1.0139 0.7279 0.7746 -0.0542 -0.0265 0.1626  894 HOH A O   
3577 O  O   . HOH C .   ? 0.4460 0.5126 0.3045 0.0184  0.0725  -0.0122 895 HOH A O   
3578 O  O   . HOH C .   ? 0.7676 0.7631 0.3974 0.1533  0.3238  0.0888  896 HOH A O   
3579 O  O   . HOH C .   ? 0.7184 0.5618 0.5131 0.1489  -0.0284 -0.0796 897 HOH A O   
3580 O  O   . HOH C .   ? 0.4084 0.5048 0.4770 -0.0052 -0.0334 -0.0828 898 HOH A O   
3581 O  O   . HOH C .   ? 0.3738 0.2347 0.2885 0.0363  -0.0488 0.0844  899 HOH A O   
3582 O  O   . HOH C .   ? 0.3660 0.2289 0.2189 0.0577  -0.0047 0.0060  900 HOH A O   
3583 O  O   . HOH C .   ? 0.3829 0.5286 0.4449 0.1454  -0.0592 0.0164  901 HOH A O   
3584 O  O   . HOH C .   ? 0.4594 0.3378 0.4851 0.0649  0.0185  -0.0025 902 HOH A O   
3585 O  O   . HOH C .   ? 0.5060 0.5450 0.3034 0.0551  -0.0182 -0.0676 903 HOH A O   
3586 O  O   . HOH C .   ? 0.2336 0.3365 0.1983 -0.0206 0.0177  -0.0297 904 HOH A O   
3587 O  O   . HOH C .   ? 0.3780 0.3787 0.3152 -0.1175 -0.0251 0.0103  905 HOH A O   
3588 O  O   . HOH C .   ? 0.6405 0.7014 0.3578 0.0777  -0.0954 -0.1481 906 HOH A O   
3589 O  O   . HOH C .   ? 0.5498 0.5274 0.4726 0.1020  0.1327  -0.0817 907 HOH A O   
3590 O  O   . HOH C .   ? 0.4969 0.8232 0.9598 0.5310  0.4024  0.3027  908 HOH A O   
3591 O  O   . HOH C .   ? 0.5302 0.4122 0.3667 -0.0371 -0.0267 -0.0358 909 HOH A O   
3592 O  O   . HOH C .   ? 0.4369 0.4115 0.4763 0.0385  -0.0032 0.0469  910 HOH A O   
3593 O  O   . HOH C .   ? 0.3064 0.5109 0.4967 0.1343  0.2246  -0.0222 911 HOH A O   
3594 O  O   . HOH C .   ? 0.4123 0.4687 0.6272 0.0215  -0.0358 -0.1332 912 HOH A O   
3595 O  O   . HOH C .   ? 0.3640 0.7575 0.4425 0.0953  -0.0280 0.0921  913 HOH A O   
3596 O  O   . HOH C .   ? 0.3965 0.3231 0.5774 -0.0220 0.0081  0.0811  914 HOH A O   
3597 O  O   . HOH C .   ? 0.2998 0.4961 0.4007 0.0045  -0.0870 0.0400  915 HOH A O   
3598 O  O   . HOH C .   ? 0.4304 0.3402 0.4140 0.1190  -0.0146 -0.0282 916 HOH A O   
3599 O  O   . HOH C .   ? 0.4062 0.3069 0.3509 0.0570  -0.0363 0.0240  917 HOH A O   
3600 O  O   . HOH C .   ? 0.3931 0.4880 0.7676 0.0207  0.0336  0.0519  918 HOH A O   
3601 O  O   . HOH C .   ? 0.4283 0.2925 0.5003 0.0843  0.0227  0.0375  919 HOH A O   
3602 O  O   . HOH C .   ? 0.3538 0.2530 0.2304 0.0564  0.0001  0.0184  920 HOH A O   
3603 O  O   . HOH C .   ? 0.4796 0.4808 0.4294 0.0683  -0.0739 -0.0680 921 HOH A O   
3604 O  O   . HOH C .   ? 0.3169 0.3179 0.4573 -0.0804 0.1275  -0.0416 922 HOH A O   
3605 O  O   . HOH C .   ? 0.5976 0.5089 0.3612 0.0972  0.0146  -0.1380 923 HOH A O   
3606 O  O   . HOH C .   ? 0.2565 0.1536 0.3245 -0.0369 0.0175  0.0468  924 HOH A O   
3607 O  O   . HOH C .   ? 0.5335 0.3920 0.4626 0.1140  0.0324  0.0371  925 HOH A O   
3608 O  O   . HOH C .   ? 0.5635 0.6319 0.5810 -0.0458 0.0190  0.0512  926 HOH A O   
3609 O  O   . HOH C .   ? 0.4021 0.5817 0.5620 0.0151  0.0424  -0.0404 927 HOH A O   
3610 O  O   . HOH C .   ? 0.3864 0.2087 0.3456 -0.0296 0.0337  0.0489  928 HOH A O   
3611 O  O   . HOH C .   ? 0.4273 0.5585 0.5264 -0.0004 0.1307  0.0318  929 HOH A O   
3612 O  O   . HOH C .   ? 0.3874 0.6608 0.3792 -0.0727 -0.0521 -0.1448 930 HOH A O   
3613 O  O   . HOH C .   ? 0.5223 0.4770 0.5103 -0.0325 0.0291  0.1438  931 HOH A O   
3614 O  O   . HOH C .   ? 0.4881 0.3333 0.4471 -0.0286 -0.0274 0.0029  932 HOH A O   
3615 O  O   . HOH C .   ? 0.3535 0.4140 0.4772 0.1170  -0.0669 -0.0443 933 HOH A O   
3616 O  O   . HOH C .   ? 0.4653 0.3204 0.3325 0.0810  -0.0210 0.0170  934 HOH A O   
3617 O  O   . HOH C .   ? 0.4035 0.3143 0.5794 0.0710  -0.0319 0.0158  935 HOH A O   
3618 O  O   . HOH C .   ? 0.5457 0.6955 0.5494 0.2448  -0.0642 0.0483  936 HOH A O   
3619 O  O   . HOH C .   ? 0.3887 0.3167 0.3378 0.0239  0.0321  0.0324  937 HOH A O   
# 
